data_3T5W
# 
_entry.id   3T5W 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.281 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   3T5W         
RCSB  RCSB067076   
WWPDB D_1000067076 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        3T5W 
_pdbx_database_status.recvd_initial_deposition_date   2011-07-28 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Ihara, K.'     1 
'Yamaguchi, Y.' 2 
'Torigoe, H.'   3 
'Wakatsuki, S.' 4 
'Taniguchi, N.' 5 
'Suzuki, K.'    6 
'Fujiwara, N.'  7 
# 
_citation.id                        primary 
_citation.title                     
;Structural switching of Cu,Zn-superoxide dismutases at loop VI: insights from the crystal structure of 2-mercaptoethanol-modified enzyme
;
_citation.journal_abbrev            Biosci.Rep. 
_citation.journal_volume            32 
_citation.page_first                539 
_citation.page_last                 548 
_citation.year                      2012 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           0144-8463 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   22804629 
_citation.pdbx_database_id_DOI      10.1042/BSR20120029 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Ihara, K.'     1 
primary 'Fujiwara, N.'  2 
primary 'Yamaguchi, Y.' 3 
primary 'Torigoe, H.'   4 
primary 'Wakatsuki, S.' 5 
primary 'Taniguchi, N.' 6 
primary 'Suzuki, K.'    7 
# 
_cell.entry_id           3T5W 
_cell.length_a           74.086 
_cell.length_b           163.277 
_cell.length_c           173.628 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              48 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         3T5W 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Superoxide dismutase [Cu-Zn]' 15903.680 12   1.15.1.1 ? ? ? 
2 non-polymer syn 'COPPER (I) ION'               63.546    12   ?        ? ? ? 
3 non-polymer syn 'ZINC ION'                     65.409    12   ?        ? ? ? 
4 non-polymer syn 'SULFATE ION'                  96.063    12   ?        ? ? ? 
5 water       nat water                          18.015    1746 ?        ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'copper zinc superoxide dismutase, Superoxide dismutase 1, hSod1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDH(CME)IIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B,D,E,F,G,H,I,J,K,L,M 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   THR n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   CYS n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  GLY n 
1 11  ASP n 
1 12  GLY n 
1 13  PRO n 
1 14  VAL n 
1 15  GLN n 
1 16  GLY n 
1 17  ILE n 
1 18  ILE n 
1 19  ASN n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  ASN n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  LYS n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  SER n 
1 35  ILE n 
1 36  LYS n 
1 37  GLY n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU n 
1 43  HIS n 
1 44  GLY n 
1 45  PHE n 
1 46  HIS n 
1 47  VAL n 
1 48  HIS n 
1 49  GLU n 
1 50  PHE n 
1 51  GLY n 
1 52  ASP n 
1 53  ASN n 
1 54  THR n 
1 55  ALA n 
1 56  GLY n 
1 57  CYS n 
1 58  THR n 
1 59  SER n 
1 60  ALA n 
1 61  GLY n 
1 62  PRO n 
1 63  HIS n 
1 64  PHE n 
1 65  ASN n 
1 66  PRO n 
1 67  LEU n 
1 68  SER n 
1 69  ARG n 
1 70  LYS n 
1 71  HIS n 
1 72  GLY n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS n 
1 76  ASP n 
1 77  GLU n 
1 78  GLU n 
1 79  ARG n 
1 80  HIS n 
1 81  VAL n 
1 82  GLY n 
1 83  ASP n 
1 84  LEU n 
1 85  GLY n 
1 86  ASN n 
1 87  VAL n 
1 88  THR n 
1 89  ALA n 
1 90  ASP n 
1 91  LYS n 
1 92  ASP n 
1 93  GLY n 
1 94  VAL n 
1 95  ALA n 
1 96  ASP n 
1 97  VAL n 
1 98  SER n 
1 99  ILE n 
1 100 GLU n 
1 101 ASP n 
1 102 SER n 
1 103 VAL n 
1 104 ILE n 
1 105 SER n 
1 106 LEU n 
1 107 SER n 
1 108 GLY n 
1 109 ASP n 
1 110 HIS n 
1 111 CME n 
1 112 ILE n 
1 113 ILE n 
1 114 GLY n 
1 115 ARG n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 HIS n 
1 121 GLU n 
1 122 LYS n 
1 123 ALA n 
1 124 ASP n 
1 125 ASP n 
1 126 LEU n 
1 127 GLY n 
1 128 LYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 GLU n 
1 133 GLU n 
1 134 SER n 
1 135 THR n 
1 136 LYS n 
1 137 THR n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 ARG n 
1 144 LEU n 
1 145 ALA n 
1 146 CYS n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 ILE n 
1 152 ALA n 
1 153 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 SOD1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_struct_ref.pdbx_align_begin           2 
_struct_ref.pdbx_db_isoform            ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1  1 3T5W A 1 ? 153 ? P00441 2 ? 154 ? 1 153 
2  1 3T5W B 1 ? 153 ? P00441 2 ? 154 ? 1 153 
3  1 3T5W D 1 ? 153 ? P00441 2 ? 154 ? 1 153 
4  1 3T5W E 1 ? 153 ? P00441 2 ? 154 ? 1 153 
5  1 3T5W F 1 ? 153 ? P00441 2 ? 154 ? 1 153 
6  1 3T5W G 1 ? 153 ? P00441 2 ? 154 ? 1 153 
7  1 3T5W H 1 ? 153 ? P00441 2 ? 154 ? 1 153 
8  1 3T5W I 1 ? 153 ? P00441 2 ? 154 ? 1 153 
9  1 3T5W J 1 ? 153 ? P00441 2 ? 154 ? 1 153 
10 1 3T5W K 1 ? 153 ? P00441 2 ? 154 ? 1 153 
11 1 3T5W L 1 ? 153 ? P00441 2 ? 154 ? 1 153 
12 1 3T5W M 1 ? 153 ? P00441 2 ? 154 ? 1 153 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE                            ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                           ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE                         ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'                    ? 'C4 H7 N O4'     133.103 
CME 'L-peptide linking' n 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' ? 'C5 H11 N O3 S2' 197.276 
CU1 non-polymer         . 'COPPER (I) ION'                   ? 'Cu 1'           63.546  
CYS 'L-peptide linking' y CYSTEINE                           ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                          ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                    ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                            ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                          ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                              ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                         ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                            ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                             ? 'C6 H15 N2 O2 1' 147.195 
PHE 'L-peptide linking' y PHENYLALANINE                      ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                            ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                             ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'                      ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE                          ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                         ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE                             ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'                         ? 'Zn 2'           65.409  
# 
_exptl.entry_id          3T5W 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.75 
_exptl_crystal.density_percent_sol   55.29 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            289 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              6 
_exptl_crystal_grow.pdbx_details    '15% PEG 3350, 300mM (NH4)2SO4, pH6.0, VAPOR DIFFUSION, HANGING DROP, temperature 289K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'ADSC QUANTUM 315' 
_diffrn_detector.pdbx_collection_date   2008-06-24 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    
;Numerical link type Si(111) double crystal monochromator, direct water cooling using micro-channel (1st crystal), indirect water cooling (2nd crystal)
;
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0000 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'PHOTON FACTORY BEAMLINE BL-5A' 
_diffrn_source.pdbx_synchrotron_site       'Photon Factory' 
_diffrn_source.pdbx_synchrotron_beamline   BL-5A 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.0000 
# 
_reflns.entry_id                     3T5W 
_reflns.observed_criterion_sigma_I   -3.0 
_reflns.observed_criterion_sigma_F   -3.0 
_reflns.d_resolution_low             118.7 
_reflns.d_resolution_high            1.8 
_reflns.number_obs                   185279 
_reflns.number_all                   195308 
_reflns.percent_possible_obs         94.9 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.115 
_reflns.pdbx_netI_over_sigmaI        12.0 
_reflns.B_iso_Wilson_estimate        19.7 
_reflns.pdbx_redundancy              5.0 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high                  1.80 
_reflns_shell.d_res_low                   1.86 
_reflns_shell.percent_possible_all        88.2 
_reflns_shell.Rmerge_I_obs                ? 
_reflns_shell.pdbx_Rsym_value             0.882 
_reflns_shell.meanI_over_sigI_obs         1.6 
_reflns_shell.pdbx_redundancy             4.8 
_reflns_shell.percent_possible_obs        ? 
_reflns_shell.number_unique_all           17868 
_reflns_shell.number_measured_all         ? 
_reflns_shell.number_measured_obs         ? 
_reflns_shell.number_unique_obs           ? 
_reflns_shell.pdbx_chi_squared            ? 
_reflns_shell.pdbx_rejects                ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs   ? 
_reflns_shell.number_possible             ? 
_reflns_shell.Rmerge_F_all                ? 
_reflns_shell.Rmerge_F_obs                ? 
_reflns_shell.Rmerge_I_all                ? 
_reflns_shell.meanI_over_sigI_all         ? 
_reflns_shell.pdbx_Rrim_I_all             ? 
_reflns_shell.pdbx_Rpim_I_all             ? 
_reflns_shell.pdbx_ordinal                1 
_reflns_shell.pdbx_diffrn_id              1 
# 
_refine.entry_id                                 3T5W 
_refine.ls_number_reflns_obs                     175704 
_refine.ls_number_reflns_all                     184956 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             34.04 
_refine.ls_d_res_high                            1.80 
_refine.ls_percent_reflns_obs                    94.87 
_refine.ls_R_factor_obs                          0.20181 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.19976 
_refine.ls_R_factor_R_free                       0.24100 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  9252 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.946 
_refine.correlation_coeff_Fo_to_Fc_free          0.920 
_refine.B_iso_mean                               18.780 
_refine.aniso_B[1][1]                            -0.55 
_refine.aniso_B[2][2]                            1.22 
_refine.aniso_B[3][3]                            -0.67 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      'PDB ENTRY 1p1v' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             Isotropic 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R_Free                  0.132 
_refine.overall_SU_ML                            0.092 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             6.564 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_free                        ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        13368 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         84 
_refine_hist.number_atoms_solvent             1746 
_refine_hist.number_atoms_total               15198 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        34.04 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_restraint_function 
_refine_ls_restr.pdbx_refine_id 
r_bond_refined_d             0.011  0.021  ? 13644 ? 'X-RAY DIFFRACTION' 
r_bond_other_d               ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_angle_refined_deg          1.269  1.954  ? 18408 ? 'X-RAY DIFFRACTION' 
r_angle_other_deg            ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_1_deg       6.209  5.000  ? 1824  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_2_deg       37.727 25.625 ? 576   ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_3_deg       13.360 15.000 ? 2208  ? 'X-RAY DIFFRACTION' 
r_dihedral_angle_4_deg       16.697 15.000 ? 48    ? 'X-RAY DIFFRACTION' 
r_chiral_restr               0.087  0.200  ? 2016  ? 'X-RAY DIFFRACTION' 
r_gen_planes_refined         0.005  0.021  ? 10344 ? 'X-RAY DIFFRACTION' 
r_gen_planes_other           ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_nbd_refined                ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_nbd_other                  ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_nbtor_refined              ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_nbtor_other                ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_xyhbond_nbd_refined        ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_xyhbond_nbd_other          ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_metal_ion_refined          ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_metal_ion_other            ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_refined       ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_symmetry_vdw_other         ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_symmetry_hbond_refined     ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_symmetry_hbond_other       ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_symmetry_metal_ion_refined ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_symmetry_metal_ion_other   ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_mcbond_it                  0.673  1.500  ? 8940  ? 'X-RAY DIFFRACTION' 
r_mcbond_other               ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_mcangle_it                 1.230  2.000  ? 14208 ? 'X-RAY DIFFRACTION' 
r_scbond_it                  1.992  3.000  ? 4704  ? 'X-RAY DIFFRACTION' 
r_scangle_it                 3.365  4.500  ? 4200  ? 'X-RAY DIFFRACTION' 
r_rigid_bond_restr           ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_sphericity_free            ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
r_sphericity_bonded          ?      ?      ? ?     ? 'X-RAY DIFFRACTION' 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.800 
_refine_ls_shell.d_res_low                        1.847 
_refine_ls_shell.number_reflns_R_work             12534 
_refine_ls_shell.R_factor_R_work                  0.276 
_refine_ls_shell.percent_reflns_obs               92.50 
_refine_ls_shell.R_factor_R_free                  0.323 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             683 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
# 
_struct.entry_id                  3T5W 
_struct.title                     '2ME modified human SOD1' 
_struct.pdbx_descriptor           'Superoxide dismutase [Cu-Zn] (E.C.1.15.1.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        3T5W 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            '2ME modification at Cys111, OXIDOREDUCTASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A  N N 1 ? 
B  N N 1 ? 
C  N N 1 ? 
D  N N 1 ? 
E  N N 1 ? 
F  N N 1 ? 
G  N N 1 ? 
H  N N 1 ? 
I  N N 1 ? 
J  N N 1 ? 
K  N N 1 ? 
L  N N 1 ? 
M  N N 2 ? 
N  N N 3 ? 
O  N N 4 ? 
P  N N 2 ? 
Q  N N 3 ? 
R  N N 4 ? 
S  N N 2 ? 
T  N N 3 ? 
U  N N 4 ? 
V  N N 2 ? 
W  N N 3 ? 
X  N N 4 ? 
Y  N N 2 ? 
Z  N N 3 ? 
AA N N 4 ? 
BA N N 2 ? 
CA N N 3 ? 
DA N N 4 ? 
EA N N 2 ? 
FA N N 3 ? 
GA N N 4 ? 
HA N N 2 ? 
IA N N 3 ? 
JA N N 4 ? 
KA N N 2 ? 
LA N N 3 ? 
MA N N 4 ? 
NA N N 2 ? 
OA N N 3 ? 
PA N N 4 ? 
QA N N 2 ? 
RA N N 3 ? 
SA N N 4 ? 
TA N N 2 ? 
UA N N 3 ? 
VA N N 4 ? 
WA N N 5 ? 
XA N N 5 ? 
YA N N 5 ? 
ZA N N 5 ? 
AB N N 5 ? 
BB N N 5 ? 
CB N N 5 ? 
DB N N 5 ? 
EB N N 5 ? 
FB N N 5 ? 
GB N N 5 ? 
HB N N 5 ? 
# 
_struct_biol.id        1 
_struct_biol.details   ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  1  ALA A 55  ? GLY A 61  ? ALA A 55  GLY A 61  5 ? 7 
HELX_P HELX_P2  2  SER A 107 ? CME A 111 ? SER A 107 CME A 111 5 ? 5 
HELX_P HELX_P3  3  GLU A 132 ? LYS A 136 ? GLU A 132 LYS A 136 5 ? 5 
HELX_P HELX_P4  4  ALA B 55  ? GLY B 61  ? ALA B 55  GLY B 61  5 ? 7 
HELX_P HELX_P5  5  GLU B 133 ? GLY B 138 ? GLU B 133 GLY B 138 1 ? 6 
HELX_P HELX_P6  6  ALA C 55  ? GLY C 61  ? ALA D 55  GLY D 61  5 ? 7 
HELX_P HELX_P7  7  SER C 107 ? CME C 111 ? SER D 107 CME D 111 5 ? 5 
HELX_P HELX_P8  8  GLU C 133 ? GLY C 138 ? GLU D 133 GLY D 138 1 ? 6 
HELX_P HELX_P9  9  ALA D 55  ? GLY D 61  ? ALA E 55  GLY E 61  5 ? 7 
HELX_P HELX_P10 10 GLU D 133 ? GLY D 138 ? GLU E 133 GLY E 138 1 ? 6 
HELX_P HELX_P11 11 ALA E 55  ? GLY E 61  ? ALA F 55  GLY F 61  5 ? 7 
HELX_P HELX_P12 12 SER E 107 ? CME E 111 ? SER F 107 CME F 111 5 ? 5 
HELX_P HELX_P13 13 GLU E 133 ? GLY E 138 ? GLU F 133 GLY F 138 1 ? 6 
HELX_P HELX_P14 14 ALA F 55  ? GLY F 61  ? ALA G 55  GLY G 61  5 ? 7 
HELX_P HELX_P15 15 GLU F 133 ? GLY F 138 ? GLU G 133 GLY G 138 1 ? 6 
HELX_P HELX_P16 16 CYS G 57  ? GLY G 61  ? CYS H 57  GLY H 61  5 ? 5 
HELX_P HELX_P17 17 SER G 107 ? CME G 111 ? SER H 107 CME H 111 5 ? 5 
HELX_P HELX_P18 18 ALA H 55  ? GLY H 61  ? ALA I 55  GLY I 61  5 ? 7 
HELX_P HELX_P19 19 ASN H 131 ? LYS H 136 ? ASN I 131 LYS I 136 5 ? 6 
HELX_P HELX_P20 20 ALA I 55  ? GLY I 61  ? ALA J 55  GLY J 61  5 ? 7 
HELX_P HELX_P21 21 GLU I 132 ? LYS I 136 ? GLU J 132 LYS J 136 5 ? 5 
HELX_P HELX_P22 22 ALA J 55  ? GLY J 61  ? ALA K 55  GLY K 61  5 ? 7 
HELX_P HELX_P23 23 ALA K 55  ? GLY K 61  ? ALA L 55  GLY L 61  5 ? 7 
HELX_P HELX_P24 24 SER K 107 ? CME K 111 ? SER L 107 CME L 111 5 ? 5 
HELX_P HELX_P25 25 GLU K 133 ? GLY K 138 ? GLU L 133 GLY L 138 1 ? 6 
HELX_P HELX_P26 26 CYS L 57  ? GLY L 61  ? CYS M 57  GLY M 61  5 ? 5 
HELX_P HELX_P27 27 ASN L 131 ? THR L 137 ? ASN M 131 THR M 137 1 ? 7 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 57  SG  ? ? ? 1_555 A  CYS 146 SG ? ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.099 ? 
disulf2  disulf ? ? B CYS 57  SG  ? ? ? 1_555 B  CYS 146 SG ? ? B CYS 57  B CYS 146 1_555 ? ? ? ? ? ? ? 2.088 ? 
disulf3  disulf ? ? C CYS 57  SG  ? ? ? 1_555 C  CYS 146 SG ? ? D CYS 57  D CYS 146 1_555 ? ? ? ? ? ? ? 2.101 ? 
disulf4  disulf ? ? D CYS 57  SG  ? ? ? 1_555 D  CYS 146 SG ? ? E CYS 57  E CYS 146 1_555 ? ? ? ? ? ? ? 2.088 ? 
disulf5  disulf ? ? E CYS 57  SG  ? ? ? 1_555 E  CYS 146 SG ? ? F CYS 57  F CYS 146 1_555 ? ? ? ? ? ? ? 2.036 ? 
disulf6  disulf ? ? F CYS 57  SG  ? ? ? 1_555 F  CYS 146 SG ? ? G CYS 57  G CYS 146 1_555 ? ? ? ? ? ? ? 2.048 ? 
disulf7  disulf ? ? G CYS 57  SG  ? ? ? 1_555 G  CYS 146 SG ? ? H CYS 57  H CYS 146 1_555 ? ? ? ? ? ? ? 2.041 ? 
disulf8  disulf ? ? H CYS 57  SG  ? ? ? 1_555 H  CYS 146 SG ? ? I CYS 57  I CYS 146 1_555 ? ? ? ? ? ? ? 2.047 ? 
disulf9  disulf ? ? I CYS 57  SG  ? ? ? 1_555 I  CYS 146 SG ? ? J CYS 57  J CYS 146 1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf10 disulf ? ? J CYS 57  SG  ? ? ? 1_555 J  CYS 146 SG ? ? K CYS 57  K CYS 146 1_555 ? ? ? ? ? ? ? 2.046 ? 
disulf11 disulf ? ? K CYS 57  SG  ? ? ? 1_555 K  CYS 146 SG ? ? L CYS 57  L CYS 146 1_555 ? ? ? ? ? ? ? 2.044 ? 
disulf12 disulf ? ? L CYS 57  SG  ? ? ? 1_555 L  CYS 146 SG ? ? M CYS 57  M CYS 146 1_555 ? ? ? ? ? ? ? 2.036 ? 
covale1  covale ? ? A HIS 110 C   ? ? ? 1_555 A  CME 111 N  ? ? A HIS 110 A CME 111 1_555 ? ? ? ? ? ? ? 1.336 ? 
covale2  covale ? ? A CME 111 C   ? ? ? 1_555 A  ILE 112 N  ? ? A CME 111 A ILE 112 1_555 ? ? ? ? ? ? ? 1.319 ? 
covale3  covale ? ? B HIS 110 C   ? ? ? 1_555 B  CME 111 N  ? ? B HIS 110 B CME 111 1_555 ? ? ? ? ? ? ? 1.329 ? 
covale4  covale ? ? B CME 111 C   ? ? ? 1_555 B  ILE 112 N  ? ? B CME 111 B ILE 112 1_555 ? ? ? ? ? ? ? 1.337 ? 
covale5  covale ? ? C HIS 110 C   ? ? ? 1_555 C  CME 111 N  ? ? D HIS 110 D CME 111 1_555 ? ? ? ? ? ? ? 1.334 ? 
covale6  covale ? ? C CME 111 C   ? ? ? 1_555 C  ILE 112 N  ? ? D CME 111 D ILE 112 1_555 ? ? ? ? ? ? ? 1.332 ? 
covale7  covale ? ? D HIS 110 C   ? ? ? 1_555 D  CME 111 N  ? ? E HIS 110 E CME 111 1_555 ? ? ? ? ? ? ? 1.329 ? 
covale8  covale ? ? D CME 111 C   ? ? ? 1_555 D  ILE 112 N  ? ? E CME 111 E ILE 112 1_555 ? ? ? ? ? ? ? 1.334 ? 
covale9  covale ? ? E HIS 110 C   ? ? ? 1_555 E  CME 111 N  ? ? F HIS 110 F CME 111 1_555 ? ? ? ? ? ? ? 1.335 ? 
covale10 covale ? ? E CME 111 C   ? ? ? 1_555 E  ILE 112 N  ? ? F CME 111 F ILE 112 1_555 ? ? ? ? ? ? ? 1.336 ? 
covale11 covale ? ? F HIS 110 C   ? ? ? 1_555 F  CME 111 N  ? ? G HIS 110 G CME 111 1_555 ? ? ? ? ? ? ? 1.331 ? 
covale12 covale ? ? F CME 111 C   ? ? ? 1_555 F  ILE 112 N  ? ? G CME 111 G ILE 112 1_555 ? ? ? ? ? ? ? 1.329 ? 
covale13 covale ? ? G HIS 110 C   ? ? ? 1_555 G  CME 111 N  ? ? H HIS 110 H CME 111 1_555 ? ? ? ? ? ? ? 1.336 ? 
covale14 covale ? ? G CME 111 C   ? ? ? 1_555 G  ILE 112 N  ? ? H CME 111 H ILE 112 1_555 ? ? ? ? ? ? ? 1.333 ? 
covale15 covale ? ? H HIS 110 C   ? ? ? 1_555 H  CME 111 N  ? ? I HIS 110 I CME 111 1_555 ? ? ? ? ? ? ? 1.329 ? 
covale16 covale ? ? H CME 111 C   ? ? ? 1_555 H  ILE 112 N  ? ? I CME 111 I ILE 112 1_555 ? ? ? ? ? ? ? 1.334 ? 
covale17 covale ? ? I HIS 110 C   ? ? ? 1_555 I  CME 111 N  ? ? J HIS 110 J CME 111 1_555 ? ? ? ? ? ? ? 1.343 ? 
covale18 covale ? ? I CME 111 C   ? ? ? 1_555 I  ILE 112 N  ? ? J CME 111 J ILE 112 1_555 ? ? ? ? ? ? ? 1.326 ? 
covale19 covale ? ? J HIS 110 C   ? ? ? 1_555 J  CME 111 N  ? ? K HIS 110 K CME 111 1_555 ? ? ? ? ? ? ? 1.332 ? 
covale20 covale ? ? J CME 111 C   ? ? ? 1_555 J  ILE 112 N  ? ? K CME 111 K ILE 112 1_555 ? ? ? ? ? ? ? 1.325 ? 
covale21 covale ? ? K HIS 110 C   ? ? ? 1_555 K  CME 111 N  ? ? L HIS 110 L CME 111 1_555 ? ? ? ? ? ? ? 1.337 ? 
covale22 covale ? ? K CME 111 C   ? ? ? 1_555 K  ILE 112 N  ? ? L CME 111 L ILE 112 1_555 ? ? ? ? ? ? ? 1.334 ? 
covale23 covale ? ? L HIS 110 C   ? ? ? 1_555 L  CME 111 N  ? ? M HIS 110 M CME 111 1_555 ? ? ? ? ? ? ? 1.335 ? 
covale24 covale ? ? L CME 111 C   ? ? ? 1_555 L  ILE 112 N  ? ? M CME 111 M ILE 112 1_555 ? ? ? ? ? ? ? 1.335 ? 
metalc1  metalc ? ? I ASP 83  OD1 ? ? ? 1_555 LA ZN  .   ZN ? ? J ASP 83  J ZN  300 1_555 ? ? ? ? ? ? ? 1.943 ? 
metalc2  metalc ? ? A ASP 83  OD1 ? ? ? 1_555 N  ZN  .   ZN ? ? A ASP 83  A ZN  300 1_555 ? ? ? ? ? ? ? 1.944 ? 
metalc3  metalc ? ? C ASP 83  OD1 ? ? ? 1_555 T  ZN  .   ZN ? ? D ASP 83  D ZN  300 1_555 ? ? ? ? ? ? ? 1.954 ? 
metalc4  metalc ? ? G ASP 83  OD1 ? ? ? 1_555 FA ZN  .   ZN ? ? H ASP 83  H ZN  300 1_555 ? ? ? ? ? ? ? 1.962 ? 
metalc5  metalc ? ? K ASP 83  OD1 ? ? ? 1_555 RA ZN  .   ZN ? ? L ASP 83  L ZN  300 1_555 ? ? ? ? ? ? ? 1.967 ? 
metalc6  metalc ? ? H ASP 83  OD1 ? ? ? 1_555 IA ZN  .   ZN ? ? I ASP 83  I ZN  300 1_555 ? ? ? ? ? ? ? 1.983 ? 
metalc7  metalc ? ? J ASP 83  OD1 ? ? ? 1_555 OA ZN  .   ZN ? ? K ASP 83  K ZN  300 1_555 ? ? ? ? ? ? ? 1.996 ? 
metalc8  metalc ? ? B ASP 83  OD1 ? ? ? 1_555 Q  ZN  .   ZN ? ? B ASP 83  B ZN  300 1_555 ? ? ? ? ? ? ? 1.999 ? 
metalc9  metalc ? ? E HIS 48  NE2 ? ? ? 1_555 Y  CU1 .   CU ? ? F HIS 48  F CU1 200 1_555 ? ? ? ? ? ? ? 2.006 ? 
metalc10 metalc ? ? D ASP 83  OD1 ? ? ? 1_555 W  ZN  .   ZN ? ? E ASP 83  E ZN  300 1_555 ? ? ? ? ? ? ? 2.009 ? 
metalc11 metalc ? ? C HIS 120 NE2 ? ? ? 1_555 S  CU1 .   CU ? ? D HIS 120 D CU1 200 1_555 ? ? ? ? ? ? ? 2.018 ? 
metalc12 metalc ? ? B HIS 48  NE2 ? ? ? 1_555 P  CU1 .   CU ? ? B HIS 48  B CU1 200 1_555 ? ? ? ? ? ? ? 2.021 ? 
metalc13 metalc ? ? A HIS 48  NE2 ? ? ? 1_555 M  CU1 .   CU ? ? A HIS 48  A CU1 200 1_555 ? ? ? ? ? ? ? 2.023 ? 
metalc14 metalc ? ? F ASP 83  OD1 ? ? ? 1_555 CA ZN  .   ZN ? ? G ASP 83  G ZN  300 1_555 ? ? ? ? ? ? ? 2.023 ? 
metalc15 metalc ? ? F HIS 46  ND1 ? ? ? 1_555 BA CU1 .   CU ? ? G HIS 46  G CU1 200 1_555 ? ? ? ? ? ? ? 2.024 ? 
metalc16 metalc ? ? D HIS 48  NE2 ? ? ? 1_555 V  CU1 .   CU ? ? E HIS 48  E CU1 200 1_555 ? ? ? ? ? ? ? 2.028 ? 
metalc17 metalc ? ? F HIS 120 NE2 ? ? ? 1_555 BA CU1 .   CU ? ? G HIS 120 G CU1 200 1_555 ? ? ? ? ? ? ? 2.030 ? 
metalc18 metalc ? ? A HIS 46  ND1 ? ? ? 1_555 M  CU1 .   CU ? ? A HIS 46  A CU1 200 1_555 ? ? ? ? ? ? ? 2.030 ? 
metalc19 metalc ? ? C HIS 48  NE2 ? ? ? 1_555 S  CU1 .   CU ? ? D HIS 48  D CU1 200 1_555 ? ? ? ? ? ? ? 2.037 ? 
metalc20 metalc ? ? C HIS 46  ND1 ? ? ? 1_555 S  CU1 .   CU ? ? D HIS 46  D CU1 200 1_555 ? ? ? ? ? ? ? 2.042 ? 
metalc21 metalc ? ? I HIS 48  NE2 ? ? ? 1_555 KA CU1 .   CU ? ? J HIS 48  J CU1 200 1_555 ? ? ? ? ? ? ? 2.044 ? 
metalc22 metalc ? ? E ASP 83  OD1 ? ? ? 1_555 Z  ZN  .   ZN ? ? F ASP 83  F ZN  300 1_555 ? ? ? ? ? ? ? 2.046 ? 
metalc23 metalc ? ? D HIS 46  ND1 ? ? ? 1_555 V  CU1 .   CU ? ? E HIS 46  E CU1 200 1_555 ? ? ? ? ? ? ? 2.050 ? 
metalc24 metalc ? ? G HIS 48  NE2 ? ? ? 1_555 EA CU1 .   CU ? ? H HIS 48  H CU1 200 1_555 ? ? ? ? ? ? ? 2.052 ? 
metalc25 metalc ? ? D HIS 120 NE2 ? ? ? 1_555 V  CU1 .   CU ? ? E HIS 120 E CU1 200 1_555 ? ? ? ? ? ? ? 2.052 ? 
metalc26 metalc ? ? B HIS 120 NE2 ? ? ? 1_555 P  CU1 .   CU ? ? B HIS 120 B CU1 200 1_555 ? ? ? ? ? ? ? 2.052 ? 
metalc27 metalc ? ? G HIS 120 NE2 ? ? ? 1_555 EA CU1 .   CU ? ? H HIS 120 H CU1 200 1_555 ? ? ? ? ? ? ? 2.053 ? 
metalc28 metalc ? ? F HIS 48  NE2 ? ? ? 1_555 BA CU1 .   CU ? ? G HIS 48  G CU1 200 1_555 ? ? ? ? ? ? ? 2.056 ? 
metalc29 metalc ? ? K HIS 48  NE2 ? ? ? 1_555 QA CU1 .   CU ? ? L HIS 48  L CU1 200 1_555 ? ? ? ? ? ? ? 2.056 ? 
metalc30 metalc ? ? H HIS 48  NE2 ? ? ? 1_555 HA CU1 .   CU ? ? I HIS 48  I CU1 200 1_555 ? ? ? ? ? ? ? 2.056 ? 
metalc31 metalc ? ? J HIS 80  ND1 ? ? ? 1_555 OA ZN  .   ZN ? ? K HIS 80  K ZN  300 1_555 ? ? ? ? ? ? ? 2.057 ? 
metalc32 metalc ? ? E HIS 46  ND1 ? ? ? 1_555 Y  CU1 .   CU ? ? F HIS 46  F CU1 200 1_555 ? ? ? ? ? ? ? 2.060 ? 
metalc33 metalc ? ? L HIS 80  ND1 ? ? ? 1_555 UA ZN  .   ZN ? ? M HIS 80  M ZN  300 1_555 ? ? ? ? ? ? ? 2.060 ? 
metalc34 metalc ? ? A HIS 63  ND1 ? ? ? 1_555 N  ZN  .   ZN ? ? A HIS 63  A ZN  300 1_555 ? ? ? ? ? ? ? 2.061 ? 
metalc35 metalc ? ? K HIS 63  ND1 ? ? ? 1_555 RA ZN  .   ZN ? ? L HIS 63  L ZN  300 1_555 ? ? ? ? ? ? ? 2.062 ? 
metalc36 metalc ? ? G HIS 46  ND1 ? ? ? 1_555 EA CU1 .   CU ? ? H HIS 46  H CU1 200 1_555 ? ? ? ? ? ? ? 2.065 ? 
metalc37 metalc ? ? J HIS 48  NE2 ? ? ? 1_555 NA CU1 .   CU ? ? K HIS 48  K CU1 200 1_555 ? ? ? ? ? ? ? 2.069 ? 
metalc38 metalc ? ? A HIS 120 NE2 ? ? ? 1_555 M  CU1 .   CU ? ? A HIS 120 A CU1 200 1_555 ? ? ? ? ? ? ? 2.070 ? 
metalc39 metalc ? ? E HIS 80  ND1 ? ? ? 1_555 Z  ZN  .   ZN ? ? F HIS 80  F ZN  300 1_555 ? ? ? ? ? ? ? 2.071 ? 
metalc40 metalc ? ? E HIS 120 NE2 ? ? ? 1_555 Y  CU1 .   CU ? ? F HIS 120 F CU1 200 1_555 ? ? ? ? ? ? ? 2.074 ? 
metalc41 metalc ? ? D HIS 63  ND1 ? ? ? 1_555 W  ZN  .   ZN ? ? E HIS 63  E ZN  300 1_555 ? ? ? ? ? ? ? 2.075 ? 
metalc42 metalc ? ? I HIS 120 NE2 ? ? ? 1_555 KA CU1 .   CU ? ? J HIS 120 J CU1 200 1_555 ? ? ? ? ? ? ? 2.075 ? 
metalc43 metalc ? ? K HIS 120 NE2 ? ? ? 1_555 QA CU1 .   CU ? ? L HIS 120 L CU1 200 1_555 ? ? ? ? ? ? ? 2.077 ? 
metalc44 metalc ? ? B HIS 63  ND1 ? ? ? 1_555 Q  ZN  .   ZN ? ? B HIS 63  B ZN  300 1_555 ? ? ? ? ? ? ? 2.078 ? 
metalc45 metalc ? ? H HIS 120 NE2 ? ? ? 1_555 HA CU1 .   CU ? ? I HIS 120 I CU1 200 1_555 ? ? ? ? ? ? ? 2.079 ? 
metalc46 metalc ? ? C HIS 63  ND1 ? ? ? 1_555 T  ZN  .   ZN ? ? D HIS 63  D ZN  300 1_555 ? ? ? ? ? ? ? 2.080 ? 
metalc47 metalc ? ? I HIS 46  ND1 ? ? ? 1_555 KA CU1 .   CU ? ? J HIS 46  J CU1 200 1_555 ? ? ? ? ? ? ? 2.081 ? 
metalc48 metalc ? ? K HIS 46  ND1 ? ? ? 1_555 QA CU1 .   CU ? ? L HIS 46  L CU1 200 1_555 ? ? ? ? ? ? ? 2.083 ? 
metalc49 metalc ? ? G HIS 80  ND1 ? ? ? 1_555 FA ZN  .   ZN ? ? H HIS 80  H ZN  300 1_555 ? ? ? ? ? ? ? 2.084 ? 
metalc50 metalc ? ? B HIS 46  ND1 ? ? ? 1_555 P  CU1 .   CU ? ? B HIS 46  B CU1 200 1_555 ? ? ? ? ? ? ? 2.085 ? 
metalc51 metalc ? ? J HIS 46  ND1 ? ? ? 1_555 NA CU1 .   CU ? ? K HIS 46  K CU1 200 1_555 ? ? ? ? ? ? ? 2.085 ? 
metalc52 metalc ? ? I HIS 63  ND1 ? ? ? 1_555 LA ZN  .   ZN ? ? J HIS 63  J ZN  300 1_555 ? ? ? ? ? ? ? 2.087 ? 
metalc53 metalc ? ? D HIS 80  ND1 ? ? ? 1_555 W  ZN  .   ZN ? ? E HIS 80  E ZN  300 1_555 ? ? ? ? ? ? ? 2.090 ? 
metalc54 metalc ? ? E HIS 63  ND1 ? ? ? 1_555 Z  ZN  .   ZN ? ? F HIS 63  F ZN  300 1_555 ? ? ? ? ? ? ? 2.093 ? 
metalc55 metalc ? ? H HIS 46  ND1 ? ? ? 1_555 HA CU1 .   CU ? ? I HIS 46  I CU1 200 1_555 ? ? ? ? ? ? ? 2.098 ? 
metalc56 metalc ? ? G HIS 63  ND1 ? ? ? 1_555 FA ZN  .   ZN ? ? H HIS 63  H ZN  300 1_555 ? ? ? ? ? ? ? 2.106 ? 
metalc57 metalc ? ? B HIS 80  ND1 ? ? ? 1_555 Q  ZN  .   ZN ? ? B HIS 80  B ZN  300 1_555 ? ? ? ? ? ? ? 2.107 ? 
metalc58 metalc ? ? L HIS 48  NE2 ? ? ? 1_555 TA CU1 .   CU ? ? M HIS 48  M CU1 200 1_555 ? ? ? ? ? ? ? 2.108 ? 
metalc59 metalc ? ? A HIS 71  ND1 ? ? ? 1_555 N  ZN  .   ZN ? ? A HIS 71  A ZN  300 1_555 ? ? ? ? ? ? ? 2.109 ? 
metalc60 metalc ? ? K HIS 80  ND1 ? ? ? 1_555 RA ZN  .   ZN ? ? L HIS 80  L ZN  300 1_555 ? ? ? ? ? ? ? 2.110 ? 
metalc61 metalc ? ? D HIS 71  ND1 ? ? ? 1_555 W  ZN  .   ZN ? ? E HIS 71  E ZN  300 1_555 ? ? ? ? ? ? ? 2.111 ? 
metalc62 metalc ? ? F HIS 63  ND1 ? ? ? 1_555 CA ZN  .   ZN ? ? G HIS 63  G ZN  300 1_555 ? ? ? ? ? ? ? 2.112 ? 
metalc63 metalc ? ? C HIS 80  ND1 ? ? ? 1_555 T  ZN  .   ZN ? ? D HIS 80  D ZN  300 1_555 ? ? ? ? ? ? ? 2.112 ? 
metalc64 metalc ? ? A HIS 80  ND1 ? ? ? 1_555 N  ZN  .   ZN ? ? A HIS 80  A ZN  300 1_555 ? ? ? ? ? ? ? 2.115 ? 
metalc65 metalc ? ? B HIS 71  ND1 ? ? ? 1_555 Q  ZN  .   ZN ? ? B HIS 71  B ZN  300 1_555 ? ? ? ? ? ? ? 2.116 ? 
metalc66 metalc ? ? G HIS 71  ND1 ? ? ? 1_555 FA ZN  .   ZN ? ? H HIS 71  H ZN  300 1_555 ? ? ? ? ? ? ? 2.117 ? 
metalc67 metalc ? ? C HIS 71  ND1 ? ? ? 1_555 T  ZN  .   ZN ? ? D HIS 71  D ZN  300 1_555 ? ? ? ? ? ? ? 2.123 ? 
metalc68 metalc ? ? I HIS 71  ND1 ? ? ? 1_555 LA ZN  .   ZN ? ? J HIS 71  J ZN  300 1_555 ? ? ? ? ? ? ? 2.124 ? 
metalc69 metalc ? ? F HIS 80  ND1 ? ? ? 1_555 CA ZN  .   ZN ? ? G HIS 80  G ZN  300 1_555 ? ? ? ? ? ? ? 2.125 ? 
metalc70 metalc ? ? J HIS 120 NE2 ? ? ? 1_555 NA CU1 .   CU ? ? K HIS 120 K CU1 200 1_555 ? ? ? ? ? ? ? 2.128 ? 
metalc71 metalc ? ? K HIS 71  ND1 ? ? ? 1_555 RA ZN  .   ZN ? ? L HIS 71  L ZN  300 1_555 ? ? ? ? ? ? ? 2.131 ? 
metalc72 metalc ? ? E HIS 71  ND1 ? ? ? 1_555 Z  ZN  .   ZN ? ? F HIS 71  F ZN  300 1_555 ? ? ? ? ? ? ? 2.133 ? 
metalc73 metalc ? ? I HIS 80  ND1 ? ? ? 1_555 LA ZN  .   ZN ? ? J HIS 80  J ZN  300 1_555 ? ? ? ? ? ? ? 2.146 ? 
metalc74 metalc ? ? J HIS 71  ND1 ? ? ? 1_555 OA ZN  .   ZN ? ? K HIS 71  K ZN  300 1_555 ? ? ? ? ? ? ? 2.150 ? 
metalc75 metalc ? ? J HIS 63  ND1 ? ? ? 1_555 OA ZN  .   ZN ? ? K HIS 63  K ZN  300 1_555 ? ? ? ? ? ? ? 2.154 ? 
metalc76 metalc ? ? L HIS 46  ND1 ? ? ? 1_555 TA CU1 .   CU ? ? M HIS 46  M CU1 200 1_555 ? ? ? ? ? ? ? 2.155 ? 
metalc77 metalc ? ? L ASP 83  OD1 ? ? ? 1_555 UA ZN  .   ZN ? ? M ASP 83  M ZN  300 1_555 ? ? ? ? ? ? ? 2.158 ? 
metalc78 metalc ? ? H HIS 71  ND1 ? ? ? 1_555 IA ZN  .   ZN ? ? I HIS 71  I ZN  300 1_555 ? ? ? ? ? ? ? 2.159 ? 
metalc79 metalc ? ? F HIS 71  ND1 ? ? ? 1_555 CA ZN  .   ZN ? ? G HIS 71  G ZN  300 1_555 ? ? ? ? ? ? ? 2.162 ? 
metalc80 metalc ? ? H HIS 80  ND1 ? ? ? 1_555 IA ZN  .   ZN ? ? I HIS 80  I ZN  300 1_555 ? ? ? ? ? ? ? 2.169 ? 
metalc81 metalc ? ? H HIS 63  ND1 ? ? ? 1_555 IA ZN  .   ZN ? ? I HIS 63  I ZN  300 1_555 ? ? ? ? ? ? ? 2.176 ? 
metalc82 metalc ? ? L HIS 120 NE2 ? ? ? 1_555 TA CU1 .   CU ? ? M HIS 120 M CU1 200 1_555 ? ? ? ? ? ? ? 2.212 ? 
metalc83 metalc ? ? L HIS 63  ND1 ? ? ? 1_555 UA ZN  .   ZN ? ? M HIS 63  M ZN  300 1_555 ? ? ? ? ? ? ? 2.308 ? 
metalc84 metalc ? ? L HIS 71  ND1 ? ? ? 1_555 UA ZN  .   ZN ? ? M HIS 71  M ZN  300 1_555 ? ? ? ? ? ? ? 2.362 ? 
metalc85 metalc ? ? L ASP 83  OD2 ? ? ? 1_555 UA ZN  .   ZN ? ? M ASP 83  M ZN  300 1_555 ? ? ? ? ? ? ? 2.648 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
covale ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 4 ? 
C ? 5 ? 
D ? 4 ? 
E ? 5 ? 
F ? 4 ? 
G ? 5 ? 
H ? 4 ? 
I ? 5 ? 
J ? 4 ? 
K ? 5 ? 
L ? 4 ? 
M ? 5 ? 
N ? 4 ? 
O ? 5 ? 
P ? 4 ? 
Q ? 5 ? 
R ? 4 ? 
S ? 5 ? 
T ? 4 ? 
U ? 5 ? 
V ? 4 ? 
W ? 5 ? 
X ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
A 4 5 ? anti-parallel 
B 1 2 ? anti-parallel 
B 2 3 ? anti-parallel 
B 3 4 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? anti-parallel 
C 3 4 ? anti-parallel 
C 4 5 ? anti-parallel 
D 1 2 ? anti-parallel 
D 2 3 ? anti-parallel 
D 3 4 ? anti-parallel 
E 1 2 ? anti-parallel 
E 2 3 ? anti-parallel 
E 3 4 ? anti-parallel 
E 4 5 ? anti-parallel 
F 1 2 ? anti-parallel 
F 2 3 ? anti-parallel 
F 3 4 ? anti-parallel 
G 1 2 ? anti-parallel 
G 2 3 ? anti-parallel 
G 3 4 ? anti-parallel 
G 4 5 ? anti-parallel 
H 1 2 ? anti-parallel 
H 2 3 ? anti-parallel 
H 3 4 ? anti-parallel 
I 1 2 ? anti-parallel 
I 2 3 ? anti-parallel 
I 3 4 ? anti-parallel 
I 4 5 ? anti-parallel 
J 1 2 ? anti-parallel 
J 2 3 ? anti-parallel 
J 3 4 ? anti-parallel 
K 1 2 ? anti-parallel 
K 2 3 ? anti-parallel 
K 3 4 ? anti-parallel 
K 4 5 ? anti-parallel 
L 1 2 ? anti-parallel 
L 2 3 ? anti-parallel 
L 3 4 ? anti-parallel 
M 1 2 ? anti-parallel 
M 2 3 ? anti-parallel 
M 3 4 ? anti-parallel 
M 4 5 ? anti-parallel 
N 1 2 ? anti-parallel 
N 2 3 ? anti-parallel 
N 3 4 ? anti-parallel 
O 1 2 ? anti-parallel 
O 2 3 ? anti-parallel 
O 3 4 ? anti-parallel 
O 4 5 ? anti-parallel 
P 1 2 ? anti-parallel 
P 2 3 ? anti-parallel 
P 3 4 ? anti-parallel 
Q 1 2 ? anti-parallel 
Q 2 3 ? anti-parallel 
Q 3 4 ? anti-parallel 
Q 4 5 ? anti-parallel 
R 1 2 ? anti-parallel 
R 2 3 ? anti-parallel 
R 3 4 ? anti-parallel 
S 1 2 ? anti-parallel 
S 2 3 ? anti-parallel 
S 3 4 ? anti-parallel 
S 4 5 ? anti-parallel 
T 1 2 ? anti-parallel 
T 2 3 ? anti-parallel 
T 3 4 ? anti-parallel 
U 1 2 ? anti-parallel 
U 2 3 ? anti-parallel 
U 3 4 ? anti-parallel 
U 4 5 ? anti-parallel 
V 1 2 ? anti-parallel 
V 2 3 ? anti-parallel 
V 3 4 ? anti-parallel 
W 1 2 ? anti-parallel 
W 2 3 ? anti-parallel 
W 3 4 ? anti-parallel 
W 4 5 ? anti-parallel 
X 1 2 ? anti-parallel 
X 2 3 ? anti-parallel 
X 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
A 1 ALA A 95  ? ASP A 101 ? ALA A 95  ASP A 101 
A 2 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
A 3 GLN A 15  ? GLN A 22  ? GLN A 15  GLN A 22  
A 4 THR A 2   ? LEU A 8   ? THR A 2   LEU A 8   
A 5 GLY A 150 ? ILE A 151 ? GLY A 150 ILE A 151 
B 1 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
B 2 GLY A 41  ? HIS A 48  ? GLY A 41  HIS A 48  
B 3 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
B 4 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
C 1 ALA B 95  ? ASP B 101 ? ALA B 95  ASP B 101 
C 2 VAL B 29  ? LYS B 36  ? VAL B 29  LYS B 36  
C 3 GLN B 15  ? GLN B 22  ? GLN B 15  GLN B 22  
C 4 THR B 2   ? LYS B 9   ? THR B 2   LYS B 9   
C 5 GLY B 150 ? ILE B 151 ? GLY B 150 ILE B 151 
D 1 ASP B 83  ? ALA B 89  ? ASP B 83  ALA B 89  
D 2 GLY B 41  ? HIS B 48  ? GLY B 41  HIS B 48  
D 3 THR B 116 ? HIS B 120 ? THR B 116 HIS B 120 
D 4 ARG B 143 ? VAL B 148 ? ARG B 143 VAL B 148 
E 1 ALA C 95  ? ASP C 101 ? ALA D 95  ASP D 101 
E 2 VAL C 29  ? LYS C 36  ? VAL D 29  LYS D 36  
E 3 GLN C 15  ? GLN C 22  ? GLN D 15  GLN D 22  
E 4 THR C 2   ? LEU C 8   ? THR D 2   LEU D 8   
E 5 GLY C 150 ? ALA C 152 ? GLY D 150 ALA D 152 
F 1 ASP C 83  ? ALA C 89  ? ASP D 83  ALA D 89  
F 2 GLY C 41  ? HIS C 48  ? GLY D 41  HIS D 48  
F 3 THR C 116 ? HIS C 120 ? THR D 116 HIS D 120 
F 4 ARG C 143 ? VAL C 148 ? ARG D 143 VAL D 148 
G 1 ALA D 95  ? ASP D 101 ? ALA E 95  ASP E 101 
G 2 VAL D 29  ? LYS D 36  ? VAL E 29  LYS E 36  
G 3 GLN D 15  ? GLN D 22  ? GLN E 15  GLN E 22  
G 4 THR D 2   ? LYS D 9   ? THR E 2   LYS E 9   
G 5 GLY D 150 ? ILE D 151 ? GLY E 150 ILE E 151 
H 1 ASP D 83  ? ALA D 89  ? ASP E 83  ALA E 89  
H 2 GLY D 41  ? HIS D 48  ? GLY E 41  HIS E 48  
H 3 THR D 116 ? HIS D 120 ? THR E 116 HIS E 120 
H 4 ARG D 143 ? VAL D 148 ? ARG E 143 VAL E 148 
I 1 ALA E 95  ? ASP E 101 ? ALA F 95  ASP F 101 
I 2 VAL E 29  ? LYS E 36  ? VAL F 29  LYS F 36  
I 3 GLN E 15  ? GLN E 22  ? GLN F 15  GLN F 22  
I 4 THR E 2   ? LEU E 8   ? THR F 2   LEU F 8   
I 5 GLY E 150 ? ALA E 152 ? GLY F 150 ALA F 152 
J 1 ASP E 83  ? ALA E 89  ? ASP F 83  ALA F 89  
J 2 GLY E 41  ? HIS E 48  ? GLY F 41  HIS F 48  
J 3 THR E 116 ? HIS E 120 ? THR F 116 HIS F 120 
J 4 ARG E 143 ? VAL E 148 ? ARG F 143 VAL F 148 
K 1 ALA F 95  ? ASP F 101 ? ALA G 95  ASP G 101 
K 2 VAL F 29  ? LYS F 36  ? VAL G 29  LYS G 36  
K 3 GLN F 15  ? GLN F 22  ? GLN G 15  GLN G 22  
K 4 THR F 2   ? LYS F 9   ? THR G 2   LYS G 9   
K 5 GLY F 150 ? ALA F 152 ? GLY G 150 ALA G 152 
L 1 ASP F 83  ? ALA F 89  ? ASP G 83  ALA G 89  
L 2 GLY F 41  ? HIS F 48  ? GLY G 41  HIS G 48  
L 3 THR F 116 ? HIS F 120 ? THR G 116 HIS G 120 
L 4 ARG F 143 ? VAL F 148 ? ARG G 143 VAL G 148 
M 1 ALA G 95  ? ASP G 101 ? ALA H 95  ASP H 101 
M 2 VAL G 29  ? LYS G 36  ? VAL H 29  LYS H 36  
M 3 GLN G 15  ? GLN G 22  ? GLN H 15  GLN H 22  
M 4 THR G 2   ? LYS G 9   ? THR H 2   LYS H 9   
M 5 GLY G 150 ? ALA G 152 ? GLY H 150 ALA H 152 
N 1 ASP G 83  ? ALA G 89  ? ASP H 83  ALA H 89  
N 2 GLY G 41  ? HIS G 48  ? GLY H 41  HIS H 48  
N 3 THR G 116 ? HIS G 120 ? THR H 116 HIS H 120 
N 4 ARG G 143 ? VAL G 148 ? ARG H 143 VAL H 148 
O 1 ALA H 95  ? ASP H 101 ? ALA I 95  ASP I 101 
O 2 VAL H 29  ? LYS H 36  ? VAL I 29  LYS I 36  
O 3 GLN H 15  ? GLN H 22  ? GLN I 15  GLN I 22  
O 4 THR H 2   ? LEU H 8   ? THR I 2   LEU I 8   
O 5 GLY H 150 ? ILE H 151 ? GLY I 150 ILE I 151 
P 1 ASP H 83  ? ALA H 89  ? ASP I 83  ALA I 89  
P 2 GLY H 41  ? HIS H 48  ? GLY I 41  HIS I 48  
P 3 THR H 116 ? HIS H 120 ? THR I 116 HIS I 120 
P 4 ARG H 143 ? VAL H 148 ? ARG I 143 VAL I 148 
Q 1 ALA I 95  ? ASP I 101 ? ALA J 95  ASP J 101 
Q 2 VAL I 29  ? LYS I 36  ? VAL J 29  LYS J 36  
Q 3 GLN I 15  ? GLN I 22  ? GLN J 15  GLN J 22  
Q 4 THR I 2   ? LEU I 8   ? THR J 2   LEU J 8   
Q 5 GLY I 150 ? ILE I 151 ? GLY J 150 ILE J 151 
R 1 ASP I 83  ? ALA I 89  ? ASP J 83  ALA J 89  
R 2 GLY I 41  ? HIS I 48  ? GLY J 41  HIS J 48  
R 3 THR I 116 ? HIS I 120 ? THR J 116 HIS J 120 
R 4 ARG I 143 ? VAL I 148 ? ARG J 143 VAL J 148 
S 1 ALA J 95  ? ASP J 101 ? ALA K 95  ASP K 101 
S 2 VAL J 29  ? LYS J 36  ? VAL K 29  LYS K 36  
S 3 GLN J 15  ? GLN J 22  ? GLN K 15  GLN K 22  
S 4 THR J 2   ? LEU J 8   ? THR K 2   LEU K 8   
S 5 GLY J 150 ? ILE J 151 ? GLY K 150 ILE K 151 
T 1 ASP J 83  ? ALA J 89  ? ASP K 83  ALA K 89  
T 2 GLY J 41  ? HIS J 48  ? GLY K 41  HIS K 48  
T 3 THR J 116 ? HIS J 120 ? THR K 116 HIS K 120 
T 4 ARG J 143 ? VAL J 148 ? ARG K 143 VAL K 148 
U 1 ALA K 95  ? ASP K 101 ? ALA L 95  ASP L 101 
U 2 VAL K 29  ? LYS K 36  ? VAL L 29  LYS L 36  
U 3 GLN K 15  ? GLN K 22  ? GLN L 15  GLN L 22  
U 4 THR K 2   ? LEU K 8   ? THR L 2   LEU L 8   
U 5 GLY K 150 ? ILE K 151 ? GLY L 150 ILE L 151 
V 1 ASP K 83  ? ALA K 89  ? ASP L 83  ALA L 89  
V 2 GLY K 41  ? HIS K 48  ? GLY L 41  HIS L 48  
V 3 THR K 116 ? HIS K 120 ? THR L 116 HIS L 120 
V 4 ARG K 143 ? VAL K 148 ? ARG L 143 VAL L 148 
W 1 ALA L 95  ? ILE L 99  ? ALA M 95  ILE M 99  
W 2 LYS L 30  ? LYS L 36  ? LYS M 30  LYS M 36  
W 3 GLN L 15  ? GLN L 22  ? GLN M 15  GLN M 22  
W 4 THR L 2   ? LEU L 8   ? THR M 2   LEU M 8   
W 5 GLY L 150 ? ILE L 151 ? GLY M 150 ILE M 151 
X 1 ASP L 83  ? ALA L 89  ? ASP M 83  ALA M 89  
X 2 GLY L 41  ? HIS L 48  ? GLY M 41  HIS M 48  
X 3 THR L 116 ? HIS L 120 ? THR M 116 HIS M 120 
X 4 ARG L 143 ? VAL L 148 ? ARG M 143 VAL M 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 O ALA A 95  ? O ALA A 95  N ILE A 35  ? N ILE A 35  
A 2 3 O TRP A 32  ? O TRP A 32  N ASN A 19  ? N ASN A 19  
A 3 4 O GLY A 16  ? O GLY A 16  N LEU A 8   ? N LEU A 8   
A 4 5 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
B 1 2 O ALA A 89  ? O ALA A 89  N GLY A 41  ? N GLY A 41  
B 2 3 N HIS A 48  ? N HIS A 48  O THR A 116 ? O THR A 116 
B 3 4 N LEU A 117 ? N LEU A 117 O GLY A 147 ? O GLY A 147 
C 1 2 O ALA B 95  ? O ALA B 95  N ILE B 35  ? N ILE B 35  
C 2 3 O TRP B 32  ? O TRP B 32  N ASN B 19  ? N ASN B 19  
C 3 4 O GLY B 16  ? O GLY B 16  N LEU B 8   ? N LEU B 8   
C 4 5 N VAL B 5   ? N VAL B 5   O GLY B 150 ? O GLY B 150 
D 1 2 O ALA B 89  ? O ALA B 89  N GLY B 41  ? N GLY B 41  
D 2 3 N HIS B 48  ? N HIS B 48  O THR B 116 ? O THR B 116 
D 3 4 N LEU B 117 ? N LEU B 117 O GLY B 147 ? O GLY B 147 
E 1 2 O ILE C 99  ? O ILE D 99  N VAL C 31  ? N VAL D 31  
E 2 3 O TRP C 32  ? O TRP D 32  N ASN C 19  ? N ASN D 19  
E 3 4 O GLY C 16  ? O GLY D 16  N LEU C 8   ? N LEU D 8   
E 4 5 N VAL C 5   ? N VAL D 5   O GLY C 150 ? O GLY D 150 
F 1 2 O ALA C 89  ? O ALA D 89  N GLY C 41  ? N GLY D 41  
F 2 3 N HIS C 48  ? N HIS D 48  O THR C 116 ? O THR D 116 
F 3 4 N LEU C 117 ? N LEU D 117 O GLY C 147 ? O GLY D 147 
G 1 2 O ASP D 101 ? O ASP E 101 N VAL D 29  ? N VAL E 29  
G 2 3 O LYS D 36  ? O LYS E 36  N GLN D 15  ? N GLN E 15  
G 3 4 O GLN D 22  ? O GLN E 22  N THR D 2   ? N THR E 2   
G 4 5 N VAL D 5   ? N VAL E 5   O GLY D 150 ? O GLY E 150 
H 1 2 O ALA D 89  ? O ALA E 89  N GLY D 41  ? N GLY E 41  
H 2 3 N HIS D 48  ? N HIS E 48  O THR D 116 ? O THR E 116 
H 3 4 N LEU D 117 ? N LEU E 117 O GLY D 147 ? O GLY E 147 
I 1 2 O ILE E 99  ? O ILE F 99  N VAL E 31  ? N VAL F 31  
I 2 3 O TRP E 32  ? O TRP F 32  N ASN E 19  ? N ASN F 19  
I 3 4 O GLN E 22  ? O GLN F 22  N THR E 2   ? N THR F 2   
I 4 5 N VAL E 5   ? N VAL F 5   O GLY E 150 ? O GLY F 150 
J 1 2 O VAL E 87  ? O VAL F 87  N HIS E 43  ? N HIS F 43  
J 2 3 N HIS E 48  ? N HIS F 48  O THR E 116 ? O THR F 116 
J 3 4 N LEU E 117 ? N LEU F 117 O GLY E 147 ? O GLY F 147 
K 1 2 O ASP F 101 ? O ASP G 101 N VAL F 29  ? N VAL G 29  
K 2 3 O TRP F 32  ? O TRP G 32  N ASN F 19  ? N ASN G 19  
K 3 4 O GLY F 16  ? O GLY G 16  N LEU F 8   ? N LEU G 8   
K 4 5 N VAL F 5   ? N VAL G 5   O GLY F 150 ? O GLY G 150 
L 1 2 O ALA F 89  ? O ALA G 89  N GLY F 41  ? N GLY G 41  
L 2 3 N HIS F 48  ? N HIS G 48  O THR F 116 ? O THR G 116 
L 3 4 N LEU F 117 ? N LEU G 117 O GLY F 147 ? O GLY G 147 
M 1 2 O ILE G 99  ? O ILE H 99  N VAL G 31  ? N VAL H 31  
M 2 3 O LYS G 36  ? O LYS H 36  N GLN G 15  ? N GLN H 15  
M 3 4 O GLY G 16  ? O GLY H 16  N LEU G 8   ? N LEU H 8   
M 4 5 N VAL G 5   ? N VAL H 5   O GLY G 150 ? O GLY H 150 
N 1 2 O ALA G 89  ? O ALA H 89  N GLY G 41  ? N GLY H 41  
N 2 3 N HIS G 48  ? N HIS H 48  O THR G 116 ? O THR H 116 
N 3 4 N LEU G 117 ? N LEU H 117 O GLY G 147 ? O GLY H 147 
O 1 2 O ILE H 99  ? O ILE I 99  N VAL H 31  ? N VAL I 31  
O 2 3 O LYS H 36  ? O LYS I 36  N GLN H 15  ? N GLN I 15  
O 3 4 O GLY H 16  ? O GLY I 16  N LEU H 8   ? N LEU I 8   
O 4 5 N VAL H 5   ? N VAL I 5   O GLY H 150 ? O GLY I 150 
P 1 2 O ALA H 89  ? O ALA I 89  N GLY H 41  ? N GLY I 41  
P 2 3 N HIS H 48  ? N HIS I 48  O THR H 116 ? O THR I 116 
P 3 4 N LEU H 117 ? N LEU I 117 O GLY H 147 ? O GLY I 147 
Q 1 2 O ILE I 99  ? O ILE J 99  N VAL I 31  ? N VAL J 31  
Q 2 3 O TRP I 32  ? O TRP J 32  N ASN I 19  ? N ASN J 19  
Q 3 4 O PHE I 20  ? O PHE J 20  N ALA I 4   ? N ALA J 4   
Q 4 5 N VAL I 5   ? N VAL J 5   O GLY I 150 ? O GLY J 150 
R 1 2 O ALA I 89  ? O ALA J 89  N GLY I 41  ? N GLY J 41  
R 2 3 N HIS I 48  ? N HIS J 48  O THR I 116 ? O THR J 116 
R 3 4 N LEU I 117 ? N LEU J 117 O GLY I 147 ? O GLY J 147 
S 1 2 O ALA J 95  ? O ALA K 95  N ILE J 35  ? N ILE K 35  
S 2 3 O TRP J 32  ? O TRP K 32  N ASN J 19  ? N ASN K 19  
S 3 4 O GLY J 16  ? O GLY K 16  N LEU J 8   ? N LEU K 8   
S 4 5 N VAL J 5   ? N VAL K 5   O GLY J 150 ? O GLY K 150 
T 1 2 O VAL J 87  ? O VAL K 87  N HIS J 43  ? N HIS K 43  
T 2 3 N HIS J 48  ? N HIS K 48  O THR J 116 ? O THR K 116 
T 3 4 N VAL J 119 ? N VAL K 119 O ALA J 145 ? O ALA K 145 
U 1 2 O ASP K 101 ? O ASP L 101 N VAL K 29  ? N VAL L 29  
U 2 3 O TRP K 32  ? O TRP L 32  N ASN K 19  ? N ASN L 19  
U 3 4 O PHE K 20  ? O PHE L 20  N ALA K 4   ? N ALA L 4   
U 4 5 N VAL K 5   ? N VAL L 5   O GLY K 150 ? O GLY L 150 
V 1 2 O ALA K 89  ? O ALA L 89  N GLY K 41  ? N GLY L 41  
V 2 3 N HIS K 48  ? N HIS L 48  O THR K 116 ? O THR L 116 
V 3 4 N VAL K 119 ? N VAL L 119 O ALA K 145 ? O ALA L 145 
W 1 2 O ALA L 95  ? O ALA M 95  N ILE L 35  ? N ILE M 35  
W 2 3 O TRP L 32  ? O TRP M 32  N ASN L 19  ? N ASN M 19  
W 3 4 O PHE L 20  ? O PHE M 20  N ALA L 4   ? N ALA M 4   
W 4 5 N VAL L 5   ? N VAL M 5   O GLY L 150 ? O GLY M 150 
X 1 2 O ALA L 89  ? O ALA M 89  N GLY L 41  ? N GLY M 41  
X 2 3 N HIS L 48  ? N HIS M 48  O THR L 116 ? O THR M 116 
X 3 4 N VAL L 119 ? N VAL M 119 O ALA L 145 ? O ALA M 145 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE CU1 A 200' 
AC2 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN A 300'  
AC3 Software ? ? ? ? 10 'BINDING SITE FOR RESIDUE SO4 A 400' 
AC4 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE CU1 B 200' 
AC5 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN B 300'  
AC6 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE SO4 B 400' 
AC7 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE CU1 D 200' 
AC8 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN D 300'  
AC9 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 D 400' 
BC1 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE CU1 E 200' 
BC2 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ZN E 300'  
BC3 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE SO4 E 400' 
BC4 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE CU1 F 200' 
BC5 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN F 300'  
BC6 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE SO4 F 400' 
BC7 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE CU1 G 200' 
BC8 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN G 300'  
BC9 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 G 400' 
CC1 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE CU1 H 200' 
CC2 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN H 300'  
CC3 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE SO4 H 400' 
CC4 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE CU1 I 200' 
CC5 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN I 300'  
CC6 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE SO4 I 400' 
CC7 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE CU1 J 200' 
CC8 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN J 300'  
CC9 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 J 400' 
DC1 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE CU1 K 200' 
DC2 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN K 300'  
DC3 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE SO4 K 400' 
DC4 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE CU1 L 200' 
DC5 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN L 300'  
DC6 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 L 400' 
DC7 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE CU1 M 200' 
DC8 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN M 300'  
DC9 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE SO4 M 400' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1   AC1 4  HIS A  46  ? HIS A 46   . ? 1_555 ? 
2   AC1 4  HIS A  48  ? HIS A 48   . ? 1_555 ? 
3   AC1 4  HIS A  63  ? HIS A 63   . ? 1_555 ? 
4   AC1 4  HIS A  120 ? HIS A 120  . ? 1_555 ? 
5   AC2 4  HIS A  63  ? HIS A 63   . ? 1_555 ? 
6   AC2 4  HIS A  71  ? HIS A 71   . ? 1_555 ? 
7   AC2 4  HIS A  80  ? HIS A 80   . ? 1_555 ? 
8   AC2 4  ASP A  83  ? ASP A 83   . ? 1_555 ? 
9   AC3 10 GLU A  133 ? GLU A 133  . ? 1_555 ? 
10  AC3 10 THR A  137 ? THR A 137  . ? 1_555 ? 
11  AC3 10 ASN A  139 ? ASN A 139  . ? 1_555 ? 
12  AC3 10 ALA A  140 ? ALA A 140  . ? 1_555 ? 
13  AC3 10 GLY A  141 ? GLY A 141  . ? 1_555 ? 
14  AC3 10 HOH WA .   ? HOH A 170  . ? 1_555 ? 
15  AC3 10 HOH WA .   ? HOH A 779  . ? 1_555 ? 
16  AC3 10 HOH WA .   ? HOH A 1035 . ? 1_555 ? 
17  AC3 10 HOH WA .   ? HOH A 1109 . ? 1_555 ? 
18  AC3 10 HOH WA .   ? HOH A 1579 . ? 1_555 ? 
19  AC4 4  HIS B  46  ? HIS B 46   . ? 1_555 ? 
20  AC4 4  HIS B  48  ? HIS B 48   . ? 1_555 ? 
21  AC4 4  HIS B  63  ? HIS B 63   . ? 1_555 ? 
22  AC4 4  HIS B  120 ? HIS B 120  . ? 1_555 ? 
23  AC5 4  HIS B  63  ? HIS B 63   . ? 1_555 ? 
24  AC5 4  HIS B  71  ? HIS B 71   . ? 1_555 ? 
25  AC5 4  HIS B  80  ? HIS B 80   . ? 1_555 ? 
26  AC5 4  ASP B  83  ? ASP B 83   . ? 1_555 ? 
27  AC6 7  GLU B  133 ? GLU B 133  . ? 1_555 ? 
28  AC6 7  THR B  137 ? THR B 137  . ? 1_555 ? 
29  AC6 7  ASN B  139 ? ASN B 139  . ? 1_555 ? 
30  AC6 7  GLY B  141 ? GLY B 141  . ? 1_555 ? 
31  AC6 7  HOH XA .   ? HOH B 171  . ? 1_555 ? 
32  AC6 7  HOH XA .   ? HOH B 482  . ? 1_555 ? 
33  AC6 7  HOH XA .   ? HOH B 1055 . ? 1_555 ? 
34  AC7 4  HIS C  46  ? HIS D 46   . ? 1_555 ? 
35  AC7 4  HIS C  48  ? HIS D 48   . ? 1_555 ? 
36  AC7 4  HIS C  63  ? HIS D 63   . ? 1_555 ? 
37  AC7 4  HIS C  120 ? HIS D 120  . ? 1_555 ? 
38  AC8 4  HIS C  63  ? HIS D 63   . ? 1_555 ? 
39  AC8 4  HIS C  71  ? HIS D 71   . ? 1_555 ? 
40  AC8 4  HIS C  80  ? HIS D 80   . ? 1_555 ? 
41  AC8 4  ASP C  83  ? ASP D 83   . ? 1_555 ? 
42  AC9 8  GLU C  133 ? GLU D 133  . ? 1_555 ? 
43  AC9 8  THR C  137 ? THR D 137  . ? 1_555 ? 
44  AC9 8  ASN C  139 ? ASN D 139  . ? 1_555 ? 
45  AC9 8  GLY C  141 ? GLY D 141  . ? 1_555 ? 
46  AC9 8  HOH YA .   ? HOH D 182  . ? 1_555 ? 
47  AC9 8  HOH YA .   ? HOH D 608  . ? 1_555 ? 
48  AC9 8  HOH YA .   ? HOH D 824  . ? 1_555 ? 
49  AC9 8  HOH YA .   ? HOH D 1058 . ? 1_555 ? 
50  BC1 4  HIS D  46  ? HIS E 46   . ? 1_555 ? 
51  BC1 4  HIS D  48  ? HIS E 48   . ? 1_555 ? 
52  BC1 4  HIS D  63  ? HIS E 63   . ? 1_555 ? 
53  BC1 4  HIS D  120 ? HIS E 120  . ? 1_555 ? 
54  BC2 5  HIS D  63  ? HIS E 63   . ? 1_555 ? 
55  BC2 5  HIS D  71  ? HIS E 71   . ? 1_555 ? 
56  BC2 5  HIS D  80  ? HIS E 80   . ? 1_555 ? 
57  BC2 5  ASP D  83  ? ASP E 83   . ? 1_555 ? 
58  BC2 5  LYS D  136 ? LYS E 136  . ? 1_555 ? 
59  BC3 7  GLU D  133 ? GLU E 133  . ? 1_555 ? 
60  BC3 7  THR D  137 ? THR E 137  . ? 1_555 ? 
61  BC3 7  ASN D  139 ? ASN E 139  . ? 1_555 ? 
62  BC3 7  GLY D  141 ? GLY E 141  . ? 1_555 ? 
63  BC3 7  HOH ZA .   ? HOH E 187  . ? 1_555 ? 
64  BC3 7  HOH ZA .   ? HOH E 460  . ? 1_555 ? 
65  BC3 7  HOH ZA .   ? HOH E 1164 . ? 1_555 ? 
66  BC4 4  HIS E  46  ? HIS F 46   . ? 1_555 ? 
67  BC4 4  HIS E  48  ? HIS F 48   . ? 1_555 ? 
68  BC4 4  HIS E  63  ? HIS F 63   . ? 1_555 ? 
69  BC4 4  HIS E  120 ? HIS F 120  . ? 1_555 ? 
70  BC5 4  HIS E  63  ? HIS F 63   . ? 1_555 ? 
71  BC5 4  HIS E  71  ? HIS F 71   . ? 1_555 ? 
72  BC5 4  HIS E  80  ? HIS F 80   . ? 1_555 ? 
73  BC5 4  ASP E  83  ? ASP F 83   . ? 1_555 ? 
74  BC6 6  GLU E  133 ? GLU F 133  . ? 1_555 ? 
75  BC6 6  THR E  137 ? THR F 137  . ? 1_555 ? 
76  BC6 6  ASN E  139 ? ASN F 139  . ? 1_555 ? 
77  BC6 6  ALA E  140 ? ALA F 140  . ? 1_555 ? 
78  BC6 6  GLY E  141 ? GLY F 141  . ? 1_555 ? 
79  BC6 6  HOH AB .   ? HOH F 274  . ? 1_555 ? 
80  BC7 4  HIS F  46  ? HIS G 46   . ? 1_555 ? 
81  BC7 4  HIS F  48  ? HIS G 48   . ? 1_555 ? 
82  BC7 4  HIS F  63  ? HIS G 63   . ? 1_555 ? 
83  BC7 4  HIS F  120 ? HIS G 120  . ? 1_555 ? 
84  BC8 4  HIS F  63  ? HIS G 63   . ? 1_555 ? 
85  BC8 4  HIS F  71  ? HIS G 71   . ? 1_555 ? 
86  BC8 4  HIS F  80  ? HIS G 80   . ? 1_555 ? 
87  BC8 4  ASP F  83  ? ASP G 83   . ? 1_555 ? 
88  BC9 8  GLU F  133 ? GLU G 133  . ? 1_555 ? 
89  BC9 8  THR F  137 ? THR G 137  . ? 1_555 ? 
90  BC9 8  ASN F  139 ? ASN G 139  . ? 1_555 ? 
91  BC9 8  ALA F  140 ? ALA G 140  . ? 1_555 ? 
92  BC9 8  GLY F  141 ? GLY G 141  . ? 1_555 ? 
93  BC9 8  HOH BB .   ? HOH G 857  . ? 1_555 ? 
94  BC9 8  HOH BB .   ? HOH G 883  . ? 1_555 ? 
95  BC9 8  HOH BB .   ? HOH G 1243 . ? 1_555 ? 
96  CC1 4  HIS G  46  ? HIS H 46   . ? 1_555 ? 
97  CC1 4  HIS G  48  ? HIS H 48   . ? 1_555 ? 
98  CC1 4  HIS G  63  ? HIS H 63   . ? 1_555 ? 
99  CC1 4  HIS G  120 ? HIS H 120  . ? 1_555 ? 
100 CC2 4  HIS G  63  ? HIS H 63   . ? 1_555 ? 
101 CC2 4  HIS G  71  ? HIS H 71   . ? 1_555 ? 
102 CC2 4  HIS G  80  ? HIS H 80   . ? 1_555 ? 
103 CC2 4  ASP G  83  ? ASP H 83   . ? 1_555 ? 
104 CC3 6  GLU G  133 ? GLU H 133  . ? 1_555 ? 
105 CC3 6  THR G  137 ? THR H 137  . ? 1_555 ? 
106 CC3 6  ASN G  139 ? ASN H 139  . ? 1_555 ? 
107 CC3 6  GLY G  141 ? GLY H 141  . ? 1_555 ? 
108 CC3 6  HOH CB .   ? HOH H 750  . ? 1_555 ? 
109 CC3 6  HOH CB .   ? HOH H 1048 . ? 1_555 ? 
110 CC4 4  HIS H  46  ? HIS I 46   . ? 1_555 ? 
111 CC4 4  HIS H  48  ? HIS I 48   . ? 1_555 ? 
112 CC4 4  HIS H  63  ? HIS I 63   . ? 1_555 ? 
113 CC4 4  HIS H  120 ? HIS I 120  . ? 1_555 ? 
114 CC5 4  HIS H  63  ? HIS I 63   . ? 1_555 ? 
115 CC5 4  HIS H  71  ? HIS I 71   . ? 1_555 ? 
116 CC5 4  HIS H  80  ? HIS I 80   . ? 1_555 ? 
117 CC5 4  ASP H  83  ? ASP I 83   . ? 1_555 ? 
118 CC6 5  GLU H  133 ? GLU I 133  . ? 1_555 ? 
119 CC6 5  THR H  137 ? THR I 137  . ? 1_555 ? 
120 CC6 5  ASN H  139 ? ASN I 139  . ? 1_555 ? 
121 CC6 5  ALA H  140 ? ALA I 140  . ? 1_555 ? 
122 CC6 5  GLY H  141 ? GLY I 141  . ? 1_555 ? 
123 CC7 4  HIS I  46  ? HIS J 46   . ? 1_555 ? 
124 CC7 4  HIS I  48  ? HIS J 48   . ? 1_555 ? 
125 CC7 4  HIS I  63  ? HIS J 63   . ? 1_555 ? 
126 CC7 4  HIS I  120 ? HIS J 120  . ? 1_555 ? 
127 CC8 4  HIS I  63  ? HIS J 63   . ? 1_555 ? 
128 CC8 4  HIS I  71  ? HIS J 71   . ? 1_555 ? 
129 CC8 4  HIS I  80  ? HIS J 80   . ? 1_555 ? 
130 CC8 4  ASP I  83  ? ASP J 83   . ? 1_555 ? 
131 CC9 8  GLU I  133 ? GLU J 133  . ? 1_555 ? 
132 CC9 8  THR I  137 ? THR J 137  . ? 1_555 ? 
133 CC9 8  ASN I  139 ? ASN J 139  . ? 1_555 ? 
134 CC9 8  ALA I  140 ? ALA J 140  . ? 1_555 ? 
135 CC9 8  GLY I  141 ? GLY J 141  . ? 1_555 ? 
136 CC9 8  HOH EB .   ? HOH J 391  . ? 1_555 ? 
137 CC9 8  HOH EB .   ? HOH J 1378 . ? 1_555 ? 
138 CC9 8  HOH EB .   ? HOH J 1547 . ? 1_555 ? 
139 DC1 4  HIS J  46  ? HIS K 46   . ? 1_555 ? 
140 DC1 4  HIS J  48  ? HIS K 48   . ? 1_555 ? 
141 DC1 4  HIS J  63  ? HIS K 63   . ? 1_555 ? 
142 DC1 4  HIS J  120 ? HIS K 120  . ? 1_555 ? 
143 DC2 4  HIS J  63  ? HIS K 63   . ? 1_555 ? 
144 DC2 4  HIS J  71  ? HIS K 71   . ? 1_555 ? 
145 DC2 4  HIS J  80  ? HIS K 80   . ? 1_555 ? 
146 DC2 4  ASP J  83  ? ASP K 83   . ? 1_555 ? 
147 DC3 5  GLU J  133 ? GLU K 133  . ? 1_555 ? 
148 DC3 5  THR J  137 ? THR K 137  . ? 1_555 ? 
149 DC3 5  ASN J  139 ? ASN K 139  . ? 1_555 ? 
150 DC3 5  ALA J  140 ? ALA K 140  . ? 1_555 ? 
151 DC3 5  GLY J  141 ? GLY K 141  . ? 1_555 ? 
152 DC4 4  HIS K  46  ? HIS L 46   . ? 1_555 ? 
153 DC4 4  HIS K  48  ? HIS L 48   . ? 1_555 ? 
154 DC4 4  HIS K  63  ? HIS L 63   . ? 1_555 ? 
155 DC4 4  HIS K  120 ? HIS L 120  . ? 1_555 ? 
156 DC5 4  HIS K  63  ? HIS L 63   . ? 1_555 ? 
157 DC5 4  HIS K  71  ? HIS L 71   . ? 1_555 ? 
158 DC5 4  HIS K  80  ? HIS L 80   . ? 1_555 ? 
159 DC5 4  ASP K  83  ? ASP L 83   . ? 1_555 ? 
160 DC6 8  LYS K  122 ? LYS L 122  . ? 1_555 ? 
161 DC6 8  GLU K  133 ? GLU L 133  . ? 1_555 ? 
162 DC6 8  THR K  137 ? THR L 137  . ? 1_555 ? 
163 DC6 8  ASN K  139 ? ASN L 139  . ? 1_555 ? 
164 DC6 8  ALA K  140 ? ALA L 140  . ? 1_555 ? 
165 DC6 8  GLY K  141 ? GLY L 141  . ? 1_555 ? 
166 DC6 8  HOH GB .   ? HOH L 162  . ? 1_555 ? 
167 DC6 8  HOH GB .   ? HOH L 527  . ? 1_555 ? 
168 DC7 4  HIS L  46  ? HIS M 46   . ? 1_555 ? 
169 DC7 4  HIS L  48  ? HIS M 48   . ? 1_555 ? 
170 DC7 4  HIS L  63  ? HIS M 63   . ? 1_555 ? 
171 DC7 4  HIS L  120 ? HIS M 120  . ? 1_555 ? 
172 DC8 4  HIS L  63  ? HIS M 63   . ? 1_555 ? 
173 DC8 4  HIS L  71  ? HIS M 71   . ? 1_555 ? 
174 DC8 4  HIS L  80  ? HIS M 80   . ? 1_555 ? 
175 DC8 4  ASP L  83  ? ASP M 83   . ? 1_555 ? 
176 DC9 5  GLU L  133 ? GLU M 133  . ? 1_555 ? 
177 DC9 5  THR L  137 ? THR M 137  . ? 1_555 ? 
178 DC9 5  ASN L  139 ? ASN M 139  . ? 1_555 ? 
179 DC9 5  ALA L  140 ? ALA M 140  . ? 1_555 ? 
180 DC9 5  GLY L  141 ? GLY M 141  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          3T5W 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    3T5W 
_atom_sites.fract_transf_matrix[1][1]   0.013498 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006125 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.005759 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CU 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1     N  N   . ALA A  1 1   ? 26.590 19.106  -13.004  1.00 17.65 ? 1    ALA A N   1 
ATOM   2     C  CA  . ALA A  1 1   ? 25.682 18.902  -14.167  1.00 17.04 ? 1    ALA A CA  1 
ATOM   3     C  C   . ALA A  1 1   ? 24.892 20.161  -14.505  1.00 16.28 ? 1    ALA A C   1 
ATOM   4     O  O   . ALA A  1 1   ? 24.598 20.976  -13.618  1.00 17.98 ? 1    ALA A O   1 
ATOM   5     C  CB  . ALA A  1 1   ? 24.727 17.721  -13.909  1.00 17.50 ? 1    ALA A CB  1 
ATOM   6     N  N   . THR A  1 2   ? 24.550 20.312  -15.783  1.00 14.20 ? 2    THR A N   1 
ATOM   7     C  CA  . THR A  1 2   ? 23.739 21.434  -16.250  1.00 12.59 ? 2    THR A CA  1 
ATOM   8     C  C   . THR A  1 2   ? 22.442 20.907  -16.851  1.00 10.59 ? 2    THR A C   1 
ATOM   9     O  O   . THR A  1 2   ? 22.415 19.863  -17.498  1.00 8.92  ? 2    THR A O   1 
ATOM   10    C  CB  . THR A  1 2   ? 24.476 22.257  -17.319  1.00 13.10 ? 2    THR A CB  1 
ATOM   11    O  OG1 . THR A  1 2   ? 25.765 22.617  -16.826  1.00 15.68 ? 2    THR A OG1 1 
ATOM   12    C  CG2 . THR A  1 2   ? 23.716 23.529  -17.664  1.00 14.93 ? 2    THR A CG2 1 
ATOM   13    N  N   . LYS A  1 3   ? 21.369 21.648  -16.642  1.00 8.94  ? 3    LYS A N   1 
ATOM   14    C  CA  . LYS A  1 3   ? 20.073 21.243  -17.155  1.00 7.92  ? 3    LYS A CA  1 
ATOM   15    C  C   . LYS A  1 3   ? 19.442 22.425  -17.849  1.00 6.50  ? 3    LYS A C   1 
ATOM   16    O  O   . LYS A  1 3   ? 19.676 23.594  -17.472  1.00 6.00  ? 3    LYS A O   1 
ATOM   17    C  CB  . LYS A  1 3   ? 19.162 20.750  -16.034  1.00 8.36  ? 3    LYS A CB  1 
ATOM   18    C  CG  . LYS A  1 3   ? 19.769 19.639  -15.184  1.00 11.54 ? 3    LYS A CG  1 
ATOM   19    C  CD  . LYS A  1 3   ? 18.754 19.153  -14.148  1.00 17.15 ? 3    LYS A CD  1 
ATOM   20    C  CE  . LYS A  1 3   ? 19.320 17.983  -13.338  1.00 19.08 ? 3    LYS A CE  1 
ATOM   21    N  NZ  . LYS A  1 3   ? 18.242 17.254  -12.585  1.00 23.90 ? 3    LYS A NZ  1 
ATOM   22    N  N   . ALA A  1 4   ? 18.660 22.121  -18.878  1.00 5.36  ? 4    ALA A N   1 
ATOM   23    C  CA  . ALA A  1 4   ? 17.956 23.142  -19.649  1.00 3.93  ? 4    ALA A CA  1 
ATOM   24    C  C   . ALA A  1 4   ? 16.558 22.637  -19.977  1.00 3.92  ? 4    ALA A C   1 
ATOM   25    O  O   . ALA A  1 4   ? 16.275 21.450  -19.850  1.00 4.31  ? 4    ALA A O   1 
ATOM   26    C  CB  . ALA A  1 4   ? 18.730 23.494  -20.934  1.00 3.56  ? 4    ALA A CB  1 
ATOM   27    N  N   . VAL A  1 5   ? 15.672 23.540  -20.376  1.00 4.30  ? 5    VAL A N   1 
ATOM   28    C  CA  . VAL A  1 5   ? 14.309 23.122  -20.676  1.00 4.23  ? 5    VAL A CA  1 
ATOM   29    C  C   . VAL A  1 5   ? 13.730 24.031  -21.766  1.00 4.29  ? 5    VAL A C   1 
ATOM   30    O  O   . VAL A  1 5   ? 14.147 25.183  -21.909  1.00 3.89  ? 5    VAL A O   1 
ATOM   31    C  CB  . VAL A  1 5   ? 13.439 23.105  -19.387  1.00 4.94  ? 5    VAL A CB  1 
ATOM   32    C  CG1 . VAL A  1 5   ? 13.286 24.504  -18.782  1.00 3.83  ? 5    VAL A CG1 1 
ATOM   33    C  CG2 . VAL A  1 5   ? 12.070 22.437  -19.643  1.00 5.83  ? 5    VAL A CG2 1 
ATOM   34    N  N   . CYS A  1 6   ? 12.773 23.513  -22.531  1.00 3.81  ? 6    CYS A N   1 
ATOM   35    C  CA  . CYS A  1 6   ? 12.161 24.283  -23.582  1.00 3.09  ? 6    CYS A CA  1 
ATOM   36    C  C   . CYS A  1 6   ? 10.693 23.941  -23.648  1.00 3.56  ? 6    CYS A C   1 
ATOM   37    O  O   . CYS A  1 6   ? 10.327 22.760  -23.690  1.00 3.14  ? 6    CYS A O   1 
ATOM   38    C  CB  . CYS A  1 6   ? 12.843 23.977  -24.923  1.00 4.01  ? 6    CYS A CB  1 
ATOM   39    S  SG  . CYS A  1 6   ? 12.172 24.899  -26.275  1.00 6.11  ? 6    CYS A SG  1 
ATOM   40    N  N   . VAL A  1 7   ? 9.860  24.984  -23.630  1.00 2.50  ? 7    VAL A N   1 
ATOM   41    C  CA  . VAL A  1 7   ? 8.429  24.822  -23.877  1.00 2.27  ? 7    VAL A CA  1 
ATOM   42    C  C   . VAL A  1 7   ? 8.130  25.120  -25.323  1.00 2.70  ? 7    VAL A C   1 
ATOM   43    O  O   . VAL A  1 7   ? 8.311  26.249  -25.797  1.00 2.00  ? 7    VAL A O   1 
ATOM   44    C  CB  . VAL A  1 7   ? 7.574  25.677  -22.926  1.00 2.75  ? 7    VAL A CB  1 
ATOM   45    C  CG1 . VAL A  1 7   ? 6.057  25.456  -23.194  1.00 3.96  ? 7    VAL A CG1 1 
ATOM   46    C  CG2 . VAL A  1 7   ? 7.930  25.330  -21.495  1.00 3.26  ? 7    VAL A CG2 1 
ATOM   47    N  N   . LEU A  1 8   ? 7.665  24.089  -26.030  1.00 2.86  ? 8    LEU A N   1 
ATOM   48    C  CA  . LEU A  1 8   ? 7.315  24.231  -27.426  1.00 3.30  ? 8    LEU A CA  1 
ATOM   49    C  C   . LEU A  1 8   ? 5.839  24.601  -27.617  1.00 3.66  ? 8    LEU A C   1 
ATOM   50    O  O   . LEU A  1 8   ? 4.964  23.900  -27.112  1.00 2.95  ? 8    LEU A O   1 
ATOM   51    C  CB  . LEU A  1 8   ? 7.605  22.924  -28.173  1.00 3.90  ? 8    LEU A CB  1 
ATOM   52    C  CG  . LEU A  1 8   ? 9.076  22.466  -28.212  1.00 6.40  ? 8    LEU A CG  1 
ATOM   53    C  CD1 . LEU A  1 8   ? 9.082  21.092  -28.836  1.00 8.15  ? 8    LEU A CD1 1 
ATOM   54    C  CD2 . LEU A  1 8   ? 9.887  23.374  -29.075  1.00 5.90  ? 8    LEU A CD2 1 
ATOM   55    N  N   . LYS A  1 9   ? 5.604  25.711  -28.326  1.00 4.07  ? 9    LYS A N   1 
ATOM   56    C  CA  . LYS A  1 9   ? 4.257  26.192  -28.719  1.00 4.24  ? 9    LYS A CA  1 
ATOM   57    C  C   . LYS A  1 9   ? 4.295  26.797  -30.126  1.00 4.87  ? 9    LYS A C   1 
ATOM   58    O  O   . LYS A  1 9   ? 5.337  27.251  -30.594  1.00 4.83  ? 9    LYS A O   1 
ATOM   59    C  CB  . LYS A  1 9   ? 3.752  27.278  -27.763  1.00 5.01  ? 9    LYS A CB  1 
ATOM   60    C  CG  . LYS A  1 9   ? 3.729  26.956  -26.291  1.00 8.22  ? 9    LYS A CG  1 
ATOM   61    C  CD  . LYS A  1 9   ? 2.985  28.057  -25.538  1.00 12.93 ? 9    LYS A CD  1 
ATOM   62    C  CE  . LYS A  1 9   ? 3.286  28.042  -24.061  1.00 18.43 ? 9    LYS A CE  1 
ATOM   63    N  NZ  . LYS A  1 9   ? 2.605  26.926  -23.356  1.00 21.72 ? 9    LYS A NZ  1 
ATOM   64    N  N   . GLY A  1 10  ? 3.153  26.834  -30.812  1.00 4.71  ? 10   GLY A N   1 
ATOM   65    C  CA  . GLY A  1 10  ? 3.109  27.458  -32.142  1.00 5.56  ? 10   GLY A CA  1 
ATOM   66    C  C   . GLY A  1 10  ? 1.681  27.894  -32.434  1.00 6.65  ? 10   GLY A C   1 
ATOM   67    O  O   . GLY A  1 10  ? 0.873  28.010  -31.506  1.00 6.81  ? 10   GLY A O   1 
ATOM   68    N  N   . ASP A  1 11  ? 1.379  28.167  -33.705  1.00 7.47  ? 11   ASP A N   1 
ATOM   69    C  CA  . ASP A  1 11  ? 0.064  28.705  -34.081  1.00 8.92  ? 11   ASP A CA  1 
ATOM   70    C  C   . ASP A  1 11  ? -0.982 27.587  -34.082  1.00 8.60  ? 11   ASP A C   1 
ATOM   71    O  O   . ASP A  1 11  ? -2.194 27.853  -33.926  1.00 9.36  ? 11   ASP A O   1 
ATOM   72    C  CB  . ASP A  1 11  ? 0.161  29.367  -35.459  1.00 9.90  ? 11   ASP A CB  1 
ATOM   73    C  CG  . ASP A  1 11  ? -1.102 30.127  -35.872  1.00 13.94 ? 11   ASP A CG  1 
ATOM   74    O  OD1 . ASP A  1 11  ? -1.604 30.984  -35.110  1.00 18.41 ? 11   ASP A OD1 1 
ATOM   75    O  OD2 . ASP A  1 11  ? -1.592 29.878  -37.002  1.00 19.84 ? 11   ASP A OD2 1 
ATOM   76    N  N   . GLY A  1 12  ? -0.507 26.354  -34.250  1.00 7.14  ? 12   GLY A N   1 
ATOM   77    C  CA  . GLY A  1 12  ? -1.363 25.166  -34.368  1.00 5.68  ? 12   GLY A CA  1 
ATOM   78    C  C   . GLY A  1 12  ? -1.375 24.372  -33.076  1.00 5.10  ? 12   GLY A C   1 
ATOM   79    O  O   . GLY A  1 12  ? -1.050 24.913  -32.026  1.00 5.28  ? 12   GLY A O   1 
ATOM   80    N  N   . PRO A  1 13  ? -1.756 23.082  -33.143  1.00 3.86  ? 13   PRO A N   1 
ATOM   81    C  CA  . PRO A  1 13  ? -1.895 22.202  -31.976  1.00 4.00  ? 13   PRO A CA  1 
ATOM   82    C  C   . PRO A  1 13  ? -0.595 21.644  -31.367  1.00 3.38  ? 13   PRO A C   1 
ATOM   83    O  O   . PRO A  1 13  ? -0.649 20.974  -30.330  1.00 3.79  ? 13   PRO A O   1 
ATOM   84    C  CB  . PRO A  1 13  ? -2.731 21.037  -32.516  1.00 4.44  ? 13   PRO A CB  1 
ATOM   85    C  CG  . PRO A  1 13  ? -2.333 20.944  -33.940  1.00 4.52  ? 13   PRO A CG  1 
ATOM   86    C  CD  . PRO A  1 13  ? -2.159 22.397  -34.393  1.00 4.72  ? 13   PRO A CD  1 
ATOM   87    N  N   . VAL A  1 14  ? 0.555  21.900  -31.986  1.00 2.77  ? 14   VAL A N   1 
ATOM   88    C  CA  . VAL A  1 14  ? 1.787  21.286  -31.473  1.00 2.99  ? 14   VAL A CA  1 
ATOM   89    C  C   . VAL A  1 14  ? 2.266  21.949  -30.182  1.00 3.69  ? 14   VAL A C   1 
ATOM   90    O  O   . VAL A  1 14  ? 2.466  23.170  -30.117  1.00 4.59  ? 14   VAL A O   1 
ATOM   91    C  CB  . VAL A  1 14  ? 2.919  21.209  -32.524  1.00 3.09  ? 14   VAL A CB  1 
ATOM   92    C  CG1 . VAL A  1 14  ? 4.181  20.537  -31.917  1.00 3.40  ? 14   VAL A CG1 1 
ATOM   93    C  CG2 . VAL A  1 14  ? 2.461  20.466  -33.778  1.00 2.00  ? 14   VAL A CG2 1 
ATOM   94    N  N   . GLN A  1 15  ? 2.399  21.143  -29.143  1.00 3.93  ? 15   GLN A N   1 
ATOM   95    C  CA  . GLN A  1 15  ? 2.787  21.634  -27.807  1.00 5.34  ? 15   GLN A CA  1 
ATOM   96    C  C   . GLN A  1 15  ? 3.656  20.572  -27.161  1.00 5.53  ? 15   GLN A C   1 
ATOM   97    O  O   . GLN A  1 15  ? 3.342  19.381  -27.226  1.00 5.26  ? 15   GLN A O   1 
ATOM   98    C  CB  . GLN A  1 15  ? 1.571  21.799  -26.887  1.00 6.50  ? 15   GLN A CB  1 
ATOM   99    C  CG  . GLN A  1 15  ? 0.398  22.636  -27.345  1.00 9.96  ? 15   GLN A CG  1 
ATOM   100   C  CD  . GLN A  1 15  ? -0.756 22.585  -26.321  1.00 11.71 ? 15   GLN A CD  1 
ATOM   101   O  OE1 . GLN A  1 15  ? -1.867 22.172  -26.631  1.00 12.43 ? 15   GLN A OE1 1 
ATOM   102   N  NE2 . GLN A  1 15  ? -0.462 22.961  -25.096  1.00 12.22 ? 15   GLN A NE2 1 
ATOM   103   N  N   . GLY A  1 16  ? 4.712  20.985  -26.482  1.00 5.23  ? 16   GLY A N   1 
ATOM   104   C  CA  . GLY A  1 16  ? 5.572  20.005  -25.838  1.00 5.75  ? 16   GLY A CA  1 
ATOM   105   C  C   . GLY A  1 16  ? 6.502  20.665  -24.837  1.00 4.64  ? 16   GLY A C   1 
ATOM   106   O  O   . GLY A  1 16  ? 6.625  21.890  -24.800  1.00 3.38  ? 16   GLY A O   1 
ATOM   107   N  N   . ILE A  1 17  ? 7.114  19.831  -24.016  1.00 4.26  ? 17   ILE A N   1 
ATOM   108   C  CA  . ILE A  1 17  ? 8.205  20.244  -23.126  1.00 3.49  ? 17   ILE A CA  1 
ATOM   109   C  C   . ILE A  1 17  ? 9.368  19.327  -23.443  1.00 3.71  ? 17   ILE A C   1 
ATOM   110   O  O   . ILE A  1 17  ? 9.203  18.097  -23.444  1.00 3.61  ? 17   ILE A O   1 
ATOM   111   C  CB  . ILE A  1 17  ? 7.823  20.062  -21.633  1.00 4.17  ? 17   ILE A CB  1 
ATOM   112   C  CG1 . ILE A  1 17  ? 6.695  21.036  -21.241  1.00 3.68  ? 17   ILE A CG1 1 
ATOM   113   C  CG2 . ILE A  1 17  ? 9.064  20.272  -20.692  1.00 3.28  ? 17   ILE A CG2 1 
ATOM   114   C  CD1 . ILE A  1 17  ? 5.942  20.597  -19.925  1.00 6.15  ? 17   ILE A CD1 1 
ATOM   115   N  N   . ILE A  1 18  ? 10.541 19.911  -23.684  1.00 2.62  ? 18   ILE A N   1 
ATOM   116   C  CA  . ILE A  1 18  ? 11.736 19.108  -23.954  1.00 2.11  ? 18   ILE A CA  1 
ATOM   117   C  C   . ILE A  1 18  ? 12.796 19.484  -22.920  1.00 3.09  ? 18   ILE A C   1 
ATOM   118   O  O   . ILE A  1 18  ? 13.032 20.657  -22.671  1.00 3.47  ? 18   ILE A O   1 
ATOM   119   C  CB  . ILE A  1 18  ? 12.256 19.343  -25.400  1.00 2.00  ? 18   ILE A CB  1 
ATOM   120   C  CG1 . ILE A  1 18  ? 11.232 18.854  -26.469  1.00 2.47  ? 18   ILE A CG1 1 
ATOM   121   C  CG2 . ILE A  1 18  ? 13.655 18.745  -25.583  1.00 2.00  ? 18   ILE A CG2 1 
ATOM   122   C  CD1 . ILE A  1 18  ? 10.896 17.348  -26.417  1.00 2.47  ? 18   ILE A CD1 1 
ATOM   123   N  N   . ASN A  1 19  ? 13.409 18.473  -22.316  1.00 3.57  ? 19   ASN A N   1 
ATOM   124   C  CA  . ASN A  1 19  ? 14.410 18.646  -21.266  1.00 4.19  ? 19   ASN A CA  1 
ATOM   125   C  C   . ASN A  1 19  ? 15.773 18.338  -21.834  1.00 3.85  ? 19   ASN A C   1 
ATOM   126   O  O   . ASN A  1 19  ? 15.888 17.504  -22.753  1.00 3.68  ? 19   ASN A O   1 
ATOM   127   C  CB  . ASN A  1 19  ? 14.141 17.669  -20.130  1.00 4.59  ? 19   ASN A CB  1 
ATOM   128   C  CG  . ASN A  1 19  ? 12.759 17.844  -19.526  1.00 6.60  ? 19   ASN A CG  1 
ATOM   129   O  OD1 . ASN A  1 19  ? 12.486 18.859  -18.879  1.00 6.06  ? 19   ASN A OD1 1 
ATOM   130   N  ND2 . ASN A  1 19  ? 11.864 16.862  -19.744  1.00 6.29  ? 19   ASN A ND2 1 
ATOM   131   N  N   . PHE A  1 20  ? 16.793 18.980  -21.270  1.00 3.52  ? 20   PHE A N   1 
ATOM   132   C  CA  . PHE A  1 20  ? 18.188 18.780  -21.653  1.00 3.02  ? 20   PHE A CA  1 
ATOM   133   C  C   . PHE A  1 20  ? 19.006 18.582  -20.390  1.00 3.91  ? 20   PHE A C   1 
ATOM   134   O  O   . PHE A  1 20  ? 18.778 19.258  -19.370  1.00 4.61  ? 20   PHE A O   1 
ATOM   135   C  CB  . PHE A  1 20  ? 18.748 20.001  -22.410  1.00 3.07  ? 20   PHE A CB  1 
ATOM   136   C  CG  . PHE A  1 20  ? 18.015 20.346  -23.683  1.00 2.00  ? 20   PHE A CG  1 
ATOM   137   C  CD1 . PHE A  1 20  ? 18.503 19.942  -24.910  1.00 3.56  ? 20   PHE A CD1 1 
ATOM   138   C  CD2 . PHE A  1 20  ? 16.896 21.173  -23.648  1.00 2.67  ? 20   PHE A CD2 1 
ATOM   139   C  CE1 . PHE A  1 20  ? 17.844 20.284  -26.098  1.00 2.00  ? 20   PHE A CE1 1 
ATOM   140   C  CE2 . PHE A  1 20  ? 16.234 21.530  -24.829  1.00 4.05  ? 20   PHE A CE2 1 
ATOM   141   C  CZ  . PHE A  1 20  ? 16.714 21.076  -26.048  1.00 2.00  ? 20   PHE A CZ  1 
ATOM   142   N  N   . GLU A  1 21  ? 19.965 17.656  -20.430  1.00 4.24  ? 21   GLU A N   1 
ATOM   143   C  CA  . GLU A  1 21  ? 20.830 17.481  -19.279  1.00 5.70  ? 21   GLU A CA  1 
ATOM   144   C  C   . GLU A  1 21  ? 22.220 17.069  -19.753  1.00 5.56  ? 21   GLU A C   1 
ATOM   145   O  O   . GLU A  1 21  ? 22.343 16.259  -20.665  1.00 5.10  ? 21   GLU A O   1 
ATOM   146   C  CB  . GLU A  1 21  ? 20.255 16.438  -18.286  1.00 6.19  ? 21   GLU A CB  1 
ATOM   147   C  CG  . GLU A  1 21  ? 21.258 16.129  -17.156  1.00 10.87 ? 21   GLU A CG  1 
ATOM   148   C  CD  . GLU A  1 21  ? 20.653 15.510  -15.908  1.00 18.66 ? 21   GLU A CD  1 
ATOM   149   O  OE1 . GLU A  1 21  ? 21.385 15.453  -14.890  1.00 21.90 ? 21   GLU A OE1 1 
ATOM   150   O  OE2 . GLU A  1 21  ? 19.466 15.091  -15.930  1.00 21.28 ? 21   GLU A OE2 1 
ATOM   151   N  N   . GLN A  1 22  ? 23.245 17.664  -19.153  1.00 5.89  ? 22   GLN A N   1 
ATOM   152   C  CA  . GLN A  1 22  ? 24.623 17.413  -19.544  1.00 7.22  ? 22   GLN A CA  1 
ATOM   153   C  C   . GLN A  1 22  ? 25.435 17.246  -18.256  1.00 8.62  ? 22   GLN A C   1 
ATOM   154   O  O   . GLN A  1 22  ? 25.631 18.195  -17.507  1.00 9.02  ? 22   GLN A O   1 
ATOM   155   C  CB  . GLN A  1 22  ? 25.154 18.591  -20.383  1.00 7.06  ? 22   GLN A CB  1 
ATOM   156   C  CG  . GLN A  1 22  ? 26.494 18.291  -21.073  1.00 5.92  ? 22   GLN A CG  1 
ATOM   157   C  CD  . GLN A  1 22  ? 26.948 19.398  -21.993  1.00 7.54  ? 22   GLN A CD  1 
ATOM   158   O  OE1 . GLN A  1 22  ? 26.579 20.556  -21.822  1.00 4.04  ? 22   GLN A OE1 1 
ATOM   159   N  NE2 . GLN A  1 22  ? 27.784 19.048  -22.964  1.00 6.53  ? 22   GLN A NE2 1 
ATOM   160   N  N   . LYS A  1 23  ? 25.889 16.034  -17.992  1.00 10.77 ? 23   LYS A N   1 
ATOM   161   C  CA  . LYS A  1 23  ? 26.645 15.751  -16.761  1.00 12.59 ? 23   LYS A CA  1 
ATOM   162   C  C   . LYS A  1 23  ? 28.007 16.417  -16.724  1.00 12.53 ? 23   LYS A C   1 
ATOM   163   O  O   . LYS A  1 23  ? 28.413 16.921  -15.677  1.00 12.92 ? 23   LYS A O   1 
ATOM   164   C  CB  . LYS A  1 23  ? 26.782 14.250  -16.546  1.00 12.94 ? 23   LYS A CB  1 
ATOM   165   C  CG  . LYS A  1 23  ? 25.433 13.584  -16.252  1.00 18.11 ? 23   LYS A CG  1 
ATOM   166   C  CD  . LYS A  1 23  ? 25.545 12.094  -15.984  1.00 23.40 ? 23   LYS A CD  1 
ATOM   167   C  CE  . LYS A  1 23  ? 24.152 11.493  -15.791  1.00 25.93 ? 23   LYS A CE  1 
ATOM   168   N  NZ  . LYS A  1 23  ? 23.303 12.341  -14.899  1.00 28.71 ? 23   LYS A NZ  1 
ATOM   169   N  N   . GLU A  1 24  ? 28.674 16.440  -17.877  1.00 13.36 ? 24   GLU A N   1 
ATOM   170   C  CA  . GLU A  1 24  ? 30.009 17.030  -18.045  1.00 13.82 ? 24   GLU A CA  1 
ATOM   171   C  C   . GLU A  1 24  ? 30.079 17.900  -19.285  1.00 13.05 ? 24   GLU A C   1 
ATOM   172   O  O   . GLU A  1 24  ? 29.435 17.603  -20.281  1.00 11.43 ? 24   GLU A O   1 
ATOM   173   C  CB  . GLU A  1 24  ? 31.045 15.910  -18.222  1.00 14.88 ? 24   GLU A CB  1 
ATOM   174   C  CG  . GLU A  1 24  ? 31.111 14.913  -17.079  1.00 17.67 ? 24   GLU A CG  1 
ATOM   175   C  CD  . GLU A  1 24  ? 31.406 15.569  -15.740  1.00 20.83 ? 24   GLU A CD  1 
ATOM   176   O  OE1 . GLU A  1 24  ? 32.221 16.510  -15.700  1.00 23.84 ? 24   GLU A OE1 1 
ATOM   177   O  OE2 . GLU A  1 24  ? 30.828 15.138  -14.714  1.00 24.90 ? 24   GLU A OE2 1 
ATOM   178   N  N   . SER A  1 25  ? 30.922 18.934  -19.259  1.00 12.67 ? 25   SER A N   1 
ATOM   179   C  CA  . SER A  1 25  ? 30.993 19.851  -20.394  1.00 12.81 ? 25   SER A CA  1 
ATOM   180   C  C   . SER A  1 25  ? 31.614 19.214  -21.645  1.00 12.32 ? 25   SER A C   1 
ATOM   181   O  O   . SER A  1 25  ? 31.377 19.664  -22.757  1.00 13.34 ? 25   SER A O   1 
ATOM   182   C  CB  . SER A  1 25  ? 31.695 21.152  -20.004  1.00 13.50 ? 25   SER A CB  1 
ATOM   183   O  OG  . SER A  1 25  ? 33.066 20.923  -19.761  1.00 13.12 ? 25   SER A OG  1 
ATOM   184   N  N   . ASN A  1 26  ? 32.389 18.155  -21.460  1.00 11.49 ? 26   ASN A N   1 
ATOM   185   C  CA  . ASN A  1 26  ? 32.986 17.429  -22.573  1.00 11.51 ? 26   ASN A CA  1 
ATOM   186   C  C   . ASN A  1 26  ? 32.167 16.176  -22.926  1.00 11.49 ? 26   ASN A C   1 
ATOM   187   O  O   . ASN A  1 26  ? 32.663 15.248  -23.576  1.00 11.44 ? 26   ASN A O   1 
ATOM   188   C  CB  . ASN A  1 26  ? 34.434 17.034  -22.220  1.00 11.92 ? 26   ASN A CB  1 
ATOM   189   C  CG  . ASN A  1 26  ? 34.517 16.058  -21.041  1.00 13.69 ? 26   ASN A CG  1 
ATOM   190   O  OD1 . ASN A  1 26  ? 33.550 15.879  -20.288  1.00 15.01 ? 26   ASN A OD1 1 
ATOM   191   N  ND2 . ASN A  1 26  ? 35.688 15.439  -20.862  1.00 11.41 ? 26   ASN A ND2 1 
ATOM   192   N  N   . GLY A  1 27  ? 30.911 16.137  -22.493  1.00 10.67 ? 27   GLY A N   1 
ATOM   193   C  CA  . GLY A  1 27  ? 30.143 14.913  -22.669  1.00 9.76  ? 27   GLY A CA  1 
ATOM   194   C  C   . GLY A  1 27  ? 28.821 15.151  -23.369  1.00 9.08  ? 27   GLY A C   1 
ATOM   195   O  O   . GLY A  1 27  ? 28.442 16.301  -23.614  1.00 8.70  ? 27   GLY A O   1 
ATOM   196   N  N   . PRO A  1 28  ? 28.081 14.064  -23.644  1.00 8.98  ? 28   PRO A N   1 
ATOM   197   C  CA  . PRO A  1 28  ? 26.858 14.192  -24.447  1.00 8.25  ? 28   PRO A CA  1 
ATOM   198   C  C   . PRO A  1 28  ? 25.732 14.946  -23.692  1.00 6.94  ? 28   PRO A C   1 
ATOM   199   O  O   . PRO A  1 28  ? 25.731 14.979  -22.456  1.00 7.68  ? 28   PRO A O   1 
ATOM   200   C  CB  . PRO A  1 28  ? 26.436 12.741  -24.702  1.00 8.02  ? 28   PRO A CB  1 
ATOM   201   C  CG  . PRO A  1 28  ? 27.351 11.854  -23.923  1.00 10.18 ? 28   PRO A CG  1 
ATOM   202   C  CD  . PRO A  1 28  ? 28.262 12.712  -23.084  1.00 9.76  ? 28   PRO A CD  1 
ATOM   203   N  N   . VAL A  1 29  ? 24.786 15.501  -24.446  1.00 5.25  ? 29   VAL A N   1 
ATOM   204   C  CA  . VAL A  1 29  ? 23.552 16.092  -23.887  1.00 4.98  ? 29   VAL A CA  1 
ATOM   205   C  C   . VAL A  1 29  ? 22.422 15.079  -24.095  1.00 4.65  ? 29   VAL A C   1 
ATOM   206   O  O   . VAL A  1 29  ? 22.220 14.631  -25.222  1.00 6.24  ? 29   VAL A O   1 
ATOM   207   C  CB  . VAL A  1 29  ? 23.205 17.408  -24.624  1.00 4.22  ? 29   VAL A CB  1 
ATOM   208   C  CG1 . VAL A  1 29  ? 21.894 18.032  -24.112  1.00 4.12  ? 29   VAL A CG1 1 
ATOM   209   C  CG2 . VAL A  1 29  ? 24.346 18.425  -24.432  1.00 3.47  ? 29   VAL A CG2 1 
ATOM   210   N  N   . LYS A  1 30  ? 21.725 14.715  -23.030  1.00 5.97  ? 30   LYS A N   1 
ATOM   211   C  CA  . LYS A  1 30  ? 20.481 13.933  -23.132  1.00 6.52  ? 30   LYS A CA  1 
ATOM   212   C  C   . LYS A  1 30  ? 19.290 14.866  -23.352  1.00 5.52  ? 30   LYS A C   1 
ATOM   213   O  O   . LYS A  1 30  ? 19.166 15.872  -22.669  1.00 5.61  ? 30   LYS A O   1 
ATOM   214   C  CB  . LYS A  1 30  ? 20.274 13.105  -21.873  1.00 6.89  ? 30   LYS A CB  1 
ATOM   215   C  CG  . LYS A  1 30  ? 21.281 11.943  -21.828  1.00 11.31 ? 30   LYS A CG  1 
ATOM   216   C  CD  . LYS A  1 30  ? 21.244 11.192  -20.536  1.00 14.80 ? 30   LYS A CD  1 
ATOM   217   C  CE  . LYS A  1 30  ? 22.101 9.925   -20.625  1.00 16.95 ? 30   LYS A CE  1 
ATOM   218   N  NZ  . LYS A  1 30  ? 22.254 9.323   -19.269  1.00 18.74 ? 30   LYS A NZ  1 
ATOM   219   N  N   . VAL A  1 31  ? 18.445 14.529  -24.325  1.00 5.91  ? 31   VAL A N   1 
ATOM   220   C  CA  . VAL A  1 31  ? 17.319 15.361  -24.744  1.00 5.52  ? 31   VAL A CA  1 
ATOM   221   C  C   . VAL A  1 31  ? 16.066 14.489  -24.699  1.00 5.99  ? 31   VAL A C   1 
ATOM   222   O  O   . VAL A  1 31  ? 15.998 13.462  -25.381  1.00 6.55  ? 31   VAL A O   1 
ATOM   223   C  CB  . VAL A  1 31  ? 17.498 15.875  -26.183  1.00 5.56  ? 31   VAL A CB  1 
ATOM   224   C  CG1 . VAL A  1 31  ? 16.342 16.821  -26.568  1.00 4.34  ? 31   VAL A CG1 1 
ATOM   225   C  CG2 . VAL A  1 31  ? 18.880 16.546  -26.398  1.00 5.54  ? 31   VAL A CG2 1 
ATOM   226   N  N   . TRP A  1 32  ? 15.109 14.853  -23.854  1.00 5.39  ? 32   TRP A N   1 
ATOM   227   C  CA  . TRP A  1 32  ? 13.941 14.004  -23.666  1.00 5.86  ? 32   TRP A CA  1 
ATOM   228   C  C   . TRP A  1 32  ? 12.732 14.824  -23.268  1.00 6.06  ? 32   TRP A C   1 
ATOM   229   O  O   . TRP A  1 32  ? 12.855 15.895  -22.680  1.00 5.53  ? 32   TRP A O   1 
ATOM   230   C  CB  . TRP A  1 32  ? 14.198 12.881  -22.647  1.00 5.74  ? 32   TRP A CB  1 
ATOM   231   C  CG  . TRP A  1 32  ? 14.104 13.326  -21.200  1.00 7.15  ? 32   TRP A CG  1 
ATOM   232   C  CD1 . TRP A  1 32  ? 13.029 13.186  -20.380  1.00 8.38  ? 32   TRP A CD1 1 
ATOM   233   C  CD2 . TRP A  1 32  ? 15.102 14.014  -20.438  1.00 7.19  ? 32   TRP A CD2 1 
ATOM   234   N  NE1 . TRP A  1 32  ? 13.294 13.731  -19.162  1.00 10.36 ? 32   TRP A NE1 1 
ATOM   235   C  CE2 . TRP A  1 32  ? 14.562 14.240  -19.162  1.00 8.33  ? 32   TRP A CE2 1 
ATOM   236   C  CE3 . TRP A  1 32  ? 16.402 14.481  -20.721  1.00 9.15  ? 32   TRP A CE3 1 
ATOM   237   C  CZ2 . TRP A  1 32  ? 15.266 14.897  -18.148  1.00 10.45 ? 32   TRP A CZ2 1 
ATOM   238   C  CZ3 . TRP A  1 32  ? 17.113 15.113  -19.714  1.00 9.86  ? 32   TRP A CZ3 1 
ATOM   239   C  CH2 . TRP A  1 32  ? 16.537 15.322  -18.438  1.00 11.31 ? 32   TRP A CH2 1 
ATOM   240   N  N   . GLY A  1 33  ? 11.564 14.297  -23.590  1.00 6.86  ? 33   GLY A N   1 
ATOM   241   C  CA  . GLY A  1 33  ? 10.309 14.968  -23.295  1.00 6.93  ? 33   GLY A CA  1 
ATOM   242   C  C   . GLY A  1 33  ? 9.234  14.385  -24.185  1.00 7.79  ? 33   GLY A C   1 
ATOM   243   O  O   . GLY A  1 33  ? 9.419  13.345  -24.818  1.00 7.70  ? 33   GLY A O   1 
ATOM   244   N  N   . SER A  1 34  ? 8.115  15.080  -24.256  1.00 8.20  ? 34   SER A N   1 
ATOM   245   C  CA  . SER A  1 34  ? 6.989  14.630  -25.028  1.00 7.86  ? 34   SER A CA  1 
ATOM   246   C  C   . SER A  1 34  ? 6.430  15.815  -25.806  1.00 7.45  ? 34   SER A C   1 
ATOM   247   O  O   . SER A  1 34  ? 6.304  16.897  -25.252  1.00 8.89  ? 34   SER A O   1 
ATOM   248   C  CB  . SER A  1 34  ? 5.942  14.074  -24.068  1.00 8.24  ? 34   SER A CB  1 
ATOM   249   O  OG  . SER A  1 34  ? 4.872  13.537  -24.816  1.00 11.14 ? 34   SER A OG  1 
ATOM   250   N  N   . ILE A  1 35  ? 6.120  15.624  -27.083  1.00 6.04  ? 35   ILE A N   1 
ATOM   251   C  CA  . ILE A  1 35  ? 5.474  16.632  -27.910  1.00 5.05  ? 35   ILE A CA  1 
ATOM   252   C  C   . ILE A  1 35  ? 4.170  16.003  -28.441  1.00 5.65  ? 35   ILE A C   1 
ATOM   253   O  O   . ILE A  1 35  ? 4.187  14.874  -28.977  1.00 5.80  ? 35   ILE A O   1 
ATOM   254   C  CB  . ILE A  1 35  ? 6.348  17.040  -29.109  1.00 4.52  ? 35   ILE A CB  1 
ATOM   255   C  CG1 . ILE A  1 35  ? 7.793  17.386  -28.676  1.00 3.35  ? 35   ILE A CG1 1 
ATOM   256   C  CG2 . ILE A  1 35  ? 5.686  18.160  -29.902  1.00 4.25  ? 35   ILE A CG2 1 
ATOM   257   C  CD1 . ILE A  1 35  ? 8.758  17.541  -29.878  1.00 6.52  ? 35   ILE A CD1 1 
ATOM   258   N  N   . LYS A  1 36  ? 3.051  16.701  -28.250  1.00 4.69  ? 36   LYS A N   1 
ATOM   259   C  CA  . LYS A  1 36  ? 1.755  16.243  -28.739  1.00 5.17  ? 36   LYS A CA  1 
ATOM   260   C  C   . LYS A  1 36  ? 1.221  17.151  -29.837  1.00 4.56  ? 36   LYS A C   1 
ATOM   261   O  O   . LYS A  1 36  ? 1.817  18.215  -30.125  1.00 3.52  ? 36   LYS A O   1 
ATOM   262   C  CB  . LYS A  1 36  ? 0.736  16.120  -27.588  1.00 4.51  ? 36   LYS A CB  1 
ATOM   263   C  CG  . LYS A  1 36  ? 0.473  17.417  -26.841  1.00 7.73  ? 36   LYS A CG  1 
ATOM   264   C  CD  . LYS A  1 36  ? -0.344 17.186  -25.571  1.00 10.17 ? 36   LYS A CD  1 
ATOM   265   C  CE  . LYS A  1 36  ? -0.955 18.503  -25.098  1.00 11.83 ? 36   LYS A CE  1 
ATOM   266   N  NZ  . LYS A  1 36  ? -1.723 18.251  -23.863  1.00 11.31 ? 36   LYS A NZ  1 
ATOM   267   N  N   . GLY A  1 37  ? 0.131  16.712  -30.489  1.00 3.12  ? 37   GLY A N   1 
ATOM   268   C  CA  . GLY A  1 37  ? -0.483 17.501  -31.559  1.00 3.35  ? 37   GLY A CA  1 
ATOM   269   C  C   . GLY A  1 37  ? 0.147  17.397  -32.930  1.00 3.05  ? 37   GLY A C   1 
ATOM   270   O  O   . GLY A  1 37  ? -0.192 18.147  -33.849  1.00 3.19  ? 37   GLY A O   1 
ATOM   271   N  N   . LEU A  1 38  ? 1.055  16.429  -33.081  1.00 4.16  ? 38   LEU A N   1 
ATOM   272   C  CA  . LEU A  1 38  ? 1.735  16.210  -34.344  1.00 3.87  ? 38   LEU A CA  1 
ATOM   273   C  C   . LEU A  1 38  ? 0.966  15.206  -35.240  1.00 4.81  ? 38   LEU A C   1 
ATOM   274   O  O   . LEU A  1 38  ? 0.219  14.378  -34.717  1.00 4.97  ? 38   LEU A O   1 
ATOM   275   C  CB  . LEU A  1 38  ? 3.114  15.637  -34.046  1.00 4.22  ? 38   LEU A CB  1 
ATOM   276   C  CG  . LEU A  1 38  ? 4.126  16.557  -33.356  1.00 2.90  ? 38   LEU A CG  1 
ATOM   277   C  CD1 . LEU A  1 38  ? 5.284  15.742  -32.755  1.00 4.05  ? 38   LEU A CD1 1 
ATOM   278   C  CD2 . LEU A  1 38  ? 4.639  17.530  -34.384  1.00 4.41  ? 38   LEU A CD2 1 
ATOM   279   N  N   . THR A  1 39  ? 1.157  15.296  -36.559  1.00 4.44  ? 39   THR A N   1 
ATOM   280   C  CA  . THR A  1 39  ? 0.737  14.218  -37.491  1.00 5.39  ? 39   THR A CA  1 
ATOM   281   C  C   . THR A  1 39  ? 1.628  13.015  -37.239  1.00 5.42  ? 39   THR A C   1 
ATOM   282   O  O   . THR A  1 39  ? 2.803  13.156  -36.841  1.00 4.62  ? 39   THR A O   1 
ATOM   283   C  CB  . THR A  1 39  ? 0.847  14.611  -39.004  1.00 6.17  ? 39   THR A CB  1 
ATOM   284   O  OG1 . THR A  1 39  ? 2.181  15.057  -39.331  1.00 3.60  ? 39   THR A OG1 1 
ATOM   285   C  CG2 . THR A  1 39  ? -0.161 15.696  -39.379  1.00 6.28  ? 39   THR A CG2 1 
ATOM   286   N  N   . GLU A  1 40  ? 1.092  11.829  -37.503  1.00 5.64  ? 40   GLU A N   1 
ATOM   287   C  CA  . GLU A  1 40  ? 1.859  10.618  -37.292  1.00 6.00  ? 40   GLU A CA  1 
ATOM   288   C  C   . GLU A  1 40  ? 3.065  10.593  -38.228  1.00 5.31  ? 40   GLU A C   1 
ATOM   289   O  O   . GLU A  1 40  ? 2.965  10.997  -39.381  1.00 5.86  ? 40   GLU A O   1 
ATOM   290   C  CB  . GLU A  1 40  ? 0.986  9.374   -37.497  1.00 7.46  ? 40   GLU A CB  1 
ATOM   291   C  CG  . GLU A  1 40  ? 1.721  8.050   -37.186  1.00 7.33  ? 40   GLU A CG  1 
ATOM   292   C  CD  . GLU A  1 40  ? 0.845  6.799   -37.413  1.00 13.75 ? 40   GLU A CD  1 
ATOM   293   O  OE1 . GLU A  1 40  ? 1.332  5.679   -37.131  1.00 15.19 ? 40   GLU A OE1 1 
ATOM   294   O  OE2 . GLU A  1 40  ? -0.312 6.944   -37.854  1.00 14.30 ? 40   GLU A OE2 1 
ATOM   295   N  N   . GLY A  1 41  ? 4.201  10.127  -37.716  1.00 5.43  ? 41   GLY A N   1 
ATOM   296   C  CA  . GLY A  1 41  ? 5.397  9.953   -38.545  1.00 5.78  ? 41   GLY A CA  1 
ATOM   297   C  C   . GLY A  1 41  ? 6.513  10.925  -38.183  1.00 6.41  ? 41   GLY A C   1 
ATOM   298   O  O   . GLY A  1 41  ? 6.562  11.438  -37.060  1.00 6.18  ? 41   GLY A O   1 
ATOM   299   N  N   . LEU A  1 42  ? 7.391  11.206  -39.146  1.00 5.59  ? 42   LEU A N   1 
ATOM   300   C  CA  . LEU A  1 42  ? 8.628  11.894  -38.860  1.00 5.76  ? 42   LEU A CA  1 
ATOM   301   C  C   . LEU A  1 42  ? 8.500  13.404  -38.953  1.00 5.28  ? 42   LEU A C   1 
ATOM   302   O  O   . LEU A  1 42  ? 7.866  13.922  -39.866  1.00 5.40  ? 42   LEU A O   1 
ATOM   303   C  CB  . LEU A  1 42  ? 9.731  11.440  -39.833  1.00 6.19  ? 42   LEU A CB  1 
ATOM   304   C  CG  . LEU A  1 42  ? 10.335 10.038  -39.717  1.00 7.67  ? 42   LEU A CG  1 
ATOM   305   C  CD1 . LEU A  1 42  ? 10.996 9.650   -41.076  1.00 7.82  ? 42   LEU A CD1 1 
ATOM   306   C  CD2 . LEU A  1 42  ? 11.329 9.905   -38.589  1.00 7.97  ? 42   LEU A CD2 1 
ATOM   307   N  N   . HIS A  1 43  ? 9.206  14.098  -38.058  1.00 4.62  ? 43   HIS A N   1 
ATOM   308   C  CA  . HIS A  1 43  ? 9.192  15.563  -38.015  1.00 4.38  ? 43   HIS A CA  1 
ATOM   309   C  C   . HIS A  1 43  ? 10.592 16.074  -37.744  1.00 3.32  ? 43   HIS A C   1 
ATOM   310   O  O   . HIS A  1 43  ? 11.153 15.719  -36.731  1.00 3.01  ? 43   HIS A O   1 
ATOM   311   C  CB  . HIS A  1 43  ? 8.231  16.024  -36.903  1.00 4.94  ? 43   HIS A CB  1 
ATOM   312   C  CG  . HIS A  1 43  ? 6.806  15.726  -37.223  1.00 3.47  ? 43   HIS A CG  1 
ATOM   313   N  ND1 . HIS A  1 43  ? 6.028  16.584  -37.963  1.00 4.85  ? 43   HIS A ND1 1 
ATOM   314   C  CD2 . HIS A  1 43  ? 6.039  14.645  -36.961  1.00 3.10  ? 43   HIS A CD2 1 
ATOM   315   C  CE1 . HIS A  1 43  ? 4.832  16.052  -38.135  1.00 4.00  ? 43   HIS A CE1 1 
ATOM   316   N  NE2 . HIS A  1 43  ? 4.819  14.865  -37.555  1.00 4.19  ? 43   HIS A NE2 1 
ATOM   317   N  N   . GLY A  1 44  ? 11.132 16.927  -38.622  1.00 4.23  ? 44   GLY A N   1 
ATOM   318   C  CA  . GLY A  1 44  ? 12.454 17.570  -38.372  1.00 3.53  ? 44   GLY A CA  1 
ATOM   319   C  C   . GLY A  1 44  ? 12.563 18.233  -36.990  1.00 3.59  ? 44   GLY A C   1 
ATOM   320   O  O   . GLY A  1 44  ? 11.566 18.770  -36.461  1.00 2.69  ? 44   GLY A O   1 
ATOM   321   N  N   . PHE A  1 45  ? 13.754 18.235  -36.395  1.00 3.11  ? 45   PHE A N   1 
ATOM   322   C  CA  . PHE A  1 45  ? 13.880 18.660  -34.975  1.00 2.96  ? 45   PHE A CA  1 
ATOM   323   C  C   . PHE A  1 45  ? 15.247 19.337  -34.854  1.00 3.55  ? 45   PHE A C   1 
ATOM   324   O  O   . PHE A  1 45  ? 16.258 18.662  -34.892  1.00 3.24  ? 45   PHE A O   1 
ATOM   325   C  CB  . PHE A  1 45  ? 13.752 17.399  -34.087  1.00 3.04  ? 45   PHE A CB  1 
ATOM   326   C  CG  . PHE A  1 45  ? 13.658 17.653  -32.593  1.00 2.98  ? 45   PHE A CG  1 
ATOM   327   C  CD1 . PHE A  1 45  ? 12.597 18.378  -32.043  1.00 4.82  ? 45   PHE A CD1 1 
ATOM   328   C  CD2 . PHE A  1 45  ? 14.594 17.106  -31.733  1.00 4.03  ? 45   PHE A CD2 1 
ATOM   329   C  CE1 . PHE A  1 45  ? 12.481 18.558  -30.684  1.00 4.38  ? 45   PHE A CE1 1 
ATOM   330   C  CE2 . PHE A  1 45  ? 14.489 17.271  -30.354  1.00 5.04  ? 45   PHE A CE2 1 
ATOM   331   C  CZ  . PHE A  1 45  ? 13.418 18.002  -29.822  1.00 5.12  ? 45   PHE A CZ  1 
ATOM   332   N  N   . HIS A  1 46  ? 15.300 20.670  -34.807  1.00 2.82  ? 46   HIS A N   1 
ATOM   333   C  CA  . HIS A  1 46  ? 16.612 21.363  -34.789  1.00 2.96  ? 46   HIS A CA  1 
ATOM   334   C  C   . HIS A  1 46  ? 16.675 22.470  -33.780  1.00 3.92  ? 46   HIS A C   1 
ATOM   335   O  O   . HIS A  1 46  ? 15.651 22.990  -33.365  1.00 3.14  ? 46   HIS A O   1 
ATOM   336   C  CB  . HIS A  1 46  ? 16.970 21.980  -36.142  1.00 2.18  ? 46   HIS A CB  1 
ATOM   337   C  CG  . HIS A  1 46  ? 16.453 21.205  -37.303  1.00 3.48  ? 46   HIS A CG  1 
ATOM   338   N  ND1 . HIS A  1 46  ? 15.364 21.614  -38.032  1.00 2.00  ? 46   HIS A ND1 1 
ATOM   339   C  CD2 . HIS A  1 46  ? 16.829 20.006  -37.814  1.00 2.00  ? 46   HIS A CD2 1 
ATOM   340   C  CE1 . HIS A  1 46  ? 15.126 20.734  -38.994  1.00 3.24  ? 46   HIS A CE1 1 
ATOM   341   N  NE2 . HIS A  1 46  ? 15.970 19.722  -38.849  1.00 3.06  ? 46   HIS A NE2 1 
ATOM   342   N  N   . VAL A  1 47  ? 17.908 22.855  -33.449  1.00 4.46  ? 47   VAL A N   1 
ATOM   343   C  CA  . VAL A  1 47  ? 18.147 24.080  -32.728  1.00 4.22  ? 47   VAL A CA  1 
ATOM   344   C  C   . VAL A  1 47  ? 18.474 25.138  -33.778  1.00 4.21  ? 47   VAL A C   1 
ATOM   345   O  O   . VAL A  1 47  ? 19.411 24.961  -34.575  1.00 4.55  ? 47   VAL A O   1 
ATOM   346   C  CB  . VAL A  1 47  ? 19.334 23.939  -31.739  1.00 3.69  ? 47   VAL A CB  1 
ATOM   347   C  CG1 . VAL A  1 47  ? 19.605 25.262  -31.032  1.00 4.14  ? 47   VAL A CG1 1 
ATOM   348   C  CG2 . VAL A  1 47  ? 19.049 22.835  -30.698  1.00 4.77  ? 47   VAL A CG2 1 
ATOM   349   N  N   . HIS A  1 48  ? 17.683 26.209  -33.789  1.00 2.81  ? 48   HIS A N   1 
ATOM   350   C  CA  . HIS A  1 48  ? 17.898 27.344  -34.647  1.00 2.76  ? 48   HIS A CA  1 
ATOM   351   C  C   . HIS A  1 48  ? 18.674 28.441  -33.920  1.00 2.73  ? 48   HIS A C   1 
ATOM   352   O  O   . HIS A  1 48  ? 18.744 28.444  -32.696  1.00 2.37  ? 48   HIS A O   1 
ATOM   353   C  CB  . HIS A  1 48  ? 16.577 27.878  -35.194  1.00 2.99  ? 48   HIS A CB  1 
ATOM   354   C  CG  . HIS A  1 48  ? 15.942 26.967  -36.197  1.00 2.00  ? 48   HIS A CG  1 
ATOM   355   N  ND1 . HIS A  1 48  ? 15.687 27.358  -37.491  1.00 2.00  ? 48   HIS A ND1 1 
ATOM   356   C  CD2 . HIS A  1 48  ? 15.521 25.684  -36.098  1.00 2.83  ? 48   HIS A CD2 1 
ATOM   357   C  CE1 . HIS A  1 48  ? 15.117 26.365  -38.148  1.00 3.92  ? 48   HIS A CE1 1 
ATOM   358   N  NE2 . HIS A  1 48  ? 14.985 25.344  -37.320  1.00 3.85  ? 48   HIS A NE2 1 
ATOM   359   N  N   . GLU A  1 49  ? 19.258 29.349  -34.703  1.00 3.33  ? 49   GLU A N   1 
ATOM   360   C  CA  . GLU A  1 49  ? 20.330 30.232  -34.246  1.00 4.36  ? 49   GLU A CA  1 
ATOM   361   C  C   . GLU A  1 49  ? 19.868 31.228  -33.183  1.00 4.17  ? 49   GLU A C   1 
ATOM   362   O  O   . GLU A  1 49  ? 20.560 31.456  -32.165  1.00 5.13  ? 49   GLU A O   1 
ATOM   363   C  CB  . GLU A  1 49  ? 20.958 30.968  -35.437  1.00 4.42  ? 49   GLU A CB  1 
ATOM   364   C  CG  . GLU A  1 49  ? 22.237 31.761  -35.088  1.00 7.02  ? 49   GLU A CG  1 
ATOM   365   C  CD  . GLU A  1 49  ? 22.792 32.559  -36.291  1.00 9.95  ? 49   GLU A CD  1 
ATOM   366   O  OE1 . GLU A  1 49  ? 23.770 33.313  -36.103  1.00 10.05 ? 49   GLU A OE1 1 
ATOM   367   O  OE2 . GLU A  1 49  ? 22.218 32.472  -37.391  1.00 7.64  ? 49   GLU A OE2 1 
ATOM   368   N  N   . PHE A  1 50  ? 18.714 31.837  -33.406  1.00 3.23  ? 50   PHE A N   1 
ATOM   369   C  CA  . PHE A  1 50  ? 18.297 32.927  -32.542  1.00 3.83  ? 50   PHE A CA  1 
ATOM   370   C  C   . PHE A  1 50  ? 17.151 32.544  -31.609  1.00 3.36  ? 50   PHE A C   1 
ATOM   371   O  O   . PHE A  1 50  ? 16.214 31.876  -32.031  1.00 2.28  ? 50   PHE A O   1 
ATOM   372   C  CB  . PHE A  1 50  ? 17.919 34.132  -33.395  1.00 5.04  ? 50   PHE A CB  1 
ATOM   373   C  CG  . PHE A  1 50  ? 19.012 34.560  -34.341  1.00 6.48  ? 50   PHE A CG  1 
ATOM   374   C  CD1 . PHE A  1 50  ? 20.279 34.883  -33.862  1.00 9.30  ? 50   PHE A CD1 1 
ATOM   375   C  CD2 . PHE A  1 50  ? 18.768 34.618  -35.720  1.00 9.38  ? 50   PHE A CD2 1 
ATOM   376   C  CE1 . PHE A  1 50  ? 21.305 35.246  -34.754  1.00 10.04 ? 50   PHE A CE1 1 
ATOM   377   C  CE2 . PHE A  1 50  ? 19.779 34.984  -36.609  1.00 11.46 ? 50   PHE A CE2 1 
ATOM   378   C  CZ  . PHE A  1 50  ? 21.037 35.292  -36.121  1.00 11.38 ? 50   PHE A CZ  1 
ATOM   379   N  N   . GLY A  1 51  ? 17.239 32.994  -30.364  1.00 2.56  ? 51   GLY A N   1 
ATOM   380   C  CA  . GLY A  1 51  ? 16.185 32.828  -29.358  1.00 2.92  ? 51   GLY A CA  1 
ATOM   381   C  C   . GLY A  1 51  ? 15.192 33.980  -29.473  1.00 3.41  ? 51   GLY A C   1 
ATOM   382   O  O   . GLY A  1 51  ? 14.818 34.603  -28.492  1.00 2.86  ? 51   GLY A O   1 
ATOM   383   N  N   . ASP A  1 52  ? 14.780 34.263  -30.707  1.00 3.79  ? 52   ASP A N   1 
ATOM   384   C  CA  . ASP A  1 52  ? 13.940 35.376  -31.017  1.00 5.24  ? 52   ASP A CA  1 
ATOM   385   C  C   . ASP A  1 52  ? 12.629 34.823  -31.539  1.00 6.49  ? 52   ASP A C   1 
ATOM   386   O  O   . ASP A  1 52  ? 12.602 34.180  -32.598  1.00 7.03  ? 52   ASP A O   1 
ATOM   387   C  CB  . ASP A  1 52  ? 14.649 36.249  -32.063  1.00 5.01  ? 52   ASP A CB  1 
ATOM   388   C  CG  . ASP A  1 52  ? 13.882 37.511  -32.409  1.00 6.10  ? 52   ASP A CG  1 
ATOM   389   O  OD1 . ASP A  1 52  ? 14.530 38.414  -32.937  1.00 9.06  ? 52   ASP A OD1 1 
ATOM   390   O  OD2 . ASP A  1 52  ? 12.652 37.594  -32.206  1.00 3.51  ? 52   ASP A OD2 1 
ATOM   391   N  N   . ASN A  1 53  ? 11.576 35.014  -30.744  1.00 6.77  ? 53   ASN A N   1 
ATOM   392   C  CA  . ASN A  1 53  ? 10.218 34.639  -31.112  1.00 7.69  ? 53   ASN A CA  1 
ATOM   393   C  C   . ASN A  1 53  ? 9.307  35.857  -31.403  1.00 6.39  ? 53   ASN A C   1 
ATOM   394   O  O   . ASN A  1 53  ? 8.088  35.752  -31.318  1.00 6.05  ? 53   ASN A O   1 
ATOM   395   C  CB  . ASN A  1 53  ? 9.602  33.786  -29.992  1.00 8.48  ? 53   ASN A CB  1 
ATOM   396   C  CG  . ASN A  1 53  ? 8.336  33.045  -30.429  1.00 13.80 ? 53   ASN A CG  1 
ATOM   397   O  OD1 . ASN A  1 53  ? 7.226  33.367  -29.979  1.00 21.63 ? 53   ASN A OD1 1 
ATOM   398   N  ND2 . ASN A  1 53  ? 8.497  32.032  -31.270  1.00 17.33 ? 53   ASN A ND2 1 
ATOM   399   N  N   . THR A  1 54  ? 9.881  37.006  -31.749  1.00 6.28  ? 54   THR A N   1 
ATOM   400   C  CA  . THR A  1 54  ? 9.052  38.197  -31.951  1.00 6.76  ? 54   THR A CA  1 
ATOM   401   C  C   . THR A  1 54  ? 8.099  38.064  -33.141  1.00 8.28  ? 54   THR A C   1 
ATOM   402   O  O   . THR A  1 54  ? 7.033  38.668  -33.144  1.00 8.83  ? 54   THR A O   1 
ATOM   403   C  CB  . THR A  1 54  ? 9.888  39.479  -32.124  1.00 6.27  ? 54   THR A CB  1 
ATOM   404   O  OG1 . THR A  1 54  ? 10.795 39.322  -33.214  1.00 6.58  ? 54   THR A OG1 1 
ATOM   405   C  CG2 . THR A  1 54  ? 10.672 39.777  -30.841  1.00 5.01  ? 54   THR A CG2 1 
ATOM   406   N  N   . ALA A  1 55  ? 8.499  37.286  -34.148  1.00 8.56  ? 55   ALA A N   1 
ATOM   407   C  CA  . ALA A  1 55  ? 7.640  36.996  -35.302  1.00 10.19 ? 55   ALA A CA  1 
ATOM   408   C  C   . ALA A  1 55  ? 7.296  35.511  -35.347  1.00 10.93 ? 55   ALA A C   1 
ATOM   409   O  O   . ALA A  1 55  ? 7.312  34.874  -36.424  1.00 13.07 ? 55   ALA A O   1 
ATOM   410   C  CB  . ALA A  1 55  ? 8.335  37.423  -36.605  1.00 10.06 ? 55   ALA A CB  1 
ATOM   411   N  N   . GLY A  1 56  ? 7.021  34.940  -34.181  1.00 10.32 ? 56   GLY A N   1 
ATOM   412   C  CA  . GLY A  1 56  ? 6.805  33.502  -34.073  1.00 9.76  ? 56   GLY A CA  1 
ATOM   413   C  C   . GLY A  1 56  ? 8.087  32.729  -34.329  1.00 8.80  ? 56   GLY A C   1 
ATOM   414   O  O   . GLY A  1 56  ? 9.185  33.244  -34.103  1.00 9.11  ? 56   GLY A O   1 
ATOM   415   N  N   . CYS A  1 57  ? 7.965  31.497  -34.823  1.00 6.74  ? 57   CYS A N   1 
ATOM   416   C  CA  . CYS A  1 57  ? 9.148  30.662  -35.065  1.00 5.21  ? 57   CYS A CA  1 
ATOM   417   C  C   . CYS A  1 57  ? 10.019 31.161  -36.244  1.00 6.02  ? 57   CYS A C   1 
ATOM   418   O  O   . CYS A  1 57  ? 11.212 30.833  -36.324  1.00 6.00  ? 57   CYS A O   1 
ATOM   419   C  CB  . CYS A  1 57  ? 8.716  29.208  -35.299  0.40 3.86  ? 57   CYS A CB  1 
ATOM   420   S  SG  . CYS A  1 57  ? 7.760  28.491  -33.940  0.40 2.00  ? 57   CYS A SG  1 
ATOM   421   N  N   . THR A  1 58  ? 9.446  31.983  -37.128  1.00 6.20  ? 58   THR A N   1 
ATOM   422   C  CA  . THR A  1 58  ? 10.229 32.537  -38.256  1.00 7.33  ? 58   THR A CA  1 
ATOM   423   C  C   . THR A  1 58  ? 11.455 33.338  -37.806  1.00 6.56  ? 58   THR A C   1 
ATOM   424   O  O   . THR A  1 58  ? 12.521 33.252  -38.429  1.00 5.86  ? 58   THR A O   1 
ATOM   425   C  CB  . THR A  1 58  ? 9.356  33.355  -39.249  1.00 7.84  ? 58   THR A CB  1 
ATOM   426   O  OG1 . THR A  1 58  ? 8.174  32.602  -39.556  1.00 11.38 ? 58   THR A OG1 1 
ATOM   427   C  CG2 . THR A  1 58  ? 10.115 33.626  -40.552  1.00 8.61  ? 58   THR A CG2 1 
ATOM   428   N  N   . SER A  1 59  ? 11.327 34.094  -36.720  1.00 6.41  ? 59   SER A N   1 
ATOM   429   C  CA  . SER A  1 59  ? 12.449 34.951  -36.295  1.00 6.40  ? 59   SER A CA  1 
ATOM   430   C  C   . SER A  1 59  ? 13.613 34.209  -35.622  1.00 6.06  ? 59   SER A C   1 
ATOM   431   O  O   . SER A  1 59  ? 14.639 34.816  -35.314  1.00 6.19  ? 59   SER A O   1 
ATOM   432   C  CB  . SER A  1 59  ? 11.955 36.156  -35.458  1.00 7.33  ? 59   SER A CB  1 
ATOM   433   O  OG  . SER A  1 59  ? 10.901 35.783  -34.602  1.00 7.81  ? 59   SER A OG  1 
ATOM   434   N  N   . ALA A  1 60  ? 13.490 32.884  -35.472  1.00 5.96  ? 60   ALA A N   1 
ATOM   435   C  CA  . ALA A  1 60  ? 14.577 32.060  -34.927  1.00 5.01  ? 60   ALA A CA  1 
ATOM   436   C  C   . ALA A  1 60  ? 15.746 31.926  -35.918  1.00 4.53  ? 60   ALA A C   1 
ATOM   437   O  O   . ALA A  1 60  ? 16.822 31.426  -35.568  1.00 3.86  ? 60   ALA A O   1 
ATOM   438   C  CB  . ALA A  1 60  ? 14.052 30.653  -34.545  1.00 4.52  ? 60   ALA A CB  1 
ATOM   439   N  N   . GLY A  1 61  ? 15.527 32.340  -37.158  1.00 5.20  ? 61   GLY A N   1 
ATOM   440   C  CA  . GLY A  1 61  ? 16.598 32.280  -38.164  1.00 5.89  ? 61   GLY A CA  1 
ATOM   441   C  C   . GLY A  1 61  ? 16.868 30.827  -38.585  1.00 5.41  ? 61   GLY A C   1 
ATOM   442   O  O   . GLY A  1 61  ? 16.035 29.943  -38.380  1.00 6.13  ? 61   GLY A O   1 
ATOM   443   N  N   . PRO A  1 62  ? 18.055 30.575  -39.137  1.00 5.52  ? 62   PRO A N   1 
ATOM   444   C  CA  . PRO A  1 62  ? 18.433 29.286  -39.703  1.00 4.78  ? 62   PRO A CA  1 
ATOM   445   C  C   . PRO A  1 62  ? 18.912 28.325  -38.613  1.00 4.07  ? 62   PRO A C   1 
ATOM   446   O  O   . PRO A  1 62  ? 18.951 28.693  -37.425  1.00 3.13  ? 62   PRO A O   1 
ATOM   447   C  CB  . PRO A  1 62  ? 19.571 29.661  -40.663  1.00 5.17  ? 62   PRO A CB  1 
ATOM   448   C  CG  . PRO A  1 62  ? 20.247 30.857  -39.980  1.00 6.20  ? 62   PRO A CG  1 
ATOM   449   C  CD  . PRO A  1 62  ? 19.109 31.606  -39.314  1.00 5.01  ? 62   PRO A CD  1 
ATOM   450   N  N   . HIS A  1 63  ? 19.309 27.112  -39.005  1.00 3.35  ? 63   HIS A N   1 
ATOM   451   C  CA  . HIS A  1 63  ? 19.787 26.139  -38.037  1.00 3.69  ? 63   HIS A CA  1 
ATOM   452   C  C   . HIS A  1 63  ? 21.061 26.674  -37.388  1.00 4.27  ? 63   HIS A C   1 
ATOM   453   O  O   . HIS A  1 63  ? 21.866 27.344  -38.056  1.00 4.49  ? 63   HIS A O   1 
ATOM   454   C  CB  . HIS A  1 63  ? 20.075 24.787  -38.695  1.00 3.60  ? 63   HIS A CB  1 
ATOM   455   C  CG  . HIS A  1 63  ? 18.870 24.149  -39.326  1.00 5.04  ? 63   HIS A CG  1 
ATOM   456   N  ND1 . HIS A  1 63  ? 18.946 22.975  -40.036  1.00 5.34  ? 63   HIS A ND1 1 
ATOM   457   C  CD2 . HIS A  1 63  ? 17.570 24.528  -39.379  1.00 2.00  ? 63   HIS A CD2 1 
ATOM   458   C  CE1 . HIS A  1 63  ? 17.751 22.644  -40.492  1.00 4.28  ? 63   HIS A CE1 1 
ATOM   459   N  NE2 . HIS A  1 63  ? 16.903 23.580  -40.124  1.00 3.21  ? 63   HIS A NE2 1 
ATOM   460   N  N   . PHE A  1 64  ? 21.233 26.382  -36.102  1.00 4.84  ? 64   PHE A N   1 
ATOM   461   C  CA  . PHE A  1 64  ? 22.419 26.857  -35.375  1.00 4.23  ? 64   PHE A CA  1 
ATOM   462   C  C   . PHE A  1 64  ? 23.661 26.175  -36.000  1.00 5.39  ? 64   PHE A C   1 
ATOM   463   O  O   . PHE A  1 64  ? 23.759 24.932  -36.044  1.00 4.42  ? 64   PHE A O   1 
ATOM   464   C  CB  . PHE A  1 64  ? 22.263 26.585  -33.877  1.00 4.12  ? 64   PHE A CB  1 
ATOM   465   C  CG  . PHE A  1 64  ? 23.473 26.963  -33.043  1.00 3.87  ? 64   PHE A CG  1 
ATOM   466   C  CD1 . PHE A  1 64  ? 23.929 26.100  -32.059  1.00 4.78  ? 64   PHE A CD1 1 
ATOM   467   C  CD2 . PHE A  1 64  ? 24.111 28.188  -33.221  1.00 2.70  ? 64   PHE A CD2 1 
ATOM   468   C  CE1 . PHE A  1 64  ? 25.028 26.435  -31.245  1.00 5.21  ? 64   PHE A CE1 1 
ATOM   469   C  CE2 . PHE A  1 64  ? 25.243 28.549  -32.424  1.00 2.29  ? 64   PHE A CE2 1 
ATOM   470   C  CZ  . PHE A  1 64  ? 25.689 27.667  -31.423  1.00 2.92  ? 64   PHE A CZ  1 
ATOM   471   N  N   . ASN A  1 65  ? 24.566 26.998  -36.536  1.00 5.34  ? 65   ASN A N   1 
ATOM   472   C  CA  . ASN A  1 65  ? 25.620 26.516  -37.438  1.00 6.97  ? 65   ASN A CA  1 
ATOM   473   C  C   . ASN A  1 65  ? 26.952 27.262  -37.246  1.00 7.75  ? 65   ASN A C   1 
ATOM   474   O  O   . ASN A  1 65  ? 27.483 27.847  -38.196  1.00 7.54  ? 65   ASN A O   1 
ATOM   475   C  CB  . ASN A  1 65  ? 25.139 26.599  -38.909  1.00 6.67  ? 65   ASN A CB  1 
ATOM   476   C  CG  . ASN A  1 65  ? 26.133 25.988  -39.907  1.00 7.88  ? 65   ASN A CG  1 
ATOM   477   O  OD1 . ASN A  1 65  ? 26.881 25.046  -39.592  1.00 8.82  ? 65   ASN A OD1 1 
ATOM   478   N  ND2 . ASN A  1 65  ? 26.084 26.473  -41.132  1.00 6.00  ? 65   ASN A ND2 1 
ATOM   479   N  N   . PRO A  1 66  ? 27.506 27.218  -36.031  1.00 8.22  ? 66   PRO A N   1 
ATOM   480   C  CA  . PRO A  1 66  ? 28.702 28.054  -35.828  1.00 10.17 ? 66   PRO A CA  1 
ATOM   481   C  C   . PRO A  1 66  ? 29.961 27.562  -36.551  1.00 11.87 ? 66   PRO A C   1 
ATOM   482   O  O   . PRO A  1 66  ? 30.930 28.321  -36.643  1.00 13.56 ? 66   PRO A O   1 
ATOM   483   C  CB  . PRO A  1 66  ? 28.901 28.015  -34.315  1.00 9.27  ? 66   PRO A CB  1 
ATOM   484   C  CG  . PRO A  1 66  ? 28.305 26.700  -33.899  1.00 9.26  ? 66   PRO A CG  1 
ATOM   485   C  CD  . PRO A  1 66  ? 27.084 26.561  -34.780  1.00 7.72  ? 66   PRO A CD  1 
ATOM   486   N  N   . LEU A  1 67  ? 29.948 26.321  -37.038  1.00 13.02 ? 67   LEU A N   1 
ATOM   487   C  CA  . LEU A  1 67  ? 31.080 25.753  -37.783  1.00 13.48 ? 67   LEU A CA  1 
ATOM   488   C  C   . LEU A  1 67  ? 30.927 25.856  -39.302  1.00 13.72 ? 67   LEU A C   1 
ATOM   489   O  O   . LEU A  1 67  ? 31.761 25.322  -40.056  1.00 12.46 ? 67   LEU A O   1 
ATOM   490   C  CB  . LEU A  1 67  ? 31.372 24.300  -37.335  1.00 13.84 ? 67   LEU A CB  1 
ATOM   491   C  CG  . LEU A  1 67  ? 31.676 24.018  -35.853  1.00 15.13 ? 67   LEU A CG  1 
ATOM   492   C  CD1 . LEU A  1 67  ? 32.058 22.542  -35.623  1.00 19.27 ? 67   LEU A CD1 1 
ATOM   493   C  CD2 . LEU A  1 67  ? 32.734 24.919  -35.237  1.00 19.35 ? 67   LEU A CD2 1 
ATOM   494   N  N   . SER A  1 68  ? 29.863 26.543  -39.744  1.00 14.04 ? 68   SER A N   1 
ATOM   495   C  CA  . SER A  1 68  ? 29.613 26.858  -41.167  1.00 14.84 ? 68   SER A CA  1 
ATOM   496   C  C   . SER A  1 68  ? 29.672 25.635  -42.080  1.00 14.57 ? 68   SER A C   1 
ATOM   497   O  O   . SER A  1 68  ? 30.341 25.636  -43.111  1.00 14.47 ? 68   SER A O   1 
ATOM   498   C  CB  . SER A  1 68  ? 30.579 27.949  -41.658  1.00 15.56 ? 68   SER A CB  1 
ATOM   499   O  OG  . SER A  1 68  ? 30.620 29.002  -40.724  1.00 18.27 ? 68   SER A OG  1 
ATOM   500   N  N   . ARG A  1 69  ? 28.948 24.595  -41.673  1.00 12.93 ? 69   ARG A N   1 
ATOM   501   C  CA  . ARG A  1 69  ? 28.881 23.340  -42.382  1.00 12.21 ? 69   ARG A CA  1 
ATOM   502   C  C   . ARG A  1 69  ? 27.527 23.217  -43.075  1.00 11.16 ? 69   ARG A C   1 
ATOM   503   O  O   . ARG A  1 69  ? 26.642 24.072  -42.889  1.00 11.03 ? 69   ARG A O   1 
ATOM   504   C  CB  . ARG A  1 69  ? 29.144 22.179  -41.408  1.00 11.70 ? 69   ARG A CB  1 
ATOM   505   C  CG  . ARG A  1 69  ? 30.634 22.025  -41.039  1.00 15.30 ? 69   ARG A CG  1 
ATOM   506   C  CD  . ARG A  1 69  ? 30.901 20.879  -40.059  1.00 18.34 ? 69   ARG A CD  1 
ATOM   507   N  NE  . ARG A  1 69  ? 32.319 20.882  -39.680  1.00 20.12 ? 69   ARG A NE  1 
ATOM   508   C  CZ  . ARG A  1 69  ? 32.929 19.974  -38.916  1.00 21.32 ? 69   ARG A CZ  1 
ATOM   509   N  NH1 . ARG A  1 69  ? 34.228 20.106  -38.670  1.00 21.38 ? 69   ARG A NH1 1 
ATOM   510   N  NH2 . ARG A  1 69  ? 32.271 18.945  -38.397  1.00 18.93 ? 69   ARG A NH2 1 
ATOM   511   N  N   . LYS A  1 70  ? 27.376 22.189  -43.911  1.00 9.83  ? 70   LYS A N   1 
ATOM   512   C  CA  . LYS A  1 70  ? 26.109 21.955  -44.572  1.00 9.40  ? 70   LYS A CA  1 
ATOM   513   C  C   . LYS A  1 70  ? 25.217 21.114  -43.657  1.00 8.16  ? 70   LYS A C   1 
ATOM   514   O  O   . LYS A  1 70  ? 25.688 20.417  -42.744  1.00 7.60  ? 70   LYS A O   1 
ATOM   515   C  CB  . LYS A  1 70  ? 26.304 21.254  -45.932  1.00 10.32 ? 70   LYS A CB  1 
ATOM   516   C  CG  . LYS A  1 70  ? 27.105 22.042  -46.978  1.00 13.11 ? 70   LYS A CG  1 
ATOM   517   C  CD  . LYS A  1 70  ? 26.402 23.317  -47.423  1.00 19.53 ? 70   LYS A CD  1 
ATOM   518   C  CE  . LYS A  1 70  ? 27.277 24.153  -48.367  1.00 22.98 ? 70   LYS A CE  1 
ATOM   519   N  NZ  . LYS A  1 70  ? 26.860 25.601  -48.340  1.00 26.03 ? 70   LYS A NZ  1 
ATOM   520   N  N   . HIS A  1 71  ? 23.917 21.179  -43.907  1.00 7.36  ? 71   HIS A N   1 
ATOM   521   C  CA  . HIS A  1 71  ? 22.960 20.402  -43.138  1.00 6.68  ? 71   HIS A CA  1 
ATOM   522   C  C   . HIS A  1 71  ? 23.192 18.898  -43.286  1.00 6.78  ? 71   HIS A C   1 
ATOM   523   O  O   . HIS A  1 71  ? 23.500 18.402  -44.381  1.00 6.03  ? 71   HIS A O   1 
ATOM   524   C  CB  . HIS A  1 71  ? 21.534 20.764  -43.589  1.00 6.21  ? 71   HIS A CB  1 
ATOM   525   C  CG  . HIS A  1 71  ? 20.462 19.999  -42.891  1.00 5.96  ? 71   HIS A CG  1 
ATOM   526   N  ND1 . HIS A  1 71  ? 20.000 20.346  -41.643  1.00 6.81  ? 71   HIS A ND1 1 
ATOM   527   C  CD2 . HIS A  1 71  ? 19.730 18.934  -43.279  1.00 5.73  ? 71   HIS A CD2 1 
ATOM   528   C  CE1 . HIS A  1 71  ? 19.049 19.511  -41.276  1.00 6.88  ? 71   HIS A CE1 1 
ATOM   529   N  NE2 . HIS A  1 71  ? 18.867 18.638  -42.251  1.00 6.50  ? 71   HIS A NE2 1 
ATOM   530   N  N   . GLY A  1 72  ? 23.008 18.183  -42.189  1.00 6.81  ? 72   GLY A N   1 
ATOM   531   C  CA  . GLY A  1 72  ? 23.056 16.727  -42.192  1.00 8.05  ? 72   GLY A CA  1 
ATOM   532   C  C   . GLY A  1 72  ? 22.175 16.114  -41.128  1.00 8.49  ? 72   GLY A C   1 
ATOM   533   O  O   . GLY A  1 72  ? 21.363 16.800  -40.471  1.00 8.51  ? 72   GLY A O   1 
ATOM   534   N  N   . GLY A  1 73  ? 22.330 14.817  -40.940  1.00 7.92  ? 73   GLY A N   1 
ATOM   535   C  CA  . GLY A  1 73  ? 21.703 14.183  -39.812  1.00 7.48  ? 73   GLY A CA  1 
ATOM   536   C  C   . GLY A  1 73  ? 22.668 14.279  -38.629  1.00 8.03  ? 73   GLY A C   1 
ATOM   537   O  O   . GLY A  1 73  ? 23.855 14.593  -38.825  1.00 6.19  ? 73   GLY A O   1 
ATOM   538   N  N   . PRO A  1 74  ? 22.183 13.962  -37.419  1.00 8.13  ? 74   PRO A N   1 
ATOM   539   C  CA  . PRO A  1 74  ? 23.003 14.045  -36.194  1.00 8.37  ? 74   PRO A CA  1 
ATOM   540   C  C   . PRO A  1 74  ? 24.217 13.109  -36.224  1.00 8.87  ? 74   PRO A C   1 
ATOM   541   O  O   . PRO A  1 74  ? 25.244 13.408  -35.602  1.00 7.95  ? 74   PRO A O   1 
ATOM   542   C  CB  . PRO A  1 74  ? 22.029 13.658  -35.081  1.00 8.14  ? 74   PRO A CB  1 
ATOM   543   C  CG  . PRO A  1 74  ? 20.909 12.942  -35.760  1.00 8.86  ? 74   PRO A CG  1 
ATOM   544   C  CD  . PRO A  1 74  ? 20.814 13.470  -37.145  1.00 9.36  ? 74   PRO A CD  1 
ATOM   545   N  N   . LYS A  1 75  ? 24.095 11.998  -36.950  1.00 8.73  ? 75   LYS A N   1 
ATOM   546   C  CA  . LYS A  1 75  ? 25.199 11.044  -37.086  1.00 9.97  ? 75   LYS A CA  1 
ATOM   547   C  C   . LYS A  1 75  ? 26.313 11.501  -38.007  1.00 9.74  ? 75   LYS A C   1 
ATOM   548   O  O   . LYS A  1 75  ? 27.408 10.925  -37.974  1.00 10.55 ? 75   LYS A O   1 
ATOM   549   C  CB  . LYS A  1 75  ? 24.677 9.689   -37.567  1.00 10.30 ? 75   LYS A CB  1 
ATOM   550   C  CG  . LYS A  1 75  ? 23.803 8.993   -36.534  1.00 12.57 ? 75   LYS A CG  1 
ATOM   551   C  CD  . LYS A  1 75  ? 23.002 7.843   -37.146  1.00 15.06 ? 75   LYS A CD  1 
ATOM   552   C  CE  . LYS A  1 75  ? 23.814 6.560   -37.260  1.00 16.93 ? 75   LYS A CE  1 
ATOM   553   N  NZ  . LYS A  1 75  ? 23.001 5.411   -37.826  1.00 16.19 ? 75   LYS A NZ  1 
ATOM   554   N  N   . ASP A  1 76  ? 26.054 12.511  -38.834  1.00 9.55  ? 76   ASP A N   1 
ATOM   555   C  CA  . ASP A  1 76  ? 27.029 12.949  -39.819  1.00 10.13 ? 76   ASP A CA  1 
ATOM   556   C  C   . ASP A  1 76  ? 28.105 13.852  -39.237  1.00 11.00 ? 76   ASP A C   1 
ATOM   557   O  O   . ASP A  1 76  ? 27.834 14.684  -38.369  1.00 10.52 ? 76   ASP A O   1 
ATOM   558   C  CB  . ASP A  1 76  ? 26.339 13.690  -40.952  1.00 10.35 ? 76   ASP A CB  1 
ATOM   559   C  CG  . ASP A  1 76  ? 25.416 12.792  -41.753  1.00 11.68 ? 76   ASP A CG  1 
ATOM   560   O  OD1 . ASP A  1 76  ? 24.300 13.236  -42.056  1.00 8.70  ? 76   ASP A OD1 1 
ATOM   561   O  OD2 . ASP A  1 76  ? 25.808 11.646  -42.072  1.00 12.80 ? 76   ASP A OD2 1 
ATOM   562   N  N   . GLU A  1 77  ? 29.325 13.684  -39.735  1.00 11.27 ? 77   GLU A N   1 
ATOM   563   C  CA  . GLU A  1 77  ? 30.383 14.619  -39.442  1.00 12.61 ? 77   GLU A CA  1 
ATOM   564   C  C   . GLU A  1 77  ? 30.008 15.972  -40.049  1.00 10.85 ? 77   GLU A C   1 
ATOM   565   O  O   . GLU A  1 77  ? 30.157 17.007  -39.399  1.00 11.91 ? 77   GLU A O   1 
ATOM   566   C  CB  . GLU A  1 77  ? 31.715 14.107  -40.004  1.00 13.49 ? 77   GLU A CB  1 
ATOM   567   C  CG  . GLU A  1 77  ? 32.863 14.110  -38.992  1.00 19.59 ? 77   GLU A CG  1 
ATOM   568   C  CD  . GLU A  1 77  ? 33.422 15.498  -38.719  1.00 27.40 ? 77   GLU A CD  1 
ATOM   569   O  OE1 . GLU A  1 77  ? 34.497 15.837  -39.280  1.00 31.96 ? 77   GLU A OE1 1 
ATOM   570   O  OE2 . GLU A  1 77  ? 32.787 16.245  -37.940  1.00 31.59 ? 77   GLU A OE2 1 
ATOM   571   N  N   . GLU A  1 78  ? 29.465 15.949  -41.261  1.00 8.97  ? 78   GLU A N   1 
ATOM   572   C  CA  . GLU A  1 78  ? 28.989 17.156  -41.912  1.00 9.26  ? 78   GLU A CA  1 
ATOM   573   C  C   . GLU A  1 78  ? 27.540 17.441  -41.520  1.00 8.31  ? 78   GLU A C   1 
ATOM   574   O  O   . GLU A  1 78  ? 26.596 16.879  -42.072  1.00 7.98  ? 78   GLU A O   1 
ATOM   575   C  CB  . GLU A  1 78  ? 29.130 17.084  -43.438  1.00 9.40  ? 78   GLU A CB  1 
ATOM   576   C  CG  . GLU A  1 78  ? 28.796 18.415  -44.166  1.00 11.73 ? 78   GLU A CG  1 
ATOM   577   C  CD  . GLU A  1 78  ? 29.868 19.484  -44.022  1.00 13.28 ? 78   GLU A CD  1 
ATOM   578   O  OE1 . GLU A  1 78  ? 29.638 20.608  -44.521  1.00 13.92 ? 78   GLU A OE1 1 
ATOM   579   O  OE2 . GLU A  1 78  ? 30.943 19.212  -43.424  1.00 17.84 ? 78   GLU A OE2 1 
ATOM   580   N  N   . ARG A  1 79  ? 27.385 18.304  -40.537  1.00 7.71  ? 79   ARG A N   1 
ATOM   581   C  CA  . ARG A  1 79  ? 26.059 18.679  -40.055  1.00 6.83  ? 79   ARG A CA  1 
ATOM   582   C  C   . ARG A  1 79  ? 26.194 20.041  -39.421  1.00 6.85  ? 79   ARG A C   1 
ATOM   583   O  O   . ARG A  1 79  ? 27.308 20.487  -39.125  1.00 6.88  ? 79   ARG A O   1 
ATOM   584   C  CB  . ARG A  1 79  ? 25.554 17.687  -39.001  1.00 6.59  ? 79   ARG A CB  1 
ATOM   585   C  CG  . ARG A  1 79  ? 26.482 17.523  -37.775  1.00 7.06  ? 79   ARG A CG  1 
ATOM   586   C  CD  . ARG A  1 79  ? 25.867 16.708  -36.660  1.00 7.98  ? 79   ARG A CD  1 
ATOM   587   N  NE  . ARG A  1 79  ? 25.146 17.564  -35.692  1.00 5.75  ? 79   ARG A NE  1 
ATOM   588   C  CZ  . ARG A  1 79  ? 24.726 17.133  -34.510  1.00 4.77  ? 79   ARG A CZ  1 
ATOM   589   N  NH1 . ARG A  1 79  ? 24.124 17.959  -33.671  1.00 7.05  ? 79   ARG A NH1 1 
ATOM   590   N  NH2 . ARG A  1 79  ? 24.906 15.874  -34.150  1.00 4.09  ? 79   ARG A NH2 1 
ATOM   591   N  N   . HIS A  1 80  ? 25.055 20.701  -39.230  1.00 6.32  ? 80   HIS A N   1 
ATOM   592   C  CA  . HIS A  1 80  ? 24.977 21.866  -38.352  1.00 4.90  ? 80   HIS A CA  1 
ATOM   593   C  C   . HIS A  1 80  ? 25.000 21.386  -36.893  1.00 3.83  ? 80   HIS A C   1 
ATOM   594   O  O   . HIS A  1 80  ? 24.529 20.291  -36.566  1.00 3.25  ? 80   HIS A O   1 
ATOM   595   C  CB  . HIS A  1 80  ? 23.674 22.671  -38.619  1.00 4.28  ? 80   HIS A CB  1 
ATOM   596   C  CG  . HIS A  1 80  ? 23.497 23.107  -40.044  1.00 6.27  ? 80   HIS A CG  1 
ATOM   597   N  ND1 . HIS A  1 80  ? 22.271 23.131  -40.676  1.00 3.45  ? 80   HIS A ND1 1 
ATOM   598   C  CD2 . HIS A  1 80  ? 24.399 23.526  -40.958  1.00 3.31  ? 80   HIS A CD2 1 
ATOM   599   C  CE1 . HIS A  1 80  ? 22.428 23.568  -41.916  1.00 5.78  ? 80   HIS A CE1 1 
ATOM   600   N  NE2 . HIS A  1 80  ? 23.712 23.815  -42.107  1.00 5.46  ? 80   HIS A NE2 1 
ATOM   601   N  N   . VAL A  1 81  ? 25.557 22.200  -36.007  1.00 3.18  ? 81   VAL A N   1 
ATOM   602   C  CA  . VAL A  1 81  ? 25.464 21.898  -34.585  1.00 3.51  ? 81   VAL A CA  1 
ATOM   603   C  C   . VAL A  1 81  ? 24.005 21.647  -34.204  1.00 3.42  ? 81   VAL A C   1 
ATOM   604   O  O   . VAL A  1 81  ? 23.717 20.756  -33.436  1.00 3.00  ? 81   VAL A O   1 
ATOM   605   C  CB  . VAL A  1 81  ? 26.080 23.021  -33.713  1.00 4.10  ? 81   VAL A CB  1 
ATOM   606   C  CG1 . VAL A  1 81  ? 25.686 22.871  -32.262  1.00 3.89  ? 81   VAL A CG1 1 
ATOM   607   C  CG2 . VAL A  1 81  ? 27.614 22.977  -33.829  1.00 4.14  ? 81   VAL A CG2 1 
ATOM   608   N  N   . GLY A  1 82  ? 23.094 22.426  -34.766  1.00 3.98  ? 82   GLY A N   1 
ATOM   609   C  CA  . GLY A  1 82  ? 21.669 22.340  -34.373  1.00 3.85  ? 82   GLY A CA  1 
ATOM   610   C  C   . GLY A  1 82  ? 20.900 21.146  -34.928  1.00 4.95  ? 82   GLY A C   1 
ATOM   611   O  O   . GLY A  1 82  ? 19.701 21.014  -34.655  1.00 3.63  ? 82   GLY A O   1 
ATOM   612   N  N   . ASP A  1 83  ? 21.574 20.280  -35.693  1.00 4.77  ? 83   ASP A N   1 
ATOM   613   C  CA  . ASP A  1 83  ? 20.890 19.178  -36.409  1.00 5.12  ? 83   ASP A CA  1 
ATOM   614   C  C   . ASP A  1 83  ? 20.622 17.931  -35.561  1.00 5.47  ? 83   ASP A C   1 
ATOM   615   O  O   . ASP A  1 83  ? 21.502 17.060  -35.392  1.00 6.71  ? 83   ASP A O   1 
ATOM   616   C  CB  . ASP A  1 83  ? 21.679 18.775  -37.667  1.00 5.55  ? 83   ASP A CB  1 
ATOM   617   C  CG  . ASP A  1 83  ? 21.666 19.817  -38.731  1.00 4.91  ? 83   ASP A CG  1 
ATOM   618   O  OD1 . ASP A  1 83  ? 20.767 20.701  -38.721  1.00 3.47  ? 83   ASP A OD1 1 
ATOM   619   O  OD2 . ASP A  1 83  ? 22.554 19.754  -39.621  1.00 2.43  ? 83   ASP A OD2 1 
ATOM   620   N  N   . LEU A  1 84  ? 19.400 17.816  -35.044  1.00 4.68  ? 84   LEU A N   1 
ATOM   621   C  CA  . LEU A  1 84  ? 19.075 16.696  -34.180  1.00 5.55  ? 84   LEU A CA  1 
ATOM   622   C  C   . LEU A  1 84  ? 18.245 15.631  -34.918  1.00 5.44  ? 84   LEU A C   1 
ATOM   623   O  O   . LEU A  1 84  ? 17.725 14.702  -34.302  1.00 6.93  ? 84   LEU A O   1 
ATOM   624   C  CB  . LEU A  1 84  ? 18.389 17.194  -32.901  1.00 5.61  ? 84   LEU A CB  1 
ATOM   625   C  CG  . LEU A  1 84  ? 19.302 18.081  -32.045  1.00 5.95  ? 84   LEU A CG  1 
ATOM   626   C  CD1 . LEU A  1 84  ? 18.532 18.703  -30.881  1.00 6.32  ? 84   LEU A CD1 1 
ATOM   627   C  CD2 . LEU A  1 84  ? 20.527 17.276  -31.523  1.00 5.21  ? 84   LEU A CD2 1 
ATOM   628   N  N   . GLY A  1 85  ? 18.125 15.795  -36.227  1.00 5.21  ? 85   GLY A N   1 
ATOM   629   C  CA  . GLY A  1 85  ? 17.417 14.846  -37.091  1.00 6.25  ? 85   GLY A CA  1 
ATOM   630   C  C   . GLY A  1 85  ? 15.902 14.942  -36.949  1.00 6.28  ? 85   GLY A C   1 
ATOM   631   O  O   . GLY A  1 85  ? 15.340 16.028  -37.036  1.00 5.74  ? 85   GLY A O   1 
ATOM   632   N  N   . ASN A  1 86  ? 15.267 13.803  -36.733  1.00 5.31  ? 86   ASN A N   1 
ATOM   633   C  CA  . ASN A  1 86  ? 13.811 13.711  -36.663  1.00 6.20  ? 86   ASN A CA  1 
ATOM   634   C  C   . ASN A  1 86  ? 13.343 13.167  -35.319  1.00 5.99  ? 86   ASN A C   1 
ATOM   635   O  O   . ASN A  1 86  ? 14.073 12.456  -34.610  1.00 6.35  ? 86   ASN A O   1 
ATOM   636   C  CB  . ASN A  1 86  ? 13.266 12.767  -37.755  1.00 5.65  ? 86   ASN A CB  1 
ATOM   637   C  CG  . ASN A  1 86  ? 13.435 13.301  -39.141  1.00 5.84  ? 86   ASN A CG  1 
ATOM   638   O  OD1 . ASN A  1 86  ? 12.818 14.278  -39.518  1.00 4.83  ? 86   ASN A OD1 1 
ATOM   639   N  ND2 . ASN A  1 86  ? 14.239 12.611  -39.944  1.00 8.64  ? 86   ASN A ND2 1 
ATOM   640   N  N   . VAL A  1 87  ? 12.109 13.524  -34.968  1.00 6.08  ? 87   VAL A N   1 
ATOM   641   C  CA  . VAL A  1 87  ? 11.388 12.829  -33.944  1.00 5.80  ? 87   VAL A CA  1 
ATOM   642   C  C   . VAL A  1 87  ? 10.200 12.139  -34.625  1.00 5.78  ? 87   VAL A C   1 
ATOM   643   O  O   . VAL A  1 87  ? 9.757  12.556  -35.705  1.00 6.96  ? 87   VAL A O   1 
ATOM   644   C  CB  . VAL A  1 87  ? 10.929 13.767  -32.801  1.00 5.41  ? 87   VAL A CB  1 
ATOM   645   C  CG1 . VAL A  1 87  ? 12.176 14.297  -32.046  1.00 7.44  ? 87   VAL A CG1 1 
ATOM   646   C  CG2 . VAL A  1 87  ? 10.106 14.910  -33.361  1.00 6.18  ? 87   VAL A CG2 1 
ATOM   647   N  N   . THR A  1 88  ? 9.682  11.115  -33.969  1.00 5.27  ? 88   THR A N   1 
ATOM   648   C  CA  . THR A  1 88  ? 8.580  10.321  -34.512  1.00 5.82  ? 88   THR A CA  1 
ATOM   649   C  C   . THR A  1 88  ? 7.352  10.404  -33.620  1.00 6.22  ? 88   THR A C   1 
ATOM   650   O  O   . THR A  1 88  ? 7.431  10.096  -32.436  1.00 6.49  ? 88   THR A O   1 
ATOM   651   C  CB  . THR A  1 88  ? 8.989  8.829   -34.640  1.00 5.76  ? 88   THR A CB  1 
ATOM   652   O  OG1 . THR A  1 88  ? 10.178 8.721   -35.440  1.00 6.15  ? 88   THR A OG1 1 
ATOM   653   C  CG2 . THR A  1 88  ? 7.875  8.029   -35.298  1.00 6.57  ? 88   THR A CG2 1 
ATOM   654   N  N   . ALA A  1 89  ? 6.233  10.838  -34.200  1.00 7.44  ? 89   ALA A N   1 
ATOM   655   C  CA  . ALA A  1 89  ? 4.960  10.883  -33.484  1.00 8.16  ? 89   ALA A CA  1 
ATOM   656   C  C   . ALA A  1 89  ? 4.173  9.608   -33.816  1.00 8.33  ? 89   ALA A C   1 
ATOM   657   O  O   . ALA A  1 89  ? 4.128  9.181   -34.985  1.00 8.92  ? 89   ALA A O   1 
ATOM   658   C  CB  . ALA A  1 89  ? 4.164  12.116  -33.867  1.00 7.89  ? 89   ALA A CB  1 
ATOM   659   N  N   . ASP A  1 90  ? 3.575  9.020   -32.781  1.00 8.52  ? 90   ASP A N   1 
ATOM   660   C  CA  . ASP A  1 90  ? 2.750  7.797   -32.916  1.00 9.23  ? 90   ASP A CA  1 
ATOM   661   C  C   . ASP A  1 90  ? 1.375  8.131   -33.535  1.00 8.97  ? 90   ASP A C   1 
ATOM   662   O  O   . ASP A  1 90  ? 1.136  9.259   -33.965  1.00 8.74  ? 90   ASP A O   1 
ATOM   663   C  CB  . ASP A  1 90  ? 2.654  7.047   -31.570  1.00 8.39  ? 90   ASP A CB  1 
ATOM   664   C  CG  . ASP A  1 90  ? 1.957  7.863   -30.474  1.00 9.55  ? 90   ASP A CG  1 
ATOM   665   O  OD1 . ASP A  1 90  ? 2.173  7.568   -29.279  1.00 13.31 ? 90   ASP A OD1 1 
ATOM   666   O  OD2 . ASP A  1 90  ? 1.186  8.788   -30.781  1.00 9.35  ? 90   ASP A OD2 1 
ATOM   667   N  N   . LYS A  1 91  ? 0.474  7.148   -33.627  1.00 10.70 ? 91   LYS A N   1 
ATOM   668   C  CA  . LYS A  1 91  ? -0.794 7.388   -34.309  1.00 10.79 ? 91   LYS A CA  1 
ATOM   669   C  C   . LYS A  1 91  ? -1.677 8.401   -33.566  1.00 10.26 ? 91   LYS A C   1 
ATOM   670   O  O   . LYS A  1 91  ? -2.569 9.008   -34.159  1.00 11.35 ? 91   LYS A O   1 
ATOM   671   C  CB  . LYS A  1 91  ? -1.554 6.063   -34.580  1.00 12.19 ? 91   LYS A CB  1 
ATOM   672   C  CG  . LYS A  1 91  ? -1.852 5.262   -33.331  1.00 14.53 ? 91   LYS A CG  1 
ATOM   673   C  CD  . LYS A  1 91  ? -2.715 4.023   -33.627  1.00 21.43 ? 91   LYS A CD  1 
ATOM   674   C  CE  . LYS A  1 91  ? -2.532 2.979   -32.511  1.00 24.29 ? 91   LYS A CE  1 
ATOM   675   N  NZ  . LYS A  1 91  ? -3.370 1.765   -32.747  1.00 26.69 ? 91   LYS A NZ  1 
ATOM   676   N  N   . ASP A  1 92  ? -1.409 8.583   -32.282  1.00 9.58  ? 92   ASP A N   1 
ATOM   677   C  CA  . ASP A  1 92  ? -2.133 9.547   -31.447  1.00 9.59  ? 92   ASP A CA  1 
ATOM   678   C  C   . ASP A  1 92  ? -1.514 10.946  -31.544  1.00 8.70  ? 92   ASP A C   1 
ATOM   679   O  O   . ASP A  1 92  ? -1.987 11.898  -30.892  1.00 7.90  ? 92   ASP A O   1 
ATOM   680   C  CB  . ASP A  1 92  ? -2.152 9.063   -30.002  1.00 9.94  ? 92   ASP A CB  1 
ATOM   681   C  CG  . ASP A  1 92  ? -3.000 7.791   -29.828  1.00 13.60 ? 92   ASP A CG  1 
ATOM   682   O  OD1 . ASP A  1 92  ? -2.922 7.168   -28.761  1.00 18.50 ? 92   ASP A OD1 1 
ATOM   683   O  OD2 . ASP A  1 92  ? -3.743 7.439   -30.762  1.00 16.11 ? 92   ASP A OD2 1 
ATOM   684   N  N   . GLY A  1 93  ? -0.459 11.060  -32.350  1.00 6.58  ? 93   GLY A N   1 
ATOM   685   C  CA  . GLY A  1 93  ? 0.200  12.363  -32.580  1.00 6.53  ? 93   GLY A CA  1 
ATOM   686   C  C   . GLY A  1 93  ? 1.198  12.808  -31.521  1.00 5.91  ? 93   GLY A C   1 
ATOM   687   O  O   . GLY A  1 93  ? 1.552  13.988  -31.464  1.00 4.92  ? 93   GLY A O   1 
ATOM   688   N  N   . VAL A  1 94  ? 1.653  11.866  -30.699  1.00 6.20  ? 94   VAL A N   1 
ATOM   689   C  CA  . VAL A  1 94  ? 2.591  12.137  -29.621  1.00 6.46  ? 94   VAL A CA  1 
ATOM   690   C  C   . VAL A  1 94  ? 3.968  11.595  -29.989  1.00 6.92  ? 94   VAL A C   1 
ATOM   691   O  O   . VAL A  1 94  ? 4.104  10.421  -30.311  1.00 7.04  ? 94   VAL A O   1 
ATOM   692   C  CB  . VAL A  1 94  ? 2.137  11.457  -28.291  1.00 6.97  ? 94   VAL A CB  1 
ATOM   693   C  CG1 . VAL A  1 94  ? 3.151  11.686  -27.149  1.00 7.62  ? 94   VAL A CG1 1 
ATOM   694   C  CG2 . VAL A  1 94  ? 0.702  11.875  -27.892  1.00 5.98  ? 94   VAL A CG2 1 
ATOM   695   N  N   . ALA A  1 95  ? 4.980  12.454  -29.902  1.00 7.19  ? 95   ALA A N   1 
ATOM   696   C  CA  . ALA A  1 95  ? 6.376  12.035  -30.016  1.00 7.86  ? 95   ALA A CA  1 
ATOM   697   C  C   . ALA A  1 95  ? 7.010  11.980  -28.621  1.00 8.40  ? 95   ALA A C   1 
ATOM   698   O  O   . ALA A  1 95  ? 7.169  13.020  -27.935  1.00 8.41  ? 95   ALA A O   1 
ATOM   699   C  CB  . ALA A  1 95  ? 7.133  12.993  -30.930  1.00 7.78  ? 95   ALA A CB  1 
ATOM   700   N  N   . ASP A  1 96  ? 7.322  10.768  -28.175  1.00 8.05  ? 96   ASP A N   1 
ATOM   701   C  CA  . ASP A  1 96  ? 8.105  10.533  -26.964  1.00 9.51  ? 96   ASP A CA  1 
ATOM   702   C  C   . ASP A  1 96  ? 9.615  10.688  -27.264  1.00 8.44  ? 96   ASP A C   1 
ATOM   703   O  O   . ASP A  1 96  ? 10.299 9.732   -27.673  1.00 9.04  ? 96   ASP A O   1 
ATOM   704   C  CB  . ASP A  1 96  ? 7.774  9.125   -26.444  1.00 10.50 ? 96   ASP A CB  1 
ATOM   705   C  CG  . ASP A  1 96  ? 8.437  8.787   -25.108  1.00 17.38 ? 96   ASP A CG  1 
ATOM   706   O  OD1 . ASP A  1 96  ? 9.070  9.654   -24.455  1.00 20.09 ? 96   ASP A OD1 1 
ATOM   707   O  OD2 . ASP A  1 96  ? 8.320  7.599   -24.696  1.00 22.58 ? 96   ASP A OD2 1 
ATOM   708   N  N   . VAL A  1 97  ? 10.141 11.883  -27.043  1.00 6.78  ? 97   VAL A N   1 
ATOM   709   C  CA  . VAL A  1 97  ? 11.487 12.223  -27.520  1.00 5.58  ? 97   VAL A CA  1 
ATOM   710   C  C   . VAL A  1 97  ? 12.540 11.683  -26.580  1.00 5.59  ? 97   VAL A C   1 
ATOM   711   O  O   . VAL A  1 97  ? 12.446 11.839  -25.381  1.00 5.67  ? 97   VAL A O   1 
ATOM   712   C  CB  . VAL A  1 97  ? 11.637 13.759  -27.684  1.00 4.51  ? 97   VAL A CB  1 
ATOM   713   C  CG1 . VAL A  1 97  ? 13.062 14.144  -28.135  1.00 5.13  ? 97   VAL A CG1 1 
ATOM   714   C  CG2 . VAL A  1 97  ? 10.641 14.251  -28.678  1.00 4.14  ? 97   VAL A CG2 1 
ATOM   715   N  N   . SER A  1 98  ? 13.547 11.045  -27.152  1.00 7.83  ? 98   SER A N   1 
ATOM   716   C  CA  . SER A  1 98  ? 14.661 10.516  -26.416  1.00 9.28  ? 98   SER A CA  1 
ATOM   717   C  C   . SER A  1 98  ? 15.867 10.464  -27.368  1.00 9.14  ? 98   SER A C   1 
ATOM   718   O  O   . SER A  1 98  ? 15.936 9.655   -28.310  1.00 8.96  ? 98   SER A O   1 
ATOM   719   C  CB  . SER A  1 98  ? 14.305 9.161   -25.813  1.00 10.67 ? 98   SER A CB  1 
ATOM   720   O  OG  . SER A  1 98  ? 15.394 8.622   -25.082  1.00 14.98 ? 98   SER A OG  1 
ATOM   721   N  N   . ILE A  1 99  ? 16.790 11.400  -27.162  1.00 9.22  ? 99   ILE A N   1 
ATOM   722   C  CA  . ILE A  1 99  ? 17.925 11.594  -28.065  1.00 8.53  ? 99   ILE A CA  1 
ATOM   723   C  C   . ILE A  1 99  ? 19.152 11.816  -27.181  1.00 8.68  ? 99   ILE A C   1 
ATOM   724   O  O   . ILE A  1 99  ? 19.047 12.300  -26.040  1.00 8.40  ? 99   ILE A O   1 
ATOM   725   C  CB  . ILE A  1 99  ? 17.709 12.818  -29.015  1.00 8.78  ? 99   ILE A CB  1 
ATOM   726   C  CG1 . ILE A  1 99  ? 16.722 12.484  -30.142  1.00 9.34  ? 99   ILE A CG1 1 
ATOM   727   C  CG2 . ILE A  1 99  ? 19.043 13.329  -29.607  1.00 10.40 ? 99   ILE A CG2 1 
ATOM   728   C  CD1 . ILE A  1 99  ? 16.090 13.729  -30.837  1.00 14.51 ? 99   ILE A CD1 1 
ATOM   729   N  N   . GLU A  1 100 ? 20.304 11.379  -27.675  1.00 8.48  ? 100  GLU A N   1 
ATOM   730   C  CA  . GLU A  1 100 ? 21.555 11.737  -27.038  1.00 8.45  ? 100  GLU A CA  1 
ATOM   731   C  C   . GLU A  1 100 ? 22.474 12.273  -28.113  1.00 8.24  ? 100  GLU A C   1 
ATOM   732   O  O   . GLU A  1 100 ? 22.592 11.702  -29.189  1.00 7.54  ? 100  GLU A O   1 
ATOM   733   C  CB  . GLU A  1 100 ? 22.168 10.574  -26.269  1.00 9.14  ? 100  GLU A CB  1 
ATOM   734   C  CG  . GLU A  1 100 ? 23.313 11.010  -25.376  1.00 14.78 ? 100  GLU A CG  1 
ATOM   735   C  CD  . GLU A  1 100 ? 23.604 10.053  -24.235  1.00 22.65 ? 100  GLU A CD  1 
ATOM   736   O  OE1 . GLU A  1 100 ? 23.104 8.894   -24.264  1.00 26.47 ? 100  GLU A OE1 1 
ATOM   737   O  OE2 . GLU A  1 100 ? 24.335 10.460  -23.304  1.00 24.39 ? 100  GLU A OE2 1 
ATOM   738   N  N   . ASP A  1 101 ? 23.102 13.409  -27.835  1.00 7.38  ? 101  ASP A N   1 
ATOM   739   C  CA  . ASP A  1 101 ? 23.857 14.083  -28.863  1.00 7.72  ? 101  ASP A CA  1 
ATOM   740   C  C   . ASP A  1 101 ? 25.116 14.665  -28.277  1.00 7.79  ? 101  ASP A C   1 
ATOM   741   O  O   . ASP A  1 101 ? 25.087 15.289  -27.225  1.00 6.59  ? 101  ASP A O   1 
ATOM   742   C  CB  . ASP A  1 101 ? 23.033 15.187  -29.544  1.00 7.72  ? 101  ASP A CB  1 
ATOM   743   C  CG  . ASP A  1 101 ? 23.694 15.688  -30.828  1.00 9.42  ? 101  ASP A CG  1 
ATOM   744   O  OD1 . ASP A  1 101 ? 24.388 16.746  -30.802  1.00 6.43  ? 101  ASP A OD1 1 
ATOM   745   O  OD2 . ASP A  1 101 ? 23.563 14.988  -31.862  1.00 9.75  ? 101  ASP A OD2 1 
ATOM   746   N  N   . SER A  1 102 ? 26.225 14.458  -28.979  1.00 8.75  ? 102  SER A N   1 
ATOM   747   C  CA  . SER A  1 102 ? 27.523 14.909  -28.485  1.00 9.02  ? 102  SER A CA  1 
ATOM   748   C  C   . SER A  1 102 ? 28.052 16.183  -29.153  1.00 7.70  ? 102  SER A C   1 
ATOM   749   O  O   . SER A  1 102 ? 29.195 16.600  -28.906  1.00 8.52  ? 102  SER A O   1 
ATOM   750   C  CB  . SER A  1 102 ? 28.522 13.763  -28.631  1.00 9.74  ? 102  SER A CB  1 
ATOM   751   O  OG  . SER A  1 102 ? 28.324 12.895  -27.528  1.00 14.12 ? 102  SER A OG  1 
ATOM   752   N  N   . VAL A  1 103 ? 27.231 16.817  -29.980  1.00 6.11  ? 103  VAL A N   1 
ATOM   753   C  CA  . VAL A  1 103 ? 27.667 17.994  -30.738  1.00 4.35  ? 103  VAL A CA  1 
ATOM   754   C  C   . VAL A  1 103 ? 27.016 19.277  -30.176  1.00 4.56  ? 103  VAL A C   1 
ATOM   755   O  O   . VAL A  1 103 ? 27.667 20.316  -30.036  1.00 3.97  ? 103  VAL A O   1 
ATOM   756   C  CB  . VAL A  1 103 ? 27.390 17.795  -32.256  1.00 4.80  ? 103  VAL A CB  1 
ATOM   757   C  CG1 . VAL A  1 103 ? 27.621 19.100  -33.078  1.00 4.98  ? 103  VAL A CG1 1 
ATOM   758   C  CG2 . VAL A  1 103 ? 28.270 16.644  -32.810  1.00 4.53  ? 103  VAL A CG2 1 
ATOM   759   N  N   . ILE A  1 104 ? 25.737 19.202  -29.830  1.00 4.45  ? 104  ILE A N   1 
ATOM   760   C  CA  . ILE A  1 104 ? 25.152 20.259  -28.992  1.00 3.68  ? 104  ILE A CA  1 
ATOM   761   C  C   . ILE A  1 104 ? 25.781 20.234  -27.616  1.00 3.20  ? 104  ILE A C   1 
ATOM   762   O  O   . ILE A  1 104 ? 26.292 19.192  -27.156  1.00 2.81  ? 104  ILE A O   1 
ATOM   763   C  CB  . ILE A  1 104 ? 23.578 20.153  -28.877  1.00 3.03  ? 104  ILE A CB  1 
ATOM   764   C  CG1 . ILE A  1 104 ? 23.177 18.859  -28.159  1.00 3.26  ? 104  ILE A CG1 1 
ATOM   765   C  CG2 . ILE A  1 104 ? 22.959 20.304  -30.264  1.00 5.44  ? 104  ILE A CG2 1 
ATOM   766   C  CD1 . ILE A  1 104 ? 21.708 18.742  -27.750  1.00 3.10  ? 104  ILE A CD1 1 
ATOM   767   N  N   . SER A  1 105 ? 25.735 21.375  -26.930  1.00 2.29  ? 105  SER A N   1 
ATOM   768   C  CA  . SER A  1 105 ? 26.245 21.439  -25.576  1.00 2.67  ? 105  SER A CA  1 
ATOM   769   C  C   . SER A  1 105 ? 25.454 22.455  -24.781  1.00 2.05  ? 105  SER A C   1 
ATOM   770   O  O   . SER A  1 105 ? 24.746 23.287  -25.358  1.00 2.00  ? 105  SER A O   1 
ATOM   771   C  CB  . SER A  1 105 ? 27.719 21.833  -25.601  1.00 2.20  ? 105  SER A CB  1 
ATOM   772   O  OG  . SER A  1 105 ? 28.217 21.775  -24.284  1.00 2.66  ? 105  SER A OG  1 
ATOM   773   N  N   . LEU A  1 106 ? 25.553 22.382  -23.468  1.00 2.86  ? 106  LEU A N   1 
ATOM   774   C  CA  . LEU A  1 106 ? 24.894 23.390  -22.613  1.00 4.17  ? 106  LEU A CA  1 
ATOM   775   C  C   . LEU A  1 106 ? 25.870 24.457  -22.096  1.00 5.21  ? 106  LEU A C   1 
ATOM   776   O  O   . LEU A  1 106 ? 25.550 25.196  -21.165  1.00 6.36  ? 106  LEU A O   1 
ATOM   777   C  CB  . LEU A  1 106 ? 24.120 22.725  -21.460  1.00 3.63  ? 106  LEU A CB  1 
ATOM   778   C  CG  . LEU A  1 106 ? 23.056 21.757  -21.969  1.00 2.92  ? 106  LEU A CG  1 
ATOM   779   C  CD1 . LEU A  1 106 ? 22.312 21.111  -20.782  1.00 2.38  ? 106  LEU A CD1 1 
ATOM   780   C  CD2 . LEU A  1 106 ? 22.101 22.457  -22.950  1.00 2.00  ? 106  LEU A CD2 1 
ATOM   781   N  N   . SER A  1 107 ? 27.045 24.549  -22.721  1.00 6.50  ? 107  SER A N   1 
ATOM   782   C  CA  . SER A  1 107 ? 28.046 25.577  -22.407  1.00 6.94  ? 107  SER A CA  1 
ATOM   783   C  C   . SER A  1 107 ? 29.029 25.652  -23.567  1.00 8.01  ? 107  SER A C   1 
ATOM   784   O  O   . SER A  1 107 ? 29.059 24.762  -24.418  1.00 7.06  ? 107  SER A O   1 
ATOM   785   C  CB  . SER A  1 107 ? 28.797 25.251  -21.115  1.00 8.02  ? 107  SER A CB  1 
ATOM   786   O  OG  . SER A  1 107 ? 29.623 24.108  -21.297  1.00 8.18  ? 107  SER A OG  1 
ATOM   787   N  N   . GLY A  1 108 ? 29.827 26.721  -23.614  1.00 7.96  ? 108  GLY A N   1 
ATOM   788   C  CA  . GLY A  1 108 ? 30.808 26.865  -24.683  1.00 8.40  ? 108  GLY A CA  1 
ATOM   789   C  C   . GLY A  1 108 ? 30.246 27.318  -26.022  1.00 9.04  ? 108  GLY A C   1 
ATOM   790   O  O   . GLY A  1 108 ? 29.105 27.788  -26.125  1.00 8.68  ? 108  GLY A O   1 
ATOM   791   N  N   . ASP A  1 109 ? 31.070 27.174  -27.055  1.00 8.53  ? 109  ASP A N   1 
ATOM   792   C  CA  . ASP A  1 109 ? 30.740 27.646  -28.402  1.00 9.58  ? 109  ASP A CA  1 
ATOM   793   C  C   . ASP A  1 109 ? 29.587 26.910  -29.070  1.00 8.12  ? 109  ASP A C   1 
ATOM   794   O  O   . ASP A  1 109 ? 28.981 27.448  -29.984  1.00 9.12  ? 109  ASP A O   1 
ATOM   795   C  CB  . ASP A  1 109 ? 31.959 27.511  -29.303  1.00 10.73 ? 109  ASP A CB  1 
ATOM   796   C  CG  . ASP A  1 109 ? 32.995 28.569  -29.031  1.00 15.72 ? 109  ASP A CG  1 
ATOM   797   O  OD1 . ASP A  1 109 ? 34.083 28.472  -29.616  1.00 16.97 ? 109  ASP A OD1 1 
ATOM   798   O  OD2 . ASP A  1 109 ? 32.715 29.492  -28.234  1.00 21.63 ? 109  ASP A OD2 1 
ATOM   799   N  N   . HIS A  1 110 ? 29.325 25.682  -28.625  1.00 6.98  ? 110  HIS A N   1 
ATOM   800   C  CA  . HIS A  1 110 ? 28.190 24.864  -29.104  1.00 7.39  ? 110  HIS A CA  1 
ATOM   801   C  C   . HIS A  1 110 ? 26.944 24.991  -28.190  1.00 6.35  ? 110  HIS A C   1 
ATOM   802   O  O   . HIS A  1 110 ? 25.970 24.269  -28.384  1.00 5.22  ? 110  HIS A O   1 
ATOM   803   C  CB  . HIS A  1 110 ? 28.578 23.367  -29.189  1.00 7.29  ? 110  HIS A CB  1 
ATOM   804   C  CG  . HIS A  1 110 ? 29.648 23.044  -30.204  1.00 11.84 ? 110  HIS A CG  1 
ATOM   805   N  ND1 . HIS A  1 110 ? 29.888 21.755  -30.638  1.00 12.95 ? 110  HIS A ND1 1 
ATOM   806   C  CD2 . HIS A  1 110 ? 30.552 23.828  -30.847  1.00 16.22 ? 110  HIS A CD2 1 
ATOM   807   C  CE1 . HIS A  1 110 ? 30.887 21.759  -31.506  1.00 15.64 ? 110  HIS A CE1 1 
ATOM   808   N  NE2 . HIS A  1 110 ? 31.308 23.004  -31.653  1.00 15.39 ? 110  HIS A NE2 1 
HETATM 809   N  N   . CME A  1 111 ? 27.003 25.890  -27.204  1.00 5.34  ? 111  CME A N   1 
HETATM 810   C  CA  . CME A  1 111 ? 25.878 26.130  -26.277  1.00 5.84  ? 111  CME A CA  1 
HETATM 811   C  CB  . CME A  1 111 ? 26.132 27.296  -25.317  1.00 5.70  ? 111  CME A CB  1 
HETATM 812   S  SG  . CME A  1 111 ? 24.956 27.203  -23.998  1.00 8.60  ? 111  CME A SG  1 
HETATM 813   S  SD  . CME A  1 111 ? 25.517 28.790  -22.845  1.00 15.83 ? 111  CME A SD  1 
HETATM 814   C  CE  . CME A  1 111 ? 24.464 30.065  -23.448  1.00 16.78 ? 111  CME A CE  1 
HETATM 815   C  CZ  . CME A  1 111 ? 25.048 30.780  -24.662  1.00 18.92 ? 111  CME A CZ  1 
HETATM 816   O  OH  . CME A  1 111 ? 24.370 30.363  -25.858  1.00 20.10 ? 111  CME A OH  1 
HETATM 817   C  C   . CME A  1 111 ? 24.604 26.467  -27.014  1.00 3.90  ? 111  CME A C   1 
HETATM 818   O  O   . CME A  1 111 ? 24.579 27.321  -27.897  1.00 4.27  ? 111  CME A O   1 
ATOM   819   N  N   . ILE A  1 112 ? 23.527 25.818  -26.616  1.00 4.07  ? 112  ILE A N   1 
ATOM   820   C  CA  . ILE A  1 112 ? 22.222 26.015  -27.249  1.00 3.17  ? 112  ILE A CA  1 
ATOM   821   C  C   . ILE A  1 112 ? 21.256 26.789  -26.347  1.00 2.96  ? 112  ILE A C   1 
ATOM   822   O  O   . ILE A  1 112 ? 20.155 27.146  -26.789  1.00 2.82  ? 112  ILE A O   1 
ATOM   823   C  CB  . ILE A  1 112 ? 21.610 24.661  -27.674  1.00 3.31  ? 112  ILE A CB  1 
ATOM   824   C  CG1 . ILE A  1 112 ? 21.485 23.722  -26.468  1.00 2.30  ? 112  ILE A CG1 1 
ATOM   825   C  CG2 . ILE A  1 112 ? 22.445 24.022  -28.842  1.00 3.15  ? 112  ILE A CG2 1 
ATOM   826   C  CD1 . ILE A  1 112 ? 20.667 22.443  -26.738  1.00 5.14  ? 112  ILE A CD1 1 
ATOM   827   N  N   . ILE A  1 113 ? 21.645 27.010  -25.089  1.00 2.29  ? 113  ILE A N   1 
ATOM   828   C  CA  . ILE A  1 113 ? 20.823 27.831  -24.155  1.00 2.48  ? 113  ILE A CA  1 
ATOM   829   C  C   . ILE A  1 113 ? 20.684 29.236  -24.755  1.00 2.35  ? 113  ILE A C   1 
ATOM   830   O  O   . ILE A  1 113 ? 21.664 29.793  -25.268  1.00 2.00  ? 113  ILE A O   1 
ATOM   831   C  CB  . ILE A  1 113 ? 21.430 27.814  -22.703  1.00 3.10  ? 113  ILE A CB  1 
ATOM   832   C  CG1 . ILE A  1 113 ? 21.237 26.408  -22.069  1.00 3.90  ? 113  ILE A CG1 1 
ATOM   833   C  CG2 . ILE A  1 113 ? 20.783 28.904  -21.795  1.00 3.22  ? 113  ILE A CG2 1 
ATOM   834   C  CD1 . ILE A  1 113 ? 22.036 26.193  -20.788  1.00 7.43  ? 113  ILE A CD1 1 
ATOM   835   N  N   . GLY A  1 114 ? 19.470 29.798  -24.731  1.00 2.00  ? 114  GLY A N   1 
ATOM   836   C  CA  . GLY A  1 114 ? 19.186 31.082  -25.374  1.00 2.12  ? 114  GLY A CA  1 
ATOM   837   C  C   . GLY A  1 114 ? 18.894 31.038  -26.877  1.00 2.00  ? 114  GLY A C   1 
ATOM   838   O  O   . GLY A  1 114 ? 18.674 32.057  -27.503  1.00 2.00  ? 114  GLY A O   1 
ATOM   839   N  N   . ARG A  1 115 ? 18.904 29.843  -27.451  1.00 2.85  ? 115  ARG A N   1 
ATOM   840   C  CA  . ARG A  1 115 ? 18.568 29.655  -28.850  1.00 2.68  ? 115  ARG A CA  1 
ATOM   841   C  C   . ARG A  1 115 ? 17.188 28.975  -28.917  1.00 3.27  ? 115  ARG A C   1 
ATOM   842   O  O   . ARG A  1 115 ? 16.568 28.757  -27.878  1.00 3.67  ? 115  ARG A O   1 
ATOM   843   C  CB  . ARG A  1 115 ? 19.690 28.873  -29.538  1.00 2.00  ? 115  ARG A CB  1 
ATOM   844   C  CG  . ARG A  1 115 ? 21.055 29.601  -29.333  1.00 3.30  ? 115  ARG A CG  1 
ATOM   845   C  CD  . ARG A  1 115 ? 22.150 29.073  -30.280  1.00 6.40  ? 115  ARG A CD  1 
ATOM   846   N  NE  . ARG A  1 115 ? 23.445 29.682  -29.975  1.00 5.51  ? 115  ARG A NE  1 
ATOM   847   C  CZ  . ARG A  1 115 ? 23.924 30.801  -30.532  1.00 7.48  ? 115  ARG A CZ  1 
ATOM   848   N  NH1 . ARG A  1 115 ? 25.120 31.246  -30.157  1.00 8.25  ? 115  ARG A NH1 1 
ATOM   849   N  NH2 . ARG A  1 115 ? 23.256 31.464  -31.477  1.00 2.89  ? 115  ARG A NH2 1 
ATOM   850   N  N   . THR A  1 116 ? 16.696 28.686  -30.108  1.00 3.38  ? 116  THR A N   1 
ATOM   851   C  CA  . THR A  1 116 ? 15.329 28.183  -30.257  1.00 4.21  ? 116  THR A CA  1 
ATOM   852   C  C   . THR A  1 116 ? 15.285 26.749  -30.729  1.00 4.05  ? 116  THR A C   1 
ATOM   853   O  O   . THR A  1 116 ? 15.952 26.417  -31.715  1.00 5.16  ? 116  THR A O   1 
ATOM   854   C  CB  . THR A  1 116 ? 14.552 29.079  -31.259  1.00 4.55  ? 116  THR A CB  1 
ATOM   855   O  OG1 . THR A  1 116 ? 14.416 30.395  -30.708  1.00 5.10  ? 116  THR A OG1 1 
ATOM   856   C  CG2 . THR A  1 116 ? 13.165 28.537  -31.575  1.00 3.25  ? 116  THR A CG2 1 
ATOM   857   N  N   . LEU A  1 117 ? 14.499 25.907  -30.059  1.00 3.57  ? 117  LEU A N   1 
ATOM   858   C  CA  . LEU A  1 117 ? 14.253 24.530  -30.522  1.00 3.38  ? 117  LEU A CA  1 
ATOM   859   C  C   . LEU A  1 117 ? 13.018 24.554  -31.399  1.00 2.60  ? 117  LEU A C   1 
ATOM   860   O  O   . LEU A  1 117 ? 11.989 25.206  -31.023  1.00 2.43  ? 117  LEU A O   1 
ATOM   861   C  CB  . LEU A  1 117 ? 14.026 23.576  -29.335  1.00 2.50  ? 117  LEU A CB  1 
ATOM   862   C  CG  . LEU A  1 117 ? 13.759 22.094  -29.597  1.00 5.79  ? 117  LEU A CG  1 
ATOM   863   C  CD1 . LEU A  1 117 ? 14.998 21.431  -30.207  1.00 7.13  ? 117  LEU A CD1 1 
ATOM   864   C  CD2 . LEU A  1 117 ? 13.368 21.383  -28.281  1.00 4.02  ? 117  LEU A CD2 1 
ATOM   865   N  N   . VAL A  1 118 ? 13.089 23.865  -32.546  1.00 2.11  ? 118  VAL A N   1 
ATOM   866   C  CA  . VAL A  1 118 ? 11.979 23.912  -33.517  1.00 2.00  ? 118  VAL A CA  1 
ATOM   867   C  C   . VAL A  1 118 ? 11.591 22.498  -33.881  1.00 3.28  ? 118  VAL A C   1 
ATOM   868   O  O   . VAL A  1 118 ? 12.476 21.651  -34.069  1.00 3.03  ? 118  VAL A O   1 
ATOM   869   C  CB  . VAL A  1 118 ? 12.350 24.697  -34.803  1.00 2.16  ? 118  VAL A CB  1 
ATOM   870   C  CG1 . VAL A  1 118 ? 11.186 24.673  -35.810  1.00 2.19  ? 118  VAL A CG1 1 
ATOM   871   C  CG2 . VAL A  1 118 ? 12.696 26.153  -34.424  1.00 2.16  ? 118  VAL A CG2 1 
ATOM   872   N  N   . VAL A  1 119 ? 10.283 22.234  -33.937  1.00 2.32  ? 119  VAL A N   1 
ATOM   873   C  CA  . VAL A  1 119 ? 9.801  20.970  -34.517  1.00 2.59  ? 119  VAL A CA  1 
ATOM   874   C  C   . VAL A  1 119 ? 8.981  21.298  -35.765  1.00 2.19  ? 119  VAL A C   1 
ATOM   875   O  O   . VAL A  1 119 ? 8.196  22.265  -35.778  1.00 2.61  ? 119  VAL A O   1 
ATOM   876   C  CB  . VAL A  1 119 ? 9.057  20.047  -33.502  1.00 2.49  ? 119  VAL A CB  1 
ATOM   877   C  CG1 . VAL A  1 119 ? 7.762  20.723  -32.910  1.00 2.00  ? 119  VAL A CG1 1 
ATOM   878   C  CG2 . VAL A  1 119 ? 8.684  18.690  -34.177  1.00 3.12  ? 119  VAL A CG2 1 
ATOM   879   N  N   . HIS A  1 120 ? 9.165  20.481  -36.801  1.00 2.04  ? 120  HIS A N   1 
ATOM   880   C  CA  . HIS A  1 120 ? 8.766  20.803  -38.166  1.00 2.80  ? 120  HIS A CA  1 
ATOM   881   C  C   . HIS A  1 120 ? 7.573  20.008  -38.709  1.00 3.59  ? 120  HIS A C   1 
ATOM   882   O  O   . HIS A  1 120 ? 7.170  19.002  -38.142  1.00 4.70  ? 120  HIS A O   1 
ATOM   883   C  CB  . HIS A  1 120 ? 9.955  20.596  -39.111  1.00 2.36  ? 120  HIS A CB  1 
ATOM   884   C  CG  . HIS A  1 120 ? 10.969 21.696  -39.042  1.00 2.32  ? 120  HIS A CG  1 
ATOM   885   N  ND1 . HIS A  1 120 ? 10.899 22.817  -39.840  1.00 3.09  ? 120  HIS A ND1 1 
ATOM   886   C  CD2 . HIS A  1 120 ? 12.059 21.858  -38.251  1.00 2.82  ? 120  HIS A CD2 1 
ATOM   887   C  CE1 . HIS A  1 120 ? 11.927 23.607  -39.574  1.00 3.45  ? 120  HIS A CE1 1 
ATOM   888   N  NE2 . HIS A  1 120 ? 12.627 23.059  -38.597  1.00 3.47  ? 120  HIS A NE2 1 
ATOM   889   N  N   . GLU A  1 121 ? 7.049  20.502  -39.824  1.00 4.92  ? 121  GLU A N   1 
ATOM   890   C  CA  . GLU A  1 121 ? 5.892  19.964  -40.538  1.00 5.47  ? 121  GLU A CA  1 
ATOM   891   C  C   . GLU A  1 121 ? 6.169  18.582  -41.117  1.00 6.03  ? 121  GLU A C   1 
ATOM   892   O  O   . GLU A  1 121 ? 5.324  17.695  -41.024  1.00 5.20  ? 121  GLU A O   1 
ATOM   893   C  CB  . GLU A  1 121 ? 5.593  20.925  -41.681  1.00 6.66  ? 121  GLU A CB  1 
ATOM   894   C  CG  . GLU A  1 121 ? 4.423  20.553  -42.590  1.00 9.83  ? 121  GLU A CG  1 
ATOM   895   C  CD  . GLU A  1 121 ? 4.343  21.444  -43.843  1.00 14.30 ? 121  GLU A CD  1 
ATOM   896   O  OE1 . GLU A  1 121 ? 3.254  21.448  -44.469  1.00 16.34 ? 121  GLU A OE1 1 
ATOM   897   O  OE2 . GLU A  1 121 ? 5.342  22.132  -44.205  1.00 11.96 ? 121  GLU A OE2 1 
ATOM   898   N  N   . LYS A  1 122 ? 7.350  18.436  -41.723  1.00 6.22  ? 122  LYS A N   1 
ATOM   899   C  CA  . LYS A  1 122 ? 7.738  17.250  -42.513  1.00 7.43  ? 122  LYS A CA  1 
ATOM   900   C  C   . LYS A  1 122 ? 9.009  16.593  -41.974  1.00 6.24  ? 122  LYS A C   1 
ATOM   901   O  O   . LYS A  1 122 ? 9.710  17.154  -41.140  1.00 5.52  ? 122  LYS A O   1 
ATOM   902   C  CB  . LYS A  1 122 ? 8.010  17.638  -43.985  1.00 7.56  ? 122  LYS A CB  1 
ATOM   903   C  CG  . LYS A  1 122 ? 6.924  18.432  -44.660  1.00 11.82 ? 122  LYS A CG  1 
ATOM   904   C  CD  . LYS A  1 122 ? 7.125  18.477  -46.148  1.00 18.72 ? 122  LYS A CD  1 
ATOM   905   C  CE  . LYS A  1 122 ? 7.765  19.776  -46.559  1.00 22.24 ? 122  LYS A CE  1 
ATOM   906   N  NZ  . LYS A  1 122 ? 7.155  20.317  -47.823  1.00 26.36 ? 122  LYS A NZ  1 
ATOM   907   N  N   . ALA A  1 123 ? 9.307  15.395  -42.473  1.00 5.79  ? 123  ALA A N   1 
ATOM   908   C  CA  . ALA A  1 123 ? 10.561 14.724  -42.169  1.00 5.35  ? 123  ALA A CA  1 
ATOM   909   C  C   . ALA A  1 123 ? 11.755 15.566  -42.632  1.00 4.09  ? 123  ALA A C   1 
ATOM   910   O  O   . ALA A  1 123 ? 11.715 16.195  -43.689  1.00 4.42  ? 123  ALA A O   1 
ATOM   911   C  CB  . ALA A  1 123 ? 10.605 13.365  -42.875  1.00 6.61  ? 123  ALA A CB  1 
ATOM   912   N  N   . ASP A  1 124 ? 12.818 15.541  -41.838  1.00 4.22  ? 124  ASP A N   1 
ATOM   913   C  CA  . ASP A  1 124 ? 14.148 16.032  -42.247  1.00 4.59  ? 124  ASP A CA  1 
ATOM   914   C  C   . ASP A  1 124 ? 14.803 14.956  -43.125  1.00 4.36  ? 124  ASP A C   1 
ATOM   915   O  O   . ASP A  1 124 ? 14.964 13.823  -42.672  1.00 4.65  ? 124  ASP A O   1 
ATOM   916   C  CB  . ASP A  1 124 ? 14.957 16.252  -40.970  1.00 3.29  ? 124  ASP A CB  1 
ATOM   917   C  CG  . ASP A  1 124 ? 16.332 16.942  -41.191  1.00 4.66  ? 124  ASP A CG  1 
ATOM   918   O  OD1 . ASP A  1 124 ? 16.950 16.860  -42.278  1.00 4.18  ? 124  ASP A OD1 1 
ATOM   919   O  OD2 . ASP A  1 124 ? 16.816 17.522  -40.200  1.00 5.11  ? 124  ASP A OD2 1 
ATOM   920   N  N   . ASP A  1 125 ? 15.163 15.297  -44.365  1.00 5.51  ? 125  ASP A N   1 
ATOM   921   C  CA  . ASP A  1 125 ? 15.797 14.316  -45.278  1.00 6.26  ? 125  ASP A CA  1 
ATOM   922   C  C   . ASP A  1 125 ? 17.289 14.092  -44.964  1.00 6.23  ? 125  ASP A C   1 
ATOM   923   O  O   . ASP A  1 125 ? 17.975 13.311  -45.646  1.00 5.56  ? 125  ASP A O   1 
ATOM   924   C  CB  . ASP A  1 125 ? 15.542 14.641  -46.779  1.00 6.43  ? 125  ASP A CB  1 
ATOM   925   C  CG  . ASP A  1 125 ? 16.261 15.906  -47.277  1.00 8.27  ? 125  ASP A CG  1 
ATOM   926   O  OD1 . ASP A  1 125 ? 15.885 16.405  -48.367  1.00 9.02  ? 125  ASP A OD1 1 
ATOM   927   O  OD2 . ASP A  1 125 ? 17.204 16.400  -46.620  1.00 10.81 ? 125  ASP A OD2 1 
ATOM   928   N  N   . LEU A  1 126 ? 17.787 14.781  -43.931  1.00 5.72  ? 126  LEU A N   1 
ATOM   929   C  CA  . LEU A  1 126 ? 19.153 14.571  -43.416  1.00 5.25  ? 126  LEU A CA  1 
ATOM   930   C  C   . LEU A  1 126 ? 20.251 14.909  -44.426  1.00 5.69  ? 126  LEU A C   1 
ATOM   931   O  O   . LEU A  1 126 ? 21.387 14.400  -44.339  1.00 5.96  ? 126  LEU A O   1 
ATOM   932   C  CB  . LEU A  1 126 ? 19.298 13.147  -42.863  1.00 5.44  ? 126  LEU A CB  1 
ATOM   933   C  CG  . LEU A  1 126 ? 18.222 12.666  -41.867  1.00 5.61  ? 126  LEU A CG  1 
ATOM   934   C  CD1 . LEU A  1 126 ? 18.578 11.306  -41.310  1.00 8.25  ? 126  LEU A CD1 1 
ATOM   935   C  CD2 . LEU A  1 126 ? 18.025 13.670  -40.670  1.00 6.65  ? 126  LEU A CD2 1 
ATOM   936   N  N   . GLY A  1 127 ? 19.916 15.784  -45.368  1.00 4.41  ? 127  GLY A N   1 
ATOM   937   C  CA  . GLY A  1 127 ? 20.887 16.284  -46.341  1.00 5.82  ? 127  GLY A CA  1 
ATOM   938   C  C   . GLY A  1 127 ? 20.976 15.422  -47.591  1.00 6.98  ? 127  GLY A C   1 
ATOM   939   O  O   . GLY A  1 127 ? 21.806 15.681  -48.464  1.00 7.26  ? 127  GLY A O   1 
ATOM   940   N  N   . LYS A  1 128 ? 20.096 14.419  -47.687  1.00 7.21  ? 128  LYS A N   1 
ATOM   941   C  CA  . LYS A  1 128 ? 20.151 13.411  -48.764  1.00 8.28  ? 128  LYS A CA  1 
ATOM   942   C  C   . LYS A  1 128 ? 19.068 13.564  -49.833  1.00 8.57  ? 128  LYS A C   1 
ATOM   943   O  O   . LYS A  1 128 ? 18.777 12.606  -50.563  1.00 8.79  ? 128  LYS A O   1 
ATOM   944   C  CB  . LYS A  1 128 ? 20.091 11.981  -48.166  1.00 8.79  ? 128  LYS A CB  1 
ATOM   945   C  CG  . LYS A  1 128 ? 21.144 11.711  -47.103  1.00 9.70  ? 128  LYS A CG  1 
ATOM   946   C  CD  . LYS A  1 128 ? 20.801 10.474  -46.283  1.00 13.97 ? 128  LYS A CD  1 
ATOM   947   C  CE  . LYS A  1 128 ? 21.367 9.199   -46.878  1.00 16.15 ? 128  LYS A CE  1 
ATOM   948   N  NZ  . LYS A  1 128 ? 21.095 8.033   -45.958  1.00 19.04 ? 128  LYS A NZ  1 
ATOM   949   N  N   . GLY A  1 129 ? 18.495 14.758  -49.962  1.00 8.15  ? 129  GLY A N   1 
ATOM   950   C  CA  . GLY A  1 129 ? 17.419 14.980  -50.935  1.00 8.69  ? 129  GLY A CA  1 
ATOM   951   C  C   . GLY A  1 129 ? 17.811 15.399  -52.341  1.00 9.40  ? 129  GLY A C   1 
ATOM   952   O  O   . GLY A  1 129 ? 16.947 15.522  -53.211  1.00 8.77  ? 129  GLY A O   1 
ATOM   953   N  N   . GLY A  1 130 ? 19.107 15.657  -52.559  1.00 9.21  ? 130  GLY A N   1 
ATOM   954   C  CA  . GLY A  1 130 ? 19.620 15.949  -53.894  1.00 9.77  ? 130  GLY A CA  1 
ATOM   955   C  C   . GLY A  1 130 ? 19.255 17.316  -54.435  1.00 10.36 ? 130  GLY A C   1 
ATOM   956   O  O   . GLY A  1 130 ? 19.279 17.531  -55.649  1.00 10.83 ? 130  GLY A O   1 
ATOM   957   N  N   . ASN A  1 131 ? 18.895 18.233  -53.534  1.00 10.43 ? 131  ASN A N   1 
ATOM   958   C  CA  . ASN A  1 131 ? 18.686 19.629  -53.885  1.00 10.05 ? 131  ASN A CA  1 
ATOM   959   C  C   . ASN A  1 131 ? 19.401 20.580  -52.893  1.00 9.92  ? 131  ASN A C   1 
ATOM   960   O  O   . ASN A  1 131 ? 19.855 20.157  -51.832  1.00 8.99  ? 131  ASN A O   1 
ATOM   961   C  CB  . ASN A  1 131 ? 17.189 19.962  -54.076  1.00 10.54 ? 131  ASN A CB  1 
ATOM   962   C  CG  . ASN A  1 131 ? 16.370 19.757  -52.833  1.00 10.09 ? 131  ASN A CG  1 
ATOM   963   O  OD1 . ASN A  1 131 ? 16.902 19.681  -51.730  1.00 10.03 ? 131  ASN A OD1 1 
ATOM   964   N  ND2 . ASN A  1 131 ? 15.043 19.650  -53.004  1.00 13.25 ? 131  ASN A ND2 1 
ATOM   965   N  N   . GLU A  1 132 ? 19.537 21.849  -53.261  1.00 10.61 ? 132  GLU A N   1 
ATOM   966   C  CA  . GLU A  1 132 ? 20.217 22.811  -52.393  1.00 11.36 ? 132  GLU A CA  1 
ATOM   967   C  C   . GLU A  1 132 ? 19.546 22.943  -51.012  1.00 10.36 ? 132  GLU A C   1 
ATOM   968   O  O   . GLU A  1 132 ? 20.221 23.022  -49.989  1.00 10.97 ? 132  GLU A O   1 
ATOM   969   C  CB  . GLU A  1 132 ? 20.300 24.185  -53.072  1.00 13.19 ? 132  GLU A CB  1 
ATOM   970   C  CG  . GLU A  1 132 ? 21.207 25.168  -52.299  1.00 17.91 ? 132  GLU A CG  1 
ATOM   971   C  CD  . GLU A  1 132 ? 21.177 26.587  -52.853  1.00 24.45 ? 132  GLU A CD  1 
ATOM   972   O  OE1 . GLU A  1 132 ? 20.670 26.795  -53.988  1.00 27.07 ? 132  GLU A OE1 1 
ATOM   973   O  OE2 . GLU A  1 132 ? 21.678 27.495  -52.148  1.00 26.36 ? 132  GLU A OE2 1 
ATOM   974   N  N   . GLU A  1 133 ? 18.219 22.949  -50.992  1.00 10.07 ? 133  GLU A N   1 
ATOM   975   C  CA  . GLU A  1 133 ? 17.467 23.112  -49.752  1.00 9.80  ? 133  GLU A CA  1 
ATOM   976   C  C   . GLU A  1 133 ? 17.732 21.960  -48.770  1.00 9.29  ? 133  GLU A C   1 
ATOM   977   O  O   . GLU A  1 133 ? 17.783 22.163  -47.547  1.00 9.66  ? 133  GLU A O   1 
ATOM   978   C  CB  . GLU A  1 133 ? 15.975 23.325  -50.064  1.00 10.08 ? 133  GLU A CB  1 
ATOM   979   C  CG  . GLU A  1 133 ? 15.123 23.658  -48.852  1.00 11.57 ? 133  GLU A CG  1 
ATOM   980   C  CD  . GLU A  1 133 ? 15.341 25.067  -48.312  1.00 11.60 ? 133  GLU A CD  1 
ATOM   981   O  OE1 . GLU A  1 133 ? 14.407 25.625  -47.694  1.00 12.82 ? 133  GLU A OE1 1 
ATOM   982   O  OE2 . GLU A  1 133 ? 16.439 25.624  -48.468  1.00 14.85 ? 133  GLU A OE2 1 
ATOM   983   N  N   . SER A  1 134 ? 17.968 20.762  -49.304  1.00 8.64  ? 134  SER A N   1 
ATOM   984   C  CA  . SER A  1 134 ? 18.352 19.612  -48.468  1.00 8.04  ? 134  SER A CA  1 
ATOM   985   C  C   . SER A  1 134 ? 19.618 19.868  -47.640  1.00 7.77  ? 134  SER A C   1 
ATOM   986   O  O   . SER A  1 134 ? 19.700 19.446  -46.486  1.00 7.15  ? 134  SER A O   1 
ATOM   987   C  CB  . SER A  1 134 ? 18.531 18.345  -49.325  1.00 8.32  ? 134  SER A CB  1 
ATOM   988   O  OG  . SER A  1 134 ? 18.927 17.241  -48.526  1.00 6.62  ? 134  SER A OG  1 
ATOM   989   N  N   . THR A  1 135 ? 20.579 20.572  -48.239  1.00 8.02  ? 135  THR A N   1 
ATOM   990   C  CA  . THR A  1 135 ? 21.849 20.969  -47.577  1.00 9.50  ? 135  THR A CA  1 
ATOM   991   C  C   . THR A  1 135 ? 21.707 22.158  -46.617  1.00 9.48  ? 135  THR A C   1 
ATOM   992   O  O   . THR A  1 135 ? 22.700 22.589  -46.012  1.00 9.36  ? 135  THR A O   1 
ATOM   993   C  CB  . THR A  1 135 ? 22.935 21.367  -48.615  1.00 9.42  ? 135  THR A CB  1 
ATOM   994   O  OG1 . THR A  1 135 ? 22.717 22.729  -49.056  1.00 12.36 ? 135  THR A OG1 1 
ATOM   995   C  CG2 . THR A  1 135 ? 22.923 20.441  -49.796  1.00 11.82 ? 135  THR A CG2 1 
ATOM   996   N  N   . LYS A  1 136 ? 20.494 22.698  -46.490  1.00 9.23  ? 136  LYS A N   1 
ATOM   997   C  CA  . LYS A  1 136 ? 20.258 23.837  -45.595  1.00 9.41  ? 136  LYS A CA  1 
ATOM   998   C  C   . LYS A  1 136 ? 19.256 23.534  -44.490  1.00 8.81  ? 136  LYS A C   1 
ATOM   999   O  O   . LYS A  1 136 ? 19.538 23.774  -43.310  1.00 7.92  ? 136  LYS A O   1 
ATOM   1000  C  CB  . LYS A  1 136 ? 19.819 25.055  -46.404  1.00 9.89  ? 136  LYS A CB  1 
ATOM   1001  C  CG  . LYS A  1 136 ? 20.932 25.620  -47.296  1.00 12.52 ? 136  LYS A CG  1 
ATOM   1002  C  CD  . LYS A  1 136 ? 20.531 26.938  -47.906  1.00 16.42 ? 136  LYS A CD  1 
ATOM   1003  C  CE  . LYS A  1 136 ? 21.759 27.624  -48.505  1.00 19.61 ? 136  LYS A CE  1 
ATOM   1004  N  NZ  . LYS A  1 136 ? 21.348 28.475  -49.634  1.00 23.27 ? 136  LYS A NZ  1 
ATOM   1005  N  N   . THR A  1 137 ? 18.105 22.970  -44.868  1.00 7.59  ? 137  THR A N   1 
ATOM   1006  C  CA  . THR A  1 137 ? 16.984 22.727  -43.944  1.00 7.32  ? 137  THR A CA  1 
ATOM   1007  C  C   . THR A  1 137 ? 16.574 21.254  -43.866  1.00 7.13  ? 137  THR A C   1 
ATOM   1008  O  O   . THR A  1 137 ? 15.768 20.863  -43.011  1.00 6.73  ? 137  THR A O   1 
ATOM   1009  C  CB  . THR A  1 137 ? 15.734 23.516  -44.392  1.00 7.53  ? 137  THR A CB  1 
ATOM   1010  O  OG1 . THR A  1 137 ? 15.244 22.970  -45.634  1.00 6.46  ? 137  THR A OG1 1 
ATOM   1011  C  CG2 . THR A  1 137 ? 16.078 24.967  -44.622  1.00 7.59  ? 137  THR A CG2 1 
ATOM   1012  N  N   . GLY A  1 138 ? 17.082 20.437  -44.786  1.00 6.43  ? 138  GLY A N   1 
ATOM   1013  C  CA  . GLY A  1 138 ? 16.678 19.027  -44.804  1.00 6.07  ? 138  GLY A CA  1 
ATOM   1014  C  C   . GLY A  1 138 ? 15.288 18.848  -45.404  1.00 6.14  ? 138  GLY A C   1 
ATOM   1015  O  O   . GLY A  1 138 ? 14.669 17.788  -45.274  1.00 5.41  ? 138  GLY A O   1 
ATOM   1016  N  N   . ASN A  1 139 ? 14.802 19.907  -46.036  1.00 6.65  ? 139  ASN A N   1 
ATOM   1017  C  CA  . ASN A  1 139 ? 13.437 19.972  -46.584  1.00 7.00  ? 139  ASN A CA  1 
ATOM   1018  C  C   . ASN A  1 139 ? 12.355 19.646  -45.559  1.00 6.39  ? 139  ASN A C   1 
ATOM   1019  O  O   . ASN A  1 139 ? 11.363 18.984  -45.880  1.00 6.98  ? 139  ASN A O   1 
ATOM   1020  C  CB  . ASN A  1 139 ? 13.292 19.095  -47.844  1.00 7.50  ? 139  ASN A CB  1 
ATOM   1021  C  CG  . ASN A  1 139 ? 14.104 19.607  -49.012  1.00 9.15  ? 139  ASN A CG  1 
ATOM   1022  O  OD1 . ASN A  1 139 ? 13.856 20.699  -49.563  1.00 9.81  ? 139  ASN A OD1 1 
ATOM   1023  N  ND2 . ASN A  1 139 ? 15.096 18.823  -49.400  1.00 7.00  ? 139  ASN A ND2 1 
ATOM   1024  N  N   . ALA A  1 140 ? 12.543 20.145  -44.332  1.00 6.30  ? 140  ALA A N   1 
ATOM   1025  C  CA  . ALA A  1 140 ? 11.662 19.805  -43.213  1.00 6.45  ? 140  ALA A CA  1 
ATOM   1026  C  C   . ALA A  1 140 ? 10.367 20.613  -43.191  1.00 6.24  ? 140  ALA A C   1 
ATOM   1027  O  O   . ALA A  1 140 ? 9.506  20.359  -42.361  1.00 7.28  ? 140  ALA A O   1 
ATOM   1028  C  CB  . ALA A  1 140 ? 12.403 19.947  -41.893  1.00 5.41  ? 140  ALA A CB  1 
ATOM   1029  N  N   . GLY A  1 141 ? 10.224 21.558  -44.114  1.00 6.59  ? 141  GLY A N   1 
ATOM   1030  C  CA  . GLY A  1 141 ? 8.994  22.357  -44.247  1.00 6.67  ? 141  GLY A CA  1 
ATOM   1031  C  C   . GLY A  1 141 ? 8.802  23.309  -43.079  1.00 6.85  ? 141  GLY A C   1 
ATOM   1032  O  O   . GLY A  1 141 ? 9.771  23.674  -42.400  1.00 6.55  ? 141  GLY A O   1 
ATOM   1033  N  N   . SER A  1 142 ? 7.558  23.685  -42.814  1.00 5.82  ? 142  SER A N   1 
ATOM   1034  C  CA  . SER A  1 142 ? 7.278  24.761  -41.858  1.00 6.33  ? 142  SER A CA  1 
ATOM   1035  C  C   . SER A  1 142 ? 7.573  24.422  -40.389  1.00 5.83  ? 142  SER A C   1 
ATOM   1036  O  O   . SER A  1 142 ? 7.739  23.256  -40.002  1.00 5.36  ? 142  SER A O   1 
ATOM   1037  C  CB  . SER A  1 142 ? 5.826  25.256  -42.017  1.00 7.09  ? 142  SER A CB  1 
ATOM   1038  O  OG  . SER A  1 142 ? 4.953  24.351  -41.368  1.00 8.58  ? 142  SER A OG  1 
ATOM   1039  N  N   . ARG A  1 143 ? 7.635  25.467  -39.583  1.00 5.64  ? 143  ARG A N   1 
ATOM   1040  C  CA  . ARG A  1 143 ? 7.977  25.376  -38.177  1.00 5.79  ? 143  ARG A CA  1 
ATOM   1041  C  C   . ARG A  1 143 ? 6.670  25.340  -37.401  1.00 6.37  ? 143  ARG A C   1 
ATOM   1042  O  O   . ARG A  1 143 ? 6.004  26.375  -37.256  1.00 7.07  ? 143  ARG A O   1 
ATOM   1043  C  CB  . ARG A  1 143 ? 8.787  26.630  -37.808  1.00 6.20  ? 143  ARG A CB  1 
ATOM   1044  C  CG  . ARG A  1 143 ? 10.008 26.762  -38.667  1.00 5.82  ? 143  ARG A CG  1 
ATOM   1045  C  CD  . ARG A  1 143 ? 10.840 28.030  -38.353  1.00 6.59  ? 143  ARG A CD  1 
ATOM   1046  N  NE  . ARG A  1 143 ? 11.913 28.153  -39.345  1.00 5.55  ? 143  ARG A NE  1 
ATOM   1047  C  CZ  . ARG A  1 143 ? 13.000 28.921  -39.192  1.00 7.01  ? 143  ARG A CZ  1 
ATOM   1048  N  NH1 . ARG A  1 143 ? 13.917 28.955  -40.148  1.00 4.42  ? 143  ARG A NH1 1 
ATOM   1049  N  NH2 . ARG A  1 143 ? 13.181 29.627  -38.076  1.00 5.11  ? 143  ARG A NH2 1 
ATOM   1050  N  N   . LEU A  1 144 ? 6.277  24.159  -36.947  1.00 4.68  ? 144  LEU A N   1 
ATOM   1051  C  CA  . LEU A  1 144 ? 4.986  24.001  -36.275  1.00 4.54  ? 144  LEU A CA  1 
ATOM   1052  C  C   . LEU A  1 144 ? 4.962  24.530  -34.842  1.00 3.93  ? 144  LEU A C   1 
ATOM   1053  O  O   . LEU A  1 144 ? 3.923  24.997  -34.378  1.00 3.44  ? 144  LEU A O   1 
ATOM   1054  C  CB  . LEU A  1 144 ? 4.532  22.558  -36.279  1.00 4.35  ? 144  LEU A CB  1 
ATOM   1055  C  CG  . LEU A  1 144 ? 4.447  21.886  -37.642  1.00 4.41  ? 144  LEU A CG  1 
ATOM   1056  C  CD1 . LEU A  1 144 ? 3.880  20.502  -37.401  1.00 8.97  ? 144  LEU A CD1 1 
ATOM   1057  C  CD2 . LEU A  1 144 ? 3.595  22.653  -38.656  1.00 5.49  ? 144  LEU A CD2 1 
ATOM   1058  N  N   . ALA A  1 145 ? 6.095  24.465  -34.155  1.00 3.39  ? 145  ALA A N   1 
ATOM   1059  C  CA  . ALA A  1 145 ? 6.165  24.904  -32.754  1.00 2.82  ? 145  ALA A CA  1 
ATOM   1060  C  C   . ALA A  1 145 ? 7.612  25.174  -32.411  1.00 2.48  ? 145  ALA A C   1 
ATOM   1061  O  O   . ALA A  1 145 ? 8.527  24.581  -33.010  1.00 2.00  ? 145  ALA A O   1 
ATOM   1062  C  CB  . ALA A  1 145 ? 5.587  23.839  -31.783  1.00 3.73  ? 145  ALA A CB  1 
ATOM   1063  N  N   . CYS A  1 146 ? 7.827  26.064  -31.459  1.00 2.00  ? 146  CYS A N   1 
ATOM   1064  C  CA  . CYS A  1 146 ? 9.200  26.386  -31.077  1.00 2.00  ? 146  CYS A CA  1 
ATOM   1065  C  C   . CYS A  1 146 ? 9.212  26.978  -29.695  1.00 2.18  ? 146  CYS A C   1 
ATOM   1066  O  O   . CYS A  1 146 ? 8.146  27.270  -29.100  1.00 2.12  ? 146  CYS A O   1 
ATOM   1067  C  CB  . CYS A  1 146 ? 9.836  27.363  -32.072  0.40 2.00  ? 146  CYS A CB  1 
ATOM   1068  S  SG  . CYS A  1 146 ? 8.926  28.897  -32.242  0.40 2.00  ? 146  CYS A SG  1 
ATOM   1069  N  N   . GLY A  1 147 ? 10.414 27.201  -29.178  1.00 2.00  ? 147  GLY A N   1 
ATOM   1070  C  CA  . GLY A  1 147 ? 10.529 27.702  -27.822  1.00 2.03  ? 147  GLY A CA  1 
ATOM   1071  C  C   . GLY A  1 147 ? 11.969 28.060  -27.603  1.00 2.40  ? 147  GLY A C   1 
ATOM   1072  O  O   . GLY A  1 147 ? 12.853 27.482  -28.240  1.00 2.00  ? 147  GLY A O   1 
ATOM   1073  N  N   . VAL A  1 148 ? 12.207 29.034  -26.731  1.00 2.23  ? 148  VAL A N   1 
ATOM   1074  C  CA  . VAL A  1 148 ? 13.591 29.378  -26.371  1.00 2.00  ? 148  VAL A CA  1 
ATOM   1075  C  C   . VAL A  1 148 ? 14.085 28.413  -25.307  1.00 2.00  ? 148  VAL A C   1 
ATOM   1076  O  O   . VAL A  1 148 ? 13.387 28.115  -24.330  1.00 2.00  ? 148  VAL A O   1 
ATOM   1077  C  CB  . VAL A  1 148 ? 13.705 30.841  -25.877  1.00 2.00  ? 148  VAL A CB  1 
ATOM   1078  C  CG1 . VAL A  1 148 ? 15.180 31.222  -25.573  1.00 2.00  ? 148  VAL A CG1 1 
ATOM   1079  C  CG2 . VAL A  1 148 ? 13.085 31.784  -26.911  1.00 3.42  ? 148  VAL A CG2 1 
ATOM   1080  N  N   . ILE A  1 149 ? 15.306 27.940  -25.483  1.00 2.00  ? 149  ILE A N   1 
ATOM   1081  C  CA  . ILE A  1 149 ? 15.903 26.988  -24.547  1.00 2.00  ? 149  ILE A CA  1 
ATOM   1082  C  C   . ILE A  1 149 ? 16.452 27.717  -23.326  1.00 2.09  ? 149  ILE A C   1 
ATOM   1083  O  O   . ILE A  1 149 ? 17.357 28.587  -23.461  1.00 3.05  ? 149  ILE A O   1 
ATOM   1084  C  CB  . ILE A  1 149 ? 17.035 26.182  -25.243  1.00 2.00  ? 149  ILE A CB  1 
ATOM   1085  C  CG1 . ILE A  1 149 ? 16.459 25.398  -26.433  1.00 2.15  ? 149  ILE A CG1 1 
ATOM   1086  C  CG2 . ILE A  1 149 ? 17.754 25.307  -24.234  1.00 2.00  ? 149  ILE A CG2 1 
ATOM   1087  C  CD1 . ILE A  1 149 ? 17.560 24.949  -27.450  1.00 2.05  ? 149  ILE A CD1 1 
ATOM   1088  N  N   . GLY A  1 150 ? 15.891 27.406  -22.153  1.00 2.00  ? 150  GLY A N   1 
ATOM   1089  C  CA  . GLY A  1 150 ? 16.238 28.136  -20.925  1.00 3.15  ? 150  GLY A CA  1 
ATOM   1090  C  C   . GLY A  1 150 ? 17.029 27.316  -19.936  1.00 3.58  ? 150  GLY A C   1 
ATOM   1091  O  O   . GLY A  1 150 ? 16.941 26.095  -19.930  1.00 4.03  ? 150  GLY A O   1 
ATOM   1092  N  N   . ILE A  1 151 ? 17.798 27.974  -19.074  1.00 4.39  ? 151  ILE A N   1 
ATOM   1093  C  CA  . ILE A  1 151 ? 18.481 27.236  -18.009  1.00 4.34  ? 151  ILE A CA  1 
ATOM   1094  C  C   . ILE A  1 151 ? 17.469 26.715  -16.994  1.00 4.27  ? 151  ILE A C   1 
ATOM   1095  O  O   . ILE A  1 151 ? 16.531 27.409  -16.612  1.00 3.41  ? 151  ILE A O   1 
ATOM   1096  C  CB  . ILE A  1 151 ? 19.622 28.051  -17.360  1.00 4.50  ? 151  ILE A CB  1 
ATOM   1097  C  CG1 . ILE A  1 151 ? 20.411 27.189  -16.357  1.00 6.98  ? 151  ILE A CG1 1 
ATOM   1098  C  CG2 . ILE A  1 151 ? 19.083 29.255  -16.649  1.00 5.91  ? 151  ILE A CG2 1 
ATOM   1099  C  CD1 . ILE A  1 151 ? 21.869 27.662  -16.156  1.00 10.85 ? 151  ILE A CD1 1 
ATOM   1100  N  N   . ALA A  1 152 ? 17.624 25.462  -16.594  1.00 4.77  ? 152  ALA A N   1 
ATOM   1101  C  CA  . ALA A  1 152 ? 16.673 24.845  -15.667  1.00 5.84  ? 152  ALA A CA  1 
ATOM   1102  C  C   . ALA A  1 152 ? 17.342 24.559  -14.335  1.00 6.86  ? 152  ALA A C   1 
ATOM   1103  O  O   . ALA A  1 152 ? 18.555 24.390  -14.286  1.00 7.55  ? 152  ALA A O   1 
ATOM   1104  C  CB  . ALA A  1 152 ? 16.059 23.551  -16.291  1.00 5.75  ? 152  ALA A CB  1 
ATOM   1105  N  N   . GLN A  1 153 ? 16.559 24.501  -13.256  1.00 9.28  ? 153  GLN A N   1 
ATOM   1106  C  CA  . GLN A  1 153 ? 17.098 24.173  -11.923  1.00 12.07 ? 153  GLN A CA  1 
ATOM   1107  C  C   . GLN A  1 153 ? 17.733 22.793  -11.889  1.00 13.29 ? 153  GLN A C   1 
ATOM   1108  O  O   . GLN A  1 153 ? 17.180 21.825  -12.417  1.00 13.95 ? 153  GLN A O   1 
ATOM   1109  C  CB  . GLN A  1 153 ? 16.012 24.261  -10.837  1.00 12.30 ? 153  GLN A CB  1 
ATOM   1110  C  CG  . GLN A  1 153 ? 16.535 24.102  -9.401   1.00 15.25 ? 153  GLN A CG  1 
ATOM   1111  C  CD  . GLN A  1 153 ? 15.485 24.403  -8.348   1.00 18.01 ? 153  GLN A CD  1 
ATOM   1112  O  OE1 . GLN A  1 153 ? 15.798 24.933  -7.288   1.00 23.58 ? 153  GLN A OE1 1 
ATOM   1113  N  NE2 . GLN A  1 153 ? 14.235 24.070  -8.637   1.00 18.99 ? 153  GLN A NE2 1 
ATOM   1114  O  OXT . GLN A  1 153 ? 18.827 22.649  -11.321  1.00 15.24 ? 153  GLN A OXT 1 
ATOM   1115  N  N   . ALA B  1 1   ? 28.821 43.982  -31.047  1.00 17.11 ? 1    ALA B N   1 
ATOM   1116  C  CA  . ALA B  1 1   ? 27.948 43.977  -29.848  1.00 15.92 ? 1    ALA B CA  1 
ATOM   1117  C  C   . ALA B  1 1   ? 27.269 42.610  -29.663  1.00 15.31 ? 1    ALA B C   1 
ATOM   1118  O  O   . ALA B  1 1   ? 27.330 41.754  -30.537  1.00 16.21 ? 1    ALA B O   1 
ATOM   1119  C  CB  . ALA B  1 1   ? 26.896 45.077  -29.977  1.00 16.58 ? 1    ALA B CB  1 
ATOM   1120  N  N   . THR B  1 2   ? 26.636 42.415  -28.513  1.00 12.98 ? 2    THR B N   1 
ATOM   1121  C  CA  . THR B  1 2   ? 25.812 41.247  -28.265  1.00 11.04 ? 2    THR B CA  1 
ATOM   1122  C  C   . THR B  1 2   ? 24.402 41.779  -28.107  1.00 8.86  ? 2    THR B C   1 
ATOM   1123  O  O   . THR B  1 2   ? 24.200 42.844  -27.540  1.00 7.64  ? 2    THR B O   1 
ATOM   1124  C  CB  . THR B  1 2   ? 26.247 40.530  -26.980  1.00 11.41 ? 2    THR B CB  1 
ATOM   1125  O  OG1 . THR B  1 2   ? 27.632 40.203  -27.084  1.00 14.80 ? 2    THR B OG1 1 
ATOM   1126  C  CG2 . THR B  1 2   ? 25.440 39.249  -26.758  1.00 11.13 ? 2    THR B CG2 1 
ATOM   1127  N  N   . LYS B  1 3   ? 23.427 41.027  -28.603  1.00 7.24  ? 3    LYS B N   1 
ATOM   1128  C  CA  . LYS B  1 3   ? 22.032 41.427  -28.579  1.00 6.53  ? 3    LYS B CA  1 
ATOM   1129  C  C   . LYS B  1 3   ? 21.183 40.255  -28.078  1.00 5.53  ? 3    LYS B C   1 
ATOM   1130  O  O   . LYS B  1 3   ? 21.497 39.084  -28.359  1.00 5.11  ? 3    LYS B O   1 
ATOM   1131  C  CB  . LYS B  1 3   ? 21.563 41.816  -29.990  1.00 7.89  ? 3    LYS B CB  1 
ATOM   1132  C  CG  . LYS B  1 3   ? 22.033 43.236  -30.448  1.00 11.37 ? 3    LYS B CG  1 
ATOM   1133  C  CD  . LYS B  1 3   ? 21.699 43.539  -31.920  1.00 17.69 ? 3    LYS B CD  1 
ATOM   1134  C  CE  . LYS B  1 3   ? 20.192 43.681  -32.216  1.00 22.43 ? 3    LYS B CE  1 
ATOM   1135  N  NZ  . LYS B  1 3   ? 19.516 44.972  -31.812  1.00 25.64 ? 3    LYS B NZ  1 
ATOM   1136  N  N   . ALA B  1 4   ? 20.133 40.581  -27.331  1.00 3.91  ? 4    ALA B N   1 
ATOM   1137  C  CA  . ALA B  1 4   ? 19.179 39.597  -26.850  1.00 2.20  ? 4    ALA B CA  1 
ATOM   1138  C  C   . ALA B  1 4   ? 17.761 40.165  -26.964  1.00 2.84  ? 4    ALA B C   1 
ATOM   1139  O  O   . ALA B  1 4   ? 17.562 41.359  -27.199  1.00 2.00  ? 4    ALA B O   1 
ATOM   1140  C  CB  . ALA B  1 4   ? 19.519 39.165  -25.433  1.00 2.15  ? 4    ALA B CB  1 
ATOM   1141  N  N   . VAL B  1 5   ? 16.758 39.306  -26.827  1.00 3.73  ? 5    VAL B N   1 
ATOM   1142  C  CA  . VAL B  1 5   ? 15.379 39.763  -26.939  1.00 3.63  ? 5    VAL B CA  1 
ATOM   1143  C  C   . VAL B  1 5   ? 14.510 38.865  -26.060  1.00 3.78  ? 5    VAL B C   1 
ATOM   1144  O  O   . VAL B  1 5   ? 14.898 37.727  -25.793  1.00 3.99  ? 5    VAL B O   1 
ATOM   1145  C  CB  . VAL B  1 5   ? 14.901 39.711  -28.419  1.00 3.85  ? 5    VAL B CB  1 
ATOM   1146  C  CG1 . VAL B  1 5   ? 14.914 38.241  -28.946  1.00 4.13  ? 5    VAL B CG1 1 
ATOM   1147  C  CG2 . VAL B  1 5   ? 13.500 40.318  -28.566  1.00 4.13  ? 5    VAL B CG2 1 
ATOM   1148  N  N   . CYS B  1 6   ? 13.350 39.368  -25.624  1.00 2.62  ? 6    CYS B N   1 
ATOM   1149  C  CA  . CYS B  1 6   ? 12.448 38.617  -24.766  1.00 4.30  ? 6    CYS B CA  1 
ATOM   1150  C  C   . CYS B  1 6   ? 11.027 38.960  -25.155  1.00 3.96  ? 6    CYS B C   1 
ATOM   1151  O  O   . CYS B  1 6   ? 10.670 40.151  -25.231  1.00 4.47  ? 6    CYS B O   1 
ATOM   1152  C  CB  . CYS B  1 6   ? 12.680 38.949  -23.277  1.00 4.06  ? 6    CYS B CB  1 
ATOM   1153  S  SG  . CYS B  1 6   ? 11.653 37.924  -22.218  1.00 6.92  ? 6    CYS B SG  1 
ATOM   1154  N  N   . VAL B  1 7   ? 10.227 37.932  -25.422  1.00 3.58  ? 7    VAL B N   1 
ATOM   1155  C  CA  . VAL B  1 7   ? 8.797  38.115  -25.656  1.00 4.36  ? 7    VAL B CA  1 
ATOM   1156  C  C   . VAL B  1 7   ? 8.054  37.812  -24.363  1.00 5.08  ? 7    VAL B C   1 
ATOM   1157  O  O   . VAL B  1 7   ? 8.149  36.706  -23.840  1.00 4.92  ? 7    VAL B O   1 
ATOM   1158  C  CB  . VAL B  1 7   ? 8.281  37.210  -26.782  1.00 4.73  ? 7    VAL B CB  1 
ATOM   1159  C  CG1 . VAL B  1 7   ? 6.757  37.244  -26.845  1.00 5.48  ? 7    VAL B CG1 1 
ATOM   1160  C  CG2 . VAL B  1 7   ? 8.910  37.619  -28.108  1.00 4.34  ? 7    VAL B CG2 1 
ATOM   1161  N  N   . LEU B  1 8   ? 7.360  38.812  -23.820  1.00 5.11  ? 8    LEU B N   1 
ATOM   1162  C  CA  . LEU B  1 8   ? 6.709  38.657  -22.535  1.00 5.50  ? 8    LEU B CA  1 
ATOM   1163  C  C   . LEU B  1 8   ? 5.274  38.244  -22.786  1.00 5.48  ? 8    LEU B C   1 
ATOM   1164  O  O   . LEU B  1 8   ? 4.573  38.917  -23.510  1.00 5.57  ? 8    LEU B O   1 
ATOM   1165  C  CB  . LEU B  1 8   ? 6.732  39.983  -21.754  1.00 5.65  ? 8    LEU B CB  1 
ATOM   1166  C  CG  . LEU B  1 8   ? 8.122  40.485  -21.309  1.00 6.04  ? 8    LEU B CG  1 
ATOM   1167  C  CD1 . LEU B  1 8   ? 8.028  41.913  -20.764  1.00 5.32  ? 8    LEU B CD1 1 
ATOM   1168  C  CD2 . LEU B  1 8   ? 8.722  39.575  -20.247  1.00 5.34  ? 8    LEU B CD2 1 
ATOM   1169  N  N   . LYS B  1 9   ? 4.844  37.147  -22.176  1.00 6.57  ? 9    LYS B N   1 
ATOM   1170  C  CA  . LYS B  1 9   ? 3.469  36.675  -22.331  1.00 8.06  ? 9    LYS B CA  1 
ATOM   1171  C  C   . LYS B  1 9   ? 2.974  36.124  -21.013  1.00 7.65  ? 9    LYS B C   1 
ATOM   1172  O  O   . LYS B  1 9   ? 3.767  35.612  -20.239  1.00 7.09  ? 9    LYS B O   1 
ATOM   1173  C  CB  . LYS B  1 9   ? 3.408  35.557  -23.387  1.00 8.53  ? 9    LYS B CB  1 
ATOM   1174  C  CG  . LYS B  1 9   ? 3.702  35.983  -24.825  1.00 11.76 ? 9    LYS B CG  1 
ATOM   1175  C  CD  . LYS B  1 9   ? 2.617  36.872  -25.425  1.00 16.50 ? 9    LYS B CD  1 
ATOM   1176  C  CE  . LYS B  1 9   ? 1.955  36.211  -26.651  1.00 19.73 ? 9    LYS B CE  1 
ATOM   1177  N  NZ  . LYS B  1 9   ? 2.979  35.884  -27.713  1.00 21.03 ? 9    LYS B NZ  1 
ATOM   1178  N  N   . GLY B  1 10  ? 1.657  36.177  -20.782  1.00 8.02  ? 10   GLY B N   1 
ATOM   1179  C  CA  . GLY B  1 10  ? 1.070  35.676  -19.534  1.00 9.65  ? 10   GLY B CA  1 
ATOM   1180  C  C   . GLY B  1 10  ? -0.347 35.161  -19.754  1.00 11.38 ? 10   GLY B C   1 
ATOM   1181  O  O   . GLY B  1 10  ? -0.751 34.929  -20.893  1.00 11.80 ? 10   GLY B O   1 
ATOM   1182  N  N   . ASP B  1 11  ? -1.077 34.975  -18.666  1.00 12.35 ? 11   ASP B N   1 
ATOM   1183  C  CA  . ASP B  1 11  ? -2.444 34.424  -18.722  1.00 13.94 ? 11   ASP B CA  1 
ATOM   1184  C  C   . ASP B  1 11  ? -3.510 35.494  -18.933  1.00 13.82 ? 11   ASP B C   1 
ATOM   1185  O  O   . ASP B  1 11  ? -4.674 35.163  -19.214  1.00 14.87 ? 11   ASP B O   1 
ATOM   1186  C  CB  . ASP B  1 11  ? -2.752 33.682  -17.431  1.00 14.80 ? 11   ASP B CB  1 
ATOM   1187  C  CG  . ASP B  1 11  ? -1.930 32.430  -17.268  1.00 17.31 ? 11   ASP B CG  1 
ATOM   1188  O  OD1 . ASP B  1 11  ? -1.695 32.067  -16.102  1.00 21.71 ? 11   ASP B OD1 1 
ATOM   1189  O  OD2 . ASP B  1 11  ? -1.513 31.821  -18.286  1.00 20.04 ? 11   ASP B OD2 1 
ATOM   1190  N  N   . GLY B  1 12  ? -3.115 36.760  -18.785  1.00 13.17 ? 12   GLY B N   1 
ATOM   1191  C  CA  . GLY B  1 12  ? -4.021 37.915  -18.908  1.00 12.07 ? 12   GLY B CA  1 
ATOM   1192  C  C   . GLY B  1 12  ? -3.685 38.750  -20.129  1.00 10.57 ? 12   GLY B C   1 
ATOM   1193  O  O   . GLY B  1 12  ? -3.118 38.224  -21.087  1.00 10.57 ? 12   GLY B O   1 
ATOM   1194  N  N   . PRO B  1 13  ? -3.994 40.063  -20.087  1.00 9.43  ? 13   PRO B N   1 
ATOM   1195  C  CA  . PRO B  1 13  ? -3.750 40.968  -21.190  1.00 8.96  ? 13   PRO B CA  1 
ATOM   1196  C  C   . PRO B  1 13  ? -2.306 41.478  -21.308  1.00 8.15  ? 13   PRO B C   1 
ATOM   1197  O  O   . PRO B  1 13  ? -1.968 42.104  -22.296  1.00 8.32  ? 13   PRO B O   1 
ATOM   1198  C  CB  . PRO B  1 13  ? -4.701 42.136  -20.882  1.00 8.46  ? 13   PRO B CB  1 
ATOM   1199  C  CG  . PRO B  1 13  ? -4.728 42.186  -19.407  1.00 8.28  ? 13   PRO B CG  1 
ATOM   1200  C  CD  . PRO B  1 13  ? -4.724 40.736  -18.994  1.00 9.64  ? 13   PRO B CD  1 
ATOM   1201  N  N   . VAL B  1 14  ? -1.461 41.222  -20.319  1.00 7.88  ? 14   VAL B N   1 
ATOM   1202  C  CA  . VAL B  1 14  ? -0.107 41.787  -20.359  1.00 6.68  ? 14   VAL B CA  1 
ATOM   1203  C  C   . VAL B  1 14  ? 0.775  41.091  -21.411  1.00 6.57  ? 14   VAL B C   1 
ATOM   1204  O  O   . VAL B  1 14  ? 0.948  39.875  -21.392  1.00 7.10  ? 14   VAL B O   1 
ATOM   1205  C  CB  . VAL B  1 14  ? 0.551  41.746  -18.975  1.00 6.81  ? 14   VAL B CB  1 
ATOM   1206  C  CG1 . VAL B  1 14  ? 1.949  42.345  -19.043  1.00 6.12  ? 14   VAL B CG1 1 
ATOM   1207  C  CG2 . VAL B  1 14  ? -0.339 42.484  -17.917  1.00 6.18  ? 14   VAL B CG2 1 
ATOM   1208  N  N   . GLN B  1 15  ? 1.344  41.869  -22.315  1.00 6.10  ? 15   GLN B N   1 
ATOM   1209  C  CA  . GLN B  1 15  ? 2.275  41.326  -23.309  1.00 7.44  ? 15   GLN B CA  1 
ATOM   1210  C  C   . GLN B  1 15  ? 3.222  42.397  -23.784  1.00 6.67  ? 15   GLN B C   1 
ATOM   1211  O  O   . GLN B  1 15  ? 2.879  43.576  -23.817  1.00 6.54  ? 15   GLN B O   1 
ATOM   1212  C  CB  . GLN B  1 15  ? 1.554  40.716  -24.514  1.00 7.69  ? 15   GLN B CB  1 
ATOM   1213  C  CG  . GLN B  1 15  ? 0.519  41.611  -25.128  1.00 11.84 ? 15   GLN B CG  1 
ATOM   1214  C  CD  . GLN B  1 15  ? -0.262 40.932  -26.249  1.00 17.01 ? 15   GLN B CD  1 
ATOM   1215  O  OE1 . GLN B  1 15  ? -1.486 41.015  -26.295  1.00 21.05 ? 15   GLN B OE1 1 
ATOM   1216  N  NE2 . GLN B  1 15  ? 0.442  40.257  -27.145  1.00 17.54 ? 15   GLN B NE2 1 
ATOM   1217  N  N   . GLY B  1 16  ? 4.425  42.000  -24.164  1.00 6.61  ? 16   GLY B N   1 
ATOM   1218  C  CA  . GLY B  1 16  ? 5.325  42.993  -24.731  1.00 6.50  ? 16   GLY B CA  1 
ATOM   1219  C  C   . GLY B  1 16  ? 6.575  42.362  -25.271  1.00 7.07  ? 16   GLY B C   1 
ATOM   1220  O  O   . GLY B  1 16  ? 6.718  41.142  -25.263  1.00 5.28  ? 16   GLY B O   1 
ATOM   1221  N  N   . ILE B  1 17  ? 7.467  43.205  -25.764  1.00 6.13  ? 17   ILE B N   1 
ATOM   1222  C  CA  . ILE B  1 17  ? 8.719  42.744  -26.358  1.00 5.58  ? 17   ILE B CA  1 
ATOM   1223  C  C   . ILE B  1 17  ? 9.816  43.645  -25.804  1.00 5.45  ? 17   ILE B C   1 
ATOM   1224  O  O   . ILE B  1 17  ? 9.704  44.872  -25.902  1.00 5.77  ? 17   ILE B O   1 
ATOM   1225  C  CB  . ILE B  1 17  ? 8.670  42.849  -27.890  1.00 6.32  ? 17   ILE B CB  1 
ATOM   1226  C  CG1 . ILE B  1 17  ? 7.659  41.806  -28.435  1.00 6.42  ? 17   ILE B CG1 1 
ATOM   1227  C  CG2 . ILE B  1 17  ? 10.081 42.749  -28.481  1.00 5.52  ? 17   ILE B CG2 1 
ATOM   1228  C  CD1 . ILE B  1 17  ? 7.477  41.823  -29.931  1.00 10.31 ? 17   ILE B CD1 1 
ATOM   1229  N  N   . ILE B  1 18  ? 10.869 43.035  -25.258  1.00 3.69  ? 18   ILE B N   1 
ATOM   1230  C  CA  . ILE B  1 18  ? 11.977 43.773  -24.647  1.00 3.48  ? 18   ILE B CA  1 
ATOM   1231  C  C   . ILE B  1 18  ? 13.297 43.363  -25.304  1.00 4.08  ? 18   ILE B C   1 
ATOM   1232  O  O   . ILE B  1 18  ? 13.592 42.168  -25.414  1.00 4.43  ? 18   ILE B O   1 
ATOM   1233  C  CB  . ILE B  1 18  ? 12.067 43.493  -23.110  1.00 2.78  ? 18   ILE B CB  1 
ATOM   1234  C  CG1 . ILE B  1 18  ? 10.774 43.953  -22.391  1.00 3.56  ? 18   ILE B CG1 1 
ATOM   1235  C  CG2 . ILE B  1 18  ? 13.343 44.127  -22.504  1.00 3.36  ? 18   ILE B CG2 1 
ATOM   1236  C  CD1 . ILE B  1 18  ? 10.478 45.461  -22.448  1.00 3.60  ? 18   ILE B CD1 1 
ATOM   1237  N  N   . ASN B  1 19  ? 14.067 44.367  -25.700  1.00 4.01  ? 19   ASN B N   1 
ATOM   1238  C  CA  . ASN B  1 19  ? 15.321 44.200  -26.409  1.00 4.52  ? 19   ASN B CA  1 
ATOM   1239  C  C   . ASN B  1 19  ? 16.479 44.470  -25.469  1.00 3.56  ? 19   ASN B C   1 
ATOM   1240  O  O   . ASN B  1 19  ? 16.345 45.287  -24.577  1.00 3.07  ? 19   ASN B O   1 
ATOM   1241  C  CB  . ASN B  1 19  ? 15.382 45.193  -27.579  1.00 4.32  ? 19   ASN B CB  1 
ATOM   1242  C  CG  . ASN B  1 19  ? 14.246 45.029  -28.550  1.00 7.38  ? 19   ASN B CG  1 
ATOM   1243  O  OD1 . ASN B  1 19  ? 14.205 44.049  -29.288  1.00 4.20  ? 19   ASN B OD1 1 
ATOM   1244  N  ND2 . ASN B  1 19  ? 13.318 46.028  -28.599  1.00 6.13  ? 19   ASN B ND2 1 
ATOM   1245  N  N   . PHE B  1 20  ? 17.602 43.778  -25.677  1.00 3.20  ? 20   PHE B N   1 
ATOM   1246  C  CA  . PHE B  1 20  ? 18.821 44.002  -24.899  1.00 3.55  ? 20   PHE B CA  1 
ATOM   1247  C  C   . PHE B  1 20  ? 19.965 44.241  -25.854  1.00 3.91  ? 20   PHE B C   1 
ATOM   1248  O  O   . PHE B  1 20  ? 20.064 43.562  -26.871  1.00 4.26  ? 20   PHE B O   1 
ATOM   1249  C  CB  . PHE B  1 20  ? 19.188 42.783  -24.027  1.00 3.00  ? 20   PHE B CB  1 
ATOM   1250  C  CG  . PHE B  1 20  ? 18.113 42.352  -23.035  1.00 2.91  ? 20   PHE B CG  1 
ATOM   1251  C  CD1 . PHE B  1 20  ? 18.278 42.607  -21.685  1.00 3.61  ? 20   PHE B CD1 1 
ATOM   1252  C  CD2 . PHE B  1 20  ? 16.999 41.625  -23.454  1.00 4.01  ? 20   PHE B CD2 1 
ATOM   1253  C  CE1 . PHE B  1 20  ? 17.307 42.256  -20.750  1.00 3.41  ? 20   PHE B CE1 1 
ATOM   1254  C  CE2 . PHE B  1 20  ? 16.020 41.223  -22.529  1.00 4.27  ? 20   PHE B CE2 1 
ATOM   1255  C  CZ  . PHE B  1 20  ? 16.182 41.529  -21.166  1.00 4.94  ? 20   PHE B CZ  1 
ATOM   1256  N  N   . GLU B  1 21  ? 20.830 45.219  -25.564  1.00 4.44  ? 21   GLU B N   1 
ATOM   1257  C  CA  . GLU B  1 21  ? 22.032 45.375  -26.401  1.00 5.70  ? 21   GLU B CA  1 
ATOM   1258  C  C   . GLU B  1 21  ? 23.222 45.742  -25.528  1.00 5.06  ? 21   GLU B C   1 
ATOM   1259  O  O   . GLU B  1 21  ? 23.111 46.581  -24.646  1.00 5.08  ? 21   GLU B O   1 
ATOM   1260  C  CB  . GLU B  1 21  ? 21.844 46.445  -27.498  1.00 6.40  ? 21   GLU B CB  1 
ATOM   1261  C  CG  . GLU B  1 21  ? 23.103 46.576  -28.382  1.00 11.57 ? 21   GLU B CG  1 
ATOM   1262  C  CD  . GLU B  1 21  ? 22.897 47.279  -29.718  1.00 18.16 ? 21   GLU B CD  1 
ATOM   1263  O  OE1 . GLU B  1 21  ? 23.922 47.623  -30.352  1.00 22.87 ? 21   GLU B OE1 1 
ATOM   1264  O  OE2 . GLU B  1 21  ? 21.746 47.491  -30.148  1.00 20.63 ? 21   GLU B OE2 1 
ATOM   1265  N  N   . GLN B  1 22  ? 24.362 45.127  -25.800  1.00 4.85  ? 22   GLN B N   1 
ATOM   1266  C  CA  . GLN B  1 22  ? 25.557 45.388  -25.016  1.00 5.07  ? 22   GLN B CA  1 
ATOM   1267  C  C   . GLN B  1 22  ? 26.700 45.578  -25.999  1.00 5.81  ? 22   GLN B C   1 
ATOM   1268  O  O   . GLN B  1 22  ? 27.109 44.621  -26.668  1.00 5.70  ? 22   GLN B O   1 
ATOM   1269  C  CB  . GLN B  1 22  ? 25.788 44.228  -24.042  1.00 3.43  ? 22   GLN B CB  1 
ATOM   1270  C  CG  . GLN B  1 22  ? 26.926 44.464  -23.046  1.00 3.51  ? 22   GLN B CG  1 
ATOM   1271  C  CD  . GLN B  1 22  ? 27.091 43.311  -22.072  1.00 2.53  ? 22   GLN B CD  1 
ATOM   1272  O  OE1 . GLN B  1 22  ? 26.650 42.200  -22.339  1.00 5.23  ? 22   GLN B OE1 1 
ATOM   1273  N  NE2 . GLN B  1 22  ? 27.714 43.579  -20.919  1.00 2.50  ? 22   GLN B NE2 1 
ATOM   1274  N  N   . LYS B  1 23  ? 27.150 46.830  -26.146  1.00 6.35  ? 23   LYS B N   1 
ATOM   1275  C  CA  . LYS B  1 23  ? 28.195 47.180  -27.122  1.00 7.52  ? 23   LYS B CA  1 
ATOM   1276  C  C   . LYS B  1 23  ? 29.546 46.523  -26.823  1.00 7.44  ? 23   LYS B C   1 
ATOM   1277  O  O   . LYS B  1 23  ? 30.274 46.123  -27.749  1.00 7.75  ? 23   LYS B O   1 
ATOM   1278  C  CB  . LYS B  1 23  ? 28.368 48.710  -27.175  1.00 8.84  ? 23   LYS B CB  1 
ATOM   1279  C  CG  . LYS B  1 23  ? 27.187 49.445  -27.788  1.00 12.56 ? 23   LYS B CG  1 
ATOM   1280  C  CD  . LYS B  1 23  ? 27.374 50.966  -27.719  1.00 20.02 ? 23   LYS B CD  1 
ATOM   1281  C  CE  . LYS B  1 23  ? 26.245 51.665  -28.474  1.00 22.46 ? 23   LYS B CE  1 
ATOM   1282  N  NZ  . LYS B  1 23  ? 26.268 53.132  -28.195  1.00 26.40 ? 23   LYS B NZ  1 
ATOM   1283  N  N   . GLU B  1 24  ? 29.868 46.411  -25.538  1.00 6.53  ? 24   GLU B N   1 
ATOM   1284  C  CA  . GLU B  1 24  ? 31.145 45.865  -25.068  1.00 7.00  ? 24   GLU B CA  1 
ATOM   1285  C  C   . GLU B  1 24  ? 30.869 44.882  -23.949  1.00 6.03  ? 24   GLU B C   1 
ATOM   1286  O  O   . GLU B  1 24  ? 30.018 45.158  -23.101  1.00 5.93  ? 24   GLU B O   1 
ATOM   1287  C  CB  . GLU B  1 24  ? 32.038 46.997  -24.524  1.00 7.77  ? 24   GLU B CB  1 
ATOM   1288  C  CG  . GLU B  1 24  ? 32.361 48.075  -25.569  1.00 9.88  ? 24   GLU B CG  1 
ATOM   1289  C  CD  . GLU B  1 24  ? 33.285 47.528  -26.648  1.00 15.66 ? 24   GLU B CD  1 
ATOM   1290  O  OE1 . GLU B  1 24  ? 34.228 46.796  -26.290  1.00 17.99 ? 24   GLU B OE1 1 
ATOM   1291  O  OE2 . GLU B  1 24  ? 33.059 47.793  -27.846  1.00 16.27 ? 24   GLU B OE2 1 
ATOM   1292  N  N   . SER B  1 25  ? 31.584 43.754  -23.926  1.00 5.50  ? 25   SER B N   1 
ATOM   1293  C  CA  . SER B  1 25  ? 31.340 42.712  -22.906  1.00 5.71  ? 25   SER B CA  1 
ATOM   1294  C  C   . SER B  1 25  ? 31.560 43.217  -21.467  1.00 5.76  ? 25   SER B C   1 
ATOM   1295  O  O   . SER B  1 25  ? 30.978 42.685  -20.514  1.00 5.73  ? 25   SER B O   1 
ATOM   1296  C  CB  . SER B  1 25  ? 32.201 41.477  -23.161  1.00 5.58  ? 25   SER B CB  1 
ATOM   1297  O  OG  . SER B  1 25  ? 33.576 41.835  -23.219  1.00 5.59  ? 25   SER B OG  1 
ATOM   1298  N  N   . ASN B  1 26  ? 32.403 44.233  -21.322  1.00 6.11  ? 26   ASN B N   1 
ATOM   1299  C  CA  . ASN B  1 26  ? 32.644 44.857  -20.025  1.00 6.38  ? 26   ASN B CA  1 
ATOM   1300  C  C   . ASN B  1 26  ? 31.916 46.196  -19.872  1.00 6.52  ? 26   ASN B C   1 
ATOM   1301  O  O   . ASN B  1 26  ? 32.273 46.989  -19.003  1.00 7.45  ? 26   ASN B O   1 
ATOM   1302  C  CB  . ASN B  1 26  ? 34.149 45.012  -19.741  1.00 6.14  ? 26   ASN B CB  1 
ATOM   1303  C  CG  . ASN B  1 26  ? 34.845 45.973  -20.706  1.00 6.08  ? 26   ASN B CG  1 
ATOM   1304  O  OD1 . ASN B  1 26  ? 34.459 46.105  -21.873  1.00 5.64  ? 26   ASN B OD1 1 
ATOM   1305  N  ND2 . ASN B  1 26  ? 35.898 46.646  -20.215  1.00 5.94  ? 26   ASN B ND2 1 
ATOM   1306  N  N   . GLY B  1 27  ? 30.911 46.423  -20.719  1.00 5.74  ? 27   GLY B N   1 
ATOM   1307  C  CA  . GLY B  1 27  ? 30.158 47.689  -20.765  1.00 5.73  ? 27   GLY B CA  1 
ATOM   1308  C  C   . GLY B  1 27  ? 28.717 47.499  -20.304  1.00 5.61  ? 27   GLY B C   1 
ATOM   1309  O  O   . GLY B  1 27  ? 28.305 46.373  -20.065  1.00 3.97  ? 27   GLY B O   1 
ATOM   1310  N  N   . PRO B  1 28  ? 27.932 48.600  -20.219  1.00 5.27  ? 28   PRO B N   1 
ATOM   1311  C  CA  . PRO B  1 28  ? 26.526 48.463  -19.779  1.00 4.64  ? 28   PRO B CA  1 
ATOM   1312  C  C   . PRO B  1 28  ? 25.615 47.795  -20.821  1.00 4.57  ? 28   PRO B C   1 
ATOM   1313  O  O   . PRO B  1 28  ? 25.956 47.727  -22.012  1.00 3.54  ? 28   PRO B O   1 
ATOM   1314  C  CB  . PRO B  1 28  ? 26.085 49.915  -19.521  1.00 5.37  ? 28   PRO B CB  1 
ATOM   1315  C  CG  . PRO B  1 28  ? 27.026 50.762  -20.331  1.00 6.24  ? 28   PRO B CG  1 
ATOM   1316  C  CD  . PRO B  1 28  ? 28.344 50.014  -20.355  1.00 6.31  ? 28   PRO B CD  1 
ATOM   1317  N  N   . VAL B  1 29  ? 24.461 47.302  -20.344  1.00 4.54  ? 29   VAL B N   1 
ATOM   1318  C  CA  . VAL B  1 29  ? 23.451 46.722  -21.211  1.00 3.68  ? 29   VAL B CA  1 
ATOM   1319  C  C   . VAL B  1 29  ? 22.281 47.670  -21.307  1.00 4.30  ? 29   VAL B C   1 
ATOM   1320  O  O   . VAL B  1 29  ? 21.767 48.103  -20.274  1.00 4.77  ? 29   VAL B O   1 
ATOM   1321  C  CB  . VAL B  1 29  ? 22.912 45.392  -20.623  1.00 3.01  ? 29   VAL B CB  1 
ATOM   1322  C  CG1 . VAL B  1 29  ? 21.794 44.843  -21.496  1.00 2.22  ? 29   VAL B CG1 1 
ATOM   1323  C  CG2 . VAL B  1 29  ? 24.058 44.373  -20.428  1.00 3.44  ? 29   VAL B CG2 1 
ATOM   1324  N  N   . LYS B  1 30  ? 21.873 48.010  -22.533  1.00 5.25  ? 30   LYS B N   1 
ATOM   1325  C  CA  . LYS B  1 30  ? 20.696 48.843  -22.735  1.00 5.24  ? 30   LYS B CA  1 
ATOM   1326  C  C   . LYS B  1 30  ? 19.473 47.934  -22.872  1.00 4.83  ? 30   LYS B C   1 
ATOM   1327  O  O   . LYS B  1 30  ? 19.541 46.919  -23.534  1.00 4.20  ? 30   LYS B O   1 
ATOM   1328  C  CB  . LYS B  1 30  ? 20.885 49.728  -23.971  1.00 6.27  ? 30   LYS B CB  1 
ATOM   1329  C  CG  . LYS B  1 30  ? 19.687 50.600  -24.299  1.00 10.33 ? 30   LYS B CG  1 
ATOM   1330  C  CD  . LYS B  1 30  ? 19.790 51.182  -25.712  1.00 16.78 ? 30   LYS B CD  1 
ATOM   1331  C  CE  . LYS B  1 30  ? 18.471 51.858  -26.125  1.00 20.88 ? 30   LYS B CE  1 
ATOM   1332  N  NZ  . LYS B  1 30  ? 18.683 52.802  -27.265  1.00 22.76 ? 30   LYS B NZ  1 
ATOM   1333  N  N   . VAL B  1 31  ? 18.366 48.279  -22.223  1.00 4.01  ? 31   VAL B N   1 
ATOM   1334  C  CA  . VAL B  1 31  ? 17.183 47.393  -22.229  1.00 4.44  ? 31   VAL B CA  1 
ATOM   1335  C  C   . VAL B  1 31  ? 16.032 48.299  -22.602  1.00 5.69  ? 31   VAL B C   1 
ATOM   1336  O  O   . VAL B  1 31  ? 15.811 49.337  -21.946  1.00 6.98  ? 31   VAL B O   1 
ATOM   1337  C  CB  . VAL B  1 31  ? 16.936 46.773  -20.829  1.00 4.57  ? 31   VAL B CB  1 
ATOM   1338  C  CG1 . VAL B  1 31  ? 15.718 45.808  -20.827  1.00 3.31  ? 31   VAL B CG1 1 
ATOM   1339  C  CG2 . VAL B  1 31  ? 18.221 46.075  -20.284  1.00 3.76  ? 31   VAL B CG2 1 
ATOM   1340  N  N   . TRP B  1 32  ? 15.335 47.969  -23.683  1.00 5.97  ? 32   TRP B N   1 
ATOM   1341  C  CA  . TRP B  1 32  ? 14.250 48.824  -24.164  1.00 6.51  ? 32   TRP B CA  1 
ATOM   1342  C  C   . TRP B  1 32  ? 13.171 48.021  -24.873  1.00 6.88  ? 32   TRP B C   1 
ATOM   1343  O  O   . TRP B  1 32  ? 13.436 46.965  -25.443  1.00 5.69  ? 32   TRP B O   1 
ATOM   1344  C  CB  . TRP B  1 32  ? 14.777 49.951  -25.079  1.00 6.93  ? 32   TRP B CB  1 
ATOM   1345  C  CG  . TRP B  1 32  ? 15.083 49.494  -26.481  1.00 8.00  ? 32   TRP B CG  1 
ATOM   1346  C  CD1 . TRP B  1 32  ? 14.290 49.653  -27.583  1.00 8.06  ? 32   TRP B CD1 1 
ATOM   1347  C  CD2 . TRP B  1 32  ? 16.265 48.817  -26.933  1.00 9.06  ? 32   TRP B CD2 1 
ATOM   1348  N  NE1 . TRP B  1 32  ? 14.896 49.102  -28.684  1.00 11.08 ? 32   TRP B NE1 1 
ATOM   1349  C  CE2 . TRP B  1 32  ? 16.106 48.579  -28.315  1.00 8.97  ? 32   TRP B CE2 1 
ATOM   1350  C  CE3 . TRP B  1 32  ? 17.423 48.350  -26.291  1.00 9.72  ? 32   TRP B CE3 1 
ATOM   1351  C  CZ2 . TRP B  1 32  ? 17.067 47.915  -29.081  1.00 11.04 ? 32   TRP B CZ2 1 
ATOM   1352  C  CZ3 . TRP B  1 32  ? 18.385 47.696  -27.045  1.00 10.34 ? 32   TRP B CZ3 1 
ATOM   1353  C  CH2 . TRP B  1 32  ? 18.198 47.480  -28.439  1.00 12.39 ? 32   TRP B CH2 1 
ATOM   1354  N  N   . GLY B  1 33  ? 11.950 48.547  -24.835  1.00 6.80  ? 33   GLY B N   1 
ATOM   1355  C  CA  . GLY B  1 33  ? 10.847 47.946  -25.555  1.00 6.04  ? 33   GLY B CA  1 
ATOM   1356  C  C   . GLY B  1 33  ? 9.561  48.532  -25.037  1.00 6.73  ? 33   GLY B C   1 
ATOM   1357  O  O   . GLY B  1 33  ? 9.528  49.669  -24.525  1.00 5.04  ? 33   GLY B O   1 
ATOM   1358  N  N   . SER B  1 34  ? 8.500  47.751  -25.152  1.00 5.99  ? 34   SER B N   1 
ATOM   1359  C  CA  . SER B  1 34  ? 7.196  48.215  -24.695  1.00 7.69  ? 34   SER B CA  1 
ATOM   1360  C  C   . SER B  1 34  ? 6.416  47.039  -24.148  1.00 7.34  ? 34   SER B C   1 
ATOM   1361  O  O   . SER B  1 34  ? 6.577  45.894  -24.609  1.00 7.44  ? 34   SER B O   1 
ATOM   1362  C  CB  . SER B  1 34  ? 6.448  48.881  -25.864  1.00 8.03  ? 34   SER B CB  1 
ATOM   1363  O  OG  . SER B  1 34  ? 5.233  49.471  -25.442  1.00 11.39 ? 34   SER B OG  1 
ATOM   1364  N  N   . ILE B  1 35  ? 5.592  47.314  -23.143  1.00 6.77  ? 35   ILE B N   1 
ATOM   1365  C  CA  . ILE B  1 35  ? 4.676  46.337  -22.582  1.00 6.35  ? 35   ILE B CA  1 
ATOM   1366  C  C   . ILE B  1 35  ? 3.280  46.982  -22.526  1.00 5.69  ? 35   ILE B C   1 
ATOM   1367  O  O   . ILE B  1 35  ? 3.143  48.131  -22.090  1.00 6.14  ? 35   ILE B O   1 
ATOM   1368  C  CB  . ILE B  1 35  ? 5.123  45.901  -21.163  1.00 5.94  ? 35   ILE B CB  1 
ATOM   1369  C  CG1 . ILE B  1 35  ? 6.616  45.480  -21.136  1.00 6.66  ? 35   ILE B CG1 1 
ATOM   1370  C  CG2 . ILE B  1 35  ? 4.209  44.792  -20.629  1.00 7.04  ? 35   ILE B CG2 1 
ATOM   1371  C  CD1 . ILE B  1 35  ? 7.199  45.420  -19.704  1.00 6.45  ? 35   ILE B CD1 1 
ATOM   1372  N  N   . LYS B  1 36  ? 2.263  46.269  -23.004  1.00 5.59  ? 36   LYS B N   1 
ATOM   1373  C  CA  . LYS B  1 36  ? 0.890  46.765  -22.973  1.00 5.47  ? 36   LYS B CA  1 
ATOM   1374  C  C   . LYS B  1 36  ? 0.052  45.935  -21.993  1.00 5.61  ? 36   LYS B C   1 
ATOM   1375  O  O   . LYS B  1 36  ? 0.501  44.883  -21.509  1.00 4.34  ? 36   LYS B O   1 
ATOM   1376  C  CB  . LYS B  1 36  ? 0.281  46.763  -24.396  1.00 6.45  ? 36   LYS B CB  1 
ATOM   1377  C  CG  . LYS B  1 36  ? 0.015  45.355  -25.006  1.00 8.15  ? 36   LYS B CG  1 
ATOM   1378  C  CD  . LYS B  1 36  ? -1.239 44.717  -24.372  1.00 13.55 ? 36   LYS B CD  1 
ATOM   1379  C  CE  . LYS B  1 36  ? -2.094 43.881  -25.337  1.00 15.51 ? 36   LYS B CE  1 
ATOM   1380  N  NZ  . LYS B  1 36  ? -3.166 43.069  -24.585  1.00 10.09 ? 36   LYS B NZ  1 
ATOM   1381  N  N   . GLY B  1 37  ? -1.174 46.387  -21.700  1.00 4.35  ? 37   GLY B N   1 
ATOM   1382  C  CA  . GLY B  1 37  ? -2.070 45.606  -20.856  1.00 4.87  ? 37   GLY B CA  1 
ATOM   1383  C  C   . GLY B  1 37  ? -1.906 45.698  -19.356  1.00 4.80  ? 37   GLY B C   1 
ATOM   1384  O  O   . GLY B  1 37  ? -2.479 44.871  -18.599  1.00 5.80  ? 37   GLY B O   1 
ATOM   1385  N  N   . LEU B  1 38  ? -1.139 46.704  -18.918  1.00 5.00  ? 38   LEU B N   1 
ATOM   1386  C  CA  . LEU B  1 38  ? -0.780 46.887  -17.500  1.00 5.03  ? 38   LEU B CA  1 
ATOM   1387  C  C   . LEU B  1 38  ? -1.622 47.988  -16.867  1.00 5.00  ? 38   LEU B C   1 
ATOM   1388  O  O   . LEU B  1 38  ? -1.979 48.952  -17.549  1.00 5.05  ? 38   LEU B O   1 
ATOM   1389  C  CB  . LEU B  1 38  ? 0.703  47.305  -17.378  1.00 4.53  ? 38   LEU B CB  1 
ATOM   1390  C  CG  . LEU B  1 38  ? 1.816  46.329  -17.728  1.00 5.99  ? 38   LEU B CG  1 
ATOM   1391  C  CD1 . LEU B  1 38  ? 3.167  47.081  -17.971  1.00 7.90  ? 38   LEU B CD1 1 
ATOM   1392  C  CD2 . LEU B  1 38  ? 1.913  45.300  -16.608  1.00 7.19  ? 38   LEU B CD2 1 
ATOM   1393  N  N   . THR B  1 39  ? -1.922 47.862  -15.572  1.00 5.14  ? 39   THR B N   1 
ATOM   1394  C  CA  . THR B  1 39  ? -2.527 48.972  -14.819  1.00 6.78  ? 39   THR B CA  1 
ATOM   1395  C  C   . THR B  1 39  ? -1.575 50.174  -14.790  1.00 7.41  ? 39   THR B C   1 
ATOM   1396  O  O   . THR B  1 39  ? -0.361 50.016  -14.704  1.00 5.91  ? 39   THR B O   1 
ATOM   1397  C  CB  . THR B  1 39  ? -2.921 48.582  -13.376  1.00 6.88  ? 39   THR B CB  1 
ATOM   1398  O  OG1 . THR B  1 39  ? -1.800 47.990  -12.703  1.00 7.10  ? 39   THR B OG1 1 
ATOM   1399  C  CG2 . THR B  1 39  ? -4.088 47.589  -13.378  1.00 8.38  ? 39   THR B CG2 1 
ATOM   1400  N  N   . GLU B  1 40  ? -2.131 51.385  -14.887  1.00 7.08  ? 40   GLU B N   1 
ATOM   1401  C  CA  . GLU B  1 40  ? -1.314 52.569  -14.789  1.00 8.51  ? 40   GLU B CA  1 
ATOM   1402  C  C   . GLU B  1 40  ? -0.461 52.523  -13.500  1.00 8.58  ? 40   GLU B C   1 
ATOM   1403  O  O   . GLU B  1 40  ? -0.956 52.124  -12.445  1.00 8.45  ? 40   GLU B O   1 
ATOM   1404  C  CB  . GLU B  1 40  ? -2.210 53.823  -14.807  1.00 8.22  ? 40   GLU B CB  1 
ATOM   1405  C  CG  . GLU B  1 40  ? -1.409 55.134  -14.725  1.00 12.38 ? 40   GLU B CG  1 
ATOM   1406  C  CD  . GLU B  1 40  ? -2.231 56.392  -15.034  1.00 18.79 ? 40   GLU B CD  1 
ATOM   1407  O  OE1 . GLU B  1 40  ? -1.629 57.484  -15.015  1.00 22.70 ? 40   GLU B OE1 1 
ATOM   1408  O  OE2 . GLU B  1 40  ? -3.451 56.303  -15.306  1.00 18.02 ? 40   GLU B OE2 1 
ATOM   1409  N  N   . GLY B  1 41  ? 0.807  52.911  -13.603  1.00 8.63  ? 41   GLY B N   1 
ATOM   1410  C  CA  . GLY B  1 41  ? 1.682  53.014  -12.435  1.00 8.81  ? 41   GLY B CA  1 
ATOM   1411  C  C   . GLY B  1 41  ? 2.867  52.064  -12.508  1.00 8.54  ? 41   GLY B C   1 
ATOM   1412  O  O   . GLY B  1 41  ? 3.195  51.558  -13.576  1.00 8.23  ? 41   GLY B O   1 
ATOM   1413  N  N   . LEU B  1 42  ? 3.507  51.823  -11.372  1.00 8.10  ? 42   LEU B N   1 
ATOM   1414  C  CA  . LEU B  1 42  ? 4.760  51.073  -11.379  1.00 7.27  ? 42   LEU B CA  1 
ATOM   1415  C  C   . LEU B  1 42  ? 4.535  49.587  -11.259  1.00 6.38  ? 42   LEU B C   1 
ATOM   1416  O  O   . LEU B  1 42  ? 3.627  49.117  -10.554  1.00 5.81  ? 42   LEU B O   1 
ATOM   1417  C  CB  . LEU B  1 42  ? 5.695  51.535  -10.255  1.00 8.71  ? 42   LEU B CB  1 
ATOM   1418  C  CG  . LEU B  1 42  ? 6.410  52.898  -10.285  1.00 11.98 ? 42   LEU B CG  1 
ATOM   1419  C  CD1 . LEU B  1 42  ? 5.568  54.029  -10.839  1.00 15.05 ? 42   LEU B CD1 1 
ATOM   1420  C  CD2 . LEU B  1 42  ? 6.822  53.250  -8.840   1.00 14.10 ? 42   LEU B CD2 1 
ATOM   1421  N  N   . HIS B  1 43  ? 5.406  48.854  -11.952  1.00 4.82  ? 43   HIS B N   1 
ATOM   1422  C  CA  . HIS B  1 43  ? 5.362  47.406  -11.983  1.00 4.76  ? 43   HIS B CA  1 
ATOM   1423  C  C   . HIS B  1 43  ? 6.785  46.894  -11.879  1.00 4.40  ? 43   HIS B C   1 
ATOM   1424  O  O   . HIS B  1 43  ? 7.654  47.349  -12.628  1.00 4.01  ? 43   HIS B O   1 
ATOM   1425  C  CB  . HIS B  1 43  ? 4.734  46.951  -13.300  1.00 4.38  ? 43   HIS B CB  1 
ATOM   1426  C  CG  . HIS B  1 43  ? 3.273  47.267  -13.389  1.00 4.71  ? 43   HIS B CG  1 
ATOM   1427  N  ND1 . HIS B  1 43  ? 2.307  46.421  -12.893  1.00 6.12  ? 43   HIS B ND1 1 
ATOM   1428  C  CD2 . HIS B  1 43  ? 2.621  48.353  -13.861  1.00 5.91  ? 43   HIS B CD2 1 
ATOM   1429  C  CE1 . HIS B  1 43  ? 1.113  46.968  -13.071  1.00 7.21  ? 43   HIS B CE1 1 
ATOM   1430  N  NE2 . HIS B  1 43  ? 1.278  48.140  -13.658  1.00 6.06  ? 43   HIS B NE2 1 
ATOM   1431  N  N   . GLY B  1 44  ? 7.009  45.970  -10.946  1.00 4.37  ? 44   GLY B N   1 
ATOM   1432  C  CA  . GLY B  1 44  ? 8.340  45.391  -10.728  1.00 3.38  ? 44   GLY B CA  1 
ATOM   1433  C  C   . GLY B  1 44  ? 8.822  44.691  -11.991  1.00 3.79  ? 44   GLY B C   1 
ATOM   1434  O  O   . GLY B  1 44  ? 8.019  44.136  -12.763  1.00 2.79  ? 44   GLY B O   1 
ATOM   1435  N  N   . PHE B  1 45  ? 10.136 44.699  -12.201  1.00 3.04  ? 45   PHE B N   1 
ATOM   1436  C  CA  . PHE B  1 45  ? 10.691 44.245  -13.476  1.00 3.21  ? 45   PHE B CA  1 
ATOM   1437  C  C   . PHE B  1 45  ? 12.032 43.625  -13.138  1.00 3.27  ? 45   PHE B C   1 
ATOM   1438  O  O   . PHE B  1 45  ? 12.961 44.348  -12.725  1.00 3.03  ? 45   PHE B O   1 
ATOM   1439  C  CB  . PHE B  1 45  ? 10.847 45.483  -14.375  1.00 3.53  ? 45   PHE B CB  1 
ATOM   1440  C  CG  . PHE B  1 45  ? 11.218 45.192  -15.830  1.00 3.58  ? 45   PHE B CG  1 
ATOM   1441  C  CD1 . PHE B  1 45  ? 10.324 44.550  -16.699  1.00 3.06  ? 45   PHE B CD1 1 
ATOM   1442  C  CD2 . PHE B  1 45  ? 12.409 45.656  -16.343  1.00 3.86  ? 45   PHE B CD2 1 
ATOM   1443  C  CE1 . PHE B  1 45  ? 10.662 44.340  -18.055  1.00 4.96  ? 45   PHE B CE1 1 
ATOM   1444  C  CE2 . PHE B  1 45  ? 12.744 45.466  -17.708  1.00 3.47  ? 45   PHE B CE2 1 
ATOM   1445  C  CZ  . PHE B  1 45  ? 11.869 44.805  -18.547  1.00 4.10  ? 45   PHE B CZ  1 
ATOM   1446  N  N   . HIS B  1 46  ? 12.130 42.293  -13.283  1.00 3.36  ? 46   HIS B N   1 
ATOM   1447  C  CA  . HIS B  1 46  ? 13.345 41.567  -12.885  1.00 3.56  ? 46   HIS B CA  1 
ATOM   1448  C  C   . HIS B  1 46  ? 13.729 40.412  -13.799  1.00 3.93  ? 46   HIS B C   1 
ATOM   1449  O  O   . HIS B  1 46  ? 12.874 39.800  -14.479  1.00 3.47  ? 46   HIS B O   1 
ATOM   1450  C  CB  . HIS B  1 46  ? 13.223 40.970  -11.478  1.00 3.84  ? 46   HIS B CB  1 
ATOM   1451  C  CG  . HIS B  1 46  ? 12.402 41.786  -10.528  1.00 3.36  ? 46   HIS B CG  1 
ATOM   1452  N  ND1 . HIS B  1 46  ? 11.157 41.387  -10.097  1.00 4.23  ? 46   HIS B ND1 1 
ATOM   1453  C  CD2 . HIS B  1 46  ? 12.664 42.955  -9.899   1.00 5.42  ? 46   HIS B CD2 1 
ATOM   1454  C  CE1 . HIS B  1 46  ? 10.675 42.287  -9.258   1.00 4.11  ? 46   HIS B CE1 1 
ATOM   1455  N  NE2 . HIS B  1 46  ? 11.567 43.249  -9.121   1.00 6.14  ? 46   HIS B NE2 1 
ATOM   1456  N  N   . VAL B  1 47  ? 15.017 40.093  -13.777  1.00 3.02  ? 47   VAL B N   1 
ATOM   1457  C  CA  . VAL B  1 47  ? 15.459 38.804  -14.313  1.00 4.07  ? 47   VAL B CA  1 
ATOM   1458  C  C   . VAL B  1 47  ? 15.404 37.727  -13.236  1.00 3.67  ? 47   VAL B C   1 
ATOM   1459  O  O   . VAL B  1 47  ? 16.034 37.840  -12.169  1.00 3.43  ? 47   VAL B O   1 
ATOM   1460  C  CB  . VAL B  1 47  ? 16.897 38.876  -14.926  1.00 3.69  ? 47   VAL B CB  1 
ATOM   1461  C  CG1 . VAL B  1 47  ? 17.301 37.528  -15.533  1.00 3.54  ? 47   VAL B CG1 1 
ATOM   1462  C  CG2 . VAL B  1 47  ? 16.946 39.961  -15.982  1.00 4.21  ? 47   VAL B CG2 1 
ATOM   1463  N  N   . HIS B  1 48  ? 14.627 36.686  -13.510  1.00 3.10  ? 48   HIS B N   1 
ATOM   1464  C  CA  . HIS B  1 48  ? 14.535 35.557  -12.581  1.00 2.40  ? 48   HIS B CA  1 
ATOM   1465  C  C   . HIS B  1 48  ? 15.504 34.452  -13.009  1.00 2.51  ? 48   HIS B C   1 
ATOM   1466  O  O   . HIS B  1 48  ? 15.990 34.431  -14.141  1.00 3.87  ? 48   HIS B O   1 
ATOM   1467  C  CB  . HIS B  1 48  ? 13.097 35.025  -12.495  1.00 2.00  ? 48   HIS B CB  1 
ATOM   1468  C  CG  . HIS B  1 48  ? 12.180 35.933  -11.757  1.00 2.44  ? 48   HIS B CG  1 
ATOM   1469  N  ND1 . HIS B  1 48  ? 11.485 35.545  -10.639  1.00 2.15  ? 48   HIS B ND1 1 
ATOM   1470  C  CD2 . HIS B  1 48  ? 11.900 37.247  -11.942  1.00 2.00  ? 48   HIS B CD2 1 
ATOM   1471  C  CE1 . HIS B  1 48  ? 10.786 36.570  -10.181  1.00 4.84  ? 48   HIS B CE1 1 
ATOM   1472  N  NE2 . HIS B  1 48  ? 11.013 37.610  -10.961  1.00 2.39  ? 48   HIS B NE2 1 
ATOM   1473  N  N   . GLU B  1 49  ? 15.749 33.538  -12.094  1.00 2.18  ? 49   GLU B N   1 
ATOM   1474  C  CA  . GLU B  1 49  ? 16.873 32.611  -12.185  1.00 2.74  ? 49   GLU B CA  1 
ATOM   1475  C  C   . GLU B  1 49  ? 16.741 31.566  -13.287  1.00 3.26  ? 49   GLU B C   1 
ATOM   1476  O  O   . GLU B  1 49  ? 17.715 31.272  -13.966  1.00 3.45  ? 49   GLU B O   1 
ATOM   1477  C  CB  . GLU B  1 49  ? 17.088 31.951  -10.834  1.00 3.45  ? 49   GLU B CB  1 
ATOM   1478  C  CG  . GLU B  1 49  ? 18.323 30.989  -10.789  1.00 4.12  ? 49   GLU B CG  1 
ATOM   1479  C  CD  . GLU B  1 49  ? 18.514 30.335  -9.427   1.00 5.97  ? 49   GLU B CD  1 
ATOM   1480  O  OE1 . GLU B  1 49  ? 19.573 29.722  -9.198   1.00 8.23  ? 49   GLU B OE1 1 
ATOM   1481  O  OE2 . GLU B  1 49  ? 17.619 30.433  -8.586   1.00 7.70  ? 49   GLU B OE2 1 
ATOM   1482  N  N   . PHE B  1 50  ? 15.543 31.027  -13.499  1.00 2.83  ? 50   PHE B N   1 
ATOM   1483  C  CA  . PHE B  1 50  ? 15.418 29.925  -14.470  1.00 3.74  ? 50   PHE B CA  1 
ATOM   1484  C  C   . PHE B  1 50  ? 14.644 30.305  -15.695  1.00 3.26  ? 50   PHE B C   1 
ATOM   1485  O  O   . PHE B  1 50  ? 13.599 30.941  -15.585  1.00 4.40  ? 50   PHE B O   1 
ATOM   1486  C  CB  . PHE B  1 50  ? 14.794 28.694  -13.812  1.00 3.81  ? 50   PHE B CB  1 
ATOM   1487  C  CG  . PHE B  1 50  ? 15.450 28.334  -12.527  1.00 6.39  ? 50   PHE B CG  1 
ATOM   1488  C  CD1 . PHE B  1 50  ? 16.792 27.962  -12.510  1.00 9.54  ? 50   PHE B CD1 1 
ATOM   1489  C  CD2 . PHE B  1 50  ? 14.743 28.383  -11.335  1.00 10.73 ? 50   PHE B CD2 1 
ATOM   1490  C  CE1 . PHE B  1 50  ? 17.437 27.645  -11.301  1.00 10.00 ? 50   PHE B CE1 1 
ATOM   1491  C  CE2 . PHE B  1 50  ? 15.376 28.055  -10.121  1.00 11.31 ? 50   PHE B CE2 1 
ATOM   1492  C  CZ  . PHE B  1 50  ? 16.710 27.697  -10.112  1.00 10.17 ? 50   PHE B CZ  1 
ATOM   1493  N  N   . GLY B  1 51  ? 15.149 29.902  -16.863  1.00 3.10  ? 51   GLY B N   1 
ATOM   1494  C  CA  . GLY B  1 51  ? 14.410 30.050  -18.125  1.00 2.46  ? 51   GLY B CA  1 
ATOM   1495  C  C   . GLY B  1 51  ? 13.424 28.879  -18.305  1.00 4.11  ? 51   GLY B C   1 
ATOM   1496  O  O   . GLY B  1 51  ? 13.359 28.267  -19.359  1.00 4.65  ? 51   GLY B O   1 
ATOM   1497  N  N   . ASP B  1 52  ? 12.653 28.595  -17.262  1.00 3.34  ? 52   ASP B N   1 
ATOM   1498  C  CA  . ASP B  1 52  ? 11.732 27.475  -17.221  1.00 4.75  ? 52   ASP B CA  1 
ATOM   1499  C  C   . ASP B  1 52  ? 10.293 27.995  -17.148  1.00 5.48  ? 52   ASP B C   1 
ATOM   1500  O  O   . ASP B  1 52  ? 9.915  28.603  -16.150  1.00 6.76  ? 52   ASP B O   1 
ATOM   1501  C  CB  . ASP B  1 52  ? 12.067 26.643  -15.976  1.00 4.18  ? 52   ASP B CB  1 
ATOM   1502  C  CG  . ASP B  1 52  ? 11.263 25.341  -15.887  1.00 4.87  ? 52   ASP B CG  1 
ATOM   1503  O  OD1 . ASP B  1 52  ? 11.703 24.433  -15.176  1.00 6.83  ? 52   ASP B OD1 1 
ATOM   1504  O  OD2 . ASP B  1 52  ? 10.176 25.254  -16.460  1.00 4.02  ? 52   ASP B OD2 1 
ATOM   1505  N  N   . ASN B  1 53  ? 9.524  27.776  -18.211  1.00 5.02  ? 53   ASN B N   1 
ATOM   1506  C  CA  . ASN B  1 53  ? 8.132  28.252  -18.309  1.00 6.04  ? 53   ASN B CA  1 
ATOM   1507  C  C   . ASN B  1 53  ? 7.177  27.071  -18.273  1.00 6.00  ? 53   ASN B C   1 
ATOM   1508  O  O   . ASN B  1 53  ? 6.016  27.161  -18.737  1.00 5.65  ? 53   ASN B O   1 
ATOM   1509  C  CB  . ASN B  1 53  ? 7.924  29.020  -19.622  1.00 6.53  ? 53   ASN B CB  1 
ATOM   1510  C  CG  . ASN B  1 53  ? 6.641  29.850  -19.623  1.00 10.07 ? 53   ASN B CG  1 
ATOM   1511  O  OD1 . ASN B  1 53  ? 5.835  29.779  -20.564  1.00 17.37 ? 53   ASN B OD1 1 
ATOM   1512  N  ND2 . ASN B  1 53  ? 6.452  30.654  -18.572  1.00 15.82 ? 53   ASN B ND2 1 
ATOM   1513  N  N   . THR B  1 54  ? 7.658  25.946  -17.748  1.00 5.94  ? 54   THR B N   1 
ATOM   1514  C  CA  . THR B  1 54  ? 6.828  24.718  -17.781  1.00 6.79  ? 54   THR B CA  1 
ATOM   1515  C  C   . THR B  1 54  ? 5.535  24.859  -16.976  1.00 8.29  ? 54   THR B C   1 
ATOM   1516  O  O   . THR B  1 54  ? 4.499  24.282  -17.345  1.00 8.53  ? 54   THR B O   1 
ATOM   1517  C  CB  . THR B  1 54  ? 7.590  23.459  -17.344  1.00 6.70  ? 54   THR B CB  1 
ATOM   1518  O  OG1 . THR B  1 54  ? 8.127  23.620  -16.016  1.00 4.43  ? 54   THR B OG1 1 
ATOM   1519  C  CG2 . THR B  1 54  ? 8.713  23.167  -18.337  1.00 6.23  ? 54   THR B CG2 1 
ATOM   1520  N  N   . ALA B  1 55  ? 5.597  25.628  -15.896  1.00 8.49  ? 55   ALA B N   1 
ATOM   1521  C  CA  . ALA B  1 55  ? 4.396  25.924  -15.083  1.00 9.25  ? 55   ALA B CA  1 
ATOM   1522  C  C   . ALA B  1 55  ? 4.055  27.399  -15.134  1.00 9.86  ? 55   ALA B C   1 
ATOM   1523  O  O   . ALA B  1 55  ? 3.633  27.989  -14.119  1.00 11.83 ? 55   ALA B O   1 
ATOM   1524  C  CB  . ALA B  1 55  ? 4.613  25.478  -13.644  1.00 8.92  ? 55   ALA B CB  1 
ATOM   1525  N  N   . GLY B  1 56  ? 4.210  27.992  -16.315  1.00 8.14  ? 56   GLY B N   1 
ATOM   1526  C  CA  . GLY B  1 56  ? 4.051  29.421  -16.470  1.00 8.09  ? 56   GLY B CA  1 
ATOM   1527  C  C   . GLY B  1 56  ? 5.202  30.143  -15.781  1.00 6.64  ? 56   GLY B C   1 
ATOM   1528  O  O   . GLY B  1 56  ? 6.294  29.592  -15.586  1.00 6.58  ? 56   GLY B O   1 
ATOM   1529  N  N   . CYS B  1 57  ? 4.941  31.364  -15.358  1.00 5.59  ? 57   CYS B N   1 
ATOM   1530  C  CA  . CYS B  1 57  ? 6.011  32.224  -14.830  1.00 4.57  ? 57   CYS B CA  1 
ATOM   1531  C  C   . CYS B  1 57  ? 6.477  31.761  -13.457  1.00 5.43  ? 57   CYS B C   1 
ATOM   1532  O  O   . CYS B  1 57  ? 7.573  32.113  -13.037  1.00 3.70  ? 57   CYS B O   1 
ATOM   1533  C  CB  . CYS B  1 57  ? 5.542  33.682  -14.781  0.40 2.93  ? 57   CYS B CB  1 
ATOM   1534  S  SG  . CYS B  1 57  ? 5.059  34.359  -16.382  0.40 2.00  ? 57   CYS B SG  1 
ATOM   1535  N  N   . THR B  1 58  ? 5.652  30.946  -12.784  1.00 4.89  ? 58   THR B N   1 
ATOM   1536  C  CA  . THR B  1 58  ? 6.006  30.421  -11.488  1.00 5.98  ? 58   THR B CA  1 
ATOM   1537  C  C   . THR B  1 58  ? 7.298  29.614  -11.532  1.00 4.64  ? 58   THR B C   1 
ATOM   1538  O  O   . THR B  1 58  ? 8.094  29.658  -10.597  1.00 5.96  ? 58   THR B O   1 
ATOM   1539  C  CB  . THR B  1 58  ? 4.827  29.624  -10.855  1.00 6.29  ? 58   THR B CB  1 
ATOM   1540  O  OG1 . THR B  1 58  ? 3.706  30.505  -10.738  1.00 9.32  ? 58   THR B OG1 1 
ATOM   1541  C  CG2 . THR B  1 58  ? 5.176  29.161  -9.437   1.00 8.08  ? 58   THR B CG2 1 
ATOM   1542  N  N   . SER B  1 59  ? 7.531  28.886  -12.622  1.00 3.94  ? 59   SER B N   1 
ATOM   1543  C  CA  . SER B  1 59  ? 8.698  28.003  -12.657  1.00 4.37  ? 59   SER B CA  1 
ATOM   1544  C  C   . SER B  1 59  ? 10.021 28.710  -12.950  1.00 3.39  ? 59   SER B C   1 
ATOM   1545  O  O   . SER B  1 59  ? 11.068 28.074  -12.952  1.00 3.84  ? 59   SER B O   1 
ATOM   1546  C  CB  . SER B  1 59  ? 8.491  26.816  -13.605  1.00 4.74  ? 59   SER B CB  1 
ATOM   1547  O  OG  . SER B  1 59  ? 7.818  27.205  -14.767  1.00 7.92  ? 59   SER B OG  1 
ATOM   1548  N  N   . ALA B  1 60  ? 9.966  30.017  -13.203  1.00 2.86  ? 60   ALA B N   1 
ATOM   1549  C  CA  . ALA B  1 60  ? 11.177 30.820  -13.329  1.00 3.34  ? 60   ALA B CA  1 
ATOM   1550  C  C   . ALA B  1 60  ? 12.001 30.901  -12.044  1.00 2.62  ? 60   ALA B C   1 
ATOM   1551  O  O   . ALA B  1 60  ? 13.192 31.274  -12.079  1.00 3.06  ? 60   ALA B O   1 
ATOM   1552  C  CB  . ALA B  1 60  ? 10.824 32.232  -13.822  1.00 2.42  ? 60   ALA B CB  1 
ATOM   1553  N  N   . GLY B  1 61  ? 11.385 30.588  -10.905  1.00 2.95  ? 61   GLY B N   1 
ATOM   1554  C  CA  . GLY B  1 61  ? 12.118 30.627  -9.648   1.00 3.46  ? 61   GLY B CA  1 
ATOM   1555  C  C   . GLY B  1 61  ? 12.266 32.079  -9.184   1.00 2.89  ? 61   GLY B C   1 
ATOM   1556  O  O   . GLY B  1 61  ? 11.541 32.959  -9.667   1.00 3.60  ? 61   GLY B O   1 
ATOM   1557  N  N   . PRO B  1 62  ? 13.212 32.325  -8.264   1.00 3.81  ? 62   PRO B N   1 
ATOM   1558  C  CA  . PRO B  1 62  ? 13.396 33.632  -7.619   1.00 3.44  ? 62   PRO B CA  1 
ATOM   1559  C  C   . PRO B  1 62  ? 14.222 34.567  -8.485   1.00 3.22  ? 62   PRO B C   1 
ATOM   1560  O  O   . PRO B  1 62  ? 14.644 34.197  -9.573   1.00 2.00  ? 62   PRO B O   1 
ATOM   1561  C  CB  . PRO B  1 62  ? 14.192 33.280  -6.350   1.00 4.74  ? 62   PRO B CB  1 
ATOM   1562  C  CG  . PRO B  1 62  ? 15.003 32.069  -6.723   1.00 3.46  ? 62   PRO B CG  1 
ATOM   1563  C  CD  . PRO B  1 62  ? 14.159 31.308  -7.752   1.00 4.02  ? 62   PRO B CD  1 
ATOM   1564  N  N   . HIS B  1 63  ? 14.490 35.764  -7.984   1.00 2.92  ? 63   HIS B N   1 
ATOM   1565  C  CA  . HIS B  1 63  ? 15.332 36.694  -8.722   1.00 3.26  ? 63   HIS B CA  1 
ATOM   1566  C  C   . HIS B  1 63  ? 16.711 36.095  -8.942   1.00 3.05  ? 63   HIS B C   1 
ATOM   1567  O  O   . HIS B  1 63  ? 17.233 35.395  -8.069   1.00 2.99  ? 63   HIS B O   1 
ATOM   1568  C  CB  . HIS B  1 63  ? 15.429 38.019  -7.977   1.00 2.83  ? 63   HIS B CB  1 
ATOM   1569  C  CG  . HIS B  1 63  ? 14.107 38.692  -7.798   1.00 3.30  ? 63   HIS B CG  1 
ATOM   1570  N  ND1 . HIS B  1 63  ? 13.980 39.952  -7.268   1.00 2.93  ? 63   HIS B ND1 1 
ATOM   1571  C  CD2 . HIS B  1 63  ? 12.856 38.301  -8.141   1.00 2.00  ? 63   HIS B CD2 1 
ATOM   1572  C  CE1 . HIS B  1 63  ? 12.701 40.298  -7.240   1.00 3.62  ? 63   HIS B CE1 1 
ATOM   1573  N  NE2 . HIS B  1 63  ? 11.996 39.306  -7.758   1.00 4.69  ? 63   HIS B NE2 1 
ATOM   1574  N  N   . PHE B  1 64  ? 17.275 36.351  -10.123  1.00 3.16  ? 64   PHE B N   1 
ATOM   1575  C  CA  . PHE B  1 64  ? 18.614 35.843  -10.459  1.00 2.16  ? 64   PHE B CA  1 
ATOM   1576  C  C   . PHE B  1 64  ? 19.607 36.496  -9.508   1.00 2.62  ? 64   PHE B C   1 
ATOM   1577  O  O   . PHE B  1 64  ? 19.687 37.720  -9.445   1.00 2.00  ? 64   PHE B O   1 
ATOM   1578  C  CB  . PHE B  1 64  ? 18.907 36.135  -11.936  1.00 2.00  ? 64   PHE B CB  1 
ATOM   1579  C  CG  . PHE B  1 64  ? 20.279 35.737  -12.388  1.00 3.63  ? 64   PHE B CG  1 
ATOM   1580  C  CD1 . PHE B  1 64  ? 21.024 36.595  -13.186  1.00 4.24  ? 64   PHE B CD1 1 
ATOM   1581  C  CD2 . PHE B  1 64  ? 20.836 34.513  -12.005  1.00 3.86  ? 64   PHE B CD2 1 
ATOM   1582  C  CE1 . PHE B  1 64  ? 22.312 36.247  -13.616  1.00 5.04  ? 64   PHE B CE1 1 
ATOM   1583  C  CE2 . PHE B  1 64  ? 22.135 34.150  -12.414  1.00 5.05  ? 64   PHE B CE2 1 
ATOM   1584  C  CZ  . PHE B  1 64  ? 22.857 35.018  -13.238  1.00 4.52  ? 64   PHE B CZ  1 
ATOM   1585  N  N   . ASN B  1 65  ? 20.345 35.677  -8.758   1.00 2.46  ? 65   ASN B N   1 
ATOM   1586  C  CA  . ASN B  1 65  ? 21.115 36.172  -7.596   1.00 4.59  ? 65   ASN B CA  1 
ATOM   1587  C  C   . ASN B  1 65  ? 22.402 35.383  -7.376   1.00 4.58  ? 65   ASN B C   1 
ATOM   1588  O  O   . ASN B  1 65  ? 22.597 34.805  -6.308   1.00 5.48  ? 65   ASN B O   1 
ATOM   1589  C  CB  . ASN B  1 65  ? 20.247 36.093  -6.339   1.00 3.83  ? 65   ASN B CB  1 
ATOM   1590  C  CG  . ASN B  1 65  ? 20.882 36.776  -5.115   1.00 5.21  ? 65   ASN B CG  1 
ATOM   1591  O  OD1 . ASN B  1 65  ? 21.692 37.688  -5.240   1.00 5.64  ? 65   ASN B OD1 1 
ATOM   1592  N  ND2 . ASN B  1 65  ? 20.475 36.345  -3.929   1.00 4.37  ? 65   ASN B ND2 1 
ATOM   1593  N  N   . PRO B  1 66  ? 23.287 35.368  -8.379   1.00 5.61  ? 66   PRO B N   1 
ATOM   1594  C  CA  . PRO B  1 66  ? 24.495 34.549  -8.292   1.00 6.15  ? 66   PRO B CA  1 
ATOM   1595  C  C   . PRO B  1 66  ? 25.482 35.050  -7.226   1.00 7.58  ? 66   PRO B C   1 
ATOM   1596  O  O   . PRO B  1 66  ? 26.331 34.291  -6.781   1.00 7.86  ? 66   PRO B O   1 
ATOM   1597  C  CB  . PRO B  1 66  ? 25.116 34.702  -9.687   1.00 5.58  ? 66   PRO B CB  1 
ATOM   1598  C  CG  . PRO B  1 66  ? 24.648 36.055  -10.156  1.00 6.48  ? 66   PRO B CG  1 
ATOM   1599  C  CD  . PRO B  1 66  ? 23.226 36.122  -9.646   1.00 4.41  ? 66   PRO B CD  1 
ATOM   1600  N  N   . LEU B  1 67  ? 25.355 36.305  -6.813   1.00 7.82  ? 67   LEU B N   1 
ATOM   1601  C  CA  . LEU B  1 67  ? 26.224 36.850  -5.761   1.00 9.64  ? 67   LEU B CA  1 
ATOM   1602  C  C   . LEU B  1 67  ? 25.630 36.800  -4.346   1.00 9.47  ? 67   LEU B C   1 
ATOM   1603  O  O   . LEU B  1 67  ? 26.255 37.260  -3.377   1.00 9.50  ? 67   LEU B O   1 
ATOM   1604  C  CB  . LEU B  1 67  ? 26.681 38.280  -6.108   1.00 9.49  ? 67   LEU B CB  1 
ATOM   1605  C  CG  . LEU B  1 67  ? 27.298 38.515  -7.480   1.00 12.46 ? 67   LEU B CG  1 
ATOM   1606  C  CD1 . LEU B  1 67  ? 27.726 39.996  -7.618   1.00 15.10 ? 67   LEU B CD1 1 
ATOM   1607  C  CD2 . LEU B  1 67  ? 28.471 37.585  -7.776   1.00 15.69 ? 67   LEU B CD2 1 
ATOM   1608  N  N   . SER B  1 68  ? 24.426 36.248  -4.226   1.00 9.82  ? 68   SER B N   1 
ATOM   1609  C  CA  . SER B  1 68  ? 23.825 35.919  -2.928   1.00 10.62 ? 68   SER B CA  1 
ATOM   1610  C  C   . SER B  1 68  ? 23.560 37.162  -2.063   1.00 9.92  ? 68   SER B C   1 
ATOM   1611  O  O   . SER B  1 68  ? 23.809 37.155  -0.851   1.00 11.65 ? 68   SER B O   1 
ATOM   1612  C  CB  . SER B  1 68  ? 24.685 34.888  -2.144   1.00 11.19 ? 68   SER B CB  1 
ATOM   1613  O  OG  . SER B  1 68  ? 24.703 33.607  -2.784   1.00 13.17 ? 68   SER B OG  1 
ATOM   1614  N  N   . ARG B  1 69  ? 23.036 38.211  -2.681   1.00 9.27  ? 69   ARG B N   1 
ATOM   1615  C  CA  . ARG B  1 69  ? 22.755 39.470  -1.988   1.00 8.31  ? 69   ARG B CA  1 
ATOM   1616  C  C   . ARG B  1 69  ? 21.247 39.554  -1.715   1.00 7.68  ? 69   ARG B C   1 
ATOM   1617  O  O   . ARG B  1 69  ? 20.468 38.673  -2.138   1.00 5.72  ? 69   ARG B O   1 
ATOM   1618  C  CB  . ARG B  1 69  ? 23.170 40.663  -2.864   1.00 9.03  ? 69   ARG B CB  1 
ATOM   1619  C  CG  . ARG B  1 69  ? 24.586 40.598  -3.446   1.00 13.84 ? 69   ARG B CG  1 
ATOM   1620  C  CD  . ARG B  1 69  ? 25.535 41.491  -2.725   1.00 20.19 ? 69   ARG B CD  1 
ATOM   1621  N  NE  . ARG B  1 69  ? 26.907 41.390  -3.249   1.00 26.03 ? 69   ARG B NE  1 
ATOM   1622  C  CZ  . ARG B  1 69  ? 27.533 42.321  -3.972   1.00 27.84 ? 69   ARG B CZ  1 
ATOM   1623  N  NH1 . ARG B  1 69  ? 28.780 42.110  -4.380   1.00 30.05 ? 69   ARG B NH1 1 
ATOM   1624  N  NH2 . ARG B  1 69  ? 26.935 43.466  -4.285   1.00 29.65 ? 69   ARG B NH2 1 
ATOM   1625  N  N   . LYS B  1 70  ? 20.863 40.599  -0.990   1.00 5.56  ? 70   LYS B N   1 
ATOM   1626  C  CA  . LYS B  1 70  ? 19.461 40.923  -0.726   1.00 5.83  ? 70   LYS B CA  1 
ATOM   1627  C  C   . LYS B  1 70  ? 18.909 41.748  -1.849   1.00 4.64  ? 70   LYS B C   1 
ATOM   1628  O  O   . LYS B  1 70  ? 19.665 42.340  -2.644   1.00 3.53  ? 70   LYS B O   1 
ATOM   1629  C  CB  . LYS B  1 70  ? 19.294 41.711  0.625    1.00 5.60  ? 70   LYS B CB  1 
ATOM   1630  C  CG  . LYS B  1 70  ? 19.760 40.938  1.870    1.00 9.38  ? 70   LYS B CG  1 
ATOM   1631  C  CD  . LYS B  1 70  ? 18.938 39.686  2.091    1.00 15.25 ? 70   LYS B CD  1 
ATOM   1632  C  CE  . LYS B  1 70  ? 19.277 39.022  3.416    1.00 17.58 ? 70   LYS B CE  1 
ATOM   1633  N  NZ  . LYS B  1 70  ? 18.646 37.670  3.472    1.00 17.52 ? 70   LYS B NZ  1 
ATOM   1634  N  N   . HIS B  1 71  ? 17.580 41.796  -1.897   1.00 4.43  ? 71   HIS B N   1 
ATOM   1635  C  CA  . HIS B  1 71  ? 16.878 42.466  -2.957   1.00 4.01  ? 71   HIS B CA  1 
ATOM   1636  C  C   . HIS B  1 71  ? 17.091 43.960  -2.794   1.00 4.27  ? 71   HIS B C   1 
ATOM   1637  O  O   . HIS B  1 71  ? 17.123 44.469  -1.661   1.00 4.35  ? 71   HIS B O   1 
ATOM   1638  C  CB  . HIS B  1 71  ? 15.386 42.138  -2.913   1.00 3.39  ? 71   HIS B CB  1 
ATOM   1639  C  CG  . HIS B  1 71  ? 14.581 42.877  -3.942   1.00 4.23  ? 71   HIS B CG  1 
ATOM   1640  N  ND1 . HIS B  1 71  ? 14.594 42.538  -5.276   1.00 3.73  ? 71   HIS B ND1 1 
ATOM   1641  C  CD2 . HIS B  1 71  ? 13.748 43.939  -3.833   1.00 4.17  ? 71   HIS B CD2 1 
ATOM   1642  C  CE1 . HIS B  1 71  ? 13.811 43.365  -5.949   1.00 3.43  ? 71   HIS B CE1 1 
ATOM   1643  N  NE2 . HIS B  1 71  ? 13.283 44.221  -5.095   1.00 4.26  ? 71   HIS B NE2 1 
ATOM   1644  N  N   . GLY B  1 72  ? 17.262 44.637  -3.922   1.00 4.66  ? 72   GLY B N   1 
ATOM   1645  C  CA  . GLY B  1 72  ? 17.474 46.074  -3.965   1.00 5.59  ? 72   GLY B CA  1 
ATOM   1646  C  C   . GLY B  1 72  ? 16.829 46.685  -5.189   1.00 6.25  ? 72   GLY B C   1 
ATOM   1647  O  O   . GLY B  1 72  ? 16.235 45.979  -6.021   1.00 5.14  ? 72   GLY B O   1 
ATOM   1648  N  N   . GLY B  1 73  ? 16.947 48.003  -5.290   1.00 5.90  ? 73   GLY B N   1 
ATOM   1649  C  CA  . GLY B  1 73  ? 16.712 48.690  -6.554   1.00 5.75  ? 73   GLY B CA  1 
ATOM   1650  C  C   . GLY B  1 73  ? 17.971 48.640  -7.409   1.00 5.71  ? 73   GLY B C   1 
ATOM   1651  O  O   . GLY B  1 73  ? 19.053 48.290  -6.911   1.00 4.90  ? 73   GLY B O   1 
ATOM   1652  N  N   . PRO B  1 74  ? 17.854 49.013  -8.702   1.00 5.80  ? 74   PRO B N   1 
ATOM   1653  C  CA  . PRO B  1 74  ? 18.988 48.856  -9.633   1.00 6.24  ? 74   PRO B CA  1 
ATOM   1654  C  C   . PRO B  1 74  ? 20.205 49.709  -9.285   1.00 7.45  ? 74   PRO B C   1 
ATOM   1655  O  O   . PRO B  1 74  ? 21.356 49.304  -9.533   1.00 6.31  ? 74   PRO B O   1 
ATOM   1656  C  CB  . PRO B  1 74  ? 18.393 49.263  -10.993  1.00 6.18  ? 74   PRO B CB  1 
ATOM   1657  C  CG  . PRO B  1 74  ? 17.184 50.098  -10.661  1.00 5.85  ? 74   PRO B CG  1 
ATOM   1658  C  CD  . PRO B  1 74  ? 16.627 49.369  -9.419   1.00 5.87  ? 74   PRO B CD  1 
ATOM   1659  N  N   . LYS B  1 75  ? 19.952 50.861  -8.667   1.00 9.03  ? 75   LYS B N   1 
ATOM   1660  C  CA  . LYS B  1 75  ? 21.034 51.761  -8.238   1.00 11.34 ? 75   LYS B CA  1 
ATOM   1661  C  C   . LYS B  1 75  ? 21.712 51.365  -6.920   1.00 11.96 ? 75   LYS B C   1 
ATOM   1662  O  O   . LYS B  1 75  ? 22.751 51.920  -6.566   1.00 12.76 ? 75   LYS B O   1 
ATOM   1663  C  CB  . LYS B  1 75  ? 20.494 53.193  -8.154   1.00 11.38 ? 75   LYS B CB  1 
ATOM   1664  C  CG  . LYS B  1 75  ? 20.007 53.724  -9.510   1.00 15.23 ? 75   LYS B CG  1 
ATOM   1665  C  CD  . LYS B  1 75  ? 20.031 55.242  -9.596   1.00 22.47 ? 75   LYS B CD  1 
ATOM   1666  C  CE  . LYS B  1 75  ? 18.699 55.841  -9.221   1.00 24.19 ? 75   LYS B CE  1 
ATOM   1667  N  NZ  . LYS B  1 75  ? 18.484 55.832  -7.755   1.00 27.19 ? 75   LYS B NZ  1 
ATOM   1668  N  N   . ASP B  1 76  ? 21.148 50.397  -6.199   1.00 12.67 ? 76   ASP B N   1 
ATOM   1669  C  CA  . ASP B  1 76  ? 21.711 49.999  -4.903   1.00 12.92 ? 76   ASP B CA  1 
ATOM   1670  C  C   . ASP B  1 76  ? 22.963 49.139  -5.067   1.00 12.76 ? 76   ASP B C   1 
ATOM   1671  O  O   . ASP B  1 76  ? 23.073 48.381  -6.018   1.00 12.67 ? 76   ASP B O   1 
ATOM   1672  C  CB  . ASP B  1 76  ? 20.670 49.261  -4.060   1.00 12.92 ? 76   ASP B CB  1 
ATOM   1673  C  CG  . ASP B  1 76  ? 19.528 50.155  -3.640   1.00 15.08 ? 76   ASP B CG  1 
ATOM   1674  O  OD1 . ASP B  1 76  ? 18.370 49.678  -3.602   1.00 14.66 ? 76   ASP B OD1 1 
ATOM   1675  O  OD2 . ASP B  1 76  ? 19.787 51.340  -3.345   1.00 17.67 ? 76   ASP B OD2 1 
ATOM   1676  N  N   . GLU B  1 77  ? 23.918 49.279  -4.150   1.00 13.07 ? 77   GLU B N   1 
ATOM   1677  C  CA  . GLU B  1 77  ? 25.055 48.348  -4.106   1.00 13.35 ? 77   GLU B CA  1 
ATOM   1678  C  C   . GLU B  1 77  ? 24.539 46.956  -3.747   1.00 11.90 ? 77   GLU B C   1 
ATOM   1679  O  O   . GLU B  1 77  ? 24.938 45.956  -4.370   1.00 12.28 ? 77   GLU B O   1 
ATOM   1680  C  CB  . GLU B  1 77  ? 26.080 48.792  -3.055   1.00 14.57 ? 77   GLU B CB  1 
ATOM   1681  C  CG  . GLU B  1 77  ? 27.546 48.547  -3.418   1.00 19.75 ? 77   GLU B CG  1 
ATOM   1682  C  CD  . GLU B  1 77  ? 27.883 47.089  -3.765   1.00 25.90 ? 77   GLU B CD  1 
ATOM   1683  O  OE1 . GLU B  1 77  ? 27.719 46.206  -2.893   1.00 29.05 ? 77   GLU B OE1 1 
ATOM   1684  O  OE2 . GLU B  1 77  ? 28.341 46.834  -4.910   1.00 28.73 ? 77   GLU B OE2 1 
ATOM   1685  N  N   . GLU B  1 78  ? 23.655 46.894  -2.750   1.00 9.31  ? 78   GLU B N   1 
ATOM   1686  C  CA  . GLU B  1 78  ? 23.065 45.633  -2.330   1.00 8.97  ? 78   GLU B CA  1 
ATOM   1687  C  C   . GLU B  1 78  ? 21.817 45.350  -3.186   1.00 7.24  ? 78   GLU B C   1 
ATOM   1688  O  O   . GLU B  1 78  ? 20.762 45.958  -2.989   1.00 6.58  ? 78   GLU B O   1 
ATOM   1689  C  CB  . GLU B  1 78  ? 22.742 45.652  -0.822   1.00 8.87  ? 78   GLU B CB  1 
ATOM   1690  C  CG  . GLU B  1 78  ? 22.168 44.357  -0.273   1.00 10.98 ? 78   GLU B CG  1 
ATOM   1691  C  CD  . GLU B  1 78  ? 23.225 43.286  0.017    1.00 15.62 ? 78   GLU B CD  1 
ATOM   1692  O  OE1 . GLU B  1 78  ? 22.825 42.184  0.447    1.00 15.42 ? 78   GLU B OE1 1 
ATOM   1693  O  OE2 . GLU B  1 78  ? 24.444 43.541  -0.175   1.00 19.13 ? 78   GLU B OE2 1 
ATOM   1694  N  N   . ARG B  1 79  ? 21.984 44.464  -4.168   1.00 6.08  ? 79   ARG B N   1 
ATOM   1695  C  CA  . ARG B  1 79  ? 20.887 44.053  -5.061   1.00 5.24  ? 79   ARG B CA  1 
ATOM   1696  C  C   . ARG B  1 79  ? 21.175 42.686  -5.636   1.00 4.42  ? 79   ARG B C   1 
ATOM   1697  O  O   . ARG B  1 79  ? 22.331 42.227  -5.668   1.00 4.72  ? 79   ARG B O   1 
ATOM   1698  C  CB  . ARG B  1 79  ? 20.703 45.044  -6.213   1.00 5.75  ? 79   ARG B CB  1 
ATOM   1699  C  CG  . ARG B  1 79  ? 21.959 45.224  -7.097   1.00 4.83  ? 79   ARG B CG  1 
ATOM   1700  C  CD  . ARG B  1 79  ? 21.674 46.049  -8.342   1.00 4.70  ? 79   ARG B CD  1 
ATOM   1701  N  NE  . ARG B  1 79  ? 21.254 45.215  -9.472   1.00 4.91  ? 79   ARG B NE  1 
ATOM   1702  C  CZ  . ARG B  1 79  ? 21.209 45.629  -10.738  1.00 4.60  ? 79   ARG B CZ  1 
ATOM   1703  N  NH1 . ARG B  1 79  ? 20.856 44.753  -11.698  1.00 5.73  ? 79   ARG B NH1 1 
ATOM   1704  N  NH2 . ARG B  1 79  ? 21.510 46.895  -11.045  1.00 4.93  ? 79   ARG B NH2 1 
ATOM   1705  N  N   . HIS B  1 80  ? 20.119 42.044  -6.119   1.00 3.88  ? 80   HIS B N   1 
ATOM   1706  C  CA  . HIS B  1 80  ? 20.268 40.864  -6.944   1.00 2.90  ? 80   HIS B CA  1 
ATOM   1707  C  C   . HIS B  1 80  ? 20.746 41.294  -8.299   1.00 2.87  ? 80   HIS B C   1 
ATOM   1708  O  O   . HIS B  1 80  ? 20.422 42.389  -8.750   1.00 2.00  ? 80   HIS B O   1 
ATOM   1709  C  CB  . HIS B  1 80  ? 18.911 40.148  -7.090   1.00 2.66  ? 80   HIS B CB  1 
ATOM   1710  C  CG  . HIS B  1 80  ? 18.339 39.691  -5.790   1.00 3.09  ? 80   HIS B CG  1 
ATOM   1711  N  ND1 . HIS B  1 80  ? 16.990 39.768  -5.497   1.00 4.77  ? 80   HIS B ND1 1 
ATOM   1712  C  CD2 . HIS B  1 80  ? 18.939 39.199  -4.681   1.00 2.00  ? 80   HIS B CD2 1 
ATOM   1713  C  CE1 . HIS B  1 80  ? 16.778 39.262  -4.291   1.00 4.95  ? 80   HIS B CE1 1 
ATOM   1714  N  NE2 . HIS B  1 80  ? 17.949 38.933  -3.765   1.00 4.39  ? 80   HIS B NE2 1 
ATOM   1715  N  N   . VAL B  1 81  ? 21.508 40.448  -8.980   1.00 2.00  ? 81   VAL B N   1 
ATOM   1716  C  CA  . VAL B  1 81  ? 21.844 40.777  -10.362  1.00 2.00  ? 81   VAL B CA  1 
ATOM   1717  C  C   . VAL B  1 81  ? 20.558 41.069  -11.172  1.00 2.47  ? 81   VAL B C   1 
ATOM   1718  O  O   . VAL B  1 81  ? 20.503 41.997  -11.974  1.00 2.00  ? 81   VAL B O   1 
ATOM   1719  C  CB  . VAL B  1 81  ? 22.673 39.643  -10.982  1.00 2.00  ? 81   VAL B CB  1 
ATOM   1720  C  CG1 . VAL B  1 81  ? 22.766 39.788  -12.520  1.00 2.11  ? 81   VAL B CG1 1 
ATOM   1721  C  CG2 . VAL B  1 81  ? 24.078 39.678  -10.339  1.00 2.00  ? 81   VAL B CG2 1 
ATOM   1722  N  N   . GLY B  1 82  ? 19.509 40.274  -10.940  1.00 2.13  ? 82   GLY B N   1 
ATOM   1723  C  CA  . GLY B  1 82  ? 18.271 40.484  -11.706  1.00 3.63  ? 82   GLY B CA  1 
ATOM   1724  C  C   . GLY B  1 82  ? 17.425 41.700  -11.384  1.00 4.05  ? 82   GLY B C   1 
ATOM   1725  O  O   . GLY B  1 82  ? 16.353 41.853  -11.975  1.00 3.90  ? 82   GLY B O   1 
ATOM   1726  N  N   . ASP B  1 83  ? 17.875 42.579  -10.478  1.00 3.83  ? 83   ASP B N   1 
ATOM   1727  C  CA  . ASP B  1 83  ? 17.006 43.670  -9.971   1.00 3.62  ? 83   ASP B CA  1 
ATOM   1728  C  C   . ASP B  1 83  ? 16.983 44.901  -10.858  1.00 3.97  ? 83   ASP B C   1 
ATOM   1729  O  O   . ASP B  1 83  ? 17.870 45.743  -10.747  1.00 3.93  ? 83   ASP B O   1 
ATOM   1730  C  CB  . ASP B  1 83  ? 17.399 44.073  -8.534   1.00 3.57  ? 83   ASP B CB  1 
ATOM   1731  C  CG  . ASP B  1 83  ? 17.048 43.017  -7.546   1.00 3.14  ? 83   ASP B CG  1 
ATOM   1732  O  OD1 . ASP B  1 83  ? 16.212 42.141  -7.893   1.00 4.19  ? 83   ASP B OD1 1 
ATOM   1733  O  OD2 . ASP B  1 83  ? 17.562 43.071  -6.416   1.00 2.02  ? 83   ASP B OD2 1 
ATOM   1734  N  N   . LEU B  1 84  ? 15.985 44.987  -11.746  1.00 3.60  ? 84   LEU B N   1 
ATOM   1735  C  CA  . LEU B  1 84  ? 15.889 46.115  -12.669  1.00 3.93  ? 84   LEU B CA  1 
ATOM   1736  C  C   . LEU B  1 84  ? 14.806 47.114  -12.292  1.00 4.10  ? 84   LEU B C   1 
ATOM   1737  O  O   . LEU B  1 84  ? 14.422 47.937  -13.117  1.00 5.92  ? 84   LEU B O   1 
ATOM   1738  C  CB  . LEU B  1 84  ? 15.695 45.644  -14.123  1.00 3.67  ? 84   LEU B CB  1 
ATOM   1739  C  CG  . LEU B  1 84  ? 16.811 44.725  -14.635  1.00 3.21  ? 84   LEU B CG  1 
ATOM   1740  C  CD1 . LEU B  1 84  ? 16.452 44.208  -16.035  1.00 3.97  ? 84   LEU B CD1 1 
ATOM   1741  C  CD2 . LEU B  1 84  ? 18.158 45.473  -14.646  1.00 3.37  ? 84   LEU B CD2 1 
ATOM   1742  N  N   . GLY B  1 85  ? 14.314 47.021  -11.066  1.00 4.06  ? 85   GLY B N   1 
ATOM   1743  C  CA  . GLY B  1 85  ? 13.436 48.059  -10.505  1.00 4.05  ? 85   GLY B CA  1 
ATOM   1744  C  C   . GLY B  1 85  ? 12.012 48.004  -10.995  1.00 4.75  ? 85   GLY B C   1 
ATOM   1745  O  O   . GLY B  1 85  ? 11.367 46.950  -10.919  1.00 4.44  ? 85   GLY B O   1 
ATOM   1746  N  N   . ASN B  1 86  ? 11.512 49.149  -11.475  1.00 4.73  ? 86   ASN B N   1 
ATOM   1747  C  CA  . ASN B  1 86  ? 10.126 49.274  -11.957  1.00 5.12  ? 86   ASN B CA  1 
ATOM   1748  C  C   . ASN B  1 86  ? 10.065 49.833  -13.360  1.00 5.05  ? 86   ASN B C   1 
ATOM   1749  O  O   . ASN B  1 86  ? 10.915 50.621  -13.735  1.00 6.03  ? 86   ASN B O   1 
ATOM   1750  C  CB  . ASN B  1 86  ? 9.287  50.198  -11.073  1.00 4.49  ? 86   ASN B CB  1 
ATOM   1751  C  CG  . ASN B  1 86  ? 9.030  49.625  -9.718   1.00 4.63  ? 86   ASN B CG  1 
ATOM   1752  O  OD1 . ASN B  1 86  ? 8.339  48.619  -9.585   1.00 4.90  ? 86   ASN B OD1 1 
ATOM   1753  N  ND2 . ASN B  1 86  ? 9.609  50.255  -8.686   1.00 5.50  ? 86   ASN B ND2 1 
ATOM   1754  N  N   . VAL B  1 87  ? 9.059  49.407  -14.124  1.00 5.29  ? 87   VAL B N   1 
ATOM   1755  C  CA  . VAL B  1 87  ? 8.658  50.098  -15.346  1.00 5.64  ? 87   VAL B CA  1 
ATOM   1756  C  C   . VAL B  1 87  ? 7.361  50.794  -15.035  1.00 6.22  ? 87   VAL B C   1 
ATOM   1757  O  O   . VAL B  1 87  ? 6.655  50.403  -14.092  1.00 6.55  ? 87   VAL B O   1 
ATOM   1758  C  CB  . VAL B  1 87  ? 8.472  49.147  -16.554  1.00 5.96  ? 87   VAL B CB  1 
ATOM   1759  C  CG1 . VAL B  1 87  ? 9.840  48.524  -16.924  1.00 6.35  ? 87   VAL B CG1 1 
ATOM   1760  C  CG2 . VAL B  1 87  ? 7.416  48.085  -16.271  1.00 4.89  ? 87   VAL B CG2 1 
ATOM   1761  N  N   . THR B  1 88  ? 7.058  51.827  -15.819  1.00 6.76  ? 88   THR B N   1 
ATOM   1762  C  CA  . THR B  1 88  ? 5.875  52.654  -15.581  1.00 6.67  ? 88   THR B CA  1 
ATOM   1763  C  C   . THR B  1 88  ? 4.896  52.598  -16.742  1.00 6.22  ? 88   THR B C   1 
ATOM   1764  O  O   . THR B  1 88  ? 5.214  53.003  -17.865  1.00 7.30  ? 88   THR B O   1 
ATOM   1765  C  CB  . THR B  1 88  ? 6.277  54.127  -15.279  1.00 7.47  ? 88   THR B CB  1 
ATOM   1766  O  OG1 . THR B  1 88  ? 7.142  54.149  -14.133  1.00 8.51  ? 88   THR B OG1 1 
ATOM   1767  C  CG2 . THR B  1 88  ? 5.022  55.013  -14.998  1.00 8.15  ? 88   THR B CG2 1 
ATOM   1768  N  N   . ALA B  1 89  ? 3.695  52.093  -16.469  1.00 6.40  ? 89   ALA B N   1 
ATOM   1769  C  CA  . ALA B  1 89  ? 2.621  52.088  -17.460  1.00 6.80  ? 89   ALA B CA  1 
ATOM   1770  C  C   . ALA B  1 89  ? 1.842  53.407  -17.423  1.00 7.14  ? 89   ALA B C   1 
ATOM   1771  O  O   . ALA B  1 89  ? 1.549  53.936  -16.347  1.00 7.66  ? 89   ALA B O   1 
ATOM   1772  C  CB  . ALA B  1 89  ? 1.675  50.955  -17.210  1.00 6.95  ? 89   ALA B CB  1 
ATOM   1773  N  N   . ASP B  1 90  ? 1.488  53.904  -18.601  1.00 7.76  ? 90   ASP B N   1 
ATOM   1774  C  CA  . ASP B  1 90  ? 0.758  55.165  -18.703  1.00 8.23  ? 90   ASP B CA  1 
ATOM   1775  C  C   . ASP B  1 90  ? -0.747 54.923  -18.574  1.00 9.13  ? 90   ASP B C   1 
ATOM   1776  O  O   . ASP B  1 90  ? -1.183 53.792  -18.301  1.00 7.29  ? 90   ASP B O   1 
ATOM   1777  C  CB  . ASP B  1 90  ? 1.135  55.904  -19.996  1.00 8.11  ? 90   ASP B CB  1 
ATOM   1778  C  CG  . ASP B  1 90  ? 0.711  55.156  -21.268  1.00 8.01  ? 90   ASP B CG  1 
ATOM   1779  O  OD1 . ASP B  1 90  ? 1.167  55.557  -22.350  1.00 8.00  ? 90   ASP B OD1 1 
ATOM   1780  O  OD2 . ASP B  1 90  ? -0.076 54.171  -21.204  1.00 8.49  ? 90   ASP B OD2 1 
ATOM   1781  N  N   . LYS B  1 91  ? -1.539 55.981  -18.792  1.00 9.67  ? 91   LYS B N   1 
ATOM   1782  C  CA  . LYS B  1 91  ? -2.991 55.921  -18.632  1.00 11.68 ? 91   LYS B CA  1 
ATOM   1783  C  C   . LYS B  1 91  ? -3.688 54.961  -19.603  1.00 11.45 ? 91   LYS B C   1 
ATOM   1784  O  O   . LYS B  1 91  ? -4.875 54.665  -19.425  1.00 12.92 ? 91   LYS B O   1 
ATOM   1785  C  CB  . LYS B  1 91  ? -3.600 57.330  -18.794  1.00 12.25 ? 91   LYS B CB  1 
ATOM   1786  C  CG  . LYS B  1 91  ? -3.491 57.841  -20.244  1.00 15.85 ? 91   LYS B CG  1 
ATOM   1787  C  CD  . LYS B  1 91  ? -3.836 59.313  -20.401  1.00 20.82 ? 91   LYS B CD  1 
ATOM   1788  C  CE  . LYS B  1 91  ? -3.763 59.738  -21.872  1.00 22.80 ? 91   LYS B CE  1 
ATOM   1789  N  NZ  . LYS B  1 91  ? -4.636 58.916  -22.774  1.00 23.77 ? 91   LYS B NZ  1 
ATOM   1790  N  N   . ASP B  1 92  ? -2.977 54.535  -20.645  1.00 10.62 ? 92   ASP B N   1 
ATOM   1791  C  CA  . ASP B  1 92  ? -3.479 53.567  -21.630  1.00 10.57 ? 92   ASP B CA  1 
ATOM   1792  C  C   . ASP B  1 92  ? -3.021 52.147  -21.298  1.00 9.29  ? 92   ASP B C   1 
ATOM   1793  O  O   . ASP B  1 92  ? -3.390 51.180  -21.989  1.00 9.81  ? 92   ASP B O   1 
ATOM   1794  C  CB  . ASP B  1 92  ? -3.015 53.913  -23.049  1.00 10.72 ? 92   ASP B CB  1 
ATOM   1795  C  CG  . ASP B  1 92  ? -3.602 55.215  -23.572  1.00 13.76 ? 92   ASP B CG  1 
ATOM   1796  O  OD1 . ASP B  1 92  ? -2.883 55.915  -24.312  1.00 17.79 ? 92   ASP B OD1 1 
ATOM   1797  O  OD2 . ASP B  1 92  ? -4.756 55.539  -23.249  1.00 13.22 ? 92   ASP B OD2 1 
ATOM   1798  N  N   . GLY B  1 93  ? -2.226 52.013  -20.244  1.00 8.11  ? 93   GLY B N   1 
ATOM   1799  C  CA  . GLY B  1 93  ? -1.746 50.700  -19.826  1.00 7.53  ? 93   GLY B CA  1 
ATOM   1800  C  C   . GLY B  1 93  ? -0.455 50.276  -20.505  1.00 6.57  ? 93   GLY B C   1 
ATOM   1801  O  O   . GLY B  1 93  ? -0.062 49.119  -20.437  1.00 5.22  ? 93   GLY B O   1 
ATOM   1802  N  N   . VAL B  1 94  ? 0.213  51.230  -21.136  1.00 6.13  ? 94   VAL B N   1 
ATOM   1803  C  CA  . VAL B  1 94  ? 1.448  50.966  -21.893  1.00 5.98  ? 94   VAL B CA  1 
ATOM   1804  C  C   . VAL B  1 94  ? 2.683  51.485  -21.174  1.00 5.94  ? 94   VAL B C   1 
ATOM   1805  O  O   . VAL B  1 94  ? 2.737  52.657  -20.765  1.00 5.15  ? 94   VAL B O   1 
ATOM   1806  C  CB  . VAL B  1 94  ? 1.396  51.572  -23.330  1.00 5.68  ? 94   VAL B CB  1 
ATOM   1807  C  CG1 . VAL B  1 94  ? 2.684  51.263  -24.092  1.00 8.14  ? 94   VAL B CG1 1 
ATOM   1808  C  CG2 . VAL B  1 94  ? 0.179  50.993  -24.100  1.00 6.93  ? 94   VAL B CG2 1 
ATOM   1809  N  N   . ALA B  1 95  ? 3.670  50.604  -20.995  1.00 5.31  ? 95   ALA B N   1 
ATOM   1810  C  CA  . ALA B  1 95  ? 4.940  50.989  -20.397  1.00 6.08  ? 95   ALA B CA  1 
ATOM   1811  C  C   . ALA B  1 95  ? 6.013  51.016  -21.470  1.00 7.58  ? 95   ALA B C   1 
ATOM   1812  O  O   . ALA B  1 95  ? 6.311  49.982  -22.074  1.00 7.59  ? 95   ALA B O   1 
ATOM   1813  C  CB  . ALA B  1 95  ? 5.334  49.988  -19.269  1.00 6.21  ? 95   ALA B CB  1 
ATOM   1814  N  N   . ASP B  1 96  ? 6.578  52.197  -21.718  1.00 7.70  ? 96   ASP B N   1 
ATOM   1815  C  CA  . ASP B  1 96  ? 7.728  52.368  -22.599  1.00 9.50  ? 96   ASP B CA  1 
ATOM   1816  C  C   . ASP B  1 96  ? 8.983  52.060  -21.768  1.00 8.51  ? 96   ASP B C   1 
ATOM   1817  O  O   . ASP B  1 96  ? 9.306  52.790  -20.831  1.00 8.79  ? 96   ASP B O   1 
ATOM   1818  C  CB  . ASP B  1 96  ? 7.732  53.822  -23.116  1.00 9.92  ? 96   ASP B CB  1 
ATOM   1819  C  CG  . ASP B  1 96  ? 8.921  54.164  -24.009  1.00 16.64 ? 96   ASP B CG  1 
ATOM   1820  O  OD1 . ASP B  1 96  ? 9.854  53.355  -24.202  1.00 21.68 ? 96   ASP B OD1 1 
ATOM   1821  O  OD2 . ASP B  1 96  ? 8.926  55.315  -24.524  1.00 23.34 ? 96   ASP B OD2 1 
ATOM   1822  N  N   . VAL B  1 97  ? 9.659  50.956  -22.065  1.00 7.13  ? 97   VAL B N   1 
ATOM   1823  C  CA  . VAL B  1 97  ? 10.785 50.566  -21.206  1.00 6.84  ? 97   VAL B CA  1 
ATOM   1824  C  C   . VAL B  1 97  ? 12.060 51.134  -21.784  1.00 6.38  ? 97   VAL B C   1 
ATOM   1825  O  O   . VAL B  1 97  ? 12.319 50.995  -22.973  1.00 4.78  ? 97   VAL B O   1 
ATOM   1826  C  CB  . VAL B  1 97  ? 10.889 49.032  -21.033  1.00 6.64  ? 97   VAL B CB  1 
ATOM   1827  C  CG1 . VAL B  1 97  ? 12.048 48.677  -20.107  1.00 6.77  ? 97   VAL B CG1 1 
ATOM   1828  C  CG2 . VAL B  1 97  ? 9.571  48.453  -20.463  1.00 6.24  ? 97   VAL B CG2 1 
ATOM   1829  N  N   . SER B  1 98  ? 12.858 51.773  -20.935  1.00 7.12  ? 98   SER B N   1 
ATOM   1830  C  CA  . SER B  1 98  ? 14.144 52.317  -21.349  1.00 8.27  ? 98   SER B CA  1 
ATOM   1831  C  C   . SER B  1 98  ? 15.057 52.341  -20.126  1.00 8.50  ? 98   SER B C   1 
ATOM   1832  O  O   . SER B  1 98  ? 14.890 53.164  -19.221  1.00 8.83  ? 98   SER B O   1 
ATOM   1833  C  CB  . SER B  1 98  ? 13.983 53.723  -21.949  1.00 8.91  ? 98   SER B CB  1 
ATOM   1834  O  OG  . SER B  1 98  ? 15.264 54.256  -22.273  1.00 12.00 ? 98   SER B OG  1 
ATOM   1835  N  N   . ILE B  1 99  ? 16.013 51.414  -20.109  1.00 7.20  ? 99   ILE B N   1 
ATOM   1836  C  CA  . ILE B  1 99  ? 16.851 51.138  -18.936  1.00 7.58  ? 99   ILE B CA  1 
ATOM   1837  C  C   . ILE B  1 99  ? 18.287 50.974  -19.422  1.00 7.58  ? 99   ILE B C   1 
ATOM   1838  O  O   . ILE B  1 99  ? 18.543 50.461  -20.517  1.00 6.48  ? 99   ILE B O   1 
ATOM   1839  C  CB  . ILE B  1 99  ? 16.387 49.823  -18.210  1.00 6.91  ? 99   ILE B CB  1 
ATOM   1840  C  CG1 . ILE B  1 99  ? 15.077 50.060  -17.432  1.00 8.11  ? 99   ILE B CG1 1 
ATOM   1841  C  CG2 . ILE B  1 99  ? 17.451 49.286  -17.226  1.00 8.21  ? 99   ILE B CG2 1 
ATOM   1842  C  CD1 . ILE B  1 99  ? 14.431 48.770  -16.900  1.00 8.98  ? 99   ILE B CD1 1 
ATOM   1843  N  N   . GLU B  1 100 ? 19.228 51.471  -18.631  1.00 8.13  ? 100  GLU B N   1 
ATOM   1844  C  CA  . GLU B  1 100 ? 20.618 51.115  -18.830  1.00 8.36  ? 100  GLU B CA  1 
ATOM   1845  C  C   . GLU B  1 100 ? 21.112 50.550  -17.522  1.00 7.37  ? 100  GLU B C   1 
ATOM   1846  O  O   . GLU B  1 100 ? 20.919 51.167  -16.471  1.00 6.94  ? 100  GLU B O   1 
ATOM   1847  C  CB  . GLU B  1 100 ? 21.457 52.331  -19.203  1.00 9.46  ? 100  GLU B CB  1 
ATOM   1848  C  CG  . GLU B  1 100 ? 22.831 51.937  -19.663  1.00 13.73 ? 100  GLU B CG  1 
ATOM   1849  C  CD  . GLU B  1 100 ? 22.915 51.777  -21.169  1.00 19.92 ? 100  GLU B CD  1 
ATOM   1850  O  OE1 . GLU B  1 100 ? 21.863 51.846  -21.847  1.00 23.01 ? 100  GLU B OE1 1 
ATOM   1851  O  OE2 . GLU B  1 100 ? 24.043 51.619  -21.676  1.00 24.15 ? 100  GLU B OE2 1 
ATOM   1852  N  N   . ASP B  1 101 ? 21.759 49.389  -17.587  1.00 6.44  ? 101  ASP B N   1 
ATOM   1853  C  CA  . ASP B  1 101 ? 22.221 48.704  -16.379  1.00 6.34  ? 101  ASP B CA  1 
ATOM   1854  C  C   . ASP B  1 101 ? 23.648 48.159  -16.510  1.00 6.25  ? 101  ASP B C   1 
ATOM   1855  O  O   . ASP B  1 101 ? 23.984 47.524  -17.508  1.00 5.49  ? 101  ASP B O   1 
ATOM   1856  C  CB  . ASP B  1 101 ? 21.264 47.555  -15.993  1.00 6.45  ? 101  ASP B CB  1 
ATOM   1857  C  CG  . ASP B  1 101 ? 21.470 47.089  -14.551  1.00 5.56  ? 101  ASP B CG  1 
ATOM   1858  O  OD1 . ASP B  1 101 ? 22.129 46.058  -14.302  1.00 3.58  ? 101  ASP B OD1 1 
ATOM   1859  O  OD2 . ASP B  1 101 ? 21.008 47.788  -13.648  1.00 7.76  ? 101  ASP B OD2 1 
ATOM   1860  N  N   . SER B  1 102 ? 24.472 48.371  -15.490  1.00 5.99  ? 102  SER B N   1 
ATOM   1861  C  CA  . SER B  1 102 ? 25.867 47.906  -15.550  1.00 6.63  ? 102  SER B CA  1 
ATOM   1862  C  C   . SER B  1 102 ? 26.133 46.628  -14.746  1.00 6.35  ? 102  SER B C   1 
ATOM   1863  O  O   . SER B  1 102 ? 27.292 46.237  -14.579  1.00 6.58  ? 102  SER B O   1 
ATOM   1864  C  CB  . SER B  1 102 ? 26.800 49.009  -15.052  1.00 7.30  ? 102  SER B CB  1 
ATOM   1865  O  OG  . SER B  1 102 ? 26.648 50.140  -15.876  1.00 10.32 ? 102  SER B OG  1 
ATOM   1866  N  N   . VAL B  1 103 ? 25.077 46.026  -14.192  1.00 5.14  ? 103  VAL B N   1 
ATOM   1867  C  CA  . VAL B  1 103 ? 25.236 44.842  -13.330  1.00 4.50  ? 103  VAL B CA  1 
ATOM   1868  C  C   . VAL B  1 103 ? 24.885 43.585  -14.116  1.00 4.05  ? 103  VAL B C   1 
ATOM   1869  O  O   . VAL B  1 103 ? 25.647 42.612  -14.120  1.00 4.13  ? 103  VAL B O   1 
ATOM   1870  C  CB  . VAL B  1 103 ? 24.420 44.950  -11.997  1.00 4.12  ? 103  VAL B CB  1 
ATOM   1871  C  CG1 . VAL B  1 103 ? 24.447 43.635  -11.181  1.00 4.73  ? 103  VAL B CG1 1 
ATOM   1872  C  CG2 . VAL B  1 103 ? 24.966 46.098  -11.134  1.00 4.70  ? 103  VAL B CG2 1 
ATOM   1873  N  N   . ILE B  1 104 ? 23.755 43.620  -14.815  1.00 3.59  ? 104  ILE B N   1 
ATOM   1874  C  CA  . ILE B  1 104 ? 23.438 42.512  -15.744  1.00 3.36  ? 104  ILE B CA  1 
ATOM   1875  C  C   . ILE B  1 104 ? 24.421 42.480  -16.909  1.00 3.37  ? 104  ILE B C   1 
ATOM   1876  O  O   . ILE B  1 104 ? 24.998 43.505  -17.287  1.00 2.63  ? 104  ILE B O   1 
ATOM   1877  C  CB  . ILE B  1 104 ? 21.994 42.592  -16.303  1.00 3.30  ? 104  ILE B CB  1 
ATOM   1878  C  CG1 . ILE B  1 104 ? 21.734 43.929  -17.025  1.00 3.14  ? 104  ILE B CG1 1 
ATOM   1879  C  CG2 . ILE B  1 104 ? 20.978 42.380  -15.157  1.00 4.38  ? 104  ILE B CG2 1 
ATOM   1880  C  CD1 . ILE B  1 104 ? 20.603 43.844  -18.035  1.00 4.45  ? 104  ILE B CD1 1 
ATOM   1881  N  N   . SER B  1 105 ? 24.589 41.299  -17.511  1.00 3.11  ? 105  SER B N   1 
ATOM   1882  C  CA  . SER B  1 105 ? 25.446 41.168  -18.681  1.00 3.40  ? 105  SER B CA  1 
ATOM   1883  C  C   . SER B  1 105 ? 24.866 40.138  -19.627  1.00 3.55  ? 105  SER B C   1 
ATOM   1884  O  O   . SER B  1 105 ? 24.175 39.208  -19.184  1.00 5.48  ? 105  SER B O   1 
ATOM   1885  C  CB  . SER B  1 105 ? 26.888 40.787  -18.306  1.00 3.24  ? 105  SER B CB  1 
ATOM   1886  O  OG  . SER B  1 105 ? 27.728 40.864  -19.448  1.00 3.39  ? 105  SER B OG  1 
ATOM   1887  N  N   . LEU B  1 106 ? 25.176 40.288  -20.911  1.00 3.50  ? 106  LEU B N   1 
ATOM   1888  C  CA  . LEU B  1 106 ? 24.733 39.338  -21.943  1.00 3.88  ? 106  LEU B CA  1 
ATOM   1889  C  C   . LEU B  1 106 ? 25.810 38.280  -22.214  1.00 5.28  ? 106  LEU B C   1 
ATOM   1890  O  O   . LEU B  1 106 ? 25.646 37.418  -23.068  1.00 5.22  ? 106  LEU B O   1 
ATOM   1891  C  CB  . LEU B  1 106 ? 24.341 40.056  -23.221  1.00 2.99  ? 106  LEU B CB  1 
ATOM   1892  C  CG  . LEU B  1 106 ? 23.221 41.105  -23.105  1.00 2.98  ? 106  LEU B CG  1 
ATOM   1893  C  CD1 . LEU B  1 106 ? 22.799 41.676  -24.487  1.00 4.27  ? 106  LEU B CD1 1 
ATOM   1894  C  CD2 . LEU B  1 106 ? 22.009 40.554  -22.330  1.00 3.48  ? 106  LEU B CD2 1 
ATOM   1895  N  N   . SER B  1 107 ? 26.917 38.359  -21.490  1.00 6.05  ? 107  SER B N   1 
ATOM   1896  C  CA  . SER B  1 107 ? 27.967 37.349  -21.637  1.00 6.66  ? 107  SER B CA  1 
ATOM   1897  C  C   . SER B  1 107 ? 28.680 37.098  -20.305  1.00 7.83  ? 107  SER B C   1 
ATOM   1898  O  O   . SER B  1 107 ? 28.440 37.777  -19.306  1.00 6.89  ? 107  SER B O   1 
ATOM   1899  C  CB  . SER B  1 107 ? 28.959 37.744  -22.741  1.00 7.16  ? 107  SER B CB  1 
ATOM   1900  O  OG  . SER B  1 107 ? 29.644 38.957  -22.442  1.00 6.75  ? 107  SER B OG  1 
ATOM   1901  N  N   . GLY B  1 108 ? 29.549 36.091  -20.299  1.00 8.14  ? 108  GLY B N   1 
ATOM   1902  C  CA  . GLY B  1 108 ? 30.354 35.808  -19.142  1.00 10.40 ? 108  GLY B CA  1 
ATOM   1903  C  C   . GLY B  1 108 ? 29.623 34.861  -18.250  1.00 11.35 ? 108  GLY B C   1 
ATOM   1904  O  O   . GLY B  1 108 ? 28.466 34.531  -18.507  1.00 12.27 ? 108  GLY B O   1 
ATOM   1905  N  N   . ASP B  1 109 ? 30.289 34.410  -17.197  1.00 12.61 ? 109  ASP B N   1 
ATOM   1906  C  CA  . ASP B  1 109 ? 29.756 33.299  -16.423  1.00 14.22 ? 109  ASP B CA  1 
ATOM   1907  C  C   . ASP B  1 109 ? 28.531 33.619  -15.562  1.00 14.33 ? 109  ASP B C   1 
ATOM   1908  O  O   . ASP B  1 109 ? 27.957 32.709  -14.947  1.00 15.49 ? 109  ASP B O   1 
ATOM   1909  C  CB  . ASP B  1 109 ? 30.854 32.591  -15.612  1.00 14.73 ? 109  ASP B CB  1 
ATOM   1910  C  CG  . ASP B  1 109 ? 31.384 33.418  -14.483  1.00 17.23 ? 109  ASP B CG  1 
ATOM   1911  O  OD1 . ASP B  1 109 ? 30.828 34.489  -14.173  1.00 21.05 ? 109  ASP B OD1 1 
ATOM   1912  O  OD2 . ASP B  1 109 ? 32.392 32.986  -13.886  1.00 24.44 ? 109  ASP B OD2 1 
ATOM   1913  N  N   . HIS B  1 110 ? 28.130 34.889  -15.534  1.00 13.81 ? 110  HIS B N   1 
ATOM   1914  C  CA  . HIS B  1 110 ? 26.860 35.299  -14.902  1.00 13.23 ? 110  HIS B CA  1 
ATOM   1915  C  C   . HIS B  1 110 ? 25.881 36.019  -15.857  1.00 12.26 ? 110  HIS B C   1 
ATOM   1916  O  O   . HIS B  1 110 ? 25.068 36.864  -15.434  1.00 12.42 ? 110  HIS B O   1 
ATOM   1917  C  CB  . HIS B  1 110 ? 27.108 36.159  -13.666  1.00 13.71 ? 110  HIS B CB  1 
ATOM   1918  C  CG  . HIS B  1 110 ? 27.821 35.445  -12.561  1.00 15.41 ? 110  HIS B CG  1 
ATOM   1919  N  ND1 . HIS B  1 110 ? 28.736 36.073  -11.741  1.00 18.64 ? 110  HIS B ND1 1 
ATOM   1920  C  CD2 . HIS B  1 110 ? 27.785 34.149  -12.163  1.00 16.93 ? 110  HIS B CD2 1 
ATOM   1921  C  CE1 . HIS B  1 110 ? 29.222 35.196  -10.879  1.00 18.05 ? 110  HIS B CE1 1 
ATOM   1922  N  NE2 . HIS B  1 110 ? 28.664 34.021  -11.116  1.00 17.00 ? 110  HIS B NE2 1 
HETATM 1923  N  N   . CME B  1 111 ? 25.951 35.692  -17.143  1.00 10.99 ? 111  CME B N   1 
HETATM 1924  C  CA  . CME B  1 111 ? 25.032 36.258  -18.144  1.00 9.20  ? 111  CME B CA  1 
HETATM 1925  C  CB  . CME B  1 111 ? 25.420 35.813  -19.567  1.00 10.15 ? 111  CME B CB  1 
HETATM 1926  S  SG  . CME B  1 111 ? 24.965 34.141  -19.935  1.00 14.36 ? 111  CME B SG  1 
HETATM 1927  S  SD  . CME B  1 111 ? 25.672 33.791  -21.792  1.00 15.45 ? 111  CME B SD  1 
HETATM 1928  C  CE  . CME B  1 111 ? 27.329 33.215  -21.534  1.00 18.24 ? 111  CME B CE  1 
HETATM 1929  C  CZ  . CME B  1 111 ? 27.441 32.177  -20.425  1.00 20.30 ? 111  CME B CZ  1 
HETATM 1930  O  OH  . CME B  1 111 ? 26.890 30.932  -20.872  1.00 21.81 ? 111  CME B OH  1 
HETATM 1931  C  C   . CME B  1 111 ? 23.568 35.973  -17.886  1.00 7.40  ? 111  CME B C   1 
HETATM 1932  O  O   . CME B  1 111 ? 23.235 35.020  -17.151  1.00 6.41  ? 111  CME B O   1 
ATOM   1933  N  N   . ILE B  1 112 ? 22.683 36.768  -18.497  1.00 5.00  ? 112  ILE B N   1 
ATOM   1934  C  CA  . ILE B  1 112 ? 21.235 36.592  -18.311  1.00 5.17  ? 112  ILE B CA  1 
ATOM   1935  C  C   . ILE B  1 112 ? 20.549 35.857  -19.462  1.00 5.02  ? 112  ILE B C   1 
ATOM   1936  O  O   . ILE B  1 112 ? 19.319 35.704  -19.459  1.00 5.45  ? 112  ILE B O   1 
ATOM   1937  C  CB  . ILE B  1 112 ? 20.483 37.921  -18.042  1.00 3.95  ? 112  ILE B CB  1 
ATOM   1938  C  CG1 . ILE B  1 112 ? 20.560 38.855  -19.287  1.00 5.86  ? 112  ILE B CG1 1 
ATOM   1939  C  CG2 . ILE B  1 112 ? 20.996 38.559  -16.678  1.00 5.61  ? 112  ILE B CG2 1 
ATOM   1940  C  CD1 . ILE B  1 112 ? 19.816 40.213  -19.160  1.00 3.40  ? 112  ILE B CD1 1 
ATOM   1941  N  N   . ILE B  1 113 ? 21.343 35.411  -20.436  1.00 5.47  ? 113  ILE B N   1 
ATOM   1942  C  CA  . ILE B  1 113 ? 20.834 34.645  -21.577  1.00 5.26  ? 113  ILE B CA  1 
ATOM   1943  C  C   . ILE B  1 113 ? 20.283 33.343  -21.018  1.00 4.31  ? 113  ILE B C   1 
ATOM   1944  O  O   . ILE B  1 113 ? 20.936 32.696  -20.201  1.00 4.30  ? 113  ILE B O   1 
ATOM   1945  C  CB  . ILE B  1 113 ? 22.005 34.287  -22.595  1.00 6.08  ? 113  ILE B CB  1 
ATOM   1946  C  CG1 . ILE B  1 113 ? 22.687 35.547  -23.114  1.00 7.85  ? 113  ILE B CG1 1 
ATOM   1947  C  CG2 . ILE B  1 113 ? 21.505 33.390  -23.764  1.00 3.88  ? 113  ILE B CG2 1 
ATOM   1948  C  CD1 . ILE B  1 113 ? 21.740 36.525  -23.856  1.00 7.83  ? 113  ILE B CD1 1 
ATOM   1949  N  N   . GLY B  1 114 ? 19.073 32.975  -21.447  1.00 3.55  ? 114  GLY B N   1 
ATOM   1950  C  CA  . GLY B  1 114 ? 18.476 31.741  -21.021  1.00 3.39  ? 114  GLY B CA  1 
ATOM   1951  C  C   . GLY B  1 114 ? 17.816 31.833  -19.674  1.00 3.31  ? 114  GLY B C   1 
ATOM   1952  O  O   . GLY B  1 114 ? 17.353 30.826  -19.160  1.00 2.78  ? 114  GLY B O   1 
ATOM   1953  N  N   . ARG B  1 115 ? 17.752 33.038  -19.100  1.00 3.34  ? 115  ARG B N   1 
ATOM   1954  C  CA  . ARG B  1 115 ? 16.984 33.242  -17.890  1.00 3.16  ? 115  ARG B CA  1 
ATOM   1955  C  C   . ARG B  1 115 ? 15.637 33.876  -18.236  1.00 3.24  ? 115  ARG B C   1 
ATOM   1956  O  O   . ARG B  1 115 ? 15.336 34.099  -19.401  1.00 3.86  ? 115  ARG B O   1 
ATOM   1957  C  CB  . ARG B  1 115 ? 17.817 34.040  -16.884  1.00 2.99  ? 115  ARG B CB  1 
ATOM   1958  C  CG  . ARG B  1 115 ? 19.150 33.332  -16.699  1.00 3.49  ? 115  ARG B CG  1 
ATOM   1959  C  CD  . ARG B  1 115 ? 19.837 33.601  -15.437  1.00 7.45  ? 115  ARG B CD  1 
ATOM   1960  N  NE  . ARG B  1 115 ? 21.147 32.945  -15.437  1.00 8.06  ? 115  ARG B NE  1 
ATOM   1961  C  CZ  . ARG B  1 115 ? 21.461 31.856  -14.740  1.00 6.28  ? 115  ARG B CZ  1 
ATOM   1962  N  NH1 . ARG B  1 115 ? 22.716 31.368  -14.776  1.00 7.30  ? 115  ARG B NH1 1 
ATOM   1963  N  NH2 . ARG B  1 115 ? 20.564 31.284  -13.955  1.00 6.21  ? 115  ARG B NH2 1 
ATOM   1964  N  N   . THR B  1 116 ? 14.806 34.129  -17.236  1.00 3.49  ? 116  THR B N   1 
ATOM   1965  C  CA  . THR B  1 116 ? 13.462 34.630  -17.511  1.00 3.34  ? 116  THR B CA  1 
ATOM   1966  C  C   . THR B  1 116 ? 13.308 36.092  -17.098  1.00 3.22  ? 116  THR B C   1 
ATOM   1967  O  O   . THR B  1 116 ? 13.658 36.437  -15.986  1.00 4.65  ? 116  THR B O   1 
ATOM   1968  C  CB  . THR B  1 116 ? 12.407 33.813  -16.781  1.00 3.93  ? 116  THR B CB  1 
ATOM   1969  O  OG1 . THR B  1 116 ? 12.415 32.471  -17.276  1.00 4.08  ? 116  THR B OG1 1 
ATOM   1970  C  CG2 . THR B  1 116 ? 11.019 34.406  -16.980  1.00 3.61  ? 116  THR B CG2 1 
ATOM   1971  N  N   . LEU B  1 117 ? 12.741 36.928  -17.975  1.00 2.81  ? 117  LEU B N   1 
ATOM   1972  C  CA  . LEU B  1 117 ? 12.390 38.317  -17.605  1.00 2.00  ? 117  LEU B CA  1 
ATOM   1973  C  C   . LEU B  1 117 ? 10.927 38.308  -17.135  1.00 2.48  ? 117  LEU B C   1 
ATOM   1974  O  O   . LEU B  1 117 ? 10.104 37.648  -17.764  1.00 2.91  ? 117  LEU B O   1 
ATOM   1975  C  CB  . LEU B  1 117 ? 12.588 39.258  -18.806  1.00 2.00  ? 117  LEU B CB  1 
ATOM   1976  C  CG  . LEU B  1 117 ? 12.337 40.766  -18.576  1.00 2.00  ? 117  LEU B CG  1 
ATOM   1977  C  CD1 . LEU B  1 117 ? 13.356 41.304  -17.582  1.00 3.01  ? 117  LEU B CD1 1 
ATOM   1978  C  CD2 . LEU B  1 117 ? 12.388 41.563  -19.916  1.00 2.00  ? 117  LEU B CD2 1 
ATOM   1979  N  N   . VAL B  1 118 ? 10.615 38.998  -16.040  1.00 2.00  ? 118  VAL B N   1 
ATOM   1980  C  CA  . VAL B  1 118 ? 9.264  39.002  -15.456  1.00 2.66  ? 118  VAL B CA  1 
ATOM   1981  C  C   . VAL B  1 118 ? 8.793  40.424  -15.226  1.00 2.54  ? 118  VAL B C   1 
ATOM   1982  O  O   . VAL B  1 118 ? 9.565  41.257  -14.753  1.00 2.86  ? 118  VAL B O   1 
ATOM   1983  C  CB  . VAL B  1 118 ? 9.210  38.217  -14.106  1.00 2.00  ? 118  VAL B CB  1 
ATOM   1984  C  CG1 . VAL B  1 118 ? 7.795  38.223  -13.507  1.00 2.74  ? 118  VAL B CG1 1 
ATOM   1985  C  CG2 . VAL B  1 118 ? 9.655  36.778  -14.311  1.00 4.63  ? 118  VAL B CG2 1 
ATOM   1986  N  N   . VAL B  1 119 ? 7.550  40.713  -15.599  1.00 2.59  ? 119  VAL B N   1 
ATOM   1987  C  CA  . VAL B  1 119 ? 6.916  41.975  -15.205  1.00 2.78  ? 119  VAL B CA  1 
ATOM   1988  C  C   . VAL B  1 119 ? 5.764  41.666  -14.251  1.00 3.03  ? 119  VAL B C   1 
ATOM   1989  O  O   . VAL B  1 119 ? 4.953  40.726  -14.493  1.00 2.27  ? 119  VAL B O   1 
ATOM   1990  C  CB  . VAL B  1 119 ? 6.479  42.854  -16.413  1.00 2.85  ? 119  VAL B CB  1 
ATOM   1991  C  CG1 . VAL B  1 119 ? 5.382  42.163  -17.296  1.00 2.59  ? 119  VAL B CG1 1 
ATOM   1992  C  CG2 . VAL B  1 119 ? 5.955  44.212  -15.914  1.00 3.78  ? 119  VAL B CG2 1 
ATOM   1993  N  N   . HIS B  1 120 ? 5.681  42.470  -13.192  1.00 3.37  ? 120  HIS B N   1 
ATOM   1994  C  CA  . HIS B  1 120 ? 4.856  42.159  -12.027  1.00 3.29  ? 120  HIS B CA  1 
ATOM   1995  C  C   . HIS B  1 120 ? 3.580  42.980  -11.857  1.00 3.72  ? 120  HIS B C   1 
ATOM   1996  O  O   . HIS B  1 120 ? 3.395  44.020  -12.483  1.00 4.41  ? 120  HIS B O   1 
ATOM   1997  C  CB  . HIS B  1 120 ? 5.712  42.331  -10.767  1.00 3.10  ? 120  HIS B CB  1 
ATOM   1998  C  CG  . HIS B  1 120 ? 6.687  41.215  -10.543  1.00 3.50  ? 120  HIS B CG  1 
ATOM   1999  N  ND1 . HIS B  1 120 ? 6.369  40.085  -9.821   1.00 2.48  ? 120  HIS B ND1 1 
ATOM   2000  C  CD2 . HIS B  1 120 ? 7.979  41.068  -10.923  1.00 2.67  ? 120  HIS B CD2 1 
ATOM   2001  C  CE1 . HIS B  1 120 ? 7.427  39.291  -9.758   1.00 2.43  ? 120  HIS B CE1 1 
ATOM   2002  N  NE2 . HIS B  1 120 ? 8.407  39.856  -10.438  1.00 2.10  ? 120  HIS B NE2 1 
ATOM   2003  N  N   . GLU B  1 121 ? 2.721  42.477  -10.977  1.00 4.52  ? 121  GLU B N   1 
ATOM   2004  C  CA  . GLU B  1 121 ? 1.403  43.026  -10.659  1.00 5.23  ? 121  GLU B CA  1 
ATOM   2005  C  C   . GLU B  1 121 ? 1.504  44.379  -9.971   1.00 6.12  ? 121  GLU B C   1 
ATOM   2006  O  O   . GLU B  1 121 ? 0.709  45.294  -10.239  1.00 6.50  ? 121  GLU B O   1 
ATOM   2007  C  CB  . GLU B  1 121 ? 0.713  42.003  -9.731   1.00 5.90  ? 121  GLU B CB  1 
ATOM   2008  C  CG  . GLU B  1 121 ? -0.570 42.456  -9.020   1.00 8.51  ? 121  GLU B CG  1 
ATOM   2009  C  CD  . GLU B  1 121 ? -0.955 41.532  -7.849   1.00 13.35 ? 121  GLU B CD  1 
ATOM   2010  O  OE1 . GLU B  1 121 ? -2.154 41.556  -7.458   1.00 15.20 ? 121  GLU B OE1 1 
ATOM   2011  O  OE2 . GLU B  1 121 ? -0.078 40.807  -7.299   1.00 8.41  ? 121  GLU B OE2 1 
ATOM   2012  N  N   . LYS B  1 122 ? 2.474  44.493  -9.075   1.00 5.88  ? 122  LYS B N   1 
ATOM   2013  C  CA  . LYS B  1 122 ? 2.608  45.634  -8.181   1.00 7.08  ? 122  LYS B CA  1 
ATOM   2014  C  C   . LYS B  1 122 ? 3.972  46.300  -8.326   1.00 5.76  ? 122  LYS B C   1 
ATOM   2015  O  O   . LYS B  1 122 ? 4.886  45.755  -8.966   1.00 5.67  ? 122  LYS B O   1 
ATOM   2016  C  CB  . LYS B  1 122 ? 2.483  45.178  -6.711   1.00 6.14  ? 122  LYS B CB  1 
ATOM   2017  C  CG  . LYS B  1 122 ? 1.229  44.381  -6.349   1.00 9.74  ? 122  LYS B CG  1 
ATOM   2018  C  CD  . LYS B  1 122 ? 1.150  44.140  -4.830   1.00 10.80 ? 122  LYS B CD  1 
ATOM   2019  C  CE  . LYS B  1 122 ? -0.039 43.233  -4.502   1.00 17.47 ? 122  LYS B CE  1 
ATOM   2020  N  NZ  . LYS B  1 122 ? 0.032  42.623  -3.133   1.00 16.82 ? 122  LYS B NZ  1 
ATOM   2021  N  N   . ALA B  1 123 ? 4.126  47.443  -7.664   1.00 4.84  ? 123  ALA B N   1 
ATOM   2022  C  CA  . ALA B  1 123 ? 5.411  48.129  -7.637   1.00 4.86  ? 123  ALA B CA  1 
ATOM   2023  C  C   . ALA B  1 123 ? 6.424  47.331  -6.803   1.00 4.84  ? 123  ALA B C   1 
ATOM   2024  O  O   . ALA B  1 123 ? 6.084  46.694  -5.775   1.00 4.37  ? 123  ALA B O   1 
ATOM   2025  C  CB  . ALA B  1 123 ? 5.240  49.564  -7.070   1.00 5.59  ? 123  ALA B CB  1 
ATOM   2026  N  N   . ASP B  1 124 ? 7.678  47.371  -7.247   1.00 4.93  ? 124  ASP B N   1 
ATOM   2027  C  CA  . ASP B  1 124 ? 8.809  46.870  -6.485   1.00 4.60  ? 124  ASP B CA  1 
ATOM   2028  C  C   . ASP B  1 124 ? 9.189  47.941  -5.459   1.00 4.34  ? 124  ASP B C   1 
ATOM   2029  O  O   . ASP B  1 124 ? 9.441  49.082  -5.838   1.00 4.26  ? 124  ASP B O   1 
ATOM   2030  C  CB  . ASP B  1 124 ? 9.953  46.649  -7.485   1.00 4.23  ? 124  ASP B CB  1 
ATOM   2031  C  CG  . ASP B  1 124 ? 11.195 46.038  -6.868   1.00 3.60  ? 124  ASP B CG  1 
ATOM   2032  O  OD1 . ASP B  1 124 ? 11.958 45.444  -7.647   1.00 4.34  ? 124  ASP B OD1 1 
ATOM   2033  O  OD2 . ASP B  1 124 ? 11.459 46.180  -5.647   1.00 5.52  ? 124  ASP B OD2 1 
ATOM   2034  N  N   . ASP B  1 125 ? 9.218  47.590  -4.172   1.00 5.33  ? 125  ASP B N   1 
ATOM   2035  C  CA  . ASP B  1 125 ? 9.540  48.589  -3.119   1.00 4.47  ? 125  ASP B CA  1 
ATOM   2036  C  C   . ASP B  1 125 ? 11.055 48.783  -2.931   1.00 4.39  ? 125  ASP B C   1 
ATOM   2037  O  O   . ASP B  1 125 ? 11.497 49.448  -1.991   1.00 2.96  ? 125  ASP B O   1 
ATOM   2038  C  CB  . ASP B  1 125 ? 8.823  48.270  -1.784   1.00 5.71  ? 125  ASP B CB  1 
ATOM   2039  C  CG  . ASP B  1 125 ? 9.333  46.988  -1.110   1.00 6.05  ? 125  ASP B CG  1 
ATOM   2040  O  OD1 . ASP B  1 125 ? 8.582  46.431  -0.290   1.00 7.12  ? 125  ASP B OD1 1 
ATOM   2041  O  OD2 . ASP B  1 125 ? 10.456 46.529  -1.393   1.00 6.36  ? 125  ASP B OD2 1 
ATOM   2042  N  N   . LEU B  1 126 ? 11.838 48.222  -3.856   1.00 4.23  ? 126  LEU B N   1 
ATOM   2043  C  CA  . LEU B  1 126 ? 13.305 48.379  -3.905   1.00 5.40  ? 126  LEU B CA  1 
ATOM   2044  C  C   . LEU B  1 126 ? 14.006 47.874  -2.640   1.00 5.88  ? 126  LEU B C   1 
ATOM   2045  O  O   . LEU B  1 126 ? 15.143 48.279  -2.332   1.00 6.43  ? 126  LEU B O   1 
ATOM   2046  C  CB  . LEU B  1 126 ? 13.706 49.826  -4.267   1.00 5.09  ? 126  LEU B CB  1 
ATOM   2047  C  CG  . LEU B  1 126 ? 12.903 50.427  -5.447   1.00 5.84  ? 126  LEU B CG  1 
ATOM   2048  C  CD1 . LEU B  1 126 ? 13.404 51.844  -5.734   1.00 9.43  ? 126  LEU B CD1 1 
ATOM   2049  C  CD2 . LEU B  1 126 ? 12.960 49.568  -6.739   1.00 6.16  ? 126  LEU B CD2 1 
ATOM   2050  N  N   . GLY B  1 127 ? 13.325 46.970  -1.929   1.00 6.53  ? 127  GLY B N   1 
ATOM   2051  C  CA  . GLY B  1 127 ? 13.893 46.332  -0.740   1.00 8.43  ? 127  GLY B CA  1 
ATOM   2052  C  C   . GLY B  1 127 ? 13.827 47.244  0.469    1.00 9.44  ? 127  GLY B C   1 
ATOM   2053  O  O   . GLY B  1 127 ? 14.485 46.994  1.490    1.00 10.00 ? 127  GLY B O   1 
ATOM   2054  N  N   . LYS B  1 128 ? 13.023 48.301  0.366    1.00 9.61  ? 128  LYS B N   1 
ATOM   2055  C  CA  . LYS B  1 128 ? 12.883 49.252  1.465    1.00 11.41 ? 128  LYS B CA  1 
ATOM   2056  C  C   . LYS B  1 128 ? 11.573 49.113  2.244    1.00 11.18 ? 128  LYS B C   1 
ATOM   2057  O  O   . LYS B  1 128 ? 11.224 49.992  3.042    1.00 11.12 ? 128  LYS B O   1 
ATOM   2058  C  CB  . LYS B  1 128 ? 13.038 50.698  0.943    1.00 12.01 ? 128  LYS B CB  1 
ATOM   2059  C  CG  . LYS B  1 128 ? 14.349 50.984  0.198    1.00 14.86 ? 128  LYS B CG  1 
ATOM   2060  C  CD  . LYS B  1 128 ? 15.567 50.797  1.096    1.00 20.91 ? 128  LYS B CD  1 
ATOM   2061  C  CE  . LYS B  1 128 ? 16.753 51.675  0.697    1.00 24.16 ? 128  LYS B CE  1 
ATOM   2062  N  NZ  . LYS B  1 128 ? 17.858 50.920  0.008    1.00 24.86 ? 128  LYS B NZ  1 
ATOM   2063  N  N   . GLY B  1 129 ? 10.865 48.004  2.028    1.00 10.88 ? 129  GLY B N   1 
ATOM   2064  C  CA  . GLY B  1 129 ? 9.533  47.808  2.595    1.00 11.37 ? 129  GLY B CA  1 
ATOM   2065  C  C   . GLY B  1 129 ? 9.433  47.461  4.075    1.00 11.49 ? 129  GLY B C   1 
ATOM   2066  O  O   . GLY B  1 129 ? 8.366  47.591  4.650    1.00 11.86 ? 129  GLY B O   1 
ATOM   2067  N  N   . GLY B  1 130 ? 10.514 46.989  4.686    1.00 11.39 ? 130  GLY B N   1 
ATOM   2068  C  CA  . GLY B  1 130 ? 10.491 46.675  6.140    1.00 10.86 ? 130  GLY B CA  1 
ATOM   2069  C  C   . GLY B  1 130 ? 9.888  45.330  6.564    1.00 10.04 ? 130  GLY B C   1 
ATOM   2070  O  O   . GLY B  1 130 ? 9.633  45.093  7.758    1.00 9.90  ? 130  GLY B O   1 
ATOM   2071  N  N   . ASN B  1 131 ? 9.638  44.449  5.606    1.00 9.04  ? 131  ASN B N   1 
ATOM   2072  C  CA  . ASN B  1 131 ? 9.294  43.056  5.923    1.00 8.66  ? 131  ASN B CA  1 
ATOM   2073  C  C   . ASN B  1 131 ? 10.282 42.124  5.233    1.00 7.59  ? 131  ASN B C   1 
ATOM   2074  O  O   . ASN B  1 131 ? 11.113 42.578  4.432    1.00 6.73  ? 131  ASN B O   1 
ATOM   2075  C  CB  . ASN B  1 131 ? 7.858  42.746  5.528    1.00 9.26  ? 131  ASN B CB  1 
ATOM   2076  C  CG  . ASN B  1 131 ? 7.521  43.298  4.169    1.00 10.39 ? 131  ASN B CG  1 
ATOM   2077  O  OD1 . ASN B  1 131 ? 8.298  43.151  3.226    1.00 8.00  ? 131  ASN B OD1 1 
ATOM   2078  N  ND2 . ASN B  1 131 ? 6.393  44.007  4.078    1.00 15.00 ? 131  ASN B ND2 1 
ATOM   2079  N  N   . GLU B  1 132 ? 10.224 40.834  5.544    1.00 6.66  ? 132  GLU B N   1 
ATOM   2080  C  CA  . GLU B  1 132 ? 11.206 39.910  4.968    1.00 7.20  ? 132  GLU B CA  1 
ATOM   2081  C  C   . GLU B  1 132 ? 11.033 39.842  3.456    1.00 6.59  ? 132  GLU B C   1 
ATOM   2082  O  O   . GLU B  1 132 ? 12.016 39.793  2.726    1.00 7.22  ? 132  GLU B O   1 
ATOM   2083  C  CB  . GLU B  1 132 ? 11.078 38.502  5.536    1.00 7.12  ? 132  GLU B CB  1 
ATOM   2084  C  CG  . GLU B  1 132 ? 12.273 37.599  5.173    1.00 9.25  ? 132  GLU B CG  1 
ATOM   2085  C  CD  . GLU B  1 132 ? 12.067 36.153  5.598    1.00 10.85 ? 132  GLU B CD  1 
ATOM   2086  O  OE1 . GLU B  1 132 ? 12.857 35.286  5.162    1.00 12.92 ? 132  GLU B OE1 1 
ATOM   2087  O  OE2 . GLU B  1 132 ? 11.108 35.878  6.355    1.00 9.05  ? 132  GLU B OE2 1 
ATOM   2088  N  N   . GLU B  1 133 ? 9.785  39.832  3.002    1.00 6.36  ? 133  GLU B N   1 
ATOM   2089  C  CA  . GLU B  1 133 ? 9.515  39.665  1.550    1.00 7.69  ? 133  GLU B CA  1 
ATOM   2090  C  C   . GLU B  1 133 ? 10.115 40.799  0.728    1.00 7.32  ? 133  GLU B C   1 
ATOM   2091  O  O   . GLU B  1 133 ? 10.516 40.597  -0.472   1.00 9.59  ? 133  GLU B O   1 
ATOM   2092  C  CB  . GLU B  1 133 ? 8.009  39.513  1.281    1.00 7.59  ? 133  GLU B CB  1 
ATOM   2093  C  CG  . GLU B  1 133 ? 7.639  39.113  -0.161   1.00 9.41  ? 133  GLU B CG  1 
ATOM   2094  C  CD  . GLU B  1 133 ? 7.954  37.646  -0.521   1.00 12.32 ? 133  GLU B CD  1 
ATOM   2095  O  OE1 . GLU B  1 133 ? 7.350  37.132  -1.484   1.00 11.73 ? 133  GLU B OE1 1 
ATOM   2096  O  OE2 . GLU B  1 133 ? 8.789  36.993  0.135    1.00 12.82 ? 133  GLU B OE2 1 
ATOM   2097  N  N   . SER B  1 134 ? 10.133 42.003  1.299    1.00 6.56  ? 134  SER B N   1 
ATOM   2098  C  CA  . SER B  1 134 ? 10.822 43.123  0.674    1.00 5.86  ? 134  SER B CA  1 
ATOM   2099  C  C   . SER B  1 134 ? 12.270 42.769  0.292    1.00 5.88  ? 134  SER B C   1 
ATOM   2100  O  O   . SER B  1 134 ? 12.719 43.128  -0.794   1.00 5.70  ? 134  SER B O   1 
ATOM   2101  C  CB  . SER B  1 134 ? 10.807 44.370  1.550    1.00 6.76  ? 134  SER B CB  1 
ATOM   2102  O  OG  . SER B  1 134 ? 11.458 45.446  0.873    1.00 4.86  ? 134  SER B OG  1 
ATOM   2103  N  N   . THR B  1 135 ? 12.977 42.059  1.179    1.00 5.37  ? 135  THR B N   1 
ATOM   2104  C  CA  . THR B  1 135 ? 14.375 41.634  0.951    1.00 6.18  ? 135  THR B CA  1 
ATOM   2105  C  C   . THR B  1 135 ? 14.555 40.447  -0.065   1.00 8.31  ? 135  THR B C   1 
ATOM   2106  O  O   . THR B  1 135 ? 15.690 40.093  -0.480   1.00 7.59  ? 135  THR B O   1 
ATOM   2107  C  CB  . THR B  1 135 ? 15.087 41.318  2.288    1.00 7.46  ? 135  THR B CB  1 
ATOM   2108  O  OG1 . THR B  1 135 ? 14.655 40.042  2.779    1.00 6.73  ? 135  THR B OG1 1 
ATOM   2109  C  CG2 . THR B  1 135 ? 14.783 42.439  3.305    1.00 7.09  ? 135  THR B CG2 1 
ATOM   2110  N  N   . LYS B  1 136 ? 13.441 39.914  -0.529   1.00 6.65  ? 136  LYS B N   1 
ATOM   2111  C  CA  . LYS B  1 136 ? 13.471 38.798  -1.473   1.00 6.50  ? 136  LYS B CA  1 
ATOM   2112  C  C   . LYS B  1 136 ? 12.915 39.254  -2.814   1.00 5.32  ? 136  LYS B C   1 
ATOM   2113  O  O   . LYS B  1 136 ? 13.562 39.080  -3.850   1.00 4.53  ? 136  LYS B O   1 
ATOM   2114  C  CB  . LYS B  1 136 ? 12.648 37.653  -0.917   1.00 6.79  ? 136  LYS B CB  1 
ATOM   2115  C  CG  . LYS B  1 136 ? 13.229 37.066  0.366    1.00 10.75 ? 136  LYS B CG  1 
ATOM   2116  C  CD  . LYS B  1 136 ? 12.347 35.903  0.815    1.00 14.18 ? 136  LYS B CD  1 
ATOM   2117  C  CE  . LYS B  1 136 ? 13.120 34.830  1.555    1.00 18.01 ? 136  LYS B CE  1 
ATOM   2118  N  NZ  . LYS B  1 136 ? 12.157 33.757  2.041    1.00 19.41 ? 136  LYS B NZ  1 
ATOM   2119  N  N   . THR B  1 137 ? 11.748 39.910  -2.787   1.00 4.66  ? 137  THR B N   1 
ATOM   2120  C  CA  . THR B  1 137 ? 11.005 40.210  -4.025   1.00 4.94  ? 137  THR B CA  1 
ATOM   2121  C  C   . THR B  1 137 ? 10.628 41.677  -4.221   1.00 4.59  ? 137  THR B C   1 
ATOM   2122  O  O   . THR B  1 137 ? 10.108 42.033  -5.278   1.00 4.65  ? 137  THR B O   1 
ATOM   2123  C  CB  . THR B  1 137 ? 9.684  39.401  -4.119   1.00 6.12  ? 137  THR B CB  1 
ATOM   2124  O  OG1 . THR B  1 137 ? 8.753  39.907  -3.157   1.00 5.57  ? 137  THR B OG1 1 
ATOM   2125  C  CG2 . THR B  1 137 ? 9.937  37.900  -3.867   1.00 5.08  ? 137  THR B CG2 1 
ATOM   2126  N  N   . GLY B  1 138 ? 10.840 42.509  -3.197   1.00 3.73  ? 138  GLY B N   1 
ATOM   2127  C  CA  . GLY B  1 138 ? 10.405 43.911  -3.267   1.00 4.10  ? 138  GLY B CA  1 
ATOM   2128  C  C   . GLY B  1 138 ? 8.899  44.057  -3.157   1.00 4.03  ? 138  GLY B C   1 
ATOM   2129  O  O   . GLY B  1 138 ? 8.352  45.141  -3.405   1.00 4.17  ? 138  GLY B O   1 
ATOM   2130  N  N   . ASN B  1 139 ? 8.237  42.967  -2.788   1.00 4.61  ? 139  ASN B N   1 
ATOM   2131  C  CA  . ASN B  1 139 ? 6.759  42.903  -2.655   1.00 5.30  ? 139  ASN B CA  1 
ATOM   2132  C  C   . ASN B  1 139 ? 6.042  43.234  -3.966   1.00 5.87  ? 139  ASN B C   1 
ATOM   2133  O  O   . ASN B  1 139 ? 4.981  43.889  -3.960   1.00 5.44  ? 139  ASN B O   1 
ATOM   2134  C  CB  . ASN B  1 139 ? 6.273  43.831  -1.527   1.00 5.82  ? 139  ASN B CB  1 
ATOM   2135  C  CG  . ASN B  1 139 ? 6.629  43.313  -0.161   1.00 8.61  ? 139  ASN B CG  1 
ATOM   2136  O  OD1 . ASN B  1 139 ? 6.183  42.222  0.232    1.00 7.04  ? 139  ASN B OD1 1 
ATOM   2137  N  ND2 . ASN B  1 139 ? 7.455  44.076  0.577    1.00 5.07  ? 139  ASN B ND2 1 
ATOM   2138  N  N   . ALA B  1 140 ? 6.636  42.806  -5.087   1.00 5.21  ? 140  ALA B N   1 
ATOM   2139  C  CA  . ALA B  1 140 ? 6.124  43.167  -6.411   1.00 5.74  ? 140  ALA B CA  1 
ATOM   2140  C  C   . ALA B  1 140 ? 4.894  42.355  -6.823   1.00 6.09  ? 140  ALA B C   1 
ATOM   2141  O  O   . ALA B  1 140 ? 4.285  42.633  -7.868   1.00 6.66  ? 140  ALA B O   1 
ATOM   2142  C  CB  . ALA B  1 140 ? 7.232  43.040  -7.468   1.00 5.60  ? 140  ALA B CB  1 
ATOM   2143  N  N   . GLY B  1 141 ? 4.519  41.369  -6.002   1.00 5.78  ? 141  GLY B N   1 
ATOM   2144  C  CA  . GLY B  1 141 ? 3.280  40.618  -6.235   1.00 5.20  ? 141  GLY B CA  1 
ATOM   2145  C  C   . GLY B  1 141 ? 3.393  39.629  -7.379   1.00 4.98  ? 141  GLY B C   1 
ATOM   2146  O  O   . GLY B  1 141 ? 4.488  39.198  -7.745   1.00 4.32  ? 141  GLY B O   1 
ATOM   2147  N  N   . SER B  1 142 ? 2.261  39.317  -7.999   1.00 4.88  ? 142  SER B N   1 
ATOM   2148  C  CA  . SER B  1 142 ? 2.216  38.204  -8.936   1.00 4.74  ? 142  SER B CA  1 
ATOM   2149  C  C   . SER B  1 142 ? 2.936  38.497  -10.264  1.00 3.96  ? 142  SER B C   1 
ATOM   2150  O  O   . SER B  1 142 ? 3.251  39.660  -10.589  1.00 3.46  ? 142  SER B O   1 
ATOM   2151  C  CB  . SER B  1 142 ? 0.745  37.794  -9.159   1.00 5.21  ? 142  SER B CB  1 
ATOM   2152  O  OG  . SER B  1 142 ? 0.141  38.726  -10.023  1.00 7.87  ? 142  SER B OG  1 
ATOM   2153  N  N   . ARG B  1 143 ? 3.184  37.439  -11.030  1.00 3.98  ? 143  ARG B N   1 
ATOM   2154  C  CA  . ARG B  1 143 ? 3.917  37.551  -12.280  1.00 4.06  ? 143  ARG B CA  1 
ATOM   2155  C  C   . ARG B  1 143 ? 2.926  37.638  -13.424  1.00 4.90  ? 143  ARG B C   1 
ATOM   2156  O  O   . ARG B  1 143 ? 2.247  36.652  -13.727  1.00 6.86  ? 143  ARG B O   1 
ATOM   2157  C  CB  . ARG B  1 143 ? 4.857  36.362  -12.422  1.00 4.00  ? 143  ARG B CB  1 
ATOM   2158  C  CG  . ARG B  1 143 ? 5.745  36.200  -11.195  1.00 3.68  ? 143  ARG B CG  1 
ATOM   2159  C  CD  . ARG B  1 143 ? 6.533  34.909  -11.201  1.00 4.71  ? 143  ARG B CD  1 
ATOM   2160  N  NE  . ARG B  1 143 ? 7.259  34.779  -9.934   1.00 6.06  ? 143  ARG B NE  1 
ATOM   2161  C  CZ  . ARG B  1 143 ? 8.336  34.007  -9.732   1.00 6.75  ? 143  ARG B CZ  1 
ATOM   2162  N  NH1 . ARG B  1 143 ? 8.911  33.977  -8.523   1.00 3.10  ? 143  ARG B NH1 1 
ATOM   2163  N  NH2 . ARG B  1 143 ? 8.867  33.297  -10.726  1.00 3.75  ? 143  ARG B NH2 1 
ATOM   2164  N  N   . LEU B  1 144 ? 2.815  38.815  -14.031  1.00 5.20  ? 144  LEU B N   1 
ATOM   2165  C  CA  . LEU B  1 144 ? 1.765  39.036  -15.042  1.00 5.08  ? 144  LEU B CA  1 
ATOM   2166  C  C   . LEU B  1 144 ? 2.162  38.517  -16.401  1.00 4.62  ? 144  LEU B C   1 
ATOM   2167  O  O   . LEU B  1 144 ? 1.305  38.024  -17.141  1.00 4.81  ? 144  LEU B O   1 
ATOM   2168  C  CB  . LEU B  1 144 ? 1.360  40.509  -15.158  1.00 5.06  ? 144  LEU B CB  1 
ATOM   2169  C  CG  . LEU B  1 144 ? 0.841  41.141  -13.854  1.00 7.56  ? 144  LEU B CG  1 
ATOM   2170  C  CD1 . LEU B  1 144 ? 0.374  42.569  -14.111  1.00 8.68  ? 144  LEU B CD1 1 
ATOM   2171  C  CD2 . LEU B  1 144 ? -0.275 40.331  -13.179  1.00 9.89  ? 144  LEU B CD2 1 
ATOM   2172  N  N   . ALA B  1 145 ? 3.446  38.645  -16.733  1.00 3.72  ? 145  ALA B N   1 
ATOM   2173  C  CA  . ALA B  1 145 ? 3.954  38.110  -17.997  1.00 2.44  ? 145  ALA B CA  1 
ATOM   2174  C  C   . ALA B  1 145 ? 5.426  37.814  -17.848  1.00 2.35  ? 145  ALA B C   1 
ATOM   2175  O  O   . ALA B  1 145 ? 6.118  38.427  -17.003  1.00 2.00  ? 145  ALA B O   1 
ATOM   2176  C  CB  . ALA B  1 145 ? 3.707  39.095  -19.165  1.00 2.47  ? 145  ALA B CB  1 
ATOM   2177  N  N   . CYS B  1 146 ? 5.915  36.889  -18.669  1.00 2.42  ? 146  CYS B N   1 
ATOM   2178  C  CA  . CYS B  1 146 ? 7.335  36.540  -18.631  1.00 2.00  ? 146  CYS B CA  1 
ATOM   2179  C  C   . CYS B  1 146 ? 7.762  35.904  -19.943  1.00 2.00  ? 146  CYS B C   1 
ATOM   2180  O  O   . CYS B  1 146 ? 6.927  35.500  -20.755  1.00 2.00  ? 146  CYS B O   1 
ATOM   2181  C  CB  . CYS B  1 146 ? 7.623  35.569  -17.493  0.40 2.00  ? 146  CYS B CB  1 
ATOM   2182  S  SG  . CYS B  1 146 ? 6.718  34.035  -17.608  0.40 2.00  ? 146  CYS B SG  1 
ATOM   2183  N  N   . GLY B  1 147 ? 9.065  35.778  -20.131  1.00 2.00  ? 147  GLY B N   1 
ATOM   2184  C  CA  . GLY B  1 147 ? 9.575  35.101  -21.335  1.00 2.69  ? 147  GLY B CA  1 
ATOM   2185  C  C   . GLY B  1 147 ? 11.031 34.770  -21.104  1.00 3.29  ? 147  GLY B C   1 
ATOM   2186  O  O   . GLY B  1 147 ? 11.676 35.341  -20.202  1.00 2.83  ? 147  GLY B O   1 
ATOM   2187  N  N   . VAL B  1 148 ? 11.550 33.818  -21.875  1.00 3.00  ? 148  VAL B N   1 
ATOM   2188  C  CA  . VAL B  1 148 ? 12.977 33.474  -21.764  1.00 3.15  ? 148  VAL B CA  1 
ATOM   2189  C  C   . VAL B  1 148 ? 13.791 34.489  -22.582  1.00 3.30  ? 148  VAL B C   1 
ATOM   2190  O  O   . VAL B  1 148 ? 13.401 34.884  -23.691  1.00 4.07  ? 148  VAL B O   1 
ATOM   2191  C  CB  . VAL B  1 148 ? 13.236 32.029  -22.276  1.00 3.14  ? 148  VAL B CB  1 
ATOM   2192  C  CG1 . VAL B  1 148 ? 14.694 31.626  -22.080  1.00 2.00  ? 148  VAL B CG1 1 
ATOM   2193  C  CG2 . VAL B  1 148 ? 12.375 31.054  -21.517  1.00 4.18  ? 148  VAL B CG2 1 
ATOM   2194  N  N   . ILE B  1 149 ? 14.926 34.909  -22.036  1.00 4.09  ? 149  ILE B N   1 
ATOM   2195  C  CA  . ILE B  1 149 ? 15.772 35.874  -22.702  1.00 3.89  ? 149  ILE B CA  1 
ATOM   2196  C  C   . ILE B  1 149 ? 16.615 35.114  -23.734  1.00 3.74  ? 149  ILE B C   1 
ATOM   2197  O  O   . ILE B  1 149 ? 17.440 34.256  -23.380  1.00 5.46  ? 149  ILE B O   1 
ATOM   2198  C  CB  . ILE B  1 149 ? 16.660 36.640  -21.683  1.00 3.41  ? 149  ILE B CB  1 
ATOM   2199  C  CG1 . ILE B  1 149 ? 15.802 37.448  -20.703  1.00 5.39  ? 149  ILE B CG1 1 
ATOM   2200  C  CG2 . ILE B  1 149 ? 17.607 37.629  -22.414  1.00 5.59  ? 149  ILE B CG2 1 
ATOM   2201  C  CD1 . ILE B  1 149 ? 16.580 37.857  -19.354  1.00 2.83  ? 149  ILE B CD1 1 
ATOM   2202  N  N   . GLY B  1 150 ? 16.426 35.427  -25.005  1.00 3.31  ? 150  GLY B N   1 
ATOM   2203  C  CA  . GLY B  1 150 ? 17.139 34.684  -26.055  1.00 4.31  ? 150  GLY B CA  1 
ATOM   2204  C  C   . GLY B  1 150 ? 18.164 35.492  -26.821  1.00 5.53  ? 150  GLY B C   1 
ATOM   2205  O  O   . GLY B  1 150 ? 18.114 36.741  -26.854  1.00 5.59  ? 150  GLY B O   1 
ATOM   2206  N  N   . ILE B  1 151 ? 19.098 34.790  -27.464  1.00 5.23  ? 151  ILE B N   1 
ATOM   2207  C  CA  . ILE B  1 151 ? 20.101 35.459  -28.310  1.00 5.73  ? 151  ILE B CA  1 
ATOM   2208  C  C   . ILE B  1 151 ? 19.421 36.022  -29.569  1.00 6.52  ? 151  ILE B C   1 
ATOM   2209  O  O   . ILE B  1 151 ? 18.624 35.328  -30.218  1.00 5.79  ? 151  ILE B O   1 
ATOM   2210  C  CB  . ILE B  1 151 ? 21.260 34.483  -28.702  1.00 5.22  ? 151  ILE B CB  1 
ATOM   2211  C  CG1 . ILE B  1 151 ? 22.007 34.003  -27.459  1.00 4.72  ? 151  ILE B CG1 1 
ATOM   2212  C  CG2 . ILE B  1 151 ? 22.224 35.157  -29.695  1.00 7.24  ? 151  ILE B CG2 1 
ATOM   2213  C  CD1 . ILE B  1 151 ? 22.776 32.641  -27.686  1.00 9.79  ? 151  ILE B CD1 1 
ATOM   2214  N  N   . ALA B  1 152 ? 19.719 37.283  -29.886  1.00 6.88  ? 152  ALA B N   1 
ATOM   2215  C  CA  . ALA B  1 152 ? 19.097 37.966  -31.028  1.00 8.57  ? 152  ALA B CA  1 
ATOM   2216  C  C   . ALA B  1 152 ? 20.157 38.285  -32.067  1.00 9.84  ? 152  ALA B C   1 
ATOM   2217  O  O   . ALA B  1 152 ? 21.361 38.316  -31.754  1.00 9.90  ? 152  ALA B O   1 
ATOM   2218  C  CB  . ALA B  1 152 ? 18.363 39.242  -30.575  1.00 8.82  ? 152  ALA B CB  1 
ATOM   2219  N  N   . GLN B  1 153 ? 19.713 38.486  -33.302  1.00 10.87 ? 153  GLN B N   1 
ATOM   2220  C  CA  . GLN B  1 153 ? 20.638 38.719  -34.409  1.00 12.70 ? 153  GLN B CA  1 
ATOM   2221  C  C   . GLN B  1 153 ? 21.254 40.102  -34.315  1.00 13.52 ? 153  GLN B C   1 
ATOM   2222  O  O   . GLN B  1 153 ? 20.536 41.067  -34.068  1.00 14.03 ? 153  GLN B O   1 
ATOM   2223  C  CB  . GLN B  1 153 ? 19.923 38.585  -35.749  1.00 12.54 ? 153  GLN B CB  1 
ATOM   2224  C  CG  . GLN B  1 153 ? 20.851 38.738  -36.959  1.00 15.98 ? 153  GLN B CG  1 
ATOM   2225  C  CD  . GLN B  1 153 ? 20.116 38.611  -38.271  1.00 18.29 ? 153  GLN B CD  1 
ATOM   2226  O  OE1 . GLN B  1 153 ? 20.626 38.022  -39.221  1.00 21.84 ? 153  GLN B OE1 1 
ATOM   2227  N  NE2 . GLN B  1 153 ? 18.903 39.149  -38.327  1.00 19.80 ? 153  GLN B NE2 1 
ATOM   2228  O  OXT . GLN B  1 153 ? 22.457 40.271  -34.530  1.00 14.77 ? 153  GLN B OXT 1 
ATOM   2229  N  N   . ALA C  1 1   ? 40.653 37.226  -42.535  1.00 18.60 ? 1    ALA D N   1 
ATOM   2230  C  CA  . ALA C  1 1   ? 41.460 36.163  -41.866  1.00 18.01 ? 1    ALA D CA  1 
ATOM   2231  C  C   . ALA C  1 1   ? 42.010 36.615  -40.496  1.00 17.44 ? 1    ALA D C   1 
ATOM   2232  O  O   . ALA C  1 1   ? 42.142 37.808  -40.234  1.00 18.43 ? 1    ALA D O   1 
ATOM   2233  C  CB  . ALA C  1 1   ? 42.605 35.722  -42.791  1.00 18.36 ? 1    ALA D CB  1 
ATOM   2234  N  N   . THR C  1 2   ? 42.308 35.649  -39.626  1.00 15.52 ? 2    THR D N   1 
ATOM   2235  C  CA  . THR C  1 2   ? 43.010 35.912  -38.377  1.00 13.81 ? 2    THR D CA  1 
ATOM   2236  C  C   . THR C  1 2   ? 44.441 35.395  -38.559  1.00 11.33 ? 2    THR D C   1 
ATOM   2237  O  O   . THR C  1 2   ? 44.655 34.357  -39.201  1.00 10.38 ? 2    THR D O   1 
ATOM   2238  C  CB  . THR C  1 2   ? 42.359 35.207  -37.168  1.00 14.19 ? 2    THR D CB  1 
ATOM   2239  O  OG1 . THR C  1 2   ? 40.953 35.436  -37.175  1.00 18.23 ? 2    THR D OG1 1 
ATOM   2240  C  CG2 . THR C  1 2   ? 42.914 35.746  -35.838  1.00 15.55 ? 2    THR D CG2 1 
ATOM   2241  N  N   . LYS C  1 3   ? 45.403 36.135  -38.007  1.00 8.74  ? 3    LYS D N   1 
ATOM   2242  C  CA  . LYS C  1 3   ? 46.794 35.711  -37.985  1.00 6.61  ? 3    LYS D CA  1 
ATOM   2243  C  C   . LYS C  1 3   ? 47.323 35.813  -36.569  1.00 5.52  ? 3    LYS D C   1 
ATOM   2244  O  O   . LYS C  1 3   ? 46.885 36.668  -35.785  1.00 4.97  ? 3    LYS D O   1 
ATOM   2245  C  CB  . LYS C  1 3   ? 47.657 36.562  -38.913  1.00 7.32  ? 3    LYS D CB  1 
ATOM   2246  C  CG  . LYS C  1 3   ? 47.256 36.514  -40.420  1.00 10.00 ? 3    LYS D CG  1 
ATOM   2247  C  CD  . LYS C  1 3   ? 48.246 37.311  -41.267  1.00 15.17 ? 3    LYS D CD  1 
ATOM   2248  C  CE  . LYS C  1 3   ? 47.941 37.213  -42.765  1.00 18.87 ? 3    LYS D CE  1 
ATOM   2249  N  NZ  . LYS C  1 3   ? 49.092 37.738  -43.581  1.00 22.91 ? 3    LYS D NZ  1 
ATOM   2250  N  N   . ALA C  1 4   ? 48.271 34.940  -36.254  1.00 3.83  ? 4    ALA D N   1 
ATOM   2251  C  CA  . ALA C  1 4   ? 48.932 34.929  -34.967  1.00 3.30  ? 4    ALA D CA  1 
ATOM   2252  C  C   . ALA C  1 4   ? 50.407 34.561  -35.184  1.00 3.45  ? 4    ALA D C   1 
ATOM   2253  O  O   . ALA C  1 4   ? 50.790 34.098  -36.266  1.00 2.88  ? 4    ALA D O   1 
ATOM   2254  C  CB  . ALA C  1 4   ? 48.250 33.951  -33.987  1.00 2.76  ? 4    ALA D CB  1 
ATOM   2255  N  N   . VAL C  1 5   ? 51.245 34.799  -34.175  1.00 3.06  ? 5    VAL D N   1 
ATOM   2256  C  CA  . VAL C  1 5   ? 52.691 34.586  -34.359  1.00 3.57  ? 5    VAL D CA  1 
ATOM   2257  C  C   . VAL C  1 5   ? 53.294 34.215  -33.008  1.00 3.50  ? 5    VAL D C   1 
ATOM   2258  O  O   . VAL C  1 5   ? 52.777 34.617  -31.964  1.00 3.24  ? 5    VAL D O   1 
ATOM   2259  C  CB  . VAL C  1 5   ? 53.420 35.832  -34.972  1.00 4.08  ? 5    VAL D CB  1 
ATOM   2260  C  CG1 . VAL C  1 5   ? 53.480 36.995  -33.988  1.00 4.40  ? 5    VAL D CG1 1 
ATOM   2261  C  CG2 . VAL C  1 5   ? 54.850 35.476  -35.503  1.00 5.23  ? 5    VAL D CG2 1 
ATOM   2262  N  N   . CYS C  1 6   ? 54.385 33.455  -33.029  1.00 3.11  ? 6    CYS D N   1 
ATOM   2263  C  CA  . CYS C  1 6   ? 55.028 33.057  -31.789  1.00 2.55  ? 6    CYS D CA  1 
ATOM   2264  C  C   . CYS C  1 6   ? 56.540 33.030  -31.978  1.00 2.39  ? 6    CYS D C   1 
ATOM   2265  O  O   . CYS C  1 6   ? 57.015 32.459  -32.939  1.00 2.04  ? 6    CYS D O   1 
ATOM   2266  C  CB  . CYS C  1 6   ? 54.505 31.689  -31.356  1.00 2.85  ? 6    CYS D CB  1 
ATOM   2267  S  SG  . CYS C  1 6   ? 55.279 31.110  -29.840  1.00 4.30  ? 6    CYS D SG  1 
ATOM   2268  N  N   . VAL C  1 7   ? 57.262 33.719  -31.102  1.00 2.04  ? 7    VAL D N   1 
ATOM   2269  C  CA  . VAL C  1 7   ? 58.721 33.679  -31.096  1.00 3.28  ? 7    VAL D CA  1 
ATOM   2270  C  C   . VAL C  1 7   ? 59.165 32.638  -30.052  1.00 3.08  ? 7    VAL D C   1 
ATOM   2271  O  O   . VAL C  1 7   ? 58.881 32.773  -28.844  1.00 2.25  ? 7    VAL D O   1 
ATOM   2272  C  CB  . VAL C  1 7   ? 59.306 35.083  -30.803  1.00 3.41  ? 7    VAL D CB  1 
ATOM   2273  C  CG1 . VAL C  1 7   ? 60.861 35.055  -30.863  1.00 4.99  ? 7    VAL D CG1 1 
ATOM   2274  C  CG2 . VAL C  1 7   ? 58.749 36.090  -31.808  1.00 3.63  ? 7    VAL D CG2 1 
ATOM   2275  N  N   . LEU C  1 8   ? 59.845 31.586  -30.515  1.00 3.42  ? 8    LEU D N   1 
ATOM   2276  C  CA  . LEU C  1 8   ? 60.297 30.534  -29.628  1.00 4.13  ? 8    LEU D CA  1 
ATOM   2277  C  C   . LEU C  1 8   ? 61.738 30.832  -29.195  1.00 4.04  ? 8    LEU D C   1 
ATOM   2278  O  O   . LEU C  1 8   ? 62.574 31.120  -30.038  1.00 3.66  ? 8    LEU D O   1 
ATOM   2279  C  CB  . LEU C  1 8   ? 60.246 29.171  -30.340  1.00 4.38  ? 8    LEU D CB  1 
ATOM   2280  C  CG  . LEU C  1 8   ? 58.863 28.669  -30.786  1.00 6.53  ? 8    LEU D CG  1 
ATOM   2281  C  CD1 . LEU C  1 8   ? 59.075 27.432  -31.710  1.00 7.46  ? 8    LEU D CD1 1 
ATOM   2282  C  CD2 . LEU C  1 8   ? 58.071 28.280  -29.569  1.00 6.46  ? 8    LEU D CD2 1 
ATOM   2283  N  N   . LYS C  1 9   ? 61.983 30.821  -27.891  1.00 3.66  ? 9    LYS D N   1 
ATOM   2284  C  CA  . LYS C  1 9   ? 63.338 30.978  -27.313  1.00 5.82  ? 9    LYS D CA  1 
ATOM   2285  C  C   . LYS C  1 9   ? 63.447 30.020  -26.131  1.00 5.78  ? 9    LYS D C   1 
ATOM   2286  O  O   . LYS C  1 9   ? 62.439 29.650  -25.548  1.00 6.34  ? 9    LYS D O   1 
ATOM   2287  C  CB  . LYS C  1 9   ? 63.562 32.418  -26.829  1.00 6.79  ? 9    LYS D CB  1 
ATOM   2288  C  CG  . LYS C  1 9   ? 63.624 33.419  -27.976  1.00 11.06 ? 9    LYS D CG  1 
ATOM   2289  C  CD  . LYS C  1 9   ? 64.157 34.799  -27.567  1.00 18.75 ? 9    LYS D CD  1 
ATOM   2290  C  CE  . LYS C  1 9   ? 64.180 35.743  -28.780  1.00 22.07 ? 9    LYS D CE  1 
ATOM   2291  N  NZ  . LYS C  1 9   ? 65.086 35.252  -29.877  1.00 22.87 ? 9    LYS D NZ  1 
ATOM   2292  N  N   . GLY C  1 10  ? 64.664 29.619  -25.775  1.00 6.02  ? 10   GLY D N   1 
ATOM   2293  C  CA  . GLY C  1 10  ? 64.860 28.768  -24.601  1.00 6.57  ? 10   GLY D CA  1 
ATOM   2294  C  C   . GLY C  1 10  ? 66.211 29.037  -23.957  1.00 7.59  ? 10   GLY D C   1 
ATOM   2295  O  O   . GLY C  1 10  ? 66.822 30.071  -24.231  1.00 8.45  ? 10   GLY D O   1 
ATOM   2296  N  N   . ASP C  1 11  ? 66.647 28.125  -23.087  1.00 8.50  ? 11   ASP D N   1 
ATOM   2297  C  CA  . ASP C  1 11  ? 67.940 28.246  -22.405  1.00 10.46 ? 11   ASP D CA  1 
ATOM   2298  C  C   . ASP C  1 11  ? 69.114 27.799  -23.252  1.00 10.42 ? 11   ASP D C   1 
ATOM   2299  O  O   . ASP C  1 11  ? 70.270 28.060  -22.897  1.00 11.48 ? 11   ASP D O   1 
ATOM   2300  C  CB  . ASP C  1 11  ? 67.968 27.422  -21.123  1.00 11.58 ? 11   ASP D CB  1 
ATOM   2301  C  CG  . ASP C  1 11  ? 67.043 27.953  -20.073  1.00 14.91 ? 11   ASP D CG  1 
ATOM   2302  O  OD1 . ASP C  1 11  ? 66.619 27.136  -19.248  1.00 20.86 ? 11   ASP D OD1 1 
ATOM   2303  O  OD2 . ASP C  1 11  ? 66.722 29.157  -20.081  1.00 17.32 ? 11   ASP D OD2 1 
ATOM   2304  N  N   . GLY C  1 12  ? 68.827 27.130  -24.358  1.00 9.05  ? 12   GLY D N   1 
ATOM   2305  C  CA  . GLY C  1 12  ? 69.881 26.697  -25.269  1.00 7.62  ? 12   GLY D CA  1 
ATOM   2306  C  C   . GLY C  1 12  ? 69.743 27.375  -26.607  1.00 6.16  ? 12   GLY D C   1 
ATOM   2307  O  O   . GLY C  1 12  ? 69.255 28.516  -26.685  1.00 5.68  ? 12   GLY D O   1 
ATOM   2308  N  N   . PRO C  1 13  ? 70.136 26.664  -27.684  1.00 5.28  ? 13   PRO D N   1 
ATOM   2309  C  CA  . PRO C  1 13  ? 70.205 27.268  -29.005  1.00 3.97  ? 13   PRO D CA  1 
ATOM   2310  C  C   . PRO C  1 13  ? 68.920 27.184  -29.822  1.00 3.90  ? 13   PRO D C   1 
ATOM   2311  O  O   . PRO C  1 13  ? 68.900 27.678  -30.942  1.00 4.29  ? 13   PRO D O   1 
ATOM   2312  C  CB  . PRO C  1 13  ? 71.294 26.434  -29.702  1.00 4.73  ? 13   PRO D CB  1 
ATOM   2313  C  CG  . PRO C  1 13  ? 71.106 25.046  -29.125  1.00 3.86  ? 13   PRO D CG  1 
ATOM   2314  C  CD  . PRO C  1 13  ? 70.702 25.295  -27.667  1.00 5.16  ? 13   PRO D CD  1 
ATOM   2315  N  N   . VAL C  1 14  ? 67.852 26.584  -29.284  1.00 3.47  ? 14   VAL D N   1 
ATOM   2316  C  CA  . VAL C  1 14  ? 66.602 26.453  -30.055  1.00 3.32  ? 14   VAL D CA  1 
ATOM   2317  C  C   . VAL C  1 14  ? 65.904 27.794  -30.148  1.00 3.97  ? 14   VAL D C   1 
ATOM   2318  O  O   . VAL C  1 14  ? 65.628 28.409  -29.131  1.00 3.63  ? 14   VAL D O   1 
ATOM   2319  C  CB  . VAL C  1 14  ? 65.647 25.371  -29.468  1.00 3.83  ? 14   VAL D CB  1 
ATOM   2320  C  CG1 . VAL C  1 14  ? 64.380 25.218  -30.346  1.00 4.61  ? 14   VAL D CG1 1 
ATOM   2321  C  CG2 . VAL C  1 14  ? 66.374 24.021  -29.450  1.00 3.15  ? 14   VAL D CG2 1 
ATOM   2322  N  N   . GLN C  1 15  ? 65.633 28.241  -31.365  1.00 4.02  ? 15   GLN D N   1 
ATOM   2323  C  CA  . GLN C  1 15  ? 64.921 29.501  -31.547  1.00 5.49  ? 15   GLN D CA  1 
ATOM   2324  C  C   . GLN C  1 15  ? 64.238 29.540  -32.902  1.00 5.40  ? 15   GLN D C   1 
ATOM   2325  O  O   . GLN C  1 15  ? 64.741 28.978  -33.879  1.00 4.63  ? 15   GLN D O   1 
ATOM   2326  C  CB  . GLN C  1 15  ? 65.872 30.698  -31.377  1.00 6.29  ? 15   GLN D CB  1 
ATOM   2327  C  CG  . GLN C  1 15  ? 67.110 30.573  -32.206  1.00 10.62 ? 15   GLN D CG  1 
ATOM   2328  C  CD  . GLN C  1 15  ? 68.021 31.796  -32.096  1.00 17.51 ? 15   GLN D CD  1 
ATOM   2329  O  OE1 . GLN C  1 15  ? 69.251 31.675  -32.128  1.00 18.54 ? 15   GLN D OE1 1 
ATOM   2330  N  NE2 . GLN C  1 15  ? 67.419 32.970  -31.974  1.00 18.24 ? 15   GLN D NE2 1 
ATOM   2331  N  N   . GLY C  1 16  ? 63.082 30.192  -32.975  1.00 5.35  ? 16   GLY D N   1 
ATOM   2332  C  CA  . GLY C  1 16  ? 62.423 30.303  -34.270  1.00 5.83  ? 16   GLY D CA  1 
ATOM   2333  C  C   . GLY C  1 16  ? 61.168 31.142  -34.173  1.00 4.97  ? 16   GLY D C   1 
ATOM   2334  O  O   . GLY C  1 16  ? 60.836 31.652  -33.114  1.00 5.22  ? 16   GLY D O   1 
ATOM   2335  N  N   . ILE C  1 17  ? 60.494 31.284  -35.293  1.00 4.47  ? 17   ILE D N   1 
ATOM   2336  C  CA  . ILE C  1 17  ? 59.304 32.101  -35.376  1.00 4.64  ? 17   ILE D CA  1 
ATOM   2337  C  C   . ILE C  1 17  ? 58.283 31.215  -36.064  1.00 4.21  ? 17   ILE D C   1 
ATOM   2338  O  O   . ILE C  1 17  ? 58.569 30.651  -37.123  1.00 3.48  ? 17   ILE D O   1 
ATOM   2339  C  CB  . ILE C  1 17  ? 59.577 33.348  -36.241  1.00 4.77  ? 17   ILE D CB  1 
ATOM   2340  C  CG1 . ILE C  1 17  ? 60.426 34.355  -35.462  1.00 7.50  ? 17   ILE D CG1 1 
ATOM   2341  C  CG2 . ILE C  1 17  ? 58.258 34.000  -36.668  1.00 5.84  ? 17   ILE D CG2 1 
ATOM   2342  C  CD1 . ILE C  1 17  ? 61.118 35.422  -36.351  1.00 9.77  ? 17   ILE D CD1 1 
ATOM   2343  N  N   . ILE C  1 18  ? 57.117 31.075  -35.450  1.00 3.46  ? 18   ILE D N   1 
ATOM   2344  C  CA  . ILE C  1 18  ? 56.051 30.246  -35.988  1.00 4.14  ? 18   ILE D CA  1 
ATOM   2345  C  C   . ILE C  1 18  ? 54.839 31.152  -36.271  1.00 3.63  ? 18   ILE D C   1 
ATOM   2346  O  O   . ILE C  1 18  ? 54.404 31.901  -35.406  1.00 4.39  ? 18   ILE D O   1 
ATOM   2347  C  CB  . ILE C  1 18  ? 55.679 29.071  -35.047  1.00 4.10  ? 18   ILE D CB  1 
ATOM   2348  C  CG1 . ILE C  1 18  ? 56.848 28.065  -34.896  1.00 3.74  ? 18   ILE D CG1 1 
ATOM   2349  C  CG2 . ILE C  1 18  ? 54.402 28.371  -35.517  1.00 3.14  ? 18   ILE D CG2 1 
ATOM   2350  C  CD1 . ILE C  1 18  ? 57.297 27.347  -36.221  1.00 6.11  ? 18   ILE D CD1 1 
ATOM   2351  N  N   . ASN C  1 19  ? 54.341 31.076  -37.499  1.00 2.29  ? 19   ASN D N   1 
ATOM   2352  C  CA  . ASN C  1 19  ? 53.186 31.815  -37.920  1.00 3.91  ? 19   ASN D CA  1 
ATOM   2353  C  C   . ASN C  1 19  ? 51.941 30.968  -37.933  1.00 4.39  ? 19   ASN D C   1 
ATOM   2354  O  O   . ASN C  1 19  ? 52.003 29.729  -38.197  1.00 4.38  ? 19   ASN D O   1 
ATOM   2355  C  CB  . ASN C  1 19  ? 53.434 32.331  -39.335  1.00 4.46  ? 19   ASN D CB  1 
ATOM   2356  C  CG  . ASN C  1 19  ? 54.660 33.210  -39.421  1.00 7.29  ? 19   ASN D CG  1 
ATOM   2357  O  OD1 . ASN C  1 19  ? 54.667 34.328  -38.902  1.00 7.37  ? 19   ASN D OD1 1 
ATOM   2358  N  ND2 . ASN C  1 19  ? 55.713 32.718  -40.115  1.00 8.95  ? 19   ASN D ND2 1 
ATOM   2359  N  N   . PHE C  1 20  ? 50.799 31.634  -37.715  1.00 4.46  ? 20   PHE D N   1 
ATOM   2360  C  CA  . PHE C  1 20  ? 49.490 30.979  -37.767  1.00 4.74  ? 20   PHE D CA  1 
ATOM   2361  C  C   . PHE C  1 20  ? 48.575 31.842  -38.621  1.00 5.90  ? 20   PHE D C   1 
ATOM   2362  O  O   . PHE C  1 20  ? 48.614 33.085  -38.541  1.00 4.88  ? 20   PHE D O   1 
ATOM   2363  C  CB  . PHE C  1 20  ? 48.853 30.866  -36.371  1.00 4.26  ? 20   PHE D CB  1 
ATOM   2364  C  CG  . PHE C  1 20  ? 49.681 30.080  -35.362  1.00 4.36  ? 20   PHE D CG  1 
ATOM   2365  C  CD1 . PHE C  1 20  ? 49.433 28.726  -35.153  1.00 4.46  ? 20   PHE D CD1 1 
ATOM   2366  C  CD2 . PHE C  1 20  ? 50.708 30.695  -34.647  1.00 4.36  ? 20   PHE D CD2 1 
ATOM   2367  C  CE1 . PHE C  1 20  ? 50.178 27.994  -34.219  1.00 5.59  ? 20   PHE D CE1 1 
ATOM   2368  C  CE2 . PHE C  1 20  ? 51.465 29.977  -33.706  1.00 2.34  ? 20   PHE D CE2 1 
ATOM   2369  C  CZ  . PHE C  1 20  ? 51.187 28.625  -33.484  1.00 3.89  ? 20   PHE D CZ  1 
ATOM   2370  N  N   . GLU C  1 21  ? 47.769 31.191  -39.460  1.00 6.87  ? 21   GLU D N   1 
ATOM   2371  C  CA  . GLU C  1 21  ? 46.766 31.919  -40.224  1.00 7.89  ? 21   GLU D CA  1 
ATOM   2372  C  C   . GLU C  1 21  ? 45.513 31.086  -40.358  1.00 8.43  ? 21   GLU D C   1 
ATOM   2373  O  O   . GLU C  1 21  ? 45.583 29.893  -40.639  1.00 8.05  ? 21   GLU D O   1 
ATOM   2374  C  CB  . GLU C  1 21  ? 47.280 32.349  -41.602  1.00 8.89  ? 21   GLU D CB  1 
ATOM   2375  C  CG  . GLU C  1 21  ? 46.290 33.312  -42.313  1.00 11.53 ? 21   GLU D CG  1 
ATOM   2376  C  CD  . GLU C  1 21  ? 46.777 33.823  -43.649  1.00 17.52 ? 21   GLU D CD  1 
ATOM   2377  O  OE1 . GLU C  1 21  ? 45.953 34.452  -44.380  1.00 20.40 ? 21   GLU D OE1 1 
ATOM   2378  O  OE2 . GLU C  1 21  ? 47.962 33.601  -43.979  1.00 18.52 ? 21   GLU D OE2 1 
ATOM   2379  N  N   . GLN C  1 22  ? 44.372 31.737  -40.190  1.00 9.03  ? 22   GLN D N   1 
ATOM   2380  C  CA  . GLN C  1 22  ? 43.100 31.051  -40.241  1.00 10.75 ? 22   GLN D CA  1 
ATOM   2381  C  C   . GLN C  1 22  ? 42.136 31.912  -41.055  1.00 12.12 ? 22   GLN D C   1 
ATOM   2382  O  O   . GLN C  1 22  ? 41.678 32.949  -40.566  1.00 11.11 ? 22   GLN D O   1 
ATOM   2383  C  CB  . GLN C  1 22  ? 42.588 30.808  -38.821  1.00 11.36 ? 22   GLN D CB  1 
ATOM   2384  C  CG  . GLN C  1 22  ? 41.356 29.918  -38.758  1.00 10.71 ? 22   GLN D CG  1 
ATOM   2385  C  CD  . GLN C  1 22  ? 40.765 29.776  -37.367  1.00 12.34 ? 22   GLN D CD  1 
ATOM   2386  O  OE1 . GLN C  1 22  ? 40.883 30.659  -36.506  1.00 12.61 ? 22   GLN D OE1 1 
ATOM   2387  N  NE2 . GLN C  1 22  ? 40.112 28.652  -37.139  1.00 10.86 ? 22   GLN D NE2 1 
ATOM   2388  N  N   . LYS C  1 23  ? 41.871 31.481  -42.292  1.00 13.90 ? 23   LYS D N   1 
ATOM   2389  C  CA  . LYS C  1 23  ? 41.073 32.249  -43.253  1.00 17.10 ? 23   LYS D CA  1 
ATOM   2390  C  C   . LYS C  1 23  ? 39.642 32.422  -42.784  1.00 17.65 ? 23   LYS D C   1 
ATOM   2391  O  O   . LYS C  1 23  ? 39.048 33.488  -42.956  1.00 18.44 ? 23   LYS D O   1 
ATOM   2392  C  CB  . LYS C  1 23  ? 41.077 31.584  -44.647  1.00 17.55 ? 23   LYS D CB  1 
ATOM   2393  C  CG  . LYS C  1 23  ? 41.890 32.349  -45.696  1.00 22.27 ? 23   LYS D CG  1 
ATOM   2394  C  CD  . LYS C  1 23  ? 41.602 31.854  -47.128  1.00 26.62 ? 23   LYS D CD  1 
ATOM   2395  C  CE  . LYS C  1 23  ? 42.742 32.218  -48.084  1.00 28.47 ? 23   LYS D CE  1 
ATOM   2396  N  NZ  . LYS C  1 23  ? 44.030 31.513  -47.725  1.00 28.66 ? 23   LYS D NZ  1 
ATOM   2397  N  N   . GLU C  1 24  ? 39.091 31.362  -42.206  1.00 18.95 ? 24   GLU D N   1 
ATOM   2398  C  CA  . GLU C  1 24  ? 37.700 31.359  -41.749  1.00 20.53 ? 24   GLU D CA  1 
ATOM   2399  C  C   . GLU C  1 24  ? 37.605 31.013  -40.279  1.00 21.03 ? 24   GLU D C   1 
ATOM   2400  O  O   . GLU C  1 24  ? 38.383 30.205  -39.780  1.00 20.31 ? 24   GLU D O   1 
ATOM   2401  C  CB  . GLU C  1 24  ? 36.848 30.380  -42.573  1.00 20.62 ? 24   GLU D CB  1 
ATOM   2402  C  CG  . GLU C  1 24  ? 36.714 30.752  -44.050  1.00 23.83 ? 24   GLU D CG  1 
ATOM   2403  C  CD  . GLU C  1 24  ? 36.107 32.141  -44.259  1.00 28.16 ? 24   GLU D CD  1 
ATOM   2404  O  OE1 . GLU C  1 24  ? 36.516 32.829  -45.228  1.00 29.38 ? 24   GLU D OE1 1 
ATOM   2405  O  OE2 . GLU C  1 24  ? 35.230 32.550  -43.451  1.00 30.45 ? 24   GLU D OE2 1 
ATOM   2406  N  N   . SER C  1 25  ? 36.626 31.614  -39.599  1.00 22.17 ? 25   SER D N   1 
ATOM   2407  C  CA  . SER C  1 25  ? 36.417 31.389  -38.166  1.00 23.92 ? 25   SER D CA  1 
ATOM   2408  C  C   . SER C  1 25  ? 36.136 29.918  -37.837  1.00 24.33 ? 25   SER D C   1 
ATOM   2409  O  O   . SER C  1 25  ? 36.486 29.435  -36.761  1.00 25.06 ? 25   SER D O   1 
ATOM   2410  C  CB  . SER C  1 25  ? 35.297 32.292  -37.640  1.00 24.05 ? 25   SER D CB  1 
ATOM   2411  O  OG  . SER C  1 25  ? 34.022 31.761  -37.940  1.00 25.52 ? 25   SER D OG  1 
ATOM   2412  N  N   . ASN C  1 26  ? 35.493 29.219  -38.765  1.00 24.43 ? 26   ASN D N   1 
ATOM   2413  C  CA  . ASN C  1 26  ? 35.279 27.783  -38.641  1.00 24.63 ? 26   ASN D CA  1 
ATOM   2414  C  C   . ASN C  1 26  ? 36.590 26.990  -38.740  1.00 23.63 ? 26   ASN D C   1 
ATOM   2415  O  O   . ASN C  1 26  ? 36.914 26.173  -37.866  1.00 23.63 ? 26   ASN D O   1 
ATOM   2416  C  CB  . ASN C  1 26  ? 34.276 27.264  -39.699  1.00 24.90 ? 26   ASN D CB  1 
ATOM   2417  C  CG  . ASN C  1 26  ? 34.291 28.079  -41.010  1.00 27.18 ? 26   ASN D CG  1 
ATOM   2418  O  OD1 . ASN C  1 26  ? 34.822 27.632  -42.046  1.00 26.27 ? 26   ASN D OD1 1 
ATOM   2419  N  ND2 . ASN C  1 26  ? 33.689 29.285  -40.967  1.00 28.50 ? 26   ASN D ND2 1 
ATOM   2420  N  N   . GLY C  1 27  ? 37.347 27.288  -39.797  1.00 21.95 ? 27   GLY D N   1 
ATOM   2421  C  CA  . GLY C  1 27  ? 38.205 26.314  -40.430  1.00 19.61 ? 27   GLY D CA  1 
ATOM   2422  C  C   . GLY C  1 27  ? 39.644 26.149  -39.976  1.00 16.84 ? 27   GLY D C   1 
ATOM   2423  O  O   . GLY C  1 27  ? 40.013 26.533  -38.869  1.00 16.99 ? 27   GLY D O   1 
ATOM   2424  N  N   . PRO C  1 28  ? 40.449 25.554  -40.851  1.00 15.37 ? 28   PRO D N   1 
ATOM   2425  C  CA  . PRO C  1 28  ? 41.814 25.124  -40.624  1.00 13.20 ? 28   PRO D CA  1 
ATOM   2426  C  C   . PRO C  1 28  ? 42.783 26.248  -40.361  1.00 11.25 ? 28   PRO D C   1 
ATOM   2427  O  O   . PRO C  1 28  ? 42.724 27.311  -40.996  1.00 10.04 ? 28   PRO D O   1 
ATOM   2428  C  CB  . PRO C  1 28  ? 42.196 24.447  -41.940  1.00 13.43 ? 28   PRO D CB  1 
ATOM   2429  C  CG  . PRO C  1 28  ? 41.137 24.747  -42.883  1.00 15.08 ? 28   PRO D CG  1 
ATOM   2430  C  CD  . PRO C  1 28  ? 39.922 25.021  -42.118  1.00 15.82 ? 28   PRO D CD  1 
ATOM   2431  N  N   . VAL C  1 29  ? 43.691 25.983  -39.439  1.00 8.89  ? 29   VAL D N   1 
ATOM   2432  C  CA  . VAL C  1 29  ? 44.754 26.918  -39.132  1.00 6.84  ? 29   VAL D CA  1 
ATOM   2433  C  C   . VAL C  1 29  ? 45.988 26.434  -39.866  1.00 6.87  ? 29   VAL D C   1 
ATOM   2434  O  O   . VAL C  1 29  ? 46.397 25.268  -39.717  1.00 6.32  ? 29   VAL D O   1 
ATOM   2435  C  CB  . VAL C  1 29  ? 45.016 26.986  -37.606  1.00 6.77  ? 29   VAL D CB  1 
ATOM   2436  C  CG1 . VAL C  1 29  ? 46.082 28.093  -37.280  1.00 6.28  ? 29   VAL D CG1 1 
ATOM   2437  C  CG2 . VAL C  1 29  ? 43.716 27.298  -36.875  1.00 5.61  ? 29   VAL D CG2 1 
ATOM   2438  N  N   . LYS C  1 30  ? 46.582 27.302  -40.679  1.00 6.53  ? 30   LYS D N   1 
ATOM   2439  C  CA  . LYS C  1 30  ? 47.873 26.952  -41.259  1.00 6.50  ? 30   LYS D CA  1 
ATOM   2440  C  C   . LYS C  1 30  ? 48.977 27.363  -40.284  1.00 6.05  ? 30   LYS D C   1 
ATOM   2441  O  O   . LYS C  1 30  ? 48.917 28.461  -39.711  1.00 4.79  ? 30   LYS D O   1 
ATOM   2442  C  CB  . LYS C  1 30  ? 48.051 27.602  -42.616  1.00 7.42  ? 30   LYS D CB  1 
ATOM   2443  C  CG  . LYS C  1 30  ? 46.969 27.165  -43.639  1.00 10.55 ? 30   LYS D CG  1 
ATOM   2444  C  CD  . LYS C  1 30  ? 47.374 27.456  -45.074  1.00 16.04 ? 30   LYS D CD  1 
ATOM   2445  C  CE  . LYS C  1 30  ? 46.191 27.220  -46.015  1.00 19.47 ? 30   LYS D CE  1 
ATOM   2446  N  NZ  . LYS C  1 30  ? 46.212 28.175  -47.179  1.00 24.46 ? 30   LYS D NZ  1 
ATOM   2447  N  N   . VAL C  1 31  ? 49.948 26.470  -40.082  1.00 5.23  ? 31   VAL D N   1 
ATOM   2448  C  CA  . VAL C  1 31  ? 51.040 26.672  -39.081  1.00 5.72  ? 31   VAL D CA  1 
ATOM   2449  C  C   . VAL C  1 31  ? 52.364 26.513  -39.831  1.00 5.88  ? 31   VAL D C   1 
ATOM   2450  O  O   . VAL C  1 31  ? 52.582 25.473  -40.447  1.00 5.99  ? 31   VAL D O   1 
ATOM   2451  C  CB  . VAL C  1 31  ? 50.980 25.627  -37.925  1.00 5.83  ? 31   VAL D CB  1 
ATOM   2452  C  CG1 . VAL C  1 31  ? 52.130 25.877  -36.893  1.00 5.59  ? 31   VAL D CG1 1 
ATOM   2453  C  CG2 . VAL C  1 31  ? 49.590 25.608  -37.229  1.00 4.72  ? 31   VAL D CG2 1 
ATOM   2454  N  N   . TRP C  1 32  ? 53.220 27.539  -39.823  1.00 4.78  ? 32   TRP D N   1 
ATOM   2455  C  CA  . TRP C  1 32  ? 54.472 27.495  -40.605  1.00 5.55  ? 32   TRP D CA  1 
ATOM   2456  C  C   . TRP C  1 32  ? 55.549 28.431  -40.062  1.00 5.78  ? 32   TRP D C   1 
ATOM   2457  O  O   . TRP C  1 32  ? 55.254 29.454  -39.429  1.00 6.09  ? 32   TRP D O   1 
ATOM   2458  C  CB  . TRP C  1 32  ? 54.225 27.819  -42.100  1.00 5.67  ? 32   TRP D CB  1 
ATOM   2459  C  CG  . TRP C  1 32  ? 54.124 29.321  -42.462  1.00 5.27  ? 32   TRP D CG  1 
ATOM   2460  C  CD1 . TRP C  1 32  ? 55.117 30.129  -42.966  1.00 7.01  ? 32   TRP D CD1 1 
ATOM   2461  C  CD2 . TRP C  1 32  ? 52.958 30.160  -42.329  1.00 5.65  ? 32   TRP D CD2 1 
ATOM   2462  N  NE1 . TRP C  1 32  ? 54.628 31.423  -43.159  1.00 9.36  ? 32   TRP D NE1 1 
ATOM   2463  C  CE2 . TRP C  1 32  ? 53.314 31.460  -42.768  1.00 8.06  ? 32   TRP D CE2 1 
ATOM   2464  C  CE3 . TRP C  1 32  ? 51.653 29.931  -41.877  1.00 5.99  ? 32   TRP D CE3 1 
ATOM   2465  C  CZ2 . TRP C  1 32  ? 52.398 32.521  -42.793  1.00 8.93  ? 32   TRP D CZ2 1 
ATOM   2466  C  CZ3 . TRP C  1 32  ? 50.745 30.991  -41.877  1.00 9.15  ? 32   TRP D CZ3 1 
ATOM   2467  C  CH2 . TRP C  1 32  ? 51.127 32.274  -42.329  1.00 6.61  ? 32   TRP D CH2 1 
ATOM   2468  N  N   . GLY C  1 33  ? 56.793 28.102  -40.384  1.00 6.03  ? 33   GLY D N   1 
ATOM   2469  C  CA  . GLY C  1 33  ? 57.948 28.934  -40.044  1.00 6.79  ? 33   GLY D CA  1 
ATOM   2470  C  C   . GLY C  1 33  ? 59.143 28.043  -39.767  1.00 7.11  ? 33   GLY D C   1 
ATOM   2471  O  O   . GLY C  1 33  ? 59.087 26.837  -39.982  1.00 8.24  ? 33   GLY D O   1 
ATOM   2472  N  N   . SER C  1 34  ? 60.225 28.633  -39.290  1.00 7.46  ? 34   SER D N   1 
ATOM   2473  C  CA  . SER C  1 34  ? 61.473 27.887  -39.155  1.00 8.62  ? 34   SER D CA  1 
ATOM   2474  C  C   . SER C  1 34  ? 61.918 27.908  -37.699  1.00 7.36  ? 34   SER D C   1 
ATOM   2475  O  O   . SER C  1 34  ? 61.817 28.946  -37.039  1.00 8.59  ? 34   SER D O   1 
ATOM   2476  C  CB  . SER C  1 34  ? 62.532 28.494  -40.061  1.00 9.12  ? 34   SER D CB  1 
ATOM   2477  O  OG  . SER C  1 34  ? 63.757 27.834  -39.865  1.00 14.71 ? 34   SER D OG  1 
ATOM   2478  N  N   . ILE C  1 35  ? 62.355 26.759  -37.190  1.00 5.17  ? 35   ILE D N   1 
ATOM   2479  C  CA  . ILE C  1 35  ? 62.975 26.684  -35.875  1.00 4.40  ? 35   ILE D CA  1 
ATOM   2480  C  C   . ILE C  1 35  ? 64.379 26.141  -36.083  1.00 4.97  ? 35   ILE D C   1 
ATOM   2481  O  O   . ILE C  1 35  ? 64.549 25.070  -36.703  1.00 4.93  ? 35   ILE D O   1 
ATOM   2482  C  CB  . ILE C  1 35  ? 62.212 25.744  -34.932  1.00 3.74  ? 35   ILE D CB  1 
ATOM   2483  C  CG1 . ILE C  1 35  ? 60.744 26.154  -34.846  1.00 4.71  ? 35   ILE D CG1 1 
ATOM   2484  C  CG2 . ILE C  1 35  ? 62.869 25.700  -33.541  1.00 2.04  ? 35   ILE D CG2 1 
ATOM   2485  C  CD1 . ILE C  1 35  ? 59.851 25.110  -34.215  1.00 6.23  ? 35   ILE D CD1 1 
ATOM   2486  N  N   . LYS C  1 36  ? 65.372 26.853  -35.557  1.00 4.33  ? 36   LYS D N   1 
ATOM   2487  C  CA  . LYS C  1 36  ? 66.763 26.367  -35.671  1.00 5.60  ? 36   LYS D CA  1 
ATOM   2488  C  C   . LYS C  1 36  ? 67.313 25.875  -34.348  1.00 4.12  ? 36   LYS D C   1 
ATOM   2489  O  O   . LYS C  1 36  ? 66.720 26.105  -33.309  1.00 4.05  ? 36   LYS D O   1 
ATOM   2490  C  CB  . LYS C  1 36  ? 67.646 27.412  -36.344  1.00 5.81  ? 36   LYS D CB  1 
ATOM   2491  C  CG  . LYS C  1 36  ? 67.965 28.623  -35.509  1.00 8.66  ? 36   LYS D CG  1 
ATOM   2492  C  CD  . LYS C  1 36  ? 68.786 29.582  -36.325  1.00 11.45 ? 36   LYS D CD  1 
ATOM   2493  C  CE  . LYS C  1 36  ? 69.232 30.750  -35.475  1.00 14.58 ? 36   LYS D CE  1 
ATOM   2494  N  NZ  . LYS C  1 36  ? 70.007 31.688  -36.349  1.00 16.89 ? 36   LYS D NZ  1 
ATOM   2495  N  N   . GLY C  1 37  ? 68.432 25.159  -34.383  1.00 3.70  ? 37   GLY D N   1 
ATOM   2496  C  CA  . GLY C  1 37  ? 69.094 24.731  -33.146  1.00 2.80  ? 37   GLY D CA  1 
ATOM   2497  C  C   . GLY C  1 37  ? 68.599 23.413  -32.580  1.00 2.00  ? 37   GLY D C   1 
ATOM   2498  O  O   . GLY C  1 37  ? 68.845 23.111  -31.412  1.00 2.66  ? 37   GLY D O   1 
ATOM   2499  N  N   . LEU C  1 38  ? 67.871 22.655  -33.397  1.00 2.00  ? 38   LEU D N   1 
ATOM   2500  C  CA  . LEU C  1 38  ? 67.254 21.406  -32.965  1.00 2.07  ? 38   LEU D CA  1 
ATOM   2501  C  C   . LEU C  1 38  ? 68.047 20.214  -33.462  1.00 2.00  ? 38   LEU D C   1 
ATOM   2502  O  O   . LEU C  1 38  ? 68.571 20.242  -34.585  1.00 3.10  ? 38   LEU D O   1 
ATOM   2503  C  CB  . LEU C  1 38  ? 65.831 21.291  -33.556  1.00 2.00  ? 38   LEU D CB  1 
ATOM   2504  C  CG  . LEU C  1 38  ? 64.726 22.139  -32.907  1.00 2.00  ? 38   LEU D CG  1 
ATOM   2505  C  CD1 . LEU C  1 38  ? 63.572 22.267  -33.932  1.00 2.00  ? 38   LEU D CD1 1 
ATOM   2506  C  CD2 . LEU C  1 38  ? 64.276 21.586  -31.527  1.00 2.00  ? 38   LEU D CD2 1 
ATOM   2507  N  N   . THR C  1 39  ? 68.134 19.151  -32.679  1.00 3.77  ? 39   THR D N   1 
ATOM   2508  C  CA  . THR C  1 39  ? 68.831 17.952  -33.186  1.00 4.28  ? 39   THR D CA  1 
ATOM   2509  C  C   . THR C  1 39  ? 68.063 17.357  -34.380  1.00 5.27  ? 39   THR D C   1 
ATOM   2510  O  O   . THR C  1 39  ? 66.825 17.354  -34.396  1.00 5.41  ? 39   THR D O   1 
ATOM   2511  C  CB  . THR C  1 39  ? 69.022 16.859  -32.098  1.00 5.13  ? 39   THR D CB  1 
ATOM   2512  O  OG1 . THR C  1 39  ? 67.752 16.491  -31.546  1.00 5.23  ? 39   THR D OG1 1 
ATOM   2513  C  CG2 . THR C  1 39  ? 69.920 17.367  -30.956  1.00 4.33  ? 39   THR D CG2 1 
ATOM   2514  N  N   . GLU C  1 40  ? 68.786 16.840  -35.369  1.00 5.28  ? 40   GLU D N   1 
ATOM   2515  C  CA  . GLU C  1 40  ? 68.139 16.170  -36.498  1.00 5.11  ? 40   GLU D CA  1 
ATOM   2516  C  C   . GLU C  1 40  ? 67.138 15.120  -36.038  1.00 5.01  ? 40   GLU D C   1 
ATOM   2517  O  O   . GLU C  1 40  ? 67.448 14.297  -35.173  1.00 4.80  ? 40   GLU D O   1 
ATOM   2518  C  CB  . GLU C  1 40  ? 69.172 15.496  -37.413  1.00 5.44  ? 40   GLU D CB  1 
ATOM   2519  C  CG  . GLU C  1 40  ? 68.519 14.992  -38.718  1.00 6.86  ? 40   GLU D CG  1 
ATOM   2520  C  CD  . GLU C  1 40  ? 69.504 14.438  -39.713  1.00 12.08 ? 40   GLU D CD  1 
ATOM   2521  O  OE1 . GLU C  1 40  ? 70.693 14.385  -39.395  1.00 12.37 ? 40   GLU D OE1 1 
ATOM   2522  O  OE2 . GLU C  1 40  ? 69.068 14.041  -40.814  1.00 15.14 ? 40   GLU D OE2 1 
ATOM   2523  N  N   . GLY C  1 41  ? 65.939 15.183  -36.607  1.00 4.41  ? 41   GLY D N   1 
ATOM   2524  C  CA  . GLY C  1 41  ? 64.898 14.221  -36.313  1.00 4.54  ? 41   GLY D CA  1 
ATOM   2525  C  C   . GLY C  1 41  ? 63.638 14.858  -35.765  1.00 4.30  ? 41   GLY D C   1 
ATOM   2526  O  O   . GLY C  1 41  ? 63.418 16.057  -35.924  1.00 3.46  ? 41   GLY D O   1 
ATOM   2527  N  N   . LEU C  1 42  ? 62.823 14.033  -35.107  1.00 3.50  ? 42   LEU D N   1 
ATOM   2528  C  CA  . LEU C  1 42  ? 61.482 14.416  -34.670  1.00 3.45  ? 42   LEU D CA  1 
ATOM   2529  C  C   . LEU C  1 42  ? 61.485 15.083  -33.301  1.00 3.54  ? 42   LEU D C   1 
ATOM   2530  O  O   . LEU C  1 42  ? 62.222 14.652  -32.404  1.00 3.94  ? 42   LEU D O   1 
ATOM   2531  C  CB  . LEU C  1 42  ? 60.622 13.144  -34.579  1.00 4.70  ? 42   LEU D CB  1 
ATOM   2532  C  CG  . LEU C  1 42  ? 60.253 12.409  -35.856  1.00 4.88  ? 42   LEU D CG  1 
ATOM   2533  C  CD1 . LEU C  1 42  ? 59.640 11.045  -35.414  1.00 8.34  ? 42   LEU D CD1 1 
ATOM   2534  C  CD2 . LEU C  1 42  ? 59.264 13.174  -36.743  1.00 5.86  ? 42   LEU D CD2 1 
ATOM   2535  N  N   . HIS C  1 43  ? 60.650 16.115  -33.138  1.00 2.90  ? 43   HIS D N   1 
ATOM   2536  C  CA  . HIS C  1 43  ? 60.521 16.856  -31.866  1.00 2.00  ? 43   HIS D CA  1 
ATOM   2537  C  C   . HIS C  1 43  ? 59.060 17.184  -31.621  1.00 2.00  ? 43   HIS D C   1 
ATOM   2538  O  O   . HIS C  1 43  ? 58.393 17.702  -32.522  1.00 2.00  ? 43   HIS D O   1 
ATOM   2539  C  CB  . HIS C  1 43  ? 61.310 18.174  -31.933  1.00 2.00  ? 43   HIS D CB  1 
ATOM   2540  C  CG  . HIS C  1 43  ? 62.793 17.971  -31.988  1.00 2.70  ? 43   HIS D CG  1 
ATOM   2541  N  ND1 . HIS C  1 43  ? 63.564 17.808  -30.851  1.00 2.00  ? 43   HIS D ND1 1 
ATOM   2542  C  CD2 . HIS C  1 43  ? 63.631 17.818  -33.044  1.00 2.00  ? 43   HIS D CD2 1 
ATOM   2543  C  CE1 . HIS C  1 43  ? 64.824 17.615  -31.208  1.00 3.03  ? 43   HIS D CE1 1 
ATOM   2544  N  NE2 . HIS C  1 43  ? 64.885 17.592  -32.533  1.00 3.50  ? 43   HIS D NE2 1 
ATOM   2545  N  N   . GLY C  1 44  ? 58.584 16.904  -30.408  1.00 2.00  ? 44   GLY D N   1 
ATOM   2546  C  CA  . GLY C  1 44  ? 57.176 17.115  -30.057  1.00 2.00  ? 44   GLY D CA  1 
ATOM   2547  C  C   . GLY C  1 44  ? 56.875 18.593  -30.164  1.00 2.08  ? 44   GLY D C   1 
ATOM   2548  O  O   . GLY C  1 44  ? 57.769 19.439  -29.957  1.00 2.11  ? 44   GLY D O   1 
ATOM   2549  N  N   . PHE C  1 45  ? 55.618 18.919  -30.467  1.00 2.27  ? 45   PHE D N   1 
ATOM   2550  C  CA  . PHE C  1 45  ? 55.274 20.295  -30.791  1.00 2.00  ? 45   PHE D CA  1 
ATOM   2551  C  C   . PHE C  1 45  ? 53.840 20.506  -30.399  1.00 2.00  ? 45   PHE D C   1 
ATOM   2552  O  O   . PHE C  1 45  ? 52.961 19.990  -31.066  1.00 2.55  ? 45   PHE D O   1 
ATOM   2553  C  CB  . PHE C  1 45  ? 55.449 20.434  -32.304  1.00 2.00  ? 45   PHE D CB  1 
ATOM   2554  C  CG  . PHE C  1 45  ? 55.322 21.824  -32.854  1.00 2.41  ? 45   PHE D CG  1 
ATOM   2555  C  CD1 . PHE C  1 45  ? 56.243 22.816  -32.522  1.00 4.82  ? 45   PHE D CD1 1 
ATOM   2556  C  CD2 . PHE C  1 45  ? 54.365 22.091  -33.822  1.00 2.00  ? 45   PHE D CD2 1 
ATOM   2557  C  CE1 . PHE C  1 45  ? 56.149 24.090  -33.092  1.00 4.07  ? 45   PHE D CE1 1 
ATOM   2558  C  CE2 . PHE C  1 45  ? 54.256 23.365  -34.420  1.00 4.87  ? 45   PHE D CE2 1 
ATOM   2559  C  CZ  . PHE C  1 45  ? 55.183 24.365  -34.051  1.00 4.07  ? 45   PHE D CZ  1 
ATOM   2560  N  N   . HIS C  1 46  ? 53.601 21.234  -29.300  1.00 2.77  ? 46   HIS D N   1 
ATOM   2561  C  CA  . HIS C  1 46  ? 52.240 21.389  -28.770  1.00 2.95  ? 46   HIS D CA  1 
ATOM   2562  C  C   . HIS C  1 46  ? 51.952 22.789  -28.297  1.00 2.59  ? 46   HIS D C   1 
ATOM   2563  O  O   . HIS C  1 46  ? 52.877 23.580  -27.995  1.00 3.06  ? 46   HIS D O   1 
ATOM   2564  C  CB  . HIS C  1 46  ? 51.982 20.462  -27.587  1.00 2.00  ? 46   HIS D CB  1 
ATOM   2565  C  CG  . HIS C  1 46  ? 52.729 19.173  -27.662  1.00 3.44  ? 46   HIS D CG  1 
ATOM   2566  N  ND1 . HIS C  1 46  ? 53.823 18.910  -26.870  1.00 4.44  ? 46   HIS D ND1 1 
ATOM   2567  C  CD2 . HIS C  1 46  ? 52.539 18.072  -28.426  1.00 4.41  ? 46   HIS D CD2 1 
ATOM   2568  C  CE1 . HIS C  1 46  ? 54.269 17.694  -27.135  1.00 5.79  ? 46   HIS D CE1 1 
ATOM   2569  N  NE2 . HIS C  1 46  ? 53.510 17.167  -28.081  1.00 2.64  ? 46   HIS D NE2 1 
ATOM   2570  N  N   . VAL C  1 47  ? 50.655 23.085  -28.234  1.00 2.92  ? 47   VAL D N   1 
ATOM   2571  C  CA  . VAL C  1 47  ? 50.193 24.269  -27.544  1.00 2.82  ? 47   VAL D CA  1 
ATOM   2572  C  C   . VAL C  1 47  ? 49.896 23.852  -26.115  1.00 2.63  ? 47   VAL D C   1 
ATOM   2573  O  O   . VAL C  1 47  ? 49.089 22.930  -25.868  1.00 3.99  ? 47   VAL D O   1 
ATOM   2574  C  CB  . VAL C  1 47  ? 48.935 24.895  -28.195  1.00 2.68  ? 47   VAL D CB  1 
ATOM   2575  C  CG1 . VAL C  1 47  ? 48.501 26.138  -27.424  1.00 3.52  ? 47   VAL D CG1 1 
ATOM   2576  C  CG2 . VAL C  1 47  ? 49.198 25.272  -29.659  1.00 3.23  ? 47   VAL D CG2 1 
ATOM   2577  N  N   . HIS C  1 48  ? 50.534 24.532  -25.164  1.00 2.62  ? 48   HIS D N   1 
ATOM   2578  C  CA  . HIS C  1 48  ? 50.291 24.299  -23.743  1.00 2.00  ? 48   HIS D CA  1 
ATOM   2579  C  C   . HIS C  1 48  ? 49.288 25.307  -23.171  1.00 2.33  ? 48   HIS D C   1 
ATOM   2580  O  O   . HIS C  1 48  ? 49.078 26.364  -23.736  1.00 2.16  ? 48   HIS D O   1 
ATOM   2581  C  CB  . HIS C  1 48  ? 51.601 24.326  -22.945  1.00 2.12  ? 48   HIS D CB  1 
ATOM   2582  C  CG  . HIS C  1 48  ? 52.476 23.152  -23.225  1.00 2.00  ? 48   HIS D CG  1 
ATOM   2583  N  ND1 . HIS C  1 48  ? 52.979 22.322  -22.239  1.00 2.37  ? 48   HIS D ND1 1 
ATOM   2584  C  CD2 . HIS C  1 48  ? 52.913 22.654  -24.406  1.00 3.20  ? 48   HIS D CD2 1 
ATOM   2585  C  CE1 . HIS C  1 48  ? 53.696 21.367  -22.808  1.00 2.39  ? 48   HIS D CE1 1 
ATOM   2586  N  NE2 . HIS C  1 48  ? 53.684 21.561  -24.119  1.00 2.00  ? 48   HIS D NE2 1 
ATOM   2587  N  N   . GLU C  1 49  ? 48.698 24.965  -22.042  1.00 2.51  ? 49   GLU D N   1 
ATOM   2588  C  CA  . GLU C  1 49  ? 47.511 25.651  -21.542  1.00 2.94  ? 49   GLU D CA  1 
ATOM   2589  C  C   . GLU C  1 49  ? 47.707 27.156  -21.236  1.00 3.57  ? 49   GLU D C   1 
ATOM   2590  O  O   . GLU C  1 49  ? 46.862 27.982  -21.604  1.00 2.79  ? 49   GLU D O   1 
ATOM   2591  C  CB  . GLU C  1 49  ? 46.996 24.947  -20.307  1.00 4.60  ? 49   GLU D CB  1 
ATOM   2592  C  CG  . GLU C  1 49  ? 45.646 25.515  -19.808  1.00 4.75  ? 49   GLU D CG  1 
ATOM   2593  C  CD  . GLU C  1 49  ? 45.101 24.731  -18.664  1.00 7.82  ? 49   GLU D CD  1 
ATOM   2594  O  OE1 . GLU C  1 49  ? 43.955 25.038  -18.233  1.00 6.25  ? 49   GLU D OE1 1 
ATOM   2595  O  OE2 . GLU C  1 49  ? 45.820 23.831  -18.189  1.00 8.70  ? 49   GLU D OE2 1 
ATOM   2596  N  N   . PHE C  1 50  ? 48.809 27.483  -20.564  1.00 3.74  ? 50   PHE D N   1 
ATOM   2597  C  CA  . PHE C  1 50  ? 49.018 28.841  -20.059  1.00 3.10  ? 50   PHE D CA  1 
ATOM   2598  C  C   . PHE C  1 50  ? 50.067 29.611  -20.837  1.00 3.94  ? 50   PHE D C   1 
ATOM   2599  O  O   . PHE C  1 50  ? 51.140 29.076  -21.122  1.00 4.67  ? 50   PHE D O   1 
ATOM   2600  C  CB  . PHE C  1 50  ? 49.396 28.803  -18.574  1.00 4.06  ? 50   PHE D CB  1 
ATOM   2601  C  CG  . PHE C  1 50  ? 48.402 28.062  -17.740  1.00 7.14  ? 50   PHE D CG  1 
ATOM   2602  C  CD1 . PHE C  1 50  ? 47.067 28.462  -17.719  1.00 7.44  ? 50   PHE D CD1 1 
ATOM   2603  C  CD2 . PHE C  1 50  ? 48.775 26.925  -17.036  1.00 8.68  ? 50   PHE D CD2 1 
ATOM   2604  C  CE1 . PHE C  1 50  ? 46.110 27.729  -16.951  1.00 11.00 ? 50   PHE D CE1 1 
ATOM   2605  C  CE2 . PHE C  1 50  ? 47.839 26.222  -16.283  1.00 11.23 ? 50   PHE D CE2 1 
ATOM   2606  C  CZ  . PHE C  1 50  ? 46.516 26.633  -16.239  1.00 8.71  ? 50   PHE D CZ  1 
ATOM   2607  N  N   . GLY C  1 51  ? 49.779 30.887  -21.099  1.00 3.45  ? 51   GLY D N   1 
ATOM   2608  C  CA  . GLY C  1 51  ? 50.725 31.820  -21.720  1.00 4.04  ? 51   GLY D CA  1 
ATOM   2609  C  C   . GLY C  1 51  ? 51.547 32.489  -20.623  1.00 3.82  ? 51   GLY D C   1 
ATOM   2610  O  O   . GLY C  1 51  ? 51.696 33.716  -20.589  1.00 2.73  ? 51   GLY D O   1 
ATOM   2611  N  N   . ASP C  1 52  ? 52.056 31.650  -19.723  1.00 4.26  ? 52   ASP D N   1 
ATOM   2612  C  CA  . ASP C  1 52  ? 52.793 32.040  -18.528  1.00 5.36  ? 52   ASP D CA  1 
ATOM   2613  C  C   . ASP C  1 52  ? 54.231 31.549  -18.661  1.00 5.89  ? 52   ASP D C   1 
ATOM   2614  O  O   . ASP C  1 52  ? 54.500 30.350  -18.575  1.00 6.68  ? 52   ASP D O   1 
ATOM   2615  C  CB  . ASP C  1 52  ? 52.154 31.395  -17.274  1.00 5.17  ? 52   ASP D CB  1 
ATOM   2616  C  CG  . ASP C  1 52  ? 52.780 31.891  -15.973  1.00 5.24  ? 52   ASP D CG  1 
ATOM   2617  O  OD1 . ASP C  1 52  ? 52.109 31.845  -14.920  1.00 7.37  ? 52   ASP D OD1 1 
ATOM   2618  O  OD2 . ASP C  1 52  ? 53.951 32.328  -15.995  1.00 5.69  ? 52   ASP D OD2 1 
ATOM   2619  N  N   . ASN C  1 53  ? 55.159 32.455  -18.906  1.00 5.87  ? 53   ASN D N   1 
ATOM   2620  C  CA  . ASN C  1 53  ? 56.551 32.032  -19.007  1.00 6.47  ? 53   ASN D CA  1 
ATOM   2621  C  C   . ASN C  1 53  ? 57.400 32.652  -17.866  1.00 6.89  ? 53   ASN D C   1 
ATOM   2622  O  O   . ASN C  1 53  ? 58.617 32.877  -18.024  1.00 6.81  ? 53   ASN D O   1 
ATOM   2623  C  CB  . ASN C  1 53  ? 57.104 32.343  -20.418  1.00 7.39  ? 53   ASN D CB  1 
ATOM   2624  C  CG  . ASN C  1 53  ? 56.457 31.475  -21.576  1.00 9.19  ? 53   ASN D CG  1 
ATOM   2625  O  OD1 . ASN C  1 53  ? 56.732 31.728  -22.768  1.00 14.03 ? 53   ASN D OD1 1 
ATOM   2626  N  ND2 . ASN C  1 53  ? 55.657 30.464  -21.236  1.00 9.17  ? 53   ASN D ND2 1 
ATOM   2627  N  N   . THR C  1 54  ? 56.752 32.925  -16.721  1.00 6.13  ? 54   THR D N   1 
ATOM   2628  C  CA  . THR C  1 54  ? 57.417 33.519  -15.533  1.00 6.04  ? 54   THR D CA  1 
ATOM   2629  C  C   . THR C  1 54  ? 58.562 32.669  -14.997  1.00 6.71  ? 54   THR D C   1 
ATOM   2630  O  O   . THR C  1 54  ? 59.546 33.209  -14.497  1.00 5.72  ? 54   THR D O   1 
ATOM   2631  C  CB  . THR C  1 54  ? 56.431 33.849  -14.370  1.00 5.39  ? 54   THR D CB  1 
ATOM   2632  O  OG1 . THR C  1 54  ? 55.662 32.685  -14.026  1.00 6.25  ? 54   THR D OG1 1 
ATOM   2633  C  CG2 . THR C  1 54  ? 55.484 34.995  -14.779  1.00 6.14  ? 54   THR D CG2 1 
ATOM   2634  N  N   . ALA C  1 55  ? 58.428 31.353  -15.123  1.00 6.21  ? 55   ALA D N   1 
ATOM   2635  C  CA  . ALA C  1 55  ? 59.508 30.436  -14.774  1.00 9.02  ? 55   ALA D CA  1 
ATOM   2636  C  C   . ALA C  1 55  ? 59.877 29.649  -16.021  1.00 9.75  ? 55   ALA D C   1 
ATOM   2637  O  O   . ALA C  1 55  ? 59.853 28.427  -16.014  1.00 12.12 ? 55   ALA D O   1 
ATOM   2638  C  CB  . ALA C  1 55  ? 59.075 29.490  -13.640  1.00 9.08  ? 55   ALA D CB  1 
ATOM   2639  N  N   . GLY C  1 56  ? 60.177 30.349  -17.103  1.00 8.90  ? 56   GLY D N   1 
ATOM   2640  C  CA  . GLY C  1 56  ? 60.568 29.681  -18.351  1.00 7.98  ? 56   GLY D CA  1 
ATOM   2641  C  C   . GLY C  1 56  ? 59.435 28.830  -18.886  1.00 6.87  ? 56   GLY D C   1 
ATOM   2642  O  O   . GLY C  1 56  ? 58.248 29.116  -18.603  1.00 7.36  ? 56   GLY D O   1 
ATOM   2643  N  N   . CYS C  1 57  ? 59.764 27.761  -19.617  1.00 4.99  ? 57   CYS D N   1 
ATOM   2644  C  CA  . CYS C  1 57  ? 58.682 26.991  -20.295  1.00 3.63  ? 57   CYS D CA  1 
ATOM   2645  C  C   . CYS C  1 57  ? 57.847 26.137  -19.334  1.00 4.14  ? 57   CYS D C   1 
ATOM   2646  O  O   . CYS C  1 57  ? 56.719 25.740  -19.651  1.00 3.48  ? 57   CYS D O   1 
ATOM   2647  C  CB  . CYS C  1 57  ? 59.260 26.148  -21.438  0.40 2.20  ? 57   CYS D CB  1 
ATOM   2648  S  SG  . CYS C  1 57  ? 60.126 27.137  -22.682  0.40 2.00  ? 57   CYS D SG  1 
ATOM   2649  N  N   . THR C  1 58  ? 58.378 25.888  -18.143  1.00 4.21  ? 58   THR D N   1 
ATOM   2650  C  CA  . THR C  1 58  ? 57.690 25.049  -17.145  1.00 5.88  ? 58   THR D CA  1 
ATOM   2651  C  C   . THR C  1 58  ? 56.354 25.618  -16.713  1.00 6.05  ? 58   THR D C   1 
ATOM   2652  O  O   . THR C  1 58  ? 55.398 24.868  -16.482  1.00 5.98  ? 58   THR D O   1 
ATOM   2653  C  CB  . THR C  1 58  ? 58.556 24.871  -15.881  1.00 6.12  ? 58   THR D CB  1 
ATOM   2654  O  OG1 . THR C  1 58  ? 59.791 24.266  -16.274  1.00 9.80  ? 58   THR D OG1 1 
ATOM   2655  C  CG2 . THR C  1 58  ? 57.868 23.962  -14.889  1.00 8.18  ? 58   THR D CG2 1 
ATOM   2656  N  N   . SER C  1 59  ? 56.320 26.950  -16.588  1.00 5.80  ? 59   SER D N   1 
ATOM   2657  C  CA  . SER C  1 59  ? 55.134 27.750  -16.222  1.00 6.99  ? 59   SER D CA  1 
ATOM   2658  C  C   . SER C  1 59  ? 53.916 27.611  -17.125  1.00 5.22  ? 59   SER D C   1 
ATOM   2659  O  O   . SER C  1 59  ? 52.811 28.001  -16.738  1.00 4.80  ? 59   SER D O   1 
ATOM   2660  C  CB  . SER C  1 59  ? 55.540 29.228  -16.274  1.00 6.14  ? 59   SER D CB  1 
ATOM   2661  O  OG  . SER C  1 59  ? 56.572 29.465  -15.407  1.00 12.82 ? 59   SER D OG  1 
ATOM   2662  N  N   . ALA C  1 60  ? 54.131 27.117  -18.348  1.00 3.77  ? 60   ALA D N   1 
ATOM   2663  C  CA  . ALA C  1 60  ? 53.094 26.985  -19.372  1.00 3.03  ? 60   ALA D CA  1 
ATOM   2664  C  C   . ALA C  1 60  ? 52.070 25.885  -19.066  1.00 3.41  ? 60   ALA D C   1 
ATOM   2665  O  O   . ALA C  1 60  ? 51.011 25.827  -19.680  1.00 2.84  ? 60   ALA D O   1 
ATOM   2666  C  CB  . ALA C  1 60  ? 53.750 26.719  -20.760  1.00 2.36  ? 60   ALA D CB  1 
ATOM   2667  N  N   . GLY C  1 61  ? 52.399 25.034  -18.094  1.00 2.93  ? 61   GLY D N   1 
ATOM   2668  C  CA  . GLY C  1 61  ? 51.506 23.986  -17.647  1.00 4.33  ? 61   GLY D CA  1 
ATOM   2669  C  C   . GLY C  1 61  ? 51.426 22.872  -18.675  1.00 4.42  ? 61   GLY D C   1 
ATOM   2670  O  O   . GLY C  1 61  ? 52.363 22.716  -19.498  1.00 4.27  ? 61   GLY D O   1 
ATOM   2671  N  N   . PRO C  1 62  ? 50.326 22.087  -18.631  1.00 4.49  ? 62   PRO D N   1 
ATOM   2672  C  CA  . PRO C  1 62  ? 50.212 20.902  -19.461  1.00 4.36  ? 62   PRO D CA  1 
ATOM   2673  C  C   . PRO C  1 62  ? 49.721 21.257  -20.862  1.00 4.23  ? 62   PRO D C   1 
ATOM   2674  O  O   . PRO C  1 62  ? 49.549 22.439  -21.178  1.00 3.90  ? 62   PRO D O   1 
ATOM   2675  C  CB  . PRO C  1 62  ? 49.180 20.032  -18.691  1.00 4.34  ? 62   PRO D CB  1 
ATOM   2676  C  CG  . PRO C  1 62  ? 48.251 21.038  -18.029  1.00 5.26  ? 62   PRO D CG  1 
ATOM   2677  C  CD  . PRO C  1 62  ? 49.187 22.218  -17.684  1.00 4.54  ? 62   PRO D CD  1 
ATOM   2678  N  N   . HIS C  1 63  ? 49.514 20.253  -21.719  1.00 3.54  ? 63   HIS D N   1 
ATOM   2679  C  CA  . HIS C  1 63  ? 48.953 20.525  -23.043  1.00 3.16  ? 63   HIS D CA  1 
ATOM   2680  C  C   . HIS C  1 63  ? 47.570 21.132  -22.915  1.00 3.30  ? 63   HIS D C   1 
ATOM   2681  O  O   . HIS C  1 63  ? 46.824 20.784  -21.997  1.00 3.47  ? 63   HIS D O   1 
ATOM   2682  C  CB  . HIS C  1 63  ? 48.893 19.248  -23.873  1.00 2.83  ? 63   HIS D CB  1 
ATOM   2683  C  CG  . HIS C  1 63  ? 50.235 18.619  -24.071  1.00 3.98  ? 63   HIS D CG  1 
ATOM   2684  N  ND1 . HIS C  1 63  ? 50.428 17.509  -24.858  1.00 2.00  ? 63   HIS D ND1 1 
ATOM   2685  C  CD2 . HIS C  1 63  ? 51.459 18.958  -23.590  1.00 2.00  ? 63   HIS D CD2 1 
ATOM   2686  C  CE1 . HIS C  1 63  ? 51.708 17.168  -24.837  1.00 3.99  ? 63   HIS D CE1 1 
ATOM   2687  N  NE2 . HIS C  1 63  ? 52.352 18.025  -24.064  1.00 4.18  ? 63   HIS D NE2 1 
ATOM   2688  N  N   . PHE C  1 64  ? 47.264 22.064  -23.808  1.00 3.60  ? 64   PHE D N   1 
ATOM   2689  C  CA  . PHE C  1 64  ? 45.949 22.741  -23.846  1.00 3.60  ? 64   PHE D CA  1 
ATOM   2690  C  C   . PHE C  1 64  ? 44.917 21.666  -24.138  1.00 3.72  ? 64   PHE D C   1 
ATOM   2691  O  O   . PHE C  1 64  ? 45.001 20.968  -25.150  1.00 3.30  ? 64   PHE D O   1 
ATOM   2692  C  CB  . PHE C  1 64  ? 45.957 23.835  -24.902  1.00 4.27  ? 64   PHE D CB  1 
ATOM   2693  C  CG  . PHE C  1 64  ? 44.627 24.572  -25.079  1.00 2.00  ? 64   PHE D CG  1 
ATOM   2694  C  CD1 . PHE C  1 64  ? 44.200 24.934  -26.345  1.00 2.10  ? 64   PHE D CD1 1 
ATOM   2695  C  CD2 . PHE C  1 64  ? 43.839 24.912  -23.975  1.00 4.82  ? 64   PHE D CD2 1 
ATOM   2696  C  CE1 . PHE C  1 64  ? 42.995 25.622  -26.539  1.00 4.14  ? 64   PHE D CE1 1 
ATOM   2697  C  CE2 . PHE C  1 64  ? 42.620 25.586  -24.148  1.00 3.93  ? 64   PHE D CE2 1 
ATOM   2698  C  CZ  . PHE C  1 64  ? 42.211 25.960  -25.420  1.00 2.72  ? 64   PHE D CZ  1 
ATOM   2699  N  N   . ASN C  1 65  ? 43.962 21.515  -23.232  1.00 4.04  ? 65   ASN D N   1 
ATOM   2700  C  CA  . ASN C  1 65  ? 43.081 20.326  -23.245  1.00 4.83  ? 65   ASN D CA  1 
ATOM   2701  C  C   . ASN C  1 65  ? 41.685 20.634  -22.675  1.00 4.60  ? 65   ASN D C   1 
ATOM   2702  O  O   . ASN C  1 65  ? 41.312 20.069  -21.663  1.00 5.63  ? 65   ASN D O   1 
ATOM   2703  C  CB  . ASN C  1 65  ? 43.733 19.207  -22.438  1.00 3.82  ? 65   ASN D CB  1 
ATOM   2704  C  CG  . ASN C  1 65  ? 42.961 17.881  -22.500  1.00 5.76  ? 65   ASN D CG  1 
ATOM   2705  O  OD1 . ASN C  1 65  ? 42.268 17.607  -23.458  1.00 6.90  ? 65   ASN D OD1 1 
ATOM   2706  N  ND2 . ASN C  1 65  ? 43.103 17.057  -21.462  1.00 5.23  ? 65   ASN D ND2 1 
ATOM   2707  N  N   . PRO C  1 66  ? 40.940 21.551  -23.311  1.00 5.87  ? 66   PRO D N   1 
ATOM   2708  C  CA  . PRO C  1 66  ? 39.678 22.008  -22.721  1.00 6.71  ? 66   PRO D CA  1 
ATOM   2709  C  C   . PRO C  1 66  ? 38.573 20.924  -22.774  1.00 8.39  ? 66   PRO D C   1 
ATOM   2710  O  O   . PRO C  1 66  ? 37.564 21.027  -22.062  1.00 9.49  ? 66   PRO D O   1 
ATOM   2711  C  CB  . PRO C  1 66  ? 39.341 23.254  -23.548  1.00 5.75  ? 66   PRO D CB  1 
ATOM   2712  C  CG  . PRO C  1 66  ? 39.933 22.972  -24.907  1.00 7.46  ? 66   PRO D CG  1 
ATOM   2713  C  CD  . PRO C  1 66  ? 41.242 22.242  -24.577  1.00 5.90  ? 66   PRO D CD  1 
ATOM   2714  N  N   . LEU C  1 67  ? 38.798 19.871  -23.558  1.00 8.07  ? 67   LEU D N   1 
ATOM   2715  C  CA  . LEU C  1 67  ? 37.855 18.744  -23.593  1.00 8.91  ? 67   LEU D CA  1 
ATOM   2716  C  C   . LEU C  1 67  ? 38.284 17.555  -22.722  1.00 8.85  ? 67   LEU D C   1 
ATOM   2717  O  O   . LEU C  1 67  ? 37.658 16.483  -22.772  1.00 9.76  ? 67   LEU D O   1 
ATOM   2718  C  CB  . LEU C  1 67  ? 37.570 18.348  -25.043  1.00 8.47  ? 67   LEU D CB  1 
ATOM   2719  C  CG  . LEU C  1 67  ? 36.734 19.386  -25.802  1.00 10.29 ? 67   LEU D CG  1 
ATOM   2720  C  CD1 . LEU C  1 67  ? 36.850 19.185  -27.295  1.00 9.83  ? 67   LEU D CD1 1 
ATOM   2721  C  CD2 . LEU C  1 67  ? 35.263 19.368  -25.339  1.00 7.87  ? 67   LEU D CD2 1 
ATOM   2722  N  N   . SER C  1 68  ? 39.321 17.749  -21.900  1.00 9.00  ? 68   SER D N   1 
ATOM   2723  C  CA  . SER C  1 68  ? 39.779 16.717  -20.926  1.00 9.29  ? 68   SER D CA  1 
ATOM   2724  C  C   . SER C  1 68  ? 39.918 15.344  -21.586  1.00 9.36  ? 68   SER D C   1 
ATOM   2725  O  O   . SER C  1 68  ? 39.404 14.325  -21.097  1.00 9.64  ? 68   SER D O   1 
ATOM   2726  C  CB  . SER C  1 68  ? 38.866 16.678  -19.672  1.00 9.80  ? 68   SER D CB  1 
ATOM   2727  O  OG  . SER C  1 68  ? 38.805 17.954  -19.023  1.00 11.03 ? 68   SER D OG  1 
ATOM   2728  N  N   . ARG C  1 69  ? 40.598 15.325  -22.729  1.00 9.10  ? 69   ARG D N   1 
ATOM   2729  C  CA  . ARG C  1 69  ? 40.884 14.072  -23.428  1.00 9.03  ? 69   ARG D CA  1 
ATOM   2730  C  C   . ARG C  1 69  ? 42.296 13.586  -23.108  1.00 8.52  ? 69   ARG D C   1 
ATOM   2731  O  O   . ARG C  1 69  ? 43.079 14.300  -22.472  1.00 8.86  ? 69   ARG D O   1 
ATOM   2732  C  CB  . ARG C  1 69  ? 40.785 14.273  -24.942  1.00 8.60  ? 69   ARG D CB  1 
ATOM   2733  C  CG  . ARG C  1 69  ? 39.509 14.965  -25.403  1.00 10.67 ? 69   ARG D CG  1 
ATOM   2734  C  CD  . ARG C  1 69  ? 38.276 14.068  -25.151  1.00 11.80 ? 69   ARG D CD  1 
ATOM   2735  N  NE  . ARG C  1 69  ? 37.080 14.660  -25.747  1.00 14.31 ? 69   ARG D NE  1 
ATOM   2736  C  CZ  . ARG C  1 69  ? 35.875 14.681  -25.185  1.00 14.24 ? 69   ARG D CZ  1 
ATOM   2737  N  NH1 . ARG C  1 69  ? 34.870 15.283  -25.815  1.00 12.88 ? 69   ARG D NH1 1 
ATOM   2738  N  NH2 . ARG C  1 69  ? 35.676 14.124  -23.998  1.00 12.25 ? 69   ARG D NH2 1 
ATOM   2739  N  N   . LYS C  1 70  ? 42.610 12.374  -23.580  1.00 7.20  ? 70   LYS D N   1 
ATOM   2740  C  CA  . LYS C  1 70  ? 43.973 11.847  -23.512  1.00 7.50  ? 70   LYS D CA  1 
ATOM   2741  C  C   . LYS C  1 70  ? 44.842 12.400  -24.644  1.00 6.09  ? 70   LYS D C   1 
ATOM   2742  O  O   . LYS C  1 70  ? 44.338 12.779  -25.684  1.00 4.45  ? 70   LYS D O   1 
ATOM   2743  C  CB  . LYS C  1 70  ? 43.963 10.314  -23.584  1.00 7.14  ? 70   LYS D CB  1 
ATOM   2744  C  CG  . LYS C  1 70  ? 43.347 9.640   -22.340  1.00 12.51 ? 70   LYS D CG  1 
ATOM   2745  C  CD  . LYS C  1 70  ? 43.509 8.117   -22.417  1.00 18.99 ? 70   LYS D CD  1 
ATOM   2746  C  CE  . LYS C  1 70  ? 42.481 7.358   -21.580  1.00 23.73 ? 70   LYS D CE  1 
ATOM   2747  N  NZ  . LYS C  1 70  ? 41.375 6.827   -22.434  1.00 25.98 ? 70   LYS D NZ  1 
ATOM   2748  N  N   . HIS C  1 71  ? 46.156 12.370  -24.442  1.00 5.84  ? 71   HIS D N   1 
ATOM   2749  C  CA  . HIS C  1 71  ? 47.143 12.778  -25.454  1.00 6.40  ? 71   HIS D CA  1 
ATOM   2750  C  C   . HIS C  1 71  ? 47.060 11.938  -26.721  1.00 6.54  ? 71   HIS D C   1 
ATOM   2751  O  O   . HIS C  1 71  ? 46.842 10.741  -26.650  1.00 6.71  ? 71   HIS D O   1 
ATOM   2752  C  CB  . HIS C  1 71  ? 48.575 12.707  -24.884  1.00 5.34  ? 71   HIS D CB  1 
ATOM   2753  C  CG  . HIS C  1 71  ? 49.617 13.159  -25.860  1.00 6.85  ? 71   HIS D CG  1 
ATOM   2754  N  ND1 . HIS C  1 71  ? 49.822 14.489  -26.147  1.00 5.90  ? 71   HIS D ND1 1 
ATOM   2755  C  CD2 . HIS C  1 71  ? 50.460 12.466  -26.666  1.00 5.16  ? 71   HIS D CD2 1 
ATOM   2756  C  CE1 . HIS C  1 71  ? 50.767 14.600  -27.065  1.00 4.34  ? 71   HIS D CE1 1 
ATOM   2757  N  NE2 . HIS C  1 71  ? 51.177 13.390  -27.392  1.00 3.28  ? 71   HIS D NE2 1 
ATOM   2758  N  N   . GLY C  1 72  ? 47.184 12.592  -27.872  1.00 5.95  ? 72   GLY D N   1 
ATOM   2759  C  CA  . GLY C  1 72  ? 47.174 11.911  -29.151  1.00 5.73  ? 72   GLY D CA  1 
ATOM   2760  C  C   . GLY C  1 72  ? 48.003 12.597  -30.193  1.00 5.89  ? 72   GLY D C   1 
ATOM   2761  O  O   . GLY C  1 72  ? 48.668 13.612  -29.923  1.00 6.29  ? 72   GLY D O   1 
ATOM   2762  N  N   . GLY C  1 73  ? 47.981 12.032  -31.400  1.00 5.70  ? 73   GLY D N   1 
ATOM   2763  C  CA  . GLY C  1 73  ? 48.545 12.701  -32.575  1.00 5.46  ? 73   GLY D CA  1 
ATOM   2764  C  C   . GLY C  1 73  ? 47.474 13.607  -33.158  1.00 6.28  ? 73   GLY D C   1 
ATOM   2765  O  O   . GLY C  1 73  ? 46.293 13.430  -32.821  1.00 5.40  ? 73   GLY D O   1 
ATOM   2766  N  N   . PRO C  1 74  ? 47.863 14.584  -34.015  1.00 6.47  ? 74   PRO D N   1 
ATOM   2767  C  CA  . PRO C  1 74  ? 46.880 15.528  -34.567  1.00 7.49  ? 74   PRO D CA  1 
ATOM   2768  C  C   . PRO C  1 74  ? 45.769 14.827  -35.370  1.00 9.14  ? 74   PRO D C   1 
ATOM   2769  O  O   . PRO C  1 74  ? 44.664 15.353  -35.447  1.00 9.18  ? 74   PRO D O   1 
ATOM   2770  C  CB  . PRO C  1 74  ? 47.711 16.449  -35.469  1.00 8.81  ? 74   PRO D CB  1 
ATOM   2771  C  CG  . PRO C  1 74  ? 49.021 15.677  -35.719  1.00 7.32  ? 74   PRO D CG  1 
ATOM   2772  C  CD  . PRO C  1 74  ? 49.240 14.905  -34.447  1.00 7.16  ? 74   PRO D CD  1 
ATOM   2773  N  N   . LYS C  1 75  ? 46.066 13.657  -35.937  1.00 9.30  ? 75   LYS D N   1 
ATOM   2774  C  CA  . LYS C  1 75  ? 45.106 12.938  -36.775  1.00 10.56 ? 75   LYS D CA  1 
ATOM   2775  C  C   . LYS C  1 75  ? 44.085 12.133  -35.949  1.00 10.29 ? 75   LYS D C   1 
ATOM   2776  O  O   . LYS C  1 75  ? 43.053 11.711  -36.489  1.00 10.75 ? 75   LYS D O   1 
ATOM   2777  C  CB  . LYS C  1 75  ? 45.826 12.000  -37.762  1.00 10.74 ? 75   LYS D CB  1 
ATOM   2778  C  CG  . LYS C  1 75  ? 46.738 12.678  -38.779  1.00 13.68 ? 75   LYS D CG  1 
ATOM   2779  C  CD  . LYS C  1 75  ? 47.017 11.765  -39.986  1.00 19.63 ? 75   LYS D CD  1 
ATOM   2780  C  CE  . LYS C  1 75  ? 47.893 10.562  -39.639  1.00 21.16 ? 75   LYS D CE  1 
ATOM   2781  N  NZ  . LYS C  1 75  ? 48.040 9.642   -40.844  1.00 21.07 ? 75   LYS D NZ  1 
ATOM   2782  N  N   . ASP C  1 76  ? 44.358 11.942  -34.655  1.00 10.06 ? 76   ASP D N   1 
ATOM   2783  C  CA  . ASP C  1 76  ? 43.475 11.164  -33.768  1.00 10.92 ? 76   ASP D CA  1 
ATOM   2784  C  C   . ASP C  1 76  ? 42.259 11.967  -33.348  1.00 11.30 ? 76   ASP D C   1 
ATOM   2785  O  O   . ASP C  1 76  ? 42.360 13.163  -33.073  1.00 10.64 ? 76   ASP D O   1 
ATOM   2786  C  CB  . ASP C  1 76  ? 44.220 10.709  -32.508  1.00 10.55 ? 76   ASP D CB  1 
ATOM   2787  C  CG  . ASP C  1 76  ? 45.299 9.686   -32.800  1.00 12.02 ? 76   ASP D CG  1 
ATOM   2788  O  OD1 . ASP C  1 76  ? 46.412 9.792   -32.223  1.00 10.90 ? 76   ASP D OD1 1 
ATOM   2789  O  OD2 . ASP C  1 76  ? 45.054 8.788   -33.640  1.00 12.99 ? 76   ASP D OD2 1 
ATOM   2790  N  N   . GLU C  1 77  ? 41.109 11.308  -33.270  1.00 11.63 ? 77   GLU D N   1 
ATOM   2791  C  CA  . GLU C  1 77  ? 39.959 11.933  -32.617  1.00 12.27 ? 77   GLU D CA  1 
ATOM   2792  C  C   . GLU C  1 77  ? 40.235 12.196  -31.126  1.00 11.12 ? 77   GLU D C   1 
ATOM   2793  O  O   . GLU C  1 77  ? 39.949 13.298  -30.590  1.00 11.52 ? 77   GLU D O   1 
ATOM   2794  C  CB  . GLU C  1 77  ? 38.696 11.079  -32.830  1.00 13.03 ? 77   GLU D CB  1 
ATOM   2795  C  CG  . GLU C  1 77  ? 38.000 11.335  -34.159  1.00 19.68 ? 77   GLU D CG  1 
ATOM   2796  C  CD  . GLU C  1 77  ? 37.135 12.606  -34.162  1.00 26.85 ? 77   GLU D CD  1 
ATOM   2797  O  OE1 . GLU C  1 77  ? 37.125 13.337  -33.142  1.00 30.10 ? 77   GLU D OE1 1 
ATOM   2798  O  OE2 . GLU C  1 77  ? 36.457 12.871  -35.185  1.00 29.03 ? 77   GLU D OE2 1 
ATOM   2799  N  N   . GLU C  1 78  ? 40.831 11.211  -30.464  1.00 9.50  ? 78   GLU D N   1 
ATOM   2800  C  CA  . GLU C  1 78  ? 41.223 11.349  -29.071  1.00 8.52  ? 78   GLU D CA  1 
ATOM   2801  C  C   . GLU C  1 78  ? 42.589 12.070  -29.020  1.00 7.67  ? 78   GLU D C   1 
ATOM   2802  O  O   . GLU C  1 78  ? 43.646 11.447  -29.194  1.00 7.40  ? 78   GLU D O   1 
ATOM   2803  C  CB  . GLU C  1 78  ? 41.299 9.980   -28.377  1.00 8.32  ? 78   GLU D CB  1 
ATOM   2804  C  CG  . GLU C  1 78  ? 41.613 10.042  -26.857  1.00 10.05 ? 78   GLU D CG  1 
ATOM   2805  C  CD  . GLU C  1 78  ? 40.420 10.474  -26.012  1.00 12.22 ? 78   GLU D CD  1 
ATOM   2806  O  OE1 . GLU C  1 78  ? 40.611 10.751  -24.806  1.00 12.52 ? 78   GLU D OE1 1 
ATOM   2807  O  OE2 . GLU C  1 78  ? 39.279 10.497  -26.536  1.00 14.45 ? 78   GLU D OE2 1 
ATOM   2808  N  N   . ARG C  1 79  ? 42.537 13.383  -28.802  1.00 7.05  ? 79   ARG D N   1 
ATOM   2809  C  CA  . ARG C  1 79  ? 43.740 14.196  -28.681  1.00 6.19  ? 79   ARG D CA  1 
ATOM   2810  C  C   . ARG C  1 79  ? 43.420 15.413  -27.817  1.00 5.95  ? 79   ARG D C   1 
ATOM   2811  O  O   . ARG C  1 79  ? 42.261 15.760  -27.622  1.00 5.25  ? 79   ARG D O   1 
ATOM   2812  C  CB  . ARG C  1 79  ? 44.246 14.641  -30.063  1.00 5.66  ? 79   ARG D CB  1 
ATOM   2813  C  CG  . ARG C  1 79  ? 43.219 15.471  -30.896  1.00 6.20  ? 79   ARG D CG  1 
ATOM   2814  C  CD  . ARG C  1 79  ? 43.819 16.086  -32.138  1.00 7.15  ? 79   ARG D CD  1 
ATOM   2815  N  NE  . ARG C  1 79  ? 44.381 17.416  -31.895  1.00 4.93  ? 79   ARG D NE  1 
ATOM   2816  C  CZ  . ARG C  1 79  ? 44.681 18.272  -32.858  1.00 5.46  ? 79   ARG D CZ  1 
ATOM   2817  N  NH1 . ARG C  1 79  ? 45.158 19.482  -32.551  1.00 4.32  ? 79   ARG D NH1 1 
ATOM   2818  N  NH2 . ARG C  1 79  ? 44.518 17.924  -34.135  1.00 3.39  ? 79   ARG D NH2 1 
ATOM   2819  N  N   . HIS C  1 80  ? 44.458 16.028  -27.270  1.00 5.01  ? 80   HIS D N   1 
ATOM   2820  C  CA  . HIS C  1 80  ? 44.336 17.361  -26.699  1.00 5.29  ? 80   HIS D CA  1 
ATOM   2821  C  C   . HIS C  1 80  ? 44.225 18.350  -27.847  1.00 4.41  ? 80   HIS D C   1 
ATOM   2822  O  O   . HIS C  1 80  ? 44.781 18.134  -28.914  1.00 4.98  ? 80   HIS D O   1 
ATOM   2823  C  CB  . HIS C  1 80  ? 45.609 17.673  -25.907  1.00 5.85  ? 80   HIS D CB  1 
ATOM   2824  C  CG  . HIS C  1 80  ? 45.884 16.713  -24.794  1.00 4.22  ? 80   HIS D CG  1 
ATOM   2825  N  ND1 . HIS C  1 80  ? 47.152 16.298  -24.463  1.00 3.70  ? 80   HIS D ND1 1 
ATOM   2826  C  CD2 . HIS C  1 80  ? 45.052 16.095  -23.921  1.00 5.10  ? 80   HIS D CD2 1 
ATOM   2827  C  CE1 . HIS C  1 80  ? 47.095 15.498  -23.414  1.00 6.46  ? 80   HIS D CE1 1 
ATOM   2828  N  NE2 . HIS C  1 80  ? 45.830 15.347  -23.075  1.00 6.19  ? 80   HIS D NE2 1 
ATOM   2829  N  N   . VAL C  1 81  ? 43.535 19.460  -27.636  1.00 4.66  ? 81   VAL D N   1 
ATOM   2830  C  CA  . VAL C  1 81  ? 43.454 20.469  -28.655  1.00 3.18  ? 81   VAL D CA  1 
ATOM   2831  C  C   . VAL C  1 81  ? 44.869 20.918  -29.004  1.00 3.56  ? 81   VAL D C   1 
ATOM   2832  O  O   . VAL C  1 81  ? 45.154 21.153  -30.175  1.00 3.32  ? 81   VAL D O   1 
ATOM   2833  C  CB  . VAL C  1 81  ? 42.595 21.673  -28.203  1.00 3.73  ? 81   VAL D CB  1 
ATOM   2834  C  CG1 . VAL C  1 81  ? 42.765 22.885  -29.159  1.00 2.38  ? 81   VAL D CG1 1 
ATOM   2835  C  CG2 . VAL C  1 81  ? 41.098 21.245  -28.085  1.00 2.00  ? 81   VAL D CG2 1 
ATOM   2836  N  N   . GLY C  1 82  ? 45.757 20.990  -28.011  1.00 3.25  ? 82   GLY D N   1 
ATOM   2837  C  CA  . GLY C  1 82  ? 47.125 21.476  -28.274  1.00 3.37  ? 82   GLY D CA  1 
ATOM   2838  C  C   . GLY C  1 82  ? 48.060 20.508  -29.020  1.00 4.75  ? 82   GLY D C   1 
ATOM   2839  O  O   . GLY C  1 82  ? 49.188 20.868  -29.351  1.00 3.67  ? 82   GLY D O   1 
ATOM   2840  N  N   . ASP C  1 83  ? 47.563 19.306  -29.345  1.00 5.22  ? 83   ASP D N   1 
ATOM   2841  C  CA  . ASP C  1 83  ? 48.413 18.215  -29.919  1.00 5.13  ? 83   ASP D CA  1 
ATOM   2842  C  C   . ASP C  1 83  ? 48.703 18.337  -31.422  1.00 5.44  ? 83   ASP D C   1 
ATOM   2843  O  O   . ASP C  1 83  ? 47.928 17.840  -32.282  1.00 5.05  ? 83   ASP D O   1 
ATOM   2844  C  CB  . ASP C  1 83  ? 47.774 16.830  -29.641  1.00 5.65  ? 83   ASP D CB  1 
ATOM   2845  C  CG  . ASP C  1 83  ? 47.843 16.426  -28.189  1.00 5.65  ? 83   ASP D CG  1 
ATOM   2846  O  OD1 . ASP C  1 83  ? 48.591 17.077  -27.426  1.00 5.32  ? 83   ASP D OD1 1 
ATOM   2847  O  OD2 . ASP C  1 83  ? 47.136 15.450  -27.783  1.00 2.00  ? 83   ASP D OD2 1 
ATOM   2848  N  N   . LEU C  1 84  ? 49.823 18.987  -31.755  1.00 5.20  ? 84   LEU D N   1 
ATOM   2849  C  CA  . LEU C  1 84  ? 50.181 19.186  -33.142  1.00 5.36  ? 84   LEU D CA  1 
ATOM   2850  C  C   . LEU C  1 84  ? 51.208 18.152  -33.624  1.00 4.83  ? 84   LEU D C   1 
ATOM   2851  O  O   . LEU C  1 84  ? 51.703 18.247  -34.746  1.00 5.94  ? 84   LEU D O   1 
ATOM   2852  C  CB  . LEU C  1 84  ? 50.673 20.599  -33.354  1.00 4.45  ? 84   LEU D CB  1 
ATOM   2853  C  CG  . LEU C  1 84  ? 49.656 21.723  -33.052  1.00 6.57  ? 84   LEU D CG  1 
ATOM   2854  C  CD1 . LEU C  1 84  ? 50.355 23.013  -33.342  1.00 5.84  ? 84   LEU D CD1 1 
ATOM   2855  C  CD2 . LEU C  1 84  ? 48.375 21.604  -33.905  1.00 6.42  ? 84   LEU D CD2 1 
ATOM   2856  N  N   . GLY C  1 85  ? 51.515 17.168  -32.778  1.00 4.70  ? 85   GLY D N   1 
ATOM   2857  C  CA  . GLY C  1 85  ? 52.387 16.051  -33.192  1.00 4.52  ? 85   GLY D CA  1 
ATOM   2858  C  C   . GLY C  1 85  ? 53.863 16.422  -33.173  1.00 4.48  ? 85   GLY D C   1 
ATOM   2859  O  O   . GLY C  1 85  ? 54.354 17.042  -32.215  1.00 3.86  ? 85   GLY D O   1 
ATOM   2860  N  N   . ASN C  1 86  ? 54.562 16.049  -34.242  1.00 3.95  ? 86   ASN D N   1 
ATOM   2861  C  CA  . ASN C  1 86  ? 55.996 16.345  -34.344  1.00 3.43  ? 86   ASN D CA  1 
ATOM   2862  C  C   . ASN C  1 86  ? 56.333 17.333  -35.426  1.00 3.08  ? 86   ASN D C   1 
ATOM   2863  O  O   . ASN C  1 86  ? 55.597 17.469  -36.402  1.00 2.31  ? 86   ASN D O   1 
ATOM   2864  C  CB  . ASN C  1 86  ? 56.797 15.067  -34.574  1.00 3.18  ? 86   ASN D CB  1 
ATOM   2865  C  CG  . ASN C  1 86  ? 56.806 14.169  -33.356  1.00 3.35  ? 86   ASN D CG  1 
ATOM   2866  O  OD1 . ASN C  1 86  ? 57.313 14.544  -32.308  1.00 2.03  ? 86   ASN D OD1 1 
ATOM   2867  N  ND2 . ASN C  1 86  ? 56.220 12.977  -33.489  1.00 4.64  ? 86   ASN D ND2 1 
ATOM   2868  N  N   . VAL C  1 87  ? 57.489 17.989  -35.269  1.00 3.66  ? 87   VAL D N   1 
ATOM   2869  C  CA  . VAL C  1 87  ? 58.129 18.684  -36.359  1.00 3.47  ? 87   VAL D CA  1 
ATOM   2870  C  C   . VAL C  1 87  ? 59.465 17.988  -36.574  1.00 3.71  ? 87   VAL D C   1 
ATOM   2871  O  O   . VAL C  1 87  ? 59.949 17.315  -35.678  1.00 4.01  ? 87   VAL D O   1 
ATOM   2872  C  CB  . VAL C  1 87  ? 58.303 20.211  -36.100  1.00 4.32  ? 87   VAL D CB  1 
ATOM   2873  C  CG1 . VAL C  1 87  ? 56.903 20.861  -35.889  1.00 4.89  ? 87   VAL D CG1 1 
ATOM   2874  C  CG2 . VAL C  1 87  ? 59.219 20.472  -34.903  1.00 3.65  ? 87   VAL D CG2 1 
ATOM   2875  N  N   . THR C  1 88  ? 60.049 18.159  -37.749  1.00 2.42  ? 88   THR D N   1 
ATOM   2876  C  CA  . THR C  1 88  ? 61.259 17.422  -38.108  1.00 3.28  ? 88   THR D CA  1 
ATOM   2877  C  C   . THR C  1 88  ? 62.373 18.394  -38.417  1.00 2.78  ? 88   THR D C   1 
ATOM   2878  O  O   . THR C  1 88  ? 62.232 19.253  -39.297  1.00 3.82  ? 88   THR D O   1 
ATOM   2879  C  CB  . THR C  1 88  ? 61.028 16.485  -39.335  1.00 3.48  ? 88   THR D CB  1 
ATOM   2880  O  OG1 . THR C  1 88  ? 60.023 15.522  -39.016  1.00 5.39  ? 88   THR D OG1 1 
ATOM   2881  C  CG2 . THR C  1 88  ? 62.333 15.766  -39.753  1.00 4.08  ? 88   THR D CG2 1 
ATOM   2882  N  N   . ALA C  1 89  ? 63.472 18.285  -37.672  1.00 2.00  ? 89   ALA D N   1 
ATOM   2883  C  CA  . ALA C  1 89  ? 64.674 19.065  -38.006  1.00 2.00  ? 89   ALA D CA  1 
ATOM   2884  C  C   . ALA C  1 89  ? 65.565 18.278  -38.966  1.00 2.73  ? 89   ALA D C   1 
ATOM   2885  O  O   . ALA C  1 89  ? 65.749 17.064  -38.790  1.00 3.05  ? 89   ALA D O   1 
ATOM   2886  C  CB  . ALA C  1 89  ? 65.433 19.427  -36.746  1.00 2.00  ? 89   ALA D CB  1 
ATOM   2887  N  N   . ASP C  1 90  ? 66.053 18.978  -39.994  1.00 3.35  ? 90   ASP D N   1 
ATOM   2888  C  CA  . ASP C  1 90  ? 66.915 18.414  -41.044  1.00 3.79  ? 90   ASP D CA  1 
ATOM   2889  C  C   . ASP C  1 90  ? 68.373 18.299  -40.570  1.00 4.73  ? 90   ASP D C   1 
ATOM   2890  O  O   . ASP C  1 90  ? 68.679 18.541  -39.404  1.00 3.47  ? 90   ASP D O   1 
ATOM   2891  C  CB  . ASP C  1 90  ? 66.790 19.250  -42.344  1.00 4.27  ? 90   ASP D CB  1 
ATOM   2892  C  CG  . ASP C  1 90  ? 67.320 20.695  -42.210  1.00 4.28  ? 90   ASP D CG  1 
ATOM   2893  O  OD1 . ASP C  1 90  ? 66.982 21.542  -43.083  1.00 6.19  ? 90   ASP D OD1 1 
ATOM   2894  O  OD2 . ASP C  1 90  ? 68.057 20.992  -41.258  1.00 3.68  ? 90   ASP D OD2 1 
ATOM   2895  N  N   . LYS C  1 91  ? 69.266 17.954  -41.489  1.00 5.26  ? 91   LYS D N   1 
ATOM   2896  C  CA  . LYS C  1 91  ? 70.666 17.691  -41.137  1.00 6.12  ? 91   LYS D CA  1 
ATOM   2897  C  C   . LYS C  1 91  ? 71.430 18.939  -40.708  1.00 5.58  ? 91   LYS D C   1 
ATOM   2898  O  O   . LYS C  1 91  ? 72.563 18.823  -40.264  1.00 5.95  ? 91   LYS D O   1 
ATOM   2899  C  CB  . LYS C  1 91  ? 71.388 17.044  -42.339  1.00 6.85  ? 91   LYS D CB  1 
ATOM   2900  C  CG  . LYS C  1 91  ? 71.449 17.926  -43.580  1.00 11.16 ? 91   LYS D CG  1 
ATOM   2901  C  CD  . LYS C  1 91  ? 72.208 17.218  -44.686  1.00 16.41 ? 91   LYS D CD  1 
ATOM   2902  C  CE  . LYS C  1 91  ? 72.486 18.132  -45.860  1.00 19.49 ? 91   LYS D CE  1 
ATOM   2903  N  NZ  . LYS C  1 91  ? 73.511 19.182  -45.544  1.00 23.62 ? 91   LYS D NZ  1 
ATOM   2904  N  N   . ASP C  1 92  ? 70.828 20.111  -40.908  1.00 5.09  ? 92   ASP D N   1 
ATOM   2905  C  CA  . ASP C  1 92  ? 71.359 21.399  -40.420  1.00 5.41  ? 92   ASP D CA  1 
ATOM   2906  C  C   . ASP C  1 92  ? 70.770 21.797  -39.050  1.00 4.86  ? 92   ASP D C   1 
ATOM   2907  O  O   . ASP C  1 92  ? 71.168 22.808  -38.450  1.00 4.81  ? 92   ASP D O   1 
ATOM   2908  C  CB  . ASP C  1 92  ? 71.076 22.498  -41.443  1.00 6.53  ? 92   ASP D CB  1 
ATOM   2909  C  CG  . ASP C  1 92  ? 71.814 22.282  -42.758  1.00 9.32  ? 92   ASP D CG  1 
ATOM   2910  O  OD1 . ASP C  1 92  ? 72.936 21.734  -42.743  1.00 9.86  ? 92   ASP D OD1 1 
ATOM   2911  O  OD2 . ASP C  1 92  ? 71.259 22.688  -43.799  1.00 12.62 ? 92   ASP D OD2 1 
ATOM   2912  N  N   . GLY C  1 93  ? 69.814 21.022  -38.561  1.00 2.68  ? 93   GLY D N   1 
ATOM   2913  C  CA  . GLY C  1 93  ? 69.194 21.348  -37.263  1.00 3.17  ? 93   GLY D CA  1 
ATOM   2914  C  C   . GLY C  1 93  ? 68.019 22.296  -37.369  1.00 2.14  ? 93   GLY D C   1 
ATOM   2915  O  O   . GLY C  1 93  ? 67.588 22.908  -36.369  1.00 2.77  ? 93   GLY D O   1 
ATOM   2916  N  N   . VAL C  1 94  ? 67.515 22.436  -38.584  1.00 2.69  ? 94   VAL D N   1 
ATOM   2917  C  CA  . VAL C  1 94  ? 66.396 23.308  -38.875  1.00 2.73  ? 94   VAL D CA  1 
ATOM   2918  C  C   . VAL C  1 94  ? 65.098 22.551  -39.141  1.00 2.99  ? 94   VAL D C   1 
ATOM   2919  O  O   . VAL C  1 94  ? 65.030 21.708  -40.046  1.00 2.50  ? 94   VAL D O   1 
ATOM   2920  C  CB  . VAL C  1 94  ? 66.720 24.207  -40.101  1.00 2.74  ? 94   VAL D CB  1 
ATOM   2921  C  CG1 . VAL C  1 94  ? 65.572 25.155  -40.402  1.00 5.60  ? 94   VAL D CG1 1 
ATOM   2922  C  CG2 . VAL C  1 94  ? 68.014 25.028  -39.833  1.00 3.97  ? 94   VAL D CG2 1 
ATOM   2923  N  N   . ALA C  1 95  ? 64.060 22.928  -38.404  1.00 3.35  ? 95   ALA D N   1 
ATOM   2924  C  CA  . ALA C  1 95  ? 62.712 22.442  -38.666  1.00 3.95  ? 95   ALA D CA  1 
ATOM   2925  C  C   . ALA C  1 95  ? 61.945 23.489  -39.462  1.00 3.95  ? 95   ALA D C   1 
ATOM   2926  O  O   . ALA C  1 95  ? 61.626 24.583  -38.944  1.00 5.03  ? 95   ALA D O   1 
ATOM   2927  C  CB  . ALA C  1 95  ? 62.016 22.113  -37.352  1.00 3.32  ? 95   ALA D CB  1 
ATOM   2928  N  N   . ASP C  1 96  ? 61.689 23.172  -40.732  1.00 4.16  ? 96   ASP D N   1 
ATOM   2929  C  CA  . ASP C  1 96  ? 60.844 24.034  -41.572  1.00 5.61  ? 96   ASP D CA  1 
ATOM   2930  C  C   . ASP C  1 96  ? 59.393 23.557  -41.420  1.00 6.07  ? 96   ASP D C   1 
ATOM   2931  O  O   . ASP C  1 96  ? 58.938 22.613  -42.088  1.00 6.09  ? 96   ASP D O   1 
ATOM   2932  C  CB  . ASP C  1 96  ? 61.323 24.018  -43.032  1.00 6.60  ? 96   ASP D CB  1 
ATOM   2933  C  CG  . ASP C  1 96  ? 62.676 24.712  -43.221  1.00 11.66 ? 96   ASP D CG  1 
ATOM   2934  O  OD1 . ASP C  1 96  ? 62.963 25.719  -42.516  1.00 14.57 ? 96   ASP D OD1 1 
ATOM   2935  O  OD2 . ASP C  1 96  ? 63.451 24.259  -44.095  1.00 17.01 ? 96   ASP D OD2 1 
ATOM   2936  N  N   . VAL C  1 97  ? 58.690 24.160  -40.466  1.00 5.19  ? 97   VAL D N   1 
ATOM   2937  C  CA  . VAL C  1 97  ? 57.388 23.643  -40.041  1.00 4.00  ? 97   VAL D CA  1 
ATOM   2938  C  C   . VAL C  1 97  ? 56.353 23.936  -41.113  1.00 4.67  ? 97   VAL D C   1 
ATOM   2939  O  O   . VAL C  1 97  ? 56.259 25.057  -41.605  1.00 3.57  ? 97   VAL D O   1 
ATOM   2940  C  CB  . VAL C  1 97  ? 56.952 24.254  -38.697  1.00 3.59  ? 97   VAL D CB  1 
ATOM   2941  C  CG1 . VAL C  1 97  ? 55.525 23.783  -38.295  1.00 2.10  ? 97   VAL D CG1 1 
ATOM   2942  C  CG2 . VAL C  1 97  ? 58.002 23.951  -37.599  1.00 4.08  ? 97   VAL D CG2 1 
ATOM   2943  N  N   . SER C  1 98  ? 55.570 22.918  -41.470  1.00 5.27  ? 98   SER D N   1 
ATOM   2944  C  CA  . SER C  1 98  ? 54.461 23.100  -42.388  1.00 6.54  ? 98   SER D CA  1 
ATOM   2945  C  C   . SER C  1 98  ? 53.346 22.184  -41.906  1.00 7.58  ? 98   SER D C   1 
ATOM   2946  O  O   . SER C  1 98  ? 53.412 20.972  -42.118  1.00 6.69  ? 98   SER D O   1 
ATOM   2947  C  CB  . SER C  1 98  ? 54.889 22.729  -43.825  1.00 6.52  ? 98   SER D CB  1 
ATOM   2948  O  OG  . SER C  1 98  ? 53.882 23.073  -44.766  1.00 9.89  ? 98   SER D OG  1 
ATOM   2949  N  N   . ILE C  1 99  ? 52.346 22.760  -41.236  1.00 6.51  ? 99   ILE D N   1 
ATOM   2950  C  CA  . ILE C  1 99  ? 51.294 21.999  -40.581  1.00 7.38  ? 99   ILE D CA  1 
ATOM   2951  C  C   . ILE C  1 99  ? 49.986 22.726  -40.896  1.00 8.08  ? 99   ILE D C   1 
ATOM   2952  O  O   . ILE C  1 99  ? 49.953 23.961  -41.023  1.00 7.49  ? 99   ILE D O   1 
ATOM   2953  C  CB  . ILE C  1 99  ? 51.513 21.864  -39.022  1.00 7.31  ? 99   ILE D CB  1 
ATOM   2954  C  CG1 . ILE C  1 99  ? 52.588 20.808  -38.701  1.00 7.18  ? 99   ILE D CG1 1 
ATOM   2955  C  CG2 . ILE C  1 99  ? 50.238 21.397  -38.243  1.00 7.33  ? 99   ILE D CG2 1 
ATOM   2956  C  CD1 . ILE C  1 99  ? 52.998 20.779  -37.192  1.00 9.00  ? 99   ILE D CD1 1 
ATOM   2957  N  N   . GLU C  1 100 ? 48.936 21.943  -41.081  1.00 8.82  ? 100  GLU D N   1 
ATOM   2958  C  CA  . GLU C  1 100 ? 47.590 22.471  -41.149  1.00 9.50  ? 100  GLU D CA  1 
ATOM   2959  C  C   . GLU C  1 100 ? 46.751 21.647  -40.174  1.00 8.67  ? 100  GLU D C   1 
ATOM   2960  O  O   . GLU C  1 100 ? 46.837 20.412  -40.132  1.00 8.66  ? 100  GLU D O   1 
ATOM   2961  C  CB  . GLU C  1 100 ? 47.025 22.412  -42.577  1.00 10.62 ? 100  GLU D CB  1 
ATOM   2962  C  CG  . GLU C  1 100 ? 45.646 23.105  -42.684  1.00 14.35 ? 100  GLU D CG  1 
ATOM   2963  C  CD  . GLU C  1 100 ? 45.217 23.467  -44.122  1.00 19.99 ? 100  GLU D CD  1 
ATOM   2964  O  OE1 . GLU C  1 100 ? 45.779 22.934  -45.094  1.00 21.98 ? 100  GLU D OE1 1 
ATOM   2965  O  OE2 . GLU C  1 100 ? 44.307 24.309  -44.276  1.00 23.40 ? 100  GLU D OE2 1 
ATOM   2966  N  N   . ASP C  1 101 ? 45.964 22.338  -39.364  1.00 7.76  ? 101  ASP D N   1 
ATOM   2967  C  CA  . ASP C  1 101 ? 45.259 21.676  -38.278  1.00 7.86  ? 101  ASP D CA  1 
ATOM   2968  C  C   . ASP C  1 101 ? 43.893 22.298  -38.098  1.00 8.38  ? 101  ASP D C   1 
ATOM   2969  O  O   . ASP C  1 101 ? 43.747 23.513  -38.133  1.00 7.95  ? 101  ASP D O   1 
ATOM   2970  C  CB  . ASP C  1 101 ? 46.044 21.745  -36.960  1.00 6.73  ? 101  ASP D CB  1 
ATOM   2971  C  CG  . ASP C  1 101 ? 45.457 20.831  -35.869  1.00 7.44  ? 101  ASP D CG  1 
ATOM   2972  O  OD1 . ASP C  1 101 ? 44.688 21.319  -35.008  1.00 6.10  ? 101  ASP D OD1 1 
ATOM   2973  O  OD2 . ASP C  1 101 ? 45.758 19.616  -35.878  1.00 9.64  ? 101  ASP D OD2 1 
ATOM   2974  N  N   . SER C  1 102 ? 42.898 21.442  -37.912  1.00 8.43  ? 102  SER D N   1 
ATOM   2975  C  CA  . SER C  1 102 ? 41.509 21.873  -37.822  1.00 9.77  ? 102  SER D CA  1 
ATOM   2976  C  C   . SER C  1 102 ? 40.946 21.871  -36.400  1.00 8.61  ? 102  SER D C   1 
ATOM   2977  O  O   . SER C  1 102 ? 39.779 22.246  -36.188  1.00 9.78  ? 102  SER D O   1 
ATOM   2978  C  CB  . SER C  1 102 ? 40.639 21.002  -38.736  1.00 10.48 ? 102  SER D CB  1 
ATOM   2979  O  OG  . SER C  1 102 ? 40.890 21.329  -40.088  1.00 14.72 ? 102  SER D OG  1 
ATOM   2980  N  N   . VAL C  1 103 ? 41.750 21.459  -35.418  1.00 7.87  ? 103  VAL D N   1 
ATOM   2981  C  CA  . VAL C  1 103 ? 41.287 21.362  -34.031  1.00 7.11  ? 103  VAL D CA  1 
ATOM   2982  C  C   . VAL C  1 103 ? 41.692 22.616  -33.234  1.00 6.94  ? 103  VAL D C   1 
ATOM   2983  O  O   . VAL C  1 103 ? 40.903 23.146  -32.463  1.00 6.43  ? 103  VAL D O   1 
ATOM   2984  C  CB  . VAL C  1 103 ? 41.766 20.041  -33.341  1.00 7.11  ? 103  VAL D CB  1 
ATOM   2985  C  CG1 . VAL C  1 103 ? 41.498 20.032  -31.817  1.00 7.59  ? 103  VAL D CG1 1 
ATOM   2986  C  CG2 . VAL C  1 103 ? 41.117 18.799  -34.027  1.00 9.31  ? 103  VAL D CG2 1 
ATOM   2987  N  N   . ILE C  1 104 ? 42.931 23.083  -33.404  1.00 5.72  ? 104  ILE D N   1 
ATOM   2988  C  CA  . ILE C  1 104 ? 43.300 24.395  -32.870  1.00 5.73  ? 104  ILE D CA  1 
ATOM   2989  C  C   . ILE C  1 104 ? 42.502 25.474  -33.607  1.00 5.43  ? 104  ILE D C   1 
ATOM   2990  O  O   . ILE C  1 104 ? 42.013 25.264  -34.725  1.00 5.50  ? 104  ILE D O   1 
ATOM   2991  C  CB  . ILE C  1 104 ? 44.840 24.707  -32.972  1.00 4.50  ? 104  ILE D CB  1 
ATOM   2992  C  CG1 . ILE C  1 104 ? 45.312 24.664  -34.443  1.00 4.03  ? 104  ILE D CG1 1 
ATOM   2993  C  CG2 . ILE C  1 104 ? 45.622 23.741  -32.098  1.00 6.01  ? 104  ILE D CG2 1 
ATOM   2994  C  CD1 . ILE C  1 104 ? 46.716 25.171  -34.714  1.00 2.00  ? 104  ILE D CD1 1 
ATOM   2995  N  N   . SER C  1 105 ? 42.377 26.634  -32.985  1.00 5.18  ? 105  SER D N   1 
ATOM   2996  C  CA  . SER C  1 105 ? 41.688 27.744  -33.623  1.00 5.14  ? 105  SER D CA  1 
ATOM   2997  C  C   . SER C  1 105 ? 42.309 29.061  -33.160  1.00 5.77  ? 105  SER D C   1 
ATOM   2998  O  O   . SER C  1 105 ? 43.070 29.089  -32.173  1.00 5.19  ? 105  SER D O   1 
ATOM   2999  C  CB  . SER C  1 105 ? 40.194 27.704  -33.277  1.00 4.68  ? 105  SER D CB  1 
ATOM   3000  O  OG  . SER C  1 105 ? 39.517 28.709  -33.998  1.00 6.01  ? 105  SER D OG  1 
ATOM   3001  N  N   . LEU C  1 106 ? 41.995 30.133  -33.878  1.00 6.29  ? 106  LEU D N   1 
ATOM   3002  C  CA  . LEU C  1 106 ? 42.440 31.472  -33.503  1.00 6.91  ? 106  LEU D CA  1 
ATOM   3003  C  C   . LEU C  1 106 ? 41.307 32.334  -32.937  1.00 8.34  ? 106  LEU D C   1 
ATOM   3004  O  O   . LEU C  1 106 ? 41.473 33.533  -32.731  1.00 7.70  ? 106  LEU D O   1 
ATOM   3005  C  CB  . LEU C  1 106 ? 43.136 32.178  -34.673  1.00 7.20  ? 106  LEU D CB  1 
ATOM   3006  C  CG  . LEU C  1 106 ? 44.405 31.524  -35.224  1.00 6.58  ? 106  LEU D CG  1 
ATOM   3007  C  CD1 . LEU C  1 106 ? 45.086 32.472  -36.179  1.00 8.01  ? 106  LEU D CD1 1 
ATOM   3008  C  CD2 . LEU C  1 106 ? 45.359 31.106  -34.097  1.00 5.49  ? 106  LEU D CD2 1 
ATOM   3009  N  N   . SER C  1 107 ? 40.164 31.713  -32.673  1.00 9.54  ? 107  SER D N   1 
ATOM   3010  C  CA  . SER C  1 107 ? 39.129 32.330  -31.843  1.00 11.10 ? 107  SER D CA  1 
ATOM   3011  C  C   . SER C  1 107 ? 38.318 31.240  -31.161  1.00 11.54 ? 107  SER D C   1 
ATOM   3012  O  O   . SER C  1 107 ? 38.476 30.047  -31.463  1.00 11.07 ? 107  SER D O   1 
ATOM   3013  C  CB  . SER C  1 107 ? 38.218 33.265  -32.659  1.00 11.57 ? 107  SER D CB  1 
ATOM   3014  O  OG  . SER C  1 107 ? 37.510 32.561  -33.660  1.00 13.48 ? 107  SER D OG  1 
ATOM   3015  N  N   . GLY C  1 108 ? 37.470 31.652  -30.221  1.00 11.71 ? 108  GLY D N   1 
ATOM   3016  C  CA  . GLY C  1 108 ? 36.501 30.739  -29.618  1.00 12.22 ? 108  GLY D CA  1 
ATOM   3017  C  C   . GLY C  1 108 ? 37.143 29.819  -28.602  1.00 12.53 ? 108  GLY D C   1 
ATOM   3018  O  O   . GLY C  1 108 ? 38.265 30.069  -28.140  1.00 13.22 ? 108  GLY D O   1 
ATOM   3019  N  N   . ASP C  1 109 ? 36.431 28.741  -28.283  1.00 12.15 ? 109  ASP D N   1 
ATOM   3020  C  CA  . ASP C  1 109 ? 36.774 27.812  -27.203  1.00 12.18 ? 109  ASP D CA  1 
ATOM   3021  C  C   . ASP C  1 109 ? 38.145 27.166  -27.354  1.00 10.69 ? 109  ASP D C   1 
ATOM   3022  O  O   . ASP C  1 109 ? 38.803 26.844  -26.375  1.00 10.16 ? 109  ASP D O   1 
ATOM   3023  C  CB  . ASP C  1 109 ? 35.757 26.663  -27.175  1.00 13.53 ? 109  ASP D CB  1 
ATOM   3024  C  CG  . ASP C  1 109 ? 34.494 27.029  -26.463  1.00 17.35 ? 109  ASP D CG  1 
ATOM   3025  O  OD1 . ASP C  1 109 ? 33.622 26.157  -26.378  1.00 20.01 ? 109  ASP D OD1 1 
ATOM   3026  O  OD2 . ASP C  1 109 ? 34.393 28.180  -25.974  1.00 23.90 ? 109  ASP D OD2 1 
ATOM   3027  N  N   . HIS C  1 110 ? 38.547 26.951  -28.592  1.00 10.22 ? 110  HIS D N   1 
ATOM   3028  C  CA  . HIS C  1 110 ? 39.800 26.260  -28.852  1.00 9.07  ? 110  HIS D CA  1 
ATOM   3029  C  C   . HIS C  1 110 ? 40.885 27.268  -29.238  1.00 8.53  ? 110  HIS D C   1 
ATOM   3030  O  O   . HIS C  1 110 ? 41.874 26.904  -29.871  1.00 6.02  ? 110  HIS D O   1 
ATOM   3031  C  CB  . HIS C  1 110 ? 39.592 25.268  -29.992  1.00 10.66 ? 110  HIS D CB  1 
ATOM   3032  C  CG  . HIS C  1 110 ? 38.703 24.110  -29.642  1.00 11.70 ? 110  HIS D CG  1 
ATOM   3033  N  ND1 . HIS C  1 110 ? 38.497 23.051  -30.505  1.00 14.98 ? 110  HIS D ND1 1 
ATOM   3034  C  CD2 . HIS C  1 110 ? 37.982 23.832  -28.527  1.00 13.85 ? 110  HIS D CD2 1 
ATOM   3035  C  CE1 . HIS C  1 110 ? 37.665 22.188  -29.946  1.00 13.60 ? 110  HIS D CE1 1 
ATOM   3036  N  NE2 . HIS C  1 110 ? 37.341 22.635  -28.748  1.00 14.18 ? 110  HIS D NE2 1 
HETATM 3037  N  N   . CME C  1 111 ? 40.664 28.546  -28.924  1.00 7.19  ? 111  CME D N   1 
HETATM 3038  C  CA  . CME C  1 111 ? 41.629 29.583  -29.305  1.00 6.75  ? 111  CME D CA  1 
HETATM 3039  C  CB  . CME C  1 111 ? 41.078 30.965  -28.925  1.00 7.40  ? 111  CME D CB  1 
HETATM 3040  S  SG  . CME C  1 111 ? 42.184 32.164  -29.598  1.00 8.33  ? 111  CME D SG  1 
HETATM 3041  S  SD  . CME C  1 111 ? 41.323 33.874  -28.974  1.00 16.56 ? 111  CME D SD  1 
HETATM 3042  C  CE  . CME C  1 111 ? 42.228 34.300  -27.505  1.00 16.75 ? 111  CME D CE  1 
HETATM 3043  C  CZ  . CME C  1 111 ? 41.643 33.613  -26.278  1.00 18.54 ? 111  CME D CZ  1 
HETATM 3044  O  OH  . CME C  1 111 ? 42.366 32.411  -25.949  1.00 20.61 ? 111  CME D OH  1 
HETATM 3045  C  C   . CME C  1 111 ? 42.978 29.338  -28.644  1.00 5.88  ? 111  CME D C   1 
HETATM 3046  O  O   . CME C  1 111 ? 43.029 29.035  -27.455  1.00 5.94  ? 111  CME D O   1 
ATOM   3047  N  N   . ILE C  1 112 ? 44.064 29.434  -29.410  1.00 5.46  ? 112  ILE D N   1 
ATOM   3048  C  CA  . ILE C  1 112 ? 45.421 29.208  -28.870  1.00 4.77  ? 112  ILE D CA  1 
ATOM   3049  C  C   . ILE C  1 112 ? 46.195 30.515  -28.641  1.00 4.36  ? 112  ILE D C   1 
ATOM   3050  O  O   . ILE C  1 112 ? 47.308 30.511  -28.114  1.00 4.05  ? 112  ILE D O   1 
ATOM   3051  C  CB  . ILE C  1 112 ? 46.248 28.245  -29.759  1.00 5.21  ? 112  ILE D CB  1 
ATOM   3052  C  CG1 . ILE C  1 112 ? 46.346 28.787  -31.196  1.00 4.69  ? 112  ILE D CG1 1 
ATOM   3053  C  CG2 . ILE C  1 112 ? 45.627 26.841  -29.760  1.00 4.92  ? 112  ILE D CG2 1 
ATOM   3054  C  CD1 . ILE C  1 112 ? 47.322 27.976  -32.047  1.00 2.00  ? 112  ILE D CD1 1 
ATOM   3055  N  N   . ILE C  1 113 ? 45.600 31.631  -29.042  1.00 3.86  ? 113  ILE D N   1 
ATOM   3056  C  CA  . ILE C  1 113 ? 46.220 32.930  -28.783  1.00 3.65  ? 113  ILE D CA  1 
ATOM   3057  C  C   . ILE C  1 113 ? 46.232 33.169  -27.264  1.00 3.43  ? 113  ILE D C   1 
ATOM   3058  O  O   . ILE C  1 113 ? 45.214 32.938  -26.571  1.00 2.89  ? 113  ILE D O   1 
ATOM   3059  C  CB  . ILE C  1 113 ? 45.459 34.037  -29.549  1.00 3.71  ? 113  ILE D CB  1 
ATOM   3060  C  CG1 . ILE C  1 113 ? 45.675 33.860  -31.072  1.00 4.73  ? 113  ILE D CG1 1 
ATOM   3061  C  CG2 . ILE C  1 113 ? 45.900 35.463  -29.101  1.00 2.27  ? 113  ILE D CG2 1 
ATOM   3062  C  CD1 . ILE C  1 113 ? 44.829 34.816  -31.920  1.00 5.59  ? 113  ILE D CD1 1 
ATOM   3063  N  N   . GLY C  1 114 ? 47.361 33.657  -26.734  1.00 2.09  ? 114  GLY D N   1 
ATOM   3064  C  CA  . GLY C  1 114 ? 47.489 33.817  -25.295  1.00 2.00  ? 114  GLY D CA  1 
ATOM   3065  C  C   . GLY C  1 114 ? 47.974 32.569  -24.570  1.00 2.00  ? 114  GLY D C   1 
ATOM   3066  O  O   . GLY C  1 114 ? 48.124 32.578  -23.363  1.00 2.00  ? 114  GLY D O   1 
ATOM   3067  N  N   . ARG C  1 115 ? 48.185 31.490  -25.321  1.00 2.00  ? 115  ARG D N   1 
ATOM   3068  C  CA  . ARG C  1 115 ? 48.729 30.251  -24.766  1.00 2.00  ? 115  ARG D CA  1 
ATOM   3069  C  C   . ARG C  1 115 ? 50.179 30.064  -25.234  1.00 2.11  ? 115  ARG D C   1 
ATOM   3070  O  O   . ARG C  1 115 ? 50.703 30.918  -25.958  1.00 3.68  ? 115  ARG D O   1 
ATOM   3071  C  CB  . ARG C  1 115 ? 47.816 29.068  -25.124  1.00 2.00  ? 115  ARG D CB  1 
ATOM   3072  C  CG  . ARG C  1 115 ? 46.347 29.370  -24.623  1.00 2.00  ? 115  ARG D CG  1 
ATOM   3073  C  CD  . ARG C  1 115 ? 45.420 28.171  -24.732  1.00 3.77  ? 115  ARG D CD  1 
ATOM   3074  N  NE  . ARG C  1 115 ? 44.042 28.599  -24.424  1.00 4.83  ? 115  ARG D NE  1 
ATOM   3075  C  CZ  . ARG C  1 115 ? 43.499 28.622  -23.204  1.00 2.88  ? 115  ARG D CZ  1 
ATOM   3076  N  NH1 . ARG C  1 115 ? 42.236 29.007  -23.062  1.00 4.23  ? 115  ARG D NH1 1 
ATOM   3077  N  NH2 . ARG C  1 115 ? 44.171 28.222  -22.120  1.00 2.71  ? 115  ARG D NH2 1 
ATOM   3078  N  N   . THR C  1 116 ? 50.845 29.004  -24.784  1.00 2.89  ? 116  THR D N   1 
ATOM   3079  C  CA  . THR C  1 116 ? 52.267 28.827  -25.107  1.00 2.20  ? 116  THR D CA  1 
ATOM   3080  C  C   . THR C  1 116 ? 52.523 27.714  -26.120  1.00 2.78  ? 116  THR D C   1 
ATOM   3081  O  O   . THR C  1 116 ? 52.045 26.597  -25.935  1.00 2.67  ? 116  THR D O   1 
ATOM   3082  C  CB  . THR C  1 116 ? 53.078 28.527  -23.845  1.00 3.80  ? 116  THR D CB  1 
ATOM   3083  O  OG1 . THR C  1 116 ? 52.984 29.634  -22.932  1.00 2.00  ? 116  THR D OG1 1 
ATOM   3084  C  CG2 . THR C  1 116 ? 54.551 28.302  -24.194  1.00 2.00  ? 116  THR D CG2 1 
ATOM   3085  N  N   . LEU C  1 117 ? 53.290 28.023  -27.171  1.00 2.00  ? 117  LEU D N   1 
ATOM   3086  C  CA  . LEU C  1 117 ? 53.756 26.997  -28.101  1.00 2.00  ? 117  LEU D CA  1 
ATOM   3087  C  C   . LEU C  1 117 ? 55.076 26.429  -27.587  1.00 2.00  ? 117  LEU D C   1 
ATOM   3088  O  O   . LEU C  1 117 ? 55.946 27.188  -27.207  1.00 2.00  ? 117  LEU D O   1 
ATOM   3089  C  CB  . LEU C  1 117 ? 53.970 27.620  -29.492  1.00 2.00  ? 117  LEU D CB  1 
ATOM   3090  C  CG  . LEU C  1 117 ? 54.376 26.678  -30.604  1.00 2.00  ? 117  LEU D CG  1 
ATOM   3091  C  CD1 . LEU C  1 117 ? 53.248 25.632  -30.846  1.00 2.00  ? 117  LEU D CD1 1 
ATOM   3092  C  CD2 . LEU C  1 117 ? 54.657 27.491  -31.874  1.00 2.00  ? 117  LEU D CD2 1 
ATOM   3093  N  N   . VAL C  1 118 ? 55.232 25.103  -27.568  1.00 2.00  ? 118  VAL D N   1 
ATOM   3094  C  CA  . VAL C  1 118 ? 56.445 24.498  -26.995  1.00 2.00  ? 118  VAL D CA  1 
ATOM   3095  C  C   . VAL C  1 118 ? 57.031 23.521  -28.012  1.00 2.00  ? 118  VAL D C   1 
ATOM   3096  O  O   . VAL C  1 118 ? 56.294 22.740  -28.614  1.00 2.00  ? 118  VAL D O   1 
ATOM   3097  C  CB  . VAL C  1 118 ? 56.146 23.781  -25.650  1.00 2.00  ? 118  VAL D CB  1 
ATOM   3098  C  CG1 . VAL C  1 118 ? 57.385 23.036  -25.099  1.00 2.00  ? 118  VAL D CG1 1 
ATOM   3099  C  CG2 . VAL C  1 118 ? 55.632 24.794  -24.580  1.00 2.00  ? 118  VAL D CG2 1 
ATOM   3100  N  N   . VAL C  1 119 ? 58.345 23.568  -28.211  1.00 2.00  ? 119  VAL D N   1 
ATOM   3101  C  CA  . VAL C  1 119 ? 59.004 22.505  -28.962  1.00 2.00  ? 119  VAL D CA  1 
ATOM   3102  C  C   . VAL C  1 119 ? 59.895 21.703  -28.004  1.00 2.00  ? 119  VAL D C   1 
ATOM   3103  O  O   . VAL C  1 119 ? 60.580 22.253  -27.118  1.00 2.00  ? 119  VAL D O   1 
ATOM   3104  C  CB  . VAL C  1 119 ? 59.761 23.065  -30.209  1.00 2.00  ? 119  VAL D CB  1 
ATOM   3105  C  CG1 . VAL C  1 119 ? 60.908 23.965  -29.781  1.00 2.00  ? 119  VAL D CG1 1 
ATOM   3106  C  CG2 . VAL C  1 119 ? 60.283 21.907  -31.110  1.00 3.43  ? 119  VAL D CG2 1 
ATOM   3107  N  N   . HIS C  1 120 ? 59.879 20.393  -28.183  1.00 2.00  ? 120  HIS D N   1 
ATOM   3108  C  CA  . HIS C  1 120 ? 60.416 19.493  -27.195  1.00 2.00  ? 120  HIS D CA  1 
ATOM   3109  C  C   . HIS C  1 120 ? 61.726 18.836  -27.566  1.00 2.00  ? 120  HIS D C   1 
ATOM   3110  O  O   . HIS C  1 120 ? 62.131 18.827  -28.726  1.00 2.13  ? 120  HIS D O   1 
ATOM   3111  C  CB  . HIS C  1 120 ? 59.408 18.397  -26.925  1.00 2.00  ? 120  HIS D CB  1 
ATOM   3112  C  CG  . HIS C  1 120 ? 58.263 18.846  -26.095  1.00 2.00  ? 120  HIS D CG  1 
ATOM   3113  N  ND1 . HIS C  1 120 ? 58.291 18.801  -24.719  1.00 5.15  ? 120  HIS D ND1 1 
ATOM   3114  C  CD2 . HIS C  1 120 ? 57.067 19.364  -26.434  1.00 2.00  ? 120  HIS D CD2 1 
ATOM   3115  C  CE1 . HIS C  1 120 ? 57.138 19.232  -24.247  1.00 4.56  ? 120  HIS D CE1 1 
ATOM   3116  N  NE2 . HIS C  1 120 ? 56.378 19.563  -25.271  1.00 2.00  ? 120  HIS D NE2 1 
ATOM   3117  N  N   . GLU C  1 121 ? 62.331 18.222  -26.545  1.00 2.69  ? 121  GLU D N   1 
ATOM   3118  C  CA  . GLU C  1 121 ? 63.617 17.552  -26.623  1.00 4.76  ? 121  GLU D CA  1 
ATOM   3119  C  C   . GLU C  1 121 ? 63.518 16.309  -27.509  1.00 4.93  ? 121  GLU D C   1 
ATOM   3120  O  O   . GLU C  1 121 ? 64.396 16.061  -28.331  1.00 5.68  ? 121  GLU D O   1 
ATOM   3121  C  CB  . GLU C  1 121 ? 64.033 17.137  -25.202  1.00 4.83  ? 121  GLU D CB  1 
ATOM   3122  C  CG  . GLU C  1 121 ? 65.196 16.125  -25.094  1.00 7.73  ? 121  GLU D CG  1 
ATOM   3123  C  CD  . GLU C  1 121 ? 65.329 15.548  -23.697  1.00 11.01 ? 121  GLU D CD  1 
ATOM   3124  O  OE1 . GLU C  1 121 ? 66.470 15.217  -23.337  1.00 12.58 ? 121  GLU D OE1 1 
ATOM   3125  O  OE2 . GLU C  1 121 ? 64.316 15.442  -22.938  1.00 10.68 ? 121  GLU D OE2 1 
ATOM   3126  N  N   . LYS C  1 122 ? 62.427 15.557  -27.347  1.00 5.50  ? 122  LYS D N   1 
ATOM   3127  C  CA  . LYS C  1 122 ? 62.262 14.236  -27.951  1.00 6.55  ? 122  LYS D CA  1 
ATOM   3128  C  C   . LYS C  1 122 ? 61.057 14.155  -28.895  1.00 6.00  ? 122  LYS D C   1 
ATOM   3129  O  O   . LYS C  1 122 ? 60.171 15.040  -28.889  1.00 5.42  ? 122  LYS D O   1 
ATOM   3130  C  CB  . LYS C  1 122 ? 62.061 13.175  -26.840  1.00 7.35  ? 122  LYS D CB  1 
ATOM   3131  C  CG  . LYS C  1 122 ? 63.180 13.037  -25.812  1.00 9.46  ? 122  LYS D CG  1 
ATOM   3132  C  CD  . LYS C  1 122 ? 62.904 11.798  -24.900  1.00 13.42 ? 122  LYS D CD  1 
ATOM   3133  C  CE  . LYS C  1 122 ? 63.905 11.707  -23.747  1.00 18.31 ? 122  LYS D CE  1 
ATOM   3134  N  NZ  . LYS C  1 122 ? 63.527 10.653  -22.743  1.00 18.74 ? 122  LYS D NZ  1 
ATOM   3135  N  N   . ALA C  1 123 ? 61.000 13.076  -29.682  1.00 5.61  ? 123  ALA D N   1 
ATOM   3136  C  CA  . ALA C  1 123 ? 59.807 12.804  -30.485  1.00 5.20  ? 123  ALA D CA  1 
ATOM   3137  C  C   . ALA C  1 123 ? 58.583 12.544  -29.582  1.00 4.86  ? 123  ALA D C   1 
ATOM   3138  O  O   . ALA C  1 123 ? 58.678 11.885  -28.543  1.00 5.31  ? 123  ALA D O   1 
ATOM   3139  C  CB  . ALA C  1 123 ? 60.042 11.598  -31.415  1.00 6.17  ? 123  ALA D CB  1 
ATOM   3140  N  N   . ASP C  1 124 ? 57.448 13.094  -29.977  1.00 3.97  ? 124  ASP D N   1 
ATOM   3141  C  CA  . ASP C  1 124 ? 56.147 12.794  -29.384  1.00 3.75  ? 124  ASP D CA  1 
ATOM   3142  C  C   . ASP C  1 124 ? 55.714 11.413  -29.877  1.00 3.10  ? 124  ASP D C   1 
ATOM   3143  O  O   . ASP C  1 124 ? 55.631 11.216  -31.082  1.00 3.79  ? 124  ASP D O   1 
ATOM   3144  C  CB  . ASP C  1 124 ? 55.159 13.834  -29.883  1.00 3.18  ? 124  ASP D CB  1 
ATOM   3145  C  CG  . ASP C  1 124 ? 53.794 13.710  -29.267  1.00 5.53  ? 124  ASP D CG  1 
ATOM   3146  O  OD1 . ASP C  1 124 ? 53.116 14.762  -29.246  1.00 6.78  ? 124  ASP D OD1 1 
ATOM   3147  O  OD2 . ASP C  1 124 ? 53.380 12.597  -28.835  1.00 6.61  ? 124  ASP D OD2 1 
ATOM   3148  N  N   . ASP C  1 125 ? 55.418 10.476  -28.975  1.00 4.48  ? 125  ASP D N   1 
ATOM   3149  C  CA  . ASP C  1 125 ? 54.990 9.121   -29.442  1.00 5.24  ? 125  ASP D CA  1 
ATOM   3150  C  C   . ASP C  1 125 ? 53.519 9.046   -29.885  1.00 6.11  ? 125  ASP D C   1 
ATOM   3151  O  O   . ASP C  1 125 ? 53.003 7.961   -30.210  1.00 6.14  ? 125  ASP D O   1 
ATOM   3152  C  CB  . ASP C  1 125 ? 55.339 8.015   -28.420  1.00 5.76  ? 125  ASP D CB  1 
ATOM   3153  C  CG  . ASP C  1 125 ? 54.542 8.101   -27.124  1.00 5.04  ? 125  ASP D CG  1 
ATOM   3154  O  OD1 . ASP C  1 125 ? 54.980 7.470   -26.132  1.00 4.51  ? 125  ASP D OD1 1 
ATOM   3155  O  OD2 . ASP C  1 125 ? 53.493 8.776   -27.071  1.00 5.89  ? 125  ASP D OD2 1 
ATOM   3156  N  N   . LEU C  1 126 ? 52.845 10.195  -29.860  1.00 6.10  ? 126  LEU D N   1 
ATOM   3157  C  CA  . LEU C  1 126 ? 51.455 10.350  -30.328  1.00 6.55  ? 126  LEU D CA  1 
ATOM   3158  C  C   . LEU C  1 126 ? 50.477 9.450   -29.552  1.00 5.94  ? 126  LEU D C   1 
ATOM   3159  O  O   . LEU C  1 126 ? 49.459 9.039   -30.086  1.00 5.57  ? 126  LEU D O   1 
ATOM   3160  C  CB  . LEU C  1 126 ? 51.338 10.131  -31.842  1.00 6.41  ? 126  LEU D CB  1 
ATOM   3161  C  CG  . LEU C  1 126 ? 52.419 10.753  -32.740  1.00 5.77  ? 126  LEU D CG  1 
ATOM   3162  C  CD1 . LEU C  1 126 ? 52.232 10.353  -34.204  1.00 7.63  ? 126  LEU D CD1 1 
ATOM   3163  C  CD2 . LEU C  1 126 ? 52.431 12.300  -32.579  1.00 5.70  ? 126  LEU D CD2 1 
ATOM   3164  N  N   . GLY C  1 127 ? 50.812 9.197   -28.290  1.00 6.02  ? 127  GLY D N   1 
ATOM   3165  C  CA  . GLY C  1 127 ? 49.940 8.499   -27.346  1.00 6.69  ? 127  GLY D CA  1 
ATOM   3166  C  C   . GLY C  1 127 ? 49.951 7.011   -27.541  1.00 7.69  ? 127  GLY D C   1 
ATOM   3167  O  O   . GLY C  1 127 ? 49.070 6.298   -27.027  1.00 7.89  ? 127  GLY D O   1 
ATOM   3168  N  N   . LYS C  1 128 ? 50.960 6.536   -28.270  1.00 6.90  ? 128  LYS D N   1 
ATOM   3169  C  CA  . LYS C  1 128 ? 51.088 5.115   -28.619  1.00 7.72  ? 128  LYS D CA  1 
ATOM   3170  C  C   . LYS C  1 128 ? 52.148 4.391   -27.792  1.00 6.68  ? 128  LYS D C   1 
ATOM   3171  O  O   . LYS C  1 128 ? 52.511 3.244   -28.097  1.00 8.49  ? 128  LYS D O   1 
ATOM   3172  C  CB  . LYS C  1 128 ? 51.435 4.961   -30.106  1.00 6.67  ? 128  LYS D CB  1 
ATOM   3173  C  CG  . LYS C  1 128 ? 50.294 5.299   -31.030  1.00 10.65 ? 128  LYS D CG  1 
ATOM   3174  C  CD  . LYS C  1 128 ? 50.385 4.453   -32.308  1.00 17.20 ? 128  LYS D CD  1 
ATOM   3175  C  CE  . LYS C  1 128 ? 50.926 5.244   -33.406  1.00 19.71 ? 128  LYS D CE  1 
ATOM   3176  N  NZ  . LYS C  1 128 ? 51.135 4.341   -34.585  1.00 20.16 ? 128  LYS D NZ  1 
ATOM   3177  N  N   . GLY C  1 129 ? 52.662 5.048   -26.765  1.00 6.72  ? 129  GLY D N   1 
ATOM   3178  C  CA  . GLY C  1 129 ? 53.773 4.486   -25.996  1.00 5.62  ? 129  GLY D CA  1 
ATOM   3179  C  C   . GLY C  1 129 ? 53.408 3.486   -24.910  1.00 6.38  ? 129  GLY D C   1 
ATOM   3180  O  O   . GLY C  1 129 ? 54.303 2.825   -24.374  1.00 6.65  ? 129  GLY D O   1 
ATOM   3181  N  N   . GLY C  1 130 ? 52.115 3.376   -24.564  1.00 6.25  ? 130  GLY D N   1 
ATOM   3182  C  CA  . GLY C  1 130 ? 51.669 2.323   -23.636  1.00 7.59  ? 130  GLY D CA  1 
ATOM   3183  C  C   . GLY C  1 130 ? 51.957 2.576   -22.162  1.00 8.00  ? 130  GLY D C   1 
ATOM   3184  O  O   . GLY C  1 130 ? 51.562 1.780   -21.314  1.00 8.87  ? 130  GLY D O   1 
ATOM   3185  N  N   . ASN C  1 131 ? 52.652 3.677   -21.857  1.00 7.94  ? 131  ASN D N   1 
ATOM   3186  C  CA  . ASN C  1 131 ? 52.845 4.101   -20.469  1.00 7.52  ? 131  ASN D CA  1 
ATOM   3187  C  C   . ASN C  1 131 ? 51.913 5.273   -20.096  1.00 8.08  ? 131  ASN D C   1 
ATOM   3188  O  O   . ASN C  1 131 ? 51.314 5.896   -20.969  1.00 7.03  ? 131  ASN D O   1 
ATOM   3189  C  CB  . ASN C  1 131 ? 54.330 4.382   -20.144  1.00 7.81  ? 131  ASN D CB  1 
ATOM   3190  C  CG  . ASN C  1 131 ? 54.873 5.632   -20.837  1.00 8.54  ? 131  ASN D CG  1 
ATOM   3191  O  OD1 . ASN C  1 131 ? 54.238 6.192   -21.716  1.00 9.72  ? 131  ASN D OD1 1 
ATOM   3192  N  ND2 . ASN C  1 131 ? 56.054 6.059   -20.440  1.00 8.63  ? 131  ASN D ND2 1 
ATOM   3193  N  N   . GLU C  1 132 ? 51.779 5.559   -18.805  1.00 8.16  ? 132  GLU D N   1 
ATOM   3194  C  CA  . GLU C  1 132 ? 50.923 6.671   -18.368  1.00 9.38  ? 132  GLU D CA  1 
ATOM   3195  C  C   . GLU C  1 132 ? 51.337 7.968   -19.021  1.00 8.62  ? 132  GLU D C   1 
ATOM   3196  O  O   . GLU C  1 132 ? 50.502 8.783   -19.409  1.00 8.43  ? 132  GLU D O   1 
ATOM   3197  C  CB  . GLU C  1 132 ? 50.988 6.851   -16.853  1.00 10.66 ? 132  GLU D CB  1 
ATOM   3198  C  CG  . GLU C  1 132 ? 50.194 8.065   -16.340  1.00 15.31 ? 132  GLU D CG  1 
ATOM   3199  C  CD  . GLU C  1 132 ? 48.687 7.909   -16.404  1.00 22.99 ? 132  GLU D CD  1 
ATOM   3200  O  OE1 . GLU C  1 132 ? 48.174 6.772   -16.598  1.00 24.90 ? 132  GLU D OE1 1 
ATOM   3201  O  OE2 . GLU C  1 132 ? 48.001 8.945   -16.239  1.00 25.91 ? 132  GLU D OE2 1 
ATOM   3202  N  N   . GLU C  1 133 ? 52.641 8.167   -19.126  1.00 8.36  ? 133  GLU D N   1 
ATOM   3203  C  CA  . GLU C  1 133 ? 53.150 9.432   -19.644  1.00 9.15  ? 133  GLU D CA  1 
ATOM   3204  C  C   . GLU C  1 133 ? 52.847 9.612   -21.149  1.00 7.94  ? 133  GLU D C   1 
ATOM   3205  O  O   . GLU C  1 133 ? 52.659 10.727  -21.634  1.00 7.20  ? 133  GLU D O   1 
ATOM   3206  C  CB  . GLU C  1 133 ? 54.639 9.596   -19.274  1.00 9.26  ? 133  GLU D CB  1 
ATOM   3207  C  CG  . GLU C  1 133 ? 55.181 10.988  -19.446  1.00 12.36 ? 133  GLU D CG  1 
ATOM   3208  C  CD  . GLU C  1 133 ? 54.663 12.035  -18.429  1.00 15.34 ? 133  GLU D CD  1 
ATOM   3209  O  OE1 . GLU C  1 133 ? 55.247 13.143  -18.400  1.00 16.09 ? 133  GLU D OE1 1 
ATOM   3210  O  OE2 . GLU C  1 133 ? 53.704 11.774  -17.671  1.00 15.37 ? 133  GLU D OE2 1 
ATOM   3211  N  N   . SER C  1 134 ? 52.725 8.516   -21.883  1.00 7.08  ? 134  SER D N   1 
ATOM   3212  C  CA  . SER C  1 134 ? 52.345 8.631   -23.291  1.00 6.39  ? 134  SER D CA  1 
ATOM   3213  C  C   . SER C  1 134 ? 50.986 9.330   -23.471  1.00 6.70  ? 134  SER D C   1 
ATOM   3214  O  O   . SER C  1 134 ? 50.812 10.156  -24.406  1.00 6.55  ? 134  SER D O   1 
ATOM   3215  C  CB  . SER C  1 134 ? 52.349 7.250   -23.953  1.00 6.66  ? 134  SER D CB  1 
ATOM   3216  O  OG  . SER C  1 134 ? 51.965 7.346   -25.314  1.00 5.54  ? 134  SER D OG  1 
ATOM   3217  N  N   . THR C  1 135 ? 50.071 9.042   -22.538  1.00 6.24  ? 135  THR D N   1 
ATOM   3218  C  CA  . THR C  1 135 ? 48.700 9.586   -22.514  1.00 8.00  ? 135  THR D CA  1 
ATOM   3219  C  C   . THR C  1 135 ? 48.595 11.032  -22.013  1.00 7.65  ? 135  THR D C   1 
ATOM   3220  O  O   . THR C  1 135 ? 47.499 11.613  -22.022  1.00 7.37  ? 135  THR D O   1 
ATOM   3221  C  CB  . THR C  1 135 ? 47.716 8.695   -21.661  1.00 7.46  ? 135  THR D CB  1 
ATOM   3222  O  OG1 . THR C  1 135 ? 47.922 8.939   -20.256  1.00 12.04 ? 135  THR D OG1 1 
ATOM   3223  C  CG2 . THR C  1 135 ? 47.931 7.245   -21.949  1.00 10.42 ? 135  THR D CG2 1 
ATOM   3224  N  N   . LYS C  1 136 ? 49.726 11.611  -21.588  1.00 7.43  ? 136  LYS D N   1 
ATOM   3225  C  CA  . LYS C  1 136 ? 49.753 12.989  -21.099  1.00 7.39  ? 136  LYS D CA  1 
ATOM   3226  C  C   . LYS C  1 136 ? 50.620 13.883  -21.969  1.00 6.29  ? 136  LYS D C   1 
ATOM   3227  O  O   . LYS C  1 136 ? 50.167 14.942  -22.419  1.00 4.75  ? 136  LYS D O   1 
ATOM   3228  C  CB  . LYS C  1 136 ? 50.213 13.042  -19.639  1.00 8.55  ? 136  LYS D CB  1 
ATOM   3229  C  CG  . LYS C  1 136 ? 49.254 12.306  -18.697  1.00 12.73 ? 136  LYS D CG  1 
ATOM   3230  C  CD  . LYS C  1 136 ? 49.960 11.897  -17.437  1.00 20.02 ? 136  LYS D CD  1 
ATOM   3231  C  CE  . LYS C  1 136 ? 49.818 12.937  -16.365  1.00 23.05 ? 136  LYS D CE  1 
ATOM   3232  N  NZ  . LYS C  1 136 ? 50.292 12.393  -15.056  1.00 28.95 ? 136  LYS D NZ  1 
ATOM   3233  N  N   . THR C  1 137 ? 51.837 13.429  -22.252  1.00 4.79  ? 137  THR D N   1 
ATOM   3234  C  CA  . THR C  1 137 ? 52.818 14.239  -22.957  1.00 5.11  ? 137  THR D CA  1 
ATOM   3235  C  C   . THR C  1 137 ? 53.352 13.604  -24.227  1.00 4.24  ? 137  THR D C   1 
ATOM   3236  O  O   . THR C  1 137 ? 54.119 14.239  -24.955  1.00 3.95  ? 137  THR D O   1 
ATOM   3237  C  CB  . THR C  1 137 ? 54.035 14.529  -22.047  1.00 4.66  ? 137  THR D CB  1 
ATOM   3238  O  OG1 . THR C  1 137 ? 54.771 13.306  -21.851  1.00 5.51  ? 137  THR D OG1 1 
ATOM   3239  C  CG2 . THR C  1 137 ? 53.562 15.096  -20.679  1.00 4.79  ? 137  THR D CG2 1 
ATOM   3240  N  N   . GLY C  1 138 ? 53.004 12.339  -24.485  1.00 3.74  ? 138  GLY D N   1 
ATOM   3241  C  CA  . GLY C  1 138 ? 53.599 11.651  -25.613  1.00 4.43  ? 138  GLY D CA  1 
ATOM   3242  C  C   . GLY C  1 138 ? 55.070 11.323  -25.382  1.00 4.57  ? 138  GLY D C   1 
ATOM   3243  O  O   . GLY C  1 138 ? 55.792 10.957  -26.324  1.00 5.02  ? 138  GLY D O   1 
ATOM   3244  N  N   . ASN C  1 139 ? 55.504 11.419  -24.122  1.00 4.62  ? 139  ASN D N   1 
ATOM   3245  C  CA  . ASN C  1 139 ? 56.898 11.215  -23.728  1.00 5.57  ? 139  ASN D CA  1 
ATOM   3246  C  C   . ASN C  1 139 ? 57.867 12.140  -24.483  1.00 5.42  ? 139  ASN D C   1 
ATOM   3247  O  O   . ASN C  1 139 ? 58.983 11.731  -24.813  1.00 5.62  ? 139  ASN D O   1 
ATOM   3248  C  CB  . ASN C  1 139 ? 57.321 9.749   -23.984  1.00 5.57  ? 139  ASN D CB  1 
ATOM   3249  C  CG  . ASN C  1 139 ? 56.692 8.803   -23.017  1.00 7.08  ? 139  ASN D CG  1 
ATOM   3250  O  OD1 . ASN C  1 139 ? 57.044 8.809   -21.845  1.00 6.65  ? 139  ASN D OD1 1 
ATOM   3251  N  ND2 . ASN C  1 139 ? 55.740 7.985   -23.493  1.00 7.98  ? 139  ASN D ND2 1 
ATOM   3252  N  N   . ALA C  1 140 ? 57.436 13.362  -24.760  1.00 4.54  ? 140  ALA D N   1 
ATOM   3253  C  CA  . ALA C  1 140 ? 58.226 14.301  -25.586  1.00 5.16  ? 140  ALA D CA  1 
ATOM   3254  C  C   . ALA C  1 140 ? 59.444 14.906  -24.846  1.00 5.20  ? 140  ALA D C   1 
ATOM   3255  O  O   . ALA C  1 140 ? 60.296 15.593  -25.454  1.00 4.51  ? 140  ALA D O   1 
ATOM   3256  C  CB  . ALA C  1 140 ? 57.314 15.409  -26.123  1.00 4.54  ? 140  ALA D CB  1 
ATOM   3257  N  N   . GLY C  1 141 ? 59.527 14.674  -23.538  1.00 5.05  ? 141  GLY D N   1 
ATOM   3258  C  CA  . GLY C  1 141 ? 60.682 15.132  -22.763  1.00 4.96  ? 141  GLY D CA  1 
ATOM   3259  C  C   . GLY C  1 141 ? 60.695 16.643  -22.545  1.00 4.00  ? 141  GLY D C   1 
ATOM   3260  O  O   . GLY C  1 141 ? 59.646 17.287  -22.535  1.00 3.64  ? 141  GLY D O   1 
ATOM   3261  N  N   . SER C  1 142 ? 61.886 17.210  -22.369  1.00 3.85  ? 142  SER D N   1 
ATOM   3262  C  CA  . SER C  1 142 ? 61.982 18.568  -21.827  1.00 4.36  ? 142  SER D CA  1 
ATOM   3263  C  C   . SER C  1 142 ? 61.513 19.604  -22.839  1.00 3.83  ? 142  SER D C   1 
ATOM   3264  O  O   . SER C  1 142 ? 61.384 19.304  -24.033  1.00 3.94  ? 142  SER D O   1 
ATOM   3265  C  CB  . SER C  1 142 ? 63.407 18.871  -21.312  1.00 5.34  ? 142  SER D CB  1 
ATOM   3266  O  OG  . SER C  1 142 ? 64.316 19.022  -22.383  1.00 8.69  ? 142  SER D OG  1 
ATOM   3267  N  N   . ARG C  1 143 ? 61.257 20.814  -22.354  1.00 2.76  ? 143  ARG D N   1 
ATOM   3268  C  CA  . ARG C  1 143 ? 60.828 21.923  -23.180  1.00 3.04  ? 143  ARG D CA  1 
ATOM   3269  C  C   . ARG C  1 143 ? 62.042 22.754  -23.594  1.00 2.78  ? 143  ARG D C   1 
ATOM   3270  O  O   . ARG C  1 143 ? 62.611 23.483  -22.790  1.00 4.04  ? 143  ARG D O   1 
ATOM   3271  C  CB  . ARG C  1 143 ? 59.800 22.760  -22.409  1.00 2.54  ? 143  ARG D CB  1 
ATOM   3272  C  CG  . ARG C  1 143 ? 58.640 21.864  -21.870  1.00 3.31  ? 143  ARG D CG  1 
ATOM   3273  C  CD  . ARG C  1 143 ? 57.809 22.558  -20.814  1.00 3.94  ? 143  ARG D CD  1 
ATOM   3274  N  NE  . ARG C  1 143 ? 56.779 21.628  -20.378  1.00 4.62  ? 143  ARG D NE  1 
ATOM   3275  C  CZ  . ARG C  1 143 ? 55.601 21.942  -19.853  1.00 4.75  ? 143  ARG D CZ  1 
ATOM   3276  N  NH1 . ARG C  1 143 ? 54.790 20.945  -19.500  1.00 4.39  ? 143  ARG D NH1 1 
ATOM   3277  N  NH2 . ARG C  1 143 ? 55.214 23.216  -19.701  1.00 5.09  ? 143  ARG D NH2 1 
ATOM   3278  N  N   . LEU C  1 144 ? 62.443 22.620  -24.848  1.00 2.54  ? 144  LEU D N   1 
ATOM   3279  C  CA  . LEU C  1 144 ? 63.651 23.278  -25.318  1.00 2.79  ? 144  LEU D CA  1 
ATOM   3280  C  C   . LEU C  1 144 ? 63.455 24.742  -25.619  1.00 2.71  ? 144  LEU D C   1 
ATOM   3281  O  O   . LEU C  1 144 ? 64.395 25.516  -25.458  1.00 3.74  ? 144  LEU D O   1 
ATOM   3282  C  CB  . LEU C  1 144 ? 64.213 22.582  -26.565  1.00 2.69  ? 144  LEU D CB  1 
ATOM   3283  C  CG  . LEU C  1 144 ? 64.568 21.093  -26.408  1.00 4.04  ? 144  LEU D CG  1 
ATOM   3284  C  CD1 . LEU C  1 144 ? 65.174 20.640  -27.737  1.00 4.95  ? 144  LEU D CD1 1 
ATOM   3285  C  CD2 . LEU C  1 144 ? 65.506 20.808  -25.226  1.00 7.55  ? 144  LEU D CD2 1 
ATOM   3286  N  N   . ALA C  1 145 ? 62.268 25.116  -26.092  1.00 2.16  ? 145  ALA D N   1 
ATOM   3287  C  CA  . ALA C  1 145 ? 61.988 26.502  -26.394  1.00 2.00  ? 145  ALA D CA  1 
ATOM   3288  C  C   . ALA C  1 145 ? 60.466 26.703  -26.388  1.00 2.03  ? 145  ALA D C   1 
ATOM   3289  O  O   . ALA C  1 145 ? 59.701 25.753  -26.635  1.00 2.00  ? 145  ALA D O   1 
ATOM   3290  C  CB  . ALA C  1 145 ? 62.580 26.903  -27.742  1.00 2.00  ? 145  ALA D CB  1 
ATOM   3291  N  N   . CYS C  1 146 ? 60.042 27.931  -26.119  1.00 2.00  ? 146  CYS D N   1 
ATOM   3292  C  CA  . CYS C  1 146 ? 58.610 28.197  -26.096  1.00 2.00  ? 146  CYS D CA  1 
ATOM   3293  C  C   . CYS C  1 146 ? 58.398 29.678  -26.252  1.00 2.00  ? 146  CYS D C   1 
ATOM   3294  O  O   . CYS C  1 146 ? 59.340 30.470  -26.148  1.00 2.00  ? 146  CYS D O   1 
ATOM   3295  C  CB  . CYS C  1 146 ? 58.007 27.739  -24.767  0.40 2.00  ? 146  CYS D CB  1 
ATOM   3296  S  SG  . CYS C  1 146 ? 58.683 28.538  -23.290  0.40 2.00  ? 146  CYS D SG  1 
ATOM   3297  N  N   . GLY C  1 147 ? 57.141 30.053  -26.434  1.00 2.00  ? 147  GLY D N   1 
ATOM   3298  C  CA  . GLY C  1 147 ? 56.790 31.479  -26.428  1.00 2.00  ? 147  GLY D CA  1 
ATOM   3299  C  C   . GLY C  1 147 ? 55.283 31.579  -26.381  1.00 2.00  ? 147  GLY D C   1 
ATOM   3300  O  O   . GLY C  1 147 ? 54.566 30.594  -26.672  1.00 2.00  ? 147  GLY D O   1 
ATOM   3301  N  N   . VAL C  1 148 ? 54.816 32.771  -26.049  1.00 2.00  ? 148  VAL D N   1 
ATOM   3302  C  CA  . VAL C  1 148 ? 53.390 33.020  -25.956  1.00 2.31  ? 148  VAL D CA  1 
ATOM   3303  C  C   . VAL C  1 148 ? 52.876 33.396  -27.352  1.00 2.00  ? 148  VAL D C   1 
ATOM   3304  O  O   . VAL C  1 148 ? 53.501 34.189  -28.088  1.00 2.00  ? 148  VAL D O   1 
ATOM   3305  C  CB  . VAL C  1 148 ? 53.041 34.144  -24.956  1.00 2.00  ? 148  VAL D CB  1 
ATOM   3306  C  CG1 . VAL C  1 148 ? 51.498 34.252  -24.869  1.00 2.00  ? 148  VAL D CG1 1 
ATOM   3307  C  CG2 . VAL C  1 148 ? 53.626 33.858  -23.590  1.00 2.20  ? 148  VAL D CG2 1 
ATOM   3308  N  N   . ILE C  1 149 ? 51.750 32.799  -27.723  1.00 2.00  ? 149  ILE D N   1 
ATOM   3309  C  CA  . ILE C  1 149 ? 51.174 33.027  -29.052  1.00 2.00  ? 149  ILE D CA  1 
ATOM   3310  C  C   . ILE C  1 149 ? 50.424 34.360  -29.041  1.00 2.00  ? 149  ILE D C   1 
ATOM   3311  O  O   . ILE C  1 149 ? 49.524 34.587  -28.207  1.00 2.00  ? 149  ILE D O   1 
ATOM   3312  C  CB  . ILE C  1 149 ? 50.236 31.867  -29.442  1.00 2.00  ? 149  ILE D CB  1 
ATOM   3313  C  CG1 . ILE C  1 149 ? 51.050 30.550  -29.528  1.00 2.00  ? 149  ILE D CG1 1 
ATOM   3314  C  CG2 . ILE C  1 149 ? 49.569 32.109  -30.810  1.00 2.00  ? 149  ILE D CG2 1 
ATOM   3315  C  CD1 . ILE C  1 149 ? 50.148 29.328  -29.554  1.00 2.00  ? 149  ILE D CD1 1 
ATOM   3316  N  N   . GLY C  1 150 ? 50.786 35.243  -29.953  1.00 2.50  ? 150  GLY D N   1 
ATOM   3317  C  CA  . GLY C  1 150 ? 50.145 36.557  -29.982  1.00 3.86  ? 150  GLY D CA  1 
ATOM   3318  C  C   . GLY C  1 150 ? 49.388 36.853  -31.263  1.00 4.60  ? 150  GLY D C   1 
ATOM   3319  O  O   . GLY C  1 150 ? 49.676 36.278  -32.320  1.00 4.81  ? 150  GLY D O   1 
ATOM   3320  N  N   . ILE C  1 151 ? 48.455 37.798  -31.189  1.00 4.79  ? 151  ILE D N   1 
ATOM   3321  C  CA  . ILE C  1 151 ? 47.738 38.221  -32.390  1.00 5.89  ? 151  ILE D CA  1 
ATOM   3322  C  C   . ILE C  1 151 ? 48.706 39.002  -33.280  1.00 5.32  ? 151  ILE D C   1 
ATOM   3323  O  O   . ILE C  1 151 ? 49.519 39.760  -32.782  1.00 5.69  ? 151  ILE D O   1 
ATOM   3324  C  CB  . ILE C  1 151 ? 46.462 39.045  -32.057  1.00 5.63  ? 151  ILE D CB  1 
ATOM   3325  C  CG1 . ILE C  1 151 ? 45.743 39.444  -33.346  1.00 9.57  ? 151  ILE D CG1 1 
ATOM   3326  C  CG2 . ILE C  1 151 ? 46.765 40.294  -31.262  1.00 7.46  ? 151  ILE D CG2 1 
ATOM   3327  C  CD1 . ILE C  1 151 ? 44.899 38.350  -33.895  1.00 13.49 ? 151  ILE D CD1 1 
ATOM   3328  N  N   . ALA C  1 152 ? 48.631 38.762  -34.578  1.00 6.00  ? 152  ALA D N   1 
ATOM   3329  C  CA  . ALA C  1 152 ? 49.529 39.357  -35.558  1.00 7.78  ? 152  ALA D CA  1 
ATOM   3330  C  C   . ALA C  1 152 ? 48.724 40.117  -36.591  1.00 9.49  ? 152  ALA D C   1 
ATOM   3331  O  O   . ALA C  1 152 ? 47.507 39.871  -36.772  1.00 9.04  ? 152  ALA D O   1 
ATOM   3332  C  CB  . ALA C  1 152 ? 50.380 38.270  -36.235  1.00 8.23  ? 152  ALA D CB  1 
ATOM   3333  N  N   . GLN C  1 153 ? 49.412 41.017  -37.282  1.00 11.10 ? 153  GLN D N   1 
ATOM   3334  C  CA  . GLN C  1 153 ? 48.780 41.927  -38.223  1.00 13.80 ? 153  GLN D CA  1 
ATOM   3335  C  C   . GLN C  1 153 ? 48.340 41.159  -39.454  1.00 15.32 ? 153  GLN D C   1 
ATOM   3336  O  O   . GLN C  1 153 ? 49.042 40.246  -39.873  1.00 17.08 ? 153  GLN D O   1 
ATOM   3337  C  CB  . GLN C  1 153 ? 49.733 43.055  -38.607  1.00 13.70 ? 153  GLN D CB  1 
ATOM   3338  C  CG  . GLN C  1 153 ? 49.009 44.172  -39.363  1.00 17.57 ? 153  GLN D CG  1 
ATOM   3339  C  CD  . GLN C  1 153 ? 49.834 45.429  -39.507  1.00 20.34 ? 153  GLN D CD  1 
ATOM   3340  O  OE1 . GLN C  1 153 ? 49.298 46.529  -39.462  1.00 23.56 ? 153  GLN D OE1 1 
ATOM   3341  N  NE2 . GLN C  1 153 ? 51.137 45.272  -39.700  1.00 22.19 ? 153  GLN D NE2 1 
ATOM   3342  O  OXT . GLN C  1 153 ? 47.276 41.417  -40.020  1.00 16.92 ? 153  GLN D OXT 1 
ATOM   3343  N  N   . ALA D  1 1   ? 36.774 33.892  -12.095  1.00 17.58 ? 1    ALA E N   1 
ATOM   3344  C  CA  . ALA D  1 1   ? 37.701 34.998  -12.471  1.00 16.82 ? 1    ALA E CA  1 
ATOM   3345  C  C   . ALA D  1 1   ? 38.530 34.617  -13.712  1.00 16.12 ? 1    ALA E C   1 
ATOM   3346  O  O   . ALA D  1 1   ? 38.590 33.442  -14.091  1.00 17.19 ? 1    ALA E O   1 
ATOM   3347  C  CB  . ALA D  1 1   ? 38.601 35.356  -11.285  1.00 17.75 ? 1    ALA E CB  1 
ATOM   3348  N  N   . THR D  1 2   ? 39.111 35.615  -14.370  1.00 13.67 ? 2    THR E N   1 
ATOM   3349  C  CA  . THR D  1 2   ? 40.053 35.393  -15.473  1.00 11.37 ? 2    THR E CA  1 
ATOM   3350  C  C   . THR D  1 2   ? 41.368 36.015  -15.003  1.00 9.05  ? 2    THR E C   1 
ATOM   3351  O  O   . THR D  1 2   ? 41.354 37.044  -14.317  1.00 7.05  ? 2    THR E O   1 
ATOM   3352  C  CB  . THR D  1 2   ? 39.551 36.053  -16.795  1.00 12.06 ? 2    THR E CB  1 
ATOM   3353  O  OG1 . THR D  1 2   ? 38.276 35.514  -17.148  1.00 15.49 ? 2    THR E OG1 1 
ATOM   3354  C  CG2 . THR D  1 2   ? 40.490 35.792  -17.950  1.00 13.69 ? 2    THR E CG2 1 
ATOM   3355  N  N   . LYS D  1 3   ? 42.486 35.366  -15.331  1.00 5.43  ? 3    LYS E N   1 
ATOM   3356  C  CA  . LYS D  1 3   ? 43.814 35.843  -14.967  1.00 5.50  ? 3    LYS E CA  1 
ATOM   3357  C  C   . LYS D  1 3   ? 44.727 35.810  -16.183  1.00 4.57  ? 3    LYS E C   1 
ATOM   3358  O  O   . LYS D  1 3   ? 44.581 34.958  -17.078  1.00 3.18  ? 3    LYS E O   1 
ATOM   3359  C  CB  . LYS D  1 3   ? 44.430 35.009  -13.865  1.00 5.76  ? 3    LYS E CB  1 
ATOM   3360  C  CG  . LYS D  1 3   ? 43.815 35.274  -12.480  1.00 8.81  ? 3    LYS E CG  1 
ATOM   3361  C  CD  . LYS D  1 3   ? 44.586 34.507  -11.391  1.00 14.14 ? 3    LYS E CD  1 
ATOM   3362  C  CE  . LYS D  1 3   ? 45.777 35.298  -10.828  1.00 18.66 ? 3    LYS E CE  1 
ATOM   3363  N  NZ  . LYS D  1 3   ? 46.477 34.602  -9.682   1.00 20.83 ? 3    LYS E NZ  1 
ATOM   3364  N  N   . ALA D  1 4   ? 45.631 36.780  -16.221  1.00 3.01  ? 4    ALA E N   1 
ATOM   3365  C  CA  . ALA D  1 4   ? 46.602 36.866  -17.280  1.00 2.74  ? 4    ALA E CA  1 
ATOM   3366  C  C   . ALA D  1 4   ? 47.949 37.310  -16.689  1.00 2.17  ? 4    ALA E C   1 
ATOM   3367  O  O   . ALA D  1 4   ? 48.032 37.736  -15.511  1.00 2.00  ? 4    ALA E O   1 
ATOM   3368  C  CB  . ALA D  1 4   ? 46.106 37.797  -18.420  1.00 3.00  ? 4    ALA E CB  1 
ATOM   3369  N  N   . VAL D  1 5   ? 49.009 37.167  -17.476  1.00 2.00  ? 5    VAL E N   1 
ATOM   3370  C  CA  . VAL D  1 5   ? 50.372 37.441  -16.997  1.00 2.26  ? 5    VAL E CA  1 
ATOM   3371  C  C   . VAL D  1 5   ? 51.245 37.859  -18.192  1.00 2.55  ? 5    VAL E C   1 
ATOM   3372  O  O   . VAL D  1 5   ? 50.949 37.483  -19.348  1.00 2.40  ? 5    VAL E O   1 
ATOM   3373  C  CB  . VAL D  1 5   ? 50.973 36.237  -16.207  1.00 2.00  ? 5    VAL E CB  1 
ATOM   3374  C  CG1 . VAL D  1 5   ? 51.283 35.001  -17.162  1.00 2.00  ? 5    VAL E CG1 1 
ATOM   3375  C  CG2 . VAL D  1 5   ? 52.226 36.660  -15.442  1.00 3.02  ? 5    VAL E CG2 1 
ATOM   3376  N  N   . CYS D  1 6   ? 52.254 38.693  -17.928  1.00 2.29  ? 6    CYS E N   1 
ATOM   3377  C  CA  . CYS D  1 6   ? 53.111 39.236  -18.975  1.00 3.22  ? 6    CYS E CA  1 
ATOM   3378  C  C   . CYS D  1 6   ? 54.530 39.364  -18.438  1.00 3.82  ? 6    CYS E C   1 
ATOM   3379  O  O   . CYS D  1 6   ? 54.745 39.971  -17.383  1.00 4.01  ? 6    CYS E O   1 
ATOM   3380  C  CB  . CYS D  1 6   ? 52.624 40.638  -19.412  1.00 3.50  ? 6    CYS E CB  1 
ATOM   3381  S  SG  . CYS D  1 6   ? 53.640 41.255  -20.778  1.00 5.44  ? 6    CYS E SG  1 
ATOM   3382  N  N   . VAL D  1 7   ? 55.481 38.748  -19.146  1.00 3.95  ? 7    VAL E N   1 
ATOM   3383  C  CA  . VAL D  1 7   ? 56.898 38.847  -18.819  1.00 3.87  ? 7    VAL E CA  1 
ATOM   3384  C  C   . VAL D  1 7   ? 57.472 39.925  -19.721  1.00 4.42  ? 7    VAL E C   1 
ATOM   3385  O  O   . VAL D  1 7   ? 57.439 39.800  -20.958  1.00 3.77  ? 7    VAL E O   1 
ATOM   3386  C  CB  . VAL D  1 7   ? 57.642 37.504  -19.030  1.00 4.04  ? 7    VAL E CB  1 
ATOM   3387  C  CG1 . VAL D  1 7   ? 59.155 37.671  -18.734  1.00 5.26  ? 7    VAL E CG1 1 
ATOM   3388  C  CG2 . VAL D  1 7   ? 57.020 36.400  -18.150  1.00 3.86  ? 7    VAL E CG2 1 
ATOM   3389  N  N   . LEU D  1 8   ? 57.968 41.004  -19.114  1.00 3.95  ? 8    LEU E N   1 
ATOM   3390  C  CA  . LEU D  1 8   ? 58.497 42.122  -19.875  1.00 5.13  ? 8    LEU E CA  1 
ATOM   3391  C  C   . LEU D  1 8   ? 60.007 42.002  -19.995  1.00 5.27  ? 8    LEU E C   1 
ATOM   3392  O  O   . LEU D  1 8   ? 60.700 41.897  -18.976  1.00 5.08  ? 8    LEU E O   1 
ATOM   3393  C  CB  . LEU D  1 8   ? 58.175 43.437  -19.163  1.00 5.89  ? 8    LEU E CB  1 
ATOM   3394  C  CG  . LEU D  1 8   ? 56.710 43.870  -19.042  1.00 8.41  ? 8    LEU E CG  1 
ATOM   3395  C  CD1 . LEU D  1 8   ? 56.653 45.170  -18.271  1.00 10.68 ? 8    LEU E CD1 1 
ATOM   3396  C  CD2 . LEU D  1 8   ? 56.211 44.103  -20.415  1.00 12.70 ? 8    LEU E CD2 1 
ATOM   3397  N  N   . LYS D  1 9   ? 60.512 42.032  -21.221  1.00 5.31  ? 9    LYS E N   1 
ATOM   3398  C  CA  . LYS D  1 9   ? 61.951 41.956  -21.455  1.00 7.33  ? 9    LYS E CA  1 
ATOM   3399  C  C   . LYS D  1 9   ? 62.262 42.853  -22.622  1.00 7.16  ? 9    LYS E C   1 
ATOM   3400  O  O   . LYS D  1 9   ? 61.397 43.088  -23.455  1.00 5.92  ? 9    LYS E O   1 
ATOM   3401  C  CB  . LYS D  1 9   ? 62.356 40.531  -21.843  1.00 7.82  ? 9    LYS E CB  1 
ATOM   3402  C  CG  . LYS D  1 9   ? 62.334 39.534  -20.705  1.00 11.33 ? 9    LYS E CG  1 
ATOM   3403  C  CD  . LYS D  1 9   ? 62.634 38.127  -21.264  1.00 16.94 ? 9    LYS E CD  1 
ATOM   3404  C  CE  . LYS D  1 9   ? 63.300 37.237  -20.230  1.00 22.69 ? 9    LYS E CE  1 
ATOM   3405  N  NZ  . LYS D  1 9   ? 62.402 36.881  -19.086  1.00 25.88 ? 9    LYS E NZ  1 
ATOM   3406  N  N   . GLY D  1 10  ? 63.515 43.314  -22.704  1.00 6.80  ? 10   GLY E N   1 
ATOM   3407  C  CA  . GLY D  1 10  ? 63.954 44.116  -23.831  1.00 8.22  ? 10   GLY E CA  1 
ATOM   3408  C  C   . GLY D  1 10  ? 65.436 43.900  -24.157  1.00 9.27  ? 10   GLY E C   1 
ATOM   3409  O  O   . GLY D  1 10  ? 66.043 42.916  -23.745  1.00 9.84  ? 10   GLY E O   1 
ATOM   3410  N  N   . ASP D  1 11  ? 65.993 44.831  -24.907  1.00 10.76 ? 11   ASP E N   1 
ATOM   3411  C  CA  . ASP D  1 11  ? 67.409 44.791  -25.285  1.00 12.29 ? 11   ASP E CA  1 
ATOM   3412  C  C   . ASP D  1 11  ? 68.279 45.378  -24.160  1.00 11.98 ? 11   ASP E C   1 
ATOM   3413  O  O   . ASP D  1 11  ? 69.495 45.115  -24.071  1.00 13.87 ? 11   ASP E O   1 
ATOM   3414  C  CB  . ASP D  1 11  ? 67.594 45.572  -26.584  1.00 13.62 ? 11   ASP E CB  1 
ATOM   3415  C  CG  . ASP D  1 11  ? 69.004 45.455  -27.142  1.00 17.40 ? 11   ASP E CG  1 
ATOM   3416  O  OD1 . ASP D  1 11  ? 69.418 44.327  -27.506  1.00 23.63 ? 11   ASP E OD1 1 
ATOM   3417  O  OD2 . ASP D  1 11  ? 69.699 46.496  -27.213  1.00 23.82 ? 11   ASP E OD2 1 
ATOM   3418  N  N   . GLY D  1 12  ? 67.666 46.175  -23.298  1.00 10.54 ? 12   GLY E N   1 
ATOM   3419  C  CA  . GLY D  1 12  ? 68.379 46.823  -22.205  1.00 8.90  ? 12   GLY E CA  1 
ATOM   3420  C  C   . GLY D  1 12  ? 68.140 46.069  -20.915  1.00 7.32  ? 12   GLY E C   1 
ATOM   3421  O  O   . GLY D  1 12  ? 67.719 44.931  -20.950  1.00 6.97  ? 12   GLY E O   1 
ATOM   3422  N  N   . PRO D  1 13  ? 68.355 46.732  -19.776  1.00 7.35  ? 13   PRO E N   1 
ATOM   3423  C  CA  . PRO D  1 13  ? 68.221 46.138  -18.456  1.00 7.07  ? 13   PRO E CA  1 
ATOM   3424  C  C   . PRO D  1 13  ? 66.784 46.003  -17.904  1.00 6.54  ? 13   PRO E C   1 
ATOM   3425  O  O   . PRO D  1 13  ? 66.597 45.470  -16.814  1.00 6.40  ? 13   PRO E O   1 
ATOM   3426  C  CB  . PRO D  1 13  ? 69.028 47.086  -17.584  1.00 7.22  ? 13   PRO E CB  1 
ATOM   3427  C  CG  . PRO D  1 13  ? 68.857 48.425  -18.239  1.00 7.14  ? 13   PRO E CG  1 
ATOM   3428  C  CD  . PRO D  1 13  ? 68.790 48.141  -19.707  1.00 7.06  ? 13   PRO E CD  1 
ATOM   3429  N  N   . VAL D  1 14  ? 65.785 46.474  -18.641  1.00 6.17  ? 14   VAL E N   1 
ATOM   3430  C  CA  . VAL D  1 14  ? 64.405 46.479  -18.095  1.00 5.51  ? 14   VAL E CA  1 
ATOM   3431  C  C   . VAL D  1 14  ? 63.797 45.077  -18.109  1.00 5.04  ? 14   VAL E C   1 
ATOM   3432  O  O   . VAL D  1 14  ? 63.739 44.415  -19.142  1.00 5.15  ? 14   VAL E O   1 
ATOM   3433  C  CB  . VAL D  1 14  ? 63.494 47.504  -18.805  1.00 5.61  ? 14   VAL E CB  1 
ATOM   3434  C  CG1 . VAL D  1 14  ? 62.025 47.464  -18.245  1.00 4.72  ? 14   VAL E CG1 1 
ATOM   3435  C  CG2 . VAL D  1 14  ? 64.072 48.909  -18.650  1.00 4.91  ? 14   VAL E CG2 1 
ATOM   3436  N  N   . GLN D  1 15  ? 63.383 44.641  -16.929  1.00 5.73  ? 15   GLN E N   1 
ATOM   3437  C  CA  . GLN D  1 15  ? 62.801 43.320  -16.711  1.00 6.59  ? 15   GLN E CA  1 
ATOM   3438  C  C   . GLN D  1 15  ? 61.625 43.464  -15.746  1.00 6.44  ? 15   GLN E C   1 
ATOM   3439  O  O   . GLN D  1 15  ? 61.738 44.100  -14.697  1.00 6.31  ? 15   GLN E O   1 
ATOM   3440  C  CB  . GLN D  1 15  ? 63.853 42.381  -16.107  1.00 7.68  ? 15   GLN E CB  1 
ATOM   3441  C  CG  . GLN D  1 15  ? 65.068 42.096  -17.010  1.00 10.55 ? 15   GLN E CG  1 
ATOM   3442  C  CD  . GLN D  1 15  ? 66.027 41.102  -16.375  1.00 16.02 ? 15   GLN E CD  1 
ATOM   3443  O  OE1 . GLN D  1 15  ? 67.045 41.467  -15.763  1.00 17.12 ? 15   GLN E OE1 1 
ATOM   3444  N  NE2 . GLN D  1 15  ? 65.686 39.841  -16.488  1.00 16.93 ? 15   GLN E NE2 1 
ATOM   3445  N  N   . GLY D  1 16  ? 60.494 42.864  -16.083  1.00 6.55  ? 16   GLY E N   1 
ATOM   3446  C  CA  . GLY D  1 16  ? 59.369 42.827  -15.124  1.00 4.65  ? 16   GLY E CA  1 
ATOM   3447  C  C   . GLY D  1 16  ? 58.400 41.671  -15.289  1.00 4.75  ? 16   GLY E C   1 
ATOM   3448  O  O   . GLY D  1 16  ? 58.444 40.927  -16.282  1.00 2.71  ? 16   GLY E O   1 
ATOM   3449  N  N   . ILE D  1 17  ? 57.517 41.514  -14.300  1.00 4.46  ? 17   ILE E N   1 
ATOM   3450  C  CA  . ILE D  1 17  ? 56.397 40.582  -14.410  1.00 4.21  ? 17   ILE E CA  1 
ATOM   3451  C  C   . ILE D  1 17  ? 55.138 41.344  -14.002  1.00 4.29  ? 17   ILE E C   1 
ATOM   3452  O  O   . ILE D  1 17  ? 55.073 41.900  -12.904  1.00 3.59  ? 17   ILE E O   1 
ATOM   3453  C  CB  . ILE D  1 17  ? 56.596 39.329  -13.543  1.00 5.32  ? 17   ILE E CB  1 
ATOM   3454  C  CG1 . ILE D  1 17  ? 57.781 38.474  -14.073  1.00 6.40  ? 17   ILE E CG1 1 
ATOM   3455  C  CG2 . ILE D  1 17  ? 55.312 38.472  -13.487  1.00 4.79  ? 17   ILE E CG2 1 
ATOM   3456  C  CD1 . ILE D  1 17  ? 58.083 37.236  -13.213  1.00 10.34 ? 17   ILE E CD1 1 
ATOM   3457  N  N   . ILE D  1 18  ? 54.143 41.337  -14.883  1.00 3.89  ? 18   ILE E N   1 
ATOM   3458  C  CA  . ILE D  1 18  ? 52.874 42.019  -14.628  1.00 3.67  ? 18   ILE E CA  1 
ATOM   3459  C  C   . ILE D  1 18  ? 51.724 41.015  -14.676  1.00 3.88  ? 18   ILE E C   1 
ATOM   3460  O  O   . ILE D  1 18  ? 51.605 40.230  -15.633  1.00 3.93  ? 18   ILE E O   1 
ATOM   3461  C  CB  . ILE D  1 18  ? 52.652 43.170  -15.660  1.00 4.58  ? 18   ILE E CB  1 
ATOM   3462  C  CG1 . ILE D  1 18  ? 53.825 44.166  -15.624  1.00 4.93  ? 18   ILE E CG1 1 
ATOM   3463  C  CG2 . ILE D  1 18  ? 51.267 43.858  -15.480  1.00 3.92  ? 18   ILE E CG2 1 
ATOM   3464  C  CD1 . ILE D  1 18  ? 53.950 44.999  -14.309  1.00 5.70  ? 18   ILE E CD1 1 
ATOM   3465  N  N   . ASN D  1 19  ? 50.898 41.045  -13.623  1.00 2.64  ? 19   ASN E N   1 
ATOM   3466  C  CA  . ASN D  1 19  ? 49.748 40.184  -13.458  1.00 2.86  ? 19   ASN E CA  1 
ATOM   3467  C  C   . ASN D  1 19  ? 48.476 40.944  -13.760  1.00 2.90  ? 19   ASN E C   1 
ATOM   3468  O  O   . ASN D  1 19  ? 48.418 42.157  -13.508  1.00 2.00  ? 19   ASN E O   1 
ATOM   3469  C  CB  . ASN D  1 19  ? 49.709 39.708  -12.004  1.00 2.85  ? 19   ASN E CB  1 
ATOM   3470  C  CG  . ASN D  1 19  ? 50.941 38.930  -11.628  1.00 5.47  ? 19   ASN E CG  1 
ATOM   3471  O  OD1 . ASN D  1 19  ? 51.129 37.806  -12.088  1.00 7.05  ? 19   ASN E OD1 1 
ATOM   3472  N  ND2 . ASN D  1 19  ? 51.806 39.531  -10.769  1.00 4.72  ? 19   ASN E ND2 1 
ATOM   3473  N  N   . PHE D  1 20  ? 47.468 40.243  -14.294  1.00 2.06  ? 20   PHE E N   1 
ATOM   3474  C  CA  . PHE D  1 20  ? 46.141 40.810  -14.562  1.00 2.00  ? 20   PHE E CA  1 
ATOM   3475  C  C   . PHE D  1 20  ? 45.077 39.908  -13.949  1.00 3.03  ? 20   PHE E C   1 
ATOM   3476  O  O   . PHE D  1 20  ? 45.169 38.678  -14.051  1.00 2.56  ? 20   PHE E O   1 
ATOM   3477  C  CB  . PHE D  1 20  ? 45.848 40.906  -16.061  1.00 2.00  ? 20   PHE E CB  1 
ATOM   3478  C  CG  . PHE D  1 20  ? 46.819 41.715  -16.846  1.00 2.05  ? 20   PHE E CG  1 
ATOM   3479  C  CD1 . PHE D  1 20  ? 46.463 43.007  -17.290  1.00 2.00  ? 20   PHE E CD1 1 
ATOM   3480  C  CD2 . PHE D  1 20  ? 48.059 41.183  -17.209  1.00 2.00  ? 20   PHE E CD2 1 
ATOM   3481  C  CE1 . PHE D  1 20  ? 47.354 43.770  -18.044  1.00 6.72  ? 20   PHE E CE1 1 
ATOM   3482  C  CE2 . PHE D  1 20  ? 48.960 41.935  -17.972  1.00 3.22  ? 20   PHE E CE2 1 
ATOM   3483  C  CZ  . PHE D  1 20  ? 48.612 43.225  -18.391  1.00 4.05  ? 20   PHE E CZ  1 
ATOM   3484  N  N   . GLU D  1 21  ? 44.060 40.498  -13.321  1.00 2.86  ? 21   GLU E N   1 
ATOM   3485  C  CA  . GLU D  1 21  ? 42.979 39.678  -12.779  1.00 4.14  ? 21   GLU E CA  1 
ATOM   3486  C  C   . GLU D  1 21  ? 41.647 40.386  -12.981  1.00 3.61  ? 21   GLU E C   1 
ATOM   3487  O  O   . GLU D  1 21  ? 41.551 41.586  -12.784  1.00 4.14  ? 21   GLU E O   1 
ATOM   3488  C  CB  . GLU D  1 21  ? 43.205 39.317  -11.310  1.00 3.85  ? 21   GLU E CB  1 
ATOM   3489  C  CG  . GLU D  1 21  ? 42.182 38.267  -10.809  1.00 8.17  ? 21   GLU E CG  1 
ATOM   3490  C  CD  . GLU D  1 21  ? 42.544 37.568  -9.494   1.00 17.31 ? 21   GLU E CD  1 
ATOM   3491  O  OE1 . GLU D  1 21  ? 41.677 36.810  -9.017   1.00 21.98 ? 21   GLU E OE1 1 
ATOM   3492  O  OE2 . GLU D  1 21  ? 43.653 37.745  -8.929   1.00 19.41 ? 21   GLU E OE2 1 
ATOM   3493  N  N   . GLN D  1 22  ? 40.644 39.632  -13.420  1.00 3.49  ? 22   GLN E N   1 
ATOM   3494  C  CA  . GLN D  1 22  ? 39.319 40.200  -13.652  1.00 3.93  ? 22   GLN E CA  1 
ATOM   3495  C  C   . GLN D  1 22  ? 38.270 39.272  -13.067  1.00 4.82  ? 22   GLN E C   1 
ATOM   3496  O  O   . GLN D  1 22  ? 38.024 38.184  -13.594  1.00 5.72  ? 22   GLN E O   1 
ATOM   3497  C  CB  . GLN D  1 22  ? 39.086 40.405  -15.145  1.00 3.29  ? 22   GLN E CB  1 
ATOM   3498  C  CG  . GLN D  1 22  ? 37.818 41.196  -15.486  1.00 2.00  ? 22   GLN E CG  1 
ATOM   3499  C  CD  . GLN D  1 22  ? 37.660 41.379  -16.978  1.00 3.50  ? 22   GLN E CD  1 
ATOM   3500  O  OE1 . GLN D  1 22  ? 38.284 40.666  -17.754  1.00 3.28  ? 22   GLN E OE1 1 
ATOM   3501  N  NE2 . GLN D  1 22  ? 36.823 42.337  -17.393  1.00 2.16  ? 22   GLN E NE2 1 
ATOM   3502  N  N   . LYS D  1 23  ? 37.650 39.716  -11.987  1.00 6.97  ? 23   LYS E N   1 
ATOM   3503  C  CA  . LYS D  1 23  ? 36.698 38.881  -11.244  1.00 8.62  ? 23   LYS E CA  1 
ATOM   3504  C  C   . LYS D  1 23  ? 35.391 38.610  -12.010  1.00 8.42  ? 23   LYS E C   1 
ATOM   3505  O  O   . LYS D  1 23  ? 34.852 37.507  -11.956  1.00 9.03  ? 23   LYS E O   1 
ATOM   3506  C  CB  . LYS D  1 23  ? 36.446 39.478  -9.860   1.00 10.03 ? 23   LYS E CB  1 
ATOM   3507  C  CG  . LYS D  1 23  ? 37.703 39.458  -8.986   1.00 15.29 ? 23   LYS E CG  1 
ATOM   3508  C  CD  . LYS D  1 23  ? 37.370 39.565  -7.496   1.00 22.55 ? 23   LYS E CD  1 
ATOM   3509  C  CE  . LYS D  1 23  ? 38.638 39.528  -6.654   1.00 26.27 ? 23   LYS E CE  1 
ATOM   3510  N  NZ  . LYS D  1 23  ? 39.251 38.157  -6.640   1.00 29.24 ? 23   LYS E NZ  1 
ATOM   3511  N  N   . GLU D  1 24  ? 34.919 39.598  -12.755  1.00 8.41  ? 24   GLU E N   1 
ATOM   3512  C  CA  . GLU D  1 24  ? 33.686 39.469  -13.528  1.00 8.20  ? 24   GLU E CA  1 
ATOM   3513  C  C   . GLU D  1 24  ? 33.939 39.968  -14.923  1.00 6.78  ? 24   GLU E C   1 
ATOM   3514  O  O   . GLU D  1 24  ? 34.695 40.928  -15.121  1.00 6.05  ? 24   GLU E O   1 
ATOM   3515  C  CB  . GLU D  1 24  ? 32.556 40.296  -12.900  1.00 8.39  ? 24   GLU E CB  1 
ATOM   3516  C  CG  . GLU D  1 24  ? 32.216 39.951  -11.445  1.00 11.34 ? 24   GLU E CG  1 
ATOM   3517  C  CD  . GLU D  1 24  ? 31.588 38.572  -11.276  1.00 16.94 ? 24   GLU E CD  1 
ATOM   3518  O  OE1 . GLU D  1 24  ? 31.227 37.914  -12.275  1.00 18.72 ? 24   GLU E OE1 1 
ATOM   3519  O  OE2 . GLU D  1 24  ? 31.444 38.150  -10.110  1.00 22.55 ? 24   GLU E OE2 1 
ATOM   3520  N  N   . SER D  1 25  ? 33.274 39.354  -15.895  1.00 5.95  ? 25   SER E N   1 
ATOM   3521  C  CA  . SER D  1 25  ? 33.512 39.699  -17.292  1.00 5.55  ? 25   SER E CA  1 
ATOM   3522  C  C   . SER D  1 25  ? 33.088 41.130  -17.593  1.00 4.98  ? 25   SER E C   1 
ATOM   3523  O  O   . SER D  1 25  ? 33.611 41.747  -18.524  1.00 4.72  ? 25   SER E O   1 
ATOM   3524  C  CB  . SER D  1 25  ? 32.789 38.709  -18.213  1.00 5.83  ? 25   SER E CB  1 
ATOM   3525  O  OG  . SER D  1 25  ? 31.378 38.789  -17.987  1.00 5.84  ? 25   SER E OG  1 
ATOM   3526  N  N   . ASN D  1 26  ? 32.162 41.671  -16.789  1.00 4.76  ? 26   ASN E N   1 
ATOM   3527  C  CA  . ASN D  1 26  ? 31.741 43.064  -16.965  1.00 5.60  ? 26   ASN E CA  1 
ATOM   3528  C  C   . ASN D  1 26  ? 32.273 43.968  -15.859  1.00 6.00  ? 26   ASN E C   1 
ATOM   3529  O  O   . ASN D  1 26  ? 31.756 45.079  -15.647  1.00 6.85  ? 26   ASN E O   1 
ATOM   3530  C  CB  . ASN D  1 26  ? 30.211 43.196  -17.104  1.00 5.30  ? 26   ASN E CB  1 
ATOM   3531  C  CG  . ASN D  1 26  ? 29.473 42.783  -15.867  1.00 6.63  ? 26   ASN E CG  1 
ATOM   3532  O  OD1 . ASN D  1 26  ? 29.935 41.942  -15.082  1.00 6.18  ? 26   ASN E OD1 1 
ATOM   3533  N  ND2 . ASN D  1 26  ? 28.290 43.372  -15.674  1.00 7.26  ? 26   ASN E ND2 1 
ATOM   3534  N  N   . GLY D  1 27  ? 33.306 43.470  -15.173  1.00 5.88  ? 27   GLY E N   1 
ATOM   3535  C  CA  . GLY D  1 27  ? 33.979 44.210  -14.117  1.00 4.78  ? 27   GLY E CA  1 
ATOM   3536  C  C   . GLY D  1 27  ? 35.369 44.708  -14.482  1.00 4.36  ? 27   GLY E C   1 
ATOM   3537  O  O   . GLY D  1 27  ? 35.859 44.503  -15.592  1.00 3.63  ? 27   GLY E O   1 
ATOM   3538  N  N   . PRO D  1 28  ? 36.006 45.410  -13.546  1.00 4.58  ? 28   PRO E N   1 
ATOM   3539  C  CA  . PRO D  1 28  ? 37.306 46.027  -13.814  1.00 4.65  ? 28   PRO E CA  1 
ATOM   3540  C  C   . PRO D  1 28  ? 38.421 45.008  -13.762  1.00 4.47  ? 28   PRO E C   1 
ATOM   3541  O  O   . PRO D  1 28  ? 38.247 43.906  -13.223  1.00 5.10  ? 28   PRO E O   1 
ATOM   3542  C  CB  . PRO D  1 28  ? 37.459 47.025  -12.660  1.00 5.27  ? 28   PRO E CB  1 
ATOM   3543  C  CG  . PRO D  1 28  ? 36.636 46.458  -11.566  1.00 6.25  ? 28   PRO E CG  1 
ATOM   3544  C  CD  . PRO D  1 28  ? 35.471 45.774  -12.221  1.00 5.45  ? 28   PRO E CD  1 
ATOM   3545  N  N   . VAL D  1 29  ? 39.572 45.396  -14.286  1.00 4.62  ? 29   VAL E N   1 
ATOM   3546  C  CA  . VAL D  1 29  ? 40.748 44.553  -14.263  1.00 3.90  ? 29   VAL E CA  1 
ATOM   3547  C  C   . VAL D  1 29  ? 41.777 45.161  -13.314  1.00 3.80  ? 29   VAL E C   1 
ATOM   3548  O  O   . VAL D  1 29  ? 42.041 46.359  -13.373  1.00 4.40  ? 29   VAL E O   1 
ATOM   3549  C  CB  . VAL D  1 29  ? 41.355 44.427  -15.675  1.00 3.69  ? 29   VAL E CB  1 
ATOM   3550  C  CG1 . VAL D  1 29  ? 42.637 43.575  -15.659  1.00 3.68  ? 29   VAL E CG1 1 
ATOM   3551  C  CG2 . VAL D  1 29  ? 40.319 43.909  -16.699  1.00 4.85  ? 29   VAL E CG2 1 
ATOM   3552  N  N   . LYS D  1 30  ? 42.311 44.335  -12.423  1.00 4.15  ? 30   LYS E N   1 
ATOM   3553  C  CA  . LYS D  1 30  ? 43.429 44.707  -11.564  1.00 5.02  ? 30   LYS E CA  1 
ATOM   3554  C  C   . LYS D  1 30  ? 44.710 44.304  -12.258  1.00 5.48  ? 30   LYS E C   1 
ATOM   3555  O  O   . LYS D  1 30  ? 44.821 43.168  -12.759  1.00 4.81  ? 30   LYS E O   1 
ATOM   3556  C  CB  . LYS D  1 30  ? 43.306 43.988  -10.217  1.00 5.87  ? 30   LYS E CB  1 
ATOM   3557  C  CG  . LYS D  1 30  ? 42.098 44.453  -9.418   1.00 7.11  ? 30   LYS E CG  1 
ATOM   3558  C  CD  . LYS D  1 30  ? 42.035 43.764  -8.041   1.00 11.75 ? 30   LYS E CD  1 
ATOM   3559  C  CE  . LYS D  1 30  ? 40.776 44.167  -7.308   1.00 15.04 ? 30   LYS E CE  1 
ATOM   3560  N  NZ  . LYS D  1 30  ? 40.714 43.539  -5.942   1.00 18.97 ? 30   LYS E NZ  1 
ATOM   3561  N  N   . VAL D  1 31  ? 45.682 45.216  -12.260  1.00 4.71  ? 31   VAL E N   1 
ATOM   3562  C  CA  . VAL D  1 31  ? 46.954 45.006  -12.925  1.00 4.68  ? 31   VAL E CA  1 
ATOM   3563  C  C   . VAL D  1 31  ? 48.037 45.322  -11.895  1.00 5.26  ? 31   VAL E C   1 
ATOM   3564  O  O   . VAL D  1 31  ? 48.070 46.443  -11.362  1.00 5.21  ? 31   VAL E O   1 
ATOM   3565  C  CB  . VAL D  1 31  ? 47.095 45.972  -14.139  1.00 5.22  ? 31   VAL E CB  1 
ATOM   3566  C  CG1 . VAL D  1 31  ? 48.421 45.760  -14.913  1.00 4.33  ? 31   VAL E CG1 1 
ATOM   3567  C  CG2 . VAL D  1 31  ? 45.884 45.844  -15.112  1.00 5.32  ? 31   VAL E CG2 1 
ATOM   3568  N  N   . TRP D  1 32  ? 48.920 44.361  -11.607  1.00 4.14  ? 32   TRP E N   1 
ATOM   3569  C  CA  . TRP D  1 32  ? 49.942 44.596  -10.579  1.00 4.25  ? 32   TRP E CA  1 
ATOM   3570  C  C   . TRP D  1 32  ? 51.220 43.816  -10.834  1.00 4.43  ? 32   TRP E C   1 
ATOM   3571  O  O   . TRP D  1 32  ? 51.169 42.727  -11.407  1.00 4.89  ? 32   TRP E O   1 
ATOM   3572  C  CB  . TRP D  1 32  ? 49.409 44.209  -9.164   1.00 3.86  ? 32   TRP E CB  1 
ATOM   3573  C  CG  . TRP D  1 32  ? 49.336 42.730  -8.878   1.00 6.91  ? 32   TRP E CG  1 
ATOM   3574  C  CD1 . TRP D  1 32  ? 50.239 41.978  -8.165   1.00 6.47  ? 32   TRP E CD1 1 
ATOM   3575  C  CD2 . TRP D  1 32  ? 48.299 41.833  -9.276   1.00 7.35  ? 32   TRP E CD2 1 
ATOM   3576  N  NE1 . TRP D  1 32  ? 49.817 40.665  -8.107   1.00 10.57 ? 32   TRP E NE1 1 
ATOM   3577  C  CE2 . TRP D  1 32  ? 48.635 40.554  -8.783   1.00 9.68  ? 32   TRP E CE2 1 
ATOM   3578  C  CE3 . TRP D  1 32  ? 47.136 41.981  -10.026  1.00 9.96  ? 32   TRP E CE3 1 
ATOM   3579  C  CZ2 . TRP D  1 32  ? 47.843 39.433  -9.001   1.00 10.62 ? 32   TRP E CZ2 1 
ATOM   3580  C  CZ3 . TRP D  1 32  ? 46.333 40.846  -10.253  1.00 12.56 ? 32   TRP E CZ3 1 
ATOM   3581  C  CH2 . TRP D  1 32  ? 46.699 39.590  -9.732   1.00 10.36 ? 32   TRP E CH2 1 
ATOM   3582  N  N   . GLY D  1 33  ? 52.345 44.338  -10.345  1.00 3.55  ? 33   GLY E N   1 
ATOM   3583  C  CA  . GLY D  1 33  ? 53.603 43.597  -10.363  1.00 5.43  ? 33   GLY E CA  1 
ATOM   3584  C  C   . GLY D  1 33  ? 54.777 44.526  -10.145  1.00 5.40  ? 33   GLY E C   1 
ATOM   3585  O  O   . GLY D  1 33  ? 54.637 45.580  -9.545   1.00 5.93  ? 33   GLY E O   1 
ATOM   3586  N  N   . SER D  1 34  ? 55.932 44.146  -10.660  1.00 6.32  ? 34   SER E N   1 
ATOM   3587  C  CA  . SER D  1 34  ? 57.128 44.935  -10.446  1.00 7.48  ? 34   SER E CA  1 
ATOM   3588  C  C   . SER D  1 34  ? 57.947 44.970  -11.735  1.00 7.27  ? 34   SER E C   1 
ATOM   3589  O  O   . SER D  1 34  ? 57.943 44.001  -12.496  1.00 7.89  ? 34   SER E O   1 
ATOM   3590  C  CB  . SER D  1 34  ? 57.918 44.329  -9.287   1.00 8.52  ? 34   SER E CB  1 
ATOM   3591  O  OG  . SER D  1 34  ? 59.148 45.001  -9.111   1.00 11.63 ? 34   SER E OG  1 
ATOM   3592  N  N   . ILE D  1 35  ? 58.581 46.105  -12.015  1.00 6.74  ? 35   ILE E N   1 
ATOM   3593  C  CA  . ILE D  1 35  ? 59.459 46.236  -13.167  1.00 6.44  ? 35   ILE E CA  1 
ATOM   3594  C  C   . ILE D  1 35  ? 60.756 46.823  -12.639  1.00 6.94  ? 35   ILE E C   1 
ATOM   3595  O  O   . ILE D  1 35  ? 60.734 47.843  -11.965  1.00 7.84  ? 35   ILE E O   1 
ATOM   3596  C  CB  . ILE D  1 35  ? 58.884 47.183  -14.249  1.00 5.78  ? 35   ILE E CB  1 
ATOM   3597  C  CG1 . ILE D  1 35  ? 57.444 46.761  -14.658  1.00 4.60  ? 35   ILE E CG1 1 
ATOM   3598  C  CG2 . ILE D  1 35  ? 59.813 47.200  -15.482  1.00 5.94  ? 35   ILE E CG2 1 
ATOM   3599  C  CD1 . ILE D  1 35  ? 56.835 47.653  -15.727  1.00 7.44  ? 35   ILE E CD1 1 
ATOM   3600  N  N   . LYS D  1 36  ? 61.878 46.192  -12.954  1.00 7.44  ? 36   LYS E N   1 
ATOM   3601  C  CA  . LYS D  1 36  ? 63.172 46.743  -12.511  1.00 7.54  ? 36   LYS E CA  1 
ATOM   3602  C  C   . LYS D  1 36  ? 64.026 47.152  -13.709  1.00 7.89  ? 36   LYS E C   1 
ATOM   3603  O  O   . LYS D  1 36  ? 63.653 46.918  -14.857  1.00 6.91  ? 36   LYS E O   1 
ATOM   3604  C  CB  . LYS D  1 36  ? 63.904 45.732  -11.636  1.00 7.59  ? 36   LYS E CB  1 
ATOM   3605  C  CG  . LYS D  1 36  ? 64.495 44.545  -12.421  1.00 8.20  ? 36   LYS E CG  1 
ATOM   3606  C  CD  . LYS D  1 36  ? 65.071 43.466  -11.502  1.00 10.33 ? 36   LYS E CD  1 
ATOM   3607  C  CE  . LYS D  1 36  ? 65.634 42.299  -12.337  1.00 14.98 ? 36   LYS E CE  1 
ATOM   3608  N  NZ  . LYS D  1 36  ? 66.071 41.168  -11.473  1.00 15.41 ? 36   LYS E NZ  1 
ATOM   3609  N  N   . GLY D  1 37  ? 65.194 47.748  -13.442  1.00 8.39  ? 37   GLY E N   1 
ATOM   3610  C  CA  . GLY D  1 37  ? 66.102 48.126  -14.513  1.00 8.51  ? 37   GLY E CA  1 
ATOM   3611  C  C   . GLY D  1 37  ? 65.763 49.457  -15.153  1.00 8.96  ? 37   GLY E C   1 
ATOM   3612  O  O   . GLY D  1 37  ? 66.322 49.816  -16.207  1.00 8.81  ? 37   GLY E O   1 
ATOM   3613  N  N   . LEU D  1 38  ? 64.869 50.207  -14.513  1.00 9.07  ? 38   LEU E N   1 
ATOM   3614  C  CA  . LEU D  1 38  ? 64.354 51.454  -15.087  1.00 8.85  ? 38   LEU E CA  1 
ATOM   3615  C  C   . LEU D  1 38  ? 65.085 52.675  -14.523  1.00 9.64  ? 38   LEU E C   1 
ATOM   3616  O  O   . LEU D  1 38  ? 65.654 52.592  -13.437  1.00 10.48 ? 38   LEU E O   1 
ATOM   3617  C  CB  . LEU D  1 38  ? 62.857 51.611  -14.782  1.00 8.71  ? 38   LEU E CB  1 
ATOM   3618  C  CG  . LEU D  1 38  ? 61.815 50.766  -15.538  1.00 7.20  ? 38   LEU E CG  1 
ATOM   3619  C  CD1 . LEU D  1 38  ? 60.496 50.745  -14.702  1.00 5.81  ? 38   LEU E CD1 1 
ATOM   3620  C  CD2 . LEU D  1 38  ? 61.540 51.351  -16.913  1.00 5.43  ? 38   LEU E CD2 1 
ATOM   3621  N  N   . THR D  1 39  ? 65.052 53.786  -15.258  1.00 9.78  ? 39   THR E N   1 
ATOM   3622  C  CA  . THR D  1 39  ? 65.494 55.083  -14.723  1.00 10.65 ? 39   THR E CA  1 
ATOM   3623  C  C   . THR D  1 39  ? 64.436 55.635  -13.768  1.00 11.12 ? 39   THR E C   1 
ATOM   3624  O  O   . THR D  1 39  ? 63.223 55.421  -13.936  1.00 10.38 ? 39   THR E O   1 
ATOM   3625  C  CB  . THR D  1 39  ? 65.822 56.135  -15.825  1.00 10.78 ? 39   THR E CB  1 
ATOM   3626  O  OG1 . THR D  1 39  ? 64.676 56.367  -16.650  1.00 9.51  ? 39   THR E OG1 1 
ATOM   3627  C  CG2 . THR D  1 39  ? 67.013 55.689  -16.697  1.00 10.33 ? 39   THR E CG2 1 
ATOM   3628  N  N   . GLU D  1 40  ? 64.897 56.348  -12.747  1.00 10.85 ? 40   GLU E N   1 
ATOM   3629  C  CA  . GLU D  1 40  ? 63.985 56.943  -11.785  1.00 11.17 ? 40   GLU E CA  1 
ATOM   3630  C  C   . GLU D  1 40  ? 62.947 57.812  -12.487  1.00 10.79 ? 40   GLU E C   1 
ATOM   3631  O  O   . GLU D  1 40  ? 63.288 58.574  -13.404  1.00 11.12 ? 40   GLU E O   1 
ATOM   3632  C  CB  . GLU D  1 40  ? 64.767 57.789  -10.791  1.00 11.65 ? 40   GLU E CB  1 
ATOM   3633  C  CG  . GLU D  1 40  ? 63.924 58.304  -9.651   1.00 12.74 ? 40   GLU E CG  1 
ATOM   3634  C  CD  . GLU D  1 40  ? 64.766 59.019  -8.617   1.00 17.12 ? 40   GLU E CD  1 
ATOM   3635  O  OE1 . GLU D  1 40  ? 64.194 59.442  -7.585   1.00 19.40 ? 40   GLU E OE1 1 
ATOM   3636  O  OE2 . GLU D  1 40  ? 65.994 59.148  -8.845   1.00 17.85 ? 40   GLU E OE2 1 
ATOM   3637  N  N   . GLY D  1 41  ? 61.682 57.670  -12.083  1.00 10.59 ? 41   GLY E N   1 
ATOM   3638  C  CA  . GLY D  1 41  ? 60.631 58.571  -12.557  1.00 10.16 ? 41   GLY E CA  1 
ATOM   3639  C  C   . GLY D  1 41  ? 59.563 57.855  -13.375  1.00 9.91  ? 41   GLY E C   1 
ATOM   3640  O  O   . GLY D  1 41  ? 59.429 56.634  -13.293  1.00 8.89  ? 41   GLY E O   1 
ATOM   3641  N  N   . LEU D  1 42  ? 58.834 58.626  -14.177  1.00 9.74  ? 42   LEU E N   1 
ATOM   3642  C  CA  . LEU D  1 42  ? 57.616 58.156  -14.861  1.00 10.30 ? 42   LEU E CA  1 
ATOM   3643  C  C   . LEU D  1 42  ? 57.911 57.530  -16.212  1.00 9.72  ? 42   LEU E C   1 
ATOM   3644  O  O   . LEU D  1 42  ? 58.684 58.071  -17.002  1.00 9.62  ? 42   LEU E O   1 
ATOM   3645  C  CB  . LEU D  1 42  ? 56.620 59.311  -15.053  1.00 11.08 ? 42   LEU E CB  1 
ATOM   3646  C  CG  . LEU D  1 42  ? 55.898 59.921  -13.852  1.00 12.95 ? 42   LEU E CG  1 
ATOM   3647  C  CD1 . LEU D  1 42  ? 55.022 61.073  -14.320  1.00 15.46 ? 42   LEU E CD1 1 
ATOM   3648  C  CD2 . LEU D  1 42  ? 55.058 58.882  -13.144  1.00 16.18 ? 42   LEU E CD2 1 
ATOM   3649  N  N   . HIS D  1 43  ? 57.247 56.405  -16.481  1.00 9.00  ? 43   HIS E N   1 
ATOM   3650  C  CA  . HIS D  1 43  ? 57.432 55.658  -17.719  1.00 8.28  ? 43   HIS E CA  1 
ATOM   3651  C  C   . HIS D  1 43  ? 56.078 55.270  -18.309  1.00 7.11  ? 43   HIS E C   1 
ATOM   3652  O  O   . HIS D  1 43  ? 55.288 54.663  -17.622  1.00 6.98  ? 43   HIS E O   1 
ATOM   3653  C  CB  . HIS D  1 43  ? 58.258 54.410  -17.418  1.00 8.08  ? 43   HIS E CB  1 
ATOM   3654  C  CG  . HIS D  1 43  ? 59.677 54.716  -17.032  1.00 8.75  ? 43   HIS E CG  1 
ATOM   3655  N  ND1 . HIS D  1 43  ? 60.666 54.926  -17.967  1.00 10.71 ? 43   HIS E ND1 1 
ATOM   3656  C  CD2 . HIS D  1 43  ? 60.266 54.865  -15.822  1.00 8.73  ? 43   HIS E CD2 1 
ATOM   3657  C  CE1 . HIS D  1 43  ? 61.807 55.191  -17.349  1.00 11.25 ? 43   HIS E CE1 1 
ATOM   3658  N  NE2 . HIS D  1 43  ? 61.591 55.154  -16.047  1.00 9.91  ? 43   HIS E NE2 1 
ATOM   3659  N  N   . GLY D  1 44  ? 55.826 55.627  -19.570  1.00 6.68  ? 44   GLY E N   1 
ATOM   3660  C  CA  . GLY D  1 44  ? 54.557 55.281  -20.259  1.00 6.04  ? 44   GLY E CA  1 
ATOM   3661  C  C   . GLY D  1 44  ? 54.331 53.770  -20.230  1.00 5.01  ? 44   GLY E C   1 
ATOM   3662  O  O   . GLY D  1 44  ? 55.277 53.006  -20.256  1.00 5.15  ? 44   GLY E O   1 
ATOM   3663  N  N   . PHE D  1 45  ? 53.068 53.338  -20.204  1.00 4.62  ? 45   PHE E N   1 
ATOM   3664  C  CA  . PHE D  1 45  ? 52.717 51.942  -19.942  1.00 3.23  ? 45   PHE E CA  1 
ATOM   3665  C  C   . PHE D  1 45  ? 51.426 51.674  -20.693  1.00 3.59  ? 45   PHE E C   1 
ATOM   3666  O  O   . PHE D  1 45  ? 50.354 52.178  -20.300  1.00 3.29  ? 45   PHE E O   1 
ATOM   3667  C  CB  . PHE D  1 45  ? 52.494 51.800  -18.438  1.00 3.66  ? 45   PHE E CB  1 
ATOM   3668  C  CG  . PHE D  1 45  ? 52.382 50.387  -17.923  1.00 2.88  ? 45   PHE E CG  1 
ATOM   3669  C  CD1 . PHE D  1 45  ? 53.459 49.513  -18.001  1.00 4.99  ? 45   PHE E CD1 1 
ATOM   3670  C  CD2 . PHE D  1 45  ? 51.231 49.983  -17.232  1.00 2.40  ? 45   PHE E CD2 1 
ATOM   3671  C  CE1 . PHE D  1 45  ? 53.394 48.244  -17.466  1.00 5.91  ? 45   PHE E CE1 1 
ATOM   3672  C  CE2 . PHE D  1 45  ? 51.146 48.687  -16.702  1.00 6.15  ? 45   PHE E CE2 1 
ATOM   3673  C  CZ  . PHE D  1 45  ? 52.252 47.820  -16.824  1.00 4.43  ? 45   PHE E CZ  1 
ATOM   3674  N  N   . HIS D  1 46  ? 51.509 50.940  -21.803  1.00 3.35  ? 46   HIS E N   1 
ATOM   3675  C  CA  . HIS D  1 46  ? 50.309 50.668  -22.622  1.00 3.65  ? 46   HIS E CA  1 
ATOM   3676  C  C   . HIS D  1 46  ? 50.212 49.248  -23.131  1.00 3.61  ? 46   HIS E C   1 
ATOM   3677  O  O   . HIS D  1 46  ? 51.217 48.570  -23.278  1.00 3.46  ? 46   HIS E O   1 
ATOM   3678  C  CB  . HIS D  1 46  ? 50.281 51.577  -23.856  1.00 4.02  ? 46   HIS E CB  1 
ATOM   3679  C  CG  . HIS D  1 46  ? 50.900 52.913  -23.620  1.00 4.26  ? 46   HIS E CG  1 
ATOM   3680  N  ND1 . HIS D  1 46  ? 52.118 53.269  -24.140  1.00 5.33  ? 46   HIS E ND1 1 
ATOM   3681  C  CD2 . HIS D  1 46  ? 50.462 53.979  -22.909  1.00 3.08  ? 46   HIS E CD2 1 
ATOM   3682  C  CE1 . HIS D  1 46  ? 52.406 54.506  -23.770  1.00 3.36  ? 46   HIS E CE1 1 
ATOM   3683  N  NE2 . HIS D  1 46  ? 51.426 54.947  -22.997  1.00 3.45  ? 46   HIS E NE2 1 
ATOM   3684  N  N   . VAL D  1 47  ? 48.987 48.813  -23.413  1.00 3.55  ? 47   VAL E N   1 
ATOM   3685  C  CA  . VAL D  1 47  ? 48.789 47.633  -24.239  1.00 2.90  ? 47   VAL E CA  1 
ATOM   3686  C  C   . VAL D  1 47  ? 48.836 48.057  -25.700  1.00 3.26  ? 47   VAL E C   1 
ATOM   3687  O  O   . VAL D  1 47  ? 48.100 48.970  -26.119  1.00 3.07  ? 47   VAL E O   1 
ATOM   3688  C  CB  . VAL D  1 47  ? 47.434 46.927  -23.925  1.00 2.81  ? 47   VAL E CB  1 
ATOM   3689  C  CG1 . VAL D  1 47  ? 47.332 45.652  -24.731  1.00 2.93  ? 47   VAL E CG1 1 
ATOM   3690  C  CG2 . VAL D  1 47  ? 47.315 46.630  -22.416  1.00 2.00  ? 47   VAL E CG2 1 
ATOM   3691  N  N   . HIS D  1 48  ? 49.704 47.408  -26.479  1.00 2.87  ? 48   HIS E N   1 
ATOM   3692  C  CA  . HIS D  1 48  ? 49.808 47.626  -27.918  1.00 3.94  ? 48   HIS E CA  1 
ATOM   3693  C  C   . HIS D  1 48  ? 49.070 46.534  -28.695  1.00 3.97  ? 48   HIS E C   1 
ATOM   3694  O  O   . HIS D  1 48  ? 48.767 45.474  -28.141  1.00 4.84  ? 48   HIS E O   1 
ATOM   3695  C  CB  . HIS D  1 48  ? 51.289 47.694  -28.358  1.00 3.90  ? 48   HIS E CB  1 
ATOM   3696  C  CG  . HIS D  1 48  ? 51.983 48.944  -27.914  1.00 4.54  ? 48   HIS E CG  1 
ATOM   3697  N  ND1 . HIS D  1 48  ? 52.627 49.798  -28.793  1.00 5.36  ? 48   HIS E ND1 1 
ATOM   3698  C  CD2 . HIS D  1 48  ? 52.110 49.500  -26.684  1.00 6.56  ? 48   HIS E CD2 1 
ATOM   3699  C  CE1 . HIS D  1 48  ? 53.153 50.801  -28.113  1.00 3.91  ? 48   HIS E CE1 1 
ATOM   3700  N  NE2 . HIS D  1 48  ? 52.838 50.653  -26.836  1.00 5.33  ? 48   HIS E NE2 1 
ATOM   3701  N  N   . GLU D  1 49  ? 48.782 46.818  -29.965  1.00 3.66  ? 49   GLU E N   1 
ATOM   3702  C  CA  . GLU D  1 49  ? 47.834 46.041  -30.762  1.00 4.84  ? 49   GLU E CA  1 
ATOM   3703  C  C   . GLU D  1 49  ? 48.238 44.574  -31.015  1.00 5.16  ? 49   GLU E C   1 
ATOM   3704  O  O   . GLU D  1 49  ? 47.397 43.655  -30.905  1.00 5.80  ? 49   GLU E O   1 
ATOM   3705  C  CB  . GLU D  1 49  ? 47.626 46.754  -32.099  1.00 4.77  ? 49   GLU E CB  1 
ATOM   3706  C  CG  . GLU D  1 49  ? 46.550 46.110  -32.995  1.00 5.59  ? 49   GLU E CG  1 
ATOM   3707  C  CD  . GLU D  1 49  ? 46.221 46.934  -34.220  1.00 7.45  ? 49   GLU E CD  1 
ATOM   3708  O  OE1 . GLU D  1 49  ? 45.272 46.540  -34.940  1.00 8.23  ? 49   GLU E OE1 1 
ATOM   3709  O  OE2 . GLU D  1 49  ? 46.919 47.947  -34.486  1.00 6.65  ? 49   GLU E OE2 1 
ATOM   3710  N  N   . PHE D  1 50  ? 49.508 44.351  -31.342  1.00 3.59  ? 50   PHE E N   1 
ATOM   3711  C  CA  . PHE D  1 50  ? 49.930 43.022  -31.799  1.00 3.99  ? 50   PHE E CA  1 
ATOM   3712  C  C   . PHE D  1 50  ? 50.843 42.321  -30.798  1.00 3.69  ? 50   PHE E C   1 
ATOM   3713  O  O   . PHE D  1 50  ? 51.726 42.959  -30.211  1.00 4.23  ? 50   PHE E O   1 
ATOM   3714  C  CB  . PHE D  1 50  ? 50.587 43.101  -33.177  1.00 3.64  ? 50   PHE E CB  1 
ATOM   3715  C  CG  . PHE D  1 50  ? 49.721 43.776  -34.221  1.00 5.06  ? 50   PHE E CG  1 
ATOM   3716  C  CD1 . PHE D  1 50  ? 48.487 43.236  -34.562  1.00 7.93  ? 50   PHE E CD1 1 
ATOM   3717  C  CD2 . PHE D  1 50  ? 50.140 44.955  -34.835  1.00 10.32 ? 50   PHE E CD2 1 
ATOM   3718  C  CE1 . PHE D  1 50  ? 47.669 43.853  -35.529  1.00 9.09  ? 50   PHE E CE1 1 
ATOM   3719  C  CE2 . PHE D  1 50  ? 49.324 45.583  -35.804  1.00 8.46  ? 50   PHE E CE2 1 
ATOM   3720  C  CZ  . PHE D  1 50  ? 48.100 45.031  -36.131  1.00 9.74  ? 50   PHE E CZ  1 
ATOM   3721  N  N   . GLY D  1 51  ? 50.594 41.030  -30.586  1.00 2.82  ? 51   GLY E N   1 
ATOM   3722  C  CA  . GLY D  1 51  ? 51.432 40.186  -29.730  1.00 3.35  ? 51   GLY E CA  1 
ATOM   3723  C  C   . GLY D  1 51  ? 52.568 39.640  -30.576  1.00 3.83  ? 51   GLY E C   1 
ATOM   3724  O  O   . GLY D  1 51  ? 52.820 38.449  -30.607  1.00 2.47  ? 51   GLY E O   1 
ATOM   3725  N  N   . ASP D  1 52  ? 53.265 40.541  -31.268  1.00 4.54  ? 52   ASP E N   1 
ATOM   3726  C  CA  . ASP D  1 52  ? 54.258 40.141  -32.269  1.00 4.46  ? 52   ASP E CA  1 
ATOM   3727  C  C   . ASP D  1 52  ? 55.593 40.717  -31.827  1.00 5.00  ? 52   ASP E C   1 
ATOM   3728  O  O   . ASP D  1 52  ? 55.770 41.931  -31.838  1.00 5.84  ? 52   ASP E O   1 
ATOM   3729  C  CB  . ASP D  1 52  ? 53.822 40.696  -33.651  1.00 4.39  ? 52   ASP E CB  1 
ATOM   3730  C  CG  . ASP D  1 52  ? 54.806 40.358  -34.789  1.00 5.48  ? 52   ASP E CG  1 
ATOM   3731  O  OD1 . ASP D  1 52  ? 54.380 40.457  -35.954  1.00 6.34  ? 52   ASP E OD1 1 
ATOM   3732  O  OD2 . ASP D  1 52  ? 55.997 40.047  -34.537  1.00 7.28  ? 52   ASP E OD2 1 
ATOM   3733  N  N   . ASN D  1 53  ? 56.509 39.846  -31.402  1.00 5.42  ? 53   ASN E N   1 
ATOM   3734  C  CA  . ASN D  1 53  ? 57.858 40.237  -30.928  1.00 5.94  ? 53   ASN E CA  1 
ATOM   3735  C  C   . ASN D  1 53  ? 58.963 39.815  -31.912  1.00 6.06  ? 53   ASN E C   1 
ATOM   3736  O  O   . ASN D  1 53  ? 60.144 39.745  -31.540  1.00 6.07  ? 53   ASN E O   1 
ATOM   3737  C  CB  . ASN D  1 53  ? 58.151 39.591  -29.552  1.00 7.18  ? 53   ASN E CB  1 
ATOM   3738  C  CG  . ASN D  1 53  ? 59.338 40.245  -28.805  1.00 9.61  ? 53   ASN E CG  1 
ATOM   3739  O  OD1 . ASN D  1 53  ? 60.257 39.557  -28.343  1.00 17.22 ? 53   ASN E OD1 1 
ATOM   3740  N  ND2 . ASN D  1 53  ? 59.312 41.558  -28.682  1.00 10.93 ? 53   ASN E ND2 1 
ATOM   3741  N  N   . THR D  1 54  ? 58.577 39.516  -33.149  1.00 6.03  ? 54   THR E N   1 
ATOM   3742  C  CA  . THR D  1 54  ? 59.530 39.116  -34.205  1.00 6.41  ? 54   THR E CA  1 
ATOM   3743  C  C   . THR D  1 54  ? 60.667 40.098  -34.475  1.00 7.43  ? 54   THR E C   1 
ATOM   3744  O  O   . THR D  1 54  ? 61.762 39.665  -34.794  1.00 7.87  ? 54   THR E O   1 
ATOM   3745  C  CB  . THR D  1 54  ? 58.838 38.784  -35.526  1.00 6.75  ? 54   THR E CB  1 
ATOM   3746  O  OG1 . THR D  1 54  ? 58.107 39.921  -35.999  1.00 6.26  ? 54   THR E OG1 1 
ATOM   3747  C  CG2 . THR D  1 54  ? 57.895 37.555  -35.352  1.00 5.88  ? 54   THR E CG2 1 
ATOM   3748  N  N   . ALA D  1 55  ? 60.396 41.395  -34.347  1.00 7.51  ? 55   ALA E N   1 
ATOM   3749  C  CA  . ALA D  1 55  ? 61.404 42.465  -34.476  1.00 9.45  ? 55   ALA E CA  1 
ATOM   3750  C  C   . ALA D  1 55  ? 61.526 43.233  -33.157  1.00 9.95  ? 55   ALA E C   1 
ATOM   3751  O  O   . ALA D  1 55  ? 61.734 44.461  -33.136  1.00 12.28 ? 55   ALA E O   1 
ATOM   3752  C  CB  . ALA D  1 55  ? 61.039 43.432  -35.632  1.00 9.11  ? 55   ALA E CB  1 
ATOM   3753  N  N   . GLY D  1 56  ? 61.404 42.510  -32.051  1.00 8.78  ? 56   GLY E N   1 
ATOM   3754  C  CA  . GLY D  1 56  ? 61.461 43.127  -30.730  1.00 7.73  ? 56   GLY E CA  1 
ATOM   3755  C  C   . GLY D  1 56  ? 60.175 43.883  -30.452  1.00 6.51  ? 56   GLY E C   1 
ATOM   3756  O  O   . GLY D  1 56  ? 59.125 43.596  -31.044  1.00 7.15  ? 56   GLY E O   1 
ATOM   3757  N  N   . CYS D  1 57  ? 60.242 44.861  -29.570  1.00 5.57  ? 57   CYS E N   1 
ATOM   3758  C  CA  . CYS D  1 57  ? 59.022 45.591  -29.195  1.00 4.91  ? 57   CYS E CA  1 
ATOM   3759  C  C   . CYS D  1 57  ? 58.419 46.441  -30.357  1.00 4.94  ? 57   CYS E C   1 
ATOM   3760  O  O   . CYS D  1 57  ? 57.252 46.808  -30.316  1.00 4.49  ? 57   CYS E O   1 
ATOM   3761  C  CB  . CYS D  1 57  ? 59.305 46.441  -27.956  0.40 2.84  ? 57   CYS E CB  1 
ATOM   3762  S  SG  . CYS D  1 57  ? 59.831 45.463  -26.532  0.40 2.00  ? 57   CYS E SG  1 
ATOM   3763  N  N   . THR D  1 58  ? 59.212 46.708  -31.401  1.00 5.35  ? 58   THR E N   1 
ATOM   3764  C  CA  . THR D  1 58  ? 58.746 47.480  -32.555  1.00 6.63  ? 58   THR E CA  1 
ATOM   3765  C  C   . THR D  1 58  ? 57.576 46.792  -33.272  1.00 6.23  ? 58   THR E C   1 
ATOM   3766  O  O   . THR D  1 58  ? 56.645 47.469  -33.730  1.00 6.09  ? 58   THR E O   1 
ATOM   3767  C  CB  . THR D  1 58  ? 59.886 47.774  -33.570  1.00 6.97  ? 58   THR E CB  1 
ATOM   3768  O  OG1 . THR D  1 58  ? 60.936 48.485  -32.895  1.00 10.83 ? 58   THR E OG1 1 
ATOM   3769  C  CG2 . THR D  1 58  ? 59.381 48.632  -34.695  1.00 9.17  ? 58   THR E CG2 1 
ATOM   3770  N  N   . SER D  1 59  ? 57.582 45.457  -33.314  1.00 4.81  ? 59   SER E N   1 
ATOM   3771  C  CA  . SER D  1 59  ? 56.553 44.750  -34.072  1.00 5.72  ? 59   SER E CA  1 
ATOM   3772  C  C   . SER D  1 59  ? 55.209 44.629  -33.351  1.00 4.88  ? 59   SER E C   1 
ATOM   3773  O  O   . SER D  1 59  ? 54.251 44.090  -33.908  1.00 4.60  ? 59   SER E O   1 
ATOM   3774  C  CB  . SER D  1 59  ? 57.041 43.385  -34.549  1.00 6.35  ? 59   SER E CB  1 
ATOM   3775  O  OG  . SER D  1 59  ? 57.816 42.784  -33.570  1.00 9.71  ? 59   SER E OG  1 
ATOM   3776  N  N   . ALA D  1 60  ? 55.144 45.141  -32.128  1.00 3.97  ? 60   ALA E N   1 
ATOM   3777  C  CA  . ALA D  1 60  ? 53.872 45.187  -31.412  1.00 3.38  ? 60   ALA E CA  1 
ATOM   3778  C  C   . ALA D  1 60  ? 52.927 46.242  -31.966  1.00 3.68  ? 60   ALA E C   1 
ATOM   3779  O  O   . ALA D  1 60  ? 51.728 46.236  -31.638  1.00 3.69  ? 60   ALA E O   1 
ATOM   3780  C  CB  . ALA D  1 60  ? 54.095 45.366  -29.922  1.00 2.56  ? 60   ALA E CB  1 
ATOM   3781  N  N   . GLY D  1 61  ? 53.427 47.116  -32.845  1.00 3.67  ? 61   GLY E N   1 
ATOM   3782  C  CA  . GLY D  1 61  ? 52.538 48.066  -33.520  1.00 5.10  ? 61   GLY E CA  1 
ATOM   3783  C  C   . GLY D  1 61  ? 52.115 49.187  -32.572  1.00 5.33  ? 61   GLY E C   1 
ATOM   3784  O  O   . GLY D  1 61  ? 52.792 49.427  -31.572  1.00 6.09  ? 61   GLY E O   1 
ATOM   3785  N  N   . PRO D  1 62  ? 51.001 49.877  -32.890  1.00 4.94  ? 62   PRO E N   1 
ATOM   3786  C  CA  . PRO D  1 62  ? 50.582 51.057  -32.148  1.00 4.93  ? 62   PRO E CA  1 
ATOM   3787  C  C   . PRO D  1 62  ? 49.770 50.671  -30.912  1.00 4.43  ? 62   PRO E C   1 
ATOM   3788  O  O   . PRO D  1 62  ? 49.575 49.473  -30.634  1.00 4.09  ? 62   PRO E O   1 
ATOM   3789  C  CB  . PRO D  1 62  ? 49.726 51.816  -33.170  1.00 5.20  ? 62   PRO E CB  1 
ATOM   3790  C  CG  . PRO D  1 62  ? 49.074 50.727  -34.009  1.00 6.10  ? 62   PRO E CG  1 
ATOM   3791  C  CD  . PRO D  1 62  ? 50.068 49.551  -33.996  1.00 5.23  ? 62   PRO E CD  1 
ATOM   3792  N  N   . HIS D  1 63  ? 49.268 51.663  -30.187  1.00 4.29  ? 63   HIS E N   1 
ATOM   3793  C  CA  . HIS D  1 63  ? 48.474 51.344  -29.025  1.00 3.99  ? 63   HIS E CA  1 
ATOM   3794  C  C   . HIS D  1 63  ? 47.208 50.624  -29.452  1.00 4.11  ? 63   HIS E C   1 
ATOM   3795  O  O   . HIS D  1 63  ? 46.643 50.889  -30.514  1.00 4.13  ? 63   HIS E O   1 
ATOM   3796  C  CB  . HIS D  1 63  ? 48.101 52.584  -28.256  1.00 3.58  ? 63   HIS E CB  1 
ATOM   3797  C  CG  . HIS D  1 63  ? 49.279 53.301  -27.704  1.00 3.74  ? 63   HIS E CG  1 
ATOM   3798  N  ND1 . HIS D  1 63  ? 49.163 54.381  -26.869  1.00 3.66  ? 63   HIS E ND1 1 
ATOM   3799  C  CD2 . HIS D  1 63  ? 50.602 53.059  -27.826  1.00 4.16  ? 63   HIS E CD2 1 
ATOM   3800  C  CE1 . HIS D  1 63  ? 50.367 54.815  -26.543  1.00 4.88  ? 63   HIS E CE1 1 
ATOM   3801  N  NE2 . HIS D  1 63  ? 51.257 54.034  -27.124  1.00 3.72  ? 63   HIS E NE2 1 
ATOM   3802  N  N   . PHE D  1 64  ? 46.771 49.722  -28.614  1.00 3.18  ? 64   PHE E N   1 
ATOM   3803  C  CA  . PHE D  1 64  ? 45.532 48.964  -28.897  1.00 3.73  ? 64   PHE E CA  1 
ATOM   3804  C  C   . PHE D  1 64  ? 44.336 49.929  -28.880  1.00 3.60  ? 64   PHE E C   1 
ATOM   3805  O  O   . PHE D  1 64  ? 44.053 50.541  -27.860  1.00 3.92  ? 64   PHE E O   1 
ATOM   3806  C  CB  . PHE D  1 64  ? 45.344 47.860  -27.862  1.00 3.52  ? 64   PHE E CB  1 
ATOM   3807  C  CG  . PHE D  1 64  ? 44.091 47.018  -28.088  1.00 5.55  ? 64   PHE E CG  1 
ATOM   3808  C  CD1 . PHE D  1 64  ? 43.266 46.688  -27.019  1.00 4.94  ? 64   PHE E CD1 1 
ATOM   3809  C  CD2 . PHE D  1 64  ? 43.752 46.569  -29.358  1.00 5.79  ? 64   PHE E CD2 1 
ATOM   3810  C  CE1 . PHE D  1 64  ? 42.109 45.901  -27.215  1.00 6.85  ? 64   PHE E CE1 1 
ATOM   3811  C  CE2 . PHE D  1 64  ? 42.613 45.780  -29.571  1.00 8.25  ? 64   PHE E CE2 1 
ATOM   3812  C  CZ  . PHE D  1 64  ? 41.790 45.441  -28.491  1.00 3.83  ? 64   PHE E CZ  1 
ATOM   3813  N  N   . ASN D  1 65  ? 43.658 50.064  -30.024  1.00 3.65  ? 65   ASN E N   1 
ATOM   3814  C  CA  . ASN D  1 65  ? 42.707 51.163  -30.230  1.00 3.37  ? 65   ASN E CA  1 
ATOM   3815  C  C   . ASN D  1 65  ? 41.517 50.701  -31.085  1.00 4.47  ? 65   ASN E C   1 
ATOM   3816  O  O   . ASN D  1 65  ? 41.288 51.235  -32.176  1.00 5.19  ? 65   ASN E O   1 
ATOM   3817  C  CB  . ASN D  1 65  ? 43.431 52.355  -30.890  1.00 3.44  ? 65   ASN E CB  1 
ATOM   3818  C  CG  . ASN D  1 65  ? 42.568 53.592  -30.975  1.00 4.80  ? 65   ASN E CG  1 
ATOM   3819  O  OD1 . ASN D  1 65  ? 41.621 53.765  -30.189  1.00 6.53  ? 65   ASN E OD1 1 
ATOM   3820  N  ND2 . ASN D  1 65  ? 42.888 54.465  -31.932  1.00 4.19  ? 65   ASN E ND2 1 
ATOM   3821  N  N   . PRO D  1 66  ? 40.760 49.696  -30.602  1.00 4.68  ? 66   PRO E N   1 
ATOM   3822  C  CA  . PRO D  1 66  ? 39.665 49.144  -31.406  1.00 5.70  ? 66   PRO E CA  1 
ATOM   3823  C  C   . PRO D  1 66  ? 38.501 50.117  -31.614  1.00 6.74  ? 66   PRO E C   1 
ATOM   3824  O  O   . PRO D  1 66  ? 37.722 49.944  -32.559  1.00 7.35  ? 66   PRO E O   1 
ATOM   3825  C  CB  . PRO D  1 66  ? 39.214 47.931  -30.610  1.00 4.91  ? 66   PRO E CB  1 
ATOM   3826  C  CG  . PRO D  1 66  ? 39.583 48.276  -29.153  1.00 5.66  ? 66   PRO E CG  1 
ATOM   3827  C  CD  . PRO D  1 66  ? 40.892 49.016  -29.296  1.00 4.63  ? 66   PRO E CD  1 
ATOM   3828  N  N   . LEU D  1 67  ? 38.392 51.133  -30.768  1.00 7.25  ? 67   LEU E N   1 
ATOM   3829  C  CA  . LEU D  1 67  ? 37.331 52.135  -30.949  1.00 8.45  ? 67   LEU E CA  1 
ATOM   3830  C  C   . LEU D  1 67  ? 37.769 53.373  -31.726  1.00 8.87  ? 67   LEU E C   1 
ATOM   3831  O  O   . LEU D  1 67  ? 36.972 54.288  -31.906  1.00 10.07 ? 67   LEU E O   1 
ATOM   3832  C  CB  . LEU D  1 67  ? 36.698 52.514  -29.607  1.00 8.23  ? 67   LEU E CB  1 
ATOM   3833  C  CG  . LEU D  1 67  ? 36.241 51.300  -28.768  1.00 10.06 ? 67   LEU E CG  1 
ATOM   3834  C  CD1 . LEU D  1 67  ? 35.620 51.765  -27.480  1.00 12.86 ? 67   LEU E CD1 1 
ATOM   3835  C  CD2 . LEU D  1 67  ? 35.281 50.401  -29.537  1.00 13.75 ? 67   LEU E CD2 1 
ATOM   3836  N  N   . SER D  1 68  ? 39.016 53.392  -32.203  1.00 8.54  ? 68   SER E N   1 
ATOM   3837  C  CA  . SER D  1 68  ? 39.539 54.475  -33.072  1.00 9.36  ? 68   SER E CA  1 
ATOM   3838  C  C   . SER D  1 68  ? 39.425 55.860  -32.446  1.00 9.06  ? 68   SER E C   1 
ATOM   3839  O  O   . SER D  1 68  ? 38.883 56.785  -33.066  1.00 10.10 ? 68   SER E O   1 
ATOM   3840  C  CB  . SER D  1 68  ? 38.871 54.471  -34.460  1.00 9.14  ? 68   SER E CB  1 
ATOM   3841  O  OG  . SER D  1 68  ? 38.887 53.179  -35.042  1.00 12.12 ? 68   SER E OG  1 
ATOM   3842  N  N   . ARG D  1 69  ? 39.917 55.982  -31.219  1.00 8.11  ? 69   ARG E N   1 
ATOM   3843  C  CA  . ARG D  1 69  ? 39.954 57.240  -30.474  1.00 9.24  ? 69   ARG E CA  1 
ATOM   3844  C  C   . ARG D  1 69  ? 41.376 57.804  -30.459  1.00 8.19  ? 69   ARG E C   1 
ATOM   3845  O  O   . ARG D  1 69  ? 42.325 57.174  -30.953  1.00 6.85  ? 69   ARG E O   1 
ATOM   3846  C  CB  . ARG D  1 69  ? 39.508 57.022  -29.029  1.00 9.21  ? 69   ARG E CB  1 
ATOM   3847  C  CG  . ARG D  1 69  ? 38.154 56.336  -28.875  1.00 14.57 ? 69   ARG E CG  1 
ATOM   3848  C  CD  . ARG D  1 69  ? 37.022 57.309  -28.671  1.00 20.77 ? 69   ARG E CD  1 
ATOM   3849  N  NE  . ARG D  1 69  ? 35.885 56.653  -28.007  1.00 25.33 ? 69   ARG E NE  1 
ATOM   3850  C  CZ  . ARG D  1 69  ? 34.806 56.191  -28.631  1.00 27.78 ? 69   ARG E CZ  1 
ATOM   3851  N  NH1 . ARG D  1 69  ? 33.831 55.619  -27.927  1.00 28.45 ? 69   ARG E NH1 1 
ATOM   3852  N  NH2 . ARG D  1 69  ? 34.690 56.300  -29.954  1.00 29.32 ? 69   ARG E NH2 1 
ATOM   3853  N  N   . LYS D  1 70  ? 41.511 58.993  -29.890  1.00 8.63  ? 70   LYS E N   1 
ATOM   3854  C  CA  . LYS D  1 70  ? 42.815 59.589  -29.675  1.00 8.63  ? 70   LYS E CA  1 
ATOM   3855  C  C   . LYS D  1 70  ? 43.411 59.144  -28.340  1.00 7.76  ? 70   LYS E C   1 
ATOM   3856  O  O   . LYS D  1 70  ? 42.701 58.662  -27.439  1.00 7.06  ? 70   LYS E O   1 
ATOM   3857  C  CB  . LYS D  1 70  ? 42.712 61.107  -29.742  1.00 9.82  ? 70   LYS E CB  1 
ATOM   3858  C  CG  . LYS D  1 70  ? 42.613 61.632  -31.168  1.00 13.58 ? 70   LYS E CG  1 
ATOM   3859  C  CD  . LYS D  1 70  ? 42.582 63.155  -31.181  1.00 19.36 ? 70   LYS E CD  1 
ATOM   3860  C  CE  . LYS D  1 70  ? 41.326 63.699  -30.518  1.00 23.85 ? 70   LYS E CE  1 
ATOM   3861  N  NZ  . LYS D  1 70  ? 41.316 65.200  -30.548  1.00 27.20 ? 70   LYS E NZ  1 
ATOM   3862  N  N   . HIS D  1 71  ? 44.723 59.290  -28.219  1.00 6.61  ? 71   HIS E N   1 
ATOM   3863  C  CA  . HIS D  1 71  ? 45.437 58.847  -27.013  1.00 5.72  ? 71   HIS E CA  1 
ATOM   3864  C  C   . HIS D  1 71  ? 45.018 59.689  -25.807  1.00 6.09  ? 71   HIS E C   1 
ATOM   3865  O  O   . HIS D  1 71  ? 44.763 60.878  -25.944  1.00 6.81  ? 71   HIS E O   1 
ATOM   3866  C  CB  . HIS D  1 71  ? 46.956 58.992  -27.236  1.00 5.36  ? 71   HIS E CB  1 
ATOM   3867  C  CG  . HIS D  1 71  ? 47.774 58.628  -26.040  1.00 5.16  ? 71   HIS E CG  1 
ATOM   3868  N  ND1 . HIS D  1 71  ? 48.092 57.327  -25.734  1.00 3.71  ? 71   HIS E ND1 1 
ATOM   3869  C  CD2 . HIS D  1 71  ? 48.351 59.391  -25.077  1.00 2.00  ? 71   HIS E CD2 1 
ATOM   3870  C  CE1 . HIS D  1 71  ? 48.802 57.294  -24.620  1.00 2.63  ? 71   HIS E CE1 1 
ATOM   3871  N  NE2 . HIS D  1 71  ? 48.985 58.535  -24.208  1.00 4.55  ? 71   HIS E NE2 1 
ATOM   3872  N  N   . GLY D  1 72  ? 44.926 59.059  -24.641  1.00 5.67  ? 72   GLY E N   1 
ATOM   3873  C  CA  . GLY D  1 72  ? 44.666 59.797  -23.406  1.00 5.73  ? 72   GLY E CA  1 
ATOM   3874  C  C   . GLY D  1 72  ? 45.338 59.137  -22.231  1.00 5.73  ? 72   GLY E C   1 
ATOM   3875  O  O   . GLY D  1 72  ? 46.066 58.155  -22.404  1.00 4.66  ? 72   GLY E O   1 
ATOM   3876  N  N   . GLY D  1 73  ? 45.099 59.690  -21.044  1.00 5.45  ? 73   GLY E N   1 
ATOM   3877  C  CA  . GLY D  1 73  ? 45.347 58.996  -19.794  1.00 5.79  ? 73   GLY E CA  1 
ATOM   3878  C  C   . GLY D  1 73  ? 44.224 57.993  -19.503  1.00 5.79  ? 73   GLY E C   1 
ATOM   3879  O  O   . GLY D  1 73  ? 43.152 58.035  -20.129  1.00 5.72  ? 73   GLY E O   1 
ATOM   3880  N  N   . PRO D  1 74  ? 44.464 57.071  -18.551  1.00 5.84  ? 74   PRO E N   1 
ATOM   3881  C  CA  . PRO D  1 74  ? 43.486 56.039  -18.224  1.00 6.67  ? 74   PRO E CA  1 
ATOM   3882  C  C   . PRO D  1 74  ? 42.163 56.601  -17.698  1.00 7.55  ? 74   PRO E C   1 
ATOM   3883  O  O   . PRO D  1 74  ? 41.121 55.999  -17.927  1.00 7.29  ? 74   PRO E O   1 
ATOM   3884  C  CB  . PRO D  1 74  ? 44.206 55.175  -17.164  1.00 6.31  ? 74   PRO E CB  1 
ATOM   3885  C  CG  . PRO D  1 74  ? 45.314 56.067  -16.629  1.00 7.39  ? 74   PRO E CG  1 
ATOM   3886  C  CD  . PRO D  1 74  ? 45.723 56.898  -17.808  1.00 6.10  ? 74   PRO E CD  1 
ATOM   3887  N  N   . LYS D  1 75  ? 42.198 57.773  -17.065  1.00 8.88  ? 75   LYS E N   1 
ATOM   3888  C  CA  . LYS D  1 75  ? 40.970 58.401  -16.552  1.00 11.01 ? 75   LYS E CA  1 
ATOM   3889  C  C   . LYS D  1 75  ? 40.213 59.247  -17.584  1.00 11.81 ? 75   LYS E C   1 
ATOM   3890  O  O   . LYS D  1 75  ? 39.082 59.687  -17.331  1.00 11.54 ? 75   LYS E O   1 
ATOM   3891  C  CB  . LYS D  1 75  ? 41.285 59.237  -15.307  1.00 11.11 ? 75   LYS E CB  1 
ATOM   3892  C  CG  . LYS D  1 75  ? 41.923 58.466  -14.181  1.00 13.54 ? 75   LYS E CG  1 
ATOM   3893  C  CD  . LYS D  1 75  ? 41.984 59.244  -12.872  1.00 20.51 ? 75   LYS E CD  1 
ATOM   3894  C  CE  . LYS D  1 75  ? 42.808 60.537  -13.005  1.00 22.00 ? 75   LYS E CE  1 
ATOM   3895  N  NZ  . LYS D  1 75  ? 43.027 61.172  -11.670  1.00 26.22 ? 75   LYS E NZ  1 
ATOM   3896  N  N   . ASP D  1 76  ? 40.820 59.480  -18.743  1.00 11.76 ? 76   ASP E N   1 
ATOM   3897  C  CA  . ASP D  1 76  ? 40.170 60.275  -19.782  1.00 13.22 ? 76   ASP E CA  1 
ATOM   3898  C  C   . ASP D  1 76  ? 39.067 59.517  -20.502  1.00 13.67 ? 76   ASP E C   1 
ATOM   3899  O  O   . ASP D  1 76  ? 39.197 58.320  -20.763  1.00 13.57 ? 76   ASP E O   1 
ATOM   3900  C  CB  . ASP D  1 76  ? 41.198 60.796  -20.782  1.00 13.13 ? 76   ASP E CB  1 
ATOM   3901  C  CG  . ASP D  1 76  ? 42.129 61.801  -20.150  1.00 16.46 ? 76   ASP E CG  1 
ATOM   3902  O  OD1 . ASP D  1 76  ? 43.347 61.747  -20.380  1.00 16.57 ? 76   ASP E OD1 1 
ATOM   3903  O  OD2 . ASP D  1 76  ? 41.621 62.597  -19.342  1.00 19.05 ? 76   ASP E OD2 1 
ATOM   3904  N  N   . GLU D  1 77  ? 37.991 60.226  -20.829  1.00 13.95 ? 77   GLU E N   1 
ATOM   3905  C  CA  . GLU D  1 77  ? 36.933 59.648  -21.637  1.00 14.25 ? 77   GLU E CA  1 
ATOM   3906  C  C   . GLU D  1 77  ? 37.481 59.336  -23.035  1.00 12.63 ? 77   GLU E C   1 
ATOM   3907  O  O   . GLU D  1 77  ? 37.127 58.328  -23.629  1.00 12.57 ? 77   GLU E O   1 
ATOM   3908  C  CB  . GLU D  1 77  ? 35.747 60.620  -21.733  1.00 15.74 ? 77   GLU E CB  1 
ATOM   3909  C  CG  . GLU D  1 77  ? 34.545 60.077  -22.532  1.00 20.76 ? 77   GLU E CG  1 
ATOM   3910  C  CD  . GLU D  1 77  ? 33.908 58.848  -21.897  1.00 27.33 ? 77   GLU E CD  1 
ATOM   3911  O  OE1 . GLU D  1 77  ? 33.111 59.016  -20.931  1.00 30.95 ? 77   GLU E OE1 1 
ATOM   3912  O  OE2 . GLU D  1 77  ? 34.195 57.714  -22.374  1.00 28.54 ? 77   GLU E OE2 1 
ATOM   3913  N  N   . GLU D  1 78  ? 38.349 60.201  -23.541  1.00 10.30 ? 78   GLU E N   1 
ATOM   3914  C  CA  . GLU D  1 78  ? 38.949 60.005  -24.866  1.00 9.28  ? 78   GLU E CA  1 
ATOM   3915  C  C   . GLU D  1 78  ? 40.315 59.337  -24.661  1.00 7.60  ? 78   GLU E C   1 
ATOM   3916  O  O   . GLU D  1 78  ? 41.266 59.962  -24.208  1.00 7.38  ? 78   GLU E O   1 
ATOM   3917  C  CB  . GLU D  1 78  ? 39.052 61.343  -25.613  1.00 9.88  ? 78   GLU E CB  1 
ATOM   3918  C  CG  . GLU D  1 78  ? 39.561 61.263  -27.072  1.00 12.42 ? 78   GLU E CG  1 
ATOM   3919  C  CD  . GLU D  1 78  ? 38.528 60.721  -28.051  1.00 16.63 ? 78   GLU E CD  1 
ATOM   3920  O  OE1 . GLU D  1 78  ? 38.924 60.407  -29.206  1.00 15.08 ? 78   GLU E OE1 1 
ATOM   3921  O  OE2 . GLU D  1 78  ? 37.325 60.609  -27.671  1.00 19.85 ? 78   GLU E OE2 1 
ATOM   3922  N  N   . ARG D  1 79  ? 40.374 58.042  -24.951  1.00 6.28  ? 79   ARG E N   1 
ATOM   3923  C  CA  . ARG D  1 79  ? 41.594 57.245  -24.781  1.00 4.79  ? 79   ARG E CA  1 
ATOM   3924  C  C   . ARG D  1 79  ? 41.527 56.021  -25.672  1.00 4.70  ? 79   ARG E C   1 
ATOM   3925  O  O   . ARG D  1 79  ? 40.446 55.595  -26.108  1.00 5.45  ? 79   ARG E O   1 
ATOM   3926  C  CB  . ARG D  1 79  ? 41.805 56.797  -23.315  1.00 4.76  ? 79   ARG E CB  1 
ATOM   3927  C  CG  . ARG D  1 79  ? 40.617 56.014  -22.705  1.00 5.82  ? 79   ARG E CG  1 
ATOM   3928  C  CD  . ARG D  1 79  ? 40.977 55.365  -21.388  1.00 7.00  ? 79   ARG E CD  1 
ATOM   3929  N  NE  . ARG D  1 79  ? 41.615 54.046  -21.545  1.00 5.07  ? 79   ARG E NE  1 
ATOM   3930  C  CZ  . ARG D  1 79  ? 41.830 53.207  -20.528  1.00 4.41  ? 79   ARG E CZ  1 
ATOM   3931  N  NH1 . ARG D  1 79  ? 42.380 52.009  -20.740  1.00 2.00  ? 79   ARG E NH1 1 
ATOM   3932  N  NH2 . ARG D  1 79  ? 41.477 53.541  -19.294  1.00 3.89  ? 79   ARG E NH2 1 
ATOM   3933  N  N   . HIS D  1 80  ? 42.704 55.453  -25.912  1.00 3.81  ? 80   HIS E N   1 
ATOM   3934  C  CA  . HIS D  1 80  ? 42.828 54.185  -26.549  1.00 3.09  ? 80   HIS E CA  1 
ATOM   3935  C  C   . HIS D  1 80  ? 42.487 53.142  -25.510  1.00 2.32  ? 80   HIS E C   1 
ATOM   3936  O  O   . HIS D  1 80  ? 42.756 53.358  -24.331  1.00 2.87  ? 80   HIS E O   1 
ATOM   3937  C  CB  . HIS D  1 80  ? 44.275 53.988  -26.943  1.00 3.55  ? 80   HIS E CB  1 
ATOM   3938  C  CG  . HIS D  1 80  ? 44.754 54.940  -27.992  1.00 2.87  ? 80   HIS E CG  1 
ATOM   3939  N  ND1 . HIS D  1 80  ? 46.062 55.365  -28.064  1.00 4.93  ? 80   HIS E ND1 1 
ATOM   3940  C  CD2 . HIS D  1 80  ? 44.110 55.530  -29.021  1.00 4.54  ? 80   HIS E CD2 1 
ATOM   3941  C  CE1 . HIS D  1 80  ? 46.207 56.165  -29.107  1.00 4.64  ? 80   HIS E CE1 1 
ATOM   3942  N  NE2 . HIS D  1 80  ? 45.035 56.288  -29.697  1.00 6.11  ? 80   HIS E NE2 1 
ATOM   3943  N  N   . VAL D  1 81  ? 41.937 52.006  -25.927  1.00 2.72  ? 81   VAL E N   1 
ATOM   3944  C  CA  . VAL D  1 81  ? 41.746 50.911  -24.939  1.00 2.09  ? 81   VAL E CA  1 
ATOM   3945  C  C   . VAL D  1 81  ? 43.048 50.660  -24.179  1.00 2.20  ? 81   VAL E C   1 
ATOM   3946  O  O   . VAL D  1 81  ? 43.045 50.433  -22.959  1.00 2.53  ? 81   VAL E O   1 
ATOM   3947  C  CB  . VAL D  1 81  ? 41.194 49.607  -25.586  1.00 2.48  ? 81   VAL E CB  1 
ATOM   3948  C  CG1 . VAL D  1 81  ? 41.255 48.426  -24.592  1.00 2.03  ? 81   VAL E CG1 1 
ATOM   3949  C  CG2 . VAL D  1 81  ? 39.729 49.807  -26.033  1.00 2.42  ? 81   VAL E CG2 1 
ATOM   3950  N  N   . GLY D  1 82  ? 44.174 50.669  -24.879  1.00 2.89  ? 82   GLY E N   1 
ATOM   3951  C  CA  . GLY D  1 82  ? 45.427 50.231  -24.244  1.00 3.58  ? 82   GLY E CA  1 
ATOM   3952  C  C   . GLY D  1 82  ? 46.128 51.254  -23.351  1.00 4.64  ? 82   GLY E C   1 
ATOM   3953  O  O   . GLY D  1 82  ? 47.200 50.978  -22.833  1.00 4.78  ? 82   GLY E O   1 
ATOM   3954  N  N   . ASP D  1 83  ? 45.532 52.436  -23.177  1.00 5.07  ? 83   ASP E N   1 
ATOM   3955  C  CA  . ASP D  1 83  ? 46.132 53.535  -22.412  1.00 5.55  ? 83   ASP E CA  1 
ATOM   3956  C  C   . ASP D  1 83  ? 46.121 53.398  -20.884  1.00 5.63  ? 83   ASP E C   1 
ATOM   3957  O  O   . ASP D  1 83  ? 45.127 53.727  -20.225  1.00 5.53  ? 83   ASP E O   1 
ATOM   3958  C  CB  . ASP D  1 83  ? 45.483 54.864  -22.829  1.00 5.56  ? 83   ASP E CB  1 
ATOM   3959  C  CG  . ASP D  1 83  ? 45.854 55.257  -24.232  1.00 6.21  ? 83   ASP E CG  1 
ATOM   3960  O  OD1 . ASP D  1 83  ? 46.767 54.598  -24.813  1.00 4.75  ? 83   ASP E OD1 1 
ATOM   3961  O  OD2 . ASP D  1 83  ? 45.259 56.216  -24.770  1.00 4.01  ? 83   ASP E OD2 1 
ATOM   3962  N  N   . LEU D  1 84  ? 47.233 52.912  -20.331  1.00 5.66  ? 84   LEU E N   1 
ATOM   3963  C  CA  . LEU D  1 84  ? 47.309 52.685  -18.891  1.00 5.51  ? 84   LEU E CA  1 
ATOM   3964  C  C   . LEU D  1 84  ? 48.184 53.715  -18.171  1.00 6.10  ? 84   LEU E C   1 
ATOM   3965  O  O   . LEU D  1 84  ? 48.564 53.519  -17.020  1.00 7.38  ? 84   LEU E O   1 
ATOM   3966  C  CB  . LEU D  1 84  ? 47.763 51.237  -18.592  1.00 5.47  ? 84   LEU E CB  1 
ATOM   3967  C  CG  . LEU D  1 84  ? 46.830 50.129  -19.099  1.00 4.86  ? 84   LEU E CG  1 
ATOM   3968  C  CD1 . LEU D  1 84  ? 47.374 48.748  -18.789  1.00 6.01  ? 84   LEU E CD1 1 
ATOM   3969  C  CD2 . LEU D  1 84  ? 45.410 50.305  -18.541  1.00 5.84  ? 84   LEU E CD2 1 
ATOM   3970  N  N   . GLY D  1 85  ? 48.500 54.809  -18.849  1.00 6.20  ? 85   GLY E N   1 
ATOM   3971  C  CA  . GLY D  1 85  ? 49.210 55.919  -18.213  1.00 6.75  ? 85   GLY E CA  1 
ATOM   3972  C  C   . GLY D  1 85  ? 50.670 55.652  -17.959  1.00 6.72  ? 85   GLY E C   1 
ATOM   3973  O  O   . GLY D  1 85  ? 51.384 55.142  -18.820  1.00 7.94  ? 85   GLY E O   1 
ATOM   3974  N  N   . ASN D  1 86  ? 51.106 56.015  -16.767  1.00 7.44  ? 86   ASN E N   1 
ATOM   3975  C  CA  . ASN D  1 86  ? 52.490 55.862  -16.345  1.00 8.21  ? 86   ASN E CA  1 
ATOM   3976  C  C   . ASN D  1 86  ? 52.653 54.983  -15.136  1.00 8.09  ? 86   ASN E C   1 
ATOM   3977  O  O   . ASN D  1 86  ? 51.778 54.925  -14.263  1.00 8.72  ? 86   ASN E O   1 
ATOM   3978  C  CB  . ASN D  1 86  ? 53.083 57.222  -15.967  1.00 8.21  ? 86   ASN E CB  1 
ATOM   3979  C  CG  . ASN D  1 86  ? 53.237 58.118  -17.144  1.00 8.04  ? 86   ASN E CG  1 
ATOM   3980  O  OD1 . ASN D  1 86  ? 54.041 57.851  -18.025  1.00 8.37  ? 86   ASN E OD1 1 
ATOM   3981  N  ND2 . ASN D  1 86  ? 52.473 59.218  -17.169  1.00 8.87  ? 86   ASN E ND2 1 
ATOM   3982  N  N   . VAL D  1 87  ? 53.798 54.316  -15.077  1.00 8.07  ? 87   VAL E N   1 
ATOM   3983  C  CA  . VAL D  1 87  ? 54.243 53.649  -13.862  1.00 8.66  ? 87   VAL E CA  1 
ATOM   3984  C  C   . VAL D  1 87  ? 55.448 54.450  -13.373  1.00 8.96  ? 87   VAL E C   1 
ATOM   3985  O  O   . VAL D  1 87  ? 56.096 55.121  -14.178  1.00 8.89  ? 87   VAL E O   1 
ATOM   3986  C  CB  . VAL D  1 87  ? 54.626 52.185  -14.100  1.00 9.10  ? 87   VAL E CB  1 
ATOM   3987  C  CG1 . VAL D  1 87  ? 53.363 51.359  -14.523  1.00 8.09  ? 87   VAL E CG1 1 
ATOM   3988  C  CG2 . VAL D  1 87  ? 55.766 52.051  -15.135  1.00 8.92  ? 87   VAL E CG2 1 
ATOM   3989  N  N   . THR D  1 88  ? 55.728 54.389  -12.073  1.00 9.72  ? 88   THR E N   1 
ATOM   3990  C  CA  . THR D  1 88  ? 56.794 55.226  -11.467  1.00 10.59 ? 88   THR E CA  1 
ATOM   3991  C  C   . THR D  1 88  ? 57.873 54.361  -10.876  1.00 10.61 ? 88   THR E C   1 
ATOM   3992  O  O   . THR D  1 88  ? 57.594 53.505  -10.025  1.00 11.13 ? 88   THR E O   1 
ATOM   3993  C  CB  . THR D  1 88  ? 56.240 56.158  -10.344  1.00 11.91 ? 88   THR E CB  1 
ATOM   3994  O  OG1 . THR D  1 88  ? 55.134 56.911  -10.848  1.00 11.76 ? 88   THR E OG1 1 
ATOM   3995  C  CG2 . THR D  1 88  ? 57.323 57.149  -9.851   1.00 11.24 ? 88   THR E CG2 1 
ATOM   3996  N  N   . ALA D  1 89  ? 59.101 54.565  -11.350  1.00 10.92 ? 89   ALA E N   1 
ATOM   3997  C  CA  . ALA D  1 89  ? 60.257 53.854  -10.817  1.00 10.92 ? 89   ALA E CA  1 
ATOM   3998  C  C   . ALA D  1 89  ? 60.927 54.702  -9.736   1.00 11.50 ? 89   ALA E C   1 
ATOM   3999  O  O   . ALA D  1 89  ? 60.981 55.945  -9.843   1.00 11.15 ? 89   ALA E O   1 
ATOM   4000  C  CB  . ALA D  1 89  ? 61.243 53.519  -11.932  1.00 10.57 ? 89   ALA E CB  1 
ATOM   4001  N  N   . ASP D  1 90  ? 61.388 54.032  -8.685   1.00 11.96 ? 90   ASP E N   1 
ATOM   4002  C  CA  . ASP D  1 90  ? 62.045 54.718  -7.576   1.00 12.78 ? 90   ASP E CA  1 
ATOM   4003  C  C   . ASP D  1 90  ? 63.518 54.960  -7.907   1.00 12.49 ? 90   ASP E C   1 
ATOM   4004  O  O   . ASP D  1 90  ? 63.990 54.608  -8.993   1.00 11.35 ? 90   ASP E O   1 
ATOM   4005  C  CB  . ASP D  1 90  ? 61.833 53.962  -6.252   1.00 13.36 ? 90   ASP E CB  1 
ATOM   4006  C  CG  . ASP D  1 90  ? 62.428 52.543  -6.240   1.00 14.09 ? 90   ASP E CG  1 
ATOM   4007  O  OD1 . ASP D  1 90  ? 61.977 51.772  -5.376   1.00 16.50 ? 90   ASP E OD1 1 
ATOM   4008  O  OD2 . ASP D  1 90  ? 63.334 52.181  -7.040   1.00 13.79 ? 90   ASP E OD2 1 
ATOM   4009  N  N   . LYS D  1 91  ? 64.254 55.536  -6.960   1.00 13.51 ? 91   LYS E N   1 
ATOM   4010  C  CA  . LYS D  1 91  ? 65.675 55.815  -7.141   1.00 14.26 ? 91   LYS E CA  1 
ATOM   4011  C  C   . LYS D  1 91  ? 66.485 54.552  -7.414   1.00 14.00 ? 91   LYS E C   1 
ATOM   4012  O  O   . LYS D  1 91  ? 67.562 54.599  -8.011   1.00 14.60 ? 91   LYS E O   1 
ATOM   4013  C  CB  . LYS D  1 91  ? 66.219 56.531  -5.885   1.00 14.73 ? 91   LYS E CB  1 
ATOM   4014  C  CG  . LYS D  1 91  ? 67.382 57.474  -6.178   1.00 17.97 ? 91   LYS E CG  1 
ATOM   4015  C  CD  . LYS D  1 91  ? 67.968 58.058  -4.891   1.00 20.32 ? 91   LYS E CD  1 
ATOM   4016  C  CE  . LYS D  1 91  ? 68.939 59.191  -5.205   1.00 22.12 ? 91   LYS E CE  1 
ATOM   4017  N  NZ  . LYS D  1 91  ? 69.241 60.027  -3.994   1.00 25.73 ? 91   LYS E NZ  1 
ATOM   4018  N  N   . ASP D  1 92  ? 65.978 53.411  -6.970   1.00 13.67 ? 92   ASP E N   1 
ATOM   4019  C  CA  . ASP D  1 92  ? 66.657 52.150  -7.238   1.00 13.92 ? 92   ASP E CA  1 
ATOM   4020  C  C   . ASP D  1 92  ? 66.255 51.520  -8.575   1.00 13.31 ? 92   ASP E C   1 
ATOM   4021  O  O   . ASP D  1 92  ? 66.698 50.427  -8.910   1.00 13.42 ? 92   ASP E O   1 
ATOM   4022  C  CB  . ASP D  1 92  ? 66.432 51.196  -6.083   1.00 14.65 ? 92   ASP E CB  1 
ATOM   4023  C  CG  . ASP D  1 92  ? 67.190 51.620  -4.846   1.00 16.80 ? 92   ASP E CG  1 
ATOM   4024  O  OD1 . ASP D  1 92  ? 68.378 51.990  -4.991   1.00 19.34 ? 92   ASP E OD1 1 
ATOM   4025  O  OD2 . ASP D  1 92  ? 66.597 51.595  -3.749   1.00 19.90 ? 92   ASP E OD2 1 
ATOM   4026  N  N   . GLY D  1 93  ? 65.433 52.230  -9.339   1.00 13.28 ? 93   GLY E N   1 
ATOM   4027  C  CA  . GLY D  1 93  ? 65.044 51.787  -10.683  1.00 12.65 ? 93   GLY E CA  1 
ATOM   4028  C  C   . GLY D  1 93  ? 63.937 50.740  -10.724  1.00 12.31 ? 93   GLY E C   1 
ATOM   4029  O  O   . GLY D  1 93  ? 63.759 50.053  -11.742  1.00 11.41 ? 93   GLY E O   1 
ATOM   4030  N  N   . VAL D  1 94  ? 63.188 50.635  -9.627   1.00 11.71 ? 94   VAL E N   1 
ATOM   4031  C  CA  . VAL D  1 94  ? 62.112 49.645  -9.498   1.00 11.64 ? 94   VAL E CA  1 
ATOM   4032  C  C   . VAL D  1 94  ? 60.762 50.335  -9.433   1.00 11.65 ? 94   VAL E C   1 
ATOM   4033  O  O   . VAL D  1 94  ? 60.561 51.271  -8.631   1.00 11.98 ? 94   VAL E O   1 
ATOM   4034  C  CB  . VAL D  1 94  ? 62.302 48.715  -8.263   1.00 10.96 ? 94   VAL E CB  1 
ATOM   4035  C  CG1 . VAL D  1 94  ? 61.204 47.621  -8.206   1.00 11.30 ? 94   VAL E CG1 1 
ATOM   4036  C  CG2 . VAL D  1 94  ? 63.679 48.082  -8.289   1.00 11.69 ? 94   VAL E CG2 1 
ATOM   4037  N  N   . ALA D  1 95  ? 59.861 49.885  -10.303  1.00 11.20 ? 95   ALA E N   1 
ATOM   4038  C  CA  . ALA D  1 95  ? 58.479 50.367  -10.348  1.00 11.75 ? 95   ALA E CA  1 
ATOM   4039  C  C   . ALA D  1 95  ? 57.569 49.324  -9.725   1.00 12.12 ? 95   ALA E C   1 
ATOM   4040  O  O   . ALA D  1 95  ? 57.540 48.180  -10.181  1.00 11.69 ? 95   ALA E O   1 
ATOM   4041  C  CB  . ALA D  1 95  ? 58.053 50.628  -11.787  1.00 10.95 ? 95   ALA E CB  1 
ATOM   4042  N  N   . ASP D  1 96  ? 56.833 49.707  -8.682   1.00 11.43 ? 96   ASP E N   1 
ATOM   4043  C  CA  . ASP D  1 96  ? 55.801 48.840  -8.124   1.00 11.83 ? 96   ASP E CA  1 
ATOM   4044  C  C   . ASP D  1 96  ? 54.540 49.200  -8.888   1.00 10.89 ? 96   ASP E C   1 
ATOM   4045  O  O   . ASP D  1 96  ? 54.069 50.343  -8.827   1.00 11.37 ? 96   ASP E O   1 
ATOM   4046  C  CB  . ASP D  1 96  ? 55.647 49.092  -6.611   1.00 12.96 ? 96   ASP E CB  1 
ATOM   4047  C  CG  . ASP D  1 96  ? 54.636 48.142  -5.913   1.00 16.88 ? 96   ASP E CG  1 
ATOM   4048  O  OD1 . ASP D  1 96  ? 53.763 47.525  -6.558   1.00 20.70 ? 96   ASP E OD1 1 
ATOM   4049  O  OD2 . ASP D  1 96  ? 54.712 48.024  -4.666   1.00 23.36 ? 96   ASP E OD2 1 
ATOM   4050  N  N   . VAL D  1 97  ? 54.000 48.248  -9.641   1.00 8.05  ? 97   VAL E N   1 
ATOM   4051  C  CA  . VAL D  1 97  ? 52.836 48.561  -10.466  1.00 6.79  ? 97   VAL E CA  1 
ATOM   4052  C  C   . VAL D  1 97  ? 51.596 48.096  -9.756   1.00 6.40  ? 97   VAL E C   1 
ATOM   4053  O  O   . VAL D  1 97  ? 51.542 46.953  -9.308   1.00 5.75  ? 97   VAL E O   1 
ATOM   4054  C  CB  . VAL D  1 97  ? 52.936 47.895  -11.850  1.00 6.31  ? 97   VAL E CB  1 
ATOM   4055  C  CG1 . VAL D  1 97  ? 51.655 48.157  -12.708  1.00 5.32  ? 97   VAL E CG1 1 
ATOM   4056  C  CG2 . VAL D  1 97  ? 54.189 48.400  -12.553  1.00 5.67  ? 97   VAL E CG2 1 
ATOM   4057  N  N   . SER D  1 98  ? 50.596 48.962  -9.705   1.00 6.04  ? 98   SER E N   1 
ATOM   4058  C  CA  . SER D  1 98  ? 49.320 48.632  -9.061   1.00 6.58  ? 98   SER E CA  1 
ATOM   4059  C  C   . SER D  1 98  ? 48.270 49.561  -9.651   1.00 7.13  ? 98   SER E C   1 
ATOM   4060  O  O   . SER D  1 98  ? 48.216 50.757  -9.319   1.00 6.65  ? 98   SER E O   1 
ATOM   4061  C  CB  . SER D  1 98  ? 49.399 48.786  -7.531   1.00 7.16  ? 98   SER E CB  1 
ATOM   4062  O  OG  . SER D  1 98  ? 48.165 48.404  -6.917   1.00 6.25  ? 98   SER E OG  1 
ATOM   4063  N  N   . ILE D  1 99  ? 47.440 48.993  -10.520  1.00 5.53  ? 99   ILE E N   1 
ATOM   4064  C  CA  . ILE D  1 99  ? 46.506 49.749  -11.357  1.00 6.34  ? 99   ILE E CA  1 
ATOM   4065  C  C   . ILE D  1 99  ? 45.174 49.027  -11.321  1.00 6.39  ? 99   ILE E C   1 
ATOM   4066  O  O   . ILE D  1 99  ? 45.143 47.800  -11.260  1.00 6.52  ? 99   ILE E O   1 
ATOM   4067  C  CB  . ILE D  1 99  ? 47.057 49.784  -12.839  1.00 5.94  ? 99   ILE E CB  1 
ATOM   4068  C  CG1 . ILE D  1 99  ? 48.288 50.701  -12.913  1.00 6.99  ? 99   ILE E CG1 1 
ATOM   4069  C  CG2 . ILE D  1 99  ? 45.979 50.204  -13.881  1.00 5.52  ? 99   ILE E CG2 1 
ATOM   4070  C  CD1 . ILE D  1 99  ? 49.107 50.491  -14.211  1.00 10.48 ? 99   ILE E CD1 1 
ATOM   4071  N  N   . GLU D  1 100 ? 44.071 49.763  -11.336  1.00 6.17  ? 100  GLU E N   1 
ATOM   4072  C  CA  . GLU D  1 100 ? 42.793 49.143  -11.645  1.00 6.93  ? 100  GLU E CA  1 
ATOM   4073  C  C   . GLU D  1 100 ? 42.172 49.893  -12.823  1.00 6.43  ? 100  GLU E C   1 
ATOM   4074  O  O   . GLU D  1 100 ? 42.207 51.117  -12.864  1.00 6.65  ? 100  GLU E O   1 
ATOM   4075  C  CB  . GLU D  1 100 ? 41.870 49.101  -10.409  1.00 7.91  ? 100  GLU E CB  1 
ATOM   4076  C  CG  . GLU D  1 100 ? 40.576 48.313  -10.656  1.00 11.26 ? 100  GLU E CG  1 
ATOM   4077  C  CD  . GLU D  1 100 ? 39.872 47.885  -9.370   1.00 16.44 ? 100  GLU E CD  1 
ATOM   4078  O  OE1 . GLU D  1 100 ? 40.190 48.408  -8.279   1.00 18.25 ? 100  GLU E OE1 1 
ATOM   4079  O  OE2 . GLU D  1 100 ? 39.003 47.000  -9.445   1.00 18.77 ? 100  GLU E OE2 1 
ATOM   4080  N  N   . ASP D  1 101 ? 41.639 49.164  -13.799  1.00 5.73  ? 101  ASP E N   1 
ATOM   4081  C  CA  . ASP D  1 101 ? 41.118 49.781  -15.016  1.00 5.08  ? 101  ASP E CA  1 
ATOM   4082  C  C   . ASP D  1 101 ? 39.809 49.121  -15.449  1.00 5.13  ? 101  ASP E C   1 
ATOM   4083  O  O   . ASP D  1 101 ? 39.680 47.898  -15.391  1.00 5.33  ? 101  ASP E O   1 
ATOM   4084  C  CB  . ASP D  1 101 ? 42.147 49.651  -16.145  1.00 5.73  ? 101  ASP E CB  1 
ATOM   4085  C  CG  . ASP D  1 101 ? 41.841 50.583  -17.326  1.00 5.55  ? 101  ASP E CG  1 
ATOM   4086  O  OD1 . ASP D  1 101 ? 41.276 50.100  -18.339  1.00 4.51  ? 101  ASP E OD1 1 
ATOM   4087  O  OD2 . ASP D  1 101 ? 42.154 51.794  -17.222  1.00 5.11  ? 101  ASP E OD2 1 
ATOM   4088  N  N   . SER D  1 102 ? 38.867 49.939  -15.913  1.00 5.32  ? 102  SER E N   1 
ATOM   4089  C  CA  . SER D  1 102 ? 37.523 49.491  -16.287  1.00 6.45  ? 102  SER E CA  1 
ATOM   4090  C  C   . SER D  1 102 ? 37.337 49.496  -17.794  1.00 4.98  ? 102  SER E C   1 
ATOM   4091  O  O   . SER D  1 102 ? 36.241 49.224  -18.285  1.00 5.65  ? 102  SER E O   1 
ATOM   4092  C  CB  . SER D  1 102 ? 36.485 50.454  -15.683  1.00 6.64  ? 102  SER E CB  1 
ATOM   4093  O  OG  . SER D  1 102 ? 36.389 50.205  -14.296  1.00 14.45 ? 102  SER E OG  1 
ATOM   4094  N  N   . VAL D  1 103 ? 38.394 49.814  -18.534  1.00 2.70  ? 103  VAL E N   1 
ATOM   4095  C  CA  . VAL D  1 103 ? 38.272 49.899  -19.987  1.00 3.55  ? 103  VAL E CA  1 
ATOM   4096  C  C   . VAL D  1 103 ? 38.846 48.670  -20.647  1.00 2.79  ? 103  VAL E C   1 
ATOM   4097  O  O   . VAL D  1 103 ? 38.214 48.086  -21.548  1.00 3.11  ? 103  VAL E O   1 
ATOM   4098  C  CB  . VAL D  1 103 ? 38.957 51.143  -20.582  1.00 2.59  ? 103  VAL E CB  1 
ATOM   4099  C  CG1 . VAL D  1 103 ? 39.038 50.997  -22.104  1.00 4.41  ? 103  VAL E CG1 1 
ATOM   4100  C  CG2 . VAL D  1 103 ? 38.217 52.430  -20.186  1.00 5.42  ? 103  VAL E CG2 1 
ATOM   4101  N  N   . ILE D  1 104 ? 40.044 48.272  -20.224  1.00 3.56  ? 104  ILE E N   1 
ATOM   4102  C  CA  . ILE D  1 104 ? 40.621 47.006  -20.713  1.00 3.30  ? 104  ILE E CA  1 
ATOM   4103  C  C   . ILE D  1 104 ? 39.809 45.817  -20.193  1.00 3.14  ? 104  ILE E C   1 
ATOM   4104  O  O   . ILE D  1 104 ? 39.171 45.897  -19.148  1.00 2.97  ? 104  ILE E O   1 
ATOM   4105  C  CB  . ILE D  1 104 ? 42.078 46.772  -20.240  1.00 2.70  ? 104  ILE E CB  1 
ATOM   4106  C  CG1 . ILE D  1 104 ? 42.190 46.804  -18.703  1.00 2.66  ? 104  ILE E CG1 1 
ATOM   4107  C  CG2 . ILE D  1 104 ? 43.078 47.715  -20.943  1.00 4.75  ? 104  ILE E CG2 1 
ATOM   4108  C  CD1 . ILE D  1 104 ? 43.581 46.492  -18.238  1.00 2.60  ? 104  ILE E CD1 1 
ATOM   4109  N  N   . SER D  1 105 ? 39.874 44.698  -20.904  1.00 3.33  ? 105  SER E N   1 
ATOM   4110  C  CA  . SER D  1 105 ? 39.205 43.477  -20.450  1.00 2.43  ? 105  SER E CA  1 
ATOM   4111  C  C   . SER D  1 105 ? 40.036 42.248  -20.835  1.00 2.59  ? 105  SER E C   1 
ATOM   4112  O  O   . SER D  1 105 ? 40.842 42.299  -21.754  1.00 2.78  ? 105  SER E O   1 
ATOM   4113  C  CB  . SER D  1 105 ? 37.790 43.371  -21.037  1.00 3.11  ? 105  SER E CB  1 
ATOM   4114  O  OG  . SER D  1 105 ? 37.055 42.311  -20.425  1.00 2.97  ? 105  SER E OG  1 
ATOM   4115  N  N   . LEU D  1 106 ? 39.842 41.164  -20.097  1.00 2.99  ? 106  LEU E N   1 
ATOM   4116  C  CA  . LEU D  1 106 ? 40.534 39.908  -20.340  1.00 3.42  ? 106  LEU E CA  1 
ATOM   4117  C  C   . LEU D  1 106 ? 39.633 38.937  -21.102  1.00 4.13  ? 106  LEU E C   1 
ATOM   4118  O  O   . LEU D  1 106 ? 39.991 37.785  -21.330  1.00 4.57  ? 106  LEU E O   1 
ATOM   4119  C  CB  . LEU D  1 106 ? 40.985 39.294  -19.011  1.00 3.34  ? 106  LEU E CB  1 
ATOM   4120  C  CG  . LEU D  1 106 ? 41.894 40.165  -18.109  1.00 2.38  ? 106  LEU E CG  1 
ATOM   4121  C  CD1 . LEU D  1 106 ? 42.336 39.414  -16.860  1.00 4.11  ? 106  LEU E CD1 1 
ATOM   4122  C  CD2 . LEU D  1 106 ? 43.152 40.633  -18.905  1.00 2.58  ? 106  LEU E CD2 1 
ATOM   4123  N  N   . SER D  1 107 ? 38.457 39.414  -21.476  1.00 4.76  ? 107  SER E N   1 
ATOM   4124  C  CA  . SER D  1 107 ? 37.532 38.613  -22.272  1.00 5.66  ? 107  SER E CA  1 
ATOM   4125  C  C   . SER D  1 107 ? 36.725 39.532  -23.176  1.00 6.32  ? 107  SER E C   1 
ATOM   4126  O  O   . SER D  1 107 ? 36.816 40.782  -23.083  1.00 3.43  ? 107  SER E O   1 
ATOM   4127  C  CB  . SER D  1 107 ? 36.636 37.742  -21.369  1.00 6.04  ? 107  SER E CB  1 
ATOM   4128  O  OG  . SER D  1 107 ? 35.773 38.541  -20.586  1.00 8.38  ? 107  SER E OG  1 
ATOM   4129  N  N   . GLY D  1 108 ? 35.945 38.906  -24.067  1.00 7.47  ? 108  GLY E N   1 
ATOM   4130  C  CA  . GLY D  1 108 ? 35.099 39.605  -25.019  1.00 8.80  ? 108  GLY E CA  1 
ATOM   4131  C  C   . GLY D  1 108 ? 35.858 39.937  -26.289  1.00 9.94  ? 108  GLY E C   1 
ATOM   4132  O  O   . GLY D  1 108 ? 37.092 39.735  -26.372  1.00 9.32  ? 108  GLY E O   1 
ATOM   4133  N  N   . ASP D  1 109 ? 35.142 40.469  -27.276  1.00 10.52 ? 109  ASP E N   1 
ATOM   4134  C  CA  . ASP D  1 109 ? 35.747 40.685  -28.591  1.00 11.51 ? 109  ASP E CA  1 
ATOM   4135  C  C   . ASP D  1 109 ? 36.860 41.740  -28.663  1.00 11.27 ? 109  ASP E C   1 
ATOM   4136  O  O   . ASP D  1 109 ? 37.618 41.745  -29.624  1.00 12.07 ? 109  ASP E O   1 
ATOM   4137  C  CB  . ASP D  1 109 ? 34.699 40.819  -29.720  1.00 12.63 ? 109  ASP E CB  1 
ATOM   4138  C  CG  . ASP D  1 109 ? 33.975 42.159  -29.736  1.00 15.66 ? 109  ASP E CG  1 
ATOM   4139  O  OD1 . ASP D  1 109 ? 34.068 42.932  -28.769  1.00 18.62 ? 109  ASP E OD1 1 
ATOM   4140  O  OD2 . ASP D  1 109 ? 33.263 42.425  -30.738  1.00 21.65 ? 109  ASP E OD2 1 
ATOM   4141  N  N   . HIS D  1 110 ? 36.984 42.593  -27.637  1.00 10.64 ? 110  HIS E N   1 
ATOM   4142  C  CA  . HIS D  1 110 ? 38.116 43.530  -27.535  1.00 8.96  ? 110  HIS E CA  1 
ATOM   4143  C  C   . HIS D  1 110 ? 39.106 43.218  -26.397  1.00 8.54  ? 110  HIS E C   1 
ATOM   4144  O  O   . HIS D  1 110 ? 39.815 44.108  -25.929  1.00 9.03  ? 110  HIS E O   1 
ATOM   4145  C  CB  . HIS D  1 110 ? 37.635 44.985  -27.435  1.00 10.76 ? 110  HIS E CB  1 
ATOM   4146  C  CG  . HIS D  1 110 ? 36.838 45.442  -28.623  1.00 10.91 ? 110  HIS E CG  1 
ATOM   4147  N  ND1 . HIS D  1 110 ? 35.918 46.462  -28.551  1.00 14.62 ? 110  HIS E ND1 1 
ATOM   4148  C  CD2 . HIS D  1 110 ? 36.814 45.004  -29.905  1.00 13.16 ? 110  HIS E CD2 1 
ATOM   4149  C  CE1 . HIS D  1 110 ? 35.371 46.645  -29.740  1.00 12.95 ? 110  HIS E CE1 1 
ATOM   4150  N  NE2 . HIS D  1 110 ? 35.885 45.760  -30.576  1.00 13.40 ? 110  HIS E NE2 1 
HETATM 4151  N  N   . CME D  1 111 ? 39.186 41.959  -25.979  1.00 7.09  ? 111  CME E N   1 
HETATM 4152  C  CA  . CME D  1 111 ? 40.158 41.559  -24.949  1.00 6.58  ? 111  CME E CA  1 
HETATM 4153  C  CB  . CME D  1 111 ? 39.965 40.077  -24.615  1.00 7.71  ? 111  CME E CB  1 
HETATM 4154  S  SG  . CME D  1 111 ? 40.699 39.010  -25.831  1.00 11.85 ? 111  CME E SG  1 
HETATM 4155  S  SD  . CME D  1 111 ? 40.282 37.136  -25.219  1.00 13.99 ? 111  CME E SD  1 
HETATM 4156  C  CE  . CME D  1 111 ? 38.729 36.698  -25.971  1.00 16.36 ? 111  CME E CE  1 
HETATM 4157  C  CZ  . CME D  1 111 ? 38.549 37.131  -27.431  1.00 18.29 ? 111  CME E CZ  1 
HETATM 4158  O  OH  . CME D  1 111 ? 39.454 36.441  -28.307  1.00 22.10 ? 111  CME E OH  1 
HETATM 4159  C  C   . CME D  1 111 ? 41.613 41.858  -25.278  1.00 5.43  ? 111  CME E C   1 
HETATM 4160  O  O   . CME D  1 111 ? 41.989 42.014  -26.463  1.00 5.80  ? 111  CME E O   1 
ATOM   4161  N  N   . ILE D  1 112 ? 42.434 41.972  -24.233  1.00 4.21  ? 112  ILE E N   1 
ATOM   4162  C  CA  . ILE D  1 112 ? 43.865 42.274  -24.374  1.00 3.87  ? 112  ILE E CA  1 
ATOM   4163  C  C   . ILE D  1 112 ? 44.727 41.029  -24.403  1.00 4.28  ? 112  ILE E C   1 
ATOM   4164  O  O   . ILE D  1 112 ? 45.949 41.122  -24.572  1.00 2.71  ? 112  ILE E O   1 
ATOM   4165  C  CB  . ILE D  1 112 ? 44.389 43.316  -23.311  1.00 4.23  ? 112  ILE E CB  1 
ATOM   4166  C  CG1 . ILE D  1 112 ? 44.296 42.760  -21.868  1.00 3.49  ? 112  ILE E CG1 1 
ATOM   4167  C  CG2 . ILE D  1 112 ? 43.628 44.660  -23.490  1.00 2.17  ? 112  ILE E CG2 1 
ATOM   4168  C  CD1 . ILE D  1 112 ? 44.946 43.618  -20.826  1.00 3.79  ? 112  ILE E CD1 1 
ATOM   4169  N  N   . ILE D  1 113 ? 44.098 39.851  -24.267  1.00 3.82  ? 113  ILE E N   1 
ATOM   4170  C  CA  . ILE D  1 113 ? 44.869 38.597  -24.338  1.00 4.69  ? 113  ILE E CA  1 
ATOM   4171  C  C   . ILE D  1 113 ? 45.503 38.457  -25.703  1.00 3.63  ? 113  ILE E C   1 
ATOM   4172  O  O   . ILE D  1 113 ? 44.840 38.593  -26.737  1.00 4.12  ? 113  ILE E O   1 
ATOM   4173  C  CB  . ILE D  1 113 ? 43.976 37.332  -24.095  1.00 4.79  ? 113  ILE E CB  1 
ATOM   4174  C  CG1 . ILE D  1 113 ? 43.180 37.482  -22.792  1.00 5.82  ? 113  ILE E CG1 1 
ATOM   4175  C  CG2 . ILE D  1 113 ? 44.836 36.022  -24.162  1.00 4.14  ? 113  ILE E CG2 1 
ATOM   4176  C  CD1 . ILE D  1 113 ? 44.036 37.530  -21.540  1.00 6.43  ? 113  ILE E CD1 1 
ATOM   4177  N  N   . GLY D  1 114 ? 46.797 38.169  -25.705  1.00 3.22  ? 114  GLY E N   1 
ATOM   4178  C  CA  . GLY D  1 114 ? 47.510 37.908  -26.946  1.00 3.26  ? 114  GLY E CA  1 
ATOM   4179  C  C   . GLY D  1 114 ? 48.056 39.189  -27.536  1.00 2.00  ? 114  GLY E C   1 
ATOM   4180  O  O   . GLY D  1 114 ? 48.610 39.194  -28.618  1.00 2.10  ? 114  GLY E O   1 
ATOM   4181  N  N   . ARG D  1 115 ? 47.859 40.292  -26.830  1.00 2.30  ? 115  ARG E N   1 
ATOM   4182  C  CA  . ARG D  1 115 ? 48.399 41.576  -27.295  1.00 3.21  ? 115  ARG E CA  1 
ATOM   4183  C  C   . ARG D  1 115 ? 49.663 41.832  -26.481  1.00 2.83  ? 115  ARG E C   1 
ATOM   4184  O  O   . ARG D  1 115 ? 50.070 40.955  -25.706  1.00 3.86  ? 115  ARG E O   1 
ATOM   4185  C  CB  . ARG D  1 115 ? 47.336 42.659  -27.197  1.00 2.50  ? 115  ARG E CB  1 
ATOM   4186  C  CG  . ARG D  1 115 ? 46.106 42.246  -28.059  1.00 4.52  ? 115  ARG E CG  1 
ATOM   4187  C  CD  . ARG D  1 115 ? 45.139 43.386  -28.311  1.00 6.84  ? 115  ARG E CD  1 
ATOM   4188  N  NE  . ARG D  1 115 ? 43.948 42.898  -29.005  1.00 6.62  ? 115  ARG E NE  1 
ATOM   4189  C  CZ  . ARG D  1 115 ? 43.754 42.898  -30.319  1.00 5.31  ? 115  ARG E CZ  1 
ATOM   4190  N  NH1 . ARG D  1 115 ? 42.602 42.444  -30.796  1.00 7.25  ? 115  ARG E NH1 1 
ATOM   4191  N  NH2 . ARG D  1 115 ? 44.662 43.364  -31.172  1.00 4.22  ? 115  ARG E NH2 1 
ATOM   4192  N  N   . THR D  1 116 ? 50.302 42.989  -26.672  1.00 2.34  ? 116  THR E N   1 
ATOM   4193  C  CA  . THR D  1 116 ? 51.601 43.258  -26.050  1.00 3.51  ? 116  THR E CA  1 
ATOM   4194  C  C   . THR D  1 116 ? 51.558 44.384  -25.034  1.00 2.56  ? 116  THR E C   1 
ATOM   4195  O  O   . THR D  1 116 ? 51.030 45.446  -25.315  1.00 4.17  ? 116  THR E O   1 
ATOM   4196  C  CB  . THR D  1 116 ? 52.648 43.605  -27.137  1.00 2.25  ? 116  THR E CB  1 
ATOM   4197  O  OG1 . THR D  1 116 ? 52.922 42.441  -27.905  1.00 4.93  ? 116  THR E OG1 1 
ATOM   4198  C  CG2 . THR D  1 116 ? 53.977 44.095  -26.511  1.00 4.45  ? 116  THR E CG2 1 
ATOM   4199  N  N   . LEU D  1 117 ? 52.109 44.152  -23.849  1.00 2.99  ? 117  LEU E N   1 
ATOM   4200  C  CA  . LEU D  1 117 ? 52.278 45.222  -22.873  1.00 2.54  ? 117  LEU E CA  1 
ATOM   4201  C  C   . LEU D  1 117 ? 53.667 45.830  -23.056  1.00 2.90  ? 117  LEU E C   1 
ATOM   4202  O  O   . LEU D  1 117 ? 54.644 45.085  -23.191  1.00 2.00  ? 117  LEU E O   1 
ATOM   4203  C  CB  . LEU D  1 117 ? 52.136 44.645  -21.470  1.00 2.00  ? 117  LEU E CB  1 
ATOM   4204  C  CG  . LEU D  1 117 ? 52.192 45.628  -20.286  1.00 2.38  ? 117  LEU E CG  1 
ATOM   4205  C  CD1 . LEU D  1 117 ? 51.027 46.668  -20.324  1.00 2.00  ? 117  LEU E CD1 1 
ATOM   4206  C  CD2 . LEU D  1 117 ? 52.206 44.893  -18.954  1.00 2.00  ? 117  LEU E CD2 1 
ATOM   4207  N  N   . VAL D  1 118 ? 53.742 47.165  -23.069  1.00 2.40  ? 118  VAL E N   1 
ATOM   4208  C  CA  . VAL D  1 118 ? 54.984 47.870  -23.299  1.00 3.29  ? 118  VAL E CA  1 
ATOM   4209  C  C   . VAL D  1 118 ? 55.206 48.869  -22.171  1.00 3.43  ? 118  VAL E C   1 
ATOM   4210  O  O   . VAL D  1 118 ? 54.264 49.545  -21.737  1.00 3.19  ? 118  VAL E O   1 
ATOM   4211  C  CB  . VAL D  1 118 ? 54.976 48.637  -24.637  1.00 2.26  ? 118  VAL E CB  1 
ATOM   4212  C  CG1 . VAL D  1 118 ? 56.336 49.365  -24.891  1.00 2.13  ? 118  VAL E CG1 1 
ATOM   4213  C  CG2 . VAL D  1 118 ? 54.680 47.683  -25.805  1.00 2.00  ? 118  VAL E CG2 1 
ATOM   4214  N  N   . VAL D  1 119 ? 56.451 48.941  -21.706  1.00 4.43  ? 119  VAL E N   1 
ATOM   4215  C  CA  . VAL D  1 119 ? 56.895 50.018  -20.812  1.00 4.86  ? 119  VAL E CA  1 
ATOM   4216  C  C   . VAL D  1 119 ? 57.916 50.892  -21.565  1.00 5.24  ? 119  VAL E C   1 
ATOM   4217  O  O   . VAL D  1 119 ? 58.801 50.374  -22.262  1.00 5.80  ? 119  VAL E O   1 
ATOM   4218  C  CB  . VAL D  1 119 ? 57.434 49.457  -19.465  1.00 4.53  ? 119  VAL E CB  1 
ATOM   4219  C  CG1 . VAL D  1 119 ? 58.698 48.580  -19.663  1.00 5.02  ? 119  VAL E CG1 1 
ATOM   4220  C  CG2 . VAL D  1 119 ? 57.695 50.586  -18.434  1.00 6.26  ? 119  VAL E CG2 1 
ATOM   4221  N  N   . HIS D  1 120 ? 57.802 52.207  -21.405  1.00 5.71  ? 120  HIS E N   1 
ATOM   4222  C  CA  . HIS D  1 120 ? 58.522 53.150  -22.252  1.00 6.30  ? 120  HIS E CA  1 
ATOM   4223  C  C   . HIS D  1 120 ? 59.650 53.908  -21.581  1.00 6.11  ? 120  HIS E C   1 
ATOM   4224  O  O   . HIS D  1 120 ? 59.757 53.963  -20.358  1.00 6.88  ? 120  HIS E O   1 
ATOM   4225  C  CB  . HIS D  1 120 ? 57.577 54.181  -22.841  1.00 4.64  ? 120  HIS E CB  1 
ATOM   4226  C  CG  . HIS D  1 120 ? 56.674 53.645  -23.906  1.00 4.06  ? 120  HIS E CG  1 
ATOM   4227  N  ND1 . HIS D  1 120 ? 56.965 53.762  -25.244  1.00 4.35  ? 120  HIS E ND1 1 
ATOM   4228  C  CD2 . HIS D  1 120 ? 55.475 53.023  -23.834  1.00 3.67  ? 120  HIS E CD2 1 
ATOM   4229  C  CE1 . HIS D  1 120 ? 56.002 53.201  -25.956  1.00 5.95  ? 120  HIS E CE1 1 
ATOM   4230  N  NE2 . HIS D  1 120 ? 55.080 52.760  -25.123  1.00 2.00  ? 120  HIS E NE2 1 
ATOM   4231  N  N   . GLU D  1 121 ? 60.453 54.521  -22.441  1.00 6.72  ? 121  GLU E N   1 
ATOM   4232  C  CA  . GLU D  1 121 ? 61.615 55.326  -22.074  1.00 8.32  ? 121  GLU E CA  1 
ATOM   4233  C  C   . GLU D  1 121 ? 61.247 56.537  -21.216  1.00 9.08  ? 121  GLU E C   1 
ATOM   4234  O  O   . GLU D  1 121 ? 61.918 56.844  -20.225  1.00 9.22  ? 121  GLU E O   1 
ATOM   4235  C  CB  . GLU D  1 121 ? 62.267 55.780  -23.372  1.00 8.45  ? 121  GLU E CB  1 
ATOM   4236  C  CG  . GLU D  1 121 ? 63.420 56.758  -23.215  1.00 12.18 ? 121  GLU E CG  1 
ATOM   4237  C  CD  . GLU D  1 121 ? 64.058 57.139  -24.544  1.00 17.06 ? 121  GLU E CD  1 
ATOM   4238  O  OE1 . GLU D  1 121 ? 65.298 57.281  -24.527  1.00 21.57 ? 121  GLU E OE1 1 
ATOM   4239  O  OE2 . GLU D  1 121 ? 63.350 57.315  -25.585  1.00 17.80 ? 121  GLU E OE2 1 
ATOM   4240  N  N   . LYS D  1 122 ? 60.181 57.215  -21.620  1.00 9.67  ? 122  LYS E N   1 
ATOM   4241  C  CA  . LYS D  1 122 ? 59.828 58.534  -21.106  1.00 11.31 ? 122  LYS E CA  1 
ATOM   4242  C  C   . LYS D  1 122 ? 58.398 58.512  -20.566  1.00 10.72 ? 122  LYS E C   1 
ATOM   4243  O  O   . LYS D  1 122 ? 57.662 57.542  -20.779  1.00 9.20  ? 122  LYS E O   1 
ATOM   4244  C  CB  . LYS D  1 122 ? 59.875 59.566  -22.233  1.00 11.35 ? 122  LYS E CB  1 
ATOM   4245  C  CG  . LYS D  1 122 ? 61.236 59.878  -22.832  1.00 16.41 ? 122  LYS E CG  1 
ATOM   4246  C  CD  . LYS D  1 122 ? 61.032 60.530  -24.178  1.00 19.76 ? 122  LYS E CD  1 
ATOM   4247  C  CE  . LYS D  1 122 ? 62.346 61.028  -24.750  1.00 24.76 ? 122  LYS E CE  1 
ATOM   4248  N  NZ  . LYS D  1 122 ? 62.141 61.601  -26.128  1.00 27.19 ? 122  LYS E NZ  1 
ATOM   4249  N  N   . ALA D  1 123 ? 58.029 59.604  -19.891  1.00 10.47 ? 123  ALA E N   1 
ATOM   4250  C  CA  . ALA D  1 123 ? 56.675 59.825  -19.381  1.00 9.55  ? 123  ALA E CA  1 
ATOM   4251  C  C   . ALA D  1 123 ? 55.689 59.930  -20.529  1.00 8.39  ? 123  ALA E C   1 
ATOM   4252  O  O   . ALA D  1 123 ? 56.003 60.454  -21.603  1.00 8.76  ? 123  ALA E O   1 
ATOM   4253  C  CB  . ALA D  1 123 ? 56.621 61.140  -18.514  1.00 9.49  ? 123  ALA E CB  1 
ATOM   4254  N  N   . ASP D  1 124 ? 54.502 59.395  -20.301  1.00 7.80  ? 124  ASP E N   1 
ATOM   4255  C  CA  . ASP D  1 124 ? 53.360 59.555  -21.191  1.00 7.73  ? 124  ASP E CA  1 
ATOM   4256  C  C   . ASP D  1 124 ? 52.714 60.875  -20.811  1.00 7.27  ? 124  ASP E C   1 
ATOM   4257  O  O   . ASP D  1 124 ? 52.360 61.056  -19.628  1.00 7.18  ? 124  ASP E O   1 
ATOM   4258  C  CB  . ASP D  1 124 ? 52.386 58.407  -20.883  1.00 7.45  ? 124  ASP E CB  1 
ATOM   4259  C  CG  . ASP D  1 124 ? 51.163 58.385  -21.790  1.00 8.08  ? 124  ASP E CG  1 
ATOM   4260  O  OD1 . ASP D  1 124 ? 50.616 57.273  -21.932  1.00 8.38  ? 124  ASP E OD1 1 
ATOM   4261  O  OD2 . ASP D  1 124 ? 50.725 59.422  -22.349  1.00 7.12  ? 124  ASP E OD2 1 
ATOM   4262  N  N   . ASP D  1 125 ? 52.563 61.793  -21.775  1.00 8.20  ? 125  ASP E N   1 
ATOM   4263  C  CA  . ASP D  1 125 ? 51.959 63.132  -21.499  1.00 9.43  ? 125  ASP E CA  1 
ATOM   4264  C  C   . ASP D  1 125 ? 50.435 63.140  -21.485  1.00 9.63  ? 125  ASP E C   1 
ATOM   4265  O  O   . ASP D  1 125 ? 49.784 64.205  -21.476  1.00 8.98  ? 125  ASP E O   1 
ATOM   4266  C  CB  . ASP D  1 125 ? 52.509 64.220  -22.463  1.00 9.75  ? 125  ASP E CB  1 
ATOM   4267  C  CG  . ASP D  1 125 ? 52.096 64.022  -23.933  1.00 10.66 ? 125  ASP E CG  1 
ATOM   4268  O  OD1 . ASP D  1 125 ? 52.794 64.630  -24.770  1.00 10.97 ? 125  ASP E OD1 1 
ATOM   4269  O  OD2 . ASP D  1 125 ? 51.094 63.312  -24.286  1.00 9.02  ? 125  ASP E OD2 1 
ATOM   4270  N  N   . LEU D  1 126 ? 49.867 61.933  -21.534  1.00 9.50  ? 126  LEU E N   1 
ATOM   4271  C  CA  . LEU D  1 126 ? 48.429 61.722  -21.412  1.00 10.60 ? 126  LEU E CA  1 
ATOM   4272  C  C   . LEU D  1 126 ? 47.597 62.405  -22.510  1.00 11.04 ? 126  LEU E C   1 
ATOM   4273  O  O   . LEU D  1 126 ? 46.420 62.673  -22.328  1.00 11.24 ? 126  LEU E O   1 
ATOM   4274  C  CB  . LEU D  1 126 ? 47.946 62.073  -19.980  1.00 10.18 ? 126  LEU E CB  1 
ATOM   4275  C  CG  . LEU D  1 126 ? 48.761 61.485  -18.813  1.00 11.58 ? 126  LEU E CG  1 
ATOM   4276  C  CD1 . LEU D  1 126 ? 48.153 61.893  -17.453  1.00 14.14 ? 126  LEU E CD1 1 
ATOM   4277  C  CD2 . LEU D  1 126 ? 48.950 59.961  -18.892  1.00 10.71 ? 126  LEU E CD2 1 
ATOM   4278  N  N   . GLY D  1 127 ? 48.228 62.678  -23.646  1.00 11.03 ? 127  GLY E N   1 
ATOM   4279  C  CA  . GLY D  1 127 ? 47.529 63.202  -24.806  1.00 11.48 ? 127  GLY E CA  1 
ATOM   4280  C  C   . GLY D  1 127 ? 47.354 64.708  -24.818  1.00 12.36 ? 127  GLY E C   1 
ATOM   4281  O  O   . GLY D  1 127 ? 46.679 65.246  -25.697  1.00 12.46 ? 127  GLY E O   1 
ATOM   4282  N  N   . LYS D  1 128 ? 47.980 65.381  -23.861  1.00 12.89 ? 128  LYS E N   1 
ATOM   4283  C  CA  . LYS D  1 128 ? 47.786 66.823  -23.663  1.00 14.95 ? 128  LYS E CA  1 
ATOM   4284  C  C   . LYS D  1 128 ? 49.054 67.608  -24.005  1.00 14.88 ? 128  LYS E C   1 
ATOM   4285  O  O   . LYS D  1 128 ? 49.223 68.744  -23.548  1.00 14.63 ? 128  LYS E O   1 
ATOM   4286  C  CB  . LYS D  1 128 ? 47.355 67.120  -22.221  1.00 15.82 ? 128  LYS E CB  1 
ATOM   4287  C  CG  . LYS D  1 128 ? 46.131 66.312  -21.725  1.00 18.05 ? 128  LYS E CG  1 
ATOM   4288  C  CD  . LYS D  1 128 ? 45.947 66.471  -20.222  1.00 21.44 ? 128  LYS E CD  1 
ATOM   4289  C  CE  . LYS D  1 128 ? 45.105 65.352  -19.626  1.00 22.75 ? 128  LYS E CE  1 
ATOM   4290  N  NZ  . LYS D  1 128 ? 43.830 65.122  -20.382  1.00 25.89 ? 128  LYS E NZ  1 
ATOM   4291  N  N   . GLY D  1 129 ? 49.935 66.998  -24.806  1.00 14.36 ? 129  GLY E N   1 
ATOM   4292  C  CA  . GLY D  1 129 ? 51.199 67.618  -25.215  1.00 14.45 ? 129  GLY E CA  1 
ATOM   4293  C  C   . GLY D  1 129 ? 51.079 68.715  -26.257  1.00 14.93 ? 129  GLY E C   1 
ATOM   4294  O  O   . GLY D  1 129 ? 52.022 69.494  -26.459  1.00 15.63 ? 129  GLY E O   1 
ATOM   4295  N  N   . GLY D  1 130 ? 49.933 68.787  -26.924  1.00 14.87 ? 130  GLY E N   1 
ATOM   4296  C  CA  . GLY D  1 130 ? 49.711 69.781  -27.982  1.00 15.34 ? 130  GLY E CA  1 
ATOM   4297  C  C   . GLY D  1 130 ? 50.492 69.564  -29.275  1.00 15.17 ? 130  GLY E C   1 
ATOM   4298  O  O   . GLY D  1 130 ? 50.850 70.524  -29.947  1.00 16.26 ? 130  GLY E O   1 
ATOM   4299  N  N   . ASN D  1 131 ? 50.795 68.305  -29.603  1.00 14.75 ? 131  ASN E N   1 
ATOM   4300  C  CA  . ASN D  1 131 ? 51.324 67.937  -30.917  1.00 14.28 ? 131  ASN E CA  1 
ATOM   4301  C  C   . ASN D  1 131 ? 50.652 66.658  -31.406  1.00 13.73 ? 131  ASN E C   1 
ATOM   4302  O  O   . ASN D  1 131 ? 49.951 65.992  -30.629  1.00 12.84 ? 131  ASN E O   1 
ATOM   4303  C  CB  . ASN D  1 131 ? 52.853 67.814  -30.901  1.00 14.35 ? 131  ASN E CB  1 
ATOM   4304  C  CG  . ASN D  1 131 ? 53.356 66.874  -29.814  1.00 15.65 ? 131  ASN E CG  1 
ATOM   4305  O  OD1 . ASN D  1 131 ? 53.035 65.695  -29.806  1.00 14.01 ? 131  ASN E OD1 1 
ATOM   4306  N  ND2 . ASN D  1 131 ? 54.146 67.407  -28.891  1.00 18.20 ? 131  ASN E ND2 1 
ATOM   4307  N  N   . GLU D  1 132 ? 50.852 66.322  -32.677  1.00 12.58 ? 132  GLU E N   1 
ATOM   4308  C  CA  . GLU D  1 132 ? 50.209 65.156  -33.260  1.00 12.46 ? 132  GLU E CA  1 
ATOM   4309  C  C   . GLU D  1 132 ? 50.660 63.841  -32.611  1.00 12.25 ? 132  GLU E C   1 
ATOM   4310  O  O   . GLU D  1 132 ? 49.833 62.955  -32.414  1.00 11.69 ? 132  GLU E O   1 
ATOM   4311  C  CB  . GLU D  1 132 ? 50.377 65.121  -34.788  1.00 12.66 ? 132  GLU E CB  1 
ATOM   4312  C  CG  . GLU D  1 132 ? 49.813 63.869  -35.491  1.00 12.78 ? 132  GLU E CG  1 
ATOM   4313  C  CD  . GLU D  1 132 ? 48.292 63.736  -35.493  1.00 13.50 ? 132  GLU E CD  1 
ATOM   4314  O  OE1 . GLU D  1 132 ? 47.801 62.712  -36.010  1.00 15.53 ? 132  GLU E OE1 1 
ATOM   4315  O  OE2 . GLU D  1 132 ? 47.578 64.635  -35.018  1.00 14.38 ? 132  GLU E OE2 1 
ATOM   4316  N  N   . GLU D  1 133 ? 51.946 63.714  -32.285  1.00 11.57 ? 133  GLU E N   1 
ATOM   4317  C  CA  . GLU D  1 133 ? 52.426 62.512  -31.593  1.00 12.09 ? 133  GLU E CA  1 
ATOM   4318  C  C   . GLU D  1 133 ? 51.805 62.321  -30.221  1.00 11.33 ? 133  GLU E C   1 
ATOM   4319  O  O   . GLU D  1 133 ? 51.558 61.189  -29.804  1.00 10.45 ? 133  GLU E O   1 
ATOM   4320  C  CB  . GLU D  1 133 ? 53.952 62.468  -31.467  1.00 12.32 ? 133  GLU E CB  1 
ATOM   4321  C  CG  . GLU D  1 133 ? 54.625 61.913  -32.679  1.00 16.48 ? 133  GLU E CG  1 
ATOM   4322  C  CD  . GLU D  1 133 ? 54.274 60.459  -32.934  1.00 18.96 ? 133  GLU E CD  1 
ATOM   4323  O  OE1 . GLU D  1 133 ? 54.770 59.568  -32.218  1.00 19.49 ? 133  GLU E OE1 1 
ATOM   4324  O  OE2 . GLU D  1 133 ? 53.523 60.209  -33.878  1.00 20.60 ? 133  GLU E OE2 1 
ATOM   4325  N  N   . SER D  1 134 ? 51.551 63.415  -29.507  1.00 10.30 ? 134  SER E N   1 
ATOM   4326  C  CA  . SER D  1 134 ? 50.843 63.307  -28.228  1.00 9.97  ? 134  SER E CA  1 
ATOM   4327  C  C   . SER D  1 134 ? 49.507 62.568  -28.366  1.00 9.85  ? 134  SER E C   1 
ATOM   4328  O  O   . SER D  1 134 ? 49.147 61.773  -27.488  1.00 10.11 ? 134  SER E O   1 
ATOM   4329  C  CB  . SER D  1 134 ? 50.617 64.679  -27.581  1.00 9.38  ? 134  SER E CB  1 
ATOM   4330  O  OG  . SER D  1 134 ? 49.995 64.512  -26.308  1.00 8.76  ? 134  SER E OG  1 
ATOM   4331  N  N   . THR D  1 135 ? 48.804 62.808  -29.471  1.00 9.65  ? 135  THR E N   1 
ATOM   4332  C  CA  . THR D  1 135 ? 47.490 62.191  -29.720  1.00 9.76  ? 135  THR E CA  1 
ATOM   4333  C  C   . THR D  1 135 ? 47.619 60.732  -30.180  1.00 9.06  ? 135  THR E C   1 
ATOM   4334  O  O   . THR D  1 135 ? 46.621 60.051  -30.366  1.00 7.79  ? 135  THR E O   1 
ATOM   4335  C  CB  . THR D  1 135 ? 46.646 62.975  -30.761  1.00 9.63  ? 135  THR E CB  1 
ATOM   4336  O  OG1 . THR D  1 135 ? 47.162 62.731  -32.080  1.00 12.27 ? 135  THR E OG1 1 
ATOM   4337  C  CG2 . THR D  1 135 ? 46.630 64.500  -30.459  1.00 10.36 ? 135  THR E CG2 1 
ATOM   4338  N  N   . LYS D  1 136 ? 48.851 60.279  -30.360  1.00 8.88  ? 136  LYS E N   1 
ATOM   4339  C  CA  . LYS D  1 136 ? 49.111 58.891  -30.780  1.00 9.07  ? 136  LYS E CA  1 
ATOM   4340  C  C   . LYS D  1 136 ? 49.787 58.058  -29.687  1.00 8.55  ? 136  LYS E C   1 
ATOM   4341  O  O   . LYS D  1 136 ? 49.278 57.004  -29.299  1.00 7.93  ? 136  LYS E O   1 
ATOM   4342  C  CB  . LYS D  1 136 ? 49.915 58.873  -32.093  1.00 9.69  ? 136  LYS E CB  1 
ATOM   4343  C  CG  . LYS D  1 136 ? 49.058 59.190  -33.324  1.00 10.37 ? 136  LYS E CG  1 
ATOM   4344  C  CD  . LYS D  1 136 ? 49.910 59.431  -34.543  1.00 13.72 ? 136  LYS E CD  1 
ATOM   4345  C  CE  . LYS D  1 136 ? 49.117 59.384  -35.839  1.00 12.03 ? 136  LYS E CE  1 
ATOM   4346  N  NZ  . LYS D  1 136 ? 47.702 59.848  -35.744  1.00 14.53 ? 136  LYS E NZ  1 
ATOM   4347  N  N   . THR D  1 137 ? 50.911 58.541  -29.166  1.00 7.86  ? 137  THR E N   1 
ATOM   4348  C  CA  . THR D  1 137 ? 51.739 57.758  -28.258  1.00 7.13  ? 137  THR E CA  1 
ATOM   4349  C  C   . THR D  1 137 ? 51.909 58.411  -26.892  1.00 6.40  ? 137  THR E C   1 
ATOM   4350  O  O   . THR D  1 137 ? 52.544 57.852  -26.006  1.00 5.37  ? 137  THR E O   1 
ATOM   4351  C  CB  . THR D  1 137 ? 53.165 57.609  -28.842  1.00 8.06  ? 137  THR E CB  1 
ATOM   4352  O  OG1 . THR D  1 137 ? 53.733 58.918  -28.974  1.00 7.19  ? 137  THR E OG1 1 
ATOM   4353  C  CG2 . THR D  1 137 ? 53.142 56.925  -30.241  1.00 8.22  ? 137  THR E CG2 1 
ATOM   4354  N  N   . GLY D  1 138 ? 51.419 59.637  -26.726  1.00 5.89  ? 138  GLY E N   1 
ATOM   4355  C  CA  . GLY D  1 138 ? 51.742 60.368  -25.513  1.00 5.18  ? 138  GLY E CA  1 
ATOM   4356  C  C   . GLY D  1 138 ? 53.204 60.815  -25.411  1.00 5.86  ? 138  GLY E C   1 
ATOM   4357  O  O   . GLY D  1 138 ? 53.668 61.179  -24.328  1.00 5.28  ? 138  GLY E O   1 
ATOM   4358  N  N   . ASN D  1 139 ? 53.930 60.802  -26.533  1.00 7.12  ? 139  ASN E N   1 
ATOM   4359  C  CA  . ASN D  1 139 ? 55.368 61.146  -26.531  1.00 7.64  ? 139  ASN E CA  1 
ATOM   4360  C  C   . ASN D  1 139 ? 56.217 60.320  -25.527  1.00 8.46  ? 139  ASN E C   1 
ATOM   4361  O  O   . ASN D  1 139 ? 57.197 60.813  -24.951  1.00 9.02  ? 139  ASN E O   1 
ATOM   4362  C  CB  . ASN D  1 139 ? 55.563 62.650  -26.337  1.00 7.96  ? 139  ASN E CB  1 
ATOM   4363  C  CG  . ASN D  1 139 ? 55.128 63.447  -27.552  1.00 9.41  ? 139  ASN E CG  1 
ATOM   4364  O  OD1 . ASN D  1 139 ? 55.691 63.291  -28.636  1.00 10.68 ? 139  ASN E OD1 1 
ATOM   4365  N  ND2 . ASN D  1 139 ? 54.104 64.289  -27.388  1.00 9.22  ? 139  ASN E ND2 1 
ATOM   4366  N  N   . ALA D  1 140 ? 55.828 59.065  -25.330  1.00 7.89  ? 140  ALA E N   1 
ATOM   4367  C  CA  . ALA D  1 140 ? 56.450 58.215  -24.311  1.00 9.10  ? 140  ALA E CA  1 
ATOM   4368  C  C   . ALA D  1 140 ? 57.796 57.651  -24.781  1.00 9.25  ? 140  ALA E C   1 
ATOM   4369  O  O   . ALA D  1 140 ? 58.512 57.008  -24.002  1.00 9.60  ? 140  ALA E O   1 
ATOM   4370  C  CB  . ALA D  1 140 ? 55.488 57.067  -23.918  1.00 9.09  ? 140  ALA E CB  1 
ATOM   4371  N  N   . GLY D  1 141 ? 58.113 57.850  -26.064  1.00 9.16  ? 141  GLY E N   1 
ATOM   4372  C  CA  . GLY D  1 141 ? 59.450 57.487  -26.571  1.00 8.76  ? 141  GLY E CA  1 
ATOM   4373  C  C   . GLY D  1 141 ? 59.648 55.994  -26.742  1.00 8.71  ? 141  GLY E C   1 
ATOM   4374  O  O   . GLY D  1 141 ? 58.693 55.245  -26.993  1.00 7.02  ? 141  GLY E O   1 
ATOM   4375  N  N   . SER D  1 142 ? 60.897 55.562  -26.614  1.00 8.23  ? 142  SER E N   1 
ATOM   4376  C  CA  . SER D  1 142 ? 61.253 54.226  -27.066  1.00 7.93  ? 142  SER E CA  1 
ATOM   4377  C  C   . SER D  1 142 ? 60.651 53.128  -26.184  1.00 7.02  ? 142  SER E C   1 
ATOM   4378  O  O   . SER D  1 142 ? 60.249 53.374  -25.033  1.00 6.87  ? 142  SER E O   1 
ATOM   4379  C  CB  . SER D  1 142 ? 62.781 54.078  -27.195  1.00 8.40  ? 142  SER E CB  1 
ATOM   4380  O  OG  . SER D  1 142 ? 63.343 53.862  -25.926  1.00 11.54 ? 142  SER E OG  1 
ATOM   4381  N  N   . ARG D  1 143 ? 60.563 51.928  -26.741  1.00 6.60  ? 143  ARG E N   1 
ATOM   4382  C  CA  . ARG D  1 143 ? 59.980 50.772  -26.035  1.00 7.00  ? 143  ARG E CA  1 
ATOM   4383  C  C   . ARG D  1 143 ? 61.085 49.982  -25.381  1.00 7.21  ? 143  ARG E C   1 
ATOM   4384  O  O   . ARG D  1 143 ? 61.886 49.346  -26.085  1.00 8.63  ? 143  ARG E O   1 
ATOM   4385  C  CB  . ARG D  1 143 ? 59.252 49.878  -27.028  1.00 7.30  ? 143  ARG E CB  1 
ATOM   4386  C  CG  . ARG D  1 143 ? 58.200 50.665  -27.790  1.00 7.12  ? 143  ARG E CG  1 
ATOM   4387  C  CD  . ARG D  1 143 ? 57.701 49.921  -29.028  1.00 7.15  ? 143  ARG E CD  1 
ATOM   4388  N  NE  . ARG D  1 143 ? 56.757 50.792  -29.744  1.00 6.41  ? 143  ARG E NE  1 
ATOM   4389  C  CZ  . ARG D  1 143 ? 55.746 50.385  -30.502  1.00 7.40  ? 143  ARG E CZ  1 
ATOM   4390  N  NH1 . ARG D  1 143 ? 54.968 51.303  -31.075  1.00 6.33  ? 143  ARG E NH1 1 
ATOM   4391  N  NH2 . ARG D  1 143 ? 55.487 49.080  -30.681  1.00 5.44  ? 143  ARG E NH2 1 
ATOM   4392  N  N   . LEU D  1 144 ? 61.133 50.015  -24.054  1.00 6.48  ? 144  LEU E N   1 
ATOM   4393  C  CA  . LEU D  1 144 ? 62.288 49.502  -23.328  1.00 6.14  ? 144  LEU E CA  1 
ATOM   4394  C  C   . LEU D  1 144 ? 62.163 48.031  -23.041  1.00 6.04  ? 144  LEU E C   1 
ATOM   4395  O  O   . LEU D  1 144 ? 63.146 47.313  -23.097  1.00 6.02  ? 144  LEU E O   1 
ATOM   4396  C  CB  . LEU D  1 144 ? 62.516 50.285  -22.035  1.00 6.84  ? 144  LEU E CB  1 
ATOM   4397  C  CG  . LEU D  1 144 ? 62.988 51.729  -22.233  1.00 8.72  ? 144  LEU E CG  1 
ATOM   4398  C  CD1 . LEU D  1 144 ? 63.356 52.271  -20.875  1.00 12.85 ? 144  LEU E CD1 1 
ATOM   4399  C  CD2 . LEU D  1 144 ? 64.166 51.864  -23.203  1.00 11.23 ? 144  LEU E CD2 1 
ATOM   4400  N  N   . ALA D  1 145 ? 60.931 47.589  -22.755  1.00 4.81  ? 145  ALA E N   1 
ATOM   4401  C  CA  . ALA D  1 145 ? 60.646 46.187  -22.582  1.00 3.37  ? 145  ALA E CA  1 
ATOM   4402  C  C   . ALA D  1 145 ? 59.203 45.925  -22.938  1.00 3.02  ? 145  ALA E C   1 
ATOM   4403  O  O   . ALA D  1 145 ? 58.370 46.845  -22.938  1.00 3.34  ? 145  ALA E O   1 
ATOM   4404  C  CB  . ALA D  1 145 ? 60.933 45.744  -21.154  1.00 2.84  ? 145  ALA E CB  1 
ATOM   4405  N  N   . CYS D  1 146 ? 58.913 44.671  -23.255  1.00 2.00  ? 146  CYS E N   1 
ATOM   4406  C  CA  . CYS D  1 146 ? 57.568 44.298  -23.677  1.00 2.00  ? 146  CYS E CA  1 
ATOM   4407  C  C   . CYS D  1 146 ? 57.400 42.809  -23.564  1.00 2.00  ? 146  CYS E C   1 
ATOM   4408  O  O   . CYS D  1 146 ? 58.369 42.080  -23.365  1.00 2.00  ? 146  CYS E O   1 
ATOM   4409  C  CB  . CYS D  1 146 ? 57.298 44.751  -25.112  0.40 2.00  ? 146  CYS E CB  1 
ATOM   4410  S  SG  . CYS D  1 146 ? 58.331 44.022  -26.350  0.40 2.00  ? 146  CYS E SG  1 
ATOM   4411  N  N   . GLY D  1 147 ? 56.159 42.358  -23.679  1.00 2.14  ? 147  GLY E N   1 
ATOM   4412  C  CA  . GLY D  1 147 ? 55.892 40.933  -23.651  1.00 2.00  ? 147  GLY E CA  1 
ATOM   4413  C  C   . GLY D  1 147 ? 54.477 40.686  -24.070  1.00 2.85  ? 147  GLY E C   1 
ATOM   4414  O  O   . GLY D  1 147 ? 53.665 41.616  -24.077  1.00 2.58  ? 147  GLY E O   1 
ATOM   4415  N  N   . VAL D  1 148 ? 54.181 39.436  -24.421  1.00 2.35  ? 148  VAL E N   1 
ATOM   4416  C  CA  . VAL D  1 148 ? 52.813 39.079  -24.841  1.00 2.91  ? 148  VAL E CA  1 
ATOM   4417  C  C   . VAL D  1 148 ? 51.994 38.800  -23.586  1.00 2.78  ? 148  VAL E C   1 
ATOM   4418  O  O   . VAL D  1 148 ? 52.506 38.218  -22.636  1.00 3.21  ? 148  VAL E O   1 
ATOM   4419  C  CB  . VAL D  1 148 ? 52.825 37.835  -25.753  1.00 2.10  ? 148  VAL E CB  1 
ATOM   4420  C  CG1 . VAL D  1 148 ? 51.380 37.456  -26.191  1.00 3.59  ? 148  VAL E CG1 1 
ATOM   4421  C  CG2 . VAL D  1 148 ? 53.706 38.093  -26.979  1.00 2.46  ? 148  VAL E CG2 1 
ATOM   4422  N  N   . ILE D  1 149 ? 50.741 39.252  -23.572  1.00 2.30  ? 149  ILE E N   1 
ATOM   4423  C  CA  . ILE D  1 149 ? 49.828 39.037  -22.447  1.00 2.00  ? 149  ILE E CA  1 
ATOM   4424  C  C   . ILE D  1 149 ? 49.212 37.650  -22.626  1.00 2.00  ? 149  ILE E C   1 
ATOM   4425  O  O   . ILE D  1 149 ? 48.513 37.415  -23.597  1.00 2.45  ? 149  ILE E O   1 
ATOM   4426  C  CB  . ILE D  1 149 ? 48.742 40.126  -22.400  1.00 2.00  ? 149  ILE E CB  1 
ATOM   4427  C  CG1 . ILE D  1 149 ? 49.433 41.483  -22.161  1.00 2.00  ? 149  ILE E CG1 1 
ATOM   4428  C  CG2 . ILE D  1 149 ? 47.789 39.861  -21.227  1.00 4.08  ? 149  ILE E CG2 1 
ATOM   4429  C  CD1 . ILE D  1 149 ? 48.520 42.737  -22.443  1.00 2.00  ? 149  ILE E CD1 1 
ATOM   4430  N  N   . GLY D  1 150 ? 49.527 36.753  -21.702  1.00 2.89  ? 150  GLY E N   1 
ATOM   4431  C  CA  . GLY D  1 150 ? 49.169 35.357  -21.789  1.00 3.36  ? 150  GLY E CA  1 
ATOM   4432  C  C   . GLY D  1 150 ? 48.146 34.974  -20.730  1.00 4.48  ? 150  GLY E C   1 
ATOM   4433  O  O   . GLY D  1 150 ? 48.078 35.566  -19.641  1.00 4.56  ? 150  GLY E O   1 
ATOM   4434  N  N   . ILE D  1 151 ? 47.332 33.986  -21.073  1.00 4.87  ? 151  ILE E N   1 
ATOM   4435  C  CA  . ILE D  1 151 ? 46.384 33.378  -20.128  1.00 5.70  ? 151  ILE E CA  1 
ATOM   4436  C  C   . ILE D  1 151 ? 47.127 32.712  -18.972  1.00 5.72  ? 151  ILE E C   1 
ATOM   4437  O  O   . ILE D  1 151 ? 48.070 31.924  -19.179  1.00 5.45  ? 151  ILE E O   1 
ATOM   4438  C  CB  . ILE D  1 151 ? 45.444 32.330  -20.850  1.00 5.05  ? 151  ILE E CB  1 
ATOM   4439  C  CG1 . ILE D  1 151 ? 44.630 33.053  -21.929  1.00 8.56  ? 151  ILE E CG1 1 
ATOM   4440  C  CG2 . ILE D  1 151 ? 44.518 31.626  -19.825  1.00 6.31  ? 151  ILE E CG2 1 
ATOM   4441  C  CD1 . ILE D  1 151 ? 43.854 32.147  -22.879  1.00 12.92 ? 151  ILE E CD1 1 
ATOM   4442  N  N   . ALA D  1 152 ? 46.711 33.050  -17.756  1.00 5.39  ? 152  ALA E N   1 
ATOM   4443  C  CA  . ALA D  1 152 ? 47.328 32.509  -16.549  1.00 7.08  ? 152  ALA E CA  1 
ATOM   4444  C  C   . ALA D  1 152 ? 46.358 31.605  -15.791  1.00 9.11  ? 152  ALA E C   1 
ATOM   4445  O  O   . ALA D  1 152 ? 45.139 31.693  -15.981  1.00 8.53  ? 152  ALA E O   1 
ATOM   4446  C  CB  . ALA D  1 152 ? 47.833 33.628  -15.639  1.00 7.17  ? 152  ALA E CB  1 
ATOM   4447  N  N   . GLN D  1 153 ? 46.932 30.725  -14.973  1.00 10.73 ? 153  GLN E N   1 
ATOM   4448  C  CA  . GLN D  1 153 ? 46.173 29.767  -14.177  1.00 13.43 ? 153  GLN E CA  1 
ATOM   4449  C  C   . GLN D  1 153 ? 45.399 30.430  -13.053  1.00 13.76 ? 153  GLN E C   1 
ATOM   4450  O  O   . GLN D  1 153 ? 45.952 31.104  -12.185  1.00 14.24 ? 153  GLN E O   1 
ATOM   4451  C  CB  . GLN D  1 153 ? 47.099 28.727  -13.566  1.00 13.21 ? 153  GLN E CB  1 
ATOM   4452  C  CG  . GLN D  1 153 ? 46.352 27.714  -12.712  1.00 15.89 ? 153  GLN E CG  1 
ATOM   4453  C  CD  . GLN D  1 153 ? 47.231 26.583  -12.262  1.00 20.12 ? 153  GLN E CD  1 
ATOM   4454  O  OE1 . GLN D  1 153 ? 46.813 25.436  -12.268  1.00 24.51 ? 153  GLN E OE1 1 
ATOM   4455  N  NE2 . GLN D  1 153 ? 48.457 26.897  -11.872  1.00 21.25 ? 153  GLN E NE2 1 
ATOM   4456  O  OXT . GLN D  1 153 ? 44.185 30.253  -12.996  1.00 16.34 ? 153  GLN E OXT 1 
ATOM   4457  N  N   . ALA E  1 1   ? 32.652 -24.750 -43.915  1.00 22.63 ? 1    ALA F N   1 
ATOM   4458  C  CA  . ALA E  1 1   ? 31.547 -23.756 -43.731  1.00 21.68 ? 1    ALA F CA  1 
ATOM   4459  C  C   . ALA E  1 1   ? 30.460 -24.243 -42.769  1.00 20.82 ? 1    ALA F C   1 
ATOM   4460  O  O   . ALA E  1 1   ? 30.232 -25.441 -42.621  1.00 21.74 ? 1    ALA F O   1 
ATOM   4461  C  CB  . ALA E  1 1   ? 30.939 -23.380 -45.087  1.00 21.99 ? 1    ALA F CB  1 
ATOM   4462  N  N   . THR E  1 2   ? 29.783 -23.309 -42.118  1.00 18.74 ? 2    THR F N   1 
ATOM   4463  C  CA  . THR E  1 2   ? 28.624 -23.653 -41.321  1.00 17.28 ? 2    THR F CA  1 
ATOM   4464  C  C   . THR E  1 2   ? 27.390 -23.105 -42.014  1.00 15.35 ? 2    THR F C   1 
ATOM   4465  O  O   . THR E  1 2   ? 27.429 -22.046 -42.633  1.00 14.86 ? 2    THR F O   1 
ATOM   4466  C  CB  . THR E  1 2   ? 28.759 -23.145 -39.880  1.00 17.06 ? 2    THR F CB  1 
ATOM   4467  O  OG1 . THR E  1 2   ? 29.944 -23.702 -39.307  1.00 19.39 ? 2    THR F OG1 1 
ATOM   4468  C  CG2 . THR E  1 2   ? 27.582 -23.552 -39.029  1.00 19.19 ? 2    THR F CG2 1 
ATOM   4469  N  N   . LYS E  1 3   ? 26.308 -23.864 -41.934  1.00 13.28 ? 3    LYS F N   1 
ATOM   4470  C  CA  . LYS E  1 3   ? 25.062 -23.498 -42.571  1.00 12.95 ? 3    LYS F CA  1 
ATOM   4471  C  C   . LYS E  1 3   ? 23.905 -23.515 -41.565  1.00 11.80 ? 3    LYS F C   1 
ATOM   4472  O  O   . LYS E  1 3   ? 23.907 -24.299 -40.621  1.00 11.96 ? 3    LYS F O   1 
ATOM   4473  C  CB  . LYS E  1 3   ? 24.792 -24.459 -43.741  1.00 11.98 ? 3    LYS F CB  1 
ATOM   4474  C  CG  . LYS E  1 3   ? 25.736 -24.251 -44.953  1.00 14.47 ? 3    LYS F CG  1 
ATOM   4475  C  CD  . LYS E  1 3   ? 25.354 -25.120 -46.160  1.00 17.44 ? 3    LYS F CD  1 
ATOM   4476  C  CE  . LYS E  1 3   ? 26.257 -24.826 -47.373  1.00 21.17 ? 3    LYS F CE  1 
ATOM   4477  N  NZ  . LYS E  1 3   ? 26.030 -25.758 -48.506  1.00 24.26 ? 3    LYS F NZ  1 
ATOM   4478  N  N   . ALA E  1 4   ? 22.916 -22.652 -41.780  1.00 10.43 ? 4    ALA F N   1 
ATOM   4479  C  CA  . ALA E  1 4   ? 21.715 -22.656 -40.950  1.00 9.77  ? 4    ALA F CA  1 
ATOM   4480  C  C   . ALA E  1 4   ? 20.489 -22.329 -41.777  1.00 9.96  ? 4    ALA F C   1 
ATOM   4481  O  O   . ALA E  1 4   ? 20.590 -21.854 -42.926  1.00 8.96  ? 4    ALA F O   1 
ATOM   4482  C  CB  . ALA E  1 4   ? 21.874 -21.661 -39.764  1.00 9.97  ? 4    ALA F CB  1 
ATOM   4483  N  N   . VAL E  1 5   ? 19.316 -22.589 -41.210  1.00 9.50  ? 5    VAL F N   1 
ATOM   4484  C  CA  . VAL E  1 5   ? 18.088 -22.378 -41.955  1.00 10.07 ? 5    VAL F CA  1 
ATOM   4485  C  C   . VAL E  1 5   ? 16.942 -21.986 -41.039  1.00 9.29  ? 5    VAL F C   1 
ATOM   4486  O  O   . VAL E  1 5   ? 16.991 -22.243 -39.868  1.00 10.73 ? 5    VAL F O   1 
ATOM   4487  C  CB  . VAL E  1 5   ? 17.740 -23.618 -42.845  1.00 8.91  ? 5    VAL F CB  1 
ATOM   4488  C  CG1 . VAL E  1 5   ? 17.286 -24.799 -42.004  1.00 9.93  ? 5    VAL F CG1 1 
ATOM   4489  C  CG2 . VAL E  1 5   ? 16.707 -23.245 -43.896  1.00 10.31 ? 5    VAL F CG2 1 
ATOM   4490  N  N   . CYS E  1 6   ? 15.917 -21.359 -41.584  1.00 10.26 ? 6    CYS F N   1 
ATOM   4491  C  CA  . CYS E  1 6   ? 14.768 -20.957 -40.771  1.00 11.05 ? 6    CYS F CA  1 
ATOM   4492  C  C   . CYS E  1 6   ? 13.544 -20.954 -41.634  1.00 11.86 ? 6    CYS F C   1 
ATOM   4493  O  O   . CYS E  1 6   ? 13.531 -20.326 -42.715  1.00 10.86 ? 6    CYS F O   1 
ATOM   4494  C  CB  . CYS E  1 6   ? 14.973 -19.564 -40.162  1.00 10.77 ? 6    CYS F CB  1 
ATOM   4495  S  SG  . CYS E  1 6   ? 13.557 -18.960 -39.205  1.00 11.88 ? 6    CYS F SG  1 
ATOM   4496  N  N   . VAL E  1 7   ? 12.519 -21.668 -41.158  1.00 12.17 ? 7    VAL F N   1 
ATOM   4497  C  CA  . VAL E  1 7   ? 11.211 -21.620 -41.782  1.00 13.16 ? 7    VAL F CA  1 
ATOM   4498  C  C   . VAL E  1 7   ? 10.374 -20.533 -41.086  1.00 13.28 ? 7    VAL F C   1 
ATOM   4499  O  O   . VAL E  1 7   ? 10.050 -20.647 -39.902  1.00 12.54 ? 7    VAL F O   1 
ATOM   4500  C  CB  . VAL E  1 7   ? 10.503 -23.010 -41.713  1.00 13.50 ? 7    VAL F CB  1 
ATOM   4501  C  CG1 . VAL E  1 7   ? 9.213  -22.999 -42.517  1.00 14.30 ? 7    VAL F CG1 1 
ATOM   4502  C  CG2 . VAL E  1 7   ? 11.451 -24.102 -42.214  1.00 13.41 ? 7    VAL F CG2 1 
ATOM   4503  N  N   . LEU E  1 8   ? 10.033 -19.480 -41.828  1.00 13.97 ? 8    LEU F N   1 
ATOM   4504  C  CA  . LEU E  1 8   ? 9.170  -18.424 -41.289  1.00 15.14 ? 8    LEU F CA  1 
ATOM   4505  C  C   . LEU E  1 8   ? 7.695  -18.776 -41.487  1.00 14.60 ? 8    LEU F C   1 
ATOM   4506  O  O   . LEU E  1 8   ? 7.284  -19.133 -42.589  1.00 14.60 ? 8    LEU F O   1 
ATOM   4507  C  CB  . LEU E  1 8   ? 9.488  -17.071 -41.949  1.00 15.33 ? 8    LEU F CB  1 
ATOM   4508  C  CG  . LEU E  1 8   ? 10.929 -16.531 -41.806  1.00 17.00 ? 8    LEU F CG  1 
ATOM   4509  C  CD1 . LEU E  1 8   ? 11.081 -15.219 -42.559  1.00 19.49 ? 8    LEU F CD1 1 
ATOM   4510  C  CD2 . LEU E  1 8   ? 11.309 -16.329 -40.365  1.00 16.98 ? 8    LEU F CD2 1 
ATOM   4511  N  N   . LYS E  1 9   ? 6.904  -18.674 -40.419  1.00 15.33 ? 9    LYS F N   1 
ATOM   4512  C  CA  . LYS E  1 9   ? 5.461  -18.896 -40.482  1.00 16.47 ? 9    LYS F CA  1 
ATOM   4513  C  C   . LYS E  1 9   ? 4.703  -17.867 -39.635  1.00 16.81 ? 9    LYS F C   1 
ATOM   4514  O  O   . LYS E  1 9   ? 5.236  -17.344 -38.678  1.00 15.48 ? 9    LYS F O   1 
ATOM   4515  C  CB  . LYS E  1 9   ? 5.119  -20.307 -39.977  1.00 17.18 ? 9    LYS F CB  1 
ATOM   4516  C  CG  . LYS E  1 9   ? 5.298  -21.432 -41.009  1.00 20.50 ? 9    LYS F CG  1 
ATOM   4517  C  CD  . LYS E  1 9   ? 4.023  -21.620 -41.839  1.00 25.87 ? 9    LYS F CD  1 
ATOM   4518  C  CE  . LYS E  1 9   ? 4.147  -22.783 -42.823  1.00 27.07 ? 9    LYS F CE  1 
ATOM   4519  N  NZ  . LYS E  1 9   ? 5.188  -22.512 -43.856  1.00 30.42 ? 9    LYS F NZ  1 
ATOM   4520  N  N   . GLY E  1 10  ? 3.446  -17.599 -39.983  1.00 18.42 ? 10   GLY F N   1 
ATOM   4521  C  CA  . GLY E  1 10  ? 2.626  -16.676 -39.194  1.00 20.29 ? 10   GLY F CA  1 
ATOM   4522  C  C   . GLY E  1 10  ? 1.165  -17.100 -39.219  1.00 22.38 ? 10   GLY F C   1 
ATOM   4523  O  O   . GLY E  1 10  ? 0.834  -18.202 -39.656  1.00 22.32 ? 10   GLY F O   1 
ATOM   4524  N  N   . ASP E  1 11  ? 0.295  -16.216 -38.742  1.00 23.97 ? 11   ASP F N   1 
ATOM   4525  C  CA  . ASP E  1 11  ? -1.142 -16.425 -38.814  1.00 25.91 ? 11   ASP F CA  1 
ATOM   4526  C  C   . ASP E  1 11  ? -1.611 -16.259 -40.244  1.00 25.77 ? 11   ASP F C   1 
ATOM   4527  O  O   . ASP E  1 11  ? -2.569 -16.911 -40.684  1.00 26.14 ? 11   ASP F O   1 
ATOM   4528  C  CB  . ASP E  1 11  ? -1.856 -15.410 -37.920  1.00 26.61 ? 11   ASP F CB  1 
ATOM   4529  C  CG  . ASP E  1 11  ? -1.522 -15.587 -36.447  1.00 29.81 ? 11   ASP F CG  1 
ATOM   4530  O  OD1 . ASP E  1 11  ? -1.527 -14.564 -35.720  1.00 31.70 ? 11   ASP F OD1 1 
ATOM   4531  O  OD2 . ASP E  1 11  ? -1.273 -16.747 -36.014  1.00 31.91 ? 11   ASP F OD2 1 
ATOM   4532  N  N   . GLY E  1 12  ? -0.913 -15.396 -40.976  1.00 25.75 ? 12   GLY F N   1 
ATOM   4533  C  CA  . GLY E  1 12  ? -1.366 -14.989 -42.285  1.00 25.00 ? 12   GLY F CA  1 
ATOM   4534  C  C   . GLY E  1 12  ? -0.792 -15.765 -43.448  1.00 24.68 ? 12   GLY F C   1 
ATOM   4535  O  O   . GLY E  1 12  ? -0.360 -16.918 -43.306  1.00 25.33 ? 12   GLY F O   1 
ATOM   4536  N  N   . PRO E  1 13  ? -0.812 -15.145 -44.625  1.00 23.41 ? 13   PRO F N   1 
ATOM   4537  C  CA  . PRO E  1 13  ? -0.166 -15.718 -45.775  1.00 22.25 ? 13   PRO F CA  1 
ATOM   4538  C  C   . PRO E  1 13  ? 1.315  -15.309 -45.826  1.00 20.46 ? 13   PRO F C   1 
ATOM   4539  O  O   . PRO E  1 13  ? 1.972  -15.527 -46.837  1.00 20.20 ? 13   PRO F O   1 
ATOM   4540  C  CB  . PRO E  1 13  ? -0.956 -15.107 -46.934  1.00 22.31 ? 13   PRO F CB  1 
ATOM   4541  C  CG  . PRO E  1 13  ? -1.301 -13.734 -46.438  1.00 23.02 ? 13   PRO F CG  1 
ATOM   4542  C  CD  . PRO E  1 13  ? -1.485 -13.870 -44.945  1.00 23.82 ? 13   PRO F CD  1 
ATOM   4543  N  N   . VAL E  1 14  ? 1.835  -14.720 -44.750  1.00 19.25 ? 14   VAL F N   1 
ATOM   4544  C  CA  . VAL E  1 14  ? 3.259  -14.368 -44.712  1.00 17.48 ? 14   VAL F CA  1 
ATOM   4545  C  C   . VAL E  1 14  ? 4.071  -15.590 -44.290  1.00 16.81 ? 14   VAL F C   1 
ATOM   4546  O  O   . VAL E  1 14  ? 3.970  -16.061 -43.159  1.00 16.16 ? 14   VAL F O   1 
ATOM   4547  C  CB  . VAL E  1 14  ? 3.579  -13.193 -43.774  1.00 17.66 ? 14   VAL F CB  1 
ATOM   4548  C  CG1 . VAL E  1 14  ? 5.057  -12.826 -43.892  1.00 16.55 ? 14   VAL F CG1 1 
ATOM   4549  C  CG2 . VAL E  1 14  ? 2.699  -11.998 -44.110  1.00 17.42 ? 14   VAL F CG2 1 
ATOM   4550  N  N   . GLN E  1 15  ? 4.872  -16.093 -45.221  1.00 16.48 ? 15   GLN F N   1 
ATOM   4551  C  CA  . GLN E  1 15  ? 5.705  -17.269 -44.965  1.00 16.01 ? 15   GLN F CA  1 
ATOM   4552  C  C   . GLN E  1 15  ? 6.934  -17.299 -45.867  1.00 14.30 ? 15   GLN F C   1 
ATOM   4553  O  O   . GLN E  1 15  ? 6.967  -16.689 -46.954  1.00 13.56 ? 15   GLN F O   1 
ATOM   4554  C  CB  . GLN E  1 15  ? 4.895  -18.580 -45.067  1.00 17.31 ? 15   GLN F CB  1 
ATOM   4555  C  CG  . GLN E  1 15  ? 4.309  -18.891 -46.434  1.00 20.48 ? 15   GLN F CG  1 
ATOM   4556  C  CD  . GLN E  1 15  ? 3.268  -20.028 -46.402  1.00 25.68 ? 15   GLN F CD  1 
ATOM   4557  O  OE1 . GLN E  1 15  ? 2.091  -19.814 -46.704  1.00 27.32 ? 15   GLN F OE1 1 
ATOM   4558  N  NE2 . GLN E  1 15  ? 3.701  -21.230 -46.025  1.00 26.29 ? 15   GLN F NE2 1 
ATOM   4559  N  N   . GLY E  1 16  ? 7.950  -18.010 -45.410  1.00 13.08 ? 16   GLY F N   1 
ATOM   4560  C  CA  . GLY E  1 16  ? 9.203  -18.061 -46.175  1.00 12.59 ? 16   GLY F CA  1 
ATOM   4561  C  C   . GLY E  1 16  ? 10.240 -19.004 -45.615  1.00 10.70 ? 16   GLY F C   1 
ATOM   4562  O  O   . GLY E  1 16  ? 10.054 -19.568 -44.543  1.00 10.46 ? 16   GLY F O   1 
ATOM   4563  N  N   . ILE E  1 17  ? 11.326 -19.191 -46.377  1.00 10.41 ? 17   ILE F N   1 
ATOM   4564  C  CA  . ILE E  1 17  ? 12.492 -19.960 -45.913  1.00 8.64  ? 17   ILE F CA  1 
ATOM   4565  C  C   . ILE E  1 17  ? 13.747 -19.083 -46.071  1.00 9.10  ? 17   ILE F C   1 
ATOM   4566  O  O   . ILE E  1 17  ? 13.992 -18.535 -47.147  1.00 8.97  ? 17   ILE F O   1 
ATOM   4567  C  CB  . ILE E  1 17  ? 12.696 -21.275 -46.725  1.00 9.47  ? 17   ILE F CB  1 
ATOM   4568  C  CG1 . ILE E  1 17  ? 11.509 -22.231 -46.516  1.00 10.57 ? 17   ILE F CG1 1 
ATOM   4569  C  CG2 . ILE E  1 17  ? 13.998 -21.944 -46.280  1.00 7.69  ? 17   ILE F CG2 1 
ATOM   4570  C  CD1 . ILE E  1 17  ? 11.379 -23.339 -47.575  1.00 10.59 ? 17   ILE F CD1 1 
ATOM   4571  N  N   . ILE E  1 18  ? 14.517 -18.945 -45.002  1.00 7.74  ? 18   ILE F N   1 
ATOM   4572  C  CA  . ILE E  1 18  ? 15.751 -18.147 -45.037  1.00 8.20  ? 18   ILE F CA  1 
ATOM   4573  C  C   . ILE E  1 18  ? 16.954 -19.035 -44.690  1.00 8.28  ? 18   ILE F C   1 
ATOM   4574  O  O   . ILE E  1 18  ? 16.959 -19.728 -43.682  1.00 8.08  ? 18   ILE F O   1 
ATOM   4575  C  CB  . ILE E  1 18  ? 15.649 -16.913 -44.073  1.00 7.82  ? 18   ILE F CB  1 
ATOM   4576  C  CG1 . ILE E  1 18  ? 14.458 -16.025 -44.446  1.00 8.39  ? 18   ILE F CG1 1 
ATOM   4577  C  CG2 . ILE E  1 18  ? 16.991 -16.137 -43.989  1.00 9.50  ? 18   ILE F CG2 1 
ATOM   4578  C  CD1 . ILE E  1 18  ? 14.626 -15.181 -45.735  1.00 10.82 ? 18   ILE F CD1 1 
ATOM   4579  N  N   . ASN E  1 19  ? 17.969 -18.981 -45.547  1.00 7.60  ? 19   ASN F N   1 
ATOM   4580  C  CA  . ASN E  1 19  ? 19.217 -19.697 -45.399  1.00 8.01  ? 19   ASN F CA  1 
ATOM   4581  C  C   . ASN E  1 19  ? 20.348 -18.816 -44.871  1.00 8.16  ? 19   ASN F C   1 
ATOM   4582  O  O   . ASN E  1 19  ? 20.377 -17.625 -45.156  1.00 8.43  ? 19   ASN F O   1 
ATOM   4583  C  CB  . ASN E  1 19  ? 19.622 -20.217 -46.790  1.00 8.22  ? 19   ASN F CB  1 
ATOM   4584  C  CG  . ASN E  1 19  ? 18.528 -21.033 -47.436  1.00 8.39  ? 19   ASN F CG  1 
ATOM   4585  O  OD1 . ASN E  1 19  ? 18.288 -22.150 -47.030  1.00 10.40 ? 19   ASN F OD1 1 
ATOM   4586  N  ND2 . ASN E  1 19  ? 17.853 -20.468 -48.446  1.00 7.90  ? 19   ASN F ND2 1 
ATOM   4587  N  N   . PHE E  1 20  ? 21.287 -19.417 -44.144  1.00 8.16  ? 20   PHE F N   1 
ATOM   4588  C  CA  . PHE E  1 20  ? 22.457 -18.721 -43.612  1.00 9.72  ? 20   PHE F CA  1 
ATOM   4589  C  C   . PHE E  1 20  ? 23.691 -19.541 -43.969  1.00 9.81  ? 20   PHE F C   1 
ATOM   4590  O  O   . PHE E  1 20  ? 23.646 -20.764 -43.911  1.00 10.37 ? 20   PHE F O   1 
ATOM   4591  C  CB  . PHE E  1 20  ? 22.365 -18.599 -42.079  1.00 9.49  ? 20   PHE F CB  1 
ATOM   4592  C  CG  . PHE E  1 20  ? 21.139 -17.843 -41.572  1.00 10.23 ? 20   PHE F CG  1 
ATOM   4593  C  CD1 . PHE E  1 20  ? 21.237 -16.501 -41.216  1.00 9.63  ? 20   PHE F CD1 1 
ATOM   4594  C  CD2 . PHE E  1 20  ? 19.913 -18.492 -41.398  1.00 9.75  ? 20   PHE F CD2 1 
ATOM   4595  C  CE1 . PHE E  1 20  ? 20.122 -15.797 -40.714  1.00 9.76  ? 20   PHE F CE1 1 
ATOM   4596  C  CE2 . PHE E  1 20  ? 18.791 -17.819 -40.923  1.00 11.71 ? 20   PHE F CE2 1 
ATOM   4597  C  CZ  . PHE E  1 20  ? 18.892 -16.449 -40.561  1.00 9.77  ? 20   PHE F CZ  1 
ATOM   4598  N  N   . GLU E  1 21  ? 24.789 -18.887 -44.344  1.00 9.86  ? 21   GLU F N   1 
ATOM   4599  C  CA  . GLU E  1 21  ? 26.032 -19.596 -44.588  1.00 10.08 ? 21   GLU F CA  1 
ATOM   4600  C  C   . GLU E  1 21  ? 27.215 -18.788 -44.142  1.00 10.55 ? 21   GLU F C   1 
ATOM   4601  O  O   . GLU E  1 21  ? 27.324 -17.596 -44.442  1.00 10.72 ? 21   GLU F O   1 
ATOM   4602  C  CB  . GLU E  1 21  ? 26.232 -19.996 -46.066  1.00 10.48 ? 21   GLU F CB  1 
ATOM   4603  C  CG  . GLU E  1 21  ? 27.526 -20.856 -46.241  1.00 11.23 ? 21   GLU F CG  1 
ATOM   4604  C  CD  . GLU E  1 21  ? 27.668 -21.524 -47.612  1.00 16.51 ? 21   GLU F CD  1 
ATOM   4605  O  OE1 . GLU E  1 21  ? 26.712 -21.488 -48.410  1.00 15.10 ? 21   GLU F OE1 1 
ATOM   4606  O  OE2 . GLU E  1 21  ? 28.755 -22.087 -47.875  1.00 17.40 ? 21   GLU F OE2 1 
ATOM   4607  N  N   . GLN E  1 22  ? 28.125 -19.451 -43.448  1.00 11.82 ? 22   GLN F N   1 
ATOM   4608  C  CA  . GLN E  1 22  ? 29.312 -18.773 -42.963  1.00 13.37 ? 22   GLN F CA  1 
ATOM   4609  C  C   . GLN E  1 22  ? 30.528 -19.601 -43.326  1.00 14.88 ? 22   GLN F C   1 
ATOM   4610  O  O   . GLN E  1 22  ? 30.801 -20.623 -42.686  1.00 15.65 ? 22   GLN F O   1 
ATOM   4611  C  CB  . GLN E  1 22  ? 29.197 -18.541 -41.444  1.00 12.50 ? 22   GLN F CB  1 
ATOM   4612  C  CG  . GLN E  1 22  ? 30.142 -17.482 -40.888  1.00 12.01 ? 22   GLN F CG  1 
ATOM   4613  C  CD  . GLN E  1 22  ? 30.032 -17.312 -39.367  1.00 12.00 ? 22   GLN F CD  1 
ATOM   4614  O  OE1 . GLN E  1 22  ? 29.423 -18.130 -38.662  1.00 12.75 ? 22   GLN F OE1 1 
ATOM   4615  N  NE2 . GLN E  1 22  ? 30.629 -16.241 -38.861  1.00 14.43 ? 22   GLN F NE2 1 
ATOM   4616  N  N   . LYS E  1 23  ? 31.249 -19.153 -44.354  1.00 16.89 ? 23   LYS F N   1 
ATOM   4617  C  CA  . LYS E  1 23  ? 32.458 -19.831 -44.845  1.00 19.04 ? 23   LYS F CA  1 
ATOM   4618  C  C   . LYS E  1 23  ? 33.507 -20.056 -43.744  1.00 20.17 ? 23   LYS F C   1 
ATOM   4619  O  O   . LYS E  1 23  ? 34.063 -21.153 -43.596  1.00 19.86 ? 23   LYS F O   1 
ATOM   4620  C  CB  . LYS E  1 23  ? 33.078 -19.023 -45.990  1.00 19.54 ? 23   LYS F CB  1 
ATOM   4621  C  CG  . LYS E  1 23  ? 34.268 -19.696 -46.722  1.00 22.74 ? 23   LYS F CG  1 
ATOM   4622  C  CD  . LYS E  1 23  ? 33.856 -20.882 -47.614  1.00 26.76 ? 23   LYS F CD  1 
ATOM   4623  C  CE  . LYS E  1 23  ? 32.685 -20.561 -48.560  1.00 28.51 ? 23   LYS F CE  1 
ATOM   4624  N  NZ  . LYS E  1 23  ? 31.345 -20.742 -47.907  1.00 28.92 ? 23   LYS F NZ  1 
ATOM   4625  N  N   . GLU E  1 24  ? 33.767 -19.002 -42.983  1.00 20.99 ? 24   GLU F N   1 
ATOM   4626  C  CA  . GLU E  1 24  ? 34.785 -19.030 -41.934  1.00 22.02 ? 24   GLU F CA  1 
ATOM   4627  C  C   . GLU E  1 24  ? 34.255 -18.407 -40.648  1.00 21.74 ? 24   GLU F C   1 
ATOM   4628  O  O   . GLU E  1 24  ? 33.437 -17.487 -40.699  1.00 21.59 ? 24   GLU F O   1 
ATOM   4629  C  CB  . GLU E  1 24  ? 36.058 -18.343 -42.424  1.00 22.50 ? 24   GLU F CB  1 
ATOM   4630  C  CG  . GLU E  1 24  ? 36.914 -19.273 -43.283  1.00 26.27 ? 24   GLU F CG  1 
ATOM   4631  C  CD  . GLU E  1 24  ? 37.509 -18.615 -44.521  1.00 31.67 ? 24   GLU F CD  1 
ATOM   4632  O  OE1 . GLU E  1 24  ? 37.508 -19.266 -45.597  1.00 33.91 ? 24   GLU F OE1 1 
ATOM   4633  O  OE2 . GLU E  1 24  ? 37.987 -17.459 -44.432  1.00 34.58 ? 24   GLU F OE2 1 
ATOM   4634  N  N   . SER E  1 25  ? 34.691 -18.935 -39.499  1.00 21.53 ? 25   SER F N   1 
ATOM   4635  C  CA  . SER E  1 25  ? 34.205 -18.457 -38.194  1.00 21.95 ? 25   SER F CA  1 
ATOM   4636  C  C   . SER E  1 25  ? 34.513 -16.967 -37.995  1.00 21.29 ? 25   SER F C   1 
ATOM   4637  O  O   . SER E  1 25  ? 33.793 -16.272 -37.284  1.00 21.84 ? 25   SER F O   1 
ATOM   4638  C  CB  . SER E  1 25  ? 34.817 -19.276 -37.059  1.00 21.77 ? 25   SER F CB  1 
ATOM   4639  O  OG  . SER E  1 25  ? 36.210 -19.038 -36.995  1.00 22.49 ? 25   SER F OG  1 
ATOM   4640  N  N   . ASN E  1 26  ? 35.573 -16.494 -38.648  1.00 20.97 ? 26   ASN F N   1 
ATOM   4641  C  CA  . ASN E  1 26  ? 35.946 -15.064 -38.655  1.00 21.33 ? 26   ASN F CA  1 
ATOM   4642  C  C   . ASN E  1 26  ? 35.364 -14.263 -39.823  1.00 20.61 ? 26   ASN F C   1 
ATOM   4643  O  O   . ASN E  1 26  ? 35.776 -13.117 -40.078  1.00 21.64 ? 26   ASN F O   1 
ATOM   4644  C  CB  . ASN E  1 26  ? 37.476 -14.909 -38.661  1.00 21.45 ? 26   ASN F CB  1 
ATOM   4645  C  CG  . ASN E  1 26  ? 38.125 -15.372 -39.976  1.00 23.50 ? 26   ASN F CG  1 
ATOM   4646  O  OD1 . ASN E  1 26  ? 37.497 -16.047 -40.794  1.00 25.83 ? 26   ASN F OD1 1 
ATOM   4647  N  ND2 . ASN E  1 26  ? 39.395 -15.012 -40.171  1.00 23.37 ? 26   ASN F ND2 1 
ATOM   4648  N  N   . GLY E  1 27  ? 34.432 -14.866 -40.554  1.00 19.34 ? 27   GLY F N   1 
ATOM   4649  C  CA  . GLY E  1 27  ? 33.926 -14.231 -41.763  1.00 17.48 ? 27   GLY F CA  1 
ATOM   4650  C  C   . GLY E  1 27  ? 32.484 -13.760 -41.676  1.00 15.46 ? 27   GLY F C   1 
ATOM   4651  O  O   . GLY E  1 27  ? 31.781 -14.027 -40.700  1.00 15.28 ? 27   GLY F O   1 
ATOM   4652  N  N   . PRO E  1 28  ? 32.030 -13.048 -42.714  1.00 13.69 ? 28   PRO F N   1 
ATOM   4653  C  CA  . PRO E  1 28  ? 30.646 -12.619 -42.805  1.00 12.24 ? 28   PRO F CA  1 
ATOM   4654  C  C   . PRO E  1 28  ? 29.678 -13.807 -42.894  1.00 10.63 ? 28   PRO F C   1 
ATOM   4655  O  O   . PRO E  1 28  ? 30.071 -14.905 -43.288  1.00 10.63 ? 28   PRO F O   1 
ATOM   4656  C  CB  . PRO E  1 28  ? 30.604 -11.846 -44.128  1.00 12.02 ? 28   PRO F CB  1 
ATOM   4657  C  CG  . PRO E  1 28  ? 32.000 -11.698 -44.572  1.00 12.37 ? 28   PRO F CG  1 
ATOM   4658  C  CD  . PRO E  1 28  ? 32.770 -12.797 -43.958  1.00 14.12 ? 28   PRO F CD  1 
ATOM   4659  N  N   . VAL E  1 29  ? 28.419 -13.566 -42.543  1.00 9.09  ? 29   VAL F N   1 
ATOM   4660  C  CA  . VAL E  1 29  ? 27.356 -14.526 -42.753  1.00 7.81  ? 29   VAL F CA  1 
ATOM   4661  C  C   . VAL E  1 29  ? 26.490 -14.074 -43.911  1.00 8.02  ? 29   VAL F C   1 
ATOM   4662  O  O   . VAL E  1 29  ? 25.964 -12.950 -43.899  1.00 7.11  ? 29   VAL F O   1 
ATOM   4663  C  CB  . VAL E  1 29  ? 26.470 -14.663 -41.501  1.00 6.66  ? 29   VAL F CB  1 
ATOM   4664  C  CG1 . VAL E  1 29  ? 25.367 -15.658 -41.744  1.00 8.66  ? 29   VAL F CG1 1 
ATOM   4665  C  CG2 . VAL E  1 29  ? 27.332 -15.041 -40.296  1.00 6.80  ? 29   VAL F CG2 1 
ATOM   4666  N  N   . LYS E  1 30  ? 26.319 -14.945 -44.901  1.00 7.88  ? 30   LYS F N   1 
ATOM   4667  C  CA  . LYS E  1 30  ? 25.421 -14.642 -46.016  1.00 7.51  ? 30   LYS F CA  1 
ATOM   4668  C  C   . LYS E  1 30  ? 24.015 -15.128 -45.675  1.00 7.21  ? 30   LYS F C   1 
ATOM   4669  O  O   . LYS E  1 30  ? 23.843 -16.240 -45.194  1.00 6.23  ? 30   LYS F O   1 
ATOM   4670  C  CB  . LYS E  1 30  ? 25.926 -15.324 -47.288  1.00 9.03  ? 30   LYS F CB  1 
ATOM   4671  C  CG  . LYS E  1 30  ? 27.224 -14.672 -47.815  1.00 11.36 ? 30   LYS F CG  1 
ATOM   4672  C  CD  . LYS E  1 30  ? 27.838 -15.458 -48.975  1.00 18.12 ? 30   LYS F CD  1 
ATOM   4673  C  CE  . LYS E  1 30  ? 29.217 -14.895 -49.326  1.00 19.59 ? 30   LYS F CE  1 
ATOM   4674  N  NZ  . LYS E  1 30  ? 29.884 -15.687 -50.407  1.00 24.01 ? 30   LYS F NZ  1 
ATOM   4675  N  N   . VAL E  1 31  ? 23.025 -14.286 -45.933  1.00 6.89  ? 31   VAL F N   1 
ATOM   4676  C  CA  . VAL E  1 31  ? 21.651 -14.552 -45.546  1.00 7.05  ? 31   VAL F CA  1 
ATOM   4677  C  C   . VAL E  1 31  ? 20.791 -14.405 -46.780  1.00 7.13  ? 31   VAL F C   1 
ATOM   4678  O  O   . VAL E  1 31  ? 20.780 -13.343 -47.408  1.00 8.26  ? 31   VAL F O   1 
ATOM   4679  C  CB  . VAL E  1 31  ? 21.153 -13.571 -44.453  1.00 6.68  ? 31   VAL F CB  1 
ATOM   4680  C  CG1 . VAL E  1 31  ? 19.770 -14.000 -43.948  1.00 6.21  ? 31   VAL F CG1 1 
ATOM   4681  C  CG2 . VAL E  1 31  ? 22.119 -13.493 -43.287  1.00 5.49  ? 31   VAL F CG2 1 
ATOM   4682  N  N   . TRP E  1 32  ? 20.058 -15.459 -47.147  1.00 6.88  ? 32   TRP F N   1 
ATOM   4683  C  CA  . TRP E  1 32  ? 19.250 -15.377 -48.363  1.00 7.47  ? 32   TRP F CA  1 
ATOM   4684  C  C   . TRP E  1 32  ? 18.067 -16.333 -48.338  1.00 6.74  ? 32   TRP F C   1 
ATOM   4685  O  O   . TRP E  1 32  ? 18.111 -17.361 -47.656  1.00 7.52  ? 32   TRP F O   1 
ATOM   4686  C  CB  . TRP E  1 32  ? 20.106 -15.631 -49.624  1.00 7.45  ? 32   TRP F CB  1 
ATOM   4687  C  CG  . TRP E  1 32  ? 20.407 -17.101 -49.881  1.00 8.67  ? 32   TRP F CG  1 
ATOM   4688  C  CD1 . TRP E  1 32  ? 19.749 -17.933 -50.760  1.00 8.98  ? 32   TRP F CD1 1 
ATOM   4689  C  CD2 . TRP E  1 32  ? 21.412 -17.902 -49.241  1.00 9.60  ? 32   TRP F CD2 1 
ATOM   4690  N  NE1 . TRP E  1 32  ? 20.305 -19.198 -50.711  1.00 11.53 ? 32   TRP F NE1 1 
ATOM   4691  C  CE2 . TRP E  1 32  ? 21.318 -19.206 -49.783  1.00 9.22  ? 32   TRP F CE2 1 
ATOM   4692  C  CE3 . TRP E  1 32  ? 22.383 -17.643 -48.259  1.00 10.30 ? 32   TRP F CE3 1 
ATOM   4693  C  CZ2 . TRP E  1 32  ? 22.170 -20.254 -49.385  1.00 8.75  ? 32   TRP F CZ2 1 
ATOM   4694  C  CZ3 . TRP E  1 32  ? 23.234 -18.679 -47.859  1.00 11.94 ? 32   TRP F CZ3 1 
ATOM   4695  C  CH2 . TRP E  1 32  ? 23.113 -19.979 -48.422  1.00 11.33 ? 32   TRP F CH2 1 
ATOM   4696  N  N   . GLY E  1 33  ? 17.035 -15.992 -49.103  1.00 8.12  ? 33   GLY F N   1 
ATOM   4697  C  CA  . GLY E  1 33  ? 15.826 -16.822 -49.226  1.00 9.36  ? 33   GLY F CA  1 
ATOM   4698  C  C   . GLY E  1 33  ? 14.650 -16.005 -49.683  1.00 10.44 ? 33   GLY F C   1 
ATOM   4699  O  O   . GLY E  1 33  ? 14.819 -14.885 -50.155  1.00 11.11 ? 33   GLY F O   1 
ATOM   4700  N  N   . SER E  1 34  ? 13.454 -16.561 -49.550  1.00 10.82 ? 34   SER F N   1 
ATOM   4701  C  CA  . SER E  1 34  ? 12.245 -15.916 -50.048  1.00 12.36 ? 34   SER F CA  1 
ATOM   4702  C  C   . SER E  1 34  ? 11.194 -15.756 -48.961  1.00 12.31 ? 34   SER F C   1 
ATOM   4703  O  O   . SER E  1 34  ? 11.002 -16.670 -48.167  1.00 12.94 ? 34   SER F O   1 
ATOM   4704  C  CB  . SER E  1 34  ? 11.639 -16.763 -51.157  1.00 11.93 ? 34   SER F CB  1 
ATOM   4705  O  OG  . SER E  1 34  ? 10.827 -15.950 -51.956  1.00 16.12 ? 34   SER F OG  1 
ATOM   4706  N  N   . ILE E  1 35  ? 10.530 -14.598 -48.918  1.00 11.73 ? 35   ILE F N   1 
ATOM   4707  C  CA  . ILE E  1 35  ? 9.350  -14.426 -48.063  1.00 11.68 ? 35   ILE F CA  1 
ATOM   4708  C  C   . ILE E  1 35  ? 8.227  -13.885 -48.919  1.00 12.09 ? 35   ILE F C   1 
ATOM   4709  O  O   . ILE E  1 35  ? 8.374  -12.840 -49.559  1.00 13.22 ? 35   ILE F O   1 
ATOM   4710  C  CB  . ILE E  1 35  ? 9.583  -13.484 -46.849  1.00 11.34 ? 35   ILE F CB  1 
ATOM   4711  C  CG1 . ILE E  1 35  ? 10.807 -13.928 -46.034  1.00 11.31 ? 35   ILE F CG1 1 
ATOM   4712  C  CG2 . ILE E  1 35  ? 8.347  -13.496 -45.947  1.00 11.88 ? 35   ILE F CG2 1 
ATOM   4713  C  CD1 . ILE E  1 35  ? 11.334 -12.836 -45.024  1.00 10.55 ? 35   ILE F CD1 1 
ATOM   4714  N  N   . LYS E  1 36  ? 7.099  -14.588 -48.912  1.00 12.07 ? 36   LYS F N   1 
ATOM   4715  C  CA  . LYS E  1 36  ? 5.953  -14.225 -49.726  1.00 12.92 ? 36   LYS F CA  1 
ATOM   4716  C  C   . LYS E  1 36  ? 4.820  -13.671 -48.844  1.00 13.11 ? 36   LYS F C   1 
ATOM   4717  O  O   . LYS E  1 36  ? 4.851  -13.807 -47.614  1.00 12.61 ? 36   LYS F O   1 
ATOM   4718  C  CB  . LYS E  1 36  ? 5.459  -15.462 -50.512  1.00 13.30 ? 36   LYS F CB  1 
ATOM   4719  C  CG  . LYS E  1 36  ? 4.883  -16.602 -49.656  1.00 15.89 ? 36   LYS F CG  1 
ATOM   4720  C  CD  . LYS E  1 36  ? 4.296  -17.707 -50.570  1.00 19.89 ? 36   LYS F CD  1 
ATOM   4721  C  CE  . LYS E  1 36  ? 3.454  -18.713 -49.802  1.00 21.85 ? 36   LYS F CE  1 
ATOM   4722  N  NZ  . LYS E  1 36  ? 2.761  -19.670 -50.723  1.00 25.75 ? 36   LYS F NZ  1 
ATOM   4723  N  N   . GLY E  1 37  ? 3.812  -13.080 -49.484  1.00 12.87 ? 37   GLY F N   1 
ATOM   4724  C  CA  . GLY E  1 37  ? 2.622  -12.630 -48.760  1.00 14.02 ? 37   GLY F CA  1 
ATOM   4725  C  C   . GLY E  1 37  ? 2.733  -11.299 -48.034  1.00 12.99 ? 37   GLY F C   1 
ATOM   4726  O  O   . GLY E  1 37  ? 1.838  -10.939 -47.275  1.00 14.26 ? 37   GLY F O   1 
ATOM   4727  N  N   . LEU E  1 38  ? 3.818  -10.567 -48.265  1.00 12.55 ? 38   LEU F N   1 
ATOM   4728  C  CA  . LEU E  1 38  ? 4.058  -9.285  -47.618  1.00 11.37 ? 38   LEU F CA  1 
ATOM   4729  C  C   . LEU E  1 38  ? 3.465  -8.162  -48.435  1.00 11.92 ? 38   LEU F C   1 
ATOM   4730  O  O   . LEU E  1 38  ? 3.286  -8.297  -49.644  1.00 11.80 ? 38   LEU F O   1 
ATOM   4731  C  CB  . LEU E  1 38  ? 5.575  -9.031  -47.497  1.00 11.01 ? 38   LEU F CB  1 
ATOM   4732  C  CG  . LEU E  1 38  ? 6.353  -9.964  -46.562  1.00 9.02  ? 38   LEU F CG  1 
ATOM   4733  C  CD1 . LEU E  1 38  ? 7.885  -9.849  -46.801  1.00 9.61  ? 38   LEU F CD1 1 
ATOM   4734  C  CD2 . LEU E  1 38  ? 6.016  -9.666  -45.116  1.00 7.73  ? 38   LEU F CD2 1 
ATOM   4735  N  N   . THR E  1 39  ? 3.187  -7.041  -47.774  1.00 12.15 ? 39   THR F N   1 
ATOM   4736  C  CA  . THR E  1 39  ? 2.873  -5.806  -48.474  1.00 11.98 ? 39   THR F CA  1 
ATOM   4737  C  C   . THR E  1 39  ? 4.141  -5.242  -49.132  1.00 12.18 ? 39   THR F C   1 
ATOM   4738  O  O   . THR E  1 39  ? 5.198  -5.167  -48.501  1.00 11.85 ? 39   THR F O   1 
ATOM   4739  C  CB  . THR E  1 39  ? 2.282  -4.752  -47.490  1.00 12.54 ? 39   THR F CB  1 
ATOM   4740  O  OG1 . THR E  1 39  ? 1.003  -5.206  -47.007  1.00 12.74 ? 39   THR F OG1 1 
ATOM   4741  C  CG2 . THR E  1 39  ? 2.134  -3.398  -48.147  1.00 12.50 ? 39   THR F CG2 1 
ATOM   4742  N  N   . GLU E  1 40  ? 4.020  -4.821  -50.389  1.00 11.56 ? 40   GLU F N   1 
ATOM   4743  C  CA  . GLU E  1 40  ? 5.127  -4.181  -51.090  1.00 12.04 ? 40   GLU F CA  1 
ATOM   4744  C  C   . GLU E  1 40  ? 5.745  -3.071  -50.248  1.00 11.78 ? 40   GLU F C   1 
ATOM   4745  O  O   . GLU E  1 40  ? 5.029  -2.225  -49.681  1.00 11.81 ? 40   GLU F O   1 
ATOM   4746  C  CB  . GLU E  1 40  ? 4.689  -3.633  -52.447  1.00 11.95 ? 40   GLU F CB  1 
ATOM   4747  C  CG  . GLU E  1 40  ? 5.850  -3.069  -53.255  1.00 14.60 ? 40   GLU F CG  1 
ATOM   4748  C  CD  . GLU E  1 40  ? 5.442  -2.449  -54.570  1.00 18.44 ? 40   GLU F CD  1 
ATOM   4749  O  OE1 . GLU E  1 40  ? 6.353  -2.141  -55.385  1.00 18.17 ? 40   GLU F OE1 1 
ATOM   4750  O  OE2 . GLU E  1 40  ? 4.221  -2.275  -54.798  1.00 18.76 ? 40   GLU F OE2 1 
ATOM   4751  N  N   . GLY E  1 41  ? 7.072  -3.104  -50.150  1.00 11.23 ? 41   GLY F N   1 
ATOM   4752  C  CA  . GLY E  1 41  ? 7.809  -2.127  -49.379  1.00 10.94 ? 41   GLY F CA  1 
ATOM   4753  C  C   . GLY E  1 41  ? 8.664  -2.709  -48.273  1.00 10.68 ? 41   GLY F C   1 
ATOM   4754  O  O   . GLY E  1 41  ? 8.927  -3.912  -48.242  1.00 11.04 ? 41   GLY F O   1 
ATOM   4755  N  N   . LEU E  1 42  ? 9.114  -1.840  -47.374  1.00 10.08 ? 42   LEU F N   1 
ATOM   4756  C  CA  . LEU E  1 42  ? 10.094 -2.224  -46.348  1.00 9.96  ? 42   LEU F CA  1 
ATOM   4757  C  C   . LEU E  1 42  ? 9.471  -2.929  -45.191  1.00 9.35  ? 42   LEU F C   1 
ATOM   4758  O  O   . LEU E  1 42  ? 8.404  -2.511  -44.712  1.00 9.26  ? 42   LEU F O   1 
ATOM   4759  C  CB  . LEU E  1 42  ? 10.828 -0.993  -45.790  1.00 10.07 ? 42   LEU F CB  1 
ATOM   4760  C  CG  . LEU E  1 42  ? 11.762 -0.235  -46.728  1.00 11.42 ? 42   LEU F CG  1 
ATOM   4761  C  CD1 . LEU E  1 42  ? 12.122 1.114   -46.108  1.00 12.16 ? 42   LEU F CD1 1 
ATOM   4762  C  CD2 . LEU E  1 42  ? 13.043 -1.056  -47.002  1.00 10.16 ? 42   LEU F CD2 1 
ATOM   4763  N  N   . HIS E  1 43  ? 10.172 -3.965  -44.718  1.00 7.64  ? 43   HIS F N   1 
ATOM   4764  C  CA  . HIS E  1 43  ? 9.798  -4.731  -43.525  1.00 7.42  ? 43   HIS F CA  1 
ATOM   4765  C  C   . HIS E  1 43  ? 10.967 -5.000  -42.611  1.00 7.76  ? 43   HIS F C   1 
ATOM   4766  O  O   . HIS E  1 43  ? 11.994 -5.472  -43.079  1.00 8.21  ? 43   HIS F O   1 
ATOM   4767  C  CB  . HIS E  1 43  ? 9.125  -6.047  -43.914  1.00 7.55  ? 43   HIS F CB  1 
ATOM   4768  C  CG  . HIS E  1 43  ? 7.831  -5.841  -44.617  1.00 7.69  ? 43   HIS F CG  1 
ATOM   4769  N  ND1 . HIS E  1 43  ? 6.631  -5.746  -43.946  1.00 9.26  ? 43   HIS F ND1 1 
ATOM   4770  C  CD2 . HIS E  1 43  ? 7.551  -5.668  -45.931  1.00 11.85 ? 43   HIS F CD2 1 
ATOM   4771  C  CE1 . HIS E  1 43  ? 5.664  -5.520  -44.820  1.00 11.89 ? 43   HIS F CE1 1 
ATOM   4772  N  NE2 . HIS E  1 43  ? 6.192  -5.478  -46.031  1.00 12.11 ? 43   HIS F NE2 1 
ATOM   4773  N  N   . GLY E  1 44  ? 10.804 -4.683  -41.315  1.00 7.85  ? 44   GLY F N   1 
ATOM   4774  C  CA  . GLY E  1 44  ? 11.787 -4.959  -40.258  1.00 7.40  ? 44   GLY F CA  1 
ATOM   4775  C  C   . GLY E  1 44  ? 12.138 -6.422  -40.144  1.00 8.68  ? 44   GLY F C   1 
ATOM   4776  O  O   . GLY E  1 44  ? 11.280 -7.267  -40.347  1.00 7.69  ? 44   GLY F O   1 
ATOM   4777  N  N   . PHE E  1 45  ? 13.404 -6.727  -39.821  1.00 8.50  ? 45   PHE F N   1 
ATOM   4778  C  CA  . PHE E  1 45  ? 13.963 -8.073  -40.058  1.00 9.42  ? 45   PHE F CA  1 
ATOM   4779  C  C   . PHE E  1 45  ? 15.079 -8.273  -39.061  1.00 9.27  ? 45   PHE F C   1 
ATOM   4780  O  O   . PHE E  1 45  ? 16.150 -7.667  -39.186  1.00 10.97 ? 45   PHE F O   1 
ATOM   4781  C  CB  . PHE E  1 45  ? 14.493 -8.204  -41.514  1.00 8.82  ? 45   PHE F CB  1 
ATOM   4782  C  CG  . PHE E  1 45  ? 14.899 -9.614  -41.925  1.00 10.99 ? 45   PHE F CG  1 
ATOM   4783  C  CD1 . PHE E  1 45  ? 13.928 -10.596 -42.151  1.00 9.91  ? 45   PHE F CD1 1 
ATOM   4784  C  CD2 . PHE E  1 45  ? 16.241 -9.949  -42.120  1.00 8.89  ? 45   PHE F CD2 1 
ATOM   4785  C  CE1 . PHE E  1 45  ? 14.292 -11.882 -42.553  1.00 12.39 ? 45   PHE F CE1 1 
ATOM   4786  C  CE2 . PHE E  1 45  ? 16.616 -11.236 -42.527  1.00 10.44 ? 45   PHE F CE2 1 
ATOM   4787  C  CZ  . PHE E  1 45  ? 15.631 -12.199 -42.753  1.00 11.97 ? 45   PHE F CZ  1 
ATOM   4788  N  N   . HIS E  1 46  ? 14.827 -9.067  -38.032  1.00 8.84  ? 46   HIS F N   1 
ATOM   4789  C  CA  . HIS E  1 46  ? 15.769 -9.165  -36.923  1.00 8.27  ? 46   HIS F CA  1 
ATOM   4790  C  C   . HIS E  1 46  ? 15.830 -10.565 -36.379  1.00 8.21  ? 46   HIS F C   1 
ATOM   4791  O  O   . HIS E  1 46  ? 14.869 -11.349 -36.498  1.00 8.55  ? 46   HIS F O   1 
ATOM   4792  C  CB  . HIS E  1 46  ? 15.380 -8.236  -35.716  1.00 7.81  ? 46   HIS F CB  1 
ATOM   4793  C  CG  . HIS E  1 46  ? 14.806 -6.909  -36.104  1.00 9.04  ? 46   HIS F CG  1 
ATOM   4794  N  ND1 . HIS E  1 46  ? 13.483 -6.572  -35.898  1.00 7.69  ? 46   HIS F ND1 1 
ATOM   4795  C  CD2 . HIS E  1 46  ? 15.381 -5.824  -36.686  1.00 9.91  ? 46   HIS F CD2 1 
ATOM   4796  C  CE1 . HIS E  1 46  ? 13.264 -5.345  -36.347  1.00 10.34 ? 46   HIS F CE1 1 
ATOM   4797  N  NE2 . HIS E  1 46  ? 14.395 -4.875  -36.843  1.00 9.55  ? 46   HIS F NE2 1 
ATOM   4798  N  N   . VAL E  1 47  ? 16.949 -10.854 -35.728  1.00 8.03  ? 47   VAL F N   1 
ATOM   4799  C  CA  . VAL E  1 47  ? 17.046 -12.005 -34.869  1.00 8.35  ? 47   VAL F CA  1 
ATOM   4800  C  C   . VAL E  1 47  ? 16.684 -11.570 -33.448  1.00 9.13  ? 47   VAL F C   1 
ATOM   4801  O  O   . VAL E  1 47  ? 17.306 -10.673 -32.902  1.00 9.55  ? 47   VAL F O   1 
ATOM   4802  C  CB  . VAL E  1 47  ? 18.474 -12.548 -34.856  1.00 7.09  ? 47   VAL F CB  1 
ATOM   4803  C  CG1 . VAL E  1 47  ? 18.572 -13.752 -33.929  1.00 6.66  ? 47   VAL F CG1 1 
ATOM   4804  C  CG2 . VAL E  1 47  ? 18.894 -12.932 -36.284  1.00 8.69  ? 47   VAL F CG2 1 
ATOM   4805  N  N   . HIS E  1 48  ? 15.682 -12.216 -32.860  1.00 10.33 ? 48   HIS F N   1 
ATOM   4806  C  CA  . HIS E  1 48  ? 15.290 -11.939 -31.479  1.00 10.68 ? 48   HIS F CA  1 
ATOM   4807  C  C   . HIS E  1 48  ? 15.893 -12.945 -30.524  1.00 11.14 ? 48   HIS F C   1 
ATOM   4808  O  O   . HIS E  1 48  ? 16.315 -14.016 -30.940  1.00 11.33 ? 48   HIS F O   1 
ATOM   4809  C  CB  . HIS E  1 48  ? 13.786 -11.921 -31.345  1.00 11.20 ? 48   HIS F CB  1 
ATOM   4810  C  CG  . HIS E  1 48  ? 13.141 -10.781 -32.068  1.00 12.89 ? 48   HIS F CG  1 
ATOM   4811  N  ND1 . HIS E  1 48  ? 12.164 -9.990  -31.498  1.00 11.78 ? 48   HIS F ND1 1 
ATOM   4812  C  CD2 . HIS E  1 48  ? 13.341 -10.299 -33.315  1.00 12.75 ? 48   HIS F CD2 1 
ATOM   4813  C  CE1 . HIS E  1 48  ? 11.754 -9.103  -32.386  1.00 10.09 ? 48   HIS F CE1 1 
ATOM   4814  N  NE2 . HIS E  1 48  ? 12.467 -9.264  -33.492  1.00 12.76 ? 48   HIS F NE2 1 
ATOM   4815  N  N   . GLU E  1 49  ? 15.902 -12.605 -29.244  1.00 10.78 ? 49   GLU F N   1 
ATOM   4816  C  CA  . GLU E  1 49  ? 16.727 -13.304 -28.268  1.00 11.77 ? 49   GLU F CA  1 
ATOM   4817  C  C   . GLU E  1 49  ? 16.394 -14.792 -28.091  1.00 12.12 ? 49   GLU F C   1 
ATOM   4818  O  O   . GLU E  1 49  ? 17.303 -15.629 -27.988  1.00 12.59 ? 49   GLU F O   1 
ATOM   4819  C  CB  . GLU E  1 49  ? 16.595 -12.618 -26.916  1.00 11.01 ? 49   GLU F CB  1 
ATOM   4820  C  CG  . GLU E  1 49  ? 17.638 -13.058 -25.925  1.00 11.08 ? 49   GLU F CG  1 
ATOM   4821  C  CD  . GLU E  1 49  ? 17.547 -12.276 -24.625  1.00 13.60 ? 49   GLU F CD  1 
ATOM   4822  O  OE1 . GLU E  1 49  ? 18.349 -12.584 -23.699  1.00 11.84 ? 49   GLU F OE1 1 
ATOM   4823  O  OE2 . GLU E  1 49  ? 16.676 -11.370 -24.553  1.00 13.55 ? 49   GLU F OE2 1 
ATOM   4824  N  N   . PHE E  1 50  ? 15.104 -15.107 -27.992  1.00 13.12 ? 50   PHE F N   1 
ATOM   4825  C  CA  . PHE E  1 50  ? 14.708 -16.491 -27.689  1.00 13.69 ? 50   PHE F CA  1 
ATOM   4826  C  C   . PHE E  1 50  ? 14.141 -17.283 -28.871  1.00 13.81 ? 50   PHE F C   1 
ATOM   4827  O  O   . PHE E  1 50  ? 13.351 -16.759 -29.668  1.00 13.70 ? 50   PHE F O   1 
ATOM   4828  C  CB  . PHE E  1 50  ? 13.716 -16.519 -26.526  1.00 13.76 ? 50   PHE F CB  1 
ATOM   4829  C  CG  . PHE E  1 50  ? 14.104 -15.624 -25.391  1.00 14.52 ? 50   PHE F CG  1 
ATOM   4830  C  CD1 . PHE E  1 50  ? 15.304 -15.830 -24.700  1.00 14.72 ? 50   PHE F CD1 1 
ATOM   4831  C  CD2 . PHE E  1 50  ? 13.293 -14.551 -25.033  1.00 16.21 ? 50   PHE F CD2 1 
ATOM   4832  C  CE1 . PHE E  1 50  ? 15.676 -14.994 -23.659  1.00 15.22 ? 50   PHE F CE1 1 
ATOM   4833  C  CE2 . PHE E  1 50  ? 13.661 -13.701 -23.986  1.00 17.10 ? 50   PHE F CE2 1 
ATOM   4834  C  CZ  . PHE E  1 50  ? 14.857 -13.925 -23.306  1.00 15.80 ? 50   PHE F CZ  1 
ATOM   4835  N  N   . GLY E  1 51  ? 14.541 -18.547 -28.959  1.00 13.56 ? 51   GLY F N   1 
ATOM   4836  C  CA  . GLY E  1 51  ? 13.976 -19.477 -29.934  1.00 13.78 ? 51   GLY F CA  1 
ATOM   4837  C  C   . GLY E  1 51  ? 12.763 -20.174 -29.345  1.00 14.28 ? 51   GLY F C   1 
ATOM   4838  O  O   . GLY E  1 51  ? 12.629 -21.398 -29.419  1.00 13.45 ? 51   GLY F O   1 
ATOM   4839  N  N   . ASP E  1 52  ? 11.902 -19.366 -28.736  1.00 15.63 ? 52   ASP F N   1 
ATOM   4840  C  CA  . ASP E  1 52  ? 10.759 -19.803 -27.981  1.00 16.33 ? 52   ASP F CA  1 
ATOM   4841  C  C   . ASP E  1 52  ? 9.512  -19.368 -28.738  1.00 17.21 ? 52   ASP F C   1 
ATOM   4842  O  O   . ASP E  1 52  ? 9.170  -18.178 -28.784  1.00 17.47 ? 52   ASP F O   1 
ATOM   4843  C  CB  . ASP E  1 52  ? 10.802 -19.169 -26.577  1.00 16.29 ? 52   ASP F CB  1 
ATOM   4844  C  CG  . ASP E  1 52  ? 9.618  -19.581 -25.694  1.00 15.97 ? 52   ASP F CG  1 
ATOM   4845  O  OD1 . ASP E  1 52  ? 9.744  -19.526 -24.449  1.00 15.83 ? 52   ASP F OD1 1 
ATOM   4846  O  OD2 . ASP E  1 52  ? 8.560  -19.948 -26.227  1.00 16.10 ? 52   ASP F OD2 1 
ATOM   4847  N  N   . ASN E  1 53  ? 8.829  -20.321 -29.354  1.00 17.54 ? 53   ASN F N   1 
ATOM   4848  C  CA  . ASN E  1 53  ? 7.640  -19.969 -30.113  1.00 18.78 ? 53   ASN F CA  1 
ATOM   4849  C  C   . ASN E  1 53  ? 6.356  -20.561 -29.488  1.00 18.60 ? 53   ASN F C   1 
ATOM   4850  O  O   . ASN E  1 53  ? 5.371  -20.837 -30.175  1.00 18.14 ? 53   ASN F O   1 
ATOM   4851  C  CB  . ASN E  1 53  ? 7.835  -20.294 -31.610  1.00 19.17 ? 53   ASN F CB  1 
ATOM   4852  C  CG  . ASN E  1 53  ? 8.759  -19.265 -32.338  1.00 22.39 ? 53   ASN F CG  1 
ATOM   4853  O  OD1 . ASN E  1 53  ? 9.100  -19.442 -33.518  1.00 25.40 ? 53   ASN F OD1 1 
ATOM   4854  N  ND2 . ASN E  1 53  ? 9.157  -18.193 -31.634  1.00 25.65 ? 53   ASN F ND2 1 
ATOM   4855  N  N   . THR E  1 54  ? 6.383  -20.735 -28.163  1.00 18.72 ? 54   THR F N   1 
ATOM   4856  C  CA  . THR E  1 54  ? 5.237  -21.295 -27.416  1.00 18.86 ? 54   THR F CA  1 
ATOM   4857  C  C   . THR E  1 54  ? 4.018  -20.368 -27.445  1.00 19.68 ? 54   THR F C   1 
ATOM   4858  O  O   . THR E  1 54  ? 2.882  -20.829 -27.322  1.00 20.25 ? 54   THR F O   1 
ATOM   4859  C  CB  . THR E  1 54  ? 5.592  -21.591 -25.938  1.00 18.56 ? 54   THR F CB  1 
ATOM   4860  O  OG1 . THR E  1 54  ? 6.121  -20.401 -25.336  1.00 16.96 ? 54   THR F OG1 1 
ATOM   4861  C  CG2 . THR E  1 54  ? 6.615  -22.693 -25.839  1.00 17.16 ? 54   THR F CG2 1 
ATOM   4862  N  N   . ALA E  1 55  ? 4.261  -19.066 -27.582  1.00 19.75 ? 55   ALA F N   1 
ATOM   4863  C  CA  . ALA E  1 55  ? 3.174  -18.093 -27.717  1.00 19.71 ? 55   ALA F CA  1 
ATOM   4864  C  C   . ALA E  1 55  ? 3.342  -17.296 -28.996  1.00 19.55 ? 55   ALA F C   1 
ATOM   4865  O  O   . ALA E  1 55  ? 3.321  -16.061 -28.978  1.00 19.98 ? 55   ALA F O   1 
ATOM   4866  C  CB  . ALA E  1 55  ? 3.115  -17.163 -26.487  1.00 19.82 ? 55   ALA F CB  1 
ATOM   4867  N  N   . GLY E  1 56  ? 3.542  -18.006 -30.107  1.00 18.55 ? 56   GLY F N   1 
ATOM   4868  C  CA  . GLY E  1 56  ? 3.758  -17.374 -31.406  1.00 16.86 ? 56   GLY F CA  1 
ATOM   4869  C  C   . GLY E  1 56  ? 5.062  -16.599 -31.394  1.00 15.57 ? 56   GLY F C   1 
ATOM   4870  O  O   . GLY E  1 56  ? 6.009  -16.954 -30.671  1.00 15.67 ? 56   GLY F O   1 
ATOM   4871  N  N   . CYS E  1 57  ? 5.089  -15.499 -32.140  1.00 14.44 ? 57   CYS F N   1 
ATOM   4872  C  CA  . CYS E  1 57  ? 6.308  -14.709 -32.280  1.00 13.05 ? 57   CYS F CA  1 
ATOM   4873  C  C   . CYS E  1 57  ? 6.582  -13.832 -31.051  1.00 13.73 ? 57   CYS F C   1 
ATOM   4874  O  O   . CYS E  1 57  ? 7.695  -13.345 -30.865  1.00 13.61 ? 57   CYS F O   1 
ATOM   4875  C  CB  . CYS E  1 57  ? 6.251  -13.898 -33.574  0.40 12.32 ? 57   CYS F CB  1 
ATOM   4876  S  SG  . CYS E  1 57  ? 5.999  -14.952 -35.026  0.40 5.85  ? 57   CYS F SG  1 
ATOM   4877  N  N   . THR E  1 58  ? 5.575  -13.659 -30.201  1.00 14.04 ? 58   THR F N   1 
ATOM   4878  C  CA  . THR E  1 58  ? 5.701  -12.835 -28.992  1.00 15.14 ? 58   THR F CA  1 
ATOM   4879  C  C   . THR E  1 58  ? 6.731  -13.414 -28.027  1.00 15.18 ? 58   THR F C   1 
ATOM   4880  O  O   . THR E  1 58  ? 7.514  -12.680 -27.419  1.00 14.94 ? 58   THR F O   1 
ATOM   4881  C  CB  . THR E  1 58  ? 4.324  -12.665 -28.300  1.00 15.33 ? 58   THR F CB  1 
ATOM   4882  O  OG1 . THR E  1 58  ? 3.360  -12.224 -29.274  1.00 17.44 ? 58   THR F OG1 1 
ATOM   4883  C  CG2 . THR E  1 58  ? 4.385  -11.634 -27.169  1.00 16.09 ? 58   THR F CG2 1 
ATOM   4884  N  N   . SER E  1 59  ? 6.777  -14.742 -27.948  1.00 15.48 ? 59   SER F N   1 
ATOM   4885  C  CA  . SER E  1 59  ? 7.589  -15.405 -26.941  1.00 15.92 ? 59   SER F CA  1 
ATOM   4886  C  C   . SER E  1 59  ? 9.071  -15.429 -27.310  1.00 15.50 ? 59   SER F C   1 
ATOM   4887  O  O   . SER E  1 59  ? 9.899  -15.900 -26.519  1.00 14.79 ? 59   SER F O   1 
ATOM   4888  C  CB  . SER E  1 59  ? 7.031  -16.810 -26.644  1.00 16.31 ? 59   SER F CB  1 
ATOM   4889  O  OG  . SER E  1 59  ? 6.555  -17.418 -27.836  1.00 18.99 ? 59   SER F OG  1 
ATOM   4890  N  N   . ALA E  1 60  ? 9.389  -14.928 -28.518  1.00 14.84 ? 60   ALA F N   1 
ATOM   4891  C  CA  . ALA E  1 60  ? 10.772 -14.689 -28.965  1.00 14.57 ? 60   ALA F CA  1 
ATOM   4892  C  C   . ALA E  1 60  ? 11.471 -13.574 -28.185  1.00 14.11 ? 60   ALA F C   1 
ATOM   4893  O  O   . ALA E  1 60  ? 12.708 -13.497 -28.161  1.00 13.36 ? 60   ALA F O   1 
ATOM   4894  C  CB  . ALA E  1 60  ? 10.801 -14.357 -30.462  1.00 14.31 ? 60   ALA F CB  1 
ATOM   4895  N  N   . GLY E  1 61  ? 10.679 -12.703 -27.567  1.00 13.61 ? 61   GLY F N   1 
ATOM   4896  C  CA  . GLY E  1 61  ? 11.246 -11.648 -26.753  1.00 13.12 ? 61   GLY F CA  1 
ATOM   4897  C  C   . GLY E  1 61  ? 11.805 -10.547 -27.642  1.00 13.32 ? 61   GLY F C   1 
ATOM   4898  O  O   . GLY E  1 61  ? 11.346 -10.385 -28.773  1.00 12.45 ? 61   GLY F O   1 
ATOM   4899  N  N   . PRO E  1 62  ? 12.790 -9.786  -27.127  1.00 13.37 ? 62   PRO F N   1 
ATOM   4900  C  CA  . PRO E  1 62  ? 13.336 -8.596  -27.778  1.00 13.13 ? 62   PRO F CA  1 
ATOM   4901  C  C   . PRO E  1 62  ? 14.431 -8.929  -28.784  1.00 12.65 ? 62   PRO F C   1 
ATOM   4902  O  O   . PRO E  1 62  ? 14.773 -10.103 -28.955  1.00 13.45 ? 62   PRO F O   1 
ATOM   4903  C  CB  . PRO E  1 62  ? 13.944 -7.831  -26.601  1.00 13.31 ? 62   PRO F CB  1 
ATOM   4904  C  CG  . PRO E  1 62  ? 14.449 -8.919  -25.707  1.00 13.59 ? 62   PRO F CG  1 
ATOM   4905  C  CD  . PRO E  1 62  ? 13.393 -9.994  -25.790  1.00 14.18 ? 62   PRO F CD  1 
ATOM   4906  N  N   . HIS E  1 63  ? 14.998 -7.919  -29.434  1.00 11.70 ? 63   HIS F N   1 
ATOM   4907  C  CA  . HIS E  1 63  ? 16.113 -8.173  -30.354  1.00 11.03 ? 63   HIS F CA  1 
ATOM   4908  C  C   . HIS E  1 63  ? 17.280 -8.762  -29.591  1.00 10.61 ? 63   HIS F C   1 
ATOM   4909  O  O   . HIS E  1 63  ? 17.539 -8.362  -28.461  1.00 11.53 ? 63   HIS F O   1 
ATOM   4910  C  CB  . HIS E  1 63  ? 16.547 -6.892  -31.066  1.00 10.16 ? 63   HIS F CB  1 
ATOM   4911  C  CG  . HIS E  1 63  ? 15.452 -6.280  -31.867  1.00 10.10 ? 63   HIS F CG  1 
ATOM   4912  N  ND1 . HIS E  1 63  ? 15.627 -5.155  -32.632  1.00 8.98  ? 63   HIS F ND1 1 
ATOM   4913  C  CD2 . HIS E  1 63  ? 14.159 -6.645  -32.022  1.00 9.57  ? 63   HIS F CD2 1 
ATOM   4914  C  CE1 . HIS E  1 63  ? 14.486 -4.839  -33.220  1.00 10.63 ? 63   HIS F CE1 1 
ATOM   4915  N  NE2 . HIS E  1 63  ? 13.577 -5.726  -32.862  1.00 8.81  ? 63   HIS F NE2 1 
ATOM   4916  N  N   . PHE E  1 64  ? 17.940 -9.747  -30.202  1.00 11.04 ? 64   PHE F N   1 
ATOM   4917  C  CA  . PHE E  1 64  ? 19.136 -10.364 -29.636  1.00 10.45 ? 64   PHE F CA  1 
ATOM   4918  C  C   . PHE E  1 64  ? 20.181 -9.289  -29.431  1.00 11.48 ? 64   PHE F C   1 
ATOM   4919  O  O   . PHE E  1 64  ? 20.645 -8.663  -30.402  1.00 10.79 ? 64   PHE F O   1 
ATOM   4920  C  CB  . PHE E  1 64  ? 19.667 -11.417 -30.587  1.00 10.98 ? 64   PHE F CB  1 
ATOM   4921  C  CG  . PHE E  1 64  ? 20.919 -12.109 -30.098  1.00 11.36 ? 64   PHE F CG  1 
ATOM   4922  C  CD1 . PHE E  1 64  ? 21.921 -12.458 -30.997  1.00 8.86  ? 64   PHE F CD1 1 
ATOM   4923  C  CD2 . PHE E  1 64  ? 21.082 -12.418 -28.750  1.00 11.92 ? 64   PHE F CD2 1 
ATOM   4924  C  CE1 . PHE E  1 64  ? 23.082 -13.106 -30.562  1.00 8.26  ? 64   PHE F CE1 1 
ATOM   4925  C  CE2 . PHE E  1 64  ? 22.249 -13.065 -28.300  1.00 13.63 ? 64   PHE F CE2 1 
ATOM   4926  C  CZ  . PHE E  1 64  ? 23.238 -13.410 -29.206  1.00 11.41 ? 64   PHE F CZ  1 
ATOM   4927  N  N   . ASN E  1 65  ? 20.532 -9.032  -28.172  1.00 11.45 ? 65   ASN F N   1 
ATOM   4928  C  CA  . ASN E  1 65  ? 21.399 -7.873  -27.875  1.00 12.00 ? 65   ASN F CA  1 
ATOM   4929  C  C   . ASN E  1 65  ? 22.445 -8.195  -26.810  1.00 12.44 ? 65   ASN F C   1 
ATOM   4930  O  O   . ASN E  1 65  ? 22.402 -7.624  -25.714  1.00 14.14 ? 65   ASN F O   1 
ATOM   4931  C  CB  . ASN E  1 65  ? 20.511 -6.694  -27.459  1.00 11.70 ? 65   ASN F CB  1 
ATOM   4932  C  CG  . ASN E  1 65  ? 21.288 -5.394  -27.193  1.00 12.65 ? 65   ASN F CG  1 
ATOM   4933  O  OD1 . ASN E  1 65  ? 22.376 -5.137  -27.751  1.00 10.24 ? 65   ASN F OD1 1 
ATOM   4934  N  ND2 . ASN E  1 65  ? 20.683 -4.537  -26.371  1.00 13.12 ? 65   ASN F ND2 1 
ATOM   4935  N  N   . PRO E  1 66  ? 23.408 -9.093  -27.119  1.00 12.87 ? 66   PRO F N   1 
ATOM   4936  C  CA  . PRO E  1 66  ? 24.325 -9.515  -26.040  1.00 13.17 ? 66   PRO F CA  1 
ATOM   4937  C  C   . PRO E  1 66  ? 25.211 -8.408  -25.501  1.00 13.99 ? 66   PRO F C   1 
ATOM   4938  O  O   . PRO E  1 66  ? 25.707 -8.514  -24.375  1.00 14.19 ? 66   PRO F O   1 
ATOM   4939  C  CB  . PRO E  1 66  ? 25.196 -10.590 -26.692  1.00 13.68 ? 66   PRO F CB  1 
ATOM   4940  C  CG  . PRO E  1 66  ? 25.025 -10.414 -28.170  1.00 12.94 ? 66   PRO F CG  1 
ATOM   4941  C  CD  . PRO E  1 66  ? 23.647 -9.844  -28.359  1.00 13.12 ? 66   PRO F CD  1 
ATOM   4942  N  N   . LEU E  1 67  ? 25.430 -7.368  -26.293  1.00 13.15 ? 67   LEU F N   1 
ATOM   4943  C  CA  . LEU E  1 67  ? 26.321 -6.282  -25.885  1.00 13.55 ? 67   LEU F CA  1 
ATOM   4944  C  C   . LEU E  1 67  ? 25.587 -5.060  -25.318  1.00 13.46 ? 67   LEU F C   1 
ATOM   4945  O  O   . LEU E  1 67  ? 26.187 -4.010  -25.101  1.00 13.67 ? 67   LEU F O   1 
ATOM   4946  C  CB  . LEU E  1 67  ? 27.236 -5.910  -27.063  1.00 13.88 ? 67   LEU F CB  1 
ATOM   4947  C  CG  . LEU E  1 67  ? 28.373 -6.915  -27.278  1.00 14.32 ? 67   LEU F CG  1 
ATOM   4948  C  CD1 . LEU E  1 67  ? 28.969 -6.798  -28.669  1.00 14.84 ? 67   LEU F CD1 1 
ATOM   4949  C  CD2 . LEU E  1 67  ? 29.445 -6.730  -26.229  1.00 15.67 ? 67   LEU F CD2 1 
ATOM   4950  N  N   . SER E  1 68  ? 24.286 -5.214  -25.082  1.00 12.95 ? 68   SER F N   1 
ATOM   4951  C  CA  . SER E  1 68  ? 23.442 -4.177  -24.475  1.00 13.09 ? 68   SER F CA  1 
ATOM   4952  C  C   . SER E  1 68  ? 23.545 -2.802  -25.144  1.00 13.02 ? 68   SER F C   1 
ATOM   4953  O  O   . SER E  1 68  ? 23.753 -1.781  -24.459  1.00 12.84 ? 68   SER F O   1 
ATOM   4954  C  CB  . SER E  1 68  ? 23.689 -4.094  -22.955  1.00 13.76 ? 68   SER F CB  1 
ATOM   4955  O  OG  . SER E  1 68  ? 23.575 -5.384  -22.355  1.00 15.43 ? 68   SER F OG  1 
ATOM   4956  N  N   . ARG E  1 69  ? 23.415 -2.782  -26.475  1.00 12.20 ? 69   ARG F N   1 
ATOM   4957  C  CA  . ARG E  1 69  ? 23.493 -1.540  -27.248  1.00 12.17 ? 69   ARG F CA  1 
ATOM   4958  C  C   . ARG E  1 69  ? 22.098 -1.018  -27.570  1.00 11.76 ? 69   ARG F C   1 
ATOM   4959  O  O   . ARG E  1 69  ? 21.089 -1.700  -27.346  1.00 11.27 ? 69   ARG F O   1 
ATOM   4960  C  CB  . ARG E  1 69  ? 24.273 -1.748  -28.544  1.00 13.10 ? 69   ARG F CB  1 
ATOM   4961  C  CG  . ARG E  1 69  ? 25.597 -2.494  -28.410  1.00 12.99 ? 69   ARG F CG  1 
ATOM   4962  C  CD  . ARG E  1 69  ? 26.611 -1.701  -27.651  1.00 16.39 ? 69   ARG F CD  1 
ATOM   4963  N  NE  . ARG E  1 69  ? 27.920 -2.326  -27.751  1.00 17.50 ? 69   ARG F NE  1 
ATOM   4964  C  CZ  . ARG E  1 69  ? 28.880 -2.200  -26.841  1.00 18.12 ? 69   ARG F CZ  1 
ATOM   4965  N  NH1 . ARG E  1 69  ? 30.039 -2.819  -27.020  1.00 17.18 ? 69   ARG F NH1 1 
ATOM   4966  N  NH2 . ARG E  1 69  ? 28.675 -1.476  -25.743  1.00 19.05 ? 69   ARG F NH2 1 
ATOM   4967  N  N   . LYS E  1 70  ? 22.034 0.202   -28.083  1.00 11.84 ? 70   LYS F N   1 
ATOM   4968  C  CA  . LYS E  1 70  ? 20.786 0.720   -28.602  1.00 13.00 ? 70   LYS F CA  1 
ATOM   4969  C  C   . LYS E  1 70  ? 20.528 0.020   -29.926  1.00 12.33 ? 70   LYS F C   1 
ATOM   4970  O  O   . LYS E  1 70  ? 21.461 -0.489  -30.559  1.00 12.80 ? 70   LYS F O   1 
ATOM   4971  C  CB  . LYS E  1 70  ? 20.866 2.236   -28.804  1.00 13.86 ? 70   LYS F CB  1 
ATOM   4972  C  CG  . LYS E  1 70  ? 20.871 3.040   -27.476  1.00 17.31 ? 70   LYS F CG  1 
ATOM   4973  C  CD  . LYS E  1 70  ? 20.947 4.533   -27.713  1.00 22.31 ? 70   LYS F CD  1 
ATOM   4974  C  CE  . LYS E  1 70  ? 22.384 5.044   -27.602  1.00 25.40 ? 70   LYS F CE  1 
ATOM   4975  N  NZ  . LYS E  1 70  ? 22.438 6.505   -27.207  1.00 27.61 ? 70   LYS F NZ  1 
ATOM   4976  N  N   . HIS E  1 71  ? 19.268 0.008   -30.343  1.00 12.52 ? 71   HIS F N   1 
ATOM   4977  C  CA  . HIS E  1 71  ? 18.887 -0.471  -31.667  1.00 11.69 ? 71   HIS F CA  1 
ATOM   4978  C  C   . HIS E  1 71  ? 19.543 0.367   -32.768  1.00 11.83 ? 71   HIS F C   1 
ATOM   4979  O  O   . HIS E  1 71  ? 19.634 1.598   -32.649  1.00 10.82 ? 71   HIS F O   1 
ATOM   4980  C  CB  . HIS E  1 71  ? 17.378 -0.375  -31.848  1.00 12.47 ? 71   HIS F CB  1 
ATOM   4981  C  CG  . HIS E  1 71  ? 16.918 -0.825  -33.201  1.00 12.70 ? 71   HIS F CG  1 
ATOM   4982  N  ND1 . HIS E  1 71  ? 16.838 -2.155  -33.553  1.00 10.86 ? 71   HIS F ND1 1 
ATOM   4983  C  CD2 . HIS E  1 71  ? 16.516 -0.123  -34.287  1.00 11.50 ? 71   HIS F CD2 1 
ATOM   4984  C  CE1 . HIS E  1 71  ? 16.415 -2.253  -34.797  1.00 10.49 ? 71   HIS F CE1 1 
ATOM   4985  N  NE2 . HIS E  1 71  ? 16.217 -1.036  -35.270  1.00 12.78 ? 71   HIS F NE2 1 
ATOM   4986  N  N   . GLY E  1 72  ? 19.963 -0.301  -33.845  1.00 10.73 ? 72   GLY F N   1 
ATOM   4987  C  CA  . GLY E  1 72  ? 20.584 0.375   -34.983  1.00 10.63 ? 72   GLY F CA  1 
ATOM   4988  C  C   . GLY E  1 72  ? 20.274 -0.346  -36.287  1.00 10.92 ? 72   GLY F C   1 
ATOM   4989  O  O   . GLY E  1 72  ? 19.458 -1.283  -36.322  1.00 10.97 ? 72   GLY F O   1 
ATOM   4990  N  N   . GLY E  1 73  ? 20.901 0.095   -37.365  1.00 10.06 ? 73   GLY F N   1 
ATOM   4991  C  CA  . GLY E  1 73  ? 20.794 -0.622  -38.632  1.00 8.96  ? 73   GLY F CA  1 
ATOM   4992  C  C   . GLY E  1 73  ? 22.048 -1.467  -38.718  1.00 8.25  ? 73   GLY F C   1 
ATOM   4993  O  O   . GLY E  1 73  ? 23.003 -1.202  -37.982  1.00 9.20  ? 73   GLY F O   1 
ATOM   4994  N  N   . PRO E  1 74  ? 22.074 -2.465  -39.627  1.00 7.50  ? 74   PRO F N   1 
ATOM   4995  C  CA  . PRO E  1 74  ? 23.218 -3.381  -39.704  1.00 7.87  ? 74   PRO F CA  1 
ATOM   4996  C  C   . PRO E  1 74  ? 24.561 -2.707  -40.024  1.00 8.74  ? 74   PRO F C   1 
ATOM   4997  O  O   . PRO E  1 74  ? 25.611 -3.239  -39.661  1.00 8.59  ? 74   PRO F O   1 
ATOM   4998  C  CB  . PRO E  1 74  ? 22.853 -4.335  -40.853  1.00 6.88  ? 74   PRO F CB  1 
ATOM   4999  C  CG  . PRO E  1 74  ? 21.728 -3.744  -41.545  1.00 7.76  ? 74   PRO F CG  1 
ATOM   5000  C  CD  . PRO E  1 74  ? 20.993 -2.882  -40.532  1.00 7.33  ? 74   PRO F CD  1 
ATOM   5001  N  N   . LYS E  1 75  ? 24.523 -1.546  -40.676  1.00 9.64  ? 75   LYS F N   1 
ATOM   5002  C  CA  . LYS E  1 75  ? 25.760 -0.806  -40.969  1.00 11.01 ? 75   LYS F CA  1 
ATOM   5003  C  C   . LYS E  1 75  ? 26.374 -0.072  -39.768  1.00 12.01 ? 75   LYS F C   1 
ATOM   5004  O  O   . LYS E  1 75  ? 27.512 0.420   -39.851  1.00 12.02 ? 75   LYS F O   1 
ATOM   5005  C  CB  . LYS E  1 75  ? 25.551 0.186   -42.104  1.00 10.92 ? 75   LYS F CB  1 
ATOM   5006  C  CG  . LYS E  1 75  ? 25.177 -0.437  -43.445  1.00 14.29 ? 75   LYS F CG  1 
ATOM   5007  C  CD  . LYS E  1 75  ? 25.592 0.490   -44.582  1.00 19.30 ? 75   LYS F CD  1 
ATOM   5008  C  CE  . LYS E  1 75  ? 24.448 1.337   -45.072  1.00 21.06 ? 75   LYS F CE  1 
ATOM   5009  N  NZ  . LYS E  1 75  ? 24.974 2.374   -46.041  1.00 19.96 ? 75   LYS F NZ  1 
ATOM   5010  N  N   . ASP E  1 76  ? 25.620 0.048   -38.680  1.00 12.43 ? 76   ASP F N   1 
ATOM   5011  C  CA  . ASP E  1 76  ? 26.056 0.826   -37.526  1.00 12.98 ? 76   ASP F CA  1 
ATOM   5012  C  C   . ASP E  1 76  ? 26.973 0.073   -36.596  1.00 14.08 ? 76   ASP F C   1 
ATOM   5013  O  O   . ASP E  1 76  ? 26.833 -1.150  -36.400  1.00 14.45 ? 76   ASP F O   1 
ATOM   5014  C  CB  . ASP E  1 76  ? 24.850 1.328   -36.723  1.00 12.72 ? 76   ASP F CB  1 
ATOM   5015  C  CG  . ASP E  1 76  ? 24.077 2.360   -37.459  1.00 12.77 ? 76   ASP F CG  1 
ATOM   5016  O  OD1 . ASP E  1 76  ? 22.838 2.319   -37.411  1.00 14.83 ? 76   ASP F OD1 1 
ATOM   5017  O  OD2 . ASP E  1 76  ? 24.717 3.191   -38.132  1.00 13.48 ? 76   ASP F OD2 1 
ATOM   5018  N  N   . GLU E  1 77  ? 27.926 0.813   -36.035  1.00 14.65 ? 77   GLU F N   1 
ATOM   5019  C  CA  . GLU E  1 77  ? 28.704 0.336   -34.894  1.00 15.47 ? 77   GLU F CA  1 
ATOM   5020  C  C   . GLU E  1 77  ? 27.763 0.104   -33.718  1.00 14.23 ? 77   GLU F C   1 
ATOM   5021  O  O   . GLU E  1 77  ? 27.858 -0.911  -33.036  1.00 13.99 ? 77   GLU F O   1 
ATOM   5022  C  CB  . GLU E  1 77  ? 29.767 1.379   -34.512  1.00 16.57 ? 77   GLU F CB  1 
ATOM   5023  C  CG  . GLU E  1 77  ? 30.827 0.907   -33.558  1.00 21.85 ? 77   GLU F CG  1 
ATOM   5024  C  CD  . GLU E  1 77  ? 31.775 2.036   -33.156  1.00 27.38 ? 77   GLU F CD  1 
ATOM   5025  O  OE1 . GLU E  1 77  ? 32.431 2.620   -34.053  1.00 29.81 ? 77   GLU F OE1 1 
ATOM   5026  O  OE2 . GLU E  1 77  ? 31.854 2.342   -31.943  1.00 29.09 ? 77   GLU F OE2 1 
ATOM   5027  N  N   . GLU E  1 78  ? 26.872 1.068   -33.478  1.00 12.75 ? 78   GLU F N   1 
ATOM   5028  C  CA  . GLU E  1 78  ? 25.888 0.963   -32.422  1.00 12.01 ? 78   GLU F CA  1 
ATOM   5029  C  C   . GLU E  1 78  ? 24.638 0.248   -32.947  1.00 10.55 ? 78   GLU F C   1 
ATOM   5030  O  O   . GLU E  1 78  ? 23.802 0.836   -33.653  1.00 10.10 ? 78   GLU F O   1 
ATOM   5031  C  CB  . GLU E  1 78  ? 25.523 2.350   -31.871  1.00 12.38 ? 78   GLU F CB  1 
ATOM   5032  C  CG  . GLU E  1 78  ? 24.486 2.301   -30.743  1.00 13.37 ? 78   GLU F CG  1 
ATOM   5033  C  CD  . GLU E  1 78  ? 25.106 2.038   -29.387  1.00 18.85 ? 78   GLU F CD  1 
ATOM   5034  O  OE1 . GLU E  1 78  ? 24.346 1.733   -28.440  1.00 18.77 ? 78   GLU F OE1 1 
ATOM   5035  O  OE2 . GLU E  1 78  ? 26.348 2.147   -29.253  1.00 19.90 ? 78   GLU F OE2 1 
ATOM   5036  N  N   . ARG E  1 79  ? 24.533 -1.028  -32.605  1.00 10.84 ? 79   ARG F N   1 
ATOM   5037  C  CA  . ARG E  1 79  ? 23.377 -1.860  -32.989  1.00 9.23  ? 79   ARG F CA  1 
ATOM   5038  C  C   . ARG E  1 79  ? 23.333 -3.074  -32.082  1.00 9.98  ? 79   ARG F C   1 
ATOM   5039  O  O   . ARG E  1 79  ? 24.352 -3.430  -31.472  1.00 10.03 ? 79   ARG F O   1 
ATOM   5040  C  CB  . ARG E  1 79  ? 23.535 -2.351  -34.442  1.00 8.89  ? 79   ARG F CB  1 
ATOM   5041  C  CG  . ARG E  1 79  ? 24.853 -3.081  -34.721  1.00 5.12  ? 79   ARG F CG  1 
ATOM   5042  C  CD  . ARG E  1 79  ? 24.858 -3.693  -36.145  1.00 7.71  ? 79   ARG F CD  1 
ATOM   5043  N  NE  . ARG E  1 79  ? 24.263 -5.050  -36.154  1.00 8.01  ? 79   ARG F NE  1 
ATOM   5044  C  CZ  . ARG E  1 79  ? 24.432 -5.944  -37.125  1.00 10.96 ? 79   ARG F CZ  1 
ATOM   5045  N  NH1 . ARG E  1 79  ? 23.875 -7.157  -37.005  1.00 11.14 ? 79   ARG F NH1 1 
ATOM   5046  N  NH2 . ARG E  1 79  ? 25.144 -5.648  -38.210  1.00 9.18  ? 79   ARG F NH2 1 
ATOM   5047  N  N   . HIS E  1 80  ? 22.174 -3.735  -32.024  1.00 10.54 ? 80   HIS F N   1 
ATOM   5048  C  CA  . HIS E  1 80  ? 22.113 -5.057  -31.406  1.00 10.82 ? 80   HIS F CA  1 
ATOM   5049  C  C   . HIS E  1 80  ? 22.664 -6.035  -32.428  1.00 11.15 ? 80   HIS F C   1 
ATOM   5050  O  O   . HIS E  1 80  ? 22.567 -5.818  -33.650  1.00 10.33 ? 80   HIS F O   1 
ATOM   5051  C  CB  . HIS E  1 80  ? 20.694 -5.530  -31.134  1.00 11.07 ? 80   HIS F CB  1 
ATOM   5052  C  CG  . HIS E  1 80  ? 19.812 -4.534  -30.457  1.00 12.15 ? 80   HIS F CG  1 
ATOM   5053  N  ND1 . HIS E  1 80  ? 18.544 -4.272  -30.917  1.00 13.56 ? 80   HIS F ND1 1 
ATOM   5054  C  CD2 . HIS E  1 80  ? 19.982 -3.773  -29.350  1.00 10.78 ? 80   HIS F CD2 1 
ATOM   5055  C  CE1 . HIS E  1 80  ? 17.963 -3.392  -30.111  1.00 12.52 ? 80   HIS F CE1 1 
ATOM   5056  N  NE2 . HIS E  1 80  ? 18.821 -3.065  -29.158  1.00 12.31 ? 80   HIS F NE2 1 
ATOM   5057  N  N   . VAL E  1 81  ? 23.200 -7.134  -31.941  1.00 11.11 ? 81   VAL F N   1 
ATOM   5058  C  CA  . VAL E  1 81  ? 23.621 -8.207  -32.843  1.00 11.79 ? 81   VAL F CA  1 
ATOM   5059  C  C   . VAL E  1 81  ? 22.525 -8.626  -33.838  1.00 11.47 ? 81   VAL F C   1 
ATOM   5060  O  O   . VAL E  1 81  ? 22.805 -8.826  -35.020  1.00 12.06 ? 81   VAL F O   1 
ATOM   5061  C  CB  . VAL E  1 81  ? 24.211 -9.376  -32.063  1.00 12.11 ? 81   VAL F CB  1 
ATOM   5062  C  CG1 . VAL E  1 81  ? 24.416 -10.604 -32.966  1.00 11.31 ? 81   VAL F CG1 1 
ATOM   5063  C  CG2 . VAL E  1 81  ? 25.533 -8.945  -31.464  1.00 11.79 ? 81   VAL F CG2 1 
ATOM   5064  N  N   . GLY E  1 82  ? 21.283 -8.710  -33.383  1.00 10.89 ? 82   GLY F N   1 
ATOM   5065  C  CA  . GLY E  1 82  ? 20.187 -9.167  -34.236  1.00 9.21  ? 82   GLY F CA  1 
ATOM   5066  C  C   . GLY E  1 82  ? 19.669 -8.184  -35.265  1.00 9.17  ? 82   GLY F C   1 
ATOM   5067  O  O   . GLY E  1 82  ? 18.749 -8.518  -36.005  1.00 8.41  ? 82   GLY F O   1 
ATOM   5068  N  N   . ASP E  1 83  ? 20.270 -6.986  -35.340  1.00 8.66  ? 83   ASP F N   1 
ATOM   5069  C  CA  . ASP E  1 83  ? 19.765 -5.922  -36.210  1.00 8.89  ? 83   ASP F CA  1 
ATOM   5070  C  C   . ASP E  1 83  ? 20.206 -6.063  -37.662  1.00 8.93  ? 83   ASP F C   1 
ATOM   5071  O  O   . ASP E  1 83  ? 21.278 -5.576  -38.050  1.00 8.24  ? 83   ASP F O   1 
ATOM   5072  C  CB  . ASP E  1 83  ? 20.206 -4.556  -35.684  1.00 8.56  ? 83   ASP F CB  1 
ATOM   5073  C  CG  . ASP E  1 83  ? 19.465 -4.162  -34.424  1.00 8.68  ? 83   ASP F CG  1 
ATOM   5074  O  OD1 . ASP E  1 83  ? 18.420 -4.795  -34.148  1.00 9.53  ? 83   ASP F OD1 1 
ATOM   5075  O  OD2 . ASP E  1 83  ? 19.908 -3.233  -33.726  1.00 7.67  ? 83   ASP F OD2 1 
ATOM   5076  N  N   . LEU E  1 84  ? 19.354 -6.686  -38.471  1.00 9.05  ? 84   LEU F N   1 
ATOM   5077  C  CA  . LEU E  1 84  ? 19.681 -6.925  -39.857  1.00 8.50  ? 84   LEU F CA  1 
ATOM   5078  C  C   . LEU E  1 84  ? 18.951 -5.945  -40.749  1.00 8.55  ? 84   LEU F C   1 
ATOM   5079  O  O   . LEU E  1 84  ? 19.000 -6.062  -41.959  1.00 7.59  ? 84   LEU F O   1 
ATOM   5080  C  CB  . LEU E  1 84  ? 19.335 -8.368  -40.235  1.00 8.53  ? 84   LEU F CB  1 
ATOM   5081  C  CG  . LEU E  1 84  ? 20.095 -9.501  -39.544  1.00 8.42  ? 84   LEU F CG  1 
ATOM   5082  C  CD1 . LEU E  1 84  ? 19.586 -10.855 -40.059  1.00 8.39  ? 84   LEU F CD1 1 
ATOM   5083  C  CD2 . LEU E  1 84  ? 21.633 -9.409  -39.702  1.00 9.47  ? 84   LEU F CD2 1 
ATOM   5084  N  N   . GLY E  1 85  ? 18.257 -4.975  -40.149  1.00 7.60  ? 85   GLY F N   1 
ATOM   5085  C  CA  . GLY E  1 85  ? 17.652 -3.918  -40.933  1.00 9.06  ? 85   GLY F CA  1 
ATOM   5086  C  C   . GLY E  1 85  ? 16.294 -4.295  -41.491  1.00 8.89  ? 85   GLY F C   1 
ATOM   5087  O  O   . GLY E  1 85  ? 15.437 -4.790  -40.763  1.00 10.31 ? 85   GLY F O   1 
ATOM   5088  N  N   . ASN E  1 86  ? 16.096 -3.980  -42.763  1.00 9.45  ? 86   ASN F N   1 
ATOM   5089  C  CA  . ASN E  1 86  ? 14.835 -4.170  -43.453  1.00 8.79  ? 86   ASN F CA  1 
ATOM   5090  C  C   . ASN E  1 86  ? 15.051 -5.138  -44.586  1.00 9.44  ? 86   ASN F C   1 
ATOM   5091  O  O   . ASN E  1 86  ? 16.158 -5.237  -45.131  1.00 8.26  ? 86   ASN F O   1 
ATOM   5092  C  CB  . ASN E  1 86  ? 14.344 -2.864  -44.067  1.00 8.81  ? 86   ASN F CB  1 
ATOM   5093  C  CG  . ASN E  1 86  ? 13.745 -1.912  -43.037  1.00 10.84 ? 86   ASN F CG  1 
ATOM   5094  O  OD1 . ASN E  1 86  ? 12.804 -2.258  -42.324  1.00 11.17 ? 86   ASN F OD1 1 
ATOM   5095  N  ND2 . ASN E  1 86  ? 14.303 -0.692  -42.958  1.00 12.98 ? 86   ASN F ND2 1 
ATOM   5096  N  N   . VAL E  1 87  ? 13.991 -5.867  -44.913  1.00 9.48  ? 87   VAL F N   1 
ATOM   5097  C  CA  . VAL E  1 87  ? 13.886 -6.564  -46.186  1.00 9.92  ? 87   VAL F CA  1 
ATOM   5098  C  C   . VAL E  1 87  ? 12.737 -5.936  -46.980  1.00 10.91 ? 87   VAL F C   1 
ATOM   5099  O  O   . VAL E  1 87  ? 11.808 -5.379  -46.381  1.00 11.45 ? 87   VAL F O   1 
ATOM   5100  C  CB  . VAL E  1 87  ? 13.687 -8.069  -45.975  1.00 9.35  ? 87   VAL F CB  1 
ATOM   5101  C  CG1 . VAL E  1 87  ? 14.870 -8.655  -45.271  1.00 8.56  ? 87   VAL F CG1 1 
ATOM   5102  C  CG2 . VAL E  1 87  ? 12.397 -8.358  -45.200  1.00 10.44 ? 87   VAL F CG2 1 
ATOM   5103  N  N   . THR E  1 88  ? 12.802 -6.020  -48.309  1.00 10.78 ? 88   THR F N   1 
ATOM   5104  C  CA  . THR E  1 88  ? 11.867 -5.314  -49.213  1.00 11.30 ? 88   THR F CA  1 
ATOM   5105  C  C   . THR E  1 88  ? 11.041 -6.317  -50.029  1.00 11.90 ? 88   THR F C   1 
ATOM   5106  O  O   . THR E  1 88  ? 11.593 -7.143  -50.756  1.00 10.83 ? 88   THR F O   1 
ATOM   5107  C  CB  . THR E  1 88  ? 12.628 -4.350  -50.159  1.00 11.83 ? 88   THR F CB  1 
ATOM   5108  O  OG1 . THR E  1 88  ? 13.357 -3.389  -49.379  1.00 9.96  ? 88   THR F OG1 1 
ATOM   5109  C  CG2 . THR E  1 88  ? 11.678 -3.592  -51.104  1.00 12.33 ? 88   THR F CG2 1 
ATOM   5110  N  N   . ALA E  1 89  ? 9.718  -6.237  -49.898  1.00 12.30 ? 89   ALA F N   1 
ATOM   5111  C  CA  . ALA E  1 89  ? 8.808  -7.018  -50.747  1.00 12.76 ? 89   ALA F CA  1 
ATOM   5112  C  C   . ALA E  1 89  ? 8.472  -6.291  -52.036  1.00 13.23 ? 89   ALA F C   1 
ATOM   5113  O  O   . ALA E  1 89  ? 8.326  -5.062  -52.045  1.00 13.66 ? 89   ALA F O   1 
ATOM   5114  C  CB  . ALA E  1 89  ? 7.566  -7.357  -49.992  1.00 12.07 ? 89   ALA F CB  1 
ATOM   5115  N  N   . ASP E  1 90  ? 8.336  -7.044  -53.128  1.00 13.28 ? 90   ASP F N   1 
ATOM   5116  C  CA  . ASP E  1 90  ? 8.056  -6.425  -54.425  1.00 14.44 ? 90   ASP F CA  1 
ATOM   5117  C  C   . ASP E  1 90  ? 6.542  -6.271  -54.623  1.00 14.69 ? 90   ASP F C   1 
ATOM   5118  O  O   . ASP E  1 90  ? 5.765  -6.548  -53.703  1.00 13.73 ? 90   ASP F O   1 
ATOM   5119  C  CB  . ASP E  1 90  ? 8.746  -7.181  -55.580  1.00 14.39 ? 90   ASP F CB  1 
ATOM   5120  C  CG  . ASP E  1 90  ? 8.273  -8.626  -55.717  1.00 16.67 ? 90   ASP F CG  1 
ATOM   5121  O  OD1 . ASP E  1 90  ? 8.913  -9.379  -56.483  1.00 18.30 ? 90   ASP F OD1 1 
ATOM   5122  O  OD2 . ASP E  1 90  ? 7.272  -9.017  -55.070  1.00 18.80 ? 90   ASP F OD2 1 
ATOM   5123  N  N   . LYS E  1 91  ? 6.140  -5.832  -55.816  1.00 15.77 ? 91   LYS F N   1 
ATOM   5124  C  CA  . LYS E  1 91  ? 4.717  -5.630  -56.131  1.00 17.12 ? 91   LYS F CA  1 
ATOM   5125  C  C   . LYS E  1 91  ? 3.890  -6.926  -56.014  1.00 17.24 ? 91   LYS F C   1 
ATOM   5126  O  O   . LYS E  1 91  ? 2.672  -6.875  -55.810  1.00 17.16 ? 91   LYS F O   1 
ATOM   5127  C  CB  . LYS E  1 91  ? 4.547  -4.982  -57.521  1.00 18.17 ? 91   LYS F CB  1 
ATOM   5128  C  CG  . LYS E  1 91  ? 5.186  -5.763  -58.686  1.00 20.65 ? 91   LYS F CG  1 
ATOM   5129  C  CD  . LYS E  1 91  ? 4.933  -5.128  -60.073  1.00 24.24 ? 91   LYS F CD  1 
ATOM   5130  C  CE  . LYS E  1 91  ? 4.941  -3.583  -60.040  1.00 25.57 ? 91   LYS F CE  1 
ATOM   5131  N  NZ  . LYS E  1 91  ? 6.256  -2.952  -59.624  1.00 28.56 ? 91   LYS F NZ  1 
ATOM   5132  N  N   . ASP E  1 92  ? 4.557  -8.076  -56.118  1.00 16.79 ? 92   ASP F N   1 
ATOM   5133  C  CA  . ASP E  1 92  ? 3.886  -9.372  -55.933  1.00 17.41 ? 92   ASP F CA  1 
ATOM   5134  C  C   . ASP E  1 92  ? 3.860  -9.892  -54.479  1.00 15.95 ? 92   ASP F C   1 
ATOM   5135  O  O   . ASP E  1 92  ? 3.391  -11.000 -54.231  1.00 16.46 ? 92   ASP F O   1 
ATOM   5136  C  CB  . ASP E  1 92  ? 4.492  -10.437 -56.864  1.00 17.50 ? 92   ASP F CB  1 
ATOM   5137  C  CG  . ASP E  1 92  ? 4.297  -10.116 -58.334  1.00 20.26 ? 92   ASP F CG  1 
ATOM   5138  O  OD1 . ASP E  1 92  ? 5.259  -10.285 -59.109  1.00 22.90 ? 92   ASP F OD1 1 
ATOM   5139  O  OD2 . ASP E  1 92  ? 3.193  -9.689  -58.717  1.00 21.22 ? 92   ASP F OD2 1 
ATOM   5140  N  N   . GLY E  1 93  ? 4.371  -9.110  -53.533  1.00 15.00 ? 93   GLY F N   1 
ATOM   5141  C  CA  . GLY E  1 93  ? 4.409  -9.513  -52.102  1.00 13.31 ? 93   GLY F CA  1 
ATOM   5142  C  C   . GLY E  1 93  ? 5.615  -10.361 -51.686  1.00 13.30 ? 93   GLY F C   1 
ATOM   5143  O  O   . GLY E  1 93  ? 5.628  -10.973 -50.590  1.00 12.61 ? 93   GLY F O   1 
ATOM   5144  N  N   . VAL E  1 94  ? 6.626  -10.400 -52.563  1.00 11.94 ? 94   VAL F N   1 
ATOM   5145  C  CA  . VAL E  1 94  ? 7.773  -11.277 -52.358  1.00 11.21 ? 94   VAL F CA  1 
ATOM   5146  C  C   . VAL E  1 94  ? 9.034  -10.500 -52.002  1.00 9.51  ? 94   VAL F C   1 
ATOM   5147  O  O   . VAL E  1 94  ? 9.459  -9.575  -52.734  1.00 9.23  ? 94   VAL F O   1 
ATOM   5148  C  CB  . VAL E  1 94  ? 8.092  -12.168 -53.592  1.00 11.27 ? 94   VAL F CB  1 
ATOM   5149  C  CG1 . VAL E  1 94  ? 9.292  -13.048 -53.284  1.00 12.29 ? 94   VAL F CG1 1 
ATOM   5150  C  CG2 . VAL E  1 94  ? 6.894  -13.025 -53.971  1.00 13.11 ? 94   VAL F CG2 1 
ATOM   5151  N  N   . ALA E  1 95  ? 9.617  -10.911 -50.890  1.00 8.92  ? 95   ALA F N   1 
ATOM   5152  C  CA  . ALA E  1 95  ? 10.919 -10.411 -50.417  1.00 9.19  ? 95   ALA F CA  1 
ATOM   5153  C  C   . ALA E  1 95  ? 12.011 -11.440 -50.746  1.00 9.27  ? 95   ALA F C   1 
ATOM   5154  O  O   . ALA E  1 95  ? 12.126 -12.473 -50.076  1.00 9.72  ? 95   ALA F O   1 
ATOM   5155  C  CB  . ALA E  1 95  ? 10.863 -10.155 -48.899  1.00 8.63  ? 95   ALA F CB  1 
ATOM   5156  N  N   . ASP E  1 96  ? 12.787 -11.167 -51.787  1.00 9.75  ? 96   ASP F N   1 
ATOM   5157  C  CA  . ASP E  1 96  ? 13.929 -12.029 -52.150  1.00 10.50 ? 96   ASP F CA  1 
ATOM   5158  C  C   . ASP E  1 96  ? 15.129 -11.566 -51.334  1.00 9.85  ? 96   ASP F C   1 
ATOM   5159  O  O   . ASP E  1 96  ? 15.888 -10.691 -51.754  1.00 9.58  ? 96   ASP F O   1 
ATOM   5160  C  CB  . ASP E  1 96  ? 14.210 -11.957 -53.648  1.00 11.20 ? 96   ASP F CB  1 
ATOM   5161  C  CG  . ASP E  1 96  ? 13.122 -12.619 -54.488  1.00 16.22 ? 96   ASP F CG  1 
ATOM   5162  O  OD1 . ASP E  1 96  ? 12.700 -13.766 -54.174  1.00 18.93 ? 96   ASP F OD1 1 
ATOM   5163  O  OD2 . ASP E  1 96  ? 12.704 -11.991 -55.493  1.00 20.90 ? 96   ASP F OD2 1 
ATOM   5164  N  N   . VAL E  1 97  ? 15.273 -12.140 -50.149  1.00 9.65  ? 97   VAL F N   1 
ATOM   5165  C  CA  . VAL E  1 97  ? 16.251 -11.640 -49.186  1.00 9.95  ? 97   VAL F CA  1 
ATOM   5166  C  C   . VAL E  1 97  ? 17.696 -11.862 -49.663  1.00 9.95  ? 97   VAL F C   1 
ATOM   5167  O  O   . VAL E  1 97  ? 18.041 -12.929 -50.172  1.00 9.35  ? 97   VAL F O   1 
ATOM   5168  C  CB  . VAL E  1 97  ? 16.011 -12.242 -47.797  1.00 9.42  ? 97   VAL F CB  1 
ATOM   5169  C  CG1 . VAL E  1 97  ? 17.077 -11.793 -46.817  1.00 8.83  ? 97   VAL F CG1 1 
ATOM   5170  C  CG2 . VAL E  1 97  ? 14.595 -11.852 -47.286  1.00 10.39 ? 97   VAL F CG2 1 
ATOM   5171  N  N   . SER E  1 98  ? 18.517 -10.831 -49.514  1.00 9.54  ? 98   SER F N   1 
ATOM   5172  C  CA  . SER E  1 98  ? 19.936 -10.928 -49.835  1.00 10.09 ? 98   SER F CA  1 
ATOM   5173  C  C   . SER E  1 98  ? 20.696 -9.985  -48.905  1.00 9.76  ? 98   SER F C   1 
ATOM   5174  O  O   . SER E  1 98  ? 20.784 -8.773  -49.153  1.00 10.67 ? 98   SER F O   1 
ATOM   5175  C  CB  . SER E  1 98  ? 20.184 -10.589 -51.308  1.00 9.76  ? 98   SER F CB  1 
ATOM   5176  O  OG  . SER E  1 98  ? 21.539 -10.809 -51.674  1.00 12.07 ? 98   SER F OG  1 
ATOM   5177  N  N   . ILE E  1 99  ? 21.212 -10.556 -47.830  1.00 9.83  ? 99   ILE F N   1 
ATOM   5178  C  CA  . ILE E  1 99  ? 21.945 -9.847  -46.795  1.00 9.51  ? 99   ILE F CA  1 
ATOM   5179  C  C   . ILE E  1 99  ? 23.285 -10.555 -46.545  1.00 9.42  ? 99   ILE F C   1 
ATOM   5180  O  O   . ILE E  1 99  ? 23.406 -11.777 -46.674  1.00 9.73  ? 99   ILE F O   1 
ATOM   5181  C  CB  . ILE E  1 99  ? 21.097 -9.687  -45.485  1.00 9.46  ? 99   ILE F CB  1 
ATOM   5182  C  CG1 . ILE E  1 99  ? 19.946 -8.690  -45.721  1.00 9.95  ? 99   ILE F CG1 1 
ATOM   5183  C  CG2 . ILE E  1 99  ? 21.966 -9.219  -44.290  1.00 10.77 ? 99   ILE F CG2 1 
ATOM   5184  C  CD1 . ILE E  1 99  ? 18.718 -8.824  -44.769  1.00 7.86  ? 99   ILE F CD1 1 
ATOM   5185  N  N   . GLU E  1 100 ? 24.303 -9.779  -46.201  1.00 9.86  ? 100  GLU F N   1 
ATOM   5186  C  CA  . GLU E  1 100 ? 25.560 -10.356 -45.727  1.00 9.75  ? 100  GLU F CA  1 
ATOM   5187  C  C   . GLU E  1 100 ? 25.932 -9.537  -44.505  1.00 9.72  ? 100  GLU F C   1 
ATOM   5188  O  O   . GLU E  1 100 ? 25.915 -8.301  -44.550  1.00 8.60  ? 100  GLU F O   1 
ATOM   5189  C  CB  . GLU E  1 100 ? 26.647 -10.255 -46.802  1.00 11.22 ? 100  GLU F CB  1 
ATOM   5190  C  CG  . GLU E  1 100 ? 27.999 -10.833 -46.387  1.00 13.80 ? 100  GLU F CG  1 
ATOM   5191  C  CD  . GLU E  1 100 ? 28.938 -11.081 -47.565  1.00 16.69 ? 100  GLU F CD  1 
ATOM   5192  O  OE1 . GLU E  1 100 ? 28.696 -10.553 -48.669  1.00 22.13 ? 100  GLU F OE1 1 
ATOM   5193  O  OE2 . GLU E  1 100 ? 29.923 -11.811 -47.389  1.00 20.12 ? 100  GLU F OE2 1 
ATOM   5194  N  N   . ASP E  1 101 ? 26.277 -10.210 -43.415  1.00 8.90  ? 101  ASP F N   1 
ATOM   5195  C  CA  . ASP E  1 101 ? 26.505 -9.490  -42.162  1.00 9.75  ? 101  ASP F CA  1 
ATOM   5196  C  C   . ASP E  1 101 ? 27.681 -10.083 -41.424  1.00 10.32 ? 101  ASP F C   1 
ATOM   5197  O  O   . ASP E  1 101 ? 27.822 -11.307 -41.362  1.00 10.89 ? 101  ASP F O   1 
ATOM   5198  C  CB  . ASP E  1 101 ? 25.251 -9.551  -41.281  1.00 9.40  ? 101  ASP F CB  1 
ATOM   5199  C  CG  . ASP E  1 101 ? 25.281 -8.525  -40.161  1.00 10.57 ? 101  ASP F CG  1 
ATOM   5200  O  OD1 . ASP E  1 101 ? 25.554 -8.901  -39.006  1.00 9.50  ? 101  ASP F OD1 1 
ATOM   5201  O  OD2 . ASP E  1 101 ? 25.042 -7.336  -40.445  1.00 12.62 ? 101  ASP F OD2 1 
ATOM   5202  N  N   . SER E  1 102 ? 28.494 -9.221  -40.821  1.00 10.42 ? 102  SER F N   1 
ATOM   5203  C  CA  . SER E  1 102 ? 29.684 -9.674  -40.100  1.00 11.82 ? 102  SER F CA  1 
ATOM   5204  C  C   . SER E  1 102 ? 29.532 -9.618  -38.572  1.00 11.66 ? 102  SER F C   1 
ATOM   5205  O  O   . SER E  1 102 ? 30.445 -10.000 -37.860  1.00 12.82 ? 102  SER F O   1 
ATOM   5206  C  CB  . SER E  1 102 ? 30.895 -8.853  -40.543  1.00 12.61 ? 102  SER F CB  1 
ATOM   5207  O  OG  . SER E  1 102 ? 31.170 -9.126  -41.906  1.00 15.49 ? 102  SER F OG  1 
ATOM   5208  N  N   . VAL E  1 103 ? 28.380 -9.150  -38.080  1.00 11.69 ? 103  VAL F N   1 
ATOM   5209  C  CA  . VAL E  1 103 ? 28.110 -9.028  -36.632  1.00 11.16 ? 103  VAL F CA  1 
ATOM   5210  C  C   . VAL E  1 103 ? 27.389 -10.274 -36.109  1.00 11.40 ? 103  VAL F C   1 
ATOM   5211  O  O   . VAL E  1 103 ? 27.804 -10.857 -35.104  1.00 11.32 ? 103  VAL F O   1 
ATOM   5212  C  CB  . VAL E  1 103 ? 27.314 -7.733  -36.310  1.00 10.69 ? 103  VAL F CB  1 
ATOM   5213  C  CG1 . VAL E  1 103 ? 26.826 -7.676  -34.846  1.00 11.15 ? 103  VAL F CG1 1 
ATOM   5214  C  CG2 . VAL E  1 103 ? 28.179 -6.507  -36.607  1.00 11.05 ? 103  VAL F CG2 1 
ATOM   5215  N  N   . ILE E  1 104 ? 26.316 -10.681 -36.781  1.00 10.42 ? 104  ILE F N   1 
ATOM   5216  C  CA  . ILE E  1 104 ? 25.733 -11.996 -36.474  1.00 10.43 ? 104  ILE F CA  1 
ATOM   5217  C  C   . ILE E  1 104 ? 26.808 -13.069 -36.780  1.00 10.13 ? 104  ILE F C   1 
ATOM   5218  O  O   . ILE E  1 104 ? 27.757 -12.819 -37.528  1.00 10.48 ? 104  ILE F O   1 
ATOM   5219  C  CB  . ILE E  1 104 ? 24.432 -12.270 -37.248  1.00 9.42  ? 104  ILE F CB  1 
ATOM   5220  C  CG1 . ILE E  1 104 ? 24.708 -12.340 -38.763  1.00 8.32  ? 104  ILE F CG1 1 
ATOM   5221  C  CG2 . ILE E  1 104 ? 23.360 -11.214 -36.928  1.00 10.59 ? 104  ILE F CG2 1 
ATOM   5222  C  CD1 . ILE E  1 104 ? 23.575 -12.945 -39.542  1.00 8.21  ? 104  ILE F CD1 1 
ATOM   5223  N  N   . SER E  1 105 ? 26.685 -14.244 -36.173  1.00 10.85 ? 105  SER F N   1 
ATOM   5224  C  CA  . SER E  1 105 ? 27.568 -15.371 -36.504  1.00 10.50 ? 105  SER F CA  1 
ATOM   5225  C  C   . SER E  1 105 ? 26.777 -16.673 -36.328  1.00 10.68 ? 105  SER F C   1 
ATOM   5226  O  O   . SER E  1 105 ? 25.671 -16.662 -35.754  1.00 9.42  ? 105  SER F O   1 
ATOM   5227  C  CB  . SER E  1 105 ? 28.808 -15.391 -35.607  1.00 10.52 ? 105  SER F CB  1 
ATOM   5228  O  OG  . SER E  1 105 ? 29.790 -16.312 -36.073  1.00 12.29 ? 105  SER F OG  1 
ATOM   5229  N  N   . LEU E  1 106 ? 27.347 -17.769 -36.826  1.00 10.20 ? 106  LEU F N   1 
ATOM   5230  C  CA  . LEU E  1 106 ? 26.763 -19.110 -36.680  1.00 12.05 ? 106  LEU F CA  1 
ATOM   5231  C  C   . LEU E  1 106 ? 27.512 -19.930 -35.628  1.00 12.79 ? 106  LEU F C   1 
ATOM   5232  O  O   . LEU E  1 106 ? 27.242 -21.126 -35.461  1.00 12.56 ? 106  LEU F O   1 
ATOM   5233  C  CB  . LEU E  1 106 ? 26.690 -19.860 -38.030  1.00 11.48 ? 106  LEU F CB  1 
ATOM   5234  C  CG  . LEU E  1 106 ? 25.878 -19.139 -39.121  1.00 12.79 ? 106  LEU F CG  1 
ATOM   5235  C  CD1 . LEU E  1 106 ? 25.859 -19.946 -40.440  1.00 14.93 ? 106  LEU F CD1 1 
ATOM   5236  C  CD2 . LEU E  1 106 ? 24.445 -18.812 -38.672  1.00 11.34 ? 106  LEU F CD2 1 
ATOM   5237  N  N   . SER E  1 107 ? 28.400 -19.265 -34.879  1.00 13.32 ? 107  SER F N   1 
ATOM   5238  C  CA  . SER E  1 107 ? 29.019 -19.847 -33.671  1.00 14.71 ? 107  SER F CA  1 
ATOM   5239  C  C   . SER E  1 107 ? 29.490 -18.735 -32.717  1.00 14.49 ? 107  SER F C   1 
ATOM   5240  O  O   . SER E  1 107 ? 29.474 -17.561 -33.076  1.00 13.60 ? 107  SER F O   1 
ATOM   5241  C  CB  . SER E  1 107 ? 30.189 -20.747 -34.050  1.00 14.08 ? 107  SER F CB  1 
ATOM   5242  O  OG  . SER E  1 107 ? 31.240 -19.970 -34.571  1.00 17.82 ? 107  SER F OG  1 
ATOM   5243  N  N   . GLY E  1 108 ? 29.905 -19.114 -31.511  1.00 15.22 ? 108  GLY F N   1 
ATOM   5244  C  CA  . GLY E  1 108 ? 30.447 -18.165 -30.534  1.00 15.14 ? 108  GLY F CA  1 
ATOM   5245  C  C   . GLY E  1 108 ? 29.406 -17.245 -29.926  1.00 15.60 ? 108  GLY F C   1 
ATOM   5246  O  O   . GLY E  1 108 ? 28.200 -17.465 -30.061  1.00 15.50 ? 108  GLY F O   1 
ATOM   5247  N  N   . ASP E  1 109 ? 29.881 -16.188 -29.274  1.00 16.52 ? 109  ASP F N   1 
ATOM   5248  C  CA  . ASP E  1 109 ? 29.037 -15.239 -28.525  1.00 16.93 ? 109  ASP F CA  1 
ATOM   5249  C  C   . ASP E  1 109 ? 27.913 -14.587 -29.318  1.00 16.35 ? 109  ASP F C   1 
ATOM   5250  O  O   . ASP E  1 109 ? 26.900 -14.147 -28.757  1.00 16.33 ? 109  ASP F O   1 
ATOM   5251  C  CB  . ASP E  1 109 ? 29.918 -14.123 -27.947  1.00 18.01 ? 109  ASP F CB  1 
ATOM   5252  C  CG  . ASP E  1 109 ? 30.826 -14.605 -26.832  1.00 21.17 ? 109  ASP F CG  1 
ATOM   5253  O  OD1 . ASP E  1 109 ? 31.721 -13.830 -26.425  1.00 24.18 ? 109  ASP F OD1 1 
ATOM   5254  O  OD2 . ASP E  1 109 ? 30.659 -15.756 -26.362  1.00 24.44 ? 109  ASP F OD2 1 
ATOM   5255  N  N   . HIS E  1 110 ? 28.108 -14.466 -30.623  1.00 15.95 ? 110  HIS F N   1 
ATOM   5256  C  CA  . HIS E  1 110 ? 27.115 -13.804 -31.452  1.00 15.61 ? 110  HIS F CA  1 
ATOM   5257  C  C   . HIS E  1 110 ? 26.297 -14.844 -32.227  1.00 15.00 ? 110  HIS F C   1 
ATOM   5258  O  O   . HIS E  1 110 ? 25.645 -14.511 -33.207  1.00 14.76 ? 110  HIS F O   1 
ATOM   5259  C  CB  . HIS E  1 110 ? 27.794 -12.804 -32.392  1.00 15.94 ? 110  HIS F CB  1 
ATOM   5260  C  CG  . HIS E  1 110 ? 28.505 -11.689 -31.682  1.00 18.07 ? 110  HIS F CG  1 
ATOM   5261  N  ND1 . HIS E  1 110 ? 29.125 -10.657 -32.351  1.00 20.87 ? 110  HIS F ND1 1 
ATOM   5262  C  CD2 . HIS E  1 110 ? 28.661 -11.430 -30.361  1.00 20.29 ? 110  HIS F CD2 1 
ATOM   5263  C  CE1 . HIS E  1 110 ? 29.658 -9.824  -31.474  1.00 21.30 ? 110  HIS F CE1 1 
ATOM   5264  N  NE2 . HIS E  1 110 ? 29.383 -10.266 -30.260  1.00 22.37 ? 110  HIS F NE2 1 
HETATM 5265  N  N   . CME E  1 111 ? 26.291 -16.095 -31.760  1.00 14.58 ? 111  CME F N   1 
HETATM 5266  C  CA  . CME E  1 111 ? 25.602 -17.173 -32.495  1.00 13.45 ? 111  CME F CA  1 
HETATM 5267  C  CB  . CME E  1 111 ? 25.829 -18.557 -31.884  1.00 14.03 ? 111  CME F CB  1 
HETATM 5268  S  SG  . CME E  1 111 ? 25.288 -19.809 -33.029  1.00 18.95 ? 111  CME F SG  1 
HETATM 5269  S  SD  . CME E  1 111 ? 25.759 -21.501 -32.040  1.00 25.02 ? 111  CME F SD  1 
HETATM 5270  C  CE  . CME E  1 111 ? 24.317 -21.746 -31.056  1.00 29.42 ? 111  CME F CE  1 
HETATM 5271  C  CZ  . CME E  1 111 ? 24.518 -21.094 -29.696  1.00 31.38 ? 111  CME F CZ  1 
HETATM 5272  O  OH  . CME E  1 111 ? 23.556 -20.043 -29.551  1.00 35.05 ? 111  CME F OH  1 
HETATM 5273  C  C   . CME E  1 111 ? 24.137 -16.880 -32.516  1.00 12.58 ? 111  CME F C   1 
HETATM 5274  O  O   . CME E  1 111 ? 23.564 -16.550 -31.481  1.00 11.33 ? 111  CME F O   1 
ATOM   5275  N  N   . ILE E  1 112 ? 23.513 -17.005 -33.691  1.00 10.48 ? 112  ILE F N   1 
ATOM   5276  C  CA  . ILE E  1 112 ? 22.083 -16.789 -33.826  1.00 10.24 ? 112  ILE F CA  1 
ATOM   5277  C  C   . ILE E  1 112 ? 21.299 -18.115 -33.969  1.00 10.07 ? 112  ILE F C   1 
ATOM   5278  O  O   . ILE E  1 112 ? 20.055 -18.124 -34.020  1.00 9.63  ? 112  ILE F O   1 
ATOM   5279  C  CB  . ILE E  1 112 ? 21.748 -15.846 -35.013  1.00 9.94  ? 112  ILE F CB  1 
ATOM   5280  C  CG1 . ILE E  1 112 ? 22.290 -16.422 -36.330  1.00 10.48 ? 112  ILE F CG1 1 
ATOM   5281  C  CG2 . ILE E  1 112 ? 22.316 -14.433 -34.764  1.00 8.63  ? 112  ILE F CG2 1 
ATOM   5282  C  CD1 . ILE E  1 112 ? 21.649 -15.820 -37.514  1.00 11.00 ? 112  ILE F CD1 1 
ATOM   5283  N  N   . ILE E  1 113 ? 22.017 -19.228 -34.041  1.00 10.92 ? 113  ILE F N   1 
ATOM   5284  C  CA  . ILE E  1 113 ? 21.340 -20.542 -34.104  1.00 11.49 ? 113  ILE F CA  1 
ATOM   5285  C  C   . ILE E  1 113 ? 20.592 -20.744 -32.771  1.00 11.84 ? 113  ILE F C   1 
ATOM   5286  O  O   . ILE E  1 113 ? 21.126 -20.435 -31.700  1.00 13.47 ? 113  ILE F O   1 
ATOM   5287  C  CB  . ILE E  1 113 ? 22.341 -21.704 -34.416  1.00 11.48 ? 113  ILE F CB  1 
ATOM   5288  C  CG1 . ILE E  1 113 ? 22.952 -21.537 -35.818  1.00 11.22 ? 113  ILE F CG1 1 
ATOM   5289  C  CG2 . ILE E  1 113 ? 21.658 -23.088 -34.309  1.00 12.96 ? 113  ILE F CG2 1 
ATOM   5290  C  CD1 . ILE E  1 113 ? 24.211 -22.401 -36.089  1.00 10.79 ? 113  ILE F CD1 1 
ATOM   5291  N  N   . GLY E  1 114 ? 19.337 -21.173 -32.848  1.00 10.84 ? 114  GLY F N   1 
ATOM   5292  C  CA  . GLY E  1 114 ? 18.527 -21.427 -31.648  1.00 11.52 ? 114  GLY F CA  1 
ATOM   5293  C  C   . GLY E  1 114 ? 17.755 -20.190 -31.228  1.00 10.70 ? 114  GLY F C   1 
ATOM   5294  O  O   . GLY E  1 114 ? 17.060 -20.191 -30.198  1.00 10.60 ? 114  GLY F O   1 
ATOM   5295  N  N   . ARG E  1 115 ? 17.880 -19.130 -32.021  1.00 10.06 ? 115  ARG F N   1 
ATOM   5296  C  CA  . ARG E  1 115 ? 17.145 -17.885 -31.754  1.00 10.03 ? 115  ARG F CA  1 
ATOM   5297  C  C   . ARG E  1 115 ? 16.083 -17.727 -32.825  1.00 9.98  ? 115  ARG F C   1 
ATOM   5298  O  O   . ARG E  1 115 ? 15.933 -18.606 -33.649  1.00 12.33 ? 115  ARG F O   1 
ATOM   5299  C  CB  . ARG E  1 115 ? 18.120 -16.703 -31.675  1.00 9.58  ? 115  ARG F CB  1 
ATOM   5300  C  CG  . ARG E  1 115 ? 19.255 -16.992 -30.671  1.00 10.02 ? 115  ARG F CG  1 
ATOM   5301  C  CD  . ARG E  1 115 ? 19.942 -15.727 -30.170  1.00 8.58  ? 115  ARG F CD  1 
ATOM   5302  N  NE  . ARG E  1 115 ? 21.063 -16.039 -29.285  1.00 9.70  ? 115  ARG F NE  1 
ATOM   5303  C  CZ  . ARG E  1 115 ? 20.983 -16.108 -27.956  1.00 11.24 ? 115  ARG F CZ  1 
ATOM   5304  N  NH1 . ARG E  1 115 ? 22.088 -16.385 -27.245  1.00 10.28 ? 115  ARG F NH1 1 
ATOM   5305  N  NH2 . ARG E  1 115 ? 19.804 -15.916 -27.337  1.00 7.50  ? 115  ARG F NH2 1 
ATOM   5306  N  N   . THR E  1 116 ? 15.285 -16.669 -32.777  1.00 11.40 ? 116  THR F N   1 
ATOM   5307  C  CA  . THR E  1 116 ? 14.110 -16.588 -33.645  1.00 10.94 ? 116  THR F CA  1 
ATOM   5308  C  C   . THR E  1 116 ? 14.262 -15.462 -34.649  1.00 10.82 ? 116  THR F C   1 
ATOM   5309  O  O   . THR E  1 116 ? 14.587 -14.340 -34.280  1.00 11.10 ? 116  THR F O   1 
ATOM   5310  C  CB  . THR E  1 116 ? 12.823 -16.379 -32.824  1.00 11.02 ? 116  THR F CB  1 
ATOM   5311  O  OG1 . THR E  1 116 ? 12.567 -17.557 -32.069  1.00 11.24 ? 116  THR F OG1 1 
ATOM   5312  C  CG2 . THR E  1 116 ? 11.617 -16.109 -33.713  1.00 9.64  ? 116  THR F CG2 1 
ATOM   5313  N  N   . LEU E  1 117 ? 14.016 -15.759 -35.919  1.00 9.80  ? 117  LEU F N   1 
ATOM   5314  C  CA  . LEU E  1 117 ? 14.091 -14.714 -36.920  1.00 9.67  ? 117  LEU F CA  1 
ATOM   5315  C  C   . LEU E  1 117 ? 12.676 -14.200 -37.099  1.00 9.63  ? 117  LEU F C   1 
ATOM   5316  O  O   . LEU E  1 117 ? 11.713 -15.001 -37.171  1.00 9.04  ? 117  LEU F O   1 
ATOM   5317  C  CB  . LEU E  1 117 ? 14.649 -15.279 -38.238  1.00 9.10  ? 117  LEU F CB  1 
ATOM   5318  C  CG  . LEU E  1 117 ? 14.704 -14.377 -39.481  1.00 8.52  ? 117  LEU F CG  1 
ATOM   5319  C  CD1 . LEU E  1 117 ? 15.756 -13.289 -39.270  1.00 8.76  ? 117  LEU F CD1 1 
ATOM   5320  C  CD2 . LEU E  1 117 ? 15.032 -15.180 -40.735  1.00 7.63  ? 117  LEU F CD2 1 
ATOM   5321  N  N   . VAL E  1 118 ? 12.544 -12.873 -37.185  1.00 9.06  ? 118  VAL F N   1 
ATOM   5322  C  CA  . VAL E  1 118 ? 11.239 -12.233 -37.284  1.00 8.46  ? 118  VAL F CA  1 
ATOM   5323  C  C   . VAL E  1 118 ? 11.204 -11.270 -38.457  1.00 8.44  ? 118  VAL F C   1 
ATOM   5324  O  O   . VAL E  1 118 ? 12.141 -10.476 -38.644  1.00 9.83  ? 118  VAL F O   1 
ATOM   5325  C  CB  . VAL E  1 118 ? 10.922 -11.423 -35.970  1.00 8.67  ? 118  VAL F CB  1 
ATOM   5326  C  CG1 . VAL E  1 118 ? 9.553  -10.721 -36.067  1.00 9.43  ? 118  VAL F CG1 1 
ATOM   5327  C  CG2 . VAL E  1 118 ? 10.958 -12.335 -34.757  1.00 7.45  ? 118  VAL F CG2 1 
ATOM   5328  N  N   . VAL E  1 119 ? 10.119 -11.319 -39.215  1.00 8.11  ? 119  VAL F N   1 
ATOM   5329  C  CA  . VAL E  1 119 ? 9.769  -10.275 -40.182  1.00 8.89  ? 119  VAL F CA  1 
ATOM   5330  C  C   . VAL E  1 119 ? 8.548  -9.469  -39.707  1.00 9.11  ? 119  VAL F C   1 
ATOM   5331  O  O   . VAL E  1 119 ? 7.576  -10.019 -39.167  1.00 9.48  ? 119  VAL F O   1 
ATOM   5332  C  CB  . VAL E  1 119 ? 9.638  -10.805 -41.662  1.00 8.22  ? 119  VAL F CB  1 
ATOM   5333  C  CG1 . VAL E  1 119 ? 8.478  -11.850 -41.823  1.00 9.42  ? 119  VAL F CG1 1 
ATOM   5334  C  CG2 . VAL E  1 119 ? 9.470  -9.663  -42.648  1.00 8.99  ? 119  VAL F CG2 1 
ATOM   5335  N  N   . HIS E  1 120 ? 8.610  -8.158  -39.916  1.00 9.30  ? 120  HIS F N   1 
ATOM   5336  C  CA  . HIS E  1 120 ? 7.695  -7.244  -39.238  1.00 8.93  ? 120  HIS F CA  1 
ATOM   5337  C  C   . HIS E  1 120 ? 6.676  -6.601  -40.164  1.00 9.50  ? 120  HIS F C   1 
ATOM   5338  O  O   . HIS E  1 120 ? 6.842  -6.609  -41.383  1.00 9.83  ? 120  HIS F O   1 
ATOM   5339  C  CB  . HIS E  1 120 ? 8.513  -6.154  -38.527  1.00 8.67  ? 120  HIS F CB  1 
ATOM   5340  C  CG  . HIS E  1 120 ? 9.096  -6.585  -37.216  1.00 8.59  ? 120  HIS F CG  1 
ATOM   5341  N  ND1 . HIS E  1 120 ? 8.415  -6.472  -36.021  1.00 6.71  ? 120  HIS F ND1 1 
ATOM   5342  C  CD2 . HIS E  1 120 ? 10.298 -7.129  -36.912  1.00 6.46  ? 120  HIS F CD2 1 
ATOM   5343  C  CE1 . HIS E  1 120 ? 9.175  -6.925  -35.036  1.00 8.25  ? 120  HIS F CE1 1 
ATOM   5344  N  NE2 . HIS E  1 120 ? 10.328 -7.313  -35.552  1.00 8.86  ? 120  HIS F NE2 1 
ATOM   5345  N  N   . GLU E  1 121 ? 5.651  -5.993  -39.553  1.00 10.24 ? 121  GLU F N   1 
ATOM   5346  C  CA  . GLU E  1 121 ? 4.580  -5.324  -40.255  1.00 11.13 ? 121  GLU F CA  1 
ATOM   5347  C  C   . GLU E  1 121 ? 5.055  -4.059  -40.921  1.00 11.87 ? 121  GLU F C   1 
ATOM   5348  O  O   . GLU E  1 121 ? 4.682  -3.775  -42.066  1.00 12.57 ? 121  GLU F O   1 
ATOM   5349  C  CB  . GLU E  1 121 ? 3.416  -5.038  -39.288  1.00 11.95 ? 121  GLU F CB  1 
ATOM   5350  C  CG  . GLU E  1 121 ? 2.215  -4.276  -39.911  1.00 13.90 ? 121  GLU F CG  1 
ATOM   5351  C  CD  . GLU E  1 121 ? 0.963  -4.305  -39.020  1.00 20.28 ? 121  GLU F CD  1 
ATOM   5352  O  OE1 . GLU E  1 121 ? 0.968  -5.011  -37.978  1.00 21.86 ? 121  GLU F OE1 1 
ATOM   5353  O  OE2 . GLU E  1 121 ? -0.038 -3.628  -39.360  1.00 19.57 ? 121  GLU F OE2 1 
ATOM   5354  N  N   . LYS E  1 122 ? 5.914  -3.330  -40.218  1.00 12.33 ? 122  LYS F N   1 
ATOM   5355  C  CA  . LYS E  1 122 ? 6.338  -1.993  -40.605  1.00 12.88 ? 122  LYS F CA  1 
ATOM   5356  C  C   . LYS E  1 122 ? 7.850  -1.925  -40.850  1.00 12.68 ? 122  LYS F C   1 
ATOM   5357  O  O   . LYS E  1 122 ? 8.605  -2.785  -40.376  1.00 11.65 ? 122  LYS F O   1 
ATOM   5358  C  CB  . LYS E  1 122 ? 5.982  -1.001  -39.499  1.00 13.59 ? 122  LYS F CB  1 
ATOM   5359  C  CG  . LYS E  1 122 ? 4.486  -0.707  -39.340  1.00 15.82 ? 122  LYS F CG  1 
ATOM   5360  C  CD  . LYS E  1 122 ? 4.263  0.199   -38.130  1.00 20.27 ? 122  LYS F CD  1 
ATOM   5361  C  CE  . LYS E  1 122 ? 2.838  0.803   -38.099  1.00 23.46 ? 122  LYS F CE  1 
ATOM   5362  N  NZ  . LYS E  1 122 ? 1.757  -0.162  -37.673  1.00 26.67 ? 122  LYS F NZ  1 
ATOM   5363  N  N   . ALA E  1 123 ? 8.265  -0.882  -41.569  1.00 12.13 ? 123  ALA F N   1 
ATOM   5364  C  CA  . ALA E  1 123 ? 9.686  -0.579  -41.760  1.00 12.19 ? 123  ALA F CA  1 
ATOM   5365  C  C   . ALA E  1 123 ? 10.375 -0.338  -40.419  1.00 12.38 ? 123  ALA F C   1 
ATOM   5366  O  O   . ALA E  1 123 ? 9.788  0.257   -39.501  1.00 12.49 ? 123  ALA F O   1 
ATOM   5367  C  CB  . ALA E  1 123 ? 9.851  0.652   -42.653  1.00 12.28 ? 123  ALA F CB  1 
ATOM   5368  N  N   . ASP E  1 124 ? 11.611 -0.819  -40.314  1.00 12.08 ? 124  ASP F N   1 
ATOM   5369  C  CA  . ASP E  1 124 ? 12.517 -0.526  -39.200  1.00 11.71 ? 124  ASP F CA  1 
ATOM   5370  C  C   . ASP E  1 124 ? 13.182 0.846   -39.511  1.00 11.36 ? 124  ASP F C   1 
ATOM   5371  O  O   . ASP E  1 124 ? 13.727 1.037   -40.604  1.00 9.47  ? 124  ASP F O   1 
ATOM   5372  C  CB  . ASP E  1 124 ? 13.528 -1.678  -39.132  1.00 12.24 ? 124  ASP F CB  1 
ATOM   5373  C  CG  . ASP E  1 124 ? 14.554 -1.553  -38.009  1.00 12.93 ? 124  ASP F CG  1 
ATOM   5374  O  OD1 . ASP E  1 124 ? 14.861 -0.430  -37.521  1.00 11.16 ? 124  ASP F OD1 1 
ATOM   5375  O  OD2 . ASP E  1 124 ? 15.094 -2.620  -37.627  1.00 10.26 ? 124  ASP F OD2 1 
ATOM   5376  N  N   . ASP E  1 125 ? 13.114 1.805   -38.573  1.00 11.00 ? 125  ASP F N   1 
ATOM   5377  C  CA  . ASP E  1 125 ? 13.725 3.125   -38.808  1.00 10.74 ? 125  ASP F CA  1 
ATOM   5378  C  C   . ASP E  1 125 ? 15.218 3.194   -38.483  1.00 10.54 ? 125  ASP F C   1 
ATOM   5379  O  O   . ASP E  1 125 ? 15.815 4.280   -38.515  1.00 9.83  ? 125  ASP F O   1 
ATOM   5380  C  CB  . ASP E  1 125 ? 12.954 4.263   -38.094  1.00 10.51 ? 125  ASP F CB  1 
ATOM   5381  C  CG  . ASP E  1 125 ? 13.029 4.193   -36.573  1.00 11.41 ? 125  ASP F CG  1 
ATOM   5382  O  OD1 . ASP E  1 125 ? 12.196 4.893   -35.925  1.00 12.90 ? 125  ASP F OD1 1 
ATOM   5383  O  OD2 . ASP E  1 125 ? 13.892 3.477   -35.994  1.00 10.14 ? 125  ASP F OD2 1 
ATOM   5384  N  N   . LEU E  1 126 ? 15.802 2.037   -38.156  1.00 10.03 ? 126  LEU F N   1 
ATOM   5385  C  CA  . LEU E  1 126 ? 17.256 1.877   -38.015  1.00 9.40  ? 126  LEU F CA  1 
ATOM   5386  C  C   . LEU E  1 126 ? 17.811 2.721   -36.855  1.00 9.21  ? 126  LEU F C   1 
ATOM   5387  O  O   . LEU E  1 126 ? 18.982 3.087   -36.833  1.00 9.04  ? 126  LEU F O   1 
ATOM   5388  C  CB  . LEU E  1 126 ? 17.969 2.162   -39.358  1.00 8.69  ? 126  LEU F CB  1 
ATOM   5389  C  CG  . LEU E  1 126 ? 17.402 1.437   -40.599  1.00 8.23  ? 126  LEU F CG  1 
ATOM   5390  C  CD1 . LEU E  1 126 ? 18.224 1.736   -41.851  1.00 8.33  ? 126  LEU F CD1 1 
ATOM   5391  C  CD2 . LEU E  1 126 ? 17.306 -0.071  -40.314  1.00 5.74  ? 126  LEU F CD2 1 
ATOM   5392  N  N   . GLY E  1 127 ? 16.966 2.980   -35.862  1.00 8.88  ? 127  GLY F N   1 
ATOM   5393  C  CA  . GLY E  1 127 ? 17.402 3.690   -34.658  1.00 7.75  ? 127  GLY F CA  1 
ATOM   5394  C  C   . GLY E  1 127 ? 17.447 5.194   -34.817  1.00 7.28  ? 127  GLY F C   1 
ATOM   5395  O  O   . GLY E  1 127 ? 17.996 5.915   -33.960  1.00 7.77  ? 127  GLY F O   1 
ATOM   5396  N  N   . LYS E  1 128 ? 16.867 5.672   -35.905  1.00 6.76  ? 128  LYS F N   1 
ATOM   5397  C  CA  . LYS E  1 128 ? 16.972 7.082   -36.275  1.00 7.62  ? 128  LYS F CA  1 
ATOM   5398  C  C   . LYS E  1 128 ? 15.648 7.839   -36.085  1.00 6.93  ? 128  LYS F C   1 
ATOM   5399  O  O   . LYS E  1 128 ? 15.478 8.945   -36.633  1.00 7.54  ? 128  LYS F O   1 
ATOM   5400  C  CB  . LYS E  1 128 ? 17.440 7.202   -37.721  1.00 8.54  ? 128  LYS F CB  1 
ATOM   5401  C  CG  . LYS E  1 128 ? 18.828 6.571   -37.998  1.00 9.33  ? 128  LYS F CG  1 
ATOM   5402  C  CD  . LYS E  1 128 ? 19.141 6.572   -39.492  1.00 12.52 ? 128  LYS F CD  1 
ATOM   5403  C  CE  . LYS E  1 128 ? 19.600 7.944   -39.983  1.00 15.18 ? 128  LYS F CE  1 
ATOM   5404  N  NZ  . LYS E  1 128 ? 19.961 7.857   -41.426  1.00 17.00 ? 128  LYS F NZ  1 
ATOM   5405  N  N   . GLY E  1 129 ? 14.740 7.240   -35.325  1.00 7.83  ? 129  GLY F N   1 
ATOM   5406  C  CA  . GLY E  1 129 ? 13.371 7.788   -35.145  1.00 8.63  ? 129  GLY F CA  1 
ATOM   5407  C  C   . GLY E  1 129 ? 13.237 8.891   -34.104  1.00 9.72  ? 129  GLY F C   1 
ATOM   5408  O  O   . GLY E  1 129 ? 12.212 9.602   -34.067  1.00 10.39 ? 129  GLY F O   1 
ATOM   5409  N  N   . GLY E  1 130 ? 14.251 9.033   -33.247  1.00 9.62  ? 130  GLY F N   1 
ATOM   5410  C  CA  . GLY E  1 130 ? 14.270 10.110  -32.258  1.00 9.81  ? 130  GLY F CA  1 
ATOM   5411  C  C   . GLY E  1 130 ? 13.318 9.923   -31.097  1.00 11.00 ? 130  GLY F C   1 
ATOM   5412  O  O   . GLY E  1 130 ? 13.250 10.749  -30.198  1.00 9.82  ? 130  GLY F O   1 
ATOM   5413  N  N   . ASN E  1 131 ? 12.566 8.828   -31.112  1.00 10.86 ? 131  ASN F N   1 
ATOM   5414  C  CA  . ASN E  1 131 ? 11.719 8.525   -29.989  1.00 11.22 ? 131  ASN F CA  1 
ATOM   5415  C  C   . ASN E  1 131 ? 12.277 7.308   -29.269  1.00 11.75 ? 131  ASN F C   1 
ATOM   5416  O  O   . ASN E  1 131 ? 13.208 6.656   -29.761  1.00 11.55 ? 131  ASN F O   1 
ATOM   5417  C  CB  . ASN E  1 131 ? 10.235 8.402   -30.412  1.00 11.47 ? 131  ASN F CB  1 
ATOM   5418  C  CG  . ASN E  1 131 ? 9.952  7.180   -31.243  1.00 10.73 ? 131  ASN F CG  1 
ATOM   5419  O  OD1 . ASN E  1 131 ? 10.874 6.496   -31.698  1.00 13.85 ? 131  ASN F OD1 1 
ATOM   5420  N  ND2 . ASN E  1 131 ? 8.660  6.889   -31.457  1.00 14.39 ? 131  ASN F ND2 1 
ATOM   5421  N  N   . GLU E  1 132 ? 11.740 7.010   -28.101  1.00 12.27 ? 132  GLU F N   1 
ATOM   5422  C  CA  . GLU E  1 132 ? 12.320 5.982   -27.251  1.00 13.57 ? 132  GLU F CA  1 
ATOM   5423  C  C   . GLU E  1 132 ? 12.227 4.613   -27.936  1.00 13.33 ? 132  GLU F C   1 
ATOM   5424  O  O   . GLU E  1 132 ? 13.124 3.790   -27.793  1.00 12.38 ? 132  GLU F O   1 
ATOM   5425  C  CB  . GLU E  1 132 ? 11.622 5.938   -25.885  1.00 14.93 ? 132  GLU F CB  1 
ATOM   5426  C  CG  . GLU E  1 132 ? 12.103 4.805   -24.958  1.00 18.39 ? 132  GLU F CG  1 
ATOM   5427  C  CD  . GLU E  1 132 ? 13.569 4.932   -24.518  1.00 22.49 ? 132  GLU F CD  1 
ATOM   5428  O  OE1 . GLU E  1 132 ? 14.078 6.068   -24.344  1.00 26.76 ? 132  GLU F OE1 1 
ATOM   5429  O  OE2 . GLU E  1 132 ? 14.217 3.881   -24.315  1.00 23.84 ? 132  GLU F OE2 1 
ATOM   5430  N  N   . GLU E  1 133 ? 11.139 4.403   -28.670  1.00 13.85 ? 133  GLU F N   1 
ATOM   5431  C  CA  . GLU E  1 133 ? 10.893 3.110   -29.320  1.00 15.02 ? 133  GLU F CA  1 
ATOM   5432  C  C   . GLU E  1 133 ? 11.868 2.856   -30.489  1.00 14.60 ? 133  GLU F C   1 
ATOM   5433  O  O   . GLU E  1 133 ? 12.253 1.709   -30.754  1.00 15.32 ? 133  GLU F O   1 
ATOM   5434  C  CB  . GLU E  1 133 ? 9.433  2.985   -29.761  1.00 15.73 ? 133  GLU F CB  1 
ATOM   5435  C  CG  . GLU E  1 133 ? 9.012  1.566   -30.162  1.00 19.18 ? 133  GLU F CG  1 
ATOM   5436  C  CD  . GLU E  1 133 ? 9.109  0.519   -29.033  1.00 21.52 ? 133  GLU F CD  1 
ATOM   5437  O  OE1 . GLU E  1 133 ? 9.920  0.660   -28.099  1.00 24.44 ? 133  GLU F OE1 1 
ATOM   5438  O  OE2 . GLU E  1 133 ? 8.377  -0.491  -29.099  1.00 25.39 ? 133  GLU F OE2 1 
ATOM   5439  N  N   . SER E  1 134 ? 12.285 3.916   -31.180  1.00 14.08 ? 134  SER F N   1 
ATOM   5440  C  CA  . SER E  1 134 ? 13.320 3.758   -32.210  1.00 13.31 ? 134  SER F CA  1 
ATOM   5441  C  C   . SER E  1 134 ? 14.570 3.022   -31.675  1.00 13.25 ? 134  SER F C   1 
ATOM   5442  O  O   . SER E  1 134 ? 15.139 2.170   -32.364  1.00 13.19 ? 134  SER F O   1 
ATOM   5443  C  CB  . SER E  1 134 ? 13.704 5.114   -32.785  1.00 12.55 ? 134  SER F CB  1 
ATOM   5444  O  OG  . SER E  1 134 ? 14.597 4.967   -33.866  1.00 11.67 ? 134  SER F OG  1 
ATOM   5445  N  N   . THR E  1 135 ? 14.977 3.352   -30.447  1.00 13.47 ? 135  THR F N   1 
ATOM   5446  C  CA  . THR E  1 135 ? 16.183 2.809   -29.798  1.00 13.75 ? 135  THR F CA  1 
ATOM   5447  C  C   . THR E  1 135 ? 16.021 1.381   -29.304  1.00 13.78 ? 135  THR F C   1 
ATOM   5448  O  O   . THR E  1 135 ? 16.993 0.780   -28.799  1.00 12.70 ? 135  THR F O   1 
ATOM   5449  C  CB  . THR E  1 135 ? 16.585 3.634   -28.537  1.00 14.86 ? 135  THR F CB  1 
ATOM   5450  O  OG1 . THR E  1 135 ? 15.638 3.387   -27.481  1.00 15.12 ? 135  THR F OG1 1 
ATOM   5451  C  CG2 . THR E  1 135 ? 16.625 5.129   -28.847  1.00 16.77 ? 135  THR F CG2 1 
ATOM   5452  N  N   . LYS E  1 136 ? 14.797 0.852   -29.417  1.00 13.88 ? 136  LYS F N   1 
ATOM   5453  C  CA  . LYS E  1 136 ? 14.514 -0.504  -28.977  1.00 14.78 ? 136  LYS F CA  1 
ATOM   5454  C  C   . LYS E  1 136 ? 14.155 -1.432  -30.129  1.00 14.30 ? 136  LYS F C   1 
ATOM   5455  O  O   . LYS E  1 136 ? 14.737 -2.482  -30.262  1.00 14.57 ? 136  LYS F O   1 
ATOM   5456  C  CB  . LYS E  1 136 ? 13.379 -0.516  -27.943  1.00 15.23 ? 136  LYS F CB  1 
ATOM   5457  C  CG  . LYS E  1 136 ? 13.565 0.455   -26.783  1.00 17.01 ? 136  LYS F CG  1 
ATOM   5458  C  CD  . LYS E  1 136 ? 12.390 0.384   -25.804  1.00 21.14 ? 136  LYS F CD  1 
ATOM   5459  C  CE  . LYS E  1 136 ? 12.763 1.073   -24.495  1.00 23.67 ? 136  LYS F CE  1 
ATOM   5460  N  NZ  . LYS E  1 136 ? 11.711 0.988   -23.458  1.00 24.59 ? 136  LYS F NZ  1 
ATOM   5461  N  N   . THR E  1 137 ? 13.203 -1.025  -30.972  1.00 14.47 ? 137  THR F N   1 
ATOM   5462  C  CA  . THR E  1 137 ? 12.657 -1.886  -32.022  1.00 14.64 ? 137  THR F CA  1 
ATOM   5463  C  C   . THR E  1 137 ? 12.719 -1.275  -33.415  1.00 14.52 ? 137  THR F C   1 
ATOM   5464  O  O   . THR E  1 137 ? 12.298 -1.907  -34.394  1.00 14.81 ? 137  THR F O   1 
ATOM   5465  C  CB  . THR E  1 137 ? 11.175 -2.130  -31.774  1.00 14.59 ? 137  THR F CB  1 
ATOM   5466  O  OG1 . THR E  1 137 ? 10.481 -0.864  -31.875  1.00 13.23 ? 137  THR F OG1 1 
ATOM   5467  C  CG2 . THR E  1 137 ? 10.950 -2.751  -30.386  1.00 15.35 ? 137  THR F CG2 1 
ATOM   5468  N  N   . GLY E  1 138 ? 13.184 -0.034  -33.506  1.00 13.58 ? 138  GLY F N   1 
ATOM   5469  C  CA  . GLY E  1 138 ? 13.124 0.687   -34.753  1.00 12.99 ? 138  GLY F CA  1 
ATOM   5470  C  C   . GLY E  1 138 ? 11.709 0.985   -35.201  1.00 12.42 ? 138  GLY F C   1 
ATOM   5471  O  O   . GLY E  1 138 ? 11.508 1.318   -36.362  1.00 12.59 ? 138  GLY F O   1 
ATOM   5472  N  N   . ASN E  1 139 ? 10.735 0.879   -34.291  1.00 12.69 ? 139  ASN F N   1 
ATOM   5473  C  CA  . ASN E  1 139 ? 9.326  1.133   -34.616  1.00 13.20 ? 139  ASN F CA  1 
ATOM   5474  C  C   . ASN E  1 139 ? 8.779  0.207   -35.713  1.00 12.50 ? 139  ASN F C   1 
ATOM   5475  O  O   . ASN E  1 139 ? 7.943  0.624   -36.530  1.00 12.86 ? 139  ASN F O   1 
ATOM   5476  C  CB  . ASN E  1 139 ? 9.137  2.596   -35.033  1.00 13.39 ? 139  ASN F CB  1 
ATOM   5477  C  CG  . ASN E  1 139 ? 9.266  3.547   -33.861  1.00 14.35 ? 139  ASN F CG  1 
ATOM   5478  O  OD1 . ASN E  1 139 ? 8.487  3.470   -32.903  1.00 14.14 ? 139  ASN F OD1 1 
ATOM   5479  N  ND2 . ASN E  1 139 ? 10.271 4.429   -33.914  1.00 13.26 ? 139  ASN F ND2 1 
ATOM   5480  N  N   . ALA E  1 140 ? 9.262  -1.034  -35.734  1.00 12.24 ? 140  ALA F N   1 
ATOM   5481  C  CA  . ALA E  1 140 ? 8.988  -1.952  -36.862  1.00 12.28 ? 140  ALA F CA  1 
ATOM   5482  C  C   . ALA E  1 140 ? 7.614  -2.615  -36.722  1.00 12.18 ? 140  ALA F C   1 
ATOM   5483  O  O   . ALA E  1 140 ? 7.123  -3.283  -37.641  1.00 12.75 ? 140  ALA F O   1 
ATOM   5484  C  CB  . ALA E  1 140 ? 10.101 -2.993  -36.984  1.00 11.23 ? 140  ALA F CB  1 
ATOM   5485  N  N   . GLY E  1 141 ? 6.996  -2.412  -35.563  1.00 12.92 ? 141  GLY F N   1 
ATOM   5486  C  CA  . GLY E  1 141 ? 5.631  -2.888  -35.331  1.00 13.36 ? 141  GLY F CA  1 
ATOM   5487  C  C   . GLY E  1 141 ? 5.473  -4.367  -35.073  1.00 13.86 ? 141  GLY F C   1 
ATOM   5488  O  O   . GLY E  1 141 ? 6.404  -5.054  -34.593  1.00 13.31 ? 141  GLY F O   1 
ATOM   5489  N  N   . SER E  1 142 ? 4.269  -4.867  -35.366  1.00 13.95 ? 142  SER F N   1 
ATOM   5490  C  CA  . SER E  1 142 ? 3.932  -6.252  -35.062  1.00 14.49 ? 142  SER F CA  1 
ATOM   5491  C  C   . SER E  1 142 ? 4.748  -7.250  -35.915  1.00 13.86 ? 142  SER F C   1 
ATOM   5492  O  O   . SER E  1 142 ? 5.312  -6.890  -36.966  1.00 13.65 ? 142  SER F O   1 
ATOM   5493  C  CB  . SER E  1 142 ? 2.408  -6.476  -35.170  1.00 15.24 ? 142  SER F CB  1 
ATOM   5494  O  OG  . SER E  1 142 ? 1.992  -6.471  -36.521  1.00 18.51 ? 142  SER F OG  1 
ATOM   5495  N  N   . ARG E  1 143 ? 4.818  -8.488  -35.415  1.00 13.64 ? 143  ARG F N   1 
ATOM   5496  C  CA  . ARG E  1 143 ? 5.608  -9.570  -35.987  1.00 13.00 ? 143  ARG F CA  1 
ATOM   5497  C  C   . ARG E  1 143 ? 4.683  -10.413 -36.849  1.00 13.25 ? 143  ARG F C   1 
ATOM   5498  O  O   . ARG E  1 143 ? 3.768  -11.060 -36.327  1.00 13.44 ? 143  ARG F O   1 
ATOM   5499  C  CB  . ARG E  1 143 ? 6.195  -10.436 -34.855  1.00 13.48 ? 143  ARG F CB  1 
ATOM   5500  C  CG  . ARG E  1 143 ? 6.492  -9.646  -33.590  1.00 11.61 ? 143  ARG F CG  1 
ATOM   5501  C  CD  . ARG E  1 143 ? 7.364  -10.381 -32.546  1.00 13.14 ? 143  ARG F CD  1 
ATOM   5502  N  NE  . ARG E  1 143 ? 7.956  -9.403  -31.622  1.00 13.72 ? 143  ARG F NE  1 
ATOM   5503  C  CZ  . ARG E  1 143 ? 8.750  -9.673  -30.586  1.00 12.95 ? 143  ARG F CZ  1 
ATOM   5504  N  NH1 . ARG E  1 143 ? 9.231  -8.665  -29.861  1.00 15.15 ? 143  ARG F NH1 1 
ATOM   5505  N  NH2 . ARG E  1 143 ? 9.079  -10.925 -30.264  1.00 11.26 ? 143  ARG F NH2 1 
ATOM   5506  N  N   . LEU E  1 144 ? 4.915  -10.398 -38.158  1.00 12.35 ? 144  LEU F N   1 
ATOM   5507  C  CA  . LEU E  1 144 ? 4.024  -11.077 -39.097  1.00 12.76 ? 144  LEU F CA  1 
ATOM   5508  C  C   . LEU E  1 144 ? 4.321  -12.556 -39.268  1.00 12.40 ? 144  LEU F C   1 
ATOM   5509  O  O   . LEU E  1 144 ? 3.390  -13.370 -39.443  1.00 11.69 ? 144  LEU F O   1 
ATOM   5510  C  CB  . LEU E  1 144 ? 4.030  -10.373 -40.451  1.00 12.46 ? 144  LEU F CB  1 
ATOM   5511  C  CG  . LEU E  1 144 ? 3.521  -8.915  -40.501  1.00 14.95 ? 144  LEU F CG  1 
ATOM   5512  C  CD1 . LEU E  1 144 ? 3.604  -8.423  -41.938  1.00 15.38 ? 144  LEU F CD1 1 
ATOM   5513  C  CD2 . LEU E  1 144 ? 2.099  -8.729  -39.947  1.00 16.84 ? 144  LEU F CD2 1 
ATOM   5514  N  N   . ALA E  1 145 ? 5.610  -12.902 -39.236  1.00 11.89 ? 145  ALA F N   1 
ATOM   5515  C  CA  . ALA E  1 145 ? 6.028  -14.302 -39.287  1.00 11.48 ? 145  ALA F CA  1 
ATOM   5516  C  C   . ALA E  1 145 ? 7.348  -14.474 -38.558  1.00 11.12 ? 145  ALA F C   1 
ATOM   5517  O  O   . ALA E  1 145 ? 8.140  -13.534 -38.473  1.00 10.60 ? 145  ALA F O   1 
ATOM   5518  C  CB  . ALA E  1 145 ? 6.154  -14.769 -40.731  1.00 12.61 ? 145  ALA F CB  1 
ATOM   5519  N  N   . CYS E  1 146 ? 7.599  -15.680 -38.052  1.00 9.87  ? 146  CYS F N   1 
ATOM   5520  C  CA  . CYS E  1 146 ? 8.845  -15.936 -37.358  1.00 8.94  ? 146  CYS F CA  1 
ATOM   5521  C  C   . CYS E  1 146 ? 9.127  -17.420 -37.369  1.00 9.09  ? 146  CYS F C   1 
ATOM   5522  O  O   . CYS E  1 146 ? 8.317  -18.217 -37.856  1.00 9.79  ? 146  CYS F O   1 
ATOM   5523  C  CB  . CYS E  1 146 ? 8.787  -15.435 -35.920  0.40 8.30  ? 146  CYS F CB  1 
ATOM   5524  S  SG  . CYS E  1 146 ? 7.554  -16.264 -34.944  0.40 4.59  ? 146  CYS F SG  1 
ATOM   5525  N  N   . GLY E  1 147 ? 10.283 -17.786 -36.845  1.00 9.53  ? 147  GLY F N   1 
ATOM   5526  C  CA  . GLY E  1 147 ? 10.627 -19.192 -36.693  1.00 9.74  ? 147  GLY F CA  1 
ATOM   5527  C  C   . GLY E  1 147 ? 11.997 -19.309 -36.092  1.00 9.09  ? 147  GLY F C   1 
ATOM   5528  O  O   . GLY E  1 147 ? 12.761 -18.342 -36.086  1.00 9.88  ? 147  GLY F O   1 
ATOM   5529  N  N   . VAL E  1 148 ? 12.326 -20.498 -35.596  1.00 8.56  ? 148  VAL F N   1 
ATOM   5530  C  CA  . VAL E  1 148 ? 13.631 -20.696 -34.943  1.00 8.78  ? 148  VAL F CA  1 
ATOM   5531  C  C   . VAL E  1 148 ? 14.746 -21.057 -35.923  1.00 9.41  ? 148  VAL F C   1 
ATOM   5532  O  O   . VAL E  1 148 ? 14.560 -21.904 -36.802  1.00 8.66  ? 148  VAL F O   1 
ATOM   5533  C  CB  . VAL E  1 148 ? 13.559 -21.812 -33.868  1.00 8.88  ? 148  VAL F CB  1 
ATOM   5534  C  CG1 . VAL E  1 148 ? 14.884 -21.946 -33.171  1.00 6.83  ? 148  VAL F CG1 1 
ATOM   5535  C  CG2 . VAL E  1 148 ? 12.435 -21.508 -32.842  1.00 11.72 ? 148  VAL F CG2 1 
ATOM   5536  N  N   . ILE E  1 149 ? 15.908 -20.423 -35.763  1.00 9.11  ? 149  ILE F N   1 
ATOM   5537  C  CA  . ILE E  1 149 ? 17.051 -20.654 -36.636  1.00 9.87  ? 149  ILE F CA  1 
ATOM   5538  C  C   . ILE E  1 149 ? 17.735 -21.969 -36.264  1.00 10.13 ? 149  ILE F C   1 
ATOM   5539  O  O   . ILE E  1 149 ? 18.177 -22.149 -35.133  1.00 10.41 ? 149  ILE F O   1 
ATOM   5540  C  CB  . ILE E  1 149 ? 18.051 -19.456 -36.586  1.00 9.17  ? 149  ILE F CB  1 
ATOM   5541  C  CG1 . ILE E  1 149 ? 17.297 -18.171 -36.966  1.00 10.45 ? 149  ILE F CG1 1 
ATOM   5542  C  CG2 . ILE E  1 149 ? 19.250 -19.730 -37.516  1.00 10.64 ? 149  ILE F CG2 1 
ATOM   5543  C  CD1 . ILE E  1 149 ? 18.006 -16.845 -36.568  1.00 7.63  ? 149  ILE F CD1 1 
ATOM   5544  N  N   . GLY E  1 150 ? 17.793 -22.890 -37.222  1.00 10.63 ? 150  GLY F N   1 
ATOM   5545  C  CA  . GLY E  1 150 ? 18.378 -24.204 -36.968  1.00 11.08 ? 150  GLY F CA  1 
ATOM   5546  C  C   . GLY E  1 150 ? 19.622 -24.445 -37.778  1.00 11.79 ? 150  GLY F C   1 
ATOM   5547  O  O   . GLY E  1 150 ? 19.805 -23.878 -38.859  1.00 11.64 ? 150  GLY F O   1 
ATOM   5548  N  N   . ILE E  1 151 ? 20.478 -25.323 -37.284  1.00 12.27 ? 151  ILE F N   1 
ATOM   5549  C  CA  . ILE E  1 151 ? 21.635 -25.726 -38.058  1.00 12.83 ? 151  ILE F CA  1 
ATOM   5550  C  C   . ILE E  1 151 ? 21.197 -26.592 -39.263  1.00 13.24 ? 151  ILE F C   1 
ATOM   5551  O  O   . ILE E  1 151 ? 20.299 -27.441 -39.165  1.00 12.97 ? 151  ILE F O   1 
ATOM   5552  C  CB  . ILE E  1 151 ? 22.687 -26.432 -37.157  1.00 12.64 ? 151  ILE F CB  1 
ATOM   5553  C  CG1 . ILE E  1 151 ? 23.901 -26.914 -37.985  1.00 13.08 ? 151  ILE F CG1 1 
ATOM   5554  C  CG2 . ILE E  1 151 ? 22.046 -27.560 -36.419  1.00 14.84 ? 151  ILE F CG2 1 
ATOM   5555  C  CD1 . ILE E  1 151 ? 25.246 -26.917 -37.264  1.00 12.15 ? 151  ILE F CD1 1 
ATOM   5556  N  N   . ALA E  1 152 ? 21.801 -26.321 -40.404  1.00 13.96 ? 152  ALA F N   1 
ATOM   5557  C  CA  . ALA E  1 152 ? 21.448 -27.009 -41.638  1.00 14.60 ? 152  ALA F CA  1 
ATOM   5558  C  C   . ALA E  1 152 ? 22.635 -27.749 -42.226  1.00 15.57 ? 152  ALA F C   1 
ATOM   5559  O  O   . ALA E  1 152 ? 23.787 -27.502 -41.845  1.00 15.17 ? 152  ALA F O   1 
ATOM   5560  C  CB  . ALA E  1 152 ? 20.884 -26.024 -42.638  1.00 14.57 ? 152  ALA F CB  1 
ATOM   5561  N  N   . GLN E  1 153 ? 22.353 -28.668 -43.157  1.00 17.38 ? 153  GLN F N   1 
ATOM   5562  C  CA  . GLN E  1 153 ? 23.401 -29.496 -43.750  1.00 19.53 ? 153  GLN F CA  1 
ATOM   5563  C  C   . GLN E  1 153 ? 24.144 -28.747 -44.830  1.00 20.15 ? 153  GLN F C   1 
ATOM   5564  O  O   . GLN E  1 153 ? 23.536 -28.147 -45.723  1.00 20.73 ? 153  GLN F O   1 
ATOM   5565  C  CB  . GLN E  1 153 ? 22.840 -30.795 -44.345  1.00 19.69 ? 153  GLN F CB  1 
ATOM   5566  C  CG  . GLN E  1 153 ? 23.935 -31.745 -44.820  1.00 22.40 ? 153  GLN F CG  1 
ATOM   5567  C  CD  . GLN E  1 153 ? 23.446 -33.154 -45.038  1.00 25.05 ? 153  GLN F CD  1 
ATOM   5568  O  OE1 . GLN E  1 153 ? 22.401 -33.377 -45.643  1.00 27.56 ? 153  GLN F OE1 1 
ATOM   5569  N  NE2 . GLN E  1 153 ? 24.214 -34.123 -44.550  1.00 27.60 ? 153  GLN F NE2 1 
ATOM   5570  O  OXT . GLN E  1 153 ? 25.370 -28.781 -44.810  1.00 21.31 ? 153  GLN F OXT 1 
ATOM   5571  N  N   . ALA F  1 1   ? 23.502 -21.754 -15.905  1.00 25.73 ? 1    ALA G N   1 
ATOM   5572  C  CA  . ALA F  1 1   ? 22.102 -22.244 -16.106  1.00 24.58 ? 1    ALA G CA  1 
ATOM   5573  C  C   . ALA F  1 1   ? 21.600 -21.869 -17.498  1.00 24.14 ? 1    ALA G C   1 
ATOM   5574  O  O   . ALA F  1 1   ? 21.614 -20.688 -17.880  1.00 23.71 ? 1    ALA G O   1 
ATOM   5575  C  CB  . ALA F  1 1   ? 21.169 -21.692 -15.014  1.00 24.72 ? 1    ALA G CB  1 
ATOM   5576  N  N   . THR F  1 2   ? 21.177 -22.891 -18.246  1.00 23.32 ? 2    THR G N   1 
ATOM   5577  C  CA  . THR F  1 2   ? 20.677 -22.754 -19.620  1.00 22.51 ? 2    THR G CA  1 
ATOM   5578  C  C   . THR F  1 2   ? 19.298 -23.418 -19.713  1.00 21.25 ? 2    THR G C   1 
ATOM   5579  O  O   . THR F  1 2   ? 19.072 -24.474 -19.132  1.00 20.85 ? 2    THR G O   1 
ATOM   5580  C  CB  . THR F  1 2   ? 21.634 -23.430 -20.642  1.00 22.79 ? 2    THR G CB  1 
ATOM   5581  O  OG1 . THR F  1 2   ? 22.978 -22.993 -20.419  1.00 24.88 ? 2    THR G OG1 1 
ATOM   5582  C  CG2 . THR F  1 2   ? 21.244 -23.097 -22.094  1.00 22.51 ? 2    THR G CG2 1 
ATOM   5583  N  N   . LYS F  1 3   ? 18.380 -22.766 -20.419  1.00 20.39 ? 3    LYS G N   1 
ATOM   5584  C  CA  . LYS F  1 3   ? 17.066 -23.331 -20.722  1.00 20.00 ? 3    LYS G CA  1 
ATOM   5585  C  C   . LYS F  1 3   ? 16.849 -23.381 -22.237  1.00 19.34 ? 3    LYS G C   1 
ATOM   5586  O  O   . LYS F  1 3   ? 17.292 -22.496 -22.977  1.00 19.03 ? 3    LYS G O   1 
ATOM   5587  C  CB  . LYS F  1 3   ? 15.942 -22.522 -20.050  1.00 20.42 ? 3    LYS G CB  1 
ATOM   5588  C  CG  . LYS F  1 3   ? 15.820 -22.694 -18.535  1.00 23.33 ? 3    LYS G CG  1 
ATOM   5589  C  CD  . LYS F  1 3   ? 14.848 -21.664 -17.900  1.00 26.14 ? 3    LYS G CD  1 
ATOM   5590  C  CE  . LYS F  1 3   ? 13.369 -21.930 -18.249  1.00 28.41 ? 3    LYS G CE  1 
ATOM   5591  N  NZ  . LYS F  1 3   ? 12.841 -23.249 -17.754  1.00 28.30 ? 3    LYS G NZ  1 
ATOM   5592  N  N   . ALA F  1 4   ? 16.190 -24.443 -22.699  1.00 18.20 ? 4    ALA G N   1 
ATOM   5593  C  CA  . ALA F  1 4   ? 15.782 -24.548 -24.098  1.00 17.09 ? 4    ALA G CA  1 
ATOM   5594  C  C   . ALA F  1 4   ? 14.344 -25.015 -24.173  1.00 16.83 ? 4    ALA G C   1 
ATOM   5595  O  O   . ALA F  1 4   ? 13.811 -25.600 -23.214  1.00 17.02 ? 4    ALA G O   1 
ATOM   5596  C  CB  . ALA F  1 4   ? 16.697 -25.475 -24.876  1.00 16.54 ? 4    ALA G CB  1 
ATOM   5597  N  N   . VAL F  1 5   ? 13.696 -24.716 -25.286  1.00 15.86 ? 5    VAL G N   1 
ATOM   5598  C  CA  . VAL F  1 5   ? 12.316 -25.107 -25.472  1.00 15.44 ? 5    VAL G CA  1 
ATOM   5599  C  C   . VAL F  1 5   ? 12.103 -25.571 -26.916  1.00 15.60 ? 5    VAL G C   1 
ATOM   5600  O  O   . VAL F  1 5   ? 12.769 -25.089 -27.844  1.00 14.41 ? 5    VAL G O   1 
ATOM   5601  C  CB  . VAL F  1 5   ? 11.335 -23.955 -25.086  1.00 15.38 ? 5    VAL G CB  1 
ATOM   5602  C  CG1 . VAL F  1 5   ? 11.446 -22.809 -26.072  1.00 14.94 ? 5    VAL G CG1 1 
ATOM   5603  C  CG2 . VAL F  1 5   ? 9.887  -24.466 -25.000  1.00 14.79 ? 5    VAL G CG2 1 
ATOM   5604  N  N   . CYS F  1 6   ? 11.168 -26.503 -27.079  1.00 15.78 ? 6    CYS G N   1 
ATOM   5605  C  CA  . CYS F  1 6   ? 10.841 -27.051 -28.382  1.00 16.59 ? 6    CYS G CA  1 
ATOM   5606  C  C   . CYS F  1 6   ? 9.329  -27.188 -28.554  1.00 16.84 ? 6    CYS G C   1 
ATOM   5607  O  O   . CYS F  1 6   ? 8.667  -27.844 -27.745  1.00 16.49 ? 6    CYS G O   1 
ATOM   5608  C  CB  . CYS F  1 6   ? 11.500 -28.420 -28.539  1.00 16.53 ? 6    CYS G CB  1 
ATOM   5609  S  SG  . CYS F  1 6   ? 11.286 -29.090 -30.185  1.00 20.09 ? 6    CYS G SG  1 
ATOM   5610  N  N   . VAL F  1 7   ? 8.789  -26.545 -29.588  1.00 17.55 ? 7    VAL G N   1 
ATOM   5611  C  CA  . VAL F  1 7   ? 7.401  -26.744 -29.983  1.00 18.75 ? 7    VAL G CA  1 
ATOM   5612  C  C   . VAL F  1 7   ? 7.344  -27.879 -31.016  1.00 20.09 ? 7    VAL G C   1 
ATOM   5613  O  O   . VAL F  1 7   ? 7.923  -27.785 -32.105  1.00 19.33 ? 7    VAL G O   1 
ATOM   5614  C  CB  . VAL F  1 7   ? 6.764  -25.467 -30.571  1.00 19.08 ? 7    VAL G CB  1 
ATOM   5615  C  CG1 . VAL F  1 7   ? 5.275  -25.688 -30.866  1.00 18.30 ? 7    VAL G CG1 1 
ATOM   5616  C  CG2 . VAL F  1 7   ? 6.965  -24.266 -29.626  1.00 19.51 ? 7    VAL G CG2 1 
ATOM   5617  N  N   . LEU F  1 8   ? 6.650  -28.958 -30.665  1.00 21.36 ? 8    LEU G N   1 
ATOM   5618  C  CA  . LEU F  1 8   ? 6.550  -30.113 -31.566  1.00 22.89 ? 8    LEU G CA  1 
ATOM   5619  C  C   . LEU F  1 8   ? 5.230  -30.063 -32.315  1.00 24.01 ? 8    LEU G C   1 
ATOM   5620  O  O   . LEU F  1 8   ? 4.156  -30.014 -31.701  1.00 24.02 ? 8    LEU G O   1 
ATOM   5621  C  CB  . LEU F  1 8   ? 6.680  -31.425 -30.795  1.00 22.86 ? 8    LEU G CB  1 
ATOM   5622  C  CG  . LEU F  1 8   ? 8.042  -31.809 -30.219  1.00 23.83 ? 8    LEU G CG  1 
ATOM   5623  C  CD1 . LEU F  1 8   ? 8.520  -30.775 -29.233  1.00 26.50 ? 8    LEU G CD1 1 
ATOM   5624  C  CD2 . LEU F  1 8   ? 7.936  -33.147 -29.518  1.00 25.68 ? 8    LEU G CD2 1 
ATOM   5625  N  N   . LYS F  1 9   ? 5.321  -30.045 -33.642  1.00 25.21 ? 9    LYS G N   1 
ATOM   5626  C  CA  . LYS F  1 9   ? 4.152  -30.015 -34.515  1.00 26.76 ? 9    LYS G CA  1 
ATOM   5627  C  C   . LYS F  1 9   ? 4.413  -30.967 -35.675  1.00 27.44 ? 9    LYS G C   1 
ATOM   5628  O  O   . LYS F  1 9   ? 5.573  -31.168 -36.063  1.00 27.40 ? 9    LYS G O   1 
ATOM   5629  C  CB  . LYS F  1 9   ? 3.896  -28.596 -35.039  1.00 27.04 ? 9    LYS G CB  1 
ATOM   5630  C  CG  . LYS F  1 9   ? 3.592  -27.543 -33.941  1.00 29.63 ? 9    LYS G CG  1 
ATOM   5631  C  CD  . LYS F  1 9   ? 3.626  -26.093 -34.465  1.00 33.42 ? 9    LYS G CD  1 
ATOM   5632  C  CE  . LYS F  1 9   ? 2.320  -25.688 -35.167  1.00 34.85 ? 9    LYS G CE  1 
ATOM   5633  N  NZ  . LYS F  1 9   ? 1.145  -25.749 -34.226  1.00 35.93 ? 9    LYS G NZ  1 
ATOM   5634  N  N   . GLY F  1 10  ? 3.347  -31.566 -36.208  1.00 28.05 ? 10   GLY G N   1 
ATOM   5635  C  CA  . GLY F  1 10  ? 3.459  -32.451 -37.371  1.00 29.04 ? 10   GLY G CA  1 
ATOM   5636  C  C   . GLY F  1 10  ? 2.353  -32.242 -38.390  1.00 29.94 ? 10   GLY G C   1 
ATOM   5637  O  O   . GLY F  1 10  ? 1.670  -31.220 -38.365  1.00 29.81 ? 10   GLY G O   1 
ATOM   5638  N  N   . ASP F  1 11  ? 2.176  -33.217 -39.281  1.00 30.82 ? 11   ASP G N   1 
ATOM   5639  C  CA  . ASP F  1 11  ? 1.109  -33.169 -40.288  1.00 31.83 ? 11   ASP G CA  1 
ATOM   5640  C  C   . ASP F  1 11  ? -0.238 -33.609 -39.726  1.00 31.63 ? 11   ASP G C   1 
ATOM   5641  O  O   . ASP F  1 11  ? -1.285 -33.344 -40.330  1.00 31.92 ? 11   ASP G O   1 
ATOM   5642  C  CB  . ASP F  1 11  ? 1.448  -34.064 -41.479  1.00 32.40 ? 11   ASP G CB  1 
ATOM   5643  C  CG  . ASP F  1 11  ? 2.525  -33.485 -42.368  1.00 34.37 ? 11   ASP G CG  1 
ATOM   5644  O  OD1 . ASP F  1 11  ? 3.033  -34.253 -43.218  1.00 37.58 ? 11   ASP G OD1 1 
ATOM   5645  O  OD2 . ASP F  1 11  ? 2.862  -32.282 -42.234  1.00 35.75 ? 11   ASP G OD2 1 
ATOM   5646  N  N   . GLY F  1 12  ? -0.206 -34.293 -38.584  1.00 31.39 ? 12   GLY G N   1 
ATOM   5647  C  CA  . GLY F  1 12  ? -1.415 -34.872 -37.993  1.00 30.85 ? 12   GLY G CA  1 
ATOM   5648  C  C   . GLY F  1 12  ? -1.775 -34.239 -36.662  1.00 30.44 ? 12   GLY G C   1 
ATOM   5649  O  O   . GLY F  1 12  ? -1.563 -33.040 -36.476  1.00 30.38 ? 12   GLY G O   1 
ATOM   5650  N  N   . PRO F  1 13  ? -2.333 -35.039 -35.727  1.00 29.98 ? 13   PRO G N   1 
ATOM   5651  C  CA  . PRO F  1 13  ? -2.814 -34.526 -34.435  1.00 29.52 ? 13   PRO G CA  1 
ATOM   5652  C  C   . PRO F  1 13  ? -1.736 -34.351 -33.360  1.00 29.07 ? 13   PRO G C   1 
ATOM   5653  O  O   . PRO F  1 13  ? -1.974 -33.649 -32.377  1.00 29.09 ? 13   PRO G O   1 
ATOM   5654  C  CB  . PRO F  1 13  ? -3.804 -35.608 -33.994  1.00 29.63 ? 13   PRO G CB  1 
ATOM   5655  C  CG  . PRO F  1 13  ? -3.239 -36.852 -34.564  1.00 29.81 ? 13   PRO G CG  1 
ATOM   5656  C  CD  . PRO F  1 13  ? -2.713 -36.453 -35.917  1.00 30.05 ? 13   PRO G CD  1 
ATOM   5657  N  N   . VAL F  1 14  ? -0.580 -34.991 -33.545  1.00 28.41 ? 14   VAL G N   1 
ATOM   5658  C  CA  . VAL F  1 14  ? 0.486  -35.003 -32.541  1.00 27.73 ? 14   VAL G CA  1 
ATOM   5659  C  C   . VAL F  1 14  ? 1.114  -33.611 -32.403  1.00 27.70 ? 14   VAL G C   1 
ATOM   5660  O  O   . VAL F  1 14  ? 1.663  -33.071 -33.362  1.00 27.34 ? 14   VAL G O   1 
ATOM   5661  C  CB  . VAL F  1 14  ? 1.576  -36.076 -32.873  1.00 27.77 ? 14   VAL G CB  1 
ATOM   5662  C  CG1 . VAL F  1 14  ? 2.638  -36.159 -31.783  1.00 26.65 ? 14   VAL G CG1 1 
ATOM   5663  C  CG2 . VAL F  1 14  ? 0.934  -37.448 -33.080  1.00 27.64 ? 14   VAL G CG2 1 
ATOM   5664  N  N   . GLN F  1 15  ? 0.994  -33.038 -31.208  1.00 27.75 ? 15   GLN G N   1 
ATOM   5665  C  CA  . GLN F  1 15  ? 1.599  -31.743 -30.879  1.00 28.11 ? 15   GLN G CA  1 
ATOM   5666  C  C   . GLN F  1 15  ? 2.001  -31.672 -29.415  1.00 27.37 ? 15   GLN G C   1 
ATOM   5667  O  O   . GLN F  1 15  ? 1.387  -32.314 -28.566  1.00 27.48 ? 15   GLN G O   1 
ATOM   5668  C  CB  . GLN F  1 15  ? 0.678  -30.570 -31.263  1.00 28.53 ? 15   GLN G CB  1 
ATOM   5669  C  CG  . GLN F  1 15  ? -0.562 -30.361 -30.369  1.00 30.77 ? 15   GLN G CG  1 
ATOM   5670  C  CD  . GLN F  1 15  ? -1.646 -29.535 -31.060  1.00 32.91 ? 15   GLN G CD  1 
ATOM   5671  O  OE1 . GLN F  1 15  ? -2.812 -29.554 -30.657  1.00 34.92 ? 15   GLN G OE1 1 
ATOM   5672  N  NE2 . GLN F  1 15  ? -1.267 -28.819 -32.114  1.00 33.90 ? 15   GLN G NE2 1 
ATOM   5673  N  N   . GLY F  1 16  ? 3.041  -30.893 -29.123  1.00 26.71 ? 16   GLY G N   1 
ATOM   5674  C  CA  . GLY F  1 16  ? 3.496  -30.746 -27.750  1.00 25.87 ? 16   GLY G CA  1 
ATOM   5675  C  C   . GLY F  1 16  ? 4.496  -29.632 -27.537  1.00 25.02 ? 16   GLY G C   1 
ATOM   5676  O  O   . GLY F  1 16  ? 4.909  -28.970 -28.485  1.00 24.96 ? 16   GLY G O   1 
ATOM   5677  N  N   . ILE F  1 17  ? 4.852  -29.428 -26.272  1.00 24.49 ? 17   ILE G N   1 
ATOM   5678  C  CA  . ILE F  1 17  ? 5.899  -28.489 -25.854  1.00 23.43 ? 17   ILE G CA  1 
ATOM   5679  C  C   . ILE F  1 17  ? 6.835  -29.244 -24.921  1.00 23.10 ? 17   ILE G C   1 
ATOM   5680  O  O   . ILE F  1 17  ? 6.384  -29.826 -23.933  1.00 23.24 ? 17   ILE G O   1 
ATOM   5681  C  CB  . ILE F  1 17  ? 5.320  -27.248 -25.104  1.00 23.69 ? 17   ILE G CB  1 
ATOM   5682  C  CG1 . ILE F  1 17  ? 4.421  -26.411 -26.031  1.00 23.84 ? 17   ILE G CG1 1 
ATOM   5683  C  CG2 . ILE F  1 17  ? 6.455  -26.394 -24.506  1.00 22.33 ? 17   ILE G CG2 1 
ATOM   5684  C  CD1 . ILE F  1 17  ? 3.499  -25.420 -25.325  1.00 24.18 ? 17   ILE G CD1 1 
ATOM   5685  N  N   . ILE F  1 18  ? 8.130  -29.234 -25.234  1.00 21.77 ? 18   ILE G N   1 
ATOM   5686  C  CA  . ILE F  1 18  ? 9.139  -29.878 -24.393  1.00 20.59 ? 18   ILE G CA  1 
ATOM   5687  C  C   . ILE F  1 18  ? 10.157 -28.855 -23.891  1.00 20.53 ? 18   ILE G C   1 
ATOM   5688  O  O   . ILE F  1 18  ? 10.649 -28.019 -24.656  1.00 20.07 ? 18   ILE G O   1 
ATOM   5689  C  CB  . ILE F  1 18  ? 9.870  -31.016 -25.142  1.00 20.39 ? 18   ILE G CB  1 
ATOM   5690  C  CG1 . ILE F  1 18  ? 8.892  -32.142 -25.539  1.00 20.51 ? 18   ILE G CG1 1 
ATOM   5691  C  CG2 . ILE F  1 18  ? 11.040 -31.538 -24.314  1.00 20.24 ? 18   ILE G CG2 1 
ATOM   5692  C  CD1 . ILE F  1 18  ? 8.409  -33.014 -24.383  1.00 20.75 ? 18   ILE G CD1 1 
ATOM   5693  N  N   . ASN F  1 19  ? 10.456 -28.935 -22.599  1.00 20.08 ? 19   ASN G N   1 
ATOM   5694  C  CA  . ASN F  1 19  ? 11.409 -28.039 -21.956  1.00 19.83 ? 19   ASN G CA  1 
ATOM   5695  C  C   . ASN F  1 19  ? 12.710 -28.765 -21.656  1.00 19.24 ? 19   ASN G C   1 
ATOM   5696  O  O   . ASN F  1 19  ? 12.711 -29.972 -21.422  1.00 18.93 ? 19   ASN G O   1 
ATOM   5697  C  CB  . ASN F  1 19  ? 10.795 -27.454 -20.674  1.00 19.51 ? 19   ASN G CB  1 
ATOM   5698  C  CG  . ASN F  1 19  ? 9.486  -26.704 -20.951  1.00 20.94 ? 19   ASN G CG  1 
ATOM   5699  O  OD1 . ASN F  1 19  ? 9.489  -25.628 -21.548  1.00 18.74 ? 19   ASN G OD1 1 
ATOM   5700  N  ND2 . ASN F  1 19  ? 8.360  -27.290 -20.537  1.00 22.26 ? 19   ASN G ND2 1 
ATOM   5701  N  N   . PHE F  1 20  ? 13.809 -28.013 -21.713  1.00 18.73 ? 20   PHE G N   1 
ATOM   5702  C  CA  . PHE F  1 20  ? 15.140 -28.484 -21.386  1.00 18.37 ? 20   PHE G CA  1 
ATOM   5703  C  C   . PHE F  1 20  ? 15.718 -27.493 -20.385  1.00 19.04 ? 20   PHE G C   1 
ATOM   5704  O  O   . PHE F  1 20  ? 15.588 -26.272 -20.554  1.00 19.31 ? 20   PHE G O   1 
ATOM   5705  C  CB  . PHE F  1 20  ? 16.055 -28.470 -22.612  1.00 18.00 ? 20   PHE G CB  1 
ATOM   5706  C  CG  . PHE F  1 20  ? 15.589 -29.330 -23.751  1.00 17.30 ? 20   PHE G CG  1 
ATOM   5707  C  CD1 . PHE F  1 20  ? 16.185 -30.573 -23.978  1.00 16.40 ? 20   PHE G CD1 1 
ATOM   5708  C  CD2 . PHE F  1 20  ? 14.564 -28.900 -24.610  1.00 16.95 ? 20   PHE G CD2 1 
ATOM   5709  C  CE1 . PHE F  1 20  ? 15.765 -31.377 -25.038  1.00 15.77 ? 20   PHE G CE1 1 
ATOM   5710  C  CE2 . PHE F  1 20  ? 14.127 -29.706 -25.682  1.00 15.86 ? 20   PHE G CE2 1 
ATOM   5711  C  CZ  . PHE F  1 20  ? 14.727 -30.939 -25.893  1.00 16.98 ? 20   PHE G CZ  1 
ATOM   5712  N  N   . GLU F  1 21  ? 16.379 -28.014 -19.359  1.00 19.66 ? 21   GLU G N   1 
ATOM   5713  C  CA  . GLU F  1 21  ? 17.051 -27.167 -18.372  1.00 20.15 ? 21   GLU G CA  1 
ATOM   5714  C  C   . GLU F  1 21  ? 18.320 -27.839 -17.853  1.00 20.00 ? 21   GLU G C   1 
ATOM   5715  O  O   . GLU F  1 21  ? 18.331 -29.020 -17.541  1.00 19.97 ? 21   GLU G O   1 
ATOM   5716  C  CB  . GLU F  1 21  ? 16.101 -26.806 -17.228  1.00 21.07 ? 21   GLU G CB  1 
ATOM   5717  C  CG  . GLU F  1 21  ? 16.648 -25.738 -16.290  1.00 22.68 ? 21   GLU G CG  1 
ATOM   5718  C  CD  . GLU F  1 21  ? 15.574 -24.892 -15.618  1.00 25.90 ? 21   GLU G CD  1 
ATOM   5719  O  OE1 . GLU F  1 21  ? 14.363 -25.087 -15.869  1.00 26.56 ? 21   GLU G OE1 1 
ATOM   5720  O  OE2 . GLU F  1 21  ? 15.963 -24.011 -14.824  1.00 29.29 ? 21   GLU G OE2 1 
ATOM   5721  N  N   . GLN F  1 22  ? 19.400 -27.079 -17.798  1.00 19.36 ? 22   GLN G N   1 
ATOM   5722  C  CA  . GLN F  1 22  ? 20.666 -27.597 -17.349  1.00 19.33 ? 22   GLN G CA  1 
ATOM   5723  C  C   . GLN F  1 22  ? 21.254 -26.565 -16.393  1.00 20.12 ? 22   GLN G C   1 
ATOM   5724  O  O   . GLN F  1 22  ? 21.519 -25.428 -16.796  1.00 19.29 ? 22   GLN G O   1 
ATOM   5725  C  CB  . GLN F  1 22  ? 21.578 -27.797 -18.548  1.00 19.50 ? 22   GLN G CB  1 
ATOM   5726  C  CG  . GLN F  1 22  ? 22.855 -28.586 -18.268  1.00 18.64 ? 22   GLN G CG  1 
ATOM   5727  C  CD  . GLN F  1 22  ? 23.723 -28.686 -19.513  1.00 19.78 ? 22   GLN G CD  1 
ATOM   5728  O  OE1 . GLN F  1 22  ? 23.508 -27.956 -20.491  1.00 20.84 ? 22   GLN G OE1 1 
ATOM   5729  N  NE2 . GLN F  1 22  ? 24.690 -29.593 -19.498  1.00 17.43 ? 22   GLN G NE2 1 
ATOM   5730  N  N   . LYS F  1 23  ? 21.435 -26.964 -15.134  1.00 20.91 ? 23   LYS G N   1 
ATOM   5731  C  CA  . LYS F  1 23  ? 21.902 -26.055 -14.085  1.00 21.99 ? 23   LYS G CA  1 
ATOM   5732  C  C   . LYS F  1 23  ? 23.339 -25.614 -14.342  1.00 22.41 ? 23   LYS G C   1 
ATOM   5733  O  O   . LYS F  1 23  ? 23.669 -24.431 -14.245  1.00 21.83 ? 23   LYS G O   1 
ATOM   5734  C  CB  . LYS F  1 23  ? 21.855 -26.735 -12.719  1.00 22.23 ? 23   LYS G CB  1 
ATOM   5735  C  CG  . LYS F  1 23  ? 20.473 -27.090 -12.196  1.00 24.41 ? 23   LYS G CG  1 
ATOM   5736  C  CD  . LYS F  1 23  ? 20.562 -27.485 -10.711  1.00 26.61 ? 23   LYS G CD  1 
ATOM   5737  C  CE  . LYS F  1 23  ? 19.184 -27.700 -10.129  1.00 28.24 ? 23   LYS G CE  1 
ATOM   5738  N  NZ  . LYS F  1 23  ? 18.569 -28.898 -10.720  1.00 28.27 ? 23   LYS G NZ  1 
ATOM   5739  N  N   . GLU F  1 24  ? 24.185 -26.591 -14.655  1.00 22.64 ? 24   GLU G N   1 
ATOM   5740  C  CA  . GLU F  1 24  ? 25.616 -26.381 -14.827  1.00 23.19 ? 24   GLU G CA  1 
ATOM   5741  C  C   . GLU F  1 24  ? 25.971 -26.817 -16.246  1.00 22.59 ? 24   GLU G C   1 
ATOM   5742  O  O   . GLU F  1 24  ? 25.322 -27.713 -16.772  1.00 22.65 ? 24   GLU G O   1 
ATOM   5743  C  CB  . GLU F  1 24  ? 26.382 -27.269 -13.838  1.00 23.58 ? 24   GLU G CB  1 
ATOM   5744  C  CG  . GLU F  1 24  ? 26.035 -27.044 -12.343  1.00 26.57 ? 24   GLU G CG  1 
ATOM   5745  C  CD  . GLU F  1 24  ? 26.570 -25.718 -11.801  1.00 30.66 ? 24   GLU G CD  1 
ATOM   5746  O  OE1 . GLU F  1 24  ? 27.492 -25.139 -12.430  1.00 31.88 ? 24   GLU G OE1 1 
ATOM   5747  O  OE2 . GLU F  1 24  ? 26.072 -25.254 -10.743  1.00 31.50 ? 24   GLU G OE2 1 
ATOM   5748  N  N   . SER F  1 25  ? 27.005 -26.220 -16.846  1.00 21.95 ? 25   SER G N   1 
ATOM   5749  C  CA  . SER F  1 25  ? 27.483 -26.644 -18.181  1.00 21.79 ? 25   SER G CA  1 
ATOM   5750  C  C   . SER F  1 25  ? 28.023 -28.083 -18.174  1.00 21.67 ? 25   SER G C   1 
ATOM   5751  O  O   . SER F  1 25  ? 27.974 -28.785 -19.191  1.00 21.39 ? 25   SER G O   1 
ATOM   5752  C  CB  . SER F  1 25  ? 28.545 -25.682 -18.742  1.00 21.60 ? 25   SER G CB  1 
ATOM   5753  O  OG  . SER F  1 25  ? 29.774 -25.796 -18.033  1.00 22.61 ? 25   SER G OG  1 
ATOM   5754  N  N   . ASN F  1 26  ? 28.528 -28.521 -17.025  1.00 21.71 ? 26   ASN G N   1 
ATOM   5755  C  CA  . ASN F  1 26  ? 29.042 -29.876 -16.910  1.00 21.37 ? 26   ASN G CA  1 
ATOM   5756  C  C   . ASN F  1 26  ? 28.107 -30.830 -16.159  1.00 21.72 ? 26   ASN G C   1 
ATOM   5757  O  O   . ASN F  1 26  ? 28.527 -31.904 -15.723  1.00 22.28 ? 26   ASN G O   1 
ATOM   5758  C  CB  . ASN F  1 26  ? 30.432 -29.864 -16.292  1.00 21.18 ? 26   ASN G CB  1 
ATOM   5759  C  CG  . ASN F  1 26  ? 30.412 -29.481 -14.832  1.00 20.44 ? 26   ASN G CG  1 
ATOM   5760  O  OD1 . ASN F  1 26  ? 29.539 -28.729 -14.383  1.00 19.00 ? 26   ASN G OD1 1 
ATOM   5761  N  ND2 . ASN F  1 26  ? 31.373 -30.002 -14.076  1.00 18.86 ? 26   ASN G ND2 1 
ATOM   5762  N  N   . GLY F  1 27  ? 26.849 -30.417 -16.005  1.00 21.58 ? 27   GLY G N   1 
ATOM   5763  C  CA  . GLY F  1 27  ? 25.832 -31.213 -15.322  1.00 21.35 ? 27   GLY G CA  1 
ATOM   5764  C  C   . GLY F  1 27  ? 24.811 -31.818 -16.286  1.00 21.01 ? 27   GLY G C   1 
ATOM   5765  O  O   . GLY F  1 27  ? 24.920 -31.649 -17.503  1.00 20.73 ? 27   GLY G O   1 
ATOM   5766  N  N   . PRO F  1 28  ? 23.800 -32.512 -15.739  1.00 20.68 ? 28   PRO G N   1 
ATOM   5767  C  CA  . PRO F  1 28  ? 22.816 -33.205 -16.572  1.00 20.28 ? 28   PRO G CA  1 
ATOM   5768  C  C   . PRO F  1 28  ? 21.674 -32.307 -17.058  1.00 20.09 ? 28   PRO G C   1 
ATOM   5769  O  O   . PRO F  1 28  ? 21.439 -31.221 -16.522  1.00 19.71 ? 28   PRO G O   1 
ATOM   5770  C  CB  . PRO F  1 28  ? 22.309 -34.327 -15.653  1.00 20.25 ? 28   PRO G CB  1 
ATOM   5771  C  CG  . PRO F  1 28  ? 22.592 -33.866 -14.254  1.00 20.11 ? 28   PRO G CG  1 
ATOM   5772  C  CD  . PRO F  1 28  ? 23.566 -32.726 -14.296  1.00 20.34 ? 28   PRO G CD  1 
ATOM   5773  N  N   . VAL F  1 29  ? 20.975 -32.757 -18.093  1.00 19.93 ? 29   VAL G N   1 
ATOM   5774  C  CA  . VAL F  1 29  ? 19.888 -31.961 -18.661  1.00 20.00 ? 29   VAL G CA  1 
ATOM   5775  C  C   . VAL F  1 29  ? 18.538 -32.576 -18.282  1.00 20.45 ? 29   VAL G C   1 
ATOM   5776  O  O   . VAL F  1 29  ? 18.323 -33.782 -18.428  1.00 20.33 ? 29   VAL G O   1 
ATOM   5777  C  CB  . VAL F  1 29  ? 20.017 -31.810 -20.199  1.00 19.67 ? 29   VAL G CB  1 
ATOM   5778  C  CG1 . VAL F  1 29  ? 18.851 -30.984 -20.758  1.00 18.68 ? 29   VAL G CG1 1 
ATOM   5779  C  CG2 . VAL F  1 29  ? 21.351 -31.158 -20.587  1.00 19.14 ? 29   VAL G CG2 1 
ATOM   5780  N  N   . LYS F  1 30  ? 17.640 -31.746 -17.768  1.00 21.31 ? 30   LYS G N   1 
ATOM   5781  C  CA  . LYS F  1 30  ? 16.307 -32.201 -17.412  1.00 21.79 ? 30   LYS G CA  1 
ATOM   5782  C  C   . LYS F  1 30  ? 15.383 -31.880 -18.572  1.00 22.03 ? 30   LYS G C   1 
ATOM   5783  O  O   . LYS F  1 30  ? 15.278 -30.717 -19.006  1.00 21.36 ? 30   LYS G O   1 
ATOM   5784  C  CB  . LYS F  1 30  ? 15.820 -31.561 -16.099  1.00 21.99 ? 30   LYS G CB  1 
ATOM   5785  C  CG  . LYS F  1 30  ? 14.379 -31.930 -15.656  1.00 25.52 ? 30   LYS G CG  1 
ATOM   5786  C  CD  . LYS F  1 30  ? 14.058 -33.435 -15.783  1.00 27.71 ? 30   LYS G CD  1 
ATOM   5787  C  CE  . LYS F  1 30  ? 12.627 -33.789 -15.365  1.00 28.35 ? 30   LYS G CE  1 
ATOM   5788  N  NZ  . LYS F  1 30  ? 12.575 -34.421 -13.995  1.00 31.03 ? 30   LYS G NZ  1 
ATOM   5789  N  N   . VAL F  1 31  ? 14.764 -32.936 -19.101  1.00 22.05 ? 31   VAL G N   1 
ATOM   5790  C  CA  . VAL F  1 31  ? 13.832 -32.816 -20.198  1.00 22.56 ? 31   VAL G CA  1 
ATOM   5791  C  C   . VAL F  1 31  ? 12.447 -33.111 -19.657  1.00 23.29 ? 31   VAL G C   1 
ATOM   5792  O  O   . VAL F  1 31  ? 12.232 -34.160 -19.050  1.00 23.58 ? 31   VAL G O   1 
ATOM   5793  C  CB  . VAL F  1 31  ? 14.158 -33.802 -21.351  1.00 22.30 ? 31   VAL G CB  1 
ATOM   5794  C  CG1 . VAL F  1 31  ? 13.333 -33.460 -22.589  1.00 22.26 ? 31   VAL G CG1 1 
ATOM   5795  C  CG2 . VAL F  1 31  ? 15.656 -33.783 -21.704  1.00 21.76 ? 31   VAL G CG2 1 
ATOM   5796  N  N   . TRP F  1 32  ? 11.504 -32.199 -19.871  1.00 23.62 ? 32   TRP G N   1 
ATOM   5797  C  CA  . TRP F  1 32  ? 10.145 -32.464 -19.436  1.00 24.73 ? 32   TRP G CA  1 
ATOM   5798  C  C   . TRP F  1 32  ? 9.119  -31.683 -20.230  1.00 25.28 ? 32   TRP G C   1 
ATOM   5799  O  O   . TRP F  1 32  ? 9.403  -30.582 -20.730  1.00 25.48 ? 32   TRP G O   1 
ATOM   5800  C  CB  . TRP F  1 32  ? 9.988  -32.161 -17.940  1.00 25.05 ? 32   TRP G CB  1 
ATOM   5801  C  CG  . TRP F  1 32  ? 9.830  -30.709 -17.648  1.00 25.47 ? 32   TRP G CG  1 
ATOM   5802  C  CD1 . TRP F  1 32  ? 8.658  -30.034 -17.449  1.00 26.91 ? 32   TRP G CD1 1 
ATOM   5803  C  CD2 . TRP F  1 32  ? 10.875 -29.738 -17.535  1.00 25.81 ? 32   TRP G CD2 1 
ATOM   5804  N  NE1 . TRP F  1 32  ? 8.911  -28.701 -17.218  1.00 26.15 ? 32   TRP G NE1 1 
ATOM   5805  C  CE2 . TRP F  1 32  ? 10.264 -28.497 -17.258  1.00 25.51 ? 32   TRP G CE2 1 
ATOM   5806  C  CE3 . TRP F  1 32  ? 12.273 -29.798 -17.636  1.00 25.99 ? 32   TRP G CE3 1 
ATOM   5807  C  CZ2 . TRP F  1 32  ? 10.999 -27.323 -17.091  1.00 26.92 ? 32   TRP G CZ2 1 
ATOM   5808  C  CZ3 . TRP F  1 32  ? 12.999 -28.643 -17.462  1.00 26.65 ? 32   TRP G CZ3 1 
ATOM   5809  C  CH2 . TRP F  1 32  ? 12.363 -27.415 -17.196  1.00 27.09 ? 32   TRP G CH2 1 
ATOM   5810  N  N   . GLY F  1 33  ? 7.917  -32.247 -20.324  1.00 25.30 ? 33   GLY G N   1 
ATOM   5811  C  CA  . GLY F  1 33  ? 6.793  -31.564 -20.946  1.00 25.76 ? 33   GLY G CA  1 
ATOM   5812  C  C   . GLY F  1 33  ? 5.656  -32.529 -21.205  1.00 26.52 ? 33   GLY G C   1 
ATOM   5813  O  O   . GLY F  1 33  ? 5.457  -33.484 -20.461  1.00 26.12 ? 33   GLY G O   1 
ATOM   5814  N  N   . SER F  1 34  ? 4.921  -32.276 -22.280  1.00 26.94 ? 34   SER G N   1 
ATOM   5815  C  CA  . SER F  1 34  ? 3.710  -33.023 -22.574  1.00 27.39 ? 34   SER G CA  1 
ATOM   5816  C  C   . SER F  1 34  ? 3.521  -33.155 -24.083  1.00 27.31 ? 34   SER G C   1 
ATOM   5817  O  O   . SER F  1 34  ? 3.639  -32.172 -24.810  1.00 27.15 ? 34   SER G O   1 
ATOM   5818  C  CB  . SER F  1 34  ? 2.509  -32.314 -21.937  1.00 27.36 ? 34   SER G CB  1 
ATOM   5819  O  OG  . SER F  1 34  ? 1.289  -32.873 -22.382  1.00 29.23 ? 34   SER G OG  1 
ATOM   5820  N  N   . ILE F  1 35  ? 3.259  -34.377 -24.547  1.00 27.58 ? 35   ILE G N   1 
ATOM   5821  C  CA  . ILE F  1 35  ? 2.908  -34.618 -25.950  1.00 27.69 ? 35   ILE G CA  1 
ATOM   5822  C  C   . ILE F  1 35  ? 1.551  -35.308 -26.021  1.00 28.06 ? 35   ILE G C   1 
ATOM   5823  O  O   . ILE F  1 35  ? 1.357  -36.359 -25.406  1.00 27.94 ? 35   ILE G O   1 
ATOM   5824  C  CB  . ILE F  1 35  ? 3.975  -35.473 -26.684  1.00 27.79 ? 35   ILE G CB  1 
ATOM   5825  C  CG1 . ILE F  1 35  ? 5.367  -34.830 -26.551  1.00 27.49 ? 35   ILE G CG1 1 
ATOM   5826  C  CG2 . ILE F  1 35  ? 3.594  -35.677 -28.156  1.00 27.31 ? 35   ILE G CG2 1 
ATOM   5827  C  CD1 . ILE F  1 35  ? 6.528  -35.756 -26.926  1.00 28.02 ? 35   ILE G CD1 1 
ATOM   5828  N  N   . LYS F  1 36  ? 0.618  -34.706 -26.761  1.00 28.34 ? 36   LYS G N   1 
ATOM   5829  C  CA  . LYS F  1 36  ? -0.703 -35.301 -26.956  1.00 28.98 ? 36   LYS G CA  1 
ATOM   5830  C  C   . LYS F  1 36  ? -0.952 -35.801 -28.385  1.00 29.01 ? 36   LYS G C   1 
ATOM   5831  O  O   . LYS F  1 36  ? -0.166 -35.530 -29.306  1.00 29.36 ? 36   LYS G O   1 
ATOM   5832  C  CB  . LYS F  1 36  ? -1.817 -34.346 -26.491  1.00 29.16 ? 36   LYS G CB  1 
ATOM   5833  C  CG  . LYS F  1 36  ? -2.097 -33.143 -27.383  1.00 30.48 ? 36   LYS G CG  1 
ATOM   5834  C  CD  . LYS F  1 36  ? -3.309 -32.393 -26.843  1.00 32.83 ? 36   LYS G CD  1 
ATOM   5835  C  CE  . LYS F  1 36  ? -3.702 -31.208 -27.705  1.00 33.46 ? 36   LYS G CE  1 
ATOM   5836  N  NZ  . LYS F  1 36  ? -2.858 -30.014 -27.458  1.00 33.67 ? 36   LYS G NZ  1 
ATOM   5837  N  N   . GLY F  1 37  ? -2.050 -36.537 -28.555  1.00 28.66 ? 37   GLY G N   1 
ATOM   5838  C  CA  . GLY F  1 37  ? -2.491 -37.014 -29.862  1.00 28.26 ? 37   GLY G CA  1 
ATOM   5839  C  C   . GLY F  1 37  ? -1.727 -38.230 -30.327  1.00 28.25 ? 37   GLY G C   1 
ATOM   5840  O  O   . GLY F  1 37  ? -1.790 -38.594 -31.497  1.00 28.34 ? 37   GLY G O   1 
ATOM   5841  N  N   . LEU F  1 38  ? -0.986 -38.837 -29.407  1.00 28.15 ? 38   LEU G N   1 
ATOM   5842  C  CA  . LEU F  1 38  ? -0.253 -40.054 -29.686  1.00 28.18 ? 38   LEU G CA  1 
ATOM   5843  C  C   . LEU F  1 38  ? -1.184 -41.257 -29.577  1.00 28.46 ? 38   LEU G C   1 
ATOM   5844  O  O   . LEU F  1 38  ? -2.227 -41.188 -28.913  1.00 28.37 ? 38   LEU G O   1 
ATOM   5845  C  CB  . LEU F  1 38  ? 0.903  -40.205 -28.700  1.00 27.69 ? 38   LEU G CB  1 
ATOM   5846  C  CG  . LEU F  1 38  ? 2.074  -39.241 -28.884  1.00 27.53 ? 38   LEU G CG  1 
ATOM   5847  C  CD1 . LEU F  1 38  ? 3.055  -39.426 -27.748  1.00 27.18 ? 38   LEU G CD1 1 
ATOM   5848  C  CD2 . LEU F  1 38  ? 2.749  -39.491 -30.220  1.00 25.65 ? 38   LEU G CD2 1 
ATOM   5849  N  N   . THR F  1 39  ? -0.813 -42.345 -30.251  1.00 28.57 ? 39   THR G N   1 
ATOM   5850  C  CA  . THR F  1 39  ? -1.399 -43.646 -29.974  1.00 28.62 ? 39   THR G CA  1 
ATOM   5851  C  C   . THR F  1 39  ? -0.797 -44.140 -28.660  1.00 28.53 ? 39   THR G C   1 
ATOM   5852  O  O   . THR F  1 39  ? 0.374  -43.871 -28.375  1.00 28.65 ? 39   THR G O   1 
ATOM   5853  C  CB  . THR F  1 39  ? -1.115 -44.672 -31.101  1.00 28.47 ? 39   THR G CB  1 
ATOM   5854  O  OG1 . THR F  1 39  ? 0.296  -44.901 -31.211  1.00 28.12 ? 39   THR G OG1 1 
ATOM   5855  C  CG2 . THR F  1 39  ? -1.674 -44.185 -32.448  1.00 29.24 ? 39   THR G CG2 1 
ATOM   5856  N  N   . GLU F  1 40  ? -1.606 -44.844 -27.866  1.00 28.33 ? 40   GLU G N   1 
ATOM   5857  C  CA  . GLU F  1 40  ? -1.187 -45.400 -26.575  1.00 28.09 ? 40   GLU G CA  1 
ATOM   5858  C  C   . GLU F  1 40  ? 0.060  -46.273 -26.710  1.00 27.27 ? 40   GLU G C   1 
ATOM   5859  O  O   . GLU F  1 40  ? 0.175  -47.053 -27.662  1.00 27.42 ? 40   GLU G O   1 
ATOM   5860  C  CB  . GLU F  1 40  ? -2.335 -46.221 -25.967  1.00 28.50 ? 40   GLU G CB  1 
ATOM   5861  C  CG  . GLU F  1 40  ? -2.029 -46.827 -24.591  1.00 30.53 ? 40   GLU G CG  1 
ATOM   5862  C  CD  . GLU F  1 40  ? -3.175 -47.676 -24.041  1.00 33.43 ? 40   GLU G CD  1 
ATOM   5863  O  OE1 . GLU F  1 40  ? -3.229 -47.863 -22.804  1.00 34.35 ? 40   GLU G OE1 1 
ATOM   5864  O  OE2 . GLU F  1 40  ? -4.020 -48.141 -24.841  1.00 33.00 ? 40   GLU G OE2 1 
ATOM   5865  N  N   . GLY F  1 41  ? 0.982  -46.149 -25.761  1.00 26.34 ? 41   GLY G N   1 
ATOM   5866  C  CA  . GLY F  1 41  ? 2.195  -46.975 -25.753  1.00 25.48 ? 41   GLY G CA  1 
ATOM   5867  C  C   . GLY F  1 41  ? 3.479  -46.193 -25.993  1.00 25.01 ? 41   GLY G C   1 
ATOM   5868  O  O   . GLY F  1 41  ? 3.522  -44.980 -25.777  1.00 24.69 ? 41   GLY G O   1 
ATOM   5869  N  N   . LEU F  1 42  ? 4.515  -46.886 -26.459  1.00 24.27 ? 42   LEU G N   1 
ATOM   5870  C  CA  . LEU F  1 42  ? 5.855  -46.299 -26.583  1.00 23.34 ? 42   LEU G CA  1 
ATOM   5871  C  C   . LEU F  1 42  ? 6.081  -45.603 -27.917  1.00 22.69 ? 42   LEU G C   1 
ATOM   5872  O  O   . LEU F  1 42  ? 5.680  -46.099 -28.979  1.00 22.63 ? 42   LEU G O   1 
ATOM   5873  C  CB  . LEU F  1 42  ? 6.947  -47.354 -26.394  1.00 23.42 ? 42   LEU G CB  1 
ATOM   5874  C  CG  . LEU F  1 42  ? 7.147  -48.105 -25.081  1.00 23.98 ? 42   LEU G CG  1 
ATOM   5875  C  CD1 . LEU F  1 42  ? 8.103  -49.288 -25.294  1.00 24.60 ? 42   LEU G CD1 1 
ATOM   5876  C  CD2 . LEU F  1 42  ? 7.668  -47.191 -23.992  1.00 25.42 ? 42   LEU G CD2 1 
ATOM   5877  N  N   . HIS F  1 43  ? 6.754  -44.459 -27.852  1.00 21.36 ? 43   HIS G N   1 
ATOM   5878  C  CA  . HIS F  1 43  ? 7.137  -43.728 -29.040  1.00 20.02 ? 43   HIS G CA  1 
ATOM   5879  C  C   . HIS F  1 43  ? 8.581  -43.279 -28.934  1.00 19.33 ? 43   HIS G C   1 
ATOM   5880  O  O   . HIS F  1 43  ? 8.989  -42.738 -27.913  1.00 19.32 ? 43   HIS G O   1 
ATOM   5881  C  CB  . HIS F  1 43  ? 6.215  -42.526 -29.243  1.00 20.35 ? 43   HIS G CB  1 
ATOM   5882  C  CG  . HIS F  1 43  ? 4.803  -42.898 -29.585  1.00 20.37 ? 43   HIS G CG  1 
ATOM   5883  N  ND1 . HIS F  1 43  ? 4.368  -43.050 -30.882  1.00 21.51 ? 43   HIS G ND1 1 
ATOM   5884  C  CD2 . HIS F  1 43  ? 3.726  -43.138 -28.798  1.00 20.63 ? 43   HIS G CD2 1 
ATOM   5885  C  CE1 . HIS F  1 43  ? 3.083  -43.364 -30.885  1.00 18.98 ? 43   HIS G CE1 1 
ATOM   5886  N  NE2 . HIS F  1 43  ? 2.669  -43.424 -29.632  1.00 20.44 ? 43   HIS G NE2 1 
ATOM   5887  N  N   . GLY F  1 44  ? 9.341  -43.525 -30.000  1.00 18.68 ? 44   GLY G N   1 
ATOM   5888  C  CA  . GLY F  1 44  ? 10.738 -43.140 -30.105  1.00 17.73 ? 44   GLY G CA  1 
ATOM   5889  C  C   . GLY F  1 44  ? 10.869 -41.642 -29.947  1.00 17.57 ? 44   GLY G C   1 
ATOM   5890  O  O   . GLY F  1 44  ? 9.984  -40.878 -30.364  1.00 17.46 ? 44   GLY G O   1 
ATOM   5891  N  N   . PHE F  1 45  ? 11.987 -41.228 -29.376  1.00 16.97 ? 45   PHE G N   1 
ATOM   5892  C  CA  . PHE F  1 45  ? 12.173 -39.847 -28.961  1.00 16.89 ? 45   PHE G CA  1 
ATOM   5893  C  C   . PHE F  1 45  ? 13.647 -39.488 -29.080  1.00 16.66 ? 45   PHE G C   1 
ATOM   5894  O  O   . PHE F  1 45  ? 14.474 -39.921 -28.269  1.00 16.13 ? 45   PHE G O   1 
ATOM   5895  C  CB  . PHE F  1 45  ? 11.703 -39.731 -27.502  1.00 17.39 ? 45   PHE G CB  1 
ATOM   5896  C  CG  . PHE F  1 45  ? 11.564 -38.321 -26.996  1.00 18.15 ? 45   PHE G CG  1 
ATOM   5897  C  CD1 . PHE F  1 45  ? 10.660 -37.438 -27.577  1.00 19.49 ? 45   PHE G CD1 1 
ATOM   5898  C  CD2 . PHE F  1 45  ? 12.283 -37.909 -25.884  1.00 18.70 ? 45   PHE G CD2 1 
ATOM   5899  C  CE1 . PHE F  1 45  ? 10.514 -36.145 -27.093  1.00 21.20 ? 45   PHE G CE1 1 
ATOM   5900  C  CE2 . PHE F  1 45  ? 12.135 -36.616 -25.382  1.00 20.39 ? 45   PHE G CE2 1 
ATOM   5901  C  CZ  . PHE F  1 45  ? 11.252 -35.735 -25.991  1.00 20.47 ? 45   PHE G CZ  1 
ATOM   5902  N  N   . HIS F  1 46  ? 14.005 -38.730 -30.114  1.00 16.10 ? 46   HIS G N   1 
ATOM   5903  C  CA  . HIS F  1 46  ? 15.413 -38.439 -30.298  1.00 16.06 ? 46   HIS G CA  1 
ATOM   5904  C  C   . HIS F  1 46  ? 15.669 -36.998 -30.730  1.00 15.18 ? 46   HIS G C   1 
ATOM   5905  O  O   . HIS F  1 46  ? 14.783 -36.289 -31.271  1.00 13.98 ? 46   HIS G O   1 
ATOM   5906  C  CB  . HIS F  1 46  ? 16.108 -39.363 -31.332  1.00 16.52 ? 46   HIS G CB  1 
ATOM   5907  C  CG  . HIS F  1 46  ? 15.520 -40.739 -31.452  1.00 18.05 ? 46   HIS G CG  1 
ATOM   5908  N  ND1 . HIS F  1 46  ? 14.691 -41.102 -32.490  1.00 20.49 ? 46   HIS G ND1 1 
ATOM   5909  C  CD2 . HIS F  1 46  ? 15.677 -41.847 -30.693  1.00 19.01 ? 46   HIS G CD2 1 
ATOM   5910  C  CE1 . HIS F  1 46  ? 14.342 -42.371 -32.356  1.00 19.14 ? 46   HIS G CE1 1 
ATOM   5911  N  NE2 . HIS F  1 46  ? 14.924 -42.845 -31.270  1.00 17.92 ? 46   HIS G NE2 1 
ATOM   5912  N  N   . VAL F  1 47  ? 16.915 -36.610 -30.536  1.00 15.32 ? 47   VAL G N   1 
ATOM   5913  C  CA  . VAL F  1 47  ? 17.412 -35.373 -31.115  1.00 16.19 ? 47   VAL G CA  1 
ATOM   5914  C  C   . VAL F  1 47  ? 18.080 -35.708 -32.455  1.00 16.19 ? 47   VAL G C   1 
ATOM   5915  O  O   . VAL F  1 47  ? 19.027 -36.503 -32.505  1.00 16.44 ? 47   VAL G O   1 
ATOM   5916  C  CB  . VAL F  1 47  ? 18.370 -34.602 -30.157  1.00 16.24 ? 47   VAL G CB  1 
ATOM   5917  C  CG1 . VAL F  1 47  ? 19.054 -33.431 -30.886  1.00 16.47 ? 47   VAL G CG1 1 
ATOM   5918  C  CG2 . VAL F  1 47  ? 17.611 -34.103 -28.920  1.00 16.36 ? 47   VAL G CG2 1 
ATOM   5919  N  N   . HIS F  1 48  ? 17.580 -35.088 -33.527  1.00 16.65 ? 48   HIS G N   1 
ATOM   5920  C  CA  . HIS F  1 48  ? 18.135 -35.291 -34.869  1.00 16.85 ? 48   HIS G CA  1 
ATOM   5921  C  C   . HIS F  1 48  ? 19.153 -34.204 -35.217  1.00 17.02 ? 48   HIS G C   1 
ATOM   5922  O  O   . HIS F  1 48  ? 19.148 -33.117 -34.628  1.00 17.04 ? 48   HIS G O   1 
ATOM   5923  C  CB  . HIS F  1 48  ? 17.014 -35.383 -35.901  1.00 17.07 ? 48   HIS G CB  1 
ATOM   5924  C  CG  . HIS F  1 48  ? 16.261 -36.671 -35.836  1.00 18.22 ? 48   HIS G CG  1 
ATOM   5925  N  ND1 . HIS F  1 48  ? 16.233 -37.574 -36.880  1.00 18.56 ? 48   HIS G ND1 1 
ATOM   5926  C  CD2 . HIS F  1 48  ? 15.551 -37.237 -34.827  1.00 19.06 ? 48   HIS G CD2 1 
ATOM   5927  C  CE1 . HIS F  1 48  ? 15.510 -38.623 -36.529  1.00 19.55 ? 48   HIS G CE1 1 
ATOM   5928  N  NE2 . HIS F  1 48  ? 15.091 -38.445 -35.288  1.00 19.87 ? 48   HIS G NE2 1 
ATOM   5929  N  N   . GLU F  1 49  ? 20.023 -34.508 -36.173  1.00 16.45 ? 49   GLU G N   1 
ATOM   5930  C  CA  . GLU F  1 49  ? 21.201 -33.709 -36.435  1.00 16.64 ? 49   GLU G CA  1 
ATOM   5931  C  C   . GLU F  1 49  ? 20.891 -32.274 -36.862  1.00 16.35 ? 49   GLU G C   1 
ATOM   5932  O  O   . GLU F  1 49  ? 21.604 -31.358 -36.451  1.00 17.10 ? 49   GLU G O   1 
ATOM   5933  C  CB  . GLU F  1 49  ? 22.084 -34.409 -37.474  1.00 16.53 ? 49   GLU G CB  1 
ATOM   5934  C  CG  . GLU F  1 49  ? 23.357 -33.680 -37.816  1.00 17.77 ? 49   GLU G CG  1 
ATOM   5935  C  CD  . GLU F  1 49  ? 24.248 -34.469 -38.753  1.00 18.42 ? 49   GLU G CD  1 
ATOM   5936  O  OE1 . GLU F  1 49  ? 25.423 -34.090 -38.900  1.00 18.03 ? 49   GLU G OE1 1 
ATOM   5937  O  OE2 . GLU F  1 49  ? 23.779 -35.461 -39.360  1.00 19.61 ? 49   GLU G OE2 1 
ATOM   5938  N  N   . PHE F  1 50  ? 19.836 -32.060 -37.648  1.00 16.01 ? 50   PHE G N   1 
ATOM   5939  C  CA  . PHE F  1 50  ? 19.651 -30.747 -38.282  1.00 15.79 ? 50   PHE G CA  1 
ATOM   5940  C  C   . PHE F  1 50  ? 18.364 -30.045 -37.873  1.00 15.92 ? 50   PHE G C   1 
ATOM   5941  O  O   . PHE F  1 50  ? 17.291 -30.654 -37.866  1.00 15.71 ? 50   PHE G O   1 
ATOM   5942  C  CB  . PHE F  1 50  ? 19.745 -30.866 -39.820  1.00 15.45 ? 50   PHE G CB  1 
ATOM   5943  C  CG  . PHE F  1 50  ? 21.084 -31.371 -40.301  1.00 15.79 ? 50   PHE G CG  1 
ATOM   5944  C  CD1 . PHE F  1 50  ? 22.238 -30.620 -40.094  1.00 16.43 ? 50   PHE G CD1 1 
ATOM   5945  C  CD2 . PHE F  1 50  ? 21.193 -32.604 -40.939  1.00 17.49 ? 50   PHE G CD2 1 
ATOM   5946  C  CE1 . PHE F  1 50  ? 23.486 -31.090 -40.518  1.00 16.97 ? 50   PHE G CE1 1 
ATOM   5947  C  CE2 . PHE F  1 50  ? 22.428 -33.081 -41.373  1.00 14.77 ? 50   PHE G CE2 1 
ATOM   5948  C  CZ  . PHE F  1 50  ? 23.579 -32.320 -41.159  1.00 16.78 ? 50   PHE G CZ  1 
ATOM   5949  N  N   . GLY F  1 51  ? 18.483 -28.763 -37.518  1.00 15.28 ? 51   GLY G N   1 
ATOM   5950  C  CA  . GLY F  1 51  ? 17.311 -27.929 -37.236  1.00 15.07 ? 51   GLY G CA  1 
ATOM   5951  C  C   . GLY F  1 51  ? 16.690 -27.448 -38.531  1.00 15.65 ? 51   GLY G C   1 
ATOM   5952  O  O   . GLY F  1 51  ? 16.340 -26.279 -38.688  1.00 15.15 ? 51   GLY G O   1 
ATOM   5953  N  N   . ASP F  1 52  ? 16.551 -28.374 -39.469  1.00 15.63 ? 52   ASP G N   1 
ATOM   5954  C  CA  . ASP F  1 52  ? 16.003 -28.090 -40.769  1.00 16.42 ? 52   ASP G CA  1 
ATOM   5955  C  C   . ASP F  1 52  ? 14.587 -28.657 -40.872  1.00 16.61 ? 52   ASP G C   1 
ATOM   5956  O  O   . ASP F  1 52  ? 14.407 -29.873 -40.822  1.00 17.26 ? 52   ASP G O   1 
ATOM   5957  C  CB  . ASP F  1 52  ? 16.899 -28.755 -41.814  1.00 16.28 ? 52   ASP G CB  1 
ATOM   5958  C  CG  . ASP F  1 52  ? 16.600 -28.303 -43.214  1.00 16.77 ? 52   ASP G CG  1 
ATOM   5959  O  OD1 . ASP F  1 52  ? 17.506 -28.447 -44.062  1.00 16.92 ? 52   ASP G OD1 1 
ATOM   5960  O  OD2 . ASP F  1 52  ? 15.480 -27.795 -43.469  1.00 17.23 ? 52   ASP G OD2 1 
ATOM   5961  N  N   . ASN F  1 53  ? 13.600 -27.775 -41.036  1.00 17.33 ? 53   ASN G N   1 
ATOM   5962  C  CA  . ASN F  1 53  ? 12.196 -28.177 -41.193  1.00 17.98 ? 53   ASN G CA  1 
ATOM   5963  C  C   . ASN F  1 53  ? 11.634 -27.850 -42.570  1.00 17.48 ? 53   ASN G C   1 
ATOM   5964  O  O   . ASN F  1 53  ? 10.406 -27.814 -42.773  1.00 16.84 ? 53   ASN G O   1 
ATOM   5965  C  CB  . ASN F  1 53  ? 11.321 -27.531 -40.099  1.00 18.92 ? 53   ASN G CB  1 
ATOM   5966  C  CG  . ASN F  1 53  ? 10.051 -28.332 -39.813  1.00 21.34 ? 53   ASN G CG  1 
ATOM   5967  O  OD1 . ASN F  1 53  ? 8.948  -27.781 -39.783  1.00 24.88 ? 53   ASN G OD1 1 
ATOM   5968  N  ND2 . ASN F  1 53  ? 10.203 -29.639 -39.606  1.00 23.42 ? 53   ASN G ND2 1 
ATOM   5969  N  N   . THR F  1 54  ? 12.525 -27.609 -43.524  1.00 16.61 ? 54   THR G N   1 
ATOM   5970  C  CA  . THR F  1 54  ? 12.080 -27.126 -44.838  1.00 16.69 ? 54   THR G CA  1 
ATOM   5971  C  C   . THR F  1 54  ? 11.189 -28.116 -45.580  1.00 17.45 ? 54   THR G C   1 
ATOM   5972  O  O   . THR F  1 54  ? 10.287 -27.704 -46.322  1.00 17.63 ? 54   THR G O   1 
ATOM   5973  C  CB  . THR F  1 54  ? 13.255 -26.704 -45.711  1.00 16.29 ? 54   THR G CB  1 
ATOM   5974  O  OG1 . THR F  1 54  ? 14.186 -27.790 -45.782  1.00 15.13 ? 54   THR G OG1 1 
ATOM   5975  C  CG2 . THR F  1 54  ? 13.944 -25.506 -45.077  1.00 15.29 ? 54   THR G CG2 1 
ATOM   5976  N  N   . ALA F  1 55  ? 11.456 -29.409 -45.384  1.00 17.94 ? 55   ALA G N   1 
ATOM   5977  C  CA  . ALA F  1 55  ? 10.601 -30.493 -45.892  1.00 18.74 ? 55   ALA G CA  1 
ATOM   5978  C  C   . ALA F  1 55  ? 10.043 -31.300 -44.712  1.00 18.92 ? 55   ALA G C   1 
ATOM   5979  O  O   . ALA F  1 55  ? 10.157 -32.535 -44.658  1.00 19.72 ? 55   ALA G O   1 
ATOM   5980  C  CB  . ALA F  1 55  ? 11.391 -31.394 -46.858  1.00 18.16 ? 55   ALA G CB  1 
ATOM   5981  N  N   . GLY F  1 56  ? 9.468  -30.587 -43.740  1.00 18.62 ? 56   GLY G N   1 
ATOM   5982  C  CA  . GLY F  1 56  ? 8.965  -31.217 -42.521  1.00 18.05 ? 56   GLY G CA  1 
ATOM   5983  C  C   . GLY F  1 56  ? 10.049 -31.879 -41.689  1.00 17.27 ? 56   GLY G C   1 
ATOM   5984  O  O   . GLY F  1 56  ? 11.226 -31.526 -41.785  1.00 17.02 ? 56   GLY G O   1 
ATOM   5985  N  N   . CYS F  1 57  ? 9.657  -32.885 -40.908  1.00 16.53 ? 57   CYS G N   1 
ATOM   5986  C  CA  . CYS F  1 57  ? 10.591 -33.588 -40.034  1.00 15.77 ? 57   CYS G CA  1 
ATOM   5987  C  C   . CYS F  1 57  ? 11.670 -34.423 -40.769  1.00 16.53 ? 57   CYS G C   1 
ATOM   5988  O  O   . CYS F  1 57  ? 12.717 -34.717 -40.189  1.00 16.32 ? 57   CYS G O   1 
ATOM   5989  C  CB  . CYS F  1 57  ? 9.808  -34.438 -39.027  0.40 15.47 ? 57   CYS G CB  1 
ATOM   5990  S  SG  . CYS F  1 57  ? 8.536  -33.503 -38.123  0.40 12.37 ? 57   CYS G SG  1 
ATOM   5991  N  N   . THR F  1 58  ? 11.422 -34.792 -42.031  1.00 17.01 ? 58   THR G N   1 
ATOM   5992  C  CA  . THR F  1 58  ? 12.413 -35.551 -42.830  1.00 17.84 ? 58   THR G CA  1 
ATOM   5993  C  C   . THR F  1 58  ? 13.746 -34.799 -42.927  1.00 17.65 ? 58   THR G C   1 
ATOM   5994  O  O   . THR F  1 58  ? 14.826 -35.402 -42.820  1.00 17.30 ? 58   THR G O   1 
ATOM   5995  C  CB  . THR F  1 58  ? 11.888 -35.862 -44.268  1.00 17.92 ? 58   THR G CB  1 
ATOM   5996  O  OG1 . THR F  1 58  ? 10.601 -36.470 -44.184  1.00 19.48 ? 58   THR G OG1 1 
ATOM   5997  C  CG2 . THR F  1 58  ? 12.830 -36.815 -45.024  1.00 19.64 ? 58   THR G CG2 1 
ATOM   5998  N  N   . SER F  1 59  ? 13.670 -33.480 -43.110  1.00 17.08 ? 59   SER G N   1 
ATOM   5999  C  CA  . SER F  1 59  ? 14.889 -32.700 -43.312  1.00 16.78 ? 59   SER G CA  1 
ATOM   6000  C  C   . SER F  1 59  ? 15.747 -32.525 -42.047  1.00 16.08 ? 59   SER G C   1 
ATOM   6001  O  O   . SER F  1 59  ? 16.893 -32.095 -42.135  1.00 16.65 ? 59   SER G O   1 
ATOM   6002  C  CB  . SER F  1 59  ? 14.610 -31.384 -44.040  1.00 17.52 ? 59   SER G CB  1 
ATOM   6003  O  OG  . SER F  1 59  ? 13.426 -30.756 -43.595  1.00 19.14 ? 59   SER G OG  1 
ATOM   6004  N  N   . ALA F  1 60  ? 15.214 -32.915 -40.887  1.00 15.32 ? 60   ALA G N   1 
ATOM   6005  C  CA  . ALA F  1 60  ? 16.020 -33.010 -39.655  1.00 14.93 ? 60   ALA G CA  1 
ATOM   6006  C  C   . ALA F  1 60  ? 17.205 -33.965 -39.805  1.00 14.80 ? 60   ALA G C   1 
ATOM   6007  O  O   . ALA F  1 60  ? 18.172 -33.884 -39.055  1.00 13.90 ? 60   ALA G O   1 
ATOM   6008  C  CB  . ALA F  1 60  ? 15.156 -33.405 -38.467  1.00 14.36 ? 60   ALA G CB  1 
ATOM   6009  N  N   . GLY F  1 61  ? 17.133 -34.868 -40.794  1.00 15.17 ? 61   GLY G N   1 
ATOM   6010  C  CA  . GLY F  1 61  ? 18.250 -35.780 -41.054  1.00 15.10 ? 61   GLY G CA  1 
ATOM   6011  C  C   . GLY F  1 61  ? 18.249 -36.897 -40.025  1.00 15.52 ? 61   GLY G C   1 
ATOM   6012  O  O   . GLY F  1 61  ? 17.221 -37.164 -39.419  1.00 16.21 ? 61   GLY G O   1 
ATOM   6013  N  N   . PRO F  1 62  ? 19.402 -37.543 -39.814  1.00 15.68 ? 62   PRO G N   1 
ATOM   6014  C  CA  . PRO F  1 62  ? 19.547 -38.682 -38.907  1.00 16.15 ? 62   PRO G CA  1 
ATOM   6015  C  C   . PRO F  1 62  ? 19.720 -38.272 -37.443  1.00 16.81 ? 62   PRO G C   1 
ATOM   6016  O  O   . PRO F  1 62  ? 19.729 -37.077 -37.117  1.00 16.09 ? 62   PRO G O   1 
ATOM   6017  C  CB  . PRO F  1 62  ? 20.846 -39.326 -39.375  1.00 16.19 ? 62   PRO G CB  1 
ATOM   6018  C  CG  . PRO F  1 62  ? 21.659 -38.190 -39.893  1.00 15.64 ? 62   PRO G CG  1 
ATOM   6019  C  CD  . PRO F  1 62  ? 20.660 -37.243 -40.520  1.00 16.65 ? 62   PRO G CD  1 
ATOM   6020  N  N   . HIS F  1 63  ? 19.873 -39.267 -36.574  1.00 16.51 ? 63   HIS G N   1 
ATOM   6021  C  CA  . HIS F  1 63  ? 20.094 -39.006 -35.161  1.00 16.76 ? 63   HIS G CA  1 
ATOM   6022  C  C   . HIS F  1 63  ? 21.395 -38.244 -34.977  1.00 16.51 ? 63   HIS G C   1 
ATOM   6023  O  O   . HIS F  1 63  ? 22.402 -38.525 -35.647  1.00 15.65 ? 63   HIS G O   1 
ATOM   6024  C  CB  . HIS F  1 63  ? 20.098 -40.329 -34.401  1.00 16.83 ? 63   HIS G CB  1 
ATOM   6025  C  CG  . HIS F  1 63  ? 18.775 -41.028 -34.431  1.00 17.27 ? 63   HIS G CG  1 
ATOM   6026  N  ND1 . HIS F  1 63  ? 18.506 -42.153 -33.685  1.00 17.16 ? 63   HIS G ND1 1 
ATOM   6027  C  CD2 . HIS F  1 63  ? 17.636 -40.751 -35.110  1.00 17.40 ? 63   HIS G CD2 1 
ATOM   6028  C  CE1 . HIS F  1 63  ? 17.263 -42.538 -33.896  1.00 17.12 ? 63   HIS G CE1 1 
ATOM   6029  N  NE2 . HIS F  1 63  ? 16.710 -41.701 -34.754  1.00 19.71 ? 63   HIS G NE2 1 
ATOM   6030  N  N   . PHE F  1 64  ? 21.367 -37.261 -34.079  1.00 16.08 ? 64   PHE G N   1 
ATOM   6031  C  CA  . PHE F  1 64  ? 22.537 -36.436 -33.814  1.00 16.05 ? 64   PHE G CA  1 
ATOM   6032  C  C   . PHE F  1 64  ? 23.608 -37.366 -33.238  1.00 16.37 ? 64   PHE G C   1 
ATOM   6033  O  O   . PHE F  1 64  ? 23.405 -37.992 -32.189  1.00 16.84 ? 64   PHE G O   1 
ATOM   6034  C  CB  . PHE F  1 64  ? 22.151 -35.273 -32.882  1.00 15.59 ? 64   PHE G CB  1 
ATOM   6035  C  CG  . PHE F  1 64  ? 23.313 -34.422 -32.422  1.00 15.33 ? 64   PHE G CG  1 
ATOM   6036  C  CD1 . PHE F  1 64  ? 23.416 -34.056 -31.078  1.00 13.85 ? 64   PHE G CD1 1 
ATOM   6037  C  CD2 . PHE F  1 64  ? 24.284 -33.972 -33.327  1.00 15.05 ? 64   PHE G CD2 1 
ATOM   6038  C  CE1 . PHE F  1 64  ? 24.490 -33.269 -30.622  1.00 17.27 ? 64   PHE G CE1 1 
ATOM   6039  C  CE2 . PHE F  1 64  ? 25.358 -33.190 -32.894  1.00 17.40 ? 64   PHE G CE2 1 
ATOM   6040  C  CZ  . PHE F  1 64  ? 25.460 -32.825 -31.534  1.00 17.43 ? 64   PHE G CZ  1 
ATOM   6041  N  N   . ASN F  1 65  ? 24.731 -37.490 -33.941  1.00 16.62 ? 65   ASN G N   1 
ATOM   6042  C  CA  . ASN F  1 65  ? 25.711 -38.536 -33.634  1.00 17.60 ? 65   ASN G CA  1 
ATOM   6043  C  C   . ASN F  1 65  ? 27.148 -38.061 -33.786  1.00 18.30 ? 65   ASN G C   1 
ATOM   6044  O  O   . ASN F  1 65  ? 27.929 -38.655 -34.536  1.00 19.23 ? 65   ASN G O   1 
ATOM   6045  C  CB  . ASN F  1 65  ? 25.446 -39.757 -34.526  1.00 18.48 ? 65   ASN G CB  1 
ATOM   6046  C  CG  . ASN F  1 65  ? 26.324 -40.946 -34.189  1.00 17.96 ? 65   ASN G CG  1 
ATOM   6047  O  OD1 . ASN F  1 65  ? 26.756 -41.119 -33.040  1.00 18.61 ? 65   ASN G OD1 1 
ATOM   6048  N  ND2 . ASN F  1 65  ? 26.565 -41.799 -35.188  1.00 15.96 ? 65   ASN G ND2 1 
ATOM   6049  N  N   . PRO F  1 66  ? 27.522 -37.002 -33.044  1.00 19.02 ? 66   PRO G N   1 
ATOM   6050  C  CA  . PRO F  1 66  ? 28.806 -36.335 -33.274  1.00 19.54 ? 66   PRO G CA  1 
ATOM   6051  C  C   . PRO F  1 66  ? 29.993 -37.254 -33.014  1.00 20.31 ? 66   PRO G C   1 
ATOM   6052  O  O   . PRO F  1 66  ? 31.074 -37.001 -33.522  1.00 20.13 ? 66   PRO G O   1 
ATOM   6053  C  CB  . PRO F  1 66  ? 28.798 -35.183 -32.265  1.00 19.57 ? 66   PRO G CB  1 
ATOM   6054  C  CG  . PRO F  1 66  ? 27.840 -35.620 -31.185  1.00 19.52 ? 66   PRO G CG  1 
ATOM   6055  C  CD  . PRO F  1 66  ? 26.794 -36.434 -31.895  1.00 18.40 ? 66   PRO G CD  1 
ATOM   6056  N  N   . LEU F  1 67  ? 29.782 -38.312 -32.236  1.00 21.47 ? 67   LEU G N   1 
ATOM   6057  C  CA  . LEU F  1 67  ? 30.859 -39.239 -31.881  1.00 22.36 ? 67   LEU G CA  1 
ATOM   6058  C  C   . LEU F  1 67  ? 30.956 -40.487 -32.770  1.00 23.07 ? 67   LEU G C   1 
ATOM   6059  O  O   . LEU F  1 67  ? 31.826 -41.335 -32.549  1.00 23.68 ? 67   LEU G O   1 
ATOM   6060  C  CB  . LEU F  1 67  ? 30.740 -39.647 -30.404  1.00 23.10 ? 67   LEU G CB  1 
ATOM   6061  C  CG  . LEU F  1 67  ? 31.253 -38.650 -29.357  1.00 23.82 ? 67   LEU G CG  1 
ATOM   6062  C  CD1 . LEU F  1 67  ? 30.825 -39.063 -27.962  1.00 25.67 ? 67   LEU G CD1 1 
ATOM   6063  C  CD2 . LEU F  1 67  ? 32.783 -38.560 -29.442  1.00 27.59 ? 67   LEU G CD2 1 
ATOM   6064  N  N   . SER F  1 68  ? 30.060 -40.599 -33.758  1.00 23.22 ? 68   SER G N   1 
ATOM   6065  C  CA  . SER F  1 68  ? 30.073 -41.694 -34.749  1.00 23.33 ? 68   SER G CA  1 
ATOM   6066  C  C   . SER F  1 68  ? 29.882 -43.087 -34.131  1.00 23.17 ? 68   SER G C   1 
ATOM   6067  O  O   . SER F  1 68  ? 30.617 -44.027 -34.436  1.00 22.62 ? 68   SER G O   1 
ATOM   6068  C  CB  . SER F  1 68  ? 31.337 -41.637 -35.611  1.00 23.38 ? 68   SER G CB  1 
ATOM   6069  O  OG  . SER F  1 68  ? 31.349 -40.432 -36.354  1.00 24.29 ? 68   SER G OG  1 
ATOM   6070  N  N   . ARG F  1 69  ? 28.873 -43.199 -33.272  1.00 22.86 ? 69   ARG G N   1 
ATOM   6071  C  CA  . ARG F  1 69  ? 28.596 -44.443 -32.563  1.00 23.33 ? 69   ARG G CA  1 
ATOM   6072  C  C   . ARG F  1 69  ? 27.348 -45.101 -33.146  1.00 22.93 ? 69   ARG G C   1 
ATOM   6073  O  O   . ARG F  1 69  ? 26.698 -44.531 -34.039  1.00 23.14 ? 69   ARG G O   1 
ATOM   6074  C  CB  . ARG F  1 69  ? 28.420 -44.179 -31.058  1.00 23.49 ? 69   ARG G CB  1 
ATOM   6075  C  CG  . ARG F  1 69  ? 29.587 -43.436 -30.370  1.00 25.63 ? 69   ARG G CG  1 
ATOM   6076  C  CD  . ARG F  1 69  ? 30.589 -44.381 -29.711  1.00 28.96 ? 69   ARG G CD  1 
ATOM   6077  N  NE  . ARG F  1 69  ? 31.643 -43.688 -28.955  1.00 30.78 ? 69   ARG G NE  1 
ATOM   6078  C  CZ  . ARG F  1 69  ? 31.511 -43.172 -27.730  1.00 31.29 ? 69   ARG G CZ  1 
ATOM   6079  N  NH1 . ARG F  1 69  ? 32.553 -42.589 -27.151  1.00 32.75 ? 69   ARG G NH1 1 
ATOM   6080  N  NH2 . ARG F  1 69  ? 30.356 -43.231 -27.071  1.00 31.84 ? 69   ARG G NH2 1 
ATOM   6081  N  N   . LYS F  1 70  ? 27.021 -46.299 -32.657  1.00 22.58 ? 70   LYS G N   1 
ATOM   6082  C  CA  . LYS F  1 70  ? 25.811 -47.010 -33.070  1.00 22.06 ? 70   LYS G CA  1 
ATOM   6083  C  C   . LYS F  1 70  ? 24.641 -46.562 -32.204  1.00 21.54 ? 70   LYS G C   1 
ATOM   6084  O  O   . LYS F  1 70  ? 24.834 -46.000 -31.125  1.00 21.37 ? 70   LYS G O   1 
ATOM   6085  C  CB  . LYS F  1 70  ? 25.998 -48.536 -32.980  1.00 22.42 ? 70   LYS G CB  1 
ATOM   6086  C  CG  . LYS F  1 70  ? 27.153 -49.090 -33.820  1.00 23.58 ? 70   LYS G CG  1 
ATOM   6087  C  CD  . LYS F  1 70  ? 27.001 -50.584 -34.079  1.00 26.42 ? 70   LYS G CD  1 
ATOM   6088  C  CE  . LYS F  1 70  ? 28.287 -51.224 -34.610  1.00 27.20 ? 70   LYS G CE  1 
ATOM   6089  N  NZ  . LYS F  1 70  ? 28.784 -50.584 -35.864  1.00 27.47 ? 70   LYS G NZ  1 
ATOM   6090  N  N   . HIS F  1 71  ? 23.429 -46.792 -32.682  1.00 20.57 ? 71   HIS G N   1 
ATOM   6091  C  CA  . HIS F  1 71  ? 22.240 -46.399 -31.946  1.00 20.11 ? 71   HIS G CA  1 
ATOM   6092  C  C   . HIS F  1 71  ? 22.142 -47.236 -30.696  1.00 20.55 ? 71   HIS G C   1 
ATOM   6093  O  O   . HIS F  1 71  ? 22.524 -48.411 -30.711  1.00 20.19 ? 71   HIS G O   1 
ATOM   6094  C  CB  . HIS F  1 71  ? 21.006 -46.618 -32.815  1.00 19.95 ? 71   HIS G CB  1 
ATOM   6095  C  CG  . HIS F  1 71  ? 19.720 -46.276 -32.146  1.00 19.51 ? 71   HIS G CG  1 
ATOM   6096  N  ND1 . HIS F  1 71  ? 19.266 -44.980 -32.019  1.00 18.56 ? 71   HIS G ND1 1 
ATOM   6097  C  CD2 . HIS F  1 71  ? 18.780 -47.060 -31.573  1.00 20.33 ? 71   HIS G CD2 1 
ATOM   6098  C  CE1 . HIS F  1 71  ? 18.101 -44.981 -31.398  1.00 19.00 ? 71   HIS G CE1 1 
ATOM   6099  N  NE2 . HIS F  1 71  ? 17.779 -46.230 -31.121  1.00 19.44 ? 71   HIS G NE2 1 
ATOM   6100  N  N   . GLY F  1 72  ? 21.648 -46.620 -29.623  1.00 20.15 ? 72   GLY G N   1 
ATOM   6101  C  CA  . GLY F  1 72  ? 21.433 -47.294 -28.358  1.00 20.02 ? 72   GLY G CA  1 
ATOM   6102  C  C   . GLY F  1 72  ? 20.285 -46.695 -27.572  1.00 20.48 ? 72   GLY G C   1 
ATOM   6103  O  O   . GLY F  1 72  ? 19.666 -45.686 -27.981  1.00 20.27 ? 72   GLY G O   1 
ATOM   6104  N  N   . GLY F  1 73  ? 19.975 -47.327 -26.440  1.00 20.21 ? 73   GLY G N   1 
ATOM   6105  C  CA  . GLY F  1 73  ? 19.059 -46.728 -25.474  1.00 20.63 ? 73   GLY G CA  1 
ATOM   6106  C  C   . GLY F  1 73  ? 19.830 -45.695 -24.657  1.00 20.32 ? 73   GLY G C   1 
ATOM   6107  O  O   . GLY F  1 73  ? 21.059 -45.746 -24.618  1.00 20.16 ? 73   GLY G O   1 
ATOM   6108  N  N   . PRO F  1 74  ? 19.120 -44.765 -23.992  1.00 21.02 ? 74   PRO G N   1 
ATOM   6109  C  CA  . PRO F  1 74  ? 19.798 -43.642 -23.293  1.00 21.73 ? 74   PRO G CA  1 
ATOM   6110  C  C   . PRO F  1 74  ? 20.783 -44.109 -22.219  1.00 22.68 ? 74   PRO G C   1 
ATOM   6111  O  O   . PRO F  1 74  ? 21.732 -43.390 -21.890  1.00 22.38 ? 74   PRO G O   1 
ATOM   6112  C  CB  . PRO F  1 74  ? 18.640 -42.874 -22.646  1.00 21.70 ? 74   PRO G CB  1 
ATOM   6113  C  CG  . PRO F  1 74  ? 17.473 -43.871 -22.618  1.00 21.16 ? 74   PRO G CG  1 
ATOM   6114  C  CD  . PRO F  1 74  ? 17.653 -44.702 -23.843  1.00 20.89 ? 74   PRO G CD  1 
ATOM   6115  N  N   . LYS F  1 75  ? 20.558 -45.312 -21.681  1.00 23.83 ? 75   LYS G N   1 
ATOM   6116  C  CA  . LYS F  1 75  ? 21.404 -45.844 -20.606  1.00 24.85 ? 75   LYS G CA  1 
ATOM   6117  C  C   . LYS F  1 75  ? 22.566 -46.702 -21.109  1.00 25.76 ? 75   LYS G C   1 
ATOM   6118  O  O   . LYS F  1 75  ? 23.400 -47.181 -20.326  1.00 25.94 ? 75   LYS G O   1 
ATOM   6119  C  CB  . LYS F  1 75  ? 20.552 -46.612 -19.592  1.00 24.81 ? 75   LYS G CB  1 
ATOM   6120  C  CG  . LYS F  1 75  ? 19.413 -45.799 -18.941  1.00 25.65 ? 75   LYS G CG  1 
ATOM   6121  C  CD  . LYS F  1 75  ? 19.928 -44.557 -18.170  1.00 29.14 ? 75   LYS G CD  1 
ATOM   6122  C  CE  . LYS F  1 75  ? 19.856 -43.269 -19.006  1.00 29.13 ? 75   LYS G CE  1 
ATOM   6123  N  NZ  . LYS F  1 75  ? 20.829 -42.260 -18.498  1.00 30.30 ? 75   LYS G NZ  1 
ATOM   6124  N  N   . ASP F  1 76  ? 22.621 -46.889 -22.420  1.00 26.46 ? 76   ASP G N   1 
ATOM   6125  C  CA  . ASP F  1 76  ? 23.678 -47.678 -23.030  1.00 27.53 ? 76   ASP G CA  1 
ATOM   6126  C  C   . ASP F  1 76  ? 24.935 -46.838 -23.197  1.00 27.59 ? 76   ASP G C   1 
ATOM   6127  O  O   . ASP F  1 76  ? 24.852 -45.633 -23.445  1.00 27.83 ? 76   ASP G O   1 
ATOM   6128  C  CB  . ASP F  1 76  ? 23.216 -48.221 -24.388  1.00 27.69 ? 76   ASP G CB  1 
ATOM   6129  C  CG  . ASP F  1 76  ? 22.148 -49.288 -24.253  1.00 29.53 ? 76   ASP G CG  1 
ATOM   6130  O  OD1 . ASP F  1 76  ? 21.218 -49.318 -25.089  1.00 31.04 ? 76   ASP G OD1 1 
ATOM   6131  O  OD2 . ASP F  1 76  ? 22.235 -50.102 -23.301  1.00 31.21 ? 76   ASP G OD2 1 
ATOM   6132  N  N   . GLU F  1 77  ? 26.090 -47.488 -23.057  1.00 27.73 ? 77   GLU G N   1 
ATOM   6133  C  CA  . GLU F  1 77  ? 27.397 -46.865 -23.285  1.00 27.96 ? 77   GLU G CA  1 
ATOM   6134  C  C   . GLU F  1 77  ? 27.556 -46.538 -24.761  1.00 27.29 ? 77   GLU G C   1 
ATOM   6135  O  O   . GLU F  1 77  ? 28.110 -45.501 -25.121  1.00 27.35 ? 77   GLU G O   1 
ATOM   6136  C  CB  . GLU F  1 77  ? 28.527 -47.802 -22.837  1.00 28.37 ? 77   GLU G CB  1 
ATOM   6137  C  CG  . GLU F  1 77  ? 28.864 -47.774 -21.324  1.00 31.23 ? 77   GLU G CG  1 
ATOM   6138  C  CD  . GLU F  1 77  ? 27.802 -48.411 -20.422  1.00 35.26 ? 77   GLU G CD  1 
ATOM   6139  O  OE1 . GLU F  1 77  ? 27.998 -48.392 -19.183  1.00 35.89 ? 77   GLU G OE1 1 
ATOM   6140  O  OE2 . GLU F  1 77  ? 26.779 -48.932 -20.938  1.00 37.48 ? 77   GLU G OE2 1 
ATOM   6141  N  N   . GLU F  1 78  ? 27.055 -47.435 -25.609  1.00 26.42 ? 78   GLU G N   1 
ATOM   6142  C  CA  . GLU F  1 78  ? 27.063 -47.244 -27.053  1.00 25.55 ? 78   GLU G CA  1 
ATOM   6143  C  C   . GLU F  1 78  ? 25.708 -46.665 -27.450  1.00 24.71 ? 78   GLU G C   1 
ATOM   6144  O  O   . GLU F  1 78  ? 24.678 -47.362 -27.430  1.00 24.73 ? 78   GLU G O   1 
ATOM   6145  C  CB  . GLU F  1 78  ? 27.354 -48.578 -27.749  1.00 25.96 ? 78   GLU G CB  1 
ATOM   6146  C  CG  . GLU F  1 78  ? 27.665 -48.526 -29.249  1.00 28.18 ? 78   GLU G CG  1 
ATOM   6147  C  CD  . GLU F  1 78  ? 28.994 -47.855 -29.591  1.00 31.14 ? 78   GLU G CD  1 
ATOM   6148  O  OE1 . GLU F  1 78  ? 29.209 -47.593 -30.801  1.00 32.25 ? 78   GLU G OE1 1 
ATOM   6149  O  OE2 . GLU F  1 78  ? 29.811 -47.579 -28.672  1.00 31.09 ? 78   GLU G OE2 1 
ATOM   6150  N  N   . ARG F  1 79  ? 25.708 -45.372 -27.755  1.00 22.71 ? 79   ARG G N   1 
ATOM   6151  C  CA  . ARG F  1 79  ? 24.490 -44.660 -28.138  1.00 21.61 ? 79   ARG G CA  1 
ATOM   6152  C  C   . ARG F  1 79  ? 24.859 -43.422 -28.930  1.00 20.56 ? 79   ARG G C   1 
ATOM   6153  O  O   . ARG F  1 79  ? 26.006 -42.951 -28.878  1.00 21.14 ? 79   ARG G O   1 
ATOM   6154  C  CB  . ARG F  1 79  ? 23.655 -44.251 -26.906  1.00 21.23 ? 79   ARG G CB  1 
ATOM   6155  C  CG  . ARG F  1 79  ? 24.383 -43.311 -25.901  1.00 20.85 ? 79   ARG G CG  1 
ATOM   6156  C  CD  . ARG F  1 79  ? 23.412 -42.743 -24.886  1.00 19.50 ? 79   ARG G CD  1 
ATOM   6157  N  NE  . ARG F  1 79  ? 22.848 -41.470 -25.341  1.00 20.38 ? 79   ARG G NE  1 
ATOM   6158  C  CZ  . ARG F  1 79  ? 22.207 -40.612 -24.550  1.00 18.49 ? 79   ARG G CZ  1 
ATOM   6159  N  NH1 . ARG F  1 79  ? 21.743 -39.469 -25.033  1.00 16.39 ? 79   ARG G NH1 1 
ATOM   6160  N  NH2 . ARG F  1 79  ? 22.011 -40.905 -23.276  1.00 20.72 ? 79   ARG G NH2 1 
ATOM   6161  N  N   . HIS F  1 80  ? 23.881 -42.900 -29.662  1.00 19.74 ? 80   HIS G N   1 
ATOM   6162  C  CA  . HIS F  1 80  ? 23.993 -41.571 -30.248  1.00 18.54 ? 80   HIS G CA  1 
ATOM   6163  C  C   . HIS F  1 80  ? 23.662 -40.548 -29.177  1.00 17.96 ? 80   HIS G C   1 
ATOM   6164  O  O   . HIS F  1 80  ? 22.777 -40.781 -28.328  1.00 17.07 ? 80   HIS G O   1 
ATOM   6165  C  CB  . HIS F  1 80  ? 22.998 -41.406 -31.388  1.00 18.64 ? 80   HIS G CB  1 
ATOM   6166  C  CG  . HIS F  1 80  ? 23.140 -42.419 -32.473  1.00 17.91 ? 80   HIS G CG  1 
ATOM   6167  N  ND1 . HIS F  1 80  ? 22.054 -43.032 -33.061  1.00 19.02 ? 80   HIS G ND1 1 
ATOM   6168  C  CD2 . HIS F  1 80  ? 24.234 -42.938 -33.070  1.00 16.89 ? 80   HIS G CD2 1 
ATOM   6169  C  CE1 . HIS F  1 80  ? 22.475 -43.838 -34.017  1.00 19.24 ? 80   HIS G CE1 1 
ATOM   6170  N  NE2 . HIS F  1 80  ? 23.795 -43.814 -34.030  1.00 17.33 ? 80   HIS G NE2 1 
ATOM   6171  N  N   . VAL F  1 81  ? 24.360 -39.410 -29.216  1.00 17.00 ? 81   VAL G N   1 
ATOM   6172  C  CA  . VAL F  1 81  ? 24.098 -38.333 -28.265  1.00 16.86 ? 81   VAL G CA  1 
ATOM   6173  C  C   . VAL F  1 81  ? 22.591 -38.059 -28.254  1.00 16.76 ? 81   VAL G C   1 
ATOM   6174  O  O   . VAL F  1 81  ? 21.987 -37.874 -27.196  1.00 16.53 ? 81   VAL G O   1 
ATOM   6175  C  CB  . VAL F  1 81  ? 24.921 -37.068 -28.638  1.00 17.19 ? 81   VAL G CB  1 
ATOM   6176  C  CG1 . VAL F  1 81  ? 24.451 -35.828 -27.868  1.00 15.95 ? 81   VAL G CG1 1 
ATOM   6177  C  CG2 . VAL F  1 81  ? 26.421 -37.323 -28.399  1.00 17.06 ? 81   VAL G CG2 1 
ATOM   6178  N  N   . GLY F  1 82  ? 21.971 -38.111 -29.430  1.00 16.07 ? 82   GLY G N   1 
ATOM   6179  C  CA  . GLY F  1 82  ? 20.544 -37.800 -29.537  1.00 16.90 ? 82   GLY G CA  1 
ATOM   6180  C  C   . GLY F  1 82  ? 19.561 -38.847 -29.046  1.00 16.96 ? 82   GLY G C   1 
ATOM   6181  O  O   . GLY F  1 82  ? 18.358 -38.596 -29.022  1.00 18.01 ? 82   GLY G O   1 
ATOM   6182  N  N   . ASP F  1 83  ? 20.060 -40.001 -28.621  1.00 16.95 ? 83   ASP G N   1 
ATOM   6183  C  CA  . ASP F  1 83  ? 19.202 -41.135 -28.214  1.00 17.10 ? 83   ASP G CA  1 
ATOM   6184  C  C   . ASP F  1 83  ? 18.564 -41.003 -26.826  1.00 17.47 ? 83   ASP G C   1 
ATOM   6185  O  O   . ASP F  1 83  ? 19.184 -41.352 -25.826  1.00 17.61 ? 83   ASP G O   1 
ATOM   6186  C  CB  . ASP F  1 83  ? 20.003 -42.440 -28.321  1.00 16.52 ? 83   ASP G CB  1 
ATOM   6187  C  CG  . ASP F  1 83  ? 20.365 -42.782 -29.751  1.00 16.08 ? 83   ASP G CG  1 
ATOM   6188  O  OD1 . ASP F  1 83  ? 19.789 -42.144 -30.654  1.00 14.07 ? 83   ASP G OD1 1 
ATOM   6189  O  OD2 . ASP F  1 83  ? 21.223 -43.681 -29.976  1.00 14.11 ? 83   ASP G OD2 1 
ATOM   6190  N  N   . LEU F  1 84  ? 17.328 -40.493 -26.779  1.00 17.78 ? 84   LEU G N   1 
ATOM   6191  C  CA  . LEU F  1 84  ? 16.605 -40.268 -25.525  1.00 18.33 ? 84   LEU G CA  1 
ATOM   6192  C  C   . LEU F  1 84  ? 15.513 -41.326 -25.332  1.00 19.15 ? 84   LEU G C   1 
ATOM   6193  O  O   . LEU F  1 84  ? 14.572 -41.140 -24.530  1.00 18.81 ? 84   LEU G O   1 
ATOM   6194  C  CB  . LEU F  1 84  ? 15.997 -38.849 -25.483  1.00 18.32 ? 84   LEU G CB  1 
ATOM   6195  C  CG  . LEU F  1 84  ? 17.002 -37.681 -25.481  1.00 19.10 ? 84   LEU G CG  1 
ATOM   6196  C  CD1 . LEU F  1 84  ? 16.283 -36.331 -25.448  1.00 19.77 ? 84   LEU G CD1 1 
ATOM   6197  C  CD2 . LEU F  1 84  ? 17.989 -37.782 -24.320  1.00 20.01 ? 84   LEU G CD2 1 
ATOM   6198  N  N   . GLY F  1 85  ? 15.645 -42.424 -26.085  1.00 19.35 ? 85   GLY G N   1 
ATOM   6199  C  CA  . GLY F  1 85  ? 14.828 -43.620 -25.893  1.00 20.13 ? 85   GLY G CA  1 
ATOM   6200  C  C   . GLY F  1 85  ? 13.368 -43.470 -26.264  1.00 20.65 ? 85   GLY G C   1 
ATOM   6201  O  O   . GLY F  1 85  ? 13.029 -43.023 -27.373  1.00 21.01 ? 85   GLY G O   1 
ATOM   6202  N  N   . ASN F  1 86  ? 12.500 -43.853 -25.334  1.00 20.58 ? 86   ASN G N   1 
ATOM   6203  C  CA  . ASN F  1 86  ? 11.065 -43.861 -25.587  1.00 20.91 ? 86   ASN G CA  1 
ATOM   6204  C  C   . ASN F  1 86  ? 10.294 -42.956 -24.641  1.00 20.85 ? 86   ASN G C   1 
ATOM   6205  O  O   . ASN F  1 86  ? 10.637 -42.856 -23.479  1.00 21.11 ? 86   ASN G O   1 
ATOM   6206  C  CB  . ASN F  1 86  ? 10.525 -45.296 -25.474  1.00 20.88 ? 86   ASN G CB  1 
ATOM   6207  C  CG  . ASN F  1 86  ? 10.981 -46.191 -26.627  1.00 20.87 ? 86   ASN G CG  1 
ATOM   6208  O  OD1 . ASN F  1 86  ? 10.538 -46.025 -27.768  1.00 20.58 ? 86   ASN G OD1 1 
ATOM   6209  N  ND2 . ASN F  1 86  ? 11.871 -47.145 -26.330  1.00 20.87 ? 86   ASN G ND2 1 
ATOM   6210  N  N   . VAL F  1 87  ? 9.261  -42.291 -25.146  1.00 21.08 ? 87   VAL G N   1 
ATOM   6211  C  CA  . VAL F  1 87  ? 8.247  -41.694 -24.270  1.00 21.62 ? 87   VAL G CA  1 
ATOM   6212  C  C   . VAL F  1 87  ? 7.001  -42.583 -24.303  1.00 22.40 ? 87   VAL G C   1 
ATOM   6213  O  O   . VAL F  1 87  ? 6.772  -43.292 -25.292  1.00 22.25 ? 87   VAL G O   1 
ATOM   6214  C  CB  . VAL F  1 87  ? 7.897  -40.224 -24.637  1.00 21.40 ? 87   VAL G CB  1 
ATOM   6215  C  CG1 . VAL F  1 87  ? 9.141  -39.340 -24.527  1.00 20.21 ? 87   VAL G CG1 1 
ATOM   6216  C  CG2 . VAL F  1 87  ? 7.259  -40.111 -26.023  1.00 21.41 ? 87   VAL G CG2 1 
ATOM   6217  N  N   . THR F  1 88  ? 6.211  -42.559 -23.227  1.00 23.46 ? 88   THR G N   1 
ATOM   6218  C  CA  . THR F  1 88  ? 5.037  -43.438 -23.117  1.00 24.59 ? 88   THR G CA  1 
ATOM   6219  C  C   . THR F  1 88  ? 3.727  -42.644 -23.096  1.00 24.94 ? 88   THR G C   1 
ATOM   6220  O  O   . THR F  1 88  ? 3.517  -41.814 -22.218  1.00 25.56 ? 88   THR G O   1 
ATOM   6221  C  CB  . THR F  1 88  ? 5.123  -44.347 -21.867  1.00 24.81 ? 88   THR G CB  1 
ATOM   6222  O  OG1 . THR F  1 88  ? 6.415  -44.967 -21.795  1.00 26.11 ? 88   THR G OG1 1 
ATOM   6223  C  CG2 . THR F  1 88  ? 4.033  -45.434 -21.904  1.00 24.42 ? 88   THR G CG2 1 
ATOM   6224  N  N   . ALA F  1 89  ? 2.861  -42.891 -24.076  1.00 25.73 ? 89   ALA G N   1 
ATOM   6225  C  CA  . ALA F  1 89  ? 1.526  -42.287 -24.107  1.00 26.75 ? 89   ALA G CA  1 
ATOM   6226  C  C   . ALA F  1 89  ? 0.509  -43.159 -23.369  1.00 27.32 ? 89   ALA G C   1 
ATOM   6227  O  O   . ALA F  1 89  ? 0.619  -44.385 -23.390  1.00 27.56 ? 89   ALA G O   1 
ATOM   6228  C  CB  . ALA F  1 89  ? 1.074  -42.050 -25.544  1.00 26.46 ? 89   ALA G CB  1 
ATOM   6229  N  N   . ASP F  1 90  ? -0.477 -42.522 -22.732  1.00 28.09 ? 90   ASP G N   1 
ATOM   6230  C  CA  . ASP F  1 90  ? -1.559 -43.251 -22.058  1.00 29.17 ? 90   ASP G CA  1 
ATOM   6231  C  C   . ASP F  1 90  ? -2.721 -43.495 -23.024  1.00 29.56 ? 90   ASP G C   1 
ATOM   6232  O  O   . ASP F  1 90  ? -2.606 -43.197 -24.218  1.00 29.76 ? 90   ASP G O   1 
ATOM   6233  C  CB  . ASP F  1 90  ? -2.029 -42.501 -20.802  1.00 28.93 ? 90   ASP G CB  1 
ATOM   6234  C  CG  . ASP F  1 90  ? -2.597 -41.124 -21.116  1.00 29.40 ? 90   ASP G CG  1 
ATOM   6235  O  OD1 . ASP F  1 90  ? -2.619 -40.272 -20.206  1.00 29.88 ? 90   ASP G OD1 1 
ATOM   6236  O  OD2 . ASP F  1 90  ? -3.023 -40.890 -22.266  1.00 29.56 ? 90   ASP G OD2 1 
ATOM   6237  N  N   . LYS F  1 91  ? -3.836 -44.018 -22.512  1.00 30.36 ? 91   LYS G N   1 
ATOM   6238  C  CA  . LYS F  1 91  ? -5.012 -44.316 -23.356  1.00 31.25 ? 91   LYS G CA  1 
ATOM   6239  C  C   . LYS F  1 91  ? -5.721 -43.064 -23.889  1.00 31.68 ? 91   LYS G C   1 
ATOM   6240  O  O   . LYS F  1 91  ? -6.467 -43.142 -24.877  1.00 32.14 ? 91   LYS G O   1 
ATOM   6241  C  CB  . LYS F  1 91  ? -6.007 -45.256 -22.649  1.00 31.36 ? 91   LYS G CB  1 
ATOM   6242  C  CG  . LYS F  1 91  ? -6.378 -44.854 -21.232  1.00 32.37 ? 91   LYS G CG  1 
ATOM   6243  C  CD  . LYS F  1 91  ? -7.263 -45.906 -20.558  1.00 33.67 ? 91   LYS G CD  1 
ATOM   6244  C  CE  . LYS F  1 91  ? -6.990 -45.972 -19.056  1.00 34.48 ? 91   LYS G CE  1 
ATOM   6245  N  NZ  . LYS F  1 91  ? -6.943 -44.621 -18.410  1.00 34.79 ? 91   LYS G NZ  1 
ATOM   6246  N  N   . ASP F  1 92  ? -5.477 -41.924 -23.242  1.00 31.95 ? 92   ASP G N   1 
ATOM   6247  C  CA  . ASP F  1 92  ? -5.953 -40.615 -23.714  1.00 32.39 ? 92   ASP G CA  1 
ATOM   6248  C  C   . ASP F  1 92  ? -5.039 -40.084 -24.828  1.00 32.18 ? 92   ASP G C   1 
ATOM   6249  O  O   . ASP F  1 92  ? -5.359 -39.096 -25.493  1.00 32.19 ? 92   ASP G O   1 
ATOM   6250  C  CB  . ASP F  1 92  ? -5.990 -39.607 -22.559  1.00 32.45 ? 92   ASP G CB  1 
ATOM   6251  C  CG  . ASP F  1 92  ? -6.929 -40.025 -21.435  1.00 33.72 ? 92   ASP G CG  1 
ATOM   6252  O  OD1 . ASP F  1 92  ? -6.542 -39.879 -20.255  1.00 34.81 ? 92   ASP G OD1 1 
ATOM   6253  O  OD2 . ASP F  1 92  ? -8.054 -40.490 -21.723  1.00 34.39 ? 92   ASP G OD2 1 
ATOM   6254  N  N   . GLY F  1 93  ? -3.900 -40.750 -25.018  1.00 31.99 ? 93   GLY G N   1 
ATOM   6255  C  CA  . GLY F  1 93  ? -2.936 -40.380 -26.047  1.00 31.79 ? 93   GLY G CA  1 
ATOM   6256  C  C   . GLY F  1 93  ? -1.950 -39.304 -25.612  1.00 31.70 ? 93   GLY G C   1 
ATOM   6257  O  O   . GLY F  1 93  ? -1.291 -38.689 -26.453  1.00 31.49 ? 93   GLY G O   1 
ATOM   6258  N  N   . VAL F  1 94  ? -1.845 -39.091 -24.300  1.00 31.44 ? 94   VAL G N   1 
ATOM   6259  C  CA  . VAL F  1 94  ? -0.953 -38.078 -23.741  1.00 31.38 ? 94   VAL G CA  1 
ATOM   6260  C  C   . VAL F  1 94  ? 0.289  -38.727 -23.131  1.00 31.10 ? 94   VAL G C   1 
ATOM   6261  O  O   . VAL F  1 94  ? 0.183  -39.641 -22.317  1.00 30.98 ? 94   VAL G O   1 
ATOM   6262  C  CB  . VAL F  1 94  ? -1.682 -37.181 -22.684  1.00 31.59 ? 94   VAL G CB  1 
ATOM   6263  C  CG1 . VAL F  1 94  ? -0.703 -36.241 -21.985  1.00 31.13 ? 94   VAL G CG1 1 
ATOM   6264  C  CG2 . VAL F  1 94  ? -2.809 -36.374 -23.336  1.00 31.69 ? 94   VAL G CG2 1 
ATOM   6265  N  N   . ALA F  1 95  ? 1.462  -38.260 -23.548  1.00 30.63 ? 95   ALA G N   1 
ATOM   6266  C  CA  . ALA F  1 95  ? 2.717  -38.665 -22.934  1.00 30.38 ? 95   ALA G CA  1 
ATOM   6267  C  C   . ALA F  1 95  ? 3.192  -37.553 -22.009  1.00 30.40 ? 95   ALA G C   1 
ATOM   6268  O  O   . ALA F  1 95  ? 3.355  -36.410 -22.442  1.00 30.64 ? 95   ALA G O   1 
ATOM   6269  C  CB  . ALA F  1 95  ? 3.773  -38.961 -23.995  1.00 30.63 ? 95   ALA G CB  1 
ATOM   6270  N  N   . ASP F  1 96  ? 3.376  -37.890 -20.735  1.00 29.88 ? 96   ASP G N   1 
ATOM   6271  C  CA  . ASP F  1 96  ? 3.962  -36.979 -19.754  1.00 29.58 ? 96   ASP G CA  1 
ATOM   6272  C  C   . ASP F  1 96  ? 5.477  -37.202 -19.755  1.00 28.62 ? 96   ASP G C   1 
ATOM   6273  O  O   . ASP F  1 96  ? 5.982  -38.150 -19.155  1.00 28.47 ? 96   ASP G O   1 
ATOM   6274  C  CB  . ASP F  1 96  ? 3.348  -37.238 -18.367  1.00 30.05 ? 96   ASP G CB  1 
ATOM   6275  C  CG  . ASP F  1 96  ? 3.800  -36.239 -17.310  1.00 32.22 ? 96   ASP G CG  1 
ATOM   6276  O  OD1 . ASP F  1 96  ? 4.953  -35.756 -17.366  1.00 34.70 ? 96   ASP G OD1 1 
ATOM   6277  O  OD2 . ASP F  1 96  ? 2.994  -35.954 -16.393  1.00 34.21 ? 96   ASP G OD2 1 
ATOM   6278  N  N   . VAL F  1 97  ? 6.204  -36.325 -20.439  1.00 27.39 ? 97   VAL G N   1 
ATOM   6279  C  CA  . VAL F  1 97  ? 7.637  -36.537 -20.609  1.00 26.26 ? 97   VAL G CA  1 
ATOM   6280  C  C   . VAL F  1 97  ? 8.418  -36.018 -19.399  1.00 25.61 ? 97   VAL G C   1 
ATOM   6281  O  O   . VAL F  1 97  ? 8.199  -34.907 -18.935  1.00 24.99 ? 97   VAL G O   1 
ATOM   6282  C  CB  . VAL F  1 97  ? 8.177  -35.940 -21.938  1.00 26.22 ? 97   VAL G CB  1 
ATOM   6283  C  CG1 . VAL F  1 97  ? 9.610  -36.377 -22.156  1.00 26.38 ? 97   VAL G CG1 1 
ATOM   6284  C  CG2 . VAL F  1 97  ? 7.314  -36.381 -23.127  1.00 25.70 ? 97   VAL G CG2 1 
ATOM   6285  N  N   . SER F  1 98  ? 9.316  -36.855 -18.888  1.00 25.13 ? 98   SER G N   1 
ATOM   6286  C  CA  . SER F  1 98  ? 10.142 -36.511 -17.737  1.00 24.56 ? 98   SER G CA  1 
ATOM   6287  C  C   . SER F  1 98  ? 11.389 -37.377 -17.814  1.00 24.15 ? 98   SER G C   1 
ATOM   6288  O  O   . SER F  1 98  ? 11.345 -38.598 -17.585  1.00 24.21 ? 98   SER G O   1 
ATOM   6289  C  CB  . SER F  1 98  ? 9.384  -36.762 -16.426  1.00 25.01 ? 98   SER G CB  1 
ATOM   6290  O  OG  . SER F  1 98  ? 9.977  -36.059 -15.351  1.00 24.65 ? 98   SER G OG  1 
ATOM   6291  N  N   . ILE F  1 99  ? 12.495 -36.738 -18.168  1.00 23.03 ? 99   ILE G N   1 
ATOM   6292  C  CA  . ILE F  1 99  ? 13.749 -37.411 -18.448  1.00 22.22 ? 99   ILE G CA  1 
ATOM   6293  C  C   . ILE F  1 99  ? 14.880 -36.593 -17.842  1.00 22.05 ? 99   ILE G C   1 
ATOM   6294  O  O   . ILE F  1 99  ? 14.855 -35.368 -17.890  1.00 21.60 ? 99   ILE G O   1 
ATOM   6295  C  CB  . ILE F  1 99  ? 13.973 -37.508 -19.997  1.00 22.06 ? 99   ILE G CB  1 
ATOM   6296  C  CG1 . ILE F  1 99  ? 13.043 -38.549 -20.625  1.00 21.92 ? 99   ILE G CG1 1 
ATOM   6297  C  CG2 . ILE F  1 99  ? 15.445 -37.793 -20.343  1.00 21.55 ? 99   ILE G CG2 1 
ATOM   6298  C  CD1 . ILE F  1 99  ? 12.873 -38.412 -22.140  1.00 22.66 ? 99   ILE G CD1 1 
ATOM   6299  N  N   . GLU F  1 100 ? 15.875 -37.273 -17.282  1.00 21.88 ? 100  GLU G N   1 
ATOM   6300  C  CA  . GLU F  1 100 ? 17.148 -36.630 -17.002  1.00 21.43 ? 100  GLU G CA  1 
ATOM   6301  C  C   . GLU F  1 100 ? 18.216 -37.343 -17.798  1.00 21.04 ? 100  GLU G C   1 
ATOM   6302  O  O   . GLU F  1 100 ? 18.297 -38.580 -17.771  1.00 20.62 ? 100  GLU G O   1 
ATOM   6303  C  CB  . GLU F  1 100 ? 17.489 -36.660 -15.514  1.00 22.16 ? 100  GLU G CB  1 
ATOM   6304  C  CG  . GLU F  1 100 ? 18.707 -35.801 -15.187  1.00 25.14 ? 100  GLU G CG  1 
ATOM   6305  C  CD  . GLU F  1 100 ? 18.730 -35.305 -13.759  1.00 30.04 ? 100  GLU G CD  1 
ATOM   6306  O  OE1 . GLU F  1 100 ? 19.587 -34.446 -13.460  1.00 32.28 ? 100  GLU G OE1 1 
ATOM   6307  O  OE2 . GLU F  1 100 ? 17.909 -35.761 -12.933  1.00 31.13 ? 100  GLU G OE2 1 
ATOM   6308  N  N   . ASP F  1 101 ? 19.015 -36.569 -18.529  1.00 19.89 ? 101  ASP G N   1 
ATOM   6309  C  CA  . ASP F  1 101 ? 20.065 -37.128 -19.372  1.00 19.85 ? 101  ASP G CA  1 
ATOM   6310  C  C   . ASP F  1 101 ? 21.392 -36.435 -19.118  1.00 19.88 ? 101  ASP G C   1 
ATOM   6311  O  O   . ASP F  1 101 ? 21.444 -35.209 -18.930  1.00 19.35 ? 101  ASP G O   1 
ATOM   6312  C  CB  . ASP F  1 101 ? 19.685 -37.055 -20.865  1.00 19.55 ? 101  ASP G CB  1 
ATOM   6313  C  CG  . ASP F  1 101 ? 20.480 -38.032 -21.718  1.00 19.72 ? 101  ASP G CG  1 
ATOM   6314  O  OD1 . ASP F  1 101 ? 21.400 -37.612 -22.454  1.00 19.71 ? 101  ASP G OD1 1 
ATOM   6315  O  OD2 . ASP F  1 101 ? 20.189 -39.238 -21.645  1.00 20.71 ? 101  ASP G OD2 1 
ATOM   6316  N  N   . SER F  1 102 ? 22.452 -37.233 -19.100  1.00 19.64 ? 102  SER G N   1 
ATOM   6317  C  CA  . SER F  1 102 ? 23.803 -36.749 -18.843  1.00 19.83 ? 102  SER G CA  1 
ATOM   6318  C  C   . SER F  1 102 ? 24.689 -36.774 -20.081  1.00 19.31 ? 102  SER G C   1 
ATOM   6319  O  O   . SER F  1 102 ? 25.888 -36.490 -19.996  1.00 19.71 ? 102  SER G O   1 
ATOM   6320  C  CB  . SER F  1 102 ? 24.453 -37.604 -17.747  1.00 20.35 ? 102  SER G CB  1 
ATOM   6321  O  OG  . SER F  1 102 ? 24.111 -37.112 -16.463  1.00 24.03 ? 102  SER G OG  1 
ATOM   6322  N  N   . VAL F  1 103 ? 24.116 -37.118 -21.234  1.00 18.58 ? 103  VAL G N   1 
ATOM   6323  C  CA  . VAL F  1 103 ? 24.894 -37.141 -22.474  1.00 17.69 ? 103  VAL G CA  1 
ATOM   6324  C  C   . VAL F  1 103 ? 24.642 -35.869 -23.306  1.00 17.66 ? 103  VAL G C   1 
ATOM   6325  O  O   . VAL F  1 103 ? 25.590 -35.168 -23.668  1.00 17.97 ? 103  VAL G O   1 
ATOM   6326  C  CB  . VAL F  1 103 ? 24.657 -38.442 -23.291  1.00 17.72 ? 103  VAL G CB  1 
ATOM   6327  C  CG1 . VAL F  1 103 ? 25.395 -38.377 -24.622  1.00 16.62 ? 103  VAL G CG1 1 
ATOM   6328  C  CG2 . VAL F  1 103 ? 25.118 -39.675 -22.484  1.00 17.39 ? 103  VAL G CG2 1 
ATOM   6329  N  N   . ILE F  1 104 ? 23.375 -35.564 -23.581  1.00 16.96 ? 104  ILE G N   1 
ATOM   6330  C  CA  . ILE F  1 104 ? 23.016 -34.331 -24.273  1.00 16.69 ? 104  ILE G CA  1 
ATOM   6331  C  C   . ILE F  1 104 ? 23.439 -33.127 -23.444  1.00 16.62 ? 104  ILE G C   1 
ATOM   6332  O  O   . ILE F  1 104 ? 23.465 -33.193 -22.229  1.00 16.06 ? 104  ILE G O   1 
ATOM   6333  C  CB  . ILE F  1 104 ? 21.487 -34.216 -24.543  1.00 16.73 ? 104  ILE G CB  1 
ATOM   6334  C  CG1 . ILE F  1 104 ? 20.679 -34.206 -23.235  1.00 17.06 ? 104  ILE G CG1 1 
ATOM   6335  C  CG2 . ILE F  1 104 ? 21.009 -35.333 -25.478  1.00 17.32 ? 104  ILE G CG2 1 
ATOM   6336  C  CD1 . ILE F  1 104 ? 19.238 -33.747 -23.411  1.00 17.56 ? 104  ILE G CD1 1 
ATOM   6337  N  N   . SER F  1 105 ? 23.800 -32.037 -24.106  1.00 16.27 ? 105  SER G N   1 
ATOM   6338  C  CA  . SER F  1 105 ? 24.089 -30.796 -23.399  1.00 16.89 ? 105  SER G CA  1 
ATOM   6339  C  C   . SER F  1 105 ? 23.363 -29.613 -24.055  1.00 16.73 ? 105  SER G C   1 
ATOM   6340  O  O   . SER F  1 105 ? 22.892 -29.730 -25.192  1.00 16.42 ? 105  SER G O   1 
ATOM   6341  C  CB  . SER F  1 105 ? 25.591 -30.566 -23.355  1.00 15.87 ? 105  SER G CB  1 
ATOM   6342  O  OG  . SER F  1 105 ? 25.879 -29.502 -22.481  1.00 17.26 ? 105  SER G OG  1 
ATOM   6343  N  N   . LEU F  1 106 ? 23.238 -28.499 -23.331  1.00 17.34 ? 106  LEU G N   1 
ATOM   6344  C  CA  . LEU F  1 106 ? 22.707 -27.251 -23.934  1.00 16.99 ? 106  LEU G CA  1 
ATOM   6345  C  C   . LEU F  1 106 ? 23.828 -26.251 -24.273  1.00 17.80 ? 106  LEU G C   1 
ATOM   6346  O  O   . LEU F  1 106 ? 23.569 -25.095 -24.657  1.00 17.13 ? 106  LEU G O   1 
ATOM   6347  C  CB  . LEU F  1 106 ? 21.628 -26.608 -23.033  1.00 16.86 ? 106  LEU G CB  1 
ATOM   6348  C  CG  . LEU F  1 106 ? 20.418 -27.445 -22.577  1.00 15.29 ? 106  LEU G CG  1 
ATOM   6349  C  CD1 . LEU F  1 106 ? 19.431 -26.585 -21.793  1.00 12.34 ? 106  LEU G CD1 1 
ATOM   6350  C  CD2 . LEU F  1 106 ? 19.697 -28.175 -23.760  1.00 13.60 ? 106  LEU G CD2 1 
ATOM   6351  N  N   . SER F  1 107 ? 25.069 -26.703 -24.124  1.00 18.28 ? 107  SER G N   1 
ATOM   6352  C  CA  . SER F  1 107 ? 26.241 -25.902 -24.443  1.00 19.64 ? 107  SER G CA  1 
ATOM   6353  C  C   . SER F  1 107 ? 27.417 -26.826 -24.761  1.00 20.54 ? 107  SER G C   1 
ATOM   6354  O  O   . SER F  1 107 ? 27.321 -28.043 -24.615  1.00 20.38 ? 107  SER G O   1 
ATOM   6355  C  CB  . SER F  1 107 ? 26.596 -24.982 -23.267  1.00 19.56 ? 107  SER G CB  1 
ATOM   6356  O  OG  . SER F  1 107 ? 27.225 -25.719 -22.231  1.00 20.72 ? 107  SER G OG  1 
ATOM   6357  N  N   . GLY F  1 108 ? 28.534 -26.237 -25.184  1.00 21.45 ? 108  GLY G N   1 
ATOM   6358  C  CA  . GLY F  1 108 ? 29.715 -27.002 -25.556  1.00 22.42 ? 108  GLY G CA  1 
ATOM   6359  C  C   . GLY F  1 108 ? 29.619 -27.314 -27.025  1.00 23.47 ? 108  GLY G C   1 
ATOM   6360  O  O   . GLY F  1 108 ? 28.537 -27.218 -27.609  1.00 23.74 ? 108  GLY G O   1 
ATOM   6361  N  N   . ASP F  1 109 ? 30.727 -27.723 -27.630  1.00 24.14 ? 109  ASP G N   1 
ATOM   6362  C  CA  . ASP F  1 109 ? 30.741 -27.841 -29.086  1.00 25.43 ? 109  ASP G CA  1 
ATOM   6363  C  C   . ASP F  1 109 ? 29.904 -29.004 -29.652  1.00 25.11 ? 109  ASP G C   1 
ATOM   6364  O  O   . ASP F  1 109 ? 29.805 -29.150 -30.877  1.00 25.65 ? 109  ASP G O   1 
ATOM   6365  C  CB  . ASP F  1 109 ? 32.172 -27.789 -29.652  1.00 26.08 ? 109  ASP G CB  1 
ATOM   6366  C  CG  . ASP F  1 109 ? 32.999 -29.005 -29.292  1.00 28.95 ? 109  ASP G CG  1 
ATOM   6367  O  OD1 . ASP F  1 109 ? 34.050 -29.196 -29.937  1.00 32.14 ? 109  ASP G OD1 1 
ATOM   6368  O  OD2 . ASP F  1 109 ? 32.618 -29.760 -28.369  1.00 32.31 ? 109  ASP G OD2 1 
ATOM   6369  N  N   . HIS F  1 110 ? 29.304 -29.807 -28.761  1.00 24.38 ? 110  HIS G N   1 
ATOM   6370  C  CA  . HIS F  1 110 ? 28.326 -30.827 -29.152  1.00 23.49 ? 110  HIS G CA  1 
ATOM   6371  C  C   . HIS F  1 110 ? 26.892 -30.564 -28.617  1.00 23.35 ? 110  HIS G C   1 
ATOM   6372  O  O   . HIS F  1 110 ? 26.109 -31.494 -28.440  1.00 23.20 ? 110  HIS G O   1 
ATOM   6373  C  CB  . HIS F  1 110 ? 28.811 -32.232 -28.755  1.00 23.60 ? 110  HIS G CB  1 
ATOM   6374  C  CG  . HIS F  1 110 ? 30.084 -32.656 -29.430  1.00 23.44 ? 110  HIS G CG  1 
ATOM   6375  N  ND1 . HIS F  1 110 ? 30.919 -33.624 -28.910  1.00 22.03 ? 110  HIS G ND1 1 
ATOM   6376  C  CD2 . HIS F  1 110 ? 30.666 -32.245 -30.584  1.00 24.74 ? 110  HIS G CD2 1 
ATOM   6377  C  CE1 . HIS F  1 110 ? 31.964 -33.779 -29.704  1.00 23.09 ? 110  HIS G CE1 1 
ATOM   6378  N  NE2 . HIS F  1 110 ? 31.834 -32.956 -30.730  1.00 24.32 ? 110  HIS G NE2 1 
HETATM 6379  N  N   . CME F  1 111 ? 26.541 -29.304 -28.373  1.00 22.19 ? 111  CME G N   1 
HETATM 6380  C  CA  . CME F  1 111 ? 25.192 -28.972 -27.899  1.00 21.73 ? 111  CME G CA  1 
HETATM 6381  C  CB  . CME F  1 111 ? 25.179 -27.484 -27.544  1.00 22.26 ? 111  CME G CB  1 
HETATM 6382  S  SG  . CME F  1 111 ? 24.997 -26.461 -28.972  1.00 26.29 ? 111  CME G SG  1 
HETATM 6383  S  SD  . CME F  1 111 ? 25.134 -24.580 -28.271  1.00 27.60 ? 111  CME G SD  1 
HETATM 6384  C  CE  . CME F  1 111 ? 26.892 -24.347 -28.194  1.00 30.38 ? 111  CME G CE  1 
HETATM 6385  C  CZ  . CME F  1 111 ? 27.610 -24.633 -29.525  1.00 32.64 ? 111  CME G CZ  1 
HETATM 6386  O  OH  . CME F  1 111 ? 27.340 -23.620 -30.516  1.00 33.39 ? 111  CME G OH  1 
HETATM 6387  C  C   . CME F  1 111 ? 24.075 -29.304 -28.866  1.00 20.70 ? 111  CME G C   1 
HETATM 6388  O  O   . CME F  1 111 ? 24.312 -29.499 -30.067  1.00 20.99 ? 111  CME G O   1 
ATOM   6389  N  N   . ILE F  1 112 ? 22.849 -29.359 -28.355  1.00 19.24 ? 112  ILE G N   1 
ATOM   6390  C  CA  . ILE F  1 112 ? 21.673 -29.720 -29.152  1.00 17.87 ? 112  ILE G CA  1 
ATOM   6391  C  C   . ILE F  1 112 ? 20.771 -28.520 -29.475  1.00 17.66 ? 112  ILE G C   1 
ATOM   6392  O  O   . ILE F  1 112 ? 19.714 -28.680 -30.109  1.00 17.18 ? 112  ILE G O   1 
ATOM   6393  C  CB  . ILE F  1 112 ? 20.815 -30.809 -28.433  1.00 17.51 ? 112  ILE G CB  1 
ATOM   6394  C  CG1 . ILE F  1 112 ? 20.160 -30.230 -27.167  1.00 17.69 ? 112  ILE G CG1 1 
ATOM   6395  C  CG2 . ILE F  1 112 ? 21.668 -32.064 -28.142  1.00 17.33 ? 112  ILE G CG2 1 
ATOM   6396  C  CD1 . ILE F  1 112 ? 19.112 -31.145 -26.516  1.00 15.18 ? 112  ILE G CD1 1 
ATOM   6397  N  N   . ILE F  1 113 ? 21.156 -27.328 -29.009  1.00 17.11 ? 113  ILE G N   1 
ATOM   6398  C  CA  . ILE F  1 113 ? 20.458 -26.108 -29.433  1.00 16.55 ? 113  ILE G CA  1 
ATOM   6399  C  C   . ILE F  1 113 ? 20.591 -25.959 -30.965  1.00 15.97 ? 113  ILE G C   1 
ATOM   6400  O  O   . ILE F  1 113 ? 21.643 -26.255 -31.546  1.00 14.66 ? 113  ILE G O   1 
ATOM   6401  C  CB  . ILE F  1 113 ? 20.907 -24.867 -28.598  1.00 17.29 ? 113  ILE G CB  1 
ATOM   6402  C  CG1 . ILE F  1 113 ? 20.349 -25.021 -27.158  1.00 17.70 ? 113  ILE G CG1 1 
ATOM   6403  C  CG2 . ILE F  1 113 ? 20.440 -23.545 -29.249  1.00 15.83 ? 113  ILE G CG2 1 
ATOM   6404  C  CD1 . ILE F  1 113 ? 20.725 -23.929 -26.183  1.00 22.99 ? 113  ILE G CD1 1 
ATOM   6405  N  N   . GLY F  1 114 ? 19.492 -25.564 -31.614  1.00 16.13 ? 114  GLY G N   1 
ATOM   6406  C  CA  . GLY F  1 114 ? 19.451 -25.421 -33.086  1.00 15.53 ? 114  GLY G CA  1 
ATOM   6407  C  C   . GLY F  1 114 ? 19.257 -26.737 -33.840  1.00 16.11 ? 114  GLY G C   1 
ATOM   6408  O  O   . GLY F  1 114 ? 19.179 -26.745 -35.077  1.00 15.30 ? 114  GLY G O   1 
ATOM   6409  N  N   . ARG F  1 115 ? 19.185 -27.844 -33.100  1.00 16.07 ? 115  ARG G N   1 
ATOM   6410  C  CA  . ARG F  1 115 ? 18.859 -29.160 -33.679  1.00 16.82 ? 115  ARG G CA  1 
ATOM   6411  C  C   . ARG F  1 115 ? 17.369 -29.474 -33.538  1.00 16.93 ? 115  ARG G C   1 
ATOM   6412  O  O   . ARG F  1 115 ? 16.597 -28.623 -33.101  1.00 17.22 ? 115  ARG G O   1 
ATOM   6413  C  CB  . ARG F  1 115 ? 19.766 -30.255 -33.107  1.00 16.32 ? 115  ARG G CB  1 
ATOM   6414  C  CG  . ARG F  1 115 ? 21.210 -29.847 -33.200  1.00 17.28 ? 115  ARG G CG  1 
ATOM   6415  C  CD  . ARG F  1 115 ? 22.211 -30.958 -33.063  1.00 18.11 ? 115  ARG G CD  1 
ATOM   6416  N  NE  . ARG F  1 115 ? 23.562 -30.380 -33.138  1.00 18.33 ? 115  ARG G NE  1 
ATOM   6417  C  CZ  . ARG F  1 115 ? 24.321 -30.336 -34.228  1.00 19.62 ? 115  ARG G CZ  1 
ATOM   6418  N  NH1 . ARG F  1 115 ? 25.526 -29.780 -34.158  1.00 20.72 ? 115  ARG G NH1 1 
ATOM   6419  N  NH2 . ARG F  1 115 ? 23.899 -30.858 -35.380  1.00 16.11 ? 115  ARG G NH2 1 
ATOM   6420  N  N   . THR F  1 116 ? 16.950 -30.679 -33.929  1.00 17.78 ? 116  THR G N   1 
ATOM   6421  C  CA  . THR F  1 116 ? 15.519 -30.995 -33.985  1.00 17.24 ? 116  THR G CA  1 
ATOM   6422  C  C   . THR F  1 116 ? 15.155 -32.119 -33.010  1.00 17.32 ? 116  THR G C   1 
ATOM   6423  O  O   . THR F  1 116 ? 15.823 -33.146 -32.967  1.00 16.90 ? 116  THR G O   1 
ATOM   6424  C  CB  . THR F  1 116 ? 15.054 -31.344 -35.441  1.00 17.88 ? 116  THR G CB  1 
ATOM   6425  O  OG1 . THR F  1 116 ? 15.121 -30.174 -36.279  1.00 17.79 ? 116  THR G OG1 1 
ATOM   6426  C  CG2 . THR F  1 116 ? 13.609 -31.829 -35.461  1.00 16.23 ? 116  THR G CG2 1 
ATOM   6427  N  N   . LEU F  1 117 ? 14.123 -31.891 -32.202  1.00 16.38 ? 117  LEU G N   1 
ATOM   6428  C  CA  . LEU F  1 117 ? 13.537 -32.977 -31.431  1.00 16.76 ? 117  LEU G CA  1 
ATOM   6429  C  C   . LEU F  1 117 ? 12.426 -33.640 -32.234  1.00 17.09 ? 117  LEU G C   1 
ATOM   6430  O  O   . LEU F  1 117 ? 11.596 -32.958 -32.857  1.00 17.51 ? 117  LEU G O   1 
ATOM   6431  C  CB  . LEU F  1 117 ? 13.011 -32.463 -30.091  1.00 16.40 ? 117  LEU G CB  1 
ATOM   6432  C  CG  . LEU F  1 117 ? 12.525 -33.484 -29.059  1.00 15.49 ? 117  LEU G CG  1 
ATOM   6433  C  CD1 . LEU F  1 117 ? 13.684 -34.398 -28.571  1.00 13.89 ? 117  LEU G CD1 1 
ATOM   6434  C  CD2 . LEU F  1 117 ? 11.879 -32.728 -27.896  1.00 16.35 ? 117  LEU G CD2 1 
ATOM   6435  N  N   . VAL F  1 118 ? 12.403 -34.971 -32.211  1.00 17.33 ? 118  VAL G N   1 
ATOM   6436  C  CA  . VAL F  1 118 ? 11.436 -35.744 -33.000  1.00 16.71 ? 118  VAL G CA  1 
ATOM   6437  C  C   . VAL F  1 118 ? 10.790 -36.809 -32.135  1.00 17.29 ? 118  VAL G C   1 
ATOM   6438  O  O   . VAL F  1 118 ? 11.478 -37.517 -31.385  1.00 15.18 ? 118  VAL G O   1 
ATOM   6439  C  CB  . VAL F  1 118 ? 12.119 -36.440 -34.203  1.00 16.94 ? 118  VAL G CB  1 
ATOM   6440  C  CG1 . VAL F  1 118 ? 11.127 -37.352 -34.954  1.00 15.71 ? 118  VAL G CG1 1 
ATOM   6441  C  CG2 . VAL F  1 118 ? 12.753 -35.400 -35.137  1.00 15.52 ? 118  VAL G CG2 1 
ATOM   6442  N  N   . VAL F  1 119 ? 9.469  -36.888 -32.231  1.00 17.96 ? 119  VAL G N   1 
ATOM   6443  C  CA  . VAL F  1 119 ? 8.729  -37.989 -31.624  1.00 19.45 ? 119  VAL G CA  1 
ATOM   6444  C  C   . VAL F  1 119 ? 8.217  -38.875 -32.753  1.00 19.88 ? 119  VAL G C   1 
ATOM   6445  O  O   . VAL F  1 119 ? 7.690  -38.389 -33.769  1.00 20.47 ? 119  VAL G O   1 
ATOM   6446  C  CB  . VAL F  1 119 ? 7.614  -37.497 -30.660  1.00 18.47 ? 119  VAL G CB  1 
ATOM   6447  C  CG1 . VAL F  1 119 ? 6.580  -36.663 -31.397  1.00 18.16 ? 119  VAL G CG1 1 
ATOM   6448  C  CG2 . VAL F  1 119 ? 6.950  -38.684 -29.900  1.00 20.92 ? 119  VAL G CG2 1 
ATOM   6449  N  N   . HIS F  1 120 ? 8.365  -40.183 -32.562  1.00 21.23 ? 120  HIS G N   1 
ATOM   6450  C  CA  . HIS F  1 120 ? 8.140  -41.159 -33.625  1.00 22.11 ? 120  HIS G CA  1 
ATOM   6451  C  C   . HIS F  1 120 ? 6.803  -41.909 -33.596  1.00 23.23 ? 120  HIS G C   1 
ATOM   6452  O  O   . HIS F  1 120 ? 6.051  -41.845 -32.617  1.00 23.17 ? 120  HIS G O   1 
ATOM   6453  C  CB  . HIS F  1 120 ? 9.302  -42.143 -33.649  1.00 21.82 ? 120  HIS G CB  1 
ATOM   6454  C  CG  . HIS F  1 120 ? 10.555 -41.560 -34.217  1.00 22.69 ? 120  HIS G CG  1 
ATOM   6455  N  ND1 . HIS F  1 120 ? 10.863 -41.631 -35.558  1.00 22.57 ? 120  HIS G ND1 1 
ATOM   6456  C  CD2 . HIS F  1 120 ? 11.565 -40.875 -33.631  1.00 21.84 ? 120  HIS G CD2 1 
ATOM   6457  C  CE1 . HIS F  1 120 ? 12.020 -41.030 -35.771  1.00 22.01 ? 120  HIS G CE1 1 
ATOM   6458  N  NE2 . HIS F  1 120 ? 12.461 -40.555 -34.621  1.00 21.91 ? 120  HIS G NE2 1 
ATOM   6459  N  N   . GLU F  1 121 ? 6.548  -42.618 -34.699  1.00 24.26 ? 121  GLU G N   1 
ATOM   6460  C  CA  . GLU F  1 121 ? 5.399  -43.519 -34.890  1.00 25.27 ? 121  GLU G CA  1 
ATOM   6461  C  C   . GLU F  1 121 ? 5.448  -44.750 -33.974  1.00 25.16 ? 121  GLU G C   1 
ATOM   6462  O  O   . GLU F  1 121 ? 4.437  -45.124 -33.361  1.00 24.92 ? 121  GLU G O   1 
ATOM   6463  C  CB  . GLU F  1 121 ? 5.348  -43.943 -36.371  1.00 25.58 ? 121  GLU G CB  1 
ATOM   6464  C  CG  . GLU F  1 121 ? 4.380  -45.084 -36.735  1.00 28.36 ? 121  GLU G CG  1 
ATOM   6465  C  CD  . GLU F  1 121 ? 4.624  -45.678 -38.133  1.00 32.23 ? 121  GLU G CD  1 
ATOM   6466  O  OE1 . GLU F  1 121 ? 3.735  -46.407 -38.624  1.00 33.71 ? 121  GLU G OE1 1 
ATOM   6467  O  OE2 . GLU F  1 121 ? 5.695  -45.439 -38.747  1.00 32.93 ? 121  GLU G OE2 1 
ATOM   6468  N  N   . LYS F  1 122 ? 6.623  -45.371 -33.893  1.00 25.18 ? 122  LYS G N   1 
ATOM   6469  C  CA  . LYS F  1 122 ? 6.782  -46.657 -33.199  1.00 25.46 ? 122  LYS G CA  1 
ATOM   6470  C  C   . LYS F  1 122 ? 7.748  -46.561 -32.033  1.00 25.14 ? 122  LYS G C   1 
ATOM   6471  O  O   . LYS F  1 122 ? 8.397  -45.529 -31.814  1.00 25.34 ? 122  LYS G O   1 
ATOM   6472  C  CB  . LYS F  1 122 ? 7.280  -47.758 -34.153  1.00 25.38 ? 122  LYS G CB  1 
ATOM   6473  C  CG  . LYS F  1 122 ? 6.387  -48.026 -35.347  1.00 27.35 ? 122  LYS G CG  1 
ATOM   6474  C  CD  . LYS F  1 122 ? 7.083  -48.922 -36.365  1.00 28.35 ? 122  LYS G CD  1 
ATOM   6475  C  CE  . LYS F  1 122 ? 6.421  -48.790 -37.723  1.00 30.84 ? 122  LYS G CE  1 
ATOM   6476  N  NZ  . LYS F  1 122 ? 7.067  -49.629 -38.770  1.00 33.08 ? 122  LYS G NZ  1 
ATOM   6477  N  N   . ALA F  1 123 ? 7.838  -47.662 -31.297  1.00 24.58 ? 123  ALA G N   1 
ATOM   6478  C  CA  . ALA F  1 123 ? 8.793  -47.818 -30.223  1.00 23.93 ? 123  ALA G CA  1 
ATOM   6479  C  C   . ALA F  1 123 ? 10.209 -47.945 -30.762  1.00 23.67 ? 123  ALA G C   1 
ATOM   6480  O  O   . ALA F  1 123 ? 10.435 -48.572 -31.794  1.00 24.20 ? 123  ALA G O   1 
ATOM   6481  C  CB  . ALA F  1 123 ? 8.431  -49.028 -29.396  1.00 23.92 ? 123  ALA G CB  1 
ATOM   6482  N  N   . ASP F  1 124 ? 11.153 -47.332 -30.054  1.00 23.05 ? 124  ASP G N   1 
ATOM   6483  C  CA  . ASP F  1 124 ? 12.587 -47.472 -30.297  1.00 22.75 ? 124  ASP G CA  1 
ATOM   6484  C  C   . ASP F  1 124 ? 13.051 -48.824 -29.753  1.00 22.60 ? 124  ASP G C   1 
ATOM   6485  O  O   . ASP F  1 124 ? 12.879 -49.091 -28.572  1.00 22.70 ? 124  ASP G O   1 
ATOM   6486  C  CB  . ASP F  1 124 ? 13.294 -46.326 -29.559  1.00 22.72 ? 124  ASP G CB  1 
ATOM   6487  C  CG  . ASP F  1 124 ? 14.754 -46.160 -29.934  1.00 23.26 ? 124  ASP G CG  1 
ATOM   6488  O  OD1 . ASP F  1 124 ? 15.241 -45.004 -29.833  1.00 22.80 ? 124  ASP G OD1 1 
ATOM   6489  O  OD2 . ASP F  1 124 ? 15.431 -47.150 -30.272  1.00 23.90 ? 124  ASP G OD2 1 
ATOM   6490  N  N   . ASP F  1 125 ? 13.632 -49.679 -30.603  1.00 22.52 ? 125  ASP G N   1 
ATOM   6491  C  CA  . ASP F  1 125 ? 14.135 -50.991 -30.155  1.00 21.96 ? 125  ASP G CA  1 
ATOM   6492  C  C   . ASP F  1 125 ? 15.462 -50.910 -29.392  1.00 21.85 ? 125  ASP G C   1 
ATOM   6493  O  O   . ASP F  1 125 ? 16.072 -51.940 -29.062  1.00 21.56 ? 125  ASP G O   1 
ATOM   6494  C  CB  . ASP F  1 125 ? 14.169 -52.035 -31.312  1.00 22.08 ? 125  ASP G CB  1 
ATOM   6495  C  CG  . ASP F  1 125 ? 15.318 -51.823 -32.315  1.00 21.62 ? 125  ASP G CG  1 
ATOM   6496  O  OD1 . ASP F  1 125 ? 15.238 -52.379 -33.434  1.00 22.52 ? 125  ASP G OD1 1 
ATOM   6497  O  OD2 . ASP F  1 125 ? 16.311 -51.148 -32.010  1.00 21.77 ? 125  ASP G OD2 1 
ATOM   6498  N  N   . LEU F  1 126 ? 15.890 -49.675 -29.117  1.00 21.35 ? 126  LEU G N   1 
ATOM   6499  C  CA  . LEU F  1 126 ? 17.100 -49.377 -28.336  1.00 20.70 ? 126  LEU G CA  1 
ATOM   6500  C  C   . LEU F  1 126 ? 18.407 -49.988 -28.899  1.00 20.63 ? 126  LEU G C   1 
ATOM   6501  O  O   . LEU F  1 126 ? 19.378 -50.212 -28.171  1.00 20.04 ? 126  LEU G O   1 
ATOM   6502  C  CB  . LEU F  1 126 ? 16.883 -49.671 -26.829  1.00 20.72 ? 126  LEU G CB  1 
ATOM   6503  C  CG  . LEU F  1 126 ? 15.601 -49.104 -26.173  1.00 20.09 ? 126  LEU G CG  1 
ATOM   6504  C  CD1 . LEU F  1 126 ? 15.412 -49.637 -24.751  1.00 20.36 ? 126  LEU G CD1 1 
ATOM   6505  C  CD2 . LEU F  1 126 ? 15.543 -47.563 -26.166  1.00 20.94 ? 126  LEU G CD2 1 
ATOM   6506  N  N   . GLY F  1 127 ? 18.428 -50.220 -30.211  1.00 20.37 ? 127  GLY G N   1 
ATOM   6507  C  CA  . GLY F  1 127 ? 19.635 -50.686 -30.895  1.00 20.54 ? 127  GLY G CA  1 
ATOM   6508  C  C   . GLY F  1 127 ? 19.915 -52.177 -30.809  1.00 20.72 ? 127  GLY G C   1 
ATOM   6509  O  O   . GLY F  1 127 ? 20.979 -52.636 -31.242  1.00 20.55 ? 127  GLY G O   1 
ATOM   6510  N  N   . LYS F  1 128 ? 18.948 -52.924 -30.282  1.00 20.74 ? 128  LYS G N   1 
ATOM   6511  C  CA  . LYS F  1 128 ? 19.084 -54.365 -30.034  1.00 21.20 ? 128  LYS G CA  1 
ATOM   6512  C  C   . LYS F  1 128 ? 18.145 -55.159 -30.958  1.00 20.90 ? 128  LYS G C   1 
ATOM   6513  O  O   . LYS F  1 128 ? 17.685 -56.262 -30.621  1.00 21.17 ? 128  LYS G O   1 
ATOM   6514  C  CB  . LYS F  1 128 ? 18.745 -54.667 -28.572  1.00 21.33 ? 128  LYS G CB  1 
ATOM   6515  C  CG  . LYS F  1 128 ? 19.588 -53.910 -27.547  1.00 23.86 ? 128  LYS G CG  1 
ATOM   6516  C  CD  . LYS F  1 128 ? 18.947 -53.957 -26.151  1.00 25.09 ? 128  LYS G CD  1 
ATOM   6517  C  CE  . LYS F  1 128 ? 19.888 -53.411 -25.056  1.00 28.33 ? 128  LYS G CE  1 
ATOM   6518  N  NZ  . LYS F  1 128 ? 20.719 -52.229 -25.476  1.00 28.18 ? 128  LYS G NZ  1 
ATOM   6519  N  N   . GLY F  1 129 ? 17.864 -54.602 -32.129  1.00 20.47 ? 129  GLY G N   1 
ATOM   6520  C  CA  . GLY F  1 129 ? 16.956 -55.253 -33.070  1.00 20.13 ? 129  GLY G CA  1 
ATOM   6521  C  C   . GLY F  1 129 ? 17.573 -56.427 -33.802  1.00 19.69 ? 129  GLY G C   1 
ATOM   6522  O  O   . GLY F  1 129 ? 16.843 -57.276 -34.330  1.00 19.49 ? 129  GLY G O   1 
ATOM   6523  N  N   . GLY F  1 130 ? 18.907 -56.478 -33.842  1.00 19.51 ? 130  GLY G N   1 
ATOM   6524  C  CA  . GLY F  1 130 ? 19.646 -57.523 -34.565  1.00 19.66 ? 130  GLY G CA  1 
ATOM   6525  C  C   . GLY F  1 130 ? 19.708 -57.328 -36.081  1.00 20.11 ? 130  GLY G C   1 
ATOM   6526  O  O   . GLY F  1 130 ? 19.909 -58.292 -36.848  1.00 19.51 ? 130  GLY G O   1 
ATOM   6527  N  N   . ASN F  1 131 ? 19.525 -56.076 -36.508  1.00 20.18 ? 131  ASN G N   1 
ATOM   6528  C  CA  . ASN F  1 131 ? 19.589 -55.687 -37.926  1.00 20.34 ? 131  ASN G CA  1 
ATOM   6529  C  C   . ASN F  1 131 ? 20.318 -54.350 -38.117  1.00 20.52 ? 131  ASN G C   1 
ATOM   6530  O  O   . ASN F  1 131 ? 20.520 -53.606 -37.145  1.00 19.77 ? 131  ASN G O   1 
ATOM   6531  C  CB  . ASN F  1 131 ? 18.190 -55.652 -38.562  1.00 20.48 ? 131  ASN G CB  1 
ATOM   6532  C  CG  . ASN F  1 131 ? 17.204 -54.779 -37.800  1.00 20.88 ? 131  ASN G CG  1 
ATOM   6533  O  OD1 . ASN F  1 131 ? 17.369 -53.568 -37.701  1.00 21.75 ? 131  ASN G OD1 1 
ATOM   6534  N  ND2 . ASN F  1 131 ? 16.143 -55.394 -37.291  1.00 22.25 ? 131  ASN G ND2 1 
ATOM   6535  N  N   . GLU F  1 132 ? 20.712 -54.048 -39.357  1.00 19.86 ? 132  GLU G N   1 
ATOM   6536  C  CA  . GLU F  1 132 ? 21.474 -52.825 -39.621  1.00 19.99 ? 132  GLU G CA  1 
ATOM   6537  C  C   . GLU F  1 132 ? 20.689 -51.576 -39.228  1.00 20.01 ? 132  GLU G C   1 
ATOM   6538  O  O   . GLU F  1 132 ? 21.252 -50.662 -38.635  1.00 20.15 ? 132  GLU G O   1 
ATOM   6539  C  CB  . GLU F  1 132 ? 21.970 -52.760 -41.074  1.00 19.94 ? 132  GLU G CB  1 
ATOM   6540  C  CG  . GLU F  1 132 ? 22.826 -51.516 -41.415  1.00 20.14 ? 132  GLU G CG  1 
ATOM   6541  C  CD  . GLU F  1 132 ? 24.142 -51.401 -40.644  1.00 21.82 ? 132  GLU G CD  1 
ATOM   6542  O  OE1 . GLU F  1 132 ? 24.618 -52.386 -40.041  1.00 21.56 ? 132  GLU G OE1 1 
ATOM   6543  O  OE2 . GLU F  1 132 ? 24.720 -50.299 -40.660  1.00 22.13 ? 132  GLU G OE2 1 
ATOM   6544  N  N   . GLU F  1 133 ? 19.390 -51.559 -39.517  1.00 19.99 ? 133  GLU G N   1 
ATOM   6545  C  CA  . GLU F  1 133 ? 18.570 -50.379 -39.261  1.00 20.13 ? 133  GLU G CA  1 
ATOM   6546  C  C   . GLU F  1 133 ? 18.398 -50.106 -37.767  1.00 20.17 ? 133  GLU G C   1 
ATOM   6547  O  O   . GLU F  1 133 ? 18.347 -48.941 -37.355  1.00 20.48 ? 133  GLU G O   1 
ATOM   6548  C  CB  . GLU F  1 133 ? 17.206 -50.490 -39.950  1.00 20.11 ? 133  GLU G CB  1 
ATOM   6549  C  CG  . GLU F  1 133 ? 16.340 -49.224 -39.854  1.00 21.36 ? 133  GLU G CG  1 
ATOM   6550  C  CD  . GLU F  1 133 ? 16.810 -48.073 -40.750  1.00 22.46 ? 133  GLU G CD  1 
ATOM   6551  O  OE1 . GLU F  1 133 ? 15.972 -47.216 -41.093  1.00 24.32 ? 133  GLU G OE1 1 
ATOM   6552  O  OE2 . GLU F  1 133 ? 17.999 -48.020 -41.123  1.00 23.38 ? 133  GLU G OE2 1 
ATOM   6553  N  N   . SER F  1 134 ? 18.307 -51.161 -36.953  1.00 19.70 ? 134  SER G N   1 
ATOM   6554  C  CA  . SER F  1 134 ? 18.256 -50.965 -35.499  1.00 18.93 ? 134  SER G CA  1 
ATOM   6555  C  C   . SER F  1 134 ? 19.452 -50.149 -35.012  1.00 18.71 ? 134  SER G C   1 
ATOM   6556  O  O   . SER F  1 134 ? 19.299 -49.244 -34.177  1.00 18.53 ? 134  SER G O   1 
ATOM   6557  C  CB  . SER F  1 134 ? 18.209 -52.296 -34.749  1.00 19.66 ? 134  SER G CB  1 
ATOM   6558  O  OG  . SER F  1 134 ? 18.223 -52.054 -33.348  1.00 18.26 ? 134  SER G OG  1 
ATOM   6559  N  N   . THR F  1 135 ? 20.633 -50.468 -35.546  1.00 18.05 ? 135  THR G N   1 
ATOM   6560  C  CA  . THR F  1 135 ? 21.865 -49.754 -35.207  1.00 18.04 ? 135  THR G CA  1 
ATOM   6561  C  C   . THR F  1 135 ? 21.896 -48.313 -35.713  1.00 17.77 ? 135  THR G C   1 
ATOM   6562  O  O   . THR F  1 135 ? 22.874 -47.597 -35.460  1.00 17.98 ? 135  THR G O   1 
ATOM   6563  C  CB  . THR F  1 135 ? 23.147 -50.466 -35.721  1.00 17.58 ? 135  THR G CB  1 
ATOM   6564  O  OG1 . THR F  1 135 ? 23.332 -50.191 -37.121  1.00 18.39 ? 135  THR G OG1 1 
ATOM   6565  C  CG2 . THR F  1 135 ? 23.076 -51.969 -35.474  1.00 17.57 ? 135  THR G CG2 1 
ATOM   6566  N  N   . LYS F  1 136 ? 20.848 -47.893 -36.420  1.00 17.51 ? 136  LYS G N   1 
ATOM   6567  C  CA  . LYS F  1 136 ? 20.802 -46.540 -36.960  1.00 17.77 ? 136  LYS G CA  1 
ATOM   6568  C  C   . LYS F  1 136 ? 19.620 -45.722 -36.415  1.00 17.79 ? 136  LYS G C   1 
ATOM   6569  O  O   . LYS F  1 136 ? 19.790 -44.578 -36.001  1.00 18.57 ? 136  LYS G O   1 
ATOM   6570  C  CB  . LYS F  1 136 ? 20.781 -46.584 -38.504  1.00 17.78 ? 136  LYS G CB  1 
ATOM   6571  C  CG  . LYS F  1 136 ? 22.040 -47.191 -39.150  1.00 16.35 ? 136  LYS G CG  1 
ATOM   6572  C  CD  . LYS F  1 136 ? 22.171 -46.776 -40.631  1.00 16.34 ? 136  LYS G CD  1 
ATOM   6573  C  CE  . LYS F  1 136 ? 23.406 -47.390 -41.280  1.00 15.26 ? 136  LYS G CE  1 
ATOM   6574  N  NZ  . LYS F  1 136 ? 24.732 -47.095 -40.602  1.00 16.43 ? 136  LYS G NZ  1 
ATOM   6575  N  N   . THR F  1 137 ? 18.426 -46.310 -36.402  1.00 17.34 ? 137  THR G N   1 
ATOM   6576  C  CA  . THR F  1 137 ? 17.213 -45.565 -36.087  1.00 16.67 ? 137  THR G CA  1 
ATOM   6577  C  C   . THR F  1 137 ? 16.436 -46.166 -34.914  1.00 17.40 ? 137  THR G C   1 
ATOM   6578  O  O   . THR F  1 137 ? 15.450 -45.589 -34.447  1.00 17.61 ? 137  THR G O   1 
ATOM   6579  C  CB  . THR F  1 137 ? 16.271 -45.547 -37.301  1.00 16.87 ? 137  THR G CB  1 
ATOM   6580  O  OG1 . THR F  1 137 ? 15.845 -46.891 -37.595  1.00 14.82 ? 137  THR G OG1 1 
ATOM   6581  C  CG2 . THR F  1 137 ? 16.951 -44.945 -38.551  1.00 14.47 ? 137  THR G CG2 1 
ATOM   6582  N  N   . GLY F  1 138 ? 16.860 -47.339 -34.458  1.00 17.20 ? 138  GLY G N   1 
ATOM   6583  C  CA  . GLY F  1 138 ? 16.064 -48.111 -33.512  1.00 18.44 ? 138  GLY G CA  1 
ATOM   6584  C  C   . GLY F  1 138 ? 14.725 -48.608 -34.063  1.00 18.93 ? 138  GLY G C   1 
ATOM   6585  O  O   . GLY F  1 138 ? 13.859 -49.045 -33.296  1.00 18.97 ? 138  GLY G O   1 
ATOM   6586  N  N   . ASN F  1 139 ? 14.556 -48.550 -35.385  1.00 19.09 ? 139  ASN G N   1 
ATOM   6587  C  CA  . ASN F  1 139 ? 13.309 -48.971 -36.051  1.00 19.65 ? 139  ASN G CA  1 
ATOM   6588  C  C   . ASN F  1 139 ? 12.044 -48.266 -35.541  1.00 19.84 ? 139  ASN G C   1 
ATOM   6589  O  O   . ASN F  1 139 ? 10.955 -48.856 -35.506  1.00 19.12 ? 139  ASN G O   1 
ATOM   6590  C  CB  . ASN F  1 139 ? 13.134 -50.506 -35.983  1.00 19.94 ? 139  ASN G CB  1 
ATOM   6591  C  CG  . ASN F  1 139 ? 14.163 -51.252 -36.827  1.00 20.12 ? 139  ASN G CG  1 
ATOM   6592  O  OD1 . ASN F  1 139 ? 14.229 -51.080 -38.054  1.00 19.63 ? 139  ASN G OD1 1 
ATOM   6593  N  ND2 . ASN F  1 139 ? 14.970 -52.081 -36.174  1.00 19.10 ? 139  ASN G ND2 1 
ATOM   6594  N  N   . ALA F  1 140 ? 12.183 -46.995 -35.163  1.00 19.81 ? 140  ALA G N   1 
ATOM   6595  C  CA  . ALA F  1 140 ? 11.083 -46.258 -34.550  1.00 19.90 ? 140  ALA G CA  1 
ATOM   6596  C  C   . ALA F  1 140 ? 10.083 -45.656 -35.550  1.00 20.32 ? 140  ALA G C   1 
ATOM   6597  O  O   . ALA F  1 140 ? 9.165  -44.928 -35.154  1.00 20.58 ? 140  ALA G O   1 
ATOM   6598  C  CB  . ALA F  1 140 ? 11.632 -45.187 -33.595  1.00 19.93 ? 140  ALA G CB  1 
ATOM   6599  N  N   . GLY F  1 141 ? 10.244 -45.968 -36.837  1.00 20.19 ? 141  GLY G N   1 
ATOM   6600  C  CA  . GLY F  1 141 ? 9.270  -45.563 -37.846  1.00 19.85 ? 141  GLY G CA  1 
ATOM   6601  C  C   . GLY F  1 141 ? 9.187  -44.070 -38.094  1.00 19.70 ? 141  GLY G C   1 
ATOM   6602  O  O   . GLY F  1 141 ? 10.138 -43.340 -37.827  1.00 19.46 ? 141  GLY G O   1 
ATOM   6603  N  N   . SER F  1 142 ? 8.042  -43.625 -38.605  1.00 19.17 ? 142  SER G N   1 
ATOM   6604  C  CA  . SER F  1 142 ? 7.908  -42.269 -39.119  1.00 19.11 ? 142  SER G CA  1 
ATOM   6605  C  C   . SER F  1 142 ? 8.082  -41.195 -38.043  1.00 19.04 ? 142  SER G C   1 
ATOM   6606  O  O   . SER F  1 142 ? 8.072  -41.466 -36.832  1.00 19.05 ? 142  SER G O   1 
ATOM   6607  C  CB  . SER F  1 142 ? 6.586  -42.074 -39.886  1.00 19.02 ? 142  SER G CB  1 
ATOM   6608  O  OG  . SER F  1 142 ? 5.469  -42.159 -39.021  1.00 19.45 ? 142  SER G OG  1 
ATOM   6609  N  N   . ARG F  1 143 ? 8.233  -39.969 -38.510  1.00 18.57 ? 143  ARG G N   1 
ATOM   6610  C  CA  . ARG F  1 143 ? 8.433  -38.837 -37.625  1.00 17.63 ? 143  ARG G CA  1 
ATOM   6611  C  C   . ARG F  1 143 ? 7.094  -38.130 -37.550  1.00 17.57 ? 143  ARG G C   1 
ATOM   6612  O  O   . ARG F  1 143 ? 6.625  -37.543 -38.528  1.00 18.16 ? 143  ARG G O   1 
ATOM   6613  C  CB  . ARG F  1 143 ? 9.558  -37.981 -38.177  1.00 17.51 ? 143  ARG G CB  1 
ATOM   6614  C  CG  . ARG F  1 143 ? 10.869 -38.762 -38.310  1.00 16.81 ? 143  ARG G CG  1 
ATOM   6615  C  CD  . ARG F  1 143 ? 11.876 -38.046 -39.171  1.00 17.34 ? 143  ARG G CD  1 
ATOM   6616  N  NE  . ARG F  1 143 ? 13.090 -38.841 -39.307  1.00 18.59 ? 143  ARG G NE  1 
ATOM   6617  C  CZ  . ARG F  1 143 ? 14.282 -38.348 -39.632  1.00 17.78 ? 143  ARG G CZ  1 
ATOM   6618  N  NH1 . ARG F  1 143 ? 15.327 -39.159 -39.732  1.00 18.01 ? 143  ARG G NH1 1 
ATOM   6619  N  NH2 . ARG F  1 143 ? 14.438 -37.048 -39.842  1.00 18.27 ? 143  ARG G NH2 1 
ATOM   6620  N  N   . LEU F  1 144 ? 6.432  -38.260 -36.409  1.00 17.60 ? 144  LEU G N   1 
ATOM   6621  C  CA  . LEU F  1 144 ? 5.040  -37.825 -36.292  1.00 17.93 ? 144  LEU G CA  1 
ATOM   6622  C  C   . LEU F  1 144 ? 4.941  -36.328 -36.032  1.00 17.80 ? 144  LEU G C   1 
ATOM   6623  O  O   . LEU F  1 144 ? 4.025  -35.650 -36.531  1.00 18.05 ? 144  LEU G O   1 
ATOM   6624  C  CB  . LEU F  1 144 ? 4.325  -38.591 -35.184  1.00 17.94 ? 144  LEU G CB  1 
ATOM   6625  C  CG  . LEU F  1 144 ? 3.956  -40.054 -35.448  1.00 19.31 ? 144  LEU G CG  1 
ATOM   6626  C  CD1 . LEU F  1 144 ? 3.224  -40.544 -34.229  1.00 22.27 ? 144  LEU G CD1 1 
ATOM   6627  C  CD2 . LEU F  1 144 ? 3.117  -40.240 -36.706  1.00 20.06 ? 144  LEU G CD2 1 
ATOM   6628  N  N   . ALA F  1 145 ? 5.890  -35.824 -35.253  1.00 17.36 ? 145  ALA G N   1 
ATOM   6629  C  CA  . ALA F  1 145 ? 5.950  -34.400 -34.945  1.00 17.16 ? 145  ALA G CA  1 
ATOM   6630  C  C   . ALA F  1 145 ? 7.367  -34.001 -34.560  1.00 16.99 ? 145  ALA G C   1 
ATOM   6631  O  O   . ALA F  1 145 ? 8.137  -34.808 -34.008  1.00 16.99 ? 145  ALA G O   1 
ATOM   6632  C  CB  . ALA F  1 145 ? 4.984  -34.065 -33.820  1.00 17.63 ? 145  ALA G CB  1 
ATOM   6633  N  N   . CYS F  1 146 ? 7.720  -32.750 -34.847  1.00 16.08 ? 146  CYS G N   1 
ATOM   6634  C  CA  . CYS F  1 146 ? 9.058  -32.293 -34.544  1.00 15.18 ? 146  CYS G CA  1 
ATOM   6635  C  C   . CYS F  1 146 ? 9.106  -30.797 -34.257  1.00 15.29 ? 146  CYS G C   1 
ATOM   6636  O  O   . CYS F  1 146 ? 8.123  -30.069 -34.449  1.00 15.69 ? 146  CYS G O   1 
ATOM   6637  C  CB  . CYS F  1 146 ? 10.035 -32.645 -35.675  0.40 14.38 ? 146  CYS G CB  1 
ATOM   6638  S  SG  . CYS F  1 146 ? 9.594  -31.972 -37.269  0.40 10.89 ? 146  CYS G SG  1 
ATOM   6639  N  N   . GLY F  1 147 ? 10.255 -30.349 -33.778  1.00 15.46 ? 147  GLY G N   1 
ATOM   6640  C  CA  . GLY F  1 147 ? 10.471 -28.907 -33.603  1.00 15.89 ? 147  GLY G CA  1 
ATOM   6641  C  C   . GLY F  1 147 ? 11.933 -28.590 -33.483  1.00 16.00 ? 147  GLY G C   1 
ATOM   6642  O  O   . GLY F  1 147 ? 12.723 -29.476 -33.129  1.00 16.13 ? 147  GLY G O   1 
ATOM   6643  N  N   . VAL F  1 148 ? 12.309 -27.333 -33.754  1.00 15.90 ? 148  VAL G N   1 
ATOM   6644  C  CA  . VAL F  1 148 ? 13.682 -26.911 -33.483  1.00 15.83 ? 148  VAL G CA  1 
ATOM   6645  C  C   . VAL F  1 148 ? 13.861 -26.607 -31.983  1.00 16.03 ? 148  VAL G C   1 
ATOM   6646  O  O   . VAL F  1 148 ? 12.973 -26.052 -31.336  1.00 16.75 ? 148  VAL G O   1 
ATOM   6647  C  CB  . VAL F  1 148 ? 14.146 -25.726 -34.383  1.00 15.76 ? 148  VAL G CB  1 
ATOM   6648  C  CG1 . VAL F  1 148 ? 15.637 -25.430 -34.150  1.00 16.27 ? 148  VAL G CG1 1 
ATOM   6649  C  CG2 . VAL F  1 148 ? 13.926 -26.071 -35.870  1.00 13.78 ? 148  VAL G CG2 1 
ATOM   6650  N  N   . ILE F  1 149 ? 15.011 -27.012 -31.452  1.00 15.56 ? 149  ILE G N   1 
ATOM   6651  C  CA  . ILE F  1 149 ? 15.395 -26.746 -30.087  1.00 15.84 ? 149  ILE G CA  1 
ATOM   6652  C  C   . ILE F  1 149 ? 15.896 -25.289 -29.991  1.00 15.85 ? 149  ILE G C   1 
ATOM   6653  O  O   . ILE F  1 149 ? 16.952 -24.939 -30.543  1.00 16.29 ? 149  ILE G O   1 
ATOM   6654  C  CB  . ILE F  1 149 ? 16.444 -27.790 -29.623  1.00 15.70 ? 149  ILE G CB  1 
ATOM   6655  C  CG1 . ILE F  1 149 ? 15.845 -29.209 -29.729  1.00 16.03 ? 149  ILE G CG1 1 
ATOM   6656  C  CG2 . ILE F  1 149 ? 16.941 -27.492 -28.202  1.00 16.16 ? 149  ILE G CG2 1 
ATOM   6657  C  CD1 . ILE F  1 149 ? 16.813 -30.341 -29.321  1.00 14.41 ? 149  ILE G CD1 1 
ATOM   6658  N  N   . GLY F  1 150 ? 15.103 -24.448 -29.327  1.00 15.69 ? 150  GLY G N   1 
ATOM   6659  C  CA  . GLY F  1 150 ? 15.357 -23.003 -29.228  1.00 15.69 ? 150  GLY G CA  1 
ATOM   6660  C  C   . GLY F  1 150 ? 15.789 -22.544 -27.845  1.00 16.34 ? 150  GLY G C   1 
ATOM   6661  O  O   . GLY F  1 150 ? 15.364 -23.133 -26.832  1.00 15.99 ? 150  GLY G O   1 
ATOM   6662  N  N   . ILE F  1 151 ? 16.663 -21.525 -27.798  1.00 16.29 ? 151  ILE G N   1 
ATOM   6663  C  CA  . ILE F  1 151 ? 17.132 -20.948 -26.514  1.00 17.44 ? 151  ILE G CA  1 
ATOM   6664  C  C   . ILE F  1 151 ? 15.948 -20.289 -25.817  1.00 17.91 ? 151  ILE G C   1 
ATOM   6665  O  O   . ILE F  1 151 ? 15.211 -19.518 -26.438  1.00 17.53 ? 151  ILE G O   1 
ATOM   6666  C  CB  . ILE F  1 151 ? 18.292 -19.900 -26.683  1.00 17.48 ? 151  ILE G CB  1 
ATOM   6667  C  CG1 . ILE F  1 151 ? 19.546 -20.557 -27.276  1.00 18.60 ? 151  ILE G CG1 1 
ATOM   6668  C  CG2 . ILE F  1 151 ? 18.671 -19.287 -25.320  1.00 17.90 ? 151  ILE G CG2 1 
ATOM   6669  C  CD1 . ILE F  1 151 ? 20.542 -19.618 -27.946  1.00 19.06 ? 151  ILE G CD1 1 
ATOM   6670  N  N   . ALA F  1 152 ? 15.764 -20.601 -24.532  1.00 18.93 ? 152  ALA G N   1 
ATOM   6671  C  CA  . ALA F  1 152 ? 14.631 -20.095 -23.768  1.00 20.28 ? 152  ALA G CA  1 
ATOM   6672  C  C   . ALA F  1 152 ? 15.080 -19.178 -22.627  1.00 20.96 ? 152  ALA G C   1 
ATOM   6673  O  O   . ALA F  1 152 ? 16.230 -19.247 -22.167  1.00 21.20 ? 152  ALA G O   1 
ATOM   6674  C  CB  . ALA F  1 152 ? 13.763 -21.263 -23.243  1.00 19.78 ? 152  ALA G CB  1 
ATOM   6675  N  N   . GLN F  1 153 ? 14.174 -18.307 -22.197  1.00 22.63 ? 153  GLN G N   1 
ATOM   6676  C  CA  . GLN F  1 153 ? 14.480 -17.303 -21.167  1.00 24.14 ? 153  GLN G CA  1 
ATOM   6677  C  C   . GLN F  1 153 ? 14.782 -17.982 -19.830  1.00 24.77 ? 153  GLN G C   1 
ATOM   6678  O  O   . GLN F  1 153 ? 15.696 -17.583 -19.095  1.00 25.25 ? 153  GLN G O   1 
ATOM   6679  C  CB  . GLN F  1 153 ? 13.322 -16.289 -21.036  1.00 24.94 ? 153  GLN G CB  1 
ATOM   6680  C  CG  . GLN F  1 153 ? 13.523 -15.227 -19.928  1.00 26.62 ? 153  GLN G CG  1 
ATOM   6681  C  CD  . GLN F  1 153 ? 12.563 -14.049 -20.032  1.00 28.28 ? 153  GLN G CD  1 
ATOM   6682  O  OE1 . GLN F  1 153 ? 12.980 -12.900 -19.943  1.00 31.15 ? 153  GLN G OE1 1 
ATOM   6683  N  NE2 . GLN F  1 153 ? 11.279 -14.331 -20.202  1.00 29.33 ? 153  GLN G NE2 1 
ATOM   6684  O  OXT . GLN F  1 153 ? 14.125 -18.976 -19.483  1.00 24.96 ? 153  GLN G OXT 1 
ATOM   6685  N  N   . ALA G  1 1   ? 31.771 -5.549  -12.000  1.00 25.36 ? 1    ALA H N   1 
ATOM   6686  C  CA  . ALA G  1 1   ? 33.209 -5.454  -12.408  1.00 24.72 ? 1    ALA H CA  1 
ATOM   6687  C  C   . ALA G  1 1   ? 33.865 -6.835  -12.459  1.00 24.28 ? 1    ALA H C   1 
ATOM   6688  O  O   . ALA G  1 1   ? 33.550 -7.707  -11.645  1.00 24.25 ? 1    ALA H O   1 
ATOM   6689  C  CB  . ALA G  1 1   ? 33.972 -4.536  -11.447  1.00 25.17 ? 1    ALA H CB  1 
ATOM   6690  N  N   . THR G  1 2   ? 34.745 -7.045  -13.439  1.00 22.90 ? 2    THR H N   1 
ATOM   6691  C  CA  . THR G  1 2   ? 35.697 -8.158  -13.397  1.00 21.94 ? 2    THR H CA  1 
ATOM   6692  C  C   . THR G  1 2   ? 37.095 -7.569  -13.302  1.00 21.10 ? 2    THR H C   1 
ATOM   6693  O  O   . THR G  1 2   ? 37.385 -6.507  -13.866  1.00 20.60 ? 2    THR H O   1 
ATOM   6694  C  CB  . THR G  1 2   ? 35.617 -9.090  -14.634  1.00 22.16 ? 2    THR H CB  1 
ATOM   6695  O  OG1 . THR G  1 2   ? 34.351 -9.740  -14.659  1.00 22.06 ? 2    THR H OG1 1 
ATOM   6696  C  CG2 . THR G  1 2   ? 36.691 -10.172 -14.587  1.00 22.15 ? 2    THR H CG2 1 
ATOM   6697  N  N   . LYS G  1 3   ? 37.946 -8.263  -12.564  1.00 20.09 ? 3    LYS H N   1 
ATOM   6698  C  CA  . LYS G  1 3   ? 39.324 -7.857  -12.400  1.00 19.52 ? 3    LYS H CA  1 
ATOM   6699  C  C   . LYS G  1 3   ? 40.208 -9.048  -12.690  1.00 18.15 ? 3    LYS H C   1 
ATOM   6700  O  O   . LYS G  1 3   ? 39.823 -10.191 -12.460  1.00 17.72 ? 3    LYS H O   1 
ATOM   6701  C  CB  . LYS G  1 3   ? 39.581 -7.327  -10.986  1.00 19.72 ? 3    LYS H CB  1 
ATOM   6702  C  CG  . LYS G  1 3   ? 38.879 -6.010  -10.682  1.00 22.34 ? 3    LYS H CG  1 
ATOM   6703  C  CD  . LYS G  1 3   ? 39.353 -5.415  -9.354   1.00 24.27 ? 3    LYS H CD  1 
ATOM   6704  C  CE  . LYS G  1 3   ? 38.593 -4.132  -9.014   1.00 26.62 ? 3    LYS H CE  1 
ATOM   6705  N  NZ  . LYS G  1 3   ? 37.368 -4.356  -8.169   1.00 28.43 ? 3    LYS H NZ  1 
ATOM   6706  N  N   . ALA G  1 4   ? 41.395 -8.773  -13.205  1.00 16.71 ? 4    ALA H N   1 
ATOM   6707  C  CA  . ALA G  1 4   ? 42.351 -9.828  -13.480  1.00 16.02 ? 4    ALA H CA  1 
ATOM   6708  C  C   . ALA G  1 4   ? 43.742 -9.322  -13.160  1.00 15.46 ? 4    ALA H C   1 
ATOM   6709  O  O   . ALA G  1 4   ? 43.949 -8.115  -13.021  1.00 15.86 ? 4    ALA H O   1 
ATOM   6710  C  CB  . ALA G  1 4   ? 42.239 -10.282 -14.952  1.00 16.18 ? 4    ALA H CB  1 
ATOM   6711  N  N   . VAL G  1 5   ? 44.701 -10.229 -13.026  1.00 15.12 ? 5    VAL H N   1 
ATOM   6712  C  CA  . VAL G  1 5   ? 46.055 -9.819  -12.658  1.00 14.81 ? 5    VAL H CA  1 
ATOM   6713  C  C   . VAL G  1 5   ? 47.083 -10.758 -13.270  1.00 15.02 ? 5    VAL H C   1 
ATOM   6714  O  O   . VAL G  1 5   ? 46.790 -11.906 -13.545  1.00 13.95 ? 5    VAL H O   1 
ATOM   6715  C  CB  . VAL G  1 5   ? 46.212 -9.716  -11.095  1.00 15.02 ? 5    VAL H CB  1 
ATOM   6716  C  CG1 . VAL G  1 5   ? 46.103 -11.085 -10.439  1.00 13.97 ? 5    VAL H CG1 1 
ATOM   6717  C  CG2 . VAL G  1 5   ? 47.521 -9.026  -10.711  1.00 14.27 ? 5    VAL H CG2 1 
ATOM   6718  N  N   . CYS G  1 6   ? 48.289 -10.256 -13.504  1.00 15.85 ? 6    CYS H N   1 
ATOM   6719  C  CA  . CYS G  1 6   ? 49.340 -11.067 -14.087  1.00 16.48 ? 6    CYS H CA  1 
ATOM   6720  C  C   . CYS G  1 6   ? 50.713 -10.717 -13.532  1.00 17.24 ? 6    CYS H C   1 
ATOM   6721  O  O   . CYS G  1 6   ? 51.154 -9.572  -13.620  1.00 16.52 ? 6    CYS H O   1 
ATOM   6722  C  CB  . CYS G  1 6   ? 49.325 -10.928 -15.613  1.00 17.17 ? 6    CYS H CB  1 
ATOM   6723  S  SG  . CYS G  1 6   ? 50.679 -11.769 -16.432  1.00 18.45 ? 6    CYS H SG  1 
ATOM   6724  N  N   . VAL G  1 7   ? 51.389 -11.715 -12.961  1.00 17.82 ? 7    VAL H N   1 
ATOM   6725  C  CA  . VAL G  1 7   ? 52.757 -11.521 -12.476  1.00 18.19 ? 7    VAL H CA  1 
ATOM   6726  C  C   . VAL G  1 7   ? 53.720 -11.928 -13.586  1.00 18.52 ? 7    VAL H C   1 
ATOM   6727  O  O   . VAL G  1 7   ? 53.798 -13.100 -13.978  1.00 16.69 ? 7    VAL H O   1 
ATOM   6728  C  CB  . VAL G  1 7   ? 53.030 -12.270 -11.125  1.00 18.72 ? 7    VAL H CB  1 
ATOM   6729  C  CG1 . VAL G  1 7   ? 54.488 -12.107 -10.695  1.00 19.02 ? 7    VAL H CG1 1 
ATOM   6730  C  CG2 . VAL G  1 7   ? 52.096 -11.730 -10.028  1.00 18.68 ? 7    VAL H CG2 1 
ATOM   6731  N  N   . LEU G  1 8   ? 54.415 -10.925 -14.118  1.00 19.10 ? 8    LEU H N   1 
ATOM   6732  C  CA  . LEU G  1 8   ? 55.397 -11.117 -15.182  1.00 20.14 ? 8    LEU H CA  1 
ATOM   6733  C  C   . LEU G  1 8   ? 56.775 -11.473 -14.634  1.00 20.65 ? 8    LEU H C   1 
ATOM   6734  O  O   . LEU G  1 8   ? 57.314 -10.758 -13.776  1.00 19.69 ? 8    LEU H O   1 
ATOM   6735  C  CB  . LEU G  1 8   ? 55.513 -9.832  -16.025  1.00 19.96 ? 8    LEU H CB  1 
ATOM   6736  C  CG  . LEU G  1 8   ? 54.830 -9.620  -17.385  1.00 20.85 ? 8    LEU H CG  1 
ATOM   6737  C  CD1 . LEU G  1 8   ? 53.604 -10.449 -17.605  1.00 20.69 ? 8    LEU H CD1 1 
ATOM   6738  C  CD2 . LEU G  1 8   ? 54.519 -8.127  -17.562  1.00 21.97 ? 8    LEU H CD2 1 
ATOM   6739  N  N   . LYS G  1 9   ? 57.347 -12.542 -15.185  1.00 21.70 ? 9    LYS H N   1 
ATOM   6740  C  CA  . LYS G  1 9   ? 58.701 -13.001 -14.848  1.00 23.59 ? 9    LYS H CA  1 
ATOM   6741  C  C   . LYS G  1 9   ? 59.384 -13.670 -16.039  1.00 23.94 ? 9    LYS H C   1 
ATOM   6742  O  O   . LYS G  1 9   ? 58.717 -14.210 -16.912  1.00 24.48 ? 9    LYS H O   1 
ATOM   6743  C  CB  . LYS G  1 9   ? 58.649 -13.995 -13.683  1.00 23.85 ? 9    LYS H CB  1 
ATOM   6744  C  CG  . LYS G  1 9   ? 58.886 -13.388 -12.322  1.00 26.22 ? 9    LYS H CG  1 
ATOM   6745  C  CD  . LYS G  1 9   ? 59.846 -14.274 -11.527  1.00 29.02 ? 9    LYS H CD  1 
ATOM   6746  C  CE  . LYS G  1 9   ? 61.285 -14.140 -12.047  1.00 30.97 ? 9    LYS H CE  1 
ATOM   6747  N  NZ  . LYS G  1 9   ? 61.953 -15.472 -12.232  1.00 31.68 ? 9    LYS H NZ  1 
ATOM   6748  N  N   . GLY G  1 10  ? 60.711 -13.655 -16.068  1.00 24.84 ? 10   GLY H N   1 
ATOM   6749  C  CA  . GLY G  1 10  ? 61.443 -14.305 -17.153  1.00 26.02 ? 10   GLY H CA  1 
ATOM   6750  C  C   . GLY G  1 10  ? 62.804 -14.839 -16.747  1.00 27.32 ? 10   GLY H C   1 
ATOM   6751  O  O   . GLY G  1 10  ? 63.096 -14.971 -15.553  1.00 27.65 ? 10   GLY H O   1 
ATOM   6752  N  N   . ASP G  1 11  ? 63.630 -15.160 -17.746  1.00 27.96 ? 11   ASP H N   1 
ATOM   6753  C  CA  . ASP G  1 11  ? 64.993 -15.658 -17.509  1.00 29.32 ? 11   ASP H CA  1 
ATOM   6754  C  C   . ASP G  1 11  ? 65.886 -14.609 -16.829  1.00 29.15 ? 11   ASP H C   1 
ATOM   6755  O  O   . ASP G  1 11  ? 66.741 -14.958 -15.990  1.00 29.69 ? 11   ASP H O   1 
ATOM   6756  C  CB  . ASP G  1 11  ? 65.640 -16.109 -18.827  1.00 29.94 ? 11   ASP H CB  1 
ATOM   6757  C  CG  . ASP G  1 11  ? 65.397 -17.576 -19.130  1.00 31.97 ? 11   ASP H CG  1 
ATOM   6758  O  OD1 . ASP G  1 11  ? 64.609 -17.881 -20.053  1.00 34.67 ? 11   ASP H OD1 1 
ATOM   6759  O  OD2 . ASP G  1 11  ? 65.995 -18.435 -18.448  1.00 35.32 ? 11   ASP H OD2 1 
ATOM   6760  N  N   . GLY G  1 12  ? 65.678 -13.338 -17.184  1.00 28.11 ? 12   GLY H N   1 
ATOM   6761  C  CA  . GLY G  1 12  ? 66.562 -12.248 -16.773  1.00 26.81 ? 12   GLY H CA  1 
ATOM   6762  C  C   . GLY G  1 12  ? 65.942 -11.253 -15.810  1.00 26.12 ? 12   GLY H C   1 
ATOM   6763  O  O   . GLY G  1 12  ? 65.097 -11.625 -14.996  1.00 26.36 ? 12   GLY H O   1 
ATOM   6764  N  N   . PRO G  1 13  ? 66.341 -9.971  -15.921  1.00 25.53 ? 13   PRO H N   1 
ATOM   6765  C  CA  . PRO G  1 13  ? 65.988 -8.905  -14.977  1.00 25.04 ? 13   PRO H CA  1 
ATOM   6766  C  C   . PRO G  1 13  ? 64.543 -8.376  -15.025  1.00 24.30 ? 13   PRO H C   1 
ATOM   6767  O  O   . PRO G  1 13  ? 64.148 -7.626  -14.131  1.00 24.48 ? 13   PRO H O   1 
ATOM   6768  C  CB  . PRO G  1 13  ? 66.967 -7.783  -15.350  1.00 25.33 ? 13   PRO H CB  1 
ATOM   6769  C  CG  . PRO G  1 13  ? 67.249 -8.002  -16.789  1.00 25.39 ? 13   PRO H CG  1 
ATOM   6770  C  CD  . PRO G  1 13  ? 67.257 -9.487  -16.973  1.00 25.47 ? 13   PRO H CD  1 
ATOM   6771  N  N   . VAL G  1 14  ? 63.772 -8.766  -16.041  1.00 23.00 ? 14   VAL H N   1 
ATOM   6772  C  CA  . VAL G  1 14  ? 62.477 -8.138  -16.299  1.00 21.96 ? 14   VAL H CA  1 
ATOM   6773  C  C   . VAL G  1 14  ? 61.395 -8.721  -15.405  1.00 21.48 ? 14   VAL H C   1 
ATOM   6774  O  O   . VAL G  1 14  ? 61.157 -9.913  -15.403  1.00 21.34 ? 14   VAL H O   1 
ATOM   6775  C  CB  . VAL G  1 14  ? 62.047 -8.278  -17.796  1.00 21.86 ? 14   VAL H CB  1 
ATOM   6776  C  CG1 . VAL G  1 14  ? 60.774 -7.494  -18.061  1.00 21.25 ? 14   VAL H CG1 1 
ATOM   6777  C  CG2 . VAL G  1 14  ? 63.169 -7.830  -18.737  1.00 20.51 ? 14   VAL H CG2 1 
ATOM   6778  N  N   . GLN G  1 15  ? 60.726 -7.867  -14.651  1.00 21.48 ? 15   GLN H N   1 
ATOM   6779  C  CA  . GLN G  1 15  ? 59.658 -8.328  -13.784  1.00 21.20 ? 15   GLN H CA  1 
ATOM   6780  C  C   . GLN G  1 15  ? 58.655 -7.229  -13.549  1.00 20.76 ? 15   GLN H C   1 
ATOM   6781  O  O   . GLN G  1 15  ? 58.982 -6.035  -13.651  1.00 20.49 ? 15   GLN H O   1 
ATOM   6782  C  CB  . GLN G  1 15  ? 60.211 -8.846  -12.432  1.00 21.73 ? 15   GLN H CB  1 
ATOM   6783  C  CG  . GLN G  1 15  ? 61.250 -7.950  -11.763  1.00 24.44 ? 15   GLN H CG  1 
ATOM   6784  C  CD  . GLN G  1 15  ? 61.923 -8.614  -10.569  1.00 28.16 ? 15   GLN H CD  1 
ATOM   6785  O  OE1 . GLN G  1 15  ? 61.322 -8.754  -9.500   1.00 29.37 ? 15   GLN H OE1 1 
ATOM   6786  N  NE2 . GLN G  1 15  ? 63.186 -9.004  -10.739  1.00 28.85 ? 15   GLN H NE2 1 
ATOM   6787  N  N   . GLY G  1 16  ? 57.430 -7.635  -13.245  1.00 19.91 ? 16   GLY H N   1 
ATOM   6788  C  CA  . GLY G  1 16  ? 56.415 -6.690  -12.853  1.00 19.39 ? 16   GLY H CA  1 
ATOM   6789  C  C   . GLY G  1 16  ? 55.061 -7.331  -12.770  1.00 19.02 ? 16   GLY H C   1 
ATOM   6790  O  O   . GLY G  1 16  ? 54.911 -8.523  -12.980  1.00 19.45 ? 16   GLY H O   1 
ATOM   6791  N  N   . ILE G  1 17  ? 54.074 -6.505  -12.467  1.00 18.62 ? 17   ILE H N   1 
ATOM   6792  C  CA  . ILE G  1 17  ? 52.738 -6.963  -12.162  1.00 17.98 ? 17   ILE H CA  1 
ATOM   6793  C  C   . ILE G  1 17  ? 51.792 -6.120  -12.981  1.00 16.81 ? 17   ILE H C   1 
ATOM   6794  O  O   . ILE G  1 17  ? 51.853 -4.892  -12.916  1.00 16.02 ? 17   ILE H O   1 
ATOM   6795  C  CB  . ILE G  1 17  ? 52.414 -6.778  -10.652  1.00 18.21 ? 17   ILE H CB  1 
ATOM   6796  C  CG1 . ILE G  1 17  ? 53.235 -7.752  -9.800   1.00 19.67 ? 17   ILE H CG1 1 
ATOM   6797  C  CG2 . ILE G  1 17  ? 50.921 -6.981  -10.403  1.00 18.08 ? 17   ILE H CG2 1 
ATOM   6798  C  CD1 . ILE G  1 17  ? 53.269 -7.413  -8.301   1.00 20.99 ? 17   ILE H CD1 1 
ATOM   6799  N  N   . ILE G  1 18  ? 50.929 -6.775  -13.757  1.00 15.50 ? 18   ILE H N   1 
ATOM   6800  C  CA  . ILE G  1 18  ? 49.939 -6.055  -14.562  1.00 15.10 ? 18   ILE H CA  1 
ATOM   6801  C  C   . ILE G  1 18  ? 48.517 -6.364  -14.082  1.00 14.51 ? 18   ILE H C   1 
ATOM   6802  O  O   . ILE G  1 18  ? 48.169 -7.523  -13.874  1.00 15.11 ? 18   ILE H O   1 
ATOM   6803  C  CB  . ILE G  1 18  ? 50.126 -6.344  -16.092  1.00 14.80 ? 18   ILE H CB  1 
ATOM   6804  C  CG1 . ILE G  1 18  ? 51.507 -5.868  -16.583  1.00 14.05 ? 18   ILE H CG1 1 
ATOM   6805  C  CG2 . ILE G  1 18  ? 49.009 -5.715  -16.927  1.00 15.03 ? 18   ILE H CG2 1 
ATOM   6806  C  CD1 . ILE G  1 18  ? 51.696 -4.340  -16.603  1.00 11.18 ? 18   ILE H CD1 1 
ATOM   6807  N  N   . ASN G  1 19  ? 47.730 -5.302  -13.903  1.00 14.16 ? 19   ASN H N   1 
ATOM   6808  C  CA  . ASN G  1 19  ? 46.334 -5.344  -13.471  1.00 13.59 ? 19   ASN H CA  1 
ATOM   6809  C  C   . ASN G  1 19  ? 45.385 -5.110  -14.634  1.00 13.00 ? 19   ASN H C   1 
ATOM   6810  O  O   . ASN G  1 19  ? 45.695 -4.328  -15.544  1.00 11.84 ? 19   ASN H O   1 
ATOM   6811  C  CB  . ASN G  1 19  ? 46.098 -4.273  -12.409  1.00 13.58 ? 19   ASN H CB  1 
ATOM   6812  C  CG  . ASN G  1 19  ? 47.048 -4.403  -11.246  1.00 15.61 ? 19   ASN H CG  1 
ATOM   6813  O  OD1 . ASN G  1 19  ? 46.918 -5.319  -10.440  1.00 16.93 ? 19   ASN H OD1 1 
ATOM   6814  N  ND2 . ASN G  1 19  ? 48.031 -3.505  -11.165  1.00 14.81 ? 19   ASN H ND2 1 
ATOM   6815  N  N   . PHE G  1 20  ? 44.237 -5.792  -14.598  1.00 12.72 ? 20   PHE H N   1 
ATOM   6816  C  CA  . PHE G  1 20  ? 43.194 -5.680  -15.602  1.00 13.17 ? 20   PHE H CA  1 
ATOM   6817  C  C   . PHE G  1 20  ? 41.878 -5.406  -14.900  1.00 13.93 ? 20   PHE H C   1 
ATOM   6818  O  O   . PHE G  1 20  ? 41.586 -6.018  -13.882  1.00 14.31 ? 20   PHE H O   1 
ATOM   6819  C  CB  . PHE G  1 20  ? 43.040 -6.987  -16.390  1.00 13.10 ? 20   PHE H CB  1 
ATOM   6820  C  CG  . PHE G  1 20  ? 44.265 -7.409  -17.150  1.00 13.08 ? 20   PHE H CG  1 
ATOM   6821  C  CD1 . PHE G  1 20  ? 44.400 -7.093  -18.503  1.00 13.78 ? 20   PHE H CD1 1 
ATOM   6822  C  CD2 . PHE G  1 20  ? 45.265 -8.162  -16.532  1.00 12.88 ? 20   PHE H CD2 1 
ATOM   6823  C  CE1 . PHE G  1 20  ? 45.533 -7.503  -19.224  1.00 13.39 ? 20   PHE H CE1 1 
ATOM   6824  C  CE2 . PHE G  1 20  ? 46.396 -8.564  -17.240  1.00 9.80  ? 20   PHE H CE2 1 
ATOM   6825  C  CZ  . PHE G  1 20  ? 46.526 -8.243  -18.584  1.00 11.09 ? 20   PHE H CZ  1 
ATOM   6826  N  N   . GLU G  1 21  ? 41.103 -4.464  -15.424  1.00 15.00 ? 21   GLU H N   1 
ATOM   6827  C  CA  . GLU G  1 21  ? 39.784 -4.166  -14.867  1.00 15.82 ? 21   GLU H CA  1 
ATOM   6828  C  C   . GLU G  1 21  ? 38.785 -3.855  -15.964  1.00 16.08 ? 21   GLU H C   1 
ATOM   6829  O  O   . GLU G  1 21  ? 39.042 -3.037  -16.872  1.00 15.43 ? 21   GLU H O   1 
ATOM   6830  C  CB  . GLU G  1 21  ? 39.826 -3.028  -13.826  1.00 17.08 ? 21   GLU H CB  1 
ATOM   6831  C  CG  . GLU G  1 21  ? 38.448 -2.637  -13.302  1.00 20.65 ? 21   GLU H CG  1 
ATOM   6832  C  CD  . GLU G  1 21  ? 38.452 -1.999  -11.912  1.00 27.27 ? 21   GLU H CD  1 
ATOM   6833  O  OE1 . GLU G  1 21  ? 37.351 -1.911  -11.322  1.00 29.52 ? 21   GLU H OE1 1 
ATOM   6834  O  OE2 . GLU G  1 21  ? 39.530 -1.593  -11.405  1.00 29.98 ? 21   GLU H OE2 1 
ATOM   6835  N  N   . GLN G  1 22  ? 37.641 -4.522  -15.881  1.00 15.07 ? 22   GLN H N   1 
ATOM   6836  C  CA  . GLN G  1 22  ? 36.594 -4.301  -16.849  1.00 15.36 ? 22   GLN H CA  1 
ATOM   6837  C  C   . GLN G  1 22  ? 35.284 -4.101  -16.082  1.00 15.66 ? 22   GLN H C   1 
ATOM   6838  O  O   . GLN G  1 22  ? 34.764 -5.027  -15.460  1.00 14.95 ? 22   GLN H O   1 
ATOM   6839  C  CB  . GLN G  1 22  ? 36.544 -5.494  -17.818  1.00 15.12 ? 22   GLN H CB  1 
ATOM   6840  C  CG  . GLN G  1 22  ? 35.606 -5.337  -19.023  1.00 14.41 ? 22   GLN H CG  1 
ATOM   6841  C  CD  . GLN G  1 22  ? 35.558 -6.590  -19.901  1.00 13.80 ? 22   GLN H CD  1 
ATOM   6842  O  OE1 . GLN G  1 22  ? 35.919 -7.698  -19.472  1.00 13.43 ? 22   GLN H OE1 1 
ATOM   6843  N  NE2 . GLN G  1 22  ? 35.124 -6.414  -21.137  1.00 10.87 ? 22   GLN H NE2 1 
ATOM   6844  N  N   . LYS G  1 23  ? 34.780 -2.875  -16.097  1.00 16.62 ? 23   LYS H N   1 
ATOM   6845  C  CA  . LYS G  1 23  ? 33.566 -2.548  -15.360  1.00 18.27 ? 23   LYS H CA  1 
ATOM   6846  C  C   . LYS G  1 23  ? 32.354 -3.337  -15.882  1.00 18.25 ? 23   LYS H C   1 
ATOM   6847  O  O   . LYS G  1 23  ? 31.535 -3.834  -15.100  1.00 18.83 ? 23   LYS H O   1 
ATOM   6848  C  CB  . LYS G  1 23  ? 33.295 -1.032  -15.411  1.00 19.02 ? 23   LYS H CB  1 
ATOM   6849  C  CG  . LYS G  1 23  ? 32.252 -0.552  -14.391  1.00 21.93 ? 23   LYS H CG  1 
ATOM   6850  C  CD  . LYS G  1 23  ? 32.639 -0.932  -12.958  1.00 24.93 ? 23   LYS H CD  1 
ATOM   6851  C  CE  . LYS G  1 23  ? 31.415 -1.266  -12.114  1.00 26.92 ? 23   LYS H CE  1 
ATOM   6852  N  NZ  . LYS G  1 23  ? 30.425 -0.140  -12.048  1.00 29.10 ? 23   LYS H NZ  1 
ATOM   6853  N  N   . GLU G  1 24  ? 32.245 -3.453  -17.198  1.00 17.88 ? 24   GLU H N   1 
ATOM   6854  C  CA  . GLU G  1 24  ? 31.086 -4.099  -17.820  1.00 18.24 ? 24   GLU H CA  1 
ATOM   6855  C  C   . GLU G  1 24  ? 31.582 -4.980  -18.940  1.00 18.20 ? 24   GLU H C   1 
ATOM   6856  O  O   . GLU G  1 24  ? 32.576 -4.645  -19.590  1.00 17.14 ? 24   GLU H O   1 
ATOM   6857  C  CB  . GLU G  1 24  ? 30.131 -3.054  -18.402  1.00 18.67 ? 24   GLU H CB  1 
ATOM   6858  C  CG  . GLU G  1 24  ? 29.650 -1.980  -17.420  1.00 19.99 ? 24   GLU H CG  1 
ATOM   6859  C  CD  . GLU G  1 24  ? 28.664 -2.519  -16.403  1.00 23.49 ? 24   GLU H CD  1 
ATOM   6860  O  OE1 . GLU G  1 24  ? 28.053 -3.589  -16.663  1.00 25.52 ? 24   GLU H OE1 1 
ATOM   6861  O  OE2 . GLU G  1 24  ? 28.511 -1.879  -15.338  1.00 24.48 ? 24   GLU H OE2 1 
ATOM   6862  N  N   . SER G  1 25  ? 30.892 -6.094  -19.194  1.00 18.15 ? 25   SER H N   1 
ATOM   6863  C  CA  . SER G  1 25  ? 31.361 -7.034  -20.227  1.00 18.14 ? 25   SER H CA  1 
ATOM   6864  C  C   . SER G  1 25  ? 31.317 -6.416  -21.637  1.00 17.70 ? 25   SER H C   1 
ATOM   6865  O  O   . SER G  1 25  ? 32.015 -6.872  -22.553  1.00 17.58 ? 25   SER H O   1 
ATOM   6866  C  CB  . SER G  1 25  ? 30.554 -8.338  -20.179  1.00 18.17 ? 25   SER H CB  1 
ATOM   6867  O  OG  . SER G  1 25  ? 29.194 -8.073  -20.455  1.00 18.20 ? 25   SER H OG  1 
ATOM   6868  N  N   . ASN G  1 26  ? 30.509 -5.373  -21.812  1.00 17.44 ? 26   ASN H N   1 
ATOM   6869  C  CA  . ASN G  1 26  ? 30.391 -4.730  -23.124  1.00 17.31 ? 26   ASN H CA  1 
ATOM   6870  C  C   . ASN G  1 26  ? 31.253 -3.473  -23.219  1.00 17.24 ? 26   ASN H C   1 
ATOM   6871  O  O   . ASN G  1 26  ? 31.075 -2.652  -24.122  1.00 17.67 ? 26   ASN H O   1 
ATOM   6872  C  CB  . ASN G  1 26  ? 28.929 -4.412  -23.455  1.00 17.95 ? 26   ASN H CB  1 
ATOM   6873  C  CG  . ASN G  1 26  ? 28.346 -3.316  -22.565  1.00 17.08 ? 26   ASN H CG  1 
ATOM   6874  O  OD1 . ASN G  1 26  ? 28.913 -2.975  -21.531  1.00 18.77 ? 26   ASN H OD1 1 
ATOM   6875  N  ND2 . ASN G  1 26  ? 27.205 -2.769  -22.966  1.00 18.83 ? 26   ASN H ND2 1 
ATOM   6876  N  N   . GLY G  1 27  ? 32.196 -3.353  -22.292  1.00 16.89 ? 27   GLY H N   1 
ATOM   6877  C  CA  . GLY G  1 27  ? 33.017 -2.149  -22.153  1.00 16.35 ? 27   GLY H CA  1 
ATOM   6878  C  C   . GLY G  1 27  ? 34.504 -2.432  -22.196  1.00 15.62 ? 27   GLY H C   1 
ATOM   6879  O  O   . GLY G  1 27  ? 34.918 -3.580  -22.259  1.00 15.83 ? 27   GLY H O   1 
ATOM   6880  N  N   . PRO G  1 28  ? 35.324 -1.370  -22.171  1.00 15.69 ? 28   PRO H N   1 
ATOM   6881  C  CA  . PRO G  1 28  ? 36.773 -1.530  -22.313  1.00 14.95 ? 28   PRO H CA  1 
ATOM   6882  C  C   . PRO G  1 28  ? 37.428 -2.136  -21.081  1.00 14.16 ? 28   PRO H C   1 
ATOM   6883  O  O   . PRO G  1 28  ? 36.862 -2.090  -19.975  1.00 14.30 ? 28   PRO H O   1 
ATOM   6884  C  CB  . PRO G  1 28  ? 37.291 -0.094  -22.541  1.00 15.40 ? 28   PRO H CB  1 
ATOM   6885  C  CG  . PRO G  1 28  ? 36.091 0.793   -22.650  1.00 16.71 ? 28   PRO H CG  1 
ATOM   6886  C  CD  . PRO G  1 28  ? 34.899 0.040   -22.124  1.00 15.71 ? 28   PRO H CD  1 
ATOM   6887  N  N   . VAL G  1 29  ? 38.622 -2.679  -21.285  1.00 12.81 ? 29   VAL H N   1 
ATOM   6888  C  CA  . VAL G  1 29  ? 39.468 -3.180  -20.216  1.00 12.72 ? 29   VAL H CA  1 
ATOM   6889  C  C   . VAL G  1 29  ? 40.600 -2.176  -19.948  1.00 13.41 ? 29   VAL H C   1 
ATOM   6890  O  O   . VAL G  1 29  ? 41.314 -1.787  -20.877  1.00 13.06 ? 29   VAL H O   1 
ATOM   6891  C  CB  . VAL G  1 29  ? 40.076 -4.521  -20.612  1.00 12.18 ? 29   VAL H CB  1 
ATOM   6892  C  CG1 . VAL G  1 29  ? 41.023 -5.039  -19.521  1.00 11.73 ? 29   VAL H CG1 1 
ATOM   6893  C  CG2 . VAL G  1 29  ? 38.956 -5.537  -20.911  1.00 11.93 ? 29   VAL H CG2 1 
ATOM   6894  N  N   . LYS G  1 30  ? 40.747 -1.758  -18.693  1.00 13.96 ? 30   LYS H N   1 
ATOM   6895  C  CA  . LYS G  1 30  ? 41.897 -0.953  -18.267  1.00 14.67 ? 30   LYS H CA  1 
ATOM   6896  C  C   . LYS G  1 30  ? 43.029 -1.901  -17.866  1.00 14.02 ? 30   LYS H C   1 
ATOM   6897  O  O   . LYS G  1 30  ? 42.807 -2.873  -17.154  1.00 13.67 ? 30   LYS H O   1 
ATOM   6898  C  CB  . LYS G  1 30  ? 41.530 -0.033  -17.093  1.00 15.37 ? 30   LYS H CB  1 
ATOM   6899  C  CG  . LYS G  1 30  ? 40.627 1.143   -17.494  1.00 18.96 ? 30   LYS H CG  1 
ATOM   6900  C  CD  . LYS G  1 30  ? 40.510 2.205   -16.395  1.00 24.59 ? 30   LYS H CD  1 
ATOM   6901  C  CE  . LYS G  1 30  ? 39.747 3.428   -16.919  1.00 26.75 ? 30   LYS H CE  1 
ATOM   6902  N  NZ  . LYS G  1 30  ? 39.082 4.226   -15.839  1.00 29.33 ? 30   LYS H NZ  1 
ATOM   6903  N  N   . VAL G  1 31  ? 44.237 -1.603  -18.334  1.00 13.69 ? 31   VAL H N   1 
ATOM   6904  C  CA  . VAL G  1 31  ? 45.421 -2.436  -18.129  1.00 13.61 ? 31   VAL H CA  1 
ATOM   6905  C  C   . VAL G  1 31  ? 46.502 -1.502  -17.566  1.00 14.22 ? 31   VAL H C   1 
ATOM   6906  O  O   . VAL G  1 31  ? 46.886 -0.511  -18.209  1.00 13.60 ? 31   VAL H O   1 
ATOM   6907  C  CB  . VAL G  1 31  ? 45.900 -3.066  -19.474  1.00 14.09 ? 31   VAL H CB  1 
ATOM   6908  C  CG1 . VAL G  1 31  ? 47.137 -3.949  -19.274  1.00 13.96 ? 31   VAL H CG1 1 
ATOM   6909  C  CG2 . VAL G  1 31  ? 44.781 -3.873  -20.159  1.00 13.05 ? 31   VAL H CG2 1 
ATOM   6910  N  N   . TRP G  1 32  ? 46.958 -1.763  -16.346  1.00 14.36 ? 32   TRP H N   1 
ATOM   6911  C  CA  . TRP G  1 32  ? 47.963 -0.890  -15.747  1.00 15.44 ? 32   TRP H CA  1 
ATOM   6912  C  C   . TRP G  1 32  ? 48.863 -1.653  -14.810  1.00 16.01 ? 32   TRP H C   1 
ATOM   6913  O  O   . TRP G  1 32  ? 48.472 -2.686  -14.259  1.00 16.28 ? 32   TRP H O   1 
ATOM   6914  C  CB  . TRP G  1 32  ? 47.333 0.316   -15.015  1.00 15.83 ? 32   TRP H CB  1 
ATOM   6915  C  CG  . TRP G  1 32  ? 46.668 -0.012  -13.676  1.00 18.22 ? 32   TRP H CG  1 
ATOM   6916  C  CD1 . TRP G  1 32  ? 47.162 0.251   -12.422  1.00 20.41 ? 32   TRP H CD1 1 
ATOM   6917  C  CD2 . TRP G  1 32  ? 45.383 -0.634  -13.478  1.00 19.81 ? 32   TRP H CD2 1 
ATOM   6918  N  NE1 . TRP G  1 32  ? 46.263 -0.188  -11.456  1.00 21.78 ? 32   TRP H NE1 1 
ATOM   6919  C  CE2 . TRP G  1 32  ? 45.169 -0.729  -12.082  1.00 21.09 ? 32   TRP H CE2 1 
ATOM   6920  C  CE3 . TRP G  1 32  ? 44.399 -1.131  -14.348  1.00 22.16 ? 32   TRP H CE3 1 
ATOM   6921  C  CZ2 . TRP G  1 32  ? 44.009 -1.295  -11.540  1.00 22.31 ? 32   TRP H CZ2 1 
ATOM   6922  C  CZ3 . TRP G  1 32  ? 43.244 -1.698  -13.805  1.00 21.32 ? 32   TRP H CZ3 1 
ATOM   6923  C  CH2 . TRP G  1 32  ? 43.060 -1.771  -12.416  1.00 22.00 ? 32   TRP H CH2 1 
ATOM   6924  N  N   . GLY G  1 33  ? 50.056 -1.109  -14.618  1.00 16.39 ? 33   GLY H N   1 
ATOM   6925  C  CA  . GLY G  1 33  ? 51.023 -1.683  -13.710  1.00 17.88 ? 33   GLY H CA  1 
ATOM   6926  C  C   . GLY G  1 33  ? 52.421 -1.234  -14.037  1.00 18.58 ? 33   GLY H C   1 
ATOM   6927  O  O   . GLY G  1 33  ? 52.651 -0.399  -14.918  1.00 18.34 ? 33   GLY H O   1 
ATOM   6928  N  N   . SER G  1 34  ? 53.369 -1.804  -13.315  1.00 19.69 ? 34   SER H N   1 
ATOM   6929  C  CA  . SER G  1 34  ? 54.754 -1.414  -13.445  1.00 20.19 ? 34   SER H CA  1 
ATOM   6930  C  C   . SER G  1 34  ? 55.597 -2.620  -13.858  1.00 20.16 ? 34   SER H C   1 
ATOM   6931  O  O   . SER G  1 34  ? 55.489 -3.687  -13.268  1.00 20.54 ? 34   SER H O   1 
ATOM   6932  C  CB  . SER G  1 34  ? 55.223 -0.821  -12.112  1.00 20.53 ? 34   SER H CB  1 
ATOM   6933  O  OG  . SER G  1 34  ? 56.602 -0.545  -12.130  1.00 22.54 ? 34   SER H OG  1 
ATOM   6934  N  N   . ILE G  1 35  ? 56.410 -2.447  -14.892  1.00 19.70 ? 35   ILE H N   1 
ATOM   6935  C  CA  . ILE G  1 35  ? 57.399 -3.450  -15.291  1.00 19.76 ? 35   ILE H CA  1 
ATOM   6936  C  C   . ILE G  1 35  ? 58.802 -2.841  -15.198  1.00 19.96 ? 35   ILE H C   1 
ATOM   6937  O  O   . ILE G  1 35  ? 59.068 -1.777  -15.785  1.00 19.35 ? 35   ILE H O   1 
ATOM   6938  C  CB  . ILE G  1 35  ? 57.150 -3.970  -16.731  1.00 19.52 ? 35   ILE H CB  1 
ATOM   6939  C  CG1 . ILE G  1 35  ? 55.694 -4.416  -16.909  1.00 18.21 ? 35   ILE H CG1 1 
ATOM   6940  C  CG2 . ILE G  1 35  ? 58.122 -5.107  -17.083  1.00 19.66 ? 35   ILE H CG2 1 
ATOM   6941  C  CD1 . ILE G  1 35  ? 55.333 -4.748  -18.358  1.00 16.39 ? 35   ILE H CD1 1 
ATOM   6942  N  N   . LYS G  1 36  ? 59.675 -3.529  -14.454  1.00 20.28 ? 36   LYS H N   1 
ATOM   6943  C  CA  . LYS G  1 36  ? 61.062 -3.119  -14.200  1.00 21.00 ? 36   LYS H CA  1 
ATOM   6944  C  C   . LYS G  1 36  ? 62.039 -4.012  -14.963  1.00 20.56 ? 36   LYS H C   1 
ATOM   6945  O  O   . LYS G  1 36  ? 61.669 -5.089  -15.407  1.00 20.65 ? 36   LYS H O   1 
ATOM   6946  C  CB  . LYS G  1 36  ? 61.383 -3.243  -12.696  1.00 21.14 ? 36   LYS H CB  1 
ATOM   6947  C  CG  . LYS G  1 36  ? 60.703 -2.230  -11.783  1.00 23.16 ? 36   LYS H CG  1 
ATOM   6948  C  CD  . LYS G  1 36  ? 61.359 -2.203  -10.379  1.00 25.75 ? 36   LYS H CD  1 
ATOM   6949  C  CE  . LYS G  1 36  ? 62.804 -1.649  -10.396  1.00 28.01 ? 36   LYS H CE  1 
ATOM   6950  N  NZ  . LYS G  1 36  ? 62.897 -0.147  -10.533  1.00 26.91 ? 36   LYS H NZ  1 
ATOM   6951  N  N   . GLY G  1 37  ? 63.288 -3.564  -15.098  1.00 20.69 ? 37   GLY H N   1 
ATOM   6952  C  CA  . GLY G  1 37  ? 64.363 -4.379  -15.667  1.00 19.83 ? 37   GLY H CA  1 
ATOM   6953  C  C   . GLY G  1 37  ? 64.555 -4.242  -17.165  1.00 20.19 ? 37   GLY H C   1 
ATOM   6954  O  O   . GLY G  1 37  ? 65.357 -4.968  -17.765  1.00 20.07 ? 37   GLY H O   1 
ATOM   6955  N  N   . LEU G  1 38  ? 63.820 -3.303  -17.768  1.00 19.73 ? 38   LEU H N   1 
ATOM   6956  C  CA  . LEU G  1 38  ? 63.771 -3.132  -19.216  1.00 19.66 ? 38   LEU H CA  1 
ATOM   6957  C  C   . LEU G  1 38  ? 64.778 -2.114  -19.716  1.00 20.13 ? 38   LEU H C   1 
ATOM   6958  O  O   . LEU G  1 38  ? 65.093 -1.149  -19.015  1.00 20.57 ? 38   LEU H O   1 
ATOM   6959  C  CB  . LEU G  1 38  ? 62.373 -2.648  -19.629  1.00 19.39 ? 38   LEU H CB  1 
ATOM   6960  C  CG  . LEU G  1 38  ? 61.231 -3.649  -19.559  1.00 18.13 ? 38   LEU H CG  1 
ATOM   6961  C  CD1 . LEU G  1 38  ? 59.881 -2.897  -19.508  1.00 19.25 ? 38   LEU H CD1 1 
ATOM   6962  C  CD2 . LEU G  1 38  ? 61.303 -4.603  -20.728  1.00 18.07 ? 38   LEU H CD2 1 
ATOM   6963  N  N   . THR G  1 39  ? 65.252 -2.321  -20.940  1.00 19.66 ? 39   THR H N   1 
ATOM   6964  C  CA  . THR G  1 39  ? 66.014 -1.302  -21.645  1.00 19.93 ? 39   THR H CA  1 
ATOM   6965  C  C   . THR G  1 39  ? 65.083 -0.121  -21.974  1.00 19.56 ? 39   THR H C   1 
ATOM   6966  O  O   . THR G  1 39  ? 63.884 -0.321  -22.234  1.00 19.06 ? 39   THR H O   1 
ATOM   6967  C  CB  . THR G  1 39  ? 66.656 -1.865  -22.917  1.00 20.11 ? 39   THR H CB  1 
ATOM   6968  O  OG1 . THR G  1 39  ? 65.636 -2.386  -23.778  1.00 20.63 ? 39   THR H OG1 1 
ATOM   6969  C  CG2 . THR G  1 39  ? 67.617 -2.992  -22.567  1.00 19.91 ? 39   THR H CG2 1 
ATOM   6970  N  N   . GLU G  1 40  ? 65.615 1.101   -21.896  1.00 18.99 ? 40   GLU H N   1 
ATOM   6971  C  CA  . GLU G  1 40  ? 64.835 2.310   -22.188  1.00 18.98 ? 40   GLU H CA  1 
ATOM   6972  C  C   . GLU G  1 40  ? 64.257 2.230   -23.599  1.00 17.78 ? 40   GLU H C   1 
ATOM   6973  O  O   . GLU G  1 40  ? 64.935 1.823   -24.535  1.00 18.03 ? 40   GLU H O   1 
ATOM   6974  C  CB  . GLU G  1 40  ? 65.709 3.563   -22.043  1.00 19.24 ? 40   GLU H CB  1 
ATOM   6975  C  CG  . GLU G  1 40  ? 64.977 4.906   -22.237  1.00 20.64 ? 40   GLU H CG  1 
ATOM   6976  C  CD  . GLU G  1 40  ? 65.928 6.105   -22.292  1.00 24.20 ? 40   GLU H CD  1 
ATOM   6977  O  OE1 . GLU G  1 40  ? 65.438 7.257   -22.384  1.00 24.79 ? 40   GLU H OE1 1 
ATOM   6978  O  OE2 . GLU G  1 40  ? 67.163 5.893   -22.261  1.00 24.82 ? 40   GLU H OE2 1 
ATOM   6979  N  N   . GLY G  1 41  ? 62.997 2.613   -23.747  1.00 17.28 ? 41   GLY H N   1 
ATOM   6980  C  CA  . GLY G  1 41  ? 62.381 2.624   -25.067  1.00 15.29 ? 41   GLY H CA  1 
ATOM   6981  C  C   . GLY G  1 41  ? 61.222 1.655   -25.230  1.00 14.85 ? 41   GLY H C   1 
ATOM   6982  O  O   . GLY G  1 41  ? 60.581 1.260   -24.244  1.00 13.39 ? 41   GLY H O   1 
ATOM   6983  N  N   . LEU G  1 42  ? 60.961 1.274   -26.486  1.00 13.44 ? 42   LEU H N   1 
ATOM   6984  C  CA  . LEU G  1 42  ? 59.759 0.513   -26.833  1.00 13.39 ? 42   LEU H CA  1 
ATOM   6985  C  C   . LEU G  1 42  ? 59.918 -0.987  -26.663  1.00 13.87 ? 42   LEU H C   1 
ATOM   6986  O  O   . LEU G  1 42  ? 60.907 -1.556  -27.108  1.00 13.21 ? 42   LEU H O   1 
ATOM   6987  C  CB  . LEU G  1 42  ? 59.334 0.803   -28.280  1.00 12.93 ? 42   LEU H CB  1 
ATOM   6988  C  CG  . LEU G  1 42  ? 58.902 2.252   -28.549  1.00 13.59 ? 42   LEU H CG  1 
ATOM   6989  C  CD1 . LEU G  1 42  ? 58.706 2.497   -30.036  1.00 13.29 ? 42   LEU H CD1 1 
ATOM   6990  C  CD2 . LEU G  1 42  ? 57.631 2.586   -27.792  1.00 13.35 ? 42   LEU H CD2 1 
ATOM   6991  N  N   . HIS G  1 43  ? 58.923 -1.617  -26.031  1.00 13.43 ? 43   HIS H N   1 
ATOM   6992  C  CA  . HIS G  1 43  ? 58.872 -3.074  -25.965  1.00 13.69 ? 43   HIS H CA  1 
ATOM   6993  C  C   . HIS G  1 43  ? 57.505 -3.625  -26.340  1.00 12.84 ? 43   HIS H C   1 
ATOM   6994  O  O   . HIS G  1 43  ? 56.485 -3.165  -25.809  1.00 13.30 ? 43   HIS H O   1 
ATOM   6995  C  CB  . HIS G  1 43  ? 59.315 -3.527  -24.575  1.00 14.11 ? 43   HIS H CB  1 
ATOM   6996  C  CG  . HIS G  1 43  ? 60.721 -3.124  -24.267  1.00 16.34 ? 43   HIS H CG  1 
ATOM   6997  N  ND1 . HIS G  1 43  ? 61.799 -3.936  -24.543  1.00 19.02 ? 43   HIS H ND1 1 
ATOM   6998  C  CD2 . HIS G  1 43  ? 61.235 -1.965  -23.793  1.00 18.99 ? 43   HIS H CD2 1 
ATOM   6999  C  CE1 . HIS G  1 43  ? 62.915 -3.310  -24.214  1.00 19.84 ? 43   HIS H CE1 1 
ATOM   7000  N  NE2 . HIS G  1 43  ? 62.602 -2.110  -23.762  1.00 18.92 ? 43   HIS H NE2 1 
ATOM   7001  N  N   . GLY G  1 44  ? 57.488 -4.598  -27.257  1.00 12.59 ? 44   GLY H N   1 
ATOM   7002  C  CA  . GLY G  1 44  ? 56.243 -5.292  -27.646  1.00 12.78 ? 44   GLY H CA  1 
ATOM   7003  C  C   . GLY G  1 44  ? 55.506 -5.913  -26.456  1.00 12.79 ? 44   GLY H C   1 
ATOM   7004  O  O   . GLY G  1 44  ? 56.120 -6.335  -25.474  1.00 12.88 ? 44   GLY H O   1 
ATOM   7005  N  N   . PHE G  1 45  ? 54.186 -5.944  -26.518  1.00 12.79 ? 45   PHE H N   1 
ATOM   7006  C  CA  . PHE G  1 45  ? 53.377 -6.260  -25.335  1.00 12.97 ? 45   PHE H CA  1 
ATOM   7007  C  C   . PHE G  1 45  ? 52.073 -6.891  -25.813  1.00 13.16 ? 45   PHE H C   1 
ATOM   7008  O  O   . PHE G  1 45  ? 51.175 -6.204  -26.280  1.00 13.57 ? 45   PHE H O   1 
ATOM   7009  C  CB  . PHE G  1 45  ? 53.151 -4.967  -24.544  1.00 12.79 ? 45   PHE H CB  1 
ATOM   7010  C  CG  . PHE G  1 45  ? 52.492 -5.130  -23.183  1.00 12.15 ? 45   PHE H CG  1 
ATOM   7011  C  CD1 . PHE G  1 45  ? 53.118 -5.819  -22.147  1.00 11.58 ? 45   PHE H CD1 1 
ATOM   7012  C  CD2 . PHE G  1 45  ? 51.268 -4.502  -22.919  1.00 11.25 ? 45   PHE H CD2 1 
ATOM   7013  C  CE1 . PHE G  1 45  ? 52.522 -5.914  -20.887  1.00 9.86  ? 45   PHE H CE1 1 
ATOM   7014  C  CE2 . PHE G  1 45  ? 50.658 -4.591  -21.653  1.00 10.40 ? 45   PHE H CE2 1 
ATOM   7015  C  CZ  . PHE G  1 45  ? 51.298 -5.292  -20.634  1.00 10.14 ? 45   PHE H CZ  1 
ATOM   7016  N  N   . HIS G  1 46  ? 51.972 -8.212  -25.693  1.00 13.73 ? 46   HIS H N   1 
ATOM   7017  C  CA  . HIS G  1 46  ? 50.829 -8.914  -26.256  1.00 13.30 ? 46   HIS H CA  1 
ATOM   7018  C  C   . HIS G  1 46  ? 50.259 -9.963  -25.313  1.00 13.87 ? 46   HIS H C   1 
ATOM   7019  O  O   . HIS G  1 46  ? 50.962 -10.441 -24.401  1.00 13.09 ? 46   HIS H O   1 
ATOM   7020  C  CB  . HIS G  1 46  ? 51.190 -9.605  -27.578  1.00 13.88 ? 46   HIS H CB  1 
ATOM   7021  C  CG  . HIS G  1 46  ? 52.142 -8.841  -28.446  1.00 13.85 ? 46   HIS H CG  1 
ATOM   7022  N  ND1 . HIS G  1 46  ? 53.425 -9.276  -28.694  1.00 12.83 ? 46   HIS H ND1 1 
ATOM   7023  C  CD2 . HIS G  1 46  ? 51.991 -7.699  -29.155  1.00 11.95 ? 46   HIS H CD2 1 
ATOM   7024  C  CE1 . HIS G  1 46  ? 54.032 -8.427  -29.500  1.00 14.20 ? 46   HIS H CE1 1 
ATOM   7025  N  NE2 . HIS G  1 46  ? 53.181 -7.463  -29.802  1.00 11.11 ? 46   HIS H NE2 1 
ATOM   7026  N  N   . VAL G  1 47  ? 48.999 -10.329 -25.554  1.00 13.40 ? 47   VAL H N   1 
ATOM   7027  C  CA  . VAL G  1 47  ? 48.422 -11.517 -24.938  1.00 13.67 ? 47   VAL H CA  1 
ATOM   7028  C  C   . VAL G  1 47  ? 48.677 -12.621 -25.952  1.00 13.57 ? 47   VAL H C   1 
ATOM   7029  O  O   . VAL G  1 47  ? 48.300 -12.505 -27.125  1.00 13.60 ? 47   VAL H O   1 
ATOM   7030  C  CB  . VAL G  1 47  ? 46.909 -11.398 -24.691  1.00 14.09 ? 47   VAL H CB  1 
ATOM   7031  C  CG1 . VAL G  1 47  ? 46.301 -12.747 -24.181  1.00 14.23 ? 47   VAL H CG1 1 
ATOM   7032  C  CG2 . VAL G  1 47  ? 46.609 -10.265 -23.716  1.00 12.66 ? 47   VAL H CG2 1 
ATOM   7033  N  N   . HIS G  1 48  ? 49.349 -13.676 -25.506  1.00 13.91 ? 48   HIS H N   1 
ATOM   7034  C  CA  . HIS G  1 48  ? 49.586 -14.848 -26.356  1.00 14.46 ? 48   HIS H CA  1 
ATOM   7035  C  C   . HIS G  1 48  ? 48.582 -15.949 -26.051  1.00 15.08 ? 48   HIS H C   1 
ATOM   7036  O  O   . HIS G  1 48  ? 47.921 -15.929 -25.007  1.00 15.94 ? 48   HIS H O   1 
ATOM   7037  C  CB  . HIS G  1 48  ? 50.998 -15.383 -26.160  1.00 14.10 ? 48   HIS H CB  1 
ATOM   7038  C  CG  . HIS G  1 48  ? 52.060 -14.525 -26.754  1.00 14.97 ? 48   HIS H CG  1 
ATOM   7039  N  ND1 . HIS G  1 48  ? 52.928 -14.986 -27.720  1.00 14.91 ? 48   HIS H ND1 1 
ATOM   7040  C  CD2 . HIS G  1 48  ? 52.410 -13.240 -26.509  1.00 14.41 ? 48   HIS H CD2 1 
ATOM   7041  C  CE1 . HIS G  1 48  ? 53.768 -14.019 -28.049  1.00 15.00 ? 48   HIS H CE1 1 
ATOM   7042  N  NE2 . HIS G  1 48  ? 53.471 -12.948 -27.332  1.00 15.46 ? 48   HIS H NE2 1 
ATOM   7043  N  N   . GLU G  1 49  ? 48.505 -16.934 -26.941  1.00 15.18 ? 49   GLU H N   1 
ATOM   7044  C  CA  . GLU G  1 49  ? 47.341 -17.813 -27.012  1.00 15.74 ? 49   GLU H CA  1 
ATOM   7045  C  C   . GLU G  1 49  ? 47.171 -18.734 -25.786  1.00 16.60 ? 49   GLU H C   1 
ATOM   7046  O  O   . GLU G  1 49  ? 46.075 -18.808 -25.227  1.00 16.52 ? 49   GLU H O   1 
ATOM   7047  C  CB  . GLU G  1 49  ? 47.358 -18.602 -28.327  1.00 16.13 ? 49   GLU H CB  1 
ATOM   7048  C  CG  . GLU G  1 49  ? 46.118 -19.475 -28.540  1.00 16.69 ? 49   GLU H CG  1 
ATOM   7049  C  CD  . GLU G  1 49  ? 46.163 -20.324 -29.818  1.00 19.21 ? 49   GLU H CD  1 
ATOM   7050  O  OE1 . GLU G  1 49  ? 45.140 -20.988 -30.091  1.00 19.11 ? 49   GLU H OE1 1 
ATOM   7051  O  OE2 . GLU G  1 49  ? 47.177 -20.307 -30.561  1.00 17.87 ? 49   GLU H OE2 1 
ATOM   7052  N  N   . PHE G  1 50  ? 48.255 -19.384 -25.355  1.00 16.67 ? 50   PHE H N   1 
ATOM   7053  C  CA  . PHE G  1 50  ? 48.188 -20.349 -24.242  1.00 17.43 ? 50   PHE H CA  1 
ATOM   7054  C  C   . PHE G  1 50  ? 48.725 -19.895 -22.886  1.00 17.66 ? 50   PHE H C   1 
ATOM   7055  O  O   . PHE G  1 50  ? 49.793 -19.258 -22.789  1.00 16.80 ? 50   PHE H O   1 
ATOM   7056  C  CB  . PHE G  1 50  ? 48.901 -21.636 -24.630  1.00 17.87 ? 50   PHE H CB  1 
ATOM   7057  C  CG  . PHE G  1 50  ? 48.565 -22.117 -26.003  1.00 18.30 ? 50   PHE H CG  1 
ATOM   7058  C  CD1 . PHE G  1 50  ? 47.262 -22.494 -26.324  1.00 20.67 ? 50   PHE H CD1 1 
ATOM   7059  C  CD2 . PHE G  1 50  ? 49.556 -22.216 -26.972  1.00 21.12 ? 50   PHE H CD2 1 
ATOM   7060  C  CE1 . PHE G  1 50  ? 46.948 -22.951 -27.605  1.00 21.29 ? 50   PHE H CE1 1 
ATOM   7061  C  CE2 . PHE G  1 50  ? 49.261 -22.674 -28.251  1.00 21.99 ? 50   PHE H CE2 1 
ATOM   7062  C  CZ  . PHE G  1 50  ? 47.954 -23.032 -28.573  1.00 22.58 ? 50   PHE H CZ  1 
ATOM   7063  N  N   . GLY G  1 51  ? 47.993 -20.267 -21.837  1.00 17.69 ? 51   GLY H N   1 
ATOM   7064  C  CA  . GLY G  1 51  ? 48.450 -20.068 -20.478  1.00 19.01 ? 51   GLY H CA  1 
ATOM   7065  C  C   . GLY G  1 51  ? 49.390 -21.190 -20.072  1.00 20.46 ? 51   GLY H C   1 
ATOM   7066  O  O   . GLY G  1 51  ? 49.250 -21.754 -18.991  1.00 19.62 ? 51   GLY H O   1 
ATOM   7067  N  N   . ASP G  1 52  ? 50.344 -21.501 -20.949  1.00 21.56 ? 52   ASP H N   1 
ATOM   7068  C  CA  . ASP G  1 52  ? 51.253 -22.615 -20.758  1.00 22.71 ? 52   ASP H CA  1 
ATOM   7069  C  C   . ASP G  1 52  ? 52.666 -22.092 -20.616  1.00 23.98 ? 52   ASP H C   1 
ATOM   7070  O  O   . ASP G  1 52  ? 53.282 -21.682 -21.596  1.00 24.19 ? 52   ASP H O   1 
ATOM   7071  C  CB  . ASP G  1 52  ? 51.151 -23.582 -21.938  1.00 23.05 ? 52   ASP H CB  1 
ATOM   7072  C  CG  . ASP G  1 52  ? 52.008 -24.827 -21.761  1.00 23.47 ? 52   ASP H CG  1 
ATOM   7073  O  OD1 . ASP G  1 52  ? 51.633 -25.893 -22.297  1.00 22.86 ? 52   ASP H OD1 1 
ATOM   7074  O  OD2 . ASP G  1 52  ? 53.054 -24.749 -21.091  1.00 23.09 ? 52   ASP H OD2 1 
ATOM   7075  N  N   . ASN G  1 53  ? 53.174 -22.085 -19.386  1.00 25.13 ? 53   ASN H N   1 
ATOM   7076  C  CA  . ASN G  1 53  ? 54.550 -21.663 -19.145  1.00 26.28 ? 53   ASN H CA  1 
ATOM   7077  C  C   . ASN G  1 53  ? 55.431 -22.831 -18.653  1.00 26.59 ? 53   ASN H C   1 
ATOM   7078  O  O   . ASN G  1 53  ? 56.367 -22.629 -17.882  1.00 26.69 ? 53   ASN H O   1 
ATOM   7079  C  CB  . ASN G  1 53  ? 54.600 -20.433 -18.210  1.00 26.28 ? 53   ASN H CB  1 
ATOM   7080  C  CG  . ASN G  1 53  ? 54.025 -19.129 -18.864  1.00 28.06 ? 53   ASN H CG  1 
ATOM   7081  O  OD1 . ASN G  1 53  ? 53.863 -18.105 -18.178  1.00 28.01 ? 53   ASN H OD1 1 
ATOM   7082  N  ND2 . ASN G  1 53  ? 53.746 -19.166 -20.176  1.00 26.17 ? 53   ASN H ND2 1 
ATOM   7083  N  N   . THR G  1 54  ? 55.129 -24.047 -19.117  1.00 27.10 ? 54   THR H N   1 
ATOM   7084  C  CA  . THR G  1 54  ? 55.941 -25.235 -18.777  1.00 27.76 ? 54   THR H CA  1 
ATOM   7085  C  C   . THR G  1 54  ? 57.322 -25.181 -19.427  1.00 28.04 ? 54   THR H C   1 
ATOM   7086  O  O   . THR G  1 54  ? 58.294 -25.705 -18.874  1.00 28.39 ? 54   THR H O   1 
ATOM   7087  C  CB  . THR G  1 54  ? 55.270 -26.573 -19.190  1.00 27.83 ? 54   THR H CB  1 
ATOM   7088  O  OG1 . THR G  1 54  ? 54.961 -26.553 -20.589  1.00 28.31 ? 54   THR H OG1 1 
ATOM   7089  C  CG2 . THR G  1 54  ? 54.005 -26.837 -18.383  1.00 28.12 ? 54   THR H CG2 1 
ATOM   7090  N  N   . ALA G  1 55  ? 57.400 -24.563 -20.606  1.00 28.11 ? 55   ALA H N   1 
ATOM   7091  C  CA  . ALA G  1 55  ? 58.671 -24.326 -21.289  1.00 27.86 ? 55   ALA H CA  1 
ATOM   7092  C  C   . ALA G  1 55  ? 58.974 -22.821 -21.361  1.00 27.77 ? 55   ALA H C   1 
ATOM   7093  O  O   . ALA G  1 55  ? 59.324 -22.291 -22.423  1.00 27.93 ? 55   ALA H O   1 
ATOM   7094  C  CB  . ALA G  1 55  ? 58.652 -24.951 -22.684  1.00 27.99 ? 55   ALA H CB  1 
ATOM   7095  N  N   . GLY G  1 56  ? 58.836 -22.143 -20.221  1.00 27.23 ? 56   GLY H N   1 
ATOM   7096  C  CA  . GLY G  1 56  ? 59.069 -20.695 -20.131  1.00 26.67 ? 56   GLY H CA  1 
ATOM   7097  C  C   . GLY G  1 56  ? 58.022 -19.910 -20.903  1.00 25.80 ? 56   GLY H C   1 
ATOM   7098  O  O   . GLY G  1 56  ? 56.857 -20.318 -20.960  1.00 25.96 ? 56   GLY H O   1 
ATOM   7099  N  N   . CYS G  1 57  ? 58.433 -18.798 -21.515  1.00 24.64 ? 57   CYS H N   1 
ATOM   7100  C  CA  . CYS G  1 57  ? 57.521 -17.988 -22.325  1.00 23.27 ? 57   CYS H CA  1 
ATOM   7101  C  C   . CYS G  1 57  ? 57.247 -18.601 -23.715  1.00 23.42 ? 57   CYS H C   1 
ATOM   7102  O  O   . CYS G  1 57  ? 56.253 -18.270 -24.371  1.00 23.02 ? 57   CYS H O   1 
ATOM   7103  C  CB  . CYS G  1 57  ? 58.040 -16.553 -22.449  0.40 22.63 ? 57   CYS H CB  1 
ATOM   7104  S  SG  . CYS G  1 57  ? 58.191 -15.642 -20.889  0.40 19.09 ? 57   CYS H SG  1 
ATOM   7105  N  N   . THR G  1 58  ? 58.116 -19.506 -24.159  1.00 23.74 ? 58   THR H N   1 
ATOM   7106  C  CA  . THR G  1 58  ? 57.949 -20.147 -25.469  1.00 23.36 ? 58   THR H CA  1 
ATOM   7107  C  C   . THR G  1 58  ? 56.666 -20.971 -25.609  1.00 23.11 ? 58   THR H C   1 
ATOM   7108  O  O   . THR G  1 58  ? 56.032 -20.956 -26.670  1.00 22.95 ? 58   THR H O   1 
ATOM   7109  C  CB  . THR G  1 58  ? 59.172 -21.004 -25.848  1.00 23.91 ? 58   THR H CB  1 
ATOM   7110  O  OG1 . THR G  1 58  ? 60.355 -20.212 -25.699  1.00 24.45 ? 58   THR H OG1 1 
ATOM   7111  C  CG2 . THR G  1 58  ? 59.067 -21.500 -27.306  1.00 23.59 ? 58   THR H CG2 1 
ATOM   7112  N  N   . SER G  1 59  ? 56.273 -21.673 -24.546  1.00 22.50 ? 59   SER H N   1 
ATOM   7113  C  CA  . SER G  1 59  ? 55.086 -22.539 -24.618  1.00 22.33 ? 59   SER H CA  1 
ATOM   7114  C  C   . SER G  1 59  ? 53.752 -21.774 -24.603  1.00 21.71 ? 59   SER H C   1 
ATOM   7115  O  O   . SER G  1 59  ? 52.691 -22.382 -24.645  1.00 22.01 ? 59   SER H O   1 
ATOM   7116  C  CB  . SER G  1 59  ? 55.121 -23.633 -23.547  1.00 22.37 ? 59   SER H CB  1 
ATOM   7117  O  OG  . SER G  1 59  ? 55.524 -23.130 -22.292  1.00 23.10 ? 59   SER H OG  1 
ATOM   7118  N  N   . ALA G  1 60  ? 53.826 -20.444 -24.560  1.00 20.99 ? 60   ALA H N   1 
ATOM   7119  C  CA  . ALA G  1 60  ? 52.639 -19.561 -24.649  1.00 19.87 ? 60   ALA H CA  1 
ATOM   7120  C  C   . ALA G  1 60  ? 52.050 -19.509 -26.066  1.00 19.27 ? 60   ALA H C   1 
ATOM   7121  O  O   . ALA G  1 60  ? 50.888 -19.110 -26.268  1.00 18.33 ? 60   ALA H O   1 
ATOM   7122  C  CB  . ALA G  1 60  ? 52.993 -18.153 -24.168  1.00 19.61 ? 60   ALA H CB  1 
ATOM   7123  N  N   . GLY G  1 61  ? 52.863 -19.906 -27.044  1.00 18.21 ? 61   GLY H N   1 
ATOM   7124  C  CA  . GLY G  1 61  ? 52.415 -19.994 -28.413  1.00 16.92 ? 61   GLY H CA  1 
ATOM   7125  C  C   . GLY G  1 61  ? 52.423 -18.613 -29.057  1.00 16.60 ? 61   GLY H C   1 
ATOM   7126  O  O   . GLY G  1 61  ? 53.119 -17.719 -28.582  1.00 16.94 ? 61   GLY H O   1 
ATOM   7127  N  N   . PRO G  1 62  ? 51.661 -18.446 -30.149  1.00 15.92 ? 62   PRO H N   1 
ATOM   7128  C  CA  . PRO G  1 62  ? 51.633 -17.189 -30.908  1.00 14.86 ? 62   PRO H CA  1 
ATOM   7129  C  C   . PRO G  1 62  ? 50.664 -16.201 -30.279  1.00 14.60 ? 62   PRO H C   1 
ATOM   7130  O  O   . PRO G  1 62  ? 50.086 -16.483 -29.226  1.00 14.04 ? 62   PRO H O   1 
ATOM   7131  C  CB  . PRO G  1 62  ? 51.124 -17.642 -32.278  1.00 15.09 ? 62   PRO H CB  1 
ATOM   7132  C  CG  . PRO G  1 62  ? 50.140 -18.731 -31.952  1.00 14.50 ? 62   PRO H CG  1 
ATOM   7133  C  CD  . PRO G  1 62  ? 50.696 -19.424 -30.692  1.00 15.65 ? 62   PRO H CD  1 
ATOM   7134  N  N   . HIS G  1 63  ? 50.474 -15.054 -30.927  1.00 13.77 ? 63   HIS H N   1 
ATOM   7135  C  CA  . HIS G  1 63  ? 49.548 -14.069 -30.413  1.00 13.84 ? 63   HIS H CA  1 
ATOM   7136  C  C   . HIS G  1 63  ? 48.121 -14.618 -30.357  1.00 13.94 ? 63   HIS H C   1 
ATOM   7137  O  O   . HIS G  1 63  ? 47.658 -15.301 -31.288  1.00 13.94 ? 63   HIS H O   1 
ATOM   7138  C  CB  . HIS G  1 63  ? 49.626 -12.791 -31.252  1.00 13.78 ? 63   HIS H CB  1 
ATOM   7139  C  CG  . HIS G  1 63  ? 50.986 -12.150 -31.252  1.00 12.75 ? 63   HIS H CG  1 
ATOM   7140  N  ND1 . HIS G  1 63  ? 51.229 -10.923 -31.830  1.00 11.46 ? 63   HIS H ND1 1 
ATOM   7141  C  CD2 . HIS G  1 63  ? 52.167 -12.547 -30.718  1.00 12.04 ? 63   HIS H CD2 1 
ATOM   7142  C  CE1 . HIS G  1 63  ? 52.505 -10.606 -31.684  1.00 11.00 ? 63   HIS H CE1 1 
ATOM   7143  N  NE2 . HIS G  1 63  ? 53.098 -11.575 -31.007  1.00 10.35 ? 63   HIS H NE2 1 
ATOM   7144  N  N   . PHE G  1 64  ? 47.423 -14.316 -29.266  1.00 13.17 ? 64   PHE H N   1 
ATOM   7145  C  CA  . PHE G  1 64  ? 46.016 -14.687 -29.150  1.00 12.89 ? 64   PHE H CA  1 
ATOM   7146  C  C   . PHE G  1 64  ? 45.218 -14.059 -30.305  1.00 13.17 ? 64   PHE H C   1 
ATOM   7147  O  O   . PHE G  1 64  ? 45.157 -12.839 -30.462  1.00 12.13 ? 64   PHE H O   1 
ATOM   7148  C  CB  . PHE G  1 64  ? 45.463 -14.324 -27.761  1.00 12.66 ? 64   PHE H CB  1 
ATOM   7149  C  CG  . PHE G  1 64  ? 44.010 -14.639 -27.574  1.00 12.83 ? 64   PHE H CG  1 
ATOM   7150  C  CD1 . PHE G  1 64  ? 43.148 -13.681 -27.042  1.00 11.57 ? 64   PHE H CD1 1 
ATOM   7151  C  CD2 . PHE G  1 64  ? 43.493 -15.894 -27.914  1.00 12.44 ? 64   PHE H CD2 1 
ATOM   7152  C  CE1 . PHE G  1 64  ? 41.793 -13.959 -26.852  1.00 11.12 ? 64   PHE H CE1 1 
ATOM   7153  C  CE2 . PHE G  1 64  ? 42.152 -16.181 -27.729  1.00 13.48 ? 64   PHE H CE2 1 
ATOM   7154  C  CZ  . PHE G  1 64  ? 41.290 -15.210 -27.198  1.00 14.20 ? 64   PHE H CZ  1 
ATOM   7155  N  N   . ASN G  1 65  ? 44.615 -14.915 -31.125  1.00 13.24 ? 65   ASN H N   1 
ATOM   7156  C  CA  . ASN G  1 65  ? 44.070 -14.487 -32.406  1.00 13.59 ? 65   ASN H CA  1 
ATOM   7157  C  C   . ASN G  1 65  ? 42.862 -15.339 -32.784  1.00 13.86 ? 65   ASN H C   1 
ATOM   7158  O  O   . ASN G  1 65  ? 42.879 -15.977 -33.825  1.00 14.07 ? 65   ASN H O   1 
ATOM   7159  C  CB  . ASN G  1 65  ? 45.195 -14.571 -33.470  1.00 13.03 ? 65   ASN H CB  1 
ATOM   7160  C  CG  . ASN G  1 65  ? 44.774 -14.087 -34.873  1.00 13.17 ? 65   ASN H CG  1 
ATOM   7161  O  OD1 . ASN G  1 65  ? 43.810 -13.338 -35.052  1.00 12.79 ? 65   ASN H OD1 1 
ATOM   7162  N  ND2 . ASN G  1 65  ? 45.522 -14.532 -35.874  1.00 12.46 ? 65   ASN H ND2 1 
ATOM   7163  N  N   . PRO G  1 66  ? 41.787 -15.320 -31.956  1.00 14.44 ? 66   PRO H N   1 
ATOM   7164  C  CA  . PRO G  1 66  ? 40.624 -16.164 -32.261  1.00 14.67 ? 66   PRO H CA  1 
ATOM   7165  C  C   . PRO G  1 66  ? 39.918 -15.808 -33.583  1.00 15.28 ? 66   PRO H C   1 
ATOM   7166  O  O   . PRO G  1 66  ? 39.217 -16.649 -34.148  1.00 15.52 ? 66   PRO H O   1 
ATOM   7167  C  CB  . PRO G  1 66  ? 39.700 -15.924 -31.068  1.00 14.58 ? 66   PRO H CB  1 
ATOM   7168  C  CG  . PRO G  1 66  ? 40.025 -14.552 -30.620  1.00 14.95 ? 66   PRO H CG  1 
ATOM   7169  C  CD  . PRO G  1 66  ? 41.516 -14.432 -30.812  1.00 14.33 ? 66   PRO H CD  1 
ATOM   7170  N  N   . LEU G  1 67  ? 40.137 -14.586 -34.078  1.00 14.69 ? 67   LEU H N   1 
ATOM   7171  C  CA  . LEU G  1 67  ? 39.576 -14.109 -35.356  1.00 15.04 ? 67   LEU H CA  1 
ATOM   7172  C  C   . LEU G  1 67  ? 40.467 -14.257 -36.607  1.00 14.26 ? 67   LEU H C   1 
ATOM   7173  O  O   . LEU G  1 67  ? 40.104 -13.757 -37.677  1.00 13.93 ? 67   LEU H O   1 
ATOM   7174  C  CB  . LEU G  1 67  ? 39.107 -12.651 -35.214  1.00 15.43 ? 67   LEU H CB  1 
ATOM   7175  C  CG  . LEU G  1 67  ? 37.779 -12.488 -34.474  1.00 17.08 ? 67   LEU H CG  1 
ATOM   7176  C  CD1 . LEU G  1 67  ? 37.603 -11.068 -33.982  1.00 19.20 ? 67   LEU H CD1 1 
ATOM   7177  C  CD2 . LEU G  1 67  ? 36.598 -12.899 -35.376  1.00 20.35 ? 67   LEU H CD2 1 
ATOM   7178  N  N   . SER G  1 68  ? 41.601 -14.949 -36.470  1.00 13.91 ? 68   SER H N   1 
ATOM   7179  C  CA  . SER G  1 68  ? 42.522 -15.256 -37.577  1.00 14.15 ? 68   SER H CA  1 
ATOM   7180  C  C   . SER G  1 68  ? 42.821 -14.068 -38.486  1.00 13.92 ? 68   SER H C   1 
ATOM   7181  O  O   . SER G  1 68  ? 42.737 -14.184 -39.720  1.00 12.85 ? 68   SER H O   1 
ATOM   7182  C  CB  . SER G  1 68  ? 42.027 -16.452 -38.430  1.00 15.42 ? 68   SER H CB  1 
ATOM   7183  O  OG  . SER G  1 68  ? 41.858 -17.604 -37.629  1.00 17.37 ? 68   SER H OG  1 
ATOM   7184  N  N   . ARG G  1 69  ? 43.184 -12.940 -37.865  1.00 12.89 ? 69   ARG H N   1 
ATOM   7185  C  CA  . ARG G  1 69  ? 43.550 -11.716 -38.568  1.00 13.09 ? 69   ARG H CA  1 
ATOM   7186  C  C   . ARG G  1 69  ? 45.060 -11.620 -38.651  1.00 12.87 ? 69   ARG H C   1 
ATOM   7187  O  O   . ARG G  1 69  ? 45.770 -12.430 -38.055  1.00 13.12 ? 69   ARG H O   1 
ATOM   7188  C  CB  . ARG G  1 69  ? 43.081 -10.494 -37.774  1.00 12.64 ? 69   ARG H CB  1 
ATOM   7189  C  CG  . ARG G  1 69  ? 41.631 -10.487 -37.367  1.00 15.38 ? 69   ARG H CG  1 
ATOM   7190  C  CD  . ARG G  1 69  ? 40.724 -10.427 -38.575  1.00 16.67 ? 69   ARG H CD  1 
ATOM   7191  N  NE  . ARG G  1 69  ? 39.317 -10.393 -38.174  1.00 21.23 ? 69   ARG H NE  1 
ATOM   7192  C  CZ  . ARG G  1 69  ? 38.318 -10.975 -38.839  1.00 21.40 ? 69   ARG H CZ  1 
ATOM   7193  N  NH1 . ARG G  1 69  ? 37.077 -10.876 -38.377  1.00 22.58 ? 69   ARG H NH1 1 
ATOM   7194  N  NH2 . ARG G  1 69  ? 38.548 -11.662 -39.950  1.00 21.72 ? 69   ARG H NH2 1 
ATOM   7195  N  N   . LYS G  1 70  ? 45.550 -10.608 -39.361  1.00 12.05 ? 70   LYS H N   1 
ATOM   7196  C  CA  . LYS G  1 70  ? 46.982 -10.329 -39.396  1.00 11.46 ? 70   LYS H CA  1 
ATOM   7197  C  C   . LYS G  1 70  ? 47.351 -9.479  -38.177  1.00 10.73 ? 70   LYS H C   1 
ATOM   7198  O  O   . LYS G  1 70  ? 46.484 -8.860  -37.562  1.00 9.57  ? 70   LYS H O   1 
ATOM   7199  C  CB  . LYS G  1 70  ? 47.378 -9.639  -40.704  1.00 12.03 ? 70   LYS H CB  1 
ATOM   7200  C  CG  . LYS G  1 70  ? 47.484 -10.617 -41.878  1.00 15.15 ? 70   LYS H CG  1 
ATOM   7201  C  CD  . LYS G  1 70  ? 47.887 -9.914  -43.159  1.00 17.48 ? 70   LYS H CD  1 
ATOM   7202  C  CE  . LYS G  1 70  ? 47.596 -10.789 -44.380  1.00 20.80 ? 70   LYS H CE  1 
ATOM   7203  N  NZ  . LYS G  1 70  ? 47.813 -10.022 -45.663  1.00 23.17 ? 70   LYS H NZ  1 
ATOM   7204  N  N   . HIS G  1 71  ? 48.630 -9.495  -37.814  1.00 9.74  ? 71   HIS H N   1 
ATOM   7205  C  CA  . HIS G  1 71  ? 49.144 -8.671  -36.718  1.00 9.95  ? 71   HIS H CA  1 
ATOM   7206  C  C   . HIS G  1 71  ? 48.962 -7.171  -37.001  1.00 9.69  ? 71   HIS H C   1 
ATOM   7207  O  O   . HIS G  1 71  ? 49.192 -6.728  -38.128  1.00 10.50 ? 71   HIS H O   1 
ATOM   7208  C  CB  . HIS G  1 71  ? 50.638 -8.953  -36.504  1.00 9.37  ? 71   HIS H CB  1 
ATOM   7209  C  CG  . HIS G  1 71  ? 51.253 -8.158  -35.397  1.00 8.38  ? 71   HIS H CG  1 
ATOM   7210  N  ND1 . HIS G  1 71  ? 51.017 -8.432  -34.074  1.00 10.08 ? 71   HIS H ND1 1 
ATOM   7211  C  CD2 . HIS G  1 71  ? 52.095 -7.093  -35.418  1.00 9.30  ? 71   HIS H CD2 1 
ATOM   7212  C  CE1 . HIS G  1 71  ? 51.682 -7.572  -33.319  1.00 10.28 ? 71   HIS H CE1 1 
ATOM   7213  N  NE2 . HIS G  1 71  ? 52.340 -6.744  -34.112  1.00 6.53  ? 71   HIS H NE2 1 
ATOM   7214  N  N   . GLY G  1 72  ? 48.588 -6.410  -35.970  1.00 9.67  ? 72   GLY H N   1 
ATOM   7215  C  CA  . GLY G  1 72  ? 48.490 -4.945  -36.064  1.00 9.34  ? 72   GLY H CA  1 
ATOM   7216  C  C   . GLY G  1 72  ? 48.872 -4.264  -34.753  1.00 9.41  ? 72   GLY H C   1 
ATOM   7217  O  O   . GLY G  1 72  ? 49.350 -4.908  -33.815  1.00 8.61  ? 72   GLY H O   1 
ATOM   7218  N  N   . GLY G  1 73  ? 48.662 -2.950  -34.693  1.00 9.43  ? 73   GLY H N   1 
ATOM   7219  C  CA  . GLY G  1 73  ? 48.673 -2.236  -33.417  1.00 8.96  ? 73   GLY H CA  1 
ATOM   7220  C  C   . GLY G  1 73  ? 47.268 -2.227  -32.814  1.00 8.44  ? 73   GLY H C   1 
ATOM   7221  O  O   . GLY G  1 73  ? 46.293 -2.511  -33.502  1.00 7.71  ? 73   GLY H O   1 
ATOM   7222  N  N   . PRO G  1 74  ? 47.145 -1.891  -31.517  1.00 8.61  ? 74   PRO H N   1 
ATOM   7223  C  CA  . PRO G  1 74  ? 45.832 -1.912  -30.821  1.00 8.87  ? 74   PRO H CA  1 
ATOM   7224  C  C   . PRO G  1 74  ? 44.766 -0.987  -31.432  1.00 9.72  ? 74   PRO H C   1 
ATOM   7225  O  O   . PRO G  1 74  ? 43.551 -1.233  -31.321  1.00 9.29  ? 74   PRO H O   1 
ATOM   7226  C  CB  . PRO G  1 74  ? 46.174 -1.479  -29.385  1.00 9.47  ? 74   PRO H CB  1 
ATOM   7227  C  CG  . PRO G  1 74  ? 47.612 -0.944  -29.434  1.00 8.65  ? 74   PRO H CG  1 
ATOM   7228  C  CD  . PRO G  1 74  ? 48.268 -1.596  -30.610  1.00 9.07  ? 74   PRO H CD  1 
ATOM   7229  N  N   . LYS G  1 75  ? 45.224 0.066   -32.092  1.00 9.31  ? 75   LYS H N   1 
ATOM   7230  C  CA  . LYS G  1 75  ? 44.345 1.019   -32.725  1.00 10.36 ? 75   LYS H CA  1 
ATOM   7231  C  C   . LYS G  1 75  ? 43.749 0.538   -34.044  1.00 10.97 ? 75   LYS H C   1 
ATOM   7232  O  O   . LYS G  1 75  ? 42.784 1.136   -34.526  1.00 11.73 ? 75   LYS H O   1 
ATOM   7233  C  CB  . LYS G  1 75  ? 45.102 2.333   -32.944  1.00 10.17 ? 75   LYS H CB  1 
ATOM   7234  C  CG  . LYS G  1 75  ? 45.446 3.066   -31.636  1.00 11.94 ? 75   LYS H CG  1 
ATOM   7235  C  CD  . LYS G  1 75  ? 46.340 4.355   -31.874  1.00 13.46 ? 75   LYS H CD  1 
ATOM   7236  C  CE  . LYS G  1 75  ? 45.599 5.474   -32.625  1.00 18.07 ? 75   LYS H CE  1 
ATOM   7237  N  NZ  . LYS G  1 75  ? 46.465 6.676   -32.948  1.00 16.26 ? 75   LYS H NZ  1 
ATOM   7238  N  N   . ASP G  1 76  ? 44.320 -0.522  -34.623  1.00 10.82 ? 76   ASP H N   1 
ATOM   7239  C  CA  . ASP G  1 76  ? 43.928 -1.007  -35.957  1.00 11.61 ? 76   ASP H CA  1 
ATOM   7240  C  C   . ASP G  1 76  ? 42.724 -1.967  -35.871  1.00 11.98 ? 76   ASP H C   1 
ATOM   7241  O  O   . ASP G  1 76  ? 42.566 -2.697  -34.881  1.00 12.22 ? 76   ASP H O   1 
ATOM   7242  C  CB  . ASP G  1 76  ? 45.070 -1.787  -36.597  1.00 11.48 ? 76   ASP H CB  1 
ATOM   7243  C  CG  . ASP G  1 76  ? 46.260 -0.934  -36.951  1.00 12.29 ? 76   ASP H CG  1 
ATOM   7244  O  OD1 . ASP G  1 76  ? 47.399 -1.426  -36.813  1.00 13.33 ? 76   ASP H OD1 1 
ATOM   7245  O  OD2 . ASP G  1 76  ? 46.086 0.209   -37.421  1.00 14.32 ? 76   ASP H OD2 1 
ATOM   7246  N  N   . GLU G  1 77  ? 41.889 -1.961  -36.903  1.00 12.52 ? 77   GLU H N   1 
ATOM   7247  C  CA  . GLU G  1 77  ? 40.792 -2.932  -36.996  1.00 13.32 ? 77   GLU H CA  1 
ATOM   7248  C  C   . GLU G  1 77  ? 41.387 -4.316  -37.295  1.00 12.77 ? 77   GLU H C   1 
ATOM   7249  O  O   . GLU G  1 77  ? 40.956 -5.324  -36.709  1.00 12.42 ? 77   GLU H O   1 
ATOM   7250  C  CB  . GLU G  1 77  ? 39.773 -2.535  -38.074  1.00 14.45 ? 77   GLU H CB  1 
ATOM   7251  C  CG  . GLU G  1 77  ? 38.648 -3.585  -38.233  1.00 19.05 ? 77   GLU H CG  1 
ATOM   7252  C  CD  . GLU G  1 77  ? 37.405 -3.080  -38.965  1.00 24.72 ? 77   GLU H CD  1 
ATOM   7253  O  OE1 . GLU G  1 77  ? 37.469 -2.032  -39.645  1.00 27.44 ? 77   GLU H OE1 1 
ATOM   7254  O  OE2 . GLU G  1 77  ? 36.348 -3.748  -38.858  1.00 26.96 ? 77   GLU H OE2 1 
ATOM   7255  N  N   . GLU G  1 78  ? 42.396 -4.345  -38.176  1.00 11.13 ? 78   GLU H N   1 
ATOM   7256  C  CA  . GLU G  1 78  ? 43.127 -5.571  -38.505  1.00 10.79 ? 78   GLU H CA  1 
ATOM   7257  C  C   . GLU G  1 78  ? 44.235 -5.789  -37.482  1.00 10.08 ? 78   GLU H C   1 
ATOM   7258  O  O   . GLU G  1 78  ? 45.311 -5.180  -37.558  1.00 9.53  ? 78   GLU H O   1 
ATOM   7259  C  CB  . GLU G  1 78  ? 43.700 -5.505  -39.929  1.00 11.24 ? 78   GLU H CB  1 
ATOM   7260  C  CG  . GLU G  1 78  ? 44.365 -6.806  -40.394  1.00 13.66 ? 78   GLU H CG  1 
ATOM   7261  C  CD  . GLU G  1 78  ? 43.363 -7.890  -40.754  1.00 15.73 ? 78   GLU H CD  1 
ATOM   7262  O  OE1 . GLU G  1 78  ? 43.765 -9.082  -40.845  1.00 17.55 ? 78   GLU H OE1 1 
ATOM   7263  O  OE2 . GLU G  1 78  ? 42.168 -7.549  -40.924  1.00 17.30 ? 78   GLU H OE2 1 
ATOM   7264  N  N   . ARG G  1 79  ? 43.931 -6.628  -36.498  1.00 9.01  ? 79   ARG H N   1 
ATOM   7265  C  CA  . ARG G  1 79  ? 44.847 -6.950  -35.425  1.00 9.23  ? 79   ARG H CA  1 
ATOM   7266  C  C   . ARG G  1 79  ? 44.411 -8.279  -34.839  1.00 9.20  ? 79   ARG H C   1 
ATOM   7267  O  O   . ARG G  1 79  ? 43.253 -8.702  -34.982  1.00 10.38 ? 79   ARG H O   1 
ATOM   7268  C  CB  . ARG G  1 79  ? 44.804 -5.895  -34.308  1.00 8.99  ? 79   ARG H CB  1 
ATOM   7269  C  CG  . ARG G  1 79  ? 43.410 -5.721  -33.658  1.00 7.45  ? 79   ARG H CG  1 
ATOM   7270  C  CD  . ARG G  1 79  ? 43.443 -4.738  -32.463  1.00 7.62  ? 79   ARG H CD  1 
ATOM   7271  N  NE  . ARG G  1 79  ? 43.656 -5.408  -31.193  1.00 8.13  ? 79   ARG H NE  1 
ATOM   7272  C  CZ  . ARG G  1 79  ? 43.431 -4.847  -30.003  1.00 7.07  ? 79   ARG H CZ  1 
ATOM   7273  N  NH1 . ARG G  1 79  ? 43.620 -5.549  -28.889  1.00 7.53  ? 79   ARG H NH1 1 
ATOM   7274  N  NH2 . ARG G  1 79  ? 43.002 -3.591  -29.919  1.00 8.64  ? 79   ARG H NH2 1 
ATOM   7275  N  N   . HIS G  1 80  ? 45.349 -8.932  -34.184  1.00 9.78  ? 80   HIS H N   1 
ATOM   7276  C  CA  . HIS G  1 80  ? 45.040 -10.021 -33.264  1.00 9.28  ? 80   HIS H CA  1 
ATOM   7277  C  C   . HIS G  1 80  ? 44.355 -9.424  -32.033  1.00 9.92  ? 80   HIS H C   1 
ATOM   7278  O  O   . HIS G  1 80  ? 44.688 -8.318  -31.605  1.00 9.05  ? 80   HIS H O   1 
ATOM   7279  C  CB  . HIS G  1 80  ? 46.329 -10.717 -32.848  1.00 8.82  ? 80   HIS H CB  1 
ATOM   7280  C  CG  . HIS G  1 80  ? 47.152 -11.194 -34.003  1.00 9.17  ? 80   HIS H CG  1 
ATOM   7281  N  ND1 . HIS G  1 80  ? 48.524 -11.103 -34.030  1.00 7.88  ? 80   HIS H ND1 1 
ATOM   7282  C  CD2 . HIS G  1 80  ? 46.791 -11.737 -35.192  1.00 9.16  ? 80   HIS H CD2 1 
ATOM   7283  C  CE1 . HIS G  1 80  ? 48.981 -11.604 -35.163  1.00 7.08  ? 80   HIS H CE1 1 
ATOM   7284  N  NE2 . HIS G  1 80  ? 47.949 -11.998 -35.887  1.00 8.53  ? 80   HIS H NE2 1 
ATOM   7285  N  N   . VAL G  1 81  ? 43.390 -10.150 -31.471  1.00 9.63  ? 81   VAL H N   1 
ATOM   7286  C  CA  . VAL G  1 81  ? 42.822 -9.764  -30.168  1.00 9.65  ? 81   VAL H CA  1 
ATOM   7287  C  C   . VAL G  1 81  ? 43.925 -9.418  -29.159  1.00 9.28  ? 81   VAL H C   1 
ATOM   7288  O  O   . VAL G  1 81  ? 43.817 -8.428  -28.429  1.00 9.13  ? 81   VAL H O   1 
ATOM   7289  C  CB  . VAL G  1 81  ? 41.828 -10.827 -29.600  1.00 9.81  ? 81   VAL H CB  1 
ATOM   7290  C  CG1 . VAL G  1 81  ? 41.304 -10.402 -28.215  1.00 8.40  ? 81   VAL H CG1 1 
ATOM   7291  C  CG2 . VAL G  1 81  ? 40.666 -11.008 -30.541  1.00 9.48  ? 81   VAL H CG2 1 
ATOM   7292  N  N   . GLY G  1 82  ? 45.020 -10.178 -29.159  1.00 9.40  ? 82   GLY H N   1 
ATOM   7293  C  CA  . GLY G  1 82  ? 46.075 -9.939  -28.188  1.00 9.53  ? 82   GLY H CA  1 
ATOM   7294  C  C   . GLY G  1 82  ? 47.060 -8.817  -28.458  1.00 10.34 ? 82   GLY H C   1 
ATOM   7295  O  O   . GLY G  1 82  ? 48.021 -8.643  -27.688  1.00 11.09 ? 82   GLY H O   1 
ATOM   7296  N  N   . ASP G  1 83  ? 46.836 -8.041  -29.526  1.00 9.71  ? 83   ASP H N   1 
ATOM   7297  C  CA  . ASP G  1 83  ? 47.812 -7.023  -29.920  1.00 9.59  ? 83   ASP H CA  1 
ATOM   7298  C  C   . ASP G  1 83  ? 47.660 -5.758  -29.094  1.00 8.95  ? 83   ASP H C   1 
ATOM   7299  O  O   . ASP G  1 83  ? 46.828 -4.918  -29.392  1.00 9.45  ? 83   ASP H O   1 
ATOM   7300  C  CB  . ASP G  1 83  ? 47.694 -6.710  -31.421  1.00 9.40  ? 83   ASP H CB  1 
ATOM   7301  C  CG  . ASP G  1 83  ? 48.229 -7.836  -32.286  1.00 9.39  ? 83   ASP H CG  1 
ATOM   7302  O  OD1 . ASP G  1 83  ? 48.982 -8.672  -31.731  1.00 10.56 ? 83   ASP H OD1 1 
ATOM   7303  O  OD2 . ASP G  1 83  ? 47.912 -7.865  -33.503  1.00 5.68  ? 83   ASP H OD2 1 
ATOM   7304  N  N   . LEU G  1 84  ? 48.467 -5.634  -28.054  1.00 9.15  ? 84   LEU H N   1 
ATOM   7305  C  CA  . LEU G  1 84  ? 48.399 -4.459  -27.184  1.00 8.83  ? 84   LEU H CA  1 
ATOM   7306  C  C   . LEU G  1 84  ? 49.486 -3.425  -27.483  1.00 8.86  ? 84   LEU H C   1 
ATOM   7307  O  O   . LEU G  1 84  ? 49.676 -2.479  -26.713  1.00 7.92  ? 84   LEU H O   1 
ATOM   7308  C  CB  . LEU G  1 84  ? 48.405 -4.906  -25.701  1.00 9.24  ? 84   LEU H CB  1 
ATOM   7309  C  CG  . LEU G  1 84  ? 47.171 -5.722  -25.286  1.00 8.95  ? 84   LEU H CG  1 
ATOM   7310  C  CD1 . LEU G  1 84  ? 47.229 -6.044  -23.813  1.00 12.34 ? 84   LEU H CD1 1 
ATOM   7311  C  CD2 . LEU G  1 84  ? 45.862 -4.974  -25.594  1.00 10.31 ? 84   LEU H CD2 1 
ATOM   7312  N  N   . GLY G  1 85  ? 50.181 -3.596  -28.606  1.00 8.84  ? 85   GLY H N   1 
ATOM   7313  C  CA  . GLY G  1 85  ? 51.221 -2.663  -29.027  1.00 10.41 ? 85   GLY H CA  1 
ATOM   7314  C  C   . GLY G  1 85  ? 52.539 -2.691  -28.272  1.00 10.49 ? 85   GLY H C   1 
ATOM   7315  O  O   . GLY G  1 85  ? 53.112 -3.752  -27.987  1.00 11.53 ? 85   GLY H O   1 
ATOM   7316  N  N   . ASN G  1 86  ? 53.032 -1.495  -27.985  1.00 10.34 ? 86   ASN H N   1 
ATOM   7317  C  CA  . ASN G  1 86  ? 54.269 -1.288  -27.250  1.00 10.29 ? 86   ASN H CA  1 
ATOM   7318  C  C   . ASN G  1 86  ? 54.035 -0.738  -25.856  1.00 10.12 ? 86   ASN H C   1 
ATOM   7319  O  O   . ASN G  1 86  ? 53.033 -0.066  -25.597  1.00 10.73 ? 86   ASN H O   1 
ATOM   7320  C  CB  . ASN G  1 86  ? 55.161 -0.321  -28.019  1.00 10.49 ? 86   ASN H CB  1 
ATOM   7321  C  CG  . ASN G  1 86  ? 55.756 -0.950  -29.236  1.00 10.85 ? 86   ASN H CG  1 
ATOM   7322  O  OD1 . ASN G  1 86  ? 56.463 -1.936  -29.133  1.00 12.01 ? 86   ASN H OD1 1 
ATOM   7323  N  ND2 . ASN G  1 86  ? 55.439 -0.409  -30.412  1.00 9.97  ? 86   ASN H ND2 1 
ATOM   7324  N  N   . VAL G  1 87  ? 54.959 -1.038  -24.959  1.00 10.22 ? 87   VAL H N   1 
ATOM   7325  C  CA  . VAL G  1 87  ? 55.061 -0.319  -23.691  1.00 10.10 ? 87   VAL H CA  1 
ATOM   7326  C  C   . VAL G  1 87  ? 56.420 0.360   -23.637  1.00 10.53 ? 87   VAL H C   1 
ATOM   7327  O  O   . VAL G  1 87  ? 57.379 -0.140  -24.200  1.00 10.13 ? 87   VAL H O   1 
ATOM   7328  C  CB  . VAL G  1 87  ? 54.815 -1.224  -22.466  1.00 10.23 ? 87   VAL H CB  1 
ATOM   7329  C  CG1 . VAL G  1 87  ? 53.330 -1.678  -22.442  1.00 8.43  ? 87   VAL H CG1 1 
ATOM   7330  C  CG2 . VAL G  1 87  ? 55.785 -2.431  -22.440  1.00 10.55 ? 87   VAL H CG2 1 
ATOM   7331  N  N   . THR G  1 88  ? 56.492 1.520   -22.989  1.00 11.57 ? 88   THR H N   1 
ATOM   7332  C  CA  . THR G  1 88  ? 57.711 2.361   -23.025  1.00 12.67 ? 88   THR H CA  1 
ATOM   7333  C  C   . THR G  1 88  ? 58.373 2.386   -21.659  1.00 13.86 ? 88   THR H C   1 
ATOM   7334  O  O   . THR G  1 88  ? 57.751 2.796   -20.667  1.00 14.23 ? 88   THR H O   1 
ATOM   7335  C  CB  . THR G  1 88  ? 57.372 3.822   -23.454  1.00 12.49 ? 88   THR H CB  1 
ATOM   7336  O  OG1 . THR G  1 88  ? 56.887 3.814   -24.796  1.00 10.18 ? 88   THR H OG1 1 
ATOM   7337  C  CG2 . THR G  1 88  ? 58.596 4.767   -23.357  1.00 12.63 ? 88   THR H CG2 1 
ATOM   7338  N  N   . ALA G  1 89  ? 59.629 1.941   -21.618  1.00 14.75 ? 89   ALA H N   1 
ATOM   7339  C  CA  . ALA G  1 89  ? 60.436 2.025   -20.418  1.00 16.01 ? 89   ALA H CA  1 
ATOM   7340  C  C   . ALA G  1 89  ? 61.213 3.330   -20.388  1.00 17.06 ? 89   ALA H C   1 
ATOM   7341  O  O   . ALA G  1 89  ? 61.741 3.783   -21.426  1.00 17.18 ? 89   ALA H O   1 
ATOM   7342  C  CB  . ALA G  1 89  ? 61.389 0.835   -20.346  1.00 15.59 ? 89   ALA H CB  1 
ATOM   7343  N  N   . ASP G  1 90  ? 61.288 3.923   -19.198  1.00 18.14 ? 90   ASP H N   1 
ATOM   7344  C  CA  . ASP G  1 90  ? 62.025 5.168   -18.996  1.00 19.71 ? 90   ASP H CA  1 
ATOM   7345  C  C   . ASP G  1 90  ? 63.523 4.895   -18.860  1.00 20.15 ? 90   ASP H C   1 
ATOM   7346  O  O   . ASP G  1 90  ? 63.962 3.755   -18.989  1.00 19.45 ? 90   ASP H O   1 
ATOM   7347  C  CB  . ASP G  1 90  ? 61.470 5.956   -17.795  1.00 20.03 ? 90   ASP H CB  1 
ATOM   7348  C  CG  . ASP G  1 90  ? 61.620 5.216   -16.457  1.00 21.22 ? 90   ASP H CG  1 
ATOM   7349  O  OD1 . ASP G  1 90  ? 60.897 5.587   -15.507  1.00 21.54 ? 90   ASP H OD1 1 
ATOM   7350  O  OD2 . ASP G  1 90  ? 62.450 4.284   -16.339  1.00 22.85 ? 90   ASP H OD2 1 
ATOM   7351  N  N   . LYS G  1 91  ? 64.307 5.945   -18.615  1.00 21.49 ? 91   LYS H N   1 
ATOM   7352  C  CA  . LYS G  1 91  ? 65.758 5.797   -18.424  1.00 22.53 ? 91   LYS H CA  1 
ATOM   7353  C  C   . LYS G  1 91  ? 66.107 4.853   -17.257  1.00 22.61 ? 91   LYS H C   1 
ATOM   7354  O  O   . LYS G  1 91  ? 67.157 4.209   -17.268  1.00 22.63 ? 91   LYS H O   1 
ATOM   7355  C  CB  . LYS G  1 91  ? 66.417 7.169   -18.211  1.00 22.91 ? 91   LYS H CB  1 
ATOM   7356  C  CG  . LYS G  1 91  ? 65.798 7.977   -17.069  1.00 25.38 ? 91   LYS H CG  1 
ATOM   7357  C  CD  . LYS G  1 91  ? 66.666 9.143   -16.586  1.00 27.27 ? 91   LYS H CD  1 
ATOM   7358  C  CE  . LYS G  1 91  ? 65.779 10.130  -15.835  1.00 29.72 ? 91   LYS H CE  1 
ATOM   7359  N  NZ  . LYS G  1 91  ? 66.309 10.539  -14.501  1.00 31.43 ? 91   LYS H NZ  1 
ATOM   7360  N  N   . ASP G  1 92  ? 65.228 4.778   -16.259  1.00 22.70 ? 92   ASP H N   1 
ATOM   7361  C  CA  . ASP G  1 92  ? 65.437 3.894   -15.111  1.00 23.10 ? 92   ASP H CA  1 
ATOM   7362  C  C   . ASP G  1 92  ? 64.985 2.460   -15.398  1.00 22.73 ? 92   ASP H C   1 
ATOM   7363  O  O   . ASP G  1 92  ? 65.067 1.594   -14.524  1.00 22.88 ? 92   ASP H O   1 
ATOM   7364  C  CB  . ASP G  1 92  ? 64.760 4.470   -13.855  1.00 23.53 ? 92   ASP H CB  1 
ATOM   7365  C  CG  . ASP G  1 92  ? 65.386 5.797   -13.408  1.00 25.15 ? 92   ASP H CG  1 
ATOM   7366  O  OD1 . ASP G  1 92  ? 64.973 6.345   -12.360  1.00 28.39 ? 92   ASP H OD1 1 
ATOM   7367  O  OD2 . ASP G  1 92  ? 66.310 6.292   -14.091  1.00 27.75 ? 92   ASP H OD2 1 
ATOM   7368  N  N   . GLY G  1 93  ? 64.524 2.215   -16.627  1.00 21.81 ? 93   GLY H N   1 
ATOM   7369  C  CA  . GLY G  1 93  ? 64.149 0.870   -17.074  1.00 20.84 ? 93   GLY H CA  1 
ATOM   7370  C  C   . GLY G  1 93  ? 62.774 0.432   -16.617  1.00 20.01 ? 93   GLY H C   1 
ATOM   7371  O  O   . GLY G  1 93  ? 62.482 -0.760  -16.556  1.00 19.74 ? 93   GLY H O   1 
ATOM   7372  N  N   . VAL G  1 94  ? 61.935 1.405   -16.280  1.00 19.63 ? 94   VAL H N   1 
ATOM   7373  C  CA  . VAL G  1 94  ? 60.608 1.135   -15.756  1.00 19.28 ? 94   VAL H CA  1 
ATOM   7374  C  C   . VAL G  1 94  ? 59.577 1.572   -16.790  1.00 19.10 ? 94   VAL H C   1 
ATOM   7375  O  O   . VAL G  1 94  ? 59.634 2.715   -17.287  1.00 18.85 ? 94   VAL H O   1 
ATOM   7376  C  CB  . VAL G  1 94  ? 60.349 1.873   -14.410  1.00 19.59 ? 94   VAL H CB  1 
ATOM   7377  C  CG1 . VAL G  1 94  ? 58.932 1.620   -13.896  1.00 18.75 ? 94   VAL H CG1 1 
ATOM   7378  C  CG2 . VAL G  1 94  ? 61.372 1.457   -13.349  1.00 20.28 ? 94   VAL H CG2 1 
ATOM   7379  N  N   . ALA G  1 95  ? 58.670 0.643   -17.115  1.00 18.05 ? 95   ALA H N   1 
ATOM   7380  C  CA  . ALA G  1 95  ? 57.477 0.898   -17.904  1.00 17.00 ? 95   ALA H CA  1 
ATOM   7381  C  C   . ALA G  1 95  ? 56.286 1.020   -16.969  1.00 16.99 ? 95   ALA H C   1 
ATOM   7382  O  O   . ALA G  1 95  ? 55.852 0.024   -16.381  1.00 16.02 ? 95   ALA H O   1 
ATOM   7383  C  CB  . ALA G  1 95  ? 57.233 -0.258  -18.917  1.00 16.94 ? 95   ALA H CB  1 
ATOM   7384  N  N   . ASP G  1 96  ? 55.761 2.233   -16.821  1.00 17.07 ? 96   ASP H N   1 
ATOM   7385  C  CA  . ASP G  1 96  ? 54.565 2.453   -16.018  1.00 17.62 ? 96   ASP H CA  1 
ATOM   7386  C  C   . ASP G  1 96  ? 53.337 2.385   -16.911  1.00 17.50 ? 96   ASP H C   1 
ATOM   7387  O  O   . ASP G  1 96  ? 52.814 3.415   -17.376  1.00 16.65 ? 96   ASP H O   1 
ATOM   7388  C  CB  . ASP G  1 96  ? 54.639 3.771   -15.256  1.00 18.68 ? 96   ASP H CB  1 
ATOM   7389  C  CG  . ASP G  1 96  ? 55.582 3.697   -14.057  1.00 20.82 ? 96   ASP H CG  1 
ATOM   7390  O  OD1 . ASP G  1 96  ? 55.629 2.632   -13.393  1.00 24.22 ? 96   ASP H OD1 1 
ATOM   7391  O  OD2 . ASP G  1 96  ? 56.273 4.709   -13.779  1.00 25.76 ? 96   ASP H OD2 1 
ATOM   7392  N  N   . VAL G  1 97  ? 52.899 1.146   -17.114  1.00 17.17 ? 97   VAL H N   1 
ATOM   7393  C  CA  . VAL G  1 97  ? 51.908 0.753   -18.121  1.00 17.16 ? 97   VAL H CA  1 
ATOM   7394  C  C   . VAL G  1 97  ? 50.506 1.287   -17.816  1.00 17.64 ? 97   VAL H C   1 
ATOM   7395  O  O   . VAL G  1 97  ? 50.008 1.149   -16.695  1.00 17.26 ? 97   VAL H O   1 
ATOM   7396  C  CB  . VAL G  1 97  ? 51.876 -0.785  -18.269  1.00 17.32 ? 97   VAL H CB  1 
ATOM   7397  C  CG1 . VAL G  1 97  ? 50.825 -1.224  -19.318  1.00 17.83 ? 97   VAL H CG1 1 
ATOM   7398  C  CG2 . VAL G  1 97  ? 53.289 -1.345  -18.611  1.00 15.89 ? 97   VAL H CG2 1 
ATOM   7399  N  N   . SER G  1 98  ? 49.890 1.899   -18.827  1.00 17.33 ? 98   SER H N   1 
ATOM   7400  C  CA  . SER G  1 98  ? 48.531 2.414   -18.742  1.00 17.36 ? 98   SER H CA  1 
ATOM   7401  C  C   . SER G  1 98  ? 47.932 2.284   -20.133  1.00 16.60 ? 98   SER H C   1 
ATOM   7402  O  O   . SER G  1 98  ? 48.323 3.008   -21.066  1.00 16.83 ? 98   SER H O   1 
ATOM   7403  C  CB  . SER G  1 98  ? 48.511 3.873   -18.266  1.00 17.80 ? 98   SER H CB  1 
ATOM   7404  O  OG  . SER G  1 98  ? 47.181 4.386   -18.248  1.00 18.26 ? 98   SER H OG  1 
ATOM   7405  N  N   . ILE G  1 99  ? 47.026 1.321   -20.273  1.00 15.40 ? 99   ILE H N   1 
ATOM   7406  C  CA  . ILE G  1 99  ? 46.436 0.949   -21.560  1.00 15.20 ? 99   ILE H CA  1 
ATOM   7407  C  C   . ILE G  1 99  ? 44.954 0.685   -21.332  1.00 14.77 ? 99   ILE H C   1 
ATOM   7408  O  O   . ILE G  1 99  ? 44.567 0.159   -20.288  1.00 15.43 ? 99   ILE H O   1 
ATOM   7409  C  CB  . ILE G  1 99  ? 47.131 -0.322  -22.176  1.00 15.04 ? 99   ILE H CB  1 
ATOM   7410  C  CG1 . ILE G  1 99  ? 48.517 0.050   -22.730  1.00 14.11 ? 99   ILE H CG1 1 
ATOM   7411  C  CG2 . ILE G  1 99  ? 46.266 -0.976  -23.284  1.00 15.42 ? 99   ILE H CG2 1 
ATOM   7412  C  CD1 . ILE G  1 99  ? 49.380 -1.116  -23.230  1.00 14.18 ? 99   ILE H CD1 1 
ATOM   7413  N  N   . GLU G  1 100 ? 44.127 1.119   -22.275  1.00 14.48 ? 100  GLU H N   1 
ATOM   7414  C  CA  . GLU G  1 100 ? 42.702 0.857   -22.244  1.00 14.36 ? 100  GLU H CA  1 
ATOM   7415  C  C   . GLU G  1 100 ? 42.373 0.255   -23.610  1.00 14.26 ? 100  GLU H C   1 
ATOM   7416  O  O   . GLU G  1 100 ? 42.715 0.820   -24.656  1.00 13.31 ? 100  GLU H O   1 
ATOM   7417  C  CB  . GLU G  1 100 ? 41.911 2.147   -22.016  1.00 15.28 ? 100  GLU H CB  1 
ATOM   7418  C  CG  . GLU G  1 100 ? 40.411 1.970   -21.966  1.00 18.95 ? 100  GLU H CG  1 
ATOM   7419  C  CD  . GLU G  1 100 ? 39.687 3.108   -21.245  1.00 25.17 ? 100  GLU H CD  1 
ATOM   7420  O  OE1 . GLU G  1 100 ? 40.314 4.161   -20.973  1.00 26.84 ? 100  GLU H OE1 1 
ATOM   7421  O  OE2 . GLU G  1 100 ? 38.474 2.942   -20.962  1.00 26.61 ? 100  GLU H OE2 1 
ATOM   7422  N  N   . ASP G  1 101 ? 41.727 -0.901  -23.600  1.00 13.42 ? 101  ASP H N   1 
ATOM   7423  C  CA  . ASP G  1 101 ? 41.486 -1.604  -24.851  1.00 13.73 ? 101  ASP H CA  1 
ATOM   7424  C  C   . ASP G  1 101 ? 40.070 -2.178  -24.913  1.00 13.73 ? 101  ASP H C   1 
ATOM   7425  O  O   . ASP G  1 101 ? 39.542 -2.609  -23.902  1.00 13.43 ? 101  ASP H O   1 
ATOM   7426  C  CB  . ASP G  1 101 ? 42.530 -2.705  -25.024  1.00 13.24 ? 101  ASP H CB  1 
ATOM   7427  C  CG  . ASP G  1 101 ? 42.624 -3.179  -26.455  1.00 14.10 ? 101  ASP H CG  1 
ATOM   7428  O  OD1 . ASP G  1 101 ? 42.142 -4.300  -26.717  1.00 10.28 ? 101  ASP H OD1 1 
ATOM   7429  O  OD2 . ASP G  1 101 ? 43.135 -2.415  -27.326  1.00 11.67 ? 101  ASP H OD2 1 
ATOM   7430  N  N   . SER G  1 102 ? 39.452 -2.147  -26.091  1.00 13.78 ? 102  SER H N   1 
ATOM   7431  C  CA  . SER G  1 102 ? 38.065 -2.574  -26.228  1.00 14.43 ? 102  SER H CA  1 
ATOM   7432  C  C   . SER G  1 102 ? 37.923 -3.891  -26.990  1.00 13.93 ? 102  SER H C   1 
ATOM   7433  O  O   . SER G  1 102 ? 36.805 -4.349  -27.212  1.00 14.32 ? 102  SER H O   1 
ATOM   7434  C  CB  . SER G  1 102 ? 37.228 -1.477  -26.889  1.00 14.69 ? 102  SER H CB  1 
ATOM   7435  O  OG  . SER G  1 102 ? 37.161 -0.337  -26.031  1.00 18.42 ? 102  SER H OG  1 
ATOM   7436  N  N   . VAL G  1 103 ? 39.054 -4.490  -27.366  1.00 12.91 ? 103  VAL H N   1 
ATOM   7437  C  CA  . VAL G  1 103 ? 39.069 -5.723  -28.146  1.00 12.50 ? 103  VAL H CA  1 
ATOM   7438  C  C   . VAL G  1 103 ? 39.351 -6.904  -27.239  1.00 12.13 ? 103  VAL H C   1 
ATOM   7439  O  O   . VAL G  1 103 ? 38.669 -7.917  -27.338  1.00 11.78 ? 103  VAL H O   1 
ATOM   7440  C  CB  . VAL G  1 103 ? 40.102 -5.665  -29.293  1.00 13.04 ? 103  VAL H CB  1 
ATOM   7441  C  CG1 . VAL G  1 103 ? 40.154 -6.987  -30.041  1.00 12.36 ? 103  VAL H CG1 1 
ATOM   7442  C  CG2 . VAL G  1 103 ? 39.719 -4.537  -30.259  1.00 12.79 ? 103  VAL H CG2 1 
ATOM   7443  N  N   . ILE G  1 104 ? 40.346 -6.784  -26.361  1.00 11.90 ? 104  ILE H N   1 
ATOM   7444  C  CA  . ILE G  1 104 ? 40.477 -7.768  -25.273  1.00 11.44 ? 104  ILE H CA  1 
ATOM   7445  C  C   . ILE G  1 104 ? 39.253 -7.733  -24.361  1.00 11.74 ? 104  ILE H C   1 
ATOM   7446  O  O   . ILE G  1 104 ? 38.527 -6.740  -24.310  1.00 11.94 ? 104  ILE H O   1 
ATOM   7447  C  CB  . ILE G  1 104 ? 41.775 -7.629  -24.437  1.00 11.56 ? 104  ILE H CB  1 
ATOM   7448  C  CG1 . ILE G  1 104 ? 41.906 -6.233  -23.791  1.00 10.99 ? 104  ILE H CG1 1 
ATOM   7449  C  CG2 . ILE G  1 104 ? 42.991 -8.038  -25.278  1.00 11.10 ? 104  ILE H CG2 1 
ATOM   7450  C  CD1 . ILE G  1 104 ? 42.960 -6.152  -22.654  1.00 12.38 ? 104  ILE H CD1 1 
ATOM   7451  N  N   . SER G  1 105 ? 39.002 -8.837  -23.669  1.00 12.50 ? 105  SER H N   1 
ATOM   7452  C  CA  . SER G  1 105 ? 37.919 -8.883  -22.706  1.00 12.81 ? 105  SER H CA  1 
ATOM   7453  C  C   . SER G  1 105 ? 38.295 -9.796  -21.552  1.00 13.00 ? 105  SER H C   1 
ATOM   7454  O  O   . SER G  1 105 ? 39.244 -10.583 -21.659  1.00 13.75 ? 105  SER H O   1 
ATOM   7455  C  CB  . SER G  1 105 ? 36.622 -9.353  -23.374  1.00 12.96 ? 105  SER H CB  1 
ATOM   7456  O  OG  . SER G  1 105 ? 35.531 -9.051  -22.534  1.00 13.05 ? 105  SER H OG  1 
ATOM   7457  N  N   . LEU G  1 106 ? 37.590 -9.652  -20.433  1.00 13.22 ? 106  LEU H N   1 
ATOM   7458  C  CA  . LEU G  1 106 ? 37.783 -10.552 -19.308  1.00 13.99 ? 106  LEU H CA  1 
ATOM   7459  C  C   . LEU G  1 106 ? 36.638 -11.583 -19.220  1.00 14.48 ? 106  LEU H C   1 
ATOM   7460  O  O   . LEU G  1 106 ? 36.510 -12.309 -18.210  1.00 14.21 ? 106  LEU H O   1 
ATOM   7461  C  CB  . LEU G  1 106 ? 37.962 -9.767  -18.011  1.00 14.00 ? 106  LEU H CB  1 
ATOM   7462  C  CG  . LEU G  1 106 ? 39.103 -8.735  -17.950  1.00 14.09 ? 106  LEU H CG  1 
ATOM   7463  C  CD1 . LEU G  1 106 ? 39.151 -8.126  -16.541  1.00 12.69 ? 106  LEU H CD1 1 
ATOM   7464  C  CD2 . LEU G  1 106 ? 40.471 -9.341  -18.323  1.00 13.91 ? 106  LEU H CD2 1 
ATOM   7465  N  N   . SER G  1 107 ? 35.828 -11.644 -20.283  1.00 14.36 ? 107  SER H N   1 
ATOM   7466  C  CA  . SER G  1 107 ? 34.765 -12.666 -20.448  1.00 15.47 ? 107  SER H CA  1 
ATOM   7467  C  C   . SER G  1 107 ? 34.427 -12.879 -21.935  1.00 16.12 ? 107  SER H C   1 
ATOM   7468  O  O   . SER G  1 107 ? 34.823 -12.070 -22.804  1.00 15.51 ? 107  SER H O   1 
ATOM   7469  C  CB  . SER G  1 107 ? 33.508 -12.333 -19.625  1.00 15.18 ? 107  SER H CB  1 
ATOM   7470  O  OG  . SER G  1 107 ? 32.836 -11.174 -20.107  1.00 16.28 ? 107  SER H OG  1 
ATOM   7471  N  N   . GLY G  1 108 ? 33.745 -13.986 -22.238  1.00 16.58 ? 108  GLY H N   1 
ATOM   7472  C  CA  . GLY G  1 108 ? 33.343 -14.269 -23.622  1.00 17.52 ? 108  GLY H CA  1 
ATOM   7473  C  C   . GLY G  1 108 ? 34.445 -14.780 -24.548  1.00 18.47 ? 108  GLY H C   1 
ATOM   7474  O  O   . GLY G  1 108 ? 35.492 -15.246 -24.094  1.00 18.08 ? 108  GLY H O   1 
ATOM   7475  N  N   . ASP G  1 109 ? 34.206 -14.691 -25.854  1.00 19.00 ? 109  ASP H N   1 
ATOM   7476  C  CA  . ASP G  1 109 ? 35.128 -15.238 -26.865  1.00 20.01 ? 109  ASP H CA  1 
ATOM   7477  C  C   . ASP G  1 109 ? 36.504 -14.560 -26.929  1.00 19.66 ? 109  ASP H C   1 
ATOM   7478  O  O   . ASP G  1 109 ? 37.482 -15.159 -27.395  1.00 19.87 ? 109  ASP H O   1 
ATOM   7479  C  CB  . ASP G  1 109 ? 34.479 -15.160 -28.251  1.00 20.41 ? 109  ASP H CB  1 
ATOM   7480  C  CG  . ASP G  1 109 ? 33.266 -16.056 -28.380  1.00 23.11 ? 109  ASP H CG  1 
ATOM   7481  O  OD1 . ASP G  1 109 ? 32.551 -15.910 -29.398  1.00 25.10 ? 109  ASP H OD1 1 
ATOM   7482  O  OD2 . ASP G  1 109 ? 33.029 -16.898 -27.473  1.00 25.20 ? 109  ASP H OD2 1 
ATOM   7483  N  N   . HIS G  1 110 ? 36.571 -13.315 -26.471  1.00 18.81 ? 110  HIS H N   1 
ATOM   7484  C  CA  . HIS G  1 110 ? 37.827 -12.563 -26.499  1.00 18.77 ? 110  HIS H CA  1 
ATOM   7485  C  C   . HIS G  1 110 ? 38.512 -12.589 -25.135  1.00 17.80 ? 110  HIS H C   1 
ATOM   7486  O  O   . HIS G  1 110 ? 39.442 -11.810 -24.895  1.00 17.33 ? 110  HIS H O   1 
ATOM   7487  C  CB  . HIS G  1 110 ? 37.561 -11.103 -26.883  1.00 18.56 ? 110  HIS H CB  1 
ATOM   7488  C  CG  . HIS G  1 110 ? 37.158 -10.899 -28.309  1.00 20.80 ? 110  HIS H CG  1 
ATOM   7489  N  ND1 . HIS G  1 110 ? 36.962 -9.640  -28.843  1.00 21.76 ? 110  HIS H ND1 1 
ATOM   7490  C  CD2 . HIS G  1 110 ? 36.916 -11.778 -29.311  1.00 21.19 ? 110  HIS H CD2 1 
ATOM   7491  C  CE1 . HIS G  1 110 ? 36.599 -9.758  -30.111  1.00 23.16 ? 110  HIS H CE1 1 
ATOM   7492  N  NE2 . HIS G  1 110 ? 36.567 -11.042 -30.420  1.00 23.99 ? 110  HIS H NE2 1 
HETATM 7493  N  N   . CME G  1 111 ? 38.051 -13.476 -24.249  1.00 17.40 ? 111  CME H N   1 
HETATM 7494  C  CA  . CME G  1 111 ? 38.568 -13.552 -22.881  1.00 17.11 ? 111  CME H CA  1 
HETATM 7495  C  CB  . CME G  1 111 ? 37.729 -14.487 -22.000  1.00 17.93 ? 111  CME H CB  1 
HETATM 7496  S  SG  . CME G  1 111 ? 38.255 -14.386 -20.317  1.00 20.46 ? 111  CME H SG  1 
HETATM 7497  S  SD  . CME G  1 111 ? 37.160 -15.820 -19.406  1.00 30.15 ? 111  CME H SD  1 
HETATM 7498  C  CE  . CME G  1 111 ? 38.390 -17.072 -19.184  1.00 30.21 ? 111  CME H CE  1 
HETATM 7499  C  CZ  . CME G  1 111 ? 38.514 -17.944 -20.432  1.00 32.70 ? 111  CME H CZ  1 
HETATM 7500  O  OH  . CME G  1 111 ? 39.691 -17.567 -21.164  1.00 35.30 ? 111  CME H OH  1 
HETATM 7501  C  C   . CME G  1 111 ? 40.027 -13.929 -22.878  1.00 16.28 ? 111  CME H C   1 
HETATM 7502  O  O   . CME G  1 111 ? 40.442 -14.881 -23.562  1.00 15.54 ? 111  CME H O   1 
ATOM   7503  N  N   . ILE G  1 112 ? 40.808 -13.163 -22.117  1.00 15.37 ? 112  ILE H N   1 
ATOM   7504  C  CA  . ILE G  1 112 ? 42.262 -13.356 -22.002  1.00 15.48 ? 112  ILE H CA  1 
ATOM   7505  C  C   . ILE G  1 112 ? 42.679 -14.038 -20.679  1.00 15.80 ? 112  ILE H C   1 
ATOM   7506  O  O   . ILE G  1 112 ? 43.841 -14.451 -20.502  1.00 15.38 ? 112  ILE H O   1 
ATOM   7507  C  CB  . ILE G  1 112 ? 43.032 -12.016 -22.154  1.00 15.24 ? 112  ILE H CB  1 
ATOM   7508  C  CG1 . ILE G  1 112 ? 42.592 -10.991 -21.099  1.00 15.50 ? 112  ILE H CG1 1 
ATOM   7509  C  CG2 . ILE G  1 112 ? 42.848 -11.434 -23.570  1.00 14.91 ? 112  ILE H CG2 1 
ATOM   7510  C  CD1 . ILE G  1 112 ? 43.504 -9.795  -21.018  1.00 15.49 ? 112  ILE H CD1 1 
ATOM   7511  N  N   . ILE G  1 113 ? 41.740 -14.126 -19.745  1.00 16.02 ? 113  ILE H N   1 
ATOM   7512  C  CA  . ILE G  1 113 ? 42.010 -14.846 -18.497  1.00 16.96 ? 113  ILE H CA  1 
ATOM   7513  C  C   . ILE G  1 113 ? 42.412 -16.293 -18.821  1.00 17.08 ? 113  ILE H C   1 
ATOM   7514  O  O   . ILE G  1 113 ? 41.783 -16.966 -19.666  1.00 17.03 ? 113  ILE H O   1 
ATOM   7515  C  CB  . ILE G  1 113 ? 40.828 -14.739 -17.496  1.00 17.07 ? 113  ILE H CB  1 
ATOM   7516  C  CG1 . ILE G  1 113 ? 40.836 -13.343 -16.847  1.00 17.70 ? 113  ILE H CG1 1 
ATOM   7517  C  CG2 . ILE G  1 113 ? 40.941 -15.809 -16.417  1.00 17.46 ? 113  ILE H CG2 1 
ATOM   7518  C  CD1 . ILE G  1 113 ? 39.519 -12.917 -16.172  1.00 17.59 ? 113  ILE H CD1 1 
ATOM   7519  N  N   . GLY G  1 114 ? 43.501 -16.748 -18.200  1.00 16.99 ? 114  GLY H N   1 
ATOM   7520  C  CA  . GLY G  1 114 ? 44.003 -18.101 -18.457  1.00 17.59 ? 114  GLY H CA  1 
ATOM   7521  C  C   . GLY G  1 114 ? 44.929 -18.156 -19.646  1.00 17.65 ? 114  GLY H C   1 
ATOM   7522  O  O   . GLY G  1 114 ? 45.330 -19.231 -20.085  1.00 16.91 ? 114  GLY H O   1 
ATOM   7523  N  N   . ARG G  1 115 ? 45.259 -16.984 -20.187  1.00 17.88 ? 115  ARG H N   1 
ATOM   7524  C  CA  . ARG G  1 115 ? 46.197 -16.889 -21.309  1.00 17.97 ? 115  ARG H CA  1 
ATOM   7525  C  C   . ARG G  1 115 ? 47.446 -16.159 -20.820  1.00 17.81 ? 115  ARG H C   1 
ATOM   7526  O  O   . ARG G  1 115 ? 47.545 -15.839 -19.631  1.00 18.04 ? 115  ARG H O   1 
ATOM   7527  C  CB  . ARG G  1 115 ? 45.542 -16.214 -22.528  1.00 18.51 ? 115  ARG H CB  1 
ATOM   7528  C  CG  . ARG G  1 115 ? 44.232 -16.904 -22.946  1.00 19.06 ? 115  ARG H CG  1 
ATOM   7529  C  CD  . ARG G  1 115 ? 43.730 -16.418 -24.293  1.00 18.36 ? 115  ARG H CD  1 
ATOM   7530  N  NE  . ARG G  1 115 ? 42.426 -16.996 -24.620  1.00 17.03 ? 115  ARG H NE  1 
ATOM   7531  C  CZ  . ARG G  1 115 ? 42.237 -18.153 -25.256  1.00 17.57 ? 115  ARG H CZ  1 
ATOM   7532  N  NH1 . ARG G  1 115 ? 41.000 -18.568 -25.502  1.00 16.67 ? 115  ARG H NH1 1 
ATOM   7533  N  NH2 . ARG G  1 115 ? 43.266 -18.894 -25.664  1.00 18.35 ? 115  ARG H NH2 1 
ATOM   7534  N  N   . THR G  1 116 ? 48.417 -15.947 -21.700  1.00 17.25 ? 116  THR H N   1 
ATOM   7535  C  CA  . THR G  1 116 ? 49.719 -15.440 -21.266  1.00 17.60 ? 116  THR H CA  1 
ATOM   7536  C  C   . THR G  1 116 ? 50.010 -14.010 -21.747  1.00 16.97 ? 116  THR H C   1 
ATOM   7537  O  O   . THR G  1 116 ? 49.930 -13.710 -22.939  1.00 16.60 ? 116  THR H O   1 
ATOM   7538  C  CB  . THR G  1 116 ? 50.856 -16.392 -21.683  1.00 17.80 ? 116  THR H CB  1 
ATOM   7539  O  OG1 . THR G  1 116 ? 50.733 -17.621 -20.949  1.00 18.61 ? 116  THR H OG1 1 
ATOM   7540  C  CG2 . THR G  1 116 ? 52.231 -15.761 -21.415  1.00 18.48 ? 116  THR H CG2 1 
ATOM   7541  N  N   . LEU G  1 117 ? 50.343 -13.136 -20.800  1.00 16.04 ? 117  LEU H N   1 
ATOM   7542  C  CA  . LEU G  1 117 ? 50.837 -11.805 -21.126  1.00 15.71 ? 117  LEU H CA  1 
ATOM   7543  C  C   . LEU G  1 117 ? 52.355 -11.828 -21.313  1.00 15.56 ? 117  LEU H C   1 
ATOM   7544  O  O   . LEU G  1 117 ? 53.056 -12.420 -20.508  1.00 15.64 ? 117  LEU H O   1 
ATOM   7545  C  CB  . LEU G  1 117 ? 50.477 -10.824 -20.010  1.00 15.15 ? 117  LEU H CB  1 
ATOM   7546  C  CG  . LEU G  1 117 ? 50.812 -9.362  -20.330  1.00 14.95 ? 117  LEU H CG  1 
ATOM   7547  C  CD1 . LEU G  1 117 ? 50.026 -8.893  -21.575  1.00 14.25 ? 117  LEU H CD1 1 
ATOM   7548  C  CD2 . LEU G  1 117 ? 50.496 -8.491  -19.143  1.00 14.18 ? 117  LEU H CD2 1 
ATOM   7549  N  N   . VAL G  1 118 ? 52.851 -11.165 -22.361  1.00 15.42 ? 118  VAL H N   1 
ATOM   7550  C  CA  . VAL G  1 118 ? 54.283 -11.161 -22.683  1.00 14.91 ? 118  VAL H CA  1 
ATOM   7551  C  C   . VAL G  1 118 ? 54.803 -9.755  -22.969  1.00 15.33 ? 118  VAL H C   1 
ATOM   7552  O  O   . VAL G  1 118 ? 54.174 -9.010  -23.727  1.00 14.93 ? 118  VAL H O   1 
ATOM   7553  C  CB  . VAL G  1 118 ? 54.590 -12.031 -23.940  1.00 14.55 ? 118  VAL H CB  1 
ATOM   7554  C  CG1 . VAL G  1 118 ? 56.098 -12.011 -24.278  1.00 13.55 ? 118  VAL H CG1 1 
ATOM   7555  C  CG2 . VAL G  1 118 ? 54.113 -13.448 -23.747  1.00 15.12 ? 118  VAL H CG2 1 
ATOM   7556  N  N   . VAL G  1 119 ? 55.961 -9.421  -22.383  1.00 15.16 ? 119  VAL H N   1 
ATOM   7557  C  CA  . VAL G  1 119 ? 56.727 -8.228  -22.744  1.00 15.29 ? 119  VAL H CA  1 
ATOM   7558  C  C   . VAL G  1 119 ? 57.984 -8.651  -23.530  1.00 15.98 ? 119  VAL H C   1 
ATOM   7559  O  O   . VAL G  1 119 ? 58.684 -9.613  -23.165  1.00 16.38 ? 119  VAL H O   1 
ATOM   7560  C  CB  . VAL G  1 119 ? 57.023 -7.290  -21.525  1.00 15.59 ? 119  VAL H CB  1 
ATOM   7561  C  CG1 . VAL G  1 119 ? 58.029 -7.905  -20.547  1.00 14.39 ? 119  VAL H CG1 1 
ATOM   7562  C  CG2 . VAL G  1 119 ? 57.504 -5.909  -21.996  1.00 14.28 ? 119  VAL H CG2 1 
ATOM   7563  N  N   . HIS G  1 120 ? 58.212 -7.965  -24.646  1.00 15.38 ? 120  HIS H N   1 
ATOM   7564  C  CA  . HIS G  1 120 ? 59.198 -8.372  -25.629  1.00 16.06 ? 120  HIS H CA  1 
ATOM   7565  C  C   . HIS G  1 120 ? 60.494 -7.571  -25.586  1.00 16.58 ? 120  HIS H C   1 
ATOM   7566  O  O   . HIS G  1 120 ? 60.575 -6.510  -24.950  1.00 17.00 ? 120  HIS H O   1 
ATOM   7567  C  CB  . HIS G  1 120 ? 58.600 -8.249  -27.034  1.00 15.99 ? 120  HIS H CB  1 
ATOM   7568  C  CG  . HIS G  1 120 ? 57.714 -9.393  -27.415  1.00 16.56 ? 120  HIS H CG  1 
ATOM   7569  N  ND1 . HIS G  1 120 ? 58.152 -10.453 -28.178  1.00 18.54 ? 120  HIS H ND1 1 
ATOM   7570  C  CD2 . HIS G  1 120 ? 56.408 -9.639  -27.149  1.00 17.19 ? 120  HIS H CD2 1 
ATOM   7571  C  CE1 . HIS G  1 120 ? 57.160 -11.303 -28.365  1.00 16.82 ? 120  HIS H CE1 1 
ATOM   7572  N  NE2 . HIS G  1 120 ? 56.092 -10.836 -27.744  1.00 16.58 ? 120  HIS H NE2 1 
ATOM   7573  N  N   . GLU G  1 121 ? 61.481 -8.090  -26.310  1.00 16.42 ? 121  GLU H N   1 
ATOM   7574  C  CA  . GLU G  1 121 ? 62.822 -7.544  -26.415  1.00 17.61 ? 121  GLU H CA  1 
ATOM   7575  C  C   . GLU G  1 121 ? 62.877 -6.189  -27.097  1.00 17.55 ? 121  GLU H C   1 
ATOM   7576  O  O   . GLU G  1 121 ? 63.568 -5.257  -26.642  1.00 18.22 ? 121  GLU H O   1 
ATOM   7577  C  CB  . GLU G  1 121 ? 63.638 -8.520  -27.268  1.00 17.93 ? 121  GLU H CB  1 
ATOM   7578  C  CG  . GLU G  1 121 ? 65.063 -8.104  -27.560  1.00 20.42 ? 121  GLU H CG  1 
ATOM   7579  C  CD  . GLU G  1 121 ? 65.718 -9.018  -28.586  1.00 23.11 ? 121  GLU H CD  1 
ATOM   7580  O  OE1 . GLU G  1 121 ? 66.939 -8.868  -28.822  1.00 24.55 ? 121  GLU H OE1 1 
ATOM   7581  O  OE2 . GLU G  1 121 ? 65.015 -9.888  -29.157  1.00 23.29 ? 121  GLU H OE2 1 
ATOM   7582  N  N   . LYS G  1 122 ? 62.165 -6.117  -28.218  1.00 17.27 ? 122  LYS H N   1 
ATOM   7583  C  CA  . LYS G  1 122 ? 62.260 -5.022  -29.174  1.00 17.35 ? 122  LYS H CA  1 
ATOM   7584  C  C   . LYS G  1 122 ? 60.896 -4.358  -29.333  1.00 16.03 ? 122  LYS H C   1 
ATOM   7585  O  O   . LYS G  1 122 ? 59.893 -4.842  -28.792  1.00 15.76 ? 122  LYS H O   1 
ATOM   7586  C  CB  . LYS G  1 122 ? 62.691 -5.553  -30.544  1.00 17.54 ? 122  LYS H CB  1 
ATOM   7587  C  CG  . LYS G  1 122 ? 64.023 -6.250  -30.609  1.00 20.48 ? 122  LYS H CG  1 
ATOM   7588  C  CD  . LYS G  1 122 ? 64.381 -6.445  -32.064  1.00 23.62 ? 122  LYS H CD  1 
ATOM   7589  C  CE  . LYS G  1 122 ? 65.466 -7.494  -32.264  1.00 27.15 ? 122  LYS H CE  1 
ATOM   7590  N  NZ  . LYS G  1 122 ? 65.521 -7.885  -33.705  1.00 28.90 ? 122  LYS H NZ  1 
ATOM   7591  N  N   . ALA G  1 123 ? 60.881 -3.250  -30.074  1.00 14.43 ? 123  ALA H N   1 
ATOM   7592  C  CA  . ALA G  1 123 ? 59.636 -2.594  -30.456  1.00 13.68 ? 123  ALA H CA  1 
ATOM   7593  C  C   . ALA G  1 123 ? 58.801 -3.484  -31.380  1.00 12.09 ? 123  ALA H C   1 
ATOM   7594  O  O   . ALA G  1 123 ? 59.324 -4.195  -32.218  1.00 11.76 ? 123  ALA H O   1 
ATOM   7595  C  CB  . ALA G  1 123 ? 59.923 -1.280  -31.145  1.00 13.11 ? 123  ALA H CB  1 
ATOM   7596  N  N   . ASP G  1 124 ? 57.493 -3.409  -31.208  1.00 11.76 ? 124  ASP H N   1 
ATOM   7597  C  CA  . ASP G  1 124 ? 56.526 -4.006  -32.113  1.00 10.29 ? 124  ASP H CA  1 
ATOM   7598  C  C   . ASP G  1 124 ? 56.340 -2.971  -33.231  1.00 10.26 ? 124  ASP H C   1 
ATOM   7599  O  O   . ASP G  1 124 ? 55.965 -1.835  -32.936  1.00 9.42  ? 124  ASP H O   1 
ATOM   7600  C  CB  . ASP G  1 124 ? 55.242 -4.213  -31.303  1.00 9.85  ? 124  ASP H CB  1 
ATOM   7601  C  CG  . ASP G  1 124 ? 54.127 -4.888  -32.082  1.00 8.76  ? 124  ASP H CG  1 
ATOM   7602  O  OD1 . ASP G  1 124 ? 53.230 -5.454  -31.412  1.00 11.47 ? 124  ASP H OD1 1 
ATOM   7603  O  OD2 . ASP G  1 124 ? 54.097 -4.811  -33.328  1.00 8.61  ? 124  ASP H OD2 1 
ATOM   7604  N  N   . ASP G  1 125 ? 56.606 -3.349  -34.497  1.00 9.14  ? 125  ASP H N   1 
ATOM   7605  C  CA  . ASP G  1 125 ? 56.448 -2.419  -35.651  1.00 8.48  ? 125  ASP H CA  1 
ATOM   7606  C  C   . ASP G  1 125 ? 54.969 -2.212  -36.066  1.00 7.37  ? 125  ASP H C   1 
ATOM   7607  O  O   . ASP G  1 125 ? 54.650 -1.490  -37.020  1.00 6.16  ? 125  ASP H O   1 
ATOM   7608  C  CB  . ASP G  1 125 ? 57.347 -2.825  -36.844  1.00 9.14  ? 125  ASP H CB  1 
ATOM   7609  C  CG  . ASP G  1 125 ? 56.894 -4.129  -37.539  1.00 10.37 ? 125  ASP H CG  1 
ATOM   7610  O  OD1 . ASP G  1 125 ? 57.730 -4.745  -38.254  1.00 10.62 ? 125  ASP H OD1 1 
ATOM   7611  O  OD2 . ASP G  1 125 ? 55.724 -4.539  -37.379  1.00 10.76 ? 125  ASP H OD2 1 
ATOM   7612  N  N   . LEU G  1 126 ? 54.082 -2.874  -35.326  1.00 6.71  ? 126  LEU H N   1 
ATOM   7613  C  CA  . LEU G  1 126 ? 52.628 -2.703  -35.418  1.00 7.03  ? 126  LEU H CA  1 
ATOM   7614  C  C   . LEU G  1 126 ? 52.084 -3.105  -36.784  1.00 6.73  ? 126  LEU H C   1 
ATOM   7615  O  O   . LEU G  1 126 ? 51.024 -2.629  -37.214  1.00 7.11  ? 126  LEU H O   1 
ATOM   7616  C  CB  . LEU G  1 126 ? 52.230 -1.251  -35.045  1.00 7.22  ? 126  LEU H CB  1 
ATOM   7617  C  CG  . LEU G  1 126 ? 52.777 -0.698  -33.723  1.00 8.16  ? 126  LEU H CG  1 
ATOM   7618  C  CD1 . LEU G  1 126 ? 52.248 0.724   -33.508  1.00 7.46  ? 126  LEU H CD1 1 
ATOM   7619  C  CD2 . LEU G  1 126 ? 52.388 -1.613  -32.564  1.00 9.18  ? 126  LEU H CD2 1 
ATOM   7620  N  N   . GLY G  1 127 ? 52.810 -3.995  -37.461  1.00 7.63  ? 127  GLY H N   1 
ATOM   7621  C  CA  . GLY G  1 127 ? 52.393 -4.494  -38.780  1.00 7.43  ? 127  GLY H CA  1 
ATOM   7622  C  C   . GLY G  1 127 ? 52.816 -3.645  -39.971  1.00 8.00  ? 127  GLY H C   1 
ATOM   7623  O  O   . GLY G  1 127 ? 52.389 -3.914  -41.100  1.00 7.95  ? 127  GLY H O   1 
ATOM   7624  N  N   . LYS G  1 128 ? 53.678 -2.653  -39.733  1.00 7.86  ? 128  LYS H N   1 
ATOM   7625  C  CA  . LYS G  1 128 ? 54.100 -1.686  -40.769  1.00 9.15  ? 128  LYS H CA  1 
ATOM   7626  C  C   . LYS G  1 128 ? 55.548 -1.890  -41.284  1.00 9.79  ? 128  LYS H C   1 
ATOM   7627  O  O   . LYS G  1 128 ? 56.142 -0.980  -41.907  1.00 10.47 ? 128  LYS H O   1 
ATOM   7628  C  CB  . LYS G  1 128 ? 53.937 -0.261  -40.250  1.00 9.70  ? 128  LYS H CB  1 
ATOM   7629  C  CG  . LYS G  1 128 ? 52.492 0.095   -39.872  1.00 12.28 ? 128  LYS H CG  1 
ATOM   7630  C  CD  . LYS G  1 128 ? 52.424 1.420   -39.101  1.00 16.59 ? 128  LYS H CD  1 
ATOM   7631  C  CE  . LYS G  1 128 ? 51.946 2.563   -39.955  1.00 18.74 ? 128  LYS H CE  1 
ATOM   7632  N  NZ  . LYS G  1 128 ? 51.621 3.784   -39.131  1.00 22.29 ? 128  LYS H NZ  1 
ATOM   7633  N  N   . GLY G  1 129 ? 56.099 -3.065  -41.007  1.00 9.42  ? 129  GLY H N   1 
ATOM   7634  C  CA  . GLY G  1 129 ? 57.474 -3.419  -41.389  1.00 9.50  ? 129  GLY H CA  1 
ATOM   7635  C  C   . GLY G  1 129 ? 57.716 -3.785  -42.849  1.00 9.71  ? 129  GLY H C   1 
ATOM   7636  O  O   . GLY G  1 129 ? 58.852 -3.713  -43.314  1.00 10.38 ? 129  GLY H O   1 
ATOM   7637  N  N   . GLY G  1 130 ? 56.677 -4.195  -43.571  1.00 9.25  ? 130  GLY H N   1 
ATOM   7638  C  CA  . GLY G  1 130 ? 56.805 -4.453  -45.007  1.00 10.05 ? 130  GLY H CA  1 
ATOM   7639  C  C   . GLY G  1 130 ? 57.337 -5.836  -45.330  1.00 11.32 ? 130  GLY H C   1 
ATOM   7640  O  O   . GLY G  1 130 ? 57.770 -6.106  -46.471  1.00 11.27 ? 130  GLY H O   1 
ATOM   7641  N  N   . ASN G  1 131 ? 57.293 -6.706  -44.318  1.00 12.02 ? 131  ASN H N   1 
ATOM   7642  C  CA  . ASN G  1 131 ? 57.645 -8.114  -44.454  1.00 13.17 ? 131  ASN H CA  1 
ATOM   7643  C  C   . ASN G  1 131 ? 56.582 -9.028  -43.862  1.00 13.24 ? 131  ASN H C   1 
ATOM   7644  O  O   . ASN G  1 131 ? 55.691 -8.564  -43.144  1.00 12.53 ? 131  ASN H O   1 
ATOM   7645  C  CB  . ASN G  1 131 ? 59.032 -8.423  -43.865  1.00 13.05 ? 131  ASN H CB  1 
ATOM   7646  C  CG  . ASN G  1 131 ? 59.217 -7.942  -42.414  1.00 13.68 ? 131  ASN H CG  1 
ATOM   7647  O  OD1 . ASN G  1 131 ? 58.370 -8.127  -41.547  1.00 12.67 ? 131  ASN H OD1 1 
ATOM   7648  N  ND2 . ASN G  1 131 ? 60.376 -7.386  -42.149  1.00 13.88 ? 131  ASN H ND2 1 
ATOM   7649  N  N   . GLU G  1 132 ? 56.680 -10.329 -44.155  1.00 13.62 ? 132  GLU H N   1 
ATOM   7650  C  CA  . GLU G  1 132 ? 55.688 -11.285 -43.664  1.00 14.88 ? 132  GLU H CA  1 
ATOM   7651  C  C   . GLU G  1 132 ? 55.673 -11.325 -42.136  1.00 14.82 ? 132  GLU H C   1 
ATOM   7652  O  O   . GLU G  1 132 ? 54.596 -11.424 -41.531  1.00 15.31 ? 132  GLU H O   1 
ATOM   7653  C  CB  . GLU G  1 132 ? 55.924 -12.690 -44.258  1.00 15.43 ? 132  GLU H CB  1 
ATOM   7654  C  CG  . GLU G  1 132 ? 54.742 -13.677 -44.085  1.00 19.12 ? 132  GLU H CG  1 
ATOM   7655  C  CD  . GLU G  1 132 ? 55.110 -15.140 -44.434  1.00 23.16 ? 132  GLU H CD  1 
ATOM   7656  O  OE1 . GLU G  1 132 ? 54.244 -16.035 -44.271  1.00 24.85 ? 132  GLU H OE1 1 
ATOM   7657  O  OE2 . GLU G  1 132 ? 56.263 -15.399 -44.860  1.00 23.98 ? 132  GLU H OE2 1 
ATOM   7658  N  N   . GLU G  1 133 ? 56.859 -11.238 -41.521  1.00 14.53 ? 133  GLU H N   1 
ATOM   7659  C  CA  . GLU G  1 133 ? 56.984 -11.368 -40.068  1.00 14.28 ? 133  GLU H CA  1 
ATOM   7660  C  C   . GLU G  1 133 ? 56.331 -10.179 -39.364  1.00 13.46 ? 133  GLU H C   1 
ATOM   7661  O  O   . GLU G  1 133 ? 55.780 -10.339 -38.289  1.00 13.50 ? 133  GLU H O   1 
ATOM   7662  C  CB  . GLU G  1 133 ? 58.450 -11.579 -39.652  1.00 14.32 ? 133  GLU H CB  1 
ATOM   7663  C  CG  . GLU G  1 133 ? 58.715 -11.926 -38.158  1.00 15.88 ? 133  GLU H CG  1 
ATOM   7664  C  CD  . GLU G  1 133 ? 58.156 -13.272 -37.673  1.00 17.06 ? 133  GLU H CD  1 
ATOM   7665  O  OE1 . GLU G  1 133 ? 58.619 -13.757 -36.623  1.00 20.46 ? 133  GLU H OE1 1 
ATOM   7666  O  OE2 . GLU G  1 133 ? 57.255 -13.847 -38.296  1.00 19.20 ? 133  GLU H OE2 1 
ATOM   7667  N  N   . SER G  1 134 ? 56.358 -9.005  -39.999  1.00 13.16 ? 134  SER H N   1 
ATOM   7668  C  CA  . SER G  1 134 ? 55.609 -7.835  -39.486  1.00 12.75 ? 134  SER H CA  1 
ATOM   7669  C  C   . SER G  1 134 ? 54.123 -8.161  -39.304  1.00 12.70 ? 134  SER H C   1 
ATOM   7670  O  O   . SER G  1 134 ? 53.524 -7.780  -38.295  1.00 12.05 ? 134  SER H O   1 
ATOM   7671  C  CB  . SER G  1 134 ? 55.804 -6.606  -40.386  1.00 12.28 ? 134  SER H CB  1 
ATOM   7672  O  OG  . SER G  1 134 ? 55.028 -5.509  -39.927  1.00 12.51 ? 134  SER H OG  1 
ATOM   7673  N  N   . THR G  1 135 ? 53.551 -8.897  -40.266  1.00 13.15 ? 135  THR H N   1 
ATOM   7674  C  CA  . THR G  1 135 ? 52.126 -9.269  -40.234  1.00 13.97 ? 135  THR H CA  1 
ATOM   7675  C  C   . THR G  1 135 ? 51.811 -10.436 -39.280  1.00 14.06 ? 135  THR H C   1 
ATOM   7676  O  O   . THR G  1 135 ? 50.651 -10.836 -39.150  1.00 13.96 ? 135  THR H O   1 
ATOM   7677  C  CB  . THR G  1 135 ? 51.572 -9.598  -41.660  1.00 14.53 ? 135  THR H CB  1 
ATOM   7678  O  OG1 . THR G  1 135 ? 51.976 -10.920 -42.054  1.00 16.70 ? 135  THR H OG1 1 
ATOM   7679  C  CG2 . THR G  1 135 ? 52.057 -8.595  -42.687  1.00 15.57 ? 135  THR H CG2 1 
ATOM   7680  N  N   . LYS G  1 136 ? 52.826 -10.966 -38.596  1.00 14.35 ? 136  LYS H N   1 
ATOM   7681  C  CA  . LYS G  1 136 ? 52.624 -12.096 -37.671  1.00 15.02 ? 136  LYS H CA  1 
ATOM   7682  C  C   . LYS G  1 136 ? 52.960 -11.773 -36.202  1.00 14.70 ? 136  LYS H C   1 
ATOM   7683  O  O   . LYS G  1 136 ? 52.174 -12.048 -35.293  1.00 15.43 ? 136  LYS H O   1 
ATOM   7684  C  CB  . LYS G  1 136 ? 53.427 -13.319 -38.146  1.00 15.62 ? 136  LYS H CB  1 
ATOM   7685  C  CG  . LYS G  1 136 ? 52.774 -14.058 -39.323  1.00 18.42 ? 136  LYS H CG  1 
ATOM   7686  C  CD  . LYS G  1 136 ? 53.683 -15.148 -39.875  1.00 21.88 ? 136  LYS H CD  1 
ATOM   7687  C  CE  . LYS G  1 136 ? 52.920 -16.098 -40.796  1.00 23.86 ? 136  LYS H CE  1 
ATOM   7688  N  NZ  . LYS G  1 136 ? 53.819 -17.221 -41.254  1.00 26.28 ? 136  LYS H NZ  1 
ATOM   7689  N  N   . THR G  1 137 ? 54.117 -11.159 -35.986  1.00 14.58 ? 137  THR H N   1 
ATOM   7690  C  CA  . THR G  1 137 ? 54.661 -10.896 -34.640  1.00 14.57 ? 137  THR H CA  1 
ATOM   7691  C  C   . THR G  1 137 ? 55.002 -9.417  -34.399  1.00 14.09 ? 137  THR H C   1 
ATOM   7692  O  O   . THR G  1 137 ? 55.269 -8.994  -33.256  1.00 13.48 ? 137  THR H O   1 
ATOM   7693  C  CB  . THR G  1 137 ? 55.980 -11.671 -34.454  1.00 14.90 ? 137  THR H CB  1 
ATOM   7694  O  OG1 . THR G  1 137 ? 56.927 -11.200 -35.417  1.00 14.41 ? 137  THR H OG1 1 
ATOM   7695  C  CG2 . THR G  1 137 ? 55.791 -13.179 -34.655  1.00 14.88 ? 137  THR H CG2 1 
ATOM   7696  N  N   . GLY G  1 138 ? 55.017 -8.642  -35.482  1.00 14.28 ? 138  GLY H N   1 
ATOM   7697  C  CA  . GLY G  1 138 ? 55.459 -7.255  -35.444  1.00 14.16 ? 138  GLY H CA  1 
ATOM   7698  C  C   . GLY G  1 138 ? 56.958 -7.098  -35.249  1.00 14.72 ? 138  GLY H C   1 
ATOM   7699  O  O   . GLY G  1 138 ? 57.447 -5.987  -35.012  1.00 13.75 ? 138  GLY H O   1 
ATOM   7700  N  N   . ASN G  1 139 ? 57.691 -8.212  -35.345  1.00 15.08 ? 139  ASN H N   1 
ATOM   7701  C  CA  . ASN G  1 139 ? 59.150 -8.202  -35.207  1.00 15.21 ? 139  ASN H CA  1 
ATOM   7702  C  C   . ASN G  1 139 ? 59.624 -7.717  -33.837  1.00 15.00 ? 139  ASN H C   1 
ATOM   7703  O  O   . ASN G  1 139 ? 60.623 -7.010  -33.747  1.00 15.80 ? 139  ASN H O   1 
ATOM   7704  C  CB  . ASN G  1 139 ? 59.784 -7.361  -36.337  1.00 15.22 ? 139  ASN H CB  1 
ATOM   7705  C  CG  . ASN G  1 139 ? 59.575 -7.976  -37.719  1.00 17.65 ? 139  ASN H CG  1 
ATOM   7706  O  OD1 . ASN G  1 139 ? 60.014 -9.100  -37.982  1.00 19.12 ? 139  ASN H OD1 1 
ATOM   7707  N  ND2 . ASN G  1 139 ? 58.927 -7.227  -38.619  1.00 17.77 ? 139  ASN H ND2 1 
ATOM   7708  N  N   . ALA G  1 140 ? 58.908 -8.105  -32.778  1.00 15.25 ? 140  ALA H N   1 
ATOM   7709  C  CA  . ALA G  1 140 ? 59.163 -7.611  -31.431  1.00 15.41 ? 140  ALA H CA  1 
ATOM   7710  C  C   . ALA G  1 140 ? 60.259 -8.415  -30.714  1.00 16.18 ? 140  ALA H C   1 
ATOM   7711  O  O   . ALA G  1 140 ? 60.586 -8.146  -29.547  1.00 15.79 ? 140  ALA H O   1 
ATOM   7712  C  CB  . ALA G  1 140 ? 57.876 -7.613  -30.605  1.00 15.96 ? 140  ALA H CB  1 
ATOM   7713  N  N   . GLY G  1 141 ? 60.830 -9.393  -31.410  1.00 16.18 ? 141  GLY H N   1 
ATOM   7714  C  CA  . GLY G  1 141 ? 61.966 -10.127 -30.859  1.00 17.50 ? 141  GLY H CA  1 
ATOM   7715  C  C   . GLY G  1 141 ? 61.575 -11.033 -29.717  1.00 17.72 ? 141  GLY H C   1 
ATOM   7716  O  O   . GLY G  1 141 ? 60.401 -11.421 -29.583  1.00 17.47 ? 141  GLY H O   1 
ATOM   7717  N  N   . SER G  1 142 ? 62.554 -11.347 -28.872  1.00 18.38 ? 142  SER H N   1 
ATOM   7718  C  CA  . SER G  1 142 ? 62.382 -12.380 -27.859  1.00 19.53 ? 142  SER H CA  1 
ATOM   7719  C  C   . SER G  1 142 ? 61.435 -11.997 -26.722  1.00 19.50 ? 142  SER H C   1 
ATOM   7720  O  O   . SER G  1 142 ? 61.077 -10.822 -26.537  1.00 20.07 ? 142  SER H O   1 
ATOM   7721  C  CB  . SER G  1 142 ? 63.746 -12.816 -27.293  1.00 19.76 ? 142  SER H CB  1 
ATOM   7722  O  OG  . SER G  1 142 ? 64.402 -11.724 -26.667  1.00 21.14 ? 142  SER H OG  1 
ATOM   7723  N  N   . ARG G  1 143 ? 61.052 -13.010 -25.957  1.00 19.41 ? 143  ARG H N   1 
ATOM   7724  C  CA  . ARG G  1 143 ? 60.105 -12.867 -24.861  1.00 19.62 ? 143  ARG H CA  1 
ATOM   7725  C  C   . ARG G  1 143 ? 60.866 -12.754 -23.552  1.00 20.08 ? 143  ARG H C   1 
ATOM   7726  O  O   . ARG G  1 143 ? 61.383 -13.743 -23.033  1.00 20.25 ? 143  ARG H O   1 
ATOM   7727  C  CB  . ARG G  1 143 ? 59.125 -14.054 -24.863  1.00 19.26 ? 143  ARG H CB  1 
ATOM   7728  C  CG  . ARG G  1 143 ? 58.413 -14.207 -26.214  1.00 19.05 ? 143  ARG H CG  1 
ATOM   7729  C  CD  . ARG G  1 143 ? 57.723 -15.552 -26.398  1.00 17.49 ? 143  ARG H CD  1 
ATOM   7730  N  NE  . ARG G  1 143 ? 57.151 -15.679 -27.743  1.00 18.06 ? 143  ARG H NE  1 
ATOM   7731  C  CZ  . ARG G  1 143 ? 56.162 -16.507 -28.089  1.00 17.69 ? 143  ARG H CZ  1 
ATOM   7732  N  NH1 . ARG G  1 143 ? 55.727 -16.530 -29.343  1.00 17.23 ? 143  ARG H NH1 1 
ATOM   7733  N  NH2 . ARG G  1 143 ? 55.593 -17.309 -27.196  1.00 16.07 ? 143  ARG H NH2 1 
ATOM   7734  N  N   . LEU G  1 144 ? 60.943 -11.531 -23.031  1.00 20.28 ? 144  LEU H N   1 
ATOM   7735  C  CA  . LEU G  1 144 ? 61.753 -11.247 -21.853  1.00 20.33 ? 144  LEU H CA  1 
ATOM   7736  C  C   . LEU G  1 144 ? 61.101 -11.679 -20.552  1.00 20.35 ? 144  LEU H C   1 
ATOM   7737  O  O   . LEU G  1 144 ? 61.799 -12.073 -19.611  1.00 19.98 ? 144  LEU H O   1 
ATOM   7738  C  CB  . LEU G  1 144 ? 62.096 -9.756  -21.774  1.00 20.45 ? 144  LEU H CB  1 
ATOM   7739  C  CG  . LEU G  1 144 ? 62.832 -9.094  -22.937  1.00 20.80 ? 144  LEU H CG  1 
ATOM   7740  C  CD1 . LEU G  1 144 ? 63.006 -7.590  -22.652  1.00 21.35 ? 144  LEU H CD1 1 
ATOM   7741  C  CD2 . LEU G  1 144 ? 64.172 -9.759  -23.213  1.00 21.15 ? 144  LEU H CD2 1 
ATOM   7742  N  N   . ALA G  1 145 ? 59.770 -11.573 -20.487  1.00 19.74 ? 145  ALA H N   1 
ATOM   7743  C  CA  . ALA G  1 145 ? 59.013 -12.004 -19.317  1.00 19.26 ? 145  ALA H CA  1 
ATOM   7744  C  C   . ALA G  1 145 ? 57.558 -12.254 -19.685  1.00 19.43 ? 145  ALA H C   1 
ATOM   7745  O  O   . ALA G  1 145 ? 57.036 -11.661 -20.631  1.00 18.68 ? 145  ALA H O   1 
ATOM   7746  C  CB  . ALA G  1 145 ? 59.097 -10.990 -18.207  1.00 19.53 ? 145  ALA H CB  1 
ATOM   7747  N  N   . CYS G  1 146 ? 56.916 -13.131 -18.917  1.00 18.35 ? 146  CYS H N   1 
ATOM   7748  C  CA  . CYS G  1 146 ? 55.531 -13.513 -19.155  1.00 17.87 ? 146  CYS H CA  1 
ATOM   7749  C  C   . CYS G  1 146 ? 54.912 -14.010 -17.851  1.00 18.01 ? 146  CYS H C   1 
ATOM   7750  O  O   . CYS G  1 146 ? 55.627 -14.289 -16.881  1.00 17.51 ? 146  CYS H O   1 
ATOM   7751  C  CB  . CYS G  1 146 ? 55.455 -14.599 -20.225  0.40 17.80 ? 146  CYS H CB  1 
ATOM   7752  S  SG  . CYS G  1 146 ? 56.467 -16.025 -19.866  0.40 16.69 ? 146  CYS H SG  1 
ATOM   7753  N  N   . GLY G  1 147 ? 53.586 -14.079 -17.825  1.00 17.59 ? 147  GLY H N   1 
ATOM   7754  C  CA  . GLY G  1 147 ? 52.859 -14.713 -16.734  1.00 17.90 ? 147  GLY H CA  1 
ATOM   7755  C  C   . GLY G  1 147 ? 51.469 -15.076 -17.215  1.00 18.27 ? 147  GLY H C   1 
ATOM   7756  O  O   . GLY G  1 147 ? 50.978 -14.481 -18.193  1.00 17.56 ? 147  GLY H O   1 
ATOM   7757  N  N   . VAL G  1 148 ? 50.838 -16.054 -16.559  1.00 17.86 ? 148  VAL H N   1 
ATOM   7758  C  CA  . VAL G  1 148 ? 49.452 -16.424 -16.898  1.00 18.35 ? 148  VAL H CA  1 
ATOM   7759  C  C   . VAL G  1 148 ? 48.487 -15.435 -16.257  1.00 18.33 ? 148  VAL H C   1 
ATOM   7760  O  O   . VAL G  1 148 ? 48.629 -15.084 -15.077  1.00 19.04 ? 148  VAL H O   1 
ATOM   7761  C  CB  . VAL G  1 148 ? 49.100 -17.895 -16.469  1.00 18.54 ? 148  VAL H CB  1 
ATOM   7762  C  CG1 . VAL G  1 148 ? 47.621 -18.222 -16.763  1.00 18.62 ? 148  VAL H CG1 1 
ATOM   7763  C  CG2 . VAL G  1 148 ? 50.011 -18.905 -17.165  1.00 18.87 ? 148  VAL H CG2 1 
ATOM   7764  N  N   . ILE G  1 149 ? 47.521 -14.962 -17.038  1.00 18.47 ? 149  ILE H N   1 
ATOM   7765  C  CA  . ILE G  1 149 ? 46.538 -13.995 -16.551  1.00 19.06 ? 149  ILE H CA  1 
ATOM   7766  C  C   . ILE G  1 149 ? 45.478 -14.732 -15.716  1.00 19.22 ? 149  ILE H C   1 
ATOM   7767  O  O   . ILE G  1 149 ? 44.800 -15.618 -16.229  1.00 19.68 ? 149  ILE H O   1 
ATOM   7768  C  CB  . ILE G  1 149 ? 45.890 -13.213 -17.721  1.00 18.19 ? 149  ILE H CB  1 
ATOM   7769  C  CG1 . ILE G  1 149 ? 46.944 -12.367 -18.462  1.00 19.17 ? 149  ILE H CG1 1 
ATOM   7770  C  CG2 . ILE G  1 149 ? 44.722 -12.346 -17.235  1.00 19.19 ? 149  ILE H CG2 1 
ATOM   7771  C  CD1 . ILE G  1 149 ? 46.508 -11.949 -19.887  1.00 17.60 ? 149  ILE H CD1 1 
ATOM   7772  N  N   . GLY G  1 150 ? 45.357 -14.367 -14.435  1.00 19.38 ? 150  GLY H N   1 
ATOM   7773  C  CA  . GLY G  1 150 ? 44.369 -14.978 -13.525  1.00 18.88 ? 150  GLY H CA  1 
ATOM   7774  C  C   . GLY G  1 150 ? 43.280 -14.048 -13.016  1.00 19.27 ? 150  GLY H C   1 
ATOM   7775  O  O   . GLY G  1 150 ? 43.424 -12.822 -13.044  1.00 18.83 ? 150  GLY H O   1 
ATOM   7776  N  N   . ILE G  1 151 ? 42.190 -14.631 -12.524  1.00 19.52 ? 151  ILE H N   1 
ATOM   7777  C  CA  . ILE G  1 151 ? 41.075 -13.855 -11.979  1.00 20.68 ? 151  ILE H CA  1 
ATOM   7778  C  C   . ILE G  1 151 ? 41.494 -13.224 -10.647  1.00 20.89 ? 151  ILE H C   1 
ATOM   7779  O  O   . ILE G  1 151 ? 42.171 -13.852 -9.849   1.00 20.55 ? 151  ILE H O   1 
ATOM   7780  C  CB  . ILE G  1 151 ? 39.776 -14.717 -11.832  1.00 20.69 ? 151  ILE H CB  1 
ATOM   7781  C  CG1 . ILE G  1 151 ? 39.407 -15.318 -13.191  1.00 21.04 ? 151  ILE H CG1 1 
ATOM   7782  C  CG2 . ILE G  1 151 ? 38.603 -13.875 -11.311  1.00 21.82 ? 151  ILE H CG2 1 
ATOM   7783  C  CD1 . ILE G  1 151 ? 38.385 -16.478 -13.166  1.00 21.10 ? 151  ILE H CD1 1 
ATOM   7784  N  N   . ALA G  1 152 ? 41.098 -11.973 -10.433  1.00 22.02 ? 152  ALA H N   1 
ATOM   7785  C  CA  . ALA G  1 152 ? 41.477 -11.216 -9.231   1.00 22.86 ? 152  ALA H CA  1 
ATOM   7786  C  C   . ALA G  1 152 ? 40.240 -10.761 -8.454   1.00 23.71 ? 152  ALA H C   1 
ATOM   7787  O  O   . ALA G  1 152 ? 39.128 -10.745 -8.991   1.00 23.59 ? 152  ALA H O   1 
ATOM   7788  C  CB  . ALA G  1 152 ? 42.348 -10.014 -9.622   1.00 23.18 ? 152  ALA H CB  1 
ATOM   7789  N  N   . GLN G  1 153 ? 40.425 -10.404 -7.186   1.00 25.07 ? 153  GLN H N   1 
ATOM   7790  C  CA  . GLN G  1 153 ? 39.307 -9.997  -6.346   1.00 26.51 ? 153  GLN H CA  1 
ATOM   7791  C  C   . GLN G  1 153 ? 38.825 -8.581  -6.648   1.00 26.94 ? 153  GLN H C   1 
ATOM   7792  O  O   . GLN G  1 153 ? 39.630 -7.667  -6.824   1.00 27.79 ? 153  GLN H O   1 
ATOM   7793  C  CB  . GLN G  1 153 ? 39.668 -10.129 -4.861   1.00 26.59 ? 153  GLN H CB  1 
ATOM   7794  C  CG  . GLN G  1 153 ? 38.482 -9.865  -3.941   1.00 28.71 ? 153  GLN H CG  1 
ATOM   7795  C  CD  . GLN G  1 153 ? 38.657 -10.436 -2.550   1.00 30.04 ? 153  GLN H CD  1 
ATOM   7796  O  OE1 . GLN G  1 153 ? 37.695 -10.930 -1.950   1.00 32.39 ? 153  GLN H OE1 1 
ATOM   7797  N  NE2 . GLN G  1 153 ? 39.880 -10.369 -2.022   1.00 28.80 ? 153  GLN H NE2 1 
ATOM   7798  O  OXT . GLN G  1 153 ? 37.618 -8.312  -6.704   1.00 27.47 ? 153  GLN H OXT 1 
ATOM   7799  N  N   . ALA H  1 1   ? 37.749 -31.451 -27.459  1.00 30.91 ? 1    ALA I N   1 
ATOM   7800  C  CA  . ALA H  1 1   ? 38.709 -31.602 -26.320  1.00 31.12 ? 1    ALA I CA  1 
ATOM   7801  C  C   . ALA H  1 1   ? 39.245 -30.240 -25.854  1.00 31.19 ? 1    ALA I C   1 
ATOM   7802  O  O   . ALA H  1 1   ? 39.717 -29.444 -26.671  1.00 31.53 ? 1    ALA I O   1 
ATOM   7803  C  CB  . ALA H  1 1   ? 39.867 -32.525 -26.716  1.00 30.97 ? 1    ALA I CB  1 
ATOM   7804  N  N   . THR H  1 2   ? 39.156 -29.977 -24.549  1.00 30.72 ? 2    THR I N   1 
ATOM   7805  C  CA  . THR H  1 2   ? 39.720 -28.758 -23.946  1.00 30.28 ? 2    THR I CA  1 
ATOM   7806  C  C   . THR H  1 2   ? 40.848 -29.156 -23.002  1.00 30.15 ? 2    THR I C   1 
ATOM   7807  O  O   . THR H  1 2   ? 40.707 -30.117 -22.236  1.00 30.28 ? 2    THR I O   1 
ATOM   7808  C  CB  . THR H  1 2   ? 38.655 -27.962 -23.151  1.00 30.20 ? 2    THR I CB  1 
ATOM   7809  O  OG1 . THR H  1 2   ? 37.566 -27.610 -24.012  1.00 30.72 ? 2    THR I OG1 1 
ATOM   7810  C  CG2 . THR H  1 2   ? 39.259 -26.673 -22.568  1.00 29.99 ? 2    THR I CG2 1 
ATOM   7811  N  N   . LYS H  1 3   ? 41.967 -28.436 -23.058  1.00 29.89 ? 3    LYS I N   1 
ATOM   7812  C  CA  . LYS H  1 3   ? 43.099 -28.736 -22.174  1.00 29.77 ? 3    LYS I CA  1 
ATOM   7813  C  C   . LYS H  1 3   ? 43.552 -27.526 -21.368  1.00 29.56 ? 3    LYS I C   1 
ATOM   7814  O  O   . LYS H  1 3   ? 43.413 -26.387 -21.816  1.00 28.71 ? 3    LYS I O   1 
ATOM   7815  C  CB  . LYS H  1 3   ? 44.282 -29.303 -22.971  1.00 30.07 ? 3    LYS I CB  1 
ATOM   7816  C  CG  . LYS H  1 3   ? 43.976 -30.583 -23.723  1.00 31.14 ? 3    LYS I CG  1 
ATOM   7817  C  CD  . LYS H  1 3   ? 45.122 -30.967 -24.653  1.00 33.57 ? 3    LYS I CD  1 
ATOM   7818  C  CE  . LYS H  1 3   ? 44.653 -32.008 -25.666  1.00 34.65 ? 3    LYS I CE  1 
ATOM   7819  N  NZ  . LYS H  1 3   ? 45.625 -32.229 -26.771  1.00 36.81 ? 3    LYS I NZ  1 
ATOM   7820  N  N   . ALA H  1 4   ? 44.106 -27.786 -20.182  1.00 29.37 ? 4    ALA I N   1 
ATOM   7821  C  CA  . ALA H  1 4   ? 44.673 -26.741 -19.338  1.00 29.46 ? 4    ALA I CA  1 
ATOM   7822  C  C   . ALA H  1 4   ? 45.978 -27.202 -18.693  1.00 29.62 ? 4    ALA I C   1 
ATOM   7823  O  O   . ALA H  1 4   ? 46.301 -28.390 -18.712  1.00 29.39 ? 4    ALA I O   1 
ATOM   7824  C  CB  . ALA H  1 4   ? 43.662 -26.309 -18.272  1.00 29.15 ? 4    ALA I CB  1 
ATOM   7825  N  N   . VAL H  1 5   ? 46.725 -26.256 -18.126  1.00 29.83 ? 5    VAL I N   1 
ATOM   7826  C  CA  . VAL H  1 5   ? 47.993 -26.570 -17.465  1.00 30.07 ? 5    VAL I CA  1 
ATOM   7827  C  C   . VAL H  1 5   ? 48.248 -25.597 -16.294  1.00 30.39 ? 5    VAL I C   1 
ATOM   7828  O  O   . VAL H  1 5   ? 47.724 -24.474 -16.281  1.00 30.09 ? 5    VAL I O   1 
ATOM   7829  C  CB  . VAL H  1 5   ? 49.167 -26.584 -18.489  1.00 30.18 ? 5    VAL I CB  1 
ATOM   7830  C  CG1 . VAL H  1 5   ? 49.533 -25.167 -18.916  1.00 30.24 ? 5    VAL I CG1 1 
ATOM   7831  C  CG2 . VAL H  1 5   ? 50.392 -27.348 -17.939  1.00 30.65 ? 5    VAL I CG2 1 
ATOM   7832  N  N   . CYS H  1 6   ? 49.031 -26.051 -15.315  1.00 30.16 ? 6    CYS I N   1 
ATOM   7833  C  CA  . CYS H  1 6   ? 49.404 -25.245 -14.155  1.00 30.48 ? 6    CYS I CA  1 
ATOM   7834  C  C   . CYS H  1 6   ? 50.842 -25.565 -13.759  1.00 31.09 ? 6    CYS I C   1 
ATOM   7835  O  O   . CYS H  1 6   ? 51.190 -26.725 -13.538  1.00 30.43 ? 6    CYS I O   1 
ATOM   7836  C  CB  . CYS H  1 6   ? 48.447 -25.509 -12.984  1.00 30.06 ? 6    CYS I CB  1 
ATOM   7837  S  SG  . CYS H  1 6   ? 48.772 -24.530 -11.464  1.00 29.27 ? 6    CYS I SG  1 
ATOM   7838  N  N   . VAL H  1 7   ? 51.687 -24.538 -13.718  1.00 31.97 ? 7    VAL I N   1 
ATOM   7839  C  CA  . VAL H  1 7   ? 53.029 -24.682 -13.171  1.00 32.85 ? 7    VAL I CA  1 
ATOM   7840  C  C   . VAL H  1 7   ? 52.963 -24.263 -11.709  1.00 33.51 ? 7    VAL I C   1 
ATOM   7841  O  O   . VAL H  1 7   ? 52.637 -23.114 -11.386  1.00 33.18 ? 7    VAL I O   1 
ATOM   7842  C  CB  . VAL H  1 7   ? 54.086 -23.866 -13.945  1.00 32.90 ? 7    VAL I CB  1 
ATOM   7843  C  CG1 . VAL H  1 7   ? 55.472 -24.038 -13.302  1.00 33.92 ? 7    VAL I CG1 1 
ATOM   7844  C  CG2 . VAL H  1 7   ? 54.131 -24.306 -15.413  1.00 33.16 ? 7    VAL I CG2 1 
ATOM   7845  N  N   . LEU H  1 8   ? 53.235 -25.219 -10.829  1.00 34.20 ? 8    LEU I N   1 
ATOM   7846  C  CA  . LEU H  1 8   ? 53.160 -24.983 -9.401   1.00 35.29 ? 8    LEU I CA  1 
ATOM   7847  C  C   . LEU H  1 8   ? 54.532 -24.535 -8.918   1.00 36.15 ? 8    LEU I C   1 
ATOM   7848  O  O   . LEU H  1 8   ? 55.537 -25.199 -9.184   1.00 36.26 ? 8    LEU I O   1 
ATOM   7849  C  CB  . LEU H  1 8   ? 52.696 -26.247 -8.670   1.00 35.15 ? 8    LEU I CB  1 
ATOM   7850  C  CG  . LEU H  1 8   ? 51.315 -26.853 -8.976   1.00 34.74 ? 8    LEU I CG  1 
ATOM   7851  C  CD1 . LEU H  1 8   ? 51.216 -28.235 -8.355   1.00 33.99 ? 8    LEU I CD1 1 
ATOM   7852  C  CD2 . LEU H  1 8   ? 50.176 -25.970 -8.472   1.00 35.38 ? 8    LEU I CD2 1 
ATOM   7853  N  N   . LYS H  1 9   ? 54.568 -23.392 -8.238   1.00 37.03 ? 9    LYS I N   1 
ATOM   7854  C  CA  . LYS H  1 9   ? 55.819 -22.811 -7.769   1.00 38.29 ? 9    LYS I CA  1 
ATOM   7855  C  C   . LYS H  1 9   ? 55.648 -22.231 -6.382   1.00 39.00 ? 9    LYS I C   1 
ATOM   7856  O  O   . LYS H  1 9   ? 54.577 -21.720 -6.040   1.00 39.07 ? 9    LYS I O   1 
ATOM   7857  C  CB  . LYS H  1 9   ? 56.318 -21.724 -8.728   1.00 38.23 ? 9    LYS I CB  1 
ATOM   7858  C  CG  . LYS H  1 9   ? 56.846 -22.257 -10.055  1.00 39.58 ? 9    LYS I CG  1 
ATOM   7859  C  CD  . LYS H  1 9   ? 58.003 -21.411 -10.589  1.00 41.70 ? 9    LYS I CD  1 
ATOM   7860  C  CE  . LYS H  1 9   ? 58.610 -22.027 -11.845  1.00 42.33 ? 9    LYS I CE  1 
ATOM   7861  N  NZ  . LYS H  1 9   ? 58.972 -23.462 -11.643  1.00 42.29 ? 9    LYS I NZ  1 
ATOM   7862  N  N   . GLY H  1 10  ? 56.713 -22.317 -5.590   1.00 39.86 ? 10   GLY I N   1 
ATOM   7863  C  CA  . GLY H  1 10  ? 56.708 -21.812 -4.225   1.00 40.97 ? 10   GLY I CA  1 
ATOM   7864  C  C   . GLY H  1 10  ? 58.077 -21.367 -3.748   1.00 41.73 ? 10   GLY I C   1 
ATOM   7865  O  O   . GLY H  1 10  ? 59.059 -21.430 -4.497   1.00 41.83 ? 10   GLY I O   1 
ATOM   7866  N  N   . ASP H  1 11  ? 58.133 -20.922 -2.492   1.00 42.56 ? 11   ASP I N   1 
ATOM   7867  C  CA  . ASP H  1 11  ? 59.355 -20.376 -1.893   1.00 43.43 ? 11   ASP I CA  1 
ATOM   7868  C  C   . ASP H  1 11  ? 60.399 -21.470 -1.681   1.00 43.60 ? 11   ASP I C   1 
ATOM   7869  O  O   . ASP H  1 11  ? 61.598 -21.237 -1.860   1.00 43.83 ? 11   ASP I O   1 
ATOM   7870  C  CB  . ASP H  1 11  ? 59.069 -19.687 -0.544   1.00 43.72 ? 11   ASP I CB  1 
ATOM   7871  C  CG  . ASP H  1 11  ? 57.799 -18.825 -0.553   1.00 44.91 ? 11   ASP I CG  1 
ATOM   7872  O  OD1 . ASP H  1 11  ? 57.337 -18.466 0.557    1.00 46.44 ? 11   ASP I OD1 1 
ATOM   7873  O  OD2 . ASP H  1 11  ? 57.262 -18.501 -1.637   1.00 45.57 ? 11   ASP I OD2 1 
ATOM   7874  N  N   . GLY H  1 12  ? 59.931 -22.657 -1.296   1.00 43.58 ? 12   GLY I N   1 
ATOM   7875  C  CA  . GLY H  1 12  ? 60.811 -23.787 -1.007   1.00 43.53 ? 12   GLY I CA  1 
ATOM   7876  C  C   . GLY H  1 12  ? 61.044 -24.727 -2.179   1.00 43.40 ? 12   GLY I C   1 
ATOM   7877  O  O   . GLY H  1 12  ? 61.048 -24.295 -3.335   1.00 43.39 ? 12   GLY I O   1 
ATOM   7878  N  N   . PRO H  1 13  ? 61.240 -26.028 -1.884   1.00 43.25 ? 13   PRO I N   1 
ATOM   7879  C  CA  . PRO H  1 13  ? 61.517 -27.047 -2.906   1.00 43.04 ? 13   PRO I CA  1 
ATOM   7880  C  C   . PRO H  1 13  ? 60.261 -27.696 -3.508   1.00 42.72 ? 13   PRO I C   1 
ATOM   7881  O  O   . PRO H  1 13  ? 60.373 -28.525 -4.421   1.00 42.62 ? 13   PRO I O   1 
ATOM   7882  C  CB  . PRO H  1 13  ? 62.344 -28.090 -2.140   1.00 43.06 ? 13   PRO I CB  1 
ATOM   7883  C  CG  . PRO H  1 13  ? 62.134 -27.790 -0.652   1.00 43.16 ? 13   PRO I CG  1 
ATOM   7884  C  CD  . PRO H  1 13  ? 61.227 -26.603 -0.527   1.00 43.20 ? 13   PRO I CD  1 
ATOM   7885  N  N   . VAL H  1 14  ? 59.090 -27.319 -2.991   1.00 42.23 ? 14   VAL I N   1 
ATOM   7886  C  CA  . VAL H  1 14  ? 57.802 -27.840 -3.452   1.00 41.77 ? 14   VAL I CA  1 
ATOM   7887  C  C   . VAL H  1 14  ? 57.453 -27.255 -4.832   1.00 41.38 ? 14   VAL I C   1 
ATOM   7888  O  O   . VAL H  1 14  ? 57.221 -26.046 -4.965   1.00 41.36 ? 14   VAL I O   1 
ATOM   7889  C  CB  . VAL H  1 14  ? 56.674 -27.563 -2.412   1.00 41.74 ? 14   VAL I CB  1 
ATOM   7890  C  CG1 . VAL H  1 14  ? 55.344 -28.152 -2.868   1.00 42.11 ? 14   VAL I CG1 1 
ATOM   7891  C  CG2 . VAL H  1 14  ? 57.050 -28.135 -1.054   1.00 42.04 ? 14   VAL I CG2 1 
ATOM   7892  N  N   . GLN H  1 15  ? 57.430 -28.118 -5.850   1.00 40.91 ? 15   GLN I N   1 
ATOM   7893  C  CA  . GLN H  1 15  ? 57.202 -27.692 -7.242   1.00 40.55 ? 15   GLN I CA  1 
ATOM   7894  C  C   . GLN H  1 15  ? 56.730 -28.839 -8.148   1.00 40.16 ? 15   GLN I C   1 
ATOM   7895  O  O   . GLN H  1 15  ? 56.860 -30.009 -7.792   1.00 40.11 ? 15   GLN I O   1 
ATOM   7896  C  CB  . GLN H  1 15  ? 58.482 -27.089 -7.815   1.00 40.58 ? 15   GLN I CB  1 
ATOM   7897  C  CG  . GLN H  1 15  ? 59.541 -28.120 -8.156   1.00 41.20 ? 15   GLN I CG  1 
ATOM   7898  C  CD  . GLN H  1 15  ? 60.930 -27.536 -8.238   1.00 42.02 ? 15   GLN I CD  1 
ATOM   7899  O  OE1 . GLN H  1 15  ? 61.917 -28.269 -8.184   1.00 42.90 ? 15   GLN I OE1 1 
ATOM   7900  N  NE2 . GLN H  1 15  ? 61.023 -26.212 -8.363   1.00 42.28 ? 15   GLN I NE2 1 
ATOM   7901  N  N   . GLY H  1 16  ? 56.201 -28.494 -9.323   1.00 39.59 ? 16   GLY I N   1 
ATOM   7902  C  CA  . GLY H  1 16  ? 55.750 -29.493 -10.299  1.00 38.81 ? 16   GLY I CA  1 
ATOM   7903  C  C   . GLY H  1 16  ? 54.746 -28.986 -11.323  1.00 38.22 ? 16   GLY I C   1 
ATOM   7904  O  O   . GLY H  1 16  ? 54.385 -27.806 -11.330  1.00 38.38 ? 16   GLY I O   1 
ATOM   7905  N  N   . ILE H  1 17  ? 54.289 -29.892 -12.185  1.00 37.61 ? 17   ILE I N   1 
ATOM   7906  C  CA  . ILE H  1 17  ? 53.401 -29.553 -13.304  1.00 36.73 ? 17   ILE I CA  1 
ATOM   7907  C  C   . ILE H  1 17  ? 52.135 -30.433 -13.313  1.00 36.03 ? 17   ILE I C   1 
ATOM   7908  O  O   . ILE H  1 17  ? 52.226 -31.660 -13.404  1.00 35.72 ? 17   ILE I O   1 
ATOM   7909  C  CB  . ILE H  1 17  ? 54.147 -29.684 -14.669  1.00 36.84 ? 17   ILE I CB  1 
ATOM   7910  C  CG1 . ILE H  1 17  ? 55.357 -28.737 -14.724  1.00 36.84 ? 17   ILE I CG1 1 
ATOM   7911  C  CG2 . ILE H  1 17  ? 53.194 -29.434 -15.833  1.00 36.95 ? 17   ILE I CG2 1 
ATOM   7912  C  CD1 . ILE H  1 17  ? 56.367 -29.066 -15.820  1.00 36.92 ? 17   ILE I CD1 1 
ATOM   7913  N  N   . ILE H  1 18  ? 50.969 -29.791 -13.219  1.00 35.06 ? 18   ILE I N   1 
ATOM   7914  C  CA  . ILE H  1 18  ? 49.668 -30.470 -13.258  1.00 34.04 ? 18   ILE I CA  1 
ATOM   7915  C  C   . ILE H  1 18  ? 48.904 -30.163 -14.562  1.00 33.60 ? 18   ILE I C   1 
ATOM   7916  O  O   . ILE H  1 18  ? 48.745 -28.997 -14.936  1.00 33.49 ? 18   ILE I O   1 
ATOM   7917  C  CB  . ILE H  1 18  ? 48.789 -30.073 -12.029  1.00 34.12 ? 18   ILE I CB  1 
ATOM   7918  C  CG1 . ILE H  1 18  ? 49.471 -30.449 -10.699  1.00 33.71 ? 18   ILE I CG1 1 
ATOM   7919  C  CG2 . ILE H  1 18  ? 47.376 -30.660 -12.140  1.00 33.91 ? 18   ILE I CG2 1 
ATOM   7920  C  CD1 . ILE H  1 18  ? 49.765 -31.956 -10.493  1.00 33.99 ? 18   ILE I CD1 1 
ATOM   7921  N  N   . ASN H  1 19  ? 48.442 -31.211 -15.241  1.00 32.64 ? 19   ASN I N   1 
ATOM   7922  C  CA  . ASN H  1 19  ? 47.689 -31.074 -16.493  1.00 31.92 ? 19   ASN I CA  1 
ATOM   7923  C  C   . ASN H  1 19  ? 46.197 -31.305 -16.287  1.00 31.11 ? 19   ASN I C   1 
ATOM   7924  O  O   . ASN H  1 19  ? 45.792 -31.980 -15.350  1.00 30.90 ? 19   ASN I O   1 
ATOM   7925  C  CB  . ASN H  1 19  ? 48.222 -32.042 -17.554  1.00 31.84 ? 19   ASN I CB  1 
ATOM   7926  C  CG  . ASN H  1 19  ? 49.714 -31.892 -17.781  1.00 32.90 ? 19   ASN I CG  1 
ATOM   7927  O  OD1 . ASN H  1 19  ? 50.178 -30.854 -18.242  1.00 33.90 ? 19   ASN I OD1 1 
ATOM   7928  N  ND2 . ASN H  1 19  ? 50.475 -32.932 -17.453  1.00 32.95 ? 19   ASN I ND2 1 
ATOM   7929  N  N   . PHE H  1 20  ? 45.389 -30.727 -17.169  1.00 30.59 ? 20   PHE I N   1 
ATOM   7930  C  CA  . PHE H  1 20  ? 43.941 -30.885 -17.144  1.00 29.94 ? 20   PHE I CA  1 
ATOM   7931  C  C   . PHE H  1 20  ? 43.441 -31.204 -18.554  1.00 29.92 ? 20   PHE I C   1 
ATOM   7932  O  O   . PHE H  1 20  ? 43.865 -30.571 -19.529  1.00 29.52 ? 20   PHE I O   1 
ATOM   7933  C  CB  . PHE H  1 20  ? 43.260 -29.601 -16.663  1.00 29.94 ? 20   PHE I CB  1 
ATOM   7934  C  CG  . PHE H  1 20  ? 43.675 -29.152 -15.284  1.00 29.19 ? 20   PHE I CG  1 
ATOM   7935  C  CD1 . PHE H  1 20  ? 42.844 -29.371 -14.193  1.00 29.66 ? 20   PHE I CD1 1 
ATOM   7936  C  CD2 . PHE H  1 20  ? 44.876 -28.475 -15.085  1.00 28.09 ? 20   PHE I CD2 1 
ATOM   7937  C  CE1 . PHE H  1 20  ? 43.212 -28.942 -12.920  1.00 29.38 ? 20   PHE I CE1 1 
ATOM   7938  C  CE2 . PHE H  1 20  ? 45.250 -28.038 -13.820  1.00 27.99 ? 20   PHE I CE2 1 
ATOM   7939  C  CZ  . PHE H  1 20  ? 44.421 -28.272 -12.737  1.00 28.79 ? 20   PHE I CZ  1 
ATOM   7940  N  N   . GLU H  1 21  ? 42.529 -32.172 -18.658  1.00 29.56 ? 21   GLU I N   1 
ATOM   7941  C  CA  . GLU H  1 21  ? 41.942 -32.537 -19.951  1.00 29.77 ? 21   GLU I CA  1 
ATOM   7942  C  C   . GLU H  1 21  ? 40.446 -32.864 -19.825  1.00 29.35 ? 21   GLU I C   1 
ATOM   7943  O  O   . GLU H  1 21  ? 40.022 -33.520 -18.870  1.00 29.05 ? 21   GLU I O   1 
ATOM   7944  C  CB  . GLU H  1 21  ? 42.710 -33.706 -20.578  1.00 30.08 ? 21   GLU I CB  1 
ATOM   7945  C  CG  . GLU H  1 21  ? 42.429 -33.932 -22.058  1.00 31.92 ? 21   GLU I CG  1 
ATOM   7946  C  CD  . GLU H  1 21  ? 43.619 -34.544 -22.796  1.00 34.76 ? 21   GLU I CD  1 
ATOM   7947  O  OE1 . GLU H  1 21  ? 43.486 -34.837 -24.005  1.00 36.61 ? 21   GLU I OE1 1 
ATOM   7948  O  OE2 . GLU H  1 21  ? 44.693 -34.714 -22.179  1.00 35.70 ? 21   GLU I OE2 1 
ATOM   7949  N  N   . GLN H  1 22  ? 39.657 -32.397 -20.790  1.00 28.34 ? 22   GLN I N   1 
ATOM   7950  C  CA  . GLN H  1 22  ? 38.213 -32.556 -20.737  1.00 27.88 ? 22   GLN I CA  1 
ATOM   7951  C  C   . GLN H  1 22  ? 37.672 -32.784 -22.159  1.00 27.83 ? 22   GLN I C   1 
ATOM   7952  O  O   . GLN H  1 22  ? 37.663 -31.871 -22.996  1.00 27.89 ? 22   GLN I O   1 
ATOM   7953  C  CB  . GLN H  1 22  ? 37.562 -31.346 -20.045  1.00 27.47 ? 22   GLN I CB  1 
ATOM   7954  C  CG  . GLN H  1 22  ? 36.135 -31.572 -19.583  1.00 27.02 ? 22   GLN I CG  1 
ATOM   7955  C  CD  . GLN H  1 22  ? 35.461 -30.329 -18.996  1.00 27.06 ? 22   GLN I CD  1 
ATOM   7956  O  OE1 . GLN H  1 22  ? 35.967 -29.210 -19.098  1.00 26.47 ? 22   GLN I OE1 1 
ATOM   7957  N  NE2 . GLN H  1 22  ? 34.298 -30.530 -18.380  1.00 25.43 ? 22   GLN I NE2 1 
ATOM   7958  N  N   . LYS H  1 23  ? 37.224 -34.012 -22.417  1.00 27.96 ? 23   LYS I N   1 
ATOM   7959  C  CA  . LYS H  1 23  ? 36.835 -34.447 -23.762  1.00 27.64 ? 23   LYS I CA  1 
ATOM   7960  C  C   . LYS H  1 23  ? 35.585 -33.721 -24.240  1.00 27.02 ? 23   LYS I C   1 
ATOM   7961  O  O   . LYS H  1 23  ? 35.481 -33.388 -25.421  1.00 26.51 ? 23   LYS I O   1 
ATOM   7962  C  CB  . LYS H  1 23  ? 36.590 -35.961 -23.810  1.00 28.32 ? 23   LYS I CB  1 
ATOM   7963  C  CG  . LYS H  1 23  ? 37.563 -36.823 -23.005  1.00 30.59 ? 23   LYS I CG  1 
ATOM   7964  C  CD  . LYS H  1 23  ? 37.051 -38.272 -22.918  1.00 34.02 ? 23   LYS I CD  1 
ATOM   7965  C  CE  . LYS H  1 23  ? 37.612 -39.030 -21.704  1.00 35.96 ? 23   LYS I CE  1 
ATOM   7966  N  NZ  . LYS H  1 23  ? 38.944 -39.651 -21.962  1.00 37.38 ? 23   LYS I NZ  1 
ATOM   7967  N  N   . GLU H  1 24  ? 34.651 -33.482 -23.315  1.00 26.20 ? 24   GLU I N   1 
ATOM   7968  C  CA  . GLU H  1 24  ? 33.387 -32.793 -23.603  1.00 26.05 ? 24   GLU I CA  1 
ATOM   7969  C  C   . GLU H  1 24  ? 33.040 -31.831 -22.484  1.00 25.15 ? 24   GLU I C   1 
ATOM   7970  O  O   . GLU H  1 24  ? 33.373 -32.082 -21.324  1.00 24.50 ? 24   GLU I O   1 
ATOM   7971  C  CB  . GLU H  1 24  ? 32.219 -33.780 -23.764  1.00 26.44 ? 24   GLU I CB  1 
ATOM   7972  C  CG  . GLU H  1 24  ? 31.917 -34.182 -25.204  1.00 29.12 ? 24   GLU I CG  1 
ATOM   7973  C  CD  . GLU H  1 24  ? 32.781 -35.334 -25.661  1.00 32.36 ? 24   GLU I CD  1 
ATOM   7974  O  OE1 . GLU H  1 24  ? 33.184 -35.351 -26.846  1.00 32.46 ? 24   GLU I OE1 1 
ATOM   7975  O  OE2 . GLU H  1 24  ? 33.064 -36.224 -24.821  1.00 34.22 ? 24   GLU I OE2 1 
ATOM   7976  N  N   . SER H  1 25  ? 32.344 -30.745 -22.833  1.00 24.34 ? 25   SER I N   1 
ATOM   7977  C  CA  . SER H  1 25  ? 31.972 -29.718 -21.847  1.00 23.66 ? 25   SER I CA  1 
ATOM   7978  C  C   . SER H  1 25  ? 31.131 -30.255 -20.677  1.00 23.66 ? 25   SER I C   1 
ATOM   7979  O  O   . SER H  1 25  ? 31.209 -29.754 -19.550  1.00 23.35 ? 25   SER I O   1 
ATOM   7980  C  CB  . SER H  1 25  ? 31.250 -28.556 -22.532  1.00 23.48 ? 25   SER I CB  1 
ATOM   7981  O  OG  . SER H  1 25  ? 30.100 -29.003 -23.210  1.00 21.73 ? 25   SER I OG  1 
ATOM   7982  N  N   . ASN H  1 26  ? 30.318 -31.268 -20.949  1.00 23.76 ? 26   ASN I N   1 
ATOM   7983  C  CA  . ASN H  1 26  ? 29.571 -31.932 -19.884  1.00 23.63 ? 26   ASN I CA  1 
ATOM   7984  C  C   . ASN H  1 26  ? 30.237 -33.242 -19.444  1.00 24.22 ? 26   ASN I C   1 
ATOM   7985  O  O   . ASN H  1 26  ? 29.609 -34.071 -18.781  1.00 24.71 ? 26   ASN I O   1 
ATOM   7986  C  CB  . ASN H  1 26  ? 28.103 -32.141 -20.287  1.00 23.27 ? 26   ASN I CB  1 
ATOM   7987  C  CG  . ASN H  1 26  ? 27.950 -33.084 -21.469  1.00 21.89 ? 26   ASN I CG  1 
ATOM   7988  O  OD1 . ASN H  1 26  ? 28.836 -33.182 -22.307  1.00 21.23 ? 26   ASN I OD1 1 
ATOM   7989  N  ND2 . ASN H  1 26  ? 26.824 -33.776 -21.538  1.00 21.51 ? 26   ASN I ND2 1 
ATOM   7990  N  N   . GLY H  1 27  ? 31.506 -33.424 -19.804  1.00 24.75 ? 27   GLY I N   1 
ATOM   7991  C  CA  . GLY H  1 27  ? 32.262 -34.609 -19.386  1.00 25.36 ? 27   GLY I CA  1 
ATOM   7992  C  C   . GLY H  1 27  ? 33.117 -34.355 -18.152  1.00 26.70 ? 27   GLY I C   1 
ATOM   7993  O  O   . GLY H  1 27  ? 33.273 -33.200 -17.720  1.00 25.95 ? 27   GLY I O   1 
ATOM   7994  N  N   . PRO H  1 28  ? 33.691 -35.433 -17.573  1.00 27.17 ? 28   PRO I N   1 
ATOM   7995  C  CA  . PRO H  1 28  ? 34.619 -35.256 -16.457  1.00 27.69 ? 28   PRO I CA  1 
ATOM   7996  C  C   . PRO H  1 28  ? 35.977 -34.696 -16.915  1.00 28.04 ? 28   PRO I C   1 
ATOM   7997  O  O   . PRO H  1 28  ? 36.299 -34.734 -18.114  1.00 27.83 ? 28   PRO I O   1 
ATOM   7998  C  CB  . PRO H  1 28  ? 34.775 -36.679 -15.903  1.00 27.82 ? 28   PRO I CB  1 
ATOM   7999  C  CG  . PRO H  1 28  ? 34.510 -37.564 -17.086  1.00 27.79 ? 28   PRO I CG  1 
ATOM   8000  C  CD  . PRO H  1 28  ? 33.434 -36.861 -17.853  1.00 27.52 ? 28   PRO I CD  1 
ATOM   8001  N  N   . VAL H  1 29  ? 36.741 -34.164 -15.963  1.00 27.84 ? 29   VAL I N   1 
ATOM   8002  C  CA  . VAL H  1 29  ? 38.096 -33.679 -16.225  1.00 28.99 ? 29   VAL I CA  1 
ATOM   8003  C  C   . VAL H  1 29  ? 39.115 -34.674 -15.670  1.00 29.39 ? 29   VAL I C   1 
ATOM   8004  O  O   . VAL H  1 29  ? 39.032 -35.045 -14.491  1.00 29.38 ? 29   VAL I O   1 
ATOM   8005  C  CB  . VAL H  1 29  ? 38.357 -32.289 -15.560  1.00 28.40 ? 29   VAL I CB  1 
ATOM   8006  C  CG1 . VAL H  1 29  ? 39.723 -31.739 -15.973  1.00 29.26 ? 29   VAL I CG1 1 
ATOM   8007  C  CG2 . VAL H  1 29  ? 37.266 -31.293 -15.913  1.00 28.82 ? 29   VAL I CG2 1 
ATOM   8008  N  N   . LYS H  1 30  ? 40.066 -35.112 -16.495  1.00 30.03 ? 30   LYS I N   1 
ATOM   8009  C  CA  . LYS H  1 30  ? 41.232 -35.797 -15.931  1.00 30.92 ? 30   LYS I CA  1 
ATOM   8010  C  C   . LYS H  1 30  ? 42.320 -34.800 -15.543  1.00 31.34 ? 30   LYS I C   1 
ATOM   8011  O  O   . LYS H  1 30  ? 42.623 -33.868 -16.288  1.00 30.83 ? 30   LYS I O   1 
ATOM   8012  C  CB  . LYS H  1 30  ? 41.762 -36.947 -16.805  1.00 31.07 ? 30   LYS I CB  1 
ATOM   8013  C  CG  . LYS H  1 30  ? 42.648 -36.586 -17.984  1.00 32.60 ? 30   LYS I CG  1 
ATOM   8014  C  CD  . LYS H  1 30  ? 43.591 -37.758 -18.294  1.00 34.63 ? 30   LYS I CD  1 
ATOM   8015  C  CE  . LYS H  1 30  ? 44.144 -37.702 -19.716  1.00 36.26 ? 30   LYS I CE  1 
ATOM   8016  N  NZ  . LYS H  1 30  ? 45.281 -38.653 -19.912  1.00 36.85 ? 30   LYS I NZ  1 
ATOM   8017  N  N   . VAL H  1 31  ? 42.866 -35.010 -14.353  1.00 31.61 ? 31   VAL I N   1 
ATOM   8018  C  CA  . VAL H  1 31  ? 43.883 -34.166 -13.756  1.00 32.49 ? 31   VAL I CA  1 
ATOM   8019  C  C   . VAL H  1 31  ? 45.092 -35.067 -13.488  1.00 33.31 ? 31   VAL I C   1 
ATOM   8020  O  O   . VAL H  1 31  ? 45.002 -36.001 -12.673  1.00 33.09 ? 31   VAL I O   1 
ATOM   8021  C  CB  . VAL H  1 31  ? 43.356 -33.584 -12.417  1.00 32.46 ? 31   VAL I CB  1 
ATOM   8022  C  CG1 . VAL H  1 31  ? 44.388 -32.680 -11.747  1.00 33.00 ? 31   VAL I CG1 1 
ATOM   8023  C  CG2 . VAL H  1 31  ? 42.012 -32.861 -12.616  1.00 32.55 ? 31   VAL I CG2 1 
ATOM   8024  N  N   . TRP H  1 32  ? 46.209 -34.823 -14.176  1.00 33.82 ? 32   TRP I N   1 
ATOM   8025  C  CA  . TRP H  1 32  ? 47.404 -35.654 -13.958  1.00 34.80 ? 32   TRP I CA  1 
ATOM   8026  C  C   . TRP H  1 32  ? 48.724 -34.896 -14.046  1.00 35.52 ? 32   TRP I C   1 
ATOM   8027  O  O   . TRP H  1 32  ? 48.811 -33.854 -14.698  1.00 35.57 ? 32   TRP I O   1 
ATOM   8028  C  CB  . TRP H  1 32  ? 47.420 -36.868 -14.897  1.00 35.00 ? 32   TRP I CB  1 
ATOM   8029  C  CG  . TRP H  1 32  ? 47.974 -36.575 -16.253  1.00 34.64 ? 32   TRP I CG  1 
ATOM   8030  C  CD1 . TRP H  1 32  ? 49.216 -36.896 -16.723  1.00 34.56 ? 32   TRP I CD1 1 
ATOM   8031  C  CD2 . TRP H  1 32  ? 47.304 -35.895 -17.315  1.00 36.00 ? 32   TRP I CD2 1 
ATOM   8032  N  NE1 . TRP H  1 32  ? 49.360 -36.460 -18.019  1.00 35.59 ? 32   TRP I NE1 1 
ATOM   8033  C  CE2 . TRP H  1 32  ? 48.201 -35.839 -18.407  1.00 35.92 ? 32   TRP I CE2 1 
ATOM   8034  C  CE3 . TRP H  1 32  ? 46.029 -35.327 -17.455  1.00 35.75 ? 32   TRP I CE3 1 
ATOM   8035  C  CZ2 . TRP H  1 32  ? 47.864 -35.239 -19.622  1.00 36.27 ? 32   TRP I CZ2 1 
ATOM   8036  C  CZ3 . TRP H  1 32  ? 45.696 -34.730 -18.664  1.00 36.34 ? 32   TRP I CZ3 1 
ATOM   8037  C  CH2 . TRP H  1 32  ? 46.611 -34.689 -19.729  1.00 36.80 ? 32   TRP I CH2 1 
ATOM   8038  N  N   . GLY H  1 33  ? 49.748 -35.441 -13.385  1.00 36.24 ? 33   GLY I N   1 
ATOM   8039  C  CA  . GLY H  1 33  ? 51.072 -34.820 -13.312  1.00 37.03 ? 33   GLY I CA  1 
ATOM   8040  C  C   . GLY H  1 33  ? 51.863 -35.306 -12.104  1.00 37.64 ? 33   GLY I C   1 
ATOM   8041  O  O   . GLY H  1 33  ? 51.605 -36.394 -11.583  1.00 37.57 ? 33   GLY I O   1 
ATOM   8042  N  N   . SER H  1 34  ? 52.827 -34.496 -11.664  1.00 38.17 ? 34   SER I N   1 
ATOM   8043  C  CA  . SER H  1 34  ? 53.673 -34.826 -10.508  1.00 38.64 ? 34   SER I CA  1 
ATOM   8044  C  C   . SER H  1 34  ? 54.153 -33.578 -9.760   1.00 38.91 ? 34   SER I C   1 
ATOM   8045  O  O   . SER H  1 34  ? 54.437 -32.543 -10.375  1.00 39.33 ? 34   SER I O   1 
ATOM   8046  C  CB  . SER H  1 34  ? 54.883 -35.660 -10.938  1.00 38.68 ? 34   SER I CB  1 
ATOM   8047  O  OG  . SER H  1 34  ? 55.895 -34.828 -11.473  1.00 38.38 ? 34   SER I OG  1 
ATOM   8048  N  N   . ILE H  1 35  ? 54.232 -33.687 -8.436   1.00 38.90 ? 35   ILE I N   1 
ATOM   8049  C  CA  . ILE H  1 35  ? 54.770 -32.631 -7.581   1.00 39.01 ? 35   ILE I CA  1 
ATOM   8050  C  C   . ILE H  1 35  ? 55.966 -33.191 -6.797   1.00 39.15 ? 35   ILE I C   1 
ATOM   8051  O  O   . ILE H  1 35  ? 55.913 -34.313 -6.297   1.00 39.36 ? 35   ILE I O   1 
ATOM   8052  C  CB  . ILE H  1 35  ? 53.687 -32.068 -6.620   1.00 39.04 ? 35   ILE I CB  1 
ATOM   8053  C  CG1 . ILE H  1 35  ? 52.380 -31.787 -7.383   1.00 38.86 ? 35   ILE I CG1 1 
ATOM   8054  C  CG2 . ILE H  1 35  ? 54.182 -30.809 -5.910   1.00 38.87 ? 35   ILE I CG2 1 
ATOM   8055  C  CD1 . ILE H  1 35  ? 51.139 -31.656 -6.503   1.00 38.92 ? 35   ILE I CD1 1 
ATOM   8056  N  N   . LYS H  1 36  ? 57.042 -32.412 -6.708   1.00 39.21 ? 36   LYS I N   1 
ATOM   8057  C  CA  . LYS H  1 36  ? 58.272 -32.849 -6.037   1.00 39.23 ? 36   LYS I CA  1 
ATOM   8058  C  C   . LYS H  1 36  ? 58.596 -31.977 -4.824   1.00 39.14 ? 36   LYS I C   1 
ATOM   8059  O  O   . LYS H  1 36  ? 58.243 -30.795 -4.792   1.00 39.10 ? 36   LYS I O   1 
ATOM   8060  C  CB  . LYS H  1 36  ? 59.440 -32.859 -7.030   1.00 39.31 ? 36   LYS I CB  1 
ATOM   8061  C  CG  . LYS H  1 36  ? 59.220 -33.829 -8.190   1.00 39.82 ? 36   LYS I CG  1 
ATOM   8062  C  CD  . LYS H  1 36  ? 60.250 -33.685 -9.297   1.00 40.41 ? 36   LYS I CD  1 
ATOM   8063  C  CE  . LYS H  1 36  ? 60.072 -34.779 -10.356  1.00 40.84 ? 36   LYS I CE  1 
ATOM   8064  N  NZ  . LYS H  1 36  ? 58.658 -34.910 -10.840  1.00 39.89 ? 36   LYS I NZ  1 
ATOM   8065  N  N   . GLY H  1 37  ? 59.243 -32.571 -3.822   1.00 38.87 ? 37   GLY I N   1 
ATOM   8066  C  CA  . GLY H  1 37  ? 59.706 -31.832 -2.647   1.00 38.70 ? 37   GLY I CA  1 
ATOM   8067  C  C   . GLY H  1 37  ? 58.763 -31.776 -1.454   1.00 38.74 ? 37   GLY I C   1 
ATOM   8068  O  O   . GLY H  1 37  ? 58.950 -30.950 -0.552   1.00 38.63 ? 37   GLY I O   1 
ATOM   8069  N  N   . LEU H  1 38  ? 57.761 -32.655 -1.444   1.00 38.62 ? 38   LEU I N   1 
ATOM   8070  C  CA  . LEU H  1 38  ? 56.791 -32.741 -0.351   1.00 38.60 ? 38   LEU I CA  1 
ATOM   8071  C  C   . LEU H  1 38  ? 57.242 -33.732 0.731    1.00 38.88 ? 38   LEU I C   1 
ATOM   8072  O  O   . LEU H  1 38  ? 58.107 -34.576 0.487    1.00 38.87 ? 38   LEU I O   1 
ATOM   8073  C  CB  . LEU H  1 38  ? 55.425 -33.177 -0.892   1.00 38.54 ? 38   LEU I CB  1 
ATOM   8074  C  CG  . LEU H  1 38  ? 54.579 -32.249 -1.766   1.00 38.15 ? 38   LEU I CG  1 
ATOM   8075  C  CD1 . LEU H  1 38  ? 53.494 -33.056 -2.480   1.00 37.71 ? 38   LEU I CD1 1 
ATOM   8076  C  CD2 . LEU H  1 38  ? 53.956 -31.130 -0.938   1.00 37.77 ? 38   LEU I CD2 1 
ATOM   8077  N  N   . THR H  1 39  ? 56.650 -33.624 1.920    1.00 39.02 ? 39   THR I N   1 
ATOM   8078  C  CA  . THR H  1 39  ? 56.846 -34.614 2.983    1.00 39.41 ? 39   THR I CA  1 
ATOM   8079  C  C   . THR H  1 39  ? 56.030 -35.859 2.640    1.00 39.33 ? 39   THR I C   1 
ATOM   8080  O  O   . THR H  1 39  ? 54.980 -35.743 1.998    1.00 39.63 ? 39   THR I O   1 
ATOM   8081  C  CB  . THR H  1 39  ? 56.379 -34.083 4.362    1.00 39.55 ? 39   THR I CB  1 
ATOM   8082  O  OG1 . THR H  1 39  ? 54.987 -33.735 4.300    1.00 39.79 ? 39   THR I OG1 1 
ATOM   8083  C  CG2 . THR H  1 39  ? 57.195 -32.862 4.786    1.00 39.75 ? 39   THR I CG2 1 
ATOM   8084  N  N   . GLU H  1 40  ? 56.500 -37.036 3.059    1.00 38.96 ? 40   GLU I N   1 
ATOM   8085  C  CA  . GLU H  1 40  ? 55.785 -38.289 2.792    1.00 38.66 ? 40   GLU I CA  1 
ATOM   8086  C  C   . GLU H  1 40  ? 54.362 -38.200 3.346    1.00 38.37 ? 40   GLU I C   1 
ATOM   8087  O  O   . GLU H  1 40  ? 54.164 -37.782 4.488    1.00 38.67 ? 40   GLU I O   1 
ATOM   8088  C  CB  . GLU H  1 40  ? 56.525 -39.486 3.413    1.00 38.51 ? 40   GLU I CB  1 
ATOM   8089  C  CG  . GLU H  1 40  ? 56.257 -40.833 2.714    1.00 38.83 ? 40   GLU I CG  1 
ATOM   8090  C  CD  . GLU H  1 40  ? 57.042 -42.003 3.320    1.00 38.99 ? 40   GLU I CD  1 
ATOM   8091  O  OE1 . GLU H  1 40  ? 56.701 -42.444 4.439    1.00 38.81 ? 40   GLU I OE1 1 
ATOM   8092  O  OE2 . GLU H  1 40  ? 57.992 -42.494 2.669    1.00 38.24 ? 40   GLU I OE2 1 
ATOM   8093  N  N   . GLY H  1 41  ? 53.372 -38.561 2.535    1.00 37.90 ? 41   GLY I N   1 
ATOM   8094  C  CA  . GLY H  1 41  ? 51.990 -38.610 3.013    1.00 37.18 ? 41   GLY I CA  1 
ATOM   8095  C  C   . GLY H  1 41  ? 51.025 -37.633 2.369    1.00 36.75 ? 41   GLY I C   1 
ATOM   8096  O  O   . GLY H  1 41  ? 51.309 -37.066 1.308    1.00 36.72 ? 41   GLY I O   1 
ATOM   8097  N  N   . LEU H  1 42  ? 49.884 -37.435 3.033    1.00 36.08 ? 42   LEU I N   1 
ATOM   8098  C  CA  . LEU H  1 42  ? 48.752 -36.685 2.481    1.00 35.40 ? 42   LEU I CA  1 
ATOM   8099  C  C   . LEU H  1 42  ? 48.977 -35.176 2.482    1.00 34.85 ? 42   LEU I C   1 
ATOM   8100  O  O   . LEU H  1 42  ? 49.493 -34.605 3.448    1.00 34.33 ? 42   LEU I O   1 
ATOM   8101  C  CB  . LEU H  1 42  ? 47.458 -37.004 3.240    1.00 35.32 ? 42   LEU I CB  1 
ATOM   8102  C  CG  . LEU H  1 42  ? 46.955 -38.447 3.340    1.00 35.71 ? 42   LEU I CG  1 
ATOM   8103  C  CD1 . LEU H  1 42  ? 46.099 -38.627 4.595    1.00 35.66 ? 42   LEU I CD1 1 
ATOM   8104  C  CD2 . LEU H  1 42  ? 46.190 -38.875 2.093    1.00 35.36 ? 42   LEU I CD2 1 
ATOM   8105  N  N   . HIS H  1 43  ? 48.559 -34.538 1.391    1.00 34.36 ? 43   HIS I N   1 
ATOM   8106  C  CA  . HIS H  1 43  ? 48.703 -33.095 1.223    1.00 33.83 ? 43   HIS I CA  1 
ATOM   8107  C  C   . HIS H  1 43  ? 47.510 -32.514 0.480    1.00 33.21 ? 43   HIS I C   1 
ATOM   8108  O  O   . HIS H  1 43  ? 47.219 -32.912 -0.653   1.00 33.03 ? 43   HIS I O   1 
ATOM   8109  C  CB  . HIS H  1 43  ? 50.008 -32.760 0.489    1.00 34.20 ? 43   HIS I CB  1 
ATOM   8110  C  CG  . HIS H  1 43  ? 51.236 -32.904 1.339    1.00 34.89 ? 43   HIS I CG  1 
ATOM   8111  N  ND1 . HIS H  1 43  ? 51.535 -32.036 2.371    1.00 35.70 ? 43   HIS I ND1 1 
ATOM   8112  C  CD2 . HIS H  1 43  ? 52.243 -33.811 1.306    1.00 35.46 ? 43   HIS I CD2 1 
ATOM   8113  C  CE1 . HIS H  1 43  ? 52.673 -32.403 2.935    1.00 36.76 ? 43   HIS I CE1 1 
ATOM   8114  N  NE2 . HIS H  1 43  ? 53.122 -33.477 2.308    1.00 36.42 ? 43   HIS I NE2 1 
ATOM   8115  N  N   . GLY H  1 44  ? 46.820 -31.586 1.146    1.00 32.54 ? 44   GLY I N   1 
ATOM   8116  C  CA  . GLY H  1 44  ? 45.696 -30.843 0.570    1.00 31.87 ? 44   GLY I CA  1 
ATOM   8117  C  C   . GLY H  1 44  ? 45.956 -30.349 -0.842   1.00 31.04 ? 44   GLY I C   1 
ATOM   8118  O  O   . GLY H  1 44  ? 47.076 -29.987 -1.189   1.00 30.84 ? 44   GLY I O   1 
ATOM   8119  N  N   . PHE H  1 45  ? 44.908 -30.333 -1.654   1.00 30.78 ? 45   PHE I N   1 
ATOM   8120  C  CA  . PHE H  1 45  ? 45.049 -30.082 -3.084   1.00 30.46 ? 45   PHE I CA  1 
ATOM   8121  C  C   . PHE H  1 45  ? 43.722 -29.536 -3.611   1.00 30.40 ? 45   PHE I C   1 
ATOM   8122  O  O   . PHE H  1 45  ? 42.759 -30.297 -3.796   1.00 30.33 ? 45   PHE I O   1 
ATOM   8123  C  CB  . PHE H  1 45  ? 45.429 -31.398 -3.782   1.00 30.51 ? 45   PHE I CB  1 
ATOM   8124  C  CG  . PHE H  1 45  ? 45.848 -31.248 -5.217   1.00 29.95 ? 45   PHE I CG  1 
ATOM   8125  C  CD1 . PHE H  1 45  ? 47.068 -30.658 -5.545   1.00 28.73 ? 45   PHE I CD1 1 
ATOM   8126  C  CD2 . PHE H  1 45  ? 45.040 -31.744 -6.239   1.00 30.73 ? 45   PHE I CD2 1 
ATOM   8127  C  CE1 . PHE H  1 45  ? 47.464 -30.528 -6.874   1.00 28.57 ? 45   PHE I CE1 1 
ATOM   8128  C  CE2 . PHE H  1 45  ? 45.426 -31.628 -7.574   1.00 30.56 ? 45   PHE I CE2 1 
ATOM   8129  C  CZ  . PHE H  1 45  ? 46.643 -31.017 -7.893   1.00 30.20 ? 45   PHE I CZ  1 
ATOM   8130  N  N   . HIS H  1 46  ? 43.671 -28.218 -3.820   1.00 29.49 ? 46   HIS I N   1 
ATOM   8131  C  CA  . HIS H  1 46  ? 42.420 -27.529 -4.163   1.00 29.40 ? 46   HIS I CA  1 
ATOM   8132  C  C   . HIS H  1 46  ? 42.605 -26.387 -5.163   1.00 28.54 ? 46   HIS I C   1 
ATOM   8133  O  O   . HIS H  1 46  ? 43.710 -25.879 -5.359   1.00 28.32 ? 46   HIS I O   1 
ATOM   8134  C  CB  . HIS H  1 46  ? 41.721 -26.939 -2.918   1.00 29.73 ? 46   HIS I CB  1 
ATOM   8135  C  CG  . HIS H  1 46  ? 42.020 -27.648 -1.634   1.00 30.83 ? 46   HIS I CG  1 
ATOM   8136  N  ND1 . HIS H  1 46  ? 42.879 -27.129 -0.688   1.00 32.29 ? 46   HIS I ND1 1 
ATOM   8137  C  CD2 . HIS H  1 46  ? 41.552 -28.813 -1.121   1.00 31.38 ? 46   HIS I CD2 1 
ATOM   8138  C  CE1 . HIS H  1 46  ? 42.943 -27.953 0.343    1.00 32.20 ? 46   HIS I CE1 1 
ATOM   8139  N  NE2 . HIS H  1 46  ? 42.148 -28.982 0.105    1.00 31.89 ? 46   HIS I NE2 1 
ATOM   8140  N  N   . VAL H  1 47  ? 41.491 -25.970 -5.759   1.00 27.92 ? 47   VAL I N   1 
ATOM   8141  C  CA  . VAL H  1 47  ? 41.466 -24.787 -6.582   1.00 27.20 ? 47   VAL I CA  1 
ATOM   8142  C  C   . VAL H  1 47  ? 40.927 -23.658 -5.706   1.00 27.03 ? 47   VAL I C   1 
ATOM   8143  O  O   . VAL H  1 47  ? 39.830 -23.766 -5.138   1.00 26.64 ? 47   VAL I O   1 
ATOM   8144  C  CB  . VAL H  1 47  ? 40.584 -24.972 -7.854   1.00 27.41 ? 47   VAL I CB  1 
ATOM   8145  C  CG1 . VAL H  1 47  ? 40.656 -23.735 -8.740   1.00 26.69 ? 47   VAL I CG1 1 
ATOM   8146  C  CG2 . VAL H  1 47  ? 41.013 -26.211 -8.636   1.00 26.29 ? 47   VAL I CG2 1 
ATOM   8147  N  N   . HIS H  1 48  ? 41.721 -22.596 -5.582   1.00 26.87 ? 48   HIS I N   1 
ATOM   8148  C  CA  . HIS H  1 48  ? 41.319 -21.392 -4.846   1.00 26.99 ? 48   HIS I CA  1 
ATOM   8149  C  C   . HIS H  1 48  ? 40.731 -20.379 -5.829   1.00 26.31 ? 48   HIS I C   1 
ATOM   8150  O  O   . HIS H  1 48  ? 40.942 -20.523 -7.033   1.00 25.87 ? 48   HIS I O   1 
ATOM   8151  C  CB  . HIS H  1 48  ? 42.502 -20.817 -4.055   1.00 27.70 ? 48   HIS I CB  1 
ATOM   8152  C  CG  . HIS H  1 48  ? 42.985 -21.717 -2.954   1.00 28.90 ? 48   HIS I CG  1 
ATOM   8153  N  ND1 . HIS H  1 48  ? 42.992 -21.336 -1.628   1.00 30.71 ? 48   HIS I ND1 1 
ATOM   8154  C  CD2 . HIS H  1 48  ? 43.474 -22.983 -2.982   1.00 30.81 ? 48   HIS I CD2 1 
ATOM   8155  C  CE1 . HIS H  1 48  ? 43.465 -22.326 -0.889   1.00 31.30 ? 48   HIS I CE1 1 
ATOM   8156  N  NE2 . HIS H  1 48  ? 43.767 -23.336 -1.687   1.00 31.90 ? 48   HIS I NE2 1 
ATOM   8157  N  N   . GLU H  1 49  ? 39.974 -19.392 -5.337   1.00 25.49 ? 49   GLU I N   1 
ATOM   8158  C  CA  . GLU H  1 49  ? 39.153 -18.589 -6.248   1.00 25.95 ? 49   GLU I CA  1 
ATOM   8159  C  C   . GLU H  1 49  ? 39.905 -17.582 -7.116   1.00 25.91 ? 49   GLU I C   1 
ATOM   8160  O  O   . GLU H  1 49  ? 39.456 -17.279 -8.225   1.00 25.79 ? 49   GLU I O   1 
ATOM   8161  C  CB  . GLU H  1 49  ? 37.882 -17.987 -5.613   1.00 25.65 ? 49   GLU I CB  1 
ATOM   8162  C  CG  . GLU H  1 49  ? 38.048 -17.064 -4.444   1.00 27.66 ? 49   GLU I CG  1 
ATOM   8163  C  CD  . GLU H  1 49  ? 36.746 -16.329 -4.080   1.00 28.61 ? 49   GLU I CD  1 
ATOM   8164  O  OE1 . GLU H  1 49  ? 36.002 -15.893 -4.991   1.00 29.80 ? 49   GLU I OE1 1 
ATOM   8165  O  OE2 . GLU H  1 49  ? 36.476 -16.170 -2.874   1.00 29.23 ? 49   GLU I OE2 1 
ATOM   8166  N  N   . PHE H  1 50  ? 41.045 -17.083 -6.642   1.00 25.93 ? 50   PHE I N   1 
ATOM   8167  C  CA  . PHE H  1 50  ? 41.740 -16.040 -7.401   1.00 26.05 ? 50   PHE I CA  1 
ATOM   8168  C  C   . PHE H  1 50  ? 43.069 -16.488 -7.988   1.00 25.76 ? 50   PHE I C   1 
ATOM   8169  O  O   . PHE H  1 50  ? 43.927 -17.007 -7.280   1.00 25.34 ? 50   PHE I O   1 
ATOM   8170  C  CB  . PHE H  1 50  ? 41.899 -14.771 -6.572   1.00 26.10 ? 50   PHE I CB  1 
ATOM   8171  C  CG  . PHE H  1 50  ? 40.613 -14.284 -5.973   1.00 27.23 ? 50   PHE I CG  1 
ATOM   8172  C  CD1 . PHE H  1 50  ? 39.534 -13.959 -6.788   1.00 28.20 ? 50   PHE I CD1 1 
ATOM   8173  C  CD2 . PHE H  1 50  ? 40.478 -14.167 -4.594   1.00 28.86 ? 50   PHE I CD2 1 
ATOM   8174  C  CE1 . PHE H  1 50  ? 38.336 -13.514 -6.241   1.00 28.95 ? 50   PHE I CE1 1 
ATOM   8175  C  CE2 . PHE H  1 50  ? 39.286 -13.724 -4.027   1.00 29.77 ? 50   PHE I CE2 1 
ATOM   8176  C  CZ  . PHE H  1 50  ? 38.209 -13.399 -4.858   1.00 30.30 ? 50   PHE I CZ  1 
ATOM   8177  N  N   . GLY H  1 51  ? 43.229 -16.270 -9.292   1.00 25.59 ? 51   GLY I N   1 
ATOM   8178  C  CA  . GLY H  1 51  ? 44.498 -16.543 -9.973   1.00 25.30 ? 51   GLY I CA  1 
ATOM   8179  C  C   . GLY H  1 51  ? 45.446 -15.380 -9.754   1.00 25.56 ? 51   GLY I C   1 
ATOM   8180  O  O   . GLY H  1 51  ? 45.971 -14.798 -10.704  1.00 25.02 ? 51   GLY I O   1 
ATOM   8181  N  N   . ASP H  1 52  ? 45.657 -15.056 -8.482   1.00 25.48 ? 52   ASP I N   1 
ATOM   8182  C  CA  . ASP H  1 52  ? 46.396 -13.879 -8.071   1.00 25.36 ? 52   ASP I CA  1 
ATOM   8183  C  C   . ASP H  1 52  ? 47.623 -14.278 -7.242   1.00 25.80 ? 52   ASP I C   1 
ATOM   8184  O  O   . ASP H  1 52  ? 47.491 -14.698 -6.082   1.00 26.13 ? 52   ASP I O   1 
ATOM   8185  C  CB  . ASP H  1 52  ? 45.471 -12.938 -7.280   1.00 24.68 ? 52   ASP I CB  1 
ATOM   8186  C  CG  . ASP H  1 52  ? 46.180 -11.679 -6.792   1.00 23.87 ? 52   ASP I CG  1 
ATOM   8187  O  OD1 . ASP H  1 52  ? 45.491 -10.666 -6.497   1.00 22.48 ? 52   ASP I OD1 1 
ATOM   8188  O  OD2 . ASP H  1 52  ? 47.424 -11.709 -6.689   1.00 22.11 ? 52   ASP I OD2 1 
ATOM   8189  N  N   . ASN H  1 53  ? 48.804 -14.133 -7.845   1.00 26.24 ? 53   ASN I N   1 
ATOM   8190  C  CA  . ASN H  1 53  ? 50.087 -14.484 -7.226   1.00 27.23 ? 53   ASN I CA  1 
ATOM   8191  C  C   . ASN H  1 53  ? 50.962 -13.289 -6.826   1.00 27.12 ? 53   ASN I C   1 
ATOM   8192  O  O   . ASN H  1 53  ? 52.188 -13.431 -6.653   1.00 27.29 ? 53   ASN I O   1 
ATOM   8193  C  CB  . ASN H  1 53  ? 50.880 -15.419 -8.151   1.00 27.91 ? 53   ASN I CB  1 
ATOM   8194  C  CG  . ASN H  1 53  ? 50.813 -16.874 -7.715   1.00 30.78 ? 53   ASN I CG  1 
ATOM   8195  O  OD1 . ASN H  1 53  ? 51.621 -17.321 -6.884   1.00 31.75 ? 53   ASN I OD1 1 
ATOM   8196  N  ND2 . ASN H  1 53  ? 49.865 -17.632 -8.288   1.00 31.32 ? 53   ASN I ND2 1 
ATOM   8197  N  N   . THR H  1 54  ? 50.337 -12.117 -6.664   1.00 27.14 ? 54   THR I N   1 
ATOM   8198  C  CA  . THR H  1 54  ? 51.048 -10.889 -6.243   1.00 26.58 ? 54   THR I CA  1 
ATOM   8199  C  C   . THR H  1 54  ? 51.632 -10.959 -4.821   1.00 26.51 ? 54   THR I C   1 
ATOM   8200  O  O   . THR H  1 54  ? 52.679 -10.368 -4.549   1.00 26.11 ? 54   THR I O   1 
ATOM   8201  C  CB  . THR H  1 54  ? 50.148 -9.638  -6.343   1.00 26.86 ? 54   THR I CB  1 
ATOM   8202  O  OG1 . THR H  1 54  ? 49.014 -9.797  -5.483   1.00 27.39 ? 54   THR I OG1 1 
ATOM   8203  C  CG2 . THR H  1 54  ? 49.674 -9.408  -7.789   1.00 26.42 ? 54   THR I CG2 1 
ATOM   8204  N  N   . ALA H  1 55  ? 50.935 -11.653 -3.921   1.00 26.07 ? 55   ALA I N   1 
ATOM   8205  C  CA  . ALA H  1 55  ? 51.448 -11.949 -2.573   1.00 25.97 ? 55   ALA I CA  1 
ATOM   8206  C  C   . ALA H  1 55  ? 51.806 -13.435 -2.447   1.00 25.93 ? 55   ALA I C   1 
ATOM   8207  O  O   . ALA H  1 55  ? 51.575 -14.062 -1.402   1.00 25.98 ? 55   ALA I O   1 
ATOM   8208  C  CB  . ALA H  1 55  ? 50.424 -11.555 -1.518   1.00 25.55 ? 55   ALA I CB  1 
ATOM   8209  N  N   . GLY H  1 56  ? 52.364 -14.005 -3.515   1.00 26.06 ? 56   GLY I N   1 
ATOM   8210  C  CA  . GLY H  1 56  ? 52.585 -15.458 -3.573   1.00 25.86 ? 56   GLY I CA  1 
ATOM   8211  C  C   . GLY H  1 56  ? 51.264 -16.209 -3.488   1.00 25.85 ? 56   GLY I C   1 
ATOM   8212  O  O   . GLY H  1 56  ? 50.245 -15.729 -3.990   1.00 25.87 ? 56   GLY I O   1 
ATOM   8213  N  N   . CYS H  1 57  ? 51.270 -17.369 -2.828   1.00 25.32 ? 57   CYS I N   1 
ATOM   8214  C  CA  . CYS H  1 57  ? 50.064 -18.213 -2.721   1.00 25.28 ? 57   CYS I CA  1 
ATOM   8215  C  C   . CYS H  1 57  ? 48.944 -17.651 -1.816   1.00 25.68 ? 57   CYS I C   1 
ATOM   8216  O  O   . CYS H  1 57  ? 47.776 -18.063 -1.921   1.00 25.67 ? 57   CYS I O   1 
ATOM   8217  C  CB  . CYS H  1 57  ? 50.452 -19.638 -2.319   0.40 24.76 ? 57   CYS I CB  1 
ATOM   8218  S  SG  . CYS H  1 57  ? 51.550 -20.421 -3.515   0.40 22.00 ? 57   CYS I SG  1 
ATOM   8219  N  N   . THR H  1 58  ? 49.291 -16.685 -0.969   1.00 25.78 ? 58   THR I N   1 
ATOM   8220  C  CA  . THR H  1 58  ? 48.347 -16.083 -0.016   1.00 26.34 ? 58   THR I CA  1 
ATOM   8221  C  C   . THR H  1 58  ? 47.235 -15.285 -0.703   1.00 26.33 ? 58   THR I C   1 
ATOM   8222  O  O   . THR H  1 58  ? 46.086 -15.283 -0.234   1.00 26.52 ? 58   THR I O   1 
ATOM   8223  C  CB  . THR H  1 58  ? 49.069 -15.140 0.978    1.00 26.05 ? 58   THR I CB  1 
ATOM   8224  O  OG1 . THR H  1 58  ? 50.358 -15.675 1.312    1.00 26.62 ? 58   THR I OG1 1 
ATOM   8225  C  CG2 . THR H  1 58  ? 48.230 -14.945 2.253    1.00 28.03 ? 58   THR I CG2 1 
ATOM   8226  N  N   . SER H  1 59  ? 47.580 -14.607 -1.804   1.00 26.21 ? 59   SER I N   1 
ATOM   8227  C  CA  . SER H  1 59  ? 46.630 -13.745 -2.539   1.00 25.58 ? 59   SER I CA  1 
ATOM   8228  C  C   . SER H  1 59  ? 45.593 -14.519 -3.377   1.00 25.38 ? 59   SER I C   1 
ATOM   8229  O  O   . SER H  1 59  ? 44.670 -13.921 -3.946   1.00 24.65 ? 59   SER I O   1 
ATOM   8230  C  CB  . SER H  1 59  ? 47.387 -12.734 -3.419   1.00 25.43 ? 59   SER I CB  1 
ATOM   8231  O  OG  . SER H  1 59  ? 48.599 -13.273 -3.920   1.00 25.61 ? 59   SER I OG  1 
ATOM   8232  N  N   . ALA H  1 60  ? 45.753 -15.840 -3.437   1.00 25.17 ? 60   ALA I N   1 
ATOM   8233  C  CA  . ALA H  1 60  ? 44.829 -16.737 -4.167   1.00 25.53 ? 60   ALA I CA  1 
ATOM   8234  C  C   . ALA H  1 60  ? 43.417 -16.845 -3.566   1.00 25.24 ? 60   ALA I C   1 
ATOM   8235  O  O   . ALA H  1 60  ? 42.478 -17.252 -4.247   1.00 25.51 ? 60   ALA I O   1 
ATOM   8236  C  CB  . ALA H  1 60  ? 45.449 -18.119 -4.310   1.00 25.04 ? 60   ALA I CB  1 
ATOM   8237  N  N   . GLY H  1 61  ? 43.264 -16.488 -2.295   1.00 24.98 ? 61   GLY I N   1 
ATOM   8238  C  CA  . GLY H  1 61  ? 41.941 -16.486 -1.656   1.00 25.12 ? 61   GLY I CA  1 
ATOM   8239  C  C   . GLY H  1 61  ? 41.520 -17.858 -1.130   1.00 25.03 ? 61   GLY I C   1 
ATOM   8240  O  O   . GLY H  1 61  ? 42.344 -18.775 -1.062   1.00 24.94 ? 61   GLY I O   1 
ATOM   8241  N  N   . PRO H  1 62  ? 40.231 -18.006 -0.765   1.00 25.43 ? 62   PRO I N   1 
ATOM   8242  C  CA  . PRO H  1 62  ? 39.732 -19.268 -0.217   1.00 26.05 ? 62   PRO I CA  1 
ATOM   8243  C  C   . PRO H  1 62  ? 39.486 -20.280 -1.342   1.00 26.68 ? 62   PRO I C   1 
ATOM   8244  O  O   . PRO H  1 62  ? 39.762 -19.967 -2.505   1.00 26.45 ? 62   PRO I O   1 
ATOM   8245  C  CB  . PRO H  1 62  ? 38.421 -18.859 0.467    1.00 25.95 ? 62   PRO I CB  1 
ATOM   8246  C  CG  . PRO H  1 62  ? 37.968 -17.625 -0.249   1.00 26.24 ? 62   PRO I CG  1 
ATOM   8247  C  CD  . PRO H  1 62  ? 39.156 -17.011 -0.943   1.00 25.44 ? 62   PRO I CD  1 
ATOM   8248  N  N   . HIS H  1 63  ? 38.984 -21.469 -1.009   1.00 27.31 ? 63   HIS I N   1 
ATOM   8249  C  CA  . HIS H  1 63  ? 38.677 -22.493 -2.020   1.00 28.07 ? 63   HIS I CA  1 
ATOM   8250  C  C   . HIS H  1 63  ? 37.607 -21.950 -2.973   1.00 28.10 ? 63   HIS I C   1 
ATOM   8251  O  O   . HIS H  1 63  ? 36.700 -21.210 -2.551   1.00 27.99 ? 63   HIS I O   1 
ATOM   8252  C  CB  . HIS H  1 63  ? 38.209 -23.806 -1.351   1.00 28.43 ? 63   HIS I CB  1 
ATOM   8253  C  CG  . HIS H  1 63  ? 39.229 -24.435 -0.440   1.00 30.64 ? 63   HIS I CG  1 
ATOM   8254  N  ND1 . HIS H  1 63  ? 39.212 -25.775 -0.112   1.00 32.84 ? 63   HIS I ND1 1 
ATOM   8255  C  CD2 . HIS H  1 63  ? 40.293 -23.906 0.216    1.00 32.57 ? 63   HIS I CD2 1 
ATOM   8256  C  CE1 . HIS H  1 63  ? 40.216 -26.044 0.702    1.00 32.76 ? 63   HIS I CE1 1 
ATOM   8257  N  NE2 . HIS H  1 63  ? 40.891 -24.929 0.912    1.00 32.76 ? 63   HIS I NE2 1 
ATOM   8258  N  N   . PHE H  1 64  ? 37.733 -22.278 -4.260   1.00 28.04 ? 64   PHE I N   1 
ATOM   8259  C  CA  . PHE H  1 64  ? 36.750 -21.858 -5.251   1.00 28.09 ? 64   PHE I CA  1 
ATOM   8260  C  C   . PHE H  1 64  ? 35.400 -22.478 -4.838   1.00 28.35 ? 64   PHE I C   1 
ATOM   8261  O  O   . PHE H  1 64  ? 35.286 -23.697 -4.709   1.00 28.20 ? 64   PHE I O   1 
ATOM   8262  C  CB  . PHE H  1 64  ? 37.212 -22.247 -6.673   1.00 27.66 ? 64   PHE I CB  1 
ATOM   8263  C  CG  . PHE H  1 64  ? 36.263 -21.835 -7.778   1.00 28.01 ? 64   PHE I CG  1 
ATOM   8264  C  CD1 . PHE H  1 64  ? 35.985 -22.712 -8.824   1.00 27.29 ? 64   PHE I CD1 1 
ATOM   8265  C  CD2 . PHE H  1 64  ? 35.641 -20.578 -7.777   1.00 28.81 ? 64   PHE I CD2 1 
ATOM   8266  C  CE1 . PHE H  1 64  ? 35.105 -22.362 -9.848   1.00 27.19 ? 64   PHE I CE1 1 
ATOM   8267  C  CE2 . PHE H  1 64  ? 34.750 -20.214 -8.801   1.00 28.10 ? 64   PHE I CE2 1 
ATOM   8268  C  CZ  . PHE H  1 64  ? 34.489 -21.109 -9.843   1.00 28.34 ? 64   PHE I CZ  1 
ATOM   8269  N  N   . ASN H  1 65  ? 34.413 -21.615 -4.580   1.00 28.66 ? 65   ASN I N   1 
ATOM   8270  C  CA  . ASN H  1 65  ? 33.114 -22.015 -3.997   1.00 28.82 ? 65   ASN I CA  1 
ATOM   8271  C  C   . ASN H  1 65  ? 31.936 -21.246 -4.618   1.00 29.39 ? 65   ASN I C   1 
ATOM   8272  O  O   . ASN H  1 65  ? 31.256 -20.462 -3.925   1.00 29.53 ? 65   ASN I O   1 
ATOM   8273  C  CB  . ASN H  1 65  ? 33.137 -21.803 -2.472   1.00 28.84 ? 65   ASN I CB  1 
ATOM   8274  C  CG  . ASN H  1 65  ? 31.927 -22.423 -1.754   1.00 28.96 ? 65   ASN I CG  1 
ATOM   8275  O  OD1 . ASN H  1 65  ? 31.218 -23.279 -2.296   1.00 28.49 ? 65   ASN I OD1 1 
ATOM   8276  N  ND2 . ASN H  1 65  ? 31.699 -21.988 -0.517   1.00 27.94 ? 65   ASN I ND2 1 
ATOM   8277  N  N   . PRO H  1 66  ? 31.686 -21.447 -5.929   1.00 29.38 ? 66   PRO I N   1 
ATOM   8278  C  CA  . PRO H  1 66  ? 30.628 -20.663 -6.574   1.00 29.82 ? 66   PRO I CA  1 
ATOM   8279  C  C   . PRO H  1 66  ? 29.207 -21.055 -6.144   1.00 30.52 ? 66   PRO I C   1 
ATOM   8280  O  O   . PRO H  1 66  ? 28.276 -20.266 -6.316   1.00 30.53 ? 66   PRO I O   1 
ATOM   8281  C  CB  . PRO H  1 66  ? 30.844 -20.940 -8.068   1.00 29.67 ? 66   PRO I CB  1 
ATOM   8282  C  CG  . PRO H  1 66  ? 31.591 -22.224 -8.116   1.00 28.94 ? 66   PRO I CG  1 
ATOM   8283  C  CD  . PRO H  1 66  ? 32.445 -22.254 -6.899   1.00 29.39 ? 66   PRO I CD  1 
ATOM   8284  N  N   . LEU H  1 67  ? 29.046 -22.252 -5.587   1.00 31.26 ? 67   LEU I N   1 
ATOM   8285  C  CA  . LEU H  1 67  ? 27.719 -22.745 -5.189   1.00 32.38 ? 67   LEU I CA  1 
ATOM   8286  C  C   . LEU H  1 67  ? 27.435 -22.497 -3.703   1.00 32.78 ? 67   LEU I C   1 
ATOM   8287  O  O   . LEU H  1 67  ? 26.352 -22.844 -3.200   1.00 32.78 ? 67   LEU I O   1 
ATOM   8288  C  CB  . LEU H  1 67  ? 27.563 -24.236 -5.530   1.00 32.62 ? 67   LEU I CB  1 
ATOM   8289  C  CG  . LEU H  1 67  ? 27.995 -24.673 -6.937   1.00 33.52 ? 67   LEU I CG  1 
ATOM   8290  C  CD1 . LEU H  1 67  ? 27.763 -26.163 -7.144   1.00 34.05 ? 67   LEU I CD1 1 
ATOM   8291  C  CD2 . LEU H  1 67  ? 27.297 -23.851 -8.027   1.00 34.34 ? 67   LEU I CD2 1 
ATOM   8292  N  N   . SER H  1 68  ? 28.422 -21.905 -3.023   1.00 33.06 ? 68   SER I N   1 
ATOM   8293  C  CA  . SER H  1 68  ? 28.322 -21.469 -1.623   1.00 33.45 ? 68   SER I CA  1 
ATOM   8294  C  C   . SER H  1 68  ? 28.011 -22.603 -0.638   1.00 33.66 ? 68   SER I C   1 
ATOM   8295  O  O   . SER H  1 68  ? 27.036 -22.537 0.121    1.00 33.42 ? 68   SER I O   1 
ATOM   8296  C  CB  . SER H  1 68  ? 27.298 -20.341 -1.497   1.00 33.46 ? 68   SER I CB  1 
ATOM   8297  O  OG  . SER H  1 68  ? 27.482 -19.385 -2.526   1.00 34.14 ? 68   SER I OG  1 
ATOM   8298  N  N   . ARG H  1 69  ? 28.858 -23.633 -0.663   1.00 33.83 ? 69   ARG I N   1 
ATOM   8299  C  CA  . ARG H  1 69  ? 28.700 -24.824 0.171    1.00 34.23 ? 69   ARG I CA  1 
ATOM   8300  C  C   . ARG H  1 69  ? 29.854 -24.952 1.166    1.00 34.27 ? 69   ARG I C   1 
ATOM   8301  O  O   . ARG H  1 69  ? 30.794 -24.163 1.126    1.00 34.21 ? 69   ARG I O   1 
ATOM   8302  C  CB  . ARG H  1 69  ? 28.617 -26.074 -0.713   1.00 34.35 ? 69   ARG I CB  1 
ATOM   8303  C  CG  . ARG H  1 69  ? 27.476 -26.014 -1.708   1.00 35.28 ? 69   ARG I CG  1 
ATOM   8304  C  CD  . ARG H  1 69  ? 27.141 -27.365 -2.274   1.00 36.09 ? 69   ARG I CD  1 
ATOM   8305  N  NE  . ARG H  1 69  ? 26.033 -27.256 -3.217   1.00 37.81 ? 69   ARG I NE  1 
ATOM   8306  C  CZ  . ARG H  1 69  ? 25.658 -28.225 -4.046   1.00 38.48 ? 69   ARG I CZ  1 
ATOM   8307  N  NH1 . ARG H  1 69  ? 24.633 -28.030 -4.866   1.00 38.94 ? 69   ARG I NH1 1 
ATOM   8308  N  NH2 . ARG H  1 69  ? 26.303 -29.388 -4.054   1.00 38.74 ? 69   ARG I NH2 1 
ATOM   8309  N  N   . LYS H  1 70  ? 29.771 -25.938 2.060    1.00 33.98 ? 70   LYS I N   1 
ATOM   8310  C  CA  . LYS H  1 70  ? 30.844 -26.212 3.019    1.00 34.19 ? 70   LYS I CA  1 
ATOM   8311  C  C   . LYS H  1 70  ? 31.941 -27.061 2.371    1.00 33.88 ? 70   LYS I C   1 
ATOM   8312  O  O   . LYS H  1 70  ? 31.723 -27.676 1.322    1.00 33.76 ? 70   LYS I O   1 
ATOM   8313  C  CB  . LYS H  1 70  ? 30.306 -26.926 4.273    1.00 34.43 ? 70   LYS I CB  1 
ATOM   8314  C  CG  . LYS H  1 70  ? 29.123 -26.237 4.971    1.00 35.62 ? 70   LYS I CG  1 
ATOM   8315  C  CD  . LYS H  1 70  ? 29.237 -26.271 6.516    1.00 37.43 ? 70   LYS I CD  1 
ATOM   8316  C  CE  . LYS H  1 70  ? 29.499 -27.673 7.095    1.00 38.23 ? 70   LYS I CE  1 
ATOM   8317  N  NZ  . LYS H  1 70  ? 28.370 -28.626 6.906    1.00 38.87 ? 70   LYS I NZ  1 
ATOM   8318  N  N   . HIS H  1 71  ? 33.113 -27.089 3.004    1.00 33.54 ? 71   HIS I N   1 
ATOM   8319  C  CA  . HIS H  1 71  ? 34.250 -27.868 2.522    1.00 33.34 ? 71   HIS I CA  1 
ATOM   8320  C  C   . HIS H  1 71  ? 34.003 -29.361 2.658    1.00 33.48 ? 71   HIS I C   1 
ATOM   8321  O  O   . HIS H  1 71  ? 33.355 -29.807 3.612    1.00 33.19 ? 71   HIS I O   1 
ATOM   8322  C  CB  . HIS H  1 71  ? 35.523 -27.479 3.279    1.00 33.23 ? 71   HIS I CB  1 
ATOM   8323  C  CG  . HIS H  1 71  ? 36.727 -28.282 2.898    1.00 33.36 ? 71   HIS I CG  1 
ATOM   8324  N  ND1 . HIS H  1 71  ? 37.492 -28.000 1.784    1.00 32.82 ? 71   HIS I ND1 1 
ATOM   8325  C  CD2 . HIS H  1 71  ? 37.305 -29.353 3.488    1.00 33.15 ? 71   HIS I CD2 1 
ATOM   8326  C  CE1 . HIS H  1 71  ? 38.484 -28.870 1.703    1.00 34.13 ? 71   HIS I CE1 1 
ATOM   8327  N  NE2 . HIS H  1 71  ? 38.392 -29.701 2.724    1.00 33.01 ? 71   HIS I NE2 1 
ATOM   8328  N  N   . GLY H  1 72  ? 34.527 -30.128 1.706    1.00 33.44 ? 72   GLY I N   1 
ATOM   8329  C  CA  . GLY H  1 72  ? 34.457 -31.583 1.771    1.00 33.95 ? 72   GLY I CA  1 
ATOM   8330  C  C   . GLY H  1 72  ? 35.586 -32.250 1.018    1.00 34.19 ? 72   GLY I C   1 
ATOM   8331  O  O   . GLY H  1 72  ? 36.553 -31.601 0.614    1.00 33.91 ? 72   GLY I O   1 
ATOM   8332  N  N   . GLY H  1 73  ? 35.468 -33.564 0.856    1.00 34.64 ? 73   GLY I N   1 
ATOM   8333  C  CA  . GLY H  1 73  ? 36.314 -34.306 -0.069   1.00 34.97 ? 73   GLY I CA  1 
ATOM   8334  C  C   . GLY H  1 73  ? 35.690 -34.206 -1.452   1.00 35.24 ? 73   GLY I C   1 
ATOM   8335  O  O   . GLY H  1 73  ? 34.580 -33.681 -1.590   1.00 35.31 ? 73   GLY I O   1 
ATOM   8336  N  N   . PRO H  1 74  ? 36.382 -34.721 -2.488   1.00 35.72 ? 74   PRO I N   1 
ATOM   8337  C  CA  . PRO H  1 74  ? 35.795 -34.670 -3.839   1.00 35.94 ? 74   PRO I CA  1 
ATOM   8338  C  C   . PRO H  1 74  ? 34.568 -35.587 -3.971   1.00 36.37 ? 74   PRO I C   1 
ATOM   8339  O  O   . PRO H  1 74  ? 33.714 -35.361 -4.840   1.00 36.43 ? 74   PRO I O   1 
ATOM   8340  C  CB  . PRO H  1 74  ? 36.933 -35.151 -4.741   1.00 35.75 ? 74   PRO I CB  1 
ATOM   8341  C  CG  . PRO H  1 74  ? 37.826 -35.952 -3.850   1.00 36.17 ? 74   PRO I CG  1 
ATOM   8342  C  CD  . PRO H  1 74  ? 37.690 -35.403 -2.463   1.00 35.42 ? 74   PRO I CD  1 
ATOM   8343  N  N   . LYS H  1 75  ? 34.490 -36.588 -3.090   1.00 36.70 ? 75   LYS I N   1 
ATOM   8344  C  CA  . LYS H  1 75  ? 33.414 -37.580 -3.074   1.00 36.93 ? 75   LYS I CA  1 
ATOM   8345  C  C   . LYS H  1 75  ? 32.130 -37.049 -2.437   1.00 36.91 ? 75   LYS I C   1 
ATOM   8346  O  O   . LYS H  1 75  ? 31.045 -37.569 -2.701   1.00 36.69 ? 75   LYS I O   1 
ATOM   8347  C  CB  . LYS H  1 75  ? 33.878 -38.837 -2.335   1.00 37.19 ? 75   LYS I CB  1 
ATOM   8348  C  CG  . LYS H  1 75  ? 35.251 -39.353 -2.758   1.00 38.01 ? 75   LYS I CG  1 
ATOM   8349  C  CD  . LYS H  1 75  ? 35.203 -39.996 -4.122   1.00 39.01 ? 75   LYS I CD  1 
ATOM   8350  C  CE  . LYS H  1 75  ? 36.584 -40.114 -4.724   1.00 39.62 ? 75   LYS I CE  1 
ATOM   8351  N  NZ  . LYS H  1 75  ? 36.478 -40.393 -6.187   1.00 39.79 ? 75   LYS I NZ  1 
ATOM   8352  N  N   . ASP H  1 76  ? 32.257 -36.013 -1.608   1.00 36.86 ? 76   ASP I N   1 
ATOM   8353  C  CA  . ASP H  1 76  ? 31.119 -35.455 -0.877   1.00 37.40 ? 76   ASP I CA  1 
ATOM   8354  C  C   . ASP H  1 76  ? 30.086 -34.755 -1.768   1.00 37.55 ? 76   ASP I C   1 
ATOM   8355  O  O   . ASP H  1 76  ? 30.439 -34.029 -2.704   1.00 37.61 ? 76   ASP I O   1 
ATOM   8356  C  CB  . ASP H  1 76  ? 31.599 -34.506 0.233    1.00 37.41 ? 76   ASP I CB  1 
ATOM   8357  C  CG  . ASP H  1 76  ? 32.221 -35.247 1.412    1.00 37.99 ? 76   ASP I CG  1 
ATOM   8358  O  OD1 . ASP H  1 76  ? 32.964 -34.621 2.202    1.00 37.58 ? 76   ASP I OD1 1 
ATOM   8359  O  OD2 . ASP H  1 76  ? 31.967 -36.462 1.553    1.00 38.92 ? 76   ASP I OD2 1 
ATOM   8360  N  N   . GLU H  1 77  ? 28.810 -35.002 -1.469   1.00 37.86 ? 77   GLU I N   1 
ATOM   8361  C  CA  . GLU H  1 77  ? 27.687 -34.279 -2.075   1.00 38.01 ? 77   GLU I CA  1 
ATOM   8362  C  C   . GLU H  1 77  ? 27.816 -32.781 -1.767   1.00 37.74 ? 77   GLU I C   1 
ATOM   8363  O  O   . GLU H  1 77  ? 27.553 -31.929 -2.623   1.00 38.06 ? 77   GLU I O   1 
ATOM   8364  C  CB  . GLU H  1 77  ? 26.357 -34.846 -1.543   1.00 38.33 ? 77   GLU I CB  1 
ATOM   8365  C  CG  . GLU H  1 77  ? 25.123 -33.952 -1.729   1.00 39.29 ? 77   GLU I CG  1 
ATOM   8366  C  CD  . GLU H  1 77  ? 23.863 -34.534 -1.094   1.00 40.76 ? 77   GLU I CD  1 
ATOM   8367  O  OE1 . GLU H  1 77  ? 23.247 -35.449 -1.688   1.00 41.13 ? 77   GLU I OE1 1 
ATOM   8368  O  OE2 . GLU H  1 77  ? 23.475 -34.063 -0.003   1.00 41.39 ? 77   GLU I OE2 1 
ATOM   8369  N  N   . GLU H  1 78  ? 28.235 -32.483 -0.539   1.00 37.18 ? 78   GLU I N   1 
ATOM   8370  C  CA  . GLU H  1 78  ? 28.481 -31.122 -0.080   1.00 36.61 ? 78   GLU I CA  1 
ATOM   8371  C  C   . GLU H  1 78  ? 29.991 -30.861 -0.066   1.00 35.87 ? 78   GLU I C   1 
ATOM   8372  O  O   . GLU H  1 78  ? 30.722 -31.448 0.737    1.00 35.41 ? 78   GLU I O   1 
ATOM   8373  C  CB  . GLU H  1 78  ? 27.870 -30.931 1.315    1.00 36.79 ? 78   GLU I CB  1 
ATOM   8374  C  CG  . GLU H  1 78  ? 27.998 -29.530 1.898    1.00 37.81 ? 78   GLU I CG  1 
ATOM   8375  C  CD  . GLU H  1 78  ? 26.901 -28.578 1.436    1.00 39.34 ? 78   GLU I CD  1 
ATOM   8376  O  OE1 . GLU H  1 78  ? 26.976 -27.380 1.797    1.00 39.03 ? 78   GLU I OE1 1 
ATOM   8377  O  OE2 . GLU H  1 78  ? 25.968 -29.014 0.717    1.00 39.86 ? 78   GLU I OE2 1 
ATOM   8378  N  N   . ARG H  1 79  ? 30.439 -29.978 -0.964   1.00 34.87 ? 79   ARG I N   1 
ATOM   8379  C  CA  . ARG H  1 79  ? 31.861 -29.661 -1.165   1.00 34.02 ? 79   ARG I CA  1 
ATOM   8380  C  C   . ARG H  1 79  ? 31.996 -28.352 -1.942   1.00 33.28 ? 79   ARG I C   1 
ATOM   8381  O  O   . ARG H  1 79  ? 31.092 -27.976 -2.691   1.00 33.73 ? 79   ARG I O   1 
ATOM   8382  C  CB  . ARG H  1 79  ? 32.585 -30.788 -1.934   1.00 34.03 ? 79   ARG I CB  1 
ATOM   8383  C  CG  . ARG H  1 79  ? 31.992 -31.113 -3.323   1.00 33.49 ? 79   ARG I CG  1 
ATOM   8384  C  CD  . ARG H  1 79  ? 32.895 -32.040 -4.161   1.00 32.88 ? 79   ARG I CD  1 
ATOM   8385  N  NE  . ARG H  1 79  ? 33.896 -31.289 -4.930   1.00 32.16 ? 79   ARG I NE  1 
ATOM   8386  C  CZ  . ARG H  1 79  ? 34.596 -31.773 -5.957   1.00 30.92 ? 79   ARG I CZ  1 
ATOM   8387  N  NH1 . ARG H  1 79  ? 35.468 -30.992 -6.579   1.00 30.13 ? 79   ARG I NH1 1 
ATOM   8388  N  NH2 . ARG H  1 79  ? 34.425 -33.025 -6.373   1.00 29.27 ? 79   ARG I NH2 1 
ATOM   8389  N  N   . HIS H  1 80  ? 33.118 -27.659 -1.766   1.00 32.30 ? 80   HIS I N   1 
ATOM   8390  C  CA  . HIS H  1 80  ? 33.451 -26.535 -2.644   1.00 31.24 ? 80   HIS I CA  1 
ATOM   8391  C  C   . HIS H  1 80  ? 33.853 -27.100 -3.998   1.00 30.41 ? 80   HIS I C   1 
ATOM   8392  O  O   . HIS H  1 80  ? 34.507 -28.137 -4.069   1.00 30.13 ? 80   HIS I O   1 
ATOM   8393  C  CB  . HIS H  1 80  ? 34.628 -25.731 -2.101   1.00 31.22 ? 80   HIS I CB  1 
ATOM   8394  C  CG  . HIS H  1 80  ? 34.425 -25.198 -0.718   1.00 31.35 ? 80   HIS I CG  1 
ATOM   8395  N  ND1 . HIS H  1 80  ? 35.406 -25.249 0.248    1.00 30.62 ? 80   HIS I ND1 1 
ATOM   8396  C  CD2 . HIS H  1 80  ? 33.364 -24.584 -0.143   1.00 31.43 ? 80   HIS I CD2 1 
ATOM   8397  C  CE1 . HIS H  1 80  ? 34.959 -24.690 1.359    1.00 31.37 ? 80   HIS I CE1 1 
ATOM   8398  N  NE2 . HIS H  1 80  ? 33.721 -24.280 1.149    1.00 30.82 ? 80   HIS I NE2 1 
ATOM   8399  N  N   . VAL H  1 81  ? 33.490 -26.414 -5.075   1.00 29.48 ? 81   VAL I N   1 
ATOM   8400  C  CA  . VAL H  1 81  ? 33.896 -26.861 -6.408   1.00 28.83 ? 81   VAL I CA  1 
ATOM   8401  C  C   . VAL H  1 81  ? 35.402 -27.184 -6.470   1.00 28.61 ? 81   VAL I C   1 
ATOM   8402  O  O   . VAL H  1 81  ? 35.801 -28.187 -7.062   1.00 28.30 ? 81   VAL I O   1 
ATOM   8403  C  CB  . VAL H  1 81  ? 33.464 -25.852 -7.502   1.00 28.56 ? 81   VAL I CB  1 
ATOM   8404  C  CG1 . VAL H  1 81  ? 34.182 -26.117 -8.817   1.00 28.58 ? 81   VAL I CG1 1 
ATOM   8405  C  CG2 . VAL H  1 81  ? 31.947 -25.915 -7.688   1.00 28.11 ? 81   VAL I CG2 1 
ATOM   8406  N  N   . GLY H  1 82  ? 36.220 -26.358 -5.818   1.00 28.57 ? 82   GLY I N   1 
ATOM   8407  C  CA  . GLY H  1 82  ? 37.671 -26.502 -5.871   1.00 28.92 ? 82   GLY I CA  1 
ATOM   8408  C  C   . GLY H  1 82  ? 38.279 -27.633 -5.058   1.00 29.43 ? 82   GLY I C   1 
ATOM   8409  O  O   . GLY H  1 82  ? 39.487 -27.858 -5.130   1.00 29.07 ? 82   GLY I O   1 
ATOM   8410  N  N   . ASP H  1 83  ? 37.448 -28.344 -4.290   1.00 30.00 ? 83   ASP I N   1 
ATOM   8411  C  CA  . ASP H  1 83  ? 37.917 -29.388 -3.366   1.00 30.57 ? 83   ASP I CA  1 
ATOM   8412  C  C   . ASP H  1 83  ? 38.357 -30.681 -4.053   1.00 30.77 ? 83   ASP I C   1 
ATOM   8413  O  O   . ASP H  1 83  ? 37.530 -31.551 -4.362   1.00 30.55 ? 83   ASP I O   1 
ATOM   8414  C  CB  . ASP H  1 83  ? 36.845 -29.702 -2.308   1.00 30.55 ? 83   ASP I CB  1 
ATOM   8415  C  CG  . ASP H  1 83  ? 36.701 -28.601 -1.274   1.00 31.34 ? 83   ASP I CG  1 
ATOM   8416  O  OD1 . ASP H  1 83  ? 37.697 -27.851 -1.060   1.00 29.88 ? 83   ASP I OD1 1 
ATOM   8417  O  OD2 . ASP H  1 83  ? 35.601 -28.508 -0.663   1.00 30.95 ? 83   ASP I OD2 1 
ATOM   8418  N  N   . LEU H  1 84  ? 39.662 -30.818 -4.263   1.00 31.06 ? 84   LEU I N   1 
ATOM   8419  C  CA  . LEU H  1 84  ? 40.203 -32.014 -4.914   1.00 31.87 ? 84   LEU I CA  1 
ATOM   8420  C  C   . LEU H  1 84  ? 40.914 -32.958 -3.942   1.00 32.50 ? 84   LEU I C   1 
ATOM   8421  O  O   . LEU H  1 84  ? 41.719 -33.797 -4.362   1.00 32.81 ? 84   LEU I O   1 
ATOM   8422  C  CB  . LEU H  1 84  ? 41.124 -31.642 -6.081   1.00 31.76 ? 84   LEU I CB  1 
ATOM   8423  C  CG  . LEU H  1 84  ? 40.532 -30.797 -7.217   1.00 31.36 ? 84   LEU I CG  1 
ATOM   8424  C  CD1 . LEU H  1 84  ? 41.638 -30.371 -8.162   1.00 30.79 ? 84   LEU I CD1 1 
ATOM   8425  C  CD2 . LEU H  1 84  ? 39.414 -31.519 -7.962   1.00 30.15 ? 84   LEU I CD2 1 
ATOM   8426  N  N   . GLY H  1 85  ? 40.614 -32.805 -2.649   1.00 33.27 ? 85   GLY I N   1 
ATOM   8427  C  CA  . GLY H  1 85  ? 41.044 -33.750 -1.616   1.00 33.99 ? 85   GLY I CA  1 
ATOM   8428  C  C   . GLY H  1 85  ? 42.526 -33.727 -1.291   1.00 34.96 ? 85   GLY I C   1 
ATOM   8429  O  O   . GLY H  1 85  ? 43.067 -32.708 -0.816   1.00 34.90 ? 85   GLY I O   1 
ATOM   8430  N  N   . ASN H  1 86  ? 43.172 -34.867 -1.544   1.00 35.75 ? 86   ASN I N   1 
ATOM   8431  C  CA  . ASN H  1 86  ? 44.577 -35.092 -1.211   1.00 36.50 ? 86   ASN I CA  1 
ATOM   8432  C  C   . ASN H  1 86  ? 45.333 -35.785 -2.336   1.00 37.18 ? 86   ASN I C   1 
ATOM   8433  O  O   . ASN H  1 86  ? 44.789 -36.652 -3.026   1.00 36.91 ? 86   ASN I O   1 
ATOM   8434  C  CB  . ASN H  1 86  ? 44.702 -35.961 0.051    1.00 36.33 ? 86   ASN I CB  1 
ATOM   8435  C  CG  . ASN H  1 86  ? 44.424 -35.193 1.332    1.00 36.28 ? 86   ASN I CG  1 
ATOM   8436  O  OD1 . ASN H  1 86  ? 45.161 -34.278 1.700    1.00 34.73 ? 86   ASN I OD1 1 
ATOM   8437  N  ND2 . ASN H  1 86  ? 43.366 -35.585 2.031    1.00 36.51 ? 86   ASN I ND2 1 
ATOM   8438  N  N   . VAL H  1 87  ? 46.588 -35.386 -2.513   1.00 38.18 ? 87   VAL I N   1 
ATOM   8439  C  CA  . VAL H  1 87  ? 47.561 -36.195 -3.235   1.00 39.39 ? 87   VAL I CA  1 
ATOM   8440  C  C   . VAL H  1 87  ? 48.549 -36.727 -2.202   1.00 40.43 ? 87   VAL I C   1 
ATOM   8441  O  O   . VAL H  1 87  ? 48.664 -36.169 -1.105   1.00 40.70 ? 87   VAL I O   1 
ATOM   8442  C  CB  . VAL H  1 87  ? 48.290 -35.409 -4.348   1.00 39.50 ? 87   VAL I CB  1 
ATOM   8443  C  CG1 . VAL H  1 87  ? 47.310 -35.045 -5.451   1.00 39.44 ? 87   VAL I CG1 1 
ATOM   8444  C  CG2 . VAL H  1 87  ? 48.993 -34.156 -3.791   1.00 39.38 ? 87   VAL I CG2 1 
ATOM   8445  N  N   . THR H  1 88  ? 49.252 -37.801 -2.546   1.00 41.52 ? 88   THR I N   1 
ATOM   8446  C  CA  . THR H  1 88  ? 50.144 -38.466 -1.595   1.00 42.48 ? 88   THR I CA  1 
ATOM   8447  C  C   . THR H  1 88  ? 51.562 -38.587 -2.145   1.00 43.07 ? 88   THR I C   1 
ATOM   8448  O  O   . THR H  1 88  ? 51.774 -39.172 -3.215   1.00 43.11 ? 88   THR I O   1 
ATOM   8449  C  CB  . THR H  1 88  ? 49.607 -39.865 -1.200   1.00 42.40 ? 88   THR I CB  1 
ATOM   8450  O  OG1 . THR H  1 88  ? 48.203 -39.780 -0.926   1.00 42.38 ? 88   THR I OG1 1 
ATOM   8451  C  CG2 . THR H  1 88  ? 50.329 -40.398 0.040    1.00 43.15 ? 88   THR I CG2 1 
ATOM   8452  N  N   . ALA H  1 89  ? 52.521 -38.031 -1.401   1.00 43.87 ? 89   ALA I N   1 
ATOM   8453  C  CA  . ALA H  1 89  ? 53.928 -38.047 -1.795   1.00 44.73 ? 89   ALA I CA  1 
ATOM   8454  C  C   . ALA H  1 89  ? 54.594 -39.345 -1.359   1.00 45.27 ? 89   ALA I C   1 
ATOM   8455  O  O   . ALA H  1 89  ? 54.447 -39.750 -0.207   1.00 45.26 ? 89   ALA I O   1 
ATOM   8456  C  CB  . ALA H  1 89  ? 54.658 -36.844 -1.205   1.00 44.78 ? 89   ALA I CB  1 
ATOM   8457  N  N   . ASP H  1 90  ? 55.321 -39.985 -2.281   1.00 46.10 ? 90   ASP I N   1 
ATOM   8458  C  CA  . ASP H  1 90  ? 56.014 -41.259 -2.007   1.00 46.72 ? 90   ASP I CA  1 
ATOM   8459  C  C   . ASP H  1 90  ? 57.281 -41.072 -1.164   1.00 47.21 ? 90   ASP I C   1 
ATOM   8460  O  O   . ASP H  1 90  ? 57.498 -39.991 -0.596   1.00 47.23 ? 90   ASP I O   1 
ATOM   8461  C  CB  . ASP H  1 90  ? 56.285 -42.063 -3.304   1.00 46.71 ? 90   ASP I CB  1 
ATOM   8462  C  CG  . ASP H  1 90  ? 57.469 -41.531 -4.127   1.00 46.96 ? 90   ASP I CG  1 
ATOM   8463  O  OD1 . ASP H  1 90  ? 57.336 -41.436 -5.363   1.00 47.64 ? 90   ASP I OD1 1 
ATOM   8464  O  OD2 . ASP H  1 90  ? 58.543 -41.236 -3.564   1.00 47.08 ? 90   ASP I OD2 1 
ATOM   8465  N  N   . LYS H  1 91  ? 58.099 -42.128 -1.080   1.00 47.91 ? 91   LYS I N   1 
ATOM   8466  C  CA  . LYS H  1 91  ? 59.341 -42.119 -0.294   1.00 48.50 ? 91   LYS I CA  1 
ATOM   8467  C  C   . LYS H  1 91  ? 60.200 -40.864 -0.529   1.00 48.68 ? 91   LYS I C   1 
ATOM   8468  O  O   . LYS H  1 91  ? 60.524 -40.138 0.423    1.00 48.87 ? 91   LYS I O   1 
ATOM   8469  C  CB  . LYS H  1 91  ? 60.156 -43.418 -0.503   1.00 48.62 ? 91   LYS I CB  1 
ATOM   8470  C  CG  . LYS H  1 91  ? 60.540 -43.746 -1.967   1.00 49.28 ? 91   LYS I CG  1 
ATOM   8471  C  CD  . LYS H  1 91  ? 61.916 -44.431 -2.069   1.00 49.59 ? 91   LYS I CD  1 
ATOM   8472  C  CE  . LYS H  1 91  ? 61.818 -45.945 -2.240   1.00 49.36 ? 91   LYS I CE  1 
ATOM   8473  N  NZ  . LYS H  1 91  ? 61.400 -46.349 -3.610   1.00 49.25 ? 91   LYS I NZ  1 
ATOM   8474  N  N   . ASP H  1 92  ? 60.520 -40.597 -1.797   1.00 48.72 ? 92   ASP I N   1 
ATOM   8475  C  CA  . ASP H  1 92  ? 61.393 -39.488 -2.197   1.00 48.69 ? 92   ASP I CA  1 
ATOM   8476  C  C   . ASP H  1 92  ? 60.670 -38.129 -2.234   1.00 48.58 ? 92   ASP I C   1 
ATOM   8477  O  O   . ASP H  1 92  ? 61.133 -37.189 -2.885   1.00 48.66 ? 92   ASP I O   1 
ATOM   8478  C  CB  . ASP H  1 92  ? 62.027 -39.790 -3.564   1.00 48.75 ? 92   ASP I CB  1 
ATOM   8479  C  CG  . ASP H  1 92  ? 62.543 -41.223 -3.674   1.00 49.01 ? 92   ASP I CG  1 
ATOM   8480  O  OD1 . ASP H  1 92  ? 61.989 -41.991 -4.490   1.00 49.27 ? 92   ASP I OD1 1 
ATOM   8481  O  OD2 . ASP H  1 92  ? 63.493 -41.586 -2.943   1.00 49.31 ? 92   ASP I OD2 1 
ATOM   8482  N  N   . GLY H  1 93  ? 59.538 -38.037 -1.536   1.00 48.35 ? 93   GLY I N   1 
ATOM   8483  C  CA  . GLY H  1 93  ? 58.746 -36.809 -1.466   1.00 48.06 ? 93   GLY I CA  1 
ATOM   8484  C  C   . GLY H  1 93  ? 58.032 -36.415 -2.749   1.00 47.85 ? 93   GLY I C   1 
ATOM   8485  O  O   . GLY H  1 93  ? 57.772 -35.230 -2.978   1.00 47.83 ? 93   GLY I O   1 
ATOM   8486  N  N   . VAL H  1 94  ? 57.699 -37.407 -3.577   1.00 47.53 ? 94   VAL I N   1 
ATOM   8487  C  CA  . VAL H  1 94  ? 57.097 -37.162 -4.894   1.00 47.21 ? 94   VAL I CA  1 
ATOM   8488  C  C   . VAL H  1 94  ? 55.651 -37.682 -4.972   1.00 47.00 ? 94   VAL I C   1 
ATOM   8489  O  O   . VAL H  1 94  ? 55.389 -38.876 -4.749   1.00 46.98 ? 94   VAL I O   1 
ATOM   8490  C  CB  . VAL H  1 94  ? 57.964 -37.757 -6.053   1.00 47.28 ? 94   VAL I CB  1 
ATOM   8491  C  CG1 . VAL H  1 94  ? 57.364 -37.421 -7.417   1.00 47.26 ? 94   VAL I CG1 1 
ATOM   8492  C  CG2 . VAL H  1 94  ? 59.404 -37.253 -5.975   1.00 47.14 ? 94   VAL I CG2 1 
ATOM   8493  N  N   . ALA H  1 95  ? 54.723 -36.776 -5.287   1.00 46.38 ? 95   ALA I N   1 
ATOM   8494  C  CA  . ALA H  1 95  ? 53.304 -37.117 -5.430   1.00 45.86 ? 95   ALA I CA  1 
ATOM   8495  C  C   . ALA H  1 95  ? 52.872 -37.273 -6.894   1.00 45.52 ? 95   ALA I C   1 
ATOM   8496  O  O   . ALA H  1 95  ? 52.780 -36.287 -7.632   1.00 45.47 ? 95   ALA I O   1 
ATOM   8497  C  CB  . ALA H  1 95  ? 52.425 -36.085 -4.706   1.00 45.79 ? 95   ALA I CB  1 
ATOM   8498  N  N   . ASP H  1 96  ? 52.609 -38.511 -7.309   1.00 44.96 ? 96   ASP I N   1 
ATOM   8499  C  CA  . ASP H  1 96  ? 52.105 -38.770 -8.660   1.00 44.51 ? 96   ASP I CA  1 
ATOM   8500  C  C   . ASP H  1 96  ? 50.581 -38.630 -8.730   1.00 43.98 ? 96   ASP I C   1 
ATOM   8501  O  O   . ASP H  1 96  ? 49.831 -39.512 -8.295   1.00 43.95 ? 96   ASP I O   1 
ATOM   8502  C  CB  . ASP H  1 96  ? 52.597 -40.119 -9.201   1.00 44.63 ? 96   ASP I CB  1 
ATOM   8503  C  CG  . ASP H  1 96  ? 53.967 -40.015 -9.862   1.00 45.07 ? 96   ASP I CG  1 
ATOM   8504  O  OD1 . ASP H  1 96  ? 54.851 -40.832 -9.536   1.00 45.99 ? 96   ASP I OD1 1 
ATOM   8505  O  OD2 . ASP H  1 96  ? 54.167 -39.110 -10.705  1.00 45.38 ? 96   ASP I OD2 1 
ATOM   8506  N  N   . VAL H  1 97  ? 50.146 -37.503 -9.289   1.00 43.12 ? 97   VAL I N   1 
ATOM   8507  C  CA  . VAL H  1 97  ? 48.737 -37.118 -9.311   1.00 42.22 ? 97   VAL I CA  1 
ATOM   8508  C  C   . VAL H  1 97  ? 47.978 -37.791 -10.460  1.00 41.82 ? 97   VAL I C   1 
ATOM   8509  O  O   . VAL H  1 97  ? 48.425 -37.769 -11.612  1.00 41.73 ? 97   VAL I O   1 
ATOM   8510  C  CB  . VAL H  1 97  ? 48.579 -35.567 -9.401   1.00 42.35 ? 97   VAL I CB  1 
ATOM   8511  C  CG1 . VAL H  1 97  ? 47.114 -35.157 -9.280   1.00 42.00 ? 97   VAL I CG1 1 
ATOM   8512  C  CG2 . VAL H  1 97  ? 49.426 -34.871 -8.331   1.00 41.53 ? 97   VAL I CG2 1 
ATOM   8513  N  N   . SER H  1 98  ? 46.841 -38.403 -10.129  1.00 40.89 ? 98   SER I N   1 
ATOM   8514  C  CA  . SER H  1 98  ? 45.896 -38.875 -11.138  1.00 40.43 ? 98   SER I CA  1 
ATOM   8515  C  C   . SER H  1 98  ? 44.470 -38.776 -10.599  1.00 39.80 ? 98   SER I C   1 
ATOM   8516  O  O   . SER H  1 98  ? 44.035 -39.609 -9.793   1.00 39.90 ? 98   SER I O   1 
ATOM   8517  C  CB  . SER H  1 98  ? 46.214 -40.302 -11.585  1.00 40.38 ? 98   SER I CB  1 
ATOM   8518  O  OG  . SER H  1 98  ? 46.000 -40.430 -12.978  1.00 40.89 ? 98   SER I OG  1 
ATOM   8519  N  N   . ILE H  1 99  ? 43.758 -37.741 -11.032  1.00 38.65 ? 99   ILE I N   1 
ATOM   8520  C  CA  . ILE H  1 99  ? 42.392 -37.484 -10.577  1.00 37.86 ? 99   ILE I CA  1 
ATOM   8521  C  C   . ILE H  1 99  ? 41.425 -37.499 -11.766  1.00 37.21 ? 99   ILE I C   1 
ATOM   8522  O  O   . ILE H  1 99  ? 41.779 -37.092 -12.877  1.00 37.06 ? 99   ILE I O   1 
ATOM   8523  C  CB  . ILE H  1 99  ? 42.281 -36.128 -9.775   1.00 37.91 ? 99   ILE I CB  1 
ATOM   8524  C  CG1 . ILE H  1 99  ? 43.137 -36.163 -8.494   1.00 38.07 ? 99   ILE I CG1 1 
ATOM   8525  C  CG2 . ILE H  1 99  ? 40.826 -35.794 -9.433   1.00 37.69 ? 99   ILE I CG2 1 
ATOM   8526  C  CD1 . ILE H  1 99  ? 43.319 -34.791 -7.790   1.00 38.17 ? 99   ILE I CD1 1 
ATOM   8527  N  N   . GLU H  1 100 ? 40.221 -38.010 -11.525  1.00 36.11 ? 100  GLU I N   1 
ATOM   8528  C  CA  . GLU H  1 100 ? 39.095 -37.853 -12.438  1.00 35.08 ? 100  GLU I CA  1 
ATOM   8529  C  C   . GLU H  1 100 ? 38.025 -37.131 -11.634  1.00 33.99 ? 100  GLU I C   1 
ATOM   8530  O  O   . GLU H  1 100 ? 37.623 -37.610 -10.566  1.00 33.38 ? 100  GLU I O   1 
ATOM   8531  C  CB  . GLU H  1 100 ? 38.570 -39.224 -12.881  1.00 35.28 ? 100  GLU I CB  1 
ATOM   8532  C  CG  . GLU H  1 100 ? 37.836 -39.229 -14.220  1.00 37.20 ? 100  GLU I CG  1 
ATOM   8533  C  CD  . GLU H  1 100 ? 38.683 -39.785 -15.363  1.00 38.83 ? 100  GLU I CD  1 
ATOM   8534  O  OE1 . GLU H  1 100 ? 39.724 -39.181 -15.706  1.00 38.50 ? 100  GLU I OE1 1 
ATOM   8535  O  OE2 . GLU H  1 100 ? 38.300 -40.841 -15.920  1.00 39.97 ? 100  GLU I OE2 1 
ATOM   8536  N  N   . ASP H  1 101 ? 37.573 -35.977 -12.112  1.00 32.36 ? 101  ASP I N   1 
ATOM   8537  C  CA  . ASP H  1 101 ? 36.592 -35.211 -11.347  1.00 31.47 ? 101  ASP I CA  1 
ATOM   8538  C  C   . ASP H  1 101 ? 35.449 -34.771 -12.226  1.00 30.92 ? 101  ASP I C   1 
ATOM   8539  O  O   . ASP H  1 101 ? 35.652 -34.450 -13.391  1.00 31.04 ? 101  ASP I O   1 
ATOM   8540  C  CB  . ASP H  1 101 ? 37.232 -34.008 -10.650  1.00 31.13 ? 101  ASP I CB  1 
ATOM   8541  C  CG  . ASP H  1 101 ? 36.432 -33.540 -9.450   1.00 31.45 ? 101  ASP I CG  1 
ATOM   8542  O  OD1 . ASP H  1 101 ? 35.767 -32.485 -9.540   1.00 27.95 ? 101  ASP I OD1 1 
ATOM   8543  O  OD2 . ASP H  1 101 ? 36.441 -34.246 -8.414   1.00 32.18 ? 101  ASP I OD2 1 
ATOM   8544  N  N   . SER H  1 102 ? 34.246 -34.760 -11.660  1.00 30.25 ? 102  SER I N   1 
ATOM   8545  C  CA  . SER H  1 102 ? 33.028 -34.459 -12.420  1.00 29.46 ? 102  SER I CA  1 
ATOM   8546  C  C   . SER H  1 102 ? 32.342 -33.200 -11.917  1.00 28.59 ? 102  SER I C   1 
ATOM   8547  O  O   . SER H  1 102 ? 31.216 -32.889 -12.325  1.00 28.14 ? 102  SER I O   1 
ATOM   8548  C  CB  . SER H  1 102 ? 32.053 -35.638 -12.335  1.00 29.88 ? 102  SER I CB  1 
ATOM   8549  O  OG  . SER H  1 102 ? 32.582 -36.774 -12.999  1.00 30.93 ? 102  SER I OG  1 
ATOM   8550  N  N   . VAL H  1 103 ? 33.017 -32.490 -11.013  1.00 27.66 ? 103  VAL I N   1 
ATOM   8551  C  CA  . VAL H  1 103 ? 32.508 -31.222 -10.480  1.00 26.67 ? 103  VAL I CA  1 
ATOM   8552  C  C   . VAL H  1 103 ? 33.267 -30.010 -11.059  1.00 25.92 ? 103  VAL I C   1 
ATOM   8553  O  O   . VAL H  1 103 ? 32.644 -29.012 -11.430  1.00 25.34 ? 103  VAL I O   1 
ATOM   8554  C  CB  . VAL H  1 103 ? 32.494 -31.198 -8.926   1.00 26.78 ? 103  VAL I CB  1 
ATOM   8555  C  CG1 . VAL H  1 103 ? 31.949 -29.867 -8.419   1.00 26.89 ? 103  VAL I CG1 1 
ATOM   8556  C  CG2 . VAL H  1 103 ? 31.635 -32.343 -8.402   1.00 26.64 ? 103  VAL I CG2 1 
ATOM   8557  N  N   . ILE H  1 104 ? 34.597 -30.108 -11.125  1.00 24.77 ? 104  ILE I N   1 
ATOM   8558  C  CA  . ILE H  1 104 ? 35.413 -29.084 -11.788  1.00 23.71 ? 104  ILE I CA  1 
ATOM   8559  C  C   . ILE H  1 104 ? 35.194 -29.154 -13.301  1.00 23.06 ? 104  ILE I C   1 
ATOM   8560  O  O   . ILE H  1 104 ? 34.875 -30.212 -13.851  1.00 22.81 ? 104  ILE I O   1 
ATOM   8561  C  CB  . ILE H  1 104 ? 36.945 -29.205 -11.468  1.00 23.60 ? 104  ILE I CB  1 
ATOM   8562  C  CG1 . ILE H  1 104 ? 37.502 -30.562 -11.926  1.00 23.23 ? 104  ILE I CG1 1 
ATOM   8563  C  CG2 . ILE H  1 104 ? 37.237 -28.887 -9.974   1.00 23.85 ? 104  ILE I CG2 1 
ATOM   8564  C  CD1 . ILE H  1 104 ? 39.019 -30.614 -12.071  1.00 20.21 ? 104  ILE I CD1 1 
ATOM   8565  N  N   . SER H  1 105 ? 35.326 -28.022 -13.969  1.00 22.02 ? 105  SER I N   1 
ATOM   8566  C  CA  . SER H  1 105 ? 35.198 -28.003 -15.422  1.00 21.54 ? 105  SER I CA  1 
ATOM   8567  C  C   . SER H  1 105 ? 36.185 -27.009 -16.008  1.00 21.39 ? 105  SER I C   1 
ATOM   8568  O  O   . SER H  1 105 ? 36.606 -26.070 -15.319  1.00 21.04 ? 105  SER I O   1 
ATOM   8569  C  CB  . SER H  1 105 ? 33.771 -27.636 -15.832  1.00 21.18 ? 105  SER I CB  1 
ATOM   8570  O  OG  . SER H  1 105 ? 33.562 -27.900 -17.216  1.00 21.71 ? 105  SER I OG  1 
ATOM   8571  N  N   . LEU H  1 106 ? 36.539 -27.227 -17.272  1.00 21.17 ? 106  LEU I N   1 
ATOM   8572  C  CA  . LEU H  1 106 ? 37.427 -26.320 -18.007  1.00 20.80 ? 106  LEU I CA  1 
ATOM   8573  C  C   . LEU H  1 106 ? 36.636 -25.318 -18.840  1.00 21.29 ? 106  LEU I C   1 
ATOM   8574  O  O   . LEU H  1 106 ? 37.211 -24.517 -19.581  1.00 20.35 ? 106  LEU I O   1 
ATOM   8575  C  CB  . LEU H  1 106 ? 38.416 -27.102 -18.884  1.00 20.13 ? 106  LEU I CB  1 
ATOM   8576  C  CG  . LEU H  1 106 ? 39.299 -28.138 -18.163  1.00 19.33 ? 106  LEU I CG  1 
ATOM   8577  C  CD1 . LEU H  1 106 ? 40.323 -28.741 -19.115  1.00 17.19 ? 106  LEU I CD1 1 
ATOM   8578  C  CD2 . LEU H  1 106 ? 39.994 -27.539 -16.899  1.00 18.90 ? 106  LEU I CD2 1 
ATOM   8579  N  N   . SER H  1 107 ? 35.316 -25.355 -18.703  1.00 22.02 ? 107  SER I N   1 
ATOM   8580  C  CA  . SER H  1 107 ? 34.465 -24.375 -19.363  1.00 22.96 ? 107  SER I CA  1 
ATOM   8581  C  C   . SER H  1 107 ? 33.190 -24.111 -18.566  1.00 24.17 ? 107  SER I C   1 
ATOM   8582  O  O   . SER H  1 107 ? 32.981 -24.681 -17.488  1.00 23.91 ? 107  SER I O   1 
ATOM   8583  C  CB  . SER H  1 107 ? 34.141 -24.815 -20.793  1.00 23.19 ? 107  SER I CB  1 
ATOM   8584  O  OG  . SER H  1 107 ? 33.287 -25.935 -20.779  1.00 22.64 ? 107  SER I OG  1 
ATOM   8585  N  N   . GLY H  1 108 ? 32.340 -23.243 -19.102  1.00 25.62 ? 108  GLY I N   1 
ATOM   8586  C  CA  . GLY H  1 108 ? 31.096 -22.900 -18.444  1.00 27.24 ? 108  GLY I CA  1 
ATOM   8587  C  C   . GLY H  1 108 ? 31.324 -21.847 -17.387  1.00 28.51 ? 108  GLY I C   1 
ATOM   8588  O  O   . GLY H  1 108 ? 32.462 -21.624 -16.952  1.00 28.90 ? 108  GLY I O   1 
ATOM   8589  N  N   . ASP H  1 109 ? 30.237 -21.208 -16.961  1.00 29.29 ? 109  ASP I N   1 
ATOM   8590  C  CA  . ASP H  1 109 ? 30.345 -20.021 -16.115  1.00 30.29 ? 109  ASP I CA  1 
ATOM   8591  C  C   . ASP H  1 109 ? 30.992 -20.265 -14.740  1.00 30.21 ? 109  ASP I C   1 
ATOM   8592  O  O   . ASP H  1 109 ? 31.217 -19.311 -13.986  1.00 30.61 ? 109  ASP I O   1 
ATOM   8593  C  CB  . ASP H  1 109 ? 29.005 -19.264 -16.014  1.00 30.70 ? 109  ASP I CB  1 
ATOM   8594  C  CG  . ASP H  1 109 ? 27.838 -20.157 -15.617  1.00 32.13 ? 109  ASP I CG  1 
ATOM   8595  O  OD1 . ASP H  1 109 ? 28.010 -21.068 -14.779  1.00 33.65 ? 109  ASP I OD1 1 
ATOM   8596  O  OD2 . ASP H  1 109 ? 26.726 -19.929 -16.144  1.00 35.51 ? 109  ASP I OD2 1 
ATOM   8597  N  N   . HIS H  1 110 ? 31.311 -21.529 -14.439  1.00 29.85 ? 110  HIS I N   1 
ATOM   8598  C  CA  . HIS H  1 110 ? 32.058 -21.881 -13.217  1.00 29.53 ? 110  HIS I CA  1 
ATOM   8599  C  C   . HIS H  1 110 ? 33.347 -22.688 -13.498  1.00 28.69 ? 110  HIS I C   1 
ATOM   8600  O  O   . HIS H  1 110 ? 33.739 -23.547 -12.706  1.00 29.31 ? 110  HIS I O   1 
ATOM   8601  C  CB  . HIS H  1 110 ? 31.165 -22.611 -12.202  1.00 29.82 ? 110  HIS I CB  1 
ATOM   8602  C  CG  . HIS H  1 110 ? 29.981 -21.814 -11.739  1.00 31.36 ? 110  HIS I CG  1 
ATOM   8603  N  ND1 . HIS H  1 110 ? 28.754 -22.387 -11.482  1.00 32.06 ? 110  HIS I ND1 1 
ATOM   8604  C  CD2 . HIS H  1 110 ? 29.834 -20.489 -11.491  1.00 33.44 ? 110  HIS I CD2 1 
ATOM   8605  C  CE1 . HIS H  1 110 ? 27.902 -21.452 -11.097  1.00 33.09 ? 110  HIS I CE1 1 
ATOM   8606  N  NE2 . HIS H  1 110 ? 28.532 -20.291 -11.094  1.00 34.02 ? 110  HIS I NE2 1 
HETATM 8607  N  N   . CME H  1 111 ? 34.006 -22.400 -14.616  1.00 27.78 ? 111  CME I N   1 
HETATM 8608  C  CA  . CME H  1 111 ? 35.279 -23.045 -14.956  1.00 26.69 ? 111  CME I CA  1 
HETATM 8609  C  CB  . CME H  1 111 ? 35.625 -22.749 -16.424  1.00 27.39 ? 111  CME I CB  1 
HETATM 8610  S  SG  . CME H  1 111 ? 36.453 -21.201 -16.594  1.00 29.59 ? 111  CME I SG  1 
HETATM 8611  S  SD  . CME H  1 111 ? 36.625 -20.756 -18.562  1.00 30.68 ? 111  CME I SD  1 
HETATM 8612  C  CE  . CME H  1 111 ? 34.961 -20.593 -19.150  1.00 34.89 ? 111  CME I CE  1 
HETATM 8613  C  CZ  . CME H  1 111 ? 34.202 -19.456 -18.467  1.00 36.70 ? 111  CME I CZ  1 
HETATM 8614  O  OH  . CME H  1 111 ? 34.879 -18.205 -18.667  1.00 39.81 ? 111  CME I OH  1 
HETATM 8615  C  C   . CME H  1 111 ? 36.404 -22.647 -14.022  1.00 25.73 ? 111  CME I C   1 
HETATM 8616  O  O   . CME H  1 111 ? 36.325 -21.604 -13.337  1.00 25.03 ? 111  CME I O   1 
ATOM   8617  N  N   . ILE H  1 112 ? 37.462 -23.459 -14.000  1.00 24.07 ? 112  ILE I N   1 
ATOM   8618  C  CA  . ILE H  1 112 ? 38.626 -23.214 -13.139  1.00 23.58 ? 112  ILE I CA  1 
ATOM   8619  C  C   . ILE H  1 112 ? 39.810 -22.555 -13.860  1.00 23.38 ? 112  ILE I C   1 
ATOM   8620  O  O   . ILE H  1 112 ? 40.874 -22.346 -13.260  1.00 23.81 ? 112  ILE I O   1 
ATOM   8621  C  CB  . ILE H  1 112 ? 39.118 -24.515 -12.451  1.00 23.77 ? 112  ILE I CB  1 
ATOM   8622  C  CG1 . ILE H  1 112 ? 39.757 -25.466 -13.485  1.00 23.80 ? 112  ILE I CG1 1 
ATOM   8623  C  CG2 . ILE H  1 112 ? 37.963 -25.186 -11.698  1.00 23.35 ? 112  ILE I CG2 1 
ATOM   8624  C  CD1 . ILE H  1 112 ? 40.418 -26.701 -12.888  1.00 20.67 ? 112  ILE I CD1 1 
ATOM   8625  N  N   . ILE H  1 113 ? 39.637 -22.255 -15.144  1.00 22.98 ? 113  ILE I N   1 
ATOM   8626  C  CA  . ILE H  1 113 ? 40.648 -21.548 -15.925  1.00 21.76 ? 113  ILE I CA  1 
ATOM   8627  C  C   . ILE H  1 113 ? 40.898 -20.174 -15.285  1.00 21.50 ? 113  ILE I C   1 
ATOM   8628  O  O   . ILE H  1 113 ? 39.939 -19.437 -14.996  1.00 21.04 ? 113  ILE I O   1 
ATOM   8629  C  CB  . ILE H  1 113 ? 40.179 -21.358 -17.412  1.00 22.62 ? 113  ILE I CB  1 
ATOM   8630  C  CG1 . ILE H  1 113 ? 40.008 -22.705 -18.135  1.00 22.60 ? 113  ILE I CG1 1 
ATOM   8631  C  CG2 . ILE H  1 113 ? 41.145 -20.467 -18.182  1.00 20.96 ? 113  ILE I CG2 1 
ATOM   8632  C  CD1 . ILE H  1 113 ? 41.295 -23.505 -18.279  1.00 24.21 ? 113  ILE I CD1 1 
ATOM   8633  N  N   . GLY H  1 114 ? 42.167 -19.843 -15.048  1.00 20.63 ? 114  GLY I N   1 
ATOM   8634  C  CA  . GLY H  1 114 ? 42.524 -18.539 -14.471  1.00 21.13 ? 114  GLY I CA  1 
ATOM   8635  C  C   . GLY H  1 114 ? 42.335 -18.421 -12.964  1.00 21.56 ? 114  GLY I C   1 
ATOM   8636  O  O   . GLY H  1 114 ? 42.456 -17.329 -12.377  1.00 21.16 ? 114  GLY I O   1 
ATOM   8637  N  N   . ARG H  1 115 ? 42.014 -19.548 -12.339  1.00 21.68 ? 115  ARG I N   1 
ATOM   8638  C  CA  . ARG H  1 115 ? 41.992 -19.649 -10.889  1.00 22.01 ? 115  ARG I CA  1 
ATOM   8639  C  C   . ARG H  1 115 ? 43.311 -20.274 -10.459  1.00 22.54 ? 115  ARG I C   1 
ATOM   8640  O  O   . ARG H  1 115 ? 44.157 -20.587 -11.309  1.00 22.35 ? 115  ARG I O   1 
ATOM   8641  C  CB  . ARG H  1 115 ? 40.788 -20.475 -10.430  1.00 21.91 ? 115  ARG I CB  1 
ATOM   8642  C  CG  . ARG H  1 115 ? 39.529 -20.037 -11.139  1.00 21.41 ? 115  ARG I CG  1 
ATOM   8643  C  CD  . ARG H  1 115 ? 38.299 -20.221 -10.346  1.00 21.36 ? 115  ARG I CD  1 
ATOM   8644  N  NE  . ARG H  1 115 ? 37.184 -19.545 -11.001  1.00 22.70 ? 115  ARG I NE  1 
ATOM   8645  C  CZ  . ARG H  1 115 ? 36.653 -18.391 -10.604  1.00 20.96 ? 115  ARG I CZ  1 
ATOM   8646  N  NH1 . ARG H  1 115 ? 35.634 -17.880 -11.268  1.00 22.63 ? 115  ARG I NH1 1 
ATOM   8647  N  NH2 . ARG H  1 115 ? 37.102 -17.773 -9.525   1.00 21.93 ? 115  ARG I NH2 1 
ATOM   8648  N  N   . THR H  1 116 ? 43.501 -20.432 -9.150   1.00 23.00 ? 116  THR I N   1 
ATOM   8649  C  CA  . THR H  1 116 ? 44.755 -20.954 -8.625   1.00 24.09 ? 116  THR I CA  1 
ATOM   8650  C  C   . THR H  1 116 ? 44.621 -22.372 -8.066   1.00 24.89 ? 116  THR I C   1 
ATOM   8651  O  O   . THR H  1 116 ? 43.726 -22.648 -7.260   1.00 24.88 ? 116  THR I O   1 
ATOM   8652  C  CB  . THR H  1 116 ? 45.335 -20.024 -7.525   1.00 24.17 ? 116  THR I CB  1 
ATOM   8653  O  OG1 . THR H  1 116 ? 45.674 -18.758 -8.095   1.00 22.84 ? 116  THR I OG1 1 
ATOM   8654  C  CG2 . THR H  1 116 ? 46.593 -20.617 -6.911   1.00 24.87 ? 116  THR I CG2 1 
ATOM   8655  N  N   . LEU H  1 117 ? 45.523 -23.247 -8.511   1.00 25.80 ? 117  LEU I N   1 
ATOM   8656  C  CA  . LEU H  1 117 ? 45.716 -24.572 -7.935   1.00 27.02 ? 117  LEU I CA  1 
ATOM   8657  C  C   . LEU H  1 117 ? 46.758 -24.491 -6.814   1.00 27.93 ? 117  LEU I C   1 
ATOM   8658  O  O   . LEU H  1 117 ? 47.837 -23.917 -7.008   1.00 27.76 ? 117  LEU I O   1 
ATOM   8659  C  CB  . LEU H  1 117 ? 46.201 -25.560 -9.003   1.00 26.87 ? 117  LEU I CB  1 
ATOM   8660  C  CG  . LEU H  1 117 ? 46.342 -27.017 -8.547   1.00 27.26 ? 117  LEU I CG  1 
ATOM   8661  C  CD1 . LEU H  1 117 ? 44.989 -27.611 -8.124   1.00 25.19 ? 117  LEU I CD1 1 
ATOM   8662  C  CD2 . LEU H  1 117 ? 47.006 -27.862 -9.637   1.00 26.52 ? 117  LEU I CD2 1 
ATOM   8663  N  N   . VAL H  1 118 ? 46.438 -25.081 -5.664   1.00 28.61 ? 118  VAL I N   1 
ATOM   8664  C  CA  . VAL H  1 118 ? 47.309 -25.050 -4.483   1.00 29.40 ? 118  VAL I CA  1 
ATOM   8665  C  C   . VAL H  1 118 ? 47.508 -26.459 -3.907   1.00 29.96 ? 118  VAL I C   1 
ATOM   8666  O  O   . VAL H  1 118 ? 46.551 -27.229 -3.820   1.00 29.85 ? 118  VAL I O   1 
ATOM   8667  C  CB  . VAL H  1 118 ? 46.708 -24.134 -3.374   1.00 29.29 ? 118  VAL I CB  1 
ATOM   8668  C  CG1 . VAL H  1 118 ? 47.467 -24.272 -2.075   1.00 29.46 ? 118  VAL I CG1 1 
ATOM   8669  C  CG2 . VAL H  1 118 ? 46.667 -22.659 -3.813   1.00 29.67 ? 118  VAL I CG2 1 
ATOM   8670  N  N   . VAL H  1 119 ? 48.743 -26.778 -3.507   1.00 30.84 ? 119  VAL I N   1 
ATOM   8671  C  CA  . VAL H  1 119 ? 49.039 -27.987 -2.699   1.00 31.77 ? 119  VAL I CA  1 
ATOM   8672  C  C   . VAL H  1 119 ? 49.517 -27.566 -1.289   1.00 32.76 ? 119  VAL I C   1 
ATOM   8673  O  O   . VAL H  1 119 ? 50.373 -26.684 -1.158   1.00 33.21 ? 119  VAL I O   1 
ATOM   8674  C  CB  . VAL H  1 119 ? 50.072 -28.925 -3.390   1.00 31.76 ? 119  VAL I CB  1 
ATOM   8675  C  CG1 . VAL H  1 119 ? 51.450 -28.252 -3.533   1.00 31.88 ? 119  VAL I CG1 1 
ATOM   8676  C  CG2 . VAL H  1 119 ? 50.202 -30.253 -2.638   1.00 31.85 ? 119  VAL I CG2 1 
ATOM   8677  N  N   . HIS H  1 120 ? 48.979 -28.194 -0.246   1.00 33.60 ? 120  HIS I N   1 
ATOM   8678  C  CA  . HIS H  1 120 ? 49.167 -27.694 1.122    1.00 34.47 ? 120  HIS I CA  1 
ATOM   8679  C  C   . HIS H  1 120 ? 50.232 -28.364 1.997    1.00 34.92 ? 120  HIS I C   1 
ATOM   8680  O  O   . HIS H  1 120 ? 50.737 -29.448 1.681    1.00 34.96 ? 120  HIS I O   1 
ATOM   8681  C  CB  . HIS H  1 120 ? 47.833 -27.683 1.868    1.00 34.56 ? 120  HIS I CB  1 
ATOM   8682  C  CG  . HIS H  1 120 ? 46.882 -26.638 1.382    1.00 34.45 ? 120  HIS I CG  1 
ATOM   8683  N  ND1 . HIS H  1 120 ? 46.632 -25.475 2.079    1.00 33.62 ? 120  HIS I ND1 1 
ATOM   8684  C  CD2 . HIS H  1 120 ? 46.110 -26.588 0.273    1.00 34.65 ? 120  HIS I CD2 1 
ATOM   8685  C  CE1 . HIS H  1 120 ? 45.745 -24.753 1.419    1.00 34.50 ? 120  HIS I CE1 1 
ATOM   8686  N  NE2 . HIS H  1 120 ? 45.415 -25.405 0.319    1.00 35.33 ? 120  HIS I NE2 1 
ATOM   8687  N  N   . GLU H  1 121 ? 50.543 -27.681 3.100    1.00 35.57 ? 121  GLU I N   1 
ATOM   8688  C  CA  . GLU H  1 121 ? 51.438 -28.143 4.162    1.00 36.40 ? 121  GLU I CA  1 
ATOM   8689  C  C   . GLU H  1 121 ? 50.986 -29.481 4.754    1.00 36.72 ? 121  GLU I C   1 
ATOM   8690  O  O   . GLU H  1 121 ? 51.813 -30.371 4.990    1.00 36.83 ? 121  GLU I O   1 
ATOM   8691  C  CB  . GLU H  1 121 ? 51.499 -27.072 5.267    1.00 36.55 ? 121  GLU I CB  1 
ATOM   8692  C  CG  . GLU H  1 121 ? 52.477 -27.319 6.430    1.00 37.46 ? 121  GLU I CG  1 
ATOM   8693  C  CD  . GLU H  1 121 ? 52.253 -26.367 7.619    1.00 38.50 ? 121  GLU I CD  1 
ATOM   8694  O  OE1 . GLU H  1 121 ? 53.034 -26.438 8.600    1.00 38.90 ? 121  GLU I OE1 1 
ATOM   8695  O  OE2 . GLU H  1 121 ? 51.297 -25.554 7.583    1.00 37.69 ? 121  GLU I OE2 1 
ATOM   8696  N  N   . LYS H  1 122 ? 49.680 -29.615 4.989    1.00 36.99 ? 122  LYS I N   1 
ATOM   8697  C  CA  . LYS H  1 122 ? 49.125 -30.794 5.675    1.00 37.59 ? 122  LYS I CA  1 
ATOM   8698  C  C   . LYS H  1 122 ? 47.914 -31.410 4.972    1.00 37.59 ? 122  LYS I C   1 
ATOM   8699  O  O   . LYS H  1 122 ? 47.417 -30.885 3.968    1.00 37.54 ? 122  LYS I O   1 
ATOM   8700  C  CB  . LYS H  1 122 ? 48.764 -30.453 7.129    1.00 37.58 ? 122  LYS I CB  1 
ATOM   8701  C  CG  . LYS H  1 122 ? 49.959 -30.405 8.068    1.00 38.52 ? 122  LYS I CG  1 
ATOM   8702  C  CD  . LYS H  1 122 ? 49.572 -29.975 9.481    1.00 39.77 ? 122  LYS I CD  1 
ATOM   8703  C  CE  . LYS H  1 122 ? 49.389 -28.459 9.585    1.00 40.34 ? 122  LYS I CE  1 
ATOM   8704  N  NZ  . LYS H  1 122 ? 49.631 -27.972 10.975   1.00 40.22 ? 122  LYS I NZ  1 
ATOM   8705  N  N   . ALA H  1 123 ? 47.450 -32.526 5.534    1.00 37.39 ? 123  ALA I N   1 
ATOM   8706  C  CA  . ALA H  1 123 ? 46.339 -33.298 5.003    1.00 37.44 ? 123  ALA I CA  1 
ATOM   8707  C  C   . ALA H  1 123 ? 45.003 -32.575 5.109    1.00 37.58 ? 123  ALA I C   1 
ATOM   8708  O  O   . ALA H  1 123 ? 44.659 -32.007 6.152    1.00 37.50 ? 123  ALA I O   1 
ATOM   8709  C  CB  . ALA H  1 123 ? 46.258 -34.650 5.709    1.00 37.54 ? 123  ALA I CB  1 
ATOM   8710  N  N   . ASP H  1 124 ? 44.264 -32.603 4.004    1.00 37.61 ? 124  ASP I N   1 
ATOM   8711  C  CA  . ASP H  1 124 ? 42.864 -32.205 3.966    1.00 37.71 ? 124  ASP I CA  1 
ATOM   8712  C  C   . ASP H  1 124 ? 42.084 -33.192 4.830    1.00 37.94 ? 124  ASP I C   1 
ATOM   8713  O  O   . ASP H  1 124 ? 42.087 -34.401 4.556    1.00 38.06 ? 124  ASP I O   1 
ATOM   8714  C  CB  . ASP H  1 124 ? 42.361 -32.263 2.515    1.00 37.30 ? 124  ASP I CB  1 
ATOM   8715  C  CG  . ASP H  1 124 ? 41.045 -31.520 2.301    1.00 36.97 ? 124  ASP I CG  1 
ATOM   8716  O  OD1 . ASP H  1 124 ? 40.776 -31.134 1.141    1.00 36.29 ? 124  ASP I OD1 1 
ATOM   8717  O  OD2 . ASP H  1 124 ? 40.279 -31.326 3.268    1.00 35.53 ? 124  ASP I OD2 1 
ATOM   8718  N  N   . ASP H  1 125 ? 41.425 -32.695 5.877    1.00 38.22 ? 125  ASP I N   1 
ATOM   8719  C  CA  . ASP H  1 125 ? 40.650 -33.590 6.745    1.00 38.43 ? 125  ASP I CA  1 
ATOM   8720  C  C   . ASP H  1 125 ? 39.254 -33.898 6.175    1.00 38.66 ? 125  ASP I C   1 
ATOM   8721  O  O   . ASP H  1 125 ? 38.394 -34.467 6.860    1.00 38.47 ? 125  ASP I O   1 
ATOM   8722  C  CB  . ASP H  1 125 ? 40.606 -33.080 8.197    1.00 38.42 ? 125  ASP I CB  1 
ATOM   8723  C  CG  . ASP H  1 125 ? 39.776 -31.816 8.373    1.00 38.82 ? 125  ASP I CG  1 
ATOM   8724  O  OD1 . ASP H  1 125 ? 40.009 -31.112 9.380    1.00 37.99 ? 125  ASP I OD1 1 
ATOM   8725  O  OD2 . ASP H  1 125 ? 38.898 -31.517 7.529    1.00 39.61 ? 125  ASP I OD2 1 
ATOM   8726  N  N   . LEU H  1 126 ? 39.056 -33.517 4.912    1.00 38.74 ? 126  LEU I N   1 
ATOM   8727  C  CA  . LEU H  1 126 ? 37.827 -33.782 4.146    1.00 39.12 ? 126  LEU I CA  1 
ATOM   8728  C  C   . LEU H  1 126 ? 36.550 -33.245 4.799    1.00 39.43 ? 126  LEU I C   1 
ATOM   8729  O  O   . LEU H  1 126 ? 35.462 -33.789 4.603    1.00 39.36 ? 126  LEU I O   1 
ATOM   8730  C  CB  . LEU H  1 126 ? 37.703 -35.272 3.790    1.00 39.07 ? 126  LEU I CB  1 
ATOM   8731  C  CG  . LEU H  1 126 ? 38.949 -35.945 3.205    1.00 39.23 ? 126  LEU I CG  1 
ATOM   8732  C  CD1 . LEU H  1 126 ? 38.694 -37.434 2.974    1.00 39.55 ? 126  LEU I CD1 1 
ATOM   8733  C  CD2 . LEU H  1 126 ? 39.404 -35.265 1.913    1.00 40.09 ? 126  LEU I CD2 1 
ATOM   8734  N  N   . GLY H  1 127 ? 36.691 -32.167 5.567    1.00 39.91 ? 127  GLY I N   1 
ATOM   8735  C  CA  . GLY H  1 127 ? 35.547 -31.529 6.214    1.00 40.78 ? 127  GLY I CA  1 
ATOM   8736  C  C   . GLY H  1 127 ? 34.955 -32.341 7.355    1.00 41.47 ? 127  GLY I C   1 
ATOM   8737  O  O   . GLY H  1 127 ? 33.822 -32.091 7.773    1.00 41.38 ? 127  GLY I O   1 
ATOM   8738  N  N   . LYS H  1 128 ? 35.724 -33.308 7.856    1.00 42.08 ? 128  LYS I N   1 
ATOM   8739  C  CA  . LYS H  1 128 ? 35.286 -34.179 8.955    1.00 42.93 ? 128  LYS I CA  1 
ATOM   8740  C  C   . LYS H  1 128 ? 36.256 -34.113 10.143   1.00 43.35 ? 128  LYS I C   1 
ATOM   8741  O  O   . LYS H  1 128 ? 36.717 -35.145 10.648   1.00 43.55 ? 128  LYS I O   1 
ATOM   8742  C  CB  . LYS H  1 128 ? 35.128 -35.626 8.466    1.00 42.95 ? 128  LYS I CB  1 
ATOM   8743  C  CG  . LYS H  1 128 ? 34.147 -35.806 7.319    1.00 43.51 ? 128  LYS I CG  1 
ATOM   8744  C  CD  . LYS H  1 128 ? 34.172 -37.241 6.797    1.00 44.29 ? 128  LYS I CD  1 
ATOM   8745  C  CE  . LYS H  1 128 ? 33.515 -37.349 5.432    1.00 44.80 ? 128  LYS I CE  1 
ATOM   8746  N  NZ  . LYS H  1 128 ? 32.066 -36.999 5.471    1.00 45.48 ? 128  LYS I NZ  1 
ATOM   8747  N  N   . GLY H  1 129 ? 36.559 -32.894 10.582   1.00 43.82 ? 129  GLY I N   1 
ATOM   8748  C  CA  . GLY H  1 129 ? 37.496 -32.667 11.683   1.00 44.27 ? 129  GLY I CA  1 
ATOM   8749  C  C   . GLY H  1 129 ? 36.803 -32.227 12.958   1.00 44.62 ? 129  GLY I C   1 
ATOM   8750  O  O   . GLY H  1 129 ? 37.423 -32.187 14.025   1.00 44.97 ? 129  GLY I O   1 
ATOM   8751  N  N   . GLY H  1 130 ? 35.518 -31.892 12.840   1.00 44.71 ? 130  GLY I N   1 
ATOM   8752  C  CA  . GLY H  1 130 ? 34.684 -31.533 13.983   1.00 44.89 ? 130  GLY I CA  1 
ATOM   8753  C  C   . GLY H  1 130 ? 34.871 -30.127 14.528   1.00 45.08 ? 130  GLY I C   1 
ATOM   8754  O  O   . GLY H  1 130 ? 34.442 -29.839 15.648   1.00 45.14 ? 130  GLY I O   1 
ATOM   8755  N  N   . ASN H  1 131 ? 35.505 -29.249 13.749   1.00 45.19 ? 131  ASN I N   1 
ATOM   8756  C  CA  . ASN H  1 131 ? 35.710 -27.847 14.157   1.00 45.27 ? 131  ASN I CA  1 
ATOM   8757  C  C   . ASN H  1 131 ? 35.442 -26.836 13.037   1.00 45.29 ? 131  ASN I C   1 
ATOM   8758  O  O   . ASN H  1 131 ? 35.317 -27.215 11.868   1.00 45.30 ? 131  ASN I O   1 
ATOM   8759  C  CB  . ASN H  1 131 ? 37.114 -27.637 14.752   1.00 45.21 ? 131  ASN I CB  1 
ATOM   8760  C  CG  . ASN H  1 131 ? 38.237 -27.944 13.763   1.00 45.08 ? 131  ASN I CG  1 
ATOM   8761  O  OD1 . ASN H  1 131 ? 38.100 -27.752 12.551   1.00 45.17 ? 131  ASN I OD1 1 
ATOM   8762  N  ND2 . ASN H  1 131 ? 39.365 -28.414 14.287   1.00 44.42 ? 131  ASN I ND2 1 
ATOM   8763  N  N   . GLU H  1 132 ? 35.376 -25.555 13.402   1.00 45.18 ? 132  GLU I N   1 
ATOM   8764  C  CA  . GLU H  1 132 ? 35.072 -24.483 12.448   1.00 45.05 ? 132  GLU I CA  1 
ATOM   8765  C  C   . GLU H  1 132 ? 35.976 -24.447 11.208   1.00 44.51 ? 132  GLU I C   1 
ATOM   8766  O  O   . GLU H  1 132 ? 35.492 -24.226 10.094   1.00 44.39 ? 132  GLU I O   1 
ATOM   8767  C  CB  . GLU H  1 132 ? 35.048 -23.113 13.140   1.00 45.40 ? 132  GLU I CB  1 
ATOM   8768  C  CG  . GLU H  1 132 ? 33.654 -22.488 13.205   1.00 46.33 ? 132  GLU I CG  1 
ATOM   8769  C  CD  . GLU H  1 132 ? 33.046 -22.272 11.823   1.00 47.74 ? 132  GLU I CD  1 
ATOM   8770  O  OE1 . GLU H  1 132 ? 33.647 -21.523 11.019   1.00 48.00 ? 132  GLU I OE1 1 
ATOM   8771  O  OE2 . GLU H  1 132 ? 31.972 -22.854 11.541   1.00 47.82 ? 132  GLU I OE2 1 
ATOM   8772  N  N   . GLU H  1 133 ? 37.274 -24.667 11.403   1.00 43.83 ? 133  GLU I N   1 
ATOM   8773  C  CA  . GLU H  1 133 ? 38.223 -24.641 10.292   1.00 43.26 ? 133  GLU I CA  1 
ATOM   8774  C  C   . GLU H  1 133 ? 37.996 -25.730 9.241    1.00 42.75 ? 133  GLU I C   1 
ATOM   8775  O  O   . GLU H  1 133 ? 38.205 -25.501 8.048    1.00 42.59 ? 133  GLU I O   1 
ATOM   8776  C  CB  . GLU H  1 133 ? 39.668 -24.680 10.796   1.00 43.38 ? 133  GLU I CB  1 
ATOM   8777  C  CG  . GLU H  1 133 ? 40.355 -23.319 10.827   1.00 43.57 ? 133  GLU I CG  1 
ATOM   8778  C  CD  . GLU H  1 133 ? 40.454 -22.662 9.452    1.00 43.64 ? 133  GLU I CD  1 
ATOM   8779  O  OE1 . GLU H  1 133 ? 41.582 -22.518 8.940    1.00 43.05 ? 133  GLU I OE1 1 
ATOM   8780  O  OE2 . GLU H  1 133 ? 39.407 -22.283 8.884    1.00 43.76 ? 133  GLU I OE2 1 
ATOM   8781  N  N   . SER H  1 134 ? 37.565 -26.906 9.695    1.00 41.78 ? 134  SER I N   1 
ATOM   8782  C  CA  . SER H  1 134 ? 37.344 -28.061 8.825    1.00 41.00 ? 134  SER I CA  1 
ATOM   8783  C  C   . SER H  1 134 ? 36.261 -27.835 7.763    1.00 40.47 ? 134  SER I C   1 
ATOM   8784  O  O   . SER H  1 134 ? 36.352 -28.376 6.661    1.00 40.10 ? 134  SER I O   1 
ATOM   8785  C  CB  . SER H  1 134 ? 36.999 -29.282 9.680    1.00 41.19 ? 134  SER I CB  1 
ATOM   8786  O  OG  . SER H  1 134 ? 36.889 -30.451 8.895    1.00 41.23 ? 134  SER I OG  1 
ATOM   8787  N  N   . THR H  1 135 ? 35.245 -27.040 8.105    1.00 39.99 ? 135  THR I N   1 
ATOM   8788  C  CA  . THR H  1 135 ? 34.131 -26.741 7.199    1.00 39.68 ? 135  THR I CA  1 
ATOM   8789  C  C   . THR H  1 135 ? 34.507 -25.686 6.153    1.00 39.43 ? 135  THR I C   1 
ATOM   8790  O  O   . THR H  1 135 ? 33.743 -25.431 5.214    1.00 39.42 ? 135  THR I O   1 
ATOM   8791  C  CB  . THR H  1 135 ? 32.864 -26.244 7.951    1.00 39.85 ? 135  THR I CB  1 
ATOM   8792  O  OG1 . THR H  1 135 ? 33.029 -24.871 8.334    1.00 39.79 ? 135  THR I OG1 1 
ATOM   8793  C  CG2 . THR H  1 135 ? 32.559 -27.106 9.185    1.00 39.76 ? 135  THR I CG2 1 
ATOM   8794  N  N   . LYS H  1 136 ? 35.675 -25.072 6.323    1.00 39.12 ? 136  LYS I N   1 
ATOM   8795  C  CA  . LYS H  1 136 ? 36.146 -24.043 5.394    1.00 38.79 ? 136  LYS I CA  1 
ATOM   8796  C  C   . LYS H  1 136 ? 37.414 -24.462 4.653    1.00 38.15 ? 136  LYS I C   1 
ATOM   8797  O  O   . LYS H  1 136 ? 37.449 -24.451 3.423    1.00 38.47 ? 136  LYS I O   1 
ATOM   8798  C  CB  . LYS H  1 136 ? 36.375 -22.701 6.112    1.00 39.15 ? 136  LYS I CB  1 
ATOM   8799  C  CG  . LYS H  1 136 ? 35.120 -22.051 6.696    1.00 39.98 ? 136  LYS I CG  1 
ATOM   8800  C  CD  . LYS H  1 136 ? 35.362 -20.578 7.033    1.00 42.33 ? 136  LYS I CD  1 
ATOM   8801  C  CE  . LYS H  1 136 ? 36.320 -20.386 8.209    1.00 42.28 ? 136  LYS I CE  1 
ATOM   8802  N  NZ  . LYS H  1 136 ? 35.594 -20.198 9.490    1.00 43.85 ? 136  LYS I NZ  1 
ATOM   8803  N  N   . THR H  1 137 ? 38.447 -24.838 5.402    1.00 37.07 ? 137  THR I N   1 
ATOM   8804  C  CA  . THR H  1 137 ? 39.783 -25.036 4.834    1.00 36.22 ? 137  THR I CA  1 
ATOM   8805  C  C   . THR H  1 137 ? 40.241 -26.489 4.864    1.00 35.71 ? 137  THR I C   1 
ATOM   8806  O  O   . THR H  1 137 ? 41.289 -26.826 4.303    1.00 35.13 ? 137  THR I O   1 
ATOM   8807  C  CB  . THR H  1 137 ? 40.831 -24.197 5.589    1.00 36.45 ? 137  THR I CB  1 
ATOM   8808  O  OG1 . THR H  1 137 ? 40.964 -24.699 6.928    1.00 36.22 ? 137  THR I OG1 1 
ATOM   8809  C  CG2 . THR H  1 137 ? 40.435 -22.714 5.619    1.00 35.54 ? 137  THR I CG2 1 
ATOM   8810  N  N   . GLY H  1 138 ? 39.461 -27.334 5.541    1.00 35.39 ? 138  GLY I N   1 
ATOM   8811  C  CA  . GLY H  1 138 ? 39.817 -28.740 5.746    1.00 35.45 ? 138  GLY I CA  1 
ATOM   8812  C  C   . GLY H  1 138 ? 41.012 -28.962 6.663    1.00 35.43 ? 138  GLY I C   1 
ATOM   8813  O  O   . GLY H  1 138 ? 41.474 -30.095 6.814    1.00 35.69 ? 138  GLY I O   1 
ATOM   8814  N  N   . ASN H  1 139 ? 41.509 -27.878 7.269    1.00 35.33 ? 139  ASN I N   1 
ATOM   8815  C  CA  . ASN H  1 139 ? 42.678 -27.896 8.175    1.00 35.06 ? 139  ASN I CA  1 
ATOM   8816  C  C   . ASN H  1 139 ? 44.012 -28.273 7.506    1.00 35.05 ? 139  ASN I C   1 
ATOM   8817  O  O   . ASN H  1 139 ? 44.937 -28.767 8.165    1.00 34.95 ? 139  ASN I O   1 
ATOM   8818  C  CB  . ASN H  1 139 ? 42.405 -28.768 9.417    1.00 35.06 ? 139  ASN I CB  1 
ATOM   8819  C  CG  . ASN H  1 139 ? 41.396 -28.141 10.356   1.00 34.74 ? 139  ASN I CG  1 
ATOM   8820  O  OD1 . ASN H  1 139 ? 41.609 -27.046 10.864   1.00 35.62 ? 139  ASN I OD1 1 
ATOM   8821  N  ND2 . ASN H  1 139 ? 40.293 -28.829 10.590   1.00 33.90 ? 139  ASN I ND2 1 
ATOM   8822  N  N   . ALA H  1 140 ? 44.117 -27.988 6.209    1.00 34.77 ? 140  ALA I N   1 
ATOM   8823  C  CA  . ALA H  1 140 ? 45.238 -28.468 5.398    1.00 34.84 ? 140  ALA I CA  1 
ATOM   8824  C  C   . ALA H  1 140 ? 46.565 -27.719 5.607    1.00 34.76 ? 140  ALA I C   1 
ATOM   8825  O  O   . ALA H  1 140 ? 47.609 -28.162 5.125    1.00 34.70 ? 140  ALA I O   1 
ATOM   8826  C  CB  . ALA H  1 140 ? 44.845 -28.510 3.907    1.00 34.69 ? 140  ALA I CB  1 
ATOM   8827  N  N   . GLY H  1 141 ? 46.529 -26.595 6.327    1.00 34.73 ? 141  GLY I N   1 
ATOM   8828  C  CA  . GLY H  1 141 ? 47.751 -25.846 6.641    1.00 34.52 ? 141  GLY I CA  1 
ATOM   8829  C  C   . GLY H  1 141 ? 48.153 -24.853 5.562    1.00 34.45 ? 141  GLY I C   1 
ATOM   8830  O  O   . GLY H  1 141 ? 47.338 -24.492 4.707    1.00 34.25 ? 141  GLY I O   1 
ATOM   8831  N  N   . SER H  1 142 ? 49.414 -24.422 5.599    1.00 34.35 ? 142  SER I N   1 
ATOM   8832  C  CA  . SER H  1 142 ? 49.920 -23.392 4.685    1.00 34.19 ? 142  SER I CA  1 
ATOM   8833  C  C   . SER H  1 142 ? 49.990 -23.878 3.232    1.00 33.90 ? 142  SER I C   1 
ATOM   8834  O  O   . SER H  1 142 ? 49.903 -25.077 2.963    1.00 34.11 ? 142  SER I O   1 
ATOM   8835  C  CB  . SER H  1 142 ? 51.289 -22.872 5.155    1.00 34.52 ? 142  SER I CB  1 
ATOM   8836  O  OG  . SER H  1 142 ? 52.348 -23.750 4.795    1.00 34.96 ? 142  SER I OG  1 
ATOM   8837  N  N   . ARG H  1 143 ? 50.149 -22.934 2.309    1.00 33.36 ? 143  ARG I N   1 
ATOM   8838  C  CA  . ARG H  1 143 ? 50.219 -23.223 0.874    1.00 32.56 ? 143  ARG I CA  1 
ATOM   8839  C  C   . ARG H  1 143 ? 51.690 -23.226 0.454    1.00 32.44 ? 143  ARG I C   1 
ATOM   8840  O  O   . ARG H  1 143 ? 52.366 -22.187 0.504    1.00 32.46 ? 143  ARG I O   1 
ATOM   8841  C  CB  . ARG H  1 143 ? 49.404 -22.183 0.093    1.00 32.25 ? 143  ARG I CB  1 
ATOM   8842  C  CG  . ARG H  1 143 ? 47.973 -22.020 0.607    1.00 31.36 ? 143  ARG I CG  1 
ATOM   8843  C  CD  . ARG H  1 143 ? 47.352 -20.673 0.256    1.00 30.72 ? 143  ARG I CD  1 
ATOM   8844  N  NE  . ARG H  1 143 ? 46.092 -20.463 0.976    1.00 29.26 ? 143  ARG I NE  1 
ATOM   8845  C  CZ  . ARG H  1 143 ? 45.171 -19.558 0.646    1.00 30.14 ? 143  ARG I CZ  1 
ATOM   8846  N  NH1 . ARG H  1 143 ? 44.055 -19.449 1.358    1.00 28.92 ? 143  ARG I NH1 1 
ATOM   8847  N  NH2 . ARG H  1 143 ? 45.355 -18.762 -0.402   1.00 28.76 ? 143  ARG I NH2 1 
ATOM   8848  N  N   . LEU H  1 144 ? 52.193 -24.398 0.073    1.00 31.85 ? 144  LEU I N   1 
ATOM   8849  C  CA  . LEU H  1 144 ? 53.629 -24.570 -0.201   1.00 31.63 ? 144  LEU I CA  1 
ATOM   8850  C  C   . LEU H  1 144 ? 53.983 -24.230 -1.643   1.00 31.03 ? 144  LEU I C   1 
ATOM   8851  O  O   . LEU H  1 144 ? 55.098 -23.768 -1.935   1.00 30.83 ? 144  LEU I O   1 
ATOM   8852  C  CB  . LEU H  1 144 ? 54.103 -25.996 0.135    1.00 32.17 ? 144  LEU I CB  1 
ATOM   8853  C  CG  . LEU H  1 144 ? 53.787 -26.663 1.485    1.00 32.49 ? 144  LEU I CG  1 
ATOM   8854  C  CD1 . LEU H  1 144 ? 54.445 -28.030 1.533    1.00 34.50 ? 144  LEU I CD1 1 
ATOM   8855  C  CD2 . LEU H  1 144 ? 54.236 -25.827 2.685    1.00 33.38 ? 144  LEU I CD2 1 
ATOM   8856  N  N   . ALA H  1 145 ? 53.024 -24.469 -2.537   1.00 30.38 ? 145  ALA I N   1 
ATOM   8857  C  CA  . ALA H  1 145 ? 53.173 -24.171 -3.956   1.00 29.49 ? 145  ALA I CA  1 
ATOM   8858  C  C   . ALA H  1 145 ? 51.818 -23.898 -4.616   1.00 28.81 ? 145  ALA I C   1 
ATOM   8859  O  O   . ALA H  1 145 ? 50.783 -24.460 -4.221   1.00 28.82 ? 145  ALA I O   1 
ATOM   8860  C  CB  . ALA H  1 145 ? 53.920 -25.298 -4.681   1.00 29.73 ? 145  ALA I CB  1 
ATOM   8861  N  N   . CYS H  1 146 ? 51.836 -23.014 -5.610   1.00 27.45 ? 146  CYS I N   1 
ATOM   8862  C  CA  . CYS H  1 146 ? 50.634 -22.683 -6.369   1.00 25.95 ? 146  CYS I CA  1 
ATOM   8863  C  C   . CYS H  1 146 ? 50.976 -22.207 -7.776   1.00 25.62 ? 146  CYS I C   1 
ATOM   8864  O  O   . CYS H  1 146 ? 52.143 -21.962 -8.095   1.00 26.36 ? 146  CYS I O   1 
ATOM   8865  C  CB  . CYS H  1 146 ? 49.785 -21.641 -5.634   0.40 25.48 ? 146  CYS I CB  1 
ATOM   8866  S  SG  . CYS H  1 146 ? 50.622 -20.095 -5.310   0.40 21.07 ? 146  CYS I SG  1 
ATOM   8867  N  N   . GLY H  1 147 ? 49.948 -22.096 -8.611   1.00 24.89 ? 147  GLY I N   1 
ATOM   8868  C  CA  . GLY H  1 147 ? 50.099 -21.638 -9.979   1.00 23.93 ? 147  GLY I CA  1 
ATOM   8869  C  C   . GLY H  1 147 ? 48.735 -21.389 -10.591  1.00 23.54 ? 147  GLY I C   1 
ATOM   8870  O  O   . GLY H  1 147 ? 47.724 -21.964 -10.156  1.00 23.23 ? 147  GLY I O   1 
ATOM   8871  N  N   . VAL H  1 148 ? 48.705 -20.542 -11.612  1.00 22.55 ? 148  VAL I N   1 
ATOM   8872  C  CA  . VAL H  1 148 ? 47.444 -20.174 -12.228  1.00 21.66 ? 148  VAL I CA  1 
ATOM   8873  C  C   . VAL H  1 148 ? 47.119 -21.234 -13.281  1.00 20.92 ? 148  VAL I C   1 
ATOM   8874  O  O   . VAL H  1 148 ? 48.010 -21.654 -14.037  1.00 20.41 ? 148  VAL I O   1 
ATOM   8875  C  CB  . VAL H  1 148 ? 47.508 -18.757 -12.865  1.00 21.61 ? 148  VAL I CB  1 
ATOM   8876  C  CG1 . VAL H  1 148 ? 46.116 -18.283 -13.235  1.00 20.92 ? 148  VAL I CG1 1 
ATOM   8877  C  CG2 . VAL H  1 148 ? 48.160 -17.752 -11.904  1.00 22.48 ? 148  VAL I CG2 1 
ATOM   8878  N  N   . ILE H  1 149 ? 45.863 -21.681 -13.312  1.00 20.18 ? 149  ILE I N   1 
ATOM   8879  C  CA  . ILE H  1 149 ? 45.436 -22.669 -14.301  1.00 19.89 ? 149  ILE I CA  1 
ATOM   8880  C  C   . ILE H  1 149 ? 45.202 -21.952 -15.633  1.00 20.27 ? 149  ILE I C   1 
ATOM   8881  O  O   . ILE H  1 149 ? 44.333 -21.098 -15.738  1.00 20.00 ? 149  ILE I O   1 
ATOM   8882  C  CB  . ILE H  1 149 ? 44.161 -23.428 -13.867  1.00 20.08 ? 149  ILE I CB  1 
ATOM   8883  C  CG1 . ILE H  1 149 ? 44.367 -24.072 -12.487  1.00 19.07 ? 149  ILE I CG1 1 
ATOM   8884  C  CG2 . ILE H  1 149 ? 43.794 -24.474 -14.910  1.00 19.50 ? 149  ILE I CG2 1 
ATOM   8885  C  CD1 . ILE H  1 149 ? 43.152 -24.009 -11.576  1.00 19.35 ? 149  ILE I CD1 1 
ATOM   8886  N  N   . GLY H  1 150 ? 45.999 -22.300 -16.634  1.00 20.21 ? 150  GLY I N   1 
ATOM   8887  C  CA  . GLY H  1 150 ? 45.967 -21.584 -17.911  1.00 21.62 ? 150  GLY I CA  1 
ATOM   8888  C  C   . GLY H  1 150 ? 45.544 -22.497 -19.039  1.00 22.34 ? 150  GLY I C   1 
ATOM   8889  O  O   . GLY H  1 150 ? 45.685 -23.719 -18.936  1.00 22.42 ? 150  GLY I O   1 
ATOM   8890  N  N   . ILE H  1 151 ? 45.031 -21.903 -20.115  1.00 22.97 ? 151  ILE I N   1 
ATOM   8891  C  CA  . ILE H  1 151 ? 44.597 -22.635 -21.307  1.00 24.25 ? 151  ILE I CA  1 
ATOM   8892  C  C   . ILE H  1 151 ? 45.825 -23.215 -22.022  1.00 25.14 ? 151  ILE I C   1 
ATOM   8893  O  O   . ILE H  1 151 ? 46.830 -22.530 -22.193  1.00 25.50 ? 151  ILE I O   1 
ATOM   8894  C  CB  . ILE H  1 151 ? 43.776 -21.695 -22.246  1.00 23.77 ? 151  ILE I CB  1 
ATOM   8895  C  CG1 . ILE H  1 151 ? 42.512 -21.208 -21.532  1.00 23.58 ? 151  ILE I CG1 1 
ATOM   8896  C  CG2 . ILE H  1 151 ? 43.402 -22.382 -23.558  1.00 24.81 ? 151  ILE I CG2 1 
ATOM   8897  C  CD1 . ILE H  1 151 ? 41.850 -19.991 -22.160  1.00 22.35 ? 151  ILE I CD1 1 
ATOM   8898  N  N   . ALA H  1 152 ? 45.761 -24.484 -22.417  1.00 25.89 ? 152  ALA I N   1 
ATOM   8899  C  CA  . ALA H  1 152 ? 46.901 -25.121 -23.080  1.00 26.73 ? 152  ALA I CA  1 
ATOM   8900  C  C   . ALA H  1 152 ? 46.496 -25.613 -24.459  1.00 27.64 ? 152  ALA I C   1 
ATOM   8901  O  O   . ALA H  1 152 ? 45.300 -25.723 -24.753  1.00 27.83 ? 152  ALA I O   1 
ATOM   8902  C  CB  . ALA H  1 152 ? 47.436 -26.286 -22.230  1.00 26.99 ? 152  ALA I CB  1 
ATOM   8903  N  N   . GLN H  1 153 ? 47.485 -25.908 -25.299  1.00 28.59 ? 153  GLN I N   1 
ATOM   8904  C  CA  . GLN H  1 153 ? 47.217 -26.361 -26.665  1.00 29.41 ? 153  GLN I CA  1 
ATOM   8905  C  C   . GLN H  1 153 ? 46.392 -27.647 -26.696  1.00 29.98 ? 153  GLN I C   1 
ATOM   8906  O  O   . GLN H  1 153 ? 46.879 -28.736 -26.374  1.00 30.20 ? 153  GLN I O   1 
ATOM   8907  C  CB  . GLN H  1 153 ? 48.506 -26.514 -27.482  1.00 29.43 ? 153  GLN I CB  1 
ATOM   8908  C  CG  . GLN H  1 153 ? 48.234 -26.892 -28.951  1.00 29.82 ? 153  GLN I CG  1 
ATOM   8909  C  CD  . GLN H  1 153 ? 49.415 -26.666 -29.880  1.00 32.06 ? 153  GLN I CD  1 
ATOM   8910  O  OE1 . GLN H  1 153 ? 49.237 -26.310 -31.052  1.00 33.04 ? 153  GLN I OE1 1 
ATOM   8911  N  NE2 . GLN H  1 153 ? 50.625 -26.882 -29.374  1.00 31.94 ? 153  GLN I NE2 1 
ATOM   8912  O  OXT . GLN H  1 153 ? 45.206 -27.608 -27.054  1.00 30.41 ? 153  GLN I OXT 1 
ATOM   8913  N  N   . ALA I  1 1   ? 38.790 23.676  -66.217  1.00 26.33 ? 1    ALA J N   1 
ATOM   8914  C  CA  . ALA I  1 1   ? 37.389 23.213  -65.989  1.00 25.88 ? 1    ALA J CA  1 
ATOM   8915  C  C   . ALA I  1 1   ? 36.851 22.374  -67.154  1.00 25.66 ? 1    ALA J C   1 
ATOM   8916  O  O   . ALA I  1 1   ? 37.022 22.729  -68.332  1.00 26.16 ? 1    ALA J O   1 
ATOM   8917  C  CB  . ALA I  1 1   ? 36.476 24.398  -65.722  1.00 25.89 ? 1    ALA J CB  1 
ATOM   8918  N  N   . THR I  1 2   ? 36.228 21.250  -66.814  1.00 24.75 ? 2    THR J N   1 
ATOM   8919  C  CA  . THR I  1 2   ? 35.463 20.460  -67.768  1.00 23.82 ? 2    THR J CA  1 
ATOM   8920  C  C   . THR I  1 2   ? 33.976 20.650  -67.459  1.00 22.92 ? 2    THR J C   1 
ATOM   8921  O  O   . THR I  1 2   ? 33.575 20.814  -66.299  1.00 21.96 ? 2    THR J O   1 
ATOM   8922  C  CB  . THR I  1 2   ? 35.861 18.962  -67.735  1.00 24.38 ? 2    THR J CB  1 
ATOM   8923  O  OG1 . THR I  1 2   ? 37.273 18.839  -67.924  1.00 24.83 ? 2    THR J OG1 1 
ATOM   8924  C  CG2 . THR I  1 2   ? 35.157 18.182  -68.836  1.00 24.20 ? 2    THR J CG2 1 
ATOM   8925  N  N   . LYS I  1 3   ? 33.169 20.664  -68.511  1.00 21.56 ? 3    LYS J N   1 
ATOM   8926  C  CA  . LYS I  1 3   ? 31.741 20.904  -68.395  1.00 20.88 ? 3    LYS J CA  1 
ATOM   8927  C  C   . LYS I  1 3   ? 31.065 19.813  -69.190  1.00 19.89 ? 3    LYS J C   1 
ATOM   8928  O  O   . LYS I  1 3   ? 31.581 19.403  -70.235  1.00 19.24 ? 3    LYS J O   1 
ATOM   8929  C  CB  . LYS I  1 3   ? 31.367 22.269  -68.983  1.00 21.20 ? 3    LYS J CB  1 
ATOM   8930  C  CG  . LYS I  1 3   ? 32.044 23.490  -68.334  1.00 23.51 ? 3    LYS J CG  1 
ATOM   8931  C  CD  . LYS I  1 3   ? 31.099 24.232  -67.430  1.00 27.88 ? 3    LYS J CD  1 
ATOM   8932  C  CE  . LYS I  1 3   ? 30.527 25.480  -68.089  1.00 28.99 ? 3    LYS J CE  1 
ATOM   8933  N  NZ  . LYS I  1 3   ? 31.339 26.691  -67.746  1.00 30.75 ? 3    LYS J NZ  1 
ATOM   8934  N  N   . ALA I  1 4   ? 29.928 19.335  -68.693  1.00 18.82 ? 4    ALA J N   1 
ATOM   8935  C  CA  . ALA I  1 4   ? 29.120 18.354  -69.403  1.00 17.96 ? 4    ALA J CA  1 
ATOM   8936  C  C   . ALA I  1 4   ? 27.649 18.682  -69.219  1.00 17.77 ? 4    ALA J C   1 
ATOM   8937  O  O   . ALA I  1 4   ? 27.276 19.434  -68.315  1.00 17.95 ? 4    ALA J O   1 
ATOM   8938  C  CB  . ALA I  1 4   ? 29.418 16.942  -68.930  1.00 18.08 ? 4    ALA J CB  1 
ATOM   8939  N  N   . VAL I  1 5   ? 26.809 18.124  -70.083  1.00 17.18 ? 5    VAL J N   1 
ATOM   8940  C  CA  . VAL I  1 5   ? 25.384 18.406  -70.026  1.00 16.63 ? 5    VAL J CA  1 
ATOM   8941  C  C   . VAL I  1 5   ? 24.574 17.183  -70.441  1.00 16.21 ? 5    VAL J C   1 
ATOM   8942  O  O   . VAL I  1 5   ? 25.052 16.358  -71.211  1.00 16.02 ? 5    VAL J O   1 
ATOM   8943  C  CB  . VAL I  1 5   ? 25.029 19.648  -70.893  1.00 16.51 ? 5    VAL J CB  1 
ATOM   8944  C  CG1 . VAL I  1 5   ? 25.325 19.400  -72.385  1.00 16.76 ? 5    VAL J CG1 1 
ATOM   8945  C  CG2 . VAL I  1 5   ? 23.576 20.076  -70.667  1.00 17.01 ? 5    VAL J CG2 1 
ATOM   8946  N  N   . CYS I  1 6   ? 23.348 17.081  -69.926  1.00 16.09 ? 6    CYS J N   1 
ATOM   8947  C  CA  . CYS I  1 6   ? 22.447 15.992  -70.273  1.00 15.60 ? 6    CYS J CA  1 
ATOM   8948  C  C   . CYS I  1 6   ? 21.022 16.496  -70.436  1.00 15.92 ? 6    CYS J C   1 
ATOM   8949  O  O   . CYS I  1 6   ? 20.475 17.134  -69.532  1.00 14.91 ? 6    CYS J O   1 
ATOM   8950  C  CB  . CYS I  1 6   ? 22.478 14.893  -69.201  1.00 15.79 ? 6    CYS J CB  1 
ATOM   8951  S  SG  . CYS I  1 6   ? 21.516 13.430  -69.593  1.00 15.22 ? 6    CYS J SG  1 
ATOM   8952  N  N   . VAL I  1 7   ? 20.430 16.198  -71.591  1.00 15.51 ? 7    VAL J N   1 
ATOM   8953  C  CA  . VAL I  1 7   ? 19.012 16.437  -71.799  1.00 15.80 ? 7    VAL J CA  1 
ATOM   8954  C  C   . VAL I  1 7   ? 18.258 15.155  -71.518  1.00 15.91 ? 7    VAL J C   1 
ATOM   8955  O  O   . VAL I  1 7   ? 18.386 14.174  -72.240  1.00 15.78 ? 7    VAL J O   1 
ATOM   8956  C  CB  . VAL I  1 7   ? 18.682 16.973  -73.217  1.00 15.98 ? 7    VAL J CB  1 
ATOM   8957  C  CG1 . VAL I  1 7   ? 17.163 17.200  -73.358  1.00 16.07 ? 7    VAL J CG1 1 
ATOM   8958  C  CG2 . VAL I  1 7   ? 19.420 18.277  -73.485  1.00 15.94 ? 7    VAL J CG2 1 
ATOM   8959  N  N   . LEU I  1 8   ? 17.478 15.169  -70.445  1.00 16.09 ? 8    LEU J N   1 
ATOM   8960  C  CA  . LEU I  1 8   ? 16.681 14.026  -70.066  1.00 16.48 ? 8    LEU J CA  1 
ATOM   8961  C  C   . LEU I  1 8   ? 15.335 14.017  -70.793  1.00 17.38 ? 8    LEU J C   1 
ATOM   8962  O  O   . LEU I  1 8   ? 14.592 14.997  -70.716  1.00 16.31 ? 8    LEU J O   1 
ATOM   8963  C  CB  . LEU I  1 8   ? 16.449 14.032  -68.553  1.00 16.35 ? 8    LEU J CB  1 
ATOM   8964  C  CG  . LEU I  1 8   ? 17.674 13.786  -67.668  1.00 16.33 ? 8    LEU J CG  1 
ATOM   8965  C  CD1 . LEU I  1 8   ? 17.355 14.195  -66.241  1.00 16.78 ? 8    LEU J CD1 1 
ATOM   8966  C  CD2 . LEU I  1 8   ? 18.079 12.325  -67.709  1.00 18.67 ? 8    LEU J CD2 1 
ATOM   8967  N  N   . LYS I  1 9   ? 15.032 12.893  -71.452  1.00 18.33 ? 9    LYS J N   1 
ATOM   8968  C  CA  . LYS I  1 9   ? 13.741 12.660  -72.100  1.00 20.41 ? 9    LYS J CA  1 
ATOM   8969  C  C   . LYS I  1 9   ? 13.255 11.222  -71.937  1.00 20.98 ? 9    LYS J C   1 
ATOM   8970  O  O   . LYS I  1 9   ? 14.050 10.304  -71.736  1.00 21.28 ? 9    LYS J O   1 
ATOM   8971  C  CB  . LYS I  1 9   ? 13.818 13.003  -73.590  1.00 20.50 ? 9    LYS J CB  1 
ATOM   8972  C  CG  . LYS I  1 9   ? 13.928 14.483  -73.865  1.00 23.41 ? 9    LYS J CG  1 
ATOM   8973  C  CD  . LYS I  1 9   ? 14.045 14.793  -75.357  1.00 25.37 ? 9    LYS J CD  1 
ATOM   8974  C  CE  . LYS I  1 9   ? 14.441 16.263  -75.557  1.00 25.71 ? 9    LYS J CE  1 
ATOM   8975  N  NZ  . LYS I  1 9   ? 13.432 17.164  -74.939  1.00 27.38 ? 9    LYS J NZ  1 
ATOM   8976  N  N   . GLY I  1 10  ? 11.944 11.026  -72.055  1.00 21.59 ? 10   GLY J N   1 
ATOM   8977  C  CA  . GLY I  1 10  ? 11.346 9.710   -71.896  1.00 22.62 ? 10   GLY J CA  1 
ATOM   8978  C  C   . GLY I  1 10  ? 10.061 9.578   -72.691  1.00 23.78 ? 10   GLY J C   1 
ATOM   8979  O  O   . GLY I  1 10  ? 9.743  10.438  -73.514  1.00 24.01 ? 10   GLY J O   1 
ATOM   8980  N  N   . ASP I  1 11  ? 9.329  8.502   -72.421  1.00 24.47 ? 11   ASP J N   1 
ATOM   8981  C  CA  . ASP I  1 11  ? 8.079  8.174   -73.109  1.00 25.57 ? 11   ASP J CA  1 
ATOM   8982  C  C   . ASP I  1 11  ? 6.908  8.916   -72.503  1.00 25.43 ? 11   ASP J C   1 
ATOM   8983  O  O   . ASP I  1 11  ? 5.791  8.867   -73.032  1.00 26.43 ? 11   ASP J O   1 
ATOM   8984  C  CB  . ASP I  1 11  ? 7.809  6.668   -73.001  1.00 26.06 ? 11   ASP J CB  1 
ATOM   8985  C  CG  . ASP I  1 11  ? 8.856  5.838   -73.707  1.00 28.01 ? 11   ASP J CG  1 
ATOM   8986  O  OD1 . ASP I  1 11  ? 9.166  4.722   -73.220  1.00 28.59 ? 11   ASP J OD1 1 
ATOM   8987  O  OD2 . ASP I  1 11  ? 9.362  6.308   -74.749  1.00 30.66 ? 11   ASP J OD2 1 
ATOM   8988  N  N   . GLY I  1 12  ? 7.161  9.587   -71.384  1.00 24.62 ? 12   GLY J N   1 
ATOM   8989  C  CA  . GLY I  1 12  ? 6.123  10.264  -70.632  1.00 23.55 ? 12   GLY J CA  1 
ATOM   8990  C  C   . GLY I  1 12  ? 6.388  11.747  -70.490  1.00 22.58 ? 12   GLY J C   1 
ATOM   8991  O  O   . GLY I  1 12  ? 7.056  12.339  -71.337  1.00 22.86 ? 12   GLY J O   1 
ATOM   8992  N  N   . PRO I  1 13  ? 5.863  12.353  -69.415  1.00 22.03 ? 13   PRO J N   1 
ATOM   8993  C  CA  . PRO I  1 13  ? 5.948  13.798  -69.183  1.00 21.46 ? 13   PRO J CA  1 
ATOM   8994  C  C   . PRO I  1 13  ? 7.257  14.247  -68.524  1.00 20.90 ? 13   PRO J C   1 
ATOM   8995  O  O   . PRO I  1 13  ? 7.488  15.441  -68.374  1.00 21.45 ? 13   PRO J O   1 
ATOM   8996  C  CB  . PRO I  1 13  ? 4.773  14.059  -68.239  1.00 21.63 ? 13   PRO J CB  1 
ATOM   8997  C  CG  . PRO I  1 13  ? 4.627  12.796  -67.461  1.00 21.38 ? 13   PRO J CG  1 
ATOM   8998  C  CD  . PRO I  1 13  ? 5.062  11.673  -68.377  1.00 21.72 ? 13   PRO J CD  1 
ATOM   8999  N  N   . VAL I  1 14  ? 8.108  13.302  -68.145  1.00 19.88 ? 14   VAL J N   1 
ATOM   9000  C  CA  . VAL I  1 14  ? 9.361  13.640  -67.459  1.00 18.96 ? 14   VAL J CA  1 
ATOM   9001  C  C   . VAL I  1 14  ? 10.446 14.149  -68.429  1.00 19.29 ? 14   VAL J C   1 
ATOM   9002  O  O   . VAL I  1 14  ? 10.823 13.472  -69.384  1.00 18.91 ? 14   VAL J O   1 
ATOM   9003  C  CB  . VAL I  1 14  ? 9.887  12.454  -66.613  1.00 18.75 ? 14   VAL J CB  1 
ATOM   9004  C  CG1 . VAL I  1 14  ? 11.113 12.881  -65.803  1.00 18.35 ? 14   VAL J CG1 1 
ATOM   9005  C  CG2 . VAL I  1 14  ? 8.795  11.915  -65.686  1.00 17.27 ? 14   VAL J CG2 1 
ATOM   9006  N  N   . GLN I  1 15  ? 10.939 15.351  -68.161  1.00 19.19 ? 15   GLN J N   1 
ATOM   9007  C  CA  . GLN I  1 15  ? 12.039 15.939  -68.915  1.00 19.71 ? 15   GLN J CA  1 
ATOM   9008  C  C   . GLN I  1 15  ? 12.809 16.916  -68.038  1.00 19.64 ? 15   GLN J C   1 
ATOM   9009  O  O   . GLN I  1 15  ? 12.315 17.363  -66.994  1.00 19.74 ? 15   GLN J O   1 
ATOM   9010  C  CB  . GLN I  1 15  ? 11.534 16.645  -70.179  1.00 20.38 ? 15   GLN J CB  1 
ATOM   9011  C  CG  . GLN I  1 15  ? 10.511 17.749  -69.932  1.00 21.79 ? 15   GLN J CG  1 
ATOM   9012  C  CD  . GLN I  1 15  ? 9.769  18.156  -71.199  1.00 24.88 ? 15   GLN J CD  1 
ATOM   9013  O  OE1 . GLN I  1 15  ? 8.544  18.016  -71.285  1.00 27.45 ? 15   GLN J OE1 1 
ATOM   9014  N  NE2 . GLN I  1 15  ? 10.505 18.644  -72.190  1.00 25.44 ? 15   GLN J NE2 1 
ATOM   9015  N  N   . GLY I  1 16  ? 14.019 17.243  -68.466  1.00 19.28 ? 16   GLY J N   1 
ATOM   9016  C  CA  . GLY I  1 16  ? 14.873 18.151  -67.718  1.00 18.94 ? 16   GLY J CA  1 
ATOM   9017  C  C   . GLY I  1 16  ? 16.213 18.329  -68.396  1.00 18.28 ? 16   GLY J C   1 
ATOM   9018  O  O   . GLY I  1 16  ? 16.488 17.700  -69.417  1.00 18.55 ? 16   GLY J O   1 
ATOM   9019  N  N   . ILE I  1 17  ? 17.019 19.219  -67.832  1.00 17.29 ? 17   ILE J N   1 
ATOM   9020  C  CA  . ILE I  1 17  ? 18.391 19.466  -68.259  1.00 16.66 ? 17   ILE J CA  1 
ATOM   9021  C  C   . ILE I  1 17  ? 19.262 19.449  -67.002  1.00 15.73 ? 17   ILE J C   1 
ATOM   9022  O  O   . ILE I  1 17  ? 18.978 20.149  -66.026  1.00 15.93 ? 17   ILE J O   1 
ATOM   9023  C  CB  . ILE I  1 17  ? 18.545 20.845  -68.980  1.00 16.99 ? 17   ILE J CB  1 
ATOM   9024  C  CG1 . ILE I  1 17  ? 17.827 20.844  -70.349  1.00 18.08 ? 17   ILE J CG1 1 
ATOM   9025  C  CG2 . ILE I  1 17  ? 20.016 21.223  -69.113  1.00 17.19 ? 17   ILE J CG2 1 
ATOM   9026  C  CD1 . ILE I  1 17  ? 17.210 22.204  -70.723  1.00 21.70 ? 17   ILE J CD1 1 
ATOM   9027  N  N   . ILE I  1 18  ? 20.306 18.630  -67.039  1.00 14.86 ? 18   ILE J N   1 
ATOM   9028  C  CA  . ILE I  1 18  ? 21.278 18.535  -65.948  1.00 13.43 ? 18   ILE J CA  1 
ATOM   9029  C  C   . ILE I  1 18  ? 22.655 18.934  -66.445  1.00 14.03 ? 18   ILE J C   1 
ATOM   9030  O  O   . ILE I  1 18  ? 23.132 18.415  -67.455  1.00 14.29 ? 18   ILE J O   1 
ATOM   9031  C  CB  . ILE I  1 18  ? 21.325 17.098  -65.349  1.00 12.76 ? 18   ILE J CB  1 
ATOM   9032  C  CG1 . ILE I  1 18  ? 19.947 16.695  -64.804  1.00 11.59 ? 18   ILE J CG1 1 
ATOM   9033  C  CG2 . ILE I  1 18  ? 22.410 16.996  -64.263  1.00 10.67 ? 18   ILE J CG2 1 
ATOM   9034  C  CD1 . ILE I  1 18  ? 19.372 17.657  -63.736  1.00 7.20  ? 18   ILE J CD1 1 
ATOM   9035  N  N   . ASN I  1 19  ? 23.281 19.857  -65.722  1.00 14.50 ? 19   ASN J N   1 
ATOM   9036  C  CA  . ASN I  1 19  ? 24.621 20.342  -66.018  1.00 14.88 ? 19   ASN J CA  1 
ATOM   9037  C  C   . ASN I  1 19  ? 25.648 19.680  -65.105  1.00 14.91 ? 19   ASN J C   1 
ATOM   9038  O  O   . ASN I  1 19  ? 25.334 19.336  -63.960  1.00 14.98 ? 19   ASN J O   1 
ATOM   9039  C  CB  . ASN I  1 19  ? 24.675 21.867  -65.831  1.00 15.50 ? 19   ASN J CB  1 
ATOM   9040  C  CG  . ASN I  1 19  ? 23.603 22.597  -66.645  1.00 16.80 ? 19   ASN J CG  1 
ATOM   9041  O  OD1 . ASN I  1 19  ? 23.658 22.626  -67.868  1.00 17.93 ? 19   ASN J OD1 1 
ATOM   9042  N  ND2 . ASN I  1 19  ? 22.620 23.172  -65.959  1.00 18.41 ? 19   ASN J ND2 1 
ATOM   9043  N  N   . PHE I  1 20  ? 26.867 19.507  -65.613  1.00 15.22 ? 20   PHE J N   1 
ATOM   9044  C  CA  . PHE I  1 20  ? 27.977 18.989  -64.826  1.00 15.04 ? 20   PHE J CA  1 
ATOM   9045  C  C   . PHE I  1 20  ? 29.159 19.959  -64.941  1.00 16.31 ? 20   PHE J C   1 
ATOM   9046  O  O   . PHE I  1 20  ? 29.421 20.505  -66.028  1.00 16.70 ? 20   PHE J O   1 
ATOM   9047  C  CB  . PHE I  1 20  ? 28.391 17.606  -65.348  1.00 14.78 ? 20   PHE J CB  1 
ATOM   9048  C  CG  . PHE I  1 20  ? 27.303 16.551  -65.268  1.00 13.26 ? 20   PHE J CG  1 
ATOM   9049  C  CD1 . PHE I  1 20  ? 27.234 15.700  -64.186  1.00 12.50 ? 20   PHE J CD1 1 
ATOM   9050  C  CD2 . PHE I  1 20  ? 26.349 16.412  -66.285  1.00 10.98 ? 20   PHE J CD2 1 
ATOM   9051  C  CE1 . PHE I  1 20  ? 26.237 14.713  -64.114  1.00 12.92 ? 20   PHE J CE1 1 
ATOM   9052  C  CE2 . PHE I  1 20  ? 25.347 15.430  -66.220  1.00 11.38 ? 20   PHE J CE2 1 
ATOM   9053  C  CZ  . PHE I  1 20  ? 25.294 14.583  -65.138  1.00 11.22 ? 20   PHE J CZ  1 
ATOM   9054  N  N   . GLU I  1 21  ? 29.869 20.180  -63.834  1.00 16.65 ? 21   GLU J N   1 
ATOM   9055  C  CA  . GLU I  1 21  ? 31.113 20.948  -63.877  1.00 17.66 ? 21   GLU J CA  1 
ATOM   9056  C  C   . GLU I  1 21  ? 32.155 20.362  -62.939  1.00 17.68 ? 21   GLU J C   1 
ATOM   9057  O  O   . GLU I  1 21  ? 31.852 19.997  -61.797  1.00 17.05 ? 21   GLU J O   1 
ATOM   9058  C  CB  . GLU I  1 21  ? 30.894 22.440  -63.571  1.00 17.53 ? 21   GLU J CB  1 
ATOM   9059  C  CG  . GLU I  1 21  ? 32.187 23.246  -63.713  1.00 21.51 ? 21   GLU J CG  1 
ATOM   9060  C  CD  . GLU I  1 21  ? 31.997 24.750  -63.861  1.00 27.36 ? 21   GLU J CD  1 
ATOM   9061  O  OE1 . GLU I  1 21  ? 33.004 25.433  -64.172  1.00 30.54 ? 21   GLU J OE1 1 
ATOM   9062  O  OE2 . GLU I  1 21  ? 30.865 25.264  -63.674  1.00 30.71 ? 21   GLU J OE2 1 
ATOM   9063  N  N   . GLN I  1 22  ? 33.379 20.262  -63.439  1.00 18.25 ? 22   GLN J N   1 
ATOM   9064  C  CA  . GLN I  1 22  ? 34.483 19.754  -62.647  1.00 19.00 ? 22   GLN J CA  1 
ATOM   9065  C  C   . GLN I  1 22  ? 35.656 20.695  -62.852  1.00 20.17 ? 22   GLN J C   1 
ATOM   9066  O  O   . GLN I  1 22  ? 36.174 20.814  -63.962  1.00 20.36 ? 22   GLN J O   1 
ATOM   9067  C  CB  . GLN I  1 22  ? 34.834 18.332  -63.082  1.00 18.85 ? 22   GLN J CB  1 
ATOM   9068  C  CG  . GLN I  1 22  ? 35.743 17.543  -62.111  1.00 17.68 ? 22   GLN J CG  1 
ATOM   9069  C  CD  . GLN I  1 22  ? 36.137 16.201  -62.691  1.00 18.62 ? 22   GLN J CD  1 
ATOM   9070  O  OE1 . GLN I  1 22  ? 36.020 15.989  -63.901  1.00 17.39 ? 22   GLN J OE1 1 
ATOM   9071  N  NE2 . GLN I  1 22  ? 36.613 15.285  -61.840  1.00 18.89 ? 22   GLN J NE2 1 
ATOM   9072  N  N   . LYS I  1 23  ? 36.061 21.374  -61.787  1.00 21.27 ? 23   LYS J N   1 
ATOM   9073  C  CA  . LYS I  1 23  ? 37.135 22.359  -61.889  1.00 23.37 ? 23   LYS J CA  1 
ATOM   9074  C  C   . LYS I  1 23  ? 38.510 21.712  -62.047  1.00 24.03 ? 23   LYS J C   1 
ATOM   9075  O  O   . LYS I  1 23  ? 39.346 22.211  -62.811  1.00 24.82 ? 23   LYS J O   1 
ATOM   9076  C  CB  . LYS I  1 23  ? 37.095 23.350  -60.722  1.00 23.40 ? 23   LYS J CB  1 
ATOM   9077  C  CG  . LYS I  1 23  ? 35.857 24.257  -60.745  1.00 26.16 ? 23   LYS J CG  1 
ATOM   9078  C  CD  . LYS I  1 23  ? 35.947 25.395  -59.714  1.00 28.49 ? 23   LYS J CD  1 
ATOM   9079  C  CE  . LYS I  1 23  ? 34.586 26.059  -59.479  1.00 30.08 ? 23   LYS J CE  1 
ATOM   9080  N  NZ  . LYS I  1 23  ? 34.088 26.801  -60.685  1.00 30.39 ? 23   LYS J NZ  1 
ATOM   9081  N  N   . GLU I  1 24  ? 38.735 20.590  -61.361  1.00 24.72 ? 24   GLU J N   1 
ATOM   9082  C  CA  . GLU I  1 24  ? 40.016 19.877  -61.432  1.00 25.54 ? 24   GLU J CA  1 
ATOM   9083  C  C   . GLU I  1 24  ? 39.790 18.378  -61.648  1.00 25.71 ? 24   GLU J C   1 
ATOM   9084  O  O   . GLU I  1 24  ? 38.779 17.845  -61.208  1.00 25.16 ? 24   GLU J O   1 
ATOM   9085  C  CB  . GLU I  1 24  ? 40.833 20.089  -60.139  1.00 26.16 ? 24   GLU J CB  1 
ATOM   9086  C  CG  . GLU I  1 24  ? 40.669 21.455  -59.414  1.00 28.51 ? 24   GLU J CG  1 
ATOM   9087  C  CD  . GLU I  1 24  ? 41.368 22.634  -60.114  1.00 33.19 ? 24   GLU J CD  1 
ATOM   9088  O  OE1 . GLU I  1 24  ? 41.869 22.478  -61.254  1.00 36.34 ? 24   GLU J OE1 1 
ATOM   9089  O  OE2 . GLU I  1 24  ? 41.412 23.736  -59.524  1.00 34.27 ? 24   GLU J OE2 1 
ATOM   9090  N  N   . SER I  1 25  ? 40.745 17.702  -62.296  1.00 26.27 ? 25   SER J N   1 
ATOM   9091  C  CA  . SER I  1 25  ? 40.713 16.233  -62.488  1.00 27.01 ? 25   SER J CA  1 
ATOM   9092  C  C   . SER I  1 25  ? 40.532 15.478  -61.165  1.00 26.83 ? 25   SER J C   1 
ATOM   9093  O  O   . SER I  1 25  ? 39.923 14.406  -61.105  1.00 27.30 ? 25   SER J O   1 
ATOM   9094  C  CB  . SER I  1 25  ? 42.017 15.751  -63.137  1.00 26.88 ? 25   SER J CB  1 
ATOM   9095  O  OG  . SER I  1 25  ? 42.556 16.725  -64.006  1.00 29.74 ? 25   SER J OG  1 
ATOM   9096  N  N   . ASN I  1 26  ? 41.083 16.043  -60.102  1.00 26.91 ? 26   ASN J N   1 
ATOM   9097  C  CA  . ASN I  1 26  ? 41.041 15.412  -58.792  1.00 26.71 ? 26   ASN J CA  1 
ATOM   9098  C  C   . ASN I  1 26  ? 39.729 15.679  -58.073  1.00 25.55 ? 26   ASN J C   1 
ATOM   9099  O  O   . ASN I  1 26  ? 39.385 15.000  -57.094  1.00 25.75 ? 26   ASN J O   1 
ATOM   9100  C  CB  . ASN I  1 26  ? 42.242 15.848  -57.935  1.00 27.16 ? 26   ASN J CB  1 
ATOM   9101  C  CG  . ASN I  1 26  ? 42.626 17.319  -58.138  1.00 29.35 ? 26   ASN J CG  1 
ATOM   9102  O  OD1 . ASN I  1 26  ? 42.499 18.130  -57.220  1.00 29.74 ? 26   ASN J OD1 1 
ATOM   9103  N  ND2 . ASN I  1 26  ? 43.121 17.658  -59.337  1.00 31.39 ? 26   ASN J ND2 1 
ATOM   9104  N  N   . GLY I  1 27  ? 38.989 16.660  -58.587  1.00 23.36 ? 27   GLY J N   1 
ATOM   9105  C  CA  . GLY I  1 27  ? 37.991 17.324  -57.783  1.00 21.16 ? 27   GLY J CA  1 
ATOM   9106  C  C   . GLY I  1 27  ? 36.582 16.815  -57.931  1.00 18.76 ? 27   GLY J C   1 
ATOM   9107  O  O   . GLY I  1 27  ? 36.289 16.022  -58.821  1.00 17.93 ? 27   GLY J O   1 
ATOM   9108  N  N   . PRO I  1 28  ? 35.694 17.287  -57.046  1.00 18.04 ? 28   PRO J N   1 
ATOM   9109  C  CA  . PRO I  1 28  ? 34.303 16.900  -57.094  1.00 16.21 ? 28   PRO J CA  1 
ATOM   9110  C  C   . PRO I  1 28  ? 33.680 17.453  -58.357  1.00 15.42 ? 28   PRO J C   1 
ATOM   9111  O  O   . PRO I  1 28  ? 34.191 18.415  -58.945  1.00 14.36 ? 28   PRO J O   1 
ATOM   9112  C  CB  . PRO I  1 28  ? 33.702 17.602  -55.878  1.00 16.91 ? 28   PRO J CB  1 
ATOM   9113  C  CG  . PRO I  1 28  ? 34.580 18.778  -55.660  1.00 18.00 ? 28   PRO J CG  1 
ATOM   9114  C  CD  . PRO I  1 28  ? 35.951 18.301  -56.005  1.00 17.92 ? 28   PRO J CD  1 
ATOM   9115  N  N   . VAL I  1 29  ? 32.591 16.823  -58.765  1.00 13.87 ? 29   VAL J N   1 
ATOM   9116  C  CA  . VAL I  1 29  ? 31.799 17.281  -59.877  1.00 12.43 ? 29   VAL J CA  1 
ATOM   9117  C  C   . VAL I  1 29  ? 30.527 17.877  -59.296  1.00 12.51 ? 29   VAL J C   1 
ATOM   9118  O  O   . VAL I  1 29  ? 29.828 17.209  -58.531  1.00 11.32 ? 29   VAL J O   1 
ATOM   9119  C  CB  . VAL I  1 29  ? 31.433 16.127  -60.800  1.00 12.70 ? 29   VAL J CB  1 
ATOM   9120  C  CG1 . VAL I  1 29  ? 30.651 16.651  -62.008  1.00 11.11 ? 29   VAL J CG1 1 
ATOM   9121  C  CG2 . VAL I  1 29  ? 32.697 15.330  -61.218  1.00 11.72 ? 29   VAL J CG2 1 
ATOM   9122  N  N   . LYS I  1 30  ? 30.242 19.131  -59.643  1.00 13.07 ? 30   LYS J N   1 
ATOM   9123  C  CA  . LYS I  1 30  ? 28.944 19.736  -59.325  1.00 13.68 ? 30   LYS J CA  1 
ATOM   9124  C  C   . LYS I  1 30  ? 27.898 19.266  -60.344  1.00 12.81 ? 30   LYS J C   1 
ATOM   9125  O  O   . LYS I  1 30  ? 28.153 19.258  -61.552  1.00 11.94 ? 30   LYS J O   1 
ATOM   9126  C  CB  . LYS I  1 30  ? 29.032 21.262  -59.316  1.00 14.38 ? 30   LYS J CB  1 
ATOM   9127  C  CG  . LYS I  1 30  ? 29.955 21.877  -58.244  1.00 18.13 ? 30   LYS J CG  1 
ATOM   9128  C  CD  . LYS I  1 30  ? 29.943 23.421  -58.343  1.00 22.57 ? 30   LYS J CD  1 
ATOM   9129  C  CE  . LYS I  1 30  ? 30.616 24.098  -57.130  1.00 25.55 ? 30   LYS J CE  1 
ATOM   9130  N  NZ  . LYS I  1 30  ? 30.021 23.648  -55.826  1.00 27.01 ? 30   LYS J NZ  1 
ATOM   9131  N  N   . VAL I  1 31  ? 26.731 18.866  -59.849  1.00 12.49 ? 31   VAL J N   1 
ATOM   9132  C  CA  . VAL I  1 31  ? 25.627 18.371  -60.680  1.00 12.36 ? 31   VAL J CA  1 
ATOM   9133  C  C   . VAL I  1 31  ? 24.389 19.209  -60.387  1.00 12.78 ? 31   VAL J C   1 
ATOM   9134  O  O   . VAL I  1 31  ? 23.928 19.247  -59.256  1.00 12.50 ? 31   VAL J O   1 
ATOM   9135  C  CB  . VAL I  1 31  ? 25.331 16.880  -60.362  1.00 12.73 ? 31   VAL J CB  1 
ATOM   9136  C  CG1 . VAL I  1 31  ? 24.270 16.302  -61.298  1.00 12.89 ? 31   VAL J CG1 1 
ATOM   9137  C  CG2 . VAL I  1 31  ? 26.616 16.050  -60.447  1.00 13.07 ? 31   VAL J CG2 1 
ATOM   9138  N  N   . TRP I  1 32  ? 23.858 19.904  -61.394  1.00 13.21 ? 32   TRP J N   1 
ATOM   9139  C  CA  . TRP I  1 32  ? 22.717 20.774  -61.144  1.00 13.84 ? 32   TRP J CA  1 
ATOM   9140  C  C   . TRP I  1 32  ? 21.852 20.992  -62.359  1.00 13.85 ? 32   TRP J C   1 
ATOM   9141  O  O   . TRP I  1 32  ? 22.342 20.975  -63.489  1.00 13.57 ? 32   TRP J O   1 
ATOM   9142  C  CB  . TRP I  1 32  ? 23.173 22.134  -60.587  1.00 14.22 ? 32   TRP J CB  1 
ATOM   9143  C  CG  . TRP I  1 32  ? 23.681 23.103  -61.620  1.00 15.24 ? 32   TRP J CG  1 
ATOM   9144  C  CD1 . TRP I  1 32  ? 23.006 24.173  -62.140  1.00 17.68 ? 32   TRP J CD1 1 
ATOM   9145  C  CD2 . TRP I  1 32  ? 24.962 23.092  -62.253  1.00 16.63 ? 32   TRP J CD2 1 
ATOM   9146  N  NE1 . TRP I  1 32  ? 23.786 24.826  -63.051  1.00 19.26 ? 32   TRP J NE1 1 
ATOM   9147  C  CE2 . TRP I  1 32  ? 24.998 24.192  -63.138  1.00 18.30 ? 32   TRP J CE2 1 
ATOM   9148  C  CE3 . TRP I  1 32  ? 26.091 22.263  -62.154  1.00 16.56 ? 32   TRP J CE3 1 
ATOM   9149  C  CZ2 . TRP I  1 32  ? 26.115 24.485  -63.927  1.00 17.91 ? 32   TRP J CZ2 1 
ATOM   9150  C  CZ3 . TRP I  1 32  ? 27.208 22.558  -62.948  1.00 16.45 ? 32   TRP J CZ3 1 
ATOM   9151  C  CH2 . TRP I  1 32  ? 27.206 23.661  -63.821  1.00 16.97 ? 32   TRP J CH2 1 
ATOM   9152  N  N   . GLY I  1 33  ? 20.571 21.242  -62.101  1.00 13.96 ? 33   GLY J N   1 
ATOM   9153  C  CA  . GLY I  1 33  ? 19.625 21.569  -63.151  1.00 14.87 ? 33   GLY J CA  1 
ATOM   9154  C  C   . GLY I  1 33  ? 18.209 21.374  -62.661  1.00 15.87 ? 33   GLY J C   1 
ATOM   9155  O  O   . GLY I  1 33  ? 17.923 21.511  -61.467  1.00 16.16 ? 33   GLY J O   1 
ATOM   9156  N  N   . SER I  1 34  ? 17.304 21.079  -63.587  1.00 16.40 ? 34   SER J N   1 
ATOM   9157  C  CA  . SER I  1 34  ? 15.916 20.862  -63.218  1.00 17.12 ? 34   SER J CA  1 
ATOM   9158  C  C   . SER I  1 34  ? 15.321 19.714  -63.997  1.00 16.75 ? 34   SER J C   1 
ATOM   9159  O  O   . SER I  1 34  ? 15.757 19.409  -65.098  1.00 17.18 ? 34   SER J O   1 
ATOM   9160  C  CB  . SER I  1 34  ? 15.074 22.145  -63.384  1.00 17.18 ? 34   SER J CB  1 
ATOM   9161  O  OG  . SER I  1 34  ? 15.362 22.793  -64.609  1.00 20.66 ? 34   SER J OG  1 
ATOM   9162  N  N   . ILE I  1 35  ? 14.356 19.050  -63.381  1.00 16.34 ? 35   ILE J N   1 
ATOM   9163  C  CA  . ILE I  1 35  ? 13.610 17.975  -64.003  1.00 15.95 ? 35   ILE J CA  1 
ATOM   9164  C  C   . ILE I  1 35  ? 12.149 18.235  -63.658  1.00 16.76 ? 35   ILE J C   1 
ATOM   9165  O  O   . ILE I  1 35  ? 11.807 18.424  -62.482  1.00 16.08 ? 35   ILE J O   1 
ATOM   9166  C  CB  . ILE I  1 35  ? 14.015 16.586  -63.447  1.00 15.93 ? 35   ILE J CB  1 
ATOM   9167  C  CG1 . ILE I  1 35  ? 15.535 16.376  -63.532  1.00 15.65 ? 35   ILE J CG1 1 
ATOM   9168  C  CG2 . ILE I  1 35  ? 13.302 15.482  -64.211  1.00 14.78 ? 35   ILE J CG2 1 
ATOM   9169  C  CD1 . ILE I  1 35  ? 16.001 15.068  -62.891  1.00 15.42 ? 35   ILE J CD1 1 
ATOM   9170  N  N   . LYS I  1 36  ? 11.294 18.268  -64.676  1.00 17.28 ? 36   LYS J N   1 
ATOM   9171  C  CA  . LYS I  1 36  ? 9.872  18.502  -64.440  1.00 17.75 ? 36   LYS J CA  1 
ATOM   9172  C  C   . LYS I  1 36  ? 9.045  17.283  -64.812  1.00 17.63 ? 36   LYS J C   1 
ATOM   9173  O  O   . LYS I  1 36  ? 9.573  16.325  -65.402  1.00 17.01 ? 36   LYS J O   1 
ATOM   9174  C  CB  . LYS I  1 36  ? 9.391  19.779  -65.158  1.00 18.24 ? 36   LYS J CB  1 
ATOM   9175  C  CG  . LYS I  1 36  ? 9.455  19.735  -66.659  1.00 19.90 ? 36   LYS J CG  1 
ATOM   9176  C  CD  . LYS I  1 36  ? 9.132  21.101  -67.260  1.00 23.24 ? 36   LYS J CD  1 
ATOM   9177  C  CE  . LYS I  1 36  ? 8.751  20.961  -68.720  1.00 24.54 ? 36   LYS J CE  1 
ATOM   9178  N  NZ  . LYS I  1 36  ? 8.955  22.238  -69.481  1.00 26.59 ? 36   LYS J NZ  1 
ATOM   9179  N  N   . GLY I  1 37  ? 7.760  17.310  -64.447  1.00 16.96 ? 37   GLY J N   1 
ATOM   9180  C  CA  . GLY I  1 37  ? 6.840  16.245  -64.820  1.00 16.81 ? 37   GLY J CA  1 
ATOM   9181  C  C   . GLY I  1 37  ? 6.854  15.036  -63.901  1.00 16.86 ? 37   GLY J C   1 
ATOM   9182  O  O   . GLY I  1 37  ? 6.284  13.998  -64.228  1.00 16.89 ? 37   GLY J O   1 
ATOM   9183  N  N   . LEU I  1 38  ? 7.501  15.162  -62.747  1.00 17.26 ? 38   LEU J N   1 
ATOM   9184  C  CA  . LEU I  1 38  ? 7.641  14.051  -61.803  1.00 16.99 ? 38   LEU J CA  1 
ATOM   9185  C  C   . LEU I  1 38  ? 6.542  14.057  -60.767  1.00 17.79 ? 38   LEU J C   1 
ATOM   9186  O  O   . LEU I  1 38  ? 6.008  15.120  -60.431  1.00 18.23 ? 38   LEU J O   1 
ATOM   9187  C  CB  . LEU I  1 38  ? 8.974  14.159  -61.056  1.00 16.97 ? 38   LEU J CB  1 
ATOM   9188  C  CG  . LEU I  1 38  ? 10.264 13.946  -61.842  1.00 16.41 ? 38   LEU J CG  1 
ATOM   9189  C  CD1 . LEU I  1 38  ? 11.443 14.630  -61.116  1.00 17.93 ? 38   LEU J CD1 1 
ATOM   9190  C  CD2 . LEU I  1 38  ? 10.506 12.440  -62.046  1.00 15.94 ? 38   LEU J CD2 1 
ATOM   9191  N  N   . THR I  1 39  ? 6.234  12.877  -60.227  1.00 17.23 ? 39   THR J N   1 
ATOM   9192  C  CA  . THR I  1 39  ? 5.441  12.789  -59.011  1.00 17.45 ? 39   THR J CA  1 
ATOM   9193  C  C   . THR I  1 39  ? 6.228  13.356  -57.833  1.00 17.29 ? 39   THR J C   1 
ATOM   9194  O  O   . THR I  1 39  ? 7.450  13.197  -57.760  1.00 17.60 ? 39   THR J O   1 
ATOM   9195  C  CB  . THR I  1 39  ? 5.026  11.325  -58.694  1.00 17.38 ? 39   THR J CB  1 
ATOM   9196  O  OG1 . THR I  1 39  ? 6.203  10.520  -58.479  1.00 17.90 ? 39   THR J OG1 1 
ATOM   9197  C  CG2 . THR I  1 39  ? 4.203  10.733  -59.847  1.00 16.84 ? 39   THR J CG2 1 
ATOM   9198  N  N   . GLU I  1 40  ? 5.527  14.016  -56.914  1.00 16.81 ? 40   GLU J N   1 
ATOM   9199  C  CA  . GLU I  1 40  ? 6.129  14.574  -55.699  1.00 16.83 ? 40   GLU J CA  1 
ATOM   9200  C  C   . GLU I  1 40  ? 6.869  13.500  -54.908  1.00 16.51 ? 40   GLU J C   1 
ATOM   9201  O  O   . GLU I  1 40  ? 6.376  12.381  -54.780  1.00 16.35 ? 40   GLU J O   1 
ATOM   9202  C  CB  . GLU I  1 40  ? 5.045  15.201  -54.810  1.00 17.53 ? 40   GLU J CB  1 
ATOM   9203  C  CG  . GLU I  1 40  ? 5.599  16.039  -53.649  1.00 19.26 ? 40   GLU J CG  1 
ATOM   9204  C  CD  . GLU I  1 40  ? 4.518  16.598  -52.719  1.00 23.15 ? 40   GLU J CD  1 
ATOM   9205  O  OE1 . GLU I  1 40  ? 4.902  17.137  -51.658  1.00 24.35 ? 40   GLU J OE1 1 
ATOM   9206  O  OE2 . GLU I  1 40  ? 3.305  16.500  -53.030  1.00 23.35 ? 40   GLU J OE2 1 
ATOM   9207  N  N   . GLY I  1 41  ? 8.053  13.840  -54.391  1.00 15.72 ? 41   GLY J N   1 
ATOM   9208  C  CA  . GLY I  1 41  ? 8.850  12.879  -53.627  1.00 14.32 ? 41   GLY J CA  1 
ATOM   9209  C  C   . GLY I  1 41  ? 10.176 12.479  -54.266  1.00 13.54 ? 41   GLY J C   1 
ATOM   9210  O  O   . GLY I  1 41  ? 10.678 13.153  -55.178  1.00 12.76 ? 41   GLY J O   1 
ATOM   9211  N  N   . LEU I  1 42  ? 10.737 11.378  -53.769  1.00 12.62 ? 42   LEU J N   1 
ATOM   9212  C  CA  . LEU I  1 42  ? 12.086 10.942  -54.141  1.00 12.28 ? 42   LEU J CA  1 
ATOM   9213  C  C   . LEU I  1 42  ? 12.108 10.096  -55.395  1.00 12.20 ? 42   LEU J C   1 
ATOM   9214  O  O   . LEU I  1 42  ? 11.259 9.208   -55.582  1.00 11.93 ? 42   LEU J O   1 
ATOM   9215  C  CB  . LEU I  1 42  ? 12.719 10.130  -53.013  1.00 12.21 ? 42   LEU J CB  1 
ATOM   9216  C  CG  . LEU I  1 42  ? 13.057 10.802  -51.682  1.00 13.35 ? 42   LEU J CG  1 
ATOM   9217  C  CD1 . LEU I  1 42  ? 13.267 9.698   -50.637  1.00 13.31 ? 42   LEU J CD1 1 
ATOM   9218  C  CD2 . LEU I  1 42  ? 14.271 11.744  -51.798  1.00 14.25 ? 42   LEU J CD2 1 
ATOM   9219  N  N   . HIS I  1 43  ? 13.115 10.353  -56.228  1.00 11.73 ? 43   HIS J N   1 
ATOM   9220  C  CA  . HIS I  1 43  ? 13.329 9.610   -57.458  1.00 11.04 ? 43   HIS J CA  1 
ATOM   9221  C  C   . HIS I  1 43  ? 14.805 9.231   -57.565  1.00 10.63 ? 43   HIS J C   1 
ATOM   9222  O  O   . HIS I  1 43  ? 15.665 10.101  -57.462  1.00 9.83  ? 43   HIS J O   1 
ATOM   9223  C  CB  . HIS I  1 43  ? 12.898 10.451  -58.658  1.00 10.70 ? 43   HIS J CB  1 
ATOM   9224  C  CG  . HIS I  1 43  ? 11.417 10.707  -58.690  1.00 12.68 ? 43   HIS J CG  1 
ATOM   9225  N  ND1 . HIS I  1 43  ? 10.533 9.826   -59.269  1.00 12.40 ? 43   HIS J ND1 1 
ATOM   9226  C  CD2 . HIS I  1 43  ? 10.665 11.705  -58.165  1.00 14.36 ? 43   HIS J CD2 1 
ATOM   9227  C  CE1 . HIS I  1 43  ? 9.301  10.282  -59.125  1.00 15.05 ? 43   HIS J CE1 1 
ATOM   9228  N  NE2 . HIS I  1 43  ? 9.352  11.419  -58.455  1.00 12.80 ? 43   HIS J NE2 1 
ATOM   9229  N  N   . GLY I  1 44  ? 15.082 7.945   -57.781  1.00 10.11 ? 44   GLY J N   1 
ATOM   9230  C  CA  . GLY I  1 44  ? 16.470 7.469   -58.034  1.00 9.24  ? 44   GLY J CA  1 
ATOM   9231  C  C   . GLY I  1 44  ? 17.127 8.196   -59.192  1.00 8.35  ? 44   GLY J C   1 
ATOM   9232  O  O   . GLY I  1 44  ? 16.453 8.610   -60.144  1.00 6.55  ? 44   GLY J O   1 
ATOM   9233  N  N   . PHE I  1 45  ? 18.454 8.364   -59.109  1.00 8.04  ? 45   PHE J N   1 
ATOM   9234  C  CA  . PHE I  1 45  ? 19.192 9.248   -60.009  1.00 8.55  ? 45   PHE J CA  1 
ATOM   9235  C  C   . PHE I  1 45  ? 20.577 8.630   -60.165  1.00 8.87  ? 45   PHE J C   1 
ATOM   9236  O  O   . PHE I  1 45  ? 21.366 8.638   -59.213  1.00 8.75  ? 45   PHE J O   1 
ATOM   9237  C  CB  . PHE I  1 45  ? 19.284 10.648  -59.357  1.00 8.62  ? 45   PHE J CB  1 
ATOM   9238  C  CG  . PHE I  1 45  ? 19.754 11.757  -60.274  1.00 10.19 ? 45   PHE J CG  1 
ATOM   9239  C  CD1 . PHE I  1 45  ? 19.091 12.038  -61.471  1.00 11.15 ? 45   PHE J CD1 1 
ATOM   9240  C  CD2 . PHE I  1 45  ? 20.848 12.550  -59.912  1.00 7.92  ? 45   PHE J CD2 1 
ATOM   9241  C  CE1 . PHE I  1 45  ? 19.517 13.085  -62.295  1.00 11.70 ? 45   PHE J CE1 1 
ATOM   9242  C  CE2 . PHE I  1 45  ? 21.289 13.586  -60.716  1.00 10.72 ? 45   PHE J CE2 1 
ATOM   9243  C  CZ  . PHE I  1 45  ? 20.624 13.870  -61.926  1.00 9.24  ? 45   PHE J CZ  1 
ATOM   9244  N  N   . HIS I  1 46  ? 20.861 8.062   -61.344  1.00 9.57  ? 46   HIS J N   1 
ATOM   9245  C  CA  . HIS I  1 46  ? 22.124 7.327   -61.553  1.00 9.01  ? 46   HIS J CA  1 
ATOM   9246  C  C   . HIS I  1 46  ? 22.692 7.525   -62.942  1.00 9.48  ? 46   HIS J C   1 
ATOM   9247  O  O   . HIS I  1 46  ? 21.947 7.809   -63.900  1.00 8.26  ? 46   HIS J O   1 
ATOM   9248  C  CB  . HIS I  1 46  ? 21.929 5.812   -61.376  1.00 10.07 ? 46   HIS J CB  1 
ATOM   9249  C  CG  . HIS I  1 46  ? 20.952 5.432   -60.313  1.00 9.74  ? 46   HIS J CG  1 
ATOM   9250  N  ND1 . HIS I  1 46  ? 19.761 4.791   -60.589  1.00 11.35 ? 46   HIS J ND1 1 
ATOM   9251  C  CD2 . HIS I  1 46  ? 21.002 5.571   -58.964  1.00 9.42  ? 46   HIS J CD2 1 
ATOM   9252  C  CE1 . HIS I  1 46  ? 19.114 4.562   -59.458  1.00 10.79 ? 46   HIS J CE1 1 
ATOM   9253  N  NE2 . HIS I  1 46  ? 19.845 5.030   -58.458  1.00 10.86 ? 46   HIS J NE2 1 
ATOM   9254  N  N   . VAL I  1 47  ? 24.013 7.330   -63.051  1.00 8.58  ? 47   VAL J N   1 
ATOM   9255  C  CA  . VAL I  1 47  ? 24.668 7.170   -64.333  1.00 8.20  ? 47   VAL J CA  1 
ATOM   9256  C  C   . VAL I  1 47  ? 24.725 5.678   -64.652  1.00 8.79  ? 47   VAL J C   1 
ATOM   9257  O  O   . VAL I  1 47  ? 25.206 4.879   -63.849  1.00 8.57  ? 47   VAL J O   1 
ATOM   9258  C  CB  . VAL I  1 47  ? 26.103 7.744   -64.363  1.00 8.04  ? 47   VAL J CB  1 
ATOM   9259  C  CG1 . VAL I  1 47  ? 26.650 7.679   -65.803  1.00 6.99  ? 47   VAL J CG1 1 
ATOM   9260  C  CG2 . VAL I  1 47  ? 26.117 9.194   -63.893  1.00 8.86  ? 47   VAL J CG2 1 
ATOM   9261  N  N   . HIS I  1 48  ? 24.192 5.308   -65.816  1.00 8.33  ? 48   HIS J N   1 
ATOM   9262  C  CA  . HIS I  1 48  ? 24.194 3.908   -66.251  1.00 9.62  ? 48   HIS J CA  1 
ATOM   9263  C  C   . HIS I  1 48  ? 25.333 3.714   -67.233  1.00 9.77  ? 48   HIS J C   1 
ATOM   9264  O  O   . HIS I  1 48  ? 25.837 4.671   -67.821  1.00 10.07 ? 48   HIS J O   1 
ATOM   9265  C  CB  . HIS I  1 48  ? 22.849 3.515   -66.889  1.00 8.48  ? 48   HIS J CB  1 
ATOM   9266  C  CG  . HIS I  1 48  ? 21.747 3.357   -65.889  1.00 7.49  ? 48   HIS J CG  1 
ATOM   9267  N  ND1 . HIS I  1 48  ? 20.982 2.218   -65.796  1.00 7.93  ? 48   HIS J ND1 1 
ATOM   9268  C  CD2 . HIS I  1 48  ? 21.306 4.188   -64.914  1.00 7.58  ? 48   HIS J CD2 1 
ATOM   9269  C  CE1 . HIS I  1 48  ? 20.109 2.355   -64.811  1.00 9.14  ? 48   HIS J CE1 1 
ATOM   9270  N  NE2 . HIS I  1 48  ? 20.287 3.541   -64.263  1.00 7.32  ? 48   HIS J NE2 1 
ATOM   9271  N  N   . GLU I  1 49  ? 25.734 2.466   -67.398  1.00 11.02 ? 49   GLU J N   1 
ATOM   9272  C  CA  . GLU I  1 49  ? 26.971 2.150   -68.125  1.00 12.27 ? 49   GLU J CA  1 
ATOM   9273  C  C   . GLU I  1 49  ? 27.050 2.664   -69.573  1.00 12.38 ? 49   GLU J C   1 
ATOM   9274  O  O   . GLU I  1 49  ? 28.068 3.261   -69.973  1.00 12.68 ? 49   GLU J O   1 
ATOM   9275  C  CB  . GLU I  1 49  ? 27.201 0.651   -68.064  1.00 12.21 ? 49   GLU J CB  1 
ATOM   9276  C  CG  . GLU I  1 49  ? 28.500 0.187   -68.705  1.00 13.79 ? 49   GLU J CG  1 
ATOM   9277  C  CD  . GLU I  1 49  ? 28.774 -1.269  -68.449  1.00 15.35 ? 49   GLU J CD  1 
ATOM   9278  O  OE1 . GLU I  1 49  ? 29.902 -1.719  -68.765  1.00 15.51 ? 49   GLU J OE1 1 
ATOM   9279  O  OE2 . GLU I  1 49  ? 27.878 -1.947  -67.915  1.00 14.39 ? 49   GLU J OE2 1 
ATOM   9280  N  N   . PHE I  1 50  ? 25.990 2.429   -70.348  1.00 12.14 ? 50   PHE J N   1 
ATOM   9281  C  CA  . PHE I  1 50  ? 26.025 2.656   -71.801  1.00 12.15 ? 50   PHE J CA  1 
ATOM   9282  C  C   . PHE I  1 50  ? 25.259 3.877   -72.239  1.00 12.31 ? 50   PHE J C   1 
ATOM   9283  O  O   . PHE I  1 50  ? 24.133 4.073   -71.820  1.00 11.72 ? 50   PHE J O   1 
ATOM   9284  C  CB  . PHE I  1 50  ? 25.513 1.421   -72.556  1.00 11.60 ? 50   PHE J CB  1 
ATOM   9285  C  CG  . PHE I  1 50  ? 26.255 0.176   -72.197  1.00 12.23 ? 50   PHE J CG  1 
ATOM   9286  C  CD1 . PHE I  1 50  ? 27.643 0.112   -72.360  1.00 12.91 ? 50   PHE J CD1 1 
ATOM   9287  C  CD2 . PHE I  1 50  ? 25.586 -0.915  -71.661  1.00 13.15 ? 50   PHE J CD2 1 
ATOM   9288  C  CE1 . PHE I  1 50  ? 28.347 -1.035  -71.993  1.00 15.08 ? 50   PHE J CE1 1 
ATOM   9289  C  CE2 . PHE I  1 50  ? 26.285 -2.057  -71.295  1.00 14.82 ? 50   PHE J CE2 1 
ATOM   9290  C  CZ  . PHE I  1 50  ? 27.663 -2.113  -71.466  1.00 14.57 ? 50   PHE J CZ  1 
ATOM   9291  N  N   . GLY I  1 51  ? 25.895 4.686   -73.085  1.00 12.87 ? 51   GLY J N   1 
ATOM   9292  C  CA  . GLY I  1 51  ? 25.255 5.839   -73.715  1.00 14.04 ? 51   GLY J CA  1 
ATOM   9293  C  C   . GLY I  1 51  ? 24.498 5.372   -74.942  1.00 14.54 ? 51   GLY J C   1 
ATOM   9294  O  O   . GLY I  1 51  ? 24.652 5.914   -76.036  1.00 14.69 ? 51   GLY J O   1 
ATOM   9295  N  N   . ASP I  1 52  ? 23.680 4.349   -74.734  1.00 15.11 ? 52   ASP J N   1 
ATOM   9296  C  CA  . ASP I  1 52  ? 22.943 3.693   -75.792  1.00 15.73 ? 52   ASP J CA  1 
ATOM   9297  C  C   . ASP I  1 52  ? 21.447 3.851   -75.543  1.00 16.24 ? 52   ASP J C   1 
ATOM   9298  O  O   . ASP I  1 52  ? 20.889 3.207   -74.654  1.00 15.44 ? 52   ASP J O   1 
ATOM   9299  C  CB  . ASP I  1 52  ? 23.310 2.207   -75.791  1.00 15.31 ? 52   ASP J CB  1 
ATOM   9300  C  CG  . ASP I  1 52  ? 22.690 1.440   -76.955  1.00 16.71 ? 52   ASP J CG  1 
ATOM   9301  O  OD1 . ASP I  1 52  ? 23.218 0.365   -77.314  1.00 15.39 ? 52   ASP J OD1 1 
ATOM   9302  O  OD2 . ASP I  1 52  ? 21.675 1.911   -77.500  1.00 15.90 ? 52   ASP J OD2 1 
ATOM   9303  N  N   . ASN I  1 53  ? 20.794 4.698   -76.325  1.00 17.65 ? 53   ASN J N   1 
ATOM   9304  C  CA  . ASN I  1 53  ? 19.349 4.862   -76.182  1.00 18.85 ? 53   ASN J CA  1 
ATOM   9305  C  C   . ASN I  1 53  ? 18.547 4.304   -77.389  1.00 19.24 ? 53   ASN J C   1 
ATOM   9306  O  O   . ASN I  1 53  ? 17.451 4.777   -77.694  1.00 19.04 ? 53   ASN J O   1 
ATOM   9307  C  CB  . ASN I  1 53  ? 18.989 6.323   -75.822  1.00 19.87 ? 53   ASN J CB  1 
ATOM   9308  C  CG  . ASN I  1 53  ? 19.611 6.790   -74.465  1.00 21.50 ? 53   ASN J CG  1 
ATOM   9309  O  OD1 . ASN I  1 53  ? 19.698 7.994   -74.191  1.00 23.67 ? 53   ASN J OD1 1 
ATOM   9310  N  ND2 . ASN I  1 53  ? 20.030 5.839   -73.628  1.00 22.97 ? 53   ASN J ND2 1 
ATOM   9311  N  N   . THR I  1 54  ? 19.090 3.265   -78.034  1.00 19.24 ? 54   THR J N   1 
ATOM   9312  C  CA  . THR I  1 54  ? 18.458 2.645   -79.216  1.00 19.29 ? 54   THR J CA  1 
ATOM   9313  C  C   . THR I  1 54  ? 17.141 1.946   -78.894  1.00 19.67 ? 54   THR J C   1 
ATOM   9314  O  O   . THR I  1 54  ? 16.259 1.854   -79.752  1.00 19.97 ? 54   THR J O   1 
ATOM   9315  C  CB  . THR I  1 54  ? 19.397 1.658   -79.943  1.00 19.05 ? 54   THR J CB  1 
ATOM   9316  O  OG1 . THR I  1 54  ? 19.749 0.577   -79.071  1.00 19.81 ? 54   THR J OG1 1 
ATOM   9317  C  CG2 . THR I  1 54  ? 20.665 2.366   -80.438  1.00 19.45 ? 54   THR J CG2 1 
ATOM   9318  N  N   . ALA I  1 55  ? 17.000 1.460   -77.663  1.00 19.09 ? 55   ALA J N   1 
ATOM   9319  C  CA  . ALA I  1 55  ? 15.745 0.865   -77.226  1.00 19.30 ? 55   ALA J CA  1 
ATOM   9320  C  C   . ALA I  1 55  ? 15.138 1.666   -76.077  1.00 18.87 ? 55   ALA J C   1 
ATOM   9321  O  O   . ALA I  1 55  ? 14.542 1.096   -75.164  1.00 20.38 ? 55   ALA J O   1 
ATOM   9322  C  CB  . ALA I  1 55  ? 15.956 -0.594  -76.829  1.00 19.22 ? 55   ALA J CB  1 
ATOM   9323  N  N   . GLY I  1 56  ? 15.278 2.990   -76.121  1.00 18.24 ? 56   GLY J N   1 
ATOM   9324  C  CA  . GLY I  1 56  ? 14.851 3.834   -75.001  1.00 17.20 ? 56   GLY J CA  1 
ATOM   9325  C  C   . GLY I  1 56  ? 15.883 3.750   -73.881  1.00 16.56 ? 56   GLY J C   1 
ATOM   9326  O  O   . GLY I  1 56  ? 17.055 3.421   -74.132  1.00 16.90 ? 56   GLY J O   1 
ATOM   9327  N  N   . CYS I  1 57  ? 15.444 4.002   -72.647  1.00 15.56 ? 57   CYS J N   1 
ATOM   9328  C  CA  . CYS I  1 57  ? 16.346 4.001   -71.489  1.00 13.98 ? 57   CYS J CA  1 
ATOM   9329  C  C   . CYS I  1 57  ? 16.826 2.604   -71.104  1.00 14.88 ? 57   CYS J C   1 
ATOM   9330  O  O   . CYS I  1 57  ? 17.879 2.455   -70.456  1.00 14.24 ? 57   CYS J O   1 
ATOM   9331  C  CB  . CYS I  1 57  ? 15.696 4.715   -70.308  0.40 12.94 ? 57   CYS J CB  1 
ATOM   9332  S  SG  . CYS I  1 57  ? 15.267 6.432   -70.674  0.40 6.36  ? 57   CYS J SG  1 
ATOM   9333  N  N   . THR I  1 58  ? 16.070 1.588   -71.523  1.00 15.42 ? 58   THR J N   1 
ATOM   9334  C  CA  . THR I  1 58  ? 16.423 0.178   -71.277  1.00 16.37 ? 58   THR J CA  1 
ATOM   9335  C  C   . THR I  1 58  ? 17.818 -0.195  -71.794  1.00 15.62 ? 58   THR J C   1 
ATOM   9336  O  O   . THR I  1 58  ? 18.523 -0.980  -71.160  1.00 15.59 ? 58   THR J O   1 
ATOM   9337  C  CB  . THR I  1 58  ? 15.367 -0.767  -71.887  1.00 16.61 ? 58   THR J CB  1 
ATOM   9338  O  OG1 . THR I  1 58  ? 14.062 -0.305  -71.510  1.00 20.32 ? 58   THR J OG1 1 
ATOM   9339  C  CG2 . THR I  1 58  ? 15.568 -2.203  -71.411  1.00 18.49 ? 58   THR J CG2 1 
ATOM   9340  N  N   . SER I  1 59  ? 18.214 0.354   -72.941  1.00 15.18 ? 59   SER J N   1 
ATOM   9341  C  CA  . SER I  1 59  ? 19.470 -0.047  -73.568  1.00 15.06 ? 59   SER J CA  1 
ATOM   9342  C  C   . SER I  1 59  ? 20.702 0.614   -72.940  1.00 14.78 ? 59   SER J C   1 
ATOM   9343  O  O   . SER I  1 59  ? 21.834 0.329   -73.341  1.00 14.81 ? 59   SER J O   1 
ATOM   9344  C  CB  . SER I  1 59  ? 19.426 0.151   -75.094  1.00 15.59 ? 59   SER J CB  1 
ATOM   9345  O  OG  . SER I  1 59  ? 18.771 1.364   -75.425  1.00 17.04 ? 59   SER J OG  1 
ATOM   9346  N  N   . ALA I  1 60  ? 20.485 1.471   -71.934  1.00 14.28 ? 60   ALA J N   1 
ATOM   9347  C  CA  . ALA I  1 60  ? 21.592 2.020   -71.128  1.00 14.25 ? 60   ALA J CA  1 
ATOM   9348  C  C   . ALA I  1 60  ? 22.305 0.983   -70.248  1.00 13.67 ? 60   ALA J C   1 
ATOM   9349  O  O   . ALA I  1 60  ? 23.371 1.257   -69.681  1.00 14.26 ? 60   ALA J O   1 
ATOM   9350  C  CB  . ALA I  1 60  ? 21.107 3.220   -70.285  1.00 14.44 ? 60   ALA J CB  1 
ATOM   9351  N  N   . GLY I  1 61  ? 21.709 -0.192  -70.115  1.00 13.06 ? 61   GLY J N   1 
ATOM   9352  C  CA  . GLY I  1 61  ? 22.241 -1.233  -69.245  1.00 12.80 ? 61   GLY J CA  1 
ATOM   9353  C  C   . GLY I  1 61  ? 22.138 -0.887  -67.761  1.00 12.35 ? 61   GLY J C   1 
ATOM   9354  O  O   . GLY I  1 61  ? 21.271 -0.112  -67.354  1.00 12.52 ? 61   GLY J O   1 
ATOM   9355  N  N   . PRO I  1 62  ? 23.036 -1.453  -66.945  1.00 12.19 ? 62   PRO J N   1 
ATOM   9356  C  CA  . PRO I  1 62  ? 22.936 -1.315  -65.495  1.00 10.99 ? 62   PRO J CA  1 
ATOM   9357  C  C   . PRO I  1 62  ? 23.708 -0.086  -65.018  1.00 9.74  ? 62   PRO J C   1 
ATOM   9358  O  O   . PRO I  1 62  ? 24.198 0.689   -65.844  1.00 9.79  ? 62   PRO J O   1 
ATOM   9359  C  CB  . PRO I  1 62  ? 23.595 -2.601  -64.997  1.00 11.44 ? 62   PRO J CB  1 
ATOM   9360  C  CG  . PRO I  1 62  ? 24.724 -2.800  -65.998  1.00 12.01 ? 62   PRO J CG  1 
ATOM   9361  C  CD  . PRO I  1 62  ? 24.122 -2.376  -67.336  1.00 12.32 ? 62   PRO J CD  1 
ATOM   9362  N  N   . HIS I  1 63  ? 23.803 0.102   -63.704  1.00 8.63  ? 63   HIS J N   1 
ATOM   9363  C  CA  . HIS I  1 63  ? 24.529 1.253   -63.170  1.00 8.09  ? 63   HIS J CA  1 
ATOM   9364  C  C   . HIS I  1 63  ? 26.000 1.174   -63.564  1.00 7.91  ? 63   HIS J C   1 
ATOM   9365  O  O   . HIS I  1 63  ? 26.568 0.092   -63.593  1.00 7.47  ? 63   HIS J O   1 
ATOM   9366  C  CB  . HIS I  1 63  ? 24.359 1.318   -61.649  1.00 7.73  ? 63   HIS J CB  1 
ATOM   9367  C  CG  . HIS I  1 63  ? 22.941 1.530   -61.224  1.00 8.44  ? 63   HIS J CG  1 
ATOM   9368  N  ND1 . HIS I  1 63  ? 22.579 1.797   -59.922  1.00 8.57  ? 63   HIS J ND1 1 
ATOM   9369  C  CD2 . HIS I  1 63  ? 21.794 1.559   -61.943  1.00 7.82  ? 63   HIS J CD2 1 
ATOM   9370  C  CE1 . HIS I  1 63  ? 21.269 1.972   -59.857  1.00 8.72  ? 63   HIS J CE1 1 
ATOM   9371  N  NE2 . HIS I  1 63  ? 20.769 1.818   -61.066  1.00 9.60  ? 63   HIS J NE2 1 
ATOM   9372  N  N   . PHE I  1 64  ? 26.583 2.317   -63.920  1.00 7.71  ? 64   PHE J N   1 
ATOM   9373  C  CA  . PHE I  1 64  ? 28.022 2.414   -64.185  1.00 8.41  ? 64   PHE J CA  1 
ATOM   9374  C  C   . PHE I  1 64  ? 28.809 1.910   -62.976  1.00 8.80  ? 64   PHE J C   1 
ATOM   9375  O  O   . PHE I  1 64  ? 28.745 2.490   -61.893  1.00 7.58  ? 64   PHE J O   1 
ATOM   9376  C  CB  . PHE I  1 64  ? 28.394 3.854   -64.553  1.00 8.66  ? 64   PHE J CB  1 
ATOM   9377  C  CG  . PHE I  1 64  ? 29.837 4.042   -64.927  1.00 10.03 ? 64   PHE J CG  1 
ATOM   9378  C  CD1 . PHE I  1 64  ? 30.530 5.182   -64.510  1.00 9.62  ? 64   PHE J CD1 1 
ATOM   9379  C  CD2 . PHE I  1 64  ? 30.510 3.085   -65.689  1.00 10.28 ? 64   PHE J CD2 1 
ATOM   9380  C  CE1 . PHE I  1 64  ? 31.854 5.378   -64.861  1.00 11.58 ? 64   PHE J CE1 1 
ATOM   9381  C  CE2 . PHE I  1 64  ? 31.853 3.266   -66.035  1.00 11.10 ? 64   PHE J CE2 1 
ATOM   9382  C  CZ  . PHE I  1 64  ? 32.525 4.421   -65.628  1.00 11.73 ? 64   PHE J CZ  1 
ATOM   9383  N  N   . ASN I  1 65  ? 29.546 0.802   -63.176  1.00 8.93  ? 65   ASN J N   1 
ATOM   9384  C  CA  . ASN I  1 65  ? 30.110 0.048   -62.060  1.00 9.26  ? 65   ASN J CA  1 
ATOM   9385  C  C   . ASN I  1 65  ? 31.495 -0.557  -62.365  1.00 10.24 ? 65   ASN J C   1 
ATOM   9386  O  O   . ASN I  1 65  ? 31.674 -1.782  -62.254  1.00 9.87  ? 65   ASN J O   1 
ATOM   9387  C  CB  . ASN I  1 65  ? 29.138 -1.063  -61.631  1.00 9.96  ? 65   ASN J CB  1 
ATOM   9388  C  CG  . ASN I  1 65  ? 29.568 -1.750  -60.345  1.00 10.33 ? 65   ASN J CG  1 
ATOM   9389  O  OD1 . ASN I  1 65  ? 30.337 -1.185  -59.558  1.00 11.15 ? 65   ASN J OD1 1 
ATOM   9390  N  ND2 . ASN I  1 65  ? 29.078 -2.977  -60.125  1.00 11.15 ? 65   ASN J ND2 1 
ATOM   9391  N  N   . PRO I  1 66  ? 32.474 0.290   -62.724  1.00 10.18 ? 66   PRO J N   1 
ATOM   9392  C  CA  . PRO I  1 66  ? 33.785 -0.242  -63.117  1.00 11.72 ? 66   PRO J CA  1 
ATOM   9393  C  C   . PRO I  1 66  ? 34.575 -0.955  -62.001  1.00 13.02 ? 66   PRO J C   1 
ATOM   9394  O  O   . PRO I  1 66  ? 35.527 -1.674  -62.316  1.00 13.31 ? 66   PRO J O   1 
ATOM   9395  C  CB  . PRO I  1 66  ? 34.544 1.002   -63.584  1.00 11.14 ? 66   PRO J CB  1 
ATOM   9396  C  CG  . PRO I  1 66  ? 33.880 2.148   -62.847  1.00 9.95  ? 66   PRO J CG  1 
ATOM   9397  C  CD  . PRO I  1 66  ? 32.444 1.769   -62.766  1.00 9.47  ? 66   PRO J CD  1 
ATOM   9398  N  N   . LEU I  1 67  ? 34.222 -0.757  -60.727  1.00 13.88 ? 67   LEU J N   1 
ATOM   9399  C  CA  . LEU I  1 67  ? 34.955 -1.425  -59.637  1.00 14.73 ? 67   LEU J CA  1 
ATOM   9400  C  C   . LEU I  1 67  ? 34.201 -2.646  -59.117  1.00 14.71 ? 67   LEU J C   1 
ATOM   9401  O  O   . LEU I  1 67  ? 34.591 -3.255  -58.112  1.00 15.32 ? 67   LEU J O   1 
ATOM   9402  C  CB  . LEU I  1 67  ? 35.313 -0.459  -58.506  1.00 14.93 ? 67   LEU J CB  1 
ATOM   9403  C  CG  . LEU I  1 67  ? 35.994 0.870   -58.902  1.00 16.51 ? 67   LEU J CG  1 
ATOM   9404  C  CD1 . LEU I  1 67  ? 36.203 1.778   -57.699  1.00 17.60 ? 67   LEU J CD1 1 
ATOM   9405  C  CD2 . LEU I  1 67  ? 37.290 0.681   -59.667  1.00 19.23 ? 67   LEU J CD2 1 
ATOM   9406  N  N   . SER I  1 68  ? 33.130 -2.992  -59.819  1.00 14.33 ? 68   SER J N   1 
ATOM   9407  C  CA  . SER I  1 68  ? 32.311 -4.181  -59.539  1.00 15.33 ? 68   SER J CA  1 
ATOM   9408  C  C   . SER I  1 68  ? 31.913 -4.275  -58.068  1.00 15.26 ? 68   SER J C   1 
ATOM   9409  O  O   . SER I  1 68  ? 32.147 -5.288  -57.390  1.00 16.07 ? 68   SER J O   1 
ATOM   9410  C  CB  . SER I  1 68  ? 32.997 -5.462  -60.024  1.00 15.28 ? 68   SER J CB  1 
ATOM   9411  O  OG  . SER I  1 68  ? 33.253 -5.388  -61.413  1.00 16.11 ? 68   SER J OG  1 
ATOM   9412  N  N   . ARG I  1 69  ? 31.331 -3.183  -57.593  1.00 15.19 ? 69   ARG J N   1 
ATOM   9413  C  CA  . ARG I  1 69  ? 30.889 -3.051  -56.219  1.00 14.37 ? 69   ARG J CA  1 
ATOM   9414  C  C   . ARG I  1 69  ? 29.372 -3.174  -56.201  1.00 13.76 ? 69   ARG J C   1 
ATOM   9415  O  O   . ARG I  1 69  ? 28.752 -3.156  -57.250  1.00 12.63 ? 69   ARG J O   1 
ATOM   9416  C  CB  . ARG I  1 69  ? 31.339 -1.700  -55.657  1.00 14.83 ? 69   ARG J CB  1 
ATOM   9417  C  CG  . ARG I  1 69  ? 32.855 -1.562  -55.534  1.00 17.84 ? 69   ARG J CG  1 
ATOM   9418  C  CD  . ARG I  1 69  ? 33.267 -0.439  -54.582  1.00 21.88 ? 69   ARG J CD  1 
ATOM   9419  N  NE  . ARG I  1 69  ? 34.729 -0.306  -54.523  1.00 24.59 ? 69   ARG J NE  1 
ATOM   9420  C  CZ  . ARG I  1 69  ? 35.385 0.723   -53.988  1.00 24.57 ? 69   ARG J CZ  1 
ATOM   9421  N  NH1 . ARG I  1 69  ? 36.712 0.734   -53.996  1.00 27.12 ? 69   ARG J NH1 1 
ATOM   9422  N  NH2 . ARG I  1 69  ? 34.729 1.739   -53.437  1.00 26.48 ? 69   ARG J NH2 1 
ATOM   9423  N  N   . LYS I  1 70  ? 28.796 -3.317  -55.008  1.00 13.67 ? 70   LYS J N   1 
ATOM   9424  C  CA  . LYS I  1 70  ? 27.346 -3.403  -54.827  1.00 12.55 ? 70   LYS J CA  1 
ATOM   9425  C  C   . LYS I  1 70  ? 26.762 -1.983  -54.853  1.00 11.65 ? 70   LYS J C   1 
ATOM   9426  O  O   . LYS I  1 70  ? 27.487 -0.992  -54.698  1.00 11.16 ? 70   LYS J O   1 
ATOM   9427  C  CB  . LYS I  1 70  ? 26.991 -4.114  -53.505  1.00 13.06 ? 70   LYS J CB  1 
ATOM   9428  C  CG  . LYS I  1 70  ? 27.530 -5.555  -53.363  1.00 15.90 ? 70   LYS J CG  1 
ATOM   9429  C  CD  . LYS I  1 70  ? 27.365 -6.076  -51.942  1.00 19.87 ? 70   LYS J CD  1 
ATOM   9430  C  CE  . LYS I  1 70  ? 27.746 -7.555  -51.815  1.00 23.34 ? 70   LYS J CE  1 
ATOM   9431  N  NZ  . LYS I  1 70  ? 27.606 -8.045  -50.397  1.00 24.94 ? 70   LYS J NZ  1 
ATOM   9432  N  N   . HIS I  1 71  ? 25.459 -1.894  -55.087  1.00 10.79 ? 71   HIS J N   1 
ATOM   9433  C  CA  . HIS I  1 71  ? 24.769 -0.602  -55.125  1.00 9.83  ? 71   HIS J CA  1 
ATOM   9434  C  C   . HIS I  1 71  ? 24.758 0.009   -53.726  1.00 9.22  ? 71   HIS J C   1 
ATOM   9435  O  O   . HIS I  1 71  ? 24.613 -0.708  -52.755  1.00 9.33  ? 71   HIS J O   1 
ATOM   9436  C  CB  . HIS I  1 71  ? 23.324 -0.773  -55.617  1.00 9.24  ? 71   HIS J CB  1 
ATOM   9437  C  CG  . HIS I  1 71  ? 22.530 0.499   -55.614  1.00 10.01 ? 71   HIS J CG  1 
ATOM   9438  N  ND1 . HIS I  1 71  ? 22.668 1.464   -56.585  1.00 8.75  ? 71   HIS J ND1 1 
ATOM   9439  C  CD2 . HIS I  1 71  ? 21.595 0.962   -54.752  1.00 7.94  ? 71   HIS J CD2 1 
ATOM   9440  C  CE1 . HIS I  1 71  ? 21.847 2.468   -56.326  1.00 8.95  ? 71   HIS J CE1 1 
ATOM   9441  N  NE2 . HIS I  1 71  ? 21.192 2.188   -55.214  1.00 9.92  ? 71   HIS J NE2 1 
ATOM   9442  N  N   . GLY I  1 72  ? 24.911 1.331   -53.656  1.00 9.04  ? 72   GLY J N   1 
ATOM   9443  C  CA  . GLY I  1 72  ? 24.772 2.089   -52.408  1.00 8.01  ? 72   GLY J CA  1 
ATOM   9444  C  C   . GLY I  1 72  ? 24.339 3.525   -52.679  1.00 7.20  ? 72   GLY J C   1 
ATOM   9445  O  O   . GLY I  1 72  ? 23.950 3.881   -53.800  1.00 6.74  ? 72   GLY J O   1 
ATOM   9446  N  N   . GLY I  1 73  ? 24.389 4.347   -51.637  1.00 7.25  ? 73   GLY J N   1 
ATOM   9447  C  CA  . GLY I  1 73  ? 24.101 5.765   -51.776  1.00 7.54  ? 73   GLY J CA  1 
ATOM   9448  C  C   . GLY I  1 73  ? 25.410 6.465   -52.057  1.00 7.72  ? 73   GLY J C   1 
ATOM   9449  O  O   . GLY I  1 73  ? 26.467 5.857   -51.882  1.00 8.33  ? 73   GLY J O   1 
ATOM   9450  N  N   . PRO I  1 74  ? 25.358 7.726   -52.523  1.00 7.90  ? 74   PRO J N   1 
ATOM   9451  C  CA  . PRO I  1 74  ? 26.575 8.455   -52.869  1.00 7.95  ? 74   PRO J CA  1 
ATOM   9452  C  C   . PRO I  1 74  ? 27.544 8.647   -51.702  1.00 9.15  ? 74   PRO J C   1 
ATOM   9453  O  O   . PRO I  1 74  ? 28.739 8.827   -51.914  1.00 9.05  ? 74   PRO J O   1 
ATOM   9454  C  CB  . PRO I  1 74  ? 26.055 9.833   -53.302  1.00 7.54  ? 74   PRO J CB  1 
ATOM   9455  C  CG  . PRO I  1 74  ? 24.620 9.897   -52.791  1.00 8.46  ? 74   PRO J CG  1 
ATOM   9456  C  CD  . PRO I  1 74  ? 24.146 8.496   -52.843  1.00 7.48  ? 74   PRO J CD  1 
ATOM   9457  N  N   . LYS I  1 75  ? 27.022 8.630   -50.480  1.00 10.58 ? 75   LYS J N   1 
ATOM   9458  C  CA  . LYS I  1 75  ? 27.859 8.779   -49.298  1.00 12.35 ? 75   LYS J CA  1 
ATOM   9459  C  C   . LYS I  1 75  ? 28.648 7.514   -48.946  1.00 12.29 ? 75   LYS J C   1 
ATOM   9460  O  O   . LYS I  1 75  ? 29.591 7.585   -48.170  1.00 12.74 ? 75   LYS J O   1 
ATOM   9461  C  CB  . LYS I  1 75  ? 27.004 9.190   -48.087  1.00 12.71 ? 75   LYS J CB  1 
ATOM   9462  C  CG  . LYS I  1 75  ? 26.412 10.587  -48.185  1.00 15.18 ? 75   LYS J CG  1 
ATOM   9463  C  CD  . LYS I  1 75  ? 25.378 10.836  -47.076  1.00 16.06 ? 75   LYS J CD  1 
ATOM   9464  C  CE  . LYS I  1 75  ? 26.034 11.114  -45.745  1.00 18.07 ? 75   LYS J CE  1 
ATOM   9465  N  NZ  . LYS I  1 75  ? 24.983 11.430  -44.713  1.00 21.17 ? 75   LYS J NZ  1 
ATOM   9466  N  N   . ASP I  1 76  ? 28.240 6.358   -49.475  1.00 12.80 ? 76   ASP J N   1 
ATOM   9467  C  CA  . ASP I  1 76  ? 28.860 5.078   -49.133  1.00 13.20 ? 76   ASP J CA  1 
ATOM   9468  C  C   . ASP I  1 76  ? 30.155 4.778   -49.874  1.00 13.92 ? 76   ASP J C   1 
ATOM   9469  O  O   . ASP I  1 76  ? 30.278 5.080   -51.063  1.00 13.15 ? 76   ASP J O   1 
ATOM   9470  C  CB  . ASP I  1 76  ? 27.905 3.925   -49.433  1.00 12.95 ? 76   ASP J CB  1 
ATOM   9471  C  CG  . ASP I  1 76  ? 26.685 3.948   -48.568  1.00 14.70 ? 76   ASP J CG  1 
ATOM   9472  O  OD1 . ASP I  1 76  ? 25.589 3.692   -49.108  1.00 13.72 ? 76   ASP J OD1 1 
ATOM   9473  O  OD2 . ASP I  1 76  ? 26.822 4.233   -47.351  1.00 16.29 ? 76   ASP J OD2 1 
ATOM   9474  N  N   . GLU I  1 77  ? 31.094 4.146   -49.173  1.00 13.95 ? 77   GLU J N   1 
ATOM   9475  C  CA  . GLU I  1 77  ? 32.285 3.573   -49.817  1.00 15.31 ? 77   GLU J CA  1 
ATOM   9476  C  C   . GLU I  1 77  ? 31.892 2.453   -50.776  1.00 13.86 ? 77   GLU J C   1 
ATOM   9477  O  O   . GLU I  1 77  ? 32.363 2.400   -51.899  1.00 13.63 ? 77   GLU J O   1 
ATOM   9478  C  CB  . GLU I  1 77  ? 33.268 3.041   -48.767  1.00 15.84 ? 77   GLU J CB  1 
ATOM   9479  C  CG  . GLU I  1 77  ? 34.039 4.130   -48.023  1.00 22.33 ? 77   GLU J CG  1 
ATOM   9480  C  CD  . GLU I  1 77  ? 35.092 4.830   -48.888  1.00 27.86 ? 77   GLU J CD  1 
ATOM   9481  O  OE1 . GLU I  1 77  ? 35.621 5.879   -48.445  1.00 29.24 ? 77   GLU J OE1 1 
ATOM   9482  O  OE2 . GLU I  1 77  ? 35.388 4.338   -50.004  1.00 28.95 ? 77   GLU J OE2 1 
ATOM   9483  N  N   . GLU I  1 78  ? 31.004 1.569   -50.325  1.00 12.87 ? 78   GLU J N   1 
ATOM   9484  C  CA  . GLU I  1 78  ? 30.461 0.532   -51.186  1.00 12.44 ? 78   GLU J CA  1 
ATOM   9485  C  C   . GLU I  1 78  ? 29.318 1.112   -52.046  1.00 11.46 ? 78   GLU J C   1 
ATOM   9486  O  O   . GLU I  1 78  ? 28.164 1.205   -51.606  1.00 10.51 ? 78   GLU J O   1 
ATOM   9487  C  CB  . GLU I  1 78  ? 29.964 -0.653  -50.344  1.00 12.96 ? 78   GLU J CB  1 
ATOM   9488  C  CG  . GLU I  1 78  ? 29.576 -1.889  -51.159  1.00 14.49 ? 78   GLU J CG  1 
ATOM   9489  C  CD  . GLU I  1 78  ? 30.767 -2.573  -51.861  1.00 16.09 ? 78   GLU J CD  1 
ATOM   9490  O  OE1 . GLU I  1 78  ? 30.514 -3.354  -52.796  1.00 16.54 ? 78   GLU J OE1 1 
ATOM   9491  O  OE2 . GLU I  1 78  ? 31.943 -2.347  -51.486  1.00 17.81 ? 78   GLU J OE2 1 
ATOM   9492  N  N   . ARG I  1 79  ? 29.656 1.496   -53.271  1.00 10.17 ? 79   ARG J N   1 
ATOM   9493  C  CA  . ARG I  1 79  ? 28.679 2.031   -54.210  1.00 9.07  ? 79   ARG J CA  1 
ATOM   9494  C  C   . ARG I  1 79  ? 29.177 1.789   -55.607  1.00 8.64  ? 79   ARG J C   1 
ATOM   9495  O  O   . ARG I  1 79  ? 30.371 1.554   -55.814  1.00 8.65  ? 79   ARG J O   1 
ATOM   9496  C  CB  . ARG I  1 79  ? 28.468 3.541   -53.998  1.00 8.32  ? 79   ARG J CB  1 
ATOM   9497  C  CG  . ARG I  1 79  ? 29.762 4.376   -54.080  1.00 7.97  ? 79   ARG J CG  1 
ATOM   9498  C  CD  . ARG I  1 79  ? 29.444 5.865   -54.071  1.00 6.29  ? 79   ARG J CD  1 
ATOM   9499  N  NE  . ARG I  1 79  ? 29.161 6.376   -55.411  1.00 6.45  ? 79   ARG J NE  1 
ATOM   9500  C  CZ  . ARG I  1 79  ? 29.156 7.671   -55.705  1.00 7.81  ? 79   ARG J CZ  1 
ATOM   9501  N  NH1 . ARG I  1 79  ? 28.921 8.073   -56.938  1.00 9.13  ? 79   ARG J NH1 1 
ATOM   9502  N  NH2 . ARG I  1 79  ? 29.377 8.570   -54.749  1.00 6.80  ? 79   ARG J NH2 1 
ATOM   9503  N  N   . HIS I  1 80  ? 28.248 1.846   -56.559  1.00 7.60  ? 80   HIS J N   1 
ATOM   9504  C  CA  . HIS I  1 80  ? 28.606 1.976   -57.968  1.00 7.58  ? 80   HIS J CA  1 
ATOM   9505  C  C   . HIS I  1 80  ? 29.105 3.389   -58.216  1.00 7.20  ? 80   HIS J C   1 
ATOM   9506  O  O   . HIS I  1 80  ? 28.638 4.333   -57.576  1.00 7.55  ? 80   HIS J O   1 
ATOM   9507  C  CB  . HIS I  1 80  ? 27.352 1.690   -58.839  1.00 5.86  ? 80   HIS J CB  1 
ATOM   9508  C  CG  . HIS I  1 80  ? 26.759 0.336   -58.618  1.00 6.57  ? 80   HIS J CG  1 
ATOM   9509  N  ND1 . HIS I  1 80  ? 25.402 0.088   -58.682  1.00 7.13  ? 80   HIS J ND1 1 
ATOM   9510  C  CD2 . HIS I  1 80  ? 27.346 -0.861  -58.365  1.00 8.19  ? 80   HIS J CD2 1 
ATOM   9511  C  CE1 . HIS I  1 80  ? 25.179 -1.199  -58.473  1.00 8.84  ? 80   HIS J CE1 1 
ATOM   9512  N  NE2 . HIS I  1 80  ? 26.343 -1.794  -58.264  1.00 8.01  ? 80   HIS J NE2 1 
ATOM   9513  N  N   . VAL I  1 81  ? 30.043 3.566   -59.148  1.00 7.58  ? 81   VAL J N   1 
ATOM   9514  C  CA  . VAL I  1 81  ? 30.464 4.924   -59.525  1.00 7.45  ? 81   VAL J CA  1 
ATOM   9515  C  C   . VAL I  1 81  ? 29.254 5.779   -59.945  1.00 8.26  ? 81   VAL J C   1 
ATOM   9516  O  O   . VAL I  1 81  ? 29.189 6.974   -59.645  1.00 7.12  ? 81   VAL J O   1 
ATOM   9517  C  CB  . VAL I  1 81  ? 31.546 4.907   -60.644  1.00 8.28  ? 81   VAL J CB  1 
ATOM   9518  C  CG1 . VAL I  1 81  ? 31.733 6.283   -61.247  1.00 6.61  ? 81   VAL J CG1 1 
ATOM   9519  C  CG2 . VAL I  1 81  ? 32.876 4.421   -60.065  1.00 7.88  ? 81   VAL J CG2 1 
ATOM   9520  N  N   . GLY I  1 82  ? 28.280 5.136   -60.598  1.00 7.91  ? 82   GLY J N   1 
ATOM   9521  C  CA  . GLY I  1 82  ? 27.091 5.818   -61.082  1.00 8.25  ? 82   GLY J CA  1 
ATOM   9522  C  C   . GLY I  1 82  ? 26.050 6.183   -60.039  1.00 8.15  ? 82   GLY J C   1 
ATOM   9523  O  O   . GLY I  1 82  ? 25.040 6.805   -60.389  1.00 8.52  ? 82   GLY J O   1 
ATOM   9524  N  N   . ASP I  1 83  ? 26.288 5.863   -58.769  1.00 7.47  ? 83   ASP J N   1 
ATOM   9525  C  CA  . ASP I  1 83  ? 25.236 6.014   -57.749  1.00 8.19  ? 83   ASP J CA  1 
ATOM   9526  C  C   . ASP I  1 83  ? 25.130 7.412   -57.179  1.00 8.61  ? 83   ASP J C   1 
ATOM   9527  O  O   . ASP I  1 83  ? 25.877 7.786   -56.271  1.00 9.92  ? 83   ASP J O   1 
ATOM   9528  C  CB  . ASP I  1 83  ? 25.414 5.020   -56.613  1.00 7.68  ? 83   ASP J CB  1 
ATOM   9529  C  CG  . ASP I  1 83  ? 25.137 3.612   -57.034  1.00 6.57  ? 83   ASP J CG  1 
ATOM   9530  O  OD1 . ASP I  1 83  ? 24.502 3.402   -58.096  1.00 4.48  ? 83   ASP J OD1 1 
ATOM   9531  O  OD2 . ASP I  1 83  ? 25.546 2.715   -56.288  1.00 5.97  ? 83   ASP J OD2 1 
ATOM   9532  N  N   . LEU I  1 84  ? 24.194 8.194   -57.694  1.00 9.12  ? 84   LEU J N   1 
ATOM   9533  C  CA  . LEU I  1 84  ? 24.034 9.546   -57.177  1.00 9.34  ? 84   LEU J CA  1 
ATOM   9534  C  C   . LEU I  1 84  ? 22.840 9.724   -56.233  1.00 10.42 ? 84   LEU J C   1 
ATOM   9535  O  O   . LEU I  1 84  ? 22.486 10.858  -55.876  1.00 11.16 ? 84   LEU J O   1 
ATOM   9536  C  CB  . LEU I  1 84  ? 23.988 10.544  -58.330  1.00 9.61  ? 84   LEU J CB  1 
ATOM   9537  C  CG  . LEU I  1 84  ? 25.198 10.526  -59.264  1.00 8.72  ? 84   LEU J CG  1 
ATOM   9538  C  CD1 . LEU I  1 84  ? 24.826 11.428  -60.439  1.00 9.33  ? 84   LEU J CD1 1 
ATOM   9539  C  CD2 . LEU I  1 84  ? 26.495 10.972  -58.540  1.00 9.84  ? 84   LEU J CD2 1 
ATOM   9540  N  N   . GLY I  1 85  ? 22.220 8.613   -55.840  1.00 10.15 ? 85   GLY J N   1 
ATOM   9541  C  CA  . GLY I  1 85  ? 21.167 8.627   -54.849  1.00 9.86  ? 85   GLY J CA  1 
ATOM   9542  C  C   . GLY I  1 85  ? 19.849 9.121   -55.393  1.00 9.91  ? 85   GLY J C   1 
ATOM   9543  O  O   . GLY I  1 85  ? 19.393 8.648   -56.435  1.00 9.57  ? 85   GLY J O   1 
ATOM   9544  N  N   . ASN I  1 86  ? 19.255 10.090  -54.690  1.00 9.63  ? 86   ASN J N   1 
ATOM   9545  C  CA  . ASN I  1 86  ? 17.921 10.597  -55.038  1.00 10.05 ? 86   ASN J CA  1 
ATOM   9546  C  C   . ASN I  1 86  ? 17.872 12.069  -55.375  1.00 9.30  ? 86   ASN J C   1 
ATOM   9547  O  O   . ASN I  1 86  ? 18.683 12.868  -54.901  1.00 9.56  ? 86   ASN J O   1 
ATOM   9548  C  CB  . ASN I  1 86  ? 16.930 10.330  -53.900  1.00 10.06 ? 86   ASN J CB  1 
ATOM   9549  C  CG  . ASN I  1 86  ? 16.583 8.872   -53.775  1.00 10.20 ? 86   ASN J CG  1 
ATOM   9550  O  OD1 . ASN I  1 86  ? 16.079 8.268   -54.708  1.00 9.37  ? 86   ASN J OD1 1 
ATOM   9551  N  ND2 . ASN I  1 86  ? 16.842 8.306   -52.617  1.00 8.42  ? 86   ASN J ND2 1 
ATOM   9552  N  N   . VAL I  1 87  ? 16.899 12.424  -56.200  1.00 9.94  ? 87   VAL J N   1 
ATOM   9553  C  CA  . VAL I  1 87  ? 16.492 13.806  -56.324  1.00 10.18 ? 87   VAL J CA  1 
ATOM   9554  C  C   . VAL I  1 87  ? 15.085 13.893  -55.724  1.00 10.91 ? 87   VAL J C   1 
ATOM   9555  O  O   . VAL I  1 87  ? 14.419 12.871  -55.561  1.00 10.32 ? 87   VAL J O   1 
ATOM   9556  C  CB  . VAL I  1 87  ? 16.560 14.306  -57.783  1.00 10.08 ? 87   VAL J CB  1 
ATOM   9557  C  CG1 . VAL I  1 87  ? 18.024 14.345  -58.238  1.00 9.85  ? 87   VAL J CG1 1 
ATOM   9558  C  CG2 . VAL I  1 87  ? 15.725 13.404  -58.728  1.00 10.39 ? 87   VAL J CG2 1 
ATOM   9559  N  N   . THR I  1 88  ? 14.657 15.099  -55.362  1.00 11.51 ? 88   THR J N   1 
ATOM   9560  C  CA  . THR I  1 88  ? 13.349 15.308  -54.693  1.00 12.53 ? 88   THR J CA  1 
ATOM   9561  C  C   . THR I  1 88  ? 12.470 16.211  -55.562  1.00 13.26 ? 88   THR J C   1 
ATOM   9562  O  O   . THR I  1 88  ? 12.862 17.349  -55.874  1.00 13.49 ? 88   THR J O   1 
ATOM   9563  C  CB  . THR I  1 88  ? 13.514 15.958  -53.291  1.00 12.32 ? 88   THR J CB  1 
ATOM   9564  O  OG1 . THR I  1 88  ? 14.407 15.178  -52.493  1.00 12.95 ? 88   THR J OG1 1 
ATOM   9565  C  CG2 . THR I  1 88  ? 12.170 16.063  -52.559  1.00 12.67 ? 88   THR J CG2 1 
ATOM   9566  N  N   . ALA I  1 89  ? 11.298 15.718  -55.959  1.00 14.15 ? 89   ALA J N   1 
ATOM   9567  C  CA  . ALA I  1 89  ? 10.347 16.567  -56.688  1.00 15.29 ? 89   ALA J CA  1 
ATOM   9568  C  C   . ALA I  1 89  ? 9.379  17.267  -55.724  1.00 15.99 ? 89   ALA J C   1 
ATOM   9569  O  O   . ALA I  1 89  ? 8.880  16.644  -54.795  1.00 15.76 ? 89   ALA J O   1 
ATOM   9570  C  CB  . ALA I  1 89  ? 9.575  15.751  -57.719  1.00 14.35 ? 89   ALA J CB  1 
ATOM   9571  N  N   . ASP I  1 90  ? 9.121  18.557  -55.960  1.00 17.42 ? 90   ASP J N   1 
ATOM   9572  C  CA  . ASP I  1 90  ? 8.124  19.311  -55.177  1.00 18.77 ? 90   ASP J CA  1 
ATOM   9573  C  C   . ASP I  1 90  ? 6.701  18.965  -55.640  1.00 19.72 ? 90   ASP J C   1 
ATOM   9574  O  O   . ASP I  1 90  ? 6.525  18.206  -56.604  1.00 19.99 ? 90   ASP J O   1 
ATOM   9575  C  CB  . ASP I  1 90  ? 8.399  20.823  -55.251  1.00 19.26 ? 90   ASP J CB  1 
ATOM   9576  C  CG  . ASP I  1 90  ? 8.173  21.418  -56.649  1.00 20.77 ? 90   ASP J CG  1 
ATOM   9577  O  OD1 . ASP I  1 90  ? 8.645  22.543  -56.887  1.00 24.85 ? 90   ASP J OD1 1 
ATOM   9578  O  OD2 . ASP I  1 90  ? 7.512  20.799  -57.508  1.00 23.53 ? 90   ASP J OD2 1 
ATOM   9579  N  N   . LYS I  1 91  ? 5.688  19.506  -54.960  1.00 20.66 ? 91   LYS J N   1 
ATOM   9580  C  CA  . LYS I  1 91  ? 4.282  19.241  -55.320  1.00 21.82 ? 91   LYS J CA  1 
ATOM   9581  C  C   . LYS I  1 91  ? 3.947  19.533  -56.790  1.00 21.62 ? 91   LYS J C   1 
ATOM   9582  O  O   . LYS I  1 91  ? 3.092  18.862  -57.377  1.00 22.29 ? 91   LYS J O   1 
ATOM   9583  C  CB  . LYS I  1 91  ? 3.324  19.986  -54.371  1.00 22.20 ? 91   LYS J CB  1 
ATOM   9584  C  CG  . LYS I  1 91  ? 1.853  20.098  -54.839  1.00 24.63 ? 91   LYS J CG  1 
ATOM   9585  C  CD  . LYS I  1 91  ? 1.108  18.770  -54.824  1.00 27.01 ? 91   LYS J CD  1 
ATOM   9586  C  CE  . LYS I  1 91  ? 0.510  18.473  -53.456  1.00 29.25 ? 91   LYS J CE  1 
ATOM   9587  N  NZ  . LYS I  1 91  ? 0.281  17.003  -53.310  1.00 29.71 ? 91   LYS J NZ  1 
ATOM   9588  N  N   . ASP I  1 92  ? 4.627  20.506  -57.388  1.00 21.16 ? 92   ASP J N   1 
ATOM   9589  C  CA  . ASP I  1 92  ? 4.390  20.835  -58.787  1.00 21.68 ? 92   ASP J CA  1 
ATOM   9590  C  C   . ASP I  1 92  ? 5.095  19.899  -59.771  1.00 20.98 ? 92   ASP J C   1 
ATOM   9591  O  O   . ASP I  1 92  ? 4.983  20.083  -60.992  1.00 21.17 ? 92   ASP J O   1 
ATOM   9592  C  CB  . ASP I  1 92  ? 4.784  22.286  -59.060  1.00 22.10 ? 92   ASP J CB  1 
ATOM   9593  C  CG  . ASP I  1 92  ? 3.828  23.277  -58.426  1.00 24.84 ? 92   ASP J CG  1 
ATOM   9594  O  OD1 . ASP I  1 92  ? 4.191  24.475  -58.352  1.00 28.13 ? 92   ASP J OD1 1 
ATOM   9595  O  OD2 . ASP I  1 92  ? 2.719  22.863  -57.999  1.00 27.35 ? 92   ASP J OD2 1 
ATOM   9596  N  N   . GLY I  1 93  ? 5.813  18.907  -59.243  1.00 20.10 ? 93   GLY J N   1 
ATOM   9597  C  CA  . GLY I  1 93  ? 6.527  17.926  -60.071  1.00 18.63 ? 93   GLY J CA  1 
ATOM   9598  C  C   . GLY I  1 93  ? 7.912  18.328  -60.563  1.00 18.15 ? 93   GLY J C   1 
ATOM   9599  O  O   . GLY I  1 93  ? 8.467  17.689  -61.479  1.00 17.68 ? 93   GLY J O   1 
ATOM   9600  N  N   . VAL I  1 94  ? 8.481  19.366  -59.949  1.00 16.76 ? 94   VAL J N   1 
ATOM   9601  C  CA  . VAL I  1 94  ? 9.793  19.864  -60.330  1.00 16.15 ? 94   VAL J CA  1 
ATOM   9602  C  C   . VAL I  1 94  ? 10.837 19.548  -59.269  1.00 15.70 ? 94   VAL J C   1 
ATOM   9603  O  O   . VAL I  1 94  ? 10.640 19.814  -58.087  1.00 16.05 ? 94   VAL J O   1 
ATOM   9604  C  CB  . VAL I  1 94  ? 9.800  21.384  -60.629  1.00 16.01 ? 94   VAL J CB  1 
ATOM   9605  C  CG1 . VAL I  1 94  ? 11.180 21.813  -61.157  1.00 15.96 ? 94   VAL J CG1 1 
ATOM   9606  C  CG2 . VAL I  1 94  ? 8.716  21.741  -61.654  1.00 15.29 ? 94   VAL J CG2 1 
ATOM   9607  N  N   . ALA I  1 95  ? 11.944 18.969  -59.725  1.00 15.52 ? 95   ALA J N   1 
ATOM   9608  C  CA  . ALA I  1 95  ? 13.085 18.668  -58.884  1.00 15.04 ? 95   ALA J CA  1 
ATOM   9609  C  C   . ALA I  1 95  ? 14.192 19.604  -59.328  1.00 15.50 ? 95   ALA J C   1 
ATOM   9610  O  O   . ALA I  1 95  ? 14.565 19.625  -60.512  1.00 15.14 ? 95   ALA J O   1 
ATOM   9611  C  CB  . ALA I  1 95  ? 13.507 17.193  -59.059  1.00 14.82 ? 95   ALA J CB  1 
ATOM   9612  N  N   . ASP I  1 96  ? 14.682 20.412  -58.394  1.00 15.53 ? 96   ASP J N   1 
ATOM   9613  C  CA  . ASP I  1 96  ? 15.792 21.308  -58.671  1.00 16.56 ? 96   ASP J CA  1 
ATOM   9614  C  C   . ASP I  1 96  ? 17.019 20.596  -58.148  1.00 15.96 ? 96   ASP J C   1 
ATOM   9615  O  O   . ASP I  1 96  ? 17.199 20.482  -56.949  1.00 17.66 ? 96   ASP J O   1 
ATOM   9616  C  CB  . ASP I  1 96  ? 15.591 22.665  -57.979  1.00 16.88 ? 96   ASP J CB  1 
ATOM   9617  C  CG  . ASP I  1 96  ? 14.487 23.495  -58.629  1.00 19.73 ? 96   ASP J CG  1 
ATOM   9618  O  OD1 . ASP I  1 96  ? 14.418 23.575  -59.880  1.00 21.91 ? 96   ASP J OD1 1 
ATOM   9619  O  OD2 . ASP I  1 96  ? 13.664 24.063  -57.879  1.00 24.95 ? 96   ASP J OD2 1 
ATOM   9620  N  N   . VAL I  1 97  ? 17.844 20.089  -59.049  1.00 15.49 ? 97   VAL J N   1 
ATOM   9621  C  CA  . VAL I  1 97  ? 18.918 19.171  -58.663  1.00 14.51 ? 97   VAL J CA  1 
ATOM   9622  C  C   . VAL I  1 97  ? 20.153 19.967  -58.306  1.00 13.99 ? 97   VAL J C   1 
ATOM   9623  O  O   . VAL I  1 97  ? 20.546 20.870  -59.033  1.00 14.08 ? 97   VAL J O   1 
ATOM   9624  C  CB  . VAL I  1 97  ? 19.201 18.156  -59.810  1.00 14.80 ? 97   VAL J CB  1 
ATOM   9625  C  CG1 . VAL I  1 97  ? 20.335 17.177  -59.448  1.00 14.28 ? 97   VAL J CG1 1 
ATOM   9626  C  CG2 . VAL I  1 97  ? 17.933 17.394  -60.114  1.00 14.34 ? 97   VAL J CG2 1 
ATOM   9627  N  N   . SER I  1 98  ? 20.741 19.647  -57.165  1.00 13.69 ? 98   SER J N   1 
ATOM   9628  C  CA  . SER I  1 98  ? 22.014 20.220  -56.782  1.00 13.32 ? 98   SER J CA  1 
ATOM   9629  C  C   . SER I  1 98  ? 22.753 19.222  -55.904  1.00 13.28 ? 98   SER J C   1 
ATOM   9630  O  O   . SER I  1 98  ? 22.374 18.956  -54.756  1.00 12.41 ? 98   SER J O   1 
ATOM   9631  C  CB  . SER I  1 98  ? 21.846 21.593  -56.119  1.00 13.60 ? 98   SER J CB  1 
ATOM   9632  O  OG  . SER I  1 98  ? 23.107 22.219  -55.951  1.00 14.42 ? 98   SER J OG  1 
ATOM   9633  N  N   . ILE I  1 99  ? 23.809 18.660  -56.486  1.00 12.61 ? 99   ILE J N   1 
ATOM   9634  C  CA  . ILE I  1 99  ? 24.544 17.532  -55.935  1.00 12.85 ? 99   ILE J CA  1 
ATOM   9635  C  C   . ILE I  1 99  ? 26.030 17.805  -56.183  1.00 13.22 ? 99   ILE J C   1 
ATOM   9636  O  O   . ILE I  1 99  ? 26.397 18.400  -57.209  1.00 12.69 ? 99   ILE J O   1 
ATOM   9637  C  CB  . ILE I  1 99  ? 24.080 16.192  -56.616  1.00 13.47 ? 99   ILE J CB  1 
ATOM   9638  C  CG1 . ILE I  1 99  ? 22.725 15.742  -56.051  1.00 12.09 ? 99   ILE J CG1 1 
ATOM   9639  C  CG2 . ILE I  1 99  ? 25.133 15.055  -56.513  1.00 13.44 ? 99   ILE J CG2 1 
ATOM   9640  C  CD1 . ILE I  1 99  ? 22.093 14.578  -56.804  1.00 16.31 ? 99   ILE J CD1 1 
ATOM   9641  N  N   . GLU I  1 100 ? 26.878 17.420  -55.232  1.00 12.95 ? 100  GLU J N   1 
ATOM   9642  C  CA  . GLU I  1 100 ? 28.316 17.399  -55.489  1.00 13.30 ? 100  GLU J CA  1 
ATOM   9643  C  C   . GLU I  1 100 ? 28.807 16.006  -55.179  1.00 12.55 ? 100  GLU J C   1 
ATOM   9644  O  O   . GLU I  1 100 ? 28.427 15.425  -54.154  1.00 11.59 ? 100  GLU J O   1 
ATOM   9645  C  CB  . GLU I  1 100 ? 29.068 18.450  -54.667  1.00 14.40 ? 100  GLU J CB  1 
ATOM   9646  C  CG  . GLU I  1 100 ? 30.239 19.047  -55.455  1.00 20.41 ? 100  GLU J CG  1 
ATOM   9647  C  CD  . GLU I  1 100 ? 31.064 20.031  -54.653  1.00 26.21 ? 100  GLU J CD  1 
ATOM   9648  O  OE1 . GLU I  1 100 ? 32.122 20.464  -55.167  1.00 29.85 ? 100  GLU J OE1 1 
ATOM   9649  O  OE2 . GLU I  1 100 ? 30.660 20.376  -53.521  1.00 28.87 ? 100  GLU J OE2 1 
ATOM   9650  N  N   . ASP I  1 101 ? 29.628 15.462  -56.075  1.00 11.67 ? 101  ASP J N   1 
ATOM   9651  C  CA  . ASP I  1 101 ? 30.077 14.092  -55.933  1.00 11.72 ? 101  ASP J CA  1 
ATOM   9652  C  C   . ASP I  1 101 ? 31.542 13.981  -56.332  1.00 12.14 ? 101  ASP J C   1 
ATOM   9653  O  O   . ASP I  1 101 ? 31.980 14.598  -57.314  1.00 12.11 ? 101  ASP J O   1 
ATOM   9654  C  CB  . ASP I  1 101 ? 29.211 13.158  -56.784  1.00 11.56 ? 101  ASP J CB  1 
ATOM   9655  C  CG  . ASP I  1 101 ? 29.389 11.695  -56.412  1.00 11.36 ? 101  ASP J CG  1 
ATOM   9656  O  OD1 . ASP I  1 101 ? 30.104 10.975  -57.151  1.00 9.92  ? 101  ASP J OD1 1 
ATOM   9657  O  OD2 . ASP I  1 101 ? 28.829 11.264  -55.375  1.00 12.17 ? 101  ASP J OD2 1 
ATOM   9658  N  N   . SER I  1 102 ? 32.289 13.195  -55.567  1.00 12.02 ? 102  SER J N   1 
ATOM   9659  C  CA  . SER I  1 102 ? 33.728 13.052  -55.793  1.00 12.36 ? 102  SER J CA  1 
ATOM   9660  C  C   . SER I  1 102 ? 34.155 11.730  -56.420  1.00 12.35 ? 102  SER J C   1 
ATOM   9661  O  O   . SER I  1 102 ? 35.353 11.514  -56.670  1.00 12.82 ? 102  SER J O   1 
ATOM   9662  C  CB  . SER I  1 102 ? 34.477 13.318  -54.486  1.00 12.58 ? 102  SER J CB  1 
ATOM   9663  O  OG  . SER I  1 102 ? 34.495 14.710  -54.277  1.00 13.45 ? 102  SER J OG  1 
ATOM   9664  N  N   . VAL I  1 103 ? 33.171 10.885  -56.729  1.00 11.57 ? 103  VAL J N   1 
ATOM   9665  C  CA  . VAL I  1 103 ? 33.403 9.543   -57.270  1.00 10.92 ? 103  VAL J CA  1 
ATOM   9666  C  C   . VAL I  1 103 ? 33.185 9.527   -58.783  1.00 10.92 ? 103  VAL J C   1 
ATOM   9667  O  O   . VAL I  1 103 ? 34.008 8.968   -59.522  1.00 10.28 ? 103  VAL J O   1 
ATOM   9668  C  CB  . VAL I  1 103 ? 32.540 8.452   -56.549  1.00 10.08 ? 103  VAL J CB  1 
ATOM   9669  C  CG1 . VAL I  1 103 ? 32.730 7.059   -57.193  1.00 10.02 ? 103  VAL J CG1 1 
ATOM   9670  C  CG2 . VAL I  1 103 ? 32.907 8.372   -55.062  1.00 11.32 ? 103  VAL J CG2 1 
ATOM   9671  N  N   . ILE I  1 104 ? 32.092 10.134  -59.255  1.00 9.59  ? 104  ILE J N   1 
ATOM   9672  C  CA  . ILE I  1 104 ? 31.989 10.389  -60.693  1.00 10.24 ? 104  ILE J CA  1 
ATOM   9673  C  C   . ILE I  1 104 ? 33.086 11.367  -61.072  1.00 10.17 ? 104  ILE J C   1 
ATOM   9674  O  O   . ILE I  1 104 ? 33.615 12.095  -60.218  1.00 10.69 ? 104  ILE J O   1 
ATOM   9675  C  CB  . ILE I  1 104 ? 30.597 10.955  -61.143  1.00 9.42  ? 104  ILE J CB  1 
ATOM   9676  C  CG1 . ILE I  1 104 ? 30.258 12.260  -60.399  1.00 10.04 ? 104  ILE J CG1 1 
ATOM   9677  C  CG2 . ILE I  1 104 ? 29.518 9.869   -60.980  1.00 10.66 ? 104  ILE J CG2 1 
ATOM   9678  C  CD1 . ILE I  1 104 ? 29.027 13.081  -60.951  1.00 8.90  ? 104  ILE J CD1 1 
ATOM   9679  N  N   . SER I  1 105 ? 33.413 11.389  -62.357  1.00 10.15 ? 105  SER J N   1 
ATOM   9680  C  CA  . SER I  1 105 ? 34.384 12.326  -62.890  1.00 10.45 ? 105  SER J CA  1 
ATOM   9681  C  C   . SER I  1 105 ? 34.007 12.643  -64.338  1.00 11.07 ? 105  SER J C   1 
ATOM   9682  O  O   . SER I  1 105 ? 33.247 11.895  -64.957  1.00 10.08 ? 105  SER J O   1 
ATOM   9683  C  CB  . SER I  1 105 ? 35.784 11.701  -62.849  1.00 11.03 ? 105  SER J CB  1 
ATOM   9684  O  OG  . SER I  1 105 ? 36.758 12.663  -63.259  1.00 10.99 ? 105  SER J OG  1 
ATOM   9685  N  N   . LEU I  1 106 ? 34.521 13.758  -64.863  1.00 11.73 ? 106  LEU J N   1 
ATOM   9686  C  CA  . LEU I  1 106 ? 34.369 14.086  -66.291  1.00 12.63 ? 106  LEU J CA  1 
ATOM   9687  C  C   . LEU I  1 106 ? 35.624 13.725  -67.113  1.00 13.45 ? 106  LEU J C   1 
ATOM   9688  O  O   . LEU I  1 106 ? 35.736 14.061  -68.305  1.00 13.26 ? 106  LEU J O   1 
ATOM   9689  C  CB  . LEU I  1 106 ? 33.976 15.555  -66.465  1.00 12.90 ? 106  LEU J CB  1 
ATOM   9690  C  CG  . LEU I  1 106 ? 32.695 15.989  -65.742  1.00 12.86 ? 106  LEU J CG  1 
ATOM   9691  C  CD1 . LEU I  1 106 ? 32.349 17.463  -65.987  1.00 12.30 ? 106  LEU J CD1 1 
ATOM   9692  C  CD2 . LEU I  1 106 ? 31.526 15.089  -66.158  1.00 11.89 ? 106  LEU J CD2 1 
ATOM   9693  N  N   . SER I  1 107 ? 36.556 13.017  -66.482  1.00 14.29 ? 107  SER J N   1 
ATOM   9694  C  CA  . SER I  1 107 ? 37.686 12.430  -67.200  1.00 15.77 ? 107  SER J CA  1 
ATOM   9695  C  C   . SER I  1 107 ? 38.176 11.197  -66.456  1.00 16.29 ? 107  SER J C   1 
ATOM   9696  O  O   . SER I  1 107 ? 37.827 11.007  -65.288  1.00 15.99 ? 107  SER J O   1 
ATOM   9697  C  CB  . SER I  1 107 ? 38.810 13.458  -67.397  1.00 16.15 ? 107  SER J CB  1 
ATOM   9698  O  OG  . SER I  1 107 ? 39.523 13.675  -66.207  1.00 17.26 ? 107  SER J OG  1 
ATOM   9699  N  N   . GLY I  1 108 ? 38.968 10.357  -67.129  1.00 16.11 ? 108  GLY J N   1 
ATOM   9700  C  CA  . GLY I  1 108 ? 39.579 9.191   -66.478  1.00 16.30 ? 108  GLY J CA  1 
ATOM   9701  C  C   . GLY I  1 108 ? 38.692 7.954   -66.442  1.00 15.74 ? 108  GLY J C   1 
ATOM   9702  O  O   . GLY I  1 108 ? 37.673 7.892   -67.131  1.00 15.95 ? 108  GLY J O   1 
ATOM   9703  N  N   . ASP I  1 109 ? 39.076 6.963   -65.640  1.00 15.58 ? 109  ASP J N   1 
ATOM   9704  C  CA  . ASP I  1 109 ? 38.353 5.679   -65.595  1.00 15.92 ? 109  ASP J CA  1 
ATOM   9705  C  C   . ASP I  1 109 ? 36.955 5.794   -65.017  1.00 15.28 ? 109  ASP J C   1 
ATOM   9706  O  O   . ASP I  1 109 ? 36.142 4.893   -65.206  1.00 15.58 ? 109  ASP J O   1 
ATOM   9707  C  CB  . ASP I  1 109 ? 39.094 4.665   -64.743  1.00 16.63 ? 109  ASP J CB  1 
ATOM   9708  C  CG  . ASP I  1 109 ? 40.343 4.179   -65.385  1.00 18.68 ? 109  ASP J CG  1 
ATOM   9709  O  OD1 . ASP I  1 109 ? 40.532 4.443   -66.592  1.00 21.47 ? 109  ASP J OD1 1 
ATOM   9710  O  OD2 . ASP I  1 109 ? 41.152 3.555   -64.664  1.00 20.81 ? 109  ASP J OD2 1 
ATOM   9711  N  N   . HIS I  1 110 ? 36.705 6.877   -64.283  1.00 14.46 ? 110  HIS J N   1 
ATOM   9712  C  CA  . HIS I  1 110 ? 35.399 7.101   -63.673  1.00 14.31 ? 110  HIS J CA  1 
ATOM   9713  C  C   . HIS I  1 110 ? 34.570 8.060   -64.524  1.00 13.58 ? 110  HIS J C   1 
ATOM   9714  O  O   . HIS I  1 110 ? 33.493 8.466   -64.088  1.00 12.91 ? 110  HIS J O   1 
ATOM   9715  C  CB  . HIS I  1 110 ? 35.538 7.638   -62.229  1.00 14.64 ? 110  HIS J CB  1 
ATOM   9716  C  CG  . HIS I  1 110 ? 36.047 6.625   -61.249  1.00 17.20 ? 110  HIS J CG  1 
ATOM   9717  N  ND1 . HIS I  1 110 ? 35.782 6.701   -59.894  1.00 20.89 ? 110  HIS J ND1 1 
ATOM   9718  C  CD2 . HIS I  1 110 ? 36.772 5.494   -61.427  1.00 20.72 ? 110  HIS J CD2 1 
ATOM   9719  C  CE1 . HIS I  1 110 ? 36.345 5.673   -59.279  1.00 19.70 ? 110  HIS J CE1 1 
ATOM   9720  N  NE2 . HIS I  1 110 ? 36.953 4.927   -60.184  1.00 20.47 ? 110  HIS J NE2 1 
HETATM 9721  N  N   . CME I  1 111 ? 35.056 8.389   -65.732  1.00 12.85 ? 111  CME J N   1 
HETATM 9722  C  CA  . CME I  1 111 ? 34.408 9.378   -66.615  1.00 12.72 ? 111  CME J CA  1 
HETATM 9723  C  CB  . CME I  1 111 ? 35.171 9.597   -67.925  1.00 13.37 ? 111  CME J CB  1 
HETATM 9724  S  SG  . CME I  1 111 ? 34.519 11.018  -68.763  1.00 15.40 ? 111  CME J SG  1 
HETATM 9725  S  SD  . CME I  1 111 ? 35.658 11.048  -70.464  1.00 22.64 ? 111  CME J SD  1 
HETATM 9726  C  CE  . CME I  1 111 ? 34.703 10.137  -71.629  1.00 22.85 ? 111  CME J CE  1 
HETATM 9727  C  CZ  . CME I  1 111 ? 35.060 8.659   -71.549  1.00 25.41 ? 111  CME J CZ  1 
HETATM 9728  O  OH  . CME I  1 111 ? 34.078 8.011   -70.728  1.00 29.66 ? 111  CME J OH  1 
HETATM 9729  C  C   . CME I  1 111 ? 33.008 8.939   -66.964  1.00 11.45 ? 111  CME J C   1 
HETATM 9730  O  O   . CME I  1 111 ? 32.792 7.791   -67.335  1.00 11.90 ? 111  CME J O   1 
ATOM   9731  N  N   . ILE I  1 112 ? 32.051 9.845   -66.817  1.00 10.90 ? 112  ILE J N   1 
ATOM   9732  C  CA  . ILE I  1 112 ? 30.645 9.548   -67.111  1.00 10.31 ? 112  ILE J CA  1 
ATOM   9733  C  C   . ILE I  1 112 ? 30.181 10.149  -68.458  1.00 11.32 ? 112  ILE J C   1 
ATOM   9734  O  O   . ILE I  1 112 ? 29.035 9.925   -68.877  1.00 10.93 ? 112  ILE J O   1 
ATOM   9735  C  CB  . ILE I  1 112 ? 29.716 10.051  -65.964  1.00 10.08 ? 112  ILE J CB  1 
ATOM   9736  C  CG1 . ILE I  1 112 ? 29.783 11.585  -65.870  1.00 8.45  ? 112  ILE J CG1 1 
ATOM   9737  C  CG2 . ILE I  1 112 ? 30.063 9.330   -64.616  1.00 9.67  ? 112  ILE J CG2 1 
ATOM   9738  C  CD1 . ILE I  1 112 ? 28.867 12.211  -64.793  1.00 10.16 ? 112  ILE J CD1 1 
ATOM   9739  N  N   . ILE I  1 113 ? 31.051 10.925  -69.112  1.00 11.88 ? 113  ILE J N   1 
ATOM   9740  C  CA  . ILE I  1 113 ? 30.752 11.456  -70.455  1.00 12.45 ? 113  ILE J CA  1 
ATOM   9741  C  C   . ILE I  1 113 ? 30.606 10.282  -71.421  1.00 12.65 ? 113  ILE J C   1 
ATOM   9742  O  O   . ILE I  1 113 ? 31.452 9.379   -71.435  1.00 12.85 ? 113  ILE J O   1 
ATOM   9743  C  CB  . ILE I  1 113 ? 31.840 12.444  -70.917  1.00 13.15 ? 113  ILE J CB  1 
ATOM   9744  C  CG1 . ILE I  1 113 ? 31.744 13.718  -70.092  1.00 12.51 ? 113  ILE J CG1 1 
ATOM   9745  C  CG2 . ILE I  1 113 ? 31.730 12.743  -72.435  1.00 13.04 ? 113  ILE J CG2 1 
ATOM   9746  C  CD1 . ILE I  1 113 ? 32.840 14.746  -70.364  1.00 13.53 ? 113  ILE J CD1 1 
ATOM   9747  N  N   . GLY I  1 114 ? 29.510 10.274  -72.184  1.00 12.17 ? 114  GLY J N   1 
ATOM   9748  C  CA  . GLY I  1 114 ? 29.204 9.178   -73.119  1.00 12.09 ? 114  GLY J CA  1 
ATOM   9749  C  C   . GLY I  1 114 ? 28.387 8.072   -72.492  1.00 11.97 ? 114  GLY J C   1 
ATOM   9750  O  O   . GLY I  1 114 ? 28.089 7.053   -73.141  1.00 12.35 ? 114  GLY J O   1 
ATOM   9751  N  N   . ARG I  1 115 ? 28.032 8.254   -71.219  1.00 11.16 ? 115  ARG J N   1 
ATOM   9752  C  CA  . ARG I  1 115 ? 27.159 7.310   -70.534  1.00 10.81 ? 115  ARG J CA  1 
ATOM   9753  C  C   . ARG I  1 115 ? 25.767 7.935   -70.355  1.00 10.97 ? 115  ARG J C   1 
ATOM   9754  O  O   . ARG I  1 115 ? 25.536 9.071   -70.782  1.00 10.96 ? 115  ARG J O   1 
ATOM   9755  C  CB  . ARG I  1 115 ? 27.810 6.854   -69.222  1.00 10.40 ? 115  ARG J CB  1 
ATOM   9756  C  CG  . ARG I  1 115 ? 29.226 6.250   -69.497  1.00 10.32 ? 115  ARG J CG  1 
ATOM   9757  C  CD  . ARG I  1 115 ? 29.861 5.569   -68.300  1.00 11.22 ? 115  ARG J CD  1 
ATOM   9758  N  NE  . ARG I  1 115 ? 31.262 5.243   -68.582  1.00 10.89 ? 115  ARG J NE  1 
ATOM   9759  C  CZ  . ARG I  1 115 ? 31.682 4.117   -69.166  1.00 11.25 ? 115  ARG J CZ  1 
ATOM   9760  N  NH1 . ARG I  1 115 ? 32.984 3.915   -69.352  1.00 9.51  ? 115  ARG J NH1 1 
ATOM   9761  N  NH2 . ARG I  1 115 ? 30.823 3.173   -69.535  1.00 9.52  ? 115  ARG J NH2 1 
ATOM   9762  N  N   . THR I  1 116 ? 24.835 7.190   -69.773  1.00 10.60 ? 116  THR J N   1 
ATOM   9763  C  CA  . THR I  1 116 ? 23.444 7.645   -69.703  1.00 10.99 ? 116  THR J CA  1 
ATOM   9764  C  C   . THR I  1 116 ? 23.079 8.035   -68.275  1.00 10.58 ? 116  THR J C   1 
ATOM   9765  O  O   . THR I  1 116 ? 23.286 7.255   -67.349  1.00 10.62 ? 116  THR J O   1 
ATOM   9766  C  CB  . THR I  1 116 ? 22.468 6.568   -70.205  1.00 10.85 ? 116  THR J CB  1 
ATOM   9767  O  OG1 . THR I  1 116 ? 22.718 6.283   -71.603  1.00 12.76 ? 116  THR J OG1 1 
ATOM   9768  C  CG2 . THR I  1 116 ? 21.024 7.034   -70.053  1.00 10.97 ? 116  THR J CG2 1 
ATOM   9769  N  N   . LEU I  1 117 ? 22.542 9.245   -68.121  1.00 10.12 ? 117  LEU J N   1 
ATOM   9770  C  CA  . LEU I  1 117 ? 21.946 9.684   -66.855  1.00 10.02 ? 117  LEU J CA  1 
ATOM   9771  C  C   . LEU I  1 117 ? 20.476 9.316   -66.847  1.00 10.26 ? 117  LEU J C   1 
ATOM   9772  O  O   . LEU I  1 117 ? 19.754 9.613   -67.829  1.00 10.49 ? 117  LEU J O   1 
ATOM   9773  C  CB  . LEU I  1 117 ? 22.104 11.197  -66.664  1.00 9.62  ? 117  LEU J CB  1 
ATOM   9774  C  CG  . LEU I  1 117 ? 21.582 11.801  -65.349  1.00 8.81  ? 117  LEU J CG  1 
ATOM   9775  C  CD1 . LEU I  1 117 ? 22.451 11.407  -64.132  1.00 9.43  ? 117  LEU J CD1 1 
ATOM   9776  C  CD2 . LEU I  1 117 ? 21.562 13.308  -65.505  1.00 12.17 ? 117  LEU J CD2 1 
ATOM   9777  N  N   . VAL I  1 118 ? 20.037 8.677   -65.761  1.00 8.90  ? 118  VAL J N   1 
ATOM   9778  C  CA  . VAL I  1 118 ? 18.659 8.155   -65.642  1.00 8.81  ? 118  VAL J CA  1 
ATOM   9779  C  C   . VAL I  1 118 ? 17.955 8.711   -64.394  1.00 9.66  ? 118  VAL J C   1 
ATOM   9780  O  O   . VAL I  1 118 ? 18.542 8.745   -63.304  1.00 8.32  ? 118  VAL J O   1 
ATOM   9781  C  CB  . VAL I  1 118 ? 18.620 6.586   -65.599  1.00 8.48  ? 118  VAL J CB  1 
ATOM   9782  C  CG1 . VAL I  1 118 ? 17.170 6.066   -65.497  1.00 9.93  ? 118  VAL J CG1 1 
ATOM   9783  C  CG2 . VAL I  1 118 ? 19.319 5.961   -66.846  1.00 9.11  ? 118  VAL J CG2 1 
ATOM   9784  N  N   . VAL I  1 119 ? 16.701 9.149   -64.564  1.00 9.80  ? 119  VAL J N   1 
ATOM   9785  C  CA  . VAL I  1 119 ? 15.860 9.435   -63.425  1.00 9.43  ? 119  VAL J CA  1 
ATOM   9786  C  C   . VAL I  1 119 ? 14.733 8.418   -63.400  1.00 10.15 ? 119  VAL J C   1 
ATOM   9787  O  O   . VAL I  1 119 ? 14.133 8.070   -64.446  1.00 10.40 ? 119  VAL J O   1 
ATOM   9788  C  CB  . VAL I  1 119 ? 15.399 10.943  -63.342  1.00 9.23  ? 119  VAL J CB  1 
ATOM   9789  C  CG1 . VAL I  1 119 ? 14.520 11.335  -64.525  1.00 7.33  ? 119  VAL J CG1 1 
ATOM   9790  C  CG2 . VAL I  1 119 ? 14.693 11.227  -62.005  1.00 9.43  ? 119  VAL J CG2 1 
ATOM   9791  N  N   . HIS I  1 120 ? 14.477 7.929   -62.193  1.00 10.18 ? 120  HIS J N   1 
ATOM   9792  C  CA  . HIS I  1 120 ? 13.625 6.783   -61.962  1.00 11.10 ? 120  HIS J CA  1 
ATOM   9793  C  C   . HIS I  1 120 ? 12.256 7.103   -61.396  1.00 12.21 ? 120  HIS J C   1 
ATOM   9794  O  O   . HIS I  1 120 ? 12.026 8.172   -60.819  1.00 10.98 ? 120  HIS J O   1 
ATOM   9795  C  CB  . HIS I  1 120 ? 14.326 5.822   -61.020  1.00 10.28 ? 120  HIS J CB  1 
ATOM   9796  C  CG  . HIS I  1 120 ? 15.438 5.063   -61.671  1.00 11.03 ? 120  HIS J CG  1 
ATOM   9797  N  ND1 . HIS I  1 120 ? 15.241 3.850   -62.291  1.00 8.52  ? 120  HIS J ND1 1 
ATOM   9798  C  CD2 . HIS I  1 120 ? 16.756 5.341   -61.791  1.00 9.35  ? 120  HIS J CD2 1 
ATOM   9799  C  CE1 . HIS I  1 120 ? 16.390 3.421   -62.785  1.00 10.43 ? 120  HIS J CE1 1 
ATOM   9800  N  NE2 . HIS I  1 120 ? 17.321 4.312   -62.501  1.00 9.40  ? 120  HIS J NE2 1 
ATOM   9801  N  N   . GLU I  1 121 ? 11.380 6.115   -61.580  1.00 13.25 ? 121  GLU J N   1 
ATOM   9802  C  CA  . GLU I  1 121 ? 10.015 6.040   -61.056  1.00 14.80 ? 121  GLU J CA  1 
ATOM   9803  C  C   . GLU I  1 121 ? 9.938  6.177   -59.545  1.00 14.84 ? 121  GLU J C   1 
ATOM   9804  O  O   . GLU I  1 121 ? 9.133  6.965   -59.023  1.00 14.91 ? 121  GLU J O   1 
ATOM   9805  C  CB  . GLU I  1 121 ? 9.429  4.679   -61.466  1.00 14.92 ? 121  GLU J CB  1 
ATOM   9806  C  CG  . GLU I  1 121 ? 8.047  4.353   -60.902  1.00 18.11 ? 121  GLU J CG  1 
ATOM   9807  C  CD  . GLU I  1 121 ? 7.684  2.863   -60.991  1.00 22.21 ? 121  GLU J CD  1 
ATOM   9808  O  OE1 . GLU I  1 121 ? 6.507  2.539   -60.714  1.00 23.99 ? 121  GLU J OE1 1 
ATOM   9809  O  OE2 . GLU I  1 121 ? 8.552  2.021   -61.328  1.00 22.43 ? 121  GLU J OE2 1 
ATOM   9810  N  N   . LYS I  1 122 ? 10.777 5.397   -58.856  1.00 15.15 ? 122  LYS J N   1 
ATOM   9811  C  CA  . LYS I  1 122 ? 10.735 5.248   -57.400  1.00 15.20 ? 122  LYS J CA  1 
ATOM   9812  C  C   . LYS I  1 122 ? 11.992 5.801   -56.734  1.00 14.17 ? 122  LYS J C   1 
ATOM   9813  O  O   . LYS I  1 122 ? 13.001 6.043   -57.398  1.00 13.91 ? 122  LYS J O   1 
ATOM   9814  C  CB  . LYS I  1 122 ? 10.650 3.773   -57.018  1.00 15.59 ? 122  LYS J CB  1 
ATOM   9815  C  CG  . LYS I  1 122 ? 9.279  3.150   -57.068  1.00 19.45 ? 122  LYS J CG  1 
ATOM   9816  C  CD  . LYS I  1 122 ? 9.424  1.664   -57.221  1.00 22.98 ? 122  LYS J CD  1 
ATOM   9817  C  CE  . LYS I  1 122 ? 8.096  0.971   -57.072  1.00 25.48 ? 122  LYS J CE  1 
ATOM   9818  N  NZ  . LYS I  1 122 ? 8.346  -0.493  -57.013  1.00 27.03 ? 122  LYS J NZ  1 
ATOM   9819  N  N   . ALA I  1 123 ? 11.908 5.947   -55.413  1.00 13.02 ? 123  ALA J N   1 
ATOM   9820  C  CA  . ALA I  1 123 ? 13.047 6.247   -54.537  1.00 11.63 ? 123  ALA J CA  1 
ATOM   9821  C  C   . ALA I  1 123 ? 14.116 5.167   -54.630  1.00 10.91 ? 123  ALA J C   1 
ATOM   9822  O  O   . ALA I  1 123 ? 13.800 3.979   -54.713  1.00 9.81  ? 123  ALA J O   1 
ATOM   9823  C  CB  . ALA I  1 123 ? 12.562 6.336   -53.094  1.00 12.13 ? 123  ALA J CB  1 
ATOM   9824  N  N   . ASP I  1 124 ? 15.377 5.597   -54.642  1.00 9.73  ? 124  ASP J N   1 
ATOM   9825  C  CA  . ASP I  1 124 ? 16.521 4.699   -54.448  1.00 9.77  ? 124  ASP J CA  1 
ATOM   9826  C  C   . ASP I  1 124 ? 16.667 4.442   -52.949  1.00 9.54  ? 124  ASP J C   1 
ATOM   9827  O  O   . ASP I  1 124 ? 16.768 5.400   -52.162  1.00 9.50  ? 124  ASP J O   1 
ATOM   9828  C  CB  . ASP I  1 124 ? 17.760 5.399   -55.024  1.00 9.60  ? 124  ASP J CB  1 
ATOM   9829  C  CG  . ASP I  1 124 ? 19.013 4.538   -55.017  1.00 8.89  ? 124  ASP J CG  1 
ATOM   9830  O  OD1 . ASP I  1 124 ? 19.139 3.614   -54.192  1.00 10.39 ? 124  ASP J OD1 1 
ATOM   9831  O  OD2 . ASP I  1 124 ? 19.889 4.830   -55.847  1.00 8.86  ? 124  ASP J OD2 1 
ATOM   9832  N  N   . ASP I  1 125 ? 16.642 3.165   -52.535  1.00 8.96  ? 125  ASP J N   1 
ATOM   9833  C  CA  . ASP I  1 125 ? 16.826 2.812   -51.126  1.00 8.74  ? 125  ASP J CA  1 
ATOM   9834  C  C   . ASP I  1 125 ? 18.291 2.806   -50.698  1.00 7.88  ? 125  ASP J C   1 
ATOM   9835  O  O   . ASP I  1 125 ? 18.612 2.387   -49.580  1.00 7.93  ? 125  ASP J O   1 
ATOM   9836  C  CB  . ASP I  1 125 ? 16.150 1.465   -50.761  1.00 8.41  ? 125  ASP J CB  1 
ATOM   9837  C  CG  . ASP I  1 125 ? 16.797 0.249   -51.439  1.00 10.56 ? 125  ASP J CG  1 
ATOM   9838  O  OD1 . ASP I  1 125 ? 16.134 -0.816  -51.510  1.00 8.29  ? 125  ASP J OD1 1 
ATOM   9839  O  OD2 . ASP I  1 125 ? 17.961 0.334   -51.869  1.00 10.79 ? 125  ASP J OD2 1 
ATOM   9840  N  N   . LEU I  1 126 ? 19.171 3.255   -51.592  1.00 7.87  ? 126  LEU J N   1 
ATOM   9841  C  CA  . LEU I  1 126 ? 20.594 3.452   -51.256  1.00 8.20  ? 126  LEU J CA  1 
ATOM   9842  C  C   . LEU I  1 126 ? 21.288 2.157   -50.807  1.00 8.12  ? 126  LEU J C   1 
ATOM   9843  O  O   . LEU I  1 126 ? 22.261 2.186   -50.050  1.00 8.53  ? 126  LEU J O   1 
ATOM   9844  C  CB  . LEU I  1 126 ? 20.744 4.572   -50.215  1.00 7.87  ? 126  LEU J CB  1 
ATOM   9845  C  CG  . LEU I  1 126 ? 19.935 5.860   -50.498  1.00 8.46  ? 126  LEU J CG  1 
ATOM   9846  C  CD1 . LEU I  1 126 ? 20.177 6.910   -49.388  1.00 9.31  ? 126  LEU J CD1 1 
ATOM   9847  C  CD2 . LEU I  1 126 ? 20.172 6.460   -51.891  1.00 7.71  ? 126  LEU J CD2 1 
ATOM   9848  N  N   . GLY I  1 127 ? 20.775 1.034   -51.299  1.00 8.50  ? 127  GLY J N   1 
ATOM   9849  C  CA  . GLY I  1 127 ? 21.344 -0.300  -51.034  1.00 7.65  ? 127  GLY J CA  1 
ATOM   9850  C  C   . GLY I  1 127 ? 20.955 -0.855  -49.681  1.00 8.12  ? 127  GLY J C   1 
ATOM   9851  O  O   . GLY I  1 127 ? 21.555 -1.817  -49.220  1.00 7.98  ? 127  GLY J O   1 
ATOM   9852  N  N   . LYS I  1 128 ? 19.976 -0.225  -49.016  1.00 7.27  ? 128  LYS J N   1 
ATOM   9853  C  CA  . LYS I  1 128 ? 19.603 -0.635  -47.654  1.00 7.93  ? 128  LYS J CA  1 
ATOM   9854  C  C   . LYS I  1 128 ? 18.304 -1.435  -47.593  1.00 7.86  ? 128  LYS J C   1 
ATOM   9855  O  O   . LYS I  1 128 ? 17.742 -1.633  -46.509  1.00 8.60  ? 128  LYS J O   1 
ATOM   9856  C  CB  . LYS I  1 128 ? 19.486 0.578   -46.728  1.00 8.15  ? 128  LYS J CB  1 
ATOM   9857  C  CG  . LYS I  1 128 ? 20.711 1.495   -46.725  1.00 11.57 ? 128  LYS J CG  1 
ATOM   9858  C  CD  . LYS I  1 128 ? 20.399 2.806   -46.022  1.00 15.39 ? 128  LYS J CD  1 
ATOM   9859  C  CE  . LYS I  1 128 ? 20.838 2.796   -44.587  1.00 20.25 ? 128  LYS J CE  1 
ATOM   9860  N  NZ  . LYS I  1 128 ? 20.619 4.146   -43.968  1.00 20.39 ? 128  LYS J NZ  1 
ATOM   9861  N  N   . GLY I  1 129 ? 17.831 -1.899  -48.747  1.00 7.01  ? 129  GLY J N   1 
ATOM   9862  C  CA  . GLY I  1 129 ? 16.538 -2.577  -48.816  1.00 7.74  ? 129  GLY J CA  1 
ATOM   9863  C  C   . GLY I  1 129 ? 16.518 -4.055  -48.421  1.00 7.88  ? 129  GLY J C   1 
ATOM   9864  O  O   . GLY I  1 129 ? 15.453 -4.596  -48.164  1.00 8.23  ? 129  GLY J O   1 
ATOM   9865  N  N   . GLY I  1 130 ? 17.675 -4.711  -48.359  1.00 8.10  ? 130  GLY J N   1 
ATOM   9866  C  CA  . GLY I  1 130 ? 17.748 -6.099  -47.846  1.00 8.13  ? 130  GLY J CA  1 
ATOM   9867  C  C   . GLY I  1 130 ? 17.252 -7.187  -48.807  1.00 8.43  ? 130  GLY J C   1 
ATOM   9868  O  O   . GLY I  1 130 ? 17.298 -8.377  -48.499  1.00 8.13  ? 130  GLY J O   1 
ATOM   9869  N  N   . ASN I  1 131 ? 16.772 -6.786  -49.975  1.00 9.61  ? 131  ASN J N   1 
ATOM   9870  C  CA  . ASN I  1 131 ? 16.481 -7.736  -51.047  1.00 10.58 ? 131  ASN J CA  1 
ATOM   9871  C  C   . ASN I  1 131 ? 17.562 -7.732  -52.122  1.00 11.30 ? 131  ASN J C   1 
ATOM   9872  O  O   . ASN I  1 131 ? 18.477 -6.915  -52.085  1.00 12.18 ? 131  ASN J O   1 
ATOM   9873  C  CB  . ASN I  1 131 ? 15.070 -7.551  -51.640  1.00 10.19 ? 131  ASN J CB  1 
ATOM   9874  C  CG  . ASN I  1 131 ? 14.917 -6.266  -52.458  1.00 11.20 ? 131  ASN J CG  1 
ATOM   9875  O  OD1 . ASN I  1 131 ? 15.777 -5.388  -52.443  1.00 12.57 ? 131  ASN J OD1 1 
ATOM   9876  N  ND2 . ASN I  1 131 ? 13.803 -6.164  -53.182  1.00 13.38 ? 131  ASN J ND2 1 
ATOM   9877  N  N   . GLU I  1 132 ? 17.473 -8.670  -53.064  1.00 11.96 ? 132  GLU J N   1 
ATOM   9878  C  CA  . GLU I  1 132 ? 18.485 -8.820  -54.098  1.00 12.15 ? 132  GLU J CA  1 
ATOM   9879  C  C   . GLU I  1 132 ? 18.604 -7.545  -54.919  1.00 11.71 ? 132  GLU J C   1 
ATOM   9880  O  O   . GLU I  1 132 ? 19.698 -7.101  -55.267  1.00 11.26 ? 132  GLU J O   1 
ATOM   9881  C  CB  . GLU I  1 132 ? 18.157 -10.012 -55.023  1.00 12.91 ? 132  GLU J CB  1 
ATOM   9882  C  CG  . GLU I  1 132 ? 19.128 -10.071 -56.209  1.00 16.30 ? 132  GLU J CG  1 
ATOM   9883  C  CD  . GLU I  1 132 ? 18.810 -11.140 -57.254  1.00 19.37 ? 132  GLU J CD  1 
ATOM   9884  O  OE1 . GLU I  1 132 ? 17.653 -11.635 -57.330  1.00 21.84 ? 132  GLU J OE1 1 
ATOM   9885  O  OE2 . GLU I  1 132 ? 19.745 -11.479 -58.008  1.00 21.64 ? 132  GLU J OE2 1 
ATOM   9886  N  N   . GLU I  1 133 ? 17.463 -6.958  -55.241  1.00 11.45 ? 133  GLU J N   1 
ATOM   9887  C  CA  . GLU I  1 133 ? 17.454 -5.767  -56.085  1.00 12.32 ? 133  GLU J CA  1 
ATOM   9888  C  C   . GLU I  1 133 ? 18.111 -4.521  -55.461  1.00 10.85 ? 133  GLU J C   1 
ATOM   9889  O  O   . GLU I  1 133 ? 18.682 -3.687  -56.176  1.00 9.84  ? 133  GLU J O   1 
ATOM   9890  C  CB  . GLU I  1 133 ? 16.032 -5.478  -56.565  1.00 13.15 ? 133  GLU J CB  1 
ATOM   9891  C  CG  . GLU I  1 133 ? 15.974 -4.677  -57.849  1.00 17.95 ? 133  GLU J CG  1 
ATOM   9892  C  CD  . GLU I  1 133 ? 16.477 -5.420  -59.102  1.00 21.00 ? 133  GLU J CD  1 
ATOM   9893  O  OE1 . GLU I  1 133 ? 16.150 -4.967  -60.209  1.00 24.71 ? 133  GLU J OE1 1 
ATOM   9894  O  OE2 . GLU I  1 133 ? 17.212 -6.422  -59.008  1.00 24.91 ? 133  GLU J OE2 1 
ATOM   9895  N  N   . SER I  1 134 ? 18.032 -4.400  -54.139  1.00 11.02 ? 134  SER J N   1 
ATOM   9896  C  CA  . SER I  1 134 ? 18.574 -3.224  -53.453  1.00 11.20 ? 134  SER J CA  1 
ATOM   9897  C  C   . SER I  1 134 ? 20.077 -3.091  -53.709  1.00 11.83 ? 134  SER J C   1 
ATOM   9898  O  O   . SER I  1 134 ? 20.591 -1.984  -53.904  1.00 11.23 ? 134  SER J O   1 
ATOM   9899  C  CB  . SER I  1 134 ? 18.266 -3.244  -51.965  1.00 10.93 ? 134  SER J CB  1 
ATOM   9900  O  OG  . SER I  1 134 ? 18.942 -2.172  -51.330  1.00 11.10 ? 134  SER J OG  1 
ATOM   9901  N  N   . THR I  1 135 ? 20.743 -4.244  -53.792  1.00 12.55 ? 135  THR J N   1 
ATOM   9902  C  CA  . THR I  1 135 ? 22.173 -4.363  -54.081  1.00 13.56 ? 135  THR J CA  1 
ATOM   9903  C  C   . THR I  1 135 ? 22.525 -4.050  -55.544  1.00 13.65 ? 135  THR J C   1 
ATOM   9904  O  O   . THR I  1 135 ? 23.700 -3.979  -55.895  1.00 14.19 ? 135  THR J O   1 
ATOM   9905  C  CB  . THR I  1 135 ? 22.702 -5.824  -53.737  1.00 13.93 ? 135  THR J CB  1 
ATOM   9906  O  OG1 . THR I  1 135 ? 22.279 -6.756  -54.746  1.00 16.93 ? 135  THR J OG1 1 
ATOM   9907  C  CG2 . THR I  1 135 ? 22.186 -6.326  -52.417  1.00 14.36 ? 135  THR J CG2 1 
ATOM   9908  N  N   . LYS I  1 136 ? 21.515 -3.880  -56.394  1.00 12.88 ? 136  LYS J N   1 
ATOM   9909  C  CA  . LYS I  1 136 ? 21.738 -3.684  -57.826  1.00 12.64 ? 136  LYS J CA  1 
ATOM   9910  C  C   . LYS I  1 136 ? 21.238 -2.314  -58.321  1.00 11.71 ? 136  LYS J C   1 
ATOM   9911  O  O   . LYS I  1 136 ? 21.977 -1.554  -58.958  1.00 11.71 ? 136  LYS J O   1 
ATOM   9912  C  CB  . LYS I  1 136 ? 21.071 -4.820  -58.624  1.00 12.97 ? 136  LYS J CB  1 
ATOM   9913  C  CG  . LYS I  1 136 ? 21.696 -6.223  -58.390  1.00 14.13 ? 136  LYS J CG  1 
ATOM   9914  C  CD  . LYS I  1 136 ? 20.998 -7.334  -59.220  1.00 16.24 ? 136  LYS J CD  1 
ATOM   9915  C  CE  . LYS I  1 136 ? 21.760 -8.678  -59.090  1.00 15.45 ? 136  LYS J CE  1 
ATOM   9916  N  NZ  . LYS I  1 136 ? 20.966 -9.802  -59.679  1.00 16.34 ? 136  LYS J NZ  1 
ATOM   9917  N  N   . THR I  1 137 ? 19.977 -2.019  -58.016  1.00 10.71 ? 137  THR J N   1 
ATOM   9918  C  CA  . THR I  1 137 ? 19.278 -0.827  -58.543  1.00 10.74 ? 137  THR J CA  1 
ATOM   9919  C  C   . THR I  1 137 ? 18.757 0.092   -57.441  1.00 9.84  ? 137  THR J C   1 
ATOM   9920  O  O   . THR I  1 137 ? 18.265 1.193   -57.728  1.00 9.90  ? 137  THR J O   1 
ATOM   9921  C  CB  . THR I  1 137 ? 18.037 -1.230  -59.338  1.00 9.92  ? 137  THR J CB  1 
ATOM   9922  O  OG1 . THR I  1 137 ? 17.136 -1.903  -58.457  1.00 10.27 ? 137  THR J OG1 1 
ATOM   9923  C  CG2 . THR I  1 137 ? 18.403 -2.163  -60.487  1.00 13.42 ? 137  THR J CG2 1 
ATOM   9924  N  N   . GLY I  1 138 ? 18.837 -0.375  -56.201  1.00 9.27  ? 138  GLY J N   1 
ATOM   9925  C  CA  . GLY I  1 138 ? 18.209 0.310   -55.057  1.00 9.15  ? 138  GLY J CA  1 
ATOM   9926  C  C   . GLY I  1 138 ? 16.688 0.280   -55.105  1.00 9.23  ? 138  GLY J C   1 
ATOM   9927  O  O   . GLY I  1 138 ? 16.038 1.072   -54.431  1.00 8.79  ? 138  GLY J O   1 
ATOM   9928  N  N   . ASN I  1 139 ? 16.112 -0.605  -55.926  1.00 8.90  ? 139  ASN J N   1 
ATOM   9929  C  CA  . ASN I  1 139 ? 14.655 -0.655  -56.092  1.00 9.09  ? 139  ASN J CA  1 
ATOM   9930  C  C   . ASN I  1 139 ? 14.069 0.658   -56.635  1.00 10.16 ? 139  ASN J C   1 
ATOM   9931  O  O   . ASN I  1 139 ? 12.944 1.055   -56.304  1.00 9.58  ? 139  ASN J O   1 
ATOM   9932  C  CB  . ASN I  1 139 ? 13.989 -1.055  -54.767  1.00 9.33  ? 139  ASN J CB  1 
ATOM   9933  C  CG  . ASN I  1 139 ? 14.313 -2.495  -54.369  1.00 10.59 ? 139  ASN J CG  1 
ATOM   9934  O  OD1 . ASN I  1 139 ? 13.896 -3.425  -55.046  1.00 12.77 ? 139  ASN J OD1 1 
ATOM   9935  N  ND2 . ASN I  1 139 ? 15.062 -2.680  -53.286  1.00 10.70 ? 139  ASN J ND2 1 
ATOM   9936  N  N   . ALA I  1 140 ? 14.833 1.310   -57.499  1.00 10.42 ? 140  ALA J N   1 
ATOM   9937  C  CA  . ALA I  1 140 ? 14.452 2.593   -58.054  1.00 11.52 ? 140  ALA J CA  1 
ATOM   9938  C  C   . ALA I  1 140 ? 13.366 2.449   -59.123  1.00 12.32 ? 140  ALA J C   1 
ATOM   9939  O  O   . ALA I  1 140 ? 12.776 3.432   -59.558  1.00 11.17 ? 140  ALA J O   1 
ATOM   9940  C  CB  . ALA I  1 140 ? 15.671 3.282   -58.620  1.00 11.52 ? 140  ALA J CB  1 
ATOM   9941  N  N   . GLY I  1 141 ? 13.111 1.220   -59.556  1.00 13.07 ? 141  GLY J N   1 
ATOM   9942  C  CA  . GLY I  1 141 ? 12.016 0.995   -60.503  1.00 14.17 ? 141  GLY J CA  1 
ATOM   9943  C  C   . GLY I  1 141 ? 12.323 1.464   -61.912  1.00 14.49 ? 141  GLY J C   1 
ATOM   9944  O  O   . GLY I  1 141 ? 13.487 1.663   -62.281  1.00 14.76 ? 141  GLY J O   1 
ATOM   9945  N  N   . SER I  1 142 ? 11.264 1.637   -62.697  1.00 14.31 ? 142  SER J N   1 
ATOM   9946  C  CA  . SER I  1 142 ? 11.364 1.982   -64.102  1.00 14.63 ? 142  SER J CA  1 
ATOM   9947  C  C   . SER I  1 142 ? 12.129 3.264   -64.374  1.00 14.27 ? 142  SER J C   1 
ATOM   9948  O  O   . SER I  1 142 ? 12.319 4.123   -63.486  1.00 14.67 ? 142  SER J O   1 
ATOM   9949  C  CB  . SER I  1 142 ? 9.955  2.086   -64.714  1.00 15.49 ? 142  SER J CB  1 
ATOM   9950  O  OG  . SER I  1 142 ? 9.372  3.334   -64.368  1.00 16.48 ? 142  SER J OG  1 
ATOM   9951  N  N   . ARG I  1 143 ? 12.560 3.394   -65.616  1.00 13.84 ? 143  ARG J N   1 
ATOM   9952  C  CA  . ARG I  1 143 ? 13.340 4.534   -66.058  1.00 13.74 ? 143  ARG J CA  1 
ATOM   9953  C  C   . ARG I  1 143 ? 12.431 5.536   -66.777  1.00 14.49 ? 143  ARG J C   1 
ATOM   9954  O  O   . ARG I  1 143 ? 12.013 5.302   -67.915  1.00 14.82 ? 143  ARG J O   1 
ATOM   9955  C  CB  . ARG I  1 143 ? 14.444 4.044   -66.996  1.00 13.85 ? 143  ARG J CB  1 
ATOM   9956  C  CG  . ARG I  1 143 ? 15.214 2.859   -66.432  1.00 12.39 ? 143  ARG J CG  1 
ATOM   9957  C  CD  . ARG I  1 143 ? 16.310 2.333   -67.374  1.00 11.75 ? 143  ARG J CD  1 
ATOM   9958  N  NE  . ARG I  1 143 ? 17.009 1.229   -66.707  1.00 12.64 ? 143  ARG J NE  1 
ATOM   9959  C  CZ  . ARG I  1 143 ? 18.141 0.642   -67.109  1.00 11.95 ? 143  ARG J CZ  1 
ATOM   9960  N  NH1 . ARG I  1 143 ? 18.649 -0.339  -66.379  1.00 13.00 ? 143  ARG J NH1 1 
ATOM   9961  N  NH2 . ARG I  1 143 ? 18.771 1.002   -68.221  1.00 12.01 ? 143  ARG J NH2 1 
ATOM   9962  N  N   . LEU I  1 144 ? 12.144 6.652   -66.111  1.00 14.20 ? 144  LEU J N   1 
ATOM   9963  C  CA  . LEU I  1 144 ? 11.188 7.647   -66.620  1.00 14.65 ? 144  LEU J CA  1 
ATOM   9964  C  C   . LEU I  1 144 ? 11.744 8.568   -67.696  1.00 14.15 ? 144  LEU J C   1 
ATOM   9965  O  O   . LEU I  1 144 ? 11.033 8.944   -68.629  1.00 14.23 ? 144  LEU J O   1 
ATOM   9966  C  CB  . LEU I  1 144 ? 10.647 8.493   -65.464  1.00 14.92 ? 144  LEU J CB  1 
ATOM   9967  C  CG  . LEU I  1 144 ? 9.988  7.776   -64.289  1.00 17.10 ? 144  LEU J CG  1 
ATOM   9968  C  CD1 . LEU I  1 144 ? 9.460  8.802   -63.268  1.00 19.54 ? 144  LEU J CD1 1 
ATOM   9969  C  CD2 . LEU I  1 144 ? 8.861  6.810   -64.714  1.00 20.38 ? 144  LEU J CD2 1 
ATOM   9970  N  N   . ALA I  1 145 ? 13.005 8.963   -67.537  1.00 13.00 ? 145  ALA J N   1 
ATOM   9971  C  CA  . ALA I  1 145 ? 13.670 9.793   -68.505  1.00 12.52 ? 145  ALA J CA  1 
ATOM   9972  C  C   . ALA I  1 145 ? 15.168 9.561   -68.466  1.00 11.84 ? 145  ALA J C   1 
ATOM   9973  O  O   . ALA I  1 145 ? 15.713 9.195   -67.435  1.00 11.76 ? 145  ALA J O   1 
ATOM   9974  C  CB  . ALA I  1 145 ? 13.333 11.268  -68.295  1.00 12.22 ? 145  ALA J CB  1 
ATOM   9975  N  N   . CYS I  1 146 ? 15.817 9.731   -69.613  1.00 11.31 ? 146  CYS J N   1 
ATOM   9976  C  CA  . CYS I  1 146 ? 17.270 9.555   -69.706  1.00 10.14 ? 146  CYS J CA  1 
ATOM   9977  C  C   . CYS I  1 146 ? 17.845 10.402  -70.809  1.00 11.08 ? 146  CYS J C   1 
ATOM   9978  O  O   . CYS I  1 146 ? 17.096 10.999  -71.629  1.00 11.46 ? 146  CYS J O   1 
ATOM   9979  C  CB  . CYS I  1 146 ? 17.640 8.079   -69.886  0.40 9.75  ? 146  CYS J CB  1 
ATOM   9980  S  SG  . CYS I  1 146 ? 16.994 7.271   -71.357  0.40 6.40  ? 146  CYS J SG  1 
ATOM   9981  N  N   . GLY I  1 147 ? 19.169 10.477  -70.823  1.00 10.71 ? 147  GLY J N   1 
ATOM   9982  C  CA  . GLY I  1 147 ? 19.889 11.083  -71.937  1.00 11.24 ? 147  GLY J CA  1 
ATOM   9983  C  C   . GLY I  1 147 ? 21.357 10.744  -71.872  1.00 11.28 ? 147  GLY J C   1 
ATOM   9984  O  O   . GLY I  1 147 ? 21.871 10.342  -70.798  1.00 10.13 ? 147  GLY J O   1 
ATOM   9985  N  N   . VAL I  1 148 ? 22.039 10.879  -73.005  1.00 11.19 ? 148  VAL J N   1 
ATOM   9986  C  CA  . VAL I  1 148 ? 23.486 10.656  -73.031  1.00 11.65 ? 148  VAL J CA  1 
ATOM   9987  C  C   . VAL I  1 148 ? 24.175 11.928  -72.553  1.00 12.03 ? 148  VAL J C   1 
ATOM   9988  O  O   . VAL I  1 148 ? 23.773 13.045  -72.913  1.00 12.09 ? 148  VAL J O   1 
ATOM   9989  C  CB  . VAL I  1 148 ? 23.998 10.192  -74.430  1.00 11.18 ? 148  VAL J CB  1 
ATOM   9990  C  CG1 . VAL I  1 148 ? 25.480 9.851   -74.369  1.00 11.88 ? 148  VAL J CG1 1 
ATOM   9991  C  CG2 . VAL I  1 148 ? 23.221 8.960   -74.878  1.00 11.30 ? 148  VAL J CG2 1 
ATOM   9992  N  N   . ILE I  1 149 ? 25.182 11.754  -71.696  1.00 12.05 ? 149  ILE J N   1 
ATOM   9993  C  CA  . ILE I  1 149 ? 25.922 12.876  -71.152  1.00 12.68 ? 149  ILE J CA  1 
ATOM   9994  C  C   . ILE I  1 149 ? 26.985 13.285  -72.152  1.00 13.31 ? 149  ILE J C   1 
ATOM   9995  O  O   . ILE I  1 149 ? 27.786 12.469  -72.589  1.00 12.61 ? 149  ILE J O   1 
ATOM   9996  C  CB  . ILE I  1 149 ? 26.574 12.514  -69.790  1.00 12.63 ? 149  ILE J CB  1 
ATOM   9997  C  CG1 . ILE I  1 149 ? 25.502 12.147  -68.760  1.00 13.22 ? 149  ILE J CG1 1 
ATOM   9998  C  CG2 . ILE I  1 149 ? 27.452 13.653  -69.280  1.00 11.99 ? 149  ILE J CG2 1 
ATOM   9999  C  CD1 . ILE I  1 149 ? 26.071 11.359  -67.537  1.00 14.17 ? 149  ILE J CD1 1 
ATOM   10000 N  N   . GLY I  1 150 ? 26.972 14.557  -72.523  1.00 14.34 ? 150  GLY J N   1 
ATOM   10001 C  CA  . GLY I  1 150 ? 27.860 15.050  -73.572  1.00 16.32 ? 150  GLY J CA  1 
ATOM   10002 C  C   . GLY I  1 150 ? 28.723 16.185  -73.082  1.00 17.17 ? 150  GLY J C   1 
ATOM   10003 O  O   . GLY I  1 150 ? 28.369 16.851  -72.118  1.00 17.55 ? 150  GLY J O   1 
ATOM   10004 N  N   . ILE I  1 151 ? 29.853 16.411  -73.745  1.00 18.20 ? 151  ILE J N   1 
ATOM   10005 C  CA  . ILE I  1 151 ? 30.724 17.542  -73.413  1.00 19.46 ? 151  ILE J CA  1 
ATOM   10006 C  C   . ILE I  1 151 ? 30.051 18.880  -73.754  1.00 20.38 ? 151  ILE J C   1 
ATOM   10007 O  O   . ILE I  1 151 ? 29.453 19.038  -74.829  1.00 20.49 ? 151  ILE J O   1 
ATOM   10008 C  CB  . ILE I  1 151 ? 32.107 17.435  -74.103  1.00 19.61 ? 151  ILE J CB  1 
ATOM   10009 C  CG1 . ILE I  1 151 ? 32.631 16.004  -74.009  1.00 20.99 ? 151  ILE J CG1 1 
ATOM   10010 C  CG2 . ILE I  1 151 ? 33.113 18.413  -73.472  1.00 19.80 ? 151  ILE J CG2 1 
ATOM   10011 C  CD1 . ILE I  1 151 ? 33.890 15.719  -74.827  1.00 22.83 ? 151  ILE J CD1 1 
ATOM   10012 N  N   . ALA I  1 152 ? 30.156 19.834  -72.826  1.00 21.47 ? 152  ALA J N   1 
ATOM   10013 C  CA  . ALA I  1 152 ? 29.596 21.187  -72.990  1.00 22.49 ? 152  ALA J CA  1 
ATOM   10014 C  C   . ALA I  1 152 ? 30.685 22.242  -73.131  1.00 23.34 ? 152  ALA J C   1 
ATOM   10015 O  O   . ALA I  1 152 ? 31.850 22.001  -72.802  1.00 23.91 ? 152  ALA J O   1 
ATOM   10016 C  CB  . ALA I  1 152 ? 28.684 21.531  -71.813  1.00 22.15 ? 152  ALA J CB  1 
ATOM   10017 N  N   . GLN I  1 153 ? 30.295 23.422  -73.604  1.00 24.70 ? 153  GLN J N   1 
ATOM   10018 C  CA  . GLN I  1 153 ? 31.222 24.543  -73.735  1.00 25.73 ? 153  GLN J CA  1 
ATOM   10019 C  C   . GLN I  1 153 ? 31.624 25.112  -72.380  1.00 25.82 ? 153  GLN J C   1 
ATOM   10020 O  O   . GLN I  1 153 ? 30.774 25.388  -71.539  1.00 26.04 ? 153  GLN J O   1 
ATOM   10021 C  CB  . GLN I  1 153 ? 30.605 25.650  -74.586  1.00 25.97 ? 153  GLN J CB  1 
ATOM   10022 C  CG  . GLN I  1 153 ? 31.568 26.781  -74.894  1.00 27.56 ? 153  GLN J CG  1 
ATOM   10023 C  CD  . GLN I  1 153 ? 31.018 27.739  -75.923  1.00 29.27 ? 153  GLN J CD  1 
ATOM   10024 O  OE1 . GLN I  1 153 ? 31.734 28.162  -76.832  1.00 30.69 ? 153  GLN J OE1 1 
ATOM   10025 N  NE2 . GLN I  1 153 ? 29.738 28.076  -75.799  1.00 29.17 ? 153  GLN J NE2 1 
ATOM   10026 O  OXT . GLN I  1 153 ? 32.806 25.326  -72.106  1.00 26.47 ? 153  GLN J OXT 1 
ATOM   10027 N  N   . ALA J  1 1   ? 37.955 -4.401  -78.435  1.00 27.71 ? 1    ALA K N   1 
ATOM   10028 C  CA  . ALA J  1 1   ? 37.206 -3.437  -79.303  1.00 27.42 ? 1    ALA K CA  1 
ATOM   10029 C  C   . ALA J  1 1   ? 36.410 -2.411  -78.488  1.00 27.16 ? 1    ALA K C   1 
ATOM   10030 O  O   . ALA J  1 1   ? 35.797 -2.753  -77.470  1.00 28.12 ? 1    ALA K O   1 
ATOM   10031 C  CB  . ALA J  1 1   ? 36.285 -4.189  -80.271  1.00 27.51 ? 1    ALA K CB  1 
ATOM   10032 N  N   . THR J  1 2   ? 36.447 -1.154  -78.934  1.00 26.00 ? 2    THR K N   1 
ATOM   10033 C  CA  . THR J  1 2   ? 35.609 -0.097  -78.382  1.00 24.36 ? 2    THR K CA  1 
ATOM   10034 C  C   . THR J  1 2   ? 34.442 0.099   -79.335  1.00 23.17 ? 2    THR K C   1 
ATOM   10035 O  O   . THR J  1 2   ? 34.622 0.168   -80.560  1.00 22.33 ? 2    THR K O   1 
ATOM   10036 C  CB  . THR J  1 2   ? 36.370 1.234   -78.223  1.00 24.37 ? 2    THR K CB  1 
ATOM   10037 O  OG1 . THR J  1 2   ? 37.574 1.021   -77.476  1.00 24.81 ? 2    THR K OG1 1 
ATOM   10038 C  CG2 . THR J  1 2   ? 35.518 2.255   -77.483  1.00 24.20 ? 2    THR K CG2 1 
ATOM   10039 N  N   . LYS J  1 3   ? 33.247 0.172   -78.768  1.00 21.52 ? 3    LYS K N   1 
ATOM   10040 C  CA  . LYS J  1 3   ? 32.040 0.371   -79.546  1.00 20.84 ? 3    LYS K CA  1 
ATOM   10041 C  C   . LYS J  1 3   ? 31.307 1.610   -79.054  1.00 20.39 ? 3    LYS K C   1 
ATOM   10042 O  O   . LYS J  1 3   ? 31.332 1.918   -77.862  1.00 18.63 ? 3    LYS K O   1 
ATOM   10043 C  CB  . LYS J  1 3   ? 31.137 -0.850  -79.433  1.00 21.27 ? 3    LYS K CB  1 
ATOM   10044 C  CG  . LYS J  1 3   ? 31.631 -2.046  -80.216  1.00 22.60 ? 3    LYS K CG  1 
ATOM   10045 C  CD  . LYS J  1 3   ? 30.996 -3.323  -79.725  1.00 25.31 ? 3    LYS K CD  1 
ATOM   10046 C  CE  . LYS J  1 3   ? 31.169 -4.419  -80.769  1.00 27.58 ? 3    LYS K CE  1 
ATOM   10047 N  NZ  . LYS J  1 3   ? 31.055 -5.780  -80.175  1.00 28.44 ? 3    LYS K NZ  1 
ATOM   10048 N  N   . ALA J  1 4   ? 30.654 2.302   -79.984  1.00 19.98 ? 4    ALA K N   1 
ATOM   10049 C  CA  . ALA J  1 4   ? 29.872 3.510   -79.683  1.00 19.88 ? 4    ALA K CA  1 
ATOM   10050 C  C   . ALA J  1 4   ? 28.624 3.543   -80.554  1.00 19.93 ? 4    ALA K C   1 
ATOM   10051 O  O   . ALA J  1 4   ? 28.542 2.822   -81.551  1.00 20.54 ? 4    ALA K O   1 
ATOM   10052 C  CB  . ALA J  1 4   ? 30.709 4.768   -79.908  1.00 19.40 ? 4    ALA K CB  1 
ATOM   10053 N  N   . VAL J  1 5   ? 27.658 4.386   -80.186  1.00 19.60 ? 5    VAL K N   1 
ATOM   10054 C  CA  . VAL J  1 5   ? 26.367 4.407   -80.858  1.00 18.85 ? 5    VAL K CA  1 
ATOM   10055 C  C   . VAL J  1 5   ? 25.722 5.781   -80.732  1.00 19.69 ? 5    VAL K C   1 
ATOM   10056 O  O   . VAL J  1 5   ? 25.890 6.484   -79.724  1.00 18.17 ? 5    VAL K O   1 
ATOM   10057 C  CB  . VAL J  1 5   ? 25.431 3.285   -80.327  1.00 18.80 ? 5    VAL K CB  1 
ATOM   10058 C  CG1 . VAL J  1 5   ? 24.890 3.621   -78.931  1.00 17.39 ? 5    VAL K CG1 1 
ATOM   10059 C  CG2 . VAL J  1 5   ? 24.266 3.017   -81.290  1.00 18.62 ? 5    VAL K CG2 1 
ATOM   10060 N  N   . CYS J  1 6   ? 24.978 6.167   -81.764  1.00 20.17 ? 6    CYS K N   1 
ATOM   10061 C  CA  . CYS J  1 6   ? 24.329 7.452   -81.753  1.00 20.99 ? 6    CYS K CA  1 
ATOM   10062 C  C   . CYS J  1 6   ? 22.948 7.342   -82.372  1.00 21.04 ? 6    CYS K C   1 
ATOM   10063 O  O   . CYS J  1 6   ? 22.816 6.871   -83.501  1.00 21.33 ? 6    CYS K O   1 
ATOM   10064 C  CB  . CYS J  1 6   ? 25.180 8.467   -82.501  1.00 20.82 ? 6    CYS K CB  1 
ATOM   10065 S  SG  . CYS J  1 6   ? 24.448 10.100  -82.609  1.00 23.61 ? 6    CYS K SG  1 
ATOM   10066 N  N   . VAL J  1 7   ? 21.936 7.749   -81.601  1.00 21.51 ? 7    VAL K N   1 
ATOM   10067 C  CA  . VAL J  1 7   ? 20.546 7.860   -82.057  1.00 21.37 ? 7    VAL K CA  1 
ATOM   10068 C  C   . VAL J  1 7   ? 20.323 9.298   -82.519  1.00 22.24 ? 7    VAL K C   1 
ATOM   10069 O  O   . VAL J  1 7   ? 20.444 10.231  -81.731  1.00 21.21 ? 7    VAL K O   1 
ATOM   10070 C  CB  . VAL J  1 7   ? 19.517 7.522   -80.927  1.00 21.27 ? 7    VAL K CB  1 
ATOM   10071 C  CG1 . VAL J  1 7   ? 18.063 7.675   -81.434  1.00 20.84 ? 7    VAL K CG1 1 
ATOM   10072 C  CG2 . VAL J  1 7   ? 19.723 6.110   -80.384  1.00 20.34 ? 7    VAL K CG2 1 
ATOM   10073 N  N   . LEU J  1 8   ? 20.018 9.470   -83.806  1.00 23.17 ? 8    LEU K N   1 
ATOM   10074 C  CA  . LEU J  1 8   ? 19.769 10.798  -84.352  1.00 24.22 ? 8    LEU K CA  1 
ATOM   10075 C  C   . LEU J  1 8   ? 18.281 11.086  -84.369  1.00 24.74 ? 8    LEU K C   1 
ATOM   10076 O  O   . LEU J  1 8   ? 17.488 10.244  -84.788  1.00 24.61 ? 8    LEU K O   1 
ATOM   10077 C  CB  . LEU J  1 8   ? 20.376 10.954  -85.746  1.00 24.52 ? 8    LEU K CB  1 
ATOM   10078 C  CG  . LEU J  1 8   ? 21.910 10.965  -85.751  1.00 25.31 ? 8    LEU K CG  1 
ATOM   10079 C  CD1 . LEU J  1 8   ? 22.396 9.671   -86.320  1.00 28.14 ? 8    LEU K CD1 1 
ATOM   10080 C  CD2 . LEU J  1 8   ? 22.449 12.130  -86.557  1.00 25.75 ? 8    LEU K CD2 1 
ATOM   10081 N  N   . LYS J  1 9   ? 17.927 12.269  -83.867  1.00 25.67 ? 9    LYS K N   1 
ATOM   10082 C  CA  . LYS J  1 9   ? 16.558 12.767  -83.814  1.00 26.38 ? 9    LYS K CA  1 
ATOM   10083 C  C   . LYS J  1 9   ? 16.617 14.260  -84.087  1.00 26.77 ? 9    LYS K C   1 
ATOM   10084 O  O   . LYS J  1 9   ? 17.620 14.913  -83.775  1.00 26.37 ? 9    LYS K O   1 
ATOM   10085 C  CB  . LYS J  1 9   ? 15.952 12.559  -82.428  1.00 27.06 ? 9    LYS K CB  1 
ATOM   10086 C  CG  . LYS J  1 9   ? 15.542 11.142  -82.085  1.00 28.65 ? 9    LYS K CG  1 
ATOM   10087 C  CD  . LYS J  1 9   ? 14.897 11.128  -80.695  1.00 33.40 ? 9    LYS K CD  1 
ATOM   10088 C  CE  . LYS J  1 9   ? 14.841 9.729   -80.096  1.00 35.07 ? 9    LYS K CE  1 
ATOM   10089 N  NZ  . LYS J  1 9   ? 14.269 8.736   -81.053  1.00 37.08 ? 9    LYS K NZ  1 
ATOM   10090 N  N   . GLY J  1 10  ? 15.548 14.811  -84.658  1.00 27.07 ? 10   GLY K N   1 
ATOM   10091 C  CA  . GLY J  1 10  ? 15.473 16.255  -84.862  1.00 27.97 ? 10   GLY K CA  1 
ATOM   10092 C  C   . GLY J  1 10  ? 14.078 16.780  -84.606  1.00 28.65 ? 10   GLY K C   1 
ATOM   10093 O  O   . GLY J  1 10  ? 13.261 16.111  -83.966  1.00 28.62 ? 10   GLY K O   1 
ATOM   10094 N  N   . ASP J  1 11  ? 13.812 17.979  -85.111  1.00 29.64 ? 11   ASP K N   1 
ATOM   10095 C  CA  . ASP J  1 11  ? 12.480 18.581  -85.030  1.00 30.63 ? 11   ASP K CA  1 
ATOM   10096 C  C   . ASP J  1 11  ? 11.550 17.976  -86.075  1.00 30.83 ? 11   ASP K C   1 
ATOM   10097 O  O   . ASP J  1 11  ? 10.328 17.888  -85.865  1.00 31.27 ? 11   ASP K O   1 
ATOM   10098 C  CB  . ASP J  1 11  ? 12.575 20.098  -85.217  1.00 30.79 ? 11   ASP K CB  1 
ATOM   10099 C  CG  . ASP J  1 11  ? 13.239 20.795  -84.037  1.00 32.07 ? 11   ASP K CG  1 
ATOM   10100 O  OD1 . ASP J  1 11  ? 13.644 21.966  -84.198  1.00 31.85 ? 11   ASP K OD1 1 
ATOM   10101 O  OD2 . ASP J  1 11  ? 13.347 20.178  -82.949  1.00 33.15 ? 11   ASP K OD2 1 
ATOM   10102 N  N   . GLY J  1 12  ? 12.143 17.557  -87.193  1.00 30.89 ? 12   GLY K N   1 
ATOM   10103 C  CA  . GLY J  1 12  ? 11.412 16.992  -88.328  1.00 31.19 ? 12   GLY K CA  1 
ATOM   10104 C  C   . GLY J  1 12  ? 11.286 15.476  -88.350  1.00 31.23 ? 12   GLY K C   1 
ATOM   10105 O  O   . GLY J  1 12  ? 11.268 14.845  -87.293  1.00 31.44 ? 12   GLY K O   1 
ATOM   10106 N  N   . PRO J  1 13  ? 11.201 14.881  -89.561  1.00 31.10 ? 13   PRO K N   1 
ATOM   10107 C  CA  . PRO J  1 13  ? 10.952 13.440  -89.746  1.00 30.76 ? 13   PRO K CA  1 
ATOM   10108 C  C   . PRO J  1 13  ? 12.222 12.573  -89.766  1.00 30.29 ? 13   PRO K C   1 
ATOM   10109 O  O   . PRO J  1 13  ? 12.130 11.343  -89.755  1.00 30.37 ? 13   PRO K O   1 
ATOM   10110 C  CB  . PRO J  1 13  ? 10.282 13.391  -91.121  1.00 30.77 ? 13   PRO K CB  1 
ATOM   10111 C  CG  . PRO J  1 13  ? 10.906 14.530  -91.875  1.00 30.70 ? 13   PRO K CG  1 
ATOM   10112 C  CD  . PRO J  1 13  ? 11.296 15.586  -90.857  1.00 31.57 ? 13   PRO K CD  1 
ATOM   10113 N  N   . VAL J  1 14  ? 13.382 13.223  -89.809  1.00 29.49 ? 14   VAL K N   1 
ATOM   10114 C  CA  . VAL J  1 14  ? 14.666 12.556  -89.993  1.00 28.90 ? 14   VAL K CA  1 
ATOM   10115 C  C   . VAL J  1 14  ? 15.069 11.816  -88.714  1.00 28.45 ? 14   VAL K C   1 
ATOM   10116 O  O   . VAL J  1 14  ? 15.169 12.426  -87.649  1.00 28.25 ? 14   VAL K O   1 
ATOM   10117 C  CB  . VAL J  1 14  ? 15.764 13.587  -90.390  1.00 28.72 ? 14   VAL K CB  1 
ATOM   10118 C  CG1 . VAL J  1 14  ? 17.094 12.906  -90.657  1.00 28.75 ? 14   VAL K CG1 1 
ATOM   10119 C  CG2 . VAL J  1 14  ? 15.328 14.404  -91.593  1.00 29.04 ? 14   VAL K CG2 1 
ATOM   10120 N  N   . GLN J  1 15  ? 15.264 10.501  -88.819  1.00 27.94 ? 15   GLN K N   1 
ATOM   10121 C  CA  . GLN J  1 15  ? 15.808 9.703   -87.699  1.00 27.34 ? 15   GLN K CA  1 
ATOM   10122 C  C   . GLN J  1 15  ? 16.728 8.561   -88.160  1.00 26.41 ? 15   GLN K C   1 
ATOM   10123 O  O   . GLN J  1 15  ? 16.722 8.165   -89.328  1.00 25.67 ? 15   GLN K O   1 
ATOM   10124 C  CB  . GLN J  1 15  ? 14.696 9.180   -86.780  1.00 27.39 ? 15   GLN K CB  1 
ATOM   10125 C  CG  . GLN J  1 15  ? 13.685 8.286   -87.457  1.00 29.28 ? 15   GLN K CG  1 
ATOM   10126 C  CD  . GLN J  1 15  ? 12.323 8.361   -86.796  1.00 31.91 ? 15   GLN K CD  1 
ATOM   10127 O  OE1 . GLN J  1 15  ? 11.335 8.759   -87.426  1.00 34.11 ? 15   GLN K OE1 1 
ATOM   10128 N  NE2 . GLN J  1 15  ? 12.259 7.985   -85.524  1.00 32.10 ? 15   GLN K NE2 1 
ATOM   10129 N  N   . GLY J  1 16  ? 17.526 8.048   -87.230  1.00 25.16 ? 16   GLY K N   1 
ATOM   10130 C  CA  . GLY J  1 16  ? 18.506 7.026   -87.560  1.00 23.88 ? 16   GLY K CA  1 
ATOM   10131 C  C   . GLY J  1 16  ? 19.317 6.580   -86.369  1.00 23.08 ? 16   GLY K C   1 
ATOM   10132 O  O   . GLY J  1 16  ? 19.370 7.270   -85.343  1.00 23.04 ? 16   GLY K O   1 
ATOM   10133 N  N   . ILE J  1 17  ? 19.922 5.407   -86.518  1.00 22.05 ? 17   ILE K N   1 
ATOM   10134 C  CA  . ILE J  1 17  ? 20.835 4.822   -85.539  1.00 21.09 ? 17   ILE K CA  1 
ATOM   10135 C  C   . ILE J  1 17  ? 22.159 4.551   -86.259  1.00 20.96 ? 17   ILE K C   1 
ATOM   10136 O  O   . ILE J  1 17  ? 22.191 3.881   -87.300  1.00 20.63 ? 17   ILE K O   1 
ATOM   10137 C  CB  . ILE J  1 17  ? 20.246 3.509   -84.927  1.00 21.12 ? 17   ILE K CB  1 
ATOM   10138 C  CG1 . ILE J  1 17  ? 18.993 3.827   -84.092  1.00 21.62 ? 17   ILE K CG1 1 
ATOM   10139 C  CG2 . ILE J  1 17  ? 21.301 2.739   -84.129  1.00 20.87 ? 17   ILE K CG2 1 
ATOM   10140 C  CD1 . ILE J  1 17  ? 18.275 2.631   -83.480  1.00 22.20 ? 17   ILE K CD1 1 
ATOM   10141 N  N   . ILE J  1 18  ? 23.245 5.082   -85.704  1.00 20.40 ? 18   ILE K N   1 
ATOM   10142 C  CA  . ILE J  1 18  ? 24.583 4.905   -86.268  1.00 19.99 ? 18   ILE K CA  1 
ATOM   10143 C  C   . ILE J  1 18  ? 25.473 4.208   -85.242  1.00 20.09 ? 18   ILE K C   1 
ATOM   10144 O  O   . ILE J  1 18  ? 25.537 4.639   -84.083  1.00 19.56 ? 18   ILE K O   1 
ATOM   10145 C  CB  . ILE J  1 18  ? 25.203 6.268   -86.695  1.00 19.65 ? 18   ILE K CB  1 
ATOM   10146 C  CG1 . ILE J  1 18  ? 24.309 6.972   -87.713  1.00 20.09 ? 18   ILE K CG1 1 
ATOM   10147 C  CG2 . ILE J  1 18  ? 26.611 6.086   -87.293  1.00 19.07 ? 18   ILE K CG2 1 
ATOM   10148 C  CD1 . ILE J  1 18  ? 24.128 6.224   -89.004  1.00 20.64 ? 18   ILE K CD1 1 
ATOM   10149 N  N   . ASN J  1 19  ? 26.129 3.130   -85.673  1.00 19.81 ? 19   ASN K N   1 
ATOM   10150 C  CA  . ASN J  1 19  ? 27.075 2.388   -84.838  1.00 20.12 ? 19   ASN K CA  1 
ATOM   10151 C  C   . ASN J  1 19  ? 28.509 2.742   -85.173  1.00 20.30 ? 19   ASN K C   1 
ATOM   10152 O  O   . ASN J  1 19  ? 28.825 3.066   -86.320  1.00 20.60 ? 19   ASN K O   1 
ATOM   10153 C  CB  . ASN J  1 19  ? 26.898 0.879   -85.012  1.00 19.67 ? 19   ASN K CB  1 
ATOM   10154 C  CG  . ASN J  1 19  ? 25.466 0.433   -84.835  1.00 20.21 ? 19   ASN K CG  1 
ATOM   10155 O  OD1 . ASN J  1 19  ? 24.957 0.405   -83.720  1.00 20.07 ? 19   ASN K OD1 1 
ATOM   10156 N  ND2 . ASN J  1 19  ? 24.804 0.070   -85.941  1.00 18.10 ? 19   ASN K ND2 1 
ATOM   10157 N  N   . PHE J  1 20  ? 29.375 2.645   -84.165  1.00 20.54 ? 20   PHE K N   1 
ATOM   10158 C  CA  . PHE J  1 20  ? 30.809 2.838   -84.334  1.00 20.78 ? 20   PHE K CA  1 
ATOM   10159 C  C   . PHE J  1 20  ? 31.526 1.652   -83.704  1.00 21.34 ? 20   PHE K C   1 
ATOM   10160 O  O   . PHE J  1 20  ? 31.139 1.166   -82.634  1.00 21.00 ? 20   PHE K O   1 
ATOM   10161 C  CB  . PHE J  1 20  ? 31.310 4.108   -83.638  1.00 20.79 ? 20   PHE K CB  1 
ATOM   10162 C  CG  . PHE J  1 20  ? 30.641 5.388   -84.079  1.00 20.31 ? 20   PHE K CG  1 
ATOM   10163 C  CD1 . PHE J  1 20  ? 31.355 6.333   -84.804  1.00 20.18 ? 20   PHE K CD1 1 
ATOM   10164 C  CD2 . PHE J  1 20  ? 29.330 5.687   -83.696  1.00 20.25 ? 20   PHE K CD2 1 
ATOM   10165 C  CE1 . PHE J  1 20  ? 30.762 7.537   -85.198  1.00 20.36 ? 20   PHE K CE1 1 
ATOM   10166 C  CE2 . PHE J  1 20  ? 28.721 6.886   -84.074  1.00 21.27 ? 20   PHE K CE2 1 
ATOM   10167 C  CZ  . PHE J  1 20  ? 29.436 7.812   -84.820  1.00 22.38 ? 20   PHE K CZ  1 
ATOM   10168 N  N   . GLU J  1 21  ? 32.575 1.193   -84.377  1.00 22.18 ? 21   GLU K N   1 
ATOM   10169 C  CA  . GLU J  1 21  ? 33.419 0.126   -83.860  1.00 23.04 ? 21   GLU K CA  1 
ATOM   10170 C  C   . GLU J  1 21  ? 34.863 0.426   -84.190  1.00 23.06 ? 21   GLU K C   1 
ATOM   10171 O  O   . GLU J  1 21  ? 35.174 0.854   -85.305  1.00 23.06 ? 21   GLU K O   1 
ATOM   10172 C  CB  . GLU J  1 21  ? 33.019 -1.226  -84.449  1.00 23.53 ? 21   GLU K CB  1 
ATOM   10173 C  CG  . GLU J  1 21  ? 33.907 -2.384  -83.986  1.00 25.82 ? 21   GLU K CG  1 
ATOM   10174 C  CD  . GLU J  1 21  ? 33.113 -3.629  -83.682  1.00 30.88 ? 21   GLU K CD  1 
ATOM   10175 O  OE1 . GLU J  1 21  ? 33.674 -4.552  -83.042  1.00 32.93 ? 21   GLU K OE1 1 
ATOM   10176 O  OE2 . GLU J  1 21  ? 31.919 -3.684  -84.071  1.00 33.11 ? 21   GLU K OE2 1 
ATOM   10177 N  N   . GLN J  1 22  ? 35.740 0.189   -83.216  1.00 23.28 ? 22   GLN K N   1 
ATOM   10178 C  CA  . GLN J  1 22  ? 37.168 0.385   -83.407  1.00 23.52 ? 22   GLN K CA  1 
ATOM   10179 C  C   . GLN J  1 22  ? 37.958 -0.758  -82.754  1.00 24.15 ? 22   GLN K C   1 
ATOM   10180 O  O   . GLN J  1 22  ? 38.178 -0.757  -81.547  1.00 23.97 ? 22   GLN K O   1 
ATOM   10181 C  CB  . GLN J  1 22  ? 37.570 1.753   -82.864  1.00 23.21 ? 22   GLN K CB  1 
ATOM   10182 C  CG  . GLN J  1 22  ? 38.993 2.161   -83.189  1.00 23.10 ? 22   GLN K CG  1 
ATOM   10183 C  CD  . GLN J  1 22  ? 39.375 3.466   -82.539  1.00 22.98 ? 22   GLN K CD  1 
ATOM   10184 O  OE1 . GLN J  1 22  ? 38.680 3.959   -81.639  1.00 24.07 ? 22   GLN K OE1 1 
ATOM   10185 N  NE2 . GLN J  1 22  ? 40.493 4.032   -82.970  1.00 21.68 ? 22   GLN K NE2 1 
ATOM   10186 N  N   . LYS J  1 23  ? 38.365 -1.736  -83.569  1.00 25.10 ? 23   LYS K N   1 
ATOM   10187 C  CA  . LYS J  1 23  ? 39.041 -2.959  -83.101  1.00 25.87 ? 23   LYS K CA  1 
ATOM   10188 C  C   . LYS J  1 23  ? 40.296 -2.702  -82.276  1.00 26.11 ? 23   LYS K C   1 
ATOM   10189 O  O   . LYS J  1 23  ? 40.571 -3.431  -81.313  1.00 26.34 ? 23   LYS K O   1 
ATOM   10190 C  CB  . LYS J  1 23  ? 39.415 -3.858  -84.286  1.00 26.28 ? 23   LYS K CB  1 
ATOM   10191 C  CG  . LYS J  1 23  ? 38.251 -4.604  -84.897  1.00 28.03 ? 23   LYS K CG  1 
ATOM   10192 C  CD  . LYS J  1 23  ? 38.330 -4.615  -86.418  1.00 30.20 ? 23   LYS K CD  1 
ATOM   10193 C  CE  . LYS J  1 23  ? 37.049 -5.175  -87.030  1.00 32.52 ? 23   LYS K CE  1 
ATOM   10194 N  NZ  . LYS J  1 23  ? 35.807 -4.563  -86.446  1.00 34.75 ? 23   LYS K NZ  1 
ATOM   10195 N  N   . GLU J  1 24  ? 41.044 -1.672  -82.668  1.00 26.04 ? 24   GLU K N   1 
ATOM   10196 C  CA  . GLU J  1 24  ? 42.308 -1.299  -82.036  1.00 26.64 ? 24   GLU K CA  1 
ATOM   10197 C  C   . GLU J  1 24  ? 42.381 0.212   -81.823  1.00 26.27 ? 24   GLU K C   1 
ATOM   10198 O  O   . GLU J  1 24  ? 41.953 0.983   -82.678  1.00 25.89 ? 24   GLU K O   1 
ATOM   10199 C  CB  . GLU J  1 24  ? 43.497 -1.765  -82.896  1.00 27.15 ? 24   GLU K CB  1 
ATOM   10200 C  CG  . GLU J  1 24  ? 44.272 -2.938  -82.300  1.00 28.97 ? 24   GLU K CG  1 
ATOM   10201 C  CD  . GLU J  1 24  ? 43.661 -4.283  -82.630  1.00 32.02 ? 24   GLU K CD  1 
ATOM   10202 O  OE1 . GLU J  1 24  ? 43.674 -5.177  -81.753  1.00 33.11 ? 24   GLU K OE1 1 
ATOM   10203 O  OE2 . GLU J  1 24  ? 43.171 -4.449  -83.768  1.00 33.52 ? 24   GLU K OE2 1 
ATOM   10204 N  N   . SER J  1 25  ? 42.939 0.632   -80.686  1.00 25.91 ? 25   SER K N   1 
ATOM   10205 C  CA  . SER J  1 25  ? 42.998 2.051   -80.311  1.00 25.94 ? 25   SER K CA  1 
ATOM   10206 C  C   . SER J  1 25  ? 43.723 2.943   -81.321  1.00 26.09 ? 25   SER K C   1 
ATOM   10207 O  O   . SER J  1 25  ? 43.420 4.131   -81.446  1.00 26.11 ? 25   SER K O   1 
ATOM   10208 C  CB  . SER J  1 25  ? 43.630 2.220   -78.920  1.00 26.11 ? 25   SER K CB  1 
ATOM   10209 O  OG  . SER J  1 25  ? 45.050 2.338   -78.992  1.00 24.94 ? 25   SER K OG  1 
ATOM   10210 N  N   . ASN J  1 26  ? 44.698 2.387   -82.029  1.00 26.45 ? 26   ASN K N   1 
ATOM   10211 C  CA  . ASN J  1 26  ? 45.378 3.161   -83.062  1.00 26.91 ? 26   ASN K CA  1 
ATOM   10212 C  C   . ASN J  1 26  ? 44.927 2.774   -84.474  1.00 26.77 ? 26   ASN K C   1 
ATOM   10213 O  O   . ASN J  1 26  ? 45.596 3.100   -85.465  1.00 27.22 ? 26   ASN K O   1 
ATOM   10214 C  CB  . ASN J  1 26  ? 46.908 3.085   -82.907  1.00 27.03 ? 26   ASN K CB  1 
ATOM   10215 C  CG  . ASN J  1 26  ? 47.451 1.695   -83.129  1.00 27.90 ? 26   ASN K CG  1 
ATOM   10216 O  OD1 . ASN J  1 26  ? 46.770 0.697   -82.891  1.00 28.23 ? 26   ASN K OD1 1 
ATOM   10217 N  ND2 . ASN J  1 26  ? 48.691 1.621   -83.602  1.00 29.13 ? 26   ASN K ND2 1 
ATOM   10218 N  N   . GLY J  1 27  ? 43.787 2.088   -84.553  1.00 26.44 ? 27   GLY K N   1 
ATOM   10219 C  CA  . GLY J  1 27  ? 43.239 1.621   -85.830  1.00 25.74 ? 27   GLY K CA  1 
ATOM   10220 C  C   . GLY J  1 27  ? 42.046 2.433   -86.298  1.00 25.28 ? 27   GLY K C   1 
ATOM   10221 O  O   . GLY J  1 27  ? 41.579 3.329   -85.582  1.00 25.04 ? 27   GLY K O   1 
ATOM   10222 N  N   . PRO J  1 28  ? 41.547 2.139   -87.516  1.00 24.89 ? 28   PRO K N   1 
ATOM   10223 C  CA  . PRO J  1 28  ? 40.390 2.856   -88.059  1.00 24.67 ? 28   PRO K CA  1 
ATOM   10224 C  C   . PRO J  1 28  ? 39.082 2.571   -87.303  1.00 24.22 ? 28   PRO K C   1 
ATOM   10225 O  O   . PRO J  1 28  ? 38.940 1.531   -86.659  1.00 23.71 ? 28   PRO K O   1 
ATOM   10226 C  CB  . PRO J  1 28  ? 40.290 2.314   -89.492  1.00 24.75 ? 28   PRO K CB  1 
ATOM   10227 C  CG  . PRO J  1 28  ? 40.876 0.948   -89.404  1.00 24.38 ? 28   PRO K CG  1 
ATOM   10228 C  CD  . PRO J  1 28  ? 42.033 1.111   -88.455  1.00 24.86 ? 28   PRO K CD  1 
ATOM   10229 N  N   . VAL J  1 29  ? 38.140 3.505   -87.411  1.00 24.27 ? 29   VAL K N   1 
ATOM   10230 C  CA  . VAL J  1 29  ? 36.796 3.357   -86.858  1.00 23.94 ? 29   VAL K CA  1 
ATOM   10231 C  C   . VAL J  1 29  ? 35.807 3.045   -87.984  1.00 24.26 ? 29   VAL K C   1 
ATOM   10232 O  O   . VAL J  1 29  ? 35.701 3.811   -88.941  1.00 24.25 ? 29   VAL K O   1 
ATOM   10233 C  CB  . VAL J  1 29  ? 36.365 4.658   -86.138  1.00 24.38 ? 29   VAL K CB  1 
ATOM   10234 C  CG1 . VAL J  1 29  ? 34.985 4.509   -85.492  1.00 23.24 ? 29   VAL K CG1 1 
ATOM   10235 C  CG2 . VAL J  1 29  ? 37.394 5.065   -85.097  1.00 22.61 ? 29   VAL K CG2 1 
ATOM   10236 N  N   . LYS J  1 30  ? 35.100 1.919   -87.870  1.00 24.56 ? 30   LYS K N   1 
ATOM   10237 C  CA  . LYS J  1 30  ? 33.971 1.605   -88.747  1.00 25.17 ? 30   LYS K CA  1 
ATOM   10238 C  C   . LYS J  1 30  ? 32.720 2.349   -88.282  1.00 25.05 ? 30   LYS K C   1 
ATOM   10239 O  O   . LYS J  1 30  ? 32.367 2.285   -87.108  1.00 24.48 ? 30   LYS K O   1 
ATOM   10240 C  CB  . LYS J  1 30  ? 33.657 0.108   -88.749  1.00 25.29 ? 30   LYS K CB  1 
ATOM   10241 C  CG  . LYS J  1 30  ? 34.716 -0.792  -89.355  1.00 27.69 ? 30   LYS K CG  1 
ATOM   10242 C  CD  . LYS J  1 30  ? 34.125 -2.179  -89.647  1.00 30.32 ? 30   LYS K CD  1 
ATOM   10243 C  CE  . LYS J  1 30  ? 35.201 -3.271  -89.630  1.00 32.22 ? 30   LYS K CE  1 
ATOM   10244 N  NZ  . LYS J  1 30  ? 36.296 -3.011  -90.608  1.00 32.43 ? 30   LYS K NZ  1 
ATOM   10245 N  N   . VAL J  1 31  ? 32.061 3.038   -89.214  1.00 24.67 ? 31   VAL K N   1 
ATOM   10246 C  CA  . VAL J  1 31  ? 30.807 3.757   -88.960  1.00 24.50 ? 31   VAL K CA  1 
ATOM   10247 C  C   . VAL J  1 31  ? 29.728 3.147   -89.852  1.00 24.80 ? 31   VAL K C   1 
ATOM   10248 O  O   . VAL J  1 31  ? 29.877 3.128   -91.075  1.00 24.88 ? 31   VAL K O   1 
ATOM   10249 C  CB  . VAL J  1 31  ? 30.959 5.257   -89.308  1.00 24.35 ? 31   VAL K CB  1 
ATOM   10250 C  CG1 . VAL J  1 31  ? 29.754 6.054   -88.845  1.00 24.29 ? 31   VAL K CG1 1 
ATOM   10251 C  CG2 . VAL J  1 31  ? 32.238 5.820   -88.706  1.00 24.53 ? 31   VAL K CG2 1 
ATOM   10252 N  N   . TRP J  1 32  ? 28.651 2.630   -89.265  1.00 24.86 ? 32   TRP K N   1 
ATOM   10253 C  CA  . TRP J  1 32  ? 27.583 2.062   -90.092  1.00 25.19 ? 32   TRP K CA  1 
ATOM   10254 C  C   . TRP J  1 32  ? 26.189 2.213   -89.488  1.00 25.29 ? 32   TRP K C   1 
ATOM   10255 O  O   . TRP J  1 32  ? 26.028 2.255   -88.272  1.00 25.12 ? 32   TRP K O   1 
ATOM   10256 C  CB  . TRP J  1 32  ? 27.881 0.596   -90.440  1.00 25.25 ? 32   TRP K CB  1 
ATOM   10257 C  CG  . TRP J  1 32  ? 27.579 -0.398  -89.351  1.00 25.04 ? 32   TRP K CG  1 
ATOM   10258 C  CD1 . TRP J  1 32  ? 26.497 -1.229  -89.282  1.00 25.28 ? 32   TRP K CD1 1 
ATOM   10259 C  CD2 . TRP J  1 32  ? 28.369 -0.669  -88.185  1.00 24.85 ? 32   TRP K CD2 1 
ATOM   10260 N  NE1 . TRP J  1 32  ? 26.560 -1.998  -88.146  1.00 25.19 ? 32   TRP K NE1 1 
ATOM   10261 C  CE2 . TRP J  1 32  ? 27.701 -1.678  -87.455  1.00 25.24 ? 32   TRP K CE2 1 
ATOM   10262 C  CE3 . TRP J  1 32  ? 29.574 -0.158  -87.686  1.00 24.58 ? 32   TRP K CE3 1 
ATOM   10263 C  CZ2 . TRP J  1 32  ? 28.204 -2.194  -86.254  1.00 24.80 ? 32   TRP K CZ2 1 
ATOM   10264 C  CZ3 . TRP J  1 32  ? 30.073 -0.667  -86.484  1.00 24.04 ? 32   TRP K CZ3 1 
ATOM   10265 C  CH2 . TRP J  1 32  ? 29.389 -1.676  -85.788  1.00 25.08 ? 32   TRP K CH2 1 
ATOM   10266 N  N   . GLY J  1 33  ? 25.177 2.287   -90.342  1.00 25.14 ? 33   GLY K N   1 
ATOM   10267 C  CA  . GLY J  1 33  ? 23.824 2.391   -89.840  1.00 25.89 ? 33   GLY K CA  1 
ATOM   10268 C  C   . GLY J  1 33  ? 22.835 2.867   -90.871  1.00 26.62 ? 33   GLY K C   1 
ATOM   10269 O  O   . GLY J  1 33  ? 23.117 2.884   -92.069  1.00 26.74 ? 33   GLY K O   1 
ATOM   10270 N  N   . SER J  1 34  ? 21.666 3.258   -90.393  1.00 26.85 ? 34   SER K N   1 
ATOM   10271 C  CA  . SER J  1 34  ? 20.573 3.604   -91.273  1.00 27.53 ? 34   SER K CA  1 
ATOM   10272 C  C   . SER J  1 34  ? 20.004 4.920   -90.810  1.00 27.23 ? 34   SER K C   1 
ATOM   10273 O  O   . SER J  1 34  ? 20.003 5.213   -89.620  1.00 26.81 ? 34   SER K O   1 
ATOM   10274 C  CB  . SER J  1 34  ? 19.503 2.517   -91.231  1.00 27.52 ? 34   SER K CB  1 
ATOM   10275 O  OG  . SER J  1 34  ? 18.637 2.624   -92.346  1.00 30.17 ? 34   SER K OG  1 
ATOM   10276 N  N   . ILE J  1 35  ? 19.555 5.713   -91.774  1.00 27.69 ? 35   ILE K N   1 
ATOM   10277 C  CA  . ILE J  1 35  ? 18.922 7.000   -91.535  1.00 27.60 ? 35   ILE K CA  1 
ATOM   10278 C  C   . ILE J  1 35  ? 17.754 7.093   -92.509  1.00 28.11 ? 35   ILE K C   1 
ATOM   10279 O  O   . ILE J  1 35  ? 17.909 6.734   -93.683  1.00 28.13 ? 35   ILE K O   1 
ATOM   10280 C  CB  . ILE J  1 35  ? 19.886 8.185   -91.823  1.00 27.69 ? 35   ILE K CB  1 
ATOM   10281 C  CG1 . ILE J  1 35  ? 21.235 8.003   -91.108  1.00 27.95 ? 35   ILE K CG1 1 
ATOM   10282 C  CG2 . ILE J  1 35  ? 19.225 9.504   -91.434  1.00 27.35 ? 35   ILE K CG2 1 
ATOM   10283 C  CD1 . ILE J  1 35  ? 22.201 9.139   -91.291  1.00 28.09 ? 35   ILE K CD1 1 
ATOM   10284 N  N   . LYS J  1 36  ? 16.601 7.567   -92.028  1.00 28.50 ? 36   LYS K N   1 
ATOM   10285 C  CA  . LYS J  1 36  ? 15.421 7.779   -92.881  1.00 28.71 ? 36   LYS K CA  1 
ATOM   10286 C  C   . LYS J  1 36  ? 14.724 9.122   -92.661  1.00 28.97 ? 36   LYS K C   1 
ATOM   10287 O  O   . LYS J  1 36  ? 15.004 9.822   -91.687  1.00 28.85 ? 36   LYS K O   1 
ATOM   10288 C  CB  . LYS J  1 36  ? 14.427 6.612   -92.771  1.00 29.08 ? 36   LYS K CB  1 
ATOM   10289 C  CG  . LYS J  1 36  ? 14.024 6.199   -91.361  1.00 30.63 ? 36   LYS K CG  1 
ATOM   10290 C  CD  . LYS J  1 36  ? 13.572 4.732   -91.324  1.00 33.14 ? 36   LYS K CD  1 
ATOM   10291 C  CE  . LYS J  1 36  ? 14.523 3.783   -92.089  1.00 34.81 ? 36   LYS K CE  1 
ATOM   10292 N  NZ  . LYS J  1 36  ? 15.871 3.545   -91.453  1.00 35.75 ? 36   LYS K NZ  1 
ATOM   10293 N  N   . GLY J  1 37  ? 13.816 9.464   -93.577  1.00 28.90 ? 37   GLY K N   1 
ATOM   10294 C  CA  . GLY J  1 37  ? 13.097 10.735  -93.551  1.00 28.98 ? 37   GLY K CA  1 
ATOM   10295 C  C   . GLY J  1 37  ? 13.834 11.842  -94.288  1.00 29.29 ? 37   GLY K C   1 
ATOM   10296 O  O   . GLY J  1 37  ? 13.436 13.003  -94.217  1.00 29.44 ? 37   GLY K O   1 
ATOM   10297 N  N   . LEU J  1 38  ? 14.903 11.478  -94.993  1.00 29.55 ? 38   LEU K N   1 
ATOM   10298 C  CA  . LEU J  1 38  ? 15.719 12.431  -95.750  1.00 30.11 ? 38   LEU K CA  1 
ATOM   10299 C  C   . LEU J  1 38  ? 15.230 12.623  -97.189  1.00 30.62 ? 38   LEU K C   1 
ATOM   10300 O  O   . LEU J  1 38  ? 14.692 11.698  -97.802  1.00 30.11 ? 38   LEU K O   1 
ATOM   10301 C  CB  . LEU J  1 38  ? 17.181 11.971  -95.793  1.00 30.22 ? 38   LEU K CB  1 
ATOM   10302 C  CG  . LEU J  1 38  ? 18.063 12.113  -94.544  1.00 29.76 ? 38   LEU K CG  1 
ATOM   10303 C  CD1 . LEU J  1 38  ? 19.420 11.503  -94.821  1.00 29.95 ? 38   LEU K CD1 1 
ATOM   10304 C  CD2 . LEU J  1 38  ? 18.229 13.576  -94.134  1.00 30.60 ? 38   LEU K CD2 1 
ATOM   10305 N  N   . THR J  1 39  ? 15.434 13.828  -97.717  1.00 31.27 ? 39   THR K N   1 
ATOM   10306 C  CA  . THR J  1 39  ? 15.216 14.097  -99.137  1.00 32.09 ? 39   THR K CA  1 
ATOM   10307 C  C   . THR J  1 39  ? 16.267 13.315  -99.917  1.00 32.37 ? 39   THR K C   1 
ATOM   10308 O  O   . THR J  1 39  ? 17.414 13.189  -99.466  1.00 32.18 ? 39   THR K O   1 
ATOM   10309 C  CB  . THR J  1 39  ? 15.357 15.598  -99.481  1.00 32.04 ? 39   THR K CB  1 
ATOM   10310 O  OG1 . THR J  1 39  ? 16.719 16.012  -99.293  1.00 33.06 ? 39   THR K OG1 1 
ATOM   10311 C  CG2 . THR J  1 39  ? 14.437 16.458  -98.614  1.00 32.01 ? 39   THR K CG2 1 
ATOM   10312 N  N   . GLU J  1 40  ? 15.868 12.775  -101.070 1.00 32.69 ? 40   GLU K N   1 
ATOM   10313 C  CA  . GLU J  1 40  ? 16.774 12.004  -101.923 1.00 32.78 ? 40   GLU K CA  1 
ATOM   10314 C  C   . GLU J  1 40  ? 18.003 12.846  -102.241 1.00 32.45 ? 40   GLU K C   1 
ATOM   10315 O  O   . GLU J  1 40  ? 17.882 14.036  -102.519 1.00 32.55 ? 40   GLU K O   1 
ATOM   10316 C  CB  . GLU J  1 40  ? 16.072 11.571  -103.217 1.00 33.01 ? 40   GLU K CB  1 
ATOM   10317 C  CG  . GLU J  1 40  ? 16.797 10.461  -103.978 1.00 33.92 ? 40   GLU K CG  1 
ATOM   10318 C  CD  . GLU J  1 40  ? 16.210 10.176  -105.362 1.00 36.44 ? 40   GLU K CD  1 
ATOM   10319 O  OE1 . GLU J  1 40  ? 15.632 11.100  -105.979 1.00 35.53 ? 40   GLU K OE1 1 
ATOM   10320 O  OE2 . GLU J  1 40  ? 16.337 9.021   -105.837 1.00 36.61 ? 40   GLU K OE2 1 
ATOM   10321 N  N   . GLY J  1 41  ? 19.180 12.228  -102.177 1.00 32.35 ? 41   GLY K N   1 
ATOM   10322 C  CA  . GLY J  1 41  ? 20.429 12.909  -102.519 1.00 32.12 ? 41   GLY K CA  1 
ATOM   10323 C  C   . GLY J  1 41  ? 21.451 12.881  -101.397 1.00 31.95 ? 41   GLY K C   1 
ATOM   10324 O  O   . GLY J  1 41  ? 21.262 12.192  -100.394 1.00 31.80 ? 41   GLY K O   1 
ATOM   10325 N  N   . LEU J  1 42  ? 22.531 13.639  -101.570 1.00 31.72 ? 42   LEU K N   1 
ATOM   10326 C  CA  . LEU J  1 42  ? 23.609 13.706  -100.580 1.00 31.33 ? 42   LEU K CA  1 
ATOM   10327 C  C   . LEU J  1 42  ? 23.243 14.589  -99.390  1.00 31.09 ? 42   LEU K C   1 
ATOM   10328 O  O   . LEU J  1 42  ? 22.636 15.653  -99.557  1.00 30.85 ? 42   LEU K O   1 
ATOM   10329 C  CB  . LEU J  1 42  ? 24.889 14.263  -101.210 1.00 31.55 ? 42   LEU K CB  1 
ATOM   10330 C  CG  . LEU J  1 42  ? 25.622 13.622  -102.386 1.00 31.66 ? 42   LEU K CG  1 
ATOM   10331 C  CD1 . LEU J  1 42  ? 26.838 14.470  -102.734 1.00 31.10 ? 42   LEU K CD1 1 
ATOM   10332 C  CD2 . LEU J  1 42  ? 26.050 12.208  -102.053 1.00 32.82 ? 42   LEU K CD2 1 
ATOM   10333 N  N   . HIS J  1 43  ? 23.651 14.160  -98.192  1.00 30.64 ? 43   HIS K N   1 
ATOM   10334 C  CA  . HIS J  1 43  ? 23.453 14.951  -96.980  1.00 30.38 ? 43   HIS K CA  1 
ATOM   10335 C  C   . HIS J  1 43  ? 24.715 14.987  -96.109  1.00 29.91 ? 43   HIS K C   1 
ATOM   10336 O  O   . HIS J  1 43  ? 25.287 13.942  -95.803  1.00 30.04 ? 43   HIS K O   1 
ATOM   10337 C  CB  . HIS J  1 43  ? 22.280 14.397  -96.175  1.00 30.52 ? 43   HIS K CB  1 
ATOM   10338 C  CG  . HIS J  1 43  ? 20.955 14.595  -96.835  1.00 30.45 ? 43   HIS K CG  1 
ATOM   10339 N  ND1 . HIS J  1 43  ? 20.148 15.679  -96.569  1.00 30.83 ? 43   HIS K ND1 1 
ATOM   10340 C  CD2 . HIS J  1 43  ? 20.294 13.849  -97.751  1.00 30.47 ? 43   HIS K CD2 1 
ATOM   10341 C  CE1 . HIS J  1 43  ? 19.046 15.594  -97.293  1.00 30.78 ? 43   HIS K CE1 1 
ATOM   10342 N  NE2 . HIS J  1 43  ? 19.110 14.492  -98.018  1.00 31.45 ? 43   HIS K NE2 1 
ATOM   10343 N  N   . GLY J  1 44  ? 25.135 16.194  -95.728  1.00 29.40 ? 44   GLY K N   1 
ATOM   10344 C  CA  . GLY J  1 44  ? 26.304 16.402  -94.860  1.00 29.10 ? 44   GLY K CA  1 
ATOM   10345 C  C   . GLY J  1 44  ? 26.219 15.591  -93.571  1.00 28.53 ? 44   GLY K C   1 
ATOM   10346 O  O   . GLY J  1 44  ? 25.135 15.380  -93.037  1.00 27.98 ? 44   GLY K O   1 
ATOM   10347 N  N   . PHE J  1 45  ? 27.370 15.143  -93.073  1.00 28.54 ? 45   PHE K N   1 
ATOM   10348 C  CA  . PHE J  1 45  ? 27.428 14.148  -92.006  1.00 28.17 ? 45   PHE K CA  1 
ATOM   10349 C  C   . PHE J  1 45  ? 28.718 14.400  -91.235  1.00 28.44 ? 45   PHE K C   1 
ATOM   10350 O  O   . PHE J  1 45  ? 29.814 14.174  -91.760  1.00 28.23 ? 45   PHE K O   1 
ATOM   10351 C  CB  . PHE J  1 45  ? 27.419 12.754  -92.645  1.00 28.33 ? 45   PHE K CB  1 
ATOM   10352 C  CG  . PHE J  1 45  ? 27.239 11.615  -91.680  1.00 27.50 ? 45   PHE K CG  1 
ATOM   10353 C  CD1 . PHE J  1 45  ? 26.102 11.516  -90.875  1.00 27.65 ? 45   PHE K CD1 1 
ATOM   10354 C  CD2 . PHE J  1 45  ? 28.186 10.601  -91.620  1.00 27.36 ? 45   PHE K CD2 1 
ATOM   10355 C  CE1 . PHE J  1 45  ? 25.931 10.432  -90.006  1.00 25.99 ? 45   PHE K CE1 1 
ATOM   10356 C  CE2 . PHE J  1 45  ? 28.025 9.522   -90.762  1.00 25.71 ? 45   PHE K CE2 1 
ATOM   10357 C  CZ  . PHE J  1 45  ? 26.895 9.435   -89.953  1.00 26.15 ? 45   PHE K CZ  1 
ATOM   10358 N  N   . HIS J  1 46  ? 28.589 14.899  -90.005  1.00 28.19 ? 46   HIS K N   1 
ATOM   10359 C  CA  . HIS J  1 46  ? 29.749 15.333  -89.241  1.00 28.19 ? 46   HIS K CA  1 
ATOM   10360 C  C   . HIS J  1 46  ? 29.626 15.011  -87.751  1.00 27.92 ? 46   HIS K C   1 
ATOM   10361 O  O   . HIS J  1 46  ? 28.526 14.741  -87.246  1.00 27.79 ? 46   HIS K O   1 
ATOM   10362 C  CB  . HIS J  1 46  ? 29.968 16.848  -89.362  1.00 28.38 ? 46   HIS K CB  1 
ATOM   10363 C  CG  . HIS J  1 46  ? 29.754 17.401  -90.736  1.00 30.27 ? 46   HIS K CG  1 
ATOM   10364 N  ND1 . HIS J  1 46  ? 28.766 18.320  -91.019  1.00 31.96 ? 46   HIS K ND1 1 
ATOM   10365 C  CD2 . HIS J  1 46  ? 30.409 17.183  -91.901  1.00 31.41 ? 46   HIS K CD2 1 
ATOM   10366 C  CE1 . HIS J  1 46  ? 28.815 18.640  -92.300  1.00 31.35 ? 46   HIS K CE1 1 
ATOM   10367 N  NE2 . HIS J  1 46  ? 29.799 17.960  -92.859  1.00 31.18 ? 46   HIS K NE2 1 
ATOM   10368 N  N   . VAL J  1 47  ? 30.773 15.055  -87.068  1.00 27.43 ? 47   VAL K N   1 
ATOM   10369 C  CA  . VAL J  1 47  ? 30.829 15.109  -85.608  1.00 27.06 ? 47   VAL K CA  1 
ATOM   10370 C  C   . VAL J  1 47  ? 31.009 16.581  -85.213  1.00 27.01 ? 47   VAL K C   1 
ATOM   10371 O  O   . VAL J  1 47  ? 32.021 17.196  -85.554  1.00 27.58 ? 47   VAL K O   1 
ATOM   10372 C  CB  . VAL J  1 47  ? 32.002 14.287  -85.020  1.00 26.70 ? 47   VAL K CB  1 
ATOM   10373 C  CG1 . VAL J  1 47  ? 32.042 14.424  -83.473  1.00 26.23 ? 47   VAL K CG1 1 
ATOM   10374 C  CG2 . VAL J  1 47  ? 31.908 12.814  -85.433  1.00 27.04 ? 47   VAL K CG2 1 
ATOM   10375 N  N   . HIS J  1 48  ? 30.029 17.136  -84.510  1.00 27.07 ? 48   HIS K N   1 
ATOM   10376 C  CA  . HIS J  1 48  ? 30.156 18.475  -83.938  1.00 27.47 ? 48   HIS K CA  1 
ATOM   10377 C  C   . HIS J  1 48  ? 30.765 18.458  -82.533  1.00 27.59 ? 48   HIS K C   1 
ATOM   10378 O  O   . HIS J  1 48  ? 30.730 17.441  -81.838  1.00 27.31 ? 48   HIS K O   1 
ATOM   10379 C  CB  . HIS J  1 48  ? 28.819 19.209  -83.960  1.00 27.43 ? 48   HIS K CB  1 
ATOM   10380 C  CG  . HIS J  1 48  ? 28.385 19.606  -85.337  1.00 28.62 ? 48   HIS K CG  1 
ATOM   10381 N  ND1 . HIS J  1 48  ? 28.239 20.923  -85.723  1.00 29.67 ? 48   HIS K ND1 1 
ATOM   10382 C  CD2 . HIS J  1 48  ? 28.085 18.861  -86.428  1.00 29.25 ? 48   HIS K CD2 1 
ATOM   10383 C  CE1 . HIS J  1 48  ? 27.851 20.970  -86.986  1.00 29.35 ? 48   HIS K CE1 1 
ATOM   10384 N  NE2 . HIS J  1 48  ? 27.735 19.732  -87.432  1.00 29.28 ? 48   HIS K NE2 1 
ATOM   10385 N  N   . GLU J  1 49  ? 31.315 19.598  -82.133  1.00 27.44 ? 49   GLU K N   1 
ATOM   10386 C  CA  . GLU J  1 49  ? 32.173 19.685  -80.962  1.00 27.81 ? 49   GLU K CA  1 
ATOM   10387 C  C   . GLU J  1 49  ? 31.506 19.320  -79.628  1.00 27.32 ? 49   GLU K C   1 
ATOM   10388 O  O   . GLU J  1 49  ? 32.102 18.615  -78.817  1.00 27.45 ? 49   GLU K O   1 
ATOM   10389 C  CB  . GLU J  1 49  ? 32.783 21.086  -80.884  1.00 27.99 ? 49   GLU K CB  1 
ATOM   10390 C  CG  . GLU J  1 49  ? 33.731 21.260  -79.729  1.00 29.37 ? 49   GLU K CG  1 
ATOM   10391 C  CD  . GLU J  1 49  ? 34.445 22.590  -79.733  1.00 30.77 ? 49   GLU K CD  1 
ATOM   10392 O  OE1 . GLU J  1 49  ? 35.384 22.733  -78.927  1.00 31.64 ? 49   GLU K OE1 1 
ATOM   10393 O  OE2 . GLU J  1 49  ? 34.074 23.485  -80.526  1.00 31.31 ? 49   GLU K OE2 1 
ATOM   10394 N  N   . PHE J  1 50  ? 30.281 19.801  -79.404  1.00 26.85 ? 50   PHE K N   1 
ATOM   10395 C  CA  . PHE J  1 50  ? 29.623 19.639  -78.101  1.00 26.26 ? 50   PHE K CA  1 
ATOM   10396 C  C   . PHE J  1 50  ? 28.457 18.668  -78.134  1.00 26.04 ? 50   PHE K C   1 
ATOM   10397 O  O   . PHE J  1 50  ? 27.611 18.728  -79.036  1.00 25.76 ? 50   PHE K O   1 
ATOM   10398 C  CB  . PHE J  1 50  ? 29.165 21.003  -77.544  1.00 26.19 ? 50   PHE K CB  1 
ATOM   10399 C  CG  . PHE J  1 50  ? 30.259 22.031  -77.496  1.00 27.05 ? 50   PHE K CG  1 
ATOM   10400 C  CD1 . PHE J  1 50  ? 31.371 21.845  -76.678  1.00 28.16 ? 50   PHE K CD1 1 
ATOM   10401 C  CD2 . PHE J  1 50  ? 30.191 23.179  -78.289  1.00 28.57 ? 50   PHE K CD2 1 
ATOM   10402 C  CE1 . PHE J  1 50  ? 32.405 22.786  -76.641  1.00 28.99 ? 50   PHE K CE1 1 
ATOM   10403 C  CE2 . PHE J  1 50  ? 31.218 24.130  -78.266  1.00 29.58 ? 50   PHE K CE2 1 
ATOM   10404 C  CZ  . PHE J  1 50  ? 32.322 23.938  -77.434  1.00 30.14 ? 50   PHE K CZ  1 
ATOM   10405 N  N   . GLY J  1 51  ? 28.412 17.776  -77.140  1.00 25.22 ? 51   GLY K N   1 
ATOM   10406 C  CA  . GLY J  1 51  ? 27.270 16.897  -76.954  1.00 25.10 ? 51   GLY K CA  1 
ATOM   10407 C  C   . GLY J  1 51  ? 26.168 17.631  -76.213  1.00 25.39 ? 51   GLY K C   1 
ATOM   10408 O  O   . GLY J  1 51  ? 25.661 17.145  -75.198  1.00 24.71 ? 51   GLY K O   1 
ATOM   10409 N  N   . ASP J  1 52  ? 25.811 18.817  -76.719  1.00 25.33 ? 52   ASP K N   1 
ATOM   10410 C  CA  . ASP J  1 52  ? 24.831 19.685  -76.080  1.00 25.12 ? 52   ASP K CA  1 
ATOM   10411 C  C   . ASP J  1 52  ? 23.574 19.829  -76.928  1.00 25.36 ? 52   ASP K C   1 
ATOM   10412 O  O   . ASP J  1 52  ? 23.603 20.421  -78.004  1.00 25.57 ? 52   ASP K O   1 
ATOM   10413 C  CB  . ASP J  1 52  ? 25.433 21.065  -75.799  1.00 24.83 ? 52   ASP K CB  1 
ATOM   10414 C  CG  . ASP J  1 52  ? 24.535 21.940  -74.923  1.00 24.33 ? 52   ASP K CG  1 
ATOM   10415 O  OD1 . ASP J  1 52  ? 25.059 22.905  -74.340  1.00 25.16 ? 52   ASP K OD1 1 
ATOM   10416 O  OD2 . ASP J  1 52  ? 23.314 21.673  -74.809  1.00 23.69 ? 52   ASP K OD2 1 
ATOM   10417 N  N   . ASN J  1 53  ? 22.461 19.302  -76.427  1.00 25.85 ? 53   ASN K N   1 
ATOM   10418 C  CA  . ASN J  1 53  ? 21.205 19.342  -77.172  1.00 25.89 ? 53   ASN K CA  1 
ATOM   10419 C  C   . ASN J  1 53  ? 20.133 20.218  -76.523  1.00 25.70 ? 53   ASN K C   1 
ATOM   10420 O  O   . ASN J  1 53  ? 18.952 20.127  -76.868  1.00 25.84 ? 53   ASN K O   1 
ATOM   10421 C  CB  . ASN J  1 53  ? 20.680 17.916  -77.407  1.00 26.32 ? 53   ASN K CB  1 
ATOM   10422 C  CG  . ASN J  1 53  ? 19.643 17.854  -78.516  1.00 26.95 ? 53   ASN K CG  1 
ATOM   10423 O  OD1 . ASN J  1 53  ? 18.525 17.377  -78.309  1.00 28.88 ? 53   ASN K OD1 1 
ATOM   10424 N  ND2 . ASN J  1 53  ? 20.001 18.356  -79.692  1.00 28.30 ? 53   ASN K ND2 1 
ATOM   10425 N  N   . THR J  1 54  ? 20.553 21.083  -75.605  1.00 25.62 ? 54   THR K N   1 
ATOM   10426 C  CA  . THR J  1 54  ? 19.627 21.913  -74.840  1.00 25.77 ? 54   THR K CA  1 
ATOM   10427 C  C   . THR J  1 54  ? 18.770 22.815  -75.729  1.00 25.97 ? 54   THR K C   1 
ATOM   10428 O  O   . THR J  1 54  ? 17.607 23.052  -75.421  1.00 25.78 ? 54   THR K O   1 
ATOM   10429 C  CB  . THR J  1 54  ? 20.354 22.766  -73.786  1.00 25.54 ? 54   THR K CB  1 
ATOM   10430 O  OG1 . THR J  1 54  ? 21.407 23.517  -74.407  1.00 24.54 ? 54   THR K OG1 1 
ATOM   10431 C  CG2 . THR J  1 54  ? 20.939 21.877  -72.695  1.00 25.50 ? 54   THR K CG2 1 
ATOM   10432 N  N   . ALA J  1 55  ? 19.351 23.291  -76.828  1.00 26.24 ? 55   ALA K N   1 
ATOM   10433 C  CA  . ALA J  1 55  ? 18.636 24.116  -77.808  1.00 26.92 ? 55   ALA K CA  1 
ATOM   10434 C  C   . ALA J  1 55  ? 18.619 23.439  -79.176  1.00 27.09 ? 55   ALA K C   1 
ATOM   10435 O  O   . ALA J  1 55  ? 18.970 24.052  -80.186  1.00 27.77 ? 55   ALA K O   1 
ATOM   10436 C  CB  . ALA J  1 55  ? 19.264 25.498  -77.900  1.00 26.57 ? 55   ALA K CB  1 
ATOM   10437 N  N   . GLY J  1 56  ? 18.197 22.176  -79.209  1.00 27.57 ? 56   GLY K N   1 
ATOM   10438 C  CA  . GLY J  1 56  ? 18.277 21.369  -80.428  1.00 27.29 ? 56   GLY K CA  1 
ATOM   10439 C  C   . GLY J  1 56  ? 19.704 21.228  -80.949  1.00 27.46 ? 56   GLY K C   1 
ATOM   10440 O  O   . GLY J  1 56  ? 20.676 21.498  -80.222  1.00 27.92 ? 56   GLY K O   1 
ATOM   10441 N  N   . CYS J  1 57  ? 19.828 20.810  -82.209  1.00 26.58 ? 57   CYS K N   1 
ATOM   10442 C  CA  . CYS J  1 57  ? 21.124 20.531  -82.839  1.00 25.65 ? 57   CYS K CA  1 
ATOM   10443 C  C   . CYS J  1 57  ? 22.039 21.759  -82.962  1.00 26.30 ? 57   CYS K C   1 
ATOM   10444 O  O   . CYS J  1 57  ? 23.238 21.628  -83.183  1.00 25.97 ? 57   CYS K O   1 
ATOM   10445 C  CB  . CYS J  1 57  ? 20.903 19.889  -84.210  0.40 24.83 ? 57   CYS K CB  1 
ATOM   10446 S  SG  . CYS J  1 57  ? 20.059 18.308  -84.113  0.40 20.77 ? 57   CYS K SG  1 
ATOM   10447 N  N   . THR J  1 58  ? 21.457 22.945  -82.806  1.00 27.06 ? 58   THR K N   1 
ATOM   10448 C  CA  . THR J  1 58  ? 22.200 24.212  -82.797  1.00 27.64 ? 58   THR K CA  1 
ATOM   10449 C  C   . THR J  1 58  ? 23.283 24.266  -81.703  1.00 28.01 ? 58   THR K C   1 
ATOM   10450 O  O   . THR J  1 58  ? 24.415 24.699  -81.959  1.00 27.66 ? 58   THR K O   1 
ATOM   10451 C  CB  . THR J  1 58  ? 21.224 25.411  -82.610  1.00 27.94 ? 58   THR K CB  1 
ATOM   10452 O  OG1 . THR J  1 58  ? 20.125 25.280  -83.524  1.00 27.91 ? 58   THR K OG1 1 
ATOM   10453 C  CG2 . THR J  1 58  ? 21.926 26.758  -82.822  1.00 28.06 ? 58   THR K CG2 1 
ATOM   10454 N  N   . SER J  1 59  ? 22.940 23.827  -80.491  1.00 28.25 ? 59   SER K N   1 
ATOM   10455 C  CA  . SER J  1 59  ? 23.871 23.960  -79.356  1.00 28.59 ? 59   SER K CA  1 
ATOM   10456 C  C   . SER J  1 59  ? 25.084 23.023  -79.423  1.00 28.72 ? 59   SER K C   1 
ATOM   10457 O  O   . SER J  1 59  ? 25.968 23.079  -78.559  1.00 29.06 ? 59   SER K O   1 
ATOM   10458 C  CB  . SER J  1 59  ? 23.136 23.853  -78.011  1.00 28.47 ? 59   SER K CB  1 
ATOM   10459 O  OG  . SER J  1 59  ? 22.043 22.959  -78.079  1.00 28.75 ? 59   SER K OG  1 
ATOM   10460 N  N   . ALA J  1 60  ? 25.136 22.188  -80.465  1.00 28.74 ? 60   ALA K N   1 
ATOM   10461 C  CA  . ALA J  1 60  ? 26.257 21.268  -80.681  1.00 28.72 ? 60   ALA K CA  1 
ATOM   10462 C  C   . ALA J  1 60  ? 27.514 21.983  -81.161  1.00 28.95 ? 60   ALA K C   1 
ATOM   10463 O  O   . ALA J  1 60  ? 28.584 21.373  -81.245  1.00 29.04 ? 60   ALA K O   1 
ATOM   10464 C  CB  . ALA J  1 60  ? 25.874 20.168  -81.660  1.00 28.51 ? 60   ALA K CB  1 
ATOM   10465 N  N   . GLY J  1 61  ? 27.375 23.268  -81.480  1.00 29.03 ? 61   GLY K N   1 
ATOM   10466 C  CA  . GLY J  1 61  ? 28.498 24.099  -81.872  1.00 29.54 ? 61   GLY K CA  1 
ATOM   10467 C  C   . GLY J  1 61  ? 29.005 23.781  -83.262  1.00 29.79 ? 61   GLY K C   1 
ATOM   10468 O  O   . GLY J  1 61  ? 28.310 23.133  -84.049  1.00 30.26 ? 61   GLY K O   1 
ATOM   10469 N  N   . PRO J  1 62  ? 30.231 24.226  -83.572  1.00 30.20 ? 62   PRO K N   1 
ATOM   10470 C  CA  . PRO J  1 62  ? 30.818 23.995  -84.890  1.00 30.26 ? 62   PRO K CA  1 
ATOM   10471 C  C   . PRO J  1 62  ? 31.249 22.536  -85.053  1.00 30.26 ? 62   PRO K C   1 
ATOM   10472 O  O   . PRO J  1 62  ? 31.048 21.717  -84.150  1.00 30.05 ? 62   PRO K O   1 
ATOM   10473 C  CB  . PRO J  1 62  ? 32.042 24.914  -84.879  1.00 30.13 ? 62   PRO K CB  1 
ATOM   10474 C  CG  . PRO J  1 62  ? 32.442 24.961  -83.434  1.00 30.30 ? 62   PRO K CG  1 
ATOM   10475 C  CD  . PRO J  1 62  ? 31.156 24.936  -82.669  1.00 30.02 ? 62   PRO K CD  1 
ATOM   10476 N  N   . HIS J  1 63  ? 31.849 22.223  -86.195  1.00 30.37 ? 63   HIS K N   1 
ATOM   10477 C  CA  . HIS J  1 63  ? 32.426 20.900  -86.436  1.00 30.27 ? 63   HIS K CA  1 
ATOM   10478 C  C   . HIS J  1 63  ? 33.554 20.643  -85.434  1.00 30.41 ? 63   HIS K C   1 
ATOM   10479 O  O   . HIS J  1 63  ? 34.264 21.580  -85.035  1.00 29.92 ? 63   HIS K O   1 
ATOM   10480 C  CB  . HIS J  1 63  ? 32.958 20.815  -87.873  1.00 30.53 ? 63   HIS K CB  1 
ATOM   10481 C  CG  . HIS J  1 63  ? 31.898 20.956  -88.925  1.00 30.35 ? 63   HIS K CG  1 
ATOM   10482 N  ND1 . HIS J  1 63  ? 32.065 20.501  -90.216  1.00 31.38 ? 63   HIS K ND1 1 
ATOM   10483 C  CD2 . HIS J  1 63  ? 30.651 21.485  -88.873  1.00 30.93 ? 63   HIS K CD2 1 
ATOM   10484 C  CE1 . HIS J  1 63  ? 30.975 20.756  -90.918  1.00 31.20 ? 63   HIS K CE1 1 
ATOM   10485 N  NE2 . HIS J  1 63  ? 30.101 21.352  -90.128  1.00 31.88 ? 63   HIS K NE2 1 
ATOM   10486 N  N   . PHE J  1 64  ? 33.716 19.379  -85.038  1.00 30.42 ? 64   PHE K N   1 
ATOM   10487 C  CA  . PHE J  1 64  ? 34.787 18.991  -84.108  1.00 30.86 ? 64   PHE K CA  1 
ATOM   10488 C  C   . PHE J  1 64  ? 36.148 19.206  -84.782  1.00 31.50 ? 64   PHE K C   1 
ATOM   10489 O  O   . PHE J  1 64  ? 36.512 18.508  -85.741  1.00 31.09 ? 64   PHE K O   1 
ATOM   10490 C  CB  . PHE J  1 64  ? 34.585 17.547  -83.598  1.00 30.32 ? 64   PHE K CB  1 
ATOM   10491 C  CG  . PHE J  1 64  ? 35.625 17.084  -82.595  1.00 29.65 ? 64   PHE K CG  1 
ATOM   10492 C  CD1 . PHE J  1 64  ? 36.101 15.776  -82.637  1.00 27.58 ? 64   PHE K CD1 1 
ATOM   10493 C  CD2 . PHE J  1 64  ? 36.127 17.947  -81.622  1.00 27.68 ? 64   PHE K CD2 1 
ATOM   10494 C  CE1 . PHE J  1 64  ? 37.056 15.330  -81.721  1.00 28.20 ? 64   PHE K CE1 1 
ATOM   10495 C  CE2 . PHE J  1 64  ? 37.090 17.513  -80.700  1.00 28.90 ? 64   PHE K CE2 1 
ATOM   10496 C  CZ  . PHE J  1 64  ? 37.554 16.203  -80.749  1.00 27.04 ? 64   PHE K CZ  1 
ATOM   10497 N  N   . ASN J  1 65  ? 36.872 20.206  -84.278  1.00 32.25 ? 65   ASN K N   1 
ATOM   10498 C  CA  . ASN J  1 65  ? 38.079 20.709  -84.927  1.00 33.45 ? 65   ASN K CA  1 
ATOM   10499 C  C   . ASN J  1 65  ? 39.218 20.941  -83.931  1.00 33.80 ? 65   ASN K C   1 
ATOM   10500 O  O   . ASN J  1 65  ? 39.641 22.079  -83.737  1.00 34.09 ? 65   ASN K O   1 
ATOM   10501 C  CB  . ASN J  1 65  ? 37.751 22.018  -85.662  1.00 33.34 ? 65   ASN K CB  1 
ATOM   10502 C  CG  . ASN J  1 65  ? 38.896 22.514  -86.553  1.00 34.83 ? 65   ASN K CG  1 
ATOM   10503 O  OD1 . ASN J  1 65  ? 39.795 21.755  -86.931  1.00 34.72 ? 65   ASN K OD1 1 
ATOM   10504 N  ND2 . ASN J  1 65  ? 38.851 23.799  -86.902  1.00 34.43 ? 65   ASN K ND2 1 
ATOM   10505 N  N   . PRO J  1 66  ? 39.717 19.868  -83.288  1.00 34.49 ? 66   PRO K N   1 
ATOM   10506 C  CA  . PRO J  1 66  ? 40.755 20.086  -82.269  1.00 34.90 ? 66   PRO K CA  1 
ATOM   10507 C  C   . PRO J  1 66  ? 42.106 20.538  -82.830  1.00 35.52 ? 66   PRO K C   1 
ATOM   10508 O  O   . PRO J  1 66  ? 42.860 21.229  -82.136  1.00 35.55 ? 66   PRO K O   1 
ATOM   10509 C  CB  . PRO J  1 66  ? 40.899 18.714  -81.602  1.00 34.60 ? 66   PRO K CB  1 
ATOM   10510 C  CG  . PRO J  1 66  ? 40.391 17.738  -82.587  1.00 34.40 ? 66   PRO K CG  1 
ATOM   10511 C  CD  . PRO J  1 66  ? 39.361 18.442  -83.421  1.00 34.43 ? 66   PRO K CD  1 
ATOM   10512 N  N   . LEU J  1 67  ? 42.407 20.151  -84.066  1.00 36.03 ? 67   LEU K N   1 
ATOM   10513 C  CA  . LEU J  1 67  ? 43.681 20.503  -84.689  1.00 36.64 ? 67   LEU K CA  1 
ATOM   10514 C  C   . LEU J  1 67  ? 43.617 21.802  -85.496  1.00 36.81 ? 67   LEU K C   1 
ATOM   10515 O  O   . LEU J  1 67  ? 44.548 22.128  -86.230  1.00 37.05 ? 67   LEU K O   1 
ATOM   10516 C  CB  . LEU J  1 67  ? 44.204 19.342  -85.539  1.00 36.64 ? 67   LEU K CB  1 
ATOM   10517 C  CG  . LEU J  1 67  ? 44.559 18.069  -84.766  1.00 37.22 ? 67   LEU K CG  1 
ATOM   10518 C  CD1 . LEU J  1 67  ? 44.771 16.889  -85.709  1.00 37.46 ? 67   LEU K CD1 1 
ATOM   10519 C  CD2 . LEU J  1 67  ? 45.787 18.282  -83.862  1.00 37.89 ? 67   LEU K CD2 1 
ATOM   10520 N  N   . SER J  1 68  ? 42.506 22.523  -85.348  1.00 37.06 ? 68   SER K N   1 
ATOM   10521 C  CA  . SER J  1 68  ? 42.312 23.874  -85.896  1.00 37.21 ? 68   SER K CA  1 
ATOM   10522 C  C   . SER J  1 68  ? 42.586 24.009  -87.402  1.00 37.49 ? 68   SER K C   1 
ATOM   10523 O  O   . SER J  1 68  ? 43.231 24.966  -87.842  1.00 37.35 ? 68   SER K O   1 
ATOM   10524 C  CB  . SER J  1 68  ? 43.117 24.903  -85.089  1.00 37.23 ? 68   SER K CB  1 
ATOM   10525 O  OG  . SER J  1 68  ? 42.723 24.882  -83.727  1.00 37.02 ? 68   SER K OG  1 
ATOM   10526 N  N   . ARG J  1 69  ? 42.085 23.040  -88.169  1.00 37.43 ? 69   ARG K N   1 
ATOM   10527 C  CA  . ARG J  1 69  ? 42.245 23.006  -89.620  1.00 37.41 ? 69   ARG K CA  1 
ATOM   10528 C  C   . ARG J  1 69  ? 40.946 23.397  -90.330  1.00 37.09 ? 69   ARG K C   1 
ATOM   10529 O  O   . ARG J  1 69  ? 39.927 23.640  -89.680  1.00 37.12 ? 69   ARG K O   1 
ATOM   10530 C  CB  . ARG J  1 69  ? 42.741 21.627  -90.062  1.00 37.50 ? 69   ARG K CB  1 
ATOM   10531 C  CG  . ARG J  1 69  ? 44.205 21.398  -89.700  1.00 38.47 ? 69   ARG K CG  1 
ATOM   10532 C  CD  . ARG J  1 69  ? 44.628 19.942  -89.808  1.00 39.66 ? 69   ARG K CD  1 
ATOM   10533 N  NE  . ARG J  1 69  ? 46.002 19.773  -89.336  1.00 39.99 ? 69   ARG K NE  1 
ATOM   10534 C  CZ  . ARG J  1 69  ? 46.566 18.609  -89.022  1.00 40.91 ? 69   ARG K CZ  1 
ATOM   10535 N  NH1 . ARG J  1 69  ? 47.822 18.579  -88.596  1.00 41.18 ? 69   ARG K NH1 1 
ATOM   10536 N  NH2 . ARG J  1 69  ? 45.885 17.474  -89.128  1.00 41.64 ? 69   ARG K NH2 1 
ATOM   10537 N  N   . LYS J  1 70  ? 40.985 23.472  -91.659  1.00 36.60 ? 70   LYS K N   1 
ATOM   10538 C  CA  . LYS J  1 70  ? 39.832 23.937  -92.433  1.00 36.37 ? 70   LYS K CA  1 
ATOM   10539 C  C   . LYS J  1 70  ? 38.948 22.771  -92.853  1.00 35.76 ? 70   LYS K C   1 
ATOM   10540 O  O   . LYS J  1 70  ? 39.416 21.636  -92.924  1.00 35.75 ? 70   LYS K O   1 
ATOM   10541 C  CB  . LYS J  1 70  ? 40.299 24.741  -93.655  1.00 36.73 ? 70   LYS K CB  1 
ATOM   10542 C  CG  . LYS J  1 70  ? 40.796 26.157  -93.322  1.00 37.47 ? 70   LYS K CG  1 
ATOM   10543 C  CD  . LYS J  1 70  ? 42.081 26.515  -94.075  1.00 38.88 ? 70   LYS K CD  1 
ATOM   10544 C  CE  . LYS J  1 70  ? 41.901 26.542  -95.592  1.00 38.72 ? 70   LYS K CE  1 
ATOM   10545 N  NZ  . LYS J  1 70  ? 43.203 26.338  -96.298  1.00 39.42 ? 70   LYS K NZ  1 
ATOM   10546 N  N   . HIS J  1 71  ? 37.674 23.054  -93.123  1.00 35.27 ? 71   HIS K N   1 
ATOM   10547 C  CA  . HIS J  1 71  ? 36.718 22.020  -93.535  1.00 35.07 ? 71   HIS K CA  1 
ATOM   10548 C  C   . HIS J  1 71  ? 37.168 21.260  -94.782  1.00 35.06 ? 71   HIS K C   1 
ATOM   10549 O  O   . HIS J  1 71  ? 37.607 21.857  -95.768  1.00 34.94 ? 71   HIS K O   1 
ATOM   10550 C  CB  . HIS J  1 71  ? 35.321 22.611  -93.763  1.00 34.93 ? 71   HIS K CB  1 
ATOM   10551 C  CG  . HIS J  1 71  ? 34.283 21.586  -94.097  1.00 35.02 ? 71   HIS K CG  1 
ATOM   10552 N  ND1 . HIS J  1 71  ? 33.670 20.809  -93.136  1.00 34.12 ? 71   HIS K ND1 1 
ATOM   10553 C  CD2 . HIS J  1 71  ? 33.761 21.197  -95.284  1.00 34.48 ? 71   HIS K CD2 1 
ATOM   10554 C  CE1 . HIS J  1 71  ? 32.806 19.995  -93.717  1.00 33.95 ? 71   HIS K CE1 1 
ATOM   10555 N  NE2 . HIS J  1 71  ? 32.843 20.208  -95.020  1.00 33.69 ? 71   HIS K NE2 1 
ATOM   10556 N  N   . GLY J  1 72  ? 37.056 19.936  -94.719  1.00 34.81 ? 72   GLY K N   1 
ATOM   10557 C  CA  . GLY J  1 72  ? 37.437 19.077  -95.825  1.00 34.75 ? 72   GLY K CA  1 
ATOM   10558 C  C   . GLY J  1 72  ? 36.478 17.915  -95.939  1.00 34.92 ? 72   GLY K C   1 
ATOM   10559 O  O   . GLY J  1 72  ? 35.485 17.832  -95.204  1.00 34.42 ? 72   GLY K O   1 
ATOM   10560 N  N   . GLY J  1 73  ? 36.762 17.031  -96.886  1.00 34.86 ? 73   GLY K N   1 
ATOM   10561 C  CA  . GLY J  1 73  ? 36.057 15.767  -96.975  1.00 35.19 ? 73   GLY K CA  1 
ATOM   10562 C  C   . GLY J  1 73  ? 36.843 14.759  -96.163  1.00 35.51 ? 73   GLY K C   1 
ATOM   10563 O  O   . GLY J  1 73  ? 37.981 15.047  -95.776  1.00 35.24 ? 73   GLY K O   1 
ATOM   10564 N  N   . PRO J  1 74  ? 36.253 13.572  -95.901  1.00 35.94 ? 74   PRO K N   1 
ATOM   10565 C  CA  . PRO J  1 74  ? 36.934 12.519  -95.142  1.00 36.60 ? 74   PRO K CA  1 
ATOM   10566 C  C   . PRO J  1 74  ? 38.350 12.223  -95.653  1.00 37.22 ? 74   PRO K C   1 
ATOM   10567 O  O   . PRO J  1 74  ? 39.284 12.130  -94.856  1.00 37.18 ? 74   PRO K O   1 
ATOM   10568 C  CB  . PRO J  1 74  ? 36.034 11.284  -95.349  1.00 36.72 ? 74   PRO K CB  1 
ATOM   10569 C  CG  . PRO J  1 74  ? 35.045 11.661  -96.409  1.00 36.18 ? 74   PRO K CG  1 
ATOM   10570 C  CD  . PRO J  1 74  ? 34.911 13.145  -96.330  1.00 35.90 ? 74   PRO K CD  1 
ATOM   10571 N  N   . LYS J  1 75  ? 38.501 12.103  -96.974  1.00 37.81 ? 75   LYS K N   1 
ATOM   10572 C  CA  . LYS J  1 75  ? 39.774 11.687  -97.587  1.00 38.23 ? 75   LYS K CA  1 
ATOM   10573 C  C   . LYS J  1 75  ? 40.810 12.807  -97.758  1.00 38.23 ? 75   LYS K C   1 
ATOM   10574 O  O   . LYS J  1 75  ? 41.942 12.541  -98.172  1.00 38.14 ? 75   LYS K O   1 
ATOM   10575 C  CB  . LYS J  1 75  ? 39.516 10.996  -98.930  1.00 38.54 ? 75   LYS K CB  1 
ATOM   10576 C  CG  . LYS J  1 75  ? 39.019 9.556   -98.822  1.00 40.01 ? 75   LYS K CG  1 
ATOM   10577 C  CD  . LYS J  1 75  ? 40.176 8.563   -98.829  1.00 42.35 ? 75   LYS K CD  1 
ATOM   10578 C  CE  . LYS J  1 75  ? 39.780 7.262   -99.523  1.00 43.58 ? 75   LYS K CE  1 
ATOM   10579 N  NZ  . LYS J  1 75  ? 40.974 6.452   -99.907  1.00 44.11 ? 75   LYS K NZ  1 
ATOM   10580 N  N   . ASP J  1 76  ? 40.428 14.045  -97.445  1.00 38.21 ? 76   ASP K N   1 
ATOM   10581 C  CA  . ASP J  1 76  ? 41.353 15.180  -97.501  1.00 38.28 ? 76   ASP K CA  1 
ATOM   10582 C  C   . ASP J  1 76  ? 42.353 15.147  -96.357  1.00 38.31 ? 76   ASP K C   1 
ATOM   10583 O  O   . ASP J  1 76  ? 42.013 14.746  -95.238  1.00 38.09 ? 76   ASP K O   1 
ATOM   10584 C  CB  . ASP J  1 76  ? 40.590 16.505  -97.456  1.00 38.27 ? 76   ASP K CB  1 
ATOM   10585 C  CG  . ASP J  1 76  ? 39.989 16.877  -98.788  1.00 38.65 ? 76   ASP K CG  1 
ATOM   10586 O  OD1 . ASP J  1 76  ? 38.761 17.092  -98.843  1.00 38.22 ? 76   ASP K OD1 1 
ATOM   10587 O  OD2 . ASP J  1 76  ? 40.744 16.947  -99.782  1.00 39.43 ? 76   ASP K OD2 1 
ATOM   10588 N  N   . GLU J  1 77  ? 43.581 15.581  -96.640  1.00 38.27 ? 77   GLU K N   1 
ATOM   10589 C  CA  . GLU J  1 77  ? 44.602 15.733  -95.603  1.00 38.21 ? 77   GLU K CA  1 
ATOM   10590 C  C   . GLU J  1 77  ? 44.283 16.933  -94.716  1.00 37.64 ? 77   GLU K C   1 
ATOM   10591 O  O   . GLU J  1 77  ? 44.657 16.968  -93.539  1.00 37.87 ? 77   GLU K O   1 
ATOM   10592 C  CB  . GLU J  1 77  ? 45.995 15.881  -96.222  1.00 38.44 ? 77   GLU K CB  1 
ATOM   10593 C  CG  . GLU J  1 77  ? 47.123 15.902  -95.188  1.00 39.83 ? 77   GLU K CG  1 
ATOM   10594 C  CD  . GLU J  1 77  ? 48.466 15.516  -95.773  1.00 41.19 ? 77   GLU K CD  1 
ATOM   10595 O  OE1 . GLU J  1 77  ? 49.102 16.375  -96.429  1.00 42.30 ? 77   GLU K OE1 1 
ATOM   10596 O  OE2 . GLU J  1 77  ? 48.887 14.354  -95.568  1.00 40.91 ? 77   GLU K OE2 1 
ATOM   10597 N  N   . GLU J  1 78  ? 43.586 17.904  -95.302  1.00 36.91 ? 78   GLU K N   1 
ATOM   10598 C  CA  . GLU J  1 78  ? 43.193 19.136  -94.630  1.00 36.07 ? 78   GLU K CA  1 
ATOM   10599 C  C   . GLU J  1 78  ? 41.690 19.111  -94.338  1.00 35.28 ? 78   GLU K C   1 
ATOM   10600 O  O   . GLU J  1 78  ? 40.863 19.426  -95.197  1.00 35.04 ? 78   GLU K O   1 
ATOM   10601 C  CB  . GLU J  1 78  ? 43.579 20.343  -95.496  1.00 36.44 ? 78   GLU K CB  1 
ATOM   10602 C  CG  . GLU J  1 78  ? 43.089 21.703  -94.995  1.00 36.82 ? 78   GLU K CG  1 
ATOM   10603 C  CD  . GLU J  1 78  ? 43.762 22.148  -93.719  1.00 37.72 ? 78   GLU K CD  1 
ATOM   10604 O  OE1 . GLU J  1 78  ? 43.171 22.999  -93.023  1.00 38.98 ? 78   GLU K OE1 1 
ATOM   10605 O  OE2 . GLU J  1 78  ? 44.872 21.658  -93.411  1.00 37.83 ? 78   GLU K OE2 1 
ATOM   10606 N  N   . ARG J  1 79  ? 41.353 18.714  -93.113  1.00 34.25 ? 79   ARG K N   1 
ATOM   10607 C  CA  . ARG J  1 79  ? 39.968 18.558  -92.695  1.00 33.00 ? 79   ARG K CA  1 
ATOM   10608 C  C   . ARG J  1 79  ? 39.818 18.746  -91.181  1.00 32.31 ? 79   ARG K C   1 
ATOM   10609 O  O   . ARG J  1 79  ? 40.805 18.699  -90.441  1.00 31.94 ? 79   ARG K O   1 
ATOM   10610 C  CB  . ARG J  1 79  ? 39.457 17.166  -93.087  1.00 33.02 ? 79   ARG K CB  1 
ATOM   10611 C  CG  . ARG J  1 79  ? 40.268 16.010  -92.501  1.00 32.37 ? 79   ARG K CG  1 
ATOM   10612 C  CD  . ARG J  1 79  ? 39.552 14.680  -92.684  1.00 32.81 ? 79   ARG K CD  1 
ATOM   10613 N  NE  . ARG J  1 79  ? 38.634 14.359  -91.586  1.00 31.62 ? 79   ARG K NE  1 
ATOM   10614 C  CZ  . ARG J  1 79  ? 38.188 13.132  -91.318  1.00 32.49 ? 79   ARG K CZ  1 
ATOM   10615 N  NH1 . ARG J  1 79  ? 37.353 12.923  -90.297  1.00 31.28 ? 79   ARG K NH1 1 
ATOM   10616 N  NH2 . ARG J  1 79  ? 38.582 12.097  -92.058  1.00 31.18 ? 79   ARG K NH2 1 
ATOM   10617 N  N   . HIS J  1 80  ? 38.578 18.957  -90.735  1.00 31.58 ? 80   HIS K N   1 
ATOM   10618 C  CA  . HIS J  1 80  ? 38.234 18.833  -89.310  1.00 30.85 ? 80   HIS K CA  1 
ATOM   10619 C  C   . HIS J  1 80  ? 38.184 17.339  -88.940  1.00 30.37 ? 80   HIS K C   1 
ATOM   10620 O  O   . HIS J  1 80  ? 37.959 16.485  -89.815  1.00 30.34 ? 80   HIS K O   1 
ATOM   10621 C  CB  . HIS J  1 80  ? 36.867 19.466  -89.015  1.00 31.00 ? 80   HIS K CB  1 
ATOM   10622 C  CG  . HIS J  1 80  ? 36.734 20.894  -89.456  1.00 30.40 ? 80   HIS K CG  1 
ATOM   10623 N  ND1 . HIS J  1 80  ? 35.650 21.356  -90.174  1.00 29.65 ? 80   HIS K ND1 1 
ATOM   10624 C  CD2 . HIS J  1 80  ? 37.534 21.967  -89.260  1.00 29.95 ? 80   HIS K CD2 1 
ATOM   10625 C  CE1 . HIS J  1 80  ? 35.786 22.651  -90.393  1.00 29.65 ? 80   HIS K CE1 1 
ATOM   10626 N  NE2 . HIS J  1 80  ? 36.929 23.043  -89.860  1.00 28.91 ? 80   HIS K NE2 1 
ATOM   10627 N  N   . VAL J  1 81  ? 38.372 17.017  -87.657  1.00 29.34 ? 81   VAL K N   1 
ATOM   10628 C  CA  . VAL J  1 81  ? 38.247 15.624  -87.219  1.00 28.29 ? 81   VAL K CA  1 
ATOM   10629 C  C   . VAL J  1 81  ? 36.816 15.127  -87.424  1.00 27.68 ? 81   VAL K C   1 
ATOM   10630 O  O   . VAL J  1 81  ? 36.599 13.976  -87.798  1.00 27.37 ? 81   VAL K O   1 
ATOM   10631 C  CB  . VAL J  1 81  ? 38.737 15.398  -85.754  1.00 28.61 ? 81   VAL K CB  1 
ATOM   10632 C  CG1 . VAL J  1 81  ? 38.503 13.953  -85.309  1.00 27.71 ? 81   VAL K CG1 1 
ATOM   10633 C  CG2 . VAL J  1 81  ? 40.223 15.723  -85.641  1.00 28.87 ? 81   VAL K CG2 1 
ATOM   10634 N  N   . GLY J  1 82  ? 35.844 16.008  -87.211  1.00 27.22 ? 82   GLY K N   1 
ATOM   10635 C  CA  . GLY J  1 82  ? 34.442 15.655  -87.382  1.00 26.86 ? 82   GLY K CA  1 
ATOM   10636 C  C   . GLY J  1 82  ? 33.939 15.545  -88.819  1.00 26.69 ? 82   GLY K C   1 
ATOM   10637 O  O   . GLY J  1 82  ? 32.746 15.322  -89.040  1.00 26.50 ? 82   GLY K O   1 
ATOM   10638 N  N   . ASP J  1 83  ? 34.835 15.669  -89.796  1.00 26.56 ? 83   ASP K N   1 
ATOM   10639 C  CA  . ASP J  1 83  ? 34.423 15.674  -91.218  1.00 25.99 ? 83   ASP K CA  1 
ATOM   10640 C  C   . ASP J  1 83  ? 34.221 14.271  -91.806  1.00 25.96 ? 83   ASP K C   1 
ATOM   10641 O  O   . ASP J  1 83  ? 35.176 13.629  -92.244  1.00 26.38 ? 83   ASP K O   1 
ATOM   10642 C  CB  . ASP J  1 83  ? 35.430 16.457  -92.049  1.00 26.02 ? 83   ASP K CB  1 
ATOM   10643 C  CG  . ASP J  1 83  ? 35.355 17.954  -91.807  1.00 26.59 ? 83   ASP K CG  1 
ATOM   10644 O  OD1 . ASP J  1 83  ? 34.321 18.456  -91.314  1.00 26.31 ? 83   ASP K OD1 1 
ATOM   10645 O  OD2 . ASP J  1 83  ? 36.340 18.641  -92.127  1.00 28.04 ? 83   ASP K OD2 1 
ATOM   10646 N  N   . LEU J  1 84  ? 32.982 13.792  -91.816  1.00 25.80 ? 84   LEU K N   1 
ATOM   10647 C  CA  . LEU J  1 84  ? 32.700 12.473  -92.365  1.00 25.79 ? 84   LEU K CA  1 
ATOM   10648 C  C   . LEU J  1 84  ? 32.037 12.529  -93.752  1.00 26.09 ? 84   LEU K C   1 
ATOM   10649 O  O   . LEU J  1 84  ? 31.578 11.505  -94.256  1.00 26.09 ? 84   LEU K O   1 
ATOM   10650 C  CB  . LEU J  1 84  ? 31.892 11.614  -91.376  1.00 25.56 ? 84   LEU K CB  1 
ATOM   10651 C  CG  . LEU J  1 84  ? 32.605 11.162  -90.085  1.00 26.03 ? 84   LEU K CG  1 
ATOM   10652 C  CD1 . LEU J  1 84  ? 31.691 10.265  -89.251  1.00 25.46 ? 84   LEU K CD1 1 
ATOM   10653 C  CD2 . LEU J  1 84  ? 33.929 10.444  -90.385  1.00 23.99 ? 84   LEU K CD2 1 
ATOM   10654 N  N   . GLY J  1 85  ? 31.986 13.730  -94.341  1.00 26.53 ? 85   GLY K N   1 
ATOM   10655 C  CA  . GLY J  1 85  ? 31.538 13.939  -95.730  1.00 26.63 ? 85   GLY K CA  1 
ATOM   10656 C  C   . GLY J  1 85  ? 30.040 13.918  -95.947  1.00 26.95 ? 85   GLY K C   1 
ATOM   10657 O  O   . GLY J  1 85  ? 29.309 14.728  -95.363  1.00 27.41 ? 85   GLY K O   1 
ATOM   10658 N  N   . ASN J  1 86  ? 29.591 12.991  -96.794  1.00 26.75 ? 86   ASN K N   1 
ATOM   10659 C  CA  . ASN J  1 86  ? 28.185 12.862  -97.161  1.00 26.62 ? 86   ASN K CA  1 
ATOM   10660 C  C   . ASN J  1 86  ? 27.649 11.447  -97.019  1.00 26.41 ? 86   ASN K C   1 
ATOM   10661 O  O   . ASN J  1 86  ? 28.351 10.471  -97.285  1.00 25.79 ? 86   ASN K O   1 
ATOM   10662 C  CB  . ASN J  1 86  ? 27.959 13.330  -98.611  1.00 26.69 ? 86   ASN K CB  1 
ATOM   10663 C  CG  . ASN J  1 86  ? 28.120 14.821  -98.765  1.00 27.28 ? 86   ASN K CG  1 
ATOM   10664 O  OD1 . ASN J  1 86  ? 27.287 15.594  -98.298  1.00 28.26 ? 86   ASN K OD1 1 
ATOM   10665 N  ND2 . ASN J  1 86  ? 29.192 15.236  -99.428  1.00 29.05 ? 86   ASN K ND2 1 
ATOM   10666 N  N   . VAL J  1 87  ? 26.396 11.349  -96.593  1.00 26.54 ? 87   VAL K N   1 
ATOM   10667 C  CA  . VAL J  1 87  ? 25.652 10.104  -96.722  1.00 26.88 ? 87   VAL K CA  1 
ATOM   10668 C  C   . VAL J  1 87  ? 24.670 10.279  -97.881  1.00 26.94 ? 87   VAL K C   1 
ATOM   10669 O  O   . VAL J  1 87  ? 24.308 11.409  -98.221  1.00 27.04 ? 87   VAL K O   1 
ATOM   10670 C  CB  . VAL J  1 87  ? 24.921 9.701   -95.414  1.00 26.76 ? 87   VAL K CB  1 
ATOM   10671 C  CG1 . VAL J  1 87  ? 25.930 9.253   -94.354  1.00 27.23 ? 87   VAL K CG1 1 
ATOM   10672 C  CG2 . VAL J  1 87  ? 24.038 10.835  -94.883  1.00 26.83 ? 87   VAL K CG2 1 
ATOM   10673 N  N   . THR J  1 88  ? 24.251 9.172   -98.490  1.00 27.16 ? 88   THR K N   1 
ATOM   10674 C  CA  . THR J  1 88  ? 23.310 9.237   -99.613  1.00 26.71 ? 88   THR K CA  1 
ATOM   10675 C  C   . THR J  1 88  ? 22.012 8.501   -99.325  1.00 26.85 ? 88   THR K C   1 
ATOM   10676 O  O   . THR J  1 88  ? 22.013 7.303   -98.990  1.00 26.58 ? 88   THR K O   1 
ATOM   10677 C  CB  . THR J  1 88  ? 23.943 8.731   -100.926 1.00 26.84 ? 88   THR K CB  1 
ATOM   10678 O  OG1 . THR J  1 88  ? 25.217 9.352   -101.100 1.00 26.00 ? 88   THR K OG1 1 
ATOM   10679 C  CG2 . THR J  1 88  ? 23.057 9.086   -102.130 1.00 26.87 ? 88   THR K CG2 1 
ATOM   10680 N  N   . ALA J  1 89  ? 20.909 9.236   -99.461  1.00 27.08 ? 89   ALA K N   1 
ATOM   10681 C  CA  . ALA J  1 89  ? 19.567 8.694   -99.288  1.00 27.50 ? 89   ALA K CA  1 
ATOM   10682 C  C   . ALA J  1 89  ? 18.964 8.329   -100.650 1.00 27.92 ? 89   ALA K C   1 
ATOM   10683 O  O   . ALA J  1 89  ? 19.065 9.101   -101.616 1.00 27.46 ? 89   ALA K O   1 
ATOM   10684 C  CB  . ALA J  1 89  ? 18.685 9.708   -98.566  1.00 27.45 ? 89   ALA K CB  1 
ATOM   10685 N  N   . ASP J  1 90  ? 18.343 7.150   -100.716 1.00 28.29 ? 90   ASP K N   1 
ATOM   10686 C  CA  . ASP J  1 90  ? 17.697 6.684   -101.941 1.00 29.05 ? 90   ASP K CA  1 
ATOM   10687 C  C   . ASP J  1 90  ? 16.334 7.366   -102.150 1.00 29.40 ? 90   ASP K C   1 
ATOM   10688 O  O   . ASP J  1 90  ? 15.975 8.287   -101.405 1.00 29.41 ? 90   ASP K O   1 
ATOM   10689 C  CB  . ASP J  1 90  ? 17.590 5.153   -101.937 1.00 29.07 ? 90   ASP K CB  1 
ATOM   10690 C  CG  . ASP J  1 90  ? 16.699 4.621   -100.825 1.00 28.77 ? 90   ASP K CG  1 
ATOM   10691 O  OD1 . ASP J  1 90  ? 16.798 3.412   -100.525 1.00 27.07 ? 90   ASP K OD1 1 
ATOM   10692 O  OD2 . ASP J  1 90  ? 15.889 5.391   -100.260 1.00 30.22 ? 90   ASP K OD2 1 
ATOM   10693 N  N   . LYS J  1 91  ? 15.580 6.925   -103.159 1.00 29.88 ? 91   LYS K N   1 
ATOM   10694 C  CA  . LYS J  1 91  ? 14.325 7.601   -103.523 1.00 30.32 ? 91   LYS K CA  1 
ATOM   10695 C  C   . LYS J  1 91  ? 13.273 7.540   -102.421 1.00 30.31 ? 91   LYS K C   1 
ATOM   10696 O  O   . LYS J  1 91  ? 12.362 8.373   -102.381 1.00 30.67 ? 91   LYS K O   1 
ATOM   10697 C  CB  . LYS J  1 91  ? 13.744 7.057   -104.844 1.00 30.31 ? 91   LYS K CB  1 
ATOM   10698 C  CG  . LYS J  1 91  ? 13.152 5.652   -104.753 1.00 30.84 ? 91   LYS K CG  1 
ATOM   10699 C  CD  . LYS J  1 91  ? 12.407 5.269   -106.029 1.00 31.86 ? 91   LYS K CD  1 
ATOM   10700 C  CE  . LYS J  1 91  ? 12.172 3.766   -106.115 1.00 32.42 ? 91   LYS K CE  1 
ATOM   10701 N  NZ  . LYS J  1 91  ? 11.156 3.274   -105.139 1.00 33.74 ? 91   LYS K NZ  1 
ATOM   10702 N  N   . ASP J  1 92  ? 13.403 6.544   -101.546 1.00 30.44 ? 92   ASP K N   1 
ATOM   10703 C  CA  . ASP J  1 92  ? 12.516 6.372   -100.398 1.00 30.45 ? 92   ASP K CA  1 
ATOM   10704 C  C   . ASP J  1 92  ? 13.063 7.077   -99.155  1.00 30.13 ? 92   ASP K C   1 
ATOM   10705 O  O   . ASP J  1 92  ? 12.561 6.864   -98.057  1.00 29.86 ? 92   ASP K O   1 
ATOM   10706 C  CB  . ASP J  1 92  ? 12.301 4.883   -100.097 1.00 30.58 ? 92   ASP K CB  1 
ATOM   10707 C  CG  . ASP J  1 92  ? 11.533 4.163   -101.195 1.00 32.37 ? 92   ASP K CG  1 
ATOM   10708 O  OD1 . ASP J  1 92  ? 12.116 3.264   -101.841 1.00 33.94 ? 92   ASP K OD1 1 
ATOM   10709 O  OD2 . ASP J  1 92  ? 10.346 4.489   -101.409 1.00 32.93 ? 92   ASP K OD2 1 
ATOM   10710 N  N   . GLY J  1 93  ? 14.094 7.899   -99.335  1.00 29.85 ? 93   GLY K N   1 
ATOM   10711 C  CA  . GLY J  1 93  ? 14.617 8.736   -98.263  1.00 29.91 ? 93   GLY K CA  1 
ATOM   10712 C  C   . GLY J  1 93  ? 15.458 8.027   -97.213  1.00 30.05 ? 93   GLY K C   1 
ATOM   10713 O  O   . GLY J  1 93  ? 15.776 8.617   -96.173  1.00 29.70 ? 93   GLY K O   1 
ATOM   10714 N  N   . VAL J  1 94  ? 15.803 6.763   -97.476  1.00 29.99 ? 94   VAL K N   1 
ATOM   10715 C  CA  . VAL J  1 94  ? 16.649 5.961   -96.577  1.00 29.86 ? 94   VAL K CA  1 
ATOM   10716 C  C   . VAL J  1 94  ? 18.122 6.034   -96.994  1.00 30.09 ? 94   VAL K C   1 
ATOM   10717 O  O   . VAL J  1 94  ? 18.471 5.754   -98.151  1.00 29.97 ? 94   VAL K O   1 
ATOM   10718 C  CB  . VAL J  1 94  ? 16.216 4.465   -96.531  1.00 29.86 ? 94   VAL K CB  1 
ATOM   10719 C  CG1 . VAL J  1 94  ? 17.147 3.652   -95.632  1.00 30.11 ? 94   VAL K CG1 1 
ATOM   10720 C  CG2 . VAL J  1 94  ? 14.772 4.318   -96.072  1.00 29.91 ? 94   VAL K CG2 1 
ATOM   10721 N  N   . ALA J  1 95  ? 18.981 6.410   -96.048  1.00 30.08 ? 95   ALA K N   1 
ATOM   10722 C  CA  . ALA J  1 95  ? 20.423 6.407   -96.266  1.00 30.13 ? 95   ALA K CA  1 
ATOM   10723 C  C   . ALA J  1 95  ? 21.070 5.212   -95.565  1.00 30.49 ? 95   ALA K C   1 
ATOM   10724 O  O   . ALA J  1 95  ? 20.954 5.054   -94.346  1.00 29.88 ? 95   ALA K O   1 
ATOM   10725 C  CB  . ALA J  1 95  ? 21.040 7.716   -95.794  1.00 30.13 ? 95   ALA K CB  1 
ATOM   10726 N  N   . ASP J  1 96  ? 21.726 4.364   -96.355  1.00 30.97 ? 96   ASP K N   1 
ATOM   10727 C  CA  . ASP J  1 96  ? 22.510 3.238   -95.849  1.00 31.53 ? 96   ASP K CA  1 
ATOM   10728 C  C   . ASP J  1 96  ? 23.936 3.740   -95.585  1.00 31.23 ? 96   ASP K C   1 
ATOM   10729 O  O   . ASP J  1 96  ? 24.700 3.993   -96.519  1.00 30.99 ? 96   ASP K O   1 
ATOM   10730 C  CB  . ASP J  1 96  ? 22.486 2.091   -96.874  1.00 32.33 ? 96   ASP K CB  1 
ATOM   10731 C  CG  . ASP J  1 96  ? 23.172 0.815   -96.380  1.00 34.29 ? 96   ASP K CG  1 
ATOM   10732 O  OD1 . ASP J  1 96  ? 22.902 -0.254  -96.973  1.00 36.41 ? 96   ASP K OD1 1 
ATOM   10733 O  OD2 . ASP J  1 96  ? 23.986 0.863   -95.429  1.00 37.05 ? 96   ASP K OD2 1 
ATOM   10734 N  N   . VAL J  1 97  ? 24.285 3.904   -94.307  1.00 30.80 ? 97   VAL K N   1 
ATOM   10735 C  CA  . VAL J  1 97  ? 25.591 4.441   -93.928  1.00 30.58 ? 97   VAL K CA  1 
ATOM   10736 C  C   . VAL J  1 97  ? 26.578 3.298   -93.717  1.00 30.69 ? 97   VAL K C   1 
ATOM   10737 O  O   . VAL J  1 97  ? 26.280 2.339   -93.004  1.00 30.50 ? 97   VAL K O   1 
ATOM   10738 C  CB  . VAL J  1 97  ? 25.519 5.323   -92.638  1.00 30.64 ? 97   VAL K CB  1 
ATOM   10739 C  CG1 . VAL J  1 97  ? 26.849 6.063   -92.408  1.00 30.36 ? 97   VAL K CG1 1 
ATOM   10740 C  CG2 . VAL J  1 97  ? 24.366 6.321   -92.724  1.00 29.86 ? 97   VAL K CG2 1 
ATOM   10741 N  N   . SER J  1 98  ? 27.739 3.393   -94.363  1.00 30.88 ? 98   SER K N   1 
ATOM   10742 C  CA  . SER J  1 98  ? 28.790 2.388   -94.227  1.00 31.22 ? 98   SER K CA  1 
ATOM   10743 C  C   . SER J  1 98  ? 30.137 3.004   -94.584  1.00 31.57 ? 98   SER K C   1 
ATOM   10744 O  O   . SER J  1 98  ? 30.451 3.182   -95.765  1.00 31.17 ? 98   SER K O   1 
ATOM   10745 C  CB  . SER J  1 98  ? 28.513 1.156   -95.100  1.00 31.45 ? 98   SER K CB  1 
ATOM   10746 O  OG  . SER J  1 98  ? 29.410 0.099   -94.781  1.00 31.80 ? 98   SER K OG  1 
ATOM   10747 N  N   . ILE J  1 99  ? 30.925 3.307   -93.549  1.00 31.66 ? 99   ILE K N   1 
ATOM   10748 C  CA  . ILE J  1 99  ? 32.162 4.087   -93.673  1.00 32.42 ? 99   ILE K CA  1 
ATOM   10749 C  C   . ILE J  1 99  ? 33.302 3.483   -92.835  1.00 32.67 ? 99   ILE K C   1 
ATOM   10750 O  O   . ILE J  1 99  ? 33.067 2.932   -91.757  1.00 32.74 ? 99   ILE K O   1 
ATOM   10751 C  CB  . ILE J  1 99  ? 31.944 5.556   -93.195  1.00 32.27 ? 99   ILE K CB  1 
ATOM   10752 C  CG1 . ILE J  1 99  ? 30.839 6.253   -94.003  1.00 33.21 ? 99   ILE K CG1 1 
ATOM   10753 C  CG2 . ILE J  1 99  ? 33.265 6.371   -93.213  1.00 33.21 ? 99   ILE K CG2 1 
ATOM   10754 C  CD1 . ILE J  1 99  ? 30.419 7.606   -93.414  1.00 33.38 ? 99   ILE K CD1 1 
ATOM   10755 N  N   . GLU J  1 100 ? 34.528 3.597   -93.342  1.00 32.88 ? 100  GLU K N   1 
ATOM   10756 C  CA  . GLU J  1 100 ? 35.742 3.357   -92.565  1.00 32.92 ? 100  GLU K CA  1 
ATOM   10757 C  C   . GLU J  1 100 ? 36.477 4.705   -92.497  1.00 32.35 ? 100  GLU K C   1 
ATOM   10758 O  O   . GLU J  1 100 ? 36.599 5.394   -93.509  1.00 32.14 ? 100  GLU K O   1 
ATOM   10759 C  CB  . GLU J  1 100 ? 36.609 2.295   -93.241  1.00 33.51 ? 100  GLU K CB  1 
ATOM   10760 C  CG  . GLU J  1 100 ? 37.750 1.722   -92.388  1.00 35.68 ? 100  GLU K CG  1 
ATOM   10761 C  CD  . GLU J  1 100 ? 37.479 0.296   -91.896  1.00 39.38 ? 100  GLU K CD  1 
ATOM   10762 O  OE1 . GLU J  1 100 ? 37.013 -0.546  -92.699  1.00 41.02 ? 100  GLU K OE1 1 
ATOM   10763 O  OE2 . GLU J  1 100 ? 37.746 0.009   -90.708  1.00 39.98 ? 100  GLU K OE2 1 
ATOM   10764 N  N   . ASP J  1 101 ? 36.935 5.092   -91.305  1.00 31.45 ? 101  ASP K N   1 
ATOM   10765 C  CA  . ASP J  1 101 ? 37.650 6.361   -91.135  1.00 30.69 ? 101  ASP K CA  1 
ATOM   10766 C  C   . ASP J  1 101 ? 38.800 6.231   -90.144  1.00 30.40 ? 101  ASP K C   1 
ATOM   10767 O  O   . ASP J  1 101 ? 38.685 5.519   -89.139  1.00 30.81 ? 101  ASP K O   1 
ATOM   10768 C  CB  . ASP J  1 101 ? 36.694 7.476   -90.697  1.00 30.79 ? 101  ASP K CB  1 
ATOM   10769 C  CG  . ASP J  1 101 ? 37.316 8.859   -90.804  1.00 30.45 ? 101  ASP K CG  1 
ATOM   10770 O  OD1 . ASP J  1 101 ? 37.801 9.391   -89.784  1.00 30.61 ? 101  ASP K OD1 1 
ATOM   10771 O  OD2 . ASP J  1 101 ? 37.327 9.423   -91.906  1.00 29.75 ? 101  ASP K OD2 1 
ATOM   10772 N  N   . SER J  1 102 ? 39.895 6.942   -90.427  1.00 29.65 ? 102  SER K N   1 
ATOM   10773 C  CA  . SER J  1 102 ? 41.135 6.831   -89.657  1.00 28.91 ? 102  SER K CA  1 
ATOM   10774 C  C   . SER J  1 102 ? 41.572 8.135   -88.978  1.00 27.94 ? 102  SER K C   1 
ATOM   10775 O  O   . SER J  1 102 ? 42.647 8.199   -88.370  1.00 27.73 ? 102  SER K O   1 
ATOM   10776 C  CB  . SER J  1 102 ? 42.257 6.296   -90.556  1.00 29.01 ? 102  SER K CB  1 
ATOM   10777 O  OG  . SER J  1 102 ? 42.003 4.950   -90.915  1.00 30.43 ? 102  SER K OG  1 
ATOM   10778 N  N   . VAL J  1 103 ? 40.740 9.168   -89.076  1.00 27.28 ? 103  VAL K N   1 
ATOM   10779 C  CA  . VAL J  1 103 ? 40.983 10.425  -88.359  1.00 26.35 ? 103  VAL K CA  1 
ATOM   10780 C  C   . VAL J  1 103 ? 40.206 10.464  -87.028  1.00 25.81 ? 103  VAL K C   1 
ATOM   10781 O  O   . VAL J  1 103 ? 40.741 10.909  -86.006  1.00 25.35 ? 103  VAL K O   1 
ATOM   10782 C  CB  . VAL J  1 103 ? 40.668 11.660  -89.217  1.00 26.37 ? 103  VAL K CB  1 
ATOM   10783 C  CG1 . VAL J  1 103 ? 40.981 12.927  -88.459  1.00 26.57 ? 103  VAL K CG1 1 
ATOM   10784 C  CG2 . VAL J  1 103 ? 41.486 11.630  -90.507  1.00 27.77 ? 103  VAL K CG2 1 
ATOM   10785 N  N   . ILE J  1 104 ? 38.959 9.985   -87.049  1.00 24.79 ? 104  ILE K N   1 
ATOM   10786 C  CA  . ILE J  1 104 ? 38.155 9.851   -85.821  1.00 23.45 ? 104  ILE K CA  1 
ATOM   10787 C  C   . ILE J  1 104 ? 38.628 8.672   -84.960  1.00 23.05 ? 104  ILE K C   1 
ATOM   10788 O  O   . ILE J  1 104 ? 39.150 7.670   -85.474  1.00 22.45 ? 104  ILE K O   1 
ATOM   10789 C  CB  . ILE J  1 104 ? 36.630 9.692   -86.095  1.00 23.14 ? 104  ILE K CB  1 
ATOM   10790 C  CG1 . ILE J  1 104 ? 36.347 8.432   -86.931  1.00 24.01 ? 104  ILE K CG1 1 
ATOM   10791 C  CG2 . ILE J  1 104 ? 36.041 10.979  -86.695  1.00 23.17 ? 104  ILE K CG2 1 
ATOM   10792 C  CD1 . ILE J  1 104 ? 34.899 8.012   -86.985  1.00 24.23 ? 104  ILE K CD1 1 
ATOM   10793 N  N   . SER J  1 105 ? 38.408 8.789   -83.648  1.00 21.61 ? 105  SER K N   1 
ATOM   10794 C  CA  . SER J  1 105 ? 38.821 7.759   -82.698  1.00 21.25 ? 105  SER K CA  1 
ATOM   10795 C  C   . SER J  1 105 ? 37.814 7.684   -81.557  1.00 20.73 ? 105  SER K C   1 
ATOM   10796 O  O   . SER J  1 105 ? 37.207 8.683   -81.181  1.00 19.79 ? 105  SER K O   1 
ATOM   10797 C  CB  . SER J  1 105 ? 40.229 8.045   -82.158  1.00 21.11 ? 105  SER K CB  1 
ATOM   10798 O  OG  . SER J  1 105 ? 40.705 6.958   -81.373  1.00 20.89 ? 105  SER K OG  1 
ATOM   10799 N  N   . LEU J  1 106 ? 37.627 6.481   -81.036  1.00 21.20 ? 106  LEU K N   1 
ATOM   10800 C  CA  . LEU J  1 106 ? 36.716 6.269   -79.916  1.00 21.64 ? 106  LEU K CA  1 
ATOM   10801 C  C   . LEU J  1 106 ? 37.425 6.333   -78.551  1.00 22.66 ? 106  LEU K C   1 
ATOM   10802 O  O   . LEU J  1 106 ? 36.806 6.129   -77.494  1.00 22.14 ? 106  LEU K O   1 
ATOM   10803 C  CB  . LEU J  1 106 ? 35.949 4.958   -80.097  1.00 21.64 ? 106  LEU K CB  1 
ATOM   10804 C  CG  . LEU J  1 106 ? 35.153 4.798   -81.400  1.00 19.55 ? 106  LEU K CG  1 
ATOM   10805 C  CD1 . LEU J  1 106 ? 34.416 3.473   -81.393  1.00 18.91 ? 106  LEU K CD1 1 
ATOM   10806 C  CD2 . LEU J  1 106 ? 34.182 5.958   -81.627  1.00 18.90 ? 106  LEU K CD2 1 
ATOM   10807 N  N   . SER J  1 107 ? 38.718 6.644   -78.580  1.00 23.48 ? 107  SER K N   1 
ATOM   10808 C  CA  . SER J  1 107 ? 39.513 6.789   -77.356  1.00 24.08 ? 107  SER K CA  1 
ATOM   10809 C  C   . SER J  1 107 ? 40.610 7.843   -77.528  1.00 25.03 ? 107  SER K C   1 
ATOM   10810 O  O   . SER J  1 107 ? 40.777 8.418   -78.615  1.00 24.82 ? 107  SER K O   1 
ATOM   10811 C  CB  . SER J  1 107 ? 40.109 5.443   -76.925  1.00 23.95 ? 107  SER K CB  1 
ATOM   10812 O  OG  . SER J  1 107 ? 41.034 4.956   -77.882  1.00 24.19 ? 107  SER K OG  1 
ATOM   10813 N  N   . GLY J  1 108 ? 41.334 8.110   -76.442  1.00 25.47 ? 108  GLY K N   1 
ATOM   10814 C  CA  . GLY J  1 108 ? 42.382 9.117   -76.435  1.00 26.57 ? 108  GLY K CA  1 
ATOM   10815 C  C   . GLY J  1 108 ? 41.852 10.524  -76.271  1.00 27.31 ? 108  GLY K C   1 
ATOM   10816 O  O   . GLY J  1 108 ? 40.645 10.762  -76.357  1.00 26.93 ? 108  GLY K O   1 
ATOM   10817 N  N   . ASP J  1 109 ? 42.772 11.460  -76.056  1.00 28.37 ? 109  ASP K N   1 
ATOM   10818 C  CA  . ASP J  1 109 ? 42.424 12.830  -75.673  1.00 29.98 ? 109  ASP K CA  1 
ATOM   10819 C  C   . ASP J  1 109 ? 41.554 13.609  -76.668  1.00 30.09 ? 109  ASP K C   1 
ATOM   10820 O  O   . ASP J  1 109 ? 41.000 14.656  -76.306  1.00 30.06 ? 109  ASP K O   1 
ATOM   10821 C  CB  . ASP J  1 109 ? 43.676 13.629  -75.250  1.00 30.83 ? 109  ASP K CB  1 
ATOM   10822 C  CG  . ASP J  1 109 ? 44.759 13.659  -76.322  1.00 33.71 ? 109  ASP K CG  1 
ATOM   10823 O  OD1 . ASP J  1 109 ? 45.834 13.046  -76.100  1.00 36.90 ? 109  ASP K OD1 1 
ATOM   10824 O  OD2 . ASP J  1 109 ? 44.542 14.295  -77.380  1.00 36.36 ? 109  ASP K OD2 1 
ATOM   10825 N  N   . HIS J  1 110 ? 41.432 13.098  -77.900  1.00 29.89 ? 110  HIS K N   1 
ATOM   10826 C  CA  . HIS J  1 110 ? 40.544 13.684  -78.925  1.00 29.58 ? 110  HIS K CA  1 
ATOM   10827 C  C   . HIS J  1 110 ? 39.432 12.734  -79.414  1.00 28.99 ? 110  HIS K C   1 
ATOM   10828 O  O   . HIS J  1 110 ? 38.934 12.880  -80.538  1.00 29.83 ? 110  HIS K O   1 
ATOM   10829 C  CB  . HIS J  1 110 ? 41.351 14.224  -80.124  1.00 29.96 ? 110  HIS K CB  1 
ATOM   10830 C  CG  . HIS J  1 110 ? 42.316 15.319  -79.768  1.00 31.05 ? 110  HIS K CG  1 
ATOM   10831 N  ND1 . HIS J  1 110 ? 43.590 15.386  -80.289  1.00 33.04 ? 110  HIS K ND1 1 
ATOM   10832 C  CD2 . HIS J  1 110 ? 42.194 16.384  -78.939  1.00 31.93 ? 110  HIS K CD2 1 
ATOM   10833 C  CE1 . HIS J  1 110 ? 44.209 16.447  -79.801  1.00 33.26 ? 110  HIS K CE1 1 
ATOM   10834 N  NE2 . HIS J  1 110 ? 43.385 17.066  -78.975  1.00 32.75 ? 110  HIS K NE2 1 
HETATM 10835 N  N   . CME J  1 111 ? 39.029 11.777  -78.580  1.00 28.11 ? 111  CME K N   1 
HETATM 10836 C  CA  . CME J  1 111 ? 37.903 10.887  -78.914  1.00 26.75 ? 111  CME K CA  1 
HETATM 10837 C  CB  . CME J  1 111 ? 37.626 9.890   -77.778  1.00 27.16 ? 111  CME K CB  1 
HETATM 10838 S  SG  . CME J  1 111 ? 36.926 10.679  -76.361  1.00 28.67 ? 111  CME K SG  1 
HETATM 10839 S  SD  . CME J  1 111 ? 36.856 9.197   -75.007  1.00 31.57 ? 111  CME K SD  1 
HETATM 10840 C  CE  . CME J  1 111 ? 38.427 9.222   -74.191  1.00 32.37 ? 111  CME K CE  1 
HETATM 10841 C  CZ  . CME J  1 111 ? 38.855 10.630  -73.789  1.00 33.51 ? 111  CME K CZ  1 
HETATM 10842 O  OH  . CME J  1 111 ? 37.939 11.173  -72.836  1.00 36.81 ? 111  CME K OH  1 
HETATM 10843 C  C   . CME J  1 111 ? 36.646 11.658  -79.254  1.00 25.64 ? 111  CME K C   1 
HETATM 10844 O  O   . CME J  1 111 ? 36.498 12.837  -78.888  1.00 25.69 ? 111  CME K O   1 
ATOM   10845 N  N   . ILE J  1 112 ? 35.731 11.007  -79.958  1.00 24.04 ? 112  ILE K N   1 
ATOM   10846 C  CA  . ILE J  1 112 ? 34.461 11.633  -80.324  1.00 23.39 ? 112  ILE K CA  1 
ATOM   10847 C  C   . ILE J  1 112 ? 33.324 11.237  -79.370  1.00 22.40 ? 112  ILE K C   1 
ATOM   10848 O  O   . ILE J  1 112 ? 32.178 11.635  -79.550  1.00 22.44 ? 112  ILE K O   1 
ATOM   10849 C  CB  . ILE J  1 112 ? 34.073 11.328  -81.786  1.00 23.22 ? 112  ILE K CB  1 
ATOM   10850 C  CG1 . ILE J  1 112 ? 33.729 9.839   -81.949  1.00 23.33 ? 112  ILE K CG1 1 
ATOM   10851 C  CG2 . ILE J  1 112 ? 35.191 11.801  -82.730  1.00 23.62 ? 112  ILE K CG2 1 
ATOM   10852 C  CD1 . ILE J  1 112 ? 33.279 9.433   -83.341  1.00 22.61 ? 112  ILE K CD1 1 
ATOM   10853 N  N   . ILE J  1 113 ? 33.649 10.445  -78.357  1.00 22.54 ? 113  ILE K N   1 
ATOM   10854 C  CA  . ILE J  1 113 ? 32.658 10.041  -77.369  1.00 21.77 ? 113  ILE K CA  1 
ATOM   10855 C  C   . ILE J  1 113 ? 32.164 11.260  -76.582  1.00 21.32 ? 113  ILE K C   1 
ATOM   10856 O  O   . ILE J  1 113 ? 32.961 12.082  -76.154  1.00 21.72 ? 113  ILE K O   1 
ATOM   10857 C  CB  . ILE J  1 113 ? 33.206 8.902   -76.475  1.00 22.43 ? 113  ILE K CB  1 
ATOM   10858 C  CG1 . ILE J  1 113 ? 33.339 7.634   -77.342  1.00 22.88 ? 113  ILE K CG1 1 
ATOM   10859 C  CG2 . ILE J  1 113 ? 32.304 8.713   -75.239  1.00 20.38 ? 113  ILE K CG2 1 
ATOM   10860 C  CD1 . ILE J  1 113 ? 33.450 6.308   -76.611  1.00 27.52 ? 113  ILE K CD1 1 
ATOM   10861 N  N   . GLY J  1 114 ? 30.846 11.403  -76.449  1.00 20.78 ? 114  GLY K N   1 
ATOM   10862 C  CA  . GLY J  1 114 ? 30.272 12.573  -75.775  1.00 20.59 ? 114  GLY K CA  1 
ATOM   10863 C  C   . GLY J  1 114 ? 30.162 13.820  -76.640  1.00 20.58 ? 114  GLY K C   1 
ATOM   10864 O  O   . GLY J  1 114 ? 29.848 14.904  -76.145  1.00 19.54 ? 114  GLY K O   1 
ATOM   10865 N  N   . ARG J  1 115 ? 30.438 13.672  -77.934  1.00 20.83 ? 115  ARG K N   1 
ATOM   10866 C  CA  . ARG J  1 115 ? 30.196 14.757  -78.878  1.00 21.40 ? 115  ARG K CA  1 
ATOM   10867 C  C   . ARG J  1 115 ? 28.974 14.408  -79.712  1.00 21.39 ? 115  ARG K C   1 
ATOM   10868 O  O   . ARG J  1 115 ? 28.295 13.408  -79.423  1.00 21.76 ? 115  ARG K O   1 
ATOM   10869 C  CB  . ARG J  1 115 ? 31.446 15.039  -79.709  1.00 22.07 ? 115  ARG K CB  1 
ATOM   10870 C  CG  . ARG J  1 115 ? 32.659 15.146  -78.808  1.00 22.68 ? 115  ARG K CG  1 
ATOM   10871 C  CD  . ARG J  1 115 ? 33.806 15.853  -79.432  1.00 22.34 ? 115  ARG K CD  1 
ATOM   10872 N  NE  . ARG J  1 115 ? 34.899 15.982  -78.466  1.00 25.06 ? 115  ARG K NE  1 
ATOM   10873 C  CZ  . ARG J  1 115 ? 35.221 17.100  -77.814  1.00 23.04 ? 115  ARG K CZ  1 
ATOM   10874 N  NH1 . ARG J  1 115 ? 36.243 17.099  -76.973  1.00 23.34 ? 115  ARG K NH1 1 
ATOM   10875 N  NH2 . ARG J  1 115 ? 34.543 18.221  -78.009  1.00 22.91 ? 115  ARG K NH2 1 
ATOM   10876 N  N   . THR J  1 116 ? 28.671 15.217  -80.725  1.00 21.08 ? 116  THR K N   1 
ATOM   10877 C  CA  . THR J  1 116 ? 27.393 15.114  -81.414  1.00 21.02 ? 116  THR K CA  1 
ATOM   10878 C  C   . THR J  1 116 ? 27.539 14.767  -82.894  1.00 20.81 ? 116  THR K C   1 
ATOM   10879 O  O   . THR J  1 116 ? 28.233 15.453  -83.633  1.00 20.85 ? 116  THR K O   1 
ATOM   10880 C  CB  . THR J  1 116 ? 26.558 16.424  -81.268  1.00 21.01 ? 116  THR K CB  1 
ATOM   10881 O  OG1 . THR J  1 116 ? 26.153 16.599  -79.903  1.00 21.26 ? 116  THR K OG1 1 
ATOM   10882 C  CG2 . THR J  1 116 ? 25.305 16.381  -82.149  1.00 19.61 ? 116  THR K CG2 1 
ATOM   10883 N  N   . LEU J  1 117 ? 26.883 13.694  -83.311  1.00 21.32 ? 117  LEU K N   1 
ATOM   10884 C  CA  . LEU J  1 117 ? 26.766 13.373  -84.730  1.00 21.47 ? 117  LEU K CA  1 
ATOM   10885 C  C   . LEU J  1 117 ? 25.601 14.175  -85.326  1.00 22.19 ? 117  LEU K C   1 
ATOM   10886 O  O   . LEU J  1 117 ? 24.522 14.227  -84.746  1.00 21.68 ? 117  LEU K O   1 
ATOM   10887 C  CB  . LEU J  1 117 ? 26.558 11.863  -84.920  1.00 21.57 ? 117  LEU K CB  1 
ATOM   10888 C  CG  . LEU J  1 117 ? 26.592 11.257  -86.338  1.00 20.22 ? 117  LEU K CG  1 
ATOM   10889 C  CD1 . LEU J  1 117 ? 27.965 11.337  -86.965  1.00 17.47 ? 117  LEU K CD1 1 
ATOM   10890 C  CD2 . LEU J  1 117 ? 26.149 9.821   -86.254  1.00 17.23 ? 117  LEU K CD2 1 
ATOM   10891 N  N   . VAL J  1 118 ? 25.835 14.804  -86.481  1.00 23.15 ? 118  VAL K N   1 
ATOM   10892 C  CA  . VAL J  1 118 ? 24.827 15.611  -87.155  1.00 23.89 ? 118  VAL K CA  1 
ATOM   10893 C  C   . VAL J  1 118 ? 24.700 15.149  -88.606  1.00 24.55 ? 118  VAL K C   1 
ATOM   10894 O  O   . VAL J  1 118 ? 25.708 14.935  -89.281  1.00 24.36 ? 118  VAL K O   1 
ATOM   10895 C  CB  . VAL J  1 118 ? 25.203 17.119  -87.121  1.00 23.95 ? 118  VAL K CB  1 
ATOM   10896 C  CG1 . VAL J  1 118 ? 24.285 17.945  -88.001  1.00 24.06 ? 118  VAL K CG1 1 
ATOM   10897 C  CG2 . VAL J  1 118 ? 25.181 17.656  -85.683  1.00 24.58 ? 118  VAL K CG2 1 
ATOM   10898 N  N   . VAL J  1 119 ? 23.463 14.971  -89.061  1.00 25.61 ? 119  VAL K N   1 
ATOM   10899 C  CA  . VAL J  1 119 ? 23.168 14.826  -90.492  1.00 26.45 ? 119  VAL K CA  1 
ATOM   10900 C  C   . VAL J  1 119 ? 22.456 16.090  -91.002  1.00 27.73 ? 119  VAL K C   1 
ATOM   10901 O  O   . VAL J  1 119 ? 21.626 16.671  -90.295  1.00 27.57 ? 119  VAL K O   1 
ATOM   10902 C  CB  . VAL J  1 119 ? 22.399 13.499  -90.817  1.00 26.16 ? 119  VAL K CB  1 
ATOM   10903 C  CG1 . VAL J  1 119 ? 21.075 13.417  -90.072  1.00 25.43 ? 119  VAL K CG1 1 
ATOM   10904 C  CG2 . VAL J  1 119 ? 22.199 13.332  -92.329  1.00 25.96 ? 119  VAL K CG2 1 
ATOM   10905 N  N   . HIS J  1 120 ? 22.779 16.505  -92.229  1.00 29.06 ? 120  HIS K N   1 
ATOM   10906 C  CA  . HIS J  1 120 ? 22.499 17.874  -92.686  1.00 30.17 ? 120  HIS K CA  1 
ATOM   10907 C  C   . HIS J  1 120 ? 21.438 18.008  -93.781  1.00 30.92 ? 120  HIS K C   1 
ATOM   10908 O  O   . HIS J  1 120 ? 21.055 17.037  -94.429  1.00 30.53 ? 120  HIS K O   1 
ATOM   10909 C  CB  . HIS J  1 120 ? 23.791 18.565  -93.144  1.00 30.20 ? 120  HIS K CB  1 
ATOM   10910 C  CG  . HIS J  1 120 ? 24.564 19.215  -92.036  1.00 30.96 ? 120  HIS K CG  1 
ATOM   10911 N  ND1 . HIS J  1 120 ? 24.291 20.490  -91.584  1.00 31.49 ? 120  HIS K ND1 1 
ATOM   10912 C  CD2 . HIS J  1 120 ? 25.622 18.778  -91.312  1.00 30.71 ? 120  HIS K CD2 1 
ATOM   10913 C  CE1 . HIS J  1 120 ? 25.137 20.802  -90.614  1.00 30.82 ? 120  HIS K CE1 1 
ATOM   10914 N  NE2 . HIS J  1 120 ? 25.955 19.782  -90.431  1.00 31.31 ? 120  HIS K NE2 1 
ATOM   10915 N  N   . GLU J  1 121 ? 20.995 19.246  -93.963  1.00 32.25 ? 121  GLU K N   1 
ATOM   10916 C  CA  . GLU J  1 121 ? 19.956 19.631  -94.917  1.00 33.56 ? 121  GLU K CA  1 
ATOM   10917 C  C   . GLU J  1 121 ? 20.444 19.521  -96.362  1.00 33.93 ? 121  GLU K C   1 
ATOM   10918 O  O   . GLU J  1 121 ? 19.718 19.019  -97.227  1.00 34.16 ? 121  GLU K O   1 
ATOM   10919 C  CB  . GLU J  1 121 ? 19.532 21.063  -94.585  1.00 34.06 ? 121  GLU K CB  1 
ATOM   10920 C  CG  . GLU J  1 121 ? 18.547 21.760  -95.516  1.00 35.70 ? 121  GLU K CG  1 
ATOM   10921 C  CD  . GLU J  1 121 ? 18.437 23.228  -95.162  1.00 37.86 ? 121  GLU K CD  1 
ATOM   10922 O  OE1 . GLU J  1 121 ? 19.434 23.960  -95.360  1.00 38.29 ? 121  GLU K OE1 1 
ATOM   10923 O  OE2 . GLU J  1 121 ? 17.369 23.644  -94.659  1.00 39.10 ? 121  GLU K OE2 1 
ATOM   10924 N  N   . LYS J  1 122 ? 21.672 19.985  -96.605  1.00 34.23 ? 122  LYS K N   1 
ATOM   10925 C  CA  . LYS J  1 122 ? 22.285 19.983  -97.946  1.00 34.55 ? 122  LYS K CA  1 
ATOM   10926 C  C   . LYS J  1 122 ? 23.469 19.022  -98.019  1.00 34.45 ? 122  LYS K C   1 
ATOM   10927 O  O   . LYS J  1 122 ? 23.955 18.529  -96.991  1.00 34.45 ? 122  LYS K O   1 
ATOM   10928 C  CB  . LYS J  1 122 ? 22.777 21.387  -98.326  1.00 34.81 ? 122  LYS K CB  1 
ATOM   10929 C  CG  . LYS J  1 122 ? 21.716 22.479  -98.355  1.00 35.92 ? 122  LYS K CG  1 
ATOM   10930 C  CD  . LYS J  1 122 ? 22.358 23.865  -98.434  1.00 37.43 ? 122  LYS K CD  1 
ATOM   10931 C  CE  . LYS J  1 122 ? 21.303 24.962  -98.380  1.00 38.47 ? 122  LYS K CE  1 
ATOM   10932 N  NZ  . LYS J  1 122 ? 21.878 26.337  -98.483  1.00 39.54 ? 122  LYS K NZ  1 
ATOM   10933 N  N   . ALA J  1 123 ? 23.932 18.770  -99.240  1.00 34.15 ? 123  ALA K N   1 
ATOM   10934 C  CA  . ALA J  1 123 ? 25.164 18.020  -99.476  1.00 33.94 ? 123  ALA K CA  1 
ATOM   10935 C  C   . ALA J  1 123 ? 26.363 18.809  -98.972  1.00 33.84 ? 123  ALA K C   1 
ATOM   10936 O  O   . ALA J  1 123 ? 26.383 20.031  -99.051  1.00 33.82 ? 123  ALA K O   1 
ATOM   10937 C  CB  . ALA J  1 123 ? 25.322 17.718  -100.960 1.00 33.94 ? 123  ALA K CB  1 
ATOM   10938 N  N   . ASP J  1 124 ? 27.355 18.104  -98.445  1.00 33.86 ? 124  ASP K N   1 
ATOM   10939 C  CA  . ASP J  1 124 ? 28.609 18.720  -98.029  1.00 33.94 ? 124  ASP K CA  1 
ATOM   10940 C  C   . ASP J  1 124 ? 29.507 18.914  -99.258  1.00 34.17 ? 124  ASP K C   1 
ATOM   10941 O  O   . ASP J  1 124 ? 29.859 17.942  -99.940  1.00 34.08 ? 124  ASP K O   1 
ATOM   10942 C  CB  . ASP J  1 124 ? 29.291 17.837  -96.975  1.00 33.32 ? 124  ASP K CB  1 
ATOM   10943 C  CG  . ASP J  1 124 ? 30.513 18.488  -96.335  1.00 32.97 ? 124  ASP K CG  1 
ATOM   10944 O  OD1 . ASP J  1 124 ? 30.939 17.984  -95.271  1.00 32.01 ? 124  ASP K OD1 1 
ATOM   10945 O  OD2 . ASP J  1 124 ? 31.058 19.481  -96.872  1.00 30.12 ? 124  ASP K OD2 1 
ATOM   10946 N  N   . ASP J  1 125 ? 29.883 20.165  -99.523  1.00 34.55 ? 125  ASP K N   1 
ATOM   10947 C  CA  . ASP J  1 125 ? 30.702 20.507  -100.693 1.00 35.25 ? 125  ASP K CA  1 
ATOM   10948 C  C   . ASP J  1 125 ? 32.184 20.151  -100.514 1.00 35.38 ? 125  ASP K C   1 
ATOM   10949 O  O   . ASP J  1 125 ? 33.008 20.424  -101.388 1.00 35.17 ? 125  ASP K O   1 
ATOM   10950 C  CB  . ASP J  1 125 ? 30.510 21.984  -101.105 1.00 35.39 ? 125  ASP K CB  1 
ATOM   10951 C  CG  . ASP J  1 125 ? 31.248 22.970  -100.198 1.00 36.39 ? 125  ASP K CG  1 
ATOM   10952 O  OD1 . ASP J  1 125 ? 30.971 24.190  -100.313 1.00 36.58 ? 125  ASP K OD1 1 
ATOM   10953 O  OD2 . ASP J  1 125 ? 32.101 22.550  -99.381  1.00 37.35 ? 125  ASP K OD2 1 
ATOM   10954 N  N   . LEU J  1 126 ? 32.503 19.556  -99.365  1.00 35.58 ? 126  LEU K N   1 
ATOM   10955 C  CA  . LEU J  1 126 ? 33.844 19.029  -99.052  1.00 35.75 ? 126  LEU K CA  1 
ATOM   10956 C  C   . LEU J  1 126 ? 34.949 20.091  -98.984  1.00 35.80 ? 126  LEU K C   1 
ATOM   10957 O  O   . LEU J  1 126 ? 36.130 19.782  -99.137  1.00 35.46 ? 126  LEU K O   1 
ATOM   10958 C  CB  . LEU J  1 126 ? 34.227 17.862  -99.990  1.00 35.78 ? 126  LEU K CB  1 
ATOM   10959 C  CG  . LEU J  1 126 ? 33.174 16.766  -100.239 1.00 36.12 ? 126  LEU K CG  1 
ATOM   10960 C  CD1 . LEU J  1 126 ? 33.662 15.719  -101.231 1.00 35.97 ? 126  LEU K CD1 1 
ATOM   10961 C  CD2 . LEU J  1 126 ? 32.705 16.098  -98.932  1.00 36.91 ? 126  LEU K CD2 1 
ATOM   10962 N  N   . GLY J  1 127 ? 34.554 21.335  -98.727  1.00 36.32 ? 127  GLY K N   1 
ATOM   10963 C  CA  . GLY J  1 127 ? 35.497 22.442  -98.594  1.00 37.44 ? 127  GLY K CA  1 
ATOM   10964 C  C   . GLY J  1 127 ? 36.053 22.917  -99.922  1.00 38.36 ? 127  GLY K C   1 
ATOM   10965 O  O   . GLY J  1 127 ? 36.985 23.729  -99.955  1.00 38.30 ? 127  GLY K O   1 
ATOM   10966 N  N   . LYS J  1 128 ? 35.482 22.398  -101.011 1.00 39.06 ? 128  LYS K N   1 
ATOM   10967 C  CA  . LYS J  1 128 ? 35.878 22.773  -102.370 1.00 40.03 ? 128  LYS K CA  1 
ATOM   10968 C  C   . LYS J  1 128 ? 34.826 23.643  -103.073 1.00 40.71 ? 128  LYS K C   1 
ATOM   10969 O  O   . LYS J  1 128 ? 34.811 23.750  -104.301 1.00 40.80 ? 128  LYS K O   1 
ATOM   10970 C  CB  . LYS J  1 128 ? 36.222 21.530  -103.211 1.00 39.84 ? 128  LYS K CB  1 
ATOM   10971 C  CG  . LYS J  1 128 ? 37.580 20.864  -102.900 1.00 39.84 ? 128  LYS K CG  1 
ATOM   10972 C  CD  . LYS J  1 128 ? 38.719 21.861  -102.565 1.00 40.80 ? 128  LYS K CD  1 
ATOM   10973 C  CE  . LYS J  1 128 ? 39.004 22.904  -103.664 1.00 41.21 ? 128  LYS K CE  1 
ATOM   10974 N  NZ  . LYS J  1 128 ? 39.636 22.327  -104.886 1.00 41.71 ? 128  LYS K NZ  1 
ATOM   10975 N  N   . GLY J  1 129 ? 33.961 24.271  -102.277 1.00 41.58 ? 129  GLY K N   1 
ATOM   10976 C  CA  . GLY J  1 129 ? 32.925 25.172  -102.789 1.00 42.25 ? 129  GLY K CA  1 
ATOM   10977 C  C   . GLY J  1 129 ? 33.466 26.535  -103.178 1.00 42.72 ? 129  GLY K C   1 
ATOM   10978 O  O   . GLY J  1 129 ? 32.776 27.324  -103.837 1.00 42.79 ? 129  GLY K O   1 
ATOM   10979 N  N   . GLY J  1 130 ? 34.697 26.814  -102.753 1.00 42.98 ? 130  GLY K N   1 
ATOM   10980 C  CA  . GLY J  1 130 ? 35.411 28.015  -103.166 1.00 43.36 ? 130  GLY K CA  1 
ATOM   10981 C  C   . GLY J  1 130 ? 34.988 29.315  -102.504 1.00 43.63 ? 130  GLY K C   1 
ATOM   10982 O  O   . GLY J  1 130 ? 35.384 30.387  -102.961 1.00 43.57 ? 130  GLY K O   1 
ATOM   10983 N  N   . ASN J  1 131 ? 34.177 29.235  -101.446 1.00 43.90 ? 131  ASN K N   1 
ATOM   10984 C  CA  . ASN J  1 131 ? 33.870 30.421  -100.632 1.00 44.29 ? 131  ASN K CA  1 
ATOM   10985 C  C   . ASN J  1 131 ? 34.267 30.282  -99.153  1.00 44.58 ? 131  ASN K C   1 
ATOM   10986 O  O   . ASN J  1 131 ? 34.737 29.219  -98.726  1.00 44.49 ? 131  ASN K O   1 
ATOM   10987 C  CB  . ASN J  1 131 ? 32.416 30.918  -100.817 1.00 44.30 ? 131  ASN K CB  1 
ATOM   10988 C  CG  . ASN J  1 131 ? 31.361 29.851  -100.526 1.00 44.50 ? 131  ASN K CG  1 
ATOM   10989 O  OD1 . ASN J  1 131 ? 31.595 28.894  -99.791  1.00 44.95 ? 131  ASN K OD1 1 
ATOM   10990 N  ND2 . ASN J  1 131 ? 30.177 30.038  -101.093 1.00 44.67 ? 131  ASN K ND2 1 
ATOM   10991 N  N   . GLU J  1 132 ? 34.094 31.358  -98.388  1.00 44.79 ? 132  GLU K N   1 
ATOM   10992 C  CA  . GLU J  1 132 ? 34.546 31.409  -96.998  1.00 44.88 ? 132  GLU K CA  1 
ATOM   10993 C  C   . GLU J  1 132 ? 33.772 30.428  -96.112  1.00 44.74 ? 132  GLU K C   1 
ATOM   10994 O  O   . GLU J  1 132 ? 34.366 29.682  -95.323  1.00 44.78 ? 132  GLU K O   1 
ATOM   10995 C  CB  . GLU J  1 132 ? 34.436 32.841  -96.471  1.00 45.05 ? 132  GLU K CB  1 
ATOM   10996 C  CG  . GLU J  1 132 ? 35.389 33.176  -95.322  1.00 46.19 ? 132  GLU K CG  1 
ATOM   10997 C  CD  . GLU J  1 132 ? 34.688 33.336  -93.979  1.00 47.88 ? 132  GLU K CD  1 
ATOM   10998 O  OE1 . GLU J  1 132 ? 35.290 33.964  -93.077  1.00 48.46 ? 132  GLU K OE1 1 
ATOM   10999 O  OE2 . GLU J  1 132 ? 33.543 32.846  -93.820  1.00 48.06 ? 132  GLU K OE2 1 
ATOM   11000 N  N   . GLU J  1 133 ? 32.449 30.422  -96.272  1.00 44.42 ? 133  GLU K N   1 
ATOM   11001 C  CA  . GLU J  1 133 ? 31.568 29.518  -95.534  1.00 44.06 ? 133  GLU K CA  1 
ATOM   11002 C  C   . GLU J  1 133 ? 31.849 28.040  -95.843  1.00 43.88 ? 133  GLU K C   1 
ATOM   11003 O  O   . GLU J  1 133 ? 31.580 27.168  -95.013  1.00 44.00 ? 133  GLU K O   1 
ATOM   11004 C  CB  . GLU J  1 133 ? 30.096 29.875  -95.804  1.00 44.03 ? 133  GLU K CB  1 
ATOM   11005 C  CG  . GLU J  1 133 ? 29.053 29.094  -94.986  1.00 43.60 ? 133  GLU K CG  1 
ATOM   11006 C  CD  . GLU J  1 133 ? 29.118 29.354  -93.482  1.00 43.28 ? 133  GLU K CD  1 
ATOM   11007 O  OE1 . GLU J  1 133 ? 30.223 29.305  -92.896  1.00 42.31 ? 133  GLU K OE1 1 
ATOM   11008 O  OE2 . GLU J  1 133 ? 28.048 29.594  -92.881  1.00 42.86 ? 133  GLU K OE2 1 
ATOM   11009 N  N   . SER J  1 134 ? 32.400 27.770  -97.027  1.00 43.48 ? 134  SER K N   1 
ATOM   11010 C  CA  . SER J  1 134 ? 32.738 26.407  -97.449  1.00 43.26 ? 134  SER K CA  1 
ATOM   11011 C  C   . SER J  1 134 ? 33.915 25.805  -96.675  1.00 43.11 ? 134  SER K C   1 
ATOM   11012 O  O   . SER J  1 134 ? 33.983 24.585  -96.494  1.00 42.95 ? 134  SER K O   1 
ATOM   11013 C  CB  . SER J  1 134 ? 33.036 26.361  -98.948  1.00 43.23 ? 134  SER K CB  1 
ATOM   11014 O  OG  . SER J  1 134 ? 33.637 25.131  -99.308  1.00 43.52 ? 134  SER K OG  1 
ATOM   11015 N  N   . THR J  1 135 ? 34.843 26.657  -96.243  1.00 42.85 ? 135  THR K N   1 
ATOM   11016 C  CA  . THR J  1 135 ? 35.990 26.205  -95.452  1.00 42.59 ? 135  THR K CA  1 
ATOM   11017 C  C   . THR J  1 135 ? 35.613 26.071  -93.978  1.00 42.33 ? 135  THR K C   1 
ATOM   11018 O  O   . THR J  1 135 ? 36.443 25.695  -93.142  1.00 42.14 ? 135  THR K O   1 
ATOM   11019 C  CB  . THR J  1 135 ? 37.194 27.151  -95.578  1.00 42.64 ? 135  THR K CB  1 
ATOM   11020 O  OG1 . THR J  1 135 ? 36.797 28.482  -95.221  1.00 42.97 ? 135  THR K OG1 1 
ATOM   11021 C  CG2 . THR J  1 135 ? 37.746 27.135  -97.003  1.00 42.97 ? 135  THR K CG2 1 
ATOM   11022 N  N   . LYS J  1 136 ? 34.355 26.380  -93.672  1.00 41.82 ? 136  LYS K N   1 
ATOM   11023 C  CA  . LYS J  1 136 ? 33.841 26.269  -92.314  1.00 41.25 ? 136  LYS K CA  1 
ATOM   11024 C  C   . LYS J  1 136 ? 32.794 25.162  -92.198  1.00 40.85 ? 136  LYS K C   1 
ATOM   11025 O  O   . LYS J  1 136 ? 33.058 24.124  -91.590  1.00 40.95 ? 136  LYS K O   1 
ATOM   11026 C  CB  . LYS J  1 136 ? 33.312 27.620  -91.817  1.00 41.22 ? 136  LYS K CB  1 
ATOM   11027 C  CG  . LYS J  1 136 ? 34.414 28.664  -91.634  1.00 41.27 ? 136  LYS K CG  1 
ATOM   11028 C  CD  . LYS J  1 136 ? 33.889 29.944  -91.009  1.00 41.79 ? 136  LYS K CD  1 
ATOM   11029 C  CE  . LYS J  1 136 ? 35.036 30.778  -90.464  1.00 41.51 ? 136  LYS K CE  1 
ATOM   11030 N  NZ  . LYS J  1 136 ? 34.548 31.902  -89.623  1.00 41.67 ? 136  LYS K NZ  1 
ATOM   11031 N  N   . THR J  1 137 ? 31.625 25.367  -92.798  1.00 40.34 ? 137  THR K N   1 
ATOM   11032 C  CA  . THR J  1 137 ? 30.523 24.417  -92.667  1.00 39.88 ? 137  THR K CA  1 
ATOM   11033 C  C   . THR J  1 137 ? 30.360 23.501  -93.885  1.00 39.57 ? 137  THR K C   1 
ATOM   11034 O  O   . THR J  1 137 ? 29.609 22.518  -93.833  1.00 39.60 ? 137  THR K O   1 
ATOM   11035 C  CB  . THR J  1 137 ? 29.192 25.140  -92.375  1.00 39.96 ? 137  THR K CB  1 
ATOM   11036 O  OG1 . THR J  1 137 ? 28.860 26.005  -93.473  1.00 40.00 ? 137  THR K OG1 1 
ATOM   11037 C  CG2 . THR J  1 137 ? 29.291 25.960  -91.091  1.00 39.81 ? 137  THR K CG2 1 
ATOM   11038 N  N   . GLY J  1 138 ? 31.067 23.820  -94.970  1.00 39.21 ? 138  GLY K N   1 
ATOM   11039 C  CA  . GLY J  1 138 ? 30.941 23.091  -96.235  1.00 38.24 ? 138  GLY K CA  1 
ATOM   11040 C  C   . GLY J  1 138 ? 29.597 23.303  -96.918  1.00 37.93 ? 138  GLY K C   1 
ATOM   11041 O  O   . GLY J  1 138 ? 29.203 22.516  -97.786  1.00 37.63 ? 138  GLY K O   1 
ATOM   11042 N  N   . ASN J  1 139 ? 28.906 24.374  -96.519  1.00 37.34 ? 139  ASN K N   1 
ATOM   11043 C  CA  . ASN J  1 139 ? 27.583 24.739  -97.048  1.00 36.79 ? 139  ASN K CA  1 
ATOM   11044 C  C   . ASN J  1 139 ? 26.563 23.600  -97.001  1.00 36.40 ? 139  ASN K C   1 
ATOM   11045 O  O   . ASN J  1 139 ? 25.843 23.345  -97.972  1.00 36.59 ? 139  ASN K O   1 
ATOM   11046 C  CB  . ASN J  1 139 ? 27.709 25.336  -98.454  1.00 36.75 ? 139  ASN K CB  1 
ATOM   11047 C  CG  . ASN J  1 139 ? 28.411 26.672  -98.443  1.00 36.47 ? 139  ASN K CG  1 
ATOM   11048 O  OD1 . ASN J  1 139 ? 27.873 27.655  -97.949  1.00 36.19 ? 139  ASN K OD1 1 
ATOM   11049 N  ND2 . ASN J  1 139 ? 29.627 26.711  -98.974  1.00 36.66 ? 139  ASN K ND2 1 
ATOM   11050 N  N   . ALA J  1 140 ? 26.505 22.922  -95.859  1.00 35.63 ? 140  ALA K N   1 
ATOM   11051 C  CA  . ALA J  1 140 ? 25.639 21.759  -95.711  1.00 34.80 ? 140  ALA K CA  1 
ATOM   11052 C  C   . ALA J  1 140 ? 24.263 22.145  -95.169  1.00 34.21 ? 140  ALA K C   1 
ATOM   11053 O  O   . ALA J  1 140 ? 23.392 21.290  -95.001  1.00 34.02 ? 140  ALA K O   1 
ATOM   11054 C  CB  . ALA J  1 140 ? 26.305 20.706  -94.831  1.00 34.91 ? 140  ALA K CB  1 
ATOM   11055 N  N   . GLY J  1 141 ? 24.077 23.437  -94.915  1.00 33.62 ? 141  GLY K N   1 
ATOM   11056 C  CA  . GLY J  1 141 ? 22.794 23.967  -94.458  1.00 32.87 ? 141  GLY K CA  1 
ATOM   11057 C  C   . GLY J  1 141 ? 22.451 23.662  -93.011  1.00 32.43 ? 141  GLY K C   1 
ATOM   11058 O  O   . GLY J  1 141 ? 23.334 23.410  -92.176  1.00 32.04 ? 141  GLY K O   1 
ATOM   11059 N  N   . SER J  1 142 ? 21.151 23.680  -92.718  1.00 31.79 ? 142  SER K N   1 
ATOM   11060 C  CA  . SER J  1 142 ? 20.655 23.417  -91.372  1.00 30.92 ? 142  SER K CA  1 
ATOM   11061 C  C   . SER J  1 142 ? 20.989 21.994  -90.892  1.00 30.37 ? 142  SER K C   1 
ATOM   11062 O  O   . SER J  1 142 ? 21.429 21.142  -91.671  1.00 29.92 ? 142  SER K O   1 
ATOM   11063 C  CB  . SER J  1 142 ? 19.145 23.711  -91.281  1.00 31.32 ? 142  SER K CB  1 
ATOM   11064 O  OG  . SER J  1 142 ? 18.347 22.661  -91.808  1.00 31.11 ? 142  SER K OG  1 
ATOM   11065 N  N   . ARG J  1 143 ? 20.794 21.767  -89.598  1.00 29.63 ? 143  ARG K N   1 
ATOM   11066 C  CA  . ARG J  1 143 ? 20.997 20.458  -88.988  1.00 28.75 ? 143  ARG K CA  1 
ATOM   11067 C  C   . ARG J  1 143 ? 19.637 19.793  -88.825  1.00 27.88 ? 143  ARG K C   1 
ATOM   11068 O  O   . ARG J  1 143 ? 18.757 20.318  -88.134  1.00 28.21 ? 143  ARG K O   1 
ATOM   11069 C  CB  . ARG J  1 143 ? 21.707 20.620  -87.640  1.00 28.82 ? 143  ARG K CB  1 
ATOM   11070 C  CG  . ARG J  1 143 ? 23.032 21.343  -87.770  1.00 28.83 ? 143  ARG K CG  1 
ATOM   11071 C  CD  . ARG J  1 143 ? 23.503 21.995  -86.492  1.00 30.89 ? 143  ARG K CD  1 
ATOM   11072 N  NE  . ARG J  1 143 ? 24.654 22.844  -86.782  1.00 30.52 ? 143  ARG K NE  1 
ATOM   11073 C  CZ  . ARG J  1 143 ? 25.573 23.216  -85.899  1.00 31.20 ? 143  ARG K CZ  1 
ATOM   11074 N  NH1 . ARG J  1 143 ? 26.577 23.981  -86.297  1.00 29.60 ? 143  ARG K NH1 1 
ATOM   11075 N  NH2 . ARG J  1 143 ? 25.502 22.827  -84.625  1.00 32.10 ? 143  ARG K NH2 1 
ATOM   11076 N  N   . LEU J  1 144 ? 19.470 18.641  -89.468  1.00 26.66 ? 144  LEU K N   1 
ATOM   11077 C  CA  . LEU J  1 144 ? 18.168 17.980  -89.549  1.00 25.66 ? 144  LEU K CA  1 
ATOM   11078 C  C   . LEU J  1 144 ? 17.911 17.038  -88.384  1.00 24.75 ? 144  LEU K C   1 
ATOM   11079 O  O   . LEU J  1 144 ? 16.794 16.970  -87.871  1.00 24.94 ? 144  LEU K O   1 
ATOM   11080 C  CB  . LEU J  1 144 ? 18.021 17.227  -90.873  1.00 25.37 ? 144  LEU K CB  1 
ATOM   11081 C  CG  . LEU J  1 144 ? 18.038 18.050  -92.172  1.00 26.41 ? 144  LEU K CG  1 
ATOM   11082 C  CD1 . LEU J  1 144 ? 17.840 17.128  -93.359  1.00 26.04 ? 144  LEU K CD1 1 
ATOM   11083 C  CD2 . LEU J  1 144 ? 16.993 19.182  -92.184  1.00 26.13 ? 144  LEU K CD2 1 
ATOM   11084 N  N   . ALA J  1 145 ? 18.947 16.299  -87.995  1.00 23.87 ? 145  ALA K N   1 
ATOM   11085 C  CA  . ALA J  1 145 ? 18.891 15.388  -86.860  1.00 22.80 ? 145  ALA K CA  1 
ATOM   11086 C  C   . ALA J  1 145 ? 20.292 15.268  -86.289  1.00 21.93 ? 145  ALA K C   1 
ATOM   11087 O  O   . ALA J  1 145 ? 21.275 15.347  -87.030  1.00 22.02 ? 145  ALA K O   1 
ATOM   11088 C  CB  . ALA J  1 145 ? 18.360 14.018  -87.281  1.00 22.89 ? 145  ALA K CB  1 
ATOM   11089 N  N   . CYS J  1 146 ? 20.370 15.114  -84.968  1.00 20.50 ? 146  CYS K N   1 
ATOM   11090 C  CA  . CYS J  1 146 ? 21.633 14.928  -84.276  1.00 19.32 ? 146  CYS K CA  1 
ATOM   11091 C  C   . CYS J  1 146 ? 21.466 14.045  -83.050  1.00 18.73 ? 146  CYS K C   1 
ATOM   11092 O  O   . CYS J  1 146 ? 20.349 13.732  -82.614  1.00 18.64 ? 146  CYS K O   1 
ATOM   11093 C  CB  . CYS J  1 146 ? 22.242 16.271  -83.872  0.40 19.23 ? 146  CYS K CB  1 
ATOM   11094 S  SG  . CYS J  1 146 ? 21.215 17.255  -82.794  0.40 17.71 ? 146  CYS K SG  1 
ATOM   11095 N  N   . GLY J  1 147 ? 22.591 13.642  -82.480  1.00 18.34 ? 147  GLY K N   1 
ATOM   11096 C  CA  . GLY J  1 147 ? 22.558 12.928  -81.222  1.00 17.63 ? 147  GLY K CA  1 
ATOM   11097 C  C   . GLY J  1 147 ? 23.936 12.884  -80.603  1.00 17.17 ? 147  GLY K C   1 
ATOM   11098 O  O   . GLY J  1 147 ? 24.935 13.093  -81.292  1.00 17.77 ? 147  GLY K O   1 
ATOM   11099 N  N   . VAL J  1 148 ? 23.984 12.616  -79.301  1.00 16.48 ? 148  VAL K N   1 
ATOM   11100 C  CA  . VAL J  1 148 ? 25.265 12.473  -78.600  1.00 16.33 ? 148  VAL K CA  1 
ATOM   11101 C  C   . VAL J  1 148 ? 25.800 11.063  -78.836  1.00 16.43 ? 148  VAL K C   1 
ATOM   11102 O  O   . VAL J  1 148 ? 25.060 10.072  -78.776  1.00 16.43 ? 148  VAL K O   1 
ATOM   11103 C  CB  . VAL J  1 148 ? 25.132 12.761  -77.095  1.00 16.15 ? 148  VAL K CB  1 
ATOM   11104 C  CG1 . VAL J  1 148 ? 26.510 12.905  -76.437  1.00 15.59 ? 148  VAL K CG1 1 
ATOM   11105 C  CG2 . VAL J  1 148 ? 24.300 14.019  -76.871  1.00 15.10 ? 148  VAL K CG2 1 
ATOM   11106 N  N   . ILE J  1 149 ? 27.084 10.993  -79.138  1.00 16.54 ? 149  ILE K N   1 
ATOM   11107 C  CA  . ILE J  1 149 ? 27.763 9.725   -79.320  1.00 16.73 ? 149  ILE K CA  1 
ATOM   11108 C  C   . ILE J  1 149 ? 28.098 9.132   -77.959  1.00 16.33 ? 149  ILE K C   1 
ATOM   11109 O  O   . ILE J  1 149 ? 28.859 9.730   -77.180  1.00 17.00 ? 149  ILE K O   1 
ATOM   11110 C  CB  . ILE J  1 149 ? 29.016 9.901   -80.181  1.00 16.85 ? 149  ILE K CB  1 
ATOM   11111 C  CG1 . ILE J  1 149 ? 28.631 10.523  -81.538  1.00 17.00 ? 149  ILE K CG1 1 
ATOM   11112 C  CG2 . ILE J  1 149 ? 29.749 8.557   -80.362  1.00 16.99 ? 149  ILE K CG2 1 
ATOM   11113 C  CD1 . ILE J  1 149 ? 29.839 10.990  -82.367  1.00 19.42 ? 149  ILE K CD1 1 
ATOM   11114 N  N   . GLY J  1 150 ? 27.532 7.955   -77.687  1.00 15.80 ? 150  GLY K N   1 
ATOM   11115 C  CA  . GLY J  1 150 ? 27.647 7.289   -76.384  1.00 15.57 ? 150  GLY K CA  1 
ATOM   11116 C  C   . GLY J  1 150 ? 28.379 5.958   -76.457  1.00 15.58 ? 150  GLY K C   1 
ATOM   11117 O  O   . GLY J  1 150 ? 28.423 5.313   -77.521  1.00 15.45 ? 150  GLY K O   1 
ATOM   11118 N  N   . ILE J  1 151 ? 28.996 5.566   -75.345  1.00 15.25 ? 151  ILE K N   1 
ATOM   11119 C  CA  . ILE J  1 151 ? 29.673 4.273   -75.236  1.00 15.63 ? 151  ILE K CA  1 
ATOM   11120 C  C   . ILE J  1 151 ? 28.658 3.146   -75.386  1.00 16.00 ? 151  ILE K C   1 
ATOM   11121 O  O   . ILE J  1 151 ? 27.606 3.199   -74.772  1.00 16.17 ? 151  ILE K O   1 
ATOM   11122 C  CB  . ILE J  1 151 ? 30.385 4.152   -73.861  1.00 15.59 ? 151  ILE K CB  1 
ATOM   11123 C  CG1 . ILE J  1 151 ? 31.442 5.251   -73.725  1.00 15.57 ? 151  ILE K CG1 1 
ATOM   11124 C  CG2 . ILE J  1 151 ? 31.005 2.767   -73.671  1.00 16.04 ? 151  ILE K CG2 1 
ATOM   11125 C  CD1 . ILE J  1 151 ? 31.732 5.649   -72.280  1.00 17.45 ? 151  ILE K CD1 1 
ATOM   11126 N  N   . ALA J  1 152 ? 28.971 2.135   -76.206  1.00 16.31 ? 152  ALA K N   1 
ATOM   11127 C  CA  . ALA J  1 152 ? 28.057 1.000   -76.410  1.00 17.23 ? 152  ALA K CA  1 
ATOM   11128 C  C   . ALA J  1 152 ? 28.635 -0.300  -75.885  1.00 17.90 ? 152  ALA K C   1 
ATOM   11129 O  O   . ALA J  1 152 ? 29.842 -0.411  -75.668  1.00 17.80 ? 152  ALA K O   1 
ATOM   11130 C  CB  . ALA J  1 152 ? 27.693 0.851   -77.889  1.00 16.64 ? 152  ALA K CB  1 
ATOM   11131 N  N   . GLN J  1 153 ? 27.768 -1.283  -75.682  1.00 19.68 ? 153  GLN K N   1 
ATOM   11132 C  CA  . GLN J  1 153 ? 28.215 -2.581  -75.224  1.00 21.86 ? 153  GLN K CA  1 
ATOM   11133 C  C   . GLN J  1 153 ? 28.847 -3.277  -76.412  1.00 22.74 ? 153  GLN K C   1 
ATOM   11134 O  O   . GLN J  1 153 ? 30.028 -3.594  -76.368  1.00 23.81 ? 153  GLN K O   1 
ATOM   11135 C  CB  . GLN J  1 153 ? 27.068 -3.409  -74.644  1.00 21.88 ? 153  GLN K CB  1 
ATOM   11136 C  CG  . GLN J  1 153 ? 27.554 -4.658  -73.922  1.00 24.22 ? 153  GLN K CG  1 
ATOM   11137 C  CD  . GLN J  1 153 ? 26.445 -5.455  -73.275  1.00 28.10 ? 153  GLN K CD  1 
ATOM   11138 O  OE1 . GLN J  1 153 ? 26.599 -5.952  -72.156  1.00 30.88 ? 153  GLN K OE1 1 
ATOM   11139 N  NE2 . GLN J  1 153 ? 25.322 -5.580  -73.966  1.00 29.41 ? 153  GLN K NE2 1 
ATOM   11140 O  OXT . GLN J  1 153 ? 28.203 -3.486  -77.434  1.00 23.46 ? 153  GLN K OXT 1 
ATOM   11141 N  N   . ALA K  1 1   ? 44.400 -13.028 -64.117  1.00 30.14 ? 1    ALA L N   1 
ATOM   11142 C  CA  . ALA K  1 1   ? 45.390 -12.295 -63.269  1.00 29.81 ? 1    ALA L CA  1 
ATOM   11143 C  C   . ALA K  1 1   ? 46.463 -11.623 -64.122  1.00 29.68 ? 1    ALA L C   1 
ATOM   11144 O  O   . ALA K  1 1   ? 46.801 -12.111 -65.203  1.00 30.10 ? 1    ALA L O   1 
ATOM   11145 C  CB  . ALA K  1 1   ? 46.028 -13.244 -62.242  1.00 29.88 ? 1    ALA L CB  1 
ATOM   11146 N  N   . THR K  1 2   ? 46.986 -10.498 -63.633  1.00 29.04 ? 2    THR L N   1 
ATOM   11147 C  CA  . THR K  1 2   ? 48.077 -9.783  -64.286  1.00 28.13 ? 2    THR L CA  1 
ATOM   11148 C  C   . THR K  1 2   ? 49.296 -9.847  -63.368  1.00 27.58 ? 2    THR L C   1 
ATOM   11149 O  O   . THR K  1 2   ? 49.154 -9.811  -62.142  1.00 26.76 ? 2    THR L O   1 
ATOM   11150 C  CB  . THR K  1 2   ? 47.698 -8.309  -64.566  1.00 28.42 ? 2    THR L CB  1 
ATOM   11151 O  OG1 . THR K  1 2   ? 46.461 -8.263  -65.282  1.00 29.62 ? 2    THR L OG1 1 
ATOM   11152 C  CG2 . THR K  1 2   ? 48.765 -7.605  -65.398  1.00 29.07 ? 2    THR L CG2 1 
ATOM   11153 N  N   . LYS K  1 3   ? 50.480 -9.958  -63.970  1.00 26.57 ? 3    LYS L N   1 
ATOM   11154 C  CA  . LYS K  1 3   ? 51.731 -10.046 -63.231  1.00 25.79 ? 3    LYS L CA  1 
ATOM   11155 C  C   . LYS K  1 3   ? 52.748 -9.025  -63.709  1.00 24.44 ? 3    LYS L C   1 
ATOM   11156 O  O   . LYS K  1 3   ? 52.820 -8.684  -64.895  1.00 24.34 ? 3    LYS L O   1 
ATOM   11157 C  CB  . LYS K  1 3   ? 52.319 -11.456 -63.306  1.00 26.23 ? 3    LYS L CB  1 
ATOM   11158 C  CG  . LYS K  1 3   ? 51.614 -12.470 -62.427  1.00 27.99 ? 3    LYS L CG  1 
ATOM   11159 C  CD  . LYS K  1 3   ? 52.046 -13.888 -62.767  1.00 30.59 ? 3    LYS L CD  1 
ATOM   11160 C  CE  . LYS K  1 3   ? 51.324 -14.905 -61.895  1.00 32.91 ? 3    LYS L CE  1 
ATOM   11161 N  NZ  . LYS K  1 3   ? 51.741 -16.309 -62.220  1.00 35.37 ? 3    LYS L NZ  1 
ATOM   11162 N  N   . ALA K  1 4   ? 53.528 -8.518  -62.762  1.00 23.02 ? 4    ALA L N   1 
ATOM   11163 C  CA  . ALA K  1 4   ? 54.586 -7.596  -63.083  1.00 21.26 ? 4    ALA L CA  1 
ATOM   11164 C  C   . ALA K  1 4   ? 55.820 -7.905  -62.239  1.00 20.27 ? 4    ALA L C   1 
ATOM   11165 O  O   . ALA K  1 4   ? 55.748 -8.663  -61.257  1.00 20.48 ? 4    ALA L O   1 
ATOM   11166 C  CB  . ALA K  1 4   ? 54.120 -6.150  -62.912  1.00 21.72 ? 4    ALA L CB  1 
ATOM   11167 N  N   . VAL K  1 5   ? 56.947 -7.337  -62.652  1.00 19.09 ? 5    VAL L N   1 
ATOM   11168 C  CA  . VAL K  1 5   ? 58.246 -7.598  -62.029  1.00 17.97 ? 5    VAL L CA  1 
ATOM   11169 C  C   . VAL K  1 5   ? 59.106 -6.356  -62.172  1.00 17.44 ? 5    VAL L C   1 
ATOM   11170 O  O   . VAL K  1 5   ? 58.910 -5.559  -63.091  1.00 17.69 ? 5    VAL L O   1 
ATOM   11171 C  CB  . VAL K  1 5   ? 58.962 -8.781  -62.723  1.00 17.89 ? 5    VAL L CB  1 
ATOM   11172 C  CG1 . VAL K  1 5   ? 59.576 -8.336  -64.054  1.00 17.98 ? 5    VAL L CG1 1 
ATOM   11173 C  CG2 . VAL K  1 5   ? 60.016 -9.410  -61.792  1.00 16.78 ? 5    VAL L CG2 1 
ATOM   11174 N  N   . CYS K  1 6   ? 60.075 -6.198  -61.269  1.00 17.49 ? 6    CYS L N   1 
ATOM   11175 C  CA  . CYS K  1 6   ? 60.976 -5.059  -61.311  1.00 16.35 ? 6    CYS L CA  1 
ATOM   11176 C  C   . CYS K  1 6   ? 62.355 -5.431  -60.761  1.00 16.42 ? 6    CYS L C   1 
ATOM   11177 O  O   . CYS K  1 6   ? 62.464 -6.036  -59.698  1.00 16.87 ? 6    CYS L O   1 
ATOM   11178 C  CB  . CYS K  1 6   ? 60.382 -3.902  -60.501  1.00 17.26 ? 6    CYS L CB  1 
ATOM   11179 S  SG  . CYS K  1 6   ? 61.447 -2.478  -60.380  1.00 15.28 ? 6    CYS L SG  1 
ATOM   11180 N  N   . VAL K  1 7   ? 63.390 -5.080  -61.516  1.00 16.27 ? 7    VAL L N   1 
ATOM   11181 C  CA  . VAL K  1 7   ? 64.770 -5.270  -61.103  1.00 16.39 ? 7    VAL L CA  1 
ATOM   11182 C  C   . VAL K  1 7   ? 65.314 -3.938  -60.606  1.00 16.45 ? 7    VAL L C   1 
ATOM   11183 O  O   . VAL K  1 7   ? 65.436 -2.968  -61.366  1.00 17.16 ? 7    VAL L O   1 
ATOM   11184 C  CB  . VAL K  1 7   ? 65.637 -5.855  -62.245  1.00 16.63 ? 7    VAL L CB  1 
ATOM   11185 C  CG1 . VAL K  1 7   ? 67.130 -5.871  -61.844  1.00 17.50 ? 7    VAL L CG1 1 
ATOM   11186 C  CG2 . VAL K  1 7   ? 65.155 -7.284  -62.598  1.00 15.69 ? 7    VAL L CG2 1 
ATOM   11187 N  N   . LEU K  1 8   ? 65.620 -3.897  -59.312  1.00 16.96 ? 8    LEU L N   1 
ATOM   11188 C  CA  . LEU K  1 8   ? 66.148 -2.708  -58.665  1.00 16.71 ? 8    LEU L CA  1 
ATOM   11189 C  C   . LEU K  1 8   ? 67.669 -2.709  -58.732  1.00 17.14 ? 8    LEU L C   1 
ATOM   11190 O  O   . LEU K  1 8   ? 68.301 -3.692  -58.327  1.00 16.07 ? 8    LEU L O   1 
ATOM   11191 C  CB  . LEU K  1 8   ? 65.685 -2.653  -57.207  1.00 16.70 ? 8    LEU L CB  1 
ATOM   11192 C  CG  . LEU K  1 8   ? 64.178 -2.500  -56.947  1.00 15.86 ? 8    LEU L CG  1 
ATOM   11193 C  CD1 . LEU K  1 8   ? 63.937 -2.418  -55.461  1.00 15.52 ? 8    LEU L CD1 1 
ATOM   11194 C  CD2 . LEU K  1 8   ? 63.647 -1.252  -57.596  1.00 17.73 ? 8    LEU L CD2 1 
ATOM   11195 N  N   . LYS K  1 9   ? 68.230 -1.601  -59.218  1.00 17.71 ? 9    LYS L N   1 
ATOM   11196 C  CA  . LYS K  1 9   ? 69.685 -1.407  -59.364  1.00 19.48 ? 9    LYS L CA  1 
ATOM   11197 C  C   . LYS K  1 9   ? 70.031 0.050   -59.137  1.00 19.40 ? 9    LYS L C   1 
ATOM   11198 O  O   . LYS K  1 9   ? 69.213 0.919   -59.401  1.00 19.45 ? 9    LYS L O   1 
ATOM   11199 C  CB  . LYS K  1 9   ? 70.144 -1.781  -60.777  1.00 19.99 ? 9    LYS L CB  1 
ATOM   11200 C  CG  . LYS K  1 9   ? 70.350 -3.262  -61.041  1.00 23.14 ? 9    LYS L CG  1 
ATOM   11201 C  CD  . LYS K  1 9   ? 70.899 -3.458  -62.477  1.00 24.97 ? 9    LYS L CD  1 
ATOM   11202 C  CE  . LYS K  1 9   ? 70.584 -4.847  -63.058  1.00 27.93 ? 9    LYS L CE  1 
ATOM   11203 N  NZ  . LYS K  1 9   ? 71.191 -5.979  -62.278  1.00 28.91 ? 9    LYS L NZ  1 
ATOM   11204 N  N   . GLY K  1 10  ? 71.252 0.335   -58.693  1.00 19.55 ? 10   GLY L N   1 
ATOM   11205 C  CA  . GLY K  1 10  ? 71.631 1.723   -58.420  1.00 20.31 ? 10   GLY L CA  1 
ATOM   11206 C  C   . GLY K  1 10  ? 73.123 1.994   -58.470  1.00 20.84 ? 10   GLY L C   1 
ATOM   11207 O  O   . GLY K  1 10  ? 73.887 1.192   -58.995  1.00 21.11 ? 10   GLY L O   1 
ATOM   11208 N  N   . ASP K  1 11  ? 73.532 3.127   -57.915  1.00 21.51 ? 11   ASP L N   1 
ATOM   11209 C  CA  . ASP K  1 11  ? 74.939 3.541   -57.933  1.00 22.54 ? 11   ASP L CA  1 
ATOM   11210 C  C   . ASP K  1 11  ? 75.784 2.851   -56.860  1.00 21.80 ? 11   ASP L C   1 
ATOM   11211 O  O   . ASP K  1 11  ? 77.025 2.913   -56.895  1.00 21.92 ? 11   ASP L O   1 
ATOM   11212 C  CB  . ASP K  1 11  ? 75.052 5.062   -57.784  1.00 23.46 ? 11   ASP L CB  1 
ATOM   11213 C  CG  . ASP K  1 11  ? 74.940 5.805   -59.118  1.00 26.62 ? 11   ASP L CG  1 
ATOM   11214 O  OD1 . ASP K  1 11  ? 75.265 7.015   -59.148  1.00 31.54 ? 11   ASP L OD1 1 
ATOM   11215 O  OD2 . ASP K  1 11  ? 74.535 5.197   -60.137  1.00 28.87 ? 11   ASP L OD2 1 
ATOM   11216 N  N   . GLY K  1 12  ? 75.124 2.203   -55.904  1.00 20.27 ? 12   GLY L N   1 
ATOM   11217 C  CA  . GLY K  1 12  ? 75.828 1.609   -54.769  1.00 18.38 ? 12   GLY L CA  1 
ATOM   11218 C  C   . GLY K  1 12  ? 75.543 0.140   -54.537  1.00 16.77 ? 12   GLY L C   1 
ATOM   11219 O  O   . GLY K  1 12  ? 75.323 -0.608  -55.487  1.00 17.52 ? 12   GLY L O   1 
ATOM   11220 N  N   . PRO K  1 13  ? 75.540 -0.287  -53.262  1.00 15.58 ? 13   PRO L N   1 
ATOM   11221 C  CA  . PRO K  1 13  ? 75.384 -1.691  -52.863  1.00 14.51 ? 13   PRO L CA  1 
ATOM   11222 C  C   . PRO K  1 13  ? 74.002 -2.309  -53.084  1.00 14.35 ? 13   PRO L C   1 
ATOM   11223 O  O   . PRO K  1 13  ? 73.864 -3.527  -52.992  1.00 14.48 ? 13   PRO L O   1 
ATOM   11224 C  CB  . PRO K  1 13  ? 75.625 -1.643  -51.351  1.00 13.93 ? 13   PRO L CB  1 
ATOM   11225 C  CG  . PRO K  1 13  ? 76.352 -0.379  -51.103  1.00 14.98 ? 13   PRO L CG  1 
ATOM   11226 C  CD  . PRO K  1 13  ? 75.771 0.575   -52.087  1.00 15.68 ? 13   PRO L CD  1 
ATOM   11227 N  N   . VAL K  1 14  ? 72.981 -1.485  -53.321  1.00 13.23 ? 14   VAL L N   1 
ATOM   11228 C  CA  . VAL K  1 14  ? 71.607 -1.980  -53.210  1.00 12.88 ? 14   VAL L CA  1 
ATOM   11229 C  C   . VAL K  1 14  ? 71.118 -2.657  -54.458  1.00 13.11 ? 14   VAL L C   1 
ATOM   11230 O  O   . VAL K  1 14  ? 71.184 -2.084  -55.541  1.00 13.79 ? 14   VAL L O   1 
ATOM   11231 C  CB  . VAL K  1 14  ? 70.626 -0.865  -52.800  1.00 12.15 ? 14   VAL L CB  1 
ATOM   11232 C  CG1 . VAL K  1 14  ? 69.191 -1.444  -52.657  1.00 11.31 ? 14   VAL L CG1 1 
ATOM   11233 C  CG2 . VAL K  1 14  ? 71.086 -0.252  -51.504  1.00 13.32 ? 14   VAL L CG2 1 
ATOM   11234 N  N   . GLN K  1 15  ? 70.633 -3.887  -54.313  1.00 13.60 ? 15   GLN L N   1 
ATOM   11235 C  CA  . GLN K  1 15  ? 70.043 -4.581  -55.442  1.00 14.30 ? 15   GLN L CA  1 
ATOM   11236 C  C   . GLN K  1 15  ? 68.889 -5.482  -55.022  1.00 14.20 ? 15   GLN L C   1 
ATOM   11237 O  O   . GLN K  1 15  ? 68.871 -6.027  -53.917  1.00 14.31 ? 15   GLN L O   1 
ATOM   11238 C  CB  . GLN K  1 15  ? 71.117 -5.360  -56.232  1.00 15.14 ? 15   GLN L CB  1 
ATOM   11239 C  CG  . GLN K  1 15  ? 71.498 -6.693  -55.610  1.00 17.51 ? 15   GLN L CG  1 
ATOM   11240 C  CD  . GLN K  1 15  ? 72.475 -7.475  -56.457  1.00 21.69 ? 15   GLN L CD  1 
ATOM   11241 O  OE1 . GLN K  1 15  ? 73.684 -7.234  -56.418  1.00 22.02 ? 15   GLN L OE1 1 
ATOM   11242 N  NE2 . GLN K  1 15  ? 71.953 -8.439  -57.229  1.00 23.91 ? 15   GLN L NE2 1 
ATOM   11243 N  N   . GLY K  1 16  ? 67.912 -5.641  -55.906  1.00 14.50 ? 16   GLY L N   1 
ATOM   11244 C  CA  . GLY K  1 16  ? 66.770 -6.486  -55.585  1.00 14.72 ? 16   GLY L CA  1 
ATOM   11245 C  C   . GLY K  1 16  ? 65.877 -6.842  -56.749  1.00 14.31 ? 16   GLY L C   1 
ATOM   11246 O  O   . GLY K  1 16  ? 65.994 -6.278  -57.843  1.00 14.70 ? 16   GLY L O   1 
ATOM   11247 N  N   . ILE K  1 17  ? 65.006 -7.814  -56.506  1.00 14.31 ? 17   ILE L N   1 
ATOM   11248 C  CA  . ILE K  1 17  ? 63.936 -8.147  -57.437  1.00 14.20 ? 17   ILE L CA  1 
ATOM   11249 C  C   . ILE K  1 17  ? 62.585 -8.111  -56.705  1.00 13.90 ? 17   ILE L C   1 
ATOM   11250 O  O   . ILE K  1 17  ? 62.405 -8.734  -55.651  1.00 13.08 ? 17   ILE L O   1 
ATOM   11251 C  CB  . ILE K  1 17  ? 64.172 -9.515  -58.143  1.00 14.56 ? 17   ILE L CB  1 
ATOM   11252 C  CG1 . ILE K  1 17  ? 65.497 -9.504  -58.897  1.00 15.09 ? 17   ILE L CG1 1 
ATOM   11253 C  CG2 . ILE K  1 17  ? 63.041 -9.828  -59.153  1.00 14.73 ? 17   ILE L CG2 1 
ATOM   11254 C  CD1 . ILE K  1 17  ? 66.125 -10.886 -59.054  1.00 16.23 ? 17   ILE L CD1 1 
ATOM   11255 N  N   . ILE K  1 18  ? 61.634 -7.382  -57.280  1.00 13.96 ? 18   ILE L N   1 
ATOM   11256 C  CA  . ILE K  1 18  ? 60.315 -7.265  -56.673  1.00 14.02 ? 18   ILE L CA  1 
ATOM   11257 C  C   . ILE K  1 18  ? 59.270 -7.773  -57.654  1.00 14.20 ? 18   ILE L C   1 
ATOM   11258 O  O   . ILE K  1 18  ? 59.266 -7.381  -58.806  1.00 14.14 ? 18   ILE L O   1 
ATOM   11259 C  CB  . ILE K  1 18  ? 60.006 -5.799  -56.265  1.00 14.00 ? 18   ILE L CB  1 
ATOM   11260 C  CG1 . ILE K  1 18  ? 61.016 -5.291  -55.223  1.00 12.33 ? 18   ILE L CG1 1 
ATOM   11261 C  CG2 . ILE K  1 18  ? 58.589 -5.671  -55.731  1.00 13.86 ? 18   ILE L CG2 1 
ATOM   11262 C  CD1 . ILE K  1 18  ? 61.028 -6.083  -53.917  1.00 10.15 ? 18   ILE L CD1 1 
ATOM   11263 N  N   . ASN K  1 19  ? 58.400 -8.650  -57.186  1.00 14.70 ? 19   ASN L N   1 
ATOM   11264 C  CA  . ASN K  1 19  ? 57.292 -9.149  -57.999  1.00 16.19 ? 19   ASN L CA  1 
ATOM   11265 C  C   . ASN K  1 19  ? 55.988 -8.484  -57.622  1.00 16.83 ? 19   ASN L C   1 
ATOM   11266 O  O   . ASN K  1 19  ? 55.817 -8.073  -56.477  1.00 16.26 ? 19   ASN L O   1 
ATOM   11267 C  CB  . ASN K  1 19  ? 57.156 -10.643 -57.790  1.00 16.61 ? 19   ASN L CB  1 
ATOM   11268 C  CG  . ASN K  1 19  ? 58.430 -11.381 -58.113  1.00 19.14 ? 19   ASN L CG  1 
ATOM   11269 O  OD1 . ASN K  1 19  ? 58.869 -11.396 -59.271  1.00 17.91 ? 19   ASN L OD1 1 
ATOM   11270 N  ND2 . ASN K  1 19  ? 59.054 -11.963 -57.094  1.00 19.63 ? 19   ASN L ND2 1 
ATOM   11271 N  N   . PHE K  1 20  ? 55.082 -8.383  -58.594  1.00 17.57 ? 20   PHE L N   1 
ATOM   11272 C  CA  . PHE K  1 20  ? 53.719 -7.916  -58.364  1.00 18.57 ? 20   PHE L CA  1 
ATOM   11273 C  C   . PHE K  1 20  ? 52.728 -8.980  -58.863  1.00 19.71 ? 20   PHE L C   1 
ATOM   11274 O  O   . PHE K  1 20  ? 52.984 -9.635  -59.864  1.00 19.87 ? 20   PHE L O   1 
ATOM   11275 C  CB  . PHE K  1 20  ? 53.470 -6.574  -59.069  1.00 18.09 ? 20   PHE L CB  1 
ATOM   11276 C  CG  . PHE K  1 20  ? 54.419 -5.456  -58.652  1.00 18.70 ? 20   PHE L CG  1 
ATOM   11277 C  CD1 . PHE K  1 20  ? 54.015 -4.482  -57.740  1.00 19.34 ? 20   PHE L CD1 1 
ATOM   11278 C  CD2 . PHE K  1 20  ? 55.714 -5.374  -59.184  1.00 18.85 ? 20   PHE L CD2 1 
ATOM   11279 C  CE1 . PHE K  1 20  ? 54.889 -3.460  -57.354  1.00 18.10 ? 20   PHE L CE1 1 
ATOM   11280 C  CE2 . PHE K  1 20  ? 56.588 -4.365  -58.809  1.00 18.57 ? 20   PHE L CE2 1 
ATOM   11281 C  CZ  . PHE K  1 20  ? 56.168 -3.397  -57.900  1.00 19.16 ? 20   PHE L CZ  1 
ATOM   11282 N  N   . GLU K  1 21  ? 51.618 -9.169  -58.157  1.00 20.72 ? 21   GLU L N   1 
ATOM   11283 C  CA  . GLU K  1 21  ? 50.526 -9.990  -58.692  1.00 22.34 ? 21   GLU L CA  1 
ATOM   11284 C  C   . GLU K  1 21  ? 49.151 -9.435  -58.337  1.00 22.10 ? 21   GLU L C   1 
ATOM   11285 O  O   . GLU K  1 21  ? 48.902 -9.077  -57.180  1.00 21.66 ? 21   GLU L O   1 
ATOM   11286 C  CB  . GLU K  1 21  ? 50.638 -11.426 -58.221  1.00 22.72 ? 21   GLU L CB  1 
ATOM   11287 C  CG  . GLU K  1 21  ? 50.006 -12.410 -59.184  1.00 26.98 ? 21   GLU L CG  1 
ATOM   11288 C  CD  . GLU K  1 21  ? 49.435 -13.614 -58.489  1.00 31.84 ? 21   GLU L CD  1 
ATOM   11289 O  OE1 . GLU K  1 21  ? 49.831 -14.749 -58.851  1.00 34.36 ? 21   GLU L OE1 1 
ATOM   11290 O  OE2 . GLU K  1 21  ? 48.585 -13.423 -57.587  1.00 34.48 ? 21   GLU L OE2 1 
ATOM   11291 N  N   . GLN K  1 22  ? 48.268 -9.375  -59.337  1.00 22.01 ? 22   GLN L N   1 
ATOM   11292 C  CA  . GLN K  1 22  ? 46.901 -8.899  -59.135  1.00 21.89 ? 22   GLN L CA  1 
ATOM   11293 C  C   . GLN K  1 22  ? 45.890 -9.802  -59.835  1.00 23.03 ? 22   GLN L C   1 
ATOM   11294 O  O   . GLN K  1 22  ? 45.820 -9.819  -61.060  1.00 23.09 ? 22   GLN L O   1 
ATOM   11295 C  CB  . GLN K  1 22  ? 46.751 -7.466  -59.628  1.00 21.21 ? 22   GLN L CB  1 
ATOM   11296 C  CG  . GLN K  1 22  ? 45.513 -6.777  -59.077  1.00 18.54 ? 22   GLN L CG  1 
ATOM   11297 C  CD  . GLN K  1 22  ? 45.228 -5.481  -59.765  1.00 15.43 ? 22   GLN L CD  1 
ATOM   11298 O  OE1 . GLN K  1 22  ? 45.765 -5.210  -60.832  1.00 14.47 ? 22   GLN L OE1 1 
ATOM   11299 N  NE2 . GLN K  1 22  ? 44.364 -4.668  -59.169  1.00 16.83 ? 22   GLN L NE2 1 
ATOM   11300 N  N   . LYS K  1 23  ? 45.126 -10.542 -59.033  1.00 24.42 ? 23   LYS L N   1 
ATOM   11301 C  CA  . LYS K  1 23  ? 44.121 -11.503 -59.500  1.00 26.17 ? 23   LYS L CA  1 
ATOM   11302 C  C   . LYS K  1 23  ? 42.975 -10.862 -60.277  1.00 26.72 ? 23   LYS L C   1 
ATOM   11303 O  O   . LYS K  1 23  ? 42.619 -11.325 -61.359  1.00 26.88 ? 23   LYS L O   1 
ATOM   11304 C  CB  . LYS K  1 23  ? 43.535 -12.269 -58.315  1.00 26.20 ? 23   LYS L CB  1 
ATOM   11305 C  CG  . LYS K  1 23  ? 44.444 -13.347 -57.759  1.00 28.99 ? 23   LYS L CG  1 
ATOM   11306 C  CD  . LYS K  1 23  ? 43.988 -13.807 -56.371  1.00 32.28 ? 23   LYS L CD  1 
ATOM   11307 C  CE  . LYS K  1 23  ? 45.107 -14.542 -55.630  1.00 33.40 ? 23   LYS L CE  1 
ATOM   11308 N  NZ  . LYS K  1 23  ? 45.779 -15.577 -56.492  1.00 34.11 ? 23   LYS L NZ  1 
ATOM   11309 N  N   . GLU K  1 24  ? 42.386 -9.819  -59.704  1.00 27.21 ? 24   GLU L N   1 
ATOM   11310 C  CA  . GLU K  1 24  ? 41.280 -9.122  -60.342  1.00 28.25 ? 24   GLU L CA  1 
ATOM   11311 C  C   . GLU K  1 24  ? 41.578 -7.642  -60.495  1.00 28.02 ? 24   GLU L C   1 
ATOM   11312 O  O   . GLU K  1 24  ? 42.307 -7.056  -59.691  1.00 28.23 ? 24   GLU L O   1 
ATOM   11313 C  CB  . GLU K  1 24  ? 39.973 -9.323  -59.561  1.00 28.40 ? 24   GLU L CB  1 
ATOM   11314 C  CG  . GLU K  1 24  ? 39.291 -10.676 -59.811  1.00 31.67 ? 24   GLU L CG  1 
ATOM   11315 C  CD  . GLU K  1 24  ? 39.701 -11.762 -58.817  1.00 35.08 ? 24   GLU L CD  1 
ATOM   11316 O  OE1 . GLU K  1 24  ? 40.322 -11.447 -57.772  1.00 36.02 ? 24   GLU L OE1 1 
ATOM   11317 O  OE2 . GLU K  1 24  ? 39.382 -12.945 -59.078  1.00 37.11 ? 24   GLU L OE2 1 
ATOM   11318 N  N   . SER K  1 25  ? 41.025 -7.079  -61.566  1.00 27.84 ? 25   SER L N   1 
ATOM   11319 C  CA  . SER K  1 25  ? 40.934 -5.648  -61.847  1.00 27.59 ? 25   SER L CA  1 
ATOM   11320 C  C   . SER K  1 25  ? 40.614 -4.779  -60.614  1.00 26.95 ? 25   SER L C   1 
ATOM   11321 O  O   . SER K  1 25  ? 41.241 -3.745  -60.387  1.00 27.00 ? 25   SER L O   1 
ATOM   11322 C  CB  . SER K  1 25  ? 39.832 -5.469  -62.909  1.00 27.69 ? 25   SER L CB  1 
ATOM   11323 O  OG  . SER K  1 25  ? 39.643 -4.126  -63.297  1.00 29.41 ? 25   SER L OG  1 
ATOM   11324 N  N   . ASN K  1 26  ? 39.627 -5.198  -59.828  1.00 26.22 ? 26   ASN L N   1 
ATOM   11325 C  CA  . ASN K  1 26  ? 39.194 -4.419  -58.666  1.00 25.56 ? 26   ASN L CA  1 
ATOM   11326 C  C   . ASN K  1 26  ? 39.852 -4.870  -57.357  1.00 24.50 ? 26   ASN L C   1 
ATOM   11327 O  O   . ASN K  1 26  ? 39.373 -4.535  -56.275  1.00 25.14 ? 26   ASN L O   1 
ATOM   11328 C  CB  . ASN K  1 26  ? 37.660 -4.466  -58.538  1.00 25.49 ? 26   ASN L CB  1 
ATOM   11329 C  CG  . ASN K  1 26  ? 37.131 -5.877  -58.252  1.00 26.26 ? 26   ASN L CG  1 
ATOM   11330 O  OD1 . ASN K  1 26  ? 37.833 -6.870  -58.440  1.00 25.31 ? 26   ASN L OD1 1 
ATOM   11331 N  ND2 . ASN K  1 26  ? 35.884 -5.962  -57.792  1.00 27.69 ? 26   ASN L ND2 1 
ATOM   11332 N  N   . GLY K  1 27  ? 40.940 -5.626  -57.462  1.00 23.63 ? 27   GLY L N   1 
ATOM   11333 C  CA  . GLY K  1 27  ? 41.506 -6.293  -56.298  1.00 21.91 ? 27   GLY L CA  1 
ATOM   11334 C  C   . GLY K  1 27  ? 42.894 -5.842  -55.871  1.00 20.38 ? 27   GLY L C   1 
ATOM   11335 O  O   . GLY K  1 27  ? 43.558 -5.072  -56.569  1.00 19.80 ? 27   GLY L O   1 
ATOM   11336 N  N   . PRO K  1 28  ? 43.331 -6.312  -54.695  1.00 19.98 ? 28   PRO L N   1 
ATOM   11337 C  CA  . PRO K  1 28  ? 44.644 -5.939  -54.150  1.00 19.27 ? 28   PRO L CA  1 
ATOM   11338 C  C   . PRO K  1 28  ? 45.777 -6.418  -55.047  1.00 18.31 ? 28   PRO L C   1 
ATOM   11339 O  O   . PRO K  1 28  ? 45.616 -7.402  -55.791  1.00 18.44 ? 28   PRO L O   1 
ATOM   11340 C  CB  . PRO K  1 28  ? 44.704 -6.682  -52.805  1.00 19.27 ? 28   PRO L CB  1 
ATOM   11341 C  CG  . PRO K  1 28  ? 43.331 -7.053  -52.481  1.00 19.99 ? 28   PRO L CG  1 
ATOM   11342 C  CD  . PRO K  1 28  ? 42.556 -7.156  -53.769  1.00 19.79 ? 28   PRO L CD  1 
ATOM   11343 N  N   . VAL K  1 29  ? 46.910 -5.730  -54.976  1.00 17.63 ? 29   VAL L N   1 
ATOM   11344 C  CA  . VAL K  1 29  ? 48.129 -6.172  -55.652  1.00 16.79 ? 29   VAL L CA  1 
ATOM   11345 C  C   . VAL K  1 29  ? 49.091 -6.688  -54.601  1.00 17.60 ? 29   VAL L C   1 
ATOM   11346 O  O   . VAL K  1 29  ? 49.453 -5.942  -53.678  1.00 16.49 ? 29   VAL L O   1 
ATOM   11347 C  CB  . VAL K  1 29  ? 48.822 -5.016  -56.413  1.00 16.17 ? 29   VAL L CB  1 
ATOM   11348 C  CG1 . VAL K  1 29  ? 50.132 -5.485  -57.066  1.00 16.02 ? 29   VAL L CG1 1 
ATOM   11349 C  CG2 . VAL K  1 29  ? 47.923 -4.435  -57.452  1.00 14.98 ? 29   VAL L CG2 1 
ATOM   11350 N  N   . LYS K  1 30  ? 49.501 -7.955  -54.732  1.00 17.57 ? 30   LYS L N   1 
ATOM   11351 C  CA  . LYS K  1 30  ? 50.579 -8.528  -53.906  1.00 18.13 ? 30   LYS L CA  1 
ATOM   11352 C  C   . LYS K  1 30  ? 51.941 -8.048  -54.405  1.00 17.53 ? 30   LYS L C   1 
ATOM   11353 O  O   . LYS K  1 30  ? 52.204 -8.040  -55.615  1.00 17.06 ? 30   LYS L O   1 
ATOM   11354 C  CB  . LYS K  1 30  ? 50.548 -10.062 -53.928  1.00 19.18 ? 30   LYS L CB  1 
ATOM   11355 C  CG  . LYS K  1 30  ? 49.469 -10.689 -53.056  1.00 22.71 ? 30   LYS L CG  1 
ATOM   11356 C  CD  . LYS K  1 30  ? 49.803 -12.154 -52.701  1.00 28.56 ? 30   LYS L CD  1 
ATOM   11357 C  CE  . LYS K  1 30  ? 49.171 -13.163 -53.675  1.00 30.83 ? 30   LYS L CE  1 
ATOM   11358 N  NZ  . LYS K  1 30  ? 47.715 -13.383 -53.424  1.00 33.04 ? 30   LYS L NZ  1 
ATOM   11359 N  N   . VAL K  1 31  ? 52.804 -7.648  -53.467  1.00 16.64 ? 31   VAL L N   1 
ATOM   11360 C  CA  . VAL K  1 31  ? 54.151 -7.171  -53.769  1.00 16.67 ? 31   VAL L CA  1 
ATOM   11361 C  C   . VAL K  1 31  ? 55.117 -7.985  -52.903  1.00 16.71 ? 31   VAL L C   1 
ATOM   11362 O  O   . VAL K  1 31  ? 54.969 -8.050  -51.682  1.00 16.74 ? 31   VAL L O   1 
ATOM   11363 C  CB  . VAL K  1 31  ? 54.305 -5.648  -53.467  1.00 16.19 ? 31   VAL L CB  1 
ATOM   11364 C  CG1 . VAL K  1 31  ? 55.594 -5.108  -54.037  1.00 16.07 ? 31   VAL L CG1 1 
ATOM   11365 C  CG2 . VAL K  1 31  ? 53.127 -4.850  -54.028  1.00 15.89 ? 31   VAL L CG2 1 
ATOM   11366 N  N   . TRP K  1 32  ? 56.084 -8.650  -53.531  1.00 17.34 ? 32   TRP L N   1 
ATOM   11367 C  CA  . TRP K  1 32  ? 56.970 -9.521  -52.779  1.00 17.43 ? 32   TRP L CA  1 
ATOM   11368 C  C   . TRP K  1 32  ? 58.298 -9.745  -53.477  1.00 16.92 ? 32   TRP L C   1 
ATOM   11369 O  O   . TRP K  1 32  ? 58.375 -9.775  -54.704  1.00 16.82 ? 32   TRP L O   1 
ATOM   11370 C  CB  . TRP K  1 32  ? 56.300 -10.855 -52.436  1.00 18.21 ? 32   TRP L CB  1 
ATOM   11371 C  CG  . TRP K  1 32  ? 56.339 -11.876 -53.541  1.00 21.15 ? 32   TRP L CG  1 
ATOM   11372 C  CD1 . TRP K  1 32  ? 57.228 -12.915 -53.677  1.00 24.40 ? 32   TRP L CD1 1 
ATOM   11373 C  CD2 . TRP K  1 32  ? 55.458 -11.956 -54.665  1.00 24.25 ? 32   TRP L CD2 1 
ATOM   11374 N  NE1 . TRP K  1 32  ? 56.953 -13.632 -54.814  1.00 24.64 ? 32   TRP L NE1 1 
ATOM   11375 C  CE2 . TRP K  1 32  ? 55.873 -13.068 -55.444  1.00 24.84 ? 32   TRP L CE2 1 
ATOM   11376 C  CE3 . TRP K  1 32  ? 54.357 -11.198 -55.095  1.00 24.41 ? 32   TRP L CE3 1 
ATOM   11377 C  CZ2 . TRP K  1 32  ? 55.221 -13.444 -56.630  1.00 24.87 ? 32   TRP L CZ2 1 
ATOM   11378 C  CZ3 . TRP K  1 32  ? 53.715 -11.565 -56.284  1.00 25.95 ? 32   TRP L CZ3 1 
ATOM   11379 C  CH2 . TRP K  1 32  ? 54.149 -12.686 -57.033  1.00 25.94 ? 32   TRP L CH2 1 
ATOM   11380 N  N   . GLY K  1 33  ? 59.338 -9.898  -52.675  1.00 16.46 ? 33   GLY L N   1 
ATOM   11381 C  CA  . GLY K  1 33  ? 60.670 -10.154 -53.207  1.00 16.80 ? 33   GLY L CA  1 
ATOM   11382 C  C   . GLY K  1 33  ? 61.723 -9.981  -52.147  1.00 16.16 ? 33   GLY L C   1 
ATOM   11383 O  O   . GLY K  1 33  ? 61.430 -10.032 -50.958  1.00 17.01 ? 33   GLY L O   1 
ATOM   11384 N  N   . SER K  1 34  ? 62.952 -9.779  -52.592  1.00 16.14 ? 34   SER L N   1 
ATOM   11385 C  CA  . SER K  1 34  ? 64.097 -9.656  -51.701  1.00 17.03 ? 34   SER L CA  1 
ATOM   11386 C  C   . SER K  1 34  ? 64.887 -8.430  -52.154  1.00 16.01 ? 34   SER L C   1 
ATOM   11387 O  O   . SER K  1 34  ? 65.018 -8.192  -53.359  1.00 16.20 ? 34   SER L O   1 
ATOM   11388 C  CB  . SER K  1 34  ? 64.969 -10.914 -51.811  1.00 17.02 ? 34   SER L CB  1 
ATOM   11389 O  OG  . SER K  1 34  ? 66.125 -10.833 -50.986  1.00 20.70 ? 34   SER L OG  1 
ATOM   11390 N  N   . ILE K  1 35  ? 65.401 -7.654  -51.201  1.00 14.87 ? 35   ILE L N   1 
ATOM   11391 C  CA  . ILE K  1 35  ? 66.301 -6.538  -51.525  1.00 13.89 ? 35   ILE L CA  1 
ATOM   11392 C  C   . ILE K  1 35  ? 67.522 -6.645  -50.611  1.00 13.51 ? 35   ILE L C   1 
ATOM   11393 O  O   . ILE K  1 35  ? 67.373 -6.735  -49.393  1.00 13.11 ? 35   ILE L O   1 
ATOM   11394 C  CB  . ILE K  1 35  ? 65.666 -5.139  -51.296  1.00 14.72 ? 35   ILE L CB  1 
ATOM   11395 C  CG1 . ILE K  1 35  ? 64.273 -5.021  -51.923  1.00 14.24 ? 35   ILE L CG1 1 
ATOM   11396 C  CG2 . ILE K  1 35  ? 66.646 -4.025  -51.768  1.00 14.20 ? 35   ILE L CG2 1 
ATOM   11397 C  CD1 . ILE K  1 35  ? 63.574 -3.650  -51.691  1.00 14.96 ? 35   ILE L CD1 1 
ATOM   11398 N  N   . LYS K  1 36  ? 68.720 -6.628  -51.192  1.00 11.97 ? 36   LYS L N   1 
ATOM   11399 C  CA  . LYS K  1 36  ? 69.947 -6.749  -50.395  1.00 11.92 ? 36   LYS L CA  1 
ATOM   11400 C  C   . LYS K  1 36  ? 70.824 -5.499  -50.498  1.00 10.94 ? 36   LYS L C   1 
ATOM   11401 O  O   . LYS K  1 36  ? 70.581 -4.633  -51.332  1.00 10.49 ? 36   LYS L O   1 
ATOM   11402 C  CB  . LYS K  1 36  ? 70.735 -8.015  -50.784  1.00 11.84 ? 36   LYS L CB  1 
ATOM   11403 C  CG  . LYS K  1 36  ? 71.070 -8.155  -52.276  1.00 14.55 ? 36   LYS L CG  1 
ATOM   11404 C  CD  . LYS K  1 36  ? 71.605 -9.572  -52.535  1.00 19.99 ? 36   LYS L CD  1 
ATOM   11405 C  CE  . LYS K  1 36  ? 72.320 -9.672  -53.846  1.00 21.97 ? 36   LYS L CE  1 
ATOM   11406 N  NZ  . LYS K  1 36  ? 72.488 -11.109 -54.224  1.00 26.20 ? 36   LYS L NZ  1 
ATOM   11407 N  N   . GLY K  1 37  ? 71.853 -5.411  -49.653  1.00 10.07 ? 37   GLY L N   1 
ATOM   11408 C  CA  . GLY K  1 37  ? 72.790 -4.282  -49.726  1.00 9.92  ? 37   GLY L CA  1 
ATOM   11409 C  C   . GLY K  1 37  ? 72.314 -3.049  -48.977  1.00 9.08  ? 37   GLY L C   1 
ATOM   11410 O  O   . GLY K  1 37  ? 72.916 -1.982  -49.099  1.00 9.27  ? 37   GLY L O   1 
ATOM   11411 N  N   . LEU K  1 38  ? 71.242 -3.211  -48.197  1.00 9.44  ? 38   LEU L N   1 
ATOM   11412 C  CA  . LEU K  1 38  ? 70.640 -2.132  -47.388  1.00 9.36  ? 38   LEU L CA  1 
ATOM   11413 C  C   . LEU K  1 38  ? 71.246 -2.006  -45.999  1.00 9.70  ? 38   LEU L C   1 
ATOM   11414 O  O   . LEU K  1 38  ? 71.606 -3.011  -45.380  1.00 10.39 ? 38   LEU L O   1 
ATOM   11415 C  CB  . LEU K  1 38  ? 69.127 -2.365  -47.237  1.00 8.96  ? 38   LEU L CB  1 
ATOM   11416 C  CG  . LEU K  1 38  ? 68.282 -2.223  -48.509  1.00 10.88 ? 38   LEU L CG  1 
ATOM   11417 C  CD1 . LEU K  1 38  ? 66.890 -2.843  -48.330  1.00 10.29 ? 38   LEU L CD1 1 
ATOM   11418 C  CD2 . LEU K  1 38  ? 68.172 -0.745  -48.964  1.00 9.76  ? 38   LEU L CD2 1 
ATOM   11419 N  N   . THR K  1 39  ? 71.332 -0.773  -45.496  1.00 10.81 ? 39   THR L N   1 
ATOM   11420 C  CA  . THR K  1 39  ? 71.604 -0.565  -44.071  1.00 11.39 ? 39   THR L CA  1 
ATOM   11421 C  C   . THR K  1 39  ? 70.464 -1.138  -43.239  1.00 12.04 ? 39   THR L C   1 
ATOM   11422 O  O   . THR K  1 39  ? 69.301 -1.071  -43.615  1.00 11.02 ? 39   THR L O   1 
ATOM   11423 C  CB  . THR K  1 39  ? 71.871 0.906   -43.685  1.00 11.69 ? 39   THR L CB  1 
ATOM   11424 O  OG1 . THR K  1 39  ? 70.739 1.722   -44.054  1.00 14.14 ? 39   THR L OG1 1 
ATOM   11425 C  CG2 . THR K  1 39  ? 73.131 1.406   -44.365  1.00 10.72 ? 39   THR L CG2 1 
ATOM   11426 N  N   . GLU K  1 40  ? 70.821 -1.754  -42.121  1.00 12.13 ? 40   GLU L N   1 
ATOM   11427 C  CA  . GLU K  1 40  ? 69.828 -2.305  -41.229  1.00 12.79 ? 40   GLU L CA  1 
ATOM   11428 C  C   . GLU K  1 40  ? 68.790 -1.245  -40.826  1.00 12.39 ? 40   GLU L C   1 
ATOM   11429 O  O   . GLU K  1 40  ? 69.128 -0.109  -40.471  1.00 12.44 ? 40   GLU L O   1 
ATOM   11430 C  CB  . GLU K  1 40  ? 70.517 -2.875  -39.987  1.00 13.54 ? 40   GLU L CB  1 
ATOM   11431 C  CG  . GLU K  1 40  ? 69.581 -3.489  -38.980  1.00 15.32 ? 40   GLU L CG  1 
ATOM   11432 C  CD  . GLU K  1 40  ? 70.335 -4.054  -37.793  1.00 21.27 ? 40   GLU L CD  1 
ATOM   11433 O  OE1 . GLU K  1 40  ? 69.688 -4.662  -36.917  1.00 23.52 ? 40   GLU L OE1 1 
ATOM   11434 O  OE2 . GLU K  1 40  ? 71.582 -3.890  -37.746  1.00 25.20 ? 40   GLU L OE2 1 
ATOM   11435 N  N   . GLY K  1 41  ? 67.524 -1.623  -40.911  1.00 12.27 ? 41   GLY L N   1 
ATOM   11436 C  CA  . GLY K  1 41  ? 66.448 -0.734  -40.503  1.00 11.84 ? 41   GLY L CA  1 
ATOM   11437 C  C   . GLY K  1 41  ? 65.487 -0.421  -41.630  1.00 11.44 ? 41   GLY L C   1 
ATOM   11438 O  O   . GLY K  1 41  ? 65.419 -1.135  -42.638  1.00 11.82 ? 41   GLY L O   1 
ATOM   11439 N  N   . LEU K  1 42  ? 64.717 0.641   -41.432  1.00 10.52 ? 42   LEU L N   1 
ATOM   11440 C  CA  . LEU K  1 42  ? 63.615 0.997   -42.320  1.00 9.69  ? 42   LEU L CA  1 
ATOM   11441 C  C   . LEU K  1 42  ? 64.097 1.797   -43.547  1.00 8.37  ? 42   LEU L C   1 
ATOM   11442 O  O   . LEU K  1 42  ? 64.986 2.661   -43.442  1.00 8.48  ? 42   LEU L O   1 
ATOM   11443 C  CB  . LEU K  1 42  ? 62.590 1.824   -41.537  1.00 10.02 ? 42   LEU L CB  1 
ATOM   11444 C  CG  . LEU K  1 42  ? 61.706 1.152   -40.470  1.00 11.70 ? 42   LEU L CG  1 
ATOM   11445 C  CD1 . LEU K  1 42  ? 61.041 2.213   -39.579  1.00 13.02 ? 42   LEU L CD1 1 
ATOM   11446 C  CD2 . LEU K  1 42  ? 60.649 0.235   -41.071  1.00 11.90 ? 42   LEU L CD2 1 
ATOM   11447 N  N   . HIS K  1 43  ? 63.505 1.505   -44.697  1.00 8.35  ? 43   HIS L N   1 
ATOM   11448 C  CA  . HIS K  1 43  ? 63.770 2.222   -45.966  1.00 7.68  ? 43   HIS L CA  1 
ATOM   11449 C  C   . HIS K  1 43  ? 62.494 2.468   -46.720  1.00 6.67  ? 43   HIS L C   1 
ATOM   11450 O  O   . HIS K  1 43  ? 61.697 1.542   -46.907  1.00 6.07  ? 43   HIS L O   1 
ATOM   11451 C  CB  . HIS K  1 43  ? 64.747 1.434   -46.855  1.00 8.13  ? 43   HIS L CB  1 
ATOM   11452 C  CG  . HIS K  1 43  ? 66.091 1.229   -46.223  1.00 8.49  ? 43   HIS L CG  1 
ATOM   11453 N  ND1 . HIS K  1 43  ? 67.152 2.083   -46.438  1.00 9.31  ? 43   HIS L ND1 1 
ATOM   11454 C  CD2 . HIS K  1 43  ? 66.525 0.303   -45.336  1.00 8.95  ? 43   HIS L CD2 1 
ATOM   11455 C  CE1 . HIS K  1 43  ? 68.192 1.674   -45.730  1.00 9.05  ? 43   HIS L CE1 1 
ATOM   11456 N  NE2 . HIS K  1 43  ? 67.834 0.604   -45.043  1.00 9.13  ? 43   HIS L NE2 1 
ATOM   11457 N  N   . GLY K  1 44  ? 62.297 3.722   -47.151  1.00 6.25  ? 44   GLY L N   1 
ATOM   11458 C  CA  . GLY K  1 44  ? 61.113 4.124   -47.921  1.00 5.61  ? 44   GLY L CA  1 
ATOM   11459 C  C   . GLY K  1 44  ? 61.031 3.376   -49.254  1.00 6.34  ? 44   GLY L C   1 
ATOM   11460 O  O   . GLY K  1 44  ? 62.065 3.036   -49.845  1.00 5.64  ? 44   GLY L O   1 
ATOM   11461 N  N   . PHE K  1 45  ? 59.806 3.129   -49.715  1.00 5.98  ? 45   PHE L N   1 
ATOM   11462 C  CA  . PHE K  1 45  ? 59.542 2.214   -50.814  1.00 6.81  ? 45   PHE L CA  1 
ATOM   11463 C  C   . PHE K  1 45  ? 58.331 2.732   -51.576  1.00 6.90  ? 45   PHE L C   1 
ATOM   11464 O  O   . PHE K  1 45  ? 57.208 2.691   -51.054  1.00 6.80  ? 45   PHE L O   1 
ATOM   11465 C  CB  . PHE K  1 45  ? 59.231 0.853   -50.205  1.00 6.47  ? 45   PHE L CB  1 
ATOM   11466 C  CG  . PHE K  1 45  ? 59.220 -0.284  -51.192  1.00 7.67  ? 45   PHE L CG  1 
ATOM   11467 C  CD1 . PHE K  1 45  ? 60.295 -0.499  -52.027  1.00 7.97  ? 45   PHE L CD1 1 
ATOM   11468 C  CD2 . PHE K  1 45  ? 58.129 -1.172  -51.230  1.00 8.84  ? 45   PHE L CD2 1 
ATOM   11469 C  CE1 . PHE K  1 45  ? 60.296 -1.575  -52.920  1.00 9.55  ? 45   PHE L CE1 1 
ATOM   11470 C  CE2 . PHE K  1 45  ? 58.113 -2.247  -52.113  1.00 11.53 ? 45   PHE L CE2 1 
ATOM   11471 C  CZ  . PHE K  1 45  ? 59.201 -2.455  -52.954  1.00 10.19 ? 45   PHE L CZ  1 
ATOM   11472 N  N   . HIS K  1 46  ? 58.551 3.285   -52.770  1.00 8.14  ? 46   HIS L N   1 
ATOM   11473 C  CA  . HIS K  1 46  ? 57.447 3.907   -53.512  1.00 8.29  ? 46   HIS L CA  1 
ATOM   11474 C  C   . HIS K  1 46  ? 57.524 3.636   -55.001  1.00 9.40  ? 46   HIS L C   1 
ATOM   11475 O  O   . HIS K  1 46  ? 58.609 3.321   -55.535  1.00 10.03 ? 46   HIS L O   1 
ATOM   11476 C  CB  . HIS K  1 46  ? 57.401 5.437   -53.312  1.00 8.11  ? 46   HIS L CB  1 
ATOM   11477 C  CG  . HIS K  1 46  ? 57.890 5.901   -51.971  1.00 7.71  ? 46   HIS L CG  1 
ATOM   11478 N  ND1 . HIS K  1 46  ? 59.031 6.667   -51.822  1.00 9.05  ? 46   HIS L ND1 1 
ATOM   11479 C  CD2 . HIS K  1 46  ? 57.386 5.733   -50.723  1.00 5.98  ? 46   HIS L CD2 1 
ATOM   11480 C  CE1 . HIS K  1 46  ? 59.214 6.940   -50.539  1.00 8.41  ? 46   HIS L CE1 1 
ATOM   11481 N  NE2 . HIS K  1 46  ? 58.233 6.380   -49.847  1.00 6.45  ? 46   HIS L NE2 1 
ATOM   11482 N  N   . VAL K  1 47  ? 56.374 3.797   -55.666  1.00 8.21  ? 47   VAL L N   1 
ATOM   11483 C  CA  . VAL K  1 47  ? 56.336 3.902   -57.127  1.00 8.29  ? 47   VAL L CA  1 
ATOM   11484 C  C   . VAL K  1 47  ? 56.413 5.375   -57.503  1.00 8.19  ? 47   VAL L C   1 
ATOM   11485 O  O   . VAL K  1 47  ? 55.613 6.183   -57.033  1.00 9.07  ? 47   VAL L O   1 
ATOM   11486 C  CB  . VAL K  1 47  ? 55.055 3.284   -57.722  1.00 8.54  ? 47   VAL L CB  1 
ATOM   11487 C  CG1 . VAL K  1 47  ? 55.110 3.320   -59.252  1.00 7.53  ? 47   VAL L CG1 1 
ATOM   11488 C  CG2 . VAL K  1 47  ? 54.896 1.865   -57.255  1.00 6.92  ? 47   VAL L CG2 1 
ATOM   11489 N  N   . HIS K  1 48  ? 57.389 5.713   -58.336  1.00 8.11  ? 48   HIS L N   1 
ATOM   11490 C  CA  . HIS K  1 48  ? 57.549 7.061   -58.851  1.00 8.96  ? 48   HIS L CA  1 
ATOM   11491 C  C   . HIS K  1 48  ? 56.918 7.182   -60.250  1.00 10.40 ? 48   HIS L C   1 
ATOM   11492 O  O   . HIS K  1 48  ? 56.657 6.175   -60.896  1.00 11.57 ? 48   HIS L O   1 
ATOM   11493 C  CB  . HIS K  1 48  ? 59.021 7.469   -58.848  1.00 8.05  ? 48   HIS L CB  1 
ATOM   11494 C  CG  . HIS K  1 48  ? 59.563 7.749   -57.481  1.00 6.61  ? 48   HIS L CG  1 
ATOM   11495 N  ND1 . HIS K  1 48  ? 60.092 8.969   -57.126  1.00 6.28  ? 48   HIS L ND1 1 
ATOM   11496 C  CD2 . HIS K  1 48  ? 59.632 6.974   -56.373  1.00 9.27  ? 48   HIS L CD2 1 
ATOM   11497 C  CE1 . HIS K  1 48  ? 60.483 8.931   -55.865  1.00 8.30  ? 48   HIS L CE1 1 
ATOM   11498 N  NE2 . HIS K  1 48  ? 60.219 7.729   -55.387  1.00 7.54  ? 48   HIS L NE2 1 
ATOM   11499 N  N   . GLU K  1 49  ? 56.681 8.411   -60.684  1.00 11.90 ? 49   GLU L N   1 
ATOM   11500 C  CA  . GLU K  1 49  ? 55.762 8.718   -61.785  1.00 13.84 ? 49   GLU L CA  1 
ATOM   11501 C  C   . GLU K  1 49  ? 56.275 8.273   -63.158  1.00 14.86 ? 49   GLU L C   1 
ATOM   11502 O  O   . GLU K  1 49  ? 55.527 7.701   -63.945  1.00 14.85 ? 49   GLU L O   1 
ATOM   11503 C  CB  . GLU K  1 49  ? 55.428 10.215  -61.783  1.00 14.38 ? 49   GLU L CB  1 
ATOM   11504 C  CG  . GLU K  1 49  ? 54.516 10.669  -62.945  1.00 15.37 ? 49   GLU L CG  1 
ATOM   11505 C  CD  . GLU K  1 49  ? 54.231 12.166  -62.946  1.00 18.86 ? 49   GLU L CD  1 
ATOM   11506 O  OE1 . GLU K  1 49  ? 53.380 12.617  -63.742  1.00 20.61 ? 49   GLU L OE1 1 
ATOM   11507 O  OE2 . GLU K  1 49  ? 54.856 12.909  -62.169  1.00 20.17 ? 49   GLU L OE2 1 
ATOM   11508 N  N   . PHE K  1 50  ? 57.551 8.525   -63.431  1.00 16.24 ? 50   PHE L N   1 
ATOM   11509 C  CA  . PHE K  1 50  ? 58.115 8.198   -64.749  1.00 17.84 ? 50   PHE L CA  1 
ATOM   11510 C  C   . PHE K  1 50  ? 58.994 6.948   -64.750  1.00 19.07 ? 50   PHE L C   1 
ATOM   11511 O  O   . PHE K  1 50  ? 59.823 6.750   -63.854  1.00 18.76 ? 50   PHE L O   1 
ATOM   11512 C  CB  . PHE K  1 50  ? 58.863 9.399   -65.305  1.00 17.22 ? 50   PHE L CB  1 
ATOM   11513 C  CG  . PHE K  1 50  ? 58.064 10.668  -65.266  1.00 18.50 ? 50   PHE L CG  1 
ATOM   11514 C  CD1 . PHE K  1 50  ? 56.836 10.765  -65.936  1.00 18.84 ? 50   PHE L CD1 1 
ATOM   11515 C  CD2 . PHE K  1 50  ? 58.531 11.770  -64.557  1.00 18.08 ? 50   PHE L CD2 1 
ATOM   11516 C  CE1 . PHE K  1 50  ? 56.086 11.950  -65.889  1.00 18.72 ? 50   PHE L CE1 1 
ATOM   11517 C  CE2 . PHE K  1 50  ? 57.787 12.957  -64.512  1.00 19.52 ? 50   PHE L CE2 1 
ATOM   11518 C  CZ  . PHE K  1 50  ? 56.568 13.043  -65.176  1.00 17.79 ? 50   PHE L CZ  1 
ATOM   11519 N  N   . GLY K  1 51  ? 58.790 6.094   -65.751  1.00 20.52 ? 51   GLY L N   1 
ATOM   11520 C  CA  . GLY K  1 51  ? 59.661 4.955   -65.983  1.00 22.18 ? 51   GLY L CA  1 
ATOM   11521 C  C   . GLY K  1 51  ? 60.867 5.421   -66.778  1.00 23.87 ? 51   GLY L C   1 
ATOM   11522 O  O   . GLY K  1 51  ? 61.275 4.767   -67.745  1.00 24.15 ? 51   GLY L O   1 
ATOM   11523 N  N   . ASP K  1 52  ? 61.429 6.559   -66.365  1.00 24.69 ? 52   ASP L N   1 
ATOM   11524 C  CA  . ASP K  1 52  ? 62.568 7.186   -67.038  1.00 25.32 ? 52   ASP L CA  1 
ATOM   11525 C  C   . ASP K  1 52  ? 63.820 7.097   -66.178  1.00 25.71 ? 52   ASP L C   1 
ATOM   11526 O  O   . ASP K  1 52  ? 63.981 7.844   -65.214  1.00 25.36 ? 52   ASP L O   1 
ATOM   11527 C  CB  . ASP K  1 52  ? 62.253 8.651   -67.371  1.00 25.67 ? 52   ASP L CB  1 
ATOM   11528 C  CG  . ASP K  1 52  ? 63.396 9.363   -68.105  1.00 27.12 ? 52   ASP L CG  1 
ATOM   11529 O  OD1 . ASP K  1 52  ? 63.187 10.511  -68.562  1.00 28.11 ? 52   ASP L OD1 1 
ATOM   11530 O  OD2 . ASP K  1 52  ? 64.508 8.800   -68.206  1.00 27.20 ? 52   ASP L OD2 1 
ATOM   11531 N  N   . ASN K  1 53  ? 64.715 6.187   -66.542  1.00 26.13 ? 53   ASN L N   1 
ATOM   11532 C  CA  . ASN K  1 53  ? 65.967 6.036   -65.813  1.00 26.82 ? 53   ASN L CA  1 
ATOM   11533 C  C   . ASN K  1 53  ? 67.185 6.449   -66.642  1.00 26.94 ? 53   ASN L C   1 
ATOM   11534 O  O   . ASN K  1 53  ? 68.269 5.870   -66.494  1.00 27.21 ? 53   ASN L O   1 
ATOM   11535 C  CB  . ASN K  1 53  ? 66.097 4.616   -65.248  1.00 27.20 ? 53   ASN L CB  1 
ATOM   11536 C  CG  . ASN K  1 53  ? 65.048 4.307   -64.142  1.00 28.38 ? 53   ASN L CG  1 
ATOM   11537 O  OD1 . ASN K  1 53  ? 64.768 3.139   -63.849  1.00 29.11 ? 53   ASN L OD1 1 
ATOM   11538 N  ND2 . ASN K  1 53  ? 64.476 5.353   -63.536  1.00 28.20 ? 53   ASN L ND2 1 
ATOM   11539 N  N   . THR K  1 54  ? 67.001 7.467   -67.493  1.00 26.86 ? 54   THR L N   1 
ATOM   11540 C  CA  . THR K  1 54  ? 68.100 8.019   -68.307  1.00 26.68 ? 54   THR L CA  1 
ATOM   11541 C  C   . THR K  1 54  ? 69.157 8.704   -67.457  1.00 26.10 ? 54   THR L C   1 
ATOM   11542 O  O   . THR K  1 54  ? 70.338 8.679   -67.802  1.00 26.00 ? 54   THR L O   1 
ATOM   11543 C  CB  . THR K  1 54  ? 67.650 9.043   -69.392  1.00 26.83 ? 54   THR L CB  1 
ATOM   11544 O  OG1 . THR K  1 54  ? 67.217 10.264  -68.779  1.00 27.74 ? 54   THR L OG1 1 
ATOM   11545 C  CG2 . THR K  1 54  ? 66.567 8.491   -70.292  1.00 26.91 ? 54   THR L CG2 1 
ATOM   11546 N  N   . ALA K  1 55  ? 68.729 9.344   -66.371  1.00 25.03 ? 55   ALA L N   1 
ATOM   11547 C  CA  . ALA K  1 55  ? 69.666 9.954   -65.438  1.00 24.25 ? 55   ALA L CA  1 
ATOM   11548 C  C   . ALA K  1 55  ? 69.673 9.227   -64.093  1.00 23.22 ? 55   ALA L C   1 
ATOM   11549 O  O   . ALA K  1 55  ? 69.695 9.858   -63.039  1.00 23.84 ? 55   ALA L O   1 
ATOM   11550 C  CB  . ALA K  1 55  ? 69.360 11.446  -65.270  1.00 24.00 ? 55   ALA L CB  1 
ATOM   11551 N  N   . GLY K  1 56  ? 69.665 7.897   -64.136  1.00 22.17 ? 56   GLY L N   1 
ATOM   11552 C  CA  . GLY K  1 56  ? 69.592 7.089   -62.919  1.00 20.48 ? 56   GLY L CA  1 
ATOM   11553 C  C   . GLY K  1 56  ? 68.197 7.187   -62.327  1.00 19.45 ? 56   GLY L C   1 
ATOM   11554 O  O   . GLY K  1 56  ? 67.216 7.351   -63.057  1.00 19.83 ? 56   GLY L O   1 
ATOM   11555 N  N   . CYS K  1 57  ? 68.115 7.128   -61.004  1.00 17.82 ? 57   CYS L N   1 
ATOM   11556 C  CA  . CYS K  1 57  ? 66.827 7.166   -60.305  1.00 16.63 ? 57   CYS L CA  1 
ATOM   11557 C  C   . CYS K  1 57  ? 66.213 8.550   -60.263  1.00 16.84 ? 57   CYS L C   1 
ATOM   11558 O  O   . CYS K  1 57  ? 65.001 8.679   -60.102  1.00 17.29 ? 57   CYS L O   1 
ATOM   11559 C  CB  . CYS K  1 57  ? 66.983 6.581   -58.905  0.40 15.31 ? 57   CYS L CB  1 
ATOM   11560 S  SG  . CYS K  1 57  ? 67.466 4.848   -58.933  0.40 9.46  ? 57   CYS L SG  1 
ATOM   11561 N  N   . THR K  1 58  ? 67.050 9.576   -60.432  1.00 17.06 ? 58   THR L N   1 
ATOM   11562 C  CA  . THR K  1 58  ? 66.627 10.981  -60.426  1.00 17.68 ? 58   THR L CA  1 
ATOM   11563 C  C   . THR K  1 58  ? 65.558 11.299  -61.479  1.00 17.56 ? 58   THR L C   1 
ATOM   11564 O  O   . THR K  1 58  ? 64.677 12.139  -61.243  1.00 17.24 ? 58   THR L O   1 
ATOM   11565 C  CB  . THR K  1 58  ? 67.836 11.935  -60.635  1.00 17.85 ? 58   THR L CB  1 
ATOM   11566 O  OG1 . THR K  1 58  ? 68.908 11.549  -59.771  1.00 19.09 ? 58   THR L OG1 1 
ATOM   11567 C  CG2 . THR K  1 58  ? 67.463 13.391  -60.323  1.00 18.89 ? 58   THR L CG2 1 
ATOM   11568 N  N   . SER K  1 59  ? 65.630 10.624  -62.627  1.00 17.31 ? 59   SER L N   1 
ATOM   11569 C  CA  . SER K  1 59  ? 64.747 10.945  -63.752  1.00 17.33 ? 59   SER L CA  1 
ATOM   11570 C  C   . SER K  1 59  ? 63.394 10.237  -63.658  1.00 17.27 ? 59   SER L C   1 
ATOM   11571 O  O   . SER K  1 59  ? 62.520 10.391  -64.522  1.00 17.16 ? 59   SER L O   1 
ATOM   11572 C  CB  . SER K  1 59  ? 65.450 10.700  -65.096  1.00 17.27 ? 59   SER L CB  1 
ATOM   11573 O  OG  . SER K  1 59  ? 66.028 9.406   -65.158  1.00 18.84 ? 59   SER L OG  1 
ATOM   11574 N  N   . ALA K  1 60  ? 63.213 9.475   -62.582  1.00 16.63 ? 60   ALA L N   1 
ATOM   11575 C  CA  . ALA K  1 60  ? 61.902 8.918   -62.264  1.00 16.48 ? 60   ALA L CA  1 
ATOM   11576 C  C   . ALA K  1 60  ? 60.906 9.970   -61.776  1.00 15.89 ? 60   ALA L C   1 
ATOM   11577 O  O   . ALA K  1 60  ? 59.713 9.692   -61.711  1.00 16.25 ? 60   ALA L O   1 
ATOM   11578 C  CB  . ALA K  1 60  ? 62.029 7.808   -61.261  1.00 16.47 ? 60   ALA L CB  1 
ATOM   11579 N  N   . GLY K  1 61  ? 61.391 11.157  -61.422  1.00 15.03 ? 61   GLY L N   1 
ATOM   11580 C  CA  . GLY K  1 61  ? 60.522 12.240  -60.953  1.00 14.57 ? 61   GLY L CA  1 
ATOM   11581 C  C   . GLY K  1 61  ? 59.881 11.903  -59.608  1.00 14.14 ? 61   GLY L C   1 
ATOM   11582 O  O   . GLY K  1 61  ? 60.420 11.074  -58.860  1.00 13.74 ? 61   GLY L O   1 
ATOM   11583 N  N   . PRO K  1 62  ? 58.730 12.534  -59.295  1.00 13.47 ? 62   PRO L N   1 
ATOM   11584 C  CA  . PRO K  1 62  ? 58.169 12.395  -57.945  1.00 12.31 ? 62   PRO L CA  1 
ATOM   11585 C  C   . PRO K  1 62  ? 57.303 11.149  -57.745  1.00 11.07 ? 62   PRO L C   1 
ATOM   11586 O  O   . PRO K  1 62  ? 57.226 10.286  -58.632  1.00 10.53 ? 62   PRO L O   1 
ATOM   11587 C  CB  . PRO K  1 62  ? 57.371 13.687  -57.766  1.00 12.54 ? 62   PRO L CB  1 
ATOM   11588 C  CG  . PRO K  1 62  ? 56.892 14.027  -59.155  1.00 12.67 ? 62   PRO L CG  1 
ATOM   11589 C  CD  . PRO K  1 62  ? 57.998 13.542  -60.096  1.00 13.60 ? 62   PRO L CD  1 
ATOM   11590 N  N   . HIS K  1 63  ? 56.683 11.028  -56.568  1.00 9.71  ? 63   HIS L N   1 
ATOM   11591 C  CA  . HIS K  1 63  ? 55.854 9.872   -56.313  1.00 9.30  ? 63   HIS L CA  1 
ATOM   11592 C  C   . HIS K  1 63  ? 54.680 9.925   -57.291  1.00 8.92  ? 63   HIS L C   1 
ATOM   11593 O  O   . HIS K  1 63  ? 54.137 10.998  -57.592  1.00 10.26 ? 63   HIS L O   1 
ATOM   11594 C  CB  . HIS K  1 63  ? 55.373 9.797   -54.844  1.00 8.43  ? 63   HIS L CB  1 
ATOM   11595 C  CG  . HIS K  1 63  ? 56.485 9.640   -53.834  1.00 8.57  ? 63   HIS L CG  1 
ATOM   11596 N  ND1 . HIS K  1 63  ? 56.250 9.524   -52.479  1.00 6.25  ? 63   HIS L ND1 1 
ATOM   11597 C  CD2 . HIS K  1 63  ? 57.831 9.560   -53.983  1.00 6.41  ? 63   HIS L CD2 1 
ATOM   11598 C  CE1 . HIS K  1 63  ? 57.400 9.430   -51.834  1.00 4.61  ? 63   HIS L CE1 1 
ATOM   11599 N  NE2 . HIS K  1 63  ? 58.374 9.448   -52.726  1.00 6.42  ? 63   HIS L NE2 1 
ATOM   11600 N  N   . PHE K  1 64  ? 54.311 8.759   -57.783  1.00 9.18  ? 64   PHE L N   1 
ATOM   11601 C  CA  . PHE K  1 64  ? 53.138 8.593   -58.637  1.00 9.33  ? 64   PHE L CA  1 
ATOM   11602 C  C   . PHE K  1 64  ? 51.888 9.005   -57.866  1.00 10.24 ? 64   PHE L C   1 
ATOM   11603 O  O   . PHE K  1 64  ? 51.562 8.421   -56.825  1.00 9.66  ? 64   PHE L O   1 
ATOM   11604 C  CB  . PHE K  1 64  ? 53.044 7.148   -59.093  1.00 9.02  ? 64   PHE L CB  1 
ATOM   11605 C  CG  . PHE K  1 64  ? 51.872 6.867   -60.012  1.00 9.38  ? 64   PHE L CG  1 
ATOM   11606 C  CD1 . PHE K  1 64  ? 51.101 5.727   -59.828  1.00 9.43  ? 64   PHE L CD1 1 
ATOM   11607 C  CD2 . PHE K  1 64  ? 51.564 7.734   -61.065  1.00 8.84  ? 64   PHE L CD2 1 
ATOM   11608 C  CE1 . PHE K  1 64  ? 50.007 5.446   -60.686  1.00 8.79  ? 64   PHE L CE1 1 
ATOM   11609 C  CE2 . PHE K  1 64  ? 50.463 7.455   -61.934  1.00 9.83  ? 64   PHE L CE2 1 
ATOM   11610 C  CZ  . PHE K  1 64  ? 49.697 6.305   -61.719  1.00 9.00  ? 64   PHE L CZ  1 
ATOM   11611 N  N   . ASN K  1 65  ? 51.214 10.030  -58.382  1.00 10.88 ? 65   ASN L N   1 
ATOM   11612 C  CA  . ASN K  1 65  ? 50.190 10.755  -57.637  1.00 12.14 ? 65   ASN L CA  1 
ATOM   11613 C  C   . ASN K  1 65  ? 49.112 11.294  -58.575  1.00 12.94 ? 65   ASN L C   1 
ATOM   11614 O  O   . ASN K  1 65  ? 48.906 12.504  -58.638  1.00 13.62 ? 65   ASN L O   1 
ATOM   11615 C  CB  . ASN K  1 65  ? 50.846 11.915  -56.884  1.00 12.36 ? 65   ASN L CB  1 
ATOM   11616 C  CG  . ASN K  1 65  ? 49.898 12.622  -55.938  1.00 12.90 ? 65   ASN L CG  1 
ATOM   11617 O  OD1 . ASN K  1 65  ? 48.878 12.074  -55.509  1.00 14.49 ? 65   ASN L OD1 1 
ATOM   11618 N  ND2 . ASN K  1 65  ? 50.231 13.858  -55.616  1.00 13.10 ? 65   ASN L ND2 1 
ATOM   11619 N  N   . PRO K  1 66  ? 48.420 10.405  -59.292  1.00 13.95 ? 66   PRO L N   1 
ATOM   11620 C  CA  . PRO K  1 66  ? 47.422 10.862  -60.275  1.00 15.40 ? 66   PRO L CA  1 
ATOM   11621 C  C   . PRO K  1 66  ? 46.146 11.453  -59.645  1.00 16.85 ? 66   PRO L C   1 
ATOM   11622 O  O   . PRO K  1 66  ? 45.322 11.995  -60.373  1.00 16.99 ? 66   PRO L O   1 
ATOM   11623 C  CB  . PRO K  1 66  ? 47.061 9.575   -60.998  1.00 15.47 ? 66   PRO L CB  1 
ATOM   11624 C  CG  . PRO K  1 66  ? 47.171 8.533   -59.922  1.00 14.51 ? 66   PRO L CG  1 
ATOM   11625 C  CD  . PRO K  1 66  ? 48.427 8.931   -59.194  1.00 13.34 ? 66   PRO L CD  1 
ATOM   11626 N  N   . LEU K  1 67  ? 45.968 11.308  -58.327  1.00 17.82 ? 67   LEU L N   1 
ATOM   11627 C  CA  . LEU K  1 67  ? 44.813 11.903  -57.617  1.00 18.94 ? 67   LEU L CA  1 
ATOM   11628 C  C   . LEU K  1 67  ? 45.181 13.197  -56.908  1.00 19.06 ? 67   LEU L C   1 
ATOM   11629 O  O   . LEU K  1 67  ? 44.375 13.727  -56.133  1.00 19.23 ? 67   LEU L O   1 
ATOM   11630 C  CB  . LEU K  1 67  ? 44.177 10.923  -56.612  1.00 19.56 ? 67   LEU L CB  1 
ATOM   11631 C  CG  . LEU K  1 67  ? 43.655 9.553   -57.086  1.00 21.36 ? 67   LEU L CG  1 
ATOM   11632 C  CD1 . LEU K  1 67  ? 42.988 8.791   -55.927  1.00 23.25 ? 67   LEU L CD1 1 
ATOM   11633 C  CD2 . LEU K  1 67  ? 42.708 9.636   -58.294  1.00 24.89 ? 67   LEU L CD2 1 
ATOM   11634 N  N   . SER K  1 68  ? 46.395 13.687  -57.170  1.00 18.90 ? 68   SER L N   1 
ATOM   11635 C  CA  . SER K  1 68  ? 46.943 14.920  -56.569  1.00 19.82 ? 68   SER L CA  1 
ATOM   11636 C  C   . SER K  1 68  ? 46.751 15.054  -55.054  1.00 19.00 ? 68   SER L C   1 
ATOM   11637 O  O   . SER K  1 68  ? 46.236 16.065  -54.572  1.00 19.31 ? 68   SER L O   1 
ATOM   11638 C  CB  . SER K  1 68  ? 46.386 16.168  -57.262  1.00 20.25 ? 68   SER L CB  1 
ATOM   11639 O  OG  . SER K  1 68  ? 46.857 16.239  -58.591  1.00 23.81 ? 68   SER L OG  1 
ATOM   11640 N  N   . ARG K  1 69  ? 47.181 14.040  -54.313  1.00 17.70 ? 69   ARG L N   1 
ATOM   11641 C  CA  . ARG K  1 69  ? 47.064 14.052  -52.855  1.00 15.90 ? 69   ARG L CA  1 
ATOM   11642 C  C   . ARG K  1 69  ? 48.423 14.282  -52.204  1.00 15.05 ? 69   ARG L C   1 
ATOM   11643 O  O   . ARG K  1 69  ? 49.442 14.318  -52.887  1.00 14.44 ? 69   ARG L O   1 
ATOM   11644 C  CB  . ARG K  1 69  ? 46.397 12.763  -52.356  1.00 16.28 ? 69   ARG L CB  1 
ATOM   11645 C  CG  . ARG K  1 69  ? 44.932 12.651  -52.801  1.00 17.21 ? 69   ARG L CG  1 
ATOM   11646 C  CD  . ARG K  1 69  ? 44.198 11.465  -52.222  1.00 20.03 ? 69   ARG L CD  1 
ATOM   11647 N  NE  . ARG K  1 69  ? 42.797 11.444  -52.665  1.00 22.24 ? 69   ARG L NE  1 
ATOM   11648 C  CZ  . ARG K  1 69  ? 41.942 10.443  -52.461  1.00 25.05 ? 69   ARG L CZ  1 
ATOM   11649 N  NH1 . ARG K  1 69  ? 40.695 10.535  -52.908  1.00 26.76 ? 69   ARG L NH1 1 
ATOM   11650 N  NH2 . ARG K  1 69  ? 42.313 9.347   -51.813  1.00 26.41 ? 69   ARG L NH2 1 
ATOM   11651 N  N   . LYS K  1 70  ? 48.429 14.475  -50.890  1.00 13.34 ? 70   LYS L N   1 
ATOM   11652 C  CA  . LYS K  1 70  ? 49.674 14.635  -50.164  1.00 12.53 ? 70   LYS L CA  1 
ATOM   11653 C  C   . LYS K  1 70  ? 50.227 13.253  -49.841  1.00 10.90 ? 70   LYS L C   1 
ATOM   11654 O  O   . LYS K  1 70  ? 49.498 12.266  -49.869  1.00 10.07 ? 70   LYS L O   1 
ATOM   11655 C  CB  . LYS K  1 70  ? 49.458 15.460  -48.897  1.00 13.29 ? 70   LYS L CB  1 
ATOM   11656 C  CG  . LYS K  1 70  ? 49.239 16.946  -49.175  1.00 16.78 ? 70   LYS L CG  1 
ATOM   11657 C  CD  . LYS K  1 70  ? 48.713 17.655  -47.920  1.00 20.77 ? 70   LYS L CD  1 
ATOM   11658 C  CE  . LYS K  1 70  ? 48.378 19.126  -48.215  1.00 24.06 ? 70   LYS L CE  1 
ATOM   11659 N  NZ  . LYS K  1 70  ? 49.465 19.781  -49.025  1.00 25.38 ? 70   LYS L NZ  1 
ATOM   11660 N  N   . HIS K  1 71  ? 51.517 13.191  -49.541  1.00 9.09  ? 71   HIS L N   1 
ATOM   11661 C  CA  . HIS K  1 71  ? 52.161 11.938  -49.175  1.00 7.09  ? 71   HIS L CA  1 
ATOM   11662 C  C   . HIS K  1 71  ? 51.610 11.378  -47.862  1.00 6.43  ? 71   HIS L C   1 
ATOM   11663 O  O   . HIS K  1 71  ? 51.439 12.106  -46.900  1.00 7.00  ? 71   HIS L O   1 
ATOM   11664 C  CB  . HIS K  1 71  ? 53.667 12.185  -49.024  1.00 6.11  ? 71   HIS L CB  1 
ATOM   11665 C  CG  . HIS K  1 71  ? 54.439 10.979  -48.616  1.00 6.64  ? 71   HIS L CG  1 
ATOM   11666 N  ND1 . HIS K  1 71  ? 54.779 9.985   -49.502  1.00 5.59  ? 71   HIS L ND1 1 
ATOM   11667 C  CD2 . HIS K  1 71  ? 54.962 10.613  -47.419  1.00 6.56  ? 71   HIS L CD2 1 
ATOM   11668 C  CE1 . HIS K  1 71  ? 55.467 9.047   -48.871  1.00 6.89  ? 71   HIS L CE1 1 
ATOM   11669 N  NE2 . HIS K  1 71  ? 55.598 9.408   -47.608  1.00 5.61  ? 71   HIS L NE2 1 
ATOM   11670 N  N   . GLY K  1 72  ? 51.359 10.071  -47.831  1.00 6.35  ? 72   GLY L N   1 
ATOM   11671 C  CA  . GLY K  1 72  ? 51.033 9.365   -46.601  1.00 6.22  ? 72   GLY L CA  1 
ATOM   11672 C  C   . GLY K  1 72  ? 51.660 7.981   -46.559  1.00 6.54  ? 72   GLY L C   1 
ATOM   11673 O  O   . GLY K  1 72  ? 52.492 7.639   -47.389  1.00 6.14  ? 72   GLY L O   1 
ATOM   11674 N  N   . GLY K  1 73  ? 51.243 7.181   -45.593  1.00 7.02  ? 73   GLY L N   1 
ATOM   11675 C  CA  . GLY K  1 73  ? 51.621 5.786   -45.583  1.00 8.02  ? 73   GLY L CA  1 
ATOM   11676 C  C   . GLY K  1 73  ? 50.548 5.023   -46.337  1.00 8.62  ? 73   GLY L C   1 
ATOM   11677 O  O   . GLY K  1 73  ? 49.495 5.605   -46.658  1.00 9.97  ? 73   GLY L O   1 
ATOM   11678 N  N   . PRO K  1 74  ? 50.773 3.722   -46.584  1.00 9.17  ? 74   PRO L N   1 
ATOM   11679 C  CA  . PRO K  1 74  ? 49.826 2.945   -47.412  1.00 9.68  ? 74   PRO L CA  1 
ATOM   11680 C  C   . PRO K  1 74  ? 48.411 2.879   -46.823  1.00 11.20 ? 74   PRO L C   1 
ATOM   11681 O  O   . PRO K  1 74  ? 47.433 2.780   -47.582  1.00 9.68  ? 74   PRO L O   1 
ATOM   11682 C  CB  . PRO K  1 74  ? 50.472 1.550   -47.519  1.00 10.12 ? 74   PRO L CB  1 
ATOM   11683 C  CG  . PRO K  1 74  ? 51.582 1.513   -46.492  1.00 9.18  ? 74   PRO L CG  1 
ATOM   11684 C  CD  . PRO K  1 74  ? 51.979 2.952   -46.221  1.00 8.80  ? 74   PRO L CD  1 
ATOM   11685 N  N   . LYS K  1 75  ? 48.313 2.963   -45.491  1.00 12.23 ? 75   LYS L N   1 
ATOM   11686 C  CA  . LYS K  1 75  ? 47.040 2.834   -44.765  1.00 13.64 ? 75   LYS L CA  1 
ATOM   11687 C  C   . LYS K  1 75  ? 46.164 4.084   -44.821  1.00 14.03 ? 75   LYS L C   1 
ATOM   11688 O  O   . LYS K  1 75  ? 44.987 4.028   -44.466  1.00 14.38 ? 75   LYS L O   1 
ATOM   11689 C  CB  . LYS K  1 75  ? 47.310 2.478   -43.290  1.00 14.77 ? 75   LYS L CB  1 
ATOM   11690 C  CG  . LYS K  1 75  ? 47.908 1.095   -43.080  1.00 16.44 ? 75   LYS L CG  1 
ATOM   11691 C  CD  . LYS K  1 75  ? 48.530 0.933   -41.685  1.00 20.07 ? 75   LYS L CD  1 
ATOM   11692 C  CE  . LYS K  1 75  ? 47.469 0.747   -40.620  1.00 21.15 ? 75   LYS L CE  1 
ATOM   11693 N  NZ  . LYS K  1 75  ? 48.026 0.900   -39.238  1.00 23.42 ? 75   LYS L NZ  1 
ATOM   11694 N  N   . ASP K  1 76  ? 46.726 5.202   -45.271  1.00 13.18 ? 76   ASP L N   1 
ATOM   11695 C  CA  . ASP K  1 76  ? 46.036 6.476   -45.237  1.00 14.49 ? 76   ASP L CA  1 
ATOM   11696 C  C   . ASP K  1 76  ? 45.161 6.722   -46.455  1.00 14.86 ? 76   ASP L C   1 
ATOM   11697 O  O   . ASP K  1 76  ? 45.549 6.407   -47.577  1.00 15.04 ? 76   ASP L O   1 
ATOM   11698 C  CB  . ASP K  1 76  ? 47.062 7.616   -45.144  1.00 13.94 ? 76   ASP L CB  1 
ATOM   11699 C  CG  . ASP K  1 76  ? 47.762 7.660   -43.820  1.00 15.46 ? 76   ASP L CG  1 
ATOM   11700 O  OD1 . ASP K  1 76  ? 48.998 7.842   -43.809  1.00 13.62 ? 76   ASP L OD1 1 
ATOM   11701 O  OD2 . ASP K  1 76  ? 47.084 7.506   -42.780  1.00 17.16 ? 76   ASP L OD2 1 
ATOM   11702 N  N   . GLU K  1 77  ? 43.988 7.314   -46.228  1.00 14.67 ? 77   GLU L N   1 
ATOM   11703 C  CA  . GLU K  1 77  ? 43.179 7.834   -47.320  1.00 15.39 ? 77   GLU L CA  1 
ATOM   11704 C  C   . GLU K  1 77  ? 43.976 8.894   -48.089  1.00 14.17 ? 77   GLU L C   1 
ATOM   11705 O  O   . GLU K  1 77  ? 44.022 8.866   -49.320  1.00 14.39 ? 77   GLU L O   1 
ATOM   11706 C  CB  . GLU K  1 77  ? 41.853 8.404   -46.783  1.00 15.62 ? 77   GLU L CB  1 
ATOM   11707 C  CG  . GLU K  1 77  ? 40.826 8.789   -47.841  1.00 19.98 ? 77   GLU L CG  1 
ATOM   11708 C  CD  . GLU K  1 77  ? 39.395 8.940   -47.268  1.00 24.54 ? 77   GLU L CD  1 
ATOM   11709 O  OE1 . GLU K  1 77  ? 39.199 8.716   -46.049  1.00 26.62 ? 77   GLU L OE1 1 
ATOM   11710 O  OE2 . GLU K  1 77  ? 38.468 9.280   -48.038  1.00 26.68 ? 77   GLU L OE2 1 
ATOM   11711 N  N   . GLU K  1 78  ? 44.600 9.821   -47.364  1.00 12.81 ? 78   GLU L N   1 
ATOM   11712 C  CA  . GLU K  1 78  ? 45.435 10.848  -47.980  1.00 12.35 ? 78   GLU L CA  1 
ATOM   11713 C  C   . GLU K  1 78  ? 46.852 10.296  -48.204  1.00 11.00 ? 78   GLU L C   1 
ATOM   11714 O  O   . GLU K  1 78  ? 47.685 10.305  -47.295  1.00 10.94 ? 78   GLU L O   1 
ATOM   11715 C  CB  . GLU K  1 78  ? 45.480 12.096  -47.098  1.00 12.49 ? 78   GLU L CB  1 
ATOM   11716 C  CG  . GLU K  1 78  ? 46.165 13.311  -47.707  1.00 15.11 ? 78   GLU L CG  1 
ATOM   11717 C  CD  . GLU K  1 78  ? 45.326 14.015  -48.768  1.00 19.21 ? 78   GLU L CD  1 
ATOM   11718 O  OE1 . GLU K  1 78  ? 45.902 14.848  -49.505  1.00 19.20 ? 78   GLU L OE1 1 
ATOM   11719 O  OE2 . GLU K  1 78  ? 44.103 13.729  -48.879  1.00 23.16 ? 78   GLU L OE2 1 
ATOM   11720 N  N   . ARG K  1 79  ? 47.092 9.784   -49.404  1.00 10.37 ? 79   ARG L N   1 
ATOM   11721 C  CA  . ARG K  1 79  ? 48.406 9.260   -49.808  1.00 8.81  ? 79   ARG L CA  1 
ATOM   11722 C  C   . ARG K  1 79  ? 48.521 9.427   -51.314  1.00 8.75  ? 79   ARG L C   1 
ATOM   11723 O  O   . ARG K  1 79  ? 47.527 9.701   -52.001  1.00 8.71  ? 79   ARG L O   1 
ATOM   11724 C  CB  . ARG K  1 79  ? 48.536 7.759   -49.463  1.00 8.55  ? 79   ARG L CB  1 
ATOM   11725 C  CG  . ARG K  1 79  ? 47.444 6.904   -50.155  1.00 7.89  ? 79   ARG L CG  1 
ATOM   11726 C  CD  . ARG K  1 79  ? 47.668 5.429   -49.937  1.00 8.77  ? 79   ARG L CD  1 
ATOM   11727 N  NE  . ARG K  1 79  ? 48.443 4.856   -51.033  1.00 7.28  ? 79   ARG L NE  1 
ATOM   11728 C  CZ  . ARG K  1 79  ? 48.656 3.549   -51.185  1.00 6.38  ? 79   ARG L CZ  1 
ATOM   11729 N  NH1 . ARG K  1 79  ? 49.342 3.124   -52.237  1.00 6.52  ? 79   ARG L NH1 1 
ATOM   11730 N  NH2 . ARG K  1 79  ? 48.141 2.665   -50.333  1.00 6.82  ? 79   ARG L NH2 1 
ATOM   11731 N  N   . HIS K  1 80  ? 49.734 9.257   -51.824  1.00 7.69  ? 80   HIS L N   1 
ATOM   11732 C  CA  . HIS K  1 80  ? 49.973 9.182   -53.259  1.00 7.35  ? 80   HIS L CA  1 
ATOM   11733 C  C   . HIS K  1 80  ? 49.669 7.767   -53.683  1.00 7.03  ? 80   HIS L C   1 
ATOM   11734 O  O   . HIS K  1 80  ? 49.837 6.852   -52.891  1.00 8.13  ? 80   HIS L O   1 
ATOM   11735 C  CB  . HIS K  1 80  ? 51.440 9.443   -53.551  1.00 6.37  ? 80   HIS L CB  1 
ATOM   11736 C  CG  . HIS K  1 80  ? 51.895 10.804  -53.164  1.00 6.59  ? 80   HIS L CG  1 
ATOM   11737 N  ND1 . HIS K  1 80  ? 53.148 11.052  -52.642  1.00 6.65  ? 80   HIS L ND1 1 
ATOM   11738 C  CD2 . HIS K  1 80  ? 51.284 12.004  -53.262  1.00 6.47  ? 80   HIS L CD2 1 
ATOM   11739 C  CE1 . HIS K  1 80  ? 53.280 12.348  -52.423  1.00 7.03  ? 80   HIS L CE1 1 
ATOM   11740 N  NE2 . HIS K  1 80  ? 52.153 12.941  -52.766  1.00 5.83  ? 80   HIS L NE2 1 
ATOM   11741 N  N   . VAL K  1 81  ? 49.258 7.553   -54.932  1.00 7.26  ? 81   VAL L N   1 
ATOM   11742 C  CA  . VAL K  1 81  ? 49.049 6.161   -55.359  1.00 6.67  ? 81   VAL L CA  1 
ATOM   11743 C  C   . VAL K  1 81  ? 50.333 5.346   -55.142  1.00 6.85  ? 81   VAL L C   1 
ATOM   11744 O  O   . VAL K  1 81  ? 50.288 4.177   -54.736  1.00 6.72  ? 81   VAL L O   1 
ATOM   11745 C  CB  . VAL K  1 81  ? 48.497 6.044   -56.831  1.00 7.09  ? 81   VAL L CB  1 
ATOM   11746 C  CG1 . VAL K  1 81  ? 48.558 4.599   -57.308  1.00 5.92  ? 81   VAL L CG1 1 
ATOM   11747 C  CG2 . VAL K  1 81  ? 47.029 6.479   -56.884  1.00 6.33  ? 81   VAL L CG2 1 
ATOM   11748 N  N   . GLY K  1 82  ? 51.484 5.984   -55.364  1.00 7.34  ? 82   GLY L N   1 
ATOM   11749 C  CA  . GLY K  1 82  ? 52.763 5.305   -55.239  1.00 6.93  ? 82   GLY L CA  1 
ATOM   11750 C  C   . GLY K  1 82  ? 53.254 4.906   -53.842  1.00 7.91  ? 82   GLY L C   1 
ATOM   11751 O  O   . GLY K  1 82  ? 54.273 4.233   -53.746  1.00 8.80  ? 82   GLY L O   1 
ATOM   11752 N  N   . ASP K  1 83  ? 52.538 5.298   -52.775  1.00 7.79  ? 83   ASP L N   1 
ATOM   11753 C  CA  . ASP K  1 83  ? 53.063 5.215   -51.406  1.00 7.50  ? 83   ASP L CA  1 
ATOM   11754 C  C   . ASP K  1 83  ? 52.897 3.845   -50.794  1.00 8.00  ? 83   ASP L C   1 
ATOM   11755 O  O   . ASP K  1 83  ? 51.840 3.515   -50.263  1.00 8.25  ? 83   ASP L O   1 
ATOM   11756 C  CB  . ASP K  1 83  ? 52.386 6.257   -50.494  1.00 7.27  ? 83   ASP L CB  1 
ATOM   11757 C  CG  . ASP K  1 83  ? 52.747 7.663   -50.838  1.00 7.57  ? 83   ASP L CG  1 
ATOM   11758 O  OD1 . ASP K  1 83  ? 53.777 7.863   -51.541  1.00 8.28  ? 83   ASP L OD1 1 
ATOM   11759 O  OD2 . ASP K  1 83  ? 52.027 8.580   -50.387  1.00 7.18  ? 83   ASP L OD2 1 
ATOM   11760 N  N   . LEU K  1 84  ? 53.963 3.051   -50.839  1.00 7.45  ? 84   LEU L N   1 
ATOM   11761 C  CA  . LEU K  1 84  ? 53.968 1.725   -50.254  1.00 7.48  ? 84   LEU L CA  1 
ATOM   11762 C  C   . LEU K  1 84  ? 54.650 1.622   -48.869  1.00 7.28  ? 84   LEU L C   1 
ATOM   11763 O  O   . LEU K  1 84  ? 54.892 0.532   -48.388  1.00 8.99  ? 84   LEU L O   1 
ATOM   11764 C  CB  . LEU K  1 84  ? 54.585 0.718   -51.253  1.00 8.15  ? 84   LEU L CB  1 
ATOM   11765 C  CG  . LEU K  1 84  ? 53.823 0.521   -52.569  1.00 7.02  ? 84   LEU L CG  1 
ATOM   11766 C  CD1 . LEU K  1 84  ? 54.552 -0.544  -53.364  1.00 7.50  ? 84   LEU L CD1 1 
ATOM   11767 C  CD2 . LEU K  1 84  ? 52.367 0.100   -52.298  1.00 8.39  ? 84   LEU L CD2 1 
ATOM   11768 N  N   . GLY K  1 85  ? 54.971 2.749   -48.238  1.00 7.44  ? 85   GLY L N   1 
ATOM   11769 C  CA  . GLY K  1 85  ? 55.547 2.733   -46.879  1.00 7.64  ? 85   GLY L CA  1 
ATOM   11770 C  C   . GLY K  1 85  ? 57.015 2.334   -46.802  1.00 7.88  ? 85   GLY L C   1 
ATOM   11771 O  O   . GLY K  1 85  ? 57.837 2.800   -47.585  1.00 8.75  ? 85   GLY L O   1 
ATOM   11772 N  N   . ASN K  1 86  ? 57.335 1.467   -45.843  1.00 8.85  ? 86   ASN L N   1 
ATOM   11773 C  CA  . ASN K  1 86  ? 58.713 1.043   -45.608  1.00 8.55  ? 86   ASN L CA  1 
ATOM   11774 C  C   . ASN K  1 86  ? 58.934 -0.445  -45.842  1.00 9.35  ? 86   ASN L C   1 
ATOM   11775 O  O   . ASN K  1 86  ? 58.002 -1.261  -45.719  1.00 9.27  ? 86   ASN L O   1 
ATOM   11776 C  CB  . ASN K  1 86  ? 59.163 1.387   -44.187  1.00 8.43  ? 86   ASN L CB  1 
ATOM   11777 C  CG  . ASN K  1 86  ? 59.294 2.887   -43.949  1.00 7.52  ? 86   ASN L CG  1 
ATOM   11778 O  OD1 . ASN K  1 86  ? 60.105 3.545   -44.573  1.00 7.00  ? 86   ASN L OD1 1 
ATOM   11779 N  ND2 . ASN K  1 86  ? 58.492 3.419   -43.035  1.00 7.71  ? 86   ASN L ND2 1 
ATOM   11780 N  N   . VAL K  1 87  ? 60.176 -0.771  -46.182  1.00 9.09  ? 87   VAL L N   1 
ATOM   11781 C  CA  . VAL K  1 87  ? 60.681 -2.140  -46.112  1.00 9.50  ? 87   VAL L CA  1 
ATOM   11782 C  C   . VAL K  1 87  ? 61.700 -2.169  -44.980  1.00 10.02 ? 87   VAL L C   1 
ATOM   11783 O  O   . VAL K  1 87  ? 62.200 -1.123  -44.581  1.00 10.90 ? 87   VAL L O   1 
ATOM   11784 C  CB  . VAL K  1 87  ? 61.244 -2.633  -47.478  1.00 8.65  ? 87   VAL L CB  1 
ATOM   11785 C  CG1 . VAL K  1 87  ? 60.166 -2.571  -48.549  1.00 10.23 ? 87   VAL L CG1 1 
ATOM   11786 C  CG2 . VAL K  1 87  ? 62.465 -1.835  -47.908  1.00 8.69  ? 87   VAL L CG2 1 
ATOM   11787 N  N   . THR K  1 88  ? 61.990 -3.340  -44.413  1.00 10.20 ? 88   THR L N   1 
ATOM   11788 C  CA  . THR K  1 88  ? 62.848 -3.372  -43.244  1.00 11.15 ? 88   THR L CA  1 
ATOM   11789 C  C   . THR K  1 88  ? 64.019 -4.268  -43.541  1.00 11.69 ? 88   THR L C   1 
ATOM   11790 O  O   . THR K  1 88  ? 63.830 -5.434  -43.853  1.00 11.40 ? 88   THR L O   1 
ATOM   11791 C  CB  . THR K  1 88  ? 62.103 -3.891  -41.985  1.00 11.20 ? 88   THR L CB  1 
ATOM   11792 O  OG1 . THR K  1 88  ? 60.898 -3.130  -41.781  1.00 10.59 ? 88   THR L OG1 1 
ATOM   11793 C  CG2 . THR K  1 88  ? 63.009 -3.765  -40.738  1.00 12.10 ? 88   THR L CG2 1 
ATOM   11794 N  N   . ALA K  1 89  ? 65.226 -3.727  -43.480  1.00 11.92 ? 89   ALA L N   1 
ATOM   11795 C  CA  . ALA K  1 89  ? 66.403 -4.579  -43.664  1.00 12.78 ? 89   ALA L CA  1 
ATOM   11796 C  C   . ALA K  1 89  ? 66.901 -5.111  -42.320  1.00 13.60 ? 89   ALA L C   1 
ATOM   11797 O  O   . ALA K  1 89  ? 66.906 -4.378  -41.311  1.00 14.31 ? 89   ALA L O   1 
ATOM   11798 C  CB  . ALA K  1 89  ? 67.506 -3.824  -44.389  1.00 12.70 ? 89   ALA L CB  1 
ATOM   11799 N  N   . ASP K  1 90  ? 67.317 -6.374  -42.312  1.00 13.75 ? 90   ASP L N   1 
ATOM   11800 C  CA  . ASP K  1 90  ? 67.885 -7.001  -41.119  1.00 14.65 ? 90   ASP L CA  1 
ATOM   11801 C  C   . ASP K  1 90  ? 69.364 -6.630  -40.951  1.00 14.87 ? 90   ASP L C   1 
ATOM   11802 O  O   . ASP K  1 90  ? 69.867 -5.782  -41.705  1.00 14.25 ? 90   ASP L O   1 
ATOM   11803 C  CB  . ASP K  1 90  ? 67.640 -8.522  -41.112  1.00 14.83 ? 90   ASP L CB  1 
ATOM   11804 C  CG  . ASP K  1 90  ? 68.336 -9.269  -42.270  1.00 15.27 ? 90   ASP L CG  1 
ATOM   11805 O  OD1 . ASP K  1 90  ? 67.919 -10.417 -42.537  1.00 17.57 ? 90   ASP L OD1 1 
ATOM   11806 O  OD2 . ASP K  1 90  ? 69.279 -8.748  -42.903  1.00 13.60 ? 90   ASP L OD2 1 
ATOM   11807 N  N   . LYS K  1 91  ? 70.049 -7.203  -39.954  1.00 14.79 ? 91   LYS L N   1 
ATOM   11808 C  CA  . LYS K  1 91  ? 71.455 -6.826  -39.716  1.00 15.61 ? 91   LYS L CA  1 
ATOM   11809 C  C   . LYS K  1 91  ? 72.361 -7.240  -40.878  1.00 15.17 ? 91   LYS L C   1 
ATOM   11810 O  O   . LYS K  1 91  ? 73.399 -6.623  -41.104  1.00 14.91 ? 91   LYS L O   1 
ATOM   11811 C  CB  . LYS K  1 91  ? 72.007 -7.360  -38.372  1.00 16.22 ? 91   LYS L CB  1 
ATOM   11812 C  CG  . LYS K  1 91  ? 72.247 -8.865  -38.307  1.00 17.70 ? 91   LYS L CG  1 
ATOM   11813 C  CD  . LYS K  1 91  ? 72.713 -9.314  -36.898  1.00 20.40 ? 91   LYS L CD  1 
ATOM   11814 C  CE  . LYS K  1 91  ? 74.239 -9.271  -36.751  1.00 22.35 ? 91   LYS L CE  1 
ATOM   11815 N  NZ  . LYS K  1 91  ? 74.735 -9.912  -35.481  1.00 22.11 ? 91   LYS L NZ  1 
ATOM   11816 N  N   . ASP K  1 92  ? 71.953 -8.271  -41.612  1.00 14.88 ? 92   ASP L N   1 
ATOM   11817 C  CA  . ASP K  1 92  ? 72.688 -8.702  -42.814  1.00 15.18 ? 92   ASP L CA  1 
ATOM   11818 C  C   . ASP K  1 92  ? 72.440 -7.812  -44.041  1.00 14.61 ? 92   ASP L C   1 
ATOM   11819 O  O   . ASP K  1 92  ? 73.026 -8.036  -45.113  1.00 13.61 ? 92   ASP L O   1 
ATOM   11820 C  CB  . ASP K  1 92  ? 72.333 -10.154 -43.157  1.00 16.23 ? 92   ASP L CB  1 
ATOM   11821 C  CG  . ASP K  1 92  ? 72.803 -11.140 -42.094  1.00 18.62 ? 92   ASP L CG  1 
ATOM   11822 O  OD1 . ASP K  1 92  ? 72.072 -12.137 -41.849  1.00 23.89 ? 92   ASP L OD1 1 
ATOM   11823 O  OD2 . ASP K  1 92  ? 73.883 -10.927 -41.500  1.00 20.41 ? 92   ASP L OD2 1 
ATOM   11824 N  N   . GLY K  1 93  ? 71.550 -6.826  -43.898  1.00 13.20 ? 93   GLY L N   1 
ATOM   11825 C  CA  . GLY K  1 93  ? 71.256 -5.912  -45.000  1.00 12.63 ? 93   GLY L CA  1 
ATOM   11826 C  C   . GLY K  1 93  ? 70.229 -6.418  -45.985  1.00 11.99 ? 93   GLY L C   1 
ATOM   11827 O  O   . GLY K  1 93  ? 70.101 -5.888  -47.098  1.00 11.88 ? 93   GLY L O   1 
ATOM   11828 N  N   . VAL K  1 94  ? 69.473 -7.431  -45.565  1.00 12.28 ? 94   VAL L N   1 
ATOM   11829 C  CA  . VAL K  1 94  ? 68.442 -8.055  -46.404  1.00 12.87 ? 94   VAL L CA  1 
ATOM   11830 C  C   . VAL K  1 94  ? 67.033 -7.663  -45.943  1.00 13.02 ? 94   VAL L C   1 
ATOM   11831 O  O   . VAL K  1 94  ? 66.689 -7.856  -44.776  1.00 12.72 ? 94   VAL L O   1 
ATOM   11832 C  CB  . VAL K  1 94  ? 68.551 -9.600  -46.370  1.00 12.83 ? 94   VAL L CB  1 
ATOM   11833 C  CG1 . VAL K  1 94  ? 67.518 -10.244 -47.294  1.00 13.42 ? 94   VAL L CG1 1 
ATOM   11834 C  CG2 . VAL K  1 94  ? 69.958 -10.042 -46.775  1.00 14.34 ? 94   VAL L CG2 1 
ATOM   11835 N  N   . ALA K  1 95  ? 66.251 -7.105  -46.863  1.00 13.32 ? 95   ALA L N   1 
ATOM   11836 C  CA  . ALA K  1 95  ? 64.837 -6.829  -46.644  1.00 13.96 ? 95   ALA L CA  1 
ATOM   11837 C  C   . ALA K  1 95  ? 64.004 -7.818  -47.439  1.00 14.45 ? 95   ALA L C   1 
ATOM   11838 O  O   . ALA K  1 95  ? 64.025 -7.787  -48.663  1.00 13.66 ? 95   ALA L O   1 
ATOM   11839 C  CB  . ALA K  1 95  ? 64.501 -5.408  -47.107  1.00 13.91 ? 95   ALA L CB  1 
ATOM   11840 N  N   . ASP K  1 96  ? 63.259 -8.682  -46.755  1.00 15.72 ? 96   ASP L N   1 
ATOM   11841 C  CA  . ASP K  1 96  ? 62.335 -9.567  -47.463  1.00 17.19 ? 96   ASP L CA  1 
ATOM   11842 C  C   . ASP K  1 96  ? 60.973 -8.916  -47.550  1.00 17.10 ? 96   ASP L C   1 
ATOM   11843 O  O   . ASP K  1 96  ? 60.291 -8.772  -46.546  1.00 19.09 ? 96   ASP L O   1 
ATOM   11844 C  CB  . ASP K  1 96  ? 62.296 -10.947 -46.805  1.00 18.11 ? 96   ASP L CB  1 
ATOM   11845 C  CG  . ASP K  1 96  ? 63.643 -11.650 -46.888  1.00 19.89 ? 96   ASP L CG  1 
ATOM   11846 O  OD1 . ASP K  1 96  ? 64.186 -12.043 -45.833  1.00 24.77 ? 96   ASP L OD1 1 
ATOM   11847 O  OD2 . ASP K  1 96  ? 64.176 -11.784 -48.014  1.00 23.60 ? 96   ASP L OD2 1 
ATOM   11848 N  N   . VAL K  1 97  ? 60.612 -8.485  -48.751  1.00 16.90 ? 97   VAL L N   1 
ATOM   11849 C  CA  . VAL K  1 97  ? 59.417 -7.678  -48.990  1.00 16.57 ? 97   VAL L CA  1 
ATOM   11850 C  C   . VAL K  1 97  ? 58.167 -8.559  -49.118  1.00 17.34 ? 97   VAL L C   1 
ATOM   11851 O  O   . VAL K  1 97  ? 58.163 -9.562  -49.843  1.00 16.33 ? 97   VAL L O   1 
ATOM   11852 C  CB  . VAL K  1 97  ? 59.629 -6.768  -50.235  1.00 16.67 ? 97   VAL L CB  1 
ATOM   11853 C  CG1 . VAL K  1 97  ? 58.415 -5.861  -50.532  1.00 15.16 ? 97   VAL L CG1 1 
ATOM   11854 C  CG2 . VAL K  1 97  ? 60.895 -5.934  -50.068  1.00 15.90 ? 97   VAL L CG2 1 
ATOM   11855 N  N   . SER K  1 98  ? 57.123 -8.205  -48.371  1.00 17.50 ? 98   SER L N   1 
ATOM   11856 C  CA  . SER K  1 98  ? 55.822 -8.850  -48.491  1.00 18.49 ? 98   SER L CA  1 
ATOM   11857 C  C   . SER K  1 98  ? 54.773 -7.823  -48.091  1.00 18.26 ? 98   SER L C   1 
ATOM   11858 O  O   . SER K  1 98  ? 54.614 -7.509  -46.910  1.00 18.61 ? 98   SER L O   1 
ATOM   11859 C  CB  . SER K  1 98  ? 55.740 -10.119 -47.631  1.00 18.53 ? 98   SER L CB  1 
ATOM   11860 O  OG  . SER K  1 98  ? 54.552 -10.858 -47.876  1.00 20.69 ? 98   SER L OG  1 
ATOM   11861 N  N   . ILE K  1 99  ? 54.095 -7.288  -49.095  1.00 17.96 ? 99   ILE L N   1 
ATOM   11862 C  CA  . ILE K  1 99  ? 53.088 -6.232  -48.937  1.00 18.24 ? 99   ILE L CA  1 
ATOM   11863 C  C   . ILE K  1 99  ? 51.868 -6.584  -49.795  1.00 18.16 ? 99   ILE L C   1 
ATOM   11864 O  O   . ILE K  1 99  ? 52.025 -7.159  -50.870  1.00 18.49 ? 99   ILE L O   1 
ATOM   11865 C  CB  . ILE K  1 99  ? 53.667 -4.869  -49.418  1.00 18.10 ? 99   ILE L CB  1 
ATOM   11866 C  CG1 . ILE K  1 99  ? 54.703 -4.334  -48.419  1.00 18.62 ? 99   ILE L CG1 1 
ATOM   11867 C  CG2 . ILE K  1 99  ? 52.576 -3.827  -49.629  1.00 19.49 ? 99   ILE L CG2 1 
ATOM   11868 C  CD1 . ILE K  1 99  ? 55.663 -3.260  -49.026  1.00 18.74 ? 99   ILE L CD1 1 
ATOM   11869 N  N   . GLU K  1 100 ? 50.663 -6.239  -49.325  1.00 17.76 ? 100  GLU L N   1 
ATOM   11870 C  CA  . GLU K  1 100 ? 49.479 -6.205  -50.190  1.00 17.23 ? 100  GLU L CA  1 
ATOM   11871 C  C   . GLU K  1 100 ? 48.916 -4.791  -50.202  1.00 16.74 ? 100  GLU L C   1 
ATOM   11872 O  O   . GLU K  1 100 ? 48.776 -4.156  -49.156  1.00 15.35 ? 100  GLU L O   1 
ATOM   11873 C  CB  . GLU K  1 100 ? 48.392 -7.178  -49.726  1.00 18.17 ? 100  GLU L CB  1 
ATOM   11874 C  CG  . GLU K  1 100 ? 48.766 -8.640  -49.883  1.00 22.04 ? 100  GLU L CG  1 
ATOM   11875 C  CD  . GLU K  1 100 ? 47.555 -9.544  -50.060  1.00 26.68 ? 100  GLU L CD  1 
ATOM   11876 O  OE1 . GLU K  1 100 ? 47.319 -10.396 -49.174  1.00 28.42 ? 100  GLU L OE1 1 
ATOM   11877 O  OE2 . GLU K  1 100 ? 46.840 -9.395  -51.079  1.00 28.31 ? 100  GLU L OE2 1 
ATOM   11878 N  N   . ASP K  1 101 ? 48.586 -4.296  -51.382  1.00 15.53 ? 101  ASP L N   1 
ATOM   11879 C  CA  . ASP K  1 101 ? 48.070 -2.949  -51.459  1.00 15.36 ? 101  ASP L CA  1 
ATOM   11880 C  C   . ASP K  1 101 ? 46.863 -2.871  -52.392  1.00 15.23 ? 101  ASP L C   1 
ATOM   11881 O  O   . ASP K  1 101 ? 46.872 -3.467  -53.473  1.00 14.74 ? 101  ASP L O   1 
ATOM   11882 C  CB  . ASP K  1 101 ? 49.176 -2.005  -51.923  1.00 15.40 ? 101  ASP L CB  1 
ATOM   11883 C  CG  . ASP K  1 101 ? 48.801 -0.567  -51.754  1.00 14.30 ? 101  ASP L CG  1 
ATOM   11884 O  OD1 . ASP K  1 101 ? 48.433 0.074   -52.764  1.00 13.21 ? 101  ASP L OD1 1 
ATOM   11885 O  OD2 . ASP K  1 101 ? 48.830 -0.090  -50.601  1.00 16.66 ? 101  ASP L OD2 1 
ATOM   11886 N  N   . SER K  1 102 ? 45.834 -2.132  -51.983  1.00 14.87 ? 102  SER L N   1 
ATOM   11887 C  CA  . SER K  1 102 ? 44.646 -1.993  -52.826  1.00 14.98 ? 102  SER L CA  1 
ATOM   11888 C  C   . SER K  1 102 ? 44.559 -0.686  -53.587  1.00 14.14 ? 102  SER L C   1 
ATOM   11889 O  O   . SER K  1 102 ? 43.536 -0.403  -54.199  1.00 13.77 ? 102  SER L O   1 
ATOM   11890 C  CB  . SER K  1 102 ? 43.390 -2.179  -51.990  1.00 15.58 ? 102  SER L CB  1 
ATOM   11891 O  OG  . SER K  1 102 ? 43.412 -3.454  -51.382  1.00 19.08 ? 102  SER L OG  1 
ATOM   11892 N  N   . VAL K  1 103 ? 45.617 0.116   -53.557  1.00 12.56 ? 103  VAL L N   1 
ATOM   11893 C  CA  . VAL K  1 103 ? 45.573 1.409   -54.235  1.00 12.30 ? 103  VAL L CA  1 
ATOM   11894 C  C   . VAL K  1 103 ? 46.380 1.382   -55.534  1.00 12.20 ? 103  VAL L C   1 
ATOM   11895 O  O   . VAL K  1 103 ? 45.915 1.852   -56.568  1.00 12.66 ? 103  VAL L O   1 
ATOM   11896 C  CB  . VAL K  1 103 ? 46.035 2.543   -53.287  1.00 12.08 ? 103  VAL L CB  1 
ATOM   11897 C  CG1 . VAL K  1 103 ? 46.199 3.858   -54.026  1.00 12.43 ? 103  VAL L CG1 1 
ATOM   11898 C  CG2 . VAL K  1 103 ? 45.024 2.690   -52.150  1.00 12.26 ? 103  VAL L CG2 1 
ATOM   11899 N  N   . ILE K  1 104 ? 47.592 0.839   -55.487  1.00 11.32 ? 104  ILE L N   1 
ATOM   11900 C  CA  . ILE K  1 104 ? 48.303 0.591   -56.741  1.00 11.32 ? 104  ILE L CA  1 
ATOM   11901 C  C   . ILE K  1 104 ? 47.495 -0.444  -57.514  1.00 11.42 ? 104  ILE L C   1 
ATOM   11902 O  O   . ILE K  1 104 ? 46.704 -1.199  -56.922  1.00 11.64 ? 104  ILE L O   1 
ATOM   11903 C  CB  . ILE K  1 104 ? 49.718 0.033   -56.532  1.00 11.12 ? 104  ILE L CB  1 
ATOM   11904 C  CG1 . ILE K  1 104 ? 49.677 -1.224  -55.656  1.00 9.91  ? 104  ILE L CG1 1 
ATOM   11905 C  CG2 . ILE K  1 104 ? 50.638 1.105   -56.008  1.00 10.07 ? 104  ILE L CG2 1 
ATOM   11906 C  CD1 . ILE K  1 104 ? 50.980 -2.036  -55.682  1.00 9.87  ? 104  ILE L CD1 1 
ATOM   11907 N  N   . SER K  1 105 ? 47.719 -0.479  -58.821  1.00 12.58 ? 105  SER L N   1 
ATOM   11908 C  CA  . SER K  1 105 ? 47.075 -1.450  -59.692  1.00 13.76 ? 105  SER L CA  1 
ATOM   11909 C  C   . SER K  1 105 ? 48.012 -1.846  -60.826  1.00 14.38 ? 105  SER L C   1 
ATOM   11910 O  O   . SER K  1 105 ? 48.965 -1.127  -61.136  1.00 14.10 ? 105  SER L O   1 
ATOM   11911 C  CB  . SER K  1 105 ? 45.821 -0.821  -60.289  1.00 13.58 ? 105  SER L CB  1 
ATOM   11912 O  OG  . SER K  1 105 ? 45.011 -1.803  -60.873  1.00 14.82 ? 105  SER L OG  1 
ATOM   11913 N  N   . LEU K  1 106 ? 47.704 -2.971  -61.473  1.00 14.97 ? 106  LEU L N   1 
ATOM   11914 C  CA  . LEU K  1 106 ? 48.418 -3.350  -62.698  1.00 14.92 ? 106  LEU L CA  1 
ATOM   11915 C  C   . LEU K  1 106 ? 47.625 -3.000  -63.967  1.00 15.61 ? 106  LEU L C   1 
ATOM   11916 O  O   . LEU K  1 106 ? 48.061 -3.295  -65.086  1.00 15.16 ? 106  LEU L O   1 
ATOM   11917 C  CB  . LEU K  1 106 ? 48.813 -4.836  -62.652  1.00 15.30 ? 106  LEU L CB  1 
ATOM   11918 C  CG  . LEU K  1 106 ? 49.561 -5.305  -61.400  1.00 14.73 ? 106  LEU L CG  1 
ATOM   11919 C  CD1 . LEU K  1 106 ? 50.079 -6.709  -61.600  1.00 17.07 ? 106  LEU L CD1 1 
ATOM   11920 C  CD2 . LEU K  1 106 ? 50.721 -4.356  -61.108  1.00 16.53 ? 106  LEU L CD2 1 
ATOM   11921 N  N   . SER K  1 107 ? 46.483 -2.338  -63.794  1.00 15.71 ? 107  SER L N   1 
ATOM   11922 C  CA  . SER K  1 107 ? 45.786 -1.716  -64.932  1.00 16.30 ? 107  SER L CA  1 
ATOM   11923 C  C   . SER K  1 107 ? 45.043 -0.451  -64.524  1.00 16.39 ? 107  SER L C   1 
ATOM   11924 O  O   . SER K  1 107 ? 44.934 -0.140  -63.332  1.00 15.65 ? 107  SER L O   1 
ATOM   11925 C  CB  . SER K  1 107 ? 44.830 -2.700  -65.612  1.00 16.15 ? 107  SER L CB  1 
ATOM   11926 O  OG  . SER K  1 107 ? 43.666 -2.923  -64.847  1.00 17.82 ? 107  SER L OG  1 
ATOM   11927 N  N   . GLY K  1 108 ? 44.537 0.276   -65.520  1.00 16.29 ? 108  GLY L N   1 
ATOM   11928 C  CA  . GLY K  1 108 ? 43.688 1.438   -65.260  1.00 16.66 ? 108  GLY L CA  1 
ATOM   11929 C  C   . GLY K  1 108 ? 44.461 2.681   -64.852  1.00 16.76 ? 108  GLY L C   1 
ATOM   11930 O  O   . GLY K  1 108 ? 45.689 2.737   -64.989  1.00 17.25 ? 108  GLY L O   1 
ATOM   11931 N  N   . ASP K  1 109 ? 43.731 3.669   -64.338  1.00 16.25 ? 109  ASP L N   1 
ATOM   11932 C  CA  . ASP K  1 109 ? 44.278 4.965   -63.946  1.00 16.20 ? 109  ASP L CA  1 
ATOM   11933 C  C   . ASP K  1 109 ? 45.385 4.885   -62.886  1.00 15.58 ? 109  ASP L C   1 
ATOM   11934 O  O   . ASP K  1 109 ? 46.226 5.761   -62.825  1.00 15.37 ? 109  ASP L O   1 
ATOM   11935 C  CB  . ASP K  1 109 ? 43.160 5.861   -63.421  1.00 16.63 ? 109  ASP L CB  1 
ATOM   11936 C  CG  . ASP K  1 109 ? 42.448 6.621   -64.529  1.00 19.03 ? 109  ASP L CG  1 
ATOM   11937 O  OD1 . ASP K  1 109 ? 41.527 7.399   -64.212  1.00 19.33 ? 109  ASP L OD1 1 
ATOM   11938 O  OD2 . ASP K  1 109 ? 42.809 6.448   -65.711  1.00 21.26 ? 109  ASP L OD2 1 
ATOM   11939 N  N   . HIS K  1 110 ? 45.356 3.854   -62.048  1.00 15.30 ? 110  HIS L N   1 
ATOM   11940 C  CA  . HIS K  1 110 ? 46.366 3.688   -60.995  1.00 15.96 ? 110  HIS L CA  1 
ATOM   11941 C  C   . HIS K  1 110 ? 47.442 2.681   -61.410  1.00 15.26 ? 110  HIS L C   1 
ATOM   11942 O  O   . HIS K  1 110 ? 48.177 2.159   -60.553  1.00 14.99 ? 110  HIS L O   1 
ATOM   11943 C  CB  . HIS K  1 110 ? 45.711 3.204   -59.691  1.00 16.12 ? 110  HIS L CB  1 
ATOM   11944 C  CG  . HIS K  1 110 ? 44.672 4.128   -59.130  1.00 18.32 ? 110  HIS L CG  1 
ATOM   11945 N  ND1 . HIS K  1 110 ? 44.079 3.903   -57.906  1.00 19.50 ? 110  HIS L ND1 1 
ATOM   11946 C  CD2 . HIS K  1 110 ? 44.124 5.274   -59.607  1.00 21.37 ? 110  HIS L CD2 1 
ATOM   11947 C  CE1 . HIS K  1 110 ? 43.199 4.859   -57.661  1.00 20.29 ? 110  HIS L CE1 1 
ATOM   11948 N  NE2 . HIS K  1 110 ? 43.209 5.705   -58.676  1.00 18.94 ? 110  HIS L NE2 1 
HETATM 11949 N  N   . CME K  1 111 ? 47.530 2.394   -62.713  1.00 14.96 ? 111  CME L N   1 
HETATM 11950 C  CA  . CME K  1 111 ? 48.462 1.386   -63.219  1.00 14.50 ? 111  CME L CA  1 
HETATM 11951 C  CB  . CME K  1 111 ? 48.273 1.170   -64.728  1.00 15.49 ? 111  CME L CB  1 
HETATM 11952 S  SG  . CME K  1 111 ? 49.361 -0.132  -65.185  1.00 18.52 ? 111  CME L SG  1 
HETATM 11953 S  SD  . CME K  1 111 ? 48.891 -0.465  -67.141  1.00 24.37 ? 111  CME L SD  1 
HETATM 11954 C  CE  . CME K  1 111 ? 50.372 -0.020  -67.981  1.00 26.11 ? 111  CME L CE  1 
HETATM 11955 C  CZ  . CME K  1 111 ? 50.301 1.462   -68.315  1.00 29.09 ? 111  CME L CZ  1 
HETATM 11956 O  OH  . CME K  1 111 ? 50.933 2.199   -67.267  1.00 30.72 ? 111  CME L OH  1 
HETATM 11957 C  C   . CME K  1 111 ? 49.895 1.759   -62.952  1.00 13.22 ? 111  CME L C   1 
HETATM 11958 O  O   . CME K  1 111 ? 50.313 2.881   -63.246  1.00 12.49 ? 111  CME L O   1 
ATOM   11959 N  N   . ILE K  1 112 ? 50.663 0.817   -62.402  1.00 12.41 ? 112  ILE L N   1 
ATOM   11960 C  CA  . ILE K  1 112 ? 52.067 1.076   -62.068  1.00 12.24 ? 112  ILE L CA  1 
ATOM   11961 C  C   . ILE K  1 112 ? 53.079 0.486   -63.054  1.00 12.94 ? 112  ILE L C   1 
ATOM   11962 O  O   . ILE K  1 112 ? 54.287 0.762   -62.946  1.00 11.90 ? 112  ILE L O   1 
ATOM   11963 C  CB  . ILE K  1 112 ? 52.429 0.638   -60.641  1.00 11.56 ? 112  ILE L CB  1 
ATOM   11964 C  CG1 . ILE K  1 112 ? 52.188 -0.874  -60.445  1.00 10.99 ? 112  ILE L CG1 1 
ATOM   11965 C  CG2 . ILE K  1 112 ? 51.652 1.518   -59.632  1.00 9.97  ? 112  ILE L CG2 1 
ATOM   11966 C  CD1 . ILE K  1 112 ? 52.724 -1.431  -59.118  1.00 11.93 ? 112  ILE L CD1 1 
ATOM   11967 N  N   . ILE K  1 113 ? 52.579 -0.328  -63.989  1.00 14.06 ? 113  ILE L N   1 
ATOM   11968 C  CA  . ILE K  1 113 ? 53.421 -0.878  -65.064  1.00 14.56 ? 113  ILE L CA  1 
ATOM   11969 C  C   . ILE K  1 113 ? 53.950 0.265   -65.922  1.00 14.40 ? 113  ILE L C   1 
ATOM   11970 O  O   . ILE K  1 113 ? 53.221 1.201   -66.265  1.00 15.26 ? 113  ILE L O   1 
ATOM   11971 C  CB  . ILE K  1 113 ? 52.669 -1.951  -65.892  1.00 15.19 ? 113  ILE L CB  1 
ATOM   11972 C  CG1 . ILE K  1 113 ? 52.246 -3.104  -64.977  1.00 15.18 ? 113  ILE L CG1 1 
ATOM   11973 C  CG2 . ILE K  1 113 ? 53.536 -2.446  -67.087  1.00 14.02 ? 113  ILE L CG2 1 
ATOM   11974 C  CD1 . ILE K  1 113 ? 51.363 -4.146  -65.634  1.00 16.98 ? 113  ILE L CD1 1 
ATOM   11975 N  N   . GLY K  1 114 ? 55.238 0.211   -66.232  1.00 14.67 ? 114  GLY L N   1 
ATOM   11976 C  CA  . GLY K  1 114 ? 55.886 1.280   -66.974  1.00 14.29 ? 114  GLY L CA  1 
ATOM   11977 C  C   . GLY K  1 114 ? 56.373 2.445   -66.128  1.00 14.56 ? 114  GLY L C   1 
ATOM   11978 O  O   . GLY K  1 114 ? 56.860 3.443   -66.664  1.00 14.64 ? 114  GLY L O   1 
ATOM   11979 N  N   . ARG K  1 115 ? 56.217 2.345   -64.807  1.00 14.13 ? 115  ARG L N   1 
ATOM   11980 C  CA  . ARG K  1 115 ? 56.712 3.411   -63.913  1.00 14.15 ? 115  ARG L CA  1 
ATOM   11981 C  C   . ARG K  1 115 ? 57.902 2.874   -63.101  1.00 13.59 ? 115  ARG L C   1 
ATOM   11982 O  O   . ARG K  1 115 ? 58.310 1.745   -63.313  1.00 13.98 ? 115  ARG L O   1 
ATOM   11983 C  CB  . ARG K  1 115 ? 55.582 3.959   -63.026  1.00 14.42 ? 115  ARG L CB  1 
ATOM   11984 C  CG  . ARG K  1 115 ? 54.474 4.627   -63.866  1.00 15.37 ? 115  ARG L CG  1 
ATOM   11985 C  CD  . ARG K  1 115 ? 53.279 5.119   -63.059  1.00 15.31 ? 115  ARG L CD  1 
ATOM   11986 N  NE  . ARG K  1 115 ? 52.120 5.401   -63.928  1.00 15.45 ? 115  ARG L NE  1 
ATOM   11987 C  CZ  . ARG K  1 115 ? 51.940 6.525   -64.633  1.00 15.86 ? 115  ARG L CZ  1 
ATOM   11988 N  NH1 . ARG K  1 115 ? 50.847 6.669   -65.378  1.00 17.81 ? 115  ARG L NH1 1 
ATOM   11989 N  NH2 . ARG K  1 115 ? 52.825 7.508   -64.602  1.00 13.88 ? 115  ARG L NH2 1 
ATOM   11990 N  N   . THR K  1 116 ? 58.435 3.675   -62.182  1.00 13.11 ? 116  THR L N   1 
ATOM   11991 C  CA  . THR K  1 116 ? 59.678 3.326   -61.478  1.00 12.59 ? 116  THR L CA  1 
ATOM   11992 C  C   . THR K  1 116 ? 59.425 3.024   -60.004  1.00 12.37 ? 116  THR L C   1 
ATOM   11993 O  O   . THR K  1 116 ? 58.812 3.836   -59.301  1.00 12.28 ? 116  THR L O   1 
ATOM   11994 C  CB  . THR K  1 116 ? 60.755 4.432   -61.629  1.00 13.03 ? 116  THR L CB  1 
ATOM   11995 O  OG1 . THR K  1 116 ? 61.051 4.636   -63.021  1.00 13.95 ? 116  THR L OG1 1 
ATOM   11996 C  CG2 . THR K  1 116 ? 62.068 4.052   -60.904  1.00 10.60 ? 116  THR L CG2 1 
ATOM   11997 N  N   . LEU K  1 117 ? 59.870 1.844   -59.564  1.00 11.43 ? 117  LEU L N   1 
ATOM   11998 C  CA  . LEU K  1 117 ? 59.898 1.510   -58.152  1.00 10.10 ? 117  LEU L CA  1 
ATOM   11999 C  C   . LEU K  1 117 ? 61.233 1.992   -57.562  1.00 10.03 ? 117  LEU L C   1 
ATOM   12000 O  O   . LEU K  1 117 ? 62.283 1.859   -58.191  1.00 9.56  ? 117  LEU L O   1 
ATOM   12001 C  CB  . LEU K  1 117 ? 59.736 0.005   -57.944  1.00 10.05 ? 117  LEU L CB  1 
ATOM   12002 C  CG  . LEU K  1 117 ? 59.649 -0.525  -56.513  1.00 10.89 ? 117  LEU L CG  1 
ATOM   12003 C  CD1 . LEU K  1 117 ? 58.375 -0.022  -55.835  1.00 12.20 ? 117  LEU L CD1 1 
ATOM   12004 C  CD2 . LEU K  1 117 ? 59.679 -2.053  -56.541  1.00 12.46 ? 117  LEU L CD2 1 
ATOM   12005 N  N   . VAL K  1 118 ? 61.190 2.538   -56.350  1.00 8.90  ? 118  VAL L N   1 
ATOM   12006 C  CA  . VAL K  1 118 ? 62.380 3.133   -55.741  1.00 9.14  ? 118  VAL L CA  1 
ATOM   12007 C  C   . VAL K  1 118 ? 62.476 2.716   -54.299  1.00 8.71  ? 118  VAL L C   1 
ATOM   12008 O  O   . VAL K  1 118 ? 61.479 2.777   -53.570  1.00 7.82  ? 118  VAL L O   1 
ATOM   12009 C  CB  . VAL K  1 118 ? 62.365 4.691   -55.817  1.00 9.47  ? 118  VAL L CB  1 
ATOM   12010 C  CG1 . VAL K  1 118 ? 63.587 5.267   -55.101  1.00 8.56  ? 118  VAL L CG1 1 
ATOM   12011 C  CG2 . VAL K  1 118 ? 62.388 5.151   -57.286  1.00 10.34 ? 118  VAL L CG2 1 
ATOM   12012 N  N   . VAL K  1 119 ? 63.674 2.289   -53.894  1.00 8.62  ? 119  VAL L N   1 
ATOM   12013 C  CA  . VAL K  1 119 ? 63.973 2.057   -52.471  1.00 8.57  ? 119  VAL L CA  1 
ATOM   12014 C  C   . VAL K  1 119 ? 64.926 3.166   -51.983  1.00 8.15  ? 119  VAL L C   1 
ATOM   12015 O  O   . VAL K  1 119 ? 65.859 3.557   -52.690  1.00 9.13  ? 119  VAL L O   1 
ATOM   12016 C  CB  . VAL K  1 119 ? 64.483 0.604   -52.217  1.00 7.92  ? 119  VAL L CB  1 
ATOM   12017 C  CG1 . VAL K  1 119 ? 65.853 0.350   -52.866  1.00 8.58  ? 119  VAL L CG1 1 
ATOM   12018 C  CG2 . VAL K  1 119 ? 64.509 0.271   -50.711  1.00 9.06  ? 119  VAL L CG2 1 
ATOM   12019 N  N   . HIS K  1 120 ? 64.655 3.686   -50.790  1.00 8.09  ? 120  HIS L N   1 
ATOM   12020 C  CA  . HIS K  1 120 ? 65.295 4.907   -50.298  1.00 7.28  ? 120  HIS L CA  1 
ATOM   12021 C  C   . HIS K  1 120 ? 66.329 4.706   -49.195  1.00 7.79  ? 120  HIS L C   1 
ATOM   12022 O  O   . HIS K  1 120 ? 66.353 3.685   -48.506  1.00 7.69  ? 120  HIS L O   1 
ATOM   12023 C  CB  . HIS K  1 120 ? 64.241 5.900   -49.796  1.00 6.91  ? 120  HIS L CB  1 
ATOM   12024 C  CG  . HIS K  1 120 ? 63.499 6.587   -50.901  1.00 4.80  ? 120  HIS L CG  1 
ATOM   12025 N  ND1 . HIS K  1 120 ? 63.914 7.783   -51.449  1.00 7.64  ? 120  HIS L ND1 1 
ATOM   12026 C  CD2 . HIS K  1 120 ? 62.380 6.229   -51.578  1.00 6.92  ? 120  HIS L CD2 1 
ATOM   12027 C  CE1 . HIS K  1 120 ? 63.079 8.134   -52.415  1.00 7.95  ? 120  HIS L CE1 1 
ATOM   12028 N  NE2 . HIS K  1 120 ? 62.152 7.200   -52.525  1.00 6.87  ? 120  HIS L NE2 1 
ATOM   12029 N  N   . GLU K  1 121 ? 67.149 5.738   -49.038  1.00 8.28  ? 121  GLU L N   1 
ATOM   12030 C  CA  . GLU K  1 121 ? 68.207 5.828   -48.051  1.00 9.34  ? 121  GLU L CA  1 
ATOM   12031 C  C   . GLU K  1 121 ? 67.690 5.747   -46.619  1.00 9.35  ? 121  GLU L C   1 
ATOM   12032 O  O   . GLU K  1 121 ? 68.295 5.062   -45.789  1.00 9.82  ? 121  GLU L O   1 
ATOM   12033 C  CB  . GLU K  1 121 ? 68.968 7.141   -48.287  1.00 9.95  ? 121  GLU L CB  1 
ATOM   12034 C  CG  . GLU K  1 121 ? 69.935 7.560   -47.210  1.00 13.68 ? 121  GLU L CG  1 
ATOM   12035 C  CD  . GLU K  1 121 ? 70.266 9.053   -47.245  1.00 16.55 ? 121  GLU L CD  1 
ATOM   12036 O  OE1 . GLU K  1 121 ? 69.614 9.844   -47.964  1.00 18.72 ? 121  GLU L OE1 1 
ATOM   12037 O  OE2 . GLU K  1 121 ? 71.193 9.445   -46.517  1.00 20.28 ? 121  GLU L OE2 1 
ATOM   12038 N  N   . LYS K  1 122 ? 66.575 6.431   -46.343  1.00 9.20  ? 122  LYS L N   1 
ATOM   12039 C  CA  . LYS K  1 122 ? 66.055 6.615   -44.983  1.00 8.82  ? 122  LYS L CA  1 
ATOM   12040 C  C   . LYS K  1 122 ? 64.638 6.066   -44.819  1.00 7.77  ? 122  LYS L C   1 
ATOM   12041 O  O   . LYS K  1 122 ? 63.964 5.727   -45.805  1.00 7.19  ? 122  LYS L O   1 
ATOM   12042 C  CB  . LYS K  1 122 ? 66.035 8.110   -44.597  1.00 8.89  ? 122  LYS L CB  1 
ATOM   12043 C  CG  . LYS K  1 122 ? 67.373 8.810   -44.665  1.00 13.04 ? 122  LYS L CG  1 
ATOM   12044 C  CD  . LYS K  1 122 ? 67.412 10.016  -43.727  1.00 18.94 ? 122  LYS L CD  1 
ATOM   12045 C  CE  . LYS K  1 122 ? 67.385 11.342  -44.452  1.00 21.20 ? 122  LYS L CE  1 
ATOM   12046 N  NZ  . LYS K  1 122 ? 66.022 11.831  -44.783  1.00 24.76 ? 122  LYS L NZ  1 
ATOM   12047 N  N   . ALA K  1 123 ? 64.187 6.010   -43.570  1.00 7.25  ? 123  ALA L N   1 
ATOM   12048 C  CA  . ALA K  1 123 ? 62.787 5.683   -43.278  1.00 7.23  ? 123  ALA L CA  1 
ATOM   12049 C  C   . ALA K  1 123 ? 61.821 6.751   -43.841  1.00 8.03  ? 123  ALA L C   1 
ATOM   12050 O  O   . ALA K  1 123 ? 62.122 7.953   -43.860  1.00 8.48  ? 123  ALA L O   1 
ATOM   12051 C  CB  . ALA K  1 123 ? 62.575 5.507   -41.790  1.00 6.60  ? 123  ALA L CB  1 
ATOM   12052 N  N   . ASP K  1 124 ? 60.686 6.265   -44.335  1.00 7.07  ? 124  ASP L N   1 
ATOM   12053 C  CA  . ASP K  1 124 ? 59.548 7.095   -44.732  1.00 6.19  ? 124  ASP L CA  1 
ATOM   12054 C  C   . ASP K  1 124 ? 58.733 7.402   -43.457  1.00 5.85  ? 124  ASP L C   1 
ATOM   12055 O  O   . ASP K  1 124 ? 58.269 6.469   -42.768  1.00 6.38  ? 124  ASP L O   1 
ATOM   12056 C  CB  . ASP K  1 124 ? 58.752 6.279   -45.768  1.00 5.94  ? 124  ASP L CB  1 
ATOM   12057 C  CG  . ASP K  1 124 ? 57.557 7.013   -46.345  1.00 5.75  ? 124  ASP L CG  1 
ATOM   12058 O  OD1 . ASP K  1 124 ? 57.109 6.615   -47.444  1.00 5.05  ? 124  ASP L OD1 1 
ATOM   12059 O  OD2 . ASP K  1 124 ? 57.056 7.983   -45.730  1.00 6.32  ? 124  ASP L OD2 1 
ATOM   12060 N  N   . ASP K  1 125 ? 58.578 8.694   -43.130  1.00 4.54  ? 125  ASP L N   1 
ATOM   12061 C  CA  . ASP K  1 125 ? 57.804 9.119   -41.953  1.00 4.32  ? 125  ASP L CA  1 
ATOM   12062 C  C   . ASP K  1 125 ? 56.285 9.098   -42.145  1.00 3.66  ? 125  ASP L C   1 
ATOM   12063 O  O   . ASP K  1 125 ? 55.517 9.474   -41.257  1.00 3.65  ? 125  ASP L O   1 
ATOM   12064 C  CB  . ASP K  1 125 ? 58.302 10.472  -41.415  1.00 4.37  ? 125  ASP L CB  1 
ATOM   12065 C  CG  . ASP K  1 125 ? 57.946 11.663  -42.322  1.00 5.82  ? 125  ASP L CG  1 
ATOM   12066 O  OD1 . ASP K  1 125 ? 58.607 12.700  -42.153  1.00 7.91  ? 125  ASP L OD1 1 
ATOM   12067 O  OD2 . ASP K  1 125 ? 57.044 11.585  -43.203  1.00 2.51  ? 125  ASP L OD2 1 
ATOM   12068 N  N   . LEU K  1 126 ? 55.851 8.628   -43.310  1.00 4.51  ? 126  LEU L N   1 
ATOM   12069 C  CA  . LEU K  1 126 ? 54.428 8.350   -43.592  1.00 5.09  ? 126  LEU L CA  1 
ATOM   12070 C  C   . LEU K  1 126 ? 53.600 9.644   -43.561  1.00 4.67  ? 126  LEU L C   1 
ATOM   12071 O  O   . LEU K  1 126 ? 52.390 9.633   -43.324  1.00 5.34  ? 126  LEU L O   1 
ATOM   12072 C  CB  . LEU K  1 126 ? 53.881 7.236   -42.675  1.00 5.89  ? 126  LEU L CB  1 
ATOM   12073 C  CG  . LEU K  1 126 ? 54.767 5.970   -42.630  1.00 5.97  ? 126  LEU L CG  1 
ATOM   12074 C  CD1 . LEU K  1 126 ? 54.150 4.885   -41.742  1.00 9.55  ? 126  LEU L CD1 1 
ATOM   12075 C  CD2 . LEU K  1 126 ? 54.996 5.417   -44.042  1.00 5.69  ? 126  LEU L CD2 1 
ATOM   12076 N  N   . GLY K  1 127 ? 54.276 10.753  -43.854  1.00 4.74  ? 127  GLY L N   1 
ATOM   12077 C  CA  . GLY K  1 127 ? 53.641 12.067  -43.910  1.00 4.92  ? 127  GLY L CA  1 
ATOM   12078 C  C   . GLY K  1 127 ? 53.376 12.721  -42.567  1.00 5.44  ? 127  GLY L C   1 
ATOM   12079 O  O   . GLY K  1 127 ? 52.645 13.730  -42.498  1.00 5.22  ? 127  GLY L O   1 
ATOM   12080 N  N   . LYS K  1 128 ? 53.956 12.167  -41.497  1.00 3.99  ? 128  LYS L N   1 
ATOM   12081 C  CA  . LYS K  1 128 ? 53.696 12.651  -40.134  1.00 5.20  ? 128  LYS L CA  1 
ATOM   12082 C  C   . LYS K  1 128 ? 54.841 13.505  -39.560  1.00 4.23  ? 128  LYS L C   1 
ATOM   12083 O  O   . LYS K  1 128 ? 54.917 13.734  -38.347  1.00 5.06  ? 128  LYS L O   1 
ATOM   12084 C  CB  . LYS K  1 128 ? 53.373 11.479  -39.186  1.00 5.53  ? 128  LYS L CB  1 
ATOM   12085 C  CG  . LYS K  1 128 ? 52.250 10.529  -39.722  1.00 9.20  ? 128  LYS L CG  1 
ATOM   12086 C  CD  . LYS K  1 128 ? 52.166 9.223   -38.940  1.00 15.12 ? 128  LYS L CD  1 
ATOM   12087 C  CE  . LYS K  1 128 ? 51.266 9.370   -37.728  1.00 18.82 ? 128  LYS L CE  1 
ATOM   12088 N  NZ  . LYS K  1 128 ? 51.527 8.239   -36.819  1.00 22.74 ? 128  LYS L NZ  1 
ATOM   12089 N  N   . GLY K  1 129 ? 55.717 13.987  -40.427  1.00 4.13  ? 129  GLY L N   1 
ATOM   12090 C  CA  . GLY K  1 129 ? 56.923 14.703  -39.972  1.00 4.87  ? 129  GLY L CA  1 
ATOM   12091 C  C   . GLY K  1 129 ? 56.765 16.184  -39.630  1.00 6.61  ? 129  GLY L C   1 
ATOM   12092 O  O   . GLY K  1 129 ? 57.660 16.770  -39.028  1.00 6.14  ? 129  GLY L O   1 
ATOM   12093 N  N   . GLY K  1 130 ? 55.652 16.794  -40.037  1.00 6.94  ? 130  GLY L N   1 
ATOM   12094 C  CA  . GLY K  1 130 ? 55.400 18.210  -39.724  1.00 8.81  ? 130  GLY L CA  1 
ATOM   12095 C  C   . GLY K  1 130 ? 56.196 19.213  -40.549  1.00 8.72  ? 130  GLY L C   1 
ATOM   12096 O  O   . GLY K  1 130 ? 56.240 20.386  -40.202  1.00 9.85  ? 130  GLY L O   1 
ATOM   12097 N  N   . ASN K  1 131 ? 56.871 18.744  -41.603  1.00 10.57 ? 131  ASN L N   1 
ATOM   12098 C  CA  . ASN K  1 131 ? 57.464 19.648  -42.614  1.00 11.04 ? 131  ASN L CA  1 
ATOM   12099 C  C   . ASN K  1 131 ? 56.930 19.462  -44.044  1.00 11.37 ? 131  ASN L C   1 
ATOM   12100 O  O   . ASN K  1 131 ? 56.253 18.458  -44.330  1.00 10.85 ? 131  ASN L O   1 
ATOM   12101 C  CB  . ASN K  1 131 ? 59.010 19.623  -42.530  1.00 11.59 ? 131  ASN L CB  1 
ATOM   12102 C  CG  . ASN K  1 131 ? 59.624 18.273  -42.892  1.00 10.14 ? 131  ASN L CG  1 
ATOM   12103 O  OD1 . ASN K  1 131 ? 58.935 17.345  -43.288  1.00 11.66 ? 131  ASN L OD1 1 
ATOM   12104 N  ND2 . ASN K  1 131 ? 60.948 18.176  -42.753  1.00 7.54  ? 131  ASN L ND2 1 
ATOM   12105 N  N   . GLU K  1 132 ? 57.235 20.389  -44.971  1.00 11.03 ? 132  GLU L N   1 
ATOM   12106 C  CA  . GLU K  1 132 ? 56.748 20.229  -46.338  1.00 12.38 ? 132  GLU L CA  1 
ATOM   12107 C  C   . GLU K  1 132 ? 57.247 18.938  -46.953  1.00 11.60 ? 132  GLU L C   1 
ATOM   12108 O  O   . GLU K  1 132 ? 56.486 18.215  -47.618  1.00 12.31 ? 132  GLU L O   1 
ATOM   12109 C  CB  . GLU K  1 132 ? 57.110 21.416  -47.259  1.00 13.04 ? 132  GLU L CB  1 
ATOM   12110 C  CG  . GLU K  1 132 ? 56.542 21.242  -48.700  1.00 16.44 ? 132  GLU L CG  1 
ATOM   12111 C  CD  . GLU K  1 132 ? 57.173 22.193  -49.709  1.00 20.71 ? 132  GLU L CD  1 
ATOM   12112 O  OE1 . GLU K  1 132 ? 57.010 21.968  -50.939  1.00 21.10 ? 132  GLU L OE1 1 
ATOM   12113 O  OE2 . GLU K  1 132 ? 57.841 23.153  -49.274  1.00 20.60 ? 132  GLU L OE2 1 
ATOM   12114 N  N   . GLU K  1 133 ? 58.519 18.632  -46.716  1.00 11.48 ? 133  GLU L N   1 
ATOM   12115 C  CA  . GLU K  1 133 ? 59.112 17.452  -47.326  1.00 11.69 ? 133  GLU L CA  1 
ATOM   12116 C  C   . GLU K  1 133 ? 58.396 16.178  -46.844  1.00 10.44 ? 133  GLU L C   1 
ATOM   12117 O  O   . GLU K  1 133 ? 58.249 15.242  -47.605  1.00 9.69  ? 133  GLU L O   1 
ATOM   12118 C  CB  . GLU K  1 133 ? 60.631 17.427  -47.106  1.00 12.74 ? 133  GLU L CB  1 
ATOM   12119 C  CG  . GLU K  1 133 ? 61.422 16.499  -48.018  1.00 16.52 ? 133  GLU L CG  1 
ATOM   12120 C  CD  . GLU K  1 133 ? 61.380 16.859  -49.515  1.00 20.00 ? 133  GLU L CD  1 
ATOM   12121 O  OE1 . GLU K  1 133 ? 61.947 16.084  -50.319  1.00 21.92 ? 133  GLU L OE1 1 
ATOM   12122 O  OE2 . GLU K  1 133 ? 60.772 17.871  -49.904  1.00 21.62 ? 133  GLU L OE2 1 
ATOM   12123 N  N   . SER K  1 134 ? 57.887 16.164  -45.613  1.00 10.23 ? 134  SER L N   1 
ATOM   12124 C  CA  . SER K  1 134 ? 57.124 14.986  -45.170  1.00 9.50  ? 134  SER L CA  1 
ATOM   12125 C  C   . SER K  1 134 ? 55.894 14.751  -46.072  1.00 9.37  ? 134  SER L C   1 
ATOM   12126 O  O   . SER K  1 134 ? 55.544 13.615  -46.373  1.00 9.04  ? 134  SER L O   1 
ATOM   12127 C  CB  . SER K  1 134 ? 56.714 15.078  -43.694  1.00 9.97  ? 134  SER L CB  1 
ATOM   12128 O  OG  . SER K  1 134 ? 55.954 13.934  -43.331  1.00 7.11  ? 134  SER L OG  1 
ATOM   12129 N  N   . THR K  1 135 ? 55.249 15.835  -46.499  1.00 9.70  ? 135  THR L N   1 
ATOM   12130 C  CA  . THR K  1 135 ? 54.039 15.761  -47.318  1.00 10.18 ? 135  THR L CA  1 
ATOM   12131 C  C   . THR K  1 135 ? 54.339 15.424  -48.780  1.00 10.24 ? 135  THR L C   1 
ATOM   12132 O  O   . THR K  1 135 ? 53.416 15.230  -49.594  1.00 9.94  ? 135  THR L O   1 
ATOM   12133 C  CB  . THR K  1 135 ? 53.237 17.104  -47.272  1.00 10.33 ? 135  THR L CB  1 
ATOM   12134 O  OG1 . THR K  1 135 ? 53.967 18.118  -47.979  1.00 13.91 ? 135  THR L OG1 1 
ATOM   12135 C  CG2 . THR K  1 135 ? 53.000 17.546  -45.875  1.00 11.50 ? 135  THR L CG2 1 
ATOM   12136 N  N   . LYS K  1 136 ? 55.625 15.310  -49.109  1.00 10.08 ? 136  LYS L N   1 
ATOM   12137 C  CA  . LYS K  1 136 ? 56.043 15.021  -50.470  1.00 10.71 ? 136  LYS L CA  1 
ATOM   12138 C  C   . LYS K  1 136 ? 56.734 13.666  -50.607  1.00 10.24 ? 136  LYS L C   1 
ATOM   12139 O  O   . LYS K  1 136 ? 56.399 12.855  -51.474  1.00 9.69  ? 136  LYS L O   1 
ATOM   12140 C  CB  . LYS K  1 136 ? 57.003 16.104  -50.955  1.00 11.60 ? 136  LYS L CB  1 
ATOM   12141 C  CG  . LYS K  1 136 ? 56.353 17.445  -51.219  1.00 14.87 ? 136  LYS L CG  1 
ATOM   12142 C  CD  . LYS K  1 136 ? 57.047 18.153  -52.384  1.00 22.35 ? 136  LYS L CD  1 
ATOM   12143 C  CE  . LYS K  1 136 ? 57.139 17.220  -53.615  1.00 25.78 ? 136  LYS L CE  1 
ATOM   12144 N  NZ  . LYS K  1 136 ? 56.857 17.880  -54.939  1.00 28.48 ? 136  LYS L NZ  1 
ATOM   12145 N  N   . THR K  1 137 ? 57.723 13.443  -49.753  1.00 9.59  ? 137  THR L N   1 
ATOM   12146 C  CA  . THR K  1 137 ? 58.601 12.294  -49.902  1.00 8.98  ? 137  THR L CA  1 
ATOM   12147 C  C   . THR K  1 137 ? 58.661 11.450  -48.648  1.00 8.41  ? 137  THR L C   1 
ATOM   12148 O  O   . THR K  1 137 ? 59.292 10.407  -48.665  1.00 8.40  ? 137  THR L O   1 
ATOM   12149 C  CB  . THR K  1 137 ? 60.051 12.734  -50.168  1.00 9.00  ? 137  THR L CB  1 
ATOM   12150 O  OG1 . THR K  1 137 ? 60.550 13.410  -49.004  1.00 8.80  ? 137  THR L OG1 1 
ATOM   12151 C  CG2 . THR K  1 137 ? 60.136 13.650  -51.383  1.00 8.68  ? 137  THR L CG2 1 
ATOM   12152 N  N   . GLY K  1 138 ? 58.053 11.929  -47.562  1.00 7.41  ? 138  GLY L N   1 
ATOM   12153 C  CA  . GLY K  1 138 ? 58.120 11.252  -46.255  1.00 6.56  ? 138  GLY L CA  1 
ATOM   12154 C  C   . GLY K  1 138 ? 59.516 11.342  -45.654  1.00 5.85  ? 138  GLY L C   1 
ATOM   12155 O  O   . GLY K  1 138 ? 59.852 10.597  -44.724  1.00 5.33  ? 138  GLY L O   1 
ATOM   12156 N  N   . ASN K  1 139 ? 60.331 12.250  -46.197  1.00 5.00  ? 139  ASN L N   1 
ATOM   12157 C  CA  . ASN K  1 139 ? 61.731 12.447  -45.754  1.00 5.53  ? 139  ASN L CA  1 
ATOM   12158 C  C   . ASN K  1 139 ? 62.569 11.193  -45.923  1.00 5.76  ? 139  ASN L C   1 
ATOM   12159 O  O   . ASN K  1 139 ? 63.476 10.952  -45.141  1.00 5.29  ? 139  ASN L O   1 
ATOM   12160 C  CB  . ASN K  1 139 ? 61.782 12.939  -44.298  1.00 5.35  ? 139  ASN L CB  1 
ATOM   12161 C  CG  . ASN K  1 139 ? 61.277 14.333  -44.164  1.00 7.55  ? 139  ASN L CG  1 
ATOM   12162 O  OD1 . ASN K  1 139 ? 61.873 15.262  -44.712  1.00 8.72  ? 139  ASN L OD1 1 
ATOM   12163 N  ND2 . ASN K  1 139 ? 60.170 14.504  -43.466  1.00 6.51  ? 139  ASN L ND2 1 
ATOM   12164 N  N   . ALA K  1 140 ? 62.252 10.406  -46.956  1.00 6.59  ? 140  ALA L N   1 
ATOM   12165 C  CA  . ALA K  1 140 ? 62.879 9.101   -47.156  1.00 6.91  ? 140  ALA L CA  1 
ATOM   12166 C  C   . ALA K  1 140 ? 64.283 9.238   -47.717  1.00 7.37  ? 140  ALA L C   1 
ATOM   12167 O  O   . ALA K  1 140 ? 65.009 8.261   -47.794  1.00 7.41  ? 140  ALA L O   1 
ATOM   12168 C  CB  . ALA K  1 140 ? 62.010 8.215   -48.080  1.00 7.23  ? 140  ALA L CB  1 
ATOM   12169 N  N   . GLY K  1 141 ? 64.650 10.440  -48.145  1.00 7.43  ? 141  GLY L N   1 
ATOM   12170 C  CA  . GLY K  1 141 ? 66.043 10.706  -48.538  1.00 9.24  ? 141  GLY L CA  1 
ATOM   12171 C  C   . GLY K  1 141 ? 66.404 10.195  -49.924  1.00 9.29  ? 141  GLY L C   1 
ATOM   12172 O  O   . GLY K  1 141 ? 65.541 10.053  -50.796  1.00 9.15  ? 141  GLY L O   1 
ATOM   12173 N  N   . SER K  1 142 ? 67.690 9.940   -50.146  1.00 9.84  ? 142  SER L N   1 
ATOM   12174 C  CA  . SER K  1 142 ? 68.178 9.667   -51.510  1.00 10.67 ? 142  SER L CA  1 
ATOM   12175 C  C   . SER K  1 142 ? 67.595 8.380   -52.087  1.00 10.73 ? 142  SER L C   1 
ATOM   12176 O  O   . SER K  1 142 ? 67.084 7.528   -51.352  1.00 10.35 ? 142  SER L O   1 
ATOM   12177 C  CB  . SER K  1 142 ? 69.716 9.615   -51.554  1.00 10.91 ? 142  SER L CB  1 
ATOM   12178 O  OG  . SER K  1 142 ? 70.175 8.345   -51.094  1.00 12.07 ? 142  SER L OG  1 
ATOM   12179 N  N   . ARG K  1 143 ? 67.674 8.242   -53.414  1.00 10.74 ? 143  ARG L N   1 
ATOM   12180 C  CA  . ARG K  1 143 ? 67.201 7.027   -54.083  1.00 11.72 ? 143  ARG L CA  1 
ATOM   12181 C  C   . ARG K  1 143 ? 68.357 6.044   -54.279  1.00 11.70 ? 143  ARG L C   1 
ATOM   12182 O  O   . ARG K  1 143 ? 69.246 6.283   -55.102  1.00 11.79 ? 143  ARG L O   1 
ATOM   12183 C  CB  . ARG K  1 143 ? 66.560 7.399   -55.417  1.00 11.70 ? 143  ARG L CB  1 
ATOM   12184 C  CG  . ARG K  1 143 ? 65.495 8.477   -55.251  1.00 13.20 ? 143  ARG L CG  1 
ATOM   12185 C  CD  . ARG K  1 143 ? 65.022 9.052   -56.567  1.00 12.52 ? 143  ARG L CD  1 
ATOM   12186 N  NE  . ARG K  1 143 ? 64.149 10.179  -56.273  1.00 13.83 ? 143  ARG L NE  1 
ATOM   12187 C  CZ  . ARG K  1 143 ? 63.259 10.701  -57.109  1.00 14.69 ? 143  ARG L CZ  1 
ATOM   12188 N  NH1 . ARG K  1 143 ? 62.503 11.727  -56.699  1.00 14.67 ? 143  ARG L NH1 1 
ATOM   12189 N  NH2 . ARG K  1 143 ? 63.113 10.210  -58.338  1.00 12.81 ? 143  ARG L NH2 1 
ATOM   12190 N  N   . LEU K  1 144 ? 68.335 4.952   -53.520  1.00 11.86 ? 144  LEU L N   1 
ATOM   12191 C  CA  . LEU K  1 144 ? 69.423 3.944   -53.526  1.00 12.23 ? 144  LEU L CA  1 
ATOM   12192 C  C   . LEU K  1 144 ? 69.429 2.988   -54.712  1.00 12.88 ? 144  LEU L C   1 
ATOM   12193 O  O   . LEU K  1 144 ? 70.490 2.525   -55.165  1.00 12.70 ? 144  LEU L O   1 
ATOM   12194 C  CB  . LEU K  1 144 ? 69.371 3.107   -52.248  1.00 12.21 ? 144  LEU L CB  1 
ATOM   12195 C  CG  . LEU K  1 144 ? 69.458 3.837   -50.902  1.00 12.32 ? 144  LEU L CG  1 
ATOM   12196 C  CD1 . LEU K  1 144 ? 69.499 2.813   -49.777  1.00 12.15 ? 144  LEU L CD1 1 
ATOM   12197 C  CD2 . LEU K  1 144 ? 70.647 4.778   -50.822  1.00 13.92 ? 144  LEU L CD2 1 
ATOM   12198 N  N   . ALA K  1 145 ? 68.236 2.640   -55.186  1.00 12.25 ? 145  ALA L N   1 
ATOM   12199 C  CA  . ALA K  1 145 ? 68.104 1.735   -56.311  1.00 12.36 ? 145  ALA L CA  1 
ATOM   12200 C  C   . ALA K  1 145 ? 66.696 1.882   -56.840  1.00 12.33 ? 145  ALA L C   1 
ATOM   12201 O  O   . ALA K  1 145 ? 65.770 2.239   -56.087  1.00 11.42 ? 145  ALA L O   1 
ATOM   12202 C  CB  . ALA K  1 145 ? 68.374 0.297   -55.903  1.00 11.76 ? 145  ALA L CB  1 
ATOM   12203 N  N   . CYS K  1 146 ? 66.559 1.627   -58.140  1.00 12.38 ? 146  CYS L N   1 
ATOM   12204 C  CA  . CYS K  1 146 ? 65.286 1.742   -58.839  1.00 12.07 ? 146  CYS L CA  1 
ATOM   12205 C  C   . CYS K  1 146 ? 65.230 0.811   -60.056  1.00 14.05 ? 146  CYS L C   1 
ATOM   12206 O  O   . CYS K  1 146 ? 66.260 0.270   -60.513  1.00 13.42 ? 146  CYS L O   1 
ATOM   12207 C  CB  . CYS K  1 146 ? 65.005 3.194   -59.253  0.40 11.85 ? 146  CYS L CB  1 
ATOM   12208 S  SG  . CYS K  1 146 ? 66.215 4.013   -60.317  0.40 8.92  ? 146  CYS L SG  1 
ATOM   12209 N  N   . GLY K  1 147 ? 64.018 0.629   -60.572  1.00 14.06 ? 147  GLY L N   1 
ATOM   12210 C  CA  . GLY K  1 147 ? 63.820 -0.041  -61.843  1.00 14.98 ? 147  GLY L CA  1 
ATOM   12211 C  C   . GLY K  1 147 ? 62.483 0.350   -62.445  1.00 15.62 ? 147  GLY L C   1 
ATOM   12212 O  O   . GLY K  1 147 ? 61.588 0.826   -61.752  1.00 15.46 ? 147  GLY L O   1 
ATOM   12213 N  N   . VAL K  1 148 ? 62.356 0.167   -63.750  1.00 15.82 ? 148  VAL L N   1 
ATOM   12214 C  CA  . VAL K  1 148 ? 61.071 0.313   -64.405  1.00 16.01 ? 148  VAL L CA  1 
ATOM   12215 C  C   . VAL K  1 148 ? 60.263 -0.977  -64.191  1.00 16.52 ? 148  VAL L C   1 
ATOM   12216 O  O   . VAL K  1 148 ? 60.799 -2.088  -64.328  1.00 16.88 ? 148  VAL L O   1 
ATOM   12217 C  CB  . VAL K  1 148 ? 61.263 0.677   -65.910  1.00 16.08 ? 148  VAL L CB  1 
ATOM   12218 C  CG1 . VAL K  1 148 ? 59.909 0.960   -66.584  1.00 15.73 ? 148  VAL L CG1 1 
ATOM   12219 C  CG2 . VAL K  1 148 ? 62.180 1.880   -66.048  1.00 15.30 ? 148  VAL L CG2 1 
ATOM   12220 N  N   . ILE K  1 149 ? 58.988 -0.837  -63.812  1.00 16.22 ? 149  ILE L N   1 
ATOM   12221 C  CA  . ILE K  1 149 ? 58.128 -1.985  -63.560  1.00 16.60 ? 149  ILE L CA  1 
ATOM   12222 C  C   . ILE K  1 149 ? 57.585 -2.545  -64.887  1.00 17.65 ? 149  ILE L C   1 
ATOM   12223 O  O   . ILE K  1 149 ? 56.886 -1.846  -65.628  1.00 17.77 ? 149  ILE L O   1 
ATOM   12224 C  CB  . ILE K  1 149 ? 56.930 -1.641  -62.639  1.00 16.14 ? 149  ILE L CB  1 
ATOM   12225 C  CG1 . ILE K  1 149 ? 57.408 -1.164  -61.260  1.00 15.16 ? 149  ILE L CG1 1 
ATOM   12226 C  CG2 . ILE K  1 149 ? 56.019 -2.853  -62.458  1.00 15.90 ? 149  ILE L CG2 1 
ATOM   12227 C  CD1 . ILE K  1 149 ? 56.273 -0.631  -60.378  1.00 14.41 ? 149  ILE L CD1 1 
ATOM   12228 N  N   . GLY K  1 150 ? 57.881 -3.808  -65.147  1.00 18.33 ? 150  GLY L N   1 
ATOM   12229 C  CA  . GLY K  1 150 ? 57.571 -4.413  -66.449  1.00 19.57 ? 150  GLY L CA  1 
ATOM   12230 C  C   . GLY K  1 150 ? 56.508 -5.474  -66.345  1.00 20.55 ? 150  GLY L C   1 
ATOM   12231 O  O   . GLY K  1 150 ? 56.401 -6.172  -65.341  1.00 19.93 ? 150  GLY L O   1 
ATOM   12232 N  N   . ILE K  1 151 ? 55.717 -5.613  -67.406  1.00 21.90 ? 151  ILE L N   1 
ATOM   12233 C  CA  . ILE K  1 151 ? 54.749 -6.681  -67.453  1.00 23.51 ? 151  ILE L CA  1 
ATOM   12234 C  C   . ILE K  1 151 ? 55.520 -8.005  -67.527  1.00 24.56 ? 151  ILE L C   1 
ATOM   12235 O  O   . ILE K  1 151 ? 56.580 -8.083  -68.165  1.00 25.16 ? 151  ILE L O   1 
ATOM   12236 C  CB  . ILE K  1 151 ? 53.700 -6.459  -68.595  1.00 23.67 ? 151  ILE L CB  1 
ATOM   12237 C  CG1 . ILE K  1 151 ? 52.537 -7.446  -68.461  1.00 24.97 ? 151  ILE L CG1 1 
ATOM   12238 C  CG2 . ILE K  1 151 ? 54.360 -6.473  -69.978  1.00 23.34 ? 151  ILE L CG2 1 
ATOM   12239 C  CD1 . ILE K  1 151 ? 51.176 -6.897  -68.937  1.00 26.44 ? 151  ILE L CD1 1 
ATOM   12240 N  N   . ALA K  1 152 ? 55.023 -9.016  -66.829  1.00 25.66 ? 152  ALA L N   1 
ATOM   12241 C  CA  . ALA K  1 152 ? 55.715 -10.290 -66.715  1.00 27.29 ? 152  ALA L CA  1 
ATOM   12242 C  C   . ALA K  1 152 ? 54.846 -11.433 -67.203  1.00 28.57 ? 152  ALA L C   1 
ATOM   12243 O  O   . ALA K  1 152 ? 53.617 -11.321 -67.237  1.00 28.72 ? 152  ALA L O   1 
ATOM   12244 C  CB  . ALA K  1 152 ? 56.147 -10.542 -65.278  1.00 26.89 ? 152  ALA L CB  1 
ATOM   12245 N  N   . GLN K  1 153 ? 55.503 -12.532 -67.569  1.00 30.02 ? 153  GLN L N   1 
ATOM   12246 C  CA  . GLN K  1 153 ? 54.827 -13.753 -68.012  1.00 31.53 ? 153  GLN L CA  1 
ATOM   12247 C  C   . GLN K  1 153 ? 53.797 -14.238 -67.002  1.00 31.56 ? 153  GLN L C   1 
ATOM   12248 O  O   . GLN K  1 153 ? 54.110 -14.549 -65.851  1.00 31.96 ? 153  GLN L O   1 
ATOM   12249 C  CB  . GLN K  1 153 ? 55.851 -14.855 -68.301  1.00 31.71 ? 153  GLN L CB  1 
ATOM   12250 C  CG  . GLN K  1 153 ? 55.267 -16.134 -68.876  1.00 33.85 ? 153  GLN L CG  1 
ATOM   12251 C  CD  . GLN K  1 153 ? 56.254 -16.846 -69.781  1.00 36.28 ? 153  GLN L CD  1 
ATOM   12252 O  OE1 . GLN K  1 153 ? 56.024 -16.971 -70.984  1.00 37.91 ? 153  GLN L OE1 1 
ATOM   12253 N  NE2 . GLN K  1 153 ? 57.373 -17.289 -69.212  1.00 37.02 ? 153  GLN L NE2 1 
ATOM   12254 O  OXT . GLN K  1 153 ? 52.619 -14.324 -67.344  1.00 32.04 ? 153  GLN L OXT 1 
ATOM   12255 N  N   . ALA L  1 1   ? 49.778 14.905  -76.362  1.00 35.30 ? 1    ALA M N   1 
ATOM   12256 C  CA  . ALA L  1 1   ? 50.907 13.994  -76.739  1.00 35.03 ? 1    ALA M CA  1 
ATOM   12257 C  C   . ALA L  1 1   ? 51.294 13.054  -75.597  1.00 35.03 ? 1    ALA M C   1 
ATOM   12258 O  O   . ALA L  1 1   ? 51.232 13.425  -74.415  1.00 35.11 ? 1    ALA M O   1 
ATOM   12259 C  CB  . ALA L  1 1   ? 52.125 14.802  -77.200  1.00 35.25 ? 1    ALA M CB  1 
ATOM   12260 N  N   . THR L  1 2   ? 51.673 11.834  -75.962  1.00 34.31 ? 2    THR M N   1 
ATOM   12261 C  CA  . THR L  1 2   ? 52.181 10.863  -75.005  1.00 33.66 ? 2    THR M CA  1 
ATOM   12262 C  C   . THR L  1 2   ? 53.659 10.662  -75.313  1.00 33.26 ? 2    THR M C   1 
ATOM   12263 O  O   . THR L  1 2   ? 54.080 10.765  -76.472  1.00 32.99 ? 2    THR M O   1 
ATOM   12264 C  CB  . THR L  1 2   ? 51.405 9.529   -75.089  1.00 33.86 ? 2    THR M CB  1 
ATOM   12265 O  OG1 . THR L  1 2   ? 50.002 9.789   -74.961  1.00 33.79 ? 2    THR M OG1 1 
ATOM   12266 C  CG2 . THR L  1 2   ? 51.820 8.571   -73.975  1.00 33.91 ? 2    THR M CG2 1 
ATOM   12267 N  N   . LYS L  1 3   ? 54.446 10.398  -74.276  1.00 32.26 ? 3    LYS M N   1 
ATOM   12268 C  CA  . LYS L  1 3   ? 55.883 10.224  -74.432  1.00 31.98 ? 3    LYS M CA  1 
ATOM   12269 C  C   . LYS L  1 3   ? 56.370 9.007   -73.659  1.00 31.29 ? 3    LYS M C   1 
ATOM   12270 O  O   . LYS L  1 3   ? 55.880 8.703   -72.568  1.00 30.61 ? 3    LYS M O   1 
ATOM   12271 C  CB  . LYS L  1 3   ? 56.625 11.476  -73.959  1.00 32.26 ? 3    LYS M CB  1 
ATOM   12272 C  CG  . LYS L  1 3   ? 56.567 12.659  -74.920  1.00 33.91 ? 3    LYS M CG  1 
ATOM   12273 C  CD  . LYS L  1 3   ? 57.327 13.887  -74.393  1.00 35.84 ? 3    LYS M CD  1 
ATOM   12274 C  CE  . LYS L  1 3   ? 58.850 13.710  -74.427  1.00 36.28 ? 3    LYS M CE  1 
ATOM   12275 N  NZ  . LYS L  1 3   ? 59.400 13.456  -75.790  1.00 37.19 ? 3    LYS M NZ  1 
ATOM   12276 N  N   . ALA L  1 4   ? 57.327 8.298   -74.236  1.00 30.48 ? 4    ALA M N   1 
ATOM   12277 C  CA  . ALA L  1 4   ? 58.007 7.244   -73.509  1.00 30.33 ? 4    ALA M CA  1 
ATOM   12278 C  C   . ALA L  1 4   ? 59.521 7.317   -73.728  1.00 30.65 ? 4    ALA M C   1 
ATOM   12279 O  O   . ALA L  1 4   ? 60.011 8.150   -74.505  1.00 30.09 ? 4    ALA M O   1 
ATOM   12280 C  CB  . ALA L  1 4   ? 57.448 5.883   -73.868  1.00 29.83 ? 4    ALA M CB  1 
ATOM   12281 N  N   . VAL L  1 5   ? 60.253 6.478   -72.997  1.00 31.32 ? 5    VAL M N   1 
ATOM   12282 C  CA  . VAL L  1 5   ? 61.712 6.452   -73.060  1.00 31.49 ? 5    VAL M CA  1 
ATOM   12283 C  C   . VAL L  1 5   ? 62.198 5.060   -72.684  1.00 31.98 ? 5    VAL M C   1 
ATOM   12284 O  O   . VAL L  1 5   ? 61.478 4.302   -72.048  1.00 32.37 ? 5    VAL M O   1 
ATOM   12285 C  CB  . VAL L  1 5   ? 62.364 7.547   -72.169  1.00 31.47 ? 5    VAL M CB  1 
ATOM   12286 C  CG1 . VAL L  1 5   ? 62.165 7.251   -70.683  1.00 30.68 ? 5    VAL M CG1 1 
ATOM   12287 C  CG2 . VAL L  1 5   ? 63.858 7.701   -72.499  1.00 31.13 ? 5    VAL M CG2 1 
ATOM   12288 N  N   . CYS L  1 6   ? 63.420 4.728   -73.091  1.00 32.80 ? 6    CYS M N   1 
ATOM   12289 C  CA  . CYS L  1 6   ? 63.984 3.408   -72.837  1.00 33.27 ? 6    CYS M CA  1 
ATOM   12290 C  C   . CYS L  1 6   ? 65.515 3.442   -72.787  1.00 33.93 ? 6    CYS M C   1 
ATOM   12291 O  O   . CYS L  1 6   ? 66.165 4.066   -73.642  1.00 33.67 ? 6    CYS M O   1 
ATOM   12292 C  CB  . CYS L  1 6   ? 63.506 2.427   -73.902  1.00 33.65 ? 6    CYS M CB  1 
ATOM   12293 S  SG  . CYS L  1 6   ? 64.142 0.771   -73.736  1.00 33.47 ? 6    CYS M SG  1 
ATOM   12294 N  N   . VAL L  1 7   ? 66.072 2.778   -71.774  1.00 34.15 ? 7    VAL M N   1 
ATOM   12295 C  CA  . VAL L  1 7   ? 67.514 2.679   -71.597  1.00 34.41 ? 7    VAL M CA  1 
ATOM   12296 C  C   . VAL L  1 7   ? 67.920 1.286   -71.992  1.00 35.13 ? 7    VAL M C   1 
ATOM   12297 O  O   . VAL L  1 7   ? 67.541 0.305   -71.348  1.00 34.94 ? 7    VAL M O   1 
ATOM   12298 C  CB  . VAL L  1 7   ? 67.972 2.955   -70.142  1.00 34.32 ? 7    VAL M CB  1 
ATOM   12299 C  CG1 . VAL L  1 7   ? 69.497 2.812   -70.021  1.00 33.77 ? 7    VAL M CG1 1 
ATOM   12300 C  CG2 . VAL L  1 7   ? 67.538 4.336   -69.694  1.00 33.57 ? 7    VAL M CG2 1 
ATOM   12301 N  N   . LEU L  1 8   ? 68.676 1.220   -73.085  1.00 36.07 ? 8    LEU M N   1 
ATOM   12302 C  CA  . LEU L  1 8   ? 69.218 -0.025  -73.590  1.00 36.87 ? 8    LEU M CA  1 
ATOM   12303 C  C   . LEU L  1 8   ? 70.571 -0.289  -72.940  1.00 37.47 ? 8    LEU M C   1 
ATOM   12304 O  O   . LEU L  1 8   ? 71.494 0.518   -73.060  1.00 37.65 ? 8    LEU M O   1 
ATOM   12305 C  CB  . LEU L  1 8   ? 69.351 0.038   -75.117  1.00 36.74 ? 8    LEU M CB  1 
ATOM   12306 C  CG  . LEU L  1 8   ? 68.051 0.025   -75.932  1.00 36.22 ? 8    LEU M CG  1 
ATOM   12307 C  CD1 . LEU L  1 8   ? 68.333 0.423   -77.371  1.00 36.57 ? 8    LEU M CD1 1 
ATOM   12308 C  CD2 . LEU L  1 8   ? 67.391 -1.346  -75.885  1.00 35.86 ? 8    LEU M CD2 1 
ATOM   12309 N  N   . LYS L  1 9   ? 70.654 -1.413  -72.236  1.00 38.24 ? 9    LYS M N   1 
ATOM   12310 C  CA  . LYS L  1 9   ? 71.866 -1.866  -71.556  1.00 39.19 ? 9    LYS M CA  1 
ATOM   12311 C  C   . LYS L  1 9   ? 71.920 -3.388  -71.630  1.00 39.57 ? 9    LYS M C   1 
ATOM   12312 O  O   . LYS L  1 9   ? 70.887 -4.052  -71.722  1.00 39.54 ? 9    LYS M O   1 
ATOM   12313 C  CB  . LYS L  1 9   ? 71.882 -1.426  -70.079  1.00 39.22 ? 9    LYS M CB  1 
ATOM   12314 C  CG  . LYS L  1 9   ? 71.933 0.088   -69.827  1.00 40.55 ? 9    LYS M CG  1 
ATOM   12315 C  CD  . LYS L  1 9   ? 73.253 0.730   -70.268  1.00 42.84 ? 9    LYS M CD  1 
ATOM   12316 C  CE  . LYS L  1 9   ? 74.154 1.068   -69.087  1.00 44.61 ? 9    LYS M CE  1 
ATOM   12317 N  NZ  . LYS L  1 9   ? 73.875 2.448   -68.579  1.00 45.40 ? 9    LYS M NZ  1 
ATOM   12318 N  N   . GLY L  1 10  ? 73.131 -3.934  -71.599  1.00 40.23 ? 10   GLY M N   1 
ATOM   12319 C  CA  . GLY L  1 10  ? 73.339 -5.382  -71.585  1.00 41.00 ? 10   GLY M CA  1 
ATOM   12320 C  C   . GLY L  1 10  ? 74.725 -5.698  -71.058  1.00 41.61 ? 10   GLY M C   1 
ATOM   12321 O  O   . GLY L  1 10  ? 75.351 -4.854  -70.410  1.00 41.62 ? 10   GLY M O   1 
ATOM   12322 N  N   . ASP L  1 11  ? 75.213 -6.903  -71.355  1.00 42.09 ? 11   ASP M N   1 
ATOM   12323 C  CA  . ASP L  1 11  ? 76.516 -7.380  -70.858  1.00 42.66 ? 11   ASP M CA  1 
ATOM   12324 C  C   . ASP L  1 11  ? 77.740 -6.726  -71.516  1.00 42.60 ? 11   ASP M C   1 
ATOM   12325 O  O   . ASP L  1 11  ? 78.715 -6.389  -70.829  1.00 42.76 ? 11   ASP M O   1 
ATOM   12326 C  CB  . ASP L  1 11  ? 76.623 -8.900  -71.013  1.00 42.98 ? 11   ASP M CB  1 
ATOM   12327 C  CG  . ASP L  1 11  ? 75.487 -9.639  -70.339  1.00 43.98 ? 11   ASP M CG  1 
ATOM   12328 O  OD1 . ASP L  1 11  ? 75.009 -10.640 -70.922  1.00 45.36 ? 11   ASP M OD1 1 
ATOM   12329 O  OD2 . ASP L  1 11  ? 75.073 -9.226  -69.232  1.00 44.95 ? 11   ASP M OD2 1 
ATOM   12330 N  N   . GLY L  1 12  ? 77.693 -6.571  -72.840  1.00 42.20 ? 12   GLY M N   1 
ATOM   12331 C  CA  . GLY L  1 12  ? 78.821 -6.051  -73.617  1.00 41.88 ? 12   GLY M CA  1 
ATOM   12332 C  C   . GLY L  1 12  ? 78.895 -4.535  -73.597  1.00 41.66 ? 12   GLY M C   1 
ATOM   12333 O  O   . GLY L  1 12  ? 78.409 -3.910  -72.655  1.00 41.69 ? 12   GLY M O   1 
ATOM   12334 N  N   . PRO L  1 13  ? 79.491 -3.929  -74.646  1.00 41.39 ? 13   PRO M N   1 
ATOM   12335 C  CA  . PRO L  1 13  ? 79.650 -2.471  -74.742  1.00 41.07 ? 13   PRO M CA  1 
ATOM   12336 C  C   . PRO L  1 13  ? 78.417 -1.720  -75.273  1.00 40.87 ? 13   PRO M C   1 
ATOM   12337 O  O   . PRO L  1 13  ? 78.430 -0.486  -75.346  1.00 40.62 ? 13   PRO M O   1 
ATOM   12338 C  CB  . PRO L  1 13  ? 80.805 -2.323  -75.736  1.00 41.13 ? 13   PRO M CB  1 
ATOM   12339 C  CG  . PRO L  1 13  ? 80.658 -3.497  -76.645  1.00 41.06 ? 13   PRO M CG  1 
ATOM   12340 C  CD  . PRO L  1 13  ? 80.106 -4.624  -75.797  1.00 41.33 ? 13   PRO M CD  1 
ATOM   12341 N  N   . VAL L  1 14  ? 77.367 -2.451  -75.631  1.00 40.56 ? 14   VAL M N   1 
ATOM   12342 C  CA  . VAL L  1 14  ? 76.219 -1.859  -76.325  1.00 40.41 ? 14   VAL M CA  1 
ATOM   12343 C  C   . VAL L  1 14  ? 75.238 -1.116  -75.400  1.00 40.06 ? 14   VAL M C   1 
ATOM   12344 O  O   . VAL L  1 14  ? 74.637 -1.720  -74.511  1.00 39.74 ? 14   VAL M O   1 
ATOM   12345 C  CB  . VAL L  1 14  ? 75.475 -2.925  -77.152  1.00 40.41 ? 14   VAL M CB  1 
ATOM   12346 C  CG1 . VAL L  1 14  ? 74.383 -2.285  -77.983  1.00 40.24 ? 14   VAL M CG1 1 
ATOM   12347 C  CG2 . VAL L  1 14  ? 76.468 -3.666  -78.048  1.00 40.79 ? 14   VAL M CG2 1 
ATOM   12348 N  N   . GLN L  1 15  ? 75.081 0.192   -75.638  1.00 39.96 ? 15   GLN M N   1 
ATOM   12349 C  CA  . GLN L  1 15  ? 74.181 1.047   -74.842  1.00 39.89 ? 15   GLN M CA  1 
ATOM   12350 C  C   . GLN L  1 15  ? 73.627 2.272   -75.601  1.00 39.39 ? 15   GLN M C   1 
ATOM   12351 O  O   . GLN L  1 15  ? 74.218 2.722   -76.585  1.00 38.91 ? 15   GLN M O   1 
ATOM   12352 C  CB  . GLN L  1 15  ? 74.865 1.500   -73.543  1.00 40.04 ? 15   GLN M CB  1 
ATOM   12353 C  CG  . GLN L  1 15  ? 75.951 2.562   -73.721  1.00 40.94 ? 15   GLN M CG  1 
ATOM   12354 C  CD  . GLN L  1 15  ? 76.760 2.796   -72.461  1.00 42.45 ? 15   GLN M CD  1 
ATOM   12355 O  OE1 . GLN L  1 15  ? 77.933 3.176   -72.527  1.00 43.45 ? 15   GLN M OE1 1 
ATOM   12356 N  NE2 . GLN L  1 15  ? 76.144 2.563   -71.303  1.00 42.95 ? 15   GLN M NE2 1 
ATOM   12357 N  N   . GLY L  1 16  ? 72.501 2.809   -75.120  1.00 38.75 ? 16   GLY M N   1 
ATOM   12358 C  CA  . GLY L  1 16  ? 71.907 4.026   -75.683  1.00 38.44 ? 16   GLY M CA  1 
ATOM   12359 C  C   . GLY L  1 16  ? 70.535 4.385   -75.121  1.00 38.28 ? 16   GLY M C   1 
ATOM   12360 O  O   . GLY L  1 16  ? 69.931 3.599   -74.386  1.00 38.32 ? 16   GLY M O   1 
ATOM   12361 N  N   . ILE L  1 17  ? 70.059 5.580   -75.484  1.00 37.76 ? 17   ILE M N   1 
ATOM   12362 C  CA  . ILE L  1 17  ? 68.762 6.115   -75.060  1.00 36.99 ? 17   ILE M CA  1 
ATOM   12363 C  C   . ILE L  1 17  ? 67.823 6.312   -76.262  1.00 37.04 ? 17   ILE M C   1 
ATOM   12364 O  O   . ILE L  1 17  ? 68.161 7.027   -77.218  1.00 36.48 ? 17   ILE M O   1 
ATOM   12365 C  CB  . ILE L  1 17  ? 68.930 7.461   -74.315  1.00 37.21 ? 17   ILE M CB  1 
ATOM   12366 C  CG1 . ILE L  1 17  ? 69.793 7.279   -73.056  1.00 36.64 ? 17   ILE M CG1 1 
ATOM   12367 C  CG2 . ILE L  1 17  ? 67.560 8.074   -73.969  1.00 36.78 ? 17   ILE M CG2 1 
ATOM   12368 C  CD1 . ILE L  1 17  ? 70.303 8.571   -72.457  1.00 36.72 ? 17   ILE M CD1 1 
ATOM   12369 N  N   . ILE L  1 18  ? 66.648 5.684   -76.187  1.00 36.55 ? 18   ILE M N   1 
ATOM   12370 C  CA  . ILE L  1 18  ? 65.643 5.712   -77.254  1.00 36.43 ? 18   ILE M CA  1 
ATOM   12371 C  C   . ILE L  1 18  ? 64.351 6.387   -76.776  1.00 36.16 ? 18   ILE M C   1 
ATOM   12372 O  O   . ILE L  1 18  ? 63.726 5.928   -75.819  1.00 35.97 ? 18   ILE M O   1 
ATOM   12373 C  CB  . ILE L  1 18  ? 65.337 4.271   -77.769  1.00 36.27 ? 18   ILE M CB  1 
ATOM   12374 C  CG1 . ILE L  1 18  ? 66.589 3.621   -78.382  1.00 36.81 ? 18   ILE M CG1 1 
ATOM   12375 C  CG2 . ILE L  1 18  ? 64.158 4.262   -78.764  1.00 36.78 ? 18   ILE M CG2 1 
ATOM   12376 C  CD1 . ILE L  1 18  ? 67.149 4.322   -79.636  1.00 37.18 ? 18   ILE M CD1 1 
ATOM   12377 N  N   . ASN L  1 19  ? 63.968 7.474   -77.450  1.00 35.86 ? 19   ASN M N   1 
ATOM   12378 C  CA  . ASN L  1 19  ? 62.758 8.232   -77.127  1.00 35.36 ? 19   ASN M CA  1 
ATOM   12379 C  C   . ASN L  1 19  ? 61.560 7.806   -77.974  1.00 35.17 ? 19   ASN M C   1 
ATOM   12380 O  O   . ASN L  1 19  ? 61.713 7.388   -79.121  1.00 34.52 ? 19   ASN M O   1 
ATOM   12381 C  CB  . ASN L  1 19  ? 62.982 9.744   -77.304  1.00 35.47 ? 19   ASN M CB  1 
ATOM   12382 C  CG  . ASN L  1 19  ? 64.192 10.273  -76.534  1.00 36.07 ? 19   ASN M CG  1 
ATOM   12383 O  OD1 . ASN L  1 19  ? 64.253 10.189  -75.309  1.00 35.48 ? 19   ASN M OD1 1 
ATOM   12384 N  ND2 . ASN L  1 19  ? 65.155 10.846  -77.263  1.00 35.91 ? 19   ASN M ND2 1 
ATOM   12385 N  N   . PHE L  1 20  ? 60.370 7.919   -77.387  1.00 34.79 ? 20   PHE M N   1 
ATOM   12386 C  CA  . PHE L  1 20  ? 59.106 7.700   -78.089  1.00 34.78 ? 20   PHE M CA  1 
ATOM   12387 C  C   . PHE L  1 20  ? 58.214 8.923   -77.890  1.00 34.85 ? 20   PHE M C   1 
ATOM   12388 O  O   . PHE L  1 20  ? 58.120 9.466   -76.777  1.00 34.36 ? 20   PHE M O   1 
ATOM   12389 C  CB  . PHE L  1 20  ? 58.361 6.480   -77.536  1.00 34.91 ? 20   PHE M CB  1 
ATOM   12390 C  CG  . PHE L  1 20  ? 59.123 5.186   -77.625  1.00 34.85 ? 20   PHE M CG  1 
ATOM   12391 C  CD1 . PHE L  1 20  ? 58.859 4.280   -78.645  1.00 34.76 ? 20   PHE M CD1 1 
ATOM   12392 C  CD2 . PHE L  1 20  ? 60.088 4.857   -76.667  1.00 34.44 ? 20   PHE M CD2 1 
ATOM   12393 C  CE1 . PHE L  1 20  ? 59.545 3.069   -78.722  1.00 34.16 ? 20   PHE M CE1 1 
ATOM   12394 C  CE2 . PHE L  1 20  ? 60.777 3.654   -76.733  1.00 34.11 ? 20   PHE M CE2 1 
ATOM   12395 C  CZ  . PHE L  1 20  ? 60.511 2.759   -77.764  1.00 34.62 ? 20   PHE M CZ  1 
ATOM   12396 N  N   . GLU L  1 21  ? 57.562 9.357   -78.965  1.00 34.38 ? 21   GLU M N   1 
ATOM   12397 C  CA  . GLU L  1 21  ? 56.493 10.338  -78.858  1.00 34.49 ? 21   GLU M CA  1 
ATOM   12398 C  C   . GLU L  1 21  ? 55.342 9.964   -79.791  1.00 34.13 ? 21   GLU M C   1 
ATOM   12399 O  O   . GLU L  1 21  ? 55.553 9.353   -80.841  1.00 33.71 ? 21   GLU M O   1 
ATOM   12400 C  CB  . GLU L  1 21  ? 57.006 11.750  -79.139  1.00 34.84 ? 21   GLU M CB  1 
ATOM   12401 C  CG  . GLU L  1 21  ? 56.004 12.848  -78.795  1.00 37.21 ? 21   GLU M CG  1 
ATOM   12402 C  CD  . GLU L  1 21  ? 56.607 14.238  -78.833  1.00 40.70 ? 21   GLU M CD  1 
ATOM   12403 O  OE1 . GLU L  1 21  ? 56.424 14.992  -77.844  1.00 42.24 ? 21   GLU M OE1 1 
ATOM   12404 O  OE2 . GLU L  1 21  ? 57.267 14.578  -79.842  1.00 42.57 ? 21   GLU M OE2 1 
ATOM   12405 N  N   . GLN L  1 22  ? 54.127 10.313  -79.384  1.00 33.48 ? 22   GLN M N   1 
ATOM   12406 C  CA  . GLN L  1 22  ? 52.933 10.040  -80.166  1.00 33.16 ? 22   GLN M CA  1 
ATOM   12407 C  C   . GLN L  1 22  ? 51.937 11.139  -79.873  1.00 33.16 ? 22   GLN M C   1 
ATOM   12408 O  O   . GLN L  1 22  ? 51.308 11.145  -78.815  1.00 32.84 ? 22   GLN M O   1 
ATOM   12409 C  CB  . GLN L  1 22  ? 52.360 8.679   -79.789  1.00 33.11 ? 22   GLN M CB  1 
ATOM   12410 C  CG  . GLN L  1 22  ? 51.147 8.274   -80.590  1.00 32.48 ? 22   GLN M CG  1 
ATOM   12411 C  CD  . GLN L  1 22  ? 50.585 6.949   -80.147  1.00 32.59 ? 22   GLN M CD  1 
ATOM   12412 O  OE1 . GLN L  1 22  ? 50.829 6.496   -79.029  1.00 32.44 ? 22   GLN M OE1 1 
ATOM   12413 N  NE2 . GLN L  1 22  ? 49.819 6.316   -81.019  1.00 32.76 ? 22   GLN M NE2 1 
ATOM   12414 N  N   . LYS L  1 23  ? 51.810 12.079  -80.803  1.00 32.66 ? 23   LYS M N   1 
ATOM   12415 C  CA  . LYS L  1 23  ? 50.961 13.243  -80.595  1.00 32.78 ? 23   LYS M CA  1 
ATOM   12416 C  C   . LYS L  1 23  ? 49.472 12.883  -80.492  1.00 32.44 ? 23   LYS M C   1 
ATOM   12417 O  O   . LYS L  1 23  ? 48.703 13.614  -79.867  1.00 32.40 ? 23   LYS M O   1 
ATOM   12418 C  CB  . LYS L  1 23  ? 51.191 14.279  -81.700  1.00 33.24 ? 23   LYS M CB  1 
ATOM   12419 C  CG  . LYS L  1 23  ? 52.583 14.897  -81.675  1.00 34.24 ? 23   LYS M CG  1 
ATOM   12420 C  CD  . LYS L  1 23  ? 52.990 15.396  -83.050  1.00 35.93 ? 23   LYS M CD  1 
ATOM   12421 C  CE  . LYS L  1 23  ? 54.495 15.645  -83.124  1.00 36.70 ? 23   LYS M CE  1 
ATOM   12422 N  NZ  . LYS L  1 23  ? 54.886 16.085  -84.499  1.00 38.22 ? 23   LYS M NZ  1 
ATOM   12423 N  N   . GLU L  1 24  ? 49.089 11.757  -81.096  1.00 32.10 ? 24   GLU M N   1 
ATOM   12424 C  CA  . GLU L  1 24  ? 47.693 11.309  -81.149  1.00 32.26 ? 24   GLU M CA  1 
ATOM   12425 C  C   . GLU L  1 24  ? 47.609 9.814   -80.897  1.00 31.66 ? 24   GLU M C   1 
ATOM   12426 O  O   . GLU L  1 24  ? 48.412 9.053   -81.435  1.00 31.47 ? 24   GLU M O   1 
ATOM   12427 C  CB  . GLU L  1 24  ? 47.066 11.626  -82.523  1.00 32.62 ? 24   GLU M CB  1 
ATOM   12428 C  CG  . GLU L  1 24  ? 47.132 13.090  -82.954  1.00 34.36 ? 24   GLU M CG  1 
ATOM   12429 C  CD  . GLU L  1 24  ? 46.302 14.018  -82.078  1.00 37.59 ? 24   GLU M CD  1 
ATOM   12430 O  OE1 . GLU L  1 24  ? 45.463 13.527  -81.290  1.00 39.37 ? 24   GLU M OE1 1 
ATOM   12431 O  OE2 . GLU L  1 24  ? 46.484 15.252  -82.181  1.00 38.93 ? 24   GLU M OE2 1 
ATOM   12432 N  N   . SER L  1 25  ? 46.624 9.397   -80.100  1.00 31.46 ? 25   SER M N   1 
ATOM   12433 C  CA  . SER L  1 25  ? 46.464 7.989   -79.714  1.00 31.19 ? 25   SER M CA  1 
ATOM   12434 C  C   . SER L  1 25  ? 46.169 7.073   -80.899  1.00 31.15 ? 25   SER M C   1 
ATOM   12435 O  O   . SER L  1 25  ? 46.487 5.878   -80.866  1.00 30.96 ? 25   SER M O   1 
ATOM   12436 C  CB  . SER L  1 25  ? 45.378 7.835   -78.643  1.00 31.15 ? 25   SER M CB  1 
ATOM   12437 O  OG  . SER L  1 25  ? 44.111 8.254   -79.124  1.00 30.92 ? 25   SER M OG  1 
ATOM   12438 N  N   . ASN L  1 26  ? 45.554 7.629   -81.941  1.00 30.94 ? 26   ASN M N   1 
ATOM   12439 C  CA  . ASN L  1 26  ? 45.378 6.893   -83.186  1.00 31.03 ? 26   ASN M CA  1 
ATOM   12440 C  C   . ASN L  1 26  ? 46.347 7.339   -84.285  1.00 31.44 ? 26   ASN M C   1 
ATOM   12441 O  O   . ASN L  1 26  ? 46.150 6.999   -85.449  1.00 31.56 ? 26   ASN M O   1 
ATOM   12442 C  CB  . ASN L  1 26  ? 43.918 6.940   -83.672  1.00 30.86 ? 26   ASN M CB  1 
ATOM   12443 C  CG  . ASN L  1 26  ? 43.488 8.322   -84.136  1.00 30.08 ? 26   ASN M CG  1 
ATOM   12444 O  OD1 . ASN L  1 26  ? 43.987 9.343   -83.655  1.00 29.51 ? 26   ASN M OD1 1 
ATOM   12445 N  ND2 . ASN L  1 26  ? 42.547 8.358   -85.079  1.00 30.76 ? 26   ASN M ND2 1 
ATOM   12446 N  N   . GLY L  1 27  ? 47.375 8.101   -83.904  1.00 31.57 ? 27   GLY M N   1 
ATOM   12447 C  CA  . GLY L  1 27  ? 48.392 8.610   -84.836  1.00 32.53 ? 27   GLY M CA  1 
ATOM   12448 C  C   . GLY L  1 27  ? 49.741 7.918   -84.694  1.00 33.15 ? 27   GLY M C   1 
ATOM   12449 O  O   . GLY L  1 27  ? 49.927 7.122   -83.768  1.00 33.19 ? 27   GLY M O   1 
ATOM   12450 N  N   . PRO L  1 28  ? 50.697 8.220   -85.607  1.00 33.60 ? 28   PRO M N   1 
ATOM   12451 C  CA  . PRO L  1 28  ? 52.010 7.551   -85.613  1.00 33.91 ? 28   PRO M CA  1 
ATOM   12452 C  C   . PRO L  1 28  ? 52.895 7.866   -84.393  1.00 34.30 ? 28   PRO M C   1 
ATOM   12453 O  O   . PRO L  1 28  ? 52.729 8.913   -83.757  1.00 34.22 ? 28   PRO M O   1 
ATOM   12454 C  CB  . PRO L  1 28  ? 52.668 8.066   -86.904  1.00 33.66 ? 28   PRO M CB  1 
ATOM   12455 C  CG  . PRO L  1 28  ? 52.008 9.361   -87.191  1.00 33.62 ? 28   PRO M CG  1 
ATOM   12456 C  CD  . PRO L  1 28  ? 50.594 9.244   -86.668  1.00 33.39 ? 28   PRO M CD  1 
ATOM   12457 N  N   . VAL L  1 29  ? 53.826 6.958   -84.099  1.00 34.67 ? 29   VAL M N   1 
ATOM   12458 C  CA  . VAL L  1 29  ? 54.788 7.106   -82.996  1.00 35.55 ? 29   VAL M CA  1 
ATOM   12459 C  C   . VAL L  1 29  ? 56.219 7.453   -83.471  1.00 36.16 ? 29   VAL M C   1 
ATOM   12460 O  O   . VAL L  1 29  ? 56.923 6.603   -84.018  1.00 36.28 ? 29   VAL M O   1 
ATOM   12461 C  CB  . VAL L  1 29  ? 54.843 5.826   -82.109  1.00 35.46 ? 29   VAL M CB  1 
ATOM   12462 C  CG1 . VAL L  1 29  ? 55.847 5.994   -80.961  1.00 35.31 ? 29   VAL M CG1 1 
ATOM   12463 C  CG2 . VAL L  1 29  ? 53.461 5.476   -81.555  1.00 35.17 ? 29   VAL M CG2 1 
ATOM   12464 N  N   . LYS L  1 30  ? 56.642 8.696   -83.234  1.00 36.84 ? 30   LYS M N   1 
ATOM   12465 C  CA  . LYS L  1 30  ? 58.006 9.146   -83.534  1.00 37.33 ? 30   LYS M CA  1 
ATOM   12466 C  C   . LYS L  1 30  ? 58.999 8.449   -82.594  1.00 37.47 ? 30   LYS M C   1 
ATOM   12467 O  O   . LYS L  1 30  ? 58.812 8.458   -81.368  1.00 36.81 ? 30   LYS M O   1 
ATOM   12468 C  CB  . LYS L  1 30  ? 58.080 10.666  -83.353  1.00 37.87 ? 30   LYS M CB  1 
ATOM   12469 C  CG  . LYS L  1 30  ? 58.518 11.469  -84.578  1.00 39.30 ? 30   LYS M CG  1 
ATOM   12470 C  CD  . LYS L  1 30  ? 58.058 12.937  -84.492  1.00 41.72 ? 30   LYS M CD  1 
ATOM   12471 C  CE  . LYS L  1 30  ? 58.945 13.747  -83.531  1.00 44.43 ? 30   LYS M CE  1 
ATOM   12472 N  NZ  . LYS L  1 30  ? 58.185 14.756  -82.719  1.00 45.35 ? 30   LYS M NZ  1 
ATOM   12473 N  N   . VAL L  1 31  ? 60.039 7.835   -83.165  1.00 37.60 ? 31   VAL M N   1 
ATOM   12474 C  CA  . VAL L  1 31  ? 61.066 7.107   -82.389  1.00 37.89 ? 31   VAL M CA  1 
ATOM   12475 C  C   . VAL L  1 31  ? 62.456 7.634   -82.726  1.00 38.38 ? 31   VAL M C   1 
ATOM   12476 O  O   . VAL L  1 31  ? 62.942 7.434   -83.837  1.00 38.52 ? 31   VAL M O   1 
ATOM   12477 C  CB  . VAL L  1 31  ? 61.046 5.569   -82.670  1.00 37.75 ? 31   VAL M CB  1 
ATOM   12478 C  CG1 . VAL L  1 31  ? 62.117 4.852   -81.857  1.00 36.86 ? 31   VAL M CG1 1 
ATOM   12479 C  CG2 . VAL L  1 31  ? 59.680 4.977   -82.384  1.00 37.60 ? 31   VAL M CG2 1 
ATOM   12480 N  N   . TRP L  1 32  ? 63.101 8.302   -81.773  1.00 38.86 ? 32   TRP M N   1 
ATOM   12481 C  CA  . TRP L  1 32  ? 64.437 8.833   -82.026  1.00 39.16 ? 32   TRP M CA  1 
ATOM   12482 C  C   . TRP L  1 32  ? 65.407 8.561   -80.887  1.00 39.23 ? 32   TRP M C   1 
ATOM   12483 O  O   . TRP L  1 32  ? 65.023 8.010   -79.848  1.00 38.97 ? 32   TRP M O   1 
ATOM   12484 C  CB  . TRP L  1 32  ? 64.387 10.327  -82.382  1.00 39.52 ? 32   TRP M CB  1 
ATOM   12485 C  CG  . TRP L  1 32  ? 64.304 11.283  -81.209  1.00 40.72 ? 32   TRP M CG  1 
ATOM   12486 C  CD1 . TRP L  1 32  ? 65.332 12.003  -80.663  1.00 41.10 ? 32   TRP M CD1 1 
ATOM   12487 C  CD2 . TRP L  1 32  ? 63.130 11.635  -80.467  1.00 41.48 ? 32   TRP M CD2 1 
ATOM   12488 N  NE1 . TRP L  1 32  ? 64.872 12.776  -79.624  1.00 41.85 ? 32   TRP M NE1 1 
ATOM   12489 C  CE2 . TRP L  1 32  ? 63.523 12.572  -79.482  1.00 41.96 ? 32   TRP M CE2 1 
ATOM   12490 C  CE3 . TRP L  1 32  ? 61.784 11.248  -80.534  1.00 42.39 ? 32   TRP M CE3 1 
ATOM   12491 C  CZ2 . TRP L  1 32  ? 62.617 13.124  -78.566  1.00 42.24 ? 32   TRP M CZ2 1 
ATOM   12492 C  CZ3 . TRP L  1 32  ? 60.879 11.801  -79.621  1.00 42.52 ? 32   TRP M CZ3 1 
ATOM   12493 C  CH2 . TRP L  1 32  ? 61.303 12.732  -78.655  1.00 42.66 ? 32   TRP M CH2 1 
ATOM   12494 N  N   . GLY L  1 33  ? 66.666 8.939   -81.104  1.00 39.22 ? 33   GLY M N   1 
ATOM   12495 C  CA  . GLY L  1 33  ? 67.729 8.744   -80.118  1.00 39.10 ? 33   GLY M CA  1 
ATOM   12496 C  C   . GLY L  1 33  ? 69.044 8.313   -80.741  1.00 39.35 ? 33   GLY M C   1 
ATOM   12497 O  O   . GLY L  1 33  ? 69.271 8.512   -81.943  1.00 39.09 ? 33   GLY M O   1 
ATOM   12498 N  N   . SER L  1 34  ? 69.899 7.702   -79.922  1.00 39.31 ? 34   SER M N   1 
ATOM   12499 C  CA  . SER L  1 34  ? 71.253 7.330   -80.320  1.00 39.56 ? 34   SER M CA  1 
ATOM   12500 C  C   . SER L  1 34  ? 71.699 6.060   -79.594  1.00 39.48 ? 34   SER M C   1 
ATOM   12501 O  O   . SER L  1 34  ? 71.493 5.935   -78.385  1.00 39.59 ? 34   SER M O   1 
ATOM   12502 C  CB  . SER L  1 34  ? 72.214 8.481   -80.004  1.00 39.41 ? 34   SER M CB  1 
ATOM   12503 O  OG  . SER L  1 34  ? 73.495 8.252   -80.562  1.00 40.62 ? 34   SER M OG  1 
ATOM   12504 N  N   . ILE L  1 35  ? 72.287 5.118   -80.334  1.00 39.21 ? 35   ILE M N   1 
ATOM   12505 C  CA  . ILE L  1 35  ? 72.891 3.904   -79.749  1.00 39.08 ? 35   ILE M CA  1 
ATOM   12506 C  C   . ILE L  1 35  ? 74.367 3.806   -80.155  1.00 39.47 ? 35   ILE M C   1 
ATOM   12507 O  O   . ILE L  1 35  ? 74.677 3.761   -81.353  1.00 39.13 ? 35   ILE M O   1 
ATOM   12508 C  CB  . ILE L  1 35  ? 72.177 2.595   -80.204  1.00 38.69 ? 35   ILE M CB  1 
ATOM   12509 C  CG1 . ILE L  1 35  ? 70.667 2.666   -79.973  1.00 38.66 ? 35   ILE M CG1 1 
ATOM   12510 C  CG2 . ILE L  1 35  ? 72.772 1.366   -79.499  1.00 38.06 ? 35   ILE M CG2 1 
ATOM   12511 C  CD1 . ILE L  1 35  ? 69.901 1.522   -80.630  1.00 38.14 ? 35   ILE M CD1 1 
ATOM   12512 N  N   . LYS L  1 36  ? 75.266 3.763   -79.168  1.00 39.65 ? 36   LYS M N   1 
ATOM   12513 C  CA  . LYS L  1 36  ? 76.712 3.639   -79.439  1.00 40.12 ? 36   LYS M CA  1 
ATOM   12514 C  C   . LYS L  1 36  ? 77.324 2.279   -79.036  1.00 40.08 ? 36   LYS M C   1 
ATOM   12515 O  O   . LYS L  1 36  ? 76.703 1.493   -78.318  1.00 40.01 ? 36   LYS M O   1 
ATOM   12516 C  CB  . LYS L  1 36  ? 77.507 4.837   -78.869  1.00 40.28 ? 36   LYS M CB  1 
ATOM   12517 C  CG  . LYS L  1 36  ? 77.335 5.138   -77.378  1.00 41.01 ? 36   LYS M CG  1 
ATOM   12518 C  CD  . LYS L  1 36  ? 78.431 4.488   -76.541  1.00 43.08 ? 36   LYS M CD  1 
ATOM   12519 C  CE  . LYS L  1 36  ? 78.615 5.210   -75.206  1.00 43.92 ? 36   LYS M CE  1 
ATOM   12520 N  NZ  . LYS L  1 36  ? 79.733 4.625   -74.407  1.00 45.19 ? 36   LYS M NZ  1 
ATOM   12521 N  N   . GLY L  1 37  ? 78.531 2.005   -79.535  1.00 40.11 ? 37   GLY M N   1 
ATOM   12522 C  CA  . GLY L  1 37  ? 79.242 0.760   -79.238  1.00 40.05 ? 37   GLY M CA  1 
ATOM   12523 C  C   . GLY L  1 37  ? 78.765 -0.464  -80.003  1.00 39.99 ? 37   GLY M C   1 
ATOM   12524 O  O   . GLY L  1 37  ? 78.866 -1.586  -79.504  1.00 39.94 ? 37   GLY M O   1 
ATOM   12525 N  N   . LEU L  1 38  ? 78.248 -0.243  -81.213  1.00 40.07 ? 38   LEU M N   1 
ATOM   12526 C  CA  . LEU L  1 38  ? 77.806 -1.322  -82.097  1.00 40.09 ? 38   LEU M CA  1 
ATOM   12527 C  C   . LEU L  1 38  ? 78.847 -1.604  -83.178  1.00 40.44 ? 38   LEU M C   1 
ATOM   12528 O  O   . LEU L  1 38  ? 79.691 -0.757  -83.473  1.00 40.15 ? 38   LEU M O   1 
ATOM   12529 C  CB  . LEU L  1 38  ? 76.482 -0.951  -82.771  1.00 40.06 ? 38   LEU M CB  1 
ATOM   12530 C  CG  . LEU L  1 38  ? 75.174 -0.975  -81.969  1.00 39.65 ? 38   LEU M CG  1 
ATOM   12531 C  CD1 . LEU L  1 38  ? 74.138 -0.076  -82.634  1.00 39.27 ? 38   LEU M CD1 1 
ATOM   12532 C  CD2 . LEU L  1 38  ? 74.641 -2.392  -81.819  1.00 37.86 ? 38   LEU M CD2 1 
ATOM   12533 N  N   . THR L  1 39  ? 78.786 -2.797  -83.763  1.00 40.89 ? 39   THR M N   1 
ATOM   12534 C  CA  . THR L  1 39  ? 79.556 -3.079  -84.972  1.00 41.55 ? 39   THR M CA  1 
ATOM   12535 C  C   . THR L  1 39  ? 78.881 -2.376  -86.158  1.00 42.03 ? 39   THR M C   1 
ATOM   12536 O  O   . THR L  1 39  ? 77.648 -2.424  -86.300  1.00 42.35 ? 39   THR M O   1 
ATOM   12537 C  CB  . THR L  1 39  ? 79.711 -4.601  -85.238  1.00 41.46 ? 39   THR M CB  1 
ATOM   12538 O  OG1 . THR L  1 39  ? 78.422 -5.209  -85.396  1.00 41.20 ? 39   THR M OG1 1 
ATOM   12539 C  CG2 . THR L  1 39  ? 80.458 -5.279  -84.095  1.00 41.56 ? 39   THR M CG2 1 
ATOM   12540 N  N   . GLU L  1 40  ? 79.690 -1.706  -86.982  1.00 42.36 ? 40   GLU M N   1 
ATOM   12541 C  CA  . GLU L  1 40  ? 79.221 -0.980  -88.170  1.00 42.49 ? 40   GLU M CA  1 
ATOM   12542 C  C   . GLU L  1 40  ? 78.154 -1.771  -88.927  1.00 42.59 ? 40   GLU M C   1 
ATOM   12543 O  O   . GLU L  1 40  ? 78.338 -2.955  -89.216  1.00 42.70 ? 40   GLU M O   1 
ATOM   12544 C  CB  . GLU L  1 40  ? 80.411 -0.655  -89.094  1.00 42.60 ? 40   GLU M CB  1 
ATOM   12545 C  CG  . GLU L  1 40  ? 80.087 0.228   -90.313  1.00 42.95 ? 40   GLU M CG  1 
ATOM   12546 C  CD  . GLU L  1 40  ? 81.327 0.642   -91.115  1.00 44.01 ? 40   GLU M CD  1 
ATOM   12547 O  OE1 . GLU L  1 40  ? 81.180 1.444   -92.069  1.00 44.03 ? 40   GLU M OE1 1 
ATOM   12548 O  OE2 . GLU L  1 40  ? 82.448 0.177   -90.797  1.00 43.74 ? 40   GLU M OE2 1 
ATOM   12549 N  N   . GLY L  1 41  ? 77.027 -1.119  -89.213  1.00 42.59 ? 41   GLY M N   1 
ATOM   12550 C  CA  . GLY L  1 41  ? 75.981 -1.734  -90.020  1.00 42.65 ? 41   GLY M CA  1 
ATOM   12551 C  C   . GLY L  1 41  ? 74.644 -2.006  -89.353  1.00 42.59 ? 41   GLY M C   1 
ATOM   12552 O  O   . GLY L  1 41  ? 74.316 -1.424  -88.307  1.00 42.70 ? 41   GLY M O   1 
ATOM   12553 N  N   . LEU L  1 42  ? 73.890 -2.918  -89.971  1.00 42.50 ? 42   LEU M N   1 
ATOM   12554 C  CA  . LEU L  1 42  ? 72.484 -3.190  -89.650  1.00 42.45 ? 42   LEU M CA  1 
ATOM   12555 C  C   . LEU L  1 42  ? 72.287 -4.111  -88.446  1.00 42.29 ? 42   LEU M C   1 
ATOM   12556 O  O   . LEU L  1 42  ? 72.949 -5.156  -88.329  1.00 42.31 ? 42   LEU M O   1 
ATOM   12557 C  CB  . LEU L  1 42  ? 71.769 -3.782  -90.876  1.00 42.59 ? 42   LEU M CB  1 
ATOM   12558 C  CG  . LEU L  1 42  ? 71.325 -2.871  -92.035  1.00 42.92 ? 42   LEU M CG  1 
ATOM   12559 C  CD1 . LEU L  1 42  ? 72.479 -2.102  -92.691  1.00 43.02 ? 42   LEU M CD1 1 
ATOM   12560 C  CD2 . LEU L  1 42  ? 70.583 -3.688  -93.083  1.00 43.16 ? 42   LEU M CD2 1 
ATOM   12561 N  N   . HIS L  1 43  ? 71.364 -3.718  -87.564  1.00 41.76 ? 43   HIS M N   1 
ATOM   12562 C  CA  . HIS L  1 43  ? 71.041 -4.486  -86.361  1.00 41.33 ? 43   HIS M CA  1 
ATOM   12563 C  C   . HIS L  1 43  ? 69.543 -4.461  -86.073  1.00 41.06 ? 43   HIS M C   1 
ATOM   12564 O  O   . HIS L  1 43  ? 68.893 -3.423  -86.206  1.00 40.78 ? 43   HIS M O   1 
ATOM   12565 C  CB  . HIS L  1 43  ? 71.799 -3.948  -85.137  1.00 41.34 ? 43   HIS M CB  1 
ATOM   12566 C  CG  . HIS L  1 43  ? 73.262 -4.287  -85.117  1.00 41.28 ? 43   HIS M CG  1 
ATOM   12567 N  ND1 . HIS L  1 43  ? 73.734 -5.566  -84.903  1.00 40.88 ? 43   HIS M ND1 1 
ATOM   12568 C  CD2 . HIS L  1 43  ? 74.358 -3.502  -85.253  1.00 40.92 ? 43   HIS M CD2 1 
ATOM   12569 C  CE1 . HIS L  1 43  ? 75.054 -5.556  -84.924  1.00 40.41 ? 43   HIS M CE1 1 
ATOM   12570 N  NE2 . HIS L  1 43  ? 75.458 -4.316  -85.133  1.00 40.43 ? 43   HIS M NE2 1 
ATOM   12571 N  N   . GLY L  1 44  ? 69.009 -5.613  -85.677  1.00 40.69 ? 44   GLY M N   1 
ATOM   12572 C  CA  . GLY L  1 44  ? 67.612 -5.743  -85.279  1.00 40.77 ? 44   GLY M CA  1 
ATOM   12573 C  C   . GLY L  1 44  ? 67.196 -4.730  -84.227  1.00 40.63 ? 44   GLY M C   1 
ATOM   12574 O  O   . GLY L  1 44  ? 68.033 -4.201  -83.493  1.00 40.41 ? 44   GLY M O   1 
ATOM   12575 N  N   . PHE L  1 45  ? 65.892 -4.467  -84.168  1.00 40.73 ? 45   PHE M N   1 
ATOM   12576 C  CA  . PHE L  1 45  ? 65.312 -3.450  -83.301  1.00 40.82 ? 45   PHE M CA  1 
ATOM   12577 C  C   . PHE L  1 45  ? 63.850 -3.855  -83.120  1.00 40.81 ? 45   PHE M C   1 
ATOM   12578 O  O   . PHE L  1 45  ? 63.035 -3.679  -84.032  1.00 40.52 ? 45   PHE M O   1 
ATOM   12579 C  CB  . PHE L  1 45  ? 65.432 -2.075  -83.980  1.00 41.15 ? 45   PHE M CB  1 
ATOM   12580 C  CG  . PHE L  1 45  ? 65.281 -0.894  -83.048  1.00 41.64 ? 45   PHE M CG  1 
ATOM   12581 C  CD1 . PHE L  1 45  ? 66.162 -0.698  -81.984  1.00 42.08 ? 45   PHE M CD1 1 
ATOM   12582 C  CD2 . PHE L  1 45  ? 64.281 0.051   -83.266  1.00 41.91 ? 45   PHE M CD2 1 
ATOM   12583 C  CE1 . PHE L  1 45  ? 66.028 0.403   -81.135  1.00 42.23 ? 45   PHE M CE1 1 
ATOM   12584 C  CE2 . PHE L  1 45  ? 64.142 1.157   -82.425  1.00 42.32 ? 45   PHE M CE2 1 
ATOM   12585 C  CZ  . PHE L  1 45  ? 65.019 1.332   -81.356  1.00 41.98 ? 45   PHE M CZ  1 
ATOM   12586 N  N   . HIS L  1 46  ? 63.535 -4.436  -81.959  1.00 40.57 ? 46   HIS M N   1 
ATOM   12587 C  CA  . HIS L  1 46  ? 62.199 -4.982  -81.696  1.00 40.43 ? 46   HIS M CA  1 
ATOM   12588 C  C   . HIS L  1 46  ? 61.643 -4.612  -80.319  1.00 40.09 ? 46   HIS M C   1 
ATOM   12589 O  O   . HIS L  1 46  ? 62.398 -4.275  -79.396  1.00 39.82 ? 46   HIS M O   1 
ATOM   12590 C  CB  . HIS L  1 46  ? 62.200 -6.509  -81.796  1.00 40.50 ? 46   HIS M CB  1 
ATOM   12591 C  CG  . HIS L  1 46  ? 62.966 -7.047  -82.962  1.00 41.70 ? 46   HIS M CG  1 
ATOM   12592 N  ND1 . HIS L  1 46  ? 64.086 -7.837  -82.811  1.00 42.82 ? 46   HIS M ND1 1 
ATOM   12593 C  CD2 . HIS L  1 46  ? 62.771 -6.918  -84.296  1.00 42.36 ? 46   HIS M CD2 1 
ATOM   12594 C  CE1 . HIS L  1 46  ? 64.551 -8.168  -84.003  1.00 42.54 ? 46   HIS M CE1 1 
ATOM   12595 N  NE2 . HIS L  1 46  ? 63.770 -7.626  -84.921  1.00 42.63 ? 46   HIS M NE2 1 
ATOM   12596 N  N   . VAL L  1 47  ? 60.318 -4.695  -80.205  1.00 39.63 ? 47   VAL M N   1 
ATOM   12597 C  CA  . VAL L  1 47  ? 59.628 -4.721  -78.914  1.00 39.22 ? 47   VAL M CA  1 
ATOM   12598 C  C   . VAL L  1 47  ? 59.296 -6.180  -78.603  1.00 39.20 ? 47   VAL M C   1 
ATOM   12599 O  O   . VAL L  1 47  ? 58.552 -6.832  -79.345  1.00 38.96 ? 47   VAL M O   1 
ATOM   12600 C  CB  . VAL L  1 47  ? 58.326 -3.873  -78.913  1.00 39.03 ? 47   VAL M CB  1 
ATOM   12601 C  CG1 . VAL L  1 47  ? 57.543 -4.078  -77.606  1.00 39.20 ? 47   VAL M CG1 1 
ATOM   12602 C  CG2 . VAL L  1 47  ? 58.639 -2.398  -79.130  1.00 38.50 ? 47   VAL M CG2 1 
ATOM   12603 N  N   . HIS L  1 48  ? 59.880 -6.684  -77.519  1.00 39.21 ? 48   HIS M N   1 
ATOM   12604 C  CA  . HIS L  1 48  ? 59.599 -8.026  -77.018  1.00 39.68 ? 48   HIS M CA  1 
ATOM   12605 C  C   . HIS L  1 48  ? 58.464 -7.970  -76.000  1.00 39.73 ? 48   HIS M C   1 
ATOM   12606 O  O   . HIS L  1 48  ? 58.087 -6.884  -75.548  1.00 40.15 ? 48   HIS M O   1 
ATOM   12607 C  CB  . HIS L  1 48  ? 60.862 -8.658  -76.424  1.00 39.97 ? 48   HIS M CB  1 
ATOM   12608 C  CG  . HIS L  1 48  ? 61.806 -9.198  -77.456  1.00 40.67 ? 48   HIS M CG  1 
ATOM   12609 N  ND1 . HIS L  1 48  ? 62.093 -10.542 -77.570  1.00 41.58 ? 48   HIS M ND1 1 
ATOM   12610 C  CD2 . HIS L  1 48  ? 62.512 -8.578  -78.431  1.00 41.46 ? 48   HIS M CD2 1 
ATOM   12611 C  CE1 . HIS L  1 48  ? 62.942 -10.725 -78.568  1.00 42.66 ? 48   HIS M CE1 1 
ATOM   12612 N  NE2 . HIS L  1 48  ? 63.213 -9.550  -79.107  1.00 43.78 ? 48   HIS M NE2 1 
ATOM   12613 N  N   . GLU L  1 49  ? 57.931 -9.135  -75.641  1.00 39.35 ? 49   GLU M N   1 
ATOM   12614 C  CA  . GLU L  1 49  ? 56.663 -9.223  -74.927  1.00 39.25 ? 49   GLU M CA  1 
ATOM   12615 C  C   . GLU L  1 49  ? 56.738 -8.709  -73.480  1.00 39.33 ? 49   GLU M C   1 
ATOM   12616 O  O   . GLU L  1 49  ? 56.055 -7.739  -73.125  1.00 39.26 ? 49   GLU M O   1 
ATOM   12617 C  CB  . GLU L  1 49  ? 56.135 -10.664 -74.973  1.00 39.16 ? 49   GLU M CB  1 
ATOM   12618 C  CG  . GLU L  1 49  ? 54.654 -10.828 -74.628  1.00 39.25 ? 49   GLU M CG  1 
ATOM   12619 C  CD  . GLU L  1 49  ? 54.211 -12.283 -74.596  1.00 39.95 ? 49   GLU M CD  1 
ATOM   12620 O  OE1 . GLU L  1 49  ? 53.168 -12.577 -73.966  1.00 40.05 ? 49   GLU M OE1 1 
ATOM   12621 O  OE2 . GLU L  1 49  ? 54.901 -13.138 -75.195  1.00 39.98 ? 49   GLU M OE2 1 
ATOM   12622 N  N   . PHE L  1 50  ? 57.567 -9.357  -72.662  1.00 39.06 ? 50   PHE M N   1 
ATOM   12623 C  CA  . PHE L  1 50  ? 57.622 -9.074  -71.229  1.00 39.02 ? 50   PHE M CA  1 
ATOM   12624 C  C   . PHE L  1 50  ? 58.685 -8.038  -70.868  1.00 38.55 ? 50   PHE M C   1 
ATOM   12625 O  O   . PHE L  1 50  ? 59.791 -8.068  -71.407  1.00 38.49 ? 50   PHE M O   1 
ATOM   12626 C  CB  . PHE L  1 50  ? 57.853 -10.365 -70.435  1.00 39.07 ? 50   PHE M CB  1 
ATOM   12627 C  CG  . PHE L  1 50  ? 56.963 -11.509 -70.851  1.00 40.04 ? 50   PHE M CG  1 
ATOM   12628 C  CD1 . PHE L  1 50  ? 55.573 -11.391 -70.797  1.00 41.12 ? 50   PHE M CD1 1 
ATOM   12629 C  CD2 . PHE L  1 50  ? 57.518 -12.713 -71.284  1.00 40.68 ? 50   PHE M CD2 1 
ATOM   12630 C  CE1 . PHE L  1 50  ? 54.746 -12.451 -71.182  1.00 41.71 ? 50   PHE M CE1 1 
ATOM   12631 C  CE2 . PHE L  1 50  ? 56.703 -13.779 -71.668  1.00 41.56 ? 50   PHE M CE2 1 
ATOM   12632 C  CZ  . PHE L  1 50  ? 55.313 -13.649 -71.615  1.00 41.31 ? 50   PHE M CZ  1 
ATOM   12633 N  N   . GLY L  1 51  ? 58.338 -7.130  -69.955  1.00 38.01 ? 51   GLY M N   1 
ATOM   12634 C  CA  . GLY L  1 51  ? 59.270 -6.135  -69.420  1.00 37.31 ? 51   GLY M CA  1 
ATOM   12635 C  C   . GLY L  1 51  ? 60.050 -6.713  -68.254  1.00 37.13 ? 51   GLY M C   1 
ATOM   12636 O  O   . GLY L  1 51  ? 60.245 -6.058  -67.226  1.00 37.09 ? 51   GLY M O   1 
ATOM   12637 N  N   . ASP L  1 52  ? 60.492 -7.953  -68.431  1.00 36.84 ? 52   ASP M N   1 
ATOM   12638 C  CA  . ASP L  1 52  ? 61.203 -8.710  -67.428  1.00 36.60 ? 52   ASP M CA  1 
ATOM   12639 C  C   . ASP L  1 52  ? 62.698 -8.778  -67.764  1.00 37.32 ? 52   ASP M C   1 
ATOM   12640 O  O   . ASP L  1 52  ? 63.096 -9.218  -68.853  1.00 37.36 ? 52   ASP M O   1 
ATOM   12641 C  CB  . ASP L  1 52  ? 60.589 -10.105 -67.323  1.00 36.40 ? 52   ASP M CB  1 
ATOM   12642 C  CG  . ASP L  1 52  ? 61.139 -10.912 -66.166  1.00 35.88 ? 52   ASP M CG  1 
ATOM   12643 O  OD1 . ASP L  1 52  ? 60.431 -11.831 -65.703  1.00 34.70 ? 52   ASP M OD1 1 
ATOM   12644 O  OD2 . ASP L  1 52  ? 62.281 -10.648 -65.726  1.00 36.27 ? 52   ASP M OD2 1 
ATOM   12645 N  N   . ASN L  1 53  ? 63.518 -8.328  -66.822  1.00 37.52 ? 53   ASN M N   1 
ATOM   12646 C  CA  . ASN L  1 53  ? 64.968 -8.316  -66.999  1.00 38.21 ? 53   ASN M CA  1 
ATOM   12647 C  C   . ASN L  1 53  ? 65.702 -9.100  -65.902  1.00 37.93 ? 53   ASN M C   1 
ATOM   12648 O  O   . ASN L  1 53  ? 66.893 -8.889  -65.677  1.00 38.22 ? 53   ASN M O   1 
ATOM   12649 C  CB  . ASN L  1 53  ? 65.470 -6.866  -67.084  1.00 38.31 ? 53   ASN M CB  1 
ATOM   12650 C  CG  . ASN L  1 53  ? 66.876 -6.753  -67.661  1.00 40.13 ? 53   ASN M CG  1 
ATOM   12651 O  OD1 . ASN L  1 53  ? 67.832 -6.449  -66.940  1.00 41.96 ? 53   ASN M OD1 1 
ATOM   12652 N  ND2 . ASN L  1 53  ? 67.011 -6.993  -68.966  1.00 40.10 ? 53   ASN M ND2 1 
ATOM   12653 N  N   . THR L  1 54  ? 65.001 -10.024 -65.245  1.00 37.84 ? 54   THR M N   1 
ATOM   12654 C  CA  . THR L  1 54  ? 65.586 -10.818 -64.154  1.00 37.87 ? 54   THR M CA  1 
ATOM   12655 C  C   . THR L  1 54  ? 66.605 -11.870 -64.620  1.00 38.18 ? 54   THR M C   1 
ATOM   12656 O  O   . THR L  1 54  ? 67.434 -12.324 -63.831  1.00 38.28 ? 54   THR M O   1 
ATOM   12657 C  CB  . THR L  1 54  ? 64.516 -11.522 -63.285  1.00 37.61 ? 54   THR M CB  1 
ATOM   12658 O  OG1 . THR L  1 54  ? 63.828 -12.503 -64.064  1.00 37.76 ? 54   THR M OG1 1 
ATOM   12659 C  CG2 . THR L  1 54  ? 63.516 -10.521 -62.726  1.00 37.51 ? 54   THR M CG2 1 
ATOM   12660 N  N   . ALA L  1 55  ? 66.521 -12.276 -65.885  1.00 38.33 ? 55   ALA M N   1 
ATOM   12661 C  CA  . ALA L  1 55  ? 67.537 -13.136 -66.476  1.00 38.53 ? 55   ALA M CA  1 
ATOM   12662 C  C   . ALA L  1 55  ? 68.133 -12.447 -67.702  1.00 38.73 ? 55   ALA M C   1 
ATOM   12663 O  O   . ALA L  1 55  ? 68.279 -13.050 -68.770  1.00 38.97 ? 55   ALA M O   1 
ATOM   12664 C  CB  . ALA L  1 55  ? 66.949 -14.505 -66.826  1.00 38.57 ? 55   ALA M CB  1 
ATOM   12665 N  N   . GLY L  1 56  ? 68.477 -11.171 -67.535  1.00 38.68 ? 56   GLY M N   1 
ATOM   12666 C  CA  . GLY L  1 56  ? 68.996 -10.350 -68.625  1.00 38.93 ? 56   GLY M CA  1 
ATOM   12667 C  C   . GLY L  1 56  ? 67.967 -10.119 -69.722  1.00 39.31 ? 56   GLY M C   1 
ATOM   12668 O  O   . GLY L  1 56  ? 66.784 -9.896  -69.446  1.00 39.27 ? 56   GLY M O   1 
ATOM   12669 N  N   . CYS L  1 57  ? 68.414 -10.181 -70.972  1.00 39.22 ? 57   CYS M N   1 
ATOM   12670 C  CA  . CYS L  1 57  ? 67.512 -9.996  -72.089  1.00 39.23 ? 57   CYS M CA  1 
ATOM   12671 C  C   . CYS L  1 57  ? 66.648 -11.227 -72.356  1.00 39.81 ? 57   CYS M C   1 
ATOM   12672 O  O   . CYS L  1 57  ? 65.615 -11.123 -73.018  1.00 39.99 ? 57   CYS M O   1 
ATOM   12673 C  CB  . CYS L  1 57  ? 68.276 -9.545  -73.329  0.40 38.82 ? 57   CYS M CB  1 
ATOM   12674 S  SG  . CYS L  1 57  ? 68.973 -7.891  -73.155  0.40 36.64 ? 57   CYS M SG  1 
ATOM   12675 N  N   . THR L  1 58  ? 67.050 -12.370 -71.797  1.00 40.36 ? 58   THR M N   1 
ATOM   12676 C  CA  . THR L  1 58  ? 66.374 -13.661 -72.015  1.00 40.67 ? 58   THR M CA  1 
ATOM   12677 C  C   . THR L  1 58  ? 64.946 -13.717 -71.464  1.00 40.85 ? 58   THR M C   1 
ATOM   12678 O  O   . THR L  1 58  ? 64.020 -14.075 -72.197  1.00 40.96 ? 58   THR M O   1 
ATOM   12679 C  CB  . THR L  1 58  ? 67.208 -14.855 -71.451  1.00 40.75 ? 58   THR M CB  1 
ATOM   12680 O  OG1 . THR L  1 58  ? 68.538 -14.801 -71.976  1.00 40.90 ? 58   THR M OG1 1 
ATOM   12681 C  CG2 . THR L  1 58  ? 66.592 -16.202 -71.832  1.00 40.91 ? 58   THR M CG2 1 
ATOM   12682 N  N   . SER L  1 59  ? 64.776 -13.362 -70.186  1.00 40.90 ? 59   SER M N   1 
ATOM   12683 C  CA  . SER L  1 59  ? 63.480 -13.494 -69.484  1.00 40.90 ? 59   SER M CA  1 
ATOM   12684 C  C   . SER L  1 59  ? 62.355 -12.630 -70.068  1.00 40.69 ? 59   SER M C   1 
ATOM   12685 O  O   . SER L  1 59  ? 61.195 -12.739 -69.638  1.00 40.43 ? 59   SER M O   1 
ATOM   12686 C  CB  . SER L  1 59  ? 63.642 -13.234 -67.978  1.00 40.87 ? 59   SER M CB  1 
ATOM   12687 O  OG  . SER L  1 59  ? 64.429 -12.075 -67.748  1.00 41.64 ? 59   SER M OG  1 
ATOM   12688 N  N   . ALA L  1 60  ? 62.714 -11.793 -71.048  1.00 40.31 ? 60   ALA M N   1 
ATOM   12689 C  CA  . ALA L  1 60  ? 61.777 -10.958 -71.808  1.00 40.55 ? 60   ALA M CA  1 
ATOM   12690 C  C   . ALA L  1 60  ? 60.901 -11.764 -72.778  1.00 40.69 ? 60   ALA M C   1 
ATOM   12691 O  O   . ALA L  1 60  ? 59.983 -11.212 -73.406  1.00 40.57 ? 60   ALA M O   1 
ATOM   12692 C  CB  . ALA L  1 60  ? 62.540 -9.878  -72.570  1.00 40.15 ? 60   ALA M CB  1 
ATOM   12693 N  N   . GLY L  1 61  ? 61.204 -13.057 -72.904  1.00 40.92 ? 61   GLY M N   1 
ATOM   12694 C  CA  . GLY L  1 61  ? 60.454 -13.973 -73.768  1.00 41.21 ? 61   GLY M CA  1 
ATOM   12695 C  C   . GLY L  1 61  ? 60.438 -13.633 -75.254  1.00 41.27 ? 61   GLY M C   1 
ATOM   12696 O  O   . GLY L  1 61  ? 61.288 -12.870 -75.736  1.00 41.32 ? 61   GLY M O   1 
ATOM   12697 N  N   . PRO L  1 62  ? 59.456 -14.196 -75.991  1.00 41.36 ? 62   PRO M N   1 
ATOM   12698 C  CA  . PRO L  1 62  ? 59.289 -14.028 -77.449  1.00 41.51 ? 62   PRO M CA  1 
ATOM   12699 C  C   . PRO L  1 62  ? 58.992 -12.590 -77.898  1.00 41.62 ? 62   PRO M C   1 
ATOM   12700 O  O   . PRO L  1 62  ? 58.816 -11.705 -77.059  1.00 41.57 ? 62   PRO M O   1 
ATOM   12701 C  CB  . PRO L  1 62  ? 58.101 -14.947 -77.784  1.00 41.44 ? 62   PRO M CB  1 
ATOM   12702 C  CG  . PRO L  1 62  ? 57.416 -15.214 -76.479  1.00 41.53 ? 62   PRO M CG  1 
ATOM   12703 C  CD  . PRO L  1 62  ? 58.468 -15.134 -75.421  1.00 41.17 ? 62   PRO M CD  1 
ATOM   12704 N  N   . HIS L  1 63  ? 58.958 -12.377 -79.217  1.00 41.53 ? 63   HIS M N   1 
ATOM   12705 C  CA  . HIS L  1 63  ? 58.557 -11.105 -79.826  1.00 41.43 ? 63   HIS M CA  1 
ATOM   12706 C  C   . HIS L  1 63  ? 57.124 -10.742 -79.419  1.00 41.05 ? 63   HIS M C   1 
ATOM   12707 O  O   . HIS L  1 63  ? 56.319 -11.633 -79.140  1.00 40.94 ? 63   HIS M O   1 
ATOM   12708 C  CB  . HIS L  1 63  ? 58.650 -11.214 -81.355  1.00 41.83 ? 63   HIS M CB  1 
ATOM   12709 C  CG  . HIS L  1 63  ? 60.025 -10.972 -81.905  1.00 43.09 ? 63   HIS M CG  1 
ATOM   12710 N  ND1 . HIS L  1 63  ? 60.241 -10.300 -83.092  1.00 45.06 ? 63   HIS M ND1 1 
ATOM   12711 C  CD2 . HIS L  1 63  ? 61.252 -11.301 -81.429  1.00 44.13 ? 63   HIS M CD2 1 
ATOM   12712 C  CE1 . HIS L  1 63  ? 61.543 -10.229 -83.322  1.00 45.23 ? 63   HIS M CE1 1 
ATOM   12713 N  NE2 . HIS L  1 63  ? 62.178 -10.826 -82.328  1.00 44.24 ? 63   HIS M NE2 1 
ATOM   12714 N  N   . PHE L  1 64  ? 56.800 -9.449  -79.372  1.00 40.62 ? 64   PHE M N   1 
ATOM   12715 C  CA  . PHE L  1 64  ? 55.450 -9.054  -78.945  1.00 40.11 ? 64   PHE M CA  1 
ATOM   12716 C  C   . PHE L  1 64  ? 54.451 -9.130  -80.085  1.00 40.20 ? 64   PHE M C   1 
ATOM   12717 O  O   . PHE L  1 64  ? 54.597 -8.468  -81.120  1.00 39.91 ? 64   PHE M O   1 
ATOM   12718 C  CB  . PHE L  1 64  ? 55.406 -7.686  -78.248  1.00 39.69 ? 64   PHE M CB  1 
ATOM   12719 C  CG  . PHE L  1 64  ? 54.030 -7.314  -77.721  1.00 37.75 ? 64   PHE M CG  1 
ATOM   12720 C  CD1 . PHE L  1 64  ? 53.441 -6.102  -78.071  1.00 35.57 ? 64   PHE M CD1 1 
ATOM   12721 C  CD2 . PHE L  1 64  ? 53.322 -8.188  -76.894  1.00 36.21 ? 64   PHE M CD2 1 
ATOM   12722 C  CE1 . PHE L  1 64  ? 52.176 -5.757  -77.598  1.00 35.02 ? 64   PHE M CE1 1 
ATOM   12723 C  CE2 . PHE L  1 64  ? 52.057 -7.856  -76.418  1.00 35.60 ? 64   PHE M CE2 1 
ATOM   12724 C  CZ  . PHE L  1 64  ? 51.482 -6.638  -76.772  1.00 35.07 ? 64   PHE M CZ  1 
ATOM   12725 N  N   . ASN L  1 65  ? 53.427 -9.947  -79.855  1.00 40.76 ? 65   ASN M N   1 
ATOM   12726 C  CA  . ASN L  1 65  ? 52.490 -10.356 -80.891  1.00 41.15 ? 65   ASN M CA  1 
ATOM   12727 C  C   . ASN L  1 65  ? 51.173 -10.891 -80.296  1.00 41.19 ? 65   ASN M C   1 
ATOM   12728 O  O   . ASN L  1 65  ? 50.969 -12.105 -80.221  1.00 41.06 ? 65   ASN M O   1 
ATOM   12729 C  CB  . ASN L  1 65  ? 53.171 -11.420 -81.756  1.00 41.46 ? 65   ASN M CB  1 
ATOM   12730 C  CG  . ASN L  1 65  ? 52.278 -11.945 -82.850  1.00 42.09 ? 65   ASN M CG  1 
ATOM   12731 O  OD1 . ASN L  1 65  ? 51.818 -11.195 -83.712  1.00 43.51 ? 65   ASN M OD1 1 
ATOM   12732 N  ND2 . ASN L  1 65  ? 52.036 -13.250 -82.826  1.00 42.14 ? 65   ASN M ND2 1 
ATOM   12733 N  N   . PRO L  1 66  ? 50.272 -9.979  -79.869  1.00 41.27 ? 66   PRO M N   1 
ATOM   12734 C  CA  . PRO L  1 66  ? 49.020 -10.390 -79.229  1.00 41.51 ? 66   PRO M CA  1 
ATOM   12735 C  C   . PRO L  1 66  ? 47.972 -10.879 -80.231  1.00 41.89 ? 66   PRO M C   1 
ATOM   12736 O  O   . PRO L  1 66  ? 46.990 -11.503 -79.831  1.00 41.62 ? 66   PRO M O   1 
ATOM   12737 C  CB  . PRO L  1 66  ? 48.541 -9.105  -78.555  1.00 41.42 ? 66   PRO M CB  1 
ATOM   12738 C  CG  . PRO L  1 66  ? 49.066 -8.014  -79.422  1.00 40.78 ? 66   PRO M CG  1 
ATOM   12739 C  CD  . PRO L  1 66  ? 50.355 -8.514  -80.018  1.00 41.26 ? 66   PRO M CD  1 
ATOM   12740 N  N   . LEU L  1 67  ? 48.201 -10.601 -81.514  1.00 42.50 ? 67   LEU M N   1 
ATOM   12741 C  CA  . LEU L  1 67  ? 47.262 -10.933 -82.589  1.00 43.20 ? 67   LEU M CA  1 
ATOM   12742 C  C   . LEU L  1 67  ? 47.505 -12.312 -83.234  1.00 43.81 ? 67   LEU M C   1 
ATOM   12743 O  O   . LEU L  1 67  ? 46.762 -12.708 -84.138  1.00 43.77 ? 67   LEU M O   1 
ATOM   12744 C  CB  . LEU L  1 67  ? 47.279 -9.831  -83.664  1.00 43.11 ? 67   LEU M CB  1 
ATOM   12745 C  CG  . LEU L  1 67  ? 47.047 -8.366  -83.258  1.00 43.17 ? 67   LEU M CG  1 
ATOM   12746 C  CD1 . LEU L  1 67  ? 47.260 -7.417  -84.441  1.00 42.36 ? 67   LEU M CD1 1 
ATOM   12747 C  CD2 . LEU L  1 67  ? 45.666 -8.150  -82.634  1.00 42.85 ? 67   LEU M CD2 1 
ATOM   12748 N  N   . SER L  1 68  ? 48.535 -13.027 -82.770  1.00 44.50 ? 68   SER M N   1 
ATOM   12749 C  CA  . SER L  1 68  ? 48.894 -14.372 -83.266  1.00 45.31 ? 68   SER M CA  1 
ATOM   12750 C  C   . SER L  1 68  ? 49.224 -14.443 -84.773  1.00 45.89 ? 68   SER M C   1 
ATOM   12751 O  O   . SER L  1 68  ? 48.633 -15.246 -85.507  1.00 46.07 ? 68   SER M O   1 
ATOM   12752 C  CB  . SER L  1 68  ? 47.810 -15.401 -82.905  1.00 45.31 ? 68   SER M CB  1 
ATOM   12753 O  OG  . SER L  1 68  ? 47.748 -15.620 -81.510  1.00 45.18 ? 68   SER M OG  1 
ATOM   12754 N  N   . ARG L  1 69  ? 50.179 -13.621 -85.215  1.00 46.49 ? 69   ARG M N   1 
ATOM   12755 C  CA  . ARG L  1 69  ? 50.571 -13.542 -86.635  1.00 47.01 ? 69   ARG M CA  1 
ATOM   12756 C  C   . ARG L  1 69  ? 52.026 -14.028 -86.859  1.00 47.23 ? 69   ARG M C   1 
ATOM   12757 O  O   . ARG L  1 69  ? 52.599 -14.713 -85.992  1.00 47.30 ? 69   ARG M O   1 
ATOM   12758 C  CB  . ARG L  1 69  ? 50.399 -12.103 -87.153  1.00 47.12 ? 69   ARG M CB  1 
ATOM   12759 C  CG  . ARG L  1 69  ? 49.075 -11.423 -86.781  1.00 48.09 ? 69   ARG M CG  1 
ATOM   12760 C  CD  . ARG L  1 69  ? 48.016 -11.581 -87.866  1.00 49.77 ? 69   ARG M CD  1 
ATOM   12761 N  NE  . ARG L  1 69  ? 46.737 -10.956 -87.504  1.00 50.96 ? 69   ARG M NE  1 
ATOM   12762 C  CZ  . ARG L  1 69  ? 46.421 -9.679  -87.727  1.00 51.14 ? 69   ARG M CZ  1 
ATOM   12763 N  NH1 . ARG L  1 69  ? 45.230 -9.219  -87.366  1.00 51.18 ? 69   ARG M NH1 1 
ATOM   12764 N  NH2 . ARG L  1 69  ? 47.287 -8.857  -88.309  1.00 51.65 ? 69   ARG M NH2 1 
ATOM   12765 N  N   . LYS L  1 70  ? 52.609 -13.664 -88.015  1.00 47.24 ? 70   LYS M N   1 
ATOM   12766 C  CA  . LYS L  1 70  ? 53.998 -14.030 -88.379  1.00 47.14 ? 70   LYS M CA  1 
ATOM   12767 C  C   . LYS L  1 70  ? 54.970 -12.838 -88.356  1.00 46.88 ? 70   LYS M C   1 
ATOM   12768 O  O   . LYS L  1 70  ? 54.551 -11.679 -88.428  1.00 46.83 ? 70   LYS M O   1 
ATOM   12769 C  CB  . LYS L  1 70  ? 54.054 -14.685 -89.778  1.00 47.24 ? 70   LYS M CB  1 
ATOM   12770 C  CG  . LYS L  1 70  ? 53.061 -15.825 -90.036  1.00 47.77 ? 70   LYS M CG  1 
ATOM   12771 C  CD  . LYS L  1 70  ? 53.365 -17.076 -89.218  1.00 48.05 ? 70   LYS M CD  1 
ATOM   12772 C  CE  . LYS L  1 70  ? 52.234 -18.087 -89.342  1.00 48.57 ? 70   LYS M CE  1 
ATOM   12773 N  NZ  . LYS L  1 70  ? 52.230 -19.055 -88.208  1.00 48.77 ? 70   LYS M NZ  1 
ATOM   12774 N  N   . HIS L  1 71  ? 56.267 -13.142 -88.291  1.00 46.71 ? 71   HIS M N   1 
ATOM   12775 C  CA  . HIS L  1 71  ? 57.334 -12.133 -88.287  1.00 46.62 ? 71   HIS M CA  1 
ATOM   12776 C  C   . HIS L  1 71  ? 57.420 -11.352 -89.605  1.00 46.64 ? 71   HIS M C   1 
ATOM   12777 O  O   . HIS L  1 71  ? 57.078 -11.873 -90.660  1.00 46.60 ? 71   HIS M O   1 
ATOM   12778 C  CB  . HIS L  1 71  ? 58.673 -12.807 -87.975  1.00 46.70 ? 71   HIS M CB  1 
ATOM   12779 C  CG  . HIS L  1 71  ? 59.785 -11.851 -87.678  1.00 46.74 ? 71   HIS M CG  1 
ATOM   12780 N  ND1 . HIS L  1 71  ? 60.111 -11.464 -86.395  1.00 46.35 ? 71   HIS M ND1 1 
ATOM   12781 C  CD2 . HIS L  1 71  ? 60.648 -11.207 -88.498  1.00 46.88 ? 71   HIS M CD2 1 
ATOM   12782 C  CE1 . HIS L  1 71  ? 61.127 -10.619 -86.440  1.00 47.15 ? 71   HIS M CE1 1 
ATOM   12783 N  NE2 . HIS L  1 71  ? 61.468 -10.444 -87.705  1.00 47.98 ? 71   HIS M NE2 1 
ATOM   12784 N  N   . GLY L  1 72  ? 57.878 -10.103 -89.536  1.00 46.78 ? 72   GLY M N   1 
ATOM   12785 C  CA  . GLY L  1 72  ? 58.021 -9.255  -90.722  1.00 46.86 ? 72   GLY M CA  1 
ATOM   12786 C  C   . GLY L  1 72  ? 58.780 -7.964  -90.466  1.00 47.15 ? 72   GLY M C   1 
ATOM   12787 O  O   . GLY L  1 72  ? 59.347 -7.767  -89.390  1.00 47.18 ? 72   GLY M O   1 
ATOM   12788 N  N   . GLY L  1 73  ? 58.797 -7.086  -91.464  1.00 47.30 ? 73   GLY M N   1 
ATOM   12789 C  CA  . GLY L  1 73  ? 59.442 -5.777  -91.342  1.00 47.66 ? 73   GLY M CA  1 
ATOM   12790 C  C   . GLY L  1 73  ? 58.454 -4.656  -91.045  1.00 47.88 ? 73   GLY M C   1 
ATOM   12791 O  O   . GLY L  1 73  ? 57.238 -4.876  -91.099  1.00 47.80 ? 73   GLY M O   1 
ATOM   12792 N  N   . PRO L  1 74  ? 58.970 -3.442  -90.743  1.00 48.06 ? 74   PRO M N   1 
ATOM   12793 C  CA  . PRO L  1 74  ? 58.154 -2.287  -90.331  1.00 48.17 ? 74   PRO M CA  1 
ATOM   12794 C  C   . PRO L  1 74  ? 57.116 -1.816  -91.363  1.00 48.33 ? 74   PRO M C   1 
ATOM   12795 O  O   . PRO L  1 74  ? 56.026 -1.382  -90.979  1.00 48.23 ? 74   PRO M O   1 
ATOM   12796 C  CB  . PRO L  1 74  ? 59.195 -1.183  -90.063  1.00 48.20 ? 74   PRO M CB  1 
ATOM   12797 C  CG  . PRO L  1 74  ? 60.432 -1.623  -90.760  1.00 48.22 ? 74   PRO M CG  1 
ATOM   12798 C  CD  . PRO L  1 74  ? 60.411 -3.119  -90.740  1.00 48.13 ? 74   PRO M CD  1 
ATOM   12799 N  N   . LYS L  1 75  ? 57.446 -1.908  -92.650  1.00 48.41 ? 75   LYS M N   1 
ATOM   12800 C  CA  . LYS L  1 75  ? 56.550 -1.427  -93.702  1.00 48.48 ? 75   LYS M CA  1 
ATOM   12801 C  C   . LYS L  1 75  ? 55.694 -2.541  -94.323  1.00 48.37 ? 75   LYS M C   1 
ATOM   12802 O  O   . LYS L  1 75  ? 55.005 -2.316  -95.319  1.00 48.39 ? 75   LYS M O   1 
ATOM   12803 C  CB  . LYS L  1 75  ? 57.343 -0.672  -94.777  1.00 48.74 ? 75   LYS M CB  1 
ATOM   12804 C  CG  . LYS L  1 75  ? 58.090 0.558   -94.256  1.00 49.13 ? 75   LYS M CG  1 
ATOM   12805 C  CD  . LYS L  1 75  ? 59.010 1.166   -95.317  1.00 50.25 ? 75   LYS M CD  1 
ATOM   12806 C  CE  . LYS L  1 75  ? 60.392 0.500   -95.369  1.00 50.73 ? 75   LYS M CE  1 
ATOM   12807 N  NZ  . LYS L  1 75  ? 60.425 -0.719  -96.232  1.00 50.83 ? 75   LYS M NZ  1 
ATOM   12808 N  N   . ASP L  1 76  ? 55.721 -3.725  -93.713  1.00 48.21 ? 76   ASP M N   1 
ATOM   12809 C  CA  . ASP L  1 76  ? 54.954 -4.877  -94.194  1.00 48.22 ? 76   ASP M CA  1 
ATOM   12810 C  C   . ASP L  1 76  ? 53.555 -4.960  -93.593  1.00 48.21 ? 76   ASP M C   1 
ATOM   12811 O  O   . ASP L  1 76  ? 53.356 -4.639  -92.417  1.00 48.20 ? 76   ASP M O   1 
ATOM   12812 C  CB  . ASP L  1 76  ? 55.709 -6.175  -93.909  1.00 48.26 ? 76   ASP M CB  1 
ATOM   12813 C  CG  . ASP L  1 76  ? 56.979 -6.310  -94.737  1.00 48.76 ? 76   ASP M CG  1 
ATOM   12814 O  OD1 . ASP L  1 76  ? 57.974 -6.861  -94.214  1.00 48.97 ? 76   ASP M OD1 1 
ATOM   12815 O  OD2 . ASP L  1 76  ? 56.987 -5.865  -95.909  1.00 49.04 ? 76   ASP M OD2 1 
ATOM   12816 N  N   . GLU L  1 77  ? 52.594 -5.404  -94.407  1.00 48.03 ? 77   GLU M N   1 
ATOM   12817 C  CA  . GLU L  1 77  ? 51.209 -5.614  -93.962  1.00 47.81 ? 77   GLU M CA  1 
ATOM   12818 C  C   . GLU L  1 77  ? 51.101 -6.852  -93.060  1.00 47.33 ? 77   GLU M C   1 
ATOM   12819 O  O   . GLU L  1 77  ? 50.122 -7.022  -92.329  1.00 47.41 ? 77   GLU M O   1 
ATOM   12820 C  CB  . GLU L  1 77  ? 50.262 -5.720  -95.166  1.00 47.99 ? 77   GLU M CB  1 
ATOM   12821 C  CG  . GLU L  1 77  ? 48.884 -5.078  -94.954  1.00 49.11 ? 77   GLU M CG  1 
ATOM   12822 C  CD  . GLU L  1 77  ? 47.900 -5.980  -94.210  1.00 50.41 ? 77   GLU M CD  1 
ATOM   12823 O  OE1 . GLU L  1 77  ? 47.431 -6.980  -94.804  1.00 50.69 ? 77   GLU M OE1 1 
ATOM   12824 O  OE2 . GLU L  1 77  ? 47.585 -5.681  -93.034  1.00 50.88 ? 77   GLU M OE2 1 
ATOM   12825 N  N   . GLU L  1 78  ? 52.115 -7.711  -93.124  1.00 46.60 ? 78   GLU M N   1 
ATOM   12826 C  CA  . GLU L  1 78  ? 52.241 -8.841  -92.215  1.00 45.98 ? 78   GLU M CA  1 
ATOM   12827 C  C   . GLU L  1 78  ? 53.490 -8.643  -91.347  1.00 45.47 ? 78   GLU M C   1 
ATOM   12828 O  O   . GLU L  1 78  ? 54.617 -8.617  -91.858  1.00 45.47 ? 78   GLU M O   1 
ATOM   12829 C  CB  . GLU L  1 78  ? 52.286 -10.165 -92.992  1.00 45.98 ? 78   GLU M CB  1 
ATOM   12830 C  CG  . GLU L  1 78  ? 52.488 -11.429 -92.140  1.00 46.29 ? 78   GLU M CG  1 
ATOM   12831 C  CD  . GLU L  1 78  ? 51.231 -11.906 -91.413  1.00 46.71 ? 78   GLU M CD  1 
ATOM   12832 O  OE1 . GLU L  1 78  ? 51.295 -12.981 -90.777  1.00 46.78 ? 78   GLU M OE1 1 
ATOM   12833 O  OE2 . GLU L  1 78  ? 50.183 -11.226 -91.470  1.00 47.14 ? 78   GLU M OE2 1 
ATOM   12834 N  N   . ARG L  1 79  ? 53.268 -8.478  -90.041  1.00 44.63 ? 79   ARG M N   1 
ATOM   12835 C  CA  . ARG L  1 79  ? 54.342 -8.289  -89.054  1.00 43.76 ? 79   ARG M CA  1 
ATOM   12836 C  C   . ARG L  1 79  ? 53.851 -8.600  -87.634  1.00 43.47 ? 79   ARG M C   1 
ATOM   12837 O  O   . ARG L  1 79  ? 52.644 -8.580  -87.373  1.00 43.31 ? 79   ARG M O   1 
ATOM   12838 C  CB  . ARG L  1 79  ? 54.928 -6.858  -89.127  1.00 43.72 ? 79   ARG M CB  1 
ATOM   12839 C  CG  . ARG L  1 79  ? 53.909 -5.712  -88.999  1.00 42.90 ? 79   ARG M CG  1 
ATOM   12840 C  CD  . ARG L  1 79  ? 54.568 -4.324  -88.993  1.00 41.83 ? 79   ARG M CD  1 
ATOM   12841 N  NE  . ARG L  1 79  ? 54.949 -3.880  -87.644  1.00 39.79 ? 79   ARG M NE  1 
ATOM   12842 C  CZ  . ARG L  1 79  ? 55.356 -2.648  -87.327  1.00 39.59 ? 79   ARG M CZ  1 
ATOM   12843 N  NH1 . ARG L  1 79  ? 55.670 -2.353  -86.070  1.00 39.33 ? 79   ARG M NH1 1 
ATOM   12844 N  NH2 . ARG L  1 79  ? 55.442 -1.699  -88.247  1.00 39.54 ? 79   ARG M NH2 1 
ATOM   12845 N  N   . HIS L  1 80  ? 54.783 -8.913  -86.729  1.00 42.87 ? 80   HIS M N   1 
ATOM   12846 C  CA  . HIS L  1 80  ? 54.491 -8.892  -85.290  1.00 42.29 ? 80   HIS M CA  1 
ATOM   12847 C  C   . HIS L  1 80  ? 54.314 -7.422  -84.914  1.00 41.52 ? 80   HIS M C   1 
ATOM   12848 O  O   . HIS L  1 80  ? 54.857 -6.531  -85.578  1.00 41.25 ? 80   HIS M O   1 
ATOM   12849 C  CB  . HIS L  1 80  ? 55.640 -9.483  -84.454  1.00 42.50 ? 80   HIS M CB  1 
ATOM   12850 C  CG  . HIS L  1 80  ? 55.792 -10.974 -84.556  1.00 42.78 ? 80   HIS M CG  1 
ATOM   12851 N  ND1 . HIS L  1 80  ? 57.025 -11.591 -84.608  1.00 42.40 ? 80   HIS M ND1 1 
ATOM   12852 C  CD2 . HIS L  1 80  ? 54.875 -11.970 -84.587  1.00 43.04 ? 80   HIS M CD2 1 
ATOM   12853 C  CE1 . HIS L  1 80  ? 56.859 -12.899 -84.671  1.00 43.19 ? 80   HIS M CE1 1 
ATOM   12854 N  NE2 . HIS L  1 80  ? 55.563 -13.156 -84.662  1.00 43.12 ? 80   HIS M NE2 1 
ATOM   12855 N  N   . VAL L  1 81  ? 53.560 -7.167  -83.850  1.00 40.97 ? 81   VAL M N   1 
ATOM   12856 C  CA  . VAL L  1 81  ? 53.377 -5.805  -83.355  1.00 40.01 ? 81   VAL M CA  1 
ATOM   12857 C  C   . VAL L  1 81  ? 54.728 -5.112  -83.070  1.00 39.39 ? 81   VAL M C   1 
ATOM   12858 O  O   . VAL L  1 81  ? 54.928 -3.960  -83.448  1.00 38.87 ? 81   VAL M O   1 
ATOM   12859 C  CB  . VAL L  1 81  ? 52.433 -5.783  -82.118  1.00 40.21 ? 81   VAL M CB  1 
ATOM   12860 C  CG1 . VAL L  1 81  ? 52.358 -4.397  -81.497  1.00 39.90 ? 81   VAL M CG1 1 
ATOM   12861 C  CG2 . VAL L  1 81  ? 51.045 -6.292  -82.508  1.00 40.30 ? 81   VAL M CG2 1 
ATOM   12862 N  N   . GLY L  1 82  ? 55.657 -5.833  -82.446  1.00 39.03 ? 82   GLY M N   1 
ATOM   12863 C  CA  . GLY L  1 82  ? 56.967 -5.269  -82.079  1.00 38.98 ? 82   GLY M CA  1 
ATOM   12864 C  C   . GLY L  1 82  ? 58.042 -5.089  -83.154  1.00 38.95 ? 82   GLY M C   1 
ATOM   12865 O  O   . GLY L  1 82  ? 59.099 -4.500  -82.887  1.00 38.57 ? 82   GLY M O   1 
ATOM   12866 N  N   . ASP L  1 83  ? 57.783 -5.574  -84.371  1.00 38.95 ? 83   ASP M N   1 
ATOM   12867 C  CA  . ASP L  1 83  ? 58.814 -5.594  -85.419  1.00 38.89 ? 83   ASP M CA  1 
ATOM   12868 C  C   . ASP L  1 83  ? 59.131 -4.217  -86.013  1.00 39.17 ? 83   ASP M C   1 
ATOM   12869 O  O   . ASP L  1 83  ? 58.380 -3.690  -86.839  1.00 39.38 ? 83   ASP M O   1 
ATOM   12870 C  CB  . ASP L  1 83  ? 58.436 -6.567  -86.536  1.00 38.67 ? 83   ASP M CB  1 
ATOM   12871 C  CG  . ASP L  1 83  ? 58.464 -8.019  -86.093  1.00 38.12 ? 83   ASP M CG  1 
ATOM   12872 O  OD1 . ASP L  1 83  ? 59.391 -8.449  -85.367  1.00 35.89 ? 83   ASP M OD1 1 
ATOM   12873 O  OD2 . ASP L  1 83  ? 57.552 -8.751  -86.515  1.00 39.00 ? 83   ASP M OD2 1 
ATOM   12874 N  N   . LEU L  1 84  ? 60.261 -3.650  -85.602  1.00 39.62 ? 84   LEU M N   1 
ATOM   12875 C  CA  . LEU L  1 84  ? 60.697 -2.345  -86.103  1.00 40.15 ? 84   LEU M CA  1 
ATOM   12876 C  C   . LEU L  1 84  ? 61.872 -2.462  -87.100  1.00 40.43 ? 84   LEU M C   1 
ATOM   12877 O  O   . LEU L  1 84  ? 62.353 -1.456  -87.649  1.00 40.66 ? 84   LEU M O   1 
ATOM   12878 C  CB  . LEU L  1 84  ? 61.010 -1.407  -84.930  1.00 40.17 ? 84   LEU M CB  1 
ATOM   12879 C  CG  . LEU L  1 84  ? 59.809 -1.185  -83.994  1.00 40.58 ? 84   LEU M CG  1 
ATOM   12880 C  CD1 . LEU L  1 84  ? 60.225 -1.108  -82.530  1.00 40.74 ? 84   LEU M CD1 1 
ATOM   12881 C  CD2 . LEU L  1 84  ? 58.990 0.044   -84.395  1.00 41.04 ? 84   LEU M CD2 1 
ATOM   12882 N  N   . GLY L  1 85  ? 62.312 -3.694  -87.347  1.00 40.47 ? 85   GLY M N   1 
ATOM   12883 C  CA  . GLY L  1 85  ? 63.255 -3.965  -88.435  1.00 40.40 ? 85   GLY M CA  1 
ATOM   12884 C  C   . GLY L  1 85  ? 64.729 -3.867  -88.085  1.00 40.29 ? 85   GLY M C   1 
ATOM   12885 O  O   . GLY L  1 85  ? 65.270 -4.765  -87.438  1.00 40.48 ? 85   GLY M O   1 
ATOM   12886 N  N   . ASN L  1 86  ? 65.376 -2.784  -88.533  1.00 40.19 ? 86   ASN M N   1 
ATOM   12887 C  CA  . ASN L  1 86  ? 66.826 -2.581  -88.367  1.00 39.74 ? 86   ASN M CA  1 
ATOM   12888 C  C   . ASN L  1 86  ? 67.227 -1.122  -88.101  1.00 39.72 ? 86   ASN M C   1 
ATOM   12889 O  O   . ASN L  1 86  ? 66.609 -0.192  -88.623  1.00 39.52 ? 86   ASN M O   1 
ATOM   12890 C  CB  . ASN L  1 86  ? 67.597 -3.085  -89.604  1.00 40.03 ? 86   ASN M CB  1 
ATOM   12891 C  CG  . ASN L  1 86  ? 67.505 -4.591  -89.789  1.00 39.74 ? 86   ASN M CG  1 
ATOM   12892 O  OD1 . ASN L  1 86  ? 68.213 -5.357  -89.137  1.00 38.47 ? 86   ASN M OD1 1 
ATOM   12893 N  ND2 . ASN L  1 86  ? 66.634 -5.019  -90.696  1.00 40.21 ? 86   ASN M ND2 1 
ATOM   12894 N  N   . VAL L  1 87  ? 68.256 -0.937  -87.272  1.00 39.60 ? 87   VAL M N   1 
ATOM   12895 C  CA  . VAL L  1 87  ? 68.967 0.344   -87.153  1.00 39.75 ? 87   VAL M CA  1 
ATOM   12896 C  C   . VAL L  1 87  ? 70.360 0.188   -87.783  1.00 39.95 ? 87   VAL M C   1 
ATOM   12897 O  O   . VAL L  1 87  ? 70.801 -0.936  -88.032  1.00 39.61 ? 87   VAL M O   1 
ATOM   12898 C  CB  . VAL L  1 87  ? 69.105 0.819   -85.682  1.00 39.81 ? 87   VAL M CB  1 
ATOM   12899 C  CG1 . VAL L  1 87  ? 67.782 1.399   -85.163  1.00 39.21 ? 87   VAL M CG1 1 
ATOM   12900 C  CG2 . VAL L  1 87  ? 69.615 -0.311  -84.786  1.00 39.77 ? 87   VAL M CG2 1 
ATOM   12901 N  N   . THR L  1 88  ? 71.047 1.305   -88.024  1.00 40.45 ? 88   THR M N   1 
ATOM   12902 C  CA  . THR L  1 88  ? 72.346 1.280   -88.711  1.00 40.98 ? 88   THR M CA  1 
ATOM   12903 C  C   . THR L  1 88  ? 73.404 2.146   -88.030  1.00 41.45 ? 88   THR M C   1 
ATOM   12904 O  O   . THR L  1 88  ? 73.230 3.359   -87.871  1.00 41.27 ? 88   THR M O   1 
ATOM   12905 C  CB  . THR L  1 88  ? 72.214 1.674   -90.214  1.00 41.00 ? 88   THR M CB  1 
ATOM   12906 O  OG1 . THR L  1 88  ? 71.351 0.741   -90.876  1.00 40.96 ? 88   THR M OG1 1 
ATOM   12907 C  CG2 . THR L  1 88  ? 73.582 1.689   -90.923  1.00 40.80 ? 88   THR M CG2 1 
ATOM   12908 N  N   . ALA L  1 89  ? 74.503 1.503   -87.641  1.00 42.15 ? 89   ALA M N   1 
ATOM   12909 C  CA  . ALA L  1 89  ? 75.649 2.192   -87.064  1.00 42.90 ? 89   ALA M CA  1 
ATOM   12910 C  C   . ALA L  1 89  ? 76.760 2.405   -88.094  1.00 43.46 ? 89   ALA M C   1 
ATOM   12911 O  O   . ALA L  1 89  ? 77.036 1.531   -88.919  1.00 43.51 ? 89   ALA M O   1 
ATOM   12912 C  CB  . ALA L  1 89  ? 76.174 1.422   -85.867  1.00 42.88 ? 89   ALA M CB  1 
ATOM   12913 N  N   . ASP L  1 90  ? 77.387 3.578   -88.035  1.00 44.18 ? 90   ASP M N   1 
ATOM   12914 C  CA  . ASP L  1 90  ? 78.557 3.894   -88.856  1.00 44.96 ? 90   ASP M CA  1 
ATOM   12915 C  C   . ASP L  1 90  ? 79.802 3.189   -88.307  1.00 45.45 ? 90   ASP M C   1 
ATOM   12916 O  O   . ASP L  1 90  ? 79.692 2.333   -87.418  1.00 45.39 ? 90   ASP M O   1 
ATOM   12917 C  CB  . ASP L  1 90  ? 78.772 5.417   -88.932  1.00 44.96 ? 90   ASP M CB  1 
ATOM   12918 C  CG  . ASP L  1 90  ? 78.768 6.093   -87.557  1.00 45.07 ? 90   ASP M CG  1 
ATOM   12919 O  OD1 . ASP L  1 90  ? 78.659 7.340   -87.509  1.00 45.26 ? 90   ASP M OD1 1 
ATOM   12920 O  OD2 . ASP L  1 90  ? 78.873 5.393   -86.527  1.00 44.75 ? 90   ASP M OD2 1 
ATOM   12921 N  N   . LYS L  1 91  ? 80.976 3.550   -88.833  1.00 45.98 ? 91   LYS M N   1 
ATOM   12922 C  CA  . LYS L  1 91  ? 82.249 2.964   -88.387  1.00 46.64 ? 91   LYS M CA  1 
ATOM   12923 C  C   . LYS L  1 91  ? 82.756 3.506   -87.043  1.00 46.86 ? 91   LYS M C   1 
ATOM   12924 O  O   . LYS L  1 91  ? 83.848 3.151   -86.592  1.00 46.97 ? 91   LYS M O   1 
ATOM   12925 C  CB  . LYS L  1 91  ? 83.340 3.055   -89.475  1.00 46.72 ? 91   LYS M CB  1 
ATOM   12926 C  CG  . LYS L  1 91  ? 83.241 4.238   -90.441  1.00 47.43 ? 91   LYS M CG  1 
ATOM   12927 C  CD  . LYS L  1 91  ? 84.029 3.944   -91.727  1.00 48.18 ? 91   LYS M CD  1 
ATOM   12928 C  CE  . LYS L  1 91  ? 83.758 4.970   -92.825  1.00 48.78 ? 91   LYS M CE  1 
ATOM   12929 N  NZ  . LYS L  1 91  ? 84.409 6.286   -92.552  1.00 49.12 ? 91   LYS M NZ  1 
ATOM   12930 N  N   . ASP L  1 92  ? 81.962 4.369   -86.416  1.00 47.12 ? 92   ASP M N   1 
ATOM   12931 C  CA  . ASP L  1 92  ? 82.234 4.832   -85.057  1.00 47.35 ? 92   ASP M CA  1 
ATOM   12932 C  C   . ASP L  1 92  ? 81.449 4.002   -84.044  1.00 47.23 ? 92   ASP M C   1 
ATOM   12933 O  O   . ASP L  1 92  ? 81.650 4.133   -82.835  1.00 47.24 ? 92   ASP M O   1 
ATOM   12934 C  CB  . ASP L  1 92  ? 81.880 6.319   -84.906  1.00 47.59 ? 92   ASP M CB  1 
ATOM   12935 C  CG  . ASP L  1 92  ? 82.893 7.238   -85.571  1.00 48.21 ? 92   ASP M CG  1 
ATOM   12936 O  OD1 . ASP L  1 92  ? 82.641 8.462   -85.616  1.00 48.78 ? 92   ASP M OD1 1 
ATOM   12937 O  OD2 . ASP L  1 92  ? 83.938 6.738   -86.047  1.00 48.58 ? 92   ASP M OD2 1 
ATOM   12938 N  N   . GLY L  1 93  ? 80.561 3.150   -84.550  1.00 47.01 ? 93   GLY M N   1 
ATOM   12939 C  CA  . GLY L  1 93  ? 79.684 2.344   -83.706  1.00 46.89 ? 93   GLY M CA  1 
ATOM   12940 C  C   . GLY L  1 93  ? 78.345 3.001   -83.408  1.00 46.64 ? 93   GLY M C   1 
ATOM   12941 O  O   . GLY L  1 93  ? 77.443 2.356   -82.871  1.00 46.67 ? 93   GLY M O   1 
ATOM   12942 N  N   . VAL L  1 94  ? 78.220 4.279   -83.772  1.00 46.47 ? 94   VAL M N   1 
ATOM   12943 C  CA  . VAL L  1 94  ? 77.031 5.090   -83.478  1.00 46.25 ? 94   VAL M CA  1 
ATOM   12944 C  C   . VAL L  1 94  ? 75.899 4.876   -84.493  1.00 46.19 ? 94   VAL M C   1 
ATOM   12945 O  O   . VAL L  1 94  ? 76.082 5.061   -85.704  1.00 46.02 ? 94   VAL M O   1 
ATOM   12946 C  CB  . VAL L  1 94  ? 77.376 6.615   -83.377  1.00 46.33 ? 94   VAL M CB  1 
ATOM   12947 C  CG1 . VAL L  1 94  ? 76.168 7.427   -82.909  1.00 46.01 ? 94   VAL M CG1 1 
ATOM   12948 C  CG2 . VAL L  1 94  ? 78.560 6.857   -82.441  1.00 46.05 ? 94   VAL M CG2 1 
ATOM   12949 N  N   . ALA L  1 95  ? 74.735 4.480   -83.980  1.00 45.95 ? 95   ALA M N   1 
ATOM   12950 C  CA  . ALA L  1 95  ? 73.506 4.389   -84.768  1.00 45.72 ? 95   ALA M CA  1 
ATOM   12951 C  C   . ALA L  1 95  ? 72.543 5.499   -84.346  1.00 45.69 ? 95   ALA M C   1 
ATOM   12952 O  O   . ALA L  1 95  ? 71.936 5.429   -83.275  1.00 45.79 ? 95   ALA M O   1 
ATOM   12953 C  CB  . ALA L  1 95  ? 72.860 3.011   -84.602  1.00 45.55 ? 95   ALA M CB  1 
ATOM   12954 N  N   . ASP L  1 96  ? 72.427 6.532   -85.181  1.00 45.39 ? 96   ASP M N   1 
ATOM   12955 C  CA  . ASP L  1 96  ? 71.548 7.662   -84.896  1.00 45.09 ? 96   ASP M CA  1 
ATOM   12956 C  C   . ASP L  1 96  ? 70.143 7.342   -85.399  1.00 44.61 ? 96   ASP M C   1 
ATOM   12957 O  O   . ASP L  1 96  ? 69.944 7.085   -86.584  1.00 44.45 ? 96   ASP M O   1 
ATOM   12958 C  CB  . ASP L  1 96  ? 72.093 8.948   -85.534  1.00 45.36 ? 96   ASP M CB  1 
ATOM   12959 C  CG  . ASP L  1 96  ? 71.388 10.208  -85.030  1.00 46.12 ? 96   ASP M CG  1 
ATOM   12960 O  OD1 . ASP L  1 96  ? 71.270 10.398  -83.793  1.00 46.25 ? 96   ASP M OD1 1 
ATOM   12961 O  OD2 . ASP L  1 96  ? 70.963 11.021  -85.880  1.00 46.80 ? 96   ASP M OD2 1 
ATOM   12962 N  N   . VAL L  1 97  ? 69.172 7.351   -84.489  1.00 43.99 ? 97   VAL M N   1 
ATOM   12963 C  CA  . VAL L  1 97  ? 67.835 6.839   -84.798  1.00 43.40 ? 97   VAL M CA  1 
ATOM   12964 C  C   . VAL L  1 97  ? 66.824 7.948   -85.086  1.00 42.93 ? 97   VAL M C   1 
ATOM   12965 O  O   . VAL L  1 97  ? 66.793 8.980   -84.408  1.00 42.61 ? 97   VAL M O   1 
ATOM   12966 C  CB  . VAL L  1 97  ? 67.306 5.881   -83.700  1.00 43.27 ? 97   VAL M CB  1 
ATOM   12967 C  CG1 . VAL L  1 97  ? 66.115 5.092   -84.214  1.00 43.60 ? 97   VAL M CG1 1 
ATOM   12968 C  CG2 . VAL L  1 97  ? 68.405 4.922   -83.250  1.00 43.41 ? 97   VAL M CG2 1 
ATOM   12969 N  N   . SER L  1 98  ? 66.016 7.708   -86.117  1.00 42.32 ? 98   SER M N   1 
ATOM   12970 C  CA  . SER L  1 98  ? 64.979 8.624   -86.568  1.00 42.03 ? 98   SER M CA  1 
ATOM   12971 C  C   . SER L  1 98  ? 63.945 7.802   -87.338  1.00 41.36 ? 98   SER M C   1 
ATOM   12972 O  O   . SER L  1 98  ? 64.210 7.353   -88.454  1.00 41.35 ? 98   SER M O   1 
ATOM   12973 C  CB  . SER L  1 98  ? 65.590 9.726   -87.442  1.00 42.21 ? 98   SER M CB  1 
ATOM   12974 O  OG  . SER L  1 98  ? 64.592 10.531  -88.040  1.00 43.50 ? 98   SER M OG  1 
ATOM   12975 N  N   . ILE L  1 99  ? 62.781 7.587   -86.725  1.00 40.79 ? 99   ILE M N   1 
ATOM   12976 C  CA  . ILE L  1 99  ? 61.766 6.650   -87.241  1.00 40.19 ? 99   ILE M CA  1 
ATOM   12977 C  C   . ILE L  1 99  ? 60.333 7.175   -87.026  1.00 40.06 ? 99   ILE M C   1 
ATOM   12978 O  O   . ILE L  1 99  ? 60.099 7.992   -86.132  1.00 39.92 ? 99   ILE M O   1 
ATOM   12979 C  CB  . ILE L  1 99  ? 61.913 5.231   -86.572  1.00 40.09 ? 99   ILE M CB  1 
ATOM   12980 C  CG1 . ILE L  1 99  ? 63.206 4.535   -87.003  1.00 40.15 ? 99   ILE M CG1 1 
ATOM   12981 C  CG2 . ILE L  1 99  ? 60.724 4.320   -86.883  1.00 39.76 ? 99   ILE M CG2 1 
ATOM   12982 C  CD1 . ILE L  1 99  ? 63.517 3.284   -86.194  1.00 40.14 ? 99   ILE M CD1 1 
ATOM   12983 N  N   . GLU L  1 100 ? 59.402 6.707   -87.866  1.00 39.69 ? 100  GLU M N   1 
ATOM   12984 C  CA  . GLU L  1 100 ? 57.952 6.839   -87.668  1.00 39.60 ? 100  GLU M CA  1 
ATOM   12985 C  C   . GLU L  1 100 ? 57.350 5.438   -87.774  1.00 39.17 ? 100  GLU M C   1 
ATOM   12986 O  O   . GLU L  1 100 ? 57.833 4.632   -88.569  1.00 39.19 ? 100  GLU M O   1 
ATOM   12987 C  CB  . GLU L  1 100 ? 57.339 7.715   -88.761  1.00 39.77 ? 100  GLU M CB  1 
ATOM   12988 C  CG  . GLU L  1 100 ? 56.169 8.585   -88.315  1.00 41.02 ? 100  GLU M CG  1 
ATOM   12989 C  CD  . GLU L  1 100 ? 56.608 9.975   -87.901  1.00 41.85 ? 100  GLU M CD  1 
ATOM   12990 O  OE1 . GLU L  1 100 ? 57.649 10.091  -87.223  1.00 42.76 ? 100  GLU M OE1 1 
ATOM   12991 O  OE2 . GLU L  1 100 ? 55.919 10.954  -88.258  1.00 41.64 ? 100  GLU M OE2 1 
ATOM   12992 N  N   . ASP L  1 101 ? 56.306 5.140   -86.991  1.00 38.55 ? 101  ASP M N   1 
ATOM   12993 C  CA  . ASP L  1 101 ? 55.662 3.807   -87.038  1.00 37.95 ? 101  ASP M CA  1 
ATOM   12994 C  C   . ASP L  1 101 ? 54.170 3.723   -86.652  1.00 37.60 ? 101  ASP M C   1 
ATOM   12995 O  O   . ASP L  1 101 ? 53.763 4.165   -85.569  1.00 37.50 ? 101  ASP M O   1 
ATOM   12996 C  CB  . ASP L  1 101 ? 56.440 2.786   -86.212  1.00 38.01 ? 101  ASP M CB  1 
ATOM   12997 C  CG  . ASP L  1 101 ? 56.020 1.369   -86.516  1.00 38.10 ? 101  ASP M CG  1 
ATOM   12998 O  OD1 . ASP L  1 101 ? 55.203 0.812   -85.756  1.00 37.98 ? 101  ASP M OD1 1 
ATOM   12999 O  OD2 . ASP L  1 101 ? 56.482 0.825   -87.538  1.00 39.58 ? 101  ASP M OD2 1 
ATOM   13000 N  N   . SER L  1 102 ? 53.390 3.070   -87.518  1.00 36.52 ? 102  SER M N   1 
ATOM   13001 C  CA  . SER L  1 102 ? 51.921 3.044   -87.430  1.00 35.62 ? 102  SER M CA  1 
ATOM   13002 C  C   . SER L  1 102 ? 51.295 1.837   -86.717  1.00 34.55 ? 102  SER M C   1 
ATOM   13003 O  O   . SER L  1 102 ? 50.074 1.803   -86.517  1.00 34.52 ? 102  SER M O   1 
ATOM   13004 C  CB  . SER L  1 102 ? 51.325 3.143   -88.840  1.00 35.46 ? 102  SER M CB  1 
ATOM   13005 O  OG  . SER L  1 102 ? 51.803 4.291   -89.512  1.00 36.04 ? 102  SER M OG  1 
ATOM   13006 N  N   . VAL L  1 103 ? 52.101 0.840   -86.357  1.00 33.08 ? 103  VAL M N   1 
ATOM   13007 C  CA  . VAL L  1 103 ? 51.541 -0.383  -85.772  1.00 31.90 ? 103  VAL M CA  1 
ATOM   13008 C  C   . VAL L  1 103 ? 51.578 -0.367  -84.237  1.00 31.27 ? 103  VAL M C   1 
ATOM   13009 O  O   . VAL L  1 103 ? 50.547 -0.533  -83.591  1.00 31.16 ? 103  VAL M O   1 
ATOM   13010 C  CB  . VAL L  1 103 ? 52.189 -1.665  -86.344  1.00 31.86 ? 103  VAL M CB  1 
ATOM   13011 C  CG1 . VAL L  1 103 ? 51.652 -2.903  -85.647  1.00 31.77 ? 103  VAL M CG1 1 
ATOM   13012 C  CG2 . VAL L  1 103 ? 51.926 -1.766  -87.854  1.00 32.17 ? 103  VAL M CG2 1 
ATOM   13013 N  N   . ILE L  1 104 ? 52.759 -0.170  -83.659  1.00 30.08 ? 104  ILE M N   1 
ATOM   13014 C  CA  . ILE L  1 104 ? 52.858 -0.054  -82.198  1.00 29.11 ? 104  ILE M CA  1 
ATOM   13015 C  C   . ILE L  1 104 ? 52.138 1.201   -81.681  1.00 28.81 ? 104  ILE M C   1 
ATOM   13016 O  O   . ILE L  1 104 ? 51.895 2.142   -82.434  1.00 28.82 ? 104  ILE M O   1 
ATOM   13017 C  CB  . ILE L  1 104 ? 54.319 -0.097  -81.694  1.00 29.00 ? 104  ILE M CB  1 
ATOM   13018 C  CG1 . ILE L  1 104 ? 55.199 0.875   -82.479  1.00 28.68 ? 104  ILE M CG1 1 
ATOM   13019 C  CG2 . ILE L  1 104 ? 54.866 -1.521  -81.748  1.00 28.87 ? 104  ILE M CG2 1 
ATOM   13020 C  CD1 . ILE L  1 104 ? 56.419 1.337   -81.731  1.00 28.83 ? 104  ILE M CD1 1 
ATOM   13021 N  N   . SER L  1 105 ? 51.786 1.201   -80.395  1.00 28.42 ? 105  SER M N   1 
ATOM   13022 C  CA  . SER L  1 105 ? 51.112 2.350   -79.782  1.00 28.02 ? 105  SER M CA  1 
ATOM   13023 C  C   . SER L  1 105 ? 51.593 2.558   -78.353  1.00 27.64 ? 105  SER M C   1 
ATOM   13024 O  O   . SER L  1 105 ? 51.978 1.602   -77.694  1.00 27.40 ? 105  SER M O   1 
ATOM   13025 C  CB  . SER L  1 105 ? 49.595 2.161   -79.789  1.00 27.50 ? 105  SER M CB  1 
ATOM   13026 O  OG  . SER L  1 105 ? 48.957 3.375   -79.449  1.00 28.70 ? 105  SER M OG  1 
ATOM   13027 N  N   . LEU L  1 106 ? 51.586 3.812   -77.900  1.00 27.96 ? 106  LEU M N   1 
ATOM   13028 C  CA  . LEU L  1 106 ? 51.937 4.145   -76.506  1.00 27.82 ? 106  LEU M CA  1 
ATOM   13029 C  C   . LEU L  1 106 ? 50.707 4.111   -75.580  1.00 28.39 ? 106  LEU M C   1 
ATOM   13030 O  O   . LEU L  1 106 ? 50.837 4.274   -74.356  1.00 28.00 ? 106  LEU M O   1 
ATOM   13031 C  CB  . LEU L  1 106 ? 52.649 5.504   -76.424  1.00 27.65 ? 106  LEU M CB  1 
ATOM   13032 C  CG  . LEU L  1 106 ? 53.948 5.685   -77.232  1.00 27.64 ? 106  LEU M CG  1 
ATOM   13033 C  CD1 . LEU L  1 106 ? 54.573 7.056   -76.985  1.00 27.52 ? 106  LEU M CD1 1 
ATOM   13034 C  CD2 . LEU L  1 106 ? 54.939 4.579   -76.932  1.00 26.56 ? 106  LEU M CD2 1 
ATOM   13035 N  N   . SER L  1 107 ? 49.525 3.894   -76.163  1.00 28.65 ? 107  SER M N   1 
ATOM   13036 C  CA  . SER L  1 107 ? 48.277 3.741   -75.393  1.00 29.13 ? 107  SER M CA  1 
ATOM   13037 C  C   . SER L  1 107 ? 47.377 2.621   -75.946  1.00 29.52 ? 107  SER M C   1 
ATOM   13038 O  O   . SER L  1 107 ? 47.752 1.922   -76.901  1.00 29.52 ? 107  SER M O   1 
ATOM   13039 C  CB  . SER L  1 107 ? 47.523 5.076   -75.292  1.00 28.93 ? 107  SER M CB  1 
ATOM   13040 O  OG  . SER L  1 107 ? 47.350 5.710   -76.559  1.00 29.54 ? 107  SER M OG  1 
ATOM   13041 N  N   . GLY L  1 108 ? 46.209 2.434   -75.332  1.00 29.62 ? 108  GLY M N   1 
ATOM   13042 C  CA  . GLY L  1 108 ? 45.276 1.377   -75.736  1.00 30.41 ? 108  GLY M CA  1 
ATOM   13043 C  C   . GLY L  1 108 ? 45.719 0.007   -75.247  1.00 30.75 ? 108  GLY M C   1 
ATOM   13044 O  O   . GLY L  1 108 ? 46.842 -0.150  -74.782  1.00 30.39 ? 108  GLY M O   1 
ATOM   13045 N  N   . ASP L  1 109 ? 44.844 -0.990  -75.369  1.00 31.53 ? 109  ASP M N   1 
ATOM   13046 C  CA  . ASP L  1 109 ? 45.096 -2.318  -74.786  1.00 32.35 ? 109  ASP M CA  1 
ATOM   13047 C  C   . ASP L  1 109 ? 46.187 -3.175  -75.458  1.00 32.57 ? 109  ASP M C   1 
ATOM   13048 O  O   . ASP L  1 109 ? 46.398 -4.326  -75.065  1.00 33.02 ? 109  ASP M O   1 
ATOM   13049 C  CB  . ASP L  1 109 ? 43.790 -3.113  -74.587  1.00 32.81 ? 109  ASP M CB  1 
ATOM   13050 C  CG  . ASP L  1 109 ? 43.052 -3.414  -75.895  1.00 34.20 ? 109  ASP M CG  1 
ATOM   13051 O  OD1 . ASP L  1 109 ? 43.486 -2.971  -76.986  1.00 34.80 ? 109  ASP M OD1 1 
ATOM   13052 O  OD2 . ASP L  1 109 ? 42.007 -4.103  -75.821  1.00 36.12 ? 109  ASP M OD2 1 
ATOM   13053 N  N   . HIS L  1 110 ? 46.871 -2.619  -76.455  1.00 32.60 ? 110  HIS M N   1 
ATOM   13054 C  CA  . HIS L  1 110 ? 48.080 -3.250  -77.005  1.00 32.64 ? 110  HIS M CA  1 
ATOM   13055 C  C   . HIS L  1 110 ? 49.273 -2.287  -77.018  1.00 32.27 ? 110  HIS M C   1 
ATOM   13056 O  O   . HIS L  1 110 ? 50.144 -2.355  -77.901  1.00 32.50 ? 110  HIS M O   1 
ATOM   13057 C  CB  . HIS L  1 110 ? 47.811 -3.845  -78.401  1.00 32.90 ? 110  HIS M CB  1 
ATOM   13058 C  CG  . HIS L  1 110 ? 46.785 -4.939  -78.399  1.00 34.02 ? 110  HIS M CG  1 
ATOM   13059 N  ND1 . HIS L  1 110 ? 45.738 -4.985  -79.295  1.00 35.95 ? 110  HIS M ND1 1 
ATOM   13060 C  CD2 . HIS L  1 110 ? 46.636 -6.019  -77.595  1.00 35.39 ? 110  HIS M CD2 1 
ATOM   13061 C  CE1 . HIS L  1 110 ? 44.991 -6.045  -79.042  1.00 36.13 ? 110  HIS M CE1 1 
ATOM   13062 N  NE2 . HIS L  1 110 ? 45.515 -6.689  -78.014  1.00 36.04 ? 110  HIS M NE2 1 
HETATM 13063 N  N   . CME L  1 111 ? 49.313 -1.394  -76.027  1.00 31.53 ? 111  CME M N   1 
HETATM 13064 C  CA  . CME L  1 111 ? 50.427 -0.458  -75.873  1.00 30.82 ? 111  CME M CA  1 
HETATM 13065 C  CB  . CME L  1 111 ? 50.142 0.505   -74.719  1.00 31.11 ? 111  CME M CB  1 
HETATM 13066 S  SG  . CME L  1 111 ? 50.197 -0.315  -73.157  1.00 32.36 ? 111  CME M SG  1 
HETATM 13067 S  SD  . CME L  1 111 ? 49.617 1.168   -71.922  1.00 34.62 ? 111  CME M SD  1 
HETATM 13068 C  CE  . CME L  1 111 ? 47.852 1.190   -72.029  1.00 34.20 ? 111  CME M CE  1 
HETATM 13069 C  CZ  . CME L  1 111 ? 47.244 -0.070  -71.431  1.00 34.06 ? 111  CME M CZ  1 
HETATM 13070 O  OH  . CME L  1 111 ? 47.661 -0.197  -70.069  1.00 37.84 ? 111  CME M OH  1 
HETATM 13071 C  C   . CME L  1 111 ? 51.729 -1.171  -75.632  1.00 29.74 ? 111  CME M C   1 
HETATM 13072 O  O   . CME L  1 111 ? 51.734 -2.312  -75.173  1.00 29.17 ? 111  CME M O   1 
ATOM   13073 N  N   . ILE L  1 112 ? 52.839 -0.500  -75.950  1.00 29.15 ? 112  ILE M N   1 
ATOM   13074 C  CA  . ILE L  1 112 ? 54.192 -1.032  -75.708  1.00 28.51 ? 112  ILE M CA  1 
ATOM   13075 C  C   . ILE L  1 112 ? 54.813 -0.566  -74.367  1.00 28.75 ? 112  ILE M C   1 
ATOM   13076 O  O   . ILE L  1 112 ? 55.954 -0.911  -74.048  1.00 28.30 ? 112  ILE M O   1 
ATOM   13077 C  CB  . ILE L  1 112 ? 55.156 -0.710  -76.875  1.00 28.49 ? 112  ILE M CB  1 
ATOM   13078 C  CG1 . ILE L  1 112 ? 55.442 0.801   -76.943  1.00 28.70 ? 112  ILE M CG1 1 
ATOM   13079 C  CG2 . ILE L  1 112 ? 54.570 -1.249  -78.198  1.00 27.92 ? 112  ILE M CG2 1 
ATOM   13080 C  CD1 . ILE L  1 112 ? 56.506 1.228   -77.954  1.00 27.78 ? 112  ILE M CD1 1 
ATOM   13081 N  N   . ILE L  1 113 ? 54.066 0.222   -73.594  1.00 28.69 ? 113  ILE M N   1 
ATOM   13082 C  CA  . ILE L  1 113 ? 54.512 0.612   -72.254  1.00 28.66 ? 113  ILE M CA  1 
ATOM   13083 C  C   . ILE L  1 113 ? 54.717 -0.632  -71.381  1.00 29.01 ? 113  ILE M C   1 
ATOM   13084 O  O   . ILE L  1 113 ? 53.846 -1.494  -71.318  1.00 29.18 ? 113  ILE M O   1 
ATOM   13085 C  CB  . ILE L  1 113 ? 53.498 1.564   -71.573  1.00 28.46 ? 113  ILE M CB  1 
ATOM   13086 C  CG1 . ILE L  1 113 ? 53.281 2.845   -72.395  1.00 27.17 ? 113  ILE M CG1 1 
ATOM   13087 C  CG2 . ILE L  1 113 ? 53.906 1.860   -70.118  1.00 28.53 ? 113  ILE M CG2 1 
ATOM   13088 C  CD1 . ILE L  1 113 ? 54.552 3.627   -72.806  1.00 27.92 ? 113  ILE M CD1 1 
ATOM   13089 N  N   . GLY L  1 114 ? 55.865 -0.724  -70.707  1.00 29.33 ? 114  GLY M N   1 
ATOM   13090 C  CA  . GLY L  1 114 ? 56.101 -1.808  -69.756  1.00 29.90 ? 114  GLY M CA  1 
ATOM   13091 C  C   . GLY L  1 114 ? 56.656 -3.049  -70.416  1.00 30.75 ? 114  GLY M C   1 
ATOM   13092 O  O   . GLY L  1 114 ? 56.806 -4.097  -69.782  1.00 30.23 ? 114  GLY M O   1 
ATOM   13093 N  N   . ARG L  1 115 ? 56.943 -2.925  -71.707  1.00 31.74 ? 115  ARG M N   1 
ATOM   13094 C  CA  . ARG L  1 115 ? 57.499 -4.016  -72.486  1.00 32.81 ? 115  ARG M CA  1 
ATOM   13095 C  C   . ARG L  1 115 ? 58.945 -3.680  -72.814  1.00 33.62 ? 115  ARG M C   1 
ATOM   13096 O  O   . ARG L  1 115 ? 59.419 -2.595  -72.475  1.00 33.42 ? 115  ARG M O   1 
ATOM   13097 C  CB  . ARG L  1 115 ? 56.638 -4.275  -73.733  1.00 32.80 ? 115  ARG M CB  1 
ATOM   13098 C  CG  . ARG L  1 115 ? 55.197 -4.642  -73.341  1.00 32.63 ? 115  ARG M CG  1 
ATOM   13099 C  CD  . ARG L  1 115 ? 54.294 -4.939  -74.521  1.00 32.94 ? 115  ARG M CD  1 
ATOM   13100 N  NE  . ARG L  1 115 ? 52.922 -5.242  -74.094  1.00 30.99 ? 115  ARG M NE  1 
ATOM   13101 C  CZ  . ARG L  1 115 ? 52.537 -6.375  -73.509  1.00 30.54 ? 115  ARG M CZ  1 
ATOM   13102 N  NH1 . ARG L  1 115 ? 51.265 -6.555  -73.172  1.00 31.50 ? 115  ARG M NH1 1 
ATOM   13103 N  NH2 . ARG L  1 115 ? 53.412 -7.334  -73.260  1.00 31.22 ? 115  ARG M NH2 1 
ATOM   13104 N  N   . THR L  1 116 ? 59.636 -4.606  -73.478  1.00 34.70 ? 116  THR M N   1 
ATOM   13105 C  CA  . THR L  1 116 ? 61.083 -4.527  -73.647  1.00 35.94 ? 116  THR M CA  1 
ATOM   13106 C  C   . THR L  1 116 ? 61.502 -4.180  -75.081  1.00 36.50 ? 116  THR M C   1 
ATOM   13107 O  O   . THR L  1 116 ? 61.066 -4.827  -76.026  1.00 36.82 ? 116  THR M O   1 
ATOM   13108 C  CB  . THR L  1 116 ? 61.743 -5.856  -73.200  1.00 36.19 ? 116  THR M CB  1 
ATOM   13109 O  OG1 . THR L  1 116 ? 61.330 -6.167  -71.863  1.00 36.21 ? 116  THR M OG1 1 
ATOM   13110 C  CG2 . THR L  1 116 ? 63.258 -5.758  -73.225  1.00 36.51 ? 116  THR M CG2 1 
ATOM   13111 N  N   . LEU L  1 117 ? 62.319 -3.139  -75.234  1.00 36.95 ? 117  LEU M N   1 
ATOM   13112 C  CA  . LEU L  1 117 ? 62.959 -2.830  -76.514  1.00 37.40 ? 117  LEU M CA  1 
ATOM   13113 C  C   . LEU L  1 117 ? 64.310 -3.537  -76.574  1.00 37.80 ? 117  LEU M C   1 
ATOM   13114 O  O   . LEU L  1 117 ? 65.012 -3.614  -75.563  1.00 37.48 ? 117  LEU M O   1 
ATOM   13115 C  CB  . LEU L  1 117 ? 63.137 -1.314  -76.684  1.00 37.50 ? 117  LEU M CB  1 
ATOM   13116 C  CG  . LEU L  1 117 ? 63.822 -0.751  -77.936  1.00 37.30 ? 117  LEU M CG  1 
ATOM   13117 C  CD1 . LEU L  1 117 ? 62.967 -0.926  -79.185  1.00 37.50 ? 117  LEU M CD1 1 
ATOM   13118 C  CD2 . LEU L  1 117 ? 64.169 0.707   -77.745  1.00 37.39 ? 117  LEU M CD2 1 
ATOM   13119 N  N   . VAL L  1 118 ? 64.664 -4.059  -77.753  1.00 38.28 ? 118  VAL M N   1 
ATOM   13120 C  CA  . VAL L  1 118 ? 65.898 -4.843  -77.930  1.00 38.93 ? 118  VAL M CA  1 
ATOM   13121 C  C   . VAL L  1 118 ? 66.669 -4.454  -79.193  1.00 39.48 ? 118  VAL M C   1 
ATOM   13122 O  O   . VAL L  1 118 ? 66.073 -4.211  -80.245  1.00 39.10 ? 118  VAL M O   1 
ATOM   13123 C  CB  . VAL L  1 118 ? 65.614 -6.379  -77.992  1.00 39.10 ? 118  VAL M CB  1 
ATOM   13124 C  CG1 . VAL L  1 118 ? 66.893 -7.163  -78.278  1.00 38.77 ? 118  VAL M CG1 1 
ATOM   13125 C  CG2 . VAL L  1 118 ? 64.982 -6.879  -76.706  1.00 38.47 ? 118  VAL M CG2 1 
ATOM   13126 N  N   . VAL L  1 119 ? 67.994 -4.392  -79.067  1.00 40.09 ? 119  VAL M N   1 
ATOM   13127 C  CA  . VAL L  1 119 ? 68.902 -4.347  -80.213  1.00 40.75 ? 119  VAL M CA  1 
ATOM   13128 C  C   . VAL L  1 119 ? 69.655 -5.689  -80.285  1.00 41.37 ? 119  VAL M C   1 
ATOM   13129 O  O   . VAL L  1 119 ? 70.065 -6.232  -79.254  1.00 41.35 ? 119  VAL M O   1 
ATOM   13130 C  CB  . VAL L  1 119 ? 69.850 -3.109  -80.155  1.00 40.82 ? 119  VAL M CB  1 
ATOM   13131 C  CG1 . VAL L  1 119 ? 70.771 -3.154  -78.934  1.00 40.52 ? 119  VAL M CG1 1 
ATOM   13132 C  CG2 . VAL L  1 119 ? 70.649 -2.952  -81.459  1.00 40.63 ? 119  VAL M CG2 1 
ATOM   13133 N  N   . HIS L  1 120 ? 69.805 -6.230  -81.497  1.00 42.07 ? 120  HIS M N   1 
ATOM   13134 C  CA  . HIS L  1 120 ? 70.271 -7.615  -81.690  1.00 42.77 ? 120  HIS M CA  1 
ATOM   13135 C  C   . HIS L  1 120 ? 71.697 -7.737  -82.263  1.00 43.24 ? 120  HIS M C   1 
ATOM   13136 O  O   . HIS L  1 120 ? 72.278 -6.760  -82.755  1.00 43.19 ? 120  HIS M O   1 
ATOM   13137 C  CB  . HIS L  1 120 ? 69.303 -8.392  -82.595  1.00 42.77 ? 120  HIS M CB  1 
ATOM   13138 C  CG  . HIS L  1 120 ? 68.126 -8.983  -81.883  1.00 43.04 ? 120  HIS M CG  1 
ATOM   13139 N  ND1 . HIS L  1 120 ? 68.178 -10.196 -81.229  1.00 43.02 ? 120  HIS M ND1 1 
ATOM   13140 C  CD2 . HIS L  1 120 ? 66.850 -8.544  -81.758  1.00 42.95 ? 120  HIS M CD2 1 
ATOM   13141 C  CE1 . HIS L  1 120 ? 66.990 -10.472 -80.719  1.00 42.93 ? 120  HIS M CE1 1 
ATOM   13142 N  NE2 . HIS L  1 120 ? 66.164 -9.487  -81.030  1.00 42.94 ? 120  HIS M NE2 1 
ATOM   13143 N  N   . GLU L  1 121 ? 72.230 -8.959  -82.197  1.00 43.76 ? 121  GLU M N   1 
ATOM   13144 C  CA  . GLU L  1 121 ? 73.571 -9.301  -82.688  1.00 44.38 ? 121  GLU M CA  1 
ATOM   13145 C  C   . GLU L  1 121 ? 73.693 -9.146  -84.213  1.00 44.54 ? 121  GLU M C   1 
ATOM   13146 O  O   . GLU L  1 121 ? 74.652 -8.547  -84.712  1.00 44.63 ? 121  GLU M O   1 
ATOM   13147 C  CB  . GLU L  1 121 ? 73.914 -10.739 -82.261  1.00 44.52 ? 121  GLU M CB  1 
ATOM   13148 C  CG  . GLU L  1 121 ? 75.188 -11.327 -82.874  1.00 45.17 ? 121  GLU M CG  1 
ATOM   13149 C  CD  . GLU L  1 121 ? 75.170 -12.850 -82.939  1.00 46.10 ? 121  GLU M CD  1 
ATOM   13150 O  OE1 . GLU L  1 121 ? 76.124 -13.425 -83.506  1.00 47.23 ? 121  GLU M OE1 1 
ATOM   13151 O  OE2 . GLU L  1 121 ? 74.207 -13.476 -82.440  1.00 46.42 ? 121  GLU M OE2 1 
ATOM   13152 N  N   . LYS L  1 122 ? 72.711 -9.686  -84.932  1.00 44.66 ? 122  LYS M N   1 
ATOM   13153 C  CA  . LYS L  1 122 ? 72.694 -9.689  -86.396  1.00 44.82 ? 122  LYS M CA  1 
ATOM   13154 C  C   . LYS L  1 122 ? 71.578 -8.795  -86.944  1.00 44.82 ? 122  LYS M C   1 
ATOM   13155 O  O   . LYS L  1 122 ? 70.716 -8.320  -86.190  1.00 44.76 ? 122  LYS M O   1 
ATOM   13156 C  CB  . LYS L  1 122 ? 72.494 -11.123 -86.904  1.00 44.80 ? 122  LYS M CB  1 
ATOM   13157 C  CG  . LYS L  1 122 ? 73.653 -12.056 -86.619  1.00 45.45 ? 122  LYS M CG  1 
ATOM   13158 C  CD  . LYS L  1 122 ? 73.198 -13.499 -86.435  1.00 46.35 ? 122  LYS M CD  1 
ATOM   13159 C  CE  . LYS L  1 122 ? 74.412 -14.432 -86.351  1.00 47.13 ? 122  LYS M CE  1 
ATOM   13160 N  NZ  . LYS L  1 122 ? 74.125 -15.715 -85.642  1.00 47.74 ? 122  LYS M NZ  1 
ATOM   13161 N  N   . ALA L  1 123 ? 71.599 -8.573  -88.258  1.00 44.70 ? 123  ALA M N   1 
ATOM   13162 C  CA  . ALA L  1 123 ? 70.494 -7.921  -88.957  1.00 44.67 ? 123  ALA M CA  1 
ATOM   13163 C  C   . ALA L  1 123 ? 69.259 -8.829  -88.956  1.00 44.68 ? 123  ALA M C   1 
ATOM   13164 O  O   . ALA L  1 123 ? 69.386 -10.054 -88.879  1.00 44.55 ? 123  ALA M O   1 
ATOM   13165 C  CB  . ALA L  1 123 ? 70.903 -7.563  -90.380  1.00 44.71 ? 123  ALA M CB  1 
ATOM   13166 N  N   . ASP L  1 124 ? 68.070 -8.228  -89.008  1.00 44.65 ? 124  ASP M N   1 
ATOM   13167 C  CA  . ASP L  1 124 ? 66.822 -8.990  -89.110  1.00 44.81 ? 124  ASP M CA  1 
ATOM   13168 C  C   . ASP L  1 124 ? 66.492 -9.171  -90.585  1.00 44.61 ? 124  ASP M C   1 
ATOM   13169 O  O   . ASP L  1 124 ? 66.427 -8.189  -91.327  1.00 44.43 ? 124  ASP M O   1 
ATOM   13170 C  CB  . ASP L  1 124 ? 65.675 -8.258  -88.397  1.00 44.79 ? 124  ASP M CB  1 
ATOM   13171 C  CG  . ASP L  1 124 ? 64.453 -9.156  -88.131  1.00 45.35 ? 124  ASP M CG  1 
ATOM   13172 O  OD1 . ASP L  1 124 ? 63.518 -8.676  -87.439  1.00 44.88 ? 124  ASP M OD1 1 
ATOM   13173 O  OD2 . ASP L  1 124 ? 64.417 -10.330 -88.586  1.00 44.81 ? 124  ASP M OD2 1 
ATOM   13174 N  N   . ASP L  1 125 ? 66.278 -10.418 -91.004  1.00 44.77 ? 125  ASP M N   1 
ATOM   13175 C  CA  . ASP L  1 125 ? 66.040 -10.725 -92.431  1.00 44.96 ? 125  ASP M CA  1 
ATOM   13176 C  C   . ASP L  1 125 ? 64.640 -10.299 -92.910  1.00 45.14 ? 125  ASP M C   1 
ATOM   13177 O  O   . ASP L  1 125 ? 64.269 -10.527 -94.068  1.00 45.13 ? 125  ASP M O   1 
ATOM   13178 C  CB  . ASP L  1 125 ? 66.342 -12.206 -92.758  1.00 44.81 ? 125  ASP M CB  1 
ATOM   13179 C  CG  . ASP L  1 125 ? 65.429 -13.186 -92.030  1.00 44.64 ? 125  ASP M CG  1 
ATOM   13180 O  OD1 . ASP L  1 125 ? 65.817 -14.366 -91.902  1.00 44.02 ? 125  ASP M OD1 1 
ATOM   13181 O  OD2 . ASP L  1 125 ? 64.328 -12.799 -91.588  1.00 45.75 ? 125  ASP M OD2 1 
ATOM   13182 N  N   . LEU L  1 126 ? 63.887 -9.676  -92.003  1.00 45.21 ? 126  LEU M N   1 
ATOM   13183 C  CA  . LEU L  1 126 ? 62.516 -9.216  -92.237  1.00 45.46 ? 126  LEU M CA  1 
ATOM   13184 C  C   . LEU L  1 126 ? 61.533 -10.368 -92.481  1.00 45.65 ? 126  LEU M C   1 
ATOM   13185 O  O   . LEU L  1 126 ? 60.493 -10.179 -93.109  1.00 45.67 ? 126  LEU M O   1 
ATOM   13186 C  CB  . LEU L  1 126 ? 62.451 -8.156  -93.357  1.00 45.42 ? 126  LEU M CB  1 
ATOM   13187 C  CG  . LEU L  1 126 ? 63.437 -6.975  -93.353  1.00 45.43 ? 126  LEU M CG  1 
ATOM   13188 C  CD1 . LEU L  1 126 ? 63.178 -6.058  -94.538  1.00 45.64 ? 126  LEU M CD1 1 
ATOM   13189 C  CD2 . LEU L  1 126 ? 63.404 -6.175  -92.048  1.00 46.28 ? 126  LEU M CD2 1 
ATOM   13190 N  N   . GLY L  1 127 ? 61.869 -11.554 -91.970  1.00 46.09 ? 127  GLY M N   1 
ATOM   13191 C  CA  . GLY L  1 127 ? 61.007 -12.737 -92.073  1.00 46.92 ? 127  GLY M CA  1 
ATOM   13192 C  C   . GLY L  1 127 ? 61.088 -13.532 -93.375  1.00 47.69 ? 127  GLY M C   1 
ATOM   13193 O  O   . GLY L  1 127 ? 60.366 -14.522 -93.549  1.00 47.58 ? 127  GLY M O   1 
ATOM   13194 N  N   . LYS L  1 128 ? 61.972 -13.113 -94.279  1.00 48.36 ? 128  LYS M N   1 
ATOM   13195 C  CA  . LYS L  1 128 ? 62.039 -13.674 -95.638  1.00 49.18 ? 128  LYS M CA  1 
ATOM   13196 C  C   . LYS L  1 128 ? 62.914 -14.936 -95.785  1.00 49.78 ? 128  LYS M C   1 
ATOM   13197 O  O   . LYS L  1 128 ? 62.948 -15.550 -96.857  1.00 49.83 ? 128  LYS M O   1 
ATOM   13198 C  CB  . LYS L  1 128 ? 62.488 -12.587 -96.628  1.00 49.16 ? 128  LYS M CB  1 
ATOM   13199 C  CG  . LYS L  1 128 ? 61.476 -11.457 -96.844  1.00 49.31 ? 128  LYS M CG  1 
ATOM   13200 C  CD  . LYS L  1 128 ? 60.470 -11.803 -97.939  1.00 50.15 ? 128  LYS M CD  1 
ATOM   13201 C  CE  . LYS L  1 128 ? 59.320 -10.804 -97.989  1.00 50.28 ? 128  LYS M CE  1 
ATOM   13202 N  NZ  . LYS L  1 128 ? 58.332 -11.046 -96.897  1.00 50.02 ? 128  LYS M NZ  1 
ATOM   13203 N  N   . GLY L  1 129 ? 63.593 -15.331 -94.706  1.00 50.47 ? 129  GLY M N   1 
ATOM   13204 C  CA  . GLY L  1 129 ? 64.598 -16.408 -94.733  1.00 51.27 ? 129  GLY M CA  1 
ATOM   13205 C  C   . GLY L  1 129 ? 64.165 -17.840 -95.025  1.00 51.83 ? 129  GLY M C   1 
ATOM   13206 O  O   . GLY L  1 129 ? 64.996 -18.751 -95.015  1.00 51.94 ? 129  GLY M O   1 
ATOM   13207 N  N   . GLY L  1 130 ? 62.870 -18.045 -95.267  1.00 52.30 ? 130  GLY M N   1 
ATOM   13208 C  CA  . GLY L  1 130 ? 62.340 -19.332 -95.729  1.00 52.90 ? 130  GLY M CA  1 
ATOM   13209 C  C   . GLY L  1 130 ? 62.442 -20.540 -94.811  1.00 53.39 ? 130  GLY M C   1 
ATOM   13210 O  O   . GLY L  1 130 ? 62.542 -21.671 -95.290  1.00 53.42 ? 130  GLY M O   1 
ATOM   13211 N  N   . ASN L  1 131 ? 62.420 -20.311 -93.498  1.00 53.86 ? 131  ASN M N   1 
ATOM   13212 C  CA  . ASN L  1 131 ? 62.371 -21.402 -92.510  1.00 54.34 ? 131  ASN M CA  1 
ATOM   13213 C  C   . ASN L  1 131 ? 61.551 -21.024 -91.268  1.00 54.56 ? 131  ASN M C   1 
ATOM   13214 O  O   . ASN L  1 131 ? 61.154 -19.865 -91.117  1.00 54.64 ? 131  ASN M O   1 
ATOM   13215 C  CB  . ASN L  1 131 ? 63.781 -21.887 -92.127  1.00 54.40 ? 131  ASN M CB  1 
ATOM   13216 C  CG  . ASN L  1 131 ? 64.571 -20.854 -91.337  1.00 54.87 ? 131  ASN M CG  1 
ATOM   13217 O  OD1 . ASN L  1 131 ? 64.807 -21.022 -90.138  1.00 54.95 ? 131  ASN M OD1 1 
ATOM   13218 N  ND2 . ASN L  1 131 ? 64.988 -19.781 -92.007  1.00 55.39 ? 131  ASN M ND2 1 
ATOM   13219 N  N   . GLU L  1 132 ? 61.304 -21.997 -90.389  1.00 54.79 ? 132  GLU M N   1 
ATOM   13220 C  CA  . GLU L  1 132 ? 60.437 -21.801 -89.217  1.00 55.07 ? 132  GLU M CA  1 
ATOM   13221 C  C   . GLU L  1 132 ? 60.991 -20.809 -88.185  1.00 55.11 ? 132  GLU M C   1 
ATOM   13222 O  O   . GLU L  1 132 ? 60.225 -20.162 -87.468  1.00 55.17 ? 132  GLU M O   1 
ATOM   13223 C  CB  . GLU L  1 132 ? 60.098 -23.145 -88.558  1.00 55.14 ? 132  GLU M CB  1 
ATOM   13224 C  CG  . GLU L  1 132 ? 59.042 -23.053 -87.448  1.00 55.55 ? 132  GLU M CG  1 
ATOM   13225 C  CD  . GLU L  1 132 ? 58.159 -24.287 -87.353  1.00 56.08 ? 132  GLU M CD  1 
ATOM   13226 O  OE1 . GLU L  1 132 ? 57.604 -24.531 -86.259  1.00 55.98 ? 132  GLU M OE1 1 
ATOM   13227 O  OE2 . GLU L  1 132 ? 58.010 -25.009 -88.366  1.00 56.09 ? 132  GLU M OE2 1 
ATOM   13228 N  N   . GLU L  1 133 ? 62.316 -20.687 -88.128  1.00 55.12 ? 133  GLU M N   1 
ATOM   13229 C  CA  . GLU L  1 133 ? 62.980 -19.739 -87.232  1.00 55.04 ? 133  GLU M CA  1 
ATOM   13230 C  C   . GLU L  1 133 ? 62.963 -18.307 -87.789  1.00 54.80 ? 133  GLU M C   1 
ATOM   13231 O  O   . GLU L  1 133 ? 63.132 -17.340 -87.039  1.00 54.77 ? 133  GLU M O   1 
ATOM   13232 C  CB  . GLU L  1 133 ? 64.414 -20.209 -86.932  1.00 55.19 ? 133  GLU M CB  1 
ATOM   13233 C  CG  . GLU L  1 133 ? 65.127 -19.492 -85.775  1.00 55.68 ? 133  GLU M CG  1 
ATOM   13234 C  CD  . GLU L  1 133 ? 64.491 -19.726 -84.401  1.00 56.56 ? 133  GLU M CD  1 
ATOM   13235 O  OE1 . GLU L  1 133 ? 64.749 -18.912 -83.487  1.00 56.77 ? 133  GLU M OE1 1 
ATOM   13236 O  OE2 . GLU L  1 133 ? 63.743 -20.714 -84.224  1.00 56.75 ? 133  GLU M OE2 1 
ATOM   13237 N  N   . SER L  1 134 ? 62.748 -18.172 -89.096  1.00 54.44 ? 134  SER M N   1 
ATOM   13238 C  CA  . SER L  1 134 ? 62.683 -16.852 -89.723  1.00 54.16 ? 134  SER M CA  1 
ATOM   13239 C  C   . SER L  1 134 ? 61.305 -16.192 -89.618  1.00 53.91 ? 134  SER M C   1 
ATOM   13240 O  O   . SER L  1 134 ? 61.176 -14.990 -89.857  1.00 53.77 ? 134  SER M O   1 
ATOM   13241 C  CB  . SER L  1 134 ? 63.127 -16.908 -91.186  1.00 54.19 ? 134  SER M CB  1 
ATOM   13242 O  OG  . SER L  1 134 ? 63.354 -15.598 -91.682  1.00 53.98 ? 134  SER M OG  1 
ATOM   13243 N  N   . THR L  1 135 ? 60.286 -16.977 -89.273  1.00 53.65 ? 135  THR M N   1 
ATOM   13244 C  CA  . THR L  1 135 ? 58.936 -16.442 -89.045  1.00 53.50 ? 135  THR M CA  1 
ATOM   13245 C  C   . THR L  1 135 ? 58.595 -16.345 -87.555  1.00 53.26 ? 135  THR M C   1 
ATOM   13246 O  O   . THR L  1 135 ? 57.590 -15.737 -87.182  1.00 53.46 ? 135  THR M O   1 
ATOM   13247 C  CB  . THR L  1 135 ? 57.843 -17.264 -89.760  1.00 53.45 ? 135  THR M CB  1 
ATOM   13248 O  OG1 . THR L  1 135 ? 57.996 -18.651 -89.436  1.00 53.77 ? 135  THR M OG1 1 
ATOM   13249 C  CG2 . THR L  1 135 ? 57.903 -17.057 -91.271  1.00 53.13 ? 135  THR M CG2 1 
ATOM   13250 N  N   . LYS L  1 136 ? 59.433 -16.956 -86.717  1.00 52.89 ? 136  LYS M N   1 
ATOM   13251 C  CA  . LYS L  1 136 ? 59.308 -16.851 -85.265  1.00 52.40 ? 136  LYS M CA  1 
ATOM   13252 C  C   . LYS L  1 136 ? 60.215 -15.756 -84.704  1.00 52.04 ? 136  LYS M C   1 
ATOM   13253 O  O   . LYS L  1 136 ? 59.788 -14.969 -83.855  1.00 51.94 ? 136  LYS M O   1 
ATOM   13254 C  CB  . LYS L  1 136 ? 59.616 -18.190 -84.590  1.00 52.41 ? 136  LYS M CB  1 
ATOM   13255 C  CG  . LYS L  1 136 ? 58.522 -19.230 -84.744  1.00 52.61 ? 136  LYS M CG  1 
ATOM   13256 C  CD  . LYS L  1 136 ? 58.682 -20.344 -83.727  1.00 52.90 ? 136  LYS M CD  1 
ATOM   13257 C  CE  . LYS L  1 136 ? 57.606 -21.402 -83.907  1.00 52.92 ? 136  LYS M CE  1 
ATOM   13258 N  NZ  . LYS L  1 136 ? 57.580 -22.356 -82.767  1.00 52.71 ? 136  LYS M NZ  1 
ATOM   13259 N  N   . THR L  1 137 ? 61.456 -15.705 -85.189  1.00 51.53 ? 137  THR M N   1 
ATOM   13260 C  CA  . THR L  1 137 ? 62.458 -14.756 -84.687  1.00 50.96 ? 137  THR M CA  1 
ATOM   13261 C  C   . THR L  1 137 ? 63.095 -13.889 -85.778  1.00 50.56 ? 137  THR M C   1 
ATOM   13262 O  O   . THR L  1 137 ? 63.532 -12.769 -85.508  1.00 50.43 ? 137  THR M O   1 
ATOM   13263 C  CB  . THR L  1 137 ? 63.580 -15.468 -83.874  1.00 51.00 ? 137  THR M CB  1 
ATOM   13264 O  OG1 . THR L  1 137 ? 64.171 -16.512 -84.663  1.00 51.02 ? 137  THR M OG1 1 
ATOM   13265 C  CG2 . THR L  1 137 ? 63.026 -16.064 -82.581  1.00 50.91 ? 137  THR M CG2 1 
ATOM   13266 N  N   . GLY L  1 138 ? 63.158 -14.410 -87.003  1.00 50.14 ? 138  GLY M N   1 
ATOM   13267 C  CA  . GLY L  1 138 ? 63.745 -13.673 -88.128  1.00 49.49 ? 138  GLY M CA  1 
ATOM   13268 C  C   . GLY L  1 138 ? 65.266 -13.673 -88.189  1.00 49.13 ? 138  GLY M C   1 
ATOM   13269 O  O   . GLY L  1 138 ? 65.866 -12.857 -88.901  1.00 49.02 ? 138  GLY M O   1 
ATOM   13270 N  N   . ASN L  1 139 ? 65.887 -14.589 -87.444  1.00 48.64 ? 139  ASN M N   1 
ATOM   13271 C  CA  . ASN L  1 139 ? 67.349 -14.738 -87.400  1.00 48.33 ? 139  ASN M CA  1 
ATOM   13272 C  C   . ASN L  1 139 ? 68.113 -13.417 -87.193  1.00 48.05 ? 139  ASN M C   1 
ATOM   13273 O  O   . ASN L  1 139 ? 68.825 -12.942 -88.082  1.00 47.92 ? 139  ASN M O   1 
ATOM   13274 C  CB  . ASN L  1 139 ? 67.858 -15.494 -88.643  1.00 48.36 ? 139  ASN M CB  1 
ATOM   13275 C  CG  . ASN L  1 139 ? 67.134 -16.814 -88.861  1.00 48.23 ? 139  ASN M CG  1 
ATOM   13276 O  OD1 . ASN L  1 139 ? 67.365 -17.792 -88.148  1.00 48.13 ? 139  ASN M OD1 1 
ATOM   13277 N  ND2 . ASN L  1 139 ? 66.254 -16.845 -89.853  1.00 48.41 ? 139  ASN M ND2 1 
ATOM   13278 N  N   . ALA L  1 140 ? 67.945 -12.828 -86.011  1.00 47.72 ? 140  ALA M N   1 
ATOM   13279 C  CA  . ALA L  1 140 ? 68.663 -11.607 -85.639  1.00 47.24 ? 140  ALA M CA  1 
ATOM   13280 C  C   . ALA L  1 140 ? 69.736 -11.898 -84.584  1.00 46.94 ? 140  ALA M C   1 
ATOM   13281 O  O   . ALA L  1 140 ? 70.566 -11.039 -84.272  1.00 46.84 ? 140  ALA M O   1 
ATOM   13282 C  CB  . ALA L  1 140 ? 67.688 -10.535 -85.155  1.00 47.27 ? 140  ALA M CB  1 
ATOM   13283 N  N   . GLY L  1 141 ? 69.708 -13.115 -84.043  1.00 46.50 ? 141  GLY M N   1 
ATOM   13284 C  CA  . GLY L  1 141 ? 70.728 -13.579 -83.107  1.00 46.09 ? 141  GLY M CA  1 
ATOM   13285 C  C   . GLY L  1 141 ? 70.429 -13.275 -81.652  1.00 45.77 ? 141  GLY M C   1 
ATOM   13286 O  O   . GLY L  1 141 ? 69.266 -13.151 -81.253  1.00 45.78 ? 141  GLY M O   1 
ATOM   13287 N  N   . SER L  1 142 ? 71.490 -13.159 -80.857  1.00 45.29 ? 142  SER M N   1 
ATOM   13288 C  CA  . SER L  1 142 ? 71.366 -12.830 -79.435  1.00 44.66 ? 142  SER M CA  1 
ATOM   13289 C  C   . SER L  1 142 ? 71.141 -11.326 -79.210  1.00 44.17 ? 142  SER M C   1 
ATOM   13290 O  O   . SER L  1 142 ? 71.050 -10.547 -80.167  1.00 44.05 ? 142  SER M O   1 
ATOM   13291 C  CB  . SER L  1 142 ? 72.597 -13.321 -78.667  1.00 44.64 ? 142  SER M CB  1 
ATOM   13292 O  OG  . SER L  1 142 ? 73.733 -12.550 -79.006  1.00 44.83 ? 142  SER M OG  1 
ATOM   13293 N  N   . ARG L  1 143 ? 71.070 -10.924 -77.940  1.00 43.51 ? 143  ARG M N   1 
ATOM   13294 C  CA  . ARG L  1 143 ? 70.622 -9.577  -77.582  1.00 42.72 ? 143  ARG M CA  1 
ATOM   13295 C  C   . ARG L  1 143 ? 71.704 -8.743  -76.896  1.00 42.09 ? 143  ARG M C   1 
ATOM   13296 O  O   . ARG L  1 143 ? 72.118 -9.040  -75.778  1.00 42.15 ? 143  ARG M O   1 
ATOM   13297 C  CB  . ARG L  1 143 ? 69.342 -9.673  -76.738  1.00 42.82 ? 143  ARG M CB  1 
ATOM   13298 C  CG  . ARG L  1 143 ? 68.309 -10.611 -77.362  1.00 42.78 ? 143  ARG M CG  1 
ATOM   13299 C  CD  . ARG L  1 143 ? 67.130 -10.910 -76.473  1.00 42.85 ? 143  ARG M CD  1 
ATOM   13300 N  NE  . ARG L  1 143 ? 66.377 -12.063 -76.967  1.00 42.63 ? 143  ARG M NE  1 
ATOM   13301 C  CZ  . ARG L  1 143 ? 65.116 -12.337 -76.643  1.00 43.67 ? 143  ARG M CZ  1 
ATOM   13302 N  NH1 . ARG L  1 143 ? 64.518 -13.412 -77.148  1.00 42.86 ? 143  ARG M NH1 1 
ATOM   13303 N  NH2 . ARG L  1 143 ? 64.446 -11.536 -75.819  1.00 43.13 ? 143  ARG M NH2 1 
ATOM   13304 N  N   . LEU L  1 144 ? 72.145 -7.693  -77.587  1.00 41.52 ? 144  LEU M N   1 
ATOM   13305 C  CA  . LEU L  1 144 ? 73.276 -6.859  -77.149  1.00 40.89 ? 144  LEU M CA  1 
ATOM   13306 C  C   . LEU L  1 144 ? 72.921 -5.856  -76.039  1.00 40.35 ? 144  LEU M C   1 
ATOM   13307 O  O   . LEU L  1 144 ? 73.749 -5.562  -75.169  1.00 40.43 ? 144  LEU M O   1 
ATOM   13308 C  CB  . LEU L  1 144 ? 73.888 -6.114  -78.343  1.00 41.12 ? 144  LEU M CB  1 
ATOM   13309 C  CG  . LEU L  1 144 ? 74.511 -6.885  -79.521  1.00 40.88 ? 144  LEU M CG  1 
ATOM   13310 C  CD1 . LEU L  1 144 ? 74.880 -5.917  -80.644  1.00 40.39 ? 144  LEU M CD1 1 
ATOM   13311 C  CD2 . LEU L  1 144 ? 75.730 -7.702  -79.098  1.00 40.69 ? 144  LEU M CD2 1 
ATOM   13312 N  N   . ALA L  1 145 ? 71.701 -5.324  -76.091  1.00 39.21 ? 145  ALA M N   1 
ATOM   13313 C  CA  . ALA L  1 145 ? 71.183 -4.433  -75.059  1.00 38.26 ? 145  ALA M CA  1 
ATOM   13314 C  C   . ALA L  1 145 ? 69.655 -4.448  -75.072  1.00 37.65 ? 145  ALA M C   1 
ATOM   13315 O  O   . ALA L  1 145 ? 69.043 -4.401  -76.139  1.00 37.38 ? 145  ALA M O   1 
ATOM   13316 C  CB  . ALA L  1 145 ? 71.707 -3.013  -75.260  1.00 38.13 ? 145  ALA M CB  1 
ATOM   13317 N  N   . CYS L  1 146 ? 69.044 -4.533  -73.889  1.00 36.71 ? 146  CYS M N   1 
ATOM   13318 C  CA  . CYS L  1 146 ? 67.585 -4.419  -73.763  1.00 35.70 ? 146  CYS M CA  1 
ATOM   13319 C  C   . CYS L  1 146 ? 67.191 -3.534  -72.586  1.00 35.27 ? 146  CYS M C   1 
ATOM   13320 O  O   . CYS L  1 146 ? 68.047 -3.094  -71.813  1.00 34.84 ? 146  CYS M O   1 
ATOM   13321 C  CB  . CYS L  1 146 ? 66.917 -5.791  -73.649  0.40 35.71 ? 146  CYS M CB  1 
ATOM   13322 S  SG  . CYS L  1 146 ? 67.481 -6.813  -72.285  0.40 35.74 ? 146  CYS M SG  1 
ATOM   13323 N  N   . GLY L  1 147 ? 65.890 -3.266  -72.474  1.00 34.44 ? 147  GLY M N   1 
ATOM   13324 C  CA  . GLY L  1 147 ? 65.348 -2.455  -71.388  1.00 33.16 ? 147  GLY M CA  1 
ATOM   13325 C  C   . GLY L  1 147 ? 63.836 -2.405  -71.429  1.00 32.60 ? 147  GLY M C   1 
ATOM   13326 O  O   . GLY L  1 147 ? 63.218 -2.737  -72.454  1.00 32.65 ? 147  GLY M O   1 
ATOM   13327 N  N   . VAL L  1 148 ? 63.238 -1.984  -70.315  1.00 31.57 ? 148  VAL M N   1 
ATOM   13328 C  CA  . VAL L  1 148 ? 61.792 -1.812  -70.225  1.00 29.94 ? 148  VAL M CA  1 
ATOM   13329 C  C   . VAL L  1 148 ? 61.405 -0.443  -70.793  1.00 29.48 ? 148  VAL M C   1 
ATOM   13330 O  O   . VAL L  1 148 ? 62.045 0.562   -70.498  1.00 29.76 ? 148  VAL M O   1 
ATOM   13331 C  CB  . VAL L  1 148 ? 61.298 -1.941  -68.753  1.00 29.87 ? 148  VAL M CB  1 
ATOM   13332 C  CG1 . VAL L  1 148 ? 59.793 -2.197  -68.701  1.00 28.54 ? 148  VAL M CG1 1 
ATOM   13333 C  CG2 . VAL L  1 148 ? 62.032 -3.067  -68.037  1.00 29.53 ? 148  VAL M CG2 1 
ATOM   13334 N  N   . ILE L  1 149 ? 60.362 -0.406  -71.617  1.00 28.43 ? 149  ILE M N   1 
ATOM   13335 C  CA  . ILE L  1 149 ? 59.827 0.859   -72.093  1.00 27.38 ? 149  ILE M CA  1 
ATOM   13336 C  C   . ILE L  1 149 ? 58.963 1.424   -70.981  1.00 26.55 ? 149  ILE M C   1 
ATOM   13337 O  O   . ILE L  1 149 ? 58.020 0.767   -70.509  1.00 26.13 ? 149  ILE M O   1 
ATOM   13338 C  CB  . ILE L  1 149 ? 59.023 0.713   -73.405  1.00 27.53 ? 149  ILE M CB  1 
ATOM   13339 C  CG1 . ILE L  1 149 ? 59.925 0.136   -74.502  1.00 27.44 ? 149  ILE M CG1 1 
ATOM   13340 C  CG2 . ILE L  1 149 ? 58.470 2.067   -73.852  1.00 27.90 ? 149  ILE M CG2 1 
ATOM   13341 C  CD1 . ILE L  1 149 ? 59.200 -0.623  -75.580  1.00 26.57 ? 149  ILE M CD1 1 
ATOM   13342 N  N   . GLY L  1 150 ? 59.301 2.642   -70.571  1.00 25.37 ? 150  GLY M N   1 
ATOM   13343 C  CA  . GLY L  1 150 ? 58.623 3.296   -69.470  1.00 24.54 ? 150  GLY M CA  1 
ATOM   13344 C  C   . GLY L  1 150 ? 58.048 4.627   -69.886  1.00 23.80 ? 150  GLY M C   1 
ATOM   13345 O  O   . GLY L  1 150 ? 58.511 5.258   -70.844  1.00 22.94 ? 150  GLY M O   1 
ATOM   13346 N  N   . ILE L  1 151 ? 57.027 5.047   -69.155  1.00 22.87 ? 151  ILE M N   1 
ATOM   13347 C  CA  . ILE L  1 151 ? 56.385 6.338   -69.359  1.00 23.13 ? 151  ILE M CA  1 
ATOM   13348 C  C   . ILE L  1 151 ? 57.361 7.480   -69.063  1.00 23.22 ? 151  ILE M C   1 
ATOM   13349 O  O   . ILE L  1 151 ? 58.034 7.470   -68.022  1.00 22.83 ? 151  ILE M O   1 
ATOM   13350 C  CB  . ILE L  1 151 ? 55.150 6.455   -68.429  1.00 22.58 ? 151  ILE M CB  1 
ATOM   13351 C  CG1 . ILE L  1 151 ? 54.148 5.342   -68.744  1.00 21.97 ? 151  ILE M CG1 1 
ATOM   13352 C  CG2 . ILE L  1 151 ? 54.507 7.854   -68.508  1.00 23.38 ? 151  ILE M CG2 1 
ATOM   13353 C  CD1 . ILE L  1 151 ? 53.236 4.992   -67.553  1.00 20.41 ? 151  ILE M CD1 1 
ATOM   13354 N  N   . ALA L  1 152 ? 57.420 8.458   -69.972  1.00 23.75 ? 152  ALA M N   1 
ATOM   13355 C  CA  . ALA L  1 152 ? 58.256 9.653   -69.803  1.00 24.54 ? 152  ALA M CA  1 
ATOM   13356 C  C   . ALA L  1 152 ? 57.423 10.913  -69.649  1.00 25.29 ? 152  ALA M C   1 
ATOM   13357 O  O   . ALA L  1 152 ? 56.251 10.950  -70.040  1.00 25.50 ? 152  ALA M O   1 
ATOM   13358 C  CB  . ALA L  1 152 ? 59.227 9.806   -70.982  1.00 24.78 ? 152  ALA M CB  1 
ATOM   13359 N  N   . GLN L  1 153 ? 58.049 11.948  -69.094  1.00 25.91 ? 153  GLN M N   1 
ATOM   13360 C  CA  . GLN L  1 153 ? 57.421 13.241  -68.885  1.00 26.91 ? 153  GLN M CA  1 
ATOM   13361 C  C   . GLN L  1 153 ? 57.114 13.926  -70.210  1.00 27.67 ? 153  GLN M C   1 
ATOM   13362 O  O   . GLN L  1 153 ? 57.859 13.768  -71.177  1.00 27.71 ? 153  GLN M O   1 
ATOM   13363 C  CB  . GLN L  1 153 ? 58.336 14.132  -68.058  1.00 26.92 ? 153  GLN M CB  1 
ATOM   13364 C  CG  . GLN L  1 153 ? 57.729 15.463  -67.653  1.00 27.61 ? 153  GLN M CG  1 
ATOM   13365 C  CD  . GLN L  1 153 ? 58.562 16.194  -66.615  1.00 29.76 ? 153  GLN M CD  1 
ATOM   13366 O  OE1 . GLN L  1 153 ? 58.044 16.644  -65.593  1.00 30.60 ? 153  GLN M OE1 1 
ATOM   13367 N  NE2 . GLN L  1 153 ? 59.863 16.318  -66.874  1.00 30.42 ? 153  GLN M NE2 1 
ATOM   13368 O  OXT . GLN L  1 153 ? 56.129 14.657  -70.318  1.00 28.25 ? 153  GLN M OXT 1 
HETATM 13369 CU CU  . CU1 M  2 .   ? 14.511 23.445  -37.830  1.00 6.81  ? 200  CU1 A CU  1 
HETATM 13370 ZN ZN  . ZN  N  3 .   ? 20.643 21.835  -40.295  1.00 5.43  ? 300  ZN  A ZN  1 
HETATM 13371 S  S   . SO4 O  4 .   ? 11.771 23.807  -46.395  1.00 18.66 ? 400  SO4 A S   1 
HETATM 13372 O  O1  . SO4 O  4 .   ? 11.024 22.568  -46.539  1.00 20.29 ? 400  SO4 A O1  1 
HETATM 13373 O  O2  . SO4 O  4 .   ? 12.847 23.559  -45.475  1.00 17.13 ? 400  SO4 A O2  1 
HETATM 13374 O  O3  . SO4 O  4 .   ? 12.287 24.265  -47.689  1.00 17.88 ? 400  SO4 A O3  1 
HETATM 13375 O  O4  . SO4 O  4 .   ? 10.916 24.886  -45.885  1.00 20.32 ? 400  SO4 A O4  1 
HETATM 13376 CU CU  . CU1 P  2 .   ? 10.420 39.516  -10.647  1.00 6.52  ? 200  CU1 B CU  1 
HETATM 13377 ZN ZN  . ZN  Q  3 .   ? 15.540 41.008  -6.390   1.00 4.21  ? 300  ZN  B ZN  1 
HETATM 13378 S  S   . SO4 R  4 .   ? 5.123  38.953  -3.318   1.00 15.61 ? 400  SO4 B S   1 
HETATM 13379 O  O1  . SO4 R  4 .   ? 6.482  39.128  -3.796   1.00 13.80 ? 400  SO4 B O1  1 
HETATM 13380 O  O2  . SO4 R  4 .   ? 4.436  40.240  -3.326   1.00 16.17 ? 400  SO4 B O2  1 
HETATM 13381 O  O3  . SO4 R  4 .   ? 4.406  38.035  -4.217   1.00 15.38 ? 400  SO4 B O3  1 
HETATM 13382 O  O4  . SO4 R  4 .   ? 5.078  38.455  -1.955   1.00 14.89 ? 400  SO4 B O4  1 
HETATM 13383 CU CU  . CU1 S  2 .   ? 54.442 20.127  -25.351  1.00 6.74  ? 200  CU1 D CU  1 
HETATM 13384 ZN ZN  . ZN  T  3 .   ? 48.902 16.335  -25.645  1.00 5.53  ? 300  ZN  D ZN  1 
HETATM 13385 S  S   . SO4 U  4 .   ? 58.132 13.521  -20.343  1.00 23.79 ? 400  SO4 D S   1 
HETATM 13386 O  O1  . SO4 U  4 .   ? 58.981 12.829  -21.316  1.00 23.74 ? 400  SO4 D O1  1 
HETATM 13387 O  O2  . SO4 U  4 .   ? 57.030 14.153  -21.048  1.00 22.91 ? 400  SO4 D O2  1 
HETATM 13388 O  O3  . SO4 U  4 .   ? 57.652 12.569  -19.348  1.00 22.83 ? 400  SO4 D O3  1 
HETATM 13389 O  O4  . SO4 U  4 .   ? 58.874 14.569  -19.635  1.00 23.30 ? 400  SO4 D O4  1 
HETATM 13390 CU CU  . CU1 V  2 .   ? 53.175 52.053  -25.408  1.00 7.86  ? 200  CU1 E CU  1 
HETATM 13391 ZN ZN  . ZN  W  3 .   ? 47.437 55.470  -26.494  1.00 5.29  ? 300  ZN  E ZN  1 
HETATM 13392 S  S   . SO4 X  4 .   ? 57.410 58.874  -29.523  1.00 21.93 ? 400  SO4 E S   1 
HETATM 13393 O  O1  . SO4 X  4 .   ? 56.211 58.225  -29.024  1.00 20.27 ? 400  SO4 E O1  1 
HETATM 13394 O  O2  . SO4 X  4 .   ? 57.982 59.631  -28.415  1.00 18.76 ? 400  SO4 E O2  1 
HETATM 13395 O  O3  . SO4 X  4 .   ? 58.325 57.830  -29.979  1.00 19.84 ? 400  SO4 E O3  1 
HETATM 13396 O  O4  . SO4 X  4 .   ? 57.130 59.783  -30.637  1.00 20.71 ? 400  SO4 E O4  1 
HETATM 13397 CU CU  . CU1 Y  2 .   ? 12.221 -7.862  -34.905  1.00 14.81 ? 200  CU1 F CU  1 
HETATM 13398 ZN ZN  . ZN  Z  3 .   ? 17.363 -3.986  -32.594  1.00 11.47 ? 300  ZN  F ZN  1 
HETATM 13399 S  S   . SO4 AA 4 .   ? 6.842  -1.231  -32.146  1.00 32.88 ? 400  SO4 F S   1 
HETATM 13400 O  O1  . SO4 AA 4 .   ? 6.843  -0.104  -31.201  1.00 33.27 ? 400  SO4 F O1  1 
HETATM 13401 O  O2  . SO4 AA 4 .   ? 6.642  -0.711  -33.494  1.00 32.07 ? 400  SO4 F O2  1 
HETATM 13402 O  O3  . SO4 AA 4 .   ? 8.117  -1.921  -32.034  1.00 30.58 ? 400  SO4 F O3  1 
HETATM 13403 O  O4  . SO4 AA 4 .   ? 5.759  -2.144  -31.793  1.00 32.86 ? 400  SO4 F O4  1 
HETATM 13404 CU CU  . CU1 BA 2 .   ? 14.291 -39.883 -34.056  1.00 23.41 ? 200  CU1 G CU  1 
HETATM 13405 ZN ZN  . ZN  CA 3 .   ? 20.012 -43.002 -32.472  1.00 16.55 ? 300  ZN  G ZN  1 
HETATM 13406 S  S   . SO4 DA 4 .   ? 12.753 -46.846 -39.491  1.00 28.24 ? 400  SO4 G S   1 
HETATM 13407 O  O1  . SO4 DA 4 .   ? 13.510 -46.360 -38.347  1.00 26.89 ? 400  SO4 G O1  1 
HETATM 13408 O  O2  . SO4 DA 4 .   ? 11.636 -47.643 -38.985  1.00 27.72 ? 400  SO4 G O2  1 
HETATM 13409 O  O3  . SO4 DA 4 .   ? 12.213 -45.742 -40.266  1.00 28.54 ? 400  SO4 G O3  1 
HETATM 13410 O  O4  . SO4 DA 4 .   ? 13.651 -47.673 -40.300  1.00 28.66 ? 400  SO4 G O4  1 
HETATM 13411 CU CU  . CU1 EA 2 .   ? 54.051 -11.044 -27.830  1.00 18.55 ? 200  CU1 H CU  1 
HETATM 13412 ZN ZN  . ZN  FA 3 .   ? 49.859 -9.859  -33.024  1.00 11.82 ? 300  ZN  H ZN  1 
HETATM 13413 S  S   . SO4 GA 4 .   ? 60.489 -11.962 -34.173  1.00 25.54 ? 400  SO4 H S   1 
HETATM 13414 O  O1  . SO4 GA 4 .   ? 61.227 -10.706 -34.024  1.00 26.86 ? 400  SO4 H O1  1 
HETATM 13415 O  O2  . SO4 GA 4 .   ? 59.121 -11.753 -33.696  1.00 27.37 ? 400  SO4 H O2  1 
HETATM 13416 O  O3  . SO4 GA 4 .   ? 60.522 -12.335 -35.584  1.00 25.11 ? 400  SO4 H O3  1 
HETATM 13417 O  O4  . SO4 GA 4 .   ? 61.105 -12.995 -33.344  1.00 26.84 ? 400  SO4 H O4  1 
HETATM 13418 CU CU  . CU1 HA 2 .   ? 43.686 -25.197 -0.816   1.00 34.58 ? 200  CU1 I CU  1 
HETATM 13419 ZN ZN  . ZN  IA 3 .   ? 37.191 -26.480 0.281    1.00 27.34 ? 300  ZN  I ZN  1 
HETATM 13420 S  S   . SO4 JA 4 .   ? 44.668 -24.320 8.020    1.00 63.96 ? 400  SO4 I S   1 
HETATM 13421 O  O1  . SO4 JA 4 .   ? 43.945 -24.738 6.818    1.00 63.87 ? 400  SO4 I O1  1 
HETATM 13422 O  O2  . SO4 JA 4 .   ? 45.325 -25.477 8.626    1.00 64.14 ? 400  SO4 I O2  1 
HETATM 13423 O  O3  . SO4 JA 4 .   ? 45.685 -23.324 7.685    1.00 63.97 ? 400  SO4 I O3  1 
HETATM 13424 O  O4  . SO4 JA 4 .   ? 43.714 -23.752 8.965    1.00 63.74 ? 400  SO4 I O4  1 
HETATM 13425 CU CU  . CU1 KA 2 .   ? 19.394 4.237   -62.561  1.00 13.10 ? 200  CU1 J CU  1 
HETATM 13426 ZN ZN  . ZN  LA 3 .   ? 23.893 1.570   -58.317  1.00 9.27  ? 300  ZN  J ZN  1 
HETATM 13427 S  S   . SO4 MA 4 .   ? 13.839 -2.349  -59.817  1.00 33.96 ? 400  SO4 J S   1 
HETATM 13428 O  O1  . SO4 MA 4 .   ? 13.026 -1.535  -58.917  1.00 33.74 ? 400  SO4 J O1  1 
HETATM 13429 O  O2  . SO4 MA 4 .   ? 15.124 -1.707  -60.001  1.00 34.88 ? 400  SO4 J O2  1 
HETATM 13430 O  O3  . SO4 MA 4 .   ? 13.964 -3.685  -59.253  1.00 34.08 ? 400  SO4 J O3  1 
HETATM 13431 O  O4  . SO4 MA 4 .   ? 13.216 -2.470  -61.130  1.00 35.30 ? 400  SO4 J O4  1 
HETATM 13432 CU CU  . CU1 NA 2 .   ? 27.758 19.237  -89.441  1.00 33.04 ? 200  CU1 K CU  1 
HETATM 13433 ZN ZN  . ZN  OA 3 .   ? 34.047 20.416  -91.056  1.00 31.35 ? 300  ZN  K ZN  1 
HETATM 13434 S  S   . SO4 PA 4 .   ? 25.438 26.568  -94.158  1.00 70.15 ? 400  SO4 K S   1 
HETATM 13435 O  O1  . SO4 PA 4 .   ? 26.421 25.497  -94.046  1.00 69.94 ? 400  SO4 K O1  1 
HETATM 13436 O  O2  . SO4 PA 4 .   ? 24.770 26.458  -95.451  1.00 70.16 ? 400  SO4 K O2  1 
HETATM 13437 O  O3  . SO4 PA 4 .   ? 24.449 26.443  -93.093  1.00 70.16 ? 400  SO4 K O3  1 
HETATM 13438 O  O4  . SO4 PA 4 .   ? 26.096 27.866  -94.039  1.00 69.84 ? 400  SO4 K O4  1 
HETATM 13439 CU CU  . CU1 QA 2 .   ? 60.282 7.115   -53.426  1.00 11.11 ? 200  CU1 L CU  1 
HETATM 13440 ZN ZN  . ZN  RA 3 .   ? 54.404 9.727   -51.584  1.00 7.47  ? 300  ZN  L ZN  1 
HETATM 13441 S  S   . SO4 SA 4 .   ? 64.197 13.994  -48.857  1.00 35.94 ? 400  SO4 L S   1 
HETATM 13442 O  O1  . SO4 SA 4 .   ? 64.874 13.707  -47.590  1.00 36.49 ? 400  SO4 L O1  1 
HETATM 13443 O  O2  . SO4 SA 4 .   ? 63.191 12.963  -49.077  1.00 34.22 ? 400  SO4 L O2  1 
HETATM 13444 O  O3  . SO4 SA 4 .   ? 63.614 15.309  -48.727  1.00 35.36 ? 400  SO4 L O3  1 
HETATM 13445 O  O4  . SO4 SA 4 .   ? 65.113 14.006  -50.008  1.00 33.96 ? 400  SO4 L O4  1 
HETATM 13446 CU CU  . CU1 TA 2 .   ? 64.065 -8.804  -80.885  1.00 48.56 ? 200  CU1 M CU  1 
HETATM 13447 ZN ZN  . ZN  UA 3 .   ? 58.706 -10.418 -84.811  1.00 38.13 ? 300  ZN  M ZN  1 
HETATM 13448 S  S   . SO4 VA 4 .   ? 68.025 -16.293 -83.757  1.00 84.12 ? 400  SO4 M S   1 
HETATM 13449 O  O1  . SO4 VA 4 .   ? 66.989 -15.302 -84.030  1.00 84.21 ? 400  SO4 M O1  1 
HETATM 13450 O  O2  . SO4 VA 4 .   ? 69.034 -16.224 -84.811  1.00 84.15 ? 400  SO4 M O2  1 
HETATM 13451 O  O3  . SO4 VA 4 .   ? 68.653 -16.014 -82.468  1.00 83.94 ? 400  SO4 M O3  1 
HETATM 13452 O  O4  . SO4 VA 4 .   ? 67.424 -17.625 -83.721  1.00 83.96 ? 400  SO4 M O4  1 
HETATM 13453 O  O   . HOH WA 5 .   ? 1.376  23.874  -34.114  1.00 3.85  ? 154  HOH A O   1 
HETATM 13454 O  O   . HOH WA 5 .   ? 10.902 27.721  -23.317  1.00 2.00  ? 155  HOH A O   1 
HETATM 13455 O  O   . HOH WA 5 .   ? 0.899  25.212  -29.984  1.00 4.10  ? 156  HOH A O   1 
HETATM 13456 O  O   . HOH WA 5 .   ? 2.140  17.887  -37.429  1.00 5.26  ? 157  HOH A O   1 
HETATM 13457 O  O   . HOH WA 5 .   ? 30.506 23.865  -26.675  1.00 6.14  ? 158  HOH A O   1 
HETATM 13458 O  O   . HOH WA 5 .   ? -3.583 29.313  -32.204  1.00 11.03 ? 159  HOH A O   1 
HETATM 13459 O  O   . HOH WA 5 .   ? 22.533 11.907  -43.346  1.00 14.88 ? 160  HOH A O   1 
HETATM 13460 O  O   . HOH WA 5 .   ? 7.002  9.677   -41.550  1.00 11.94 ? 161  HOH A O   1 
HETATM 13461 O  O   . HOH WA 5 .   ? -1.733 14.583  -30.371  1.00 7.16  ? 162  HOH A O   1 
HETATM 13462 O  O   . HOH WA 5 .   ? 12.341 35.628  -28.009  1.00 5.10  ? 163  HOH A O   1 
HETATM 13463 O  O   . HOH WA 5 .   ? 0.112  19.270  -36.195  1.00 4.06  ? 164  HOH A O   1 
HETATM 13464 O  O   . HOH WA 5 .   ? 18.491 22.829  -55.731  1.00 12.51 ? 165  HOH A O   1 
HETATM 13465 O  O   . HOH WA 5 .   ? 22.317 12.681  -31.711  1.00 12.82 ? 166  HOH A O   1 
HETATM 13466 O  O   . HOH WA 5 .   ? 19.309 26.135  -41.830  1.00 5.41  ? 167  HOH A O   1 
HETATM 13467 O  O   . HOH WA 5 .   ? 2.429  26.734  -35.923  1.00 10.23 ? 168  HOH A O   1 
HETATM 13468 O  O   . HOH WA 5 .   ? 27.807 24.145  -37.054  1.00 8.02  ? 169  HOH A O   1 
HETATM 13469 O  O   . HOH WA 5 .   ? 12.420 23.948  -42.852  1.00 4.79  ? 170  HOH A O   1 
HETATM 13470 O  O   . HOH WA 5 .   ? 21.518 15.713  -51.130  1.00 3.88  ? 171  HOH A O   1 
HETATM 13471 O  O   . HOH WA 5 .   ? 19.105 17.061  -38.791  1.00 7.56  ? 172  HOH A O   1 
HETATM 13472 O  O   . HOH WA 5 .   ? 15.712 31.141  -41.367  1.00 9.29  ? 173  HOH A O   1 
HETATM 13473 O  O   . HOH WA 5 .   ? 20.531 10.944  -52.139  1.00 17.26 ? 174  HOH A O   1 
HETATM 13474 O  O   . HOH WA 5 .   ? 21.970 10.911  -38.772  1.00 10.76 ? 175  HOH A O   1 
HETATM 13475 O  O   . HOH WA 5 .   ? 16.817 12.285  -34.157  1.00 10.79 ? 176  HOH A O   1 
HETATM 13476 O  O   . HOH WA 5 .   ? 16.955 10.634  -45.484  1.00 16.73 ? 177  HOH A O   1 
HETATM 13477 O  O   . HOH WA 5 .   ? 26.213 12.828  -31.396  1.00 23.81 ? 178  HOH A O   1 
HETATM 13478 O  O   . HOH WA 5 .   ? 10.069 30.408  -25.467  1.00 5.60  ? 179  HOH A O   1 
HETATM 13479 O  O   . HOH WA 5 .   ? 20.139 9.833   -30.153  1.00 13.16 ? 180  HOH A O   1 
HETATM 13480 O  O   . HOH WA 5 .   ? 16.999 38.121  -33.957  1.00 13.57 ? 181  HOH A O   1 
HETATM 13481 O  O   . HOH WA 5 .   ? 11.031 15.839  -46.336  1.00 15.50 ? 182  HOH A O   1 
HETATM 13482 O  O   . HOH WA 5 .   ? 24.532 33.626  -33.159  1.00 19.29 ? 183  HOH A O   1 
HETATM 13483 O  O   . HOH WA 5 .   ? 14.740 20.256  -17.649  1.00 15.13 ? 184  HOH A O   1 
HETATM 13484 O  O   . HOH WA 5 .   ? 28.692 21.632  -37.000  1.00 7.22  ? 185  HOH A O   1 
HETATM 13485 O  O   . HOH WA 5 .   ? 16.338 26.912  -41.342  1.00 9.80  ? 187  HOH A O   1 
HETATM 13486 O  O   . HOH WA 5 .   ? 27.643 14.880  -20.302  1.00 9.17  ? 189  HOH A O   1 
HETATM 13487 O  O   . HOH WA 5 .   ? 14.734 11.056  -43.286  1.00 22.63 ? 206  HOH A O   1 
HETATM 13488 O  O   . HOH WA 5 .   ? 0.162  26.344  -27.421  1.00 9.90  ? 207  HOH A O   1 
HETATM 13489 O  O   . HOH WA 5 .   ? 29.526 13.667  -42.903  1.00 16.01 ? 208  HOH A O   1 
HETATM 13490 O  O   . HOH WA 5 .   ? 28.691 14.465  -35.696  1.00 18.00 ? 216  HOH A O   1 
HETATM 13491 O  O   . HOH WA 5 .   ? -2.071 15.174  -33.249  1.00 10.16 ? 232  HOH A O   1 
HETATM 13492 O  O   . HOH WA 5 .   ? 24.883 14.322  -48.027  1.00 16.07 ? 235  HOH A O   1 
HETATM 13493 O  O   . HOH WA 5 .   ? 30.789 21.981  -24.092  1.00 13.93 ? 247  HOH A O   1 
HETATM 13494 O  O   . HOH WA 5 .   ? 24.480 29.870  -36.581  1.00 8.78  ? 253  HOH A O   1 
HETATM 13495 O  O   . HOH WA 5 .   ? 7.779  16.631  -21.386  1.00 17.07 ? 254  HOH A O   1 
HETATM 13496 O  O   . HOH WA 5 .   ? 26.490 29.244  -28.270  1.00 14.22 ? 264  HOH A O   1 
HETATM 13497 O  O   . HOH WA 5 .   ? 3.336  23.949  -24.751  1.00 14.42 ? 280  HOH A O   1 
HETATM 13498 O  O   . HOH WA 5 .   ? 6.966  29.708  -28.417  1.00 15.80 ? 308  HOH A O   1 
HETATM 13499 O  O   . HOH WA 5 .   ? 17.796 10.052  -50.374  1.00 21.11 ? 309  HOH A O   1 
HETATM 13500 O  O   . HOH WA 5 .   ? 5.931  13.689  -41.620  1.00 19.48 ? 313  HOH A O   1 
HETATM 13501 O  O   . HOH WA 5 .   ? 16.378 23.566  -53.475  1.00 17.85 ? 327  HOH A O   1 
HETATM 13502 O  O   . HOH WA 5 .   ? 26.029 11.247  -27.707  1.00 21.34 ? 328  HOH A O   1 
HETATM 13503 O  O   . HOH WA 5 .   ? 7.231  13.848  -44.014  1.00 16.66 ? 331  HOH A O   1 
HETATM 13504 O  O   . HOH WA 5 .   ? 2.426  14.821  -24.350  1.00 19.91 ? 338  HOH A O   1 
HETATM 13505 O  O   . HOH WA 5 .   ? -3.138 18.114  -27.515  1.00 12.05 ? 341  HOH A O   1 
HETATM 13506 O  O   . HOH WA 5 .   ? 9.082  31.164  -27.744  1.00 22.29 ? 349  HOH A O   1 
HETATM 13507 O  O   . HOH WA 5 .   ? 16.377 17.486  -56.160  1.00 19.49 ? 352  HOH A O   1 
HETATM 13508 O  O   . HOH WA 5 .   ? 0.691  22.256  -36.356  1.00 8.29  ? 353  HOH A O   1 
HETATM 13509 O  O   . HOH WA 5 .   ? -2.636 20.634  -28.676  1.00 8.83  ? 359  HOH A O   1 
HETATM 13510 O  O   . HOH WA 5 .   ? 6.945  8.658   -30.107  1.00 22.37 ? 377  HOH A O   1 
HETATM 13511 O  O   . HOH WA 5 .   ? 28.388 21.951  -20.438  1.00 17.11 ? 392  HOH A O   1 
HETATM 13512 O  O   . HOH WA 5 .   ? -1.670 11.607  -38.348  1.00 13.62 ? 395  HOH A O   1 
HETATM 13513 O  O   . HOH WA 5 .   ? 17.698 10.881  -23.700  1.00 19.96 ? 397  HOH A O   1 
HETATM 13514 O  O   . HOH WA 5 .   ? 26.656 30.678  -35.266  1.00 20.21 ? 399  HOH A O   1 
HETATM 13515 O  O   . HOH WA 5 .   ? 21.348 23.688  -14.606  1.00 6.46  ? 401  HOH A O   1 
HETATM 13516 O  O   . HOH WA 5 .   ? 15.929 36.943  -36.310  1.00 12.14 ? 407  HOH A O   1 
HETATM 13517 O  O   . HOH WA 5 .   ? -2.447 27.141  -37.577  1.00 15.04 ? 409  HOH A O   1 
HETATM 13518 O  O   . HOH WA 5 .   ? -1.597 29.917  -30.607  1.00 17.09 ? 424  HOH A O   1 
HETATM 13519 O  O   . HOH WA 5 .   ? 14.668 24.710  -41.057  1.00 11.33 ? 448  HOH A O   1 
HETATM 13520 O  O   . HOH WA 5 .   ? 10.592 20.049  -17.318  1.00 11.37 ? 449  HOH A O   1 
HETATM 13521 O  O   . HOH WA 5 .   ? 1.560  4.271   -33.523  1.00 18.89 ? 453  HOH A O   1 
HETATM 13522 O  O   . HOH WA 5 .   ? 5.013  30.466  -34.836  1.00 27.24 ? 465  HOH A O   1 
HETATM 13523 O  O   . HOH WA 5 .   ? -6.245 9.834   -30.146  1.00 40.38 ? 473  HOH A O   1 
HETATM 13524 O  O   . HOH WA 5 .   ? 30.213 11.313  -41.009  1.00 25.39 ? 494  HOH A O   1 
HETATM 13525 O  O   . HOH WA 5 .   ? 22.311 33.897  -39.572  1.00 24.10 ? 496  HOH A O   1 
HETATM 13526 O  O   . HOH WA 5 .   ? 18.067 7.814   -26.379  1.00 34.99 ? 503  HOH A O   1 
HETATM 13527 O  O   . HOH WA 5 .   ? 10.588 40.331  -35.575  1.00 27.52 ? 533  HOH A O   1 
HETATM 13528 O  O   . HOH WA 5 .   ? 3.769  13.041  -40.912  1.00 24.08 ? 535  HOH A O   1 
HETATM 13529 O  O   . HOH WA 5 .   ? 13.177 32.165  -40.798  1.00 13.48 ? 549  HOH A O   1 
HETATM 13530 O  O   . HOH WA 5 .   ? 24.413 13.587  -19.850  1.00 28.51 ? 556  HOH A O   1 
HETATM 13531 O  O   . HOH WA 5 .   ? 14.594 21.488  -12.973  1.00 22.23 ? 562  HOH A O   1 
HETATM 13532 O  O   . HOH WA 5 .   ? 31.480 13.664  -25.961  1.00 32.23 ? 568  HOH A O   1 
HETATM 13533 O  O   . HOH WA 5 .   ? 22.851 10.618  -33.709  1.00 19.83 ? 569  HOH A O   1 
HETATM 13534 O  O   . HOH WA 5 .   ? 6.573  32.429  -37.530  1.00 25.58 ? 578  HOH A O   1 
HETATM 13535 O  O   . HOH WA 5 .   ? 23.584 6.453   -47.448  1.00 20.40 ? 580  HOH A O   1 
HETATM 13536 O  O   . HOH WA 5 .   ? 34.122 22.946  -39.566  1.00 31.85 ? 590  HOH A O   1 
HETATM 13537 O  O   . HOH WA 5 .   ? 13.883 41.045  -32.925  1.00 12.62 ? 596  HOH A O   1 
HETATM 13538 O  O   . HOH WA 5 .   ? 23.880 25.304  -44.384  1.00 13.68 ? 626  HOH A O   1 
HETATM 13539 O  O   . HOH WA 5 .   ? 22.931 13.876  -52.258  1.00 16.50 ? 629  HOH A O   1 
HETATM 13540 O  O   . HOH WA 5 .   ? 0.513  25.906  -37.747  1.00 17.94 ? 636  HOH A O   1 
HETATM 13541 O  O   . HOH WA 5 .   ? 15.635 28.872  -42.959  1.00 21.70 ? 644  HOH A O   1 
HETATM 13542 O  O   . HOH WA 5 .   ? 16.639 18.830  -17.247  1.00 23.95 ? 655  HOH A O   1 
HETATM 13543 O  O   . HOH WA 5 .   ? 28.312 17.722  -25.930  1.00 19.65 ? 669  HOH A O   1 
HETATM 13544 O  O   . HOH WA 5 .   ? 2.840  17.527  -23.992  1.00 29.03 ? 722  HOH A O   1 
HETATM 13545 O  O   . HOH WA 5 .   ? 11.117 30.484  -41.804  1.00 20.18 ? 733  HOH A O   1 
HETATM 13546 O  O   . HOH WA 5 .   ? -2.004 13.877  -26.155  1.00 10.86 ? 734  HOH A O   1 
HETATM 13547 O  O   . HOH WA 5 .   ? 0.090  13.293  -24.661  1.00 18.12 ? 744  HOH A O   1 
HETATM 13548 O  O   . HOH WA 5 .   ? 5.430  32.120  -30.893  1.00 32.34 ? 753  HOH A O   1 
HETATM 13549 O  O   . HOH WA 5 .   ? 2.783  17.834  -40.163  1.00 18.33 ? 758  HOH A O   1 
HETATM 13550 O  O   . HOH WA 5 .   ? -2.494 9.189   -38.754  1.00 20.32 ? 760  HOH A O   1 
HETATM 13551 O  O   . HOH WA 5 .   ? 11.363 36.960  -38.986  1.00 12.68 ? 764  HOH A O   1 
HETATM 13552 O  O   . HOH WA 5 .   ? 25.893 27.067  -19.252  1.00 16.86 ? 769  HOH A O   1 
HETATM 13553 O  O   . HOH WA 5 .   ? 22.596 28.036  -40.680  1.00 24.97 ? 771  HOH A O   1 
HETATM 13554 O  O   . HOH WA 5 .   ? 0.515  8.206   -27.400  1.00 24.90 ? 772  HOH A O   1 
HETATM 13555 O  O   . HOH WA 5 .   ? 11.383 21.916  -49.226  1.00 15.64 ? 779  HOH A O   1 
HETATM 13556 O  O   . HOH WA 5 .   ? 5.112  7.680   -28.844  1.00 30.59 ? 780  HOH A O   1 
HETATM 13557 O  O   . HOH WA 5 .   ? 7.338  28.588  -25.517  1.00 22.39 ? 789  HOH A O   1 
HETATM 13558 O  O   . HOH WA 5 .   ? 0.786  11.182  -40.875  1.00 18.25 ? 791  HOH A O   1 
HETATM 13559 O  O   . HOH WA 5 .   ? 34.520 18.750  -18.983  1.00 20.33 ? 793  HOH A O   1 
HETATM 13560 O  O   . HOH WA 5 .   ? 13.781 20.802  -15.105  1.00 20.44 ? 803  HOH A O   1 
HETATM 13561 O  O   . HOH WA 5 .   ? 3.622  22.334  -22.747  1.00 26.63 ? 821  HOH A O   1 
HETATM 13562 O  O   . HOH WA 5 .   ? 29.686 28.883  -21.888  1.00 22.27 ? 823  HOH A O   1 
HETATM 13563 O  O   . HOH WA 5 .   ? 32.524 13.360  -20.049  1.00 25.89 ? 834  HOH A O   1 
HETATM 13564 O  O   . HOH WA 5 .   ? 24.280 12.632  -50.247  1.00 18.34 ? 853  HOH A O   1 
HETATM 13565 O  O   . HOH WA 5 .   ? -0.399 31.816  -32.883  1.00 30.34 ? 867  HOH A O   1 
HETATM 13566 O  O   . HOH WA 5 .   ? 27.847 20.052  -17.689  1.00 27.57 ? 872  HOH A O   1 
HETATM 13567 O  O   . HOH WA 5 .   ? 31.138 16.163  -26.765  1.00 28.17 ? 874  HOH A O   1 
HETATM 13568 O  O   . HOH WA 5 .   ? 12.353 26.642  -42.081  1.00 25.40 ? 893  HOH A O   1 
HETATM 13569 O  O   . HOH WA 5 .   ? 7.915  11.419  -43.784  1.00 28.93 ? 917  HOH A O   1 
HETATM 13570 O  O   . HOH WA 5 .   ? 4.767  6.260   -36.016  1.00 25.10 ? 931  HOH A O   1 
HETATM 13571 O  O   . HOH WA 5 .   ? 15.416 10.501  -47.920  1.00 23.00 ? 945  HOH A O   1 
HETATM 13572 O  O   . HOH WA 5 .   ? 27.030 12.241  -50.998  1.00 19.56 ? 954  HOH A O   1 
HETATM 13573 O  O   . HOH WA 5 .   ? 24.545 30.734  -39.109  1.00 24.44 ? 958  HOH A O   1 
HETATM 13574 O  O   . HOH WA 5 .   ? 18.295 26.730  -50.884  1.00 21.05 ? 986  HOH A O   1 
HETATM 13575 O  O   . HOH WA 5 .   ? 2.733  30.629  -30.045  1.00 39.62 ? 988  HOH A O   1 
HETATM 13576 O  O   . HOH WA 5 .   ? 4.715  17.985  -22.519  1.00 34.38 ? 992  HOH A O   1 
HETATM 13577 O  O   . HOH WA 5 .   ? 19.252 9.126   -23.707  1.00 31.59 ? 995  HOH A O   1 
HETATM 13578 O  O   . HOH WA 5 .   ? 36.449 13.247  -19.076  1.00 29.46 ? 1002 HOH A O   1 
HETATM 13579 O  O   . HOH WA 5 .   ? 25.777 16.040  -44.420  1.00 18.00 ? 1014 HOH A O   1 
HETATM 13580 O  O   . HOH WA 5 .   ? 29.068 25.275  -45.717  1.00 29.03 ? 1020 HOH A O   1 
HETATM 13581 O  O   . HOH WA 5 .   ? 11.803 38.792  -37.279  1.00 29.77 ? 1027 HOH A O   1 
HETATM 13582 O  O   . HOH WA 5 .   ? 8.138  25.565  -45.358  1.00 26.53 ? 1035 HOH A O   1 
HETATM 13583 O  O   . HOH WA 5 .   ? 17.152 33.734  -41.930  1.00 30.50 ? 1039 HOH A O   1 
HETATM 13584 O  O   . HOH WA 5 .   ? 31.509 19.439  -33.484  1.00 19.23 ? 1045 HOH A O   1 
HETATM 13585 O  O   . HOH WA 5 .   ? 16.810 26.226  -53.068  1.00 30.56 ? 1054 HOH A O   1 
HETATM 13586 O  O   . HOH WA 5 .   ? 0.545  10.864  -24.173  1.00 28.00 ? 1057 HOH A O   1 
HETATM 13587 O  O   . HOH WA 5 .   ? 2.413  24.509  -41.979  1.00 24.95 ? 1074 HOH A O   1 
HETATM 13588 O  O   . HOH WA 5 .   ? 8.992  29.612  -23.234  1.00 19.90 ? 1077 HOH A O   1 
HETATM 13589 O  O   . HOH WA 5 .   ? -1.403 9.525   -26.390  1.00 22.00 ? 1079 HOH A O   1 
HETATM 13590 O  O   . HOH WA 5 .   ? 20.390 24.766  -10.190  1.00 35.44 ? 1101 HOH A O   1 
HETATM 13591 O  O   . HOH WA 5 .   ? 14.279 38.909  -35.414  1.00 27.96 ? 1105 HOH A O   1 
HETATM 13592 O  O   . HOH WA 5 .   ? 8.333  22.916  -47.770  1.00 21.40 ? 1109 HOH A O   1 
HETATM 13593 O  O   . HOH WA 5 .   ? 21.475 21.643  -12.630  1.00 28.60 ? 1122 HOH A O   1 
HETATM 13594 O  O   . HOH WA 5 .   ? 31.930 14.637  -43.755  1.00 25.74 ? 1131 HOH A O   1 
HETATM 13595 O  O   . HOH WA 5 .   ? 18.782 8.743   -44.210  1.00 45.75 ? 1149 HOH A O   1 
HETATM 13596 O  O   . HOH WA 5 .   ? 24.274 28.204  -42.366  1.00 25.06 ? 1155 HOH A O   1 
HETATM 13597 O  O   . HOH WA 5 .   ? 6.087  23.991  -46.217  1.00 24.42 ? 1162 HOH A O   1 
HETATM 13598 O  O   . HOH WA 5 .   ? 32.044 19.466  -16.868  1.00 22.93 ? 1168 HOH A O   1 
HETATM 13599 O  O   . HOH WA 5 .   ? 34.392 31.328  -27.339  1.00 29.65 ? 1175 HOH A O   1 
HETATM 13600 O  O   . HOH WA 5 .   ? 8.096  19.103  -17.142  1.00 21.71 ? 1178 HOH A O   1 
HETATM 13601 O  O   . HOH WA 5 .   ? 9.164  16.377  -19.152  1.00 22.31 ? 1179 HOH A O   1 
HETATM 13602 O  O   . HOH WA 5 .   ? 16.602 28.002  -47.073  1.00 19.51 ? 1192 HOH A O   1 
HETATM 13603 O  O   . HOH WA 5 .   ? 11.612 13.268  -16.994  1.00 36.25 ? 1200 HOH A O   1 
HETATM 13604 O  O   . HOH WA 5 .   ? 31.190 22.516  -45.477  1.00 25.71 ? 1227 HOH A O   1 
HETATM 13605 O  O   . HOH WA 5 .   ? -3.187 11.325  -27.068  1.00 30.68 ? 1261 HOH A O   1 
HETATM 13606 O  O   . HOH WA 5 .   ? 13.966 27.549  -7.005   1.00 36.34 ? 1266 HOH A O   1 
HETATM 13607 O  O   . HOH WA 5 .   ? 30.719 18.730  -25.743  1.00 25.28 ? 1267 HOH A O   1 
HETATM 13608 O  O   . HOH WA 5 .   ? 27.709 31.487  -32.793  1.00 28.16 ? 1281 HOH A O   1 
HETATM 13609 O  O   . HOH WA 5 .   ? 16.061 35.342  -44.045  1.00 31.97 ? 1292 HOH A O   1 
HETATM 13610 O  O   . HOH WA 5 .   ? 31.034 21.202  -27.222  1.00 30.32 ? 1297 HOH A O   1 
HETATM 13611 O  O   . HOH WA 5 .   ? 27.803 16.609  -13.148  1.00 21.71 ? 1308 HOH A O   1 
HETATM 13612 O  O   . HOH WA 5 .   ? 13.417 36.434  -40.121  1.00 26.70 ? 1314 HOH A O   1 
HETATM 13613 O  O   . HOH WA 5 .   ? 25.944 33.717  -31.031  1.00 34.53 ? 1315 HOH A O   1 
HETATM 13614 O  O   . HOH WA 5 .   ? 16.084 32.962  -45.255  1.00 36.11 ? 1334 HOH A O   1 
HETATM 13615 O  O   . HOH WA 5 .   ? 11.601 15.919  -48.985  1.00 20.34 ? 1363 HOH A O   1 
HETATM 13616 O  O   . HOH WA 5 .   ? 34.240 22.822  -32.330  1.00 35.08 ? 1368 HOH A O   1 
HETATM 13617 O  O   . HOH WA 5 .   ? 21.924 30.685  -47.148  1.00 35.76 ? 1370 HOH A O   1 
HETATM 13618 O  O   . HOH WA 5 .   ? 27.132 30.379  -39.958  1.00 27.77 ? 1380 HOH A O   1 
HETATM 13619 O  O   . HOH WA 5 .   ? 2.682  19.916  -23.044  1.00 38.23 ? 1387 HOH A O   1 
HETATM 13620 O  O   . HOH WA 5 .   ? 0.595  2.195   -35.244  1.00 33.86 ? 1402 HOH A O   1 
HETATM 13621 O  O   . HOH WA 5 .   ? 7.424  28.309  -40.874  1.00 14.98 ? 1409 HOH A O   1 
HETATM 13622 O  O   . HOH WA 5 .   ? 30.055 19.476  -35.744  1.00 22.42 ? 1411 HOH A O   1 
HETATM 13623 O  O   . HOH WA 5 .   ? 33.061 12.368  -22.681  1.00 28.50 ? 1434 HOH A O   1 
HETATM 13624 O  O   . HOH WA 5 .   ? 0.513  17.350  -21.884  1.00 31.93 ? 1436 HOH A O   1 
HETATM 13625 O  O   . HOH WA 5 .   ? -4.635 11.836  -30.109  1.00 25.75 ? 1448 HOH A O   1 
HETATM 13626 O  O   . HOH WA 5 .   ? 31.273 14.795  -11.611  1.00 41.08 ? 1454 HOH A O   1 
HETATM 13627 O  O   . HOH WA 5 .   ? 0.882  25.164  -24.935  1.00 29.13 ? 1457 HOH A O   1 
HETATM 13628 O  O   . HOH WA 5 .   ? 27.825 9.920   -41.970  1.00 33.80 ? 1464 HOH A O   1 
HETATM 13629 O  O   . HOH WA 5 .   ? 24.467 22.459  -11.394  1.00 36.12 ? 1471 HOH A O   1 
HETATM 13630 O  O   . HOH WA 5 .   ? -2.864 23.850  -23.282  1.00 33.40 ? 1501 HOH A O   1 
HETATM 13631 O  O   . HOH WA 5 .   ? 24.152 16.657  -48.320  1.00 21.38 ? 1510 HOH A O   1 
HETATM 13632 O  O   . HOH WA 5 .   ? 34.411 13.739  -41.289  1.00 32.45 ? 1512 HOH A O   1 
HETATM 13633 O  O   . HOH WA 5 .   ? -0.648 5.624   -30.413  1.00 21.49 ? 1543 HOH A O   1 
HETATM 13634 O  O   . HOH WA 5 .   ? 16.006 35.421  -38.535  1.00 28.99 ? 1557 HOH A O   1 
HETATM 13635 O  O   . HOH WA 5 .   ? 5.161  35.899  -30.445  1.00 31.63 ? 1564 HOH A O   1 
HETATM 13636 O  O   . HOH WA 5 .   ? 29.171 29.878  -31.137  1.00 31.30 ? 1571 HOH A O   1 
HETATM 13637 O  O   . HOH WA 5 .   ? 30.810 10.542  -23.957  1.00 27.89 ? 1573 HOH A O   1 
HETATM 13638 O  O   . HOH WA 5 .   ? 10.883 26.068  -49.248  1.00 41.84 ? 1579 HOH A O   1 
HETATM 13639 O  O   . HOH WA 5 .   ? 2.255  19.409  -19.949  1.00 33.65 ? 1581 HOH A O   1 
HETATM 13640 O  O   . HOH WA 5 .   ? 19.029 29.195  -50.878  1.00 24.27 ? 1582 HOH A O   1 
HETATM 13641 O  O   . HOH WA 5 .   ? 25.363 17.787  -46.131  1.00 27.56 ? 1584 HOH A O   1 
HETATM 13642 O  O   . HOH WA 5 .   ? 19.399 30.425  -53.132  1.00 32.84 ? 1629 HOH A O   1 
HETATM 13643 O  O   . HOH WA 5 .   ? 31.146 30.479  -32.716  1.00 27.92 ? 1640 HOH A O   1 
HETATM 13644 O  O   . HOH WA 5 .   ? 18.295 30.281  -48.033  1.00 36.07 ? 1653 HOH A O   1 
HETATM 13645 O  O   . HOH WA 5 .   ? -1.213 16.342  -18.355  1.00 67.44 ? 1654 HOH A O   1 
HETATM 13646 O  O   . HOH WA 5 .   ? -3.610 15.052  -20.947  1.00 70.82 ? 1655 HOH A O   1 
HETATM 13647 O  O   . HOH WA 5 .   ? 30.146 31.855  -29.461  1.00 30.64 ? 1656 HOH A O   1 
HETATM 13648 O  O   . HOH WA 5 .   ? 11.166 10.409  -23.654  1.00 24.86 ? 1664 HOH A O   1 
HETATM 13649 O  O   . HOH WA 5 .   ? 8.285  30.026  -39.848  1.00 29.01 ? 1675 HOH A O   1 
HETATM 13650 O  O   . HOH WA 5 .   ? 29.908 17.063  -36.316  1.00 26.32 ? 1676 HOH A O   1 
HETATM 13651 O  O   . HOH WA 5 .   ? -3.403 11.638  -34.385  1.00 39.00 ? 1694 HOH A O   1 
HETATM 13652 O  O   . HOH WA 5 .   ? 26.558 25.587  -17.172  1.00 34.29 ? 1703 HOH A O   1 
HETATM 13653 O  O   . HOH WA 5 .   ? 28.496 30.604  -24.117  1.00 37.95 ? 1711 HOH A O   1 
HETATM 13654 O  O   . HOH WA 5 .   ? 5.659  10.782  -24.741  1.00 25.31 ? 1716 HOH A O   1 
HETATM 13655 O  O   . HOH WA 5 .   ? 6.841  33.377  -26.658  1.00 18.55 ? 1720 HOH A O   1 
HETATM 13656 O  O   . HOH WA 5 .   ? 12.382 10.807  -44.524  1.00 19.86 ? 1728 HOH A O   1 
HETATM 13657 O  O   . HOH WA 5 .   ? 9.909  10.208  -44.697  1.00 30.42 ? 1729 HOH A O   1 
HETATM 13658 O  O   . HOH WA 5 .   ? 8.688  14.428  -46.363  1.00 30.91 ? 1730 HOH A O   1 
HETATM 13659 O  O   . HOH WA 5 .   ? -0.002 14.036  -42.794  1.00 19.40 ? 1731 HOH A O   1 
HETATM 13660 O  O   . HOH WA 5 .   ? 26.666 6.738   -39.168  1.00 35.63 ? 1732 HOH A O   1 
HETATM 13661 O  O   . HOH WA 5 .   ? -1.434 19.266  -37.158  1.00 12.72 ? 1746 HOH A O   1 
HETATM 13662 O  O   . HOH XA 5 .   ? 24.008 38.763  -30.453  1.00 10.56 ? 154  HOH B O   1 
HETATM 13663 O  O   . HOH XA 5 .   ? 27.090 45.288  -17.717  1.00 4.27  ? 155  HOH B O   1 
HETATM 13664 O  O   . HOH XA 5 .   ? 11.170 27.171  -20.530  1.00 5.16  ? 156  HOH B O   1 
HETATM 13665 O  O   . HOH XA 5 .   ? 23.373 38.585  -7.255   1.00 3.38  ? 157  HOH B O   1 
HETATM 13666 O  O   . HOH XA 5 .   ? 11.257 35.125  -25.482  1.00 3.64  ? 158  HOH B O   1 
HETATM 13667 O  O   . HOH XA 5 .   ? 30.292 40.194  -19.992  1.00 6.37  ? 159  HOH B O   1 
HETATM 13668 O  O   . HOH XA 5 .   ? 13.449 36.696  -5.269   1.00 4.89  ? 160  HOH B O   1 
HETATM 13669 O  O   . HOH XA 5 .   ? 11.001 52.800  -9.017   1.00 10.16 ? 161  HOH B O   1 
HETATM 13670 O  O   . HOH XA 5 .   ? -1.492 44.952  -11.696  1.00 9.94  ? 162  HOH B O   1 
HETATM 13671 O  O   . HOH XA 5 .   ? 14.853 50.432  -13.884  1.00 7.02  ? 163  HOH B O   1 
HETATM 13672 O  O   . HOH XA 5 .   ? 14.557 45.940  -8.392   1.00 3.19  ? 164  HOH B O   1 
HETATM 13673 O  O   . HOH XA 5 .   ? 17.350 51.900  -7.480   1.00 7.25  ? 165  HOH B O   1 
HETATM 13674 O  O   . HOH XA 5 .   ? 24.334 39.181  -15.662  1.00 10.64 ? 166  HOH B O   1 
HETATM 13675 O  O   . HOH XA 5 .   ? 9.968  32.718  -23.902  1.00 10.63 ? 167  HOH B O   1 
HETATM 13676 O  O   . HOH XA 5 .   ? 23.781 50.099  -13.344  1.00 13.66 ? 168  HOH B O   1 
HETATM 13677 O  O   . HOH XA 5 .   ? 24.661 32.982  -15.984  1.00 9.12  ? 169  HOH B O   1 
HETATM 13678 O  O   . HOH XA 5 .   ? -1.380 45.256  -14.541  1.00 5.55  ? 170  HOH B O   1 
HETATM 13679 O  O   . HOH XA 5 .   ? 6.999  38.814  -6.465   1.00 5.04  ? 171  HOH B O   1 
HETATM 13680 O  O   . HOH XA 5 .   ? -1.347 38.985  -18.189  1.00 11.31 ? 172  HOH B O   1 
HETATM 13681 O  O   . HOH XA 5 .   ? 10.992 36.053  -6.714   1.00 5.09  ? 173  HOH B O   1 
HETATM 13682 O  O   . HOH XA 5 .   ? -2.764 48.541  -22.670  1.00 6.35  ? 174  HOH B O   1 
HETATM 13683 O  O   . HOH XA 5 .   ? 10.401 31.801  -6.763   1.00 11.70 ? 175  HOH B O   1 
HETATM 13684 O  O   . HOH XA 5 .   ? 28.171 48.060  -23.535  1.00 7.70  ? 176  HOH B O   1 
HETATM 13685 O  O   . HOH XA 5 .   ? -6.013 51.137  -22.878  1.00 9.07  ? 177  HOH B O   1 
HETATM 13686 O  O   . HOH XA 5 .   ? -3.229 43.645  -16.262  1.00 8.78  ? 178  HOH B O   1 
HETATM 13687 O  O   . HOH XA 5 .   ? 2.564  34.535  -9.932   1.00 15.42 ? 179  HOH B O   1 
HETATM 13688 O  O   . HOH XA 5 .   ? 28.314 40.776  -23.768  1.00 6.84  ? 180  HOH B O   1 
HETATM 13689 O  O   . HOH XA 5 .   ? 23.019 49.134  -1.078   1.00 17.20 ? 181  HOH B O   1 
HETATM 13690 O  O   . HOH XA 5 .   ? 11.761 51.977  -18.125  1.00 10.47 ? 182  HOH B O   1 
HETATM 13691 O  O   . HOH XA 5 .   ? 28.931 37.823  -16.602  1.00 11.02 ? 183  HOH B O   1 
HETATM 13692 O  O   . HOH XA 5 .   ? 7.352  39.405  4.531    1.00 6.68  ? 184  HOH B O   1 
HETATM 13693 O  O   . HOH XA 5 .   ? 33.491 43.270  -25.936  1.00 11.73 ? 185  HOH B O   1 
HETATM 13694 O  O   . HOH XA 5 .   ? 18.171 53.071  -16.262  1.00 9.00  ? 186  HOH B O   1 
HETATM 13695 O  O   . HOH XA 5 .   ? 24.460 41.065  -6.966   1.00 13.73 ? 187  HOH B O   1 
HETATM 13696 O  O   . HOH XA 5 .   ? 28.999 42.948  -25.845  1.00 15.47 ? 188  HOH B O   1 
HETATM 13697 O  O   . HOH XA 5 .   ? 19.810 50.126  -14.119  1.00 5.23  ? 189  HOH B O   1 
HETATM 13698 O  O   . HOH XA 5 .   ? 20.197 32.874  -8.797   1.00 6.23  ? 195  HOH B O   1 
HETATM 13699 O  O   . HOH XA 5 .   ? 16.594 42.746  -29.759  1.00 16.28 ? 197  HOH B O   1 
HETATM 13700 O  O   . HOH XA 5 .   ? 7.348  34.381  -24.478  1.00 21.02 ? 203  HOH B O   1 
HETATM 13701 O  O   . HOH XA 5 .   ? 12.733 51.562  -15.423  1.00 8.59  ? 205  HOH B O   1 
HETATM 13702 O  O   . HOH XA 5 .   ? 13.076 46.812  4.053    1.00 14.95 ? 211  HOH B O   1 
HETATM 13703 O  O   . HOH XA 5 .   ? 3.380  45.413  -26.608  1.00 23.51 ? 213  HOH B O   1 
HETATM 13704 O  O   . HOH XA 5 .   ? 33.204 34.993  -17.075  1.00 20.41 ? 230  HOH B O   1 
HETATM 13705 O  O   . HOH XA 5 .   ? 13.761 24.806  -13.521  1.00 11.27 ? 231  HOH B O   1 
HETATM 13706 O  O   . HOH XA 5 .   ? 17.300 37.834  -1.280   1.00 8.95  ? 241  HOH B O   1 
HETATM 13707 O  O   . HOH XA 5 .   ? 12.926 44.518  5.479    1.00 15.76 ? 242  HOH B O   1 
HETATM 13708 O  O   . HOH XA 5 .   ? 6.389  47.597  0.433    1.00 14.21 ? 251  HOH B O   1 
HETATM 13709 O  O   . HOH XA 5 .   ? 9.024  52.532  -17.773  1.00 11.45 ? 259  HOH B O   1 
HETATM 13710 O  O   . HOH XA 5 .   ? 9.699  53.396  -14.044  1.00 16.71 ? 265  HOH B O   1 
HETATM 13711 O  O   . HOH XA 5 .   ? 26.543 39.902  -13.596  1.00 16.88 ? 273  HOH B O   1 
HETATM 13712 O  O   . HOH XA 5 .   ? -0.661 49.962  -11.069  1.00 21.94 ? 276  HOH B O   1 
HETATM 13713 O  O   . HOH XA 5 .   ? 8.063  30.773  -8.106   1.00 13.91 ? 278  HOH B O   1 
HETATM 13714 O  O   . HOH XA 5 .   ? -0.347 58.767  -18.713  1.00 19.47 ? 282  HOH B O   1 
HETATM 13715 O  O   . HOH XA 5 .   ? 30.253 46.476  -30.277  1.00 20.18 ? 284  HOH B O   1 
HETATM 13716 O  O   . HOH XA 5 .   ? 2.205  53.048  -8.895   1.00 13.80 ? 286  HOH B O   1 
HETATM 13717 O  O   . HOH XA 5 .   ? -5.005 51.867  -15.270  1.00 23.19 ? 290  HOH B O   1 
HETATM 13718 O  O   . HOH XA 5 .   ? 18.321 34.517  -3.556   1.00 19.14 ? 294  HOH B O   1 
HETATM 13719 O  O   . HOH XA 5 .   ? 16.363 44.428  0.970    1.00 9.26  ? 299  HOH B O   1 
HETATM 13720 O  O   . HOH XA 5 .   ? 6.079  33.166  -21.745  1.00 20.22 ? 303  HOH B O   1 
HETATM 13721 O  O   . HOH XA 5 .   ? -6.890 53.860  -22.899  1.00 15.44 ? 319  HOH B O   1 
HETATM 13722 O  O   . HOH XA 5 .   ? 9.125  46.411  -28.101  1.00 20.86 ? 323  HOH B O   1 
HETATM 13723 O  O   . HOH XA 5 .   ? 21.222 29.400  -11.808  1.00 16.94 ? 325  HOH B O   1 
HETATM 13724 O  O   . HOH XA 5 .   ? 13.461 51.469  -11.870  1.00 14.96 ? 369  HOH B O   1 
HETATM 13725 O  O   . HOH XA 5 .   ? 9.484  38.158  -7.589   1.00 9.47  ? 370  HOH B O   1 
HETATM 13726 O  O   . HOH XA 5 .   ? 10.124 31.865  -18.833  1.00 18.55 ? 376  HOH B O   1 
HETATM 13727 O  O   . HOH XA 5 .   ? 6.106  29.584  -23.228  1.00 14.66 ? 380  HOH B O   1 
HETATM 13728 O  O   . HOH XA 5 .   ? 12.561 42.719  -31.316  1.00 14.43 ? 403  HOH B O   1 
HETATM 13729 O  O   . HOH XA 5 .   ? 1.361  49.665  -9.442   1.00 29.89 ? 410  HOH B O   1 
HETATM 13730 O  O   . HOH XA 5 .   ? -7.372 55.330  -20.602  1.00 20.49 ? 416  HOH B O   1 
HETATM 13731 O  O   . HOH XA 5 .   ? -0.481 37.918  -22.082  1.00 21.21 ? 421  HOH B O   1 
HETATM 13732 O  O   . HOH XA 5 .   ? 0.201  54.772  -24.645  1.00 15.93 ? 425  HOH B O   1 
HETATM 13733 O  O   . HOH XA 5 .   ? 7.268  56.559  -12.757  1.00 17.97 ? 429  HOH B O   1 
HETATM 13734 O  O   . HOH XA 5 .   ? 36.458 48.328  -25.974  1.00 11.98 ? 433  HOH B O   1 
HETATM 13735 O  O   . HOH XA 5 .   ? 29.909 48.942  -17.638  1.00 15.67 ? 441  HOH B O   1 
HETATM 13736 O  O   . HOH XA 5 .   ? 19.130 46.382  -0.866   1.00 12.53 ? 458  HOH B O   1 
HETATM 13737 O  O   . HOH XA 5 .   ? 24.399 51.454  -16.727  1.00 17.78 ? 472  HOH B O   1 
HETATM 13738 O  O   . HOH XA 5 .   ? 26.769 35.900  -24.976  1.00 15.17 ? 474  HOH B O   1 
HETATM 13739 O  O   . HOH XA 5 .   ? 3.803  27.533  -20.609  1.00 26.92 ? 478  HOH B O   1 
HETATM 13740 O  O   . HOH XA 5 .   ? 4.080  41.147  -0.701   1.00 20.88 ? 482  HOH B O   1 
HETATM 13741 O  O   . HOH XA 5 .   ? 18.743 44.078  -29.448  1.00 21.88 ? 483  HOH B O   1 
HETATM 13742 O  O   . HOH XA 5 .   ? 5.578  45.321  -27.731  1.00 37.78 ? 489  HOH B O   1 
HETATM 13743 O  O   . HOH XA 5 .   ? 9.849  34.206  -5.388   1.00 12.85 ? 493  HOH B O   1 
HETATM 13744 O  O   . HOH XA 5 .   ? 4.604  54.307  -25.141  1.00 32.46 ? 501  HOH B O   1 
HETATM 13745 O  O   . HOH XA 5 .   ? 8.217  39.453  7.231    1.00 4.31  ? 507  HOH B O   1 
HETATM 13746 O  O   . HOH XA 5 .   ? 5.777  32.300  -7.470   1.00 14.74 ? 517  HOH B O   1 
HETATM 13747 O  O   . HOH XA 5 .   ? 13.023 55.150  -18.822  1.00 27.95 ? 518  HOH B O   1 
HETATM 13748 O  O   . HOH XA 5 .   ? 10.934 46.295  -30.262  1.00 16.70 ? 530  HOH B O   1 
HETATM 13749 O  O   . HOH XA 5 .   ? 8.840  51.823  -5.390   1.00 21.99 ? 541  HOH B O   1 
HETATM 13750 O  O   . HOH XA 5 .   ? 4.160  46.871  -3.837   1.00 17.45 ? 544  HOH B O   1 
HETATM 13751 O  O   . HOH XA 5 .   ? 17.348 52.167  -23.043  1.00 28.86 ? 548  HOH B O   1 
HETATM 13752 O  O   . HOH XA 5 .   ? 9.500  35.994  2.990    1.00 30.01 ? 555  HOH B O   1 
HETATM 13753 O  O   . HOH XA 5 .   ? 8.748  31.081  -16.870  1.00 9.85  ? 561  HOH B O   1 
HETATM 13754 O  O   . HOH XA 5 .   ? 20.402 54.195  -15.679  1.00 19.17 ? 566  HOH B O   1 
HETATM 13755 O  O   . HOH XA 5 .   ? 27.606 39.604  -11.210  1.00 26.14 ? 597  HOH B O   1 
HETATM 13756 O  O   . HOH XA 5 .   ? -0.065 39.418  -4.995   1.00 15.43 ? 610  HOH B O   1 
HETATM 13757 O  O   . HOH XA 5 .   ? 2.027  48.924  -6.361   1.00 25.35 ? 612  HOH B O   1 
HETATM 13758 O  O   . HOH XA 5 .   ? 17.401 51.432  -13.944  1.00 9.69  ? 616  HOH B O   1 
HETATM 13759 O  O   . HOH XA 5 .   ? 8.550  31.700  -21.474  1.00 18.10 ? 630  HOH B O   1 
HETATM 13760 O  O   . HOH XA 5 .   ? 16.987 35.233  -5.286   1.00 19.01 ? 649  HOH B O   1 
HETATM 13761 O  O   . HOH XA 5 .   ? 8.887  36.821  7.497    1.00 10.16 ? 651  HOH B O   1 
HETATM 13762 O  O   . HOH XA 5 .   ? 25.364 32.414  -12.959  1.00 14.69 ? 656  HOH B O   1 
HETATM 13763 O  O   . HOH XA 5 .   ? -5.214 52.208  -17.658  1.00 29.70 ? 663  HOH B O   1 
HETATM 13764 O  O   . HOH XA 5 .   ? 22.525 31.873  -9.193   1.00 16.80 ? 694  HOH B O   1 
HETATM 13765 O  O   . HOH XA 5 .   ? 35.916 45.465  -23.946  1.00 13.12 ? 699  HOH B O   1 
HETATM 13766 O  O   . HOH XA 5 .   ? 12.146 25.953  -11.599  1.00 19.22 ? 701  HOH B O   1 
HETATM 13767 O  O   . HOH XA 5 .   ? 10.638 55.335  -20.667  1.00 25.83 ? 702  HOH B O   1 
HETATM 13768 O  O   . HOH XA 5 .   ? 2.208  32.192  -16.075  1.00 18.66 ? 711  HOH B O   1 
HETATM 13769 O  O   . HOH XA 5 .   ? 20.698 26.774  -12.266  1.00 30.40 ? 712  HOH B O   1 
HETATM 13770 O  O   . HOH XA 5 .   ? 3.646  32.375  -19.367  1.00 20.54 ? 717  HOH B O   1 
HETATM 13771 O  O   . HOH XA 5 .   ? 11.646 29.882  -5.475   1.00 23.16 ? 718  HOH B O   1 
HETATM 13772 O  O   . HOH XA 5 .   ? 25.259 48.898  -24.917  1.00 17.00 ? 723  HOH B O   1 
HETATM 13773 O  O   . HOH XA 5 .   ? 20.001 45.583  1.825    1.00 17.69 ? 729  HOH B O   1 
HETATM 13774 O  O   . HOH XA 5 .   ? 29.248 50.535  -24.083  1.00 14.80 ? 740  HOH B O   1 
HETATM 13775 O  O   . HOH XA 5 .   ? 22.166 37.922  1.389    1.00 25.01 ? 754  HOH B O   1 
HETATM 13776 O  O   . HOH XA 5 .   ? 10.549 44.060  -32.270  1.00 22.78 ? 776  HOH B O   1 
HETATM 13777 O  O   . HOH XA 5 .   ? 17.153 29.067  -6.335   1.00 24.82 ? 792  HOH B O   1 
HETATM 13778 O  O   . HOH XA 5 .   ? 7.163  22.466  -13.936  1.00 25.36 ? 820  HOH B O   1 
HETATM 13779 O  O   . HOH XA 5 .   ? -3.805 51.649  -11.946  1.00 28.63 ? 830  HOH B O   1 
HETATM 13780 O  O   . HOH XA 5 .   ? 17.343 48.218  -0.340   1.00 28.20 ? 832  HOH B O   1 
HETATM 13781 O  O   . HOH XA 5 .   ? 23.435 36.806  -38.540  1.00 29.64 ? 838  HOH B O   1 
HETATM 13782 O  O   . HOH XA 5 .   ? 15.557 53.117  -9.033   1.00 26.45 ? 842  HOH B O   1 
HETATM 13783 O  O   . HOH XA 5 .   ? 10.394 51.754  -1.062   1.00 22.99 ? 866  HOH B O   1 
HETATM 13784 O  O   . HOH XA 5 .   ? 11.370 21.758  -15.330  1.00 27.72 ? 869  HOH B O   1 
HETATM 13785 O  O   . HOH XA 5 .   ? 20.764 52.235  -12.019  1.00 23.19 ? 896  HOH B O   1 
HETATM 13786 O  O   . HOH XA 5 .   ? 25.554 45.746  -7.254   1.00 35.84 ? 903  HOH B O   1 
HETATM 13787 O  O   . HOH XA 5 .   ? 1.846  56.824  -15.425  1.00 20.18 ? 913  HOH B O   1 
HETATM 13788 O  O   . HOH XA 5 .   ? 24.290 48.407  -8.172   1.00 25.95 ? 924  HOH B O   1 
HETATM 13789 O  O   . HOH XA 5 .   ? 12.826 32.777  4.065    1.00 26.09 ? 935  HOH B O   1 
HETATM 13790 O  O   . HOH XA 5 .   ? 15.626 54.197  -16.857  1.00 21.54 ? 965  HOH B O   1 
HETATM 13791 O  O   . HOH XA 5 .   ? 3.585  31.862  -21.548  1.00 28.58 ? 967  HOH B O   1 
HETATM 13792 O  O   . HOH XA 5 .   ? 7.748  45.393  -31.963  1.00 35.42 ? 991  HOH B O   1 
HETATM 13793 O  O   . HOH XA 5 .   ? 13.634 54.546  -15.073  1.00 29.58 ? 994  HOH B O   1 
HETATM 13794 O  O   . HOH XA 5 .   ? 11.687 52.399  -25.319  1.00 23.19 ? 997  HOH B O   1 
HETATM 13795 O  O   . HOH XA 5 .   ? 19.245 31.978  -6.132   1.00 14.83 ? 1003 HOH B O   1 
HETATM 13796 O  O   . HOH XA 5 .   ? 28.742 45.489  -12.370  1.00 25.90 ? 1017 HOH B O   1 
HETATM 13797 O  O   . HOH XA 5 .   ? 17.589 53.254  -12.058  1.00 22.36 ? 1043 HOH B O   1 
HETATM 13798 O  O   . HOH XA 5 .   ? 4.548  54.835  -21.430  1.00 25.09 ? 1049 HOH B O   1 
HETATM 13799 O  O   . HOH XA 5 .   ? 2.190  37.220  -5.439   1.00 18.35 ? 1055 HOH B O   1 
HETATM 13800 O  O   . HOH XA 5 .   ? 6.573  54.395  -19.706  1.00 26.24 ? 1063 HOH B O   1 
HETATM 13801 O  O   . HOH XA 5 .   ? 17.980 41.321  -34.274  1.00 23.01 ? 1073 HOH B O   1 
HETATM 13802 O  O   . HOH XA 5 .   ? 13.762 51.657  -9.611   1.00 24.18 ? 1075 HOH B O   1 
HETATM 13803 O  O   . HOH XA 5 .   ? 9.542  34.739  -1.132   1.00 25.24 ? 1078 HOH B O   1 
HETATM 13804 O  O   . HOH XA 5 .   ? 3.008  47.893  -26.462  1.00 23.84 ? 1084 HOH B O   1 
HETATM 13805 O  O   . HOH XA 5 .   ? 2.504  30.603  -13.129  1.00 26.01 ? 1093 HOH B O   1 
HETATM 13806 O  O   . HOH XA 5 .   ? 7.732  43.303  -33.142  1.00 29.26 ? 1113 HOH B O   1 
HETATM 13807 O  O   . HOH XA 5 .   ? -3.196 41.349  -15.389  1.00 24.87 ? 1129 HOH B O   1 
HETATM 13808 O  O   . HOH XA 5 .   ? 21.518 32.880  -4.181   1.00 29.87 ? 1137 HOH B O   1 
HETATM 13809 O  O   . HOH XA 5 .   ? 25.421 36.897  -29.810  1.00 23.13 ? 1139 HOH B O   1 
HETATM 13810 O  O   . HOH XA 5 .   ? 23.424 36.687  -32.728  1.00 23.14 ? 1159 HOH B O   1 
HETATM 13811 O  O   . HOH XA 5 .   ? 16.974 52.169  -4.797   1.00 31.94 ? 1176 HOH B O   1 
HETATM 13812 O  O   . HOH XA 5 .   ? 20.274 37.200  -41.909  1.00 40.89 ? 1183 HOH B O   1 
HETATM 13813 O  O   . HOH XA 5 .   ? 6.669  36.320  4.626    1.00 35.60 ? 1190 HOH B O   1 
HETATM 13814 O  O   . HOH XA 5 .   ? 23.043 52.630  -14.910  1.00 26.22 ? 1194 HOH B O   1 
HETATM 13815 O  O   . HOH XA 5 .   ? 10.639 23.332  -12.329  1.00 37.83 ? 1196 HOH B O   1 
HETATM 13816 O  O   . HOH XA 5 .   ? 2.128  27.795  -11.675  1.00 31.57 ? 1206 HOH B O   1 
HETATM 13817 O  O   . HOH XA 5 .   ? 23.968 30.918  -11.188  1.00 34.19 ? 1216 HOH B O   1 
HETATM 13818 O  O   . HOH XA 5 .   ? 11.267 27.348  -9.400   1.00 29.03 ? 1217 HOH B O   1 
HETATM 13819 O  O   . HOH XA 5 .   ? 4.457  39.807  -26.936  1.00 20.62 ? 1225 HOH B O   1 
HETATM 13820 O  O   . HOH XA 5 .   ? 25.794 43.310  -7.711   1.00 34.13 ? 1230 HOH B O   1 
HETATM 13821 O  O   . HOH XA 5 .   ? 13.677 30.311  -3.957   1.00 26.86 ? 1246 HOH B O   1 
HETATM 13822 O  O   . HOH XA 5 .   ? -3.220 41.640  -4.453   1.00 33.93 ? 1247 HOH B O   1 
HETATM 13823 O  O   . HOH XA 5 .   ? 0.816  49.379  -27.347  1.00 37.42 ? 1248 HOH B O   1 
HETATM 13824 O  O   . HOH XA 5 .   ? -2.280 37.135  -14.461  1.00 31.84 ? 1249 HOH B O   1 
HETATM 13825 O  O   . HOH XA 5 .   ? 9.317  49.923  -28.091  1.00 26.31 ? 1259 HOH B O   1 
HETATM 13826 O  O   . HOH XA 5 .   ? 29.030 34.470  -24.819  1.00 34.18 ? 1271 HOH B O   1 
HETATM 13827 O  O   . HOH XA 5 .   ? 10.960 53.785  -11.705  1.00 40.29 ? 1280 HOH B O   1 
HETATM 13828 O  O   . HOH XA 5 .   ? 3.823  42.596  -27.880  1.00 36.43 ? 1294 HOH B O   1 
HETATM 13829 O  O   . HOH XA 5 .   ? 25.044 41.277  -32.101  1.00 38.93 ? 1311 HOH B O   1 
HETATM 13830 O  O   . HOH XA 5 .   ? 15.746 38.943  4.847    1.00 26.07 ? 1312 HOH B O   1 
HETATM 13831 O  O   . HOH XA 5 .   ? 32.740 37.796  -22.698  1.00 25.31 ? 1317 HOH B O   1 
HETATM 13832 O  O   . HOH XA 5 .   ? 16.450 50.784  -2.488   1.00 25.03 ? 1325 HOH B O   1 
HETATM 13833 O  O   . HOH XA 5 .   ? 25.220 35.640  1.222    1.00 35.17 ? 1327 HOH B O   1 
HETATM 13834 O  O   . HOH XA 5 .   ? 15.394 31.294  -2.839   1.00 36.83 ? 1331 HOH B O   1 
HETATM 13835 O  O   . HOH XA 5 .   ? 28.085 48.919  -11.712  1.00 31.87 ? 1338 HOH B O   1 
HETATM 13836 O  O   . HOH XA 5 .   ? 7.179  47.139  6.879    1.00 21.80 ? 1343 HOH B O   1 
HETATM 13837 O  O   . HOH XA 5 .   ? 13.364 35.085  -3.279   1.00 24.12 ? 1355 HOH B O   1 
HETATM 13838 O  O   . HOH XA 5 .   ? 8.800  56.819  -10.514  1.00 36.91 ? 1362 HOH B O   1 
HETATM 13839 O  O   . HOH XA 5 .   ? 5.853  36.393  1.524    1.00 21.78 ? 1372 HOH B O   1 
HETATM 13840 O  O   . HOH XA 5 .   ? 31.191 38.493  -25.337  1.00 25.02 ? 1377 HOH B O   1 
HETATM 13841 O  O   . HOH XA 5 .   ? 19.935 36.486  -0.049   1.00 29.59 ? 1382 HOH B O   1 
HETATM 13842 O  O   . HOH XA 5 .   ? 31.774 49.893  -28.220  1.00 19.99 ? 1386 HOH B O   1 
HETATM 13843 O  O   . HOH XA 5 .   ? 23.831 40.242  1.766    1.00 28.00 ? 1391 HOH B O   1 
HETATM 13844 O  O   . HOH XA 5 .   ? 23.467 28.973  -13.395  1.00 33.38 ? 1404 HOH B O   1 
HETATM 13845 O  O   . HOH XA 5 .   ? 1.435  34.618  -15.511  1.00 22.99 ? 1412 HOH B O   1 
HETATM 13846 O  O   . HOH XA 5 .   ? 5.931  52.272  -25.279  1.00 16.87 ? 1413 HOH B O   1 
HETATM 13847 O  O   . HOH XA 5 .   ? 2.391  58.183  -22.810  1.00 31.22 ? 1425 HOH B O   1 
HETATM 13848 O  O   . HOH XA 5 .   ? 23.999 51.515  -2.510   1.00 19.08 ? 1426 HOH B O   1 
HETATM 13849 O  O   . HOH XA 5 .   ? 0.370  30.532  -16.602  1.00 30.81 ? 1432 HOH B O   1 
HETATM 13850 O  O   . HOH XA 5 .   ? 31.234 31.344  -18.608  1.00 30.87 ? 1442 HOH B O   1 
HETATM 13851 O  O   . HOH XA 5 .   ? -2.936 41.065  -28.970  1.00 33.95 ? 1443 HOH B O   1 
HETATM 13852 O  O   . HOH XA 5 .   ? 3.064  22.055  -17.050  1.00 31.78 ? 1444 HOH B O   1 
HETATM 13853 O  O   . HOH XA 5 .   ? 17.270 48.688  2.719    1.00 42.75 ? 1451 HOH B O   1 
HETATM 13854 O  O   . HOH XA 5 .   ? 30.722 34.586  -22.461  1.00 25.69 ? 1484 HOH B O   1 
HETATM 13855 O  O   . HOH XA 5 .   ? 26.688 52.313  -23.436  1.00 39.36 ? 1485 HOH B O   1 
HETATM 13856 O  O   . HOH XA 5 .   ? 26.861 51.914  -1.921   1.00 35.74 ? 1500 HOH B O   1 
HETATM 13857 O  O   . HOH XA 5 .   ? 27.174 31.916  -7.938   1.00 25.09 ? 1502 HOH B O   1 
HETATM 13858 O  O   . HOH XA 5 .   ? -0.559 36.046  -12.116  1.00 34.22 ? 1507 HOH B O   1 
HETATM 13859 O  O   . HOH XA 5 .   ? -3.288 35.505  -22.297  1.00 31.15 ? 1509 HOH B O   1 
HETATM 13860 O  O   . HOH XA 5 .   ? 26.430 45.057  -0.916   1.00 30.62 ? 1511 HOH B O   1 
HETATM 13861 O  O   . HOH XA 5 .   ? 22.473 32.422  -17.962  1.00 18.42 ? 1514 HOH B O   1 
HETATM 13862 O  O   . HOH XA 5 .   ? 27.060 33.666  -4.288   1.00 23.44 ? 1522 HOH B O   1 
HETATM 13863 O  O   . HOH XA 5 .   ? 26.570 42.146  0.610    1.00 26.28 ? 1524 HOH B O   1 
HETATM 13864 O  O   . HOH XA 5 .   ? 7.577  34.487  -3.296   1.00 24.69 ? 1528 HOH B O   1 
HETATM 13865 O  O   . HOH XA 5 .   ? 27.932 43.401  -10.511  1.00 43.34 ? 1529 HOH B O   1 
HETATM 13866 O  O   . HOH XA 5 .   ? 31.554 32.655  -20.834  1.00 34.99 ? 1532 HOH B O   1 
HETATM 13867 O  O   . HOH XA 5 .   ? 27.906 46.932  -7.453   1.00 35.61 ? 1538 HOH B O   1 
HETATM 13868 O  O   . HOH XA 5 .   ? 5.881  47.376  3.442    1.00 25.31 ? 1549 HOH B O   1 
HETATM 13869 O  O   . HOH XA 5 .   ? 19.873 54.994  -25.183  1.00 46.62 ? 1610 HOH B O   1 
HETATM 13870 O  O   . HOH XA 5 .   ? -0.841 42.315  -30.180  1.00 43.09 ? 1625 HOH B O   1 
HETATM 13871 O  O   . HOH XA 5 .   ? 0.757  33.070  -22.940  1.00 27.62 ? 1631 HOH B O   1 
HETATM 13872 O  O   . HOH XA 5 .   ? 30.096 42.566  -8.442   1.00 29.65 ? 1634 HOH B O   1 
HETATM 13873 O  O   . HOH XA 5 .   ? 29.036 29.937  -17.687  1.00 19.15 ? 1641 HOH B O   1 
HETATM 13874 O  O   . HOH XA 5 .   ? 28.726 46.468  -10.026  1.00 33.34 ? 1648 HOH B O   1 
HETATM 13875 O  O   . HOH XA 5 .   ? 30.494 46.501  -7.807   1.00 38.27 ? 1650 HOH B O   1 
HETATM 13876 O  O   . HOH XA 5 .   ? 27.672 33.200  -28.252  1.00 33.34 ? 1658 HOH B O   1 
HETATM 13877 O  O   . HOH XA 5 .   ? 26.307 35.283  -27.426  1.00 36.25 ? 1663 HOH B O   1 
HETATM 13878 O  O   . HOH XA 5 .   ? 6.309  36.224  -7.544   1.00 25.57 ? 1666 HOH B O   1 
HETATM 13879 O  O   . HOH XA 5 .   ? -0.335 35.794  -16.428  1.00 18.81 ? 1673 HOH B O   1 
HETATM 13880 O  O   . HOH XA 5 .   ? 21.197 49.864  -28.125  1.00 36.01 ? 1674 HOH B O   1 
HETATM 13881 O  O   . HOH XA 5 .   ? 18.983 36.859  6.208    1.00 32.99 ? 1701 HOH B O   1 
HETATM 13882 O  O   . HOH XA 5 .   ? -2.894 44.796  -7.501   1.00 32.89 ? 1708 HOH B O   1 
HETATM 13883 O  O   . HOH XA 5 .   ? 6.580  25.855  -10.496  1.00 20.96 ? 1709 HOH B O   1 
HETATM 13884 O  O   . HOH XA 5 .   ? -3.341 46.405  -9.969   1.00 21.59 ? 1712 HOH B O   1 
HETATM 13885 O  O   . HOH XA 5 .   ? 4.129  25.398  -9.998   1.00 28.61 ? 1713 HOH B O   1 
HETATM 13886 O  O   . HOH XA 5 .   ? 34.424 49.443  -21.859  1.00 32.15 ? 1717 HOH B O   1 
HETATM 13887 O  O   . HOH XA 5 .   ? 32.196 50.211  -21.051  1.00 27.01 ? 1718 HOH B O   1 
HETATM 13888 O  O   . HOH YA 5 .   ? 70.252 24.893  -36.656  1.00 2.00  ? 154  HOH D O   1 
HETATM 13889 O  O   . HOH YA 5 .   ? 67.283 19.513  -29.888  1.00 2.34  ? 155  HOH D O   1 
HETATM 13890 O  O   . HOH YA 5 .   ? 54.027 34.964  -19.779  1.00 2.70  ? 156  HOH D O   1 
HETATM 13891 O  O   . HOH YA 5 .   ? 55.862 35.252  -28.921  1.00 3.12  ? 157  HOH D O   1 
HETATM 13892 O  O   . HOH YA 5 .   ? 49.487 4.330   -25.378  1.00 8.56  ? 158  HOH D O   1 
HETATM 13893 O  O   . HOH YA 5 .   ? 40.400 17.725  -27.783  1.00 7.58  ? 159  HOH D O   1 
HETATM 13894 O  O   . HOH YA 5 .   ? 58.189 33.549  -23.607  1.00 11.13 ? 160  HOH D O   1 
HETATM 13895 O  O   . HOH YA 5 .   ? 49.825 30.472  -14.962  1.00 8.77  ? 161  HOH D O   1 
HETATM 13896 O  O   . HOH YA 5 .   ? 67.206 25.811  -26.373  1.00 5.62  ? 162  HOH D O   1 
HETATM 13897 O  O   . HOH YA 5 .   ? 48.449 11.971  -35.819  1.00 9.03  ? 163  HOH D O   1 
HETATM 13898 O  O   . HOH YA 5 .   ? 52.874 17.108  -36.840  1.00 8.42  ? 164  HOH D O   1 
HETATM 13899 O  O   . HOH YA 5 .   ? 62.437 20.640  -41.811  1.00 4.68  ? 165  HOH D O   1 
HETATM 13900 O  O   . HOH YA 5 .   ? 54.353 6.672   -32.118  1.00 11.63 ? 166  HOH D O   1 
HETATM 13901 O  O   . HOH YA 5 .   ? 41.049 19.067  -25.449  1.00 4.89  ? 167  HOH D O   1 
HETATM 13902 O  O   . HOH YA 5 .   ? 71.566 17.754  -35.588  1.00 9.67  ? 168  HOH D O   1 
HETATM 13903 O  O   . HOH YA 5 .   ? 66.914 29.684  -27.473  1.00 10.22 ? 169  HOH D O   1 
HETATM 13904 O  O   . HOH YA 5 .   ? 56.547 34.930  -25.313  1.00 6.50  ? 170  HOH D O   1 
HETATM 13905 O  O   . HOH YA 5 .   ? 50.734 15.431  -30.390  1.00 5.16  ? 171  HOH D O   1 
HETATM 13906 O  O   . HOH YA 5 .   ? 66.898 17.327  -28.315  1.00 7.45  ? 172  HOH D O   1 
HETATM 13907 O  O   . HOH YA 5 .   ? 63.371 11.409  -29.638  1.00 14.22 ? 173  HOH D O   1 
HETATM 13908 O  O   . HOH YA 5 .   ? 52.931 20.752  -16.937  1.00 10.25 ? 174  HOH D O   1 
HETATM 13909 O  O   . HOH YA 5 .   ? 74.929 22.317  -40.827  1.00 9.52  ? 175  HOH D O   1 
HETATM 13910 O  O   . HOH YA 5 .   ? 49.567 19.109  -41.315  1.00 13.78 ? 176  HOH D O   1 
HETATM 13911 O  O   . HOH YA 5 .   ? 68.276 16.522  -43.802  1.00 8.64  ? 177  HOH D O   1 
HETATM 13912 O  O   . HOH YA 5 .   ? 47.188 18.749  -38.128  1.00 10.43 ? 178  HOH D O   1 
HETATM 13913 O  O   . HOH YA 5 .   ? 69.888 13.911  -33.911  1.00 7.71  ? 179  HOH D O   1 
HETATM 13914 O  O   . HOH YA 5 .   ? 73.738 23.473  -38.655  1.00 10.73 ? 180  HOH D O   1 
HETATM 13915 O  O   . HOH YA 5 .   ? 43.843 22.905  -20.798  1.00 6.76  ? 181  HOH D O   1 
HETATM 13916 O  O   . HOH YA 5 .   ? 57.035 16.731  -22.139  1.00 5.39  ? 182  HOH D O   1 
HETATM 13917 O  O   . HOH YA 5 .   ? 68.990 21.502  -29.156  1.00 5.06  ? 183  HOH D O   1 
HETATM 13918 O  O   . HOH YA 5 .   ? 37.417 27.440  -31.151  1.00 12.41 ? 190  HOH D O   1 
HETATM 13919 O  O   . HOH YA 5 .   ? 64.365 21.509  -43.673  1.00 10.61 ? 214  HOH D O   1 
HETATM 13920 O  O   . HOH YA 5 .   ? 63.605 11.206  -34.759  1.00 10.46 ? 223  HOH D O   1 
HETATM 13921 O  O   . HOH YA 5 .   ? 42.920 27.868  -19.603  1.00 19.15 ? 224  HOH D O   1 
HETATM 13922 O  O   . HOH YA 5 .   ? 48.587 8.331   -32.653  1.00 13.49 ? 225  HOH D O   1 
HETATM 13923 O  O   . HOH YA 5 .   ? 43.324 20.890  -41.209  1.00 20.24 ? 229  HOH D O   1 
HETATM 13924 O  O   . HOH YA 5 .   ? 59.806 9.821   -27.353  1.00 19.59 ? 239  HOH D O   1 
HETATM 13925 O  O   . HOH YA 5 .   ? 51.213 27.951  -14.682  1.00 13.44 ? 240  HOH D O   1 
HETATM 13926 O  O   . HOH YA 5 .   ? 45.873 13.757  -20.792  1.00 9.78  ? 267  HOH D O   1 
HETATM 13927 O  O   . HOH YA 5 .   ? 55.071 22.146  -16.194  1.00 12.32 ? 268  HOH D O   1 
HETATM 13928 O  O   . HOH YA 5 .   ? 52.502 35.575  -38.435  1.00 17.12 ? 287  HOH D O   1 
HETATM 13929 O  O   . HOH YA 5 .   ? 66.661 14.022  -32.543  1.00 18.79 ? 288  HOH D O   1 
HETATM 13930 O  O   . HOH YA 5 .   ? 59.963 31.584  -39.465  1.00 11.69 ? 296  HOH D O   1 
HETATM 13931 O  O   . HOH YA 5 .   ? 68.272 23.063  -26.592  1.00 16.75 ? 297  HOH D O   1 
HETATM 13932 O  O   . HOH YA 5 .   ? 50.070 17.570  -20.988  1.00 6.02  ? 307  HOH D O   1 
HETATM 13933 O  O   . HOH YA 5 .   ? 46.506 5.308   -28.306  1.00 23.00 ? 310  HOH D O   1 
HETATM 13934 O  O   . HOH YA 5 .   ? 39.636 32.994  -36.607  1.00 25.98 ? 316  HOH D O   1 
HETATM 13935 O  O   . HOH YA 5 .   ? 59.721 34.375  -26.957  1.00 29.61 ? 320  HOH D O   1 
HETATM 13936 O  O   . HOH YA 5 .   ? 42.969 18.716  -38.267  1.00 16.41 ? 321  HOH D O   1 
HETATM 13937 O  O   . HOH YA 5 .   ? 50.978 0.823   -28.770  1.00 12.37 ? 330  HOH D O   1 
HETATM 13938 O  O   . HOH YA 5 .   ? 48.039 5.126   -35.984  1.00 22.93 ? 339  HOH D O   1 
HETATM 13939 O  O   . HOH YA 5 .   ? 41.339 24.321  -20.750  1.00 16.35 ? 345  HOH D O   1 
HETATM 13940 O  O   . HOH YA 5 .   ? 56.369 36.391  -38.625  1.00 13.58 ? 356  HOH D O   1 
HETATM 13941 O  O   . HOH YA 5 .   ? 52.716 18.728  -20.639  1.00 14.82 ? 360  HOH D O   1 
HETATM 13942 O  O   . HOH YA 5 .   ? 47.026 7.479   -29.930  1.00 13.95 ? 361  HOH D O   1 
HETATM 13943 O  O   . HOH YA 5 .   ? 68.451 14.968  -28.302  1.00 18.45 ? 366  HOH D O   1 
HETATM 13944 O  O   . HOH YA 5 .   ? 60.295 32.595  -24.705  1.00 19.43 ? 374  HOH D O   1 
HETATM 13945 O  O   . HOH YA 5 .   ? 41.292 8.539   -31.486  1.00 13.16 ? 383  HOH D O   1 
HETATM 13946 O  O   . HOH YA 5 .   ? 54.142 2.227   -30.246  1.00 14.92 ? 384  HOH D O   1 
HETATM 13947 O  O   . HOH YA 5 .   ? 40.799 29.530  -25.733  1.00 16.22 ? 389  HOH D O   1 
HETATM 13948 O  O   . HOH YA 5 .   ? 44.965 38.980  -37.057  1.00 15.85 ? 398  HOH D O   1 
HETATM 13949 O  O   . HOH YA 5 .   ? 54.724 6.933   -17.436  1.00 14.27 ? 404  HOH D O   1 
HETATM 13950 O  O   . HOH YA 5 .   ? 64.224 13.094  -31.862  1.00 24.71 ? 415  HOH D O   1 
HETATM 13951 O  O   . HOH YA 5 .   ? 52.081 33.455  -12.673  1.00 20.54 ? 417  HOH D O   1 
HETATM 13952 O  O   . HOH YA 5 .   ? 39.571 25.681  -35.975  1.00 23.31 ? 432  HOH D O   1 
HETATM 13953 O  O   . HOH YA 5 .   ? 47.560 37.248  -46.246  1.00 35.22 ? 443  HOH D O   1 
HETATM 13954 O  O   . HOH YA 5 .   ? 49.548 18.106  -44.135  1.00 27.47 ? 469  HOH D O   1 
HETATM 13955 O  O   . HOH YA 5 .   ? 37.374 15.415  -28.080  1.00 26.17 ? 471  HOH D O   1 
HETATM 13956 O  O   . HOH YA 5 .   ? 49.532 11.354  -42.847  1.00 25.05 ? 506  HOH D O   1 
HETATM 13957 O  O   . HOH YA 5 .   ? 44.514 25.702  -48.621  1.00 30.09 ? 508  HOH D O   1 
HETATM 13958 O  O   . HOH YA 5 .   ? 57.274 7.583   -17.712  1.00 19.10 ? 515  HOH D O   1 
HETATM 13959 O  O   . HOH YA 5 .   ? 55.855 31.480  -11.666  1.00 15.52 ? 520  HOH D O   1 
HETATM 13960 O  O   . HOH YA 5 .   ? 38.448 26.880  -23.652  1.00 13.58 ? 521  HOH D O   1 
HETATM 13961 O  O   . HOH YA 5 .   ? 71.868 13.185  -41.567  1.00 23.23 ? 522  HOH D O   1 
HETATM 13962 O  O   . HOH YA 5 .   ? 58.486 8.481   -29.784  1.00 22.81 ? 528  HOH D O   1 
HETATM 13963 O  O   . HOH YA 5 .   ? 40.842 11.668  -20.671  1.00 26.52 ? 534  HOH D O   1 
HETATM 13964 O  O   . HOH YA 5 .   ? 51.313 39.827  -39.850  1.00 27.02 ? 543  HOH D O   1 
HETATM 13965 O  O   . HOH YA 5 .   ? 44.082 21.138  -18.776  1.00 24.85 ? 547  HOH D O   1 
HETATM 13966 O  O   . HOH YA 5 .   ? 53.358 25.676  -45.135  1.00 19.05 ? 554  HOH D O   1 
HETATM 13967 O  O   . HOH YA 5 .   ? 52.449 10.112  -15.807  1.00 29.76 ? 560  HOH D O   1 
HETATM 13968 O  O   . HOH YA 5 .   ? 37.499 20.589  -34.976  1.00 28.20 ? 567  HOH D O   1 
HETATM 13969 O  O   . HOH YA 5 .   ? 68.610 18.483  -26.132  1.00 18.14 ? 570  HOH D O   1 
HETATM 13970 O  O   . HOH YA 5 .   ? 47.247 15.959  -38.978  1.00 25.03 ? 581  HOH D O   1 
HETATM 13971 O  O   . HOH YA 5 .   ? 37.701 24.574  -34.343  1.00 33.47 ? 582  HOH D O   1 
HETATM 13972 O  O   . HOH YA 5 .   ? 36.787 23.501  -20.954  1.00 18.90 ? 583  HOH D O   1 
HETATM 13973 O  O   . HOH YA 5 .   ? 58.901 22.798  -44.997  1.00 21.77 ? 600  HOH D O   1 
HETATM 13974 O  O   . HOH YA 5 .   ? 58.852 10.246  -20.638  1.00 15.58 ? 608  HOH D O   1 
HETATM 13975 O  O   . HOH YA 5 .   ? 51.505 16.774  -39.040  1.00 10.38 ? 613  HOH D O   1 
HETATM 13976 O  O   . HOH YA 5 .   ? 54.640 18.339  -22.607  1.00 7.29  ? 620  HOH D O   1 
HETATM 13977 O  O   . HOH YA 5 .   ? 57.554 36.467  -27.276  1.00 12.28 ? 622  HOH D O   1 
HETATM 13978 O  O   . HOH YA 5 .   ? 48.365 2.062   -26.123  1.00 14.39 ? 623  HOH D O   1 
HETATM 13979 O  O   . HOH YA 5 .   ? 47.385 2.861   -28.561  1.00 20.20 ? 628  HOH D O   1 
HETATM 13980 O  O   . HOH YA 5 .   ? 51.235 25.825  -43.384  1.00 17.82 ? 633  HOH D O   1 
HETATM 13981 O  O   . HOH YA 5 .   ? 71.219 15.587  -28.142  1.00 10.32 ? 635  HOH D O   1 
HETATM 13982 O  O   . HOH YA 5 .   ? 44.892 9.104   -28.955  1.00 20.80 ? 639  HOH D O   1 
HETATM 13983 O  O   . HOH YA 5 .   ? 46.908 8.456   -25.047  1.00 24.81 ? 641  HOH D O   1 
HETATM 13984 O  O   . HOH YA 5 .   ? 59.423 7.528   -25.851  1.00 16.16 ? 645  HOH D O   1 
HETATM 13985 O  O   . HOH YA 5 .   ? 56.744 18.800  -20.374  1.00 18.34 ? 657  HOH D O   1 
HETATM 13986 O  O   . HOH YA 5 .   ? 65.763 25.387  -23.019  1.00 13.36 ? 666  HOH D O   1 
HETATM 13987 O  O   . HOH YA 5 .   ? 40.266 28.576  -42.162  1.00 16.90 ? 668  HOH D O   1 
HETATM 13988 O  O   . HOH YA 5 .   ? 46.425 18.608  -20.289  1.00 27.59 ? 671  HOH D O   1 
HETATM 13989 O  O   . HOH YA 5 .   ? 39.551 16.086  -31.798  1.00 17.47 ? 678  HOH D O   1 
HETATM 13990 O  O   . HOH YA 5 .   ? 42.784 7.511   -34.395  1.00 19.65 ? 682  HOH D O   1 
HETATM 13991 O  O   . HOH YA 5 .   ? 41.412 19.923  -18.993  1.00 24.99 ? 684  HOH D O   1 
HETATM 13992 O  O   . HOH YA 5 .   ? 53.386 18.010  -17.978  1.00 20.46 ? 687  HOH D O   1 
HETATM 13993 O  O   . HOH YA 5 .   ? 53.589 18.233  -42.628  1.00 23.62 ? 691  HOH D O   1 
HETATM 13994 O  O   . HOH YA 5 .   ? 40.632 8.757   -34.589  1.00 19.88 ? 708  HOH D O   1 
HETATM 13995 O  O   . HOH YA 5 .   ? 39.206 10.448  -22.478  1.00 25.96 ? 716  HOH D O   1 
HETATM 13996 O  O   . HOH YA 5 .   ? 65.178 30.540  -36.959  1.00 22.15 ? 724  HOH D O   1 
HETATM 13997 O  O   . HOH YA 5 .   ? 50.407 34.738  -39.993  1.00 15.06 ? 726  HOH D O   1 
HETATM 13998 O  O   . HOH YA 5 .   ? 69.661 14.344  -44.273  1.00 29.83 ? 738  HOH D O   1 
HETATM 13999 O  O   . HOH YA 5 .   ? 32.256 29.540  -25.373  1.00 23.48 ? 751  HOH D O   1 
HETATM 14000 O  O   . HOH YA 5 .   ? 50.990 21.116  -14.664  1.00 27.53 ? 752  HOH D O   1 
HETATM 14001 O  O   . HOH YA 5 .   ? 47.564 16.149  -19.676  1.00 27.95 ? 757  HOH D O   1 
HETATM 14002 O  O   . HOH YA 5 .   ? 38.920 17.497  -29.942  1.00 19.68 ? 787  HOH D O   1 
HETATM 14003 O  O   . HOH YA 5 .   ? 53.267 3.175   -36.356  1.00 26.08 ? 801  HOH D O   1 
HETATM 14004 O  O   . HOH YA 5 .   ? 64.821 27.415  -42.982  1.00 27.99 ? 812  HOH D O   1 
HETATM 14005 O  O   . HOH YA 5 .   ? 59.468 20.580  -39.447  1.00 13.31 ? 814  HOH D O   1 
HETATM 14006 O  O   . HOH YA 5 .   ? 60.994 16.080  -19.152  1.00 32.10 ? 824  HOH D O   1 
HETATM 14007 O  O   . HOH YA 5 .   ? 61.467 31.036  -21.581  1.00 27.70 ? 837  HOH D O   1 
HETATM 14008 O  O   . HOH YA 5 .   ? 41.993 14.902  -35.355  1.00 24.13 ? 841  HOH D O   1 
HETATM 14009 O  O   . HOH YA 5 .   ? 49.005 2.118   -35.231  1.00 21.35 ? 850  HOH D O   1 
HETATM 14010 O  O   . HOH YA 5 .   ? 65.750 14.603  -40.950  1.00 29.40 ? 855  HOH D O   1 
HETATM 14011 O  O   . HOH YA 5 .   ? 35.109 30.812  -32.638  1.00 30.42 ? 862  HOH D O   1 
HETATM 14012 O  O   . HOH YA 5 .   ? 43.278 29.060  -42.985  1.00 26.34 ? 880  HOH D O   1 
HETATM 14013 O  O   . HOH YA 5 .   ? 58.399 33.225  -40.698  1.00 18.59 ? 887  HOH D O   1 
HETATM 14014 O  O   . HOH YA 5 .   ? 40.720 35.921  -32.325  1.00 21.59 ? 888  HOH D O   1 
HETATM 14015 O  O   . HOH YA 5 .   ? 68.376 23.733  -43.580  1.00 17.24 ? 891  HOH D O   1 
HETATM 14016 O  O   . HOH YA 5 .   ? 70.563 12.436  -36.665  1.00 24.47 ? 920  HOH D O   1 
HETATM 14017 O  O   . HOH YA 5 .   ? 67.897 32.339  -28.000  1.00 22.29 ? 922  HOH D O   1 
HETATM 14018 O  O   . HOH YA 5 .   ? 52.780 29.942  -12.829  1.00 29.61 ? 929  HOH D O   1 
HETATM 14019 O  O   . HOH YA 5 .   ? 70.842 32.036  -27.931  1.00 30.12 ? 932  HOH D O   1 
HETATM 14020 O  O   . HOH YA 5 .   ? 58.401 26.080  -43.327  1.00 21.85 ? 933  HOH D O   1 
HETATM 14021 O  O   . HOH YA 5 .   ? 62.984 32.264  -37.564  1.00 29.50 ? 937  HOH D O   1 
HETATM 14022 O  O   . HOH YA 5 .   ? 67.244 20.798  -45.569  1.00 30.63 ? 948  HOH D O   1 
HETATM 14023 O  O   . HOH YA 5 .   ? 45.646 22.839  -15.809  1.00 20.46 ? 953  HOH D O   1 
HETATM 14024 O  O   . HOH YA 5 .   ? 43.231 29.122  -48.153  1.00 33.99 ? 981  HOH D O   1 
HETATM 14025 O  O   . HOH YA 5 .   ? 62.589 27.742  -20.181  1.00 26.38 ? 1016 HOH D O   1 
HETATM 14026 O  O   . HOH YA 5 .   ? 75.062 19.630  -40.517  1.00 25.60 ? 1018 HOH D O   1 
HETATM 14027 O  O   . HOH YA 5 .   ? 65.092 10.522  -20.216  1.00 20.50 ? 1021 HOH D O   1 
HETATM 14028 O  O   . HOH YA 5 .   ? 35.060 33.903  -40.606  1.00 29.51 ? 1029 HOH D O   1 
HETATM 14029 O  O   . HOH YA 5 .   ? 57.484 20.569  -16.804  1.00 23.32 ? 1036 HOH D O   1 
HETATM 14030 O  O   . HOH YA 5 .   ? 37.214 12.457  -22.317  1.00 25.65 ? 1044 HOH D O   1 
HETATM 14031 O  O   . HOH YA 5 .   ? 61.929 12.350  -20.635  1.00 26.82 ? 1058 HOH D O   1 
HETATM 14032 O  O   . HOH YA 5 .   ? 34.856 20.565  -21.954  1.00 34.42 ? 1064 HOH D O   1 
HETATM 14033 O  O   . HOH YA 5 .   ? 50.628 6.662   -13.708  1.00 27.61 ? 1068 HOH D O   1 
HETATM 14034 O  O   . HOH YA 5 .   ? 66.805 23.331  -22.403  1.00 25.99 ? 1100 HOH D O   1 
HETATM 14035 O  O   . HOH YA 5 .   ? 53.530 32.090  -10.661  1.00 22.54 ? 1102 HOH D O   1 
HETATM 14036 O  O   . HOH YA 5 .   ? 63.130 10.022  -32.391  1.00 30.00 ? 1106 HOH D O   1 
HETATM 14037 O  O   . HOH YA 5 .   ? 53.704 4.111   -33.094  1.00 23.87 ? 1112 HOH D O   1 
HETATM 14038 O  O   . HOH YA 5 .   ? 55.380 28.734  -12.196  1.00 31.67 ? 1117 HOH D O   1 
HETATM 14039 O  O   . HOH YA 5 .   ? 56.552 5.206   -31.072  1.00 22.20 ? 1118 HOH D O   1 
HETATM 14040 O  O   . HOH YA 5 .   ? 52.246 25.419  -14.273  1.00 32.31 ? 1120 HOH D O   1 
HETATM 14041 O  O   . HOH YA 5 .   ? 43.202 7.172   -30.723  1.00 26.83 ? 1126 HOH D O   1 
HETATM 14042 O  O   . HOH YA 5 .   ? 62.373 9.402   -28.088  1.00 19.63 ? 1136 HOH D O   1 
HETATM 14043 O  O   . HOH YA 5 .   ? 42.674 27.859  -45.495  1.00 23.77 ? 1146 HOH D O   1 
HETATM 14044 O  O   . HOH YA 5 .   ? 61.233 26.816  -13.905  1.00 40.75 ? 1147 HOH D O   1 
HETATM 14045 O  O   . HOH YA 5 .   ? 39.222 33.732  -39.281  1.00 34.22 ? 1148 HOH D O   1 
HETATM 14046 O  O   . HOH YA 5 .   ? 44.865 17.772  -18.716  1.00 38.64 ? 1151 HOH D O   1 
HETATM 14047 O  O   . HOH YA 5 .   ? 43.029 5.085   -35.176  1.00 39.69 ? 1153 HOH D O   1 
HETATM 14048 O  O   . HOH YA 5 .   ? 39.877 26.482  -21.436  1.00 26.07 ? 1171 HOH D O   1 
HETATM 14049 O  O   . HOH YA 5 .   ? 33.040 30.826  -43.163  1.00 46.82 ? 1177 HOH D O   1 
HETATM 14050 O  O   . HOH YA 5 .   ? 60.570 7.602   -23.163  1.00 28.64 ? 1186 HOH D O   1 
HETATM 14051 O  O   . HOH YA 5 .   ? 68.066 14.474  -25.311  1.00 24.26 ? 1223 HOH D O   1 
HETATM 14052 O  O   . HOH YA 5 .   ? 44.731 3.616   -36.369  1.00 32.24 ? 1224 HOH D O   1 
HETATM 14053 O  O   . HOH YA 5 .   ? 54.123 7.567   -14.937  1.00 31.58 ? 1228 HOH D O   1 
HETATM 14054 O  O   . HOH YA 5 .   ? 33.785 24.185  -28.831  1.00 27.23 ? 1253 HOH D O   1 
HETATM 14055 O  O   . HOH YA 5 .   ? 63.038 32.601  -23.022  1.00 30.66 ? 1258 HOH D O   1 
HETATM 14056 O  O   . HOH YA 5 .   ? 40.564 37.750  -34.677  1.00 26.07 ? 1283 HOH D O   1 
HETATM 14057 O  O   . HOH YA 5 .   ? 62.050 33.230  -39.574  1.00 26.93 ? 1309 HOH D O   1 
HETATM 14058 O  O   . HOH YA 5 .   ? 57.598 5.241   -35.633  1.00 23.76 ? 1319 HOH D O   1 
HETATM 14059 O  O   . HOH YA 5 .   ? 64.360 29.486  -18.918  1.00 32.47 ? 1320 HOH D O   1 
HETATM 14060 O  O   . HOH YA 5 .   ? 33.717 21.549  -28.458  1.00 38.00 ? 1322 HOH D O   1 
HETATM 14061 O  O   . HOH YA 5 .   ? 56.180 26.483  -13.077  1.00 19.66 ? 1324 HOH D O   1 
HETATM 14062 O  O   . HOH YA 5 .   ? 49.356 49.467  -37.698  1.00 35.51 ? 1352 HOH D O   1 
HETATM 14063 O  O   . HOH YA 5 .   ? 67.441 11.164  -36.834  1.00 29.73 ? 1375 HOH D O   1 
HETATM 14064 O  O   . HOH YA 5 .   ? 58.626 5.509   -32.909  1.00 26.21 ? 1398 HOH D O   1 
HETATM 14065 O  O   . HOH YA 5 .   ? 56.359 9.251   -33.270  1.00 22.02 ? 1414 HOH D O   1 
HETATM 14066 O  O   . HOH YA 5 .   ? 66.382 26.980  -16.158  1.00 41.43 ? 1421 HOH D O   1 
HETATM 14067 O  O   . HOH YA 5 .   ? 66.435 13.169  -21.632  1.00 29.83 ? 1460 HOH D O   1 
HETATM 14068 O  O   . HOH YA 5 .   ? 68.395 36.223  -31.228  1.00 43.07 ? 1463 HOH D O   1 
HETATM 14069 O  O   . HOH YA 5 .   ? 66.242 16.328  -20.346  1.00 41.10 ? 1469 HOH D O   1 
HETATM 14070 O  O   . HOH YA 5 .   ? 74.660 20.327  -47.775  1.00 32.09 ? 1475 HOH D O   1 
HETATM 14071 O  O   . HOH YA 5 .   ? 40.520 39.348  -38.397  1.00 35.95 ? 1481 HOH D O   1 
HETATM 14072 O  O   . HOH YA 5 .   ? 63.852 14.458  -20.547  1.00 19.26 ? 1487 HOH D O   1 
HETATM 14073 O  O   . HOH YA 5 .   ? 37.719 35.372  -40.716  1.00 39.58 ? 1505 HOH D O   1 
HETATM 14074 O  O   . HOH YA 5 .   ? 68.541 31.121  -18.688  1.00 38.73 ? 1506 HOH D O   1 
HETATM 14075 O  O   . HOH YA 5 .   ? 53.349 14.454  -16.675  1.00 27.52 ? 1519 HOH D O   1 
HETATM 14076 O  O   . HOH YA 5 .   ? 72.078 20.864  -48.497  1.00 32.95 ? 1548 HOH D O   1 
HETATM 14077 O  O   . HOH YA 5 .   ? 38.113 31.131  -35.325  1.00 37.67 ? 1551 HOH D O   1 
HETATM 14078 O  O   . HOH YA 5 .   ? 73.693 22.363  -45.243  1.00 34.33 ? 1580 HOH D O   1 
HETATM 14079 O  O   . HOH YA 5 .   ? 35.068 33.456  -34.593  1.00 26.35 ? 1587 HOH D O   1 
HETATM 14080 O  O   . HOH YA 5 .   ? 44.898 39.468  -40.105  1.00 41.14 ? 1592 HOH D O   1 
HETATM 14081 O  O   . HOH YA 5 .   ? 66.748 10.445  -21.999  1.00 40.65 ? 1597 HOH D O   1 
HETATM 14082 O  O   . HOH YA 5 .   ? 40.689 28.909  -20.705  1.00 33.78 ? 1601 HOH D O   1 
HETATM 14083 O  O   . HOH YA 5 .   ? 46.693 8.016   -36.301  1.00 45.98 ? 1605 HOH D O   1 
HETATM 14084 O  O   . HOH YA 5 .   ? 63.378 25.996  -21.893  1.00 48.82 ? 1612 HOH D O   1 
HETATM 14085 O  O   . HOH YA 5 .   ? 60.267 36.302  -15.807  1.00 29.38 ? 1617 HOH D O   1 
HETATM 14086 O  O   . HOH YA 5 .   ? 39.161 17.484  -37.090  1.00 37.32 ? 1660 HOH D O   1 
HETATM 14087 O  O   . HOH YA 5 .   ? 60.398 34.200  -19.814  1.00 32.44 ? 1671 HOH D O   1 
HETATM 14088 O  O   . HOH YA 5 .   ? 61.349 21.155  -19.408  1.00 5.42  ? 1697 HOH D O   1 
HETATM 14089 O  O   . HOH YA 5 .   ? 61.360 26.244  -17.217  1.00 24.31 ? 1706 HOH D O   1 
HETATM 14090 O  O   . HOH YA 5 .   ? 39.296 35.933  -44.412  1.00 35.49 ? 1710 HOH D O   1 
HETATM 14091 O  O   . HOH YA 5 .   ? 54.341 24.893  -12.767  1.00 29.16 ? 1745 HOH D O   1 
HETATM 14092 O  O   . HOH ZA 5 .   ? 36.883 46.188  -17.439  1.00 2.74  ? 154  HOH E O   1 
HETATM 14093 O  O   . HOH ZA 5 .   ? 45.334 63.267  -27.428  1.00 10.23 ? 155  HOH E O   1 
HETATM 14094 O  O   . HOH ZA 5 .   ? 48.003 56.478  -21.275  1.00 5.30  ? 156  HOH E O   1 
HETATM 14095 O  O   . HOH ZA 5 .   ? 43.900 44.273  -33.945  1.00 12.91 ? 157  HOH E O   1 
HETATM 14096 O  O   . HOH ZA 5 .   ? 65.488 47.394  -21.573  1.00 7.15  ? 158  HOH E O   1 
HETATM 14097 O  O   . HOH ZA 5 .   ? 64.569 53.296  -18.111  1.00 7.59  ? 159  HOH E O   1 
HETATM 14098 O  O   . HOH ZA 5 .   ? 40.182 52.211  -28.527  1.00 6.90  ? 160  HOH E O   1 
HETATM 14099 O  O   . HOH ZA 5 .   ? 65.445 43.106  -20.687  1.00 5.47  ? 161  HOH E O   1 
HETATM 14100 O  O   . HOH ZA 5 .   ? 62.800 56.829  -4.707   1.00 22.87 ? 162  HOH E O   1 
HETATM 14101 O  O   . HOH ZA 5 .   ? 54.654 37.158  -21.417  1.00 2.36  ? 163  HOH E O   1 
HETATM 14102 O  O   . HOH ZA 5 .   ? 40.160 45.206  -23.611  1.00 8.86  ? 164  HOH E O   1 
HETATM 14103 O  O   . HOH ZA 5 .   ? 51.340 51.475  -10.880  1.00 10.42 ? 165  HOH E O   1 
HETATM 14104 O  O   . HOH ZA 5 .   ? 58.615 38.221  -22.811  1.00 8.11  ? 166  HOH E O   1 
HETATM 14105 O  O   . HOH ZA 5 .   ? 34.061 48.029  -17.118  1.00 9.09  ? 167  HOH E O   1 
HETATM 14106 O  O   . HOH ZA 5 .   ? 32.336 40.649  -27.128  1.00 12.92 ? 168  HOH E O   1 
HETATM 14107 O  O   . HOH ZA 5 .   ? 35.890 42.281  -12.299  1.00 7.32  ? 169  HOH E O   1 
HETATM 14108 O  O   . HOH ZA 5 .   ? 49.020 36.319  -13.261  1.00 10.96 ? 170  HOH E O   1 
HETATM 14109 O  O   . HOH ZA 5 .   ? 44.592 52.679  -11.234  1.00 9.34  ? 171  HOH E O   1 
HETATM 14110 O  O   . HOH ZA 5 .   ? 34.729 40.957  -20.776  1.00 4.35  ? 172  HOH E O   1 
HETATM 14111 O  O   . HOH ZA 5 .   ? 55.326 37.124  -30.818  1.00 4.80  ? 173  HOH E O   1 
HETATM 14112 O  O   . HOH ZA 5 .   ? 40.713 41.716  -28.904  1.00 11.49 ? 174  HOH E O   1 
HETATM 14113 O  O   . HOH ZA 5 .   ? 56.121 37.291  -23.968  1.00 8.90  ? 175  HOH E O   1 
HETATM 14114 O  O   . HOH ZA 5 .   ? 48.029 54.030  -14.455  1.00 10.23 ? 176  HOH E O   1 
HETATM 14115 O  O   . HOH ZA 5 .   ? 59.633 40.132  -24.851  1.00 12.93 ? 177  HOH E O   1 
HETATM 14116 O  O   . HOH ZA 5 .   ? 38.721 53.516  -26.531  1.00 5.30  ? 178  HOH E O   1 
HETATM 14117 O  O   . HOH ZA 5 .   ? 66.440 49.987  -21.091  1.00 11.12 ? 179  HOH E O   1 
HETATM 14118 O  O   . HOH ZA 5 .   ? 52.014 41.737  -36.454  1.00 5.78  ? 180  HOH E O   1 
HETATM 14119 O  O   . HOH ZA 5 .   ? 42.554 32.610  -16.059  1.00 13.32 ? 181  HOH E O   1 
HETATM 14120 O  O   . HOH ZA 5 .   ? 53.113 35.962  -12.015  1.00 12.61 ? 182  HOH E O   1 
HETATM 14121 O  O   . HOH ZA 5 .   ? 38.033 46.987  -24.108  1.00 10.77 ? 183  HOH E O   1 
HETATM 14122 O  O   . HOH ZA 5 .   ? 43.044 52.862  -14.827  1.00 6.52  ? 184  HOH E O   1 
HETATM 14123 O  O   . HOH ZA 5 .   ? 61.377 51.486  -29.517  1.00 11.73 ? 185  HOH E O   1 
HETATM 14124 O  O   . HOH ZA 5 .   ? 37.041 38.302  -18.114  1.00 8.23  ? 186  HOH E O   1 
HETATM 14125 O  O   . HOH ZA 5 .   ? 56.145 55.762  -28.003  1.00 5.89  ? 187  HOH E O   1 
HETATM 14126 O  O   . HOH ZA 5 .   ? 65.934 40.574  -20.317  1.00 14.64 ? 188  HOH E O   1 
HETATM 14127 O  O   . HOH ZA 5 .   ? 56.193 50.216  -33.982  1.00 15.48 ? 189  HOH E O   1 
HETATM 14128 O  O   . HOH ZA 5 .   ? 55.824 40.739  -10.442  1.00 16.40 ? 191  HOH E O   1 
HETATM 14129 O  O   . HOH ZA 5 .   ? 44.217 48.563  -32.359  1.00 3.34  ? 192  HOH E O   1 
HETATM 14130 O  O   . HOH ZA 5 .   ? 59.536 61.295  -14.323  1.00 13.58 ? 193  HOH E O   1 
HETATM 14131 O  O   . HOH ZA 5 .   ? 49.885 54.623  -30.781  1.00 8.42  ? 194  HOH E O   1 
HETATM 14132 O  O   . HOH ZA 5 .   ? 53.769 51.203  -34.101  1.00 16.73 ? 210  HOH E O   1 
HETATM 14133 O  O   . HOH ZA 5 .   ? 49.005 56.553  -14.602  1.00 9.77  ? 212  HOH E O   1 
HETATM 14134 O  O   . HOH ZA 5 .   ? 39.315 52.919  -15.673  1.00 15.34 ? 217  HOH E O   1 
HETATM 14135 O  O   . HOH ZA 5 .   ? 50.143 53.478  -12.547  1.00 11.82 ? 219  HOH E O   1 
HETATM 14136 O  O   . HOH ZA 5 .   ? 39.258 35.216  -21.894  1.00 16.43 ? 221  HOH E O   1 
HETATM 14137 O  O   . HOH ZA 5 .   ? 53.915 53.985  -28.284  1.00 15.29 ? 222  HOH E O   1 
HETATM 14138 O  O   . HOH ZA 5 .   ? 66.939 48.474  -11.199  1.00 15.21 ? 226  HOH E O   1 
HETATM 14139 O  O   . HOH ZA 5 .   ? 36.203 37.530  -15.485  1.00 14.93 ? 233  HOH E O   1 
HETATM 14140 O  O   . HOH ZA 5 .   ? 39.790 43.745  -31.124  1.00 19.42 ? 244  HOH E O   1 
HETATM 14141 O  O   . HOH ZA 5 .   ? 42.522 62.053  -25.232  1.00 12.37 ? 245  HOH E O   1 
HETATM 14142 O  O   . HOH ZA 5 .   ? 44.392 59.622  -16.675  1.00 9.11  ? 246  HOH E O   1 
HETATM 14143 O  O   . HOH ZA 5 .   ? 67.594 56.687  -12.480  1.00 14.72 ? 249  HOH E O   1 
HETATM 14144 O  O   . HOH ZA 5 .   ? 68.153 43.979  -15.381  1.00 7.32  ? 258  HOH E O   1 
HETATM 14145 O  O   . HOH ZA 5 .   ? 37.841 56.207  -19.529  1.00 21.68 ? 262  HOH E O   1 
HETATM 14146 O  O   . HOH ZA 5 .   ? 53.942 52.724  -10.373  1.00 13.56 ? 269  HOH E O   1 
HETATM 14147 O  O   . HOH ZA 5 .   ? 64.483 55.584  -19.454  1.00 15.38 ? 271  HOH E O   1 
HETATM 14148 O  O   . HOH ZA 5 .   ? 57.194 39.251  -26.484  1.00 14.78 ? 283  HOH E O   1 
HETATM 14149 O  O   . HOH ZA 5 .   ? 45.447 57.870  -31.983  1.00 12.45 ? 293  HOH E O   1 
HETATM 14150 O  O   . HOH ZA 5 .   ? 66.501 51.241  -18.368  1.00 16.38 ? 311  HOH E O   1 
HETATM 14151 O  O   . HOH ZA 5 .   ? 50.887 60.105  -14.960  1.00 17.37 ? 314  HOH E O   1 
HETATM 14152 O  O   . HOH ZA 5 .   ? 68.389 44.119  -12.565  1.00 15.80 ? 324  HOH E O   1 
HETATM 14153 O  O   . HOH ZA 5 .   ? 43.218 40.674  -8.227   1.00 19.90 ? 333  HOH E O   1 
HETATM 14154 O  O   . HOH ZA 5 .   ? 38.809 42.415  -10.740  1.00 10.76 ? 335  HOH E O   1 
HETATM 14155 O  O   . HOH ZA 5 .   ? 29.722 46.705  -15.904  1.00 11.50 ? 350  HOH E O   1 
HETATM 14156 O  O   . HOH ZA 5 .   ? 41.225 40.569  -5.594   1.00 30.68 ? 372  HOH E O   1 
HETATM 14157 O  O   . HOH ZA 5 .   ? 52.110 68.246  -34.619  1.00 16.57 ? 375  HOH E O   1 
HETATM 14158 O  O   . HOH ZA 5 .   ? 36.044 42.813  -24.814  1.00 10.52 ? 378  HOH E O   1 
HETATM 14159 O  O   . HOH ZA 5 .   ? 52.352 53.630  -30.570  1.00 12.96 ? 379  HOH E O   1 
HETATM 14160 O  O   . HOH ZA 5 .   ? 42.301 56.326  -34.516  1.00 23.92 ? 408  HOH E O   1 
HETATM 14161 O  O   . HOH ZA 5 .   ? 54.155 38.477  -9.582   1.00 12.55 ? 418  HOH E O   1 
HETATM 14162 O  O   . HOH ZA 5 .   ? 37.527 62.766  -19.552  1.00 27.87 ? 419  HOH E O   1 
HETATM 14163 O  O   . HOH ZA 5 .   ? 65.107 47.347  -24.965  1.00 19.23 ? 430  HOH E O   1 
HETATM 14164 O  O   . HOH ZA 5 .   ? 62.684 44.884  -28.208  1.00 18.79 ? 442  HOH E O   1 
HETATM 14165 O  O   . HOH ZA 5 .   ? 38.350 60.948  -31.682  1.00 28.30 ? 452  HOH E O   1 
HETATM 14166 O  O   . HOH ZA 5 .   ? 56.805 52.276  -7.737   1.00 22.41 ? 455  HOH E O   1 
HETATM 14167 O  O   . HOH ZA 5 .   ? 53.213 44.080  -36.384  1.00 13.86 ? 459  HOH E O   1 
HETATM 14168 O  O   . HOH ZA 5 .   ? 58.242 61.999  -28.814  1.00 18.96 ? 460  HOH E O   1 
HETATM 14169 O  O   . HOH ZA 5 .   ? 65.497 59.898  -13.855  1.00 28.28 ? 468  HOH E O   1 
HETATM 14170 O  O   . HOH ZA 5 .   ? 36.880 51.617  -34.605  1.00 18.14 ? 479  HOH E O   1 
HETATM 14171 O  O   . HOH ZA 5 .   ? 56.657 42.825  -29.195  1.00 8.47  ? 499  HOH E O   1 
HETATM 14172 O  O   . HOH ZA 5 .   ? 43.159 39.753  -28.455  1.00 17.58 ? 500  HOH E O   1 
HETATM 14173 O  O   . HOH ZA 5 .   ? 55.661 41.740  -37.965  1.00 22.63 ? 502  HOH E O   1 
HETATM 14174 O  O   . HOH ZA 5 .   ? 54.145 65.462  -33.094  1.00 12.77 ? 511  HOH E O   1 
HETATM 14175 O  O   . HOH ZA 5 .   ? 37.254 53.043  -24.557  1.00 21.30 ? 525  HOH E O   1 
HETATM 14176 O  O   . HOH ZA 5 .   ? 61.517 44.066  -9.624   1.00 18.99 ? 531  HOH E O   1 
HETATM 14177 O  O   . HOH ZA 5 .   ? 33.726 47.575  -14.635  1.00 23.23 ? 532  HOH E O   1 
HETATM 14178 O  O   . HOH ZA 5 .   ? 35.061 35.315  -10.295  1.00 24.28 ? 539  HOH E O   1 
HETATM 14179 O  O   . HOH ZA 5 .   ? 61.941 39.478  -17.622  1.00 29.86 ? 545  HOH E O   1 
HETATM 14180 O  O   . HOH ZA 5 .   ? 60.918 59.594  -17.027  1.00 22.08 ? 558  HOH E O   1 
HETATM 14181 O  O   . HOH ZA 5 .   ? 46.773 37.450  -12.097  1.00 14.95 ? 573  HOH E O   1 
HETATM 14182 O  O   . HOH ZA 5 .   ? 30.855 42.470  -27.714  1.00 23.72 ? 574  HOH E O   1 
HETATM 14183 O  O   . HOH ZA 5 .   ? 68.355 41.117  -24.436  1.00 18.48 ? 576  HOH E O   1 
HETATM 14184 O  O   . HOH ZA 5 .   ? 45.279 54.038  -13.825  1.00 9.22  ? 588  HOH E O   1 
HETATM 14185 O  O   . HOH ZA 5 .   ? 38.095 58.122  -14.512  1.00 37.34 ? 592  HOH E O   1 
HETATM 14186 O  O   . HOH ZA 5 .   ? 54.779 65.992  -24.275  1.00 18.41 ? 595  HOH E O   1 
HETATM 14187 O  O   . HOH ZA 5 .   ? 60.523 36.740  -27.224  1.00 25.72 ? 598  HOH E O   1 
HETATM 14188 O  O   . HOH ZA 5 .   ? 54.849 59.206  -9.409   1.00 22.32 ? 599  HOH E O   1 
HETATM 14189 O  O   . HOH ZA 5 .   ? 51.957 71.511  -32.352  1.00 14.93 ? 601  HOH E O   1 
HETATM 14190 O  O   . HOH ZA 5 .   ? 52.941 56.238  -11.758  1.00 24.70 ? 603  HOH E O   1 
HETATM 14191 O  O   . HOH ZA 5 .   ? 55.591 41.228  -27.403  1.00 21.97 ? 624  HOH E O   1 
HETATM 14192 O  O   . HOH ZA 5 .   ? 63.663 44.315  -7.974   1.00 14.27 ? 640  HOH E O   1 
HETATM 14193 O  O   . HOH ZA 5 .   ? 51.625 58.828  -12.576  1.00 25.43 ? 660  HOH E O   1 
HETATM 14194 O  O   . HOH ZA 5 .   ? 44.810 56.477  -12.775  1.00 14.88 ? 667  HOH E O   1 
HETATM 14195 O  O   . HOH ZA 5 .   ? 70.346 48.153  -25.166  1.00 19.45 ? 672  HOH E O   1 
HETATM 14196 O  O   . HOH ZA 5 .   ? 34.616 35.602  -19.146  1.00 34.36 ? 680  HOH E O   1 
HETATM 14197 O  O   . HOH ZA 5 .   ? 47.574 67.202  -27.270  1.00 18.81 ? 689  HOH E O   1 
HETATM 14198 O  O   . HOH ZA 5 .   ? 67.953 50.587  -13.037  1.00 17.54 ? 705  HOH E O   1 
HETATM 14199 O  O   . HOH ZA 5 .   ? 59.605 35.815  -22.277  1.00 12.91 ? 707  HOH E O   1 
HETATM 14200 O  O   . HOH ZA 5 .   ? 61.840 48.459  -29.368  1.00 25.24 ? 725  HOH E O   1 
HETATM 14201 O  O   . HOH ZA 5 .   ? 38.792 62.873  -22.454  1.00 29.88 ? 728  HOH E O   1 
HETATM 14202 O  O   . HOH ZA 5 .   ? 37.444 34.651  -23.515  1.00 30.56 ? 746  HOH E O   1 
HETATM 14203 O  O   . HOH ZA 5 .   ? 31.561 37.226  -15.149  1.00 16.93 ? 747  HOH E O   1 
HETATM 14204 O  O   . HOH ZA 5 .   ? 38.385 50.618  -12.479  1.00 21.92 ? 756  HOH E O   1 
HETATM 14205 O  O   . HOH ZA 5 .   ? 53.028 63.007  -17.772  1.00 30.82 ? 763  HOH E O   1 
HETATM 14206 O  O   . HOH ZA 5 .   ? 34.828 43.081  -9.925   1.00 20.16 ? 766  HOH E O   1 
HETATM 14207 O  O   . HOH ZA 5 .   ? 46.802 53.210  -9.813   1.00 20.23 ? 774  HOH E O   1 
HETATM 14208 O  O   . HOH ZA 5 .   ? 62.637 38.516  -30.781  1.00 25.10 ? 775  HOH E O   1 
HETATM 14209 O  O   . HOH ZA 5 .   ? 50.693 58.055  -38.222  1.00 31.53 ? 808  HOH E O   1 
HETATM 14210 O  O   . HOH ZA 5 .   ? 57.429 62.471  -22.377  1.00 20.12 ? 810  HOH E O   1 
HETATM 14211 O  O   . HOH ZA 5 .   ? 56.492 64.871  -30.729  1.00 23.30 ? 815  HOH E O   1 
HETATM 14212 O  O   . HOH ZA 5 .   ? 58.056 46.661  -6.861   1.00 15.05 ? 819  HOH E O   1 
HETATM 14213 O  O   . HOH ZA 5 .   ? 42.297 37.648  -29.324  1.00 31.46 ? 827  HOH E O   1 
HETATM 14214 O  O   . HOH ZA 5 .   ? 60.554 40.048  -12.437  1.00 27.73 ? 828  HOH E O   1 
HETATM 14215 O  O   . HOH ZA 5 .   ? 44.687 46.996  -8.296   1.00 22.17 ? 843  HOH E O   1 
HETATM 14216 O  O   . HOH ZA 5 .   ? 59.910 61.616  -19.265  1.00 23.86 ? 845  HOH E O   1 
HETATM 14217 O  O   . HOH ZA 5 .   ? 48.882 55.052  -10.504  1.00 22.64 ? 847  HOH E O   1 
HETATM 14218 O  O   . HOH ZA 5 .   ? 41.476 64.141  -26.602  1.00 27.32 ? 856  HOH E O   1 
HETATM 14219 O  O   . HOH ZA 5 .   ? 52.902 38.010  -38.832  1.00 31.96 ? 878  HOH E O   1 
HETATM 14220 O  O   . HOH ZA 5 .   ? 63.159 58.598  -16.106  1.00 26.05 ? 886  HOH E O   1 
HETATM 14221 O  O   . HOH ZA 5 .   ? 55.853 41.896  -7.595   1.00 18.18 ? 906  HOH E O   1 
HETATM 14222 O  O   . HOH ZA 5 .   ? 52.519 60.800  -11.017  1.00 29.08 ? 909  HOH E O   1 
HETATM 14223 O  O   . HOH ZA 5 .   ? 54.947 38.662  -37.787  1.00 21.27 ? 911  HOH E O   1 
HETATM 14224 O  O   . HOH ZA 5 .   ? 55.150 35.975  -10.153  1.00 16.71 ? 912  HOH E O   1 
HETATM 14225 O  O   . HOH ZA 5 .   ? 52.644 50.871  -36.440  1.00 30.33 ? 916  HOH E O   1 
HETATM 14226 O  O   . HOH ZA 5 .   ? 61.434 42.386  -26.758  1.00 26.35 ? 941  HOH E O   1 
HETATM 14227 O  O   . HOH ZA 5 .   ? 36.946 43.309  -8.864   1.00 25.43 ? 943  HOH E O   1 
HETATM 14228 O  O   . HOH ZA 5 .   ? 40.974 31.669  -18.145  1.00 22.97 ? 947  HOH E O   1 
HETATM 14229 O  O   . HOH ZA 5 .   ? 42.077 53.232  -10.539  1.00 23.46 ? 957  HOH E O   1 
HETATM 14230 O  O   . HOH ZA 5 .   ? 62.211 46.960  -31.517  1.00 26.52 ? 960  HOH E O   1 
HETATM 14231 O  O   . HOH ZA 5 .   ? 34.410 35.805  -14.871  1.00 23.17 ? 973  HOH E O   1 
HETATM 14232 O  O   . HOH ZA 5 .   ? 31.479 35.684  -9.129   1.00 27.50 ? 979  HOH E O   1 
HETATM 14233 O  O   . HOH ZA 5 .   ? 28.464 39.706  -14.948  1.00 19.63 ? 989  HOH E O   1 
HETATM 14234 O  O   . HOH ZA 5 .   ? 69.114 53.973  -11.546  1.00 35.59 ? 999  HOH E O   1 
HETATM 14235 O  O   . HOH ZA 5 .   ? 61.293 42.369  -11.950  1.00 34.72 ? 1007 HOH E O   1 
HETATM 14236 O  O   . HOH ZA 5 .   ? 41.368 33.292  -11.383  1.00 31.97 ? 1013 HOH E O   1 
HETATM 14237 O  O   . HOH ZA 5 .   ? 31.383 46.039  -11.928  1.00 28.25 ? 1028 HOH E O   1 
HETATM 14238 O  O   . HOH ZA 5 .   ? 66.378 45.548  -8.679   1.00 14.55 ? 1040 HOH E O   1 
HETATM 14239 O  O   . HOH ZA 5 .   ? 52.340 51.386  -6.801   1.00 22.01 ? 1070 HOH E O   1 
HETATM 14240 O  O   . HOH ZA 5 .   ? 34.596 53.672  -33.785  1.00 37.23 ? 1085 HOH E O   1 
HETATM 14241 O  O   . HOH ZA 5 .   ? 63.327 46.635  -26.644  1.00 30.12 ? 1086 HOH E O   1 
HETATM 14242 O  O   . HOH ZA 5 .   ? 63.414 49.364  -4.724   1.00 20.19 ? 1098 HOH E O   1 
HETATM 14243 O  O   . HOH ZA 5 .   ? 66.657 36.211  -20.877  1.00 39.02 ? 1116 HOH E O   1 
HETATM 14244 O  O   . HOH ZA 5 .   ? 58.084 51.828  -32.810  1.00 24.05 ? 1141 HOH E O   1 
HETATM 14245 O  O   . HOH ZA 5 .   ? 47.032 48.911  -36.739  1.00 30.67 ? 1142 HOH E O   1 
HETATM 14246 O  O   . HOH ZA 5 .   ? 50.207 52.427  -8.031   1.00 20.47 ? 1145 HOH E O   1 
HETATM 14247 O  O   . HOH ZA 5 .   ? 64.506 53.728  -4.098   1.00 35.52 ? 1150 HOH E O   1 
HETATM 14248 O  O   . HOH ZA 5 .   ? 66.777 60.998  -11.823  1.00 36.55 ? 1158 HOH E O   1 
HETATM 14249 O  O   . HOH ZA 5 .   ? 62.627 35.260  -23.222  1.00 35.50 ? 1161 HOH E O   1 
HETATM 14250 O  O   . HOH ZA 5 .   ? 60.921 56.451  -29.687  1.00 27.61 ? 1164 HOH E O   1 
HETATM 14251 O  O   . HOH ZA 5 .   ? 46.404 52.936  -32.219  1.00 24.23 ? 1169 HOH E O   1 
HETATM 14252 O  O   . HOH ZA 5 .   ? 64.960 60.566  -5.124   1.00 37.47 ? 1187 HOH E O   1 
HETATM 14253 O  O   . HOH ZA 5 .   ? 58.788 51.330  -6.472   1.00 31.54 ? 1195 HOH E O   1 
HETATM 14254 O  O   . HOH ZA 5 .   ? 35.310 50.930  -24.290  1.00 22.08 ? 1197 HOH E O   1 
HETATM 14255 O  O   . HOH ZA 5 .   ? 41.967 42.118  -3.749   1.00 39.27 ? 1198 HOH E O   1 
HETATM 14256 O  O   . HOH ZA 5 .   ? 40.245 52.601  -8.482   1.00 39.86 ? 1203 HOH E O   1 
HETATM 14257 O  O   . HOH ZA 5 .   ? 58.697 56.427  -6.274   1.00 29.01 ? 1213 HOH E O   1 
HETATM 14258 O  O   . HOH ZA 5 .   ? 56.674 53.454  -29.801  1.00 25.73 ? 1221 HOH E O   1 
HETATM 14259 O  O   . HOH ZA 5 .   ? 41.834 31.573  -13.483  1.00 26.98 ? 1231 HOH E O   1 
HETATM 14260 O  O   . HOH ZA 5 .   ? 52.552 45.263  -7.057   1.00 26.27 ? 1237 HOH E O   1 
HETATM 14261 O  O   . HOH ZA 5 .   ? 67.463 49.448  -24.877  1.00 28.42 ? 1239 HOH E O   1 
HETATM 14262 O  O   . HOH ZA 5 .   ? 44.172 63.779  -23.429  1.00 23.21 ? 1284 HOH E O   1 
HETATM 14263 O  O   . HOH ZA 5 .   ? 53.051 54.897  -9.256   1.00 36.37 ? 1289 HOH E O   1 
HETATM 14264 O  O   . HOH ZA 5 .   ? 38.422 37.546  -4.161   1.00 36.76 ? 1293 HOH E O   1 
HETATM 14265 O  O   . HOH ZA 5 .   ? 58.179 45.579  -36.794  1.00 26.22 ? 1296 HOH E O   1 
HETATM 14266 O  O   . HOH ZA 5 .   ? 43.424 64.884  -28.169  1.00 24.31 ? 1301 HOH E O   1 
HETATM 14267 O  O   . HOH ZA 5 .   ? 44.061 31.961  -10.097  1.00 30.29 ? 1303 HOH E O   1 
HETATM 14268 O  O   . HOH ZA 5 .   ? 42.179 36.813  -6.516   1.00 38.86 ? 1332 HOH E O   1 
HETATM 14269 O  O   . HOH ZA 5 .   ? 35.578 60.569  -25.821  1.00 31.56 ? 1336 HOH E O   1 
HETATM 14270 O  O   . HOH ZA 5 .   ? 50.290 65.534  -19.163  1.00 31.43 ? 1340 HOH E O   1 
HETATM 14271 O  O   . HOH ZA 5 .   ? 45.922 60.751  -33.512  1.00 17.27 ? 1356 HOH E O   1 
HETATM 14272 O  O   . HOH ZA 5 .   ? 59.200 48.293  -5.292   1.00 23.12 ? 1359 HOH E O   1 
HETATM 14273 O  O   . HOH ZA 5 .   ? 56.641 40.924  -40.156  1.00 35.40 ? 1374 HOH E O   1 
HETATM 14274 O  O   . HOH ZA 5 .   ? 34.563 49.542  -12.583  1.00 24.85 ? 1384 HOH E O   1 
HETATM 14275 O  O   . HOH ZA 5 .   ? 53.620 54.083  -32.879  1.00 23.22 ? 1388 HOH E O   1 
HETATM 14276 O  O   . HOH ZA 5 .   ? 47.615 55.704  -32.408  1.00 27.97 ? 1399 HOH E O   1 
HETATM 14277 O  O   . HOH ZA 5 .   ? 49.468 33.962  -12.265  1.00 18.46 ? 1406 HOH E O   1 
HETATM 14278 O  O   . HOH ZA 5 .   ? 66.506 51.539  -0.627   1.00 40.07 ? 1420 HOH E O   1 
HETATM 14279 O  O   . HOH ZA 5 .   ? 45.052 62.694  -36.479  1.00 35.31 ? 1427 HOH E O   1 
HETATM 14280 O  O   . HOH ZA 5 .   ? 61.242 34.548  -17.417  1.00 34.11 ? 1430 HOH E O   1 
HETATM 14281 O  O   . HOH ZA 5 .   ? 35.384 36.017  -24.338  1.00 22.46 ? 1435 HOH E O   1 
HETATM 14282 O  O   . HOH ZA 5 .   ? 30.705 43.632  -12.382  1.00 22.85 ? 1439 HOH E O   1 
HETATM 14283 O  O   . HOH ZA 5 .   ? 58.900 53.112  -30.569  1.00 25.08 ? 1459 HOH E O   1 
HETATM 14284 O  O   . HOH ZA 5 .   ? 38.018 39.642  -31.203  1.00 27.85 ? 1473 HOH E O   1 
HETATM 14285 O  O   . HOH ZA 5 .   ? 37.512 46.281  -7.647   1.00 25.12 ? 1479 HOH E O   1 
HETATM 14286 O  O   . HOH ZA 5 .   ? 35.096 46.558  -33.028  1.00 45.18 ? 1491 HOH E O   1 
HETATM 14287 O  O   . HOH ZA 5 .   ? 65.174 48.886  -2.802   1.00 30.85 ? 1498 HOH E O   1 
HETATM 14288 O  O   . HOH ZA 5 .   ? 37.602 56.516  -25.073  1.00 23.56 ? 1513 HOH E O   1 
HETATM 14289 O  O   . HOH ZA 5 .   ? 41.112 65.657  -19.419  1.00 40.23 ? 1517 HOH E O   1 
HETATM 14290 O  O   . HOH ZA 5 .   ? 42.184 51.410  -34.629  1.00 25.25 ? 1530 HOH E O   1 
HETATM 14291 O  O   . HOH ZA 5 .   ? 70.716 53.848  -6.601   1.00 35.55 ? 1534 HOH E O   1 
HETATM 14292 O  O   . HOH ZA 5 .   ? 69.085 49.464  -8.007   1.00 24.97 ? 1568 HOH E O   1 
HETATM 14293 O  O   . HOH ZA 5 .   ? 67.492 39.644  -9.015   1.00 42.92 ? 1575 HOH E O   1 
HETATM 14294 O  O   . HOH ZA 5 .   ? 37.021 34.666  -19.818  1.00 27.18 ? 1588 HOH E O   1 
HETATM 14295 O  O   . HOH ZA 5 .   ? 53.115 57.522  -34.215  1.00 26.44 ? 1589 HOH E O   1 
HETATM 14296 O  O   . HOH ZA 5 .   ? 39.831 52.591  -11.496  1.00 37.84 ? 1594 HOH E O   1 
HETATM 14297 O  O   . HOH ZA 5 .   ? 58.623 40.956  -38.280  1.00 40.27 ? 1604 HOH E O   1 
HETATM 14298 O  O   . HOH ZA 5 .   ? 44.867 58.683  -36.204  1.00 32.44 ? 1607 HOH E O   1 
HETATM 14299 O  O   . HOH ZA 5 .   ? 41.832 41.706  -33.580  1.00 27.69 ? 1615 HOH E O   1 
HETATM 14300 O  O   . HOH ZA 5 .   ? 46.546 56.652  -34.547  1.00 41.15 ? 1624 HOH E O   1 
HETATM 14301 O  O   . HOH ZA 5 .   ? 40.154 54.146  -13.488  1.00 37.45 ? 1633 HOH E O   1 
HETATM 14302 O  O   . HOH ZA 5 .   ? 34.201 46.839  -8.890   1.00 29.46 ? 1635 HOH E O   1 
HETATM 14303 O  O   . HOH ZA 5 .   ? 34.710 36.299  -27.273  1.00 32.19 ? 1636 HOH E O   1 
HETATM 14304 O  O   . HOH ZA 5 .   ? 44.640 50.709  -34.429  1.00 25.20 ? 1639 HOH E O   1 
HETATM 14305 O  O   . HOH ZA 5 .   ? 33.605 48.850  -32.454  1.00 37.94 ? 1642 HOH E O   1 
HETATM 14306 O  O   . HOH ZA 5 .   ? 32.775 48.322  -10.789  1.00 31.34 ? 1646 HOH E O   1 
HETATM 14307 O  O   . HOH ZA 5 .   ? 40.665 68.294  -20.268  1.00 37.96 ? 1647 HOH E O   1 
HETATM 14308 O  O   . HOH ZA 5 .   ? 67.452 42.287  -8.671   1.00 31.06 ? 1649 HOH E O   1 
HETATM 14309 O  O   . HOH ZA 5 .   ? 43.865 67.076  -29.536  1.00 27.98 ? 1657 HOH E O   1 
HETATM 14310 O  O   . HOH ZA 5 .   ? 60.427 57.977  -8.263   1.00 23.72 ? 1665 HOH E O   1 
HETATM 14311 O  O   . HOH ZA 5 .   ? 38.713 45.748  -5.230   1.00 35.93 ? 1681 HOH E O   1 
HETATM 14312 O  O   . HOH ZA 5 .   ? 56.845 47.549  -37.045  1.00 27.34 ? 1686 HOH E O   1 
HETATM 14313 O  O   . HOH ZA 5 .   ? 43.587 66.062  -31.934  1.00 38.33 ? 1689 HOH E O   1 
HETATM 14314 O  O   . HOH ZA 5 .   ? 62.042 58.719  -6.346   1.00 41.03 ? 1692 HOH E O   1 
HETATM 14315 O  O   . HOH ZA 5 .   ? 44.720 64.469  -33.665  1.00 37.59 ? 1695 HOH E O   1 
HETATM 14316 O  O   . HOH ZA 5 .   ? 48.118 31.815  -11.927  1.00 18.21 ? 1699 HOH E O   1 
HETATM 14317 O  O   . HOH ZA 5 .   ? 61.153 39.042  -15.466  1.00 31.71 ? 1700 HOH E O   1 
HETATM 14318 O  O   . HOH ZA 5 .   ? 37.554 54.733  -23.494  1.00 33.12 ? 1704 HOH E O   1 
HETATM 14319 O  O   . HOH ZA 5 .   ? 67.835 46.018  -10.716  1.00 16.41 ? 1719 HOH E O   1 
HETATM 14320 O  O   . HOH AB 5 .   ? 18.014 -3.308  -37.725  1.00 10.27 ? 154  HOH F O   1 
HETATM 14321 O  O   . HOH AB 5 .   ? 22.240 0.149   -41.453  1.00 8.18  ? 155  HOH F O   1 
HETATM 14322 O  O   . HOH AB 5 .   ? 17.353 11.290  -37.001  1.00 17.11 ? 156  HOH F O   1 
HETATM 14323 O  O   . HOH AB 5 .   ? 10.426 6.547   -37.120  1.00 10.32 ? 157  HOH F O   1 
HETATM 14324 O  O   . HOH AB 5 .   ? 15.515 5.296   -41.052  1.00 19.51 ? 158  HOH F O   1 
HETATM 14325 O  O   . HOH AB 5 .   ? 12.853 -23.077 -38.650  1.00 8.85  ? 159  HOH F O   1 
HETATM 14326 O  O   . HOH AB 5 .   ? 3.084  -7.390  -44.901  1.00 15.21 ? 160  HOH F O   1 
HETATM 14327 O  O   . HOH AB 5 .   ? 26.973 3.670   -34.571  1.00 18.95 ? 161  HOH F O   1 
HETATM 14328 O  O   . HOH AB 5 .   ? 24.652 -6.481  -42.857  1.00 13.90 ? 162  HOH F O   1 
HETATM 14329 O  O   . HOH AB 5 .   ? 18.842 -4.974  -44.257  1.00 14.62 ? 163  HOH F O   1 
HETATM 14330 O  O   . HOH AB 5 .   ? 3.429  -12.724 -52.394  1.00 16.28 ? 164  HOH F O   1 
HETATM 14331 O  O   . HOH AB 5 .   ? 21.031 3.591   -38.715  1.00 13.74 ? 165  HOH F O   1 
HETATM 14332 O  O   . HOH AB 5 .   ? 15.489 10.051  -39.200  1.00 16.51 ? 166  HOH F O   1 
HETATM 14333 O  O   . HOH AB 5 .   ? 8.356  0.832   -47.943  1.00 12.49 ? 172  HOH F O   1 
HETATM 14334 O  O   . HOH AB 5 .   ? 26.021 -6.571  -22.158  1.00 17.21 ? 178  HOH F O   1 
HETATM 14335 O  O   . HOH AB 5 .   ? 20.208 -6.280  -49.967  1.00 15.88 ? 180  HOH F O   1 
HETATM 14336 O  O   . HOH AB 5 .   ? 10.168 -22.720 -29.677  1.00 12.47 ? 182  HOH F O   1 
HETATM 14337 O  O   . HOH AB 5 .   ? 23.585 -6.831  -46.474  1.00 16.50 ? 202  HOH F O   1 
HETATM 14338 O  O   . HOH AB 5 .   ? 24.162 -6.611  -29.017  1.00 10.37 ? 204  HOH F O   1 
HETATM 14339 O  O   . HOH AB 5 .   ? 21.124 4.579   -35.654  1.00 14.20 ? 215  HOH F O   1 
HETATM 14340 O  O   . HOH AB 5 .   ? 12.167 -8.622  -53.360  1.00 12.58 ? 218  HOH F O   1 
HETATM 14341 O  O   . HOH AB 5 .   ? -0.022 -3.702  -45.077  1.00 15.08 ? 227  HOH F O   1 
HETATM 14342 O  O   . HOH AB 5 .   ? 16.317 -0.150  -44.658  1.00 17.79 ? 248  HOH F O   1 
HETATM 14343 O  O   . HOH AB 5 .   ? 7.564  -9.948  -27.079  1.00 11.45 ? 252  HOH F O   1 
HETATM 14344 O  O   . HOH AB 5 .   ? 8.700  -4.113  -33.231  1.00 13.60 ? 274  HOH F O   1 
HETATM 14345 O  O   . HOH AB 5 .   ? 16.869 8.083   -32.819  1.00 7.37  ? 275  HOH F O   1 
HETATM 14346 O  O   . HOH AB 5 .   ? -0.412 -9.856  -48.634  1.00 15.18 ? 281  HOH F O   1 
HETATM 14347 O  O   . HOH AB 5 .   ? 25.951 -5.437  -30.723  1.00 14.54 ? 295  HOH F O   1 
HETATM 14348 O  O   . HOH AB 5 .   ? 29.531 -8.544  -44.107  1.00 24.23 ? 315  HOH F O   1 
HETATM 14349 O  O   . HOH AB 5 .   ? 28.626 -25.086 -50.026  1.00 33.58 ? 334  HOH F O   1 
HETATM 14350 O  O   . HOH AB 5 .   ? 26.369 0.319   -24.751  1.00 24.44 ? 342  HOH F O   1 
HETATM 14351 O  O   . HOH AB 5 .   ? 1.129  -9.977  -50.662  1.00 16.78 ? 344  HOH F O   1 
HETATM 14352 O  O   . HOH AB 5 .   ? 1.953  -15.440 -41.922  1.00 29.88 ? 346  HOH F O   1 
HETATM 14353 O  O   . HOH AB 5 .   ? 3.249  -8.951  -32.750  1.00 16.31 ? 358  HOH F O   1 
HETATM 14354 O  O   . HOH AB 5 .   ? 13.965 -19.592 -49.881  1.00 25.88 ? 364  HOH F O   1 
HETATM 14355 O  O   . HOH AB 5 .   ? 9.603  -8.370  -26.692  1.00 19.30 ? 373  HOH F O   1 
HETATM 14356 O  O   . HOH AB 5 .   ? 30.276 -15.063 -32.361  1.00 22.64 ? 394  HOH F O   1 
HETATM 14357 O  O   . HOH AB 5 .   ? 8.499  2.628   -39.316  1.00 22.80 ? 411  HOH F O   1 
HETATM 14358 O  O   . HOH AB 5 .   ? 8.349  -21.469 -34.874  1.00 15.75 ? 420  HOH F O   1 
HETATM 14359 O  O   . HOH AB 5 .   ? 24.373 0.614   -48.376  1.00 23.22 ? 440  HOH F O   1 
HETATM 14360 O  O   . HOH AB 5 .   ? 28.943 3.165   -37.205  1.00 20.66 ? 445  HOH F O   1 
HETATM 14361 O  O   . HOH AB 5 .   ? 8.497  6.090   -28.390  1.00 16.20 ? 462  HOH F O   1 
HETATM 14362 O  O   . HOH AB 5 .   ? 9.455  -1.766  -27.239  1.00 26.54 ? 470  HOH F O   1 
HETATM 14363 O  O   . HOH AB 5 .   ? 26.396 -26.467 -41.003  1.00 18.82 ? 476  HOH F O   1 
HETATM 14364 O  O   . HOH AB 5 .   ? 16.753 -24.550 -47.369  1.00 22.20 ? 481  HOH F O   1 
HETATM 14365 O  O   . HOH AB 5 .   ? 32.804 -16.411 -43.546  1.00 20.79 ? 484  HOH F O   1 
HETATM 14366 O  O   . HOH AB 5 .   ? 32.339 -7.451  -36.806  1.00 26.45 ? 486  HOH F O   1 
HETATM 14367 O  O   . HOH AB 5 .   ? 28.872 2.098   -30.622  1.00 26.75 ? 495  HOH F O   1 
HETATM 14368 O  O   . HOH AB 5 .   ? 2.757  -5.044  -43.519  1.00 16.26 ? 498  HOH F O   1 
HETATM 14369 O  O   . HOH AB 5 .   ? 6.271  -1.067  -45.388  1.00 21.08 ? 509  HOH F O   1 
HETATM 14370 O  O   . HOH AB 5 .   ? 20.204 -23.364 -45.471  1.00 16.42 ? 514  HOH F O   1 
HETATM 14371 O  O   . HOH AB 5 .   ? 22.759 3.323   -33.894  1.00 27.38 ? 516  HOH F O   1 
HETATM 14372 O  O   . HOH AB 5 .   ? 19.839 -10.553 -25.978  1.00 16.78 ? 523  HOH F O   1 
HETATM 14373 O  O   . HOH AB 5 .   ? 2.610  -14.506 -36.164  1.00 28.65 ? 536  HOH F O   1 
HETATM 14374 O  O   . HOH AB 5 .   ? 21.054 -0.796  -43.777  1.00 12.10 ? 551  HOH F O   1 
HETATM 14375 O  O   . HOH AB 5 .   ? 6.355  0.899   -42.559  1.00 28.54 ? 565  HOH F O   1 
HETATM 14376 O  O   . HOH AB 5 .   ? 24.370 -17.026 -28.910  1.00 20.40 ? 571  HOH F O   1 
HETATM 14377 O  O   . HOH AB 5 .   ? 11.695 -6.383  -29.927  1.00 21.63 ? 577  HOH F O   1 
HETATM 14378 O  O   . HOH AB 5 .   ? 24.540 8.065   -27.747  1.00 42.36 ? 587  HOH F O   1 
HETATM 14379 O  O   . HOH AB 5 .   ? 28.537 -3.744  -34.220  1.00 28.04 ? 593  HOH F O   1 
HETATM 14380 O  O   . HOH AB 5 .   ? 17.846 -1.324  -26.986  1.00 13.50 ? 594  HOH F O   1 
HETATM 14381 O  O   . HOH AB 5 .   ? 14.012 -4.878  -29.080  1.00 13.48 ? 607  HOH F O   1 
HETATM 14382 O  O   . HOH AB 5 .   ? 8.618  -22.499 -38.589  1.00 23.55 ? 609  HOH F O   1 
HETATM 14383 O  O   . HOH AB 5 .   ? 19.803 10.041  -37.344  1.00 12.15 ? 614  HOH F O   1 
HETATM 14384 O  O   . HOH AB 5 .   ? 21.114 -4.790  -45.747  1.00 15.85 ? 618  HOH F O   1 
HETATM 14385 O  O   . HOH AB 5 .   ? 20.394 9.419   -34.770  1.00 16.00 ? 627  HOH F O   1 
HETATM 14386 O  O   . HOH AB 5 .   ? 10.560 -5.739  -32.384  1.00 25.30 ? 634  HOH F O   1 
HETATM 14387 O  O   . HOH AB 5 .   ? 11.655 -18.136 -23.434  1.00 16.06 ? 637  HOH F O   1 
HETATM 14388 O  O   . HOH AB 5 .   ? 18.270 10.113  -33.371  1.00 14.65 ? 638  HOH F O   1 
HETATM 14389 O  O   . HOH AB 5 .   ? 11.569 -9.672  -55.710  1.00 17.77 ? 652  HOH F O   1 
HETATM 14390 O  O   . HOH AB 5 .   ? 15.623 7.763   -30.483  1.00 25.07 ? 674  HOH F O   1 
HETATM 14391 O  O   . HOH AB 5 .   ? 22.749 -22.354 -46.161  1.00 24.15 ? 683  HOH F O   1 
HETATM 14392 O  O   . HOH AB 5 .   ? 25.097 5.177   -34.726  1.00 23.01 ? 700  HOH F O   1 
HETATM 14393 O  O   . HOH AB 5 .   ? 28.365 -6.364  -41.105  1.00 27.33 ? 703  HOH F O   1 
HETATM 14394 O  O   . HOH AB 5 .   ? 7.981  -4.684  -57.717  1.00 23.72 ? 706  HOH F O   1 
HETATM 14395 O  O   . HOH AB 5 .   ? -2.086 -12.026 -49.121  1.00 26.20 ? 713  HOH F O   1 
HETATM 14396 O  O   . HOH AB 5 .   ? 17.896 -5.075  -25.388  1.00 22.99 ? 715  HOH F O   1 
HETATM 14397 O  O   . HOH AB 5 .   ? 26.001 -14.367 -26.200  1.00 26.44 ? 719  HOH F O   1 
HETATM 14398 O  O   . HOH AB 5 .   ? 10.820 6.509   -39.846  1.00 25.77 ? 720  HOH F O   1 
HETATM 14399 O  O   . HOH AB 5 .   ? 34.359 -15.868 -45.305  1.00 25.79 ? 721  HOH F O   1 
HETATM 14400 O  O   . HOH AB 5 .   ? 16.912 6.680   -44.999  1.00 25.07 ? 730  HOH F O   1 
HETATM 14401 O  O   . HOH AB 5 .   ? 30.133 -6.661  -32.295  1.00 22.84 ? 743  HOH F O   1 
HETATM 14402 O  O   . HOH AB 5 .   ? 10.732 -22.806 -35.738  1.00 21.18 ? 749  HOH F O   1 
HETATM 14403 O  O   . HOH AB 5 .   ? 21.875 10.043  -41.475  1.00 16.86 ? 765  HOH F O   1 
HETATM 14404 O  O   . HOH AB 5 .   ? 18.710 4.088   -31.664  1.00 23.07 ? 770  HOH F O   1 
HETATM 14405 O  O   . HOH AB 5 .   ? 8.224  5.186   -37.806  1.00 19.99 ? 784  HOH F O   1 
HETATM 14406 O  O   . HOH AB 5 .   ? 30.201 -16.596 -46.074  1.00 23.34 ? 788  HOH F O   1 
HETATM 14407 O  O   . HOH AB 5 .   ? 20.332 -3.179  -23.711  1.00 27.90 ? 798  HOH F O   1 
HETATM 14408 O  O   . HOH AB 5 .   ? 2.565  -3.104  -36.349  1.00 32.64 ? 800  HOH F O   1 
HETATM 14409 O  O   . HOH AB 5 .   ? 20.029 -15.374 -24.392  1.00 17.58 ? 802  HOH F O   1 
HETATM 14410 O  O   . HOH AB 5 .   ? 6.333  5.433   -32.612  1.00 25.13 ? 811  HOH F O   1 
HETATM 14411 O  O   . HOH AB 5 .   ? 25.240 -4.065  -43.677  1.00 22.27 ? 846  HOH F O   1 
HETATM 14412 O  O   . HOH AB 5 .   ? 10.092 -5.745  -28.085  1.00 27.53 ? 860  HOH F O   1 
HETATM 14413 O  O   . HOH AB 5 .   ? 28.235 -5.220  -32.147  1.00 19.86 ? 870  HOH F O   1 
HETATM 14414 O  O   . HOH AB 5 .   ? 8.611  7.029   -41.435  1.00 17.95 ? 871  HOH F O   1 
HETATM 14415 O  O   . HOH AB 5 .   ? 2.281  -18.673 -42.290  1.00 28.53 ? 898  HOH F O   1 
HETATM 14416 O  O   . HOH AB 5 .   ? 38.058 -18.783 -38.688  1.00 23.35 ? 899  HOH F O   1 
HETATM 14417 O  O   . HOH AB 5 .   ? 37.372 -15.443 -43.325  1.00 29.63 ? 910  HOH F O   1 
HETATM 14418 O  O   . HOH AB 5 .   ? 28.140 -3.108  -37.619  1.00 26.95 ? 970  HOH F O   1 
HETATM 14419 O  O   . HOH AB 5 .   ? 16.729 4.950   -43.139  1.00 27.22 ? 971  HOH F O   1 
HETATM 14420 O  O   . HOH AB 5 .   ? 5.485  -14.323 -24.635  1.00 26.72 ? 977  HOH F O   1 
HETATM 14421 O  O   . HOH AB 5 .   ? 19.584 -0.215  -24.723  1.00 29.66 ? 982  HOH F O   1 
HETATM 14422 O  O   . HOH AB 5 .   ? 1.250  -16.049 -49.407  1.00 29.38 ? 984  HOH F O   1 
HETATM 14423 O  O   . HOH AB 5 .   ? 8.922  -21.208 -22.525  1.00 35.36 ? 987  HOH F O   1 
HETATM 14424 O  O   . HOH AB 5 .   ? 30.348 -12.850 -38.098  1.00 29.83 ? 990  HOH F O   1 
HETATM 14425 O  O   . HOH AB 5 .   ? 7.029  -20.572 -36.910  1.00 21.05 ? 1025 HOH F O   1 
HETATM 14426 O  O   . HOH AB 5 .   ? 32.319 -21.094 -40.316  1.00 26.34 ? 1026 HOH F O   1 
HETATM 14427 O  O   . HOH AB 5 .   ? 21.047 6.793   -33.956  1.00 26.15 ? 1041 HOH F O   1 
HETATM 14428 O  O   . HOH AB 5 .   ? 18.741 -8.625  -24.204  1.00 23.92 ? 1059 HOH F O   1 
HETATM 14429 O  O   . HOH AB 5 .   ? 11.084 -3.736  -25.887  1.00 36.42 ? 1060 HOH F O   1 
HETATM 14430 O  O   . HOH AB 5 .   ? 6.364  5.557   -29.800  1.00 33.95 ? 1062 HOH F O   1 
HETATM 14431 O  O   . HOH AB 5 .   ? 14.000 2.678   -42.461  1.00 23.50 ? 1081 HOH F O   1 
HETATM 14432 O  O   . HOH AB 5 .   ? 4.362  -0.700  -47.618  1.00 19.78 ? 1111 HOH F O   1 
HETATM 14433 O  O   . HOH AB 5 .   ? 8.340  -11.547 -57.660  1.00 27.55 ? 1119 HOH F O   1 
HETATM 14434 O  O   . HOH AB 5 .   ? 9.413  -2.517  -53.674  1.00 29.49 ? 1123 HOH F O   1 
HETATM 14435 O  O   . HOH AB 5 .   ? 32.166 -15.293 -47.487  1.00 26.82 ? 1132 HOH F O   1 
HETATM 14436 O  O   . HOH AB 5 .   ? 37.204 -21.399 -40.227  1.00 29.92 ? 1163 HOH F O   1 
HETATM 14437 O  O   . HOH AB 5 .   ? -0.380 -1.924  -41.341  1.00 20.93 ? 1182 HOH F O   1 
HETATM 14438 O  O   . HOH AB 5 .   ? 4.023  -15.330 -53.699  1.00 23.48 ? 1199 HOH F O   1 
HETATM 14439 O  O   . HOH AB 5 .   ? 13.764 -3.888  -26.592  1.00 24.35 ? 1207 HOH F O   1 
HETATM 14440 O  O   . HOH AB 5 .   ? 21.965 -11.710 -25.227  1.00 24.83 ? 1211 HOH F O   1 
HETATM 14441 O  O   . HOH AB 5 .   ? 10.080 -15.829 -23.948  1.00 21.29 ? 1212 HOH F O   1 
HETATM 14442 O  O   . HOH AB 5 .   ? 17.403 -7.375  -26.211  1.00 20.08 ? 1215 HOH F O   1 
HETATM 14443 O  O   . HOH AB 5 .   ? 6.374  -16.377 -54.133  1.00 35.69 ? 1220 HOH F O   1 
HETATM 14444 O  O   . HOH AB 5 .   ? 2.657  -14.795 -33.461  1.00 31.81 ? 1234 HOH F O   1 
HETATM 14445 O  O   . HOH AB 5 .   ? 3.537  -0.119  -34.663  1.00 27.14 ? 1235 HOH F O   1 
HETATM 14446 O  O   . HOH AB 5 .   ? 14.320 6.783   -45.293  1.00 22.10 ? 1240 HOH F O   1 
HETATM 14447 O  O   . HOH AB 5 .   ? -4.289 -13.677 -48.190  1.00 23.40 ? 1256 HOH F O   1 
HETATM 14448 O  O   . HOH AB 5 .   ? 4.499  -10.087 -30.851  1.00 40.17 ? 1257 HOH F O   1 
HETATM 14449 O  O   . HOH AB 5 .   ? 7.464  -6.773  -31.979  1.00 33.93 ? 1272 HOH F O   1 
HETATM 14450 O  O   . HOH AB 5 .   ? 32.185 -17.461 -50.476  1.00 45.32 ? 1273 HOH F O   1 
HETATM 14451 O  O   . HOH AB 5 .   ? 23.735 -13.671 -24.702  1.00 23.41 ? 1276 HOH F O   1 
HETATM 14452 O  O   . HOH AB 5 .   ? 11.028 -15.707 -54.756  1.00 26.17 ? 1282 HOH F O   1 
HETATM 14453 O  O   . HOH AB 5 .   ? 27.763 2.342   -26.863  1.00 35.13 ? 1287 HOH F O   1 
HETATM 14454 O  O   . HOH AB 5 .   ? 7.920  -15.707 -56.401  1.00 33.75 ? 1298 HOH F O   1 
HETATM 14455 O  O   . HOH AB 5 .   ? 8.080  -17.311 -52.115  1.00 33.11 ? 1302 HOH F O   1 
HETATM 14456 O  O   . HOH AB 5 .   ? 5.148  1.268   -53.631  1.00 30.66 ? 1318 HOH F O   1 
HETATM 14457 O  O   . HOH AB 5 .   ? 30.993 -19.725 -51.642  1.00 45.43 ? 1329 HOH F O   1 
HETATM 14458 O  O   . HOH AB 5 .   ? 8.645  -18.407 -49.967  1.00 29.17 ? 1358 HOH F O   1 
HETATM 14459 O  O   . HOH AB 5 .   ? 10.781 3.902   -40.564  1.00 30.29 ? 1371 HOH F O   1 
HETATM 14460 O  O   . HOH AB 5 .   ? 9.205  3.478   -44.067  1.00 27.29 ? 1392 HOH F O   1 
HETATM 14461 O  O   . HOH AB 5 .   ? 6.832  0.489   -51.865  1.00 34.80 ? 1403 HOH F O   1 
HETATM 14462 O  O   . HOH AB 5 .   ? 23.359 -13.301 -49.605  1.00 20.68 ? 1410 HOH F O   1 
HETATM 14463 O  O   . HOH AB 5 .   ? 20.950 -7.542  -23.253  1.00 30.73 ? 1423 HOH F O   1 
HETATM 14464 O  O   . HOH AB 5 .   ? 5.168  -21.319 -51.038  1.00 33.79 ? 1437 HOH F O   1 
HETATM 14465 O  O   . HOH AB 5 .   ? 22.258 0.497   -24.493  1.00 23.84 ? 1445 HOH F O   1 
HETATM 14466 O  O   . HOH AB 5 .   ? 33.048 -13.627 -37.821  1.00 47.66 ? 1470 HOH F O   1 
HETATM 14467 O  O   . HOH AB 5 .   ? 3.223  -22.605 -49.604  1.00 42.83 ? 1480 HOH F O   1 
HETATM 14468 O  O   . HOH AB 5 .   ? 24.510 2.065   -25.787  1.00 28.82 ? 1495 HOH F O   1 
HETATM 14469 O  O   . HOH AB 5 .   ? 26.117 -10.648 -22.915  1.00 16.90 ? 1550 HOH F O   1 
HETATM 14470 O  O   . HOH AB 5 .   ? -0.032 -19.176 -48.118  1.00 35.52 ? 1565 HOH F O   1 
HETATM 14471 O  O   . HOH AB 5 .   ? 24.010 -37.108 -43.371  1.00 33.21 ? 1598 HOH F O   1 
HETATM 14472 O  O   . HOH AB 5 .   ? 22.732 -16.149 -24.273  1.00 30.85 ? 1599 HOH F O   1 
HETATM 14473 O  O   . HOH AB 5 .   ? 41.672 -15.934 -42.289  1.00 38.24 ? 1602 HOH F O   1 
HETATM 14474 O  O   . HOH AB 5 .   ? 2.002  -19.724 -37.392  1.00 32.62 ? 1608 HOH F O   1 
HETATM 14475 O  O   . HOH AB 5 .   ? 28.618 -26.226 -45.565  1.00 33.24 ? 1614 HOH F O   1 
HETATM 14476 O  O   . HOH AB 5 .   ? 4.270  -1.897  -44.106  1.00 30.95 ? 1620 HOH F O   1 
HETATM 14477 O  O   . HOH AB 5 .   ? -0.938 -20.181 -37.365  1.00 44.86 ? 1627 HOH F O   1 
HETATM 14478 O  O   . HOH AB 5 .   ? -1.021 -22.502 -38.829  1.00 26.93 ? 1661 HOH F O   1 
HETATM 14479 O  O   . HOH AB 5 .   ? -1.444 -23.606 -42.133  1.00 40.90 ? 1662 HOH F O   1 
HETATM 14480 O  O   . HOH AB 5 .   ? 28.901 -3.133  -30.057  1.00 32.75 ? 1668 HOH F O   1 
HETATM 14481 O  O   . HOH AB 5 .   ? 24.151 3.597   -41.348  1.00 33.23 ? 1707 HOH F O   1 
HETATM 14482 O  O   . HOH AB 5 .   ? 23.271 7.055   -42.000  1.00 33.41 ? 1715 HOH F O   1 
HETATM 14483 O  O   . HOH AB 5 .   ? 7.082  2.023   -44.906  1.00 19.84 ? 1727 HOH F O   1 
HETATM 14484 O  O   . HOH AB 5 .   ? 18.772 -13.740 -52.824  1.00 26.32 ? 1733 HOH F O   1 
HETATM 14485 O  O   . HOH BB 5 .   ? 14.156 -25.096 -39.961  1.00 12.10 ? 167  HOH G O   1 
HETATM 14486 O  O   . HOH BB 5 .   ? 10.345 -24.942 -31.481  1.00 16.92 ? 168  HOH G O   1 
HETATM 14487 O  O   . HOH BB 5 .   ? 33.229 -27.923 -26.073  1.00 25.17 ? 257  HOH G O   1 
HETATM 14488 O  O   . HOH BB 5 .   ? 18.570 -20.120 -21.484  1.00 16.90 ? 270  HOH G O   1 
HETATM 14489 O  O   . HOH BB 5 .   ? 0.848  -41.789 -32.656  1.00 25.65 ? 292  HOH G O   1 
HETATM 14490 O  O   . HOH BB 5 .   ? 31.730 -27.204 -18.849  1.00 17.33 ? 306  HOH G O   1 
HETATM 14491 O  O   . HOH BB 5 .   ? 26.541 -28.870 -31.676  1.00 14.30 ? 355  HOH G O   1 
HETATM 14492 O  O   . HOH BB 5 .   ? 19.784 -42.097 -37.433  1.00 15.77 ? 367  HOH G O   1 
HETATM 14493 O  O   . HOH BB 5 .   ? 16.962 -43.913 -28.113  1.00 16.13 ? 381  HOH G O   1 
HETATM 14494 O  O   . HOH BB 5 .   ? 28.097 -28.190 -21.731  1.00 17.57 ? 396  HOH G O   1 
HETATM 14495 O  O   . HOH BB 5 .   ? 19.720 -29.446 -43.560  1.00 16.56 ? 406  HOH G O   1 
HETATM 14496 O  O   . HOH BB 5 .   ? 8.034  -26.257 -34.217  1.00 22.62 ? 437  HOH G O   1 
HETATM 14497 O  O   . HOH BB 5 .   ? 3.694  -35.937 -39.190  1.00 31.54 ? 447  HOH G O   1 
HETATM 14498 O  O   . HOH BB 5 .   ? -4.524 -45.335 -28.905  1.00 24.93 ? 454  HOH G O   1 
HETATM 14499 O  O   . HOH BB 5 .   ? 24.579 -45.361 -36.297  1.00 21.72 ? 487  HOH G O   1 
HETATM 14500 O  O   . HOH BB 5 .   ? 24.742 -32.625 -26.722  1.00 23.27 ? 510  HOH G O   1 
HETATM 14501 O  O   . HOH BB 5 .   ? 28.411 -30.856 -32.571  1.00 29.75 ? 519  HOH G O   1 
HETATM 14502 O  O   . HOH BB 5 .   ? 3.920  -49.714 -27.250  1.00 27.67 ? 524  HOH G O   1 
HETATM 14503 O  O   . HOH BB 5 .   ? 27.176 -34.170 -26.137  1.00 22.41 ? 546  HOH G O   1 
HETATM 14504 O  O   . HOH BB 5 .   ? 24.832 -25.444 -20.457  1.00 22.73 ? 557  HOH G O   1 
HETATM 14505 O  O   . HOH BB 5 .   ? 1.580  -43.722 -34.521  1.00 30.28 ? 564  HOH G O   1 
HETATM 14506 O  O   . HOH BB 5 .   ? 17.203 -41.473 -38.281  1.00 33.82 ? 575  HOH G O   1 
HETATM 14507 O  O   . HOH BB 5 .   ? 18.318 -24.960 -13.752  1.00 31.94 ? 591  HOH G O   1 
HETATM 14508 O  O   . HOH BB 5 .   ? 25.283 -35.913 -36.226  1.00 24.34 ? 611  HOH G O   1 
HETATM 14509 O  O   . HOH BB 5 .   ? 27.869 -40.739 -28.530  1.00 17.21 ? 625  HOH G O   1 
HETATM 14510 O  O   . HOH BB 5 .   ? 27.408 -39.678 -30.867  1.00 20.21 ? 647  HOH G O   1 
HETATM 14511 O  O   . HOH BB 5 .   ? 22.705 -50.786 -32.289  1.00 17.82 ? 675  HOH G O   1 
HETATM 14512 O  O   . HOH BB 5 .   ? 18.111 -53.570 -41.236  1.00 16.90 ? 697  HOH G O   1 
HETATM 14513 O  O   . HOH BB 5 .   ? -4.325 -37.147 -27.261  1.00 26.67 ? 714  HOH G O   1 
HETATM 14514 O  O   . HOH BB 5 .   ? 26.210 -34.730 -15.634  1.00 24.79 ? 768  HOH G O   1 
HETATM 14515 O  O   . HOH BB 5 .   ? 17.583 -26.745 -46.437  1.00 26.88 ? 773  HOH G O   1 
HETATM 14516 O  O   . HOH BB 5 .   ? 25.972 -31.170 -37.513  1.00 27.84 ? 777  HOH G O   1 
HETATM 14517 O  O   . HOH BB 5 .   ? 26.861 -34.966 -17.988  1.00 23.67 ? 796  HOH G O   1 
HETATM 14518 O  O   . HOH BB 5 .   ? 13.245 -18.551 -16.941  1.00 42.71 ? 809  HOH G O   1 
HETATM 14519 O  O   . HOH BB 5 .   ? 25.179 -48.223 -38.020  1.00 23.69 ? 817  HOH G O   1 
HETATM 14520 O  O   . HOH BB 5 .   ? 8.465  -39.348 -41.290  1.00 24.16 ? 822  HOH G O   1 
HETATM 14521 O  O   . HOH BB 5 .   ? 1.448  -35.476 -36.773  1.00 44.40 ? 825  HOH G O   1 
HETATM 14522 O  O   . HOH BB 5 .   ? 6.590  -33.722 -17.068  1.00 25.99 ? 831  HOH G O   1 
HETATM 14523 O  O   . HOH BB 5 .   ? 11.687 -19.184 -20.476  1.00 36.01 ? 835  HOH G O   1 
HETATM 14524 O  O   . HOH BB 5 .   ? 18.160 -16.772 -22.929  1.00 29.77 ? 839  HOH G O   1 
HETATM 14525 O  O   . HOH BB 5 .   ? 9.184  -39.552 -20.186  1.00 29.69 ? 848  HOH G O   1 
HETATM 14526 O  O   . HOH BB 5 .   ? 11.730 -50.134 -39.252  1.00 30.04 ? 857  HOH G O   1 
HETATM 14527 O  O   . HOH BB 5 .   ? 23.957 -49.578 -28.730  1.00 24.71 ? 859  HOH G O   1 
HETATM 14528 O  O   . HOH BB 5 .   ? 24.239 -24.622 -17.939  1.00 19.21 ? 873  HOH G O   1 
HETATM 14529 O  O   . HOH BB 5 .   ? 17.964 -28.673 -14.199  1.00 35.64 ? 876  HOH G O   1 
HETATM 14530 O  O   . HOH BB 5 .   ? 13.316 -24.681 -20.108  1.00 40.43 ? 881  HOH G O   1 
HETATM 14531 O  O   . HOH BB 5 .   ? 12.853 -43.743 -37.624  1.00 28.75 ? 883  HOH G O   1 
HETATM 14532 O  O   . HOH BB 5 .   ? 9.871  -50.826 -33.219  1.00 35.54 ? 890  HOH G O   1 
HETATM 14533 O  O   . HOH BB 5 .   ? 22.814 -45.607 -44.016  1.00 30.56 ? 904  HOH G O   1 
HETATM 14534 O  O   . HOH BB 5 .   ? 1.856  -46.186 -29.808  1.00 27.78 ? 907  HOH G O   1 
HETATM 14535 O  O   . HOH BB 5 .   ? 28.799 -30.189 -25.723  1.00 23.50 ? 921  HOH G O   1 
HETATM 14536 O  O   . HOH BB 5 .   ? 28.018 -23.916 -16.060  1.00 33.42 ? 927  HOH G O   1 
HETATM 14537 O  O   . HOH BB 5 .   ? 14.858 -41.857 -36.732  1.00 28.70 ? 962  HOH G O   1 
HETATM 14538 O  O   . HOH BB 5 .   ? 21.015 -37.885 -15.670  1.00 32.41 ? 974  HOH G O   1 
HETATM 14539 O  O   . HOH BB 5 .   ? 12.601 -29.282 -36.965  1.00 32.89 ? 976  HOH G O   1 
HETATM 14540 O  O   . HOH BB 5 .   ? 33.425 -25.994 -24.631  1.00 31.05 ? 993  HOH G O   1 
HETATM 14541 O  O   . HOH BB 5 .   ? 13.320 -44.358 -22.597  1.00 22.27 ? 1005 HOH G O   1 
HETATM 14542 O  O   . HOH BB 5 .   ? 12.810 -40.876 -17.130  1.00 30.45 ? 1008 HOH G O   1 
HETATM 14543 O  O   . HOH BB 5 .   ? 30.306 -33.630 -14.876  1.00 26.73 ? 1009 HOH G O   1 
HETATM 14544 O  O   . HOH BB 5 .   ? 14.861 -53.479 -26.900  1.00 27.63 ? 1023 HOH G O   1 
HETATM 14545 O  O   . HOH BB 5 .   ? 34.197 -31.708 -27.565  1.00 37.82 ? 1031 HOH G O   1 
HETATM 14546 O  O   . HOH BB 5 .   ? 17.385 -41.831 -40.992  1.00 28.47 ? 1032 HOH G O   1 
HETATM 14547 O  O   . HOH BB 5 .   ? 28.364 -37.263 -20.623  1.00 24.55 ? 1066 HOH G O   1 
HETATM 14548 O  O   . HOH BB 5 .   ? 29.030 -23.335 -25.462  1.00 23.12 ? 1072 HOH G O   1 
HETATM 14549 O  O   . HOH BB 5 .   ? 11.860 -51.104 -26.817  1.00 34.23 ? 1083 HOH G O   1 
HETATM 14550 O  O   . HOH BB 5 .   ? 8.103  -34.423 -43.516  1.00 39.90 ? 1087 HOH G O   1 
HETATM 14551 O  O   . HOH BB 5 .   ? 10.998 -41.198 -21.386  1.00 29.78 ? 1092 HOH G O   1 
HETATM 14552 O  O   . HOH BB 5 .   ? 19.185 -32.021 -43.754  1.00 18.71 ? 1095 HOH G O   1 
HETATM 14553 O  O   . HOH BB 5 .   ? 13.059 -41.905 -39.793  1.00 26.34 ? 1099 HOH G O   1 
HETATM 14554 O  O   . HOH BB 5 .   ? 17.975 -39.011 -42.223  1.00 32.15 ? 1104 HOH G O   1 
HETATM 14555 O  O   . HOH BB 5 .   ? 18.341 -47.403 -22.293  1.00 20.08 ? 1110 HOH G O   1 
HETATM 14556 O  O   . HOH BB 5 .   ? 0.626  -37.677 -37.921  1.00 33.40 ? 1114 HOH G O   1 
HETATM 14557 O  O   . HOH BB 5 .   ? 15.291 -37.855 -43.092  1.00 20.94 ? 1127 HOH G O   1 
HETATM 14558 O  O   . HOH BB 5 .   ? 10.756 -27.309 -36.873  1.00 21.12 ? 1138 HOH G O   1 
HETATM 14559 O  O   . HOH BB 5 .   ? 10.468 -25.167 -34.387  1.00 23.18 ? 1140 HOH G O   1 
HETATM 14560 O  O   . HOH BB 5 .   ? 6.195  -29.246 -38.832  1.00 50.09 ? 1152 HOH G O   1 
HETATM 14561 O  O   . HOH BB 5 .   ? 34.422 -34.967 -31.150  1.00 41.81 ? 1156 HOH G O   1 
HETATM 14562 O  O   . HOH BB 5 .   ? 12.622 -30.826 -38.838  1.00 22.23 ? 1167 HOH G O   1 
HETATM 14563 O  O   . HOH BB 5 .   ? 33.824 -41.763 -24.003  1.00 43.09 ? 1180 HOH G O   1 
HETATM 14564 O  O   . HOH BB 5 .   ? 3.111  -40.726 -19.916  1.00 38.41 ? 1189 HOH G O   1 
HETATM 14565 O  O   . HOH BB 5 .   ? 14.772 -52.807 -40.022  1.00 31.25 ? 1205 HOH G O   1 
HETATM 14566 O  O   . HOH BB 5 .   ? 17.832 -40.654 -16.100  1.00 45.94 ? 1210 HOH G O   1 
HETATM 14567 O  O   . HOH BB 5 .   ? 32.276 -39.660 -24.565  1.00 36.91 ? 1214 HOH G O   1 
HETATM 14568 O  O   . HOH BB 5 .   ? 17.624 -19.445 -18.570  1.00 34.64 ? 1238 HOH G O   1 
HETATM 14569 O  O   . HOH BB 5 .   ? 12.954 -49.705 -42.531  1.00 28.83 ? 1243 HOH G O   1 
HETATM 14570 O  O   . HOH BB 5 .   ? 22.848 -29.531 -14.768  1.00 28.28 ? 1250 HOH G O   1 
HETATM 14571 O  O   . HOH BB 5 .   ? 25.303 -41.605 -37.756  1.00 27.40 ? 1251 HOH G O   1 
HETATM 14572 O  O   . HOH BB 5 .   ? 12.003 -48.005 -23.624  1.00 24.82 ? 1264 HOH G O   1 
HETATM 14573 O  O   . HOH BB 5 .   ? 7.888  -36.076 -41.346  1.00 31.32 ? 1265 HOH G O   1 
HETATM 14574 O  O   . HOH BB 5 .   ? -1.271 -40.001 -33.729  1.00 30.71 ? 1269 HOH G O   1 
HETATM 14575 O  O   . HOH BB 5 .   ? 13.650 -55.152 -36.051  1.00 29.44 ? 1275 HOH G O   1 
HETATM 14576 O  O   . HOH BB 5 .   ? 33.155 -38.478 -34.459  1.00 29.07 ? 1278 HOH G O   1 
HETATM 14577 O  O   . HOH BB 5 .   ? 18.215 -40.207 -20.105  1.00 28.18 ? 1307 HOH G O   1 
HETATM 14578 O  O   . HOH BB 5 .   ? 15.958 -41.433 -19.977  1.00 20.20 ? 1316 HOH G O   1 
HETATM 14579 O  O   . HOH BB 5 .   ? 29.165 -35.385 -26.713  1.00 30.78 ? 1335 HOH G O   1 
HETATM 14580 O  O   . HOH BB 5 .   ? 27.243 -41.741 -25.086  1.00 28.40 ? 1344 HOH G O   1 
HETATM 14581 O  O   . HOH BB 5 .   ? 2.402  -38.443 -39.504  1.00 46.15 ? 1349 HOH G O   1 
HETATM 14582 O  O   . HOH BB 5 .   ? -0.245 -32.561 -24.411  1.00 44.12 ? 1351 HOH G O   1 
HETATM 14583 O  O   . HOH BB 5 .   ? 15.252 -40.370 -17.362  1.00 34.76 ? 1353 HOH G O   1 
HETATM 14584 O  O   . HOH BB 5 .   ? 13.201 -37.840 -14.251  1.00 32.01 ? 1360 HOH G O   1 
HETATM 14585 O  O   . HOH BB 5 .   ? 15.966 -43.887 -42.322  1.00 35.37 ? 1361 HOH G O   1 
HETATM 14586 O  O   . HOH BB 5 .   ? 12.587 -39.362 -42.823  1.00 22.16 ? 1394 HOH G O   1 
HETATM 14587 O  O   . HOH BB 5 .   ? -3.375 -45.503 -19.746  1.00 28.72 ? 1405 HOH G O   1 
HETATM 14588 O  O   . HOH BB 5 .   ? 22.663 -40.387 -18.959  1.00 36.61 ? 1415 HOH G O   1 
HETATM 14589 O  O   . HOH BB 5 .   ? 26.729 -46.149 -37.011  1.00 27.92 ? 1424 HOH G O   1 
HETATM 14590 O  O   . HOH BB 5 .   ? 24.118 -45.960 -17.680  1.00 35.12 ? 1477 HOH G O   1 
HETATM 14591 O  O   . HOH BB 5 .   ? 23.724 -27.310 -31.806  1.00 30.86 ? 1489 HOH G O   1 
HETATM 14592 O  O   . HOH BB 5 .   ? -7.622 -37.847 -25.629  1.00 30.42 ? 1497 HOH G O   1 
HETATM 14593 O  O   . HOH BB 5 .   ? 4.233  -48.313 -29.986  1.00 26.60 ? 1521 HOH G O   1 
HETATM 14594 O  O   . HOH BB 5 .   ? 20.299 -30.041 -14.193  1.00 39.08 ? 1525 HOH G O   1 
HETATM 14595 O  O   . HOH BB 5 .   ? 26.335 -50.427 -25.101  1.00 31.99 ? 1540 HOH G O   1 
HETATM 14596 O  O   . HOH BB 5 .   ? 6.710  -39.436 -17.049  1.00 24.41 ? 1541 HOH G O   1 
HETATM 14597 O  O   . HOH BB 5 .   ? 13.293 -53.966 -33.674  1.00 25.15 ? 1554 HOH G O   1 
HETATM 14598 O  O   . HOH BB 5 .   ? 27.598 -49.463 -38.116  1.00 35.05 ? 1555 HOH G O   1 
HETATM 14599 O  O   . HOH BB 5 .   ? 7.818  -28.228 -36.883  1.00 31.38 ? 1569 HOH G O   1 
HETATM 14600 O  O   . HOH BB 5 .   ? 28.757 -47.513 -39.258  1.00 37.69 ? 1609 HOH G O   1 
HETATM 14601 O  O   . HOH BB 5 .   ? 7.837  -26.394 -43.183  1.00 39.47 ? 1632 HOH G O   1 
HETATM 14602 O  O   . HOH BB 5 .   ? 7.796  -24.847 -45.365  1.00 37.54 ? 1643 HOH G O   1 
HETATM 14603 O  O   . HOH BB 5 .   ? 20.660 -39.650 -17.758  1.00 35.42 ? 1677 HOH G O   1 
HETATM 14604 O  O   . HOH BB 5 .   ? -3.539 -38.070 -19.591  1.00 28.03 ? 1679 HOH G O   1 
HETATM 14605 O  O   . HOH BB 5 .   ? 15.382 -12.513 -19.339  1.00 38.42 ? 1683 HOH G O   1 
HETATM 14606 O  O   . HOH BB 5 .   ? 36.149 -28.817 -28.217  1.00 41.57 ? 1685 HOH G O   1 
HETATM 14607 O  O   . HOH BB 5 .   ? 13.341 -9.644  -18.721  1.00 33.29 ? 1688 HOH G O   1 
HETATM 14608 O  O   . HOH CB 5 .   ? 53.967 -4.311  -43.326  1.00 13.38 ? 154  HOH H O   1 
HETATM 14609 O  O   . HOH CB 5 .   ? 50.521 -4.886  -31.204  1.00 11.59 ? 155  HOH H O   1 
HETATM 14610 O  O   . HOH CB 5 .   ? 40.528 -0.482  -28.216  1.00 17.22 ? 156  HOH H O   1 
HETATM 14611 O  O   . HOH CB 5 .   ? 48.040 0.885   -32.734  1.00 8.37  ? 157  HOH H O   1 
HETATM 14612 O  O   . HOH CB 5 .   ? 50.300 0.029   -26.423  1.00 12.36 ? 158  HOH H O   1 
HETATM 14613 O  O   . HOH CB 5 .   ? 41.023 -9.790  -33.917  1.00 16.33 ? 159  HOH H O   1 
HETATM 14614 O  O   . HOH CB 5 .   ? 43.232 -2.027  -39.901  1.00 12.15 ? 160  HOH H O   1 
HETATM 14615 O  O   . HOH CB 5 .   ? 49.442 4.819   -22.642  1.00 11.57 ? 161  HOH H O   1 
HETATM 14616 O  O   . HOH CB 5 .   ? 42.000 -12.229 -33.380  1.00 14.08 ? 162  HOH H O   1 
HETATM 14617 O  O   . HOH CB 5 .   ? 51.834 -14.304 -33.524  1.00 17.21 ? 163  HOH H O   1 
HETATM 14618 O  O   . HOH CB 5 .   ? 55.277 1.059   -36.527  1.00 16.35 ? 164  HOH H O   1 
HETATM 14619 O  O   . HOH CB 5 .   ? 57.153 5.919   -26.375  1.00 8.91  ? 176  HOH H O   1 
HETATM 14620 O  O   . HOH CB 5 .   ? 45.446 2.525   -24.532  1.00 12.41 ? 209  HOH H O   1 
HETATM 14621 O  O   . HOH CB 5 .   ? 56.597 0.774   -33.826  1.00 20.67 ? 255  HOH H O   1 
HETATM 14622 O  O   . HOH CB 5 .   ? 49.199 -2.287  -39.632  1.00 20.30 ? 298  HOH H O   1 
HETATM 14623 O  O   . HOH CB 5 .   ? 34.543 -11.327 -25.398  1.00 17.97 ? 301  HOH H O   1 
HETATM 14624 O  O   . HOH CB 5 .   ? 44.332 -0.457  -26.671  1.00 17.16 ? 302  HOH H O   1 
HETATM 14625 O  O   . HOH CB 5 .   ? 61.047 -3.802  -34.072  1.00 29.40 ? 304  HOH H O   1 
HETATM 14626 O  O   . HOH CB 5 .   ? 63.426 8.484   -18.980  1.00 24.89 ? 312  HOH H O   1 
HETATM 14627 O  O   . HOH CB 5 .   ? 58.651 -11.527 -45.727  1.00 17.43 ? 348  HOH H O   1 
HETATM 14628 O  O   . HOH CB 5 .   ? 62.456 2.808   -28.616  1.00 17.10 ? 368  HOH H O   1 
HETATM 14629 O  O   . HOH CB 5 .   ? 44.721 -17.837 -30.968  1.00 13.76 ? 371  HOH H O   1 
HETATM 14630 O  O   . HOH CB 5 .   ? 55.217 0.631   -43.854  1.00 37.10 ? 387  HOH H O   1 
HETATM 14631 O  O   . HOH CB 5 .   ? 42.745 -10.946 -6.107   1.00 26.49 ? 431  HOH H O   1 
HETATM 14632 O  O   . HOH CB 5 .   ? 39.891 -5.444  -33.945  1.00 23.54 ? 464  HOH H O   1 
HETATM 14633 O  O   . HOH CB 5 .   ? 65.543 -5.462  -24.525  1.00 20.33 ? 467  HOH H O   1 
HETATM 14634 O  O   . HOH CB 5 .   ? 54.627 -18.857 -30.952  1.00 28.44 ? 490  HOH H O   1 
HETATM 14635 O  O   . HOH CB 5 .   ? 48.806 3.880   -38.606  1.00 20.12 ? 492  HOH H O   1 
HETATM 14636 O  O   . HOH CB 5 .   ? 46.857 -3.877  -39.226  1.00 15.41 ? 497  HOH H O   1 
HETATM 14637 O  O   . HOH CB 5 .   ? 34.040 -1.858  -18.969  1.00 18.09 ? 537  HOH H O   1 
HETATM 14638 O  O   . HOH CB 5 .   ? 37.466 -17.641 -28.301  1.00 25.46 ? 540  HOH H O   1 
HETATM 14639 O  O   . HOH CB 5 .   ? 63.790 -10.947 -17.762  1.00 32.82 ? 563  HOH H O   1 
HETATM 14640 O  O   . HOH CB 5 .   ? 64.838 -4.857  -22.136  1.00 23.53 ? 584  HOH H O   1 
HETATM 14641 O  O   . HOH CB 5 .   ? 64.359 -0.948  -13.992  1.00 25.35 ? 589  HOH H O   1 
HETATM 14642 O  O   . HOH CB 5 .   ? 49.760 -2.617  -42.082  1.00 27.10 ? 604  HOH H O   1 
HETATM 14643 O  O   . HOH CB 5 .   ? 49.271 1.942   -30.613  1.00 10.06 ? 619  HOH H O   1 
HETATM 14644 O  O   . HOH CB 5 .   ? 57.147 4.222   -18.297  1.00 14.46 ? 642  HOH H O   1 
HETATM 14645 O  O   . HOH CB 5 .   ? 50.200 5.043   -41.413  1.00 20.17 ? 643  HOH H O   1 
HETATM 14646 O  O   . HOH CB 5 .   ? 50.352 -14.412 -13.048  1.00 18.72 ? 648  HOH H O   1 
HETATM 14647 O  O   . HOH CB 5 .   ? 49.066 -13.178 -38.337  1.00 25.40 ? 650  HOH H O   1 
HETATM 14648 O  O   . HOH CB 5 .   ? 58.225 5.861   -28.991  1.00 13.65 ? 654  HOH H O   1 
HETATM 14649 O  O   . HOH CB 5 .   ? 33.748 -9.006  -18.707  1.00 27.68 ? 670  HOH H O   1 
HETATM 14650 O  O   . HOH CB 5 .   ? 56.835 -14.781 -41.356  1.00 30.92 ? 686  HOH H O   1 
HETATM 14651 O  O   . HOH CB 5 .   ? 36.445 -5.138  -24.162  1.00 25.10 ? 692  HOH H O   1 
HETATM 14652 O  O   . HOH CB 5 .   ? 39.452 -17.595 -37.020  1.00 34.93 ? 698  HOH H O   1 
HETATM 14653 O  O   . HOH CB 5 .   ? 49.790 -0.108  -37.079  1.00 14.65 ? 742  HOH H O   1 
HETATM 14654 O  O   . HOH CB 5 .   ? 41.761 0.403   -38.770  1.00 20.30 ? 745  HOH H O   1 
HETATM 14655 O  O   . HOH CB 5 .   ? 58.258 -11.607 -31.338  1.00 18.34 ? 750  HOH H O   1 
HETATM 14656 O  O   . HOH CB 5 .   ? 52.600 -3.210  -10.766  1.00 24.16 ? 761  HOH H O   1 
HETATM 14657 O  O   . HOH CB 5 .   ? 48.236 -6.137  -8.249   1.00 22.28 ? 781  HOH H O   1 
HETATM 14658 O  O   . HOH CB 5 .   ? 51.250 -22.611 -16.997  1.00 21.55 ? 794  HOH H O   1 
HETATM 14659 O  O   . HOH CB 5 .   ? 67.509 1.405   -24.582  1.00 35.82 ? 799  HOH H O   1 
HETATM 14660 O  O   . HOH CB 5 .   ? 56.731 -27.858 -22.258  1.00 27.57 ? 806  HOH H O   1 
HETATM 14661 O  O   . HOH CB 5 .   ? 38.806 -8.364  -36.709  1.00 37.78 ? 807  HOH H O   1 
HETATM 14662 O  O   . HOH CB 5 .   ? 36.780 -10.335 -10.830  1.00 20.50 ? 840  HOH H O   1 
HETATM 14663 O  O   . HOH CB 5 .   ? 62.585 -11.434 -14.048  1.00 33.84 ? 851  HOH H O   1 
HETATM 14664 O  O   . HOH CB 5 .   ? 57.389 -10.093 -10.897  1.00 39.66 ? 861  HOH H O   1 
HETATM 14665 O  O   . HOH CB 5 .   ? 36.836 -0.839  -17.293  1.00 37.56 ? 875  HOH H O   1 
HETATM 14666 O  O   . HOH CB 5 .   ? 53.290 6.041   -38.134  1.00 31.64 ? 879  HOH H O   1 
HETATM 14667 O  O   . HOH CB 5 .   ? 57.282 -17.229 -16.773  1.00 38.86 ? 884  HOH H O   1 
HETATM 14668 O  O   . HOH CB 5 .   ? 61.577 -16.124 -27.045  1.00 25.13 ? 889  HOH H O   1 
HETATM 14669 O  O   . HOH CB 5 .   ? 43.133 -11.087 -42.597  1.00 31.43 ? 895  HOH H O   1 
HETATM 14670 O  O   . HOH CB 5 .   ? 54.087 -14.821 -31.943  1.00 29.63 ? 901  HOH H O   1 
HETATM 14671 O  O   . HOH CB 5 .   ? 38.961 -16.899 -24.770  1.00 26.41 ? 934  HOH H O   1 
HETATM 14672 O  O   . HOH CB 5 .   ? 63.392 -1.025  -27.702  1.00 28.75 ? 940  HOH H O   1 
HETATM 14673 O  O   . HOH CB 5 .   ? 41.067 -12.399 -41.478  1.00 38.64 ? 951  HOH H O   1 
HETATM 14674 O  O   . HOH CB 5 .   ? 50.202 2.863   -14.499  1.00 27.19 ? 952  HOH H O   1 
HETATM 14675 O  O   . HOH CB 5 .   ? 40.394 -9.412  -42.080  1.00 34.19 ? 961  HOH H O   1 
HETATM 14676 O  O   . HOH CB 5 .   ? 66.383 -5.922  -19.725  1.00 18.59 ? 964  HOH H O   1 
HETATM 14677 O  O   . HOH CB 5 .   ? 42.408 -5.566  -10.897  1.00 28.32 ? 1015 HOH H O   1 
HETATM 14678 O  O   . HOH CB 5 .   ? 59.656 -12.086 -43.021  1.00 31.64 ? 1022 HOH H O   1 
HETATM 14679 O  O   . HOH CB 5 .   ? 45.343 4.736   -20.471  1.00 42.69 ? 1038 HOH H O   1 
HETATM 14680 O  O   . HOH CB 5 .   ? 62.143 -10.274 -36.404  1.00 19.22 ? 1048 HOH H O   1 
HETATM 14681 O  O   . HOH CB 5 .   ? 33.076 -9.483  -23.293  1.00 23.05 ? 1065 HOH H O   1 
HETATM 14682 O  O   . HOH CB 5 .   ? 47.352 -0.596  -8.500   1.00 32.66 ? 1067 HOH H O   1 
HETATM 14683 O  O   . HOH CB 5 .   ? 69.114 5.576   -18.528  1.00 23.54 ? 1091 HOH H O   1 
HETATM 14684 O  O   . HOH CB 5 .   ? 63.542 -1.987  -30.950  1.00 31.26 ? 1115 HOH H O   1 
HETATM 14685 O  O   . HOH CB 5 .   ? 69.228 -4.386  -19.994  1.00 37.38 ? 1134 HOH H O   1 
HETATM 14686 O  O   . HOH CB 5 .   ? 45.894 -18.921 -33.174  1.00 29.84 ? 1144 HOH H O   1 
HETATM 14687 O  O   . HOH CB 5 .   ? 44.304 2.321   -17.705  1.00 47.93 ? 1154 HOH H O   1 
HETATM 14688 O  O   . HOH CB 5 .   ? 59.161 -15.403 -29.753  1.00 38.74 ? 1165 HOH H O   1 
HETATM 14689 O  O   . HOH CB 5 .   ? 61.853 -10.323 -39.801  1.00 22.06 ? 1166 HOH H O   1 
HETATM 14690 O  O   . HOH CB 5 .   ? 42.178 -18.501 -30.663  1.00 32.80 ? 1173 HOH H O   1 
HETATM 14691 O  O   . HOH CB 5 .   ? 41.216 -1.765  -32.450  1.00 32.74 ? 1188 HOH H O   1 
HETATM 14692 O  O   . HOH CB 5 .   ? 35.888 1.484   -17.889  1.00 39.97 ? 1202 HOH H O   1 
HETATM 14693 O  O   . HOH CB 5 .   ? 47.816 -16.254 -35.626  1.00 31.29 ? 1218 HOH H O   1 
HETATM 14694 O  O   . HOH CB 5 .   ? 45.203 -8.474  -43.845  1.00 26.66 ? 1233 HOH H O   1 
HETATM 14695 O  O   . HOH CB 5 .   ? 39.238 -7.867  -33.563  1.00 21.75 ? 1236 HOH H O   1 
HETATM 14696 O  O   . HOH CB 5 .   ? 43.125 -21.327 -27.356  1.00 31.17 ? 1285 HOH H O   1 
HETATM 14697 O  O   . HOH CB 5 .   ? 30.128 -0.559  -20.886  1.00 31.86 ? 1286 HOH H O   1 
HETATM 14698 O  O   . HOH CB 5 .   ? 44.548 1.548   -28.841  1.00 20.68 ? 1288 HOH H O   1 
HETATM 14699 O  O   . HOH CB 5 .   ? 32.987 -7.294  -16.590  1.00 23.88 ? 1304 HOH H O   1 
HETATM 14700 O  O   . HOH CB 5 .   ? 65.357 -6.807  -11.826  1.00 24.47 ? 1321 HOH H O   1 
HETATM 14701 O  O   . HOH CB 5 .   ? 34.678 -8.774  -26.234  1.00 32.11 ? 1328 HOH H O   1 
HETATM 14702 O  O   . HOH CB 5 .   ? 39.781 -4.796  -41.300  1.00 36.17 ? 1341 HOH H O   1 
HETATM 14703 O  O   . HOH CB 5 .   ? 29.558 -3.918  -12.663  1.00 49.05 ? 1346 HOH H O   1 
HETATM 14704 O  O   . HOH CB 5 .   ? 45.259 -1.632  -40.759  1.00 35.13 ? 1379 HOH H O   1 
HETATM 14705 O  O   . HOH CB 5 .   ? 40.246 1.457   -36.014  1.00 35.27 ? 1383 HOH H O   1 
HETATM 14706 O  O   . HOH CB 5 .   ? 33.914 -0.617  -25.702  1.00 39.67 ? 1389 HOH H O   1 
HETATM 14707 O  O   . HOH CB 5 .   ? 67.171 -0.606  -17.695  1.00 42.97 ? 1393 HOH H O   1 
HETATM 14708 O  O   . HOH CB 5 .   ? 36.855 1.032   -39.665  1.00 40.92 ? 1400 HOH H O   1 
HETATM 14709 O  O   . HOH CB 5 .   ? 63.407 7.772   -14.866  1.00 39.68 ? 1407 HOH H O   1 
HETATM 14710 O  O   . HOH CB 5 .   ? 36.859 5.391   -16.908  1.00 41.27 ? 1428 HOH H O   1 
HETATM 14711 O  O   . HOH CB 5 .   ? 40.624 -21.054 -26.950  1.00 31.36 ? 1429 HOH H O   1 
HETATM 14712 O  O   . HOH CB 5 .   ? 68.244 1.786   -16.809  1.00 34.77 ? 1431 HOH H O   1 
HETATM 14713 O  O   . HOH CB 5 .   ? 68.561 -13.806 -18.515  1.00 32.16 ? 1438 HOH H O   1 
HETATM 14714 O  O   . HOH CB 5 .   ? 65.321 -0.420  -26.502  1.00 33.90 ? 1456 HOH H O   1 
HETATM 14715 O  O   . HOH CB 5 .   ? 61.073 4.855   -13.038  1.00 33.61 ? 1461 HOH H O   1 
HETATM 14716 O  O   . HOH CB 5 .   ? 58.387 -22.638 -15.586  1.00 41.79 ? 1467 HOH H O   1 
HETATM 14717 O  O   . HOH CB 5 .   ? 53.812 -17.883 -15.672  1.00 30.43 ? 1474 HOH H O   1 
HETATM 14718 O  O   . HOH CB 5 .   ? 68.682 -7.782  -26.566  1.00 31.62 ? 1483 HOH H O   1 
HETATM 14719 O  O   . HOH CB 5 .   ? 44.713 -6.615  -10.269  1.00 27.52 ? 1488 HOH H O   1 
HETATM 14720 O  O   . HOH CB 5 .   ? 40.709 1.882   -27.084  1.00 35.81 ? 1504 HOH H O   1 
HETATM 14721 O  O   . HOH CB 5 .   ? 51.617 -28.530 -21.635  1.00 32.36 ? 1523 HOH H O   1 
HETATM 14722 O  O   . HOH CB 5 .   ? 50.321 -5.080  -42.201  1.00 23.37 ? 1531 HOH H O   1 
HETATM 14723 O  O   . HOH CB 5 .   ? 61.800 -6.789  -39.611  1.00 32.09 ? 1533 HOH H O   1 
HETATM 14724 O  O   . HOH CB 5 .   ? 39.656 -18.917 -28.790  1.00 28.32 ? 1544 HOH H O   1 
HETATM 14725 O  O   . HOH CB 5 .   ? 68.234 1.574   -20.869  1.00 22.09 ? 1553 HOH H O   1 
HETATM 14726 O  O   . HOH CB 5 .   ? 33.507 -5.916  -24.758  1.00 40.38 ? 1591 HOH H O   1 
HETATM 14727 O  O   . HOH CB 5 .   ? 41.643 -8.221  -2.275   1.00 37.61 ? 1600 HOH H O   1 
HETATM 14728 O  O   . HOH CB 5 .   ? 47.373 -14.451 -39.961  1.00 32.75 ? 1622 HOH H O   1 
HETATM 14729 O  O   . HOH CB 5 .   ? 68.475 4.727   -14.389  1.00 35.66 ? 1623 HOH H O   1 
HETATM 14730 O  O   . HOH CB 5 .   ? 67.951 -4.618  -16.224  1.00 40.21 ? 1626 HOH H O   1 
HETATM 14731 O  O   . HOH CB 5 .   ? 43.916 -17.844 -35.123  1.00 34.92 ? 1628 HOH H O   1 
HETATM 14732 O  O   . HOH CB 5 .   ? 42.143 -20.556 -33.037  1.00 30.03 ? 1659 HOH H O   1 
HETATM 14733 O  O   . HOH CB 5 .   ? 55.763 -10.467 -31.140  1.00 23.64 ? 1670 HOH H O   1 
HETATM 14734 O  O   . HOH CB 5 .   ? 56.438 -16.355 -36.978  1.00 31.36 ? 1680 HOH H O   1 
HETATM 14735 O  O   . HOH CB 5 .   ? 54.076 -16.993 -36.667  1.00 32.80 ? 1690 HOH H O   1 
HETATM 14736 O  O   . HOH DB 5 .   ? 50.812 -22.098 -14.400  1.00 23.91 ? 236  HOH I O   1 
HETATM 14737 O  O   . HOH DB 5 .   ? 51.364 -19.572 -12.840  1.00 25.25 ? 343  HOH I O   1 
HETATM 14738 O  O   . HOH DB 5 .   ? 26.716 -22.326 -17.550  1.00 32.93 ? 405  HOH I O   1 
HETATM 14739 O  O   . HOH DB 5 .   ? 34.543 -19.619 -13.113  1.00 27.48 ? 413  HOH I O   1 
HETATM 14740 O  O   . HOH DB 5 .   ? 31.092 -24.213 -4.751   1.00 24.47 ? 435  HOH I O   1 
HETATM 14741 O  O   . HOH DB 5 .   ? 39.021 -31.547 -0.538   1.00 19.43 ? 446  HOH I O   1 
HETATM 14742 O  O   . HOH DB 5 .   ? 53.967 -8.478  -5.161   1.00 24.59 ? 451  HOH I O   1 
HETATM 14743 O  O   . HOH DB 5 .   ? 33.285 -31.939 -15.093  1.00 20.71 ? 475  HOH I O   1 
HETATM 14744 O  O   . HOH DB 5 .   ? 48.512 -38.711 -5.054   1.00 34.05 ? 485  HOH I O   1 
HETATM 14745 O  O   . HOH DB 5 .   ? 24.737 -33.401 -19.796  1.00 20.30 ? 685  HOH I O   1 
HETATM 14746 O  O   . HOH DB 5 .   ? 50.123 -25.556 -24.701  1.00 34.71 ? 735  HOH I O   1 
HETATM 14747 O  O   . HOH DB 5 .   ? 30.137 -23.896 -21.647  1.00 33.22 ? 782  HOH I O   1 
HETATM 14748 O  O   . HOH DB 5 .   ? 30.128 -26.807 -4.884   1.00 30.76 ? 818  HOH I O   1 
HETATM 14749 O  O   . HOH DB 5 .   ? 38.678 -22.120 2.079    1.00 29.30 ? 858  HOH I O   1 
HETATM 14750 O  O   . HOH DB 5 .   ? 62.344 -35.981 -6.767   1.00 24.23 ? 885  HOH I O   1 
HETATM 14751 O  O   . HOH DB 5 .   ? 43.422 -13.951 -0.688   1.00 38.09 ? 900  HOH I O   1 
HETATM 14752 O  O   . HOH DB 5 .   ? 34.775 -18.759 -4.821   1.00 23.17 ? 902  HOH I O   1 
HETATM 14753 O  O   . HOH DB 5 .   ? 57.869 -27.087 -11.936  1.00 34.57 ? 914  HOH I O   1 
HETATM 14754 O  O   . HOH DB 5 .   ? 61.300 -34.662 -4.275   1.00 24.15 ? 959  HOH I O   1 
HETATM 14755 O  O   . HOH DB 5 .   ? 35.454 -29.806 -23.224  1.00 34.76 ? 969  HOH I O   1 
HETATM 14756 O  O   . HOH DB 5 .   ? 45.155 -7.892  -7.523   1.00 25.01 ? 980  HOH I O   1 
HETATM 14757 O  O   . HOH DB 5 .   ? 35.532 -27.823 -21.409  1.00 25.07 ? 1012 HOH I O   1 
HETATM 14758 O  O   . HOH DB 5 .   ? 39.240 -37.482 7.390    1.00 31.02 ? 1047 HOH I O   1 
HETATM 14759 O  O   . HOH DB 5 .   ? 30.681 -26.392 -11.161  1.00 38.96 ? 1082 HOH I O   1 
HETATM 14760 O  O   . HOH DB 5 .   ? 48.749 -13.700 -10.736  1.00 23.34 ? 1094 HOH I O   1 
HETATM 14761 O  O   . HOH DB 5 .   ? 35.600 -15.673 -8.066   1.00 33.00 ? 1096 HOH I O   1 
HETATM 14762 O  O   . HOH DB 5 .   ? 39.116 -36.351 -19.629  1.00 33.18 ? 1208 HOH I O   1 
HETATM 14763 O  O   . HOH DB 5 .   ? 53.673 -20.612 -11.240  1.00 34.39 ? 1209 HOH I O   1 
HETATM 14764 O  O   . HOH DB 5 .   ? 31.696 -24.890 -23.111  1.00 41.44 ? 1241 HOH I O   1 
HETATM 14765 O  O   . HOH DB 5 .   ? 48.389 -30.009 -20.187  1.00 28.42 ? 1244 HOH I O   1 
HETATM 14766 O  O   . HOH DB 5 .   ? 35.342 -35.525 -20.515  1.00 25.81 ? 1268 HOH I O   1 
HETATM 14767 O  O   . HOH DB 5 .   ? 39.876 -26.750 -28.339  1.00 32.13 ? 1299 HOH I O   1 
HETATM 14768 O  O   . HOH DB 5 .   ? 28.705 -31.710 -11.930  1.00 34.56 ? 1305 HOH I O   1 
HETATM 14769 O  O   . HOH DB 5 .   ? 42.138 -16.797 1.826    1.00 37.69 ? 1367 HOH I O   1 
HETATM 14770 O  O   . HOH DB 5 .   ? 46.159 -31.195 -20.787  1.00 34.91 ? 1385 HOH I O   1 
HETATM 14771 O  O   . HOH DB 5 .   ? 33.228 -36.175 -8.553   1.00 40.10 ? 1396 HOH I O   1 
HETATM 14772 O  O   . HOH DB 5 .   ? 62.545 -21.187 -4.406   1.00 33.76 ? 1419 HOH I O   1 
HETATM 14773 O  O   . HOH DB 5 .   ? 54.525 -18.692 -5.760   1.00 32.15 ? 1433 HOH I O   1 
HETATM 14774 O  O   . HOH DB 5 .   ? 42.309 -40.276 -15.194  1.00 40.87 ? 1440 HOH I O   1 
HETATM 14775 O  O   . HOH DB 5 .   ? 41.756 -38.144 1.563    1.00 33.27 ? 1441 HOH I O   1 
HETATM 14776 O  O   . HOH DB 5 .   ? 54.294 -15.015 -7.911   1.00 27.11 ? 1462 HOH I O   1 
HETATM 14777 O  O   . HOH DB 5 .   ? 30.931 -34.757 -5.661   1.00 45.03 ? 1466 HOH I O   1 
HETATM 14778 O  O   . HOH DB 5 .   ? 46.997 -42.025 0.840    1.00 34.72 ? 1508 HOH I O   1 
HETATM 14779 O  O   . HOH DB 5 .   ? 55.530 -30.793 2.595    1.00 27.41 ? 1559 HOH I O   1 
HETATM 14780 O  O   . HOH DB 5 .   ? 30.879 -19.755 -20.443  1.00 34.21 ? 1566 HOH I O   1 
HETATM 14781 O  O   . HOH DB 5 .   ? 31.039 -31.186 3.311    1.00 36.64 ? 1593 HOH I O   1 
HETATM 14782 O  O   . HOH DB 5 .   ? 48.508 -40.889 -13.907  1.00 33.44 ? 1613 HOH I O   1 
HETATM 14783 O  O   . HOH DB 5 .   ? 56.016 -17.194 -3.983   1.00 46.06 ? 1619 HOH I O   1 
HETATM 14784 O  O   . HOH DB 5 .   ? 34.738 -25.496 -12.567  1.00 27.49 ? 1672 HOH I O   1 
HETATM 14785 O  O   . HOH DB 5 .   ? 54.452 -41.503 -6.507   1.00 47.09 ? 1678 HOH I O   1 
HETATM 14786 O  O   . HOH DB 5 .   ? 53.022 -40.181 -5.125   1.00 34.80 ? 1682 HOH I O   1 
HETATM 14787 O  O   . HOH DB 5 .   ? 41.106 -37.259 5.697    1.00 31.29 ? 1705 HOH I O   1 
HETATM 14788 O  O   . HOH EB 5 .   ? 20.351 -4.173  -48.355  1.00 9.93  ? 154  HOH J O   1 
HETATM 14789 O  O   . HOH EB 5 .   ? 24.281 8.196   -49.580  1.00 5.77  ? 155  HOH J O   1 
HETATM 14790 O  O   . HOH EB 5 .   ? 32.688 2.127   -57.135  1.00 12.31 ? 156  HOH J O   1 
HETATM 14791 O  O   . HOH EB 5 .   ? 13.567 -0.790  -50.599  1.00 9.96  ? 157  HOH J O   1 
HETATM 14792 O  O   . HOH EB 5 .   ? 38.201 9.112   -63.198  1.00 10.60 ? 158  HOH J O   1 
HETATM 14793 O  O   . HOH EB 5 .   ? 31.968 0.872   -59.569  1.00 11.27 ? 159  HOH J O   1 
HETATM 14794 O  O   . HOH EB 5 .   ? 24.085 13.984  -45.568  1.00 17.72 ? 160  HOH J O   1 
HETATM 14795 O  O   . HOH EB 5 .   ? 22.448 5.896   -55.473  1.00 8.78  ? 161  HOH J O   1 
HETATM 14796 O  O   . HOH EB 5 .   ? 13.989 15.008  -49.905  1.00 13.37 ? 162  HOH J O   1 
HETATM 14797 O  O   . HOH EB 5 .   ? 21.300 12.396  -53.997  1.00 10.51 ? 163  HOH J O   1 
HETATM 14798 O  O   . HOH EB 5 .   ? 12.046 2.413   -53.718  1.00 15.64 ? 196  HOH J O   1 
HETATM 14799 O  O   . HOH EB 5 .   ? 14.995 -8.428  -55.338  1.00 16.34 ? 256  HOH J O   1 
HETATM 14800 O  O   . HOH EB 5 .   ? 25.715 16.459  -52.677  1.00 13.14 ? 261  HOH J O   1 
HETATM 14801 O  O   . HOH EB 5 .   ? 22.510 18.060  -52.461  1.00 22.69 ? 277  HOH J O   1 
HETATM 14802 O  O   . HOH EB 5 .   ? 25.759 -4.298  -58.226  1.00 13.08 ? 285  HOH J O   1 
HETATM 14803 O  O   . HOH EB 5 .   ? 22.595 6.313   -77.868  1.00 15.08 ? 291  HOH J O   1 
HETATM 14804 O  O   . HOH EB 5 .   ? 34.053 21.382  -71.195  1.00 25.95 ? 305  HOH J O   1 
HETATM 14805 O  O   . HOH EB 5 .   ? 8.569  10.353  -68.968  1.00 20.54 ? 336  HOH J O   1 
HETATM 14806 O  O   . HOH EB 5 .   ? 23.256 3.816   -47.893  1.00 11.58 ? 340  HOH J O   1 
HETATM 14807 O  O   . HOH EB 5 .   ? 22.476 -1.690  -61.700  1.00 10.30 ? 347  HOH J O   1 
HETATM 14808 O  O   . HOH EB 5 .   ? 7.255  10.400  -61.521  1.00 16.91 ? 357  HOH J O   1 
HETATM 14809 O  O   . HOH EB 5 .   ? 20.204 -0.903  -63.282  1.00 14.91 ? 362  HOH J O   1 
HETATM 14810 O  O   . HOH EB 5 .   ? 27.504 12.958  -53.858  1.00 10.75 ? 363  HOH J O   1 
HETATM 14811 O  O   . HOH EB 5 .   ? 20.171 -3.164  -66.823  1.00 18.69 ? 365  HOH J O   1 
HETATM 14812 O  O   . HOH EB 5 .   ? 30.149 1.344   -47.609  1.00 14.83 ? 382  HOH J O   1 
HETATM 14813 O  O   . HOH EB 5 .   ? 21.940 14.956  -73.759  1.00 12.31 ? 385  HOH J O   1 
HETATM 14814 O  O   . HOH EB 5 .   ? 24.290 8.620   -44.357  1.00 37.16 ? 390  HOH J O   1 
HETATM 14815 O  O   . HOH EB 5 .   ? 15.795 0.205   -61.520  1.00 10.30 ? 391  HOH J O   1 
HETATM 14816 O  O   . HOH EB 5 .   ? 24.159 -1.991  -47.389  1.00 19.14 ? 412  HOH J O   1 
HETATM 14817 O  O   . HOH EB 5 .   ? 36.547 19.957  -59.179  1.00 20.97 ? 422  HOH J O   1 
HETATM 14818 O  O   . HOH EB 5 .   ? 18.627 -2.410  -43.932  1.00 16.71 ? 426  HOH J O   1 
HETATM 14819 O  O   . HOH EB 5 .   ? 35.942 13.604  -59.229  1.00 20.53 ? 428  HOH J O   1 
HETATM 14820 O  O   . HOH EB 5 .   ? 16.518 10.617  -74.457  1.00 25.97 ? 438  HOH J O   1 
HETATM 14821 O  O   . HOH EB 5 .   ? 32.027 15.687  -53.549  1.00 25.71 ? 439  HOH J O   1 
HETATM 14822 O  O   . HOH EB 5 .   ? 31.385 12.313  -53.215  1.00 20.17 ? 444  HOH J O   1 
HETATM 14823 O  O   . HOH EB 5 .   ? 20.823 11.865  -75.379  1.00 17.31 ? 456  HOH J O   1 
HETATM 14824 O  O   . HOH EB 5 .   ? 31.538 7.440   -51.460  1.00 36.44 ? 457  HOH J O   1 
HETATM 14825 O  O   . HOH EB 5 .   ? 33.300 4.864   -53.387  1.00 22.14 ? 463  HOH J O   1 
HETATM 14826 O  O   . HOH EB 5 .   ? 26.338 -0.416  -50.246  1.00 20.28 ? 491  HOH J O   1 
HETATM 14827 O  O   . HOH EB 5 .   ? 23.558 -3.073  -51.599  1.00 24.55 ? 505  HOH J O   1 
HETATM 14828 O  O   . HOH EB 5 .   ? 31.134 4.080   -46.365  1.00 21.36 ? 513  HOH J O   1 
HETATM 14829 O  O   . HOH EB 5 .   ? 9.398  10.098  -51.515  1.00 15.27 ? 526  HOH J O   1 
HETATM 14830 O  O   . HOH EB 5 .   ? 20.112 24.540  -66.718  1.00 30.95 ? 552  HOH J O   1 
HETATM 14831 O  O   . HOH EB 5 .   ? 32.340 -0.808  -66.076  1.00 19.93 ? 572  HOH J O   1 
HETATM 14832 O  O   . HOH EB 5 .   ? 25.758 6.482   -46.072  1.00 21.92 ? 579  HOH J O   1 
HETATM 14833 O  O   . HOH EB 5 .   ? 18.479 0.824   -62.116  1.00 21.21 ? 585  HOH J O   1 
HETATM 14834 O  O   . HOH EB 5 .   ? 12.067 21.835  -65.570  1.00 35.31 ? 602  HOH J O   1 
HETATM 14835 O  O   . HOH EB 5 .   ? 26.204 22.525  -68.815  1.00 24.79 ? 605  HOH J O   1 
HETATM 14836 O  O   . HOH EB 5 .   ? 22.723 -2.607  -45.131  1.00 12.79 ? 615  HOH J O   1 
HETATM 14837 O  O   . HOH EB 5 .   ? 22.740 10.363  -49.866  1.00 16.01 ? 631  HOH J O   1 
HETATM 14838 O  O   . HOH EB 5 .   ? 28.089 -0.143  -47.061  1.00 23.71 ? 662  HOH J O   1 
HETATM 14839 O  O   . HOH EB 5 .   ? 28.150 23.305  -66.867  1.00 22.57 ? 664  HOH J O   1 
HETATM 14840 O  O   . HOH EB 5 .   ? 25.023 -0.930  -75.750  1.00 17.88 ? 673  HOH J O   1 
HETATM 14841 O  O   . HOH EB 5 .   ? 34.646 5.981   -68.209  1.00 15.84 ? 679  HOH J O   1 
HETATM 14842 O  O   . HOH EB 5 .   ? 38.653 19.028  -65.150  1.00 39.16 ? 693  HOH J O   1 
HETATM 14843 O  O   . HOH EB 5 .   ? 29.940 -0.464  -65.532  1.00 15.63 ? 695  HOH J O   1 
HETATM 14844 O  O   . HOH EB 5 .   ? 6.035  20.636  -52.672  1.00 22.70 ? 727  HOH J O   1 
HETATM 14845 O  O   . HOH EB 5 .   ? 38.392 16.358  -65.216  1.00 29.25 ? 731  HOH J O   1 
HETATM 14846 O  O   . HOH EB 5 .   ? 9.513  3.171   -53.202  1.00 25.45 ? 732  HOH J O   1 
HETATM 14847 O  O   . HOH EB 5 .   ? 15.112 2.553   -47.232  1.00 20.33 ? 736  HOH J O   1 
HETATM 14848 O  O   . HOH EB 5 .   ? 13.325 12.348  -48.309  1.00 20.38 ? 739  HOH J O   1 
HETATM 14849 O  O   . HOH EB 5 .   ? 31.678 -5.423  -53.458  1.00 20.53 ? 786  HOH J O   1 
HETATM 14850 O  O   . HOH EB 5 .   ? 36.139 2.401   -66.818  1.00 19.97 ? 790  HOH J O   1 
HETATM 14851 O  O   . HOH EB 5 .   ? 9.250  5.668   -54.220  1.00 21.63 ? 795  HOH J O   1 
HETATM 14852 O  O   . HOH EB 5 .   ? 36.886 -1.843  -55.591  1.00 27.73 ? 797  HOH J O   1 
HETATM 14853 O  O   . HOH EB 5 .   ? 36.182 5.652   -56.066  1.00 19.31 ? 804  HOH J O   1 
HETATM 14854 O  O   . HOH EB 5 .   ? 9.783  12.688  -71.619  1.00 26.65 ? 816  HOH J O   1 
HETATM 14855 O  O   . HOH EB 5 .   ? 41.804 12.866  -59.717  1.00 42.19 ? 849  HOH J O   1 
HETATM 14856 O  O   . HOH EB 5 .   ? 18.373 22.900  -66.233  1.00 26.72 ? 852  HOH J O   1 
HETATM 14857 O  O   . HOH EB 5 .   ? 34.518 0.987   -67.539  1.00 25.56 ? 865  HOH J O   1 
HETATM 14858 O  O   . HOH EB 5 .   ? 28.894 -3.008  -65.214  1.00 25.10 ? 892  HOH J O   1 
HETATM 14859 O  O   . HOH EB 5 .   ? 5.852  13.447  -51.433  1.00 24.67 ? 894  HOH J O   1 
HETATM 14860 O  O   . HOH EB 5 .   ? 42.503 3.322   -67.944  1.00 26.91 ? 905  HOH J O   1 
HETATM 14861 O  O   . HOH EB 5 .   ? 39.720 10.983  -69.613  1.00 32.22 ? 915  HOH J O   1 
HETATM 14862 O  O   . HOH EB 5 .   ? 17.294 3.966   -47.633  1.00 23.32 ? 926  HOH J O   1 
HETATM 14863 O  O   . HOH EB 5 .   ? 37.025 15.260  -53.913  1.00 39.42 ? 928  HOH J O   1 
HETATM 14864 O  O   . HOH EB 5 .   ? 32.546 7.175   -47.750  1.00 49.00 ? 930  HOH J O   1 
HETATM 14865 O  O   . HOH EB 5 .   ? 27.740 23.905  -74.710  1.00 30.44 ? 936  HOH J O   1 
HETATM 14866 O  O   . HOH EB 5 .   ? 8.784  17.413  -52.125  1.00 25.68 ? 938  HOH J O   1 
HETATM 14867 O  O   . HOH EB 5 .   ? 33.637 21.505  -59.704  1.00 23.67 ? 950  HOH J O   1 
HETATM 14868 O  O   . HOH EB 5 .   ? 20.193 25.261  -69.876  1.00 30.29 ? 963  HOH J O   1 
HETATM 14869 O  O   . HOH EB 5 .   ? 28.994 3.080   -45.874  1.00 29.08 ? 968  HOH J O   1 
HETATM 14870 O  O   . HOH EB 5 .   ? 12.851 4.108   -72.009  1.00 26.78 ? 975  HOH J O   1 
HETATM 14871 O  O   . HOH EB 5 .   ? 7.198  12.062  -74.454  1.00 33.03 ? 998  HOH J O   1 
HETATM 14872 O  O   . HOH EB 5 .   ? 23.107 -2.265  -74.036  1.00 23.22 ? 1006 HOH J O   1 
HETATM 14873 O  O   . HOH EB 5 .   ? 31.061 -4.190  -63.230  1.00 27.78 ? 1010 HOH J O   1 
HETATM 14874 O  O   . HOH EB 5 .   ? 33.815 4.115   -55.685  1.00 24.52 ? 1011 HOH J O   1 
HETATM 14875 O  O   . HOH EB 5 .   ? 14.968 -10.502 -57.016  1.00 24.86 ? 1030 HOH J O   1 
HETATM 14876 O  O   . HOH EB 5 .   ? 23.901 22.462  -52.924  1.00 30.53 ? 1034 HOH J O   1 
HETATM 14877 O  O   . HOH EB 5 .   ? 31.556 0.510   -70.514  1.00 21.25 ? 1050 HOH J O   1 
HETATM 14878 O  O   . HOH EB 5 .   ? 7.018  7.932   -60.650  1.00 18.75 ? 1051 HOH J O   1 
HETATM 14879 O  O   . HOH EB 5 .   ? 5.710  11.623  -63.972  1.00 26.75 ? 1056 HOH J O   1 
HETATM 14880 O  O   . HOH EB 5 .   ? 23.801 5.037   -43.520  1.00 39.52 ? 1076 HOH J O   1 
HETATM 14881 O  O   . HOH EB 5 .   ? 39.263 12.206  -62.693  1.00 26.06 ? 1088 HOH J O   1 
HETATM 14882 O  O   . HOH EB 5 .   ? 15.915 6.109   -49.704  1.00 21.49 ? 1108 HOH J O   1 
HETATM 14883 O  O   . HOH EB 5 .   ? 3.656  15.866  -60.582  1.00 26.75 ? 1170 HOH J O   1 
HETATM 14884 O  O   . HOH EB 5 .   ? 5.545  9.407   -65.480  1.00 24.54 ? 1219 HOH J O   1 
HETATM 14885 O  O   . HOH EB 5 .   ? 37.034 21.779  -56.937  1.00 27.34 ? 1229 HOH J O   1 
HETATM 14886 O  O   . HOH EB 5 .   ? 17.703 -13.188 -55.049  1.00 25.69 ? 1232 HOH J O   1 
HETATM 14887 O  O   . HOH EB 5 .   ? 2.695  13.892  -57.325  1.00 28.84 ? 1242 HOH J O   1 
HETATM 14888 O  O   . HOH EB 5 .   ? 18.993 -3.314  -64.072  1.00 38.98 ? 1262 HOH J O   1 
HETATM 14889 O  O   . HOH EB 5 .   ? 12.669 -7.169  -56.240  1.00 19.96 ? 1270 HOH J O   1 
HETATM 14890 O  O   . HOH EB 5 .   ? 6.083  19.287  -63.394  1.00 20.31 ? 1274 HOH J O   1 
HETATM 14891 O  O   . HOH EB 5 .   ? 20.301 14.314  -75.841  1.00 24.15 ? 1279 HOH J O   1 
HETATM 14892 O  O   . HOH EB 5 .   ? 7.737  23.899  -58.359  1.00 29.84 ? 1306 HOH J O   1 
HETATM 14893 O  O   . HOH EB 5 .   ? 13.875 19.905  -55.654  1.00 22.62 ? 1313 HOH J O   1 
HETATM 14894 O  O   . HOH EB 5 .   ? 7.010  8.425   -67.146  1.00 25.86 ? 1326 HOH J O   1 
HETATM 14895 O  O   . HOH EB 5 .   ? 36.911 -1.628  -64.615  1.00 25.71 ? 1333 HOH J O   1 
HETATM 14896 O  O   . HOH EB 5 .   ? 27.347 -4.182  -61.924  1.00 29.26 ? 1337 HOH J O   1 
HETATM 14897 O  O   . HOH EB 5 .   ? 22.371 -4.341  -61.887  1.00 31.13 ? 1342 HOH J O   1 
HETATM 14898 O  O   . HOH EB 5 .   ? 29.716 -6.948  -55.871  1.00 29.33 ? 1354 HOH J O   1 
HETATM 14899 O  O   . HOH EB 5 .   ? 25.824 21.859  -57.492  1.00 33.96 ? 1376 HOH J O   1 
HETATM 14900 O  O   . HOH EB 5 .   ? 10.305 -1.532  -58.708  1.00 37.14 ? 1378 HOH J O   1 
HETATM 14901 O  O   . HOH EB 5 .   ? 0.692  23.025  -56.066  1.00 40.14 ? 1390 HOH J O   1 
HETATM 14902 O  O   . HOH EB 5 .   ? 4.044  11.140  -54.801  1.00 29.92 ? 1401 HOH J O   1 
HETATM 14903 O  O   . HOH EB 5 .   ? 10.222 11.984  -49.279  1.00 30.24 ? 1408 HOH J O   1 
HETATM 14904 O  O   . HOH EB 5 .   ? 37.461 15.608  -70.182  1.00 41.15 ? 1455 HOH J O   1 
HETATM 14905 O  O   . HOH EB 5 .   ? 7.010  19.086  -51.010  1.00 30.38 ? 1458 HOH J O   1 
HETATM 14906 O  O   . HOH EB 5 .   ? 17.305 -12.103 -59.949  1.00 21.34 ? 1472 HOH J O   1 
HETATM 14907 O  O   . HOH EB 5 .   ? 8.676  4.093   -67.795  1.00 39.85 ? 1482 HOH J O   1 
HETATM 14908 O  O   . HOH EB 5 .   ? 8.820  8.838   -55.037  1.00 28.62 ? 1490 HOH J O   1 
HETATM 14909 O  O   . HOH EB 5 .   ? 15.306 5.668   -79.449  1.00 38.56 ? 1499 HOH J O   1 
HETATM 14910 O  O   . HOH EB 5 .   ? 10.709 18.428  -50.483  1.00 20.57 ? 1515 HOH J O   1 
HETATM 14911 O  O   . HOH EB 5 .   ? 5.274  22.785  -55.405  1.00 29.01 ? 1516 HOH J O   1 
HETATM 14912 O  O   . HOH EB 5 .   ? 33.761 22.582  -55.132  1.00 43.06 ? 1526 HOH J O   1 
HETATM 14913 O  O   . HOH EB 5 .   ? 18.588 -9.067  -60.722  1.00 45.10 ? 1535 HOH J O   1 
HETATM 14914 O  O   . HOH EB 5 .   ? 30.274 9.648   -46.173  1.00 33.78 ? 1536 HOH J O   1 
HETATM 14915 O  O   . HOH EB 5 .   ? 22.582 23.886  -70.065  1.00 28.73 ? 1539 HOH J O   1 
HETATM 14916 O  O   . HOH EB 5 .   ? 29.034 16.946  -51.422  1.00 28.62 ? 1542 HOH J O   1 
HETATM 14917 O  O   . HOH EB 5 .   ? 19.986 23.408  -59.376  1.00 35.82 ? 1545 HOH J O   1 
HETATM 14918 O  O   . HOH EB 5 .   ? 10.800 -2.154  -61.863  1.00 37.36 ? 1547 HOH J O   1 
HETATM 14919 O  O   . HOH EB 5 .   ? 37.516 13.114  -56.572  1.00 30.17 ? 1556 HOH J O   1 
HETATM 14920 O  O   . HOH EB 5 .   ? 11.487 6.303   -70.730  1.00 35.74 ? 1560 HOH J O   1 
HETATM 14921 O  O   . HOH EB 5 .   ? 28.996 -6.011  -61.924  1.00 39.93 ? 1586 HOH J O   1 
HETATM 14922 O  O   . HOH EB 5 .   ? 3.521  12.175  -71.590  1.00 33.88 ? 1590 HOH J O   1 
HETATM 14923 O  O   . HOH EB 5 .   ? 29.221 -6.806  -59.347  1.00 34.80 ? 1595 HOH J O   1 
HETATM 14924 O  O   . HOH EB 5 .   ? 16.202 -14.423 -57.194  1.00 34.99 ? 1611 HOH J O   1 
HETATM 14925 O  O   . HOH EB 5 .   ? 16.622 -4.330  -63.211  1.00 37.55 ? 1621 HOH J O   1 
HETATM 14926 O  O   . HOH EB 5 .   ? 33.818 1.753   -70.853  1.00 44.87 ? 1630 HOH J O   1 
HETATM 14927 O  O   . HOH EB 5 .   ? 17.554 27.113  -57.935  1.00 68.63 ? 1637 HOH J O   1 
HETATM 14928 O  O   . HOH EB 5 .   ? 27.192 18.606  -50.454  1.00 27.51 ? 1645 HOH J O   1 
HETATM 14929 O  O   . HOH EB 5 .   ? 6.766  23.398  -52.735  1.00 41.19 ? 1652 HOH J O   1 
HETATM 14930 O  O   . HOH EB 5 .   ? 16.248 -0.404  -64.316  1.00 27.98 ? 1669 HOH J O   1 
HETATM 14931 O  O   . HOH EB 5 .   ? 40.991 3.744   -61.755  1.00 34.66 ? 1687 HOH J O   1 
HETATM 14932 O  O   . HOH EB 5 .   ? 12.291 0.991   -67.549  1.00 18.86 ? 1698 HOH J O   1 
HETATM 14933 O  O   . HOH EB 5 .   ? 14.053 0.074   -68.557  1.00 29.89 ? 1714 HOH J O   1 
HETATM 14934 O  O   . HOH EB 5 .   ? 25.297 20.507  -53.432  1.00 31.43 ? 1721 HOH J O   1 
HETATM 14935 O  O   . HOH EB 5 .   ? 30.037 14.600  -51.730  1.00 39.78 ? 1722 HOH J O   1 
HETATM 14936 O  O   . HOH EB 5 .   ? 37.492 11.638  -59.640  1.00 35.72 ? 1723 HOH J O   1 
HETATM 14937 O  O   . HOH EB 5 .   ? 13.045 1.857   -49.446  1.00 30.97 ? 1725 HOH J O   1 
HETATM 14938 O  O   . HOH EB 5 .   ? 10.941 5.996   -49.742  1.00 23.82 ? 1726 HOH J O   1 
HETATM 14939 O  O   . HOH EB 5 .   ? 25.691 26.470  -67.510  1.00 67.44 ? 1734 HOH J O   1 
HETATM 14940 O  O   . HOH FB 5 .   ? 16.058 15.748  -95.667  1.00 26.93 ? 234  HOH K O   1 
HETATM 14941 O  O   . HOH FB 5 .   ? 22.849 17.155  -74.295  1.00 16.58 ? 237  HOH K O   1 
HETATM 14942 O  O   . HOH FB 5 .   ? 26.546 0.221   -81.607  1.00 23.25 ? 263  HOH K O   1 
HETATM 14943 O  O   . HOH FB 5 .   ? 32.699 -0.394  -75.994  1.00 18.41 ? 272  HOH K O   1 
HETATM 14944 O  O   . HOH FB 5 .   ? 22.522 8.913   -78.940  1.00 21.13 ? 329  HOH K O   1 
HETATM 14945 O  O   . HOH FB 5 .   ? 32.970 16.431  -94.548  1.00 22.77 ? 388  HOH K O   1 
HETATM 14946 O  O   . HOH FB 5 .   ? 39.369 3.290   -79.256  1.00 16.14 ? 434  HOH K O   1 
HETATM 14947 O  O   . HOH FB 5 .   ? 36.541 4.811   -74.920  1.00 33.98 ? 466  HOH K O   1 
HETATM 14948 O  O   . HOH FB 5 .   ? 41.230 6.067   -86.085  1.00 23.47 ? 488  HOH K O   1 
HETATM 14949 O  O   . HOH FB 5 .   ? 22.510 -0.251  -82.426  1.00 24.98 ? 529  HOH K O   1 
HETATM 14950 O  O   . HOH FB 5 .   ? 19.340 11.379  -79.616  1.00 28.59 ? 704  HOH K O   1 
HETATM 14951 O  O   . HOH FB 5 .   ? 40.528 19.399  -86.495  1.00 30.68 ? 759  HOH K O   1 
HETATM 14952 O  O   . HOH FB 5 .   ? 12.132 11.499  -99.019  1.00 37.66 ? 826  HOH K O   1 
HETATM 14953 O  O   . HOH FB 5 .   ? 42.230 10.487  -79.586  1.00 23.86 ? 844  HOH K O   1 
HETATM 14954 O  O   . HOH FB 5 .   ? 31.616 9.624   -95.906  1.00 23.25 ? 897  HOH K O   1 
HETATM 14955 O  O   . HOH FB 5 .   ? 46.434 4.140   -78.937  1.00 23.21 ? 908  HOH K O   1 
HETATM 14956 O  O   . HOH FB 5 .   ? 42.630 12.488  -93.984  1.00 29.69 ? 918  HOH K O   1 
HETATM 14957 O  O   . HOH FB 5 .   ? 27.241 25.142  -77.324  1.00 32.95 ? 944  HOH K O   1 
HETATM 14958 O  O   . HOH FB 5 .   ? 35.227 13.565  -76.374  1.00 23.88 ? 949  HOH K O   1 
HETATM 14959 O  O   . HOH FB 5 .   ? 41.273 7.310   -73.758  1.00 29.64 ? 972  HOH K O   1 
HETATM 14960 O  O   . HOH FB 5 .   ? 42.612 5.805   -79.744  1.00 21.44 ? 978  HOH K O   1 
HETATM 14961 O  O   . HOH FB 5 .   ? 13.295 12.769  -85.478  1.00 28.73 ? 983  HOH K O   1 
HETATM 14962 O  O   . HOH FB 5 .   ? 20.214 16.606  -101.088 1.00 39.30 ? 996  HOH K O   1 
HETATM 14963 O  O   . HOH FB 5 .   ? 19.945 24.004  -87.681  1.00 31.41 ? 1000 HOH K O   1 
HETATM 14964 O  O   . HOH FB 5 .   ? 36.596 13.532  -99.138  1.00 30.11 ? 1004 HOH K O   1 
HETATM 14965 O  O   . HOH FB 5 .   ? 43.780 5.984   -75.366  1.00 36.72 ? 1033 HOH K O   1 
HETATM 14966 O  O   . HOH FB 5 .   ? 18.020 9.981   -78.144  1.00 21.02 ? 1046 HOH K O   1 
HETATM 14967 O  O   . HOH FB 5 .   ? 12.206 6.130   -95.107  1.00 21.10 ? 1053 HOH K O   1 
HETATM 14968 O  O   . HOH FB 5 .   ? 39.761 17.554  -77.782  1.00 37.71 ? 1121 HOH K O   1 
HETATM 14969 O  O   . HOH FB 5 .   ? 25.324 6.469   -97.201  1.00 28.38 ? 1133 HOH K O   1 
HETATM 14970 O  O   . HOH FB 5 .   ? 40.513 -0.839  -85.407  1.00 27.35 ? 1135 HOH K O   1 
HETATM 14971 O  O   . HOH FB 5 .   ? 42.485 16.484  -88.260  1.00 27.31 ? 1201 HOH K O   1 
HETATM 14972 O  O   . HOH FB 5 .   ? 38.665 11.411  -82.925  1.00 20.21 ? 1222 HOH K O   1 
HETATM 14973 O  O   . HOH FB 5 .   ? 23.008 16.392  -79.286  1.00 40.40 ? 1226 HOH K O   1 
HETATM 14974 O  O   . HOH FB 5 .   ? 18.769 14.160  -80.521  1.00 27.36 ? 1252 HOH K O   1 
HETATM 14975 O  O   . HOH FB 5 .   ? 37.877 14.779  -77.123  1.00 28.91 ? 1255 HOH K O   1 
HETATM 14976 O  O   . HOH FB 5 .   ? 32.175 24.168  -88.522  1.00 28.78 ? 1290 HOH K O   1 
HETATM 14977 O  O   . HOH FB 5 .   ? 21.003 14.892  -78.748  1.00 24.66 ? 1295 HOH K O   1 
HETATM 14978 O  O   . HOH FB 5 .   ? 27.746 5.973   -96.329  1.00 26.35 ? 1300 HOH K O   1 
HETATM 14979 O  O   . HOH FB 5 .   ? 16.213 19.099  -76.591  1.00 43.54 ? 1330 HOH K O   1 
HETATM 14980 O  O   . HOH FB 5 .   ? 39.371 15.707  -74.594  1.00 34.27 ? 1348 HOH K O   1 
HETATM 14981 O  O   . HOH FB 5 .   ? 24.339 24.788  -72.143  1.00 30.65 ? 1365 HOH K O   1 
HETATM 14982 O  O   . HOH FB 5 .   ? 43.351 -4.136  -86.381  1.00 39.88 ? 1416 HOH K O   1 
HETATM 14983 O  O   . HOH FB 5 .   ? 45.484 10.396  -76.031  1.00 38.81 ? 1422 HOH K O   1 
HETATM 14984 O  O   . HOH FB 5 .   ? 39.874 0.867   -79.744  1.00 23.61 ? 1452 HOH K O   1 
HETATM 14985 O  O   . HOH FB 5 .   ? 40.011 7.948   -93.047  1.00 30.50 ? 1486 HOH K O   1 
HETATM 14986 O  O   . HOH FB 5 .   ? 29.546 29.703  -90.067  1.00 33.77 ? 1503 HOH K O   1 
HETATM 14987 O  O   . HOH FB 5 .   ? 29.431 8.046   -96.740  1.00 27.65 ? 1520 HOH K O   1 
HETATM 14988 O  O   . HOH FB 5 .   ? 46.806 -1.115  -81.082  1.00 27.76 ? 1546 HOH K O   1 
HETATM 14989 O  O   . HOH FB 5 .   ? 21.552 11.541  -77.936  1.00 21.38 ? 1552 HOH K O   1 
HETATM 14990 O  O   . HOH FB 5 .   ? 37.554 -0.944  -86.475  1.00 43.66 ? 1558 HOH K O   1 
HETATM 14991 O  O   . HOH FB 5 .   ? 22.012 4.776   -99.061  1.00 31.74 ? 1561 HOH K O   1 
HETATM 14992 O  O   . HOH FB 5 .   ? 15.647 23.024  -85.810  1.00 37.10 ? 1570 HOH K O   1 
HETATM 14993 O  O   . HOH FB 5 .   ? 26.536 2.584   -97.913  1.00 34.93 ? 1574 HOH K O   1 
HETATM 14994 O  O   . HOH FB 5 .   ? 35.834 20.077  -76.695  1.00 40.87 ? 1576 HOH K O   1 
HETATM 14995 O  O   . HOH FB 5 .   ? 22.942 18.971  -80.128  1.00 35.44 ? 1606 HOH K O   1 
HETATM 14996 O  O   . HOH FB 5 .   ? 48.201 -3.829  -81.734  1.00 44.32 ? 1644 HOH K O   1 
HETATM 14997 O  O   . HOH FB 5 .   ? 35.309 21.619  -74.470  1.00 30.28 ? 1651 HOH K O   1 
HETATM 14998 O  O   . HOH FB 5 .   ? 15.065 2.417   -99.273  1.00 37.87 ? 1684 HOH K O   1 
HETATM 14999 O  O   . HOH FB 5 .   ? 31.110 -3.419  -72.634  1.00 27.05 ? 1735 HOH K O   1 
HETATM 15000 O  O   . HOH FB 5 .   ? 23.493 -3.709  -87.823  1.00 34.74 ? 1736 HOH K O   1 
HETATM 15001 O  O   . HOH FB 5 .   ? 41.533 -2.715  -86.995  1.00 36.03 ? 1737 HOH K O   1 
HETATM 15002 O  O   . HOH FB 5 .   ? 34.272 7.970   -96.001  1.00 32.27 ? 1738 HOH K O   1 
HETATM 15003 O  O   . HOH FB 5 .   ? 38.831 19.851  -99.409  1.00 34.23 ? 1739 HOH K O   1 
HETATM 15004 O  O   . HOH FB 5 .   ? 25.399 -5.310  -77.854  1.00 33.81 ? 1740 HOH K O   1 
HETATM 15005 O  O   . HOH GB 5 .   ? 53.122 16.144  -41.250  1.00 3.01  ? 154  HOH L O   1 
HETATM 15006 O  O   . HOH GB 5 .   ? 60.333 12.978  -40.110  1.00 7.74  ? 155  HOH L O   1 
HETATM 15007 O  O   . HOH GB 5 .   ? 54.666 5.687   -48.034  1.00 8.07  ? 156  HOH L O   1 
HETATM 15008 O  O   . HOH GB 5 .   ? 55.170 12.028  -36.060  1.00 12.35 ? 157  HOH L O   1 
HETATM 15009 O  O   . HOH GB 5 .   ? 43.436 1.767   -61.853  1.00 16.89 ? 158  HOH L O   1 
HETATM 15010 O  O   . HOH GB 5 .   ? 47.532 9.823   -56.130  1.00 11.70 ? 159  HOH L O   1 
HETATM 15011 O  O   . HOH GB 5 .   ? 71.181 1.340   -47.452  1.00 8.74  ? 160  HOH L O   1 
HETATM 15012 O  O   . HOH GB 5 .   ? 73.581 0.499   -48.462  1.00 16.15 ? 161  HOH L O   1 
HETATM 15013 O  O   . HOH GB 5 .   ? 63.033 11.273  -51.167  1.00 11.07 ? 162  HOH L O   1 
HETATM 15014 O  O   . HOH GB 5 .   ? 49.621 13.917  -41.911  1.00 15.41 ? 163  HOH L O   1 
HETATM 15015 O  O   . HOH GB 5 .   ? 64.324 12.711  -53.811  1.00 25.47 ? 164  HOH L O   1 
HETATM 15016 O  O   . HOH GB 5 .   ? 60.711 20.328  -45.387  1.00 13.29 ? 168  HOH L O   1 
HETATM 15017 O  O   . HOH GB 5 .   ? 68.733 10.361  -55.010  1.00 21.66 ? 170  HOH L O   1 
HETATM 15018 O  O   . HOH GB 5 .   ? 70.744 3.891   -46.306  1.00 14.75 ? 173  HOH L O   1 
HETATM 15019 O  O   . HOH GB 5 .   ? 62.736 -7.935  -44.118  1.00 15.28 ? 198  HOH L O   1 
HETATM 15020 O  O   . HOH GB 5 .   ? 60.425 -2.518  -39.036  1.00 17.80 ? 199  HOH L O   1 
HETATM 15021 O  O   . HOH GB 5 .   ? 44.458 6.639   -53.137  1.00 24.63 ? 201  HOH L O   1 
HETATM 15022 O  O   . HOH GB 5 .   ? 57.135 13.081  -54.311  1.00 8.23  ? 220  HOH L O   1 
HETATM 15023 O  O   . HOH GB 5 .   ? 72.678 1.360   -54.546  1.00 24.61 ? 228  HOH L O   1 
HETATM 15024 O  O   . HOH GB 5 .   ? 50.997 -0.948  -43.825  1.00 22.99 ? 238  HOH L O   1 
HETATM 15025 O  O   . HOH GB 5 .   ? 59.707 12.265  -54.649  1.00 11.23 ? 243  HOH L O   1 
HETATM 15026 O  O   . HOH GB 5 .   ? 73.146 -7.380  -47.713  1.00 11.29 ? 250  HOH L O   1 
HETATM 15027 O  O   . HOH GB 5 .   ? 48.816 11.749  -45.472  1.00 14.26 ? 260  HOH L O   1 
HETATM 15028 O  O   . HOH GB 5 .   ? 52.717 14.486  -36.244  1.00 9.56  ? 266  HOH L O   1 
HETATM 15029 O  O   . HOH GB 5 .   ? 55.366 -1.151  -46.153  1.00 12.08 ? 279  HOH L O   1 
HETATM 15030 O  O   . HOH GB 5 .   ? 75.562 -5.372  -51.847  1.00 16.09 ? 289  HOH L O   1 
HETATM 15031 O  O   . HOH GB 5 .   ? 45.727 -0.675  -49.484  1.00 19.62 ? 317  HOH L O   1 
HETATM 15032 O  O   . HOH GB 5 .   ? 50.534 3.457   -43.505  1.00 13.46 ? 322  HOH L O   1 
HETATM 15033 O  O   . HOH GB 5 .   ? 60.655 -5.461  -45.323  1.00 18.09 ? 326  HOH L O   1 
HETATM 15034 O  O   . HOH GB 5 .   ? 45.996 8.827   -54.148  1.00 14.13 ? 332  HOH L O   1 
HETATM 15035 O  O   . HOH GB 5 .   ? 75.427 -9.351  -44.924  1.00 15.76 ? 337  HOH L O   1 
HETATM 15036 O  O   . HOH GB 5 .   ? 53.697 -6.674  -44.756  1.00 20.52 ? 351  HOH L O   1 
HETATM 15037 O  O   . HOH GB 5 .   ? 50.807 -5.114  -46.576  1.00 17.13 ? 354  HOH L O   1 
HETATM 15038 O  O   . HOH GB 5 .   ? 56.177 8.213   -38.898  1.00 19.20 ? 386  HOH L O   1 
HETATM 15039 O  O   . HOH GB 5 .   ? 50.578 8.095   -41.859  1.00 17.16 ? 393  HOH L O   1 
HETATM 15040 O  O   . HOH GB 5 .   ? 64.958 2.125   -38.979  1.00 19.79 ? 402  HOH L O   1 
HETATM 15041 O  O   . HOH GB 5 .   ? 57.708 5.681   -40.273  1.00 20.99 ? 414  HOH L O   1 
HETATM 15042 O  O   . HOH GB 5 .   ? 52.511 15.519  -52.584  1.00 24.04 ? 423  HOH L O   1 
HETATM 15043 O  O   . HOH GB 5 .   ? 47.660 -4.711  -46.504  1.00 29.38 ? 427  HOH L O   1 
HETATM 15044 O  O   . HOH GB 5 .   ? 42.933 7.564   -43.609  1.00 27.70 ? 436  HOH L O   1 
HETATM 15045 O  O   . HOH GB 5 .   ? 42.481 4.906   -54.486  1.00 27.25 ? 450  HOH L O   1 
HETATM 15046 O  O   . HOH GB 5 .   ? 63.182 9.956   -42.253  1.00 15.80 ? 477  HOH L O   1 
HETATM 15047 O  O   . HOH GB 5 .   ? 41.664 6.631   -68.359  1.00 25.13 ? 504  HOH L O   1 
HETATM 15048 O  O   . HOH GB 5 .   ? 41.712 13.638  -54.318  1.00 35.07 ? 512  HOH L O   1 
HETATM 15049 O  O   . HOH GB 5 .   ? 67.407 13.583  -46.734  1.00 27.65 ? 527  HOH L O   1 
HETATM 15050 O  O   . HOH GB 5 .   ? 64.044 14.049  -58.977  1.00 22.70 ? 538  HOH L O   1 
HETATM 15051 O  O   . HOH GB 5 .   ? 52.569 10.393  -65.854  1.00 23.39 ? 542  HOH L O   1 
HETATM 15052 O  O   . HOH GB 5 .   ? 50.594 -10.987 -66.489  1.00 21.24 ? 550  HOH L O   1 
HETATM 15053 O  O   . HOH GB 5 .   ? 44.330 10.100  -44.434  1.00 16.15 ? 553  HOH L O   1 
HETATM 15054 O  O   . HOH GB 5 .   ? 53.953 13.251  -56.136  1.00 25.38 ? 586  HOH L O   1 
HETATM 15055 O  O   . HOH GB 5 .   ? 49.625 -1.539  -48.620  1.00 23.07 ? 606  HOH L O   1 
HETATM 15056 O  O   . HOH GB 5 .   ? 50.853 12.804  -37.248  1.00 11.53 ? 617  HOH L O   1 
HETATM 15057 O  O   . HOH GB 5 .   ? 75.994 -0.116  -46.772  1.00 18.13 ? 621  HOH L O   1 
HETATM 15058 O  O   . HOH GB 5 .   ? 75.792 -1.616  -44.694  1.00 17.00 ? 632  HOH L O   1 
HETATM 15059 O  O   . HOH GB 5 .   ? 56.786 1.909   -41.361  1.00 18.92 ? 646  HOH L O   1 
HETATM 15060 O  O   . HOH GB 5 .   ? 53.151 -1.958  -45.126  1.00 23.17 ? 653  HOH L O   1 
HETATM 15061 O  O   . HOH GB 5 .   ? 59.914 -1.330  -34.955  1.00 21.38 ? 658  HOH L O   1 
HETATM 15062 O  O   . HOH GB 5 .   ? 66.902 3.525   -41.844  1.00 19.22 ? 659  HOH L O   1 
HETATM 15063 O  O   . HOH GB 5 .   ? 43.375 -9.043  -56.915  1.00 19.83 ? 665  HOH L O   1 
HETATM 15064 O  O   . HOH GB 5 .   ? 63.293 19.480  -45.062  1.00 13.63 ? 676  HOH L O   1 
HETATM 15065 O  O   . HOH GB 5 .   ? 60.045 -0.517  -37.520  1.00 20.73 ? 677  HOH L O   1 
HETATM 15066 O  O   . HOH GB 5 .   ? 46.541 -10.310 -56.100  1.00 28.95 ? 681  HOH L O   1 
HETATM 15067 O  O   . HOH GB 5 .   ? 52.163 1.297   -43.118  1.00 17.74 ? 688  HOH L O   1 
HETATM 15068 O  O   . HOH GB 5 .   ? 73.068 -1.331  -57.022  1.00 21.24 ? 690  HOH L O   1 
HETATM 15069 O  O   . HOH GB 5 .   ? 63.020 -3.647  -64.228  1.00 20.31 ? 696  HOH L O   1 
HETATM 15070 O  O   . HOH GB 5 .   ? 51.623 14.454  -45.442  1.00 22.14 ? 709  HOH L O   1 
HETATM 15071 O  O   . HOH GB 5 .   ? 44.260 -2.251  -56.951  1.00 21.45 ? 737  HOH L O   1 
HETATM 15072 O  O   . HOH GB 5 .   ? 58.795 24.240  -46.705  1.00 16.81 ? 741  HOH L O   1 
HETATM 15073 O  O   . HOH GB 5 .   ? 49.842 14.408  -39.333  1.00 18.11 ? 748  HOH L O   1 
HETATM 15074 O  O   . HOH GB 5 .   ? 61.918 12.900  -65.680  1.00 22.61 ? 762  HOH L O   1 
HETATM 15075 O  O   . HOH GB 5 .   ? 60.954 10.362  -52.833  1.00 15.46 ? 767  HOH L O   1 
HETATM 15076 O  O   . HOH GB 5 .   ? 73.079 4.621   -47.846  1.00 23.55 ? 778  HOH L O   1 
HETATM 15077 O  O   . HOH GB 5 .   ? 57.091 -11.266 -61.425  1.00 34.33 ? 783  HOH L O   1 
HETATM 15078 O  O   . HOH GB 5 .   ? 40.338 -3.828  -53.509  1.00 39.46 ? 785  HOH L O   1 
HETATM 15079 O  O   . HOH GB 5 .   ? 64.060 11.284  -38.493  1.00 21.01 ? 813  HOH L O   1 
HETATM 15080 O  O   . HOH GB 5 .   ? 51.989 11.097  -60.852  1.00 16.92 ? 829  HOH L O   1 
HETATM 15081 O  O   . HOH GB 5 .   ? 67.479 11.108  -57.028  1.00 27.35 ? 833  HOH L O   1 
HETATM 15082 O  O   . HOH GB 5 .   ? 66.034 6.389   -41.371  1.00 21.63 ? 836  HOH L O   1 
HETATM 15083 O  O   . HOH GB 5 .   ? 61.485 14.227  -58.154  1.00 19.89 ? 868  HOH L O   1 
HETATM 15084 O  O   . HOH GB 5 .   ? 69.292 2.358   -41.971  1.00 26.37 ? 877  HOH L O   1 
HETATM 15085 O  O   . HOH GB 5 .   ? 47.424 -4.780  -67.511  1.00 16.61 ? 882  HOH L O   1 
HETATM 15086 O  O   . HOH GB 5 .   ? 65.947 -4.616  -38.691  1.00 20.70 ? 919  HOH L O   1 
HETATM 15087 O  O   . HOH GB 5 .   ? 48.805 4.707   -65.181  1.00 20.94 ? 923  HOH L O   1 
HETATM 15088 O  O   . HOH GB 5 .   ? 68.225 12.930  -50.673  1.00 40.50 ? 925  HOH L O   1 
HETATM 15089 O  O   . HOH GB 5 .   ? 73.963 2.662   -50.053  1.00 18.83 ? 939  HOH L O   1 
HETATM 15090 O  O   . HOH GB 5 .   ? 68.222 -8.653  -37.703  1.00 23.08 ? 942  HOH L O   1 
HETATM 15091 O  O   . HOH GB 5 .   ? 73.177 2.398   -52.491  1.00 25.60 ? 946  HOH L O   1 
HETATM 15092 O  O   . HOH GB 5 .   ? 51.904 -9.885  -46.296  1.00 36.35 ? 956  HOH L O   1 
HETATM 15093 O  O   . HOH GB 5 .   ? 70.175 9.370   -59.536  1.00 29.26 ? 966  HOH L O   1 
HETATM 15094 O  O   . HOH GB 5 .   ? 49.499 8.151   -35.135  1.00 23.74 ? 1001 HOH L O   1 
HETATM 15095 O  O   . HOH GB 5 .   ? 52.466 -10.486 -50.492  1.00 31.72 ? 1019 HOH L O   1 
HETATM 15096 O  O   . HOH GB 5 .   ? 69.681 -12.123 -43.769  1.00 23.45 ? 1024 HOH L O   1 
HETATM 15097 O  O   . HOH GB 5 .   ? 58.028 -13.219 -66.882  1.00 24.53 ? 1037 HOH L O   1 
HETATM 15098 O  O   . HOH GB 5 .   ? 63.843 4.489   -68.583  1.00 26.49 ? 1042 HOH L O   1 
HETATM 15099 O  O   . HOH GB 5 .   ? 61.778 -13.379 -56.650  1.00 24.97 ? 1052 HOH L O   1 
HETATM 15100 O  O   . HOH GB 5 .   ? 42.436 -1.081  -61.401  1.00 23.61 ? 1061 HOH L O   1 
HETATM 15101 O  O   . HOH GB 5 .   ? 57.440 1.435   -37.991  1.00 23.04 ? 1069 HOH L O   1 
HETATM 15102 O  O   . HOH GB 5 .   ? 61.784 -3.824  -37.162  1.00 24.02 ? 1071 HOH L O   1 
HETATM 15103 O  O   . HOH GB 5 .   ? 52.392 14.101  -59.737  1.00 33.42 ? 1089 HOH L O   1 
HETATM 15104 O  O   . HOH GB 5 .   ? 71.521 0.760   -39.565  1.00 28.90 ? 1090 HOH L O   1 
HETATM 15105 O  O   . HOH GB 5 .   ? 41.978 11.884  -48.606  1.00 27.56 ? 1124 HOH L O   1 
HETATM 15106 O  O   . HOH GB 5 .   ? 62.745 12.326  -40.962  1.00 19.40 ? 1125 HOH L O   1 
HETATM 15107 O  O   . HOH GB 5 .   ? 64.607 -1.525  -65.223  1.00 24.42 ? 1128 HOH L O   1 
HETATM 15108 O  O   . HOH GB 5 .   ? 64.793 -2.400  -37.629  1.00 31.79 ? 1130 HOH L O   1 
HETATM 15109 O  O   . HOH GB 5 .   ? 65.671 15.951  -43.163  1.00 18.64 ? 1143 HOH L O   1 
HETATM 15110 O  O   . HOH GB 5 .   ? 59.662 20.138  -49.875  1.00 33.26 ? 1157 HOH L O   1 
HETATM 15111 O  O   . HOH GB 5 .   ? 40.242 6.225   -58.107  1.00 30.04 ? 1160 HOH L O   1 
HETATM 15112 O  O   . HOH GB 5 .   ? 65.125 8.846   -40.662  1.00 27.22 ? 1172 HOH L O   1 
HETATM 15113 O  O   . HOH GB 5 .   ? 44.169 -7.987  -62.670  1.00 40.91 ? 1174 HOH L O   1 
HETATM 15114 O  O   . HOH GB 5 .   ? 39.647 -8.559  -63.334  1.00 24.48 ? 1181 HOH L O   1 
HETATM 15115 O  O   . HOH GB 5 .   ? 44.697 3.673   -48.327  1.00 29.33 ? 1184 HOH L O   1 
HETATM 15116 O  O   . HOH GB 5 .   ? 52.608 6.413   -35.695  1.00 39.89 ? 1185 HOH L O   1 
HETATM 15117 O  O   . HOH GB 5 .   ? 69.039 -7.484  -58.721  1.00 35.49 ? 1191 HOH L O   1 
HETATM 15118 O  O   . HOH GB 5 .   ? 60.781 11.574  -68.043  1.00 24.82 ? 1193 HOH L O   1 
HETATM 15119 O  O   . HOH GB 5 .   ? 75.237 -4.185  -55.686  1.00 24.60 ? 1204 HOH L O   1 
HETATM 15120 O  O   . HOH GB 5 .   ? 55.480 9.544   -35.875  1.00 30.56 ? 1245 HOH L O   1 
HETATM 15121 O  O   . HOH GB 5 .   ? 66.305 1.259   -64.540  1.00 27.93 ? 1254 HOH L O   1 
HETATM 15122 O  O   . HOH GB 5 .   ? 75.782 -0.531  -42.297  1.00 26.47 ? 1260 HOH L O   1 
HETATM 15123 O  O   . HOH GB 5 .   ? 50.489 -10.973 -48.854  1.00 43.94 ? 1263 HOH L O   1 
HETATM 15124 O  O   . HOH GB 5 .   ? 46.891 7.841   -64.319  1.00 22.41 ? 1277 HOH L O   1 
HETATM 15125 O  O   . HOH GB 5 .   ? 48.796 9.652   -64.474  1.00 22.78 ? 1291 HOH L O   1 
HETATM 15126 O  O   . HOH GB 5 .   ? 42.051 -1.124  -57.870  1.00 31.88 ? 1310 HOH L O   1 
HETATM 15127 O  O   . HOH GB 5 .   ? 69.402 12.222  -48.099  1.00 30.68 ? 1323 HOH L O   1 
HETATM 15128 O  O   . HOH GB 5 .   ? 48.512 -0.693  -45.782  1.00 21.58 ? 1339 HOH L O   1 
HETATM 15129 O  O   . HOH GB 5 .   ? 46.512 3.689   -39.609  1.00 33.38 ? 1345 HOH L O   1 
HETATM 15130 O  O   . HOH GB 5 .   ? 50.065 11.253  -62.589  1.00 25.36 ? 1347 HOH L O   1 
HETATM 15131 O  O   . HOH GB 5 .   ? 69.331 -13.859 -41.215  1.00 22.83 ? 1350 HOH L O   1 
HETATM 15132 O  O   . HOH GB 5 .   ? 69.040 2.260   -62.183  1.00 40.58 ? 1357 HOH L O   1 
HETATM 15133 O  O   . HOH GB 5 .   ? 67.495 -0.729  -62.926  1.00 29.08 ? 1364 HOH L O   1 
HETATM 15134 O  O   . HOH GB 5 .   ? 65.966 13.279  -56.898  1.00 34.54 ? 1373 HOH L O   1 
HETATM 15135 O  O   . HOH GB 5 .   ? 65.409 -3.891  -34.600  1.00 32.46 ? 1395 HOH L O   1 
HETATM 15136 O  O   . HOH GB 5 .   ? 39.671 8.628   -56.779  1.00 40.58 ? 1397 HOH L O   1 
HETATM 15137 O  O   . HOH GB 5 .   ? 59.298 -11.909 -49.828  1.00 28.65 ? 1446 HOH L O   1 
HETATM 15138 O  O   . HOH GB 5 .   ? 45.665 12.590  -62.901  1.00 30.20 ? 1447 HOH L O   1 
HETATM 15139 O  O   . HOH GB 5 .   ? 45.490 17.057  -50.837  1.00 37.02 ? 1449 HOH L O   1 
HETATM 15140 O  O   . HOH GB 5 .   ? 71.213 -12.706 -39.169  1.00 30.15 ? 1450 HOH L O   1 
HETATM 15141 O  O   . HOH GB 5 .   ? 54.976 15.387  -62.320  1.00 38.55 ? 1453 HOH L O   1 
HETATM 15142 O  O   . HOH GB 5 .   ? 64.112 10.699  -71.201  1.00 37.70 ? 1465 HOH L O   1 
HETATM 15143 O  O   . HOH GB 5 .   ? 61.131 -12.998 -51.507  1.00 38.81 ? 1468 HOH L O   1 
HETATM 15144 O  O   . HOH GB 5 .   ? 60.759 17.764  -52.695  1.00 36.23 ? 1476 HOH L O   1 
HETATM 15145 O  O   . HOH GB 5 .   ? 63.609 17.101  -44.145  1.00 46.51 ? 1478 HOH L O   1 
HETATM 15146 O  O   . HOH GB 5 .   ? 52.199 20.499  -48.212  1.00 30.53 ? 1492 HOH L O   1 
HETATM 15147 O  O   . HOH GB 5 .   ? 74.672 -12.920 -39.511  1.00 40.74 ? 1493 HOH L O   1 
HETATM 15148 O  O   . HOH GB 5 .   ? 66.707 13.243  -66.900  1.00 31.98 ? 1494 HOH L O   1 
HETATM 15149 O  O   . HOH GB 5 .   ? 63.081 -11.576 -55.119  1.00 26.94 ? 1496 HOH L O   1 
HETATM 15150 O  O   . HOH GB 5 .   ? 45.044 5.669   -67.622  1.00 31.53 ? 1518 HOH L O   1 
HETATM 15151 O  O   . HOH GB 5 .   ? 41.547 -2.312  -55.165  1.00 32.26 ? 1527 HOH L O   1 
HETATM 15152 O  O   . HOH GB 5 .   ? 70.572 6.983   -59.482  1.00 34.88 ? 1562 HOH L O   1 
HETATM 15153 O  O   . HOH GB 5 .   ? 61.351 14.315  -55.242  1.00 37.70 ? 1563 HOH L O   1 
HETATM 15154 O  O   . HOH GB 5 .   ? 65.608 -12.332 -42.321  1.00 37.50 ? 1567 HOH L O   1 
HETATM 15155 O  O   . HOH GB 5 .   ? 65.366 12.992  -70.825  1.00 34.97 ? 1572 HOH L O   1 
HETATM 15156 O  O   . HOH GB 5 .   ? 38.234 -8.566  -56.112  1.00 35.01 ? 1577 HOH L O   1 
HETATM 15157 O  O   . HOH GB 5 .   ? 44.747 -0.440  -68.323  1.00 35.92 ? 1578 HOH L O   1 
HETATM 15158 O  O   . HOH GB 5 .   ? 71.879 -11.272 -57.279  1.00 29.15 ? 1583 HOH L O   1 
HETATM 15159 O  O   . HOH GB 5 .   ? 54.726 -11.658 -60.611  1.00 27.96 ? 1585 HOH L O   1 
HETATM 15160 O  O   . HOH GB 5 .   ? 42.124 14.726  -50.873  1.00 30.09 ? 1603 HOH L O   1 
HETATM 15161 O  O   . HOH GB 5 .   ? 41.306 -0.652  -64.196  1.00 31.68 ? 1616 HOH L O   1 
HETATM 15162 O  O   . HOH GB 5 .   ? 52.151 15.341  -63.430  1.00 38.29 ? 1618 HOH L O   1 
HETATM 15163 O  O   . HOH GB 5 .   ? 51.184 20.539  -45.261  1.00 38.02 ? 1638 HOH L O   1 
HETATM 15164 O  O   . HOH GB 5 .   ? 40.651 6.159   -60.852  1.00 33.19 ? 1696 HOH L O   1 
HETATM 15165 O  O   . HOH GB 5 .   ? 74.755 -7.464  -53.072  1.00 46.03 ? 1702 HOH L O   1 
HETATM 15166 O  O   . HOH GB 5 .   ? 39.298 7.631   -51.296  1.00 35.97 ? 1724 HOH L O   1 
HETATM 15167 O  O   . HOH GB 5 .   ? 56.184 3.208   -39.447  1.00 26.17 ? 1741 HOH L O   1 
HETATM 15168 O  O   . HOH GB 5 .   ? 59.902 5.969   -39.144  1.00 24.70 ? 1742 HOH L O   1 
HETATM 15169 O  O   . HOH GB 5 .   ? 62.285 5.983   -38.209  1.00 27.02 ? 1743 HOH L O   1 
HETATM 15170 O  O   . HOH GB 5 .   ? 60.394 10.293  -38.702  1.00 17.02 ? 1744 HOH L O   1 
HETATM 15171 O  O   . HOH HB 5 .   ? 55.818 -9.923  -93.250  1.00 32.48 ? 318  HOH M O   1 
HETATM 15172 O  O   . HOH HB 5 .   ? 78.928 -3.987  -80.086  1.00 30.99 ? 319  HOH M O   1 
HETATM 15173 O  O   . HOH HB 5 .   ? 49.908 -4.328  -74.095  1.00 32.31 ? 461  HOH M O   1 
HETATM 15174 O  O   . HOH HB 5 .   ? 80.658 4.103   -80.383  1.00 27.24 ? 480  HOH M O   1 
HETATM 15175 O  O   . HOH HB 5 .   ? 48.385 4.751   -86.805  1.00 35.63 ? 559  HOH M O   1 
HETATM 15176 O  O   . HOH HB 5 .   ? 49.072 7.981   -77.121  1.00 26.20 ? 661  HOH M O   1 
HETATM 15177 O  O   . HOH HB 5 .   ? 64.527 2.577   -69.615  1.00 27.71 ? 710  HOH M O   1 
HETATM 15178 O  O   . HOH HB 5 .   ? 64.889 -1.024  -68.054  1.00 28.06 ? 755  HOH M O   1 
HETATM 15179 O  O   . HOH HB 5 .   ? 62.422 -6.153  -65.201  1.00 21.13 ? 805  HOH M O   1 
HETATM 15180 O  O   . HOH HB 5 .   ? 42.241 -0.226  -76.150  1.00 30.94 ? 854  HOH M O   1 
HETATM 15181 O  O   . HOH HB 5 .   ? 49.700 5.297   -72.083  1.00 35.81 ? 863  HOH M O   1 
HETATM 15182 O  O   . HOH HB 5 .   ? 45.049 2.819   -72.721  1.00 36.96 ? 864  HOH M O   1 
HETATM 15183 O  O   . HOH HB 5 .   ? 48.590 -7.004  -75.472  1.00 35.99 ? 955  HOH M O   1 
HETATM 15184 O  O   . HOH HB 5 .   ? 50.417 4.834   -84.054  1.00 22.64 ? 985  HOH M O   1 
HETATM 15185 O  O   . HOH HB 5 .   ? 61.845 11.013  -85.134  1.00 29.44 ? 1080 HOH M O   1 
HETATM 15186 O  O   . HOH HB 5 .   ? 63.017 7.783   -90.651  1.00 33.13 ? 1097 HOH M O   1 
HETATM 15187 O  O   . HOH HB 5 .   ? 45.819 -2.805  -68.976  1.00 28.88 ? 1103 HOH M O   1 
HETATM 15188 O  O   . HOH HB 5 .   ? 47.163 -0.081  -78.321  1.00 26.31 ? 1107 HOH M O   1 
HETATM 15189 O  O   . HOH HB 5 .   ? 53.771 10.433  -71.613  1.00 30.04 ? 1366 HOH M O   1 
HETATM 15190 O  O   . HOH HB 5 .   ? 60.661 5.647   -90.094  1.00 32.00 ? 1369 HOH M O   1 
HETATM 15191 O  O   . HOH HB 5 .   ? 60.011 -12.917 -63.220  1.00 33.91 ? 1381 HOH M O   1 
HETATM 15192 O  O   . HOH HB 5 .   ? 79.763 4.114   -92.363  1.00 27.46 ? 1417 HOH M O   1 
HETATM 15193 O  O   . HOH HB 5 .   ? 51.581 -1.029  -79.688  1.00 31.55 ? 1418 HOH M O   1 
HETATM 15194 O  O   . HOH HB 5 .   ? 61.738 10.840  -74.214  1.00 35.25 ? 1537 HOH M O   1 
HETATM 15195 O  O   . HOH HB 5 .   ? 45.314 -3.102  -71.622  1.00 34.60 ? 1596 HOH M O   1 
HETATM 15196 O  O   . HOH HB 5 .   ? 70.394 -13.282 -76.165  1.00 36.56 ? 1667 HOH M O   1 
HETATM 15197 O  O   . HOH HB 5 .   ? 71.446 -10.212 -73.117  1.00 43.99 ? 1691 HOH M O   1 
HETATM 15198 O  O   . HOH HB 5 .   ? 68.436 -4.316  -68.897  1.00 40.50 ? 1693 HOH M O   1 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   1   ALA ALA A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  CYS 57  57  57  CYS CYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 CME 111 111 111 CME CME A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
B 1 1   ALA 1   1   1   ALA ALA B . n 
B 1 2   THR 2   2   2   THR THR B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   ALA 4   4   4   ALA ALA B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   CYS 6   6   6   CYS CYS B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   LEU 8   8   8   LEU LEU B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  GLY 10  10  10  GLY GLY B . n 
B 1 11  ASP 11  11  11  ASP ASP B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  GLN 15  15  15  GLN GLN B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  ILE 17  17  17  ILE ILE B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  ASN 19  19  19  ASN ASN B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  GLN 22  22  22  GLN GLN B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  SER 25  25  25  SER SER B . n 
B 1 26  ASN 26  26  26  ASN ASN B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  TRP 32  32  32  TRP TRP B . n 
B 1 33  GLY 33  33  33  GLY GLY B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  THR 39  39  39  THR THR B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  LEU 42  42  42  LEU LEU B . n 
B 1 43  HIS 43  43  43  HIS HIS B . n 
B 1 44  GLY 44  44  44  GLY GLY B . n 
B 1 45  PHE 45  45  45  PHE PHE B . n 
B 1 46  HIS 46  46  46  HIS HIS B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  HIS 48  48  48  HIS HIS B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  PHE 50  50  50  PHE PHE B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ASP 52  52  52  ASP ASP B . n 
B 1 53  ASN 53  53  53  ASN ASN B . n 
B 1 54  THR 54  54  54  THR THR B . n 
B 1 55  ALA 55  55  55  ALA ALA B . n 
B 1 56  GLY 56  56  56  GLY GLY B . n 
B 1 57  CYS 57  57  57  CYS CYS B . n 
B 1 58  THR 58  58  58  THR THR B . n 
B 1 59  SER 59  59  59  SER SER B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  GLY 61  61  61  GLY GLY B . n 
B 1 62  PRO 62  62  62  PRO PRO B . n 
B 1 63  HIS 63  63  63  HIS HIS B . n 
B 1 64  PHE 64  64  64  PHE PHE B . n 
B 1 65  ASN 65  65  65  ASN ASN B . n 
B 1 66  PRO 66  66  66  PRO PRO B . n 
B 1 67  LEU 67  67  67  LEU LEU B . n 
B 1 68  SER 68  68  68  SER SER B . n 
B 1 69  ARG 69  69  69  ARG ARG B . n 
B 1 70  LYS 70  70  70  LYS LYS B . n 
B 1 71  HIS 71  71  71  HIS HIS B . n 
B 1 72  GLY 72  72  72  GLY GLY B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LYS 75  75  75  LYS LYS B . n 
B 1 76  ASP 76  76  76  ASP ASP B . n 
B 1 77  GLU 77  77  77  GLU GLU B . n 
B 1 78  GLU 78  78  78  GLU GLU B . n 
B 1 79  ARG 79  79  79  ARG ARG B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  VAL 81  81  81  VAL VAL B . n 
B 1 82  GLY 82  82  82  GLY GLY B . n 
B 1 83  ASP 83  83  83  ASP ASP B . n 
B 1 84  LEU 84  84  84  LEU LEU B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  ASN 86  86  86  ASN ASN B . n 
B 1 87  VAL 87  87  87  VAL VAL B . n 
B 1 88  THR 88  88  88  THR THR B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  ASP 90  90  90  ASP ASP B . n 
B 1 91  LYS 91  91  91  LYS LYS B . n 
B 1 92  ASP 92  92  92  ASP ASP B . n 
B 1 93  GLY 93  93  93  GLY GLY B . n 
B 1 94  VAL 94  94  94  VAL VAL B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  ASP 96  96  96  ASP ASP B . n 
B 1 97  VAL 97  97  97  VAL VAL B . n 
B 1 98  SER 98  98  98  SER SER B . n 
B 1 99  ILE 99  99  99  ILE ILE B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 SER 102 102 102 SER SER B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 ILE 104 104 104 ILE ILE B . n 
B 1 105 SER 105 105 105 SER SER B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 SER 107 107 107 SER SER B . n 
B 1 108 GLY 108 108 108 GLY GLY B . n 
B 1 109 ASP 109 109 109 ASP ASP B . n 
B 1 110 HIS 110 110 110 HIS HIS B . n 
B 1 111 CME 111 111 111 CME CME B . n 
B 1 112 ILE 112 112 112 ILE ILE B . n 
B 1 113 ILE 113 113 113 ILE ILE B . n 
B 1 114 GLY 114 114 114 GLY GLY B . n 
B 1 115 ARG 115 115 115 ARG ARG B . n 
B 1 116 THR 116 116 116 THR THR B . n 
B 1 117 LEU 117 117 117 LEU LEU B . n 
B 1 118 VAL 118 118 118 VAL VAL B . n 
B 1 119 VAL 119 119 119 VAL VAL B . n 
B 1 120 HIS 120 120 120 HIS HIS B . n 
B 1 121 GLU 121 121 121 GLU GLU B . n 
B 1 122 LYS 122 122 122 LYS LYS B . n 
B 1 123 ALA 123 123 123 ALA ALA B . n 
B 1 124 ASP 124 124 124 ASP ASP B . n 
B 1 125 ASP 125 125 125 ASP ASP B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 GLY 127 127 127 GLY GLY B . n 
B 1 128 LYS 128 128 128 LYS LYS B . n 
B 1 129 GLY 129 129 129 GLY GLY B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ASN 131 131 131 ASN ASN B . n 
B 1 132 GLU 132 132 132 GLU GLU B . n 
B 1 133 GLU 133 133 133 GLU GLU B . n 
B 1 134 SER 134 134 134 SER SER B . n 
B 1 135 THR 135 135 135 THR THR B . n 
B 1 136 LYS 136 136 136 LYS LYS B . n 
B 1 137 THR 137 137 137 THR THR B . n 
B 1 138 GLY 138 138 138 GLY GLY B . n 
B 1 139 ASN 139 139 139 ASN ASN B . n 
B 1 140 ALA 140 140 140 ALA ALA B . n 
B 1 141 GLY 141 141 141 GLY GLY B . n 
B 1 142 SER 142 142 142 SER SER B . n 
B 1 143 ARG 143 143 143 ARG ARG B . n 
B 1 144 LEU 144 144 144 LEU LEU B . n 
B 1 145 ALA 145 145 145 ALA ALA B . n 
B 1 146 CYS 146 146 146 CYS CYS B . n 
B 1 147 GLY 147 147 147 GLY GLY B . n 
B 1 148 VAL 148 148 148 VAL VAL B . n 
B 1 149 ILE 149 149 149 ILE ILE B . n 
B 1 150 GLY 150 150 150 GLY GLY B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 ALA 152 152 152 ALA ALA B . n 
B 1 153 GLN 153 153 153 GLN GLN B . n 
C 1 1   ALA 1   1   1   ALA ALA D . n 
C 1 2   THR 2   2   2   THR THR D . n 
C 1 3   LYS 3   3   3   LYS LYS D . n 
C 1 4   ALA 4   4   4   ALA ALA D . n 
C 1 5   VAL 5   5   5   VAL VAL D . n 
C 1 6   CYS 6   6   6   CYS CYS D . n 
C 1 7   VAL 7   7   7   VAL VAL D . n 
C 1 8   LEU 8   8   8   LEU LEU D . n 
C 1 9   LYS 9   9   9   LYS LYS D . n 
C 1 10  GLY 10  10  10  GLY GLY D . n 
C 1 11  ASP 11  11  11  ASP ASP D . n 
C 1 12  GLY 12  12  12  GLY GLY D . n 
C 1 13  PRO 13  13  13  PRO PRO D . n 
C 1 14  VAL 14  14  14  VAL VAL D . n 
C 1 15  GLN 15  15  15  GLN GLN D . n 
C 1 16  GLY 16  16  16  GLY GLY D . n 
C 1 17  ILE 17  17  17  ILE ILE D . n 
C 1 18  ILE 18  18  18  ILE ILE D . n 
C 1 19  ASN 19  19  19  ASN ASN D . n 
C 1 20  PHE 20  20  20  PHE PHE D . n 
C 1 21  GLU 21  21  21  GLU GLU D . n 
C 1 22  GLN 22  22  22  GLN GLN D . n 
C 1 23  LYS 23  23  23  LYS LYS D . n 
C 1 24  GLU 24  24  24  GLU GLU D . n 
C 1 25  SER 25  25  25  SER SER D . n 
C 1 26  ASN 26  26  26  ASN ASN D . n 
C 1 27  GLY 27  27  27  GLY GLY D . n 
C 1 28  PRO 28  28  28  PRO PRO D . n 
C 1 29  VAL 29  29  29  VAL VAL D . n 
C 1 30  LYS 30  30  30  LYS LYS D . n 
C 1 31  VAL 31  31  31  VAL VAL D . n 
C 1 32  TRP 32  32  32  TRP TRP D . n 
C 1 33  GLY 33  33  33  GLY GLY D . n 
C 1 34  SER 34  34  34  SER SER D . n 
C 1 35  ILE 35  35  35  ILE ILE D . n 
C 1 36  LYS 36  36  36  LYS LYS D . n 
C 1 37  GLY 37  37  37  GLY GLY D . n 
C 1 38  LEU 38  38  38  LEU LEU D . n 
C 1 39  THR 39  39  39  THR THR D . n 
C 1 40  GLU 40  40  40  GLU GLU D . n 
C 1 41  GLY 41  41  41  GLY GLY D . n 
C 1 42  LEU 42  42  42  LEU LEU D . n 
C 1 43  HIS 43  43  43  HIS HIS D . n 
C 1 44  GLY 44  44  44  GLY GLY D . n 
C 1 45  PHE 45  45  45  PHE PHE D . n 
C 1 46  HIS 46  46  46  HIS HIS D . n 
C 1 47  VAL 47  47  47  VAL VAL D . n 
C 1 48  HIS 48  48  48  HIS HIS D . n 
C 1 49  GLU 49  49  49  GLU GLU D . n 
C 1 50  PHE 50  50  50  PHE PHE D . n 
C 1 51  GLY 51  51  51  GLY GLY D . n 
C 1 52  ASP 52  52  52  ASP ASP D . n 
C 1 53  ASN 53  53  53  ASN ASN D . n 
C 1 54  THR 54  54  54  THR THR D . n 
C 1 55  ALA 55  55  55  ALA ALA D . n 
C 1 56  GLY 56  56  56  GLY GLY D . n 
C 1 57  CYS 57  57  57  CYS CYS D . n 
C 1 58  THR 58  58  58  THR THR D . n 
C 1 59  SER 59  59  59  SER SER D . n 
C 1 60  ALA 60  60  60  ALA ALA D . n 
C 1 61  GLY 61  61  61  GLY GLY D . n 
C 1 62  PRO 62  62  62  PRO PRO D . n 
C 1 63  HIS 63  63  63  HIS HIS D . n 
C 1 64  PHE 64  64  64  PHE PHE D . n 
C 1 65  ASN 65  65  65  ASN ASN D . n 
C 1 66  PRO 66  66  66  PRO PRO D . n 
C 1 67  LEU 67  67  67  LEU LEU D . n 
C 1 68  SER 68  68  68  SER SER D . n 
C 1 69  ARG 69  69  69  ARG ARG D . n 
C 1 70  LYS 70  70  70  LYS LYS D . n 
C 1 71  HIS 71  71  71  HIS HIS D . n 
C 1 72  GLY 72  72  72  GLY GLY D . n 
C 1 73  GLY 73  73  73  GLY GLY D . n 
C 1 74  PRO 74  74  74  PRO PRO D . n 
C 1 75  LYS 75  75  75  LYS LYS D . n 
C 1 76  ASP 76  76  76  ASP ASP D . n 
C 1 77  GLU 77  77  77  GLU GLU D . n 
C 1 78  GLU 78  78  78  GLU GLU D . n 
C 1 79  ARG 79  79  79  ARG ARG D . n 
C 1 80  HIS 80  80  80  HIS HIS D . n 
C 1 81  VAL 81  81  81  VAL VAL D . n 
C 1 82  GLY 82  82  82  GLY GLY D . n 
C 1 83  ASP 83  83  83  ASP ASP D . n 
C 1 84  LEU 84  84  84  LEU LEU D . n 
C 1 85  GLY 85  85  85  GLY GLY D . n 
C 1 86  ASN 86  86  86  ASN ASN D . n 
C 1 87  VAL 87  87  87  VAL VAL D . n 
C 1 88  THR 88  88  88  THR THR D . n 
C 1 89  ALA 89  89  89  ALA ALA D . n 
C 1 90  ASP 90  90  90  ASP ASP D . n 
C 1 91  LYS 91  91  91  LYS LYS D . n 
C 1 92  ASP 92  92  92  ASP ASP D . n 
C 1 93  GLY 93  93  93  GLY GLY D . n 
C 1 94  VAL 94  94  94  VAL VAL D . n 
C 1 95  ALA 95  95  95  ALA ALA D . n 
C 1 96  ASP 96  96  96  ASP ASP D . n 
C 1 97  VAL 97  97  97  VAL VAL D . n 
C 1 98  SER 98  98  98  SER SER D . n 
C 1 99  ILE 99  99  99  ILE ILE D . n 
C 1 100 GLU 100 100 100 GLU GLU D . n 
C 1 101 ASP 101 101 101 ASP ASP D . n 
C 1 102 SER 102 102 102 SER SER D . n 
C 1 103 VAL 103 103 103 VAL VAL D . n 
C 1 104 ILE 104 104 104 ILE ILE D . n 
C 1 105 SER 105 105 105 SER SER D . n 
C 1 106 LEU 106 106 106 LEU LEU D . n 
C 1 107 SER 107 107 107 SER SER D . n 
C 1 108 GLY 108 108 108 GLY GLY D . n 
C 1 109 ASP 109 109 109 ASP ASP D . n 
C 1 110 HIS 110 110 110 HIS HIS D . n 
C 1 111 CME 111 111 111 CME CME D . n 
C 1 112 ILE 112 112 112 ILE ILE D . n 
C 1 113 ILE 113 113 113 ILE ILE D . n 
C 1 114 GLY 114 114 114 GLY GLY D . n 
C 1 115 ARG 115 115 115 ARG ARG D . n 
C 1 116 THR 116 116 116 THR THR D . n 
C 1 117 LEU 117 117 117 LEU LEU D . n 
C 1 118 VAL 118 118 118 VAL VAL D . n 
C 1 119 VAL 119 119 119 VAL VAL D . n 
C 1 120 HIS 120 120 120 HIS HIS D . n 
C 1 121 GLU 121 121 121 GLU GLU D . n 
C 1 122 LYS 122 122 122 LYS LYS D . n 
C 1 123 ALA 123 123 123 ALA ALA D . n 
C 1 124 ASP 124 124 124 ASP ASP D . n 
C 1 125 ASP 125 125 125 ASP ASP D . n 
C 1 126 LEU 126 126 126 LEU LEU D . n 
C 1 127 GLY 127 127 127 GLY GLY D . n 
C 1 128 LYS 128 128 128 LYS LYS D . n 
C 1 129 GLY 129 129 129 GLY GLY D . n 
C 1 130 GLY 130 130 130 GLY GLY D . n 
C 1 131 ASN 131 131 131 ASN ASN D . n 
C 1 132 GLU 132 132 132 GLU GLU D . n 
C 1 133 GLU 133 133 133 GLU GLU D . n 
C 1 134 SER 134 134 134 SER SER D . n 
C 1 135 THR 135 135 135 THR THR D . n 
C 1 136 LYS 136 136 136 LYS LYS D . n 
C 1 137 THR 137 137 137 THR THR D . n 
C 1 138 GLY 138 138 138 GLY GLY D . n 
C 1 139 ASN 139 139 139 ASN ASN D . n 
C 1 140 ALA 140 140 140 ALA ALA D . n 
C 1 141 GLY 141 141 141 GLY GLY D . n 
C 1 142 SER 142 142 142 SER SER D . n 
C 1 143 ARG 143 143 143 ARG ARG D . n 
C 1 144 LEU 144 144 144 LEU LEU D . n 
C 1 145 ALA 145 145 145 ALA ALA D . n 
C 1 146 CYS 146 146 146 CYS CYS D . n 
C 1 147 GLY 147 147 147 GLY GLY D . n 
C 1 148 VAL 148 148 148 VAL VAL D . n 
C 1 149 ILE 149 149 149 ILE ILE D . n 
C 1 150 GLY 150 150 150 GLY GLY D . n 
C 1 151 ILE 151 151 151 ILE ILE D . n 
C 1 152 ALA 152 152 152 ALA ALA D . n 
C 1 153 GLN 153 153 153 GLN GLN D . n 
D 1 1   ALA 1   1   1   ALA ALA E . n 
D 1 2   THR 2   2   2   THR THR E . n 
D 1 3   LYS 3   3   3   LYS LYS E . n 
D 1 4   ALA 4   4   4   ALA ALA E . n 
D 1 5   VAL 5   5   5   VAL VAL E . n 
D 1 6   CYS 6   6   6   CYS CYS E . n 
D 1 7   VAL 7   7   7   VAL VAL E . n 
D 1 8   LEU 8   8   8   LEU LEU E . n 
D 1 9   LYS 9   9   9   LYS LYS E . n 
D 1 10  GLY 10  10  10  GLY GLY E . n 
D 1 11  ASP 11  11  11  ASP ASP E . n 
D 1 12  GLY 12  12  12  GLY GLY E . n 
D 1 13  PRO 13  13  13  PRO PRO E . n 
D 1 14  VAL 14  14  14  VAL VAL E . n 
D 1 15  GLN 15  15  15  GLN GLN E . n 
D 1 16  GLY 16  16  16  GLY GLY E . n 
D 1 17  ILE 17  17  17  ILE ILE E . n 
D 1 18  ILE 18  18  18  ILE ILE E . n 
D 1 19  ASN 19  19  19  ASN ASN E . n 
D 1 20  PHE 20  20  20  PHE PHE E . n 
D 1 21  GLU 21  21  21  GLU GLU E . n 
D 1 22  GLN 22  22  22  GLN GLN E . n 
D 1 23  LYS 23  23  23  LYS LYS E . n 
D 1 24  GLU 24  24  24  GLU GLU E . n 
D 1 25  SER 25  25  25  SER SER E . n 
D 1 26  ASN 26  26  26  ASN ASN E . n 
D 1 27  GLY 27  27  27  GLY GLY E . n 
D 1 28  PRO 28  28  28  PRO PRO E . n 
D 1 29  VAL 29  29  29  VAL VAL E . n 
D 1 30  LYS 30  30  30  LYS LYS E . n 
D 1 31  VAL 31  31  31  VAL VAL E . n 
D 1 32  TRP 32  32  32  TRP TRP E . n 
D 1 33  GLY 33  33  33  GLY GLY E . n 
D 1 34  SER 34  34  34  SER SER E . n 
D 1 35  ILE 35  35  35  ILE ILE E . n 
D 1 36  LYS 36  36  36  LYS LYS E . n 
D 1 37  GLY 37  37  37  GLY GLY E . n 
D 1 38  LEU 38  38  38  LEU LEU E . n 
D 1 39  THR 39  39  39  THR THR E . n 
D 1 40  GLU 40  40  40  GLU GLU E . n 
D 1 41  GLY 41  41  41  GLY GLY E . n 
D 1 42  LEU 42  42  42  LEU LEU E . n 
D 1 43  HIS 43  43  43  HIS HIS E . n 
D 1 44  GLY 44  44  44  GLY GLY E . n 
D 1 45  PHE 45  45  45  PHE PHE E . n 
D 1 46  HIS 46  46  46  HIS HIS E . n 
D 1 47  VAL 47  47  47  VAL VAL E . n 
D 1 48  HIS 48  48  48  HIS HIS E . n 
D 1 49  GLU 49  49  49  GLU GLU E . n 
D 1 50  PHE 50  50  50  PHE PHE E . n 
D 1 51  GLY 51  51  51  GLY GLY E . n 
D 1 52  ASP 52  52  52  ASP ASP E . n 
D 1 53  ASN 53  53  53  ASN ASN E . n 
D 1 54  THR 54  54  54  THR THR E . n 
D 1 55  ALA 55  55  55  ALA ALA E . n 
D 1 56  GLY 56  56  56  GLY GLY E . n 
D 1 57  CYS 57  57  57  CYS CYS E . n 
D 1 58  THR 58  58  58  THR THR E . n 
D 1 59  SER 59  59  59  SER SER E . n 
D 1 60  ALA 60  60  60  ALA ALA E . n 
D 1 61  GLY 61  61  61  GLY GLY E . n 
D 1 62  PRO 62  62  62  PRO PRO E . n 
D 1 63  HIS 63  63  63  HIS HIS E . n 
D 1 64  PHE 64  64  64  PHE PHE E . n 
D 1 65  ASN 65  65  65  ASN ASN E . n 
D 1 66  PRO 66  66  66  PRO PRO E . n 
D 1 67  LEU 67  67  67  LEU LEU E . n 
D 1 68  SER 68  68  68  SER SER E . n 
D 1 69  ARG 69  69  69  ARG ARG E . n 
D 1 70  LYS 70  70  70  LYS LYS E . n 
D 1 71  HIS 71  71  71  HIS HIS E . n 
D 1 72  GLY 72  72  72  GLY GLY E . n 
D 1 73  GLY 73  73  73  GLY GLY E . n 
D 1 74  PRO 74  74  74  PRO PRO E . n 
D 1 75  LYS 75  75  75  LYS LYS E . n 
D 1 76  ASP 76  76  76  ASP ASP E . n 
D 1 77  GLU 77  77  77  GLU GLU E . n 
D 1 78  GLU 78  78  78  GLU GLU E . n 
D 1 79  ARG 79  79  79  ARG ARG E . n 
D 1 80  HIS 80  80  80  HIS HIS E . n 
D 1 81  VAL 81  81  81  VAL VAL E . n 
D 1 82  GLY 82  82  82  GLY GLY E . n 
D 1 83  ASP 83  83  83  ASP ASP E . n 
D 1 84  LEU 84  84  84  LEU LEU E . n 
D 1 85  GLY 85  85  85  GLY GLY E . n 
D 1 86  ASN 86  86  86  ASN ASN E . n 
D 1 87  VAL 87  87  87  VAL VAL E . n 
D 1 88  THR 88  88  88  THR THR E . n 
D 1 89  ALA 89  89  89  ALA ALA E . n 
D 1 90  ASP 90  90  90  ASP ASP E . n 
D 1 91  LYS 91  91  91  LYS LYS E . n 
D 1 92  ASP 92  92  92  ASP ASP E . n 
D 1 93  GLY 93  93  93  GLY GLY E . n 
D 1 94  VAL 94  94  94  VAL VAL E . n 
D 1 95  ALA 95  95  95  ALA ALA E . n 
D 1 96  ASP 96  96  96  ASP ASP E . n 
D 1 97  VAL 97  97  97  VAL VAL E . n 
D 1 98  SER 98  98  98  SER SER E . n 
D 1 99  ILE 99  99  99  ILE ILE E . n 
D 1 100 GLU 100 100 100 GLU GLU E . n 
D 1 101 ASP 101 101 101 ASP ASP E . n 
D 1 102 SER 102 102 102 SER SER E . n 
D 1 103 VAL 103 103 103 VAL VAL E . n 
D 1 104 ILE 104 104 104 ILE ILE E . n 
D 1 105 SER 105 105 105 SER SER E . n 
D 1 106 LEU 106 106 106 LEU LEU E . n 
D 1 107 SER 107 107 107 SER SER E . n 
D 1 108 GLY 108 108 108 GLY GLY E . n 
D 1 109 ASP 109 109 109 ASP ASP E . n 
D 1 110 HIS 110 110 110 HIS HIS E . n 
D 1 111 CME 111 111 111 CME CME E . n 
D 1 112 ILE 112 112 112 ILE ILE E . n 
D 1 113 ILE 113 113 113 ILE ILE E . n 
D 1 114 GLY 114 114 114 GLY GLY E . n 
D 1 115 ARG 115 115 115 ARG ARG E . n 
D 1 116 THR 116 116 116 THR THR E . n 
D 1 117 LEU 117 117 117 LEU LEU E . n 
D 1 118 VAL 118 118 118 VAL VAL E . n 
D 1 119 VAL 119 119 119 VAL VAL E . n 
D 1 120 HIS 120 120 120 HIS HIS E . n 
D 1 121 GLU 121 121 121 GLU GLU E . n 
D 1 122 LYS 122 122 122 LYS LYS E . n 
D 1 123 ALA 123 123 123 ALA ALA E . n 
D 1 124 ASP 124 124 124 ASP ASP E . n 
D 1 125 ASP 125 125 125 ASP ASP E . n 
D 1 126 LEU 126 126 126 LEU LEU E . n 
D 1 127 GLY 127 127 127 GLY GLY E . n 
D 1 128 LYS 128 128 128 LYS LYS E . n 
D 1 129 GLY 129 129 129 GLY GLY E . n 
D 1 130 GLY 130 130 130 GLY GLY E . n 
D 1 131 ASN 131 131 131 ASN ASN E . n 
D 1 132 GLU 132 132 132 GLU GLU E . n 
D 1 133 GLU 133 133 133 GLU GLU E . n 
D 1 134 SER 134 134 134 SER SER E . n 
D 1 135 THR 135 135 135 THR THR E . n 
D 1 136 LYS 136 136 136 LYS LYS E . n 
D 1 137 THR 137 137 137 THR THR E . n 
D 1 138 GLY 138 138 138 GLY GLY E . n 
D 1 139 ASN 139 139 139 ASN ASN E . n 
D 1 140 ALA 140 140 140 ALA ALA E . n 
D 1 141 GLY 141 141 141 GLY GLY E . n 
D 1 142 SER 142 142 142 SER SER E . n 
D 1 143 ARG 143 143 143 ARG ARG E . n 
D 1 144 LEU 144 144 144 LEU LEU E . n 
D 1 145 ALA 145 145 145 ALA ALA E . n 
D 1 146 CYS 146 146 146 CYS CYS E . n 
D 1 147 GLY 147 147 147 GLY GLY E . n 
D 1 148 VAL 148 148 148 VAL VAL E . n 
D 1 149 ILE 149 149 149 ILE ILE E . n 
D 1 150 GLY 150 150 150 GLY GLY E . n 
D 1 151 ILE 151 151 151 ILE ILE E . n 
D 1 152 ALA 152 152 152 ALA ALA E . n 
D 1 153 GLN 153 153 153 GLN GLN E . n 
E 1 1   ALA 1   1   1   ALA ALA F . n 
E 1 2   THR 2   2   2   THR THR F . n 
E 1 3   LYS 3   3   3   LYS LYS F . n 
E 1 4   ALA 4   4   4   ALA ALA F . n 
E 1 5   VAL 5   5   5   VAL VAL F . n 
E 1 6   CYS 6   6   6   CYS CYS F . n 
E 1 7   VAL 7   7   7   VAL VAL F . n 
E 1 8   LEU 8   8   8   LEU LEU F . n 
E 1 9   LYS 9   9   9   LYS LYS F . n 
E 1 10  GLY 10  10  10  GLY GLY F . n 
E 1 11  ASP 11  11  11  ASP ASP F . n 
E 1 12  GLY 12  12  12  GLY GLY F . n 
E 1 13  PRO 13  13  13  PRO PRO F . n 
E 1 14  VAL 14  14  14  VAL VAL F . n 
E 1 15  GLN 15  15  15  GLN GLN F . n 
E 1 16  GLY 16  16  16  GLY GLY F . n 
E 1 17  ILE 17  17  17  ILE ILE F . n 
E 1 18  ILE 18  18  18  ILE ILE F . n 
E 1 19  ASN 19  19  19  ASN ASN F . n 
E 1 20  PHE 20  20  20  PHE PHE F . n 
E 1 21  GLU 21  21  21  GLU GLU F . n 
E 1 22  GLN 22  22  22  GLN GLN F . n 
E 1 23  LYS 23  23  23  LYS LYS F . n 
E 1 24  GLU 24  24  24  GLU GLU F . n 
E 1 25  SER 25  25  25  SER SER F . n 
E 1 26  ASN 26  26  26  ASN ASN F . n 
E 1 27  GLY 27  27  27  GLY GLY F . n 
E 1 28  PRO 28  28  28  PRO PRO F . n 
E 1 29  VAL 29  29  29  VAL VAL F . n 
E 1 30  LYS 30  30  30  LYS LYS F . n 
E 1 31  VAL 31  31  31  VAL VAL F . n 
E 1 32  TRP 32  32  32  TRP TRP F . n 
E 1 33  GLY 33  33  33  GLY GLY F . n 
E 1 34  SER 34  34  34  SER SER F . n 
E 1 35  ILE 35  35  35  ILE ILE F . n 
E 1 36  LYS 36  36  36  LYS LYS F . n 
E 1 37  GLY 37  37  37  GLY GLY F . n 
E 1 38  LEU 38  38  38  LEU LEU F . n 
E 1 39  THR 39  39  39  THR THR F . n 
E 1 40  GLU 40  40  40  GLU GLU F . n 
E 1 41  GLY 41  41  41  GLY GLY F . n 
E 1 42  LEU 42  42  42  LEU LEU F . n 
E 1 43  HIS 43  43  43  HIS HIS F . n 
E 1 44  GLY 44  44  44  GLY GLY F . n 
E 1 45  PHE 45  45  45  PHE PHE F . n 
E 1 46  HIS 46  46  46  HIS HIS F . n 
E 1 47  VAL 47  47  47  VAL VAL F . n 
E 1 48  HIS 48  48  48  HIS HIS F . n 
E 1 49  GLU 49  49  49  GLU GLU F . n 
E 1 50  PHE 50  50  50  PHE PHE F . n 
E 1 51  GLY 51  51  51  GLY GLY F . n 
E 1 52  ASP 52  52  52  ASP ASP F . n 
E 1 53  ASN 53  53  53  ASN ASN F . n 
E 1 54  THR 54  54  54  THR THR F . n 
E 1 55  ALA 55  55  55  ALA ALA F . n 
E 1 56  GLY 56  56  56  GLY GLY F . n 
E 1 57  CYS 57  57  57  CYS CYS F . n 
E 1 58  THR 58  58  58  THR THR F . n 
E 1 59  SER 59  59  59  SER SER F . n 
E 1 60  ALA 60  60  60  ALA ALA F . n 
E 1 61  GLY 61  61  61  GLY GLY F . n 
E 1 62  PRO 62  62  62  PRO PRO F . n 
E 1 63  HIS 63  63  63  HIS HIS F . n 
E 1 64  PHE 64  64  64  PHE PHE F . n 
E 1 65  ASN 65  65  65  ASN ASN F . n 
E 1 66  PRO 66  66  66  PRO PRO F . n 
E 1 67  LEU 67  67  67  LEU LEU F . n 
E 1 68  SER 68  68  68  SER SER F . n 
E 1 69  ARG 69  69  69  ARG ARG F . n 
E 1 70  LYS 70  70  70  LYS LYS F . n 
E 1 71  HIS 71  71  71  HIS HIS F . n 
E 1 72  GLY 72  72  72  GLY GLY F . n 
E 1 73  GLY 73  73  73  GLY GLY F . n 
E 1 74  PRO 74  74  74  PRO PRO F . n 
E 1 75  LYS 75  75  75  LYS LYS F . n 
E 1 76  ASP 76  76  76  ASP ASP F . n 
E 1 77  GLU 77  77  77  GLU GLU F . n 
E 1 78  GLU 78  78  78  GLU GLU F . n 
E 1 79  ARG 79  79  79  ARG ARG F . n 
E 1 80  HIS 80  80  80  HIS HIS F . n 
E 1 81  VAL 81  81  81  VAL VAL F . n 
E 1 82  GLY 82  82  82  GLY GLY F . n 
E 1 83  ASP 83  83  83  ASP ASP F . n 
E 1 84  LEU 84  84  84  LEU LEU F . n 
E 1 85  GLY 85  85  85  GLY GLY F . n 
E 1 86  ASN 86  86  86  ASN ASN F . n 
E 1 87  VAL 87  87  87  VAL VAL F . n 
E 1 88  THR 88  88  88  THR THR F . n 
E 1 89  ALA 89  89  89  ALA ALA F . n 
E 1 90  ASP 90  90  90  ASP ASP F . n 
E 1 91  LYS 91  91  91  LYS LYS F . n 
E 1 92  ASP 92  92  92  ASP ASP F . n 
E 1 93  GLY 93  93  93  GLY GLY F . n 
E 1 94  VAL 94  94  94  VAL VAL F . n 
E 1 95  ALA 95  95  95  ALA ALA F . n 
E 1 96  ASP 96  96  96  ASP ASP F . n 
E 1 97  VAL 97  97  97  VAL VAL F . n 
E 1 98  SER 98  98  98  SER SER F . n 
E 1 99  ILE 99  99  99  ILE ILE F . n 
E 1 100 GLU 100 100 100 GLU GLU F . n 
E 1 101 ASP 101 101 101 ASP ASP F . n 
E 1 102 SER 102 102 102 SER SER F . n 
E 1 103 VAL 103 103 103 VAL VAL F . n 
E 1 104 ILE 104 104 104 ILE ILE F . n 
E 1 105 SER 105 105 105 SER SER F . n 
E 1 106 LEU 106 106 106 LEU LEU F . n 
E 1 107 SER 107 107 107 SER SER F . n 
E 1 108 GLY 108 108 108 GLY GLY F . n 
E 1 109 ASP 109 109 109 ASP ASP F . n 
E 1 110 HIS 110 110 110 HIS HIS F . n 
E 1 111 CME 111 111 111 CME CME F . n 
E 1 112 ILE 112 112 112 ILE ILE F . n 
E 1 113 ILE 113 113 113 ILE ILE F . n 
E 1 114 GLY 114 114 114 GLY GLY F . n 
E 1 115 ARG 115 115 115 ARG ARG F . n 
E 1 116 THR 116 116 116 THR THR F . n 
E 1 117 LEU 117 117 117 LEU LEU F . n 
E 1 118 VAL 118 118 118 VAL VAL F . n 
E 1 119 VAL 119 119 119 VAL VAL F . n 
E 1 120 HIS 120 120 120 HIS HIS F . n 
E 1 121 GLU 121 121 121 GLU GLU F . n 
E 1 122 LYS 122 122 122 LYS LYS F . n 
E 1 123 ALA 123 123 123 ALA ALA F . n 
E 1 124 ASP 124 124 124 ASP ASP F . n 
E 1 125 ASP 125 125 125 ASP ASP F . n 
E 1 126 LEU 126 126 126 LEU LEU F . n 
E 1 127 GLY 127 127 127 GLY GLY F . n 
E 1 128 LYS 128 128 128 LYS LYS F . n 
E 1 129 GLY 129 129 129 GLY GLY F . n 
E 1 130 GLY 130 130 130 GLY GLY F . n 
E 1 131 ASN 131 131 131 ASN ASN F . n 
E 1 132 GLU 132 132 132 GLU GLU F . n 
E 1 133 GLU 133 133 133 GLU GLU F . n 
E 1 134 SER 134 134 134 SER SER F . n 
E 1 135 THR 135 135 135 THR THR F . n 
E 1 136 LYS 136 136 136 LYS LYS F . n 
E 1 137 THR 137 137 137 THR THR F . n 
E 1 138 GLY 138 138 138 GLY GLY F . n 
E 1 139 ASN 139 139 139 ASN ASN F . n 
E 1 140 ALA 140 140 140 ALA ALA F . n 
E 1 141 GLY 141 141 141 GLY GLY F . n 
E 1 142 SER 142 142 142 SER SER F . n 
E 1 143 ARG 143 143 143 ARG ARG F . n 
E 1 144 LEU 144 144 144 LEU LEU F . n 
E 1 145 ALA 145 145 145 ALA ALA F . n 
E 1 146 CYS 146 146 146 CYS CYS F . n 
E 1 147 GLY 147 147 147 GLY GLY F . n 
E 1 148 VAL 148 148 148 VAL VAL F . n 
E 1 149 ILE 149 149 149 ILE ILE F . n 
E 1 150 GLY 150 150 150 GLY GLY F . n 
E 1 151 ILE 151 151 151 ILE ILE F . n 
E 1 152 ALA 152 152 152 ALA ALA F . n 
E 1 153 GLN 153 153 153 GLN GLN F . n 
F 1 1   ALA 1   1   1   ALA ALA G . n 
F 1 2   THR 2   2   2   THR THR G . n 
F 1 3   LYS 3   3   3   LYS LYS G . n 
F 1 4   ALA 4   4   4   ALA ALA G . n 
F 1 5   VAL 5   5   5   VAL VAL G . n 
F 1 6   CYS 6   6   6   CYS CYS G . n 
F 1 7   VAL 7   7   7   VAL VAL G . n 
F 1 8   LEU 8   8   8   LEU LEU G . n 
F 1 9   LYS 9   9   9   LYS LYS G . n 
F 1 10  GLY 10  10  10  GLY GLY G . n 
F 1 11  ASP 11  11  11  ASP ASP G . n 
F 1 12  GLY 12  12  12  GLY GLY G . n 
F 1 13  PRO 13  13  13  PRO PRO G . n 
F 1 14  VAL 14  14  14  VAL VAL G . n 
F 1 15  GLN 15  15  15  GLN GLN G . n 
F 1 16  GLY 16  16  16  GLY GLY G . n 
F 1 17  ILE 17  17  17  ILE ILE G . n 
F 1 18  ILE 18  18  18  ILE ILE G . n 
F 1 19  ASN 19  19  19  ASN ASN G . n 
F 1 20  PHE 20  20  20  PHE PHE G . n 
F 1 21  GLU 21  21  21  GLU GLU G . n 
F 1 22  GLN 22  22  22  GLN GLN G . n 
F 1 23  LYS 23  23  23  LYS LYS G . n 
F 1 24  GLU 24  24  24  GLU GLU G . n 
F 1 25  SER 25  25  25  SER SER G . n 
F 1 26  ASN 26  26  26  ASN ASN G . n 
F 1 27  GLY 27  27  27  GLY GLY G . n 
F 1 28  PRO 28  28  28  PRO PRO G . n 
F 1 29  VAL 29  29  29  VAL VAL G . n 
F 1 30  LYS 30  30  30  LYS LYS G . n 
F 1 31  VAL 31  31  31  VAL VAL G . n 
F 1 32  TRP 32  32  32  TRP TRP G . n 
F 1 33  GLY 33  33  33  GLY GLY G . n 
F 1 34  SER 34  34  34  SER SER G . n 
F 1 35  ILE 35  35  35  ILE ILE G . n 
F 1 36  LYS 36  36  36  LYS LYS G . n 
F 1 37  GLY 37  37  37  GLY GLY G . n 
F 1 38  LEU 38  38  38  LEU LEU G . n 
F 1 39  THR 39  39  39  THR THR G . n 
F 1 40  GLU 40  40  40  GLU GLU G . n 
F 1 41  GLY 41  41  41  GLY GLY G . n 
F 1 42  LEU 42  42  42  LEU LEU G . n 
F 1 43  HIS 43  43  43  HIS HIS G . n 
F 1 44  GLY 44  44  44  GLY GLY G . n 
F 1 45  PHE 45  45  45  PHE PHE G . n 
F 1 46  HIS 46  46  46  HIS HIS G . n 
F 1 47  VAL 47  47  47  VAL VAL G . n 
F 1 48  HIS 48  48  48  HIS HIS G . n 
F 1 49  GLU 49  49  49  GLU GLU G . n 
F 1 50  PHE 50  50  50  PHE PHE G . n 
F 1 51  GLY 51  51  51  GLY GLY G . n 
F 1 52  ASP 52  52  52  ASP ASP G . n 
F 1 53  ASN 53  53  53  ASN ASN G . n 
F 1 54  THR 54  54  54  THR THR G . n 
F 1 55  ALA 55  55  55  ALA ALA G . n 
F 1 56  GLY 56  56  56  GLY GLY G . n 
F 1 57  CYS 57  57  57  CYS CYS G . n 
F 1 58  THR 58  58  58  THR THR G . n 
F 1 59  SER 59  59  59  SER SER G . n 
F 1 60  ALA 60  60  60  ALA ALA G . n 
F 1 61  GLY 61  61  61  GLY GLY G . n 
F 1 62  PRO 62  62  62  PRO PRO G . n 
F 1 63  HIS 63  63  63  HIS HIS G . n 
F 1 64  PHE 64  64  64  PHE PHE G . n 
F 1 65  ASN 65  65  65  ASN ASN G . n 
F 1 66  PRO 66  66  66  PRO PRO G . n 
F 1 67  LEU 67  67  67  LEU LEU G . n 
F 1 68  SER 68  68  68  SER SER G . n 
F 1 69  ARG 69  69  69  ARG ARG G . n 
F 1 70  LYS 70  70  70  LYS LYS G . n 
F 1 71  HIS 71  71  71  HIS HIS G . n 
F 1 72  GLY 72  72  72  GLY GLY G . n 
F 1 73  GLY 73  73  73  GLY GLY G . n 
F 1 74  PRO 74  74  74  PRO PRO G . n 
F 1 75  LYS 75  75  75  LYS LYS G . n 
F 1 76  ASP 76  76  76  ASP ASP G . n 
F 1 77  GLU 77  77  77  GLU GLU G . n 
F 1 78  GLU 78  78  78  GLU GLU G . n 
F 1 79  ARG 79  79  79  ARG ARG G . n 
F 1 80  HIS 80  80  80  HIS HIS G . n 
F 1 81  VAL 81  81  81  VAL VAL G . n 
F 1 82  GLY 82  82  82  GLY GLY G . n 
F 1 83  ASP 83  83  83  ASP ASP G . n 
F 1 84  LEU 84  84  84  LEU LEU G . n 
F 1 85  GLY 85  85  85  GLY GLY G . n 
F 1 86  ASN 86  86  86  ASN ASN G . n 
F 1 87  VAL 87  87  87  VAL VAL G . n 
F 1 88  THR 88  88  88  THR THR G . n 
F 1 89  ALA 89  89  89  ALA ALA G . n 
F 1 90  ASP 90  90  90  ASP ASP G . n 
F 1 91  LYS 91  91  91  LYS LYS G . n 
F 1 92  ASP 92  92  92  ASP ASP G . n 
F 1 93  GLY 93  93  93  GLY GLY G . n 
F 1 94  VAL 94  94  94  VAL VAL G . n 
F 1 95  ALA 95  95  95  ALA ALA G . n 
F 1 96  ASP 96  96  96  ASP ASP G . n 
F 1 97  VAL 97  97  97  VAL VAL G . n 
F 1 98  SER 98  98  98  SER SER G . n 
F 1 99  ILE 99  99  99  ILE ILE G . n 
F 1 100 GLU 100 100 100 GLU GLU G . n 
F 1 101 ASP 101 101 101 ASP ASP G . n 
F 1 102 SER 102 102 102 SER SER G . n 
F 1 103 VAL 103 103 103 VAL VAL G . n 
F 1 104 ILE 104 104 104 ILE ILE G . n 
F 1 105 SER 105 105 105 SER SER G . n 
F 1 106 LEU 106 106 106 LEU LEU G . n 
F 1 107 SER 107 107 107 SER SER G . n 
F 1 108 GLY 108 108 108 GLY GLY G . n 
F 1 109 ASP 109 109 109 ASP ASP G . n 
F 1 110 HIS 110 110 110 HIS HIS G . n 
F 1 111 CME 111 111 111 CME CME G . n 
F 1 112 ILE 112 112 112 ILE ILE G . n 
F 1 113 ILE 113 113 113 ILE ILE G . n 
F 1 114 GLY 114 114 114 GLY GLY G . n 
F 1 115 ARG 115 115 115 ARG ARG G . n 
F 1 116 THR 116 116 116 THR THR G . n 
F 1 117 LEU 117 117 117 LEU LEU G . n 
F 1 118 VAL 118 118 118 VAL VAL G . n 
F 1 119 VAL 119 119 119 VAL VAL G . n 
F 1 120 HIS 120 120 120 HIS HIS G . n 
F 1 121 GLU 121 121 121 GLU GLU G . n 
F 1 122 LYS 122 122 122 LYS LYS G . n 
F 1 123 ALA 123 123 123 ALA ALA G . n 
F 1 124 ASP 124 124 124 ASP ASP G . n 
F 1 125 ASP 125 125 125 ASP ASP G . n 
F 1 126 LEU 126 126 126 LEU LEU G . n 
F 1 127 GLY 127 127 127 GLY GLY G . n 
F 1 128 LYS 128 128 128 LYS LYS G . n 
F 1 129 GLY 129 129 129 GLY GLY G . n 
F 1 130 GLY 130 130 130 GLY GLY G . n 
F 1 131 ASN 131 131 131 ASN ASN G . n 
F 1 132 GLU 132 132 132 GLU GLU G . n 
F 1 133 GLU 133 133 133 GLU GLU G . n 
F 1 134 SER 134 134 134 SER SER G . n 
F 1 135 THR 135 135 135 THR THR G . n 
F 1 136 LYS 136 136 136 LYS LYS G . n 
F 1 137 THR 137 137 137 THR THR G . n 
F 1 138 GLY 138 138 138 GLY GLY G . n 
F 1 139 ASN 139 139 139 ASN ASN G . n 
F 1 140 ALA 140 140 140 ALA ALA G . n 
F 1 141 GLY 141 141 141 GLY GLY G . n 
F 1 142 SER 142 142 142 SER SER G . n 
F 1 143 ARG 143 143 143 ARG ARG G . n 
F 1 144 LEU 144 144 144 LEU LEU G . n 
F 1 145 ALA 145 145 145 ALA ALA G . n 
F 1 146 CYS 146 146 146 CYS CYS G . n 
F 1 147 GLY 147 147 147 GLY GLY G . n 
F 1 148 VAL 148 148 148 VAL VAL G . n 
F 1 149 ILE 149 149 149 ILE ILE G . n 
F 1 150 GLY 150 150 150 GLY GLY G . n 
F 1 151 ILE 151 151 151 ILE ILE G . n 
F 1 152 ALA 152 152 152 ALA ALA G . n 
F 1 153 GLN 153 153 153 GLN GLN G . n 
G 1 1   ALA 1   1   1   ALA ALA H . n 
G 1 2   THR 2   2   2   THR THR H . n 
G 1 3   LYS 3   3   3   LYS LYS H . n 
G 1 4   ALA 4   4   4   ALA ALA H . n 
G 1 5   VAL 5   5   5   VAL VAL H . n 
G 1 6   CYS 6   6   6   CYS CYS H . n 
G 1 7   VAL 7   7   7   VAL VAL H . n 
G 1 8   LEU 8   8   8   LEU LEU H . n 
G 1 9   LYS 9   9   9   LYS LYS H . n 
G 1 10  GLY 10  10  10  GLY GLY H . n 
G 1 11  ASP 11  11  11  ASP ASP H . n 
G 1 12  GLY 12  12  12  GLY GLY H . n 
G 1 13  PRO 13  13  13  PRO PRO H . n 
G 1 14  VAL 14  14  14  VAL VAL H . n 
G 1 15  GLN 15  15  15  GLN GLN H . n 
G 1 16  GLY 16  16  16  GLY GLY H . n 
G 1 17  ILE 17  17  17  ILE ILE H . n 
G 1 18  ILE 18  18  18  ILE ILE H . n 
G 1 19  ASN 19  19  19  ASN ASN H . n 
G 1 20  PHE 20  20  20  PHE PHE H . n 
G 1 21  GLU 21  21  21  GLU GLU H . n 
G 1 22  GLN 22  22  22  GLN GLN H . n 
G 1 23  LYS 23  23  23  LYS LYS H . n 
G 1 24  GLU 24  24  24  GLU GLU H . n 
G 1 25  SER 25  25  25  SER SER H . n 
G 1 26  ASN 26  26  26  ASN ASN H . n 
G 1 27  GLY 27  27  27  GLY GLY H . n 
G 1 28  PRO 28  28  28  PRO PRO H . n 
G 1 29  VAL 29  29  29  VAL VAL H . n 
G 1 30  LYS 30  30  30  LYS LYS H . n 
G 1 31  VAL 31  31  31  VAL VAL H . n 
G 1 32  TRP 32  32  32  TRP TRP H . n 
G 1 33  GLY 33  33  33  GLY GLY H . n 
G 1 34  SER 34  34  34  SER SER H . n 
G 1 35  ILE 35  35  35  ILE ILE H . n 
G 1 36  LYS 36  36  36  LYS LYS H . n 
G 1 37  GLY 37  37  37  GLY GLY H . n 
G 1 38  LEU 38  38  38  LEU LEU H . n 
G 1 39  THR 39  39  39  THR THR H . n 
G 1 40  GLU 40  40  40  GLU GLU H . n 
G 1 41  GLY 41  41  41  GLY GLY H . n 
G 1 42  LEU 42  42  42  LEU LEU H . n 
G 1 43  HIS 43  43  43  HIS HIS H . n 
G 1 44  GLY 44  44  44  GLY GLY H . n 
G 1 45  PHE 45  45  45  PHE PHE H . n 
G 1 46  HIS 46  46  46  HIS HIS H . n 
G 1 47  VAL 47  47  47  VAL VAL H . n 
G 1 48  HIS 48  48  48  HIS HIS H . n 
G 1 49  GLU 49  49  49  GLU GLU H . n 
G 1 50  PHE 50  50  50  PHE PHE H . n 
G 1 51  GLY 51  51  51  GLY GLY H . n 
G 1 52  ASP 52  52  52  ASP ASP H . n 
G 1 53  ASN 53  53  53  ASN ASN H . n 
G 1 54  THR 54  54  54  THR THR H . n 
G 1 55  ALA 55  55  55  ALA ALA H . n 
G 1 56  GLY 56  56  56  GLY GLY H . n 
G 1 57  CYS 57  57  57  CYS CYS H . n 
G 1 58  THR 58  58  58  THR THR H . n 
G 1 59  SER 59  59  59  SER SER H . n 
G 1 60  ALA 60  60  60  ALA ALA H . n 
G 1 61  GLY 61  61  61  GLY GLY H . n 
G 1 62  PRO 62  62  62  PRO PRO H . n 
G 1 63  HIS 63  63  63  HIS HIS H . n 
G 1 64  PHE 64  64  64  PHE PHE H . n 
G 1 65  ASN 65  65  65  ASN ASN H . n 
G 1 66  PRO 66  66  66  PRO PRO H . n 
G 1 67  LEU 67  67  67  LEU LEU H . n 
G 1 68  SER 68  68  68  SER SER H . n 
G 1 69  ARG 69  69  69  ARG ARG H . n 
G 1 70  LYS 70  70  70  LYS LYS H . n 
G 1 71  HIS 71  71  71  HIS HIS H . n 
G 1 72  GLY 72  72  72  GLY GLY H . n 
G 1 73  GLY 73  73  73  GLY GLY H . n 
G 1 74  PRO 74  74  74  PRO PRO H . n 
G 1 75  LYS 75  75  75  LYS LYS H . n 
G 1 76  ASP 76  76  76  ASP ASP H . n 
G 1 77  GLU 77  77  77  GLU GLU H . n 
G 1 78  GLU 78  78  78  GLU GLU H . n 
G 1 79  ARG 79  79  79  ARG ARG H . n 
G 1 80  HIS 80  80  80  HIS HIS H . n 
G 1 81  VAL 81  81  81  VAL VAL H . n 
G 1 82  GLY 82  82  82  GLY GLY H . n 
G 1 83  ASP 83  83  83  ASP ASP H . n 
G 1 84  LEU 84  84  84  LEU LEU H . n 
G 1 85  GLY 85  85  85  GLY GLY H . n 
G 1 86  ASN 86  86  86  ASN ASN H . n 
G 1 87  VAL 87  87  87  VAL VAL H . n 
G 1 88  THR 88  88  88  THR THR H . n 
G 1 89  ALA 89  89  89  ALA ALA H . n 
G 1 90  ASP 90  90  90  ASP ASP H . n 
G 1 91  LYS 91  91  91  LYS LYS H . n 
G 1 92  ASP 92  92  92  ASP ASP H . n 
G 1 93  GLY 93  93  93  GLY GLY H . n 
G 1 94  VAL 94  94  94  VAL VAL H . n 
G 1 95  ALA 95  95  95  ALA ALA H . n 
G 1 96  ASP 96  96  96  ASP ASP H . n 
G 1 97  VAL 97  97  97  VAL VAL H . n 
G 1 98  SER 98  98  98  SER SER H . n 
G 1 99  ILE 99  99  99  ILE ILE H . n 
G 1 100 GLU 100 100 100 GLU GLU H . n 
G 1 101 ASP 101 101 101 ASP ASP H . n 
G 1 102 SER 102 102 102 SER SER H . n 
G 1 103 VAL 103 103 103 VAL VAL H . n 
G 1 104 ILE 104 104 104 ILE ILE H . n 
G 1 105 SER 105 105 105 SER SER H . n 
G 1 106 LEU 106 106 106 LEU LEU H . n 
G 1 107 SER 107 107 107 SER SER H . n 
G 1 108 GLY 108 108 108 GLY GLY H . n 
G 1 109 ASP 109 109 109 ASP ASP H . n 
G 1 110 HIS 110 110 110 HIS HIS H . n 
G 1 111 CME 111 111 111 CME CME H . n 
G 1 112 ILE 112 112 112 ILE ILE H . n 
G 1 113 ILE 113 113 113 ILE ILE H . n 
G 1 114 GLY 114 114 114 GLY GLY H . n 
G 1 115 ARG 115 115 115 ARG ARG H . n 
G 1 116 THR 116 116 116 THR THR H . n 
G 1 117 LEU 117 117 117 LEU LEU H . n 
G 1 118 VAL 118 118 118 VAL VAL H . n 
G 1 119 VAL 119 119 119 VAL VAL H . n 
G 1 120 HIS 120 120 120 HIS HIS H . n 
G 1 121 GLU 121 121 121 GLU GLU H . n 
G 1 122 LYS 122 122 122 LYS LYS H . n 
G 1 123 ALA 123 123 123 ALA ALA H . n 
G 1 124 ASP 124 124 124 ASP ASP H . n 
G 1 125 ASP 125 125 125 ASP ASP H . n 
G 1 126 LEU 126 126 126 LEU LEU H . n 
G 1 127 GLY 127 127 127 GLY GLY H . n 
G 1 128 LYS 128 128 128 LYS LYS H . n 
G 1 129 GLY 129 129 129 GLY GLY H . n 
G 1 130 GLY 130 130 130 GLY GLY H . n 
G 1 131 ASN 131 131 131 ASN ASN H . n 
G 1 132 GLU 132 132 132 GLU GLU H . n 
G 1 133 GLU 133 133 133 GLU GLU H . n 
G 1 134 SER 134 134 134 SER SER H . n 
G 1 135 THR 135 135 135 THR THR H . n 
G 1 136 LYS 136 136 136 LYS LYS H . n 
G 1 137 THR 137 137 137 THR THR H . n 
G 1 138 GLY 138 138 138 GLY GLY H . n 
G 1 139 ASN 139 139 139 ASN ASN H . n 
G 1 140 ALA 140 140 140 ALA ALA H . n 
G 1 141 GLY 141 141 141 GLY GLY H . n 
G 1 142 SER 142 142 142 SER SER H . n 
G 1 143 ARG 143 143 143 ARG ARG H . n 
G 1 144 LEU 144 144 144 LEU LEU H . n 
G 1 145 ALA 145 145 145 ALA ALA H . n 
G 1 146 CYS 146 146 146 CYS CYS H . n 
G 1 147 GLY 147 147 147 GLY GLY H . n 
G 1 148 VAL 148 148 148 VAL VAL H . n 
G 1 149 ILE 149 149 149 ILE ILE H . n 
G 1 150 GLY 150 150 150 GLY GLY H . n 
G 1 151 ILE 151 151 151 ILE ILE H . n 
G 1 152 ALA 152 152 152 ALA ALA H . n 
G 1 153 GLN 153 153 153 GLN GLN H . n 
H 1 1   ALA 1   1   1   ALA ALA I . n 
H 1 2   THR 2   2   2   THR THR I . n 
H 1 3   LYS 3   3   3   LYS LYS I . n 
H 1 4   ALA 4   4   4   ALA ALA I . n 
H 1 5   VAL 5   5   5   VAL VAL I . n 
H 1 6   CYS 6   6   6   CYS CYS I . n 
H 1 7   VAL 7   7   7   VAL VAL I . n 
H 1 8   LEU 8   8   8   LEU LEU I . n 
H 1 9   LYS 9   9   9   LYS LYS I . n 
H 1 10  GLY 10  10  10  GLY GLY I . n 
H 1 11  ASP 11  11  11  ASP ASP I . n 
H 1 12  GLY 12  12  12  GLY GLY I . n 
H 1 13  PRO 13  13  13  PRO PRO I . n 
H 1 14  VAL 14  14  14  VAL VAL I . n 
H 1 15  GLN 15  15  15  GLN GLN I . n 
H 1 16  GLY 16  16  16  GLY GLY I . n 
H 1 17  ILE 17  17  17  ILE ILE I . n 
H 1 18  ILE 18  18  18  ILE ILE I . n 
H 1 19  ASN 19  19  19  ASN ASN I . n 
H 1 20  PHE 20  20  20  PHE PHE I . n 
H 1 21  GLU 21  21  21  GLU GLU I . n 
H 1 22  GLN 22  22  22  GLN GLN I . n 
H 1 23  LYS 23  23  23  LYS LYS I . n 
H 1 24  GLU 24  24  24  GLU GLU I . n 
H 1 25  SER 25  25  25  SER SER I . n 
H 1 26  ASN 26  26  26  ASN ASN I . n 
H 1 27  GLY 27  27  27  GLY GLY I . n 
H 1 28  PRO 28  28  28  PRO PRO I . n 
H 1 29  VAL 29  29  29  VAL VAL I . n 
H 1 30  LYS 30  30  30  LYS LYS I . n 
H 1 31  VAL 31  31  31  VAL VAL I . n 
H 1 32  TRP 32  32  32  TRP TRP I . n 
H 1 33  GLY 33  33  33  GLY GLY I . n 
H 1 34  SER 34  34  34  SER SER I . n 
H 1 35  ILE 35  35  35  ILE ILE I . n 
H 1 36  LYS 36  36  36  LYS LYS I . n 
H 1 37  GLY 37  37  37  GLY GLY I . n 
H 1 38  LEU 38  38  38  LEU LEU I . n 
H 1 39  THR 39  39  39  THR THR I . n 
H 1 40  GLU 40  40  40  GLU GLU I . n 
H 1 41  GLY 41  41  41  GLY GLY I . n 
H 1 42  LEU 42  42  42  LEU LEU I . n 
H 1 43  HIS 43  43  43  HIS HIS I . n 
H 1 44  GLY 44  44  44  GLY GLY I . n 
H 1 45  PHE 45  45  45  PHE PHE I . n 
H 1 46  HIS 46  46  46  HIS HIS I . n 
H 1 47  VAL 47  47  47  VAL VAL I . n 
H 1 48  HIS 48  48  48  HIS HIS I . n 
H 1 49  GLU 49  49  49  GLU GLU I . n 
H 1 50  PHE 50  50  50  PHE PHE I . n 
H 1 51  GLY 51  51  51  GLY GLY I . n 
H 1 52  ASP 52  52  52  ASP ASP I . n 
H 1 53  ASN 53  53  53  ASN ASN I . n 
H 1 54  THR 54  54  54  THR THR I . n 
H 1 55  ALA 55  55  55  ALA ALA I . n 
H 1 56  GLY 56  56  56  GLY GLY I . n 
H 1 57  CYS 57  57  57  CYS CYS I . n 
H 1 58  THR 58  58  58  THR THR I . n 
H 1 59  SER 59  59  59  SER SER I . n 
H 1 60  ALA 60  60  60  ALA ALA I . n 
H 1 61  GLY 61  61  61  GLY GLY I . n 
H 1 62  PRO 62  62  62  PRO PRO I . n 
H 1 63  HIS 63  63  63  HIS HIS I . n 
H 1 64  PHE 64  64  64  PHE PHE I . n 
H 1 65  ASN 65  65  65  ASN ASN I . n 
H 1 66  PRO 66  66  66  PRO PRO I . n 
H 1 67  LEU 67  67  67  LEU LEU I . n 
H 1 68  SER 68  68  68  SER SER I . n 
H 1 69  ARG 69  69  69  ARG ARG I . n 
H 1 70  LYS 70  70  70  LYS LYS I . n 
H 1 71  HIS 71  71  71  HIS HIS I . n 
H 1 72  GLY 72  72  72  GLY GLY I . n 
H 1 73  GLY 73  73  73  GLY GLY I . n 
H 1 74  PRO 74  74  74  PRO PRO I . n 
H 1 75  LYS 75  75  75  LYS LYS I . n 
H 1 76  ASP 76  76  76  ASP ASP I . n 
H 1 77  GLU 77  77  77  GLU GLU I . n 
H 1 78  GLU 78  78  78  GLU GLU I . n 
H 1 79  ARG 79  79  79  ARG ARG I . n 
H 1 80  HIS 80  80  80  HIS HIS I . n 
H 1 81  VAL 81  81  81  VAL VAL I . n 
H 1 82  GLY 82  82  82  GLY GLY I . n 
H 1 83  ASP 83  83  83  ASP ASP I . n 
H 1 84  LEU 84  84  84  LEU LEU I . n 
H 1 85  GLY 85  85  85  GLY GLY I . n 
H 1 86  ASN 86  86  86  ASN ASN I . n 
H 1 87  VAL 87  87  87  VAL VAL I . n 
H 1 88  THR 88  88  88  THR THR I . n 
H 1 89  ALA 89  89  89  ALA ALA I . n 
H 1 90  ASP 90  90  90  ASP ASP I . n 
H 1 91  LYS 91  91  91  LYS LYS I . n 
H 1 92  ASP 92  92  92  ASP ASP I . n 
H 1 93  GLY 93  93  93  GLY GLY I . n 
H 1 94  VAL 94  94  94  VAL VAL I . n 
H 1 95  ALA 95  95  95  ALA ALA I . n 
H 1 96  ASP 96  96  96  ASP ASP I . n 
H 1 97  VAL 97  97  97  VAL VAL I . n 
H 1 98  SER 98  98  98  SER SER I . n 
H 1 99  ILE 99  99  99  ILE ILE I . n 
H 1 100 GLU 100 100 100 GLU GLU I . n 
H 1 101 ASP 101 101 101 ASP ASP I . n 
H 1 102 SER 102 102 102 SER SER I . n 
H 1 103 VAL 103 103 103 VAL VAL I . n 
H 1 104 ILE 104 104 104 ILE ILE I . n 
H 1 105 SER 105 105 105 SER SER I . n 
H 1 106 LEU 106 106 106 LEU LEU I . n 
H 1 107 SER 107 107 107 SER SER I . n 
H 1 108 GLY 108 108 108 GLY GLY I . n 
H 1 109 ASP 109 109 109 ASP ASP I . n 
H 1 110 HIS 110 110 110 HIS HIS I . n 
H 1 111 CME 111 111 111 CME CME I . n 
H 1 112 ILE 112 112 112 ILE ILE I . n 
H 1 113 ILE 113 113 113 ILE ILE I . n 
H 1 114 GLY 114 114 114 GLY GLY I . n 
H 1 115 ARG 115 115 115 ARG ARG I . n 
H 1 116 THR 116 116 116 THR THR I . n 
H 1 117 LEU 117 117 117 LEU LEU I . n 
H 1 118 VAL 118 118 118 VAL VAL I . n 
H 1 119 VAL 119 119 119 VAL VAL I . n 
H 1 120 HIS 120 120 120 HIS HIS I . n 
H 1 121 GLU 121 121 121 GLU GLU I . n 
H 1 122 LYS 122 122 122 LYS LYS I . n 
H 1 123 ALA 123 123 123 ALA ALA I . n 
H 1 124 ASP 124 124 124 ASP ASP I . n 
H 1 125 ASP 125 125 125 ASP ASP I . n 
H 1 126 LEU 126 126 126 LEU LEU I . n 
H 1 127 GLY 127 127 127 GLY GLY I . n 
H 1 128 LYS 128 128 128 LYS LYS I . n 
H 1 129 GLY 129 129 129 GLY GLY I . n 
H 1 130 GLY 130 130 130 GLY GLY I . n 
H 1 131 ASN 131 131 131 ASN ASN I . n 
H 1 132 GLU 132 132 132 GLU GLU I . n 
H 1 133 GLU 133 133 133 GLU GLU I . n 
H 1 134 SER 134 134 134 SER SER I . n 
H 1 135 THR 135 135 135 THR THR I . n 
H 1 136 LYS 136 136 136 LYS LYS I . n 
H 1 137 THR 137 137 137 THR THR I . n 
H 1 138 GLY 138 138 138 GLY GLY I . n 
H 1 139 ASN 139 139 139 ASN ASN I . n 
H 1 140 ALA 140 140 140 ALA ALA I . n 
H 1 141 GLY 141 141 141 GLY GLY I . n 
H 1 142 SER 142 142 142 SER SER I . n 
H 1 143 ARG 143 143 143 ARG ARG I . n 
H 1 144 LEU 144 144 144 LEU LEU I . n 
H 1 145 ALA 145 145 145 ALA ALA I . n 
H 1 146 CYS 146 146 146 CYS CYS I . n 
H 1 147 GLY 147 147 147 GLY GLY I . n 
H 1 148 VAL 148 148 148 VAL VAL I . n 
H 1 149 ILE 149 149 149 ILE ILE I . n 
H 1 150 GLY 150 150 150 GLY GLY I . n 
H 1 151 ILE 151 151 151 ILE ILE I . n 
H 1 152 ALA 152 152 152 ALA ALA I . n 
H 1 153 GLN 153 153 153 GLN GLN I . n 
I 1 1   ALA 1   1   1   ALA ALA J . n 
I 1 2   THR 2   2   2   THR THR J . n 
I 1 3   LYS 3   3   3   LYS LYS J . n 
I 1 4   ALA 4   4   4   ALA ALA J . n 
I 1 5   VAL 5   5   5   VAL VAL J . n 
I 1 6   CYS 6   6   6   CYS CYS J . n 
I 1 7   VAL 7   7   7   VAL VAL J . n 
I 1 8   LEU 8   8   8   LEU LEU J . n 
I 1 9   LYS 9   9   9   LYS LYS J . n 
I 1 10  GLY 10  10  10  GLY GLY J . n 
I 1 11  ASP 11  11  11  ASP ASP J . n 
I 1 12  GLY 12  12  12  GLY GLY J . n 
I 1 13  PRO 13  13  13  PRO PRO J . n 
I 1 14  VAL 14  14  14  VAL VAL J . n 
I 1 15  GLN 15  15  15  GLN GLN J . n 
I 1 16  GLY 16  16  16  GLY GLY J . n 
I 1 17  ILE 17  17  17  ILE ILE J . n 
I 1 18  ILE 18  18  18  ILE ILE J . n 
I 1 19  ASN 19  19  19  ASN ASN J . n 
I 1 20  PHE 20  20  20  PHE PHE J . n 
I 1 21  GLU 21  21  21  GLU GLU J . n 
I 1 22  GLN 22  22  22  GLN GLN J . n 
I 1 23  LYS 23  23  23  LYS LYS J . n 
I 1 24  GLU 24  24  24  GLU GLU J . n 
I 1 25  SER 25  25  25  SER SER J . n 
I 1 26  ASN 26  26  26  ASN ASN J . n 
I 1 27  GLY 27  27  27  GLY GLY J . n 
I 1 28  PRO 28  28  28  PRO PRO J . n 
I 1 29  VAL 29  29  29  VAL VAL J . n 
I 1 30  LYS 30  30  30  LYS LYS J . n 
I 1 31  VAL 31  31  31  VAL VAL J . n 
I 1 32  TRP 32  32  32  TRP TRP J . n 
I 1 33  GLY 33  33  33  GLY GLY J . n 
I 1 34  SER 34  34  34  SER SER J . n 
I 1 35  ILE 35  35  35  ILE ILE J . n 
I 1 36  LYS 36  36  36  LYS LYS J . n 
I 1 37  GLY 37  37  37  GLY GLY J . n 
I 1 38  LEU 38  38  38  LEU LEU J . n 
I 1 39  THR 39  39  39  THR THR J . n 
I 1 40  GLU 40  40  40  GLU GLU J . n 
I 1 41  GLY 41  41  41  GLY GLY J . n 
I 1 42  LEU 42  42  42  LEU LEU J . n 
I 1 43  HIS 43  43  43  HIS HIS J . n 
I 1 44  GLY 44  44  44  GLY GLY J . n 
I 1 45  PHE 45  45  45  PHE PHE J . n 
I 1 46  HIS 46  46  46  HIS HIS J . n 
I 1 47  VAL 47  47  47  VAL VAL J . n 
I 1 48  HIS 48  48  48  HIS HIS J . n 
I 1 49  GLU 49  49  49  GLU GLU J . n 
I 1 50  PHE 50  50  50  PHE PHE J . n 
I 1 51  GLY 51  51  51  GLY GLY J . n 
I 1 52  ASP 52  52  52  ASP ASP J . n 
I 1 53  ASN 53  53  53  ASN ASN J . n 
I 1 54  THR 54  54  54  THR THR J . n 
I 1 55  ALA 55  55  55  ALA ALA J . n 
I 1 56  GLY 56  56  56  GLY GLY J . n 
I 1 57  CYS 57  57  57  CYS CYS J . n 
I 1 58  THR 58  58  58  THR THR J . n 
I 1 59  SER 59  59  59  SER SER J . n 
I 1 60  ALA 60  60  60  ALA ALA J . n 
I 1 61  GLY 61  61  61  GLY GLY J . n 
I 1 62  PRO 62  62  62  PRO PRO J . n 
I 1 63  HIS 63  63  63  HIS HIS J . n 
I 1 64  PHE 64  64  64  PHE PHE J . n 
I 1 65  ASN 65  65  65  ASN ASN J . n 
I 1 66  PRO 66  66  66  PRO PRO J . n 
I 1 67  LEU 67  67  67  LEU LEU J . n 
I 1 68  SER 68  68  68  SER SER J . n 
I 1 69  ARG 69  69  69  ARG ARG J . n 
I 1 70  LYS 70  70  70  LYS LYS J . n 
I 1 71  HIS 71  71  71  HIS HIS J . n 
I 1 72  GLY 72  72  72  GLY GLY J . n 
I 1 73  GLY 73  73  73  GLY GLY J . n 
I 1 74  PRO 74  74  74  PRO PRO J . n 
I 1 75  LYS 75  75  75  LYS LYS J . n 
I 1 76  ASP 76  76  76  ASP ASP J . n 
I 1 77  GLU 77  77  77  GLU GLU J . n 
I 1 78  GLU 78  78  78  GLU GLU J . n 
I 1 79  ARG 79  79  79  ARG ARG J . n 
I 1 80  HIS 80  80  80  HIS HIS J . n 
I 1 81  VAL 81  81  81  VAL VAL J . n 
I 1 82  GLY 82  82  82  GLY GLY J . n 
I 1 83  ASP 83  83  83  ASP ASP J . n 
I 1 84  LEU 84  84  84  LEU LEU J . n 
I 1 85  GLY 85  85  85  GLY GLY J . n 
I 1 86  ASN 86  86  86  ASN ASN J . n 
I 1 87  VAL 87  87  87  VAL VAL J . n 
I 1 88  THR 88  88  88  THR THR J . n 
I 1 89  ALA 89  89  89  ALA ALA J . n 
I 1 90  ASP 90  90  90  ASP ASP J . n 
I 1 91  LYS 91  91  91  LYS LYS J . n 
I 1 92  ASP 92  92  92  ASP ASP J . n 
I 1 93  GLY 93  93  93  GLY GLY J . n 
I 1 94  VAL 94  94  94  VAL VAL J . n 
I 1 95  ALA 95  95  95  ALA ALA J . n 
I 1 96  ASP 96  96  96  ASP ASP J . n 
I 1 97  VAL 97  97  97  VAL VAL J . n 
I 1 98  SER 98  98  98  SER SER J . n 
I 1 99  ILE 99  99  99  ILE ILE J . n 
I 1 100 GLU 100 100 100 GLU GLU J . n 
I 1 101 ASP 101 101 101 ASP ASP J . n 
I 1 102 SER 102 102 102 SER SER J . n 
I 1 103 VAL 103 103 103 VAL VAL J . n 
I 1 104 ILE 104 104 104 ILE ILE J . n 
I 1 105 SER 105 105 105 SER SER J . n 
I 1 106 LEU 106 106 106 LEU LEU J . n 
I 1 107 SER 107 107 107 SER SER J . n 
I 1 108 GLY 108 108 108 GLY GLY J . n 
I 1 109 ASP 109 109 109 ASP ASP J . n 
I 1 110 HIS 110 110 110 HIS HIS J . n 
I 1 111 CME 111 111 111 CME CME J . n 
I 1 112 ILE 112 112 112 ILE ILE J . n 
I 1 113 ILE 113 113 113 ILE ILE J . n 
I 1 114 GLY 114 114 114 GLY GLY J . n 
I 1 115 ARG 115 115 115 ARG ARG J . n 
I 1 116 THR 116 116 116 THR THR J . n 
I 1 117 LEU 117 117 117 LEU LEU J . n 
I 1 118 VAL 118 118 118 VAL VAL J . n 
I 1 119 VAL 119 119 119 VAL VAL J . n 
I 1 120 HIS 120 120 120 HIS HIS J . n 
I 1 121 GLU 121 121 121 GLU GLU J . n 
I 1 122 LYS 122 122 122 LYS LYS J . n 
I 1 123 ALA 123 123 123 ALA ALA J . n 
I 1 124 ASP 124 124 124 ASP ASP J . n 
I 1 125 ASP 125 125 125 ASP ASP J . n 
I 1 126 LEU 126 126 126 LEU LEU J . n 
I 1 127 GLY 127 127 127 GLY GLY J . n 
I 1 128 LYS 128 128 128 LYS LYS J . n 
I 1 129 GLY 129 129 129 GLY GLY J . n 
I 1 130 GLY 130 130 130 GLY GLY J . n 
I 1 131 ASN 131 131 131 ASN ASN J . n 
I 1 132 GLU 132 132 132 GLU GLU J . n 
I 1 133 GLU 133 133 133 GLU GLU J . n 
I 1 134 SER 134 134 134 SER SER J . n 
I 1 135 THR 135 135 135 THR THR J . n 
I 1 136 LYS 136 136 136 LYS LYS J . n 
I 1 137 THR 137 137 137 THR THR J . n 
I 1 138 GLY 138 138 138 GLY GLY J . n 
I 1 139 ASN 139 139 139 ASN ASN J . n 
I 1 140 ALA 140 140 140 ALA ALA J . n 
I 1 141 GLY 141 141 141 GLY GLY J . n 
I 1 142 SER 142 142 142 SER SER J . n 
I 1 143 ARG 143 143 143 ARG ARG J . n 
I 1 144 LEU 144 144 144 LEU LEU J . n 
I 1 145 ALA 145 145 145 ALA ALA J . n 
I 1 146 CYS 146 146 146 CYS CYS J . n 
I 1 147 GLY 147 147 147 GLY GLY J . n 
I 1 148 VAL 148 148 148 VAL VAL J . n 
I 1 149 ILE 149 149 149 ILE ILE J . n 
I 1 150 GLY 150 150 150 GLY GLY J . n 
I 1 151 ILE 151 151 151 ILE ILE J . n 
I 1 152 ALA 152 152 152 ALA ALA J . n 
I 1 153 GLN 153 153 153 GLN GLN J . n 
J 1 1   ALA 1   1   1   ALA ALA K . n 
J 1 2   THR 2   2   2   THR THR K . n 
J 1 3   LYS 3   3   3   LYS LYS K . n 
J 1 4   ALA 4   4   4   ALA ALA K . n 
J 1 5   VAL 5   5   5   VAL VAL K . n 
J 1 6   CYS 6   6   6   CYS CYS K . n 
J 1 7   VAL 7   7   7   VAL VAL K . n 
J 1 8   LEU 8   8   8   LEU LEU K . n 
J 1 9   LYS 9   9   9   LYS LYS K . n 
J 1 10  GLY 10  10  10  GLY GLY K . n 
J 1 11  ASP 11  11  11  ASP ASP K . n 
J 1 12  GLY 12  12  12  GLY GLY K . n 
J 1 13  PRO 13  13  13  PRO PRO K . n 
J 1 14  VAL 14  14  14  VAL VAL K . n 
J 1 15  GLN 15  15  15  GLN GLN K . n 
J 1 16  GLY 16  16  16  GLY GLY K . n 
J 1 17  ILE 17  17  17  ILE ILE K . n 
J 1 18  ILE 18  18  18  ILE ILE K . n 
J 1 19  ASN 19  19  19  ASN ASN K . n 
J 1 20  PHE 20  20  20  PHE PHE K . n 
J 1 21  GLU 21  21  21  GLU GLU K . n 
J 1 22  GLN 22  22  22  GLN GLN K . n 
J 1 23  LYS 23  23  23  LYS LYS K . n 
J 1 24  GLU 24  24  24  GLU GLU K . n 
J 1 25  SER 25  25  25  SER SER K . n 
J 1 26  ASN 26  26  26  ASN ASN K . n 
J 1 27  GLY 27  27  27  GLY GLY K . n 
J 1 28  PRO 28  28  28  PRO PRO K . n 
J 1 29  VAL 29  29  29  VAL VAL K . n 
J 1 30  LYS 30  30  30  LYS LYS K . n 
J 1 31  VAL 31  31  31  VAL VAL K . n 
J 1 32  TRP 32  32  32  TRP TRP K . n 
J 1 33  GLY 33  33  33  GLY GLY K . n 
J 1 34  SER 34  34  34  SER SER K . n 
J 1 35  ILE 35  35  35  ILE ILE K . n 
J 1 36  LYS 36  36  36  LYS LYS K . n 
J 1 37  GLY 37  37  37  GLY GLY K . n 
J 1 38  LEU 38  38  38  LEU LEU K . n 
J 1 39  THR 39  39  39  THR THR K . n 
J 1 40  GLU 40  40  40  GLU GLU K . n 
J 1 41  GLY 41  41  41  GLY GLY K . n 
J 1 42  LEU 42  42  42  LEU LEU K . n 
J 1 43  HIS 43  43  43  HIS HIS K . n 
J 1 44  GLY 44  44  44  GLY GLY K . n 
J 1 45  PHE 45  45  45  PHE PHE K . n 
J 1 46  HIS 46  46  46  HIS HIS K . n 
J 1 47  VAL 47  47  47  VAL VAL K . n 
J 1 48  HIS 48  48  48  HIS HIS K . n 
J 1 49  GLU 49  49  49  GLU GLU K . n 
J 1 50  PHE 50  50  50  PHE PHE K . n 
J 1 51  GLY 51  51  51  GLY GLY K . n 
J 1 52  ASP 52  52  52  ASP ASP K . n 
J 1 53  ASN 53  53  53  ASN ASN K . n 
J 1 54  THR 54  54  54  THR THR K . n 
J 1 55  ALA 55  55  55  ALA ALA K . n 
J 1 56  GLY 56  56  56  GLY GLY K . n 
J 1 57  CYS 57  57  57  CYS CYS K . n 
J 1 58  THR 58  58  58  THR THR K . n 
J 1 59  SER 59  59  59  SER SER K . n 
J 1 60  ALA 60  60  60  ALA ALA K . n 
J 1 61  GLY 61  61  61  GLY GLY K . n 
J 1 62  PRO 62  62  62  PRO PRO K . n 
J 1 63  HIS 63  63  63  HIS HIS K . n 
J 1 64  PHE 64  64  64  PHE PHE K . n 
J 1 65  ASN 65  65  65  ASN ASN K . n 
J 1 66  PRO 66  66  66  PRO PRO K . n 
J 1 67  LEU 67  67  67  LEU LEU K . n 
J 1 68  SER 68  68  68  SER SER K . n 
J 1 69  ARG 69  69  69  ARG ARG K . n 
J 1 70  LYS 70  70  70  LYS LYS K . n 
J 1 71  HIS 71  71  71  HIS HIS K . n 
J 1 72  GLY 72  72  72  GLY GLY K . n 
J 1 73  GLY 73  73  73  GLY GLY K . n 
J 1 74  PRO 74  74  74  PRO PRO K . n 
J 1 75  LYS 75  75  75  LYS LYS K . n 
J 1 76  ASP 76  76  76  ASP ASP K . n 
J 1 77  GLU 77  77  77  GLU GLU K . n 
J 1 78  GLU 78  78  78  GLU GLU K . n 
J 1 79  ARG 79  79  79  ARG ARG K . n 
J 1 80  HIS 80  80  80  HIS HIS K . n 
J 1 81  VAL 81  81  81  VAL VAL K . n 
J 1 82  GLY 82  82  82  GLY GLY K . n 
J 1 83  ASP 83  83  83  ASP ASP K . n 
J 1 84  LEU 84  84  84  LEU LEU K . n 
J 1 85  GLY 85  85  85  GLY GLY K . n 
J 1 86  ASN 86  86  86  ASN ASN K . n 
J 1 87  VAL 87  87  87  VAL VAL K . n 
J 1 88  THR 88  88  88  THR THR K . n 
J 1 89  ALA 89  89  89  ALA ALA K . n 
J 1 90  ASP 90  90  90  ASP ASP K . n 
J 1 91  LYS 91  91  91  LYS LYS K . n 
J 1 92  ASP 92  92  92  ASP ASP K . n 
J 1 93  GLY 93  93  93  GLY GLY K . n 
J 1 94  VAL 94  94  94  VAL VAL K . n 
J 1 95  ALA 95  95  95  ALA ALA K . n 
J 1 96  ASP 96  96  96  ASP ASP K . n 
J 1 97  VAL 97  97  97  VAL VAL K . n 
J 1 98  SER 98  98  98  SER SER K . n 
J 1 99  ILE 99  99  99  ILE ILE K . n 
J 1 100 GLU 100 100 100 GLU GLU K . n 
J 1 101 ASP 101 101 101 ASP ASP K . n 
J 1 102 SER 102 102 102 SER SER K . n 
J 1 103 VAL 103 103 103 VAL VAL K . n 
J 1 104 ILE 104 104 104 ILE ILE K . n 
J 1 105 SER 105 105 105 SER SER K . n 
J 1 106 LEU 106 106 106 LEU LEU K . n 
J 1 107 SER 107 107 107 SER SER K . n 
J 1 108 GLY 108 108 108 GLY GLY K . n 
J 1 109 ASP 109 109 109 ASP ASP K . n 
J 1 110 HIS 110 110 110 HIS HIS K . n 
J 1 111 CME 111 111 111 CME CME K . n 
J 1 112 ILE 112 112 112 ILE ILE K . n 
J 1 113 ILE 113 113 113 ILE ILE K . n 
J 1 114 GLY 114 114 114 GLY GLY K . n 
J 1 115 ARG 115 115 115 ARG ARG K . n 
J 1 116 THR 116 116 116 THR THR K . n 
J 1 117 LEU 117 117 117 LEU LEU K . n 
J 1 118 VAL 118 118 118 VAL VAL K . n 
J 1 119 VAL 119 119 119 VAL VAL K . n 
J 1 120 HIS 120 120 120 HIS HIS K . n 
J 1 121 GLU 121 121 121 GLU GLU K . n 
J 1 122 LYS 122 122 122 LYS LYS K . n 
J 1 123 ALA 123 123 123 ALA ALA K . n 
J 1 124 ASP 124 124 124 ASP ASP K . n 
J 1 125 ASP 125 125 125 ASP ASP K . n 
J 1 126 LEU 126 126 126 LEU LEU K . n 
J 1 127 GLY 127 127 127 GLY GLY K . n 
J 1 128 LYS 128 128 128 LYS LYS K . n 
J 1 129 GLY 129 129 129 GLY GLY K . n 
J 1 130 GLY 130 130 130 GLY GLY K . n 
J 1 131 ASN 131 131 131 ASN ASN K . n 
J 1 132 GLU 132 132 132 GLU GLU K . n 
J 1 133 GLU 133 133 133 GLU GLU K . n 
J 1 134 SER 134 134 134 SER SER K . n 
J 1 135 THR 135 135 135 THR THR K . n 
J 1 136 LYS 136 136 136 LYS LYS K . n 
J 1 137 THR 137 137 137 THR THR K . n 
J 1 138 GLY 138 138 138 GLY GLY K . n 
J 1 139 ASN 139 139 139 ASN ASN K . n 
J 1 140 ALA 140 140 140 ALA ALA K . n 
J 1 141 GLY 141 141 141 GLY GLY K . n 
J 1 142 SER 142 142 142 SER SER K . n 
J 1 143 ARG 143 143 143 ARG ARG K . n 
J 1 144 LEU 144 144 144 LEU LEU K . n 
J 1 145 ALA 145 145 145 ALA ALA K . n 
J 1 146 CYS 146 146 146 CYS CYS K . n 
J 1 147 GLY 147 147 147 GLY GLY K . n 
J 1 148 VAL 148 148 148 VAL VAL K . n 
J 1 149 ILE 149 149 149 ILE ILE K . n 
J 1 150 GLY 150 150 150 GLY GLY K . n 
J 1 151 ILE 151 151 151 ILE ILE K . n 
J 1 152 ALA 152 152 152 ALA ALA K . n 
J 1 153 GLN 153 153 153 GLN GLN K . n 
K 1 1   ALA 1   1   1   ALA ALA L . n 
K 1 2   THR 2   2   2   THR THR L . n 
K 1 3   LYS 3   3   3   LYS LYS L . n 
K 1 4   ALA 4   4   4   ALA ALA L . n 
K 1 5   VAL 5   5   5   VAL VAL L . n 
K 1 6   CYS 6   6   6   CYS CYS L . n 
K 1 7   VAL 7   7   7   VAL VAL L . n 
K 1 8   LEU 8   8   8   LEU LEU L . n 
K 1 9   LYS 9   9   9   LYS LYS L . n 
K 1 10  GLY 10  10  10  GLY GLY L . n 
K 1 11  ASP 11  11  11  ASP ASP L . n 
K 1 12  GLY 12  12  12  GLY GLY L . n 
K 1 13  PRO 13  13  13  PRO PRO L . n 
K 1 14  VAL 14  14  14  VAL VAL L . n 
K 1 15  GLN 15  15  15  GLN GLN L . n 
K 1 16  GLY 16  16  16  GLY GLY L . n 
K 1 17  ILE 17  17  17  ILE ILE L . n 
K 1 18  ILE 18  18  18  ILE ILE L . n 
K 1 19  ASN 19  19  19  ASN ASN L . n 
K 1 20  PHE 20  20  20  PHE PHE L . n 
K 1 21  GLU 21  21  21  GLU GLU L . n 
K 1 22  GLN 22  22  22  GLN GLN L . n 
K 1 23  LYS 23  23  23  LYS LYS L . n 
K 1 24  GLU 24  24  24  GLU GLU L . n 
K 1 25  SER 25  25  25  SER SER L . n 
K 1 26  ASN 26  26  26  ASN ASN L . n 
K 1 27  GLY 27  27  27  GLY GLY L . n 
K 1 28  PRO 28  28  28  PRO PRO L . n 
K 1 29  VAL 29  29  29  VAL VAL L . n 
K 1 30  LYS 30  30  30  LYS LYS L . n 
K 1 31  VAL 31  31  31  VAL VAL L . n 
K 1 32  TRP 32  32  32  TRP TRP L . n 
K 1 33  GLY 33  33  33  GLY GLY L . n 
K 1 34  SER 34  34  34  SER SER L . n 
K 1 35  ILE 35  35  35  ILE ILE L . n 
K 1 36  LYS 36  36  36  LYS LYS L . n 
K 1 37  GLY 37  37  37  GLY GLY L . n 
K 1 38  LEU 38  38  38  LEU LEU L . n 
K 1 39  THR 39  39  39  THR THR L . n 
K 1 40  GLU 40  40  40  GLU GLU L . n 
K 1 41  GLY 41  41  41  GLY GLY L . n 
K 1 42  LEU 42  42  42  LEU LEU L . n 
K 1 43  HIS 43  43  43  HIS HIS L . n 
K 1 44  GLY 44  44  44  GLY GLY L . n 
K 1 45  PHE 45  45  45  PHE PHE L . n 
K 1 46  HIS 46  46  46  HIS HIS L . n 
K 1 47  VAL 47  47  47  VAL VAL L . n 
K 1 48  HIS 48  48  48  HIS HIS L . n 
K 1 49  GLU 49  49  49  GLU GLU L . n 
K 1 50  PHE 50  50  50  PHE PHE L . n 
K 1 51  GLY 51  51  51  GLY GLY L . n 
K 1 52  ASP 52  52  52  ASP ASP L . n 
K 1 53  ASN 53  53  53  ASN ASN L . n 
K 1 54  THR 54  54  54  THR THR L . n 
K 1 55  ALA 55  55  55  ALA ALA L . n 
K 1 56  GLY 56  56  56  GLY GLY L . n 
K 1 57  CYS 57  57  57  CYS CYS L . n 
K 1 58  THR 58  58  58  THR THR L . n 
K 1 59  SER 59  59  59  SER SER L . n 
K 1 60  ALA 60  60  60  ALA ALA L . n 
K 1 61  GLY 61  61  61  GLY GLY L . n 
K 1 62  PRO 62  62  62  PRO PRO L . n 
K 1 63  HIS 63  63  63  HIS HIS L . n 
K 1 64  PHE 64  64  64  PHE PHE L . n 
K 1 65  ASN 65  65  65  ASN ASN L . n 
K 1 66  PRO 66  66  66  PRO PRO L . n 
K 1 67  LEU 67  67  67  LEU LEU L . n 
K 1 68  SER 68  68  68  SER SER L . n 
K 1 69  ARG 69  69  69  ARG ARG L . n 
K 1 70  LYS 70  70  70  LYS LYS L . n 
K 1 71  HIS 71  71  71  HIS HIS L . n 
K 1 72  GLY 72  72  72  GLY GLY L . n 
K 1 73  GLY 73  73  73  GLY GLY L . n 
K 1 74  PRO 74  74  74  PRO PRO L . n 
K 1 75  LYS 75  75  75  LYS LYS L . n 
K 1 76  ASP 76  76  76  ASP ASP L . n 
K 1 77  GLU 77  77  77  GLU GLU L . n 
K 1 78  GLU 78  78  78  GLU GLU L . n 
K 1 79  ARG 79  79  79  ARG ARG L . n 
K 1 80  HIS 80  80  80  HIS HIS L . n 
K 1 81  VAL 81  81  81  VAL VAL L . n 
K 1 82  GLY 82  82  82  GLY GLY L . n 
K 1 83  ASP 83  83  83  ASP ASP L . n 
K 1 84  LEU 84  84  84  LEU LEU L . n 
K 1 85  GLY 85  85  85  GLY GLY L . n 
K 1 86  ASN 86  86  86  ASN ASN L . n 
K 1 87  VAL 87  87  87  VAL VAL L . n 
K 1 88  THR 88  88  88  THR THR L . n 
K 1 89  ALA 89  89  89  ALA ALA L . n 
K 1 90  ASP 90  90  90  ASP ASP L . n 
K 1 91  LYS 91  91  91  LYS LYS L . n 
K 1 92  ASP 92  92  92  ASP ASP L . n 
K 1 93  GLY 93  93  93  GLY GLY L . n 
K 1 94  VAL 94  94  94  VAL VAL L . n 
K 1 95  ALA 95  95  95  ALA ALA L . n 
K 1 96  ASP 96  96  96  ASP ASP L . n 
K 1 97  VAL 97  97  97  VAL VAL L . n 
K 1 98  SER 98  98  98  SER SER L . n 
K 1 99  ILE 99  99  99  ILE ILE L . n 
K 1 100 GLU 100 100 100 GLU GLU L . n 
K 1 101 ASP 101 101 101 ASP ASP L . n 
K 1 102 SER 102 102 102 SER SER L . n 
K 1 103 VAL 103 103 103 VAL VAL L . n 
K 1 104 ILE 104 104 104 ILE ILE L . n 
K 1 105 SER 105 105 105 SER SER L . n 
K 1 106 LEU 106 106 106 LEU LEU L . n 
K 1 107 SER 107 107 107 SER SER L . n 
K 1 108 GLY 108 108 108 GLY GLY L . n 
K 1 109 ASP 109 109 109 ASP ASP L . n 
K 1 110 HIS 110 110 110 HIS HIS L . n 
K 1 111 CME 111 111 111 CME CME L . n 
K 1 112 ILE 112 112 112 ILE ILE L . n 
K 1 113 ILE 113 113 113 ILE ILE L . n 
K 1 114 GLY 114 114 114 GLY GLY L . n 
K 1 115 ARG 115 115 115 ARG ARG L . n 
K 1 116 THR 116 116 116 THR THR L . n 
K 1 117 LEU 117 117 117 LEU LEU L . n 
K 1 118 VAL 118 118 118 VAL VAL L . n 
K 1 119 VAL 119 119 119 VAL VAL L . n 
K 1 120 HIS 120 120 120 HIS HIS L . n 
K 1 121 GLU 121 121 121 GLU GLU L . n 
K 1 122 LYS 122 122 122 LYS LYS L . n 
K 1 123 ALA 123 123 123 ALA ALA L . n 
K 1 124 ASP 124 124 124 ASP ASP L . n 
K 1 125 ASP 125 125 125 ASP ASP L . n 
K 1 126 LEU 126 126 126 LEU LEU L . n 
K 1 127 GLY 127 127 127 GLY GLY L . n 
K 1 128 LYS 128 128 128 LYS LYS L . n 
K 1 129 GLY 129 129 129 GLY GLY L . n 
K 1 130 GLY 130 130 130 GLY GLY L . n 
K 1 131 ASN 131 131 131 ASN ASN L . n 
K 1 132 GLU 132 132 132 GLU GLU L . n 
K 1 133 GLU 133 133 133 GLU GLU L . n 
K 1 134 SER 134 134 134 SER SER L . n 
K 1 135 THR 135 135 135 THR THR L . n 
K 1 136 LYS 136 136 136 LYS LYS L . n 
K 1 137 THR 137 137 137 THR THR L . n 
K 1 138 GLY 138 138 138 GLY GLY L . n 
K 1 139 ASN 139 139 139 ASN ASN L . n 
K 1 140 ALA 140 140 140 ALA ALA L . n 
K 1 141 GLY 141 141 141 GLY GLY L . n 
K 1 142 SER 142 142 142 SER SER L . n 
K 1 143 ARG 143 143 143 ARG ARG L . n 
K 1 144 LEU 144 144 144 LEU LEU L . n 
K 1 145 ALA 145 145 145 ALA ALA L . n 
K 1 146 CYS 146 146 146 CYS CYS L . n 
K 1 147 GLY 147 147 147 GLY GLY L . n 
K 1 148 VAL 148 148 148 VAL VAL L . n 
K 1 149 ILE 149 149 149 ILE ILE L . n 
K 1 150 GLY 150 150 150 GLY GLY L . n 
K 1 151 ILE 151 151 151 ILE ILE L . n 
K 1 152 ALA 152 152 152 ALA ALA L . n 
K 1 153 GLN 153 153 153 GLN GLN L . n 
L 1 1   ALA 1   1   1   ALA ALA M . n 
L 1 2   THR 2   2   2   THR THR M . n 
L 1 3   LYS 3   3   3   LYS LYS M . n 
L 1 4   ALA 4   4   4   ALA ALA M . n 
L 1 5   VAL 5   5   5   VAL VAL M . n 
L 1 6   CYS 6   6   6   CYS CYS M . n 
L 1 7   VAL 7   7   7   VAL VAL M . n 
L 1 8   LEU 8   8   8   LEU LEU M . n 
L 1 9   LYS 9   9   9   LYS LYS M . n 
L 1 10  GLY 10  10  10  GLY GLY M . n 
L 1 11  ASP 11  11  11  ASP ASP M . n 
L 1 12  GLY 12  12  12  GLY GLY M . n 
L 1 13  PRO 13  13  13  PRO PRO M . n 
L 1 14  VAL 14  14  14  VAL VAL M . n 
L 1 15  GLN 15  15  15  GLN GLN M . n 
L 1 16  GLY 16  16  16  GLY GLY M . n 
L 1 17  ILE 17  17  17  ILE ILE M . n 
L 1 18  ILE 18  18  18  ILE ILE M . n 
L 1 19  ASN 19  19  19  ASN ASN M . n 
L 1 20  PHE 20  20  20  PHE PHE M . n 
L 1 21  GLU 21  21  21  GLU GLU M . n 
L 1 22  GLN 22  22  22  GLN GLN M . n 
L 1 23  LYS 23  23  23  LYS LYS M . n 
L 1 24  GLU 24  24  24  GLU GLU M . n 
L 1 25  SER 25  25  25  SER SER M . n 
L 1 26  ASN 26  26  26  ASN ASN M . n 
L 1 27  GLY 27  27  27  GLY GLY M . n 
L 1 28  PRO 28  28  28  PRO PRO M . n 
L 1 29  VAL 29  29  29  VAL VAL M . n 
L 1 30  LYS 30  30  30  LYS LYS M . n 
L 1 31  VAL 31  31  31  VAL VAL M . n 
L 1 32  TRP 32  32  32  TRP TRP M . n 
L 1 33  GLY 33  33  33  GLY GLY M . n 
L 1 34  SER 34  34  34  SER SER M . n 
L 1 35  ILE 35  35  35  ILE ILE M . n 
L 1 36  LYS 36  36  36  LYS LYS M . n 
L 1 37  GLY 37  37  37  GLY GLY M . n 
L 1 38  LEU 38  38  38  LEU LEU M . n 
L 1 39  THR 39  39  39  THR THR M . n 
L 1 40  GLU 40  40  40  GLU GLU M . n 
L 1 41  GLY 41  41  41  GLY GLY M . n 
L 1 42  LEU 42  42  42  LEU LEU M . n 
L 1 43  HIS 43  43  43  HIS HIS M . n 
L 1 44  GLY 44  44  44  GLY GLY M . n 
L 1 45  PHE 45  45  45  PHE PHE M . n 
L 1 46  HIS 46  46  46  HIS HIS M . n 
L 1 47  VAL 47  47  47  VAL VAL M . n 
L 1 48  HIS 48  48  48  HIS HIS M . n 
L 1 49  GLU 49  49  49  GLU GLU M . n 
L 1 50  PHE 50  50  50  PHE PHE M . n 
L 1 51  GLY 51  51  51  GLY GLY M . n 
L 1 52  ASP 52  52  52  ASP ASP M . n 
L 1 53  ASN 53  53  53  ASN ASN M . n 
L 1 54  THR 54  54  54  THR THR M . n 
L 1 55  ALA 55  55  55  ALA ALA M . n 
L 1 56  GLY 56  56  56  GLY GLY M . n 
L 1 57  CYS 57  57  57  CYS CYS M . n 
L 1 58  THR 58  58  58  THR THR M . n 
L 1 59  SER 59  59  59  SER SER M . n 
L 1 60  ALA 60  60  60  ALA ALA M . n 
L 1 61  GLY 61  61  61  GLY GLY M . n 
L 1 62  PRO 62  62  62  PRO PRO M . n 
L 1 63  HIS 63  63  63  HIS HIS M . n 
L 1 64  PHE 64  64  64  PHE PHE M . n 
L 1 65  ASN 65  65  65  ASN ASN M . n 
L 1 66  PRO 66  66  66  PRO PRO M . n 
L 1 67  LEU 67  67  67  LEU LEU M . n 
L 1 68  SER 68  68  68  SER SER M . n 
L 1 69  ARG 69  69  69  ARG ARG M . n 
L 1 70  LYS 70  70  70  LYS LYS M . n 
L 1 71  HIS 71  71  71  HIS HIS M . n 
L 1 72  GLY 72  72  72  GLY GLY M . n 
L 1 73  GLY 73  73  73  GLY GLY M . n 
L 1 74  PRO 74  74  74  PRO PRO M . n 
L 1 75  LYS 75  75  75  LYS LYS M . n 
L 1 76  ASP 76  76  76  ASP ASP M . n 
L 1 77  GLU 77  77  77  GLU GLU M . n 
L 1 78  GLU 78  78  78  GLU GLU M . n 
L 1 79  ARG 79  79  79  ARG ARG M . n 
L 1 80  HIS 80  80  80  HIS HIS M . n 
L 1 81  VAL 81  81  81  VAL VAL M . n 
L 1 82  GLY 82  82  82  GLY GLY M . n 
L 1 83  ASP 83  83  83  ASP ASP M . n 
L 1 84  LEU 84  84  84  LEU LEU M . n 
L 1 85  GLY 85  85  85  GLY GLY M . n 
L 1 86  ASN 86  86  86  ASN ASN M . n 
L 1 87  VAL 87  87  87  VAL VAL M . n 
L 1 88  THR 88  88  88  THR THR M . n 
L 1 89  ALA 89  89  89  ALA ALA M . n 
L 1 90  ASP 90  90  90  ASP ASP M . n 
L 1 91  LYS 91  91  91  LYS LYS M . n 
L 1 92  ASP 92  92  92  ASP ASP M . n 
L 1 93  GLY 93  93  93  GLY GLY M . n 
L 1 94  VAL 94  94  94  VAL VAL M . n 
L 1 95  ALA 95  95  95  ALA ALA M . n 
L 1 96  ASP 96  96  96  ASP ASP M . n 
L 1 97  VAL 97  97  97  VAL VAL M . n 
L 1 98  SER 98  98  98  SER SER M . n 
L 1 99  ILE 99  99  99  ILE ILE M . n 
L 1 100 GLU 100 100 100 GLU GLU M . n 
L 1 101 ASP 101 101 101 ASP ASP M . n 
L 1 102 SER 102 102 102 SER SER M . n 
L 1 103 VAL 103 103 103 VAL VAL M . n 
L 1 104 ILE 104 104 104 ILE ILE M . n 
L 1 105 SER 105 105 105 SER SER M . n 
L 1 106 LEU 106 106 106 LEU LEU M . n 
L 1 107 SER 107 107 107 SER SER M . n 
L 1 108 GLY 108 108 108 GLY GLY M . n 
L 1 109 ASP 109 109 109 ASP ASP M . n 
L 1 110 HIS 110 110 110 HIS HIS M . n 
L 1 111 CME 111 111 111 CME CME M . n 
L 1 112 ILE 112 112 112 ILE ILE M . n 
L 1 113 ILE 113 113 113 ILE ILE M . n 
L 1 114 GLY 114 114 114 GLY GLY M . n 
L 1 115 ARG 115 115 115 ARG ARG M . n 
L 1 116 THR 116 116 116 THR THR M . n 
L 1 117 LEU 117 117 117 LEU LEU M . n 
L 1 118 VAL 118 118 118 VAL VAL M . n 
L 1 119 VAL 119 119 119 VAL VAL M . n 
L 1 120 HIS 120 120 120 HIS HIS M . n 
L 1 121 GLU 121 121 121 GLU GLU M . n 
L 1 122 LYS 122 122 122 LYS LYS M . n 
L 1 123 ALA 123 123 123 ALA ALA M . n 
L 1 124 ASP 124 124 124 ASP ASP M . n 
L 1 125 ASP 125 125 125 ASP ASP M . n 
L 1 126 LEU 126 126 126 LEU LEU M . n 
L 1 127 GLY 127 127 127 GLY GLY M . n 
L 1 128 LYS 128 128 128 LYS LYS M . n 
L 1 129 GLY 129 129 129 GLY GLY M . n 
L 1 130 GLY 130 130 130 GLY GLY M . n 
L 1 131 ASN 131 131 131 ASN ASN M . n 
L 1 132 GLU 132 132 132 GLU GLU M . n 
L 1 133 GLU 133 133 133 GLU GLU M . n 
L 1 134 SER 134 134 134 SER SER M . n 
L 1 135 THR 135 135 135 THR THR M . n 
L 1 136 LYS 136 136 136 LYS LYS M . n 
L 1 137 THR 137 137 137 THR THR M . n 
L 1 138 GLY 138 138 138 GLY GLY M . n 
L 1 139 ASN 139 139 139 ASN ASN M . n 
L 1 140 ALA 140 140 140 ALA ALA M . n 
L 1 141 GLY 141 141 141 GLY GLY M . n 
L 1 142 SER 142 142 142 SER SER M . n 
L 1 143 ARG 143 143 143 ARG ARG M . n 
L 1 144 LEU 144 144 144 LEU LEU M . n 
L 1 145 ALA 145 145 145 ALA ALA M . n 
L 1 146 CYS 146 146 146 CYS CYS M . n 
L 1 147 GLY 147 147 147 GLY GLY M . n 
L 1 148 VAL 148 148 148 VAL VAL M . n 
L 1 149 ILE 149 149 149 ILE ILE M . n 
L 1 150 GLY 150 150 150 GLY GLY M . n 
L 1 151 ILE 151 151 151 ILE ILE M . n 
L 1 152 ALA 152 152 152 ALA ALA M . n 
L 1 153 GLN 153 153 153 GLN GLN M . n 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1  A CME 111 A CME 111 ? CYS 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' 
2  B CME 111 B CME 111 ? CYS 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' 
3  C CME 111 D CME 111 ? CYS 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' 
4  D CME 111 E CME 111 ? CYS 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' 
5  E CME 111 F CME 111 ? CYS 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' 
6  F CME 111 G CME 111 ? CYS 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' 
7  G CME 111 H CME 111 ? CYS 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' 
8  H CME 111 I CME 111 ? CYS 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' 
9  I CME 111 J CME 111 ? CYS 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' 
10 J CME 111 K CME 111 ? CYS 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' 
11 K CME 111 L CME 111 ? CYS 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' 
12 L CME 111 M CME 111 ? CYS 'S,S-(2-HYDROXYETHYL)THIOCYSTEINE' 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA dimeric 2 
2 author_and_software_defined_assembly PISA dimeric 2 
3 author_and_software_defined_assembly PISA dimeric 2 
4 author_and_software_defined_assembly PISA dimeric 2 
5 author_and_software_defined_assembly PISA dimeric 2 
6 author_and_software_defined_assembly PISA dimeric 2 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,M,N,O,P,Q,R,WA,XA       
2 1 C,D,S,T,U,V,W,X,YA,ZA       
3 1 E,F,Y,Z,AA,BA,CA,DA,AB,BB   
4 1 G,H,EA,FA,GA,HA,IA,JA,CB,DB 
5 1 I,J,KA,LA,MA,NA,OA,PA,EB,FB 
6 1 K,L,QA,RA,SA,TA,UA,VA,GB,HB 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 1860  ? 
1 MORE         -43   ? 
1 'SSA (A^2)'  13940 ? 
2 'ABSA (A^2)' 1840  ? 
2 MORE         -43   ? 
2 'SSA (A^2)'  14040 ? 
3 'ABSA (A^2)' 1850  ? 
3 MORE         -43   ? 
3 'SSA (A^2)'  13990 ? 
4 'ABSA (A^2)' 1840  ? 
4 MORE         -42   ? 
4 'SSA (A^2)'  14030 ? 
5 'ABSA (A^2)' 1860  ? 
5 MORE         -44   ? 
5 'SSA (A^2)'  13980 ? 
6 'ABSA (A^2)' 1860  ? 
6 MORE         -43   ? 
6 'SSA (A^2)'  14170 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   OD1 ? I ASP 83  ? J ASP 83  ? 1_555 ZN ? LA ZN  . ? J ZN  300 ? 1_555 ND1 ? I HIS 63  ? J HIS 63  ? 1_555 100.5 ? 
2   OD1 ? I ASP 83  ? J ASP 83  ? 1_555 ZN ? LA ZN  . ? J ZN  300 ? 1_555 ND1 ? I HIS 71  ? J HIS 71  ? 1_555 97.8  ? 
3   ND1 ? I HIS 63  ? J HIS 63  ? 1_555 ZN ? LA ZN  . ? J ZN  300 ? 1_555 ND1 ? I HIS 71  ? J HIS 71  ? 1_555 105.6 ? 
4   OD1 ? I ASP 83  ? J ASP 83  ? 1_555 ZN ? LA ZN  . ? J ZN  300 ? 1_555 ND1 ? I HIS 80  ? J HIS 80  ? 1_555 116.7 ? 
5   ND1 ? I HIS 63  ? J HIS 63  ? 1_555 ZN ? LA ZN  . ? J ZN  300 ? 1_555 ND1 ? I HIS 80  ? J HIS 80  ? 1_555 112.8 ? 
6   ND1 ? I HIS 71  ? J HIS 71  ? 1_555 ZN ? LA ZN  . ? J ZN  300 ? 1_555 ND1 ? I HIS 80  ? J HIS 80  ? 1_555 120.6 ? 
7   OD1 ? A ASP 83  ? A ASP 83  ? 1_555 ZN ? N  ZN  . ? A ZN  300 ? 1_555 ND1 ? A HIS 63  ? A HIS 63  ? 1_555 105.9 ? 
8   OD1 ? A ASP 83  ? A ASP 83  ? 1_555 ZN ? N  ZN  . ? A ZN  300 ? 1_555 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 97.2  ? 
9   ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? N  ZN  . ? A ZN  300 ? 1_555 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 102.7 ? 
10  OD1 ? A ASP 83  ? A ASP 83  ? 1_555 ZN ? N  ZN  . ? A ZN  300 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 117.0 ? 
11  ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? N  ZN  . ? A ZN  300 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 108.5 ? 
12  ND1 ? A HIS 71  ? A HIS 71  ? 1_555 ZN ? N  ZN  . ? A ZN  300 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 123.5 ? 
13  OD1 ? C ASP 83  ? D ASP 83  ? 1_555 ZN ? T  ZN  . ? D ZN  300 ? 1_555 ND1 ? C HIS 63  ? D HIS 63  ? 1_555 104.3 ? 
14  OD1 ? C ASP 83  ? D ASP 83  ? 1_555 ZN ? T  ZN  . ? D ZN  300 ? 1_555 ND1 ? C HIS 80  ? D HIS 80  ? 1_555 112.6 ? 
15  ND1 ? C HIS 63  ? D HIS 63  ? 1_555 ZN ? T  ZN  . ? D ZN  300 ? 1_555 ND1 ? C HIS 80  ? D HIS 80  ? 1_555 114.0 ? 
16  OD1 ? C ASP 83  ? D ASP 83  ? 1_555 ZN ? T  ZN  . ? D ZN  300 ? 1_555 ND1 ? C HIS 71  ? D HIS 71  ? 1_555 100.6 ? 
17  ND1 ? C HIS 63  ? D HIS 63  ? 1_555 ZN ? T  ZN  . ? D ZN  300 ? 1_555 ND1 ? C HIS 71  ? D HIS 71  ? 1_555 105.2 ? 
18  ND1 ? C HIS 80  ? D HIS 80  ? 1_555 ZN ? T  ZN  . ? D ZN  300 ? 1_555 ND1 ? C HIS 71  ? D HIS 71  ? 1_555 118.4 ? 
19  OD1 ? G ASP 83  ? H ASP 83  ? 1_555 ZN ? FA ZN  . ? H ZN  300 ? 1_555 ND1 ? G HIS 80  ? H HIS 80  ? 1_555 113.1 ? 
20  OD1 ? G ASP 83  ? H ASP 83  ? 1_555 ZN ? FA ZN  . ? H ZN  300 ? 1_555 ND1 ? G HIS 63  ? H HIS 63  ? 1_555 102.9 ? 
21  ND1 ? G HIS 80  ? H HIS 80  ? 1_555 ZN ? FA ZN  . ? H ZN  300 ? 1_555 ND1 ? G HIS 63  ? H HIS 63  ? 1_555 112.9 ? 
22  OD1 ? G ASP 83  ? H ASP 83  ? 1_555 ZN ? FA ZN  . ? H ZN  300 ? 1_555 ND1 ? G HIS 71  ? H HIS 71  ? 1_555 99.4  ? 
23  ND1 ? G HIS 80  ? H HIS 80  ? 1_555 ZN ? FA ZN  . ? H ZN  300 ? 1_555 ND1 ? G HIS 71  ? H HIS 71  ? 1_555 120.9 ? 
24  ND1 ? G HIS 63  ? H HIS 63  ? 1_555 ZN ? FA ZN  . ? H ZN  300 ? 1_555 ND1 ? G HIS 71  ? H HIS 71  ? 1_555 105.4 ? 
25  OD1 ? K ASP 83  ? L ASP 83  ? 1_555 ZN ? RA ZN  . ? L ZN  300 ? 1_555 ND1 ? K HIS 63  ? L HIS 63  ? 1_555 101.6 ? 
26  OD1 ? K ASP 83  ? L ASP 83  ? 1_555 ZN ? RA ZN  . ? L ZN  300 ? 1_555 ND1 ? K HIS 80  ? L HIS 80  ? 1_555 114.6 ? 
27  ND1 ? K HIS 63  ? L HIS 63  ? 1_555 ZN ? RA ZN  . ? L ZN  300 ? 1_555 ND1 ? K HIS 80  ? L HIS 80  ? 1_555 112.2 ? 
28  OD1 ? K ASP 83  ? L ASP 83  ? 1_555 ZN ? RA ZN  . ? L ZN  300 ? 1_555 ND1 ? K HIS 71  ? L HIS 71  ? 1_555 98.6  ? 
29  ND1 ? K HIS 63  ? L HIS 63  ? 1_555 ZN ? RA ZN  . ? L ZN  300 ? 1_555 ND1 ? K HIS 71  ? L HIS 71  ? 1_555 106.2 ? 
30  ND1 ? K HIS 80  ? L HIS 80  ? 1_555 ZN ? RA ZN  . ? L ZN  300 ? 1_555 ND1 ? K HIS 71  ? L HIS 71  ? 1_555 121.2 ? 
31  OD1 ? H ASP 83  ? I ASP 83  ? 1_555 ZN ? IA ZN  . ? I ZN  300 ? 1_555 ND1 ? H HIS 71  ? I HIS 71  ? 1_555 87.0  ? 
32  OD1 ? H ASP 83  ? I ASP 83  ? 1_555 ZN ? IA ZN  . ? I ZN  300 ? 1_555 ND1 ? H HIS 80  ? I HIS 80  ? 1_555 126.3 ? 
33  ND1 ? H HIS 71  ? I HIS 71  ? 1_555 ZN ? IA ZN  . ? I ZN  300 ? 1_555 ND1 ? H HIS 80  ? I HIS 80  ? 1_555 121.7 ? 
34  OD1 ? H ASP 83  ? I ASP 83  ? 1_555 ZN ? IA ZN  . ? I ZN  300 ? 1_555 ND1 ? H HIS 63  ? I HIS 63  ? 1_555 82.2  ? 
35  ND1 ? H HIS 71  ? I HIS 71  ? 1_555 ZN ? IA ZN  . ? I ZN  300 ? 1_555 ND1 ? H HIS 63  ? I HIS 63  ? 1_555 103.0 ? 
36  ND1 ? H HIS 80  ? I HIS 80  ? 1_555 ZN ? IA ZN  . ? I ZN  300 ? 1_555 ND1 ? H HIS 63  ? I HIS 63  ? 1_555 125.3 ? 
37  OD1 ? J ASP 83  ? K ASP 83  ? 1_555 ZN ? OA ZN  . ? K ZN  300 ? 1_555 ND1 ? J HIS 80  ? K HIS 80  ? 1_555 113.4 ? 
38  OD1 ? J ASP 83  ? K ASP 83  ? 1_555 ZN ? OA ZN  . ? K ZN  300 ? 1_555 ND1 ? J HIS 71  ? K HIS 71  ? 1_555 94.5  ? 
39  ND1 ? J HIS 80  ? K HIS 80  ? 1_555 ZN ? OA ZN  . ? K ZN  300 ? 1_555 ND1 ? J HIS 71  ? K HIS 71  ? 1_555 117.9 ? 
40  OD1 ? J ASP 83  ? K ASP 83  ? 1_555 ZN ? OA ZN  . ? K ZN  300 ? 1_555 ND1 ? J HIS 63  ? K HIS 63  ? 1_555 102.4 ? 
41  ND1 ? J HIS 80  ? K HIS 80  ? 1_555 ZN ? OA ZN  . ? K ZN  300 ? 1_555 ND1 ? J HIS 63  ? K HIS 63  ? 1_555 122.1 ? 
42  ND1 ? J HIS 71  ? K HIS 71  ? 1_555 ZN ? OA ZN  . ? K ZN  300 ? 1_555 ND1 ? J HIS 63  ? K HIS 63  ? 1_555 102.0 ? 
43  OD1 ? B ASP 83  ? B ASP 83  ? 1_555 ZN ? Q  ZN  . ? B ZN  300 ? 1_555 ND1 ? B HIS 63  ? B HIS 63  ? 1_555 102.9 ? 
44  OD1 ? B ASP 83  ? B ASP 83  ? 1_555 ZN ? Q  ZN  . ? B ZN  300 ? 1_555 ND1 ? B HIS 80  ? B HIS 80  ? 1_555 114.9 ? 
45  ND1 ? B HIS 63  ? B HIS 63  ? 1_555 ZN ? Q  ZN  . ? B ZN  300 ? 1_555 ND1 ? B HIS 80  ? B HIS 80  ? 1_555 113.4 ? 
46  OD1 ? B ASP 83  ? B ASP 83  ? 1_555 ZN ? Q  ZN  . ? B ZN  300 ? 1_555 ND1 ? B HIS 71  ? B HIS 71  ? 1_555 97.8  ? 
47  ND1 ? B HIS 63  ? B HIS 63  ? 1_555 ZN ? Q  ZN  . ? B ZN  300 ? 1_555 ND1 ? B HIS 71  ? B HIS 71  ? 1_555 104.7 ? 
48  ND1 ? B HIS 80  ? B HIS 80  ? 1_555 ZN ? Q  ZN  . ? B ZN  300 ? 1_555 ND1 ? B HIS 71  ? B HIS 71  ? 1_555 120.7 ? 
49  NE2 ? E HIS 48  ? F HIS 48  ? 1_555 CU ? Y  CU1 . ? F CU1 200 ? 1_555 ND1 ? E HIS 46  ? F HIS 46  ? 1_555 134.6 ? 
50  NE2 ? E HIS 48  ? F HIS 48  ? 1_555 CU ? Y  CU1 . ? F CU1 200 ? 1_555 NE2 ? E HIS 120 ? F HIS 120 ? 1_555 121.1 ? 
51  ND1 ? E HIS 46  ? F HIS 46  ? 1_555 CU ? Y  CU1 . ? F CU1 200 ? 1_555 NE2 ? E HIS 120 ? F HIS 120 ? 1_555 104.1 ? 
52  OD1 ? D ASP 83  ? E ASP 83  ? 1_555 ZN ? W  ZN  . ? E ZN  300 ? 1_555 ND1 ? D HIS 63  ? E HIS 63  ? 1_555 101.6 ? 
53  OD1 ? D ASP 83  ? E ASP 83  ? 1_555 ZN ? W  ZN  . ? E ZN  300 ? 1_555 ND1 ? D HIS 80  ? E HIS 80  ? 1_555 112.8 ? 
54  ND1 ? D HIS 63  ? E HIS 63  ? 1_555 ZN ? W  ZN  . ? E ZN  300 ? 1_555 ND1 ? D HIS 80  ? E HIS 80  ? 1_555 112.7 ? 
55  OD1 ? D ASP 83  ? E ASP 83  ? 1_555 ZN ? W  ZN  . ? E ZN  300 ? 1_555 ND1 ? D HIS 71  ? E HIS 71  ? 1_555 100.6 ? 
56  ND1 ? D HIS 63  ? E HIS 63  ? 1_555 ZN ? W  ZN  . ? E ZN  300 ? 1_555 ND1 ? D HIS 71  ? E HIS 71  ? 1_555 105.6 ? 
57  ND1 ? D HIS 80  ? E HIS 80  ? 1_555 ZN ? W  ZN  . ? E ZN  300 ? 1_555 ND1 ? D HIS 71  ? E HIS 71  ? 1_555 121.3 ? 
58  NE2 ? C HIS 120 ? D HIS 120 ? 1_555 CU ? S  CU1 . ? D CU1 200 ? 1_555 NE2 ? C HIS 48  ? D HIS 48  ? 1_555 122.0 ? 
59  NE2 ? C HIS 120 ? D HIS 120 ? 1_555 CU ? S  CU1 . ? D CU1 200 ? 1_555 ND1 ? C HIS 46  ? D HIS 46  ? 1_555 98.8  ? 
60  NE2 ? C HIS 48  ? D HIS 48  ? 1_555 CU ? S  CU1 . ? D CU1 200 ? 1_555 ND1 ? C HIS 46  ? D HIS 46  ? 1_555 139.2 ? 
61  NE2 ? B HIS 48  ? B HIS 48  ? 1_555 CU ? P  CU1 . ? B CU1 200 ? 1_555 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 117.4 ? 
62  NE2 ? B HIS 48  ? B HIS 48  ? 1_555 CU ? P  CU1 . ? B CU1 200 ? 1_555 ND1 ? B HIS 46  ? B HIS 46  ? 1_555 141.6 ? 
63  NE2 ? B HIS 120 ? B HIS 120 ? 1_555 CU ? P  CU1 . ? B CU1 200 ? 1_555 ND1 ? B HIS 46  ? B HIS 46  ? 1_555 99.9  ? 
64  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 CU ? M  CU1 . ? A CU1 200 ? 1_555 ND1 ? A HIS 46  ? A HIS 46  ? 1_555 140.7 ? 
65  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 CU ? M  CU1 . ? A CU1 200 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 118.8 ? 
66  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 CU ? M  CU1 . ? A CU1 200 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 100.2 ? 
67  OD1 ? F ASP 83  ? G ASP 83  ? 1_555 ZN ? CA ZN  . ? G ZN  300 ? 1_555 ND1 ? F HIS 63  ? G HIS 63  ? 1_555 105.5 ? 
68  OD1 ? F ASP 83  ? G ASP 83  ? 1_555 ZN ? CA ZN  . ? G ZN  300 ? 1_555 ND1 ? F HIS 80  ? G HIS 80  ? 1_555 111.2 ? 
69  ND1 ? F HIS 63  ? G HIS 63  ? 1_555 ZN ? CA ZN  . ? G ZN  300 ? 1_555 ND1 ? F HIS 80  ? G HIS 80  ? 1_555 122.1 ? 
70  OD1 ? F ASP 83  ? G ASP 83  ? 1_555 ZN ? CA ZN  . ? G ZN  300 ? 1_555 ND1 ? F HIS 71  ? G HIS 71  ? 1_555 99.3  ? 
71  ND1 ? F HIS 63  ? G HIS 63  ? 1_555 ZN ? CA ZN  . ? G ZN  300 ? 1_555 ND1 ? F HIS 71  ? G HIS 71  ? 1_555 104.0 ? 
72  ND1 ? F HIS 80  ? G HIS 80  ? 1_555 ZN ? CA ZN  . ? G ZN  300 ? 1_555 ND1 ? F HIS 71  ? G HIS 71  ? 1_555 112.1 ? 
73  ND1 ? F HIS 46  ? G HIS 46  ? 1_555 CU ? BA CU1 . ? G CU1 200 ? 1_555 NE2 ? F HIS 120 ? G HIS 120 ? 1_555 101.2 ? 
74  ND1 ? F HIS 46  ? G HIS 46  ? 1_555 CU ? BA CU1 . ? G CU1 200 ? 1_555 NE2 ? F HIS 48  ? G HIS 48  ? 1_555 143.9 ? 
75  NE2 ? F HIS 120 ? G HIS 120 ? 1_555 CU ? BA CU1 . ? G CU1 200 ? 1_555 NE2 ? F HIS 48  ? G HIS 48  ? 1_555 114.6 ? 
76  NE2 ? D HIS 48  ? E HIS 48  ? 1_555 CU ? V  CU1 . ? E CU1 200 ? 1_555 ND1 ? D HIS 46  ? E HIS 46  ? 1_555 139.4 ? 
77  NE2 ? D HIS 48  ? E HIS 48  ? 1_555 CU ? V  CU1 . ? E CU1 200 ? 1_555 NE2 ? D HIS 120 ? E HIS 120 ? 1_555 119.3 ? 
78  ND1 ? D HIS 46  ? E HIS 46  ? 1_555 CU ? V  CU1 . ? E CU1 200 ? 1_555 NE2 ? D HIS 120 ? E HIS 120 ? 1_555 100.9 ? 
79  NE2 ? I HIS 48  ? J HIS 48  ? 1_555 CU ? KA CU1 . ? J CU1 200 ? 1_555 NE2 ? I HIS 120 ? J HIS 120 ? 1_555 118.2 ? 
80  NE2 ? I HIS 48  ? J HIS 48  ? 1_555 CU ? KA CU1 . ? J CU1 200 ? 1_555 ND1 ? I HIS 46  ? J HIS 46  ? 1_555 143.4 ? 
81  NE2 ? I HIS 120 ? J HIS 120 ? 1_555 CU ? KA CU1 . ? J CU1 200 ? 1_555 ND1 ? I HIS 46  ? J HIS 46  ? 1_555 98.0  ? 
82  OD1 ? E ASP 83  ? F ASP 83  ? 1_555 ZN ? Z  ZN  . ? F ZN  300 ? 1_555 ND1 ? E HIS 80  ? F HIS 80  ? 1_555 105.4 ? 
83  OD1 ? E ASP 83  ? F ASP 83  ? 1_555 ZN ? Z  ZN  . ? F ZN  300 ? 1_555 ND1 ? E HIS 63  ? F HIS 63  ? 1_555 101.2 ? 
84  ND1 ? E HIS 80  ? F HIS 80  ? 1_555 ZN ? Z  ZN  . ? F ZN  300 ? 1_555 ND1 ? E HIS 63  ? F HIS 63  ? 1_555 114.2 ? 
85  OD1 ? E ASP 83  ? F ASP 83  ? 1_555 ZN ? Z  ZN  . ? F ZN  300 ? 1_555 ND1 ? E HIS 71  ? F HIS 71  ? 1_555 97.2  ? 
86  ND1 ? E HIS 80  ? F HIS 80  ? 1_555 ZN ? Z  ZN  . ? F ZN  300 ? 1_555 ND1 ? E HIS 71  ? F HIS 71  ? 1_555 128.5 ? 
87  ND1 ? E HIS 63  ? F HIS 63  ? 1_555 ZN ? Z  ZN  . ? F ZN  300 ? 1_555 ND1 ? E HIS 71  ? F HIS 71  ? 1_555 105.5 ? 
88  NE2 ? G HIS 48  ? H HIS 48  ? 1_555 CU ? EA CU1 . ? H CU1 200 ? 1_555 NE2 ? G HIS 120 ? H HIS 120 ? 1_555 111.4 ? 
89  NE2 ? G HIS 48  ? H HIS 48  ? 1_555 CU ? EA CU1 . ? H CU1 200 ? 1_555 ND1 ? G HIS 46  ? H HIS 46  ? 1_555 144.1 ? 
90  NE2 ? G HIS 120 ? H HIS 120 ? 1_555 CU ? EA CU1 . ? H CU1 200 ? 1_555 ND1 ? G HIS 46  ? H HIS 46  ? 1_555 103.4 ? 
91  NE2 ? K HIS 48  ? L HIS 48  ? 1_555 CU ? QA CU1 . ? L CU1 200 ? 1_555 NE2 ? K HIS 120 ? L HIS 120 ? 1_555 115.4 ? 
92  NE2 ? K HIS 48  ? L HIS 48  ? 1_555 CU ? QA CU1 . ? L CU1 200 ? 1_555 ND1 ? K HIS 46  ? L HIS 46  ? 1_555 141.3 ? 
93  NE2 ? K HIS 120 ? L HIS 120 ? 1_555 CU ? QA CU1 . ? L CU1 200 ? 1_555 ND1 ? K HIS 46  ? L HIS 46  ? 1_555 102.4 ? 
94  NE2 ? H HIS 48  ? I HIS 48  ? 1_555 CU ? HA CU1 . ? I CU1 200 ? 1_555 NE2 ? H HIS 120 ? I HIS 120 ? 1_555 106.8 ? 
95  NE2 ? H HIS 48  ? I HIS 48  ? 1_555 CU ? HA CU1 . ? I CU1 200 ? 1_555 ND1 ? H HIS 46  ? I HIS 46  ? 1_555 151.0 ? 
96  NE2 ? H HIS 120 ? I HIS 120 ? 1_555 CU ? HA CU1 . ? I CU1 200 ? 1_555 ND1 ? H HIS 46  ? I HIS 46  ? 1_555 101.2 ? 
97  ND1 ? L HIS 80  ? M HIS 80  ? 1_555 ZN ? UA ZN  . ? M ZN  300 ? 1_555 OD1 ? L ASP 83  ? M ASP 83  ? 1_555 143.5 ? 
98  ND1 ? L HIS 80  ? M HIS 80  ? 1_555 ZN ? UA ZN  . ? M ZN  300 ? 1_555 ND1 ? L HIS 63  ? M HIS 63  ? 1_555 119.9 ? 
99  OD1 ? L ASP 83  ? M ASP 83  ? 1_555 ZN ? UA ZN  . ? M ZN  300 ? 1_555 ND1 ? L HIS 63  ? M HIS 63  ? 1_555 86.2  ? 
100 ND1 ? L HIS 80  ? M HIS 80  ? 1_555 ZN ? UA ZN  . ? M ZN  300 ? 1_555 ND1 ? L HIS 71  ? M HIS 71  ? 1_555 107.4 ? 
101 OD1 ? L ASP 83  ? M ASP 83  ? 1_555 ZN ? UA ZN  . ? M ZN  300 ? 1_555 ND1 ? L HIS 71  ? M HIS 71  ? 1_555 92.4  ? 
102 ND1 ? L HIS 63  ? M HIS 63  ? 1_555 ZN ? UA ZN  . ? M ZN  300 ? 1_555 ND1 ? L HIS 71  ? M HIS 71  ? 1_555 97.3  ? 
103 ND1 ? L HIS 80  ? M HIS 80  ? 1_555 ZN ? UA ZN  . ? M ZN  300 ? 1_555 OD2 ? L ASP 83  ? M ASP 83  ? 1_555 93.8  ? 
104 OD1 ? L ASP 83  ? M ASP 83  ? 1_555 ZN ? UA ZN  . ? M ZN  300 ? 1_555 OD2 ? L ASP 83  ? M ASP 83  ? 1_555 53.0  ? 
105 ND1 ? L HIS 63  ? M HIS 63  ? 1_555 ZN ? UA ZN  . ? M ZN  300 ? 1_555 OD2 ? L ASP 83  ? M ASP 83  ? 1_555 137.5 ? 
106 ND1 ? L HIS 71  ? M HIS 71  ? 1_555 ZN ? UA ZN  . ? M ZN  300 ? 1_555 OD2 ? L ASP 83  ? M ASP 83  ? 1_555 96.1  ? 
107 NE2 ? J HIS 48  ? K HIS 48  ? 1_555 CU ? NA CU1 . ? K CU1 200 ? 1_555 ND1 ? J HIS 46  ? K HIS 46  ? 1_555 147.7 ? 
108 NE2 ? J HIS 48  ? K HIS 48  ? 1_555 CU ? NA CU1 . ? K CU1 200 ? 1_555 NE2 ? J HIS 120 ? K HIS 120 ? 1_555 112.4 ? 
109 ND1 ? J HIS 46  ? K HIS 46  ? 1_555 CU ? NA CU1 . ? K CU1 200 ? 1_555 NE2 ? J HIS 120 ? K HIS 120 ? 1_555 99.8  ? 
110 NE2 ? L HIS 48  ? M HIS 48  ? 1_555 CU ? TA CU1 . ? M CU1 200 ? 1_555 ND1 ? L HIS 46  ? M HIS 46  ? 1_555 156.4 ? 
111 NE2 ? L HIS 48  ? M HIS 48  ? 1_555 CU ? TA CU1 . ? M CU1 200 ? 1_555 NE2 ? L HIS 120 ? M HIS 120 ? 1_555 109.2 ? 
112 ND1 ? L HIS 46  ? M HIS 46  ? 1_555 CU ? TA CU1 . ? M CU1 200 ? 1_555 NE2 ? L HIS 120 ? M HIS 120 ? 1_555 94.1  ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2012-08-01 
2 'Structure model' 1 1 2013-07-03 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1  ? refined 16.1812 20.6740  -32.8619 0.3014 0.3164 0.3701 -0.0080 0.0060  -0.0380 0.2828 0.3490 0.4956 
-0.0845 0.0051  0.0888  0.0013  0.0358  -0.0586 0.0028  -0.0145 -0.0102 -0.0299 0.0218  0.0132  
'X-RAY DIFFRACTION' 2  ? refined 13.8542 42.1128  -14.8219 0.3232 0.3134 0.3414 0.0008  -0.0074 -0.0186 0.4820 0.3622 0.4409 
-0.0201 -0.1349 0.0414  -0.0050 -0.0123 0.0069  0.0110  0.0003  -0.0306 -0.0119 -0.0361 0.0047  
'X-RAY DIFFRACTION' 3  ? refined 52.7238 22.6185  -30.3196 0.3070 0.3237 0.3556 -0.0017 -0.0022 -0.0206 0.1156 0.7610 0.2549 
0.0248  -0.0726 0.1706  -0.0108 0.0064  -0.0066 0.0012  -0.0125 0.0559  0.0133  -0.0025 0.0233  
'X-RAY DIFFRACTION' 4  ? refined 50.2834 49.1757  -20.9185 0.3165 0.3159 0.3480 -0.0148 0.0036  -0.0160 0.4893 0.4510 0.3796 
-0.1048 -0.2499 -0.0269 0.0226  -0.0148 0.0283  0.0115  -0.0091 -0.0056 -0.0311 0.0187  -0.0136 
'X-RAY DIFFRACTION' 5  ? refined 16.3978 -10.5228 -38.5758 0.3533 0.2847 0.3382 -0.0238 0.0219  -0.0389 0.4980 0.7142 0.3416 
0.0110  0.0237  0.0912  0.0494  0.0335  0.0222  0.1154  -0.0588 0.0727  0.0413  0.0006  0.0094  
'X-RAY DIFFRACTION' 6  ? refined 15.0907 -36.8038 -28.7806 0.4469 0.2555 0.3019 -0.0829 0.0212  -0.0196 0.1582 0.8610 0.4902 
-0.2658 0.1677  0.0384  0.0596  -0.0255 -0.0040 0.0832  -0.0398 0.0805  0.0993  -0.0222 -0.0197 
'X-RAY DIFFRACTION' 7  ? refined 50.1706 -7.9051  -24.7035 0.3672 0.2820 0.3293 -0.0203 -0.0267 0.0211  0.6794 0.6553 0.7429 
0.4046  -0.0825 -0.0828 0.0536  -0.0628 -0.0994 0.0501  -0.0749 -0.0870 0.0861  -0.0016 0.0212  
'X-RAY DIFFRACTION' 8  ? refined 43.2810 -28.2269 -6.2239  0.4648 0.2661 0.2882 -0.0389 -0.0410 0.1115  0.7882 1.4415 1.0061 
0.4729  -0.2815 0.3111  0.0340  -0.1365 -0.1605 0.2284  -0.1164 -0.0739 0.1636  0.0787  0.0824  
'X-RAY DIFFRACTION' 9  ? refined 22.5131 9.2886   -61.9096 0.2990 0.3607 0.3101 0.0396  -0.0209 -0.0364 0.5126 0.8147 0.9467 
0.0941  -0.0995 -0.1754 0.0248  0.0793  -0.0177 -0.0445 -0.0752 0.0888  -0.0205 0.0409  0.0504  
'X-RAY DIFFRACTION' 10 ? refined 29.5590 13.0932  -88.5014 0.3797 0.5032 0.1525 0.0403  -0.0412 0.0109  0.8459 0.8026 1.4788 
-0.0635 -0.0017 0.3576  0.0046  0.2871  -0.0639 -0.1263 -0.0342 0.1184  -0.2376 0.1997  0.0296  
'X-RAY DIFFRACTION' 11 ? refined 57.4377 1.9947   -53.9087 0.3029 0.3898 0.2982 0.0240  -0.0050 -0.0379 1.3603 0.4599 0.4000 
-0.2258 0.0608  0.1105  0.0446  0.3251  -0.0474 0.0711  -0.0820 0.0074  -0.0011 0.0186  0.0374  
'X-RAY DIFFRACTION' 12 ? refined 62.1522 -2.7915  -81.0306 0.1803 1.2178 0.0794 0.1917  -0.0065 -0.2001 1.8230 1.3527 1.1021 
-0.6703 0.1029  -0.9374 0.1926  1.1576  -0.1065 -0.0708 -0.2079 -0.0101 0.0739  0.2449  0.0153  
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1  1  A 1 ? ? A 153 ? ? ? ? 
'X-RAY DIFFRACTION' 2  2  B 1 ? ? B 153 ? ? ? ? 
'X-RAY DIFFRACTION' 3  3  D 1 ? ? D 153 ? ? ? ? 
'X-RAY DIFFRACTION' 4  4  E 1 ? ? E 153 ? ? ? ? 
'X-RAY DIFFRACTION' 5  5  F 1 ? ? F 153 ? ? ? ? 
'X-RAY DIFFRACTION' 6  6  G 1 ? ? G 153 ? ? ? ? 
'X-RAY DIFFRACTION' 7  7  H 1 ? ? H 153 ? ? ? ? 
'X-RAY DIFFRACTION' 8  8  I 1 ? ? I 153 ? ? ? ? 
'X-RAY DIFFRACTION' 9  9  J 1 ? ? J 153 ? ? ? ? 
'X-RAY DIFFRACTION' 10 10 K 1 ? ? K 153 ? ? ? ? 
'X-RAY DIFFRACTION' 11 11 L 1 ? ? L 153 ? ? ? ? 
'X-RAY DIFFRACTION' 12 12 M 1 ? ? M 153 ? ? ? ? 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
HKL-2000 'data collection' .        ? 1 
MOLREP   phasing           .        ? 2 
REFMAC   refinement        5.5.0088 ? 3 
HKL-2000 'data reduction'  .        ? 4 
HKL-2000 'data scaling'    .        ? 5 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O A HOH 164  ? ? O A HOH 1746 ? ? 1.82 
2 1 O E HOH 525  ? ? O E HOH 1704 ? ? 2.02 
3 1 O A HOH 1409 ? ? O A HOH 1675 ? ? 2.18 
4 1 O I HIS 110  ? ? O I HOH 1672 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1  1 ASN A 65 ? ? -143.75 58.73   
2  1 ASN B 65 ? ? -147.82 59.23   
3  1 ALA D 55 ? ? -119.93 53.90   
4  1 ASN D 65 ? ? -150.39 61.69   
5  1 ALA G 55 ? ? -117.73 50.53   
6  1 ASN G 65 ? ? -141.87 57.96   
7  1 ASP I 90 ? ? -75.37  -167.94 
8  1 ASN J 65 ? ? -144.46 57.99   
9  1 ALA K 55 ? ? -119.28 51.53   
10 1 ASN M 65 ? ? -160.83 79.10   
11 1 ARG M 69 ? ? -114.59 -162.24 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   ASN 
_pdbx_validate_peptide_omega.auth_asym_id_1   D 
_pdbx_validate_peptide_omega.auth_seq_id_1    26 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_2   D 
_pdbx_validate_peptide_omega.auth_seq_id_2    27 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -149.27 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'COPPER (I) ION' CU1 
3 'ZINC ION'       ZN  
4 'SULFATE ION'    SO4 
5 water            HOH 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
M  2 CU1 1   200  200  CU1 CU1 A . 
N  3 ZN  1   300  300  ZN  ZN  A . 
O  4 SO4 1   400  400  SO4 SO4 A . 
P  2 CU1 1   200  200  CU1 CU1 B . 
Q  3 ZN  1   300  300  ZN  ZN  B . 
R  4 SO4 1   400  400  SO4 SO4 B . 
S  2 CU1 1   200  200  CU1 CU1 D . 
T  3 ZN  1   300  300  ZN  ZN  D . 
U  4 SO4 1   400  400  SO4 SO4 D . 
V  2 CU1 1   200  200  CU1 CU1 E . 
W  3 ZN  1   300  300  ZN  ZN  E . 
X  4 SO4 1   400  400  SO4 SO4 E . 
Y  2 CU1 1   200  200  CU1 CU1 F . 
Z  3 ZN  1   300  300  ZN  ZN  F . 
AA 4 SO4 1   400  400  SO4 SO4 F . 
BA 2 CU1 1   200  200  CU1 CU1 G . 
CA 3 ZN  1   300  300  ZN  ZN  G . 
DA 4 SO4 1   400  400  SO4 SO4 G . 
EA 2 CU1 1   200  200  CU1 CU1 H . 
FA 3 ZN  1   300  300  ZN  ZN  H . 
GA 4 SO4 1   400  400  SO4 SO4 H . 
HA 2 CU1 1   200  200  CU1 CU1 I . 
IA 3 ZN  1   300  300  ZN  ZN  I . 
JA 4 SO4 1   400  400  SO4 SO4 I . 
KA 2 CU1 1   200  200  CU1 CU1 J . 
LA 3 ZN  1   300  300  ZN  ZN  J . 
MA 4 SO4 1   400  400  SO4 SO4 J . 
NA 2 CU1 1   200  200  CU1 CU1 K . 
OA 3 ZN  1   300  300  ZN  ZN  K . 
PA 4 SO4 1   400  400  SO4 SO4 K . 
QA 2 CU1 1   200  200  CU1 CU1 L . 
RA 3 ZN  1   300  300  ZN  ZN  L . 
SA 4 SO4 1   400  400  SO4 SO4 L . 
TA 2 CU1 1   200  200  CU1 CU1 M . 
UA 3 ZN  1   300  300  ZN  ZN  M . 
VA 4 SO4 1   400  400  SO4 SO4 M . 
WA 5 HOH 1   154  8    HOH HOH A . 
WA 5 HOH 2   155  14   HOH HOH A . 
WA 5 HOH 3   156  15   HOH HOH A . 
WA 5 HOH 4   157  27   HOH HOH A . 
WA 5 HOH 5   158  37   HOH HOH A . 
WA 5 HOH 6   159  38   HOH HOH A . 
WA 5 HOH 7   160  160  HOH HOH A . 
WA 5 HOH 8   161  42   HOH HOH A . 
WA 5 HOH 9   162  43   HOH HOH A . 
WA 5 HOH 10  163  44   HOH HOH A . 
WA 5 HOH 11  164  48   HOH HOH A . 
WA 5 HOH 12  165  59   HOH HOH A . 
WA 5 HOH 13  166  70   HOH HOH A . 
WA 5 HOH 14  167  74   HOH HOH A . 
WA 5 HOH 15  168  75   HOH HOH A . 
WA 5 HOH 16  169  169  HOH HOH A . 
WA 5 HOH 17  170  78   HOH HOH A . 
WA 5 HOH 18  171  80   HOH HOH A . 
WA 5 HOH 19  172  82   HOH HOH A . 
WA 5 HOH 20  173  83   HOH HOH A . 
WA 5 HOH 21  174  174  HOH HOH A . 
WA 5 HOH 22  175  88   HOH HOH A . 
WA 5 HOH 23  176  99   HOH HOH A . 
WA 5 HOH 24  177  177  HOH HOH A . 
WA 5 HOH 25  178  101  HOH HOH A . 
WA 5 HOH 26  179  179  HOH HOH A . 
WA 5 HOH 27  180  108  HOH HOH A . 
WA 5 HOH 28  181  125  HOH HOH A . 
WA 5 HOH 29  182  137  HOH HOH A . 
WA 5 HOH 30  183  144  HOH HOH A . 
WA 5 HOH 31  184  147  HOH HOH A . 
WA 5 HOH 32  185  185  HOH HOH A . 
WA 5 HOH 33  187  187  HOH HOH A . 
WA 5 HOH 34  189  189  HOH HOH A . 
WA 5 HOH 35  206  206  HOH HOH A . 
WA 5 HOH 36  207  207  HOH HOH A . 
WA 5 HOH 37  208  208  HOH HOH A . 
WA 5 HOH 38  216  216  HOH HOH A . 
WA 5 HOH 39  232  232  HOH HOH A . 
WA 5 HOH 40  235  235  HOH HOH A . 
WA 5 HOH 41  247  247  HOH HOH A . 
WA 5 HOH 42  253  253  HOH HOH A . 
WA 5 HOH 43  254  254  HOH HOH A . 
WA 5 HOH 44  264  264  HOH HOH A . 
WA 5 HOH 45  280  280  HOH HOH A . 
WA 5 HOH 46  308  308  HOH HOH A . 
WA 5 HOH 47  309  309  HOH HOH A . 
WA 5 HOH 48  313  313  HOH HOH A . 
WA 5 HOH 49  327  327  HOH HOH A . 
WA 5 HOH 50  328  328  HOH HOH A . 
WA 5 HOH 51  331  331  HOH HOH A . 
WA 5 HOH 52  338  338  HOH HOH A . 
WA 5 HOH 53  341  341  HOH HOH A . 
WA 5 HOH 54  349  349  HOH HOH A . 
WA 5 HOH 55  352  352  HOH HOH A . 
WA 5 HOH 56  353  353  HOH HOH A . 
WA 5 HOH 57  359  359  HOH HOH A . 
WA 5 HOH 58  377  377  HOH HOH A . 
WA 5 HOH 59  392  392  HOH HOH A . 
WA 5 HOH 60  395  395  HOH HOH A . 
WA 5 HOH 61  397  397  HOH HOH A . 
WA 5 HOH 62  399  399  HOH HOH A . 
WA 5 HOH 63  401  401  HOH HOH A . 
WA 5 HOH 64  407  407  HOH HOH A . 
WA 5 HOH 65  409  409  HOH HOH A . 
WA 5 HOH 66  424  424  HOH HOH A . 
WA 5 HOH 67  448  448  HOH HOH A . 
WA 5 HOH 68  449  449  HOH HOH A . 
WA 5 HOH 69  453  453  HOH HOH A . 
WA 5 HOH 70  465  465  HOH HOH A . 
WA 5 HOH 71  473  473  HOH HOH A . 
WA 5 HOH 72  494  494  HOH HOH A . 
WA 5 HOH 73  496  496  HOH HOH A . 
WA 5 HOH 74  503  503  HOH HOH A . 
WA 5 HOH 75  533  533  HOH HOH A . 
WA 5 HOH 76  535  535  HOH HOH A . 
WA 5 HOH 77  549  549  HOH HOH A . 
WA 5 HOH 78  556  556  HOH HOH A . 
WA 5 HOH 79  562  562  HOH HOH A . 
WA 5 HOH 80  568  568  HOH HOH A . 
WA 5 HOH 81  569  569  HOH HOH A . 
WA 5 HOH 82  578  578  HOH HOH A . 
WA 5 HOH 83  580  580  HOH HOH A . 
WA 5 HOH 84  590  590  HOH HOH A . 
WA 5 HOH 85  596  596  HOH HOH A . 
WA 5 HOH 86  626  626  HOH HOH A . 
WA 5 HOH 87  629  629  HOH HOH A . 
WA 5 HOH 88  636  636  HOH HOH A . 
WA 5 HOH 89  644  644  HOH HOH A . 
WA 5 HOH 90  655  655  HOH HOH A . 
WA 5 HOH 91  669  669  HOH HOH A . 
WA 5 HOH 92  722  722  HOH HOH A . 
WA 5 HOH 93  733  733  HOH HOH A . 
WA 5 HOH 94  734  734  HOH HOH A . 
WA 5 HOH 95  744  744  HOH HOH A . 
WA 5 HOH 96  753  753  HOH HOH A . 
WA 5 HOH 97  758  758  HOH HOH A . 
WA 5 HOH 98  760  760  HOH HOH A . 
WA 5 HOH 99  764  764  HOH HOH A . 
WA 5 HOH 100 769  769  HOH HOH A . 
WA 5 HOH 101 771  771  HOH HOH A . 
WA 5 HOH 102 772  772  HOH HOH A . 
WA 5 HOH 103 779  779  HOH HOH A . 
WA 5 HOH 104 780  780  HOH HOH A . 
WA 5 HOH 105 789  789  HOH HOH A . 
WA 5 HOH 106 791  791  HOH HOH A . 
WA 5 HOH 107 793  793  HOH HOH A . 
WA 5 HOH 108 803  803  HOH HOH A . 
WA 5 HOH 109 821  821  HOH HOH A . 
WA 5 HOH 110 823  823  HOH HOH A . 
WA 5 HOH 111 834  834  HOH HOH A . 
WA 5 HOH 112 853  853  HOH HOH A . 
WA 5 HOH 113 867  867  HOH HOH A . 
WA 5 HOH 114 872  872  HOH HOH A . 
WA 5 HOH 115 874  874  HOH HOH A . 
WA 5 HOH 116 893  893  HOH HOH A . 
WA 5 HOH 117 917  917  HOH HOH A . 
WA 5 HOH 118 931  931  HOH HOH A . 
WA 5 HOH 119 945  945  HOH HOH A . 
WA 5 HOH 120 954  954  HOH HOH A . 
WA 5 HOH 121 958  958  HOH HOH A . 
WA 5 HOH 122 986  986  HOH HOH A . 
WA 5 HOH 123 988  988  HOH HOH A . 
WA 5 HOH 124 992  992  HOH HOH A . 
WA 5 HOH 125 995  995  HOH HOH A . 
WA 5 HOH 126 1002 1002 HOH HOH A . 
WA 5 HOH 127 1014 1014 HOH HOH A . 
WA 5 HOH 128 1020 1020 HOH HOH A . 
WA 5 HOH 129 1027 1027 HOH HOH A . 
WA 5 HOH 130 1035 1035 HOH HOH A . 
WA 5 HOH 131 1039 1039 HOH HOH A . 
WA 5 HOH 132 1045 1045 HOH HOH A . 
WA 5 HOH 133 1054 1054 HOH HOH A . 
WA 5 HOH 134 1057 1057 HOH HOH A . 
WA 5 HOH 135 1074 1074 HOH HOH A . 
WA 5 HOH 136 1077 1077 HOH HOH A . 
WA 5 HOH 137 1079 1079 HOH HOH A . 
WA 5 HOH 138 1101 1101 HOH HOH A . 
WA 5 HOH 139 1105 1105 HOH HOH A . 
WA 5 HOH 140 1109 1109 HOH HOH A . 
WA 5 HOH 141 1122 1122 HOH HOH A . 
WA 5 HOH 142 1131 1131 HOH HOH A . 
WA 5 HOH 143 1149 1149 HOH HOH A . 
WA 5 HOH 144 1155 1155 HOH HOH A . 
WA 5 HOH 145 1162 1162 HOH HOH A . 
WA 5 HOH 146 1168 1168 HOH HOH A . 
WA 5 HOH 147 1175 1175 HOH HOH A . 
WA 5 HOH 148 1178 1178 HOH HOH A . 
WA 5 HOH 149 1179 1179 HOH HOH A . 
WA 5 HOH 150 1192 1192 HOH HOH A . 
WA 5 HOH 151 1200 1200 HOH HOH A . 
WA 5 HOH 152 1227 1227 HOH HOH A . 
WA 5 HOH 153 1261 1261 HOH HOH A . 
WA 5 HOH 154 1266 1266 HOH HOH A . 
WA 5 HOH 155 1267 1267 HOH HOH A . 
WA 5 HOH 156 1281 1281 HOH HOH A . 
WA 5 HOH 157 1292 1292 HOH HOH A . 
WA 5 HOH 158 1297 1297 HOH HOH A . 
WA 5 HOH 159 1308 1308 HOH HOH A . 
WA 5 HOH 160 1314 1314 HOH HOH A . 
WA 5 HOH 161 1315 1315 HOH HOH A . 
WA 5 HOH 162 1334 1334 HOH HOH A . 
WA 5 HOH 163 1363 1363 HOH HOH A . 
WA 5 HOH 164 1368 1368 HOH HOH A . 
WA 5 HOH 165 1370 1370 HOH HOH A . 
WA 5 HOH 166 1380 1380 HOH HOH A . 
WA 5 HOH 167 1387 1387 HOH HOH A . 
WA 5 HOH 168 1402 1402 HOH HOH A . 
WA 5 HOH 169 1409 1409 HOH HOH A . 
WA 5 HOH 170 1411 1411 HOH HOH A . 
WA 5 HOH 171 1434 1434 HOH HOH A . 
WA 5 HOH 172 1436 1436 HOH HOH A . 
WA 5 HOH 173 1448 1448 HOH HOH A . 
WA 5 HOH 174 1454 1454 HOH HOH A . 
WA 5 HOH 175 1457 1457 HOH HOH A . 
WA 5 HOH 176 1464 1464 HOH HOH A . 
WA 5 HOH 177 1471 1471 HOH HOH A . 
WA 5 HOH 178 1501 1501 HOH HOH A . 
WA 5 HOH 179 1510 1510 HOH HOH A . 
WA 5 HOH 180 1512 1512 HOH HOH A . 
WA 5 HOH 181 1543 1543 HOH HOH A . 
WA 5 HOH 182 1557 1557 HOH HOH A . 
WA 5 HOH 183 1564 1564 HOH HOH A . 
WA 5 HOH 184 1571 1571 HOH HOH A . 
WA 5 HOH 185 1573 1573 HOH HOH A . 
WA 5 HOH 186 1579 1579 HOH HOH A . 
WA 5 HOH 187 1581 1581 HOH HOH A . 
WA 5 HOH 188 1582 1582 HOH HOH A . 
WA 5 HOH 189 1584 1584 HOH HOH A . 
WA 5 HOH 190 1629 1629 HOH HOH A . 
WA 5 HOH 191 1640 1640 HOH HOH A . 
WA 5 HOH 192 1653 1653 HOH HOH A . 
WA 5 HOH 193 1654 1654 HOH HOH A . 
WA 5 HOH 194 1655 1655 HOH HOH A . 
WA 5 HOH 195 1656 1656 HOH HOH A . 
WA 5 HOH 196 1664 1664 HOH HOH A . 
WA 5 HOH 197 1675 1675 HOH HOH A . 
WA 5 HOH 198 1676 1676 HOH HOH A . 
WA 5 HOH 199 1694 1694 HOH HOH A . 
WA 5 HOH 200 1703 1703 HOH HOH A . 
WA 5 HOH 201 1711 1711 HOH HOH A . 
WA 5 HOH 202 1716 1716 HOH HOH A . 
WA 5 HOH 203 1720 1720 HOH HOH A . 
WA 5 HOH 204 1728 1728 HOH HOH A . 
WA 5 HOH 205 1729 1729 HOH HOH A . 
WA 5 HOH 206 1730 1730 HOH HOH A . 
WA 5 HOH 207 1731 1731 HOH HOH A . 
WA 5 HOH 208 1732 1732 HOH HOH A . 
WA 5 HOH 209 1746 1746 HOH HOH A . 
XA 5 HOH 1   154  154  HOH HOH B . 
XA 5 HOH 2   155  4    HOH HOH B . 
XA 5 HOH 3   156  6    HOH HOH B . 
XA 5 HOH 4   157  7    HOH HOH B . 
XA 5 HOH 5   158  10   HOH HOH B . 
XA 5 HOH 6   159  12   HOH HOH B . 
XA 5 HOH 7   160  19   HOH HOH B . 
XA 5 HOH 8   161  23   HOH HOH B . 
XA 5 HOH 9   162  30   HOH HOH B . 
XA 5 HOH 10  163  32   HOH HOH B . 
XA 5 HOH 11  164  34   HOH HOH B . 
XA 5 HOH 12  165  165  HOH HOH B . 
XA 5 HOH 13  166  36   HOH HOH B . 
XA 5 HOH 14  167  40   HOH HOH B . 
XA 5 HOH 15  168  50   HOH HOH B . 
XA 5 HOH 16  169  55   HOH HOH B . 
XA 5 HOH 17  170  65   HOH HOH B . 
XA 5 HOH 18  171  67   HOH HOH B . 
XA 5 HOH 19  172  69   HOH HOH B . 
XA 5 HOH 20  173  102  HOH HOH B . 
XA 5 HOH 21  174  105  HOH HOH B . 
XA 5 HOH 22  175  175  HOH HOH B . 
XA 5 HOH 23  176  116  HOH HOH B . 
XA 5 HOH 24  177  120  HOH HOH B . 
XA 5 HOH 25  178  121  HOH HOH B . 
XA 5 HOH 26  179  124  HOH HOH B . 
XA 5 HOH 27  180  129  HOH HOH B . 
XA 5 HOH 28  181  181  HOH HOH B . 
XA 5 HOH 29  182  135  HOH HOH B . 
XA 5 HOH 30  183  138  HOH HOH B . 
XA 5 HOH 31  184  184  HOH HOH B . 
XA 5 HOH 32  185  141  HOH HOH B . 
XA 5 HOH 33  186  143  HOH HOH B . 
XA 5 HOH 34  187  146  HOH HOH B . 
XA 5 HOH 35  188  188  HOH HOH B . 
XA 5 HOH 36  189  149  HOH HOH B . 
XA 5 HOH 37  195  195  HOH HOH B . 
XA 5 HOH 38  197  197  HOH HOH B . 
XA 5 HOH 39  203  203  HOH HOH B . 
XA 5 HOH 40  205  205  HOH HOH B . 
XA 5 HOH 41  211  211  HOH HOH B . 
XA 5 HOH 42  213  213  HOH HOH B . 
XA 5 HOH 43  230  230  HOH HOH B . 
XA 5 HOH 44  231  231  HOH HOH B . 
XA 5 HOH 45  241  241  HOH HOH B . 
XA 5 HOH 46  242  242  HOH HOH B . 
XA 5 HOH 47  251  251  HOH HOH B . 
XA 5 HOH 48  259  259  HOH HOH B . 
XA 5 HOH 49  265  265  HOH HOH B . 
XA 5 HOH 50  273  273  HOH HOH B . 
XA 5 HOH 51  276  276  HOH HOH B . 
XA 5 HOH 52  278  278  HOH HOH B . 
XA 5 HOH 53  282  282  HOH HOH B . 
XA 5 HOH 54  284  284  HOH HOH B . 
XA 5 HOH 55  286  286  HOH HOH B . 
XA 5 HOH 56  290  290  HOH HOH B . 
XA 5 HOH 57  294  294  HOH HOH B . 
XA 5 HOH 58  299  299  HOH HOH B . 
XA 5 HOH 59  303  303  HOH HOH B . 
XA 5 HOH 60  319  319  HOH HOH B . 
XA 5 HOH 61  323  323  HOH HOH B . 
XA 5 HOH 62  325  325  HOH HOH B . 
XA 5 HOH 63  369  369  HOH HOH B . 
XA 5 HOH 64  370  370  HOH HOH B . 
XA 5 HOH 65  376  376  HOH HOH B . 
XA 5 HOH 66  380  380  HOH HOH B . 
XA 5 HOH 67  403  403  HOH HOH B . 
XA 5 HOH 68  410  410  HOH HOH B . 
XA 5 HOH 69  416  416  HOH HOH B . 
XA 5 HOH 70  421  421  HOH HOH B . 
XA 5 HOH 71  425  425  HOH HOH B . 
XA 5 HOH 72  429  429  HOH HOH B . 
XA 5 HOH 73  433  433  HOH HOH B . 
XA 5 HOH 74  441  441  HOH HOH B . 
XA 5 HOH 75  458  458  HOH HOH B . 
XA 5 HOH 76  472  472  HOH HOH B . 
XA 5 HOH 77  474  474  HOH HOH B . 
XA 5 HOH 78  478  478  HOH HOH B . 
XA 5 HOH 79  482  482  HOH HOH B . 
XA 5 HOH 80  483  483  HOH HOH B . 
XA 5 HOH 81  489  489  HOH HOH B . 
XA 5 HOH 82  493  493  HOH HOH B . 
XA 5 HOH 83  501  501  HOH HOH B . 
XA 5 HOH 84  507  507  HOH HOH B . 
XA 5 HOH 85  517  517  HOH HOH B . 
XA 5 HOH 86  518  518  HOH HOH B . 
XA 5 HOH 87  530  530  HOH HOH B . 
XA 5 HOH 88  541  541  HOH HOH B . 
XA 5 HOH 89  544  544  HOH HOH B . 
XA 5 HOH 90  548  548  HOH HOH B . 
XA 5 HOH 91  555  555  HOH HOH B . 
XA 5 HOH 92  561  561  HOH HOH B . 
XA 5 HOH 93  566  566  HOH HOH B . 
XA 5 HOH 94  597  597  HOH HOH B . 
XA 5 HOH 95  610  610  HOH HOH B . 
XA 5 HOH 96  612  612  HOH HOH B . 
XA 5 HOH 97  616  616  HOH HOH B . 
XA 5 HOH 98  630  630  HOH HOH B . 
XA 5 HOH 99  649  649  HOH HOH B . 
XA 5 HOH 100 651  651  HOH HOH B . 
XA 5 HOH 101 656  656  HOH HOH B . 
XA 5 HOH 102 663  663  HOH HOH B . 
XA 5 HOH 103 694  694  HOH HOH B . 
XA 5 HOH 104 699  699  HOH HOH B . 
XA 5 HOH 105 701  701  HOH HOH B . 
XA 5 HOH 106 702  702  HOH HOH B . 
XA 5 HOH 107 711  711  HOH HOH B . 
XA 5 HOH 108 712  712  HOH HOH B . 
XA 5 HOH 109 717  717  HOH HOH B . 
XA 5 HOH 110 718  718  HOH HOH B . 
XA 5 HOH 111 723  723  HOH HOH B . 
XA 5 HOH 112 729  729  HOH HOH B . 
XA 5 HOH 113 740  740  HOH HOH B . 
XA 5 HOH 114 754  754  HOH HOH B . 
XA 5 HOH 115 776  776  HOH HOH B . 
XA 5 HOH 116 792  792  HOH HOH B . 
XA 5 HOH 117 820  820  HOH HOH B . 
XA 5 HOH 118 830  830  HOH HOH B . 
XA 5 HOH 119 832  832  HOH HOH B . 
XA 5 HOH 120 838  838  HOH HOH B . 
XA 5 HOH 121 842  842  HOH HOH B . 
XA 5 HOH 122 866  866  HOH HOH B . 
XA 5 HOH 123 869  869  HOH HOH B . 
XA 5 HOH 124 896  896  HOH HOH B . 
XA 5 HOH 125 903  903  HOH HOH B . 
XA 5 HOH 126 913  913  HOH HOH B . 
XA 5 HOH 127 924  924  HOH HOH B . 
XA 5 HOH 128 935  935  HOH HOH B . 
XA 5 HOH 129 965  965  HOH HOH B . 
XA 5 HOH 130 967  967  HOH HOH B . 
XA 5 HOH 131 991  991  HOH HOH B . 
XA 5 HOH 132 994  994  HOH HOH B . 
XA 5 HOH 133 997  997  HOH HOH B . 
XA 5 HOH 134 1003 1003 HOH HOH B . 
XA 5 HOH 135 1017 1017 HOH HOH B . 
XA 5 HOH 136 1043 1043 HOH HOH B . 
XA 5 HOH 137 1049 1049 HOH HOH B . 
XA 5 HOH 138 1055 1055 HOH HOH B . 
XA 5 HOH 139 1063 1063 HOH HOH B . 
XA 5 HOH 140 1073 1073 HOH HOH B . 
XA 5 HOH 141 1075 1075 HOH HOH B . 
XA 5 HOH 142 1078 1078 HOH HOH B . 
XA 5 HOH 143 1084 1084 HOH HOH B . 
XA 5 HOH 144 1093 1093 HOH HOH B . 
XA 5 HOH 145 1113 1113 HOH HOH B . 
XA 5 HOH 146 1129 1129 HOH HOH B . 
XA 5 HOH 147 1137 1137 HOH HOH B . 
XA 5 HOH 148 1139 1139 HOH HOH B . 
XA 5 HOH 149 1159 1159 HOH HOH B . 
XA 5 HOH 150 1176 1176 HOH HOH B . 
XA 5 HOH 151 1183 1183 HOH HOH B . 
XA 5 HOH 152 1190 1190 HOH HOH B . 
XA 5 HOH 153 1194 1194 HOH HOH B . 
XA 5 HOH 154 1196 1196 HOH HOH B . 
XA 5 HOH 155 1206 1206 HOH HOH B . 
XA 5 HOH 156 1216 1216 HOH HOH B . 
XA 5 HOH 157 1217 1217 HOH HOH B . 
XA 5 HOH 158 1225 1225 HOH HOH B . 
XA 5 HOH 159 1230 1230 HOH HOH B . 
XA 5 HOH 160 1246 1246 HOH HOH B . 
XA 5 HOH 161 1247 1247 HOH HOH B . 
XA 5 HOH 162 1248 1248 HOH HOH B . 
XA 5 HOH 163 1249 1249 HOH HOH B . 
XA 5 HOH 164 1259 1259 HOH HOH B . 
XA 5 HOH 165 1271 1271 HOH HOH B . 
XA 5 HOH 166 1280 1280 HOH HOH B . 
XA 5 HOH 167 1294 1294 HOH HOH B . 
XA 5 HOH 168 1311 1311 HOH HOH B . 
XA 5 HOH 169 1312 1312 HOH HOH B . 
XA 5 HOH 170 1317 1317 HOH HOH B . 
XA 5 HOH 171 1325 1325 HOH HOH B . 
XA 5 HOH 172 1327 1327 HOH HOH B . 
XA 5 HOH 173 1331 1331 HOH HOH B . 
XA 5 HOH 174 1338 1338 HOH HOH B . 
XA 5 HOH 175 1343 1343 HOH HOH B . 
XA 5 HOH 176 1355 1355 HOH HOH B . 
XA 5 HOH 177 1362 1362 HOH HOH B . 
XA 5 HOH 178 1372 1372 HOH HOH B . 
XA 5 HOH 179 1377 1377 HOH HOH B . 
XA 5 HOH 180 1382 1382 HOH HOH B . 
XA 5 HOH 181 1386 1386 HOH HOH B . 
XA 5 HOH 182 1391 1391 HOH HOH B . 
XA 5 HOH 183 1404 1404 HOH HOH B . 
XA 5 HOH 184 1412 1412 HOH HOH B . 
XA 5 HOH 185 1413 1413 HOH HOH B . 
XA 5 HOH 186 1425 1425 HOH HOH B . 
XA 5 HOH 187 1426 1426 HOH HOH B . 
XA 5 HOH 188 1432 1432 HOH HOH B . 
XA 5 HOH 189 1442 1442 HOH HOH B . 
XA 5 HOH 190 1443 1443 HOH HOH B . 
XA 5 HOH 191 1444 1444 HOH HOH B . 
XA 5 HOH 192 1451 1451 HOH HOH B . 
XA 5 HOH 193 1484 1484 HOH HOH B . 
XA 5 HOH 194 1485 1485 HOH HOH B . 
XA 5 HOH 195 1500 1500 HOH HOH B . 
XA 5 HOH 196 1502 1502 HOH HOH B . 
XA 5 HOH 197 1507 1507 HOH HOH B . 
XA 5 HOH 198 1509 1509 HOH HOH B . 
XA 5 HOH 199 1511 1511 HOH HOH B . 
XA 5 HOH 200 1514 1514 HOH HOH B . 
XA 5 HOH 201 1522 1522 HOH HOH B . 
XA 5 HOH 202 1524 1524 HOH HOH B . 
XA 5 HOH 203 1528 1528 HOH HOH B . 
XA 5 HOH 204 1529 1529 HOH HOH B . 
XA 5 HOH 205 1532 1532 HOH HOH B . 
XA 5 HOH 206 1538 1538 HOH HOH B . 
XA 5 HOH 207 1549 1549 HOH HOH B . 
XA 5 HOH 208 1610 1610 HOH HOH B . 
XA 5 HOH 209 1625 1625 HOH HOH B . 
XA 5 HOH 210 1631 1631 HOH HOH B . 
XA 5 HOH 211 1634 1634 HOH HOH B . 
XA 5 HOH 212 1641 1641 HOH HOH B . 
XA 5 HOH 213 1648 1648 HOH HOH B . 
XA 5 HOH 214 1650 1650 HOH HOH B . 
XA 5 HOH 215 1658 1658 HOH HOH B . 
XA 5 HOH 216 1663 1663 HOH HOH B . 
XA 5 HOH 217 1666 1666 HOH HOH B . 
XA 5 HOH 218 1673 1673 HOH HOH B . 
XA 5 HOH 219 1674 1674 HOH HOH B . 
XA 5 HOH 220 1701 1701 HOH HOH B . 
XA 5 HOH 221 1708 1708 HOH HOH B . 
XA 5 HOH 222 1709 1709 HOH HOH B . 
XA 5 HOH 223 1712 1712 HOH HOH B . 
XA 5 HOH 224 1713 1713 HOH HOH B . 
XA 5 HOH 225 1717 1717 HOH HOH B . 
XA 5 HOH 226 1718 1718 HOH HOH B . 
YA 5 HOH 1   154  2    HOH HOH D . 
YA 5 HOH 2   155  3    HOH HOH D . 
YA 5 HOH 3   156  5    HOH HOH D . 
YA 5 HOH 4   157  9    HOH HOH D . 
YA 5 HOH 5   158  11   HOH HOH D . 
YA 5 HOH 6   159  159  HOH HOH D . 
YA 5 HOH 7   160  26   HOH HOH D . 
YA 5 HOH 8   161  31   HOH HOH D . 
YA 5 HOH 9   162  53   HOH HOH D . 
YA 5 HOH 10  163  54   HOH HOH D . 
YA 5 HOH 11  164  57   HOH HOH D . 
YA 5 HOH 12  165  58   HOH HOH D . 
YA 5 HOH 13  166  166  HOH HOH D . 
YA 5 HOH 14  167  60   HOH HOH D . 
YA 5 HOH 15  168  66   HOH HOH D . 
YA 5 HOH 16  169  72   HOH HOH D . 
YA 5 HOH 17  170  77   HOH HOH D . 
YA 5 HOH 18  171  87   HOH HOH D . 
YA 5 HOH 19  172  100  HOH HOH D . 
YA 5 HOH 20  173  103  HOH HOH D . 
YA 5 HOH 21  174  104  HOH HOH D . 
YA 5 HOH 22  175  107  HOH HOH D . 
YA 5 HOH 23  176  109  HOH HOH D . 
YA 5 HOH 24  177  115  HOH HOH D . 
YA 5 HOH 25  178  118  HOH HOH D . 
YA 5 HOH 26  179  126  HOH HOH D . 
YA 5 HOH 27  180  127  HOH HOH D . 
YA 5 HOH 28  181  150  HOH HOH D . 
YA 5 HOH 29  182  151  HOH HOH D . 
YA 5 HOH 30  183  152  HOH HOH D . 
YA 5 HOH 31  190  190  HOH HOH D . 
YA 5 HOH 32  214  214  HOH HOH D . 
YA 5 HOH 33  223  223  HOH HOH D . 
YA 5 HOH 34  224  224  HOH HOH D . 
YA 5 HOH 35  225  225  HOH HOH D . 
YA 5 HOH 36  229  229  HOH HOH D . 
YA 5 HOH 37  239  239  HOH HOH D . 
YA 5 HOH 38  240  240  HOH HOH D . 
YA 5 HOH 39  267  267  HOH HOH D . 
YA 5 HOH 40  268  268  HOH HOH D . 
YA 5 HOH 41  287  287  HOH HOH D . 
YA 5 HOH 42  288  288  HOH HOH D . 
YA 5 HOH 43  296  296  HOH HOH D . 
YA 5 HOH 44  297  297  HOH HOH D . 
YA 5 HOH 45  307  307  HOH HOH D . 
YA 5 HOH 46  310  310  HOH HOH D . 
YA 5 HOH 47  316  316  HOH HOH D . 
YA 5 HOH 48  320  320  HOH HOH D . 
YA 5 HOH 49  321  321  HOH HOH D . 
YA 5 HOH 50  330  330  HOH HOH D . 
YA 5 HOH 51  339  339  HOH HOH D . 
YA 5 HOH 52  345  345  HOH HOH D . 
YA 5 HOH 53  356  356  HOH HOH D . 
YA 5 HOH 54  360  360  HOH HOH D . 
YA 5 HOH 55  361  361  HOH HOH D . 
YA 5 HOH 56  366  366  HOH HOH D . 
YA 5 HOH 57  374  374  HOH HOH D . 
YA 5 HOH 58  383  383  HOH HOH D . 
YA 5 HOH 59  384  384  HOH HOH D . 
YA 5 HOH 60  389  389  HOH HOH D . 
YA 5 HOH 61  398  398  HOH HOH D . 
YA 5 HOH 62  404  404  HOH HOH D . 
YA 5 HOH 63  415  415  HOH HOH D . 
YA 5 HOH 64  417  417  HOH HOH D . 
YA 5 HOH 65  432  432  HOH HOH D . 
YA 5 HOH 66  443  443  HOH HOH D . 
YA 5 HOH 67  469  469  HOH HOH D . 
YA 5 HOH 68  471  471  HOH HOH D . 
YA 5 HOH 69  506  506  HOH HOH D . 
YA 5 HOH 70  508  508  HOH HOH D . 
YA 5 HOH 71  515  515  HOH HOH D . 
YA 5 HOH 72  520  520  HOH HOH D . 
YA 5 HOH 73  521  521  HOH HOH D . 
YA 5 HOH 74  522  522  HOH HOH D . 
YA 5 HOH 75  528  528  HOH HOH D . 
YA 5 HOH 76  534  534  HOH HOH D . 
YA 5 HOH 77  543  543  HOH HOH D . 
YA 5 HOH 78  547  547  HOH HOH D . 
YA 5 HOH 79  554  554  HOH HOH D . 
YA 5 HOH 80  560  560  HOH HOH D . 
YA 5 HOH 81  567  567  HOH HOH D . 
YA 5 HOH 82  570  570  HOH HOH D . 
YA 5 HOH 83  581  581  HOH HOH D . 
YA 5 HOH 84  582  582  HOH HOH D . 
YA 5 HOH 85  583  583  HOH HOH D . 
YA 5 HOH 86  600  600  HOH HOH D . 
YA 5 HOH 87  608  608  HOH HOH D . 
YA 5 HOH 88  613  613  HOH HOH D . 
YA 5 HOH 89  620  620  HOH HOH D . 
YA 5 HOH 90  622  622  HOH HOH D . 
YA 5 HOH 91  623  623  HOH HOH D . 
YA 5 HOH 92  628  628  HOH HOH D . 
YA 5 HOH 93  633  633  HOH HOH D . 
YA 5 HOH 94  635  635  HOH HOH D . 
YA 5 HOH 95  639  639  HOH HOH D . 
YA 5 HOH 96  641  641  HOH HOH D . 
YA 5 HOH 97  645  645  HOH HOH D . 
YA 5 HOH 98  657  657  HOH HOH D . 
YA 5 HOH 99  666  666  HOH HOH D . 
YA 5 HOH 100 668  668  HOH HOH D . 
YA 5 HOH 101 671  671  HOH HOH D . 
YA 5 HOH 102 678  678  HOH HOH D . 
YA 5 HOH 103 682  682  HOH HOH D . 
YA 5 HOH 104 684  684  HOH HOH D . 
YA 5 HOH 105 687  687  HOH HOH D . 
YA 5 HOH 106 691  691  HOH HOH D . 
YA 5 HOH 107 708  708  HOH HOH D . 
YA 5 HOH 108 716  716  HOH HOH D . 
YA 5 HOH 109 724  724  HOH HOH D . 
YA 5 HOH 110 726  726  HOH HOH D . 
YA 5 HOH 111 738  738  HOH HOH D . 
YA 5 HOH 112 751  751  HOH HOH D . 
YA 5 HOH 113 752  752  HOH HOH D . 
YA 5 HOH 114 757  757  HOH HOH D . 
YA 5 HOH 115 787  787  HOH HOH D . 
YA 5 HOH 116 801  801  HOH HOH D . 
YA 5 HOH 117 812  812  HOH HOH D . 
YA 5 HOH 118 814  814  HOH HOH D . 
YA 5 HOH 119 824  824  HOH HOH D . 
YA 5 HOH 120 837  837  HOH HOH D . 
YA 5 HOH 121 841  841  HOH HOH D . 
YA 5 HOH 122 850  850  HOH HOH D . 
YA 5 HOH 123 855  855  HOH HOH D . 
YA 5 HOH 124 862  862  HOH HOH D . 
YA 5 HOH 125 880  880  HOH HOH D . 
YA 5 HOH 126 887  887  HOH HOH D . 
YA 5 HOH 127 888  888  HOH HOH D . 
YA 5 HOH 128 891  891  HOH HOH D . 
YA 5 HOH 129 920  920  HOH HOH D . 
YA 5 HOH 130 922  922  HOH HOH D . 
YA 5 HOH 131 929  929  HOH HOH D . 
YA 5 HOH 132 932  932  HOH HOH D . 
YA 5 HOH 133 933  933  HOH HOH D . 
YA 5 HOH 134 937  937  HOH HOH D . 
YA 5 HOH 135 948  948  HOH HOH D . 
YA 5 HOH 136 953  953  HOH HOH D . 
YA 5 HOH 137 981  981  HOH HOH D . 
YA 5 HOH 138 1016 1016 HOH HOH D . 
YA 5 HOH 139 1018 1018 HOH HOH D . 
YA 5 HOH 140 1021 1021 HOH HOH D . 
YA 5 HOH 141 1029 1029 HOH HOH D . 
YA 5 HOH 142 1036 1036 HOH HOH D . 
YA 5 HOH 143 1044 1044 HOH HOH D . 
YA 5 HOH 144 1058 1058 HOH HOH D . 
YA 5 HOH 145 1064 1064 HOH HOH D . 
YA 5 HOH 146 1068 1068 HOH HOH D . 
YA 5 HOH 147 1100 1100 HOH HOH D . 
YA 5 HOH 148 1102 1102 HOH HOH D . 
YA 5 HOH 149 1106 1106 HOH HOH D . 
YA 5 HOH 150 1112 1112 HOH HOH D . 
YA 5 HOH 151 1117 1117 HOH HOH D . 
YA 5 HOH 152 1118 1118 HOH HOH D . 
YA 5 HOH 153 1120 1120 HOH HOH D . 
YA 5 HOH 154 1126 1126 HOH HOH D . 
YA 5 HOH 155 1136 1136 HOH HOH D . 
YA 5 HOH 156 1146 1146 HOH HOH D . 
YA 5 HOH 157 1147 1147 HOH HOH D . 
YA 5 HOH 158 1148 1148 HOH HOH D . 
YA 5 HOH 159 1151 1151 HOH HOH D . 
YA 5 HOH 160 1153 1153 HOH HOH D . 
YA 5 HOH 161 1171 1171 HOH HOH D . 
YA 5 HOH 162 1177 1177 HOH HOH D . 
YA 5 HOH 163 1186 1186 HOH HOH D . 
YA 5 HOH 164 1223 1223 HOH HOH D . 
YA 5 HOH 165 1224 1224 HOH HOH D . 
YA 5 HOH 166 1228 1228 HOH HOH D . 
YA 5 HOH 167 1253 1253 HOH HOH D . 
YA 5 HOH 168 1258 1258 HOH HOH D . 
YA 5 HOH 169 1283 1283 HOH HOH D . 
YA 5 HOH 170 1309 1309 HOH HOH D . 
YA 5 HOH 171 1319 1319 HOH HOH D . 
YA 5 HOH 172 1320 1320 HOH HOH D . 
YA 5 HOH 173 1322 1322 HOH HOH D . 
YA 5 HOH 174 1324 1324 HOH HOH D . 
YA 5 HOH 175 1352 1352 HOH HOH D . 
YA 5 HOH 176 1375 1375 HOH HOH D . 
YA 5 HOH 177 1398 1398 HOH HOH D . 
YA 5 HOH 178 1414 1414 HOH HOH D . 
YA 5 HOH 179 1421 1421 HOH HOH D . 
YA 5 HOH 180 1460 1460 HOH HOH D . 
YA 5 HOH 181 1463 1463 HOH HOH D . 
YA 5 HOH 182 1469 1469 HOH HOH D . 
YA 5 HOH 183 1475 1475 HOH HOH D . 
YA 5 HOH 184 1481 1481 HOH HOH D . 
YA 5 HOH 185 1487 1487 HOH HOH D . 
YA 5 HOH 186 1505 1505 HOH HOH D . 
YA 5 HOH 187 1506 1506 HOH HOH D . 
YA 5 HOH 188 1519 1519 HOH HOH D . 
YA 5 HOH 189 1548 1548 HOH HOH D . 
YA 5 HOH 190 1551 1551 HOH HOH D . 
YA 5 HOH 191 1580 1580 HOH HOH D . 
YA 5 HOH 192 1587 1587 HOH HOH D . 
YA 5 HOH 193 1592 1592 HOH HOH D . 
YA 5 HOH 194 1597 1597 HOH HOH D . 
YA 5 HOH 195 1601 1601 HOH HOH D . 
YA 5 HOH 196 1605 1605 HOH HOH D . 
YA 5 HOH 197 1612 1612 HOH HOH D . 
YA 5 HOH 198 1617 1617 HOH HOH D . 
YA 5 HOH 199 1660 1660 HOH HOH D . 
YA 5 HOH 200 1671 1671 HOH HOH D . 
YA 5 HOH 201 1697 1697 HOH HOH D . 
YA 5 HOH 202 1706 1706 HOH HOH D . 
YA 5 HOH 203 1710 1710 HOH HOH D . 
YA 5 HOH 204 1745 1745 HOH HOH D . 
ZA 5 HOH 1   154  1    HOH HOH E . 
ZA 5 HOH 2   155  155  HOH HOH E . 
ZA 5 HOH 3   156  16   HOH HOH E . 
ZA 5 HOH 4   157  157  HOH HOH E . 
ZA 5 HOH 5   158  18   HOH HOH E . 
ZA 5 HOH 6   159  20   HOH HOH E . 
ZA 5 HOH 7   160  22   HOH HOH E . 
ZA 5 HOH 8   161  24   HOH HOH E . 
ZA 5 HOH 9   162  162  HOH HOH E . 
ZA 5 HOH 10  163  28   HOH HOH E . 
ZA 5 HOH 11  164  29   HOH HOH E . 
ZA 5 HOH 12  165  33   HOH HOH E . 
ZA 5 HOH 13  166  35   HOH HOH E . 
ZA 5 HOH 14  167  45   HOH HOH E . 
ZA 5 HOH 15  168  46   HOH HOH E . 
ZA 5 HOH 16  169  47   HOH HOH E . 
ZA 5 HOH 17  170  49   HOH HOH E . 
ZA 5 HOH 18  171  171  HOH HOH E . 
ZA 5 HOH 19  172  51   HOH HOH E . 
ZA 5 HOH 20  173  63   HOH HOH E . 
ZA 5 HOH 21  174  73   HOH HOH E . 
ZA 5 HOH 22  175  86   HOH HOH E . 
ZA 5 HOH 23  176  91   HOH HOH E . 
ZA 5 HOH 24  177  94   HOH HOH E . 
ZA 5 HOH 25  178  96   HOH HOH E . 
ZA 5 HOH 26  179  97   HOH HOH E . 
ZA 5 HOH 27  180  111  HOH HOH E . 
ZA 5 HOH 28  181  112  HOH HOH E . 
ZA 5 HOH 29  182  114  HOH HOH E . 
ZA 5 HOH 30  183  183  HOH HOH E . 
ZA 5 HOH 31  184  117  HOH HOH E . 
ZA 5 HOH 32  185  119  HOH HOH E . 
ZA 5 HOH 33  186  186  HOH HOH E . 
ZA 5 HOH 34  187  122  HOH HOH E . 
ZA 5 HOH 35  188  130  HOH HOH E . 
ZA 5 HOH 36  189  140  HOH HOH E . 
ZA 5 HOH 37  191  191  HOH HOH E . 
ZA 5 HOH 38  192  192  HOH HOH E . 
ZA 5 HOH 39  193  193  HOH HOH E . 
ZA 5 HOH 40  194  194  HOH HOH E . 
ZA 5 HOH 41  210  210  HOH HOH E . 
ZA 5 HOH 42  212  212  HOH HOH E . 
ZA 5 HOH 43  217  217  HOH HOH E . 
ZA 5 HOH 44  219  219  HOH HOH E . 
ZA 5 HOH 45  221  221  HOH HOH E . 
ZA 5 HOH 46  222  222  HOH HOH E . 
ZA 5 HOH 47  226  226  HOH HOH E . 
ZA 5 HOH 48  233  233  HOH HOH E . 
ZA 5 HOH 49  244  244  HOH HOH E . 
ZA 5 HOH 50  245  245  HOH HOH E . 
ZA 5 HOH 51  246  246  HOH HOH E . 
ZA 5 HOH 52  249  249  HOH HOH E . 
ZA 5 HOH 53  258  258  HOH HOH E . 
ZA 5 HOH 54  262  262  HOH HOH E . 
ZA 5 HOH 55  269  269  HOH HOH E . 
ZA 5 HOH 56  271  271  HOH HOH E . 
ZA 5 HOH 57  283  283  HOH HOH E . 
ZA 5 HOH 58  293  293  HOH HOH E . 
ZA 5 HOH 59  311  311  HOH HOH E . 
ZA 5 HOH 60  314  314  HOH HOH E . 
ZA 5 HOH 61  324  324  HOH HOH E . 
ZA 5 HOH 62  333  333  HOH HOH E . 
ZA 5 HOH 63  335  335  HOH HOH E . 
ZA 5 HOH 64  350  350  HOH HOH E . 
ZA 5 HOH 65  372  372  HOH HOH E . 
ZA 5 HOH 66  375  375  HOH HOH E . 
ZA 5 HOH 67  378  378  HOH HOH E . 
ZA 5 HOH 68  379  379  HOH HOH E . 
ZA 5 HOH 69  408  408  HOH HOH E . 
ZA 5 HOH 70  418  418  HOH HOH E . 
ZA 5 HOH 71  419  419  HOH HOH E . 
ZA 5 HOH 72  430  430  HOH HOH E . 
ZA 5 HOH 73  442  442  HOH HOH E . 
ZA 5 HOH 74  452  452  HOH HOH E . 
ZA 5 HOH 75  455  455  HOH HOH E . 
ZA 5 HOH 76  459  459  HOH HOH E . 
ZA 5 HOH 77  460  460  HOH HOH E . 
ZA 5 HOH 78  468  468  HOH HOH E . 
ZA 5 HOH 79  479  479  HOH HOH E . 
ZA 5 HOH 80  499  499  HOH HOH E . 
ZA 5 HOH 81  500  500  HOH HOH E . 
ZA 5 HOH 82  502  502  HOH HOH E . 
ZA 5 HOH 83  511  511  HOH HOH E . 
ZA 5 HOH 84  525  525  HOH HOH E . 
ZA 5 HOH 85  531  531  HOH HOH E . 
ZA 5 HOH 86  532  532  HOH HOH E . 
ZA 5 HOH 87  539  539  HOH HOH E . 
ZA 5 HOH 88  545  545  HOH HOH E . 
ZA 5 HOH 89  558  558  HOH HOH E . 
ZA 5 HOH 90  573  573  HOH HOH E . 
ZA 5 HOH 91  574  574  HOH HOH E . 
ZA 5 HOH 92  576  576  HOH HOH E . 
ZA 5 HOH 93  588  588  HOH HOH E . 
ZA 5 HOH 94  592  592  HOH HOH E . 
ZA 5 HOH 95  595  595  HOH HOH E . 
ZA 5 HOH 96  598  598  HOH HOH E . 
ZA 5 HOH 97  599  599  HOH HOH E . 
ZA 5 HOH 98  601  601  HOH HOH E . 
ZA 5 HOH 99  603  603  HOH HOH E . 
ZA 5 HOH 100 624  624  HOH HOH E . 
ZA 5 HOH 101 640  640  HOH HOH E . 
ZA 5 HOH 102 660  660  HOH HOH E . 
ZA 5 HOH 103 667  667  HOH HOH E . 
ZA 5 HOH 104 672  672  HOH HOH E . 
ZA 5 HOH 105 680  680  HOH HOH E . 
ZA 5 HOH 106 689  689  HOH HOH E . 
ZA 5 HOH 107 705  705  HOH HOH E . 
ZA 5 HOH 108 707  707  HOH HOH E . 
ZA 5 HOH 109 725  725  HOH HOH E . 
ZA 5 HOH 110 728  728  HOH HOH E . 
ZA 5 HOH 111 746  746  HOH HOH E . 
ZA 5 HOH 112 747  747  HOH HOH E . 
ZA 5 HOH 113 756  756  HOH HOH E . 
ZA 5 HOH 114 763  763  HOH HOH E . 
ZA 5 HOH 115 766  766  HOH HOH E . 
ZA 5 HOH 116 774  774  HOH HOH E . 
ZA 5 HOH 117 775  775  HOH HOH E . 
ZA 5 HOH 118 808  808  HOH HOH E . 
ZA 5 HOH 119 810  810  HOH HOH E . 
ZA 5 HOH 120 815  815  HOH HOH E . 
ZA 5 HOH 121 819  819  HOH HOH E . 
ZA 5 HOH 122 827  827  HOH HOH E . 
ZA 5 HOH 123 828  828  HOH HOH E . 
ZA 5 HOH 124 843  843  HOH HOH E . 
ZA 5 HOH 125 845  845  HOH HOH E . 
ZA 5 HOH 126 847  847  HOH HOH E . 
ZA 5 HOH 127 856  856  HOH HOH E . 
ZA 5 HOH 128 878  878  HOH HOH E . 
ZA 5 HOH 129 886  886  HOH HOH E . 
ZA 5 HOH 130 906  906  HOH HOH E . 
ZA 5 HOH 131 909  909  HOH HOH E . 
ZA 5 HOH 132 911  911  HOH HOH E . 
ZA 5 HOH 133 912  912  HOH HOH E . 
ZA 5 HOH 134 916  916  HOH HOH E . 
ZA 5 HOH 135 941  941  HOH HOH E . 
ZA 5 HOH 136 943  943  HOH HOH E . 
ZA 5 HOH 137 947  947  HOH HOH E . 
ZA 5 HOH 138 957  957  HOH HOH E . 
ZA 5 HOH 139 960  960  HOH HOH E . 
ZA 5 HOH 140 973  973  HOH HOH E . 
ZA 5 HOH 141 979  979  HOH HOH E . 
ZA 5 HOH 142 989  989  HOH HOH E . 
ZA 5 HOH 143 999  999  HOH HOH E . 
ZA 5 HOH 144 1007 1007 HOH HOH E . 
ZA 5 HOH 145 1013 1013 HOH HOH E . 
ZA 5 HOH 146 1028 1028 HOH HOH E . 
ZA 5 HOH 147 1040 1040 HOH HOH E . 
ZA 5 HOH 148 1070 1070 HOH HOH E . 
ZA 5 HOH 149 1085 1085 HOH HOH E . 
ZA 5 HOH 150 1086 1086 HOH HOH E . 
ZA 5 HOH 151 1098 1098 HOH HOH E . 
ZA 5 HOH 152 1116 1116 HOH HOH E . 
ZA 5 HOH 153 1141 1141 HOH HOH E . 
ZA 5 HOH 154 1142 1142 HOH HOH E . 
ZA 5 HOH 155 1145 1145 HOH HOH E . 
ZA 5 HOH 156 1150 1150 HOH HOH E . 
ZA 5 HOH 157 1158 1158 HOH HOH E . 
ZA 5 HOH 158 1161 1161 HOH HOH E . 
ZA 5 HOH 159 1164 1164 HOH HOH E . 
ZA 5 HOH 160 1169 1169 HOH HOH E . 
ZA 5 HOH 161 1187 1187 HOH HOH E . 
ZA 5 HOH 162 1195 1195 HOH HOH E . 
ZA 5 HOH 163 1197 1197 HOH HOH E . 
ZA 5 HOH 164 1198 1198 HOH HOH E . 
ZA 5 HOH 165 1203 1203 HOH HOH E . 
ZA 5 HOH 166 1213 1213 HOH HOH E . 
ZA 5 HOH 167 1221 1221 HOH HOH E . 
ZA 5 HOH 168 1231 1231 HOH HOH E . 
ZA 5 HOH 169 1237 1237 HOH HOH E . 
ZA 5 HOH 170 1239 1239 HOH HOH E . 
ZA 5 HOH 171 1284 1284 HOH HOH E . 
ZA 5 HOH 172 1289 1289 HOH HOH E . 
ZA 5 HOH 173 1293 1293 HOH HOH E . 
ZA 5 HOH 174 1296 1296 HOH HOH E . 
ZA 5 HOH 175 1301 1301 HOH HOH E . 
ZA 5 HOH 176 1303 1303 HOH HOH E . 
ZA 5 HOH 177 1332 1332 HOH HOH E . 
ZA 5 HOH 178 1336 1336 HOH HOH E . 
ZA 5 HOH 179 1340 1340 HOH HOH E . 
ZA 5 HOH 180 1356 1356 HOH HOH E . 
ZA 5 HOH 181 1359 1359 HOH HOH E . 
ZA 5 HOH 182 1374 1374 HOH HOH E . 
ZA 5 HOH 183 1384 1384 HOH HOH E . 
ZA 5 HOH 184 1388 1388 HOH HOH E . 
ZA 5 HOH 185 1399 1399 HOH HOH E . 
ZA 5 HOH 186 1406 1406 HOH HOH E . 
ZA 5 HOH 187 1420 1420 HOH HOH E . 
ZA 5 HOH 188 1427 1427 HOH HOH E . 
ZA 5 HOH 189 1430 1430 HOH HOH E . 
ZA 5 HOH 190 1435 1435 HOH HOH E . 
ZA 5 HOH 191 1439 1439 HOH HOH E . 
ZA 5 HOH 192 1459 1459 HOH HOH E . 
ZA 5 HOH 193 1473 1473 HOH HOH E . 
ZA 5 HOH 194 1479 1479 HOH HOH E . 
ZA 5 HOH 195 1491 1491 HOH HOH E . 
ZA 5 HOH 196 1498 1498 HOH HOH E . 
ZA 5 HOH 197 1513 1513 HOH HOH E . 
ZA 5 HOH 198 1517 1517 HOH HOH E . 
ZA 5 HOH 199 1530 1530 HOH HOH E . 
ZA 5 HOH 200 1534 1534 HOH HOH E . 
ZA 5 HOH 201 1568 1568 HOH HOH E . 
ZA 5 HOH 202 1575 1575 HOH HOH E . 
ZA 5 HOH 203 1588 1588 HOH HOH E . 
ZA 5 HOH 204 1589 1589 HOH HOH E . 
ZA 5 HOH 205 1594 1594 HOH HOH E . 
ZA 5 HOH 206 1604 1604 HOH HOH E . 
ZA 5 HOH 207 1607 1607 HOH HOH E . 
ZA 5 HOH 208 1615 1615 HOH HOH E . 
ZA 5 HOH 209 1624 1624 HOH HOH E . 
ZA 5 HOH 210 1633 1633 HOH HOH E . 
ZA 5 HOH 211 1635 1635 HOH HOH E . 
ZA 5 HOH 212 1636 1636 HOH HOH E . 
ZA 5 HOH 213 1639 1639 HOH HOH E . 
ZA 5 HOH 214 1642 1642 HOH HOH E . 
ZA 5 HOH 215 1646 1646 HOH HOH E . 
ZA 5 HOH 216 1647 1647 HOH HOH E . 
ZA 5 HOH 217 1649 1649 HOH HOH E . 
ZA 5 HOH 218 1657 1657 HOH HOH E . 
ZA 5 HOH 219 1665 1665 HOH HOH E . 
ZA 5 HOH 220 1681 1681 HOH HOH E . 
ZA 5 HOH 221 1686 1686 HOH HOH E . 
ZA 5 HOH 222 1689 1689 HOH HOH E . 
ZA 5 HOH 223 1692 1692 HOH HOH E . 
ZA 5 HOH 224 1695 1695 HOH HOH E . 
ZA 5 HOH 225 1699 1699 HOH HOH E . 
ZA 5 HOH 226 1700 1700 HOH HOH E . 
ZA 5 HOH 227 1704 1704 HOH HOH E . 
ZA 5 HOH 228 1719 1719 HOH HOH E . 
AB 5 HOH 1   154  41   HOH HOH F . 
AB 5 HOH 2   155  56   HOH HOH F . 
AB 5 HOH 3   156  62   HOH HOH F . 
AB 5 HOH 4   157  71   HOH HOH F . 
AB 5 HOH 5   158  79   HOH HOH F . 
AB 5 HOH 6   159  89   HOH HOH F . 
AB 5 HOH 7   160  92   HOH HOH F . 
AB 5 HOH 8   161  161  HOH HOH F . 
AB 5 HOH 9   162  93   HOH HOH F . 
AB 5 HOH 10  163  163  HOH HOH F . 
AB 5 HOH 11  164  164  HOH HOH F . 
AB 5 HOH 12  165  133  HOH HOH F . 
AB 5 HOH 13  166  136  HOH HOH F . 
AB 5 HOH 14  172  172  HOH HOH F . 
AB 5 HOH 15  178  178  HOH HOH F . 
AB 5 HOH 16  180  180  HOH HOH F . 
AB 5 HOH 17  182  182  HOH HOH F . 
AB 5 HOH 18  202  202  HOH HOH F . 
AB 5 HOH 19  204  204  HOH HOH F . 
AB 5 HOH 20  215  215  HOH HOH F . 
AB 5 HOH 21  218  218  HOH HOH F . 
AB 5 HOH 22  227  227  HOH HOH F . 
AB 5 HOH 23  248  248  HOH HOH F . 
AB 5 HOH 24  252  252  HOH HOH F . 
AB 5 HOH 25  274  274  HOH HOH F . 
AB 5 HOH 26  275  275  HOH HOH F . 
AB 5 HOH 27  281  281  HOH HOH F . 
AB 5 HOH 28  295  295  HOH HOH F . 
AB 5 HOH 29  315  315  HOH HOH F . 
AB 5 HOH 30  334  334  HOH HOH F . 
AB 5 HOH 31  342  342  HOH HOH F . 
AB 5 HOH 32  344  344  HOH HOH F . 
AB 5 HOH 33  346  346  HOH HOH F . 
AB 5 HOH 34  358  358  HOH HOH F . 
AB 5 HOH 35  364  364  HOH HOH F . 
AB 5 HOH 36  373  373  HOH HOH F . 
AB 5 HOH 37  394  394  HOH HOH F . 
AB 5 HOH 38  411  411  HOH HOH F . 
AB 5 HOH 39  420  420  HOH HOH F . 
AB 5 HOH 40  440  440  HOH HOH F . 
AB 5 HOH 41  445  445  HOH HOH F . 
AB 5 HOH 42  462  462  HOH HOH F . 
AB 5 HOH 43  470  470  HOH HOH F . 
AB 5 HOH 44  476  476  HOH HOH F . 
AB 5 HOH 45  481  481  HOH HOH F . 
AB 5 HOH 46  484  484  HOH HOH F . 
AB 5 HOH 47  486  486  HOH HOH F . 
AB 5 HOH 48  495  495  HOH HOH F . 
AB 5 HOH 49  498  498  HOH HOH F . 
AB 5 HOH 50  509  509  HOH HOH F . 
AB 5 HOH 51  514  514  HOH HOH F . 
AB 5 HOH 52  516  516  HOH HOH F . 
AB 5 HOH 53  523  523  HOH HOH F . 
AB 5 HOH 54  536  536  HOH HOH F . 
AB 5 HOH 55  551  551  HOH HOH F . 
AB 5 HOH 56  565  565  HOH HOH F . 
AB 5 HOH 57  571  571  HOH HOH F . 
AB 5 HOH 58  577  577  HOH HOH F . 
AB 5 HOH 59  587  587  HOH HOH F . 
AB 5 HOH 60  593  593  HOH HOH F . 
AB 5 HOH 61  594  594  HOH HOH F . 
AB 5 HOH 62  607  607  HOH HOH F . 
AB 5 HOH 63  609  609  HOH HOH F . 
AB 5 HOH 64  614  614  HOH HOH F . 
AB 5 HOH 65  618  618  HOH HOH F . 
AB 5 HOH 66  627  627  HOH HOH F . 
AB 5 HOH 67  634  634  HOH HOH F . 
AB 5 HOH 68  637  637  HOH HOH F . 
AB 5 HOH 69  638  638  HOH HOH F . 
AB 5 HOH 70  652  652  HOH HOH F . 
AB 5 HOH 71  674  674  HOH HOH F . 
AB 5 HOH 72  683  683  HOH HOH F . 
AB 5 HOH 73  700  700  HOH HOH F . 
AB 5 HOH 74  703  703  HOH HOH F . 
AB 5 HOH 75  706  706  HOH HOH F . 
AB 5 HOH 76  713  713  HOH HOH F . 
AB 5 HOH 77  715  715  HOH HOH F . 
AB 5 HOH 78  719  719  HOH HOH F . 
AB 5 HOH 79  720  720  HOH HOH F . 
AB 5 HOH 80  721  721  HOH HOH F . 
AB 5 HOH 81  730  730  HOH HOH F . 
AB 5 HOH 82  743  743  HOH HOH F . 
AB 5 HOH 83  749  749  HOH HOH F . 
AB 5 HOH 84  765  765  HOH HOH F . 
AB 5 HOH 85  770  770  HOH HOH F . 
AB 5 HOH 86  784  784  HOH HOH F . 
AB 5 HOH 87  788  788  HOH HOH F . 
AB 5 HOH 88  798  798  HOH HOH F . 
AB 5 HOH 89  800  800  HOH HOH F . 
AB 5 HOH 90  802  802  HOH HOH F . 
AB 5 HOH 91  811  811  HOH HOH F . 
AB 5 HOH 92  846  846  HOH HOH F . 
AB 5 HOH 93  860  860  HOH HOH F . 
AB 5 HOH 94  870  870  HOH HOH F . 
AB 5 HOH 95  871  871  HOH HOH F . 
AB 5 HOH 96  898  898  HOH HOH F . 
AB 5 HOH 97  899  899  HOH HOH F . 
AB 5 HOH 98  910  910  HOH HOH F . 
AB 5 HOH 99  970  970  HOH HOH F . 
AB 5 HOH 100 971  971  HOH HOH F . 
AB 5 HOH 101 977  977  HOH HOH F . 
AB 5 HOH 102 982  982  HOH HOH F . 
AB 5 HOH 103 984  984  HOH HOH F . 
AB 5 HOH 104 987  987  HOH HOH F . 
AB 5 HOH 105 990  990  HOH HOH F . 
AB 5 HOH 106 1025 1025 HOH HOH F . 
AB 5 HOH 107 1026 1026 HOH HOH F . 
AB 5 HOH 108 1041 1041 HOH HOH F . 
AB 5 HOH 109 1059 1059 HOH HOH F . 
AB 5 HOH 110 1060 1060 HOH HOH F . 
AB 5 HOH 111 1062 1062 HOH HOH F . 
AB 5 HOH 112 1081 1081 HOH HOH F . 
AB 5 HOH 113 1111 1111 HOH HOH F . 
AB 5 HOH 114 1119 1119 HOH HOH F . 
AB 5 HOH 115 1123 1123 HOH HOH F . 
AB 5 HOH 116 1132 1132 HOH HOH F . 
AB 5 HOH 117 1163 1163 HOH HOH F . 
AB 5 HOH 118 1182 1182 HOH HOH F . 
AB 5 HOH 119 1199 1199 HOH HOH F . 
AB 5 HOH 120 1207 1207 HOH HOH F . 
AB 5 HOH 121 1211 1211 HOH HOH F . 
AB 5 HOH 122 1212 1212 HOH HOH F . 
AB 5 HOH 123 1215 1215 HOH HOH F . 
AB 5 HOH 124 1220 1220 HOH HOH F . 
AB 5 HOH 125 1234 1234 HOH HOH F . 
AB 5 HOH 126 1235 1235 HOH HOH F . 
AB 5 HOH 127 1240 1240 HOH HOH F . 
AB 5 HOH 128 1256 1256 HOH HOH F . 
AB 5 HOH 129 1257 1257 HOH HOH F . 
AB 5 HOH 130 1272 1272 HOH HOH F . 
AB 5 HOH 131 1273 1273 HOH HOH F . 
AB 5 HOH 132 1276 1276 HOH HOH F . 
AB 5 HOH 133 1282 1282 HOH HOH F . 
AB 5 HOH 134 1287 1287 HOH HOH F . 
AB 5 HOH 135 1298 1298 HOH HOH F . 
AB 5 HOH 136 1302 1302 HOH HOH F . 
AB 5 HOH 137 1318 1318 HOH HOH F . 
AB 5 HOH 138 1329 1329 HOH HOH F . 
AB 5 HOH 139 1358 1358 HOH HOH F . 
AB 5 HOH 140 1371 1371 HOH HOH F . 
AB 5 HOH 141 1392 1392 HOH HOH F . 
AB 5 HOH 142 1403 1403 HOH HOH F . 
AB 5 HOH 143 1410 1410 HOH HOH F . 
AB 5 HOH 144 1423 1423 HOH HOH F . 
AB 5 HOH 145 1437 1437 HOH HOH F . 
AB 5 HOH 146 1445 1445 HOH HOH F . 
AB 5 HOH 147 1470 1470 HOH HOH F . 
AB 5 HOH 148 1480 1480 HOH HOH F . 
AB 5 HOH 149 1495 1495 HOH HOH F . 
AB 5 HOH 150 1550 1550 HOH HOH F . 
AB 5 HOH 151 1565 1565 HOH HOH F . 
AB 5 HOH 152 1598 1598 HOH HOH F . 
AB 5 HOH 153 1599 1599 HOH HOH F . 
AB 5 HOH 154 1602 1602 HOH HOH F . 
AB 5 HOH 155 1608 1608 HOH HOH F . 
AB 5 HOH 156 1614 1614 HOH HOH F . 
AB 5 HOH 157 1620 1620 HOH HOH F . 
AB 5 HOH 158 1627 1627 HOH HOH F . 
AB 5 HOH 159 1661 1661 HOH HOH F . 
AB 5 HOH 160 1662 1662 HOH HOH F . 
AB 5 HOH 161 1668 1668 HOH HOH F . 
AB 5 HOH 162 1707 1707 HOH HOH F . 
AB 5 HOH 163 1715 1715 HOH HOH F . 
AB 5 HOH 164 1727 1727 HOH HOH F . 
AB 5 HOH 165 1733 1733 HOH HOH F . 
BB 5 HOH 1   167  167  HOH HOH G . 
BB 5 HOH 2   168  200  HOH HOH G . 
BB 5 HOH 3   257  257  HOH HOH G . 
BB 5 HOH 4   270  270  HOH HOH G . 
BB 5 HOH 5   292  292  HOH HOH G . 
BB 5 HOH 6   306  306  HOH HOH G . 
BB 5 HOH 7   355  355  HOH HOH G . 
BB 5 HOH 8   367  367  HOH HOH G . 
BB 5 HOH 9   381  381  HOH HOH G . 
BB 5 HOH 10  396  396  HOH HOH G . 
BB 5 HOH 11  406  406  HOH HOH G . 
BB 5 HOH 12  437  437  HOH HOH G . 
BB 5 HOH 13  447  447  HOH HOH G . 
BB 5 HOH 14  454  454  HOH HOH G . 
BB 5 HOH 15  487  487  HOH HOH G . 
BB 5 HOH 16  510  510  HOH HOH G . 
BB 5 HOH 17  519  519  HOH HOH G . 
BB 5 HOH 18  524  524  HOH HOH G . 
BB 5 HOH 19  546  546  HOH HOH G . 
BB 5 HOH 20  557  557  HOH HOH G . 
BB 5 HOH 21  564  564  HOH HOH G . 
BB 5 HOH 22  575  575  HOH HOH G . 
BB 5 HOH 23  591  591  HOH HOH G . 
BB 5 HOH 24  611  611  HOH HOH G . 
BB 5 HOH 25  625  625  HOH HOH G . 
BB 5 HOH 26  647  647  HOH HOH G . 
BB 5 HOH 27  675  675  HOH HOH G . 
BB 5 HOH 28  697  697  HOH HOH G . 
BB 5 HOH 29  714  714  HOH HOH G . 
BB 5 HOH 30  768  768  HOH HOH G . 
BB 5 HOH 31  773  773  HOH HOH G . 
BB 5 HOH 32  777  777  HOH HOH G . 
BB 5 HOH 33  796  796  HOH HOH G . 
BB 5 HOH 34  809  809  HOH HOH G . 
BB 5 HOH 35  817  817  HOH HOH G . 
BB 5 HOH 36  822  822  HOH HOH G . 
BB 5 HOH 37  825  825  HOH HOH G . 
BB 5 HOH 38  831  831  HOH HOH G . 
BB 5 HOH 39  835  835  HOH HOH G . 
BB 5 HOH 40  839  839  HOH HOH G . 
BB 5 HOH 41  848  848  HOH HOH G . 
BB 5 HOH 42  857  857  HOH HOH G . 
BB 5 HOH 43  859  859  HOH HOH G . 
BB 5 HOH 44  873  873  HOH HOH G . 
BB 5 HOH 45  876  876  HOH HOH G . 
BB 5 HOH 46  881  881  HOH HOH G . 
BB 5 HOH 47  883  883  HOH HOH G . 
BB 5 HOH 48  890  890  HOH HOH G . 
BB 5 HOH 49  904  904  HOH HOH G . 
BB 5 HOH 50  907  907  HOH HOH G . 
BB 5 HOH 51  921  921  HOH HOH G . 
BB 5 HOH 52  927  927  HOH HOH G . 
BB 5 HOH 53  962  962  HOH HOH G . 
BB 5 HOH 54  974  974  HOH HOH G . 
BB 5 HOH 55  976  976  HOH HOH G . 
BB 5 HOH 56  993  993  HOH HOH G . 
BB 5 HOH 57  1005 1005 HOH HOH G . 
BB 5 HOH 58  1008 1008 HOH HOH G . 
BB 5 HOH 59  1009 1009 HOH HOH G . 
BB 5 HOH 60  1023 1023 HOH HOH G . 
BB 5 HOH 61  1031 1031 HOH HOH G . 
BB 5 HOH 62  1032 1032 HOH HOH G . 
BB 5 HOH 63  1066 1066 HOH HOH G . 
BB 5 HOH 64  1072 1072 HOH HOH G . 
BB 5 HOH 65  1083 1083 HOH HOH G . 
BB 5 HOH 66  1087 1087 HOH HOH G . 
BB 5 HOH 67  1092 1092 HOH HOH G . 
BB 5 HOH 68  1095 1095 HOH HOH G . 
BB 5 HOH 69  1099 1099 HOH HOH G . 
BB 5 HOH 70  1104 1104 HOH HOH G . 
BB 5 HOH 71  1110 1110 HOH HOH G . 
BB 5 HOH 72  1114 1114 HOH HOH G . 
BB 5 HOH 73  1127 1127 HOH HOH G . 
BB 5 HOH 74  1138 1138 HOH HOH G . 
BB 5 HOH 75  1140 1140 HOH HOH G . 
BB 5 HOH 76  1152 1152 HOH HOH G . 
BB 5 HOH 77  1156 1156 HOH HOH G . 
BB 5 HOH 78  1167 1167 HOH HOH G . 
BB 5 HOH 79  1180 1180 HOH HOH G . 
BB 5 HOH 80  1189 1189 HOH HOH G . 
BB 5 HOH 81  1205 1205 HOH HOH G . 
BB 5 HOH 82  1210 1210 HOH HOH G . 
BB 5 HOH 83  1214 1214 HOH HOH G . 
BB 5 HOH 84  1238 1238 HOH HOH G . 
BB 5 HOH 85  1243 1243 HOH HOH G . 
BB 5 HOH 86  1250 1250 HOH HOH G . 
BB 5 HOH 87  1251 1251 HOH HOH G . 
BB 5 HOH 88  1264 1264 HOH HOH G . 
BB 5 HOH 89  1265 1265 HOH HOH G . 
BB 5 HOH 90  1269 1269 HOH HOH G . 
BB 5 HOH 91  1275 1275 HOH HOH G . 
BB 5 HOH 92  1278 1278 HOH HOH G . 
BB 5 HOH 93  1307 1307 HOH HOH G . 
BB 5 HOH 94  1316 1316 HOH HOH G . 
BB 5 HOH 95  1335 1335 HOH HOH G . 
BB 5 HOH 96  1344 1344 HOH HOH G . 
BB 5 HOH 97  1349 1349 HOH HOH G . 
BB 5 HOH 98  1351 1351 HOH HOH G . 
BB 5 HOH 99  1353 1353 HOH HOH G . 
BB 5 HOH 100 1360 1360 HOH HOH G . 
BB 5 HOH 101 1361 1361 HOH HOH G . 
BB 5 HOH 102 1394 1394 HOH HOH G . 
BB 5 HOH 103 1405 1405 HOH HOH G . 
BB 5 HOH 104 1415 1415 HOH HOH G . 
BB 5 HOH 105 1424 1424 HOH HOH G . 
BB 5 HOH 106 1477 1477 HOH HOH G . 
BB 5 HOH 107 1489 1489 HOH HOH G . 
BB 5 HOH 108 1497 1497 HOH HOH G . 
BB 5 HOH 109 1521 1521 HOH HOH G . 
BB 5 HOH 110 1525 1525 HOH HOH G . 
BB 5 HOH 111 1540 1540 HOH HOH G . 
BB 5 HOH 112 1541 1541 HOH HOH G . 
BB 5 HOH 113 1554 1554 HOH HOH G . 
BB 5 HOH 114 1555 1555 HOH HOH G . 
BB 5 HOH 115 1569 1569 HOH HOH G . 
BB 5 HOH 116 1609 1609 HOH HOH G . 
BB 5 HOH 117 1632 1632 HOH HOH G . 
BB 5 HOH 118 1643 1643 HOH HOH G . 
BB 5 HOH 119 1677 1677 HOH HOH G . 
BB 5 HOH 120 1679 1679 HOH HOH G . 
BB 5 HOH 121 1683 1683 HOH HOH G . 
BB 5 HOH 122 1685 1685 HOH HOH G . 
BB 5 HOH 123 1688 1688 HOH HOH G . 
CB 5 HOH 1   154  64   HOH HOH H . 
CB 5 HOH 2   155  76   HOH HOH H . 
CB 5 HOH 3   156  84   HOH HOH H . 
CB 5 HOH 4   157  98   HOH HOH H . 
CB 5 HOH 5   158  106  HOH HOH H . 
CB 5 HOH 6   159  110  HOH HOH H . 
CB 5 HOH 7   160  123  HOH HOH H . 
CB 5 HOH 8   161  128  HOH HOH H . 
CB 5 HOH 9   162  131  HOH HOH H . 
CB 5 HOH 10  163  145  HOH HOH H . 
CB 5 HOH 11  164  153  HOH HOH H . 
CB 5 HOH 12  176  176  HOH HOH H . 
CB 5 HOH 13  209  209  HOH HOH H . 
CB 5 HOH 14  255  255  HOH HOH H . 
CB 5 HOH 15  298  298  HOH HOH H . 
CB 5 HOH 16  301  301  HOH HOH H . 
CB 5 HOH 17  302  302  HOH HOH H . 
CB 5 HOH 18  304  304  HOH HOH H . 
CB 5 HOH 19  312  312  HOH HOH H . 
CB 5 HOH 20  348  348  HOH HOH H . 
CB 5 HOH 21  368  368  HOH HOH H . 
CB 5 HOH 22  371  371  HOH HOH H . 
CB 5 HOH 23  387  387  HOH HOH H . 
CB 5 HOH 24  431  431  HOH HOH H . 
CB 5 HOH 25  464  464  HOH HOH H . 
CB 5 HOH 26  467  467  HOH HOH H . 
CB 5 HOH 27  490  490  HOH HOH H . 
CB 5 HOH 28  492  492  HOH HOH H . 
CB 5 HOH 29  497  497  HOH HOH H . 
CB 5 HOH 30  537  537  HOH HOH H . 
CB 5 HOH 31  540  540  HOH HOH H . 
CB 5 HOH 32  563  563  HOH HOH H . 
CB 5 HOH 33  584  584  HOH HOH H . 
CB 5 HOH 34  589  589  HOH HOH H . 
CB 5 HOH 35  604  604  HOH HOH H . 
CB 5 HOH 36  619  619  HOH HOH H . 
CB 5 HOH 37  642  642  HOH HOH H . 
CB 5 HOH 38  643  643  HOH HOH H . 
CB 5 HOH 39  648  648  HOH HOH H . 
CB 5 HOH 40  650  650  HOH HOH H . 
CB 5 HOH 41  654  654  HOH HOH H . 
CB 5 HOH 42  670  670  HOH HOH H . 
CB 5 HOH 43  686  686  HOH HOH H . 
CB 5 HOH 44  692  692  HOH HOH H . 
CB 5 HOH 45  698  698  HOH HOH H . 
CB 5 HOH 46  742  742  HOH HOH H . 
CB 5 HOH 47  745  745  HOH HOH H . 
CB 5 HOH 48  750  750  HOH HOH H . 
CB 5 HOH 49  761  761  HOH HOH H . 
CB 5 HOH 50  781  781  HOH HOH H . 
CB 5 HOH 51  794  794  HOH HOH H . 
CB 5 HOH 52  799  799  HOH HOH H . 
CB 5 HOH 53  806  806  HOH HOH H . 
CB 5 HOH 54  807  807  HOH HOH H . 
CB 5 HOH 55  840  840  HOH HOH H . 
CB 5 HOH 56  851  851  HOH HOH H . 
CB 5 HOH 57  861  861  HOH HOH H . 
CB 5 HOH 58  875  875  HOH HOH H . 
CB 5 HOH 59  879  879  HOH HOH H . 
CB 5 HOH 60  884  884  HOH HOH H . 
CB 5 HOH 61  889  889  HOH HOH H . 
CB 5 HOH 62  895  895  HOH HOH H . 
CB 5 HOH 63  901  901  HOH HOH H . 
CB 5 HOH 64  934  934  HOH HOH H . 
CB 5 HOH 65  940  940  HOH HOH H . 
CB 5 HOH 66  951  951  HOH HOH H . 
CB 5 HOH 67  952  952  HOH HOH H . 
CB 5 HOH 68  961  961  HOH HOH H . 
CB 5 HOH 69  964  964  HOH HOH H . 
CB 5 HOH 70  1015 1015 HOH HOH H . 
CB 5 HOH 71  1022 1022 HOH HOH H . 
CB 5 HOH 72  1038 1038 HOH HOH H . 
CB 5 HOH 73  1048 1048 HOH HOH H . 
CB 5 HOH 74  1065 1065 HOH HOH H . 
CB 5 HOH 75  1067 1067 HOH HOH H . 
CB 5 HOH 76  1091 1091 HOH HOH H . 
CB 5 HOH 77  1115 1115 HOH HOH H . 
CB 5 HOH 78  1134 1134 HOH HOH H . 
CB 5 HOH 79  1144 1144 HOH HOH H . 
CB 5 HOH 80  1154 1154 HOH HOH H . 
CB 5 HOH 81  1165 1165 HOH HOH H . 
CB 5 HOH 82  1166 1166 HOH HOH H . 
CB 5 HOH 83  1173 1173 HOH HOH H . 
CB 5 HOH 84  1188 1188 HOH HOH H . 
CB 5 HOH 85  1202 1202 HOH HOH H . 
CB 5 HOH 86  1218 1218 HOH HOH H . 
CB 5 HOH 87  1233 1233 HOH HOH H . 
CB 5 HOH 88  1236 1236 HOH HOH H . 
CB 5 HOH 89  1285 1285 HOH HOH H . 
CB 5 HOH 90  1286 1286 HOH HOH H . 
CB 5 HOH 91  1288 1288 HOH HOH H . 
CB 5 HOH 92  1304 1304 HOH HOH H . 
CB 5 HOH 93  1321 1321 HOH HOH H . 
CB 5 HOH 94  1328 1328 HOH HOH H . 
CB 5 HOH 95  1341 1341 HOH HOH H . 
CB 5 HOH 96  1346 1346 HOH HOH H . 
CB 5 HOH 97  1379 1379 HOH HOH H . 
CB 5 HOH 98  1383 1383 HOH HOH H . 
CB 5 HOH 99  1389 1389 HOH HOH H . 
CB 5 HOH 100 1393 1393 HOH HOH H . 
CB 5 HOH 101 1400 1400 HOH HOH H . 
CB 5 HOH 102 1407 1407 HOH HOH H . 
CB 5 HOH 103 1428 1428 HOH HOH H . 
CB 5 HOH 104 1429 1429 HOH HOH H . 
CB 5 HOH 105 1431 1431 HOH HOH H . 
CB 5 HOH 106 1438 1438 HOH HOH H . 
CB 5 HOH 107 1456 1456 HOH HOH H . 
CB 5 HOH 108 1461 1461 HOH HOH H . 
CB 5 HOH 109 1467 1467 HOH HOH H . 
CB 5 HOH 110 1474 1474 HOH HOH H . 
CB 5 HOH 111 1483 1483 HOH HOH H . 
CB 5 HOH 112 1488 1488 HOH HOH H . 
CB 5 HOH 113 1504 1504 HOH HOH H . 
CB 5 HOH 114 1523 1523 HOH HOH H . 
CB 5 HOH 115 1531 1531 HOH HOH H . 
CB 5 HOH 116 1533 1533 HOH HOH H . 
CB 5 HOH 117 1544 1544 HOH HOH H . 
CB 5 HOH 118 1553 1553 HOH HOH H . 
CB 5 HOH 119 1591 1591 HOH HOH H . 
CB 5 HOH 120 1600 1600 HOH HOH H . 
CB 5 HOH 121 1622 1622 HOH HOH H . 
CB 5 HOH 122 1623 1623 HOH HOH H . 
CB 5 HOH 123 1626 1626 HOH HOH H . 
CB 5 HOH 124 1628 1628 HOH HOH H . 
CB 5 HOH 125 1659 1659 HOH HOH H . 
CB 5 HOH 126 1670 1670 HOH HOH H . 
CB 5 HOH 127 1680 1680 HOH HOH H . 
CB 5 HOH 128 1690 1690 HOH HOH H . 
DB 5 HOH 1   236  236  HOH HOH I . 
DB 5 HOH 2   343  343  HOH HOH I . 
DB 5 HOH 3   405  405  HOH HOH I . 
DB 5 HOH 4   413  413  HOH HOH I . 
DB 5 HOH 5   435  435  HOH HOH I . 
DB 5 HOH 6   446  446  HOH HOH I . 
DB 5 HOH 7   451  451  HOH HOH I . 
DB 5 HOH 8   475  475  HOH HOH I . 
DB 5 HOH 9   485  485  HOH HOH I . 
DB 5 HOH 10  685  685  HOH HOH I . 
DB 5 HOH 11  735  735  HOH HOH I . 
DB 5 HOH 12  782  782  HOH HOH I . 
DB 5 HOH 13  818  818  HOH HOH I . 
DB 5 HOH 14  858  858  HOH HOH I . 
DB 5 HOH 15  885  885  HOH HOH I . 
DB 5 HOH 16  900  900  HOH HOH I . 
DB 5 HOH 17  902  902  HOH HOH I . 
DB 5 HOH 18  914  914  HOH HOH I . 
DB 5 HOH 19  959  959  HOH HOH I . 
DB 5 HOH 20  969  969  HOH HOH I . 
DB 5 HOH 21  980  980  HOH HOH I . 
DB 5 HOH 22  1012 1012 HOH HOH I . 
DB 5 HOH 23  1047 1047 HOH HOH I . 
DB 5 HOH 24  1082 1082 HOH HOH I . 
DB 5 HOH 25  1094 1094 HOH HOH I . 
DB 5 HOH 26  1096 1096 HOH HOH I . 
DB 5 HOH 27  1208 1208 HOH HOH I . 
DB 5 HOH 28  1209 1209 HOH HOH I . 
DB 5 HOH 29  1241 1241 HOH HOH I . 
DB 5 HOH 30  1244 1244 HOH HOH I . 
DB 5 HOH 31  1268 1268 HOH HOH I . 
DB 5 HOH 32  1299 1299 HOH HOH I . 
DB 5 HOH 33  1305 1305 HOH HOH I . 
DB 5 HOH 34  1367 1367 HOH HOH I . 
DB 5 HOH 35  1385 1385 HOH HOH I . 
DB 5 HOH 36  1396 1396 HOH HOH I . 
DB 5 HOH 37  1419 1419 HOH HOH I . 
DB 5 HOH 38  1433 1433 HOH HOH I . 
DB 5 HOH 39  1440 1440 HOH HOH I . 
DB 5 HOH 40  1441 1441 HOH HOH I . 
DB 5 HOH 41  1462 1462 HOH HOH I . 
DB 5 HOH 42  1466 1466 HOH HOH I . 
DB 5 HOH 43  1508 1508 HOH HOH I . 
DB 5 HOH 44  1559 1559 HOH HOH I . 
DB 5 HOH 45  1566 1566 HOH HOH I . 
DB 5 HOH 46  1593 1593 HOH HOH I . 
DB 5 HOH 47  1613 1613 HOH HOH I . 
DB 5 HOH 48  1619 1619 HOH HOH I . 
DB 5 HOH 49  1672 1672 HOH HOH I . 
DB 5 HOH 50  1678 1678 HOH HOH I . 
DB 5 HOH 51  1682 1682 HOH HOH I . 
DB 5 HOH 52  1705 1705 HOH HOH I . 
EB 5 HOH 1   154  13   HOH HOH J . 
EB 5 HOH 2   155  39   HOH HOH J . 
EB 5 HOH 3   156  156  HOH HOH J . 
EB 5 HOH 4   157  61   HOH HOH J . 
EB 5 HOH 5   158  81   HOH HOH J . 
EB 5 HOH 6   159  113  HOH HOH J . 
EB 5 HOH 7   160  132  HOH HOH J . 
EB 5 HOH 8   161  139  HOH HOH J . 
EB 5 HOH 9   162  142  HOH HOH J . 
EB 5 HOH 10  163  300  HOH HOH J . 
EB 5 HOH 11  196  196  HOH HOH J . 
EB 5 HOH 12  256  256  HOH HOH J . 
EB 5 HOH 13  261  261  HOH HOH J . 
EB 5 HOH 14  277  277  HOH HOH J . 
EB 5 HOH 15  285  285  HOH HOH J . 
EB 5 HOH 16  291  291  HOH HOH J . 
EB 5 HOH 17  305  305  HOH HOH J . 
EB 5 HOH 18  336  336  HOH HOH J . 
EB 5 HOH 19  340  340  HOH HOH J . 
EB 5 HOH 20  347  347  HOH HOH J . 
EB 5 HOH 21  357  357  HOH HOH J . 
EB 5 HOH 22  362  362  HOH HOH J . 
EB 5 HOH 23  363  363  HOH HOH J . 
EB 5 HOH 24  365  365  HOH HOH J . 
EB 5 HOH 25  382  382  HOH HOH J . 
EB 5 HOH 26  385  385  HOH HOH J . 
EB 5 HOH 27  390  390  HOH HOH J . 
EB 5 HOH 28  391  391  HOH HOH J . 
EB 5 HOH 29  412  412  HOH HOH J . 
EB 5 HOH 30  422  422  HOH HOH J . 
EB 5 HOH 31  426  426  HOH HOH J . 
EB 5 HOH 32  428  428  HOH HOH J . 
EB 5 HOH 33  438  438  HOH HOH J . 
EB 5 HOH 34  439  439  HOH HOH J . 
EB 5 HOH 35  444  444  HOH HOH J . 
EB 5 HOH 36  456  456  HOH HOH J . 
EB 5 HOH 37  457  457  HOH HOH J . 
EB 5 HOH 38  463  463  HOH HOH J . 
EB 5 HOH 39  491  491  HOH HOH J . 
EB 5 HOH 40  505  505  HOH HOH J . 
EB 5 HOH 41  513  513  HOH HOH J . 
EB 5 HOH 42  526  526  HOH HOH J . 
EB 5 HOH 43  552  552  HOH HOH J . 
EB 5 HOH 44  572  572  HOH HOH J . 
EB 5 HOH 45  579  579  HOH HOH J . 
EB 5 HOH 46  585  585  HOH HOH J . 
EB 5 HOH 47  602  602  HOH HOH J . 
EB 5 HOH 48  605  605  HOH HOH J . 
EB 5 HOH 49  615  615  HOH HOH J . 
EB 5 HOH 50  631  631  HOH HOH J . 
EB 5 HOH 51  662  662  HOH HOH J . 
EB 5 HOH 52  664  664  HOH HOH J . 
EB 5 HOH 53  673  673  HOH HOH J . 
EB 5 HOH 54  679  679  HOH HOH J . 
EB 5 HOH 55  693  693  HOH HOH J . 
EB 5 HOH 56  695  695  HOH HOH J . 
EB 5 HOH 57  727  727  HOH HOH J . 
EB 5 HOH 58  731  731  HOH HOH J . 
EB 5 HOH 59  732  732  HOH HOH J . 
EB 5 HOH 60  736  736  HOH HOH J . 
EB 5 HOH 61  739  739  HOH HOH J . 
EB 5 HOH 62  786  786  HOH HOH J . 
EB 5 HOH 63  790  790  HOH HOH J . 
EB 5 HOH 64  795  795  HOH HOH J . 
EB 5 HOH 65  797  797  HOH HOH J . 
EB 5 HOH 66  804  804  HOH HOH J . 
EB 5 HOH 67  816  816  HOH HOH J . 
EB 5 HOH 68  849  849  HOH HOH J . 
EB 5 HOH 69  852  852  HOH HOH J . 
EB 5 HOH 70  865  865  HOH HOH J . 
EB 5 HOH 71  892  892  HOH HOH J . 
EB 5 HOH 72  894  894  HOH HOH J . 
EB 5 HOH 73  905  905  HOH HOH J . 
EB 5 HOH 74  915  915  HOH HOH J . 
EB 5 HOH 75  926  926  HOH HOH J . 
EB 5 HOH 76  928  928  HOH HOH J . 
EB 5 HOH 77  930  930  HOH HOH J . 
EB 5 HOH 78  936  936  HOH HOH J . 
EB 5 HOH 79  938  938  HOH HOH J . 
EB 5 HOH 80  950  950  HOH HOH J . 
EB 5 HOH 81  963  963  HOH HOH J . 
EB 5 HOH 82  968  968  HOH HOH J . 
EB 5 HOH 83  975  975  HOH HOH J . 
EB 5 HOH 84  998  998  HOH HOH J . 
EB 5 HOH 85  1006 1006 HOH HOH J . 
EB 5 HOH 86  1010 1010 HOH HOH J . 
EB 5 HOH 87  1011 1011 HOH HOH J . 
EB 5 HOH 88  1030 1030 HOH HOH J . 
EB 5 HOH 89  1034 1034 HOH HOH J . 
EB 5 HOH 90  1050 1050 HOH HOH J . 
EB 5 HOH 91  1051 1051 HOH HOH J . 
EB 5 HOH 92  1056 1056 HOH HOH J . 
EB 5 HOH 93  1076 1076 HOH HOH J . 
EB 5 HOH 94  1088 1088 HOH HOH J . 
EB 5 HOH 95  1108 1108 HOH HOH J . 
EB 5 HOH 96  1170 1170 HOH HOH J . 
EB 5 HOH 97  1219 1219 HOH HOH J . 
EB 5 HOH 98  1229 1229 HOH HOH J . 
EB 5 HOH 99  1232 1232 HOH HOH J . 
EB 5 HOH 100 1242 1242 HOH HOH J . 
EB 5 HOH 101 1262 1262 HOH HOH J . 
EB 5 HOH 102 1270 1270 HOH HOH J . 
EB 5 HOH 103 1274 1274 HOH HOH J . 
EB 5 HOH 104 1279 1279 HOH HOH J . 
EB 5 HOH 105 1306 1306 HOH HOH J . 
EB 5 HOH 106 1313 1313 HOH HOH J . 
EB 5 HOH 107 1326 1326 HOH HOH J . 
EB 5 HOH 108 1333 1333 HOH HOH J . 
EB 5 HOH 109 1337 1337 HOH HOH J . 
EB 5 HOH 110 1342 1342 HOH HOH J . 
EB 5 HOH 111 1354 1354 HOH HOH J . 
EB 5 HOH 112 1376 1376 HOH HOH J . 
EB 5 HOH 113 1378 1378 HOH HOH J . 
EB 5 HOH 114 1390 1390 HOH HOH J . 
EB 5 HOH 115 1401 1401 HOH HOH J . 
EB 5 HOH 116 1408 1408 HOH HOH J . 
EB 5 HOH 117 1455 1455 HOH HOH J . 
EB 5 HOH 118 1458 1458 HOH HOH J . 
EB 5 HOH 119 1472 1472 HOH HOH J . 
EB 5 HOH 120 1482 1482 HOH HOH J . 
EB 5 HOH 121 1490 1490 HOH HOH J . 
EB 5 HOH 122 1499 1499 HOH HOH J . 
EB 5 HOH 123 1515 1515 HOH HOH J . 
EB 5 HOH 124 1516 1516 HOH HOH J . 
EB 5 HOH 125 1526 1526 HOH HOH J . 
EB 5 HOH 126 1535 1535 HOH HOH J . 
EB 5 HOH 127 1536 1536 HOH HOH J . 
EB 5 HOH 128 1539 1539 HOH HOH J . 
EB 5 HOH 129 1542 1542 HOH HOH J . 
EB 5 HOH 130 1545 1545 HOH HOH J . 
EB 5 HOH 131 1547 1547 HOH HOH J . 
EB 5 HOH 132 1556 1556 HOH HOH J . 
EB 5 HOH 133 1560 1560 HOH HOH J . 
EB 5 HOH 134 1586 1586 HOH HOH J . 
EB 5 HOH 135 1590 1590 HOH HOH J . 
EB 5 HOH 136 1595 1595 HOH HOH J . 
EB 5 HOH 137 1611 1611 HOH HOH J . 
EB 5 HOH 138 1621 1621 HOH HOH J . 
EB 5 HOH 139 1630 1630 HOH HOH J . 
EB 5 HOH 140 1637 1637 HOH HOH J . 
EB 5 HOH 141 1645 1645 HOH HOH J . 
EB 5 HOH 142 1652 1652 HOH HOH J . 
EB 5 HOH 143 1669 1669 HOH HOH J . 
EB 5 HOH 144 1687 1687 HOH HOH J . 
EB 5 HOH 145 1698 1698 HOH HOH J . 
EB 5 HOH 146 1714 1714 HOH HOH J . 
EB 5 HOH 147 1721 1721 HOH HOH J . 
EB 5 HOH 148 1722 1722 HOH HOH J . 
EB 5 HOH 149 1723 1723 HOH HOH J . 
EB 5 HOH 150 1725 1725 HOH HOH J . 
EB 5 HOH 151 1726 1726 HOH HOH J . 
EB 5 HOH 152 1734 1734 HOH HOH J . 
FB 5 HOH 1   234  234  HOH HOH K . 
FB 5 HOH 2   237  237  HOH HOH K . 
FB 5 HOH 3   263  263  HOH HOH K . 
FB 5 HOH 4   272  272  HOH HOH K . 
FB 5 HOH 5   329  329  HOH HOH K . 
FB 5 HOH 6   388  388  HOH HOH K . 
FB 5 HOH 7   434  434  HOH HOH K . 
FB 5 HOH 8   466  466  HOH HOH K . 
FB 5 HOH 9   488  488  HOH HOH K . 
FB 5 HOH 10  529  529  HOH HOH K . 
FB 5 HOH 11  704  704  HOH HOH K . 
FB 5 HOH 12  759  759  HOH HOH K . 
FB 5 HOH 13  826  826  HOH HOH K . 
FB 5 HOH 14  844  844  HOH HOH K . 
FB 5 HOH 15  897  897  HOH HOH K . 
FB 5 HOH 16  908  908  HOH HOH K . 
FB 5 HOH 17  918  918  HOH HOH K . 
FB 5 HOH 18  944  944  HOH HOH K . 
FB 5 HOH 19  949  949  HOH HOH K . 
FB 5 HOH 20  972  972  HOH HOH K . 
FB 5 HOH 21  978  978  HOH HOH K . 
FB 5 HOH 22  983  983  HOH HOH K . 
FB 5 HOH 23  996  996  HOH HOH K . 
FB 5 HOH 24  1000 1000 HOH HOH K . 
FB 5 HOH 25  1004 1004 HOH HOH K . 
FB 5 HOH 26  1033 1033 HOH HOH K . 
FB 5 HOH 27  1046 1046 HOH HOH K . 
FB 5 HOH 28  1053 1053 HOH HOH K . 
FB 5 HOH 29  1121 1121 HOH HOH K . 
FB 5 HOH 30  1133 1133 HOH HOH K . 
FB 5 HOH 31  1135 1135 HOH HOH K . 
FB 5 HOH 32  1201 1201 HOH HOH K . 
FB 5 HOH 33  1222 1222 HOH HOH K . 
FB 5 HOH 34  1226 1226 HOH HOH K . 
FB 5 HOH 35  1252 1252 HOH HOH K . 
FB 5 HOH 36  1255 1255 HOH HOH K . 
FB 5 HOH 37  1290 1290 HOH HOH K . 
FB 5 HOH 38  1295 1295 HOH HOH K . 
FB 5 HOH 39  1300 1300 HOH HOH K . 
FB 5 HOH 40  1330 1330 HOH HOH K . 
FB 5 HOH 41  1348 1348 HOH HOH K . 
FB 5 HOH 42  1365 1365 HOH HOH K . 
FB 5 HOH 43  1416 1416 HOH HOH K . 
FB 5 HOH 44  1422 1422 HOH HOH K . 
FB 5 HOH 45  1452 1452 HOH HOH K . 
FB 5 HOH 46  1486 1486 HOH HOH K . 
FB 5 HOH 47  1503 1503 HOH HOH K . 
FB 5 HOH 48  1520 1520 HOH HOH K . 
FB 5 HOH 49  1546 1546 HOH HOH K . 
FB 5 HOH 50  1552 1552 HOH HOH K . 
FB 5 HOH 51  1558 1558 HOH HOH K . 
FB 5 HOH 52  1561 1561 HOH HOH K . 
FB 5 HOH 53  1570 1570 HOH HOH K . 
FB 5 HOH 54  1574 1574 HOH HOH K . 
FB 5 HOH 55  1576 1576 HOH HOH K . 
FB 5 HOH 56  1606 1606 HOH HOH K . 
FB 5 HOH 57  1644 1644 HOH HOH K . 
FB 5 HOH 58  1651 1651 HOH HOH K . 
FB 5 HOH 59  1684 1684 HOH HOH K . 
FB 5 HOH 60  1735 1735 HOH HOH K . 
FB 5 HOH 61  1736 1736 HOH HOH K . 
FB 5 HOH 62  1737 1737 HOH HOH K . 
FB 5 HOH 63  1738 1738 HOH HOH K . 
FB 5 HOH 64  1739 1739 HOH HOH K . 
FB 5 HOH 65  1740 1740 HOH HOH K . 
GB 5 HOH 1   154  17   HOH HOH L . 
GB 5 HOH 2   155  21   HOH HOH L . 
GB 5 HOH 3   156  25   HOH HOH L . 
GB 5 HOH 4   157  52   HOH HOH L . 
GB 5 HOH 5   158  158  HOH HOH L . 
GB 5 HOH 6   159  68   HOH HOH L . 
GB 5 HOH 7   160  85   HOH HOH L . 
GB 5 HOH 8   161  90   HOH HOH L . 
GB 5 HOH 9   162  95   HOH HOH L . 
GB 5 HOH 10  163  134  HOH HOH L . 
GB 5 HOH 11  164  148  HOH HOH L . 
GB 5 HOH 12  168  168  HOH HOH L . 
GB 5 HOH 13  170  170  HOH HOH L . 
GB 5 HOH 14  173  173  HOH HOH L . 
GB 5 HOH 15  198  198  HOH HOH L . 
GB 5 HOH 16  199  199  HOH HOH L . 
GB 5 HOH 17  201  201  HOH HOH L . 
GB 5 HOH 18  220  220  HOH HOH L . 
GB 5 HOH 19  228  228  HOH HOH L . 
GB 5 HOH 20  238  238  HOH HOH L . 
GB 5 HOH 21  243  243  HOH HOH L . 
GB 5 HOH 22  250  250  HOH HOH L . 
GB 5 HOH 23  260  260  HOH HOH L . 
GB 5 HOH 24  266  266  HOH HOH L . 
GB 5 HOH 25  279  279  HOH HOH L . 
GB 5 HOH 26  289  289  HOH HOH L . 
GB 5 HOH 27  317  317  HOH HOH L . 
GB 5 HOH 28  322  322  HOH HOH L . 
GB 5 HOH 29  326  326  HOH HOH L . 
GB 5 HOH 30  332  332  HOH HOH L . 
GB 5 HOH 31  337  337  HOH HOH L . 
GB 5 HOH 32  351  351  HOH HOH L . 
GB 5 HOH 33  354  354  HOH HOH L . 
GB 5 HOH 34  386  386  HOH HOH L . 
GB 5 HOH 35  393  393  HOH HOH L . 
GB 5 HOH 36  402  402  HOH HOH L . 
GB 5 HOH 37  414  414  HOH HOH L . 
GB 5 HOH 38  423  423  HOH HOH L . 
GB 5 HOH 39  427  427  HOH HOH L . 
GB 5 HOH 40  436  436  HOH HOH L . 
GB 5 HOH 41  450  450  HOH HOH L . 
GB 5 HOH 42  477  477  HOH HOH L . 
GB 5 HOH 43  504  504  HOH HOH L . 
GB 5 HOH 44  512  512  HOH HOH L . 
GB 5 HOH 45  527  527  HOH HOH L . 
GB 5 HOH 46  538  538  HOH HOH L . 
GB 5 HOH 47  542  542  HOH HOH L . 
GB 5 HOH 48  550  550  HOH HOH L . 
GB 5 HOH 49  553  553  HOH HOH L . 
GB 5 HOH 50  586  586  HOH HOH L . 
GB 5 HOH 51  606  606  HOH HOH L . 
GB 5 HOH 52  617  617  HOH HOH L . 
GB 5 HOH 53  621  621  HOH HOH L . 
GB 5 HOH 54  632  632  HOH HOH L . 
GB 5 HOH 55  646  646  HOH HOH L . 
GB 5 HOH 56  653  653  HOH HOH L . 
GB 5 HOH 57  658  658  HOH HOH L . 
GB 5 HOH 58  659  659  HOH HOH L . 
GB 5 HOH 59  665  665  HOH HOH L . 
GB 5 HOH 60  676  676  HOH HOH L . 
GB 5 HOH 61  677  677  HOH HOH L . 
GB 5 HOH 62  681  681  HOH HOH L . 
GB 5 HOH 63  688  688  HOH HOH L . 
GB 5 HOH 64  690  690  HOH HOH L . 
GB 5 HOH 65  696  696  HOH HOH L . 
GB 5 HOH 66  709  709  HOH HOH L . 
GB 5 HOH 67  737  737  HOH HOH L . 
GB 5 HOH 68  741  741  HOH HOH L . 
GB 5 HOH 69  748  748  HOH HOH L . 
GB 5 HOH 70  762  762  HOH HOH L . 
GB 5 HOH 71  767  767  HOH HOH L . 
GB 5 HOH 72  778  778  HOH HOH L . 
GB 5 HOH 73  783  783  HOH HOH L . 
GB 5 HOH 74  785  785  HOH HOH L . 
GB 5 HOH 75  813  813  HOH HOH L . 
GB 5 HOH 76  829  829  HOH HOH L . 
GB 5 HOH 77  833  833  HOH HOH L . 
GB 5 HOH 78  836  836  HOH HOH L . 
GB 5 HOH 79  868  868  HOH HOH L . 
GB 5 HOH 80  877  877  HOH HOH L . 
GB 5 HOH 81  882  882  HOH HOH L . 
GB 5 HOH 82  919  919  HOH HOH L . 
GB 5 HOH 83  923  923  HOH HOH L . 
GB 5 HOH 84  925  925  HOH HOH L . 
GB 5 HOH 85  939  939  HOH HOH L . 
GB 5 HOH 86  942  942  HOH HOH L . 
GB 5 HOH 87  946  946  HOH HOH L . 
GB 5 HOH 88  956  956  HOH HOH L . 
GB 5 HOH 89  966  966  HOH HOH L . 
GB 5 HOH 90  1001 1001 HOH HOH L . 
GB 5 HOH 91  1019 1019 HOH HOH L . 
GB 5 HOH 92  1024 1024 HOH HOH L . 
GB 5 HOH 93  1037 1037 HOH HOH L . 
GB 5 HOH 94  1042 1042 HOH HOH L . 
GB 5 HOH 95  1052 1052 HOH HOH L . 
GB 5 HOH 96  1061 1061 HOH HOH L . 
GB 5 HOH 97  1069 1069 HOH HOH L . 
GB 5 HOH 98  1071 1071 HOH HOH L . 
GB 5 HOH 99  1089 1089 HOH HOH L . 
GB 5 HOH 100 1090 1090 HOH HOH L . 
GB 5 HOH 101 1124 1124 HOH HOH L . 
GB 5 HOH 102 1125 1125 HOH HOH L . 
GB 5 HOH 103 1128 1128 HOH HOH L . 
GB 5 HOH 104 1130 1130 HOH HOH L . 
GB 5 HOH 105 1143 1143 HOH HOH L . 
GB 5 HOH 106 1157 1157 HOH HOH L . 
GB 5 HOH 107 1160 1160 HOH HOH L . 
GB 5 HOH 108 1172 1172 HOH HOH L . 
GB 5 HOH 109 1174 1174 HOH HOH L . 
GB 5 HOH 110 1181 1181 HOH HOH L . 
GB 5 HOH 111 1184 1184 HOH HOH L . 
GB 5 HOH 112 1185 1185 HOH HOH L . 
GB 5 HOH 113 1191 1191 HOH HOH L . 
GB 5 HOH 114 1193 1193 HOH HOH L . 
GB 5 HOH 115 1204 1204 HOH HOH L . 
GB 5 HOH 116 1245 1245 HOH HOH L . 
GB 5 HOH 117 1254 1254 HOH HOH L . 
GB 5 HOH 118 1260 1260 HOH HOH L . 
GB 5 HOH 119 1263 1263 HOH HOH L . 
GB 5 HOH 120 1277 1277 HOH HOH L . 
GB 5 HOH 121 1291 1291 HOH HOH L . 
GB 5 HOH 122 1310 1310 HOH HOH L . 
GB 5 HOH 123 1323 1323 HOH HOH L . 
GB 5 HOH 124 1339 1339 HOH HOH L . 
GB 5 HOH 125 1345 1345 HOH HOH L . 
GB 5 HOH 126 1347 1347 HOH HOH L . 
GB 5 HOH 127 1350 1350 HOH HOH L . 
GB 5 HOH 128 1357 1357 HOH HOH L . 
GB 5 HOH 129 1364 1364 HOH HOH L . 
GB 5 HOH 130 1373 1373 HOH HOH L . 
GB 5 HOH 131 1395 1395 HOH HOH L . 
GB 5 HOH 132 1397 1397 HOH HOH L . 
GB 5 HOH 133 1446 1446 HOH HOH L . 
GB 5 HOH 134 1447 1447 HOH HOH L . 
GB 5 HOH 135 1449 1449 HOH HOH L . 
GB 5 HOH 136 1450 1450 HOH HOH L . 
GB 5 HOH 137 1453 1453 HOH HOH L . 
GB 5 HOH 138 1465 1465 HOH HOH L . 
GB 5 HOH 139 1468 1468 HOH HOH L . 
GB 5 HOH 140 1476 1476 HOH HOH L . 
GB 5 HOH 141 1478 1478 HOH HOH L . 
GB 5 HOH 142 1492 1492 HOH HOH L . 
GB 5 HOH 143 1493 1493 HOH HOH L . 
GB 5 HOH 144 1494 1494 HOH HOH L . 
GB 5 HOH 145 1496 1496 HOH HOH L . 
GB 5 HOH 146 1518 1518 HOH HOH L . 
GB 5 HOH 147 1527 1527 HOH HOH L . 
GB 5 HOH 148 1562 1562 HOH HOH L . 
GB 5 HOH 149 1563 1563 HOH HOH L . 
GB 5 HOH 150 1567 1567 HOH HOH L . 
GB 5 HOH 151 1572 1572 HOH HOH L . 
GB 5 HOH 152 1577 1577 HOH HOH L . 
GB 5 HOH 153 1578 1578 HOH HOH L . 
GB 5 HOH 154 1583 1583 HOH HOH L . 
GB 5 HOH 155 1585 1585 HOH HOH L . 
GB 5 HOH 156 1603 1603 HOH HOH L . 
GB 5 HOH 157 1616 1616 HOH HOH L . 
GB 5 HOH 158 1618 1618 HOH HOH L . 
GB 5 HOH 159 1638 1638 HOH HOH L . 
GB 5 HOH 160 1696 1696 HOH HOH L . 
GB 5 HOH 161 1702 1702 HOH HOH L . 
GB 5 HOH 162 1724 1724 HOH HOH L . 
GB 5 HOH 163 1741 1741 HOH HOH L . 
GB 5 HOH 164 1742 1742 HOH HOH L . 
GB 5 HOH 165 1743 1743 HOH HOH L . 
GB 5 HOH 166 1744 1744 HOH HOH L . 
HB 5 HOH 1   318  318  HOH HOH M . 
HB 5 HOH 2   319  400  HOH HOH M . 
HB 5 HOH 3   461  461  HOH HOH M . 
HB 5 HOH 4   480  480  HOH HOH M . 
HB 5 HOH 5   559  559  HOH HOH M . 
HB 5 HOH 6   661  661  HOH HOH M . 
HB 5 HOH 7   710  710  HOH HOH M . 
HB 5 HOH 8   755  755  HOH HOH M . 
HB 5 HOH 9   805  805  HOH HOH M . 
HB 5 HOH 10  854  854  HOH HOH M . 
HB 5 HOH 11  863  863  HOH HOH M . 
HB 5 HOH 12  864  864  HOH HOH M . 
HB 5 HOH 13  955  955  HOH HOH M . 
HB 5 HOH 14  985  985  HOH HOH M . 
HB 5 HOH 15  1080 1080 HOH HOH M . 
HB 5 HOH 16  1097 1097 HOH HOH M . 
HB 5 HOH 17  1103 1103 HOH HOH M . 
HB 5 HOH 18  1107 1107 HOH HOH M . 
HB 5 HOH 19  1366 1366 HOH HOH M . 
HB 5 HOH 20  1369 1369 HOH HOH M . 
HB 5 HOH 21  1381 1381 HOH HOH M . 
HB 5 HOH 22  1417 1417 HOH HOH M . 
HB 5 HOH 23  1418 1418 HOH HOH M . 
HB 5 HOH 24  1537 1537 HOH HOH M . 
HB 5 HOH 25  1596 1596 HOH HOH M . 
HB 5 HOH 26  1667 1667 HOH HOH M . 
HB 5 HOH 27  1691 1691 HOH HOH M . 
HB 5 HOH 28  1693 1693 HOH HOH M . 
# 
