data_1PU0
# 
_entry.id   1PU0 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.286 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   1PU0         
RCSB  RCSB019562   
WWPDB D_1000019562 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.db_id          1PTZ 
_pdbx_database_related.details        
'Crystal structure of the human C,Zn Superoxide Dismutase, Familial Amyotrophic Lateral Sclerosis (FALS) Mutant H43R.' 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1PU0 
_pdbx_database_status.recvd_initial_deposition_date   2003-06-23 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'DiDonato, M.'    1  
'Craig, L.'       2  
'Huff, M.E.'      3  
'Thayer, M.M.'    4  
'Cardoso, R.M.F.' 5  
'Kassmann, C.J.'  6  
'Lo, T.P.'        7  
'Bruns, C.K.'     8  
'Powers, E.T.'    9  
'Kelly, J.W.'     10 
'Getzoff, E.D.'   11 
'Tainer, J.A.'    12 
# 
_citation.id                        primary 
_citation.title                     
'ALS Mutants of Human Superoxide Dismutase Form Fibrous Aggregates Via Framework Destabilization' 
_citation.journal_abbrev            J.Mol.Biol. 
_citation.journal_volume            332 
_citation.page_first                601 
_citation.page_last                 615 
_citation.year                      2003 
_citation.journal_id_ASTM           JMOBAK 
_citation.country                   UK 
_citation.journal_id_ISSN           0022-2836 
_citation.journal_id_CSD            0070 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   12963370 
_citation.pdbx_database_id_DOI      '10.1016/S0022-2836(03)00889-1' 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'DiDonato, M.'    1  
primary 'Craig, L.'       2  
primary 'Huff, M.E.'      3  
primary 'Thayer, M.M.'    4  
primary 'Cardoso, R.M.F.' 5  
primary 'Kassmann, C.J.'  6  
primary 'Lo, T.P.'        7  
primary 'Bruns, C.K.'     8  
primary 'Powers, E.T.'    9  
primary 'Kelly, J.W.'     10 
primary 'Getzoff, E.D.'   11 
primary 'Tainer, J.A.'    12 
# 
_cell.entry_id           1PU0 
_cell.length_a           203.580 
_cell.length_b           165.680 
_cell.length_c           144.150 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              80 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1PU0 
_symmetry.space_group_name_H-M             'C 2 2 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                20 
# 
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]' 15827.561 10   1.15.1.1 ? ? ? 
2 non-polymer syn 'COPPER (I) ION'               63.546    10   ?        ? ? ? 
3 non-polymer syn 'ZINC ION'                     65.409    10   ?        ? ? ? 
4 non-polymer syn 'SULFATE ION'                  96.063    3    ?        ? ? ? 
5 water       nat water                          18.015    1047 ?        ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D,E,F,G,H,I,J 
_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 CYS 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                     Homo 
_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                     Escherichia 
_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          ? 
_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           1 
_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 1PU0 A 1 ? 153 ? P00441 1 ? 153 ? 1 153 
2  1 1PU0 B 1 ? 153 ? P00441 1 ? 153 ? 1 153 
3  1 1PU0 C 1 ? 153 ? P00441 1 ? 153 ? 1 153 
4  1 1PU0 D 1 ? 153 ? P00441 1 ? 153 ? 1 153 
5  1 1PU0 E 1 ? 153 ? P00441 1 ? 153 ? 1 153 
6  1 1PU0 F 1 ? 153 ? P00441 1 ? 153 ? 1 153 
7  1 1PU0 G 1 ? 153 ? P00441 1 ? 153 ? 1 153 
8  1 1PU0 H 1 ? 153 ? P00441 1 ? 153 ? 1 153 
9  1 1PU0 I 1 ? 153 ? P00441 1 ? 153 ? 1 153 
10 1 1PU0 J 1 ? 153 ? P00441 1 ? 153 ? 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 
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          1PU0 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      3.28 
_exptl_crystal.density_percent_sol   67.96 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.temp            298 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.pdbx_details    'ammonium sulphate, sodium chloride, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 298K' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           96 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   1999-03-17 
_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                    GRAPHITE 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.08 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SSRL BEAMLINE BL7-1' 
_diffrn_source.pdbx_synchrotron_site       SSRL 
_diffrn_source.pdbx_synchrotron_beamline   BL7-1 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.08 
# 
_reflns.entry_id                     1PU0 
_reflns.observed_criterion_sigma_I   -3 
_reflns.observed_criterion_sigma_F   0 
_reflns.d_resolution_low             30 
_reflns.d_resolution_high            1.70 
_reflns.number_obs                   262366 
_reflns.number_all                   262366 
_reflns.percent_possible_obs         99.5 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.061 
_reflns.pdbx_netI_over_sigmaI        ? 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              ? 
_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_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.70 
_reflns_shell.d_res_low              1.76 
_reflns_shell.percent_possible_all   99.2 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.32 
_reflns_shell.meanI_over_sigI_obs    ? 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1PU0 
_refine.ls_number_reflns_obs                     262366 
_refine.ls_number_reflns_all                     262366 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_d_res_low                             30.00 
_refine.ls_d_res_high                            1.70 
_refine.ls_percent_reflns_obs                    93.6 
_refine.ls_R_factor_obs                          0.2102 
_refine.ls_R_factor_all                          0.2114 
_refine.ls_R_factor_R_work                       0.2102 
_refine.ls_R_factor_R_free                       0.2432 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.3 
_refine.ls_number_reflns_R_free                  13096 
_refine.ls_number_parameters                     49294 
_refine.ls_number_restraints                     45691 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_ls_cross_valid_method               'FREE R' 
_refine.details                                  ? 
_refine.pdbx_starting_model                      1SOS 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'Engh & Huber' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_SU_ML                            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        1PU0 
_refine_analyze.Luzzati_coordinate_error_obs    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      20 
_refine_analyze.occupancy_sum_hydrogen          0.00 
_refine_analyze.occupancy_sum_non_hydrogen      12181.50 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        11140 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         35 
_refine_hist.number_atoms_solvent             1047 
_refine_hist.number_atoms_total               12222 
_refine_hist.d_res_high                       1.70 
_refine_hist.d_res_low                        30.00 
# 
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_refine_id 
_refine_ls_restr.pdbx_restraint_function 
s_bond_d               0.020  ? ? ? 'X-RAY DIFFRACTION' ? 
s_angle_d              0.025  ? ? ? 'X-RAY DIFFRACTION' ? 
s_similar_dist         0.000  ? ? ? 'X-RAY DIFFRACTION' ? 
s_from_restr_planes    0.0289 ? ? ? 'X-RAY DIFFRACTION' ? 
s_zero_chiral_vol      0.041  ? ? ? 'X-RAY DIFFRACTION' ? 
s_non_zero_chiral_vol  0.053  ? ? ? 'X-RAY DIFFRACTION' ? 
s_anti_bump_dis_restr  0.014  ? ? ? 'X-RAY DIFFRACTION' ? 
s_rigid_bond_adp_cmpnt 0.003  ? ? ? 'X-RAY DIFFRACTION' ? 
s_similar_adp_cmpnt    0.084  ? ? ? 'X-RAY DIFFRACTION' ? 
s_approx_iso_adps      0.000  ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_pdbx_refine.entry_id                                    1PU0 
_pdbx_refine.R_factor_all_no_cutoff                      0.2114 
_pdbx_refine.R_factor_obs_no_cutoff                      0.2102 
_pdbx_refine.free_R_factor_no_cutoff                     0.2432 
_pdbx_refine.free_R_val_test_set_size_perc_no_cutoff     5.3 
_pdbx_refine.free_R_val_test_set_ct_no_cutoff            13096 
_pdbx_refine.R_factor_all_4sig_cutoff                    0.2024 
_pdbx_refine.R_factor_obs_4sig_cutoff                    0.2015 
_pdbx_refine.free_R_factor_4sig_cutoff                   0.2332 
_pdbx_refine.free_R_val_test_set_size_perc_4sig_cutoff   5.3 
_pdbx_refine.free_R_val_test_set_ct_4sig_cutoff          11627 
_pdbx_refine.number_reflns_obs_4sig_cutoff               221399 
_pdbx_refine.number_reflns_obs_no_cutoff                 ? 
_pdbx_refine.pdbx_refine_id                              'X-RAY DIFFRACTION' 
_pdbx_refine.free_R_error_no_cutoff                      ? 
# 
_struct.entry_id                  1PU0 
_struct.title                     'Structure of Human Cu,Zn Superoxide Dismutase' 
_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        1PU0 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            
;ALS, FALS, Lou Gehrig's disease, 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 2 ? 
L  N N 3 ? 
M  N N 2 ? 
N  N N 3 ? 
O  N N 4 ? 
P  N N 2 ? 
Q  N N 3 ? 
R  N N 2 ? 
S  N N 3 ? 
T  N N 2 ? 
U  N N 3 ? 
V  N N 2 ? 
W  N N 3 ? 
X  N N 2 ? 
Y  N N 3 ? 
Z  N N 2 ? 
AA N N 3 ? 
BA N N 2 ? 
CA N N 3 ? 
DA N N 2 ? 
EA N N 3 ? 
FA N N 4 ? 
GA N N 4 ? 
HA N N 5 ? 
IA N N 5 ? 
JA N N 5 ? 
KA N N 5 ? 
LA N N 5 ? 
MA N N 5 ? 
NA N N 5 ? 
OA N N 5 ? 
PA N N 5 ? 
QA N N 5 ? 
# 
loop_
_struct_biol.id 
_struct_biol.details 
_struct_biol.pdbx_parent_biol_id 
1 'The biological assembly is a homodimer. The asymmetric unit contain 5 homodimers.' ? 
2 ?                                                                                   ? 
3 ?                                                                                   ? 
4 ?                                                                                   ? 
5 ?                                                                                   ? 
# 
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  GLU A 133 ? GLY A 138 ? GLU A 133 GLY A 138 1 ? 6 
HELX_P HELX_P3  3  ALA B 55  ? GLY B 61  ? ALA B 55  GLY B 61  5 ? 7 
HELX_P HELX_P4  4  GLU B 133 ? GLY B 138 ? GLU B 133 GLY B 138 1 ? 6 
HELX_P HELX_P5  5  ALA C 55  ? GLY C 61  ? ALA C 55  GLY C 61  5 ? 7 
HELX_P HELX_P6  6  ASN C 131 ? THR C 137 ? ASN C 131 THR C 137 1 ? 7 
HELX_P HELX_P7  7  ALA D 55  ? GLY D 61  ? ALA D 55  GLY D 61  5 ? 7 
HELX_P HELX_P8  8  SER D 107 ? CYS D 111 ? SER D 107 CYS D 111 5 ? 5 
HELX_P HELX_P9  9  GLU D 133 ? GLY D 138 ? GLU D 133 GLY D 138 1 ? 6 
HELX_P HELX_P10 10 ALA E 55  ? GLY E 61  ? ALA E 55  GLY E 61  5 ? 7 
HELX_P HELX_P11 11 GLU E 133 ? GLY E 138 ? GLU E 133 GLY E 138 1 ? 6 
HELX_P HELX_P12 12 ALA F 55  ? GLY F 61  ? ALA F 55  GLY F 61  5 ? 7 
HELX_P HELX_P13 13 GLU F 133 ? GLY F 138 ? GLU F 133 GLY F 138 1 ? 6 
HELX_P HELX_P14 14 ALA G 55  ? GLY G 61  ? ALA G 55  GLY G 61  5 ? 7 
HELX_P HELX_P15 15 GLU G 133 ? GLY G 138 ? GLU G 133 GLY G 138 1 ? 6 
HELX_P HELX_P16 16 ALA H 55  ? GLY H 61  ? ALA H 55  GLY H 61  5 ? 7 
HELX_P HELX_P17 17 GLU H 133 ? GLY H 138 ? GLU H 133 GLY H 138 1 ? 6 
HELX_P HELX_P18 18 ALA I 55  ? GLY I 61  ? ALA I 55  GLY I 61  5 ? 7 
HELX_P HELX_P19 19 ASN I 131 ? GLY I 138 ? ASN I 131 GLY I 138 1 ? 8 
HELX_P HELX_P20 20 ALA J 55  ? GLY J 61  ? ALA J 55  GLY J 61  5 ? 7 
HELX_P HELX_P21 21 GLU J 133 ? GLY J 138 ? GLU J 133 GLY J 138 1 ? 6 
# 
_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 A ? ? 1_555 A CYS 146 SG  A ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.048 ? 
disulf2  disulf ? ? A  CYS 57 SG B ? ? 1_555 A CYS 146 SG  B ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.677 ? 
disulf3  disulf ? ? B  CYS 57 SG A ? ? 1_555 B CYS 146 SG  A ? B CYS 57  B CYS 146 1_555 ? ? ? ? ? ? ? 2.039 ? 
disulf4  disulf ? ? B  CYS 57 SG B ? ? 1_555 B CYS 146 SG  B ? B CYS 57  B CYS 146 1_555 ? ? ? ? ? ? ? 2.667 ? 
disulf5  disulf ? ? C  CYS 57 SG A ? ? 1_555 C CYS 146 SG  A ? C CYS 57  C CYS 146 1_555 ? ? ? ? ? ? ? 2.045 ? 
disulf6  disulf ? ? C  CYS 57 SG B ? ? 1_555 C CYS 146 SG  B ? C CYS 57  C CYS 146 1_555 ? ? ? ? ? ? ? 2.669 ? 
disulf7  disulf ? ? D  CYS 57 SG A ? ? 1_555 D CYS 146 SG  A ? D CYS 57  D CYS 146 1_555 ? ? ? ? ? ? ? 2.046 ? 
disulf8  disulf ? ? D  CYS 57 SG B ? ? 1_555 D CYS 146 SG  B ? D CYS 57  D CYS 146 1_555 ? ? ? ? ? ? ? 2.672 ? 
disulf9  disulf ? ? E  CYS 57 SG A ? ? 1_555 E CYS 146 SG  A ? E CYS 57  E CYS 146 1_555 ? ? ? ? ? ? ? 2.051 ? 
disulf10 disulf ? ? E  CYS 57 SG B ? ? 1_555 E CYS 146 SG  B ? E CYS 57  E CYS 146 1_555 ? ? ? ? ? ? ? 2.675 ? 
disulf11 disulf ? ? F  CYS 57 SG A ? ? 1_555 F CYS 146 SG  A ? F CYS 57  F CYS 146 1_555 ? ? ? ? ? ? ? 2.035 ? 
disulf12 disulf ? ? F  CYS 57 SG B ? ? 1_555 F CYS 146 SG  B ? F CYS 57  F CYS 146 1_555 ? ? ? ? ? ? ? 2.661 ? 
disulf13 disulf ? ? G  CYS 57 SG A ? ? 1_555 G CYS 146 SG  A ? G CYS 57  G CYS 146 1_555 ? ? ? ? ? ? ? 2.043 ? 
disulf14 disulf ? ? G  CYS 57 SG B ? ? 1_555 G CYS 146 SG  B ? G CYS 57  G CYS 146 1_555 ? ? ? ? ? ? ? 2.674 ? 
disulf15 disulf ? ? H  CYS 57 SG A ? ? 1_555 H CYS 146 SG  A ? H CYS 57  H CYS 146 1_555 ? ? ? ? ? ? ? 2.050 ? 
disulf16 disulf ? ? H  CYS 57 SG B ? ? 1_555 H CYS 146 SG  B ? H CYS 57  H CYS 146 1_555 ? ? ? ? ? ? ? 2.674 ? 
disulf17 disulf ? ? I  CYS 57 SG A ? ? 1_555 I CYS 146 SG  A ? I CYS 57  I CYS 146 1_555 ? ? ? ? ? ? ? 2.042 ? 
disulf18 disulf ? ? I  CYS 57 SG B ? ? 1_555 I CYS 146 SG  B ? I CYS 57  I CYS 146 1_555 ? ? ? ? ? ? ? 2.672 ? 
disulf19 disulf ? ? J  CYS 57 SG A ? ? 1_555 J CYS 146 SG  A ? J CYS 57  J CYS 146 1_555 ? ? ? ? ? ? ? 2.038 ? 
disulf20 disulf ? ? J  CYS 57 SG B ? ? 1_555 J CYS 146 SG  B ? J CYS 57  J CYS 146 1_555 ? ? ? ? ? ? ? 2.668 ? 
metalc1  metalc ? ? L  ZN  .  ZN ? ? ? 1_555 A ASP 83  OD1 ? ? A ZN  201 A ASP 83  1_555 ? ? ? ? ? ? ? 1.985 ? 
metalc2  metalc ? ? L  ZN  .  ZN ? ? ? 1_555 A HIS 63  ND1 ? ? A ZN  201 A HIS 63  1_555 ? ? ? ? ? ? ? 1.991 ? 
metalc3  metalc ? ? L  ZN  .  ZN ? ? ? 1_555 A HIS 71  ND1 ? ? A ZN  201 A HIS 71  1_555 ? ? ? ? ? ? ? 2.051 ? 
metalc4  metalc ? ? L  ZN  .  ZN ? ? ? 1_555 A HIS 80  ND1 ? ? A ZN  201 A HIS 80  1_555 ? ? ? ? ? ? ? 2.079 ? 
metalc5  metalc ? ? K  CU1 .  CU ? ? ? 1_555 A HIS 46  ND1 ? ? A CU1 200 A HIS 46  1_555 ? ? ? ? ? ? ? 2.076 ? 
metalc6  metalc ? ? K  CU1 .  CU ? ? ? 1_555 A HIS 48  NE2 ? ? A CU1 200 A HIS 48  1_555 ? ? ? ? ? ? ? 2.028 ? 
metalc7  metalc ? ? K  CU1 .  CU ? ? ? 1_555 A HIS 120 NE2 ? ? A CU1 200 A HIS 120 1_555 ? ? ? ? ? ? ? 2.060 ? 
metalc8  metalc ? ? N  ZN  .  ZN ? ? ? 1_555 B ASP 83  OD1 ? ? B ZN  201 B ASP 83  1_555 ? ? ? ? ? ? ? 1.931 ? 
metalc9  metalc ? ? N  ZN  .  ZN ? ? ? 1_555 B HIS 63  ND1 ? ? B ZN  201 B HIS 63  1_555 ? ? ? ? ? ? ? 2.028 ? 
metalc10 metalc ? ? N  ZN  .  ZN ? ? ? 1_555 B HIS 71  ND1 ? ? B ZN  201 B HIS 71  1_555 ? ? ? ? ? ? ? 2.023 ? 
metalc11 metalc ? ? N  ZN  .  ZN ? ? ? 1_555 B HIS 80  ND1 ? ? B ZN  201 B HIS 80  1_555 ? ? ? ? ? ? ? 2.064 ? 
metalc12 metalc ? ? M  CU1 .  CU ? ? ? 1_555 B HIS 46  ND1 ? ? B CU1 200 B HIS 46  1_555 ? ? ? ? ? ? ? 2.031 ? 
metalc13 metalc ? ? M  CU1 .  CU ? ? ? 1_555 B HIS 48  NE2 ? ? B CU1 200 B HIS 48  1_555 ? ? ? ? ? ? ? 1.995 ? 
metalc14 metalc ? ? M  CU1 .  CU ? ? ? 1_555 B HIS 120 NE2 ? ? B CU1 200 B HIS 120 1_555 ? ? ? ? ? ? ? 2.038 ? 
metalc15 metalc ? ? Q  ZN  .  ZN ? ? ? 1_555 C ASP 83  OD1 ? ? C ZN  201 C ASP 83  1_555 ? ? ? ? ? ? ? 1.985 ? 
metalc16 metalc ? ? Q  ZN  .  ZN ? ? ? 1_555 C HIS 63  ND1 ? ? C ZN  201 C HIS 63  1_555 ? ? ? ? ? ? ? 2.215 ? 
metalc17 metalc ? ? Q  ZN  .  ZN ? ? ? 1_555 C HIS 71  ND1 ? ? C ZN  201 C HIS 71  1_555 ? ? ? ? ? ? ? 2.025 ? 
metalc18 metalc ? ? Q  ZN  .  ZN ? ? ? 1_555 C HIS 80  ND1 ? ? C ZN  201 C HIS 80  1_555 ? ? ? ? ? ? ? 1.951 ? 
metalc19 metalc ? ? P  CU1 .  CU ? ? ? 1_555 C HIS 46  ND1 ? ? C CU1 200 C HIS 46  1_555 ? ? ? ? ? ? ? 2.046 ? 
metalc20 metalc ? ? P  CU1 .  CU ? ? ? 1_555 C HIS 48  NE2 ? ? C CU1 200 C HIS 48  1_555 ? ? ? ? ? ? ? 1.968 ? 
metalc21 metalc ? ? P  CU1 .  CU ? ? ? 1_555 C HIS 120 NE2 ? ? C CU1 200 C HIS 120 1_555 ? ? ? ? ? ? ? 1.960 ? 
metalc22 metalc ? ? S  ZN  .  ZN ? ? ? 1_555 D ASP 83  OD1 ? ? D ZN  201 D ASP 83  1_555 ? ? ? ? ? ? ? 1.897 ? 
metalc23 metalc ? ? S  ZN  .  ZN ? ? ? 1_555 D HIS 63  ND1 ? ? D ZN  201 D HIS 63  1_555 ? ? ? ? ? ? ? 1.957 ? 
metalc24 metalc ? ? S  ZN  .  ZN ? ? ? 1_555 D HIS 71  ND1 ? ? D ZN  201 D HIS 71  1_555 ? ? ? ? ? ? ? 2.034 ? 
metalc25 metalc ? ? S  ZN  .  ZN ? ? ? 1_555 D HIS 80  ND1 ? ? D ZN  201 D HIS 80  1_555 ? ? ? ? ? ? ? 2.028 ? 
metalc26 metalc ? ? R  CU1 .  CU ? ? ? 1_555 D HIS 46  ND1 ? ? D CU1 200 D HIS 46  1_555 ? ? ? ? ? ? ? 2.025 ? 
metalc27 metalc ? ? R  CU1 .  CU ? ? ? 1_555 D HIS 48  NE2 ? ? D CU1 200 D HIS 48  1_555 ? ? ? ? ? ? ? 2.000 ? 
metalc28 metalc ? ? R  CU1 .  CU ? ? ? 1_555 D HIS 120 NE2 ? ? D CU1 200 D HIS 120 1_555 ? ? ? ? ? ? ? 2.012 ? 
metalc29 metalc ? ? U  ZN  .  ZN ? ? ? 1_555 E ASP 83  OD1 ? ? E ZN  201 E ASP 83  1_555 ? ? ? ? ? ? ? 1.970 ? 
metalc30 metalc ? ? U  ZN  .  ZN ? ? ? 1_555 E HIS 63  ND1 ? ? E ZN  201 E HIS 63  1_555 ? ? ? ? ? ? ? 2.069 ? 
metalc31 metalc ? ? U  ZN  .  ZN ? ? ? 1_555 E HIS 71  ND1 ? ? E ZN  201 E HIS 71  1_555 ? ? ? ? ? ? ? 2.081 ? 
metalc32 metalc ? ? U  ZN  .  ZN ? ? ? 1_555 E HIS 80  ND1 ? ? E ZN  201 E HIS 80  1_555 ? ? ? ? ? ? ? 2.004 ? 
metalc33 metalc ? ? T  CU1 .  CU ? ? ? 1_555 E HIS 46  ND1 ? ? E CU1 200 E HIS 46  1_555 ? ? ? ? ? ? ? 2.014 ? 
metalc34 metalc ? ? T  CU1 .  CU ? ? ? 1_555 E HIS 48  NE2 ? ? E CU1 200 E HIS 48  1_555 ? ? ? ? ? ? ? 1.974 ? 
metalc35 metalc ? ? T  CU1 .  CU ? ? ? 1_555 E HIS 120 NE2 ? ? E CU1 200 E HIS 120 1_555 ? ? ? ? ? ? ? 2.029 ? 
metalc36 metalc ? ? W  ZN  .  ZN ? ? ? 1_555 F ASP 83  OD1 ? ? F ZN  201 F ASP 83  1_555 ? ? ? ? ? ? ? 1.970 ? 
metalc37 metalc ? ? W  ZN  .  ZN ? ? ? 1_555 F HIS 63  ND1 ? ? F ZN  201 F HIS 63  1_555 ? ? ? ? ? ? ? 1.960 ? 
metalc38 metalc ? ? W  ZN  .  ZN ? ? ? 1_555 F HIS 71  ND1 ? ? F ZN  201 F HIS 71  1_555 ? ? ? ? ? ? ? 2.044 ? 
metalc39 metalc ? ? W  ZN  .  ZN ? ? ? 1_555 F HIS 80  ND1 ? ? F ZN  201 F HIS 80  1_555 ? ? ? ? ? ? ? 2.000 ? 
metalc40 metalc ? ? V  CU1 .  CU ? ? ? 1_555 F HIS 46  ND1 ? ? F CU1 200 F HIS 46  1_555 ? ? ? ? ? ? ? 2.077 ? 
metalc41 metalc ? ? V  CU1 .  CU ? ? ? 1_555 F HIS 48  NE2 ? ? F CU1 200 F HIS 48  1_555 ? ? ? ? ? ? ? 1.980 ? 
metalc42 metalc ? ? V  CU1 .  CU ? ? ? 1_555 F HIS 120 NE2 ? ? F CU1 200 F HIS 120 1_555 ? ? ? ? ? ? ? 1.995 ? 
metalc43 metalc ? ? Y  ZN  .  ZN ? ? ? 1_555 G ASP 83  OD1 ? ? G ZN  201 G ASP 83  1_555 ? ? ? ? ? ? ? 1.879 ? 
metalc44 metalc ? ? Y  ZN  .  ZN ? ? ? 1_555 G HIS 63  ND1 ? ? G ZN  201 G HIS 63  1_555 ? ? ? ? ? ? ? 2.005 ? 
metalc45 metalc ? ? Y  ZN  .  ZN ? ? ? 1_555 G HIS 71  ND1 ? ? G ZN  201 G HIS 71  1_555 ? ? ? ? ? ? ? 2.058 ? 
metalc46 metalc ? ? Y  ZN  .  ZN ? ? ? 1_555 G HIS 80  ND1 ? ? G ZN  201 G HIS 80  1_555 ? ? ? ? ? ? ? 1.953 ? 
metalc47 metalc ? ? X  CU1 .  CU ? ? ? 1_555 G HIS 46  ND1 ? ? G CU1 200 G HIS 46  1_555 ? ? ? ? ? ? ? 1.946 ? 
metalc48 metalc ? ? X  CU1 .  CU ? ? ? 1_555 G HIS 48  NE2 ? ? G CU1 200 G HIS 48  1_555 ? ? ? ? ? ? ? 2.104 ? 
metalc49 metalc ? ? X  CU1 .  CU ? ? ? 1_555 G HIS 120 NE2 ? ? G CU1 200 G HIS 120 1_555 ? ? ? ? ? ? ? 1.964 ? 
metalc50 metalc ? ? AA ZN  .  ZN ? ? ? 1_555 H ASP 83  OD1 ? ? H ZN  201 H ASP 83  1_555 ? ? ? ? ? ? ? 1.919 ? 
metalc51 metalc ? ? AA ZN  .  ZN ? ? ? 1_555 H HIS 63  ND1 ? ? H ZN  201 H HIS 63  1_555 ? ? ? ? ? ? ? 2.021 ? 
metalc52 metalc ? ? AA ZN  .  ZN ? ? ? 1_555 H HIS 71  ND1 ? ? H ZN  201 H HIS 71  1_555 ? ? ? ? ? ? ? 2.006 ? 
metalc53 metalc ? ? AA ZN  .  ZN ? ? ? 1_555 H HIS 80  ND1 ? ? H ZN  201 H HIS 80  1_555 ? ? ? ? ? ? ? 2.065 ? 
metalc54 metalc ? ? Z  CU1 .  CU ? ? ? 1_555 H HIS 46  ND1 ? ? H CU1 200 H HIS 46  1_555 ? ? ? ? ? ? ? 1.989 ? 
metalc55 metalc ? ? Z  CU1 .  CU ? ? ? 1_555 H HIS 48  NE2 ? ? H CU1 200 H HIS 48  1_555 ? ? ? ? ? ? ? 2.006 ? 
metalc56 metalc ? ? Z  CU1 .  CU ? ? ? 1_555 H HIS 120 NE2 ? ? H CU1 200 H HIS 120 1_555 ? ? ? ? ? ? ? 2.017 ? 
metalc57 metalc ? ? CA ZN  .  ZN ? ? ? 1_555 I ASP 83  OD1 ? ? I ZN  201 I ASP 83  1_555 ? ? ? ? ? ? ? 1.913 ? 
metalc58 metalc ? ? CA ZN  .  ZN ? ? ? 1_555 I HIS 63  ND1 ? ? I ZN  201 I HIS 63  1_555 ? ? ? ? ? ? ? 2.057 ? 
metalc59 metalc ? ? CA ZN  .  ZN ? ? ? 1_555 I HIS 71  ND1 ? ? I ZN  201 I HIS 71  1_555 ? ? ? ? ? ? ? 2.015 ? 
metalc60 metalc ? ? CA ZN  .  ZN ? ? ? 1_555 I HIS 80  ND1 ? ? I ZN  201 I HIS 80  1_555 ? ? ? ? ? ? ? 2.048 ? 
metalc61 metalc ? ? BA CU1 .  CU ? ? ? 1_555 I HIS 46  ND1 ? ? I CU1 200 I HIS 46  1_555 ? ? ? ? ? ? ? 2.016 ? 
metalc62 metalc ? ? BA CU1 .  CU ? ? ? 1_555 I HIS 48  NE2 ? ? I CU1 200 I HIS 48  1_555 ? ? ? ? ? ? ? 2.037 ? 
metalc63 metalc ? ? BA CU1 .  CU ? ? ? 1_555 I HIS 120 NE2 ? ? I CU1 200 I HIS 120 1_555 ? ? ? ? ? ? ? 1.992 ? 
metalc64 metalc ? ? EA ZN  .  ZN ? ? ? 1_555 J ASP 83  OD1 ? ? J ZN  201 J ASP 83  1_555 ? ? ? ? ? ? ? 1.952 ? 
metalc65 metalc ? ? EA ZN  .  ZN ? ? ? 1_555 J HIS 63  ND1 ? ? J ZN  201 J HIS 63  1_555 ? ? ? ? ? ? ? 2.007 ? 
metalc66 metalc ? ? EA ZN  .  ZN ? ? ? 1_555 J HIS 71  ND1 ? ? J ZN  201 J HIS 71  1_555 ? ? ? ? ? ? ? 2.069 ? 
metalc67 metalc ? ? EA ZN  .  ZN ? ? ? 1_555 J HIS 80  ND1 ? ? J ZN  201 J HIS 80  1_555 ? ? ? ? ? ? ? 2.019 ? 
metalc68 metalc ? ? DA CU1 .  CU ? ? ? 1_555 J HIS 46  ND1 ? ? J CU1 200 J HIS 46  1_555 ? ? ? ? ? ? ? 2.108 ? 
metalc69 metalc ? ? DA CU1 .  CU ? ? ? 1_555 J HIS 48  NE2 ? ? J CU1 200 J HIS 48  1_555 ? ? ? ? ? ? ? 1.981 ? 
metalc70 metalc ? ? DA CU1 .  CU ? ? ? 1_555 J HIS 120 NE2 ? ? J CU1 200 J HIS 120 1_555 ? ? ? ? ? ? ? 2.070 ? 
metalc71 metalc ? ? L  ZN  .  ZN ? ? ? 1_555 A ASP 83  OD2 ? ? A ZN  201 A ASP 83  1_555 ? ? ? ? ? ? ? 2.736 ? 
metalc72 metalc ? ? Q  ZN  .  ZN ? ? ? 1_555 C ASP 83  OD2 ? ? C ZN  201 C ASP 83  1_555 ? ? ? ? ? ? ? 2.575 ? 
metalc73 metalc ? ? Y  ZN  .  ZN ? ? ? 1_555 G ASP 83  OD2 ? ? G ZN  201 G ASP 83  1_555 ? ? ? ? ? ? ? 2.754 ? 
metalc74 metalc ? ? CA ZN  .  ZN ? ? ? 1_555 I ASP 83  OD2 ? ? I ZN  201 I ASP 83  1_555 ? ? ? ? ? ? ? 2.610 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
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 ? 
# 
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 
# 
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   ? LEU B 8   ? THR B 2   LEU B 8   
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 C 95  ASP C 101 
E 2 VAL C 29  ? LYS C 36  ? VAL C 29  LYS C 36  
E 3 GLN C 15  ? GLN C 22  ? GLN C 15  GLN C 22  
E 4 THR C 2   ? LEU C 8   ? THR C 2   LEU C 8   
E 5 GLY C 150 ? ILE C 151 ? GLY C 150 ILE C 151 
F 1 ASP C 83  ? ALA C 89  ? ASP C 83  ALA C 89  
F 2 GLY C 41  ? HIS C 48  ? GLY C 41  HIS C 48  
F 3 THR C 116 ? HIS C 120 ? THR C 116 HIS C 120 
F 4 ARG C 143 ? VAL C 148 ? ARG C 143 VAL C 148 
G 1 ALA D 95  ? ASP D 101 ? ALA D 95  ASP D 101 
G 2 VAL D 29  ? LYS D 36  ? VAL D 29  LYS D 36  
G 3 GLN D 15  ? GLU D 21  ? GLN D 15  GLU D 21  
G 4 LYS D 3   ? LEU D 8   ? LYS D 3   LEU D 8   
G 5 GLY D 150 ? ILE D 151 ? GLY D 150 ILE D 151 
H 1 ASP D 83  ? ALA D 89  ? ASP D 83  ALA D 89  
H 2 GLY D 41  ? HIS D 48  ? GLY D 41  HIS D 48  
H 3 THR D 116 ? HIS D 120 ? THR D 116 HIS D 120 
H 4 ARG D 143 ? VAL D 148 ? ARG D 143 VAL D 148 
I 1 ALA E 95  ? ASP E 101 ? ALA E 95  ASP E 101 
I 2 VAL E 29  ? LYS E 36  ? VAL E 29  LYS E 36  
I 3 GLN E 15  ? GLN E 22  ? GLN E 15  GLN E 22  
I 4 THR E 2   ? LYS E 9   ? THR E 2   LYS E 9   
I 5 GLY E 150 ? ILE E 151 ? GLY E 150 ILE E 151 
J 1 ASP E 83  ? ALA E 89  ? ASP E 83  ALA E 89  
J 2 GLY E 41  ? HIS E 48  ? GLY E 41  HIS E 48  
J 3 THR E 116 ? HIS E 120 ? THR E 116 HIS E 120 
J 4 ARG E 143 ? VAL E 148 ? ARG E 143 VAL E 148 
K 1 ALA F 95  ? ASP F 101 ? ALA F 95  ASP F 101 
K 2 VAL F 29  ? LYS F 36  ? VAL F 29  LYS F 36  
K 3 GLN F 15  ? GLN F 22  ? GLN F 15  GLN F 22  
K 4 THR F 2   ? LEU F 8   ? THR F 2   LEU F 8   
K 5 GLY F 150 ? ILE F 151 ? GLY F 150 ILE F 151 
L 1 ASP F 83  ? ALA F 89  ? ASP F 83  ALA F 89  
L 2 GLY F 41  ? HIS F 48  ? GLY F 41  HIS F 48  
L 3 THR F 116 ? HIS F 120 ? THR F 116 HIS F 120 
L 4 ARG F 143 ? VAL F 148 ? ARG F 143 VAL F 148 
M 1 ALA G 95  ? ASP G 101 ? ALA G 95  ASP G 101 
M 2 VAL G 29  ? LYS G 36  ? VAL G 29  LYS G 36  
M 3 GLN G 15  ? GLN G 22  ? GLN G 15  GLN G 22  
M 4 THR G 2   ? LEU G 8   ? THR G 2   LEU G 8   
M 5 GLY G 150 ? ILE G 151 ? GLY G 150 ILE G 151 
N 1 ASP G 83  ? ALA G 89  ? ASP G 83  ALA G 89  
N 2 GLY G 41  ? HIS G 48  ? GLY G 41  HIS G 48  
N 3 THR G 116 ? HIS G 120 ? THR G 116 HIS G 120 
N 4 ARG G 143 ? VAL G 148 ? ARG G 143 VAL G 148 
O 1 ALA H 95  ? ASP H 101 ? ALA H 95  ASP H 101 
O 2 VAL H 29  ? LYS H 36  ? VAL H 29  LYS H 36  
O 3 GLN H 15  ? GLU H 21  ? GLN H 15  GLU H 21  
O 4 LYS H 3   ? LEU H 8   ? LYS H 3   LEU H 8   
O 5 GLY H 150 ? ILE H 151 ? GLY H 150 ILE H 151 
P 1 ASP H 83  ? ALA H 89  ? ASP H 83  ALA H 89  
P 2 GLY H 41  ? HIS H 48  ? GLY H 41  HIS H 48  
P 3 THR H 116 ? HIS H 120 ? THR H 116 HIS H 120 
P 4 ARG H 143 ? VAL H 148 ? ARG H 143 VAL H 148 
Q 1 ALA I 95  ? ASP I 101 ? ALA I 95  ASP I 101 
Q 2 VAL I 29  ? LYS I 36  ? VAL I 29  LYS I 36  
Q 3 GLN I 15  ? GLN I 22  ? GLN I 15  GLN I 22  
Q 4 THR I 2   ? LEU I 8   ? THR I 2   LEU I 8   
Q 5 GLY I 150 ? ILE I 151 ? GLY I 150 ILE I 151 
R 1 ASP I 83  ? ALA I 89  ? ASP I 83  ALA I 89  
R 2 GLY I 41  ? HIS I 48  ? GLY I 41  HIS I 48  
R 3 THR I 116 ? HIS I 120 ? THR I 116 HIS I 120 
R 4 ARG I 143 ? VAL I 148 ? ARG I 143 VAL I 148 
S 1 ALA J 95  ? ASP J 101 ? ALA J 95  ASP J 101 
S 2 VAL J 29  ? LYS J 36  ? VAL J 29  LYS J 36  
S 3 GLN J 15  ? GLN J 22  ? GLN J 15  GLN J 22  
S 4 THR J 2   ? LEU J 8   ? THR J 2   LEU J 8   
S 5 GLY J 150 ? ILE J 151 ? GLY J 150 ILE J 151 
T 1 ASP J 83  ? ALA J 89  ? ASP J 83  ALA J 89  
T 2 GLY J 41  ? HIS J 48  ? GLY J 41  HIS J 48  
T 3 THR J 116 ? HIS J 120 ? THR J 116 HIS J 120 
T 4 ARG J 143 ? VAL J 148 ? ARG J 143 VAL J 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 GLN A 22  ? O GLN A 22  N THR A 2   ? N THR A 2   
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 VAL A 119 ? N VAL A 119 O ALA A 145 ? O ALA A 145 
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 ASP C 101 ? O ASP C 101 N VAL C 29  ? N VAL C 29  
E 2 3 O LYS C 36  ? O LYS C 36  N GLN C 15  ? N GLN C 15  
E 3 4 O GLN C 22  ? O GLN C 22  N THR C 2   ? N THR C 2   
E 4 5 N VAL C 5   ? N VAL C 5   O GLY C 150 ? O GLY C 150 
F 1 2 O ALA C 89  ? O ALA C 89  N GLY C 41  ? N GLY C 41  
F 2 3 N HIS C 48  ? N HIS C 48  O THR C 116 ? O THR C 116 
F 3 4 N LEU C 117 ? N LEU C 117 O GLY C 147 ? O GLY C 147 
G 1 2 O ALA D 95  ? O ALA D 95  N ILE D 35  ? N ILE D 35  
G 2 3 O TRP D 32  ? O TRP D 32  N ASN D 19  ? N ASN D 19  
G 3 4 O ILE D 18  ? O ILE D 18  N CYS D 6   ? N CYS D 6   
G 4 5 N VAL D 5   ? N VAL D 5   O GLY D 150 ? O GLY D 150 
H 1 2 O ALA D 89  ? O ALA D 89  N GLY D 41  ? N GLY D 41  
H 2 3 N HIS D 48  ? N HIS D 48  O THR D 116 ? O THR D 116 
H 3 4 N VAL D 119 ? N VAL D 119 O ALA D 145 ? O ALA D 145 
I 1 2 O ILE E 99  ? O ILE E 99  N VAL E 31  ? N VAL E 31  
I 2 3 O TRP E 32  ? O TRP E 32  N ASN E 19  ? N ASN E 19  
I 3 4 O GLN E 22  ? O GLN E 22  N THR E 2   ? N THR E 2   
I 4 5 N VAL E 5   ? N VAL E 5   O GLY E 150 ? O GLY E 150 
J 1 2 O ALA E 89  ? O ALA E 89  N GLY E 41  ? N GLY E 41  
J 2 3 N HIS E 48  ? N HIS E 48  O THR E 116 ? O THR E 116 
J 3 4 N VAL E 119 ? N VAL E 119 O ALA E 145 ? O ALA E 145 
K 1 2 O ALA F 95  ? O ALA F 95  N ILE F 35  ? N ILE F 35  
K 2 3 O TRP F 32  ? O TRP F 32  N ASN F 19  ? N ASN F 19  
K 3 4 O GLY F 16  ? O GLY F 16  N LEU F 8   ? N LEU F 8   
K 4 5 N VAL F 5   ? N VAL F 5   O GLY F 150 ? O GLY F 150 
L 1 2 O ALA F 89  ? O ALA F 89  N GLY F 41  ? N GLY F 41  
L 2 3 N HIS F 48  ? N HIS F 48  O THR F 116 ? O THR F 116 
L 3 4 N VAL F 119 ? N VAL F 119 O ALA F 145 ? O ALA F 145 
M 1 2 O ILE G 99  ? O ILE G 99  N VAL G 31  ? N VAL G 31  
M 2 3 O LYS G 30  ? O LYS G 30  N GLU G 21  ? N GLU G 21  
M 3 4 O ILE G 18  ? O ILE G 18  N CYS G 6   ? N CYS G 6   
M 4 5 N VAL G 5   ? N VAL G 5   O GLY G 150 ? O GLY G 150 
N 1 2 O ALA G 89  ? O ALA G 89  N GLY G 41  ? N GLY G 41  
N 2 3 N HIS G 48  ? N HIS G 48  O THR G 116 ? O THR G 116 
N 3 4 N VAL G 119 ? N VAL G 119 O LEU G 144 ? O LEU G 144 
O 1 2 O ASP H 101 ? O ASP H 101 N VAL H 29  ? N VAL H 29  
O 2 3 O TRP H 32  ? O TRP H 32  N ASN H 19  ? N ASN H 19  
O 3 4 O ILE H 18  ? O ILE H 18  N CYS H 6   ? N CYS H 6   
O 4 5 N VAL H 5   ? N VAL H 5   O GLY H 150 ? O GLY H 150 
P 1 2 O VAL H 87  ? O VAL H 87  N HIS H 43  ? N HIS H 43  
P 2 3 N HIS H 48  ? N HIS H 48  O THR H 116 ? O THR H 116 
P 3 4 N VAL H 119 ? N VAL H 119 O ALA H 145 ? O ALA H 145 
Q 1 2 O ILE I 99  ? O ILE I 99  N VAL I 31  ? N VAL I 31  
Q 2 3 O TRP I 32  ? O TRP I 32  N ASN I 19  ? N ASN I 19  
Q 3 4 O GLY I 16  ? O GLY I 16  N LEU I 8   ? N LEU I 8   
Q 4 5 N VAL I 5   ? N VAL I 5   O GLY I 150 ? O GLY I 150 
R 1 2 O ALA I 89  ? O ALA I 89  N GLY I 41  ? N GLY I 41  
R 2 3 N HIS I 48  ? N HIS I 48  O THR I 116 ? O THR I 116 
R 3 4 N LEU I 117 ? N LEU I 117 O GLY I 147 ? O GLY I 147 
S 1 2 O ALA J 95  ? O ALA J 95  N ILE J 35  ? N ILE J 35  
S 2 3 O TRP J 32  ? O TRP J 32  N ASN J 19  ? N ASN J 19  
S 3 4 O GLY J 16  ? O GLY J 16  N LEU J 8   ? N LEU J 8   
S 4 5 N VAL J 5   ? N VAL J 5   O GLY J 150 ? O GLY J 150 
T 1 2 O ALA J 89  ? O ALA J 89  N GLY J 41  ? N GLY J 41  
T 2 3 N HIS J 48  ? N HIS J 48  O THR J 116 ? O THR J 116 
T 3 4 N VAL J 119 ? N VAL J 119 O ALA J 145 ? O ALA J 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 201'  
AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU1 B 200' 
AC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN B 201'  
AC5 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU1 C 200' 
AC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN C 201'  
AC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU1 D 200' 
AC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN D 201'  
AC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU1 E 200' 
BC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN E 201'  
BC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU1 F 200' 
BC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN F 201'  
BC4 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU1 G 200' 
BC5 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE ZN G 201'  
BC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU1 H 200' 
BC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN H 201'  
BC8 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU1 I 200' 
BC9 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN I 201'  
CC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU1 J 200' 
CC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN J 201'  
CC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE SO4 B 300' 
CC4 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE SO4 J 301' 
CC5 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE SO4 J 302' 
# 
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 4 HIS B  46  ? HIS B 46   . ? 1_555 ? 
10 AC3 4 HIS B  48  ? HIS B 48   . ? 1_555 ? 
11 AC3 4 HIS B  63  ? HIS B 63   . ? 1_555 ? 
12 AC3 4 HIS B  120 ? HIS B 120  . ? 1_555 ? 
13 AC4 4 HIS B  63  ? HIS B 63   . ? 1_555 ? 
14 AC4 4 HIS B  71  ? HIS B 71   . ? 1_555 ? 
15 AC4 4 HIS B  80  ? HIS B 80   . ? 1_555 ? 
16 AC4 4 ASP B  83  ? ASP B 83   . ? 1_555 ? 
17 AC5 4 HIS C  46  ? HIS C 46   . ? 1_555 ? 
18 AC5 4 HIS C  48  ? HIS C 48   . ? 1_555 ? 
19 AC5 4 HIS C  63  ? HIS C 63   . ? 1_555 ? 
20 AC5 4 HIS C  120 ? HIS C 120  . ? 1_555 ? 
21 AC6 4 HIS C  63  ? HIS C 63   . ? 1_555 ? 
22 AC6 4 HIS C  71  ? HIS C 71   . ? 1_555 ? 
23 AC6 4 HIS C  80  ? HIS C 80   . ? 1_555 ? 
24 AC6 4 ASP C  83  ? ASP C 83   . ? 1_555 ? 
25 AC7 4 HIS D  46  ? HIS D 46   . ? 1_555 ? 
26 AC7 4 HIS D  48  ? HIS D 48   . ? 1_555 ? 
27 AC7 4 HIS D  63  ? HIS D 63   . ? 1_555 ? 
28 AC7 4 HIS D  120 ? HIS D 120  . ? 1_555 ? 
29 AC8 4 HIS D  63  ? HIS D 63   . ? 1_555 ? 
30 AC8 4 HIS D  71  ? HIS D 71   . ? 1_555 ? 
31 AC8 4 HIS D  80  ? HIS D 80   . ? 1_555 ? 
32 AC8 4 ASP D  83  ? ASP D 83   . ? 1_555 ? 
33 AC9 4 HIS E  46  ? HIS E 46   . ? 1_555 ? 
34 AC9 4 HIS E  48  ? HIS E 48   . ? 1_555 ? 
35 AC9 4 HIS E  63  ? HIS E 63   . ? 1_555 ? 
36 AC9 4 HIS E  120 ? HIS E 120  . ? 1_555 ? 
37 BC1 4 HIS E  63  ? HIS E 63   . ? 1_555 ? 
38 BC1 4 HIS E  71  ? HIS E 71   . ? 1_555 ? 
39 BC1 4 HIS E  80  ? HIS E 80   . ? 1_555 ? 
40 BC1 4 ASP E  83  ? ASP E 83   . ? 1_555 ? 
41 BC2 4 HIS F  46  ? HIS F 46   . ? 1_555 ? 
42 BC2 4 HIS F  48  ? HIS F 48   . ? 1_555 ? 
43 BC2 4 HIS F  63  ? HIS F 63   . ? 1_555 ? 
44 BC2 4 HIS F  120 ? HIS F 120  . ? 1_555 ? 
45 BC3 4 HIS F  63  ? HIS F 63   . ? 1_555 ? 
46 BC3 4 HIS F  71  ? HIS F 71   . ? 1_555 ? 
47 BC3 4 HIS F  80  ? HIS F 80   . ? 1_555 ? 
48 BC3 4 ASP F  83  ? ASP F 83   . ? 1_555 ? 
49 BC4 4 HIS G  46  ? HIS G 46   . ? 1_555 ? 
50 BC4 4 HIS G  48  ? HIS G 48   . ? 1_555 ? 
51 BC4 4 HIS G  63  ? HIS G 63   . ? 1_555 ? 
52 BC4 4 HIS G  120 ? HIS G 120  . ? 1_555 ? 
53 BC5 5 HIS G  63  ? HIS G 63   . ? 1_555 ? 
54 BC5 5 HIS G  71  ? HIS G 71   . ? 1_555 ? 
55 BC5 5 HIS G  80  ? HIS G 80   . ? 1_555 ? 
56 BC5 5 ASP G  83  ? ASP G 83   . ? 1_555 ? 
57 BC5 5 LYS G  136 ? LYS G 136  . ? 1_555 ? 
58 BC6 4 HIS H  46  ? HIS H 46   . ? 1_555 ? 
59 BC6 4 HIS H  48  ? HIS H 48   . ? 1_555 ? 
60 BC6 4 HIS H  63  ? HIS H 63   . ? 1_555 ? 
61 BC6 4 HIS H  120 ? HIS H 120  . ? 1_555 ? 
62 BC7 4 HIS H  63  ? HIS H 63   . ? 1_555 ? 
63 BC7 4 HIS H  71  ? HIS H 71   . ? 1_555 ? 
64 BC7 4 HIS H  80  ? HIS H 80   . ? 1_555 ? 
65 BC7 4 ASP H  83  ? ASP H 83   . ? 1_555 ? 
66 BC8 4 HIS I  46  ? HIS I 46   . ? 1_555 ? 
67 BC8 4 HIS I  48  ? HIS I 48   . ? 1_555 ? 
68 BC8 4 HIS I  63  ? HIS I 63   . ? 1_555 ? 
69 BC8 4 HIS I  120 ? HIS I 120  . ? 1_555 ? 
70 BC9 4 HIS I  63  ? HIS I 63   . ? 1_555 ? 
71 BC9 4 HIS I  71  ? HIS I 71   . ? 1_555 ? 
72 BC9 4 HIS I  80  ? HIS I 80   . ? 1_555 ? 
73 BC9 4 ASP I  83  ? ASP I 83   . ? 1_555 ? 
74 CC1 4 HIS J  46  ? HIS J 46   . ? 1_555 ? 
75 CC1 4 HIS J  48  ? HIS J 48   . ? 1_555 ? 
76 CC1 4 HIS J  63  ? HIS J 63   . ? 1_555 ? 
77 CC1 4 HIS J  120 ? HIS J 120  . ? 1_555 ? 
78 CC2 4 HIS J  63  ? HIS J 63   . ? 1_555 ? 
79 CC2 4 HIS J  71  ? HIS J 71   . ? 1_555 ? 
80 CC2 4 HIS J  80  ? HIS J 80   . ? 1_555 ? 
81 CC2 4 ASP J  83  ? ASP J 83   . ? 1_555 ? 
82 CC3 4 LYS B  75  ? LYS B 75   . ? 1_555 ? 
83 CC3 4 LYS D  128 ? LYS D 128  . ? 1_555 ? 
84 CC3 4 HOH KA .   ? HOH D 692  . ? 1_555 ? 
85 CC3 4 HOH KA .   ? HOH D 1022 . ? 1_555 ? 
86 CC4 7 LYS E  128 ? LYS E 128  . ? 5_555 ? 
87 CC4 7 HOH LA .   ? HOH E 1004 . ? 5_555 ? 
88 CC4 7 HOH LA .   ? HOH E 1386 . ? 5_555 ? 
89 CC4 7 HOH LA .   ? HOH E 1430 . ? 5_555 ? 
90 CC4 7 LYS H  75  ? LYS H 75   . ? 1_555 ? 
91 CC4 7 LYS H  128 ? LYS H 128  . ? 1_555 ? 
92 CC4 7 LYS J  128 ? LYS J 128  . ? 1_555 ? 
93 CC5 2 THR J  39  ? THR J 39   . ? 1_555 ? 
94 CC5 2 GLU J  40  ? GLU J 40   . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1PU0 
_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]   0.000000 
_database_PDB_matrix.origx_vector[2]   0.000000 
_database_PDB_matrix.origx_vector[3]   0.000000 
# 
_atom_sites.entry_id                    1PU0 
_atom_sites.fract_transf_matrix[1][1]   0.004912 
_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]   0.006036 
_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]   0.006937 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
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   ? 45.526  28.488  6.906  1.00 53.11  ? 1    ALA A N   1 
ATOM   2     C  CA  . ALA A  1 1   ? 46.177  29.575  7.626  1.00 50.28  ? 1    ALA A CA  1 
ATOM   3     C  C   . ALA A  1 1   ? 47.533  29.200  8.211  1.00 38.03  ? 1    ALA A C   1 
ATOM   4     O  O   . ALA A  1 1   ? 47.801  28.182  8.854  1.00 39.93  ? 1    ALA A O   1 
ATOM   5     C  CB  . ALA A  1 1   ? 45.249  30.086  8.730  1.00 44.75  ? 1    ALA A CB  1 
ATOM   6     N  N   . THR A  1 2   ? 48.498  30.100  7.989  1.00 36.49  ? 2    THR A N   1 
ATOM   7     C  CA  . THR A  1 2   ? 49.790  29.814  8.650  1.00 30.80  ? 2    THR A CA  1 
ATOM   8     C  C   . THR A  1 2   ? 49.682  30.417  10.045 1.00 32.92  ? 2    THR A C   1 
ATOM   9     O  O   . THR A  1 2   ? 49.017  31.445  10.220 1.00 26.22  ? 2    THR A O   1 
ATOM   10    C  CB  . THR A  1 2   ? 50.939  30.329  7.786  1.00 43.05  ? 2    THR A CB  1 
ATOM   11    O  OG1 . THR A  1 2   ? 50.894  29.654  6.516  1.00 72.17  ? 2    THR A OG1 1 
ATOM   12    C  CG2 . THR A  1 2   ? 52.305  29.996  8.345  1.00 35.60  ? 2    THR A CG2 1 
ATOM   13    N  N   . LYS A  1 3   ? 50.292  29.771  11.041 1.00 26.03  ? 3    LYS A N   1 
ATOM   14    C  CA  . LYS A  1 3   ? 50.243  30.268  12.406 1.00 23.64  ? 3    LYS A CA  1 
ATOM   15    C  C   . LYS A  1 3   ? 51.628  30.236  13.042 1.00 26.23  ? 3    LYS A C   1 
ATOM   16    O  O   . LYS A  1 3   ? 52.428  29.350  12.762 1.00 23.34  ? 3    LYS A O   1 
ATOM   17    C  CB  . LYS A  1 3   ? 49.284  29.427  13.252 1.00 30.41  ? 3    LYS A CB  1 
ATOM   18    C  CG  . LYS A  1 3   ? 47.850  29.549  12.727 1.00 31.85  ? 3    LYS A CG  1 
ATOM   19    C  CD  . LYS A  1 3   ? 46.899  28.677  13.529 1.00 48.48  ? 3    LYS A CD  1 
ATOM   20    C  CE  . LYS A  1 3   ? 46.058  27.833  12.571 1.00 71.20  ? 3    LYS A CE  1 
ATOM   21    N  NZ  . LYS A  1 3   ? 46.779  27.612  11.279 1.00 79.63  ? 3    LYS A NZ  1 
ATOM   22    N  N   . ALA A  1 4   ? 51.863  31.232  13.887 1.00 21.86  ? 4    ALA A N   1 
ATOM   23    C  CA  . ALA A  1 4   ? 53.137  31.287  14.602 1.00 21.58  ? 4    ALA A CA  1 
ATOM   24    C  C   . ALA A  1 4   ? 52.878  31.762  16.033 1.00 28.97  ? 4    ALA A C   1 
ATOM   25    O  O   . ALA A  1 4   ? 51.779  32.198  16.366 1.00 23.80  ? 4    ALA A O   1 
ATOM   26    C  CB  . ALA A  1 4   ? 54.128  32.197  13.911 1.00 21.65  ? 4    ALA A CB  1 
ATOM   27    N  N   . VAL A  1 5   ? 53.909  31.677  16.875 1.00 23.32  ? 5    VAL A N   1 
ATOM   28    C  CA  . VAL A  1 5   ? 53.685  32.054  18.277 1.00 25.84  ? 5    VAL A CA  1 
ATOM   29    C  C   . VAL A  1 5   ? 55.025  32.476  18.860 1.00 22.73  ? 5    VAL A C   1 
ATOM   30    O  O   . VAL A  1 5   ? 56.090  32.069  18.386 1.00 22.98  ? 5    VAL A O   1 
ATOM   31    C  CB  . VAL A  1 5   ? 53.048  30.919  19.085 1.00 25.28  ? 5    VAL A CB  1 
ATOM   32    C  CG1 . VAL A  1 5   ? 54.046  29.777  19.254 1.00 27.81  ? 5    VAL A CG1 1 
ATOM   33    C  CG2 . VAL A  1 5   ? 52.583  31.371  20.466 1.00 26.07  ? 5    VAL A CG2 1 
ATOM   34    N  N   . CYS A  1 6   ? 54.955  33.365  19.851 1.00 20.42  ? 6    CYS A N   1 
ATOM   35    C  CA  . CYS A  1 6   ? 56.201  33.827  20.437 1.00 18.32  ? 6    CYS A CA  1 
ATOM   36    C  C   . CYS A  1 6   ? 56.030  34.004  21.936 1.00 28.81  ? 6    CYS A C   1 
ATOM   37    O  O   . CYS A  1 6   ? 55.102  34.705  22.376 1.00 25.64  ? 6    CYS A O   1 
ATOM   38    C  CB  . CYS A  1 6   ? 56.600  35.147  19.770 1.00 21.41  ? 6    CYS A CB  1 
ATOM   39    S  SG  . CYS A  1 6   ? 58.133  35.807  20.467 1.00 25.83  ? 6    CYS A SG  1 
ATOM   40    N  N   . VAL A  1 7   ? 56.900  33.399  22.735 1.00 19.47  ? 7    VAL A N   1 
ATOM   41    C  CA  . VAL A  1 7   ? 56.828  33.614  24.187 1.00 22.29  ? 7    VAL A CA  1 
ATOM   42    C  C   . VAL A  1 7   ? 57.866  34.655  24.559 1.00 22.90  ? 7    VAL A C   1 
ATOM   43    O  O   . VAL A  1 7   ? 59.068  34.429  24.328 1.00 22.90  ? 7    VAL A O   1 
ATOM   44    C  CB  . VAL A  1 7   ? 57.026  32.311  24.963 1.00 25.62  ? 7    VAL A CB  1 
ATOM   45    C  CG1 . VAL A  1 7   ? 57.069  32.537  26.472 1.00 27.94  ? 7    VAL A CG1 1 
ATOM   46    C  CG2 . VAL A  1 7   ? 55.903  31.326  24.620 1.00 25.95  ? 7    VAL A CG2 1 
ATOM   47    N  N   . LEU A  1 8   ? 57.428  35.802  25.090 1.00 19.97  ? 8    LEU A N   1 
ATOM   48    C  CA  . LEU A  1 8   ? 58.361  36.869  25.417 1.00 18.63  ? 8    LEU A CA  1 
ATOM   49    C  C   . LEU A  1 8   ? 58.847  36.770  26.859 1.00 23.85  ? 8    LEU A C   1 
ATOM   50    O  O   . LEU A  1 8   ? 58.011  36.646  27.752 1.00 25.30  ? 8    LEU A O   1 
ATOM   51    C  CB  . LEU A  1 8   ? 57.687  38.238  25.235 1.00 23.36  ? 8    LEU A CB  1 
ATOM   52    C  CG  . LEU A  1 8   ? 57.255  38.543  23.788 1.00 30.47  ? 8    LEU A CG  1 
ATOM   53    C  CD1 . LEU A  1 8   ? 56.115  39.542  23.771 1.00 39.31  ? 8    LEU A CD1 1 
ATOM   54    C  CD2 . LEU A  1 8   ? 58.441  39.083  23.009 1.00 39.16  ? 8    LEU A CD2 1 
ATOM   55    N  N   . LYS A  1 9   ? 60.156  36.829  27.054 1.00 25.33  ? 9    LYS A N   1 
ATOM   56    C  CA  . LYS A  1 9   ? 60.768  36.776  28.382 1.00 25.69  ? 9    LYS A CA  1 
ATOM   57    C  C   . LYS A  1 9   ? 62.034  37.632  28.404 1.00 23.53  ? 9    LYS A C   1 
ATOM   58    O  O   . LYS A  1 9   ? 62.674  37.923  27.394 1.00 21.34  ? 9    LYS A O   1 
ATOM   59    C  CB  . LYS A  1 9   ? 61.117  35.342  28.800 1.00 29.28  ? 9    LYS A CB  1 
ATOM   60    C  CG  . LYS A  1 9   ? 59.956  34.380  28.846 1.00 46.51  ? 9    LYS A CG  1 
ATOM   61    C  CD  . LYS A  1 9   ? 60.417  32.927  28.895 1.00 60.13  ? 9    LYS A CD  1 
ATOM   62    C  CE  . LYS A  1 9   ? 59.319  32.013  29.424 1.00 58.98  ? 9    LYS A CE  1 
ATOM   63    N  NZ  . LYS A  1 9   ? 59.437  30.625  28.894 1.00 58.91  ? 9    LYS A NZ  1 
ATOM   64    N  N   . GLY A  1 10  ? 62.443  38.050  29.611 1.00 24.67  ? 10   GLY A N   1 
ATOM   65    C  CA  . GLY A  1 10  ? 63.615  38.913  29.735 1.00 26.35  ? 10   GLY A CA  1 
ATOM   66    C  C   . GLY A  1 10  ? 64.187  38.806  31.150 1.00 26.87  ? 10   GLY A C   1 
ATOM   67    O  O   . GLY A  1 10  ? 63.828  37.883  31.878 1.00 31.49  ? 10   GLY A O   1 
ATOM   68    N  N   . ASP A  1 11  ? 65.049  39.741  31.488 1.00 32.81  ? 11   ASP A N   1 
ATOM   69    C  CA  . ASP A  1 11  ? 65.675  39.727  32.807 1.00 41.38  ? 11   ASP A CA  1 
ATOM   70    C  C   . ASP A  1 11  ? 64.797  40.343  33.887 1.00 43.36  ? 11   ASP A C   1 
ATOM   71    O  O   . ASP A  1 11  ? 65.133  40.169  35.058 1.00 45.00  ? 11   ASP A O   1 
ATOM   72    C  CB  . ASP A  1 11  ? 66.981  40.513  32.730 1.00 37.32  ? 11   ASP A CB  1 
ATOM   73    C  CG  . ASP A  1 11  ? 67.931  39.882  31.729 1.00 45.77  ? 11   ASP A CG  1 
ATOM   74    O  OD1 . ASP A  1 11  ? 68.619  40.660  31.039 1.00 52.97  ? 11   ASP A OD1 1 
ATOM   75    O  OD2 . ASP A  1 11  ? 67.949  38.634  31.675 1.00 53.18  ? 11   ASP A OD2 1 
ATOM   76    N  N   . GLY A  1 12  ? 63.733  41.036  33.511 1.00 37.44  ? 12   GLY A N   1 
ATOM   77    C  CA  . GLY A  1 12  ? 62.839  41.686  34.462 1.00 31.01  ? 12   GLY A CA  1 
ATOM   78    C  C   . GLY A  1 12  ? 61.500  40.994  34.545 1.00 29.99  ? 12   GLY A C   1 
ATOM   79    O  O   . GLY A  1 12  ? 61.470  39.793  34.274 1.00 31.19  ? 12   GLY A O   1 
ATOM   80    N  N   . PRO A  1 13  ? 60.412  41.683  34.914 1.00 27.43  ? 13   PRO A N   1 
ATOM   81    C  CA  . PRO A  1 13  ? 59.081  41.096  34.997 1.00 25.89  ? 13   PRO A CA  1 
ATOM   82    C  C   . PRO A  1 13  ? 58.322  41.051  33.670 1.00 27.14  ? 13   PRO A C   1 
ATOM   83    O  O   . PRO A  1 13  ? 57.230  40.469  33.592 1.00 28.64  ? 13   PRO A O   1 
ATOM   84    C  CB  . PRO A  1 13  ? 58.332  42.080  35.928 1.00 27.45  ? 13   PRO A CB  1 
ATOM   85    C  CG  . PRO A  1 13  ? 58.971  43.385  35.625 1.00 25.93  ? 13   PRO A CG  1 
ATOM   86    C  CD  . PRO A  1 13  ? 60.414  43.114  35.308 1.00 31.42  ? 13   PRO A CD  1 
ATOM   87    N  N   . VAL A  1 14  ? 58.910  41.671  32.644 1.00 26.53  ? 14   VAL A N   1 
ATOM   88    C  CA  . VAL A  1 14  ? 58.133  41.744  31.398 1.00 29.01  ? 14   VAL A CA  1 
ATOM   89    C  C   . VAL A  1 14  ? 58.046  40.376  30.744 1.00 29.02  ? 14   VAL A C   1 
ATOM   90    O  O   . VAL A  1 14  ? 59.038  39.710  30.477 1.00 27.55  ? 14   VAL A O   1 
ATOM   91    C  CB  . VAL A  1 14  ? 58.727  42.779  30.426 1.00 23.23  ? 14   VAL A CB  1 
ATOM   92    C  CG1 . VAL A  1 14  ? 57.872  42.869  29.153 1.00 20.55  ? 14   VAL A CG1 1 
ATOM   93    C  CG2 . VAL A  1 14  ? 58.811  44.137  31.090 1.00 23.45  ? 14   VAL A CG2 1 
ATOM   94    N  N   . GLN A  1 15  ? 56.842  39.910  30.470 1.00 25.57  ? 15   GLN A N   1 
ATOM   95    C  CA  . GLN A  1 15  ? 56.648  38.649  29.758 1.00 30.84  ? 15   GLN A CA  1 
ATOM   96    C  C   . GLN A  1 15  ? 55.298  38.644  29.066 1.00 30.76  ? 15   GLN A C   1 
ATOM   97    O  O   . GLN A  1 15  ? 54.425  39.470  29.361 1.00 28.22  ? 15   GLN A O   1 
ATOM   98    C  CB  . GLN A  1 15  ? 56.716  37.448  30.697 1.00 31.98  ? 15   GLN A CB  1 
ATOM   99    C  CG  . GLN A  1 15  ? 55.723  37.607  31.838 1.00 28.34  ? 15   GLN A CG  1 
ATOM   100   C  CD  . GLN A  1 15  ? 56.110  36.672  32.984 1.00 44.24  ? 15   GLN A CD  1 
ATOM   101   O  OE1 . GLN A  1 15  ? 55.549  35.585  33.091 1.00 40.59  ? 15   GLN A OE1 1 
ATOM   102   N  NE2 . GLN A  1 15  ? 57.052  37.128  33.794 1.00 38.73  ? 15   GLN A NE2 1 
ATOM   103   N  N   . GLY A  1 16  ? 55.107  37.717  28.132 1.00 27.41  ? 16   GLY A N   1 
ATOM   104   C  CA  . GLY A  1 16  ? 53.877  37.759  27.352 1.00 28.13  ? 16   GLY A CA  1 
ATOM   105   C  C   . GLY A  1 16  ? 53.886  36.633  26.334 1.00 31.84  ? 16   GLY A C   1 
ATOM   106   O  O   . GLY A  1 16  ? 54.874  35.915  26.225 1.00 25.71  ? 16   GLY A O   1 
ATOM   107   N  N   . ILE A  1 17  ? 52.768  36.510  25.646 1.00 27.02  ? 17   ILE A N   1 
ATOM   108   C  CA  . ILE A  1 17  ? 52.558  35.511  24.605 1.00 25.22  ? 17   ILE A CA  1 
ATOM   109   C  C   . ILE A  1 17  ? 51.920  36.244  23.423 1.00 29.51  ? 17   ILE A C   1 
ATOM   110   O  O   . ILE A  1 17  ? 50.904  36.918  23.576 1.00 27.49  ? 17   ILE A O   1 
ATOM   111   C  CB  . ILE A  1 17  ? 51.706  34.345  25.111 1.00 30.99  ? 17   ILE A CB  1 
ATOM   112   C  CG1 . ILE A  1 17  ? 52.362  33.534  26.242 1.00 28.56  ? 17   ILE A CG1 1 
ATOM   113   C  CG2 . ILE A  1 17  ? 51.300  33.401  23.988 1.00 33.14  ? 17   ILE A CG2 1 
ATOM   114   C  CD1 . ILE A  1 17  ? 51.477  32.450  26.817 1.00 31.55  ? 17   ILE A CD1 1 
ATOM   115   N  N   . ILE A  1 18  ? 52.551  36.147  22.257 1.00 22.78  ? 18   ILE A N   1 
ATOM   116   C  CA  . ILE A  1 18  ? 52.022  36.833  21.071 1.00 19.24  ? 18   ILE A CA  1 
ATOM   117   C  C   . ILE A  1 18  ? 51.747  35.782  20.004 1.00 26.80  ? 18   ILE A C   1 
ATOM   118   O  O   . ILE A  1 18  ? 52.596  34.922  19.701 1.00 24.09  ? 18   ILE A O   1 
ATOM   119   C  CB  . ILE A  1 18  ? 52.987  37.917  20.598 1.00 23.43  ? 18   ILE A CB  1 
ATOM   120   C  CG1 . ILE A  1 18  ? 53.231  39.017  21.648 1.00 24.83  ? 18   ILE A CG1 1 
ATOM   121   C  CG2 . ILE A  1 18  ? 52.515  38.557  19.295 1.00 27.33  ? 18   ILE A CG2 1 
ATOM   122   C  CD1 . ILE A  1 18  ? 51.932  39.799  21.838 1.00 24.27  ? 18   ILE A CD1 1 
ATOM   123   N  N   . ASN A  1 19  ? 50.543  35.830  19.435 1.00 23.30  ? 19   ASN A N   1 
ATOM   124   C  CA  . ASN A  1 19  ? 50.125  34.919  18.384 1.00 21.44  ? 19   ASN A CA  1 
ATOM   125   C  C   . ASN A  1 19  ? 50.148  35.639  17.040 1.00 20.71  ? 19   ASN A C   1 
ATOM   126   O  O   . ASN A  1 19  ? 49.976  36.844  16.994 1.00 23.30  ? 19   ASN A O   1 
ATOM   127   C  CB  . ASN A  1 19  ? 48.713  34.372  18.614 1.00 29.18  ? 19   ASN A CB  1 
ATOM   128   C  CG  . ASN A  1 19  ? 48.604  33.767  20.008 1.00 36.22  ? 19   ASN A CG  1 
ATOM   129   O  OD1 . ASN A  1 19  ? 49.072  32.649  20.204 1.00 25.21  ? 19   ASN A OD1 1 
ATOM   130   N  ND2 . ASN A  1 19  ? 48.022  34.532  20.927 1.00 32.94  ? 19   ASN A ND2 1 
ATOM   131   N  N   . PHE A  1 20  ? 50.394  34.849  16.001 1.00 23.04  ? 20   PHE A N   1 
ATOM   132   C  CA  . PHE A  1 20  ? 50.374  35.318  14.621 1.00 22.42  ? 20   PHE A CA  1 
ATOM   133   C  C   . PHE A  1 20  ? 49.517  34.374  13.781 1.00 24.05  ? 20   PHE A C   1 
ATOM   134   O  O   . PHE A  1 20  ? 49.578  33.144  13.918 1.00 24.70  ? 20   PHE A O   1 
ATOM   135   C  CB  . PHE A  1 20  ? 51.761  35.374  13.998 1.00 22.43  ? 20   PHE A CB  1 
ATOM   136   C  CG  . PHE A  1 20  ? 52.800  36.204  14.728 1.00 21.92  ? 20   PHE A CG  1 
ATOM   137   C  CD1 . PHE A  1 20  ? 53.135  37.462  14.288 1.00 21.17  ? 20   PHE A CD1 1 
ATOM   138   C  CD2 . PHE A  1 20  ? 53.438  35.683  15.861 1.00 22.61  ? 20   PHE A CD2 1 
ATOM   139   C  CE1 . PHE A  1 20  ? 54.103  38.220  14.914 1.00 24.66  ? 20   PHE A CE1 1 
ATOM   140   C  CE2 . PHE A  1 20  ? 54.434  36.433  16.499 1.00 18.25  ? 20   PHE A CE2 1 
ATOM   141   C  CZ  . PHE A  1 20  ? 54.756  37.680  16.016 1.00 23.25  ? 20   PHE A CZ  1 
ATOM   142   N  N   . GLU A  1 21  ? 48.720  34.974  12.885 1.00 24.90  ? 21   GLU A N   1 
ATOM   143   C  CA  . GLU A  1 21  ? 47.934  34.123  11.987 1.00 22.76  ? 21   GLU A CA  1 
ATOM   144   C  C   . GLU A  1 21  ? 47.900  34.772  10.608 1.00 23.55  ? 21   GLU A C   1 
ATOM   145   O  O   . GLU A  1 21  ? 47.714  35.982  10.518 1.00 24.06  ? 21   GLU A O   1 
ATOM   146   C  CB  . GLU A  1 21  ? 46.522  33.908  12.519 1.00 25.11  ? 21   GLU A CB  1 
ATOM   147   C  CG  . GLU A  1 21  ? 45.647  33.098  11.571 1.00 35.55  ? 21   GLU A CG  1 
ATOM   148   C  CD  . GLU A  1 21  ? 44.338  32.717  12.247 1.00 51.97  ? 21   GLU A CD  1 
ATOM   149   O  OE1 . GLU A  1 21  ? 44.390  32.138  13.353 1.00 65.30  ? 21   GLU A OE1 1 
ATOM   150   O  OE2 . GLU A  1 21  ? 43.275  33.018  11.668 1.00 69.26  ? 21   GLU A OE2 1 
ATOM   151   N  N   . GLN A  1 22  ? 48.094  33.970  9.560  1.00 24.92  ? 22   GLN A N   1 
ATOM   152   C  CA  . GLN A  1 22  ? 48.104  34.498  8.204  1.00 22.58  ? 22   GLN A CA  1 
ATOM   153   C  C   . GLN A  1 22  ? 47.335  33.482  7.352  1.00 26.18  ? 22   GLN A C   1 
ATOM   154   O  O   . GLN A  1 22  ? 47.879  32.422  7.063  1.00 28.29  ? 22   GLN A O   1 
ATOM   155   C  CB  . GLN A  1 22  ? 49.502  34.703  7.642  1.00 27.97  ? 22   GLN A CB  1 
ATOM   156   C  CG  . GLN A  1 22  ? 49.570  35.527  6.351  1.00 27.21  ? 22   GLN A CG  1 
ATOM   157   C  CD  . GLN A  1 22  ? 50.982  35.621  5.800  1.00 28.05  ? 22   GLN A CD  1 
ATOM   158   O  OE1 . GLN A  1 22  ? 51.870  34.895  6.266  1.00 27.46  ? 22   GLN A OE1 1 
ATOM   159   N  NE2 . GLN A  1 22  ? 51.250  36.487  4.833  1.00 24.38  ? 22   GLN A NE2 1 
ATOM   160   N  N   . LYS A  1 23  ? 46.112  33.882  7.033  1.00 26.96  ? 23   LYS A N   1 
ATOM   161   C  CA  . LYS A  1 23  ? 45.145  33.044  6.339  1.00 32.53  ? 23   LYS A CA  1 
ATOM   162   C  C   . LYS A  1 23  ? 45.593  32.770  4.909  1.00 27.33  ? 23   LYS A C   1 
ATOM   163   O  O   . LYS A  1 23  ? 45.469  31.653  4.427  1.00 33.56  ? 23   LYS A O   1 
ATOM   164   C  CB  . LYS A  1 23  ? 43.769  33.716  6.284  1.00 38.32  ? 23   LYS A CB  1 
ATOM   165   C  CG  . LYS A  1 23  ? 42.968  33.724  7.568  1.00 60.79  ? 23   LYS A CG  1 
ATOM   166   C  CD  . LYS A  1 23  ? 42.804  32.329  8.144  1.00 69.36  ? 23   LYS A CD  1 
ATOM   167   C  CE  . LYS A  1 23  ? 41.384  32.066  8.625  1.00 70.18  ? 23   LYS A CE  1 
ATOM   168   N  NZ  . LYS A  1 23  ? 41.060  30.614  8.505  1.00 51.12  ? 23   LYS A NZ  1 
ATOM   169   N  N   . GLU A  1 24  ? 46.110  33.801  4.245  1.00 31.11  ? 24   GLU A N   1 
ATOM   170   C  CA  . GLU A  1 24  ? 46.622  33.620  2.886  1.00 34.34  ? 24   GLU A CA  1 
ATOM   171   C  C   . GLU A  1 24  ? 48.070  34.077  2.794  1.00 27.79  ? 24   GLU A C   1 
ATOM   172   O  O   . GLU A  1 24  ? 48.468  35.100  3.350  1.00 29.49  ? 24   GLU A O   1 
ATOM   173   C  CB  . GLU A  1 24  ? 45.778  34.382  1.854  1.00 33.61  ? 24   GLU A CB  1 
ATOM   174   C  CG  . GLU A  1 24  ? 44.273  34.157  2.029  1.00 43.97  ? 24   GLU A CG  1 
ATOM   175   C  CD  . GLU A  1 24  ? 43.838  32.888  1.309  1.00 57.77  ? 24   GLU A CD  1 
ATOM   176   O  OE1 . GLU A  1 24  ? 44.660  32.353  0.531  1.00 55.58  ? 24   GLU A OE1 1 
ATOM   177   O  OE2 . GLU A  1 24  ? 42.687  32.455  1.535  1.00 66.62  ? 24   GLU A OE2 1 
ATOM   178   N  N   . SER A  1 25  ? 48.889  33.331  2.056  1.00 28.28  ? 25   SER A N   1 
ATOM   179   C  CA  . SER A  1 25  ? 50.312  33.675  1.994  1.00 24.78  ? 25   SER A CA  1 
ATOM   180   C  C   . SER A  1 25  ? 50.543  35.037  1.417  1.00 28.45  ? 25   SER A C   1 
ATOM   181   O  O   . SER A  1 25  ? 51.584  35.672  1.593  1.00 30.88  ? 25   SER A O   1 
ATOM   182   C  CB  . SER A  1 25  ? 51.034  32.586  1.174  1.00 31.21  ? 25   SER A CB  1 
ATOM   183   O  OG  . SER A  1 25  ? 50.818  32.829  -0.213 1.00 35.26  ? 25   SER A OG  1 
ATOM   184   N  N   . ASN A  1 26  ? 49.550  35.572  0.660  1.00 28.14  ? 26   ASN A N   1 
ATOM   185   C  CA  . ASN A  1 26  ? 49.781  36.910  0.148  1.00 24.73  ? 26   ASN A CA  1 
ATOM   186   C  C   . ASN A  1 26  ? 48.853  37.924  0.834  1.00 32.84  ? 26   ASN A C   1 
ATOM   187   O  O   . ASN A  1 26  ? 48.636  39.020  0.317  1.00 34.48  ? 26   ASN A O   1 
ATOM   188   C  CB  . ASN A  1 26  ? 49.578  37.028  -1.367 1.00 25.90  ? 26   ASN A CB  1 
ATOM   189   C  CG  . ASN A  1 26  ? 48.183  36.655  -1.819 1.00 25.66  ? 26   ASN A CG  1 
ATOM   190   O  OD1 . ASN A  1 26  ? 47.521  35.832  -1.192 1.00 31.32  ? 26   ASN A OD1 1 
ATOM   191   N  ND2 . ASN A  1 26  ? 47.731  37.241  -2.934 1.00 29.47  ? 26   ASN A ND2 1 
ATOM   192   N  N   . GLY A  1 27  ? 48.328  37.518  1.983  1.00 27.93  ? 27   GLY A N   1 
ATOM   193   C  CA  . GLY A  1 27  ? 47.460  38.377  2.761  1.00 37.35  ? 27   GLY A CA  1 
ATOM   194   C  C   . GLY A  1 27  ? 48.154  38.901  4.003  1.00 37.79  ? 27   GLY A C   1 
ATOM   195   O  O   . GLY A  1 27  ? 49.331  38.636  4.258  1.00 30.10  ? 27   GLY A O   1 
ATOM   196   N  N   . PRO A  1 28  ? 47.411  39.671  4.790  1.00 32.23  ? 28   PRO A N   1 
ATOM   197   C  CA  . PRO A  1 28  ? 47.999  40.281  5.980  1.00 28.31  ? 28   PRO A CA  1 
ATOM   198   C  C   . PRO A  1 28  ? 48.138  39.277  7.109  1.00 21.76  ? 28   PRO A C   1 
ATOM   199   O  O   . PRO A  1 28  ? 47.481  38.237  7.140  1.00 22.55  ? 28   PRO A O   1 
ATOM   200   C  CB  . PRO A  1 28  ? 46.980  41.356  6.383  1.00 37.36  ? 28   PRO A CB  1 
ATOM   201   C  CG  . PRO A  1 28  ? 45.692  40.936  5.751  1.00 46.09  ? 28   PRO A CG  1 
ATOM   202   C  CD  . PRO A  1 28  ? 45.991  40.017  4.603  1.00 36.79  ? 28   PRO A CD  1 
ATOM   203   N  N   . VAL A  1 29  ? 48.982  39.669  8.069  1.00 24.84  ? 29   VAL A N   1 
ATOM   204   C  CA  . VAL A  1 29  ? 49.125  38.893  9.294  1.00 24.20  ? 29   VAL A CA  1 
ATOM   205   C  C   . VAL A  1 29  ? 48.447  39.558  10.502 1.00 19.52  ? 29   VAL A C   1 
ATOM   206   O  O   . VAL A  1 29  ? 48.736  40.732  10.753 1.00 25.08  ? 29   VAL A O   1 
ATOM   207   C  CB  . VAL A  1 29  ? 50.626  38.742  9.621  1.00 24.83  ? 29   VAL A CB  1 
ATOM   208   C  CG1 . VAL A  1 29  ? 50.896  37.874  10.843 1.00 21.12  ? 29   VAL A CG1 1 
ATOM   209   C  CG2 . VAL A  1 29  ? 51.385  38.187  8.417  1.00 23.15  ? 29   VAL A CG2 1 
ATOM   210   N  N   . LYS A  1 30  ? 47.644  38.780  11.207 1.00 22.04  ? 30   LYS A N   1 
ATOM   211   C  CA  . LYS A  1 30  ? 47.056  39.188  12.469 1.00 24.26  ? 30   LYS A CA  1 
ATOM   212   C  C   . LYS A  1 30  ? 47.992  38.837  13.637 1.00 25.15  ? 30   LYS A C   1 
ATOM   213   O  O   . LYS A  1 30  ? 48.478  37.713  13.739 1.00 27.07  ? 30   LYS A O   1 
ATOM   214   C  CB  . LYS A  1 30  ? 45.711  38.497  12.723 1.00 27.83  ? 30   LYS A CB  1 
ATOM   215   C  CG  . LYS A  1 30  ? 44.653  38.928  11.718 1.00 40.29  ? 30   LYS A CG  1 
ATOM   216   C  CD  . LYS A  1 30  ? 43.442  38.011  11.770 1.00 55.80  ? 30   LYS A CD  1 
ATOM   217   C  CE  . LYS A  1 30  ? 42.746  37.957  10.417 1.00 70.25  ? 30   LYS A CE  1 
ATOM   218   N  NZ  . LYS A  1 30  ? 41.972  39.200  10.132 1.00 57.68  ? 30   LYS A NZ  1 
ATOM   219   N  N   . VAL A  1 31  ? 48.209  39.827  14.486 1.00 24.54  ? 31   VAL A N   1 
ATOM   220   C  CA  . VAL A  1 31  ? 49.126  39.701  15.611 1.00 23.57  ? 31   VAL A CA  1 
ATOM   221   C  C   . VAL A  1 31  ? 48.377  40.036  16.897 1.00 29.47  ? 31   VAL A C   1 
ATOM   222   O  O   . VAL A  1 31  ? 47.838  41.133  17.023 1.00 33.50  ? 31   VAL A O   1 
ATOM   223   C  CB  . VAL A  1 31  ? 50.293  40.668  15.467 1.00 21.12  ? 31   VAL A CB  1 
ATOM   224   C  CG1 . VAL A  1 31  ? 51.304  40.489  16.609 1.00 26.62  ? 31   VAL A CG1 1 
ATOM   225   C  CG2 . VAL A  1 31  ? 50.979  40.496  14.115 1.00 23.86  ? 31   VAL A CG2 1 
ATOM   226   N  N   . TRP A  1 32  ? 48.311  39.125  17.850 1.00 24.87  ? 32   TRP A N   1 
ATOM   227   C  CA  . TRP A  1 32  ? 47.507  39.470  19.020 1.00 24.98  ? 32   TRP A CA  1 
ATOM   228   C  C   . TRP A  1 32  ? 47.982  38.666  20.210 1.00 25.68  ? 32   TRP A C   1 
ATOM   229   O  O   . TRP A  1 32  ? 48.501  37.561  20.082 1.00 27.70  ? 32   TRP A O   1 
ATOM   230   C  CB  . TRP A  1 32  ? 46.029  39.195  18.750 1.00 30.82  ? 32   TRP A CB  1 
ATOM   231   C  CG  . TRP A  1 32  ? 45.668  37.751  18.788 1.00 29.30  ? 32   TRP A CG  1 
ATOM   232   C  CD1 . TRP A  1 32  ? 45.117  37.075  19.842 1.00 33.75  ? 32   TRP A CD1 1 
ATOM   233   C  CD2 . TRP A  1 32  ? 45.830  36.787  17.735 1.00 25.49  ? 32   TRP A CD2 1 
ATOM   234   N  NE1 . TRP A  1 32  ? 44.930  35.765  19.502 1.00 34.71  ? 32   TRP A NE1 1 
ATOM   235   C  CE2 . TRP A  1 32  ? 45.359  35.557  18.214 1.00 30.57  ? 32   TRP A CE2 1 
ATOM   236   C  CE3 . TRP A  1 32  ? 46.336  36.854  16.430 1.00 33.74  ? 32   TRP A CE3 1 
ATOM   237   C  CZ2 . TRP A  1 32  ? 45.362  34.384  17.453 1.00 37.09  ? 32   TRP A CZ2 1 
ATOM   238   C  CZ3 . TRP A  1 32  ? 46.337  35.689  15.673 1.00 34.46  ? 32   TRP A CZ3 1 
ATOM   239   C  CH2 . TRP A  1 32  ? 45.859  34.473  16.176 1.00 40.67  ? 32   TRP A CH2 1 
ATOM   240   N  N   . GLY A  1 33  ? 47.778  39.265  21.374 1.00 24.86  ? 33   GLY A N   1 
ATOM   241   C  CA  . GLY A  1 33  ? 48.112  38.530  22.595 1.00 23.78  ? 33   GLY A CA  1 
ATOM   242   C  C   . GLY A  1 33  ? 48.205  39.547  23.721 1.00 25.76  ? 33   GLY A C   1 
ATOM   243   O  O   . GLY A  1 33  ? 47.516  40.562  23.718 1.00 27.69  ? 33   GLY A O   1 
ATOM   244   N  N   . SER A  1 34  ? 49.073  39.288  24.681 1.00 25.73  ? 34   SER A N   1 
ATOM   245   C  CA  . SER A  1 34  ? 49.193  40.214  25.809 1.00 24.37  ? 34   SER A CA  1 
ATOM   246   C  C   . SER A  1 34  ? 50.618  40.197  26.341 1.00 29.18  ? 34   SER A C   1 
ATOM   247   O  O   . SER A  1 34  ? 51.278  39.156  26.246 1.00 27.58  ? 34   SER A O   1 
ATOM   248   C  CB  . SER A  1 34  ? 48.214  39.766  26.900 1.00 33.00  ? 34   SER A CB  1 
ATOM   249   O  OG  . SER A  1 34  ? 48.291  40.613  28.025 1.00 52.36  ? 34   SER A OG  1 
ATOM   250   N  N   . ILE A  1 35  ? 51.054  41.319  26.877 1.00 28.30  ? 35   ILE A N   1 
ATOM   251   C  CA  . ILE A  1 35  ? 52.328  41.447  27.558 1.00 22.03  ? 35   ILE A CA  1 
ATOM   252   C  C   . ILE A  1 35  ? 52.129  42.143  28.907 1.00 29.57  ? 35   ILE A C   1 
ATOM   253   O  O   . ILE A  1 35  ? 51.419  43.147  28.977 1.00 31.12  ? 35   ILE A O   1 
ATOM   254   C  CB  . ILE A  1 35  ? 53.327  42.246  26.715 1.00 22.70  ? 35   ILE A CB  1 
ATOM   255   C  CG1 . ILE A  1 35  ? 53.389  41.748  25.252 1.00 23.18  ? 35   ILE A CG1 1 
ATOM   256   C  CG2 . ILE A  1 35  ? 54.697  42.261  27.368 1.00 25.15  ? 35   ILE A CG2 1 
ATOM   257   C  CD1 . ILE A  1 35  ? 53.886  42.841  24.331 1.00 28.92  ? 35   ILE A CD1 1 
ATOM   258   N  N   . LYS A  1 36  ? 52.727  41.612  29.965 1.00 26.33  ? 36   LYS A N   1 
ATOM   259   C  CA  . LYS A  1 36  ? 52.533  42.189  31.295 1.00 27.39  ? 36   LYS A CA  1 
ATOM   260   C  C   . LYS A  1 36  ? 53.852  42.639  31.898 1.00 31.36  ? 36   LYS A C   1 
ATOM   261   O  O   . LYS A  1 36  ? 54.902  42.347  31.325 1.00 28.44  ? 36   LYS A O   1 
ATOM   262   C  CB  . LYS A  1 36  ? 51.871  41.204  32.243 1.00 24.32  ? 36   LYS A CB  1 
ATOM   263   C  CG  . LYS A  1 36  ? 52.600  39.877  32.446 1.00 27.30  ? 36   LYS A CG  1 
ATOM   264   C  CD  . LYS A  1 36  ? 51.682  38.934  33.204 1.00 34.12  ? 36   LYS A CD  1 
ATOM   265   C  CE  . LYS A  1 36  ? 52.379  37.645  33.620 1.00 41.70  ? 36   LYS A CE  1 
ATOM   266   N  NZ  . LYS A  1 36  ? 51.322  36.671  34.067 1.00 33.79  ? 36   LYS A NZ  1 
ATOM   267   N  N   . GLY A  1 37  ? 53.767  43.352  33.021 1.00 25.30  ? 37   GLY A N   1 
ATOM   268   C  CA  . GLY A  1 37  ? 54.990  43.793  33.677 1.00 23.17  ? 37   GLY A CA  1 
ATOM   269   C  C   . GLY A  1 37  ? 55.578  45.059  33.097 1.00 21.77  ? 37   GLY A C   1 
ATOM   270   O  O   . GLY A  1 37  ? 56.705  45.417  33.459 1.00 25.66  ? 37   GLY A O   1 
ATOM   271   N  N   . LEU A  1 38  ? 54.867  45.768  32.215 1.00 22.15  ? 38   LEU A N   1 
ATOM   272   C  CA  . LEU A  1 38  ? 55.328  46.976  31.566 1.00 22.76  ? 38   LEU A CA  1 
ATOM   273   C  C   . LEU A  1 38  ? 54.977  48.258  32.331 1.00 25.01  ? 38   LEU A C   1 
ATOM   274   O  O   . LEU A  1 38  ? 53.941  48.182  32.997 1.00 27.63  ? 38   LEU A O   1 
ATOM   275   C  CB  . LEU A  1 38  ? 54.637  47.086  30.192 1.00 25.36  ? 38   LEU A CB  1 
ATOM   276   C  CG  . LEU A  1 38  ? 55.128  46.067  29.138 1.00 26.47  ? 38   LEU A CG  1 
ATOM   277   C  CD1 . LEU A  1 38  ? 54.122  46.008  28.003 1.00 26.47  ? 38   LEU A CD1 1 
ATOM   278   C  CD2 . LEU A  1 38  ? 56.521  46.424  28.653 1.00 22.65  ? 38   LEU A CD2 1 
ATOM   279   N  N   . THR A  1 39  ? 55.739  49.333  32.219 1.00 25.05  ? 39   THR A N   1 
ATOM   280   C  CA  . THR A  1 39  ? 55.226  50.595  32.788 1.00 30.61  ? 39   THR A CA  1 
ATOM   281   C  C   . THR A  1 39  ? 54.041  51.056  31.946 1.00 36.06  ? 39   THR A C   1 
ATOM   282   O  O   . THR A  1 39  ? 53.944  50.753  30.746 1.00 27.62  ? 39   THR A O   1 
ATOM   283   C  CB  . THR A  1 39  ? 56.281  51.700  32.852 1.00 28.88  ? 39   THR A CB  1 
ATOM   284   O  OG1 . THR A  1 39  ? 56.918  51.839  31.577 1.00 28.93  ? 39   THR A OG1 1 
ATOM   285   C  CG2 . THR A  1 39  ? 57.409  51.351  33.820 1.00 28.09  ? 39   THR A CG2 1 
ATOM   286   N  N   . GLU A  1 40  ? 53.109  51.812  32.513 1.00 33.06  ? 40   GLU A N   1 
ATOM   287   C  CA  . GLU A  1 40  ? 51.983  52.325  31.706 1.00 23.53  ? 40   GLU A CA  1 
ATOM   288   C  C   . GLU A  1 40  ? 52.423  53.191  30.555 1.00 22.79  ? 40   GLU A C   1 
ATOM   289   O  O   . GLU A  1 40  ? 53.324  54.052  30.687 1.00 28.37  ? 40   GLU A O   1 
ATOM   290   C  CB  . GLU A  1 40  ? 51.080  53.119  32.686 1.00 27.14  ? 40   GLU A CB  1 
ATOM   291   C  CG  . GLU A  1 40  ? 49.918  53.838  32.001 1.00 34.04  ? 40   GLU A CG  1 
ATOM   292   C  CD  . GLU A  1 40  ? 48.998  54.561  32.971 1.00 42.33  ? 40   GLU A CD  1 
ATOM   293   O  OE1 . GLU A  1 40  ? 47.828  54.827  32.626 1.00 47.30  ? 40   GLU A OE1 1 
ATOM   294   O  OE2 . GLU A  1 40  ? 49.453  54.877  34.089 1.00 35.18  ? 40   GLU A OE2 1 
ATOM   295   N  N   . GLY A  1 41  ? 51.838  53.067  29.355 1.00 28.77  ? 41   GLY A N   1 
ATOM   296   C  CA  . GLY A  1 41  ? 52.308  53.933  28.261 1.00 27.49  ? 41   GLY A CA  1 
ATOM   297   C  C   . GLY A  1 41  ? 52.755  53.137  27.029 1.00 26.04  ? 41   GLY A C   1 
ATOM   298   O  O   . GLY A  1 41  ? 52.521  51.926  27.004 1.00 28.56  ? 41   GLY A O   1 
ATOM   299   N  N   . LEU A  1 42  ? 53.376  53.792  26.056 1.00 28.75  ? 42   LEU A N   1 
ATOM   300   C  CA  . LEU A  1 42  ? 53.773  53.157  24.799 1.00 26.72  ? 42   LEU A CA  1 
ATOM   301   C  C   . LEU A  1 42  ? 55.129  52.454  24.910 1.00 24.82  ? 42   LEU A C   1 
ATOM   302   O  O   . LEU A  1 42  ? 56.065  52.967  25.530 1.00 25.15  ? 42   LEU A O   1 
ATOM   303   C  CB  . LEU A  1 42  ? 53.886  54.183  23.668 1.00 27.09  ? 42   LEU A CB  1 
ATOM   304   C  CG  . LEU A  1 42  ? 52.600  54.911  23.251 1.00 25.07  ? 42   LEU A CG  1 
ATOM   305   C  CD1 . LEU A  1 42  ? 52.929  56.010  22.244 1.00 40.84  ? 42   LEU A CD1 1 
ATOM   306   C  CD2 . LEU A  1 42  ? 51.583  53.955  22.695 1.00 29.90  ? 42   LEU A CD2 1 
ATOM   307   N  N   . HIS A  1 43  ? 55.250  51.306  24.264 1.00 23.27  ? 43   HIS A N   1 
ATOM   308   C  CA  . HIS A  1 43  ? 56.502  50.563  24.191 1.00 23.78  ? 43   HIS A CA  1 
ATOM   309   C  C   . HIS A  1 43  ? 56.747  50.060  22.753 1.00 19.49  ? 43   HIS A C   1 
ATOM   310   O  O   . HIS A  1 43  ? 55.838  49.401  22.253 1.00 23.97  ? 43   HIS A O   1 
ATOM   311   C  CB  . HIS A  1 43  ? 56.467  49.364  25.127 1.00 23.59  ? 43   HIS A CB  1 
ATOM   312   C  CG  . HIS A  1 43  ? 56.322  49.767  26.569 1.00 27.04  ? 43   HIS A CG  1 
ATOM   313   N  ND1 . HIS A  1 43  ? 57.409  49.996  27.377 1.00 30.43  ? 43   HIS A ND1 1 
ATOM   314   C  CD2 . HIS A  1 43  ? 55.218  49.985  27.330 1.00 25.18  ? 43   HIS A CD2 1 
ATOM   315   C  CE1 . HIS A  1 43  ? 56.999  50.336  28.594 1.00 27.86  ? 43   HIS A CE1 1 
ATOM   316   N  NE2 . HIS A  1 43  ? 55.677  50.336  28.578 1.00 28.81  ? 43   HIS A NE2 1 
ATOM   317   N  N   . GLY A  1 44  ? 57.927  50.384  22.238 1.00 23.82  ? 44   GLY A N   1 
ATOM   318   C  CA  . GLY A  1 44  ? 58.375  49.950  20.928 1.00 26.46  ? 44   GLY A CA  1 
ATOM   319   C  C   . GLY A  1 44  ? 58.272  48.433  20.817 1.00 25.68  ? 44   GLY A C   1 
ATOM   320   O  O   . GLY A  1 44  ? 58.451  47.689  21.791 1.00 23.87  ? 44   GLY A O   1 
ATOM   321   N  N   . PHE A  1 45  ? 57.949  47.959  19.619 1.00 21.40  ? 45   PHE A N   1 
ATOM   322   C  CA  . PHE A  1 45  ? 57.610  46.561  19.392 1.00 21.78  ? 45   PHE A CA  1 
ATOM   323   C  C   . PHE A  1 45  ? 58.049  46.159  17.998 1.00 27.89  ? 45   PHE A C   1 
ATOM   324   O  O   . PHE A  1 45  ? 57.480  46.627  16.999 1.00 24.19  ? 45   PHE A O   1 
ATOM   325   C  CB  . PHE A  1 45  ? 56.104  46.421  19.534 1.00 22.76  ? 45   PHE A CB  1 
ATOM   326   C  CG  . PHE A  1 45  ? 55.501  45.046  19.591 1.00 22.33  ? 45   PHE A CG  1 
ATOM   327   C  CD1 . PHE A  1 45  ? 55.897  44.109  20.531 1.00 24.34  ? 45   PHE A CD1 1 
ATOM   328   C  CD2 . PHE A  1 45  ? 54.502  44.686  18.698 1.00 22.89  ? 45   PHE A CD2 1 
ATOM   329   C  CE1 . PHE A  1 45  ? 55.331  42.860  20.592 1.00 24.41  ? 45   PHE A CE1 1 
ATOM   330   C  CE2 . PHE A  1 45  ? 53.922  43.438  18.758 1.00 22.65  ? 45   PHE A CE2 1 
ATOM   331   C  CZ  . PHE A  1 45  ? 54.310  42.517  19.718 1.00 24.12  ? 45   PHE A CZ  1 
ATOM   332   N  N   . HIS A  1 46  ? 59.090  45.349  17.850 1.00 23.03  ? 46   HIS A N   1 
ATOM   333   C  CA  . HIS A  1 46  ? 59.613  45.076  16.510 1.00 22.26  ? 46   HIS A CA  1 
ATOM   334   C  C   . HIS A  1 46  ? 60.098  43.627  16.380 1.00 28.57  ? 46   HIS A C   1 
ATOM   335   O  O   . HIS A  1 46  ? 60.421  42.972  17.359 1.00 20.60  ? 46   HIS A O   1 
ATOM   336   C  CB  . HIS A  1 46  ? 60.819  45.942  16.118 1.00 22.96  ? 46   HIS A CB  1 
ATOM   337   C  CG  . HIS A  1 46  ? 60.845  47.311  16.734 1.00 28.22  ? 46   HIS A CG  1 
ATOM   338   N  ND1 . HIS A  1 46  ? 61.623  47.677  17.808 1.00 25.47  ? 46   HIS A ND1 1 
ATOM   339   C  CD2 . HIS A  1 46  ? 60.105  48.402  16.396 1.00 23.72  ? 46   HIS A CD2 1 
ATOM   340   C  CE1 . HIS A  1 46  ? 61.388  48.950  18.095 1.00 28.63  ? 46   HIS A CE1 1 
ATOM   341   N  NE2 . HIS A  1 46  ? 60.470  49.411  17.257 1.00 24.31  ? 46   HIS A NE2 1 
ATOM   342   N  N   . VAL A  1 47  ? 60.178  43.192  15.130 1.00 20.42  ? 47   VAL A N   1 
ATOM   343   C  CA  . VAL A  1 47  ? 60.890  41.949  14.799 1.00 18.05  ? 47   VAL A CA  1 
ATOM   344   C  C   . VAL A  1 47  ? 62.335  42.326  14.497 1.00 21.38  ? 47   VAL A C   1 
ATOM   345   O  O   . VAL A  1 47  ? 62.638  43.151  13.625 1.00 23.05  ? 47   VAL A O   1 
ATOM   346   C  CB  . VAL A  1 47  ? 60.263  41.211  13.622 1.00 20.25  ? 47   VAL A CB  1 
ATOM   347   C  CG1 . VAL A  1 47  ? 60.978  39.892  13.308 1.00 17.66  ? 47   VAL A CG1 1 
ATOM   348   C  CG2 . VAL A  1 47  ? 58.783  40.880  13.880 1.00 25.16  ? 47   VAL A CG2 1 
ATOM   349   N  N   . HIS A  1 48  ? 63.282  41.719  15.220 1.00 22.86  ? 48   HIS A N   1 
ATOM   350   C  CA  . HIS A  1 48  ? 64.701  41.892  14.982 1.00 21.29  ? 48   HIS A CA  1 
ATOM   351   C  C   . HIS A  1 48  ? 65.261  40.742  14.143 1.00 21.26  ? 48   HIS A C   1 
ATOM   352   O  O   . HIS A  1 48  ? 64.624  39.690  14.075 1.00 21.93  ? 48   HIS A O   1 
ATOM   353   C  CB  . HIS A  1 48  ? 65.461  41.949  16.316 1.00 22.07  ? 48   HIS A CB  1 
ATOM   354   C  CG  . HIS A  1 48  ? 65.148  43.246  17.020 1.00 23.35  ? 48   HIS A CG  1 
ATOM   355   N  ND1 . HIS A  1 48  ? 66.165  44.073  17.436 1.00 22.32  ? 48   HIS A ND1 1 
ATOM   356   C  CD2 . HIS A  1 48  ? 63.974  43.831  17.370 1.00 18.61  ? 48   HIS A CD2 1 
ATOM   357   C  CE1 . HIS A  1 48  ? 65.620  45.155  18.018 1.00 24.30  ? 48   HIS A CE1 1 
ATOM   358   N  NE2 . HIS A  1 48  ? 64.316  45.011  17.992 1.00 20.99  ? 48   HIS A NE2 1 
ATOM   359   N  N   . GLU A  1 49  ? 66.409  41.003  13.518 1.00 20.52  ? 49   GLU A N   1 
ATOM   360   C  CA  . GLU A  1 49  ? 66.833  40.115  12.449 1.00 22.63  ? 49   GLU A CA  1 
ATOM   361   C  C   . GLU A  1 49  ? 67.131  38.690  12.881 1.00 25.15  ? 49   GLU A C   1 
ATOM   362   O  O   . GLU A  1 49  ? 66.735  37.761  12.152 1.00 21.86  ? 49   GLU A O   1 
ATOM   363   C  CB  . GLU A  1 49  ? 68.076  40.715  11.753 1.00 23.77  ? 49   GLU A CB  1 
ATOM   364   C  CG  . GLU A  1 49  ? 68.456  39.822  10.550 1.00 27.79  ? 49   GLU A CG  1 
ATOM   365   C  CD  . GLU A  1 49  ? 69.513  40.487  9.680  1.00 38.27  ? 49   GLU A CD  1 
ATOM   366   O  OE1 . GLU A  1 49  ? 69.988  39.806  8.735  1.00 35.63  ? 49   GLU A OE1 1 
ATOM   367   O  OE2 . GLU A  1 49  ? 69.853  41.658  9.960  1.00 29.99  ? 49   GLU A OE2 1 
ATOM   368   N  N   . PHE A  1 50  ? 67.807  38.486  14.012 1.00 20.92  ? 50   PHE A N   1 
ATOM   369   C  CA  . PHE A  1 50  ? 68.261  37.119  14.336 1.00 20.19  ? 50   PHE A CA  1 
ATOM   370   C  C   . PHE A  1 50  ? 67.482  36.500  15.472 1.00 21.79  ? 50   PHE A C   1 
ATOM   371   O  O   . PHE A  1 50  ? 67.190  37.199  16.451 1.00 22.54  ? 50   PHE A O   1 
ATOM   372   C  CB  . PHE A  1 50  ? 69.766  37.109  14.686 1.00 20.50  ? 50   PHE A CB  1 
ATOM   373   C  CG  . PHE A  1 50  ? 70.567  37.816  13.601 1.00 20.46  ? 50   PHE A CG  1 
ATOM   374   C  CD1 . PHE A  1 50  ? 70.699  37.209  12.361 1.00 26.18  ? 50   PHE A CD1 1 
ATOM   375   C  CD2 . PHE A  1 50  ? 71.146  39.048  13.846 1.00 23.17  ? 50   PHE A CD2 1 
ATOM   376   C  CE1 . PHE A  1 50  ? 71.410  37.889  11.376 1.00 30.75  ? 50   PHE A CE1 1 
ATOM   377   C  CE2 . PHE A  1 50  ? 71.836  39.731  12.852 1.00 24.19  ? 50   PHE A CE2 1 
ATOM   378   C  CZ  . PHE A  1 50  ? 71.959  39.146  11.614 1.00 23.99  ? 50   PHE A CZ  1 
ATOM   379   N  N   . GLY A  1 51  ? 67.180  35.210  15.338 1.00 18.40  ? 51   GLY A N   1 
ATOM   380   C  CA  . GLY A  1 51  ? 66.455  34.509  16.415 1.00 18.48  ? 51   GLY A CA  1 
ATOM   381   C  C   . GLY A  1 51  ? 67.538  33.905  17.319 1.00 20.94  ? 51   GLY A C   1 
ATOM   382   O  O   . GLY A  1 51  ? 67.574  32.706  17.534 1.00 20.74  ? 51   GLY A O   1 
ATOM   383   N  N   . ASP A  1 52  ? 68.426  34.774  17.782 1.00 22.97  ? 52   ASP A N   1 
ATOM   384   C  CA  . ASP A  1 52  ? 69.582  34.329  18.579 1.00 22.02  ? 52   ASP A CA  1 
ATOM   385   C  C   . ASP A  1 52  ? 69.416  34.889  19.991 1.00 25.64  ? 52   ASP A C   1 
ATOM   386   O  O   . ASP A  1 52  ? 69.532  36.105  20.165 1.00 23.82  ? 52   ASP A O   1 
ATOM   387   C  CB  . ASP A  1 52  ? 70.850  34.814  17.925 1.00 18.71  ? 52   ASP A CB  1 
ATOM   388   C  CG  . ASP A  1 52  ? 72.133  34.466  18.664 1.00 24.90  ? 52   ASP A CG  1 
ATOM   389   O  OD1 . ASP A  1 52  ? 73.191  34.385  18.012 1.00 21.99  ? 52   ASP A OD1 1 
ATOM   390   O  OD2 . ASP A  1 52  ? 72.136  34.250  19.891 1.00 21.15  ? 52   ASP A OD2 1 
ATOM   391   N  N   . ASN A  1 53  ? 69.121  34.037  20.949 1.00 23.27  ? 53   ASN A N   1 
ATOM   392   C  CA  . ASN A  1 53  ? 68.863  34.451  22.325 1.00 22.96  ? 53   ASN A CA  1 
ATOM   393   C  C   . ASN A  1 53  ? 70.041  34.063  23.210 1.00 21.10  ? 53   ASN A C   1 
ATOM   394   O  O   . ASN A  1 53  ? 69.930  33.986  24.438 1.00 23.04  ? 53   ASN A O   1 
ATOM   395   C  CB  . ASN A  1 53  ? 67.554  33.797  22.786 1.00 24.64  ? 53   ASN A CB  1 
ATOM   396   C  CG  . ASN A  1 53  ? 67.031  34.346  24.096 1.00 38.63  ? 53   ASN A CG  1 
ATOM   397   O  OD1 . ASN A  1 53  ? 67.001  33.660  25.118 1.00 44.45  ? 53   ASN A OD1 1 
ATOM   398   N  ND2 . ASN A  1 53  ? 66.621  35.612  24.059 1.00 40.70  ? 53   ASN A ND2 1 
ATOM   399   N  N   . THR A  1 54  ? 71.200  33.823  22.595 1.00 20.91  ? 54   THR A N   1 
ATOM   400   C  CA  . THR A  1 54  ? 72.365  33.398  23.379 1.00 21.46  ? 54   THR A CA  1 
ATOM   401   C  C   . THR A  1 54  ? 72.864  34.479  24.336 1.00 25.30  ? 54   THR A C   1 
ATOM   402   O  O   . THR A  1 54  ? 73.519  34.155  25.354 1.00 22.67  ? 54   THR A O   1 
ATOM   403   C  CB  . THR A  1 54  ? 73.564  32.947  22.518 1.00 22.85  ? 54   THR A CB  1 
ATOM   404   O  OG1 . THR A  1 54  ? 73.979  33.987  21.638 1.00 23.32  ? 54   THR A OG1 1 
ATOM   405   C  CG2 . THR A  1 54  ? 73.215  31.757  21.631 1.00 22.76  ? 54   THR A CG2 1 
ATOM   406   N  N   . ALA A  1 55  ? 72.592  35.741  24.041 1.00 20.59  ? 55   ALA A N   1 
ATOM   407   C  CA  . ALA A  1 55  ? 72.866  36.862  24.929 1.00 17.10  ? 55   ALA A CA  1 
ATOM   408   C  C   . ALA A  1 55  ? 71.550  37.526  25.327 1.00 19.79  ? 55   ALA A C   1 
ATOM   409   O  O   . ALA A  1 55  ? 71.430  38.742  25.418 1.00 26.37  ? 55   ALA A O   1 
ATOM   410   C  CB  . ALA A  1 55  ? 73.795  37.866  24.274 1.00 19.03  ? 55   ALA A CB  1 
ATOM   411   N  N   . GLY A  1 56  ? 70.515  36.740  25.541 1.00 21.93  ? 56   GLY A N   1 
ATOM   412   C  CA  . GLY A  1 56  ? 69.203  37.333  25.756 1.00 27.06  ? 56   GLY A CA  1 
ATOM   413   C  C   . GLY A  1 56  ? 68.777  38.138  24.548 1.00 29.57  ? 56   GLY A C   1 
ATOM   414   O  O   . GLY A  1 56  ? 69.008  37.776  23.391 1.00 23.76  ? 56   GLY A O   1 
ATOM   415   N  N   . CYS A  1 57  ? 68.138  39.282  24.780 1.00 24.60  ? 57   CYS A N   1 
ATOM   416   C  CA  . CYS A  1 57  ? 67.655  40.039  23.620 1.00 28.52  ? 57   CYS A CA  1 
ATOM   417   C  C   . CYS A  1 57  ? 68.780  40.734  22.880 1.00 24.79  ? 57   CYS A C   1 
ATOM   418   O  O   . CYS A  1 57  ? 68.633  41.188  21.739 1.00 24.33  ? 57   CYS A O   1 
ATOM   419   C  CB  A CYS A  1 57  ? 66.637  41.085  24.085 0.40 29.80  ? 57   CYS A CB  1 
ATOM   420   C  CB  B CYS A  1 57  ? 66.592  41.049  24.045 0.60 30.77  ? 57   CYS A CB  1 
ATOM   421   S  SG  A CYS A  1 57  ? 65.299  40.401  25.096 0.40 35.37  ? 57   CYS A SG  1 
ATOM   422   S  SG  B CYS A  1 57  ? 65.353  40.432  25.204 0.60 31.98  ? 57   CYS A SG  1 
ATOM   423   N  N   . THR A  1 58  ? 69.940  40.820  23.540 1.00 20.99  ? 58   THR A N   1 
ATOM   424   C  CA  . THR A  1 58  ? 71.045  41.567  22.948 1.00 23.39  ? 58   THR A CA  1 
ATOM   425   C  C   . THR A  1 58  ? 71.581  40.917  21.682 1.00 26.65  ? 58   THR A C   1 
ATOM   426   O  O   . THR A  1 58  ? 72.073  41.609  20.797 1.00 31.39  ? 58   THR A O   1 
ATOM   427   C  CB  . THR A  1 58  ? 72.198  41.700  23.968 1.00 31.68  ? 58   THR A CB  1 
ATOM   428   O  OG1 . THR A  1 58  ? 71.651  42.130  25.220 1.00 33.25  ? 58   THR A OG1 1 
ATOM   429   C  CG2 . THR A  1 58  ? 73.176  42.782  23.538 1.00 44.95  ? 58   THR A CG2 1 
ATOM   430   N  N   . SER A  1 59  ? 71.504  39.595  21.550 1.00 21.21  ? 59   SER A N   1 
ATOM   431   C  CA  . SER A  1 59  ? 72.089  38.964  20.371 1.00 19.35  ? 59   SER A CA  1 
ATOM   432   C  C   . SER A  1 59  ? 71.104  38.961  19.212 1.00 23.81  ? 59   SER A C   1 
ATOM   433   O  O   . SER A  1 59  ? 71.440  38.424  18.157 1.00 21.36  ? 59   SER A O   1 
ATOM   434   C  CB  . SER A  1 59  ? 72.491  37.525  20.696 1.00 21.27  ? 59   SER A CB  1 
ATOM   435   O  OG  . SER A  1 59  ? 71.570  37.010  21.680 1.00 20.39  ? 59   SER A OG  1 
ATOM   436   N  N   . ALA A  1 60  ? 69.914  39.553  19.361 1.00 21.04  ? 60   ALA A N   1 
ATOM   437   C  CA  . ALA A  1 60  ? 68.959  39.510  18.255 1.00 19.98  ? 60   ALA A CA  1 
ATOM   438   C  C   . ALA A  1 60  ? 69.311  40.438  17.104 1.00 23.07  ? 60   ALA A C   1 
ATOM   439   O  O   . ALA A  1 60  ? 68.653  40.369  16.055 1.00 24.68  ? 60   ALA A O   1 
ATOM   440   C  CB  . ALA A  1 60  ? 67.564  39.859  18.783 1.00 22.26  ? 60   ALA A CB  1 
ATOM   441   N  N   . GLY A  1 61  ? 70.292  41.320  17.236 1.00 19.88  ? 61   GLY A N   1 
ATOM   442   C  CA  . GLY A  1 61  ? 70.690  42.159  16.105 1.00 19.83  ? 61   GLY A CA  1 
ATOM   443   C  C   . GLY A  1 61  ? 69.745  43.343  15.964 1.00 21.81  ? 61   GLY A C   1 
ATOM   444   O  O   . GLY A  1 61  ? 68.940  43.577  16.864 1.00 24.17  ? 61   GLY A O   1 
ATOM   445   N  N   . PRO A  1 62  ? 69.846  44.063  14.866 1.00 24.07  ? 62   PRO A N   1 
ATOM   446   C  CA  . PRO A  1 62  ? 68.987  45.240  14.623 1.00 22.17  ? 62   PRO A CA  1 
ATOM   447   C  C   . PRO A  1 62  ? 67.604  44.859  14.142 1.00 22.35  ? 62   PRO A C   1 
ATOM   448   O  O   . PRO A  1 62  ? 67.241  43.694  14.006 1.00 22.25  ? 62   PRO A O   1 
ATOM   449   C  CB  . PRO A  1 62  ? 69.775  45.977  13.529 1.00 23.48  ? 62   PRO A CB  1 
ATOM   450   C  CG  . PRO A  1 62  ? 70.456  44.884  12.761 1.00 27.03  ? 62   PRO A CG  1 
ATOM   451   C  CD  . PRO A  1 62  ? 70.823  43.831  13.779 1.00 24.29  ? 62   PRO A CD  1 
ATOM   452   N  N   . HIS A  1 63  ? 66.743  45.847  13.853 1.00 24.14  ? 63   HIS A N   1 
ATOM   453   C  CA  . HIS A  1 63  ? 65.423  45.539  13.316 1.00 21.54  ? 63   HIS A CA  1 
ATOM   454   C  C   . HIS A  1 63  ? 65.535  44.754  12.002 1.00 20.62  ? 63   HIS A C   1 
ATOM   455   O  O   . HIS A  1 63  ? 66.433  45.042  11.204 1.00 23.99  ? 63   HIS A O   1 
ATOM   456   C  CB  . HIS A  1 63  ? 64.652  46.845  13.074 1.00 22.80  ? 63   HIS A CB  1 
ATOM   457   C  CG  . HIS A  1 63  ? 64.378  47.679  14.293 1.00 29.13  ? 63   HIS A CG  1 
ATOM   458   N  ND1 . HIS A  1 63  ? 63.673  48.875  14.285 1.00 25.10  ? 63   HIS A ND1 1 
ATOM   459   C  CD2 . HIS A  1 63  ? 64.727  47.467  15.588 1.00 32.15  ? 63   HIS A CD2 1 
ATOM   460   C  CE1 . HIS A  1 63  ? 63.607  49.360  15.512 1.00 27.56  ? 63   HIS A CE1 1 
ATOM   461   N  NE2 . HIS A  1 63  ? 64.242  48.522  16.323 1.00 34.34  ? 63   HIS A NE2 1 
ATOM   462   N  N   . PHE A  1 64  ? 64.651  43.804  11.762 1.00 20.33  ? 64   PHE A N   1 
ATOM   463   C  CA  . PHE A  1 64  ? 64.700  43.016  10.511 1.00 20.78  ? 64   PHE A CA  1 
ATOM   464   C  C   . PHE A  1 64  ? 64.481  43.943  9.319  1.00 26.91  ? 64   PHE A C   1 
ATOM   465   O  O   . PHE A  1 64  ? 63.425  44.570  9.245  1.00 22.49  ? 64   PHE A O   1 
ATOM   466   C  CB  . PHE A  1 64  ? 63.677  41.913  10.554 1.00 22.06  ? 64   PHE A CB  1 
ATOM   467   C  CG  . PHE A  1 64  ? 63.574  41.030  9.312  1.00 23.91  ? 64   PHE A CG  1 
ATOM   468   C  CD1 . PHE A  1 64  ? 62.323  40.688  8.829  1.00 21.41  ? 64   PHE A CD1 1 
ATOM   469   C  CD2 . PHE A  1 64  ? 64.722  40.575  8.682  1.00 26.07  ? 64   PHE A CD2 1 
ATOM   470   C  CE1 . PHE A  1 64  ? 62.207  39.889  7.704  1.00 23.44  ? 64   PHE A CE1 1 
ATOM   471   C  CE2 . PHE A  1 64  ? 64.607  39.765  7.557  1.00 31.93  ? 64   PHE A CE2 1 
ATOM   472   C  CZ  . PHE A  1 64  ? 63.350  39.426  7.079  1.00 27.68  ? 64   PHE A CZ  1 
ATOM   473   N  N   . ASN A  1 65  ? 65.471  44.039  8.415  1.00 22.98  ? 65   ASN A N   1 
ATOM   474   C  CA  . ASN A  1 65  ? 65.376  45.084  7.382  1.00 24.65  ? 65   ASN A CA  1 
ATOM   475   C  C   . ASN A  1 65  ? 65.869  44.564  6.036  1.00 29.14  ? 65   ASN A C   1 
ATOM   476   O  O   . ASN A  1 65  ? 66.894  45.061  5.570  1.00 29.94  ? 65   ASN A O   1 
ATOM   477   C  CB  . ASN A  1 65  ? 66.199  46.285  7.822  1.00 23.87  ? 65   ASN A CB  1 
ATOM   478   C  CG  . ASN A  1 65  ? 66.141  47.494  6.912  1.00 25.72  ? 65   ASN A CG  1 
ATOM   479   O  OD1 . ASN A  1 65  ? 65.193  47.678  6.152  1.00 28.66  ? 65   ASN A OD1 1 
ATOM   480   N  ND2 . ASN A  1 65  ? 67.128  48.389  6.994  1.00 27.11  ? 65   ASN A ND2 1 
ATOM   481   N  N   . PRO A  1 66  ? 65.208  43.591  5.435  1.00 26.31  ? 66   PRO A N   1 
ATOM   482   C  CA  . PRO A  1 66  ? 65.713  43.020  4.177  1.00 29.06  ? 66   PRO A CA  1 
ATOM   483   C  C   . PRO A  1 66  ? 65.752  43.994  3.016  1.00 32.39  ? 66   PRO A C   1 
ATOM   484   O  O   . PRO A  1 66  ? 66.479  43.753  2.046  1.00 35.52  ? 66   PRO A O   1 
ATOM   485   C  CB  . PRO A  1 66  ? 64.691  41.911  3.857  1.00 28.81  ? 66   PRO A CB  1 
ATOM   486   C  CG  . PRO A  1 66  ? 63.453  42.341  4.581  1.00 28.94  ? 66   PRO A CG  1 
ATOM   487   C  CD  . PRO A  1 66  ? 63.973  42.920  5.877  1.00 22.42  ? 66   PRO A CD  1 
ATOM   488   N  N   . LEU A  1 67  ? 64.998  45.081  3.032  1.00 31.35  ? 67   LEU A N   1 
ATOM   489   C  CA  . LEU A  1 67  ? 64.965  45.980  1.874  1.00 25.83  ? 67   LEU A CA  1 
ATOM   490   C  C   . LEU A  1 67  ? 65.834  47.201  2.070  1.00 39.24  ? 67   LEU A C   1 
ATOM   491   O  O   . LEU A  1 67  ? 65.853  48.099  1.220  1.00 45.17  ? 67   LEU A O   1 
ATOM   492   C  CB  . LEU A  1 67  ? 63.506  46.384  1.618  1.00 31.38  ? 67   LEU A CB  1 
ATOM   493   C  CG  . LEU A  1 67  ? 62.597  45.182  1.326  1.00 34.76  ? 67   LEU A CG  1 
ATOM   494   C  CD1 . LEU A  1 67  ? 61.146  45.595  1.193  1.00 40.87  ? 67   LEU A CD1 1 
ATOM   495   C  CD2 . LEU A  1 67  ? 63.087  44.483  0.062  1.00 47.40  ? 67   LEU A CD2 1 
ATOM   496   N  N   . SER A  1 68  ? 66.554  47.215  3.189  1.00 32.76  ? 68   SER A N   1 
ATOM   497   C  CA  . SER A  1 68  ? 67.534  48.242  3.488  1.00 28.82  ? 68   SER A CA  1 
ATOM   498   C  C   . SER A  1 68  ? 66.935  49.639  3.547  1.00 34.03  ? 68   SER A C   1 
ATOM   499   O  O   . SER A  1 68  ? 67.441  50.573  2.909  1.00 40.18  ? 68   SER A O   1 
ATOM   500   C  CB  . SER A  1 68  ? 68.651  48.214  2.428  1.00 38.18  ? 68   SER A CB  1 
ATOM   501   O  OG  . SER A  1 68  ? 69.220  46.912  2.364  1.00 46.21  ? 68   SER A OG  1 
ATOM   502   N  N   . ARG A  1 69  ? 65.859  49.800  4.313  1.00 35.60  ? 69   ARG A N   1 
ATOM   503   C  CA  . ARG A  1 69  ? 65.222  51.120  4.417  1.00 36.14  ? 69   ARG A CA  1 
ATOM   504   C  C   . ARG A  1 69  ? 65.467  51.719  5.792  1.00 34.07  ? 69   ARG A C   1 
ATOM   505   O  O   . ARG A  1 69  ? 66.070  51.038  6.628  1.00 34.30  ? 69   ARG A O   1 
ATOM   506   C  CB  . ARG A  1 69  ? 63.740  50.980  4.086  1.00 37.93  ? 69   ARG A CB  1 
ATOM   507   C  CG  . ARG A  1 69  ? 63.491  50.664  2.608  1.00 42.18  ? 69   ARG A CG  1 
ATOM   508   C  CD  . ARG A  1 69  ? 62.010  50.457  2.357  1.00 50.86  ? 69   ARG A CD  1 
ATOM   509   N  NE  . ARG A  1 69  ? 61.695  50.006  1.000  1.00 54.14  ? 69   ARG A NE  1 
ATOM   510   C  CZ  . ARG A  1 69  ? 60.449  49.693  0.647  1.00 61.87  ? 69   ARG A CZ  1 
ATOM   511   N  NH1 . ARG A  1 69  ? 60.169  49.283  -0.581 1.00 49.78  ? 69   ARG A NH1 1 
ATOM   512   N  NH2 . ARG A  1 69  ? 59.477  49.799  1.548  1.00 70.78  ? 69   ARG A NH2 1 
ATOM   513   N  N   . LYS A  1 70  ? 65.038  52.947  6.035  1.00 30.82  ? 70   LYS A N   1 
ATOM   514   C  CA  . LYS A  1 70  ? 65.098  53.595  7.342  1.00 29.69  ? 70   LYS A CA  1 
ATOM   515   C  C   . LYS A  1 70  ? 63.978  53.129  8.269  1.00 26.03  ? 70   LYS A C   1 
ATOM   516   O  O   . LYS A  1 70  ? 62.944  52.656  7.779  1.00 26.76  ? 70   LYS A O   1 
ATOM   517   C  CB  . LYS A  1 70  ? 64.968  55.118  7.189  1.00 36.11  ? 70   LYS A CB  1 
ATOM   518   C  CG  . LYS A  1 70  ? 66.303  55.827  6.964  1.00 48.25  ? 70   LYS A CG  1 
ATOM   519   C  CD  . LYS A  1 70  ? 66.088  57.182  6.304  1.00 59.76  ? 70   LYS A CD  1 
ATOM   520   C  CE  . LYS A  1 70  ? 67.395  57.889  6.000  1.00 69.23  ? 70   LYS A CE  1 
ATOM   521   N  NZ  . LYS A  1 70  ? 67.950  58.642  7.162  1.00 76.11  ? 70   LYS A NZ  1 
ATOM   522   N  N   . HIS A  1 71  ? 64.177  53.259  9.576  1.00 26.80  ? 71   HIS A N   1 
ATOM   523   C  CA  . HIS A  1 71  ? 63.154  52.902  10.555 1.00 23.91  ? 71   HIS A CA  1 
ATOM   524   C  C   . HIS A  1 71  ? 61.896  53.754  10.384 1.00 26.30  ? 71   HIS A C   1 
ATOM   525   O  O   . HIS A  1 71  ? 62.058  54.953  10.130 1.00 31.39  ? 71   HIS A O   1 
ATOM   526   C  CB  . HIS A  1 71  ? 63.669  53.139  11.985 1.00 21.48  ? 71   HIS A CB  1 
ATOM   527   C  CG  . HIS A  1 71  ? 62.669  52.804  13.051 1.00 22.63  ? 71   HIS A CG  1 
ATOM   528   N  ND1 . HIS A  1 71  ? 62.256  51.516  13.343 1.00 24.28  ? 71   HIS A ND1 1 
ATOM   529   C  CD2 . HIS A  1 71  ? 61.983  53.636  13.887 1.00 20.70  ? 71   HIS A CD2 1 
ATOM   530   C  CE1 . HIS A  1 71  ? 61.362  51.554  14.326 1.00 26.66  ? 71   HIS A CE1 1 
ATOM   531   N  NE2 . HIS A  1 71  ? 61.180  52.842  14.668 1.00 25.57  ? 71   HIS A NE2 1 
ATOM   532   N  N   . GLY A  1 72  ? 60.720  53.193  10.532 1.00 26.28  ? 72   GLY A N   1 
ATOM   533   C  CA  . GLY A  1 72  ? 59.472  53.962  10.445 1.00 27.67  ? 72   GLY A CA  1 
ATOM   534   C  C   . GLY A  1 72  ? 58.389  53.349  11.302 1.00 32.81  ? 72   GLY A C   1 
ATOM   535   O  O   . GLY A  1 72  ? 58.644  52.393  12.043 1.00 29.27  ? 72   GLY A O   1 
ATOM   536   N  N   . GLY A  1 73  ? 57.164  53.866  11.218 1.00 29.62  ? 73   GLY A N   1 
ATOM   537   C  CA  . GLY A  1 73  ? 55.990  53.255  11.808 1.00 29.60  ? 73   GLY A CA  1 
ATOM   538   C  C   . GLY A  1 73  ? 55.437  52.149  10.922 1.00 28.24  ? 73   GLY A C   1 
ATOM   539   O  O   . GLY A  1 73  ? 55.793  52.100  9.740  1.00 31.46  ? 73   GLY A O   1 
ATOM   540   N  N   . PRO A  1 74  ? 54.578  51.258  11.381 1.00 22.08  ? 74   PRO A N   1 
ATOM   541   C  CA  . PRO A  1 74  ? 54.120  50.153  10.534 1.00 21.51  ? 74   PRO A CA  1 
ATOM   542   C  C   . PRO A  1 74  ? 53.334  50.647  9.318  1.00 36.98  ? 74   PRO A C   1 
ATOM   543   O  O   . PRO A  1 74  ? 53.239  49.963  8.295  1.00 27.84  ? 74   PRO A O   1 
ATOM   544   C  CB  . PRO A  1 74  ? 53.187  49.340  11.412 1.00 26.26  ? 74   PRO A CB  1 
ATOM   545   C  CG  . PRO A  1 74  ? 52.947  50.143  12.642 1.00 29.07  ? 74   PRO A CG  1 
ATOM   546   C  CD  . PRO A  1 74  ? 53.989  51.210  12.721 1.00 26.89  ? 74   PRO A CD  1 
ATOM   547   N  N   . LYS A  1 75  ? 52.758  51.840  9.429  1.00 31.02  ? 75   LYS A N   1 
ATOM   548   C  CA  . LYS A  1 75  ? 51.940  52.321  8.316  1.00 35.78  ? 75   LYS A CA  1 
ATOM   549   C  C   . LYS A  1 75  ? 52.713  53.226  7.377  1.00 37.22  ? 75   LYS A C   1 
ATOM   550   O  O   . LYS A  1 75  ? 52.154  53.794  6.433  1.00 47.42  ? 75   LYS A O   1 
ATOM   551   C  CB  . LYS A  1 75  ? 50.698  53.015  8.900  1.00 40.51  ? 75   LYS A CB  1 
ATOM   552   C  CG  . LYS A  1 75  ? 49.827  52.040  9.693  1.00 38.72  ? 75   LYS A CG  1 
ATOM   553   C  CD  . LYS A  1 75  ? 49.755  50.691  8.984  1.00 40.64  ? 75   LYS A CD  1 
ATOM   554   C  CE  . LYS A  1 75  ? 48.550  49.871  9.400  1.00 39.62  ? 75   LYS A CE  1 
ATOM   555   N  NZ  . LYS A  1 75  ? 48.491  48.528  8.740  1.00 43.60  ? 75   LYS A NZ  1 
ATOM   556   N  N   . ASP A  1 76  ? 54.013  53.392  7.574  1.00 30.94  ? 76   ASP A N   1 
ATOM   557   C  CA  . ASP A  1 76  ? 54.840  54.202  6.676  1.00 26.50  ? 76   ASP A CA  1 
ATOM   558   C  C   . ASP A  1 76  ? 55.286  53.371  5.479  1.00 42.43  ? 76   ASP A C   1 
ATOM   559   O  O   . ASP A  1 76  ? 55.522  52.171  5.637  1.00 38.50  ? 76   ASP A O   1 
ATOM   560   C  CB  . ASP A  1 76  ? 56.078  54.760  7.361  1.00 26.79  ? 76   ASP A CB  1 
ATOM   561   C  CG  . ASP A  1 76  ? 55.732  55.703  8.497  1.00 42.04  ? 76   ASP A CG  1 
ATOM   562   O  OD1 . ASP A  1 76  ? 56.593  55.923  9.373  1.00 37.38  ? 76   ASP A OD1 1 
ATOM   563   O  OD2 . ASP A  1 76  ? 54.583  56.208  8.503  1.00 50.52  ? 76   ASP A OD2 1 
ATOM   564   N  N   . GLU A  1 77  ? 55.425  53.965  4.294  1.00 44.96  ? 77   GLU A N   1 
ATOM   565   C  CA  . GLU A  1 77  ? 55.996  53.159  3.203  1.00 43.78  ? 77   GLU A CA  1 
ATOM   566   C  C   . GLU A  1 77  ? 57.487  52.971  3.469  1.00 34.62  ? 77   GLU A C   1 
ATOM   567   O  O   . GLU A  1 77  ? 58.044  51.916  3.171  1.00 39.90  ? 77   GLU A O   1 
ATOM   568   C  CB  . GLU A  1 77  ? 55.761  53.788  1.835  1.00 55.67  ? 77   GLU A CB  1 
ATOM   569   C  CG  . GLU A  1 77  ? 55.559  52.797  0.705  1.00 68.92  ? 77   GLU A CG  1 
ATOM   570   C  CD  . GLU A  1 77  ? 56.779  51.963  0.377  1.00 76.55  ? 77   GLU A CD  1 
ATOM   571   O  OE1 . GLU A  1 77  ? 57.911  52.432  0.625  1.00 82.91  ? 77   GLU A OE1 1 
ATOM   572   O  OE2 . GLU A  1 77  ? 56.607  50.835  -0.139 1.00 78.54  ? 77   GLU A OE2 1 
ATOM   573   N  N   . GLU A  1 78  ? 58.140  53.986  4.039  1.00 29.59  ? 78   GLU A N   1 
ATOM   574   C  CA  . GLU A  1 78  ? 59.535  53.806  4.404  1.00 30.12  ? 78   GLU A CA  1 
ATOM   575   C  C   . GLU A  1 78  ? 59.611  53.185  5.804  1.00 30.96  ? 78   GLU A C   1 
ATOM   576   O  O   . GLU A  1 78  ? 59.456  53.906  6.780  1.00 30.15  ? 78   GLU A O   1 
ATOM   577   C  CB  . GLU A  1 78  ? 60.340  55.103  4.426  1.00 29.74  ? 78   GLU A CB  1 
ATOM   578   C  CG  . GLU A  1 78  ? 61.791  54.924  4.851  1.00 36.69  ? 78   GLU A CG  1 
ATOM   579   C  CD  . GLU A  1 78  ? 62.642  54.298  3.762  1.00 49.15  ? 78   GLU A CD  1 
ATOM   580   O  OE1 . GLU A  1 78  ? 63.890  54.327  3.853  1.00 44.19  ? 78   GLU A OE1 1 
ATOM   581   O  OE2 . GLU A  1 78  ? 62.037  53.779  2.799  1.00 75.70  ? 78   GLU A OE2 1 
ATOM   582   N  N   . ARG A  1 79  ? 59.842  51.880  5.894  1.00 33.31  ? 79   ARG A N   1 
ATOM   583   C  CA  . ARG A  1 79  ? 59.988  51.239  7.195  1.00 27.30  ? 79   ARG A CA  1 
ATOM   584   C  C   . ARG A  1 79  ? 60.869  49.995  7.047  1.00 31.88  ? 79   ARG A C   1 
ATOM   585   O  O   . ARG A  1 79  ? 60.997  49.467  5.948  1.00 25.96  ? 79   ARG A O   1 
ATOM   586   C  CB  . ARG A  1 79  ? 58.637  50.827  7.791  1.00 24.02  ? 79   ARG A CB  1 
ATOM   587   C  CG  . ARG A  1 79  ? 57.868  49.858  6.909  1.00 27.00  ? 79   ARG A CG  1 
ATOM   588   C  CD  . ARG A  1 79  ? 56.586  49.312  7.519  1.00 28.80  ? 79   ARG A CD  1 
ATOM   589   N  NE  . ARG A  1 79  ? 56.846  47.987  8.133  1.00 25.66  ? 79   ARG A NE  1 
ATOM   590   C  CZ  . ARG A  1 79  ? 55.918  47.176  8.602  1.00 27.20  ? 79   ARG A CZ  1 
ATOM   591   N  NH1 . ARG A  1 79  ? 56.228  45.992  9.130  1.00 23.63  ? 79   ARG A NH1 1 
ATOM   592   N  NH2 . ARG A  1 79  ? 54.645  47.580  8.531  1.00 24.52  ? 79   ARG A NH2 1 
ATOM   593   N  N   . HIS A  1 80  ? 61.441  49.541  8.153  1.00 28.40  ? 80   HIS A N   1 
ATOM   594   C  CA  . HIS A  1 80  ? 61.943  48.175  8.268  1.00 27.78  ? 80   HIS A CA  1 
ATOM   595   C  C   . HIS A  1 80  ? 60.809  47.169  8.180  1.00 24.32  ? 80   HIS A C   1 
ATOM   596   O  O   . HIS A  1 80  ? 59.702  47.406  8.683  1.00 26.34  ? 80   HIS A O   1 
ATOM   597   C  CB  . HIS A  1 80  ? 62.646  48.023  9.626  1.00 22.49  ? 80   HIS A CB  1 
ATOM   598   C  CG  . HIS A  1 80  ? 63.769  48.980  9.835  1.00 25.48  ? 80   HIS A CG  1 
ATOM   599   N  ND1 . HIS A  1 80  ? 64.164  49.436  11.054 1.00 23.10  ? 80   HIS A ND1 1 
ATOM   600   C  CD2 . HIS A  1 80  ? 64.614  49.561  8.953  1.00 25.41  ? 80   HIS A CD2 1 
ATOM   601   C  CE1 . HIS A  1 80  ? 65.192  50.249  10.937 1.00 23.94  ? 80   HIS A CE1 1 
ATOM   602   N  NE2 . HIS A  1 80  ? 65.489  50.348  9.647  1.00 25.28  ? 80   HIS A NE2 1 
ATOM   603   N  N   . VAL A  1 81  ? 60.981  45.984  7.574  1.00 22.01  ? 81   VAL A N   1 
ATOM   604   C  CA  . VAL A  1 81  ? 59.922  44.979  7.648  1.00 21.75  ? 81   VAL A CA  1 
ATOM   605   C  C   . VAL A  1 81  ? 59.557  44.659  9.088  1.00 22.53  ? 81   VAL A C   1 
ATOM   606   O  O   . VAL A  1 81  ? 58.409  44.384  9.368  1.00 22.21  ? 81   VAL A O   1 
ATOM   607   C  CB  . VAL A  1 81  ? 60.413  43.702  6.935  1.00 24.75  ? 81   VAL A CB  1 
ATOM   608   C  CG1 . VAL A  1 81  ? 59.499  42.527  7.192  1.00 20.99  ? 81   VAL A CG1 1 
ATOM   609   C  CG2 . VAL A  1 81  ? 60.582  44.009  5.445  1.00 30.05  ? 81   VAL A CG2 1 
ATOM   610   N  N   . GLY A  1 82  ? 60.553  44.746  9.988  1.00 22.57  ? 82   GLY A N   1 
ATOM   611   C  CA  . GLY A  1 82  ? 60.257  44.389  11.372 1.00 24.15  ? 82   GLY A CA  1 
ATOM   612   C  C   . GLY A  1 82  ? 59.539  45.465  12.172 1.00 32.28  ? 82   GLY A C   1 
ATOM   613   O  O   . GLY A  1 82  ? 59.250  45.239  13.360 1.00 24.28  ? 82   GLY A O   1 
ATOM   614   N  N   . ASP A  1 83  ? 59.216  46.628  11.608 1.00 25.20  ? 83   ASP A N   1 
ATOM   615   C  CA  . ASP A  1 83  ? 58.651  47.710  12.421 1.00 24.88  ? 83   ASP A CA  1 
ATOM   616   C  C   . ASP A  1 83  ? 57.172  47.552  12.714 1.00 27.14  ? 83   ASP A C   1 
ATOM   617   O  O   . ASP A  1 83  ? 56.341  47.815  11.841 1.00 25.40  ? 83   ASP A O   1 
ATOM   618   C  CB  . ASP A  1 83  ? 58.876  49.078  11.745 1.00 23.87  ? 83   ASP A CB  1 
ATOM   619   C  CG  . ASP A  1 83  ? 60.342  49.447  11.748 1.00 24.34  ? 83   ASP A CG  1 
ATOM   620   O  OD1 . ASP A  1 83  ? 61.049  48.873  12.602 1.00 24.64  ? 83   ASP A OD1 1 
ATOM   621   O  OD2 . ASP A  1 83  ? 60.816  50.269  10.935 1.00 25.24  ? 83   ASP A OD2 1 
ATOM   622   N  N   . LEU A  1 84  ? 56.807  47.161  13.930 1.00 22.65  ? 84   LEU A N   1 
ATOM   623   C  CA  . LEU A  1 84  ? 55.395  47.023  14.285 1.00 19.56  ? 84   LEU A CA  1 
ATOM   624   C  C   . LEU A  1 84  ? 54.916  48.128  15.236 1.00 24.49  ? 84   LEU A C   1 
ATOM   625   O  O   . LEU A  1 84  ? 53.863  47.957  15.860 1.00 27.33  ? 84   LEU A O   1 
ATOM   626   C  CB  . LEU A  1 84  ? 55.101  45.646  14.880 1.00 19.19  ? 84   LEU A CB  1 
ATOM   627   C  CG  . LEU A  1 84  ? 55.408  44.468  13.940 1.00 23.71  ? 84   LEU A CG  1 
ATOM   628   C  CD1 . LEU A  1 84  ? 55.183  43.145  14.653 1.00 25.11  ? 84   LEU A CD1 1 
ATOM   629   C  CD2 . LEU A  1 84  ? 54.543  44.585  12.691 1.00 23.78  ? 84   LEU A CD2 1 
ATOM   630   N  N   . GLY A  1 85  ? 55.649  49.225  15.353 1.00 27.49  ? 85   GLY A N   1 
ATOM   631   C  CA  . GLY A  1 85  ? 55.188  50.411  16.050 1.00 28.86  ? 85   GLY A CA  1 
ATOM   632   C  C   . GLY A  1 85  ? 55.213  50.292  17.555 1.00 30.05  ? 85   GLY A C   1 
ATOM   633   O  O   . GLY A  1 85  ? 56.236  49.874  18.106 1.00 28.99  ? 85   GLY A O   1 
ATOM   634   N  N   . ASN A  1 86  ? 54.112  50.637  18.212 1.00 24.50  ? 86   ASN A N   1 
ATOM   635   C  CA  . ASN A  1 86  ? 54.049  50.591  19.662 1.00 24.48  ? 86   ASN A CA  1 
ATOM   636   C  C   . ASN A  1 86  ? 52.927  49.712  20.177 1.00 28.24  ? 86   ASN A C   1 
ATOM   637   O  O   . ASN A  1 86  ? 51.859  49.631  19.579 1.00 28.84  ? 86   ASN A O   1 
ATOM   638   C  CB  . ASN A  1 86  ? 53.804  52.006  20.233 1.00 26.69  ? 86   ASN A CB  1 
ATOM   639   C  CG  . ASN A  1 86  ? 55.045  52.854  20.132 1.00 26.20  ? 86   ASN A CG  1 
ATOM   640   O  OD1 . ASN A  1 86  ? 56.067  52.551  20.762 1.00 26.17  ? 86   ASN A OD1 1 
ATOM   641   N  ND2 . ASN A  1 86  ? 54.978  53.918  19.341 1.00 25.04  ? 86   ASN A ND2 1 
ATOM   642   N  N   . VAL A  1 87  ? 53.148  49.092  21.338 1.00 25.45  ? 87   VAL A N   1 
ATOM   643   C  CA  . VAL A  1 87  ? 52.049  48.484  22.072 1.00 20.85  ? 87   VAL A CA  1 
ATOM   644   C  C   . VAL A  1 87  ? 51.743  49.420  23.255 1.00 24.01  ? 87   VAL A C   1 
ATOM   645   O  O   . VAL A  1 87  ? 52.654  50.174  23.584 1.00 25.06  ? 87   VAL A O   1 
ATOM   646   C  CB  . VAL A  1 87  ? 52.325  47.062  22.579 1.00 28.27  ? 87   VAL A CB  1 
ATOM   647   C  CG1 . VAL A  1 87  ? 52.535  46.126  21.392 1.00 23.44  ? 87   VAL A CG1 1 
ATOM   648   C  CG2 . VAL A  1 87  ? 53.516  47.032  23.527 1.00 22.80  ? 87   VAL A CG2 1 
ATOM   649   N  N   . THR A  1 88  ? 50.548  49.346  23.804 1.00 23.42  ? 88   THR A N   1 
ATOM   650   C  CA  . THR A  1 88  ? 50.176  50.263  24.880 1.00 28.12  ? 88   THR A CA  1 
ATOM   651   C  C   . THR A  1 88  ? 49.817  49.496  26.147 1.00 20.63  ? 88   THR A C   1 
ATOM   652   O  O   . THR A  1 88  ? 48.928  48.655  26.196 1.00 26.23  ? 88   THR A O   1 
ATOM   653   C  CB  . THR A  1 88  ? 48.980  51.170  24.517 1.00 36.90  ? 88   THR A CB  1 
ATOM   654   O  OG1 . THR A  1 88  ? 49.279  51.955  23.358 1.00 35.89  ? 88   THR A OG1 1 
ATOM   655   C  CG2 . THR A  1 88  ? 48.755  52.189  25.638 1.00 34.92  ? 88   THR A CG2 1 
ATOM   656   N  N   . ALA A  1 89  ? 50.576  49.782  27.218 1.00 24.80  ? 89   ALA A N   1 
ATOM   657   C  CA  . ALA A  1 89  ? 50.311  49.164  28.504 1.00 22.56  ? 89   ALA A CA  1 
ATOM   658   C  C   . ALA A  1 89  ? 49.364  50.052  29.341 1.00 22.54  ? 89   ALA A C   1 
ATOM   659   O  O   . ALA A  1 89  ? 49.580  51.269  29.359 1.00 28.20  ? 89   ALA A O   1 
ATOM   660   C  CB  . ALA A  1 89  ? 51.617  48.971  29.279 1.00 22.70  ? 89   ALA A CB  1 
ATOM   661   N  N   . ASP A  1 90  ? 48.405  49.433  29.984 1.00 24.12  ? 90   ASP A N   1 
ATOM   662   C  CA  . ASP A  1 90  ? 47.433  50.143  30.824 1.00 31.59  ? 90   ASP A CA  1 
ATOM   663   C  C   . ASP A  1 90  ? 48.021  50.424  32.198 1.00 41.71  ? 90   ASP A C   1 
ATOM   664   O  O   . ASP A  1 90  ? 49.201  50.199  32.471 1.00 26.31  ? 90   ASP A O   1 
ATOM   665   C  CB  . ASP A  1 90  ? 46.140  49.343  30.921 1.00 33.08  ? 90   ASP A CB  1 
ATOM   666   C  CG  . ASP A  1 90  ? 46.227  48.011  31.629 1.00 36.67  ? 90   ASP A CG  1 
ATOM   667   O  OD1 . ASP A  1 90  ? 45.281  47.205  31.433 1.00 34.06  ? 90   ASP A OD1 1 
ATOM   668   O  OD2 . ASP A  1 90  ? 47.189  47.739  32.391 1.00 30.89  ? 90   ASP A OD2 1 
ATOM   669   N  N   . LYS A  1 91  ? 47.196  50.954  33.116 1.00 32.93  ? 91   LYS A N   1 
ATOM   670   C  CA  . LYS A  1 91  ? 47.805  51.330  34.391 1.00 25.95  ? 91   LYS A CA  1 
ATOM   671   C  C   . LYS A  1 91  ? 48.149  50.126  35.239 1.00 22.55  ? 91   LYS A C   1 
ATOM   672   O  O   . LYS A  1 91  ? 48.843  50.295  36.243 1.00 31.64  ? 91   LYS A O   1 
ATOM   673   C  CB  . LYS A  1 91  ? 46.827  52.244  35.166 1.00 33.79  ? 91   LYS A CB  1 
ATOM   674   C  CG  . LYS A  1 91  ? 45.574  51.443  35.534 1.00 39.05  ? 91   LYS A CG  1 
ATOM   675   C  CD  . LYS A  1 91  ? 44.589  52.340  36.286 1.00 57.80  ? 91   LYS A CD  1 
ATOM   676   C  CE  . LYS A  1 91  ? 43.405  51.536  36.805 1.00 66.06  ? 91   LYS A CE  1 
ATOM   677   N  NZ  . LYS A  1 91  ? 43.516  51.254  38.266 1.00 102.54 ? 91   LYS A NZ  1 
ATOM   678   N  N   . ASP A  1 92  ? 47.675  48.936  34.885 1.00 27.38  ? 92   ASP A N   1 
ATOM   679   C  CA  . ASP A  1 92  ? 48.028  47.687  35.512 1.00 27.70  ? 92   ASP A CA  1 
ATOM   680   C  C   . ASP A  1 92  ? 49.264  47.030  34.880 1.00 25.07  ? 92   ASP A C   1 
ATOM   681   O  O   . ASP A  1 92  ? 49.593  45.923  35.287 1.00 26.13  ? 92   ASP A O   1 
ATOM   682   C  CB  . ASP A  1 92  ? 46.880  46.677  35.456 1.00 29.33  ? 92   ASP A CB  1 
ATOM   683   C  CG  . ASP A  1 92  ? 45.721  47.213  36.294 1.00 49.42  ? 92   ASP A CG  1 
ATOM   684   O  OD1 . ASP A  1 92  ? 44.567  47.130  35.839 1.00 57.47  ? 92   ASP A OD1 1 
ATOM   685   O  OD2 . ASP A  1 92  ? 46.011  47.718  37.401 1.00 48.16  ? 92   ASP A OD2 1 
ATOM   686   N  N   . GLY A  1 93  ? 49.898  47.691  33.942 1.00 27.72  ? 93   GLY A N   1 
ATOM   687   C  CA  . GLY A  1 93  ? 51.110  47.236  33.282 1.00 26.63  ? 93   GLY A CA  1 
ATOM   688   C  C   . GLY A  1 93  ? 50.874  46.198  32.212 1.00 30.07  ? 93   GLY A C   1 
ATOM   689   O  O   . GLY A  1 93  ? 51.811  45.488  31.821 1.00 29.86  ? 93   GLY A O   1 
ATOM   690   N  N   . VAL A  1 94  ? 49.637  46.089  31.743 1.00 25.83  ? 94   VAL A N   1 
ATOM   691   C  CA  . VAL A  1 94  ? 49.259  45.041  30.806 1.00 29.35  ? 94   VAL A CA  1 
ATOM   692   C  C   . VAL A  1 94  ? 48.925  45.637  29.443 1.00 32.49  ? 94   VAL A C   1 
ATOM   693   O  O   . VAL A  1 94  ? 48.096  46.541  29.356 1.00 27.29  ? 94   VAL A O   1 
ATOM   694   C  CB  . VAL A  1 94  ? 48.051  44.203  31.234 1.00 30.05  ? 94   VAL A CB  1 
ATOM   695   C  CG1 . VAL A  1 94  ? 47.770  43.160  30.155 1.00 32.18  ? 94   VAL A CG1 1 
ATOM   696   C  CG2 . VAL A  1 94  ? 48.269  43.524  32.578 1.00 29.08  ? 94   VAL A CG2 1 
ATOM   697   N  N   . ALA A  1 95  ? 49.591  45.113  28.429 1.00 26.27  ? 95   ALA A N   1 
ATOM   698   C  CA  . ALA A  1 95  ? 49.354  45.544  27.062 1.00 25.26  ? 95   ALA A CA  1 
ATOM   699   C  C   . ALA A  1 95  ? 48.581  44.448  26.358 1.00 32.93  ? 95   ALA A C   1 
ATOM   700   O  O   . ALA A  1 95  ? 49.026  43.306  26.259 1.00 32.42  ? 95   ALA A O   1 
ATOM   701   C  CB  . ALA A  1 95  ? 50.646  45.840  26.304 1.00 26.62  ? 95   ALA A CB  1 
ATOM   702   N  N   . ASP A  1 96  ? 47.408  44.818  25.863 1.00 24.00  ? 96   ASP A N   1 
ATOM   703   C  CA  . ASP A  1 96  ? 46.674  43.825  25.075 1.00 27.89  ? 96   ASP A CA  1 
ATOM   704   C  C   . ASP A  1 96  ? 46.892  44.194  23.617 1.00 30.44  ? 96   ASP A C   1 
ATOM   705   O  O   . ASP A  1 96  ? 46.546  45.280  23.166 1.00 33.37  ? 96   ASP A O   1 
ATOM   706   C  CB  . ASP A  1 96  ? 45.205  43.769  25.477 1.00 46.64  ? 96   ASP A CB  1 
ATOM   707   C  CG  . ASP A  1 96  ? 45.072  43.230  26.897 1.00 60.41  ? 96   ASP A CG  1 
ATOM   708   O  OD1 . ASP A  1 96  ? 45.460  42.063  27.161 1.00 42.94  ? 96   ASP A OD1 1 
ATOM   709   O  OD2 . ASP A  1 96  ? 44.591  44.003  27.758 1.00 59.97  ? 96   ASP A OD2 1 
ATOM   710   N  N   . VAL A  1 97  ? 47.534  43.260  22.923 1.00 29.66  ? 97   VAL A N   1 
ATOM   711   C  CA  . VAL A  1 97  ? 48.007  43.535  21.573 1.00 26.84  ? 97   VAL A CA  1 
ATOM   712   C  C   . VAL A  1 97  ? 47.022  43.014  20.541 1.00 20.80  ? 97   VAL A C   1 
ATOM   713   O  O   . VAL A  1 97  ? 46.522  41.899  20.663 1.00 24.45  ? 97   VAL A O   1 
ATOM   714   C  CB  . VAL A  1 97  ? 49.386  42.876  21.371 1.00 32.81  ? 97   VAL A CB  1 
ATOM   715   C  CG1 . VAL A  1 97  ? 49.930  43.163  19.978 1.00 26.71  ? 97   VAL A CG1 1 
ATOM   716   C  CG2 . VAL A  1 97  ? 50.319  43.372  22.471 1.00 23.84  ? 97   VAL A CG2 1 
ATOM   717   N  N   . SER A  1 98  ? 46.757  43.842  19.545 1.00 26.07  ? 98   SER A N   1 
ATOM   718   C  CA  . SER A  1 98  ? 45.891  43.426  18.431 1.00 27.87  ? 98   SER A CA  1 
ATOM   719   C  C   . SER A  1 98  ? 46.298  44.332  17.262 1.00 35.19  ? 98   SER A C   1 
ATOM   720   O  O   . SER A  1 98  ? 46.027  45.534  17.278 1.00 36.47  ? 98   SER A O   1 
ATOM   721   C  CB  . SER A  1 98  ? 44.403  43.509  18.734 1.00 35.84  ? 98   SER A CB  1 
ATOM   722   O  OG  . SER A  1 98  ? 43.692  43.677  17.516 1.00 41.50  ? 98   SER A OG  1 
ATOM   723   N  N   . ILE A  1 99  ? 46.999  43.730  16.318 1.00 26.53  ? 99   ILE A N   1 
ATOM   724   C  CA  . ILE A  1 99  ? 47.666  44.426  15.213 1.00 29.33  ? 99   ILE A CA  1 
ATOM   725   C  C   . ILE A  1 99  ? 47.309  43.655  13.954 1.00 27.52  ? 99   ILE A C   1 
ATOM   726   O  O   . ILE A  1 99  ? 47.067  42.447  14.044 1.00 30.41  ? 99   ILE A O   1 
ATOM   727   C  CB  . ILE A  1 99  ? 49.183  44.471  15.451 1.00 31.42  ? 99   ILE A CB  1 
ATOM   728   C  CG1 . ILE A  1 99  ? 49.589  45.425  16.592 1.00 49.59  ? 99   ILE A CG1 1 
ATOM   729   C  CG2 . ILE A  1 99  ? 49.994  44.794  14.214 1.00 32.61  ? 99   ILE A CG2 1 
ATOM   730   C  CD1 . ILE A  1 99  ? 51.082  45.434  16.897 1.00 33.83  ? 99   ILE A CD1 1 
ATOM   731   N  N   . GLU A  1 100 ? 47.204  44.312  12.810 1.00 29.15  ? 100  GLU A N   1 
ATOM   732   C  CA  . GLU A  1 100 ? 47.129  43.567  11.552 1.00 30.86  ? 100  GLU A CA  1 
ATOM   733   C  C   . GLU A  1 100 ? 48.201  44.233  10.703 1.00 23.48  ? 100  GLU A C   1 
ATOM   734   O  O   . GLU A  1 100 ? 48.243  45.461  10.710 1.00 26.41  ? 100  GLU A O   1 
ATOM   735   C  CB  . GLU A  1 100 ? 45.774  43.578  10.853 1.00 46.42  ? 100  GLU A CB  1 
ATOM   736   C  CG  . GLU A  1 100 ? 45.815  42.960  9.454  1.00 46.51  ? 100  GLU A CG  1 
ATOM   737   C  CD  . GLU A  1 100 ? 44.464  42.934  8.760  1.00 56.72  ? 100  GLU A CD  1 
ATOM   738   O  OE1 . GLU A  1 100 ? 43.476  42.516  9.408  1.00 52.39  ? 100  GLU A OE1 1 
ATOM   739   O  OE2 . GLU A  1 100 ? 44.385  43.331  7.569  1.00 43.60  ? 100  GLU A OE2 1 
ATOM   740   N  N   . ASP A  1 101 ? 49.036  43.441  10.045 1.00 23.36  ? 101  ASP A N   1 
ATOM   741   C  CA  . ASP A  1 101 ? 50.118  44.069  9.311  1.00 23.78  ? 101  ASP A CA  1 
ATOM   742   C  C   . ASP A  1 101 ? 50.229  43.409  7.937  1.00 23.62  ? 101  ASP A C   1 
ATOM   743   O  O   . ASP A  1 101 ? 50.080  42.202  7.833  1.00 27.33  ? 101  ASP A O   1 
ATOM   744   C  CB  . ASP A  1 101 ? 51.446  43.969  10.071 1.00 25.49  ? 101  ASP A CB  1 
ATOM   745   C  CG  . ASP A  1 101 ? 52.531  44.828  9.477  1.00 30.19  ? 101  ASP A CG  1 
ATOM   746   O  OD1 . ASP A  1 101 ? 53.502  44.317  8.865  1.00 25.30  ? 101  ASP A OD1 1 
ATOM   747   O  OD2 . ASP A  1 101 ? 52.454  46.071  9.600  1.00 32.25  ? 101  ASP A OD2 1 
ATOM   748   N  N   . SER A  1 102 ? 50.508  44.232  6.934  1.00 24.25  ? 102  SER A N   1 
ATOM   749   C  CA  . SER A  1 102 ? 50.575  43.618  5.604  1.00 28.88  ? 102  SER A CA  1 
ATOM   750   C  C   . SER A  1 102 ? 51.965  43.642  5.018  1.00 34.71  ? 102  SER A C   1 
ATOM   751   O  O   . SER A  1 102 ? 52.193  43.373  3.833  1.00 32.25  ? 102  SER A O   1 
ATOM   752   C  CB  . SER A  1 102 ? 49.591  44.421  4.726  1.00 28.81  ? 102  SER A CB  1 
ATOM   753   O  OG  . SER A  1 102 ? 50.202  45.704  4.582  1.00 40.09  ? 102  SER A OG  1 
ATOM   754   N  N   . VAL A  1 103 ? 52.975  43.970  5.822  1.00 24.99  ? 103  VAL A N   1 
ATOM   755   C  CA  . VAL A  1 103 ? 54.355  43.984  5.351  1.00 23.88  ? 103  VAL A CA  1 
ATOM   756   C  C   . VAL A  1 103 ? 55.063  42.736  5.888  1.00 31.04  ? 103  VAL A C   1 
ATOM   757   O  O   . VAL A  1 103 ? 55.747  42.046  5.124  1.00 27.31  ? 103  VAL A O   1 
ATOM   758   C  CB  . VAL A  1 103 ? 55.069  45.279  5.756  1.00 28.11  ? 103  VAL A CB  1 
ATOM   759   C  CG1 . VAL A  1 103 ? 56.571  45.202  5.580  1.00 27.58  ? 103  VAL A CG1 1 
ATOM   760   C  CG2 . VAL A  1 103 ? 54.519  46.450  4.927  1.00 25.82  ? 103  VAL A CG2 1 
ATOM   761   N  N   . ILE A  1 104 ? 54.902  42.383  7.165  1.00 22.25  ? 104  ILE A N   1 
ATOM   762   C  CA  . ILE A  1 104 ? 55.522  41.123  7.614  1.00 25.71  ? 104  ILE A CA  1 
ATOM   763   C  C   . ILE A  1 104 ? 54.819  39.926  7.010  1.00 29.84  ? 104  ILE A C   1 
ATOM   764   O  O   . ILE A  1 104 ? 53.653  40.006  6.576  1.00 27.07  ? 104  ILE A O   1 
ATOM   765   C  CB  . ILE A  1 104 ? 55.456  40.969  9.155  1.00 24.25  ? 104  ILE A CB  1 
ATOM   766   C  CG1 . ILE A  1 104 ? 54.023  40.981  9.677  1.00 26.37  ? 104  ILE A CG1 1 
ATOM   767   C  CG2 . ILE A  1 104 ? 56.329  42.022  9.823  1.00 22.75  ? 104  ILE A CG2 1 
ATOM   768   C  CD1 . ILE A  1 104 ? 53.756  40.493  11.091 1.00 22.15  ? 104  ILE A CD1 1 
ATOM   769   N  N   . SER A  1 105 ? 55.490  38.766  6.996  1.00 21.28  ? 105  SER A N   1 
ATOM   770   C  CA  . SER A  1 105 ? 54.831  37.574  6.484  1.00 20.40  ? 105  SER A CA  1 
ATOM   771   C  C   . SER A  1 105 ? 55.277  36.319  7.253  1.00 24.86  ? 105  SER A C   1 
ATOM   772   O  O   . SER A  1 105 ? 56.358  36.373  7.852  1.00 26.82  ? 105  SER A O   1 
ATOM   773   C  CB  . SER A  1 105 ? 55.141  37.375  4.978  1.00 20.94  ? 105  SER A CB  1 
ATOM   774   O  OG  . SER A  1 105 ? 54.278  36.329  4.497  1.00 23.68  ? 105  SER A OG  1 
ATOM   775   N  N   . LEU A  1 106 ? 54.514  35.254  7.268  1.00 21.02  ? 106  LEU A N   1 
ATOM   776   C  CA  . LEU A  1 106 ? 54.832  33.987  7.935  1.00 19.63  ? 106  LEU A CA  1 
ATOM   777   C  C   . LEU A  1 106 ? 55.412  32.994  6.927  1.00 25.98  ? 106  LEU A C   1 
ATOM   778   O  O   . LEU A  1 106 ? 55.692  31.855  7.279  1.00 25.48  ? 106  LEU A O   1 
ATOM   779   C  CB  . LEU A  1 106 ? 53.611  33.385  8.626  1.00 25.36  ? 106  LEU A CB  1 
ATOM   780   C  CG  . LEU A  1 106 ? 52.979  34.249  9.732  1.00 24.92  ? 106  LEU A CG  1 
ATOM   781   C  CD1 . LEU A  1 106 ? 51.916  33.464  10.470 1.00 21.11  ? 106  LEU A CD1 1 
ATOM   782   C  CD2 . LEU A  1 106 ? 54.047  34.785  10.679 1.00 23.15  ? 106  LEU A CD2 1 
ATOM   783   N  N   . SER A  1 107 ? 55.570  33.467  5.689  1.00 25.28  ? 107  SER A N   1 
ATOM   784   C  CA  . SER A  1 107 ? 56.221  32.613  4.697  1.00 25.35  ? 107  SER A CA  1 
ATOM   785   C  C   . SER A  1 107 ? 56.914  33.479  3.654  1.00 28.41  ? 107  SER A C   1 
ATOM   786   O  O   . SER A  1 107 ? 56.831  34.709  3.609  1.00 26.44  ? 107  SER A O   1 
ATOM   787   C  CB  . SER A  1 107 ? 55.245  31.664  4.017  1.00 31.47  ? 107  SER A CB  1 
ATOM   788   O  OG  . SER A  1 107 ? 54.190  32.356  3.342  1.00 31.86  ? 107  SER A OG  1 
ATOM   789   N  N   . GLY A  1 108 ? 57.628  32.758  2.790  1.00 27.82  ? 108  GLY A N   1 
ATOM   790   C  CA  . GLY A  1 108 ? 58.311  33.413  1.703  1.00 31.06  ? 108  GLY A CA  1 
ATOM   791   C  C   . GLY A  1 108 ? 59.703  33.815  2.114  1.00 44.64  ? 108  GLY A C   1 
ATOM   792   O  O   . GLY A  1 108 ? 60.018  33.814  3.306  1.00 43.76  ? 108  GLY A O   1 
ATOM   793   N  N   . ASP A  1 109 ? 60.522  34.183  1.136  1.00 50.96  ? 109  ASP A N   1 
ATOM   794   C  CA  . ASP A  1 109 ? 61.961  34.394  1.328  1.00 38.68  ? 109  ASP A CA  1 
ATOM   795   C  C   . ASP A  1 109 ? 62.212  35.434  2.417  1.00 50.75  ? 109  ASP A C   1 
ATOM   796   O  O   . ASP A  1 109 ? 63.297  35.441  3.021  1.00 44.85  ? 109  ASP A O   1 
ATOM   797   C  CB  . ASP A  1 109 ? 62.605  34.708  -0.017 1.00 41.06  ? 109  ASP A CB  1 
ATOM   798   C  CG  . ASP A  1 109 ? 63.117  36.112  -0.212 1.00 65.80  ? 109  ASP A CG  1 
ATOM   799   O  OD1 . ASP A  1 109 ? 62.306  37.068  -0.207 1.00 77.26  ? 109  ASP A OD1 1 
ATOM   800   O  OD2 . ASP A  1 109 ? 64.350  36.279  -0.387 1.00 77.71  ? 109  ASP A OD2 1 
ATOM   801   N  N   . HIS A  1 110 ? 61.240  36.293  2.731  1.00 48.70  ? 110  HIS A N   1 
ATOM   802   C  CA  . HIS A  1 110 ? 61.397  37.261  3.813  1.00 42.16  ? 110  HIS A CA  1 
ATOM   803   C  C   . HIS A  1 110 ? 60.443  37.085  4.988  1.00 42.23  ? 110  HIS A C   1 
ATOM   804   O  O   . HIS A  1 110 ? 60.025  38.071  5.599  1.00 45.23  ? 110  HIS A O   1 
ATOM   805   C  CB  . HIS A  1 110 ? 61.205  38.665  3.218  1.00 46.90  ? 110  HIS A CB  1 
ATOM   806   C  CG  . HIS A  1 110 ? 62.290  39.022  2.241  1.00 59.88  ? 110  HIS A CG  1 
ATOM   807   N  ND1 . HIS A  1 110 ? 62.115  39.941  1.229  1.00 62.55  ? 110  HIS A ND1 1 
ATOM   808   C  CD2 . HIS A  1 110 ? 63.567  38.591  2.119  1.00 60.59  ? 110  HIS A CD2 1 
ATOM   809   C  CE1 . HIS A  1 110 ? 63.230  40.057  0.528  1.00 59.99  ? 110  HIS A CE1 1 
ATOM   810   N  NE2 . HIS A  1 110 ? 64.132  39.249  1.048  1.00 57.76  ? 110  HIS A NE2 1 
ATOM   811   N  N   . CYS A  1 111 ? 60.048  35.898  5.394  1.00 34.74  ? 111  CYS A N   1 
ATOM   812   C  CA  . CYS A  1 111 ? 59.149  35.737  6.543  1.00 23.95  ? 111  CYS A CA  1 
ATOM   813   C  C   . CYS A  1 111 ? 59.820  35.953  7.888  1.00 24.35  ? 111  CYS A C   1 
ATOM   814   O  O   . CYS A  1 111 ? 61.055  35.991  7.969  1.00 29.65  ? 111  CYS A O   1 
ATOM   815   C  CB  . CYS A  1 111 ? 58.510  34.359  6.405  1.00 34.43  ? 111  CYS A CB  1 
ATOM   816   S  SG  . CYS A  1 111 ? 59.276  33.018  7.283  1.00 52.31  ? 111  CYS A SG  1 
ATOM   817   N  N   . ILE A  1 112 ? 59.072  36.126  8.970  1.00 21.83  ? 112  ILE A N   1 
ATOM   818   C  CA  . ILE A  1 112 ? 59.630  36.463  10.281 1.00 23.32  ? 112  ILE A CA  1 
ATOM   819   C  C   . ILE A  1 112 ? 59.779  35.259  11.199 1.00 23.34  ? 112  ILE A C   1 
ATOM   820   O  O   . ILE A  1 112 ? 60.207  35.362  12.355 1.00 22.70  ? 112  ILE A O   1 
ATOM   821   C  CB  . ILE A  1 112 ? 58.737  37.506  11.011 1.00 19.72  ? 112  ILE A CB  1 
ATOM   822   C  CG1 . ILE A  1 112 ? 57.303  37.018  11.243 1.00 22.70  ? 112  ILE A CG1 1 
ATOM   823   C  CG2 . ILE A  1 112 ? 58.770  38.846  10.289 1.00 21.18  ? 112  ILE A CG2 1 
ATOM   824   C  CD1 . ILE A  1 112 ? 56.476  38.032  12.045 1.00 28.43  ? 112  ILE A CD1 1 
ATOM   825   N  N   . ILE A  1 113 ? 59.427  34.071  10.709 1.00 20.10  ? 113  ILE A N   1 
ATOM   826   C  CA  . ILE A  1 113 ? 59.569  32.880  11.560 1.00 21.16  ? 113  ILE A CA  1 
ATOM   827   C  C   . ILE A  1 113 ? 61.048  32.616  11.823 1.00 24.62  ? 113  ILE A C   1 
ATOM   828   O  O   . ILE A  1 113 ? 61.913  32.749  10.950 1.00 20.30  ? 113  ILE A O   1 
ATOM   829   C  CB  . ILE A  1 113 ? 58.806  31.706  10.933 1.00 23.24  ? 113  ILE A CB  1 
ATOM   830   C  CG1 . ILE A  1 113 ? 57.287  31.855  11.182 1.00 25.75  ? 113  ILE A CG1 1 
ATOM   831   C  CG2 . ILE A  1 113 ? 59.338  30.371  11.434 1.00 23.12  ? 113  ILE A CG2 1 
ATOM   832   C  CD1 . ILE A  1 113 ? 56.413  30.946  10.372 1.00 40.67  ? 113  ILE A CD1 1 
ATOM   833   N  N   . GLY A  1 114 ? 61.406  32.279  13.075 1.00 22.03  ? 114  GLY A N   1 
ATOM   834   C  CA  . GLY A  1 114 ? 62.837  32.109  13.371 1.00 19.29  ? 114  GLY A CA  1 
ATOM   835   C  C   . GLY A  1 114 ? 63.557  33.394  13.710 1.00 21.88  ? 114  GLY A C   1 
ATOM   836   O  O   . GLY A  1 114 ? 64.772  33.359  13.977 1.00 21.18  ? 114  GLY A O   1 
ATOM   837   N  N   . ARG A  1 115 ? 62.848  34.517  13.725 1.00 19.81  ? 115  ARG A N   1 
ATOM   838   C  CA  . ARG A  1 115 ? 63.438  35.811  14.074 1.00 19.75  ? 115  ARG A CA  1 
ATOM   839   C  C   . ARG A  1 115 ? 62.985  36.177  15.473 1.00 18.12  ? 115  ARG A C   1 
ATOM   840   O  O   . ARG A  1 115 ? 62.285  35.359  16.069 1.00 21.54  ? 115  ARG A O   1 
ATOM   841   C  CB  . ARG A  1 115 ? 63.074  36.878  13.026 1.00 19.03  ? 115  ARG A CB  1 
ATOM   842   C  CG  . ARG A  1 115 ? 63.638  36.394  11.684 1.00 19.07  ? 115  ARG A CG  1 
ATOM   843   C  CD  . ARG A  1 115 ? 63.613  37.419  10.583 1.00 24.56  ? 115  ARG A CD  1 
ATOM   844   N  NE  . ARG A  1 115 ? 63.975  36.894  9.266  1.00 22.37  ? 115  ARG A NE  1 
ATOM   845   C  CZ  . ARG A  1 115 ? 65.194  36.756  8.769  1.00 32.72  ? 115  ARG A CZ  1 
ATOM   846   N  NH1 . ARG A  1 115 ? 65.348  36.259  7.530  1.00 28.76  ? 115  ARG A NH1 1 
ATOM   847   N  NH2 . ARG A  1 115 ? 66.283  37.104  9.454  1.00 22.75  ? 115  ARG A NH2 1 
ATOM   848   N  N   . THR A  1 116 ? 63.392  37.329  15.980 1.00 19.43  ? 116  THR A N   1 
ATOM   849   C  CA  . THR A  1 116 ? 63.087  37.637  17.387 1.00 21.08  ? 116  THR A CA  1 
ATOM   850   C  C   . THR A  1 116 ? 62.119  38.811  17.517 1.00 21.54  ? 116  THR A C   1 
ATOM   851   O  O   . THR A  1 116 ? 62.389  39.897  16.982 1.00 22.46  ? 116  THR A O   1 
ATOM   852   C  CB  . THR A  1 116 ? 64.381  37.998  18.140 1.00 22.22  ? 116  THR A CB  1 
ATOM   853   O  OG1 . THR A  1 116 ? 65.217  36.829  18.283 1.00 23.91  ? 116  THR A OG1 1 
ATOM   854   C  CG2 . THR A  1 116 ? 64.077  38.446  19.565 1.00 21.05  ? 116  THR A CG2 1 
ATOM   855   N  N   . LEU A  1 117 ? 61.058  38.616  18.284 1.00 19.79  ? 117  LEU A N   1 
ATOM   856   C  CA  . LEU A  1 117 ? 60.120  39.709  18.568 1.00 17.54  ? 117  LEU A CA  1 
ATOM   857   C  C   . LEU A  1 117 ? 60.606  40.386  19.847 1.00 20.34  ? 117  LEU A C   1 
ATOM   858   O  O   . LEU A  1 117 ? 60.837  39.611  20.784 1.00 21.72  ? 117  LEU A O   1 
ATOM   859   C  CB  . LEU A  1 117 ? 58.714  39.171  18.745 1.00 21.74  ? 117  LEU A CB  1 
ATOM   860   C  CG  . LEU A  1 117 ? 57.537  40.123  18.992 1.00 21.40  ? 117  LEU A CG  1 
ATOM   861   C  CD1 . LEU A  1 117 ? 57.335  41.046  17.784 1.00 22.17  ? 117  LEU A CD1 1 
ATOM   862   C  CD2 . LEU A  1 117 ? 56.254  39.357  19.294 1.00 19.17  ? 117  LEU A CD2 1 
ATOM   863   N  N   . VAL A  1 118 ? 60.712  41.702  19.880 1.00 19.22  ? 118  VAL A N   1 
ATOM   864   C  CA  . VAL A  1 118 ? 61.257  42.454  21.018 1.00 21.00  ? 118  VAL A CA  1 
ATOM   865   C  C   . VAL A  1 118 ? 60.278  43.534  21.501 1.00 23.01  ? 118  VAL A C   1 
ATOM   866   O  O   . VAL A  1 118 ? 59.678  44.189  20.651 1.00 21.29  ? 118  VAL A O   1 
ATOM   867   C  CB  . VAL A  1 118 ? 62.592  43.126  20.673 1.00 22.81  ? 118  VAL A CB  1 
ATOM   868   C  CG1 . VAL A  1 118 ? 63.113  43.865  21.909 1.00 22.43  ? 118  VAL A CG1 1 
ATOM   869   C  CG2 . VAL A  1 118 ? 63.626  42.120  20.167 1.00 20.69  ? 118  VAL A CG2 1 
ATOM   870   N  N   . VAL A  1 119 ? 60.086  43.693  22.806 1.00 21.15  ? 119  VAL A N   1 
ATOM   871   C  CA  . VAL A  1 119 ? 59.283  44.807  23.366 1.00 22.80  ? 119  VAL A CA  1 
ATOM   872   C  C   . VAL A  1 119 ? 60.243  45.645  24.195 1.00 26.91  ? 119  VAL A C   1 
ATOM   873   O  O   . VAL A  1 119 ? 61.095  45.110  24.928 1.00 23.78  ? 119  VAL A O   1 
ATOM   874   C  CB  . VAL A  1 119 ? 58.048  44.373  24.161 1.00 22.14  ? 119  VAL A CB  1 
ATOM   875   C  CG1 . VAL A  1 119 ? 58.408  43.586  25.412 1.00 25.26  ? 119  VAL A CG1 1 
ATOM   876   C  CG2 . VAL A  1 119 ? 57.186  45.584  24.565 1.00 22.05  ? 119  VAL A CG2 1 
ATOM   877   N  N   . HIS A  1 120 ? 60.120  46.963  24.026 1.00 24.32  ? 120  HIS A N   1 
ATOM   878   C  CA  . HIS A  1 120 ? 61.162  47.868  24.476 1.00 20.81  ? 120  HIS A CA  1 
ATOM   879   C  C   . HIS A  1 120 ? 60.781  48.713  25.699 1.00 26.63  ? 120  HIS A C   1 
ATOM   880   O  O   . HIS A  1 120 ? 59.616  48.795  26.083 1.00 25.47  ? 120  HIS A O   1 
ATOM   881   C  CB  . HIS A  1 120 ? 61.517  48.835  23.345 1.00 23.84  ? 120  HIS A CB  1 
ATOM   882   C  CG  . HIS A  1 120 ? 62.417  48.264  22.290 1.00 27.81  ? 120  HIS A CG  1 
ATOM   883   N  ND1 . HIS A  1 120 ? 63.780  48.463  22.291 1.00 23.17  ? 120  HIS A ND1 1 
ATOM   884   C  CD2 . HIS A  1 120 ? 62.142  47.514  21.192 1.00 29.66  ? 120  HIS A CD2 1 
ATOM   885   C  CE1 . HIS A  1 120 ? 64.307  47.844  21.239 1.00 24.72  ? 120  HIS A CE1 1 
ATOM   886   N  NE2 . HIS A  1 120 ? 63.342  47.258  20.554 1.00 20.34  ? 120  HIS A NE2 1 
ATOM   887   N  N   . GLU A  1 121 ? 61.821  49.331  26.250 1.00 29.07  ? 121  GLU A N   1 
ATOM   888   C  CA  . GLU A  1 121 ? 61.759  50.208  27.399 1.00 33.87  ? 121  GLU A CA  1 
ATOM   889   C  C   . GLU A  1 121 ? 60.804  51.393  27.229 1.00 30.41  ? 121  GLU A C   1 
ATOM   890   O  O   . GLU A  1 121 ? 59.992  51.678  28.094 1.00 29.20  ? 121  GLU A O   1 
ATOM   891   C  CB  . GLU A  1 121 ? 63.165  50.774  27.631 1.00 29.72  ? 121  GLU A CB  1 
ATOM   892   C  CG  . GLU A  1 121 ? 63.280  51.687  28.845 1.00 37.53  ? 121  GLU A CG  1 
ATOM   893   C  CD  . GLU A  1 121 ? 64.636  52.373  28.890 1.00 44.67  ? 121  GLU A CD  1 
ATOM   894   O  OE1 . GLU A  1 121 ? 65.002  52.868  29.979 1.00 55.42  ? 121  GLU A OE1 1 
ATOM   895   O  OE2 . GLU A  1 121 ? 65.350  52.416  27.855 1.00 36.90  ? 121  GLU A OE2 1 
ATOM   896   N  N   . LYS A  1 122 ? 60.956  52.089  26.118 1.00 27.41  ? 122  LYS A N   1 
ATOM   897   C  CA  . LYS A  1 122 ? 60.342  53.369  25.817 1.00 28.03  ? 122  LYS A CA  1 
ATOM   898   C  C   . LYS A  1 122 ? 59.512  53.309  24.542 1.00 32.32  ? 122  LYS A C   1 
ATOM   899   O  O   . LYS A  1 122 ? 59.526  52.315  23.810 1.00 29.04  ? 122  LYS A O   1 
ATOM   900   C  CB  . LYS A  1 122 ? 61.422  54.434  25.623 1.00 29.90  ? 122  LYS A CB  1 
ATOM   901   C  CG  . LYS A  1 122 ? 62.558  54.439  26.634 1.00 34.96  ? 122  LYS A CG  1 
ATOM   902   C  CD  . LYS A  1 122 ? 63.319  55.762  26.564 1.00 43.52  ? 122  LYS A CD  1 
ATOM   903   C  CE  . LYS A  1 122 ? 64.428  55.712  25.526 1.00 58.01  ? 122  LYS A CE  1 
ATOM   904   N  NZ  . LYS A  1 122 ? 65.047  57.040  25.246 1.00 65.06  ? 122  LYS A NZ  1 
ATOM   905   N  N   . ALA A  1 123 ? 58.800  54.401  24.286 1.00 28.84  ? 123  ALA A N   1 
ATOM   906   C  CA  . ALA A  1 123 ? 58.055  54.550  23.048 1.00 26.11  ? 123  ALA A CA  1 
ATOM   907   C  C   . ALA A  1 123 ? 58.955  54.571  21.817 1.00 28.06  ? 123  ALA A C   1 
ATOM   908   O  O   . ALA A  1 123 ? 60.083  55.075  21.785 1.00 28.96  ? 123  ALA A O   1 
ATOM   909   C  CB  . ALA A  1 123 ? 57.272  55.863  23.093 1.00 35.42  ? 123  ALA A CB  1 
ATOM   910   N  N   . ASP A  1 124 ? 58.426  54.008  20.736 1.00 25.72  ? 124  ASP A N   1 
ATOM   911   C  CA  . ASP A  1 124 ? 59.053  54.152  19.424 1.00 25.23  ? 124  ASP A CA  1 
ATOM   912   C  C   . ASP A  1 124 ? 58.538  55.473  18.827 1.00 27.69  ? 124  ASP A C   1 
ATOM   913   O  O   . ASP A  1 124 ? 57.312  55.612  18.770 1.00 28.74  ? 124  ASP A O   1 
ATOM   914   C  CB  . ASP A  1 124 ? 58.644  52.968  18.565 1.00 25.75  ? 124  ASP A CB  1 
ATOM   915   C  CG  . ASP A  1 124 ? 59.323  52.874  17.220 1.00 30.52  ? 124  ASP A CG  1 
ATOM   916   O  OD1 . ASP A  1 124 ? 59.397  51.721  16.708 1.00 30.28  ? 124  ASP A OD1 1 
ATOM   917   O  OD2 . ASP A  1 124 ? 59.763  53.921  16.691 1.00 27.89  ? 124  ASP A OD2 1 
ATOM   918   N  N   . ASP A  1 125 ? 59.397  56.379  18.415 1.00 26.03  ? 125  ASP A N   1 
ATOM   919   C  CA  . ASP A  1 125 ? 58.983  57.657  17.839 1.00 29.03  ? 125  ASP A CA  1 
ATOM   920   C  C   . ASP A  1 125 ? 58.669  57.501  16.355 1.00 32.63  ? 125  ASP A C   1 
ATOM   921   O  O   . ASP A  1 125 ? 58.497  58.499  15.654 1.00 32.13  ? 125  ASP A O   1 
ATOM   922   C  CB  . ASP A  1 125 ? 60.069  58.696  18.076 1.00 31.14  ? 125  ASP A CB  1 
ATOM   923   C  CG  . ASP A  1 125 ? 61.375  58.479  17.351 1.00 34.70  ? 125  ASP A CG  1 
ATOM   924   O  OD1 . ASP A  1 125 ? 62.391  59.086  17.766 1.00 34.73  ? 125  ASP A OD1 1 
ATOM   925   O  OD2 . ASP A  1 125 ? 61.451  57.721  16.354 1.00 28.98  ? 125  ASP A OD2 1 
ATOM   926   N  N   . LEU A  1 126 ? 58.630  56.275  15.871 1.00 29.28  ? 126  LEU A N   1 
ATOM   927   C  CA  . LEU A  1 126 ? 58.280  55.901  14.504 1.00 25.50  ? 126  LEU A CA  1 
ATOM   928   C  C   . LEU A  1 126 ? 59.142  56.528  13.424 1.00 29.28  ? 126  LEU A C   1 
ATOM   929   O  O   . LEU A  1 126 ? 58.703  56.703  12.273 1.00 30.54  ? 126  LEU A O   1 
ATOM   930   C  CB  . LEU A  1 126 ? 56.790  56.239  14.274 1.00 28.29  ? 126  LEU A CB  1 
ATOM   931   C  CG  . LEU A  1 126 ? 55.848  55.659  15.338 1.00 32.81  ? 126  LEU A CG  1 
ATOM   932   C  CD1 . LEU A  1 126 ? 54.407  55.983  14.976 1.00 35.73  ? 126  LEU A CD1 1 
ATOM   933   C  CD2 . LEU A  1 126 ? 56.022  54.157  15.504 1.00 27.29  ? 126  LEU A CD2 1 
ATOM   934   N  N   . GLY A  1 127 ? 60.377  56.873  13.778 1.00 27.55  ? 127  GLY A N   1 
ATOM   935   C  CA  . GLY A  1 127 ? 61.360  57.405  12.861 1.00 30.78  ? 127  GLY A CA  1 
ATOM   936   C  C   . GLY A  1 127 ? 61.211  58.901  12.637 1.00 36.75  ? 127  GLY A C   1 
ATOM   937   O  O   . GLY A  1 127 ? 61.851  59.464  11.744 1.00 34.72  ? 127  GLY A O   1 
ATOM   938   N  N   . LYS A  1 128 ? 60.354  59.528  13.445 1.00 35.17  ? 128  LYS A N   1 
ATOM   939   C  CA  . LYS A  1 128 ? 60.071  60.955  13.229 1.00 33.00  ? 128  LYS A CA  1 
ATOM   940   C  C   . LYS A  1 128 ? 60.705  61.801  14.337 1.00 43.10  ? 128  LYS A C   1 
ATOM   941   O  O   . LYS A  1 128 ? 60.242  62.921  14.554 1.00 45.51  ? 128  LYS A O   1 
ATOM   942   C  CB  . LYS A  1 128 ? 58.580  61.220  13.174 1.00 34.01  ? 128  LYS A CB  1 
ATOM   943   C  CG  . LYS A  1 128 ? 57.709  60.208  12.448 1.00 36.21  ? 128  LYS A CG  1 
ATOM   944   C  CD  . LYS A  1 128 ? 58.072  60.067  10.983 1.00 38.10  ? 128  LYS A CD  1 
ATOM   945   C  CE  . LYS A  1 128 ? 57.013  59.368  10.160 1.00 36.67  ? 128  LYS A CE  1 
ATOM   946   N  NZ  . LYS A  1 128 ? 56.367  58.208  10.835 1.00 39.41  ? 128  LYS A NZ  1 
ATOM   947   N  N   . GLY A  1 129 ? 61.720  61.268  15.003 1.00 41.07  ? 129  GLY A N   1 
ATOM   948   C  CA  . GLY A  1 129 ? 62.407  61.890  16.117 1.00 43.52  ? 129  GLY A CA  1 
ATOM   949   C  C   . GLY A  1 129 ? 63.464  62.886  15.703 1.00 44.76  ? 129  GLY A C   1 
ATOM   950   O  O   . GLY A  1 129 ? 64.092  63.570  16.514 1.00 56.04  ? 129  GLY A O   1 
ATOM   951   N  N   . GLY A  1 130 ? 63.712  63.015  14.401 1.00 50.13  ? 130  GLY A N   1 
ATOM   952   C  CA  . GLY A  1 130 ? 64.618  64.061  13.959 1.00 51.72  ? 130  GLY A CA  1 
ATOM   953   C  C   . GLY A  1 130 ? 66.049  63.853  14.381 1.00 56.73  ? 130  GLY A C   1 
ATOM   954   O  O   . GLY A  1 130 ? 66.856  64.785  14.454 1.00 61.79  ? 130  GLY A O   1 
ATOM   955   N  N   . ASN A  1 131 ? 66.443  62.613  14.671 1.00 47.70  ? 131  ASN A N   1 
ATOM   956   C  CA  . ASN A  1 131 ? 67.875  62.392  14.896 1.00 46.34  ? 131  ASN A CA  1 
ATOM   957   C  C   . ASN A  1 131 ? 68.252  61.039  14.306 1.00 53.76  ? 131  ASN A C   1 
ATOM   958   O  O   . ASN A  1 131 ? 67.362  60.235  14.017 1.00 54.83  ? 131  ASN A O   1 
ATOM   959   C  CB  . ASN A  1 131 ? 68.237  62.476  16.373 1.00 49.06  ? 131  ASN A CB  1 
ATOM   960   C  CG  . ASN A  1 131 ? 67.377  61.570  17.234 1.00 52.74  ? 131  ASN A CG  1 
ATOM   961   O  OD1 . ASN A  1 131 ? 66.915  60.538  16.754 1.00 35.92  ? 131  ASN A OD1 1 
ATOM   962   N  ND2 . ASN A  1 131 ? 67.163  61.955  18.483 1.00 57.69  ? 131  ASN A ND2 1 
ATOM   963   N  N   . GLU A  1 132 ? 69.546  60.796  14.123 1.00 50.07  ? 132  GLU A N   1 
ATOM   964   C  CA  . GLU A  1 132 ? 69.939  59.549  13.473 1.00 47.41  ? 132  GLU A CA  1 
ATOM   965   C  C   . GLU A  1 132 ? 69.520  58.333  14.279 1.00 45.66  ? 132  GLU A C   1 
ATOM   966   O  O   . GLU A  1 132 ? 69.271  57.270  13.697 1.00 41.76  ? 132  GLU A O   1 
ATOM   967   C  CB  . GLU A  1 132 ? 71.452  59.534  13.214 1.00 40.86  ? 132  GLU A CB  1 
ATOM   968   C  CG  . GLU A  1 132 ? 71.768  60.105  11.831 1.00 55.95  ? 132  GLU A CG  1 
ATOM   969   C  CD  . GLU A  1 132 ? 72.660  59.198  11.006 1.00 74.76  ? 132  GLU A CD  1 
ATOM   970   O  OE1 . GLU A  1 132 ? 72.111  58.366  10.247 1.00 99.31  ? 132  GLU A OE1 1 
ATOM   971   O  OE2 . GLU A  1 132 ? 73.901  59.317  11.110 1.00 76.75  ? 132  GLU A OE2 1 
ATOM   972   N  N   . GLU A  1 133 ? 69.422  58.444  15.604 1.00 36.33  ? 133  GLU A N   1 
ATOM   973   C  CA  . GLU A  1 133 ? 68.939  57.264  16.328 1.00 37.93  ? 133  GLU A CA  1 
ATOM   974   C  C   . GLU A  1 133 ? 67.488  56.980  15.943 1.00 40.69  ? 133  GLU A C   1 
ATOM   975   O  O   . GLU A  1 133 ? 67.054  55.829  15.825 1.00 32.85  ? 133  GLU A O   1 
ATOM   976   C  CB  . GLU A  1 133 ? 69.099  57.457  17.829 1.00 47.57  ? 133  GLU A CB  1 
ATOM   977   C  CG  . GLU A  1 133 ? 68.863  56.226  18.676 1.00 53.85  ? 133  GLU A CG  1 
ATOM   978   C  CD  . GLU A  1 133 ? 69.980  55.199  18.632 1.00 46.88  ? 133  GLU A CD  1 
ATOM   979   O  OE1 . GLU A  1 133 ? 69.869  54.195  19.365 1.00 57.97  ? 133  GLU A OE1 1 
ATOM   980   O  OE2 . GLU A  1 133 ? 70.958  55.376  17.887 1.00 45.04  ? 133  GLU A OE2 1 
ATOM   981   N  N   . SER A  1 134 ? 66.695  58.036  15.730 1.00 30.29  ? 134  SER A N   1 
ATOM   982   C  CA  . SER A  1 134 ? 65.288  57.820  15.434 1.00 30.34  ? 134  SER A CA  1 
ATOM   983   C  C   . SER A  1 134 ? 65.138  57.004  14.159 1.00 34.19  ? 134  SER A C   1 
ATOM   984   O  O   . SER A  1 134 ? 64.229  56.167  14.088 1.00 31.75  ? 134  SER A O   1 
ATOM   985   C  CB  . SER A  1 134 ? 64.540  59.149  15.312 1.00 35.53  ? 134  SER A CB  1 
ATOM   986   O  OG  . SER A  1 134 ? 63.232  58.966  14.789 1.00 37.24  ? 134  SER A OG  1 
ATOM   987   N  N   . THR A  1 135 ? 65.988  57.224  13.150 1.00 35.33  ? 135  THR A N   1 
ATOM   988   C  CA  . THR A  1 135 ? 65.750  56.470  11.908 1.00 40.73  ? 135  THR A CA  1 
ATOM   989   C  C   . THR A  1 135 ? 66.484  55.124  11.859 1.00 34.82  ? 135  THR A C   1 
ATOM   990   O  O   . THR A  1 135 ? 66.550  54.498  10.794 1.00 35.14  ? 135  THR A O   1 
ATOM   991   C  CB  . THR A  1 135 ? 66.087  57.308  10.659 1.00 47.85  ? 135  THR A CB  1 
ATOM   992   O  OG1 . THR A  1 135 ? 67.157  58.209  10.921 1.00 46.23  ? 135  THR A OG1 1 
ATOM   993   C  CG2 . THR A  1 135 ? 64.880  58.169  10.277 1.00 50.12  ? 135  THR A CG2 1 
ATOM   994   N  N   . LYS A  1 136 ? 67.001  54.694  12.993 1.00 27.73  ? 136  LYS A N   1 
ATOM   995   C  CA  . LYS A  1 136 ? 67.588  53.380  13.233 1.00 33.70  ? 136  LYS A CA  1 
ATOM   996   C  C   . LYS A  1 136 ? 66.736  52.521  14.168 1.00 33.93  ? 136  LYS A C   1 
ATOM   997   O  O   . LYS A  1 136 ? 66.319  51.404  13.829 1.00 31.80  ? 136  LYS A O   1 
ATOM   998   C  CB  . LYS A  1 136 ? 69.000  53.555  13.794 1.00 44.92  ? 136  LYS A CB  1 
ATOM   999   C  CG  . LYS A  1 136 ? 69.764  52.278  14.115 1.00 50.64  ? 136  LYS A CG  1 
ATOM   1000  C  CD  . LYS A  1 136 ? 70.530  52.451  15.420 1.00 57.78  ? 136  LYS A CD  1 
ATOM   1001  C  CE  . LYS A  1 136 ? 71.508  51.322  15.684 1.00 60.18  ? 136  LYS A CE  1 
ATOM   1002  N  NZ  . LYS A  1 136 ? 72.643  51.800  16.530 1.00 63.22  ? 136  LYS A NZ  1 
ATOM   1003  N  N   . THR A  1 137 ? 66.451  52.998  15.379 1.00 28.28  ? 137  THR A N   1 
ATOM   1004  C  CA  . THR A  1 137 ? 65.656  52.246  16.332 1.00 29.00  ? 137  THR A CA  1 
ATOM   1005  C  C   . THR A  1 137 ? 64.377  52.925  16.781 1.00 30.03  ? 137  THR A C   1 
ATOM   1006  O  O   . THR A  1 137 ? 63.611  52.384  17.589 1.00 27.21  ? 137  THR A O   1 
ATOM   1007  C  CB  . THR A  1 137 ? 66.494  52.032  17.618 1.00 35.89  ? 137  THR A CB  1 
ATOM   1008  O  OG1 . THR A  1 137 ? 66.718  53.330  18.203 1.00 38.53  ? 137  THR A OG1 1 
ATOM   1009  C  CG2 . THR A  1 137 ? 67.840  51.412  17.302 1.00 34.04  ? 137  THR A CG2 1 
ATOM   1010  N  N   . GLY A  1 138 ? 64.098  54.158  16.347 1.00 28.97  ? 138  GLY A N   1 
ATOM   1011  C  CA  . GLY A  1 138 ? 62.932  54.853  16.905 1.00 24.83  ? 138  GLY A CA  1 
ATOM   1012  C  C   . GLY A  1 138 ? 63.144  55.399  18.305 1.00 25.90  ? 138  GLY A C   1 
ATOM   1013  O  O   . GLY A  1 138 ? 62.201  55.832  18.975 1.00 29.64  ? 138  GLY A O   1 
ATOM   1014  N  N   . ASN A  1 139 ? 64.368  55.397  18.810 1.00 30.29  ? 139  ASN A N   1 
ATOM   1015  C  CA  . ASN A  1 139 ? 64.629  55.867  20.171 1.00 37.30  ? 139  ASN A CA  1 
ATOM   1016  C  C   . ASN A  1 139 ? 63.879  55.044  21.196 1.00 29.91  ? 139  ASN A C   1 
ATOM   1017  O  O   . ASN A  1 139 ? 63.453  55.552  22.246 1.00 31.44  ? 139  ASN A O   1 
ATOM   1018  C  CB  . ASN A  1 139 ? 64.249  57.361  20.284 1.00 33.72  ? 139  ASN A CB  1 
ATOM   1019  C  CG  . ASN A  1 139 ? 65.313  58.244  19.638 1.00 30.84  ? 139  ASN A CG  1 
ATOM   1020  O  OD1 . ASN A  1 139 ? 66.480  58.230  20.034 1.00 35.92  ? 139  ASN A OD1 1 
ATOM   1021  N  ND2 . ASN A  1 139 ? 64.910  59.001  18.631 1.00 34.69  ? 139  ASN A ND2 1 
ATOM   1022  N  N   . ALA A  1 140 ? 63.678  53.741  20.944 1.00 27.37  ? 140  ALA A N   1 
ATOM   1023  C  CA  . ALA A  1 140 ? 62.821  52.974  21.854 1.00 23.64  ? 140  ALA A CA  1 
ATOM   1024  C  C   . ALA A  1 140 ? 63.562  52.422  23.066 1.00 26.84  ? 140  ALA A C   1 
ATOM   1025  O  O   . ALA A  1 140 ? 62.977  51.777  23.936 1.00 27.73  ? 140  ALA A O   1 
ATOM   1026  C  CB  . ALA A  1 140 ? 62.128  51.866  21.067 1.00 27.61  ? 140  ALA A CB  1 
ATOM   1027  N  N   . GLY A  1 141 ? 64.856  52.665  23.179 1.00 27.34  ? 141  GLY A N   1 
ATOM   1028  C  CA  . GLY A  1 141 ? 65.642  52.256  24.321 1.00 29.96  ? 141  GLY A CA  1 
ATOM   1029  C  C   . GLY A  1 141 ? 65.871  50.773  24.464 1.00 29.56  ? 141  GLY A C   1 
ATOM   1030  O  O   . GLY A  1 141 ? 65.873  49.955  23.549 1.00 29.08  ? 141  GLY A O   1 
ATOM   1031  N  N   . SER A  1 142 ? 66.077  50.344  25.702 1.00 28.95  ? 142  SER A N   1 
ATOM   1032  C  CA  . SER A  1 142 ? 66.510  48.980  25.982 1.00 29.74  ? 142  SER A CA  1 
ATOM   1033  C  C   . SER A  1 142 ? 65.462  47.939  25.637 1.00 26.43  ? 142  SER A C   1 
ATOM   1034  O  O   . SER A  1 142 ? 64.263  48.164  25.463 1.00 27.52  ? 142  SER A O   1 
ATOM   1035  C  CB  . SER A  1 142 ? 66.923  48.907  27.463 1.00 33.48  ? 142  SER A CB  1 
ATOM   1036  O  OG  . SER A  1 142 ? 65.769  48.794  28.279 1.00 39.86  ? 142  SER A OG  1 
ATOM   1037  N  N   . ARG A  1 143 ? 65.949  46.698  25.509 1.00 24.51  ? 143  ARG A N   1 
ATOM   1038  C  CA  . ARG A  1 143 ? 65.063  45.589  25.168 1.00 25.01  ? 143  ARG A CA  1 
ATOM   1039  C  C   . ARG A  1 143 ? 64.634  44.889  26.449 1.00 30.11  ? 143  ARG A C   1 
ATOM   1040  O  O   . ARG A  1 143 ? 65.459  44.301  27.155 1.00 27.05  ? 143  ARG A O   1 
ATOM   1041  C  CB  . ARG A  1 143 ? 65.774  44.649  24.180 1.00 21.72  ? 143  ARG A CB  1 
ATOM   1042  C  CG  . ARG A  1 143 ? 66.447  45.403  23.051 1.00 21.89  ? 143  ARG A CG  1 
ATOM   1043  C  CD  . ARG A  1 143 ? 67.343  44.516  22.187 1.00 27.11  ? 143  ARG A CD  1 
ATOM   1044  N  NE  . ARG A  1 143 ? 67.900  45.268  21.064 1.00 26.06  ? 143  ARG A NE  1 
ATOM   1045  C  CZ  . ARG A  1 143 ? 68.593  44.792  20.048 1.00 25.56  ? 143  ARG A CZ  1 
ATOM   1046  N  NH1 . ARG A  1 143 ? 69.030  45.602  19.090 1.00 23.86  ? 143  ARG A NH1 1 
ATOM   1047  N  NH2 . ARG A  1 143 ? 68.856  43.489  19.980 1.00 24.78  ? 143  ARG A NH2 1 
ATOM   1048  N  N   . LEU A  1 144 ? 63.348  44.951  26.793 1.00 23.67  ? 144  LEU A N   1 
ATOM   1049  C  CA  . LEU A  1 144 ? 62.901  44.427  28.079 1.00 23.05  ? 144  LEU A CA  1 
ATOM   1050  C  C   . LEU A  1 144 ? 62.547  42.955  28.032 1.00 25.28  ? 144  LEU A C   1 
ATOM   1051  O  O   . LEU A  1 144 ? 62.616  42.191  29.001 1.00 25.68  ? 144  LEU A O   1 
ATOM   1052  C  CB  . LEU A  1 144 ? 61.657  45.194  28.571 1.00 22.73  ? 144  LEU A CB  1 
ATOM   1053  C  CG  . LEU A  1 144 ? 61.860  46.695  28.765 1.00 26.58  ? 144  LEU A CG  1 
ATOM   1054  C  CD1 . LEU A  1 144 ? 60.631  47.275  29.443 1.00 34.39  ? 144  LEU A CD1 1 
ATOM   1055  C  CD2 . LEU A  1 144 ? 63.125  46.982  29.566 1.00 28.15  ? 144  LEU A CD2 1 
ATOM   1056  N  N   . ALA A  1 145 ? 62.128  42.497  26.850 1.00 20.64  ? 145  ALA A N   1 
ATOM   1057  C  CA  . ALA A  1 145 ? 61.781  41.099  26.744 1.00 19.48  ? 145  ALA A CA  1 
ATOM   1058  C  C   . ALA A  1 145 ? 61.709  40.719  25.255 1.00 20.70  ? 145  ALA A C   1 
ATOM   1059  O  O   . ALA A  1 145 ? 61.504  41.618  24.445 1.00 19.46  ? 145  ALA A O   1 
ATOM   1060  C  CB  . ALA A  1 145 ? 60.446  40.771  27.388 1.00 22.94  ? 145  ALA A CB  1 
ATOM   1061  N  N   . CYS A  1 146 ? 61.880  39.414  25.045 1.00 22.88  ? 146  CYS A N   1 
ATOM   1062  C  CA  . CYS A  1 146 ? 61.938  38.964  23.641 1.00 18.89  ? 146  CYS A CA  1 
ATOM   1063  C  C   . CYS A  1 146 ? 61.713  37.481  23.567 1.00 18.78  ? 146  CYS A C   1 
ATOM   1064  O  O   . CYS A  1 146 ? 61.716  36.775  24.581 1.00 22.88  ? 146  CYS A O   1 
ATOM   1065  C  CB  A CYS A  1 146 ? 63.296  39.347  23.048 0.40 21.36  ? 146  CYS A CB  1 
ATOM   1066  C  CB  B CYS A  1 146 ? 63.275  39.396  23.039 0.60 21.47  ? 146  CYS A CB  1 
ATOM   1067  S  SG  A CYS A  1 146 ? 64.689  38.754  24.042 0.40 36.60  ? 146  CYS A SG  1 
ATOM   1068  S  SG  B CYS A  1 146 ? 64.716  38.435  23.539 0.60 21.97  ? 146  CYS A SG  1 
ATOM   1069  N  N   . GLY A  1 147 ? 61.511  36.983  22.344 1.00 19.73  ? 147  GLY A N   1 
ATOM   1070  C  CA  . GLY A  1 147 ? 61.442  35.534  22.153 1.00 21.30  ? 147  GLY A CA  1 
ATOM   1071  C  C   . GLY A  1 147 ? 61.641  35.200  20.683 1.00 23.14  ? 147  GLY A C   1 
ATOM   1072  O  O   . GLY A  1 147 ? 61.437  36.068  19.837 1.00 21.18  ? 147  GLY A O   1 
ATOM   1073  N  N   . VAL A  1 148 ? 62.017  33.963  20.362 1.00 19.98  ? 148  VAL A N   1 
ATOM   1074  C  CA  . VAL A  1 148 ? 62.037  33.559  18.957 1.00 18.80  ? 148  VAL A CA  1 
ATOM   1075  C  C   . VAL A  1 148 ? 60.637  33.223  18.467 1.00 22.70  ? 148  VAL A C   1 
ATOM   1076  O  O   . VAL A  1 148 ? 59.849  32.581  19.160 1.00 23.25  ? 148  VAL A O   1 
ATOM   1077  C  CB  . VAL A  1 148 ? 62.946  32.326  18.762 1.00 20.04  ? 148  VAL A CB  1 
ATOM   1078  C  CG1 . VAL A  1 148 ? 63.113  31.978  17.289 1.00 20.62  ? 148  VAL A CG1 1 
ATOM   1079  C  CG2 . VAL A  1 148 ? 64.305  32.651  19.389 1.00 23.97  ? 148  VAL A CG2 1 
ATOM   1080  N  N   . ILE A  1 149 ? 60.330  33.643  17.239 1.00 19.68  ? 149  ILE A N   1 
ATOM   1081  C  CA  . ILE A  1 149 ? 59.004  33.385  16.677 1.00 19.31  ? 149  ILE A CA  1 
ATOM   1082  C  C   . ILE A  1 149 ? 58.941  32.004  16.073 1.00 18.34  ? 149  ILE A C   1 
ATOM   1083  O  O   . ILE A  1 149 ? 59.713  31.717  15.152 1.00 23.47  ? 149  ILE A O   1 
ATOM   1084  C  CB  . ILE A  1 149 ? 58.696  34.450  15.609 1.00 20.68  ? 149  ILE A CB  1 
ATOM   1085  C  CG1 . ILE A  1 149 ? 58.627  35.859  16.217 1.00 21.93  ? 149  ILE A CG1 1 
ATOM   1086  C  CG2 . ILE A  1 149 ? 57.433  34.156  14.816 1.00 23.17  ? 149  ILE A CG2 1 
ATOM   1087  C  CD1 . ILE A  1 149 ? 58.697  36.981  15.187 1.00 27.11  ? 149  ILE A CD1 1 
ATOM   1088  N  N   . GLY A  1 150 ? 58.073  31.144  16.570 1.00 19.08  ? 150  GLY A N   1 
ATOM   1089  C  CA  . GLY A  1 150 ? 58.045  29.762  16.142 1.00 21.58  ? 150  GLY A CA  1 
ATOM   1090  C  C   . GLY A  1 150 ? 56.767  29.383  15.422 1.00 23.40  ? 150  GLY A C   1 
ATOM   1091  O  O   . GLY A  1 150 ? 55.731  30.037  15.555 1.00 21.85  ? 150  GLY A O   1 
ATOM   1092  N  N   . ILE A  1 151 ? 56.867  28.285  14.690 1.00 20.52  ? 151  ILE A N   1 
ATOM   1093  C  CA  . ILE A  1 151 ? 55.714  27.733  13.990 1.00 23.56  ? 151  ILE A CA  1 
ATOM   1094  C  C   . ILE A  1 151 ? 54.727  27.132  14.972 1.00 22.22  ? 151  ILE A C   1 
ATOM   1095  O  O   . ILE A  1 151 ? 55.115  26.373  15.857 1.00 25.16  ? 151  ILE A O   1 
ATOM   1096  C  CB  . ILE A  1 151 ? 56.160  26.659  12.979 1.00 29.53  ? 151  ILE A CB  1 
ATOM   1097  C  CG1 . ILE A  1 151 ? 56.962  27.252  11.818 1.00 27.44  ? 151  ILE A CG1 1 
ATOM   1098  C  CG2 . ILE A  1 151 ? 54.973  25.830  12.492 1.00 28.38  ? 151  ILE A CG2 1 
ATOM   1099  C  CD1 . ILE A  1 151 ? 57.819  26.251  11.061 1.00 36.88  ? 151  ILE A CD1 1 
ATOM   1100  N  N   . ALA A  1 152 ? 53.443  27.470  14.804 1.00 21.34  ? 152  ALA A N   1 
ATOM   1101  C  CA  . ALA A  1 152 ? 52.409  26.973  15.707 1.00 22.15  ? 152  ALA A CA  1 
ATOM   1102  C  C   . ALA A  1 152 ? 51.418  26.058  14.997 1.00 29.35  ? 152  ALA A C   1 
ATOM   1103  O  O   . ALA A  1 152 ? 51.274  26.020  13.775 1.00 27.30  ? 152  ALA A O   1 
ATOM   1104  C  CB  . ALA A  1 152 ? 51.674  28.156  16.330 1.00 30.80  ? 152  ALA A CB  1 
ATOM   1105  N  N   . GLN A  1 153 ? 50.709  25.258  15.786 1.00 23.25  ? 153  GLN A N   1 
ATOM   1106  C  CA  . GLN A  1 153 ? 49.798  24.291  15.189 1.00 25.18  ? 153  GLN A CA  1 
ATOM   1107  C  C   . GLN A  1 153 ? 48.547  24.975  14.648 1.00 45.07  ? 153  GLN A C   1 
ATOM   1108  O  O   . GLN A  1 153 ? 47.950  25.771  15.412 1.00 43.23  ? 153  GLN A O   1 
ATOM   1109  C  CB  . GLN A  1 153 ? 49.424  23.241  16.234 1.00 25.81  ? 153  GLN A CB  1 
ATOM   1110  C  CG  . GLN A  1 153 ? 48.370  22.241  15.764 1.00 39.03  ? 153  GLN A CG  1 
ATOM   1111  C  CD  . GLN A  1 153 ? 48.146  21.191  16.839 1.00 47.78  ? 153  GLN A CD  1 
ATOM   1112  O  OE1 . GLN A  1 153 ? 48.215  19.994  16.567 1.00 54.37  ? 153  GLN A OE1 1 
ATOM   1113  N  NE2 . GLN A  1 153 ? 47.890  21.691  18.043 1.00 42.97  ? 153  GLN A NE2 1 
ATOM   1114  O  OXT . GLN A  1 153 ? 48.198  24.704  13.479 1.00 57.36  ? 153  GLN A OXT 1 
ATOM   1115  N  N   . ALA B  1 1   ? 77.144  29.633  4.479  1.00 58.84  ? 1    ALA B N   1 
ATOM   1116  C  CA  . ALA B  1 1   ? 75.752  29.930  4.143  1.00 66.88  ? 1    ALA B CA  1 
ATOM   1117  C  C   . ALA B  1 1   ? 74.847  30.046  5.362  1.00 51.12  ? 1    ALA B C   1 
ATOM   1118  O  O   . ALA B  1 1   ? 75.044  30.846  6.284  1.00 46.92  ? 1    ALA B O   1 
ATOM   1119  C  CB  . ALA B  1 1   ? 75.203  28.877  3.180  1.00 72.24  ? 1    ALA B CB  1 
ATOM   1120  N  N   . THR B  1 2   ? 73.775  29.262  5.403  1.00 42.54  ? 2    THR B N   1 
ATOM   1121  C  CA  . THR B  1 2   ? 72.793  29.451  6.473  1.00 33.45  ? 2    THR B CA  1 
ATOM   1122  C  C   . THR B  1 2   ? 73.385  28.969  7.797  1.00 28.86  ? 2    THR B C   1 
ATOM   1123  O  O   . THR B  1 2   ? 74.173  28.024  7.928  1.00 26.73  ? 2    THR B O   1 
ATOM   1124  C  CB  . THR B  1 2   ? 71.465  28.743  6.145  1.00 39.30  ? 2    THR B CB  1 
ATOM   1125  O  OG1 . THR B  1 2   ? 71.408  28.503  4.735  1.00 57.99  ? 2    THR B OG1 1 
ATOM   1126  C  CG2 . THR B  1 2   ? 70.240  29.581  6.466  1.00 48.37  ? 2    THR B CG2 1 
ATOM   1127  N  N   . LYS B  1 3   ? 72.999  29.732  8.823  1.00 23.51  ? 3    LYS B N   1 
ATOM   1128  C  CA  . LYS B  1 3   ? 73.328  29.405  10.206 1.00 19.24  ? 3    LYS B CA  1 
ATOM   1129  C  C   . LYS B  1 3   ? 72.054  29.550  11.045 1.00 20.86  ? 3    LYS B C   1 
ATOM   1130  O  O   . LYS B  1 3   ? 71.199  30.397  10.754 1.00 19.84  ? 3    LYS B O   1 
ATOM   1131  C  CB  . LYS B  1 3   ? 74.389  30.324  10.796 1.00 23.01  ? 3    LYS B CB  1 
ATOM   1132  C  CG  . LYS B  1 3   ? 75.774  30.152  10.191 1.00 29.10  ? 3    LYS B CG  1 
ATOM   1133  C  CD  . LYS B  1 3   ? 76.736  31.216  10.717 1.00 32.86  ? 3    LYS B CD  1 
ATOM   1134  C  CE  . LYS B  1 3   ? 77.379  30.840  12.037 1.00 29.24  ? 3    LYS B CE  1 
ATOM   1135  N  NZ  . LYS B  1 3   ? 78.234  31.938  12.594 1.00 34.80  ? 3    LYS B NZ  1 
ATOM   1136  N  N   . ALA B  1 4   ? 71.969  28.697  12.064 1.00 20.52  ? 4    ALA B N   1 
ATOM   1137  C  CA  . ALA B  1 4   ? 70.869  28.827  13.011 1.00 18.86  ? 4    ALA B CA  1 
ATOM   1138  C  C   . ALA B  1 4   ? 71.427  28.556  14.412 1.00 20.08  ? 4    ALA B C   1 
ATOM   1139  O  O   . ALA B  1 4   ? 72.560  28.094  14.560 1.00 19.28  ? 4    ALA B O   1 
ATOM   1140  C  CB  . ALA B  1 4   ? 69.717  27.886  12.715 1.00 20.02  ? 4    ALA B CB  1 
ATOM   1141  N  N   . VAL B  1 5   ? 70.602  28.848  15.415 1.00 17.86  ? 5    VAL B N   1 
ATOM   1142  C  CA  . VAL B  1 5   ? 71.078  28.654  16.782 1.00 16.97  ? 5    VAL B CA  1 
ATOM   1143  C  C   . VAL B  1 5   ? 69.873  28.401  17.672 1.00 20.26  ? 5    VAL B C   1 
ATOM   1144  O  O   . VAL B  1 5   ? 68.747  28.753  17.339 1.00 19.92  ? 5    VAL B O   1 
ATOM   1145  C  CB  . VAL B  1 5   ? 71.879  29.877  17.260 1.00 18.45  ? 5    VAL B CB  1 
ATOM   1146  C  CG1 . VAL B  1 5   ? 70.992  31.087  17.503 1.00 21.14  ? 5    VAL B CG1 1 
ATOM   1147  C  CG2 . VAL B  1 5   ? 72.640  29.552  18.547 1.00 19.91  ? 5    VAL B CG2 1 
ATOM   1148  N  N   . CYS B  1 6   ? 70.098  27.754  18.814 1.00 20.16  ? 6    CYS B N   1 
ATOM   1149  C  CA  . CYS B  1 6   ? 69.006  27.354  19.689 1.00 20.12  ? 6    CYS B CA  1 
ATOM   1150  C  C   . CYS B  1 6   ? 69.521  27.393  21.117 1.00 22.27  ? 6    CYS B C   1 
ATOM   1151  O  O   . CYS B  1 6   ? 70.600  26.842  21.380 1.00 21.66  ? 6    CYS B O   1 
ATOM   1152  C  CB  . CYS B  1 6   ? 68.516  25.942  19.335 1.00 20.10  ? 6    CYS B CB  1 
ATOM   1153  S  SG  . CYS B  1 6   ? 67.187  25.353  20.398 1.00 25.91  ? 6    CYS B SG  1 
ATOM   1154  N  N   . VAL B  1 7   ? 68.778  28.035  21.995 1.00 19.85  ? 7    VAL B N   1 
ATOM   1155  C  CA  . VAL B  1 7   ? 69.146  28.034  23.414 1.00 17.19  ? 7    VAL B CA  1 
ATOM   1156  C  C   . VAL B  1 7   ? 68.211  27.074  24.132 1.00 19.33  ? 7    VAL B C   1 
ATOM   1157  O  O   . VAL B  1 7   ? 66.985  27.319  24.068 1.00 19.27  ? 7    VAL B O   1 
ATOM   1158  C  CB  . VAL B  1 7   ? 68.991  29.448  24.006 1.00 22.57  ? 7    VAL B CB  1 
ATOM   1159  C  CG1 . VAL B  1 7   ? 69.269  29.400  25.507 1.00 27.71  ? 7    VAL B CG1 1 
ATOM   1160  C  CG2 . VAL B  1 7   ? 69.882  30.450  23.300 1.00 23.59  ? 7    VAL B CG2 1 
ATOM   1161  N  N   . LEU B  1 8   ? 68.774  26.038  24.745 1.00 19.47  ? 8    LEU B N   1 
ATOM   1162  C  CA  . LEU B  1 8   ? 67.992  24.989  25.397 1.00 22.08  ? 8    LEU B CA  1 
ATOM   1163  C  C   . LEU B  1 8   ? 67.736  25.376  26.849 1.00 23.77  ? 8    LEU B C   1 
ATOM   1164  O  O   . LEU B  1 8   ? 68.705  25.703  27.543 1.00 25.59  ? 8    LEU B O   1 
ATOM   1165  C  CB  . LEU B  1 8   ? 68.723  23.630  25.337 1.00 19.82  ? 8    LEU B CB  1 
ATOM   1166  C  CG  . LEU B  1 8   ? 68.771  22.985  23.949 1.00 25.39  ? 8    LEU B CG  1 
ATOM   1167  C  CD1 . LEU B  1 8   ? 69.618  21.710  23.931 1.00 27.90  ? 8    LEU B CD1 1 
ATOM   1168  C  CD2 . LEU B  1 8   ? 67.381  22.624  23.452 1.00 31.27  ? 8    LEU B CD2 1 
ATOM   1169  N  N   . LYS B  1 9   ? 66.508  25.347  27.306 1.00 24.12  ? 9    LYS B N   1 
ATOM   1170  C  CA  . LYS B  1 9   ? 66.190  25.594  28.709 1.00 24.33  ? 9    LYS B CA  1 
ATOM   1171  C  C   . LYS B  1 9   ? 65.006  24.725  29.111 1.00 26.80  ? 9    LYS B C   1 
ATOM   1172  O  O   . LYS B  1 9   ? 64.162  24.372  28.277 1.00 23.48  ? 9    LYS B O   1 
ATOM   1173  C  CB  . LYS B  1 9   ? 65.869  27.068  28.976 1.00 26.19  ? 9    LYS B CB  1 
ATOM   1174  C  CG  . LYS B  1 9   ? 67.081  27.970  28.779 1.00 45.56  ? 9    LYS B CG  1 
ATOM   1175  C  CD  . LYS B  1 9   ? 66.636  29.430  28.824 1.00 57.17  ? 9    LYS B CD  1 
ATOM   1176  C  CE  . LYS B  1 9   ? 67.852  30.354  28.865 1.00 56.05  ? 9    LYS B CE  1 
ATOM   1177  N  NZ  . LYS B  1 9   ? 68.870  29.822  29.820 1.00 61.91  ? 9    LYS B NZ  1 
ATOM   1178  N  N   . GLY B  1 10  ? 64.945  24.393  30.403 1.00 25.61  ? 10   GLY B N   1 
ATOM   1179  C  CA  . GLY B  1 10  ? 63.811  23.571  30.830 1.00 30.02  ? 10   GLY B CA  1 
ATOM   1180  C  C   . GLY B  1 10  ? 63.497  23.836  32.294 1.00 31.43  ? 10   GLY B C   1 
ATOM   1181  O  O   . GLY B  1 10  ? 63.845  24.884  32.818 1.00 31.53  ? 10   GLY B O   1 
ATOM   1182  N  N   . ASP B  1 11  ? 62.827  22.902  32.949 1.00 41.31  ? 11   ASP B N   1 
ATOM   1183  C  CA  . ASP B  1 11  ? 62.383  23.171  34.315 1.00 47.62  ? 11   ASP B CA  1 
ATOM   1184  C  C   . ASP B  1 11  ? 63.464  22.827  35.322 1.00 46.92  ? 11   ASP B C   1 
ATOM   1185  O  O   . ASP B  1 11  ? 63.394  23.264  36.467 1.00 50.12  ? 11   ASP B O   1 
ATOM   1186  C  CB  . ASP B  1 11  ? 61.110  22.366  34.594 1.00 45.93  ? 11   ASP B CB  1 
ATOM   1187  C  CG  . ASP B  1 11  ? 59.947  22.953  33.809 1.00 54.53  ? 11   ASP B CG  1 
ATOM   1188  O  OD1 . ASP B  1 11  ? 59.091  22.180  33.336 1.00 71.73  ? 11   ASP B OD1 1 
ATOM   1189  O  OD2 . ASP B  1 11  ? 59.926  24.194  33.673 1.00 55.26  ? 11   ASP B OD2 1 
ATOM   1190  N  N   . GLY B  1 12  ? 64.445  22.054  34.884 1.00 35.74  ? 12   GLY B N   1 
ATOM   1191  C  CA  . GLY B  1 12  ? 65.517  21.603  35.765 1.00 34.38  ? 12   GLY B CA  1 
ATOM   1192  C  C   . GLY B  1 12  ? 66.810  22.297  35.382 1.00 23.67  ? 12   GLY B C   1 
ATOM   1193  O  O   . GLY B  1 12  ? 66.751  23.409  34.853 1.00 31.76  ? 12   GLY B O   1 
ATOM   1194  N  N   . PRO B  1 13  ? 67.942  21.653  35.629 1.00 30.02  ? 13   PRO B N   1 
ATOM   1195  C  CA  . PRO B  1 13  ? 69.252  22.258  35.391 1.00 32.21  ? 13   PRO B CA  1 
ATOM   1196  C  C   . PRO B  1 13  ? 69.772  22.124  33.967 1.00 25.62  ? 13   PRO B C   1 
ATOM   1197  O  O   . PRO B  1 13  ? 70.832  22.638  33.628 1.00 31.05  ? 13   PRO B O   1 
ATOM   1198  C  CB  . PRO B  1 13  ? 70.152  21.394  36.297 1.00 34.62  ? 13   PRO B CB  1 
ATOM   1199  C  CG  . PRO B  1 13  ? 69.539  20.029  36.150 1.00 27.31  ? 13   PRO B CG  1 
ATOM   1200  C  CD  . PRO B  1 13  ? 68.055  20.281  36.162 1.00 28.51  ? 13   PRO B CD  1 
ATOM   1201  N  N   . VAL B  1 14  ? 69.046  21.415  33.104 1.00 25.82  ? 14   VAL B N   1 
ATOM   1202  C  CA  . VAL B  1 14  ? 69.618  21.163  31.773 1.00 23.48  ? 14   VAL B CA  1 
ATOM   1203  C  C   . VAL B  1 14  ? 69.569  22.421  30.931 1.00 26.88  ? 14   VAL B C   1 
ATOM   1204  O  O   . VAL B  1 14  ? 68.499  23.013  30.789 1.00 27.22  ? 14   VAL B O   1 
ATOM   1205  C  CB  . VAL B  1 14  ? 68.880  20.011  31.078 1.00 24.08  ? 14   VAL B CB  1 
ATOM   1206  C  CG1 . VAL B  1 14  ? 69.412  19.842  29.656 1.00 21.54  ? 14   VAL B CG1 1 
ATOM   1207  C  CG2 . VAL B  1 14  ? 68.994  18.724  31.891 1.00 24.68  ? 14   VAL B CG2 1 
ATOM   1208  N  N   . GLN B  1 15  ? 70.711  22.838  30.378 1.00 23.83  ? 15   GLN B N   1 
ATOM   1209  C  CA  . GLN B  1 15  ? 70.683  24.035  29.548 1.00 26.66  ? 15   GLN B CA  1 
ATOM   1210  C  C   . GLN B  1 15  ? 71.851  24.039  28.580 1.00 24.02  ? 15   GLN B C   1 
ATOM   1211  O  O   . GLN B  1 15  ? 72.873  23.379  28.814 1.00 23.00  ? 15   GLN B O   1 
ATOM   1212  C  CB  . GLN B  1 15  ? 70.747  25.298  30.419 1.00 33.33  ? 15   GLN B CB  1 
ATOM   1213  C  CG  . GLN B  1 15  ? 71.982  25.269  31.314 1.00 33.53  ? 15   GLN B CG  1 
ATOM   1214  C  CD  . GLN B  1 15  ? 72.291  26.673  31.822 1.00 53.39  ? 15   GLN B CD  1 
ATOM   1215  O  OE1 . GLN B  1 15  ? 72.964  27.445  31.139 1.00 86.35  ? 15   GLN B OE1 1 
ATOM   1216  N  NE2 . GLN B  1 15  ? 71.773  26.958  33.007 1.00 40.59  ? 15   GLN B NE2 1 
ATOM   1217  N  N   . GLY B  1 16  ? 71.726  24.795  27.488 1.00 24.79  ? 16   GLY B N   1 
ATOM   1218  C  CA  . GLY B  1 16  ? 72.870  24.766  26.565 1.00 23.84  ? 16   GLY B CA  1 
ATOM   1219  C  C   . GLY B  1 16  ? 72.558  25.559  25.306 1.00 21.77  ? 16   GLY B C   1 
ATOM   1220  O  O   . GLY B  1 16  ? 71.459  26.095  25.180 1.00 22.83  ? 16   GLY B O   1 
ATOM   1221  N  N   . ILE B  1 17  ? 73.533  25.667  24.438 1.00 19.90  ? 17   ILE B N   1 
ATOM   1222  C  CA  . ILE B  1 17  ? 73.448  26.356  23.161 1.00 21.28  ? 17   ILE B CA  1 
ATOM   1223  C  C   . ILE B  1 17  ? 73.865  25.405  22.055 1.00 19.78  ? 17   ILE B C   1 
ATOM   1224  O  O   . ILE B  1 17  ? 74.935  24.817  22.083 1.00 19.25  ? 17   ILE B O   1 
ATOM   1225  C  CB  . ILE B  1 17  ? 74.326  27.615  23.168 1.00 22.46  ? 17   ILE B CB  1 
ATOM   1226  C  CG1 . ILE B  1 17  ? 73.842  28.645  24.205 1.00 23.53  ? 17   ILE B CG1 1 
ATOM   1227  C  CG2 . ILE B  1 17  ? 74.441  28.257  21.793 1.00 21.01  ? 17   ILE B CG2 1 
ATOM   1228  C  CD1 . ILE B  1 17  ? 74.848  29.774  24.371 1.00 24.05  ? 17   ILE B CD1 1 
ATOM   1229  N  N   . ILE B  1 18  ? 73.008  25.267  21.055 1.00 18.66  ? 18   ILE B N   1 
ATOM   1230  C  CA  . ILE B  1 18  ? 73.336  24.428  19.902 1.00 17.38  ? 18   ILE B CA  1 
ATOM   1231  C  C   . ILE B  1 18  ? 73.305  25.281  18.642 1.00 19.46  ? 18   ILE B C   1 
ATOM   1232  O  O   . ILE B  1 18  ? 72.347  26.021  18.402 1.00 20.31  ? 18   ILE B O   1 
ATOM   1233  C  CB  . ILE B  1 18  ? 72.352  23.252  19.814 1.00 19.79  ? 18   ILE B CB  1 
ATOM   1234  C  CG1 . ILE B  1 18  ? 72.416  22.350  21.054 1.00 19.90  ? 18   ILE B CG1 1 
ATOM   1235  C  CG2 . ILE B  1 18  ? 72.520  22.463  18.510 1.00 15.64  ? 18   ILE B CG2 1 
ATOM   1236  C  CD1 . ILE B  1 18  ? 73.729  21.586  21.245 1.00 18.90  ? 18   ILE B CD1 1 
ATOM   1237  N  N   . ASN B  1 19  ? 74.363  25.163  17.872 1.00 19.09  ? 19   ASN B N   1 
ATOM   1238  C  CA  . ASN B  1 19  ? 74.595  25.856  16.607 1.00 21.66  ? 19   ASN B CA  1 
ATOM   1239  C  C   . ASN B  1 19  ? 74.305  24.922  15.438 1.00 18.66  ? 19   ASN B C   1 
ATOM   1240  O  O   . ASN B  1 19  ? 74.545  23.718  15.536 1.00 19.99  ? 19   ASN B O   1 
ATOM   1241  C  CB  . ASN B  1 19  ? 76.054  26.314  16.506 1.00 24.07  ? 19   ASN B CB  1 
ATOM   1242  C  CG  . ASN B  1 19  ? 76.455  27.137  17.709 1.00 26.83  ? 19   ASN B CG  1 
ATOM   1243  O  OD1 . ASN B  1 19  ? 76.011  28.285  17.773 1.00 24.55  ? 19   ASN B OD1 1 
ATOM   1244  N  ND2 . ASN B  1 19  ? 77.239  26.608  18.647 1.00 24.01  ? 19   ASN B ND2 1 
ATOM   1245  N  N   . PHE B  1 20  ? 73.792  25.496  14.368 1.00 19.11  ? 20   PHE B N   1 
ATOM   1246  C  CA  . PHE B  1 20  ? 73.508  24.768  13.139 1.00 22.54  ? 20   PHE B CA  1 
ATOM   1247  C  C   . PHE B  1 20  ? 74.189  25.528  11.997 1.00 23.43  ? 20   PHE B C   1 
ATOM   1248  O  O   . PHE B  1 20  ? 74.076  26.762  11.920 1.00 20.68  ? 20   PHE B O   1 
ATOM   1249  C  CB  . PHE B  1 20  ? 72.019  24.676  12.822 1.00 20.59  ? 20   PHE B CB  1 
ATOM   1250  C  CG  . PHE B  1 20  ? 71.180  23.940  13.864 1.00 17.02  ? 20   PHE B CG  1 
ATOM   1251  C  CD1 . PHE B  1 20  ? 70.821  22.636  13.675 1.00 19.52  ? 20   PHE B CD1 1 
ATOM   1252  C  CD2 . PHE B  1 20  ? 70.781  24.626  15.020 1.00 21.94  ? 20   PHE B CD2 1 
ATOM   1253  C  CE1 . PHE B  1 20  ? 70.056  21.955  14.608 1.00 25.69  ? 20   PHE B CE1 1 
ATOM   1254  C  CE2 . PHE B  1 20  ? 69.997  23.953  15.964 1.00 18.15  ? 20   PHE B CE2 1 
ATOM   1255  C  CZ  . PHE B  1 20  ? 69.631  22.642  15.739 1.00 21.84  ? 20   PHE B CZ  1 
ATOM   1256  N  N   . GLU B  1 21  ? 74.890  24.791  11.141 1.00 20.56  ? 21   GLU B N   1 
ATOM   1257  C  CA  . GLU B  1 21  ? 75.555  25.469  10.021 1.00 21.11  ? 21   GLU B CA  1 
ATOM   1258  C  C   . GLU B  1 21  ? 75.293  24.666  8.759  1.00 22.54  ? 21   GLU B C   1 
ATOM   1259  O  O   . GLU B  1 21  ? 75.478  23.441  8.753  1.00 23.23  ? 21   GLU B O   1 
ATOM   1260  C  CB  . GLU B  1 21  ? 77.061  25.597  10.300 1.00 30.65  ? 21   GLU B CB  1 
ATOM   1261  C  CG  . GLU B  1 21  ? 77.461  25.723  11.761 1.00 52.61  ? 21   GLU B CG  1 
ATOM   1262  C  CD  . GLU B  1 21  ? 78.887  26.131  12.057 1.00 66.64  ? 21   GLU B CD  1 
ATOM   1263  O  OE1 . GLU B  1 21  ? 79.632  26.386  11.081 1.00 56.06  ? 21   GLU B OE1 1 
ATOM   1264  O  OE2 . GLU B  1 21  ? 79.259  26.191  13.259 1.00 45.88  ? 21   GLU B OE2 1 
ATOM   1265  N  N   . GLN B  1 22  ? 74.872  25.289  7.683  1.00 22.30  ? 22   GLN B N   1 
ATOM   1266  C  CA  . GLN B  1 22  ? 74.658  24.633  6.406  1.00 22.49  ? 22   GLN B CA  1 
ATOM   1267  C  C   . GLN B  1 22  ? 75.347  25.457  5.310  1.00 27.41  ? 22   GLN B C   1 
ATOM   1268  O  O   . GLN B  1 22  ? 74.805  26.497  4.921  1.00 28.20  ? 22   GLN B O   1 
ATOM   1269  C  CB  . GLN B  1 22  ? 73.166  24.466  6.146  1.00 21.69  ? 22   GLN B CB  1 
ATOM   1270  C  CG  . GLN B  1 22  ? 72.839  23.615  4.930  1.00 24.17  ? 22   GLN B CG  1 
ATOM   1271  C  CD  . GLN B  1 22  ? 71.357  23.358  4.773  1.00 32.07  ? 22   GLN B CD  1 
ATOM   1272  O  OE1 . GLN B  1 22  ? 70.539  24.220  5.097  1.00 30.86  ? 22   GLN B OE1 1 
ATOM   1273  N  NE2 . GLN B  1 22  ? 70.964  22.192  4.262  1.00 30.72  ? 22   GLN B NE2 1 
ATOM   1274  N  N   . LYS B  1 23  ? 76.522  24.986  4.892  1.00 36.99  ? 23   LYS B N   1 
ATOM   1275  C  CA  . LYS B  1 23  ? 77.334  25.727  3.924  1.00 48.71  ? 23   LYS B CA  1 
ATOM   1276  C  C   . LYS B  1 23  ? 76.657  25.786  2.554  1.00 50.01  ? 23   LYS B C   1 
ATOM   1277  O  O   . LYS B  1 23  ? 76.727  26.827  1.898  1.00 59.57  ? 23   LYS B O   1 
ATOM   1278  C  CB  . LYS B  1 23  ? 78.744  25.135  3.803  1.00 63.03  ? 23   LYS B CB  1 
ATOM   1279  C  CG  . LYS B  1 23  ? 78.804  23.790  3.100  1.00 77.25  ? 23   LYS B CG  1 
ATOM   1280  C  CD  . LYS B  1 23  ? 79.918  22.908  3.641  1.00 82.60  ? 23   LYS B CD  1 
ATOM   1281  C  CE  . LYS B  1 23  ? 79.479  21.452  3.786  1.00 75.77  ? 23   LYS B CE  1 
ATOM   1282  N  NZ  . LYS B  1 23  ? 78.778  20.954  2.570  1.00 48.18  ? 23   LYS B NZ  1 
ATOM   1283  N  N   . GLU B  1 24  ? 76.004  24.716  2.131  1.00 37.29  ? 24   GLU B N   1 
ATOM   1284  C  CA  . GLU B  1 24  ? 75.332  24.574  0.863  1.00 47.84  ? 24   GLU B CA  1 
ATOM   1285  C  C   . GLU B  1 24  ? 73.841  24.261  1.037  1.00 44.77  ? 24   GLU B C   1 
ATOM   1286  O  O   . GLU B  1 24  ? 73.568  23.365  1.830  1.00 47.41  ? 24   GLU B O   1 
ATOM   1287  C  CB  . GLU B  1 24  ? 75.890  23.415  0.008  1.00 61.27  ? 24   GLU B CB  1 
ATOM   1288  C  CG  . GLU B  1 24  ? 75.177  23.281  -1.326 1.00 81.13  ? 24   GLU B CG  1 
ATOM   1289  C  CD  . GLU B  1 24  ? 74.326  22.066  -1.592 1.00 89.10  ? 24   GLU B CD  1 
ATOM   1290  O  OE1 . GLU B  1 24  ? 73.282  21.869  -0.934 1.00 100.31 ? 24   GLU B OE1 1 
ATOM   1291  O  OE2 . GLU B  1 24  ? 74.653  21.256  -2.499 1.00 51.75  ? 24   GLU B OE2 1 
ATOM   1292  N  N   . SER B  1 25  ? 73.039  24.959  0.287  1.00 49.78  ? 25   SER B N   1 
ATOM   1293  C  CA  . SER B  1 25  ? 71.612  24.993  0.111  1.00 52.07  ? 25   SER B CA  1 
ATOM   1294  C  C   . SER B  1 25  ? 70.907  23.807  0.750  1.00 58.47  ? 25   SER B C   1 
ATOM   1295  O  O   . SER B  1 25  ? 70.117  23.929  1.687  1.00 91.56  ? 25   SER B O   1 
ATOM   1296  C  CB  . SER B  1 25  ? 71.266  25.022  -1.388 1.00 52.30  ? 25   SER B CB  1 
ATOM   1297  O  OG  . SER B  1 25  ? 69.862  24.960  -1.578 1.00 67.99  ? 25   SER B OG  1 
ATOM   1298  N  N   . ASN B  1 26  ? 71.207  22.644  0.197  1.00 49.48  ? 26   ASN B N   1 
ATOM   1299  C  CA  . ASN B  1 26  ? 70.640  21.412  0.711  1.00 52.95  ? 26   ASN B CA  1 
ATOM   1300  C  C   . ASN B  1 26  ? 71.770  20.435  1.001  1.00 52.88  ? 26   ASN B C   1 
ATOM   1301  O  O   . ASN B  1 26  ? 71.608  19.224  0.887  1.00 74.17  ? 26   ASN B O   1 
ATOM   1302  C  CB  . ASN B  1 26  ? 69.643  20.822  -0.282 1.00 74.49  ? 26   ASN B CB  1 
ATOM   1303  C  CG  . ASN B  1 26  ? 68.932  21.900  -1.078 1.00 85.05  ? 26   ASN B CG  1 
ATOM   1304  O  OD1 . ASN B  1 26  ? 67.750  22.158  -0.851 1.00 119.74 ? 26   ASN B OD1 1 
ATOM   1305  N  ND2 . ASN B  1 26  ? 69.659  22.508  -2.008 1.00 57.42  ? 26   ASN B ND2 1 
ATOM   1306  N  N   . GLY B  1 27  ? 72.907  21.003  1.380  1.00 44.54  ? 27   GLY B N   1 
ATOM   1307  C  CA  . GLY B  1 27  ? 74.042  20.253  1.877  1.00 47.54  ? 27   GLY B CA  1 
ATOM   1308  C  C   . GLY B  1 27  ? 73.783  19.702  3.275  1.00 32.86  ? 27   GLY B C   1 
ATOM   1309  O  O   . GLY B  1 27  ? 72.710  19.824  3.870  1.00 33.01  ? 27   GLY B O   1 
ATOM   1310  N  N   . PRO B  1 28  ? 74.789  19.072  3.851  1.00 33.15  ? 28   PRO B N   1 
ATOM   1311  C  CA  . PRO B  1 28  ? 74.589  18.553  5.209  1.00 27.91  ? 28   PRO B CA  1 
ATOM   1312  C  C   . PRO B  1 28  ? 74.528  19.747  6.179  1.00 29.18  ? 28   PRO B C   1 
ATOM   1313  O  O   . PRO B  1 28  ? 75.058  20.823  5.906  1.00 25.81  ? 28   PRO B O   1 
ATOM   1314  C  CB  . PRO B  1 28  ? 75.823  17.712  5.452  1.00 38.40  ? 28   PRO B CB  1 
ATOM   1315  C  CG  . PRO B  1 28  ? 76.586  17.652  4.170  1.00 46.20  ? 28   PRO B CG  1 
ATOM   1316  C  CD  . PRO B  1 28  ? 76.135  18.818  3.334  1.00 42.49  ? 28   PRO B CD  1 
ATOM   1317  N  N   . VAL B  1 29  ? 73.884  19.538  7.319  1.00 20.48  ? 29   VAL B N   1 
ATOM   1318  C  CA  . VAL B  1 29  ? 73.883  20.501  8.416  1.00 19.57  ? 29   VAL B CA  1 
ATOM   1319  C  C   . VAL B  1 29  ? 74.796  19.988  9.530  1.00 23.32  ? 29   VAL B C   1 
ATOM   1320  O  O   . VAL B  1 29  ? 74.638  18.854  9.971  1.00 22.59  ? 29   VAL B O   1 
ATOM   1321  C  CB  . VAL B  1 29  ? 72.468  20.733  8.966  1.00 20.63  ? 29   VAL B CB  1 
ATOM   1322  C  CG1 . VAL B  1 29  ? 72.481  21.777  10.078 1.00 19.40  ? 29   VAL B CG1 1 
ATOM   1323  C  CG2 . VAL B  1 29  ? 71.554  21.169  7.827  1.00 20.47  ? 29   VAL B CG2 1 
ATOM   1324  N  N   . LYS B  1 30  ? 75.755  20.793  9.945  1.00 20.74  ? 30   LYS B N   1 
ATOM   1325  C  CA  . LYS B  1 30  ? 76.620  20.568  11.096 1.00 20.72  ? 30   LYS B CA  1 
ATOM   1326  C  C   . LYS B  1 30  ? 75.888  21.067  12.339 1.00 24.36  ? 30   LYS B C   1 
ATOM   1327  O  O   . LYS B  1 30  ? 75.389  22.199  12.318 1.00 21.49  ? 30   LYS B O   1 
ATOM   1328  C  CB  . LYS B  1 30  ? 77.952  21.310  10.938 1.00 27.40  ? 30   LYS B CB  1 
ATOM   1329  C  CG  . LYS B  1 30  ? 78.842  20.703  9.853  1.00 51.22  ? 30   LYS B CG  1 
ATOM   1330  C  CD  . LYS B  1 30  ? 80.230  21.328  9.877  1.00 66.42  ? 30   LYS B CD  1 
ATOM   1331  C  CE  . LYS B  1 30  ? 80.898  21.280  8.512  1.00 74.38  ? 30   LYS B CE  1 
ATOM   1332  N  NZ  . LYS B  1 30  ? 82.191  22.034  8.496  1.00 91.26  ? 30   LYS B NZ  1 
ATOM   1333  N  N   . VAL B  1 31  ? 75.798  20.210  13.340 1.00 20.87  ? 31   VAL B N   1 
ATOM   1334  C  CA  . VAL B  1 31  ? 75.071  20.576  14.553 1.00 19.16  ? 31   VAL B CA  1 
ATOM   1335  C  C   . VAL B  1 31  ? 76.069  20.497  15.704 1.00 23.97  ? 31   VAL B C   1 
ATOM   1336  O  O   . VAL B  1 31  ? 76.607  19.412  15.942 1.00 23.05  ? 31   VAL B O   1 
ATOM   1337  C  CB  . VAL B  1 31  ? 73.889  19.631  14.790 1.00 17.08  ? 31   VAL B CB  1 
ATOM   1338  C  CG1 . VAL B  1 31  ? 73.108  20.013  16.054 1.00 21.24  ? 31   VAL B CG1 1 
ATOM   1339  C  CG2 . VAL B  1 31  ? 72.944  19.633  13.589 1.00 21.67  ? 31   VAL B CG2 1 
ATOM   1340  N  N   . TRP B  1 32  ? 76.333  21.572  16.432 1.00 20.16  ? 32   TRP B N   1 
ATOM   1341  C  CA  . TRP B  1 32  ? 77.309  21.404  17.504 1.00 18.99  ? 32   TRP B CA  1 
ATOM   1342  C  C   . TRP B  1 32  ? 77.078  22.402  18.615 1.00 23.62  ? 32   TRP B C   1 
ATOM   1343  O  O   . TRP B  1 32  ? 76.489  23.473  18.410 1.00 22.86  ? 32   TRP B O   1 
ATOM   1344  C  CB  . TRP B  1 32  ? 78.730  21.596  16.934 1.00 20.56  ? 32   TRP B CB  1 
ATOM   1345  C  CG  . TRP B  1 32  ? 79.042  23.018  16.567 1.00 22.99  ? 32   TRP B CG  1 
ATOM   1346  C  CD1 . TRP B  1 32  ? 78.767  23.673  15.388 1.00 29.15  ? 32   TRP B CD1 1 
ATOM   1347  C  CD2 . TRP B  1 32  ? 79.708  23.978  17.403 1.00 27.92  ? 32   TRP B CD2 1 
ATOM   1348  N  NE1 . TRP B  1 32  ? 79.220  24.983  15.445 1.00 36.32  ? 32   TRP B NE1 1 
ATOM   1349  C  CE2 . TRP B  1 32  ? 79.799  25.188  16.675 1.00 25.82  ? 32   TRP B CE2 1 
ATOM   1350  C  CE3 . TRP B  1 32  ? 80.227  23.930  18.694 1.00 39.06  ? 32   TRP B CE3 1 
ATOM   1351  C  CZ2 . TRP B  1 32  ? 80.393  26.306  17.221 1.00 30.60  ? 32   TRP B CZ2 1 
ATOM   1352  C  CZ3 . TRP B  1 32  ? 80.822  25.065  19.233 1.00 41.57  ? 32   TRP B CZ3 1 
ATOM   1353  C  CH2 . TRP B  1 32  ? 80.892  26.237  18.484 1.00 41.25  ? 32   TRP B CH2 1 
ATOM   1354  N  N   . GLY B  1 33  ? 77.573  22.064  19.808 1.00 18.55  ? 33   GLY B N   1 
ATOM   1355  C  CA  . GLY B  1 33  ? 77.395  23.056  20.892 1.00 20.45  ? 33   GLY B CA  1 
ATOM   1356  C  C   . GLY B  1 33  ? 77.565  22.290  22.187 1.00 23.25  ? 33   GLY B C   1 
ATOM   1357  O  O   . GLY B  1 33  ? 78.080  21.167  22.188 1.00 27.32  ? 33   GLY B O   1 
ATOM   1358  N  N   . SER B  1 34  ? 77.151  22.890  23.287 1.00 22.52  ? 34   SER B N   1 
ATOM   1359  C  CA  . SER B  1 34  ? 77.380  22.223  24.576 1.00 19.69  ? 34   SER B CA  1 
ATOM   1360  C  C   . SER B  1 34  ? 76.111  22.253  25.408 1.00 25.59  ? 34   SER B C   1 
ATOM   1361  O  O   . SER B  1 34  ? 75.451  23.294  25.516 1.00 27.73  ? 34   SER B O   1 
ATOM   1362  C  CB  . SER B  1 34  ? 78.531  22.933  25.291 1.00 26.86  ? 34   SER B CB  1 
ATOM   1363  O  OG  . SER B  1 34  ? 78.585  22.596  26.663 1.00 34.47  ? 34   SER B OG  1 
ATOM   1364  N  N   . ILE B  1 35  ? 75.771  21.112  25.982 1.00 19.19  ? 35   ILE B N   1 
ATOM   1365  C  CA  . ILE B  1 35  ? 74.629  21.072  26.874 1.00 15.76  ? 35   ILE B CA  1 
ATOM   1366  C  C   . ILE B  1 35  ? 75.151  20.600  28.233 1.00 19.28  ? 35   ILE B C   1 
ATOM   1367  O  O   . ILE B  1 35  ? 75.847  19.586  28.286 1.00 24.04  ? 35   ILE B O   1 
ATOM   1368  C  CB  . ILE B  1 35  ? 73.550  20.113  26.383 1.00 21.01  ? 35   ILE B CB  1 
ATOM   1369  C  CG1 . ILE B  1 35  ? 73.067  20.386  24.943 1.00 27.07  ? 35   ILE B CG1 1 
ATOM   1370  C  CG2 . ILE B  1 35  ? 72.332  20.087  27.301 1.00 21.68  ? 35   ILE B CG2 1 
ATOM   1371  C  CD1 . ILE B  1 35  ? 72.216  19.228  24.423 1.00 25.89  ? 35   ILE B CD1 1 
ATOM   1372  N  N   . LYS B  1 36  ? 74.756  21.301  29.290 1.00 22.91  ? 36   LYS B N   1 
ATOM   1373  C  CA  . LYS B  1 36  ? 75.155  20.846  30.624 1.00 22.45  ? 36   LYS B CA  1 
ATOM   1374  C  C   . LYS B  1 36  ? 73.966  20.484  31.502 1.00 21.80  ? 36   LYS B C   1 
ATOM   1375  O  O   . LYS B  1 36  ? 72.796  20.707  31.202 1.00 23.22  ? 36   LYS B O   1 
ATOM   1376  C  CB  . LYS B  1 36  ? 76.001  21.917  31.316 1.00 24.04  ? 36   LYS B CB  1 
ATOM   1377  C  CG  . LYS B  1 36  ? 75.328  23.252  31.524 1.00 30.81  ? 36   LYS B CG  1 
ATOM   1378  C  CD  . LYS B  1 36  ? 76.237  24.189  32.329 1.00 39.52  ? 36   LYS B CD  1 
ATOM   1379  C  CE  . LYS B  1 36  ? 75.389  25.223  33.065 1.00 45.58  ? 36   LYS B CE  1 
ATOM   1380  N  NZ  . LYS B  1 36  ? 76.190  26.387  33.537 1.00 43.20  ? 36   LYS B NZ  1 
ATOM   1381  N  N   . GLY B  1 37  ? 74.325  19.881  32.647 1.00 22.16  ? 37   GLY B N   1 
ATOM   1382  C  CA  . GLY B  1 37  ? 73.371  19.464  33.645 1.00 25.27  ? 37   GLY B CA  1 
ATOM   1383  C  C   . GLY B  1 37  ? 72.639  18.183  33.315 1.00 21.51  ? 37   GLY B C   1 
ATOM   1384  O  O   . GLY B  1 37  ? 71.582  17.888  33.889 1.00 26.44  ? 37   GLY B O   1 
ATOM   1385  N  N   . LEU B  1 38  ? 73.166  17.371  32.405 1.00 19.56  ? 38   LEU B N   1 
ATOM   1386  C  CA  . LEU B  1 38  ? 72.558  16.098  32.054 1.00 19.75  ? 38   LEU B CA  1 
ATOM   1387  C  C   . LEU B  1 38  ? 73.105  14.972  32.896 1.00 23.19  ? 38   LEU B C   1 
ATOM   1388  O  O   . LEU B  1 38  ? 74.244  15.114  33.339 1.00 26.00  ? 38   LEU B O   1 
ATOM   1389  C  CB  . LEU B  1 38  ? 72.876  15.748  30.584 1.00 27.84  ? 38   LEU B CB  1 
ATOM   1390  C  CG  . LEU B  1 38  ? 72.156  16.623  29.546 1.00 26.32  ? 38   LEU B CG  1 
ATOM   1391  C  CD1 . LEU B  1 38  ? 72.885  16.538  28.212 1.00 22.05  ? 38   LEU B CD1 1 
ATOM   1392  C  CD2 . LEU B  1 38  ? 70.703  16.201  29.421 1.00 20.76  ? 38   LEU B CD2 1 
ATOM   1393  N  N   . THR B  1 39  ? 72.370  13.890  33.072 1.00 22.24  ? 39   THR B N   1 
ATOM   1394  C  CA  . THR B  1 39  ? 72.941  12.681  33.643 1.00 23.69  ? 39   THR B CA  1 
ATOM   1395  C  C   . THR B  1 39  ? 73.965  12.093  32.669 1.00 29.03  ? 39   THR B C   1 
ATOM   1396  O  O   . THR B  1 39  ? 73.820  12.164  31.438 1.00 25.71  ? 39   THR B O   1 
ATOM   1397  C  CB  . THR B  1 39  ? 71.916  11.564  33.905 1.00 26.51  ? 39   THR B CB  1 
ATOM   1398  O  OG1 . THR B  1 39  ? 71.130  11.344  32.715 1.00 24.37  ? 39   THR B OG1 1 
ATOM   1399  C  CG2 . THR B  1 39  ? 70.937  11.913  35.007 1.00 27.88  ? 39   THR B CG2 1 
ATOM   1400  N  N   . GLU B  1 40  ? 75.000  11.457  33.184 1.00 23.80  ? 40   GLU B N   1 
ATOM   1401  C  CA  . GLU B  1 40  ? 75.977  10.809  32.293 1.00 25.67  ? 40   GLU B CA  1 
ATOM   1402  C  C   . GLU B  1 40  ? 75.333  9.810   31.347 1.00 26.84  ? 40   GLU B C   1 
ATOM   1403  O  O   . GLU B  1 40  ? 74.503  9.007   31.780 1.00 26.48  ? 40   GLU B O   1 
ATOM   1404  C  CB  . GLU B  1 40  ? 77.041  10.081  33.142 1.00 21.16  ? 40   GLU B CB  1 
ATOM   1405  C  CG  . GLU B  1 40  ? 78.187  9.520   32.300 1.00 26.51  ? 40   GLU B CG  1 
ATOM   1406  C  CD  . GLU B  1 40  ? 79.222  8.778   33.136 1.00 34.52  ? 40   GLU B CD  1 
ATOM   1407  O  OE1 . GLU B  1 40  ? 80.120  8.124   32.570 1.00 42.84  ? 40   GLU B OE1 1 
ATOM   1408  O  OE2 . GLU B  1 40  ? 79.134  8.842   34.379 1.00 43.10  ? 40   GLU B OE2 1 
ATOM   1409  N  N   . GLY B  1 41  ? 75.709  9.776   30.069 1.00 25.41  ? 41   GLY B N   1 
ATOM   1410  C  CA  . GLY B  1 41  ? 75.199  8.748   29.171 1.00 25.54  ? 41   GLY B CA  1 
ATOM   1411  C  C   . GLY B  1 41  ? 74.307  9.323   28.066 1.00 22.03  ? 41   GLY B C   1 
ATOM   1412  O  O   . GLY B  1 41  ? 74.379  10.520  27.825 1.00 20.77  ? 41   GLY B O   1 
ATOM   1413  N  N   . LEU B  1 42  ? 73.518  8.478   27.409 1.00 21.37  ? 42   LEU B N   1 
ATOM   1414  C  CA  . LEU B  1 42  ? 72.770  8.841   26.209 1.00 21.67  ? 42   LEU B CA  1 
ATOM   1415  C  C   . LEU B  1 42  ? 71.457  9.551   26.504 1.00 28.98  ? 42   LEU B C   1 
ATOM   1416  O  O   . LEU B  1 42  ? 70.746  9.197   27.448 1.00 25.32  ? 42   LEU B O   1 
ATOM   1417  C  CB  . LEU B  1 42  ? 72.436  7.574   25.421 1.00 20.94  ? 42   LEU B CB  1 
ATOM   1418  C  CG  . LEU B  1 42  ? 73.542  6.754   24.814 1.00 24.22  ? 42   LEU B CG  1 
ATOM   1419  C  CD1 . LEU B  1 42  ? 73.037  5.375   24.389 1.00 24.25  ? 42   LEU B CD1 1 
ATOM   1420  C  CD2 . LEU B  1 42  ? 74.118  7.498   23.606 1.00 26.87  ? 42   LEU B CD2 1 
ATOM   1421  N  N   . HIS B  1 43  ? 71.118  10.543  25.685 1.00 19.35  ? 43   HIS B N   1 
ATOM   1422  C  CA  . HIS B  1 43  ? 69.890  11.308  25.770 1.00 17.25  ? 43   HIS B CA  1 
ATOM   1423  C  C   . HIS B  1 43  ? 69.325  11.547  24.369 1.00 21.66  ? 43   HIS B C   1 
ATOM   1424  O  O   . HIS B  1 43  ? 70.048  12.059  23.506 1.00 18.32  ? 43   HIS B O   1 
ATOM   1425  C  CB  . HIS B  1 43  ? 70.150  12.682  26.413 1.00 18.92  ? 43   HIS B CB  1 
ATOM   1426  C  CG  . HIS B  1 43  ? 70.553  12.512  27.855 1.00 22.62  ? 43   HIS B CG  1 
ATOM   1427  N  ND1 . HIS B  1 43  ? 69.623  12.435  28.865 1.00 22.82  ? 43   HIS B ND1 1 
ATOM   1428  C  CD2 . HIS B  1 43  ? 71.778  12.375  28.433 1.00 25.91  ? 43   HIS B CD2 1 
ATOM   1429  C  CE1 . HIS B  1 43  ? 70.271  12.270  30.017 1.00 26.77  ? 43   HIS B CE1 1 
ATOM   1430  N  NE2 . HIS B  1 43  ? 71.575  12.231  29.793 1.00 24.35  ? 43   HIS B NE2 1 
ATOM   1431  N  N   . GLY B  1 44  ? 68.060  11.198  24.148 1.00 19.82  ? 44   GLY B N   1 
ATOM   1432  C  CA  . GLY B  1 44  ? 67.441  11.474  22.861 1.00 20.79  ? 44   GLY B CA  1 
ATOM   1433  C  C   . GLY B  1 44  ? 67.458  12.962  22.526 1.00 20.51  ? 44   GLY B C   1 
ATOM   1434  O  O   . GLY B  1 44  ? 67.397  13.872  23.362 1.00 18.93  ? 44   GLY B O   1 
ATOM   1435  N  N   . PHE B  1 45  ? 67.525  13.214  21.211 1.00 16.60  ? 45   PHE B N   1 
ATOM   1436  C  CA  . PHE B  1 45  ? 67.744  14.579  20.714 1.00 16.03  ? 45   PHE B CA  1 
ATOM   1437  C  C   . PHE B  1 45  ? 67.030  14.727  19.384 1.00 18.05  ? 45   PHE B C   1 
ATOM   1438  O  O   . PHE B  1 45  ? 67.424  14.059  18.425 1.00 19.55  ? 45   PHE B O   1 
ATOM   1439  C  CB  . PHE B  1 45  ? 69.242  14.708  20.522 1.00 17.50  ? 45   PHE B CB  1 
ATOM   1440  C  CG  . PHE B  1 45  ? 69.854  16.055  20.267 1.00 15.35  ? 45   PHE B CG  1 
ATOM   1441  C  CD1 . PHE B  1 45  ? 69.722  17.066  21.206 1.00 21.30  ? 45   PHE B CD1 1 
ATOM   1442  C  CD2 . PHE B  1 45  ? 70.579  16.302  19.114 1.00 21.39  ? 45   PHE B CD2 1 
ATOM   1443  C  CE1 . PHE B  1 45  ? 70.310  18.297  21.007 1.00 22.61  ? 45   PHE B CE1 1 
ATOM   1444  C  CE2 . PHE B  1 45  ? 71.165  17.548  18.894 1.00 18.94  ? 45   PHE B CE2 1 
ATOM   1445  C  CZ  . PHE B  1 45  ? 71.018  18.535  19.849 1.00 19.50  ? 45   PHE B CZ  1 
ATOM   1446  N  N   . HIS B  1 46  ? 65.976  15.517  19.292 1.00 17.78  ? 46   HIS B N   1 
ATOM   1447  C  CA  . HIS B  1 46  ? 65.163  15.584  18.083 1.00 18.83  ? 46   HIS B CA  1 
ATOM   1448  C  C   . HIS B  1 46  ? 64.676  17.006  17.825 1.00 19.11  ? 46   HIS B C   1 
ATOM   1449  O  O   . HIS B  1 46  ? 64.537  17.789  18.754 1.00 18.81  ? 46   HIS B O   1 
ATOM   1450  C  CB  . HIS B  1 46  ? 63.888  14.735  18.174 1.00 20.68  ? 46   HIS B CB  1 
ATOM   1451  C  CG  . HIS B  1 46  ? 64.045  13.461  18.953 1.00 22.46  ? 46   HIS B CG  1 
ATOM   1452  N  ND1 . HIS B  1 46  ? 63.547  13.268  20.222 1.00 20.28  ? 46   HIS B ND1 1 
ATOM   1453  C  CD2 . HIS B  1 46  ? 64.739  12.331  18.630 1.00 22.97  ? 46   HIS B CD2 1 
ATOM   1454  C  CE1 . HIS B  1 46  ? 63.876  12.050  20.623 1.00 21.54  ? 46   HIS B CE1 1 
ATOM   1455  N  NE2 . HIS B  1 46  ? 64.605  11.449  19.681 1.00 19.63  ? 46   HIS B NE2 1 
ATOM   1456  N  N   . VAL B  1 47  ? 64.364  17.288  16.561 1.00 15.37  ? 47   VAL B N   1 
ATOM   1457  C  CA  . VAL B  1 47  ? 63.592  18.476  16.229 1.00 16.82  ? 47   VAL B CA  1 
ATOM   1458  C  C   . VAL B  1 47  ? 62.096  18.126  16.284 1.00 24.88  ? 47   VAL B C   1 
ATOM   1459  O  O   . VAL B  1 47  ? 61.698  17.171  15.625 1.00 20.28  ? 47   VAL B O   1 
ATOM   1460  C  CB  . VAL B  1 47  ? 63.920  19.025  14.841 1.00 18.00  ? 47   VAL B CB  1 
ATOM   1461  C  CG1 . VAL B  1 47  ? 63.087  20.266  14.529 1.00 18.30  ? 47   VAL B CG1 1 
ATOM   1462  C  CG2 . VAL B  1 47  ? 65.410  19.369  14.764 1.00 20.95  ? 47   VAL B CG2 1 
ATOM   1463  N  N   . HIS B  1 48  ? 61.316  18.870  17.056 1.00 20.46  ? 48   HIS B N   1 
ATOM   1464  C  CA  . HIS B  1 48  ? 59.875  18.646  17.193 1.00 16.97  ? 48   HIS B CA  1 
ATOM   1465  C  C   . HIS B  1 48  ? 59.140  19.678  16.346 1.00 19.13  ? 48   HIS B C   1 
ATOM   1466  O  O   . HIS B  1 48  ? 59.736  20.691  15.977 1.00 20.59  ? 48   HIS B O   1 
ATOM   1467  C  CB  . HIS B  1 48  ? 59.410  18.757  18.649 1.00 18.66  ? 48   HIS B CB  1 
ATOM   1468  C  CG  . HIS B  1 48  ? 59.863  17.582  19.466 1.00 21.27  ? 48   HIS B CG  1 
ATOM   1469  N  ND1 . HIS B  1 48  ? 59.001  16.815  20.213 1.00 24.15  ? 48   HIS B ND1 1 
ATOM   1470  C  CD2 . HIS B  1 48  ? 61.104  17.041  19.638 1.00 20.11  ? 48   HIS B CD2 1 
ATOM   1471  C  CE1 . HIS B  1 48  ? 59.700  15.834  20.814 1.00 21.07  ? 48   HIS B CE1 1 
ATOM   1472  N  NE2 . HIS B  1 48  ? 60.966  15.978  20.479 1.00 20.04  ? 48   HIS B NE2 1 
ATOM   1473  N  N   . GLU B  1 49  ? 57.885  19.347  16.043 1.00 18.65  ? 49   GLU B N   1 
ATOM   1474  C  CA  . GLU B  1 49  ? 57.150  20.065  15.026 1.00 19.54  ? 49   GLU B CA  1 
ATOM   1475  C  C   . GLU B  1 49  ? 56.909  21.541  15.320 1.00 24.23  ? 49   GLU B C   1 
ATOM   1476  O  O   . GLU B  1 49  ? 57.062  22.301  14.359 1.00 23.84  ? 49   GLU B O   1 
ATOM   1477  C  CB  . GLU B  1 49  ? 55.789  19.367  14.812 1.00 20.71  ? 49   GLU B CB  1 
ATOM   1478  C  CG  . GLU B  1 49  ? 55.070  19.915  13.579 1.00 24.80  ? 49   GLU B CG  1 
ATOM   1479  C  CD  . GLU B  1 49  ? 53.839  19.102  13.218 1.00 33.66  ? 49   GLU B CD  1 
ATOM   1480  O  OE1 . GLU B  1 49  ? 53.203  19.432  12.190 1.00 34.12  ? 49   GLU B OE1 1 
ATOM   1481  O  OE2 . GLU B  1 49  ? 53.534  18.164  13.982 1.00 28.83  ? 49   GLU B OE2 1 
ATOM   1482  N  N   . PHE B  1 50  ? 56.521  21.970  16.522 1.00 18.71  ? 50   PHE B N   1 
ATOM   1483  C  CA  . PHE B  1 50  ? 56.127  23.371  16.729 1.00 19.53  ? 50   PHE B CA  1 
ATOM   1484  C  C   . PHE B  1 50  ? 57.117  24.157  17.567 1.00 22.81  ? 50   PHE B C   1 
ATOM   1485  O  O   . PHE B  1 50  ? 57.692  23.632  18.540 1.00 22.42  ? 50   PHE B O   1 
ATOM   1486  C  CB  . PHE B  1 50  ? 54.741  23.398  17.413 1.00 20.36  ? 50   PHE B CB  1 
ATOM   1487  C  CG  . PHE B  1 50  ? 53.701  22.528  16.702 1.00 18.56  ? 50   PHE B CG  1 
ATOM   1488  C  CD1 . PHE B  1 50  ? 53.351  22.829  15.400 1.00 24.50  ? 50   PHE B CD1 1 
ATOM   1489  C  CD2 . PHE B  1 50  ? 53.125  21.453  17.340 1.00 23.36  ? 50   PHE B CD2 1 
ATOM   1490  C  CE1 . PHE B  1 50  ? 52.413  22.059  14.720 1.00 29.18  ? 50   PHE B CE1 1 
ATOM   1491  C  CE2 . PHE B  1 50  ? 52.187  20.675  16.667 1.00 37.04  ? 50   PHE B CE2 1 
ATOM   1492  C  CZ  . PHE B  1 50  ? 51.846  20.973  15.354 1.00 29.84  ? 50   PHE B CZ  1 
ATOM   1493  N  N   . GLY B  1 51  ? 57.351  25.396  17.203 1.00 19.57  ? 51   GLY B N   1 
ATOM   1494  C  CA  . GLY B  1 51  ? 58.211  26.335  17.896 1.00 20.39  ? 51   GLY B CA  1 
ATOM   1495  C  C   . GLY B  1 51  ? 57.369  27.019  18.978 1.00 23.53  ? 51   GLY B C   1 
ATOM   1496  O  O   . GLY B  1 51  ? 57.414  28.243  19.072 1.00 21.58  ? 51   GLY B O   1 
ATOM   1497  N  N   . ASP B  1 52  ? 56.630  26.200  19.710 1.00 25.62  ? 52   ASP B N   1 
ATOM   1498  C  CA  . ASP B  1 52  ? 55.642  26.713  20.679 1.00 21.27  ? 52   ASP B CA  1 
ATOM   1499  C  C   . ASP B  1 52  ? 56.030  26.314  22.094 1.00 24.16  ? 52   ASP B C   1 
ATOM   1500  O  O   . ASP B  1 52  ? 55.946  25.131  22.425 1.00 24.31  ? 52   ASP B O   1 
ATOM   1501  C  CB  . ASP B  1 52  ? 54.266  26.159  20.298 1.00 20.78  ? 52   ASP B CB  1 
ATOM   1502  C  CG  . ASP B  1 52  ? 53.132  26.686  21.148 1.00 25.66  ? 52   ASP B CG  1 
ATOM   1503  O  OD1 . ASP B  1 52  ? 51.978  26.582  20.660 1.00 26.45  ? 52   ASP B OD1 1 
ATOM   1504  O  OD2 . ASP B  1 52  ? 53.352  27.160  22.286 1.00 24.83  ? 52   ASP B OD2 1 
ATOM   1505  N  N   . ASN B  1 53  ? 56.452  27.304  22.868 1.00 23.52  ? 53   ASN B N   1 
ATOM   1506  C  CA  . ASN B  1 53  ? 56.886  27.084  24.239 1.00 24.81  ? 53   ASN B CA  1 
ATOM   1507  C  C   . ASN B  1 53  ? 55.857  27.602  25.240 1.00 30.36  ? 53   ASN B C   1 
ATOM   1508  O  O   . ASN B  1 53  ? 56.187  27.775  26.416 1.00 26.70  ? 53   ASN B O   1 
ATOM   1509  C  CB  . ASN B  1 53  ? 58.244  27.762  24.437 1.00 26.11  ? 53   ASN B CB  1 
ATOM   1510  C  CG  . ASN B  1 53  ? 58.890  27.443  25.777 1.00 34.96  ? 53   ASN B CG  1 
ATOM   1511  O  OD1 . ASN B  1 53  ? 59.243  28.347  26.543 1.00 38.88  ? 53   ASN B OD1 1 
ATOM   1512  N  ND2 . ASN B  1 53  ? 59.056  26.159  26.059 1.00 32.85  ? 53   ASN B ND2 1 
ATOM   1513  N  N   . THR B  1 54  ? 54.626  27.833  24.781 1.00 26.01  ? 54   THR B N   1 
ATOM   1514  C  CA  . THR B  1 54  ? 53.623  28.400  25.688 1.00 30.44  ? 54   THR B CA  1 
ATOM   1515  C  C   . THR B  1 54  ? 53.365  27.465  26.861 1.00 31.28  ? 54   THR B C   1 
ATOM   1516  O  O   . THR B  1 54  ? 52.969  27.947  27.926 1.00 35.84  ? 54   THR B O   1 
ATOM   1517  C  CB  . THR B  1 54  ? 52.253  28.693  25.034 1.00 32.62  ? 54   THR B CB  1 
ATOM   1518  O  OG1 . THR B  1 54  ? 51.752  27.512  24.402 1.00 29.02  ? 54   THR B OG1 1 
ATOM   1519  C  CG2 . THR B  1 54  ? 52.355  29.716  23.913 1.00 25.95  ? 54   THR B CG2 1 
ATOM   1520  N  N   . ALA B  1 55  ? 53.540  26.156  26.714 1.00 25.12  ? 55   ALA B N   1 
ATOM   1521  C  CA  . ALA B  1 55  ? 53.400  25.253  27.853 1.00 28.88  ? 55   ALA B CA  1 
ATOM   1522  C  C   . ALA B  1 55  ? 54.697  24.481  28.083 1.00 34.19  ? 55   ALA B C   1 
ATOM   1523  O  O   . ALA B  1 55  ? 54.637  23.260  28.253 1.00 34.67  ? 55   ALA B O   1 
ATOM   1524  C  CB  . ALA B  1 55  ? 52.261  24.266  27.645 1.00 32.66  ? 55   ALA B CB  1 
ATOM   1525  N  N   . GLY B  1 56  ? 55.817  25.185  28.054 1.00 29.89  ? 56   GLY B N   1 
ATOM   1526  C  CA  . GLY B  1 56  ? 57.116  24.543  28.161 1.00 30.67  ? 56   GLY B CA  1 
ATOM   1527  C  C   . GLY B  1 56  ? 57.318  23.554  27.026 1.00 30.99  ? 56   GLY B C   1 
ATOM   1528  O  O   . GLY B  1 56  ? 56.780  23.770  25.933 1.00 28.70  ? 56   GLY B O   1 
ATOM   1529  N  N   . CYS B  1 57  ? 58.072  22.468  27.253 1.00 29.05  ? 57   CYS B N   1 
ATOM   1530  C  CA  . CYS B  1 57  ? 58.443  21.673  26.079 1.00 27.95  ? 57   CYS B CA  1 
ATOM   1531  C  C   . CYS B  1 57  ? 57.298  20.792  25.598 1.00 26.58  ? 57   CYS B C   1 
ATOM   1532  O  O   . CYS B  1 57  ? 57.347  20.231  24.499 1.00 26.87  ? 57   CYS B O   1 
ATOM   1533  C  CB  A CYS B  1 57  ? 59.653  20.802  26.412 0.43 28.94  ? 57   CYS B CB  1 
ATOM   1534  C  CB  B CYS B  1 57  ? 59.690  20.835  26.325 0.57 30.16  ? 57   CYS B CB  1 
ATOM   1535  S  SG  A CYS B  1 57  ? 61.119  21.713  26.951 0.43 35.33  ? 57   CYS B SG  1 
ATOM   1536  S  SG  B CYS B  1 57  ? 61.059  21.655  27.153 0.57 33.29  ? 57   CYS B SG  1 
ATOM   1537  N  N   . THR B  1 58  ? 56.250  20.658  26.391 1.00 23.63  ? 58   THR B N   1 
ATOM   1538  C  CA  . THR B  1 58  ? 55.118  19.844  25.936 1.00 24.50  ? 58   THR B CA  1 
ATOM   1539  C  C   . THR B  1 58  ? 54.421  20.412  24.713 1.00 25.40  ? 58   THR B C   1 
ATOM   1540  O  O   . THR B  1 58  ? 53.920  19.678  23.855 1.00 28.09  ? 58   THR B O   1 
ATOM   1541  C  CB  . THR B  1 58  ? 54.096  19.722  27.088 1.00 31.39  ? 58   THR B CB  1 
ATOM   1542  O  OG1 . THR B  1 58  ? 54.834  19.338  28.259 1.00 37.71  ? 58   THR B OG1 1 
ATOM   1543  C  CG2 . THR B  1 58  ? 53.077  18.631  26.805 1.00 35.54  ? 58   THR B CG2 1 
ATOM   1544  N  N   . SER B  1 59  ? 54.355  21.744  24.586 1.00 23.58  ? 59   SER B N   1 
ATOM   1545  C  CA  . SER B  1 59  ? 53.618  22.280  23.441 1.00 24.34  ? 59   SER B CA  1 
ATOM   1546  C  C   . SER B  1 59  ? 54.441  22.211  22.159 1.00 26.61  ? 59   SER B C   1 
ATOM   1547  O  O   . SER B  1 59  ? 53.933  22.614  21.104 1.00 24.24  ? 59   SER B O   1 
ATOM   1548  C  CB  . SER B  1 59  ? 53.166  23.711  23.726 1.00 30.68  ? 59   SER B CB  1 
ATOM   1549  O  OG  . SER B  1 59  ? 54.110  24.492  24.407 1.00 32.24  ? 59   SER B OG  1 
ATOM   1550  N  N   . ALA B  1 60  ? 55.682  21.694  22.219 1.00 21.70  ? 60   ALA B N   1 
ATOM   1551  C  CA  . ALA B  1 60  ? 56.447  21.541  20.974 1.00 25.04  ? 60   ALA B CA  1 
ATOM   1552  C  C   . ALA B  1 60  ? 55.855  20.486  20.055 1.00 23.86  ? 60   ALA B C   1 
ATOM   1553  O  O   . ALA B  1 60  ? 56.239  20.365  18.896 1.00 22.87  ? 60   ALA B O   1 
ATOM   1554  C  CB  . ALA B  1 60  ? 57.903  21.169  21.260 1.00 24.06  ? 60   ALA B CB  1 
ATOM   1555  N  N   . GLY B  1 61  ? 54.932  19.664  20.523 1.00 21.55  ? 61   GLY B N   1 
ATOM   1556  C  CA  . GLY B  1 61  ? 54.351  18.656  19.647 1.00 22.22  ? 61   GLY B CA  1 
ATOM   1557  C  C   . GLY B  1 61  ? 55.261  17.456  19.456 1.00 20.76  ? 61   GLY B C   1 
ATOM   1558  O  O   . GLY B  1 61  ? 56.213  17.278  20.222 1.00 23.94  ? 61   GLY B O   1 
ATOM   1559  N  N   . PRO B  1 62  ? 54.954  16.620  18.475 1.00 24.63  ? 62   PRO B N   1 
ATOM   1560  C  CA  . PRO B  1 62  ? 55.713  15.403  18.205 1.00 22.36  ? 62   PRO B CA  1 
ATOM   1561  C  C   . PRO B  1 62  ? 56.964  15.678  17.377 1.00 21.06  ? 62   PRO B C   1 
ATOM   1562  O  O   . PRO B  1 62  ? 57.217  16.841  17.070 1.00 21.53  ? 62   PRO B O   1 
ATOM   1563  C  CB  . PRO B  1 62  ? 54.719  14.565  17.387 1.00 23.62  ? 62   PRO B CB  1 
ATOM   1564  C  CG  . PRO B  1 62  ? 53.941  15.596  16.628 1.00 22.19  ? 62   PRO B CG  1 
ATOM   1565  C  CD  . PRO B  1 62  ? 53.782  16.764  17.563 1.00 26.50  ? 62   PRO B CD  1 
ATOM   1566  N  N   . HIS B  1 63  ? 57.704  14.622  17.060 1.00 21.71  ? 63   HIS B N   1 
ATOM   1567  C  CA  . HIS B  1 63  ? 58.899  14.821  16.220 1.00 19.99  ? 63   HIS B CA  1 
ATOM   1568  C  C   . HIS B  1 63  ? 58.474  15.418  14.877 1.00 21.26  ? 63   HIS B C   1 
ATOM   1569  O  O   . HIS B  1 63  ? 57.402  15.043  14.360 1.00 23.28  ? 63   HIS B O   1 
ATOM   1570  C  CB  . HIS B  1 63  ? 59.671  13.514  16.021 1.00 18.78  ? 63   HIS B CB  1 
ATOM   1571  C  CG  . HIS B  1 63  ? 60.119  12.840  17.279 1.00 17.82  ? 63   HIS B CG  1 
ATOM   1572  N  ND1 . HIS B  1 63  ? 60.785  11.645  17.346 1.00 19.24  ? 63   HIS B ND1 1 
ATOM   1573  C  CD2 . HIS B  1 63  ? 60.005  13.271  18.573 1.00 25.46  ? 63   HIS B CD2 1 
ATOM   1574  C  CE1 . HIS B  1 63  ? 61.046  11.348  18.611 1.00 21.84  ? 63   HIS B CE1 1 
ATOM   1575  N  NE2 . HIS B  1 63  ? 60.584  12.316  19.376 1.00 21.66  ? 63   HIS B NE2 1 
ATOM   1576  N  N   . PHE B  1 64  ? 59.286  16.323  14.354 1.00 21.95  ? 64   PHE B N   1 
ATOM   1577  C  CA  . PHE B  1 64  ? 59.051  16.918  13.029 1.00 19.44  ? 64   PHE B CA  1 
ATOM   1578  C  C   . PHE B  1 64  ? 59.032  15.804  11.994 1.00 22.46  ? 64   PHE B C   1 
ATOM   1579  O  O   . PHE B  1 64  ? 59.999  15.055  11.836 1.00 21.27  ? 64   PHE B O   1 
ATOM   1580  C  CB  . PHE B  1 64  ? 60.088  17.981  12.717 1.00 22.07  ? 64   PHE B CB  1 
ATOM   1581  C  CG  . PHE B  1 64  ? 59.969  18.672  11.365 1.00 21.13  ? 64   PHE B CG  1 
ATOM   1582  C  CD1 . PHE B  1 64  ? 61.081  18.937  10.599 1.00 25.81  ? 64   PHE B CD1 1 
ATOM   1583  C  CD2 . PHE B  1 64  ? 58.703  19.053  10.912 1.00 23.64  ? 64   PHE B CD2 1 
ATOM   1584  C  CE1 . PHE B  1 64  ? 61.003  19.553  9.360  1.00 24.35  ? 64   PHE B CE1 1 
ATOM   1585  C  CE2 . PHE B  1 64  ? 58.609  19.664  9.662  1.00 20.72  ? 64   PHE B CE2 1 
ATOM   1586  C  CZ  . PHE B  1 64  ? 59.736  19.921  8.923  1.00 24.21  ? 64   PHE B CZ  1 
ATOM   1587  N  N   . ASN B  1 65  ? 57.915  15.663  11.277 1.00 22.89  ? 65   ASN B N   1 
ATOM   1588  C  CA  . ASN B  1 65  ? 57.751  14.466  10.444 1.00 22.24  ? 65   ASN B CA  1 
ATOM   1589  C  C   . ASN B  1 65  ? 56.969  14.769  9.166  1.00 28.47  ? 65   ASN B C   1 
ATOM   1590  O  O   . ASN B  1 65  ? 55.886  14.210  8.982  1.00 30.67  ? 65   ASN B O   1 
ATOM   1591  C  CB  . ASN B  1 65  ? 57.021  13.411  11.257 1.00 20.19  ? 65   ASN B CB  1 
ATOM   1592  C  CG  . ASN B  1 65  ? 56.876  12.068  10.576 1.00 24.67  ? 65   ASN B CG  1 
ATOM   1593  O  OD1 . ASN B  1 65  ? 57.576  11.659  9.640  1.00 21.85  ? 65   ASN B OD1 1 
ATOM   1594  N  ND2 . ASN B  1 65  ? 55.947  11.271  11.119 1.00 26.23  ? 65   ASN B ND2 1 
ATOM   1595  N  N   . PRO B  1 66  ? 57.459  15.635  8.311  1.00 25.02  ? 66   PRO B N   1 
ATOM   1596  C  CA  . PRO B  1 66  ? 56.620  16.038  7.167  1.00 30.21  ? 66   PRO B CA  1 
ATOM   1597  C  C   . PRO B  1 66  ? 56.366  14.869  6.233  1.00 32.32  ? 66   PRO B C   1 
ATOM   1598  O  O   . PRO B  1 66  ? 55.364  14.892  5.504  1.00 33.18  ? 66   PRO B O   1 
ATOM   1599  C  CB  . PRO B  1 66  ? 57.469  17.119  6.480  1.00 33.48  ? 66   PRO B CB  1 
ATOM   1600  C  CG  . PRO B  1 66  ? 58.878  16.748  6.850  1.00 29.48  ? 66   PRO B CG  1 
ATOM   1601  C  CD  . PRO B  1 66  ? 58.767  16.318  8.294  1.00 20.95  ? 66   PRO B CD  1 
ATOM   1602  N  N   . LEU B  1 67  ? 57.224  13.852  6.219  1.00 28.38  ? 67   LEU B N   1 
ATOM   1603  C  CA  . LEU B  1 67  ? 56.993  12.748  5.286  1.00 30.21  ? 67   LEU B CA  1 
ATOM   1604  C  C   . LEU B  1 67  ? 56.182  11.616  5.903  1.00 32.49  ? 67   LEU B C   1 
ATOM   1605  O  O   . LEU B  1 67  ? 56.088  10.536  5.301  1.00 31.97  ? 67   LEU B O   1 
ATOM   1606  C  CB  . LEU B  1 67  ? 58.319  12.187  4.777  1.00 33.67  ? 67   LEU B CB  1 
ATOM   1607  C  CG  . LEU B  1 67  ? 59.206  13.131  3.973  1.00 38.37  ? 67   LEU B CG  1 
ATOM   1608  C  CD1 . LEU B  1 67  ? 60.387  12.400  3.359  1.00 33.93  ? 67   LEU B CD1 1 
ATOM   1609  C  CD2 . LEU B  1 67  ? 58.412  13.810  2.868  1.00 48.03  ? 67   LEU B CD2 1 
ATOM   1610  N  N   . SER B  1 68  ? 55.610  11.826  7.077  1.00 25.65  ? 68   SER B N   1 
ATOM   1611  C  CA  . SER B  1 68  ? 54.784  10.831  7.740  1.00 30.39  ? 68   SER B CA  1 
ATOM   1612  C  C   . SER B  1 68  ? 55.397  9.441   7.799  1.00 33.32  ? 68   SER B C   1 
ATOM   1613  O  O   . SER B  1 68  ? 54.784  8.420   7.474  1.00 34.18  ? 68   SER B O   1 
ATOM   1614  C  CB  . SER B  1 68  ? 53.409  10.708  7.040  1.00 39.88  ? 68   SER B CB  1 
ATOM   1615  O  OG  . SER B  1 68  ? 52.793  11.983  6.927  1.00 38.42  ? 68   SER B OG  1 
ATOM   1616  N  N   . ARG B  1 69  ? 56.641  9.355   8.251  1.00 25.69  ? 69   ARG B N   1 
ATOM   1617  C  CA  . ARG B  1 69  ? 57.278  8.066   8.482  1.00 22.10  ? 69   ARG B CA  1 
ATOM   1618  C  C   . ARG B  1 69  ? 57.305  7.683   9.950  1.00 25.13  ? 69   ARG B C   1 
ATOM   1619  O  O   . ARG B  1 69  ? 56.897  8.443   10.834 1.00 26.30  ? 69   ARG B O   1 
ATOM   1620  C  CB  . ARG B  1 69  ? 58.698  8.191   7.905  1.00 25.42  ? 69   ARG B CB  1 
ATOM   1621  C  CG  . ARG B  1 69  ? 58.628  8.328   6.386  1.00 35.56  ? 69   ARG B CG  1 
ATOM   1622  C  CD  . ARG B  1 69  ? 60.005  8.260   5.757  1.00 51.49  ? 69   ARG B CD  1 
ATOM   1623  N  NE  . ARG B  1 69  ? 59.932  8.550   4.325  1.00 56.69  ? 69   ARG B NE  1 
ATOM   1624  C  CZ  . ARG B  1 69  ? 60.988  8.596   3.525  1.00 53.32  ? 69   ARG B CZ  1 
ATOM   1625  N  NH1 . ARG B  1 69  ? 62.197  8.370   4.023  1.00 55.12  ? 69   ARG B NH1 1 
ATOM   1626  N  NH2 . ARG B  1 69  ? 60.815  8.870   2.238  1.00 51.83  ? 69   ARG B NH2 1 
ATOM   1627  N  N   . LYS B  1 70  ? 57.791  6.477   10.230 1.00 28.74  ? 70   LYS B N   1 
ATOM   1628  C  CA  . LYS B  1 70  ? 57.984  6.019   11.600 1.00 30.64  ? 70   LYS B CA  1 
ATOM   1629  C  C   . LYS B  1 70  ? 59.322  6.541   12.143 1.00 21.10  ? 70   LYS B C   1 
ATOM   1630  O  O   . LYS B  1 70  ? 60.216  6.871   11.375 1.00 22.88  ? 70   LYS B O   1 
ATOM   1631  C  CB  . LYS B  1 70  ? 57.984  4.495   11.716 1.00 41.98  ? 70   LYS B CB  1 
ATOM   1632  C  CG  . LYS B  1 70  ? 56.687  3.847   11.230 1.00 61.64  ? 70   LYS B CG  1 
ATOM   1633  C  CD  . LYS B  1 70  ? 56.957  2.835   10.130 1.00 85.02  ? 70   LYS B CD  1 
ATOM   1634  C  CE  . LYS B  1 70  ? 56.422  1.449   10.476 1.00 99.61  ? 70   LYS B CE  1 
ATOM   1635  N  NZ  . LYS B  1 70  ? 56.192  0.617   9.261  1.00 120.25 ? 70   LYS B NZ  1 
ATOM   1636  N  N   . HIS B  1 71  ? 59.398  6.559   13.464 1.00 20.30  ? 71   HIS B N   1 
ATOM   1637  C  CA  . HIS B  1 71  ? 60.626  6.941   14.151 1.00 21.07  ? 71   HIS B CA  1 
ATOM   1638  C  C   . HIS B  1 71  ? 61.767  6.011   13.839 1.00 22.30  ? 71   HIS B C   1 
ATOM   1639  O  O   . HIS B  1 71  ? 61.550  4.785   13.734 1.00 22.31  ? 71   HIS B O   1 
ATOM   1640  C  CB  . HIS B  1 71  ? 60.354  6.932   15.674 1.00 18.31  ? 71   HIS B CB  1 
ATOM   1641  C  CG  . HIS B  1 71  ? 61.568  7.414   16.433 1.00 22.23  ? 71   HIS B CG  1 
ATOM   1642  N  ND1 . HIS B  1 71  ? 61.939  8.749   16.453 1.00 18.48  ? 71   HIS B ND1 1 
ATOM   1643  C  CD2 . HIS B  1 71  ? 62.478  6.746   17.175 1.00 23.20  ? 71   HIS B CD2 1 
ATOM   1644  C  CE1 . HIS B  1 71  ? 63.041  8.884   17.190 1.00 19.53  ? 71   HIS B CE1 1 
ATOM   1645  N  NE2 . HIS B  1 71  ? 63.386  7.686   17.630 1.00 18.81  ? 71   HIS B NE2 1 
ATOM   1646  N  N   . GLY B  1 72  ? 62.966  6.582   13.740 1.00 19.67  ? 72   GLY B N   1 
ATOM   1647  C  CA  . GLY B  1 72  ? 64.185  5.823   13.532 1.00 18.18  ? 72   GLY B CA  1 
ATOM   1648  C  C   . GLY B  1 72  ? 65.408  6.575   14.057 1.00 20.58  ? 72   GLY B C   1 
ATOM   1649  O  O   . GLY B  1 72  ? 65.347  7.611   14.709 1.00 18.55  ? 72   GLY B O   1 
ATOM   1650  N  N   . GLY B  1 73  ? 66.571  6.006   13.751 1.00 21.36  ? 73   GLY B N   1 
ATOM   1651  C  CA  . GLY B  1 73  ? 67.838  6.672   14.044 1.00 22.66  ? 73   GLY B CA  1 
ATOM   1652  C  C   . GLY B  1 73  ? 68.184  7.525   12.832 1.00 24.21  ? 73   GLY B C   1 
ATOM   1653  O  O   . GLY B  1 73  ? 67.618  7.306   11.761 1.00 24.53  ? 73   GLY B O   1 
ATOM   1654  N  N   . PRO B  1 74  ? 69.075  8.482   13.006 1.00 21.66  ? 74   PRO B N   1 
ATOM   1655  C  CA  . PRO B  1 74  ? 69.430  9.384   11.907 1.00 17.73  ? 74   PRO B CA  1 
ATOM   1656  C  C   . PRO B  1 74  ? 70.064  8.619   10.745 1.00 21.91  ? 74   PRO B C   1 
ATOM   1657  O  O   . PRO B  1 74  ? 69.978  9.129   9.617  1.00 23.76  ? 74   PRO B O   1 
ATOM   1658  C  CB  . PRO B  1 74  ? 70.427  10.371  12.523 1.00 20.24  ? 74   PRO B CB  1 
ATOM   1659  C  CG  . PRO B  1 74  ? 70.931  9.689   13.760 1.00 22.40  ? 74   PRO B CG  1 
ATOM   1660  C  CD  . PRO B  1 74  ? 69.819  8.785   14.238 1.00 20.82  ? 74   PRO B CD  1 
ATOM   1661  N  N   . LYS B  1 75  ? 70.682  7.456   10.974 1.00 18.68  ? 75   LYS B N   1 
ATOM   1662  C  CA  . LYS B  1 75  ? 71.290  6.770   9.828  1.00 27.79  ? 75   LYS B CA  1 
ATOM   1663  C  C   . LYS B  1 75  ? 70.264  6.016   8.978  1.00 26.57  ? 75   LYS B C   1 
ATOM   1664  O  O   . LYS B  1 75  ? 70.579  5.511   7.897  1.00 29.30  ? 75   LYS B O   1 
ATOM   1665  C  CB  . LYS B  1 75  ? 72.385  5.784   10.293 1.00 27.45  ? 75   LYS B CB  1 
ATOM   1666  C  CG  . LYS B  1 75  ? 73.515  6.488   11.060 1.00 25.37  ? 75   LYS B CG  1 
ATOM   1667  C  CD  . LYS B  1 75  ? 74.320  5.483   11.869 1.00 33.76  ? 75   LYS B CD  1 
ATOM   1668  C  CE  . LYS B  1 75  ? 75.235  4.644   10.989 1.00 46.14  ? 75   LYS B CE  1 
ATOM   1669  N  NZ  . LYS B  1 75  ? 76.110  3.745   11.814 1.00 39.56  ? 75   LYS B NZ  1 
ATOM   1670  N  N   . ASP B  1 76  ? 69.041  5.888   9.449  1.00 21.59  ? 76   ASP B N   1 
ATOM   1671  C  CA  . ASP B  1 76  ? 68.004  5.111   8.784  1.00 24.34  ? 76   ASP B CA  1 
ATOM   1672  C  C   . ASP B  1 76  ? 67.320  5.884   7.662  1.00 25.03  ? 76   ASP B C   1 
ATOM   1673  O  O   . ASP B  1 76  ? 67.165  7.094   7.724  1.00 24.42  ? 76   ASP B O   1 
ATOM   1674  C  CB  . ASP B  1 76  ? 66.933  4.669   9.787  1.00 21.86  ? 76   ASP B CB  1 
ATOM   1675  C  CG  . ASP B  1 76  ? 67.447  3.731   10.854 1.00 27.50  ? 76   ASP B CG  1 
ATOM   1676  O  OD1 . ASP B  1 76  ? 66.923  3.807   11.979 1.00 29.75  ? 76   ASP B OD1 1 
ATOM   1677  O  OD2 . ASP B  1 76  ? 68.369  2.906   10.615 1.00 30.17  ? 76   ASP B OD2 1 
ATOM   1678  N  N   . GLU B  1 77  ? 66.884  5.163   6.625  1.00 27.50  ? 77   GLU B N   1 
ATOM   1679  C  CA  . GLU B  1 77  ? 66.024  5.807   5.630  1.00 27.67  ? 77   GLU B CA  1 
ATOM   1680  C  C   . GLU B  1 77  ? 64.638  6.005   6.234  1.00 26.30  ? 77   GLU B C   1 
ATOM   1681  O  O   . GLU B  1 77  ? 64.013  7.051   6.034  1.00 27.59  ? 77   GLU B O   1 
ATOM   1682  C  CB  . GLU B  1 77  ? 65.974  4.970   4.340  1.00 38.69  ? 77   GLU B CB  1 
ATOM   1683  C  CG  . GLU B  1 77  ? 64.848  5.381   3.410  1.00 55.42  ? 77   GLU B CG  1 
ATOM   1684  C  CD  . GLU B  1 77  ? 65.154  5.350   1.930  1.00 81.02  ? 77   GLU B CD  1 
ATOM   1685  O  OE1 . GLU B  1 77  ? 64.956  4.292   1.286  1.00 102.61 ? 77   GLU B OE1 1 
ATOM   1686  O  OE2 . GLU B  1 77  ? 65.585  6.382   1.366  1.00 99.07  ? 77   GLU B OE2 1 
ATOM   1687  N  N   . GLU B  1 78  ? 64.168  5.015   6.999  1.00 24.65  ? 78   GLU B N   1 
ATOM   1688  C  CA  . GLU B  1 78  ? 62.867  5.182   7.666  1.00 24.56  ? 78   GLU B CA  1 
ATOM   1689  C  C   . GLU B  1 78  ? 63.108  5.900   9.006  1.00 21.41  ? 78   GLU B C   1 
ATOM   1690  O  O   . GLU B  1 78  ? 63.485  5.232   9.972  1.00 23.31  ? 78   GLU B O   1 
ATOM   1691  C  CB  . GLU B  1 78  ? 62.145  3.872   7.912  1.00 22.29  ? 78   GLU B CB  1 
ATOM   1692  C  CG  . GLU B  1 78  ? 60.792  3.965   8.596  1.00 26.53  ? 78   GLU B CG  1 
ATOM   1693  C  CD  . GLU B  1 78  ? 59.714  4.444   7.640  1.00 36.42  ? 78   GLU B CD  1 
ATOM   1694  O  OE1 . GLU B  1 78  ? 58.575  4.706   8.073  1.00 32.57  ? 78   GLU B OE1 1 
ATOM   1695  O  OE2 . GLU B  1 78  ? 60.003  4.554   6.422  1.00 40.38  ? 78   GLU B OE2 1 
ATOM   1696  N  N   . ARG B  1 79  ? 62.886  7.199   8.974  1.00 22.12  ? 79   ARG B N   1 
ATOM   1697  C  CA  . ARG B  1 79  ? 63.023  8.068   10.134 1.00 22.23  ? 79   ARG B CA  1 
ATOM   1698  C  C   . ARG B  1 79  ? 62.136  9.289   10.008 1.00 25.37  ? 79   ARG B C   1 
ATOM   1699  O  O   . ARG B  1 79  ? 61.650  9.637   8.918  1.00 23.15  ? 79   ARG B O   1 
ATOM   1700  C  CB  . ARG B  1 79  ? 64.503  8.485   10.267 1.00 22.19  ? 79   ARG B CB  1 
ATOM   1701  C  CG  . ARG B  1 79  ? 64.994  9.310   9.073  1.00 20.46  ? 79   ARG B CG  1 
ATOM   1702  C  CD  . ARG B  1 79  ? 66.390  9.865   9.373  1.00 20.46  ? 79   ARG B CD  1 
ATOM   1703  N  NE  . ARG B  1 79  ? 66.313  11.259  9.873  1.00 21.04  ? 79   ARG B NE  1 
ATOM   1704  C  CZ  . ARG B  1 79  ? 67.365  12.058  9.986  1.00 23.66  ? 79   ARG B CZ  1 
ATOM   1705  N  NH1 . ARG B  1 79  ? 67.196  13.312  10.443 1.00 20.31  ? 79   ARG B NH1 1 
ATOM   1706  N  NH2 . ARG B  1 79  ? 68.587  11.654  9.664  1.00 20.73  ? 79   ARG B NH2 1 
ATOM   1707  N  N   . HIS B  1 80  ? 61.941  9.976   11.141 1.00 20.27  ? 80   HIS B N   1 
ATOM   1708  C  CA  . HIS B  1 80  ? 61.372  11.315  11.095 1.00 23.37  ? 80   HIS B CA  1 
ATOM   1709  C  C   . HIS B  1 80  ? 62.401  12.305  10.596 1.00 20.69  ? 80   HIS B C   1 
ATOM   1710  O  O   . HIS B  1 80  ? 63.593  12.094  10.836 1.00 20.96  ? 80   HIS B O   1 
ATOM   1711  C  CB  . HIS B  1 80  ? 60.904  11.730  12.489 1.00 24.66  ? 80   HIS B CB  1 
ATOM   1712  C  CG  . HIS B  1 80  ? 59.838  10.865  13.057 1.00 22.08  ? 80   HIS B CG  1 
ATOM   1713  N  ND1 . HIS B  1 80  ? 59.701  10.590  14.395 1.00 21.24  ? 80   HIS B ND1 1 
ATOM   1714  C  CD2 . HIS B  1 80  ? 58.818  10.200  12.439 1.00 20.03  ? 80   HIS B CD2 1 
ATOM   1715  C  CE1 . HIS B  1 80  ? 58.655  9.810   14.587 1.00 20.29  ? 80   HIS B CE1 1 
ATOM   1716  N  NE2 . HIS B  1 80  ? 58.095  9.559   13.399 1.00 21.70  ? 80   HIS B NE2 1 
ATOM   1717  N  N   . VAL B  1 81  ? 62.028  13.402  9.923  1.00 22.25  ? 81   VAL B N   1 
ATOM   1718  C  CA  . VAL B  1 81  ? 63.017  14.414  9.588  1.00 20.17  ? 81   VAL B CA  1 
ATOM   1719  C  C   . VAL B  1 81  ? 63.758  14.884  10.843 1.00 20.20  ? 81   VAL B C   1 
ATOM   1720  O  O   . VAL B  1 81  ? 64.975  15.089  10.828 1.00 19.62  ? 81   VAL B O   1 
ATOM   1721  C  CB  . VAL B  1 81  ? 62.390  15.618  8.861  1.00 21.70  ? 81   VAL B CB  1 
ATOM   1722  C  CG1 . VAL B  1 81  ? 63.305  16.826  8.825  1.00 21.21  ? 81   VAL B CG1 1 
ATOM   1723  C  CG2 . VAL B  1 81  ? 62.047  15.195  7.426  1.00 26.06  ? 81   VAL B CG2 1 
ATOM   1724  N  N   . GLY B  1 82  ? 63.015  15.025  11.949 1.00 22.22  ? 82   GLY B N   1 
ATOM   1725  C  CA  . GLY B  1 82  ? 63.710  15.550  13.130 1.00 20.54  ? 82   GLY B CA  1 
ATOM   1726  C  C   . GLY B  1 82  ? 64.472  14.535  13.943 1.00 22.48  ? 82   GLY B C   1 
ATOM   1727  O  O   . GLY B  1 82  ? 64.972  14.919  15.021 1.00 21.59  ? 82   GLY B O   1 
ATOM   1728  N  N   . ASP B  1 83  ? 64.621  13.291  13.521 1.00 18.02  ? 83   ASP B N   1 
ATOM   1729  C  CA  . ASP B  1 83  ? 65.335  12.287  14.318 1.00 16.69  ? 83   ASP B CA  1 
ATOM   1730  C  C   . ASP B  1 83  ? 66.852  12.413  14.256 1.00 22.83  ? 83   ASP B C   1 
ATOM   1731  O  O   . ASP B  1 83  ? 67.502  11.930  13.314 1.00 21.45  ? 83   ASP B O   1 
ATOM   1732  C  CB  . ASP B  1 83  ? 64.937  10.885  13.828 1.00 16.53  ? 83   ASP B CB  1 
ATOM   1733  C  CG  . ASP B  1 83  ? 63.490  10.572  14.177 1.00 22.10  ? 83   ASP B CG  1 
ATOM   1734  O  OD1 . ASP B  1 83  ? 62.887  11.296  15.014 1.00 21.06  ? 83   ASP B OD1 1 
ATOM   1735  O  OD2 . ASP B  1 83  ? 62.992  9.571   13.609 1.00 22.32  ? 83   ASP B OD2 1 
ATOM   1736  N  N   . LEU B  1 84  ? 67.435  13.048  15.276 1.00 20.02  ? 84   LEU B N   1 
ATOM   1737  C  CA  . LEU B  1 84  ? 68.871  13.258  15.338 1.00 16.66  ? 84   LEU B CA  1 
ATOM   1738  C  C   . LEU B  1 84  ? 69.566  12.245  16.248 1.00 21.16  ? 84   LEU B C   1 
ATOM   1739  O  O   . LEU B  1 84  ? 70.786  12.324  16.463 1.00 22.06  ? 84   LEU B O   1 
ATOM   1740  C  CB  . LEU B  1 84  ? 69.182  14.705  15.751 1.00 17.27  ? 84   LEU B CB  1 
ATOM   1741  C  CG  . LEU B  1 84  ? 68.724  15.799  14.772 1.00 19.16  ? 84   LEU B CG  1 
ATOM   1742  C  CD1 . LEU B  1 84  ? 69.091  17.195  15.269 1.00 17.76  ? 84   LEU B CD1 1 
ATOM   1743  C  CD2 . LEU B  1 84  ? 69.325  15.602  13.389 1.00 21.01  ? 84   LEU B CD2 1 
ATOM   1744  N  N   . GLY B  1 85  ? 68.849  11.258  16.750 1.00 17.49  ? 85   GLY B N   1 
ATOM   1745  C  CA  . GLY B  1 85  ? 69.434  10.165  17.509 1.00 18.73  ? 85   GLY B CA  1 
ATOM   1746  C  C   . GLY B  1 85  ? 69.758  10.580  18.943 1.00 19.43  ? 85   GLY B C   1 
ATOM   1747  O  O   . GLY B  1 85  ? 68.898  11.189  19.565 1.00 21.03  ? 85   GLY B O   1 
ATOM   1748  N  N   . ASN B  1 86  ? 70.933  10.207  19.450 1.00 17.35  ? 86   ASN B N   1 
ATOM   1749  C  CA  . ASN B  1 86  ? 71.316  10.543  20.819 1.00 18.21  ? 86   ASN B CA  1 
ATOM   1750  C  C   . ASN B  1 86  ? 72.488  11.526  20.882 1.00 20.87  ? 86   ASN B C   1 
ATOM   1751  O  O   . ASN B  1 86  ? 73.293  11.593  19.955 1.00 19.24  ? 86   ASN B O   1 
ATOM   1752  C  CB  . ASN B  1 86  ? 71.748  9.273   21.575 1.00 18.92  ? 86   ASN B CB  1 
ATOM   1753  C  CG  . ASN B  1 86  ? 70.521  8.403   21.818 1.00 19.27  ? 86   ASN B CG  1 
ATOM   1754  O  OD1 . ASN B  1 86  ? 69.628  8.851   22.532 1.00 20.35  ? 86   ASN B OD1 1 
ATOM   1755  N  ND2 . ASN B  1 86  ? 70.549  7.206   21.236 1.00 19.81  ? 86   ASN B ND2 1 
ATOM   1756  N  N   . VAL B  1 87  ? 72.553  12.244  21.996 1.00 18.21  ? 87   VAL B N   1 
ATOM   1757  C  CA  . VAL B  1 87  ? 73.774  12.950  22.390 1.00 17.49  ? 87   VAL B CA  1 
ATOM   1758  C  C   . VAL B  1 87  ? 74.268  12.310  23.694 1.00 18.14  ? 87   VAL B C   1 
ATOM   1759  O  O   . VAL B  1 87  ? 73.467  11.787  24.470 1.00 21.93  ? 87   VAL B O   1 
ATOM   1760  C  CB  . VAL B  1 87  ? 73.593  14.451  22.565 1.00 18.01  ? 87   VAL B CB  1 
ATOM   1761  C  CG1 . VAL B  1 87  ? 73.277  15.075  21.206 1.00 20.57  ? 87   VAL B CG1 1 
ATOM   1762  C  CG2 . VAL B  1 87  ? 72.481  14.784  23.560 1.00 20.72  ? 87   VAL B CG2 1 
ATOM   1763  N  N   . THR B  1 88  ? 75.564  12.364  23.925 1.00 17.91  ? 88   THR B N   1 
ATOM   1764  C  CA  . THR B  1 88  ? 76.174  11.697  25.070 1.00 18.10  ? 88   THR B CA  1 
ATOM   1765  C  C   . THR B  1 88  ? 76.741  12.724  26.038 1.00 19.91  ? 88   THR B C   1 
ATOM   1766  O  O   . THR B  1 88  ? 77.589  13.533  25.623 1.00 20.46  ? 88   THR B O   1 
ATOM   1767  C  CB  . THR B  1 88  ? 77.290  10.770  24.539 1.00 21.75  ? 88   THR B CB  1 
ATOM   1768  O  OG1 . THR B  1 88  ? 76.728  9.690   23.771 1.00 22.28  ? 88   THR B OG1 1 
ATOM   1769  C  CG2 . THR B  1 88  ? 78.074  10.116  25.681 1.00 22.04  ? 88   THR B CG2 1 
ATOM   1770  N  N   . ALA B  1 89  ? 76.304  12.667  27.297 1.00 18.09  ? 89   ALA B N   1 
ATOM   1771  C  CA  . ALA B  1 89  ? 76.855  13.481  28.364 1.00 19.41  ? 89   ALA B CA  1 
ATOM   1772  C  C   . ALA B  1 89  ? 77.978  12.714  29.091 1.00 21.94  ? 89   ALA B C   1 
ATOM   1773  O  O   . ALA B  1 89  ? 77.887  11.508  29.321 1.00 22.48  ? 89   ALA B O   1 
ATOM   1774  C  CB  . ALA B  1 89  ? 75.826  13.904  29.398 1.00 19.32  ? 89   ALA B CB  1 
ATOM   1775  N  N   . ASP B  1 90  ? 79.048  13.428  29.431 1.00 22.62  ? 90   ASP B N   1 
ATOM   1776  C  CA  . ASP B  1 90  ? 80.193  12.810  30.102 1.00 21.92  ? 90   ASP B CA  1 
ATOM   1777  C  C   . ASP B  1 90  ? 79.913  12.742  31.603 1.00 22.42  ? 90   ASP B C   1 
ATOM   1778  O  O   . ASP B  1 90  ? 78.813  13.091  32.046 1.00 24.64  ? 90   ASP B O   1 
ATOM   1779  C  CB  . ASP B  1 90  ? 81.493  13.586  29.820 1.00 23.35  ? 90   ASP B CB  1 
ATOM   1780  C  CG  . ASP B  1 90  ? 81.502  15.018  30.304 1.00 21.66  ? 90   ASP B CG  1 
ATOM   1781  O  OD1 . ASP B  1 90  ? 82.294  15.843  29.761 1.00 29.98  ? 90   ASP B OD1 1 
ATOM   1782  O  OD2 . ASP B  1 90  ? 80.739  15.397  31.229 1.00 24.29  ? 90   ASP B OD2 1 
ATOM   1783  N  N   . LYS B  1 91  ? 80.933  12.294  32.350 1.00 26.70  ? 91   LYS B N   1 
ATOM   1784  C  CA  . LYS B  1 91  ? 80.767  12.104  33.788 1.00 30.20  ? 91   LYS B CA  1 
ATOM   1785  C  C   . LYS B  1 91  ? 80.483  13.402  34.528 1.00 28.49  ? 91   LYS B C   1 
ATOM   1786  O  O   . LYS B  1 91  ? 79.964  13.350  35.654 1.00 34.49  ? 91   LYS B O   1 
ATOM   1787  C  CB  . LYS B  1 91  ? 82.011  11.449  34.414 1.00 28.37  ? 91   LYS B CB  1 
ATOM   1788  C  CG  . LYS B  1 91  ? 83.214  12.375  34.514 1.00 45.22  ? 91   LYS B CG  1 
ATOM   1789  C  CD  . LYS B  1 91  ? 84.509  11.591  34.691 1.00 52.03  ? 91   LYS B CD  1 
ATOM   1790  C  CE  . LYS B  1 91  ? 85.724  12.513  34.626 1.00 57.48  ? 91   LYS B CE  1 
ATOM   1791  N  NZ  . LYS B  1 91  ? 85.817  13.345  35.865 1.00 95.46  ? 91   LYS B NZ  1 
ATOM   1792  N  N   . ASP B  1 92  ? 80.793  14.551  33.939 1.00 23.56  ? 92   ASP B N   1 
ATOM   1793  C  CA  . ASP B  1 92  ? 80.431  15.808  34.587 1.00 22.66  ? 92   ASP B CA  1 
ATOM   1794  C  C   . ASP B  1 92  ? 79.098  16.373  34.087 1.00 20.08  ? 92   ASP B C   1 
ATOM   1795  O  O   . ASP B  1 92  ? 78.779  17.522  34.416 1.00 21.71  ? 92   ASP B O   1 
ATOM   1796  C  CB  . ASP B  1 92  ? 81.514  16.864  34.323 1.00 29.91  ? 92   ASP B CB  1 
ATOM   1797  C  CG  . ASP B  1 92  ? 82.844  16.419  34.916 1.00 46.55  ? 92   ASP B CG  1 
ATOM   1798  O  OD1 . ASP B  1 92  ? 83.873  16.568  34.236 1.00 52.03  ? 92   ASP B OD1 1 
ATOM   1799  O  OD2 . ASP B  1 92  ? 82.829  15.904  36.055 1.00 37.65  ? 92   ASP B OD2 1 
ATOM   1800  N  N   . GLY B  1 93  ? 78.373  15.577  33.315 1.00 24.03  ? 93   GLY B N   1 
ATOM   1801  C  CA  . GLY B  1 93  ? 77.043  15.884  32.834 1.00 23.64  ? 93   GLY B CA  1 
ATOM   1802  C  C   . GLY B  1 93  ? 77.029  16.844  31.646 1.00 27.08  ? 93   GLY B C   1 
ATOM   1803  O  O   . GLY B  1 93  ? 76.023  17.522  31.401 1.00 23.51  ? 93   GLY B O   1 
ATOM   1804  N  N   . VAL B  1 94  ? 78.129  16.898  30.904 1.00 20.88  ? 94   VAL B N   1 
ATOM   1805  C  CA  . VAL B  1 94  ? 78.255  17.805  29.764 1.00 21.95  ? 94   VAL B CA  1 
ATOM   1806  C  C   . VAL B  1 94  ? 78.223  17.005  28.461 1.00 23.01  ? 94   VAL B C   1 
ATOM   1807  O  O   . VAL B  1 94  ? 78.972  16.036  28.289 1.00 20.51  ? 94   VAL B O   1 
ATOM   1808  C  CB  . VAL B  1 94  ? 79.567  18.613  29.797 1.00 23.72  ? 94   VAL B CB  1 
ATOM   1809  C  CG1 . VAL B  1 94  ? 79.710  19.422  28.523 1.00 23.05  ? 94   VAL B CG1 1 
ATOM   1810  C  CG2 . VAL B  1 94  ? 79.599  19.501  31.036 1.00 25.07  ? 94   VAL B CG2 1 
ATOM   1811  N  N   . ALA B  1 95  ? 77.333  17.441  27.562 1.00 21.38  ? 95   ALA B N   1 
ATOM   1812  C  CA  . ALA B  1 95  ? 77.355  16.842  26.222 1.00 21.00  ? 95   ALA B CA  1 
ATOM   1813  C  C   . ALA B  1 95  ? 77.943  17.821  25.214 1.00 20.93  ? 95   ALA B C   1 
ATOM   1814  O  O   . ALA B  1 95  ? 77.331  18.857  24.935 1.00 20.46  ? 95   ALA B O   1 
ATOM   1815  C  CB  . ALA B  1 95  ? 75.950  16.450  25.780 1.00 20.85  ? 95   ALA B CB  1 
ATOM   1816  N  N   . ASP B  1 96  ? 79.109  17.522  24.675 1.00 19.95  ? 96   ASP B N   1 
ATOM   1817  C  CA  . ASP B  1 96  ? 79.758  18.355  23.646 1.00 18.53  ? 96   ASP B CA  1 
ATOM   1818  C  C   . ASP B  1 96  ? 79.254  17.842  22.313 1.00 19.32  ? 96   ASP B C   1 
ATOM   1819  O  O   . ASP B  1 96  ? 79.805  16.945  21.699 1.00 21.20  ? 96   ASP B O   1 
ATOM   1820  C  CB  . ASP B  1 96  ? 81.283  18.253  23.783 1.00 19.26  ? 96   ASP B CB  1 
ATOM   1821  C  CG  . ASP B  1 96  ? 81.768  19.069  24.986 1.00 30.32  ? 96   ASP B CG  1 
ATOM   1822  O  OD1 . ASP B  1 96  ? 82.517  18.515  25.821 1.00 31.31  ? 96   ASP B OD1 1 
ATOM   1823  O  OD2 . ASP B  1 96  ? 81.389  20.263  25.111 1.00 30.64  ? 96   ASP B OD2 1 
ATOM   1824  N  N   . VAL B  1 97  ? 78.117  18.393  21.909 1.00 18.79  ? 97   VAL B N   1 
ATOM   1825  C  CA  . VAL B  1 97  ? 77.395  17.811  20.782 1.00 18.76  ? 97   VAL B CA  1 
ATOM   1826  C  C   . VAL B  1 97  ? 78.147  18.022  19.481 1.00 20.07  ? 97   VAL B C   1 
ATOM   1827  O  O   . VAL B  1 97  ? 78.653  19.097  19.230 1.00 20.58  ? 97   VAL B O   1 
ATOM   1828  C  CB  . VAL B  1 97  ? 75.983  18.428  20.668 1.00 21.56  ? 97   VAL B CB  1 
ATOM   1829  C  CG1 . VAL B  1 97  ? 75.257  17.894  19.437 1.00 18.04  ? 97   VAL B CG1 1 
ATOM   1830  C  CG2 . VAL B  1 97  ? 75.176  18.111  21.929 1.00 19.21  ? 97   VAL B CG2 1 
ATOM   1831  N  N   . SER B  1 98  ? 78.194  16.962  18.670 1.00 20.02  ? 98   SER B N   1 
ATOM   1832  C  CA  . SER B  1 98  ? 78.830  17.103  17.361 1.00 25.15  ? 98   SER B CA  1 
ATOM   1833  C  C   . SER B  1 98  ? 78.158  16.135  16.395 1.00 25.98  ? 98   SER B C   1 
ATOM   1834  O  O   . SER B  1 98  ? 78.467  14.929  16.391 1.00 28.37  ? 98   SER B O   1 
ATOM   1835  C  CB  . SER B  1 98  ? 80.326  16.815  17.508 1.00 29.12  ? 98   SER B CB  1 
ATOM   1836  O  OG  . SER B  1 98  ? 81.010  16.962  16.279 1.00 33.69  ? 98   SER B OG  1 
ATOM   1837  N  N   . ILE B  1 99  ? 77.236  16.662  15.600 1.00 18.88  ? 99   ILE B N   1 
ATOM   1838  C  CA  . ILE B  1 99  ? 76.457  15.790  14.703 1.00 24.65  ? 99   ILE B CA  1 
ATOM   1839  C  C   . ILE B  1 99  ? 76.544  16.319  13.291 1.00 25.84  ? 99   ILE B C   1 
ATOM   1840  O  O   . ILE B  1 99  ? 76.665  17.548  13.159 1.00 24.14  ? 99   ILE B O   1 
ATOM   1841  C  CB  . ILE B  1 99  ? 75.005  15.784  15.236 1.00 23.10  ? 99   ILE B CB  1 
ATOM   1842  C  CG1 . ILE B  1 99  ? 74.873  14.815  16.435 1.00 21.70  ? 99   ILE B CG1 1 
ATOM   1843  C  CG2 . ILE B  1 99  ? 73.953  15.494  14.186 1.00 25.85  ? 99   ILE B CG2 1 
ATOM   1844  C  CD1 . ILE B  1 99  ? 73.557  15.002  17.155 1.00 22.19  ? 99   ILE B CD1 1 
ATOM   1845  N  N   . GLU B  1 100 ? 76.470  15.496  12.268 1.00 20.74  ? 100  GLU B N   1 
ATOM   1846  C  CA  . GLU B  1 100 ? 76.253  15.985  10.905 1.00 20.01  ? 100  GLU B CA  1 
ATOM   1847  C  C   . GLU B  1 100 ? 75.055  15.264  10.332 1.00 20.25  ? 100  GLU B C   1 
ATOM   1848  O  O   . GLU B  1 100 ? 74.981  14.025  10.402 1.00 23.24  ? 100  GLU B O   1 
ATOM   1849  C  CB  . GLU B  1 100 ? 77.515  15.755  10.071 1.00 26.62  ? 100  GLU B CB  1 
ATOM   1850  C  CG  . GLU B  1 100 ? 77.332  16.236  8.637  1.00 36.32  ? 100  GLU B CG  1 
ATOM   1851  C  CD  . GLU B  1 100 ? 78.616  16.050  7.835  1.00 49.37  ? 100  GLU B CD  1 
ATOM   1852  O  OE1 . GLU B  1 100 ? 78.564  15.414  6.757  1.00 44.87  ? 100  GLU B OE1 1 
ATOM   1853  O  OE2 . GLU B  1 100 ? 79.661  16.544  8.305  1.00 47.77  ? 100  GLU B OE2 1 
ATOM   1854  N  N   . ASP B  1 101 ? 74.093  16.021  9.789  1.00 22.54  ? 101  ASP B N   1 
ATOM   1855  C  CA  . ASP B  1 101 ? 72.918  15.305  9.303  1.00 20.23  ? 101  ASP B CA  1 
ATOM   1856  C  C   . ASP B  1 101 ? 72.547  15.815  7.914  1.00 24.06  ? 101  ASP B C   1 
ATOM   1857  O  O   . ASP B  1 101 ? 72.602  17.029  7.705  1.00 25.55  ? 101  ASP B O   1 
ATOM   1858  C  CB  . ASP B  1 101 ? 71.720  15.508  10.244 1.00 21.39  ? 101  ASP B CB  1 
ATOM   1859  C  CG  . ASP B  1 101 ? 70.594  14.554  9.908  1.00 23.98  ? 101  ASP B CG  1 
ATOM   1860  O  OD1 . ASP B  1 101 ? 69.582  14.986  9.320  1.00 22.73  ? 101  ASP B OD1 1 
ATOM   1861  O  OD2 . ASP B  1 101 ? 70.766  13.352  10.215 1.00 28.29  ? 101  ASP B OD2 1 
ATOM   1862  N  N   . SER B  1 102 ? 72.131  14.935  7.008  1.00 20.94  ? 102  SER B N   1 
ATOM   1863  C  CA  . SER B  1 102 ? 71.783  15.498  5.700  1.00 29.88  ? 102  SER B CA  1 
ATOM   1864  C  C   . SER B  1 102 ? 70.294  15.431  5.437  1.00 29.60  ? 102  SER B C   1 
ATOM   1865  O  O   . SER B  1 102 ? 69.885  15.664  4.303  1.00 27.70  ? 102  SER B O   1 
ATOM   1866  C  CB  . SER B  1 102 ? 72.578  14.736  4.627  1.00 34.97  ? 102  SER B CB  1 
ATOM   1867  O  OG  . SER B  1 102 ? 72.428  13.335  4.881  1.00 49.51  ? 102  SER B OG  1 
ATOM   1868  N  N   . VAL B  1 103 ? 69.464  15.152  6.444  1.00 22.92  ? 103  VAL B N   1 
ATOM   1869  C  CA  . VAL B  1 103 ? 68.011  15.111  6.226  1.00 21.27  ? 103  VAL B CA  1 
ATOM   1870  C  C   . VAL B  1 103 ? 67.360  16.385  6.724  1.00 24.10  ? 103  VAL B C   1 
ATOM   1871  O  O   . VAL B  1 103 ? 66.491  16.965  6.076  1.00 22.67  ? 103  VAL B O   1 
ATOM   1872  C  CB  . VAL B  1 103 ? 67.399  13.866  6.887  1.00 21.36  ? 103  VAL B CB  1 
ATOM   1873  C  CG1 . VAL B  1 103 ? 65.885  13.872  6.830  1.00 26.72  ? 103  VAL B CG1 1 
ATOM   1874  C  CG2 . VAL B  1 103 ? 67.961  12.617  6.186  1.00 20.94  ? 103  VAL B CG2 1 
ATOM   1875  N  N   . ILE B  1 104 ? 67.779  16.885  7.891  1.00 23.85  ? 104  ILE B N   1 
ATOM   1876  C  CA  . ILE B  1 104 ? 67.326  18.212  8.289  1.00 22.16  ? 104  ILE B CA  1 
ATOM   1877  C  C   . ILE B  1 104 ? 67.926  19.243  7.337  1.00 23.67  ? 104  ILE B C   1 
ATOM   1878  O  O   . ILE B  1 104 ? 68.946  19.004  6.685  1.00 20.76  ? 104  ILE B O   1 
ATOM   1879  C  CB  . ILE B  1 104 ? 67.780  18.599  9.720  1.00 20.35  ? 104  ILE B CB  1 
ATOM   1880  C  CG1 . ILE B  1 104 ? 69.280  18.427  9.935  1.00 23.69  ? 104  ILE B CG1 1 
ATOM   1881  C  CG2 . ILE B  1 104 ? 66.948  17.840  10.748 1.00 20.04  ? 104  ILE B CG2 1 
ATOM   1882  C  CD1 . ILE B  1 104 ? 69.880  19.156  11.132 1.00 21.29  ? 104  ILE B CD1 1 
ATOM   1883  N  N   . SER B  1 105 ? 67.307  20.414  7.288  1.00 21.90  ? 105  SER B N   1 
ATOM   1884  C  CA  . SER B  1 105 ? 67.836  21.504  6.469  1.00 22.86  ? 105  SER B CA  1 
ATOM   1885  C  C   . SER B  1 105 ? 67.528  22.845  7.133  1.00 20.85  ? 105  SER B C   1 
ATOM   1886  O  O   . SER B  1 105 ? 66.654  22.916  8.003  1.00 21.02  ? 105  SER B O   1 
ATOM   1887  C  CB  . SER B  1 105 ? 67.245  21.431  5.051  1.00 27.02  ? 105  SER B CB  1 
ATOM   1888  O  OG  . SER B  1 105 ? 67.870  22.391  4.198  1.00 28.41  ? 105  SER B OG  1 
ATOM   1889  N  N   . LEU B  1 106 ? 68.208  23.904  6.728  1.00 22.81  ? 106  LEU B N   1 
ATOM   1890  C  CA  . LEU B  1 106 ? 67.906  25.263  7.178  1.00 22.04  ? 106  LEU B CA  1 
ATOM   1891  C  C   . LEU B  1 106 ? 67.106  26.046  6.128  1.00 30.10  ? 106  LEU B C   1 
ATOM   1892  O  O   . LEU B  1 106 ? 66.969  27.263  6.238  1.00 27.68  ? 106  LEU B O   1 
ATOM   1893  C  CB  . LEU B  1 106 ? 69.189  26.014  7.521  1.00 22.07  ? 106  LEU B CB  1 
ATOM   1894  C  CG  . LEU B  1 106 ? 70.077  25.379  8.605  1.00 25.75  ? 106  LEU B CG  1 
ATOM   1895  C  CD1 . LEU B  1 106 ? 71.194  26.325  9.035  1.00 23.22  ? 106  LEU B CD1 1 
ATOM   1896  C  CD2 . LEU B  1 106 ? 69.217  24.946  9.797  1.00 25.99  ? 106  LEU B CD2 1 
ATOM   1897  N  N   . SER B  1 107 ? 66.568  25.356  5.135  1.00 27.75  ? 107  SER B N   1 
ATOM   1898  C  CA  . SER B  1 107 ? 65.692  25.935  4.126  1.00 33.37  ? 107  SER B CA  1 
ATOM   1899  C  C   . SER B  1 107 ? 64.822  24.874  3.464  1.00 38.47  ? 107  SER B C   1 
ATOM   1900  O  O   . SER B  1 107 ? 65.109  23.673  3.601  1.00 32.25  ? 107  SER B O   1 
ATOM   1901  C  CB  . SER B  1 107 ? 66.509  26.642  3.044  1.00 38.78  ? 107  SER B CB  1 
ATOM   1902  O  OG  . SER B  1 107 ? 67.057  25.689  2.151  1.00 42.48  ? 107  SER B OG  1 
ATOM   1903  N  N   . GLY B  1 108 ? 63.767  25.295  2.763  1.00 34.76  ? 108  GLY B N   1 
ATOM   1904  C  CA  . GLY B  1 108 ? 62.912  24.333  2.062  1.00 34.29  ? 108  GLY B CA  1 
ATOM   1905  C  C   . GLY B  1 108 ? 61.983  23.554  2.973  1.00 33.51  ? 108  GLY B C   1 
ATOM   1906  O  O   . GLY B  1 108 ? 61.728  23.995  4.098  1.00 37.33  ? 108  GLY B O   1 
ATOM   1907  N  N   . ASP B  1 109 ? 61.470  22.414  2.524  1.00 32.52  ? 109  ASP B N   1 
ATOM   1908  C  CA  . ASP B  1 109 ? 60.482  21.540  3.110  1.00 35.11  ? 109  ASP B CA  1 
ATOM   1909  C  C   . ASP B  1 109 ? 60.942  20.882  4.414  1.00 32.49  ? 109  ASP B C   1 
ATOM   1910  O  O   . ASP B  1 109 ? 60.132  20.621  5.298  1.00 33.45  ? 109  ASP B O   1 
ATOM   1911  C  CB  . ASP B  1 109 ? 60.148  20.360  2.183  1.00 46.03  ? 109  ASP B CB  1 
ATOM   1912  C  CG  . ASP B  1 109 ? 59.350  20.745  0.958  1.00 55.42  ? 109  ASP B CG  1 
ATOM   1913  O  OD1 . ASP B  1 109 ? 58.856  21.889  0.929  1.00 52.86  ? 109  ASP B OD1 1 
ATOM   1914  O  OD2 . ASP B  1 109 ? 59.239  19.886  0.056  1.00 62.08  ? 109  ASP B OD2 1 
ATOM   1915  N  N   . HIS B  1 110 ? 62.241  20.600  4.478  1.00 29.78  ? 110  HIS B N   1 
ATOM   1916  C  CA  . HIS B  1 110 ? 62.768  19.987  5.691  1.00 27.73  ? 110  HIS B CA  1 
ATOM   1917  C  C   . HIS B  1 110 ? 63.370  21.044  6.612  1.00 27.30  ? 110  HIS B C   1 
ATOM   1918  O  O   . HIS B  1 110 ? 64.144  20.658  7.500  1.00 24.57  ? 110  HIS B O   1 
ATOM   1919  C  CB  . HIS B  1 110 ? 63.858  18.977  5.355  1.00 27.75  ? 110  HIS B CB  1 
ATOM   1920  C  CG  . HIS B  1 110 ? 63.282  17.803  4.611  1.00 35.42  ? 110  HIS B CG  1 
ATOM   1921  N  ND1 . HIS B  1 110 ? 64.027  16.683  4.313  1.00 40.82  ? 110  HIS B ND1 1 
ATOM   1922  C  CD2 . HIS B  1 110 ? 62.041  17.585  4.132  1.00 41.77  ? 110  HIS B CD2 1 
ATOM   1923  C  CE1 . HIS B  1 110 ? 63.255  15.827  3.666  1.00 45.92  ? 110  HIS B CE1 1 
ATOM   1924  N  NE2 . HIS B  1 110 ? 62.042  16.343  3.538  1.00 43.19  ? 110  HIS B NE2 1 
ATOM   1925  N  N   . CYS B  1 111 ? 63.005  22.296  6.366  1.00 22.68  ? 111  CYS B N   1 
ATOM   1926  C  CA  . CYS B  1 111 ? 63.522  23.388  7.171  1.00 23.37  ? 111  CYS B CA  1 
ATOM   1927  C  C   . CYS B  1 111 ? 63.121  23.261  8.642  1.00 23.35  ? 111  CYS B C   1 
ATOM   1928  O  O   . CYS B  1 111 ? 61.965  22.985  8.979  1.00 23.06  ? 111  CYS B O   1 
ATOM   1929  C  CB  . CYS B  1 111 ? 63.038  24.731  6.592  1.00 27.16  ? 111  CYS B CB  1 
ATOM   1930  S  SG  . CYS B  1 111 ? 63.797  26.123  7.460  1.00 39.55  ? 111  CYS B SG  1 
ATOM   1931  N  N   . ILE B  1 112 ? 64.088  23.450  9.537  1.00 20.74  ? 112  ILE B N   1 
ATOM   1932  C  CA  . ILE B  1 112 ? 63.832  23.298  10.972 1.00 21.11  ? 112  ILE B CA  1 
ATOM   1933  C  C   . ILE B  1 112 ? 63.794  24.636  11.686 1.00 21.94  ? 112  ILE B C   1 
ATOM   1934  O  O   . ILE B  1 112 ? 63.576  24.697  12.899 1.00 20.66  ? 112  ILE B O   1 
ATOM   1935  C  CB  . ILE B  1 112 ? 64.909  22.404  11.621 1.00 19.87  ? 112  ILE B CB  1 
ATOM   1936  C  CG1 . ILE B  1 112 ? 66.341  22.910  11.429 1.00 18.52  ? 112  ILE B CG1 1 
ATOM   1937  C  CG2 . ILE B  1 112 ? 64.748  20.975  11.110 1.00 21.55  ? 112  ILE B CG2 1 
ATOM   1938  C  CD1 . ILE B  1 112 ? 67.391  22.149  12.221 1.00 24.60  ? 112  ILE B CD1 1 
ATOM   1939  N  N   . ILE B  1 113 ? 64.014  25.725  10.947 1.00 22.03  ? 113  ILE B N   1 
ATOM   1940  C  CA  . ILE B  1 113 ? 63.965  27.054  11.585 1.00 21.44  ? 113  ILE B CA  1 
ATOM   1941  C  C   . ILE B  1 113 ? 62.548  27.299  12.054 1.00 23.37  ? 113  ILE B C   1 
ATOM   1942  O  O   . ILE B  1 113 ? 61.574  27.005  11.363 1.00 21.23  ? 113  ILE B O   1 
ATOM   1943  C  CB  . ILE B  1 113 ? 64.568  28.102  10.637 1.00 27.88  ? 113  ILE B CB  1 
ATOM   1944  C  CG1 . ILE B  1 113 ? 66.103  27.940  10.576 1.00 23.06  ? 113  ILE B CG1 1 
ATOM   1945  C  CG2 . ILE B  1 113 ? 64.201  29.512  11.044 1.00 22.19  ? 113  ILE B CG2 1 
ATOM   1946  C  CD1 . ILE B  1 113 ? 66.818  28.862  9.625  1.00 31.12  ? 113  ILE B CD1 1 
ATOM   1947  N  N   . GLY B  1 114 ? 62.387  27.800  13.285 1.00 22.03  ? 114  GLY B N   1 
ATOM   1948  C  CA  . GLY B  1 114 ? 61.030  28.015  13.774 1.00 18.03  ? 114  GLY B CA  1 
ATOM   1949  C  C   . GLY B  1 114 ? 60.484  26.809  14.492 1.00 20.57  ? 114  GLY B C   1 
ATOM   1950  O  O   . GLY B  1 114 ? 59.357  26.847  15.009 1.00 21.41  ? 114  GLY B O   1 
ATOM   1951  N  N   . ARG B  1 115 ? 61.234  25.716  14.544 1.00 18.56  ? 115  ARG B N   1 
ATOM   1952  C  CA  . ARG B  1 115 ? 60.737  24.494  15.198 1.00 21.48  ? 115  ARG B CA  1 
ATOM   1953  C  C   . ARG B  1 115 ? 61.484  24.322  16.512 1.00 20.51  ? 115  ARG B C   1 
ATOM   1954  O  O   . ARG B  1 115 ? 62.207  25.276  16.848 1.00 23.03  ? 115  ARG B O   1 
ATOM   1955  C  CB  . ARG B  1 115 ? 60.841  23.266  14.283 1.00 19.78  ? 115  ARG B CB  1 
ATOM   1956  C  CG  . ARG B  1 115 ? 60.139  23.603  12.941 1.00 23.76  ? 115  ARG B CG  1 
ATOM   1957  C  CD  . ARG B  1 115 ? 59.823  22.339  12.153 1.00 25.23  ? 115  ARG B CD  1 
ATOM   1958  N  NE  . ARG B  1 115 ? 59.233  22.694  10.851 1.00 26.78  ? 115  ARG B NE  1 
ATOM   1959  C  CZ  . ARG B  1 115 ? 57.920  22.733  10.612 1.00 24.98  ? 115  ARG B CZ  1 
ATOM   1960  N  NH1 . ARG B  1 115 ? 57.528  23.064  9.376  1.00 26.91  ? 115  ARG B NH1 1 
ATOM   1961  N  NH2 . ARG B  1 115 ? 56.973  22.450  11.494 1.00 22.86  ? 115  ARG B NH2 1 
ATOM   1962  N  N   . THR B  1 116 ? 61.283  23.242  17.220 1.00 18.38  ? 116  THR B N   1 
ATOM   1963  C  CA  . THR B  1 116 ? 61.827  23.183  18.590 1.00 17.74  ? 116  THR B CA  1 
ATOM   1964  C  C   . THR B  1 116 ? 62.840  22.055  18.693 1.00 18.63  ? 116  THR B C   1 
ATOM   1965  O  O   . THR B  1 116 ? 62.495  20.944  18.294 1.00 21.56  ? 116  THR B O   1 
ATOM   1966  C  CB  . THR B  1 116 ? 60.678  22.988  19.591 1.00 20.76  ? 116  THR B CB  1 
ATOM   1967  O  OG1 . THR B  1 116 ? 59.945  24.230  19.690 1.00 20.39  ? 116  THR B OG1 1 
ATOM   1968  C  CG2 . THR B  1 116 ? 61.251  22.678  20.976 1.00 20.58  ? 116  THR B CG2 1 
ATOM   1969  N  N   . LEU B  1 117 ? 64.042  22.337  19.205 1.00 16.53  ? 117  LEU B N   1 
ATOM   1970  C  CA  . LEU B  1 117 ? 64.996  21.286  19.519 1.00 18.45  ? 117  LEU B CA  1 
ATOM   1971  C  C   . LEU B  1 117 ? 64.748  20.809  20.963 1.00 19.44  ? 117  LEU B C   1 
ATOM   1972  O  O   . LEU B  1 117 ? 64.584  21.691  21.831 1.00 19.70  ? 117  LEU B O   1 
ATOM   1973  C  CB  . LEU B  1 117 ? 66.423  21.822  19.374 1.00 18.14  ? 117  LEU B CB  1 
ATOM   1974  C  CG  . LEU B  1 117 ? 67.563  20.823  19.592 1.00 18.72  ? 117  LEU B CG  1 
ATOM   1975  C  CD1 . LEU B  1 117 ? 67.513  19.698  18.563 1.00 18.45  ? 117  LEU B CD1 1 
ATOM   1976  C  CD2 . LEU B  1 117 ? 68.921  21.544  19.537 1.00 16.45  ? 117  LEU B CD2 1 
ATOM   1977  N  N   . VAL B  1 118 ? 64.718  19.501  21.166 1.00 17.47  ? 118  VAL B N   1 
ATOM   1978  C  CA  . VAL B  1 118 ? 64.447  18.922  22.497 1.00 17.37  ? 118  VAL B CA  1 
ATOM   1979  C  C   . VAL B  1 118 ? 65.517  17.913  22.881 1.00 19.90  ? 118  VAL B C   1 
ATOM   1980  O  O   . VAL B  1 118 ? 65.914  17.092  22.042 1.00 17.97  ? 118  VAL B O   1 
ATOM   1981  C  CB  . VAL B  1 118 ? 63.085  18.205  22.513 1.00 20.17  ? 118  VAL B CB  1 
ATOM   1982  C  CG1 . VAL B  1 118 ? 62.830  17.609  23.887 1.00 17.71  ? 118  VAL B CG1 1 
ATOM   1983  C  CG2 . VAL B  1 118 ? 61.949  19.149  22.108 1.00 20.42  ? 118  VAL B CG2 1 
ATOM   1984  N  N   . VAL B  1 119 ? 65.986  17.940  24.125 1.00 20.94  ? 119  VAL B N   1 
ATOM   1985  C  CA  . VAL B  1 119 ? 66.895  16.913  24.644 1.00 15.34  ? 119  VAL B CA  1 
ATOM   1986  C  C   . VAL B  1 119 ? 66.134  16.166  25.744 1.00 19.51  ? 119  VAL B C   1 
ATOM   1987  O  O   . VAL B  1 119 ? 65.399  16.807  26.514 1.00 19.69  ? 119  VAL B O   1 
ATOM   1988  C  CB  . VAL B  1 119 ? 68.216  17.520  25.131 1.00 15.83  ? 119  VAL B CB  1 
ATOM   1989  C  CG1 . VAL B  1 119 ? 67.999  18.485  26.276 1.00 18.60  ? 119  VAL B CG1 1 
ATOM   1990  C  CG2 . VAL B  1 119 ? 69.196  16.414  25.544 1.00 20.61  ? 119  VAL B CG2 1 
ATOM   1991  N  N   . HIS B  1 120 ? 66.231  14.855  25.778 1.00 20.24  ? 120  HIS B N   1 
ATOM   1992  C  CA  . HIS B  1 120 ? 65.348  14.003  26.560 1.00 17.85  ? 120  HIS B CA  1 
ATOM   1993  C  C   . HIS B  1 120 ? 66.010  13.359  27.772 1.00 21.14  ? 120  HIS B C   1 
ATOM   1994  O  O   . HIS B  1 120 ? 67.231  13.265  27.915 1.00 20.52  ? 120  HIS B O   1 
ATOM   1995  C  CB  . HIS B  1 120 ? 64.839  12.846  25.675 1.00 19.21  ? 120  HIS B CB  1 
ATOM   1996  C  CG  . HIS B  1 120 ? 63.767  13.292  24.720 1.00 18.01  ? 120  HIS B CG  1 
ATOM   1997  N  ND1 . HIS B  1 120 ? 62.419  13.224  24.998 1.00 17.70  ? 120  HIS B ND1 1 
ATOM   1998  C  CD2 . HIS B  1 120 ? 63.870  13.844  23.487 1.00 25.78  ? 120  HIS B CD2 1 
ATOM   1999  C  CE1 . HIS B  1 120 ? 61.720  13.691  23.963 1.00 20.36  ? 120  HIS B CE1 1 
ATOM   2000  N  NE2 . HIS B  1 120 ? 62.574  14.085  23.030 1.00 23.91  ? 120  HIS B NE2 1 
ATOM   2001  N  N   . GLU B  1 121 ? 65.128  12.875  28.631 1.00 22.12  ? 121  GLU B N   1 
ATOM   2002  C  CA  . GLU B  1 121 ? 65.469  12.192  29.877 1.00 21.70  ? 121  GLU B CA  1 
ATOM   2003  C  C   . GLU B  1 121 ? 66.318  10.956  29.712 1.00 20.87  ? 121  GLU B C   1 
ATOM   2004  O  O   . GLU B  1 121 ? 67.289  10.702  30.430 1.00 24.14  ? 121  GLU B O   1 
ATOM   2005  C  CB  . GLU B  1 121 ? 64.095  11.825  30.508 1.00 26.04  ? 121  GLU B CB  1 
ATOM   2006  C  CG  . GLU B  1 121 ? 64.236  10.845  31.659 1.00 30.17  ? 121  GLU B CG  1 
ATOM   2007  C  CD  . GLU B  1 121 ? 62.885  10.323  32.119 1.00 41.61  ? 121  GLU B CD  1 
ATOM   2008  O  OE1 . GLU B  1 121 ? 62.866  9.881   33.287 1.00 42.71  ? 121  GLU B OE1 1 
ATOM   2009  O  OE2 . GLU B  1 121 ? 61.880  10.347  31.371 1.00 34.51  ? 121  GLU B OE2 1 
ATOM   2010  N  N   . LYS B  1 122 ? 65.974  10.139  28.717 1.00 21.64  ? 122  LYS B N   1 
ATOM   2011  C  CA  . LYS B  1 122 ? 66.598  8.860   28.458 1.00 22.27  ? 122  LYS B CA  1 
ATOM   2012  C  C   . LYS B  1 122 ? 67.110  8.689   27.024 1.00 20.34  ? 122  LYS B C   1 
ATOM   2013  O  O   . LYS B  1 122 ? 66.847  9.546   26.172 1.00 21.12  ? 122  LYS B O   1 
ATOM   2014  C  CB  . LYS B  1 122 ? 65.558  7.730   28.661 1.00 31.40  ? 122  LYS B CB  1 
ATOM   2015  C  CG  . LYS B  1 122 ? 64.727  7.852   29.924 1.00 44.69  ? 122  LYS B CG  1 
ATOM   2016  C  CD  . LYS B  1 122 ? 64.119  6.521   30.336 1.00 47.55  ? 122  LYS B CD  1 
ATOM   2017  C  CE  . LYS B  1 122 ? 62.848  6.215   29.561 1.00 52.22  ? 122  LYS B CE  1 
ATOM   2018  N  NZ  . LYS B  1 122 ? 61.764  5.717   30.461 1.00 67.48  ? 122  LYS B NZ  1 
ATOM   2019  N  N   . ALA B  1 123 ? 67.766  7.571   26.781 1.00 21.74  ? 123  ALA B N   1 
ATOM   2020  C  CA  . ALA B  1 123 ? 68.251  7.252   25.437 1.00 23.74  ? 123  ALA B CA  1 
ATOM   2021  C  C   . ALA B  1 123 ? 67.090  7.017   24.468 1.00 25.20  ? 123  ALA B C   1 
ATOM   2022  O  O   . ALA B  1 123 ? 66.045  6.457   24.807 1.00 23.54  ? 123  ALA B O   1 
ATOM   2023  C  CB  . ALA B  1 123 ? 69.132  6.016   25.420 1.00 21.80  ? 123  ALA B CB  1 
ATOM   2024  N  N   . ASP B  1 124 ? 67.346  7.426   23.242 1.00 19.56  ? 124  ASP B N   1 
ATOM   2025  C  CA  . ASP B  1 124 ? 66.491  7.080   22.110 1.00 21.19  ? 124  ASP B CA  1 
ATOM   2026  C  C   . ASP B  1 124 ? 66.836  5.679   21.630 1.00 23.19  ? 124  ASP B C   1 
ATOM   2027  O  O   . ASP B  1 124 ? 68.018  5.419   21.360 1.00 20.51  ? 124  ASP B O   1 
ATOM   2028  C  CB  . ASP B  1 124 ? 66.733  8.123   21.024 1.00 20.05  ? 124  ASP B CB  1 
ATOM   2029  C  CG  . ASP B  1 124 ? 65.826  8.004   19.804 1.00 22.53  ? 124  ASP B CG  1 
ATOM   2030  O  OD1 . ASP B  1 124 ? 65.581  9.035   19.141 1.00 20.50  ? 124  ASP B OD1 1 
ATOM   2031  O  OD2 . ASP B  1 124 ? 65.377  6.886   19.488 1.00 21.55  ? 124  ASP B OD2 1 
ATOM   2032  N  N   . ASP B  1 125 ? 65.872  4.775   21.516 1.00 17.99  ? 125  ASP B N   1 
ATOM   2033  C  CA  . ASP B  1 125 ? 66.196  3.400   21.109 1.00 18.41  ? 125  ASP B CA  1 
ATOM   2034  C  C   . ASP B  1 125 ? 66.231  3.264   19.591 1.00 19.27  ? 125  ASP B C   1 
ATOM   2035  O  O   . ASP B  1 125 ? 66.424  2.171   19.071 1.00 21.19  ? 125  ASP B O   1 
ATOM   2036  C  CB  . ASP B  1 125 ? 65.243  2.374   21.721 1.00 22.93  ? 125  ASP B CB  1 
ATOM   2037  C  CG  . ASP B  1 125 ? 63.825  2.391   21.204 1.00 26.78  ? 125  ASP B CG  1 
ATOM   2038  O  OD1 . ASP B  1 125 ? 62.964  1.840   21.936 1.00 23.29  ? 125  ASP B OD1 1 
ATOM   2039  O  OD2 . ASP B  1 125 ? 63.503  2.909   20.105 1.00 24.04  ? 125  ASP B OD2 1 
ATOM   2040  N  N   . LEU B  1 126 ? 66.121  4.399   18.911 1.00 21.12  ? 126  LEU B N   1 
ATOM   2041  C  CA  . LEU B  1 126 ? 66.335  4.496   17.465 1.00 22.81  ? 126  LEU B CA  1 
ATOM   2042  C  C   . LEU B  1 126 ? 65.350  3.587   16.731 1.00 22.75  ? 126  LEU B C   1 
ATOM   2043  O  O   . LEU B  1 126 ? 65.612  3.120   15.620 1.00 23.04  ? 126  LEU B O   1 
ATOM   2044  C  CB  . LEU B  1 126 ? 67.785  4.187   17.078 1.00 20.30  ? 126  LEU B CB  1 
ATOM   2045  C  CG  . LEU B  1 126 ? 68.874  4.946   17.883 1.00 19.45  ? 126  LEU B CG  1 
ATOM   2046  C  CD1 . LEU B  1 126 ? 70.279  4.520   17.463 1.00 21.98  ? 126  LEU B CD1 1 
ATOM   2047  C  CD2 . LEU B  1 126 ? 68.704  6.445   17.728 1.00 19.43  ? 126  LEU B CD2 1 
ATOM   2048  N  N   . GLY B  1 127 ? 64.200  3.336   17.339 1.00 20.58  ? 127  GLY B N   1 
ATOM   2049  C  CA  . GLY B  1 127 ? 63.155  2.573   16.678 1.00 18.21  ? 127  GLY B CA  1 
ATOM   2050  C  C   . GLY B  1 127 ? 63.319  1.080   16.781 1.00 20.47  ? 127  GLY B C   1 
ATOM   2051  O  O   . GLY B  1 127 ? 62.589  0.330   16.122 1.00 21.62  ? 127  GLY B O   1 
ATOM   2052  N  N   . LYS B  1 128 ? 64.255  0.629   17.614 1.00 21.38  ? 128  LYS B N   1 
ATOM   2053  C  CA  . LYS B  1 128 ? 64.553  -0.797  17.738 1.00 21.78  ? 128  LYS B CA  1 
ATOM   2054  C  C   . LYS B  1 128 ? 64.027  -1.427  19.012 1.00 20.76  ? 128  LYS B C   1 
ATOM   2055  O  O   . LYS B  1 128 ? 64.509  -2.483  19.439 1.00 26.24  ? 128  LYS B O   1 
ATOM   2056  C  CB  . LYS B  1 128 ? 66.089  -0.990  17.696 1.00 18.51  ? 128  LYS B CB  1 
ATOM   2057  C  CG  . LYS B  1 128 ? 66.643  -0.625  16.321 1.00 22.43  ? 128  LYS B CG  1 
ATOM   2058  C  CD  . LYS B  1 128 ? 68.160  -0.478  16.362 1.00 32.26  ? 128  LYS B CD  1 
ATOM   2059  C  CE  . LYS B  1 128 ? 68.855  -1.434  15.421 1.00 42.88  ? 128  LYS B CE  1 
ATOM   2060  N  NZ  . LYS B  1 128 ? 70.320  -1.502  15.677 1.00 57.00  ? 128  LYS B NZ  1 
ATOM   2061  N  N   . GLY B  1 129 ? 63.068  -0.822  19.682 1.00 21.07  ? 129  GLY B N   1 
ATOM   2062  C  CA  . GLY B  1 129 ? 62.601  -1.316  20.964 1.00 22.71  ? 129  GLY B CA  1 
ATOM   2063  C  C   . GLY B  1 129 ? 61.451  -2.305  20.842 1.00 27.54  ? 129  GLY B C   1 
ATOM   2064  O  O   . GLY B  1 129 ? 61.032  -2.848  21.873 1.00 23.95  ? 129  GLY B O   1 
ATOM   2065  N  N   . GLY B  1 130 ? 60.966  -2.528  19.617 1.00 20.19  ? 130  GLY B N   1 
ATOM   2066  C  CA  . GLY B  1 130 ? 59.930  -3.516  19.406 1.00 22.39  ? 130  GLY B CA  1 
ATOM   2067  C  C   . GLY B  1 130 ? 58.547  -3.220  19.940 1.00 29.74  ? 130  GLY B C   1 
ATOM   2068  O  O   . GLY B  1 130 ? 57.746  -4.171  20.024 1.00 25.00  ? 130  GLY B O   1 
ATOM   2069  N  N   . ASN B  1 131 ? 58.176  -2.003  20.308 1.00 26.02  ? 131  ASN B N   1 
ATOM   2070  C  CA  . ASN B  1 131 ? 56.806  -1.642  20.687 1.00 25.61  ? 131  ASN B CA  1 
ATOM   2071  C  C   . ASN B  1 131 ? 56.366  -0.443  19.874 1.00 31.64  ? 131  ASN B C   1 
ATOM   2072  O  O   . ASN B  1 131 ? 57.142  0.200   19.152 1.00 27.55  ? 131  ASN B O   1 
ATOM   2073  C  CB  . ASN B  1 131 ? 56.668  -1.379  22.184 1.00 34.97  ? 131  ASN B CB  1 
ATOM   2074  C  CG  . ASN B  1 131 ? 57.617  -0.375  22.789 1.00 34.63  ? 131  ASN B CG  1 
ATOM   2075  O  OD1 . ASN B  1 131 ? 58.180  0.460   22.082 1.00 27.49  ? 131  ASN B OD1 1 
ATOM   2076  N  ND2 . ASN B  1 131 ? 57.801  -0.405  24.103 1.00 32.98  ? 131  ASN B ND2 1 
ATOM   2077  N  N   . GLU B  1 132 ? 55.074  -0.089  19.946 1.00 29.47  ? 132  GLU B N   1 
ATOM   2078  C  CA  . GLU B  1 132 ? 54.662  1.077   19.171 1.00 27.70  ? 132  GLU B CA  1 
ATOM   2079  C  C   . GLU B  1 132 ? 55.321  2.362   19.621 1.00 25.96  ? 132  GLU B C   1 
ATOM   2080  O  O   . GLU B  1 132 ? 55.556  3.303   18.862 1.00 29.81  ? 132  GLU B O   1 
ATOM   2081  C  CB  . GLU B  1 132 ? 53.138  1.283   19.336 1.00 39.42  ? 132  GLU B CB  1 
ATOM   2082  C  CG  . GLU B  1 132 ? 52.375  1.238   18.026 1.00 57.91  ? 132  GLU B CG  1 
ATOM   2083  C  CD  . GLU B  1 132 ? 50.870  1.273   18.227 1.00 70.38  ? 132  GLU B CD  1 
ATOM   2084  O  OE1 . GLU B  1 132 ? 50.219  0.243   17.956 1.00 79.38  ? 132  GLU B OE1 1 
ATOM   2085  O  OE2 . GLU B  1 132 ? 50.343  2.320   18.655 1.00 84.27  ? 132  GLU B OE2 1 
ATOM   2086  N  N   . GLU B  1 133 ? 55.591  2.444   20.933 1.00 25.25  ? 133  GLU B N   1 
ATOM   2087  C  CA  . GLU B  1 133 ? 56.231  3.683   21.379 1.00 24.41  ? 133  GLU B CA  1 
ATOM   2088  C  C   . GLU B  1 133 ? 57.601  3.848   20.717 1.00 22.76  ? 133  GLU B C   1 
ATOM   2089  O  O   . GLU B  1 133 ? 57.952  4.995   20.400 1.00 23.80  ? 133  GLU B O   1 
ATOM   2090  C  CB  . GLU B  1 133 ? 56.347  3.730   22.903 1.00 29.86  ? 133  GLU B CB  1 
ATOM   2091  C  CG  . GLU B  1 133 ? 56.692  5.098   23.466 1.00 37.67  ? 133  GLU B CG  1 
ATOM   2092  C  CD  . GLU B  1 133 ? 55.625  6.153   23.287 1.00 49.19  ? 133  GLU B CD  1 
ATOM   2093  O  OE1 . GLU B  1 133 ? 55.964  7.267   22.819 1.00 44.02  ? 133  GLU B OE1 1 
ATOM   2094  O  OE2 . GLU B  1 133 ? 54.445  5.905   23.608 1.00 46.38  ? 133  GLU B OE2 1 
ATOM   2095  N  N   . SER B  1 134 ? 58.356  2.786   20.514 1.00 23.63  ? 134  SER B N   1 
ATOM   2096  C  CA  . SER B  1 134 ? 59.679  2.876   19.877 1.00 20.93  ? 134  SER B CA  1 
ATOM   2097  C  C   . SER B  1 134 ? 59.596  3.499   18.488 1.00 26.33  ? 134  SER B C   1 
ATOM   2098  O  O   . SER B  1 134 ? 60.456  4.290   18.100 1.00 21.26  ? 134  SER B O   1 
ATOM   2099  C  CB  . SER B  1 134 ? 60.307  1.485   19.771 1.00 22.50  ? 134  SER B CB  1 
ATOM   2100  O  OG  . SER B  1 134 ? 61.571  1.596   19.103 1.00 19.66  ? 134  SER B OG  1 
ATOM   2101  N  N   . THR B  1 135 ? 58.552  3.178   17.696 1.00 22.52  ? 135  THR B N   1 
ATOM   2102  C  CA  . THR B  1 135 ? 58.509  3.789   16.357 1.00 20.73  ? 135  THR B CA  1 
ATOM   2103  C  C   . THR B  1 135 ? 57.712  5.089   16.334 1.00 22.49  ? 135  THR B C   1 
ATOM   2104  O  O   . THR B  1 135 ? 57.405  5.610   15.248 1.00 21.35  ? 135  THR B O   1 
ATOM   2105  C  CB  . THR B  1 135 ? 57.977  2.800   15.306 1.00 37.14  ? 135  THR B CB  1 
ATOM   2106  O  OG1 . THR B  1 135 ? 56.871  2.083   15.835 1.00 39.25  ? 135  THR B OG1 1 
ATOM   2107  C  CG2 . THR B  1 135 ? 59.063  1.769   14.977 1.00 30.35  ? 135  THR B CG2 1 
ATOM   2108  N  N   . LYS B  1 136 ? 57.441  5.675   17.497 1.00 24.08  ? 136  LYS B N   1 
ATOM   2109  C  CA  . LYS B  1 136 ? 56.931  7.036   17.615 1.00 26.09  ? 136  LYS B CA  1 
ATOM   2110  C  C   . LYS B  1 136 ? 57.944  8.005   18.235 1.00 26.25  ? 136  LYS B C   1 
ATOM   2111  O  O   . LYS B  1 136 ? 58.199  9.092   17.704 1.00 25.16  ? 136  LYS B O   1 
ATOM   2112  C  CB  . LYS B  1 136 ? 55.669  7.099   18.487 1.00 23.27  ? 136  LYS B CB  1 
ATOM   2113  C  CG  . LYS B  1 136 ? 54.547  6.178   18.027 1.00 38.67  ? 136  LYS B CG  1 
ATOM   2114  C  CD  . LYS B  1 136 ? 53.275  6.422   18.839 1.00 53.74  ? 136  LYS B CD  1 
ATOM   2115  C  CE  . LYS B  1 136 ? 52.049  6.331   17.946 1.00 66.79  ? 136  LYS B CE  1 
ATOM   2116  N  NZ  . LYS B  1 136 ? 51.018  7.361   18.265 1.00 89.39  ? 136  LYS B NZ  1 
ATOM   2117  N  N   . THR B  1 137 ? 58.509  7.647   19.386 1.00 23.52  ? 137  THR B N   1 
ATOM   2118  C  CA  . THR B  1 137 ? 59.383  8.547   20.130 1.00 24.00  ? 137  THR B CA  1 
ATOM   2119  C  C   . THR B  1 137 ? 60.715  7.887   20.464 1.00 24.00  ? 137  THR B C   1 
ATOM   2120  O  O   . THR B  1 137 ? 61.551  8.541   21.093 1.00 27.71  ? 137  THR B O   1 
ATOM   2121  C  CB  . THR B  1 137 ? 58.765  8.980   21.483 1.00 32.21  ? 137  THR B CB  1 
ATOM   2122  O  OG1 . THR B  1 137 ? 58.725  7.812   22.333 1.00 27.69  ? 137  THR B OG1 1 
ATOM   2123  C  CG2 . THR B  1 137 ? 57.334  9.492   21.314 1.00 27.15  ? 137  THR B CG2 1 
ATOM   2124  N  N   . GLY B  1 138 ? 60.906  6.615   20.120 1.00 20.65  ? 138  GLY B N   1 
ATOM   2125  C  CA  . GLY B  1 138 ? 62.153  5.946   20.500 1.00 19.51  ? 138  GLY B CA  1 
ATOM   2126  C  C   . GLY B  1 138 ? 62.231  5.693   21.999 1.00 21.29  ? 138  GLY B C   1 
ATOM   2127  O  O   . GLY B  1 138 ? 63.303  5.332   22.498 1.00 22.55  ? 138  GLY B O   1 
ATOM   2128  N  N   . ASN B  1 139 ? 61.144  5.867   22.744 1.00 24.87  ? 139  ASN B N   1 
ATOM   2129  C  CA  . ASN B  1 139 ? 61.128  5.627   24.186 1.00 22.87  ? 139  ASN B CA  1 
ATOM   2130  C  C   . ASN B  1 139 ? 62.147  6.482   24.940 1.00 24.99  ? 139  ASN B C   1 
ATOM   2131  O  O   . ASN B  1 139 ? 62.744  6.047   25.927 1.00 24.09  ? 139  ASN B O   1 
ATOM   2132  C  CB  . ASN B  1 139 ? 61.428  4.176   24.499 1.00 22.54  ? 139  ASN B CB  1 
ATOM   2133  C  CG  . ASN B  1 139 ? 60.276  3.254   24.169 1.00 29.90  ? 139  ASN B CG  1 
ATOM   2134  O  OD1 . ASN B  1 139 ? 59.251  3.307   24.840 1.00 31.64  ? 139  ASN B OD1 1 
ATOM   2135  N  ND2 . ASN B  1 139 ? 60.428  2.416   23.147 1.00 26.25  ? 139  ASN B ND2 1 
ATOM   2136  N  N   . ALA B  1 140 ? 62.337  7.727   24.514 1.00 22.11  ? 140  ALA B N   1 
ATOM   2137  C  CA  . ALA B  1 140 ? 63.351  8.581   25.125 1.00 23.51  ? 140  ALA B CA  1 
ATOM   2138  C  C   . ALA B  1 140 ? 62.850  9.299   26.372 1.00 23.16  ? 140  ALA B C   1 
ATOM   2139  O  O   . ALA B  1 140 ? 63.580  10.091  26.985 1.00 22.73  ? 140  ALA B O   1 
ATOM   2140  C  CB  . ALA B  1 140 ? 63.840  9.588   24.083 1.00 23.40  ? 140  ALA B CB  1 
ATOM   2141  N  N   . GLY B  1 141 ? 61.590  9.050   26.757 1.00 25.03  ? 141  GLY B N   1 
ATOM   2142  C  CA  . GLY B  1 141 ? 61.092  9.658   27.980 1.00 24.77  ? 141  GLY B CA  1 
ATOM   2143  C  C   . GLY B  1 141 ? 60.841  11.132  27.936 1.00 24.64  ? 141  GLY B C   1 
ATOM   2144  O  O   . GLY B  1 141 ? 60.593  11.768  26.896 1.00 23.21  ? 141  GLY B O   1 
ATOM   2145  N  N   . SER B  1 142 ? 60.847  11.777  29.112 1.00 22.00  ? 142  SER B N   1 
ATOM   2146  C  CA  . SER B  1 142 ? 60.444  13.168  29.155 1.00 22.57  ? 142  SER B CA  1 
ATOM   2147  C  C   . SER B  1 142 ? 61.422  14.163  28.525 1.00 21.92  ? 142  SER B C   1 
ATOM   2148  O  O   . SER B  1 142 ? 62.571  13.867  28.209 1.00 21.03  ? 142  SER B O   1 
ATOM   2149  C  CB  . SER B  1 142 ? 60.210  13.528  30.646 1.00 28.75  ? 142  SER B CB  1 
ATOM   2150  O  OG  . SER B  1 142 ? 61.509  13.706  31.210 1.00 33.80  ? 142  SER B OG  1 
ATOM   2151  N  N   . ARG B  1 143 ? 60.918  15.373  28.329 1.00 20.65  ? 143  ARG B N   1 
ATOM   2152  C  CA  . ARG B  1 143 ? 61.595  16.496  27.698 1.00 21.99  ? 143  ARG B CA  1 
ATOM   2153  C  C   . ARG B  1 143 ? 62.313  17.337  28.745 1.00 29.99  ? 143  ARG B C   1 
ATOM   2154  O  O   . ARG B  1 143 ? 61.687  18.064  29.520 1.00 27.42  ? 143  ARG B O   1 
ATOM   2155  C  CB  . ARG B  1 143 ? 60.579  17.307  26.894 1.00 23.29  ? 143  ARG B CB  1 
ATOM   2156  C  CG  . ARG B  1 143 ? 59.761  16.359  25.997 1.00 22.67  ? 143  ARG B CG  1 
ATOM   2157  C  CD  . ARG B  1 143 ? 58.734  17.162  25.204 1.00 24.04  ? 143  ARG B CD  1 
ATOM   2158  N  NE  . ARG B  1 143 ? 57.973  16.272  24.332 1.00 24.53  ? 143  ARG B NE  1 
ATOM   2159  C  CZ  . ARG B  1 143 ? 57.173  16.553  23.319 1.00 28.50  ? 143  ARG B CZ  1 
ATOM   2160  N  NH1 . ARG B  1 143 ? 56.584  15.537  22.669 1.00 21.53  ? 143  ARG B NH1 1 
ATOM   2161  N  NH2 . ARG B  1 143 ? 56.965  17.807  22.959 1.00 23.34  ? 143  ARG B NH2 1 
ATOM   2162  N  N   . LEU B  1 144 ? 63.649  17.238  28.789 1.00 22.30  ? 144  LEU B N   1 
ATOM   2163  C  CA  . LEU B  1 144 ? 64.310  17.979  29.879 1.00 20.60  ? 144  LEU B CA  1 
ATOM   2164  C  C   . LEU B  1 144 ? 64.564  19.436  29.556 1.00 23.49  ? 144  LEU B C   1 
ATOM   2165  O  O   . LEU B  1 144 ? 64.570  20.321  30.418 1.00 26.64  ? 144  LEU B O   1 
ATOM   2166  C  CB  . LEU B  1 144 ? 65.657  17.322  30.195 1.00 18.61  ? 144  LEU B CB  1 
ATOM   2167  C  CG  . LEU B  1 144 ? 65.629  15.849  30.593 1.00 26.50  ? 144  LEU B CG  1 
ATOM   2168  C  CD1 . LEU B  1 144 ? 67.010  15.364  31.003 1.00 28.77  ? 144  LEU B CD1 1 
ATOM   2169  C  CD2 . LEU B  1 144 ? 64.616  15.641  31.717 1.00 26.58  ? 144  LEU B CD2 1 
ATOM   2170  N  N   . ALA B  1 145 ? 64.836  19.734  28.281 1.00 17.93  ? 145  ALA B N   1 
ATOM   2171  C  CA  . ALA B  1 145 ? 65.053  21.107  27.900 1.00 17.60  ? 145  ALA B CA  1 
ATOM   2172  C  C   . ALA B  1 145 ? 64.758  21.281  26.406 1.00 20.20  ? 145  ALA B C   1 
ATOM   2173  O  O   . ALA B  1 145 ? 64.843  20.304  25.657 1.00 21.27  ? 145  ALA B O   1 
ATOM   2174  C  CB  . ALA B  1 145 ? 66.489  21.550  28.172 1.00 19.05  ? 145  ALA B CB  1 
ATOM   2175  N  N   . CYS B  1 146 ? 64.451  22.502  26.029 1.00 19.60  ? 146  CYS B N   1 
ATOM   2176  C  CA  . CYS B  1 146 ? 64.083  22.717  24.627 1.00 20.35  ? 146  CYS B CA  1 
ATOM   2177  C  C   . CYS B  1 146 ? 64.272  24.167  24.291 1.00 23.08  ? 146  CYS B C   1 
ATOM   2178  O  O   . CYS B  1 146 ? 64.436  25.022  25.169 1.00 21.28  ? 146  CYS B O   1 
ATOM   2179  C  CB  A CYS B  1 146 ? 62.641  22.278  24.366 0.43 22.69  ? 146  CYS B CB  1 
ATOM   2180  C  CB  B CYS B  1 146 ? 62.638  22.236  24.452 0.57 24.24  ? 146  CYS B CB  1 
ATOM   2181  S  SG  A CYS B  1 146 ? 61.452  23.078  25.474 0.43 33.82  ? 146  CYS B SG  1 
ATOM   2182  S  SG  B CYS B  1 146 ? 61.381  23.348  25.118 0.57 23.10  ? 146  CYS B SG  1 
ATOM   2183  N  N   . GLY B  1 147 ? 64.293  24.470  22.993 1.00 21.76  ? 147  GLY B N   1 
ATOM   2184  C  CA  . GLY B  1 147 ? 64.423  25.872  22.601 1.00 20.56  ? 147  GLY B CA  1 
ATOM   2185  C  C   . GLY B  1 147 ? 63.914  26.011  21.166 1.00 20.44  ? 147  GLY B C   1 
ATOM   2186  O  O   . GLY B  1 147 ? 63.962  25.029  20.417 1.00 20.30  ? 147  GLY B O   1 
ATOM   2187  N  N   . VAL B  1 148 ? 63.450  27.209  20.809 1.00 19.67  ? 148  VAL B N   1 
ATOM   2188  C  CA  . VAL B  1 148 ? 63.047  27.403  19.416 1.00 19.96  ? 148  VAL B CA  1 
ATOM   2189  C  C   . VAL B  1 148 ? 64.268  27.629  18.526 1.00 20.53  ? 148  VAL B C   1 
ATOM   2190  O  O   . VAL B  1 148 ? 65.170  28.387  18.901 1.00 22.78  ? 148  VAL B O   1 
ATOM   2191  C  CB  . VAL B  1 148 ? 62.094  28.608  19.289 1.00 22.02  ? 148  VAL B CB  1 
ATOM   2192  C  CG1 . VAL B  1 148 ? 61.643  28.747  17.834 1.00 20.19  ? 148  VAL B CG1 1 
ATOM   2193  C  CG2 . VAL B  1 148 ? 60.896  28.450  20.220 1.00 22.41  ? 148  VAL B CG2 1 
ATOM   2194  N  N   . ILE B  1 149 ? 64.325  27.022  17.338 1.00 18.50  ? 149  ILE B N   1 
ATOM   2195  C  CA  . ILE B  1 149 ? 65.481  27.210  16.457 1.00 20.08  ? 149  ILE B CA  1 
ATOM   2196  C  C   . ILE B  1 149 ? 65.404  28.501  15.676 1.00 21.80  ? 149  ILE B C   1 
ATOM   2197  O  O   . ILE B  1 149 ? 64.449  28.719  14.927 1.00 23.32  ? 149  ILE B O   1 
ATOM   2198  C  CB  . ILE B  1 149 ? 65.622  25.976  15.535 1.00 19.90  ? 149  ILE B CB  1 
ATOM   2199  C  CG1 . ILE B  1 149 ? 65.773  24.698  16.346 1.00 17.30  ? 149  ILE B CG1 1 
ATOM   2200  C  CG2 . ILE B  1 149 ? 66.795  26.168  14.574 1.00 18.32  ? 149  ILE B CG2 1 
ATOM   2201  C  CD1 . ILE B  1 149 ? 65.548  23.390  15.594 1.00 21.02  ? 149  ILE B CD1 1 
ATOM   2202  N  N   . GLY B  1 150 ? 66.383  29.394  15.852 1.00 19.43  ? 150  GLY B N   1 
ATOM   2203  C  CA  . GLY B  1 150 ? 66.265  30.700  15.223 1.00 17.26  ? 150  GLY B CA  1 
ATOM   2204  C  C   . GLY B  1 150 ? 67.332  30.940  14.189 1.00 21.41  ? 150  GLY B C   1 
ATOM   2205  O  O   . GLY B  1 150 ? 68.379  30.295  14.218 1.00 19.50  ? 150  GLY B O   1 
ATOM   2206  N  N   . ILE B  1 151 ? 67.108  31.896  13.296 1.00 21.01  ? 151  ILE B N   1 
ATOM   2207  C  CA  . ILE B  1 151 ? 68.107  32.297  12.300 1.00 20.72  ? 151  ILE B CA  1 
ATOM   2208  C  C   . ILE B  1 151 ? 69.275  33.005  12.944 1.00 19.69  ? 151  ILE B C   1 
ATOM   2209  O  O   . ILE B  1 151 ? 69.046  33.856  13.808 1.00 21.92  ? 151  ILE B O   1 
ATOM   2210  C  CB  . ILE B  1 151 ? 67.412  33.207  11.253 1.00 26.85  ? 151  ILE B CB  1 
ATOM   2211  C  CG1 . ILE B  1 151 ? 66.284  32.470  10.527 1.00 31.93  ? 151  ILE B CG1 1 
ATOM   2212  C  CG2 . ILE B  1 151 ? 68.398  33.788  10.262 1.00 32.97  ? 151  ILE B CG2 1 
ATOM   2213  C  CD1 . ILE B  1 151 ? 65.309  33.377  9.798  1.00 48.86  ? 151  ILE B CD1 1 
ATOM   2214  N  N   . ALA B  1 152 ? 70.524  32.692  12.566 1.00 18.06  ? 152  ALA B N   1 
ATOM   2215  C  CA  . ALA B  1 152 ? 71.674  33.310  13.201 1.00 21.26  ? 152  ALA B CA  1 
ATOM   2216  C  C   . ALA B  1 152 ? 72.606  33.891  12.143 1.00 24.30  ? 152  ALA B C   1 
ATOM   2217  O  O   . ALA B  1 152 ? 72.345  33.702  10.944 1.00 27.08  ? 152  ALA B O   1 
ATOM   2218  C  CB  . ALA B  1 152 ? 72.467  32.281  14.012 1.00 24.40  ? 152  ALA B CB  1 
ATOM   2219  N  N   . GLN B  1 153 ? 73.658  34.563  12.595 1.00 26.48  ? 153  GLN B N   1 
ATOM   2220  C  CA  . GLN B  1 153 ? 74.702  35.019  11.656 1.00 40.92  ? 153  GLN B CA  1 
ATOM   2221  C  C   . GLN B  1 153 ? 76.089  34.563  12.104 1.00 47.94  ? 153  GLN B C   1 
ATOM   2222  O  O   . GLN B  1 153 ? 76.194  34.023  13.233 1.00 42.42  ? 153  GLN B O   1 
ATOM   2223  C  CB  . GLN B  1 153 ? 74.720  36.550  11.508 1.00 38.05  ? 153  GLN B CB  1 
ATOM   2224  C  CG  . GLN B  1 153 ? 74.937  37.259  12.829 1.00 47.35  ? 153  GLN B CG  1 
ATOM   2225  C  CD  . GLN B  1 153 ? 75.214  38.746  12.760 1.00 44.14  ? 153  GLN B CD  1 
ATOM   2226  O  OE1 . GLN B  1 153 ? 75.706  39.289  11.782 1.00 39.52  ? 153  GLN B OE1 1 
ATOM   2227  N  NE2 . GLN B  1 153 ? 74.876  39.443  13.844 1.00 28.07  ? 153  GLN B NE2 1 
ATOM   2228  O  OXT . GLN B  1 153 ? 77.066  34.765  11.340 1.00 49.50  ? 153  GLN B OXT 1 
ATOM   2229  N  N   . ALA C  1 1   ? 111.237 9.648   6.890  1.00 53.66  ? 1    ALA C N   1 
ATOM   2230  C  CA  . ALA C  1 1   ? 111.869 8.530   7.576  1.00 54.56  ? 1    ALA C CA  1 
ATOM   2231  C  C   . ALA C  1 1   ? 110.848 7.604   8.235  1.00 56.26  ? 1    ALA C C   1 
ATOM   2232  O  O   . ALA C  1 1   ? 109.974 7.999   9.006  1.00 73.27  ? 1    ALA C O   1 
ATOM   2233  C  CB  . ALA C  1 1   ? 112.852 9.053   8.614  1.00 48.90  ? 1    ALA C CB  1 
ATOM   2234  N  N   . THR C  1 2   ? 110.971 6.325   7.920  1.00 46.86  ? 2    THR C N   1 
ATOM   2235  C  CA  . THR C  1 2   ? 110.218 5.270   8.601  1.00 40.83  ? 2    THR C CA  1 
ATOM   2236  C  C   . THR C  1 2   ? 110.832 5.057   9.976  1.00 41.14  ? 2    THR C C   1 
ATOM   2237  O  O   . THR C  1 2   ? 112.066 5.036   10.082 1.00 37.72  ? 2    THR C O   1 
ATOM   2238  C  CB  . THR C  1 2   ? 110.244 3.999   7.746  1.00 40.38  ? 2    THR C CB  1 
ATOM   2239  O  OG1 . THR C  1 2   ? 109.890 4.341   6.388  1.00 51.01  ? 2    THR C OG1 1 
ATOM   2240  C  CG2 . THR C  1 2   ? 109.215 2.995   8.202  1.00 37.85  ? 2    THR C CG2 1 
ATOM   2241  N  N   . LYS C  1 3   ? 110.025 4.930   11.018 1.00 33.36  ? 3    LYS C N   1 
ATOM   2242  C  CA  . LYS C  1 3   ? 110.532 4.614   12.346 1.00 30.94  ? 3    LYS C CA  1 
ATOM   2243  C  C   . LYS C  1 3   ? 109.841 3.389   12.948 1.00 38.19  ? 3    LYS C C   1 
ATOM   2244  O  O   . LYS C  1 3   ? 108.657 3.142   12.702 1.00 29.83  ? 3    LYS C O   1 
ATOM   2245  C  CB  . LYS C  1 3   ? 110.356 5.810   13.275 1.00 36.16  ? 3    LYS C CB  1 
ATOM   2246  C  CG  . LYS C  1 3   ? 110.912 7.109   12.704 1.00 45.89  ? 3    LYS C CG  1 
ATOM   2247  C  CD  . LYS C  1 3   ? 110.734 8.259   13.677 1.00 56.37  ? 3    LYS C CD  1 
ATOM   2248  C  CE  . LYS C  1 3   ? 110.664 9.591   12.937 1.00 69.18  ? 3    LYS C CE  1 
ATOM   2249  N  NZ  . LYS C  1 3   ? 110.295 10.713  13.847 1.00 72.30  ? 3    LYS C NZ  1 
ATOM   2250  N  N   . ALA C  1 4   ? 110.594 2.625   13.731 1.00 32.01  ? 4    ALA C N   1 
ATOM   2251  C  CA  . ALA C  1 4   ? 110.064 1.509   14.521 1.00 24.38  ? 4    ALA C CA  1 
ATOM   2252  C  C   . ALA C  1 4   ? 110.564 1.584   15.958 1.00 33.27  ? 4    ALA C C   1 
ATOM   2253  O  O   . ALA C  1 4   ? 111.457 2.348   16.344 1.00 29.18  ? 4    ALA C O   1 
ATOM   2254  C  CB  . ALA C  1 4   ? 110.371 0.173   13.905 1.00 24.66  ? 4    ALA C CB  1 
ATOM   2255  N  N   . VAL C  1 5   ? 109.943 0.781   16.821 1.00 35.71  ? 5    VAL C N   1 
ATOM   2256  C  CA  . VAL C  1 5   ? 110.371 0.827   18.238 1.00 28.24  ? 5    VAL C CA  1 
ATOM   2257  C  C   . VAL C  1 5   ? 110.161 -0.569  18.799 1.00 29.13  ? 5    VAL C C   1 
ATOM   2258  O  O   . VAL C  1 5   ? 109.364 -1.359  18.284 1.00 26.46  ? 5    VAL C O   1 
ATOM   2259  C  CB  . VAL C  1 5   ? 109.655 1.907   19.041 1.00 33.41  ? 5    VAL C CB  1 
ATOM   2260  C  CG1 . VAL C  1 5   ? 108.163 1.584   19.203 1.00 28.03  ? 5    VAL C CG1 1 
ATOM   2261  C  CG2 . VAL C  1 5   ? 110.294 2.099   20.420 1.00 31.22  ? 5    VAL C CG2 1 
ATOM   2262  N  N   . CYS C  1 6   ? 110.926 -0.920  19.837 1.00 27.65  ? 6    CYS C N   1 
ATOM   2263  C  CA  . CYS C  1 6   ? 110.797 -2.255  20.416 1.00 28.95  ? 6    CYS C CA  1 
ATOM   2264  C  C   . CYS C  1 6   ? 111.092 -2.125  21.921 1.00 41.79  ? 6    CYS C C   1 
ATOM   2265  O  O   . CYS C  1 6   ? 112.104 -1.499  22.287 1.00 26.83  ? 6    CYS C O   1 
ATOM   2266  C  CB  . CYS C  1 6   ? 111.722 -3.267  19.755 1.00 31.62  ? 6    CYS C CB  1 
ATOM   2267  S  SG  . CYS C  1 6   ? 111.660 -4.943  20.460 1.00 31.33  ? 6    CYS C SG  1 
ATOM   2268  N  N   . VAL C  1 7   ? 110.212 -2.714  22.719 1.00 28.41  ? 7    VAL C N   1 
ATOM   2269  C  CA  . VAL C  1 7   ? 110.357 -2.782  24.176 1.00 29.58  ? 7    VAL C CA  1 
ATOM   2270  C  C   . VAL C  1 7   ? 110.765 -4.195  24.555 1.00 32.47  ? 7    VAL C C   1 
ATOM   2271  O  O   . VAL C  1 7   ? 109.974 -5.140  24.430 1.00 26.17  ? 7    VAL C O   1 
ATOM   2272  C  CB  . VAL C  1 7   ? 109.052 -2.347  24.880 1.00 28.84  ? 7    VAL C CB  1 
ATOM   2273  C  CG1 . VAL C  1 7   ? 109.219 -2.422  26.396 1.00 31.51  ? 7    VAL C CG1 1 
ATOM   2274  C  CG2 . VAL C  1 7   ? 108.653 -0.929  24.502 1.00 24.40  ? 7    VAL C CG2 1 
ATOM   2275  N  N   . LEU C  1 8   ? 112.012 -4.402  25.017 1.00 27.18  ? 8    LEU C N   1 
ATOM   2276  C  CA  . LEU C  1 8   ? 112.486 -5.718  25.387 1.00 23.38  ? 8    LEU C CA  1 
ATOM   2277  C  C   . LEU C  1 8   ? 112.156 -6.120  26.829 1.00 25.24  ? 8    LEU C C   1 
ATOM   2278  O  O   . LEU C  1 8   ? 112.458 -5.391  27.769 1.00 28.64  ? 8    LEU C O   1 
ATOM   2279  C  CB  . LEU C  1 8   ? 114.025 -5.773  25.263 1.00 26.59  ? 8    LEU C CB  1 
ATOM   2280  C  CG  . LEU C  1 8   ? 114.569 -5.386  23.875 1.00 29.54  ? 8    LEU C CG  1 
ATOM   2281  C  CD1 . LEU C  1 8   ? 115.985 -4.853  24.002 1.00 48.16  ? 8    LEU C CD1 1 
ATOM   2282  C  CD2 . LEU C  1 8   ? 114.520 -6.572  22.935 1.00 28.26  ? 8    LEU C CD2 1 
ATOM   2283  N  N   . LYS C  1 9   ? 111.553 -7.282  27.022 1.00 27.27  ? 9    LYS C N   1 
ATOM   2284  C  CA  . LYS C  1 9   ? 111.204 -7.746  28.366 1.00 27.71  ? 9    LYS C CA  1 
ATOM   2285  C  C   . LYS C  1 9   ? 111.430 -9.234  28.432 1.00 22.36  ? 9    LYS C C   1 
ATOM   2286  O  O   . LYS C  1 9   ? 111.341 -9.942  27.428 1.00 25.62  ? 9    LYS C O   1 
ATOM   2287  C  CB  . LYS C  1 9   ? 109.743 -7.470  28.739 1.00 33.02  ? 9    LYS C CB  1 
ATOM   2288  C  CG  . LYS C  1 9   ? 109.374 -6.002  28.649 1.00 37.34  ? 9    LYS C CG  1 
ATOM   2289  C  CD  . LYS C  1 9   ? 107.898 -5.793  29.013 1.00 39.44  ? 9    LYS C CD  1 
ATOM   2290  C  CE  . LYS C  1 9   ? 107.679 -4.300  29.249 1.00 47.38  ? 9    LYS C CE  1 
ATOM   2291  N  NZ  . LYS C  1 9   ? 106.292 -3.876  28.919 1.00 58.01  ? 9    LYS C NZ  1 
ATOM   2292  N  N   . GLY C  1 10  ? 111.704 -9.745  29.638 1.00 25.05  ? 10   GLY C N   1 
ATOM   2293  C  CA  . GLY C  1 10  ? 111.740 -11.190 29.802 1.00 23.57  ? 10   GLY C CA  1 
ATOM   2294  C  C   . GLY C  1 10  ? 111.345 -11.576 31.232 1.00 31.04  ? 10   GLY C C   1 
ATOM   2295  O  O   . GLY C  1 10  ? 110.778 -10.743 31.945 1.00 34.22  ? 10   GLY C O   1 
ATOM   2296  N  N   . ASP C  1 11  ? 111.635 -12.797 31.652 1.00 36.97  ? 11   ASP C N   1 
ATOM   2297  C  CA  . ASP C  1 11  ? 111.289 -13.226 33.009 1.00 40.97  ? 11   ASP C CA  1 
ATOM   2298  C  C   . ASP C  1 11  ? 112.270 -12.712 34.054 1.00 42.81  ? 11   ASP C C   1 
ATOM   2299  O  O   . ASP C  1 11  ? 111.998 -12.750 35.259 1.00 48.40  ? 11   ASP C O   1 
ATOM   2300  C  CB  . ASP C  1 11  ? 111.238 -14.752 33.069 1.00 45.16  ? 11   ASP C CB  1 
ATOM   2301  C  CG  . ASP C  1 11  ? 110.134 -15.337 32.208 1.00 54.57  ? 11   ASP C CG  1 
ATOM   2302  O  OD1 . ASP C  1 11  ? 110.384 -16.349 31.518 1.00 62.56  ? 11   ASP C OD1 1 
ATOM   2303  O  OD2 . ASP C  1 11  ? 109.015 -14.784 32.230 1.00 73.47  ? 11   ASP C OD2 1 
ATOM   2304  N  N   . GLY C  1 12  ? 113.425 -12.228 33.604 1.00 30.99  ? 12   GLY C N   1 
ATOM   2305  C  CA  . GLY C  1 12  ? 114.451 -11.727 34.509 1.00 29.99  ? 12   GLY C CA  1 
ATOM   2306  C  C   . GLY C  1 12  ? 114.602 -10.232 34.480 1.00 29.84  ? 12   GLY C C   1 
ATOM   2307  O  O   . GLY C  1 12  ? 113.701 -9.469  34.138 1.00 31.13  ? 12   GLY C O   1 
ATOM   2308  N  N   . PRO C  1 13  ? 115.779 -9.726  34.862 1.00 26.79  ? 13   PRO C N   1 
ATOM   2309  C  CA  . PRO C  1 13  ? 116.011 -8.291  34.946 1.00 30.33  ? 13   PRO C CA  1 
ATOM   2310  C  C   . PRO C  1 13  ? 116.367 -7.599  33.621 1.00 23.12  ? 13   PRO C C   1 
ATOM   2311  O  O   . PRO C  1 13  ? 116.423 -6.373  33.625 1.00 32.64  ? 13   PRO C O   1 
ATOM   2312  C  CB  . PRO C  1 13  ? 117.248 -8.202  35.859 1.00 35.29  ? 13   PRO C CB  1 
ATOM   2313  C  CG  . PRO C  1 13  ? 117.929 -9.514  35.720 1.00 32.00  ? 13   PRO C CG  1 
ATOM   2314  C  CD  . PRO C  1 13  ? 116.944 -10.546 35.249 1.00 29.76  ? 13   PRO C CD  1 
ATOM   2315  N  N   . VAL C  1 14  ? 116.561 -8.380  32.552 1.00 31.79  ? 14   VAL C N   1 
ATOM   2316  C  CA  . VAL C  1 14  ? 116.944 -7.717  31.291 1.00 30.36  ? 14   VAL C CA  1 
ATOM   2317  C  C   . VAL C  1 14  ? 115.777 -6.920  30.731 1.00 32.28  ? 14   VAL C C   1 
ATOM   2318  O  O   . VAL C  1 14  ? 114.742 -7.531  30.409 1.00 32.18  ? 14   VAL C O   1 
ATOM   2319  C  CB  . VAL C  1 14  ? 117.435 -8.739  30.267 1.00 33.96  ? 14   VAL C CB  1 
ATOM   2320  C  CG1 . VAL C  1 14  ? 117.865 -8.065  28.966 1.00 32.69  ? 14   VAL C CG1 1 
ATOM   2321  C  CG2 . VAL C  1 14  ? 118.612 -9.541  30.825 1.00 32.81  ? 14   VAL C CG2 1 
ATOM   2322  N  N   . GLN C  1 15  ? 115.909 -5.613  30.626 1.00 28.59  ? 15   GLN C N   1 
ATOM   2323  C  CA  . GLN C  1 15  ? 114.903 -4.720  30.073 1.00 37.99  ? 15   GLN C CA  1 
ATOM   2324  C  C   . GLN C  1 15  ? 115.516 -3.650  29.181 1.00 40.51  ? 15   GLN C C   1 
ATOM   2325  O  O   . GLN C  1 15  ? 116.628 -3.176  29.416 1.00 32.61  ? 15   GLN C O   1 
ATOM   2326  C  CB  . GLN C  1 15  ? 114.125 -3.961  31.154 1.00 42.90  ? 15   GLN C CB  1 
ATOM   2327  C  CG  . GLN C  1 15  ? 113.905 -4.725  32.447 1.00 50.58  ? 15   GLN C CG  1 
ATOM   2328  C  CD  . GLN C  1 15  ? 113.215 -3.876  33.500 1.00 43.47  ? 15   GLN C CD  1 
ATOM   2329  O  OE1 . GLN C  1 15  ? 112.350 -3.058  33.191 1.00 50.38  ? 15   GLN C OE1 1 
ATOM   2330  N  NE2 . GLN C  1 15  ? 113.581 -4.059  34.757 1.00 62.39  ? 15   GLN C NE2 1 
ATOM   2331  N  N   . GLY C  1 16  ? 114.799 -3.202  28.149 1.00 32.00  ? 16   GLY C N   1 
ATOM   2332  C  CA  . GLY C  1 16  ? 115.355 -2.083  27.382 1.00 34.81  ? 16   GLY C CA  1 
ATOM   2333  C  C   . GLY C  1 16  ? 114.422 -1.569  26.301 1.00 44.89  ? 16   GLY C C   1 
ATOM   2334  O  O   . GLY C  1 16  ? 113.377 -2.176  26.053 1.00 37.11  ? 16   GLY C O   1 
ATOM   2335  N  N   . ILE C  1 17  ? 114.805 -0.465  25.681 1.00 29.60  ? 17   ILE C N   1 
ATOM   2336  C  CA  . ILE C  1 17  ? 114.050 0.140   24.594 1.00 34.61  ? 17   ILE C CA  1 
ATOM   2337  C  C   . ILE C  1 17  ? 114.961 0.390   23.398 1.00 40.82  ? 17   ILE C C   1 
ATOM   2338  O  O   . ILE C  1 17  ? 115.943 1.108   23.567 1.00 34.66  ? 17   ILE C O   1 
ATOM   2339  C  CB  . ILE C  1 17  ? 113.419 1.450   25.057 1.00 34.82  ? 17   ILE C CB  1 
ATOM   2340  C  CG1 . ILE C  1 17  ? 112.362 1.219   26.151 1.00 34.84  ? 17   ILE C CG1 1 
ATOM   2341  C  CG2 . ILE C  1 17  ? 112.838 2.254   23.907 1.00 34.73  ? 17   ILE C CG2 1 
ATOM   2342  C  CD1 . ILE C  1 17  ? 112.071 2.511   26.891 1.00 54.46  ? 17   ILE C CD1 1 
ATOM   2343  N  N   . ILE C  1 18  ? 114.633 -0.194  22.256 1.00 28.67  ? 18   ILE C N   1 
ATOM   2344  C  CA  . ILE C  1 18  ? 115.462 -0.055  21.063 1.00 29.70  ? 18   ILE C CA  1 
ATOM   2345  C  C   . ILE C  1 18  ? 114.694 0.623   19.926 1.00 35.44  ? 18   ILE C C   1 
ATOM   2346  O  O   . ILE C  1 18  ? 113.614 0.132   19.608 1.00 29.00  ? 18   ILE C O   1 
ATOM   2347  C  CB  . ILE C  1 18  ? 115.969 -1.423  20.605 1.00 30.66  ? 18   ILE C CB  1 
ATOM   2348  C  CG1 . ILE C  1 18  ? 116.787 -2.140  21.689 1.00 30.88  ? 18   ILE C CG1 1 
ATOM   2349  C  CG2 . ILE C  1 18  ? 116.747 -1.306  19.300 1.00 33.04  ? 18   ILE C CG2 1 
ATOM   2350  C  CD1 . ILE C  1 18  ? 118.081 -1.402  22.008 1.00 38.05  ? 18   ILE C CD1 1 
ATOM   2351  N  N   . ASN C  1 19  ? 115.289 1.681   19.395 1.00 29.63  ? 19   ASN C N   1 
ATOM   2352  C  CA  . ASN C  1 19  ? 114.783 2.527   18.334 1.00 32.58  ? 19   ASN C CA  1 
ATOM   2353  C  C   . ASN C  1 19  ? 115.338 2.160   16.964 1.00 39.27  ? 19   ASN C C   1 
ATOM   2354  O  O   . ASN C  1 19  ? 116.476 1.724   16.804 1.00 38.34  ? 19   ASN C O   1 
ATOM   2355  C  CB  . ASN C  1 19  ? 115.089 4.000   18.633 1.00 38.18  ? 19   ASN C CB  1 
ATOM   2356  C  CG  . ASN C  1 19  ? 114.511 4.439   19.959 1.00 45.73  ? 19   ASN C CG  1 
ATOM   2357  O  OD1 . ASN C  1 19  ? 113.295 4.599   20.083 1.00 40.36  ? 19   ASN C OD1 1 
ATOM   2358  N  ND2 . ASN C  1 19  ? 115.349 4.635   20.968 1.00 34.20  ? 19   ASN C ND2 1 
ATOM   2359  N  N   . PHE C  1 20  ? 114.495 2.346   15.940 1.00 34.91  ? 20   PHE C N   1 
ATOM   2360  C  CA  . PHE C  1 20  ? 114.923 2.077   14.567 1.00 30.47  ? 20   PHE C CA  1 
ATOM   2361  C  C   . PHE C  1 20  ? 114.495 3.281   13.717 1.00 35.49  ? 20   PHE C C   1 
ATOM   2362  O  O   . PHE C  1 20  ? 113.427 3.842   13.971 1.00 38.40  ? 20   PHE C O   1 
ATOM   2363  C  CB  . PHE C  1 20  ? 114.355 0.827   13.950 1.00 32.60  ? 20   PHE C CB  1 
ATOM   2364  C  CG  . PHE C  1 20  ? 114.529 -0.466  14.704 1.00 28.57  ? 20   PHE C CG  1 
ATOM   2365  C  CD1 . PHE C  1 20  ? 115.391 -1.431  14.258 1.00 29.58  ? 20   PHE C CD1 1 
ATOM   2366  C  CD2 . PHE C  1 20  ? 113.794 -0.695  15.858 1.00 32.36  ? 20   PHE C CD2 1 
ATOM   2367  C  CE1 . PHE C  1 20  ? 115.545 -2.637  14.916 1.00 37.38  ? 20   PHE C CE1 1 
ATOM   2368  C  CE2 . PHE C  1 20  ? 113.947 -1.899  16.516 1.00 28.71  ? 20   PHE C CE2 1 
ATOM   2369  C  CZ  . PHE C  1 20  ? 114.804 -2.876  16.062 1.00 32.30  ? 20   PHE C CZ  1 
ATOM   2370  N  N   . GLU C  1 21  ? 115.350 3.635   12.770 1.00 36.98  ? 21   GLU C N   1 
ATOM   2371  C  CA  . GLU C  1 21  ? 115.118 4.839   11.968 1.00 41.18  ? 21   GLU C CA  1 
ATOM   2372  C  C   . GLU C  1 21  ? 115.677 4.635   10.565 1.00 44.81  ? 21   GLU C C   1 
ATOM   2373  O  O   . GLU C  1 21  ? 116.841 4.284   10.383 1.00 40.36  ? 21   GLU C O   1 
ATOM   2374  C  CB  . GLU C  1 21  ? 115.736 6.051   12.646 1.00 54.29  ? 21   GLU C CB  1 
ATOM   2375  C  CG  . GLU C  1 21  ? 115.023 7.370   12.372 1.00 61.19  ? 21   GLU C CG  1 
ATOM   2376  C  CD  . GLU C  1 21  ? 116.033 8.463   12.059 1.00 72.81  ? 21   GLU C CD  1 
ATOM   2377  O  OE1 . GLU C  1 21  ? 115.642 9.646   12.023 1.00 92.56  ? 21   GLU C OE1 1 
ATOM   2378  O  OE2 . GLU C  1 21  ? 117.214 8.105   11.858 1.00 88.43  ? 21   GLU C OE2 1 
ATOM   2379  N  N   . GLN C  1 22  ? 114.828 4.825   9.553  1.00 36.50  ? 22   GLN C N   1 
ATOM   2380  C  CA  . GLN C  1 22  ? 115.284 4.623   8.177  1.00 33.76  ? 22   GLN C CA  1 
ATOM   2381  C  C   . GLN C  1 22  ? 114.803 5.812   7.358  1.00 43.33  ? 22   GLN C C   1 
ATOM   2382  O  O   . GLN C  1 22  ? 113.626 5.985   7.043  1.00 41.78  ? 22   GLN C O   1 
ATOM   2383  C  CB  . GLN C  1 22  ? 114.815 3.287   7.636  1.00 27.88  ? 22   GLN C CB  1 
ATOM   2384  C  CG  . GLN C  1 22  ? 115.489 2.831   6.360  1.00 27.63  ? 22   GLN C CG  1 
ATOM   2385  C  CD  . GLN C  1 22  ? 114.954 1.552   5.779  1.00 30.86  ? 22   GLN C CD  1 
ATOM   2386  O  OE1 . GLN C  1 22  ? 113.862 1.048   6.113  1.00 39.05  ? 22   GLN C OE1 1 
ATOM   2387  N  NE2 . GLN C  1 22  ? 115.716 0.975   4.860  1.00 33.11  ? 22   GLN C NE2 1 
ATOM   2388  N  N   . LYS C  1 23  ? 115.762 6.674   7.056  1.00 46.47  ? 23   LYS C N   1 
ATOM   2389  C  CA  . LYS C  1 23  ? 115.467 7.906   6.327  1.00 47.87  ? 23   LYS C CA  1 
ATOM   2390  C  C   . LYS C  1 23  ? 114.958 7.557   4.937  1.00 38.28  ? 23   LYS C C   1 
ATOM   2391  O  O   . LYS C  1 23  ? 113.979 8.122   4.457  1.00 52.03  ? 23   LYS C O   1 
ATOM   2392  C  CB  . LYS C  1 23  ? 116.737 8.747   6.302  1.00 57.01  ? 23   LYS C CB  1 
ATOM   2393  C  CG  . LYS C  1 23  ? 116.623 10.170  5.804  1.00 67.11  ? 23   LYS C CG  1 
ATOM   2394  C  CD  . LYS C  1 23  ? 117.985 10.728  5.404  1.00 72.11  ? 23   LYS C CD  1 
ATOM   2395  C  CE  . LYS C  1 23  ? 118.274 10.531  3.923  1.00 71.79  ? 23   LYS C CE  1 
ATOM   2396  N  NZ  . LYS C  1 23  ? 119.716 10.732  3.602  1.00 75.61  ? 23   LYS C NZ  1 
ATOM   2397  N  N   . GLU C  1 24  ? 115.616 6.601   4.291  1.00 38.47  ? 24   GLU C N   1 
ATOM   2398  C  CA  . GLU C  1 24  ? 115.288 6.185   2.941  1.00 39.97  ? 24   GLU C CA  1 
ATOM   2399  C  C   . GLU C  1 24  ? 115.036 4.691   2.803  1.00 45.44  ? 24   GLU C C   1 
ATOM   2400  O  O   . GLU C  1 24  ? 115.696 3.849   3.414  1.00 49.30  ? 24   GLU C O   1 
ATOM   2401  C  CB  . GLU C  1 24  ? 116.438 6.564   1.991  1.00 49.62  ? 24   GLU C CB  1 
ATOM   2402  C  CG  . GLU C  1 24  ? 116.875 8.007   2.077  1.00 53.97  ? 24   GLU C CG  1 
ATOM   2403  C  CD  . GLU C  1 24  ? 115.944 8.993   1.402  1.00 58.85  ? 24   GLU C CD  1 
ATOM   2404  O  OE1 . GLU C  1 24  ? 115.178 8.592   0.503  1.00 55.59  ? 24   GLU C OE1 1 
ATOM   2405  O  OE2 . GLU C  1 24  ? 115.995 10.187  1.779  1.00 67.64  ? 24   GLU C OE2 1 
ATOM   2406  N  N   . SER C  1 25  ? 114.067 4.355   1.944  1.00 40.68  ? 25   SER C N   1 
ATOM   2407  C  CA  . SER C  1 25  ? 113.590 2.984   1.803  1.00 31.74  ? 25   SER C CA  1 
ATOM   2408  C  C   . SER C  1 25  ? 114.651 2.088   1.222  1.00 37.07  ? 25   SER C C   1 
ATOM   2409  O  O   . SER C  1 25  ? 114.679 0.857   1.332  1.00 44.15  ? 25   SER C O   1 
ATOM   2410  C  CB  . SER C  1 25  ? 112.309 3.011   0.952  1.00 44.38  ? 25   SER C CB  1 
ATOM   2411  O  OG  . SER C  1 25  ? 112.599 2.857   -0.427 1.00 46.10  ? 25   SER C OG  1 
ATOM   2412  N  N   . ASN C  1 26  ? 115.620 2.726   0.547  1.00 39.16  ? 26   ASN C N   1 
ATOM   2413  C  CA  . ASN C  1 26  ? 116.722 1.880   0.071  1.00 45.39  ? 26   ASN C CA  1 
ATOM   2414  C  C   . ASN C  1 26  ? 118.005 2.263   0.807  1.00 49.37  ? 26   ASN C C   1 
ATOM   2415  O  O   . ASN C  1 26  ? 119.107 1.959   0.358  1.00 55.52  ? 26   ASN C O   1 
ATOM   2416  C  CB  . ASN C  1 26  ? 116.860 2.000   -1.443 1.00 45.45  ? 26   ASN C CB  1 
ATOM   2417  C  CG  . ASN C  1 26  ? 117.227 3.384   -1.929 1.00 40.60  ? 26   ASN C CG  1 
ATOM   2418  O  OD1 . ASN C  1 26  ? 116.850 4.416   -1.377 1.00 44.63  ? 26   ASN C OD1 1 
ATOM   2419  N  ND2 . ASN C  1 26  ? 118.006 3.422   -3.010 1.00 51.84  ? 26   ASN C ND2 1 
ATOM   2420  N  N   . GLY C  1 27  ? 117.842 2.949   1.935  1.00 45.65  ? 27   GLY C N   1 
ATOM   2421  C  CA  . GLY C  1 27  ? 118.945 3.380   2.773  1.00 44.46  ? 27   GLY C CA  1 
ATOM   2422  C  C   . GLY C  1 27  ? 119.160 2.465   3.967  1.00 53.92  ? 27   GLY C C   1 
ATOM   2423  O  O   . GLY C  1 27  ? 118.480 1.438   4.115  1.00 41.98  ? 27   GLY C O   1 
ATOM   2424  N  N   . PRO C  1 28  ? 120.110 2.828   4.826  1.00 44.68  ? 28   PRO C N   1 
ATOM   2425  C  CA  . PRO C  1 28  ? 120.375 2.020   6.021  1.00 45.52  ? 28   PRO C CA  1 
ATOM   2426  C  C   . PRO C  1 28  ? 119.432 2.382   7.165  1.00 37.41  ? 28   PRO C C   1 
ATOM   2427  O  O   . PRO C  1 28  ? 118.829 3.459   7.181  1.00 32.38  ? 28   PRO C O   1 
ATOM   2428  C  CB  . PRO C  1 28  ? 121.817 2.407   6.385  1.00 40.43  ? 28   PRO C CB  1 
ATOM   2429  C  CG  . PRO C  1 28  ? 121.965 3.806   5.893  1.00 45.20  ? 28   PRO C CG  1 
ATOM   2430  C  CD  . PRO C  1 28  ? 120.999 3.997   4.751  1.00 41.12  ? 28   PRO C CD  1 
ATOM   2431  N  N   . VAL C  1 29  ? 119.344 1.462   8.123  1.00 38.99  ? 29   VAL C N   1 
ATOM   2432  C  CA  . VAL C  1 29  ? 118.553 1.668   9.333  1.00 40.02  ? 29   VAL C CA  1 
ATOM   2433  C  C   . VAL C  1 29  ? 119.419 2.006   10.537 1.00 23.10  ? 29   VAL C C   1 
ATOM   2434  O  O   . VAL C  1 29  ? 120.312 1.228   10.891 1.00 33.66  ? 29   VAL C O   1 
ATOM   2435  C  CB  . VAL C  1 29  ? 117.719 0.400   9.615  1.00 38.72  ? 29   VAL C CB  1 
ATOM   2436  C  CG1 . VAL C  1 29  ? 116.842 0.563   10.855 1.00 32.72  ? 29   VAL C CG1 1 
ATOM   2437  C  CG2 . VAL C  1 29  ? 116.862 0.050   8.407  1.00 44.22  ? 29   VAL C CG2 1 
ATOM   2438  N  N   . LYS C  1 30  ? 119.191 3.121   11.210 1.00 34.56  ? 30   LYS C N   1 
ATOM   2439  C  CA  . LYS C  1 30  ? 119.910 3.328   12.475 1.00 44.57  ? 30   LYS C CA  1 
ATOM   2440  C  C   . LYS C  1 30  ? 119.195 2.591   13.608 1.00 48.92  ? 30   LYS C C   1 
ATOM   2441  O  O   . LYS C  1 30  ? 117.986 2.796   13.787 1.00 40.29  ? 30   LYS C O   1 
ATOM   2442  C  CB  . LYS C  1 30  ? 120.021 4.808   12.800 1.00 52.29  ? 30   LYS C CB  1 
ATOM   2443  C  CG  . LYS C  1 30  ? 120.923 5.584   11.850 1.00 73.64  ? 30   LYS C CG  1 
ATOM   2444  C  CD  . LYS C  1 30  ? 120.118 6.194   10.710 1.00 87.37  ? 30   LYS C CD  1 
ATOM   2445  C  CE  . LYS C  1 30  ? 121.012 6.987   9.770  1.00 92.41  ? 30   LYS C CE  1 
ATOM   2446  N  NZ  . LYS C  1 30  ? 121.728 8.091   10.489 1.00 98.15  ? 30   LYS C NZ  1 
ATOM   2447  N  N   . VAL C  1 31  ? 119.926 1.759   14.340 1.00 41.74  ? 31   VAL C N   1 
ATOM   2448  C  CA  . VAL C  1 31  ? 119.423 1.051   15.517 1.00 33.17  ? 31   VAL C CA  1 
ATOM   2449  C  C   . VAL C  1 31  ? 120.119 1.530   16.789 1.00 41.39  ? 31   VAL C C   1 
ATOM   2450  O  O   . VAL C  1 31  ? 121.319 1.265   16.921 1.00 49.43  ? 31   VAL C O   1 
ATOM   2451  C  CB  . VAL C  1 31  ? 119.657 -0.452  15.399 1.00 33.60  ? 31   VAL C CB  1 
ATOM   2452  C  CG1 . VAL C  1 31  ? 118.901 -1.183  16.505 1.00 42.94  ? 31   VAL C CG1 1 
ATOM   2453  C  CG2 . VAL C  1 31  ? 119.252 -0.954  14.027 1.00 39.05  ? 31   VAL C CG2 1 
ATOM   2454  N  N   . TRP C  1 32  ? 119.400 2.215   17.663 1.00 34.89  ? 32   TRP C N   1 
ATOM   2455  C  CA  . TRP C  1 32  ? 119.996 2.779   18.866 1.00 39.51  ? 32   TRP C CA  1 
ATOM   2456  C  C   . TRP C  1 32  ? 119.059 2.657   20.061 1.00 51.02  ? 32   TRP C C   1 
ATOM   2457  O  O   . TRP C  1 32  ? 117.834 2.589   19.907 1.00 41.23  ? 32   TRP C O   1 
ATOM   2458  C  CB  . TRP C  1 32  ? 120.389 4.242   18.639 1.00 30.70  ? 32   TRP C CB  1 
ATOM   2459  C  CG  . TRP C  1 32  ? 119.262 5.210   18.732 1.00 32.45  ? 32   TRP C CG  1 
ATOM   2460  C  CD1 . TRP C  1 32  ? 118.899 5.962   19.808 1.00 36.22  ? 32   TRP C CD1 1 
ATOM   2461  C  CD2 . TRP C  1 32  ? 118.334 5.527   17.677 1.00 39.01  ? 32   TRP C CD2 1 
ATOM   2462  N  NE1 . TRP C  1 32  ? 117.803 6.730   19.489 1.00 45.76  ? 32   TRP C NE1 1 
ATOM   2463  C  CE2 . TRP C  1 32  ? 117.438 6.481   18.189 1.00 41.55  ? 32   TRP C CE2 1 
ATOM   2464  C  CE3 . TRP C  1 32  ? 118.182 5.094   16.357 1.00 47.32  ? 32   TRP C CE3 1 
ATOM   2465  C  CZ2 . TRP C  1 32  ? 116.401 7.012   17.423 1.00 40.79  ? 32   TRP C CZ2 1 
ATOM   2466  C  CZ3 . TRP C  1 32  ? 117.151 5.620   15.598 1.00 45.21  ? 32   TRP C CZ3 1 
ATOM   2467  C  CH2 . TRP C  1 32  ? 116.276 6.568   16.137 1.00 42.05  ? 32   TRP C CH2 1 
ATOM   2468  N  N   . GLY C  1 33  ? 119.653 2.626   21.256 1.00 36.33  ? 33   GLY C N   1 
ATOM   2469  C  CA  . GLY C  1 33  ? 118.848 2.565   22.471 1.00 34.96  ? 33   GLY C CA  1 
ATOM   2470  C  C   . GLY C  1 33  ? 119.661 2.040   23.638 1.00 51.54  ? 33   GLY C C   1 
ATOM   2471  O  O   . GLY C  1 33  ? 120.891 1.986   23.560 1.00 37.61  ? 33   GLY C O   1 
ATOM   2472  N  N   . SER C  1 34  ? 119.002 1.650   24.727 1.00 48.29  ? 34   SER C N   1 
ATOM   2473  C  CA  . SER C  1 34  ? 119.742 1.050   25.833 1.00 37.19  ? 34   SER C CA  1 
ATOM   2474  C  C   . SER C  1 34  ? 119.023 -0.202  26.316 1.00 46.62  ? 34   SER C C   1 
ATOM   2475  O  O   . SER C  1 34  ? 117.799 -0.272  26.248 1.00 44.08  ? 34   SER C O   1 
ATOM   2476  C  CB  . SER C  1 34  ? 119.892 2.017   27.001 1.00 44.52  ? 34   SER C CB  1 
ATOM   2477  O  OG  . SER C  1 34  ? 119.192 3.219   26.736 1.00 68.44  ? 34   SER C OG  1 
ATOM   2478  N  N   . ILE C  1 35  ? 119.815 -1.135  26.798 1.00 43.49  ? 35   ILE C N   1 
ATOM   2479  C  CA  . ILE C  1 35  ? 119.348 -2.338  27.471 1.00 35.92  ? 35   ILE C CA  1 
ATOM   2480  C  C   . ILE C  1 35  ? 120.005 -2.347  28.854 1.00 47.92  ? 35   ILE C C   1 
ATOM   2481  O  O   . ILE C  1 35  ? 121.204 -2.063  28.928 1.00 41.60  ? 35   ILE C O   1 
ATOM   2482  C  CB  . ILE C  1 35  ? 119.666 -3.593  26.665 1.00 31.15  ? 35   ILE C CB  1 
ATOM   2483  C  CG1 . ILE C  1 35  ? 119.278 -3.457  25.168 1.00 28.20  ? 35   ILE C CG1 1 
ATOM   2484  C  CG2 . ILE C  1 35  ? 119.048 -4.856  27.259 1.00 32.93  ? 35   ILE C CG2 1 
ATOM   2485  C  CD1 . ILE C  1 35  ? 119.703 -4.649  24.347 1.00 30.47  ? 35   ILE C CD1 1 
ATOM   2486  N  N   . LYS C  1 36  ? 119.244 -2.642  29.900 1.00 40.76  ? 36   LYS C N   1 
ATOM   2487  C  CA  . LYS C  1 36  ? 119.821 -2.831  31.227 1.00 41.95  ? 36   LYS C CA  1 
ATOM   2488  C  C   . LYS C  1 36  ? 119.610 -4.258  31.734 1.00 42.91  ? 36   LYS C C   1 
ATOM   2489  O  O   . LYS C  1 36  ? 118.873 -5.084  31.189 1.00 34.39  ? 36   LYS C O   1 
ATOM   2490  C  CB  . LYS C  1 36  ? 119.267 -1.826  32.228 1.00 44.00  ? 36   LYS C CB  1 
ATOM   2491  C  CG  . LYS C  1 36  ? 117.784 -1.979  32.545 1.00 47.33  ? 36   LYS C CG  1 
ATOM   2492  C  CD  . LYS C  1 36  ? 117.236 -0.684  33.124 1.00 65.00  ? 36   LYS C CD  1 
ATOM   2493  C  CE  . LYS C  1 36  ? 116.252 -0.916  34.259 1.00 71.87  ? 36   LYS C CE  1 
ATOM   2494  N  NZ  . LYS C  1 36  ? 116.849 -1.659  35.405 1.00 48.49  ? 36   LYS C NZ  1 
ATOM   2495  N  N   . GLY C  1 37  ? 120.324 -4.533  32.827 1.00 35.69  ? 37   GLY C N   1 
ATOM   2496  C  CA  . GLY C  1 37  ? 120.247 -5.756  33.573 1.00 29.06  ? 37   GLY C CA  1 
ATOM   2497  C  C   . GLY C  1 37  ? 121.007 -6.913  33.032 1.00 37.29  ? 37   GLY C C   1 
ATOM   2498  O  O   . GLY C  1 37  ? 120.741 -8.074  33.372 1.00 35.18  ? 37   GLY C O   1 
ATOM   2499  N  N   . LEU C  1 38  ? 121.988 -6.605  32.164 1.00 35.91  ? 38   LEU C N   1 
ATOM   2500  C  CA  . LEU C  1 38  ? 122.732 -7.702  31.569 1.00 27.64  ? 38   LEU C CA  1 
ATOM   2501  C  C   . LEU C  1 38  ? 124.040 -7.929  32.364 1.00 29.02  ? 38   LEU C C   1 
ATOM   2502  O  O   . LEU C  1 38  ? 124.439 -7.015  33.063 1.00 33.97  ? 38   LEU C O   1 
ATOM   2503  C  CB  . LEU C  1 38  ? 123.111 -7.455  30.110 1.00 35.18  ? 38   LEU C CB  1 
ATOM   2504  C  CG  . LEU C  1 38  ? 121.964 -7.257  29.105 1.00 30.97  ? 38   LEU C CG  1 
ATOM   2505  C  CD1 . LEU C  1 38  ? 122.310 -6.114  28.153 1.00 36.89  ? 38   LEU C CD1 1 
ATOM   2506  C  CD2 . LEU C  1 38  ? 121.666 -8.554  28.390 1.00 31.04  ? 38   LEU C CD2 1 
ATOM   2507  N  N   . THR C  1 39  ? 124.595 -9.119  32.194 1.00 40.45  ? 39   THR C N   1 
ATOM   2508  C  CA  . THR C  1 39  ? 125.949 -9.354  32.714 1.00 50.90  ? 39   THR C CA  1 
ATOM   2509  C  C   . THR C  1 39  ? 126.927 -8.547  31.855 1.00 50.36  ? 39   THR C C   1 
ATOM   2510  O  O   . THR C  1 39  ? 126.821 -8.617  30.623 1.00 36.37  ? 39   THR C O   1 
ATOM   2511  C  CB  . THR C  1 39  ? 126.346 -10.829 32.700 1.00 54.28  ? 39   THR C CB  1 
ATOM   2512  O  OG1 . THR C  1 39  ? 126.255 -11.338 31.361 1.00 61.49  ? 39   THR C OG1 1 
ATOM   2513  C  CG2 . THR C  1 39  ? 125.392 -11.684 33.529 1.00 67.78  ? 39   THR C CG2 1 
ATOM   2514  N  N   . GLU C  1 40  ? 127.821 -7.810  32.498 1.00 51.64  ? 40   GLU C N   1 
ATOM   2515  C  CA  . GLU C  1 40  ? 128.741 -6.903  31.804 1.00 48.67  ? 40   GLU C CA  1 
ATOM   2516  C  C   . GLU C  1 40  ? 129.444 -7.656  30.692 1.00 43.27  ? 40   GLU C C   1 
ATOM   2517  O  O   . GLU C  1 40  ? 129.710 -8.857  30.834 1.00 46.68  ? 40   GLU C O   1 
ATOM   2518  C  CB  . GLU C  1 40  ? 129.728 -6.281  32.777 1.00 63.99  ? 40   GLU C CB  1 
ATOM   2519  C  CG  . GLU C  1 40  ? 131.191 -6.449  32.391 1.00 72.99  ? 40   GLU C CG  1 
ATOM   2520  C  CD  . GLU C  1 40  ? 132.087 -6.014  33.539 1.00 81.77  ? 40   GLU C CD  1 
ATOM   2521  O  OE1 . GLU C  1 40  ? 132.711 -6.908  34.147 1.00 105.66 ? 40   GLU C OE1 1 
ATOM   2522  O  OE2 . GLU C  1 40  ? 132.147 -4.796  33.822 1.00 61.28  ? 40   GLU C OE2 1 
ATOM   2523  N  N   . GLY C  1 41  ? 129.710 -6.991  29.555 1.00 34.57  ? 41   GLY C N   1 
ATOM   2524  C  CA  . GLY C  1 41  ? 130.154 -7.814  28.434 1.00 32.52  ? 41   GLY C CA  1 
ATOM   2525  C  C   . GLY C  1 41  ? 129.213 -7.891  27.244 1.00 41.15  ? 41   GLY C C   1 
ATOM   2526  O  O   . GLY C  1 41  ? 128.255 -7.130  27.082 1.00 41.78  ? 41   GLY C O   1 
ATOM   2527  N  N   . LEU C  1 42  ? 129.469 -8.856  26.366 1.00 40.36  ? 42   LEU C N   1 
ATOM   2528  C  CA  . LEU C  1 42  ? 128.810 -9.029  25.089 1.00 50.82  ? 42   LEU C CA  1 
ATOM   2529  C  C   . LEU C  1 42  ? 127.669 -10.042 25.056 1.00 50.78  ? 42   LEU C C   1 
ATOM   2530  O  O   . LEU C  1 42  ? 127.709 -11.119 25.638 1.00 40.26  ? 42   LEU C O   1 
ATOM   2531  C  CB  . LEU C  1 42  ? 129.822 -9.499  24.036 1.00 46.64  ? 42   LEU C CB  1 
ATOM   2532  C  CG  . LEU C  1 42  ? 131.123 -8.707  23.889 1.00 45.73  ? 42   LEU C CG  1 
ATOM   2533  C  CD1 . LEU C  1 42  ? 131.802 -9.142  22.602 1.00 33.26  ? 42   LEU C CD1 1 
ATOM   2534  C  CD2 . LEU C  1 42  ? 130.880 -7.206  23.908 1.00 64.33  ? 42   LEU C CD2 1 
ATOM   2535  N  N   . HIS C  1 43  ? 126.615 -9.679  24.323 1.00 39.77  ? 43   HIS C N   1 
ATOM   2536  C  CA  . HIS C  1 43  ? 125.433 -10.513 24.188 1.00 36.43  ? 43   HIS C CA  1 
ATOM   2537  C  C   . HIS C  1 43  ? 124.857 -10.407 22.761 1.00 26.11  ? 43   HIS C C   1 
ATOM   2538  O  O   . HIS C  1 43  ? 124.773 -9.256  22.304 1.00 38.80  ? 43   HIS C O   1 
ATOM   2539  C  CB  . HIS C  1 43  ? 124.347 -10.101 25.170 1.00 41.79  ? 43   HIS C CB  1 
ATOM   2540  C  CG  . HIS C  1 43  ? 124.760 -9.925  26.594 1.00 42.35  ? 43   HIS C CG  1 
ATOM   2541  N  ND1 . HIS C  1 43  ? 124.576 -10.907 27.544 1.00 43.86  ? 43   HIS C ND1 1 
ATOM   2542  C  CD2 . HIS C  1 43  ? 125.347 -8.892  27.230 1.00 35.31  ? 43   HIS C CD2 1 
ATOM   2543  C  CE1 . HIS C  1 43  ? 125.038 -10.471 28.704 1.00 40.43  ? 43   HIS C CE1 1 
ATOM   2544  N  NE2 . HIS C  1 43  ? 125.514 -9.249  28.550 1.00 40.68  ? 43   HIS C NE2 1 
ATOM   2545  N  N   . GLY C  1 44  ? 124.556 -11.568 22.249 1.00 28.01  ? 44   GLY C N   1 
ATOM   2546  C  CA  . GLY C  1 44  ? 123.945 -11.828 20.957 1.00 47.63  ? 44   GLY C CA  1 
ATOM   2547  C  C   . GLY C  1 44  ? 122.670 -10.995 20.830 1.00 52.86  ? 44   GLY C C   1 
ATOM   2548  O  O   . GLY C  1 44  ? 121.945 -10.832 21.816 1.00 35.40  ? 44   GLY C O   1 
ATOM   2549  N  N   . PHE C  1 45  ? 122.428 -10.468 19.639 1.00 39.32  ? 45   PHE C N   1 
ATOM   2550  C  CA  . PHE C  1 45  ? 121.377 -9.478  19.399 1.00 31.02  ? 45   PHE C CA  1 
ATOM   2551  C  C   . PHE C  1 45  ? 120.849 -9.674  17.985 1.00 44.17  ? 45   PHE C C   1 
ATOM   2552  O  O   . PHE C  1 45  ? 121.594 -9.367  17.048 1.00 36.72  ? 45   PHE C O   1 
ATOM   2553  C  CB  . PHE C  1 45  ? 121.928 -8.085  19.506 1.00 31.41  ? 45   PHE C CB  1 
ATOM   2554  C  CG  . PHE C  1 45  ? 121.029 -6.884  19.592 1.00 37.59  ? 45   PHE C CG  1 
ATOM   2555  C  CD1 . PHE C  1 45  ? 120.111 -6.741  20.620 1.00 35.27  ? 45   PHE C CD1 1 
ATOM   2556  C  CD2 . PHE C  1 45  ? 121.118 -5.868  18.644 1.00 30.38  ? 45   PHE C CD2 1 
ATOM   2557  C  CE1 . PHE C  1 45  ? 119.327 -5.611  20.718 1.00 33.98  ? 45   PHE C CE1 1 
ATOM   2558  C  CE2 . PHE C  1 45  ? 120.343 -4.738  18.739 1.00 35.60  ? 45   PHE C CE2 1 
ATOM   2559  C  CZ  . PHE C  1 45  ? 119.430 -4.607  19.776 1.00 39.65  ? 45   PHE C CZ  1 
ATOM   2560  N  N   . HIS C  1 46  ? 119.635 -10.203 17.869 1.00 36.06  ? 46   HIS C N   1 
ATOM   2561  C  CA  . HIS C  1 46  ? 119.098 -10.544 16.572 1.00 26.36  ? 46   HIS C CA  1 
ATOM   2562  C  C   . HIS C  1 46  ? 117.607 -10.175 16.481 1.00 37.61  ? 46   HIS C C   1 
ATOM   2563  O  O   . HIS C  1 46  ? 116.975 -10.016 17.523 1.00 32.51  ? 46   HIS C O   1 
ATOM   2564  C  CB  . HIS C  1 46  ? 119.202 -12.031 16.274 1.00 26.21  ? 46   HIS C CB  1 
ATOM   2565  C  CG  . HIS C  1 46  ? 120.410 -12.720 16.834 1.00 45.77  ? 46   HIS C CG  1 
ATOM   2566  N  ND1 . HIS C  1 46  ? 120.367 -13.557 17.927 1.00 51.24  ? 46   HIS C ND1 1 
ATOM   2567  C  CD2 . HIS C  1 46  ? 121.710 -12.675 16.449 1.00 46.04  ? 46   HIS C CD2 1 
ATOM   2568  C  CE1 . HIS C  1 46  ? 121.584 -14.007 18.187 1.00 56.34  ? 46   HIS C CE1 1 
ATOM   2569  N  NE2 . HIS C  1 46  ? 122.423 -13.486 17.300 1.00 45.57  ? 46   HIS C NE2 1 
ATOM   2570  N  N   . VAL C  1 47  ? 117.141 -10.095 15.253 1.00 30.76  ? 47   VAL C N   1 
ATOM   2571  C  CA  . VAL C  1 47  ? 115.734 -10.181 14.866 1.00 29.44  ? 47   VAL C CA  1 
ATOM   2572  C  C   . VAL C  1 47  ? 115.367 -11.618 14.597 1.00 28.36  ? 47   VAL C C   1 
ATOM   2573  O  O   . VAL C  1 47  ? 115.961 -12.310 13.764 1.00 33.69  ? 47   VAL C O   1 
ATOM   2574  C  CB  . VAL C  1 47  ? 115.434 -9.308  13.620 1.00 22.26  ? 47   VAL C CB  1 
ATOM   2575  C  CG1 . VAL C  1 47  ? 113.944 -9.357  13.289 1.00 30.47  ? 47   VAL C CG1 1 
ATOM   2576  C  CG2 . VAL C  1 47  ? 115.870 -7.893  13.881 1.00 29.34  ? 47   VAL C CG2 1 
ATOM   2577  N  N   . HIS C  1 48  ? 114.379 -12.188 15.288 1.00 24.08  ? 48   HIS C N   1 
ATOM   2578  C  CA  . HIS C  1 48  ? 113.902 -13.527 15.040 1.00 22.75  ? 48   HIS C CA  1 
ATOM   2579  C  C   . HIS C  1 48  ? 112.614 -13.488 14.182 1.00 27.63  ? 48   HIS C C   1 
ATOM   2580  O  O   . HIS C  1 48  ? 112.041 -12.400 14.111 1.00 29.97  ? 48   HIS C O   1 
ATOM   2581  C  CB  . HIS C  1 48  ? 113.626 -14.283 16.343 1.00 30.13  ? 48   HIS C CB  1 
ATOM   2582  C  CG  . HIS C  1 48  ? 114.888 -14.624 17.098 1.00 27.10  ? 48   HIS C CG  1 
ATOM   2583  N  ND1 . HIS C  1 48  ? 115.118 -15.920 17.469 1.00 29.31  ? 48   HIS C ND1 1 
ATOM   2584  C  CD2 . HIS C  1 48  ? 115.945 -13.917 17.530 1.00 30.79  ? 48   HIS C CD2 1 
ATOM   2585  C  CE1 . HIS C  1 48  ? 116.271 -15.992 18.106 1.00 24.09  ? 48   HIS C CE1 1 
ATOM   2586  N  NE2 . HIS C  1 48  ? 116.792 -14.794 18.165 1.00 23.42  ? 48   HIS C NE2 1 
ATOM   2587  N  N   . GLU C  1 49  ? 112.237 -14.593 13.581 1.00 29.49  ? 49   GLU C N   1 
ATOM   2588  C  CA  . GLU C  1 49  ? 111.225 -14.659 12.544 1.00 31.89  ? 49   GLU C CA  1 
ATOM   2589  C  C   . GLU C  1 49  ? 109.827 -14.244 12.998 1.00 37.04  ? 49   GLU C C   1 
ATOM   2590  O  O   . GLU C  1 49  ? 109.188 -13.461 12.291 1.00 32.32  ? 49   GLU C O   1 
ATOM   2591  C  CB  . GLU C  1 49  ? 111.145 -16.077 11.988 1.00 31.16  ? 49   GLU C CB  1 
ATOM   2592  C  CG  . GLU C  1 49  ? 110.238 -16.145 10.748 1.00 41.75  ? 49   GLU C CG  1 
ATOM   2593  C  CD  . GLU C  1 49  ? 110.233 -17.554 10.188 1.00 47.03  ? 49   GLU C CD  1 
ATOM   2594  O  OE1 . GLU C  1 49  ? 109.425 -17.933 9.313  1.00 41.83  ? 49   GLU C OE1 1 
ATOM   2595  O  OE2 . GLU C  1 49  ? 111.088 -18.327 10.674 1.00 48.09  ? 49   GLU C OE2 1 
ATOM   2596  N  N   . PHE C  1 50  ? 109.357 -14.750 14.137 1.00 27.93  ? 50   PHE C N   1 
ATOM   2597  C  CA  . PHE C  1 50  ? 107.960 -14.444 14.490 1.00 27.64  ? 50   PHE C CA  1 
ATOM   2598  C  C   . PHE C  1 50  ? 107.806 -13.426 15.610 1.00 29.10  ? 50   PHE C C   1 
ATOM   2599  O  O   . PHE C  1 50  ? 108.562 -13.417 16.584 1.00 32.01  ? 50   PHE C O   1 
ATOM   2600  C  CB  . PHE C  1 50  ? 107.238 -15.741 14.864 1.00 26.39  ? 50   PHE C CB  1 
ATOM   2601  C  CG  . PHE C  1 50  ? 107.424 -16.837 13.837 1.00 35.95  ? 50   PHE C CG  1 
ATOM   2602  C  CD1 . PHE C  1 50  ? 107.022 -16.642 12.527 1.00 37.32  ? 50   PHE C CD1 1 
ATOM   2603  C  CD2 . PHE C  1 50  ? 108.009 -18.040 14.204 1.00 44.15  ? 50   PHE C CD2 1 
ATOM   2604  C  CE1 . PHE C  1 50  ? 107.214 -17.649 11.594 1.00 39.28  ? 50   PHE C CE1 1 
ATOM   2605  C  CE2 . PHE C  1 50  ? 108.184 -19.051 13.276 1.00 40.71  ? 50   PHE C CE2 1 
ATOM   2606  C  CZ  . PHE C  1 50  ? 107.780 -18.855 11.968 1.00 34.41  ? 50   PHE C CZ  1 
ATOM   2607  N  N   . GLY C  1 51  ? 106.793 -12.563 15.497 1.00 23.73  ? 51   GLY C N   1 
ATOM   2608  C  CA  . GLY C  1 51  ? 106.481 -11.601 16.556 1.00 23.64  ? 51   GLY C CA  1 
ATOM   2609  C  C   . GLY C  1 51  ? 105.446 -12.222 17.496 1.00 28.85  ? 51   GLY C C   1 
ATOM   2610  O  O   . GLY C  1 51  ? 104.425 -11.594 17.752 1.00 26.67  ? 51   GLY C O   1 
ATOM   2611  N  N   . ASP C  1 52  ? 105.741 -13.416 17.979 1.00 27.61  ? 52   ASP C N   1 
ATOM   2612  C  CA  . ASP C  1 52  ? 104.876 -14.237 18.815 1.00 24.16  ? 52   ASP C CA  1 
ATOM   2613  C  C   . ASP C  1 52  ? 105.450 -14.398 20.213 1.00 33.35  ? 52   ASP C C   1 
ATOM   2614  O  O   . ASP C  1 52  ? 106.444 -15.107 20.391 1.00 38.42  ? 52   ASP C O   1 
ATOM   2615  C  CB  . ASP C  1 52  ? 104.683 -15.585 18.135 1.00 23.28  ? 52   ASP C CB  1 
ATOM   2616  C  CG  . ASP C  1 52  ? 103.712 -16.511 18.834 1.00 27.19  ? 52   ASP C CG  1 
ATOM   2617  O  OD1 . ASP C  1 52  ? 103.201 -17.424 18.171 1.00 30.85  ? 52   ASP C OD1 1 
ATOM   2618  O  OD2 . ASP C  1 52  ? 103.466 -16.352 20.046 1.00 26.42  ? 52   ASP C OD2 1 
ATOM   2619  N  N   . ASN C  1 53  ? 104.831 -13.763 21.198 1.00 27.04  ? 53   ASN C N   1 
ATOM   2620  C  CA  . ASN C  1 53  ? 105.318 -13.850 22.580 1.00 25.92  ? 53   ASN C CA  1 
ATOM   2621  C  C   . ASN C  1 53  ? 104.417 -14.707 23.466 1.00 25.00  ? 53   ASN C C   1 
ATOM   2622  O  O   . ASN C  1 53  ? 104.439 -14.556 24.694 1.00 29.62  ? 53   ASN C O   1 
ATOM   2623  C  CB  . ASN C  1 53  ? 105.433 -12.428 23.118 1.00 24.91  ? 53   ASN C CB  1 
ATOM   2624  C  CG  . ASN C  1 53  ? 106.117 -12.331 24.463 1.00 44.78  ? 53   ASN C CG  1 
ATOM   2625  O  OD1 . ASN C  1 53  ? 105.607 -11.756 25.427 1.00 53.07  ? 53   ASN C OD1 1 
ATOM   2626  N  ND2 . ASN C  1 53  ? 107.308 -12.905 24.520 1.00 41.40  ? 53   ASN C ND2 1 
ATOM   2627  N  N   . THR C  1 54  ? 103.632 -15.588 22.851 1.00 24.92  ? 54   THR C N   1 
ATOM   2628  C  CA  . THR C  1 54  ? 102.650 -16.362 23.591 1.00 26.88  ? 54   THR C CA  1 
ATOM   2629  C  C   . THR C  1 54  ? 103.362 -17.305 24.562 1.00 38.87  ? 54   THR C C   1 
ATOM   2630  O  O   . THR C  1 54  ? 102.834 -17.616 25.632 1.00 42.14  ? 54   THR C O   1 
ATOM   2631  C  CB  . THR C  1 54  ? 101.666 -17.142 22.708 1.00 34.66  ? 54   THR C CB  1 
ATOM   2632  O  OG1 . THR C  1 54  ? 102.355 -18.032 21.826 1.00 33.76  ? 54   THR C OG1 1 
ATOM   2633  C  CG2 . THR C  1 54  ? 100.838 -16.186 21.842 1.00 23.84  ? 54   THR C CG2 1 
ATOM   2634  N  N   . ALA C  1 55  ? 104.563 -17.755 24.225 1.00 31.46  ? 55   ALA C N   1 
ATOM   2635  C  CA  . ALA C  1 55  ? 105.352 -18.563 25.170 1.00 36.41  ? 55   ALA C CA  1 
ATOM   2636  C  C   . ALA C  1 55  ? 106.627 -17.832 25.542 1.00 33.61  ? 55   ALA C C   1 
ATOM   2637  O  O   . ALA C  1 55  ? 107.707 -18.424 25.593 1.00 44.70  ? 55   ALA C O   1 
ATOM   2638  C  CB  . ALA C  1 55  ? 105.651 -19.933 24.577 1.00 40.65  ? 55   ALA C CB  1 
ATOM   2639  N  N   . GLY C  1 56  ? 106.543 -16.524 25.776 1.00 34.17  ? 56   GLY C N   1 
ATOM   2640  C  CA  . GLY C  1 56  ? 107.752 -15.744 26.047 1.00 32.56  ? 56   GLY C CA  1 
ATOM   2641  C  C   . GLY C  1 56  ? 108.680 -15.740 24.845 1.00 37.75  ? 56   GLY C C   1 
ATOM   2642  O  O   . GLY C  1 56  ? 108.263 -15.914 23.695 1.00 29.45  ? 56   GLY C O   1 
ATOM   2643  N  N   . CYS C  1 57  ? 109.988 -15.562 25.031 1.00 36.08  ? 57   CYS C N   1 
ATOM   2644  C  CA  . CYS C  1 57  ? 110.807 -15.409 23.814 1.00 36.07  ? 57   CYS C CA  1 
ATOM   2645  C  C   . CYS C  1 57  ? 110.950 -16.679 23.006 1.00 33.45  ? 57   CYS C C   1 
ATOM   2646  O  O   . CYS C  1 57  ? 111.373 -16.660 21.844 1.00 31.08  ? 57   CYS C O   1 
ATOM   2647  C  CB  A CYS C  1 57  ? 112.207 -14.929 24.226 0.42 41.57  ? 57   CYS C CB  1 
ATOM   2648  C  CB  B CYS C  1 57  ? 112.181 -14.845 24.189 0.58 42.78  ? 57   CYS C CB  1 
ATOM   2649  S  SG  A CYS C  1 57  ? 112.174 -13.392 25.182 0.42 49.93  ? 57   CYS C SG  1 
ATOM   2650  S  SG  B CYS C  1 57  ? 112.113 -13.465 25.352 0.58 53.39  ? 57   CYS C SG  1 
ATOM   2651  N  N   . THR C  1 58  ? 110.628 -17.826 23.584 1.00 28.74  ? 58   THR C N   1 
ATOM   2652  C  CA  . THR C  1 58  ? 110.770 -19.091 22.898 1.00 31.78  ? 58   THR C CA  1 
ATOM   2653  C  C   . THR C  1 58  ? 109.930 -19.180 21.638 1.00 37.80  ? 58   THR C C   1 
ATOM   2654  O  O   . THR C  1 58  ? 110.351 -19.805 20.655 1.00 35.29  ? 58   THR C O   1 
ATOM   2655  C  CB  . THR C  1 58  ? 110.365 -20.250 23.840 1.00 43.90  ? 58   THR C CB  1 
ATOM   2656  O  OG1 . THR C  1 58  ? 111.020 -20.088 25.102 1.00 44.34  ? 58   THR C OG1 1 
ATOM   2657  C  CG2 . THR C  1 58  ? 110.818 -21.574 23.250 1.00 40.06  ? 58   THR C CG2 1 
ATOM   2658  N  N   . SER C  1 59  ? 108.730 -18.571 21.628 1.00 27.64  ? 59   SER C N   1 
ATOM   2659  C  CA  . SER C  1 59  ? 107.919 -18.771 20.413 1.00 29.76  ? 59   SER C CA  1 
ATOM   2660  C  C   . SER C  1 59  ? 108.286 -17.760 19.337 1.00 29.15  ? 59   SER C C   1 
ATOM   2661  O  O   . SER C  1 59  ? 107.652 -17.716 18.275 1.00 43.49  ? 59   SER C O   1 
ATOM   2662  C  CB  . SER C  1 59  ? 106.427 -18.729 20.772 1.00 32.82  ? 59   SER C CB  1 
ATOM   2663  O  OG  . SER C  1 59  ? 106.225 -17.719 21.752 1.00 32.34  ? 59   SER C OG  1 
ATOM   2664  N  N   . ALA C  1 60  ? 109.305 -16.929 19.518 1.00 27.88  ? 60   ALA C N   1 
ATOM   2665  C  CA  . ALA C  1 60  ? 109.749 -16.047 18.460 1.00 22.70  ? 60   ALA C CA  1 
ATOM   2666  C  C   . ALA C  1 60  ? 110.382 -16.840 17.303 1.00 30.32  ? 60   ALA C C   1 
ATOM   2667  O  O   . ALA C  1 60  ? 110.680 -16.241 16.267 1.00 33.04  ? 60   ALA C O   1 
ATOM   2668  C  CB  . ALA C  1 60  ? 110.782 -15.039 18.942 1.00 23.29  ? 60   ALA C CB  1 
ATOM   2669  N  N   . GLY C  1 61  ? 110.605 -18.125 17.467 1.00 27.92  ? 61   GLY C N   1 
ATOM   2670  C  CA  . GLY C  1 61  ? 111.220 -18.955 16.425 1.00 32.50  ? 61   GLY C CA  1 
ATOM   2671  C  C   . GLY C  1 61  ? 112.670 -18.572 16.200 1.00 29.02  ? 61   GLY C C   1 
ATOM   2672  O  O   . GLY C  1 61  ? 113.269 -17.875 17.014 1.00 31.79  ? 61   GLY C O   1 
ATOM   2673  N  N   . PRO C  1 62  ? 113.252 -18.991 15.077 1.00 36.57  ? 62   PRO C N   1 
ATOM   2674  C  CA  . PRO C  1 62  ? 114.673 -18.747 14.803 1.00 36.06  ? 62   PRO C CA  1 
ATOM   2675  C  C   . PRO C  1 62  ? 114.985 -17.382 14.212 1.00 43.45  ? 62   PRO C C   1 
ATOM   2676  O  O   . PRO C  1 62  ? 114.152 -16.487 14.077 1.00 35.27  ? 62   PRO C O   1 
ATOM   2677  C  CB  . PRO C  1 62  ? 115.012 -19.841 13.794 1.00 40.45  ? 62   PRO C CB  1 
ATOM   2678  C  CG  . PRO C  1 62  ? 113.739 -20.323 13.209 1.00 52.00  ? 62   PRO C CG  1 
ATOM   2679  C  CD  . PRO C  1 62  ? 112.601 -19.749 14.008 1.00 44.94  ? 62   PRO C CD  1 
ATOM   2680  N  N   . HIS C  1 63  ? 116.272 -17.203 13.871 1.00 30.27  ? 63   HIS C N   1 
ATOM   2681  C  CA  . HIS C  1 63  ? 116.664 -15.891 13.371 1.00 31.79  ? 63   HIS C CA  1 
ATOM   2682  C  C   . HIS C  1 63  ? 115.897 -15.675 12.055 1.00 28.57  ? 63   HIS C C   1 
ATOM   2683  O  O   . HIS C  1 63  ? 115.667 -16.669 11.374 1.00 34.26  ? 63   HIS C O   1 
ATOM   2684  C  CB  . HIS C  1 63  ? 118.158 -15.753 13.135 1.00 41.17  ? 63   HIS C CB  1 
ATOM   2685  C  CG  . HIS C  1 63  ? 118.997 -16.002 14.345 1.00 44.74  ? 63   HIS C CG  1 
ATOM   2686  N  ND1 . HIS C  1 63  ? 120.295 -15.551 14.456 1.00 45.63  ? 63   HIS C ND1 1 
ATOM   2687  C  CD2 . HIS C  1 63  ? 118.725 -16.657 15.497 1.00 46.18  ? 63   HIS C CD2 1 
ATOM   2688  C  CE1 . HIS C  1 63  ? 120.780 -15.919 15.625 1.00 51.78  ? 63   HIS C CE1 1 
ATOM   2689  N  NE2 . HIS C  1 63  ? 119.848 -16.589 16.275 1.00 50.59  ? 63   HIS C NE2 1 
ATOM   2690  N  N   . PHE C  1 64  ? 115.528 -14.429 11.816 1.00 31.05  ? 64   PHE C N   1 
ATOM   2691  C  CA  . PHE C  1 64  ? 114.837 -14.063 10.584 1.00 34.54  ? 64   PHE C CA  1 
ATOM   2692  C  C   . PHE C  1 64  ? 115.760 -14.307 9.382  1.00 34.35  ? 64   PHE C C   1 
ATOM   2693  O  O   . PHE C  1 64  ? 116.867 -13.774 9.335  1.00 33.32  ? 64   PHE C O   1 
ATOM   2694  C  CB  . PHE C  1 64  ? 114.415 -12.603 10.669 1.00 29.95  ? 64   PHE C CB  1 
ATOM   2695  C  CG  . PHE C  1 64  ? 113.664 -12.121 9.426  1.00 28.63  ? 64   PHE C CG  1 
ATOM   2696  C  CD1 . PHE C  1 64  ? 113.940 -10.847 8.960  1.00 29.92  ? 64   PHE C CD1 1 
ATOM   2697  C  CD2 . PHE C  1 64  ? 112.742 -12.941 8.806  1.00 35.85  ? 64   PHE C CD2 1 
ATOM   2698  C  CE1 . PHE C  1 64  ? 113.269 -10.373 7.840  1.00 31.18  ? 64   PHE C CE1 1 
ATOM   2699  C  CE2 . PHE C  1 64  ? 112.075 -12.481 7.676  1.00 38.68  ? 64   PHE C CE2 1 
ATOM   2700  C  CZ  . PHE C  1 64  ? 112.363 -11.203 7.214  1.00 26.41  ? 64   PHE C CZ  1 
ATOM   2701  N  N   . ASN C  1 65  ? 115.309 -15.107 8.436  1.00 38.69  ? 65   ASN C N   1 
ATOM   2702  C  CA  . ASN C  1 65  ? 116.235 -15.577 7.405  1.00 45.67  ? 65   ASN C CA  1 
ATOM   2703  C  C   . ASN C  1 65  ? 115.534 -15.781 6.077  1.00 36.26  ? 65   ASN C C   1 
ATOM   2704  O  O   . ASN C  1 65  ? 115.450 -16.893 5.555  1.00 38.64  ? 65   ASN C O   1 
ATOM   2705  C  CB  . ASN C  1 65  ? 116.824 -16.908 7.866  1.00 47.90  ? 65   ASN C CB  1 
ATOM   2706  C  CG  . ASN C  1 65  ? 117.987 -17.336 6.992  1.00 49.43  ? 65   ASN C CG  1 
ATOM   2707  O  OD1 . ASN C  1 65  ? 118.673 -16.491 6.417  1.00 46.57  ? 65   ASN C OD1 1 
ATOM   2708  N  ND2 . ASN C  1 65  ? 118.200 -18.639 6.957  1.00 36.44  ? 65   ASN C ND2 1 
ATOM   2709  N  N   . PRO C  1 66  ? 115.003 -14.694 5.531  1.00 29.51  ? 66   PRO C N   1 
ATOM   2710  C  CA  . PRO C  1 66  ? 114.244 -14.845 4.286  1.00 34.49  ? 66   PRO C CA  1 
ATOM   2711  C  C   . PRO C  1 66  ? 115.152 -15.345 3.163  1.00 43.26  ? 66   PRO C C   1 
ATOM   2712  O  O   . PRO C  1 66  ? 114.680 -15.992 2.235  1.00 45.53  ? 66   PRO C O   1 
ATOM   2713  C  CB  . PRO C  1 66  ? 113.768 -13.429 4.011  1.00 33.80  ? 66   PRO C CB  1 
ATOM   2714  C  CG  . PRO C  1 66  ? 114.665 -12.531 4.790  1.00 35.27  ? 66   PRO C CG  1 
ATOM   2715  C  CD  . PRO C  1 66  ? 115.074 -13.314 6.009  1.00 32.95  ? 66   PRO C CD  1 
ATOM   2716  N  N   . LEU C  1 67  ? 116.451 -15.059 3.239  1.00 42.42  ? 67   LEU C N   1 
ATOM   2717  C  CA  . LEU C  1 67  ? 117.322 -15.470 2.137  1.00 53.64  ? 67   LEU C CA  1 
ATOM   2718  C  C   . LEU C  1 67  ? 117.994 -16.818 2.348  1.00 56.23  ? 67   LEU C C   1 
ATOM   2719  O  O   . LEU C  1 67  ? 118.996 -17.098 1.692  1.00 64.48  ? 67   LEU C O   1 
ATOM   2720  C  CB  . LEU C  1 67  ? 118.370 -14.368 1.910  1.00 40.55  ? 67   LEU C CB  1 
ATOM   2721  C  CG  . LEU C  1 67  ? 117.816 -13.162 1.137  1.00 44.07  ? 67   LEU C CG  1 
ATOM   2722  C  CD1 . LEU C  1 67  ? 118.680 -11.934 1.372  1.00 66.13  ? 67   LEU C CD1 1 
ATOM   2723  C  CD2 . LEU C  1 67  ? 117.701 -13.488 -0.343 1.00 61.32  ? 67   LEU C CD2 1 
ATOM   2724  N  N   . SER C  1 68  ? 117.458 -17.636 3.228  1.00 53.45  ? 68   SER C N   1 
ATOM   2725  C  CA  . SER C  1 68  ? 117.951 -18.946 3.606  1.00 54.61  ? 68   SER C CA  1 
ATOM   2726  C  C   . SER C  1 68  ? 119.473 -19.070 3.619  1.00 54.85  ? 68   SER C C   1 
ATOM   2727  O  O   . SER C  1 68  ? 120.009 -19.972 2.968  1.00 81.52  ? 68   SER C O   1 
ATOM   2728  C  CB  . SER C  1 68  ? 117.380 -20.018 2.670  1.00 49.11  ? 68   SER C CB  1 
ATOM   2729  O  OG  . SER C  1 68  ? 115.968 -20.003 2.643  1.00 55.25  ? 68   SER C OG  1 
ATOM   2730  N  N   . ARG C  1 69  ? 120.193 -18.224 4.336  1.00 53.98  ? 69   ARG C N   1 
ATOM   2731  C  CA  . ARG C  1 69  ? 121.650 -18.304 4.382  1.00 61.12  ? 69   ARG C CA  1 
ATOM   2732  C  C   . ARG C  1 69  ? 122.168 -18.999 5.639  1.00 71.69  ? 69   ARG C C   1 
ATOM   2733  O  O   . ARG C  1 69  ? 121.565 -19.976 6.098  1.00 82.02  ? 69   ARG C O   1 
ATOM   2734  C  CB  . ARG C  1 69  ? 122.231 -16.888 4.271  1.00 57.77  ? 69   ARG C CB  1 
ATOM   2735  C  CG  . ARG C  1 69  ? 122.759 -16.609 2.868  1.00 62.90  ? 69   ARG C CG  1 
ATOM   2736  C  CD  . ARG C  1 69  ? 122.378 -15.219 2.397  1.00 71.16  ? 69   ARG C CD  1 
ATOM   2737  N  NE  . ARG C  1 69  ? 121.533 -15.269 1.204  1.00 86.90  ? 69   ARG C NE  1 
ATOM   2738  C  CZ  . ARG C  1 69  ? 121.372 -14.265 0.349  1.00 98.97  ? 69   ARG C CZ  1 
ATOM   2739  N  NH1 . ARG C  1 69  ? 120.575 -14.404 -0.710 1.00 112.19 ? 69   ARG C NH1 1 
ATOM   2740  N  NH2 . ARG C  1 69  ? 122.012 -13.117 0.557  1.00 105.53 ? 69   ARG C NH2 1 
ATOM   2741  N  N   . LYS C  1 70  ? 123.279 -18.519 6.203  1.00 54.02  ? 70   LYS C N   1 
ATOM   2742  C  CA  . LYS C  1 70  ? 123.796 -19.046 7.466  1.00 38.44  ? 70   LYS C CA  1 
ATOM   2743  C  C   . LYS C  1 70  ? 124.242 -17.907 8.370  1.00 45.28  ? 70   LYS C C   1 
ATOM   2744  O  O   . LYS C  1 70  ? 124.494 -16.795 7.891  1.00 50.63  ? 70   LYS C O   1 
ATOM   2745  C  CB  . LYS C  1 70  ? 124.934 -20.044 7.236  1.00 51.85  ? 70   LYS C CB  1 
ATOM   2746  C  CG  . LYS C  1 70  ? 124.598 -21.146 6.251  1.00 51.47  ? 70   LYS C CG  1 
ATOM   2747  C  CD  . LYS C  1 70  ? 124.229 -22.462 6.917  1.00 58.46  ? 70   LYS C CD  1 
ATOM   2748  C  CE  . LYS C  1 70  ? 125.213 -23.570 6.580  1.00 64.37  ? 70   LYS C CE  1 
ATOM   2749  N  NZ  . LYS C  1 70  ? 124.638 -24.649 5.732  1.00 68.60  ? 70   LYS C NZ  1 
ATOM   2750  N  N   . HIS C  1 71  ? 124.317 -18.178 9.672  1.00 39.43  ? 71   HIS C N   1 
ATOM   2751  C  CA  . HIS C  1 71  ? 124.533 -17.122 10.650 1.00 38.58  ? 71   HIS C CA  1 
ATOM   2752  C  C   . HIS C  1 71  ? 125.871 -16.408 10.529 1.00 43.42  ? 71   HIS C C   1 
ATOM   2753  O  O   . HIS C  1 71  ? 126.903 -16.997 10.200 1.00 61.53  ? 71   HIS C O   1 
ATOM   2754  C  CB  . HIS C  1 71  ? 124.323 -17.728 12.066 1.00 41.83  ? 71   HIS C CB  1 
ATOM   2755  C  CG  . HIS C  1 71  ? 124.436 -16.681 13.133 1.00 40.17  ? 71   HIS C CG  1 
ATOM   2756  N  ND1 . HIS C  1 71  ? 123.454 -15.743 13.386 1.00 35.17  ? 71   HIS C ND1 1 
ATOM   2757  C  CD2 . HIS C  1 71  ? 125.440 -16.412 13.994 1.00 31.38  ? 71   HIS C CD2 1 
ATOM   2758  C  CE1 . HIS C  1 71  ? 123.849 -14.956 14.361 1.00 37.27  ? 71   HIS C CE1 1 
ATOM   2759  N  NE2 . HIS C  1 71  ? 125.055 -15.334 14.756 1.00 47.93  ? 71   HIS C NE2 1 
ATOM   2760  N  N   . GLY C  1 72  ? 125.899 -15.103 10.810 1.00 43.80  ? 72   GLY C N   1 
ATOM   2761  C  CA  . GLY C  1 72  ? 127.099 -14.290 10.784 1.00 42.40  ? 72   GLY C CA  1 
ATOM   2762  C  C   . GLY C  1 72  ? 126.986 -13.054 11.659 1.00 45.80  ? 72   GLY C C   1 
ATOM   2763  O  O   . GLY C  1 72  ? 125.970 -12.857 12.345 1.00 46.44  ? 72   GLY C O   1 
ATOM   2764  N  N   . GLY C  1 73  ? 128.016 -12.219 11.648 1.00 33.28  ? 73   GLY C N   1 
ATOM   2765  C  CA  . GLY C  1 73  ? 128.020 -10.930 12.347 1.00 32.11  ? 73   GLY C CA  1 
ATOM   2766  C  C   . GLY C  1 73  ? 127.396 -9.853  11.470 1.00 35.88  ? 73   GLY C C   1 
ATOM   2767  O  O   . GLY C  1 73  ? 127.172 -10.165 10.291 1.00 40.91  ? 73   GLY C O   1 
ATOM   2768  N  N   . PRO C  1 74  ? 127.102 -8.649  11.962 1.00 34.54  ? 74   PRO C N   1 
ATOM   2769  C  CA  . PRO C  1 74  ? 126.462 -7.632  11.123 1.00 37.45  ? 74   PRO C CA  1 
ATOM   2770  C  C   . PRO C  1 74  ? 127.281 -7.192  9.911  1.00 57.17  ? 74   PRO C C   1 
ATOM   2771  O  O   . PRO C  1 74  ? 126.724 -6.859  8.855  1.00 50.04  ? 74   PRO C O   1 
ATOM   2772  C  CB  . PRO C  1 74  ? 126.299 -6.412  12.038 1.00 42.26  ? 74   PRO C CB  1 
ATOM   2773  C  CG  . PRO C  1 74  ? 127.086 -6.688  13.259 1.00 36.39  ? 74   PRO C CG  1 
ATOM   2774  C  CD  . PRO C  1 74  ? 127.315 -8.164  13.321 1.00 36.82  ? 74   PRO C CD  1 
ATOM   2775  N  N   . LYS C  1 75  ? 128.609 -7.154  10.034 1.00 53.72  ? 75   LYS C N   1 
ATOM   2776  C  CA  . LYS C  1 75  ? 129.376 -6.644  8.887  1.00 44.09  ? 75   LYS C CA  1 
ATOM   2777  C  C   . LYS C  1 75  ? 129.820 -7.769  7.974  1.00 47.29  ? 75   LYS C C   1 
ATOM   2778  O  O   . LYS C  1 75  ? 130.755 -7.601  7.194  1.00 73.29  ? 75   LYS C O   1 
ATOM   2779  C  CB  . LYS C  1 75  ? 130.531 -5.813  9.419  1.00 47.22  ? 75   LYS C CB  1 
ATOM   2780  C  CG  . LYS C  1 75  ? 130.093 -4.811  10.482 1.00 64.65  ? 75   LYS C CG  1 
ATOM   2781  C  CD  . LYS C  1 75  ? 129.054 -3.838  9.930  1.00 68.32  ? 75   LYS C CD  1 
ATOM   2782  C  CE  . LYS C  1 75  ? 129.123 -2.494  10.641 1.00 68.29  ? 75   LYS C CE  1 
ATOM   2783  N  NZ  . LYS C  1 75  ? 127.784 -1.877  10.855 1.00 65.90  ? 75   LYS C NZ  1 
ATOM   2784  N  N   . ASP C  1 76  ? 129.154 -8.913  8.038  1.00 35.19  ? 76   ASP C N   1 
ATOM   2785  C  CA  . ASP C  1 76  ? 129.422 -10.022 7.140  1.00 34.86  ? 76   ASP C CA  1 
ATOM   2786  C  C   . ASP C  1 76  ? 128.453 -10.029 5.959  1.00 60.06  ? 76   ASP C C   1 
ATOM   2787  O  O   . ASP C  1 76  ? 127.317 -9.574  6.078  1.00 62.57  ? 76   ASP C O   1 
ATOM   2788  C  CB  . ASP C  1 76  ? 129.314 -11.384 7.830  1.00 40.99  ? 76   ASP C CB  1 
ATOM   2789  C  CG  . ASP C  1 76  ? 130.063 -11.408 9.153  1.00 63.55  ? 76   ASP C CG  1 
ATOM   2790  O  OD1 . ASP C  1 76  ? 130.179 -12.476 9.793  1.00 57.71  ? 76   ASP C OD1 1 
ATOM   2791  O  OD2 . ASP C  1 76  ? 130.540 -10.328 9.563  1.00 81.98  ? 76   ASP C OD2 1 
ATOM   2792  N  N   . GLU C  1 77  ? 128.932 -10.569 4.843  1.00 71.14  ? 77   GLU C N   1 
ATOM   2793  C  CA  . GLU C  1 77  ? 128.112 -10.714 3.649  1.00 77.83  ? 77   GLU C CA  1 
ATOM   2794  C  C   . GLU C  1 77  ? 127.162 -11.898 3.794  1.00 72.23  ? 77   GLU C C   1 
ATOM   2795  O  O   . GLU C  1 77  ? 126.001 -11.850 3.386  1.00 84.00  ? 77   GLU C O   1 
ATOM   2796  C  CB  . GLU C  1 77  ? 128.978 -10.890 2.398  1.00 85.79  ? 77   GLU C CB  1 
ATOM   2797  C  CG  . GLU C  1 77  ? 128.802 -9.717  1.424  1.00 96.52  ? 77   GLU C CG  1 
ATOM   2798  C  CD  . GLU C  1 77  ? 128.019 -8.576  2.059  1.00 101.51 ? 77   GLU C CD  1 
ATOM   2799  O  OE1 . GLU C  1 77  ? 128.658 -7.659  2.613  1.00 104.86 ? 77   GLU C OE1 1 
ATOM   2800  O  OE2 . GLU C  1 77  ? 126.772 -8.621  2.001  1.00 111.33 ? 77   GLU C OE2 1 
ATOM   2801  N  N   . GLU C  1 78  ? 127.689 -12.965 4.391  1.00 60.72  ? 78   GLU C N   1 
ATOM   2802  C  CA  . GLU C  1 78  ? 126.835 -14.122 4.661  1.00 62.01  ? 78   GLU C CA  1 
ATOM   2803  C  C   . GLU C  1 78  ? 126.427 -14.108 6.138  1.00 63.72  ? 78   GLU C C   1 
ATOM   2804  O  O   . GLU C  1 78  ? 127.208 -14.369 7.053  1.00 46.01  ? 78   GLU C O   1 
ATOM   2805  C  CB  . GLU C  1 78  ? 127.513 -15.426 4.270  1.00 58.59  ? 78   GLU C CB  1 
ATOM   2806  C  CG  . GLU C  1 78  ? 126.601 -16.321 3.434  1.00 54.52  ? 78   GLU C CG  1 
ATOM   2807  C  CD  . GLU C  1 78  ? 126.108 -17.489 4.262  1.00 55.02  ? 78   GLU C CD  1 
ATOM   2808  O  OE1 . GLU C  1 78  ? 124.947 -17.402 4.715  1.00 90.16  ? 78   GLU C OE1 1 
ATOM   2809  O  OE2 . GLU C  1 78  ? 126.874 -18.454 4.448  1.00 66.87  ? 78   GLU C OE2 1 
ATOM   2810  N  N   . ARG C  1 79  ? 125.158 -13.758 6.305  1.00 50.55  ? 79   ARG C N   1 
ATOM   2811  C  CA  . ARG C  1 79  ? 124.508 -13.487 7.565  1.00 33.68  ? 79   ARG C CA  1 
ATOM   2812  C  C   . ARG C  1 79  ? 122.998 -13.587 7.389  1.00 48.78  ? 79   ARG C C   1 
ATOM   2813  O  O   . ARG C  1 79  ? 122.561 -13.191 6.305  1.00 50.82  ? 79   ARG C O   1 
ATOM   2814  C  CB  . ARG C  1 79  ? 124.817 -12.062 8.048  1.00 39.37  ? 79   ARG C CB  1 
ATOM   2815  C  CG  . ARG C  1 79  ? 124.210 -10.967 7.170  1.00 36.61  ? 79   ARG C CG  1 
ATOM   2816  C  CD  . ARG C  1 79  ? 124.391 -9.603  7.838  1.00 44.64  ? 79   ARG C CD  1 
ATOM   2817  N  NE  . ARG C  1 79  ? 123.117 -9.120  8.356  1.00 34.40  ? 79   ARG C NE  1 
ATOM   2818  C  CZ  . ARG C  1 79  ? 122.826 -7.925  8.817  1.00 44.38  ? 79   ARG C CZ  1 
ATOM   2819  N  NH1 . ARG C  1 79  ? 121.578 -7.695  9.240  1.00 41.11  ? 79   ARG C NH1 1 
ATOM   2820  N  NH2 . ARG C  1 79  ? 123.711 -6.936  8.886  1.00 40.04  ? 79   ARG C NH2 1 
ATOM   2821  N  N   . HIS C  1 80  ? 122.291 -14.063 8.404  1.00 45.28  ? 80   HIS C N   1 
ATOM   2822  C  CA  . HIS C  1 80  ? 120.837 -13.933 8.458  1.00 31.02  ? 80   HIS C CA  1 
ATOM   2823  C  C   . HIS C  1 80  ? 120.520 -12.454 8.366  1.00 23.62  ? 80   HIS C C   1 
ATOM   2824  O  O   . HIS C  1 80  ? 121.251 -11.632 8.940  1.00 36.58  ? 80   HIS C O   1 
ATOM   2825  C  CB  . HIS C  1 80  ? 120.295 -14.516 9.762  1.00 33.81  ? 80   HIS C CB  1 
ATOM   2826  C  CG  . HIS C  1 80  ? 120.554 -15.982 9.930  1.00 38.91  ? 80   HIS C CG  1 
ATOM   2827  N  ND1 . HIS C  1 80  ? 120.872 -16.596 11.121 1.00 42.88  ? 80   HIS C ND1 1 
ATOM   2828  C  CD2 . HIS C  1 80  ? 120.546 -16.974 9.013  1.00 43.49  ? 80   HIS C CD2 1 
ATOM   2829  C  CE1 . HIS C  1 80  ? 121.034 -17.893 10.920 1.00 38.52  ? 80   HIS C CE1 1 
ATOM   2830  N  NE2 . HIS C  1 80  ? 120.841 -18.155 9.641  1.00 44.55  ? 80   HIS C NE2 1 
ATOM   2831  N  N   . VAL C  1 81  ? 119.422 -12.118 7.673  1.00 35.48  ? 81   VAL C N   1 
ATOM   2832  C  CA  . VAL C  1 81  ? 118.962 -10.739 7.710  1.00 28.73  ? 81   VAL C CA  1 
ATOM   2833  C  C   . VAL C  1 81  ? 118.852 -10.259 9.145  1.00 19.91  ? 81   VAL C C   1 
ATOM   2834  O  O   . VAL C  1 81  ? 119.217 -9.149  9.504  1.00 33.92  ? 81   VAL C O   1 
ATOM   2835  C  CB  . VAL C  1 81  ? 117.585 -10.599 7.027  1.00 42.27  ? 81   VAL C CB  1 
ATOM   2836  C  CG1 . VAL C  1 81  ? 117.012 -9.203  7.225  1.00 35.03  ? 81   VAL C CG1 1 
ATOM   2837  C  CG2 . VAL C  1 81  ? 117.716 -10.946 5.550  1.00 56.66  ? 81   VAL C CG2 1 
ATOM   2838  N  N   . GLY C  1 82  ? 118.377 -11.161 10.017 1.00 35.73  ? 82   GLY C N   1 
ATOM   2839  C  CA  . GLY C  1 82  ? 118.261 -10.772 11.413 1.00 36.19  ? 82   GLY C CA  1 
ATOM   2840  C  C   . GLY C  1 82  ? 119.533 -10.690 12.215 1.00 44.87  ? 82   GLY C C   1 
ATOM   2841  O  O   . GLY C  1 82  ? 119.523 -10.343 13.411 1.00 34.74  ? 82   GLY C O   1 
ATOM   2842  N  N   . ASP C  1 83  ? 120.704 -10.971 11.633 1.00 45.82  ? 83   ASP C N   1 
ATOM   2843  C  CA  . ASP C  1 83  ? 121.919 -10.952 12.468 1.00 33.37  ? 83   ASP C CA  1 
ATOM   2844  C  C   . ASP C  1 83  ? 122.490 -9.580  12.702 1.00 39.98  ? 83   ASP C C   1 
ATOM   2845  O  O   . ASP C  1 83  ? 122.999 -8.877  11.832 1.00 52.65  ? 83   ASP C O   1 
ATOM   2846  C  CB  . ASP C  1 83  ? 122.962 -11.856 11.802 1.00 30.83  ? 83   ASP C CB  1 
ATOM   2847  C  CG  . ASP C  1 83  ? 122.534 -13.298 11.832 1.00 41.27  ? 83   ASP C CG  1 
ATOM   2848  O  OD1 . ASP C  1 83  ? 121.553 -13.623 12.543 1.00 53.57  ? 83   ASP C OD1 1 
ATOM   2849  O  OD2 . ASP C  1 83  ? 123.091 -14.175 11.137 1.00 50.05  ? 83   ASP C OD2 1 
ATOM   2850  N  N   . LEU C  1 84  ? 122.414 -9.174  13.969 1.00 29.70  ? 84   LEU C N   1 
ATOM   2851  C  CA  . LEU C  1 84  ? 122.856 -7.858  14.355 1.00 26.85  ? 84   LEU C CA  1 
ATOM   2852  C  C   . LEU C  1 84  ? 124.035 -7.932  15.338 1.00 30.83  ? 84   LEU C C   1 
ATOM   2853  O  O   . LEU C  1 84  ? 124.338 -6.932  15.976 1.00 35.71  ? 84   LEU C O   1 
ATOM   2854  C  CB  . LEU C  1 84  ? 121.711 -7.032  14.941 1.00 36.13  ? 84   LEU C CB  1 
ATOM   2855  C  CG  . LEU C  1 84  ? 120.476 -6.898  14.026 1.00 41.00  ? 84   LEU C CG  1 
ATOM   2856  C  CD1 . LEU C  1 84  ? 119.390 -6.125  14.744 1.00 37.24  ? 84   LEU C CD1 1 
ATOM   2857  C  CD2 . LEU C  1 84  ? 120.821 -6.212  12.715 1.00 51.04  ? 84   LEU C CD2 1 
ATOM   2858  N  N   . GLY C  1 85  ? 124.703 -9.070  15.441 1.00 39.67  ? 85   GLY C N   1 
ATOM   2859  C  CA  . GLY C  1 85  ? 125.955 -9.082  16.186 1.00 50.78  ? 85   GLY C CA  1 
ATOM   2860  C  C   . GLY C  1 85  ? 125.845 -9.119  17.699 1.00 52.52  ? 85   GLY C C   1 
ATOM   2861  O  O   . GLY C  1 85  ? 125.074 -9.917  18.246 1.00 58.27  ? 85   GLY C O   1 
ATOM   2862  N  N   . ASN C  1 86  ? 126.606 -8.266  18.376 1.00 40.00  ? 86   ASN C N   1 
ATOM   2863  C  CA  . ASN C  1 86  ? 126.690 -8.170  19.816 1.00 42.37  ? 86   ASN C CA  1 
ATOM   2864  C  C   . ASN C  1 86  ? 126.513 -6.773  20.371 1.00 42.38  ? 86   ASN C C   1 
ATOM   2865  O  O   . ASN C  1 86  ? 127.036 -5.762  19.895 1.00 42.72  ? 86   ASN C O   1 
ATOM   2866  C  CB  . ASN C  1 86  ? 128.075 -8.669  20.305 1.00 44.46  ? 86   ASN C CB  1 
ATOM   2867  C  CG  . ASN C  1 86  ? 128.201 -10.164 20.159 1.00 41.13  ? 86   ASN C CG  1 
ATOM   2868  O  OD1 . ASN C  1 86  ? 127.388 -10.940 20.667 1.00 60.32  ? 86   ASN C OD1 1 
ATOM   2869  N  ND2 . ASN C  1 86  ? 129.237 -10.605 19.444 1.00 56.08  ? 86   ASN C ND2 1 
ATOM   2870  N  N   . VAL C  1 87  ? 125.751 -6.673  21.468 1.00 31.86  ? 87   VAL C N   1 
ATOM   2871  C  CA  . VAL C  1 87  ? 125.777 -5.390  22.170 1.00 28.82  ? 87   VAL C CA  1 
ATOM   2872  C  C   . VAL C  1 87  ? 126.708 -5.602  23.380 1.00 29.26  ? 87   VAL C C   1 
ATOM   2873  O  O   . VAL C  1 87  ? 126.953 -6.782  23.642 1.00 39.53  ? 87   VAL C O   1 
ATOM   2874  C  CB  . VAL C  1 87  ? 124.418 -4.887  22.658 1.00 38.27  ? 87   VAL C CB  1 
ATOM   2875  C  CG1 . VAL C  1 87  ? 123.480 -4.616  21.490 1.00 40.30  ? 87   VAL C CG1 1 
ATOM   2876  C  CG2 . VAL C  1 87  ? 123.781 -5.898  23.609 1.00 40.57  ? 87   VAL C CG2 1 
ATOM   2877  N  N   . THR C  1 88  ? 127.122 -4.523  23.986 1.00 35.16  ? 88   THR C N   1 
ATOM   2878  C  CA  . THR C  1 88  ? 128.086 -4.520  25.068 1.00 36.66  ? 88   THR C CA  1 
ATOM   2879  C  C   . THR C  1 88  ? 127.595 -3.938  26.369 1.00 32.00  ? 88   THR C C   1 
ATOM   2880  O  O   . THR C  1 88  ? 127.370 -2.731  26.515 1.00 37.93  ? 88   THR C O   1 
ATOM   2881  C  CB  . THR C  1 88  ? 129.317 -3.670  24.623 1.00 43.74  ? 88   THR C CB  1 
ATOM   2882  O  OG1 . THR C  1 88  ? 130.060 -4.453  23.696 1.00 42.26  ? 88   THR C OG1 1 
ATOM   2883  C  CG2 . THR C  1 88  ? 130.182 -3.357  25.826 1.00 46.04  ? 88   THR C CG2 1 
ATOM   2884  N  N   . ALA C  1 89  ? 127.428 -4.800  27.375 1.00 34.30  ? 89   ALA C N   1 
ATOM   2885  C  CA  . ALA C  1 89  ? 127.050 -4.284  28.682 1.00 40.05  ? 89   ALA C CA  1 
ATOM   2886  C  C   . ALA C  1 89  ? 128.267 -3.817  29.479 1.00 43.26  ? 89   ALA C C   1 
ATOM   2887  O  O   . ALA C  1 89  ? 129.253 -4.509  29.686 1.00 41.40  ? 89   ALA C O   1 
ATOM   2888  C  CB  . ALA C  1 89  ? 126.301 -5.325  29.510 1.00 31.55  ? 89   ALA C CB  1 
ATOM   2889  N  N   . ASP C  1 90  ? 128.173 -2.583  29.962 1.00 42.23  ? 90   ASP C N   1 
ATOM   2890  C  CA  . ASP C  1 90  ? 129.261 -2.134  30.813 1.00 47.62  ? 90   ASP C CA  1 
ATOM   2891  C  C   . ASP C  1 90  ? 129.228 -2.817  32.174 1.00 55.69  ? 90   ASP C C   1 
ATOM   2892  O  O   . ASP C  1 90  ? 128.431 -3.705  32.465 1.00 46.82  ? 90   ASP C O   1 
ATOM   2893  C  CB  . ASP C  1 90  ? 129.168 -0.623  30.960 1.00 44.56  ? 90   ASP C CB  1 
ATOM   2894  C  CG  . ASP C  1 90  ? 127.887 -0.136  31.593 1.00 49.60  ? 90   ASP C CG  1 
ATOM   2895  O  OD1 . ASP C  1 90  ? 127.537 1.013   31.247 1.00 53.52  ? 90   ASP C OD1 1 
ATOM   2896  O  OD2 . ASP C  1 90  ? 127.263 -0.849  32.409 1.00 51.45  ? 90   ASP C OD2 1 
ATOM   2897  N  N   . LYS C  1 91  ? 130.133 -2.339  33.030 1.00 61.61  ? 91   LYS C N   1 
ATOM   2898  C  CA  . LYS C  1 91  ? 130.274 -2.830  34.391 1.00 63.26  ? 91   LYS C CA  1 
ATOM   2899  C  C   . LYS C  1 91  ? 128.924 -2.875  35.101 1.00 64.55  ? 91   LYS C C   1 
ATOM   2900  O  O   . LYS C  1 91  ? 128.649 -3.757  35.916 1.00 61.26  ? 91   LYS C O   1 
ATOM   2901  C  CB  . LYS C  1 91  ? 131.260 -1.951  35.167 1.00 64.44  ? 91   LYS C CB  1 
ATOM   2902  C  CG  . LYS C  1 91  ? 132.434 -1.457  34.340 1.00 72.53  ? 91   LYS C CG  1 
ATOM   2903  C  CD  . LYS C  1 91  ? 133.619 -1.060  35.210 1.00 76.86  ? 91   LYS C CD  1 
ATOM   2904  C  CE  . LYS C  1 91  ? 134.684 -0.308  34.429 1.00 77.18  ? 91   LYS C CE  1 
ATOM   2905  N  NZ  . LYS C  1 91  ? 136.000 -0.286  35.128 1.00 74.36  ? 91   LYS C NZ  1 
ATOM   2906  N  N   . ASP C  1 92  ? 128.077 -1.901  34.782 1.00 53.64  ? 92   ASP C N   1 
ATOM   2907  C  CA  . ASP C  1 92  ? 126.788 -1.793  35.443 1.00 47.31  ? 92   ASP C CA  1 
ATOM   2908  C  C   . ASP C  1 92  ? 125.704 -2.561  34.706 1.00 44.08  ? 92   ASP C C   1 
ATOM   2909  O  O   . ASP C  1 92  ? 124.561 -2.573  35.160 1.00 45.47  ? 92   ASP C O   1 
ATOM   2910  C  CB  . ASP C  1 92  ? 126.437 -0.307  35.581 1.00 57.99  ? 92   ASP C CB  1 
ATOM   2911  C  CG  . ASP C  1 92  ? 127.669 0.405   36.133 1.00 72.69  ? 92   ASP C CG  1 
ATOM   2912  O  OD1 . ASP C  1 92  ? 127.872 1.594   35.833 1.00 79.91  ? 92   ASP C OD1 1 
ATOM   2913  O  OD2 . ASP C  1 92  ? 128.418 -0.286  36.857 1.00 93.08  ? 92   ASP C OD2 1 
ATOM   2914  N  N   . GLY C  1 93  ? 126.045 -3.227  33.609 1.00 48.82  ? 93   GLY C N   1 
ATOM   2915  C  CA  . GLY C  1 93  ? 125.044 -4.056  32.947 1.00 55.57  ? 93   GLY C CA  1 
ATOM   2916  C  C   . GLY C  1 93  ? 124.150 -3.270  32.001 1.00 49.87  ? 93   GLY C C   1 
ATOM   2917  O  O   . GLY C  1 93  ? 123.098 -3.766  31.596 1.00 37.94  ? 93   GLY C O   1 
ATOM   2918  N  N   . VAL C  1 94  ? 124.569 -2.071  31.647 1.00 45.65  ? 94   VAL C N   1 
ATOM   2919  C  CA  . VAL C  1 94  ? 123.964 -1.188  30.675 1.00 41.51  ? 94   VAL C CA  1 
ATOM   2920  C  C   . VAL C  1 94  ? 124.667 -1.240  29.323 1.00 51.91  ? 94   VAL C C   1 
ATOM   2921  O  O   . VAL C  1 94  ? 125.845 -0.882  29.188 1.00 47.37  ? 94   VAL C O   1 
ATOM   2922  C  CB  . VAL C  1 94  ? 124.018 0.284   31.131 1.00 45.95  ? 94   VAL C CB  1 
ATOM   2923  C  CG1 . VAL C  1 94  ? 123.372 1.162   30.069 1.00 51.50  ? 94   VAL C CG1 1 
ATOM   2924  C  CG2 . VAL C  1 94  ? 123.361 0.473   32.487 1.00 48.88  ? 94   VAL C CG2 1 
ATOM   2925  N  N   . ALA C  1 95  ? 123.927 -1.689  28.314 1.00 40.47  ? 95   ALA C N   1 
ATOM   2926  C  CA  . ALA C  1 95  ? 124.446 -1.611  26.952 1.00 43.52  ? 95   ALA C CA  1 
ATOM   2927  C  C   . ALA C  1 95  ? 123.833 -0.395  26.259 1.00 55.47  ? 95   ALA C C   1 
ATOM   2928  O  O   . ALA C  1 95  ? 122.623 -0.154  26.302 1.00 51.18  ? 95   ALA C O   1 
ATOM   2929  C  CB  . ALA C  1 95  ? 124.213 -2.890  26.172 1.00 39.10  ? 95   ALA C CB  1 
ATOM   2930  N  N   . ASP C  1 96  ? 124.693 0.398   25.624 1.00 44.66  ? 96   ASP C N   1 
ATOM   2931  C  CA  . ASP C  1 96  ? 124.231 1.590   24.914 1.00 53.97  ? 96   ASP C CA  1 
ATOM   2932  C  C   . ASP C  1 96  ? 124.327 1.277   23.426 1.00 52.51  ? 96   ASP C C   1 
ATOM   2933  O  O   . ASP C  1 96  ? 125.408 1.311   22.843 1.00 63.32  ? 96   ASP C O   1 
ATOM   2934  C  CB  . ASP C  1 96  ? 125.044 2.823   25.274 1.00 74.19  ? 96   ASP C CB  1 
ATOM   2935  C  CG  . ASP C  1 96  ? 124.618 3.480   26.572 1.00 93.15  ? 96   ASP C CG  1 
ATOM   2936  O  OD1 . ASP C  1 96  ? 125.063 4.624   26.824 1.00 121.68 ? 96   ASP C OD1 1 
ATOM   2937  O  OD2 . ASP C  1 96  ? 123.842 2.862   27.329 1.00 110.32 ? 96   ASP C OD2 1 
ATOM   2938  N  N   . VAL C  1 97  ? 123.185 0.938   22.844 1.00 36.58  ? 97   VAL C N   1 
ATOM   2939  C  CA  . VAL C  1 97  ? 123.199 0.302   21.529 1.00 34.86  ? 97   VAL C CA  1 
ATOM   2940  C  C   . VAL C  1 97  ? 123.364 1.402   20.485 1.00 33.29  ? 97   VAL C C   1 
ATOM   2941  O  O   . VAL C  1 97  ? 122.730 2.453   20.607 1.00 38.64  ? 97   VAL C O   1 
ATOM   2942  C  CB  . VAL C  1 97  ? 121.929 -0.534  21.289 1.00 36.32  ? 97   VAL C CB  1 
ATOM   2943  C  CG1 . VAL C  1 97  ? 121.878 -1.163  19.912 1.00 40.33  ? 97   VAL C CG1 1 
ATOM   2944  C  CG2 . VAL C  1 97  ? 121.846 -1.633  22.342 1.00 31.44  ? 97   VAL C CG2 1 
ATOM   2945  N  N   . SER C  1 98  ? 124.234 1.122   19.517 1.00 44.07  ? 98   SER C N   1 
ATOM   2946  C  CA  . SER C  1 98  ? 124.450 2.059   18.416 1.00 45.79  ? 98   SER C CA  1 
ATOM   2947  C  C   . SER C  1 98  ? 124.907 1.262   17.205 1.00 50.49  ? 98   SER C C   1 
ATOM   2948  O  O   . SER C  1 98  ? 126.000 0.728   17.045 1.00 48.65  ? 98   SER C O   1 
ATOM   2949  C  CB  . SER C  1 98  ? 125.445 3.168   18.727 1.00 58.52  ? 98   SER C CB  1 
ATOM   2950  O  OG  . SER C  1 98  ? 125.299 4.236   17.796 1.00 71.14  ? 98   SER C OG  1 
ATOM   2951  N  N   . ILE C  1 99  ? 123.945 1.151   16.290 1.00 36.80  ? 99   ILE C N   1 
ATOM   2952  C  CA  . ILE C  1 99  ? 124.216 0.249   15.177 1.00 35.60  ? 99   ILE C CA  1 
ATOM   2953  C  C   . ILE C  1 99  ? 123.693 0.918   13.919 1.00 46.94  ? 99   ILE C C   1 
ATOM   2954  O  O   . ILE C  1 99  ? 122.646 1.565   13.960 1.00 47.67  ? 99   ILE C O   1 
ATOM   2955  C  CB  . ILE C  1 99  ? 123.553 -1.111  15.399 1.00 40.94  ? 99   ILE C CB  1 
ATOM   2956  C  CG1 . ILE C  1 99  ? 124.045 -1.867  16.639 1.00 50.30  ? 99   ILE C CG1 1 
ATOM   2957  C  CG2 . ILE C  1 99  ? 123.680 -1.994  14.167 1.00 48.01  ? 99   ILE C CG2 1 
ATOM   2958  C  CD1 . ILE C  1 99  ? 123.350 -3.198  16.848 1.00 56.61  ? 99   ILE C CD1 1 
ATOM   2959  N  N   . GLU C  1 100 ? 124.430 0.789   12.830 1.00 49.73  ? 100  GLU C N   1 
ATOM   2960  C  CA  . GLU C  1 100 ? 123.876 1.265   11.550 1.00 49.05  ? 100  GLU C CA  1 
ATOM   2961  C  C   . GLU C  1 100 ? 123.791 0.001   10.729 1.00 33.21  ? 100  GLU C C   1 
ATOM   2962  O  O   . GLU C  1 100 ? 124.747 -0.781  10.733 1.00 49.24  ? 100  GLU C O   1 
ATOM   2963  C  CB  . GLU C  1 100 ? 124.711 2.332   10.866 1.00 62.88  ? 100  GLU C CB  1 
ATOM   2964  C  CG  . GLU C  1 100 ? 124.216 3.754   11.040 1.00 74.94  ? 100  GLU C CG  1 
ATOM   2965  C  CD  . GLU C  1 100 ? 124.420 4.653   9.840  1.00 84.50  ? 100  GLU C CD  1 
ATOM   2966  O  OE1 . GLU C  1 100 ? 124.078 4.251   8.707  1.00 85.18  ? 100  GLU C OE1 1 
ATOM   2967  O  OE2 . GLU C  1 100 ? 124.920 5.787   10.021 1.00 94.42  ? 100  GLU C OE2 1 
ATOM   2968  N  N   . ASP C  1 101 ? 122.682 -0.273  10.045 1.00 32.96  ? 101  ASP C N   1 
ATOM   2969  C  CA  . ASP C  1 101 ? 122.676 -1.545  9.326  1.00 22.79  ? 101  ASP C CA  1 
ATOM   2970  C  C   . ASP C  1 101 ? 121.999 -1.447  7.966  1.00 41.50  ? 101  ASP C C   1 
ATOM   2971  O  O   . ASP C  1 101 ? 120.998 -0.736  7.850  1.00 40.95  ? 101  ASP C O   1 
ATOM   2972  C  CB  . ASP C  1 101 ? 121.915 -2.601  10.131 1.00 30.10  ? 101  ASP C CB  1 
ATOM   2973  C  CG  . ASP C  1 101 ? 122.169 -3.978  9.585  1.00 29.57  ? 101  ASP C CG  1 
ATOM   2974  O  OD1 . ASP C  1 101 ? 121.285 -4.614  8.986  1.00 42.51  ? 101  ASP C OD1 1 
ATOM   2975  O  OD2 . ASP C  1 101 ? 123.330 -4.443  9.745  1.00 52.74  ? 101  ASP C OD2 1 
ATOM   2976  N  N   . SER C  1 102 ? 122.519 -2.167  6.976  1.00 39.86  ? 102  SER C N   1 
ATOM   2977  C  CA  . SER C  1 102 ? 121.989 -1.970  5.620  1.00 48.49  ? 102  SER C CA  1 
ATOM   2978  C  C   . SER C  1 102 ? 121.422 -3.248  5.053  1.00 42.79  ? 102  SER C C   1 
ATOM   2979  O  O   . SER C  1 102 ? 121.075 -3.435  3.882  1.00 39.69  ? 102  SER C O   1 
ATOM   2980  C  CB  . SER C  1 102 ? 123.106 -1.412  4.724  1.00 45.06  ? 102  SER C CB  1 
ATOM   2981  O  OG  . SER C  1 102 ? 123.904 -2.494  4.251  1.00 47.91  ? 102  SER C OG  1 
ATOM   2982  N  N   . VAL C  1 103 ? 121.304 -4.250  5.937  1.00 32.94  ? 103  VAL C N   1 
ATOM   2983  C  CA  . VAL C  1 103 ? 120.741 -5.483  5.405  1.00 27.44  ? 103  VAL C CA  1 
ATOM   2984  C  C   . VAL C  1 103 ? 119.283 -5.578  5.872  1.00 45.49  ? 103  VAL C C   1 
ATOM   2985  O  O   . VAL C  1 103 ? 118.481 -6.172  5.152  1.00 53.26  ? 103  VAL C O   1 
ATOM   2986  C  CB  . VAL C  1 103 ? 121.483 -6.744  5.833  1.00 43.19  ? 103  VAL C CB  1 
ATOM   2987  C  CG1 . VAL C  1 103 ? 120.649 -7.965  5.470  1.00 37.07  ? 103  VAL C CG1 1 
ATOM   2988  C  CG2 . VAL C  1 103 ? 122.870 -6.768  5.188  1.00 43.81  ? 103  VAL C CG2 1 
ATOM   2989  N  N   . ILE C  1 104 ? 119.019 -4.998  7.052  1.00 35.04  ? 104  ILE C N   1 
ATOM   2990  C  CA  . ILE C  1 104 ? 117.621 -5.054  7.509  1.00 39.07  ? 104  ILE C CA  1 
ATOM   2991  C  C   . ILE C  1 104 ? 116.880 -3.842  6.941  1.00 36.86  ? 104  ILE C C   1 
ATOM   2992  O  O   . ILE C  1 104 ? 117.548 -2.860  6.614  1.00 34.12  ? 104  ILE C O   1 
ATOM   2993  C  CB  . ILE C  1 104 ? 117.456 -5.052  9.033  1.00 35.16  ? 104  ILE C CB  1 
ATOM   2994  C  CG1 . ILE C  1 104 ? 118.033 -3.822  9.739  1.00 34.58  ? 104  ILE C CG1 1 
ATOM   2995  C  CG2 . ILE C  1 104 ? 118.006 -6.317  9.680  1.00 32.91  ? 104  ILE C CG2 1 
ATOM   2996  C  CD1 . ILE C  1 104 ? 117.954 -3.933  11.252 1.00 52.73  ? 104  ILE C CD1 1 
ATOM   2997  N  N   . SER C  1 105 ? 115.547 -3.882  6.865  1.00 36.70  ? 105  SER C N   1 
ATOM   2998  C  CA  . SER C  1 105 ? 114.766 -2.737  6.433  1.00 33.64  ? 105  SER C CA  1 
ATOM   2999  C  C   . SER C  1 105 ? 113.445 -2.614  7.219  1.00 26.12  ? 105  SER C C   1 
ATOM   3000  O  O   . SER C  1 105 ? 113.026 -3.659  7.710  1.00 31.05  ? 105  SER C O   1 
ATOM   3001  C  CB  . SER C  1 105 ? 114.395 -2.818  4.939  1.00 37.19  ? 105  SER C CB  1 
ATOM   3002  O  OG  . SER C  1 105 ? 114.013 -1.509  4.509  1.00 38.72  ? 105  SER C OG  1 
ATOM   3003  N  N   . LEU C  1 106 ? 112.884 -1.427  7.284  1.00 29.82  ? 106  LEU C N   1 
ATOM   3004  C  CA  . LEU C  1 106 ? 111.592 -1.171  7.930  1.00 26.43  ? 106  LEU C CA  1 
ATOM   3005  C  C   . LEU C  1 106 ? 110.455 -1.211  6.902  1.00 35.04  ? 106  LEU C C   1 
ATOM   3006  O  O   . LEU C  1 106 ? 109.325 -0.881  7.262  1.00 34.72  ? 106  LEU C O   1 
ATOM   3007  C  CB  . LEU C  1 106 ? 111.598 0.159   8.660  1.00 23.79  ? 106  LEU C CB  1 
ATOM   3008  C  CG  . LEU C  1 106 ? 112.723 0.379   9.695  1.00 26.77  ? 106  LEU C CG  1 
ATOM   3009  C  CD1 . LEU C  1 106 ? 112.495 1.665   10.438 1.00 25.98  ? 106  LEU C CD1 1 
ATOM   3010  C  CD2 . LEU C  1 106 ? 112.799 -0.814  10.632 1.00 31.50  ? 106  LEU C CD2 1 
ATOM   3011  N  N   . SER C  1 107 ? 110.740 -1.606  5.669  1.00 30.02  ? 107  SER C N   1 
ATOM   3012  C  CA  . SER C  1 107 ? 109.751 -1.726  4.605  1.00 34.56  ? 107  SER C CA  1 
ATOM   3013  C  C   . SER C  1 107 ? 110.215 -2.715  3.552  1.00 43.37  ? 107  SER C C   1 
ATOM   3014  O  O   . SER C  1 107 ? 111.294 -3.308  3.561  1.00 34.14  ? 107  SER C O   1 
ATOM   3015  C  CB  . SER C  1 107 ? 109.437 -0.368  3.966  1.00 41.75  ? 107  SER C CB  1 
ATOM   3016  O  OG  . SER C  1 107 ? 110.523 0.188   3.243  1.00 41.89  ? 107  SER C OG  1 
ATOM   3017  N  N   . GLY C  1 108 ? 109.326 -2.919  2.574  1.00 45.71  ? 108  GLY C N   1 
ATOM   3018  C  CA  . GLY C  1 108 ? 109.666 -3.880  1.536  1.00 36.76  ? 108  GLY C CA  1 
ATOM   3019  C  C   . GLY C  1 108 ? 109.276 -5.272  1.986  1.00 35.92  ? 108  GLY C C   1 
ATOM   3020  O  O   . GLY C  1 108 ? 108.900 -5.453  3.142  1.00 49.45  ? 108  GLY C O   1 
ATOM   3021  N  N   . ASP C  1 109 ? 109.390 -6.197  1.054  1.00 45.86  ? 109  ASP C N   1 
ATOM   3022  C  CA  . ASP C  1 109 ? 109.013 -7.588  1.170  1.00 57.47  ? 109  ASP C CA  1 
ATOM   3023  C  C   . ASP C  1 109 ? 109.662 -8.255  2.372  1.00 61.98  ? 109  ASP C C   1 
ATOM   3024  O  O   . ASP C  1 109 ? 109.131 -9.228  2.911  1.00 66.53  ? 109  ASP C O   1 
ATOM   3025  C  CB  . ASP C  1 109 ? 109.411 -8.339  -0.109 1.00 64.28  ? 109  ASP C CB  1 
ATOM   3026  C  CG  . ASP C  1 109 ? 110.887 -8.156  -0.415 1.00 77.10  ? 109  ASP C CG  1 
ATOM   3027  O  OD1 . ASP C  1 109 ? 111.719 -8.410  0.484  1.00 88.34  ? 109  ASP C OD1 1 
ATOM   3028  O  OD2 . ASP C  1 109 ? 111.227 -7.753  -1.549 1.00 85.00  ? 109  ASP C OD2 1 
ATOM   3029  N  N   . HIS C  1 110 ? 110.821 -7.750  2.794  1.00 55.64  ? 110  HIS C N   1 
ATOM   3030  C  CA  . HIS C  1 110 ? 111.501 -8.456  3.890  1.00 50.63  ? 110  HIS C CA  1 
ATOM   3031  C  C   . HIS C  1 110 ? 111.724 -7.613  5.119  1.00 46.55  ? 110  HIS C C   1 
ATOM   3032  O  O   . HIS C  1 110 ? 112.745 -7.635  5.808  1.00 45.93  ? 110  HIS C O   1 
ATOM   3033  C  CB  . HIS C  1 110 ? 112.826 -9.000  3.334  1.00 47.73  ? 110  HIS C CB  1 
ATOM   3034  C  CG  . HIS C  1 110 ? 112.513 -10.198 2.479  1.00 61.54  ? 110  HIS C CG  1 
ATOM   3035  N  ND1 . HIS C  1 110 ? 113.094 -10.442 1.258  1.00 67.59  ? 110  HIS C ND1 1 
ATOM   3036  C  CD2 . HIS C  1 110 ? 111.635 -11.209 2.693  1.00 64.71  ? 110  HIS C CD2 1 
ATOM   3037  C  CE1 . HIS C  1 110 ? 112.604 -11.564 0.753  1.00 67.86  ? 110  HIS C CE1 1 
ATOM   3038  N  NE2 . HIS C  1 110 ? 111.714 -12.051 1.609  1.00 65.70  ? 110  HIS C NE2 1 
ATOM   3039  N  N   . CYS C  1 111 ? 110.726 -6.790  5.485  1.00 42.42  ? 111  CYS C N   1 
ATOM   3040  C  CA  . CYS C  1 111 ? 111.075 -5.962  6.639  1.00 38.67  ? 111  CYS C CA  1 
ATOM   3041  C  C   . CYS C  1 111 ? 110.892 -6.727  7.946  1.00 32.77  ? 111  CYS C C   1 
ATOM   3042  O  O   . CYS C  1 111 ? 110.416 -7.861  8.035  1.00 33.62  ? 111  CYS C O   1 
ATOM   3043  C  CB  . CYS C  1 111 ? 110.273 -4.663  6.643  1.00 44.33  ? 111  CYS C CB  1 
ATOM   3044  S  SG  . CYS C  1 111 ? 108.562 -4.978  7.111  1.00 54.59  ? 111  CYS C SG  1 
ATOM   3045  N  N   . ILE C  1 112 ? 111.341 -6.037  8.982  1.00 30.01  ? 112  ILE C N   1 
ATOM   3046  C  CA  . ILE C  1 112 ? 111.355 -6.634  10.309 1.00 32.97  ? 112  ILE C CA  1 
ATOM   3047  C  C   . ILE C  1 112 ? 110.244 -6.087  11.185 1.00 36.08  ? 112  ILE C C   1 
ATOM   3048  O  O   . ILE C  1 112 ? 110.180 -6.440  12.364 1.00 29.54  ? 112  ILE C O   1 
ATOM   3049  C  CB  . ILE C  1 112 ? 112.720 -6.344  10.966 1.00 27.16  ? 112  ILE C CB  1 
ATOM   3050  C  CG1 . ILE C  1 112 ? 113.001 -4.873  11.193 1.00 27.32  ? 112  ILE C CG1 1 
ATOM   3051  C  CG2 . ILE C  1 112 ? 113.816 -6.986  10.119 1.00 33.95  ? 112  ILE C CG2 1 
ATOM   3052  C  CD1 . ILE C  1 112 ? 114.271 -4.584  11.950 1.00 28.22  ? 112  ILE C CD1 1 
ATOM   3053  N  N   . ILE C  1 113 ? 109.388 -5.230  10.623 1.00 30.39  ? 113  ILE C N   1 
ATOM   3054  C  CA  . ILE C  1 113 ? 108.265 -4.751  11.454 1.00 26.29  ? 113  ILE C CA  1 
ATOM   3055  C  C   . ILE C  1 113 ? 107.453 -5.957  11.828 1.00 23.11  ? 113  ILE C C   1 
ATOM   3056  O  O   . ILE C  1 113 ? 107.230 -6.848  11.002 1.00 26.87  ? 113  ILE C O   1 
ATOM   3057  C  CB  . ILE C  1 113 ? 107.428 -3.710  10.712 1.00 31.18  ? 113  ILE C CB  1 
ATOM   3058  C  CG1 . ILE C  1 113 ? 108.183 -2.445  10.288 1.00 32.63  ? 113  ILE C CG1 1 
ATOM   3059  C  CG2 . ILE C  1 113 ? 106.202 -3.346  11.538 1.00 26.65  ? 113  ILE C CG2 1 
ATOM   3060  C  CD1 . ILE C  1 113 ? 108.618 -1.563  11.435 1.00 32.57  ? 113  ILE C CD1 1 
ATOM   3061  N  N   . GLY C  1 114 ? 106.963 -6.104  13.071 1.00 24.70  ? 114  GLY C N   1 
ATOM   3062  C  CA  . GLY C  1 114 ? 106.174 -7.312  13.300 1.00 20.02  ? 114  GLY C CA  1 
ATOM   3063  C  C   . GLY C  1 114 ? 106.918 -8.551  13.693 1.00 24.56  ? 114  GLY C C   1 
ATOM   3064  O  O   . GLY C  1 114 ? 106.328 -9.592  13.993 1.00 22.69  ? 114  GLY C O   1 
ATOM   3065  N  N   . ARG C  1 115 ? 108.260 -8.476  13.686 1.00 21.06  ? 115  ARG C N   1 
ATOM   3066  C  CA  . ARG C  1 115 ? 109.020 -9.651  14.103 1.00 27.10  ? 115  ARG C CA  1 
ATOM   3067  C  C   . ARG C  1 115 ? 109.558 -9.362  15.502 1.00 25.95  ? 115  ARG C C   1 
ATOM   3068  O  O   . ARG C  1 115 ? 109.162 -8.349  16.079 1.00 25.47  ? 115  ARG C O   1 
ATOM   3069  C  CB  . ARG C  1 115 ? 110.146 -9.991  13.106 1.00 25.82  ? 115  ARG C CB  1 
ATOM   3070  C  CG  . ARG C  1 115 ? 109.613 -9.888  11.676 1.00 30.19  ? 115  ARG C CG  1 
ATOM   3071  C  CD  . ARG C  1 115 ? 110.080 -10.980 10.758 1.00 40.66  ? 115  ARG C CD  1 
ATOM   3072  N  NE  . ARG C  1 115 ? 109.570 -10.842 9.375  1.00 31.51  ? 115  ARG C NE  1 
ATOM   3073  C  CZ  . ARG C  1 115 ? 109.000 -11.900 8.812  1.00 30.50  ? 115  ARG C CZ  1 
ATOM   3074  N  NH1 . ARG C  1 115 ? 108.522 -11.882 7.579  1.00 32.58  ? 115  ARG C NH1 1 
ATOM   3075  N  NH2 . ARG C  1 115 ? 108.922 -13.015 9.540  1.00 31.28  ? 115  ARG C NH2 1 
ATOM   3076  N  N   . THR C  1 116 ? 110.420 -10.228 16.028 1.00 24.58  ? 116  THR C N   1 
ATOM   3077  C  CA  . THR C  1 116 ? 110.886 -10.067 17.405 1.00 27.52  ? 116  THR C CA  1 
ATOM   3078  C  C   . THR C  1 116 ? 112.380 -9.769  17.530 1.00 30.47  ? 116  THR C C   1 
ATOM   3079  O  O   . THR C  1 116 ? 113.187 -10.509 16.972 1.00 32.66  ? 116  THR C O   1 
ATOM   3080  C  CB  . THR C  1 116 ? 110.564 -11.362 18.177 1.00 31.05  ? 116  THR C CB  1 
ATOM   3081  O  OG1 . THR C  1 116 ? 109.139 -11.464 18.314 1.00 27.69  ? 116  THR C OG1 1 
ATOM   3082  C  CG2 . THR C  1 116 ? 111.141 -11.341 19.586 1.00 30.12  ? 116  THR C CG2 1 
ATOM   3083  N  N   . LEU C  1 117 ? 112.726 -8.716  18.255 1.00 29.05  ? 117  LEU C N   1 
ATOM   3084  C  CA  . LEU C  1 117 ? 114.139 -8.470  18.613 1.00 27.22  ? 117  LEU C CA  1 
ATOM   3085  C  C   . LEU C  1 117 ? 114.492 -9.255  19.884 1.00 37.29  ? 117  LEU C C   1 
ATOM   3086  O  O   . LEU C  1 117 ? 113.730 -9.180  20.853 1.00 26.30  ? 117  LEU C O   1 
ATOM   3087  C  CB  . LEU C  1 117 ? 114.332 -7.005  18.819 1.00 25.70  ? 117  LEU C CB  1 
ATOM   3088  C  CG  . LEU C  1 117 ? 115.701 -6.402  19.082 1.00 25.35  ? 117  LEU C CG  1 
ATOM   3089  C  CD1 . LEU C  1 117 ? 116.618 -6.710  17.903 1.00 37.38  ? 117  LEU C CD1 1 
ATOM   3090  C  CD2 . LEU C  1 117 ? 115.555 -4.914  19.294 1.00 24.54  ? 117  LEU C CD2 1 
ATOM   3091  N  N   . VAL C  1 118 ? 115.606 -9.991  19.888 1.00 26.53  ? 118  VAL C N   1 
ATOM   3092  C  CA  . VAL C  1 118 ? 115.990 -10.781 21.061 1.00 27.55  ? 118  VAL C CA  1 
ATOM   3093  C  C   . VAL C  1 118 ? 117.388 -10.401 21.553 1.00 42.27  ? 118  VAL C C   1 
ATOM   3094  O  O   . VAL C  1 118 ? 118.301 -10.166 20.745 1.00 34.06  ? 118  VAL C O   1 
ATOM   3095  C  CB  . VAL C  1 118 ? 115.956 -12.281 20.754 1.00 28.99  ? 118  VAL C CB  1 
ATOM   3096  C  CG1 . VAL C  1 118 ? 116.360 -13.112 21.976 1.00 35.79  ? 118  VAL C CG1 1 
ATOM   3097  C  CG2 . VAL C  1 118 ? 114.591 -12.791 20.311 1.00 28.56  ? 118  VAL C CG2 1 
ATOM   3098  N  N   . VAL C  1 119 ? 117.589 -10.316 22.864 1.00 31.57  ? 119  VAL C N   1 
ATOM   3099  C  CA  . VAL C  1 119 ? 118.959 -10.150 23.421 1.00 32.92  ? 119  VAL C CA  1 
ATOM   3100  C  C   . VAL C  1 119 ? 119.310 -11.423 24.169 1.00 39.10  ? 119  VAL C C   1 
ATOM   3101  O  O   . VAL C  1 119 ? 118.501 -12.134 24.773 1.00 28.94  ? 119  VAL C O   1 
ATOM   3102  C  CB  . VAL C  1 119 ? 119.101 -8.856  24.229 1.00 31.59  ? 119  VAL C CB  1 
ATOM   3103  C  CG1 . VAL C  1 119 ? 118.282 -8.822  25.510 1.00 28.26  ? 119  VAL C CG1 1 
ATOM   3104  C  CG2 . VAL C  1 119 ? 120.572 -8.585  24.569 1.00 37.56  ? 119  VAL C CG2 1 
ATOM   3105  N  N   . HIS C  1 120 ? 120.580 -11.852 24.090 1.00 33.64  ? 120  HIS C N   1 
ATOM   3106  C  CA  . HIS C  1 120 ? 120.837 -13.241 24.469 1.00 32.06  ? 120  HIS C CA  1 
ATOM   3107  C  C   . HIS C  1 120 ? 121.731 -13.308 25.713 1.00 34.21  ? 120  HIS C C   1 
ATOM   3108  O  O   . HIS C  1 120 ? 122.226 -12.305 26.225 1.00 33.45  ? 120  HIS C O   1 
ATOM   3109  C  CB  . HIS C  1 120 ? 121.455 -14.028 23.326 1.00 36.89  ? 120  HIS C CB  1 
ATOM   3110  C  CG  . HIS C  1 120 ? 120.532 -14.499 22.250 1.00 33.25  ? 120  HIS C CG  1 
ATOM   3111  N  ND1 . HIS C  1 120 ? 120.025 -15.777 22.228 1.00 30.65  ? 120  HIS C ND1 1 
ATOM   3112  C  CD2 . HIS C  1 120 ? 120.039 -13.880 21.142 1.00 27.43  ? 120  HIS C CD2 1 
ATOM   3113  C  CE1 . HIS C  1 120 ? 119.249 -15.932 21.161 1.00 36.81  ? 120  HIS C CE1 1 
ATOM   3114  N  NE2 . HIS C  1 120 ? 119.244 -14.787 20.491 1.00 31.01  ? 120  HIS C NE2 1 
ATOM   3115  N  N   . GLU C  1 121 ? 121.878 -14.535 26.195 1.00 36.56  ? 121  GLU C N   1 
ATOM   3116  C  CA  . GLU C  1 121 ? 122.572 -14.747 27.467 1.00 40.91  ? 121  GLU C CA  1 
ATOM   3117  C  C   . GLU C  1 121 ? 124.084 -14.608 27.281 1.00 42.67  ? 121  GLU C C   1 
ATOM   3118  O  O   . GLU C  1 121 ? 124.749 -13.966 28.093 1.00 38.42  ? 121  GLU C O   1 
ATOM   3119  C  CB  . GLU C  1 121 ? 122.184 -16.128 27.982 1.00 44.69  ? 121  GLU C CB  1 
ATOM   3120  C  CG  . GLU C  1 121 ? 123.305 -16.895 28.652 1.00 53.46  ? 121  GLU C CG  1 
ATOM   3121  C  CD  . GLU C  1 121 ? 122.952 -18.345 28.920 1.00 52.97  ? 121  GLU C CD  1 
ATOM   3122  O  OE1 . GLU C  1 121 ? 122.924 -18.709 30.117 1.00 86.59  ? 121  GLU C OE1 1 
ATOM   3123  O  OE2 . GLU C  1 121 ? 122.714 -19.113 27.962 1.00 41.41  ? 121  GLU C OE2 1 
ATOM   3124  N  N   . LYS C  1 122 ? 124.558 -15.193 26.190 1.00 38.97  ? 122  LYS C N   1 
ATOM   3125  C  CA  . LYS C  1 122 ? 125.968 -15.231 25.829 1.00 50.69  ? 122  LYS C CA  1 
ATOM   3126  C  C   . LYS C  1 122 ? 126.352 -14.374 24.635 1.00 59.28  ? 122  LYS C C   1 
ATOM   3127  O  O   . LYS C  1 122 ? 125.559 -13.790 23.896 1.00 40.83  ? 122  LYS C O   1 
ATOM   3128  C  CB  . LYS C  1 122 ? 126.338 -16.698 25.521 1.00 53.29  ? 122  LYS C CB  1 
ATOM   3129  C  CG  . LYS C  1 122 ? 126.497 -17.534 26.782 1.00 67.45  ? 122  LYS C CG  1 
ATOM   3130  C  CD  . LYS C  1 122 ? 127.344 -18.769 26.525 1.00 80.60  ? 122  LYS C CD  1 
ATOM   3131  C  CE  . LYS C  1 122 ? 126.513 -19.891 25.921 1.00 88.89  ? 122  LYS C CE  1 
ATOM   3132  N  NZ  . LYS C  1 122 ? 126.685 -19.957 24.442 1.00 109.49 ? 122  LYS C NZ  1 
ATOM   3133  N  N   . ALA C  1 123 ? 127.662 -14.276 24.375 1.00 56.07  ? 123  ALA C N   1 
ATOM   3134  C  CA  . ALA C  1 123 ? 128.102 -13.517 23.210 1.00 56.78  ? 123  ALA C CA  1 
ATOM   3135  C  C   . ALA C  1 123 ? 127.778 -14.245 21.910 1.00 47.99  ? 123  ALA C C   1 
ATOM   3136  O  O   . ALA C  1 123 ? 127.708 -15.476 21.830 1.00 35.18  ? 123  ALA C O   1 
ATOM   3137  C  CB  . ALA C  1 123 ? 129.596 -13.222 23.269 1.00 52.65  ? 123  ALA C CB  1 
ATOM   3138  N  N   . ASP C  1 124 ? 127.576 -13.423 20.869 1.00 37.58  ? 124  ASP C N   1 
ATOM   3139  C  CA  . ASP C  1 124 ? 127.432 -14.011 19.544 1.00 41.36  ? 124  ASP C CA  1 
ATOM   3140  C  C   . ASP C  1 124 ? 128.866 -14.252 19.041 1.00 40.76  ? 124  ASP C C   1 
ATOM   3141  O  O   . ASP C  1 124 ? 129.606 -13.277 19.225 1.00 40.66  ? 124  ASP C O   1 
ATOM   3142  C  CB  . ASP C  1 124 ? 126.675 -13.102 18.586 1.00 43.88  ? 124  ASP C CB  1 
ATOM   3143  C  CG  . ASP C  1 124 ? 126.207 -13.777 17.319 1.00 50.64  ? 124  ASP C CG  1 
ATOM   3144  O  OD1 . ASP C  1 124 ? 125.073 -13.505 16.862 1.00 66.25  ? 124  ASP C OD1 1 
ATOM   3145  O  OD2 . ASP C  1 124 ? 126.941 -14.592 16.726 1.00 44.11  ? 124  ASP C OD2 1 
ATOM   3146  N  N   . ASP C  1 125 ? 129.108 -15.438 18.518 1.00 33.74  ? 125  ASP C N   1 
ATOM   3147  C  CA  . ASP C  1 125 ? 130.445 -15.798 18.023 1.00 45.77  ? 125  ASP C CA  1 
ATOM   3148  C  C   . ASP C  1 125 ? 130.583 -15.398 16.556 1.00 56.77  ? 125  ASP C C   1 
ATOM   3149  O  O   . ASP C  1 125 ? 131.470 -15.834 15.822 1.00 62.21  ? 125  ASP C O   1 
ATOM   3150  C  CB  . ASP C  1 125 ? 130.733 -17.279 18.207 1.00 38.17  ? 125  ASP C CB  1 
ATOM   3151  C  CG  . ASP C  1 125 ? 130.000 -18.275 17.361 1.00 43.84  ? 125  ASP C CG  1 
ATOM   3152  O  OD1 . ASP C  1 125 ? 130.057 -19.504 17.651 1.00 43.92  ? 125  ASP C OD1 1 
ATOM   3153  O  OD2 . ASP C  1 125 ? 129.340 -17.894 16.369 1.00 57.41  ? 125  ASP C OD2 1 
ATOM   3154  N  N   . LEU C  1 126 ? 129.647 -14.569 16.117 1.00 50.25  ? 126  LEU C N   1 
ATOM   3155  C  CA  . LEU C  1 126 ? 129.515 -14.057 14.766 1.00 38.91  ? 126  LEU C CA  1 
ATOM   3156  C  C   . LEU C  1 126 ? 129.550 -15.146 13.713 1.00 31.24  ? 126  LEU C C   1 
ATOM   3157  O  O   . LEU C  1 126 ? 129.832 -14.886 12.541 1.00 59.43  ? 126  LEU C O   1 
ATOM   3158  C  CB  . LEU C  1 126 ? 130.617 -13.007 14.544 1.00 36.50  ? 126  LEU C CB  1 
ATOM   3159  C  CG  . LEU C  1 126 ? 130.581 -11.922 15.632 1.00 45.05  ? 126  LEU C CG  1 
ATOM   3160  C  CD1 . LEU C  1 126 ? 131.579 -10.817 15.344 1.00 38.01  ? 126  LEU C CD1 1 
ATOM   3161  C  CD2 . LEU C  1 126 ? 129.168 -11.366 15.783 1.00 36.25  ? 126  LEU C CD2 1 
ATOM   3162  N  N   . GLY C  1 127 ? 129.241 -16.377 14.073 1.00 29.72  ? 127  GLY C N   1 
ATOM   3163  C  CA  . GLY C  1 127 ? 129.023 -17.480 13.180 1.00 24.71  ? 127  GLY C CA  1 
ATOM   3164  C  C   . GLY C  1 127 ? 130.221 -18.363 12.920 1.00 59.59  ? 127  GLY C C   1 
ATOM   3165  O  O   . GLY C  1 127 ? 130.137 -19.304 12.125 1.00 84.18  ? 127  GLY C O   1 
ATOM   3166  N  N   . LYS C  1 128 ? 131.337 -18.081 13.579 1.00 63.99  ? 128  LYS C N   1 
ATOM   3167  C  CA  . LYS C  1 128 ? 132.564 -18.840 13.335 1.00 74.63  ? 128  LYS C CA  1 
ATOM   3168  C  C   . LYS C  1 128 ? 132.866 -19.806 14.474 1.00 82.33  ? 128  LYS C C   1 
ATOM   3169  O  O   . LYS C  1 128 ? 133.970 -19.814 15.025 1.00 111.78 ? 128  LYS C O   1 
ATOM   3170  C  CB  . LYS C  1 128 ? 133.716 -17.852 13.118 1.00 74.83  ? 128  LYS C CB  1 
ATOM   3171  C  CG  . LYS C  1 128 ? 133.694 -17.204 11.740 1.00 74.74  ? 128  LYS C CG  1 
ATOM   3172  C  CD  . LYS C  1 128 ? 133.376 -15.722 11.811 1.00 73.34  ? 128  LYS C CD  1 
ATOM   3173  C  CE  . LYS C  1 128 ? 132.619 -15.273 10.565 1.00 70.29  ? 128  LYS C CE  1 
ATOM   3174  N  NZ  . LYS C  1 128 ? 131.793 -14.065 10.851 1.00 53.11  ? 128  LYS C NZ  1 
ATOM   3175  N  N   . GLY C  1 129 ? 131.881 -20.620 14.838 1.00 70.17  ? 129  GLY C N   1 
ATOM   3176  C  CA  . GLY C  1 129 ? 132.010 -21.514 15.965 1.00 69.73  ? 129  GLY C CA  1 
ATOM   3177  C  C   . GLY C  1 129 ? 132.898 -22.708 15.696 1.00 72.02  ? 129  GLY C C   1 
ATOM   3178  O  O   . GLY C  1 129 ? 133.909 -22.892 16.377 1.00 83.85  ? 129  GLY C O   1 
ATOM   3179  N  N   . GLY C  1 130 ? 132.521 -23.527 14.723 1.00 70.91  ? 130  GLY C N   1 
ATOM   3180  C  CA  . GLY C  1 130 ? 133.204 -24.771 14.414 1.00 70.05  ? 130  GLY C CA  1 
ATOM   3181  C  C   . GLY C  1 130 ? 132.247 -25.952 14.535 1.00 75.27  ? 130  GLY C C   1 
ATOM   3182  O  O   . GLY C  1 130 ? 132.621 -27.104 14.315 1.00 84.48  ? 130  GLY C O   1 
ATOM   3183  N  N   . ASN C  1 131 ? 131.018 -25.621 14.888 1.00 75.14  ? 131  ASN C N   1 
ATOM   3184  C  CA  . ASN C  1 131 ? 129.903 -26.503 15.169 1.00 70.05  ? 131  ASN C CA  1 
ATOM   3185  C  C   . ASN C  1 131 ? 128.626 -26.015 14.485 1.00 62.98  ? 131  ASN C C   1 
ATOM   3186  O  O   . ASN C  1 131 ? 128.423 -24.798 14.450 1.00 79.77  ? 131  ASN C O   1 
ATOM   3187  C  CB  . ASN C  1 131 ? 129.693 -26.572 16.686 1.00 68.30  ? 131  ASN C CB  1 
ATOM   3188  C  CG  . ASN C  1 131 ? 130.035 -25.247 17.346 1.00 69.40  ? 131  ASN C CG  1 
ATOM   3189  O  OD1 . ASN C  1 131 ? 129.840 -24.183 16.755 1.00 71.20  ? 131  ASN C OD1 1 
ATOM   3190  N  ND2 . ASN C  1 131 ? 130.545 -25.297 18.570 1.00 60.56  ? 131  ASN C ND2 1 
ATOM   3191  N  N   . GLU C  1 132 ? 127.811 -26.923 13.969 1.00 59.71  ? 132  GLU C N   1 
ATOM   3192  C  CA  . GLU C  1 132 ? 126.596 -26.584 13.234 1.00 75.61  ? 132  GLU C CA  1 
ATOM   3193  C  C   . GLU C  1 132 ? 125.769 -25.517 13.945 1.00 76.88  ? 132  GLU C C   1 
ATOM   3194  O  O   . GLU C  1 132 ? 125.297 -24.561 13.325 1.00 73.07  ? 132  GLU C O   1 
ATOM   3195  C  CB  . GLU C  1 132 ? 125.752 -27.838 12.990 1.00 81.53  ? 132  GLU C CB  1 
ATOM   3196  C  CG  . GLU C  1 132 ? 125.145 -28.444 14.244 1.00 86.56  ? 132  GLU C CG  1 
ATOM   3197  C  CD  . GLU C  1 132 ? 123.961 -29.339 13.922 1.00 96.39  ? 132  GLU C CD  1 
ATOM   3198  O  OE1 . GLU C  1 132 ? 123.742 -29.616 12.723 1.00 117.34 ? 132  GLU C OE1 1 
ATOM   3199  O  OE2 . GLU C  1 132 ? 123.260 -29.762 14.864 1.00 109.55 ? 132  GLU C OE2 1 
ATOM   3200  N  N   . GLU C  1 133 ? 125.615 -25.661 15.254 1.00 70.29  ? 133  GLU C N   1 
ATOM   3201  C  CA  . GLU C  1 133 ? 124.927 -24.674 16.075 1.00 67.97  ? 133  GLU C CA  1 
ATOM   3202  C  C   . GLU C  1 133 ? 125.466 -23.276 15.805 1.00 61.04  ? 133  GLU C C   1 
ATOM   3203  O  O   . GLU C  1 133 ? 124.735 -22.276 15.818 1.00 51.99  ? 133  GLU C O   1 
ATOM   3204  C  CB  . GLU C  1 133 ? 125.083 -25.051 17.548 1.00 69.06  ? 133  GLU C CB  1 
ATOM   3205  C  CG  . GLU C  1 133 ? 124.155 -24.336 18.506 1.00 71.78  ? 133  GLU C CG  1 
ATOM   3206  C  CD  . GLU C  1 133 ? 122.721 -24.267 18.027 1.00 75.01  ? 133  GLU C CD  1 
ATOM   3207  O  OE1 . GLU C  1 133 ? 122.153 -23.156 18.084 1.00 70.63  ? 133  GLU C OE1 1 
ATOM   3208  O  OE2 . GLU C  1 133 ? 122.168 -25.301 17.600 1.00 77.78  ? 133  GLU C OE2 1 
ATOM   3209  N  N   . SER C  1 134 ? 126.777 -23.192 15.543 1.00 42.20  ? 134  SER C N   1 
ATOM   3210  C  CA  . SER C  1 134 ? 127.351 -21.889 15.250 1.00 39.44  ? 134  SER C CA  1 
ATOM   3211  C  C   . SER C  1 134 ? 126.707 -21.330 13.975 1.00 33.79  ? 134  SER C C   1 
ATOM   3212  O  O   . SER C  1 134 ? 126.629 -20.116 13.836 1.00 43.12  ? 134  SER C O   1 
ATOM   3213  C  CB  . SER C  1 134 ? 128.866 -21.905 15.042 1.00 42.55  ? 134  SER C CB  1 
ATOM   3214  O  OG  . SER C  1 134 ? 129.372 -20.582 14.948 1.00 52.99  ? 134  SER C OG  1 
ATOM   3215  N  N   . THR C  1 135 ? 126.281 -22.240 13.113 1.00 50.65  ? 135  THR C N   1 
ATOM   3216  C  CA  . THR C  1 135 ? 125.660 -21.892 11.842 1.00 69.85  ? 135  THR C CA  1 
ATOM   3217  C  C   . THR C  1 135 ? 124.237 -21.365 12.045 1.00 68.89  ? 135  THR C C   1 
ATOM   3218  O  O   . THR C  1 135 ? 123.824 -20.397 11.411 1.00 67.86  ? 135  THR C O   1 
ATOM   3219  C  CB  . THR C  1 135 ? 125.620 -23.097 10.884 1.00 72.64  ? 135  THR C CB  1 
ATOM   3220  O  OG1 . THR C  1 135 ? 126.490 -24.127 11.372 1.00 101.89 ? 135  THR C OG1 1 
ATOM   3221  C  CG2 . THR C  1 135 ? 126.144 -22.693 9.516  1.00 78.52  ? 135  THR C CG2 1 
ATOM   3222  N  N   . LYS C  1 136 ? 123.521 -22.033 12.936 1.00 60.52  ? 136  LYS C N   1 
ATOM   3223  C  CA  . LYS C  1 136 ? 122.194 -21.680 13.382 1.00 51.65  ? 136  LYS C CA  1 
ATOM   3224  C  C   . LYS C  1 136 ? 122.146 -20.382 14.165 1.00 53.65  ? 136  LYS C C   1 
ATOM   3225  O  O   . LYS C  1 136 ? 121.585 -19.344 13.829 1.00 44.68  ? 136  LYS C O   1 
ATOM   3226  C  CB  . LYS C  1 136 ? 121.702 -22.803 14.299 1.00 55.99  ? 136  LYS C CB  1 
ATOM   3227  C  CG  . LYS C  1 136 ? 121.810 -24.187 13.681 1.00 56.23  ? 136  LYS C CG  1 
ATOM   3228  C  CD  . LYS C  1 136 ? 120.405 -24.753 13.510 1.00 48.39  ? 136  LYS C CD  1 
ATOM   3229  C  CE  . LYS C  1 136 ? 120.373 -25.718 12.338 1.00 59.82  ? 136  LYS C CE  1 
ATOM   3230  N  NZ  . LYS C  1 136 ? 121.629 -26.519 12.255 1.00 92.12  ? 136  LYS C NZ  1 
ATOM   3231  N  N   . THR C  1 137 ? 122.790 -20.450 15.333 1.00 54.98  ? 137  THR C N   1 
ATOM   3232  C  CA  . THR C  1 137 ? 122.588 -19.408 16.318 1.00 50.75  ? 137  THR C CA  1 
ATOM   3233  C  C   . THR C  1 137 ? 123.814 -18.624 16.708 1.00 48.24  ? 137  THR C C   1 
ATOM   3234  O  O   . THR C  1 137 ? 123.683 -17.549 17.301 1.00 41.96  ? 137  THR C O   1 
ATOM   3235  C  CB  . THR C  1 137 ? 122.067 -20.083 17.616 1.00 55.22  ? 137  THR C CB  1 
ATOM   3236  O  OG1 . THR C  1 137 ? 123.053 -21.043 18.012 1.00 49.73  ? 137  THR C OG1 1 
ATOM   3237  C  CG2 . THR C  1 137 ? 120.781 -20.831 17.341 1.00 38.49  ? 137  THR C CG2 1 
ATOM   3238  N  N   . GLY C  1 138 ? 125.024 -19.124 16.440 1.00 48.67  ? 138  GLY C N   1 
ATOM   3239  C  CA  . GLY C  1 138 ? 126.179 -18.387 16.945 1.00 37.23  ? 138  GLY C CA  1 
ATOM   3240  C  C   . GLY C  1 138 ? 126.456 -18.667 18.418 1.00 32.01  ? 138  GLY C C   1 
ATOM   3241  O  O   . GLY C  1 138 ? 127.147 -17.861 19.060 1.00 37.18  ? 138  GLY C O   1 
ATOM   3242  N  N   . ASN C  1 139 ? 125.926 -19.758 18.951 1.00 37.37  ? 139  ASN C N   1 
ATOM   3243  C  CA  . ASN C  1 139 ? 126.085 -20.096 20.372 1.00 44.53  ? 139  ASN C CA  1 
ATOM   3244  C  C   . ASN C  1 139 ? 125.801 -18.944 21.320 1.00 53.66  ? 139  ASN C C   1 
ATOM   3245  O  O   . ASN C  1 139 ? 126.519 -18.689 22.296 1.00 36.43  ? 139  ASN C O   1 
ATOM   3246  C  CB  . ASN C  1 139 ? 127.513 -20.645 20.589 1.00 36.60  ? 139  ASN C CB  1 
ATOM   3247  C  CG  . ASN C  1 139 ? 127.729 -21.883 19.738 1.00 38.17  ? 139  ASN C CG  1 
ATOM   3248  O  OD1 . ASN C  1 139 ? 127.137 -22.940 19.973 1.00 43.58  ? 139  ASN C OD1 1 
ATOM   3249  N  ND2 . ASN C  1 139 ? 128.578 -21.739 18.720 1.00 55.87  ? 139  ASN C ND2 1 
ATOM   3250  N  N   . ALA C  1 140 ? 124.724 -18.178 21.093 1.00 46.13  ? 140  ALA C N   1 
ATOM   3251  C  CA  . ALA C  1 140 ? 124.482 -16.995 21.917 1.00 34.85  ? 140  ALA C CA  1 
ATOM   3252  C  C   . ALA C  1 140 ? 123.655 -17.338 23.162 1.00 29.93  ? 140  ALA C C   1 
ATOM   3253  O  O   . ALA C  1 140 ? 123.401 -16.507 24.035 1.00 39.83  ? 140  ALA C O   1 
ATOM   3254  C  CB  . ALA C  1 140 ? 123.781 -15.903 21.114 1.00 31.95  ? 140  ALA C CB  1 
ATOM   3255  N  N   . GLY C  1 141 ? 123.273 -18.608 23.201 1.00 32.90  ? 141  GLY C N   1 
ATOM   3256  C  CA  . GLY C  1 141 ? 122.651 -19.069 24.429 1.00 51.03  ? 141  GLY C CA  1 
ATOM   3257  C  C   . GLY C  1 141 ? 121.182 -18.711 24.503 1.00 52.60  ? 141  GLY C C   1 
ATOM   3258  O  O   . GLY C  1 141 ? 120.500 -18.460 23.515 1.00 38.38  ? 141  GLY C O   1 
ATOM   3259  N  N   . SER C  1 142 ? 120.678 -18.711 25.733 1.00 45.29  ? 142  SER C N   1 
ATOM   3260  C  CA  . SER C  1 142 ? 119.231 -18.558 25.894 1.00 39.64  ? 142  SER C CA  1 
ATOM   3261  C  C   . SER C  1 142 ? 118.852 -17.099 25.738 1.00 35.76  ? 142  SER C C   1 
ATOM   3262  O  O   . SER C  1 142 ? 119.659 -16.169 25.751 1.00 38.17  ? 142  SER C O   1 
ATOM   3263  C  CB  . SER C  1 142 ? 118.828 -19.166 27.246 1.00 38.83  ? 142  SER C CB  1 
ATOM   3264  O  OG  . SER C  1 142 ? 119.280 -18.301 28.267 1.00 36.78  ? 142  SER C OG  1 
ATOM   3265  N  N   . ARG C  1 143 ? 117.540 -16.924 25.568 1.00 31.97  ? 143  ARG C N   1 
ATOM   3266  C  CA  . ARG C  1 143 ? 116.962 -15.646 25.243 1.00 26.18  ? 143  ARG C CA  1 
ATOM   3267  C  C   . ARG C  1 143 ? 116.559 -14.935 26.527 1.00 34.38  ? 143  ARG C C   1 
ATOM   3268  O  O   . ARG C  1 143 ? 115.647 -15.456 27.175 1.00 33.86  ? 143  ARG C O   1 
ATOM   3269  C  CB  . ARG C  1 143 ? 115.738 -15.858 24.333 1.00 32.97  ? 143  ARG C CB  1 
ATOM   3270  C  CG  . ARG C  1 143 ? 115.966 -16.919 23.274 1.00 34.17  ? 143  ARG C CG  1 
ATOM   3271  C  CD  . ARG C  1 143 ? 114.892 -17.020 22.224 1.00 32.62  ? 143  ARG C CD  1 
ATOM   3272  N  NE  . ARG C  1 143 ? 115.240 -17.929 21.149 1.00 36.64  ? 143  ARG C NE  1 
ATOM   3273  C  CZ  . ARG C  1 143 ? 114.527 -18.346 20.126 1.00 45.08  ? 143  ARG C CZ  1 
ATOM   3274  N  NH1 . ARG C  1 143 ? 115.067 -19.192 19.252 1.00 32.38  ? 143  ARG C NH1 1 
ATOM   3275  N  NH2 . ARG C  1 143 ? 113.274 -17.932 19.959 1.00 35.26  ? 143  ARG C NH2 1 
ATOM   3276  N  N   . LEU C  1 144 ? 117.197 -13.835 26.863 1.00 33.91  ? 144  LEU C N   1 
ATOM   3277  C  CA  . LEU C  1 144 ? 117.017 -13.107 28.091 1.00 31.41  ? 144  LEU C CA  1 
ATOM   3278  C  C   . LEU C  1 144 ? 115.845 -12.126 28.052 1.00 35.44  ? 144  LEU C C   1 
ATOM   3279  O  O   . LEU C  1 144 ? 115.142 -12.004 29.054 1.00 30.32  ? 144  LEU C O   1 
ATOM   3280  C  CB  . LEU C  1 144 ? 118.253 -12.265 28.433 1.00 31.64  ? 144  LEU C CB  1 
ATOM   3281  C  CG  . LEU C  1 144 ? 119.603 -12.989 28.442 1.00 41.10  ? 144  LEU C CG  1 
ATOM   3282  C  CD1 . LEU C  1 144 ? 120.629 -12.172 29.218 1.00 39.85  ? 144  LEU C CD1 1 
ATOM   3283  C  CD2 . LEU C  1 144 ? 119.466 -14.383 29.020 1.00 37.36  ? 144  LEU C CD2 1 
ATOM   3284  N  N   . ALA C  1 145 ? 115.680 -11.398 26.953 1.00 29.62  ? 145  ALA C N   1 
ATOM   3285  C  CA  . ALA C  1 145 ? 114.577 -10.436 26.849 1.00 22.82  ? 145  ALA C CA  1 
ATOM   3286  C  C   . ALA C  1 145 ? 114.190 -10.329 25.376 1.00 36.58  ? 145  ALA C C   1 
ATOM   3287  O  O   . ALA C  1 145 ? 115.021 -10.610 24.514 1.00 28.54  ? 145  ALA C O   1 
ATOM   3288  C  CB  . ALA C  1 145 ? 114.900 -9.063  27.387 1.00 25.47  ? 145  ALA C CB  1 
ATOM   3289  N  N   . CYS C  1 146 ? 112.959 -9.932  25.087 1.00 26.16  ? 146  CYS C N   1 
ATOM   3290  C  CA  . CYS C  1 146 ? 112.585 -9.857  23.662 1.00 25.18  ? 146  CYS C CA  1 
ATOM   3291  C  C   . CYS C  1 146 ? 111.392 -8.928  23.534 1.00 34.57  ? 146  CYS C C   1 
ATOM   3292  O  O   . CYS C  1 146 ? 110.768 -8.639  24.564 1.00 26.60  ? 146  CYS C O   1 
ATOM   3293  C  CB  A CYS C  1 146 ? 112.263 -11.232 23.100 0.42 25.15  ? 146  CYS C CB  1 
ATOM   3294  C  CB  B CYS C  1 146 ? 112.289 -11.240 23.109 0.58 25.03  ? 146  CYS C CB  1 
ATOM   3295  S  SG  A CYS C  1 146 ? 111.015 -12.148 24.046 0.42 40.16  ? 146  CYS C SG  1 
ATOM   3296  S  SG  B CYS C  1 146 ? 110.722 -11.992 23.614 0.58 30.56  ? 146  CYS C SG  1 
ATOM   3297  N  N   . GLY C  1 147 ? 111.081 -8.480  22.325 1.00 27.93  ? 147  GLY C N   1 
ATOM   3298  C  CA  . GLY C  1 147 ? 109.927 -7.610  22.127 1.00 27.37  ? 147  GLY C CA  1 
ATOM   3299  C  C   . GLY C  1 147 ? 109.517 -7.624  20.666 1.00 29.72  ? 147  GLY C C   1 
ATOM   3300  O  O   . GLY C  1 147 ? 110.369 -7.904  19.814 1.00 24.02  ? 147  GLY C O   1 
ATOM   3301  N  N   . VAL C  1 148 ? 108.238 -7.342  20.396 1.00 24.01  ? 148  VAL C N   1 
ATOM   3302  C  CA  . VAL C  1 148 ? 107.804 -7.267  18.987 1.00 23.41  ? 148  VAL C CA  1 
ATOM   3303  C  C   . VAL C  1 148 ? 108.174 -5.897  18.436 1.00 20.92  ? 148  VAL C C   1 
ATOM   3304  O  O   . VAL C  1 148 ? 108.103 -4.847  19.053 1.00 22.47  ? 148  VAL C O   1 
ATOM   3305  C  CB  . VAL C  1 148 ? 106.291 -7.512  18.864 1.00 22.99  ? 148  VAL C CB  1 
ATOM   3306  C  CG1 . VAL C  1 148 ? 105.842 -7.471  17.400 1.00 30.46  ? 148  VAL C CG1 1 
ATOM   3307  C  CG2 . VAL C  1 148 ? 105.925 -8.845  19.490 1.00 20.90  ? 148  VAL C CG2 1 
ATOM   3308  N  N   . ILE C  1 149 ? 108.616 -5.849  17.172 1.00 27.09  ? 149  ILE C N   1 
ATOM   3309  C  CA  . ILE C  1 149 ? 109.087 -4.582  16.615 1.00 21.49  ? 149  ILE C CA  1 
ATOM   3310  C  C   . ILE C  1 149 ? 107.924 -3.799  16.011 1.00 21.83  ? 149  ILE C C   1 
ATOM   3311  O  O   . ILE C  1 149 ? 107.322 -4.339  15.081 1.00 29.11  ? 149  ILE C O   1 
ATOM   3312  C  CB  . ILE C  1 149 ? 110.150 -4.882  15.537 1.00 24.09  ? 149  ILE C CB  1 
ATOM   3313  C  CG1 . ILE C  1 149 ? 111.380 -5.586  16.122 1.00 28.35  ? 149  ILE C CG1 1 
ATOM   3314  C  CG2 . ILE C  1 149 ? 110.505 -3.613  14.799 1.00 26.94  ? 149  ILE C CG2 1 
ATOM   3315  C  CD1 . ILE C  1 149 ? 112.250 -6.296  15.109 1.00 29.12  ? 149  ILE C CD1 1 
ATOM   3316  N  N   . GLY C  1 150 ? 107.635 -2.638  16.557 1.00 22.04  ? 150  GLY C N   1 
ATOM   3317  C  CA  . GLY C  1 150 ? 106.411 -1.923  16.242 1.00 27.45  ? 150  GLY C CA  1 
ATOM   3318  C  C   . GLY C  1 150 ? 106.664 -0.671  15.441 1.00 31.80  ? 150  GLY C C   1 
ATOM   3319  O  O   . GLY C  1 150 ? 107.741 -0.086  15.528 1.00 26.50  ? 150  GLY C O   1 
ATOM   3320  N  N   . ILE C  1 151 ? 105.657 -0.268  14.670 1.00 23.22  ? 151  ILE C N   1 
ATOM   3321  C  CA  . ILE C  1 151 ? 105.736 1.020   13.971 1.00 23.79  ? 151  ILE C CA  1 
ATOM   3322  C  C   . ILE C  1 151 ? 105.662 2.166   14.948 1.00 31.32  ? 151  ILE C C   1 
ATOM   3323  O  O   . ILE C  1 151 ? 104.822 2.223   15.861 1.00 33.74  ? 151  ILE C O   1 
ATOM   3324  C  CB  . ILE C  1 151 ? 104.591 1.088   12.927 1.00 25.83  ? 151  ILE C CB  1 
ATOM   3325  C  CG1 . ILE C  1 151 ? 104.601 -0.117  12.003 1.00 27.96  ? 151  ILE C CG1 1 
ATOM   3326  C  CG2 . ILE C  1 151 ? 104.642 2.400   12.170 1.00 32.21  ? 151  ILE C CG2 1 
ATOM   3327  C  CD1 . ILE C  1 151 ? 103.423 -0.238  11.072 1.00 37.19  ? 151  ILE C CD1 1 
ATOM   3328  N  N   . ALA C  1 152 ? 106.549 3.155   14.816 1.00 23.49  ? 152  ALA C N   1 
ATOM   3329  C  CA  . ALA C  1 152 ? 106.608 4.264   15.747 1.00 25.14  ? 152  ALA C CA  1 
ATOM   3330  C  C   . ALA C  1 152 ? 106.294 5.579   15.063 1.00 32.87  ? 152  ALA C C   1 
ATOM   3331  O  O   . ALA C  1 152 ? 106.410 5.676   13.831 1.00 31.86  ? 152  ALA C O   1 
ATOM   3332  C  CB  . ALA C  1 152 ? 108.017 4.288   16.361 1.00 30.59  ? 152  ALA C CB  1 
ATOM   3333  N  N   . GLN C  1 153 ? 105.892 6.585   15.844 1.00 26.09  ? 153  GLN C N   1 
ATOM   3334  C  CA  . GLN C  1 153 ? 105.473 7.800   15.177 1.00 30.10  ? 153  GLN C CA  1 
ATOM   3335  C  C   . GLN C  1 153 ? 106.676 8.600   14.685 1.00 47.34  ? 153  GLN C C   1 
ATOM   3336  O  O   . GLN C  1 153 ? 107.666 8.662   15.436 1.00 48.39  ? 153  GLN C O   1 
ATOM   3337  C  CB  . GLN C  1 153 ? 104.614 8.696   16.078 1.00 39.68  ? 153  GLN C CB  1 
ATOM   3338  C  CG  . GLN C  1 153 ? 104.233 9.967   15.312 1.00 51.58  ? 153  GLN C CG  1 
ATOM   3339  C  CD  . GLN C  1 153 ? 103.237 10.863  16.009 1.00 69.74  ? 153  GLN C CD  1 
ATOM   3340  O  OE1 . GLN C  1 153 ? 102.308 11.387  15.381 1.00 88.19  ? 153  GLN C OE1 1 
ATOM   3341  N  NE2 . GLN C  1 153 ? 103.425 11.053  17.310 1.00 78.89  ? 153  GLN C NE2 1 
ATOM   3342  O  OXT . GLN C  1 153 ? 106.583 9.148   13.569 1.00 65.30  ? 153  GLN C OXT 1 
ATOM   3343  N  N   . ALA D  1 1   ? 102.343 -14.586 4.600  1.00 57.51  ? 1    ALA D N   1 
ATOM   3344  C  CA  . ALA D  1 1   ? 101.847 -13.445 5.369  1.00 63.15  ? 1    ALA D CA  1 
ATOM   3345  C  C   . ALA D  1 1   ? 100.404 -13.667 5.776  1.00 57.93  ? 1    ALA D C   1 
ATOM   3346  O  O   . ALA D  1 1   ? 99.487  -12.913 5.468  1.00 45.95  ? 1    ALA D O   1 
ATOM   3347  C  CB  . ALA D  1 1   ? 102.002 -12.177 4.543  1.00 52.47  ? 1    ALA D CB  1 
ATOM   3348  N  N   . THR D  1 2   ? 100.110 -14.765 6.490  1.00 51.38  ? 2    THR D N   1 
ATOM   3349  C  CA  . THR D  1 2   ? 98.681  -14.992 6.679  1.00 37.64  ? 2    THR D CA  1 
ATOM   3350  C  C   . THR D  1 2   ? 98.298  -15.252 8.129  1.00 32.48  ? 2    THR D C   1 
ATOM   3351  O  O   . THR D  1 2   ? 97.098  -15.417 8.391  1.00 30.93  ? 2    THR D O   1 
ATOM   3352  C  CB  . THR D  1 2   ? 98.214  -16.158 5.787  1.00 41.86  ? 2    THR D CB  1 
ATOM   3353  O  OG1 . THR D  1 2   ? 99.070  -17.288 6.031  1.00 63.35  ? 2    THR D OG1 1 
ATOM   3354  C  CG2 . THR D  1 2   ? 98.353  -15.800 4.320  1.00 60.08  ? 2    THR D CG2 1 
ATOM   3355  N  N   . LYS D  1 3   ? 99.236  -15.287 9.071  1.00 28.55  ? 3    LYS D N   1 
ATOM   3356  C  CA  . LYS D  1 3   ? 98.816  -15.376 10.473 1.00 32.20  ? 3    LYS D CA  1 
ATOM   3357  C  C   . LYS D  1 3   ? 99.525  -14.307 11.300 1.00 28.66  ? 3    LYS D C   1 
ATOM   3358  O  O   . LYS D  1 3   ? 100.669 -13.957 11.028 1.00 28.75  ? 3    LYS D O   1 
ATOM   3359  C  CB  . LYS D  1 3   ? 99.094  -16.734 11.100 1.00 32.24  ? 3    LYS D CB  1 
ATOM   3360  C  CG  . LYS D  1 3   ? 98.149  -17.840 10.646 1.00 38.30  ? 3    LYS D CG  1 
ATOM   3361  C  CD  . LYS D  1 3   ? 98.908  -19.143 10.495 1.00 46.78  ? 3    LYS D CD  1 
ATOM   3362  C  CE  . LYS D  1 3   ? 97.967  -20.332 10.441 1.00 67.94  ? 3    LYS D CE  1 
ATOM   3363  N  NZ  . LYS D  1 3   ? 98.112  -21.238 11.620 1.00 88.69  ? 3    LYS D NZ  1 
ATOM   3364  N  N   . ALA D  1 4   ? 98.829  -13.798 12.310 1.00 22.57  ? 4    ALA D N   1 
ATOM   3365  C  CA  . ALA D  1 4   ? 99.416  -12.856 13.243 1.00 22.36  ? 4    ALA D CA  1 
ATOM   3366  C  C   . ALA D  1 4   ? 98.883  -13.154 14.654 1.00 22.86  ? 4    ALA D C   1 
ATOM   3367  O  O   . ALA D  1 4   ? 97.956  -13.946 14.831 1.00 24.05  ? 4    ALA D O   1 
ATOM   3368  C  CB  . ALA D  1 4   ? 99.160  -11.400 12.869 1.00 23.47  ? 4    ALA D CB  1 
ATOM   3369  N  N   . VAL D  1 5   ? 99.515  -12.537 15.652 1.00 22.63  ? 5    VAL D N   1 
ATOM   3370  C  CA  . VAL D  1 5   ? 99.155  -12.907 17.022 1.00 24.20  ? 5    VAL D CA  1 
ATOM   3371  C  C   . VAL D  1 5   ? 99.454  -11.716 17.905 1.00 24.28  ? 5    VAL D C   1 
ATOM   3372  O  O   . VAL D  1 5   ? 100.317 -10.898 17.600 1.00 22.91  ? 5    VAL D O   1 
ATOM   3373  C  CB  . VAL D  1 5   ? 99.924  -14.140 17.545 1.00 28.71  ? 5    VAL D CB  1 
ATOM   3374  C  CG1 . VAL D  1 5   ? 101.394 -13.784 17.788 1.00 26.07  ? 5    VAL D CG1 1 
ATOM   3375  C  CG2 . VAL D  1 5   ? 99.312  -14.695 18.826 1.00 20.87  ? 5    VAL D CG2 1 
ATOM   3376  N  N   . CYS D  1 6   ? 98.718  -11.601 19.009 1.00 22.75  ? 6    CYS D N   1 
ATOM   3377  C  CA  . CYS D  1 6   ? 98.925  -10.447 19.874 1.00 22.40  ? 6    CYS D CA  1 
ATOM   3378  C  C   . CYS D  1 6   ? 98.715  -10.880 21.329 1.00 27.12  ? 6    CYS D C   1 
ATOM   3379  O  O   . CYS D  1 6   ? 97.656  -11.420 21.662 1.00 21.22  ? 6    CYS D O   1 
ATOM   3380  C  CB  . CYS D  1 6   ? 97.924  -9.339  19.540 1.00 24.82  ? 6    CYS D CB  1 
ATOM   3381  S  SG  . CYS D  1 6   ? 98.086  -7.859  20.585 1.00 26.01  ? 6    CYS D SG  1 
ATOM   3382  N  N   . VAL D  1 7   ? 99.710  -10.628 22.155 1.00 23.53  ? 7    VAL D N   1 
ATOM   3383  C  CA  . VAL D  1 7   ? 99.582  -10.893 23.583 1.00 22.32  ? 7    VAL D CA  1 
ATOM   3384  C  C   . VAL D  1 7   ? 99.159  -9.626  24.275 1.00 17.77  ? 7    VAL D C   1 
ATOM   3385  O  O   . VAL D  1 7   ? 99.884  -8.623  24.281 1.00 21.94  ? 7    VAL D O   1 
ATOM   3386  C  CB  . VAL D  1 7   ? 100.915 -11.454 24.171 1.00 21.70  ? 7    VAL D CB  1 
ATOM   3387  C  CG1 . VAL D  1 7   ? 100.706 -11.546 25.683 1.00 23.53  ? 7    VAL D CG1 1 
ATOM   3388  C  CG2 . VAL D  1 7   ? 101.244 -12.769 23.505 1.00 20.77  ? 7    VAL D CG2 1 
ATOM   3389  N  N   . LEU D  1 8   ? 97.951  -9.562  24.865 1.00 20.28  ? 8    LEU D N   1 
ATOM   3390  C  CA  . LEU D  1 8   ? 97.532  -8.327  25.494 1.00 21.22  ? 8    LEU D CA  1 
ATOM   3391  C  C   . LEU D  1 8   ? 97.881  -8.306  26.987 1.00 19.11  ? 8    LEU D C   1 
ATOM   3392  O  O   . LEU D  1 8   ? 97.597  -9.264  27.705 1.00 25.31  ? 8    LEU D O   1 
ATOM   3393  C  CB  . LEU D  1 8   ? 96.007  -8.162  25.387 1.00 24.55  ? 8    LEU D CB  1 
ATOM   3394  C  CG  . LEU D  1 8   ? 95.371  -8.064  24.005 1.00 28.14  ? 8    LEU D CG  1 
ATOM   3395  C  CD1 . LEU D  1 8   ? 93.852  -8.254  24.091 1.00 37.19  ? 8    LEU D CD1 1 
ATOM   3396  C  CD2 . LEU D  1 8   ? 95.653  -6.725  23.378 1.00 28.37  ? 8    LEU D CD2 1 
ATOM   3397  N  N   . LYS D  1 9   ? 98.462  -7.216  27.437 1.00 23.34  ? 9    LYS D N   1 
ATOM   3398  C  CA  . LYS D  1 9   ? 98.798  -7.034  28.843 1.00 26.19  ? 9    LYS D CA  1 
ATOM   3399  C  C   . LYS D  1 9   ? 98.502  -5.614  29.268 1.00 24.07  ? 9    LYS D C   1 
ATOM   3400  O  O   . LYS D  1 9   ? 98.478  -4.674  28.470 1.00 28.18  ? 9    LYS D O   1 
ATOM   3401  C  CB  . LYS D  1 9   ? 100.293 -7.325  29.072 1.00 28.52  ? 9    LYS D CB  1 
ATOM   3402  C  CG  . LYS D  1 9   ? 100.587 -8.811  28.927 1.00 37.94  ? 9    LYS D CG  1 
ATOM   3403  C  CD  . LYS D  1 9   ? 102.027 -9.155  29.255 1.00 52.49  ? 9    LYS D CD  1 
ATOM   3404  C  CE  . LYS D  1 9   ? 102.321 -10.637 29.021 1.00 54.51  ? 9    LYS D CE  1 
ATOM   3405  N  NZ  . LYS D  1 9   ? 103.648 -10.817 28.349 1.00 75.61  ? 9    LYS D NZ  1 
ATOM   3406  N  N   . GLY D  1 10  ? 98.285  -5.461  30.583 1.00 26.51  ? 10   GLY D N   1 
ATOM   3407  C  CA  . GLY D  1 10  ? 98.093  -4.103  31.082 1.00 28.42  ? 10   GLY D CA  1 
ATOM   3408  C  C   . GLY D  1 10  ? 98.467  -4.040  32.556 1.00 34.44  ? 10   GLY D C   1 
ATOM   3409  O  O   . GLY D  1 10  ? 99.071  -4.981  33.079 1.00 37.22  ? 10   GLY D O   1 
ATOM   3410  N  N   . ASP D  1 11  ? 98.090  -2.950  33.207 1.00 32.63  ? 11   ASP D N   1 
ATOM   3411  C  CA  . ASP D  1 11  ? 98.489  -2.809  34.610 1.00 39.76  ? 11   ASP D CA  1 
ATOM   3412  C  C   . ASP D  1 11  ? 97.521  -3.471  35.566 1.00 42.33  ? 11   ASP D C   1 
ATOM   3413  O  O   . ASP D  1 11  ? 97.855  -3.681  36.742 1.00 43.00  ? 11   ASP D O   1 
ATOM   3414  C  CB  . ASP D  1 11  ? 98.651  -1.302  34.881 1.00 48.39  ? 11   ASP D CB  1 
ATOM   3415  C  CG  . ASP D  1 11  ? 99.774  -0.775  33.992 1.00 48.46  ? 11   ASP D CG  1 
ATOM   3416  O  OD1 . ASP D  1 11  ? 99.640  0.309   33.397 1.00 63.04  ? 11   ASP D OD1 1 
ATOM   3417  O  OD2 . ASP D  1 11  ? 100.800 -1.484  33.891 1.00 61.65  ? 11   ASP D OD2 1 
ATOM   3418  N  N   . GLY D  1 12  ? 96.324  -3.824  35.116 1.00 34.70  ? 12   GLY D N   1 
ATOM   3419  C  CA  . GLY D  1 12  ? 95.338  -4.482  35.959 1.00 28.19  ? 12   GLY D CA  1 
ATOM   3420  C  C   . GLY D  1 12  ? 95.195  -5.959  35.658 1.00 29.76  ? 12   GLY D C   1 
ATOM   3421  O  O   . GLY D  1 12  ? 96.148  -6.587  35.204 1.00 29.31  ? 12   GLY D O   1 
ATOM   3422  N  N   . PRO D  1 13  ? 94.015  -6.535  35.904 1.00 25.10  ? 13   PRO D N   1 
ATOM   3423  C  CA  . PRO D  1 13  ? 93.783  -7.959  35.693 1.00 22.55  ? 13   PRO D CA  1 
ATOM   3424  C  C   . PRO D  1 13  ? 93.529  -8.368  34.245 1.00 21.05  ? 13   PRO D C   1 
ATOM   3425  O  O   . PRO D  1 13  ? 93.370  -9.539  33.887 1.00 24.14  ? 13   PRO D O   1 
ATOM   3426  C  CB  . PRO D  1 13  ? 92.509  -8.163  36.528 1.00 25.04  ? 13   PRO D CB  1 
ATOM   3427  C  CG  . PRO D  1 13  ? 91.757  -6.878  36.385 1.00 24.66  ? 13   PRO D CG  1 
ATOM   3428  C  CD  . PRO D  1 13  ? 92.821  -5.812  36.398 1.00 27.52  ? 13   PRO D CD  1 
ATOM   3429  N  N   . VAL D  1 14  ? 93.481  -7.387  33.331 1.00 27.21  ? 14   VAL D N   1 
ATOM   3430  C  CA  . VAL D  1 14  ? 93.073  -7.764  31.966 1.00 23.78  ? 14   VAL D CA  1 
ATOM   3431  C  C   . VAL D  1 14  ? 94.258  -8.328  31.192 1.00 25.37  ? 14   VAL D C   1 
ATOM   3432  O  O   . VAL D  1 14  ? 95.302  -7.663  31.129 1.00 24.37  ? 14   VAL D O   1 
ATOM   3433  C  CB  . VAL D  1 14  ? 92.499  -6.556  31.202 1.00 23.45  ? 14   VAL D CB  1 
ATOM   3434  C  CG1 . VAL D  1 14  ? 92.133  -6.969  29.774 1.00 24.48  ? 14   VAL D CG1 1 
ATOM   3435  C  CG2 . VAL D  1 14  ? 91.300  -5.967  31.929 1.00 22.11  ? 14   VAL D CG2 1 
ATOM   3436  N  N   . GLN D  1 15  ? 94.102  -9.512  30.631 1.00 23.72  ? 15   GLN D N   1 
ATOM   3437  C  CA  . GLN D  1 15  ? 95.147  -10.061 29.772 1.00 28.88  ? 15   GLN D CA  1 
ATOM   3438  C  C   . GLN D  1 15  ? 94.558  -11.144 28.880 1.00 24.16  ? 15   GLN D C   1 
ATOM   3439  O  O   . GLN D  1 15  ? 93.509  -11.746 29.141 1.00 23.82  ? 15   GLN D O   1 
ATOM   3440  C  CB  . GLN D  1 15  ? 96.325  -10.650 30.567 1.00 35.00  ? 15   GLN D CB  1 
ATOM   3441  C  CG  . GLN D  1 15  ? 95.837  -11.499 31.712 1.00 30.00  ? 15   GLN D CG  1 
ATOM   3442  C  CD  . GLN D  1 15  ? 96.932  -12.049 32.605 1.00 41.45  ? 15   GLN D CD  1 
ATOM   3443  O  OE1 . GLN D  1 15  ? 97.447  -13.135 32.349 1.00 48.46  ? 15   GLN D OE1 1 
ATOM   3444  N  NE2 . GLN D  1 15  ? 97.272  -11.313 33.655 1.00 63.97  ? 15   GLN D NE2 1 
ATOM   3445  N  N   . GLY D  1 16  ? 95.271  -11.379 27.772 1.00 22.33  ? 16   GLY D N   1 
ATOM   3446  C  CA  . GLY D  1 16  ? 94.742  -12.382 26.858 1.00 27.11  ? 16   GLY D CA  1 
ATOM   3447  C  C   . GLY D  1 16  ? 95.606  -12.556 25.621 1.00 27.32  ? 16   GLY D C   1 
ATOM   3448  O  O   . GLY D  1 16  ? 96.660  -11.931 25.527 1.00 24.01  ? 16   GLY D O   1 
ATOM   3449  N  N   . ILE D  1 17  ? 95.150  -13.439 24.736 1.00 27.17  ? 17   ILE D N   1 
ATOM   3450  C  CA  . ILE D  1 17  ? 95.897  -13.724 23.504 1.00 26.62  ? 17   ILE D CA  1 
ATOM   3451  C  C   . ILE D  1 17  ? 94.903  -13.665 22.340 1.00 24.06  ? 17   ILE D C   1 
ATOM   3452  O  O   . ILE D  1 17  ? 93.873  -14.333 22.453 1.00 23.54  ? 17   ILE D O   1 
ATOM   3453  C  CB  . ILE D  1 17  ? 96.598  -15.075 23.494 1.00 24.59  ? 17   ILE D CB  1 
ATOM   3454  C  CG1 . ILE D  1 17  ? 97.721  -15.194 24.525 1.00 34.16  ? 17   ILE D CG1 1 
ATOM   3455  C  CG2 . ILE D  1 17  ? 97.154  -15.418 22.102 1.00 23.73  ? 17   ILE D CG2 1 
ATOM   3456  C  CD1 . ILE D  1 17  ? 98.105  -16.648 24.801 1.00 35.19  ? 17   ILE D CD1 1 
ATOM   3457  N  N   . ILE D  1 18  ? 95.262  -12.881 21.329 1.00 20.05  ? 18   ILE D N   1 
ATOM   3458  C  CA  . ILE D  1 18  ? 94.367  -12.759 20.181 1.00 23.04  ? 18   ILE D CA  1 
ATOM   3459  C  C   . ILE D  1 18  ? 95.110  -13.182 18.916 1.00 24.44  ? 18   ILE D C   1 
ATOM   3460  O  O   . ILE D  1 18  ? 96.223  -12.704 18.688 1.00 23.55  ? 18   ILE D O   1 
ATOM   3461  C  CB  . ILE D  1 18  ? 93.814  -11.324 20.046 1.00 20.56  ? 18   ILE D CB  1 
ATOM   3462  C  CG1 . ILE D  1 18  ? 92.942  -10.850 21.222 1.00 20.51  ? 18   ILE D CG1 1 
ATOM   3463  C  CG2 . ILE D  1 18  ? 93.029  -11.180 18.740 1.00 22.43  ? 18   ILE D CG2 1 
ATOM   3464  C  CD1 . ILE D  1 18  ? 91.677  -11.720 21.353 1.00 21.17  ? 18   ILE D CD1 1 
ATOM   3465  N  N   . ASN D  1 19  ? 94.473  -14.027 18.141 1.00 20.35  ? 19   ASN D N   1 
ATOM   3466  C  CA  . ASN D  1 19  ? 94.966  -14.607 16.906 1.00 22.72  ? 19   ASN D CA  1 
ATOM   3467  C  C   . ASN D  1 19  ? 94.283  -13.961 15.704 1.00 26.36  ? 19   ASN D C   1 
ATOM   3468  O  O   . ASN D  1 19  ? 93.107  -13.589 15.758 1.00 23.61  ? 19   ASN D O   1 
ATOM   3469  C  CB  . ASN D  1 19  ? 94.694  -16.119 16.882 1.00 24.44  ? 19   ASN D CB  1 
ATOM   3470  C  CG  . ASN D  1 19  ? 95.247  -16.833 18.102 1.00 30.68  ? 19   ASN D CG  1 
ATOM   3471  O  OD1 . ASN D  1 19  ? 96.475  -16.987 18.175 1.00 28.11  ? 19   ASN D OD1 1 
ATOM   3472  N  ND2 . ASN D  1 19  ? 94.388  -17.245 19.029 1.00 24.19  ? 19   ASN D ND2 1 
ATOM   3473  N  N   . PHE D  1 20  ? 95.030  -13.847 14.607 1.00 24.25  ? 20   PHE D N   1 
ATOM   3474  C  CA  . PHE D  1 20  ? 94.505  -13.330 13.350 1.00 23.62  ? 20   PHE D CA  1 
ATOM   3475  C  C   . PHE D  1 20  ? 94.923  -14.266 12.227 1.00 24.80  ? 20   PHE D C   1 
ATOM   3476  O  O   . PHE D  1 20  ? 96.067  -14.763 12.252 1.00 25.18  ? 20   PHE D O   1 
ATOM   3477  C  CB  . PHE D  1 20  ? 95.078  -11.964 12.976 1.00 22.53  ? 20   PHE D CB  1 
ATOM   3478  C  CG  . PHE D  1 20  ? 94.965  -10.868 14.007 1.00 24.01  ? 20   PHE D CG  1 
ATOM   3479  C  CD1 . PHE D  1 20  ? 94.021  -9.871  13.822 1.00 23.16  ? 20   PHE D CD1 1 
ATOM   3480  C  CD2 . PHE D  1 20  ? 95.795  -10.867 15.123 1.00 20.85  ? 20   PHE D CD2 1 
ATOM   3481  C  CE1 . PHE D  1 20  ? 93.870  -8.837  14.730 1.00 22.99  ? 20   PHE D CE1 1 
ATOM   3482  C  CE2 . PHE D  1 20  ? 95.662  -9.828  16.025 1.00 21.44  ? 20   PHE D CE2 1 
ATOM   3483  C  CZ  . PHE D  1 20  ? 94.722  -8.831  15.831 1.00 23.26  ? 20   PHE D CZ  1 
ATOM   3484  N  N   . GLU D  1 21  ? 94.016  -14.466 11.285 1.00 23.89  ? 21   GLU D N   1 
ATOM   3485  C  CA  . GLU D  1 21  ? 94.348  -15.322 10.150 1.00 22.44  ? 21   GLU D CA  1 
ATOM   3486  C  C   . GLU D  1 21  ? 93.641  -14.804 8.900  1.00 27.87  ? 21   GLU D C   1 
ATOM   3487  O  O   . GLU D  1 21  ? 92.457  -14.478 8.881  1.00 24.46  ? 21   GLU D O   1 
ATOM   3488  C  CB  . GLU D  1 21  ? 93.976  -16.785 10.394 1.00 23.27  ? 21   GLU D CB  1 
ATOM   3489  C  CG  . GLU D  1 21  ? 94.144  -17.595 9.108  1.00 33.26  ? 21   GLU D CG  1 
ATOM   3490  C  CD  . GLU D  1 21  ? 94.016  -19.091 9.338  1.00 49.69  ? 21   GLU D CD  1 
ATOM   3491  O  OE1 . GLU D  1 21  ? 94.611  -19.871 8.566  1.00 50.63  ? 21   GLU D OE1 1 
ATOM   3492  O  OE2 . GLU D  1 21  ? 93.319  -19.497 10.290 1.00 54.58  ? 21   GLU D OE2 1 
ATOM   3493  N  N   . GLN D  1 22  ? 94.431  -14.716 7.826  1.00 24.90  ? 22   GLN D N   1 
ATOM   3494  C  CA  . GLN D  1 22  ? 93.893  -14.238 6.543  1.00 26.45  ? 22   GLN D CA  1 
ATOM   3495  C  C   . GLN D  1 22  ? 94.333  -15.229 5.464  1.00 24.48  ? 22   GLN D C   1 
ATOM   3496  O  O   . GLN D  1 22  ? 95.499  -15.210 5.068  1.00 30.18  ? 22   GLN D O   1 
ATOM   3497  C  CB  . GLN D  1 22  ? 94.401  -12.834 6.252  1.00 26.83  ? 22   GLN D CB  1 
ATOM   3498  C  CG  . GLN D  1 22  ? 93.798  -12.166 5.012  1.00 21.41  ? 22   GLN D CG  1 
ATOM   3499  C  CD  . GLN D  1 22  ? 94.389  -10.797 4.787  1.00 25.25  ? 22   GLN D CD  1 
ATOM   3500  O  OE1 . GLN D  1 22  ? 95.517  -10.480 5.178  1.00 27.14  ? 22   GLN D OE1 1 
ATOM   3501  N  NE2 . GLN D  1 22  ? 93.631  -9.898  4.150  1.00 28.88  ? 22   GLN D NE2 1 
ATOM   3502  N  N   . LYS D  1 23  ? 93.425  -16.069 5.050  1.00 29.31  ? 23   LYS D N   1 
ATOM   3503  C  CA  . LYS D  1 23  ? 93.732  -17.103 4.062  1.00 38.50  ? 23   LYS D CA  1 
ATOM   3504  C  C   . LYS D  1 23  ? 94.083  -16.517 2.703  1.00 40.57  ? 23   LYS D C   1 
ATOM   3505  O  O   . LYS D  1 23  ? 94.876  -17.105 1.966  1.00 46.71  ? 23   LYS D O   1 
ATOM   3506  C  CB  . LYS D  1 23  ? 92.541  -18.063 3.937  1.00 54.24  ? 23   LYS D CB  1 
ATOM   3507  C  CG  . LYS D  1 23  ? 92.549  -19.187 4.966  1.00 70.05  ? 23   LYS D CG  1 
ATOM   3508  C  CD  . LYS D  1 23  ? 92.612  -18.649 6.385  1.00 85.95  ? 23   LYS D CD  1 
ATOM   3509  C  CE  . LYS D  1 23  ? 91.236  -18.546 7.021  1.00 91.84  ? 23   LYS D CE  1 
ATOM   3510  N  NZ  . LYS D  1 23  ? 91.281  -18.218 8.475  1.00 87.04  ? 23   LYS D NZ  1 
ATOM   3511  N  N   . GLU D  1 24  ? 93.540  -15.375 2.280  1.00 35.86  ? 24   GLU D N   1 
ATOM   3512  C  CA  . GLU D  1 24  ? 93.881  -14.841 0.963  1.00 39.42  ? 24   GLU D CA  1 
ATOM   3513  C  C   . GLU D  1 24  ? 94.121  -13.339 1.055  1.00 40.63  ? 24   GLU D C   1 
ATOM   3514  O  O   . GLU D  1 24  ? 93.436  -12.719 1.864  1.00 36.69  ? 24   GLU D O   1 
ATOM   3515  C  CB  . GLU D  1 24  ? 92.764  -15.089 -0.057 1.00 46.43  ? 24   GLU D CB  1 
ATOM   3516  C  CG  . GLU D  1 24  ? 91.942  -16.330 0.206  1.00 48.87  ? 24   GLU D CG  1 
ATOM   3517  C  CD  . GLU D  1 24  ? 90.608  -16.369 -0.510 1.00 60.33  ? 24   GLU D CD  1 
ATOM   3518  O  OE1 . GLU D  1 24  ? 90.390  -17.362 -1.240 1.00 68.95  ? 24   GLU D OE1 1 
ATOM   3519  O  OE2 . GLU D  1 24  ? 89.798  -15.431 -0.346 1.00 90.75  ? 24   GLU D OE2 1 
ATOM   3520  N  N   . SER D  1 25  ? 95.023  -12.805 0.261  1.00 38.07  ? 25   SER D N   1 
ATOM   3521  C  CA  . SER D  1 25  ? 95.457  -11.423 0.261  1.00 52.07  ? 25   SER D CA  1 
ATOM   3522  C  C   . SER D  1 25  ? 94.326  -10.416 0.212  1.00 51.63  ? 25   SER D C   1 
ATOM   3523  O  O   . SER D  1 25  ? 94.377  -9.323  0.789  1.00 56.27  ? 25   SER D O   1 
ATOM   3524  C  CB  . SER D  1 25  ? 96.385  -11.189 -0.948 1.00 62.23  ? 25   SER D CB  1 
ATOM   3525  O  OG  . SER D  1 25  ? 96.365  -9.823  -1.328 1.00 69.55  ? 25   SER D OG  1 
ATOM   3526  N  N   . ASN D  1 26  ? 93.244  -10.744 -0.504 1.00 52.73  ? 26   ASN D N   1 
ATOM   3527  C  CA  . ASN D  1 26  ? 92.161  -9.745  -0.486 1.00 58.86  ? 26   ASN D CA  1 
ATOM   3528  C  C   . ASN D  1 26  ? 90.926  -10.328 0.184  1.00 58.04  ? 26   ASN D C   1 
ATOM   3529  O  O   . ASN D  1 26  ? 89.801  -10.130 -0.262 1.00 64.26  ? 26   ASN D O   1 
ATOM   3530  C  CB  . ASN D  1 26  ? 91.866  -9.267  -1.909 1.00 54.16  ? 26   ASN D CB  1 
ATOM   3531  C  CG  . ASN D  1 26  ? 93.165  -8.800  -2.550 1.00 62.30  ? 26   ASN D CG  1 
ATOM   3532  O  OD1 . ASN D  1 26  ? 93.783  -7.857  -2.052 1.00 83.40  ? 26   ASN D OD1 1 
ATOM   3533  N  ND2 . ASN D  1 26  ? 93.567  -9.468  -3.624 1.00 79.53  ? 26   ASN D ND2 1 
ATOM   3534  N  N   . GLY D  1 27  ? 91.166  -11.066 1.265  1.00 41.71  ? 27   GLY D N   1 
ATOM   3535  C  CA  . GLY D  1 27  ? 90.091  -11.765 1.954  1.00 35.94  ? 27   GLY D CA  1 
ATOM   3536  C  C   . GLY D  1 27  ? 89.939  -11.234 3.373  1.00 28.42  ? 27   GLY D C   1 
ATOM   3537  O  O   . GLY D  1 27  ? 90.729  -10.423 3.864  1.00 29.37  ? 27   GLY D O   1 
ATOM   3538  N  N   . PRO D  1 28  ? 88.895  -11.708 4.027  1.00 29.50  ? 28   PRO D N   1 
ATOM   3539  C  CA  . PRO D  1 28  ? 88.619  -11.246 5.388  1.00 29.56  ? 28   PRO D CA  1 
ATOM   3540  C  C   . PRO D  1 28  ? 89.658  -11.848 6.332  1.00 25.93  ? 28   PRO D C   1 
ATOM   3541  O  O   . PRO D  1 28  ? 90.270  -12.876 6.048  1.00 26.51  ? 28   PRO D O   1 
ATOM   3542  C  CB  . PRO D  1 28  ? 87.232  -11.819 5.689  1.00 38.44  ? 28   PRO D CB  1 
ATOM   3543  C  CG  . PRO D  1 28  ? 87.158  -13.035 4.828  1.00 44.71  ? 28   PRO D CG  1 
ATOM   3544  C  CD  . PRO D  1 28  ? 87.911  -12.701 3.561  1.00 42.33  ? 28   PRO D CD  1 
ATOM   3545  N  N   . VAL D  1 29  ? 89.819  -11.167 7.448  1.00 24.25  ? 29   VAL D N   1 
ATOM   3546  C  CA  . VAL D  1 29  ? 90.683  -11.602 8.532  1.00 20.10  ? 29   VAL D CA  1 
ATOM   3547  C  C   . VAL D  1 29  ? 89.805  -12.147 9.655  1.00 23.13  ? 29   VAL D C   1 
ATOM   3548  O  O   . VAL D  1 29  ? 88.886  -11.440 10.073 1.00 23.91  ? 29   VAL D O   1 
ATOM   3549  C  CB  . VAL D  1 29  ? 91.528  -10.430 9.048  1.00 22.51  ? 29   VAL D CB  1 
ATOM   3550  C  CG1 . VAL D  1 29  ? 92.484  -10.894 10.147 1.00 25.41  ? 29   VAL D CG1 1 
ATOM   3551  C  CG2 . VAL D  1 29  ? 92.299  -9.746  7.923  1.00 23.19  ? 29   VAL D CG2 1 
ATOM   3552  N  N   . LYS D  1 30  ? 90.102  -13.353 10.100 1.00 23.56  ? 30   LYS D N   1 
ATOM   3553  C  CA  . LYS D  1 30  ? 89.448  -13.925 11.268 1.00 24.09  ? 30   LYS D CA  1 
ATOM   3554  C  C   . LYS D  1 30  ? 90.256  -13.529 12.499 1.00 24.22  ? 30   LYS D C   1 
ATOM   3555  O  O   . LYS D  1 30  ? 91.495  -13.585 12.452 1.00 22.12  ? 30   LYS D O   1 
ATOM   3556  C  CB  . LYS D  1 30  ? 89.362  -15.437 11.125 1.00 22.17  ? 30   LYS D CB  1 
ATOM   3557  C  CG  . LYS D  1 30  ? 88.303  -15.841 10.097 1.00 40.70  ? 30   LYS D CG  1 
ATOM   3558  C  CD  . LYS D  1 30  ? 88.181  -17.360 10.035 1.00 55.50  ? 30   LYS D CD  1 
ATOM   3559  C  CE  . LYS D  1 30  ? 86.810  -17.780 9.519  1.00 67.06  ? 30   LYS D CE  1 
ATOM   3560  N  NZ  . LYS D  1 30  ? 86.068  -18.583 10.537 1.00 85.75  ? 30   LYS D NZ  1 
ATOM   3561  N  N   . VAL D  1 31  ? 89.539  -13.116 13.525 1.00 21.48  ? 31   VAL D N   1 
ATOM   3562  C  CA  . VAL D  1 31  ? 90.140  -12.597 14.751 1.00 21.18  ? 31   VAL D CA  1 
ATOM   3563  C  C   . VAL D  1 31  ? 89.539  -13.382 15.916 1.00 25.25  ? 31   VAL D C   1 
ATOM   3564  O  O   . VAL D  1 31  ? 88.313  -13.334 16.052 1.00 24.97  ? 31   VAL D O   1 
ATOM   3565  C  CB  . VAL D  1 31  ? 89.869  -11.100 14.963 1.00 18.77  ? 31   VAL D CB  1 
ATOM   3566  C  CG1 . VAL D  1 31  ? 90.610  -10.606 16.187 1.00 19.94  ? 31   VAL D CG1 1 
ATOM   3567  C  CG2 . VAL D  1 31  ? 90.292  -10.256 13.765 1.00 20.84  ? 31   VAL D CG2 1 
ATOM   3568  N  N   . TRP D  1 32  ? 90.337  -14.110 16.698 1.00 20.90  ? 32   TRP D N   1 
ATOM   3569  C  CA  . TRP D  1 32  ? 89.748  -14.890 17.775 1.00 20.42  ? 32   TRP D CA  1 
ATOM   3570  C  C   . TRP D  1 32  ? 90.776  -15.123 18.880 1.00 22.16  ? 32   TRP D C   1 
ATOM   3571  O  O   . TRP D  1 32  ? 91.997  -15.066 18.715 1.00 26.10  ? 32   TRP D O   1 
ATOM   3572  C  CB  . TRP D  1 32  ? 89.201  -16.223 17.251 1.00 22.93  ? 32   TRP D CB  1 
ATOM   3573  C  CG  . TRP D  1 32  ? 90.310  -17.221 17.033 1.00 28.61  ? 32   TRP D CG  1 
ATOM   3574  C  CD1 . TRP D  1 32  ? 90.687  -18.245 17.858 1.00 31.51  ? 32   TRP D CD1 1 
ATOM   3575  C  CD2 . TRP D  1 32  ? 91.179  -17.270 15.896 1.00 27.27  ? 32   TRP D CD2 1 
ATOM   3576  N  NE1 . TRP D  1 32  ? 91.746  -18.934 17.304 1.00 35.13  ? 32   TRP D NE1 1 
ATOM   3577  C  CE2 . TRP D  1 32  ? 92.065  -18.355 16.107 1.00 35.58  ? 32   TRP D CE2 1 
ATOM   3578  C  CE3 . TRP D  1 32  ? 91.306  -16.510 14.729 1.00 33.34  ? 32   TRP D CE3 1 
ATOM   3579  C  CZ2 . TRP D  1 32  ? 93.059  -18.702 15.196 1.00 37.03  ? 32   TRP D CZ2 1 
ATOM   3580  C  CZ3 . TRP D  1 32  ? 92.301  -16.858 13.816 1.00 31.27  ? 32   TRP D CZ3 1 
ATOM   3581  C  CH2 . TRP D  1 32  ? 93.148  -17.938 14.068 1.00 29.96  ? 32   TRP D CH2 1 
ATOM   3582  N  N   . GLY D  1 33  ? 90.230  -15.422 20.047 1.00 20.64  ? 33   GLY D N   1 
ATOM   3583  C  CA  . GLY D  1 33  ? 91.121  -15.704 21.189 1.00 22.22  ? 33   GLY D CA  1 
ATOM   3584  C  C   . GLY D  1 33  ? 90.348  -15.440 22.468 1.00 24.95  ? 33   GLY D C   1 
ATOM   3585  O  O   . GLY D  1 33  ? 89.125  -15.346 22.395 1.00 27.21  ? 33   GLY D O   1 
ATOM   3586  N  N   . SER D  1 34  ? 91.039  -15.306 23.575 1.00 26.26  ? 34   SER D N   1 
ATOM   3587  C  CA  . SER D  1 34  ? 90.420  -15.150 24.877 1.00 25.87  ? 34   SER D CA  1 
ATOM   3588  C  C   . SER D  1 34  ? 91.063  -14.009 25.660 1.00 30.03  ? 34   SER D C   1 
ATOM   3589  O  O   . SER D  1 34  ? 92.291  -13.933 25.659 1.00 27.84  ? 34   SER D O   1 
ATOM   3590  C  CB  . SER D  1 34  ? 90.571  -16.441 25.692 1.00 32.81  ? 34   SER D CB  1 
ATOM   3591  O  OG  . SER D  1 34  ? 89.660  -16.408 26.782 1.00 39.30  ? 34   SER D OG  1 
ATOM   3592  N  N   . ILE D  1 35  ? 90.226  -13.191 26.298 1.00 19.70  ? 35   ILE D N   1 
ATOM   3593  C  CA  . ILE D  1 35  ? 90.731  -12.119 27.149 1.00 18.56  ? 35   ILE D CA  1 
ATOM   3594  C  C   . ILE D  1 35  ? 90.034  -12.259 28.497 1.00 23.18  ? 35   ILE D C   1 
ATOM   3595  O  O   . ILE D  1 35  ? 88.805  -12.447 28.518 1.00 26.86  ? 35   ILE D O   1 
ATOM   3596  C  CB  . ILE D  1 35  ? 90.446  -10.721 26.578 1.00 21.16  ? 35   ILE D CB  1 
ATOM   3597  C  CG1 . ILE D  1 35  ? 90.841  -10.543 25.106 1.00 24.58  ? 35   ILE D CG1 1 
ATOM   3598  C  CG2 . ILE D  1 35  ? 91.085  -9.629  27.425 1.00 22.50  ? 35   ILE D CG2 1 
ATOM   3599  C  CD1 . ILE D  1 35  ? 90.382  -9.192  24.580 1.00 25.62  ? 35   ILE D CD1 1 
ATOM   3600  N  N   . LYS D  1 36  ? 90.790  -12.230 29.586 1.00 19.96  ? 36   LYS D N   1 
ATOM   3601  C  CA  . LYS D  1 36  ? 90.110  -12.379 30.880 1.00 19.80  ? 36   LYS D CA  1 
ATOM   3602  C  C   . LYS D  1 36  ? 90.290  -11.098 31.673 1.00 25.18  ? 36   LYS D C   1 
ATOM   3603  O  O   . LYS D  1 36  ? 90.998  -10.177 31.251 1.00 24.63  ? 36   LYS D O   1 
ATOM   3604  C  CB  . LYS D  1 36  ? 90.641  -13.571 31.680 1.00 28.69  ? 36   LYS D CB  1 
ATOM   3605  C  CG  . LYS D  1 36  ? 92.139  -13.504 31.939 1.00 30.54  ? 36   LYS D CG  1 
ATOM   3606  C  CD  . LYS D  1 36  ? 92.538  -14.461 33.059 1.00 50.96  ? 36   LYS D CD  1 
ATOM   3607  C  CE  . LYS D  1 36  ? 93.862  -14.039 33.682 1.00 62.17  ? 36   LYS D CE  1 
ATOM   3608  N  NZ  . LYS D  1 36  ? 94.843  -15.163 33.710 1.00 91.72  ? 36   LYS D NZ  1 
ATOM   3609  N  N   . GLY D  1 37  ? 89.633  -11.037 32.832 1.00 22.78  ? 37   GLY D N   1 
ATOM   3610  C  CA  . GLY D  1 37  ? 89.830  -9.883  33.685 1.00 20.40  ? 37   GLY D CA  1 
ATOM   3611  C  C   . GLY D  1 37  ? 88.908  -8.723  33.403 1.00 23.40  ? 37   GLY D C   1 
ATOM   3612  O  O   . GLY D  1 37  ? 89.084  -7.646  33.982 1.00 23.49  ? 37   GLY D O   1 
ATOM   3613  N  N   . LEU D  1 38  ? 87.904  -8.913  32.518 1.00 25.20  ? 38   LEU D N   1 
ATOM   3614  C  CA  . LEU D  1 38  ? 87.082  -7.809  32.043 1.00 24.91  ? 38   LEU D CA  1 
ATOM   3615  C  C   . LEU D  1 38  ? 85.731  -7.688  32.740 1.00 20.45  ? 38   LEU D C   1 
ATOM   3616  O  O   . LEU D  1 38  ? 85.123  -8.714  33.046 1.00 23.35  ? 38   LEU D O   1 
ATOM   3617  C  CB  . LEU D  1 38  ? 86.810  -7.975  30.535 1.00 21.17  ? 38   LEU D CB  1 
ATOM   3618  C  CG  . LEU D  1 38  ? 87.994  -7.698  29.595 1.00 24.04  ? 38   LEU D CG  1 
ATOM   3619  C  CD1 . LEU D  1 38  ? 87.667  -8.280  28.216 1.00 26.43  ? 38   LEU D CD1 1 
ATOM   3620  C  CD2 . LEU D  1 38  ? 88.302  -6.212  29.497 1.00 21.82  ? 38   LEU D CD2 1 
ATOM   3621  N  N   . THR D  1 39  ? 85.250  -6.455  32.949 1.00 22.87  ? 39   THR D N   1 
ATOM   3622  C  CA  . THR D  1 39  ? 83.891  -6.401  33.527 1.00 25.38  ? 39   THR D CA  1 
ATOM   3623  C  C   . THR D  1 39  ? 82.873  -6.961  32.534 1.00 29.48  ? 39   THR D C   1 
ATOM   3624  O  O   . THR D  1 39  ? 83.047  -6.864  31.309 1.00 23.74  ? 39   THR D O   1 
ATOM   3625  C  CB  . THR D  1 39  ? 83.478  -4.978  33.919 1.00 28.04  ? 39   THR D CB  1 
ATOM   3626  O  OG1 . THR D  1 39  ? 83.580  -4.110  32.776 1.00 24.51  ? 39   THR D OG1 1 
ATOM   3627  C  CG2 . THR D  1 39  ? 84.425  -4.426  34.994 1.00 26.55  ? 39   THR D CG2 1 
ATOM   3628  N  N   . GLU D  1 40  ? 81.799  -7.547  33.055 1.00 26.73  ? 40   GLU D N   1 
ATOM   3629  C  CA  . GLU D  1 40  ? 80.796  -8.165  32.194 1.00 24.35  ? 40   GLU D CA  1 
ATOM   3630  C  C   . GLU D  1 40  ? 80.216  -7.127  31.245 1.00 23.15  ? 40   GLU D C   1 
ATOM   3631  O  O   . GLU D  1 40  ? 79.902  -5.980  31.591 1.00 25.92  ? 40   GLU D O   1 
ATOM   3632  C  CB  . GLU D  1 40  ? 79.681  -8.810  33.032 1.00 26.22  ? 40   GLU D CB  1 
ATOM   3633  C  CG  . GLU D  1 40  ? 78.679  -9.558  32.180 1.00 35.40  ? 40   GLU D CG  1 
ATOM   3634  C  CD  . GLU D  1 40  ? 77.568  -10.249 32.943 1.00 52.50  ? 40   GLU D CD  1 
ATOM   3635  O  OE1 . GLU D  1 40  ? 76.845  -11.063 32.315 1.00 56.03  ? 40   GLU D OE1 1 
ATOM   3636  O  OE2 . GLU D  1 40  ? 77.419  -9.981  34.155 1.00 46.48  ? 40   GLU D OE2 1 
ATOM   3637  N  N   . GLY D  1 41  ? 80.074  -7.522  29.977 1.00 24.55  ? 41   GLY D N   1 
ATOM   3638  C  CA  . GLY D  1 41  ? 79.495  -6.611  28.997 1.00 22.86  ? 41   GLY D CA  1 
ATOM   3639  C  C   . GLY D  1 41  ? 80.462  -6.192  27.902 1.00 22.89  ? 41   GLY D C   1 
ATOM   3640  O  O   . GLY D  1 41  ? 81.471  -6.851  27.653 1.00 22.72  ? 41   GLY D O   1 
ATOM   3641  N  N   . LEU D  1 42  ? 80.154  -5.096  27.225 1.00 21.08  ? 42   LEU D N   1 
ATOM   3642  C  CA  . LEU D  1 42  ? 80.866  -4.709  26.019 1.00 22.10  ? 42   LEU D CA  1 
ATOM   3643  C  C   . LEU D  1 42  ? 82.130  -3.919  26.311 1.00 23.74  ? 42   LEU D C   1 
ATOM   3644  O  O   . LEU D  1 42  ? 82.118  -3.045  27.188 1.00 23.70  ? 42   LEU D O   1 
ATOM   3645  C  CB  . LEU D  1 42  ? 79.978  -3.782  25.165 1.00 24.20  ? 42   LEU D CB  1 
ATOM   3646  C  CG  . LEU D  1 42  ? 78.733  -4.398  24.532 1.00 23.71  ? 42   LEU D CG  1 
ATOM   3647  C  CD1 . LEU D  1 42  ? 77.838  -3.260  24.024 1.00 24.32  ? 42   LEU D CD1 1 
ATOM   3648  C  CD2 . LEU D  1 42  ? 79.061  -5.371  23.419 1.00 21.17  ? 42   LEU D CD2 1 
ATOM   3649  N  N   . HIS D  1 43  ? 83.198  -4.168  25.583 1.00 18.61  ? 43   HIS D N   1 
ATOM   3650  C  CA  . HIS D  1 43  ? 84.430  -3.397  25.678 1.00 19.99  ? 43   HIS D CA  1 
ATOM   3651  C  C   . HIS D  1 43  ? 84.924  -3.014  24.285 1.00 18.70  ? 43   HIS D C   1 
ATOM   3652  O  O   . HIS D  1 43  ? 85.042  -3.921  23.453 1.00 18.03  ? 43   HIS D O   1 
ATOM   3653  C  CB  . HIS D  1 43  ? 85.537  -4.230  26.387 1.00 19.71  ? 43   HIS D CB  1 
ATOM   3654  C  CG  . HIS D  1 43  ? 85.125  -4.472  27.818 1.00 20.48  ? 43   HIS D CG  1 
ATOM   3655  N  ND1 . HIS D  1 43  ? 85.468  -3.630  28.840 1.00 25.24  ? 43   HIS D ND1 1 
ATOM   3656  C  CD2 . HIS D  1 43  ? 84.345  -5.430  28.374 1.00 24.40  ? 43   HIS D CD2 1 
ATOM   3657  C  CE1 . HIS D  1 43  ? 84.941  -4.065  29.988 1.00 22.90  ? 43   HIS D CE1 1 
ATOM   3658  N  NE2 . HIS D  1 43  ? 84.258  -5.163  29.729 1.00 21.94  ? 43   HIS D NE2 1 
ATOM   3659  N  N   . GLY D  1 44  ? 85.236  -1.729  24.075 1.00 19.40  ? 44   GLY D N   1 
ATOM   3660  C  CA  . GLY D  1 44  ? 85.793  -1.309  22.782 1.00 19.19  ? 44   GLY D CA  1 
ATOM   3661  C  C   . GLY D  1 44  ? 87.043  -2.089  22.428 1.00 19.07  ? 44   GLY D C   1 
ATOM   3662  O  O   . GLY D  1 44  ? 87.797  -2.479  23.329 1.00 19.35  ? 44   GLY D O   1 
ATOM   3663  N  N   . PHE D  1 45  ? 87.261  -2.342  21.142 1.00 18.46  ? 45   PHE D N   1 
ATOM   3664  C  CA  . PHE D  1 45  ? 88.331  -3.222  20.678 1.00 18.87  ? 45   PHE D CA  1 
ATOM   3665  C  C   . PHE D  1 45  ? 88.896  -2.698  19.378 1.00 25.97  ? 45   PHE D C   1 
ATOM   3666  O  O   . PHE D  1 45  ? 88.188  -2.704  18.354 1.00 19.23  ? 45   PHE D O   1 
ATOM   3667  C  CB  . PHE D  1 45  ? 87.745  -4.630  20.488 1.00 16.63  ? 45   PHE D CB  1 
ATOM   3668  C  CG  . PHE D  1 45  ? 88.681  -5.794  20.287 1.00 19.68  ? 45   PHE D CG  1 
ATOM   3669  C  CD1 . PHE D  1 45  ? 89.601  -6.179  21.251 1.00 20.72  ? 45   PHE D CD1 1 
ATOM   3670  C  CD2 . PHE D  1 45  ? 88.640  -6.528  19.111 1.00 19.93  ? 45   PHE D CD2 1 
ATOM   3671  C  CE1 . PHE D  1 45  ? 90.426  -7.275  21.040 1.00 21.07  ? 45   PHE D CE1 1 
ATOM   3672  C  CE2 . PHE D  1 45  ? 89.435  -7.627  18.901 1.00 20.62  ? 45   PHE D CE2 1 
ATOM   3673  C  CZ  . PHE D  1 45  ? 90.349  -8.013  19.883 1.00 20.62  ? 45   PHE D CZ  1 
ATOM   3674  N  N   . HIS D  1 46  ? 90.124  -2.145  19.356 1.00 18.87  ? 46   HIS D N   1 
ATOM   3675  C  CA  . HIS D  1 46  ? 90.556  -1.510  18.105 1.00 17.29  ? 46   HIS D CA  1 
ATOM   3676  C  C   . HIS D  1 46  ? 92.050  -1.689  17.868 1.00 21.93  ? 46   HIS D C   1 
ATOM   3677  O  O   . HIS D  1 46  ? 92.821  -1.896  18.810 1.00 20.73  ? 46   HIS D O   1 
ATOM   3678  C  CB  . HIS D  1 46  ? 90.356  0.014   18.088 1.00 17.95  ? 46   HIS D CB  1 
ATOM   3679  C  CG  . HIS D  1 46  ? 89.199  0.519   18.887 1.00 23.30  ? 46   HIS D CG  1 
ATOM   3680  N  ND1 . HIS D  1 46  ? 89.281  1.061   20.142 1.00 21.06  ? 46   HIS D ND1 1 
ATOM   3681  C  CD2 . HIS D  1 46  ? 87.876  0.473   18.586 1.00 22.60  ? 46   HIS D CD2 1 
ATOM   3682  C  CE1 . HIS D  1 46  ? 88.079  1.377   20.589 1.00 22.20  ? 46   HIS D CE1 1 
ATOM   3683  N  NE2 . HIS D  1 46  ? 87.209  1.027   19.651 1.00 21.86  ? 46   HIS D NE2 1 
ATOM   3684  N  N   . VAL D  1 47  ? 92.429  -1.534  16.599 1.00 18.85  ? 47   VAL D N   1 
ATOM   3685  C  CA  . VAL D  1 47  ? 93.843  -1.467  16.230 1.00 17.97  ? 47   VAL D CA  1 
ATOM   3686  C  C   . VAL D  1 47  ? 94.253  -0.003  16.251 1.00 23.44  ? 47   VAL D C   1 
ATOM   3687  O  O   . VAL D  1 47  ? 93.624  0.842   15.619 1.00 22.71  ? 47   VAL D O   1 
ATOM   3688  C  CB  . VAL D  1 47  ? 94.148  -2.048  14.846 1.00 16.00  ? 47   VAL D CB  1 
ATOM   3689  C  CG1 . VAL D  1 47  ? 95.643  -1.917  14.558 1.00 22.75  ? 47   VAL D CG1 1 
ATOM   3690  C  CG2 . VAL D  1 47  ? 93.712  -3.495  14.768 1.00 19.08  ? 47   VAL D CG2 1 
ATOM   3691  N  N   . HIS D  1 48  ? 95.309  0.289   17.006 1.00 22.52  ? 48   HIS D N   1 
ATOM   3692  C  CA  . HIS D  1 48  ? 95.774  1.676   17.120 1.00 21.42  ? 48   HIS D CA  1 
ATOM   3693  C  C   . HIS D  1 48  ? 97.021  1.830   16.243 1.00 18.04  ? 48   HIS D C   1 
ATOM   3694  O  O   . HIS D  1 48  ? 97.649  0.844   15.859 1.00 23.72  ? 48   HIS D O   1 
ATOM   3695  C  CB  . HIS D  1 48  ? 96.012  2.042   18.568 1.00 22.69  ? 48   HIS D CB  1 
ATOM   3696  C  CG  . HIS D  1 48  ? 94.785  2.248   19.414 1.00 21.13  ? 48   HIS D CG  1 
ATOM   3697  N  ND1 . HIS D  1 48  ? 94.562  3.425   20.093 1.00 19.97  ? 48   HIS D ND1 1 
ATOM   3698  C  CD2 . HIS D  1 48  ? 93.732  1.453   19.700 1.00 23.09  ? 48   HIS D CD2 1 
ATOM   3699  C  CE1 . HIS D  1 48  ? 93.416  3.355   20.768 1.00 25.17  ? 48   HIS D CE1 1 
ATOM   3700  N  NE2 . HIS D  1 48  ? 92.896  2.161   20.541 1.00 24.47  ? 48   HIS D NE2 1 
ATOM   3701  N  N   . GLU D  1 49  ? 97.317  3.070   15.933 1.00 21.78  ? 49   GLU D N   1 
ATOM   3702  C  CA  . GLU D  1 49  ? 98.309  3.409   14.924 1.00 22.27  ? 49   GLU D CA  1 
ATOM   3703  C  C   . GLU D  1 49  ? 99.713  2.922   15.237 1.00 26.23  ? 49   GLU D C   1 
ATOM   3704  O  O   . GLU D  1 49  ? 100.384 2.347   14.372 1.00 23.34  ? 49   GLU D O   1 
ATOM   3705  C  CB  . GLU D  1 49  ? 98.335  4.945   14.755 1.00 23.47  ? 49   GLU D CB  1 
ATOM   3706  C  CG  . GLU D  1 49  ? 99.032  5.326   13.459 1.00 28.88  ? 49   GLU D CG  1 
ATOM   3707  C  CD  . GLU D  1 49  ? 98.987  6.822   13.203 1.00 30.02  ? 49   GLU D CD  1 
ATOM   3708  O  OE1 . GLU D  1 49  ? 99.532  7.216   12.152 1.00 38.94  ? 49   GLU D OE1 1 
ATOM   3709  O  OE2 . GLU D  1 49  ? 98.439  7.571   14.030 1.00 32.89  ? 49   GLU D OE2 1 
ATOM   3710  N  N   . PHE D  1 50  ? 100.203 3.130   16.450 1.00 25.36  ? 50   PHE D N   1 
ATOM   3711  C  CA  . PHE D  1 50  ? 101.613 2.764   16.677 1.00 29.35  ? 50   PHE D CA  1 
ATOM   3712  C  C   . PHE D  1 50  ? 101.826 1.503   17.503 1.00 26.20  ? 50   PHE D C   1 
ATOM   3713  O  O   . PHE D  1 50  ? 101.151 1.293   18.505 1.00 25.45  ? 50   PHE D O   1 
ATOM   3714  C  CB  . PHE D  1 50  ? 102.282 3.955   17.370 1.00 22.98  ? 50   PHE D CB  1 
ATOM   3715  C  CG  . PHE D  1 50  ? 102.054 5.237   16.594 1.00 21.26  ? 50   PHE D CG  1 
ATOM   3716  C  CD1 . PHE D  1 50  ? 102.493 5.300   15.279 1.00 29.69  ? 50   PHE D CD1 1 
ATOM   3717  C  CD2 . PHE D  1 50  ? 101.432 6.319   17.169 1.00 27.51  ? 50   PHE D CD2 1 
ATOM   3718  C  CE1 . PHE D  1 50  ? 102.285 6.469   14.560 1.00 32.55  ? 50   PHE D CE1 1 
ATOM   3719  C  CE2 . PHE D  1 50  ? 101.215 7.490   16.457 1.00 29.78  ? 50   PHE D CE2 1 
ATOM   3720  C  CZ  . PHE D  1 50  ? 101.653 7.544   15.139 1.00 28.91  ? 50   PHE D CZ  1 
ATOM   3721  N  N   . GLY D  1 51  ? 102.781 0.682   17.113 1.00 21.84  ? 51   GLY D N   1 
ATOM   3722  C  CA  . GLY D  1 51  ? 103.242 -0.501  17.833 1.00 23.24  ? 51   GLY D CA  1 
ATOM   3723  C  C   . GLY D  1 51  ? 104.261 -0.061  18.890 1.00 25.38  ? 51   GLY D C   1 
ATOM   3724  O  O   . GLY D  1 51  ? 105.321 -0.667  19.018 1.00 27.09  ? 51   GLY D O   1 
ATOM   3725  N  N   . ASP D  1 52  ? 103.927 0.999   19.606 1.00 25.88  ? 52   ASP D N   1 
ATOM   3726  C  CA  . ASP D  1 52  ? 104.808 1.636   20.579 1.00 26.69  ? 52   ASP D CA  1 
ATOM   3727  C  C   . ASP D  1 52  ? 104.282 1.439   22.001 1.00 27.80  ? 52   ASP D C   1 
ATOM   3728  O  O   . ASP D  1 52  ? 103.316 2.106   22.368 1.00 28.20  ? 52   ASP D O   1 
ATOM   3729  C  CB  . ASP D  1 52  ? 104.970 3.127   20.289 1.00 25.85  ? 52   ASP D CB  1 
ATOM   3730  C  CG  . ASP D  1 52  ? 105.921 3.876   21.200 1.00 39.10  ? 52   ASP D CG  1 
ATOM   3731  O  OD1 . ASP D  1 52  ? 106.363 5.008   20.875 1.00 31.38  ? 52   ASP D OD1 1 
ATOM   3732  O  OD2 . ASP D  1 52  ? 106.261 3.362   22.288 1.00 30.87  ? 52   ASP D OD2 1 
ATOM   3733  N  N   . ASN D  1 53  ? 104.983 0.587   22.746 1.00 27.40  ? 53   ASN D N   1 
ATOM   3734  C  CA  . ASN D  1 53  ? 104.586 0.360   24.131 1.00 28.31  ? 53   ASN D CA  1 
ATOM   3735  C  C   . ASN D  1 53  ? 105.537 1.008   25.121 1.00 31.51  ? 53   ASN D C   1 
ATOM   3736  O  O   . ASN D  1 53  ? 105.601 0.588   26.283 1.00 33.89  ? 53   ASN D O   1 
ATOM   3737  C  CB  . ASN D  1 53  ? 104.506 -1.156  24.382 1.00 30.92  ? 53   ASN D CB  1 
ATOM   3738  C  CG  . ASN D  1 53  ? 103.832 -1.483  25.706 1.00 42.98  ? 53   ASN D CG  1 
ATOM   3739  O  OD1 . ASN D  1 53  ? 104.448 -2.105  26.568 1.00 46.60  ? 53   ASN D OD1 1 
ATOM   3740  N  ND2 . ASN D  1 53  ? 102.590 -1.038  25.866 1.00 57.58  ? 53   ASN D ND2 1 
ATOM   3741  N  N   . THR D  1 54  ? 106.285 2.032   24.716 1.00 29.57  ? 54   THR D N   1 
ATOM   3742  C  CA  . THR D  1 54  ? 107.288 2.575   25.640 1.00 34.14  ? 54   THR D CA  1 
ATOM   3743  C  C   . THR D  1 54  ? 106.632 3.129   26.902 1.00 45.89  ? 54   THR D C   1 
ATOM   3744  O  O   . THR D  1 54  ? 107.213 3.020   27.986 1.00 48.84  ? 54   THR D O   1 
ATOM   3745  C  CB  . THR D  1 54  ? 108.190 3.653   25.000 1.00 29.86  ? 54   THR D CB  1 
ATOM   3746  O  OG1 . THR D  1 54  ? 107.455 4.696   24.365 1.00 31.45  ? 54   THR D OG1 1 
ATOM   3747  C  CG2 . THR D  1 54  ? 109.014 3.013   23.883 1.00 29.28  ? 54   THR D CG2 1 
ATOM   3748  N  N   . ALA D  1 55  ? 105.441 3.700   26.753 1.00 36.44  ? 55   ALA D N   1 
ATOM   3749  C  CA  . ALA D  1 55  ? 104.660 4.267   27.834 1.00 31.17  ? 55   ALA D CA  1 
ATOM   3750  C  C   . ALA D  1 55  ? 103.312 3.560   27.977 1.00 38.65  ? 55   ALA D C   1 
ATOM   3751  O  O   . ALA D  1 55  ? 102.270 4.223   27.954 1.00 47.27  ? 55   ALA D O   1 
ATOM   3752  C  CB  . ALA D  1 55  ? 104.443 5.758   27.555 1.00 29.34  ? 55   ALA D CB  1 
ATOM   3753  N  N   . GLY D  1 56  ? 103.303 2.240   28.099 1.00 32.47  ? 56   GLY D N   1 
ATOM   3754  C  CA  . GLY D  1 56  ? 102.099 1.430   28.169 1.00 31.88  ? 56   GLY D CA  1 
ATOM   3755  C  C   . GLY D  1 56  ? 101.229 1.625   26.946 1.00 31.30  ? 56   GLY D C   1 
ATOM   3756  O  O   . GLY D  1 56  ? 101.716 1.921   25.862 1.00 27.83  ? 56   GLY D O   1 
ATOM   3757  N  N   . CYS D  1 57  ? 99.911  1.485   27.094 1.00 31.86  ? 57   CYS D N   1 
ATOM   3758  C  CA  . CYS D  1 57  ? 99.020  1.602   25.942 1.00 25.47  ? 57   CYS D CA  1 
ATOM   3759  C  C   . CYS D  1 57  ? 98.920  3.019   25.430 1.00 26.87  ? 57   CYS D C   1 
ATOM   3760  O  O   . CYS D  1 57  ? 98.495  3.273   24.310 1.00 26.94  ? 57   CYS D O   1 
ATOM   3761  C  CB  A CYS D  1 57  ? 97.600  1.141   26.333 0.43 24.12  ? 57   CYS D CB  1 
ATOM   3762  C  CB  B CYS D  1 57  ? 97.633  1.038   26.305 0.57 25.91  ? 57   CYS D CB  1 
ATOM   3763  S  SG  A CYS D  1 57  ? 97.544  -0.571  26.926 0.43 43.78  ? 57   CYS D SG  1 
ATOM   3764  S  SG  B CYS D  1 57  ? 97.718  -0.561  27.160 0.57 29.60  ? 57   CYS D SG  1 
ATOM   3765  N  N   . THR D  1 58  ? 99.310  3.999   26.248 1.00 28.47  ? 58   THR D N   1 
ATOM   3766  C  CA  . THR D  1 58  ? 99.137  5.396   25.870 1.00 31.30  ? 58   THR D CA  1 
ATOM   3767  C  C   . THR D  1 58  ? 99.909  5.748   24.613 1.00 29.31  ? 58   THR D C   1 
ATOM   3768  O  O   . THR D  1 58  ? 99.509  6.501   23.726 1.00 32.31  ? 58   THR D O   1 
ATOM   3769  C  CB  . THR D  1 58  ? 99.629  6.304   27.019 1.00 36.01  ? 58   THR D CB  1 
ATOM   3770  O  OG1 . THR D  1 58  ? 98.784  6.086   28.153 1.00 44.12  ? 58   THR D OG1 1 
ATOM   3771  C  CG2 . THR D  1 58  ? 99.525  7.762   26.617 1.00 38.85  ? 58   THR D CG2 1 
ATOM   3772  N  N   . SER D  1 59  ? 101.102 5.149   24.514 1.00 27.70  ? 59   SER D N   1 
ATOM   3773  C  CA  . SER D  1 59  ? 101.968 5.522   23.397 1.00 24.80  ? 59   SER D CA  1 
ATOM   3774  C  C   . SER D  1 59  ? 101.519 4.880   22.103 1.00 28.88  ? 59   SER D C   1 
ATOM   3775  O  O   . SER D  1 59  ? 102.094 5.113   21.035 1.00 25.25  ? 59   SER D O   1 
ATOM   3776  C  CB  . SER D  1 59  ? 103.410 5.143   23.764 1.00 28.32  ? 59   SER D CB  1 
ATOM   3777  O  OG  . SER D  1 59  ? 103.496 3.874   24.387 1.00 31.67  ? 59   SER D OG  1 
ATOM   3778  N  N   . ALA D  1 60  ? 100.456 4.046   22.165 1.00 26.62  ? 60   ALA D N   1 
ATOM   3779  C  CA  . ALA D  1 60  ? 99.974  3.486   20.898 1.00 23.03  ? 60   ALA D CA  1 
ATOM   3780  C  C   . ALA D  1 60  ? 99.305  4.496   19.968 1.00 26.15  ? 60   ALA D C   1 
ATOM   3781  O  O   . ALA D  1 60  ? 99.026  4.184   18.797 1.00 27.29  ? 60   ALA D O   1 
ATOM   3782  C  CB  . ALA D  1 60  ? 98.982  2.361   21.192 1.00 21.62  ? 60   ALA D CB  1 
ATOM   3783  N  N   . GLY D  1 61  ? 98.999  5.692   20.429 1.00 24.99  ? 61   GLY D N   1 
ATOM   3784  C  CA  . GLY D  1 61  ? 98.378  6.721   19.619 1.00 25.34  ? 61   GLY D CA  1 
ATOM   3785  C  C   . GLY D  1 61  ? 96.882  6.419   19.408 1.00 22.70  ? 61   GLY D C   1 
ATOM   3786  O  O   . GLY D  1 61  ? 96.367  5.591   20.169 1.00 23.56  ? 61   GLY D O   1 
ATOM   3787  N  N   . PRO D  1 62  ? 96.326  7.075   18.401 1.00 26.75  ? 62   PRO D N   1 
ATOM   3788  C  CA  . PRO D  1 62  ? 94.875  6.985   18.121 1.00 23.13  ? 62   PRO D CA  1 
ATOM   3789  C  C   . PRO D  1 62  ? 94.557  5.750   17.309 1.00 20.89  ? 62   PRO D C   1 
ATOM   3790  O  O   . PRO D  1 62  ? 95.386  4.903   16.985 1.00 20.38  ? 62   PRO D O   1 
ATOM   3791  C  CB  . PRO D  1 62  ? 94.645  8.269   17.312 1.00 24.79  ? 62   PRO D CB  1 
ATOM   3792  C  CG  . PRO D  1 62  ? 95.886  8.341   16.460 1.00 26.16  ? 62   PRO D CG  1 
ATOM   3793  C  CD  . PRO D  1 62  ? 96.988  7.928   17.399 1.00 23.64  ? 62   PRO D CD  1 
ATOM   3794  N  N   . HIS D  1 63  ? 93.276  5.584   16.935 1.00 22.71  ? 63   HIS D N   1 
ATOM   3795  C  CA  . HIS D  1 63  ? 92.911  4.436   16.100 1.00 21.36  ? 63   HIS D CA  1 
ATOM   3796  C  C   . HIS D  1 63  ? 93.626  4.497   14.750 1.00 22.05  ? 63   HIS D C   1 
ATOM   3797  O  O   . HIS D  1 63  ? 93.779  5.564   14.157 1.00 23.43  ? 63   HIS D O   1 
ATOM   3798  C  CB  . HIS D  1 63  ? 91.402  4.353   15.870 1.00 20.19  ? 63   HIS D CB  1 
ATOM   3799  C  CG  . HIS D  1 63  ? 90.576  4.304   17.110 1.00 23.73  ? 63   HIS D CG  1 
ATOM   3800  N  ND1 . HIS D  1 63  ? 89.187  4.257   17.120 1.00 21.08  ? 63   HIS D ND1 1 
ATOM   3801  C  CD2 . HIS D  1 63  ? 90.975  4.301   18.410 1.00 24.01  ? 63   HIS D CD2 1 
ATOM   3802  C  CE1 . HIS D  1 63  ? 88.790  4.219   18.391 1.00 19.57  ? 63   HIS D CE1 1 
ATOM   3803  N  NE2 . HIS D  1 63  ? 89.843  4.248   19.187 1.00 27.03  ? 63   HIS D NE2 1 
ATOM   3804  N  N   . PHE D  1 64  ? 94.067  3.345   14.270 1.00 21.17  ? 64   PHE D N   1 
ATOM   3805  C  CA  . PHE D  1 64  ? 94.694  3.248   12.944 1.00 20.77  ? 64   PHE D CA  1 
ATOM   3806  C  C   . PHE D  1 64  ? 93.731  3.786   11.895 1.00 24.06  ? 64   PHE D C   1 
ATOM   3807  O  O   . PHE D  1 64  ? 92.626  3.247   11.789 1.00 22.20  ? 64   PHE D O   1 
ATOM   3808  C  CB  . PHE D  1 64  ? 95.065  1.786   12.704 1.00 21.52  ? 64   PHE D CB  1 
ATOM   3809  C  CG  . PHE D  1 64  ? 95.725  1.533   11.355 1.00 22.43  ? 64   PHE D CG  1 
ATOM   3810  C  CD1 . PHE D  1 64  ? 95.413  0.431   10.606 1.00 22.35  ? 64   PHE D CD1 1 
ATOM   3811  C  CD2 . PHE D  1 64  ? 96.671  2.435   10.881 1.00 28.09  ? 64   PHE D CD2 1 
ATOM   3812  C  CE1 . PHE D  1 64  ? 95.994  0.189   9.368  1.00 25.65  ? 64   PHE D CE1 1 
ATOM   3813  C  CE2 . PHE D  1 64  ? 97.261  2.216   9.642  1.00 29.86  ? 64   PHE D CE2 1 
ATOM   3814  C  CZ  . PHE D  1 64  ? 96.946  1.095   8.910  1.00 30.51  ? 64   PHE D CZ  1 
ATOM   3815  N  N   . ASN D  1 65  ? 94.077  4.825   11.138 1.00 24.07  ? 65   ASN D N   1 
ATOM   3816  C  CA  . ASN D  1 65  ? 93.115  5.558   10.316 1.00 24.04  ? 65   ASN D CA  1 
ATOM   3817  C  C   . ASN D  1 65  ? 93.778  6.140   9.058  1.00 24.81  ? 65   ASN D C   1 
ATOM   3818  O  O   . ASN D  1 65  ? 93.782  7.354   8.907  1.00 31.60  ? 65   ASN D O   1 
ATOM   3819  C  CB  . ASN D  1 65  ? 92.517  6.717   11.107 1.00 22.85  ? 65   ASN D CB  1 
ATOM   3820  C  CG  . ASN D  1 65  ? 91.423  7.486   10.411 1.00 21.74  ? 65   ASN D CG  1 
ATOM   3821  O  OD1 . ASN D  1 65  ? 90.761  6.972   9.519  1.00 29.27  ? 65   ASN D OD1 1 
ATOM   3822  N  ND2 . ASN D  1 65  ? 91.141  8.711   10.818 1.00 30.50  ? 65   ASN D ND2 1 
ATOM   3823  N  N   . PRO D  1 66  ? 94.299  5.282   8.200  1.00 26.91  ? 66   PRO D N   1 
ATOM   3824  C  CA  . PRO D  1 66  ? 95.068  5.742   7.041  1.00 35.45  ? 66   PRO D CA  1 
ATOM   3825  C  C   . PRO D  1 66  ? 94.214  6.527   6.053  1.00 45.88  ? 66   PRO D C   1 
ATOM   3826  O  O   . PRO D  1 66  ? 94.779  7.245   5.218  1.00 38.64  ? 66   PRO D O   1 
ATOM   3827  C  CB  . PRO D  1 66  ? 95.556  4.437   6.395  1.00 34.17  ? 66   PRO D CB  1 
ATOM   3828  C  CG  . PRO D  1 66  ? 94.539  3.429   6.821  1.00 36.45  ? 66   PRO D CG  1 
ATOM   3829  C  CD  . PRO D  1 66  ? 94.184  3.821   8.232  1.00 25.08  ? 66   PRO D CD  1 
ATOM   3830  N  N   . LEU D  1 67  ? 92.895  6.408   6.137  1.00 41.78  ? 67   LEU D N   1 
ATOM   3831  C  CA  . LEU D  1 67  ? 92.003  7.107   5.209  1.00 32.75  ? 67   LEU D CA  1 
ATOM   3832  C  C   . LEU D  1 67  ? 91.383  8.344   5.813  1.00 34.71  ? 67   LEU D C   1 
ATOM   3833  O  O   . LEU D  1 67  ? 90.540  8.973   5.158  1.00 40.53  ? 67   LEU D O   1 
ATOM   3834  C  CB  . LEU D  1 67  ? 90.893  6.154   4.734  1.00 31.99  ? 67   LEU D CB  1 
ATOM   3835  C  CG  . LEU D  1 67  ? 91.450  5.062   3.815  1.00 32.82  ? 67   LEU D CG  1 
ATOM   3836  C  CD1 . LEU D  1 67  ? 90.596  3.812   3.787  1.00 38.94  ? 67   LEU D CD1 1 
ATOM   3837  C  CD2 . LEU D  1 67  ? 91.600  5.654   2.415  1.00 74.34  ? 67   LEU D CD2 1 
ATOM   3838  N  N   . SER D  1 68  ? 91.824  8.657   7.022  1.00 33.66  ? 68   SER D N   1 
ATOM   3839  C  CA  . SER D  1 68  ? 91.379  9.860   7.716  1.00 38.22  ? 68   SER D CA  1 
ATOM   3840  C  C   . SER D  1 68  ? 89.852  9.952   7.750  1.00 47.34  ? 68   SER D C   1 
ATOM   3841  O  O   . SER D  1 68  ? 89.325  11.028  7.445  1.00 33.04  ? 68   SER D O   1 
ATOM   3842  C  CB  . SER D  1 68  ? 91.923  11.131  7.065  1.00 41.24  ? 68   SER D CB  1 
ATOM   3843  O  OG  . SER D  1 68  ? 93.318  11.276  7.222  1.00 55.18  ? 68   SER D OG  1 
ATOM   3844  N  N   . ARG D  1 69  ? 89.219  8.838   8.118  1.00 33.91  ? 69   ARG D N   1 
ATOM   3845  C  CA  . ARG D  1 69  ? 87.770  8.791   8.257  1.00 30.66  ? 69   ARG D CA  1 
ATOM   3846  C  C   . ARG D  1 69  ? 87.361  9.035   9.698  1.00 31.86  ? 69   ARG D C   1 
ATOM   3847  O  O   . ARG D  1 69  ? 88.209  9.048   10.589 1.00 30.41  ? 69   ARG D O   1 
ATOM   3848  C  CB  . ARG D  1 69  ? 87.221  7.450   7.768  1.00 34.60  ? 69   ARG D CB  1 
ATOM   3849  C  CG  . ARG D  1 69  ? 87.320  7.256   6.268  1.00 47.49  ? 69   ARG D CG  1 
ATOM   3850  C  CD  . ARG D  1 69  ? 86.490  6.088   5.754  1.00 63.90  ? 69   ARG D CD  1 
ATOM   3851  N  NE  . ARG D  1 69  ? 86.838  5.720   4.389  1.00 71.59  ? 69   ARG D NE  1 
ATOM   3852  C  CZ  . ARG D  1 69  ? 86.325  4.800   3.596  1.00 70.41  ? 69   ARG D CZ  1 
ATOM   3853  N  NH1 . ARG D  1 69  ? 86.816  4.644   2.367  1.00 59.01  ? 69   ARG D NH1 1 
ATOM   3854  N  NH2 . ARG D  1 69  ? 85.328  4.005   3.960  1.00 53.74  ? 69   ARG D NH2 1 
ATOM   3855  N  N   . LYS D  1 70  ? 86.073  9.236   9.951  1.00 28.61  ? 70   LYS D N   1 
ATOM   3856  C  CA  . LYS D  1 70  ? 85.600  9.366   11.319 1.00 28.76  ? 70   LYS D CA  1 
ATOM   3857  C  C   . LYS D  1 70  ? 85.408  7.981   11.959 1.00 19.98  ? 70   LYS D C   1 
ATOM   3858  O  O   . LYS D  1 70  ? 85.308  7.025   11.214 1.00 24.36  ? 70   LYS D O   1 
ATOM   3859  C  CB  . LYS D  1 70  ? 84.287  10.146  11.369 1.00 39.91  ? 70   LYS D CB  1 
ATOM   3860  C  CG  . LYS D  1 70  ? 84.476  11.661  11.255 1.00 44.32  ? 70   LYS D CG  1 
ATOM   3861  C  CD  . LYS D  1 70  ? 83.102  12.324  11.138 1.00 68.01  ? 70   LYS D CD  1 
ATOM   3862  C  CE  . LYS D  1 70  ? 83.174  13.644  10.396 1.00 82.57  ? 70   LYS D CE  1 
ATOM   3863  N  NZ  . LYS D  1 70  ? 81.888  13.997  9.721  1.00 92.11  ? 70   LYS D NZ  1 
ATOM   3864  N  N   . HIS D  1 71  ? 85.353  7.940   13.295 1.00 21.41  ? 71   HIS D N   1 
ATOM   3865  C  CA  . HIS D  1 71  ? 85.173  6.649   13.970 1.00 19.85  ? 71   HIS D CA  1 
ATOM   3866  C  C   . HIS D  1 71  ? 83.823  6.019   13.665 1.00 22.11  ? 71   HIS D C   1 
ATOM   3867  O  O   . HIS D  1 71  ? 82.792  6.712   13.589 1.00 25.22  ? 71   HIS D O   1 
ATOM   3868  C  CB  . HIS D  1 71  ? 85.340  6.864   15.494 1.00 19.74  ? 71   HIS D CB  1 
ATOM   3869  C  CG  . HIS D  1 71  ? 85.152  5.570   16.242 1.00 21.90  ? 71   HIS D CG  1 
ATOM   3870  N  ND1 . HIS D  1 71  ? 86.112  4.595   16.353 1.00 22.27  ? 71   HIS D ND1 1 
ATOM   3871  C  CD2 . HIS D  1 71  ? 84.063  5.108   16.895 1.00 21.31  ? 71   HIS D CD2 1 
ATOM   3872  C  CE1 . HIS D  1 71  ? 85.636  3.580   17.051 1.00 20.63  ? 71   HIS D CE1 1 
ATOM   3873  N  NE2 . HIS D  1 71  ? 84.387  3.874   17.400 1.00 20.58  ? 71   HIS D NE2 1 
ATOM   3874  N  N   . GLY D  1 72  ? 83.745  4.710   13.482 1.00 21.50  ? 72   GLY D N   1 
ATOM   3875  C  CA  . GLY D  1 72  ? 82.428  4.072   13.270 1.00 20.21  ? 72   GLY D CA  1 
ATOM   3876  C  C   . GLY D  1 72  ? 82.471  2.657   13.819 1.00 26.98  ? 72   GLY D C   1 
ATOM   3877  O  O   . GLY D  1 72  ? 83.437  2.278   14.507 1.00 23.65  ? 72   GLY D O   1 
ATOM   3878  N  N   . GLY D  1 73  ? 81.451  1.856   13.534 1.00 18.48  ? 73   GLY D N   1 
ATOM   3879  C  CA  . GLY D  1 73  ? 81.460  0.450   13.830 1.00 20.14  ? 73   GLY D CA  1 
ATOM   3880  C  C   . GLY D  1 73  ? 82.007  -0.339  12.642 1.00 24.42  ? 73   GLY D C   1 
ATOM   3881  O  O   . GLY D  1 73  ? 82.116  0.179   11.527 1.00 24.09  ? 73   GLY D O   1 
ATOM   3882  N  N   . PRO D  1 74  ? 82.395  -1.581  12.877 1.00 23.13  ? 74   PRO D N   1 
ATOM   3883  C  CA  . PRO D  1 74  ? 83.047  -2.339  11.797 1.00 23.89  ? 74   PRO D CA  1 
ATOM   3884  C  C   . PRO D  1 74  ? 82.138  -2.508  10.580 1.00 27.53  ? 74   PRO D C   1 
ATOM   3885  O  O   . PRO D  1 74  ? 82.664  -2.640  9.464  1.00 22.04  ? 74   PRO D O   1 
ATOM   3886  C  CB  . PRO D  1 74  ? 83.375  -3.688  12.442 1.00 24.12  ? 74   PRO D CB  1 
ATOM   3887  C  CG  . PRO D  1 74  ? 82.474  -3.772  13.647 1.00 22.03  ? 74   PRO D CG  1 
ATOM   3888  C  CD  . PRO D  1 74  ? 82.322  -2.358  14.132 1.00 20.31  ? 74   PRO D CD  1 
ATOM   3889  N  N   . LYS D  1 75  ? 80.816  -2.509  10.750 1.00 21.96  ? 75   LYS D N   1 
ATOM   3890  C  CA  . LYS D  1 75  ? 79.960  -2.651  9.555  1.00 28.08  ? 75   LYS D CA  1 
ATOM   3891  C  C   . LYS D  1 75  ? 79.779  -1.357  8.787  1.00 31.38  ? 75   LYS D C   1 
ATOM   3892  O  O   . LYS D  1 75  ? 79.232  -1.357  7.670  1.00 32.44  ? 75   LYS D O   1 
ATOM   3893  C  CB  . LYS D  1 75  ? 78.570  -3.181  9.959  1.00 32.14  ? 75   LYS D CB  1 
ATOM   3894  C  CG  . LYS D  1 75  ? 78.611  -4.516  10.680 1.00 37.24  ? 75   LYS D CG  1 
ATOM   3895  C  CD  . LYS D  1 75  ? 77.308  -4.827  11.395 1.00 48.01  ? 75   LYS D CD  1 
ATOM   3896  C  CE  . LYS D  1 75  ? 77.178  -4.067  12.703 1.00 60.71  ? 75   LYS D CE  1 
ATOM   3897  N  NZ  . LYS D  1 75  ? 75.828  -3.453  12.866 1.00 92.72  ? 75   LYS D NZ  1 
ATOM   3898  N  N   . ASP D  1 76  ? 80.179  -0.210  9.333  1.00 23.77  ? 76   ASP D N   1 
ATOM   3899  C  CA  . ASP D  1 76  ? 80.036  1.067   8.653  1.00 25.38  ? 76   ASP D CA  1 
ATOM   3900  C  C   . ASP D  1 76  ? 81.058  1.313   7.547  1.00 35.75  ? 76   ASP D C   1 
ATOM   3901  O  O   . ASP D  1 76  ? 82.230  0.940   7.602  1.00 25.14  ? 76   ASP D O   1 
ATOM   3902  C  CB  . ASP D  1 76  ? 80.200  2.221   9.651  1.00 26.18  ? 76   ASP D CB  1 
ATOM   3903  C  CG  . ASP D  1 76  ? 79.055  2.270   10.647 1.00 30.63  ? 76   ASP D CG  1 
ATOM   3904  O  OD1 . ASP D  1 76  ? 79.323  2.593   11.819 1.00 31.54  ? 76   ASP D OD1 1 
ATOM   3905  O  OD2 . ASP D  1 76  ? 77.896  1.993   10.266 1.00 34.49  ? 76   ASP D OD2 1 
ATOM   3906  N  N   . GLU D  1 77  ? 80.617  2.005   6.490  1.00 36.30  ? 77   GLU D N   1 
ATOM   3907  C  CA  . GLU D  1 77  ? 81.605  2.418   5.480  1.00 38.05  ? 77   GLU D CA  1 
ATOM   3908  C  C   . GLU D  1 77  ? 82.456  3.556   6.019  1.00 32.00  ? 77   GLU D C   1 
ATOM   3909  O  O   . GLU D  1 77  ? 83.648  3.699   5.778  1.00 41.35  ? 77   GLU D O   1 
ATOM   3910  C  CB  . GLU D  1 77  ? 80.879  2.814   4.197  1.00 40.68  ? 77   GLU D CB  1 
ATOM   3911  C  CG  . GLU D  1 77  ? 81.787  3.392   3.124  1.00 54.76  ? 77   GLU D CG  1 
ATOM   3912  C  CD  . GLU D  1 77  ? 82.639  2.312   2.484  1.00 68.10  ? 77   GLU D CD  1 
ATOM   3913  O  OE1 . GLU D  1 77  ? 82.267  1.121   2.594  1.00 62.70  ? 77   GLU D OE1 1 
ATOM   3914  O  OE2 . GLU D  1 77  ? 83.672  2.678   1.884  1.00 87.42  ? 77   GLU D OE2 1 
ATOM   3915  N  N   . GLU D  1 78  ? 81.839  4.428   6.813  1.00 23.04  ? 78   GLU D N   1 
ATOM   3916  C  CA  . GLU D  1 78  ? 82.603  5.469   7.472  1.00 26.34  ? 78   GLU D CA  1 
ATOM   3917  C  C   . GLU D  1 78  ? 83.128  4.909   8.799  1.00 27.74  ? 78   GLU D C   1 
ATOM   3918  O  O   . GLU D  1 78  ? 82.417  4.813   9.792  1.00 23.42  ? 78   GLU D O   1 
ATOM   3919  C  CB  . GLU D  1 78  ? 81.753  6.713   7.704  1.00 30.32  ? 78   GLU D CB  1 
ATOM   3920  C  CG  . GLU D  1 78  ? 82.504  7.893   8.283  1.00 33.19  ? 78   GLU D CG  1 
ATOM   3921  C  CD  . GLU D  1 78  ? 83.377  8.619   7.279  1.00 50.68  ? 78   GLU D CD  1 
ATOM   3922  O  OE1 . GLU D  1 78  ? 84.085  9.565   7.704  1.00 36.39  ? 78   GLU D OE1 1 
ATOM   3923  O  OE2 . GLU D  1 78  ? 83.374  8.272   6.074  1.00 50.52  ? 78   GLU D OE2 1 
ATOM   3924  N  N   . ARG D  1 79  ? 84.409  4.545   8.782  1.00 24.94  ? 79   ARG D N   1 
ATOM   3925  C  CA  . ARG D  1 79  ? 85.025  3.996   9.983  1.00 21.60  ? 79   ARG D CA  1 
ATOM   3926  C  C   . ARG D  1 79  ? 86.537  4.146   9.847  1.00 27.29  ? 79   ARG D C   1 
ATOM   3927  O  O   . ARG D  1 79  ? 87.034  4.333   8.730  1.00 22.73  ? 79   ARG D O   1 
ATOM   3928  C  CB  . ARG D  1 79  ? 84.703  2.508   10.140 1.00 19.51  ? 79   ARG D CB  1 
ATOM   3929  C  CG  . ARG D  1 79  ? 85.198  1.673   8.955  1.00 20.52  ? 79   ARG D CG  1 
ATOM   3930  C  CD  . ARG D  1 79  ? 84.999  0.167   9.198  1.00 19.99  ? 79   ARG D CD  1 
ATOM   3931  N  NE  . ARG D  1 79  ? 86.254  -0.433  9.724  1.00 20.55  ? 79   ARG D NE  1 
ATOM   3932  C  CZ  . ARG D  1 79  ? 86.459  -1.726  9.857  1.00 24.39  ? 79   ARG D CZ  1 
ATOM   3933  N  NH1 . ARG D  1 79  ? 87.632  -2.204  10.331 1.00 22.06  ? 79   ARG D NH1 1 
ATOM   3934  N  NH2 . ARG D  1 79  ? 85.541  -2.640  9.536  1.00 24.51  ? 79   ARG D NH2 1 
ATOM   3935  N  N   . HIS D  1 80  ? 87.212  4.025   10.982 1.00 20.80  ? 80   HIS D N   1 
ATOM   3936  C  CA  . HIS D  1 80  ? 88.667  3.863   10.986 1.00 26.10  ? 80   HIS D CA  1 
ATOM   3937  C  C   . HIS D  1 80  ? 89.028  2.457   10.530 1.00 27.09  ? 80   HIS D C   1 
ATOM   3938  O  O   . HIS D  1 80  ? 88.304  1.495   10.818 1.00 21.43  ? 80   HIS D O   1 
ATOM   3939  C  CB  . HIS D  1 80  ? 89.201  4.139   12.396 1.00 22.23  ? 80   HIS D CB  1 
ATOM   3940  C  CG  . HIS D  1 80  ? 88.951  5.512   12.942 1.00 22.82  ? 80   HIS D CG  1 
ATOM   3941  N  ND1 . HIS D  1 80  ? 88.698  5.734   14.279 1.00 23.08  ? 80   HIS D ND1 1 
ATOM   3942  C  CD2 . HIS D  1 80  ? 88.887  6.737   12.360 1.00 20.44  ? 80   HIS D CD2 1 
ATOM   3943  C  CE1 . HIS D  1 80  ? 88.514  7.025   14.498 1.00 19.35  ? 80   HIS D CE1 1 
ATOM   3944  N  NE2 . HIS D  1 80  ? 88.621  7.662   13.330 1.00 24.38  ? 80   HIS D NE2 1 
ATOM   3945  N  N   . VAL D  1 81  ? 90.156  2.265   9.827  1.00 23.52  ? 81   VAL D N   1 
ATOM   3946  C  CA  . VAL D  1 81  ? 90.556  0.882   9.540  1.00 20.58  ? 81   VAL D CA  1 
ATOM   3947  C  C   . VAL D  1 81  ? 90.670  0.071   10.829 1.00 16.59  ? 81   VAL D C   1 
ATOM   3948  O  O   . VAL D  1 81  ? 90.261  -1.088  10.871 1.00 19.66  ? 81   VAL D O   1 
ATOM   3949  C  CB  . VAL D  1 81  ? 91.885  0.827   8.758  1.00 31.33  ? 81   VAL D CB  1 
ATOM   3950  C  CG1 . VAL D  1 81  ? 92.493  -0.554  8.818  1.00 23.94  ? 81   VAL D CG1 1 
ATOM   3951  C  CG2 . VAL D  1 81  ? 91.644  1.227   7.289  1.00 27.17  ? 81   VAL D CG2 1 
ATOM   3952  N  N   . GLY D  1 82  ? 91.160  0.683   11.896 1.00 19.94  ? 82   GLY D N   1 
ATOM   3953  C  CA  . GLY D  1 82  ? 91.274  -0.152  13.093 1.00 20.39  ? 82   GLY D CA  1 
ATOM   3954  C  C   . GLY D  1 82  ? 89.985  -0.393  13.850 1.00 22.84  ? 82   GLY D C   1 
ATOM   3955  O  O   . GLY D  1 82  ? 90.003  -1.029  14.923 1.00 20.54  ? 82   GLY D O   1 
ATOM   3956  N  N   . ASP D  1 83  ? 88.820  0.037   13.404 1.00 19.54  ? 83   ASP D N   1 
ATOM   3957  C  CA  . ASP D  1 83  ? 87.624  -0.101  14.232 1.00 16.14  ? 83   ASP D CA  1 
ATOM   3958  C  C   . ASP D  1 83  ? 87.013  -1.489  14.168 1.00 21.82  ? 83   ASP D C   1 
ATOM   3959  O  O   . ASP D  1 83  ? 86.259  -1.794  13.237 1.00 25.16  ? 83   ASP D O   1 
ATOM   3960  C  CB  . ASP D  1 83  ? 86.558  0.913   13.771 1.00 20.47  ? 83   ASP D CB  1 
ATOM   3961  C  CG  . ASP D  1 83  ? 86.960  2.319   14.113 1.00 22.93  ? 83   ASP D CG  1 
ATOM   3962  O  OD1 . ASP D  1 83  ? 87.840  2.568   14.968 1.00 19.76  ? 83   ASP D OD1 1 
ATOM   3963  O  OD2 . ASP D  1 83  ? 86.395  3.271   13.532 1.00 25.96  ? 83   ASP D OD2 1 
ATOM   3964  N  N   . LEU D  1 84  ? 87.283  -2.296  15.180 1.00 20.41  ? 84   LEU D N   1 
ATOM   3965  C  CA  . LEU D  1 84  ? 86.715  -3.631  15.241 1.00 16.79  ? 84   LEU D CA  1 
ATOM   3966  C  C   . LEU D  1 84  ? 85.508  -3.723  16.164 1.00 20.22  ? 84   LEU D C   1 
ATOM   3967  O  O   . LEU D  1 84  ? 85.015  -4.836  16.346 1.00 22.03  ? 84   LEU D O   1 
ATOM   3968  C  CB  . LEU D  1 84  ? 87.785  -4.628  15.701 1.00 18.57  ? 84   LEU D CB  1 
ATOM   3969  C  CG  . LEU D  1 84  ? 88.992  -4.683  14.739 1.00 21.91  ? 84   LEU D CG  1 
ATOM   3970  C  CD1 . LEU D  1 84  ? 90.014  -5.632  15.329 1.00 21.11  ? 84   LEU D CD1 1 
ATOM   3971  C  CD2 . LEU D  1 84  ? 88.539  -5.101  13.348 1.00 19.20  ? 84   LEU D CD2 1 
ATOM   3972  N  N   . GLY D  1 85  ? 85.050  -2.599  16.689 1.00 21.04  ? 85   GLY D N   1 
ATOM   3973  C  CA  . GLY D  1 85  ? 83.783  -2.619  17.432 1.00 20.49  ? 85   GLY D CA  1 
ATOM   3974  C  C   . GLY D  1 85  ? 83.977  -3.003  18.889 1.00 21.24  ? 85   GLY D C   1 
ATOM   3975  O  O   . GLY D  1 85  ? 84.864  -2.469  19.550 1.00 22.62  ? 85   GLY D O   1 
ATOM   3976  N  N   . ASN D  1 86  ? 83.139  -3.910  19.367 1.00 20.72  ? 86   ASN D N   1 
ATOM   3977  C  CA  . ASN D  1 86  ? 83.213  -4.388  20.752 1.00 19.28  ? 86   ASN D CA  1 
ATOM   3978  C  C   . ASN D  1 86  ? 83.501  -5.879  20.841 1.00 20.22  ? 86   ASN D C   1 
ATOM   3979  O  O   . ASN D  1 86  ? 83.210  -6.675  19.944 1.00 20.52  ? 86   ASN D O   1 
ATOM   3980  C  CB  . ASN D  1 86  ? 81.891  -4.144  21.492 1.00 17.04  ? 86   ASN D CB  1 
ATOM   3981  C  CG  . ASN D  1 86  ? 81.673  -2.676  21.760 1.00 20.48  ? 86   ASN D CG  1 
ATOM   3982  O  OD1 . ASN D  1 86  ? 82.376  -2.028  22.549 1.00 21.46  ? 86   ASN D OD1 1 
ATOM   3983  N  ND2 . ASN D  1 86  ? 80.690  -2.087  21.087 1.00 22.09  ? 86   ASN D ND2 1 
ATOM   3984  N  N   . VAL D  1 87  ? 84.056  -6.253  21.999 1.00 18.45  ? 87   VAL D N   1 
ATOM   3985  C  CA  . VAL D  1 87  ? 84.089  -7.657  22.400 1.00 17.07  ? 87   VAL D CA  1 
ATOM   3986  C  C   . VAL D  1 87  ? 83.246  -7.780  23.675 1.00 20.03  ? 87   VAL D C   1 
ATOM   3987  O  O   . VAL D  1 87  ? 83.144  -6.761  24.370 1.00 21.43  ? 87   VAL D O   1 
ATOM   3988  C  CB  . VAL D  1 87  ? 85.524  -8.172  22.603 1.00 19.48  ? 87   VAL D CB  1 
ATOM   3989  C  CG1 . VAL D  1 87  ? 86.269  -8.095  21.276 1.00 21.03  ? 87   VAL D CG1 1 
ATOM   3990  C  CG2 . VAL D  1 87  ? 86.244  -7.391  23.691 1.00 18.87  ? 87   VAL D CG2 1 
ATOM   3991  N  N   . THR D  1 88  ? 82.643  -8.931  23.942 1.00 16.23  ? 88   THR D N   1 
ATOM   3992  C  CA  . THR D  1 88  ? 81.769  -9.043  25.117 1.00 17.30  ? 88   THR D CA  1 
ATOM   3993  C  C   . THR D  1 88  ? 82.351  -9.969  26.168 1.00 19.25  ? 88   THR D C   1 
ATOM   3994  O  O   . THR D  1 88  ? 82.678  -11.112 25.828 1.00 20.74  ? 88   THR D O   1 
ATOM   3995  C  CB  . THR D  1 88  ? 80.412  -9.637  24.691 1.00 26.48  ? 88   THR D CB  1 
ATOM   3996  O  OG1 . THR D  1 88  ? 79.768  -8.692  23.826 1.00 25.34  ? 88   THR D OG1 1 
ATOM   3997  C  CG2 . THR D  1 88  ? 79.519  -9.851  25.912 1.00 21.82  ? 88   THR D CG2 1 
ATOM   3998  N  N   . ALA D  1 89  ? 82.470  -9.514  27.416 1.00 19.88  ? 89   ALA D N   1 
ATOM   3999  C  CA  . ALA D  1 89  ? 82.934  -10.387 28.489 1.00 20.57  ? 89   ALA D CA  1 
ATOM   4000  C  C   . ALA D  1 89  ? 81.736  -11.043 29.189 1.00 24.46  ? 89   ALA D C   1 
ATOM   4001  O  O   . ALA D  1 89  ? 80.744  -10.339 29.372 1.00 25.16  ? 89   ALA D O   1 
ATOM   4002  C  CB  . ALA D  1 89  ? 83.713  -9.603  29.528 1.00 21.46  ? 89   ALA D CB  1 
ATOM   4003  N  N   . ASP D  1 90  ? 81.876  -12.300 29.560 1.00 24.44  ? 90   ASP D N   1 
ATOM   4004  C  CA  . ASP D  1 90  ? 80.808  -13.029 30.245 1.00 28.54  ? 90   ASP D CA  1 
ATOM   4005  C  C   . ASP D  1 90  ? 80.835  -12.734 31.743 1.00 24.63  ? 90   ASP D C   1 
ATOM   4006  O  O   . ASP D  1 90  ? 81.622  -11.919 32.225 1.00 23.32  ? 90   ASP D O   1 
ATOM   4007  C  CB  . ASP D  1 90  ? 80.920  -14.514 29.907 1.00 23.62  ? 90   ASP D CB  1 
ATOM   4008  C  CG  . ASP D  1 90  ? 82.136  -15.228 30.462 1.00 24.70  ? 90   ASP D CG  1 
ATOM   4009  O  OD1 . ASP D  1 90  ? 82.433  -16.350 29.983 1.00 28.28  ? 90   ASP D OD1 1 
ATOM   4010  O  OD2 . ASP D  1 90  ? 82.801  -14.678 31.379 1.00 28.43  ? 90   ASP D OD2 1 
ATOM   4011  N  N   . LYS D  1 91  ? 79.960  -13.399 32.500 1.00 23.68  ? 91   LYS D N   1 
ATOM   4012  C  CA  . LYS D  1 91  ? 79.836  -13.013 33.906 1.00 29.20  ? 91   LYS D CA  1 
ATOM   4013  C  C   . LYS D  1 91  ? 81.071  -13.399 34.706 1.00 29.27  ? 91   LYS D C   1 
ATOM   4014  O  O   . LYS D  1 91  ? 81.239  -12.873 35.802 1.00 31.54  ? 91   LYS D O   1 
ATOM   4015  C  CB  . LYS D  1 91  ? 78.588  -13.665 34.525 1.00 32.24  ? 91   LYS D CB  1 
ATOM   4016  C  CG  . LYS D  1 91  ? 78.757  -15.173 34.672 1.00 40.57  ? 91   LYS D CG  1 
ATOM   4017  C  CD  . LYS D  1 91  ? 77.449  -15.889 34.960 1.00 49.70  ? 91   LYS D CD  1 
ATOM   4018  C  CE  . LYS D  1 91  ? 77.678  -17.367 35.246 1.00 61.45  ? 91   LYS D CE  1 
ATOM   4019  N  NZ  . LYS D  1 91  ? 77.496  -18.225 34.044 1.00 70.48  ? 91   LYS D NZ  1 
ATOM   4020  N  N   . ASP D  1 92  ? 81.909  -14.275 34.176 1.00 25.52  ? 92   ASP D N   1 
ATOM   4021  C  CA  . ASP D  1 92  ? 83.205  -14.607 34.727 1.00 29.39  ? 92   ASP D CA  1 
ATOM   4022  C  C   . ASP D  1 92  ? 84.308  -13.631 34.329 1.00 34.33  ? 92   ASP D C   1 
ATOM   4023  O  O   . ASP D  1 92  ? 85.448  -13.771 34.798 1.00 31.41  ? 92   ASP D O   1 
ATOM   4024  C  CB  . ASP D  1 92  ? 83.621  -16.033 34.275 1.00 27.58  ? 92   ASP D CB  1 
ATOM   4025  C  CG  . ASP D  1 92  ? 82.700  -17.081 34.863 1.00 36.02  ? 92   ASP D CG  1 
ATOM   4026  O  OD1 . ASP D  1 92  ? 82.367  -18.073 34.186 1.00 46.32  ? 92   ASP D OD1 1 
ATOM   4027  O  OD2 . ASP D  1 92  ? 82.300  -16.895 36.033 1.00 47.84  ? 92   ASP D OD2 1 
ATOM   4028  N  N   . GLY D  1 93  ? 84.042  -12.642 33.490 1.00 24.41  ? 93   GLY D N   1 
ATOM   4029  C  CA  . GLY D  1 93  ? 85.029  -11.660 33.068 1.00 21.94  ? 93   GLY D CA  1 
ATOM   4030  C  C   . GLY D  1 93  ? 85.778  -12.116 31.828 1.00 22.81  ? 93   GLY D C   1 
ATOM   4031  O  O   . GLY D  1 93  ? 86.801  -11.520 31.484 1.00 22.34  ? 93   GLY D O   1 
ATOM   4032  N  N   . VAL D  1 94  ? 85.323  -13.160 31.162 1.00 20.38  ? 94   VAL D N   1 
ATOM   4033  C  CA  . VAL D  1 94  ? 86.013  -13.735 30.016 1.00 25.66  ? 94   VAL D CA  1 
ATOM   4034  C  C   . VAL D  1 94  ? 85.354  -13.346 28.690 1.00 24.71  ? 94   VAL D C   1 
ATOM   4035  O  O   . VAL D  1 94  ? 84.159  -13.584 28.499 1.00 22.72  ? 94   VAL D O   1 
ATOM   4036  C  CB  . VAL D  1 94  ? 86.069  -15.275 30.103 1.00 34.09  ? 94   VAL D CB  1 
ATOM   4037  C  CG1 . VAL D  1 94  ? 86.618  -15.882 28.820 1.00 28.53  ? 94   VAL D CG1 1 
ATOM   4038  C  CG2 . VAL D  1 94  ? 86.923  -15.707 31.293 1.00 32.11  ? 94   VAL D CG2 1 
ATOM   4039  N  N   . ALA D  1 95  ? 86.160  -12.761 27.792 1.00 23.17  ? 95   ALA D N   1 
ATOM   4040  C  CA  . ALA D  1 95  ? 85.738  -12.500 26.427 1.00 20.57  ? 95   ALA D CA  1 
ATOM   4041  C  C   . ALA D  1 95  ? 86.306  -13.550 25.480 1.00 29.81  ? 95   ALA D C   1 
ATOM   4042  O  O   . ALA D  1 95  ? 87.509  -13.547 25.195 1.00 24.99  ? 95   ALA D O   1 
ATOM   4043  C  CB  . ALA D  1 95  ? 86.174  -11.127 25.959 1.00 18.27  ? 95   ALA D CB  1 
ATOM   4044  N  N   . ASP D  1 96  ? 85.432  -14.429 25.003 1.00 21.66  ? 96   ASP D N   1 
ATOM   4045  C  CA  . ASP D  1 96  ? 85.818  -15.344 23.932 1.00 23.64  ? 96   ASP D CA  1 
ATOM   4046  C  C   . ASP D  1 96  ? 85.601  -14.670 22.578 1.00 25.49  ? 96   ASP D C   1 
ATOM   4047  O  O   . ASP D  1 96  ? 84.536  -14.695 21.967 1.00 26.06  ? 96   ASP D O   1 
ATOM   4048  C  CB  . ASP D  1 96  ? 85.027  -16.654 24.002 1.00 24.85  ? 96   ASP D CB  1 
ATOM   4049  C  CG  . ASP D  1 96  ? 85.415  -17.380 25.291 1.00 34.10  ? 96   ASP D CG  1 
ATOM   4050  O  OD1 . ASP D  1 96  ? 84.486  -17.720 26.050 1.00 39.40  ? 96   ASP D OD1 1 
ATOM   4051  O  OD2 . ASP D  1 96  ? 86.623  -17.589 25.538 1.00 33.53  ? 96   ASP D OD2 1 
ATOM   4052  N  N   . VAL D  1 97  ? 86.654  -14.041 22.107 1.00 21.22  ? 97   VAL D N   1 
ATOM   4053  C  CA  . VAL D  1 97  ? 86.530  -13.152 20.952 1.00 20.83  ? 97   VAL D CA  1 
ATOM   4054  C  C   . VAL D  1 97  ? 86.372  -13.953 19.672 1.00 23.84  ? 97   VAL D C   1 
ATOM   4055  O  O   . VAL D  1 97  ? 87.095  -14.928 19.455 1.00 24.69  ? 97   VAL D O   1 
ATOM   4056  C  CB  . VAL D  1 97  ? 87.782  -12.259 20.871 1.00 21.76  ? 97   VAL D CB  1 
ATOM   4057  C  CG1 . VAL D  1 97  ? 87.741  -11.371 19.633 1.00 25.20  ? 97   VAL D CG1 1 
ATOM   4058  C  CG2 . VAL D  1 97  ? 87.910  -11.422 22.131 1.00 22.04  ? 97   VAL D CG2 1 
ATOM   4059  N  N   . SER D  1 98  ? 85.450  -13.491 18.836 1.00 24.15  ? 98   SER D N   1 
ATOM   4060  C  CA  . SER D  1 98  ? 85.264  -14.102 17.538 1.00 25.61  ? 98   SER D CA  1 
ATOM   4061  C  C   . SER D  1 98  ? 84.740  -13.082 16.549 1.00 27.61  ? 98   SER D C   1 
ATOM   4062  O  O   . SER D  1 98  ? 83.543  -12.804 16.538 1.00 27.75  ? 98   SER D O   1 
ATOM   4063  C  CB  . SER D  1 98  ? 84.269  -15.271 17.639 1.00 34.50  ? 98   SER D CB  1 
ATOM   4064  O  OG  . SER D  1 98  ? 84.238  -15.975 16.411 1.00 43.22  ? 98   SER D OG  1 
ATOM   4065  N  N   . ILE D  1 99  ? 85.622  -12.513 15.742 1.00 20.12  ? 99   ILE D N   1 
ATOM   4066  C  CA  . ILE D  1 99  ? 85.273  -11.417 14.844 1.00 21.64  ? 99   ILE D CA  1 
ATOM   4067  C  C   . ILE D  1 99  ? 85.763  -11.769 13.446 1.00 27.48  ? 99   ILE D C   1 
ATOM   4068  O  O   . ILE D  1 99  ? 86.785  -12.433 13.293 1.00 24.49  ? 99   ILE D O   1 
ATOM   4069  C  CB  . ILE D  1 99  ? 85.909  -10.113 15.336 1.00 23.45  ? 99   ILE D CB  1 
ATOM   4070  C  CG1 . ILE D  1 99  ? 85.165  -9.561  16.581 1.00 21.60  ? 99   ILE D CG1 1 
ATOM   4071  C  CG2 . ILE D  1 99  ? 86.000  -9.027  14.278 1.00 27.48  ? 99   ILE D CG2 1 
ATOM   4072  C  CD1 . ILE D  1 99  ? 85.901  -8.417  17.249 1.00 22.02  ? 99   ILE D CD1 1 
ATOM   4073  N  N   . GLU D  1 100 ? 85.038  -11.320 12.426 1.00 25.28  ? 100  GLU D N   1 
ATOM   4074  C  CA  . GLU D  1 100 ? 85.568  -11.477 11.074 1.00 24.03  ? 100  GLU D CA  1 
ATOM   4075  C  C   . GLU D  1 100 ? 85.515  -10.112 10.416 1.00 21.32  ? 100  GLU D C   1 
ATOM   4076  O  O   . GLU D  1 100 ? 84.475  -9.440  10.499 1.00 25.04  ? 100  GLU D O   1 
ATOM   4077  C  CB  . GLU D  1 100 ? 84.769  -12.504 10.263 1.00 29.64  ? 100  GLU D CB  1 
ATOM   4078  C  CG  . GLU D  1 100 ? 85.427  -12.707 8.891  1.00 44.19  ? 100  GLU D CG  1 
ATOM   4079  C  CD  . GLU D  1 100 ? 84.828  -13.900 8.155  1.00 60.15  ? 100  GLU D CD  1 
ATOM   4080  O  OE1 . GLU D  1 100 ? 84.736  -14.987 8.763  1.00 51.39  ? 100  GLU D OE1 1 
ATOM   4081  O  OE2 . GLU D  1 100 ? 84.442  -13.751 6.975  1.00 77.77  ? 100  GLU D OE2 1 
ATOM   4082  N  N   . ASP D  1 101 ? 86.618  -9.647  9.830  1.00 23.81  ? 101  ASP D N   1 
ATOM   4083  C  CA  . ASP D  1 101 ? 86.610  -8.272  9.326  1.00 25.34  ? 101  ASP D CA  1 
ATOM   4084  C  C   . ASP D  1 101 ? 87.305  -8.196  7.967  1.00 30.13  ? 101  ASP D C   1 
ATOM   4085  O  O   . ASP D  1 101 ? 88.378  -8.763  7.779  1.00 26.16  ? 101  ASP D O   1 
ATOM   4086  C  CB  . ASP D  1 101 ? 87.311  -7.292  10.279 1.00 20.26  ? 101  ASP D CB  1 
ATOM   4087  C  CG  . ASP D  1 101 ? 87.084  -5.844  9.906  1.00 27.62  ? 101  ASP D CG  1 
ATOM   4088  O  OD1 . ASP D  1 101 ? 87.980  -5.193  9.307  1.00 24.23  ? 101  ASP D OD1 1 
ATOM   4089  O  OD2 . ASP D  1 101 ? 85.985  -5.311  10.200 1.00 28.56  ? 101  ASP D OD2 1 
ATOM   4090  N  N   . SER D  1 102 ? 86.674  -7.470  7.051  1.00 24.10  ? 102  SER D N   1 
ATOM   4091  C  CA  . SER D  1 102 ? 87.299  -7.342  5.742  1.00 28.31  ? 102  SER D CA  1 
ATOM   4092  C  C   . SER D  1 102 ? 87.964  -6.009  5.482  1.00 29.98  ? 102  SER D C   1 
ATOM   4093  O  O   . SER D  1 102 ? 88.342  -5.808  4.316  1.00 31.03  ? 102  SER D O   1 
ATOM   4094  C  CB  . SER D  1 102 ? 86.202  -7.575  4.676  1.00 35.43  ? 102  SER D CB  1 
ATOM   4095  O  OG  . SER D  1 102 ? 86.165  -8.974  4.435  1.00 41.54  ? 102  SER D OG  1 
ATOM   4096  N  N   . VAL D  1 103 ? 88.134  -5.129  6.466  1.00 23.57  ? 103  VAL D N   1 
ATOM   4097  C  CA  . VAL D  1 103 ? 88.737  -3.821  6.239  1.00 19.50  ? 103  VAL D CA  1 
ATOM   4098  C  C   . VAL D  1 103 ? 90.176  -3.878  6.759  1.00 27.74  ? 103  VAL D C   1 
ATOM   4099  O  O   . VAL D  1 103 ? 91.116  -3.381  6.142  1.00 25.22  ? 103  VAL D O   1 
ATOM   4100  C  CB  . VAL D  1 103 ? 87.990  -2.677  6.923  1.00 22.54  ? 103  VAL D CB  1 
ATOM   4101  C  CG1 . VAL D  1 103 ? 88.705  -1.325  6.802  1.00 19.17  ? 103  VAL D CG1 1 
ATOM   4102  C  CG2 . VAL D  1 103 ? 86.588  -2.569  6.312  1.00 31.14  ? 103  VAL D CG2 1 
ATOM   4103  N  N   . ILE D  1 104 ? 90.364  -4.507  7.921  1.00 22.82  ? 104  ILE D N   1 
ATOM   4104  C  CA  . ILE D  1 104 ? 91.744  -4.801  8.289  1.00 23.99  ? 104  ILE D CA  1 
ATOM   4105  C  C   . ILE D  1 104 ? 92.376  -5.813  7.348  1.00 23.57  ? 104  ILE D C   1 
ATOM   4106  O  O   . ILE D  1 104 ? 91.728  -6.599  6.674  1.00 24.01  ? 104  ILE D O   1 
ATOM   4107  C  CB  . ILE D  1 104 ? 91.881  -5.378  9.720  1.00 18.05  ? 104  ILE D CB  1 
ATOM   4108  C  CG1 . ILE D  1 104 ? 91.075  -6.654  9.963  1.00 20.57  ? 104  ILE D CG1 1 
ATOM   4109  C  CG2 . ILE D  1 104 ? 91.555  -4.239  10.703 1.00 20.08  ? 104  ILE D CG2 1 
ATOM   4110  C  CD1 . ILE D  1 104 ? 91.482  -7.336  11.269 1.00 21.28  ? 104  ILE D CD1 1 
ATOM   4111  N  N   . SER D  1 105 ? 93.710  -5.793  7.324  1.00 21.29  ? 105  SER D N   1 
ATOM   4112  C  CA  . SER D  1 105 ? 94.435  -6.777  6.548  1.00 21.43  ? 105  SER D CA  1 
ATOM   4113  C  C   . SER D  1 105 ? 95.781  -7.147  7.184  1.00 21.96  ? 105  SER D C   1 
ATOM   4114  O  O   . SER D  1 105 ? 96.251  -6.370  8.015  1.00 22.68  ? 105  SER D O   1 
ATOM   4115  C  CB  . SER D  1 105 ? 94.689  -6.201  5.139  1.00 26.80  ? 105  SER D CB  1 
ATOM   4116  O  OG  . SER D  1 105 ? 95.205  -7.248  4.328  1.00 26.30  ? 105  SER D OG  1 
ATOM   4117  N  N   . LEU D  1 106 ? 96.349  -8.278  6.772  1.00 21.34  ? 106  LEU D N   1 
ATOM   4118  C  CA  . LEU D  1 106 ? 97.709  -8.609  7.223  1.00 22.93  ? 106  LEU D CA  1 
ATOM   4119  C  C   . LEU D  1 106 ? 98.749  -8.278  6.149  1.00 33.50  ? 106  LEU D C   1 
ATOM   4120  O  O   . LEU D  1 106 ? 99.911  -8.654  6.316  1.00 33.83  ? 106  LEU D O   1 
ATOM   4121  C  CB  . LEU D  1 106 ? 97.833  -10.072 7.624  1.00 23.82  ? 106  LEU D CB  1 
ATOM   4122  C  CG  . LEU D  1 106 ? 96.860  -10.559 8.706  1.00 23.65  ? 106  LEU D CG  1 
ATOM   4123  C  CD1 . LEU D  1 106 ? 97.138  -11.981 9.132  1.00 28.30  ? 106  LEU D CD1 1 
ATOM   4124  C  CD2 . LEU D  1 106 ? 96.938  -9.622  9.906  1.00 29.62  ? 106  LEU D CD2 1 
ATOM   4125  N  N   . SER D  1 107 ? 98.347  -7.584  5.094  1.00 32.50  ? 107  SER D N   1 
ATOM   4126  C  CA  . SER D  1 107 ? 99.278  -7.080  4.088  1.00 33.88  ? 107  SER D CA  1 
ATOM   4127  C  C   . SER D  1 107 ? 98.812  -5.756  3.512  1.00 41.87  ? 107  SER D C   1 
ATOM   4128  O  O   . SER D  1 107 ? 97.634  -5.418  3.663  1.00 32.65  ? 107  SER D O   1 
ATOM   4129  C  CB  . SER D  1 107 ? 99.412  -8.087  2.942  1.00 30.15  ? 107  SER D CB  1 
ATOM   4130  O  OG  . SER D  1 107 ? 98.163  -8.676  2.637  1.00 61.50  ? 107  SER D OG  1 
ATOM   4131  N  N   . GLY D  1 108 ? 99.692  -5.007  2.842  1.00 33.58  ? 108  GLY D N   1 
ATOM   4132  C  CA  . GLY D  1 108 ? 99.220  -3.836  2.114  1.00 36.24  ? 108  GLY D CA  1 
ATOM   4133  C  C   . GLY D  1 108 ? 99.026  -2.601  2.957  1.00 42.43  ? 108  GLY D C   1 
ATOM   4134  O  O   . GLY D  1 108 ? 99.454  -2.509  4.111  1.00 35.11  ? 108  GLY D O   1 
ATOM   4135  N  N   . ASP D  1 109 ? 98.358  -1.597  2.396  1.00 29.12  ? 109  ASP D N   1 
ATOM   4136  C  CA  . ASP D  1 109 ? 98.121  -0.365  3.128  1.00 31.81  ? 109  ASP D CA  1 
ATOM   4137  C  C   . ASP D  1 109 ? 97.210  -0.525  4.345  1.00 28.40  ? 109  ASP D C   1 
ATOM   4138  O  O   . ASP D  1 109 ? 97.250  0.340   5.204  1.00 31.01  ? 109  ASP D O   1 
ATOM   4139  C  CB  . ASP D  1 109 ? 97.428  0.649   2.210  1.00 44.15  ? 109  ASP D CB  1 
ATOM   4140  C  CG  . ASP D  1 109 ? 98.375  1.179   1.153  1.00 50.41  ? 109  ASP D CG  1 
ATOM   4141  O  OD1 . ASP D  1 109 ? 97.908  2.016   0.355  1.00 50.99  ? 109  ASP D OD1 1 
ATOM   4142  O  OD2 . ASP D  1 109 ? 99.542  0.743   1.140  1.00 63.39  ? 109  ASP D OD2 1 
ATOM   4143  N  N   . HIS D  1 110 ? 96.386  -1.567  4.412  1.00 33.18  ? 110  HIS D N   1 
ATOM   4144  C  CA  . HIS D  1 110 ? 95.527  -1.721  5.586  1.00 34.15  ? 110  HIS D CA  1 
ATOM   4145  C  C   . HIS D  1 110 ? 96.153  -2.665  6.602  1.00 34.86  ? 110  HIS D C   1 
ATOM   4146  O  O   . HIS D  1 110 ? 95.502  -3.149  7.530  1.00 25.32  ? 110  HIS D O   1 
ATOM   4147  C  CB  . HIS D  1 110 ? 94.154  -2.269  5.173  1.00 33.10  ? 110  HIS D CB  1 
ATOM   4148  C  CG  . HIS D  1 110 ? 93.374  -1.168  4.515  1.00 34.41  ? 110  HIS D CG  1 
ATOM   4149  N  ND1 . HIS D  1 110 ? 92.031  -1.247  4.231  1.00 48.54  ? 110  HIS D ND1 1 
ATOM   4150  C  CD2 . HIS D  1 110 ? 93.777  0.055   4.103  1.00 38.15  ? 110  HIS D CD2 1 
ATOM   4151  C  CE1 . HIS D  1 110 ? 91.632  -0.116  3.659  1.00 50.03  ? 110  HIS D CE1 1 
ATOM   4152  N  NE2 . HIS D  1 110 ? 92.679  0.688   3.572  1.00 49.64  ? 110  HIS D NE2 1 
ATOM   4153  N  N   . CYS D  1 111 ? 97.444  -2.916  6.404  1.00 27.40  ? 111  CYS D N   1 
ATOM   4154  C  CA  . CYS D  1 111 ? 98.149  -3.857  7.250  1.00 24.68  ? 111  CYS D CA  1 
ATOM   4155  C  C   . CYS D  1 111 ? 98.200  -3.412  8.713  1.00 21.79  ? 111  CYS D C   1 
ATOM   4156  O  O   . CYS D  1 111 ? 98.523  -2.265  8.994  1.00 23.90  ? 111  CYS D O   1 
ATOM   4157  C  CB  . CYS D  1 111 ? 99.610  -4.033  6.762  1.00 26.64  ? 111  CYS D CB  1 
ATOM   4158  S  SG  . CYS D  1 111 ? 100.299 -5.529  7.508  1.00 39.42  ? 111  CYS D SG  1 
ATOM   4159  N  N   . ILE D  1 112 ? 97.872  -4.331  9.620  1.00 24.78  ? 112  ILE D N   1 
ATOM   4160  C  CA  . ILE D  1 112 ? 97.854  -4.042  11.054 1.00 21.90  ? 112  ILE D CA  1 
ATOM   4161  C  C   . ILE D  1 112 ? 99.046  -4.662  11.786 1.00 24.52  ? 112  ILE D C   1 
ATOM   4162  O  O   . ILE D  1 112 ? 99.241  -4.504  12.993 1.00 20.77  ? 112  ILE D O   1 
ATOM   4163  C  CB  . ILE D  1 112 ? 96.543  -4.574  11.671 1.00 23.22  ? 112  ILE D CB  1 
ATOM   4164  C  CG1 . ILE D  1 112 ? 96.341  -6.072  11.437 1.00 24.74  ? 112  ILE D CG1 1 
ATOM   4165  C  CG2 . ILE D  1 112 ? 95.351  -3.760  11.167 1.00 22.07  ? 112  ILE D CG2 1 
ATOM   4166  C  CD1 . ILE D  1 112 ? 95.262  -6.682  12.322 1.00 22.60  ? 112  ILE D CD1 1 
ATOM   4167  N  N   . ILE D  1 113 ? 99.876  -5.363  11.012 1.00 20.65  ? 113  ILE D N   1 
ATOM   4168  C  CA  . ILE D  1 113 ? 101.073 -5.934  11.648 1.00 23.41  ? 113  ILE D CA  1 
ATOM   4169  C  C   . ILE D  1 113 ? 101.986 -4.809  12.087 1.00 25.30  ? 113  ILE D C   1 
ATOM   4170  O  O   . ILE D  1 113 ? 102.206 -3.816  11.410 1.00 25.26  ? 113  ILE D O   1 
ATOM   4171  C  CB  . ILE D  1 113 ? 101.715 -6.972  10.717 1.00 23.27  ? 113  ILE D CB  1 
ATOM   4172  C  CG1 . ILE D  1 113 ? 100.902 -8.291  10.727 1.00 26.00  ? 113  ILE D CG1 1 
ATOM   4173  C  CG2 . ILE D  1 113 ? 103.170 -7.208  11.087 1.00 30.32  ? 113  ILE D CG2 1 
ATOM   4174  C  CD1 . ILE D  1 113 ? 101.306 -9.297  9.681  1.00 35.38  ? 113  ILE D CD1 1 
ATOM   4175  N  N   . GLY D  1 114 ? 102.546 -4.922  13.308 1.00 25.53  ? 114  GLY D N   1 
ATOM   4176  C  CA  . GLY D  1 114 ? 103.392 -3.845  13.788 1.00 22.33  ? 114  GLY D CA  1 
ATOM   4177  C  C   . GLY D  1 114 ? 102.642 -2.736  14.484 1.00 28.70  ? 114  GLY D C   1 
ATOM   4178  O  O   . GLY D  1 114 ? 103.210 -1.757  14.963 1.00 22.86  ? 114  GLY D O   1 
ATOM   4179  N  N   . ARG D  1 115 ? 101.299 -2.854  14.558 1.00 22.92  ? 115  ARG D N   1 
ATOM   4180  C  CA  . ARG D  1 115 ? 100.522 -1.844  15.266 1.00 19.91  ? 115  ARG D CA  1 
ATOM   4181  C  C   . ARG D  1 115 ? 99.961  -2.457  16.545 1.00 20.34  ? 115  ARG D C   1 
ATOM   4182  O  O   . ARG D  1 115 ? 100.304 -3.585  16.903 1.00 23.31  ? 115  ARG D O   1 
ATOM   4183  C  CB  . ARG D  1 115 ? 99.416  -1.312  14.349 1.00 25.64  ? 115  ARG D CB  1 
ATOM   4184  C  CG  . ARG D  1 115 ? 100.030 -0.905  13.005 1.00 28.09  ? 115  ARG D CG  1 
ATOM   4185  C  CD  . ARG D  1 115 ? 99.035  -0.247  12.077 1.00 31.52  ? 115  ARG D CD  1 
ATOM   4186  N  NE  . ARG D  1 115 ? 99.659  0.142   10.815 1.00 30.75  ? 115  ARG D NE  1 
ATOM   4187  C  CZ  . ARG D  1 115 ? 100.287 1.277   10.543 1.00 29.92  ? 115  ARG D CZ  1 
ATOM   4188  N  NH1 . ARG D  1 115 ? 100.780 1.417   9.302  1.00 28.77  ? 115  ARG D NH1 1 
ATOM   4189  N  NH2 . ARG D  1 115 ? 100.440 2.264   11.410 1.00 25.48  ? 115  ARG D NH2 1 
ATOM   4190  N  N   . THR D  1 116 ? 99.127  -1.728  17.257 1.00 21.23  ? 116  THR D N   1 
ATOM   4191  C  CA  . THR D  1 116 ? 98.753  -2.194  18.595 1.00 21.68  ? 116  THR D CA  1 
ATOM   4192  C  C   . THR D  1 116 ? 97.255  -2.495  18.728 1.00 23.09  ? 116  THR D C   1 
ATOM   4193  O  O   . THR D  1 116 ? 96.478  -1.626  18.352 1.00 22.33  ? 116  THR D O   1 
ATOM   4194  C  CB  . THR D  1 116 ? 99.119  -1.115  19.629 1.00 26.35  ? 116  THR D CB  1 
ATOM   4195  O  OG1 . THR D  1 116 ? 100.553 -0.971  19.651 1.00 24.02  ? 116  THR D OG1 1 
ATOM   4196  C  CG2 . THR D  1 116 ? 98.662  -1.515  21.023 1.00 26.93  ? 116  THR D CG2 1 
ATOM   4197  N  N   . LEU D  1 117 ? 96.957  -3.666  19.261 1.00 20.35  ? 117  LEU D N   1 
ATOM   4198  C  CA  . LEU D  1 117 ? 95.564  -4.017  19.573 1.00 17.97  ? 117  LEU D CA  1 
ATOM   4199  C  C   . LEU D  1 117 ? 95.262  -3.527  20.978 1.00 22.03  ? 117  LEU D C   1 
ATOM   4200  O  O   . LEU D  1 117 ? 96.075  -3.774  21.878 1.00 20.88  ? 117  LEU D O   1 
ATOM   4201  C  CB  . LEU D  1 117 ? 95.380  -5.527  19.468 1.00 19.47  ? 117  LEU D CB  1 
ATOM   4202  C  CG  . LEU D  1 117 ? 93.932  -6.042  19.609 1.00 22.24  ? 117  LEU D CG  1 
ATOM   4203  C  CD1 . LEU D  1 117 ? 93.060  -5.511  18.484 1.00 19.12  ? 117  LEU D CD1 1 
ATOM   4204  C  CD2 . LEU D  1 117 ? 93.938  -7.569  19.651 1.00 18.77  ? 117  LEU D CD2 1 
ATOM   4205  N  N   . VAL D  1 118 ? 94.145  -2.842  21.184 1.00 18.61  ? 118  VAL D N   1 
ATOM   4206  C  CA  . VAL D  1 118 ? 93.797  -2.312  22.499 1.00 19.50  ? 118  VAL D CA  1 
ATOM   4207  C  C   . VAL D  1 118 ? 92.408  -2.773  22.936 1.00 22.34  ? 118  VAL D C   1 
ATOM   4208  O  O   . VAL D  1 118 ? 91.511  -2.735  22.090 1.00 20.79  ? 118  VAL D O   1 
ATOM   4209  C  CB  . VAL D  1 118 ? 93.811  -0.772  22.490 1.00 19.02  ? 118  VAL D CB  1 
ATOM   4210  C  CG1 . VAL D  1 118 ? 93.338  -0.216  23.834 1.00 20.81  ? 118  VAL D CG1 1 
ATOM   4211  C  CG2 . VAL D  1 118 ? 95.193  -0.256  22.136 1.00 22.15  ? 118  VAL D CG2 1 
ATOM   4212  N  N   . VAL D  1 119 ? 92.209  -3.195  24.177 1.00 17.36  ? 119  VAL D N   1 
ATOM   4213  C  CA  . VAL D  1 119 ? 90.842  -3.461  24.673 1.00 17.10  ? 119  VAL D CA  1 
ATOM   4214  C  C   . VAL D  1 119 ? 90.556  -2.404  25.740 1.00 23.90  ? 119  VAL D C   1 
ATOM   4215  O  O   . VAL D  1 119 ? 91.439  -2.001  26.523 1.00 20.40  ? 119  VAL D O   1 
ATOM   4216  C  CB  . VAL D  1 119 ? 90.630  -4.893  25.136 1.00 20.15  ? 119  VAL D CB  1 
ATOM   4217  C  CG1 . VAL D  1 119 ? 91.573  -5.325  26.260 1.00 21.78  ? 119  VAL D CG1 1 
ATOM   4218  C  CG2 . VAL D  1 119 ? 89.165  -5.107  25.584 1.00 18.89  ? 119  VAL D CG2 1 
ATOM   4219  N  N   . HIS D  1 120 ? 89.328  -1.869  25.736 1.00 18.97  ? 120  HIS D N   1 
ATOM   4220  C  CA  . HIS D  1 120 ? 89.013  -0.669  26.492 1.00 18.52  ? 120  HIS D CA  1 
ATOM   4221  C  C   . HIS D  1 120 ? 88.139  -0.879  27.720 1.00 21.83  ? 120  HIS D C   1 
ATOM   4222  O  O   . HIS D  1 120 ? 87.520  -1.920  27.919 1.00 20.64  ? 120  HIS D O   1 
ATOM   4223  C  CB  . HIS D  1 120 ? 88.268  0.338   25.590 1.00 18.51  ? 120  HIS D CB  1 
ATOM   4224  C  CG  . HIS D  1 120 ? 89.208  0.995   24.619 1.00 19.75  ? 120  HIS D CG  1 
ATOM   4225  N  ND1 . HIS D  1 120 ? 89.800  2.217   24.871 1.00 18.41  ? 120  HIS D ND1 1 
ATOM   4226  C  CD2 . HIS D  1 120 ? 89.636  0.609   23.394 1.00 19.35  ? 120  HIS D CD2 1 
ATOM   4227  C  CE1 . HIS D  1 120 ? 90.563  2.550   23.841 1.00 21.35  ? 120  HIS D CE1 1 
ATOM   4228  N  NE2 . HIS D  1 120 ? 90.486  1.592   22.938 1.00 19.94  ? 120  HIS D NE2 1 
ATOM   4229  N  N   . GLU D  1 121 ? 88.093  0.180   28.522 1.00 20.76  ? 121  GLU D N   1 
ATOM   4230  C  CA  . GLU D  1 121 ? 87.305  0.261   29.743 1.00 21.07  ? 121  GLU D CA  1 
ATOM   4231  C  C   . GLU D  1 121 ? 85.803  0.177   29.491 1.00 22.44  ? 121  GLU D C   1 
ATOM   4232  O  O   . GLU D  1 121 ? 85.102  -0.527  30.222 1.00 23.27  ? 121  GLU D O   1 
ATOM   4233  C  CB  . GLU D  1 121 ? 87.659  1.618   30.367 1.00 29.83  ? 121  GLU D CB  1 
ATOM   4234  C  CG  . GLU D  1 121 ? 86.987  1.961   31.675 1.00 37.24  ? 121  GLU D CG  1 
ATOM   4235  C  CD  . GLU D  1 121 ? 86.966  3.460   31.944 1.00 38.34  ? 121  GLU D CD  1 
ATOM   4236  O  OE1 . GLU D  1 121 ? 86.356  3.804   32.978 1.00 44.90  ? 121  GLU D OE1 1 
ATOM   4237  O  OE2 . GLU D  1 121 ? 87.510  4.312   31.202 1.00 29.36  ? 121  GLU D OE2 1 
ATOM   4238  N  N   . LYS D  1 122 ? 85.327  0.876   28.468 1.00 23.03  ? 122  LYS D N   1 
ATOM   4239  C  CA  . LYS D  1 122 ? 83.903  1.010   28.188 1.00 22.44  ? 122  LYS D CA  1 
ATOM   4240  C  C   . LYS D  1 122 ? 83.503  0.496   26.806 1.00 21.78  ? 122  LYS D C   1 
ATOM   4241  O  O   . LYS D  1 122 ? 84.355  0.238   25.969 1.00 19.82  ? 122  LYS D O   1 
ATOM   4242  C  CB  . LYS D  1 122 ? 83.474  2.481   28.264 1.00 25.73  ? 122  LYS D CB  1 
ATOM   4243  C  CG  . LYS D  1 122 ? 83.953  3.236   29.496 1.00 30.57  ? 122  LYS D CG  1 
ATOM   4244  C  CD  . LYS D  1 122 ? 83.756  4.729   29.237 1.00 35.48  ? 122  LYS D CD  1 
ATOM   4245  C  CE  . LYS D  1 122 ? 83.662  5.506   30.538 1.00 45.30  ? 122  LYS D CE  1 
ATOM   4246  N  NZ  . LYS D  1 122 ? 83.284  6.926   30.253 1.00 39.82  ? 122  LYS D NZ  1 
ATOM   4247  N  N   . ALA D  1 123 ? 82.183  0.387   26.615 1.00 21.56  ? 123  ALA D N   1 
ATOM   4248  C  CA  . ALA D  1 123 ? 81.632  0.048   25.318 1.00 19.99  ? 123  ALA D CA  1 
ATOM   4249  C  C   . ALA D  1 123 ? 82.004  1.099   24.289 1.00 17.43  ? 123  ALA D C   1 
ATOM   4250  O  O   . ALA D  1 123 ? 82.057  2.315   24.533 1.00 22.71  ? 123  ALA D O   1 
ATOM   4251  C  CB  . ALA D  1 123 ? 80.104  -0.048  25.374 1.00 21.85  ? 123  ALA D CB  1 
ATOM   4252  N  N   . ASP D  1 124 ? 82.260  0.643   23.081 1.00 17.58  ? 124  ASP D N   1 
ATOM   4253  C  CA  . ASP D  1 124 ? 82.396  1.537   21.925 1.00 19.06  ? 124  ASP D CA  1 
ATOM   4254  C  C   . ASP D  1 124 ? 80.994  1.864   21.420 1.00 19.84  ? 124  ASP D C   1 
ATOM   4255  O  O   . ASP D  1 124 ? 80.225  0.939   21.182 1.00 20.66  ? 124  ASP D O   1 
ATOM   4256  C  CB  . ASP D  1 124 ? 83.270  0.814   20.905 1.00 20.40  ? 124  ASP D CB  1 
ATOM   4257  C  CG  . ASP D  1 124 ? 83.562  1.583   19.634 1.00 22.85  ? 124  ASP D CG  1 
ATOM   4258  O  OD1 . ASP D  1 124 ? 84.570  1.238   18.969 1.00 21.69  ? 124  ASP D OD1 1 
ATOM   4259  O  OD2 . ASP D  1 124 ? 82.802  2.520   19.283 1.00 19.22  ? 124  ASP D OD2 1 
ATOM   4260  N  N   . ASP D  1 125 ? 80.616  3.124   21.262 1.00 18.10  ? 125  ASP D N   1 
ATOM   4261  C  CA  . ASP D  1 125 ? 79.243  3.424   20.831 1.00 17.85  ? 125  ASP D CA  1 
ATOM   4262  C  C   . ASP D  1 125 ? 79.138  3.426   19.318 1.00 20.51  ? 125  ASP D C   1 
ATOM   4263  O  O   . ASP D  1 125 ? 78.110  3.810   18.760 1.00 19.77  ? 125  ASP D O   1 
ATOM   4264  C  CB  . ASP D  1 125 ? 78.799  4.757   21.410 1.00 19.47  ? 125  ASP D CB  1 
ATOM   4265  C  CG  . ASP D  1 125 ? 79.514  5.977   20.890 1.00 25.58  ? 125  ASP D CG  1 
ATOM   4266  O  OD1 . ASP D  1 125 ? 79.336  7.030   21.568 1.00 25.08  ? 125  ASP D OD1 1 
ATOM   4267  O  OD2 . ASP D  1 125 ? 80.217  5.984   19.859 1.00 20.81  ? 125  ASP D OD2 1 
ATOM   4268  N  N   . LEU D  1 126 ? 80.196  2.995   18.641 1.00 18.74  ? 126  LEU D N   1 
ATOM   4269  C  CA  . LEU D  1 126 ? 80.161  2.782   17.187 1.00 19.72  ? 126  LEU D CA  1 
ATOM   4270  C  C   . LEU D  1 126 ? 79.903  4.063   16.431 1.00 19.09  ? 126  LEU D C   1 
ATOM   4271  O  O   . LEU D  1 126 ? 79.436  4.063   15.289 1.00 21.37  ? 126  LEU D O   1 
ATOM   4272  C  CB  . LEU D  1 126 ? 79.142  1.687   16.829 1.00 21.96  ? 126  LEU D CB  1 
ATOM   4273  C  CG  . LEU D  1 126 ? 79.283  0.384   17.634 1.00 22.70  ? 126  LEU D CG  1 
ATOM   4274  C  CD1 . LEU D  1 126 ? 78.330  -0.696  17.122 1.00 23.60  ? 126  LEU D CD1 1 
ATOM   4275  C  CD2 . LEU D  1 126 ? 80.720  -0.110  17.591 1.00 22.17  ? 126  LEU D CD2 1 
ATOM   4276  N  N   . GLY D  1 127 ? 80.281  5.206   17.029 1.00 20.83  ? 127  GLY D N   1 
ATOM   4277  C  CA  . GLY D  1 127 ? 80.148  6.471   16.308 1.00 22.06  ? 127  GLY D CA  1 
ATOM   4278  C  C   . GLY D  1 127 ? 78.758  7.066   16.408 1.00 18.88  ? 127  GLY D C   1 
ATOM   4279  O  O   . GLY D  1 127 ? 78.501  8.040   15.699 1.00 22.24  ? 127  GLY D O   1 
ATOM   4280  N  N   . LYS D  1 128 ? 77.881  6.515   17.229 1.00 17.54  ? 128  LYS D N   1 
ATOM   4281  C  CA  . LYS D  1 128 ? 76.479  6.965   17.276 1.00 18.88  ? 128  LYS D CA  1 
ATOM   4282  C  C   . LYS D  1 128 ? 76.127  7.737   18.551 1.00 19.88  ? 128  LYS D C   1 
ATOM   4283  O  O   . LYS D  1 128 ? 74.955  7.856   18.892 1.00 20.90  ? 128  LYS D O   1 
ATOM   4284  C  CB  . LYS D  1 128 ? 75.551  5.752   17.173 1.00 18.83  ? 128  LYS D CB  1 
ATOM   4285  C  CG  . LYS D  1 128 ? 75.795  4.990   15.859 1.00 19.08  ? 128  LYS D CG  1 
ATOM   4286  C  CD  . LYS D  1 128 ? 75.146  3.601   15.970 1.00 23.96  ? 128  LYS D CD  1 
ATOM   4287  C  CE  . LYS D  1 128 ? 73.652  3.753   15.719 1.00 33.07  ? 128  LYS D CE  1 
ATOM   4288  N  NZ  . LYS D  1 128 ? 72.974  2.444   15.513 1.00 33.53  ? 128  LYS D NZ  1 
ATOM   4289  N  N   . GLY D  1 129 ? 77.142  8.233   19.235 1.00 18.82  ? 129  GLY D N   1 
ATOM   4290  C  CA  . GLY D  1 129 ? 76.978  8.902   20.503 1.00 22.01  ? 129  GLY D CA  1 
ATOM   4291  C  C   . GLY D  1 129 ? 76.640  10.377  20.420 1.00 19.29  ? 129  GLY D C   1 
ATOM   4292  O  O   . GLY D  1 129 ? 76.245  10.938  21.446 1.00 18.14  ? 129  GLY D O   1 
ATOM   4293  N  N   . GLY D  1 130 ? 76.785  11.004  19.258 1.00 18.32  ? 130  GLY D N   1 
ATOM   4294  C  CA  . GLY D  1 130 ? 76.377  12.389  19.087 1.00 18.23  ? 130  GLY D CA  1 
ATOM   4295  C  C   . GLY D  1 130 ? 77.272  13.432  19.707 1.00 23.53  ? 130  GLY D C   1 
ATOM   4296  O  O   . GLY D  1 130 ? 76.944  14.631  19.623 1.00 21.32  ? 130  GLY D O   1 
ATOM   4297  N  N   . ASN D  1 131 ? 78.386  13.034  20.338 1.00 22.69  ? 131  ASN D N   1 
ATOM   4298  C  CA  . ASN D  1 131 ? 79.318  14.040  20.858 1.00 18.70  ? 131  ASN D CA  1 
ATOM   4299  C  C   . ASN D  1 131 ? 80.638  13.950  20.108 1.00 21.77  ? 131  ASN D C   1 
ATOM   4300  O  O   . ASN D  1 131 ? 80.880  13.055  19.296 1.00 22.39  ? 131  ASN D O   1 
ATOM   4301  C  CB  . ASN D  1 131 ? 79.502  13.866  22.369 1.00 17.65  ? 131  ASN D CB  1 
ATOM   4302  C  CG  . ASN D  1 131 ? 80.223  12.568  22.718 1.00 24.67  ? 131  ASN D CG  1 
ATOM   4303  O  OD1 . ASN D  1 131 ? 80.383  11.637  21.927 1.00 22.32  ? 131  ASN D OD1 1 
ATOM   4304  N  ND2 . ASN D  1 131 ? 80.664  12.462  23.973 1.00 20.46  ? 131  ASN D ND2 1 
ATOM   4305  N  N   . GLU D  1 132 ? 81.547  14.904  20.343 1.00 22.51  ? 132  GLU D N   1 
ATOM   4306  C  CA  . GLU D  1 132 ? 82.818  14.929  19.629 1.00 26.20  ? 132  GLU D CA  1 
ATOM   4307  C  C   . GLU D  1 132 ? 83.573  13.623  19.808 1.00 22.87  ? 132  GLU D C   1 
ATOM   4308  O  O   . GLU D  1 132 ? 84.160  13.071  18.873 1.00 23.03  ? 132  GLU D O   1 
ATOM   4309  C  CB  . GLU D  1 132 ? 83.690  16.098  20.138 1.00 21.20  ? 132  GLU D CB  1 
ATOM   4310  C  CG  . GLU D  1 132 ? 82.993  17.434  19.860 1.00 25.03  ? 132  GLU D CG  1 
ATOM   4311  C  CD  . GLU D  1 132 ? 83.786  18.651  20.307 1.00 40.89  ? 132  GLU D CD  1 
ATOM   4312  O  OE1 . GLU D  1 132 ? 83.567  19.761  19.770 1.00 44.51  ? 132  GLU D OE1 1 
ATOM   4313  O  OE2 . GLU D  1 132 ? 84.635  18.530  21.214 1.00 44.61  ? 132  GLU D OE2 1 
ATOM   4314  N  N   . GLU D  1 133 ? 83.549  13.125  21.043 1.00 23.93  ? 133  GLU D N   1 
ATOM   4315  C  CA  . GLU D  1 133 ? 84.365  11.941  21.363 1.00 24.17  ? 133  GLU D CA  1 
ATOM   4316  C  C   . GLU D  1 133 ? 83.895  10.738  20.581 1.00 24.18  ? 133  GLU D C   1 
ATOM   4317  O  O   . GLU D  1 133 ? 84.646  9.836   20.220 1.00 22.08  ? 133  GLU D O   1 
ATOM   4318  C  CB  . GLU D  1 133 ? 84.291  11.700  22.868 1.00 26.90  ? 133  GLU D CB  1 
ATOM   4319  C  CG  . GLU D  1 133 ? 85.393  10.852  23.489 1.00 36.43  ? 133  GLU D CG  1 
ATOM   4320  C  CD  . GLU D  1 133 ? 86.769  11.318  23.023 1.00 40.30  ? 133  GLU D CD  1 
ATOM   4321  O  OE1 . GLU D  1 133 ? 87.460  10.518  22.364 1.00 45.80  ? 133  GLU D OE1 1 
ATOM   4322  O  OE2 . GLU D  1 133 ? 87.142  12.473  23.296 1.00 36.73  ? 133  GLU D OE2 1 
ATOM   4323  N  N   . SER D  1 134 ? 82.592  10.662  20.274 1.00 23.21  ? 134  SER D N   1 
ATOM   4324  C  CA  . SER D  1 134 ? 82.090  9.482   19.583 1.00 20.75  ? 134  SER D CA  1 
ATOM   4325  C  C   . SER D  1 134 ? 82.728  9.278   18.220 1.00 22.17  ? 134  SER D C   1 
ATOM   4326  O  O   . SER D  1 134 ? 82.951  8.145   17.785 1.00 23.03  ? 134  SER D O   1 
ATOM   4327  C  CB  . SER D  1 134 ? 80.542  9.607   19.457 1.00 19.65  ? 134  SER D CB  1 
ATOM   4328  O  OG  . SER D  1 134 ? 80.102  8.421   18.774 1.00 22.24  ? 134  SER D OG  1 
ATOM   4329  N  N   . THR D  1 135 ? 83.030  10.369  17.527 1.00 20.96  ? 135  THR D N   1 
ATOM   4330  C  CA  . THR D  1 135 ? 83.575  10.392  16.183 1.00 19.42  ? 135  THR D CA  1 
ATOM   4331  C  C   . THR D  1 135 ? 85.085  10.164  16.176 1.00 20.10  ? 135  THR D C   1 
ATOM   4332  O  O   . THR D  1 135 ? 85.691  10.066  15.109 1.00 26.73  ? 135  THR D O   1 
ATOM   4333  C  CB  . THR D  1 135 ? 83.350  11.754  15.473 1.00 27.86  ? 135  THR D CB  1 
ATOM   4334  O  OG1 . THR D  1 135 ? 84.163  12.755  16.098 1.00 44.10  ? 135  THR D OG1 1 
ATOM   4335  C  CG2 . THR D  1 135 ? 81.925  12.242  15.635 1.00 38.02  ? 135  THR D CG2 1 
ATOM   4336  N  N   . LYS D  1 136 ? 85.645  10.090  17.369 1.00 23.33  ? 136  LYS D N   1 
ATOM   4337  C  CA  . LYS D  1 136 ? 87.068  9.808   17.519 1.00 21.94  ? 136  LYS D CA  1 
ATOM   4338  C  C   . LYS D  1 136 ? 87.348  8.433   18.103 1.00 18.96  ? 136  LYS D C   1 
ATOM   4339  O  O   . LYS D  1 136 ? 88.162  7.705   17.551 1.00 24.19  ? 136  LYS D O   1 
ATOM   4340  C  CB  . LYS D  1 136 ? 87.697  10.846  18.471 1.00 30.20  ? 136  LYS D CB  1 
ATOM   4341  C  CG  . LYS D  1 136 ? 87.583  12.289  18.013 1.00 34.81  ? 136  LYS D CG  1 
ATOM   4342  C  CD  . LYS D  1 136 ? 88.352  13.226  18.936 1.00 38.46  ? 136  LYS D CD  1 
ATOM   4343  C  CE  . LYS D  1 136 ? 87.654  14.567  19.097 1.00 50.71  ? 136  LYS D CE  1 
ATOM   4344  N  NZ  . LYS D  1 136 ? 88.215  15.369  20.217 1.00 50.77  ? 136  LYS D NZ  1 
ATOM   4345  N  N   . THR D  1 137 ? 86.751  8.125   19.247 1.00 20.33  ? 137  THR D N   1 
ATOM   4346  C  CA  . THR D  1 137 ? 87.059  6.903   19.985 1.00 21.31  ? 137  THR D CA  1 
ATOM   4347  C  C   . THR D  1 137 ? 85.842  6.055   20.339 1.00 25.09  ? 137  THR D C   1 
ATOM   4348  O  O   . THR D  1 137 ? 86.005  5.017   20.989 1.00 21.95  ? 137  THR D O   1 
ATOM   4349  C  CB  . THR D  1 137 ? 87.720  7.233   21.348 1.00 24.90  ? 137  THR D CB  1 
ATOM   4350  O  OG1 . THR D  1 137 ? 86.722  7.922   22.139 1.00 25.92  ? 137  THR D OG1 1 
ATOM   4351  C  CG2 . THR D  1 137 ? 88.919  8.141   21.162 1.00 26.56  ? 137  THR D CG2 1 
ATOM   4352  N  N   . GLY D  1 138 ? 84.634  6.497   20.003 1.00 23.38  ? 138  GLY D N   1 
ATOM   4353  C  CA  . GLY D  1 138 ? 83.438  5.752   20.371 1.00 16.70  ? 138  GLY D CA  1 
ATOM   4354  C  C   . GLY D  1 138 ? 83.131  5.890   21.853 1.00 19.39  ? 138  GLY D C   1 
ATOM   4355  O  O   . GLY D  1 138 ? 82.297  5.150   22.369 1.00 21.96  ? 138  GLY D O   1 
ATOM   4356  N  N   . ASN D  1 139 ? 83.787  6.849   22.514 1.00 19.97  ? 139  ASN D N   1 
ATOM   4357  C  CA  . ASN D  1 139 ? 83.599  6.965   23.968 1.00 20.30  ? 139  ASN D CA  1 
ATOM   4358  C  C   . ASN D  1 139 ? 83.999  5.687   24.693 1.00 21.94  ? 139  ASN D C   1 
ATOM   4359  O  O   . ASN D  1 139 ? 83.412  5.361   25.737 1.00 23.29  ? 139  ASN D O   1 
ATOM   4360  C  CB  . ASN D  1 139 ? 82.137  7.305   24.271 1.00 23.53  ? 139  ASN D CB  1 
ATOM   4361  C  CG  . ASN D  1 139 ? 81.812  8.744   23.920 1.00 27.21  ? 139  ASN D CG  1 
ATOM   4362  O  OD1 . ASN D  1 139 ? 82.283  9.681   24.571 1.00 24.37  ? 139  ASN D OD1 1 
ATOM   4363  N  ND2 . ASN D  1 139 ? 81.029  8.970   22.872 1.00 21.96  ? 139  ASN D ND2 1 
ATOM   4364  N  N   . ALA D  1 140 ? 84.982  4.940   24.179 1.00 21.64  ? 140  ALA D N   1 
ATOM   4365  C  CA  . ALA D  1 140 ? 85.405  3.682   24.782 1.00 25.53  ? 140  ALA D CA  1 
ATOM   4366  C  C   . ALA D  1 140 ? 86.233  3.839   26.059 1.00 23.03  ? 140  ALA D C   1 
ATOM   4367  O  O   . ALA D  1 140 ? 86.561  2.879   26.764 1.00 21.62  ? 140  ALA D O   1 
ATOM   4368  C  CB  . ALA D  1 140 ? 86.198  2.882   23.740 1.00 22.12  ? 140  ALA D CB  1 
ATOM   4369  N  N   . GLY D  1 141 ? 86.632  5.049   26.420 1.00 24.12  ? 141  GLY D N   1 
ATOM   4370  C  CA  . GLY D  1 141 ? 87.301  5.186   27.715 1.00 24.33  ? 141  GLY D CA  1 
ATOM   4371  C  C   . GLY D  1 141 ? 88.721  4.674   27.717 1.00 29.74  ? 141  GLY D C   1 
ATOM   4372  O  O   . GLY D  1 141 ? 89.440  4.603   26.727 1.00 23.04  ? 141  GLY D O   1 
ATOM   4373  N  N   . SER D  1 142 ? 89.221  4.293   28.887 1.00 22.12  ? 142  SER D N   1 
ATOM   4374  C  CA  . SER D  1 142 ? 90.658  4.036   28.943 1.00 27.68  ? 142  SER D CA  1 
ATOM   4375  C  C   . SER D  1 142 ? 91.064  2.683   28.386 1.00 25.18  ? 142  SER D C   1 
ATOM   4376  O  O   . SER D  1 142 ? 90.222  1.823   28.163 1.00 25.39  ? 142  SER D O   1 
ATOM   4377  C  CB  . SER D  1 142 ? 91.120  4.215   30.408 1.00 32.63  ? 142  SER D CB  1 
ATOM   4378  O  OG  . SER D  1 142 ? 90.670  3.164   31.236 1.00 34.79  ? 142  SER D OG  1 
ATOM   4379  N  N   . ARG D  1 143 ? 92.380  2.524   28.204 1.00 22.76  ? 143  ARG D N   1 
ATOM   4380  C  CA  . ARG D  1 143 ? 92.997  1.340   27.617 1.00 21.90  ? 143  ARG D CA  1 
ATOM   4381  C  C   . ARG D  1 143 ? 93.418  0.388   28.717 1.00 29.42  ? 143  ARG D C   1 
ATOM   4382  O  O   . ARG D  1 143 ? 94.333  0.649   29.507 1.00 27.95  ? 143  ARG D O   1 
ATOM   4383  C  CB  . ARG D  1 143 ? 94.181  1.779   26.739 1.00 21.09  ? 143  ARG D CB  1 
ATOM   4384  C  CG  . ARG D  1 143 ? 93.800  3.019   25.927 1.00 23.28  ? 143  ARG D CG  1 
ATOM   4385  C  CD  . ARG D  1 143 ? 94.922  3.540   25.062 1.00 25.53  ? 143  ARG D CD  1 
ATOM   4386  N  NE  . ARG D  1 143 ? 94.502  4.644   24.220 1.00 27.98  ? 143  ARG D NE  1 
ATOM   4387  C  CZ  . ARG D  1 143 ? 95.145  5.198   23.205 1.00 32.33  ? 143  ARG D CZ  1 
ATOM   4388  N  NH1 . ARG D  1 143 ? 94.549  6.212   22.577 1.00 26.11  ? 143  ARG D NH1 1 
ATOM   4389  N  NH2 . ARG D  1 143 ? 96.348  4.785   22.804 1.00 28.03  ? 143  ARG D NH2 1 
ATOM   4390  N  N   . LEU D  1 144 ? 92.710  -0.728  28.807 1.00 21.75  ? 144  LEU D N   1 
ATOM   4391  C  CA  . LEU D  1 144 ? 92.952  -1.621  29.930 1.00 19.56  ? 144  LEU D CA  1 
ATOM   4392  C  C   . LEU D  1 144 ? 94.086  -2.603  29.631 1.00 25.46  ? 144  LEU D C   1 
ATOM   4393  O  O   . LEU D  1 144 ? 94.751  -3.061  30.565 1.00 21.85  ? 144  LEU D O   1 
ATOM   4394  C  CB  . LEU D  1 144 ? 91.692  -2.403  30.264 1.00 21.34  ? 144  LEU D CB  1 
ATOM   4395  C  CG  . LEU D  1 144 ? 90.459  -1.598  30.704 1.00 24.06  ? 144  LEU D CG  1 
ATOM   4396  C  CD1 . LEU D  1 144 ? 89.352  -2.571  31.087 1.00 23.42  ? 144  LEU D CD1 1 
ATOM   4397  C  CD2 . LEU D  1 144 ? 90.821  -0.655  31.831 1.00 29.31  ? 144  LEU D CD2 1 
ATOM   4398  N  N   . ALA D  1 145 ? 94.272  -2.964  28.360 1.00 19.99  ? 145  ALA D N   1 
ATOM   4399  C  CA  . ALA D  1 145 ? 95.335  -3.906  28.027 1.00 19.01  ? 145  ALA D CA  1 
ATOM   4400  C  C   . ALA D  1 145 ? 95.667  -3.745  26.544 1.00 26.01  ? 145  ALA D C   1 
ATOM   4401  O  O   . ALA D  1 145 ? 94.786  -3.341  25.784 1.00 22.78  ? 145  ALA D O   1 
ATOM   4402  C  CB  . ALA D  1 145 ? 94.989  -5.339  28.333 1.00 21.02  ? 145  ALA D CB  1 
ATOM   4403  N  N   . CYS D  1 146 ? 96.912  -4.041  26.168 1.00 20.67  ? 146  CYS D N   1 
ATOM   4404  C  CA  . CYS D  1 146 ? 97.279  -3.807  24.761 1.00 17.67  ? 146  CYS D CA  1 
ATOM   4405  C  C   . CYS D  1 146 ? 98.476  -4.676  24.414 1.00 21.05  ? 146  CYS D C   1 
ATOM   4406  O  O   . CYS D  1 146 ? 99.088  -5.254  25.321 1.00 21.16  ? 146  CYS D O   1 
ATOM   4407  C  CB  A CYS D  1 146 ? 97.578  -2.341  24.469 0.43 23.07  ? 146  CYS D CB  1 
ATOM   4408  C  CB  B CYS D  1 146 ? 97.545  -2.323  24.525 0.57 23.57  ? 146  CYS D CB  1 
ATOM   4409  S  SG  A CYS D  1 146 ? 98.749  -1.572  25.610 0.43 31.52  ? 146  CYS D SG  1 
ATOM   4410  S  SG  B CYS D  1 146 ? 99.092  -1.625  25.130 0.57 27.85  ? 146  CYS D SG  1 
ATOM   4411  N  N   . GLY D  1 147 ? 98.772  -4.767  23.127 1.00 20.98  ? 147  GLY D N   1 
ATOM   4412  C  CA  . GLY D  1 147 ? 99.905  -5.579  22.688 1.00 22.90  ? 147  GLY D CA  1 
ATOM   4413  C  C   . GLY D  1 147 ? 100.279 -5.225  21.267 1.00 29.13  ? 147  GLY D C   1 
ATOM   4414  O  O   . GLY D  1 147 ? 99.401  -4.797  20.523 1.00 23.10  ? 147  GLY D O   1 
ATOM   4415  N  N   . VAL D  1 148 ? 101.549 -5.393  20.892 1.00 24.52  ? 148  VAL D N   1 
ATOM   4416  C  CA  . VAL D  1 148 ? 101.903 -5.192  19.484 1.00 19.84  ? 148  VAL D CA  1 
ATOM   4417  C  C   . VAL D  1 148 ? 101.538 -6.430  18.710 1.00 22.38  ? 148  VAL D C   1 
ATOM   4418  O  O   . VAL D  1 148 ? 101.723 -7.585  19.141 1.00 23.91  ? 148  VAL D O   1 
ATOM   4419  C  CB  . VAL D  1 148 ? 103.396 -4.832  19.332 1.00 22.54  ? 148  VAL D CB  1 
ATOM   4420  C  CG1 . VAL D  1 148 ? 103.717 -4.541  17.864 1.00 24.29  ? 148  VAL D CG1 1 
ATOM   4421  C  CG2 . VAL D  1 148 ? 103.728 -3.618  20.184 1.00 22.53  ? 148  VAL D CG2 1 
ATOM   4422  N  N   . ILE D  1 149 ? 100.962 -6.194  17.512 1.00 23.37  ? 149  ILE D N   1 
ATOM   4423  C  CA  . ILE D  1 149 ? 100.567 -7.318  16.660 1.00 19.93  ? 149  ILE D CA  1 
ATOM   4424  C  C   . ILE D  1 149 ? 101.749 -7.849  15.867 1.00 25.64  ? 149  ILE D C   1 
ATOM   4425  O  O   . ILE D  1 149 ? 102.394 -7.105  15.129 1.00 22.09  ? 149  ILE D O   1 
ATOM   4426  C  CB  . ILE D  1 149 ? 99.451  -6.863  15.689 1.00 21.66  ? 149  ILE D CB  1 
ATOM   4427  C  CG1 . ILE D  1 149 ? 98.214  -6.367  16.460 1.00 20.32  ? 149  ILE D CG1 1 
ATOM   4428  C  CG2 . ILE D  1 149 ? 99.105  -7.962  14.705 1.00 23.05  ? 149  ILE D CG2 1 
ATOM   4429  C  CD1 . ILE D  1 149 ? 97.225  -5.638  15.557 1.00 23.17  ? 149  ILE D CD1 1 
ATOM   4430  N  N   . GLY D  1 150 ? 102.051 -9.129  16.039 1.00 23.02  ? 150  GLY D N   1 
ATOM   4431  C  CA  . GLY D  1 150 ? 103.217 -9.647  15.323 1.00 29.27  ? 150  GLY D CA  1 
ATOM   4432  C  C   . GLY D  1 150 ? 102.913 -10.739 14.346 1.00 28.75  ? 150  GLY D C   1 
ATOM   4433  O  O   . GLY D  1 150 ? 101.892 -11.435 14.349 1.00 27.53  ? 150  GLY D O   1 
ATOM   4434  N  N   . ILE D  1 151 ? 103.885 -10.975 13.444 1.00 23.18  ? 151  ILE D N   1 
ATOM   4435  C  CA  . ILE D  1 151 ? 103.711 -12.106 12.544 1.00 24.20  ? 151  ILE D CA  1 
ATOM   4436  C  C   . ILE D  1 151 ? 103.742 -13.459 13.226 1.00 24.66  ? 151  ILE D C   1 
ATOM   4437  O  O   . ILE D  1 151 ? 104.616 -13.688 14.062 1.00 28.21  ? 151  ILE D O   1 
ATOM   4438  C  CB  . ILE D  1 151 ? 104.824 -12.061 11.454 1.00 31.21  ? 151  ILE D CB  1 
ATOM   4439  C  CG1 . ILE D  1 151 ? 104.785 -10.732 10.706 1.00 37.57  ? 151  ILE D CG1 1 
ATOM   4440  C  CG2 . ILE D  1 151 ? 104.692 -13.260 10.552 1.00 33.68  ? 151  ILE D CG2 1 
ATOM   4441  C  CD1 . ILE D  1 151 ? 106.124 -10.250 10.197 1.00 39.83  ? 151  ILE D CD1 1 
ATOM   4442  N  N   . ALA D  1 152 ? 102.809 -14.354 12.889 1.00 23.68  ? 152  ALA D N   1 
ATOM   4443  C  CA  . ALA D  1 152 ? 102.828 -15.669 13.530 1.00 22.91  ? 152  ALA D CA  1 
ATOM   4444  C  C   . ALA D  1 152 ? 103.160 -16.790 12.554 1.00 28.75  ? 152  ALA D C   1 
ATOM   4445  O  O   . ALA D  1 152 ? 102.993 -16.643 11.334 1.00 30.93  ? 152  ALA D O   1 
ATOM   4446  C  CB  . ALA D  1 152 ? 101.480 -15.909 14.181 1.00 23.34  ? 152  ALA D CB  1 
ATOM   4447  N  N   . GLN D  1 153 ? 103.630 -17.939 13.051 1.00 32.20  ? 153  GLN D N   1 
ATOM   4448  C  CA  . GLN D  1 153 ? 103.980 -19.020 12.120 1.00 45.51  ? 153  GLN D CA  1 
ATOM   4449  C  C   . GLN D  1 153 ? 102.721 -19.628 11.512 1.00 55.86  ? 153  GLN D C   1 
ATOM   4450  O  O   . GLN D  1 153 ? 101.653 -19.495 12.147 1.00 87.27  ? 153  GLN D O   1 
ATOM   4451  C  CB  . GLN D  1 153 ? 104.826 -20.083 12.825 1.00 56.67  ? 153  GLN D CB  1 
ATOM   4452  C  CG  . GLN D  1 153 ? 105.072 -21.363 12.042 1.00 57.30  ? 153  GLN D CG  1 
ATOM   4453  C  CD  . GLN D  1 153 ? 106.131 -22.269 12.634 1.00 48.91  ? 153  GLN D CD  1 
ATOM   4454  O  OE1 . GLN D  1 153 ? 107.077 -22.679 11.957 1.00 71.20  ? 153  GLN D OE1 1 
ATOM   4455  N  NE2 . GLN D  1 153 ? 105.991 -22.612 13.908 1.00 42.45  ? 153  GLN D NE2 1 
ATOM   4456  O  OXT . GLN D  1 153 ? 102.782 -20.226 10.417 1.00 74.63  ? 153  GLN D OXT 1 
ATOM   4457  N  N   . ALA E  1 1   ? 62.768  -38.285 6.956  1.00 48.50  ? 1    ALA E N   1 
ATOM   4458  C  CA  . ALA E  1 1   ? 61.361  -38.137 7.320  1.00 50.00  ? 1    ALA E CA  1 
ATOM   4459  C  C   . ALA E  1 1   ? 61.004  -36.763 7.874  1.00 44.01  ? 1    ALA E C   1 
ATOM   4460  O  O   . ALA E  1 1   ? 61.748  -36.119 8.608  1.00 42.98  ? 1    ALA E O   1 
ATOM   4461  C  CB  . ALA E  1 1   ? 60.984  -39.199 8.358  1.00 32.32  ? 1    ALA E CB  1 
ATOM   4462  N  N   . THR E  1 2   ? 59.817  -36.263 7.575  1.00 34.92  ? 2    THR E N   1 
ATOM   4463  C  CA  . THR E  1 2   ? 59.271  -35.127 8.327  1.00 30.52  ? 2    THR E CA  1 
ATOM   4464  C  C   . THR E  1 2   ? 58.760  -35.629 9.678  1.00 27.50  ? 2    THR E C   1 
ATOM   4465  O  O   . THR E  1 2   ? 58.179  -36.716 9.776  1.00 25.17  ? 2    THR E O   1 
ATOM   4466  C  CB  . THR E  1 2   ? 58.202  -34.461 7.458  1.00 36.42  ? 2    THR E CB  1 
ATOM   4467  O  OG1 . THR E  1 2   ? 58.852  -34.104 6.215  1.00 54.81  ? 2    THR E OG1 1 
ATOM   4468  C  CG2 . THR E  1 2   ? 57.670  -33.176 8.027  1.00 32.23  ? 2    THR E CG2 1 
ATOM   4469  N  N   . LYS E  1 3   ? 59.032  -34.833 10.720 1.00 23.94  ? 3    LYS E N   1 
ATOM   4470  C  CA  . LYS E  1 3   ? 58.682  -35.147 12.091 1.00 19.34  ? 3    LYS E CA  1 
ATOM   4471  C  C   . LYS E  1 3   ? 57.940  -33.996 12.760 1.00 23.14  ? 3    LYS E C   1 
ATOM   4472  O  O   . LYS E  1 3   ? 58.221  -32.820 12.529 1.00 24.01  ? 3    LYS E O   1 
ATOM   4473  C  CB  . LYS E  1 3   ? 59.937  -35.463 12.912 1.00 22.90  ? 3    LYS E CB  1 
ATOM   4474  C  CG  . LYS E  1 3   ? 60.616  -36.756 12.496 1.00 31.64  ? 3    LYS E CG  1 
ATOM   4475  C  CD  . LYS E  1 3   ? 61.569  -37.229 13.582 1.00 43.41  ? 3    LYS E CD  1 
ATOM   4476  C  CE  . LYS E  1 3   ? 61.598  -38.754 13.630 1.00 69.75  ? 3    LYS E CE  1 
ATOM   4477  N  NZ  . LYS E  1 3   ? 60.915  -39.324 14.823 1.00 84.18  ? 3    LYS E NZ  1 
ATOM   4478  N  N   . ALA E  1 4   ? 56.977  -34.322 13.625 1.00 24.41  ? 4    ALA E N   1 
ATOM   4479  C  CA  . ALA E  1 4   ? 56.294  -33.287 14.397 1.00 16.89  ? 4    ALA E CA  1 
ATOM   4480  C  C   . ALA E  1 4   ? 56.091  -33.849 15.811 1.00 17.48  ? 4    ALA E C   1 
ATOM   4481  O  O   . ALA E  1 4   ? 56.242  -35.045 16.072 1.00 19.64  ? 4    ALA E O   1 
ATOM   4482  C  CB  . ALA E  1 4   ? 54.987  -32.857 13.769 1.00 19.80  ? 4    ALA E CB  1 
ATOM   4483  N  N   . VAL E  1 5   ? 55.728  -32.942 16.716 1.00 20.15  ? 5    VAL E N   1 
ATOM   4484  C  CA  . VAL E  1 5   ? 55.487  -33.372 18.092 1.00 19.76  ? 5    VAL E CA  1 
ATOM   4485  C  C   . VAL E  1 5   ? 54.450  -32.462 18.705 1.00 19.74  ? 5    VAL E C   1 
ATOM   4486  O  O   . VAL E  1 5   ? 54.234  -31.335 18.275 1.00 19.75  ? 5    VAL E O   1 
ATOM   4487  C  CB  . VAL E  1 5   ? 56.809  -33.334 18.889 1.00 20.07  ? 5    VAL E CB  1 
ATOM   4488  C  CG1 . VAL E  1 5   ? 57.273  -31.881 19.014 1.00 22.53  ? 5    VAL E CG1 1 
ATOM   4489  C  CG2 . VAL E  1 5   ? 56.646  -34.004 20.242 1.00 20.51  ? 5    VAL E CG2 1 
ATOM   4490  N  N   . CYS E  1 6   ? 53.741  -32.977 19.718 1.00 20.43  ? 6    CYS E N   1 
ATOM   4491  C  CA  . CYS E  1 6   ? 52.699  -32.186 20.349 1.00 20.91  ? 6    CYS E CA  1 
ATOM   4492  C  C   . CYS E  1 6   ? 52.694  -32.513 21.845 1.00 21.52  ? 6    CYS E C   1 
ATOM   4493  O  O   . CYS E  1 6   ? 52.712  -33.697 22.181 1.00 20.17  ? 6    CYS E O   1 
ATOM   4494  C  CB  . CYS E  1 6   ? 51.338  -32.523 19.736 1.00 17.90  ? 6    CYS E CB  1 
ATOM   4495  S  SG  . CYS E  1 6   ? 49.947  -31.675 20.488 1.00 23.90  ? 6    CYS E SG  1 
ATOM   4496  N  N   . VAL E  1 7   ? 52.698  -31.469 22.655 1.00 18.89  ? 7    VAL E N   1 
ATOM   4497  C  CA  . VAL E  1 7   ? 52.605  -31.655 24.107 1.00 19.85  ? 7    VAL E CA  1 
ATOM   4498  C  C   . VAL E  1 7   ? 51.184  -31.323 24.537 1.00 16.66  ? 7    VAL E C   1 
ATOM   4499  O  O   . VAL E  1 7   ? 50.700  -30.198 24.385 1.00 20.71  ? 7    VAL E O   1 
ATOM   4500  C  CB  . VAL E  1 7   ? 53.635  -30.768 24.827 1.00 22.01  ? 7    VAL E CB  1 
ATOM   4501  C  CG1 . VAL E  1 7   ? 53.508  -30.860 26.338 1.00 24.19  ? 7    VAL E CG1 1 
ATOM   4502  C  CG2 . VAL E  1 7   ? 55.041  -31.190 24.397 1.00 23.96  ? 7    VAL E CG2 1 
ATOM   4503  N  N   . LEU E  1 8   ? 50.458  -32.311 25.036 1.00 19.18  ? 8    LEU E N   1 
ATOM   4504  C  CA  . LEU E  1 8   ? 49.075  -32.107 25.426 1.00 20.03  ? 8    LEU E CA  1 
ATOM   4505  C  C   . LEU E  1 8   ? 48.939  -31.688 26.885 1.00 18.78  ? 8    LEU E C   1 
ATOM   4506  O  O   . LEU E  1 8   ? 49.538  -32.334 27.737 1.00 22.51  ? 8    LEU E O   1 
ATOM   4507  C  CB  . LEU E  1 8   ? 48.308  -33.424 25.260 1.00 19.86  ? 8    LEU E CB  1 
ATOM   4508  C  CG  . LEU E  1 8   ? 48.277  -34.019 23.857 1.00 26.59  ? 8    LEU E CG  1 
ATOM   4509  C  CD1 . LEU E  1 8   ? 47.694  -35.429 23.860 1.00 38.28  ? 8    LEU E CD1 1 
ATOM   4510  C  CD2 . LEU E  1 8   ? 47.415  -33.152 22.961 1.00 24.59  ? 8    LEU E CD2 1 
ATOM   4511  N  N   . LYS E  1 9   ? 48.154  -30.664 27.131 1.00 18.21  ? 9    LYS E N   1 
ATOM   4512  C  CA  . LYS E  1 9   ? 47.897  -30.156 28.469 1.00 24.39  ? 9    LYS E CA  1 
ATOM   4513  C  C   . LYS E  1 9   ? 46.471  -29.636 28.568 1.00 22.51  ? 9    LYS E C   1 
ATOM   4514  O  O   . LYS E  1 9   ? 45.927  -29.174 27.558 1.00 23.86  ? 9    LYS E O   1 
ATOM   4515  C  CB  . LYS E  1 9   ? 48.797  -28.984 28.866 1.00 29.88  ? 9    LYS E CB  1 
ATOM   4516  C  CG  . LYS E  1 9   ? 50.180  -28.953 28.267 1.00 49.41  ? 9    LYS E CG  1 
ATOM   4517  C  CD  . LYS E  1 9   ? 51.190  -28.348 29.238 1.00 67.37  ? 9    LYS E CD  1 
ATOM   4518  C  CE  . LYS E  1 9   ? 52.337  -29.306 29.517 1.00 74.54  ? 9    LYS E CE  1 
ATOM   4519  N  NZ  . LYS E  1 9   ? 53.665  -28.631 29.575 1.00 65.80  ? 9    LYS E NZ  1 
ATOM   4520  N  N   . GLY E  1 10  ? 45.929  -29.667 29.793 1.00 25.46  ? 10   GLY E N   1 
ATOM   4521  C  CA  . GLY E  1 10  ? 44.610  -29.081 30.015 1.00 23.89  ? 10   GLY E CA  1 
ATOM   4522  C  C   . GLY E  1 10  ? 44.446  -28.572 31.440 1.00 30.88  ? 10   GLY E C   1 
ATOM   4523  O  O   . GLY E  1 10  ? 45.443  -28.368 32.142 1.00 33.46  ? 10   GLY E O   1 
ATOM   4524  N  N   . ASP E  1 11  ? 43.200  -28.384 31.855 1.00 30.23  ? 11   ASP E N   1 
ATOM   4525  C  CA  . ASP E  1 11  ? 42.954  -27.848 33.202 1.00 32.77  ? 11   ASP E CA  1 
ATOM   4526  C  C   . ASP E  1 11  ? 42.937  -28.932 34.269 1.00 38.05  ? 11   ASP E C   1 
ATOM   4527  O  O   . ASP E  1 11  ? 43.057  -28.671 35.470 1.00 34.50  ? 11   ASP E O   1 
ATOM   4528  C  CB  . ASP E  1 11  ? 41.619  -27.115 33.197 1.00 32.54  ? 11   ASP E CB  1 
ATOM   4529  C  CG  . ASP E  1 11  ? 41.626  -25.797 32.441 1.00 43.92  ? 11   ASP E CG  1 
ATOM   4530  O  OD1 . ASP E  1 11  ? 40.513  -25.329 32.098 1.00 68.58  ? 11   ASP E OD1 1 
ATOM   4531  O  OD2 . ASP E  1 11  ? 42.699  -25.213 32.184 1.00 42.13  ? 11   ASP E OD2 1 
ATOM   4532  N  N   . GLY E  1 12  ? 42.779  -30.178 33.838 1.00 31.18  ? 12   GLY E N   1 
ATOM   4533  C  CA  . GLY E  1 12  ? 42.802  -31.335 34.712 1.00 27.02  ? 12   GLY E CA  1 
ATOM   4534  C  C   . GLY E  1 12  ? 44.140  -32.040 34.664 1.00 26.30  ? 12   GLY E C   1 
ATOM   4535  O  O   . GLY E  1 12  ? 45.181  -31.445 34.344 1.00 29.04  ? 12   GLY E O   1 
ATOM   4536  N  N   . PRO E  1 13  ? 44.165  -33.321 35.011 1.00 27.39  ? 13   PRO E N   1 
ATOM   4537  C  CA  . PRO E  1 13  ? 45.405  -34.078 35.042 1.00 23.83  ? 13   PRO E CA  1 
ATOM   4538  C  C   . PRO E  1 13  ? 45.813  -34.729 33.729 1.00 22.10  ? 13   PRO E C   1 
ATOM   4539  O  O   . PRO E  1 13  ? 46.797  -35.453 33.640 1.00 25.90  ? 13   PRO E O   1 
ATOM   4540  C  CB  . PRO E  1 13  ? 45.031  -35.208 36.028 1.00 28.13  ? 13   PRO E CB  1 
ATOM   4541  C  CG  . PRO E  1 13  ? 43.608  -35.487 35.651 1.00 28.00  ? 13   PRO E CG  1 
ATOM   4542  C  CD  . PRO E  1 13  ? 42.999  -34.129 35.447 1.00 32.57  ? 13   PRO E CD  1 
ATOM   4543  N  N   . VAL E  1 14  ? 45.054  -34.494 32.652 1.00 24.67  ? 14   VAL E N   1 
ATOM   4544  C  CA  . VAL E  1 14  ? 45.445  -35.192 31.423 1.00 23.62  ? 14   VAL E CA  1 
ATOM   4545  C  C   . VAL E  1 14  ? 46.633  -34.475 30.777 1.00 22.95  ? 14   VAL E C   1 
ATOM   4546  O  O   . VAL E  1 14  ? 46.602  -33.259 30.564 1.00 23.63  ? 14   VAL E O   1 
ATOM   4547  C  CB  . VAL E  1 14  ? 44.276  -35.232 30.431 1.00 20.86  ? 14   VAL E CB  1 
ATOM   4548  C  CG1 . VAL E  1 14  ? 44.714  -35.873 29.112 1.00 22.79  ? 14   VAL E CG1 1 
ATOM   4549  C  CG2 . VAL E  1 14  ? 43.084  -36.000 31.009 1.00 22.52  ? 14   VAL E CG2 1 
ATOM   4550  N  N   . GLN E  1 15  ? 47.653  -35.240 30.464 1.00 25.73  ? 15   GLN E N   1 
ATOM   4551  C  CA  . GLN E  1 15  ? 48.797  -34.703 29.747 1.00 24.10  ? 15   GLN E CA  1 
ATOM   4552  C  C   . GLN E  1 15  ? 49.518  -35.801 28.991 1.00 28.39  ? 15   GLN E C   1 
ATOM   4553  O  O   . GLN E  1 15  ? 49.459  -37.002 29.261 1.00 27.25  ? 15   GLN E O   1 
ATOM   4554  C  CB  . GLN E  1 15  ? 49.752  -34.038 30.727 1.00 31.16  ? 15   GLN E CB  1 
ATOM   4555  C  CG  . GLN E  1 15  ? 50.330  -34.947 31.794 1.00 33.83  ? 15   GLN E CG  1 
ATOM   4556  C  CD  . GLN E  1 15  ? 51.232  -34.120 32.711 1.00 51.70  ? 15   GLN E CD  1 
ATOM   4557  O  OE1 . GLN E  1 15  ? 51.990  -33.275 32.219 1.00 51.67  ? 15   GLN E OE1 1 
ATOM   4558  N  NE2 . GLN E  1 15  ? 51.158  -34.332 34.017 1.00 33.29  ? 15   GLN E NE2 1 
ATOM   4559  N  N   . GLY E  1 16  ? 50.255  -35.364 27.956 1.00 24.23  ? 16   GLY E N   1 
ATOM   4560  C  CA  . GLY E  1 16  ? 51.037  -36.379 27.260 1.00 26.16  ? 16   GLY E CA  1 
ATOM   4561  C  C   . GLY E  1 16  ? 51.853  -35.786 26.117 1.00 23.45  ? 16   GLY E C   1 
ATOM   4562  O  O   . GLY E  1 16  ? 51.839  -34.565 25.928 1.00 22.33  ? 16   GLY E O   1 
ATOM   4563  N  N   . ILE E  1 17  ? 52.508  -36.723 25.444 1.00 23.06  ? 17   ILE E N   1 
ATOM   4564  C  CA  . ILE E  1 17  ? 53.403  -36.333 24.347 1.00 20.81  ? 17   ILE E CA  1 
ATOM   4565  C  C   . ILE E  1 17  ? 53.084  -37.256 23.176 1.00 22.09  ? 17   ILE E C   1 
ATOM   4566  O  O   . ILE E  1 17  ? 53.082  -38.463 23.353 1.00 23.41  ? 17   ILE E O   1 
ATOM   4567  C  CB  . ILE E  1 17  ? 54.866  -36.397 24.740 1.00 27.18  ? 17   ILE E CB  1 
ATOM   4568  C  CG1 . ILE E  1 17  ? 55.248  -35.392 25.853 1.00 27.44  ? 17   ILE E CG1 1 
ATOM   4569  C  CG2 . ILE E  1 17  ? 55.801  -36.163 23.562 1.00 22.55  ? 17   ILE E CG2 1 
ATOM   4570  C  CD1 . ILE E  1 17  ? 56.643  -35.700 26.358 1.00 27.72  ? 17   ILE E CD1 1 
ATOM   4571  N  N   . ILE E  1 18  ? 52.790  -36.612 22.053 1.00 20.57  ? 18   ILE E N   1 
ATOM   4572  C  CA  . ILE E  1 18  ? 52.478  -37.388 20.845 1.00 18.03  ? 18   ILE E CA  1 
ATOM   4573  C  C   . ILE E  1 18  ? 53.446  -36.992 19.735 1.00 16.29  ? 18   ILE E C   1 
ATOM   4574  O  O   . ILE E  1 18  ? 53.581  -35.802 19.501 1.00 20.06  ? 18   ILE E O   1 
ATOM   4575  C  CB  . ILE E  1 18  ? 51.019  -37.116 20.444 1.00 21.60  ? 18   ILE E CB  1 
ATOM   4576  C  CG1 . ILE E  1 18  ? 50.058  -37.525 21.582 1.00 18.49  ? 18   ILE E CG1 1 
ATOM   4577  C  CG2 . ILE E  1 18  ? 50.651  -37.778 19.124 1.00 18.49  ? 18   ILE E CG2 1 
ATOM   4578  C  CD1 . ILE E  1 18  ? 49.946  -39.034 21.709 1.00 22.43  ? 18   ILE E CD1 1 
ATOM   4579  N  N   . ASN E  1 19  ? 54.024  -37.986 19.107 1.00 18.96  ? 19   ASN E N   1 
ATOM   4580  C  CA  . ASN E  1 19  ? 55.004  -37.873 18.031 1.00 19.27  ? 19   ASN E CA  1 
ATOM   4581  C  C   . ASN E  1 19  ? 54.304  -38.182 16.715 1.00 22.96  ? 19   ASN E C   1 
ATOM   4582  O  O   . ASN E  1 19  ? 53.366  -38.990 16.712 1.00 20.34  ? 19   ASN E O   1 
ATOM   4583  C  CB  . ASN E  1 19  ? 56.183  -38.832 18.221 1.00 21.75  ? 19   ASN E CB  1 
ATOM   4584  C  CG  . ASN E  1 19  ? 56.820  -38.602 19.588 1.00 28.50  ? 19   ASN E CG  1 
ATOM   4585  O  OD1 . ASN E  1 19  ? 57.465  -37.573 19.766 1.00 28.66  ? 19   ASN E OD1 1 
ATOM   4586  N  ND2 . ASN E  1 19  ? 56.584  -39.553 20.482 1.00 23.65  ? 19   ASN E ND2 1 
ATOM   4587  N  N   . PHE E  1 20  ? 54.788  -37.507 15.684 1.00 19.08  ? 20   PHE E N   1 
ATOM   4588  C  CA  . PHE E  1 20  ? 54.344  -37.767 14.322 1.00 20.63  ? 20   PHE E CA  1 
ATOM   4589  C  C   . PHE E  1 20  ? 55.551  -38.020 13.432 1.00 27.45  ? 20   PHE E C   1 
ATOM   4590  O  O   . PHE E  1 20  ? 56.535  -37.285 13.538 1.00 24.46  ? 20   PHE E O   1 
ATOM   4591  C  CB  . PHE E  1 20  ? 53.605  -36.564 13.745 1.00 21.66  ? 20   PHE E CB  1 
ATOM   4592  C  CG  . PHE E  1 20  ? 52.374  -36.118 14.534 1.00 22.62  ? 20   PHE E CG  1 
ATOM   4593  C  CD1 . PHE E  1 20  ? 51.105  -36.432 14.062 1.00 21.89  ? 20   PHE E CD1 1 
ATOM   4594  C  CD2 . PHE E  1 20  ? 52.522  -35.398 15.717 1.00 24.08  ? 20   PHE E CD2 1 
ATOM   4595  C  CE1 . PHE E  1 20  ? 49.969  -36.031 14.755 1.00 19.06  ? 20   PHE E CE1 1 
ATOM   4596  C  CE2 . PHE E  1 20  ? 51.375  -34.999 16.420 1.00 23.50  ? 20   PHE E CE2 1 
ATOM   4597  C  CZ  . PHE E  1 20  ? 50.127  -35.326 15.935 1.00 19.92  ? 20   PHE E CZ  1 
ATOM   4598  N  N   . GLU E  1 21  ? 55.480  -39.004 12.547 1.00 20.74  ? 21   GLU E N   1 
ATOM   4599  C  CA  . GLU E  1 21  ? 56.590  -39.143 11.582 1.00 24.19  ? 21   GLU E CA  1 
ATOM   4600  C  C   . GLU E  1 21  ? 56.023  -39.488 10.207 1.00 27.81  ? 21   GLU E C   1 
ATOM   4601  O  O   . GLU E  1 21  ? 55.152  -40.360 10.100 1.00 24.98  ? 21   GLU E O   1 
ATOM   4602  C  CB  . GLU E  1 21  ? 57.531  -40.227 12.068 1.00 25.51  ? 21   GLU E CB  1 
ATOM   4603  C  CG  . GLU E  1 21  ? 58.561  -40.677 11.030 1.00 38.80  ? 21   GLU E CG  1 
ATOM   4604  C  CD  . GLU E  1 21  ? 59.564  -41.597 11.735 1.00 49.74  ? 21   GLU E CD  1 
ATOM   4605  O  OE1 . GLU E  1 21  ? 60.435  -41.066 12.451 1.00 52.99  ? 21   GLU E OE1 1 
ATOM   4606  O  OE2 . GLU E  1 21  ? 59.438  -42.828 11.587 1.00 57.53  ? 21   GLU E OE2 1 
ATOM   4607  N  N   . GLN E  1 22  ? 56.500  -38.812 9.180  1.00 25.77  ? 22   GLN E N   1 
ATOM   4608  C  CA  . GLN E  1 22  ? 56.073  -39.072 7.814  1.00 22.77  ? 22   GLN E CA  1 
ATOM   4609  C  C   . GLN E  1 22  ? 57.297  -39.222 6.903  1.00 26.68  ? 22   GLN E C   1 
ATOM   4610  O  O   . GLN E  1 22  ? 57.875  -38.217 6.493  1.00 26.24  ? 22   GLN E O   1 
ATOM   4611  C  CB  . GLN E  1 22  ? 55.196  -37.934 7.334  1.00 23.42  ? 22   GLN E CB  1 
ATOM   4612  C  CG  . GLN E  1 22  ? 54.486  -38.268 6.028  1.00 24.67  ? 22   GLN E CG  1 
ATOM   4613  C  CD  . GLN E  1 22  ? 53.636  -37.119 5.564  1.00 24.87  ? 22   GLN E CD  1 
ATOM   4614  O  OE1 . GLN E  1 22  ? 53.851  -35.965 5.957  1.00 26.77  ? 22   GLN E OE1 1 
ATOM   4615  N  NE2 . GLN E  1 22  ? 52.665  -37.425 4.690  1.00 26.16  ? 22   GLN E NE2 1 
ATOM   4616  N  N   . LYS E  1 23  ? 57.631  -40.481 6.631  1.00 29.36  ? 23   LYS E N   1 
ATOM   4617  C  CA  . LYS E  1 23  ? 58.878  -40.752 5.913  1.00 35.38  ? 23   LYS E CA  1 
ATOM   4618  C  C   . LYS E  1 23  ? 58.876  -40.180 4.507  1.00 33.35  ? 23   LYS E C   1 
ATOM   4619  O  O   . LYS E  1 23  ? 59.912  -39.701 4.035  1.00 31.51  ? 23   LYS E O   1 
ATOM   4620  C  CB  . LYS E  1 23  ? 59.125  -42.268 5.878  1.00 38.49  ? 23   LYS E CB  1 
ATOM   4621  C  CG  . LYS E  1 23  ? 59.466  -42.784 7.279  1.00 59.11  ? 23   LYS E CG  1 
ATOM   4622  C  CD  . LYS E  1 23  ? 58.440  -43.802 7.750  1.00 72.46  ? 23   LYS E CD  1 
ATOM   4623  C  CE  . LYS E  1 23  ? 58.187  -43.689 9.245  1.00 76.62  ? 23   LYS E CE  1 
ATOM   4624  N  NZ  . LYS E  1 23  ? 58.336  -45.011 9.933  1.00 100.25 ? 23   LYS E NZ  1 
ATOM   4625  N  N   . GLU E  1 24  ? 57.728  -40.224 3.861  1.00 30.60  ? 24   GLU E N   1 
ATOM   4626  C  CA  . GLU E  1 24  ? 57.570  -39.687 2.512  1.00 27.52  ? 24   GLU E CA  1 
ATOM   4627  C  C   . GLU E  1 24  ? 56.423  -38.704 2.449  1.00 29.13  ? 24   GLU E C   1 
ATOM   4628  O  O   . GLU E  1 24  ? 55.350  -38.942 3.018  1.00 29.00  ? 24   GLU E O   1 
ATOM   4629  C  CB  . GLU E  1 24  ? 57.312  -40.855 1.553  1.00 34.41  ? 24   GLU E CB  1 
ATOM   4630  C  CG  . GLU E  1 24  ? 58.191  -42.070 1.786  1.00 42.27  ? 24   GLU E CG  1 
ATOM   4631  C  CD  . GLU E  1 24  ? 59.658  -41.820 1.491  1.00 55.58  ? 24   GLU E CD  1 
ATOM   4632  O  OE1 . GLU E  1 24  ? 60.519  -42.469 2.124  1.00 77.08  ? 24   GLU E OE1 1 
ATOM   4633  O  OE2 . GLU E  1 24  ? 59.963  -40.973 0.627  1.00 60.66  ? 24   GLU E OE2 1 
ATOM   4634  N  N   . SER E  1 25  ? 56.556  -37.589 1.747  1.00 24.85  ? 25   SER E N   1 
ATOM   4635  C  CA  . SER E  1 25  ? 55.536  -36.561 1.701  1.00 27.53  ? 25   SER E CA  1 
ATOM   4636  C  C   . SER E  1 25  ? 54.239  -37.115 1.131  1.00 28.52  ? 25   SER E C   1 
ATOM   4637  O  O   . SER E  1 25  ? 53.160  -36.571 1.366  1.00 27.89  ? 25   SER E O   1 
ATOM   4638  C  CB  . SER E  1 25  ? 55.988  -35.355 0.870  1.00 33.90  ? 25   SER E CB  1 
ATOM   4639  O  OG  . SER E  1 25  ? 56.180  -35.702 -0.491 1.00 31.61  ? 25   SER E OG  1 
ATOM   4640  N  N   . ASN E  1 26  ? 54.327  -38.202 0.366  1.00 29.96  ? 26   ASN E N   1 
ATOM   4641  C  CA  . ASN E  1 26  ? 53.064  -38.739 -0.163 1.00 29.49  ? 26   ASN E CA  1 
ATOM   4642  C  C   . ASN E  1 26  ? 52.714  -40.029 0.554  1.00 27.71  ? 26   ASN E C   1 
ATOM   4643  O  O   . ASN E  1 26  ? 51.884  -40.812 0.081  1.00 42.36  ? 26   ASN E O   1 
ATOM   4644  C  CB  . ASN E  1 26  ? 53.165  -38.887 -1.685 1.00 28.81  ? 26   ASN E CB  1 
ATOM   4645  C  CG  . ASN E  1 26  ? 54.172  -39.927 -2.127 1.00 30.74  ? 26   ASN E CG  1 
ATOM   4646  O  OD1 . ASN E  1 26  ? 55.171  -40.174 -1.451 1.00 31.24  ? 26   ASN E OD1 1 
ATOM   4647  N  ND2 . ASN E  1 26  ? 53.936  -40.564 -3.282 1.00 32.61  ? 26   ASN E ND2 1 
ATOM   4648  N  N   . GLY E  1 27  ? 53.318  -40.306 1.699  1.00 23.99  ? 27   GLY E N   1 
ATOM   4649  C  CA  . GLY E  1 27  ? 53.066  -41.542 2.430  1.00 27.74  ? 27   GLY E CA  1 
ATOM   4650  C  C   . GLY E  1 27  ? 52.282  -41.301 3.726  1.00 26.73  ? 27   GLY E C   1 
ATOM   4651  O  O   . GLY E  1 27  ? 51.914  -40.170 4.032  1.00 27.97  ? 27   GLY E O   1 
ATOM   4652  N  N   . PRO E  1 28  ? 52.011  -42.362 4.473  1.00 30.62  ? 28   PRO E N   1 
ATOM   4653  C  CA  . PRO E  1 28  ? 51.273  -42.255 5.736  1.00 32.59  ? 28   PRO E CA  1 
ATOM   4654  C  C   . PRO E  1 28  ? 52.085  -41.619 6.870  1.00 28.26  ? 28   PRO E C   1 
ATOM   4655  O  O   . PRO E  1 28  ? 53.306  -41.680 6.889  1.00 26.04  ? 28   PRO E O   1 
ATOM   4656  C  CB  . PRO E  1 28  ? 50.983  -43.700 6.147  1.00 34.57  ? 28   PRO E CB  1 
ATOM   4657  C  CG  . PRO E  1 28  ? 51.339  -44.535 4.967  1.00 42.93  ? 28   PRO E CG  1 
ATOM   4658  C  CD  . PRO E  1 28  ? 52.357  -43.764 4.170  1.00 33.60  ? 28   PRO E CD  1 
ATOM   4659  N  N   . VAL E  1 29  ? 51.319  -41.053 7.792  1.00 26.01  ? 29   VAL E N   1 
ATOM   4660  C  CA  . VAL E  1 29  ? 51.816  -40.447 9.022  1.00 25.69  ? 29   VAL E CA  1 
ATOM   4661  C  C   . VAL E  1 29  ? 51.648  -41.463 10.159 1.00 28.45  ? 29   VAL E C   1 
ATOM   4662  O  O   . VAL E  1 29  ? 50.524  -41.942 10.365 1.00 24.28  ? 29   VAL E O   1 
ATOM   4663  C  CB  . VAL E  1 29  ? 51.092  -39.132 9.329  1.00 24.44  ? 29   VAL E CB  1 
ATOM   4664  C  CG1 . VAL E  1 29  ? 51.626  -38.498 10.618 1.00 22.19  ? 29   VAL E CG1 1 
ATOM   4665  C  CG2 . VAL E  1 29  ? 51.212  -38.104 8.201  1.00 20.84  ? 29   VAL E CG2 1 
ATOM   4666  N  N   . LYS E  1 30  ? 52.722  -41.790 10.862 1.00 24.68  ? 30   LYS E N   1 
ATOM   4667  C  CA  . LYS E  1 30  ? 52.713  -42.611 12.073 1.00 23.78  ? 30   LYS E CA  1 
ATOM   4668  C  C   . LYS E  1 30  ? 52.516  -41.685 13.273 1.00 29.03  ? 30   LYS E C   1 
ATOM   4669  O  O   . LYS E  1 30  ? 53.267  -40.702 13.336 1.00 25.49  ? 30   LYS E O   1 
ATOM   4670  C  CB  . LYS E  1 30  ? 54.005  -43.377 12.278 1.00 24.06  ? 30   LYS E CB  1 
ATOM   4671  C  CG  . LYS E  1 30  ? 54.209  -44.541 11.318 1.00 35.90  ? 30   LYS E CG  1 
ATOM   4672  C  CD  . LYS E  1 30  ? 55.594  -45.147 11.557 1.00 53.03  ? 30   LYS E CD  1 
ATOM   4673  C  CE  . LYS E  1 30  ? 56.164  -44.625 12.874 1.00 70.68  ? 30   LYS E CE  1 
ATOM   4674  N  NZ  . LYS E  1 30  ? 57.534  -44.051 12.699 1.00 93.79  ? 30   LYS E NZ  1 
ATOM   4675  N  N   . VAL E  1 31  ? 51.553  -41.982 14.133 1.00 19.51  ? 31   VAL E N   1 
ATOM   4676  C  CA  . VAL E  1 31  ? 51.252  -41.144 15.289 1.00 20.58  ? 31   VAL E CA  1 
ATOM   4677  C  C   . VAL E  1 31  ? 51.458  -41.974 16.547 1.00 26.41  ? 31   VAL E C   1 
ATOM   4678  O  O   . VAL E  1 31  ? 50.759  -42.985 16.688 1.00 24.40  ? 31   VAL E O   1 
ATOM   4679  C  CB  . VAL E  1 31  ? 49.820  -40.614 15.228 1.00 21.92  ? 31   VAL E CB  1 
ATOM   4680  C  CG1 . VAL E  1 31  ? 49.527  -39.700 16.413 1.00 21.99  ? 31   VAL E CG1 1 
ATOM   4681  C  CG2 . VAL E  1 31  ? 49.561  -39.821 13.942 1.00 26.04  ? 31   VAL E CG2 1 
ATOM   4682  N  N   . TRP E  1 32  ? 52.370  -41.631 17.458 1.00 20.33  ? 32   TRP E N   1 
ATOM   4683  C  CA  . TRP E  1 32  ? 52.516  -42.526 18.619 1.00 19.24  ? 32   TRP E CA  1 
ATOM   4684  C  C   . TRP E  1 32  ? 53.019  -41.738 19.812 1.00 22.38  ? 32   TRP E C   1 
ATOM   4685  O  O   . TRP E  1 32  ? 53.625  -40.674 19.682 1.00 23.70  ? 32   TRP E O   1 
ATOM   4686  C  CB  . TRP E  1 32  ? 53.488  -43.686 18.386 1.00 28.64  ? 32   TRP E CB  1 
ATOM   4687  C  CG  . TRP E  1 32  ? 54.925  -43.260 18.449 1.00 28.56  ? 32   TRP E CG  1 
ATOM   4688  C  CD1 . TRP E  1 32  ? 55.805  -43.463 19.478 1.00 26.85  ? 32   TRP E CD1 1 
ATOM   4689  C  CD2 . TRP E  1 32  ? 55.645  -42.555 17.430 1.00 26.86  ? 32   TRP E CD2 1 
ATOM   4690  N  NE1 . TRP E  1 32  ? 57.020  -42.923 19.153 1.00 37.36  ? 32   TRP E NE1 1 
ATOM   4691  C  CE2 . TRP E  1 32  ? 56.958  -42.358 17.905 1.00 31.00  ? 32   TRP E CE2 1 
ATOM   4692  C  CE3 . TRP E  1 32  ? 55.336  -42.059 16.167 1.00 30.23  ? 32   TRP E CE3 1 
ATOM   4693  C  CZ2 . TRP E  1 32  ? 57.936  -41.700 17.169 1.00 31.53  ? 32   TRP E CZ2 1 
ATOM   4694  C  CZ3 . TRP E  1 32  ? 56.316  -41.408 15.442 1.00 31.81  ? 32   TRP E CZ3 1 
ATOM   4695  C  CH2 . TRP E  1 32  ? 57.614  -41.220 15.923 1.00 26.88  ? 32   TRP E CH2 1 
ATOM   4696  N  N   . GLY E  1 33  ? 52.723  -42.294 20.980 1.00 20.24  ? 33   GLY E N   1 
ATOM   4697  C  CA  . GLY E  1 33  ? 53.082  -41.579 22.197 1.00 22.84  ? 33   GLY E CA  1 
ATOM   4698  C  C   . GLY E  1 33  ? 52.239  -42.060 23.360 1.00 25.63  ? 33   GLY E C   1 
ATOM   4699  O  O   . GLY E  1 33  ? 51.641  -43.130 23.302 1.00 30.16  ? 33   GLY E O   1 
ATOM   4700  N  N   . SER E  1 34  ? 52.228  -41.268 24.416 1.00 24.49  ? 34   SER E N   1 
ATOM   4701  C  CA  . SER E  1 34  ? 51.466  -41.704 25.594 1.00 29.53  ? 34   SER E CA  1 
ATOM   4702  C  C   . SER E  1 34  ? 50.691  -40.523 26.162 1.00 30.83  ? 34   SER E C   1 
ATOM   4703  O  O   . SER E  1 34  ? 51.166  -39.380 26.174 1.00 31.25  ? 34   SER E O   1 
ATOM   4704  C  CB  . SER E  1 34  ? 52.438  -42.326 26.595 1.00 32.55  ? 34   SER E CB  1 
ATOM   4705  O  OG  . SER E  1 34  ? 52.252  -41.854 27.908 1.00 61.63  ? 34   SER E OG  1 
ATOM   4706  N  N   . ILE E  1 35  ? 49.484  -40.790 26.631 1.00 21.42  ? 35   ILE E N   1 
ATOM   4707  C  CA  . ILE E  1 35  ? 48.672  -39.774 27.300 1.00 21.09  ? 35   ILE E CA  1 
ATOM   4708  C  C   . ILE E  1 35  ? 48.301  -40.331 28.681 1.00 27.81  ? 35   ILE E C   1 
ATOM   4709  O  O   . ILE E  1 35  ? 47.798  -41.456 28.759 1.00 27.11  ? 35   ILE E O   1 
ATOM   4710  C  CB  . ILE E  1 35  ? 47.431  -39.406 26.502 1.00 21.96  ? 35   ILE E CB  1 
ATOM   4711  C  CG1 . ILE E  1 35  ? 47.721  -38.968 25.040 1.00 23.42  ? 35   ILE E CG1 1 
ATOM   4712  C  CG2 . ILE E  1 35  ? 46.653  -38.309 27.205 1.00 20.29  ? 35   ILE E CG2 1 
ATOM   4713  C  CD1 . ILE E  1 35  ? 46.452  -38.894 24.198 1.00 23.64  ? 35   ILE E CD1 1 
ATOM   4714  N  N   . LYS E  1 36  ? 48.573  -39.585 29.742 1.00 25.64  ? 36   LYS E N   1 
ATOM   4715  C  CA  . LYS E  1 36  ? 48.221  -40.102 31.072 1.00 25.63  ? 36   LYS E CA  1 
ATOM   4716  C  C   . LYS E  1 36  ? 47.124  -39.280 31.712 1.00 27.06  ? 36   LYS E C   1 
ATOM   4717  O  O   . LYS E  1 36  ? 46.688  -38.237 31.203 1.00 24.21  ? 36   LYS E O   1 
ATOM   4718  C  CB  . LYS E  1 36  ? 49.501  -40.166 31.913 1.00 26.92  ? 36   LYS E CB  1 
ATOM   4719  C  CG  . LYS E  1 36  ? 50.175  -38.818 32.147 1.00 33.80  ? 36   LYS E CG  1 
ATOM   4720  C  CD  . LYS E  1 36  ? 51.655  -39.088 32.448 1.00 46.14  ? 36   LYS E CD  1 
ATOM   4721  C  CE  . LYS E  1 36  ? 52.312  -37.960 33.224 1.00 48.51  ? 36   LYS E CE  1 
ATOM   4722  N  NZ  . LYS E  1 36  ? 53.786  -38.200 33.346 1.00 44.60  ? 36   LYS E NZ  1 
ATOM   4723  N  N   . GLY E  1 37  ? 46.608  -39.722 32.865 1.00 24.12  ? 37   GLY E N   1 
ATOM   4724  C  CA  . GLY E  1 37  ? 45.573  -38.936 33.518 1.00 21.72  ? 37   GLY E CA  1 
ATOM   4725  C  C   . GLY E  1 37  ? 44.167  -39.170 33.011 1.00 18.89  ? 37   GLY E C   1 
ATOM   4726  O  O   . GLY E  1 37  ? 43.269  -38.354 33.228 1.00 24.65  ? 37   GLY E O   1 
ATOM   4727  N  N   . LEU E  1 38  ? 43.921  -40.267 32.305 1.00 23.64  ? 38   LEU E N   1 
ATOM   4728  C  CA  . LEU E  1 38  ? 42.644  -40.469 31.656 1.00 21.98  ? 38   LEU E CA  1 
ATOM   4729  C  C   . LEU E  1 38  ? 41.753  -41.487 32.354 1.00 22.29  ? 38   LEU E C   1 
ATOM   4730  O  O   . LEU E  1 38  ? 42.288  -42.430 32.934 1.00 26.76  ? 38   LEU E O   1 
ATOM   4731  C  CB  . LEU E  1 38  ? 42.923  -41.006 30.232 1.00 26.02  ? 38   LEU E CB  1 
ATOM   4732  C  CG  . LEU E  1 38  ? 43.509  -39.988 29.231 1.00 19.68  ? 38   LEU E CG  1 
ATOM   4733  C  CD1 . LEU E  1 38  ? 43.934  -40.716 27.965 1.00 25.49  ? 38   LEU E CD1 1 
ATOM   4734  C  CD2 . LEU E  1 38  ? 42.503  -38.909 28.918 1.00 21.18  ? 38   LEU E CD2 1 
ATOM   4735  N  N   . THR E  1 39  ? 40.444  -41.336 32.271 1.00 26.97  ? 39   THR E N   1 
ATOM   4736  C  CA  . THR E  1 39  ? 39.612  -42.477 32.706 1.00 31.46  ? 39   THR E CA  1 
ATOM   4737  C  C   . THR E  1 39  ? 39.781  -43.650 31.760 1.00 35.76  ? 39   THR E C   1 
ATOM   4738  O  O   . THR E  1 39  ? 40.007  -43.476 30.560 1.00 30.49  ? 39   THR E O   1 
ATOM   4739  C  CB  . THR E  1 39  ? 38.150  -42.035 32.761 1.00 27.50  ? 39   THR E CB  1 
ATOM   4740  O  OG1 . THR E  1 39  ? 37.750  -41.639 31.437 1.00 33.60  ? 39   THR E OG1 1 
ATOM   4741  C  CG2 . THR E  1 39  ? 38.000  -40.798 33.641 1.00 36.24  ? 39   THR E CG2 1 
ATOM   4742  N  N   . GLU E  1 40  ? 39.671  -44.880 32.259 1.00 33.66  ? 40   GLU E N   1 
ATOM   4743  C  CA  . GLU E  1 40  ? 39.782  -46.082 31.438 1.00 27.42  ? 40   GLU E CA  1 
ATOM   4744  C  C   . GLU E  1 40  ? 38.726  -46.086 30.350 1.00 26.92  ? 40   GLU E C   1 
ATOM   4745  O  O   . GLU E  1 40  ? 37.572  -45.666 30.537 1.00 32.03  ? 40   GLU E O   1 
ATOM   4746  C  CB  . GLU E  1 40  ? 39.665  -47.313 32.356 1.00 33.10  ? 40   GLU E CB  1 
ATOM   4747  C  CG  . GLU E  1 40  ? 39.688  -48.650 31.646 1.00 35.13  ? 40   GLU E CG  1 
ATOM   4748  C  CD  . GLU E  1 40  ? 39.370  -49.817 32.575 1.00 52.70  ? 40   GLU E CD  1 
ATOM   4749  O  OE1 . GLU E  1 40  ? 39.356  -50.969 32.086 1.00 57.79  ? 40   GLU E OE1 1 
ATOM   4750  O  OE2 . GLU E  1 40  ? 39.137  -49.587 33.784 1.00 45.60  ? 40   GLU E OE2 1 
ATOM   4751  N  N   . GLY E  1 41  ? 39.054  -46.532 29.148 1.00 28.56  ? 41   GLY E N   1 
ATOM   4752  C  CA  . GLY E  1 41  ? 38.118  -46.577 28.041 1.00 26.67  ? 41   GLY E CA  1 
ATOM   4753  C  C   . GLY E  1 41  ? 38.540  -45.685 26.874 1.00 29.51  ? 41   GLY E C   1 
ATOM   4754  O  O   . GLY E  1 41  ? 39.670  -45.191 26.808 1.00 26.32  ? 41   GLY E O   1 
ATOM   4755  N  N   . LEU E  1 42  ? 37.610  -45.502 25.946 1.00 25.34  ? 42   LEU E N   1 
ATOM   4756  C  CA  . LEU E  1 42  ? 37.779  -44.777 24.711 1.00 22.54  ? 42   LEU E CA  1 
ATOM   4757  C  C   . LEU E  1 42  ? 37.694  -43.273 24.906 1.00 27.63  ? 42   LEU E C   1 
ATOM   4758  O  O   . LEU E  1 42  ? 36.782  -42.814 25.588 1.00 25.14  ? 42   LEU E O   1 
ATOM   4759  C  CB  . LEU E  1 42  ? 36.671  -45.134 23.696 1.00 20.52  ? 42   LEU E CB  1 
ATOM   4760  C  CG  . LEU E  1 42  ? 36.675  -46.617 23.306 1.00 27.23  ? 42   LEU E CG  1 
ATOM   4761  C  CD1 . LEU E  1 42  ? 35.416  -46.997 22.543 1.00 24.98  ? 42   LEU E CD1 1 
ATOM   4762  C  CD2 . LEU E  1 42  ? 37.944  -46.898 22.491 1.00 32.96  ? 42   LEU E CD2 1 
ATOM   4763  N  N   . HIS E  1 43  ? 38.614  -42.555 24.266 1.00 20.23  ? 43   HIS E N   1 
ATOM   4764  C  CA  . HIS E  1 43  ? 38.555  -41.099 24.226 1.00 21.17  ? 43   HIS E CA  1 
ATOM   4765  C  C   . HIS E  1 43  ? 38.763  -40.576 22.800 1.00 23.04  ? 43   HIS E C   1 
ATOM   4766  O  O   . HIS E  1 43  ? 39.707  -40.986 22.116 1.00 18.90  ? 43   HIS E O   1 
ATOM   4767  C  CB  . HIS E  1 43  ? 39.653  -40.505 25.125 1.00 22.41  ? 43   HIS E CB  1 
ATOM   4768  C  CG  . HIS E  1 43  ? 39.444  -40.914 26.567 1.00 26.41  ? 43   HIS E CG  1 
ATOM   4769  N  ND1 . HIS E  1 43  ? 38.783  -40.092 27.465 1.00 29.65  ? 43   HIS E ND1 1 
ATOM   4770  C  CD2 . HIS E  1 43  ? 39.804  -42.021 27.250 1.00 25.74  ? 43   HIS E CD2 1 
ATOM   4771  C  CE1 . HIS E  1 43  ? 38.748  -40.696 28.651 1.00 25.32  ? 43   HIS E CE1 1 
ATOM   4772  N  NE2 . HIS E  1 43  ? 39.353  -41.866 28.546 1.00 25.93  ? 43   HIS E NE2 1 
ATOM   4773  N  N   . GLY E  1 44  ? 37.893  -39.683 22.367 1.00 22.66  ? 44   GLY E N   1 
ATOM   4774  C  CA  . GLY E  1 44  ? 38.019  -39.087 21.030 1.00 21.47  ? 44   GLY E CA  1 
ATOM   4775  C  C   . GLY E  1 44  ? 39.366  -38.383 20.885 1.00 21.98  ? 44   GLY E C   1 
ATOM   4776  O  O   . GLY E  1 44  ? 39.912  -37.835 21.849 1.00 18.49  ? 44   GLY E O   1 
ATOM   4777  N  N   . PHE E  1 45  ? 39.885  -38.397 19.652 1.00 20.81  ? 45   PHE E N   1 
ATOM   4778  C  CA  . PHE E  1 45  ? 41.239  -37.910 19.371 1.00 17.62  ? 45   PHE E CA  1 
ATOM   4779  C  C   . PHE E  1 45  ? 41.277  -37.274 18.000 1.00 18.35  ? 45   PHE E C   1 
ATOM   4780  O  O   . PHE E  1 45  ? 41.120  -37.992 17.010 1.00 20.82  ? 45   PHE E O   1 
ATOM   4781  C  CB  . PHE E  1 45  ? 42.151  -39.136 19.414 1.00 19.94  ? 45   PHE E CB  1 
ATOM   4782  C  CG  . PHE E  1 45  ? 43.662  -38.911 19.404 1.00 21.51  ? 45   PHE E CG  1 
ATOM   4783  C  CD1 . PHE E  1 45  ? 44.271  -38.243 20.461 1.00 23.07  ? 45   PHE E CD1 1 
ATOM   4784  C  CD2 . PHE E  1 45  ? 44.421  -39.394 18.358 1.00 21.26  ? 45   PHE E CD2 1 
ATOM   4785  C  CE1 . PHE E  1 45  ? 45.652  -38.049 20.456 1.00 23.29  ? 45   PHE E CE1 1 
ATOM   4786  C  CE2 . PHE E  1 45  ? 45.795  -39.212 18.340 1.00 21.37  ? 45   PHE E CE2 1 
ATOM   4787  C  CZ  . PHE E  1 45  ? 46.392  -38.574 19.413 1.00 21.53  ? 45   PHE E CZ  1 
ATOM   4788  N  N   . HIS E  1 46  ? 41.409  -35.966 17.875 1.00 19.60  ? 46   HIS E N   1 
ATOM   4789  C  CA  . HIS E  1 46  ? 41.266  -35.305 16.582 1.00 22.14  ? 46   HIS E CA  1 
ATOM   4790  C  C   . HIS E  1 46  ? 42.251  -34.132 16.454 1.00 22.98  ? 46   HIS E C   1 
ATOM   4791  O  O   . HIS E  1 46  ? 42.642  -33.520 17.441 1.00 20.19  ? 46   HIS E O   1 
ATOM   4792  C  CB  . HIS E  1 46  ? 39.887  -34.671 16.314 1.00 20.93  ? 46   HIS E CB  1 
ATOM   4793  C  CG  . HIS E  1 46  ? 38.764  -35.470 16.922 1.00 19.27  ? 46   HIS E CG  1 
ATOM   4794  N  ND1 . HIS E  1 46  ? 38.109  -35.078 18.050 1.00 19.76  ? 46   HIS E ND1 1 
ATOM   4795  C  CD2 . HIS E  1 46  ? 38.251  -36.674 16.559 1.00 24.59  ? 46   HIS E CD2 1 
ATOM   4796  C  CE1 . HIS E  1 46  ? 37.194  -35.982 18.353 1.00 21.35  ? 46   HIS E CE1 1 
ATOM   4797  N  NE2 . HIS E  1 46  ? 37.253  -36.959 17.475 1.00 25.27  ? 46   HIS E NE2 1 
ATOM   4798  N  N   . VAL E  1 47  ? 42.570  -33.838 15.200 1.00 18.56  ? 47   VAL E N   1 
ATOM   4799  C  CA  . VAL E  1 47  ? 43.207  -32.551 14.903 1.00 16.08  ? 47   VAL E CA  1 
ATOM   4800  C  C   . VAL E  1 47  ? 42.113  -31.524 14.666 1.00 18.79  ? 47   VAL E C   1 
ATOM   4801  O  O   . VAL E  1 47  ? 41.250  -31.721 13.783 1.00 19.95  ? 47   VAL E O   1 
ATOM   4802  C  CB  . VAL E  1 47  ? 44.077  -32.671 13.633 1.00 17.71  ? 47   VAL E CB  1 
ATOM   4803  C  CG1 . VAL E  1 47  ? 44.739  -31.324 13.342 1.00 20.39  ? 47   VAL E CG1 1 
ATOM   4804  C  CG2 . VAL E  1 47  ? 45.094  -33.785 13.782 1.00 21.95  ? 47   VAL E CG2 1 
ATOM   4805  N  N   . HIS E  1 48  ? 42.136  -30.459 15.425 1.00 17.23  ? 48   HIS E N   1 
ATOM   4806  C  CA  . HIS E  1 48  ? 41.224  -29.341 15.280 1.00 16.89  ? 48   HIS E CA  1 
ATOM   4807  C  C   . HIS E  1 48  ? 41.833  -28.246 14.427 1.00 25.69  ? 48   HIS E C   1 
ATOM   4808  O  O   . HIS E  1 48  ? 43.052  -28.179 14.253 1.00 24.00  ? 48   HIS E O   1 
ATOM   4809  C  CB  . HIS E  1 48  ? 40.839  -28.803 16.660 1.00 20.13  ? 48   HIS E CB  1 
ATOM   4810  C  CG  . HIS E  1 48  ? 39.880  -29.739 17.363 1.00 20.52  ? 48   HIS E CG  1 
ATOM   4811  N  ND1 . HIS E  1 48  ? 38.641  -29.338 17.788 1.00 22.54  ? 48   HIS E ND1 1 
ATOM   4812  C  CD2 . HIS E  1 48  ? 39.992  -31.036 17.725 1.00 23.38  ? 48   HIS E CD2 1 
ATOM   4813  C  CE1 . HIS E  1 48  ? 38.009  -30.340 18.384 1.00 20.65  ? 48   HIS E CE1 1 
ATOM   4814  N  NE2 . HIS E  1 48  ? 38.808  -31.395 18.353 1.00 20.84  ? 48   HIS E NE2 1 
ATOM   4815  N  N   . GLU E  1 49  ? 41.005  -27.374 13.881 1.00 24.24  ? 49   GLU E N   1 
ATOM   4816  C  CA  . GLU E  1 49  ? 41.462  -26.420 12.886 1.00 24.42  ? 49   GLU E CA  1 
ATOM   4817  C  C   . GLU E  1 49  ? 42.474  -25.363 13.323 1.00 22.50  ? 49   GLU E C   1 
ATOM   4818  O  O   . GLU E  1 49  ? 43.409  -25.099 12.544 1.00 24.51  ? 49   GLU E O   1 
ATOM   4819  C  CB  . GLU E  1 49  ? 40.202  -25.693 12.337 1.00 22.60  ? 49   GLU E CB  1 
ATOM   4820  C  CG  . GLU E  1 49  ? 40.508  -24.952 11.040 1.00 28.36  ? 49   GLU E CG  1 
ATOM   4821  C  CD  . GLU E  1 49  ? 39.279  -24.238 10.497 1.00 35.21  ? 49   GLU E CD  1 
ATOM   4822  O  OE1 . GLU E  1 49  ? 39.442  -23.492 9.512  1.00 35.93  ? 49   GLU E OE1 1 
ATOM   4823  O  OE2 . GLU E  1 49  ? 38.182  -24.415 11.058 1.00 31.58  ? 49   GLU E OE2 1 
ATOM   4824  N  N   . PHE E  1 50  ? 42.332  -24.745 14.488 1.00 20.94  ? 50   PHE E N   1 
ATOM   4825  C  CA  . PHE E  1 50  ? 43.233  -23.647 14.858 1.00 22.97  ? 50   PHE E CA  1 
ATOM   4826  C  C   . PHE E  1 50  ? 44.251  -24.017 15.920 1.00 22.97  ? 50   PHE E C   1 
ATOM   4827  O  O   . PHE E  1 50  ? 43.944  -24.668 16.920 1.00 22.63  ? 50   PHE E O   1 
ATOM   4828  C  CB  . PHE E  1 50  ? 42.413  -22.440 15.354 1.00 22.62  ? 50   PHE E CB  1 
ATOM   4829  C  CG  . PHE E  1 50  ? 41.362  -22.067 14.309 1.00 31.77  ? 50   PHE E CG  1 
ATOM   4830  C  CD1 . PHE E  1 50  ? 41.752  -21.776 13.015 1.00 25.36  ? 50   PHE E CD1 1 
ATOM   4831  C  CD2 . PHE E  1 50  ? 40.024  -22.035 14.672 1.00 33.77  ? 50   PHE E CD2 1 
ATOM   4832  C  CE1 . PHE E  1 50  ? 40.781  -21.471 12.072 1.00 30.99  ? 50   PHE E CE1 1 
ATOM   4833  C  CE2 . PHE E  1 50  ? 39.052  -21.722 13.730 1.00 32.27  ? 50   PHE E CE2 1 
ATOM   4834  C  CZ  . PHE E  1 50  ? 39.454  -21.442 12.440 1.00 31.22  ? 50   PHE E CZ  1 
ATOM   4835  N  N   . GLY E  1 51  ? 45.501  -23.577 15.707 1.00 22.74  ? 51   GLY E N   1 
ATOM   4836  C  CA  . GLY E  1 51  ? 46.548  -23.781 16.722 1.00 20.17  ? 51   GLY E CA  1 
ATOM   4837  C  C   . GLY E  1 51  ? 46.478  -22.607 17.701 1.00 28.16  ? 51   GLY E C   1 
ATOM   4838  O  O   . GLY E  1 51  ? 47.447  -21.876 17.958 1.00 23.00  ? 51   GLY E O   1 
ATOM   4839  N  N   . ASP E  1 52  ? 45.273  -22.417 18.240 1.00 24.15  ? 52   ASP E N   1 
ATOM   4840  C  CA  . ASP E  1 52  ? 44.978  -21.245 19.080 1.00 22.49  ? 52   ASP E CA  1 
ATOM   4841  C  C   . ASP E  1 52  ? 44.604  -21.678 20.492 1.00 23.95  ? 52   ASP E C   1 
ATOM   4842  O  O   . ASP E  1 52  ? 43.527  -22.247 20.701 1.00 24.93  ? 52   ASP E O   1 
ATOM   4843  C  CB  . ASP E  1 52  ? 43.854  -20.430 18.452 1.00 19.51  ? 52   ASP E CB  1 
ATOM   4844  C  CG  . ASP E  1 52  ? 43.566  -19.140 19.196 1.00 26.22  ? 52   ASP E CG  1 
ATOM   4845  O  OD1 . ASP E  1 52  ? 43.014  -18.205 18.558 1.00 26.16  ? 52   ASP E OD1 1 
ATOM   4846  O  OD2 . ASP E  1 52  ? 43.840  -18.988 20.403 1.00 25.81  ? 52   ASP E OD2 1 
ATOM   4847  N  N   . ASN E  1 53  ? 45.484  -21.408 21.448 1.00 20.81  ? 53   ASN E N   1 
ATOM   4848  C  CA  . ASN E  1 53  ? 45.238  -21.799 22.834 1.00 23.62  ? 53   ASN E CA  1 
ATOM   4849  C  C   . ASN E  1 53  ? 44.874  -20.594 23.699 1.00 23.46  ? 53   ASN E C   1 
ATOM   4850  O  O   . ASN E  1 53  ? 44.999  -20.690 24.929 1.00 23.87  ? 53   ASN E O   1 
ATOM   4851  C  CB  . ASN E  1 53  ? 46.471  -22.481 23.430 1.00 23.49  ? 53   ASN E CB  1 
ATOM   4852  C  CG  . ASN E  1 53  ? 46.156  -23.237 24.708 1.00 34.13  ? 53   ASN E CG  1 
ATOM   4853  O  OD1 . ASN E  1 53  ? 46.835  -23.133 25.729 1.00 39.06  ? 53   ASN E OD1 1 
ATOM   4854  N  ND2 . ASN E  1 53  ? 45.106  -24.053 24.679 1.00 41.25  ? 53   ASN E ND2 1 
ATOM   4855  N  N   . THR E  1 54  ? 44.462  -19.496 23.074 1.00 21.57  ? 54   THR E N   1 
ATOM   4856  C  CA  . THR E  1 54  ? 44.293  -18.288 23.878 1.00 26.29  ? 54   THR E CA  1 
ATOM   4857  C  C   . THR E  1 54  ? 43.144  -18.455 24.871 1.00 36.82  ? 54   THR E C   1 
ATOM   4858  O  O   . THR E  1 54  ? 43.138  -17.823 25.934 1.00 32.51  ? 54   THR E O   1 
ATOM   4859  C  CB  . THR E  1 54  ? 44.035  -17.034 23.026 1.00 26.07  ? 54   THR E CB  1 
ATOM   4860  O  OG1 . THR E  1 54  ? 42.927  -17.290 22.146 1.00 29.02  ? 54   THR E OG1 1 
ATOM   4861  C  CG2 . THR E  1 54  ? 45.237  -16.700 22.164 1.00 26.09  ? 54   THR E CG2 1 
ATOM   4862  N  N   . ALA E  1 55  ? 42.162  -19.293 24.550 1.00 26.74  ? 55   ALA E N   1 
ATOM   4863  C  CA  . ALA E  1 55  ? 41.108  -19.572 25.532 1.00 33.32  ? 55   ALA E CA  1 
ATOM   4864  C  C   . ALA E  1 55  ? 41.102  -21.055 25.869 1.00 32.59  ? 55   ALA E C   1 
ATOM   4865  O  O   . ALA E  1 55  ? 40.055  -21.706 25.910 1.00 44.22  ? 55   ALA E O   1 
ATOM   4866  C  CB  . ALA E  1 55  ? 39.735  -19.151 25.025 1.00 38.73  ? 55   ALA E CB  1 
ATOM   4867  N  N   . GLY E  1 56  ? 42.286  -21.596 26.096 1.00 24.82  ? 56   GLY E N   1 
ATOM   4868  C  CA  . GLY E  1 56  ? 42.430  -23.027 26.331 1.00 25.17  ? 56   GLY E CA  1 
ATOM   4869  C  C   . GLY E  1 56  ? 42.011  -23.817 25.104 1.00 25.80  ? 56   GLY E C   1 
ATOM   4870  O  O   . GLY E  1 56  ? 41.997  -23.303 23.987 1.00 28.99  ? 56   GLY E O   1 
ATOM   4871  N  N   . CYS E  1 57  ? 41.633  -25.086 25.303 1.00 27.29  ? 57   CYS E N   1 
ATOM   4872  C  CA  . CYS E  1 57  ? 41.293  -25.889 24.124 1.00 28.37  ? 57   CYS E CA  1 
ATOM   4873  C  C   . CYS E  1 57  ? 40.077  -25.360 23.382 1.00 28.59  ? 57   CYS E C   1 
ATOM   4874  O  O   . CYS E  1 57  ? 39.864  -25.696 22.214 1.00 24.72  ? 57   CYS E O   1 
ATOM   4875  C  CB  A CYS E  1 57  ? 40.944  -27.320 24.550 0.44 25.64  ? 57   CYS E CB  1 
ATOM   4876  C  CB  B CYS E  1 57  ? 41.130  -27.365 24.478 0.56 32.91  ? 57   CYS E CB  1 
ATOM   4877  S  SG  A CYS E  1 57  ? 42.293  -28.272 25.276 0.44 40.32  ? 57   CYS E SG  1 
ATOM   4878  S  SG  B CYS E  1 57  ? 42.369  -28.037 25.599 0.56 32.56  ? 57   CYS E SG  1 
ATOM   4879  N  N   . THR E  1 58  ? 39.231  -24.541 24.012 1.00 24.74  ? 58   THR E N   1 
ATOM   4880  C  CA  . THR E  1 58  ? 38.055  -24.093 23.269 1.00 25.88  ? 58   THR E CA  1 
ATOM   4881  C  C   . THR E  1 58  ? 38.370  -23.294 22.028 1.00 27.03  ? 58   THR E C   1 
ATOM   4882  O  O   . THR E  1 58  ? 37.604  -23.286 21.062 1.00 27.54  ? 58   THR E O   1 
ATOM   4883  C  CB  . THR E  1 58  ? 37.176  -23.218 24.198 1.00 36.38  ? 58   THR E CB  1 
ATOM   4884  O  OG1 . THR E  1 58  ? 36.997  -23.897 25.447 1.00 39.93  ? 58   THR E OG1 1 
ATOM   4885  C  CG2 . THR E  1 58  ? 35.802  -23.013 23.590 1.00 31.91  ? 58   THR E CG2 1 
ATOM   4886  N  N   . SER E  1 59  ? 39.497  -22.564 22.023 1.00 21.20  ? 59   SER E N   1 
ATOM   4887  C  CA  . SER E  1 59  ? 39.806  -21.727 20.883 1.00 25.00  ? 59   SER E CA  1 
ATOM   4888  C  C   . SER E  1 59  ? 40.452  -22.497 19.736 1.00 25.11  ? 59   SER E C   1 
ATOM   4889  O  O   . SER E  1 59  ? 40.750  -21.883 18.700 1.00 26.36  ? 59   SER E O   1 
ATOM   4890  C  CB  . SER E  1 59  ? 40.698  -20.539 21.314 1.00 26.92  ? 59   SER E CB  1 
ATOM   4891  O  OG  . SER E  1 59  ? 41.634  -20.931 22.275 1.00 28.82  ? 59   SER E OG  1 
ATOM   4892  N  N   . ALA E  1 60  ? 40.639  -23.811 19.872 1.00 22.71  ? 60   ALA E N   1 
ATOM   4893  C  CA  . ALA E  1 60  ? 41.102  -24.584 18.724 1.00 21.10  ? 60   ALA E CA  1 
ATOM   4894  C  C   . ALA E  1 60  ? 40.052  -24.731 17.626 1.00 26.22  ? 60   ALA E C   1 
ATOM   4895  O  O   . ALA E  1 60  ? 40.381  -25.235 16.546 1.00 21.65  ? 60   ALA E O   1 
ATOM   4896  C  CB  . ALA E  1 60  ? 41.524  -25.995 19.147 1.00 20.57  ? 60   ALA E CB  1 
ATOM   4897  N  N   . GLY E  1 61  ? 38.805  -24.312 17.860 1.00 25.02  ? 61   GLY E N   1 
ATOM   4898  C  CA  . GLY E  1 61  ? 37.806  -24.419 16.795 1.00 19.47  ? 61   GLY E CA  1 
ATOM   4899  C  C   . GLY E  1 61  ? 37.360  -25.857 16.584 1.00 21.54  ? 61   GLY E C   1 
ATOM   4900  O  O   . GLY E  1 61  ? 37.622  -26.772 17.374 1.00 22.39  ? 61   GLY E O   1 
ATOM   4901  N  N   . PRO E  1 62  ? 36.655  -26.110 15.477 1.00 22.48  ? 62   PRO E N   1 
ATOM   4902  C  CA  . PRO E  1 62  ? 36.115  -27.465 15.215 1.00 23.33  ? 62   PRO E CA  1 
ATOM   4903  C  C   . PRO E  1 62  ? 37.159  -28.393 14.611 1.00 26.39  ? 62   PRO E C   1 
ATOM   4904  O  O   . PRO E  1 62  ? 38.335  -27.995 14.561 1.00 23.12  ? 62   PRO E O   1 
ATOM   4905  C  CB  . PRO E  1 62  ? 35.029  -27.161 14.182 1.00 26.34  ? 62   PRO E CB  1 
ATOM   4906  C  CG  . PRO E  1 62  ? 35.615  -26.010 13.398 1.00 30.74  ? 62   PRO E CG  1 
ATOM   4907  C  CD  . PRO E  1 62  ? 36.310  -25.150 14.425 1.00 25.02  ? 62   PRO E CD  1 
ATOM   4908  N  N   . HIS E  1 63  ? 36.788  -29.597 14.162 1.00 21.94  ? 63   HIS E N   1 
ATOM   4909  C  CA  . HIS E  1 63  ? 37.759  -30.520 13.587 1.00 21.48  ? 63   HIS E CA  1 
ATOM   4910  C  C   . HIS E  1 63  ? 38.315  -29.974 12.263 1.00 23.98  ? 63   HIS E C   1 
ATOM   4911  O  O   . HIS E  1 63  ? 37.557  -29.312 11.560 1.00 22.50  ? 63   HIS E O   1 
ATOM   4912  C  CB  . HIS E  1 63  ? 37.146  -31.898 13.310 1.00 22.50  ? 63   HIS E CB  1 
ATOM   4913  C  CG  . HIS E  1 63  ? 36.598  -32.546 14.553 1.00 25.00  ? 63   HIS E CG  1 
ATOM   4914  N  ND1 . HIS E  1 63  ? 35.981  -33.779 14.551 1.00 25.68  ? 63   HIS E ND1 1 
ATOM   4915  C  CD2 . HIS E  1 63  ? 36.583  -32.118 15.840 1.00 23.66  ? 63   HIS E CD2 1 
ATOM   4916  C  CE1 . HIS E  1 63  ? 35.617  -34.068 15.792 1.00 26.20  ? 63   HIS E CE1 1 
ATOM   4917  N  NE2 . HIS E  1 63  ? 35.965  -33.081 16.598 1.00 25.64  ? 63   HIS E NE2 1 
ATOM   4918  N  N   . PHE E  1 64  ? 39.579  -30.259 11.990 1.00 21.47  ? 64   PHE E N   1 
ATOM   4919  C  CA  . PHE E  1 64  ? 40.242  -29.772 10.774 1.00 20.11  ? 64   PHE E CA  1 
ATOM   4920  C  C   . PHE E  1 64  ? 39.521  -30.410 9.587  1.00 21.05  ? 64   PHE E C   1 
ATOM   4921  O  O   . PHE E  1 64  ? 39.468  -31.648 9.563  1.00 21.70  ? 64   PHE E O   1 
ATOM   4922  C  CB  . PHE E  1 64  ? 41.729  -30.124 10.798 1.00 20.38  ? 64   PHE E CB  1 
ATOM   4923  C  CG  . PHE E  1 64  ? 42.488  -29.686 9.542  1.00 20.00  ? 64   PHE E CG  1 
ATOM   4924  C  CD1 . PHE E  1 64  ? 43.427  -30.538 8.998  1.00 21.24  ? 64   PHE E CD1 1 
ATOM   4925  C  CD2 . PHE E  1 64  ? 42.214  -28.442 8.983  1.00 22.51  ? 64   PHE E CD2 1 
ATOM   4926  C  CE1 . PHE E  1 64  ? 44.123  -30.124 7.862  1.00 24.19  ? 64   PHE E CE1 1 
ATOM   4927  C  CE2 . PHE E  1 64  ? 42.920  -28.031 7.853  1.00 23.31  ? 64   PHE E CE2 1 
ATOM   4928  C  CZ  . PHE E  1 64  ? 43.873  -28.870 7.339  1.00 20.24  ? 64   PHE E CZ  1 
ATOM   4929  N  N   . ASN E  1 65  ? 39.006  -29.567 8.691  1.00 24.97  ? 65   ASN E N   1 
ATOM   4930  C  CA  . ASN E  1 65  ? 38.112  -30.093 7.656  1.00 25.98  ? 65   ASN E CA  1 
ATOM   4931  C  C   . ASN E  1 65  ? 38.209  -29.339 6.339  1.00 31.23  ? 65   ASN E C   1 
ATOM   4932  O  O   . ASN E  1 65  ? 37.230  -28.724 5.900  1.00 30.40  ? 65   ASN E O   1 
ATOM   4933  C  CB  . ASN E  1 65  ? 36.682  -29.981 8.177  1.00 21.74  ? 65   ASN E CB  1 
ATOM   4934  C  CG  . ASN E  1 65  ? 35.634  -30.635 7.280  1.00 24.64  ? 65   ASN E CG  1 
ATOM   4935  O  OD1 . ASN E  1 65  ? 35.921  -31.500 6.459  1.00 26.82  ? 65   ASN E OD1 1 
ATOM   4936  N  ND2 . ASN E  1 65  ? 34.406  -30.174 7.531  1.00 29.98  ? 65   ASN E ND2 1 
ATOM   4937  N  N   . PRO E  1 66  ? 39.371  -29.396 5.722  1.00 25.39  ? 66   PRO E N   1 
ATOM   4938  C  CA  . PRO E  1 66  ? 39.571  -28.594 4.514  1.00 34.13  ? 66   PRO E CA  1 
ATOM   4939  C  C   . PRO E  1 66  ? 38.679  -29.067 3.362  1.00 32.89  ? 66   PRO E C   1 
ATOM   4940  O  O   . PRO E  1 66  ? 38.455  -28.268 2.449  1.00 32.32  ? 66   PRO E O   1 
ATOM   4941  C  CB  . PRO E  1 66  ? 41.063  -28.804 4.216  1.00 30.62  ? 66   PRO E CB  1 
ATOM   4942  C  CG  . PRO E  1 66  ? 41.390  -30.120 4.825  1.00 27.67  ? 66   PRO E CG  1 
ATOM   4943  C  CD  . PRO E  1 66  ? 40.552  -30.198 6.082  1.00 22.53  ? 66   PRO E CD  1 
ATOM   4944  N  N   . LEU E  1 67  ? 38.162  -30.282 3.338  1.00 33.02  ? 67   LEU E N   1 
ATOM   4945  C  CA  . LEU E  1 67  ? 37.335  -30.740 2.210  1.00 34.86  ? 67   LEU E CA  1 
ATOM   4946  C  C   . LEU E  1 67  ? 35.856  -30.616 2.509  1.00 35.24  ? 67   LEU E C   1 
ATOM   4947  O  O   . LEU E  1 67  ? 34.999  -31.035 1.724  1.00 41.21  ? 67   LEU E O   1 
ATOM   4948  C  CB  . LEU E  1 67  ? 37.682  -32.184 1.837  1.00 29.96  ? 67   LEU E CB  1 
ATOM   4949  C  CG  . LEU E  1 67  ? 39.158  -32.342 1.455  1.00 35.44  ? 67   LEU E CG  1 
ATOM   4950  C  CD1 . LEU E  1 67  ? 39.499  -33.776 1.110  1.00 52.36  ? 67   LEU E CD1 1 
ATOM   4951  C  CD2 . LEU E  1 67  ? 39.477  -31.394 0.304  1.00 40.33  ? 67   LEU E CD2 1 
ATOM   4952  N  N   . SER E  1 68  ? 35.537  -30.013 3.653  1.00 31.39  ? 68   SER E N   1 
ATOM   4953  C  CA  . SER E  1 68  ? 34.157  -29.706 3.980  1.00 34.34  ? 68   SER E CA  1 
ATOM   4954  C  C   . SER E  1 68  ? 33.295  -30.965 3.939  1.00 48.69  ? 68   SER E C   1 
ATOM   4955  O  O   . SER E  1 68  ? 32.253  -31.018 3.285  1.00 48.75  ? 68   SER E O   1 
ATOM   4956  C  CB  . SER E  1 68  ? 33.593  -28.670 2.999  1.00 35.11  ? 68   SER E CB  1 
ATOM   4957  O  OG  . SER E  1 68  ? 33.999  -27.366 3.378  1.00 37.86  ? 68   SER E OG  1 
ATOM   4958  N  N   . ARG E  1 69  ? 33.760  -31.991 4.643  1.00 35.20  ? 69   ARG E N   1 
ATOM   4959  C  CA  . ARG E  1 69  ? 32.992  -33.228 4.749  1.00 30.52  ? 69   ARG E CA  1 
ATOM   4960  C  C   . ARG E  1 69  ? 32.360  -33.359 6.126  1.00 35.32  ? 69   ARG E C   1 
ATOM   4961  O  O   . ARG E  1 69  ? 32.546  -32.518 7.004  1.00 28.84  ? 69   ARG E O   1 
ATOM   4962  C  CB  . ARG E  1 69  ? 33.923  -34.385 4.388  1.00 28.23  ? 69   ARG E CB  1 
ATOM   4963  C  CG  . ARG E  1 69  ? 34.293  -34.314 2.905  1.00 34.34  ? 69   ARG E CG  1 
ATOM   4964  C  CD  . ARG E  1 69  ? 34.711  -35.688 2.404  1.00 56.34  ? 69   ARG E CD  1 
ATOM   4965  N  NE  . ARG E  1 69  ? 35.416  -35.617 1.129  1.00 60.56  ? 69   ARG E NE  1 
ATOM   4966  C  CZ  . ARG E  1 69  ? 36.421  -36.393 0.750  1.00 54.45  ? 69   ARG E CZ  1 
ATOM   4967  N  NH1 . ARG E  1 69  ? 36.957  -36.198 -0.448 1.00 51.23  ? 69   ARG E NH1 1 
ATOM   4968  N  NH2 . ARG E  1 69  ? 36.888  -37.349 1.538  1.00 45.42  ? 69   ARG E NH2 1 
ATOM   4969  N  N   . LYS E  1 70  ? 31.573  -34.414 6.325  1.00 34.17  ? 70   LYS E N   1 
ATOM   4970  C  CA  . LYS E  1 70  ? 30.993  -34.679 7.634  1.00 34.30  ? 70   LYS E CA  1 
ATOM   4971  C  C   . LYS E  1 70  ? 31.940  -35.510 8.483  1.00 26.35  ? 70   LYS E C   1 
ATOM   4972  O  O   . LYS E  1 70  ? 32.848  -36.144 7.938  1.00 29.51  ? 70   LYS E O   1 
ATOM   4973  C  CB  . LYS E  1 70  ? 29.639  -35.402 7.465  1.00 37.36  ? 70   LYS E CB  1 
ATOM   4974  C  CG  . LYS E  1 70  ? 28.555  -34.353 7.168  1.00 42.18  ? 70   LYS E CG  1 
ATOM   4975  C  CD  . LYS E  1 70  ? 27.180  -34.976 7.055  1.00 65.85  ? 70   LYS E CD  1 
ATOM   4976  C  CE  . LYS E  1 70  ? 26.092  -34.090 7.640  1.00 79.40  ? 70   LYS E CE  1 
ATOM   4977  N  NZ  . LYS E  1 70  ? 25.052  -34.897 8.349  1.00 98.94  ? 70   LYS E NZ  1 
ATOM   4978  N  N   . HIS E  1 71  ? 31.721  -35.519 9.791  1.00 28.55  ? 71   HIS E N   1 
ATOM   4979  C  CA  . HIS E  1 71  ? 32.525  -36.331 10.700 1.00 25.92  ? 71   HIS E CA  1 
ATOM   4980  C  C   . HIS E  1 71  ? 32.374  -37.823 10.495 1.00 27.43  ? 71   HIS E C   1 
ATOM   4981  O  O   . HIS E  1 71  ? 31.266  -38.335 10.304 1.00 28.58  ? 71   HIS E O   1 
ATOM   4982  C  CB  . HIS E  1 71  ? 32.140  -35.963 12.146 1.00 23.00  ? 71   HIS E CB  1 
ATOM   4983  C  CG  . HIS E  1 71  ? 32.955  -36.719 13.157 1.00 24.41  ? 71   HIS E CG  1 
ATOM   4984  N  ND1 . HIS E  1 71  ? 34.270  -36.396 13.444 1.00 27.20  ? 71   HIS E ND1 1 
ATOM   4985  C  CD2 . HIS E  1 71  ? 32.655  -37.778 13.931 1.00 22.30  ? 71   HIS E CD2 1 
ATOM   4986  C  CE1 . HIS E  1 71  ? 34.754  -37.215 14.352 1.00 22.41  ? 71   HIS E CE1 1 
ATOM   4987  N  NE2 . HIS E  1 71  ? 33.779  -38.081 14.682 1.00 24.45  ? 71   HIS E NE2 1 
ATOM   4988  N  N   . GLY E  1 72  ? 33.488  -38.548 10.540 1.00 21.29  ? 72   GLY E N   1 
ATOM   4989  C  CA  . GLY E  1 72  ? 33.501  -39.995 10.494 1.00 23.18  ? 72   GLY E CA  1 
ATOM   4990  C  C   . GLY E  1 72  ? 34.661  -40.555 11.310 1.00 26.26  ? 72   GLY E C   1 
ATOM   4991  O  O   . GLY E  1 72  ? 35.302  -39.861 12.097 1.00 26.69  ? 72   GLY E O   1 
ATOM   4992  N  N   . GLY E  1 73  ? 34.920  -41.830 11.122 1.00 20.76  ? 73   GLY E N   1 
ATOM   4993  C  CA  . GLY E  1 73  ? 36.017  -42.555 11.729 1.00 20.05  ? 73   GLY E CA  1 
ATOM   4994  C  C   . GLY E  1 73  ? 37.151  -42.531 10.695 1.00 23.60  ? 73   GLY E C   1 
ATOM   4995  O  O   . GLY E  1 73  ? 36.859  -42.228 9.535  1.00 26.94  ? 73   GLY E O   1 
ATOM   4996  N  N   . PRO E  1 74  ? 38.352  -42.816 11.140 1.00 21.00  ? 74   PRO E N   1 
ATOM   4997  C  CA  . PRO E  1 74  ? 39.513  -42.642 10.254 1.00 26.36  ? 74   PRO E CA  1 
ATOM   4998  C  C   . PRO E  1 74  ? 39.399  -43.559 9.044  1.00 31.91  ? 74   PRO E C   1 
ATOM   4999  O  O   . PRO E  1 74  ? 39.963  -43.208 8.003  1.00 28.91  ? 74   PRO E O   1 
ATOM   5000  C  CB  . PRO E  1 74  ? 40.708  -43.011 11.132 1.00 29.04  ? 74   PRO E CB  1 
ATOM   5001  C  CG  . PRO E  1 74  ? 40.165  -43.723 12.318 1.00 29.81  ? 74   PRO E CG  1 
ATOM   5002  C  CD  . PRO E  1 74  ? 38.729  -43.296 12.468 1.00 28.43  ? 74   PRO E CD  1 
ATOM   5003  N  N   . LYS E  1 75  ? 38.683  -44.687 9.143  1.00 24.79  ? 75   LYS E N   1 
ATOM   5004  C  CA  . LYS E  1 75  ? 38.620  -45.516 7.935  1.00 32.29  ? 75   LYS E CA  1 
ATOM   5005  C  C   . LYS E  1 75  ? 37.522  -45.106 6.969  1.00 34.39  ? 75   LYS E C   1 
ATOM   5006  O  O   . LYS E  1 75  ? 37.332  -45.683 5.886  1.00 33.35  ? 75   LYS E O   1 
ATOM   5007  C  CB  . LYS E  1 75  ? 38.396  -46.978 8.338  1.00 33.49  ? 75   LYS E CB  1 
ATOM   5008  C  CG  . LYS E  1 75  ? 39.321  -47.517 9.421  1.00 30.32  ? 75   LYS E CG  1 
ATOM   5009  C  CD  . LYS E  1 75  ? 38.592  -48.676 10.112 1.00 38.84  ? 75   LYS E CD  1 
ATOM   5010  C  CE  . LYS E  1 75  ? 38.309  -49.773 9.094  1.00 42.27  ? 75   LYS E CE  1 
ATOM   5011  N  NZ  . LYS E  1 75  ? 37.754  -50.989 9.753  1.00 53.62  ? 75   LYS E NZ  1 
ATOM   5012  N  N   . ASP E  1 76  ? 36.700  -44.121 7.294  1.00 27.37  ? 76   ASP E N   1 
ATOM   5013  C  CA  . ASP E  1 76  ? 35.626  -43.750 6.373  1.00 27.19  ? 76   ASP E CA  1 
ATOM   5014  C  C   . ASP E  1 76  ? 36.127  -42.849 5.258  1.00 36.22  ? 76   ASP E C   1 
ATOM   5015  O  O   . ASP E  1 76  ? 37.068  -42.081 5.467  1.00 31.63  ? 76   ASP E O   1 
ATOM   5016  C  CB  . ASP E  1 76  ? 34.523  -43.013 7.134  1.00 30.21  ? 76   ASP E CB  1 
ATOM   5017  C  CG  . ASP E  1 76  ? 33.802  -43.866 8.157  1.00 32.25  ? 76   ASP E CG  1 
ATOM   5018  O  OD1 . ASP E  1 76  ? 33.403  -43.405 9.243  1.00 33.32  ? 76   ASP E OD1 1 
ATOM   5019  O  OD2 . ASP E  1 76  ? 33.613  -45.065 7.886  1.00 34.44  ? 76   ASP E OD2 1 
ATOM   5020  N  N   . GLU E  1 77  ? 35.515  -42.880 4.068  1.00 34.43  ? 77   GLU E N   1 
ATOM   5021  C  CA  . GLU E  1 77  ? 35.884  -41.857 3.084  1.00 32.96  ? 77   GLU E CA  1 
ATOM   5022  C  C   . GLU E  1 77  ? 35.195  -40.552 3.458  1.00 37.48  ? 77   GLU E C   1 
ATOM   5023  O  O   . GLU E  1 77  ? 35.737  -39.471 3.223  1.00 38.23  ? 77   GLU E O   1 
ATOM   5024  C  CB  . GLU E  1 77  ? 35.552  -42.249 1.641  1.00 37.08  ? 77   GLU E CB  1 
ATOM   5025  C  CG  . GLU E  1 77  ? 36.127  -41.287 0.606  1.00 48.39  ? 77   GLU E CG  1 
ATOM   5026  C  CD  . GLU E  1 77  ? 37.617  -41.426 0.354  1.00 65.15  ? 77   GLU E CD  1 
ATOM   5027  O  OE1 . GLU E  1 77  ? 38.146  -42.557 0.429  1.00 82.14  ? 77   GLU E OE1 1 
ATOM   5028  O  OE2 . GLU E  1 77  ? 38.299  -40.408 0.073  1.00 72.34  ? 77   GLU E OE2 1 
ATOM   5029  N  N   . GLU E  1 78  ? 33.997  -40.642 4.055  1.00 30.56  ? 78   GLU E N   1 
ATOM   5030  C  CA  . GLU E  1 78  ? 33.391  -39.426 4.582  1.00 26.09  ? 78   GLU E CA  1 
ATOM   5031  C  C   . GLU E  1 78  ? 33.878  -39.230 6.034  1.00 29.18  ? 78   GLU E C   1 
ATOM   5032  O  O   . GLU E  1 78  ? 33.420  -39.862 6.980  1.00 25.02  ? 78   GLU E O   1 
ATOM   5033  C  CB  . GLU E  1 78  ? 31.873  -39.411 4.544  1.00 28.26  ? 78   GLU E CB  1 
ATOM   5034  C  CG  . GLU E  1 78  ? 31.285  -38.077 4.960  1.00 30.51  ? 78   GLU E CG  1 
ATOM   5035  C  CD  . GLU E  1 78  ? 31.408  -36.996 3.898  1.00 40.53  ? 78   GLU E CD  1 
ATOM   5036  O  OE1 . GLU E  1 78  ? 30.847  -35.888 4.102  1.00 38.95  ? 78   GLU E OE1 1 
ATOM   5037  O  OE2 . GLU E  1 78  ? 32.047  -37.225 2.844  1.00 53.73  ? 78   GLU E OE2 1 
ATOM   5038  N  N   . ARG E  1 79  ? 34.858  -38.339 6.145  1.00 25.41  ? 79   ARG E N   1 
ATOM   5039  C  CA  . ARG E  1 79  ? 35.505  -37.975 7.400  1.00 24.31  ? 79   ARG E CA  1 
ATOM   5040  C  C   . ARG E  1 79  ? 36.101  -36.581 7.258  1.00 27.93  ? 79   ARG E C   1 
ATOM   5041  O  O   . ARG E  1 79  ? 36.336  -36.121 6.141  1.00 26.70  ? 79   ARG E O   1 
ATOM   5042  C  CB  . ARG E  1 79  ? 36.612  -38.940 7.795  1.00 22.29  ? 79   ARG E CB  1 
ATOM   5043  C  CG  . ARG E  1 79  ? 37.777  -39.072 6.811  1.00 23.50  ? 79   ARG E CG  1 
ATOM   5044  C  CD  . ARG E  1 79  ? 38.881  -39.943 7.417  1.00 26.25  ? 79   ARG E CD  1 
ATOM   5045  N  NE  . ARG E  1 79  ? 39.876  -39.060 8.068  1.00 28.62  ? 79   ARG E NE  1 
ATOM   5046  C  CZ  . ARG E  1 79  ? 41.079  -39.490 8.406  1.00 25.11  ? 79   ARG E CZ  1 
ATOM   5047  N  NH1 . ARG E  1 79  ? 41.962  -38.687 8.982  1.00 21.82  ? 79   ARG E NH1 1 
ATOM   5048  N  NH2 . ARG E  1 79  ? 41.404  -40.751 8.162  1.00 26.20  ? 79   ARG E NH2 1 
ATOM   5049  N  N   . HIS E  1 80  ? 36.370  -35.944 8.382  1.00 24.41  ? 80   HIS E N   1 
ATOM   5050  C  CA  . HIS E  1 80  ? 37.218  -34.755 8.379  1.00 22.38  ? 80   HIS E CA  1 
ATOM   5051  C  C   . HIS E  1 80  ? 38.669  -35.202 8.246  1.00 22.31  ? 80   HIS E C   1 
ATOM   5052  O  O   . HIS E  1 80  ? 39.029  -36.296 8.690  1.00 23.41  ? 80   HIS E O   1 
ATOM   5053  C  CB  . HIS E  1 80  ? 37.016  -33.990 9.680  1.00 21.94  ? 80   HIS E CB  1 
ATOM   5054  C  CG  . HIS E  1 80  ? 35.627  -33.585 10.032 1.00 27.52  ? 80   HIS E CG  1 
ATOM   5055  N  ND1 . HIS E  1 80  ? 35.081  -33.670 11.296 1.00 24.90  ? 80   HIS E ND1 1 
ATOM   5056  C  CD2 . HIS E  1 80  ? 34.650  -33.061 9.268  1.00 24.86  ? 80   HIS E CD2 1 
ATOM   5057  C  CE1 . HIS E  1 80  ? 33.844  -33.211 11.291 1.00 24.87  ? 80   HIS E CE1 1 
ATOM   5058  N  NE2 . HIS E  1 80  ? 33.550  -32.827 10.055 1.00 25.31  ? 80   HIS E NE2 1 
ATOM   5059  N  N   . VAL E  1 81  ? 39.527  -34.344 7.667  1.00 21.93  ? 81   VAL E N   1 
ATOM   5060  C  CA  . VAL E  1 81  ? 40.947  -34.696 7.671  1.00 22.61  ? 81   VAL E CA  1 
ATOM   5061  C  C   . VAL E  1 81  ? 41.442  -34.983 9.080  1.00 17.67  ? 81   VAL E C   1 
ATOM   5062  O  O   . VAL E  1 81  ? 42.184  -35.921 9.289  1.00 19.96  ? 81   VAL E O   1 
ATOM   5063  C  CB  . VAL E  1 81  ? 41.770  -33.562 7.013  1.00 23.10  ? 81   VAL E CB  1 
ATOM   5064  C  CG1 . VAL E  1 81  ? 43.255  -33.769 7.249  1.00 23.22  ? 81   VAL E CG1 1 
ATOM   5065  C  CG2 . VAL E  1 81  ? 41.448  -33.549 5.522  1.00 23.52  ? 81   VAL E CG2 1 
ATOM   5066  N  N   . GLY E  1 82  ? 40.957  -34.203 10.045 1.00 21.48  ? 82   GLY E N   1 
ATOM   5067  C  CA  . GLY E  1 82  ? 41.454  -34.399 11.403 1.00 22.42  ? 82   GLY E CA  1 
ATOM   5068  C  C   . GLY E  1 82  ? 40.903  -35.584 12.159 1.00 26.75  ? 82   GLY E C   1 
ATOM   5069  O  O   . GLY E  1 82  ? 41.241  -35.764 13.340 1.00 23.84  ? 82   GLY E O   1 
ATOM   5070  N  N   . ASP E  1 83  ? 40.051  -36.423 11.556 1.00 20.56  ? 83   ASP E N   1 
ATOM   5071  C  CA  . ASP E  1 83  ? 39.406  -37.498 12.308 1.00 22.08  ? 83   ASP E CA  1 
ATOM   5072  C  C   . ASP E  1 83  ? 40.298  -38.709 12.512 1.00 22.24  ? 83   ASP E C   1 
ATOM   5073  O  O   . ASP E  1 83  ? 40.422  -39.571 11.639 1.00 22.88  ? 83   ASP E O   1 
ATOM   5074  C  CB  . ASP E  1 83  ? 38.103  -37.931 11.590 1.00 19.37  ? 83   ASP E CB  1 
ATOM   5075  C  CG  . ASP E  1 83  ? 37.018  -36.889 11.693 1.00 24.06  ? 83   ASP E CG  1 
ATOM   5076  O  OD1 . ASP E  1 83  ? 37.124  -35.993 12.568 1.00 22.63  ? 83   ASP E OD1 1 
ATOM   5077  O  OD2 . ASP E  1 83  ? 36.025  -36.932 10.908 1.00 24.72  ? 83   ASP E OD2 1 
ATOM   5078  N  N   . LEU E  1 84  ? 40.921  -38.796 13.690 1.00 20.94  ? 84   LEU E N   1 
ATOM   5079  C  CA  . LEU E  1 84  ? 41.819  -39.899 14.022 1.00 18.01  ? 84   LEU E CA  1 
ATOM   5080  C  C   . LEU E  1 84  ? 41.156  -40.950 14.899 1.00 22.86  ? 84   LEU E C   1 
ATOM   5081  O  O   . LEU E  1 84  ? 41.822  -41.861 15.380 1.00 21.97  ? 84   LEU E O   1 
ATOM   5082  C  CB  . LEU E  1 84  ? 43.065  -39.321 14.712 1.00 18.79  ? 84   LEU E CB  1 
ATOM   5083  C  CG  . LEU E  1 84  ? 43.885  -38.381 13.799 1.00 24.77  ? 84   LEU E CG  1 
ATOM   5084  C  CD1 . LEU E  1 84  ? 45.146  -37.909 14.513 1.00 21.75  ? 84   LEU E CD1 1 
ATOM   5085  C  CD2 . LEU E  1 84  ? 44.268  -39.083 12.513 1.00 23.39  ? 84   LEU E CD2 1 
ATOM   5086  N  N   . GLY E  1 85  ? 39.846  -40.842 15.140 1.00 22.47  ? 85   GLY E N   1 
ATOM   5087  C  CA  . GLY E  1 85  ? 39.137  -41.896 15.871 1.00 22.53  ? 85   GLY E CA  1 
ATOM   5088  C  C   . GLY E  1 85  ? 39.230  -41.786 17.376 1.00 18.66  ? 85   GLY E C   1 
ATOM   5089  O  O   . GLY E  1 85  ? 39.054  -40.714 17.949 1.00 21.97  ? 85   GLY E O   1 
ATOM   5090  N  N   . ASN E  1 86  ? 39.514  -42.899 18.047 1.00 21.29  ? 86   ASN E N   1 
ATOM   5091  C  CA  . ASN E  1 86  ? 39.704  -42.936 19.480 1.00 18.08  ? 86   ASN E CA  1 
ATOM   5092  C  C   . ASN E  1 86  ? 41.078  -43.447 19.882 1.00 21.61  ? 86   ASN E C   1 
ATOM   5093  O  O   . ASN E  1 86  ? 41.743  -44.146 19.109 1.00 23.27  ? 86   ASN E O   1 
ATOM   5094  C  CB  . ASN E  1 86  ? 38.696  -43.905 20.139 1.00 21.20  ? 86   ASN E CB  1 
ATOM   5095  C  CG  . ASN E  1 86  ? 37.283  -43.369 20.027 1.00 20.11  ? 86   ASN E CG  1 
ATOM   5096  O  OD1 . ASN E  1 86  ? 36.928  -42.350 20.615 1.00 22.93  ? 86   ASN E OD1 1 
ATOM   5097  N  ND2 . ASN E  1 86  ? 36.475  -44.051 19.225 1.00 23.10  ? 86   ASN E ND2 1 
ATOM   5098  N  N   . VAL E  1 87  ? 41.479  -43.138 21.106 1.00 18.84  ? 87   VAL E N   1 
ATOM   5099  C  CA  . VAL E  1 87  ? 42.588  -43.804 21.777 1.00 19.75  ? 87   VAL E CA  1 
ATOM   5100  C  C   . VAL E  1 87  ? 41.988  -44.490 23.001 1.00 22.49  ? 87   VAL E C   1 
ATOM   5101  O  O   . VAL E  1 87  ? 40.901  -44.067 23.406 1.00 25.25  ? 87   VAL E O   1 
ATOM   5102  C  CB  . VAL E  1 87  ? 43.687  -42.823 22.206 1.00 22.69  ? 87   VAL E CB  1 
ATOM   5103  C  CG1 . VAL E  1 87  ? 44.328  -42.171 20.983 1.00 22.89  ? 87   VAL E CG1 1 
ATOM   5104  C  CG2 . VAL E  1 87  ? 43.078  -41.771 23.126 1.00 26.93  ? 87   VAL E CG2 1 
ATOM   5105  N  N   . THR E  1 88  ? 42.633  -45.510 23.530 1.00 23.58  ? 88   THR E N   1 
ATOM   5106  C  CA  . THR E  1 88  ? 42.117  -46.316 24.632 1.00 21.10  ? 88   THR E CA  1 
ATOM   5107  C  C   . THR E  1 88  ? 43.026  -46.199 25.846 1.00 27.22  ? 88   THR E C   1 
ATOM   5108  O  O   . THR E  1 88  ? 44.221  -46.507 25.770 1.00 26.19  ? 88   THR E O   1 
ATOM   5109  C  CB  . THR E  1 88  ? 42.048  -47.802 24.232 1.00 26.64  ? 88   THR E CB  1 
ATOM   5110  O  OG1 . THR E  1 88  ? 41.210  -47.933 23.070 1.00 26.19  ? 88   THR E OG1 1 
ATOM   5111  C  CG2 . THR E  1 88  ? 41.441  -48.618 25.369 1.00 26.93  ? 88   THR E CG2 1 
ATOM   5112  N  N   . ALA E  1 89  ? 42.456  -45.756 26.953 1.00 22.71  ? 89   ALA E N   1 
ATOM   5113  C  CA  . ALA E  1 89  ? 43.230  -45.679 28.188 1.00 24.55  ? 89   ALA E CA  1 
ATOM   5114  C  C   . ALA E  1 89  ? 43.030  -46.976 28.975 1.00 28.01  ? 89   ALA E C   1 
ATOM   5115  O  O   . ALA E  1 89  ? 41.887  -47.433 29.092 1.00 30.07  ? 89   ALA E O   1 
ATOM   5116  C  CB  . ALA E  1 89  ? 42.815  -44.458 28.995 1.00 24.67  ? 89   ALA E CB  1 
ATOM   5117  N  N   . ASP E  1 90  ? 44.133  -47.505 29.478 1.00 27.97  ? 90   ASP E N   1 
ATOM   5118  C  CA  . ASP E  1 90  ? 44.112  -48.764 30.233 1.00 34.07  ? 90   ASP E CA  1 
ATOM   5119  C  C   . ASP E  1 90  ? 43.652  -48.493 31.658 1.00 35.08  ? 90   ASP E C   1 
ATOM   5120  O  O   . ASP E  1 90  ? 43.300  -47.382 32.046 1.00 33.54  ? 90   ASP E O   1 
ATOM   5121  C  CB  . ASP E  1 90  ? 45.476  -49.448 30.200 1.00 29.95  ? 90   ASP E CB  1 
ATOM   5122  C  CG  . ASP E  1 90  ? 46.601  -48.701 30.887 1.00 39.58  ? 90   ASP E CG  1 
ATOM   5123  O  OD1 . ASP E  1 90  ? 47.775  -48.835 30.460 1.00 51.40  ? 90   ASP E OD1 1 
ATOM   5124  O  OD2 . ASP E  1 90  ? 46.385  -47.946 31.867 1.00 44.05  ? 90   ASP E OD2 1 
ATOM   5125  N  N   . LYS E  1 91  ? 43.653  -49.548 32.475 1.00 37.95  ? 91   LYS E N   1 
ATOM   5126  C  CA  . LYS E  1 91  ? 43.160  -49.388 33.839 1.00 33.38  ? 91   LYS E CA  1 
ATOM   5127  C  C   . LYS E  1 91  ? 44.046  -48.490 34.679 1.00 33.82  ? 91   LYS E C   1 
ATOM   5128  O  O   . LYS E  1 91  ? 43.647  -48.003 35.739 1.00 39.56  ? 91   LYS E O   1 
ATOM   5129  C  CB  . LYS E  1 91  ? 43.051  -50.802 34.459 1.00 37.91  ? 91   LYS E CB  1 
ATOM   5130  C  CG  . LYS E  1 91  ? 44.417  -51.478 34.560 1.00 57.14  ? 91   LYS E CG  1 
ATOM   5131  C  CD  . LYS E  1 91  ? 44.394  -52.622 35.559 1.00 66.27  ? 91   LYS E CD  1 
ATOM   5132  C  CE  . LYS E  1 91  ? 45.126  -53.844 35.024 1.00 75.04  ? 91   LYS E CE  1 
ATOM   5133  N  NZ  . LYS E  1 91  ? 44.609  -55.108 35.633 1.00 82.31  ? 91   LYS E NZ  1 
ATOM   5134  N  N   . ASP E  1 92  ? 45.282  -48.219 34.258 1.00 29.57  ? 92   ASP E N   1 
ATOM   5135  C  CA  . ASP E  1 92  ? 46.152  -47.365 35.083 1.00 28.19  ? 92   ASP E CA  1 
ATOM   5136  C  C   . ASP E  1 92  ? 46.122  -45.906 34.641 1.00 29.03  ? 92   ASP E C   1 
ATOM   5137  O  O   . ASP E  1 92  ? 46.994  -45.145 35.059 1.00 32.56  ? 92   ASP E O   1 
ATOM   5138  C  CB  . ASP E  1 92  ? 47.573  -47.915 35.033 1.00 31.41  ? 92   ASP E CB  1 
ATOM   5139  C  CG  . ASP E  1 92  ? 47.775  -48.976 36.099 1.00 58.64  ? 92   ASP E CG  1 
ATOM   5140  O  OD1 . ASP E  1 92  ? 47.869  -48.581 37.284 1.00 95.40  ? 92   ASP E OD1 1 
ATOM   5141  O  OD2 . ASP E  1 92  ? 47.839  -50.183 35.772 1.00 53.15  ? 92   ASP E OD2 1 
ATOM   5142  N  N   . GLY E  1 93  ? 45.155  -45.538 33.831 1.00 27.06  ? 93   GLY E N   1 
ATOM   5143  C  CA  . GLY E  1 93  ? 44.930  -44.177 33.376 1.00 30.59  ? 93   GLY E CA  1 
ATOM   5144  C  C   . GLY E  1 93  ? 45.796  -43.731 32.210 1.00 29.12  ? 93   GLY E C   1 
ATOM   5145  O  O   . GLY E  1 93  ? 45.899  -42.520 31.975 1.00 32.77  ? 93   GLY E O   1 
ATOM   5146  N  N   . VAL E  1 94  ? 46.408  -44.625 31.465 1.00 28.00  ? 94   VAL E N   1 
ATOM   5147  C  CA  . VAL E  1 94  ? 47.314  -44.337 30.365 1.00 31.64  ? 94   VAL E CA  1 
ATOM   5148  C  C   . VAL E  1 94  ? 46.875  -44.922 29.030 1.00 29.77  ? 94   VAL E C   1 
ATOM   5149  O  O   . VAL E  1 94  ? 46.603  -46.112 28.901 1.00 28.27  ? 94   VAL E O   1 
ATOM   5150  C  CB  . VAL E  1 94  ? 48.731  -44.876 30.681 1.00 38.31  ? 94   VAL E CB  1 
ATOM   5151  C  CG1 . VAL E  1 94  ? 49.690  -44.693 29.512 1.00 33.78  ? 94   VAL E CG1 1 
ATOM   5152  C  CG2 . VAL E  1 94  ? 49.266  -44.158 31.916 1.00 28.98  ? 94   VAL E CG2 1 
ATOM   5153  N  N   . ALA E  1 95  ? 46.807  -44.078 28.007 1.00 29.63  ? 95   ALA E N   1 
ATOM   5154  C  CA  . ALA E  1 95  ? 46.652  -44.489 26.617 1.00 28.35  ? 95   ALA E CA  1 
ATOM   5155  C  C   . ALA E  1 95  ? 47.998  -44.494 25.897 1.00 27.95  ? 95   ALA E C   1 
ATOM   5156  O  O   . ALA E  1 95  ? 48.620  -43.437 25.706 1.00 25.92  ? 95   ALA E O   1 
ATOM   5157  C  CB  . ALA E  1 95  ? 45.686  -43.578 25.880 1.00 25.97  ? 95   ALA E CB  1 
ATOM   5158  N  N   . ASP E  1 96  ? 48.446  -45.675 25.498 1.00 24.63  ? 96   ASP E N   1 
ATOM   5159  C  CA  . ASP E  1 96  ? 49.658  -45.786 24.705 1.00 28.95  ? 96   ASP E CA  1 
ATOM   5160  C  C   . ASP E  1 96  ? 49.327  -45.746 23.215 1.00 30.69  ? 96   ASP E C   1 
ATOM   5161  O  O   . ASP E  1 96  ? 48.967  -46.750 22.616 1.00 42.87  ? 96   ASP E O   1 
ATOM   5162  C  CB  . ASP E  1 96  ? 50.428  -47.071 24.997 1.00 33.44  ? 96   ASP E CB  1 
ATOM   5163  C  CG  . ASP E  1 96  ? 51.050  -46.964 26.385 1.00 42.91  ? 96   ASP E CG  1 
ATOM   5164  O  OD1 . ASP E  1 96  ? 51.614  -45.899 26.707 1.00 52.01  ? 96   ASP E OD1 1 
ATOM   5165  O  OD2 . ASP E  1 96  ? 50.933  -47.948 27.131 1.00 47.08  ? 96   ASP E OD2 1 
ATOM   5166  N  N   . VAL E  1 97  ? 49.485  -44.578 22.638 1.00 21.20  ? 97   VAL E N   1 
ATOM   5167  C  CA  . VAL E  1 97  ? 48.901  -44.278 21.343 1.00 20.89  ? 97   VAL E CA  1 
ATOM   5168  C  C   . VAL E  1 97  ? 49.820  -44.796 20.236 1.00 21.54  ? 97   VAL E C   1 
ATOM   5169  O  O   . VAL E  1 97  ? 51.014  -44.614 20.309 1.00 22.83  ? 97   VAL E O   1 
ATOM   5170  C  CB  . VAL E  1 97  ? 48.691  -42.767 21.158 1.00 23.40  ? 97   VAL E CB  1 
ATOM   5171  C  CG1 . VAL E  1 97  ? 48.107  -42.445 19.792 1.00 19.90  ? 97   VAL E CG1 1 
ATOM   5172  C  CG2 . VAL E  1 97  ? 47.793  -42.229 22.270 1.00 24.95  ? 97   VAL E CG2 1 
ATOM   5173  N  N   . SER E  1 98  ? 49.175  -45.415 19.265 1.00 25.23  ? 98   SER E N   1 
ATOM   5174  C  CA  . SER E  1 98  ? 49.857  -45.917 18.093 1.00 28.74  ? 98   SER E CA  1 
ATOM   5175  C  C   . SER E  1 98  ? 48.853  -46.034 16.958 1.00 30.45  ? 98   SER E C   1 
ATOM   5176  O  O   . SER E  1 98  ? 48.055  -46.967 16.977 1.00 31.50  ? 98   SER E O   1 
ATOM   5177  C  CB  . SER E  1 98  ? 50.475  -47.286 18.380 1.00 38.94  ? 98   SER E CB  1 
ATOM   5178  O  OG  . SER E  1 98  ? 51.503  -47.564 17.439 1.00 42.15  ? 98   SER E OG  1 
ATOM   5179  N  N   . ILE E  1 99  ? 48.936  -45.091 16.051 1.00 21.65  ? 99   ILE E N   1 
ATOM   5180  C  CA  . ILE E  1 99  ? 48.021  -44.922 14.933 1.00 25.99  ? 99   ILE E CA  1 
ATOM   5181  C  C   . ILE E  1 99  ? 48.845  -44.670 13.670 1.00 32.25  ? 99   ILE E C   1 
ATOM   5182  O  O   . ILE E  1 99  ? 49.916  -44.058 13.795 1.00 29.50  ? 99   ILE E O   1 
ATOM   5183  C  CB  . ILE E  1 99  ? 47.055  -43.751 15.182 1.00 27.86  ? 99   ILE E CB  1 
ATOM   5184  C  CG1 . ILE E  1 99  ? 45.982  -44.083 16.242 1.00 36.06  ? 99   ILE E CG1 1 
ATOM   5185  C  CG2 . ILE E  1 99  ? 46.343  -43.255 13.940 1.00 32.04  ? 99   ILE E CG2 1 
ATOM   5186  C  CD1 . ILE E  1 99  ? 45.282  -42.824 16.745 1.00 32.14  ? 99   ILE E CD1 1 
ATOM   5187  N  N   . GLU E  1 100 ? 48.342  -45.132 12.539 1.00 26.93  ? 100  GLU E N   1 
ATOM   5188  C  CA  . GLU E  1 100 ? 48.912  -44.792 11.240 1.00 24.81  ? 100  GLU E CA  1 
ATOM   5189  C  C   . GLU E  1 100 ? 47.796  -44.226 10.378 1.00 28.94  ? 100  GLU E C   1 
ATOM   5190  O  O   . GLU E  1 100 ? 46.728  -44.860 10.324 1.00 28.13  ? 100  GLU E O   1 
ATOM   5191  C  CB  . GLU E  1 100 ? 49.527  -45.994 10.507 1.00 26.84  ? 100  GLU E CB  1 
ATOM   5192  C  CG  . GLU E  1 100 ? 49.861  -45.602 9.063  1.00 41.05  ? 100  GLU E CG  1 
ATOM   5193  C  CD  . GLU E  1 100 ? 50.497  -46.732 8.275  1.00 59.31  ? 100  GLU E CD  1 
ATOM   5194  O  OE1 . GLU E  1 100 ? 51.657  -47.058 8.616  1.00 45.33  ? 100  GLU E OE1 1 
ATOM   5195  O  OE2 . GLU E  1 100 ? 49.843  -47.265 7.344  1.00 47.78  ? 100  GLU E OE2 1 
ATOM   5196  N  N   . ASP E  1 101 ? 47.999  -43.081 9.748  1.00 22.21  ? 101  ASP E N   1 
ATOM   5197  C  CA  . ASP E  1 101 ? 46.900  -42.483 9.001  1.00 22.07  ? 101  ASP E CA  1 
ATOM   5198  C  C   . ASP E  1 101 ? 47.387  -41.959 7.649  1.00 28.78  ? 101  ASP E C   1 
ATOM   5199  O  O   . ASP E  1 101 ? 48.435  -41.309 7.587  1.00 28.27  ? 101  ASP E O   1 
ATOM   5200  C  CB  . ASP E  1 101 ? 46.256  -41.307 9.730  1.00 26.65  ? 101  ASP E CB  1 
ATOM   5201  C  CG  . ASP E  1 101 ? 44.926  -40.892 9.135  1.00 30.98  ? 101  ASP E CG  1 
ATOM   5202  O  OD1 . ASP E  1 101 ? 44.830  -39.843 8.475  1.00 22.91  ? 101  ASP E OD1 1 
ATOM   5203  O  OD2 . ASP E  1 101 ? 43.915  -41.621 9.321  1.00 30.20  ? 101  ASP E OD2 1 
ATOM   5204  N  N   . SER E  1 102 ? 46.598  -42.218 6.614  1.00 27.24  ? 102  SER E N   1 
ATOM   5205  C  CA  . SER E  1 102 ? 47.022  -41.783 5.284  1.00 28.97  ? 102  SER E CA  1 
ATOM   5206  C  C   . SER E  1 102 ? 46.275  -40.584 4.766  1.00 24.85  ? 102  SER E C   1 
ATOM   5207  O  O   . SER E  1 102 ? 46.420  -40.205 3.599  1.00 29.81  ? 102  SER E O   1 
ATOM   5208  C  CB  . SER E  1 102 ? 46.849  -42.975 4.332  1.00 32.86  ? 102  SER E CB  1 
ATOM   5209  O  OG  . SER E  1 102 ? 47.971  -43.827 4.498  1.00 49.18  ? 102  SER E OG  1 
ATOM   5210  N  N   . VAL E  1 103 ? 45.451  -39.940 5.597  1.00 21.55  ? 103  VAL E N   1 
ATOM   5211  C  CA  . VAL E  1 103 ? 44.718  -38.780 5.156  1.00 20.52  ? 103  VAL E CA  1 
ATOM   5212  C  C   . VAL E  1 103 ? 45.365  -37.508 5.714  1.00 24.61  ? 103  VAL E C   1 
ATOM   5213  O  O   . VAL E  1 103 ? 45.456  -36.491 5.018  1.00 27.29  ? 103  VAL E O   1 
ATOM   5214  C  CB  . VAL E  1 103 ? 43.234  -38.880 5.571  1.00 22.54  ? 103  VAL E CB  1 
ATOM   5215  C  CG1 . VAL E  1 103 ? 42.516  -37.562 5.436  1.00 25.19  ? 103  VAL E CG1 1 
ATOM   5216  C  CG2 . VAL E  1 103 ? 42.567  -39.975 4.714  1.00 23.90  ? 103  VAL E CG2 1 
ATOM   5217  N  N   . ILE E  1 104 ? 45.813  -37.526 6.974  1.00 19.99  ? 104  ILE E N   1 
ATOM   5218  C  CA  . ILE E  1 104 ? 46.546  -36.340 7.441  1.00 18.70  ? 104  ILE E CA  1 
ATOM   5219  C  C   . ILE E  1 104 ? 47.926  -36.311 6.798  1.00 20.29  ? 104  ILE E C   1 
ATOM   5220  O  O   . ILE E  1 104 ? 48.427  -37.342 6.354  1.00 22.37  ? 104  ILE E O   1 
ATOM   5221  C  CB  . ILE E  1 104 ? 46.783  -36.356 8.962  1.00 19.16  ? 104  ILE E CB  1 
ATOM   5222  C  CG1 . ILE E  1 104 ? 47.404  -37.661 9.441  1.00 22.44  ? 104  ILE E CG1 1 
ATOM   5223  C  CG2 . ILE E  1 104 ? 45.492  -36.069 9.731  1.00 22.64  ? 104  ILE E CG2 1 
ATOM   5224  C  CD1 . ILE E  1 104 ? 47.979  -37.587 10.854 1.00 23.35  ? 104  ILE E CD1 1 
ATOM   5225  N  N   . SER E  1 105 ? 48.559  -35.143 6.839  1.00 19.95  ? 105  SER E N   1 
ATOM   5226  C  CA  . SER E  1 105 ? 49.922  -35.066 6.321  1.00 20.57  ? 105  SER E CA  1 
ATOM   5227  C  C   . SER E  1 105 ? 50.726  -34.021 7.091  1.00 20.80  ? 105  SER E C   1 
ATOM   5228  O  O   . SER E  1 105 ? 50.125  -33.132 7.692  1.00 21.68  ? 105  SER E O   1 
ATOM   5229  C  CB  . SER E  1 105 ? 49.878  -34.668 4.833  1.00 26.73  ? 105  SER E CB  1 
ATOM   5230  O  OG  . SER E  1 105 ? 51.190  -34.714 4.277  1.00 24.90  ? 105  SER E OG  1 
ATOM   5231  N  N   . LEU E  1 106 ? 52.033  -34.098 7.050  1.00 20.10  ? 106  LEU E N   1 
ATOM   5232  C  CA  . LEU E  1 106 ? 52.870  -33.069 7.698  1.00 22.86  ? 106  LEU E CA  1 
ATOM   5233  C  C   . LEU E  1 106 ? 53.383  -32.028 6.713  1.00 27.33  ? 106  LEU E C   1 
ATOM   5234  O  O   . LEU E  1 106 ? 54.196  -31.163 7.069  1.00 24.66  ? 106  LEU E O   1 
ATOM   5235  C  CB  . LEU E  1 106 ? 54.029  -33.759 8.419  1.00 20.86  ? 106  LEU E CB  1 
ATOM   5236  C  CG  . LEU E  1 106 ? 53.696  -34.842 9.454  1.00 21.04  ? 106  LEU E CG  1 
ATOM   5237  C  CD1 . LEU E  1 106 ? 54.966  -35.374 10.105 1.00 21.81  ? 106  LEU E CD1 1 
ATOM   5238  C  CD2 . LEU E  1 106 ? 52.766  -34.259 10.510 1.00 24.64  ? 106  LEU E CD2 1 
ATOM   5239  N  N   . SER E  1 107 ? 52.929  -32.048 5.469  1.00 25.07  ? 107  SER E N   1 
ATOM   5240  C  CA  . SER E  1 107 ? 53.261  -31.030 4.468  1.00 30.54  ? 107  SER E CA  1 
ATOM   5241  C  C   . SER E  1 107 ? 52.115  -30.890 3.470  1.00 34.57  ? 107  SER E C   1 
ATOM   5242  O  O   . SER E  1 107 ? 51.232  -31.767 3.440  1.00 27.81  ? 107  SER E O   1 
ATOM   5243  C  CB  . SER E  1 107 ? 54.588  -31.376 3.792  1.00 33.09  ? 107  SER E CB  1 
ATOM   5244  O  OG  . SER E  1 107 ? 54.550  -32.638 3.135  1.00 30.97  ? 107  SER E OG  1 
ATOM   5245  N  N   . GLY E  1 108 ? 52.040  -29.834 2.663  1.00 33.82  ? 108  GLY E N   1 
ATOM   5246  C  CA  . GLY E  1 108 ? 50.942  -29.621 1.736  1.00 40.57  ? 108  GLY E CA  1 
ATOM   5247  C  C   . GLY E  1 108 ? 49.645  -29.078 2.312  1.00 60.58  ? 108  GLY E C   1 
ATOM   5248  O  O   . GLY E  1 108 ? 49.725  -28.348 3.306  1.00 72.61  ? 108  GLY E O   1 
ATOM   5249  N  N   . ASP E  1 109 ? 48.494  -29.404 1.729  1.00 62.45  ? 109  ASP E N   1 
ATOM   5250  C  CA  . ASP E  1 109 ? 47.142  -28.965 1.996  1.00 58.29  ? 109  ASP E CA  1 
ATOM   5251  C  C   . ASP E  1 109 ? 46.445  -29.653 3.162  1.00 53.82  ? 109  ASP E C   1 
ATOM   5252  O  O   . ASP E  1 109 ? 45.652  -29.039 3.882  1.00 45.16  ? 109  ASP E O   1 
ATOM   5253  C  CB  . ASP E  1 109 ? 46.176  -29.208 0.807  1.00 67.80  ? 109  ASP E CB  1 
ATOM   5254  C  CG  . ASP E  1 109 ? 44.711  -29.118 1.204  1.00 69.58  ? 109  ASP E CG  1 
ATOM   5255  O  OD1 . ASP E  1 109 ? 44.314  -28.252 2.015  1.00 72.00  ? 109  ASP E OD1 1 
ATOM   5256  O  OD2 . ASP E  1 109 ? 43.881  -29.911 0.711  1.00 81.76  ? 109  ASP E OD2 1 
ATOM   5257  N  N   . HIS E  1 110 ? 46.713  -30.945 3.358  1.00 44.73  ? 110  HIS E N   1 
ATOM   5258  C  CA  . HIS E  1 110 ? 46.128  -31.644 4.496  1.00 48.04  ? 110  HIS E CA  1 
ATOM   5259  C  C   . HIS E  1 110 ? 47.000  -31.486 5.734  1.00 39.04  ? 110  HIS E C   1 
ATOM   5260  O  O   . HIS E  1 110 ? 46.914  -32.401 6.562  1.00 37.08  ? 110  HIS E O   1 
ATOM   5261  C  CB  . HIS E  1 110 ? 45.964  -33.151 4.221  1.00 42.35  ? 110  HIS E CB  1 
ATOM   5262  C  CG  . HIS E  1 110 ? 44.776  -33.355 3.321  1.00 43.49  ? 110  HIS E CG  1 
ATOM   5263  N  ND1 . HIS E  1 110 ? 44.129  -34.543 3.133  1.00 45.71  ? 110  HIS E ND1 1 
ATOM   5264  C  CD2 . HIS E  1 110 ? 44.135  -32.445 2.547  1.00 45.50  ? 110  HIS E CD2 1 
ATOM   5265  C  CE1 . HIS E  1 110 ? 43.137  -34.368 2.286  1.00 42.78  ? 110  HIS E CE1 1 
ATOM   5266  N  NE2 . HIS E  1 110 ? 43.115  -33.103 1.916  1.00 43.65  ? 110  HIS E NE2 1 
ATOM   5267  N  N   . CYS E  1 111 ? 47.787  -30.411 5.709  1.00 35.09  ? 111  CYS E N   1 
ATOM   5268  C  CA  . CYS E  1 111 ? 48.964  -30.333 6.576  1.00 29.75  ? 111  CYS E CA  1 
ATOM   5269  C  C   . CYS E  1 111 ? 48.502  -29.907 7.967  1.00 22.78  ? 111  CYS E C   1 
ATOM   5270  O  O   . CYS E  1 111 ? 47.787  -28.913 8.083  1.00 29.13  ? 111  CYS E O   1 
ATOM   5271  C  CB  . CYS E  1 111 ? 50.001  -29.384 6.008  1.00 39.32  ? 111  CYS E CB  1 
ATOM   5272  S  SG  . CYS E  1 111 ? 51.257  -28.861 7.190  1.00 40.97  ? 111  CYS E SG  1 
ATOM   5273  N  N   . ILE E  1 112 ? 48.889  -30.664 8.974  1.00 21.54  ? 112  ILE E N   1 
ATOM   5274  C  CA  . ILE E  1 112 ? 48.339  -30.384 10.312 1.00 19.79  ? 112  ILE E CA  1 
ATOM   5275  C  C   . ILE E  1 112 ? 49.330  -29.629 11.178 1.00 22.57  ? 112  ILE E C   1 
ATOM   5276  O  O   . ILE E  1 112 ? 49.071  -29.405 12.354 1.00 20.78  ? 112  ILE E O   1 
ATOM   5277  C  CB  . ILE E  1 112 ? 47.990  -31.722 10.967 1.00 20.17  ? 112  ILE E CB  1 
ATOM   5278  C  CG1 . ILE E  1 112 ? 49.184  -32.680 11.065 1.00 20.82  ? 112  ILE E CG1 1 
ATOM   5279  C  CG2 . ILE E  1 112 ? 46.833  -32.364 10.198 1.00 22.95  ? 112  ILE E CG2 1 
ATOM   5280  C  CD1 . ILE E  1 112 ? 48.936  -33.944 11.851 1.00 21.53  ? 112  ILE E CD1 1 
ATOM   5281  N  N   . ILE E  1 113 ? 50.496  -29.267 10.622 1.00 21.76  ? 113  ILE E N   1 
ATOM   5282  C  CA  . ILE E  1 113 ? 51.427  -28.547 11.534 1.00 24.97  ? 113  ILE E CA  1 
ATOM   5283  C  C   . ILE E  1 113 ? 50.837  -27.183 11.842 1.00 23.23  ? 113  ILE E C   1 
ATOM   5284  O  O   . ILE E  1 113 ? 50.218  -26.463 11.053 1.00 21.55  ? 113  ILE E O   1 
ATOM   5285  C  CB  . ILE E  1 113 ? 52.834  -28.538 10.934 1.00 23.73  ? 113  ILE E CB  1 
ATOM   5286  C  CG1 . ILE E  1 113 ? 53.544  -29.906 11.123 1.00 27.60  ? 113  ILE E CG1 1 
ATOM   5287  C  CG2 . ILE E  1 113 ? 53.693  -27.424 11.501 1.00 23.23  ? 113  ILE E CG2 1 
ATOM   5288  C  CD1 . ILE E  1 113 ? 54.972  -29.891 10.636 1.00 56.05  ? 113  ILE E CD1 1 
ATOM   5289  N  N   . GLY E  1 114 ? 50.963  -26.723 13.098 1.00 17.78  ? 114  GLY E N   1 
ATOM   5290  C  CA  . GLY E  1 114 ? 50.362  -25.476 13.495 1.00 18.89  ? 114  GLY E CA  1 
ATOM   5291  C  C   . GLY E  1 114 ? 48.887  -25.606 13.855 1.00 16.74  ? 114  GLY E C   1 
ATOM   5292  O  O   . GLY E  1 114 ? 48.256  -24.614 14.204 1.00 20.97  ? 114  GLY E O   1 
ATOM   5293  N  N   . ARG E  1 115 ? 48.330  -26.808 13.744 1.00 18.29  ? 115  ARG E N   1 
ATOM   5294  C  CA  . ARG E  1 115 ? 46.949  -26.997 14.206 1.00 19.32  ? 115  ARG E CA  1 
ATOM   5295  C  C   . ARG E  1 115 ? 46.963  -27.647 15.579 1.00 22.59  ? 115  ARG E C   1 
ATOM   5296  O  O   . ARG E  1 115 ? 48.037  -27.847 16.152 1.00 21.74  ? 115  ARG E O   1 
ATOM   5297  C  CB  . ARG E  1 115 ? 46.122  -27.802 13.173 1.00 19.58  ? 115  ARG E CB  1 
ATOM   5298  C  CG  . ARG E  1 115 ? 46.176  -26.982 11.874 1.00 20.69  ? 115  ARG E CG  1 
ATOM   5299  C  CD  . ARG E  1 115 ? 45.349  -27.562 10.750 1.00 31.29  ? 115  ARG E CD  1 
ATOM   5300  N  NE  . ARG E  1 115 ? 45.520  -26.813 9.514  1.00 28.34  ? 115  ARG E NE  1 
ATOM   5301  C  CZ  . ARG E  1 115 ? 44.938  -25.730 9.060  1.00 28.45  ? 115  ARG E CZ  1 
ATOM   5302  N  NH1 . ARG E  1 115 ? 45.332  -25.293 7.859  1.00 28.16  ? 115  ARG E NH1 1 
ATOM   5303  N  NH2 . ARG E  1 115 ? 43.990  -25.064 9.700  1.00 23.78  ? 115  ARG E NH2 1 
ATOM   5304  N  N   . THR E  1 116 ? 45.807  -27.962 16.155 1.00 20.96  ? 116  THR E N   1 
ATOM   5305  C  CA  . THR E  1 116 ? 45.767  -28.418 17.547 1.00 17.33  ? 116  THR E CA  1 
ATOM   5306  C  C   . THR E  1 116 ? 45.308  -29.873 17.650 1.00 21.28  ? 116  THR E C   1 
ATOM   5307  O  O   . THR E  1 116 ? 44.287  -30.241 17.051 1.00 20.90  ? 116  THR E O   1 
ATOM   5308  C  CB  . THR E  1 116 ? 44.779  -27.554 18.356 1.00 20.66  ? 116  THR E CB  1 
ATOM   5309  O  OG1 . THR E  1 116 ? 45.298  -26.229 18.496 1.00 24.50  ? 116  THR E OG1 1 
ATOM   5310  C  CG2 . THR E  1 116 ? 44.597  -28.070 19.776 1.00 19.51  ? 116  THR E CG2 1 
ATOM   5311  N  N   . LEU E  1 117 ? 46.024  -30.702 18.383 1.00 17.74  ? 117  LEU E N   1 
ATOM   5312  C  CA  . LEU E  1 117 ? 45.626  -32.078 18.684 1.00 19.31  ? 117  LEU E CA  1 
ATOM   5313  C  C   . LEU E  1 117 ? 44.831  -32.044 19.991 1.00 20.77  ? 117  LEU E C   1 
ATOM   5314  O  O   . LEU E  1 117 ? 45.305  -31.427 20.948 1.00 19.07  ? 117  LEU E O   1 
ATOM   5315  C  CB  . LEU E  1 117 ? 46.848  -32.997 18.803 1.00 21.59  ? 117  LEU E CB  1 
ATOM   5316  C  CG  . LEU E  1 117 ? 46.614  -34.475 19.097 1.00 22.28  ? 117  LEU E CG  1 
ATOM   5317  C  CD1 . LEU E  1 117 ? 45.929  -35.134 17.903 1.00 21.43  ? 117  LEU E CD1 1 
ATOM   5318  C  CD2 . LEU E  1 117 ? 47.906  -35.225 19.418 1.00 20.45  ? 117  LEU E CD2 1 
ATOM   5319  N  N   . VAL E  1 118 ? 43.669  -32.672 20.024 1.00 20.43  ? 118  VAL E N   1 
ATOM   5320  C  CA  . VAL E  1 118 ? 42.789  -32.666 21.189 1.00 19.39  ? 118  VAL E CA  1 
ATOM   5321  C  C   . VAL E  1 118 ? 42.425  -34.073 21.622 1.00 22.83  ? 118  VAL E C   1 
ATOM   5322  O  O   . VAL E  1 118 ? 42.135  -34.899 20.742 1.00 19.96  ? 118  VAL E O   1 
ATOM   5323  C  CB  . VAL E  1 118 ? 41.487  -31.911 20.877 1.00 20.31  ? 118  VAL E CB  1 
ATOM   5324  C  CG1 . VAL E  1 118 ? 40.583  -31.920 22.099 1.00 22.34  ? 118  VAL E CG1 1 
ATOM   5325  C  CG2 . VAL E  1 118 ? 41.795  -30.474 20.451 1.00 20.69  ? 118  VAL E CG2 1 
ATOM   5326  N  N   . VAL E  1 119 ? 42.451  -34.333 22.935 1.00 17.46  ? 119  VAL E N   1 
ATOM   5327  C  CA  . VAL E  1 119 ? 41.944  -35.654 23.399 1.00 16.01  ? 119  VAL E CA  1 
ATOM   5328  C  C   . VAL E  1 119 ? 40.707  -35.352 24.238 1.00 21.11  ? 119  VAL E C   1 
ATOM   5329  O  O   . VAL E  1 119 ? 40.699  -34.346 24.972 1.00 19.38  ? 119  VAL E O   1 
ATOM   5330  C  CB  . VAL E  1 119 ? 42.978  -36.476 24.151 1.00 19.06  ? 119  VAL E CB  1 
ATOM   5331  C  CG1 . VAL E  1 119 ? 43.512  -35.742 25.388 1.00 18.77  ? 119  VAL E CG1 1 
ATOM   5332  C  CG2 . VAL E  1 119 ? 42.414  -37.848 24.531 1.00 19.80  ? 119  VAL E CG2 1 
ATOM   5333  N  N   . HIS E  1 120 ? 39.679  -36.184 24.088 1.00 20.15  ? 120  HIS E N   1 
ATOM   5334  C  CA  . HIS E  1 120 ? 38.365  -35.806 24.591 1.00 21.76  ? 120  HIS E CA  1 
ATOM   5335  C  C   . HIS E  1 120 ? 37.910  -36.614 25.804 1.00 22.65  ? 120  HIS E C   1 
ATOM   5336  O  O   . HIS E  1 120 ? 38.477  -37.647 26.125 1.00 21.36  ? 120  HIS E O   1 
ATOM   5337  C  CB  . HIS E  1 120 ? 37.301  -36.025 23.499 1.00 19.12  ? 120  HIS E CB  1 
ATOM   5338  C  CG  . HIS E  1 120 ? 37.327  -34.946 22.459 1.00 19.85  ? 120  HIS E CG  1 
ATOM   5339  N  ND1 . HIS E  1 120 ? 36.583  -33.802 22.538 1.00 21.29  ? 120  HIS E ND1 1 
ATOM   5340  C  CD2 . HIS E  1 120 ? 38.061  -34.839 21.321 1.00 19.28  ? 120  HIS E CD2 1 
ATOM   5341  C  CE1 . HIS E  1 120 ? 36.812  -33.033 21.488 1.00 27.07  ? 120  HIS E CE1 1 
ATOM   5342  N  NE2 . HIS E  1 120 ? 37.714  -33.647 20.737 1.00 21.19  ? 120  HIS E NE2 1 
ATOM   5343  N  N   . GLU E  1 121 ? 36.834  -36.090 26.393 1.00 24.90  ? 121  GLU E N   1 
ATOM   5344  C  CA  . GLU E  1 121 ? 36.200  -36.680 27.571 1.00 25.38  ? 121  GLU E CA  1 
ATOM   5345  C  C   . GLU E  1 121 ? 35.594  -38.050 27.307 1.00 20.09  ? 121  GLU E C   1 
ATOM   5346  O  O   . GLU E  1 121 ? 35.772  -38.949 28.142 1.00 24.42  ? 121  GLU E O   1 
ATOM   5347  C  CB  . GLU E  1 121 ? 35.109  -35.722 28.058 1.00 28.78  ? 121  GLU E CB  1 
ATOM   5348  C  CG  . GLU E  1 121 ? 34.241  -36.176 29.215 1.00 33.61  ? 121  GLU E CG  1 
ATOM   5349  C  CD  . GLU E  1 121 ? 32.960  -35.361 29.328 1.00 44.08  ? 121  GLU E CD  1 
ATOM   5350  O  OE1 . GLU E  1 121 ? 32.367  -35.374 30.430 1.00 60.06  ? 121  GLU E OE1 1 
ATOM   5351  O  OE2 . GLU E  1 121 ? 32.511  -34.704 28.353 1.00 35.46  ? 121  GLU E OE2 1 
ATOM   5352  N  N   . LYS E  1 122 ? 34.881  -38.169 26.201 1.00 21.79  ? 122  LYS E N   1 
ATOM   5353  C  CA  . LYS E  1 122 ? 34.175  -39.406 25.906 1.00 27.90  ? 122  LYS E CA  1 
ATOM   5354  C  C   . LYS E  1 122 ? 34.610  -40.012 24.580 1.00 26.71  ? 122  LYS E C   1 
ATOM   5355  O  O   . LYS E  1 122 ? 35.387  -39.434 23.833 1.00 23.08  ? 122  LYS E O   1 
ATOM   5356  C  CB  . LYS E  1 122 ? 32.661  -39.158 25.816 1.00 32.72  ? 122  LYS E CB  1 
ATOM   5357  C  CG  . LYS E  1 122 ? 32.070  -38.309 26.925 1.00 42.75  ? 122  LYS E CG  1 
ATOM   5358  C  CD  . LYS E  1 122 ? 30.545  -38.292 26.795 1.00 40.16  ? 122  LYS E CD  1 
ATOM   5359  C  CE  . LYS E  1 122 ? 30.098  -37.124 25.932 1.00 37.10  ? 122  LYS E CE  1 
ATOM   5360  N  NZ  . LYS E  1 122 ? 28.820  -37.391 25.217 1.00 51.65  ? 122  LYS E NZ  1 
ATOM   5361  N  N   . ALA E  1 123 ? 34.098  -41.205 24.296 1.00 26.33  ? 123  ALA E N   1 
ATOM   5362  C  CA  . ALA E  1 123 ? 34.348  -41.883 23.037 1.00 23.96  ? 123  ALA E CA  1 
ATOM   5363  C  C   . ALA E  1 123 ? 33.811  -41.088 21.857 1.00 21.80  ? 123  ALA E C   1 
ATOM   5364  O  O   . ALA E  1 123 ? 32.761  -40.450 21.945 1.00 23.36  ? 123  ALA E O   1 
ATOM   5365  C  CB  . ALA E  1 123 ? 33.679  -43.262 23.016 1.00 24.20  ? 123  ALA E CB  1 
ATOM   5366  N  N   . ASP E  1 124 ? 34.558  -41.184 20.760 1.00 20.90  ? 124  ASP E N   1 
ATOM   5367  C  CA  . ASP E  1 124 ? 34.089  -40.730 19.459 1.00 19.13  ? 124  ASP E CA  1 
ATOM   5368  C  C   . ASP E  1 124 ? 33.181  -41.799 18.834 1.00 21.28  ? 124  ASP E C   1 
ATOM   5369  O  O   . ASP E  1 124 ? 33.614  -42.934 18.673 1.00 23.94  ? 124  ASP E O   1 
ATOM   5370  C  CB  . ASP E  1 124 ? 35.272  -40.466 18.534 1.00 22.35  ? 124  ASP E CB  1 
ATOM   5371  C  CG  . ASP E  1 124 ? 34.976  -39.843 17.198 1.00 28.34  ? 124  ASP E CG  1 
ATOM   5372  O  OD1 . ASP E  1 124 ? 35.886  -39.193 16.631 1.00 25.07  ? 124  ASP E OD1 1 
ATOM   5373  O  OD2 . ASP E  1 124 ? 33.860  -39.982 16.655 1.00 24.13  ? 124  ASP E OD2 1 
ATOM   5374  N  N   . ASP E  1 125 ? 31.950  -41.458 18.497 1.00 21.78  ? 125  ASP E N   1 
ATOM   5375  C  CA  . ASP E  1 125 ? 31.008  -42.480 17.997 1.00 28.13  ? 125  ASP E CA  1 
ATOM   5376  C  C   . ASP E  1 125 ? 31.179  -42.705 16.494 1.00 31.20  ? 125  ASP E C   1 
ATOM   5377  O  O   . ASP E  1 125 ? 30.477  -43.499 15.858 1.00 23.57  ? 125  ASP E O   1 
ATOM   5378  C  CB  . ASP E  1 125 ? 29.580  -42.097 18.391 1.00 25.69  ? 125  ASP E CB  1 
ATOM   5379  C  CG  . ASP E  1 125 ? 28.959  -40.942 17.653 1.00 28.14  ? 125  ASP E CG  1 
ATOM   5380  O  OD1 . ASP E  1 125 ? 27.902  -40.421 18.102 1.00 24.59  ? 125  ASP E OD1 1 
ATOM   5381  O  OD2 . ASP E  1 125 ? 29.471  -40.492 16.595 1.00 20.64  ? 125  ASP E OD2 1 
ATOM   5382  N  N   . LEU E  1 126 ? 32.169  -42.034 15.907 1.00 22.77  ? 126  LEU E N   1 
ATOM   5383  C  CA  . LEU E  1 126 ? 32.569  -42.193 14.518 1.00 19.46  ? 126  LEU E CA  1 
ATOM   5384  C  C   . LEU E  1 126 ? 31.425  -41.854 13.548 1.00 21.66  ? 126  LEU E C   1 
ATOM   5385  O  O   . LEU E  1 126 ? 31.422  -42.383 12.433 1.00 23.90  ? 126  LEU E O   1 
ATOM   5386  C  CB  . LEU E  1 126 ? 33.093  -43.604 14.218 1.00 23.14  ? 126  LEU E CB  1 
ATOM   5387  C  CG  . LEU E  1 126 ? 34.104  -44.173 15.228 1.00 25.53  ? 126  LEU E CG  1 
ATOM   5388  C  CD1 . LEU E  1 126 ? 34.578  -45.557 14.820 1.00 26.64  ? 126  LEU E CD1 1 
ATOM   5389  C  CD2 . LEU E  1 126 ? 35.287  -43.206 15.374 1.00 21.21  ? 126  LEU E CD2 1 
ATOM   5390  N  N   . GLY E  1 127 ? 30.527  -40.966 13.950 1.00 21.59  ? 127  GLY E N   1 
ATOM   5391  C  CA  . GLY E  1 127 ? 29.503  -40.418 13.067 1.00 21.66  ? 127  GLY E CA  1 
ATOM   5392  C  C   . GLY E  1 127 ? 28.290  -41.335 13.027 1.00 25.99  ? 127  GLY E C   1 
ATOM   5393  O  O   . GLY E  1 127 ? 27.392  -41.093 12.222 1.00 25.39  ? 127  GLY E O   1 
ATOM   5394  N  N   . LYS E  1 128 ? 28.309  -42.343 13.907 1.00 21.62  ? 128  LYS E N   1 
ATOM   5395  C  CA  . LYS E  1 128 ? 27.197  -43.301 13.891 1.00 27.52  ? 128  LYS E CA  1 
ATOM   5396  C  C   . LYS E  1 128 ? 26.183  -43.131 15.018 1.00 24.86  ? 128  LYS E C   1 
ATOM   5397  O  O   . LYS E  1 128 ? 25.406  -44.080 15.239 1.00 23.70  ? 128  LYS E O   1 
ATOM   5398  C  CB  . LYS E  1 128 ? 27.781  -44.718 13.936 1.00 23.29  ? 128  LYS E CB  1 
ATOM   5399  C  CG  . LYS E  1 128 ? 28.741  -44.957 12.758 1.00 29.02  ? 128  LYS E CG  1 
ATOM   5400  C  CD  . LYS E  1 128 ? 29.432  -46.290 12.999 1.00 38.96  ? 128  LYS E CD  1 
ATOM   5401  C  CE  . LYS E  1 128 ? 28.642  -47.414 12.350 1.00 42.41  ? 128  LYS E CE  1 
ATOM   5402  N  NZ  . LYS E  1 128 ? 29.553  -48.513 11.917 1.00 70.67  ? 128  LYS E NZ  1 
ATOM   5403  N  N   . GLY E  1 129 ? 26.162  -41.995 15.680 1.00 21.45  ? 129  GLY E N   1 
ATOM   5404  C  CA  . GLY E  1 129 ? 25.292  -41.691 16.806 1.00 21.16  ? 129  GLY E CA  1 
ATOM   5405  C  C   . GLY E  1 129 ? 23.884  -41.233 16.453 1.00 27.08  ? 129  GLY E C   1 
ATOM   5406  O  O   . GLY E  1 129 ? 23.058  -41.031 17.351 1.00 26.29  ? 129  GLY E O   1 
ATOM   5407  N  N   . GLY E  1 130 ? 23.547  -41.046 15.181 1.00 20.57  ? 130  GLY E N   1 
ATOM   5408  C  CA  . GLY E  1 130 ? 22.139  -40.754 14.867 1.00 26.73  ? 130  GLY E CA  1 
ATOM   5409  C  C   . GLY E  1 130 ? 21.732  -39.319 15.070 1.00 29.47  ? 130  GLY E C   1 
ATOM   5410  O  O   . GLY E  1 130 ? 20.543  -38.989 15.041 1.00 23.77  ? 130  GLY E O   1 
ATOM   5411  N  N   . ASN E  1 131 ? 22.664  -38.371 15.243 1.00 28.01  ? 131  ASN E N   1 
ATOM   5412  C  CA  . ASN E  1 131 ? 22.219  -36.974 15.336 1.00 30.02  ? 131  ASN E CA  1 
ATOM   5413  C  C   . ASN E  1 131 ? 23.212  -36.019 14.689 1.00 33.09  ? 131  ASN E C   1 
ATOM   5414  O  O   . ASN E  1 131 ? 24.194  -36.452 14.087 1.00 30.03  ? 131  ASN E O   1 
ATOM   5415  C  CB  . ASN E  1 131 ? 21.954  -36.586 16.783 1.00 30.08  ? 131  ASN E CB  1 
ATOM   5416  C  CG  . ASN E  1 131 ? 23.090  -36.877 17.730 1.00 39.33  ? 131  ASN E CG  1 
ATOM   5417  O  OD1 . ASN E  1 131 ? 24.268  -36.940 17.358 1.00 32.18  ? 131  ASN E OD1 1 
ATOM   5418  N  ND2 . ASN E  1 131 ? 22.710  -37.056 18.983 1.00 36.98  ? 131  ASN E ND2 1 
ATOM   5419  N  N   . GLU E  1 132 ? 22.928  -34.715 14.787 1.00 30.23  ? 132  GLU E N   1 
ATOM   5420  C  CA  . GLU E  1 132 ? 23.799  -33.760 14.103 1.00 31.20  ? 132  GLU E CA  1 
ATOM   5421  C  C   . GLU E  1 132 ? 25.138  -33.681 14.816 1.00 24.12  ? 132  GLU E C   1 
ATOM   5422  O  O   . GLU E  1 132 ? 26.199  -33.522 14.216 1.00 30.20  ? 132  GLU E O   1 
ATOM   5423  C  CB  . GLU E  1 132 ? 23.141  -32.381 14.055 1.00 38.67  ? 132  GLU E CB  1 
ATOM   5424  C  CG  . GLU E  1 132 ? 22.112  -32.299 12.932 1.00 45.72  ? 132  GLU E CG  1 
ATOM   5425  C  CD  . GLU E  1 132 ? 22.749  -32.627 11.594 1.00 58.47  ? 132  GLU E CD  1 
ATOM   5426  O  OE1 . GLU E  1 132 ? 23.559  -31.794 11.123 1.00 100.83 ? 132  GLU E OE1 1 
ATOM   5427  O  OE2 . GLU E  1 132 ? 22.444  -33.698 11.027 1.00 64.67  ? 132  GLU E OE2 1 
ATOM   5428  N  N   . GLU E  1 133 ? 25.068  -33.789 16.133 1.00 25.24  ? 133  GLU E N   1 
ATOM   5429  C  CA  . GLU E  1 133 ? 26.321  -33.738 16.900 1.00 29.55  ? 133  GLU E CA  1 
ATOM   5430  C  C   . GLU E  1 133 ? 27.246  -34.870 16.482 1.00 27.24  ? 133  GLU E C   1 
ATOM   5431  O  O   . GLU E  1 133 ? 28.464  -34.739 16.350 1.00 28.98  ? 133  GLU E O   1 
ATOM   5432  C  CB  . GLU E  1 133 ? 26.001  -33.804 18.393 1.00 25.60  ? 133  GLU E CB  1 
ATOM   5433  C  CG  . GLU E  1 133 ? 27.178  -33.531 19.304 1.00 32.59  ? 133  GLU E CG  1 
ATOM   5434  C  CD  . GLU E  1 133 ? 27.637  -32.086 19.167 1.00 49.18  ? 133  GLU E CD  1 
ATOM   5435  O  OE1 . GLU E  1 133 ? 28.858  -31.881 19.030 1.00 43.24  ? 133  GLU E OE1 1 
ATOM   5436  O  OE2 . GLU E  1 133 ? 26.775  -31.184 19.190 1.00 54.28  ? 133  GLU E OE2 1 
ATOM   5437  N  N   . SER E  1 134 ? 26.678  -36.055 16.233 1.00 21.58  ? 134  SER E N   1 
ATOM   5438  C  CA  . SER E  1 134 ? 27.550  -37.148 15.835 1.00 22.88  ? 134  SER E CA  1 
ATOM   5439  C  C   . SER E  1 134 ? 28.289  -36.857 14.536 1.00 26.39  ? 134  SER E C   1 
ATOM   5440  O  O   . SER E  1 134 ? 29.440  -37.281 14.405 1.00 27.54  ? 134  SER E O   1 
ATOM   5441  C  CB  . SER E  1 134 ? 26.685  -38.403 15.635 1.00 25.07  ? 134  SER E CB  1 
ATOM   5442  O  OG  . SER E  1 134 ? 27.452  -39.476 15.130 1.00 22.01  ? 134  SER E OG  1 
ATOM   5443  N  N   . THR E  1 135 ? 27.629  -36.173 13.590 1.00 23.72  ? 135  THR E N   1 
ATOM   5444  C  CA  . THR E  1 135 ? 28.287  -35.958 12.297 1.00 22.10  ? 135  THR E CA  1 
ATOM   5445  C  C   . THR E  1 135 ? 29.089  -34.654 12.298 1.00 29.84  ? 135  THR E C   1 
ATOM   5446  O  O   . THR E  1 135 ? 29.604  -34.197 11.272 1.00 27.52  ? 135  THR E O   1 
ATOM   5447  C  CB  . THR E  1 135 ? 27.283  -35.970 11.126 1.00 34.51  ? 135  THR E CB  1 
ATOM   5448  O  OG1 . THR E  1 135 ? 26.281  -34.975 11.308 1.00 38.61  ? 135  THR E OG1 1 
ATOM   5449  C  CG2 . THR E  1 135 ? 26.574  -37.323 11.067 1.00 42.95  ? 135  THR E CG2 1 
ATOM   5450  N  N   . LYS E  1 136 ? 29.248  -34.055 13.475 1.00 27.20  ? 136  LYS E N   1 
ATOM   5451  C  CA  . LYS E  1 136 ? 30.131  -32.913 13.664 1.00 33.87  ? 136  LYS E CA  1 
ATOM   5452  C  C   . LYS E  1 136 ? 31.346  -33.252 14.528 1.00 33.16  ? 136  LYS E C   1 
ATOM   5453  O  O   . LYS E  1 136 ? 32.490  -33.008 14.111 1.00 24.88  ? 136  LYS E O   1 
ATOM   5454  C  CB  . LYS E  1 136 ? 29.340  -31.762 14.320 1.00 34.36  ? 136  LYS E CB  1 
ATOM   5455  C  CG  . LYS E  1 136 ? 28.923  -30.691 13.329 1.00 52.14  ? 136  LYS E CG  1 
ATOM   5456  C  CD  . LYS E  1 136 ? 27.952  -29.708 13.955 1.00 65.36  ? 136  LYS E CD  1 
ATOM   5457  C  CE  . LYS E  1 136 ? 26.684  -29.554 13.124 1.00 61.35  ? 136  LYS E CE  1 
ATOM   5458  N  NZ  . LYS E  1 136 ? 25.589  -28.966 13.960 1.00 66.73  ? 136  LYS E NZ  1 
ATOM   5459  N  N   . THR E  1 137 ? 31.069  -33.774 15.729 1.00 23.91  ? 137  THR E N   1 
ATOM   5460  C  CA  . THR E  1 137 ? 32.089  -34.055 16.723 1.00 22.82  ? 137  THR E CA  1 
ATOM   5461  C  C   . THR E  1 137 ? 32.164  -35.525 17.102 1.00 25.99  ? 137  THR E C   1 
ATOM   5462  O  O   . THR E  1 137 ? 33.048  -35.902 17.875 1.00 24.68  ? 137  THR E O   1 
ATOM   5463  C  CB  . THR E  1 137 ? 31.895  -33.320 18.068 1.00 29.70  ? 137  THR E CB  1 
ATOM   5464  O  OG1 . THR E  1 137 ? 30.709  -33.803 18.722 1.00 28.96  ? 137  THR E OG1 1 
ATOM   5465  C  CG2 . THR E  1 137 ? 31.706  -31.820 17.864 1.00 33.93  ? 137  THR E CG2 1 
ATOM   5466  N  N   . GLY E  1 138 ? 31.259  -36.365 16.627 1.00 21.71  ? 138  GLY E N   1 
ATOM   5467  C  CA  . GLY E  1 138 ? 31.291  -37.736 17.115 1.00 19.46  ? 138  GLY E CA  1 
ATOM   5468  C  C   . GLY E  1 138 ? 30.808  -37.825 18.557 1.00 21.25  ? 138  GLY E C   1 
ATOM   5469  O  O   . GLY E  1 138 ? 30.988  -38.870 19.198 1.00 22.50  ? 138  GLY E O   1 
ATOM   5470  N  N   . ASN E  1 139 ? 30.164  -36.798 19.105 1.00 23.04  ? 139  ASN E N   1 
ATOM   5471  C  CA  . ASN E  1 139 ? 29.704  -36.872 20.501 1.00 26.41  ? 139  ASN E CA  1 
ATOM   5472  C  C   . ASN E  1 139 ? 30.810  -37.166 21.506 1.00 26.32  ? 139  ASN E C   1 
ATOM   5473  O  O   . ASN E  1 139 ? 30.621  -37.692 22.605 1.00 24.29  ? 139  ASN E O   1 
ATOM   5474  C  CB  . ASN E  1 139 ? 28.596  -37.921 20.655 1.00 24.11  ? 139  ASN E CB  1 
ATOM   5475  C  CG  . ASN E  1 139 ? 27.269  -37.355 20.166 1.00 30.74  ? 139  ASN E CG  1 
ATOM   5476  O  OD1 . ASN E  1 139 ? 26.753  -36.351 20.674 1.00 29.83  ? 139  ASN E OD1 1 
ATOM   5477  N  ND2 . ASN E  1 139 ? 26.737  -38.028 19.152 1.00 27.85  ? 139  ASN E ND2 1 
ATOM   5478  N  N   . ALA E  1 140 ? 32.049  -36.788 21.177 1.00 23.66  ? 140  ALA E N   1 
ATOM   5479  C  CA  . ALA E  1 140 ? 33.149  -37.071 22.096 1.00 22.56  ? 140  ALA E CA  1 
ATOM   5480  C  C   . ALA E  1 140 ? 33.197  -36.130 23.293 1.00 27.99  ? 140  ALA E C   1 
ATOM   5481  O  O   . ALA E  1 140 ? 34.054  -36.342 24.168 1.00 25.68  ? 140  ALA E O   1 
ATOM   5482  C  CB  . ALA E  1 140 ? 34.488  -36.966 21.352 1.00 21.56  ? 140  ALA E CB  1 
ATOM   5483  N  N   . GLY E  1 141 ? 32.331  -35.111 23.325 1.00 24.68  ? 141  GLY E N   1 
ATOM   5484  C  CA  . GLY E  1 141 ? 32.266  -34.307 24.538 1.00 23.59  ? 141  GLY E CA  1 
ATOM   5485  C  C   . GLY E  1 141 ? 33.428  -33.350 24.747 1.00 25.24  ? 141  GLY E C   1 
ATOM   5486  O  O   . GLY E  1 141 ? 34.057  -32.837 23.827 1.00 24.53  ? 141  GLY E O   1 
ATOM   5487  N  N   . SER E  1 142 ? 33.733  -33.037 26.011 1.00 26.86  ? 142  SER E N   1 
ATOM   5488  C  CA  . SER E  1 142 ? 34.608  -31.892 26.254 1.00 25.86  ? 142  SER E CA  1 
ATOM   5489  C  C   . SER E  1 142 ? 36.062  -32.235 25.933 1.00 24.81  ? 142  SER E C   1 
ATOM   5490  O  O   . SER E  1 142 ? 36.463  -33.386 25.770 1.00 22.20  ? 142  SER E O   1 
ATOM   5491  C  CB  . SER E  1 142 ? 34.480  -31.431 27.712 1.00 26.40  ? 142  SER E CB  1 
ATOM   5492  O  OG  . SER E  1 142 ? 35.125  -32.410 28.522 1.00 36.25  ? 142  SER E OG  1 
ATOM   5493  N  N   . ARG E  1 143 ? 36.823  -31.131 25.853 1.00 22.99  ? 143  ARG E N   1 
ATOM   5494  C  CA  . ARG E  1 143 ? 38.245  -31.173 25.554 1.00 24.04  ? 143  ARG E CA  1 
ATOM   5495  C  C   . ARG E  1 143 ? 39.085  -31.266 26.817 1.00 28.15  ? 143  ARG E C   1 
ATOM   5496  O  O   . ARG E  1 143 ? 39.238  -30.329 27.594 1.00 27.64  ? 143  ARG E O   1 
ATOM   5497  C  CB  . ARG E  1 143 ? 38.551  -29.932 24.677 1.00 24.05  ? 143  ARG E CB  1 
ATOM   5498  C  CG  . ARG E  1 143 ? 37.630  -29.917 23.450 1.00 23.66  ? 143  ARG E CG  1 
ATOM   5499  C  CD  . ARG E  1 143 ? 37.861  -28.694 22.572 1.00 28.37  ? 143  ARG E CD  1 
ATOM   5500  N  NE  . ARG E  1 143 ? 36.815  -28.578 21.547 1.00 24.51  ? 143  ARG E NE  1 
ATOM   5501  C  CZ  . ARG E  1 143 ? 36.870  -27.782 20.492 1.00 24.64  ? 143  ARG E CZ  1 
ATOM   5502  N  NH1 . ARG E  1 143 ? 35.862  -27.762 19.617 1.00 22.37  ? 143  ARG E NH1 1 
ATOM   5503  N  NH2 . ARG E  1 143 ? 37.934  -27.005 20.294 1.00 24.82  ? 143  ARG E NH2 1 
ATOM   5504  N  N   . LEU E  1 144 ? 39.680  -32.431 27.071 1.00 22.02  ? 144  LEU E N   1 
ATOM   5505  C  CA  . LEU E  1 144 ? 40.426  -32.632 28.305 1.00 19.78  ? 144  LEU E CA  1 
ATOM   5506  C  C   . LEU E  1 144 ? 41.842  -32.078 28.208 1.00 24.48  ? 144  LEU E C   1 
ATOM   5507  O  O   . LEU E  1 144 ? 42.351  -31.542 29.181 1.00 22.95  ? 144  LEU E O   1 
ATOM   5508  C  CB  . LEU E  1 144 ? 40.531  -34.108 28.647 1.00 20.25  ? 144  LEU E CB  1 
ATOM   5509  C  CG  . LEU E  1 144 ? 39.181  -34.837 28.829 1.00 25.15  ? 144  LEU E CG  1 
ATOM   5510  C  CD1 . LEU E  1 144 ? 39.435  -36.185 29.485 1.00 27.97  ? 144  LEU E CD1 1 
ATOM   5511  C  CD2 . LEU E  1 144 ? 38.212  -33.989 29.620 1.00 27.91  ? 144  LEU E CD2 1 
ATOM   5512  N  N   . ALA E  1 145 ? 42.478  -32.219 27.042 1.00 21.04  ? 145  ALA E N   1 
ATOM   5513  C  CA  . ALA E  1 145 ? 43.833  -31.667 26.905 1.00 18.95  ? 145  ALA E CA  1 
ATOM   5514  C  C   . ALA E  1 145 ? 44.101  -31.441 25.410 1.00 26.53  ? 145  ALA E C   1 
ATOM   5515  O  O   . ALA E  1 145 ? 43.483  -32.103 24.572 1.00 20.54  ? 145  ALA E O   1 
ATOM   5516  C  CB  . ALA E  1 145 ? 44.873  -32.578 27.513 1.00 20.52  ? 145  ALA E CB  1 
ATOM   5517  N  N   . CYS E  1 146 ? 45.008  -30.507 25.136 1.00 18.91  ? 146  CYS E N   1 
ATOM   5518  C  CA  . CYS E  1 146 ? 45.282  -30.160 23.740 1.00 17.69  ? 146  CYS E CA  1 
ATOM   5519  C  C   . CYS E  1 146 ? 46.691  -29.581 23.656 1.00 21.62  ? 146  CYS E C   1 
ATOM   5520  O  O   . CYS E  1 146 ? 47.289  -29.260 24.683 1.00 19.89  ? 146  CYS E O   1 
ATOM   5521  C  CB  A CYS E  1 146 ? 44.264  -29.204 23.145 0.44 19.84  ? 146  CYS E CB  1 
ATOM   5522  C  CB  B CYS E  1 146 ? 44.212  -29.179 23.273 0.56 25.92  ? 146  CYS E CB  1 
ATOM   5523  S  SG  A CYS E  1 146 ? 43.881  -27.728 24.098 0.44 35.07  ? 146  CYS E SG  1 
ATOM   5524  S  SG  B CYS E  1 146 ? 44.327  -27.481 23.864 0.56 20.49  ? 146  CYS E SG  1 
ATOM   5525  N  N   . GLY E  1 147 ? 47.213  -29.463 22.457 1.00 20.02  ? 147  GLY E N   1 
ATOM   5526  C  CA  . GLY E  1 147 ? 48.526  -28.843 22.230 1.00 21.30  ? 147  GLY E CA  1 
ATOM   5527  C  C   . GLY E  1 147 ? 48.625  -28.474 20.755 1.00 21.45  ? 147  GLY E C   1 
ATOM   5528  O  O   . GLY E  1 147 ? 47.952  -29.127 19.963 1.00 19.53  ? 147  GLY E O   1 
ATOM   5529  N  N   . VAL E  1 148 ? 49.449  -27.491 20.427 1.00 21.23  ? 148  VAL E N   1 
ATOM   5530  C  CA  . VAL E  1 148 ? 49.710  -27.172 19.030 1.00 17.06  ? 148  VAL E CA  1 
ATOM   5531  C  C   . VAL E  1 148 ? 50.711  -28.155 18.451 1.00 21.08  ? 148  VAL E C   1 
ATOM   5532  O  O   . VAL E  1 148 ? 51.686  -28.553 19.101 1.00 21.48  ? 148  VAL E O   1 
ATOM   5533  C  CB  . VAL E  1 148 ? 50.257  -25.731 18.915 1.00 18.39  ? 148  VAL E CB  1 
ATOM   5534  C  CG1 . VAL E  1 148 ? 50.503  -25.330 17.467 1.00 17.57  ? 148  VAL E CG1 1 
ATOM   5535  C  CG2 . VAL E  1 148 ? 49.267  -24.810 19.607 1.00 21.83  ? 148  VAL E CG2 1 
ATOM   5536  N  N   . ILE E  1 149 ? 50.477  -28.569 17.205 1.00 17.84  ? 149  ILE E N   1 
ATOM   5537  C  CA  . ILE E  1 149 ? 51.378  -29.553 16.593 1.00 19.28  ? 149  ILE E CA  1 
ATOM   5538  C  C   . ILE E  1 149 ? 52.582  -28.823 16.022 1.00 20.69  ? 149  ILE E C   1 
ATOM   5539  O  O   . ILE E  1 149 ? 52.414  -27.961 15.170 1.00 21.31  ? 149  ILE E O   1 
ATOM   5540  C  CB  . ILE E  1 149 ? 50.595  -30.356 15.541 1.00 23.90  ? 149  ILE E CB  1 
ATOM   5541  C  CG1 . ILE E  1 149 ? 49.509  -31.216 16.217 1.00 20.12  ? 149  ILE E CG1 1 
ATOM   5542  C  CG2 . ILE E  1 149 ? 51.461  -31.257 14.691 1.00 21.62  ? 149  ILE E CG2 1 
ATOM   5543  C  CD1 . ILE E  1 149 ? 48.479  -31.757 15.218 1.00 22.43  ? 149  ILE E CD1 1 
ATOM   5544  N  N   . GLY E  1 150 ? 53.782  -29.101 16.487 1.00 17.96  ? 150  GLY E N   1 
ATOM   5545  C  CA  . GLY E  1 150 ? 54.958  -28.322 16.087 1.00 18.88  ? 150  GLY E CA  1 
ATOM   5546  C  C   . GLY E  1 150 ? 55.979  -29.170 15.354 1.00 21.20  ? 150  GLY E C   1 
ATOM   5547  O  O   . GLY E  1 150 ? 56.067  -30.391 15.519 1.00 22.73  ? 150  GLY E O   1 
ATOM   5548  N  N   . ILE E  1 151 ? 56.792  -28.510 14.528 1.00 19.36  ? 151  ILE E N   1 
ATOM   5549  C  CA  . ILE E  1 151 ? 57.870  -29.174 13.811 1.00 21.62  ? 151  ILE E CA  1 
ATOM   5550  C  C   . ILE E  1 151 ? 58.937  -29.714 14.743 1.00 19.73  ? 151  ILE E C   1 
ATOM   5551  O  O   . ILE E  1 151 ? 59.342  -29.001 15.663 1.00 26.52  ? 151  ILE E O   1 
ATOM   5552  C  CB  . ILE E  1 151 ? 58.519  -28.182 12.807 1.00 24.77  ? 151  ILE E CB  1 
ATOM   5553  C  CG1 . ILE E  1 151 ? 57.557  -27.806 11.694 1.00 27.53  ? 151  ILE E CG1 1 
ATOM   5554  C  CG2 . ILE E  1 151 ? 59.827  -28.773 12.284 1.00 29.03  ? 151  ILE E CG2 1 
ATOM   5555  C  CD1 . ILE E  1 151 ? 57.818  -26.525 10.938 1.00 27.99  ? 151  ILE E CD1 1 
ATOM   5556  N  N   . ALA E  1 152 ? 59.378  -30.956 14.548 1.00 20.34  ? 152  ALA E N   1 
ATOM   5557  C  CA  . ALA E  1 152 ? 60.324  -31.595 15.442 1.00 19.71  ? 152  ALA E CA  1 
ATOM   5558  C  C   . ALA E  1 152 ? 61.608  -31.955 14.691 1.00 24.79  ? 152  ALA E C   1 
ATOM   5559  O  O   . ALA E  1 152 ? 61.581  -32.027 13.468 1.00 26.10  ? 152  ALA E O   1 
ATOM   5560  C  CB  . ALA E  1 152 ? 59.742  -32.848 16.092 1.00 22.34  ? 152  ALA E CB  1 
ATOM   5561  N  N   . GLN E  1 153 ? 62.663  -32.157 15.473 1.00 22.46  ? 153  GLN E N   1 
ATOM   5562  C  CA  . GLN E  1 153 ? 63.985  -32.349 14.893 1.00 27.94  ? 153  GLN E CA  1 
ATOM   5563  C  C   . GLN E  1 153 ? 64.050  -33.664 14.138 1.00 42.72  ? 153  GLN E C   1 
ATOM   5564  O  O   . GLN E  1 153 ? 63.622  -34.649 14.778 1.00 42.37  ? 153  GLN E O   1 
ATOM   5565  C  CB  . GLN E  1 153 ? 65.044  -32.343 15.996 1.00 26.10  ? 153  GLN E CB  1 
ATOM   5566  C  CG  . GLN E  1 153 ? 66.451  -32.378 15.390 1.00 32.64  ? 153  GLN E CG  1 
ATOM   5567  C  CD  . GLN E  1 153 ? 67.492  -32.129 16.467 1.00 37.04  ? 153  GLN E CD  1 
ATOM   5568  O  OE1 . GLN E  1 153 ? 68.467  -31.434 16.198 1.00 53.57  ? 153  GLN E OE1 1 
ATOM   5569  N  NE2 . GLN E  1 153 ? 67.300  -32.691 17.654 1.00 36.63  ? 153  GLN E NE2 1 
ATOM   5570  O  OXT . GLN E  1 153 ? 64.516  -33.633 12.985 1.00 53.93  ? 153  GLN E OXT 1 
ATOM   5571  N  N   . ALA F  1 1   ? 44.293  -13.732 3.717  1.00 104.96 ? 1    ALA F N   1 
ATOM   5572  C  CA  . ALA F  1 1   ? 45.334  -13.244 4.620  1.00 77.93  ? 1    ALA F CA  1 
ATOM   5573  C  C   . ALA F  1 1   ? 45.558  -14.196 5.788  1.00 61.44  ? 1    ALA F C   1 
ATOM   5574  O  O   . ALA F  1 1   ? 44.697  -14.483 6.624  1.00 51.69  ? 1    ALA F O   1 
ATOM   5575  C  CB  . ALA F  1 1   ? 44.988  -11.847 5.119  1.00 83.17  ? 1    ALA F CB  1 
ATOM   5576  N  N   . THR F  1 2   ? 46.778  -14.722 5.870  1.00 47.50  ? 2    THR F N   1 
ATOM   5577  C  CA  . THR F  1 2   ? 47.028  -15.689 6.937  1.00 42.65  ? 2    THR F CA  1 
ATOM   5578  C  C   . THR F  1 2   ? 47.163  -14.964 8.277  1.00 36.38  ? 2    THR F C   1 
ATOM   5579  O  O   . THR F  1 2   ? 47.600  -13.813 8.391  1.00 30.08  ? 2    THR F O   1 
ATOM   5580  C  CB  . THR F  1 2   ? 48.260  -16.552 6.616  1.00 49.11  ? 2    THR F CB  1 
ATOM   5581  O  OG1 . THR F  1 2   ? 48.509  -16.503 5.209  1.00 60.14  ? 2    THR F OG1 1 
ATOM   5582  C  CG2 . THR F  1 2   ? 48.023  -18.020 6.945  1.00 60.39  ? 2    THR F CG2 1 
ATOM   5583  N  N   . LYS F  1 3   ? 46.725  -15.691 9.304  1.00 28.40  ? 3    LYS F N   1 
ATOM   5584  C  CA  . LYS F  1 3   ? 46.790  -15.236 10.691 1.00 24.55  ? 3    LYS F CA  1 
ATOM   5585  C  C   . LYS F  1 3   ? 47.379  -16.375 11.522 1.00 22.42  ? 3    LYS F C   1 
ATOM   5586  O  O   . LYS F  1 3   ? 47.122  -17.552 11.257 1.00 24.18  ? 3    LYS F O   1 
ATOM   5587  C  CB  . LYS F  1 3   ? 45.451  -14.818 11.272 1.00 33.64  ? 3    LYS F CB  1 
ATOM   5588  C  CG  . LYS F  1 3   ? 44.878  -13.575 10.600 1.00 42.08  ? 3    LYS F CG  1 
ATOM   5589  C  CD  . LYS F  1 3   ? 43.767  -12.961 11.447 1.00 47.74  ? 3    LYS F CD  1 
ATOM   5590  C  CE  . LYS F  1 3   ? 43.792  -11.445 11.288 1.00 58.68  ? 3    LYS F CE  1 
ATOM   5591  N  NZ  . LYS F  1 3   ? 44.029  -11.053 9.868  1.00 75.64  ? 3    LYS F NZ  1 
ATOM   5592  N  N   . ALA F  1 4   ? 48.171  -15.998 12.515 1.00 24.51  ? 4    ALA F N   1 
ATOM   5593  C  CA  . ALA F  1 4   ? 48.723  -17.002 13.418 1.00 17.12  ? 4    ALA F CA  1 
ATOM   5594  C  C   . ALA F  1 4   ? 48.709  -16.408 14.822 1.00 22.87  ? 4    ALA F C   1 
ATOM   5595  O  O   . ALA F  1 4   ? 48.488  -15.197 14.991 1.00 21.30  ? 4    ALA F O   1 
ATOM   5596  C  CB  . ALA F  1 4   ? 50.107  -17.427 12.980 1.00 19.96  ? 4    ALA F CB  1 
ATOM   5597  N  N   . VAL F  1 5   ? 48.933  -17.262 15.803 1.00 22.17  ? 5    VAL F N   1 
ATOM   5598  C  CA  . VAL F  1 5   ? 48.886  -16.786 17.190 1.00 20.55  ? 5    VAL F CA  1 
ATOM   5599  C  C   . VAL F  1 5   ? 49.812  -17.644 18.044 1.00 21.09  ? 5    VAL F C   1 
ATOM   5600  O  O   . VAL F  1 5   ? 50.099  -18.789 17.671 1.00 21.05  ? 5    VAL F O   1 
ATOM   5601  C  CB  . VAL F  1 5   ? 47.451  -16.815 17.746 1.00 19.95  ? 5    VAL F CB  1 
ATOM   5602  C  CG1 . VAL F  1 5   ? 46.979  -18.255 17.873 1.00 21.28  ? 5    VAL F CG1 1 
ATOM   5603  C  CG2 . VAL F  1 5   ? 47.393  -16.094 19.082 1.00 21.94  ? 5    VAL F CG2 1 
ATOM   5604  N  N   . CYS F  1 6   ? 50.280  -17.092 19.173 1.00 20.15  ? 6    CYS F N   1 
ATOM   5605  C  CA  . CYS F  1 6   ? 51.177  -17.880 20.021 1.00 19.33  ? 6    CYS F CA  1 
ATOM   5606  C  C   . CYS F  1 6   ? 50.908  -17.552 21.485 1.00 15.46  ? 6    CYS F C   1 
ATOM   5607  O  O   . CYS F  1 6   ? 50.849  -16.367 21.812 1.00 19.53  ? 6    CYS F O   1 
ATOM   5608  C  CB  . CYS F  1 6   ? 52.627  -17.545 19.645 1.00 19.68  ? 6    CYS F CB  1 
ATOM   5609  S  SG  . CYS F  1 6   ? 53.880  -18.364 20.654 1.00 24.55  ? 6    CYS F SG  1 
ATOM   5610  N  N   . VAL F  1 7   ? 50.772  -18.574 22.304 1.00 18.65  ? 7    VAL F N   1 
ATOM   5611  C  CA  . VAL F  1 7   ? 50.599  -18.324 23.743 1.00 19.22  ? 7    VAL F CA  1 
ATOM   5612  C  C   . VAL F  1 7   ? 51.944  -18.598 24.402 1.00 22.62  ? 7    VAL F C   1 
ATOM   5613  O  O   . VAL F  1 7   ? 52.414  -19.731 24.331 1.00 21.83  ? 7    VAL F O   1 
ATOM   5614  C  CB  . VAL F  1 7   ? 49.493  -19.213 24.315 1.00 26.61  ? 7    VAL F CB  1 
ATOM   5615  C  CG1 . VAL F  1 7   ? 49.343  -19.033 25.823 1.00 23.01  ? 7    VAL F CG1 1 
ATOM   5616  C  CG2 . VAL F  1 7   ? 48.171  -18.907 23.624 1.00 21.40  ? 7    VAL F CG2 1 
ATOM   5617  N  N   . LEU F  1 8   ? 52.580  -17.590 25.002 1.00 22.52  ? 8    LEU F N   1 
ATOM   5618  C  CA  . LEU F  1 8   ? 53.839  -17.807 25.679 1.00 17.41  ? 8    LEU F CA  1 
ATOM   5619  C  C   . LEU F  1 8   ? 53.692  -18.165 27.162 1.00 19.06  ? 8    LEU F C   1 
ATOM   5620  O  O   . LEU F  1 8   ? 52.926  -17.491 27.851 1.00 23.23  ? 8    LEU F O   1 
ATOM   5621  C  CB  . LEU F  1 8   ? 54.686  -16.524 25.600 1.00 24.74  ? 8    LEU F CB  1 
ATOM   5622  C  CG  . LEU F  1 8   ? 55.018  -15.987 24.204 1.00 30.17  ? 8    LEU F CG  1 
ATOM   5623  C  CD1 . LEU F  1 8   ? 55.411  -14.517 24.214 1.00 37.73  ? 8    LEU F CD1 1 
ATOM   5624  C  CD2 . LEU F  1 8   ? 56.177  -16.794 23.639 1.00 30.76  ? 8    LEU F CD2 1 
ATOM   5625  N  N   . LYS F  1 9   ? 54.424  -19.178 27.600 1.00 20.81  ? 9    LYS F N   1 
ATOM   5626  C  CA  . LYS F  1 9   ? 54.445  -19.633 28.978 1.00 25.04  ? 9    LYS F CA  1 
ATOM   5627  C  C   . LYS F  1 9   ? 55.810  -20.182 29.312 1.00 23.54  ? 9    LYS F C   1 
ATOM   5628  O  O   . LYS F  1 9   ? 56.525  -20.602 28.405 1.00 22.43  ? 9    LYS F O   1 
ATOM   5629  C  CB  . LYS F  1 9   ? 53.455  -20.783 29.234 1.00 28.98  ? 9    LYS F CB  1 
ATOM   5630  C  CG  . LYS F  1 9   ? 52.029  -20.490 28.811 1.00 46.81  ? 9    LYS F CG  1 
ATOM   5631  C  CD  . LYS F  1 9   ? 51.381  -19.549 29.811 1.00 67.49  ? 9    LYS F CD  1 
ATOM   5632  C  CE  . LYS F  1 9   ? 50.154  -18.886 29.201 1.00 70.15  ? 9    LYS F CE  1 
ATOM   5633  N  NZ  . LYS F  1 9   ? 50.395  -17.451 28.899 1.00 43.21  ? 9    LYS F NZ  1 
ATOM   5634  N  N   . GLY F  1 10  ? 56.163  -20.233 30.597 1.00 22.68  ? 10   GLY F N   1 
ATOM   5635  C  CA  . GLY F  1 10  ? 57.477  -20.777 30.916 1.00 21.75  ? 10   GLY F CA  1 
ATOM   5636  C  C   . GLY F  1 10  ? 57.480  -21.191 32.388 1.00 27.58  ? 10   GLY F C   1 
ATOM   5637  O  O   . GLY F  1 10  ? 56.400  -21.314 32.956 1.00 34.05  ? 10   GLY F O   1 
ATOM   5638  N  N   . ASP F  1 11  ? 58.651  -21.415 32.974 1.00 27.37  ? 11   ASP F N   1 
ATOM   5639  C  CA  . ASP F  1 11  ? 58.654  -21.904 34.357 1.00 33.53  ? 11   ASP F CA  1 
ATOM   5640  C  C   . ASP F  1 11  ? 58.395  -20.797 35.360 1.00 37.91  ? 11   ASP F C   1 
ATOM   5641  O  O   . ASP F  1 11  ? 58.002  -21.018 36.509 1.00 36.96  ? 11   ASP F O   1 
ATOM   5642  C  CB  . ASP F  1 11  ? 59.990  -22.586 34.648 1.00 37.87  ? 11   ASP F CB  1 
ATOM   5643  C  CG  . ASP F  1 11  ? 60.131  -23.893 33.885 1.00 54.41  ? 11   ASP F CG  1 
ATOM   5644  O  OD1 . ASP F  1 11  ? 61.268  -24.277 33.545 1.00 74.86  ? 11   ASP F OD1 1 
ATOM   5645  O  OD2 . ASP F  1 11  ? 59.097  -24.537 33.628 1.00 46.98  ? 11   ASP F OD2 1 
ATOM   5646  N  N   . GLY F  1 12  ? 58.606  -19.551 34.943 1.00 28.23  ? 12   GLY F N   1 
ATOM   5647  C  CA  . GLY F  1 12  ? 58.408  -18.434 35.847 1.00 27.21  ? 12   GLY F CA  1 
ATOM   5648  C  C   . GLY F  1 12  ? 57.093  -17.742 35.554 1.00 27.30  ? 12   GLY F C   1 
ATOM   5649  O  O   . GLY F  1 12  ? 56.155  -18.373 35.056 1.00 33.36  ? 12   GLY F O   1 
ATOM   5650  N  N   . PRO F  1 13  ? 57.012  -16.456 35.861 1.00 26.21  ? 13   PRO F N   1 
ATOM   5651  C  CA  . PRO F  1 13  ? 55.802  -15.683 35.674 1.00 22.44  ? 13   PRO F CA  1 
ATOM   5652  C  C   . PRO F  1 13  ? 55.614  -15.094 34.289 1.00 27.84  ? 13   PRO F C   1 
ATOM   5653  O  O   . PRO F  1 13  ? 54.585  -14.459 34.079 1.00 26.05  ? 13   PRO F O   1 
ATOM   5654  C  CB  . PRO F  1 13  ? 56.027  -14.469 36.623 1.00 29.35  ? 13   PRO F CB  1 
ATOM   5655  C  CG  . PRO F  1 13  ? 57.502  -14.268 36.522 1.00 29.67  ? 13   PRO F CG  1 
ATOM   5656  C  CD  . PRO F  1 13  ? 58.112  -15.647 36.454 1.00 28.39  ? 13   PRO F CD  1 
ATOM   5657  N  N   . VAL F  1 14  ? 56.553  -15.269 33.346 1.00 27.07  ? 14   VAL F N   1 
ATOM   5658  C  CA  . VAL F  1 14  ? 56.332  -14.594 32.051 1.00 21.26  ? 14   VAL F CA  1 
ATOM   5659  C  C   . VAL F  1 14  ? 55.226  -15.269 31.251 1.00 20.87  ? 14   VAL F C   1 
ATOM   5660  O  O   . VAL F  1 14  ? 55.249  -16.486 31.097 1.00 23.40  ? 14   VAL F O   1 
ATOM   5661  C  CB  . VAL F  1 14  ? 57.645  -14.553 31.238 1.00 23.48  ? 14   VAL F CB  1 
ATOM   5662  C  CG1 . VAL F  1 14  ? 57.491  -13.822 29.911 1.00 21.01  ? 14   VAL F CG1 1 
ATOM   5663  C  CG2 . VAL F  1 14  ? 58.754  -13.912 32.071 1.00 23.20  ? 14   VAL F CG2 1 
ATOM   5664  N  N   . GLN F  1 15  ? 54.281  -14.505 30.742 1.00 25.72  ? 15   GLN F N   1 
ATOM   5665  C  CA  . GLN F  1 15  ? 53.153  -15.023 29.998 1.00 24.93  ? 15   GLN F CA  1 
ATOM   5666  C  C   . GLN F  1 15  ? 52.752  -14.021 28.946 1.00 22.06  ? 15   GLN F C   1 
ATOM   5667  O  O   . GLN F  1 15  ? 52.834  -12.824 29.219 1.00 23.27  ? 15   GLN F O   1 
ATOM   5668  C  CB  . GLN F  1 15  ? 51.927  -15.194 30.907 1.00 31.80  ? 15   GLN F CB  1 
ATOM   5669  C  CG  . GLN F  1 15  ? 52.017  -16.344 31.886 1.00 47.65  ? 15   GLN F CG  1 
ATOM   5670  C  CD  . GLN F  1 15  ? 50.901  -16.329 32.917 1.00 60.85  ? 15   GLN F CD  1 
ATOM   5671  O  OE1 . GLN F  1 15  ? 50.410  -15.275 33.333 1.00 45.97  ? 15   GLN F OE1 1 
ATOM   5672  N  NE2 . GLN F  1 15  ? 50.496  -17.520 33.352 1.00 93.83  ? 15   GLN F NE2 1 
ATOM   5673  N  N   . GLY F  1 16  ? 52.270  -14.445 27.779 1.00 20.80  ? 16   GLY F N   1 
ATOM   5674  C  CA  . GLY F  1 16  ? 51.855  -13.426 26.834 1.00 20.68  ? 16   GLY F CA  1 
ATOM   5675  C  C   . GLY F  1 16  ? 51.079  -14.065 25.690 1.00 22.81  ? 16   GLY F C   1 
ATOM   5676  O  O   . GLY F  1 16  ? 51.080  -15.284 25.576 1.00 24.59  ? 16   GLY F O   1 
ATOM   5677  N  N   . ILE F  1 17  ? 50.471  -13.226 24.882 1.00 22.74  ? 17   ILE F N   1 
ATOM   5678  C  CA  . ILE F  1 17  ? 49.804  -13.647 23.662 1.00 22.58  ? 17   ILE F CA  1 
ATOM   5679  C  C   . ILE F  1 17  ? 50.328  -12.765 22.535 1.00 26.61  ? 17   ILE F C   1 
ATOM   5680  O  O   . ILE F  1 17  ? 50.281  -11.523 22.666 1.00 24.00  ? 17   ILE F O   1 
ATOM   5681  C  CB  . ILE F  1 17  ? 48.267  -13.522 23.765 1.00 22.72  ? 17   ILE F CB  1 
ATOM   5682  C  CG1 . ILE F  1 17  ? 47.696  -14.388 24.885 1.00 26.21  ? 17   ILE F CG1 1 
ATOM   5683  C  CG2 . ILE F  1 17  ? 47.664  -13.785 22.398 1.00 24.58  ? 17   ILE F CG2 1 
ATOM   5684  C  CD1 . ILE F  1 17  ? 46.192  -14.262 25.109 1.00 28.02  ? 17   ILE F CD1 1 
ATOM   5685  N  N   . ILE F  1 18  ? 50.843  -13.445 21.512 1.00 21.98  ? 18   ILE F N   1 
ATOM   5686  C  CA  . ILE F  1 18  ? 51.312  -12.720 20.337 1.00 18.33  ? 18   ILE F CA  1 
ATOM   5687  C  C   . ILE F  1 18  ? 50.568  -13.162 19.073 1.00 18.47  ? 18   ILE F C   1 
ATOM   5688  O  O   . ILE F  1 18  ? 50.492  -14.351 18.764 1.00 20.61  ? 18   ILE F O   1 
ATOM   5689  C  CB  . ILE F  1 18  ? 52.825  -12.932 20.193 1.00 19.66  ? 18   ILE F CB  1 
ATOM   5690  C  CG1 . ILE F  1 18  ? 53.604  -12.443 21.429 1.00 20.35  ? 18   ILE F CG1 1 
ATOM   5691  C  CG2 . ILE F  1 18  ? 53.328  -12.294 18.911 1.00 25.26  ? 18   ILE F CG2 1 
ATOM   5692  C  CD1 . ILE F  1 18  ? 53.694  -10.921 21.499 1.00 23.07  ? 18   ILE F CD1 1 
ATOM   5693  N  N   . ASN F  1 19  ? 50.037  -12.183 18.362 1.00 21.86  ? 19   ASN F N   1 
ATOM   5694  C  CA  . ASN F  1 19  ? 49.357  -12.280 17.074 1.00 22.29  ? 19   ASN F CA  1 
ATOM   5695  C  C   . ASN F  1 19  ? 50.279  -12.012 15.902 1.00 24.72  ? 19   ASN F C   1 
ATOM   5696  O  O   . ASN F  1 19  ? 51.196  -11.190 15.971 1.00 24.20  ? 19   ASN F O   1 
ATOM   5697  C  CB  . ASN F  1 19  ? 48.193  -11.269 17.072 1.00 23.52  ? 19   ASN F CB  1 
ATOM   5698  C  CG  . ASN F  1 19  ? 47.322  -11.507 18.293 1.00 27.70  ? 19   ASN F CG  1 
ATOM   5699  O  OD1 . ASN F  1 19  ? 46.612  -12.507 18.342 1.00 27.12  ? 19   ASN F OD1 1 
ATOM   5700  N  ND2 . ASN F  1 19  ? 47.405  -10.626 19.270 1.00 32.31  ? 19   ASN F ND2 1 
ATOM   5701  N  N   . PHE F  1 20  ? 50.062  -12.703 14.789 1.00 21.06  ? 20   PHE F N   1 
ATOM   5702  C  CA  . PHE F  1 20  ? 50.771  -12.513 13.540 1.00 20.73  ? 20   PHE F CA  1 
ATOM   5703  C  C   . PHE F  1 20  ? 49.742  -12.339 12.417 1.00 25.88  ? 20   PHE F C   1 
ATOM   5704  O  O   . PHE F  1 20  ? 48.762  -13.085 12.417 1.00 24.55  ? 20   PHE F O   1 
ATOM   5705  C  CB  . PHE F  1 20  ? 51.633  -13.700 13.143 1.00 19.06  ? 20   PHE F CB  1 
ATOM   5706  C  CG  . PHE F  1 20  ? 52.701  -14.096 14.142 1.00 26.31  ? 20   PHE F CG  1 
ATOM   5707  C  CD1 . PHE F  1 20  ? 54.024  -13.740 13.961 1.00 26.80  ? 20   PHE F CD1 1 
ATOM   5708  C  CD2 . PHE F  1 20  ? 52.371  -14.831 15.270 1.00 27.12  ? 20   PHE F CD2 1 
ATOM   5709  C  CE1 . PHE F  1 20  ? 54.973  -14.128 14.901 1.00 28.74  ? 20   PHE F CE1 1 
ATOM   5710  C  CE2 . PHE F  1 20  ? 53.313  -15.231 16.197 1.00 21.90  ? 20   PHE F CE2 1 
ATOM   5711  C  CZ  . PHE F  1 20  ? 54.639  -14.882 16.011 1.00 21.43  ? 20   PHE F CZ  1 
ATOM   5712  N  N   . GLU F  1 21  ? 49.999  -11.428 11.505 1.00 23.48  ? 21   GLU F N   1 
ATOM   5713  C  CA  . GLU F  1 21  ? 49.098  -11.321 10.358 1.00 23.42  ? 21   GLU F CA  1 
ATOM   5714  C  C   . GLU F  1 21  ? 49.898  -10.920 9.122  1.00 24.54  ? 21   GLU F C   1 
ATOM   5715  O  O   . GLU F  1 21  ? 50.756  -10.041 9.158  1.00 31.23  ? 21   GLU F O   1 
ATOM   5716  C  CB  . GLU F  1 21  ? 47.980  -10.327 10.596 1.00 29.78  ? 21   GLU F CB  1 
ATOM   5717  C  CG  . GLU F  1 21  ? 47.044  -10.171 9.401  1.00 34.74  ? 21   GLU F CG  1 
ATOM   5718  C  CD  . GLU F  1 21  ? 46.223  -8.900  9.565  1.00 53.19  ? 21   GLU F CD  1 
ATOM   5719  O  OE1 . GLU F  1 21  ? 45.264  -8.936  10.361 1.00 45.03  ? 21   GLU F OE1 1 
ATOM   5720  O  OE2 . GLU F  1 21  ? 46.574  -7.898  8.909  1.00 78.70  ? 21   GLU F OE2 1 
ATOM   5721  N  N   . GLN F  1 22  ? 49.577  -11.615 8.046  1.00 24.28  ? 22   GLN F N   1 
ATOM   5722  C  CA  . GLN F  1 22  ? 50.207  -11.405 6.749  1.00 27.73  ? 22   GLN F CA  1 
ATOM   5723  C  C   . GLN F  1 22  ? 49.085  -11.226 5.720  1.00 32.13  ? 22   GLN F C   1 
ATOM   5724  O  O   . GLN F  1 22  ? 48.507  -12.243 5.346  1.00 32.69  ? 22   GLN F O   1 
ATOM   5725  C  CB  . GLN F  1 22  ? 51.114  -12.565 6.377  1.00 26.75  ? 22   GLN F CB  1 
ATOM   5726  C  CG  . GLN F  1 22  ? 52.088  -12.287 5.245  1.00 25.26  ? 22   GLN F CG  1 
ATOM   5727  C  CD  . GLN F  1 22  ? 53.011  -13.433 4.948  1.00 28.11  ? 22   GLN F CD  1 
ATOM   5728  O  OE1 . GLN F  1 22  ? 52.693  -14.590 5.244  1.00 29.42  ? 22   GLN F OE1 1 
ATOM   5729  N  NE2 . GLN F  1 22  ? 54.172  -13.128 4.363  1.00 32.09  ? 22   GLN F NE2 1 
ATOM   5730  N  N   . LYS F  1 23  ? 48.826  -9.987  5.361  1.00 39.11  ? 23   LYS F N   1 
ATOM   5731  C  CA  . LYS F  1 23  ? 47.780  -9.630  4.411  1.00 48.50  ? 23   LYS F CA  1 
ATOM   5732  C  C   . LYS F  1 23  ? 48.047  -10.235 3.031  1.00 49.06  ? 23   LYS F C   1 
ATOM   5733  O  O   . LYS F  1 23  ? 47.100  -10.571 2.317  1.00 61.80  ? 23   LYS F O   1 
ATOM   5734  C  CB  . LYS F  1 23  ? 47.664  -8.118  4.253  1.00 55.09  ? 23   LYS F CB  1 
ATOM   5735  C  CG  . LYS F  1 23  ? 47.069  -7.342  5.410  1.00 69.41  ? 23   LYS F CG  1 
ATOM   5736  C  CD  . LYS F  1 23  ? 47.077  -5.850  5.092  1.00 74.66  ? 23   LYS F CD  1 
ATOM   5737  C  CE  . LYS F  1 23  ? 47.594  -4.995  6.233  1.00 65.83  ? 23   LYS F CE  1 
ATOM   5738  N  NZ  . LYS F  1 23  ? 48.512  -3.915  5.774  1.00 68.04  ? 23   LYS F NZ  1 
ATOM   5739  N  N   . GLU F  1 24  ? 49.314  -10.364 2.651  1.00 40.60  ? 24   GLU F N   1 
ATOM   5740  C  CA  . GLU F  1 24  ? 49.700  -10.856 1.339  1.00 41.14  ? 24   GLU F CA  1 
ATOM   5741  C  C   . GLU F  1 24  ? 50.852  -11.837 1.447  1.00 46.97  ? 24   GLU F C   1 
ATOM   5742  O  O   . GLU F  1 24  ? 51.781  -11.613 2.222  1.00 48.86  ? 24   GLU F O   1 
ATOM   5743  C  CB  . GLU F  1 24  ? 50.111  -9.701  0.414  1.00 48.54  ? 24   GLU F CB  1 
ATOM   5744  C  CG  . GLU F  1 24  ? 48.920  -8.891  -0.068 1.00 61.38  ? 24   GLU F CG  1 
ATOM   5745  C  CD  . GLU F  1 24  ? 47.797  -9.745  -0.637 1.00 79.44  ? 24   GLU F CD  1 
ATOM   5746  O  OE1 . GLU F  1 24  ? 46.674  -9.202  -0.791 1.00 91.35  ? 24   GLU F OE1 1 
ATOM   5747  O  OE2 . GLU F  1 24  ? 48.011  -10.943 -0.934 1.00 84.14  ? 24   GLU F OE2 1 
ATOM   5748  N  N   . SER F  1 25  ? 50.778  -12.908 0.661  1.00 41.91  ? 25   SER F N   1 
ATOM   5749  C  CA  . SER F  1 25  ? 51.801  -13.947 0.757  1.00 44.08  ? 25   SER F CA  1 
ATOM   5750  C  C   . SER F  1 25  ? 53.178  -13.380 0.447  1.00 48.79  ? 25   SER F C   1 
ATOM   5751  O  O   . SER F  1 25  ? 54.208  -13.887 0.898  1.00 53.65  ? 25   SER F O   1 
ATOM   5752  C  CB  . SER F  1 25  ? 51.417  -15.105 -0.163 1.00 59.60  ? 25   SER F CB  1 
ATOM   5753  O  OG  . SER F  1 25  ? 52.240  -15.249 -1.300 1.00 72.53  ? 25   SER F OG  1 
ATOM   5754  N  N   . ASN F  1 26  ? 53.210  -12.309 -0.341 1.00 47.06  ? 26   ASN F N   1 
ATOM   5755  C  CA  . ASN F  1 26  ? 54.466  -11.686 -0.742 1.00 61.34  ? 26   ASN F CA  1 
ATOM   5756  C  C   . ASN F  1 26  ? 54.782  -10.492 0.151  1.00 67.14  ? 26   ASN F C   1 
ATOM   5757  O  O   . ASN F  1 26  ? 55.504  -9.578  -0.257 1.00 82.24  ? 26   ASN F O   1 
ATOM   5758  C  CB  . ASN F  1 26  ? 54.385  -11.235 -2.206 1.00 66.11  ? 26   ASN F CB  1 
ATOM   5759  C  CG  . ASN F  1 26  ? 53.459  -10.050 -2.424 1.00 74.10  ? 26   ASN F CG  1 
ATOM   5760  O  OD1 . ASN F  1 26  ? 52.359  -9.952  -1.870 1.00 79.94  ? 26   ASN F OD1 1 
ATOM   5761  N  ND2 . ASN F  1 26  ? 53.884  -9.100  -3.259 1.00 72.44  ? 26   ASN F ND2 1 
ATOM   5762  N  N   . GLY F  1 27  ? 54.213  -10.493 1.361  1.00 55.88  ? 27   GLY F N   1 
ATOM   5763  C  CA  . GLY F  1 27  ? 54.207  -9.287  2.163  1.00 41.99  ? 27   GLY F CA  1 
ATOM   5764  C  C   . GLY F  1 27  ? 54.766  -9.407  3.565  1.00 31.64  ? 27   GLY F C   1 
ATOM   5765  O  O   . GLY F  1 27  ? 55.164  -10.482 4.020  1.00 40.40  ? 27   GLY F O   1 
ATOM   5766  N  N   . PRO F  1 28  ? 54.800  -8.254  4.220  1.00 38.35  ? 28   PRO F N   1 
ATOM   5767  C  CA  . PRO F  1 28  ? 55.325  -8.186  5.582  1.00 32.70  ? 28   PRO F CA  1 
ATOM   5768  C  C   . PRO F  1 28  ? 54.336  -8.839  6.542  1.00 31.62  ? 28   PRO F C   1 
ATOM   5769  O  O   . PRO F  1 28  ? 53.135  -8.884  6.249  1.00 28.08  ? 28   PRO F O   1 
ATOM   5770  C  CB  . PRO F  1 28  ? 55.405  -6.691  5.881  1.00 40.46  ? 28   PRO F CB  1 
ATOM   5771  C  CG  . PRO F  1 28  ? 54.552  -6.002  4.867  1.00 42.84  ? 28   PRO F CG  1 
ATOM   5772  C  CD  . PRO F  1 28  ? 54.344  -6.941  3.719  1.00 40.41  ? 28   PRO F CD  1 
ATOM   5773  N  N   . VAL F  1 29  ? 54.887  -9.315  7.645  1.00 28.49  ? 29   VAL F N   1 
ATOM   5774  C  CA  . VAL F  1 29  ? 54.106  -9.885  8.733  1.00 25.45  ? 29   VAL F CA  1 
ATOM   5775  C  C   . VAL F  1 29  ? 54.012  -8.889  9.877  1.00 26.22  ? 29   VAL F C   1 
ATOM   5776  O  O   . VAL F  1 29  ? 55.065  -8.417  10.325 1.00 31.01  ? 29   VAL F O   1 
ATOM   5777  C  CB  . VAL F  1 29  ? 54.722  -11.207 9.239  1.00 26.89  ? 29   VAL F CB  1 
ATOM   5778  C  CG1 . VAL F  1 29  ? 53.846  -11.804 10.353 1.00 25.71  ? 29   VAL F CG1 1 
ATOM   5779  C  CG2 . VAL F  1 29  ? 54.884  -12.209 8.112  1.00 24.40  ? 29   VAL F CG2 1 
ATOM   5780  N  N   . LYS F  1 30  ? 52.807  -8.570  10.323 1.00 24.51  ? 30   LYS F N   1 
ATOM   5781  C  CA  . LYS F  1 30  ? 52.609  -7.736  11.502 1.00 26.74  ? 30   LYS F CA  1 
ATOM   5782  C  C   . LYS F  1 30  ? 52.596  -8.592  12.766 1.00 28.63  ? 30   LYS F C   1 
ATOM   5783  O  O   . LYS F  1 30  ? 51.897  -9.602  12.784 1.00 24.96  ? 30   LYS F O   1 
ATOM   5784  C  CB  . LYS F  1 30  ? 51.303  -6.971  11.390 1.00 25.73  ? 30   LYS F CB  1 
ATOM   5785  C  CG  . LYS F  1 30  ? 51.304  -5.950  10.267 1.00 43.92  ? 30   LYS F CG  1 
ATOM   5786  C  CD  . LYS F  1 30  ? 49.908  -5.349  10.111 1.00 61.77  ? 30   LYS F CD  1 
ATOM   5787  C  CE  . LYS F  1 30  ? 49.743  -4.754  8.721  1.00 76.94  ? 30   LYS F CE  1 
ATOM   5788  N  NZ  . LYS F  1 30  ? 49.869  -3.271  8.704  1.00 81.31  ? 30   LYS F NZ  1 
ATOM   5789  N  N   . VAL F  1 31  ? 53.360  -8.234  13.790 1.00 25.10  ? 31   VAL F N   1 
ATOM   5790  C  CA  . VAL F  1 31  ? 53.479  -9.048  14.995 1.00 25.62  ? 31   VAL F CA  1 
ATOM   5791  C  C   . VAL F  1 31  ? 53.127  -8.176  16.182 1.00 28.51  ? 31   VAL F C   1 
ATOM   5792  O  O   . VAL F  1 31  ? 53.808  -7.167  16.399 1.00 29.11  ? 31   VAL F O   1 
ATOM   5793  C  CB  . VAL F  1 31  ? 54.906  -9.606  15.197 1.00 25.72  ? 31   VAL F CB  1 
ATOM   5794  C  CG1 . VAL F  1 31  ? 54.969  -10.496 16.437 1.00 22.14  ? 31   VAL F CG1 1 
ATOM   5795  C  CG2 . VAL F  1 31  ? 55.374  -10.344 13.962 1.00 22.16  ? 31   VAL F CG2 1 
ATOM   5796  N  N   . TRP F  1 32  ? 52.085  -8.521  16.932 1.00 21.04  ? 32   TRP F N   1 
ATOM   5797  C  CA  . TRP F  1 32  ? 51.722  -7.635  18.024 1.00 23.08  ? 32   TRP F CA  1 
ATOM   5798  C  C   . TRP F  1 32  ? 51.014  -8.431  19.114 1.00 25.33  ? 32   TRP F C   1 
ATOM   5799  O  O   . TRP F  1 32  ? 50.428  -9.476  18.850 1.00 24.80  ? 32   TRP F O   1 
ATOM   5800  C  CB  . TRP F  1 32  ? 50.827  -6.508  17.502 1.00 26.65  ? 32   TRP F CB  1 
ATOM   5801  C  CG  . TRP F  1 32  ? 49.412  -6.959  17.265 1.00 30.17  ? 32   TRP F CG  1 
ATOM   5802  C  CD1 . TRP F  1 32  ? 48.350  -6.776  18.112 1.00 38.04  ? 32   TRP F CD1 1 
ATOM   5803  C  CD2 . TRP F  1 32  ? 48.909  -7.663  16.128 1.00 32.21  ? 32   TRP F CD2 1 
ATOM   5804  N  NE1 . TRP F  1 32  ? 47.219  -7.328  17.563 1.00 38.50  ? 32   TRP F NE1 1 
ATOM   5805  C  CE2 . TRP F  1 32  ? 47.528  -7.878  16.345 1.00 32.97  ? 32   TRP F CE2 1 
ATOM   5806  C  CE3 . TRP F  1 32  ? 49.474  -8.147  14.939 1.00 36.27  ? 32   TRP F CE3 1 
ATOM   5807  C  CZ2 . TRP F  1 32  ? 46.702  -8.542  15.433 1.00 33.66  ? 32   TRP F CZ2 1 
ATOM   5808  C  CZ3 . TRP F  1 32  ? 48.652  -8.802  14.038 1.00 40.95  ? 32   TRP F CZ3 1 
ATOM   5809  C  CH2 . TRP F  1 32  ? 47.284  -9.001  14.273 1.00 33.12  ? 32   TRP F CH2 1 
ATOM   5810  N  N   . GLY F  1 33  ? 51.057  -7.884  20.312 1.00 23.01  ? 33   GLY F N   1 
ATOM   5811  C  CA  . GLY F  1 33  ? 50.405  -8.465  21.475 1.00 19.98  ? 33   GLY F CA  1 
ATOM   5812  C  C   . GLY F  1 33  ? 51.089  -7.967  22.733 1.00 24.06  ? 33   GLY F C   1 
ATOM   5813  O  O   . GLY F  1 33  ? 51.734  -6.925  22.753 1.00 30.61  ? 33   GLY F O   1 
ATOM   5814  N  N   . SER F  1 34  ? 50.916  -8.705  23.810 1.00 26.98  ? 34   SER F N   1 
ATOM   5815  C  CA  . SER F  1 34  ? 51.366  -8.251  25.116 1.00 30.94  ? 34   SER F CA  1 
ATOM   5816  C  C   . SER F  1 34  ? 52.126  -9.340  25.845 1.00 28.48  ? 34   SER F C   1 
ATOM   5817  O  O   . SER F  1 34  ? 51.667  -10.498 25.826 1.00 28.84  ? 34   SER F O   1 
ATOM   5818  C  CB  . SER F  1 34  ? 50.112  -7.862  25.909 1.00 29.26  ? 34   SER F CB  1 
ATOM   5819  O  OG  . SER F  1 34  ? 50.436  -6.914  26.902 1.00 46.63  ? 34   SER F OG  1 
ATOM   5820  N  N   . ILE F  1 35  ? 53.249  -9.022  26.473 1.00 21.93  ? 35   ILE F N   1 
ATOM   5821  C  CA  . ILE F  1 35  ? 53.929  -10.011 27.317 1.00 21.83  ? 35   ILE F CA  1 
ATOM   5822  C  C   . ILE F  1 35  ? 54.079  -9.430  28.728 1.00 28.91  ? 35   ILE F C   1 
ATOM   5823  O  O   . ILE F  1 35  ? 54.566  -8.296  28.837 1.00 28.41  ? 35   ILE F O   1 
ATOM   5824  C  CB  . ILE F  1 35  ? 55.301  -10.411 26.754 1.00 26.28  ? 35   ILE F CB  1 
ATOM   5825  C  CG1 . ILE F  1 35  ? 55.244  -10.785 25.262 1.00 25.50  ? 35   ILE F CG1 1 
ATOM   5826  C  CG2 . ILE F  1 35  ? 55.940  -11.541 27.545 1.00 26.07  ? 35   ILE F CG2 1 
ATOM   5827  C  CD1 . ILE F  1 35  ? 56.626  -11.001 24.679 1.00 25.46  ? 35   ILE F CD1 1 
ATOM   5828  N  N   . LYS F  1 36  ? 53.645  -10.170 29.748 1.00 22.95  ? 36   LYS F N   1 
ATOM   5829  C  CA  . LYS F  1 36  ? 53.763  -9.669  31.121 1.00 23.39  ? 36   LYS F CA  1 
ATOM   5830  C  C   . LYS F  1 36  ? 54.677  -10.525 31.951 1.00 25.29  ? 36   LYS F C   1 
ATOM   5831  O  O   . LYS F  1 36  ? 55.153  -11.597 31.577 1.00 25.82  ? 36   LYS F O   1 
ATOM   5832  C  CB  . LYS F  1 36  ? 52.384  -9.551  31.783 1.00 29.91  ? 36   LYS F CB  1 
ATOM   5833  C  CG  . LYS F  1 36  ? 51.646  -10.848 32.055 1.00 33.53  ? 36   LYS F CG  1 
ATOM   5834  C  CD  . LYS F  1 36  ? 50.242  -10.525 32.611 1.00 40.88  ? 36   LYS F CD  1 
ATOM   5835  C  CE  . LYS F  1 36  ? 49.278  -11.661 32.351 1.00 50.95  ? 36   LYS F CE  1 
ATOM   5836  N  NZ  . LYS F  1 36  ? 47.838  -11.263 32.337 1.00 42.43  ? 36   LYS F NZ  1 
ATOM   5837  N  N   . GLY F  1 37  ? 55.014  -10.032 33.164 1.00 24.71  ? 37   GLY F N   1 
ATOM   5838  C  CA  . GLY F  1 37  ? 55.915  -10.801 33.986 1.00 20.32  ? 37   GLY F CA  1 
ATOM   5839  C  C   . GLY F  1 37  ? 57.398  -10.566 33.720 1.00 20.87  ? 37   GLY F C   1 
ATOM   5840  O  O   . GLY F  1 37  ? 58.203  -11.354 34.200 1.00 24.61  ? 37   GLY F O   1 
ATOM   5841  N  N   . LEU F  1 38  ? 57.780  -9.533  32.992 1.00 23.21  ? 38   LEU F N   1 
ATOM   5842  C  CA  . LEU F  1 38  ? 59.138  -9.274  32.566 1.00 24.68  ? 38   LEU F CA  1 
ATOM   5843  C  C   . LEU F  1 38  ? 59.836  -8.178  33.373 1.00 32.38  ? 38   LEU F C   1 
ATOM   5844  O  O   . LEU F  1 38  ? 59.116  -7.246  33.752 1.00 25.73  ? 38   LEU F O   1 
ATOM   5845  C  CB  . LEU F  1 38  ? 59.127  -8.780  31.108 1.00 23.98  ? 38   LEU F CB  1 
ATOM   5846  C  CG  . LEU F  1 38  ? 58.808  -9.862  30.059 1.00 24.33  ? 38   LEU F CG  1 
ATOM   5847  C  CD1 . LEU F  1 38  ? 58.553  -9.184  28.717 1.00 25.33  ? 38   LEU F CD1 1 
ATOM   5848  C  CD2 . LEU F  1 38  ? 59.934  -10.894 30.008 1.00 19.96  ? 38   LEU F CD2 1 
ATOM   5849  N  N   . THR F  1 39  ? 61.142  -8.280  33.563 1.00 30.26  ? 39   THR F N   1 
ATOM   5850  C  CA  . THR F  1 39  ? 61.885  -7.131  34.136 1.00 29.20  ? 39   THR F CA  1 
ATOM   5851  C  C   . THR F  1 39  ? 61.923  -5.983  33.144 1.00 33.90  ? 39   THR F C   1 
ATOM   5852  O  O   . THR F  1 39  ? 61.918  -6.137  31.911 1.00 29.03  ? 39   THR F O   1 
ATOM   5853  C  CB  . THR F  1 39  ? 63.288  -7.573  34.576 1.00 29.11  ? 39   THR F CB  1 
ATOM   5854  O  OG1 . THR F  1 39  ? 64.001  -8.122  33.453 1.00 42.39  ? 39   THR F OG1 1 
ATOM   5855  C  CG2 . THR F  1 39  ? 63.225  -8.738  35.555 1.00 31.06  ? 39   THR F CG2 1 
ATOM   5856  N  N   . GLU F  1 40  ? 61.927  -4.746  33.667 1.00 27.91  ? 40   GLU F N   1 
ATOM   5857  C  CA  . GLU F  1 40  ? 61.868  -3.583  32.792 1.00 27.57  ? 40   GLU F CA  1 
ATOM   5858  C  C   . GLU F  1 40  ? 63.075  -3.601  31.857 1.00 30.03  ? 40   GLU F C   1 
ATOM   5859  O  O   . GLU F  1 40  ? 64.148  -4.016  32.300 1.00 33.12  ? 40   GLU F O   1 
ATOM   5860  C  CB  . GLU F  1 40  ? 61.829  -2.291  33.604 1.00 34.24  ? 40   GLU F CB  1 
ATOM   5861  C  CG  . GLU F  1 40  ? 61.674  -1.009  32.794 1.00 36.67  ? 40   GLU F CG  1 
ATOM   5862  C  CD  . GLU F  1 40  ? 61.813  0.229   33.674 1.00 50.81  ? 40   GLU F CD  1 
ATOM   5863  O  OE1 . GLU F  1 40  ? 61.687  1.368   33.173 1.00 49.20  ? 40   GLU F OE1 1 
ATOM   5864  O  OE2 . GLU F  1 40  ? 62.061  0.084   34.892 1.00 53.86  ? 40   GLU F OE2 1 
ATOM   5865  N  N   . GLY F  1 41  ? 62.916  -3.201  30.602 1.00 30.46  ? 41   GLY F N   1 
ATOM   5866  C  CA  . GLY F  1 41  ? 64.057  -3.142  29.687 1.00 30.62  ? 41   GLY F CA  1 
ATOM   5867  C  C   . GLY F  1 41  ? 63.945  -4.094  28.515 1.00 25.69  ? 41   GLY F C   1 
ATOM   5868  O  O   . GLY F  1 41  ? 62.870  -4.608  28.227 1.00 25.03  ? 41   GLY F O   1 
ATOM   5869  N  N   . LEU F  1 42  ? 65.056  -4.326  27.832 1.00 25.17  ? 42   LEU F N   1 
ATOM   5870  C  CA  . LEU F  1 42  ? 65.052  -5.076  26.577 1.00 24.45  ? 42   LEU F CA  1 
ATOM   5871  C  C   . LEU F  1 42  ? 65.122  -6.573  26.772 1.00 25.36  ? 42   LEU F C   1 
ATOM   5872  O  O   . LEU F  1 42  ? 65.859  -7.037  27.643 1.00 23.24  ? 42   LEU F O   1 
ATOM   5873  C  CB  . LEU F  1 42  ? 66.279  -4.689  25.733 1.00 22.36  ? 42   LEU F CB  1 
ATOM   5874  C  CG  . LEU F  1 42  ? 66.328  -3.258  25.216 1.00 29.14  ? 42   LEU F CG  1 
ATOM   5875  C  CD1 . LEU F  1 42  ? 67.735  -2.983  24.651 1.00 32.05  ? 42   LEU F CD1 1 
ATOM   5876  C  CD2 . LEU F  1 42  ? 65.249  -2.969  24.184 1.00 24.67  ? 42   LEU F CD2 1 
ATOM   5877  N  N   . HIS F  1 43  ? 64.415  -7.352  25.955 1.00 22.12  ? 43   HIS F N   1 
ATOM   5878  C  CA  . HIS F  1 43  ? 64.475  -8.809  26.062 1.00 22.39  ? 43   HIS F CA  1 
ATOM   5879  C  C   . HIS F  1 43  ? 64.539  -9.380  24.653 1.00 18.92  ? 43   HIS F C   1 
ATOM   5880  O  O   . HIS F  1 43  ? 63.665  -9.005  23.865 1.00 19.04  ? 43   HIS F O   1 
ATOM   5881  C  CB  . HIS F  1 43  ? 63.220  -9.365  26.770 1.00 24.90  ? 43   HIS F CB  1 
ATOM   5882  C  CG  . HIS F  1 43  ? 63.201  -8.952  28.212 1.00 25.29  ? 43   HIS F CG  1 
ATOM   5883  N  ND1 . HIS F  1 43  ? 63.734  -9.739  29.200 1.00 26.97  ? 43   HIS F ND1 1 
ATOM   5884  C  CD2 . HIS F  1 43  ? 62.727  -7.821  28.805 1.00 27.60  ? 43   HIS F CD2 1 
ATOM   5885  C  CE1 . HIS F  1 43  ? 63.587  -9.100  30.356 1.00 27.82  ? 43   HIS F CE1 1 
ATOM   5886  N  NE2 . HIS F  1 43  ? 62.983  -7.940  30.158 1.00 24.41  ? 43   HIS F NE2 1 
ATOM   5887  N  N   . GLY F  1 44  ? 65.500  -10.242 24.370 1.00 19.01  ? 44   GLY F N   1 
ATOM   5888  C  CA  . GLY F  1 44  ? 65.600  -10.869 23.053 1.00 18.57  ? 44   GLY F CA  1 
ATOM   5889  C  C   . GLY F  1 44  ? 64.326  -11.608 22.677 1.00 23.34  ? 44   GLY F C   1 
ATOM   5890  O  O   . GLY F  1 44  ? 63.603  -12.121 23.532 1.00 18.14  ? 44   GLY F O   1 
ATOM   5891  N  N   . PHE F  1 45  ? 64.029  -11.669 21.375 1.00 19.89  ? 45   PHE F N   1 
ATOM   5892  C  CA  . PHE F  1 45  ? 62.701  -12.156 20.927 1.00 18.07  ? 45   PHE F CA  1 
ATOM   5893  C  C   . PHE F  1 45  ? 62.879  -12.833 19.587 1.00 18.07  ? 45   PHE F C   1 
ATOM   5894  O  O   . PHE F  1 45  ? 63.191  -12.163 18.607 1.00 19.12  ? 45   PHE F O   1 
ATOM   5895  C  CB  . PHE F  1 45  ? 61.786  -10.970 20.820 1.00 18.75  ? 45   PHE F CB  1 
ATOM   5896  C  CG  . PHE F  1 45  ? 60.316  -11.192 20.543 1.00 20.75  ? 45   PHE F CG  1 
ATOM   5897  C  CD1 . PHE F  1 45  ? 59.552  -11.934 21.441 1.00 23.09  ? 45   PHE F CD1 1 
ATOM   5898  C  CD2 . PHE F  1 45  ? 59.741  -10.634 19.419 1.00 21.86  ? 45   PHE F CD2 1 
ATOM   5899  C  CE1 . PHE F  1 45  ? 58.194  -12.084 21.202 1.00 22.62  ? 45   PHE F CE1 1 
ATOM   5900  C  CE2 . PHE F  1 45  ? 58.386  -10.798 19.168 1.00 21.96  ? 45   PHE F CE2 1 
ATOM   5901  C  CZ  . PHE F  1 45  ? 57.624  -11.516 20.080 1.00 22.02  ? 45   PHE F CZ  1 
ATOM   5902  N  N   . HIS F  1 46  ? 62.796  -14.159 19.518 1.00 16.08  ? 46   HIS F N   1 
ATOM   5903  C  CA  . HIS F  1 46  ? 63.103  -14.826 18.253 1.00 16.18  ? 46   HIS F CA  1 
ATOM   5904  C  C   . HIS F  1 46  ? 62.155  -15.982 17.978 1.00 23.62  ? 46   HIS F C   1 
ATOM   5905  O  O   . HIS F  1 46  ? 61.590  -16.589 18.887 1.00 19.50  ? 46   HIS F O   1 
ATOM   5906  C  CB  . HIS F  1 46  ? 64.514  -15.470 18.249 1.00 20.75  ? 46   HIS F CB  1 
ATOM   5907  C  CG  . HIS F  1 46  ? 65.525  -14.664 19.014 1.00 18.11  ? 46   HIS F CG  1 
ATOM   5908  N  ND1 . HIS F  1 46  ? 65.993  -15.012 20.252 1.00 22.42  ? 46   HIS F ND1 1 
ATOM   5909  C  CD2 . HIS F  1 46  ? 66.083  -13.469 18.693 1.00 18.48  ? 46   HIS F CD2 1 
ATOM   5910  C  CE1 . HIS F  1 46  ? 66.843  -14.078 20.664 1.00 22.17  ? 46   HIS F CE1 1 
ATOM   5911  N  NE2 . HIS F  1 46  ? 66.920  -13.129 19.739 1.00 21.37  ? 46   HIS F NE2 1 
ATOM   5912  N  N   . VAL F  1 47  ? 62.058  -16.362 16.703 1.00 19.92  ? 47   VAL F N   1 
ATOM   5913  C  CA  . VAL F  1 47  ? 61.516  -17.675 16.364 1.00 15.94  ? 47   VAL F CA  1 
ATOM   5914  C  C   . VAL F  1 47  ? 62.605  -18.727 16.343 1.00 23.43  ? 47   VAL F C   1 
ATOM   5915  O  O   . VAL F  1 47  ? 63.599  -18.535 15.617 1.00 19.32  ? 47   VAL F O   1 
ATOM   5916  C  CB  . VAL F  1 47  ? 60.820  -17.619 14.981 1.00 20.13  ? 47   VAL F CB  1 
ATOM   5917  C  CG1 . VAL F  1 47  ? 60.219  -18.999 14.669 1.00 22.04  ? 47   VAL F CG1 1 
ATOM   5918  C  CG2 . VAL F  1 47  ? 59.768  -16.520 14.964 1.00 21.24  ? 47   VAL F CG2 1 
ATOM   5919  N  N   . HIS F  1 48  ? 62.442  -19.814 17.081 1.00 18.75  ? 48   HIS F N   1 
ATOM   5920  C  CA  . HIS F  1 48  ? 63.374  -20.927 17.116 1.00 15.72  ? 48   HIS F CA  1 
ATOM   5921  C  C   . HIS F  1 48  ? 62.893  -22.075 16.254 1.00 22.70  ? 48   HIS F C   1 
ATOM   5922  O  O   . HIS F  1 48  ? 61.711  -22.108 15.915 1.00 21.55  ? 48   HIS F O   1 
ATOM   5923  C  CB  . HIS F  1 48  ? 63.578  -21.406 18.562 1.00 19.51  ? 48   HIS F CB  1 
ATOM   5924  C  CG  . HIS F  1 48  ? 64.344  -20.417 19.396 1.00 19.12  ? 48   HIS F CG  1 
ATOM   5925  N  ND1 . HIS F  1 48  ? 65.477  -20.764 20.083 1.00 18.95  ? 48   HIS F ND1 1 
ATOM   5926  C  CD2 . HIS F  1 48  ? 64.128  -19.113 19.681 1.00 19.31  ? 48   HIS F CD2 1 
ATOM   5927  C  CE1 . HIS F  1 48  ? 65.955  -19.727 20.749 1.00 19.72  ? 48   HIS F CE1 1 
ATOM   5928  N  NE2 . HIS F  1 48  ? 65.156  -18.712 20.528 1.00 16.65  ? 48   HIS F NE2 1 
ATOM   5929  N  N   . GLU F  1 49  ? 63.780  -22.990 15.911 1.00 21.34  ? 49   GLU F N   1 
ATOM   5930  C  CA  . GLU F  1 49  ? 63.546  -23.924 14.828 1.00 21.26  ? 49   GLU F CA  1 
ATOM   5931  C  C   . GLU F  1 49  ? 62.438  -24.930 15.091 1.00 25.52  ? 49   GLU F C   1 
ATOM   5932  O  O   . GLU F  1 49  ? 61.639  -25.261 14.200 1.00 23.17  ? 49   GLU F O   1 
ATOM   5933  C  CB  . GLU F  1 49  ? 64.868  -24.689 14.551 1.00 23.03  ? 49   GLU F CB  1 
ATOM   5934  C  CG  . GLU F  1 49  ? 64.718  -25.534 13.285 1.00 26.54  ? 49   GLU F CG  1 
ATOM   5935  C  CD  . GLU F  1 49  ? 66.000  -26.273 12.951 1.00 31.89  ? 49   GLU F CD  1 
ATOM   5936  O  OE1 . GLU F  1 49  ? 65.985  -27.118 12.021 1.00 29.40  ? 49   GLU F OE1 1 
ATOM   5937  O  OE2 . GLU F  1 49  ? 67.001  -26.024 13.660 1.00 31.76  ? 49   GLU F OE2 1 
ATOM   5938  N  N   . PHE F  1 50  ? 62.363  -25.454 16.314 1.00 21.06  ? 50   PHE F N   1 
ATOM   5939  C  CA  . PHE F  1 50  ? 61.464  -26.590 16.530 1.00 20.69  ? 50   PHE F CA  1 
ATOM   5940  C  C   . PHE F  1 50  ? 60.275  -26.217 17.402 1.00 23.72  ? 50   PHE F C   1 
ATOM   5941  O  O   . PHE F  1 50  ? 60.434  -25.542 18.431 1.00 19.71  ? 50   PHE F O   1 
ATOM   5942  C  CB  . PHE F  1 50  ? 62.240  -27.739 17.204 1.00 20.82  ? 50   PHE F CB  1 
ATOM   5943  C  CG  . PHE F  1 50  ? 63.416  -28.189 16.346 1.00 21.44  ? 50   PHE F CG  1 
ATOM   5944  C  CD1 . PHE F  1 50  ? 63.160  -28.615 15.048 1.00 26.43  ? 50   PHE F CD1 1 
ATOM   5945  C  CD2 . PHE F  1 50  ? 64.701  -28.162 16.839 1.00 30.87  ? 50   PHE F CD2 1 
ATOM   5946  C  CE1 . PHE F  1 50  ? 64.219  -29.025 14.251 1.00 29.29  ? 50   PHE F CE1 1 
ATOM   5947  C  CE2 . PHE F  1 50  ? 65.774  -28.575 16.045 1.00 22.63  ? 50   PHE F CE2 1 
ATOM   5948  C  CZ  . PHE F  1 50  ? 65.502  -28.982 14.764 1.00 23.72  ? 50   PHE F CZ  1 
ATOM   5949  N  N   . GLY F  1 51  ? 59.088  -26.677 17.006 1.00 21.48  ? 51   GLY F N   1 
ATOM   5950  C  CA  . GLY F  1 51  ? 57.901  -26.460 17.836 1.00 21.50  ? 51   GLY F CA  1 
ATOM   5951  C  C   . GLY F  1 51  ? 57.744  -27.590 18.836 1.00 25.18  ? 51   GLY F C   1 
ATOM   5952  O  O   . GLY F  1 51  ? 56.730  -28.284 18.936 1.00 20.77  ? 51   GLY F O   1 
ATOM   5953  N  N   . ASP F  1 52  ? 58.806  -27.787 19.603 1.00 22.61  ? 52   ASP F N   1 
ATOM   5954  C  CA  . ASP F  1 52  ? 58.945  -28.926 20.495 1.00 22.24  ? 52   ASP F CA  1 
ATOM   5955  C  C   . ASP F  1 52  ? 59.031  -28.430 21.929 1.00 23.78  ? 52   ASP F C   1 
ATOM   5956  O  O   . ASP F  1 52  ? 60.068  -27.883 22.286 1.00 24.07  ? 52   ASP F O   1 
ATOM   5957  C  CB  . ASP F  1 52  ? 60.201  -29.722 20.121 1.00 23.31  ? 52   ASP F CB  1 
ATOM   5958  C  CG  . ASP F  1 52  ? 60.389  -30.995 20.919 1.00 24.15  ? 52   ASP F CG  1 
ATOM   5959  O  OD1 . ASP F  1 52  ? 61.071  -31.926 20.413 1.00 24.31  ? 52   ASP F OD1 1 
ATOM   5960  O  OD2 . ASP F  1 52  ? 59.879  -31.073 22.049 1.00 24.77  ? 52   ASP F OD2 1 
ATOM   5961  N  N   . ASN F  1 53  ? 57.984  -28.638 22.719 1.00 20.50  ? 53   ASN F N   1 
ATOM   5962  C  CA  . ASN F  1 53  ? 58.070  -28.178 24.112 1.00 21.05  ? 53   ASN F CA  1 
ATOM   5963  C  C   . ASN F  1 53  ? 58.239  -29.340 25.075 1.00 22.18  ? 53   ASN F C   1 
ATOM   5964  O  O   . ASN F  1 53  ? 57.897  -29.163 26.249 1.00 25.49  ? 53   ASN F O   1 
ATOM   5965  C  CB  . ASN F  1 53  ? 56.809  -27.374 24.414 1.00 24.36  ? 53   ASN F CB  1 
ATOM   5966  C  CG  . ASN F  1 53  ? 56.841  -26.604 25.712 1.00 40.61  ? 53   ASN F CG  1 
ATOM   5967  O  OD1 . ASN F  1 53  ? 55.920  -26.763 26.515 1.00 46.62  ? 53   ASN F OD1 1 
ATOM   5968  N  ND2 . ASN F  1 53  ? 57.861  -25.778 25.904 1.00 37.07  ? 53   ASN F ND2 1 
ATOM   5969  N  N   . THR F  1 54  ? 58.764  -30.470 24.603 1.00 20.19  ? 54   THR F N   1 
ATOM   5970  C  CA  . THR F  1 54  ? 58.839  -31.652 25.455 1.00 20.62  ? 54   THR F CA  1 
ATOM   5971  C  C   . THR F  1 54  ? 59.781  -31.428 26.637 1.00 29.34  ? 54   THR F C   1 
ATOM   5972  O  O   . THR F  1 54  ? 59.554  -32.094 27.650 1.00 30.52  ? 54   THR F O   1 
ATOM   5973  C  CB  . THR F  1 54  ? 59.275  -32.947 24.742 1.00 23.48  ? 54   THR F CB  1 
ATOM   5974  O  OG1 . THR F  1 54  ? 60.561  -32.739 24.146 1.00 24.70  ? 54   THR F OG1 1 
ATOM   5975  C  CG2 . THR F  1 54  ? 58.279  -33.301 23.647 1.00 24.35  ? 54   THR F CG2 1 
ATOM   5976  N  N   . ALA F  1 55  ? 60.764  -30.547 26.547 1.00 25.65  ? 55   ALA F N   1 
ATOM   5977  C  CA  . ALA F  1 55  ? 61.624  -30.230 27.702 1.00 26.21  ? 55   ALA F CA  1 
ATOM   5978  C  C   . ALA F  1 55  ? 61.660  -28.731 27.959 1.00 31.52  ? 55   ALA F C   1 
ATOM   5979  O  O   . ALA F  1 55  ? 62.672  -28.058 28.146 1.00 42.01  ? 55   ALA F O   1 
ATOM   5980  C  CB  . ALA F  1 55  ? 63.014  -30.787 27.477 1.00 29.94  ? 55   ALA F CB  1 
ATOM   5981  N  N   . GLY F  1 56  ? 60.472  -28.142 27.971 1.00 26.09  ? 56   GLY F N   1 
ATOM   5982  C  CA  . GLY F  1 56  ? 60.334  -26.708 28.168 1.00 26.93  ? 56   GLY F CA  1 
ATOM   5983  C  C   . GLY F  1 56  ? 60.876  -25.997 26.940 1.00 30.26  ? 56   GLY F C   1 
ATOM   5984  O  O   . GLY F  1 56  ? 60.963  -26.565 25.851 1.00 24.76  ? 56   GLY F O   1 
ATOM   5985  N  N   . CYS F  1 57  ? 61.265  -24.740 27.124 1.00 26.31  ? 57   CYS F N   1 
ATOM   5986  C  CA  . CYS F  1 57  ? 61.760  -23.957 25.992 1.00 24.35  ? 57   CYS F CA  1 
ATOM   5987  C  C   . CYS F  1 57  ? 63.081  -24.478 25.463 1.00 22.83  ? 57   CYS F C   1 
ATOM   5988  O  O   . CYS F  1 57  ? 63.465  -24.207 24.324 1.00 20.92  ? 57   CYS F O   1 
ATOM   5989  C  CB  A CYS F  1 57  ? 61.982  -22.511 26.468 0.47 22.43  ? 57   CYS F CB  1 
ATOM   5990  C  CB  B CYS F  1 57  ? 61.806  -22.473 26.360 0.53 28.20  ? 57   CYS F CB  1 
ATOM   5991  S  SG  A CYS F  1 57  ? 60.406  -21.739 26.943 0.47 29.28  ? 57   CYS F SG  1 
ATOM   5992  S  SG  B CYS F  1 57  ? 60.342  -21.832 27.210 0.53 34.76  ? 57   CYS F SG  1 
ATOM   5993  N  N   . THR F  1 58  ? 63.805  -25.266 26.252 1.00 19.37  ? 58   THR F N   1 
ATOM   5994  C  CA  . THR F  1 58  ? 65.070  -25.792 25.745 1.00 22.07  ? 58   THR F CA  1 
ATOM   5995  C  C   . THR F  1 58  ? 64.940  -26.624 24.490 1.00 27.20  ? 58   THR F C   1 
ATOM   5996  O  O   . THR F  1 58  ? 65.826  -26.655 23.641 1.00 24.54  ? 58   THR F O   1 
ATOM   5997  C  CB  . THR F  1 58  ? 65.732  -26.678 26.831 1.00 35.98  ? 58   THR F CB  1 
ATOM   5998  O  OG1 . THR F  1 58  ? 65.811  -25.938 28.049 1.00 39.31  ? 58   THR F OG1 1 
ATOM   5999  C  CG2 . THR F  1 58  ? 67.144  -27.041 26.384 1.00 32.65  ? 58   THR F CG2 1 
ATOM   6000  N  N   . SER F  1 59  ? 63.838  -27.384 24.351 1.00 24.36  ? 59   SER F N   1 
ATOM   6001  C  CA  . SER F  1 59  ? 63.782  -28.289 23.205 1.00 23.39  ? 59   SER F CA  1 
ATOM   6002  C  C   . SER F  1 59  ? 63.375  -27.566 21.934 1.00 23.04  ? 59   SER F C   1 
ATOM   6003  O  O   . SER F  1 59  ? 63.254  -28.180 20.863 1.00 25.20  ? 59   SER F O   1 
ATOM   6004  C  CB  . SER F  1 59  ? 62.840  -29.447 23.550 1.00 26.56  ? 59   SER F CB  1 
ATOM   6005  O  OG  . SER F  1 59  ? 61.766  -29.020 24.368 1.00 31.00  ? 59   SER F OG  1 
ATOM   6006  N  N   . ALA F  1 60  ? 63.180  -26.244 21.974 1.00 20.81  ? 60   ALA F N   1 
ATOM   6007  C  CA  . ALA F  1 60  ? 62.859  -25.536 20.738 1.00 18.05  ? 60   ALA F CA  1 
ATOM   6008  C  C   . ALA F  1 60  ? 64.088  -25.419 19.827 1.00 23.08  ? 60   ALA F C   1 
ATOM   6009  O  O   . ALA F  1 60  ? 63.972  -24.973 18.688 1.00 24.12  ? 60   ALA F O   1 
ATOM   6010  C  CB  . ALA F  1 60  ? 62.304  -24.145 20.964 1.00 18.50  ? 60   ALA F CB  1 
ATOM   6011  N  N   . GLY F  1 61  ? 65.240  -25.825 20.330 1.00 21.99  ? 61   GLY F N   1 
ATOM   6012  C  CA  . GLY F  1 61  ? 66.447  -25.766 19.497 1.00 23.79  ? 61   GLY F CA  1 
ATOM   6013  C  C   . GLY F  1 61  ? 66.910  -24.337 19.280 1.00 23.48  ? 61   GLY F C   1 
ATOM   6014  O  O   . GLY F  1 61  ? 66.554  -23.419 19.997 1.00 20.22  ? 61   GLY F O   1 
ATOM   6015  N  N   . PRO F  1 62  ? 67.765  -24.133 18.272 1.00 22.41  ? 62   PRO F N   1 
ATOM   6016  C  CA  . PRO F  1 62  ? 68.340  -22.809 18.012 1.00 21.84  ? 62   PRO F CA  1 
ATOM   6017  C  C   . PRO F  1 62  ? 67.424  -21.899 17.226 1.00 20.62  ? 62   PRO F C   1 
ATOM   6018  O  O   . PRO F  1 62  ? 66.291  -22.233 16.866 1.00 23.08  ? 62   PRO F O   1 
ATOM   6019  C  CB  . PRO F  1 62  ? 69.591  -23.168 17.176 1.00 26.56  ? 62   PRO F CB  1 
ATOM   6020  C  CG  . PRO F  1 62  ? 69.286  -24.467 16.524 1.00 29.99  ? 62   PRO F CG  1 
ATOM   6021  C  CD  . PRO F  1 62  ? 68.252  -25.174 17.363 1.00 22.33  ? 62   PRO F CD  1 
ATOM   6022  N  N   . HIS F  1 63  ? 67.904  -20.693 16.926 1.00 20.20  ? 63   HIS F N   1 
ATOM   6023  C  CA  . HIS F  1 63  ? 67.117  -19.748 16.143 1.00 19.05  ? 63   HIS F CA  1 
ATOM   6024  C  C   . HIS F  1 63  ? 66.754  -20.347 14.790 1.00 21.04  ? 63   HIS F C   1 
ATOM   6025  O  O   . HIS F  1 63  ? 67.609  -21.033 14.211 1.00 22.61  ? 63   HIS F O   1 
ATOM   6026  C  CB  . HIS F  1 63  ? 67.892  -18.442 15.902 1.00 20.60  ? 63   HIS F CB  1 
ATOM   6027  C  CG  . HIS F  1 63  ? 68.160  -17.659 17.130 1.00 19.44  ? 63   HIS F CG  1 
ATOM   6028  N  ND1 . HIS F  1 63  ? 68.668  -16.379 17.181 1.00 20.09  ? 63   HIS F ND1 1 
ATOM   6029  C  CD2 . HIS F  1 63  ? 67.958  -18.045 18.420 1.00 24.91  ? 63   HIS F CD2 1 
ATOM   6030  C  CE1 . HIS F  1 63  ? 68.770  -15.995 18.440 1.00 21.19  ? 63   HIS F CE1 1 
ATOM   6031  N  NE2 . HIS F  1 63  ? 68.352  -17.001 19.214 1.00 24.63  ? 63   HIS F NE2 1 
ATOM   6032  N  N   . PHE F  1 64  ? 65.548  -20.098 14.288 1.00 21.94  ? 64   PHE F N   1 
ATOM   6033  C  CA  . PHE F  1 64  ? 65.172  -20.633 12.962 1.00 21.63  ? 64   PHE F CA  1 
ATOM   6034  C  C   . PHE F  1 64  ? 66.087  -20.001 11.910 1.00 25.92  ? 64   PHE F C   1 
ATOM   6035  O  O   . PHE F  1 64  ? 66.118  -18.785 11.755 1.00 22.10  ? 64   PHE F O   1 
ATOM   6036  C  CB  . PHE F  1 64  ? 63.686  -20.368 12.759 1.00 23.47  ? 64   PHE F CB  1 
ATOM   6037  C  CG  . PHE F  1 64  ? 63.113  -20.720 11.389 1.00 23.66  ? 64   PHE F CG  1 
ATOM   6038  C  CD1 . PHE F  1 64  ? 62.245  -19.843 10.767 1.00 25.70  ? 64   PHE F CD1 1 
ATOM   6039  C  CD2 . PHE F  1 64  ? 63.466  -21.916 10.793 1.00 25.40  ? 64   PHE F CD2 1 
ATOM   6040  C  CE1 . PHE F  1 64  ? 61.720  -20.129 9.515  1.00 29.72  ? 64   PHE F CE1 1 
ATOM   6041  C  CE2 . PHE F  1 64  ? 62.960  -22.219 9.525  1.00 25.26  ? 64   PHE F CE2 1 
ATOM   6042  C  CZ  . PHE F  1 64  ? 62.104  -21.317 8.923  1.00 27.07  ? 64   PHE F CZ  1 
ATOM   6043  N  N   . ASN F  1 65  ? 66.854  -20.791 11.172 1.00 25.16  ? 65   ASN F N   1 
ATOM   6044  C  CA  . ASN F  1 65  ? 67.917  -20.290 10.301 1.00 25.81  ? 65   ASN F CA  1 
ATOM   6045  C  C   . ASN F  1 65  ? 68.096  -21.136 9.053  1.00 24.28  ? 65   ASN F C   1 
ATOM   6046  O  O   . ASN F  1 65  ? 69.140  -21.760 8.864  1.00 32.91  ? 65   ASN F O   1 
ATOM   6047  C  CB  . ASN F  1 65  ? 69.237  -20.328 11.082 1.00 25.96  ? 65   ASN F CB  1 
ATOM   6048  C  CG  . ASN F  1 65  ? 70.440  -19.753 10.357 1.00 24.70  ? 65   ASN F CG  1 
ATOM   6049  O  OD1 . ASN F  1 65  ? 70.326  -18.885 9.508  1.00 28.58  ? 65   ASN F OD1 1 
ATOM   6050  N  ND2 . ASN F  1 65  ? 71.613  -20.179 10.817 1.00 29.97  ? 65   ASN F ND2 1 
ATOM   6051  N  N   . PRO F  1 66  ? 67.100  -21.175 8.206  1.00 24.20  ? 66   PRO F N   1 
ATOM   6052  C  CA  . PRO F  1 66  ? 67.225  -22.102 7.072  1.00 37.06  ? 66   PRO F CA  1 
ATOM   6053  C  C   . PRO F  1 66  ? 68.322  -21.694 6.099  1.00 46.53  ? 66   PRO F C   1 
ATOM   6054  O  O   . PRO F  1 66  ? 68.699  -22.519 5.252  1.00 36.82  ? 66   PRO F O   1 
ATOM   6055  C  CB  . PRO F  1 66  ? 65.843  -22.010 6.422  1.00 32.18  ? 66   PRO F CB  1 
ATOM   6056  C  CG  . PRO F  1 66  ? 65.379  -20.634 6.775  1.00 28.83  ? 66   PRO F CG  1 
ATOM   6057  C  CD  . PRO F  1 66  ? 65.846  -20.438 8.198  1.00 26.37  ? 66   PRO F CD  1 
ATOM   6058  N  N   . LEU F  1 67  ? 68.835  -20.469 6.195  1.00 42.45  ? 67   LEU F N   1 
ATOM   6059  C  CA  . LEU F  1 67  ? 69.858  -20.034 5.243  1.00 34.15  ? 67   LEU F CA  1 
ATOM   6060  C  C   . LEU F  1 67  ? 71.258  -20.091 5.837  1.00 41.29  ? 67   LEU F C   1 
ATOM   6061  O  O   . LEU F  1 67  ? 72.204  -19.574 5.234  1.00 49.70  ? 67   LEU F O   1 
ATOM   6062  C  CB  . LEU F  1 67  ? 69.583  -18.614 4.746  1.00 33.30  ? 67   LEU F CB  1 
ATOM   6063  C  CG  . LEU F  1 67  ? 68.233  -18.379 4.073  1.00 37.35  ? 67   LEU F CG  1 
ATOM   6064  C  CD1 . LEU F  1 67  ? 68.198  -17.017 3.395  1.00 39.91  ? 67   LEU F CD1 1 
ATOM   6065  C  CD2 . LEU F  1 67  ? 67.930  -19.475 3.068  1.00 49.72  ? 67   LEU F CD2 1 
ATOM   6066  N  N   . SER F  1 68  ? 71.389  -20.719 6.992  1.00 33.89  ? 68   SER F N   1 
ATOM   6067  C  CA  . SER F  1 68  ? 72.685  -20.922 7.635  1.00 35.39  ? 68   SER F CA  1 
ATOM   6068  C  C   . SER F  1 68  ? 73.504  -19.642 7.747  1.00 39.56  ? 68   SER F C   1 
ATOM   6069  O  O   . SER F  1 68  ? 74.713  -19.654 7.498  1.00 41.64  ? 68   SER F O   1 
ATOM   6070  C  CB  . SER F  1 68  ? 73.507  -21.984 6.892  1.00 33.84  ? 68   SER F CB  1 
ATOM   6071  O  OG  . SER F  1 68  ? 72.683  -23.065 6.497  1.00 47.02  ? 68   SER F OG  1 
ATOM   6072  N  N   . ARG F  1 69  ? 72.853  -18.551 8.141  1.00 33.32  ? 69   ARG F N   1 
ATOM   6073  C  CA  . ARG F  1 69  ? 73.599  -17.307 8.334  1.00 33.01  ? 69   ARG F CA  1 
ATOM   6074  C  C   . ARG F  1 69  ? 73.968  -17.113 9.794  1.00 30.33  ? 69   ARG F C   1 
ATOM   6075  O  O   . ARG F  1 69  ? 73.626  -17.920 10.662 1.00 31.04  ? 69   ARG F O   1 
ATOM   6076  C  CB  . ARG F  1 69  ? 72.789  -16.116 7.810  1.00 35.11  ? 69   ARG F CB  1 
ATOM   6077  C  CG  . ARG F  1 69  ? 72.616  -16.197 6.292  1.00 40.95  ? 69   ARG F CG  1 
ATOM   6078  C  CD  . ARG F  1 69  ? 71.336  -15.524 5.848  1.00 58.68  ? 69   ARG F CD  1 
ATOM   6079  N  NE  . ARG F  1 69  ? 71.381  -15.270 4.405  1.00 71.45  ? 69   ARG F NE  1 
ATOM   6080  C  CZ  . ARG F  1 69  ? 70.538  -14.438 3.802  1.00 80.64  ? 69   ARG F CZ  1 
ATOM   6081  N  NH1 . ARG F  1 69  ? 70.634  -14.255 2.493  1.00 103.28 ? 69   ARG F NH1 1 
ATOM   6082  N  NH2 . ARG F  1 69  ? 69.607  -13.802 4.504  1.00 91.28  ? 69   ARG F NH2 1 
ATOM   6083  N  N   . LYS F  1 70  ? 74.700  -16.039 10.060 1.00 28.73  ? 70   LYS F N   1 
ATOM   6084  C  CA  . LYS F  1 70  ? 75.018  -15.680 11.440 1.00 27.73  ? 70   LYS F CA  1 
ATOM   6085  C  C   . LYS F  1 70  ? 73.882  -14.844 12.038 1.00 23.70  ? 70   LYS F C   1 
ATOM   6086  O  O   . LYS F  1 70  ? 73.086  -14.248 11.319 1.00 23.69  ? 70   LYS F O   1 
ATOM   6087  C  CB  . LYS F  1 70  ? 76.366  -14.965 11.456 1.00 35.07  ? 70   LYS F CB  1 
ATOM   6088  C  CG  . LYS F  1 70  ? 77.539  -15.943 11.242 1.00 33.23  ? 70   LYS F CG  1 
ATOM   6089  C  CD  . LYS F  1 70  ? 78.818  -15.165 10.980 1.00 50.08  ? 70   LYS F CD  1 
ATOM   6090  C  CE  . LYS F  1 70  ? 79.950  -16.052 10.483 1.00 59.66  ? 70   LYS F CE  1 
ATOM   6091  N  NZ  . LYS F  1 70  ? 80.362  -17.092 11.471 1.00 74.50  ? 70   LYS F NZ  1 
ATOM   6092  N  N   . HIS F  1 71  ? 73.819  -14.793 13.365 1.00 25.26  ? 71   HIS F N   1 
ATOM   6093  C  CA  . HIS F  1 71  ? 72.780  -14.042 14.050 1.00 23.88  ? 71   HIS F CA  1 
ATOM   6094  C  C   . HIS F  1 71  ? 72.883  -12.552 13.778 1.00 24.15  ? 71   HIS F C   1 
ATOM   6095  O  O   . HIS F  1 71  ? 74.002  -12.008 13.733 1.00 24.60  ? 71   HIS F O   1 
ATOM   6096  C  CB  . HIS F  1 71  ? 72.892  -14.342 15.559 1.00 22.35  ? 71   HIS F CB  1 
ATOM   6097  C  CG  . HIS F  1 71  ? 71.887  -13.576 16.364 1.00 18.47  ? 71   HIS F CG  1 
ATOM   6098  N  ND1 . HIS F  1 71  ? 70.563  -13.933 16.470 1.00 21.37  ? 71   HIS F ND1 1 
ATOM   6099  C  CD2 . HIS F  1 71  ? 72.016  -12.441 17.081 1.00 18.20  ? 71   HIS F CD2 1 
ATOM   6100  C  CE1 . HIS F  1 71  ? 69.921  -13.065 17.225 1.00 21.90  ? 71   HIS F CE1 1 
ATOM   6101  N  NE2 . HIS F  1 71  ? 70.787  -12.132 17.627 1.00 20.75  ? 71   HIS F NE2 1 
ATOM   6102  N  N   . GLY F  1 72  ? 71.757  -11.880 13.611 1.00 21.56  ? 72   GLY F N   1 
ATOM   6103  C  CA  . GLY F  1 72  ? 71.673  -10.446 13.401 1.00 23.84  ? 72   GLY F CA  1 
ATOM   6104  C  C   . GLY F  1 72  ? 70.463  -9.797  14.041 1.00 26.57  ? 72   GLY F C   1 
ATOM   6105  O  O   . GLY F  1 72  ? 69.695  -10.452 14.748 1.00 26.21  ? 72   GLY F O   1 
ATOM   6106  N  N   . GLY F  1 73  ? 70.289  -8.502  13.796 1.00 22.16  ? 73   GLY F N   1 
ATOM   6107  C  CA  . GLY F  1 73  ? 69.099  -7.758  14.181 1.00 20.51  ? 73   GLY F CA  1 
ATOM   6108  C  C   . GLY F  1 73  ? 68.134  -7.890  12.986 1.00 21.57  ? 73   GLY F C   1 
ATOM   6109  O  O   . GLY F  1 73  ? 68.593  -8.282  11.909 1.00 23.75  ? 73   GLY F O   1 
ATOM   6110  N  N   . PRO F  1 74  ? 66.861  -7.607  13.171 1.00 21.14  ? 74   PRO F N   1 
ATOM   6111  C  CA  . PRO F  1 74  ? 65.909  -7.777  12.055 1.00 22.58  ? 74   PRO F CA  1 
ATOM   6112  C  C   . PRO F  1 74  ? 66.233  -6.890  10.860 1.00 26.03  ? 74   PRO F C   1 
ATOM   6113  O  O   . PRO F  1 74  ? 65.832  -7.237  9.746  1.00 25.50  ? 74   PRO F O   1 
ATOM   6114  C  CB  . PRO F  1 74  ? 64.562  -7.396  12.668 1.00 28.88  ? 74   PRO F CB  1 
ATOM   6115  C  CG  . PRO F  1 74  ? 64.866  -6.649  13.920 1.00 26.16  ? 74   PRO F CG  1 
ATOM   6116  C  CD  . PRO F  1 74  ? 66.196  -7.148  14.410 1.00 22.90  ? 74   PRO F CD  1 
ATOM   6117  N  N   . LYS F  1 75  ? 66.959  -5.791  11.033 1.00 25.79  ? 75   LYS F N   1 
ATOM   6118  C  CA  . LYS F  1 75  ? 67.242  -4.928  9.885  1.00 29.22  ? 75   LYS F CA  1 
ATOM   6119  C  C   . LYS F  1 75  ? 68.493  -5.330  9.123  1.00 39.69  ? 75   LYS F C   1 
ATOM   6120  O  O   . LYS F  1 75  ? 68.825  -4.724  8.095  1.00 36.34  ? 75   LYS F O   1 
ATOM   6121  C  CB  . LYS F  1 75  ? 67.401  -3.469  10.364 1.00 31.63  ? 75   LYS F CB  1 
ATOM   6122  C  CG  . LYS F  1 75  ? 66.144  -2.991  11.071 1.00 37.35  ? 75   LYS F CG  1 
ATOM   6123  C  CD  . LYS F  1 75  ? 66.451  -1.834  12.012 1.00 45.24  ? 75   LYS F CD  1 
ATOM   6124  C  CE  . LYS F  1 75  ? 66.104  -0.496  11.361 1.00 49.26  ? 75   LYS F CE  1 
ATOM   6125  N  NZ  . LYS F  1 75  ? 67.359  0.302   11.205 1.00 69.60  ? 75   LYS F NZ  1 
ATOM   6126  N  N   . ASP F  1 76  ? 69.214  -6.334  9.601  1.00 29.22  ? 76   ASP F N   1 
ATOM   6127  C  CA  . ASP F  1 76  ? 70.389  -6.825  8.906  1.00 32.68  ? 76   ASP F CA  1 
ATOM   6128  C  C   . ASP F  1 76  ? 70.109  -7.814  7.782  1.00 41.16  ? 76   ASP F C   1 
ATOM   6129  O  O   . ASP F  1 76  ? 69.264  -8.705  7.909  1.00 32.40  ? 76   ASP F O   1 
ATOM   6130  C  CB  . ASP F  1 76  ? 71.292  -7.578  9.898  1.00 35.06  ? 76   ASP F CB  1 
ATOM   6131  C  CG  . ASP F  1 76  ? 71.859  -6.680  10.968 1.00 36.20  ? 76   ASP F CG  1 
ATOM   6132  O  OD1 . ASP F  1 76  ? 71.864  -7.084  12.144 1.00 43.27  ? 76   ASP F OD1 1 
ATOM   6133  O  OD2 . ASP F  1 76  ? 72.292  -5.571  10.604 1.00 47.99  ? 76   ASP F OD2 1 
ATOM   6134  N  N   . GLU F  1 77  ? 70.869  -7.714  6.685  1.00 34.34  ? 77   GLU F N   1 
ATOM   6135  C  CA  . GLU F  1 77  ? 70.765  -8.775  5.675  1.00 36.93  ? 77   GLU F CA  1 
ATOM   6136  C  C   . GLU F  1 77  ? 71.332  -10.076 6.227  1.00 37.44  ? 77   GLU F C   1 
ATOM   6137  O  O   . GLU F  1 77  ? 70.855  -11.197 6.002  1.00 37.99  ? 77   GLU F O   1 
ATOM   6138  C  CB  . GLU F  1 77  ? 71.482  -8.350  4.394  1.00 54.70  ? 77   GLU F CB  1 
ATOM   6139  C  CG  . GLU F  1 77  ? 71.031  -9.032  3.119  1.00 73.40  ? 77   GLU F CG  1 
ATOM   6140  C  CD  . GLU F  1 77  ? 69.531  -9.219  3.010  1.00 90.98  ? 77   GLU F CD  1 
ATOM   6141  O  OE1 . GLU F  1 77  ? 68.860  -8.393  2.347  1.00 113.09 ? 77   GLU F OE1 1 
ATOM   6142  O  OE2 . GLU F  1 77  ? 69.007  -10.203 3.580  1.00 107.38 ? 77   GLU F OE2 1 
ATOM   6143  N  N   . GLU F  1 78  ? 72.401  -9.966  7.020  1.00 26.00  ? 78   GLU F N   1 
ATOM   6144  C  CA  . GLU F  1 78  ? 72.926  -11.149 7.689  1.00 30.79  ? 78   GLU F CA  1 
ATOM   6145  C  C   . GLU F  1 78  ? 72.215  -11.313 9.037  1.00 28.44  ? 78   GLU F C   1 
ATOM   6146  O  O   . GLU F  1 78  ? 72.446  -10.639 10.042 1.00 24.84  ? 78   GLU F O   1 
ATOM   6147  C  CB  . GLU F  1 78  ? 74.445  -11.114 7.900  1.00 33.14  ? 78   GLU F CB  1 
ATOM   6148  C  CG  . GLU F  1 78  ? 75.024  -12.409 8.449  1.00 36.66  ? 78   GLU F CG  1 
ATOM   6149  C  CD  . GLU F  1 78  ? 75.365  -13.473 7.434  1.00 42.12  ? 78   GLU F CD  1 
ATOM   6150  O  OE1 . GLU F  1 78  ? 75.816  -14.565 7.855  1.00 35.37  ? 78   GLU F OE1 1 
ATOM   6151  O  OE2 . GLU F  1 78  ? 75.213  -13.252 6.213  1.00 47.28  ? 78   GLU F OE2 1 
ATOM   6152  N  N   . ARG F  1 79  ? 71.291  -12.262 9.003  1.00 28.27  ? 79   ARG F N   1 
ATOM   6153  C  CA  . ARG F  1 79  ? 70.434  -12.511 10.165 1.00 23.38  ? 79   ARG F CA  1 
ATOM   6154  C  C   . ARG F  1 79  ? 69.833  -13.899 9.990  1.00 32.38  ? 79   ARG F C   1 
ATOM   6155  O  O   . ARG F  1 79  ? 69.733  -14.353 8.844  1.00 27.50  ? 79   ARG F O   1 
ATOM   6156  C  CB  . ARG F  1 79  ? 69.300  -11.498 10.261 1.00 23.68  ? 79   ARG F CB  1 
ATOM   6157  C  CG  . ARG F  1 79  ? 68.337  -11.521 9.072  1.00 26.26  ? 79   ARG F CG  1 
ATOM   6158  C  CD  . ARG F  1 79  ? 67.118  -10.666 9.371  1.00 27.01  ? 79   ARG F CD  1 
ATOM   6159  N  NE  . ARG F  1 79  ? 66.027  -11.493 9.947  1.00 24.54  ? 79   ARG F NE  1 
ATOM   6160  C  CZ  . ARG F  1 79  ? 64.810  -11.009 10.092 1.00 23.05  ? 79   ARG F CZ  1 
ATOM   6161  N  NH1 . ARG F  1 79  ? 63.823  -11.776 10.607 1.00 23.77  ? 79   ARG F NH1 1 
ATOM   6162  N  NH2 . ARG F  1 79  ? 64.519  -9.766  9.746  1.00 23.02  ? 79   ARG F NH2 1 
ATOM   6163  N  N   . HIS F  1 80  ? 69.442  -14.529 11.085 1.00 26.11  ? 80   HIS F N   1 
ATOM   6164  C  CA  . HIS F  1 80  ? 68.593  -15.710 10.982 1.00 25.40  ? 80   HIS F CA  1 
ATOM   6165  C  C   . HIS F  1 80  ? 67.192  -15.324 10.576 1.00 21.08  ? 80   HIS F C   1 
ATOM   6166  O  O   . HIS F  1 80  ? 66.748  -14.226 10.930 1.00 21.46  ? 80   HIS F O   1 
ATOM   6167  C  CB  . HIS F  1 80  ? 68.557  -16.390 12.346 1.00 23.81  ? 80   HIS F CB  1 
ATOM   6168  C  CG  . HIS F  1 80  ? 69.880  -16.759 12.919 1.00 21.13  ? 80   HIS F CG  1 
ATOM   6169  N  ND1 . HIS F  1 80  ? 70.150  -16.647 14.259 1.00 23.49  ? 80   HIS F ND1 1 
ATOM   6170  C  CD2 . HIS F  1 80  ? 71.018  -17.268 12.376 1.00 22.04  ? 80   HIS F CD2 1 
ATOM   6171  C  CE1 . HIS F  1 80  ? 71.383  -17.073 14.493 1.00 25.19  ? 80   HIS F CE1 1 
ATOM   6172  N  NE2 . HIS F  1 80  ? 71.938  -17.465 13.351 1.00 24.61  ? 80   HIS F NE2 1 
ATOM   6173  N  N   . VAL F  1 81  ? 66.443  -16.155 9.867  1.00 22.81  ? 81   VAL F N   1 
ATOM   6174  C  CA  . VAL F  1 81  ? 65.039  -15.804 9.623  1.00 24.08  ? 81   VAL F CA  1 
ATOM   6175  C  C   . VAL F  1 81  ? 64.293  -15.539 10.928 1.00 18.94  ? 81   VAL F C   1 
ATOM   6176  O  O   . VAL F  1 81  ? 63.492  -14.595 11.009 1.00 20.13  ? 81   VAL F O   1 
ATOM   6177  C  CB  . VAL F  1 81  ? 64.303  -16.902 8.825  1.00 28.34  ? 81   VAL F CB  1 
ATOM   6178  C  CG1 . VAL F  1 81  ? 62.826  -16.563 8.712  1.00 25.97  ? 81   VAL F CG1 1 
ATOM   6179  C  CG2 . VAL F  1 81  ? 64.908  -17.071 7.429  1.00 29.34  ? 81   VAL F CG2 1 
ATOM   6180  N  N   . GLY F  1 82  ? 64.555  -16.297 11.993 1.00 24.06  ? 82   GLY F N   1 
ATOM   6181  C  CA  . GLY F  1 82  ? 63.827  -15.997 13.230 1.00 21.36  ? 82   GLY F CA  1 
ATOM   6182  C  C   . GLY F  1 82  ? 64.239  -14.791 14.034 1.00 22.15  ? 82   GLY F C   1 
ATOM   6183  O  O   . GLY F  1 82  ? 63.759  -14.565 15.159 1.00 22.11  ? 82   GLY F O   1 
ATOM   6184  N  N   . ASP F  1 83  ? 65.151  -13.945 13.556 1.00 24.95  ? 83   ASP F N   1 
ATOM   6185  C  CA  . ASP F  1 83  ? 65.687  -12.842 14.370 1.00 20.90  ? 83   ASP F CA  1 
ATOM   6186  C  C   . ASP F  1 83  ? 64.782  -11.631 14.373 1.00 21.34  ? 83   ASP F C   1 
ATOM   6187  O  O   . ASP F  1 83  ? 64.821  -10.788 13.474 1.00 24.70  ? 83   ASP F O   1 
ATOM   6188  C  CB  . ASP F  1 83  ? 67.077  -12.446 13.836 1.00 21.26  ? 83   ASP F CB  1 
ATOM   6189  C  CG  . ASP F  1 83  ? 68.140  -13.459 14.163 1.00 25.92  ? 83   ASP F CG  1 
ATOM   6190  O  OD1 . ASP F  1 83  ? 67.876  -14.363 15.007 1.00 21.57  ? 83   ASP F OD1 1 
ATOM   6191  O  OD2 . ASP F  1 83  ? 69.265  -13.376 13.587 1.00 22.85  ? 83   ASP F OD2 1 
ATOM   6192  N  N   . LEU F  1 84  ? 63.944  -11.478 15.398 1.00 19.64  ? 84   LEU F N   1 
ATOM   6193  C  CA  . LEU F  1 84  ? 63.047  -10.345 15.518 1.00 17.90  ? 84   LEU F CA  1 
ATOM   6194  C  C   . LEU F  1 84  ? 63.564  -9.301  16.489 1.00 23.58  ? 84   LEU F C   1 
ATOM   6195  O  O   . LEU F  1 84  ? 62.864  -8.345  16.803 1.00 22.73  ? 84   LEU F O   1 
ATOM   6196  C  CB  . LEU F  1 84  ? 61.654  -10.837 15.950 1.00 21.07  ? 84   LEU F CB  1 
ATOM   6197  C  CG  . LEU F  1 84  ? 61.017  -11.840 14.982 1.00 23.44  ? 84   LEU F CG  1 
ATOM   6198  C  CD1 . LEU F  1 84  ? 59.659  -12.262 15.512 1.00 21.06  ? 84   LEU F CD1 1 
ATOM   6199  C  CD2 . LEU F  1 84  ? 60.875  -11.238 13.589 1.00 23.51  ? 84   LEU F CD2 1 
ATOM   6200  N  N   . GLY F  1 85  ? 64.805  -9.427  16.973 1.00 21.89  ? 85   GLY F N   1 
ATOM   6201  C  CA  . GLY F  1 85  ? 65.370  -8.341  17.763 1.00 23.57  ? 85   GLY F CA  1 
ATOM   6202  C  C   . GLY F  1 85  ? 64.994  -8.367  19.237 1.00 20.92  ? 85   GLY F C   1 
ATOM   6203  O  O   . GLY F  1 85  ? 65.051  -9.440  19.839 1.00 24.66  ? 85   GLY F O   1 
ATOM   6204  N  N   . ASN F  1 86  ? 64.654  -7.214  19.779 1.00 20.69  ? 86   ASN F N   1 
ATOM   6205  C  CA  . ASN F  1 86  ? 64.246  -7.054  21.161 1.00 19.40  ? 86   ASN F CA  1 
ATOM   6206  C  C   . ASN F  1 86  ? 62.800  -6.571  21.310 1.00 21.64  ? 86   ASN F C   1 
ATOM   6207  O  O   . ASN F  1 86  ? 62.269  -5.896  20.432 1.00 22.05  ? 86   ASN F O   1 
ATOM   6208  C  CB  . ASN F  1 86  ? 65.155  -6.027  21.855 1.00 20.52  ? 86   ASN F CB  1 
ATOM   6209  C  CG  . ASN F  1 86  ? 66.538  -6.614  22.099 1.00 22.24  ? 86   ASN F CG  1 
ATOM   6210  O  OD1 . ASN F  1 86  ? 66.708  -7.550  22.885 1.00 22.60  ? 86   ASN F OD1 1 
ATOM   6211  N  ND2 . ASN F  1 86  ? 67.518  -6.063  21.404 1.00 24.64  ? 86   ASN F ND2 1 
ATOM   6212  N  N   . VAL F  1 87  ? 62.213  -6.901  22.452 1.00 23.11  ? 87   VAL F N   1 
ATOM   6213  C  CA  . VAL F  1 87  ? 60.980  -6.228  22.889 1.00 20.49  ? 87   VAL F CA  1 
ATOM   6214  C  C   . VAL F  1 87  ? 61.335  -5.446  24.155 1.00 27.13  ? 87   VAL F C   1 
ATOM   6215  O  O   . VAL F  1 87  ? 62.310  -5.808  24.822 1.00 24.71  ? 87   VAL F O   1 
ATOM   6216  C  CB  . VAL F  1 87  ? 59.802  -7.186  23.107 1.00 20.88  ? 87   VAL F CB  1 
ATOM   6217  C  CG1 . VAL F  1 87  ? 59.454  -7.843  21.774 1.00 25.00  ? 87   VAL F CG1 1 
ATOM   6218  C  CG2 . VAL F  1 87  ? 60.125  -8.236  24.153 1.00 23.04  ? 87   VAL F CG2 1 
ATOM   6219  N  N   . THR F  1 88  ? 60.557  -4.403  24.443 1.00 20.72  ? 88   THR F N   1 
ATOM   6220  C  CA  . THR F  1 88  ? 60.819  -3.590  25.617 1.00 23.37  ? 88   THR F CA  1 
ATOM   6221  C  C   . THR F  1 88  ? 59.673  -3.705  26.632 1.00 21.20  ? 88   THR F C   1 
ATOM   6222  O  O   . THR F  1 88  ? 58.559  -3.388  26.256 1.00 26.99  ? 88   THR F O   1 
ATOM   6223  C  CB  . THR F  1 88  ? 60.992  -2.116  25.199 1.00 24.44  ? 88   THR F CB  1 
ATOM   6224  O  OG1 . THR F  1 88  ? 62.002  -2.044  24.184 1.00 21.77  ? 88   THR F OG1 1 
ATOM   6225  C  CG2 . THR F  1 88  ? 61.460  -1.277  26.378 1.00 33.15  ? 88   THR F CG2 1 
ATOM   6226  N  N   . ALA F  1 89  ? 60.009  -4.127  27.840 1.00 22.45  ? 89   ALA F N   1 
ATOM   6227  C  CA  . ALA F  1 89  ? 59.072  -4.173  28.953 1.00 24.46  ? 89   ALA F CA  1 
ATOM   6228  C  C   . ALA F  1 89  ? 59.092  -2.829  29.692 1.00 36.84  ? 89   ALA F C   1 
ATOM   6229  O  O   . ALA F  1 89  ? 60.208  -2.333  29.912 1.00 26.67  ? 89   ALA F O   1 
ATOM   6230  C  CB  . ALA F  1 89  ? 59.469  -5.265  29.905 1.00 19.78  ? 89   ALA F CB  1 
ATOM   6231  N  N   . ASP F  1 90  ? 57.933  -2.294  30.028 1.00 26.40  ? 90   ASP F N   1 
ATOM   6232  C  CA  . ASP F  1 90  ? 57.830  -0.988  30.692 1.00 23.79  ? 90   ASP F CA  1 
ATOM   6233  C  C   . ASP F  1 90  ? 58.039  -1.197  32.177 1.00 26.19  ? 90   ASP F C   1 
ATOM   6234  O  O   . ASP F  1 90  ? 58.366  -2.295  32.606 1.00 27.12  ? 90   ASP F O   1 
ATOM   6235  C  CB  . ASP F  1 90  ? 56.503  -0.327  30.391 1.00 31.32  ? 90   ASP F CB  1 
ATOM   6236  C  CG  . ASP F  1 90  ? 55.262  -1.071  30.853 1.00 38.77  ? 90   ASP F CG  1 
ATOM   6237  O  OD1 . ASP F  1 90  ? 54.201  -0.962  30.183 1.00 35.95  ? 90   ASP F OD1 1 
ATOM   6238  O  OD2 . ASP F  1 90  ? 55.305  -1.770  31.891 1.00 37.96  ? 90   ASP F OD2 1 
ATOM   6239  N  N   . LYS F  1 91  ? 57.859  -0.172  33.020 1.00 33.12  ? 91   LYS F N   1 
ATOM   6240  C  CA  . LYS F  1 91  ? 58.175  -0.379  34.439 1.00 31.58  ? 91   LYS F CA  1 
ATOM   6241  C  C   . LYS F  1 91  ? 57.130  -1.215  35.161 1.00 33.27  ? 91   LYS F C   1 
ATOM   6242  O  O   . LYS F  1 91  ? 57.330  -1.723  36.269 1.00 33.99  ? 91   LYS F O   1 
ATOM   6243  C  CB  . LYS F  1 91  ? 58.375  0.996   35.097 1.00 41.04  ? 91   LYS F CB  1 
ATOM   6244  C  CG  . LYS F  1 91  ? 57.144  1.522   35.811 1.00 59.54  ? 91   LYS F CG  1 
ATOM   6245  C  CD  . LYS F  1 91  ? 57.136  3.040   35.889 1.00 64.92  ? 91   LYS F CD  1 
ATOM   6246  C  CE  . LYS F  1 91  ? 55.715  3.571   36.000 1.00 69.24  ? 91   LYS F CE  1 
ATOM   6247  N  NZ  . LYS F  1 91  ? 55.277  3.671   37.424 1.00 83.13  ? 91   LYS F NZ  1 
ATOM   6248  N  N   . ASP F  1 92  ? 55.983  -1.398  34.516 1.00 27.16  ? 92   ASP F N   1 
ATOM   6249  C  CA  . ASP F  1 92  ? 54.921  -2.243  35.047 1.00 28.06  ? 92   ASP F CA  1 
ATOM   6250  C  C   . ASP F  1 92  ? 55.127  -3.702  34.692 1.00 36.29  ? 92   ASP F C   1 
ATOM   6251  O  O   . ASP F  1 92  ? 54.307  -4.550  35.029 1.00 31.28  ? 92   ASP F O   1 
ATOM   6252  C  CB  . ASP F  1 92  ? 53.604  -1.675  34.488 1.00 34.56  ? 92   ASP F CB  1 
ATOM   6253  C  CG  . ASP F  1 92  ? 53.656  -0.166  34.758 1.00 64.88  ? 92   ASP F CG  1 
ATOM   6254  O  OD1 . ASP F  1 92  ? 53.930  0.195   35.931 1.00 66.02  ? 92   ASP F OD1 1 
ATOM   6255  O  OD2 . ASP F  1 92  ? 53.464  0.633   33.820 1.00 91.72  ? 92   ASP F OD2 1 
ATOM   6256  N  N   . GLY F  1 93  ? 56.240  -4.027  34.017 1.00 29.56  ? 93   GLY F N   1 
ATOM   6257  C  CA  . GLY F  1 93  ? 56.515  -5.447  33.763 1.00 28.97  ? 93   GLY F CA  1 
ATOM   6258  C  C   . GLY F  1 93  ? 55.925  -5.962  32.463 1.00 27.05  ? 93   GLY F C   1 
ATOM   6259  O  O   . GLY F  1 93  ? 55.972  -7.173  32.214 1.00 31.12  ? 93   GLY F O   1 
ATOM   6260  N  N   . VAL F  1 94  ? 55.380  -5.091  31.632 1.00 28.08  ? 94   VAL F N   1 
ATOM   6261  C  CA  . VAL F  1 94  ? 54.666  -5.445  30.425 1.00 26.46  ? 94   VAL F CA  1 
ATOM   6262  C  C   . VAL F  1 94  ? 55.363  -4.937  29.170 1.00 26.61  ? 94   VAL F C   1 
ATOM   6263  O  O   . VAL F  1 94  ? 55.721  -3.754  29.123 1.00 29.43  ? 94   VAL F O   1 
ATOM   6264  C  CB  . VAL F  1 94  ? 53.244  -4.834  30.415 1.00 35.51  ? 94   VAL F CB  1 
ATOM   6265  C  CG1 . VAL F  1 94  ? 52.573  -5.185  29.096 1.00 38.56  ? 94   VAL F CG1 1 
ATOM   6266  C  CG2 . VAL F  1 94  ? 52.439  -5.318  31.607 1.00 28.38  ? 94   VAL F CG2 1 
ATOM   6267  N  N   . ALA F  1 95  ? 55.528  -5.838  28.214 1.00 24.29  ? 95   ALA F N   1 
ATOM   6268  C  CA  . ALA F  1 95  ? 55.993  -5.503  26.879 1.00 27.69  ? 95   ALA F CA  1 
ATOM   6269  C  C   . ALA F  1 95  ? 54.816  -5.481  25.912 1.00 25.58  ? 95   ALA F C   1 
ATOM   6270  O  O   . ALA F  1 95  ? 54.248  -6.518  25.573 1.00 26.31  ? 95   ALA F O   1 
ATOM   6271  C  CB  . ALA F  1 95  ? 57.045  -6.478  26.353 1.00 22.35  ? 95   ALA F CB  1 
ATOM   6272  N  N   . ASP F  1 96  ? 54.456  -4.284  25.457 1.00 25.01  ? 96   ASP F N   1 
ATOM   6273  C  CA  . ASP F  1 96  ? 53.451  -4.150  24.405 1.00 27.63  ? 96   ASP F CA  1 
ATOM   6274  C  C   . ASP F  1 96  ? 54.119  -4.265  23.041 1.00 36.09  ? 96   ASP F C   1 
ATOM   6275  O  O   . ASP F  1 96  ? 54.721  -3.367  22.466 1.00 46.59  ? 96   ASP F O   1 
ATOM   6276  C  CB  . ASP F  1 96  ? 52.743  -2.810  24.538 1.00 30.86  ? 96   ASP F CB  1 
ATOM   6277  C  CG  . ASP F  1 96  ? 51.855  -2.849  25.778 1.00 46.94  ? 96   ASP F CG  1 
ATOM   6278  O  OD1 . ASP F  1 96  ? 52.032  -1.961  26.629 1.00 45.47  ? 96   ASP F OD1 1 
ATOM   6279  O  OD2 . ASP F  1 96  ? 51.034  -3.789  25.844 1.00 43.27  ? 96   ASP F OD2 1 
ATOM   6280  N  N   . VAL F  1 97  ? 54.021  -5.455  22.468 1.00 23.03  ? 97   VAL F N   1 
ATOM   6281  C  CA  . VAL F  1 97  ? 54.799  -5.729  21.272 1.00 21.04  ? 97   VAL F CA  1 
ATOM   6282  C  C   . VAL F  1 97  ? 54.109  -5.230  20.019 1.00 26.17  ? 97   VAL F C   1 
ATOM   6283  O  O   . VAL F  1 97  ? 52.920  -5.475  19.816 1.00 25.24  ? 97   VAL F O   1 
ATOM   6284  C  CB  . VAL F  1 97  ? 55.011  -7.253  21.141 1.00 26.12  ? 97   VAL F CB  1 
ATOM   6285  C  CG1 . VAL F  1 97  ? 55.751  -7.576  19.845 1.00 25.77  ? 97   VAL F CG1 1 
ATOM   6286  C  CG2 . VAL F  1 97  ? 55.717  -7.780  22.377 1.00 24.10  ? 97   VAL F CG2 1 
ATOM   6287  N  N   . SER F  1 98  ? 54.912  -4.566  19.197 1.00 21.94  ? 98   SER F N   1 
ATOM   6288  C  CA  . SER F  1 98  ? 54.404  -4.181  17.882 1.00 30.13  ? 98   SER F CA  1 
ATOM   6289  C  C   . SER F  1 98  ? 55.579  -4.046  16.924 1.00 31.45  ? 98   SER F C   1 
ATOM   6290  O  O   . SER F  1 98  ? 56.392  -3.128  17.048 1.00 29.58  ? 98   SER F O   1 
ATOM   6291  C  CB  . SER F  1 98  ? 53.571  -2.899  18.019 1.00 27.74  ? 98   SER F CB  1 
ATOM   6292  O  OG  . SER F  1 98  ? 53.056  -2.553  16.737 1.00 32.63  ? 98   SER F OG  1 
ATOM   6293  N  N   . ILE F  1 99  ? 55.695  -4.981  15.993 1.00 25.18  ? 99   ILE F N   1 
ATOM   6294  C  CA  . ILE F  1 99  ? 56.813  -5.184  15.073 1.00 26.45  ? 99   ILE F CA  1 
ATOM   6295  C  C   . ILE F  1 99  ? 56.294  -5.537  13.693 1.00 35.07  ? 99   ILE F C   1 
ATOM   6296  O  O   . ILE F  1 99  ? 55.220  -6.137  13.575 1.00 28.53  ? 99   ILE F O   1 
ATOM   6297  C  CB  . ILE F  1 99  ? 57.705  -6.325  15.606 1.00 31.30  ? 99   ILE F CB  1 
ATOM   6298  C  CG1 . ILE F  1 99  ? 58.599  -5.860  16.775 1.00 28.32  ? 99   ILE F CG1 1 
ATOM   6299  C  CG2 . ILE F  1 99  ? 58.559  -6.998  14.547 1.00 34.16  ? 99   ILE F CG2 1 
ATOM   6300  C  CD1 . ILE F  1 99  ? 59.421  -7.030  17.305 1.00 41.85  ? 99   ILE F CD1 1 
ATOM   6301  N  N   . GLU F  1 100 ? 57.008  -5.184  12.639 1.00 28.22  ? 100  GLU F N   1 
ATOM   6302  C  CA  . GLU F  1 100 ? 56.618  -5.695  11.324 1.00 25.91  ? 100  GLU F CA  1 
ATOM   6303  C  C   . GLU F  1 100 ? 57.873  -6.274  10.696 1.00 31.03  ? 100  GLU F C   1 
ATOM   6304  O  O   . GLU F  1 100 ? 58.938  -5.636  10.774 1.00 28.95  ? 100  GLU F O   1 
ATOM   6305  C  CB  . GLU F  1 100 ? 56.006  -4.585  10.489 1.00 35.95  ? 100  GLU F CB  1 
ATOM   6306  C  CG  . GLU F  1 100 ? 55.803  -4.948  9.023  1.00 41.51  ? 100  GLU F CG  1 
ATOM   6307  C  CD  . GLU F  1 100 ? 55.432  -3.708  8.215  1.00 53.36  ? 100  GLU F CD  1 
ATOM   6308  O  OE1 . GLU F  1 100 ? 54.419  -3.075  8.594  1.00 47.35  ? 100  GLU F OE1 1 
ATOM   6309  O  OE2 . GLU F  1 100 ? 56.160  -3.406  7.240  1.00 56.85  ? 100  GLU F OE2 1 
ATOM   6310  N  N   . ASP F  1 101 ? 57.796  -7.451  10.097 1.00 27.77  ? 101  ASP F N   1 
ATOM   6311  C  CA  . ASP F  1 101 ? 58.995  -8.079  9.542  1.00 26.75  ? 101  ASP F CA  1 
ATOM   6312  C  C   . ASP F  1 101 ? 58.744  -8.682  8.175  1.00 32.48  ? 101  ASP F C   1 
ATOM   6313  O  O   . ASP F  1 101 ? 57.698  -9.299  7.962  1.00 30.60  ? 101  ASP F O   1 
ATOM   6314  C  CB  . ASP F  1 101 ? 59.491  -9.185  10.481 1.00 22.31  ? 101  ASP F CB  1 
ATOM   6315  C  CG  . ASP F  1 101 ? 60.886  -9.640  10.155 1.00 26.50  ? 101  ASP F CG  1 
ATOM   6316  O  OD1 . ASP F  1 101 ? 61.104  -10.774 9.665  1.00 26.64  ? 101  ASP F OD1 1 
ATOM   6317  O  OD2 . ASP F  1 101 ? 61.808  -8.816  10.398 1.00 32.90  ? 101  ASP F OD2 1 
ATOM   6318  N  N   . SER F  1 102 ? 59.701  -8.542  7.262  1.00 34.47  ? 102  SER F N   1 
ATOM   6319  C  CA  . SER F  1 102 ? 59.456  -9.050  5.912  1.00 33.17  ? 102  SER F CA  1 
ATOM   6320  C  C   . SER F  1 102 ? 60.284  -10.270 5.618  1.00 30.42  ? 102  SER F C   1 
ATOM   6321  O  O   . SER F  1 102 ? 60.277  -10.808 4.507  1.00 35.26  ? 102  SER F O   1 
ATOM   6322  C  CB  . SER F  1 102 ? 59.706  -7.928  4.888  1.00 37.56  ? 102  SER F CB  1 
ATOM   6323  O  OG  . SER F  1 102 ? 58.555  -7.087  4.934  1.00 42.43  ? 102  SER F OG  1 
ATOM   6324  N  N   . VAL F  1 103 ? 61.000  -10.761 6.641  1.00 23.57  ? 103  VAL F N   1 
ATOM   6325  C  CA  . VAL F  1 103 ? 61.800  -11.958 6.386  1.00 22.91  ? 103  VAL F CA  1 
ATOM   6326  C  C   . VAL F  1 103 ? 61.084  -13.200 6.895  1.00 24.17  ? 103  VAL F C   1 
ATOM   6327  O  O   . VAL F  1 103 ? 61.150  -14.246 6.257  1.00 26.72  ? 103  VAL F O   1 
ATOM   6328  C  CB  . VAL F  1 103 ? 63.177  -11.800 7.043  1.00 28.83  ? 103  VAL F CB  1 
ATOM   6329  C  CG1 . VAL F  1 103 ? 63.991  -13.057 6.899  1.00 27.88  ? 103  VAL F CG1 1 
ATOM   6330  C  CG2 . VAL F  1 103 ? 63.866  -10.585 6.412  1.00 27.76  ? 103  VAL F CG2 1 
ATOM   6331  N  N   . ILE F  1 104 ? 60.408  -13.060 8.038  1.00 25.82  ? 104  ILE F N   1 
ATOM   6332  C  CA  . ILE F  1 104 ? 59.549  -14.183 8.444  1.00 25.34  ? 104  ILE F CA  1 
ATOM   6333  C  C   . ILE F  1 104 ? 58.337  -14.199 7.527  1.00 25.60  ? 104  ILE F C   1 
ATOM   6334  O  O   . ILE F  1 104 ? 57.987  -13.191 6.901  1.00 24.89  ? 104  ILE F O   1 
ATOM   6335  C  CB  . ILE F  1 104 ? 59.067  -14.088 9.905  1.00 23.09  ? 104  ILE F CB  1 
ATOM   6336  C  CG1 . ILE F  1 104 ? 58.371  -12.780 10.258 1.00 27.33  ? 104  ILE F CG1 1 
ATOM   6337  C  CG2 . ILE F  1 104 ? 60.241  -14.344 10.858 1.00 21.82  ? 104  ILE F CG2 1 
ATOM   6338  C  CD1 . ILE F  1 104 ? 57.524  -12.806 11.522 1.00 24.17  ? 104  ILE F CD1 1 
ATOM   6339  N  N   . SER F  1 105 ? 57.670  -15.360 7.466  1.00 27.44  ? 105  SER F N   1 
ATOM   6340  C  CA  . SER F  1 105 ? 56.464  -15.440 6.637  1.00 22.41  ? 105  SER F CA  1 
ATOM   6341  C  C   . SER F  1 105 ? 55.465  -16.424 7.225  1.00 24.33  ? 105  SER F C   1 
ATOM   6342  O  O   . SER F  1 105 ? 55.874  -17.235 8.071  1.00 28.12  ? 105  SER F O   1 
ATOM   6343  C  CB  . SER F  1 105 ? 56.838  -15.928 5.228  1.00 26.31  ? 105  SER F CB  1 
ATOM   6344  O  OG  . SER F  1 105 ? 55.645  -15.899 4.434  1.00 31.37  ? 105  SER F OG  1 
ATOM   6345  N  N   . LEU F  1 106 ? 54.216  -16.400 6.789  1.00 23.53  ? 106  LEU F N   1 
ATOM   6346  C  CA  . LEU F  1 106 ? 53.311  -17.431 7.326  1.00 28.10  ? 106  LEU F CA  1 
ATOM   6347  C  C   . LEU F  1 106 ? 53.096  -18.499 6.252  1.00 32.50  ? 106  LEU F C   1 
ATOM   6348  O  O   . LEU F  1 106 ? 52.186  -19.313 6.327  1.00 32.63  ? 106  LEU F O   1 
ATOM   6349  C  CB  . LEU F  1 106 ? 51.992  -16.843 7.812  1.00 25.14  ? 106  LEU F CB  1 
ATOM   6350  C  CG  . LEU F  1 106 ? 52.099  -15.734 8.868  1.00 26.70  ? 106  LEU F CG  1 
ATOM   6351  C  CD1 . LEU F  1 106 ? 50.748  -15.160 9.258  1.00 28.81  ? 106  LEU F CD1 1 
ATOM   6352  C  CD2 . LEU F  1 106 ? 52.846  -16.255 10.094 1.00 22.38  ? 106  LEU F CD2 1 
ATOM   6353  N  N   . SER F  1 107 ? 53.928  -18.515 5.221  1.00 29.86  ? 107  SER F N   1 
ATOM   6354  C  CA  . SER F  1 107 ? 53.880  -19.551 4.194  1.00 31.93  ? 107  SER F CA  1 
ATOM   6355  C  C   . SER F  1 107 ? 55.243  -19.700 3.532  1.00 35.79  ? 107  SER F C   1 
ATOM   6356  O  O   . SER F  1 107 ? 56.063  -18.798 3.690  1.00 33.16  ? 107  SER F O   1 
ATOM   6357  C  CB  . SER F  1 107 ? 52.848  -19.201 3.116  1.00 41.94  ? 107  SER F CB  1 
ATOM   6358  O  OG  . SER F  1 107 ? 53.381  -18.145 2.330  1.00 51.07  ? 107  SER F OG  1 
ATOM   6359  N  N   . GLY F  1 108 ? 55.480  -20.784 2.811  1.00 34.71  ? 108  GLY F N   1 
ATOM   6360  C  CA  . GLY F  1 108 ? 56.733  -21.010 2.129  1.00 39.43  ? 108  GLY F CA  1 
ATOM   6361  C  C   . GLY F  1 108 ? 57.889  -21.439 2.999  1.00 38.97  ? 108  GLY F C   1 
ATOM   6362  O  O   . GLY F  1 108 ? 57.700  -21.962 4.097  1.00 40.38  ? 108  GLY F O   1 
ATOM   6363  N  N   . ASP F  1 109 ? 59.093  -21.220 2.498  1.00 37.87  ? 109  ASP F N   1 
ATOM   6364  C  CA  . ASP F  1 109 ? 60.379  -21.578 3.032  1.00 42.89  ? 109  ASP F CA  1 
ATOM   6365  C  C   . ASP F  1 109 ? 60.655  -20.972 4.416  1.00 30.20  ? 109  ASP F C   1 
ATOM   6366  O  O   . ASP F  1 109 ? 61.291  -21.616 5.242  1.00 38.60  ? 109  ASP F O   1 
ATOM   6367  C  CB  . ASP F  1 109 ? 61.516  -21.018 2.154  1.00 51.68  ? 109  ASP F CB  1 
ATOM   6368  C  CG  . ASP F  1 109 ? 61.847  -21.813 0.915  1.00 57.19  ? 109  ASP F CG  1 
ATOM   6369  O  OD1 . ASP F  1 109 ? 61.222  -22.867 0.678  1.00 67.39  ? 109  ASP F OD1 1 
ATOM   6370  O  OD2 . ASP F  1 109 ? 62.750  -21.370 0.169  1.00 71.42  ? 109  ASP F OD2 1 
ATOM   6371  N  N   . HIS F  1 110 ? 60.191  -19.736 4.511  1.00 26.70  ? 110  HIS F N   1 
ATOM   6372  C  CA  . HIS F  1 110 ? 60.416  -18.915 5.685  1.00 30.15  ? 110  HIS F CA  1 
ATOM   6373  C  C   . HIS F  1 110 ? 59.232  -18.959 6.649  1.00 29.36  ? 110  HIS F C   1 
ATOM   6374  O  O   . HIS F  1 110 ? 59.116  -18.111 7.542  1.00 24.92  ? 110  HIS F O   1 
ATOM   6375  C  CB  . HIS F  1 110 ? 60.634  -17.447 5.279  1.00 37.80  ? 110  HIS F CB  1 
ATOM   6376  C  CG  . HIS F  1 110 ? 61.980  -17.262 4.641  1.00 44.59  ? 110  HIS F CG  1 
ATOM   6377  N  ND1 . HIS F  1 110 ? 62.555  -16.029 4.457  1.00 44.39  ? 110  HIS F ND1 1 
ATOM   6378  C  CD2 . HIS F  1 110 ? 62.856  -18.171 4.163  1.00 46.54  ? 110  HIS F CD2 1 
ATOM   6379  C  CE1 . HIS F  1 110 ? 63.740  -16.189 3.882  1.00 41.24  ? 110  HIS F CE1 1 
ATOM   6380  N  NE2 . HIS F  1 110 ? 63.949  -17.481 3.689  1.00 38.30  ? 110  HIS F NE2 1 
ATOM   6381  N  N   . CYS F  1 111 ? 58.351  -19.929 6.428  1.00 27.88  ? 111  CYS F N   1 
ATOM   6382  C  CA  . CYS F  1 111 ? 57.181  -20.063 7.274  1.00 28.73  ? 111  CYS F CA  1 
ATOM   6383  C  C   . CYS F  1 111 ? 57.530  -20.373 8.735  1.00 21.17  ? 111  CYS F C   1 
ATOM   6384  O  O   . CYS F  1 111 ? 58.338  -21.279 8.967  1.00 23.50  ? 111  CYS F O   1 
ATOM   6385  C  CB  . CYS F  1 111 ? 56.307  -21.227 6.749  1.00 27.69  ? 111  CYS F CB  1 
ATOM   6386  S  SG  . CYS F  1 111 ? 54.729  -21.212 7.655  1.00 37.86  ? 111  CYS F SG  1 
ATOM   6387  N  N   . ILE F  1 112 ? 56.908  -19.654 9.671  1.00 21.16  ? 112  ILE F N   1 
ATOM   6388  C  CA  . ILE F  1 112 ? 57.195  -19.866 11.084 1.00 21.54  ? 112  ILE F CA  1 
ATOM   6389  C  C   . ILE F  1 112 ? 56.069  -20.637 11.777 1.00 27.04  ? 112  ILE F C   1 
ATOM   6390  O  O   . ILE F  1 112 ? 56.174  -20.859 12.984 1.00 20.68  ? 112  ILE F O   1 
ATOM   6391  C  CB  . ILE F  1 112 ? 57.392  -18.507 11.787 1.00 19.32  ? 112  ILE F CB  1 
ATOM   6392  C  CG1 . ILE F  1 112 ? 56.207  -17.560 11.670 1.00 24.06  ? 112  ILE F CG1 1 
ATOM   6393  C  CG2 . ILE F  1 112 ? 58.667  -17.866 11.223 1.00 24.35  ? 112  ILE F CG2 1 
ATOM   6394  C  CD1 . ILE F  1 112 ? 56.324  -16.265 12.470 1.00 26.07  ? 112  ILE F CD1 1 
ATOM   6395  N  N   . ILE F  1 113 ? 55.003  -21.031 11.078 1.00 25.32  ? 113  ILE F N   1 
ATOM   6396  C  CA  . ILE F  1 113 ? 53.950  -21.859 11.675 1.00 23.46  ? 113  ILE F CA  1 
ATOM   6397  C  C   . ILE F  1 113 ? 54.515  -23.172 12.166 1.00 22.12  ? 113  ILE F C   1 
ATOM   6398  O  O   . ILE F  1 113 ? 55.285  -23.833 11.443 1.00 21.89  ? 113  ILE F O   1 
ATOM   6399  C  CB  . ILE F  1 113 ? 52.855  -22.170 10.648 1.00 30.33  ? 113  ILE F CB  1 
ATOM   6400  C  CG1 . ILE F  1 113 ? 52.342  -20.903 9.958  1.00 38.69  ? 113  ILE F CG1 1 
ATOM   6401  C  CG2 . ILE F  1 113 ? 51.697  -22.960 11.262 1.00 22.06  ? 113  ILE F CG2 1 
ATOM   6402  C  CD1 . ILE F  1 113 ? 51.653  -20.005 10.946 1.00 27.11  ? 113  ILE F CD1 1 
ATOM   6403  N  N   . GLY F  1 114 ? 54.178  -23.601 13.392 1.00 17.07  ? 114  GLY F N   1 
ATOM   6404  C  CA  . GLY F  1 114 ? 54.722  -24.859 13.887 1.00 17.43  ? 114  GLY F CA  1 
ATOM   6405  C  C   . GLY F  1 114 ? 56.095  -24.731 14.527 1.00 19.61  ? 114  GLY F C   1 
ATOM   6406  O  O   . GLY F  1 114 ? 56.682  -25.685 15.018 1.00 20.49  ? 114  GLY F O   1 
ATOM   6407  N  N   . ARG F  1 115 ? 56.662  -23.525 14.524 1.00 17.24  ? 115  ARG F N   1 
ATOM   6408  C  CA  . ARG F  1 115 ? 57.924  -23.301 15.214 1.00 19.71  ? 115  ARG F CA  1 
ATOM   6409  C  C   . ARG F  1 115 ? 57.681  -22.579 16.531 1.00 21.61  ? 115  ARG F C   1 
ATOM   6410  O  O   . ARG F  1 115 ? 56.522  -22.316 16.866 1.00 23.54  ? 115  ARG F O   1 
ATOM   6411  C  CB  . ARG F  1 115 ? 58.847  -22.514 14.269 1.00 22.03  ? 115  ARG F CB  1 
ATOM   6412  C  CG  . ARG F  1 115 ? 59.060  -23.351 12.990 1.00 24.33  ? 115  ARG F CG  1 
ATOM   6413  C  CD  . ARG F  1 115 ? 60.173  -22.795 12.119 1.00 29.66  ? 115  ARG F CD  1 
ATOM   6414  N  NE  . ARG F  1 115 ? 60.195  -23.452 10.797 1.00 27.40  ? 115  ARG F NE  1 
ATOM   6415  C  CZ  . ARG F  1 115 ? 60.856  -24.558 10.502 1.00 28.78  ? 115  ARG F CZ  1 
ATOM   6416  N  NH1 . ARG F  1 115 ? 60.783  -25.038 9.246  1.00 26.27  ? 115  ARG F NH1 1 
ATOM   6417  N  NH2 . ARG F  1 115 ? 61.587  -25.200 11.406 1.00 21.67  ? 115  ARG F NH2 1 
ATOM   6418  N  N   . THR F  1 116 ? 58.711  -22.233 17.278 1.00 19.03  ? 116  THR F N   1 
ATOM   6419  C  CA  . THR F  1 116 ? 58.512  -21.679 18.631 1.00 16.64  ? 116  THR F CA  1 
ATOM   6420  C  C   . THR F  1 116 ? 58.962  -20.238 18.731 1.00 21.21  ? 116  THR F C   1 
ATOM   6421  O  O   . THR F  1 116 ? 60.101  -19.891 18.349 1.00 23.54  ? 116  THR F O   1 
ATOM   6422  C  CB  . THR F  1 116 ? 59.284  -22.542 19.658 1.00 22.22  ? 116  THR F CB  1 
ATOM   6423  O  OG1 . THR F  1 116 ? 58.704  -23.854 19.727 1.00 20.90  ? 116  THR F OG1 1 
ATOM   6424  C  CG2 . THR F  1 116 ? 59.228  -21.944 21.070 1.00 16.42  ? 116  THR F CG2 1 
ATOM   6425  N  N   . LEU F  1 117 ? 58.097  -19.406 19.299 1.00 19.19  ? 117  LEU F N   1 
ATOM   6426  C  CA  . LEU F  1 117 ? 58.437  -18.025 19.648 1.00 17.40  ? 117  LEU F CA  1 
ATOM   6427  C  C   . LEU F  1 117 ? 59.000  -18.013 21.066 1.00 21.51  ? 117  LEU F C   1 
ATOM   6428  O  O   . LEU F  1 117 ? 58.433  -18.652 21.956 1.00 19.37  ? 117  LEU F O   1 
ATOM   6429  C  CB  . LEU F  1 117 ? 57.183  -17.140 19.514 1.00 18.07  ? 117  LEU F CB  1 
ATOM   6430  C  CG  . LEU F  1 117 ? 57.403  -15.639 19.735 1.00 22.57  ? 117  LEU F CG  1 
ATOM   6431  C  CD1 . LEU F  1 117 ? 58.302  -15.086 18.637 1.00 20.25  ? 117  LEU F CD1 1 
ATOM   6432  C  CD2 . LEU F  1 117 ? 56.094  -14.871 19.813 1.00 21.36  ? 117  LEU F CD2 1 
ATOM   6433  N  N   . VAL F  1 118 ? 60.117  -17.340 21.310 1.00 19.23  ? 118  VAL F N   1 
ATOM   6434  C  CA  . VAL F  1 118 ? 60.804  -17.340 22.599 1.00 19.25  ? 118  VAL F CA  1 
ATOM   6435  C  C   . VAL F  1 118 ? 61.108  -15.905 23.004 1.00 21.51  ? 118  VAL F C   1 
ATOM   6436  O  O   . VAL F  1 118 ? 61.559  -15.114 22.177 1.00 18.52  ? 118  VAL F O   1 
ATOM   6437  C  CB  . VAL F  1 118 ? 62.137  -18.118 22.560 1.00 19.55  ? 118  VAL F CB  1 
ATOM   6438  C  CG1 . VAL F  1 118 ? 62.832  -18.130 23.921 1.00 23.24  ? 118  VAL F CG1 1 
ATOM   6439  C  CG2 . VAL F  1 118 ? 61.876  -19.553 22.116 1.00 21.00  ? 118  VAL F CG2 1 
ATOM   6440  N  N   . VAL F  1 119 ? 60.853  -15.593 24.279 1.00 19.03  ? 119  VAL F N   1 
ATOM   6441  C  CA  . VAL F  1 119 ? 61.287  -14.315 24.826 1.00 17.94  ? 119  VAL F CA  1 
ATOM   6442  C  C   . VAL F  1 119 ? 62.327  -14.592 25.907 1.00 20.27  ? 119  VAL F C   1 
ATOM   6443  O  O   . VAL F  1 119 ? 62.232  -15.547 26.683 1.00 19.31  ? 119  VAL F O   1 
ATOM   6444  C  CB  . VAL F  1 119 ? 60.108  -13.467 25.336 1.00 19.77  ? 119  VAL F CB  1 
ATOM   6445  C  CG1 . VAL F  1 119 ? 59.300  -14.161 26.421 1.00 19.94  ? 119  VAL F CG1 1 
ATOM   6446  C  CG2 . VAL F  1 119 ? 60.630  -12.115 25.857 1.00 19.23  ? 119  VAL F CG2 1 
ATOM   6447  N  N   . HIS F  1 120 ? 63.373  -13.771 25.949 1.00 16.74  ? 120  HIS F N   1 
ATOM   6448  C  CA  . HIS F  1 120 ? 64.584  -14.112 26.675 1.00 18.63  ? 120  HIS F CA  1 
ATOM   6449  C  C   . HIS F  1 120 ? 64.857  -13.264 27.908 1.00 18.87  ? 120  HIS F C   1 
ATOM   6450  O  O   . HIS F  1 120 ? 64.278  -12.205 28.108 1.00 23.32  ? 120  HIS F O   1 
ATOM   6451  C  CB  . HIS F  1 120 ? 65.798  -13.945 25.741 1.00 20.19  ? 120  HIS F CB  1 
ATOM   6452  C  CG  . HIS F  1 120 ? 65.954  -15.042 24.731 1.00 16.97  ? 120  HIS F CG  1 
ATOM   6453  N  ND1 . HIS F  1 120 ? 66.736  -16.140 24.965 1.00 17.93  ? 120  HIS F ND1 1 
ATOM   6454  C  CD2 . HIS F  1 120 ? 65.450  -15.199 23.472 1.00 17.49  ? 120  HIS F CD2 1 
ATOM   6455  C  CE1 . HIS F  1 120 ? 66.726  -16.952 23.914 1.00 18.43  ? 120  HIS F CE1 1 
ATOM   6456  N  NE2 . HIS F  1 120 ? 65.954  -16.405 23.004 1.00 19.48  ? 120  HIS F NE2 1 
ATOM   6457  N  N   . GLU F  1 121 ? 65.794  -13.797 28.684 1.00 19.12  ? 121  GLU F N   1 
ATOM   6458  C  CA  . GLU F  1 121 ? 66.230  -13.159 29.930 1.00 24.97  ? 121  GLU F CA  1 
ATOM   6459  C  C   . GLU F  1 121 ? 66.838  -11.783 29.728 1.00 23.15  ? 121  GLU F C   1 
ATOM   6460  O  O   . GLU F  1 121 ? 66.509  -10.815 30.426 1.00 24.70  ? 121  GLU F O   1 
ATOM   6461  C  CB  . GLU F  1 121 ? 67.238  -14.123 30.564 1.00 28.03  ? 121  GLU F CB  1 
ATOM   6462  C  CG  . GLU F  1 121 ? 67.809  -13.699 31.903 1.00 34.40  ? 121  GLU F CG  1 
ATOM   6463  C  CD  . GLU F  1 121 ? 69.130  -14.401 32.192 1.00 47.29  ? 121  GLU F CD  1 
ATOM   6464  O  OE1 . GLU F  1 121 ? 69.753  -14.036 33.216 1.00 53.60  ? 121  GLU F OE1 1 
ATOM   6465  O  OE2 . GLU F  1 121 ? 69.575  -15.287 31.422 1.00 34.05  ? 121  GLU F OE2 1 
ATOM   6466  N  N   . LYS F  1 122 ? 67.765  -11.691 28.779 1.00 21.32  ? 122  LYS F N   1 
ATOM   6467  C  CA  . LYS F  1 122 ? 68.549  -10.465 28.572 1.00 25.45  ? 122  LYS F CA  1 
ATOM   6468  C  C   . LYS F  1 122 ? 68.315  -9.869  27.194 1.00 22.58  ? 122  LYS F C   1 
ATOM   6469  O  O   . LYS F  1 122 ? 67.652  -10.493 26.350 1.00 23.00  ? 122  LYS F O   1 
ATOM   6470  C  CB  . LYS F  1 122 ? 70.059  -10.732 28.677 1.00 26.45  ? 122  LYS F CB  1 
ATOM   6471  C  CG  . LYS F  1 122 ? 70.533  -11.691 29.738 1.00 38.59  ? 122  LYS F CG  1 
ATOM   6472  C  CD  . LYS F  1 122 ? 72.052  -11.757 29.825 1.00 36.31  ? 122  LYS F CD  1 
ATOM   6473  C  CE  . LYS F  1 122 ? 72.628  -12.918 29.031 1.00 35.96  ? 122  LYS F CE  1 
ATOM   6474  N  NZ  . LYS F  1 122 ? 74.114  -12.829 28.832 1.00 39.87  ? 122  LYS F NZ  1 
ATOM   6475  N  N   . ALA F  1 123 ? 68.885  -8.686  26.970 1.00 20.83  ? 123  ALA F N   1 
ATOM   6476  C  CA  . ALA F  1 123 ? 68.827  -8.047  25.669 1.00 22.86  ? 123  ALA F CA  1 
ATOM   6477  C  C   . ALA F  1 123 ? 69.552  -8.876  24.622 1.00 20.27  ? 123  ALA F C   1 
ATOM   6478  O  O   . ALA F  1 123 ? 70.567  -9.485  24.935 1.00 23.22  ? 123  ALA F O   1 
ATOM   6479  C  CB  . ALA F  1 123 ? 69.423  -6.638  25.719 1.00 22.03  ? 123  ALA F CB  1 
ATOM   6480  N  N   . ASP F  1 124 ? 69.055  -8.839  23.393 1.00 19.86  ? 124  ASP F N   1 
ATOM   6481  C  CA  . ASP F  1 124 ? 69.744  -9.344  22.211 1.00 19.83  ? 124  ASP F CA  1 
ATOM   6482  C  C   . ASP F  1 124 ? 70.729  -8.279  21.711 1.00 20.66  ? 124  ASP F C   1 
ATOM   6483  O  O   . ASP F  1 124 ? 70.336  -7.131  21.504 1.00 19.99  ? 124  ASP F O   1 
ATOM   6484  C  CB  . ASP F  1 124 ? 68.676  -9.704  21.183 1.00 21.20  ? 124  ASP F CB  1 
ATOM   6485  C  CG  . ASP F  1 124 ? 69.210  -10.336 19.916 1.00 23.91  ? 124  ASP F CG  1 
ATOM   6486  O  OD1 . ASP F  1 124 ? 68.434  -11.059 19.252 1.00 21.89  ? 124  ASP F OD1 1 
ATOM   6487  O  OD2 . ASP F  1 124 ? 70.394  -10.112 19.541 1.00 22.09  ? 124  ASP F OD2 1 
ATOM   6488  N  N   . ASP F  1 125 ? 72.014  -8.607  21.547 1.00 19.70  ? 125  ASP F N   1 
ATOM   6489  C  CA  . ASP F  1 125 ? 72.995  -7.585  21.142 1.00 22.48  ? 125  ASP F CA  1 
ATOM   6490  C  C   . ASP F  1 125 ? 73.074  -7.458  19.620 1.00 22.61  ? 125  ASP F C   1 
ATOM   6491  O  O   . ASP F  1 125 ? 73.942  -6.764  19.094 1.00 22.64  ? 125  ASP F O   1 
ATOM   6492  C  CB  . ASP F  1 125 ? 74.368  -7.929  21.716 1.00 21.19  ? 125  ASP F CB  1 
ATOM   6493  C  CG  . ASP F  1 125 ? 75.066  -9.138  21.135 1.00 21.77  ? 125  ASP F CG  1 
ATOM   6494  O  OD1 . ASP F  1 125 ? 76.094  -9.577  21.766 1.00 24.58  ? 125  ASP F OD1 1 
ATOM   6495  O  OD2 . ASP F  1 125 ? 74.710  -9.680  20.063 1.00 19.73  ? 125  ASP F OD2 1 
ATOM   6496  N  N   . LEU F  1 126 ? 72.165  -8.114  18.905 1.00 20.50  ? 126  LEU F N   1 
ATOM   6497  C  CA  . LEU F  1 126 ? 71.942  -7.996  17.469 1.00 18.76  ? 126  LEU F CA  1 
ATOM   6498  C  C   . LEU F  1 126 ? 73.163  -8.431  16.659 1.00 21.06  ? 126  LEU F C   1 
ATOM   6499  O  O   . LEU F  1 126 ? 73.385  -8.041  15.506 1.00 20.74  ? 126  LEU F O   1 
ATOM   6500  C  CB  . LEU F  1 126 ? 71.484  -6.576  17.116 1.00 21.43  ? 126  LEU F CB  1 
ATOM   6501  C  CG  . LEU F  1 126 ? 70.293  -6.010  17.919 1.00 23.32  ? 126  LEU F CG  1 
ATOM   6502  C  CD1 . LEU F  1 126 ? 69.944  -4.615  17.389 1.00 22.31  ? 126  LEU F CD1 1 
ATOM   6503  C  CD2 . LEU F  1 126 ? 69.068  -6.909  17.914 1.00 22.89  ? 126  LEU F CD2 1 
ATOM   6504  N  N   . GLY F  1 127 ? 73.961  -9.322  17.239 1.00 20.93  ? 127  GLY F N   1 
ATOM   6505  C  CA  . GLY F  1 127 ? 75.063  -9.967  16.538 1.00 20.59  ? 127  GLY F CA  1 
ATOM   6506  C  C   . GLY F  1 127 ? 76.326  -9.104  16.555 1.00 24.48  ? 127  GLY F C   1 
ATOM   6507  O  O   . GLY F  1 127 ? 77.297  -9.442  15.847 1.00 20.55  ? 127  GLY F O   1 
ATOM   6508  N  N   . LYS F  1 128 ? 76.284  -8.044  17.339 1.00 17.35  ? 128  LYS F N   1 
ATOM   6509  C  CA  . LYS F  1 128 ? 77.416  -7.097  17.348 1.00 20.18  ? 128  LYS F CA  1 
ATOM   6510  C  C   . LYS F  1 128 ? 78.275  -7.185  18.610 1.00 23.70  ? 128  LYS F C   1 
ATOM   6511  O  O   . LYS F  1 128 ? 78.956  -6.205  18.958 1.00 21.67  ? 128  LYS F O   1 
ATOM   6512  C  CB  . LYS F  1 128 ? 76.870  -5.675  17.214 1.00 18.35  ? 128  LYS F CB  1 
ATOM   6513  C  CG  . LYS F  1 128 ? 76.113  -5.506  15.892 1.00 25.59  ? 128  LYS F CG  1 
ATOM   6514  C  CD  . LYS F  1 128 ? 75.299  -4.216  15.904 1.00 35.47  ? 128  LYS F CD  1 
ATOM   6515  C  CE  . LYS F  1 128 ? 76.208  -2.997  15.807 1.00 37.02  ? 128  LYS F CE  1 
ATOM   6516  N  NZ  . LYS F  1 128 ? 75.451  -1.778  15.403 1.00 52.52  ? 128  LYS F NZ  1 
ATOM   6517  N  N   . GLY F  1 129 ? 78.234  -8.304  19.312 1.00 20.83  ? 129  GLY F N   1 
ATOM   6518  C  CA  . GLY F  1 129 ? 78.932  -8.413  20.586 1.00 21.24  ? 129  GLY F CA  1 
ATOM   6519  C  C   . GLY F  1 129 ? 80.365  -8.876  20.476 1.00 22.65  ? 129  GLY F C   1 
ATOM   6520  O  O   . GLY F  1 129 ? 81.067  -8.803  21.499 1.00 20.87  ? 129  GLY F O   1 
ATOM   6521  N  N   . GLY F  1 130 ? 80.789  -9.331  19.304 1.00 18.08  ? 130  GLY F N   1 
ATOM   6522  C  CA  . GLY F  1 130 ? 82.197  -9.680  19.110 1.00 18.69  ? 130  GLY F CA  1 
ATOM   6523  C  C   . GLY F  1 130 ? 82.643  -10.964 19.758 1.00 30.42  ? 130  GLY F C   1 
ATOM   6524  O  O   . GLY F  1 130 ? 83.822  -11.334 19.691 1.00 22.69  ? 130  GLY F O   1 
ATOM   6525  N  N   . ASN F  1 131 ? 81.743  -11.709 20.401 1.00 24.35  ? 131  ASN F N   1 
ATOM   6526  C  CA  . ASN F  1 131 ? 82.165  -13.010 20.925 1.00 23.68  ? 131  ASN F CA  1 
ATOM   6527  C  C   . ASN F  1 131 ? 81.461  -14.079 20.123 1.00 29.33  ? 131  ASN F C   1 
ATOM   6528  O  O   . ASN F  1 131 ? 80.577  -13.847 19.288 1.00 29.28  ? 131  ASN F O   1 
ATOM   6529  C  CB  . ASN F  1 131 ? 81.930  -13.155 22.424 1.00 22.46  ? 131  ASN F CB  1 
ATOM   6530  C  CG  . ASN F  1 131 ? 80.481  -13.098 22.841 1.00 29.78  ? 131  ASN F CG  1 
ATOM   6531  O  OD1 . ASN F  1 131 ? 79.605  -12.854 22.010 1.00 25.98  ? 131  ASN F OD1 1 
ATOM   6532  N  ND2 . ASN F  1 131 ? 80.233  -13.326 24.124 1.00 28.29  ? 131  ASN F ND2 1 
ATOM   6533  N  N   . GLU F  1 132 ? 81.847  -15.337 20.336 1.00 26.43  ? 132  GLU F N   1 
ATOM   6534  C  CA  . GLU F  1 132 ? 81.208  -16.353 19.524 1.00 21.55  ? 132  GLU F CA  1 
ATOM   6535  C  C   . GLU F  1 132 ? 79.700  -16.461 19.754 1.00 25.50  ? 132  GLU F C   1 
ATOM   6536  O  O   . GLU F  1 132 ? 78.903  -16.718 18.848 1.00 28.46  ? 132  GLU F O   1 
ATOM   6537  C  CB  . GLU F  1 132 ? 81.844  -17.711 19.876 1.00 30.04  ? 132  GLU F CB  1 
ATOM   6538  C  CG  . GLU F  1 132 ? 83.287  -17.529 20.390 1.00 33.87  ? 132  GLU F CG  1 
ATOM   6539  C  CD  . GLU F  1 132 ? 83.957  -18.874 20.634 1.00 58.73  ? 132  GLU F CD  1 
ATOM   6540  O  OE1 . GLU F  1 132 ? 83.282  -19.832 21.081 1.00 48.67  ? 132  GLU F OE1 1 
ATOM   6541  O  OE2 . GLU F  1 132 ? 85.179  -18.979 20.375 1.00 68.74  ? 132  GLU F OE2 1 
ATOM   6542  N  N   . GLU F  1 133 ? 79.314  -16.279 21.011 1.00 25.09  ? 133  GLU F N   1 
ATOM   6543  C  CA  . GLU F  1 133 ? 77.877  -16.416 21.336 1.00 25.94  ? 133  GLU F CA  1 
ATOM   6544  C  C   . GLU F  1 133 ? 77.059  -15.324 20.671 1.00 27.27  ? 133  GLU F C   1 
ATOM   6545  O  O   . GLU F  1 133 ? 75.887  -15.537 20.319 1.00 27.56  ? 133  GLU F O   1 
ATOM   6546  C  CB  . GLU F  1 133 ? 77.743  -16.414 22.855 1.00 27.41  ? 133  GLU F CB  1 
ATOM   6547  C  CG  . GLU F  1 133 ? 76.317  -16.584 23.360 1.00 36.87  ? 133  GLU F CG  1 
ATOM   6548  C  CD  . GLU F  1 133 ? 75.773  -17.992 23.192 1.00 43.22  ? 133  GLU F CD  1 
ATOM   6549  O  OE1 . GLU F  1 133 ? 74.534  -18.132 23.138 1.00 57.48  ? 133  GLU F OE1 1 
ATOM   6550  O  OE2 . GLU F  1 133 ? 76.570  -18.953 23.129 1.00 51.02  ? 133  GLU F OE2 1 
ATOM   6551  N  N   . SER F  1 134 ? 77.612  -14.135 20.451 1.00 22.33  ? 134  SER F N   1 
ATOM   6552  C  CA  . SER F  1 134 ? 76.840  -13.077 19.791 1.00 23.67  ? 134  SER F CA  1 
ATOM   6553  C  C   . SER F  1 134 ? 76.363  -13.546 18.414 1.00 23.30  ? 134  SER F C   1 
ATOM   6554  O  O   . SER F  1 134 ? 75.225  -13.237 18.024 1.00 23.20  ? 134  SER F O   1 
ATOM   6555  C  CB  . SER F  1 134 ? 77.647  -11.779 19.666 1.00 20.16  ? 134  SER F CB  1 
ATOM   6556  O  OG  . SER F  1 134 ? 76.925  -10.764 18.957 1.00 21.78  ? 134  SER F OG  1 
ATOM   6557  N  N   . THR F  1 135 ? 77.196  -14.308 17.719 1.00 20.88  ? 135  THR F N   1 
ATOM   6558  C  CA  . THR F  1 135 ? 76.916  -14.754 16.376 1.00 21.06  ? 135  THR F CA  1 
ATOM   6559  C  C   . THR F  1 135 ? 75.890  -15.897 16.342 1.00 20.83  ? 135  THR F C   1 
ATOM   6560  O  O   . THR F  1 135 ? 75.484  -16.256 15.242 1.00 25.88  ? 135  THR F O   1 
ATOM   6561  C  CB  . THR F  1 135 ? 78.148  -15.320 15.616 1.00 27.76  ? 135  THR F CB  1 
ATOM   6562  O  OG1 . THR F  1 135 ? 78.556  -16.543 16.268 1.00 35.52  ? 135  THR F OG1 1 
ATOM   6563  C  CG2 . THR F  1 135 ? 79.324  -14.382 15.683 1.00 27.46  ? 135  THR F CG2 1 
ATOM   6564  N  N   . LYS F  1 136 ? 75.536  -16.368 17.522 1.00 23.95  ? 136  LYS F N   1 
ATOM   6565  C  CA  . LYS F  1 136 ? 74.576  -17.457 17.589 1.00 25.80  ? 136  LYS F CA  1 
ATOM   6566  C  C   . LYS F  1 136 ? 73.255  -16.997 18.176 1.00 23.91  ? 136  LYS F C   1 
ATOM   6567  O  O   . LYS F  1 136 ? 72.189  -17.215 17.601 1.00 25.70  ? 136  LYS F O   1 
ATOM   6568  C  CB  . LYS F  1 136 ? 75.178  -18.590 18.440 1.00 26.25  ? 136  LYS F CB  1 
ATOM   6569  C  CG  . LYS F  1 136 ? 76.324  -19.283 17.697 1.00 29.63  ? 136  LYS F CG  1 
ATOM   6570  C  CD  . LYS F  1 136 ? 76.741  -20.545 18.444 1.00 44.25  ? 136  LYS F CD  1 
ATOM   6571  C  CE  . LYS F  1 136 ? 78.043  -20.318 19.203 1.00 50.42  ? 136  LYS F CE  1 
ATOM   6572  N  NZ  . LYS F  1 136 ? 78.311  -21.388 20.204 1.00 60.00  ? 136  LYS F NZ  1 
ATOM   6573  N  N   . THR F  1 137 ? 73.352  -16.360 19.338 1.00 24.74  ? 137  THR F N   1 
ATOM   6574  C  CA  . THR F  1 137 ? 72.141  -16.053 20.092 1.00 27.02  ? 137  THR F CA  1 
ATOM   6575  C  C   . THR F  1 137 ? 71.994  -14.586 20.405 1.00 26.70  ? 137  THR F C   1 
ATOM   6576  O  O   . THR F  1 137 ? 70.982  -14.163 20.982 1.00 23.26  ? 137  THR F O   1 
ATOM   6577  C  CB  . THR F  1 137 ? 72.175  -16.809 21.436 1.00 27.14  ? 137  THR F CB  1 
ATOM   6578  O  OG1 . THR F  1 137 ? 73.273  -16.308 22.225 1.00 27.23  ? 137  THR F OG1 1 
ATOM   6579  C  CG2 . THR F  1 137 ? 72.464  -18.291 21.263 1.00 28.81  ? 137  THR F CG2 1 
ATOM   6580  N  N   . GLY F  1 138 ? 72.994  -13.752 20.101 1.00 21.48  ? 138  GLY F N   1 
ATOM   6581  C  CA  . GLY F  1 138 ? 72.886  -12.363 20.497 1.00 18.87  ? 138  GLY F CA  1 
ATOM   6582  C  C   . GLY F  1 138 ? 73.156  -12.183 21.992 1.00 20.79  ? 138  GLY F C   1 
ATOM   6583  O  O   . GLY F  1 138 ? 72.926  -11.098 22.524 1.00 21.57  ? 138  GLY F O   1 
ATOM   6584  N  N   . ASN F  1 139 ? 73.670  -13.237 22.641 1.00 18.73  ? 139  ASN F N   1 
ATOM   6585  C  CA  . ASN F  1 139 ? 73.891  -13.174 24.087 1.00 19.40  ? 139  ASN F CA  1 
ATOM   6586  C  C   . ASN F  1 139 ? 72.590  -12.883 24.836 1.00 23.68  ? 139  ASN F C   1 
ATOM   6587  O  O   . ASN F  1 139 ? 72.596  -12.168 25.837 1.00 21.04  ? 139  ASN F O   1 
ATOM   6588  C  CB  . ASN F  1 139 ? 74.937  -12.112 24.468 1.00 21.59  ? 139  ASN F CB  1 
ATOM   6589  C  CG  . ASN F  1 139 ? 76.337  -12.574 24.089 1.00 27.51  ? 139  ASN F CG  1 
ATOM   6590  O  OD1 . ASN F  1 139 ? 76.832  -13.521 24.693 1.00 27.27  ? 139  ASN F OD1 1 
ATOM   6591  N  ND2 . ASN F  1 139 ? 76.987  -11.959 23.104 1.00 20.96  ? 139  ASN F ND2 1 
ATOM   6592  N  N   . ALA F  1 140 ? 71.461  -13.446 24.370 1.00 18.25  ? 140  ALA F N   1 
ATOM   6593  C  CA  . ALA F  1 140 ? 70.201  -13.049 25.017 1.00 20.86  ? 140  ALA F CA  1 
ATOM   6594  C  C   . ALA F  1 140 ? 69.884  -13.868 26.259 1.00 20.99  ? 140  ALA F C   1 
ATOM   6595  O  O   . ALA F  1 140 ? 68.900  -13.611 26.971 1.00 20.77  ? 140  ALA F O   1 
ATOM   6596  C  CB  . ALA F  1 140 ? 69.056  -13.121 24.001 1.00 20.32  ? 140  ALA F CB  1 
ATOM   6597  N  N   . GLY F  1 141 ? 70.731  -14.839 26.569 1.00 26.62  ? 141  GLY F N   1 
ATOM   6598  C  CA  . GLY F  1 141 ? 70.585  -15.562 27.827 1.00 25.08  ? 141  GLY F CA  1 
ATOM   6599  C  C   . GLY F  1 141 ? 69.418  -16.520 27.819 1.00 25.94  ? 141  GLY F C   1 
ATOM   6600  O  O   . GLY F  1 141 ? 69.021  -17.048 26.782 1.00 23.40  ? 141  GLY F O   1 
ATOM   6601  N  N   . SER F  1 142 ? 68.870  -16.781 29.006 1.00 24.22  ? 142  SER F N   1 
ATOM   6602  C  CA  . SER F  1 142 ? 67.967  -17.929 29.087 1.00 27.00  ? 142  SER F CA  1 
ATOM   6603  C  C   . SER F  1 142 ? 66.608  -17.601 28.498 1.00 19.10  ? 142  SER F C   1 
ATOM   6604  O  O   . SER F  1 142 ? 66.235  -16.468 28.216 1.00 22.81  ? 142  SER F O   1 
ATOM   6605  C  CB  . SER F  1 142 ? 67.875  -18.389 30.554 1.00 28.14  ? 142  SER F CB  1 
ATOM   6606  O  OG  . SER F  1 142 ? 66.957  -17.510 31.183 1.00 30.19  ? 142  SER F OG  1 
ATOM   6607  N  N   . ARG F  1 143 ? 65.841  -18.668 28.276 1.00 20.39  ? 143  ARG F N   1 
ATOM   6608  C  CA  . ARG F  1 143 ? 64.507  -18.603 27.678 1.00 21.72  ? 143  ARG F CA  1 
ATOM   6609  C  C   . ARG F  1 143 ? 63.455  -18.468 28.770 1.00 21.10  ? 143  ARG F C   1 
ATOM   6610  O  O   . ARG F  1 143 ? 63.212  -19.418 29.521 1.00 23.60  ? 143  ARG F O   1 
ATOM   6611  C  CB  . ARG F  1 143 ? 64.323  -19.871 26.830 1.00 19.89  ? 143  ARG F CB  1 
ATOM   6612  C  CG  . ARG F  1 143 ? 65.511  -20.089 25.896 1.00 22.72  ? 143  ARG F CG  1 
ATOM   6613  C  CD  . ARG F  1 143 ? 65.379  -21.341 25.020 1.00 21.27  ? 143  ARG F CD  1 
ATOM   6614  N  NE  . ARG F  1 143 ? 66.591  -21.382 24.166 1.00 21.06  ? 143  ARG F NE  1 
ATOM   6615  C  CZ  . ARG F  1 143 ? 66.769  -22.228 23.169 1.00 23.46  ? 143  ARG F CZ  1 
ATOM   6616  N  NH1 . ARG F  1 143 ? 67.893  -22.195 22.448 1.00 21.40  ? 143  ARG F NH1 1 
ATOM   6617  N  NH2 . ARG F  1 143 ? 65.830  -23.125 22.859 1.00 24.93  ? 143  ARG F NH2 1 
ATOM   6618  N  N   . LEU F  1 144 ? 62.820  -17.311 28.898 1.00 20.07  ? 144  LEU F N   1 
ATOM   6619  C  CA  . LEU F  1 144 ? 61.870  -17.151 30.002 1.00 22.30  ? 144  LEU F CA  1 
ATOM   6620  C  C   . LEU F  1 144 ? 60.499  -17.729 29.682 1.00 22.41  ? 144  LEU F C   1 
ATOM   6621  O  O   . LEU F  1 144 ? 59.802  -18.175 30.586 1.00 23.64  ? 144  LEU F O   1 
ATOM   6622  C  CB  . LEU F  1 144 ? 61.662  -15.670 30.331 1.00 19.11  ? 144  LEU F CB  1 
ATOM   6623  C  CG  . LEU F  1 144 ? 62.958  -14.932 30.711 1.00 26.81  ? 144  LEU F CG  1 
ATOM   6624  C  CD1 . LEU F  1 144 ? 62.613  -13.492 31.062 1.00 24.73  ? 144  LEU F CD1 1 
ATOM   6625  C  CD2 . LEU F  1 144 ? 63.653  -15.687 31.830 1.00 29.79  ? 144  LEU F CD2 1 
ATOM   6626  N  N   . ALA F  1 145 ? 60.110  -17.664 28.420 1.00 18.26  ? 145  ALA F N   1 
ATOM   6627  C  CA  . ALA F  1 145 ? 58.789  -18.192 28.063 1.00 20.21  ? 145  ALA F CA  1 
ATOM   6628  C  C   . ALA F  1 145 ? 58.787  -18.467 26.558 1.00 25.04  ? 145  ALA F C   1 
ATOM   6629  O  O   . ALA F  1 145 ? 59.551  -17.844 25.818 1.00 21.99  ? 145  ALA F O   1 
ATOM   6630  C  CB  . ALA F  1 145 ? 57.674  -17.246 28.458 1.00 20.25  ? 145  ALA F CB  1 
ATOM   6631  N  N   . CYS F  1 146 ? 57.949  -19.402 26.131 1.00 20.47  ? 146  CYS F N   1 
ATOM   6632  C  CA  . CYS F  1 146 ? 57.915  -19.767 24.720 1.00 20.62  ? 146  CYS F CA  1 
ATOM   6633  C  C   . CYS F  1 146 ? 56.561  -20.371 24.389 1.00 23.15  ? 146  CYS F C   1 
ATOM   6634  O  O   . CYS F  1 146 ? 55.762  -20.692 25.298 1.00 20.74  ? 146  CYS F O   1 
ATOM   6635  C  CB  A CYS F  1 146 ? 59.063  -20.723 24.392 0.47 20.56  ? 146  CYS F CB  1 
ATOM   6636  C  CB  B CYS F  1 146 ? 59.093  -20.727 24.501 0.53 20.21  ? 146  CYS F CB  1 
ATOM   6637  S  SG  A CYS F  1 146 ? 59.145  -22.201 25.414 0.47 41.12  ? 146  CYS F SG  1 
ATOM   6638  S  SG  B CYS F  1 146 ? 58.783  -22.384 25.125 0.53 19.40  ? 146  CYS F SG  1 
ATOM   6639  N  N   . GLY F  1 147 ? 56.232  -20.523 23.112 1.00 19.50  ? 147  GLY F N   1 
ATOM   6640  C  CA  . GLY F  1 147 ? 54.960  -21.124 22.697 1.00 17.07  ? 147  GLY F CA  1 
ATOM   6641  C  C   . GLY F  1 147 ? 55.082  -21.580 21.247 1.00 22.94  ? 147  GLY F C   1 
ATOM   6642  O  O   . GLY F  1 147 ? 55.910  -20.989 20.546 1.00 19.54  ? 147  GLY F O   1 
ATOM   6643  N  N   . VAL F  1 148 ? 54.274  -22.577 20.867 1.00 17.29  ? 148  VAL F N   1 
ATOM   6644  C  CA  . VAL F  1 148 ? 54.345  -22.993 19.469 1.00 18.22  ? 148  VAL F CA  1 
ATOM   6645  C  C   . VAL F  1 148 ? 53.476  -22.074 18.640 1.00 22.34  ? 148  VAL F C   1 
ATOM   6646  O  O   . VAL F  1 148 ? 52.372  -21.710 19.054 1.00 25.37  ? 148  VAL F O   1 
ATOM   6647  C  CB  . VAL F  1 148 ? 53.887  -24.458 19.321 1.00 22.90  ? 148  VAL F CB  1 
ATOM   6648  C  CG1 . VAL F  1 148 ? 53.914  -24.841 17.843 1.00 21.05  ? 148  VAL F CG1 1 
ATOM   6649  C  CG2 . VAL F  1 148 ? 54.786  -25.374 20.135 1.00 20.68  ? 148  VAL F CG2 1 
ATOM   6650  N  N   . ILE F  1 149 ? 53.927  -21.627 17.463 1.00 18.37  ? 149  ILE F N   1 
ATOM   6651  C  CA  . ILE F  1 149 ? 53.089  -20.669 16.730 1.00 18.67  ? 149  ILE F CA  1 
ATOM   6652  C  C   . ILE F  1 149 ? 52.004  -21.426 15.956 1.00 22.57  ? 149  ILE F C   1 
ATOM   6653  O  O   . ILE F  1 149 ? 52.347  -22.336 15.182 1.00 20.71  ? 149  ILE F O   1 
ATOM   6654  C  CB  . ILE F  1 149 ? 53.974  -19.830 15.787 1.00 19.54  ? 149  ILE F CB  1 
ATOM   6655  C  CG1 . ILE F  1 149 ? 55.023  -19.001 16.529 1.00 18.57  ? 149  ILE F CG1 1 
ATOM   6656  C  CG2 . ILE F  1 149 ? 53.084  -18.948 14.915 1.00 22.26  ? 149  ILE F CG2 1 
ATOM   6657  C  CD1 . ILE F  1 149 ? 56.248  -18.613 15.722 1.00 22.81  ? 149  ILE F CD1 1 
ATOM   6658  N  N   . GLY F  1 150 ? 50.733  -21.092 16.157 1.00 19.15  ? 150  GLY F N   1 
ATOM   6659  C  CA  . GLY F  1 150 ? 49.677  -21.897 15.540 1.00 18.89  ? 150  GLY F CA  1 
ATOM   6660  C  C   . GLY F  1 150 ? 48.839  -21.073 14.575 1.00 22.67  ? 150  GLY F C   1 
ATOM   6661  O  O   . GLY F  1 150 ? 48.803  -19.852 14.638 1.00 20.32  ? 150  GLY F O   1 
ATOM   6662  N  N   . ILE F  1 151 ? 48.139  -21.761 13.679 1.00 21.23  ? 151  ILE F N   1 
ATOM   6663  C  CA  . ILE F  1 151 ? 47.233  -21.124 12.728 1.00 23.40  ? 151  ILE F CA  1 
ATOM   6664  C  C   . ILE F  1 151 ? 46.039  -20.546 13.460 1.00 24.82  ? 151  ILE F C   1 
ATOM   6665  O  O   . ILE F  1 151 ? 45.491  -21.194 14.350 1.00 23.51  ? 151  ILE F O   1 
ATOM   6666  C  CB  . ILE F  1 151 ? 46.798  -22.130 11.636 1.00 25.37  ? 151  ILE F CB  1 
ATOM   6667  C  CG1 . ILE F  1 151 ? 48.027  -22.647 10.874 1.00 28.73  ? 151  ILE F CG1 1 
ATOM   6668  C  CG2 . ILE F  1 151 ? 45.774  -21.542 10.690 1.00 27.91  ? 151  ILE F CG2 1 
ATOM   6669  C  CD1 . ILE F  1 151 ? 47.765  -23.874 10.026 1.00 39.27  ? 151  ILE F CD1 1 
ATOM   6670  N  N   . ALA F  1 152 ? 45.710  -19.305 13.079 1.00 22.90  ? 152  ALA F N   1 
ATOM   6671  C  CA  . ALA F  1 152 ? 44.636  -18.620 13.768 1.00 24.82  ? 152  ALA F CA  1 
ATOM   6672  C  C   . ALA F  1 152 ? 43.468  -18.334 12.815 1.00 26.47  ? 152  ALA F C   1 
ATOM   6673  O  O   . ALA F  1 152 ? 43.660  -18.267 11.596 1.00 24.65  ? 152  ALA F O   1 
ATOM   6674  C  CB  . ALA F  1 152 ? 45.120  -17.298 14.366 1.00 25.07  ? 152  ALA F CB  1 
ATOM   6675  N  N   . GLN F  1 153 ? 42.293  -18.126 13.404 1.00 25.43  ? 153  GLN F N   1 
ATOM   6676  C  CA  . GLN F  1 153 ? 41.126  -17.837 12.569 1.00 33.47  ? 153  GLN F CA  1 
ATOM   6677  C  C   . GLN F  1 153 ? 41.137  -16.420 11.994 1.00 46.21  ? 153  GLN F C   1 
ATOM   6678  O  O   . GLN F  1 153 ? 41.407  -15.470 12.765 1.00 45.99  ? 153  GLN F O   1 
ATOM   6679  C  CB  . GLN F  1 153 ? 39.824  -18.008 13.352 1.00 30.81  ? 153  GLN F CB  1 
ATOM   6680  C  CG  . GLN F  1 153 ? 38.598  -17.926 12.427 1.00 38.08  ? 153  GLN F CG  1 
ATOM   6681  C  CD  . GLN F  1 153 ? 37.331  -18.073 13.251 1.00 38.64  ? 153  GLN F CD  1 
ATOM   6682  O  OE1 . GLN F  1 153 ? 36.340  -18.627 12.792 1.00 47.62  ? 153  GLN F OE1 1 
ATOM   6683  N  NE2 . GLN F  1 153 ? 37.401  -17.585 14.484 1.00 44.74  ? 153  GLN F NE2 1 
ATOM   6684  O  OXT . GLN F  1 153 ? 40.848  -16.306 10.782 1.00 54.74  ? 153  GLN F OXT 1 
ATOM   6685  N  N   . ALA G  1 1   ? 161.797 4.113   7.376  1.00 94.72  ? 1    ALA G N   1 
ATOM   6686  C  CA  . ALA G  1 1   ? 161.917 3.826   8.801  1.00 66.96  ? 1    ALA G CA  1 
ATOM   6687  C  C   . ALA G  1 1   ? 160.623 4.144   9.534  1.00 53.76  ? 1    ALA G C   1 
ATOM   6688  O  O   . ALA G  1 1   ? 160.579 5.026   10.389 1.00 60.37  ? 1    ALA G O   1 
ATOM   6689  C  CB  . ALA G  1 1   ? 163.069 4.608   9.417  1.00 60.56  ? 1    ALA G CB  1 
ATOM   6690  N  N   . THR G  1 2   ? 159.549 3.429   9.208  1.00 51.59  ? 2    THR G N   1 
ATOM   6691  C  CA  . THR G  1 2   ? 158.333 3.671   9.986  1.00 49.07  ? 2    THR G CA  1 
ATOM   6692  C  C   . THR G  1 2   ? 158.526 3.081   11.385 1.00 51.49  ? 2    THR G C   1 
ATOM   6693  O  O   . THR G  1 2   ? 159.343 2.189   11.622 1.00 40.47  ? 2    THR G O   1 
ATOM   6694  C  CB  . THR G  1 2   ? 157.069 3.071   9.359  1.00 55.90  ? 2    THR G CB  1 
ATOM   6695  O  OG1 . THR G  1 2   ? 156.964 3.459   7.985  1.00 60.07  ? 2    THR G OG1 1 
ATOM   6696  C  CG2 . THR G  1 2   ? 155.806 3.598   10.036 1.00 81.48  ? 2    THR G CG2 1 
ATOM   6697  N  N   . LYS G  1 3   ? 157.747 3.617   12.318 1.00 35.31  ? 3    LYS G N   1 
ATOM   6698  C  CA  . LYS G  1 3   ? 157.685 3.069   13.663 1.00 33.61  ? 3    LYS G CA  1 
ATOM   6699  C  C   . LYS G  1 3   ? 156.200 2.996   14.033 1.00 34.02  ? 3    LYS G C   1 
ATOM   6700  O  O   . LYS G  1 3   ? 155.420 3.865   13.654 1.00 30.71  ? 3    LYS G O   1 
ATOM   6701  C  CB  . LYS G  1 3   ? 158.481 3.879   14.663 1.00 36.23  ? 3    LYS G CB  1 
ATOM   6702  C  CG  . LYS G  1 3   ? 159.973 3.561   14.677 1.00 47.56  ? 3    LYS G CG  1 
ATOM   6703  C  CD  . LYS G  1 3   ? 160.567 3.771   16.062 1.00 52.04  ? 3    LYS G CD  1 
ATOM   6704  C  CE  . LYS G  1 3   ? 161.920 4.463   15.960 1.00 65.47  ? 3    LYS G CE  1 
ATOM   6705  N  NZ  . LYS G  1 3   ? 162.383 4.994   17.273 1.00 74.72  ? 3    LYS G NZ  1 
ATOM   6706  N  N   . ALA G  1 4   ? 155.842 1.931   14.734 1.00 30.43  ? 4    ALA G N   1 
ATOM   6707  C  CA  . ALA G  1 4   ? 154.465 1.845   15.226 1.00 26.02  ? 4    ALA G CA  1 
ATOM   6708  C  C   . ALA G  1 4   ? 154.540 1.341   16.670 1.00 31.45  ? 4    ALA G C   1 
ATOM   6709  O  O   . ALA G  1 4   ? 155.603 0.939   17.130 1.00 32.38  ? 4    ALA G O   1 
ATOM   6710  C  CB  . ALA G  1 4   ? 153.578 0.995   14.354 1.00 29.67  ? 4    ALA G CB  1 
ATOM   6711  N  N   . VAL G  1 5   ? 153.402 1.414   17.338 1.00 35.81  ? 5    VAL G N   1 
ATOM   6712  C  CA  . VAL G  1 5   ? 153.357 1.023   18.750 1.00 33.53  ? 5    VAL G CA  1 
ATOM   6713  C  C   . VAL G  1 5   ? 151.934 0.581   19.045 1.00 31.99  ? 5    VAL G C   1 
ATOM   6714  O  O   . VAL G  1 5   ? 150.983 0.969   18.365 1.00 26.42  ? 5    VAL G O   1 
ATOM   6715  C  CB  . VAL G  1 5   ? 153.802 2.136   19.704 1.00 29.96  ? 5    VAL G CB  1 
ATOM   6716  C  CG1 . VAL G  1 5   ? 152.797 3.292   19.655 1.00 25.78  ? 5    VAL G CG1 1 
ATOM   6717  C  CG2 . VAL G  1 5   ? 153.944 1.582   21.112 1.00 32.11  ? 5    VAL G CG2 1 
ATOM   6718  N  N   . CYS G  1 6   ? 151.823 -0.284  20.055 1.00 29.36  ? 6    CYS G N   1 
ATOM   6719  C  CA  . CYS G  1 6   ? 150.524 -0.816  20.436 1.00 27.84  ? 6    CYS G CA  1 
ATOM   6720  C  C   . CYS G  1 6   ? 150.483 -1.028  21.947 1.00 35.33  ? 6    CYS G C   1 
ATOM   6721  O  O   . CYS G  1 6   ? 151.428 -1.644  22.469 1.00 32.59  ? 6    CYS G O   1 
ATOM   6722  C  CB  . CYS G  1 6   ? 150.269 -2.122  19.685 1.00 34.02  ? 6    CYS G CB  1 
ATOM   6723  S  SG  . CYS G  1 6   ? 148.677 -2.893  20.037 1.00 32.56  ? 6    CYS G SG  1 
ATOM   6724  N  N   . VAL G  1 7   ? 149.433 -0.521  22.573 1.00 31.27  ? 7    VAL G N   1 
ATOM   6725  C  CA  . VAL G  1 7   ? 149.181 -0.731  24.000 1.00 25.25  ? 7    VAL G CA  1 
ATOM   6726  C  C   . VAL G  1 7   ? 148.096 -1.784  24.121 1.00 31.38  ? 7    VAL G C   1 
ATOM   6727  O  O   . VAL G  1 7   ? 146.973 -1.596  23.642 1.00 29.43  ? 7    VAL G O   1 
ATOM   6728  C  CB  . VAL G  1 7   ? 148.763 0.555   24.735 1.00 27.84  ? 7    VAL G CB  1 
ATOM   6729  C  CG1 . VAL G  1 7   ? 148.411 0.225   26.179 1.00 32.97  ? 7    VAL G CG1 1 
ATOM   6730  C  CG2 . VAL G  1 7   ? 149.852 1.608   24.696 1.00 28.33  ? 7    VAL G CG2 1 
ATOM   6731  N  N   . LEU G  1 8   ? 148.423 -2.947  24.714 1.00 27.67  ? 8    LEU G N   1 
ATOM   6732  C  CA  . LEU G  1 8   ? 147.441 -4.012  24.781 1.00 25.20  ? 8    LEU G CA  1 
ATOM   6733  C  C   . LEU G  1 8   ? 146.739 -3.923  26.145 1.00 26.89  ? 8    LEU G C   1 
ATOM   6734  O  O   . LEU G  1 8   ? 147.454 -3.717  27.135 1.00 30.08  ? 8    LEU G O   1 
ATOM   6735  C  CB  . LEU G  1 8   ? 148.049 -5.410  24.678 1.00 33.91  ? 8    LEU G CB  1 
ATOM   6736  C  CG  . LEU G  1 8   ? 148.696 -5.853  23.369 1.00 35.53  ? 8    LEU G CG  1 
ATOM   6737  C  CD1 . LEU G  1 8   ? 149.551 -7.103  23.579 1.00 46.43  ? 8    LEU G CD1 1 
ATOM   6738  C  CD2 . LEU G  1 8   ? 147.649 -6.155  22.311 1.00 41.96  ? 8    LEU G CD2 1 
ATOM   6739  N  N   . LYS G  1 9   ? 145.441 -4.084  26.129 1.00 30.14  ? 9    LYS G N   1 
ATOM   6740  C  CA  . LYS G  1 9   ? 144.563 -4.059  27.294 1.00 37.08  ? 9    LYS G CA  1 
ATOM   6741  C  C   . LYS G  1 9   ? 143.387 -4.994  27.114 1.00 29.41  ? 9    LYS G C   1 
ATOM   6742  O  O   . LYS G  1 9   ? 142.925 -5.294  26.006 1.00 30.34  ? 9    LYS G O   1 
ATOM   6743  C  CB  . LYS G  1 9   ? 144.053 -2.634  27.569 1.00 44.36  ? 9    LYS G CB  1 
ATOM   6744  C  CG  . LYS G  1 9   ? 145.156 -1.661  27.934 1.00 51.56  ? 9    LYS G CG  1 
ATOM   6745  C  CD  . LYS G  1 9   ? 144.694 -0.236  28.152 1.00 61.96  ? 9    LYS G CD  1 
ATOM   6746  C  CE  . LYS G  1 9   ? 145.688 0.493   29.059 1.00 63.08  ? 9    LYS G CE  1 
ATOM   6747  N  NZ  . LYS G  1 9   ? 146.290 1.668   28.375 1.00 60.45  ? 9    LYS G NZ  1 
ATOM   6748  N  N   . GLY G  1 10  ? 142.856 -5.501  28.237 1.00 27.22  ? 10   GLY G N   1 
ATOM   6749  C  CA  . GLY G  1 10  ? 141.722 -6.391  28.153 1.00 30.05  ? 10   GLY G CA  1 
ATOM   6750  C  C   . GLY G  1 10  ? 140.814 -6.303  29.390 1.00 30.40  ? 10   GLY G C   1 
ATOM   6751  O  O   . GLY G  1 10  ? 140.996 -5.389  30.191 1.00 32.44  ? 10   GLY G O   1 
ATOM   6752  N  N   . ASP G  1 11  ? 139.900 -7.244  29.481 1.00 36.22  ? 11   ASP G N   1 
ATOM   6753  C  CA  . ASP G  1 11  ? 138.953 -7.432  30.566 1.00 51.95  ? 11   ASP G CA  1 
ATOM   6754  C  C   . ASP G  1 11  ? 139.618 -8.097  31.772 1.00 61.00  ? 11   ASP G C   1 
ATOM   6755  O  O   . ASP G  1 11  ? 139.035 -8.156  32.855 1.00 53.76  ? 11   ASP G O   1 
ATOM   6756  C  CB  . ASP G  1 11  ? 137.767 -8.294  30.122 1.00 54.36  ? 11   ASP G CB  1 
ATOM   6757  C  CG  . ASP G  1 11  ? 136.978 -7.705  28.969 1.00 61.60  ? 11   ASP G CG  1 
ATOM   6758  O  OD1 . ASP G  1 11  ? 136.902 -6.459  28.874 1.00 76.39  ? 11   ASP G OD1 1 
ATOM   6759  O  OD2 . ASP G  1 11  ? 136.432 -8.485  28.155 1.00 61.72  ? 11   ASP G OD2 1 
ATOM   6760  N  N   . GLY G  1 12  ? 140.833 -8.599  31.578 1.00 59.75  ? 12   GLY G N   1 
ATOM   6761  C  CA  . GLY G  1 12  ? 141.615 -9.228  32.627 1.00 52.65  ? 12   GLY G CA  1 
ATOM   6762  C  C   . GLY G  1 12  ? 142.826 -8.398  33.006 1.00 43.61  ? 12   GLY G C   1 
ATOM   6763  O  O   . GLY G  1 12  ? 142.842 -7.180  32.797 1.00 36.46  ? 12   GLY G O   1 
ATOM   6764  N  N   . PRO G  1 13  ? 143.851 -9.017  33.598 1.00 33.91  ? 13   PRO G N   1 
ATOM   6765  C  CA  . PRO G  1 13  ? 145.072 -8.308  33.945 1.00 32.62  ? 13   PRO G CA  1 
ATOM   6766  C  C   . PRO G  1 13  ? 146.111 -8.225  32.832 1.00 28.35  ? 13   PRO G C   1 
ATOM   6767  O  O   . PRO G  1 13  ? 147.187 -7.651  33.013 1.00 30.96  ? 13   PRO G O   1 
ATOM   6768  C  CB  . PRO G  1 13  ? 145.665 -9.218  35.046 1.00 36.04  ? 13   PRO G CB  1 
ATOM   6769  C  CG  . PRO G  1 13  ? 145.225 -10.584 34.656 1.00 28.74  ? 13   PRO G CG  1 
ATOM   6770  C  CD  . PRO G  1 13  ? 143.868 -10.428 34.030 1.00 32.68  ? 13   PRO G CD  1 
ATOM   6771  N  N   . VAL G  1 14  ? 145.789 -8.805  31.675 1.00 33.38  ? 14   VAL G N   1 
ATOM   6772  C  CA  . VAL G  1 14  ? 146.873 -8.794  30.670 1.00 29.02  ? 14   VAL G CA  1 
ATOM   6773  C  C   . VAL G  1 14  ? 147.084 -7.416  30.063 1.00 29.02  ? 14   VAL G C   1 
ATOM   6774  O  O   . VAL G  1 14  ? 146.132 -6.879  29.498 1.00 33.46  ? 14   VAL G O   1 
ATOM   6775  C  CB  . VAL G  1 14  ? 146.545 -9.820  29.585 1.00 29.95  ? 14   VAL G CB  1 
ATOM   6776  C  CG1 . VAL G  1 14  ? 147.644 -9.816  28.535 1.00 31.97  ? 14   VAL G CG1 1 
ATOM   6777  C  CG2 . VAL G  1 14  ? 146.380 -11.207 30.200 1.00 28.53  ? 14   VAL G CG2 1 
ATOM   6778  N  N   . GLN G  1 15  ? 148.270 -6.868  30.190 1.00 28.88  ? 15   GLN G N   1 
ATOM   6779  C  CA  . GLN G  1 15  ? 148.681 -5.590  29.653 1.00 36.83  ? 15   GLN G CA  1 
ATOM   6780  C  C   . GLN G  1 15  ? 150.122 -5.631  29.147 1.00 35.99  ? 15   GLN G C   1 
ATOM   6781  O  O   . GLN G  1 15  ? 150.908 -6.498  29.511 1.00 32.01  ? 15   GLN G O   1 
ATOM   6782  C  CB  . GLN G  1 15  ? 148.588 -4.475  30.698 1.00 39.50  ? 15   GLN G CB  1 
ATOM   6783  C  CG  . GLN G  1 15  ? 148.724 -4.943  32.133 1.00 46.83  ? 15   GLN G CG  1 
ATOM   6784  C  CD  . GLN G  1 15  ? 148.246 -3.854  33.085 1.00 47.18  ? 15   GLN G CD  1 
ATOM   6785  O  OE1 . GLN G  1 15  ? 148.899 -2.817  33.191 1.00 52.18  ? 15   GLN G OE1 1 
ATOM   6786  N  NE2 . GLN G  1 15  ? 147.126 -4.101  33.746 1.00 50.64  ? 15   GLN G NE2 1 
ATOM   6787  N  N   . GLY G  1 16  ? 150.458 -4.664  28.300 1.00 30.79  ? 16   GLY G N   1 
ATOM   6788  C  CA  . GLY G  1 16  ? 151.806 -4.561  27.778 1.00 32.75  ? 16   GLY G CA  1 
ATOM   6789  C  C   . GLY G  1 16  ? 151.906 -3.544  26.658 1.00 35.43  ? 16   GLY G C   1 
ATOM   6790  O  O   . GLY G  1 16  ? 150.912 -2.985  26.204 1.00 30.82  ? 16   GLY G O   1 
ATOM   6791  N  N   . ILE G  1 17  ? 153.128 -3.309  26.220 1.00 35.53  ? 17   ILE G N   1 
ATOM   6792  C  CA  . ILE G  1 17  ? 153.413 -2.407  25.121 1.00 31.41  ? 17   ILE G CA  1 
ATOM   6793  C  C   . ILE G  1 17  ? 154.253 -3.110  24.065 1.00 35.98  ? 17   ILE G C   1 
ATOM   6794  O  O   . ILE G  1 17  ? 155.309 -3.614  24.448 1.00 36.63  ? 17   ILE G O   1 
ATOM   6795  C  CB  . ILE G  1 17  ? 154.163 -1.173  25.640 1.00 35.31  ? 17   ILE G CB  1 
ATOM   6796  C  CG1 . ILE G  1 17  ? 153.246 -0.328  26.544 1.00 42.04  ? 17   ILE G CG1 1 
ATOM   6797  C  CG2 . ILE G  1 17  ? 154.783 -0.331  24.537 1.00 33.16  ? 17   ILE G CG2 1 
ATOM   6798  C  CD1 . ILE G  1 17  ? 153.985 0.673   27.401 1.00 49.08  ? 17   ILE G CD1 1 
ATOM   6799  N  N   . ILE G  1 18  ? 153.775 -3.110  22.821 1.00 27.21  ? 18   ILE G N   1 
ATOM   6800  C  CA  . ILE G  1 18  ? 154.546 -3.712  21.741 1.00 27.74  ? 18   ILE G CA  1 
ATOM   6801  C  C   . ILE G  1 18  ? 154.962 -2.653  20.715 1.00 35.73  ? 18   ILE G C   1 
ATOM   6802  O  O   . ILE G  1 18  ? 154.084 -1.925  20.261 1.00 35.91  ? 18   ILE G O   1 
ATOM   6803  C  CB  . ILE G  1 18  ? 153.751 -4.775  20.984 1.00 29.64  ? 18   ILE G CB  1 
ATOM   6804  C  CG1 . ILE G  1 18  ? 153.293 -5.960  21.853 1.00 32.52  ? 18   ILE G CG1 1 
ATOM   6805  C  CG2 . ILE G  1 18  ? 154.545 -5.270  19.780 1.00 26.75  ? 18   ILE G CG2 1 
ATOM   6806  C  CD1 . ILE G  1 18  ? 154.463 -6.731  22.430 1.00 30.88  ? 18   ILE G CD1 1 
ATOM   6807  N  N   . ASN G  1 19  ? 156.222 -2.611  20.373 1.00 31.99  ? 19   ASN G N   1 
ATOM   6808  C  CA  . ASN G  1 19  ? 156.850 -1.737  19.402 1.00 34.13  ? 19   ASN G CA  1 
ATOM   6809  C  C   . ASN G  1 19  ? 157.136 -2.449  18.083 1.00 35.06  ? 19   ASN G C   1 
ATOM   6810  O  O   . ASN G  1 19  ? 157.435 -3.637  18.018 1.00 32.07  ? 19   ASN G O   1 
ATOM   6811  C  CB  . ASN G  1 19  ? 158.161 -1.189  19.957 1.00 29.56  ? 19   ASN G CB  1 
ATOM   6812  C  CG  . ASN G  1 19  ? 157.966 -0.455  21.265 1.00 45.02  ? 19   ASN G CG  1 
ATOM   6813  O  OD1 . ASN G  1 19  ? 157.481 0.675   21.263 1.00 38.75  ? 19   ASN G OD1 1 
ATOM   6814  N  ND2 . ASN G  1 19  ? 158.341 -1.090  22.369 1.00 44.50  ? 19   ASN G ND2 1 
ATOM   6815  N  N   . PHE G  1 20  ? 157.029 -1.673  17.016 1.00 33.21  ? 20   PHE G N   1 
ATOM   6816  C  CA  . PHE G  1 20  ? 157.244 -2.124  15.656 1.00 31.47  ? 20   PHE G CA  1 
ATOM   6817  C  C   . PHE G  1 20  ? 158.260 -1.185  14.998 1.00 38.77  ? 20   PHE G C   1 
ATOM   6818  O  O   . PHE G  1 20  ? 158.228 0.032   15.178 1.00 31.55  ? 20   PHE G O   1 
ATOM   6819  C  CB  . PHE G  1 20  ? 155.976 -2.147  14.825 1.00 27.48  ? 20   PHE G CB  1 
ATOM   6820  C  CG  . PHE G  1 20  ? 154.865 -3.032  15.364 1.00 36.96  ? 20   PHE G CG  1 
ATOM   6821  C  CD1 . PHE G  1 20  ? 154.627 -4.289  14.847 1.00 40.15  ? 20   PHE G CD1 1 
ATOM   6822  C  CD2 . PHE G  1 20  ? 154.054 -2.586  16.397 1.00 38.27  ? 20   PHE G CD2 1 
ATOM   6823  C  CE1 . PHE G  1 20  ? 153.612 -5.097  15.341 1.00 35.95  ? 20   PHE G CE1 1 
ATOM   6824  C  CE2 . PHE G  1 20  ? 153.031 -3.376  16.889 1.00 32.17  ? 20   PHE G CE2 1 
ATOM   6825  C  CZ  . PHE G  1 20  ? 152.798 -4.634  16.355 1.00 33.50  ? 20   PHE G CZ  1 
ATOM   6826  N  N   . GLU G  1 21  ? 159.162 -1.808  14.243 1.00 39.55  ? 21   GLU G N   1 
ATOM   6827  C  CA  . GLU G  1 21  ? 160.127 -0.980  13.523 1.00 50.35  ? 21   GLU G CA  1 
ATOM   6828  C  C   . GLU G  1 21  ? 160.478 -1.626  12.185 1.00 52.93  ? 21   GLU G C   1 
ATOM   6829  O  O   . GLU G  1 21  ? 160.869 -2.789  12.185 1.00 35.68  ? 21   GLU G O   1 
ATOM   6830  C  CB  . GLU G  1 21  ? 161.378 -0.748  14.365 1.00 51.07  ? 21   GLU G CB  1 
ATOM   6831  C  CG  . GLU G  1 21  ? 161.671 0.735   14.557 1.00 61.46  ? 21   GLU G CG  1 
ATOM   6832  C  CD  . GLU G  1 21  ? 163.147 1.039   14.383 1.00 61.84  ? 21   GLU G CD  1 
ATOM   6833  O  OE1 . GLU G  1 21  ? 163.548 1.452   13.276 1.00 84.89  ? 21   GLU G OE1 1 
ATOM   6834  O  OE2 . GLU G  1 21  ? 163.886 0.848   15.371 1.00 60.83  ? 21   GLU G OE2 1 
ATOM   6835  N  N   . GLN G  1 22  ? 160.315 -0.842  11.137 1.00 53.31  ? 22   GLN G N   1 
ATOM   6836  C  CA  . GLN G  1 22  ? 160.629 -1.136  9.753  1.00 45.19  ? 22   GLN G CA  1 
ATOM   6837  C  C   . GLN G  1 22  ? 161.621 -0.085  9.227  1.00 54.39  ? 22   GLN G C   1 
ATOM   6838  O  O   . GLN G  1 22  ? 161.156 0.997   8.864  1.00 41.87  ? 22   GLN G O   1 
ATOM   6839  C  CB  . GLN G  1 22  ? 159.376 -1.138  8.887  1.00 36.49  ? 22   GLN G CB  1 
ATOM   6840  C  CG  . GLN G  1 22  ? 159.473 -2.015  7.652  1.00 36.00  ? 22   GLN G CG  1 
ATOM   6841  C  CD  . GLN G  1 22  ? 158.162 -2.058  6.899  1.00 33.48  ? 22   GLN G CD  1 
ATOM   6842  O  OE1 . GLN G  1 22  ? 157.345 -1.147  7.053  1.00 44.59  ? 22   GLN G OE1 1 
ATOM   6843  N  NE2 . GLN G  1 22  ? 157.961 -3.096  6.094  1.00 34.93  ? 22   GLN G NE2 1 
ATOM   6844  N  N   . LYS G  1 23  ? 162.898 -0.424  9.226  1.00 57.19  ? 23   LYS G N   1 
ATOM   6845  C  CA  . LYS G  1 23  ? 164.019 0.426   8.855  1.00 69.29  ? 23   LYS G CA  1 
ATOM   6846  C  C   . LYS G  1 23  ? 164.033 0.780   7.367  1.00 62.06  ? 23   LYS G C   1 
ATOM   6847  O  O   . LYS G  1 23  ? 164.368 1.904   6.980  1.00 53.77  ? 23   LYS G O   1 
ATOM   6848  C  CB  . LYS G  1 23  ? 165.334 -0.266  9.233  1.00 80.21  ? 23   LYS G CB  1 
ATOM   6849  C  CG  . LYS G  1 23  ? 165.278 -0.941  10.599 1.00 95.27  ? 23   LYS G CG  1 
ATOM   6850  C  CD  . LYS G  1 23  ? 166.654 -1.024  11.246 1.00 103.80 ? 23   LYS G CD  1 
ATOM   6851  C  CE  . LYS G  1 23  ? 166.823 0.033   12.331 1.00 106.10 ? 23   LYS G CE  1 
ATOM   6852  N  NZ  . LYS G  1 23  ? 167.724 -0.412  13.427 1.00 102.09 ? 23   LYS G NZ  1 
ATOM   6853  N  N   . GLU G  1 24  ? 163.658 -0.196  6.556  1.00 54.67  ? 24   GLU G N   1 
ATOM   6854  C  CA  . GLU G  1 24  ? 163.555 -0.096  5.116  1.00 59.55  ? 24   GLU G CA  1 
ATOM   6855  C  C   . GLU G  1 24  ? 162.133 -0.385  4.615  1.00 57.84  ? 24   GLU G C   1 
ATOM   6856  O  O   . GLU G  1 24  ? 161.478 -1.323  5.058  1.00 62.49  ? 24   GLU G O   1 
ATOM   6857  C  CB  . GLU G  1 24  ? 164.504 -1.071  4.416  1.00 59.54  ? 24   GLU G CB  1 
ATOM   6858  C  CG  . GLU G  1 24  ? 165.878 -0.541  4.071  1.00 74.65  ? 24   GLU G CG  1 
ATOM   6859  C  CD  . GLU G  1 24  ? 166.784 -1.639  3.538  1.00 94.18  ? 24   GLU G CD  1 
ATOM   6860  O  OE1 . GLU G  1 24  ? 166.263 -2.598  2.928  1.00 111.67 ? 24   GLU G OE1 1 
ATOM   6861  O  OE2 . GLU G  1 24  ? 168.015 -1.544  3.737  1.00 122.51 ? 24   GLU G OE2 1 
ATOM   6862  N  N   . SER G  1 25  ? 161.728 0.439   3.676  1.00 57.68  ? 25   SER G N   1 
ATOM   6863  C  CA  . SER G  1 25  ? 160.513 0.491   2.901  1.00 62.32  ? 25   SER G CA  1 
ATOM   6864  C  C   . SER G  1 25  ? 159.685 -0.776  2.982  1.00 67.70  ? 25   SER G C   1 
ATOM   6865  O  O   . SER G  1 25  ? 158.555 -0.757  3.489  1.00 88.87  ? 25   SER G O   1 
ATOM   6866  C  CB  . SER G  1 25  ? 160.889 0.795   1.444  1.00 72.07  ? 25   SER G CB  1 
ATOM   6867  O  OG  . SER G  1 25  ? 162.304 0.886   1.312  1.00 105.80 ? 25   SER G OG  1 
ATOM   6868  N  N   . ASN G  1 26  ? 160.214 -1.901  2.496  1.00 67.12  ? 26   ASN G N   1 
ATOM   6869  C  CA  . ASN G  1 26  ? 159.411 -3.125  2.642  1.00 63.53  ? 26   ASN G CA  1 
ATOM   6870  C  C   . ASN G  1 26  ? 160.290 -4.277  3.112  1.00 47.54  ? 26   ASN G C   1 
ATOM   6871  O  O   . ASN G  1 26  ? 160.165 -5.439  2.733  1.00 52.50  ? 26   ASN G O   1 
ATOM   6872  C  CB  . ASN G  1 26  ? 158.680 -3.458  1.346  1.00 71.87  ? 26   ASN G CB  1 
ATOM   6873  C  CG  . ASN G  1 26  ? 157.182 -3.555  1.595  1.00 84.21  ? 26   ASN G CG  1 
ATOM   6874  O  OD1 . ASN G  1 26  ? 156.576 -2.646  2.162  1.00 81.80  ? 26   ASN G OD1 1 
ATOM   6875  N  ND2 . ASN G  1 26  ? 156.600 -4.672  1.173  1.00 106.99 ? 26   ASN G ND2 1 
ATOM   6876  N  N   . GLY G  1 27  ? 161.217 -3.887  3.991  1.00 43.43  ? 27   GLY G N   1 
ATOM   6877  C  CA  . GLY G  1 27  ? 162.051 -4.865  4.661  1.00 47.84  ? 27   GLY G CA  1 
ATOM   6878  C  C   . GLY G  1 27  ? 161.299 -5.508  5.817  1.00 44.96  ? 27   GLY G C   1 
ATOM   6879  O  O   . GLY G  1 27  ? 160.104 -5.318  6.031  1.00 45.05  ? 27   GLY G O   1 
ATOM   6880  N  N   . PRO G  1 28  ? 162.027 -6.290  6.600  1.00 58.69  ? 28   PRO G N   1 
ATOM   6881  C  CA  . PRO G  1 28  ? 161.440 -6.934  7.769  1.00 51.37  ? 28   PRO G CA  1 
ATOM   6882  C  C   . PRO G  1 28  ? 160.970 -5.902  8.786  1.00 48.80  ? 28   PRO G C   1 
ATOM   6883  O  O   . PRO G  1 28  ? 161.490 -4.793  8.893  1.00 39.73  ? 28   PRO G O   1 
ATOM   6884  C  CB  . PRO G  1 28  ? 162.601 -7.704  8.398  1.00 61.98  ? 28   PRO G CB  1 
ATOM   6885  C  CG  . PRO G  1 28  ? 163.679 -7.749  7.375  1.00 65.29  ? 28   PRO G CG  1 
ATOM   6886  C  CD  . PRO G  1 28  ? 163.453 -6.607  6.427  1.00 59.90  ? 28   PRO G CD  1 
ATOM   6887  N  N   . VAL G  1 29  ? 159.967 -6.328  9.544  1.00 40.97  ? 29   VAL G N   1 
ATOM   6888  C  CA  . VAL G  1 29  ? 159.518 -5.536  10.688 1.00 36.26  ? 29   VAL G CA  1 
ATOM   6889  C  C   . VAL G  1 29  ? 160.026 -6.162  11.980 1.00 39.96  ? 29   VAL G C   1 
ATOM   6890  O  O   . VAL G  1 29  ? 159.840 -7.363  12.239 1.00 41.16  ? 29   VAL G O   1 
ATOM   6891  C  CB  . VAL G  1 29  ? 157.983 -5.444  10.717 1.00 41.57  ? 29   VAL G CB  1 
ATOM   6892  C  CG1 . VAL G  1 29  ? 157.526 -4.466  11.789 1.00 40.28  ? 29   VAL G CG1 1 
ATOM   6893  C  CG2 . VAL G  1 29  ? 157.434 -5.051  9.351  1.00 42.95  ? 29   VAL G CG2 1 
ATOM   6894  N  N   . LYS G  1 30  ? 160.683 -5.349  12.799 1.00 41.06  ? 30   LYS G N   1 
ATOM   6895  C  CA  . LYS G  1 30  ? 161.045 -5.797  14.140 1.00 42.70  ? 30   LYS G CA  1 
ATOM   6896  C  C   . LYS G  1 30  ? 159.840 -5.541  15.056 1.00 50.47  ? 30   LYS G C   1 
ATOM   6897  O  O   . LYS G  1 30  ? 159.348 -4.409  15.055 1.00 37.51  ? 30   LYS G O   1 
ATOM   6898  C  CB  . LYS G  1 30  ? 162.274 -5.086  14.694 1.00 38.60  ? 30   LYS G CB  1 
ATOM   6899  C  CG  . LYS G  1 30  ? 163.588 -5.535  14.082 1.00 54.27  ? 30   LYS G CG  1 
ATOM   6900  C  CD  . LYS G  1 30  ? 164.721 -4.563  14.365 1.00 64.27  ? 30   LYS G CD  1 
ATOM   6901  C  CE  . LYS G  1 30  ? 166.047 -5.142  13.878 1.00 66.87  ? 30   LYS G CE  1 
ATOM   6902  N  NZ  . LYS G  1 30  ? 167.210 -4.328  14.341 1.00 60.24  ? 30   LYS G NZ  1 
ATOM   6903  N  N   . VAL G  1 31  ? 159.431 -6.571  15.779 1.00 47.83  ? 31   VAL G N   1 
ATOM   6904  C  CA  . VAL G  1 31  ? 158.357 -6.490  16.774 1.00 33.99  ? 31   VAL G CA  1 
ATOM   6905  C  C   . VAL G  1 31  ? 158.930 -6.797  18.148 1.00 41.25  ? 31   VAL G C   1 
ATOM   6906  O  O   . VAL G  1 31  ? 159.443 -7.902  18.378 1.00 41.57  ? 31   VAL G O   1 
ATOM   6907  C  CB  . VAL G  1 31  ? 157.237 -7.457  16.409 1.00 32.86  ? 31   VAL G CB  1 
ATOM   6908  C  CG1 . VAL G  1 31  ? 156.033 -7.262  17.320 1.00 37.33  ? 31   VAL G CG1 1 
ATOM   6909  C  CG2 . VAL G  1 31  ? 156.814 -7.268  14.962 1.00 30.96  ? 31   VAL G CG2 1 
ATOM   6910  N  N   . TRP G  1 32  ? 158.883 -5.838  19.073 1.00 33.18  ? 32   TRP G N   1 
ATOM   6911  C  CA  . TRP G  1 32  ? 159.412 -6.089  20.408 1.00 33.84  ? 32   TRP G CA  1 
ATOM   6912  C  C   . TRP G  1 32  ? 158.714 -5.296  21.518 1.00 39.77  ? 32   TRP G C   1 
ATOM   6913  O  O   . TRP G  1 32  ? 158.235 -4.179  21.312 1.00 41.45  ? 32   TRP G O   1 
ATOM   6914  C  CB  . TRP G  1 32  ? 160.901 -5.761  20.507 1.00 33.73  ? 32   TRP G CB  1 
ATOM   6915  C  CG  . TRP G  1 32  ? 161.196 -4.300  20.659 1.00 40.94  ? 32   TRP G CG  1 
ATOM   6916  C  CD1 . TRP G  1 32  ? 161.511 -3.576  21.768 1.00 34.10  ? 32   TRP G CD1 1 
ATOM   6917  C  CD2 . TRP G  1 32  ? 161.187 -3.373  19.556 1.00 40.49  ? 32   TRP G CD2 1 
ATOM   6918  N  NE1 . TRP G  1 32  ? 161.700 -2.256  21.426 1.00 43.32  ? 32   TRP G NE1 1 
ATOM   6919  C  CE2 . TRP G  1 32  ? 161.505 -2.115  20.078 1.00 42.67  ? 32   TRP G CE2 1 
ATOM   6920  C  CE3 . TRP G  1 32  ? 160.933 -3.536  18.192 1.00 46.17  ? 32   TRP G CE3 1 
ATOM   6921  C  CZ2 . TRP G  1 32  ? 161.580 -0.986  19.258 1.00 49.59  ? 32   TRP G CZ2 1 
ATOM   6922  C  CZ3 . TRP G  1 32  ? 161.008 -2.415  17.383 1.00 49.42  ? 32   TRP G CZ3 1 
ATOM   6923  C  CH2 . TRP G  1 32  ? 161.328 -1.166  17.926 1.00 46.85  ? 32   TRP G CH2 1 
ATOM   6924  N  N   . GLY G  1 33  ? 158.721 -5.889  22.713 1.00 31.50  ? 33   GLY G N   1 
ATOM   6925  C  CA  . GLY G  1 33  ? 158.222 -5.234  23.918 1.00 39.28  ? 33   GLY G CA  1 
ATOM   6926  C  C   . GLY G  1 33  ? 157.970 -6.199  25.059 1.00 43.08  ? 33   GLY G C   1 
ATOM   6927  O  O   . GLY G  1 33  ? 158.695 -7.180  25.250 1.00 34.55  ? 33   GLY G O   1 
ATOM   6928  N  N   . SER G  1 34  ? 156.939 -5.972  25.866 1.00 38.42  ? 34   SER G N   1 
ATOM   6929  C  CA  . SER G  1 34  ? 156.617 -6.910  26.938 1.00 35.55  ? 34   SER G CA  1 
ATOM   6930  C  C   . SER G  1 34  ? 155.107 -6.948  27.176 1.00 37.40  ? 34   SER G C   1 
ATOM   6931  O  O   . SER G  1 34  ? 154.498 -5.910  26.918 1.00 34.17  ? 34   SER G O   1 
ATOM   6932  C  CB  . SER G  1 34  ? 157.310 -6.488  28.233 1.00 37.01  ? 34   SER G CB  1 
ATOM   6933  O  OG  . SER G  1 34  ? 157.900 -5.206  28.014 1.00 70.36  ? 34   SER G OG  1 
ATOM   6934  N  N   . ILE G  1 35  ? 154.623 -8.088  27.628 1.00 28.50  ? 35   ILE G N   1 
ATOM   6935  C  CA  . ILE G  1 35  ? 153.254 -8.359  28.038 1.00 27.33  ? 35   ILE G CA  1 
ATOM   6936  C  C   . ILE G  1 35  ? 153.291 -8.985  29.429 1.00 37.77  ? 35   ILE G C   1 
ATOM   6937  O  O   . ILE G  1 35  ? 154.020 -9.944  29.691 1.00 36.47  ? 35   ILE G O   1 
ATOM   6938  C  CB  . ILE G  1 35  ? 152.528 -9.259  27.036 1.00 29.58  ? 35   ILE G CB  1 
ATOM   6939  C  CG1 . ILE G  1 35  ? 152.570 -8.726  25.585 1.00 26.63  ? 35   ILE G CG1 1 
ATOM   6940  C  CG2 . ILE G  1 35  ? 151.087 -9.559  27.413 1.00 28.86  ? 35   ILE G CG2 1 
ATOM   6941  C  CD1 . ILE G  1 35  ? 152.074 -9.730  24.583 1.00 24.87  ? 35   ILE G CD1 1 
ATOM   6942  N  N   . LYS G  1 36  ? 152.516 -8.453  30.365 1.00 28.70  ? 36   LYS G N   1 
ATOM   6943  C  CA  . LYS G  1 36  ? 152.509 -9.069  31.692 1.00 30.74  ? 36   LYS G CA  1 
ATOM   6944  C  C   . LYS G  1 36  ? 151.111 -9.570  32.008 1.00 40.90  ? 36   LYS G C   1 
ATOM   6945  O  O   . LYS G  1 36  ? 150.169 -9.332  31.254 1.00 32.23  ? 36   LYS G O   1 
ATOM   6946  C  CB  . LYS G  1 36  ? 153.007 -8.106  32.760 1.00 35.26  ? 36   LYS G CB  1 
ATOM   6947  C  CG  . LYS G  1 36  ? 152.109 -6.910  33.077 1.00 37.06  ? 36   LYS G CG  1 
ATOM   6948  C  CD  . LYS G  1 36  ? 152.835 -5.945  34.013 1.00 40.16  ? 36   LYS G CD  1 
ATOM   6949  C  CE  . LYS G  1 36  ? 152.116 -4.605  34.094 1.00 34.48  ? 36   LYS G CE  1 
ATOM   6950  N  NZ  . LYS G  1 36  ? 152.996 -3.531  34.652 1.00 32.36  ? 36   LYS G NZ  1 
ATOM   6951  N  N   . GLY G  1 37  ? 150.950 -10.274 33.130 1.00 39.87  ? 37   GLY G N   1 
ATOM   6952  C  CA  . GLY G  1 37  ? 149.659 -10.775 33.527 1.00 31.37  ? 37   GLY G CA  1 
ATOM   6953  C  C   . GLY G  1 37  ? 149.220 -12.047 32.836 1.00 29.92  ? 37   GLY G C   1 
ATOM   6954  O  O   . GLY G  1 37  ? 148.032 -12.379 32.931 1.00 32.38  ? 37   GLY G O   1 
ATOM   6955  N  N   . LEU G  1 38  ? 150.113 -12.778 32.150 1.00 29.48  ? 38   LEU G N   1 
ATOM   6956  C  CA  . LEU G  1 38  ? 149.748 -13.986 31.418 1.00 31.96  ? 38   LEU G CA  1 
ATOM   6957  C  C   . LEU G  1 38  ? 150.016 -15.275 32.212 1.00 30.55  ? 38   LEU G C   1 
ATOM   6958  O  O   . LEU G  1 38  ? 150.825 -15.306 33.132 1.00 35.21  ? 38   LEU G O   1 
ATOM   6959  C  CB  . LEU G  1 38  ? 150.502 -14.133 30.089 1.00 33.67  ? 38   LEU G CB  1 
ATOM   6960  C  CG  . LEU G  1 38  ? 150.205 -13.157 28.952 1.00 34.94  ? 38   LEU G CG  1 
ATOM   6961  C  CD1 . LEU G  1 38  ? 151.313 -13.228 27.896 1.00 30.72  ? 38   LEU G CD1 1 
ATOM   6962  C  CD2 . LEU G  1 38  ? 148.853 -13.430 28.320 1.00 32.73  ? 38   LEU G CD2 1 
ATOM   6963  N  N   . THR G  1 39  ? 149.340 -16.362 31.854 1.00 27.56  ? 39   THR G N   1 
ATOM   6964  C  CA  . THR G  1 39  ? 149.782 -17.626 32.468 1.00 34.72  ? 39   THR G CA  1 
ATOM   6965  C  C   . THR G  1 39  ? 151.107 -18.088 31.855 1.00 43.07  ? 39   THR G C   1 
ATOM   6966  O  O   . THR G  1 39  ? 151.335 -17.906 30.656 1.00 39.56  ? 39   THR G O   1 
ATOM   6967  C  CB  . THR G  1 39  ? 148.742 -18.738 32.311 1.00 38.36  ? 39   THR G CB  1 
ATOM   6968  O  OG1 . THR G  1 39  ? 148.392 -18.882 30.930 1.00 35.71  ? 39   THR G OG1 1 
ATOM   6969  C  CG2 . THR G  1 39  ? 147.467 -18.359 33.069 1.00 39.99  ? 39   THR G CG2 1 
ATOM   6970  N  N   . GLU G  1 40  ? 151.967 -18.679 32.684 1.00 37.08  ? 40   GLU G N   1 
ATOM   6971  C  CA  . GLU G  1 40  ? 153.270 -19.165 32.246 1.00 37.29  ? 40   GLU G CA  1 
ATOM   6972  C  C   . GLU G  1 40  ? 153.077 -20.059 31.045 1.00 29.76  ? 40   GLU G C   1 
ATOM   6973  O  O   . GLU G  1 40  ? 152.156 -20.876 31.042 1.00 37.27  ? 40   GLU G O   1 
ATOM   6974  C  CB  . GLU G  1 40  ? 154.002 -19.934 33.346 1.00 42.38  ? 40   GLU G CB  1 
ATOM   6975  C  CG  . GLU G  1 40  ? 155.466 -20.170 32.991 1.00 52.12  ? 40   GLU G CG  1 
ATOM   6976  C  CD  . GLU G  1 40  ? 156.159 -21.071 33.995 1.00 61.42  ? 40   GLU G CD  1 
ATOM   6977  O  OE1 . GLU G  1 40  ? 155.429 -21.748 34.747 1.00 50.86  ? 40   GLU G OE1 1 
ATOM   6978  O  OE2 . GLU G  1 40  ? 157.405 -21.089 34.021 1.00 87.39  ? 40   GLU G OE2 1 
ATOM   6979  N  N   . GLY G  1 41  ? 153.884 -19.933 29.983 1.00 32.69  ? 41   GLY G N   1 
ATOM   6980  C  CA  . GLY G  1 41  ? 153.498 -20.757 28.825 1.00 27.01  ? 41   GLY G CA  1 
ATOM   6981  C  C   . GLY G  1 41  ? 153.344 -19.954 27.535 1.00 30.81  ? 41   GLY G C   1 
ATOM   6982  O  O   . GLY G  1 41  ? 153.654 -18.762 27.498 1.00 33.05  ? 41   GLY G O   1 
ATOM   6983  N  N   . LEU G  1 42  ? 152.859 -20.600 26.493 1.00 34.28  ? 42   LEU G N   1 
ATOM   6984  C  CA  . LEU G  1 42  ? 152.675 -20.123 25.142 1.00 43.53  ? 42   LEU G CA  1 
ATOM   6985  C  C   . LEU G  1 42  ? 151.305 -19.478 24.905 1.00 46.59  ? 42   LEU G C   1 
ATOM   6986  O  O   . LEU G  1 42  ? 150.288 -20.089 25.249 1.00 33.72  ? 42   LEU G O   1 
ATOM   6987  C  CB  . LEU G  1 42  ? 152.782 -21.285 24.152 1.00 36.82  ? 42   LEU G CB  1 
ATOM   6988  C  CG  . LEU G  1 42  ? 154.166 -21.886 23.906 1.00 40.17  ? 42   LEU G CG  1 
ATOM   6989  C  CD1 . LEU G  1 42  ? 154.013 -23.226 23.199 1.00 42.10  ? 42   LEU G CD1 1 
ATOM   6990  C  CD2 . LEU G  1 42  ? 155.029 -20.948 23.081 1.00 42.23  ? 42   LEU G CD2 1 
ATOM   6991  N  N   . HIS G  1 43  ? 151.306 -18.292 24.303 1.00 39.17  ? 43   HIS G N   1 
ATOM   6992  C  CA  . HIS G  1 43  ? 150.067 -17.588 23.964 1.00 34.81  ? 43   HIS G CA  1 
ATOM   6993  C  C   . HIS G  1 43  ? 150.063 -17.091 22.511 1.00 24.92  ? 43   HIS G C   1 
ATOM   6994  O  O   . HIS G  1 43  ? 151.045 -16.460 22.125 1.00 30.23  ? 43   HIS G O   1 
ATOM   6995  C  CB  . HIS G  1 43  ? 149.866 -16.414 24.925 1.00 32.57  ? 43   HIS G CB  1 
ATOM   6996  C  CG  . HIS G  1 43  ? 149.745 -16.824 26.364 1.00 36.40  ? 43   HIS G CG  1 
ATOM   6997  N  ND1 . HIS G  1 43  ? 148.541 -17.205 26.930 1.00 37.41  ? 43   HIS G ND1 1 
ATOM   6998  C  CD2 . HIS G  1 43  ? 150.667 -16.897 27.353 1.00 30.54  ? 43   HIS G CD2 1 
ATOM   6999  C  CE1 . HIS G  1 43  ? 148.741 -17.503 28.206 1.00 35.54  ? 43   HIS G CE1 1 
ATOM   7000  N  NE2 . HIS G  1 43  ? 150.021 -17.326 28.492 1.00 30.81  ? 43   HIS G NE2 1 
ATOM   7001  N  N   . GLY G  1 44  ? 148.996 -17.408 21.804 1.00 30.01  ? 44   GLY G N   1 
ATOM   7002  C  CA  . GLY G  1 44  ? 148.811 -17.085 20.393 1.00 31.76  ? 44   GLY G CA  1 
ATOM   7003  C  C   . GLY G  1 44  ? 148.901 -15.575 20.217 1.00 40.77  ? 44   GLY G C   1 
ATOM   7004  O  O   . GLY G  1 44  ? 148.410 -14.830 21.069 1.00 32.59  ? 44   GLY G O   1 
ATOM   7005  N  N   . PHE G  1 45  ? 149.520 -15.105 19.148 1.00 35.04  ? 45   PHE G N   1 
ATOM   7006  C  CA  . PHE G  1 45  ? 149.760 -13.664 18.972 1.00 35.76  ? 45   PHE G CA  1 
ATOM   7007  C  C   . PHE G  1 45  ? 149.488 -13.298 17.523 1.00 42.29  ? 45   PHE G C   1 
ATOM   7008  O  O   . PHE G  1 45  ? 150.164 -13.850 16.632 1.00 33.17  ? 45   PHE G O   1 
ATOM   7009  C  CB  . PHE G  1 45  ? 151.185 -13.415 19.400 1.00 30.11  ? 45   PHE G CB  1 
ATOM   7010  C  CG  . PHE G  1 45  ? 151.722 -12.025 19.602 1.00 35.32  ? 45   PHE G CG  1 
ATOM   7011  C  CD1 . PHE G  1 45  ? 151.077 -11.111 20.432 1.00 28.57  ? 45   PHE G CD1 1 
ATOM   7012  C  CD2 . PHE G  1 45  ? 152.892 -11.636 18.956 1.00 28.35  ? 45   PHE G CD2 1 
ATOM   7013  C  CE1 . PHE G  1 45  ? 151.598 -9.848  20.607 1.00 25.55  ? 45   PHE G CE1 1 
ATOM   7014  C  CE2 . PHE G  1 45  ? 153.394 -10.365 19.142 1.00 36.22  ? 45   PHE G CE2 1 
ATOM   7015  C  CZ  . PHE G  1 45  ? 152.760 -9.447  19.966 1.00 32.84  ? 45   PHE G CZ  1 
ATOM   7016  N  N   . HIS G  1 46  ? 148.500 -12.435 17.231 1.00 30.42  ? 46   HIS G N   1 
ATOM   7017  C  CA  . HIS G  1 46  ? 148.174 -12.194 15.822 1.00 29.02  ? 46   HIS G CA  1 
ATOM   7018  C  C   . HIS G  1 46  ? 147.715 -10.737 15.618 1.00 43.75  ? 46   HIS G C   1 
ATOM   7019  O  O   . HIS G  1 46  ? 147.172 -10.100 16.519 1.00 27.79  ? 46   HIS G O   1 
ATOM   7020  C  CB  . HIS G  1 46  ? 147.110 -13.121 15.254 1.00 33.56  ? 46   HIS G CB  1 
ATOM   7021  C  CG  . HIS G  1 46  ? 146.958 -14.504 15.800 1.00 42.76  ? 46   HIS G CG  1 
ATOM   7022  N  ND1 . HIS G  1 46  ? 145.948 -14.895 16.656 1.00 41.64  ? 46   HIS G ND1 1 
ATOM   7023  C  CD2 . HIS G  1 46  ? 147.722 -15.614 15.597 1.00 37.63  ? 46   HIS G CD2 1 
ATOM   7024  C  CE1 . HIS G  1 46  ? 146.091 -16.185 16.957 1.00 43.97  ? 46   HIS G CE1 1 
ATOM   7025  N  NE2 . HIS G  1 46  ? 147.163 -16.644 16.329 1.00 39.64  ? 46   HIS G NE2 1 
ATOM   7026  N  N   . VAL G  1 47  ? 147.940 -10.234 14.406 1.00 33.58  ? 47   VAL G N   1 
ATOM   7027  C  CA  . VAL G  1 47  ? 147.283 -9.008  13.964 1.00 31.19  ? 47   VAL G CA  1 
ATOM   7028  C  C   . VAL G  1 47  ? 145.927 -9.385  13.391 1.00 31.41  ? 47   VAL G C   1 
ATOM   7029  O  O   . VAL G  1 47  ? 145.797 -10.203 12.465 1.00 32.55  ? 47   VAL G O   1 
ATOM   7030  C  CB  . VAL G  1 47  ? 148.120 -8.246  12.926 1.00 27.18  ? 47   VAL G CB  1 
ATOM   7031  C  CG1 . VAL G  1 47  ? 147.342 -7.053  12.364 1.00 29.24  ? 47   VAL G CG1 1 
ATOM   7032  C  CG2 . VAL G  1 47  ? 149.449 -7.811  13.524 1.00 26.63  ? 47   VAL G CG2 1 
ATOM   7033  N  N   . HIS G  1 48  ? 144.856 -8.800  13.939 1.00 28.47  ? 48   HIS G N   1 
ATOM   7034  C  CA  . HIS G  1 48  ? 143.531 -9.047  13.394 1.00 25.64  ? 48   HIS G CA  1 
ATOM   7035  C  C   . HIS G  1 48  ? 143.104 -7.863  12.521 1.00 31.32  ? 48   HIS G C   1 
ATOM   7036  O  O   . HIS G  1 48  ? 143.710 -6.792  12.582 1.00 31.11  ? 48   HIS G O   1 
ATOM   7037  C  CB  . HIS G  1 48  ? 142.452 -9.278  14.445 1.00 29.50  ? 48   HIS G CB  1 
ATOM   7038  C  CG  . HIS G  1 48  ? 142.617 -10.519 15.262 1.00 22.87  ? 48   HIS G CG  1 
ATOM   7039  N  ND1 . HIS G  1 48  ? 141.560 -11.340 15.566 1.00 31.17  ? 48   HIS G ND1 1 
ATOM   7040  C  CD2 . HIS G  1 48  ? 143.711 -11.078 15.834 1.00 29.59  ? 48   HIS G CD2 1 
ATOM   7041  C  CE1 . HIS G  1 48  ? 141.978 -12.360 16.300 1.00 30.44  ? 48   HIS G CE1 1 
ATOM   7042  N  NE2 . HIS G  1 48  ? 143.278 -12.219 16.475 1.00 35.71  ? 48   HIS G NE2 1 
ATOM   7043  N  N   . GLU G  1 49  ? 142.065 -8.105  11.729 1.00 26.97  ? 49   GLU G N   1 
ATOM   7044  C  CA  . GLU G  1 49  ? 141.873 -7.211  10.584 1.00 36.12  ? 49   GLU G CA  1 
ATOM   7045  C  C   . GLU G  1 49  ? 141.395 -5.816  10.972 1.00 30.17  ? 49   GLU G C   1 
ATOM   7046  O  O   . GLU G  1 49  ? 141.894 -4.856  10.391 1.00 30.36  ? 49   GLU G O   1 
ATOM   7047  C  CB  . GLU G  1 49  ? 140.913 -7.884  9.605  1.00 34.35  ? 49   GLU G CB  1 
ATOM   7048  C  CG  . GLU G  1 49  ? 140.641 -7.060  8.358  1.00 40.24  ? 49   GLU G CG  1 
ATOM   7049  C  CD  . GLU G  1 49  ? 139.562 -7.638  7.464  1.00 46.37  ? 49   GLU G CD  1 
ATOM   7050  O  OE1 . GLU G  1 49  ? 139.249 -6.950  6.465  1.00 51.38  ? 49   GLU G OE1 1 
ATOM   7051  O  OE2 . GLU G  1 49  ? 139.011 -8.739  7.707  1.00 41.60  ? 49   GLU G OE2 1 
ATOM   7052  N  N   . PHE G  1 50  ? 140.466 -5.677  11.905 1.00 26.85  ? 50   PHE G N   1 
ATOM   7053  C  CA  . PHE G  1 50  ? 139.903 -4.358  12.209 1.00 33.62  ? 50   PHE G CA  1 
ATOM   7054  C  C   . PHE G  1 50  ? 140.475 -3.722  13.462 1.00 34.58  ? 50   PHE G C   1 
ATOM   7055  O  O   . PHE G  1 50  ? 140.696 -4.376  14.483 1.00 32.44  ? 50   PHE G O   1 
ATOM   7056  C  CB  . PHE G  1 50  ? 138.378 -4.483  12.354 1.00 34.75  ? 50   PHE G CB  1 
ATOM   7057  C  CG  . PHE G  1 50  ? 137.801 -5.113  11.091 1.00 33.26  ? 50   PHE G CG  1 
ATOM   7058  C  CD1 . PHE G  1 50  ? 138.052 -4.522  9.868  1.00 40.73  ? 50   PHE G CD1 1 
ATOM   7059  C  CD2 . PHE G  1 50  ? 137.044 -6.259  11.183 1.00 36.75  ? 50   PHE G CD2 1 
ATOM   7060  C  CE1 . PHE G  1 50  ? 137.559 -5.084  8.705  1.00 41.56  ? 50   PHE G CE1 1 
ATOM   7061  C  CE2 . PHE G  1 50  ? 136.559 -6.835  10.028 1.00 44.83  ? 50   PHE G CE2 1 
ATOM   7062  C  CZ  . PHE G  1 50  ? 136.811 -6.240  8.805  1.00 50.25  ? 50   PHE G CZ  1 
ATOM   7063  N  N   . GLY G  1 51  ? 140.705 -2.412  13.390 1.00 27.37  ? 51   GLY G N   1 
ATOM   7064  C  CA  . GLY G  1 51  ? 141.144 -1.647  14.545 1.00 27.85  ? 51   GLY G CA  1 
ATOM   7065  C  C   . GLY G  1 51  ? 139.931 -1.106  15.303 1.00 35.50  ? 51   GLY G C   1 
ATOM   7066  O  O   . GLY G  1 51  ? 139.886 0.086   15.589 1.00 33.82  ? 51   GLY G O   1 
ATOM   7067  N  N   . ASP G  1 52  ? 138.974 -1.974  15.590 1.00 34.18  ? 52   ASP G N   1 
ATOM   7068  C  CA  . ASP G  1 52  ? 137.687 -1.668  16.190 1.00 29.98  ? 52   ASP G CA  1 
ATOM   7069  C  C   . ASP G  1 52  ? 137.599 -2.308  17.572 1.00 37.47  ? 52   ASP G C   1 
ATOM   7070  O  O   . ASP G  1 52  ? 137.433 -3.521  17.680 1.00 31.71  ? 52   ASP G O   1 
ATOM   7071  C  CB  . ASP G  1 52  ? 136.563 -2.171  15.298 1.00 27.29  ? 52   ASP G CB  1 
ATOM   7072  C  CG  . ASP G  1 52  ? 135.158 -1.911  15.786 1.00 29.66  ? 52   ASP G CG  1 
ATOM   7073  O  OD1 . ASP G  1 52  ? 134.214 -2.063  14.969 1.00 34.38  ? 52   ASP G OD1 1 
ATOM   7074  O  OD2 . ASP G  1 52  ? 134.967 -1.562  16.974 1.00 33.17  ? 52   ASP G OD2 1 
ATOM   7075  N  N   . ASN G  1 53  ? 137.717 -1.477  18.593 1.00 30.72  ? 53   ASN G N   1 
ATOM   7076  C  CA  . ASN G  1 53  ? 137.633 -1.929  19.974 1.00 27.09  ? 53   ASN G CA  1 
ATOM   7077  C  C   . ASN G  1 53  ? 136.292 -1.590  20.622 1.00 29.32  ? 53   ASN G C   1 
ATOM   7078  O  O   . ASN G  1 53  ? 136.223 -1.499  21.850 1.00 28.37  ? 53   ASN G O   1 
ATOM   7079  C  CB  . ASN G  1 53  ? 138.765 -1.262  20.741 1.00 31.49  ? 53   ASN G CB  1 
ATOM   7080  C  CG  . ASN G  1 53  ? 139.010 -1.986  22.048 1.00 45.60  ? 53   ASN G CG  1 
ATOM   7081  O  OD1 . ASN G  1 53  ? 139.027 -1.347  23.093 1.00 49.64  ? 53   ASN G OD1 1 
ATOM   7082  N  ND2 . ASN G  1 53  ? 139.176 -3.294  21.932 1.00 76.72  ? 53   ASN G ND2 1 
ATOM   7083  N  N   . THR G  1 54  ? 135.249 -1.396  19.833 1.00 25.52  ? 54   THR G N   1 
ATOM   7084  C  CA  . THR G  1 54  ? 133.920 -1.077  20.331 1.00 35.95  ? 54   THR G CA  1 
ATOM   7085  C  C   . THR G  1 54  ? 133.277 -2.254  21.061 1.00 43.52  ? 54   THR G C   1 
ATOM   7086  O  O   . THR G  1 54  ? 132.370 -2.012  21.860 1.00 47.08  ? 54   THR G O   1 
ATOM   7087  C  CB  . THR G  1 54  ? 132.916 -0.608  19.249 1.00 36.52  ? 54   THR G CB  1 
ATOM   7088  O  OG1 . THR G  1 54  ? 132.632 -1.649  18.303 1.00 33.56  ? 54   THR G OG1 1 
ATOM   7089  C  CG2 . THR G  1 54  ? 133.507 0.576   18.486 1.00 31.02  ? 54   THR G CG2 1 
ATOM   7090  N  N   . ALA G  1 55  ? 133.689 -3.491  20.819 1.00 32.44  ? 55   ALA G N   1 
ATOM   7091  C  CA  . ALA G  1 55  ? 133.161 -4.581  21.662 1.00 31.69  ? 55   ALA G CA  1 
ATOM   7092  C  C   . ALA G  1 55  ? 134.333 -5.334  22.284 1.00 29.29  ? 55   ALA G C   1 
ATOM   7093  O  O   . ALA G  1 55  ? 134.437 -6.552  22.243 1.00 48.58  ? 55   ALA G O   1 
ATOM   7094  C  CB  . ALA G  1 55  ? 132.239 -5.478  20.863 1.00 35.84  ? 55   ALA G CB  1 
ATOM   7095  N  N   . GLY G  1 56  ? 135.290 -4.593  22.848 1.00 44.14  ? 56   GLY G N   1 
ATOM   7096  C  CA  . GLY G  1 56  ? 136.507 -5.261  23.301 1.00 43.46  ? 56   GLY G CA  1 
ATOM   7097  C  C   . GLY G  1 56  ? 137.231 -5.872  22.102 1.00 42.03  ? 56   GLY G C   1 
ATOM   7098  O  O   . GLY G  1 56  ? 137.073 -5.365  20.997 1.00 25.55  ? 56   GLY G O   1 
ATOM   7099  N  N   . CYS G  1 57  ? 137.981 -6.949  22.319 1.00 42.19  ? 57   CYS G N   1 
ATOM   7100  C  CA  . CYS G  1 57  ? 138.793 -7.589  21.288 1.00 33.62  ? 57   CYS G CA  1 
ATOM   7101  C  C   . CYS G  1 57  ? 137.964 -8.380  20.290 1.00 31.72  ? 57   CYS G C   1 
ATOM   7102  O  O   . CYS G  1 57  ? 138.482 -8.762  19.229 1.00 34.34  ? 57   CYS G O   1 
ATOM   7103  C  CB  A CYS G  1 57  ? 139.824 -8.506  21.968 0.43 40.97  ? 57   CYS G CB  1 
ATOM   7104  C  CB  B CYS G  1 57  ? 139.856 -8.495  21.919 0.57 41.64  ? 57   CYS G CB  1 
ATOM   7105  S  SG  A CYS G  1 57  ? 140.767 -7.637  23.253 0.43 59.34  ? 57   CYS G SG  1 
ATOM   7106  S  SG  B CYS G  1 57  ? 140.746 -7.800  23.331 0.57 45.64  ? 57   CYS G SG  1 
ATOM   7107  N  N   . THR G  1 58  ? 136.681 -8.622  20.573 1.00 26.70  ? 58   THR G N   1 
ATOM   7108  C  CA  . THR G  1 58  ? 135.862 -9.359  19.621 1.00 27.51  ? 58   THR G CA  1 
ATOM   7109  C  C   . THR G  1 58  ? 135.618 -8.615  18.313 1.00 40.21  ? 58   THR G C   1 
ATOM   7110  O  O   . THR G  1 58  ? 135.479 -9.223  17.248 1.00 29.93  ? 58   THR G O   1 
ATOM   7111  C  CB  . THR G  1 58  ? 134.473 -9.688  20.223 1.00 43.07  ? 58   THR G CB  1 
ATOM   7112  O  OG1 . THR G  1 58  ? 134.643 -10.665 21.255 1.00 47.50  ? 58   THR G OG1 1 
ATOM   7113  C  CG2 . THR G  1 58  ? 133.556 -10.307 19.184 1.00 37.62  ? 58   THR G CG2 1 
ATOM   7114  N  N   . SER G  1 59  ? 135.535 -7.284  18.367 1.00 38.64  ? 59   SER G N   1 
ATOM   7115  C  CA  . SER G  1 59  ? 135.212 -6.520  17.164 1.00 31.04  ? 59   SER G CA  1 
ATOM   7116  C  C   . SER G  1 59  ? 136.455 -6.347  16.296 1.00 32.84  ? 59   SER G C   1 
ATOM   7117  O  O   . SER G  1 59  ? 136.350 -5.812  15.190 1.00 31.80  ? 59   SER G O   1 
ATOM   7118  C  CB  . SER G  1 59  ? 134.594 -5.161  17.503 1.00 30.71  ? 59   SER G CB  1 
ATOM   7119  O  OG  . SER G  1 59  ? 135.196 -4.530  18.614 1.00 29.59  ? 59   SER G OG  1 
ATOM   7120  N  N   . ALA G  1 60  ? 137.629 -6.791  16.739 1.00 30.14  ? 60   ALA G N   1 
ATOM   7121  C  CA  . ALA G  1 60  ? 138.770 -6.793  15.822 1.00 30.95  ? 60   ALA G CA  1 
ATOM   7122  C  C   . ALA G  1 60  ? 138.580 -7.766  14.657 1.00 29.78  ? 60   ALA G C   1 
ATOM   7123  O  O   . ALA G  1 60  ? 139.350 -7.743  13.688 1.00 33.15  ? 60   ALA G O   1 
ATOM   7124  C  CB  . ALA G  1 60  ? 140.053 -7.094  16.587 1.00 34.79  ? 60   ALA G CB  1 
ATOM   7125  N  N   . GLY G  1 61  ? 137.576 -8.633  14.698 1.00 30.75  ? 61   GLY G N   1 
ATOM   7126  C  CA  . GLY G  1 61  ? 137.352 -9.543  13.576 1.00 39.07  ? 61   GLY G CA  1 
ATOM   7127  C  C   . GLY G  1 61  ? 138.392 -10.655 13.566 1.00 38.51  ? 61   GLY G C   1 
ATOM   7128  O  O   . GLY G  1 61  ? 139.020 -10.913 14.593 1.00 33.49  ? 61   GLY G O   1 
ATOM   7129  N  N   . PRO G  1 62  ? 138.582 -11.302 12.424 1.00 38.92  ? 62   PRO G N   1 
ATOM   7130  C  CA  . PRO G  1 62  ? 139.522 -12.425 12.312 1.00 34.08  ? 62   PRO G CA  1 
ATOM   7131  C  C   . PRO G  1 62  ? 140.934 -11.960 12.022 1.00 34.35  ? 62   PRO G C   1 
ATOM   7132  O  O   . PRO G  1 62  ? 141.184 -10.778 11.810 1.00 31.45  ? 62   PRO G O   1 
ATOM   7133  C  CB  . PRO G  1 62  ? 139.009 -13.142 11.057 1.00 38.69  ? 62   PRO G CB  1 
ATOM   7134  C  CG  . PRO G  1 62  ? 138.658 -11.957 10.192 1.00 45.45  ? 62   PRO G CG  1 
ATOM   7135  C  CD  . PRO G  1 62  ? 137.931 -11.019 11.134 1.00 35.22  ? 62   PRO G CD  1 
ATOM   7136  N  N   . HIS G  1 63  ? 141.850 -12.929 12.011 1.00 33.13  ? 63   HIS G N   1 
ATOM   7137  C  CA  . HIS G  1 63  ? 143.233 -12.667 11.654 1.00 34.15  ? 63   HIS G CA  1 
ATOM   7138  C  C   . HIS G  1 63  ? 143.250 -11.918 10.324 1.00 31.24  ? 63   HIS G C   1 
ATOM   7139  O  O   . HIS G  1 63  ? 142.463 -12.231 9.439  1.00 30.81  ? 63   HIS G O   1 
ATOM   7140  C  CB  . HIS G  1 63  ? 144.060 -13.950 11.544 1.00 38.47  ? 63   HIS G CB  1 
ATOM   7141  C  CG  . HIS G  1 63  ? 144.024 -14.840 12.746 1.00 37.99  ? 63   HIS G CG  1 
ATOM   7142  N  ND1 . HIS G  1 63  ? 144.698 -16.048 12.803 1.00 38.25  ? 63   HIS G ND1 1 
ATOM   7143  C  CD2 . HIS G  1 63  ? 143.393 -14.699 13.939 1.00 33.80  ? 63   HIS G CD2 1 
ATOM   7144  C  CE1 . HIS G  1 63  ? 144.474 -16.597 13.985 1.00 42.85  ? 63   HIS G CE1 1 
ATOM   7145  N  NE2 . HIS G  1 63  ? 143.686 -15.804 14.696 1.00 39.98  ? 63   HIS G NE2 1 
ATOM   7146  N  N   . PHE G  1 64  ? 144.121 -10.929 10.217 1.00 33.83  ? 64   PHE G N   1 
ATOM   7147  C  CA  . PHE G  1 64  ? 144.206 -10.200 8.948  1.00 33.93  ? 64   PHE G CA  1 
ATOM   7148  C  C   . PHE G  1 64  ? 144.609 -11.144 7.818  1.00 38.78  ? 64   PHE G C   1 
ATOM   7149  O  O   . PHE G  1 64  ? 145.687 -11.739 7.900  1.00 38.53  ? 64   PHE G O   1 
ATOM   7150  C  CB  . PHE G  1 64  ? 145.231 -9.105  9.133  1.00 33.43  ? 64   PHE G CB  1 
ATOM   7151  C  CG  . PHE G  1 64  ? 145.376 -8.197  7.924  1.00 40.91  ? 64   PHE G CG  1 
ATOM   7152  C  CD1 . PHE G  1 64  ? 146.616 -7.661  7.618  1.00 45.83  ? 64   PHE G CD1 1 
ATOM   7153  C  CD2 . PHE G  1 64  ? 144.270 -7.921  7.146  1.00 39.83  ? 64   PHE G CD2 1 
ATOM   7154  C  CE1 . PHE G  1 64  ? 146.766 -6.827  6.522  1.00 41.10  ? 64   PHE G CE1 1 
ATOM   7155  C  CE2 . PHE G  1 64  ? 144.421 -7.081  6.052  1.00 48.24  ? 64   PHE G CE2 1 
ATOM   7156  C  CZ  . PHE G  1 64  ? 145.660 -6.546  5.748  1.00 39.62  ? 64   PHE G CZ  1 
ATOM   7157  N  N   . ASN G  1 65  ? 143.779 -11.293 6.796  1.00 44.87  ? 65   ASN G N   1 
ATOM   7158  C  CA  . ASN G  1 65  ? 143.980 -12.328 5.783  1.00 51.48  ? 65   ASN G CA  1 
ATOM   7159  C  C   . ASN G  1 65  ? 143.560 -11.915 4.382  1.00 40.68  ? 65   ASN G C   1 
ATOM   7160  O  O   . ASN G  1 65  ? 142.589 -12.457 3.841  1.00 43.75  ? 65   ASN G O   1 
ATOM   7161  C  CB  . ASN G  1 65  ? 143.161 -13.571 6.167  1.00 53.78  ? 65   ASN G CB  1 
ATOM   7162  C  CG  . ASN G  1 65  ? 143.402 -14.742 5.226  1.00 52.96  ? 65   ASN G CG  1 
ATOM   7163  O  OD1 . ASN G  1 65  ? 144.335 -14.753 4.427  1.00 42.48  ? 65   ASN G OD1 1 
ATOM   7164  N  ND2 . ASN G  1 65  ? 142.548 -15.751 5.394  1.00 36.50  ? 65   ASN G ND2 1 
ATOM   7165  N  N   . PRO G  1 66  ? 144.252 -10.957 3.793  1.00 35.35  ? 66   PRO G N   1 
ATOM   7166  C  CA  . PRO G  1 66  ? 143.864 -10.499 2.454  1.00 48.37  ? 66   PRO G CA  1 
ATOM   7167  C  C   . PRO G  1 66  ? 144.059 -11.565 1.382  1.00 49.59  ? 66   PRO G C   1 
ATOM   7168  O  O   . PRO G  1 66  ? 143.517 -11.417 0.279  1.00 58.02  ? 66   PRO G O   1 
ATOM   7169  C  CB  . PRO G  1 66  ? 144.797 -9.308  2.220  1.00 43.93  ? 66   PRO G CB  1 
ATOM   7170  C  CG  . PRO G  1 66  ? 145.965 -9.528  3.120  1.00 35.36  ? 66   PRO G CG  1 
ATOM   7171  C  CD  . PRO G  1 66  ? 145.406 -10.223 4.341  1.00 33.12  ? 66   PRO G CD  1 
ATOM   7172  N  N   . LEU G  1 67  ? 144.804 -12.635 1.653  1.00 51.73  ? 67   LEU G N   1 
ATOM   7173  C  CA  . LEU G  1 67  ? 145.036 -13.665 0.638  1.00 52.64  ? 67   LEU G CA  1 
ATOM   7174  C  C   . LEU G  1 67  ? 144.238 -14.937 0.859  1.00 52.78  ? 67   LEU G C   1 
ATOM   7175  O  O   . LEU G  1 67  ? 144.557 -15.966 0.257  1.00 52.53  ? 67   LEU G O   1 
ATOM   7176  C  CB  . LEU G  1 67  ? 146.534 -14.022 0.588  1.00 51.69  ? 67   LEU G CB  1 
ATOM   7177  C  CG  . LEU G  1 67  ? 147.405 -12.763 0.443  1.00 61.57  ? 67   LEU G CG  1 
ATOM   7178  C  CD1 . LEU G  1 67  ? 148.820 -13.113 0.047  1.00 78.99  ? 67   LEU G CD1 1 
ATOM   7179  C  CD2 . LEU G  1 67  ? 146.717 -11.839 -0.546 1.00 62.55  ? 67   LEU G CD2 1 
ATOM   7180  N  N   . SER G  1 68  ? 143.230 -14.852 1.707  1.00 59.84  ? 68   SER G N   1 
ATOM   7181  C  CA  . SER G  1 68  ? 142.328 -15.941 2.055  1.00 60.67  ? 68   SER G CA  1 
ATOM   7182  C  C   . SER G  1 68  ? 143.089 -17.245 2.256  1.00 63.03  ? 68   SER G C   1 
ATOM   7183  O  O   . SER G  1 68  ? 142.687 -18.330 1.842  1.00 73.75  ? 68   SER G O   1 
ATOM   7184  C  CB  . SER G  1 68  ? 141.254 -16.088 0.977  1.00 67.80  ? 68   SER G CB  1 
ATOM   7185  O  OG  . SER G  1 68  ? 139.957 -16.004 1.546  1.00 81.41  ? 68   SER G OG  1 
ATOM   7186  N  N   . ARG G  1 69  ? 144.244 -17.124 2.908  1.00 60.00  ? 69   ARG G N   1 
ATOM   7187  C  CA  . ARG G  1 69  ? 145.067 -18.300 3.148  1.00 65.22  ? 69   ARG G CA  1 
ATOM   7188  C  C   . ARG G  1 69  ? 144.554 -19.036 4.376  1.00 61.99  ? 69   ARG G C   1 
ATOM   7189  O  O   . ARG G  1 69  ? 143.803 -18.478 5.180  1.00 56.87  ? 69   ARG G O   1 
ATOM   7190  C  CB  . ARG G  1 69  ? 146.531 -17.906 3.349  1.00 66.03  ? 69   ARG G CB  1 
ATOM   7191  C  CG  . ARG G  1 69  ? 147.194 -17.347 2.102  1.00 74.32  ? 69   ARG G CG  1 
ATOM   7192  C  CD  . ARG G  1 69  ? 148.079 -18.403 1.463  1.00 86.04  ? 69   ARG G CD  1 
ATOM   7193  N  NE  . ARG G  1 69  ? 147.385 -19.692 1.332  1.00 84.27  ? 69   ARG G NE  1 
ATOM   7194  C  CZ  . ARG G  1 69  ? 148.008 -20.791 0.920  1.00 76.00  ? 69   ARG G CZ  1 
ATOM   7195  N  NH1 . ARG G  1 69  ? 149.300 -20.723 0.620  1.00 58.94  ? 69   ARG G NH1 1 
ATOM   7196  N  NH2 . ARG G  1 69  ? 147.359 -21.940 0.810  1.00 62.40  ? 69   ARG G NH2 1 
ATOM   7197  N  N   . LYS G  1 70  ? 144.979 -20.288 4.522  1.00 52.24  ? 70   LYS G N   1 
ATOM   7198  C  CA  . LYS G  1 70  ? 144.695 -20.947 5.796  1.00 61.62  ? 70   LYS G CA  1 
ATOM   7199  C  C   . LYS G  1 70  ? 145.622 -20.357 6.856  1.00 57.33  ? 70   LYS G C   1 
ATOM   7200  O  O   . LYS G  1 70  ? 146.615 -19.710 6.517  1.00 68.68  ? 70   LYS G O   1 
ATOM   7201  C  CB  . LYS G  1 70  ? 144.856 -22.458 5.688  1.00 74.43  ? 70   LYS G CB  1 
ATOM   7202  C  CG  . LYS G  1 70  ? 143.961 -23.109 4.643  1.00 83.54  ? 70   LYS G CG  1 
ATOM   7203  C  CD  . LYS G  1 70  ? 143.141 -24.244 5.232  1.00 86.30  ? 70   LYS G CD  1 
ATOM   7204  C  CE  . LYS G  1 70  ? 143.983 -25.491 5.457  1.00 87.22  ? 70   LYS G CE  1 
ATOM   7205  N  NZ  . LYS G  1 70  ? 143.133 -26.685 5.728  1.00 101.46 ? 70   LYS G NZ  1 
ATOM   7206  N  N   . HIS G  1 71  ? 145.294 -20.576 8.119  1.00 56.50  ? 71   HIS G N   1 
ATOM   7207  C  CA  . HIS G  1 71  ? 146.101 -20.101 9.237  1.00 52.33  ? 71   HIS G CA  1 
ATOM   7208  C  C   . HIS G  1 71  ? 147.408 -20.873 9.336  1.00 56.44  ? 71   HIS G C   1 
ATOM   7209  O  O   . HIS G  1 71  ? 147.439 -22.071 9.050  1.00 55.81  ? 71   HIS G O   1 
ATOM   7210  C  CB  . HIS G  1 71  ? 145.291 -20.240 10.529 1.00 47.68  ? 71   HIS G CB  1 
ATOM   7211  C  CG  . HIS G  1 71  ? 146.032 -19.899 11.780 1.00 45.53  ? 71   HIS G CG  1 
ATOM   7212  N  ND1 . HIS G  1 71  ? 146.380 -18.600 12.109 1.00 39.63  ? 71   HIS G ND1 1 
ATOM   7213  C  CD2 . HIS G  1 71  ? 146.496 -20.692 12.775 1.00 41.71  ? 71   HIS G CD2 1 
ATOM   7214  C  CE1 . HIS G  1 71  ? 147.023 -18.614 13.257 1.00 43.41  ? 71   HIS G CE1 1 
ATOM   7215  N  NE2 . HIS G  1 71  ? 147.108 -19.870 13.689 1.00 50.97  ? 71   HIS G NE2 1 
ATOM   7216  N  N   . GLY G  1 72  ? 148.496 -20.227 9.737  1.00 55.61  ? 72   GLY G N   1 
ATOM   7217  C  CA  . GLY G  1 72  ? 149.758 -20.918 9.947  1.00 46.41  ? 72   GLY G CA  1 
ATOM   7218  C  C   . GLY G  1 72  ? 150.618 -20.141 10.933 1.00 51.36  ? 72   GLY G C   1 
ATOM   7219  O  O   . GLY G  1 72  ? 150.132 -19.150 11.484 1.00 53.00  ? 72   GLY G O   1 
ATOM   7220  N  N   . GLY G  1 73  ? 151.841 -20.600 11.112 1.00 46.20  ? 73   GLY G N   1 
ATOM   7221  C  CA  . GLY G  1 73  ? 152.902 -19.973 11.880 1.00 40.01  ? 73   GLY G CA  1 
ATOM   7222  C  C   . GLY G  1 73  ? 153.603 -18.929 11.018 1.00 34.97  ? 73   GLY G C   1 
ATOM   7223  O  O   . GLY G  1 73  ? 153.459 -18.959 9.794  1.00 39.74  ? 73   GLY G O   1 
ATOM   7224  N  N   . PRO G  1 74  ? 154.325 -18.038 11.665 1.00 35.68  ? 74   PRO G N   1 
ATOM   7225  C  CA  . PRO G  1 74  ? 154.967 -16.900 11.015 1.00 43.10  ? 74   PRO G CA  1 
ATOM   7226  C  C   . PRO G  1 74  ? 155.983 -17.349 9.968  1.00 59.01  ? 74   PRO G C   1 
ATOM   7227  O  O   . PRO G  1 74  ? 156.264 -16.600 9.026  1.00 49.10  ? 74   PRO G O   1 
ATOM   7228  C  CB  . PRO G  1 74  ? 155.711 -16.184 12.145 1.00 37.99  ? 74   PRO G CB  1 
ATOM   7229  C  CG  . PRO G  1 74  ? 155.820 -17.194 13.237 1.00 36.58  ? 74   PRO G CG  1 
ATOM   7230  C  CD  . PRO G  1 74  ? 154.594 -18.054 13.119 1.00 43.55  ? 74   PRO G CD  1 
ATOM   7231  N  N   . LYS G  1 75  ? 156.541 -18.553 10.123 1.00 49.56  ? 75   LYS G N   1 
ATOM   7232  C  CA  . LYS G  1 75  ? 157.526 -18.960 9.113  1.00 53.26  ? 75   LYS G CA  1 
ATOM   7233  C  C   . LYS G  1 75  ? 156.893 -19.900 8.098  1.00 62.58  ? 75   LYS G C   1 
ATOM   7234  O  O   . LYS G  1 75  ? 157.386 -20.062 6.984  1.00 76.95  ? 75   LYS G O   1 
ATOM   7235  C  CB  . LYS G  1 75  ? 158.738 -19.606 9.774  1.00 51.61  ? 75   LYS G CB  1 
ATOM   7236  C  CG  . LYS G  1 75  ? 159.451 -18.700 10.771 1.00 50.58  ? 75   LYS G CG  1 
ATOM   7237  C  CD  . LYS G  1 75  ? 159.452 -17.261 10.291 1.00 55.03  ? 75   LYS G CD  1 
ATOM   7238  C  CE  . LYS G  1 75  ? 160.719 -16.507 10.655 1.00 65.14  ? 75   LYS G CE  1 
ATOM   7239  N  NZ  . LYS G  1 75  ? 160.838 -15.221 9.896  1.00 69.04  ? 75   LYS G NZ  1 
ATOM   7240  N  N   . ASP G  1 76  ? 155.792 -20.515 8.512  1.00 66.52  ? 76   ASP G N   1 
ATOM   7241  C  CA  . ASP G  1 76  ? 155.114 -21.503 7.683  1.00 65.21  ? 76   ASP G CA  1 
ATOM   7242  C  C   . ASP G  1 76  ? 154.806 -20.915 6.312  1.00 67.50  ? 76   ASP G C   1 
ATOM   7243  O  O   . ASP G  1 76  ? 154.498 -19.739 6.139  1.00 74.41  ? 76   ASP G O   1 
ATOM   7244  C  CB  . ASP G  1 76  ? 153.854 -22.021 8.375  1.00 71.95  ? 76   ASP G CB  1 
ATOM   7245  C  CG  . ASP G  1 76  ? 154.125 -22.517 9.784  1.00 85.18  ? 76   ASP G CG  1 
ATOM   7246  O  OD1 . ASP G  1 76  ? 153.327 -23.341 10.290 1.00 101.06 ? 76   ASP G OD1 1 
ATOM   7247  O  OD2 . ASP G  1 76  ? 155.124 -22.105 10.408 1.00 92.76  ? 76   ASP G OD2 1 
ATOM   7248  N  N   . GLU G  1 77  ? 154.928 -21.780 5.317  1.00 75.62  ? 77   GLU G N   1 
ATOM   7249  C  CA  . GLU G  1 77  ? 154.735 -21.429 3.918  1.00 76.42  ? 77   GLU G CA  1 
ATOM   7250  C  C   . GLU G  1 77  ? 153.398 -20.754 3.678  1.00 68.68  ? 77   GLU G C   1 
ATOM   7251  O  O   . GLU G  1 77  ? 153.309 -19.700 3.048  1.00 68.66  ? 77   GLU G O   1 
ATOM   7252  C  CB  . GLU G  1 77  ? 154.867 -22.719 3.094  1.00 81.36  ? 77   GLU G CB  1 
ATOM   7253  C  CG  . GLU G  1 77  ? 155.508 -23.846 3.901  1.00 77.18  ? 77   GLU G CG  1 
ATOM   7254  C  CD  . GLU G  1 77  ? 155.512 -25.164 3.157  1.00 78.73  ? 77   GLU G CD  1 
ATOM   7255  O  OE1 . GLU G  1 77  ? 155.546 -25.144 1.906  1.00 68.28  ? 77   GLU G OE1 1 
ATOM   7256  O  OE2 . GLU G  1 77  ? 155.485 -26.219 3.829  1.00 59.69  ? 77   GLU G OE2 1 
ATOM   7257  N  N   . GLU G  1 78  ? 152.322 -21.357 4.183  1.00 65.64  ? 78   GLU G N   1 
ATOM   7258  C  CA  . GLU G  1 78  ? 151.001 -20.745 3.991  1.00 74.94  ? 78   GLU G CA  1 
ATOM   7259  C  C   . GLU G  1 78  ? 150.470 -20.209 5.320  1.00 71.87  ? 78   GLU G C   1 
ATOM   7260  O  O   . GLU G  1 78  ? 150.352 -20.923 6.315  1.00 65.53  ? 78   GLU G O   1 
ATOM   7261  C  CB  . GLU G  1 78  ? 150.043 -21.732 3.342  1.00 78.53  ? 78   GLU G CB  1 
ATOM   7262  C  CG  . GLU G  1 78  ? 149.280 -22.702 4.216  1.00 80.66  ? 78   GLU G CG  1 
ATOM   7263  C  CD  . GLU G  1 78  ? 148.021 -23.231 3.550  1.00 79.40  ? 78   GLU G CD  1 
ATOM   7264  O  OE1 . GLU G  1 78  ? 147.127 -22.410 3.250  1.00 78.79  ? 78   GLU G OE1 1 
ATOM   7265  O  OE2 . GLU G  1 78  ? 147.911 -24.456 3.333  1.00 75.38  ? 78   GLU G OE2 1 
ATOM   7266  N  N   . ARG G  1 79  ? 150.160 -18.917 5.323  1.00 65.47  ? 79   ARG G N   1 
ATOM   7267  C  CA  . ARG G  1 79  ? 149.745 -18.219 6.527  1.00 56.65  ? 79   ARG G CA  1 
ATOM   7268  C  C   . ARG G  1 79  ? 148.853 -17.017 6.250  1.00 55.41  ? 79   ARG G C   1 
ATOM   7269  O  O   . ARG G  1 79  ? 148.759 -16.506 5.135  1.00 50.76  ? 79   ARG G O   1 
ATOM   7270  C  CB  . ARG G  1 79  ? 150.987 -17.694 7.271  1.00 42.48  ? 79   ARG G CB  1 
ATOM   7271  C  CG  . ARG G  1 79  ? 151.762 -16.680 6.429  1.00 38.31  ? 79   ARG G CG  1 
ATOM   7272  C  CD  . ARG G  1 79  ? 152.957 -16.115 7.176  1.00 35.90  ? 79   ARG G CD  1 
ATOM   7273  N  NE  . ARG G  1 79  ? 152.597 -14.881 7.871  1.00 47.55  ? 79   ARG G NE  1 
ATOM   7274  C  CZ  . ARG G  1 79  ? 153.336 -14.107 8.637  1.00 43.45  ? 79   ARG G CZ  1 
ATOM   7275  N  NH1 . ARG G  1 79  ? 152.802 -13.007 9.180  1.00 42.68  ? 79   ARG G NH1 1 
ATOM   7276  N  NH2 . ARG G  1 79  ? 154.608 -14.380 8.886  1.00 40.88  ? 79   ARG G NH2 1 
ATOM   7277  N  N   . HIS G  1 80  ? 148.204 -16.554 7.314  1.00 50.12  ? 80   HIS G N   1 
ATOM   7278  C  CA  . HIS G  1 80  ? 147.560 -15.243 7.278  1.00 38.03  ? 80   HIS G CA  1 
ATOM   7279  C  C   . HIS G  1 80  ? 148.661 -14.196 7.406  1.00 37.04  ? 80   HIS G C   1 
ATOM   7280  O  O   . HIS G  1 80  ? 149.665 -14.415 8.087  1.00 43.18  ? 80   HIS G O   1 
ATOM   7281  C  CB  . HIS G  1 80  ? 146.560 -15.093 8.405  1.00 35.15  ? 80   HIS G CB  1 
ATOM   7282  C  CG  . HIS G  1 80  ? 145.459 -16.097 8.450  1.00 34.17  ? 80   HIS G CG  1 
ATOM   7283  N  ND1 . HIS G  1 80  ? 144.955 -16.603 9.627  1.00 40.55  ? 80   HIS G ND1 1 
ATOM   7284  C  CD2 . HIS G  1 80  ? 144.744 -16.689 7.478  1.00 41.11  ? 80   HIS G CD2 1 
ATOM   7285  C  CE1 . HIS G  1 80  ? 143.980 -17.462 9.363  1.00 47.64  ? 80   HIS G CE1 1 
ATOM   7286  N  NE2 . HIS G  1 80  ? 143.827 -17.532 8.049  1.00 47.30  ? 80   HIS G NE2 1 
ATOM   7287  N  N   . VAL G  1 81  ? 148.483 -13.062 6.750  1.00 40.34  ? 81   VAL G N   1 
ATOM   7288  C  CA  . VAL G  1 81  ? 149.415 -11.947 6.923  1.00 41.83  ? 81   VAL G CA  1 
ATOM   7289  C  C   . VAL G  1 81  ? 149.627 -11.635 8.391  1.00 29.86  ? 81   VAL G C   1 
ATOM   7290  O  O   . VAL G  1 81  ? 150.708 -11.343 8.884  1.00 45.15  ? 81   VAL G O   1 
ATOM   7291  C  CB  . VAL G  1 81  ? 148.860 -10.706 6.194  1.00 45.45  ? 81   VAL G CB  1 
ATOM   7292  C  CG1 . VAL G  1 81  ? 149.738 -9.499  6.464  1.00 35.57  ? 81   VAL G CG1 1 
ATOM   7293  C  CG2 . VAL G  1 81  ? 148.730 -11.003 4.703  1.00 39.85  ? 81   VAL G CG2 1 
ATOM   7294  N  N   . GLY G  1 82  ? 148.553 -11.702 9.179  1.00 34.05  ? 82   GLY G N   1 
ATOM   7295  C  CA  . GLY G  1 82  ? 148.742 -11.355 10.577 1.00 35.40  ? 82   GLY G CA  1 
ATOM   7296  C  C   . GLY G  1 82  ? 149.239 -12.443 11.495 1.00 41.23  ? 82   GLY G C   1 
ATOM   7297  O  O   . GLY G  1 82  ? 149.301 -12.165 12.701 1.00 38.98  ? 82   GLY G O   1 
ATOM   7298  N  N   . ASP G  1 83  ? 149.612 -13.638 11.032 1.00 45.41  ? 83   ASP G N   1 
ATOM   7299  C  CA  . ASP G  1 83  ? 149.996 -14.736 11.915 1.00 39.26  ? 83   ASP G CA  1 
ATOM   7300  C  C   . ASP G  1 83  ? 151.416 -14.601 12.441 1.00 35.47  ? 83   ASP G C   1 
ATOM   7301  O  O   . ASP G  1 83  ? 152.358 -14.836 11.690 1.00 40.17  ? 83   ASP G O   1 
ATOM   7302  C  CB  . ASP G  1 83  ? 149.877 -16.111 11.230 1.00 33.08  ? 83   ASP G CB  1 
ATOM   7303  C  CG  . ASP G  1 83  ? 148.436 -16.421 10.903 1.00 45.86  ? 83   ASP G CG  1 
ATOM   7304  O  OD1 . ASP G  1 83  ? 147.528 -15.900 11.595 1.00 41.94  ? 83   ASP G OD1 1 
ATOM   7305  O  OD2 . ASP G  1 83  ? 148.205 -17.180 9.937  1.00 48.55  ? 83   ASP G OD2 1 
ATOM   7306  N  N   . LEU G  1 84  ? 151.541 -14.246 13.716 1.00 30.53  ? 84   LEU G N   1 
ATOM   7307  C  CA  . LEU G  1 84  ? 152.827 -13.996 14.335 1.00 31.94  ? 84   LEU G CA  1 
ATOM   7308  C  C   . LEU G  1 84  ? 153.201 -15.040 15.392 1.00 29.84  ? 84   LEU G C   1 
ATOM   7309  O  O   . LEU G  1 84  ? 154.135 -14.828 16.171 1.00 36.86  ? 84   LEU G O   1 
ATOM   7310  C  CB  . LEU G  1 84  ? 152.855 -12.588 14.947 1.00 39.34  ? 84   LEU G CB  1 
ATOM   7311  C  CG  . LEU G  1 84  ? 152.698 -11.436 13.941 1.00 41.71  ? 84   LEU G CG  1 
ATOM   7312  C  CD1 . LEU G  1 84  ? 152.507 -10.101 14.654 1.00 40.21  ? 84   LEU G CD1 1 
ATOM   7313  C  CD2 . LEU G  1 84  ? 153.897 -11.378 13.005 1.00 30.98  ? 84   LEU G CD2 1 
ATOM   7314  N  N   . GLY G  1 85  ? 152.481 -16.151 15.381 1.00 34.17  ? 85   GLY G N   1 
ATOM   7315  C  CA  . GLY G  1 85  ? 152.756 -17.310 16.197 1.00 34.63  ? 85   GLY G CA  1 
ATOM   7316  C  C   . GLY G  1 85  ? 152.380 -17.192 17.660 1.00 38.03  ? 85   GLY G C   1 
ATOM   7317  O  O   . GLY G  1 85  ? 151.289 -16.745 18.015 1.00 37.54  ? 85   GLY G O   1 
ATOM   7318  N  N   . ASN G  1 86  ? 153.308 -17.612 18.508 1.00 32.46  ? 86   ASN G N   1 
ATOM   7319  C  CA  . ASN G  1 86  ? 153.157 -17.577 19.946 1.00 34.20  ? 86   ASN G CA  1 
ATOM   7320  C  C   . ASN G  1 86  ? 154.194 -16.668 20.579 1.00 33.09  ? 86   ASN G C   1 
ATOM   7321  O  O   . ASN G  1 86  ? 155.302 -16.575 20.053 1.00 39.85  ? 86   ASN G O   1 
ATOM   7322  C  CB  . ASN G  1 86  ? 153.333 -18.966 20.583 1.00 35.35  ? 86   ASN G CB  1 
ATOM   7323  C  CG  . ASN G  1 86  ? 152.205 -19.912 20.259 1.00 44.03  ? 86   ASN G CG  1 
ATOM   7324  O  OD1 . ASN G  1 86  ? 151.048 -19.700 20.629 1.00 41.50  ? 86   ASN G OD1 1 
ATOM   7325  N  ND2 . ASN G  1 86  ? 152.555 -20.985 19.551 1.00 46.65  ? 86   ASN G ND2 1 
ATOM   7326  N  N   . VAL G  1 87  ? 153.797 -16.074 21.694 1.00 24.84  ? 87   VAL G N   1 
ATOM   7327  C  CA  . VAL G  1 87  ? 154.723 -15.444 22.611 1.00 25.14  ? 87   VAL G CA  1 
ATOM   7328  C  C   . VAL G  1 87  ? 154.844 -16.373 23.840 1.00 27.27  ? 87   VAL G C   1 
ATOM   7329  O  O   . VAL G  1 87  ? 153.929 -17.170 24.008 1.00 30.40  ? 87   VAL G O   1 
ATOM   7330  C  CB  . VAL G  1 87  ? 154.308 -14.032 23.039 1.00 39.94  ? 87   VAL G CB  1 
ATOM   7331  C  CG1 . VAL G  1 87  ? 154.325 -13.068 21.861 1.00 38.87  ? 87   VAL G CG1 1 
ATOM   7332  C  CG2 . VAL G  1 87  ? 152.911 -14.032 23.664 1.00 35.84  ? 87   VAL G CG2 1 
ATOM   7333  N  N   . THR G  1 88  ? 155.897 -16.276 24.635 1.00 30.21  ? 88   THR G N   1 
ATOM   7334  C  CA  . THR G  1 88  ? 156.106 -17.146 25.784 1.00 30.73  ? 88   THR G CA  1 
ATOM   7335  C  C   . THR G  1 88  ? 156.197 -16.377 27.082 1.00 25.77  ? 88   THR G C   1 
ATOM   7336  O  O   . THR G  1 88  ? 157.044 -15.517 27.328 1.00 31.72  ? 88   THR G O   1 
ATOM   7337  C  CB  . THR G  1 88  ? 157.415 -17.968 25.637 1.00 42.13  ? 88   THR G CB  1 
ATOM   7338  O  OG1 . THR G  1 88  ? 157.182 -19.040 24.720 1.00 44.19  ? 88   THR G OG1 1 
ATOM   7339  C  CG2 . THR G  1 88  ? 157.798 -18.589 26.970 1.00 36.90  ? 88   THR G CG2 1 
ATOM   7340  N  N   . ALA G  1 89  ? 155.267 -16.683 28.006 1.00 29.44  ? 89   ALA G N   1 
ATOM   7341  C  CA  . ALA G  1 89  ? 155.366 -16.001 29.289 1.00 28.60  ? 89   ALA G CA  1 
ATOM   7342  C  C   . ALA G  1 89  ? 156.109 -16.903 30.280 1.00 33.89  ? 89   ALA G C   1 
ATOM   7343  O  O   . ALA G  1 89  ? 155.869 -18.114 30.324 1.00 32.87  ? 89   ALA G O   1 
ATOM   7344  C  CB  . ALA G  1 89  ? 153.999 -15.651 29.862 1.00 27.09  ? 89   ALA G CB  1 
ATOM   7345  N  N   . ASP G  1 90  ? 156.973 -16.252 31.040 1.00 32.24  ? 90   ASP G N   1 
ATOM   7346  C  CA  . ASP G  1 90  ? 157.780 -16.924 32.054 1.00 36.74  ? 90   ASP G CA  1 
ATOM   7347  C  C   . ASP G  1 90  ? 156.960 -17.256 33.292 1.00 46.34  ? 90   ASP G C   1 
ATOM   7348  O  O   . ASP G  1 90  ? 155.777 -16.936 33.394 1.00 36.57  ? 90   ASP G O   1 
ATOM   7349  C  CB  . ASP G  1 90  ? 158.972 -16.039 32.397 1.00 34.27  ? 90   ASP G CB  1 
ATOM   7350  C  CG  . ASP G  1 90  ? 158.653 -14.751 33.106 1.00 36.82  ? 90   ASP G CG  1 
ATOM   7351  O  OD1 . ASP G  1 90  ? 159.537 -13.861 33.157 1.00 42.32  ? 90   ASP G OD1 1 
ATOM   7352  O  OD2 . ASP G  1 90  ? 157.543 -14.548 33.637 1.00 37.67  ? 90   ASP G OD2 1 
ATOM   7353  N  N   . LYS G  1 91  ? 157.580 -17.890 34.278 1.00 42.07  ? 91   LYS G N   1 
ATOM   7354  C  CA  . LYS G  1 91  ? 156.868 -18.227 35.507 1.00 40.04  ? 91   LYS G CA  1 
ATOM   7355  C  C   . LYS G  1 91  ? 156.310 -17.005 36.221 1.00 37.73  ? 91   LYS G C   1 
ATOM   7356  O  O   . LYS G  1 91  ? 155.394 -17.199 37.025 1.00 44.72  ? 91   LYS G O   1 
ATOM   7357  C  CB  . LYS G  1 91  ? 157.816 -19.011 36.436 1.00 38.22  ? 91   LYS G CB  1 
ATOM   7358  C  CG  . LYS G  1 91  ? 158.886 -18.130 37.058 1.00 49.67  ? 91   LYS G CG  1 
ATOM   7359  C  CD  . LYS G  1 91  ? 160.066 -18.925 37.589 1.00 63.88  ? 91   LYS G CD  1 
ATOM   7360  C  CE  . LYS G  1 91  ? 161.274 -18.027 37.832 1.00 68.55  ? 91   LYS G CE  1 
ATOM   7361  N  NZ  . LYS G  1 91  ? 162.485 -18.506 37.105 1.00 97.70  ? 91   LYS G NZ  1 
ATOM   7362  N  N   . ASP G  1 92  ? 156.794 -15.791 35.973 1.00 39.74  ? 92   ASP G N   1 
ATOM   7363  C  CA  . ASP G  1 92  ? 156.252 -14.567 36.546 1.00 36.49  ? 92   ASP G CA  1 
ATOM   7364  C  C   . ASP G  1 92  ? 155.132 -13.955 35.698 1.00 31.41  ? 92   ASP G C   1 
ATOM   7365  O  O   . ASP G  1 92  ? 154.739 -12.823 35.993 1.00 35.79  ? 92   ASP G O   1 
ATOM   7366  C  CB  . ASP G  1 92  ? 157.290 -13.459 36.729 1.00 37.91  ? 92   ASP G CB  1 
ATOM   7367  C  CG  . ASP G  1 92  ? 158.317 -13.827 37.783 1.00 59.65  ? 92   ASP G CG  1 
ATOM   7368  O  OD1 . ASP G  1 92  ? 157.904 -14.460 38.779 1.00 81.02  ? 92   ASP G OD1 1 
ATOM   7369  O  OD2 . ASP G  1 92  ? 159.505 -13.493 37.602 1.00 55.56  ? 92   ASP G OD2 1 
ATOM   7370  N  N   . GLY G  1 93  ? 154.642 -14.663 34.698 1.00 30.93  ? 93   GLY G N   1 
ATOM   7371  C  CA  . GLY G  1 93  ? 153.541 -14.155 33.890 1.00 30.33  ? 93   GLY G CA  1 
ATOM   7372  C  C   . GLY G  1 93  ? 153.967 -13.122 32.866 1.00 36.33  ? 93   GLY G C   1 
ATOM   7373  O  O   . GLY G  1 93  ? 153.122 -12.500 32.221 1.00 30.43  ? 93   GLY G O   1 
ATOM   7374  N  N   . VAL G  1 94  ? 155.272 -12.910 32.695 1.00 36.30  ? 94   VAL G N   1 
ATOM   7375  C  CA  . VAL G  1 94  ? 155.748 -11.895 31.758 1.00 37.47  ? 94   VAL G CA  1 
ATOM   7376  C  C   . VAL G  1 94  ? 156.284 -12.487 30.465 1.00 43.21  ? 94   VAL G C   1 
ATOM   7377  O  O   . VAL G  1 94  ? 157.202 -13.321 30.480 1.00 41.02  ? 94   VAL G O   1 
ATOM   7378  C  CB  . VAL G  1 94  ? 156.883 -11.073 32.398 1.00 34.23  ? 94   VAL G CB  1 
ATOM   7379  C  CG1 . VAL G  1 94  ? 157.472 -10.095 31.387 1.00 50.57  ? 94   VAL G CG1 1 
ATOM   7380  C  CG2 . VAL G  1 94  ? 156.398 -10.325 33.623 1.00 38.47  ? 94   VAL G CG2 1 
ATOM   7381  N  N   . ALA G  1 95  ? 155.732 -12.069 29.337 1.00 34.98  ? 95   ALA G N   1 
ATOM   7382  C  CA  . ALA G  1 95  ? 156.255 -12.484 28.037 1.00 28.70  ? 95   ALA G CA  1 
ATOM   7383  C  C   . ALA G  1 95  ? 157.176 -11.391 27.521 1.00 36.96  ? 95   ALA G C   1 
ATOM   7384  O  O   . ALA G  1 95  ? 156.831 -10.217 27.352 1.00 36.69  ? 95   ALA G O   1 
ATOM   7385  C  CB  . ALA G  1 95  ? 155.167 -12.768 27.023 1.00 30.40  ? 95   ALA G CB  1 
ATOM   7386  N  N   . ASP G  1 96  ? 158.428 -11.735 27.241 1.00 35.00  ? 96   ASP G N   1 
ATOM   7387  C  CA  . ASP G  1 96  ? 159.241 -10.688 26.597 1.00 40.19  ? 96   ASP G CA  1 
ATOM   7388  C  C   . ASP G  1 96  ? 159.314 -11.020 25.118 1.00 37.13  ? 96   ASP G C   1 
ATOM   7389  O  O   . ASP G  1 96  ? 159.674 -12.105 24.661 1.00 37.77  ? 96   ASP G O   1 
ATOM   7390  C  CB  . ASP G  1 96  ? 160.554 -10.548 27.362 1.00 53.36  ? 96   ASP G CB  1 
ATOM   7391  C  CG  . ASP G  1 96  ? 160.270 -9.702  28.607 1.00 68.78  ? 96   ASP G CG  1 
ATOM   7392  O  OD1 . ASP G  1 96  ? 159.345 -8.864  28.526 1.00 65.95  ? 96   ASP G OD1 1 
ATOM   7393  O  OD2 . ASP G  1 96  ? 160.941 -9.869  29.643 1.00 94.83  ? 96   ASP G OD2 1 
ATOM   7394  N  N   . VAL G  1 97  ? 158.903 -10.063 24.302 1.00 31.09  ? 97   VAL G N   1 
ATOM   7395  C  CA  . VAL G  1 97  ? 158.717 -10.296 22.875 1.00 30.47  ? 97   VAL G CA  1 
ATOM   7396  C  C   . VAL G  1 97  ? 159.843 -9.685  22.050 1.00 30.72  ? 97   VAL G C   1 
ATOM   7397  O  O   . VAL G  1 97  ? 160.213 -8.517  22.249 1.00 37.43  ? 97   VAL G O   1 
ATOM   7398  C  CB  . VAL G  1 97  ? 157.376 -9.677  22.423 1.00 38.74  ? 97   VAL G CB  1 
ATOM   7399  C  CG1 . VAL G  1 97  ? 157.218 -9.770  20.916 1.00 36.30  ? 97   VAL G CG1 1 
ATOM   7400  C  CG2 . VAL G  1 97  ? 156.200 -10.332 23.144 1.00 34.70  ? 97   VAL G CG2 1 
ATOM   7401  N  N   . SER G  1 98  ? 160.389 -10.469 21.126 1.00 41.47  ? 98   SER G N   1 
ATOM   7402  C  CA  . SER G  1 98  ? 161.419 -10.000 20.200 1.00 38.93  ? 98   SER G CA  1 
ATOM   7403  C  C   . SER G  1 98  ? 161.357 -10.822 18.908 1.00 47.29  ? 98   SER G C   1 
ATOM   7404  O  O   . SER G  1 98  ? 162.101 -11.794 18.805 1.00 57.72  ? 98   SER G O   1 
ATOM   7405  C  CB  . SER G  1 98  ? 162.829 -10.073 20.767 1.00 50.80  ? 98   SER G CB  1 
ATOM   7406  O  OG  . SER G  1 98  ? 163.719 -9.262  20.007 1.00 69.44  ? 98   SER G OG  1 
ATOM   7407  N  N   . ILE G  1 99  ? 160.467 -10.394 18.031 1.00 36.18  ? 99   ILE G N   1 
ATOM   7408  C  CA  . ILE G  1 99  ? 160.046 -11.083 16.817 1.00 38.04  ? 99   ILE G CA  1 
ATOM   7409  C  C   . ILE G  1 99  ? 160.559 -10.317 15.602 1.00 44.77  ? 99   ILE G C   1 
ATOM   7410  O  O   . ILE G  1 99  ? 160.768 -9.108  15.709 1.00 41.95  ? 99   ILE G O   1 
ATOM   7411  C  CB  . ILE G  1 99  ? 158.517 -11.205 16.753 1.00 39.00  ? 99   ILE G CB  1 
ATOM   7412  C  CG1 . ILE G  1 99  ? 157.929 -12.131 17.837 1.00 49.90  ? 99   ILE G CG1 1 
ATOM   7413  C  CG2 . ILE G  1 99  ? 157.988 -11.655 15.402 1.00 45.27  ? 99   ILE G CG2 1 
ATOM   7414  C  CD1 . ILE G  1 99  ? 158.959 -13.110 18.360 1.00 82.44  ? 99   ILE G CD1 1 
ATOM   7415  N  N   . GLU G  1 100 ? 160.769 -11.005 14.491 1.00 40.76  ? 100  GLU G N   1 
ATOM   7416  C  CA  . GLU G  1 100 ? 161.094 -10.331 13.232 1.00 44.41  ? 100  GLU G CA  1 
ATOM   7417  C  C   . GLU G  1 100 ? 160.250 -10.986 12.151 1.00 44.78  ? 100  GLU G C   1 
ATOM   7418  O  O   . GLU G  1 100 ? 160.363 -12.202 11.967 1.00 42.17  ? 100  GLU G O   1 
ATOM   7419  C  CB  . GLU G  1 100 ? 162.577 -10.427 12.934 1.00 59.71  ? 100  GLU G CB  1 
ATOM   7420  C  CG  . GLU G  1 100 ? 163.322 -9.133  12.682 1.00 65.53  ? 100  GLU G CG  1 
ATOM   7421  C  CD  . GLU G  1 100 ? 164.409 -9.308  11.638 1.00 81.87  ? 100  GLU G CD  1 
ATOM   7422  O  OE1 . GLU G  1 100 ? 165.574 -8.963  11.933 1.00 92.97  ? 100  GLU G OE1 1 
ATOM   7423  O  OE2 . GLU G  1 100 ? 164.109 -9.796  10.525 1.00 96.79  ? 100  GLU G OE2 1 
ATOM   7424  N  N   . ASP G  1 101 ? 159.399 -10.226 11.472 1.00 41.84  ? 101  ASP G N   1 
ATOM   7425  C  CA  . ASP G  1 101 ? 158.550 -10.809 10.440 1.00 42.47  ? 101  ASP G CA  1 
ATOM   7426  C  C   . ASP G  1 101 ? 158.764 -10.068 9.123  1.00 49.59  ? 101  ASP G C   1 
ATOM   7427  O  O   . ASP G  1 101 ? 159.358 -8.991  9.145  1.00 50.44  ? 101  ASP G O   1 
ATOM   7428  C  CB  . ASP G  1 101 ? 157.079 -10.748 10.830 1.00 36.37  ? 101  ASP G CB  1 
ATOM   7429  C  CG  . ASP G  1 101 ? 156.185 -11.574 9.932  1.00 45.48  ? 101  ASP G CG  1 
ATOM   7430  O  OD1 . ASP G  1 101 ? 155.507 -10.991 9.058  1.00 38.73  ? 101  ASP G OD1 1 
ATOM   7431  O  OD2 . ASP G  1 101 ? 156.137 -12.816 10.086 1.00 57.18  ? 101  ASP G OD2 1 
ATOM   7432  N  N   . SER G  1 102 ? 158.288 -10.631 8.019  1.00 46.27  ? 102  SER G N   1 
ATOM   7433  C  CA  . SER G  1 102 ? 158.537 -10.028 6.714  1.00 41.38  ? 102  SER G CA  1 
ATOM   7434  C  C   . SER G  1 102 ? 157.307 -10.095 5.831  1.00 42.37  ? 102  SER G C   1 
ATOM   7435  O  O   . SER G  1 102 ? 157.340 -9.634  4.689  1.00 58.14  ? 102  SER G O   1 
ATOM   7436  C  CB  . SER G  1 102 ? 159.717 -10.740 6.037  1.00 58.53  ? 102  SER G CB  1 
ATOM   7437  O  OG  . SER G  1 102 ? 160.942 -10.296 6.599  1.00 65.70  ? 102  SER G OG  1 
ATOM   7438  N  N   . VAL G  1 103 ? 156.238 -10.664 6.380  1.00 32.88  ? 103  VAL G N   1 
ATOM   7439  C  CA  . VAL G  1 103 ? 154.935 -10.694 5.732  1.00 40.05  ? 103  VAL G CA  1 
ATOM   7440  C  C   . VAL G  1 103 ? 154.111 -9.475  6.159  1.00 40.86  ? 103  VAL G C   1 
ATOM   7441  O  O   . VAL G  1 103 ? 153.516 -8.804  5.317  1.00 45.95  ? 103  VAL G O   1 
ATOM   7442  C  CB  . VAL G  1 103 ? 154.202 -12.005 6.037  1.00 34.93  ? 103  VAL G CB  1 
ATOM   7443  C  CG1 . VAL G  1 103 ? 152.804 -12.017 5.452  1.00 49.14  ? 103  VAL G CG1 1 
ATOM   7444  C  CG2 . VAL G  1 103 ? 155.014 -13.179 5.488  1.00 54.97  ? 103  VAL G CG2 1 
ATOM   7445  N  N   . ILE G  1 104 ? 154.074 -9.154  7.454  1.00 42.86  ? 104  ILE G N   1 
ATOM   7446  C  CA  . ILE G  1 104 ? 153.378 -7.929  7.866  1.00 40.10  ? 104  ILE G CA  1 
ATOM   7447  C  C   . ILE G  1 104 ? 154.184 -6.731  7.382  1.00 46.96  ? 104  ILE G C   1 
ATOM   7448  O  O   . ILE G  1 104 ? 155.341 -6.940  6.990  1.00 44.12  ? 104  ILE G O   1 
ATOM   7449  C  CB  . ILE G  1 104 ? 153.213 -7.856  9.394  1.00 33.33  ? 104  ILE G CB  1 
ATOM   7450  C  CG1 . ILE G  1 104 ? 154.536 -7.746  10.129 1.00 29.09  ? 104  ILE G CG1 1 
ATOM   7451  C  CG2 . ILE G  1 104 ? 152.397 -9.038  9.887  1.00 41.90  ? 104  ILE G CG2 1 
ATOM   7452  C  CD1 . ILE G  1 104 ? 154.489 -7.430  11.604 1.00 35.26  ? 104  ILE G CD1 1 
ATOM   7453  N  N   . SER G  1 105 ? 153.655 -5.515  7.380  1.00 39.51  ? 105  SER G N   1 
ATOM   7454  C  CA  . SER G  1 105 ? 154.459 -4.327  7.067  1.00 32.96  ? 105  SER G CA  1 
ATOM   7455  C  C   . SER G  1 105 ? 153.806 -3.097  7.695  1.00 33.17  ? 105  SER G C   1 
ATOM   7456  O  O   . SER G  1 105 ? 152.658 -3.197  8.145  1.00 32.83  ? 105  SER G O   1 
ATOM   7457  C  CB  . SER G  1 105 ? 154.625 -4.128  5.561  1.00 41.10  ? 105  SER G CB  1 
ATOM   7458  O  OG  . SER G  1 105 ? 155.502 -3.061  5.240  1.00 47.66  ? 105  SER G OG  1 
ATOM   7459  N  N   . LEU G  1 106 ? 154.529 -1.990  7.723  1.00 37.06  ? 106  LEU G N   1 
ATOM   7460  C  CA  . LEU G  1 106 ? 153.998 -0.732  8.248  1.00 34.50  ? 106  LEU G CA  1 
ATOM   7461  C  C   . LEU G  1 106 ? 153.623 0.187   7.081  1.00 47.23  ? 106  LEU G C   1 
ATOM   7462  O  O   . LEU G  1 106 ? 153.416 1.389   7.230  1.00 48.94  ? 106  LEU G O   1 
ATOM   7463  C  CB  . LEU G  1 106 ? 154.985 -0.094  9.220  1.00 34.04  ? 106  LEU G CB  1 
ATOM   7464  C  CG  . LEU G  1 106 ? 155.469 -0.991  10.376 1.00 33.42  ? 106  LEU G CG  1 
ATOM   7465  C  CD1 . LEU G  1 106 ? 156.298 -0.203  11.366 1.00 33.34  ? 106  LEU G CD1 1 
ATOM   7466  C  CD2 . LEU G  1 106 ? 154.329 -1.677  11.109 1.00 38.73  ? 106  LEU G CD2 1 
ATOM   7467  N  N   . SER G  1 107 ? 153.519 -0.442  5.917  1.00 52.98  ? 107  SER G N   1 
ATOM   7468  C  CA  . SER G  1 107 ? 153.058 0.126   4.675  1.00 58.60  ? 107  SER G CA  1 
ATOM   7469  C  C   . SER G  1 107 ? 152.553 -0.920  3.683  1.00 56.91  ? 107  SER G C   1 
ATOM   7470  O  O   . SER G  1 107 ? 152.968 -2.075  3.742  1.00 65.34  ? 107  SER G O   1 
ATOM   7471  C  CB  . SER G  1 107 ? 154.192 0.902   3.983  1.00 63.56  ? 107  SER G CB  1 
ATOM   7472  O  OG  . SER G  1 107 ? 153.685 1.377   2.742  1.00 94.56  ? 107  SER G OG  1 
ATOM   7473  N  N   . GLY G  1 108 ? 151.676 -0.510  2.768  1.00 53.04  ? 108  GLY G N   1 
ATOM   7474  C  CA  . GLY G  1 108 ? 151.216 -1.329  1.678  1.00 46.24  ? 108  GLY G CA  1 
ATOM   7475  C  C   . GLY G  1 108 ? 149.889 -2.016  1.905  1.00 63.20  ? 108  GLY G C   1 
ATOM   7476  O  O   . GLY G  1 108 ? 149.122 -1.649  2.802  1.00 51.66  ? 108  GLY G O   1 
ATOM   7477  N  N   . ASP G  1 109 ? 149.606 -3.024  1.069  1.00 63.68  ? 109  ASP G N   1 
ATOM   7478  C  CA  . ASP G  1 109 ? 148.334 -3.735  1.190  1.00 63.55  ? 109  ASP G CA  1 
ATOM   7479  C  C   . ASP G  1 109 ? 148.372 -4.628  2.435  1.00 54.09  ? 109  ASP G C   1 
ATOM   7480  O  O   . ASP G  1 109 ? 147.310 -4.955  2.965  1.00 48.83  ? 109  ASP G O   1 
ATOM   7481  C  CB  . ASP G  1 109 ? 148.014 -4.566  -0.048 1.00 74.49  ? 109  ASP G CB  1 
ATOM   7482  C  CG  . ASP G  1 109 ? 146.770 -4.145  -0.806 1.00 85.37  ? 109  ASP G CG  1 
ATOM   7483  O  OD1 . ASP G  1 109 ? 146.242 -3.033  -0.588 1.00 87.56  ? 109  ASP G OD1 1 
ATOM   7484  O  OD2 . ASP G  1 109 ? 146.285 -4.934  -1.652 1.00 94.95  ? 109  ASP G OD2 1 
ATOM   7485  N  N   . HIS G  1 110 ? 149.586 -4.981  2.833  1.00 40.72  ? 110  HIS G N   1 
ATOM   7486  C  CA  . HIS G  1 110 ? 149.829 -5.802  4.015  1.00 48.54  ? 110  HIS G CA  1 
ATOM   7487  C  C   . HIS G  1 110 ? 150.045 -4.910  5.231  1.00 45.40  ? 110  HIS G C   1 
ATOM   7488  O  O   . HIS G  1 110 ? 150.545 -5.330  6.278  1.00 46.44  ? 110  HIS G O   1 
ATOM   7489  C  CB  . HIS G  1 110 ? 151.034 -6.735  3.816  1.00 43.21  ? 110  HIS G CB  1 
ATOM   7490  C  CG  . HIS G  1 110 ? 150.727 -7.844  2.845  1.00 60.18  ? 110  HIS G CG  1 
ATOM   7491  N  ND1 . HIS G  1 110 ? 151.486 -8.988  2.731  1.00 60.32  ? 110  HIS G ND1 1 
ATOM   7492  C  CD2 . HIS G  1 110 ? 149.726 -7.985  1.938  1.00 58.58  ? 110  HIS G CD2 1 
ATOM   7493  C  CE1 . HIS G  1 110 ? 150.977 -9.782  1.802  1.00 52.23  ? 110  HIS G CE1 1 
ATOM   7494  N  NE2 . HIS G  1 110 ? 149.899 -9.194  1.301  1.00 56.32  ? 110  HIS G NE2 1 
ATOM   7495  N  N   . CYS G  1 111 ? 149.664 -3.637  5.083  1.00 39.96  ? 111  CYS G N   1 
ATOM   7496  C  CA  . CYS G  1 111 ? 149.964 -2.733  6.200  1.00 39.41  ? 111  CYS G CA  1 
ATOM   7497  C  C   . CYS G  1 111 ? 149.127 -3.131  7.416  1.00 31.11  ? 111  CYS G C   1 
ATOM   7498  O  O   . CYS G  1 111 ? 147.950 -3.479  7.271  1.00 39.43  ? 111  CYS G O   1 
ATOM   7499  C  CB  . CYS G  1 111 ? 149.714 -1.282  5.803  1.00 42.17  ? 111  CYS G CB  1 
ATOM   7500  S  SG  . CYS G  1 111 ? 150.114 -0.069  7.084  1.00 47.44  ? 111  CYS G SG  1 
ATOM   7501  N  N   . ILE G  1 112 ? 149.749 -3.078  8.591  1.00 33.25  ? 112  ILE G N   1 
ATOM   7502  C  CA  . ILE G  1 112 ? 149.046 -3.426  9.821  1.00 38.76  ? 112  ILE G CA  1 
ATOM   7503  C  C   . ILE G  1 112 ? 148.704 -2.209  10.676 1.00 42.79  ? 112  ILE G C   1 
ATOM   7504  O  O   . ILE G  1 112 ? 148.081 -2.365  11.723 1.00 27.82  ? 112  ILE G O   1 
ATOM   7505  C  CB  . ILE G  1 112 ? 149.860 -4.405  10.689 1.00 36.40  ? 112  ILE G CB  1 
ATOM   7506  C  CG1 . ILE G  1 112 ? 151.137 -3.810  11.282 1.00 33.84  ? 112  ILE G CG1 1 
ATOM   7507  C  CG2 . ILE G  1 112 ? 150.169 -5.678  9.912  1.00 33.29  ? 112  ILE G CG2 1 
ATOM   7508  C  CD1 . ILE G  1 112 ? 151.842 -4.804  12.193 1.00 33.40  ? 112  ILE G CD1 1 
ATOM   7509  N  N   . ILE G  1 113 ? 149.078 -0.999  10.280 1.00 39.66  ? 113  ILE G N   1 
ATOM   7510  C  CA  . ILE G  1 113 ? 148.725 0.168   11.105 1.00 32.84  ? 113  ILE G CA  1 
ATOM   7511  C  C   . ILE G  1 113 ? 147.236 0.390   11.051 1.00 31.70  ? 113  ILE G C   1 
ATOM   7512  O  O   . ILE G  1 113 ? 146.608 0.277   10.000 1.00 29.19  ? 113  ILE G O   1 
ATOM   7513  C  CB  . ILE G  1 113 ? 149.490 1.416   10.634 1.00 32.31  ? 113  ILE G CB  1 
ATOM   7514  C  CG1 . ILE G  1 113 ? 150.986 1.348   10.958 1.00 39.43  ? 113  ILE G CG1 1 
ATOM   7515  C  CG2 . ILE G  1 113 ? 148.875 2.692   11.199 1.00 32.13  ? 113  ILE G CG2 1 
ATOM   7516  C  CD1 . ILE G  1 113 ? 151.836 2.273   10.121 1.00 55.50  ? 113  ILE G CD1 1 
ATOM   7517  N  N   . GLY G  1 114 ? 146.611 0.693   12.192 1.00 29.49  ? 114  GLY G N   1 
ATOM   7518  C  CA  . GLY G  1 114 ? 145.178 0.805   12.177 1.00 24.61  ? 114  GLY G CA  1 
ATOM   7519  C  C   . GLY G  1 114 ? 144.466 -0.503  12.384 1.00 27.65  ? 114  GLY G C   1 
ATOM   7520  O  O   . GLY G  1 114 ? 143.238 -0.561  12.402 1.00 30.73  ? 114  GLY G O   1 
ATOM   7521  N  N   . ARG G  1 115 ? 145.216 -1.597  12.534 1.00 29.33  ? 115  ARG G N   1 
ATOM   7522  C  CA  . ARG G  1 115 ? 144.500 -2.861  12.793 1.00 27.70  ? 115  ARG G CA  1 
ATOM   7523  C  C   . ARG G  1 115 ? 144.778 -3.258  14.244 1.00 29.92  ? 115  ARG G C   1 
ATOM   7524  O  O   . ARG G  1 115 ? 145.419 -2.447  14.921 1.00 30.06  ? 115  ARG G O   1 
ATOM   7525  C  CB  . ARG G  1 115 ? 144.928 -3.954  11.807 1.00 35.73  ? 115  ARG G CB  1 
ATOM   7526  C  CG  . ARG G  1 115 ? 145.128 -3.453  10.375 1.00 32.26  ? 115  ARG G CG  1 
ATOM   7527  C  CD  . ARG G  1 115 ? 145.056 -4.580  9.361  1.00 34.72  ? 115  ARG G CD  1 
ATOM   7528  N  NE  . ARG G  1 115 ? 144.866 -4.109  7.989  1.00 35.92  ? 115  ARG G NE  1 
ATOM   7529  C  CZ  . ARG G  1 115 ? 143.707 -4.029  7.348  1.00 29.36  ? 115  ARG G CZ  1 
ATOM   7530  N  NH1 . ARG G  1 115 ? 143.681 -3.583  6.090  1.00 36.52  ? 115  ARG G NH1 1 
ATOM   7531  N  NH2 . ARG G  1 115 ? 142.560 -4.382  7.907  1.00 35.45  ? 115  ARG G NH2 1 
ATOM   7532  N  N   . THR G  1 116 ? 144.339 -4.431  14.696 1.00 28.40  ? 116  THR G N   1 
ATOM   7533  C  CA  . THR G  1 116 ? 144.486 -4.775  16.109 1.00 24.62  ? 116  THR G CA  1 
ATOM   7534  C  C   . THR G  1 116 ? 145.430 -5.929  16.430 1.00 30.75  ? 116  THR G C   1 
ATOM   7535  O  O   . THR G  1 116 ? 145.279 -6.976  15.804 1.00 28.66  ? 116  THR G O   1 
ATOM   7536  C  CB  . THR G  1 116 ? 143.094 -5.176  16.615 1.00 27.72  ? 116  THR G CB  1 
ATOM   7537  O  OG1 . THR G  1 116 ? 142.295 -3.986  16.521 1.00 28.85  ? 116  THR G OG1 1 
ATOM   7538  C  CG2 . THR G  1 116 ? 143.163 -5.617  18.064 1.00 28.36  ? 116  THR G CG2 1 
ATOM   7539  N  N   . LEU G  1 117 ? 146.344 -5.721  17.373 1.00 26.16  ? 117  LEU G N   1 
ATOM   7540  C  CA  . LEU G  1 117 ? 147.205 -6.813  17.874 1.00 28.07  ? 117  LEU G CA  1 
ATOM   7541  C  C   . LEU G  1 117 ? 146.462 -7.509  19.015 1.00 34.56  ? 117  LEU G C   1 
ATOM   7542  O  O   . LEU G  1 117 ? 145.904 -6.815  19.886 1.00 27.46  ? 117  LEU G O   1 
ATOM   7543  C  CB  . LEU G  1 117 ? 148.526 -6.257  18.331 1.00 24.94  ? 117  LEU G CB  1 
ATOM   7544  C  CG  . LEU G  1 117 ? 149.690 -7.151  18.739 1.00 25.93  ? 117  LEU G CG  1 
ATOM   7545  C  CD1 . LEU G  1 117 ? 150.148 -8.015  17.569 1.00 30.31  ? 117  LEU G CD1 1 
ATOM   7546  C  CD2 . LEU G  1 117 ? 150.860 -6.327  19.254 1.00 27.31  ? 117  LEU G CD2 1 
ATOM   7547  N  N   . VAL G  1 118 ? 146.444 -8.831  18.983 1.00 23.01  ? 118  VAL G N   1 
ATOM   7548  C  CA  . VAL G  1 118 ? 145.702 -9.631  19.960 1.00 22.14  ? 118  VAL G CA  1 
ATOM   7549  C  C   . VAL G  1 118 ? 146.607 -10.700 20.581 1.00 30.90  ? 118  VAL G C   1 
ATOM   7550  O  O   . VAL G  1 118 ? 147.322 -11.400 19.861 1.00 28.17  ? 118  VAL G O   1 
ATOM   7551  C  CB  . VAL G  1 118 ? 144.478 -10.304 19.333 1.00 26.88  ? 118  VAL G CB  1 
ATOM   7552  C  CG1 . VAL G  1 118 ? 143.674 -11.141 20.332 1.00 29.49  ? 118  VAL G CG1 1 
ATOM   7553  C  CG2 . VAL G  1 118 ? 143.545 -9.274  18.703 1.00 35.49  ? 118  VAL G CG2 1 
ATOM   7554  N  N   . VAL G  1 119 ? 146.588 -10.821 21.907 1.00 31.83  ? 119  VAL G N   1 
ATOM   7555  C  CA  . VAL G  1 119 ? 147.300 -11.927 22.586 1.00 23.47  ? 119  VAL G CA  1 
ATOM   7556  C  C   . VAL G  1 119 ? 146.214 -12.824 23.144 1.00 35.63  ? 119  VAL G C   1 
ATOM   7557  O  O   . VAL G  1 119 ? 145.160 -12.371 23.610 1.00 31.84  ? 119  VAL G O   1 
ATOM   7558  C  CB  . VAL G  1 119 ? 148.287 -11.447 23.646 1.00 31.14  ? 119  VAL G CB  1 
ATOM   7559  C  CG1 . VAL G  1 119 ? 147.591 -10.685 24.770 1.00 27.86  ? 119  VAL G CG1 1 
ATOM   7560  C  CG2 . VAL G  1 119 ? 149.095 -12.621 24.222 1.00 28.63  ? 119  VAL G CG2 1 
ATOM   7561  N  N   . HIS G  1 120 ? 146.458 -14.132 23.051 1.00 35.15  ? 120  HIS G N   1 
ATOM   7562  C  CA  . HIS G  1 120 ? 145.371 -15.063 23.348 1.00 30.88  ? 120  HIS G CA  1 
ATOM   7563  C  C   . HIS G  1 120 ? 145.632 -15.877 24.629 1.00 37.47  ? 120  HIS G C   1 
ATOM   7564  O  O   . HIS G  1 120 ? 146.703 -15.849 25.241 1.00 29.90  ? 120  HIS G O   1 
ATOM   7565  C  CB  . HIS G  1 120 ? 145.135 -15.994 22.176 1.00 28.01  ? 120  HIS G CB  1 
ATOM   7566  C  CG  . HIS G  1 120 ? 144.531 -15.420 20.938 1.00 28.42  ? 120  HIS G CG  1 
ATOM   7567  N  ND1 . HIS G  1 120 ? 143.219 -15.601 20.594 1.00 36.57  ? 120  HIS G ND1 1 
ATOM   7568  C  CD2 . HIS G  1 120 ? 145.082 -14.667 19.942 1.00 31.23  ? 120  HIS G CD2 1 
ATOM   7569  C  CE1 . HIS G  1 120 ? 142.966 -14.986 19.446 1.00 37.89  ? 120  HIS G CE1 1 
ATOM   7570  N  NE2 . HIS G  1 120 ? 144.088 -14.414 19.039 1.00 30.88  ? 120  HIS G NE2 1 
ATOM   7571  N  N   . GLU G  1 121 ? 144.552 -16.568 24.961 1.00 33.56  ? 121  GLU G N   1 
ATOM   7572  C  CA  . GLU G  1 121 ? 144.398 -17.472 26.076 1.00 34.70  ? 121  GLU G CA  1 
ATOM   7573  C  C   . GLU G  1 121 ? 145.290 -18.698 25.910 1.00 44.78  ? 121  GLU G C   1 
ATOM   7574  O  O   . GLU G  1 121 ? 146.042 -19.075 26.803 1.00 47.76  ? 121  GLU G O   1 
ATOM   7575  C  CB  . GLU G  1 121 ? 142.936 -17.918 26.181 1.00 39.76  ? 121  GLU G CB  1 
ATOM   7576  C  CG  . GLU G  1 121 ? 142.659 -18.743 27.428 1.00 49.59  ? 121  GLU G CG  1 
ATOM   7577  C  CD  . GLU G  1 121 ? 141.491 -19.686 27.232 1.00 59.15  ? 121  GLU G CD  1 
ATOM   7578  O  OE1 . GLU G  1 121 ? 140.963 -19.755 26.101 1.00 49.67  ? 121  GLU G OE1 1 
ATOM   7579  O  OE2 . GLU G  1 121 ? 141.121 -20.352 28.223 1.00 67.55  ? 121  GLU G OE2 1 
ATOM   7580  N  N   . LYS G  1 122 ? 145.206 -19.346 24.746 1.00 40.80  ? 122  LYS G N   1 
ATOM   7581  C  CA  . LYS G  1 122 ? 145.972 -20.575 24.586 1.00 47.91  ? 122  LYS G CA  1 
ATOM   7582  C  C   . LYS G  1 122 ? 147.120 -20.432 23.595 1.00 49.06  ? 122  LYS G C   1 
ATOM   7583  O  O   . LYS G  1 122 ? 147.376 -19.402 22.980 1.00 42.47  ? 122  LYS G O   1 
ATOM   7584  C  CB  . LYS G  1 122 ? 145.046 -21.697 24.102 1.00 45.75  ? 122  LYS G CB  1 
ATOM   7585  C  CG  . LYS G  1 122 ? 143.775 -21.865 24.913 1.00 52.79  ? 122  LYS G CG  1 
ATOM   7586  C  CD  . LYS G  1 122 ? 143.012 -23.109 24.468 1.00 57.46  ? 122  LYS G CD  1 
ATOM   7587  C  CE  . LYS G  1 122 ? 141.812 -23.342 25.381 1.00 76.10  ? 122  LYS G CE  1 
ATOM   7588  N  NZ  . LYS G  1 122 ? 142.218 -23.370 26.820 1.00 104.43 ? 122  LYS G NZ  1 
ATOM   7589  N  N   . ALA G  1 123 ? 147.805 -21.561 23.453 1.00 42.00  ? 123  ALA G N   1 
ATOM   7590  C  CA  . ALA G  1 123 ? 148.865 -21.745 22.487 1.00 37.14  ? 123  ALA G CA  1 
ATOM   7591  C  C   . ALA G  1 123 ? 148.289 -21.776 21.082 1.00 35.49  ? 123  ALA G C   1 
ATOM   7592  O  O   . ALA G  1 123 ? 147.198 -22.330 20.892 1.00 40.71  ? 123  ALA G O   1 
ATOM   7593  C  CB  . ALA G  1 123 ? 149.602 -23.047 22.771 1.00 48.42  ? 123  ALA G CB  1 
ATOM   7594  N  N   . ASP G  1 124 ? 149.021 -21.199 20.136 1.00 36.47  ? 124  ASP G N   1 
ATOM   7595  C  CA  . ASP G  1 124 ? 148.641 -21.260 18.730 1.00 35.09  ? 124  ASP G CA  1 
ATOM   7596  C  C   . ASP G  1 124 ? 149.154 -22.549 18.088 1.00 34.93  ? 124  ASP G C   1 
ATOM   7597  O  O   . ASP G  1 124 ? 150.379 -22.671 18.052 1.00 42.86  ? 124  ASP G O   1 
ATOM   7598  C  CB  . ASP G  1 124 ? 149.253 -20.096 17.953 1.00 31.16  ? 124  ASP G CB  1 
ATOM   7599  C  CG  . ASP G  1 124 ? 148.773 -19.991 16.520 1.00 46.56  ? 124  ASP G CG  1 
ATOM   7600  O  OD1 . ASP G  1 124 ? 148.760 -18.836 16.015 1.00 42.32  ? 124  ASP G OD1 1 
ATOM   7601  O  OD2 . ASP G  1 124 ? 148.415 -21.002 15.875 1.00 39.50  ? 124  ASP G OD2 1 
ATOM   7602  N  N   . ASP G  1 125 ? 148.320 -23.431 17.563 1.00 47.27  ? 125  ASP G N   1 
ATOM   7603  C  CA  . ASP G  1 125 ? 148.846 -24.685 16.996 1.00 52.03  ? 125  ASP G CA  1 
ATOM   7604  C  C   . ASP G  1 125 ? 149.484 -24.469 15.628 1.00 53.24  ? 125  ASP G C   1 
ATOM   7605  O  O   . ASP G  1 125 ? 149.829 -25.436 14.942 1.00 49.06  ? 125  ASP G O   1 
ATOM   7606  C  CB  . ASP G  1 125 ? 147.772 -25.767 16.921 1.00 45.32  ? 125  ASP G CB  1 
ATOM   7607  C  CG  . ASP G  1 125 ? 146.653 -25.570 15.933 1.00 47.41  ? 125  ASP G CG  1 
ATOM   7608  O  OD1 . ASP G  1 125 ? 145.610 -26.258 16.067 1.00 56.81  ? 125  ASP G OD1 1 
ATOM   7609  O  OD2 . ASP G  1 125 ? 146.785 -24.745 15.005 1.00 53.75  ? 125  ASP G OD2 1 
ATOM   7610  N  N   . LEU G  1 126 ? 149.657 -23.221 15.219 1.00 47.76  ? 126  LEU G N   1 
ATOM   7611  C  CA  . LEU G  1 126 ? 150.357 -22.830 14.012 1.00 41.33  ? 126  LEU G CA  1 
ATOM   7612  C  C   . LEU G  1 126 ? 149.710 -23.416 12.763 1.00 35.64  ? 126  LEU G C   1 
ATOM   7613  O  O   . LEU G  1 126 ? 150.376 -23.476 11.730 1.00 53.43  ? 126  LEU G O   1 
ATOM   7614  C  CB  . LEU G  1 126 ? 151.837 -23.232 14.089 1.00 44.04  ? 126  LEU G CB  1 
ATOM   7615  C  CG  . LEU G  1 126 ? 152.557 -22.606 15.291 1.00 45.15  ? 126  LEU G CG  1 
ATOM   7616  C  CD1 . LEU G  1 126 ? 154.065 -22.747 15.184 1.00 40.16  ? 126  LEU G CD1 1 
ATOM   7617  C  CD2 . LEU G  1 126 ? 152.159 -21.133 15.423 1.00 40.91  ? 126  LEU G CD2 1 
ATOM   7618  N  N   . GLY G  1 127 ? 148.457 -23.792 12.896 1.00 32.73  ? 127  GLY G N   1 
ATOM   7619  C  CA  . GLY G  1 127 ? 147.588 -24.256 11.838 1.00 47.47  ? 127  GLY G CA  1 
ATOM   7620  C  C   . GLY G  1 127 ? 147.822 -25.722 11.506 1.00 56.32  ? 127  GLY G C   1 
ATOM   7621  O  O   . GLY G  1 127 ? 147.337 -26.223 10.488 1.00 56.15  ? 127  GLY G O   1 
ATOM   7622  N  N   . LYS G  1 128 ? 148.574 -26.408 12.363 1.00 46.68  ? 128  LYS G N   1 
ATOM   7623  C  CA  . LYS G  1 128 ? 148.900 -27.811 12.082 1.00 46.50  ? 128  LYS G CA  1 
ATOM   7624  C  C   . LYS G  1 128 ? 148.167 -28.709 13.060 1.00 52.90  ? 128  LYS G C   1 
ATOM   7625  O  O   . LYS G  1 128 ? 148.520 -29.856 13.298 1.00 75.27  ? 128  LYS G O   1 
ATOM   7626  C  CB  . LYS G  1 128 ? 150.403 -28.031 12.161 1.00 43.41  ? 128  LYS G CB  1 
ATOM   7627  C  CG  . LYS G  1 128 ? 151.266 -26.910 11.592 1.00 39.88  ? 128  LYS G CG  1 
ATOM   7628  C  CD  . LYS G  1 128 ? 151.029 -26.720 10.099 1.00 42.48  ? 128  LYS G CD  1 
ATOM   7629  C  CE  . LYS G  1 128 ? 152.016 -25.698 9.544  1.00 51.98  ? 128  LYS G CE  1 
ATOM   7630  N  NZ  . LYS G  1 128 ? 151.616 -25.218 8.190  1.00 74.58  ? 128  LYS G NZ  1 
ATOM   7631  N  N   . GLY G  1 129 ? 147.104 -28.162 13.642 1.00 54.78  ? 129  GLY G N   1 
ATOM   7632  C  CA  . GLY G  1 129 ? 146.318 -28.910 14.601 1.00 58.34  ? 129  GLY G CA  1 
ATOM   7633  C  C   . GLY G  1 129 ? 145.771 -30.195 14.017 1.00 62.68  ? 129  GLY G C   1 
ATOM   7634  O  O   . GLY G  1 129 ? 145.920 -31.270 14.595 1.00 97.52  ? 129  GLY G O   1 
ATOM   7635  N  N   . GLY G  1 130 ? 145.116 -30.115 12.864 1.00 63.03  ? 130  GLY G N   1 
ATOM   7636  C  CA  . GLY G  1 130 ? 144.443 -31.290 12.336 1.00 70.36  ? 130  GLY G CA  1 
ATOM   7637  C  C   . GLY G  1 130 ? 142.960 -31.282 12.682 1.00 84.52  ? 130  GLY G C   1 
ATOM   7638  O  O   . GLY G  1 130 ? 142.363 -32.328 12.939 1.00 105.47 ? 130  GLY G O   1 
ATOM   7639  N  N   . ASN G  1 131 ? 142.357 -30.100 12.686 1.00 82.00  ? 131  ASN G N   1 
ATOM   7640  C  CA  . ASN G  1 131 ? 140.932 -29.911 12.931 1.00 74.74  ? 131  ASN G CA  1 
ATOM   7641  C  C   . ASN G  1 131 ? 140.530 -28.558 12.346 1.00 76.55  ? 131  ASN G C   1 
ATOM   7642  O  O   . ASN G  1 131 ? 141.213 -27.580 12.658 1.00 65.73  ? 131  ASN G O   1 
ATOM   7643  C  CB  . ASN G  1 131 ? 140.601 -29.987 14.413 1.00 78.42  ? 131  ASN G CB  1 
ATOM   7644  C  CG  . ASN G  1 131 ? 141.051 -28.786 15.217 1.00 82.71  ? 131  ASN G CG  1 
ATOM   7645  O  OD1 . ASN G  1 131 ? 140.617 -27.654 14.993 1.00 76.99  ? 131  ASN G OD1 1 
ATOM   7646  N  ND2 . ASN G  1 131 ? 141.932 -29.023 16.187 1.00 82.36  ? 131  ASN G ND2 1 
ATOM   7647  N  N   . GLU G  1 132 ? 139.491 -28.525 11.536 1.00 78.44  ? 132  GLU G N   1 
ATOM   7648  C  CA  . GLU G  1 132 ? 139.102 -27.392 10.710 1.00 77.53  ? 132  GLU G CA  1 
ATOM   7649  C  C   . GLU G  1 132 ? 139.267 -26.024 11.364 1.00 74.82  ? 132  GLU G C   1 
ATOM   7650  O  O   . GLU G  1 132 ? 139.468 -25.038 10.639 1.00 68.58  ? 132  GLU G O   1 
ATOM   7651  C  CB  . GLU G  1 132 ? 137.650 -27.578 10.239 1.00 71.00  ? 132  GLU G CB  1 
ATOM   7652  C  CG  . GLU G  1 132 ? 137.031 -26.290 9.718  1.00 71.01  ? 132  GLU G CG  1 
ATOM   7653  C  CD  . GLU G  1 132 ? 136.050 -25.695 10.712 1.00 75.49  ? 132  GLU G CD  1 
ATOM   7654  O  OE1 . GLU G  1 132 ? 136.394 -25.579 11.909 1.00 86.02  ? 132  GLU G OE1 1 
ATOM   7655  O  OE2 . GLU G  1 132 ? 134.927 -25.343 10.294 1.00 68.17  ? 132  GLU G OE2 1 
ATOM   7656  N  N   . GLU G  1 133 ? 139.204 -25.890 12.684 1.00 72.29  ? 133  GLU G N   1 
ATOM   7657  C  CA  . GLU G  1 133 ? 139.408 -24.591 13.319 1.00 76.20  ? 133  GLU G CA  1 
ATOM   7658  C  C   . GLU G  1 133 ? 140.883 -24.218 13.434 1.00 70.30  ? 133  GLU G C   1 
ATOM   7659  O  O   . GLU G  1 133 ? 141.226 -23.033 13.380 1.00 54.98  ? 133  GLU G O   1 
ATOM   7660  C  CB  . GLU G  1 133 ? 138.770 -24.540 14.714 1.00 79.75  ? 133  GLU G CB  1 
ATOM   7661  C  CG  . GLU G  1 133 ? 138.757 -23.139 15.312 1.00 82.42  ? 133  GLU G CG  1 
ATOM   7662  C  CD  . GLU G  1 133 ? 137.933 -22.148 14.515 1.00 83.03  ? 133  GLU G CD  1 
ATOM   7663  O  OE1 . GLU G  1 133 ? 137.813 -22.292 13.280 1.00 81.58  ? 133  GLU G OE1 1 
ATOM   7664  O  OE2 . GLU G  1 133 ? 137.393 -21.197 15.124 1.00 87.72  ? 133  GLU G OE2 1 
ATOM   7665  N  N   . SER G  1 134 ? 141.774 -25.192 13.587 1.00 55.62  ? 134  SER G N   1 
ATOM   7666  C  CA  . SER G  1 134 ? 143.210 -24.936 13.585 1.00 47.45  ? 134  SER G CA  1 
ATOM   7667  C  C   . SER G  1 134 ? 143.619 -24.084 12.386 1.00 43.44  ? 134  SER G C   1 
ATOM   7668  O  O   . SER G  1 134 ? 144.515 -23.246 12.463 1.00 56.67  ? 134  SER G O   1 
ATOM   7669  C  CB  . SER G  1 134 ? 143.975 -26.264 13.566 1.00 48.47  ? 134  SER G CB  1 
ATOM   7670  O  OG  . SER G  1 134 ? 145.372 -26.072 13.464 1.00 59.89  ? 134  SER G OG  1 
ATOM   7671  N  N   . THR G  1 135 ? 142.952 -24.311 11.270 1.00 44.25  ? 135  THR G N   1 
ATOM   7672  C  CA  . THR G  1 135 ? 143.165 -23.707 9.973  1.00 43.46  ? 135  THR G CA  1 
ATOM   7673  C  C   . THR G  1 135 ? 142.580 -22.300 9.891  1.00 50.93  ? 135  THR G C   1 
ATOM   7674  O  O   . THR G  1 135 ? 142.658 -21.654 8.844  1.00 50.76  ? 135  THR G O   1 
ATOM   7675  C  CB  . THR G  1 135 ? 142.528 -24.568 8.869  1.00 50.18  ? 135  THR G CB  1 
ATOM   7676  O  OG1 . THR G  1 135 ? 141.100 -24.429 8.917  1.00 54.41  ? 135  THR G OG1 1 
ATOM   7677  C  CG2 . THR G  1 135 ? 142.807 -26.051 9.101  1.00 52.50  ? 135  THR G CG2 1 
ATOM   7678  N  N   . LYS G  1 136 ? 142.000 -21.821 10.985 1.00 54.11  ? 136  LYS G N   1 
ATOM   7679  C  CA  . LYS G  1 136 ? 141.448 -20.467 11.018 1.00 56.69  ? 136  LYS G CA  1 
ATOM   7680  C  C   . LYS G  1 136 ? 142.136 -19.611 12.077 1.00 55.30  ? 136  LYS G C   1 
ATOM   7681  O  O   . LYS G  1 136 ? 142.731 -18.561 11.827 1.00 52.22  ? 136  LYS G O   1 
ATOM   7682  C  CB  . LYS G  1 136 ? 139.946 -20.539 11.293 1.00 63.51  ? 136  LYS G CB  1 
ATOM   7683  C  CG  . LYS G  1 136 ? 139.109 -20.735 10.039 1.00 69.30  ? 136  LYS G CG  1 
ATOM   7684  C  CD  . LYS G  1 136 ? 138.082 -21.837 10.224 1.00 75.52  ? 136  LYS G CD  1 
ATOM   7685  C  CE  . LYS G  1 136 ? 137.406 -22.171 8.899  1.00 83.94  ? 136  LYS G CE  1 
ATOM   7686  N  NZ  . LYS G  1 136 ? 137.690 -23.575 8.485  1.00 105.23 ? 136  LYS G NZ  1 
ATOM   7687  N  N   . THR G  1 137 ? 142.047 -20.112 13.300 1.00 47.15  ? 137  THR G N   1 
ATOM   7688  C  CA  . THR G  1 137 ? 142.547 -19.493 14.503 1.00 45.54  ? 137  THR G CA  1 
ATOM   7689  C  C   . THR G  1 137 ? 143.635 -20.267 15.224 1.00 50.05  ? 137  THR G C   1 
ATOM   7690  O  O   . THR G  1 137 ? 144.073 -19.873 16.310 1.00 36.90  ? 137  THR G O   1 
ATOM   7691  C  CB  . THR G  1 137 ? 141.351 -19.364 15.480 1.00 51.25  ? 137  THR G CB  1 
ATOM   7692  O  OG1 . THR G  1 137 ? 141.175 -20.625 16.140 1.00 60.78  ? 137  THR G OG1 1 
ATOM   7693  C  CG2 . THR G  1 137 ? 140.085 -19.064 14.701 1.00 51.24  ? 137  THR G CG2 1 
ATOM   7694  N  N   . GLY G  1 138 ? 144.082 -21.398 14.673 1.00 54.49  ? 138  GLY G N   1 
ATOM   7695  C  CA  . GLY G  1 138 ? 145.084 -22.199 15.346 1.00 46.66  ? 138  GLY G CA  1 
ATOM   7696  C  C   . GLY G  1 138 ? 144.718 -22.650 16.741 1.00 50.32  ? 138  GLY G C   1 
ATOM   7697  O  O   . GLY G  1 138 ? 145.620 -22.966 17.520 1.00 47.57  ? 138  GLY G O   1 
ATOM   7698  N  N   . ASN G  1 139 ? 143.443 -22.699 17.101 1.00 57.41  ? 139  ASN G N   1 
ATOM   7699  C  CA  . ASN G  1 139 ? 142.985 -23.152 18.411 1.00 51.17  ? 139  ASN G CA  1 
ATOM   7700  C  C   . ASN G  1 139 ? 143.561 -22.377 19.583 1.00 49.97  ? 139  ASN G C   1 
ATOM   7701  O  O   . ASN G  1 139 ? 143.740 -22.907 20.690 1.00 50.53  ? 139  ASN G O   1 
ATOM   7702  C  CB  . ASN G  1 139 ? 143.309 -24.659 18.541 1.00 52.94  ? 139  ASN G CB  1 
ATOM   7703  C  CG  . ASN G  1 139 ? 142.517 -25.445 17.507 1.00 59.31  ? 139  ASN G CG  1 
ATOM   7704  O  OD1 . ASN G  1 139 ? 141.312 -25.655 17.671 1.00 63.69  ? 139  ASN G OD1 1 
ATOM   7705  N  ND2 . ASN G  1 139 ? 143.173 -25.866 16.436 1.00 70.03  ? 139  ASN G ND2 1 
ATOM   7706  N  N   . ALA G  1 140 ? 143.844 -21.092 19.379 1.00 45.02  ? 140  ALA G N   1 
ATOM   7707  C  CA  . ALA G  1 140 ? 144.452 -20.241 20.383 1.00 36.93  ? 140  ALA G CA  1 
ATOM   7708  C  C   . ALA G  1 140 ? 143.486 -19.767 21.461 1.00 29.40  ? 140  ALA G C   1 
ATOM   7709  O  O   . ALA G  1 140 ? 143.909 -19.151 22.446 1.00 40.99  ? 140  ALA G O   1 
ATOM   7710  C  CB  . ALA G  1 140 ? 145.072 -19.020 19.698 1.00 34.70  ? 140  ALA G CB  1 
ATOM   7711  N  N   . GLY G  1 141 ? 142.201 -20.030 21.332 1.00 35.09  ? 141  GLY G N   1 
ATOM   7712  C  CA  . GLY G  1 141 ? 141.273 -19.699 22.388 1.00 36.46  ? 141  GLY G CA  1 
ATOM   7713  C  C   . GLY G  1 141 ? 140.908 -18.234 22.462 1.00 38.42  ? 141  GLY G C   1 
ATOM   7714  O  O   . GLY G  1 141 ? 141.030 -17.456 21.510 1.00 35.22  ? 141  GLY G O   1 
ATOM   7715  N  N   . SER G  1 142 ? 140.469 -17.826 23.648 1.00 32.17  ? 142  SER G N   1 
ATOM   7716  C  CA  . SER G  1 142 ? 139.934 -16.468 23.798 1.00 40.36  ? 142  SER G CA  1 
ATOM   7717  C  C   . SER G  1 142 ? 140.999 -15.392 23.653 1.00 38.89  ? 142  SER G C   1 
ATOM   7718  O  O   . SER G  1 142 ? 142.187 -15.668 23.756 1.00 33.00  ? 142  SER G O   1 
ATOM   7719  C  CB  . SER G  1 142 ? 139.238 -16.350 25.163 1.00 40.73  ? 142  SER G CB  1 
ATOM   7720  O  OG  . SER G  1 142 ? 140.198 -16.044 26.162 1.00 43.76  ? 142  SER G OG  1 
ATOM   7721  N  N   . ARG G  1 143 ? 140.557 -14.159 23.422 1.00 35.49  ? 143  ARG G N   1 
ATOM   7722  C  CA  . ARG G  1 143 ? 141.406 -12.980 23.296 1.00 32.85  ? 143  ARG G CA  1 
ATOM   7723  C  C   . ARG G  1 143 ? 141.646 -12.313 24.624 1.00 29.44  ? 143  ARG G C   1 
ATOM   7724  O  O   . ARG G  1 143 ? 140.675 -11.785 25.189 1.00 35.89  ? 143  ARG G O   1 
ATOM   7725  C  CB  . ARG G  1 143 ? 140.687 -12.038 22.308 1.00 31.03  ? 143  ARG G CB  1 
ATOM   7726  C  CG  . ARG G  1 143 ? 140.294 -12.820 21.044 1.00 26.82  ? 143  ARG G CG  1 
ATOM   7727  C  CD  . ARG G  1 143 ? 139.711 -11.869 20.000 1.00 34.37  ? 143  ARG G CD  1 
ATOM   7728  N  NE  . ARG G  1 143 ? 139.351 -12.601 18.811 1.00 31.14  ? 143  ARG G NE  1 
ATOM   7729  C  CZ  . ARG G  1 143 ? 138.931 -12.144 17.651 1.00 42.56  ? 143  ARG G CZ  1 
ATOM   7730  N  NH1 . ARG G  1 143 ? 138.658 -13.010 16.681 1.00 35.28  ? 143  ARG G NH1 1 
ATOM   7731  N  NH2 . ARG G  1 143 ? 138.786 -10.837 17.473 1.00 33.56  ? 143  ARG G NH2 1 
ATOM   7732  N  N   . LEU G  1 144 ? 142.851 -12.271 25.196 1.00 29.47  ? 144  LEU G N   1 
ATOM   7733  C  CA  . LEU G  1 144 ? 142.969 -11.716 26.546 1.00 30.73  ? 144  LEU G CA  1 
ATOM   7734  C  C   . LEU G  1 144 ? 143.238 -10.218 26.600 1.00 37.01  ? 144  LEU G C   1 
ATOM   7735  O  O   . LEU G  1 144 ? 142.808 -9.571  27.564 1.00 29.24  ? 144  LEU G O   1 
ATOM   7736  C  CB  . LEU G  1 144 ? 144.066 -12.402 27.365 1.00 28.56  ? 144  LEU G CB  1 
ATOM   7737  C  CG  . LEU G  1 144 ? 143.976 -13.941 27.425 1.00 30.66  ? 144  LEU G CG  1 
ATOM   7738  C  CD1 . LEU G  1 144 ? 145.115 -14.476 28.278 1.00 34.72  ? 144  LEU G CD1 1 
ATOM   7739  C  CD2 . LEU G  1 144 ? 142.632 -14.399 27.964 1.00 33.49  ? 144  LEU G CD2 1 
ATOM   7740  N  N   . ALA G  1 145 ? 143.950 -9.668  25.630 1.00 29.66  ? 145  ALA G N   1 
ATOM   7741  C  CA  . ALA G  1 145 ? 144.264 -8.241  25.574 1.00 21.80  ? 145  ALA G CA  1 
ATOM   7742  C  C   . ALA G  1 145 ? 144.453 -7.883  24.091 1.00 31.54  ? 145  ALA G C   1 
ATOM   7743  O  O   . ALA G  1 145 ? 144.803 -8.730  23.255 1.00 29.66  ? 145  ALA G O   1 
ATOM   7744  C  CB  . ALA G  1 145 ? 145.461 -7.827  26.387 1.00 25.42  ? 145  ALA G CB  1 
ATOM   7745  N  N   . CYS G  1 146 ? 144.175 -6.629  23.762 1.00 28.00  ? 146  CYS G N   1 
ATOM   7746  C  CA  . CYS G  1 146 ? 144.309 -6.227  22.358 1.00 29.93  ? 146  CYS G CA  1 
ATOM   7747  C  C   . CYS G  1 146 ? 144.573 -4.730  22.333 1.00 39.90  ? 146  CYS G C   1 
ATOM   7748  O  O   . CYS G  1 146 ? 144.293 -4.109  23.357 1.00 30.19  ? 146  CYS G O   1 
ATOM   7749  C  CB  A CYS G  1 146 ? 143.061 -6.571  21.560 0.43 25.72  ? 146  CYS G CB  1 
ATOM   7750  C  CB  B CYS G  1 146 ? 143.089 -6.620  21.547 0.57 25.52  ? 146  CYS G CB  1 
ATOM   7751  S  SG  A CYS G  1 146 ? 141.509 -5.996  22.289 0.43 46.64  ? 146  CYS G SG  1 
ATOM   7752  S  SG  B CYS G  1 146 ? 141.561 -5.722  21.858 0.57 33.40  ? 146  CYS G SG  1 
ATOM   7753  N  N   . GLY G  1 147 ? 145.090 -4.179  21.248 1.00 30.30  ? 147  GLY G N   1 
ATOM   7754  C  CA  . GLY G  1 147 ? 145.328 -2.740  21.139 1.00 24.58  ? 147  GLY G CA  1 
ATOM   7755  C  C   . GLY G  1 147 ? 145.304 -2.385  19.654 1.00 36.66  ? 147  GLY G C   1 
ATOM   7756  O  O   . GLY G  1 147 ? 145.608 -3.212  18.779 1.00 26.63  ? 147  GLY G O   1 
ATOM   7757  N  N   . VAL G  1 148 ? 144.933 -1.150  19.351 1.00 31.69  ? 148  VAL G N   1 
ATOM   7758  C  CA  . VAL G  1 148 ? 145.041 -0.677  17.967 1.00 29.54  ? 148  VAL G CA  1 
ATOM   7759  C  C   . VAL G  1 148 ? 146.479 -0.284  17.691 1.00 27.21  ? 148  VAL G C   1 
ATOM   7760  O  O   . VAL G  1 148 ? 147.189 0.352   18.469 1.00 26.44  ? 148  VAL G O   1 
ATOM   7761  C  CB  . VAL G  1 148 ? 144.047 0.471   17.712 1.00 30.12  ? 148  VAL G CB  1 
ATOM   7762  C  CG1 . VAL G  1 148 ? 144.231 1.001   16.295 1.00 33.71  ? 148  VAL G CG1 1 
ATOM   7763  C  CG2 . VAL G  1 148 ? 142.611 -0.004  17.951 1.00 22.32  ? 148  VAL G CG2 1 
ATOM   7764  N  N   . ILE G  1 149 ? 147.011 -0.703  16.536 1.00 26.45  ? 149  ILE G N   1 
ATOM   7765  C  CA  . ILE G  1 149 ? 148.408 -0.431  16.208 1.00 26.13  ? 149  ILE G CA  1 
ATOM   7766  C  C   . ILE G  1 149 ? 148.574 0.964   15.614 1.00 27.88  ? 149  ILE G C   1 
ATOM   7767  O  O   . ILE G  1 149 ? 147.969 1.239   14.579 1.00 31.12  ? 149  ILE G O   1 
ATOM   7768  C  CB  . ILE G  1 149 ? 148.939 -1.488  15.224 1.00 26.81  ? 149  ILE G CB  1 
ATOM   7769  C  CG1 . ILE G  1 149 ? 148.849 -2.890  15.831 1.00 27.13  ? 149  ILE G CG1 1 
ATOM   7770  C  CG2 . ILE G  1 149 ? 150.358 -1.173  14.767 1.00 26.13  ? 149  ILE G CG2 1 
ATOM   7771  C  CD1 . ILE G  1 149 ? 148.902 -4.031  14.840 1.00 29.63  ? 149  ILE G CD1 1 
ATOM   7772  N  N   . GLY G  1 150 ? 149.339 1.821   16.273 1.00 27.43  ? 150  GLY G N   1 
ATOM   7773  C  CA  . GLY G  1 150 ? 149.329 3.243   15.972 1.00 27.11  ? 150  GLY G CA  1 
ATOM   7774  C  C   . GLY G  1 150 ? 150.651 3.701   15.403 1.00 32.68  ? 150  GLY G C   1 
ATOM   7775  O  O   . GLY G  1 150 ? 151.683 3.101   15.683 1.00 29.75  ? 150  GLY G O   1 
ATOM   7776  N  N   . ILE G  1 151 ? 150.634 4.768   14.603 1.00 28.23  ? 151  ILE G N   1 
ATOM   7777  C  CA  . ILE G  1 151 ? 151.877 5.351   14.122 1.00 29.31  ? 151  ILE G CA  1 
ATOM   7778  C  C   . ILE G  1 151 ? 152.627 6.001   15.280 1.00 30.35  ? 151  ILE G C   1 
ATOM   7779  O  O   . ILE G  1 151 ? 151.981 6.740   16.029 1.00 32.90  ? 151  ILE G O   1 
ATOM   7780  C  CB  . ILE G  1 151 ? 151.609 6.395   13.030 1.00 31.12  ? 151  ILE G CB  1 
ATOM   7781  C  CG1 . ILE G  1 151 ? 150.911 5.783   11.815 1.00 29.52  ? 151  ILE G CG1 1 
ATOM   7782  C  CG2 . ILE G  1 151 ? 152.897 7.103   12.636 1.00 42.56  ? 151  ILE G CG2 1 
ATOM   7783  C  CD1 . ILE G  1 151 ? 150.613 6.817   10.747 1.00 45.26  ? 151  ILE G CD1 1 
ATOM   7784  N  N   . ALA G  1 152 ? 153.923 5.713   15.389 1.00 27.18  ? 152  ALA G N   1 
ATOM   7785  C  CA  . ALA G  1 152 ? 154.801 6.235   16.438 1.00 27.68  ? 152  ALA G CA  1 
ATOM   7786  C  C   . ALA G  1 152 ? 155.904 7.121   15.887 1.00 37.69  ? 152  ALA G C   1 
ATOM   7787  O  O   . ALA G  1 152 ? 156.304 7.021   14.719 1.00 39.36  ? 152  ALA G O   1 
ATOM   7788  C  CB  . ALA G  1 152 ? 155.409 5.056   17.210 1.00 31.24  ? 152  ALA G CB  1 
ATOM   7789  N  N   . GLN G  1 153 ? 156.439 8.008   16.711 1.00 30.25  ? 153  GLN G N   1 
ATOM   7790  C  CA  . GLN G  1 153 ? 157.353 9.023   16.209 1.00 38.81  ? 153  GLN G CA  1 
ATOM   7791  C  C   . GLN G  1 153 ? 158.729 8.466   15.865 1.00 60.81  ? 153  GLN G C   1 
ATOM   7792  O  O   . GLN G  1 153 ? 159.204 7.591   16.619 1.00 52.68  ? 153  GLN G O   1 
ATOM   7793  C  CB  . GLN G  1 153 ? 157.522 10.106  17.266 1.00 39.72  ? 153  GLN G CB  1 
ATOM   7794  C  CG  . GLN G  1 153 ? 158.847 10.857  17.224 1.00 39.71  ? 153  GLN G CG  1 
ATOM   7795  C  CD  . GLN G  1 153 ? 158.829 11.942  18.293 1.00 48.82  ? 153  GLN G CD  1 
ATOM   7796  O  OE1 . GLN G  1 153 ? 158.469 13.090  18.037 1.00 78.07  ? 153  GLN G OE1 1 
ATOM   7797  N  NE2 . GLN G  1 153 ? 159.196 11.580  19.515 1.00 54.27  ? 153  GLN G NE2 1 
ATOM   7798  O  OXT . GLN G  1 153 ? 159.325 8.912   14.865 1.00 81.60  ? 153  GLN G OXT 1 
ATOM   7799  N  N   . ALA H  1 1   ? 139.648 1.517   2.277  1.00 57.64  ? 1    ALA H N   1 
ATOM   7800  C  CA  . ALA H  1 1   ? 139.484 2.271   3.523  1.00 60.96  ? 1    ALA H CA  1 
ATOM   7801  C  C   . ALA H  1 1   ? 138.256 3.171   3.498  1.00 48.06  ? 1    ALA H C   1 
ATOM   7802  O  O   . ALA H  1 1   ? 138.344 4.374   3.269  1.00 64.58  ? 1    ALA H O   1 
ATOM   7803  C  CB  . ALA H  1 1   ? 140.735 3.092   3.804  1.00 88.04  ? 1    ALA H CB  1 
ATOM   7804  N  N   . THR H  1 2   ? 137.071 2.601   3.733  1.00 52.56  ? 2    THR H N   1 
ATOM   7805  C  CA  . THR H  1 2   ? 135.900 3.466   3.703  1.00 48.87  ? 2    THR H CA  1 
ATOM   7806  C  C   . THR H  1 2   ? 135.344 3.667   5.110  1.00 50.90  ? 2    THR H C   1 
ATOM   7807  O  O   . THR H  1 2   ? 134.584 4.636   5.228  1.00 43.64  ? 2    THR H O   1 
ATOM   7808  C  CB  . THR H  1 2   ? 134.760 2.964   2.800  1.00 51.77  ? 2    THR H CB  1 
ATOM   7809  O  OG1 . THR H  1 2   ? 134.241 1.719   3.291  1.00 47.78  ? 2    THR H OG1 1 
ATOM   7810  C  CG2 . THR H  1 2   ? 135.282 2.728   1.392  1.00 78.24  ? 2    THR H CG2 1 
ATOM   7811  N  N   . LYS H  1 3   ? 135.680 2.827   6.097  1.00 36.25  ? 3    LYS H N   1 
ATOM   7812  C  CA  . LYS H  1 3   ? 135.223 3.166   7.446  1.00 28.20  ? 3    LYS H CA  1 
ATOM   7813  C  C   . LYS H  1 3   ? 136.341 3.062   8.487  1.00 35.69  ? 3    LYS H C   1 
ATOM   7814  O  O   . LYS H  1 3   ? 137.303 2.305   8.405  1.00 34.73  ? 3    LYS H O   1 
ATOM   7815  C  CB  . LYS H  1 3   ? 134.058 2.311   7.911  1.00 29.38  ? 3    LYS H CB  1 
ATOM   7816  C  CG  . LYS H  1 3   ? 132.769 2.431   7.134  1.00 43.01  ? 3    LYS H CG  1 
ATOM   7817  C  CD  . LYS H  1 3   ? 132.084 1.076   7.013  1.00 52.93  ? 3    LYS H CD  1 
ATOM   7818  C  CE  . LYS H  1 3   ? 130.618 1.270   6.643  1.00 66.67  ? 3    LYS H CE  1 
ATOM   7819  N  NZ  . LYS H  1 3   ? 130.201 2.693   6.817  1.00 73.38  ? 3    LYS H NZ  1 
ATOM   7820  N  N   . ALA H  1 4   ? 136.181 3.892   9.527  1.00 24.80  ? 4    ALA H N   1 
ATOM   7821  C  CA  . ALA H  1 4   ? 137.139 3.860   10.621 1.00 25.51  ? 4    ALA H CA  1 
ATOM   7822  C  C   . ALA H  1 4   ? 136.356 4.103   11.912 1.00 23.34  ? 4    ALA H C   1 
ATOM   7823  O  O   . ALA H  1 4   ? 135.190 4.509   11.871 1.00 30.08  ? 4    ALA H O   1 
ATOM   7824  C  CB  . ALA H  1 4   ? 138.282 4.836   10.471 1.00 25.64  ? 4    ALA H CB  1 
ATOM   7825  N  N   . VAL H  1 5   ? 137.004 3.789   13.035 1.00 25.86  ? 5    VAL H N   1 
ATOM   7826  C  CA  . VAL H  1 5   ? 136.288 3.937   14.299 1.00 23.79  ? 5    VAL H CA  1 
ATOM   7827  C  C   . VAL H  1 5   ? 137.319 4.265   15.369 1.00 27.24  ? 5    VAL H C   1 
ATOM   7828  O  O   . VAL H  1 5   ? 138.487 3.952   15.204 1.00 29.29  ? 5    VAL H O   1 
ATOM   7829  C  CB  . VAL H  1 5   ? 135.486 2.687   14.684 1.00 25.07  ? 5    VAL H CB  1 
ATOM   7830  C  CG1 . VAL H  1 5   ? 136.470 1.554   14.966 1.00 27.19  ? 5    VAL H CG1 1 
ATOM   7831  C  CG2 . VAL H  1 5   ? 134.578 2.991   15.866 1.00 27.45  ? 5    VAL H CG2 1 
ATOM   7832  N  N   . CYS H  1 6   ? 136.870 4.922   16.432 1.00 23.22  ? 6    CYS H N   1 
ATOM   7833  C  CA  . CYS H  1 6   ? 137.804 5.304   17.478 1.00 27.38  ? 6    CYS H CA  1 
ATOM   7834  C  C   . CYS H  1 6   ? 137.103 5.182   18.823 1.00 25.51  ? 6    CYS H C   1 
ATOM   7835  O  O   . CYS H  1 6   ? 135.993 5.689   18.958 1.00 25.67  ? 6    CYS H O   1 
ATOM   7836  C  CB  . CYS H  1 6   ? 138.275 6.742   17.243 1.00 31.32  ? 6    CYS H CB  1 
ATOM   7837  S  SG  . CYS H  1 6   ? 139.411 7.365   18.506 1.00 32.13  ? 6    CYS H SG  1 
ATOM   7838  N  N   . VAL H  1 7   ? 137.732 4.546   19.799 1.00 23.93  ? 7    VAL H N   1 
ATOM   7839  C  CA  . VAL H  1 7   ? 137.167 4.478   21.141 1.00 21.02  ? 7    VAL H CA  1 
ATOM   7840  C  C   . VAL H  1 7   ? 137.934 5.473   21.994 1.00 21.03  ? 7    VAL H C   1 
ATOM   7841  O  O   . VAL H  1 7   ? 139.143 5.310   22.164 1.00 27.70  ? 7    VAL H O   1 
ATOM   7842  C  CB  . VAL H  1 7   ? 137.288 3.060   21.743 1.00 29.46  ? 7    VAL H CB  1 
ATOM   7843  C  CG1 . VAL H  1 7   ? 136.976 3.082   23.231 1.00 28.73  ? 7    VAL H CG1 1 
ATOM   7844  C  CG2 . VAL H  1 7   ? 136.340 2.070   21.055 1.00 26.40  ? 7    VAL H CG2 1 
ATOM   7845  N  N   . LEU H  1 8   ? 137.265 6.503   22.501 1.00 24.80  ? 8    LEU H N   1 
ATOM   7846  C  CA  . LEU H  1 8   ? 137.896 7.536   23.297 1.00 23.51  ? 8    LEU H CA  1 
ATOM   7847  C  C   . LEU H  1 8   ? 137.814 7.236   24.794 1.00 23.61  ? 8    LEU H C   1 
ATOM   7848  O  O   . LEU H  1 8   ? 136.732 6.983   25.332 1.00 25.40  ? 8    LEU H O   1 
ATOM   7849  C  CB  . LEU H  1 8   ? 137.189 8.872   23.084 1.00 25.55  ? 8    LEU H CB  1 
ATOM   7850  C  CG  . LEU H  1 8   ? 137.180 9.486   21.680 1.00 26.44  ? 8    LEU H CG  1 
ATOM   7851  C  CD1 . LEU H  1 8   ? 136.265 10.709  21.713 1.00 31.38  ? 8    LEU H CD1 1 
ATOM   7852  C  CD2 . LEU H  1 8   ? 138.559 9.885   21.209 1.00 29.15  ? 8    LEU H CD2 1 
ATOM   7853  N  N   . LYS H  1 9   ? 138.962 7.301   25.440 1.00 26.18  ? 9    LYS H N   1 
ATOM   7854  C  CA  . LYS H  1 9   ? 139.071 7.113   26.877 1.00 28.64  ? 9    LYS H CA  1 
ATOM   7855  C  C   . LYS H  1 9   ? 140.163 8.025   27.420 1.00 29.69  ? 9    LYS H C   1 
ATOM   7856  O  O   . LYS H  1 9   ? 141.075 8.413   26.693 1.00 28.53  ? 9    LYS H O   1 
ATOM   7857  C  CB  . LYS H  1 9   ? 139.425 5.657   27.211 1.00 32.43  ? 9    LYS H CB  1 
ATOM   7858  C  CG  . LYS H  1 9   ? 138.534 4.586   26.614 1.00 45.91  ? 9    LYS H CG  1 
ATOM   7859  C  CD  . LYS H  1 9   ? 137.406 4.187   27.554 1.00 65.88  ? 9    LYS H CD  1 
ATOM   7860  C  CE  . LYS H  1 9   ? 136.211 3.609   26.810 1.00 69.98  ? 9    LYS H CE  1 
ATOM   7861  N  NZ  . LYS H  1 9   ? 136.158 2.120   26.905 1.00 78.67  ? 9    LYS H NZ  1 
ATOM   7862  N  N   . GLY H  1 10  ? 140.114 8.349   28.703 1.00 31.82  ? 10   GLY H N   1 
ATOM   7863  C  CA  . GLY H  1 10  ? 141.192 9.083   29.345 1.00 27.03  ? 10   GLY H CA  1 
ATOM   7864  C  C   . GLY H  1 10  ? 141.218 8.752   30.831 1.00 33.87  ? 10   GLY H C   1 
ATOM   7865  O  O   . GLY H  1 10  ? 140.835 7.666   31.252 1.00 40.04  ? 10   GLY H O   1 
ATOM   7866  N  N   . ASP H  1 11  ? 141.686 9.684   31.647 1.00 44.16  ? 11   ASP H N   1 
ATOM   7867  C  CA  . ASP H  1 11  ? 141.810 9.370   33.068 1.00 46.60  ? 11   ASP H CA  1 
ATOM   7868  C  C   . ASP H  1 11  ? 140.520 9.609   33.835 1.00 50.61  ? 11   ASP H C   1 
ATOM   7869  O  O   . ASP H  1 11  ? 140.261 8.978   34.859 1.00 55.41  ? 11   ASP H O   1 
ATOM   7870  C  CB  . ASP H  1 11  ? 142.940 10.241  33.632 1.00 46.16  ? 11   ASP H CB  1 
ATOM   7871  C  CG  . ASP H  1 11  ? 144.283 9.716   33.149 1.00 57.95  ? 11   ASP H CG  1 
ATOM   7872  O  OD1 . ASP H  1 11  ? 145.085 10.520  32.637 1.00 59.13  ? 11   ASP H OD1 1 
ATOM   7873  O  OD2 . ASP H  1 11  ? 144.477 8.487   33.305 1.00 69.98  ? 11   ASP H OD2 1 
ATOM   7874  N  N   . GLY H  1 12  ? 139.741 10.543  33.319 1.00 34.21  ? 12   GLY H N   1 
ATOM   7875  C  CA  . GLY H  1 12  ? 138.546 11.071  33.947 1.00 32.08  ? 12   GLY H CA  1 
ATOM   7876  C  C   . GLY H  1 12  ? 137.327 10.385  33.366 1.00 30.74  ? 12   GLY H C   1 
ATOM   7877  O  O   . GLY H  1 12  ? 137.473 9.272   32.870 1.00 30.20  ? 12   GLY H O   1 
ATOM   7878  N  N   . PRO H  1 13  ? 136.163 11.015  33.476 1.00 28.33  ? 13   PRO H N   1 
ATOM   7879  C  CA  . PRO H  1 13  ? 134.955 10.338  33.022 1.00 29.58  ? 13   PRO H CA  1 
ATOM   7880  C  C   . PRO H  1 13  ? 134.679 10.441  31.532 1.00 33.68  ? 13   PRO H C   1 
ATOM   7881  O  O   . PRO H  1 13  ? 133.679 9.874   31.080 1.00 31.18  ? 13   PRO H O   1 
ATOM   7882  C  CB  . PRO H  1 13  ? 133.873 11.131  33.780 1.00 33.38  ? 13   PRO H CB  1 
ATOM   7883  C  CG  . PRO H  1 13  ? 134.418 12.515  33.880 1.00 26.21  ? 13   PRO H CG  1 
ATOM   7884  C  CD  . PRO H  1 13  ? 135.899 12.331  34.068 1.00 26.91  ? 13   PRO H CD  1 
ATOM   7885  N  N   . VAL H  1 14  ? 135.507 11.143  30.759 1.00 26.87  ? 14   VAL H N   1 
ATOM   7886  C  CA  . VAL H  1 14  ? 135.084 11.401  29.370 1.00 25.07  ? 14   VAL H CA  1 
ATOM   7887  C  C   . VAL H  1 14  ? 135.286 10.151  28.533 1.00 24.51  ? 14   VAL H C   1 
ATOM   7888  O  O   . VAL H  1 14  ? 136.372 9.558   28.497 1.00 25.58  ? 14   VAL H O   1 
ATOM   7889  C  CB  . VAL H  1 14  ? 135.837 12.616  28.790 1.00 27.10  ? 14   VAL H CB  1 
ATOM   7890  C  CG1 . VAL H  1 14  ? 135.498 12.841  27.314 1.00 25.19  ? 14   VAL H CG1 1 
ATOM   7891  C  CG2 . VAL H  1 14  ? 135.524 13.882  29.588 1.00 23.82  ? 14   VAL H CG2 1 
ATOM   7892  N  N   . GLN H  1 15  ? 134.266 9.684   27.817 1.00 25.14  ? 15   GLN H N   1 
ATOM   7893  C  CA  . GLN H  1 15  ? 134.500 8.470   27.019 1.00 25.60  ? 15   GLN H CA  1 
ATOM   7894  C  C   . GLN H  1 15  ? 133.534 8.473   25.850 1.00 21.33  ? 15   GLN H C   1 
ATOM   7895  O  O   . GLN H  1 15  ? 132.471 9.096   25.947 1.00 24.53  ? 15   GLN H O   1 
ATOM   7896  C  CB  . GLN H  1 15  ? 134.330 7.211   27.864 1.00 28.59  ? 15   GLN H CB  1 
ATOM   7897  C  CG  . GLN H  1 15  ? 133.022 7.081   28.625 1.00 33.06  ? 15   GLN H CG  1 
ATOM   7898  C  CD  . GLN H  1 15  ? 133.042 5.872   29.563 1.00 43.53  ? 15   GLN H CD  1 
ATOM   7899  O  OE1 . GLN H  1 15  ? 133.296 4.742   29.141 1.00 54.70  ? 15   GLN H OE1 1 
ATOM   7900  N  NE2 . GLN H  1 15  ? 132.799 6.056   30.853 1.00 53.15  ? 15   GLN H NE2 1 
ATOM   7901  N  N   . GLY H  1 16  ? 133.827 7.778   24.756 1.00 25.41  ? 16   GLY H N   1 
ATOM   7902  C  CA  . GLY H  1 16  ? 132.803 7.679   23.716 1.00 25.43  ? 16   GLY H CA  1 
ATOM   7903  C  C   . GLY H  1 16  ? 133.305 6.879   22.531 1.00 23.71  ? 16   GLY H C   1 
ATOM   7904  O  O   . GLY H  1 16  ? 134.395 6.324   22.523 1.00 27.71  ? 16   GLY H O   1 
ATOM   7905  N  N   . ILE H  1 17  ? 132.461 6.820   21.502 1.00 25.67  ? 17   ILE H N   1 
ATOM   7906  C  CA  . ILE H  1 17  ? 132.839 6.099   20.286 1.00 22.34  ? 17   ILE H CA  1 
ATOM   7907  C  C   . ILE H  1 17  ? 132.625 6.999   19.077 1.00 27.05  ? 17   ILE H C   1 
ATOM   7908  O  O   . ILE H  1 17  ? 131.508 7.506   18.938 1.00 26.54  ? 17   ILE H O   1 
ATOM   7909  C  CB  . ILE H  1 17  ? 131.998 4.833   20.129 1.00 21.06  ? 17   ILE H CB  1 
ATOM   7910  C  CG1 . ILE H  1 17  ? 132.371 3.783   21.193 1.00 26.20  ? 17   ILE H CG1 1 
ATOM   7911  C  CG2 . ILE H  1 17  ? 132.069 4.263   18.718 1.00 28.25  ? 17   ILE H CG2 1 
ATOM   7912  C  CD1 . ILE H  1 17  ? 131.214 2.807   21.432 1.00 33.21  ? 17   ILE H CD1 1 
ATOM   7913  N  N   . ILE H  1 18  ? 133.663 7.171   18.267 1.00 23.49  ? 18   ILE H N   1 
ATOM   7914  C  CA  . ILE H  1 18  ? 133.454 8.023   17.094 1.00 26.06  ? 18   ILE H CA  1 
ATOM   7915  C  C   . ILE H  1 18  ? 133.692 7.225   15.818 1.00 26.35  ? 18   ILE H C   1 
ATOM   7916  O  O   . ILE H  1 18  ? 134.685 6.508   15.722 1.00 26.19  ? 18   ILE H O   1 
ATOM   7917  C  CB  . ILE H  1 18  ? 134.393 9.238   17.178 1.00 29.15  ? 18   ILE H CB  1 
ATOM   7918  C  CG1 . ILE H  1 18  ? 134.072 10.128  18.395 1.00 23.52  ? 18   ILE H CG1 1 
ATOM   7919  C  CG2 . ILE H  1 18  ? 134.391 10.038  15.886 1.00 24.15  ? 18   ILE H CG2 1 
ATOM   7920  C  CD1 . ILE H  1 18  ? 132.732 10.832  18.214 1.00 26.44  ? 18   ILE H CD1 1 
ATOM   7921  N  N   . ASN H  1 19  ? 132.757 7.378   14.895 1.00 26.94  ? 19   ASN H N   1 
ATOM   7922  C  CA  . ASN H  1 19  ? 132.763 6.711   13.612 1.00 29.63  ? 19   ASN H CA  1 
ATOM   7923  C  C   . ASN H  1 19  ? 133.193 7.661   12.496 1.00 31.89  ? 19   ASN H C   1 
ATOM   7924  O  O   . ASN H  1 19  ? 132.834 8.838   12.526 1.00 30.33  ? 19   ASN H O   1 
ATOM   7925  C  CB  . ASN H  1 19  ? 131.356 6.201   13.276 1.00 30.79  ? 19   ASN H CB  1 
ATOM   7926  C  CG  . ASN H  1 19  ? 130.806 5.265   14.335 1.00 32.29  ? 19   ASN H CG  1 
ATOM   7927  O  OD1 . ASN H  1 19  ? 131.236 4.116   14.339 1.00 31.90  ? 19   ASN H OD1 1 
ATOM   7928  N  ND2 . ASN H  1 19  ? 129.902 5.713   15.191 1.00 25.71  ? 19   ASN H ND2 1 
ATOM   7929  N  N   . PHE H  1 20  ? 133.913 7.123   11.532 1.00 26.07  ? 20   PHE H N   1 
ATOM   7930  C  CA  . PHE H  1 20  ? 134.299 7.862   10.341 1.00 27.60  ? 20   PHE H CA  1 
ATOM   7931  C  C   . PHE H  1 20  ? 133.848 7.110   9.103  1.00 31.56  ? 20   PHE H C   1 
ATOM   7932  O  O   . PHE H  1 20  ? 134.044 5.887   9.025  1.00 27.70  ? 20   PHE H O   1 
ATOM   7933  C  CB  . PHE H  1 20  ? 135.821 8.033   10.252 1.00 28.54  ? 20   PHE H CB  1 
ATOM   7934  C  CG  . PHE H  1 20  ? 136.504 8.744   11.405 1.00 29.35  ? 20   PHE H CG  1 
ATOM   7935  C  CD1 . PHE H  1 20  ? 136.845 10.079  11.320 1.00 29.75  ? 20   PHE H CD1 1 
ATOM   7936  C  CD2 . PHE H  1 20  ? 136.798 8.058   12.577 1.00 30.25  ? 20   PHE H CD2 1 
ATOM   7937  C  CE1 . PHE H  1 20  ? 137.460 10.748  12.369 1.00 31.02  ? 20   PHE H CE1 1 
ATOM   7938  C  CE2 . PHE H  1 20  ? 137.428 8.712   13.631 1.00 31.49  ? 20   PHE H CE2 1 
ATOM   7939  C  CZ  . PHE H  1 20  ? 137.772 10.044  13.514 1.00 29.18  ? 20   PHE H CZ  1 
ATOM   7940  N  N   . GLU H  1 21  ? 133.276 7.806   8.125  1.00 31.06  ? 21   GLU H N   1 
ATOM   7941  C  CA  . GLU H  1 21  ? 132.920 7.102   6.885  1.00 29.72  ? 21   GLU H CA  1 
ATOM   7942  C  C   . GLU H  1 21  ? 133.337 7.923   5.668  1.00 35.55  ? 21   GLU H C   1 
ATOM   7943  O  O   . GLU H  1 21  ? 133.044 9.128   5.687  1.00 30.48  ? 21   GLU H O   1 
ATOM   7944  C  CB  . GLU H  1 21  ? 131.418 6.797   6.840  1.00 36.92  ? 21   GLU H CB  1 
ATOM   7945  C  CG  . GLU H  1 21  ? 131.006 6.360   5.434  1.00 48.38  ? 21   GLU H CG  1 
ATOM   7946  C  CD  . GLU H  1 21  ? 129.654 5.678   5.407  1.00 65.75  ? 21   GLU H CD  1 
ATOM   7947  O  OE1 . GLU H  1 21  ? 129.074 5.480   6.495  1.00 82.16  ? 21   GLU H OE1 1 
ATOM   7948  O  OE2 . GLU H  1 21  ? 129.186 5.348   4.298  1.00 83.47  ? 21   GLU H OE2 1 
ATOM   7949  N  N   . GLN H  1 22  ? 133.983 7.353   4.659  1.00 31.25  ? 22   GLN H N   1 
ATOM   7950  C  CA  . GLN H  1 22  ? 134.391 8.109   3.466  1.00 33.05  ? 22   GLN H CA  1 
ATOM   7951  C  C   . GLN H  1 22  ? 134.088 7.290   2.215  1.00 40.83  ? 22   GLN H C   1 
ATOM   7952  O  O   . GLN H  1 22  ? 134.843 6.380   1.862  1.00 36.23  ? 22   GLN H O   1 
ATOM   7953  C  CB  . GLN H  1 22  ? 135.867 8.465   3.494  1.00 28.93  ? 22   GLN H CB  1 
ATOM   7954  C  CG  . GLN H  1 22  ? 136.448 9.186   2.284  1.00 28.15  ? 22   GLN H CG  1 
ATOM   7955  C  CD  . GLN H  1 22  ? 137.934 9.463   2.443  1.00 32.41  ? 22   GLN H CD  1 
ATOM   7956  O  OE1 . GLN H  1 22  ? 138.636 8.712   3.124  1.00 40.15  ? 22   GLN H OE1 1 
ATOM   7957  N  NE2 . GLN H  1 22  ? 138.492 10.522  1.862  1.00 33.14  ? 22   GLN H NE2 1 
ATOM   7958  N  N   . LYS H  1 23  ? 132.983 7.623   1.566  1.00 35.88  ? 23   LYS H N   1 
ATOM   7959  C  CA  . LYS H  1 23  ? 132.547 6.829   0.415  1.00 41.92  ? 23   LYS H CA  1 
ATOM   7960  C  C   . LYS H  1 23  ? 133.459 6.991   -0.790 1.00 45.15  ? 23   LYS H C   1 
ATOM   7961  O  O   . LYS H  1 23  ? 133.586 6.091   -1.627 1.00 52.30  ? 23   LYS H O   1 
ATOM   7962  C  CB  . LYS H  1 23  ? 131.097 7.205   0.092  1.00 51.56  ? 23   LYS H CB  1 
ATOM   7963  C  CG  . LYS H  1 23  ? 130.177 6.887   1.267  1.00 66.28  ? 23   LYS H CG  1 
ATOM   7964  C  CD  . LYS H  1 23  ? 128.771 6.544   0.802  1.00 78.54  ? 23   LYS H CD  1 
ATOM   7965  C  CE  . LYS H  1 23  ? 128.641 5.089   0.370  1.00 88.13  ? 23   LYS H CE  1 
ATOM   7966  N  NZ  . LYS H  1 23  ? 127.343 4.826   -0.311 1.00 87.80  ? 23   LYS H NZ  1 
ATOM   7967  N  N   . GLU H  1 24  ? 134.155 8.110   -0.950 1.00 38.27  ? 24   GLU H N   1 
ATOM   7968  C  CA  . GLU H  1 24  ? 135.051 8.258   -2.095 1.00 38.81  ? 24   GLU H CA  1 
ATOM   7969  C  C   . GLU H  1 24  ? 136.464 8.642   -1.669 1.00 40.72  ? 24   GLU H C   1 
ATOM   7970  O  O   . GLU H  1 24  ? 136.640 9.242   -0.610 1.00 47.88  ? 24   GLU H O   1 
ATOM   7971  C  CB  . GLU H  1 24  ? 134.492 9.330   -3.040 1.00 37.07  ? 24   GLU H CB  1 
ATOM   7972  C  CG  . GLU H  1 24  ? 132.976 9.202   -3.188 1.00 52.45  ? 24   GLU H CG  1 
ATOM   7973  C  CD  . GLU H  1 24  ? 132.453 10.151  -4.248 1.00 66.64  ? 24   GLU H CD  1 
ATOM   7974  O  OE1 . GLU H  1 24  ? 131.572 10.969  -3.912 1.00 94.60  ? 24   GLU H OE1 1 
ATOM   7975  O  OE2 . GLU H  1 24  ? 132.945 10.059  -5.393 1.00 75.34  ? 24   GLU H OE2 1 
ATOM   7976  N  N   . SER H  1 25  ? 137.449 8.328   -2.485 1.00 42.10  ? 25   SER H N   1 
ATOM   7977  C  CA  . SER H  1 25  ? 138.870 8.596   -2.299 1.00 45.03  ? 25   SER H CA  1 
ATOM   7978  C  C   . SER H  1 25  ? 139.197 10.039  -1.998 1.00 40.54  ? 25   SER H C   1 
ATOM   7979  O  O   . SER H  1 25  ? 139.942 10.515  -1.146 1.00 50.58  ? 25   SER H O   1 
ATOM   7980  C  CB  . SER H  1 25  ? 139.598 8.201   -3.609 1.00 42.88  ? 25   SER H CB  1 
ATOM   7981  O  OG  . SER H  1 25  ? 140.998 8.373   -3.478 1.00 70.63  ? 25   SER H OG  1 
ATOM   7982  N  N   . ASN H  1 26  ? 138.594 10.895  -2.821 1.00 42.81  ? 26   ASN H N   1 
ATOM   7983  C  CA  . ASN H  1 26  ? 138.892 12.314  -2.587 1.00 54.18  ? 26   ASN H CA  1 
ATOM   7984  C  C   . ASN H  1 26  ? 137.655 12.956  -1.989 1.00 38.03  ? 26   ASN H C   1 
ATOM   7985  O  O   . ASN H  1 26  ? 137.348 14.121  -2.216 1.00 56.11  ? 26   ASN H O   1 
ATOM   7986  C  CB  . ASN H  1 26  ? 139.309 12.928  -3.922 1.00 55.28  ? 26   ASN H CB  1 
ATOM   7987  C  CG  . ASN H  1 26  ? 138.309 12.590  -5.020 1.00 64.35  ? 26   ASN H CG  1 
ATOM   7988  O  OD1 . ASN H  1 26  ? 137.383 11.801  -4.813 1.00 50.10  ? 26   ASN H OD1 1 
ATOM   7989  N  ND2 . ASN H  1 26  ? 138.481 13.195  -6.194 1.00 72.87  ? 26   ASN H ND2 1 
ATOM   7990  N  N   . GLY H  1 27  ? 136.886 12.166  -1.233 1.00 35.22  ? 27   GLY H N   1 
ATOM   7991  C  CA  . GLY H  1 27  ? 135.580 12.668  -0.828 1.00 38.04  ? 27   GLY H CA  1 
ATOM   7992  C  C   . GLY H  1 27  ? 135.583 13.058  0.641  1.00 36.57  ? 27   GLY H C   1 
ATOM   7993  O  O   . GLY H  1 27  ? 136.540 12.749  1.350  1.00 35.29  ? 27   GLY H O   1 
ATOM   7994  N  N   . PRO H  1 28  ? 134.525 13.732  1.073  1.00 35.00  ? 28   PRO H N   1 
ATOM   7995  C  CA  . PRO H  1 28  ? 134.425 14.134  2.475  1.00 32.52  ? 28   PRO H CA  1 
ATOM   7996  C  C   . PRO H  1 28  ? 134.297 12.924  3.391  1.00 27.52  ? 28   PRO H C   1 
ATOM   7997  O  O   . PRO H  1 28  ? 133.780 11.863  3.042  1.00 36.10  ? 28   PRO H O   1 
ATOM   7998  C  CB  . PRO H  1 28  ? 133.143 14.969  2.538  1.00 37.22  ? 28   PRO H CB  1 
ATOM   7999  C  CG  . PRO H  1 28  ? 132.349 14.526  1.362  1.00 41.64  ? 28   PRO H CG  1 
ATOM   8000  C  CD  . PRO H  1 28  ? 133.357 14.171  0.296  1.00 44.69  ? 28   PRO H CD  1 
ATOM   8001  N  N   . VAL H  1 29  ? 134.799 13.130  4.601  1.00 29.07  ? 29   VAL H N   1 
ATOM   8002  C  CA  . VAL H  1 29  ? 134.655 12.111  5.642  1.00 26.13  ? 29   VAL H CA  1 
ATOM   8003  C  C   . VAL H  1 29  ? 133.541 12.520  6.592  1.00 26.24  ? 29   VAL H C   1 
ATOM   8004  O  O   . VAL H  1 29  ? 133.551 13.635  7.124  1.00 29.27  ? 29   VAL H O   1 
ATOM   8005  C  CB  . VAL H  1 29  ? 135.979 11.951  6.407  1.00 28.97  ? 29   VAL H CB  1 
ATOM   8006  C  CG1 . VAL H  1 29  ? 135.844 10.910  7.502  1.00 26.83  ? 29   VAL H CG1 1 
ATOM   8007  C  CG2 . VAL H  1 29  ? 137.091 11.599  5.431  1.00 35.30  ? 29   VAL H CG2 1 
ATOM   8008  N  N   . LYS H  1 30  ? 132.590 11.622  6.813  1.00 24.85  ? 30   LYS H N   1 
ATOM   8009  C  CA  . LYS H  1 30  ? 131.543 11.917  7.805  1.00 27.58  ? 30   LYS H CA  1 
ATOM   8010  C  C   . LYS H  1 30  ? 132.054 11.379  9.145  1.00 36.07  ? 30   LYS H C   1 
ATOM   8011  O  O   . LYS H  1 30  ? 132.616 10.279  9.201  1.00 33.04  ? 30   LYS H O   1 
ATOM   8012  C  CB  . LYS H  1 30  ? 130.219 11.312  7.407  1.00 35.24  ? 30   LYS H CB  1 
ATOM   8013  C  CG  . LYS H  1 30  ? 129.965 11.314  5.904  1.00 58.76  ? 30   LYS H CG  1 
ATOM   8014  C  CD  . LYS H  1 30  ? 129.460 12.652  5.395  1.00 71.04  ? 30   LYS H CD  1 
ATOM   8015  C  CE  . LYS H  1 30  ? 128.784 12.513  4.036  1.00 80.02  ? 30   LYS H CE  1 
ATOM   8016  N  NZ  . LYS H  1 30  ? 127.333 12.169  4.165  1.00 79.70  ? 30   LYS H NZ  1 
ATOM   8017  N  N   . VAL H  1 31  ? 131.888 12.175  10.181 1.00 26.13  ? 31   VAL H N   1 
ATOM   8018  C  CA  . VAL H  1 31  ? 132.407 11.862  11.518 1.00 30.49  ? 31   VAL H CA  1 
ATOM   8019  C  C   . VAL H  1 31  ? 131.235 11.940  12.484 1.00 35.03  ? 31   VAL H C   1 
ATOM   8020  O  O   . VAL H  1 31  ? 130.627 13.013  12.568 1.00 32.15  ? 31   VAL H O   1 
ATOM   8021  C  CB  . VAL H  1 31  ? 133.534 12.812  11.936 1.00 29.34  ? 31   VAL H CB  1 
ATOM   8022  C  CG1 . VAL H  1 31  ? 134.138 12.413  13.282 1.00 39.66  ? 31   VAL H CG1 1 
ATOM   8023  C  CG2 . VAL H  1 31  ? 134.643 12.841  10.901 1.00 27.77  ? 31   VAL H CG2 1 
ATOM   8024  N  N   . TRP H  1 32  ? 130.892 10.830  13.156 1.00 29.04  ? 32   TRP H N   1 
ATOM   8025  C  CA  . TRP H  1 32  ? 129.727 10.891  14.028 1.00 28.62  ? 32   TRP H CA  1 
ATOM   8026  C  C   . TRP H  1 32  ? 129.857 9.897   15.188 1.00 32.09  ? 32   TRP H C   1 
ATOM   8027  O  O   . TRP H  1 32  ? 130.607 8.930   15.118 1.00 29.01  ? 32   TRP H O   1 
ATOM   8028  C  CB  . TRP H  1 32  ? 128.438 10.624  13.252 1.00 29.75  ? 32   TRP H CB  1 
ATOM   8029  C  CG  . TRP H  1 32  ? 128.270 9.183   12.880 1.00 34.17  ? 32   TRP H CG  1 
ATOM   8030  C  CD1 . TRP H  1 32  ? 127.490 8.212   13.448 1.00 35.90  ? 32   TRP H CD1 1 
ATOM   8031  C  CD2 . TRP H  1 32  ? 128.961 8.557   11.789 1.00 35.97  ? 32   TRP H CD2 1 
ATOM   8032  N  NE1 . TRP H  1 32  ? 127.656 7.026   12.772 1.00 38.00  ? 32   TRP H NE1 1 
ATOM   8033  C  CE2 . TRP H  1 32  ? 128.552 7.208   11.753 1.00 38.54  ? 32   TRP H CE2 1 
ATOM   8034  C  CE3 . TRP H  1 32  ? 129.886 9.036   10.860 1.00 42.19  ? 32   TRP H CE3 1 
ATOM   8035  C  CZ2 . TRP H  1 32  ? 129.036 6.309   10.807 1.00 46.01  ? 32   TRP H CZ2 1 
ATOM   8036  C  CZ3 . TRP H  1 32  ? 130.361 8.134   9.920  1.00 52.80  ? 32   TRP H CZ3 1 
ATOM   8037  C  CH2 . TRP H  1 32  ? 129.938 6.799   9.904  1.00 52.49  ? 32   TRP H CH2 1 
ATOM   8038  N  N   . GLY H  1 33  ? 129.108 10.174  16.259 1.00 26.88  ? 33   GLY H N   1 
ATOM   8039  C  CA  . GLY H  1 33  ? 129.149 9.281   17.409 1.00 29.04  ? 33   GLY H CA  1 
ATOM   8040  C  C   . GLY H  1 33  ? 128.798 10.052  18.657 1.00 29.53  ? 33   GLY H C   1 
ATOM   8041  O  O   . GLY H  1 33  ? 128.252 11.132  18.563 1.00 32.79  ? 33   GLY H O   1 
ATOM   8042  N  N   . SER H  1 34  ? 129.103 9.507   19.825 1.00 26.67  ? 34   SER H N   1 
ATOM   8043  C  CA  . SER H  1 34  ? 128.633 10.146  21.043 1.00 21.14  ? 34   SER H CA  1 
ATOM   8044  C  C   . SER H  1 34  ? 129.798 10.163  22.034 1.00 23.60  ? 34   SER H C   1 
ATOM   8045  O  O   . SER H  1 34  ? 130.464 9.139   22.119 1.00 27.22  ? 34   SER H O   1 
ATOM   8046  C  CB  . SER H  1 34  ? 127.470 9.362   21.649 1.00 32.99  ? 34   SER H CB  1 
ATOM   8047  O  OG  . SER H  1 34  ? 126.991 10.016  22.823 1.00 40.67  ? 34   SER H OG  1 
ATOM   8048  N  N   . ILE H  1 35  ? 129.990 11.251  22.728 1.00 23.45  ? 35   ILE H N   1 
ATOM   8049  C  CA  . ILE H  1 35  ? 130.993 11.405  23.780 1.00 20.19  ? 35   ILE H CA  1 
ATOM   8050  C  C   . ILE H  1 35  ? 130.227 11.845  25.016 1.00 23.26  ? 35   ILE H C   1 
ATOM   8051  O  O   . ILE H  1 35  ? 129.417 12.774  24.952 1.00 25.84  ? 35   ILE H O   1 
ATOM   8052  C  CB  . ILE H  1 35  ? 132.069 12.438  23.435 1.00 22.75  ? 35   ILE H CB  1 
ATOM   8053  C  CG1 . ILE H  1 35  ? 132.658 12.217  22.027 1.00 25.66  ? 35   ILE H CG1 1 
ATOM   8054  C  CG2 . ILE H  1 35  ? 133.172 12.463  24.484 1.00 21.21  ? 35   ILE H CG2 1 
ATOM   8055  C  CD1 . ILE H  1 35  ? 133.610 13.324  21.628 1.00 23.87  ? 35   ILE H CD1 1 
ATOM   8056  N  N   . LYS H  1 36  ? 130.456 11.140  26.118 1.00 23.67  ? 36   LYS H N   1 
ATOM   8057  C  CA  . LYS H  1 36  ? 129.752 11.530  27.333 1.00 22.37  ? 36   LYS H CA  1 
ATOM   8058  C  C   . LYS H  1 36  ? 130.797 11.920  28.383 1.00 22.22  ? 36   LYS H C   1 
ATOM   8059  O  O   . LYS H  1 36  ? 131.973 11.677  28.152 1.00 23.13  ? 36   LYS H O   1 
ATOM   8060  C  CB  . LYS H  1 36  ? 128.865 10.402  27.844 1.00 28.26  ? 36   LYS H CB  1 
ATOM   8061  C  CG  . LYS H  1 36  ? 129.622 9.177   28.310 1.00 32.60  ? 36   LYS H CG  1 
ATOM   8062  C  CD  . LYS H  1 36  ? 128.627 8.028   28.526 1.00 41.87  ? 36   LYS H CD  1 
ATOM   8063  C  CE  . LYS H  1 36  ? 129.244 6.926   29.381 1.00 47.78  ? 36   LYS H CE  1 
ATOM   8064  N  NZ  . LYS H  1 36  ? 128.259 5.845   29.706 1.00 41.68  ? 36   LYS H NZ  1 
ATOM   8065  N  N   . GLY H  1 37  ? 130.283 12.501  29.461 1.00 25.14  ? 37   GLY H N   1 
ATOM   8066  C  CA  . GLY H  1 37  ? 131.090 12.893  30.589 1.00 25.87  ? 37   GLY H CA  1 
ATOM   8067  C  C   . GLY H  1 37  ? 131.756 14.248  30.445 1.00 24.43  ? 37   GLY H C   1 
ATOM   8068  O  O   . GLY H  1 37  ? 132.620 14.582  31.265 1.00 25.63  ? 37   GLY H O   1 
ATOM   8069  N  N   . LEU H  1 38  ? 131.376 15.030  29.440 1.00 23.95  ? 38   LEU H N   1 
ATOM   8070  C  CA  . LEU H  1 38  ? 131.931 16.338  29.162 1.00 25.03  ? 38   LEU H CA  1 
ATOM   8071  C  C   . LEU H  1 38  ? 131.223 17.464  29.882 1.00 24.63  ? 38   LEU H C   1 
ATOM   8072  O  O   . LEU H  1 38  ? 130.047 17.323  30.177 1.00 27.69  ? 38   LEU H O   1 
ATOM   8073  C  CB  . LEU H  1 38  ? 131.778 16.646  27.648 1.00 22.94  ? 38   LEU H CB  1 
ATOM   8074  C  CG  . LEU H  1 38  ? 132.749 15.851  26.769 1.00 22.63  ? 38   LEU H CG  1 
ATOM   8075  C  CD1 . LEU H  1 38  ? 132.243 15.833  25.337 1.00 23.89  ? 38   LEU H CD1 1 
ATOM   8076  C  CD2 . LEU H  1 38  ? 134.158 16.423  26.846 1.00 25.07  ? 38   LEU H CD2 1 
ATOM   8077  N  N   . THR H  1 39  ? 131.889 18.580  30.152 1.00 24.50  ? 39   THR H N   1 
ATOM   8078  C  CA  . THR H  1 39  ? 131.180 19.757  30.612 1.00 24.96  ? 39   THR H CA  1 
ATOM   8079  C  C   . THR H  1 39  ? 130.357 20.342  29.468 1.00 27.31  ? 39   THR H C   1 
ATOM   8080  O  O   . THR H  1 39  ? 130.759 20.327  28.305 1.00 26.49  ? 39   THR H O   1 
ATOM   8081  C  CB  . THR H  1 39  ? 132.118 20.870  31.110 1.00 28.01  ? 39   THR H CB  1 
ATOM   8082  O  OG1 . THR H  1 39  ? 133.002 21.181  30.030 1.00 27.67  ? 39   THR H OG1 1 
ATOM   8083  C  CG2 . THR H  1 39  ? 132.949 20.396  32.295 1.00 24.88  ? 39   THR H CG2 1 
ATOM   8084  N  N   . GLU H  1 40  ? 129.193 20.876  29.798 1.00 24.85  ? 40   GLU H N   1 
ATOM   8085  C  CA  . GLU H  1 40  ? 128.347 21.486  28.765 1.00 27.98  ? 40   GLU H CA  1 
ATOM   8086  C  C   . GLU H  1 40  ? 129.096 22.551  27.980 1.00 29.29  ? 40   GLU H C   1 
ATOM   8087  O  O   . GLU H  1 40  ? 129.813 23.387  28.533 1.00 26.18  ? 40   GLU H O   1 
ATOM   8088  C  CB  . GLU H  1 40  ? 127.086 22.017  29.443 1.00 28.95  ? 40   GLU H CB  1 
ATOM   8089  C  CG  . GLU H  1 40  ? 126.129 22.739  28.503 1.00 29.22  ? 40   GLU H CG  1 
ATOM   8090  C  CD  . GLU H  1 40  ? 124.962 23.351  29.264 1.00 40.65  ? 40   GLU H CD  1 
ATOM   8091  O  OE1 . GLU H  1 40  ? 123.985 23.769  28.610 1.00 46.29  ? 40   GLU H OE1 1 
ATOM   8092  O  OE2 . GLU H  1 40  ? 125.038 23.395  30.507 1.00 38.40  ? 40   GLU H OE2 1 
ATOM   8093  N  N   . GLY H  1 41  ? 128.956 22.549  26.645 1.00 22.10  ? 41   GLY H N   1 
ATOM   8094  C  CA  . GLY H  1 41  ? 129.597 23.632  25.884 1.00 23.57  ? 41   GLY H CA  1 
ATOM   8095  C  C   . GLY H  1 41  ? 130.599 23.084  24.875 1.00 24.87  ? 41   GLY H C   1 
ATOM   8096  O  O   . GLY H  1 41  ? 130.599 21.887  24.579 1.00 23.04  ? 41   GLY H O   1 
ATOM   8097  N  N   . LEU H  1 42  ? 131.475 23.945  24.372 1.00 24.62  ? 42   LEU H N   1 
ATOM   8098  C  CA  . LEU H  1 42  ? 132.424 23.644  23.305 1.00 22.28  ? 42   LEU H CA  1 
ATOM   8099  C  C   . LEU H  1 42  ? 133.680 22.935  23.775 1.00 28.58  ? 42   LEU H C   1 
ATOM   8100  O  O   . LEU H  1 42  ? 134.279 23.325  24.781 1.00 24.58  ? 42   LEU H O   1 
ATOM   8101  C  CB  . LEU H  1 42  ? 132.900 24.949  22.624 1.00 26.70  ? 42   LEU H CB  1 
ATOM   8102  C  CG  . LEU H  1 42  ? 131.864 25.704  21.797 1.00 28.08  ? 42   LEU H CG  1 
ATOM   8103  C  CD1 . LEU H  1 42  ? 132.347 27.128  21.492 1.00 34.85  ? 42   LEU H CD1 1 
ATOM   8104  C  CD2 . LEU H  1 42  ? 131.526 24.984  20.499 1.00 22.02  ? 42   LEU H CD2 1 
ATOM   8105  N  N   . HIS H  1 43  ? 134.114 21.913  23.039 1.00 24.34  ? 43   HIS H N   1 
ATOM   8106  C  CA  . HIS H  1 43  ? 135.363 21.221  23.307 1.00 20.57  ? 43   HIS H CA  1 
ATOM   8107  C  C   . HIS H  1 43  ? 136.202 21.030  22.046 1.00 22.62  ? 43   HIS H C   1 
ATOM   8108  O  O   . HIS H  1 43  ? 135.685 20.518  21.059 1.00 23.18  ? 43   HIS H O   1 
ATOM   8109  C  CB  . HIS H  1 43  ? 135.037 19.848  23.918 1.00 21.10  ? 43   HIS H CB  1 
ATOM   8110  C  CG  . HIS H  1 43  ? 134.424 19.982  25.282 1.00 24.91  ? 43   HIS H CG  1 
ATOM   8111  N  ND1 . HIS H  1 43  ? 135.206 20.024  26.422 1.00 26.03  ? 43   HIS H ND1 1 
ATOM   8112  C  CD2 . HIS H  1 43  ? 133.139 20.121  25.671 1.00 27.03  ? 43   HIS H CD2 1 
ATOM   8113  C  CE1 . HIS H  1 43  ? 134.402 20.160  27.469 1.00 29.31  ? 43   HIS H CE1 1 
ATOM   8114  N  NE2 . HIS H  1 43  ? 133.143 20.223  27.045 1.00 29.03  ? 43   HIS H NE2 1 
ATOM   8115  N  N   . GLY H  1 44  ? 137.478 21.413  22.054 1.00 23.74  ? 44   GLY H N   1 
ATOM   8116  C  CA  . GLY H  1 44  ? 138.321 21.193  20.880 1.00 21.71  ? 44   GLY H CA  1 
ATOM   8117  C  C   . GLY H  1 44  ? 138.369 19.721  20.511 1.00 27.31  ? 44   GLY H C   1 
ATOM   8118  O  O   . GLY H  1 44  ? 138.233 18.830  21.345 1.00 23.01  ? 44   GLY H O   1 
ATOM   8119  N  N   . PHE H  1 45  ? 138.564 19.427  19.230 1.00 21.69  ? 45   PHE H N   1 
ATOM   8120  C  CA  . PHE H  1 45  ? 138.407 18.064  18.706 1.00 18.10  ? 45   PHE H CA  1 
ATOM   8121  C  C   . PHE H  1 45  ? 139.351 17.930  17.517 1.00 22.99  ? 45   PHE H C   1 
ATOM   8122  O  O   . PHE H  1 45  ? 139.102 18.554  16.476 1.00 22.51  ? 45   PHE H O   1 
ATOM   8123  C  CB  . PHE H  1 45  ? 136.947 17.901  18.318 1.00 19.43  ? 45   PHE H CB  1 
ATOM   8124  C  CG  . PHE H  1 45  ? 136.469 16.512  17.964 1.00 22.99  ? 45   PHE H CG  1 
ATOM   8125  C  CD1 . PHE H  1 45  ? 136.511 15.489  18.900 1.00 21.28  ? 45   PHE H CD1 1 
ATOM   8126  C  CD2 . PHE H  1 45  ? 135.978 16.247  16.693 1.00 24.35  ? 45   PHE H CD2 1 
ATOM   8127  C  CE1 . PHE H  1 45  ? 136.070 14.221  18.578 1.00 22.89  ? 45   PHE H CE1 1 
ATOM   8128  C  CE2 . PHE H  1 45  ? 135.513 14.977  16.366 1.00 27.79  ? 45   PHE H CE2 1 
ATOM   8129  C  CZ  . PHE H  1 45  ? 135.546 13.964  17.316 1.00 25.62  ? 45   PHE H CZ  1 
ATOM   8130  N  N   . HIS H  1 46  ? 140.466 17.214  17.620 1.00 20.87  ? 46   HIS H N   1 
ATOM   8131  C  CA  . HIS H  1 46  ? 141.452 17.136  16.540 1.00 23.11  ? 46   HIS H CA  1 
ATOM   8132  C  C   . HIS H  1 46  ? 142.079 15.751  16.400 1.00 26.33  ? 46   HIS H C   1 
ATOM   8133  O  O   . HIS H  1 46  ? 142.098 15.012  17.379 1.00 23.36  ? 46   HIS H O   1 
ATOM   8134  C  CB  . HIS H  1 46  ? 142.670 18.051  16.759 1.00 24.59  ? 46   HIS H CB  1 
ATOM   8135  C  CG  . HIS H  1 46  ? 142.341 19.288  17.532 1.00 23.86  ? 46   HIS H CG  1 
ATOM   8136  N  ND1 . HIS H  1 46  ? 142.692 19.469  18.840 1.00 23.12  ? 46   HIS H ND1 1 
ATOM   8137  C  CD2 . HIS H  1 46  ? 141.651 20.385  17.144 1.00 22.78  ? 46   HIS H CD2 1 
ATOM   8138  C  CE1 . HIS H  1 46  ? 142.247 20.649  19.243 1.00 25.75  ? 46   HIS H CE1 1 
ATOM   8139  N  NE2 . HIS H  1 46  ? 141.607 21.231  18.238 1.00 25.01  ? 46   HIS H NE2 1 
ATOM   8140  N  N   . VAL H  1 47  ? 142.599 15.477  15.221 1.00 23.76  ? 47   VAL H N   1 
ATOM   8141  C  CA  . VAL H  1 47  ? 143.484 14.333  14.979 1.00 24.41  ? 47   VAL H CA  1 
ATOM   8142  C  C   . VAL H  1 47  ? 144.914 14.761  15.252 1.00 23.93  ? 47   VAL H C   1 
ATOM   8143  O  O   . VAL H  1 47  ? 145.386 15.722  14.651 1.00 25.35  ? 47   VAL H O   1 
ATOM   8144  C  CB  . VAL H  1 47  ? 143.372 13.812  13.534 1.00 24.99  ? 47   VAL H CB  1 
ATOM   8145  C  CG1 . VAL H  1 47  ? 144.287 12.608  13.324 1.00 22.25  ? 47   VAL H CG1 1 
ATOM   8146  C  CG2 . VAL H  1 47  ? 141.918 13.469  13.243 1.00 25.77  ? 47   VAL H CG2 1 
ATOM   8147  N  N   . HIS H  1 48  ? 145.587 14.098  16.170 1.00 22.47  ? 48   HIS H N   1 
ATOM   8148  C  CA  . HIS H  1 48  ? 146.958 14.328  16.566 1.00 20.27  ? 48   HIS H CA  1 
ATOM   8149  C  C   . HIS H  1 48  ? 147.837 13.277  15.862 1.00 22.71  ? 48   HIS H C   1 
ATOM   8150  O  O   . HIS H  1 48  ? 147.301 12.251  15.434 1.00 26.89  ? 48   HIS H O   1 
ATOM   8151  C  CB  . HIS H  1 48  ? 147.139 14.248  18.080 1.00 24.38  ? 48   HIS H CB  1 
ATOM   8152  C  CG  . HIS H  1 48  ? 146.580 15.412  18.837 1.00 20.86  ? 48   HIS H CG  1 
ATOM   8153  N  ND1 . HIS H  1 48  ? 147.312 16.155  19.722 1.00 24.42  ? 48   HIS H ND1 1 
ATOM   8154  C  CD2 . HIS H  1 48  ? 145.327 15.952  18.855 1.00 24.39  ? 48   HIS H CD2 1 
ATOM   8155  C  CE1 . HIS H  1 48  ? 146.552 17.125  20.242 1.00 28.48  ? 48   HIS H CE1 1 
ATOM   8156  N  NE2 . HIS H  1 48  ? 145.339 17.016  19.735 1.00 23.93  ? 48   HIS H NE2 1 
ATOM   8157  N  N   . GLU H  1 49  ? 149.117 13.569  15.747 1.00 27.26  ? 49   GLU H N   1 
ATOM   8158  C  CA  . GLU H  1 49  ? 150.069 12.964  14.858 1.00 28.85  ? 49   GLU H CA  1 
ATOM   8159  C  C   . GLU H  1 49  ? 150.300 11.486  15.144 1.00 29.63  ? 49   GLU H C   1 
ATOM   8160  O  O   . GLU H  1 49  ? 150.299 10.678  14.223 1.00 29.19  ? 49   GLU H O   1 
ATOM   8161  C  CB  . GLU H  1 49  ? 151.413 13.725  14.941 1.00 27.95  ? 49   GLU H CB  1 
ATOM   8162  C  CG  . GLU H  1 49  ? 152.425 13.187  13.932 1.00 32.80  ? 49   GLU H CG  1 
ATOM   8163  C  CD  . GLU H  1 49  ? 153.649 14.067  13.756 1.00 37.75  ? 49   GLU H CD  1 
ATOM   8164  O  OE1 . GLU H  1 49  ? 154.416 13.797  12.804 1.00 40.07  ? 49   GLU H OE1 1 
ATOM   8165  O  OE2 . GLU H  1 49  ? 153.885 15.008  14.538 1.00 36.29  ? 49   GLU H OE2 1 
ATOM   8166  N  N   . PHE H  1 50  ? 150.526 11.149  16.406 1.00 29.79  ? 50   PHE H N   1 
ATOM   8167  C  CA  . PHE H  1 50  ? 150.953 9.782   16.718 1.00 33.07  ? 50   PHE H CA  1 
ATOM   8168  C  C   . PHE H  1 50  ? 149.856 8.955   17.369 1.00 28.92  ? 50   PHE H C   1 
ATOM   8169  O  O   . PHE H  1 50  ? 149.184 9.470   18.261 1.00 31.12  ? 50   PHE H O   1 
ATOM   8170  C  CB  . PHE H  1 50  ? 152.155 9.837   17.672 1.00 30.57  ? 50   PHE H CB  1 
ATOM   8171  C  CG  . PHE H  1 50  ? 153.289 10.692  17.114 1.00 27.18  ? 50   PHE H CG  1 
ATOM   8172  C  CD1 . PHE H  1 50  ? 153.877 10.359  15.905 1.00 40.89  ? 50   PHE H CD1 1 
ATOM   8173  C  CD2 . PHE H  1 50  ? 153.718 11.787  17.831 1.00 26.07  ? 50   PHE H CD2 1 
ATOM   8174  C  CE1 . PHE H  1 50  ? 154.914 11.131  15.382 1.00 36.36  ? 50   PHE H CE1 1 
ATOM   8175  C  CE2 . PHE H  1 50  ? 154.737 12.577  17.310 1.00 39.50  ? 50   PHE H CE2 1 
ATOM   8176  C  CZ  . PHE H  1 50  ? 155.302 12.248  16.094 1.00 33.46  ? 50   PHE H CZ  1 
ATOM   8177  N  N   . GLY H  1 51  ? 149.713 7.713   16.938 1.00 23.52  ? 51   GLY H N   1 
ATOM   8178  C  CA  . GLY H  1 51  ? 148.790 6.763   17.538 1.00 22.99  ? 51   GLY H CA  1 
ATOM   8179  C  C   . GLY H  1 51  ? 149.486 6.051   18.697 1.00 30.82  ? 51   GLY H C   1 
ATOM   8180  O  O   . GLY H  1 51  ? 149.495 4.816   18.742 1.00 34.44  ? 51   GLY H O   1 
ATOM   8181  N  N   . ASP H  1 52  ? 150.059 6.858   19.576 1.00 30.42  ? 52   ASP H N   1 
ATOM   8182  C  CA  . ASP H  1 52  ? 150.877 6.402   20.697 1.00 31.78  ? 52   ASP H CA  1 
ATOM   8183  C  C   . ASP H  1 52  ? 150.230 6.728   22.040 1.00 31.97  ? 52   ASP H C   1 
ATOM   8184  O  O   . ASP H  1 52  ? 150.220 7.874   22.492 1.00 32.28  ? 52   ASP H O   1 
ATOM   8185  C  CB  . ASP H  1 52  ? 152.270 7.023   20.618 1.00 34.11  ? 52   ASP H CB  1 
ATOM   8186  C  CG  . ASP H  1 52  ? 153.243 6.485   21.648 1.00 36.95  ? 52   ASP H CG  1 
ATOM   8187  O  OD1 . ASP H  1 52  ? 154.448 6.519   21.333 1.00 37.77  ? 52   ASP H OD1 1 
ATOM   8188  O  OD2 . ASP H  1 52  ? 152.843 6.032   22.744 1.00 34.26  ? 52   ASP H OD2 1 
ATOM   8189  N  N   . ASN H  1 53  ? 149.693 5.678   22.656 1.00 29.06  ? 53   ASN H N   1 
ATOM   8190  C  CA  . ASN H  1 53  ? 149.031 5.822   23.949 1.00 31.09  ? 53   ASN H CA  1 
ATOM   8191  C  C   . ASN H  1 53  ? 149.892 5.362   25.112 1.00 34.77  ? 53   ASN H C   1 
ATOM   8192  O  O   . ASN H  1 53  ? 149.340 5.102   26.181 1.00 30.52  ? 53   ASN H O   1 
ATOM   8193  C  CB  . ASN H  1 53  ? 147.731 5.018   23.927 1.00 36.89  ? 53   ASN H CB  1 
ATOM   8194  C  CG  . ASN H  1 53  ? 146.812 5.441   25.063 1.00 55.07  ? 53   ASN H CG  1 
ATOM   8195  O  OD1 . ASN H  1 53  ? 146.128 4.600   25.648 1.00 41.61  ? 53   ASN H OD1 1 
ATOM   8196  N  ND2 . ASN H  1 53  ? 146.847 6.735   25.372 1.00 39.55  ? 53   ASN H ND2 1 
ATOM   8197  N  N   . THR H  1 54  ? 151.207 5.258   24.931 1.00 30.01  ? 54   THR H N   1 
ATOM   8198  C  CA  . THR H  1 54  ? 152.051 4.711   25.992 1.00 34.86  ? 54   THR H CA  1 
ATOM   8199  C  C   . THR H  1 54  ? 152.088 5.615   27.215 1.00 40.51  ? 54   THR H C   1 
ATOM   8200  O  O   . THR H  1 54  ? 152.323 5.147   28.326 1.00 48.84  ? 54   THR H O   1 
ATOM   8201  C  CB  . THR H  1 54  ? 153.512 4.475   25.566 1.00 33.56  ? 54   THR H CB  1 
ATOM   8202  O  OG1 . THR H  1 54  ? 154.049 5.656   24.967 1.00 38.15  ? 54   THR H OG1 1 
ATOM   8203  C  CG2 . THR H  1 54  ? 153.598 3.394   24.496 1.00 42.84  ? 54   THR H CG2 1 
ATOM   8204  N  N   . ALA H  1 55  ? 151.862 6.908   27.025 1.00 38.19  ? 55   ALA H N   1 
ATOM   8205  C  CA  . ALA H  1 55  ? 151.783 7.822   28.151 1.00 29.74  ? 55   ALA H CA  1 
ATOM   8206  C  C   . ALA H  1 55  ? 150.454 8.553   28.166 1.00 32.83  ? 55   ALA H C   1 
ATOM   8207  O  O   . ALA H  1 55  ? 150.383 9.767   28.372 1.00 40.39  ? 55   ALA H O   1 
ATOM   8208  C  CB  . ALA H  1 55  ? 152.934 8.821   28.111 1.00 29.97  ? 55   ALA H CB  1 
ATOM   8209  N  N   . GLY H  1 56  ? 149.356 7.836   27.949 1.00 33.09  ? 56   GLY H N   1 
ATOM   8210  C  CA  . GLY H  1 56  ? 148.081 8.566   28.010 1.00 33.02  ? 56   GLY H CA  1 
ATOM   8211  C  C   . GLY H  1 56  ? 147.964 9.445   26.770 1.00 36.93  ? 56   GLY H C   1 
ATOM   8212  O  O   . GLY H  1 56  ? 148.594 9.164   25.746 1.00 31.84  ? 56   GLY H O   1 
ATOM   8213  N  N   . CYS H  1 57  ? 147.163 10.506  26.849 1.00 29.70  ? 57   CYS H N   1 
ATOM   8214  C  CA  . CYS H  1 57  ? 146.963 11.277  25.621 1.00 29.25  ? 57   CYS H CA  1 
ATOM   8215  C  C   . CYS H  1 57  ? 148.156 12.147  25.282 1.00 29.52  ? 57   CYS H C   1 
ATOM   8216  O  O   . CYS H  1 57  ? 148.304 12.615  24.147 1.00 29.58  ? 57   CYS H O   1 
ATOM   8217  C  CB  A CYS H  1 57  ? 145.725 12.167  25.811 0.43 31.60  ? 57   CYS H CB  1 
ATOM   8218  C  CB  B CYS H  1 57  ? 145.647 12.052  25.722 0.57 37.16  ? 57   CYS H CB  1 
ATOM   8219  S  SG  A CYS H  1 57  ? 144.195 11.212  25.983 0.43 40.38  ? 57   CYS H SG  1 
ATOM   8220  S  SG  B CYS H  1 57  ? 144.248 11.055  26.304 0.57 42.92  ? 57   CYS H SG  1 
ATOM   8221  N  N   . THR H  1 58  ? 149.061 12.368  26.229 1.00 30.89  ? 58   THR H N   1 
ATOM   8222  C  CA  . THR H  1 58  ? 150.252 13.180  25.966 1.00 29.23  ? 58   THR H CA  1 
ATOM   8223  C  C   . THR H  1 58  ? 151.147 12.661  24.858 1.00 32.77  ? 58   THR H C   1 
ATOM   8224  O  O   . THR H  1 58  ? 151.726 13.431  24.085 1.00 31.57  ? 58   THR H O   1 
ATOM   8225  C  CB  . THR H  1 58  ? 151.109 13.229  27.251 1.00 35.61  ? 58   THR H CB  1 
ATOM   8226  O  OG1 . THR H  1 58  ? 150.246 13.560  28.339 1.00 47.57  ? 58   THR H OG1 1 
ATOM   8227  C  CG2 . THR H  1 58  ? 152.188 14.299  27.148 1.00 36.45  ? 58   THR H CG2 1 
ATOM   8228  N  N   . SER H  1 59  ? 151.301 11.330  24.766 1.00 28.97  ? 59   SER H N   1 
ATOM   8229  C  CA  . SER H  1 59  ? 152.262 10.805  23.795 1.00 28.35  ? 59   SER H CA  1 
ATOM   8230  C  C   . SER H  1 59  ? 151.652 10.802  22.402 1.00 32.67  ? 59   SER H C   1 
ATOM   8231  O  O   . SER H  1 59  ? 152.308 10.268  21.504 1.00 35.68  ? 59   SER H O   1 
ATOM   8232  C  CB  . SER H  1 59  ? 152.752 9.404   24.180 1.00 26.89  ? 59   SER H CB  1 
ATOM   8233  O  OG  . SER H  1 59  ? 151.640 8.602   24.553 1.00 34.92  ? 59   SER H OG  1 
ATOM   8234  N  N   . ALA H  1 60  ? 150.459 11.383  22.222 1.00 31.68  ? 60   ALA H N   1 
ATOM   8235  C  CA  . ALA H  1 60  ? 149.875 11.553  20.896 1.00 26.03  ? 60   ALA H CA  1 
ATOM   8236  C  C   . ALA H  1 60  ? 150.561 12.646  20.061 1.00 28.79  ? 60   ALA H C   1 
ATOM   8237  O  O   . ALA H  1 60  ? 150.316 12.741  18.844 1.00 29.22  ? 60   ALA H O   1 
ATOM   8238  C  CB  . ALA H  1 60  ? 148.393 11.888  20.978 1.00 28.92  ? 60   ALA H CB  1 
ATOM   8239  N  N   . GLY H  1 61  ? 151.391 13.451  20.690 1.00 28.93  ? 61   GLY H N   1 
ATOM   8240  C  CA  . GLY H  1 61  ? 152.133 14.522  20.009 1.00 27.00  ? 61   GLY H CA  1 
ATOM   8241  C  C   . GLY H  1 61  ? 151.171 15.638  19.615 1.00 33.13  ? 61   GLY H C   1 
ATOM   8242  O  O   . GLY H  1 61  ? 150.085 15.772  20.182 1.00 27.83  ? 61   GLY H O   1 
ATOM   8243  N  N   . PRO H  1 62  ? 151.580 16.456  18.667 1.00 33.11  ? 62   PRO H N   1 
ATOM   8244  C  CA  . PRO H  1 62  ? 150.796 17.635  18.280 1.00 27.45  ? 62   PRO H CA  1 
ATOM   8245  C  C   . PRO H  1 62  ? 149.764 17.334  17.223 1.00 26.65  ? 62   PRO H C   1 
ATOM   8246  O  O   . PRO H  1 62  ? 149.571 16.210  16.771 1.00 24.61  ? 62   PRO H O   1 
ATOM   8247  C  CB  . PRO H  1 62  ? 151.900 18.552  17.708 1.00 28.18  ? 62   PRO H CB  1 
ATOM   8248  C  CG  . PRO H  1 62  ? 152.761 17.558  16.978 1.00 29.16  ? 62   PRO H CG  1 
ATOM   8249  C  CD  . PRO H  1 62  ? 152.843 16.361  17.905 1.00 35.63  ? 62   PRO H CD  1 
ATOM   8250  N  N   . HIS H  1 63  ? 149.038 18.390  16.816 1.00 24.83  ? 63   HIS H N   1 
ATOM   8251  C  CA  . HIS H  1 63  ? 148.039 18.173  15.802 1.00 22.51  ? 63   HIS H CA  1 
ATOM   8252  C  C   . HIS H  1 63  ? 148.637 17.584  14.528 1.00 24.17  ? 63   HIS H C   1 
ATOM   8253  O  O   . HIS H  1 63  ? 149.758 17.934  14.161 1.00 28.12  ? 63   HIS H O   1 
ATOM   8254  C  CB  . HIS H  1 63  ? 147.329 19.493  15.466 1.00 26.43  ? 63   HIS H CB  1 
ATOM   8255  C  CG  . HIS H  1 63  ? 146.556 20.073  16.606 1.00 29.22  ? 63   HIS H CG  1 
ATOM   8256  N  ND1 . HIS H  1 63  ? 145.757 21.194  16.449 1.00 28.69  ? 63   HIS H ND1 1 
ATOM   8257  C  CD2 . HIS H  1 63  ? 146.466 19.720  17.904 1.00 27.92  ? 63   HIS H CD2 1 
ATOM   8258  C  CE1 . HIS H  1 63  ? 145.203 21.502  17.610 1.00 29.87  ? 63   HIS H CE1 1 
ATOM   8259  N  NE2 . HIS H  1 63  ? 145.618 20.620  18.509 1.00 29.06  ? 63   HIS H NE2 1 
ATOM   8260  N  N   . PHE H  1 64  ? 147.889 16.704  13.868 1.00 23.76  ? 64   PHE H N   1 
ATOM   8261  C  CA  . PHE H  1 64  ? 148.412 16.135  12.612 1.00 26.13  ? 64   PHE H CA  1 
ATOM   8262  C  C   . PHE H  1 64  ? 148.509 17.244  11.555 1.00 26.34  ? 64   PHE H C   1 
ATOM   8263  O  O   . PHE H  1 64  ? 147.498 17.854  11.233 1.00 26.34  ? 64   PHE H O   1 
ATOM   8264  C  CB  . PHE H  1 64  ? 147.538 14.993  12.128 1.00 29.57  ? 64   PHE H CB  1 
ATOM   8265  C  CG  . PHE H  1 64  ? 147.960 14.332  10.828 1.00 28.62  ? 64   PHE H CG  1 
ATOM   8266  C  CD1 . PHE H  1 64  ? 147.011 14.020  9.868  1.00 37.94  ? 64   PHE H CD1 1 
ATOM   8267  C  CD2 . PHE H  1 64  ? 149.304 14.034  10.604 1.00 29.33  ? 64   PHE H CD2 1 
ATOM   8268  C  CE1 . PHE H  1 64  ? 147.357 13.412  8.670  1.00 34.13  ? 64   PHE H CE1 1 
ATOM   8269  C  CE2 . PHE H  1 64  ? 149.654 13.431  9.401  1.00 27.45  ? 64   PHE H CE2 1 
ATOM   8270  C  CZ  . PHE H  1 64  ? 148.691 13.129  8.453  1.00 29.37  ? 64   PHE H CZ  1 
ATOM   8271  N  N   . ASN H  1 65  ? 149.703 17.466  11.017 1.00 35.88  ? 65   ASN H N   1 
ATOM   8272  C  CA  . ASN H  1 65  ? 150.042 18.634  10.221 1.00 37.27  ? 65   ASN H CA  1 
ATOM   8273  C  C   . ASN H  1 65  ? 151.020 18.338  9.078  1.00 26.69  ? 65   ASN H C   1 
ATOM   8274  O  O   . ASN H  1 65  ? 152.093 18.962  9.120  1.00 37.25  ? 65   ASN H O   1 
ATOM   8275  C  CB  . ASN H  1 65  ? 150.708 19.682  11.122 1.00 28.05  ? 65   ASN H CB  1 
ATOM   8276  C  CG  . ASN H  1 65  ? 150.846 21.058  10.495 1.00 29.88  ? 65   ASN H CG  1 
ATOM   8277  O  OD1 . ASN H  1 65  ? 150.213 21.368  9.477  1.00 30.82  ? 65   ASN H OD1 1 
ATOM   8278  N  ND2 . ASN H  1 65  ? 151.606 21.946  11.125 1.00 31.88  ? 65   ASN H ND2 1 
ATOM   8279  N  N   . PRO H  1 66  ? 150.649 17.470  8.156  1.00 29.97  ? 66   PRO H N   1 
ATOM   8280  C  CA  . PRO H  1 66  ? 151.585 17.062  7.092  1.00 33.61  ? 66   PRO H CA  1 
ATOM   8281  C  C   . PRO H  1 66  ? 151.966 18.215  6.163  1.00 36.63  ? 66   PRO H C   1 
ATOM   8282  O  O   . PRO H  1 66  ? 152.993 18.124  5.484  1.00 43.84  ? 66   PRO H O   1 
ATOM   8283  C  CB  . PRO H  1 66  ? 150.814 15.984  6.327  1.00 37.91  ? 66   PRO H CB  1 
ATOM   8284  C  CG  . PRO H  1 66  ? 149.369 16.239  6.624  1.00 34.25  ? 66   PRO H CG  1 
ATOM   8285  C  CD  . PRO H  1 66  ? 149.358 16.794  8.021  1.00 31.48  ? 66   PRO H CD  1 
ATOM   8286  N  N   . LEU H  1 67  ? 151.216 19.299  6.093  1.00 34.30  ? 67   LEU H N   1 
ATOM   8287  C  CA  . LEU H  1 67  ? 151.487 20.378  5.138  1.00 32.71  ? 67   LEU H CA  1 
ATOM   8288  C  C   . LEU H  1 67  ? 152.101 21.547  5.884  1.00 31.11  ? 67   LEU H C   1 
ATOM   8289  O  O   . LEU H  1 67  ? 152.321 22.638  5.363  1.00 40.42  ? 67   LEU H O   1 
ATOM   8290  C  CB  . LEU H  1 67  ? 150.215 20.796  4.402  1.00 34.15  ? 67   LEU H CB  1 
ATOM   8291  C  CG  . LEU H  1 67  ? 149.580 19.755  3.474  1.00 39.48  ? 67   LEU H CG  1 
ATOM   8292  C  CD1 . LEU H  1 67  ? 148.260 20.255  2.910  1.00 46.46  ? 67   LEU H CD1 1 
ATOM   8293  C  CD2 . LEU H  1 67  ? 150.541 19.389  2.347  1.00 34.28  ? 67   LEU H CD2 1 
ATOM   8294  N  N   . SER H  1 68  ? 152.393 21.284  7.155  1.00 30.76  ? 68   SER H N   1 
ATOM   8295  C  CA  . SER H  1 68  ? 153.152 22.242  7.945  1.00 28.81  ? 68   SER H CA  1 
ATOM   8296  C  C   . SER H  1 68  ? 152.538 23.622  7.968  1.00 42.50  ? 68   SER H C   1 
ATOM   8297  O  O   . SER H  1 68  ? 153.126 24.667  7.684  1.00 42.63  ? 68   SER H O   1 
ATOM   8298  C  CB  . SER H  1 68  ? 154.575 22.313  7.367  1.00 39.32  ? 68   SER H CB  1 
ATOM   8299  O  OG  . SER H  1 68  ? 155.264 21.150  7.803  1.00 42.50  ? 68   SER H OG  1 
ATOM   8300  N  N   . ARG H  1 69  ? 151.256 23.668  8.323  1.00 36.57  ? 69   ARG H N   1 
ATOM   8301  C  CA  . ARG H  1 69  ? 150.620 24.985  8.356  1.00 33.46  ? 69   ARG H CA  1 
ATOM   8302  C  C   . ARG H  1 69  ? 150.306 25.367  9.794  1.00 37.54  ? 69   ARG H C   1 
ATOM   8303  O  O   . ARG H  1 69  ? 150.532 24.612  10.737 1.00 37.06  ? 69   ARG H O   1 
ATOM   8304  C  CB  . ARG H  1 69  ? 149.380 24.959  7.463  1.00 35.84  ? 69   ARG H CB  1 
ATOM   8305  C  CG  . ARG H  1 69  ? 149.700 24.875  5.972  1.00 44.28  ? 69   ARG H CG  1 
ATOM   8306  C  CD  . ARG H  1 69  ? 148.424 24.721  5.160  1.00 47.51  ? 69   ARG H CD  1 
ATOM   8307  N  NE  . ARG H  1 69  ? 148.688 24.401  3.765  1.00 52.77  ? 69   ARG H NE  1 
ATOM   8308  C  CZ  . ARG H  1 69  ? 147.803 24.331  2.782  1.00 61.38  ? 69   ARG H CZ  1 
ATOM   8309  N  NH1 . ARG H  1 69  ? 146.508 24.561  2.979  1.00 56.44  ? 69   ARG H NH1 1 
ATOM   8310  N  NH2 . ARG H  1 69  ? 148.205 24.020  1.550  1.00 57.63  ? 69   ARG H NH2 1 
ATOM   8311  N  N   . LYS H  1 70  ? 149.762 26.566  9.971  1.00 32.87  ? 70   LYS H N   1 
ATOM   8312  C  CA  . LYS H  1 70  ? 149.267 27.001  11.261 1.00 28.31  ? 70   LYS H CA  1 
ATOM   8313  C  C   . LYS H  1 70  ? 147.877 26.419  11.569 1.00 25.09  ? 70   LYS H C   1 
ATOM   8314  O  O   . LYS H  1 70  ? 147.095 26.033  10.707 1.00 26.39  ? 70   LYS H O   1 
ATOM   8315  C  CB  . LYS H  1 70  ? 149.176 28.527  11.284 1.00 33.23  ? 70   LYS H CB  1 
ATOM   8316  C  CG  . LYS H  1 70  ? 150.512 29.263  11.255 1.00 41.52  ? 70   LYS H CG  1 
ATOM   8317  C  CD  . LYS H  1 70  ? 151.374 28.840  12.434 1.00 58.79  ? 70   LYS H CD  1 
ATOM   8318  C  CE  . LYS H  1 70  ? 152.702 29.579  12.473 1.00 74.03  ? 70   LYS H CE  1 
ATOM   8319  N  NZ  . LYS H  1 70  ? 153.810 28.676  12.908 1.00 101.51 ? 70   LYS H NZ  1 
ATOM   8320  N  N   . HIS H  1 71  ? 147.553 26.396  12.851 1.00 26.97  ? 71   HIS H N   1 
ATOM   8321  C  CA  . HIS H  1 71  ? 146.266 25.924  13.343 1.00 25.90  ? 71   HIS H CA  1 
ATOM   8322  C  C   . HIS H  1 71  ? 145.129 26.814  12.915 1.00 25.82  ? 71   HIS H C   1 
ATOM   8323  O  O   . HIS H  1 71  ? 145.208 28.058  12.949 1.00 24.30  ? 71   HIS H O   1 
ATOM   8324  C  CB  . HIS H  1 71  ? 146.380 25.898  14.884 1.00 22.74  ? 71   HIS H CB  1 
ATOM   8325  C  CG  . HIS H  1 71  ? 145.095 25.433  15.489 1.00 21.52  ? 71   HIS H CG  1 
ATOM   8326  N  ND1 . HIS H  1 71  ? 144.763 24.098  15.534 1.00 21.69  ? 71   HIS H ND1 1 
ATOM   8327  C  CD2 . HIS H  1 71  ? 144.089 26.140  16.050 1.00 23.70  ? 71   HIS H CD2 1 
ATOM   8328  C  CE1 . HIS H  1 71  ? 143.576 23.998  16.110 1.00 23.56  ? 71   HIS H CE1 1 
ATOM   8329  N  NE2 . HIS H  1 71  ? 143.149 25.210  16.427 1.00 23.60  ? 71   HIS H NE2 1 
ATOM   8330  N  N   . GLY H  1 72  ? 144.009 26.224  12.482 1.00 23.89  ? 72   GLY H N   1 
ATOM   8331  C  CA  . GLY H  1 72  ? 142.858 27.044  12.142 1.00 24.67  ? 72   GLY H CA  1 
ATOM   8332  C  C   . GLY H  1 72  ? 141.590 26.277  12.484 1.00 28.36  ? 72   GLY H C   1 
ATOM   8333  O  O   . GLY H  1 72  ? 141.677 25.263  13.193 1.00 25.19  ? 72   GLY H O   1 
ATOM   8334  N  N   . GLY H  1 73  ? 140.468 26.742  11.976 1.00 23.74  ? 73   GLY H N   1 
ATOM   8335  C  CA  . GLY H  1 73  ? 139.200 26.029  12.156 1.00 23.07  ? 73   GLY H CA  1 
ATOM   8336  C  C   . GLY H  1 73  ? 138.985 25.137  10.945 1.00 26.63  ? 73   GLY H C   1 
ATOM   8337  O  O   . GLY H  1 73  ? 139.716 25.352  9.978  1.00 27.65  ? 73   GLY H O   1 
ATOM   8338  N  N   . PRO H  1 74  ? 138.099 24.164  10.963 1.00 27.00  ? 74   PRO H N   1 
ATOM   8339  C  CA  . PRO H  1 74  ? 137.969 23.254  9.816  1.00 24.64  ? 74   PRO H CA  1 
ATOM   8340  C  C   . PRO H  1 74  ? 137.577 23.990  8.533  1.00 31.93  ? 74   PRO H C   1 
ATOM   8341  O  O   . PRO H  1 74  ? 137.896 23.472  7.462  1.00 28.11  ? 74   PRO H O   1 
ATOM   8342  C  CB  . PRO H  1 74  ? 136.877 22.265  10.239 1.00 23.94  ? 74   PRO H CB  1 
ATOM   8343  C  CG  . PRO H  1 74  ? 136.113 23.034  11.286 1.00 23.04  ? 74   PRO H CG  1 
ATOM   8344  C  CD  . PRO H  1 74  ? 137.166 23.801  12.050 1.00 24.89  ? 74   PRO H CD  1 
ATOM   8345  N  N   . LYS H  1 75  ? 136.915 25.130  8.613  1.00 32.87  ? 75   LYS H N   1 
ATOM   8346  C  CA  . LYS H  1 75  ? 136.458 25.846  7.418  1.00 32.07  ? 75   LYS H CA  1 
ATOM   8347  C  C   . LYS H  1 75  ? 137.580 26.650  6.764  1.00 31.08  ? 75   LYS H C   1 
ATOM   8348  O  O   . LYS H  1 75  ? 137.420 27.105  5.622  1.00 35.05  ? 75   LYS H O   1 
ATOM   8349  C  CB  . LYS H  1 75  ? 135.334 26.815  7.765  1.00 34.59  ? 75   LYS H CB  1 
ATOM   8350  C  CG  . LYS H  1 75  ? 133.955 26.268  8.078  1.00 35.26  ? 75   LYS H CG  1 
ATOM   8351  C  CD  . LYS H  1 75  ? 133.140 27.314  8.854  1.00 39.29  ? 75   LYS H CD  1 
ATOM   8352  C  CE  . LYS H  1 75  ? 131.910 27.758  8.082  1.00 46.19  ? 75   LYS H CE  1 
ATOM   8353  N  NZ  . LYS H  1 75  ? 130.938 28.530  8.919  1.00 49.13  ? 75   LYS H NZ  1 
ATOM   8354  N  N   . ASP H  1 76  ? 138.701 26.882  7.437  1.00 29.42  ? 76   ASP H N   1 
ATOM   8355  C  CA  . ASP H  1 76  ? 139.818 27.634  6.875  1.00 31.24  ? 76   ASP H CA  1 
ATOM   8356  C  C   . ASP H  1 76  ? 140.721 26.859  5.926  1.00 32.68  ? 76   ASP H C   1 
ATOM   8357  O  O   . ASP H  1 76  ? 140.920 25.656  6.100  1.00 33.20  ? 76   ASP H O   1 
ATOM   8358  C  CB  . ASP H  1 76  ? 140.754 28.140  7.985  1.00 31.16  ? 76   ASP H CB  1 
ATOM   8359  C  CG  . ASP H  1 76  ? 139.981 28.987  8.980  1.00 46.76  ? 76   ASP H CG  1 
ATOM   8360  O  OD1 . ASP H  1 76  ? 140.353 28.964  10.170 1.00 43.97  ? 76   ASP H OD1 1 
ATOM   8361  O  OD2 . ASP H  1 76  ? 139.018 29.663  8.557  1.00 32.05  ? 76   ASP H OD2 1 
ATOM   8362  N  N   . GLU H  1 77  ? 141.304 27.553  4.945  1.00 37.32  ? 77   GLU H N   1 
ATOM   8363  C  CA  . GLU H  1 77  ? 142.344 26.972  4.115  1.00 40.35  ? 77   GLU H CA  1 
ATOM   8364  C  C   . GLU H  1 77  ? 143.647 26.809  4.892  1.00 37.74  ? 77   GLU H C   1 
ATOM   8365  O  O   . GLU H  1 77  ? 144.399 25.851  4.728  1.00 39.23  ? 77   GLU H O   1 
ATOM   8366  C  CB  . GLU H  1 77  ? 142.685 27.812  2.869  1.00 43.67  ? 77   GLU H CB  1 
ATOM   8367  C  CG  . GLU H  1 77  ? 143.627 27.022  1.962  1.00 48.88  ? 77   GLU H CG  1 
ATOM   8368  C  CD  . GLU H  1 77  ? 145.072 27.453  1.992  1.00 61.22  ? 77   GLU H CD  1 
ATOM   8369  O  OE1 . GLU H  1 77  ? 145.455 28.300  2.827  1.00 71.45  ? 77   GLU H OE1 1 
ATOM   8370  O  OE2 . GLU H  1 77  ? 145.860 26.940  1.162  1.00 83.47  ? 77   GLU H OE2 1 
ATOM   8371  N  N   . GLU H  1 78  ? 143.929 27.792  5.751  1.00 27.74  ? 78   GLU H N   1 
ATOM   8372  C  CA  . GLU H  1 78  ? 145.088 27.657  6.613  1.00 30.30  ? 78   GLU H CA  1 
ATOM   8373  C  C   . GLU H  1 78  ? 144.663 26.922  7.892  1.00 33.17  ? 78   GLU H C   1 
ATOM   8374  O  O   . GLU H  1 78  ? 144.094 27.529  8.802  1.00 28.34  ? 78   GLU H O   1 
ATOM   8375  C  CB  . GLU H  1 78  ? 145.694 29.009  6.968  1.00 30.26  ? 78   GLU H CB  1 
ATOM   8376  C  CG  . GLU H  1 78  ? 146.986 28.882  7.760  1.00 34.72  ? 78   GLU H CG  1 
ATOM   8377  C  CD  . GLU H  1 78  ? 148.199 28.559  6.909  1.00 48.21  ? 78   GLU H CD  1 
ATOM   8378  O  OE1 . GLU H  1 78  ? 149.306 28.438  7.492  1.00 44.42  ? 78   GLU H OE1 1 
ATOM   8379  O  OE2 . GLU H  1 78  ? 148.049 28.428  5.669  1.00 48.54  ? 78   GLU H OE2 1 
ATOM   8380  N  N   . ARG H  1 79  ? 144.944 25.629  7.912  1.00 28.44  ? 79   ARG H N   1 
ATOM   8381  C  CA  . ARG H  1 79  ? 144.617 24.791  9.059  1.00 29.24  ? 79   ARG H CA  1 
ATOM   8382  C  C   . ARG H  1 79  ? 145.530 23.572  9.064  1.00 30.00  ? 79   ARG H C   1 
ATOM   8383  O  O   . ARG H  1 79  ? 146.125 23.288  8.026  1.00 26.79  ? 79   ARG H O   1 
ATOM   8384  C  CB  . ARG H  1 79  ? 143.159 24.335  9.021  1.00 24.79  ? 79   ARG H CB  1 
ATOM   8385  C  CG  . ARG H  1 79  ? 142.891 23.412  7.821  1.00 28.59  ? 79   ARG H CG  1 
ATOM   8386  C  CD  . ARG H  1 79  ? 141.461 22.880  7.951  1.00 29.90  ? 79   ARG H CD  1 
ATOM   8387  N  NE  . ARG H  1 79  ? 141.523 21.472  8.344  1.00 28.80  ? 79   ARG H NE  1 
ATOM   8388  C  CZ  . ARG H  1 79  ? 140.522 20.611  8.264  1.00 23.61  ? 79   ARG H CZ  1 
ATOM   8389  N  NH1 . ARG H  1 79  ? 140.804 19.369  8.672  1.00 25.57  ? 79   ARG H NH1 1 
ATOM   8390  N  NH2 . ARG H  1 79  ? 139.326 20.927  7.818  1.00 26.75  ? 79   ARG H NH2 1 
ATOM   8391  N  N   . HIS H  1 80  ? 145.623 22.891  10.203 1.00 25.13  ? 80   HIS H N   1 
ATOM   8392  C  CA  . HIS H  1 80  ? 146.293 21.590  10.238 1.00 22.85  ? 80   HIS H CA  1 
ATOM   8393  C  C   . HIS H  1 80  ? 145.357 20.552  9.646  1.00 26.06  ? 80   HIS H C   1 
ATOM   8394  O  O   . HIS H  1 80  ? 144.142 20.734  9.824  1.00 28.37  ? 80   HIS H O   1 
ATOM   8395  C  CB  . HIS H  1 80  ? 146.631 21.221  11.681 1.00 26.12  ? 80   HIS H CB  1 
ATOM   8396  C  CG  . HIS H  1 80  ? 147.515 22.128  12.461 1.00 27.72  ? 80   HIS H CG  1 
ATOM   8397  N  ND1 . HIS H  1 80  ? 147.308 22.418  13.802 1.00 25.37  ? 80   HIS H ND1 1 
ATOM   8398  C  CD2 . HIS H  1 80  ? 148.619 22.833  12.122 1.00 24.40  ? 80   HIS H CD2 1 
ATOM   8399  C  CE1 . HIS H  1 80  ? 148.243 23.237  14.235 1.00 27.01  ? 80   HIS H CE1 1 
ATOM   8400  N  NE2 . HIS H  1 80  ? 149.073 23.510  13.225 1.00 29.58  ? 80   HIS H NE2 1 
ATOM   8401  N  N   . VAL H  1 81  ? 145.832 19.491  8.991  1.00 24.41  ? 81   VAL H N   1 
ATOM   8402  C  CA  . VAL H  1 81  ? 144.910 18.477  8.470  1.00 23.09  ? 81   VAL H CA  1 
ATOM   8403  C  C   . VAL H  1 81  ? 144.021 17.961  9.604  1.00 25.63  ? 81   VAL H C   1 
ATOM   8404  O  O   . VAL H  1 81  ? 142.819 17.723  9.468  1.00 24.79  ? 81   VAL H O   1 
ATOM   8405  C  CB  . VAL H  1 81  ? 145.643 17.313  7.780  1.00 27.33  ? 81   VAL H CB  1 
ATOM   8406  C  CG1 . VAL H  1 81  ? 144.736 16.091  7.631  1.00 29.50  ? 81   VAL H CG1 1 
ATOM   8407  C  CG2 . VAL H  1 81  ? 146.143 17.702  6.388  1.00 22.89  ? 81   VAL H CG2 1 
ATOM   8408  N  N   . GLY H  1 82  ? 144.595 17.819  10.805 1.00 27.97  ? 82   GLY H N   1 
ATOM   8409  C  CA  . GLY H  1 82  ? 143.729 17.265  11.852 1.00 26.42  ? 82   GLY H CA  1 
ATOM   8410  C  C   . GLY H  1 82  ? 142.802 18.266  12.500 1.00 35.36  ? 82   GLY H C   1 
ATOM   8411  O  O   . GLY H  1 82  ? 142.169 17.927  13.505 1.00 24.59  ? 82   GLY H O   1 
ATOM   8412  N  N   . ASP H  1 83  ? 142.658 19.504  12.019 1.00 25.31  ? 83   ASP H N   1 
ATOM   8413  C  CA  . ASP H  1 83  ? 141.804 20.448  12.751 1.00 23.74  ? 83   ASP H CA  1 
ATOM   8414  C  C   . ASP H  1 83  ? 140.318 20.267  12.503 1.00 29.79  ? 83   ASP H C   1 
ATOM   8415  O  O   . ASP H  1 83  ? 139.780 20.661  11.466 1.00 27.52  ? 83   ASP H O   1 
ATOM   8416  C  CB  . ASP H  1 83  ? 142.220 21.887  12.380 1.00 20.00  ? 83   ASP H CB  1 
ATOM   8417  C  CG  . ASP H  1 83  ? 143.565 22.279  12.954 1.00 24.26  ? 83   ASP H CG  1 
ATOM   8418  O  OD1 . ASP H  1 83  ? 144.034 21.594  13.898 1.00 22.42  ? 83   ASP H OD1 1 
ATOM   8419  O  OD2 . ASP H  1 83  ? 144.188 23.252  12.481 1.00 23.03  ? 83   ASP H OD2 1 
ATOM   8420  N  N   . LEU H  1 84  ? 139.586 19.676  13.449 1.00 23.09  ? 84   LEU H N   1 
ATOM   8421  C  CA  . LEU H  1 84  ? 138.178 19.381  13.209 1.00 25.32  ? 84   LEU H CA  1 
ATOM   8422  C  C   . LEU H  1 84  ? 137.294 20.348  13.969 1.00 19.68  ? 84   LEU H C   1 
ATOM   8423  O  O   . LEU H  1 84  ? 136.067 20.188  14.003 1.00 28.49  ? 84   LEU H O   1 
ATOM   8424  C  CB  . LEU H  1 84  ? 137.878 17.925  13.617 1.00 27.67  ? 84   LEU H CB  1 
ATOM   8425  C  CG  . LEU H  1 84  ? 138.557 16.849  12.756 1.00 27.08  ? 84   LEU H CG  1 
ATOM   8426  C  CD1 . LEU H  1 84  ? 138.096 15.453  13.175 1.00 24.79  ? 84   LEU H CD1 1 
ATOM   8427  C  CD2 . LEU H  1 84  ? 138.259 17.068  11.284 1.00 30.11  ? 84   LEU H CD2 1 
ATOM   8428  N  N   . GLY H  1 85  ? 137.933 21.361  14.562 1.00 20.72  ? 85   GLY H N   1 
ATOM   8429  C  CA  . GLY H  1 85  ? 137.133 22.381  15.238 1.00 24.19  ? 85   GLY H CA  1 
ATOM   8430  C  C   . GLY H  1 85  ? 136.711 21.959  16.635 1.00 25.29  ? 85   GLY H C   1 
ATOM   8431  O  O   . GLY H  1 85  ? 137.500 21.403  17.405 1.00 25.34  ? 85   GLY H O   1 
ATOM   8432  N  N   . ASN H  1 86  ? 135.464 22.270  16.966 1.00 24.36  ? 86   ASN H N   1 
ATOM   8433  C  CA  . ASN H  1 86  ? 134.860 21.960  18.252 1.00 18.48  ? 86   ASN H CA  1 
ATOM   8434  C  C   . ASN H  1 86  ? 133.721 20.947  18.115 1.00 22.49  ? 86   ASN H C   1 
ATOM   8435  O  O   . ASN H  1 86  ? 133.072 20.882  17.071 1.00 23.86  ? 86   ASN H O   1 
ATOM   8436  C  CB  . ASN H  1 86  ? 134.246 23.224  18.867 1.00 22.77  ? 86   ASN H CB  1 
ATOM   8437  C  CG  . ASN H  1 86  ? 135.329 24.188  19.328 1.00 26.08  ? 86   ASN H CG  1 
ATOM   8438  O  OD1 . ASN H  1 86  ? 136.055 23.818  20.247 1.00 25.12  ? 86   ASN H OD1 1 
ATOM   8439  N  ND2 . ASN H  1 86  ? 135.412 25.371  18.729 1.00 21.71  ? 86   ASN H ND2 1 
ATOM   8440  N  N   . VAL H  1 87  ? 133.474 20.227  19.200 1.00 21.37  ? 87   VAL H N   1 
ATOM   8441  C  CA  . VAL H  1 87  ? 132.210 19.525  19.433 1.00 20.10  ? 87   VAL H CA  1 
ATOM   8442  C  C   . VAL H  1 87  ? 131.534 20.163  20.644 1.00 22.47  ? 87   VAL H C   1 
ATOM   8443  O  O   . VAL H  1 87  ? 132.148 20.821  21.492 1.00 24.30  ? 87   VAL H O   1 
ATOM   8444  C  CB  . VAL H  1 87  ? 132.415 18.017  19.619 1.00 22.34  ? 87   VAL H CB  1 
ATOM   8445  C  CG1 . VAL H  1 87  ? 133.060 17.423  18.353 1.00 22.35  ? 87   VAL H CG1 1 
ATOM   8446  C  CG2 . VAL H  1 87  ? 133.286 17.676  20.821 1.00 19.78  ? 87   VAL H CG2 1 
ATOM   8447  N  N   . THR H  1 88  ? 130.219 20.000  20.741 1.00 22.53  ? 88   THR H N   1 
ATOM   8448  C  CA  . THR H  1 88  ? 129.394 20.663  21.744 1.00 21.40  ? 88   THR H CA  1 
ATOM   8449  C  C   . THR H  1 88  ? 128.681 19.624  22.600 1.00 23.82  ? 88   THR H C   1 
ATOM   8450  O  O   . THR H  1 88  ? 127.967 18.779  22.035 1.00 26.01  ? 88   THR H O   1 
ATOM   8451  C  CB  . THR H  1 88  ? 128.367 21.560  21.048 1.00 24.36  ? 88   THR H CB  1 
ATOM   8452  O  OG1 . THR H  1 88  ? 129.064 22.605  20.339 1.00 24.68  ? 88   THR H OG1 1 
ATOM   8453  C  CG2 . THR H  1 88  ? 127.430 22.226  22.057 1.00 27.67  ? 88   THR H CG2 1 
ATOM   8454  N  N   . ALA H  1 89  ? 128.904 19.691  23.906 1.00 20.17  ? 89   ALA H N   1 
ATOM   8455  C  CA  . ALA H  1 89  ? 128.209 18.833  24.860 1.00 19.30  ? 89   ALA H CA  1 
ATOM   8456  C  C   . ALA H  1 89  ? 126.970 19.538  25.393 1.00 22.42  ? 89   ALA H C   1 
ATOM   8457  O  O   . ALA H  1 89  ? 126.994 20.750  25.639 1.00 26.57  ? 89   ALA H O   1 
ATOM   8458  C  CB  . ALA H  1 89  ? 129.170 18.418  25.963 1.00 22.96  ? 89   ALA H CB  1 
ATOM   8459  N  N   . ASP H  1 90  ? 125.875 18.797  25.555 1.00 22.12  ? 90   ASP H N   1 
ATOM   8460  C  CA  . ASP H  1 90  ? 124.612 19.382  26.027 1.00 25.74  ? 90   ASP H CA  1 
ATOM   8461  C  C   . ASP H  1 90  ? 124.623 19.485  27.553 1.00 26.75  ? 90   ASP H C   1 
ATOM   8462  O  O   . ASP H  1 90  ? 125.663 19.234  28.165 1.00 24.82  ? 90   ASP H O   1 
ATOM   8463  C  CB  . ASP H  1 90  ? 123.403 18.583  25.537 1.00 25.12  ? 90   ASP H CB  1 
ATOM   8464  C  CG  . ASP H  1 90  ? 123.360 17.148  26.016 1.00 26.32  ? 90   ASP H CG  1 
ATOM   8465  O  OD1 . ASP H  1 90  ? 122.703 16.291  25.370 1.00 27.25  ? 90   ASP H OD1 1 
ATOM   8466  O  OD2 . ASP H  1 90  ? 124.004 16.807  27.035 1.00 27.76  ? 90   ASP H OD2 1 
ATOM   8467  N  N   . LYS H  1 91  ? 123.487 19.852  28.156 1.00 27.23  ? 91   LYS H N   1 
ATOM   8468  C  CA  . LYS H  1 91  ? 123.518 20.022  29.609 1.00 28.88  ? 91   LYS H CA  1 
ATOM   8469  C  C   . LYS H  1 91  ? 123.674 18.707  30.357 1.00 31.11  ? 91   LYS H C   1 
ATOM   8470  O  O   . LYS H  1 91  ? 123.934 18.744  31.571 1.00 35.03  ? 91   LYS H O   1 
ATOM   8471  C  CB  . LYS H  1 91  ? 122.252 20.739  30.082 1.00 36.54  ? 91   LYS H CB  1 
ATOM   8472  C  CG  . LYS H  1 91  ? 120.946 20.056  29.701 1.00 52.31  ? 91   LYS H CG  1 
ATOM   8473  C  CD  . LYS H  1 91  ? 119.759 20.919  30.119 1.00 66.29  ? 91   LYS H CD  1 
ATOM   8474  C  CE  . LYS H  1 91  ? 118.445 20.159  30.120 1.00 77.33  ? 91   LYS H CE  1 
ATOM   8475  N  NZ  . LYS H  1 91  ? 117.348 20.899  30.816 1.00 81.48  ? 91   LYS H NZ  1 
ATOM   8476  N  N   . ASP H  1 92  ? 123.532 17.572  29.699 1.00 27.27  ? 92   ASP H N   1 
ATOM   8477  C  CA  . ASP H  1 92  ? 123.755 16.278  30.327 1.00 29.63  ? 92   ASP H CA  1 
ATOM   8478  C  C   . ASP H  1 92  ? 125.184 15.793  30.093 1.00 29.17  ? 92   ASP H C   1 
ATOM   8479  O  O   . ASP H  1 92  ? 125.484 14.669  30.494 1.00 27.29  ? 92   ASP H O   1 
ATOM   8480  C  CB  . ASP H  1 92  ? 122.782 15.209  29.810 1.00 30.73  ? 92   ASP H CB  1 
ATOM   8481  C  CG  . ASP H  1 92  ? 121.345 15.530  30.175 1.00 43.76  ? 92   ASP H CG  1 
ATOM   8482  O  OD1 . ASP H  1 92  ? 120.448 15.200  29.373 1.00 51.11  ? 92   ASP H OD1 1 
ATOM   8483  O  OD2 . ASP H  1 92  ? 121.107 16.117  31.257 1.00 36.58  ? 92   ASP H OD2 1 
ATOM   8484  N  N   . GLY H  1 93  ? 126.019 16.604  29.444 1.00 26.25  ? 93   GLY H N   1 
ATOM   8485  C  CA  . GLY H  1 93  ? 127.419 16.205  29.259 1.00 24.50  ? 93   GLY H CA  1 
ATOM   8486  C  C   . GLY H  1 93  ? 127.646 15.328  28.047 1.00 25.79  ? 93   GLY H C   1 
ATOM   8487  O  O   . GLY H  1 93  ? 128.744 14.759  27.890 1.00 25.94  ? 93   GLY H O   1 
ATOM   8488  N  N   . VAL H  1 94  ? 126.614 15.240  27.209 1.00 21.64  ? 94   VAL H N   1 
ATOM   8489  C  CA  . VAL H  1 94  ? 126.701 14.423  26.003 1.00 25.21  ? 94   VAL H CA  1 
ATOM   8490  C  C   . VAL H  1 94  ? 126.943 15.244  24.734 1.00 24.36  ? 94   VAL H C   1 
ATOM   8491  O  O   . VAL H  1 94  ? 126.236 16.210  24.430 1.00 25.25  ? 94   VAL H O   1 
ATOM   8492  C  CB  . VAL H  1 94  ? 125.427 13.588  25.797 1.00 28.27  ? 94   VAL H CB  1 
ATOM   8493  C  CG1 . VAL H  1 94  ? 125.544 12.751  24.532 1.00 24.57  ? 94   VAL H CG1 1 
ATOM   8494  C  CG2 . VAL H  1 94  ? 125.204 12.652  26.990 1.00 28.34  ? 94   VAL H CG2 1 
ATOM   8495  N  N   . ALA H  1 95  ? 127.935 14.849  23.957 1.00 23.39  ? 95   ALA H N   1 
ATOM   8496  C  CA  . ALA H  1 95  ? 128.174 15.444  22.646 1.00 27.88  ? 95   ALA H CA  1 
ATOM   8497  C  C   . ALA H  1 95  ? 127.762 14.436  21.562 1.00 23.51  ? 95   ALA H C   1 
ATOM   8498  O  O   . ALA H  1 95  ? 128.403 13.403  21.442 1.00 24.01  ? 95   ALA H O   1 
ATOM   8499  C  CB  . ALA H  1 95  ? 129.624 15.867  22.444 1.00 25.18  ? 95   ALA H CB  1 
ATOM   8500  N  N   . ASP H  1 96  ? 126.714 14.779  20.833 1.00 20.81  ? 96   ASP H N   1 
ATOM   8501  C  CA  . ASP H  1 96  ? 126.266 13.969  19.717 1.00 23.70  ? 96   ASP H CA  1 
ATOM   8502  C  C   . ASP H  1 96  ? 126.955 14.560  18.484 1.00 25.47  ? 96   ASP H C   1 
ATOM   8503  O  O   . ASP H  1 96  ? 126.389 15.466  17.868 1.00 25.52  ? 96   ASP H O   1 
ATOM   8504  C  CB  . ASP H  1 96  ? 124.751 13.986  19.577 1.00 26.90  ? 96   ASP H CB  1 
ATOM   8505  C  CG  . ASP H  1 96  ? 124.137 13.222  20.756 1.00 38.16  ? 96   ASP H CG  1 
ATOM   8506  O  OD1 . ASP H  1 96  ? 123.324 13.796  21.510 1.00 36.56  ? 96   ASP H OD1 1 
ATOM   8507  O  OD2 . ASP H  1 96  ? 124.519 12.042  20.904 1.00 29.56  ? 96   ASP H OD2 1 
ATOM   8508  N  N   . VAL H  1 97  ? 128.134 14.024  18.250 1.00 21.82  ? 97   VAL H N   1 
ATOM   8509  C  CA  . VAL H  1 97  ? 129.063 14.580  17.271 1.00 20.90  ? 97   VAL H CA  1 
ATOM   8510  C  C   . VAL H  1 97  ? 128.521 14.359  15.872 1.00 22.19  ? 97   VAL H C   1 
ATOM   8511  O  O   . VAL H  1 97  ? 128.089 13.275  15.477 1.00 25.33  ? 97   VAL H O   1 
ATOM   8512  C  CB  . VAL H  1 97  ? 130.446 13.920  17.407 1.00 22.96  ? 97   VAL H CB  1 
ATOM   8513  C  CG1 . VAL H  1 97  ? 131.421 14.392  16.336 1.00 26.02  ? 97   VAL H CG1 1 
ATOM   8514  C  CG2 . VAL H  1 97  ? 131.010 14.185  18.814 1.00 22.09  ? 97   VAL H CG2 1 
ATOM   8515  N  N   . SER H  1 98  ? 128.580 15.431  15.070 1.00 20.92  ? 98   SER H N   1 
ATOM   8516  C  CA  . SER H  1 98  ? 128.184 15.211  13.675 1.00 23.37  ? 98   SER H CA  1 
ATOM   8517  C  C   . SER H  1 98  ? 128.955 16.247  12.868 1.00 25.85  ? 98   SER H C   1 
ATOM   8518  O  O   . SER H  1 98  ? 128.626 17.434  12.945 1.00 25.99  ? 98   SER H O   1 
ATOM   8519  C  CB  . SER H  1 98  ? 126.680 15.304  13.511 1.00 33.91  ? 98   SER H CB  1 
ATOM   8520  O  OG  . SER H  1 98  ? 126.308 15.451  12.157 1.00 37.91  ? 98   SER H OG  1 
ATOM   8521  N  N   . ILE H  1 99  ? 129.961 15.742  12.174 1.00 23.14  ? 99   ILE H N   1 
ATOM   8522  C  CA  . ILE H  1 99  ? 130.883 16.601  11.415 1.00 26.23  ? 99   ILE H CA  1 
ATOM   8523  C  C   . ILE H  1 99  ? 131.030 16.020  10.014 1.00 33.08  ? 99   ILE H C   1 
ATOM   8524  O  O   . ILE H  1 99  ? 130.896 14.811  9.834  1.00 28.34  ? 99   ILE H O   1 
ATOM   8525  C  CB  . ILE H  1 99  ? 132.213 16.720  12.177 1.00 26.64  ? 99   ILE H CB  1 
ATOM   8526  C  CG1 . ILE H  1 99  ? 132.117 17.707  13.363 1.00 27.15  ? 99   ILE H CG1 1 
ATOM   8527  C  CG2 . ILE H  1 99  ? 133.421 17.089  11.348 1.00 27.31  ? 99   ILE H CG2 1 
ATOM   8528  C  CD1 . ILE H  1 99  ? 133.329 17.593  14.278 1.00 33.46  ? 99   ILE H CD1 1 
ATOM   8529  N  N   . GLU H  1 100 ? 131.258 16.856  9.007  1.00 27.74  ? 100  GLU H N   1 
ATOM   8530  C  CA  . GLU H  1 100 ? 131.664 16.384  7.681  1.00 25.61  ? 100  GLU H CA  1 
ATOM   8531  C  C   . GLU H  1 100 ? 132.918 17.159  7.320  1.00 26.21  ? 100  GLU H C   1 
ATOM   8532  O  O   . GLU H  1 100 ? 132.923 18.403  7.423  1.00 29.04  ? 100  GLU H O   1 
ATOM   8533  C  CB  . GLU H  1 100 ? 130.583 16.560  6.647  1.00 30.01  ? 100  GLU H CB  1 
ATOM   8534  C  CG  . GLU H  1 100 ? 130.845 15.889  5.302  1.00 46.56  ? 100  GLU H CG  1 
ATOM   8535  C  CD  . GLU H  1 100 ? 129.682 16.153  4.350  1.00 60.79  ? 100  GLU H CD  1 
ATOM   8536  O  OE1 . GLU H  1 100 ? 128.558 15.709  4.670  1.00 77.66  ? 100  GLU H OE1 1 
ATOM   8537  O  OE2 . GLU H  1 100 ? 129.890 16.813  3.310  1.00 62.67  ? 100  GLU H OE2 1 
ATOM   8538  N  N   . ASP H  1 101 ? 133.999 16.471  6.955  1.00 23.55  ? 101  ASP H N   1 
ATOM   8539  C  CA  . ASP H  1 101 ? 135.233 17.225  6.754  1.00 21.99  ? 101  ASP H CA  1 
ATOM   8540  C  C   . ASP H  1 101 ? 135.898 16.746  5.463  1.00 37.18  ? 101  ASP H C   1 
ATOM   8541  O  O   . ASP H  1 101 ? 135.962 15.535  5.258  1.00 35.98  ? 101  ASP H O   1 
ATOM   8542  C  CB  . ASP H  1 101 ? 136.214 17.073  7.917  1.00 28.41  ? 101  ASP H CB  1 
ATOM   8543  C  CG  . ASP H  1 101 ? 137.393 18.026  7.789  1.00 31.78  ? 101  ASP H CG  1 
ATOM   8544  O  OD1 . ASP H  1 101 ? 138.470 17.558  7.350  1.00 29.90  ? 101  ASP H OD1 1 
ATOM   8545  O  OD2 . ASP H  1 101 ? 137.232 19.226  8.096  1.00 32.84  ? 101  ASP H OD2 1 
ATOM   8546  N  N   . SER H  1 102 ? 136.360 17.683  4.632  1.00 33.43  ? 102  SER H N   1 
ATOM   8547  C  CA  . SER H  1 102 ? 136.868 17.302  3.321  1.00 29.03  ? 102  SER H CA  1 
ATOM   8548  C  C   . SER H  1 102 ? 138.377 17.338  3.252  1.00 29.15  ? 102  SER H C   1 
ATOM   8549  O  O   . SER H  1 102 ? 138.942 17.115  2.179  1.00 33.88  ? 102  SER H O   1 
ATOM   8550  C  CB  . SER H  1 102 ? 136.298 18.237  2.242  1.00 37.63  ? 102  SER H CB  1 
ATOM   8551  O  OG  . SER H  1 102 ? 136.744 19.557  2.520  1.00 60.03  ? 102  SER H OG  1 
ATOM   8552  N  N   . VAL H  1 103 ? 139.033 17.599  4.375  1.00 26.39  ? 103  VAL H N   1 
ATOM   8553  C  CA  . VAL H  1 103 ? 140.488 17.669  4.365  1.00 24.64  ? 103  VAL H CA  1 
ATOM   8554  C  C   . VAL H  1 103 ? 141.110 16.416  4.949  1.00 36.04  ? 103  VAL H C   1 
ATOM   8555  O  O   . VAL H  1 103 ? 142.147 15.931  4.490  1.00 34.63  ? 103  VAL H O   1 
ATOM   8556  C  CB  . VAL H  1 103 ? 140.951 18.910  5.141  1.00 27.80  ? 103  VAL H CB  1 
ATOM   8557  C  CG1 . VAL H  1 103 ? 142.456 18.884  5.397  1.00 26.85  ? 103  VAL H CG1 1 
ATOM   8558  C  CG2 . VAL H  1 103 ? 140.502 20.146  4.357  1.00 28.06  ? 103  VAL H CG2 1 
ATOM   8559  N  N   . ILE H  1 104 ? 140.485 15.868  5.993  1.00 27.58  ? 104  ILE H N   1 
ATOM   8560  C  CA  . ILE H  1 104 ? 141.021 14.581  6.468  1.00 26.38  ? 104  ILE H CA  1 
ATOM   8561  C  C   . ILE H  1 104 ? 140.685 13.517  5.435  1.00 29.02  ? 104  ILE H C   1 
ATOM   8562  O  O   . ILE H  1 104 ? 139.768 13.676  4.621  1.00 28.88  ? 104  ILE H O   1 
ATOM   8563  C  CB  . ILE H  1 104 ? 140.434 14.174  7.826  1.00 26.51  ? 104  ILE H CB  1 
ATOM   8564  C  CG1 . ILE H  1 104 ? 138.900 14.135  7.900  1.00 27.73  ? 104  ILE H CG1 1 
ATOM   8565  C  CG2 . ILE H  1 104 ? 140.993 15.072  8.925  1.00 25.62  ? 104  ILE H CG2 1 
ATOM   8566  C  CD1 . ILE H  1 104 ? 138.350 13.483  9.168  1.00 24.10  ? 104  ILE H CD1 1 
ATOM   8567  N  N   . SER H  1 105 ? 141.404 12.404  5.519  1.00 33.24  ? 105  SER H N   1 
ATOM   8568  C  CA  . SER H  1 105 ? 141.140 11.247  4.690  1.00 32.76  ? 105  SER H CA  1 
ATOM   8569  C  C   . SER H  1 105 ? 141.436 9.929   5.421  1.00 34.06  ? 105  SER H C   1 
ATOM   8570  O  O   . SER H  1 105 ? 142.279 9.941   6.325  1.00 36.39  ? 105  SER H O   1 
ATOM   8571  C  CB  . SER H  1 105 ? 142.029 11.243  3.433  1.00 37.82  ? 105  SER H CB  1 
ATOM   8572  O  OG  . SER H  1 105 ? 141.461 10.304  2.518  1.00 45.77  ? 105  SER H OG  1 
ATOM   8573  N  N   . LEU H  1 106 ? 140.763 8.888   4.970  1.00 32.70  ? 106  LEU H N   1 
ATOM   8574  C  CA  . LEU H  1 106 ? 140.969 7.522   5.436  1.00 35.68  ? 106  LEU H CA  1 
ATOM   8575  C  C   . LEU H  1 106 ? 141.933 6.743   4.536  1.00 43.55  ? 106  LEU H C   1 
ATOM   8576  O  O   . LEU H  1 106 ? 141.978 5.510   4.660  1.00 46.11  ? 106  LEU H O   1 
ATOM   8577  C  CB  . LEU H  1 106 ? 139.637 6.765   5.544  1.00 38.29  ? 106  LEU H CB  1 
ATOM   8578  C  CG  . LEU H  1 106 ? 138.566 7.401   6.436  1.00 32.92  ? 106  LEU H CG  1 
ATOM   8579  C  CD1 . LEU H  1 106 ? 137.383 6.489   6.647  1.00 35.37  ? 106  LEU H CD1 1 
ATOM   8580  C  CD2 . LEU H  1 106 ? 139.165 7.820   7.782  1.00 38.58  ? 106  LEU H CD2 1 
ATOM   8581  N  N   . SER H  1 107 ? 142.690 7.388   3.664  1.00 45.87  ? 107  SER H N   1 
ATOM   8582  C  CA  . SER H  1 107 ? 143.756 6.764   2.875  1.00 44.74  ? 107  SER H CA  1 
ATOM   8583  C  C   . SER H  1 107 ? 144.676 7.833   2.295  1.00 48.61  ? 107  SER H C   1 
ATOM   8584  O  O   . SER H  1 107 ? 144.344 9.021   2.340  1.00 46.73  ? 107  SER H O   1 
ATOM   8585  C  CB  . SER H  1 107 ? 143.205 5.894   1.750  1.00 42.29  ? 107  SER H CB  1 
ATOM   8586  O  OG  . SER H  1 107 ? 142.956 6.677   0.593  1.00 61.21  ? 107  SER H OG  1 
ATOM   8587  N  N   . GLY H  1 108 ? 145.830 7.440   1.762  1.00 50.94  ? 108  GLY H N   1 
ATOM   8588  C  CA  . GLY H  1 108 ? 146.820 8.403   1.304  1.00 57.80  ? 108  GLY H CA  1 
ATOM   8589  C  C   . GLY H  1 108 ? 147.694 8.944   2.428  1.00 69.02  ? 108  GLY H C   1 
ATOM   8590  O  O   . GLY H  1 108 ? 147.713 8.391   3.532  1.00 55.31  ? 108  GLY H O   1 
ATOM   8591  N  N   . ASP H  1 109 ? 148.430 10.021  2.172  1.00 74.34  ? 109  ASP H N   1 
ATOM   8592  C  CA  . ASP H  1 109 ? 149.302 10.700  3.117  1.00 82.17  ? 109  ASP H CA  1 
ATOM   8593  C  C   . ASP H  1 109 ? 148.544 11.613  4.075  1.00 73.05  ? 109  ASP H C   1 
ATOM   8594  O  O   . ASP H  1 109 ? 149.039 11.844  5.186  1.00 72.39  ? 109  ASP H O   1 
ATOM   8595  C  CB  . ASP H  1 109 ? 150.370 11.532  2.395  1.00 96.02  ? 109  ASP H CB  1 
ATOM   8596  C  CG  . ASP H  1 109 ? 151.266 10.724  1.483  1.00 100.88 ? 109  ASP H CG  1 
ATOM   8597  O  OD1 . ASP H  1 109 ? 151.537 9.542   1.802  1.00 109.58 ? 109  ASP H OD1 1 
ATOM   8598  O  OD2 . ASP H  1 109 ? 151.713 11.272  0.447  1.00 82.47  ? 109  ASP H OD2 1 
ATOM   8599  N  N   . HIS H  1 110 ? 147.367 12.123  3.723  1.00 68.32  ? 110  HIS H N   1 
ATOM   8600  C  CA  . HIS H  1 110 ? 146.549 12.907  4.651  1.00 62.65  ? 110  HIS H CA  1 
ATOM   8601  C  C   . HIS H  1 110 ? 145.672 11.958  5.483  1.00 55.94  ? 110  HIS H C   1 
ATOM   8602  O  O   . HIS H  1 110 ? 144.620 12.342  6.006  1.00 42.84  ? 110  HIS H O   1 
ATOM   8603  C  CB  . HIS H  1 110 ? 145.602 13.905  3.995  1.00 53.51  ? 110  HIS H CB  1 
ATOM   8604  C  CG  . HIS H  1 110 ? 146.192 15.108  3.343  1.00 62.13  ? 110  HIS H CG  1 
ATOM   8605  N  ND1 . HIS H  1 110 ? 145.391 16.083  2.766  1.00 66.42  ? 110  HIS H ND1 1 
ATOM   8606  C  CD2 . HIS H  1 110 ? 147.474 15.504  3.144  1.00 55.60  ? 110  HIS H CD2 1 
ATOM   8607  C  CE1 . HIS H  1 110 ? 146.159 17.031  2.261  1.00 61.65  ? 110  HIS H CE1 1 
ATOM   8608  N  NE2 . HIS H  1 110 ? 147.426 16.711  2.482  1.00 56.47  ? 110  HIS H NE2 1 
ATOM   8609  N  N   . CYS H  1 111 ? 146.121 10.718  5.575  1.00 46.17  ? 111  CYS H N   1 
ATOM   8610  C  CA  . CYS H  1 111 ? 145.339 9.653   6.172  1.00 41.84  ? 111  CYS H CA  1 
ATOM   8611  C  C   . CYS H  1 111 ? 145.533 9.604   7.690  1.00 31.86  ? 111  CYS H C   1 
ATOM   8612  O  O   . CYS H  1 111 ? 146.644 9.666   8.210  1.00 46.01  ? 111  CYS H O   1 
ATOM   8613  C  CB  . CYS H  1 111 ? 145.718 8.341   5.492  1.00 45.26  ? 111  CYS H CB  1 
ATOM   8614  S  SG  . CYS H  1 111 ? 145.640 6.924   6.580  1.00 72.35  ? 111  CYS H SG  1 
ATOM   8615  N  N   . ILE H  1 112 ? 144.409 9.522   8.372  1.00 31.69  ? 112  ILE H N   1 
ATOM   8616  C  CA  . ILE H  1 112 ? 144.331 9.589   9.819  1.00 30.71  ? 112  ILE H CA  1 
ATOM   8617  C  C   . ILE H  1 112 ? 144.261 8.208   10.440 1.00 38.75  ? 112  ILE H C   1 
ATOM   8618  O  O   . ILE H  1 112 ? 144.194 8.076   11.662 1.00 30.70  ? 112  ILE H O   1 
ATOM   8619  C  CB  . ILE H  1 112 ? 143.076 10.377  10.230 1.00 27.38  ? 112  ILE H CB  1 
ATOM   8620  C  CG1 . ILE H  1 112 ? 141.766 9.713   9.828  1.00 28.70  ? 112  ILE H CG1 1 
ATOM   8621  C  CG2 . ILE H  1 112 ? 143.186 11.796  9.680  1.00 35.17  ? 112  ILE H CG2 1 
ATOM   8622  C  CD1 . ILE H  1 112 ? 140.528 10.442  10.314 1.00 29.18  ? 112  ILE H CD1 1 
ATOM   8623  N  N   . ILE H  1 113 ? 144.273 7.162   9.612  1.00 31.05  ? 113  ILE H N   1 
ATOM   8624  C  CA  . ILE H  1 113 ? 144.300 5.828   10.243 1.00 36.30  ? 113  ILE H CA  1 
ATOM   8625  C  C   . ILE H  1 113 ? 145.576 5.651   11.041 1.00 27.25  ? 113  ILE H C   1 
ATOM   8626  O  O   . ILE H  1 113 ? 146.694 6.020   10.669 1.00 31.17  ? 113  ILE H O   1 
ATOM   8627  C  CB  . ILE H  1 113 ? 144.175 4.707   9.197  1.00 38.95  ? 113  ILE H CB  1 
ATOM   8628  C  CG1 . ILE H  1 113 ? 142.929 4.811   8.324  1.00 34.10  ? 113  ILE H CG1 1 
ATOM   8629  C  CG2 . ILE H  1 113 ? 144.262 3.327   9.851  1.00 34.55  ? 113  ILE H CG2 1 
ATOM   8630  C  CD1 . ILE H  1 113 ? 141.630 4.600   9.076  1.00 29.13  ? 113  ILE H CD1 1 
ATOM   8631  N  N   . GLY H  1 114 ? 145.494 5.054   12.237 1.00 27.15  ? 114  GLY H N   1 
ATOM   8632  C  CA  . GLY H  1 114 ? 146.742 4.884   12.971 1.00 27.59  ? 114  GLY H CA  1 
ATOM   8633  C  C   . GLY H  1 114 ? 147.121 6.102   13.779 1.00 30.93  ? 114  GLY H C   1 
ATOM   8634  O  O   . GLY H  1 114 ? 148.108 6.118   14.527 1.00 28.29  ? 114  GLY H O   1 
ATOM   8635  N  N   . ARG H  1 115 ? 146.338 7.188   13.649 1.00 25.30  ? 115  ARG H N   1 
ATOM   8636  C  CA  . ARG H  1 115 ? 146.713 8.354   14.456 1.00 22.94  ? 115  ARG H CA  1 
ATOM   8637  C  C   . ARG H  1 115 ? 145.715 8.502   15.596 1.00 26.57  ? 115  ARG H C   1 
ATOM   8638  O  O   . ARG H  1 115 ? 144.879 7.614   15.783 1.00 29.33  ? 115  ARG H O   1 
ATOM   8639  C  CB  . ARG H  1 115 ? 146.776 9.620   13.570 1.00 25.21  ? 115  ARG H CB  1 
ATOM   8640  C  CG  . ARG H  1 115 ? 147.812 9.405   12.467 1.00 28.61  ? 115  ARG H CG  1 
ATOM   8641  C  CD  . ARG H  1 115 ? 147.886 10.554  11.490 1.00 37.82  ? 115  ARG H CD  1 
ATOM   8642  N  NE  . ARG H  1 115 ? 148.769 10.248  10.364 1.00 33.11  ? 115  ARG H NE  1 
ATOM   8643  C  CZ  . ARG H  1 115 ? 150.086 10.307  10.364 1.00 33.56  ? 115  ARG H CZ  1 
ATOM   8644  N  NH1 . ARG H  1 115 ? 150.766 10.003  9.256  1.00 41.20  ? 115  ARG H NH1 1 
ATOM   8645  N  NH2 . ARG H  1 115 ? 150.780 10.667  11.436 1.00 32.38  ? 115  ARG H NH2 1 
ATOM   8646  N  N   . THR H  1 116 ? 145.776 9.590   16.365 1.00 26.44  ? 116  THR H N   1 
ATOM   8647  C  CA  . THR H  1 116 ? 144.954 9.674   17.576 1.00 22.92  ? 116  THR H CA  1 
ATOM   8648  C  C   . THR H  1 116 ? 143.903 10.784  17.519 1.00 28.44  ? 116  THR H C   1 
ATOM   8649  O  O   . THR H  1 116 ? 144.216 11.932  17.198 1.00 24.89  ? 116  THR H O   1 
ATOM   8650  C  CB  . THR H  1 116 ? 145.861 9.929   18.792 1.00 28.14  ? 116  THR H CB  1 
ATOM   8651  O  OG1 . THR H  1 116 ? 146.698 8.766   19.005 1.00 26.99  ? 116  THR H OG1 1 
ATOM   8652  C  CG2 . THR H  1 116 ? 145.024 10.131  20.045 1.00 26.29  ? 116  THR H CG2 1 
ATOM   8653  N  N   . LEU H  1 117 ? 142.670 10.441  17.856 1.00 20.24  ? 117  LEU H N   1 
ATOM   8654  C  CA  . LEU H  1 117 ? 141.611 11.442  17.983 1.00 24.93  ? 117  LEU H CA  1 
ATOM   8655  C  C   . LEU H  1 117 ? 141.599 11.952  19.428 1.00 32.07  ? 117  LEU H C   1 
ATOM   8656  O  O   . LEU H  1 117 ? 141.635 11.084  20.309 1.00 24.53  ? 117  LEU H O   1 
ATOM   8657  C  CB  . LEU H  1 117 ? 140.271 10.834  17.602 1.00 19.98  ? 117  LEU H CB  1 
ATOM   8658  C  CG  . LEU H  1 117 ? 139.057 11.764  17.687 1.00 23.38  ? 117  LEU H CG  1 
ATOM   8659  C  CD1 . LEU H  1 117 ? 139.133 12.908  16.687 1.00 22.96  ? 117  LEU H CD1 1 
ATOM   8660  C  CD2 . LEU H  1 117 ? 137.764 10.968  17.465 1.00 26.62  ? 117  LEU H CD2 1 
ATOM   8661  N  N   . VAL H  1 118 ? 141.558 13.254  19.663 1.00 22.06  ? 118  VAL H N   1 
ATOM   8662  C  CA  . VAL H  1 118 ? 141.570 13.849  20.997 1.00 19.81  ? 118  VAL H CA  1 
ATOM   8663  C  C   . VAL H  1 118 ? 140.430 14.831  21.202 1.00 24.04  ? 118  VAL H C   1 
ATOM   8664  O  O   . VAL H  1 118 ? 140.158 15.672  20.345 1.00 24.90  ? 118  VAL H O   1 
ATOM   8665  C  CB  . VAL H  1 118 ? 142.890 14.606  21.272 1.00 25.18  ? 118  VAL H CB  1 
ATOM   8666  C  CG1 . VAL H  1 118 ? 142.941 15.228  22.663 1.00 22.77  ? 118  VAL H CG1 1 
ATOM   8667  C  CG2 . VAL H  1 118 ? 144.083 13.664  21.080 1.00 29.14  ? 118  VAL H CG2 1 
ATOM   8668  N  N   . VAL H  1 119 ? 139.744 14.758  22.335 1.00 23.21  ? 119  VAL H N   1 
ATOM   8669  C  CA  . VAL H  1 119 ? 138.746 15.771  22.689 1.00 21.96  ? 119  VAL H CA  1 
ATOM   8670  C  C   . VAL H  1 119 ? 139.266 16.533  23.908 1.00 22.76  ? 119  VAL H C   1 
ATOM   8671  O  O   . VAL H  1 119 ? 139.820 15.888  24.821 1.00 24.44  ? 119  VAL H O   1 
ATOM   8672  C  CB  . VAL H  1 119 ? 137.354 15.174  22.951 1.00 21.18  ? 119  VAL H CB  1 
ATOM   8673  C  CG1 . VAL H  1 119 ? 137.363 14.132  24.070 1.00 23.84  ? 119  VAL H CG1 1 
ATOM   8674  C  CG2 . VAL H  1 119 ? 136.395 16.321  23.288 1.00 19.82  ? 119  VAL H CG2 1 
ATOM   8675  N  N   . HIS H  1 120 ? 139.131 17.848  23.926 1.00 20.35  ? 120  HIS H N   1 
ATOM   8676  C  CA  . HIS H  1 120 ? 139.832 18.701  24.864 1.00 22.15  ? 120  HIS H CA  1 
ATOM   8677  C  C   . HIS H  1 120 ? 138.925 19.292  25.938 1.00 24.49  ? 120  HIS H C   1 
ATOM   8678  O  O   . HIS H  1 120 ? 137.687 19.312  25.870 1.00 23.87  ? 120  HIS H O   1 
ATOM   8679  C  CB  . HIS H  1 120 ? 140.516 19.880  24.134 1.00 22.32  ? 120  HIS H CB  1 
ATOM   8680  C  CG  . HIS H  1 120 ? 141.745 19.450  23.362 1.00 26.07  ? 120  HIS H CG  1 
ATOM   8681  N  ND1 . HIS H  1 120 ? 143.039 19.607  23.790 1.00 23.50  ? 120  HIS H ND1 1 
ATOM   8682  C  CD2 . HIS H  1 120 ? 141.852 18.850  22.153 1.00 21.82  ? 120  HIS H CD2 1 
ATOM   8683  C  CE1 . HIS H  1 120 ? 143.889 19.113  22.885 1.00 22.96  ? 120  HIS H CE1 1 
ATOM   8684  N  NE2 . HIS H  1 120 ? 143.177 18.643  21.868 1.00 21.73  ? 120  HIS H NE2 1 
ATOM   8685  N  N   . GLU H  1 121 ? 139.647 19.807  26.930 1.00 24.34  ? 121  GLU H N   1 
ATOM   8686  C  CA  . GLU H  1 121 ? 139.135 20.477  28.108 1.00 22.01  ? 121  GLU H CA  1 
ATOM   8687  C  C   . GLU H  1 121 ? 138.285 21.702  27.800 1.00 23.85  ? 121  GLU H C   1 
ATOM   8688  O  O   . GLU H  1 121 ? 137.210 21.834  28.401 1.00 28.15  ? 121  GLU H O   1 
ATOM   8689  C  CB  . GLU H  1 121 ? 140.327 20.971  28.944 1.00 26.69  ? 121  GLU H CB  1 
ATOM   8690  C  CG  . GLU H  1 121 ? 139.971 21.819  30.144 1.00 30.31  ? 121  GLU H CG  1 
ATOM   8691  C  CD  . GLU H  1 121 ? 141.226 22.489  30.700 1.00 44.87  ? 121  GLU H CD  1 
ATOM   8692  O  OE1 . GLU H  1 121 ? 141.102 23.094  31.783 1.00 46.64  ? 121  GLU H OE1 1 
ATOM   8693  O  OE2 . GLU H  1 121 ? 142.297 22.405  30.056 1.00 40.18  ? 121  GLU H OE2 1 
ATOM   8694  N  N   . LYS H  1 122 ? 138.810 22.544  26.919 1.00 23.27  ? 122  LYS H N   1 
ATOM   8695  C  CA  . LYS H  1 122 ? 138.303 23.858  26.566 1.00 30.30  ? 122  LYS H CA  1 
ATOM   8696  C  C   . LYS H  1 122 ? 137.918 24.012  25.092 1.00 24.77  ? 122  LYS H C   1 
ATOM   8697  O  O   . LYS H  1 122 ? 138.235 23.159  24.263 1.00 23.45  ? 122  LYS H O   1 
ATOM   8698  C  CB  . LYS H  1 122 ? 139.386 24.938  26.789 1.00 29.99  ? 122  LYS H CB  1 
ATOM   8699  C  CG  . LYS H  1 122 ? 139.768 25.204  28.222 1.00 39.04  ? 122  LYS H CG  1 
ATOM   8700  C  CD  . LYS H  1 122 ? 140.588 26.487  28.328 1.00 44.13  ? 122  LYS H CD  1 
ATOM   8701  C  CE  . LYS H  1 122 ? 142.009 26.164  28.756 1.00 60.76  ? 122  LYS H CE  1 
ATOM   8702  N  NZ  . LYS H  1 122 ? 142.066 25.790  30.198 1.00 82.02  ? 122  LYS H NZ  1 
ATOM   8703  N  N   . ALA H  1 123 ? 137.280 25.129  24.786 1.00 23.32  ? 123  ALA H N   1 
ATOM   8704  C  CA  . ALA H  1 123 ? 136.974 25.438  23.394 1.00 26.30  ? 123  ALA H CA  1 
ATOM   8705  C  C   . ALA H  1 123 ? 138.227 25.699  22.562 1.00 27.28  ? 123  ALA H C   1 
ATOM   8706  O  O   . ALA H  1 123 ? 139.228 26.249  23.032 1.00 24.45  ? 123  ALA H O   1 
ATOM   8707  C  CB  . ALA H  1 123 ? 136.060 26.659  23.300 1.00 26.55  ? 123  ALA H CB  1 
ATOM   8708  N  N   . ASP H  1 124 ? 138.148 25.313  21.290 1.00 23.21  ? 124  ASP H N   1 
ATOM   8709  C  CA  . ASP H  1 124 ? 139.188 25.609  20.289 1.00 22.80  ? 124  ASP H CA  1 
ATOM   8710  C  C   . ASP H  1 124 ? 138.877 27.013  19.759 1.00 23.53  ? 124  ASP H C   1 
ATOM   8711  O  O   . ASP H  1 124 ? 137.756 27.232  19.287 1.00 22.38  ? 124  ASP H O   1 
ATOM   8712  C  CB  . ASP H  1 124 ? 139.197 24.514  19.229 1.00 18.47  ? 124  ASP H CB  1 
ATOM   8713  C  CG  . ASP H  1 124 ? 140.260 24.639  18.163 1.00 23.91  ? 124  ASP H CG  1 
ATOM   8714  O  OD1 . ASP H  1 124 ? 140.624 23.648  17.485 1.00 23.49  ? 124  ASP H OD1 1 
ATOM   8715  O  OD2 . ASP H  1 124 ? 140.759 25.772  17.998 1.00 24.31  ? 124  ASP H OD2 1 
ATOM   8716  N  N   . ASP H  1 125 ? 139.844 27.938  19.875 1.00 20.16  ? 125  ASP H N   1 
ATOM   8717  C  CA  . ASP H  1 125 ? 139.519 29.294  19.413 1.00 20.63  ? 125  ASP H CA  1 
ATOM   8718  C  C   . ASP H  1 125 ? 139.707 29.423  17.899 1.00 28.09  ? 125  ASP H C   1 
ATOM   8719  O  O   . ASP H  1 125 ? 139.544 30.518  17.358 1.00 23.26  ? 125  ASP H O   1 
ATOM   8720  C  CB  . ASP H  1 125 ? 140.347 30.347  20.136 1.00 21.05  ? 125  ASP H CB  1 
ATOM   8721  C  CG  . ASP H  1 125 ? 141.838 30.349  19.896 1.00 26.55  ? 125  ASP H CG  1 
ATOM   8722  O  OD1 . ASP H  1 125 ? 142.563 30.981  20.700 1.00 26.34  ? 125  ASP H OD1 1 
ATOM   8723  O  OD2 . ASP H  1 125 ? 142.369 29.740  18.944 1.00 23.59  ? 125  ASP H OD2 1 
ATOM   8724  N  N   . LEU H  1 126 ? 140.038 28.327  17.240 1.00 21.82  ? 126  LEU H N   1 
ATOM   8725  C  CA  . LEU H  1 126 ? 140.044 28.230  15.789 1.00 20.36  ? 126  LEU H CA  1 
ATOM   8726  C  C   . LEU H  1 126 ? 141.125 29.120  15.181 1.00 21.96  ? 126  LEU H C   1 
ATOM   8727  O  O   . LEU H  1 126 ? 141.028 29.528  14.019 1.00 23.42  ? 126  LEU H O   1 
ATOM   8728  C  CB  . LEU H  1 126 ? 138.661 28.541  15.217 1.00 22.78  ? 126  LEU H CB  1 
ATOM   8729  C  CG  . LEU H  1 126 ? 137.468 27.752  15.790 1.00 24.05  ? 126  LEU H CG  1 
ATOM   8730  C  CD1 . LEU H  1 126 ? 136.184 28.145  15.093 1.00 28.39  ? 126  LEU H CD1 1 
ATOM   8731  C  CD2 . LEU H  1 126 ? 137.657 26.237  15.676 1.00 22.67  ? 126  LEU H CD2 1 
ATOM   8732  N  N   . GLY H  1 127 ? 142.161 29.367  15.976 1.00 20.38  ? 127  GLY H N   1 
ATOM   8733  C  CA  . GLY H  1 127 ? 143.301 30.152  15.514 1.00 21.63  ? 127  GLY H CA  1 
ATOM   8734  C  C   . GLY H  1 127 ? 143.049 31.648  15.576 1.00 25.13  ? 127  GLY H C   1 
ATOM   8735  O  O   . GLY H  1 127 ? 143.872 32.420  15.068 1.00 22.56  ? 127  GLY H O   1 
ATOM   8736  N  N   . LYS H  1 128 ? 141.954 32.088  16.188 1.00 23.28  ? 128  LYS H N   1 
ATOM   8737  C  CA  . LYS H  1 128 ? 141.602 33.506  16.255 1.00 21.03  ? 128  LYS H CA  1 
ATOM   8738  C  C   . LYS H  1 128 ? 141.940 34.201  17.573 1.00 20.64  ? 128  LYS H C   1 
ATOM   8739  O  O   . LYS H  1 128 ? 141.394 35.298  17.797 1.00 22.97  ? 128  LYS H O   1 
ATOM   8740  C  CB  . LYS H  1 128 ? 140.083 33.661  15.997 1.00 24.07  ? 128  LYS H CB  1 
ATOM   8741  C  CG  . LYS H  1 128 ? 139.711 33.011  14.654 1.00 30.08  ? 128  LYS H CG  1 
ATOM   8742  C  CD  . LYS H  1 128 ? 138.279 33.378  14.276 1.00 36.89  ? 128  LYS H CD  1 
ATOM   8743  C  CE  . LYS H  1 128 ? 138.054 33.378  12.775 1.00 46.43  ? 128  LYS H CE  1 
ATOM   8744  N  NZ  . LYS H  1 128 ? 136.798 34.123  12.443 1.00 61.68  ? 128  LYS H NZ  1 
ATOM   8745  N  N   . GLY H  1 129 ? 142.799 33.618  18.391 1.00 22.23  ? 129  GLY H N   1 
ATOM   8746  C  CA  . GLY H  1 129 ? 143.121 34.060  19.734 1.00 23.60  ? 129  GLY H CA  1 
ATOM   8747  C  C   . GLY H  1 129 ? 144.240 35.079  19.829 1.00 26.21  ? 129  GLY H C   1 
ATOM   8748  O  O   . GLY H  1 129 ? 144.437 35.665  20.896 1.00 25.38  ? 129  GLY H O   1 
ATOM   8749  N  N   . GLY H  1 130 ? 144.982 35.317  18.758 1.00 22.00  ? 130  GLY H N   1 
ATOM   8750  C  CA  . GLY H  1 130 ? 145.954 36.410  18.803 1.00 22.39  ? 130  GLY H CA  1 
ATOM   8751  C  C   . GLY H  1 130 ? 147.271 36.082  19.484 1.00 28.21  ? 130  GLY H C   1 
ATOM   8752  O  O   . GLY H  1 130 ? 148.104 37.008  19.573 1.00 27.43  ? 130  GLY H O   1 
ATOM   8753  N  N   . ASN H  1 131 ? 147.515 34.861  19.946 1.00 30.16  ? 131  ASN H N   1 
ATOM   8754  C  CA  . ASN H  1 131 ? 148.805 34.420  20.478 1.00 26.67  ? 131  ASN H CA  1 
ATOM   8755  C  C   . ASN H  1 131 ? 149.345 33.200  19.755 1.00 31.11  ? 131  ASN H C   1 
ATOM   8756  O  O   . ASN H  1 131 ? 148.709 32.518  18.970 1.00 31.82  ? 131  ASN H O   1 
ATOM   8757  C  CB  . ASN H  1 131 ? 148.756 34.126  21.979 1.00 33.64  ? 131  ASN H CB  1 
ATOM   8758  C  CG  . ASN H  1 131 ? 147.643 33.189  22.398 1.00 40.19  ? 131  ASN H CG  1 
ATOM   8759  O  OD1 . ASN H  1 131 ? 147.189 32.399  21.582 1.00 31.80  ? 131  ASN H OD1 1 
ATOM   8760  N  ND2 . ASN H  1 131 ? 147.191 33.272  23.643 1.00 34.17  ? 131  ASN H ND2 1 
ATOM   8761  N  N   . GLU H  1 132 ? 150.609 32.896  20.041 1.00 32.70  ? 132  GLU H N   1 
ATOM   8762  C  CA  . GLU H  1 132 ? 151.335 31.752  19.510 1.00 37.14  ? 132  GLU H CA  1 
ATOM   8763  C  C   . GLU H  1 132 ? 150.549 30.458  19.697 1.00 27.75  ? 132  GLU H C   1 
ATOM   8764  O  O   . GLU H  1 132 ? 150.400 29.625  18.807 1.00 35.59  ? 132  GLU H O   1 
ATOM   8765  C  CB  . GLU H  1 132 ? 152.679 31.685  20.246 1.00 44.51  ? 132  GLU H CB  1 
ATOM   8766  C  CG  . GLU H  1 132 ? 153.779 30.823  19.672 1.00 62.91  ? 132  GLU H CG  1 
ATOM   8767  C  CD  . GLU H  1 132 ? 154.904 30.605  20.676 1.00 75.36  ? 132  GLU H CD  1 
ATOM   8768  O  OE1 . GLU H  1 132 ? 155.695 31.550  20.886 1.00 98.16  ? 132  GLU H OE1 1 
ATOM   8769  O  OE2 . GLU H  1 132 ? 154.995 29.503  21.261 1.00 80.43  ? 132  GLU H OE2 1 
ATOM   8770  N  N   . GLU H  1 133 ? 150.045 30.321  20.923 1.00 29.19  ? 133  GLU H N   1 
ATOM   8771  C  CA  . GLU H  1 133 ? 149.290 29.135  21.321 1.00 28.82  ? 133  GLU H CA  1 
ATOM   8772  C  C   . GLU H  1 133 ? 148.068 28.954  20.433 1.00 26.61  ? 133  GLU H C   1 
ATOM   8773  O  O   . GLU H  1 133 ? 147.755 27.847  20.004 1.00 28.83  ? 133  GLU H O   1 
ATOM   8774  C  CB  . GLU H  1 133 ? 148.920 29.270  22.802 1.00 27.83  ? 133  GLU H CB  1 
ATOM   8775  C  CG  . GLU H  1 133 ? 148.368 27.987  23.406 1.00 38.65  ? 133  GLU H CG  1 
ATOM   8776  C  CD  . GLU H  1 133 ? 149.406 26.877  23.349 1.00 51.31  ? 133  GLU H CD  1 
ATOM   8777  O  OE1 . GLU H  1 133 ? 149.109 25.809  22.779 1.00 60.34  ? 133  GLU H OE1 1 
ATOM   8778  O  OE2 . GLU H  1 133 ? 150.515 27.089  23.880 1.00 49.22  ? 133  GLU H OE2 1 
ATOM   8779  N  N   . SER H  1 134 ? 147.347 30.043  20.136 1.00 25.94  ? 134  SER H N   1 
ATOM   8780  C  CA  . SER H  1 134 ? 146.189 29.940  19.263 1.00 21.94  ? 134  SER H CA  1 
ATOM   8781  C  C   . SER H  1 134 ? 146.560 29.323  17.927 1.00 24.28  ? 134  SER H C   1 
ATOM   8782  O  O   . SER H  1 134 ? 145.796 28.521  17.374 1.00 26.09  ? 134  SER H O   1 
ATOM   8783  C  CB  . SER H  1 134 ? 145.561 31.329  19.062 1.00 28.20  ? 134  SER H CB  1 
ATOM   8784  O  OG  . SER H  1 134 ? 144.451 31.244  18.180 1.00 24.95  ? 134  SER H OG  1 
ATOM   8785  N  N   . THR H  1 135 ? 147.742 29.673  17.375 1.00 24.18  ? 135  THR H N   1 
ATOM   8786  C  CA  . THR H  1 135 ? 148.009 29.142  16.025 1.00 26.63  ? 135  THR H CA  1 
ATOM   8787  C  C   . THR H  1 135 ? 148.812 27.851  16.088 1.00 22.22  ? 135  THR H C   1 
ATOM   8788  O  O   . THR H  1 135 ? 149.294 27.362  15.071 1.00 29.25  ? 135  THR H O   1 
ATOM   8789  C  CB  . THR H  1 135 ? 148.633 30.228  15.147 1.00 41.00  ? 135  THR H CB  1 
ATOM   8790  O  OG1 . THR H  1 135 ? 149.512 31.041  15.923 1.00 45.84  ? 135  THR H OG1 1 
ATOM   8791  C  CG2 . THR H  1 135 ? 147.511 31.157  14.662 1.00 39.66  ? 135  THR H CG2 1 
ATOM   8792  N  N   . LYS H  1 136 ? 148.886 27.278  17.289 1.00 26.64  ? 136  LYS H N   1 
ATOM   8793  C  CA  . LYS H  1 136 ? 149.420 25.933  17.482 1.00 28.34  ? 136  LYS H CA  1 
ATOM   8794  C  C   . LYS H  1 136 ? 148.322 24.941  17.886 1.00 26.79  ? 136  LYS H C   1 
ATOM   8795  O  O   . LYS H  1 136 ? 148.139 23.888  17.278 1.00 26.68  ? 136  LYS H O   1 
ATOM   8796  C  CB  . LYS H  1 136 ? 150.489 25.915  18.567 1.00 32.95  ? 136  LYS H CB  1 
ATOM   8797  C  CG  . LYS H  1 136 ? 151.821 26.521  18.161 1.00 51.73  ? 136  LYS H CG  1 
ATOM   8798  C  CD  . LYS H  1 136 ? 152.743 26.612  19.366 1.00 57.90  ? 136  LYS H CD  1 
ATOM   8799  C  CE  . LYS H  1 136 ? 153.914 25.647  19.252 1.00 60.07  ? 136  LYS H CE  1 
ATOM   8800  N  NZ  . LYS H  1 136 ? 154.909 25.919  20.334 1.00 76.10  ? 136  LYS H NZ  1 
ATOM   8801  N  N   . THR H  1 137 ? 147.577 25.291  18.934 1.00 26.03  ? 137  THR H N   1 
ATOM   8802  C  CA  . THR H  1 137 ? 146.610 24.368  19.534 1.00 27.80  ? 137  THR H CA  1 
ATOM   8803  C  C   . THR H  1 137 ? 145.216 24.951  19.643 1.00 31.41  ? 137  THR H C   1 
ATOM   8804  O  O   . THR H  1 137 ? 144.301 24.218  20.048 1.00 27.34  ? 137  THR H O   1 
ATOM   8805  C  CB  . THR H  1 137 ? 147.048 23.970  20.961 1.00 30.91  ? 137  THR H CB  1 
ATOM   8806  O  OG1 . THR H  1 137 ? 147.067 25.143  21.797 1.00 34.17  ? 137  THR H OG1 1 
ATOM   8807  C  CG2 . THR H  1 137 ? 148.459 23.423  20.979 1.00 31.40  ? 137  THR H CG2 1 
ATOM   8808  N  N   . GLY H  1 138 ? 145.006 26.228  19.291 1.00 22.86  ? 138  GLY H N   1 
ATOM   8809  C  CA  . GLY H  1 138 ? 143.661 26.782  19.453 1.00 21.44  ? 138  GLY H CA  1 
ATOM   8810  C  C   . GLY H  1 138 ? 143.357 27.089  20.910 1.00 22.75  ? 138  GLY H C   1 
ATOM   8811  O  O   . GLY H  1 138 ? 142.215 27.404  21.230 1.00 23.23  ? 138  GLY H O   1 
ATOM   8812  N  N   . ASN H  1 139 ? 144.347 26.988  21.797 1.00 25.52  ? 139  ASN H N   1 
ATOM   8813  C  CA  . ASN H  1 139 ? 144.096 27.227  23.233 1.00 23.05  ? 139  ASN H CA  1 
ATOM   8814  C  C   . ASN H  1 139 ? 143.048 26.261  23.794 1.00 25.64  ? 139  ASN H C   1 
ATOM   8815  O  O   . ASN H  1 139 ? 142.276 26.600  24.698 1.00 25.21  ? 139  ASN H O   1 
ATOM   8816  C  CB  . ASN H  1 139 ? 143.660 28.670  23.462 1.00 23.35  ? 139  ASN H CB  1 
ATOM   8817  C  CG  . ASN H  1 139 ? 144.803 29.661  23.325 1.00 32.53  ? 139  ASN H CG  1 
ATOM   8818  O  OD1 . ASN H  1 139 ? 145.792 29.577  24.061 1.00 28.80  ? 139  ASN H OD1 1 
ATOM   8819  N  ND2 . ASN H  1 139 ? 144.696 30.604  22.392 1.00 27.70  ? 139  ASN H ND2 1 
ATOM   8820  N  N   . ALA H  1 140 ? 142.979 25.034  23.298 1.00 22.93  ? 140  ALA H N   1 
ATOM   8821  C  CA  . ALA H  1 140 ? 141.916 24.124  23.722 1.00 32.34  ? 140  ALA H CA  1 
ATOM   8822  C  C   . ALA H  1 140 ? 142.252 23.432  25.043 1.00 29.08  ? 140  ALA H C   1 
ATOM   8823  O  O   . ALA H  1 140 ? 141.430 22.675  25.566 1.00 25.54  ? 140  ALA H O   1 
ATOM   8824  C  CB  . ALA H  1 140 ? 141.625 23.062  22.661 1.00 24.36  ? 140  ALA H CB  1 
ATOM   8825  N  N   . GLY H  1 141 ? 143.431 23.686  25.588 1.00 26.11  ? 141  GLY H N   1 
ATOM   8826  C  CA  . GLY H  1 141 ? 143.760 23.180  26.912 1.00 26.68  ? 141  GLY H CA  1 
ATOM   8827  C  C   . GLY H  1 141 ? 143.989 21.698  26.984 1.00 28.28  ? 141  GLY H C   1 
ATOM   8828  O  O   . GLY H  1 141 ? 144.442 21.061  26.026 1.00 26.12  ? 141  GLY H O   1 
ATOM   8829  N  N   . SER H  1 142 ? 143.701 21.061  28.139 1.00 23.31  ? 142  SER H N   1 
ATOM   8830  C  CA  . SER H  1 142 ? 144.193 19.682  28.227 1.00 25.58  ? 142  SER H CA  1 
ATOM   8831  C  C   . SER H  1 142 ? 143.364 18.678  27.423 1.00 24.27  ? 142  SER H C   1 
ATOM   8832  O  O   . SER H  1 142 ? 142.304 18.949  26.897 1.00 27.67  ? 142  SER H O   1 
ATOM   8833  C  CB  . SER H  1 142 ? 144.246 19.235  29.696 1.00 31.23  ? 142  SER H CB  1 
ATOM   8834  O  OG  . SER H  1 142 ? 142.913 19.135  30.173 1.00 43.16  ? 142  SER H OG  1 
ATOM   8835  N  N   . ARG H  1 143 ? 143.920 17.479  27.351 1.00 23.01  ? 143  ARG H N   1 
ATOM   8836  C  CA  . ARG H  1 143 ? 143.398 16.345  26.626 1.00 25.20  ? 143  ARG H CA  1 
ATOM   8837  C  C   . ARG H  1 143 ? 142.593 15.457  27.571 1.00 36.80  ? 143  ARG H C   1 
ATOM   8838  O  O   . ARG H  1 143 ? 143.184 14.791  28.425 1.00 29.77  ? 143  ARG H O   1 
ATOM   8839  C  CB  . ARG H  1 143 ? 144.562 15.551  26.015 1.00 29.49  ? 143  ARG H CB  1 
ATOM   8840  C  CG  . ARG H  1 143 ? 145.445 16.401  25.111 1.00 28.89  ? 143  ARG H CG  1 
ATOM   8841  C  CD  . ARG H  1 143 ? 146.733 15.698  24.701 1.00 30.17  ? 143  ARG H CD  1 
ATOM   8842  N  NE  . ARG H  1 143 ? 147.576 16.627  23.949 1.00 27.85  ? 143  ARG H NE  1 
ATOM   8843  C  CZ  . ARG H  1 143 ? 148.540 16.370  23.085 1.00 31.19  ? 143  ARG H CZ  1 
ATOM   8844  N  NH1 . ARG H  1 143 ? 149.161 17.405  22.522 1.00 30.63  ? 143  ARG H NH1 1 
ATOM   8845  N  NH2 . ARG H  1 143 ? 148.930 15.148  22.755 1.00 29.39  ? 143  ARG H NH2 1 
ATOM   8846  N  N   . LEU H  1 144 ? 141.292 15.473  27.403 1.00 26.59  ? 144  LEU H N   1 
ATOM   8847  C  CA  . LEU H  1 144 ? 140.387 14.778  28.331 1.00 25.59  ? 144  LEU H CA  1 
ATOM   8848  C  C   . LEU H  1 144 ? 140.284 13.317  27.985 1.00 25.89  ? 144  LEU H C   1 
ATOM   8849  O  O   . LEU H  1 144 ? 140.159 12.490  28.879 1.00 25.16  ? 144  LEU H O   1 
ATOM   8850  C  CB  . LEU H  1 144 ? 138.990 15.410  28.347 1.00 22.97  ? 144  LEU H CB  1 
ATOM   8851  C  CG  . LEU H  1 144 ? 138.977 16.858  28.885 1.00 29.62  ? 144  LEU H CG  1 
ATOM   8852  C  CD1 . LEU H  1 144 ? 137.558 17.350  29.082 1.00 36.76  ? 144  LEU H CD1 1 
ATOM   8853  C  CD2 . LEU H  1 144 ? 139.789 16.955  30.173 1.00 32.38  ? 144  LEU H CD2 1 
ATOM   8854  N  N   . ALA H  1 145 ? 140.341 12.987  26.695 1.00 22.57  ? 145  ALA H N   1 
ATOM   8855  C  CA  . ALA H  1 145 ? 140.212 11.612  26.283 1.00 20.79  ? 145  ALA H CA  1 
ATOM   8856  C  C   . ALA H  1 145 ? 140.716 11.521  24.832 1.00 26.70  ? 145  ALA H C   1 
ATOM   8857  O  O   . ALA H  1 145 ? 140.665 12.536  24.135 1.00 25.89  ? 145  ALA H O   1 
ATOM   8858  C  CB  . ALA H  1 145 ? 138.786 11.086  26.348 1.00 25.07  ? 145  ALA H CB  1 
ATOM   8859  N  N   . CYS H  1 146 ? 141.149 10.319  24.499 1.00 25.90  ? 146  CYS H N   1 
ATOM   8860  C  CA  . CYS H  1 146 ? 141.791 10.057  23.210 1.00 24.41  ? 146  CYS H CA  1 
ATOM   8861  C  C   . CYS H  1 146 ? 141.697 8.583   22.863 1.00 27.15  ? 146  CYS H C   1 
ATOM   8862  O  O   . CYS H  1 146 ? 141.438 7.711   23.702 1.00 25.00  ? 146  CYS H O   1 
ATOM   8863  C  CB  A CYS H  1 146 ? 143.240 10.528  23.182 0.43 28.94  ? 146  CYS H CB  1 
ATOM   8864  C  CB  B CYS H  1 146 ? 143.239 10.536  23.331 0.57 31.96  ? 146  CYS H CB  1 
ATOM   8865  S  SG  A CYS H  1 146 ? 144.312 9.840   24.464 0.43 35.20  ? 146  CYS H SG  1 
ATOM   8866  S  SG  B CYS H  1 146 ? 144.423 9.458   24.167 0.57 35.95  ? 146  CYS H SG  1 
ATOM   8867  N  N   . GLY H  1 147 ? 141.901 8.284   21.584 1.00 22.99  ? 147  GLY H N   1 
ATOM   8868  C  CA  . GLY H  1 147 ? 141.946 6.860   21.224 1.00 27.49  ? 147  GLY H CA  1 
ATOM   8869  C  C   . GLY H  1 147 ? 142.536 6.724   19.840 1.00 31.92  ? 147  GLY H C   1 
ATOM   8870  O  O   . GLY H  1 147 ? 142.474 7.664   19.031 1.00 31.64  ? 147  GLY H O   1 
ATOM   8871  N  N   . VAL H  1 148 ? 143.132 5.576   19.543 1.00 25.52  ? 148  VAL H N   1 
ATOM   8872  C  CA  . VAL H  1 148 ? 143.738 5.428   18.220 1.00 25.72  ? 148  VAL H CA  1 
ATOM   8873  C  C   . VAL H  1 148 ? 142.684 5.181   17.167 1.00 27.99  ? 148  VAL H C   1 
ATOM   8874  O  O   . VAL H  1 148 ? 141.719 4.430   17.362 1.00 30.25  ? 148  VAL H O   1 
ATOM   8875  C  CB  . VAL H  1 148 ? 144.780 4.281   18.216 1.00 26.34  ? 148  VAL H CB  1 
ATOM   8876  C  CG1 . VAL H  1 148 ? 145.468 4.190   16.866 1.00 29.27  ? 148  VAL H CG1 1 
ATOM   8877  C  CG2 . VAL H  1 148 ? 145.799 4.502   19.327 1.00 27.86  ? 148  VAL H CG2 1 
ATOM   8878  N  N   . ILE H  1 149 ? 142.855 5.816   16.002 1.00 27.27  ? 149  ILE H N   1 
ATOM   8879  C  CA  . ILE H  1 149 ? 141.817 5.645   14.970 1.00 26.27  ? 149  ILE H CA  1 
ATOM   8880  C  C   . ILE H  1 149 ? 142.049 4.357   14.191 1.00 32.39  ? 149  ILE H C   1 
ATOM   8881  O  O   . ILE H  1 149 ? 143.131 4.219   13.603 1.00 28.45  ? 149  ILE H O   1 
ATOM   8882  C  CB  . ILE H  1 149 ? 141.819 6.858   14.027 1.00 25.98  ? 149  ILE H CB  1 
ATOM   8883  C  CG1 . ILE H  1 149 ? 141.385 8.139   14.751 1.00 24.80  ? 149  ILE H CG1 1 
ATOM   8884  C  CG2 . ILE H  1 149 ? 140.942 6.616   12.811 1.00 28.62  ? 149  ILE H CG2 1 
ATOM   8885  C  CD1 . ILE H  1 149 ? 141.778 9.410   14.036 1.00 23.24  ? 149  ILE H CD1 1 
ATOM   8886  N  N   . GLY H  1 150 ? 141.091 3.434   14.196 1.00 31.87  ? 150  GLY H N   1 
ATOM   8887  C  CA  . GLY H  1 150 ? 141.371 2.128   13.589 1.00 30.30  ? 150  GLY H CA  1 
ATOM   8888  C  C   . GLY H  1 150 ? 140.485 1.811   12.415 1.00 33.57  ? 150  GLY H C   1 
ATOM   8889  O  O   . GLY H  1 150 ? 139.403 2.362   12.205 1.00 29.65  ? 150  GLY H O   1 
ATOM   8890  N  N   . ILE H  1 151 ? 140.930 0.872   11.566 1.00 32.67  ? 151  ILE H N   1 
ATOM   8891  C  CA  . ILE H  1 151 ? 140.093 0.507   10.425 1.00 26.45  ? 151  ILE H CA  1 
ATOM   8892  C  C   . ILE H  1 151 ? 138.874 -0.288  10.836 1.00 33.35  ? 151  ILE H C   1 
ATOM   8893  O  O   . ILE H  1 151 ? 138.994 -1.210  11.646 1.00 36.46  ? 151  ILE H O   1 
ATOM   8894  C  CB  . ILE H  1 151 ? 140.932 -0.337  9.433  1.00 39.06  ? 151  ILE H CB  1 
ATOM   8895  C  CG1 . ILE H  1 151 ? 142.175 0.428   8.980  1.00 36.60  ? 151  ILE H CG1 1 
ATOM   8896  C  CG2 . ILE H  1 151 ? 140.082 -0.837  8.279  1.00 34.01  ? 151  ILE H CG2 1 
ATOM   8897  C  CD1 . ILE H  1 151 ? 143.340 -0.455  8.598  1.00 56.05  ? 151  ILE H CD1 1 
ATOM   8898  N  N   . ALA H  1 152 ? 137.721 0.068   10.278 1.00 27.01  ? 152  ALA H N   1 
ATOM   8899  C  CA  . ALA H  1 152 ? 136.478 -0.598  10.612 1.00 29.14  ? 152  ALA H CA  1 
ATOM   8900  C  C   . ALA H  1 152 ? 135.924 -1.342  9.404  1.00 34.17  ? 152  ALA H C   1 
ATOM   8901  O  O   . ALA H  1 152 ? 136.270 -1.044  8.266  1.00 42.78  ? 152  ALA H O   1 
ATOM   8902  C  CB  . ALA H  1 152 ? 135.433 0.371   11.146 1.00 29.28  ? 152  ALA H CB  1 
ATOM   8903  N  N   . GLN H  1 153 ? 135.069 -2.320  9.681  1.00 38.17  ? 153  GLN H N   1 
ATOM   8904  C  CA  . GLN H  1 153 ? 134.512 -3.072  8.553  1.00 55.53  ? 153  GLN H CA  1 
ATOM   8905  C  C   . GLN H  1 153 ? 133.635 -2.124  7.739  1.00 61.34  ? 153  GLN H C   1 
ATOM   8906  O  O   . GLN H  1 153 ? 132.594 -1.712  8.294  1.00 77.75  ? 153  GLN H O   1 
ATOM   8907  C  CB  . GLN H  1 153 ? 133.737 -4.304  9.013  1.00 56.75  ? 153  GLN H CB  1 
ATOM   8908  C  CG  . GLN H  1 153 ? 133.709 -5.452  8.015  1.00 55.24  ? 153  GLN H CG  1 
ATOM   8909  C  CD  . GLN H  1 153 ? 133.568 -6.821  8.655  1.00 61.06  ? 153  GLN H CD  1 
ATOM   8910  O  OE1 . GLN H  1 153 ? 133.310 -6.933  9.857  1.00 49.05  ? 153  GLN H OE1 1 
ATOM   8911  N  NE2 . GLN H  1 153 ? 133.726 -7.877  7.864  1.00 71.78  ? 153  GLN H NE2 1 
ATOM   8912  O  OXT . GLN H  1 153 ? 134.015 -1.805  6.594  1.00 78.43  ? 153  GLN H OXT 1 
ATOM   8913  N  N   . ALA I  1 1   ? 95.307  24.297  -0.739 1.00 79.70  ? 1    ALA I N   1 
ATOM   8914  C  CA  . ALA I  1 1   ? 95.344  23.963  0.682  1.00 71.62  ? 1    ALA I CA  1 
ATOM   8915  C  C   . ALA I  1 1   ? 96.152  24.981  1.481  1.00 62.50  ? 1    ALA I C   1 
ATOM   8916  O  O   . ALA I  1 1   ? 97.287  24.731  1.889  1.00 73.61  ? 1    ALA I O   1 
ATOM   8917  C  CB  . ALA I  1 1   ? 95.905  22.558  0.868  1.00 60.11  ? 1    ALA I CB  1 
ATOM   8918  N  N   . THR I  1 2   ? 95.563  26.151  1.706  1.00 51.76  ? 2    THR I N   1 
ATOM   8919  C  CA  . THR I  1 2   ? 96.248  27.196  2.462  1.00 62.22  ? 2    THR I CA  1 
ATOM   8920  C  C   . THR I  1 2   ? 95.662  27.294  3.866  1.00 54.31  ? 2    THR I C   1 
ATOM   8921  O  O   . THR I  1 2   ? 94.463  27.091  4.064  1.00 42.22  ? 2    THR I O   1 
ATOM   8922  C  CB  . THR I  1 2   ? 96.164  28.564  1.761  1.00 69.73  ? 2    THR I CB  1 
ATOM   8923  O  OG1 . THR I  1 2   ? 96.159  28.413  0.333  1.00 80.53  ? 2    THR I OG1 1 
ATOM   8924  C  CG2 . THR I  1 2   ? 97.394  29.398  2.080  1.00 40.67  ? 2    THR I CG2 1 
ATOM   8925  N  N   . LYS I  1 3   ? 96.496  27.598  4.854  1.00 39.56  ? 3    LYS I N   1 
ATOM   8926  C  CA  . LYS I  1 3   ? 96.010  27.778  6.213  1.00 32.28  ? 3    LYS I CA  1 
ATOM   8927  C  C   . LYS I  1 3   ? 96.675  28.997  6.855  1.00 41.17  ? 3    LYS I C   1 
ATOM   8928  O  O   . LYS I  1 3   ? 97.856  29.189  6.584  1.00 38.37  ? 3    LYS I O   1 
ATOM   8929  C  CB  . LYS I  1 3   ? 96.279  26.546  7.061  1.00 34.10  ? 3    LYS I CB  1 
ATOM   8930  C  CG  . LYS I  1 3   ? 95.580  25.275  6.621  1.00 43.66  ? 3    LYS I CG  1 
ATOM   8931  C  CD  . LYS I  1 3   ? 96.020  24.080  7.460  1.00 53.17  ? 3    LYS I CD  1 
ATOM   8932  C  CE  . LYS I  1 3   ? 94.985  22.963  7.389  1.00 70.69  ? 3    LYS I CE  1 
ATOM   8933  N  NZ  . LYS I  1 3   ? 95.504  21.668  7.913  1.00 81.95  ? 3    LYS I NZ  1 
ATOM   8934  N  N   . ALA I  1 4   ? 95.934  29.760  7.650  1.00 29.52  ? 4    ALA I N   1 
ATOM   8935  C  CA  . ALA I  1 4   ? 96.446  30.883  8.414  1.00 25.34  ? 4    ALA I CA  1 
ATOM   8936  C  C   . ALA I  1 4   ? 95.849  30.809  9.818  1.00 36.23  ? 4    ALA I C   1 
ATOM   8937  O  O   . ALA I  1 4   ? 94.934  30.035  10.119 1.00 33.41  ? 4    ALA I O   1 
ATOM   8938  C  CB  . ALA I  1 4   ? 96.155  32.237  7.788  1.00 26.11  ? 4    ALA I CB  1 
ATOM   8939  N  N   . VAL I  1 5   ? 96.393  31.629  10.711 1.00 25.87  ? 5    VAL I N   1 
ATOM   8940  C  CA  . VAL I  1 5   ? 95.905  31.601  12.088 1.00 25.05  ? 5    VAL I CA  1 
ATOM   8941  C  C   . VAL I  1 5   ? 96.193  32.967  12.688 1.00 29.28  ? 5    VAL I C   1 
ATOM   8942  O  O   . VAL I  1 5   ? 97.083  33.670  12.212 1.00 30.85  ? 5    VAL I O   1 
ATOM   8943  C  CB  . VAL I  1 5   ? 96.539  30.499  12.940 1.00 34.86  ? 5    VAL I CB  1 
ATOM   8944  C  CG1 . VAL I  1 5   ? 98.036  30.753  13.130 1.00 34.02  ? 5    VAL I CG1 1 
ATOM   8945  C  CG2 . VAL I  1 5   ? 95.846  30.391  14.294 1.00 32.35  ? 5    VAL I CG2 1 
ATOM   8946  N  N   . CYS I  1 6   ? 95.423  33.300  13.702 1.00 26.15  ? 6    CYS I N   1 
ATOM   8947  C  CA  . CYS I  1 6   ? 95.514  34.591  14.346 1.00 24.85  ? 6    CYS I CA  1 
ATOM   8948  C  C   . CYS I  1 6   ? 95.169  34.468  15.828 1.00 25.64  ? 6    CYS I C   1 
ATOM   8949  O  O   . CYS I  1 6   ? 94.102  33.948  16.175 1.00 26.85  ? 6    CYS I O   1 
ATOM   8950  C  CB  . CYS I  1 6   ? 94.555  35.584  13.672 1.00 30.81  ? 6    CYS I CB  1 
ATOM   8951  S  SG  . CYS I  1 6   ? 94.673  37.267  14.339 1.00 33.77  ? 6    CYS I SG  1 
ATOM   8952  N  N   . VAL I  1 7   ? 96.054  34.969  16.677 1.00 22.46  ? 7    VAL I N   1 
ATOM   8953  C  CA  . VAL I  1 7   ? 95.847  35.047  18.121 1.00 23.76  ? 7    VAL I CA  1 
ATOM   8954  C  C   . VAL I  1 7   ? 95.463  36.462  18.512 1.00 27.50  ? 7    VAL I C   1 
ATOM   8955  O  O   . VAL I  1 7   ? 96.237  37.400  18.344 1.00 29.12  ? 7    VAL I O   1 
ATOM   8956  C  CB  . VAL I  1 7   ? 97.095  34.651  18.927 1.00 27.13  ? 7    VAL I CB  1 
ATOM   8957  C  CG1 . VAL I  1 7   ? 96.916  34.820  20.433 1.00 26.15  ? 7    VAL I CG1 1 
ATOM   8958  C  CG2 . VAL I  1 7   ? 97.460  33.211  18.617 1.00 27.32  ? 7    VAL I CG2 1 
ATOM   8959  N  N   . LEU I  1 8   ? 94.260  36.631  19.043 1.00 25.48  ? 8    LEU I N   1 
ATOM   8960  C  CA  . LEU I  1 8   ? 93.764  37.965  19.328 1.00 26.19  ? 8    LEU I CA  1 
ATOM   8961  C  C   . LEU I  1 8   ? 94.032  38.349  20.773 1.00 26.02  ? 8    LEU I C   1 
ATOM   8962  O  O   . LEU I  1 8   ? 93.762  37.565  21.686 1.00 27.25  ? 8    LEU I O   1 
ATOM   8963  C  CB  . LEU I  1 8   ? 92.252  38.051  19.120 1.00 25.14  ? 8    LEU I CB  1 
ATOM   8964  C  CG  . LEU I  1 8   ? 91.741  37.754  17.714 1.00 31.56  ? 8    LEU I CG  1 
ATOM   8965  C  CD1 . LEU I  1 8   ? 90.226  37.565  17.714 1.00 43.06  ? 8    LEU I CD1 1 
ATOM   8966  C  CD2 . LEU I  1 8   ? 92.116  38.885  16.781 1.00 28.81  ? 8    LEU I CD2 1 
ATOM   8967  N  N   . LYS I  1 9   ? 94.549  39.557  20.962 1.00 26.98  ? 9    LYS I N   1 
ATOM   8968  C  CA  . LYS I  1 9   ? 94.793  40.029  22.327 1.00 27.71  ? 9    LYS I CA  1 
ATOM   8969  C  C   . LYS I  1 9   ? 94.793  41.555  22.306 1.00 26.29  ? 9    LYS I C   1 
ATOM   8970  O  O   . LYS I  1 9   ? 94.948  42.142  21.237 1.00 30.25  ? 9    LYS I O   1 
ATOM   8971  C  CB  . LYS I  1 9   ? 96.094  39.425  22.879 1.00 41.10  ? 9    LYS I CB  1 
ATOM   8972  C  CG  . LYS I  1 9   ? 95.851  38.053  23.501 1.00 54.49  ? 9    LYS I CG  1 
ATOM   8973  C  CD  . LYS I  1 9   ? 97.023  37.492  24.264 1.00 70.69  ? 9    LYS I CD  1 
ATOM   8974  C  CE  . LYS I  1 9   ? 97.079  35.975  24.135 1.00 74.69  ? 9    LYS I CE  1 
ATOM   8975  N  NZ  . LYS I  1 9   ? 98.106  35.560  23.133 1.00 72.04  ? 9    LYS I NZ  1 
ATOM   8976  N  N   . GLY I  1 10  ? 94.628  42.189  23.451 1.00 27.85  ? 10   GLY I N   1 
ATOM   8977  C  CA  . GLY I  1 10  ? 94.560  43.647  23.543 1.00 28.48  ? 10   GLY I CA  1 
ATOM   8978  C  C   . GLY I  1 10  ? 94.912  44.043  24.968 1.00 34.99  ? 10   GLY I C   1 
ATOM   8979  O  O   . GLY I  1 10  ? 95.589  43.284  25.664 1.00 38.59  ? 10   GLY I O   1 
ATOM   8980  N  N   . ASP I  1 11  ? 94.467  45.211  25.422 1.00 49.38  ? 11   ASP I N   1 
ATOM   8981  C  CA  . ASP I  1 11  ? 94.880  45.660  26.754 1.00 63.41  ? 11   ASP I CA  1 
ATOM   8982  C  C   . ASP I  1 11  ? 94.010  45.066  27.852 1.00 56.67  ? 11   ASP I C   1 
ATOM   8983  O  O   . ASP I  1 11  ? 94.467  44.901  28.985 1.00 65.64  ? 11   ASP I O   1 
ATOM   8984  C  CB  . ASP I  1 11  ? 94.866  47.189  26.811 1.00 73.62  ? 11   ASP I CB  1 
ATOM   8985  C  CG  . ASP I  1 11  ? 95.588  47.821  25.637 1.00 83.53  ? 11   ASP I CG  1 
ATOM   8986  O  OD1 . ASP I  1 11  ? 96.680  47.334  25.270 1.00 87.43  ? 11   ASP I OD1 1 
ATOM   8987  O  OD2 . ASP I  1 11  ? 95.074  48.810  25.070 1.00 103.26 ? 11   ASP I OD2 1 
ATOM   8988  N  N   . GLY I  1 12  ? 92.766  44.752  27.510 1.00 47.84  ? 12   GLY I N   1 
ATOM   8989  C  CA  . GLY I  1 12  ? 91.807  44.222  28.461 1.00 35.79  ? 12   GLY I CA  1 
ATOM   8990  C  C   . GLY I  1 12  ? 91.682  42.713  28.411 1.00 40.96  ? 12   GLY I C   1 
ATOM   8991  O  O   . GLY I  1 12  ? 92.643  42.010  28.077 1.00 42.31  ? 12   GLY I O   1 
ATOM   8992  N  N   . PRO I  1 13  ? 90.513  42.176  28.739 1.00 36.23  ? 13   PRO I N   1 
ATOM   8993  C  CA  . PRO I  1 13  ? 90.356  40.735  28.930 1.00 35.41  ? 13   PRO I CA  1 
ATOM   8994  C  C   . PRO I  1 13  ? 90.029  39.994  27.646 1.00 30.62  ? 13   PRO I C   1 
ATOM   8995  O  O   . PRO I  1 13  ? 89.885  38.768  27.669 1.00 33.39  ? 13   PRO I O   1 
ATOM   8996  C  CB  . PRO I  1 13  ? 89.148  40.669  29.876 1.00 36.03  ? 13   PRO I CB  1 
ATOM   8997  C  CG  . PRO I  1 13  ? 88.311  41.833  29.467 1.00 43.64  ? 13   PRO I CG  1 
ATOM   8998  C  CD  . PRO I  1 13  ? 89.244  42.894  28.950 1.00 45.99  ? 13   PRO I CD  1 
ATOM   8999  N  N   . VAL I  1 14  ? 89.909  40.735  26.546 1.00 30.22  ? 14   VAL I N   1 
ATOM   9000  C  CA  . VAL I  1 14  ? 89.434  40.053  25.333 1.00 33.02  ? 14   VAL I CA  1 
ATOM   9001  C  C   . VAL I  1 14  ? 90.555  39.285  24.647 1.00 42.90  ? 14   VAL I C   1 
ATOM   9002  O  O   . VAL I  1 14  ? 91.666  39.740  24.391 1.00 30.39  ? 14   VAL I O   1 
ATOM   9003  C  CB  . VAL I  1 14  ? 88.769  41.036  24.357 1.00 28.37  ? 14   VAL I CB  1 
ATOM   9004  C  CG1 . VAL I  1 14  ? 88.483  40.339  23.032 1.00 29.20  ? 14   VAL I CG1 1 
ATOM   9005  C  CG2 . VAL I  1 14  ? 87.464  41.596  24.909 1.00 25.52  ? 14   VAL I CG2 1 
ATOM   9006  N  N   . GLN I  1 15  ? 90.288  38.021  24.292 1.00 31.58  ? 15   GLN I N   1 
ATOM   9007  C  CA  . GLN I  1 15  ? 91.313  37.250  23.609 1.00 32.44  ? 15   GLN I CA  1 
ATOM   9008  C  C   . GLN I  1 15  ? 90.722  36.008  22.964 1.00 29.50  ? 15   GLN I C   1 
ATOM   9009  O  O   . GLN I  1 15  ? 89.683  35.493  23.365 1.00 26.88  ? 15   GLN I O   1 
ATOM   9010  C  CB  . GLN I  1 15  ? 92.399  36.808  24.603 1.00 37.15  ? 15   GLN I CB  1 
ATOM   9011  C  CG  . GLN I  1 15  ? 91.857  35.720  25.525 1.00 38.31  ? 15   GLN I CG  1 
ATOM   9012  C  CD  . GLN I  1 15  ? 92.818  35.405  26.656 1.00 48.04  ? 15   GLN I CD  1 
ATOM   9013  O  OE1 . GLN I  1 15  ? 93.440  34.343  26.628 1.00 66.18  ? 15   GLN I OE1 1 
ATOM   9014  N  NE2 . GLN I  1 15  ? 92.934  36.306  27.614 1.00 45.80  ? 15   GLN I NE2 1 
ATOM   9015  N  N   . GLY I  1 16  ? 91.423  35.510  21.945 1.00 29.26  ? 16   GLY I N   1 
ATOM   9016  C  CA  . GLY I  1 16  ? 90.900  34.341  21.264 1.00 24.38  ? 16   GLY I CA  1 
ATOM   9017  C  C   . GLY I  1 16  ? 91.822  33.928  20.137 1.00 32.66  ? 16   GLY I C   1 
ATOM   9018  O  O   . GLY I  1 16  ? 92.858  34.562  19.931 1.00 32.18  ? 16   GLY I O   1 
ATOM   9019  N  N   . ILE I  1 17  ? 91.416  32.853  19.484 1.00 25.43  ? 17   ILE I N   1 
ATOM   9020  C  CA  . ILE I  1 17  ? 92.142  32.239  18.392 1.00 22.38  ? 17   ILE I CA  1 
ATOM   9021  C  C   . ILE I  1 17  ? 91.210  32.016  17.210 1.00 29.26  ? 17   ILE I C   1 
ATOM   9022  O  O   . ILE I  1 17  ? 90.105  31.464  17.354 1.00 30.75  ? 17   ILE I O   1 
ATOM   9023  C  CB  . ILE I  1 17  ? 92.806  30.910  18.811 1.00 27.80  ? 17   ILE I CB  1 
ATOM   9024  C  CG1 . ILE I  1 17  ? 93.921  31.074  19.855 1.00 35.33  ? 17   ILE I CG1 1 
ATOM   9025  C  CG2 . ILE I  1 17  ? 93.343  30.155  17.611 1.00 28.76  ? 17   ILE I CG2 1 
ATOM   9026  C  CD1 . ILE I  1 17  ? 94.392  29.750  20.446 1.00 40.36  ? 17   ILE I CD1 1 
ATOM   9027  N  N   . ILE I  1 18  ? 91.686  32.479  16.067 1.00 23.65  ? 18   ILE I N   1 
ATOM   9028  C  CA  . ILE I  1 18  ? 90.895  32.380  14.839 1.00 24.90  ? 18   ILE I CA  1 
ATOM   9029  C  C   . ILE I  1 18  ? 91.711  31.686  13.748 1.00 33.74  ? 18   ILE I C   1 
ATOM   9030  O  O   . ILE I  1 18  ? 92.829  32.122  13.456 1.00 27.72  ? 18   ILE I O   1 
ATOM   9031  C  CB  . ILE I  1 18  ? 90.418  33.755  14.348 1.00 24.55  ? 18   ILE I CB  1 
ATOM   9032  C  CG1 . ILE I  1 18  ? 89.499  34.480  15.345 1.00 27.28  ? 18   ILE I CG1 1 
ATOM   9033  C  CG2 . ILE I  1 18  ? 89.768  33.646  12.973 1.00 31.06  ? 18   ILE I CG2 1 
ATOM   9034  C  CD1 . ILE I  1 18  ? 88.192  33.754  15.604 1.00 28.72  ? 18   ILE I CD1 1 
ATOM   9035  N  N   . ASN I  1 19  ? 91.140  30.621  13.195 1.00 23.48  ? 19   ASN I N   1 
ATOM   9036  C  CA  . ASN I  1 19  ? 91.754  29.831  12.142 1.00 23.71  ? 19   ASN I CA  1 
ATOM   9037  C  C   . ASN I  1 19  ? 91.206  30.214  10.779 1.00 29.90  ? 19   ASN I C   1 
ATOM   9038  O  O   . ASN I  1 19  ? 90.045  30.631  10.716 1.00 30.03  ? 19   ASN I O   1 
ATOM   9039  C  CB  . ASN I  1 19  ? 91.478  28.346  12.406 1.00 27.63  ? 19   ASN I CB  1 
ATOM   9040  C  CG  . ASN I  1 19  ? 92.033  27.953  13.764 1.00 42.62  ? 19   ASN I CG  1 
ATOM   9041  O  OD1 . ASN I  1 19  ? 93.246  27.826  13.920 1.00 33.84  ? 19   ASN I OD1 1 
ATOM   9042  N  ND2 . ASN I  1 19  ? 91.128  27.773  14.717 1.00 38.98  ? 19   ASN I ND2 1 
ATOM   9043  N  N   . PHE I  1 20  ? 92.014  30.058  9.740  1.00 25.37  ? 20   PHE I N   1 
ATOM   9044  C  CA  . PHE I  1 20  ? 91.638  30.338  8.361  1.00 28.98  ? 20   PHE I CA  1 
ATOM   9045  C  C   . PHE I  1 20  ? 92.013  29.128  7.502  1.00 39.52  ? 20   PHE I C   1 
ATOM   9046  O  O   . PHE I  1 20  ? 93.077  28.552  7.738  1.00 31.52  ? 20   PHE I O   1 
ATOM   9047  C  CB  . PHE I  1 20  ? 92.298  31.576  7.744  1.00 26.62  ? 20   PHE I CB  1 
ATOM   9048  C  CG  . PHE I  1 20  ? 92.018  32.866  8.486  1.00 28.19  ? 20   PHE I CG  1 
ATOM   9049  C  CD1 . PHE I  1 20  ? 91.071  33.772  8.055  1.00 30.13  ? 20   PHE I CD1 1 
ATOM   9050  C  CD2 . PHE I  1 20  ? 92.721  33.167  9.648  1.00 32.69  ? 20   PHE I CD2 1 
ATOM   9051  C  CE1 . PHE I  1 20  ? 90.824  34.946  8.749  1.00 27.25  ? 20   PHE I CE1 1 
ATOM   9052  C  CE2 . PHE I  1 20  ? 92.474  34.335  10.341 1.00 27.57  ? 20   PHE I CE2 1 
ATOM   9053  C  CZ  . PHE I  1 20  ? 91.516  35.230  9.904  1.00 29.52  ? 20   PHE I CZ  1 
ATOM   9054  N  N   . GLU I  1 21  ? 91.156  28.775  6.548  1.00 36.95  ? 21   GLU I N   1 
ATOM   9055  C  CA  . GLU I  1 21  ? 91.484  27.675  5.634  1.00 34.19  ? 21   GLU I CA  1 
ATOM   9056  C  C   . GLU I  1 21  ? 90.904  27.961  4.255  1.00 39.60  ? 21   GLU I C   1 
ATOM   9057  O  O   . GLU I  1 21  ? 89.764  28.405  4.127  1.00 31.56  ? 21   GLU I O   1 
ATOM   9058  C  CB  . GLU I  1 21  ? 90.990  26.346  6.205  1.00 39.79  ? 21   GLU I CB  1 
ATOM   9059  C  CG  . GLU I  1 21  ? 91.457  25.115  5.448  1.00 50.19  ? 21   GLU I CG  1 
ATOM   9060  C  CD  . GLU I  1 21  ? 91.228  23.818  6.191  1.00 56.92  ? 21   GLU I CD  1 
ATOM   9061  O  OE1 . GLU I  1 21  ? 92.191  23.274  6.771  1.00 75.82  ? 21   GLU I OE1 1 
ATOM   9062  O  OE2 . GLU I  1 21  ? 90.080  23.326  6.209  1.00 74.65  ? 21   GLU I OE2 1 
ATOM   9063  N  N   . GLN I  1 22  ? 91.700  27.713  3.223  1.00 32.48  ? 22   GLN I N   1 
ATOM   9064  C  CA  . GLN I  1 22  ? 91.319  27.917  1.829  1.00 35.95  ? 22   GLN I CA  1 
ATOM   9065  C  C   . GLN I  1 22  ? 91.822  26.767  0.954  1.00 48.61  ? 22   GLN I C   1 
ATOM   9066  O  O   . GLN I  1 22  ? 93.001  26.702  0.591  1.00 51.26  ? 22   GLN I O   1 
ATOM   9067  C  CB  . GLN I  1 22  ? 91.862  29.247  1.304  1.00 33.87  ? 22   GLN I CB  1 
ATOM   9068  C  CG  . GLN I  1 22  ? 91.281  29.686  -0.028 1.00 32.43  ? 22   GLN I CG  1 
ATOM   9069  C  CD  . GLN I  1 22  ? 91.908  30.968  -0.529 1.00 38.80  ? 22   GLN I CD  1 
ATOM   9070  O  OE1 . GLN I  1 22  ? 93.077  31.275  -0.286 1.00 50.22  ? 22   GLN I OE1 1 
ATOM   9071  N  NE2 . GLN I  1 22  ? 91.118  31.760  -1.235 1.00 40.29  ? 22   GLN I NE2 1 
ATOM   9072  N  N   . LYS I  1 23  ? 90.927  25.840  0.616  1.00 54.44  ? 23   LYS I N   1 
ATOM   9073  C  CA  . LYS I  1 23  ? 91.302  24.643  -0.131 1.00 60.43  ? 23   LYS I CA  1 
ATOM   9074  C  C   . LYS I  1 23  ? 91.613  24.926  -1.598 1.00 60.93  ? 23   LYS I C   1 
ATOM   9075  O  O   . LYS I  1 23  ? 92.462  24.245  -2.174 1.00 72.97  ? 23   LYS I O   1 
ATOM   9076  C  CB  . LYS I  1 23  ? 90.188  23.589  -0.042 1.00 59.77  ? 23   LYS I CB  1 
ATOM   9077  C  CG  . LYS I  1 23  ? 89.724  23.332  1.381  1.00 56.84  ? 23   LYS I CG  1 
ATOM   9078  C  CD  . LYS I  1 23  ? 90.561  22.284  2.086  1.00 58.70  ? 23   LYS I CD  1 
ATOM   9079  C  CE  . LYS I  1 23  ? 90.072  22.043  3.507  1.00 63.50  ? 23   LYS I CE  1 
ATOM   9080  N  NZ  . LYS I  1 23  ? 89.766  20.615  3.786  1.00 81.43  ? 23   LYS I NZ  1 
ATOM   9081  N  N   . GLU I  1 24  ? 90.930  25.899  -2.167 1.00 69.95  ? 24   GLU I N   1 
ATOM   9082  C  CA  . GLU I  1 24  ? 91.034  26.332  -3.543 1.00 81.96  ? 24   GLU I CA  1 
ATOM   9083  C  C   . GLU I  1 24  ? 91.783  27.669  -3.626 1.00 83.19  ? 24   GLU I C   1 
ATOM   9084  O  O   . GLU I  1 24  ? 91.433  28.564  -2.852 1.00 98.58  ? 24   GLU I O   1 
ATOM   9085  C  CB  . GLU I  1 24  ? 89.662  26.519  -4.182 1.00 98.77  ? 24   GLU I CB  1 
ATOM   9086  C  CG  . GLU I  1 24  ? 88.876  25.271  -4.548 1.00 105.78 ? 24   GLU I CG  1 
ATOM   9087  C  CD  . GLU I  1 24  ? 87.624  25.591  -5.347 1.00 107.46 ? 24   GLU I CD  1 
ATOM   9088  O  OE1 . GLU I  1 24  ? 86.657  26.133  -4.765 1.00 89.13  ? 24   GLU I OE1 1 
ATOM   9089  O  OE2 . GLU I  1 24  ? 87.608  25.301  -6.565 1.00 117.13 ? 24   GLU I OE2 1 
ATOM   9090  N  N   . SER I  1 25  ? 92.737  27.731  -4.531 1.00 83.43  ? 25   SER I N   1 
ATOM   9091  C  CA  . SER I  1 25  ? 93.594  28.858  -4.842 1.00 84.40  ? 25   SER I CA  1 
ATOM   9092  C  C   . SER I  1 25  ? 92.887  30.185  -4.596 1.00 78.56  ? 25   SER I C   1 
ATOM   9093  O  O   . SER I  1 25  ? 93.306  30.983  -3.756 1.00 92.50  ? 25   SER I O   1 
ATOM   9094  C  CB  . SER I  1 25  ? 94.060  28.795  -6.304 1.00 88.39  ? 25   SER I CB  1 
ATOM   9095  O  OG  . SER I  1 25  ? 95.015  29.820  -6.549 1.00 100.15 ? 25   SER I OG  1 
ATOM   9096  N  N   . ASN I  1 26  ? 91.790  30.399  -5.323 1.00 68.26  ? 26   ASN I N   1 
ATOM   9097  C  CA  . ASN I  1 26  ? 90.986  31.584  -4.991 1.00 74.79  ? 26   ASN I CA  1 
ATOM   9098  C  C   . ASN I  1 26  ? 89.575  31.155  -4.609 1.00 64.70  ? 26   ASN I C   1 
ATOM   9099  O  O   . ASN I  1 26  ? 88.563  31.752  -4.960 1.00 54.58  ? 26   ASN I O   1 
ATOM   9100  C  CB  . ASN I  1 26  ? 90.993  32.606  -6.126 1.00 85.64  ? 26   ASN I CB  1 
ATOM   9101  C  CG  . ASN I  1 26  ? 92.085  33.644  -5.925 1.00 97.21  ? 26   ASN I CG  1 
ATOM   9102  O  OD1 . ASN I  1 26  ? 92.148  34.295  -4.880 1.00 107.37 ? 26   ASN I OD1 1 
ATOM   9103  N  ND2 . ASN I  1 26  ? 92.955  33.795  -6.919 1.00 108.89 ? 26   ASN I ND2 1 
ATOM   9104  N  N   . GLY I  1 27  ? 89.519  30.063  -3.841 1.00 54.28  ? 27   GLY I N   1 
ATOM   9105  C  CA  . GLY I  1 27  ? 88.229  29.603  -3.362 1.00 55.98  ? 27   GLY I CA  1 
ATOM   9106  C  C   . GLY I  1 27  ? 87.804  30.372  -2.123 1.00 56.88  ? 27   GLY I C   1 
ATOM   9107  O  O   . GLY I  1 27  ? 88.448  31.338  -1.709 1.00 47.01  ? 27   GLY I O   1 
ATOM   9108  N  N   . PRO I  1 28  ? 86.710  29.910  -1.530 1.00 56.72  ? 28   PRO I N   1 
ATOM   9109  C  CA  . PRO I  1 28  ? 86.211  30.515  -0.295 1.00 45.69  ? 28   PRO I CA  1 
ATOM   9110  C  C   . PRO I  1 28  ? 87.141  30.187  0.870  1.00 33.14  ? 28   PRO I C   1 
ATOM   9111  O  O   . PRO I  1 28  ? 87.827  29.161  0.884  1.00 40.09  ? 28   PRO I O   1 
ATOM   9112  C  CB  . PRO I  1 28  ? 84.852  29.829  -0.085 1.00 50.36  ? 28   PRO I CB  1 
ATOM   9113  C  CG  . PRO I  1 28  ? 85.043  28.491  -0.730 1.00 57.66  ? 28   PRO I CG  1 
ATOM   9114  C  CD  . PRO I  1 28  ? 85.871  28.777  -1.963 1.00 61.87  ? 28   PRO I CD  1 
ATOM   9115  N  N   . VAL I  1 29  ? 87.142  31.074  1.854  1.00 35.65  ? 29   VAL I N   1 
ATOM   9116  C  CA  . VAL I  1 29  ? 87.899  30.871  3.076  1.00 36.22  ? 29   VAL I CA  1 
ATOM   9117  C  C   . VAL I  1 29  ? 86.941  30.605  4.236  1.00 32.27  ? 29   VAL I C   1 
ATOM   9118  O  O   . VAL I  1 29  ? 86.028  31.393  4.464  1.00 41.02  ? 29   VAL I O   1 
ATOM   9119  C  CB  . VAL I  1 29  ? 88.768  32.102  3.401  1.00 36.86  ? 29   VAL I CB  1 
ATOM   9120  C  CG1 . VAL I  1 29  ? 89.577  31.886  4.672  1.00 28.72  ? 29   VAL I CG1 1 
ATOM   9121  C  CG2 . VAL I  1 29  ? 89.657  32.424  2.208  1.00 38.38  ? 29   VAL I CG2 1 
ATOM   9122  N  N   . LYS I  1 30  ? 87.173  29.519  4.937  1.00 31.75  ? 30   LYS I N   1 
ATOM   9123  C  CA  . LYS I  1 30  ? 86.531  29.185  6.199  1.00 36.86  ? 30   LYS I CA  1 
ATOM   9124  C  C   . LYS I  1 30  ? 87.313  29.882  7.317  1.00 32.92  ? 30   LYS I C   1 
ATOM   9125  O  O   . LYS I  1 30  ? 88.540  29.792  7.374  1.00 34.30  ? 30   LYS I O   1 
ATOM   9126  C  CB  . LYS I  1 30  ? 86.461  27.677  6.403  1.00 43.93  ? 30   LYS I CB  1 
ATOM   9127  C  CG  . LYS I  1 30  ? 85.667  27.219  7.610  1.00 53.10  ? 30   LYS I CG  1 
ATOM   9128  C  CD  . LYS I  1 30  ? 85.938  25.760  7.953  1.00 62.44  ? 30   LYS I CD  1 
ATOM   9129  C  CE  . LYS I  1 30  ? 85.142  25.318  9.174  1.00 73.31  ? 30   LYS I CE  1 
ATOM   9130  N  NZ  . LYS I  1 30  ? 85.983  24.660  10.212 1.00 89.54  ? 30   LYS I NZ  1 
ATOM   9131  N  N   . VAL I  1 31  ? 86.570  30.585  8.148  1.00 27.26  ? 31   VAL I N   1 
ATOM   9132  C  CA  . VAL I  1 31  ? 87.096  31.332  9.283  1.00 24.64  ? 31   VAL I CA  1 
ATOM   9133  C  C   . VAL I  1 31  ? 86.407  30.850  10.550 1.00 36.28  ? 31   VAL I C   1 
ATOM   9134  O  O   . VAL I  1 31  ? 85.173  30.951  10.591 1.00 45.43  ? 31   VAL I O   1 
ATOM   9135  C  CB  . VAL I  1 31  ? 86.855  32.833  9.138  1.00 27.26  ? 31   VAL I CB  1 
ATOM   9136  C  CG1 . VAL I  1 31  ? 87.479  33.586  10.317 1.00 30.82  ? 31   VAL I CG1 1 
ATOM   9137  C  CG2 . VAL I  1 31  ? 87.422  33.369  7.837  1.00 31.45  ? 31   VAL I CG2 1 
ATOM   9138  N  N   . TRP I  1 32  ? 87.161  30.334  11.514 1.00 29.85  ? 32   TRP I N   1 
ATOM   9139  C  CA  . TRP I  1 32  ? 86.491  29.791  12.695 1.00 26.95  ? 32   TRP I CA  1 
ATOM   9140  C  C   . TRP I  1 32  ? 87.418  29.755  13.896 1.00 34.19  ? 32   TRP I C   1 
ATOM   9141  O  O   . TRP I  1 32  ? 88.642  29.737  13.803 1.00 31.45  ? 32   TRP I O   1 
ATOM   9142  C  CB  . TRP I  1 32  ? 85.978  28.379  12.401 1.00 30.05  ? 32   TRP I CB  1 
ATOM   9143  C  CG  . TRP I  1 32  ? 87.026  27.314  12.476 1.00 40.12  ? 32   TRP I CG  1 
ATOM   9144  C  CD1 . TRP I  1 32  ? 87.258  26.451  13.512 1.00 37.24  ? 32   TRP I CD1 1 
ATOM   9145  C  CD2 . TRP I  1 32  ? 87.992  26.997  11.462 1.00 38.14  ? 32   TRP I CD2 1 
ATOM   9146  N  NE1 . TRP I  1 32  ? 88.310  25.620  13.197 1.00 43.99  ? 32   TRP I NE1 1 
ATOM   9147  C  CE2 . TRP I  1 32  ? 88.777  25.933  11.949 1.00 36.77  ? 32   TRP I CE2 1 
ATOM   9148  C  CE3 . TRP I  1 32  ? 88.257  27.523  10.193 1.00 40.55  ? 32   TRP I CE3 1 
ATOM   9149  C  CZ2 . TRP I  1 32  ? 89.820  25.365  11.219 1.00 40.62  ? 32   TRP I CZ2 1 
ATOM   9150  C  CZ3 . TRP I  1 32  ? 89.297  26.951  9.476  1.00 41.24  ? 32   TRP I CZ3 1 
ATOM   9151  C  CH2 . TRP I  1 32  ? 90.059  25.895  9.981  1.00 42.86  ? 32   TRP I CH2 1 
ATOM   9152  N  N   . GLY I  1 33  ? 86.788  29.753  15.062 1.00 25.22  ? 33   GLY I N   1 
ATOM   9153  C  CA  . GLY I  1 33  ? 87.542  29.771  16.303 1.00 25.94  ? 33   GLY I CA  1 
ATOM   9154  C  C   . GLY I  1 33  ? 86.667  30.336  17.407 1.00 30.43  ? 33   GLY I C   1 
ATOM   9155  O  O   . GLY I  1 33  ? 85.440  30.280  17.311 1.00 28.16  ? 33   GLY I O   1 
ATOM   9156  N  N   . SER I  1 34  ? 87.294  30.876  18.437 1.00 29.32  ? 34   SER I N   1 
ATOM   9157  C  CA  . SER I  1 34  ? 86.567  31.341  19.615 1.00 34.37  ? 34   SER I CA  1 
ATOM   9158  C  C   . SER I  1 34  ? 87.174  32.643  20.134 1.00 35.34  ? 34   SER I C   1 
ATOM   9159  O  O   . SER I  1 34  ? 88.396  32.818  20.053 1.00 27.52  ? 34   SER I O   1 
ATOM   9160  C  CB  . SER I  1 34  ? 86.603  30.246  20.690 1.00 26.93  ? 34   SER I CB  1 
ATOM   9161  O  OG  . SER I  1 34  ? 85.674  30.524  21.717 1.00 42.36  ? 34   SER I OG  1 
ATOM   9162  N  N   . ILE I  1 35  ? 86.334  33.532  20.653 1.00 25.26  ? 35   ILE I N   1 
ATOM   9163  C  CA  . ILE I  1 35  ? 86.824  34.764  21.271 1.00 25.90  ? 35   ILE I CA  1 
ATOM   9164  C  C   . ILE I  1 35  ? 86.156  34.847  22.632 1.00 31.27  ? 35   ILE I C   1 
ATOM   9165  O  O   . ILE I  1 35  ? 84.936  34.717  22.737 1.00 33.52  ? 35   ILE I O   1 
ATOM   9166  C  CB  . ILE I  1 35  ? 86.557  36.036  20.457 1.00 26.55  ? 35   ILE I CB  1 
ATOM   9167  C  CG1 . ILE I  1 35  ? 87.044  35.946  18.995 1.00 33.79  ? 35   ILE I CG1 1 
ATOM   9168  C  CG2 . ILE I  1 35  ? 87.176  37.267  21.111 1.00 24.79  ? 35   ILE I CG2 1 
ATOM   9169  C  CD1 . ILE I  1 35  ? 86.592  37.111  18.140 1.00 32.91  ? 35   ILE I CD1 1 
ATOM   9170  N  N   . LYS I  1 36  ? 86.937  35.055  23.681 1.00 25.00  ? 36   LYS I N   1 
ATOM   9171  C  CA  . LYS I  1 36  ? 86.294  35.213  24.987 1.00 25.62  ? 36   LYS I CA  1 
ATOM   9172  C  C   . LYS I  1 36  ? 86.605  36.581  25.593 1.00 28.76  ? 36   LYS I C   1 
ATOM   9173  O  O   . LYS I  1 36  ? 87.374  37.403  25.080 1.00 27.79  ? 36   LYS I O   1 
ATOM   9174  C  CB  . LYS I  1 36  ? 86.702  34.046  25.883 1.00 33.77  ? 36   LYS I CB  1 
ATOM   9175  C  CG  . LYS I  1 36  ? 88.171  34.005  26.259 1.00 34.78  ? 36   LYS I CG  1 
ATOM   9176  C  CD  . LYS I  1 36  ? 88.448  32.856  27.228 1.00 39.68  ? 36   LYS I CD  1 
ATOM   9177  C  CE  . LYS I  1 36  ? 89.860  32.999  27.792 1.00 52.14  ? 36   LYS I CE  1 
ATOM   9178  N  NZ  . LYS I  1 36  ? 90.393  31.721  28.340 1.00 60.61  ? 36   LYS I NZ  1 
ATOM   9179  N  N   . GLY I  1 37  ? 85.973  36.853  26.733 1.00 24.92  ? 37   GLY I N   1 
ATOM   9180  C  CA  . GLY I  1 37  ? 86.178  38.110  27.427 1.00 29.20  ? 37   GLY I CA  1 
ATOM   9181  C  C   . GLY I  1 37  ? 85.299  39.238  26.939 1.00 31.85  ? 37   GLY I C   1 
ATOM   9182  O  O   . GLY I  1 37  ? 85.482  40.370  27.401 1.00 28.86  ? 37   GLY I O   1 
ATOM   9183  N  N   . LEU I  1 38  ? 84.368  38.941  26.013 1.00 29.06  ? 38   LEU I N   1 
ATOM   9184  C  CA  . LEU I  1 38  ? 83.579  40.008  25.412 1.00 28.02  ? 38   LEU I CA  1 
ATOM   9185  C  C   . LEU I  1 38  ? 82.314  40.332  26.214 1.00 29.71  ? 38   LEU I C   1 
ATOM   9186  O  O   . LEU I  1 38  ? 81.765  39.473  26.892 1.00 29.36  ? 38   LEU I O   1 
ATOM   9187  C  CB  . LEU I  1 38  ? 83.137  39.657  23.987 1.00 26.18  ? 38   LEU I CB  1 
ATOM   9188  C  CG  . LEU I  1 38  ? 84.231  39.437  22.941 1.00 26.85  ? 38   LEU I CG  1 
ATOM   9189  C  CD1 . LEU I  1 38  ? 83.744  38.485  21.858 1.00 24.47  ? 38   LEU I CD1 1 
ATOM   9190  C  CD2 . LEU I  1 38  ? 84.697  40.752  22.327 1.00 25.56  ? 38   LEU I CD2 1 
ATOM   9191  N  N   . THR I  1 39  ? 81.859  41.580  26.103 1.00 27.44  ? 39   THR I N   1 
ATOM   9192  C  CA  . THR I  1 39  ? 80.521  41.962  26.519 1.00 26.27  ? 39   THR I CA  1 
ATOM   9193  C  C   . THR I  1 39  ? 79.520  41.203  25.631 1.00 27.54  ? 39   THR I C   1 
ATOM   9194  O  O   . THR I  1 39  ? 79.752  41.011  24.424 1.00 25.40  ? 39   THR I O   1 
ATOM   9195  C  CB  . THR I  1 39  ? 80.227  43.463  26.403 1.00 29.86  ? 39   THR I CB  1 
ATOM   9196  O  OG1 . THR I  1 39  ? 80.436  43.938  25.063 1.00 31.05  ? 39   THR I OG1 1 
ATOM   9197  C  CG2 . THR I  1 39  ? 81.179  44.255  27.295 1.00 29.77  ? 39   THR I CG2 1 
ATOM   9198  N  N   . GLU I  1 40  ? 78.414  40.774  26.224 1.00 26.47  ? 40   GLU I N   1 
ATOM   9199  C  CA  . GLU I  1 40  ? 77.472  39.948  25.457 1.00 29.21  ? 40   GLU I CA  1 
ATOM   9200  C  C   . GLU I  1 40  ? 76.924  40.783  24.311 1.00 26.00  ? 40   GLU I C   1 
ATOM   9201  O  O   . GLU I  1 40  ? 76.764  42.005  24.446 1.00 26.19  ? 40   GLU I O   1 
ATOM   9202  C  CB  . GLU I  1 40  ? 76.392  39.387  26.387 1.00 29.30  ? 40   GLU I CB  1 
ATOM   9203  C  CG  . GLU I  1 40  ? 75.331  40.412  26.769 1.00 31.08  ? 40   GLU I CG  1 
ATOM   9204  C  CD  . GLU I  1 40  ? 74.266  39.884  27.708 1.00 36.79  ? 40   GLU I CD  1 
ATOM   9205  O  OE1 . GLU I  1 40  ? 73.451  40.670  28.237 1.00 39.42  ? 40   GLU I OE1 1 
ATOM   9206  O  OE2 . GLU I  1 40  ? 74.172  38.664  27.952 1.00 38.68  ? 40   GLU I OE2 1 
ATOM   9207  N  N   . GLY I  1 41  ? 76.643  40.141  23.168 1.00 30.71  ? 41   GLY I N   1 
ATOM   9208  C  CA  . GLY I  1 41  ? 76.096  40.845  22.015 1.00 26.39  ? 41   GLY I CA  1 
ATOM   9209  C  C   . GLY I  1 41  ? 77.008  40.910  20.809 1.00 30.14  ? 41   GLY I C   1 
ATOM   9210  O  O   . GLY I  1 41  ? 78.000  40.164  20.721 1.00 23.92  ? 41   GLY I O   1 
ATOM   9211  N  N   . LEU I  1 42  ? 76.680  41.801  19.873 1.00 26.11  ? 42   LEU I N   1 
ATOM   9212  C  CA  . LEU I  1 42  ? 77.348  41.901  18.579 1.00 26.26  ? 42   LEU I CA  1 
ATOM   9213  C  C   . LEU I  1 42  ? 78.633  42.730  18.592 1.00 32.73  ? 42   LEU I C   1 
ATOM   9214  O  O   . LEU I  1 42  ? 78.712  43.811  19.180 1.00 26.41  ? 42   LEU I O   1 
ATOM   9215  C  CB  . LEU I  1 42  ? 76.382  42.510  17.552 1.00 21.63  ? 42   LEU I CB  1 
ATOM   9216  C  CG  . LEU I  1 42  ? 75.375  41.540  16.930 1.00 22.67  ? 42   LEU I CG  1 
ATOM   9217  C  CD1 . LEU I  1 42  ? 74.479  40.955  18.019 1.00 26.85  ? 42   LEU I CD1 1 
ATOM   9218  C  CD2 . LEU I  1 42  ? 74.561  42.259  15.864 1.00 29.02  ? 42   LEU I CD2 1 
ATOM   9219  N  N   . HIS I  1 43  ? 79.674  42.236  17.910 1.00 23.35  ? 43   HIS I N   1 
ATOM   9220  C  CA  . HIS I  1 43  ? 80.923  42.985  17.874 1.00 26.09  ? 43   HIS I CA  1 
ATOM   9221  C  C   . HIS I  1 43  ? 81.506  43.017  16.473 1.00 24.18  ? 43   HIS I C   1 
ATOM   9222  O  O   . HIS I  1 43  ? 81.614  41.957  15.856 1.00 26.45  ? 43   HIS I O   1 
ATOM   9223  C  CB  . HIS I  1 43  ? 81.964  42.327  18.796 1.00 26.97  ? 43   HIS I CB  1 
ATOM   9224  C  CG  . HIS I  1 43  ? 81.591  42.436  20.245 1.00 25.12  ? 43   HIS I CG  1 
ATOM   9225  N  ND1 . HIS I  1 43  ? 82.000  43.486  21.023 1.00 25.31  ? 43   HIS I ND1 1 
ATOM   9226  C  CD2 . HIS I  1 43  ? 80.864  41.629  21.048 1.00 24.83  ? 43   HIS I CD2 1 
ATOM   9227  C  CE1 . HIS I  1 43  ? 81.540  43.325  22.250 1.00 26.97  ? 43   HIS I CE1 1 
ATOM   9228  N  NE2 . HIS I  1 43  ? 80.829  42.202  22.302 1.00 25.28  ? 43   HIS I NE2 1 
ATOM   9229  N  N   . GLY I  1 44  ? 81.907  44.183  15.981 1.00 25.86  ? 44   GLY I N   1 
ATOM   9230  C  CA  . GLY I  1 44  ? 82.484  44.231  14.642 1.00 25.14  ? 44   GLY I CA  1 
ATOM   9231  C  C   . GLY I  1 44  ? 83.751  43.395  14.517 1.00 25.25  ? 44   GLY I C   1 
ATOM   9232  O  O   . GLY I  1 44  ? 84.470  43.216  15.491 1.00 26.31  ? 44   GLY I O   1 
ATOM   9233  N  N   . PHE I  1 45  ? 84.013  42.886  13.330 1.00 27.31  ? 45   PHE I N   1 
ATOM   9234  C  CA  . PHE I  1 45  ? 85.076  41.935  13.015 1.00 26.97  ? 45   PHE I CA  1 
ATOM   9235  C  C   . PHE I  1 45  ? 85.605  42.164  11.610 1.00 29.51  ? 45   PHE I C   1 
ATOM   9236  O  O   . PHE I  1 45  ? 84.891  41.864  10.641 1.00 30.88  ? 45   PHE I O   1 
ATOM   9237  C  CB  . PHE I  1 45  ? 84.474  40.545  13.158 1.00 25.10  ? 45   PHE I CB  1 
ATOM   9238  C  CG  . PHE I  1 45  ? 85.362  39.318  13.221 1.00 26.90  ? 45   PHE I CG  1 
ATOM   9239  C  CD1 . PHE I  1 45  ? 86.326  39.185  14.222 1.00 35.11  ? 45   PHE I CD1 1 
ATOM   9240  C  CD2 . PHE I  1 45  ? 85.242  38.305  12.296 1.00 23.31  ? 45   PHE I CD2 1 
ATOM   9241  C  CE1 . PHE I  1 45  ? 87.117  38.048  14.291 1.00 26.92  ? 45   PHE I CE1 1 
ATOM   9242  C  CE2 . PHE I  1 45  ? 85.998  37.143  12.354 1.00 24.86  ? 45   PHE I CE2 1 
ATOM   9243  C  CZ  . PHE I  1 45  ? 86.944  37.038  13.366 1.00 22.47  ? 45   PHE I CZ  1 
ATOM   9244  N  N   . HIS I  1 46  ? 86.823  42.705  11.447 1.00 28.12  ? 46   HIS I N   1 
ATOM   9245  C  CA  . HIS I  1 46  ? 87.351  43.070  10.136 1.00 28.53  ? 46   HIS I CA  1 
ATOM   9246  C  C   . HIS I  1 46  ? 88.841  42.727  10.012 1.00 30.44  ? 46   HIS I C   1 
ATOM   9247  O  O   . HIS I  1 46  ? 89.509  42.647  11.042 1.00 27.32  ? 46   HIS I O   1 
ATOM   9248  C  CB  . HIS I  1 46  ? 87.236  44.589  9.867  1.00 26.78  ? 46   HIS I CB  1 
ATOM   9249  C  CG  . HIS I  1 46  ? 86.040  45.229  10.503 1.00 33.59  ? 46   HIS I CG  1 
ATOM   9250  N  ND1 . HIS I  1 46  ? 86.050  45.925  11.690 1.00 32.03  ? 46   HIS I ND1 1 
ATOM   9251  C  CD2 . HIS I  1 46  ? 84.743  45.212  10.088 1.00 31.67  ? 46   HIS I CD2 1 
ATOM   9252  C  CE1 . HIS I  1 46  ? 84.823  46.338  11.979 1.00 29.88  ? 46   HIS I CE1 1 
ATOM   9253  N  NE2 . HIS I  1 46  ? 84.023  45.907  11.013 1.00 26.30  ? 46   HIS I NE2 1 
ATOM   9254  N  N   . VAL I  1 47  ? 89.328  42.554  8.804  1.00 25.51  ? 47   VAL I N   1 
ATOM   9255  C  CA  . VAL I  1 47  ? 90.763  42.504  8.534  1.00 27.95  ? 47   VAL I CA  1 
ATOM   9256  C  C   . VAL I  1 47  ? 91.209  43.944  8.239  1.00 40.01  ? 47   VAL I C   1 
ATOM   9257  O  O   . VAL I  1 47  ? 90.654  44.587  7.329  1.00 31.51  ? 47   VAL I O   1 
ATOM   9258  C  CB  . VAL I  1 47  ? 91.146  41.608  7.353  1.00 29.73  ? 47   VAL I CB  1 
ATOM   9259  C  CG1 . VAL I  1 47  ? 92.661  41.631  7.139  1.00 30.40  ? 47   VAL I CG1 1 
ATOM   9260  C  CG2 . VAL I  1 47  ? 90.720  40.160  7.514  1.00 31.27  ? 47   VAL I CG2 1 
ATOM   9261  N  N   . HIS I  1 48  ? 92.172  44.456  9.001  1.00 26.91  ? 48   HIS I N   1 
ATOM   9262  C  CA  . HIS I  1 48  ? 92.661  45.818  8.787  1.00 29.79  ? 48   HIS I CA  1 
ATOM   9263  C  C   . HIS I  1 48  ? 93.945  45.782  7.973  1.00 38.07  ? 48   HIS I C   1 
ATOM   9264  O  O   . HIS I  1 48  ? 94.559  44.713  7.868  1.00 35.50  ? 48   HIS I O   1 
ATOM   9265  C  CB  . HIS I  1 48  ? 92.929  46.542  10.104 1.00 32.21  ? 48   HIS I CB  1 
ATOM   9266  C  CG  . HIS I  1 48  ? 91.646  46.947  10.758 1.00 33.66  ? 48   HIS I CG  1 
ATOM   9267  N  ND1 . HIS I  1 48  ? 91.354  48.227  11.138 1.00 32.81  ? 48   HIS I ND1 1 
ATOM   9268  C  CD2 . HIS I  1 48  ? 90.575  46.181  11.085 1.00 31.95  ? 48   HIS I CD2 1 
ATOM   9269  C  CE1 . HIS I  1 48  ? 90.151  48.260  11.687 1.00 32.00  ? 48   HIS I CE1 1 
ATOM   9270  N  NE2 . HIS I  1 48  ? 89.661  47.035  11.661 1.00 35.68  ? 48   HIS I NE2 1 
ATOM   9271  N  N   . GLU I  1 49  ? 94.336  46.924  7.414  1.00 33.07  ? 49   GLU I N   1 
ATOM   9272  C  CA  . GLU I  1 49  ? 95.396  46.918  6.408  1.00 32.85  ? 49   GLU I CA  1 
ATOM   9273  C  C   . GLU I  1 49  ? 96.772  46.434  6.862  1.00 29.66  ? 49   GLU I C   1 
ATOM   9274  O  O   . GLU I  1 49  ? 97.453  45.656  6.177  1.00 33.29  ? 49   GLU I O   1 
ATOM   9275  C  CB  . GLU I  1 49  ? 95.549  48.360  5.878  1.00 36.55  ? 49   GLU I CB  1 
ATOM   9276  C  CG  . GLU I  1 49  ? 96.305  48.370  4.554  1.00 39.93  ? 49   GLU I CG  1 
ATOM   9277  C  CD  . GLU I  1 49  ? 96.263  49.747  3.899  1.00 49.56  ? 49   GLU I CD  1 
ATOM   9278  O  OE1 . GLU I  1 49  ? 96.628  49.806  2.707  1.00 45.51  ? 49   GLU I OE1 1 
ATOM   9279  O  OE2 . GLU I  1 49  ? 95.878  50.718  4.589  1.00 43.09  ? 49   GLU I OE2 1 
ATOM   9280  N  N   . PHE I  1 50  ? 97.234  46.899  8.011  1.00 37.91  ? 50   PHE I N   1 
ATOM   9281  C  CA  . PHE I  1 50  ? 98.613  46.622  8.391  1.00 32.46  ? 50   PHE I CA  1 
ATOM   9282  C  C   . PHE I  1 50  ? 98.706  45.597  9.501  1.00 30.29  ? 50   PHE I C   1 
ATOM   9283  O  O   . PHE I  1 50  ? 97.931  45.664  10.458 1.00 30.60  ? 50   PHE I O   1 
ATOM   9284  C  CB  . PHE I  1 50  ? 99.300  47.906  8.892  1.00 29.96  ? 50   PHE I CB  1 
ATOM   9285  C  CG  . PHE I  1 50  ? 99.070  49.056  7.911  1.00 33.46  ? 50   PHE I CG  1 
ATOM   9286  C  CD1 . PHE I  1 50  ? 99.408  48.876  6.582  1.00 38.07  ? 50   PHE I CD1 1 
ATOM   9287  C  CD2 . PHE I  1 50  ? 98.532  50.246  8.335  1.00 36.20  ? 50   PHE I CD2 1 
ATOM   9288  C  CE1 . PHE I  1 50  ? 99.211  49.908  5.681  1.00 43.86  ? 50   PHE I CE1 1 
ATOM   9289  C  CE2 . PHE I  1 50  ? 98.323  51.281  7.443  1.00 39.56  ? 50   PHE I CE2 1 
ATOM   9290  C  CZ  . PHE I  1 50  ? 98.650  51.095  6.114  1.00 41.64  ? 50   PHE I CZ  1 
ATOM   9291  N  N   . GLY I  1 51  ? 99.696  44.722  9.332  1.00 30.33  ? 51   GLY I N   1 
ATOM   9292  C  CA  . GLY I  1 51  ? 100.046 43.812  10.418 1.00 31.49  ? 51   GLY I CA  1 
ATOM   9293  C  C   . GLY I  1 51  ? 101.042 44.514  11.329 1.00 34.43  ? 51   GLY I C   1 
ATOM   9294  O  O   . GLY I  1 51  ? 102.108 43.959  11.587 1.00 31.99  ? 51   GLY I O   1 
ATOM   9295  N  N   . ASP I  1 52  ? 100.691 45.719  11.759 1.00 37.02  ? 52   ASP I N   1 
ATOM   9296  C  CA  . ASP I  1 52  ? 101.485 46.539  12.663 1.00 29.21  ? 52   ASP I CA  1 
ATOM   9297  C  C   . ASP I  1 52  ? 100.757 46.729  13.987 1.00 27.50  ? 52   ASP I C   1 
ATOM   9298  O  O   . ASP I  1 52  ? 99.718  47.377  14.072 1.00 30.91  ? 52   ASP I O   1 
ATOM   9299  C  CB  . ASP I  1 52  ? 101.830 47.899  12.060 1.00 34.82  ? 52   ASP I CB  1 
ATOM   9300  C  CG  . ASP I  1 52  ? 102.722 48.775  12.915 1.00 41.05  ? 52   ASP I CG  1 
ATOM   9301  O  OD1 . ASP I  1 52  ? 103.345 49.715  12.356 1.00 43.73  ? 52   ASP I OD1 1 
ATOM   9302  O  OD2 . ASP I  1 52  ? 102.840 48.582  14.147 1.00 36.65  ? 52   ASP I OD2 1 
ATOM   9303  N  N   . ASN I  1 53  ? 101.355 46.177  15.029 1.00 27.41  ? 53   ASN I N   1 
ATOM   9304  C  CA  . ASN I  1 53  ? 100.870 46.254  16.389 1.00 32.95  ? 53   ASN I CA  1 
ATOM   9305  C  C   . ASN I  1 53  ? 101.728 47.124  17.290 1.00 36.58  ? 53   ASN I C   1 
ATOM   9306  O  O   . ASN I  1 53  ? 101.634 47.063  18.526 1.00 30.59  ? 53   ASN I O   1 
ATOM   9307  C  CB  . ASN I  1 53  ? 100.843 44.823  16.966 1.00 38.52  ? 53   ASN I CB  1 
ATOM   9308  C  CG  . ASN I  1 53  ? 100.058 44.769  18.263 1.00 46.77  ? 53   ASN I CG  1 
ATOM   9309  O  OD1 . ASN I  1 53  ? 100.546 44.304  19.294 1.00 55.88  ? 53   ASN I OD1 1 
ATOM   9310  N  ND2 . ASN I  1 53  ? 98.820  45.261  18.199 1.00 51.71  ? 53   ASN I ND2 1 
ATOM   9311  N  N   . THR I  1 54  ? 102.599 47.972  16.724 1.00 29.98  ? 54   THR I N   1 
ATOM   9312  C  CA  . THR I  1 54  ? 103.527 48.627  17.670 1.00 41.71  ? 54   THR I CA  1 
ATOM   9313  C  C   . THR I  1 54  ? 102.850 49.575  18.644 1.00 46.82  ? 54   THR I C   1 
ATOM   9314  O  O   . THR I  1 54  ? 103.365 49.747  19.754 1.00 43.25  ? 54   THR I O   1 
ATOM   9315  C  CB  . THR I  1 54  ? 104.631 49.382  16.910 1.00 45.68  ? 54   THR I CB  1 
ATOM   9316  O  OG1 . THR I  1 54  ? 104.023 50.284  15.986 1.00 37.57  ? 54   THR I OG1 1 
ATOM   9317  C  CG2 . THR I  1 54  ? 105.450 48.388  16.097 1.00 30.18  ? 54   THR I CG2 1 
ATOM   9318  N  N   . ALA I  1 55  ? 101.721 50.165  18.272 1.00 41.90  ? 55   ALA I N   1 
ATOM   9319  C  CA  . ALA I  1 55  ? 100.948 51.023  19.162 1.00 46.72  ? 55   ALA I CA  1 
ATOM   9320  C  C   . ALA I  1 55  ? 99.641  50.371  19.596 1.00 49.57  ? 55   ALA I C   1 
ATOM   9321  O  O   . ALA I  1 55  ? 98.637  51.026  19.897 1.00 42.62  ? 55   ALA I O   1 
ATOM   9322  C  CB  . ALA I  1 55  ? 100.670 52.354  18.468 1.00 39.74  ? 55   ALA I CB  1 
ATOM   9323  N  N   . GLY I  1 56  ? 99.621  49.039  19.649 1.00 43.95  ? 56   GLY I N   1 
ATOM   9324  C  CA  . GLY I  1 56  ? 98.361  48.349  19.919 1.00 33.84  ? 56   GLY I CA  1 
ATOM   9325  C  C   . GLY I  1 56  ? 97.569  48.209  18.641 1.00 41.17  ? 56   GLY I C   1 
ATOM   9326  O  O   . GLY I  1 56  ? 98.031  48.449  17.517 1.00 33.34  ? 56   GLY I O   1 
ATOM   9327  N  N   . CYS I  1 57  ? 96.292  47.815  18.757 1.00 36.86  ? 57   CYS I N   1 
ATOM   9328  C  CA  . CYS I  1 57  ? 95.512  47.702  17.525 1.00 39.25  ? 57   CYS I CA  1 
ATOM   9329  C  C   . CYS I  1 57  ? 95.401  49.000  16.739 1.00 38.01  ? 57   CYS I C   1 
ATOM   9330  O  O   . CYS I  1 57  ? 95.036  48.953  15.554 1.00 31.09  ? 57   CYS I O   1 
ATOM   9331  C  CB  A CYS I  1 57  ? 94.093  47.228  17.878 0.34 44.88  ? 57   CYS I CB  1 
ATOM   9332  C  CB  B CYS I  1 57  ? 94.106  47.178  17.845 0.66 46.33  ? 57   CYS I CB  1 
ATOM   9333  S  SG  A CYS I  1 57  ? 94.064  45.817  19.007 0.34 52.33  ? 57   CYS I SG  1 
ATOM   9334  S  SG  B CYS I  1 57  ? 94.067  45.909  19.124 0.66 46.86  ? 57   CYS I SG  1 
ATOM   9335  N  N   . THR I  1 58  ? 95.702  50.147  17.339 1.00 40.50  ? 58   THR I N   1 
ATOM   9336  C  CA  . THR I  1 58  ? 95.618  51.416  16.614 1.00 41.65  ? 58   THR I CA  1 
ATOM   9337  C  C   . THR I  1 58  ? 96.530  51.474  15.399 1.00 45.78  ? 58   THR I C   1 
ATOM   9338  O  O   . THR I  1 58  ? 96.162  52.099  14.397 1.00 40.53  ? 58   THR I O   1 
ATOM   9339  C  CB  . THR I  1 58  ? 95.962  52.587  17.557 1.00 49.05  ? 58   THR I CB  1 
ATOM   9340  O  OG1 . THR I  1 58  ? 95.094  52.506  18.696 1.00 47.15  ? 58   THR I OG1 1 
ATOM   9341  C  CG2 . THR I  1 58  ? 95.719  53.912  16.858 1.00 45.48  ? 58   THR I CG2 1 
ATOM   9342  N  N   . SER I  1 59  ? 97.702  50.834  15.469 1.00 31.22  ? 59   SER I N   1 
ATOM   9343  C  CA  . SER I  1 59  ? 98.619  50.846  14.330 1.00 30.73  ? 59   SER I CA  1 
ATOM   9344  C  C   . SER I  1 59  ? 98.195  49.975  13.165 1.00 32.48  ? 59   SER I C   1 
ATOM   9345  O  O   . SER I  1 59  ? 98.843  50.020  12.115 1.00 32.96  ? 59   SER I O   1 
ATOM   9346  C  CB  . SER I  1 59  ? 100.014 50.388  14.802 1.00 37.91  ? 59   SER I CB  1 
ATOM   9347  O  OG  . SER I  1 59  ? 100.172 50.644  16.185 1.00 45.33  ? 59   SER I OG  1 
ATOM   9348  N  N   . ALA I  1 60  ? 97.132  49.172  13.302 1.00 32.20  ? 60   ALA I N   1 
ATOM   9349  C  CA  . ALA I  1 60  ? 96.670  48.338  12.206 1.00 37.55  ? 60   ALA I CA  1 
ATOM   9350  C  C   . ALA I  1 60  ? 96.019  49.149  11.090 1.00 33.96  ? 60   ALA I C   1 
ATOM   9351  O  O   . ALA I  1 60  ? 95.747  48.597  10.016 1.00 32.61  ? 60   ALA I O   1 
ATOM   9352  C  CB  . ALA I  1 60  ? 95.677  47.287  12.689 1.00 39.84  ? 60   ALA I CB  1 
ATOM   9353  N  N   . GLY I  1 61  ? 95.788  50.444  11.321 1.00 37.08  ? 61   GLY I N   1 
ATOM   9354  C  CA  . GLY I  1 61  ? 95.300  51.235  10.189 1.00 33.72  ? 61   GLY I CA  1 
ATOM   9355  C  C   . GLY I  1 61  ? 93.809  51.027  9.976  1.00 36.58  ? 61   GLY I C   1 
ATOM   9356  O  O   . GLY I  1 61  ? 93.165  50.600  10.933 1.00 33.68  ? 61   GLY I O   1 
ATOM   9357  N  N   . PRO I  1 62  ? 93.296  51.317  8.792  1.00 41.38  ? 62   PRO I N   1 
ATOM   9358  C  CA  . PRO I  1 62  ? 91.883  51.072  8.486  1.00 40.98  ? 62   PRO I CA  1 
ATOM   9359  C  C   . PRO I  1 62  ? 91.611  49.686  7.937  1.00 37.74  ? 62   PRO I C   1 
ATOM   9360  O  O   . PRO I  1 62  ? 92.448  48.800  7.790  1.00 37.25  ? 62   PRO I O   1 
ATOM   9361  C  CB  . PRO I  1 62  ? 91.625  52.076  7.344  1.00 33.09  ? 62   PRO I CB  1 
ATOM   9362  C  CG  . PRO I  1 62  ? 92.907  51.874  6.563  1.00 42.40  ? 62   PRO I CG  1 
ATOM   9363  C  CD  . PRO I  1 62  ? 93.978  51.920  7.628  1.00 35.63  ? 62   PRO I CD  1 
ATOM   9364  N  N   . HIS I  1 63  ? 90.331  49.498  7.605  1.00 31.76  ? 63   HIS I N   1 
ATOM   9365  C  CA  . HIS I  1 63  ? 89.879  48.250  7.032  1.00 32.92  ? 63   HIS I CA  1 
ATOM   9366  C  C   . HIS I  1 63  ? 90.636  47.998  5.736  1.00 35.28  ? 63   HIS I C   1 
ATOM   9367  O  O   . HIS I  1 63  ? 90.899  48.914  4.962  1.00 37.31  ? 63   HIS I O   1 
ATOM   9368  C  CB  . HIS I  1 63  ? 88.368  48.270  6.764  1.00 32.58  ? 63   HIS I CB  1 
ATOM   9369  C  CG  . HIS I  1 63  ? 87.531  48.470  7.987  1.00 36.19  ? 63   HIS I CG  1 
ATOM   9370  N  ND1 . HIS I  1 63  ? 86.154  48.332  7.983  1.00 32.23  ? 63   HIS I ND1 1 
ATOM   9371  C  CD2 . HIS I  1 63  ? 87.875  48.797  9.262  1.00 33.03  ? 63   HIS I CD2 1 
ATOM   9372  C  CE1 . HIS I  1 63  ? 85.702  48.570  9.200  1.00 33.46  ? 63   HIS I CE1 1 
ATOM   9373  N  NE2 . HIS I  1 63  ? 86.722  48.855  10.001 1.00 34.47  ? 63   HIS I NE2 1 
ATOM   9374  N  N   . PHE I  1 64  ? 90.968  46.737  5.514  1.00 33.21  ? 64   PHE I N   1 
ATOM   9375  C  CA  . PHE I  1 64  ? 91.694  46.376  4.301  1.00 39.19  ? 64   PHE I CA  1 
ATOM   9376  C  C   . PHE I  1 64  ? 90.794  46.519  3.080  1.00 48.93  ? 64   PHE I C   1 
ATOM   9377  O  O   . PHE I  1 64  ? 89.728  45.899  2.971  1.00 36.86  ? 64   PHE I O   1 
ATOM   9378  C  CB  . PHE I  1 64  ? 92.257  44.963  4.472  1.00 32.79  ? 64   PHE I CB  1 
ATOM   9379  C  CG  . PHE I  1 64  ? 92.990  44.454  3.243  1.00 38.10  ? 64   PHE I CG  1 
ATOM   9380  C  CD1 . PHE I  1 64  ? 92.773  43.181  2.763  1.00 32.24  ? 64   PHE I CD1 1 
ATOM   9381  C  CD2 . PHE I  1 64  ? 93.893  45.286  2.587  1.00 41.95  ? 64   PHE I CD2 1 
ATOM   9382  C  CE1 . PHE I  1 64  ? 93.427  42.704  1.639  1.00 42.52  ? 64   PHE I CE1 1 
ATOM   9383  C  CE2 . PHE I  1 64  ? 94.558  44.816  1.471  1.00 39.23  ? 64   PHE I CE2 1 
ATOM   9384  C  CZ  . PHE I  1 64  ? 94.337  43.535  1.000  1.00 40.72  ? 64   PHE I CZ  1 
ATOM   9385  N  N   . ASN I  1 65  ? 91.246  47.361  2.144  1.00 41.83  ? 65   ASN I N   1 
ATOM   9386  C  CA  . ASN I  1 65  ? 90.380  47.799  1.054  1.00 42.44  ? 65   ASN I CA  1 
ATOM   9387  C  C   . ASN I  1 65  ? 91.138  48.089  -0.231 1.00 48.76  ? 65   ASN I C   1 
ATOM   9388  O  O   . ASN I  1 65  ? 91.197  49.223  -0.706 1.00 41.44  ? 65   ASN I O   1 
ATOM   9389  C  CB  . ASN I  1 65  ? 89.630  49.057  1.502  1.00 36.09  ? 65   ASN I CB  1 
ATOM   9390  C  CG  . ASN I  1 65  ? 88.575  49.495  0.494  1.00 34.02  ? 65   ASN I CG  1 
ATOM   9391  O  OD1 . ASN I  1 65  ? 88.113  48.670  -0.292 1.00 42.43  ? 65   ASN I OD1 1 
ATOM   9392  N  ND2 . ASN I  1 65  ? 88.214  50.766  0.557  1.00 37.63  ? 65   ASN I ND2 1 
ATOM   9393  N  N   . PRO I  1 66  ? 91.706  47.053  -0.827 1.00 46.62  ? 66   PRO I N   1 
ATOM   9394  C  CA  . PRO I  1 66  ? 92.547  47.270  -2.008 1.00 46.25  ? 66   PRO I CA  1 
ATOM   9395  C  C   . PRO I  1 66  ? 91.692  47.818  -3.143 1.00 61.48  ? 66   PRO I C   1 
ATOM   9396  O  O   . PRO I  1 66  ? 92.131  48.647  -3.934 1.00 80.36  ? 66   PRO I O   1 
ATOM   9397  C  CB  . PRO I  1 66  ? 93.038  45.859  -2.342 1.00 43.44  ? 66   PRO I CB  1 
ATOM   9398  C  CG  . PRO I  1 66  ? 91.945  44.980  -1.806 1.00 45.85  ? 66   PRO I CG  1 
ATOM   9399  C  CD  . PRO I  1 66  ? 91.571  45.628  -0.493 1.00 40.70  ? 66   PRO I CD  1 
ATOM   9400  N  N   . LEU I  1 67  ? 90.449  47.340  -3.204 1.00 63.68  ? 67   LEU I N   1 
ATOM   9401  C  CA  . LEU I  1 67  ? 89.543  47.692  -4.292 1.00 53.16  ? 67   LEU I CA  1 
ATOM   9402  C  C   . LEU I  1 67  ? 88.908  49.060  -4.116 1.00 43.17  ? 67   LEU I C   1 
ATOM   9403  O  O   . LEU I  1 67  ? 88.171  49.526  -4.989 1.00 62.87  ? 67   LEU I O   1 
ATOM   9404  C  CB  . LEU I  1 67  ? 88.450  46.622  -4.418 1.00 55.09  ? 67   LEU I CB  1 
ATOM   9405  C  CG  . LEU I  1 67  ? 88.992  45.238  -4.795 1.00 53.00  ? 67   LEU I CG  1 
ATOM   9406  C  CD1 . LEU I  1 67  ? 87.876  44.382  -5.358 1.00 45.86  ? 67   LEU I CD1 1 
ATOM   9407  C  CD2 . LEU I  1 67  ? 90.139  45.377  -5.783 1.00 50.30  ? 67   LEU I CD2 1 
ATOM   9408  N  N   . SER I  1 68  ? 89.195  49.720  -3.002 1.00 41.66  ? 68   SER I N   1 
ATOM   9409  C  CA  . SER I  1 68  ? 88.719  51.081  -2.799 1.00 47.64  ? 68   SER I CA  1 
ATOM   9410  C  C   . SER I  1 68  ? 87.206  51.195  -2.963 1.00 58.05  ? 68   SER I C   1 
ATOM   9411  O  O   . SER I  1 68  ? 86.692  52.060  -3.674 1.00 43.58  ? 68   SER I O   1 
ATOM   9412  C  CB  . SER I  1 68  ? 89.442  52.025  -3.766 1.00 53.01  ? 68   SER I CB  1 
ATOM   9413  O  OG  . SER I  1 68  ? 90.721  52.344  -3.234 1.00 56.99  ? 68   SER I OG  1 
ATOM   9414  N  N   . ARG I  1 69  ? 86.507  50.304  -2.272 1.00 52.71  ? 69   ARG I N   1 
ATOM   9415  C  CA  . ARG I  1 69  ? 85.060  50.313  -2.148 1.00 46.69  ? 69   ARG I CA  1 
ATOM   9416  C  C   . ARG I  1 69  ? 84.628  51.005  -0.861 1.00 43.21  ? 69   ARG I C   1 
ATOM   9417  O  O   . ARG I  1 69  ? 85.400  51.505  -0.042 1.00 49.32  ? 69   ARG I O   1 
ATOM   9418  C  CB  . ARG I  1 69  ? 84.491  48.892  -2.166 1.00 51.42  ? 69   ARG I CB  1 
ATOM   9419  C  CG  . ARG I  1 69  ? 84.663  48.131  -3.465 1.00 57.23  ? 69   ARG I CG  1 
ATOM   9420  C  CD  . ARG I  1 69  ? 83.466  48.292  -4.384 1.00 69.11  ? 69   ARG I CD  1 
ATOM   9421  N  NE  . ARG I  1 69  ? 83.659  47.590  -5.650 1.00 76.55  ? 69   ARG I NE  1 
ATOM   9422  C  CZ  . ARG I  1 69  ? 83.825  46.278  -5.752 1.00 77.47  ? 69   ARG I CZ  1 
ATOM   9423  N  NH1 . ARG I  1 69  ? 83.995  45.713  -6.940 1.00 90.39  ? 69   ARG I NH1 1 
ATOM   9424  N  NH2 . ARG I  1 69  ? 83.821  45.516  -4.668 1.00 70.57  ? 69   ARG I NH2 1 
ATOM   9425  N  N   . LYS I  1 70  ? 83.310  51.047  -0.642 1.00 44.32  ? 70   LYS I N   1 
ATOM   9426  C  CA  . LYS I  1 70  ? 82.837  51.654  0.607  1.00 42.43  ? 70   LYS I CA  1 
ATOM   9427  C  C   . LYS I  1 70  ? 82.603  50.533  1.626  1.00 30.17  ? 70   LYS I C   1 
ATOM   9428  O  O   . LYS I  1 70  ? 82.512  49.388  1.179  1.00 39.66  ? 70   LYS I O   1 
ATOM   9429  C  CB  . LYS I  1 70  ? 81.568  52.461  0.355  1.00 54.42  ? 70   LYS I CB  1 
ATOM   9430  C  CG  . LYS I  1 70  ? 81.761  53.662  -0.558 1.00 57.16  ? 70   LYS I CG  1 
ATOM   9431  C  CD  . LYS I  1 70  ? 81.842  54.953  0.241  1.00 67.69  ? 70   LYS I CD  1 
ATOM   9432  C  CE  . LYS I  1 70  ? 82.671  54.825  1.503  1.00 77.88  ? 70   LYS I CE  1 
ATOM   9433  N  NZ  . LYS I  1 70  ? 83.250  56.129  1.936  1.00 88.40  ? 70   LYS I NZ  1 
ATOM   9434  N  N   . HIS I  1 71  ? 82.529  50.879  2.905  1.00 33.94  ? 71   HIS I N   1 
ATOM   9435  C  CA  . HIS I  1 71  ? 82.318  49.882  3.956  1.00 39.55  ? 71   HIS I CA  1 
ATOM   9436  C  C   . HIS I  1 71  ? 80.971  49.181  3.837  1.00 47.81  ? 71   HIS I C   1 
ATOM   9437  O  O   . HIS I  1 71  ? 79.933  49.757  3.491  1.00 41.70  ? 71   HIS I O   1 
ATOM   9438  C  CB  . HIS I  1 71  ? 82.415  50.518  5.348  1.00 33.59  ? 71   HIS I CB  1 
ATOM   9439  C  CG  . HIS I  1 71  ? 82.173  49.521  6.450  1.00 42.81  ? 71   HIS I CG  1 
ATOM   9440  N  ND1 . HIS I  1 71  ? 83.058  48.509  6.758  1.00 40.84  ? 71   HIS I ND1 1 
ATOM   9441  C  CD2 . HIS I  1 71  ? 81.143  49.375  7.322  1.00 46.62  ? 71   HIS I CD2 1 
ATOM   9442  C  CE1 . HIS I  1 71  ? 82.583  47.795  7.765  1.00 44.25  ? 71   HIS I CE1 1 
ATOM   9443  N  NE2 . HIS I  1 71  ? 81.409  48.295  8.139  1.00 38.33  ? 71   HIS I NE2 1 
ATOM   9444  N  N   . GLY I  1 72  ? 80.932  47.879  4.137  1.00 37.88  ? 72   GLY I N   1 
ATOM   9445  C  CA  . GLY I  1 72  ? 79.617  47.238  4.151  1.00 41.53  ? 72   GLY I CA  1 
ATOM   9446  C  C   . GLY I  1 72  ? 79.669  45.980  4.998  1.00 43.53  ? 72   GLY I C   1 
ATOM   9447  O  O   . GLY I  1 72  ? 80.612  45.806  5.766  1.00 40.33  ? 72   GLY I O   1 
ATOM   9448  N  N   . GLY I  1 73  ? 78.680  45.120  4.858  1.00 44.11  ? 73   GLY I N   1 
ATOM   9449  C  CA  . GLY I  1 73  ? 78.683  43.816  5.488  1.00 34.96  ? 73   GLY I CA  1 
ATOM   9450  C  C   . GLY I  1 73  ? 79.218  42.819  4.474  1.00 34.05  ? 73   GLY I C   1 
ATOM   9451  O  O   . GLY I  1 73  ? 79.317  43.122  3.283  1.00 36.65  ? 73   GLY I O   1 
ATOM   9452  N  N   . PRO I  1 74  ? 79.569  41.649  4.984  1.00 31.58  ? 74   PRO I N   1 
ATOM   9453  C  CA  . PRO I  1 74  ? 80.152  40.589  4.185  1.00 37.46  ? 74   PRO I CA  1 
ATOM   9454  C  C   . PRO I  1 74  ? 79.273  40.167  3.011  1.00 49.25  ? 74   PRO I C   1 
ATOM   9455  O  O   . PRO I  1 74  ? 79.769  39.642  2.013  1.00 40.26  ? 74   PRO I O   1 
ATOM   9456  C  CB  . PRO I  1 74  ? 80.247  39.405  5.153  1.00 38.91  ? 74   PRO I CB  1 
ATOM   9457  C  CG  . PRO I  1 74  ? 79.447  39.793  6.338  1.00 38.13  ? 74   PRO I CG  1 
ATOM   9458  C  CD  . PRO I  1 74  ? 79.442  41.291  6.407  1.00 31.56  ? 74   PRO I CD  1 
ATOM   9459  N  N   . LYS I  1 75  ? 77.967  40.377  3.134  1.00 45.73  ? 75   LYS I N   1 
ATOM   9460  C  CA  . LYS I  1 75  ? 77.066  39.957  2.060  1.00 51.91  ? 75   LYS I CA  1 
ATOM   9461  C  C   . LYS I  1 75  ? 76.874  41.053  1.019  1.00 48.64  ? 75   LYS I C   1 
ATOM   9462  O  O   . LYS I  1 75  ? 76.212  40.859  -0.006 1.00 58.58  ? 75   LYS I O   1 
ATOM   9463  C  CB  . LYS I  1 75  ? 75.721  39.503  2.661  1.00 52.11  ? 75   LYS I CB  1 
ATOM   9464  C  CG  . LYS I  1 75  ? 75.605  37.991  2.745  1.00 64.81  ? 75   LYS I CG  1 
ATOM   9465  C  CD  . LYS I  1 75  ? 74.868  37.470  3.965  1.00 74.48  ? 75   LYS I CD  1 
ATOM   9466  C  CE  . LYS I  1 75  ? 75.165  35.990  4.191  1.00 79.72  ? 75   LYS I CE  1 
ATOM   9467  N  NZ  . LYS I  1 75  ? 74.346  35.373  5.270  1.00 75.51  ? 75   LYS I NZ  1 
ATOM   9468  N  N   . ASP I  1 76  ? 77.440  42.235  1.223  1.00 40.13  ? 76   ASP I N   1 
ATOM   9469  C  CA  . ASP I  1 76  ? 77.309  43.320  0.261  1.00 42.68  ? 76   ASP I CA  1 
ATOM   9470  C  C   . ASP I  1 76  ? 78.422  43.312  -0.793 1.00 56.90  ? 76   ASP I C   1 
ATOM   9471  O  O   . ASP I  1 76  ? 79.604  43.229  -0.463 1.00 61.77  ? 76   ASP I O   1 
ATOM   9472  C  CB  . ASP I  1 76  ? 77.330  44.684  0.950  1.00 39.43  ? 76   ASP I CB  1 
ATOM   9473  C  CG  . ASP I  1 76  ? 76.233  44.868  1.980  1.00 53.57  ? 76   ASP I CG  1 
ATOM   9474  O  OD1 . ASP I  1 76  ? 76.479  45.561  2.994  1.00 61.56  ? 76   ASP I OD1 1 
ATOM   9475  O  OD2 . ASP I  1 76  ? 75.116  44.337  1.792  1.00 44.59  ? 76   ASP I OD2 1 
ATOM   9476  N  N   . GLU I  1 77  ? 78.016  43.414  -2.045 1.00 55.14  ? 77   GLU I N   1 
ATOM   9477  C  CA  . GLU I  1 77  ? 78.808  43.737  -3.223 1.00 52.19  ? 77   GLU I CA  1 
ATOM   9478  C  C   . GLU I  1 77  ? 79.671  44.961  -2.950 1.00 41.80  ? 77   GLU I C   1 
ATOM   9479  O  O   . GLU I  1 77  ? 80.884  45.010  -3.165 1.00 46.44  ? 77   GLU I O   1 
ATOM   9480  C  CB  . GLU I  1 77  ? 77.903  43.963  -4.430 1.00 73.40  ? 77   GLU I CB  1 
ATOM   9481  C  CG  . GLU I  1 77  ? 77.034  45.202  -4.457 1.00 91.11  ? 77   GLU I CG  1 
ATOM   9482  C  CD  . GLU I  1 77  ? 76.229  45.507  -3.213 1.00 97.03  ? 77   GLU I CD  1 
ATOM   9483  O  OE1 . GLU I  1 77  ? 75.388  44.660  -2.824 1.00 120.24 ? 77   GLU I OE1 1 
ATOM   9484  O  OE2 . GLU I  1 77  ? 76.424  46.578  -2.588 1.00 64.89  ? 77   GLU I OE2 1 
ATOM   9485  N  N   . GLU I  1 78  ? 79.073  46.025  -2.428 1.00 34.21  ? 78   GLU I N   1 
ATOM   9486  C  CA  . GLU I  1 78  ? 79.869  47.162  -2.023 1.00 36.25  ? 78   GLU I CA  1 
ATOM   9487  C  C   . GLU I  1 78  ? 80.343  46.964  -0.575 1.00 45.95  ? 78   GLU I C   1 
ATOM   9488  O  O   . GLU I  1 78  ? 79.667  47.357  0.373  1.00 52.12  ? 78   GLU I O   1 
ATOM   9489  C  CB  . GLU I  1 78  ? 79.097  48.465  -2.167 1.00 39.77  ? 78   GLU I CB  1 
ATOM   9490  C  CG  . GLU I  1 78  ? 79.881  49.689  -1.730 1.00 40.99  ? 78   GLU I CG  1 
ATOM   9491  C  CD  . GLU I  1 78  ? 80.839  50.218  -2.782 1.00 50.45  ? 78   GLU I CD  1 
ATOM   9492  O  OE1 . GLU I  1 78  ? 81.598  51.158  -2.456 1.00 49.00  ? 78   GLU I OE1 1 
ATOM   9493  O  OE2 . GLU I  1 78  ? 80.850  49.705  -3.922 1.00 49.71  ? 78   GLU I OE2 1 
ATOM   9494  N  N   . ARG I  1 79  ? 81.520  46.367  -0.456 1.00 47.98  ? 79   ARG I N   1 
ATOM   9495  C  CA  . ARG I  1 79  ? 82.225  46.153  0.795  1.00 43.43  ? 79   ARG I CA  1 
ATOM   9496  C  C   . ARG I  1 79  ? 83.749  46.222  0.661  1.00 42.44  ? 79   ARG I C   1 
ATOM   9497  O  O   . ARG I  1 79  ? 84.268  45.947  -0.420 1.00 47.67  ? 79   ARG I O   1 
ATOM   9498  C  CB  . ARG I  1 79  ? 81.857  44.779  1.349  1.00 32.68  ? 79   ARG I CB  1 
ATOM   9499  C  CG  . ARG I  1 79  ? 82.307  43.602  0.495  1.00 34.17  ? 79   ARG I CG  1 
ATOM   9500  C  CD  . ARG I  1 79  ? 82.191  42.314  1.303  1.00 44.61  ? 79   ARG I CD  1 
ATOM   9501  N  NE  . ARG I  1 79  ? 83.452  41.934  1.939  1.00 38.98  ? 79   ARG I NE  1 
ATOM   9502  C  CZ  . ARG I  1 79  ? 83.738  40.677  2.266  1.00 41.51  ? 79   ARG I CZ  1 
ATOM   9503  N  NH1 . ARG I  1 79  ? 84.897  40.358  2.833  1.00 34.12  ? 79   ARG I NH1 1 
ATOM   9504  N  NH2 . ARG I  1 79  ? 82.834  39.738  2.014  1.00 40.81  ? 79   ARG I NH2 1 
ATOM   9505  N  N   . HIS I  1 80  ? 84.428  46.564  1.751  1.00 43.82  ? 80   HIS I N   1 
ATOM   9506  C  CA  . HIS I  1 80  ? 85.875  46.426  1.878  1.00 35.48  ? 80   HIS I CA  1 
ATOM   9507  C  C   . HIS I  1 80  ? 86.228  44.947  1.883  1.00 45.59  ? 80   HIS I C   1 
ATOM   9508  O  O   . HIS I  1 80  ? 85.470  44.174  2.473  1.00 36.34  ? 80   HIS I O   1 
ATOM   9509  C  CB  . HIS I  1 80  ? 86.408  47.001  3.180  1.00 34.86  ? 80   HIS I CB  1 
ATOM   9510  C  CG  . HIS I  1 80  ? 86.116  48.433  3.441  1.00 30.22  ? 80   HIS I CG  1 
ATOM   9511  N  ND1 . HIS I  1 80  ? 85.847  48.916  4.698  1.00 33.35  ? 80   HIS I ND1 1 
ATOM   9512  C  CD2 . HIS I  1 80  ? 86.049  49.505  2.614  1.00 30.49  ? 80   HIS I CD2 1 
ATOM   9513  C  CE1 . HIS I  1 80  ? 85.625  50.225  4.655  1.00 34.22  ? 80   HIS I CE1 1 
ATOM   9514  N  NE2 . HIS I  1 80  ? 85.742  50.594  3.387  1.00 34.79  ? 80   HIS I NE2 1 
ATOM   9515  N  N   . VAL I  1 81  ? 87.348  44.566  1.277  1.00 46.50  ? 81   VAL I N   1 
ATOM   9516  C  CA  . VAL I  1 81  ? 87.730  43.157  1.313  1.00 47.45  ? 81   VAL I CA  1 
ATOM   9517  C  C   . VAL I  1 81  ? 87.764  42.623  2.745  1.00 33.73  ? 81   VAL I C   1 
ATOM   9518  O  O   . VAL I  1 81  ? 87.498  41.441  2.930  1.00 33.98  ? 81   VAL I O   1 
ATOM   9519  C  CB  . VAL I  1 81  ? 89.102  42.908  0.652  1.00 44.75  ? 81   VAL I CB  1 
ATOM   9520  C  CG1 . VAL I  1 81  ? 89.540  41.468  0.867  1.00 35.62  ? 81   VAL I CG1 1 
ATOM   9521  C  CG2 . VAL I  1 81  ? 89.045  43.245  -0.829 1.00 41.18  ? 81   VAL I CG2 1 
ATOM   9522  N  N   . GLY I  1 82  ? 88.074  43.463  3.722  1.00 36.48  ? 82   GLY I N   1 
ATOM   9523  C  CA  . GLY I  1 82  ? 88.289  42.990  5.084  1.00 39.00  ? 82   GLY I CA  1 
ATOM   9524  C  C   . GLY I  1 82  ? 87.047  42.968  5.948  1.00 36.27  ? 82   GLY I C   1 
ATOM   9525  O  O   . GLY I  1 82  ? 87.095  42.587  7.119  1.00 30.32  ? 82   GLY I O   1 
ATOM   9526  N  N   . ASP I  1 83  ? 85.923  43.378  5.358  1.00 31.23  ? 83   ASP I N   1 
ATOM   9527  C  CA  . ASP I  1 83  ? 84.673  43.457  6.108  1.00 34.11  ? 83   ASP I CA  1 
ATOM   9528  C  C   . ASP I  1 83  ? 84.088  42.092  6.411  1.00 38.03  ? 83   ASP I C   1 
ATOM   9529  O  O   . ASP I  1 83  ? 83.591  41.399  5.516  1.00 43.54  ? 83   ASP I O   1 
ATOM   9530  C  CB  . ASP I  1 83  ? 83.688  44.320  5.281  1.00 32.93  ? 83   ASP I CB  1 
ATOM   9531  C  CG  . ASP I  1 83  ? 84.050  45.780  5.389  1.00 31.13  ? 83   ASP I CG  1 
ATOM   9532  O  OD1 . ASP I  1 83  ? 84.819  46.131  6.312  1.00 38.63  ? 83   ASP I OD1 1 
ATOM   9533  O  OD2 . ASP I  1 83  ? 83.597  46.641  4.602  1.00 38.91  ? 83   ASP I OD2 1 
ATOM   9534  N  N   . LEU I  1 84  ? 84.120  41.632  7.668  1.00 31.45  ? 84   LEU I N   1 
ATOM   9535  C  CA  . LEU I  1 84  ? 83.519  40.323  7.942  1.00 28.28  ? 84   LEU I CA  1 
ATOM   9536  C  C   . LEU I  1 84  ? 82.307  40.427  8.862  1.00 25.54  ? 84   LEU I C   1 
ATOM   9537  O  O   . LEU I  1 84  ? 81.945  39.403  9.450  1.00 28.55  ? 84   LEU I O   1 
ATOM   9538  C  CB  . LEU I  1 84  ? 84.572  39.372  8.542  1.00 30.77  ? 84   LEU I CB  1 
ATOM   9539  C  CG  . LEU I  1 84  ? 85.776  39.200  7.599  1.00 32.36  ? 84   LEU I CG  1 
ATOM   9540  C  CD1 . LEU I  1 84  ? 86.915  38.463  8.278  1.00 30.71  ? 84   LEU I CD1 1 
ATOM   9541  C  CD2 . LEU I  1 84  ? 85.325  38.473  6.340  1.00 33.13  ? 84   LEU I CD2 1 
ATOM   9542  N  N   . GLY I  1 85  ? 81.699  41.593  8.966  1.00 25.45  ? 85   GLY I N   1 
ATOM   9543  C  CA  . GLY I  1 85  ? 80.463  41.759  9.712  1.00 28.63  ? 85   GLY I CA  1 
ATOM   9544  C  C   . GLY I  1 85  ? 80.621  41.730  11.219 1.00 28.99  ? 85   GLY I C   1 
ATOM   9545  O  O   . GLY I  1 85  ? 81.495  42.390  11.789 1.00 26.37  ? 85   GLY I O   1 
ATOM   9546  N  N   . ASN I  1 86  ? 79.756  40.975  11.906 1.00 28.19  ? 86   ASN I N   1 
ATOM   9547  C  CA  . ASN I  1 86  ? 79.766  40.873  13.353 1.00 24.07  ? 86   ASN I CA  1 
ATOM   9548  C  C   . ASN I  1 86  ? 79.950  39.449  13.853 1.00 25.91  ? 86   ASN I C   1 
ATOM   9549  O  O   . ASN I  1 86  ? 79.445  38.503  13.254 1.00 26.74  ? 86   ASN I O   1 
ATOM   9550  C  CB  . ASN I  1 86  ? 78.406  41.317  13.939 1.00 25.00  ? 86   ASN I CB  1 
ATOM   9551  C  CG  . ASN I  1 86  ? 78.214  42.809  13.806 1.00 29.69  ? 86   ASN I CG  1 
ATOM   9552  O  OD1 . ASN I  1 86  ? 78.896  43.586  14.477 1.00 33.36  ? 86   ASN I OD1 1 
ATOM   9553  N  ND2 . ASN I  1 86  ? 77.283  43.206  12.944 1.00 26.25  ? 86   ASN I ND2 1 
ATOM   9554  N  N   . VAL I  1 87  ? 80.629  39.288  14.989 1.00 21.73  ? 87   VAL I N   1 
ATOM   9555  C  CA  . VAL I  1 87  ? 80.555  38.032  15.740 1.00 26.01  ? 87   VAL I CA  1 
ATOM   9556  C  C   . VAL I  1 87  ? 79.661  38.259  16.957 1.00 28.52  ? 87   VAL I C   1 
ATOM   9557  O  O   . VAL I  1 87  ? 79.437  39.387  17.405 1.00 28.06  ? 87   VAL I O   1 
ATOM   9558  C  CB  . VAL I  1 87  ? 81.952  37.544  16.147 1.00 26.68  ? 87   VAL I CB  1 
ATOM   9559  C  CG1 . VAL I  1 87  ? 82.836  37.272  14.943 1.00 25.73  ? 87   VAL I CG1 1 
ATOM   9560  C  CG2 . VAL I  1 87  ? 82.612  38.604  17.026 1.00 27.64  ? 87   VAL I CG2 1 
ATOM   9561  N  N   . THR I  1 88  ? 79.091  37.182  17.498 1.00 23.99  ? 88   THR I N   1 
ATOM   9562  C  CA  . THR I  1 88  ? 78.132  37.369  18.588 1.00 23.65  ? 88   THR I CA  1 
ATOM   9563  C  C   . THR I  1 88  ? 78.601  36.703  19.867 1.00 23.89  ? 88   THR I C   1 
ATOM   9564  O  O   . THR I  1 88  ? 78.783  35.475  19.857 1.00 24.50  ? 88   THR I O   1 
ATOM   9565  C  CB  . THR I  1 88  ? 76.772  36.773  18.158 1.00 26.18  ? 88   THR I CB  1 
ATOM   9566  O  OG1 . THR I  1 88  ? 76.294  37.466  16.999 1.00 26.88  ? 88   THR I OG1 1 
ATOM   9567  C  CG2 . THR I  1 88  ? 75.718  36.992  19.234 1.00 27.99  ? 88   THR I CG2 1 
ATOM   9568  N  N   . ALA I  1 89  ? 78.789  37.486  20.928 1.00 22.19  ? 89   ALA I N   1 
ATOM   9569  C  CA  . ALA I  1 89  ? 79.156  36.932  22.227 1.00 23.80  ? 89   ALA I CA  1 
ATOM   9570  C  C   . ALA I  1 89  ? 77.924  36.545  23.036 1.00 24.87  ? 89   ALA I C   1 
ATOM   9571  O  O   . ALA I  1 89  ? 76.947  37.299  23.139 1.00 26.74  ? 89   ALA I O   1 
ATOM   9572  C  CB  . ALA I  1 89  ? 80.032  37.892  23.020 1.00 21.37  ? 89   ALA I CB  1 
ATOM   9573  N  N   . ASP I  1 90  ? 77.969  35.342  23.612 1.00 22.26  ? 90   ASP I N   1 
ATOM   9574  C  CA  . ASP I  1 90  ? 76.829  34.910  24.429 1.00 21.34  ? 90   ASP I CA  1 
ATOM   9575  C  C   . ASP I  1 90  ? 76.868  35.542  25.818 1.00 22.76  ? 90   ASP I C   1 
ATOM   9576  O  O   . ASP I  1 90  ? 77.685  36.431  26.074 1.00 25.11  ? 90   ASP I O   1 
ATOM   9577  C  CB  . ASP I  1 90  ? 76.777  33.387  24.508 1.00 25.18  ? 90   ASP I CB  1 
ATOM   9578  C  CG  . ASP I  1 90  ? 77.967  32.765  25.212 1.00 32.79  ? 90   ASP I CG  1 
ATOM   9579  O  OD1 . ASP I  1 90  ? 78.204  31.569  24.961 1.00 27.15  ? 90   ASP I OD1 1 
ATOM   9580  O  OD2 . ASP I  1 90  ? 78.663  33.413  26.004 1.00 28.76  ? 90   ASP I OD2 1 
ATOM   9581  N  N   . LYS I  1 91  ? 75.983  35.084  26.689 1.00 23.25  ? 91   LYS I N   1 
ATOM   9582  C  CA  . LYS I  1 91  ? 75.866  35.711  28.000 1.00 26.15  ? 91   LYS I CA  1 
ATOM   9583  C  C   . LYS I  1 91  ? 77.112  35.497  28.843 1.00 37.34  ? 91   LYS I C   1 
ATOM   9584  O  O   . LYS I  1 91  ? 77.307  36.206  29.834 1.00 36.89  ? 91   LYS I O   1 
ATOM   9585  C  CB  . LYS I  1 91  ? 74.673  35.109  28.760 1.00 33.89  ? 91   LYS I CB  1 
ATOM   9586  C  CG  . LYS I  1 91  ? 74.745  33.584  28.773 1.00 44.05  ? 91   LYS I CG  1 
ATOM   9587  C  CD  . LYS I  1 91  ? 74.004  33.021  29.979 1.00 57.91  ? 91   LYS I CD  1 
ATOM   9588  C  CE  . LYS I  1 91  ? 74.458  31.606  30.304 1.00 63.28  ? 91   LYS I CE  1 
ATOM   9589  N  NZ  . LYS I  1 91  ? 73.354  30.621  30.127 1.00 76.66  ? 91   LYS I NZ  1 
ATOM   9590  N  N   . ASP I  1 92  ? 77.914  34.517  28.433 1.00 30.52  ? 92   ASP I N   1 
ATOM   9591  C  CA  . ASP I  1 92  ? 79.182  34.248  29.112 1.00 30.29  ? 92   ASP I CA  1 
ATOM   9592  C  C   . ASP I  1 92  ? 80.337  35.022  28.514 1.00 31.81  ? 92   ASP I C   1 
ATOM   9593  O  O   . ASP I  1 92  ? 81.485  34.884  28.950 1.00 30.65  ? 92   ASP I O   1 
ATOM   9594  C  CB  . ASP I  1 92  ? 79.448  32.735  29.054 1.00 32.11  ? 92   ASP I CB  1 
ATOM   9595  C  CG  . ASP I  1 92  ? 78.475  31.989  29.958 1.00 40.24  ? 92   ASP I CG  1 
ATOM   9596  O  OD1 . ASP I  1 92  ? 78.115  30.834  29.645 1.00 47.49  ? 92   ASP I OD1 1 
ATOM   9597  O  OD2 . ASP I  1 92  ? 78.074  32.575  30.984 1.00 41.01  ? 92   ASP I OD2 1 
ATOM   9598  N  N   . GLY I  1 93  ? 80.114  35.852  27.498 1.00 28.87  ? 93   GLY I N   1 
ATOM   9599  C  CA  . GLY I  1 93  ? 81.186  36.643  26.911 1.00 28.23  ? 93   GLY I CA  1 
ATOM   9600  C  C   . GLY I  1 93  ? 81.962  35.876  25.855 1.00 23.55  ? 93   GLY I C   1 
ATOM   9601  O  O   . GLY I  1 93  ? 83.043  36.282  25.437 1.00 28.69  ? 93   GLY I O   1 
ATOM   9602  N  N   . VAL I  1 94  ? 81.414  34.739  25.424 1.00 21.67  ? 94   VAL I N   1 
ATOM   9603  C  CA  . VAL I  1 94  ? 82.149  33.922  24.457 1.00 25.08  ? 94   VAL I CA  1 
ATOM   9604  C  C   . VAL I  1 94  ? 81.477  33.970  23.081 1.00 28.90  ? 94   VAL I C   1 
ATOM   9605  O  O   . VAL I  1 94  ? 80.270  33.696  22.963 1.00 25.74  ? 94   VAL I O   1 
ATOM   9606  C  CB  . VAL I  1 94  ? 82.251  32.441  24.880 1.00 27.01  ? 94   VAL I CB  1 
ATOM   9607  C  CG1 . VAL I  1 94  ? 82.908  31.643  23.750 1.00 28.04  ? 94   VAL I CG1 1 
ATOM   9608  C  CG2 . VAL I  1 94  ? 82.989  32.267  26.199 1.00 26.60  ? 94   VAL I CG2 1 
ATOM   9609  N  N   . ALA I  1 95  ? 82.243  34.308  22.069 1.00 25.81  ? 95   ALA I N   1 
ATOM   9610  C  CA  . ALA I  1 95  ? 81.820  34.305  20.673 1.00 29.05  ? 95   ALA I CA  1 
ATOM   9611  C  C   . ALA I  1 95  ? 82.450  33.113  19.952 1.00 28.45  ? 95   ALA I C   1 
ATOM   9612  O  O   . ALA I  1 95  ? 83.665  33.069  19.767 1.00 27.73  ? 95   ALA I O   1 
ATOM   9613  C  CB  . ALA I  1 95  ? 82.195  35.609  19.986 1.00 25.68  ? 95   ALA I CB  1 
ATOM   9614  N  N   . ASP I  1 96  ? 81.621  32.163  19.556 1.00 22.64  ? 96   ASP I N   1 
ATOM   9615  C  CA  . ASP I  1 96  ? 82.081  31.019  18.765 1.00 23.39  ? 96   ASP I CA  1 
ATOM   9616  C  C   . ASP I  1 96  ? 81.953  31.457  17.318 1.00 29.72  ? 96   ASP I C   1 
ATOM   9617  O  O   . ASP I  1 96  ? 80.882  31.745  16.791 1.00 31.65  ? 96   ASP I O   1 
ATOM   9618  C  CB  . ASP I  1 96  ? 81.298  29.777  19.158 1.00 35.40  ? 96   ASP I CB  1 
ATOM   9619  C  CG  . ASP I  1 96  ? 81.779  29.176  20.469 1.00 48.68  ? 96   ASP I CG  1 
ATOM   9620  O  OD1 . ASP I  1 96  ? 81.003  28.483  21.159 1.00 60.22  ? 96   ASP I OD1 1 
ATOM   9621  O  OD2 . ASP I  1 96  ? 82.954  29.377  20.870 1.00 53.91  ? 96   ASP I OD2 1 
ATOM   9622  N  N   . VAL I  1 97  ? 83.089  31.589  16.644 1.00 26.06  ? 97   VAL I N   1 
ATOM   9623  C  CA  . VAL I  1 97  ? 83.119  32.203  15.329 1.00 24.65  ? 97   VAL I CA  1 
ATOM   9624  C  C   . VAL I  1 97  ? 83.067  31.142  14.248 1.00 24.64  ? 97   VAL I C   1 
ATOM   9625  O  O   . VAL I  1 97  ? 83.785  30.149  14.298 1.00 25.37  ? 97   VAL I O   1 
ATOM   9626  C  CB  . VAL I  1 97  ? 84.370  33.091  15.203 1.00 27.06  ? 97   VAL I CB  1 
ATOM   9627  C  CG1 . VAL I  1 97  ? 84.543  33.608  13.788 1.00 24.28  ? 97   VAL I CG1 1 
ATOM   9628  C  CG2 . VAL I  1 97  ? 84.227  34.247  16.184 1.00 24.95  ? 97   VAL I CG2 1 
ATOM   9629  N  N   . SER I  1 98  ? 82.186  31.321  13.261 1.00 28.90  ? 98   SER I N   1 
ATOM   9630  C  CA  . SER I  1 98  ? 82.134  30.366  12.150 1.00 28.67  ? 98   SER I CA  1 
ATOM   9631  C  C   . SER I  1 98  ? 81.582  31.057  10.913 1.00 39.91  ? 98   SER I C   1 
ATOM   9632  O  O   . SER I  1 98  ? 80.406  31.367  10.761 1.00 30.75  ? 98   SER I O   1 
ATOM   9633  C  CB  . SER I  1 98  ? 81.313  29.123  12.495 1.00 33.06  ? 98   SER I CB  1 
ATOM   9634  O  OG  . SER I  1 98  ? 81.351  28.210  11.405 1.00 36.01  ? 98   SER I OG  1 
ATOM   9635  N  N   . ILE I  1 99  ? 82.519  31.318  10.015 1.00 36.92  ? 99   ILE I N   1 
ATOM   9636  C  CA  . ILE I  1 99  ? 82.259  32.178  8.874  1.00 34.09  ? 99   ILE I CA  1 
ATOM   9637  C  C   . ILE I  1 99  ? 82.889  31.562  7.631  1.00 36.86  ? 99   ILE I C   1 
ATOM   9638  O  O   . ILE I  1 99  ? 83.920  30.905  7.709  1.00 32.98  ? 99   ILE I O   1 
ATOM   9639  C  CB  . ILE I  1 99  ? 82.860  33.570  9.130  1.00 36.11  ? 99   ILE I CB  1 
ATOM   9640  C  CG1 . ILE I  1 99  ? 82.054  34.418  10.122 1.00 47.20  ? 99   ILE I CG1 1 
ATOM   9641  C  CG2 . ILE I  1 99  ? 83.095  34.324  7.830  1.00 43.16  ? 99   ILE I CG2 1 
ATOM   9642  C  CD1 . ILE I  1 99  ? 82.803  35.634  10.654 1.00 36.71  ? 99   ILE I CD1 1 
ATOM   9643  N  N   . GLU I  1 100 ? 82.249  31.773  6.497  1.00 34.99  ? 100  GLU I N   1 
ATOM   9644  C  CA  . GLU I  1 100 ? 82.829  31.478  5.201  1.00 37.08  ? 100  GLU I CA  1 
ATOM   9645  C  C   . GLU I  1 100 ? 82.752  32.755  4.367  1.00 37.17  ? 100  GLU I C   1 
ATOM   9646  O  O   . GLU I  1 100 ? 81.694  33.388  4.335  1.00 38.28  ? 100  GLU I O   1 
ATOM   9647  C  CB  . GLU I  1 100 ? 82.148  30.330  4.465  1.00 42.13  ? 100  GLU I CB  1 
ATOM   9648  C  CG  . GLU I  1 100 ? 83.093  29.685  3.452  1.00 57.95  ? 100  GLU I CG  1 
ATOM   9649  C  CD  . GLU I  1 100 ? 82.378  28.553  2.730  1.00 70.14  ? 100  GLU I CD  1 
ATOM   9650  O  OE1 . GLU I  1 100 ? 82.612  27.399  3.143  1.00 65.52  ? 100  GLU I OE1 1 
ATOM   9651  O  OE2 . GLU I  1 100 ? 81.610  28.868  1.796  1.00 67.06  ? 100  GLU I OE2 1 
ATOM   9652  N  N   . ASP I  1 101 ? 83.874  33.123  3.747  1.00 35.52  ? 101  ASP I N   1 
ATOM   9653  C  CA  . ASP I  1 101 ? 83.915  34.363  2.977  1.00 30.13  ? 101  ASP I CA  1 
ATOM   9654  C  C   . ASP I  1 101 ? 84.651  34.126  1.665  1.00 34.24  ? 101  ASP I C   1 
ATOM   9655  O  O   . ASP I  1 101 ? 85.650  33.411  1.636  1.00 38.75  ? 101  ASP I O   1 
ATOM   9656  C  CB  . ASP I  1 101 ? 84.573  35.503  3.753  1.00 32.89  ? 101  ASP I CB  1 
ATOM   9657  C  CG  . ASP I  1 101 ? 84.275  36.843  3.101  1.00 51.87  ? 101  ASP I CG  1 
ATOM   9658  O  OD1 . ASP I  1 101 ? 85.165  37.397  2.416  1.00 46.53  ? 101  ASP I OD1 1 
ATOM   9659  O  OD2 . ASP I  1 101 ? 83.143  37.362  3.265  1.00 47.26  ? 101  ASP I OD2 1 
ATOM   9660  N  N   . SER I  1 102 ? 84.150  34.718  0.591  1.00 35.55  ? 102  SER I N   1 
ATOM   9661  C  CA  . SER I  1 102 ? 84.726  34.422  -0.721 1.00 42.49  ? 102  SER I CA  1 
ATOM   9662  C  C   . SER I  1 102 ? 85.473  35.623  -1.283 1.00 38.34  ? 102  SER I C   1 
ATOM   9663  O  O   . SER I  1 102 ? 85.984  35.554  -2.408 1.00 45.91  ? 102  SER I O   1 
ATOM   9664  C  CB  . SER I  1 102 ? 83.606  33.984  -1.674 1.00 57.46  ? 102  SER I CB  1 
ATOM   9665  O  OG  . SER I  1 102 ? 82.628  35.015  -1.794 1.00 58.90  ? 102  SER I OG  1 
ATOM   9666  N  N   . VAL I  1 103 ? 85.516  36.694  -0.495 1.00 36.29  ? 103  VAL I N   1 
ATOM   9667  C  CA  . VAL I  1 103 ? 86.172  37.934  -0.893 1.00 39.31  ? 103  VAL I CA  1 
ATOM   9668  C  C   . VAL I  1 103 ? 87.570  38.029  -0.287 1.00 47.36  ? 103  VAL I C   1 
ATOM   9669  O  O   . VAL I  1 103 ? 88.476  38.503  -0.973 1.00 42.56  ? 103  VAL I O   1 
ATOM   9670  C  CB  . VAL I  1 103 ? 85.336  39.157  -0.498 1.00 42.00  ? 103  VAL I CB  1 
ATOM   9671  C  CG1 . VAL I  1 103 ? 86.103  40.448  -0.702 1.00 39.07  ? 103  VAL I CG1 1 
ATOM   9672  C  CG2 . VAL I  1 103 ? 84.044  39.180  -1.309 1.00 34.82  ? 103  VAL I CG2 1 
ATOM   9673  N  N   . ILE I  1 104 ? 87.781  37.581  0.949  1.00 38.55  ? 104  ILE I N   1 
ATOM   9674  C  CA  . ILE I  1 104 ? 89.133  37.437  1.474  1.00 39.05  ? 104  ILE I CA  1 
ATOM   9675  C  C   . ILE I  1 104 ? 89.811  36.219  0.862  1.00 35.32  ? 104  ILE I C   1 
ATOM   9676  O  O   . ILE I  1 104 ? 89.162  35.251  0.479  1.00 44.46  ? 104  ILE I O   1 
ATOM   9677  C  CB  . ILE I  1 104 ? 89.187  37.227  3.003  1.00 34.27  ? 104  ILE I CB  1 
ATOM   9678  C  CG1 . ILE I  1 104 ? 88.420  35.980  3.438  1.00 30.09  ? 104  ILE I CG1 1 
ATOM   9679  C  CG2 . ILE I  1 104 ? 88.708  38.464  3.721  1.00 30.29  ? 104  ILE I CG2 1 
ATOM   9680  C  CD1 . ILE I  1 104 ? 88.598  35.633  4.903  1.00 34.36  ? 104  ILE I CD1 1 
ATOM   9681  N  N   . SER I  1 105 ? 91.140  36.273  0.802  1.00 34.65  ? 105  SER I N   1 
ATOM   9682  C  CA  . SER I  1 105 ? 91.911  35.158  0.279  1.00 39.25  ? 105  SER I CA  1 
ATOM   9683  C  C   . SER I  1 105 ? 93.180  34.909  1.093  1.00 34.49  ? 105  SER I C   1 
ATOM   9684  O  O   . SER I  1 105 ? 93.665  35.817  1.773  1.00 43.88  ? 105  SER I O   1 
ATOM   9685  C  CB  . SER I  1 105 ? 92.322  35.404  -1.187 1.00 36.72  ? 105  SER I CB  1 
ATOM   9686  O  OG  . SER I  1 105 ? 92.783  34.165  -1.717 1.00 40.47  ? 105  SER I OG  1 
ATOM   9687  N  N   . LEU I  1 106 ? 93.720  33.696  1.014  1.00 39.69  ? 106  LEU I N   1 
ATOM   9688  C  CA  . LEU I  1 106 ? 95.014  33.467  1.661  1.00 38.69  ? 106  LEU I CA  1 
ATOM   9689  C  C   . LEU I  1 106 ? 96.136  33.539  0.629  1.00 50.99  ? 106  LEU I C   1 
ATOM   9690  O  O   . LEU I  1 106 ? 97.283  33.205  0.929  1.00 39.96  ? 106  LEU I O   1 
ATOM   9691  C  CB  . LEU I  1 106 ? 95.027  32.124  2.381  1.00 34.99  ? 106  LEU I CB  1 
ATOM   9692  C  CG  . LEU I  1 106 ? 93.933  31.988  3.452  1.00 35.24  ? 106  LEU I CG  1 
ATOM   9693  C  CD1 . LEU I  1 106 ? 94.135  30.737  4.277  1.00 33.68  ? 106  LEU I CD1 1 
ATOM   9694  C  CD2 . LEU I  1 106 ? 93.925  33.242  4.312  1.00 35.33  ? 106  LEU I CD2 1 
ATOM   9695  N  N   . SER I  1 107 ? 95.791  33.990  -0.564 1.00 58.20  ? 107  SER I N   1 
ATOM   9696  C  CA  . SER I  1 107 ? 96.719  34.145  -1.682 1.00 64.24  ? 107  SER I CA  1 
ATOM   9697  C  C   . SER I  1 107 ? 96.215  35.196  -2.660 1.00 61.38  ? 107  SER I C   1 
ATOM   9698  O  O   . SER I  1 107 ? 95.001  35.412  -2.742 1.00 46.42  ? 107  SER I O   1 
ATOM   9699  C  CB  . SER I  1 107 ? 96.891  32.806  -2.402 1.00 67.08  ? 107  SER I CB  1 
ATOM   9700  O  OG  . SER I  1 107 ? 95.786  31.947  -2.150 1.00 88.89  ? 107  SER I OG  1 
ATOM   9701  N  N   . GLY I  1 108 ? 97.097  35.858  -3.401 1.00 66.48  ? 108  GLY I N   1 
ATOM   9702  C  CA  . GLY I  1 108 ? 96.681  36.813  -4.409 1.00 62.80  ? 108  GLY I CA  1 
ATOM   9703  C  C   . GLY I  1 108 ? 96.552  38.254  -3.959 1.00 63.21  ? 108  GLY I C   1 
ATOM   9704  O  O   . GLY I  1 108 ? 96.967  38.617  -2.860 1.00 74.12  ? 108  GLY I O   1 
ATOM   9705  N  N   . ASP I  1 109 ? 95.973  39.093  -4.815 1.00 55.12  ? 109  ASP I N   1 
ATOM   9706  C  CA  . ASP I  1 109 ? 95.792  40.513  -4.599 1.00 66.37  ? 109  ASP I CA  1 
ATOM   9707  C  C   . ASP I  1 109 ? 94.906  40.792  -3.386 1.00 69.51  ? 109  ASP I C   1 
ATOM   9708  O  O   . ASP I  1 109 ? 94.898  41.915  -2.874 1.00 65.61  ? 109  ASP I O   1 
ATOM   9709  C  CB  . ASP I  1 109 ? 95.152  41.182  -5.819 1.00 77.88  ? 109  ASP I CB  1 
ATOM   9710  C  CG  . ASP I  1 109 ? 95.878  40.947  -7.129 1.00 82.98  ? 109  ASP I CG  1 
ATOM   9711  O  OD1 . ASP I  1 109 ? 97.089  41.244  -7.214 1.00 67.46  ? 109  ASP I OD1 1 
ATOM   9712  O  OD2 . ASP I  1 109 ? 95.226  40.469  -8.087 1.00 87.45  ? 109  ASP I OD2 1 
ATOM   9713  N  N   . HIS I  1 110 ? 94.161  39.777  -2.955 1.00 68.69  ? 110  HIS I N   1 
ATOM   9714  C  CA  . HIS I  1 110 ? 93.255  39.949  -1.823 1.00 68.69  ? 110  HIS I CA  1 
ATOM   9715  C  C   . HIS I  1 110 ? 93.736  39.235  -0.568 1.00 60.41  ? 110  HIS I C   1 
ATOM   9716  O  O   . HIS I  1 110 ? 92.942  38.964  0.336  1.00 49.10  ? 110  HIS I O   1 
ATOM   9717  C  CB  . HIS I  1 110 ? 91.853  39.434  -2.203 1.00 72.99  ? 110  HIS I CB  1 
ATOM   9718  C  CG  . HIS I  1 110 ? 91.168  40.440  -3.081 1.00 79.44  ? 110  HIS I CG  1 
ATOM   9719  N  ND1 . HIS I  1 110 ? 89.806  40.546  -3.209 1.00 82.27  ? 110  HIS I ND1 1 
ATOM   9720  C  CD2 . HIS I  1 110 ? 91.703  41.404  -3.866 1.00 79.66  ? 110  HIS I CD2 1 
ATOM   9721  C  CE1 . HIS I  1 110 ? 89.521  41.525  -4.046 1.00 85.98  ? 110  HIS I CE1 1 
ATOM   9722  N  NE2 . HIS I  1 110 ? 90.658  42.064  -4.462 1.00 87.05  ? 110  HIS I NE2 1 
ATOM   9723  N  N   . CYS I  1 111 ? 95.023  38.941  -0.545 1.00 51.63  ? 111  CYS I N   1 
ATOM   9724  C  CA  . CYS I  1 111 ? 95.678  38.194  0.509  1.00 50.61  ? 111  CYS I CA  1 
ATOM   9725  C  C   . CYS I  1 111 ? 95.592  38.871  1.864  1.00 39.43  ? 111  CYS I C   1 
ATOM   9726  O  O   . CYS I  1 111 ? 95.827  40.072  1.979  1.00 46.91  ? 111  CYS I O   1 
ATOM   9727  C  CB  . CYS I  1 111 ? 97.170  38.012  0.158  1.00 49.01  ? 111  CYS I CB  1 
ATOM   9728  S  SG  . CYS I  1 111 ? 97.941  36.698  1.125  1.00 67.44  ? 111  CYS I SG  1 
ATOM   9729  N  N   . ILE I  1 112 ? 95.280  38.129  2.924  1.00 31.96  ? 112  ILE I N   1 
ATOM   9730  C  CA  . ILE I  1 112 ? 95.186  38.808  4.217  1.00 31.40  ? 112  ILE I CA  1 
ATOM   9731  C  C   . ILE I  1 112 ? 96.325  38.373  5.120  1.00 34.16  ? 112  ILE I C   1 
ATOM   9732  O  O   . ILE I  1 112 ? 96.476  38.839  6.250  1.00 36.50  ? 112  ILE I O   1 
ATOM   9733  C  CB  . ILE I  1 112 ? 93.845  38.512  4.910  1.00 29.77  ? 112  ILE I CB  1 
ATOM   9734  C  CG1 . ILE I  1 112 ? 93.615  37.043  5.229  1.00 32.10  ? 112  ILE I CG1 1 
ATOM   9735  C  CG2 . ILE I  1 112 ? 92.720  39.060  4.038  1.00 33.70  ? 112  ILE I CG2 1 
ATOM   9736  C  CD1 . ILE I  1 112 ? 92.276  36.781  5.903  1.00 35.66  ? 112  ILE I CD1 1 
ATOM   9737  N  N   . ILE I  1 113 ? 97.149  37.456  4.617  1.00 40.18  ? 113  ILE I N   1 
ATOM   9738  C  CA  . ILE I  1 113 ? 98.272  37.065  5.494  1.00 41.27  ? 113  ILE I CA  1 
ATOM   9739  C  C   . ILE I  1 113 ? 99.187  38.255  5.734  1.00 33.96  ? 113  ILE I C   1 
ATOM   9740  O  O   . ILE I  1 113 ? 99.510  39.022  4.827  1.00 34.07  ? 113  ILE I O   1 
ATOM   9741  C  CB  . ILE I  1 113 ? 98.992  35.849  4.894  1.00 43.23  ? 113  ILE I CB  1 
ATOM   9742  C  CG1 . ILE I  1 113 ? 98.176  34.557  5.031  1.00 36.11  ? 113  ILE I CG1 1 
ATOM   9743  C  CG2 . ILE I  1 113 ? 100.377 35.687  5.486  1.00 27.10  ? 113  ILE I CG2 1 
ATOM   9744  C  CD1 . ILE I  1 113 ? 98.350  33.597  3.876  1.00 49.68  ? 113  ILE I CD1 1 
ATOM   9745  N  N   . GLY I  1 114 ? 99.610  38.463  6.988  1.00 28.69  ? 114  GLY I N   1 
ATOM   9746  C  CA  . GLY I  1 114 ? 100.469 39.613  7.231  1.00 29.82  ? 114  GLY I CA  1 
ATOM   9747  C  C   . GLY I  1 114 ? 99.683  40.832  7.666  1.00 34.54  ? 114  GLY I C   1 
ATOM   9748  O  O   . GLY I  1 114 ? 100.282 41.821  8.080  1.00 28.79  ? 114  GLY I O   1 
ATOM   9749  N  N   . ARG I  1 115 ? 98.356  40.776  7.588  1.00 28.72  ? 115  ARG I N   1 
ATOM   9750  C  CA  . ARG I  1 115 ? 97.523  41.905  8.018  1.00 30.83  ? 115  ARG I CA  1 
ATOM   9751  C  C   . ARG I  1 115 ? 96.916  41.634  9.376  1.00 26.41  ? 115  ARG I C   1 
ATOM   9752  O  O   . ARG I  1 115 ? 97.246  40.646  10.036 1.00 32.26  ? 115  ARG I O   1 
ATOM   9753  C  CB  . ARG I  1 115 ? 96.437  42.177  6.959  1.00 31.01  ? 115  ARG I CB  1 
ATOM   9754  C  CG  . ARG I  1 115 ? 97.090  42.308  5.582  1.00 37.47  ? 115  ARG I CG  1 
ATOM   9755  C  CD  . ARG I  1 115 ? 96.145  42.854  4.535  1.00 42.29  ? 115  ARG I CD  1 
ATOM   9756  N  NE  . ARG I  1 115 ? 96.762  42.872  3.207  1.00 40.34  ? 115  ARG I NE  1 
ATOM   9757  C  CZ  . ARG I  1 115 ? 97.585  43.855  2.836  1.00 36.22  ? 115  ARG I CZ  1 
ATOM   9758  N  NH1 . ARG I  1 115 ? 98.128  43.856  1.632  1.00 33.17  ? 115  ARG I NH1 1 
ATOM   9759  N  NH2 . ARG I  1 115 ? 97.856  44.837  3.679  1.00 40.13  ? 115  ARG I NH2 1 
ATOM   9760  N  N   . THR I  1 116 ? 96.022  42.492  9.847  1.00 26.51  ? 116  THR I N   1 
ATOM   9761  C  CA  . THR I  1 116 ? 95.596  42.352  11.229 1.00 32.11  ? 116  THR I CA  1 
ATOM   9762  C  C   . THR I  1 116 ? 94.102  42.049  11.325 1.00 35.27  ? 116  THR I C   1 
ATOM   9763  O  O   . THR I  1 116 ? 93.344  42.737  10.648 1.00 35.86  ? 116  THR I O   1 
ATOM   9764  C  CB  . THR I  1 116 ? 95.891  43.643  12.006 1.00 28.78  ? 116  THR I CB  1 
ATOM   9765  O  OG1 . THR I  1 116 ? 97.319  43.775  12.113 1.00 33.77  ? 116  THR I OG1 1 
ATOM   9766  C  CG2 . THR I  1 116 ? 95.353  43.568  13.423 1.00 25.96  ? 116  THR I CG2 1 
ATOM   9767  N  N   . LEU I  1 117 ? 93.725  41.075  12.134 1.00 26.71  ? 117  LEU I N   1 
ATOM   9768  C  CA  . LEU I  1 117 ? 92.304  40.817  12.417 1.00 23.20  ? 117  LEU I CA  1 
ATOM   9769  C  C   . LEU I  1 117 ? 91.956  41.594  13.679 1.00 30.87  ? 117  LEU I C   1 
ATOM   9770  O  O   . LEU I  1 117 ? 92.702  41.538  14.658 1.00 29.03  ? 117  LEU I O   1 
ATOM   9771  C  CB  . LEU I  1 117 ? 92.047  39.323  12.569 1.00 22.46  ? 117  LEU I CB  1 
ATOM   9772  C  CG  . LEU I  1 117 ? 90.623  38.849  12.845 1.00 27.14  ? 117  LEU I CG  1 
ATOM   9773  C  CD1 . LEU I  1 117 ? 89.714  39.231  11.677 1.00 27.39  ? 117  LEU I CD1 1 
ATOM   9774  C  CD2 . LEU I  1 117 ? 90.555  37.346  13.122 1.00 23.58  ? 117  LEU I CD2 1 
ATOM   9775  N  N   . VAL I  1 118 ? 90.856  42.330  13.720 1.00 27.66  ? 118  VAL I N   1 
ATOM   9776  C  CA  . VAL I  1 118 ? 90.423  43.092  14.879 1.00 25.39  ? 118  VAL I CA  1 
ATOM   9777  C  C   . VAL I  1 118 ? 88.988  42.754  15.284 1.00 24.16  ? 118  VAL I C   1 
ATOM   9778  O  O   . VAL I  1 118 ? 88.139  42.604  14.404 1.00 27.49  ? 118  VAL I O   1 
ATOM   9779  C  CB  . VAL I  1 118 ? 90.457  44.615  14.574 1.00 31.34  ? 118  VAL I CB  1 
ATOM   9780  C  CG1 . VAL I  1 118 ? 90.068  45.431  15.794 1.00 23.37  ? 118  VAL I CG1 1 
ATOM   9781  C  CG2 . VAL I  1 118 ? 91.830  45.036  14.040 1.00 30.83  ? 118  VAL I CG2 1 
ATOM   9782  N  N   . VAL I  1 119 ? 88.708  42.656  16.574 1.00 27.32  ? 119  VAL I N   1 
ATOM   9783  C  CA  . VAL I  1 119 ? 87.337  42.565  17.098 1.00 26.57  ? 119  VAL I CA  1 
ATOM   9784  C  C   . VAL I  1 119 ? 87.056  43.849  17.883 1.00 34.22  ? 119  VAL I C   1 
ATOM   9785  O  O   . VAL I  1 119 ? 87.887  44.363  18.650 1.00 27.54  ? 119  VAL I O   1 
ATOM   9786  C  CB  . VAL I  1 119 ? 87.094  41.298  17.922 1.00 25.74  ? 119  VAL I CB  1 
ATOM   9787  C  CG1 . VAL I  1 119 ? 87.921  41.227  19.199 1.00 27.20  ? 119  VAL I CG1 1 
ATOM   9788  C  CG2 . VAL I  1 119 ? 85.607  41.158  18.295 1.00 25.51  ? 119  VAL I CG2 1 
ATOM   9789  N  N   . HIS I  1 120 ? 85.873  44.428  17.668 1.00 29.77  ? 120  HIS I N   1 
ATOM   9790  C  CA  . HIS I  1 120 ? 85.567  45.768  18.174 1.00 25.66  ? 120  HIS I CA  1 
ATOM   9791  C  C   . HIS I  1 120 ? 84.632  45.841  19.365 1.00 34.70  ? 120  HIS I C   1 
ATOM   9792  O  O   . HIS I  1 120 ? 83.891  44.927  19.733 1.00 30.64  ? 120  HIS I O   1 
ATOM   9793  C  CB  . HIS I  1 120 ? 84.910  46.564  17.038 1.00 27.56  ? 120  HIS I CB  1 
ATOM   9794  C  CG  . HIS I  1 120 ? 85.864  46.935  15.948 1.00 30.83  ? 120  HIS I CG  1 
ATOM   9795  N  ND1 . HIS I  1 120 ? 86.405  48.206  15.901 1.00 36.92  ? 120  HIS I ND1 1 
ATOM   9796  C  CD2 . HIS I  1 120 ? 86.373  46.282  14.886 1.00 30.68  ? 120  HIS I CD2 1 
ATOM   9797  C  CE1 . HIS I  1 120 ? 87.201  48.305  14.856 1.00 31.51  ? 120  HIS I CE1 1 
ATOM   9798  N  NE2 . HIS I  1 120 ? 87.202  47.142  14.218 1.00 31.95  ? 120  HIS I NE2 1 
ATOM   9799  N  N   . GLU I  1 121 ? 84.658  47.014  19.992 1.00 29.20  ? 121  GLU I N   1 
ATOM   9800  C  CA  . GLU I  1 121 ? 83.784  47.298  21.121 1.00 30.32  ? 121  GLU I CA  1 
ATOM   9801  C  C   . GLU I  1 121 ? 82.294  47.146  20.818 1.00 30.35  ? 121  GLU I C   1 
ATOM   9802  O  O   . GLU I  1 121 ? 81.563  46.599  21.655 1.00 31.55  ? 121  GLU I O   1 
ATOM   9803  C  CB  . GLU I  1 121 ? 84.089  48.740  21.577 1.00 33.25  ? 121  GLU I CB  1 
ATOM   9804  C  CG  . GLU I  1 121 ? 83.250  49.277  22.721 1.00 43.40  ? 121  GLU I CG  1 
ATOM   9805  C  CD  . GLU I  1 121 ? 83.309  50.789  22.883 1.00 52.13  ? 121  GLU I CD  1 
ATOM   9806  O  OE1 . GLU I  1 121 ? 83.048  51.269  24.009 1.00 56.77  ? 121  GLU I OE1 1 
ATOM   9807  O  OE2 . GLU I  1 121 ? 83.599  51.526  21.912 1.00 43.10  ? 121  GLU I OE2 1 
ATOM   9808  N  N   . LYS I  1 122 ? 81.800  47.633  19.680 1.00 34.27  ? 122  LYS I N   1 
ATOM   9809  C  CA  . LYS I  1 122 ? 80.369  47.600  19.388 1.00 29.27  ? 122  LYS I CA  1 
ATOM   9810  C  C   . LYS I  1 122 ? 80.065  46.847  18.106 1.00 31.37  ? 122  LYS I C   1 
ATOM   9811  O  O   . LYS I  1 122 ? 80.936  46.396  17.367 1.00 34.97  ? 122  LYS I O   1 
ATOM   9812  C  CB  . LYS I  1 122 ? 79.786  49.002  19.167 1.00 35.94  ? 122  LYS I CB  1 
ATOM   9813  C  CG  . LYS I  1 122 ? 80.041  50.083  20.190 1.00 40.62  ? 122  LYS I CG  1 
ATOM   9814  C  CD  . LYS I  1 122 ? 79.567  51.429  19.658 1.00 49.52  ? 122  LYS I CD  1 
ATOM   9815  C  CE  . LYS I  1 122 ? 80.525  52.555  20.003 1.00 55.71  ? 122  LYS I CE  1 
ATOM   9816  N  NZ  . LYS I  1 122 ? 79.933  53.882  19.638 1.00 65.95  ? 122  LYS I NZ  1 
ATOM   9817  N  N   . ALA I  1 123 ? 78.765  46.776  17.819 1.00 30.53  ? 123  ALA I N   1 
ATOM   9818  C  CA  . ALA I  1 123 ? 78.282  46.199  16.571 1.00 29.68  ? 123  ALA I CA  1 
ATOM   9819  C  C   . ALA I  1 123 ? 78.663  47.032  15.358 1.00 29.26  ? 123  ALA I C   1 
ATOM   9820  O  O   . ALA I  1 123 ? 78.686  48.260  15.354 1.00 31.12  ? 123  ALA I O   1 
ATOM   9821  C  CB  . ALA I  1 123 ? 76.757  46.079  16.630 1.00 28.96  ? 123  ALA I CB  1 
ATOM   9822  N  N   . ASP I  1 124 ? 78.941  46.338  14.273 1.00 32.47  ? 124  ASP I N   1 
ATOM   9823  C  CA  . ASP I  1 124 ? 79.142  46.951  12.969 1.00 31.56  ? 124  ASP I CA  1 
ATOM   9824  C  C   . ASP I  1 124 ? 77.770  47.204  12.347 1.00 34.38  ? 124  ASP I C   1 
ATOM   9825  O  O   . ASP I  1 124 ? 77.014  46.235  12.264 1.00 29.34  ? 124  ASP I O   1 
ATOM   9826  C  CB  . ASP I  1 124 ? 79.995  46.000  12.136 1.00 26.71  ? 124  ASP I CB  1 
ATOM   9827  C  CG  . ASP I  1 124 ? 80.356  46.447  10.745 1.00 40.68  ? 124  ASP I CG  1 
ATOM   9828  O  OD1 . ASP I  1 124 ? 81.399  45.982  10.220 1.00 36.13  ? 124  ASP I OD1 1 
ATOM   9829  O  OD2 . ASP I  1 124 ? 79.609  47.252  10.140 1.00 40.37  ? 124  ASP I OD2 1 
ATOM   9830  N  N   . ASP I  1 125 ? 77.407  48.403  11.918 1.00 36.67  ? 125  ASP I N   1 
ATOM   9831  C  CA  . ASP I  1 125 ? 76.079  48.639  11.343 1.00 33.66  ? 125  ASP I CA  1 
ATOM   9832  C  C   . ASP I  1 125 ? 76.051  48.256  9.874  1.00 34.90  ? 125  ASP I C   1 
ATOM   9833  O  O   . ASP I  1 125 ? 75.030  48.484  9.216  1.00 40.80  ? 125  ASP I O   1 
ATOM   9834  C  CB  . ASP I  1 125 ? 75.668  50.102  11.532 1.00 36.05  ? 125  ASP I CB  1 
ATOM   9835  C  CG  . ASP I  1 125 ? 76.559  51.132  10.852 1.00 41.41  ? 125  ASP I CG  1 
ATOM   9836  O  OD1 . ASP I  1 125 ? 76.663  52.258  11.390 1.00 39.74  ? 125  ASP I OD1 1 
ATOM   9837  O  OD2 . ASP I  1 125 ? 77.173  50.851  9.792  1.00 39.09  ? 125  ASP I OD2 1 
ATOM   9838  N  N   . LEU I  1 126 ? 77.144  47.705  9.380  1.00 26.70  ? 126  LEU I N   1 
ATOM   9839  C  CA  . LEU I  1 126 ? 77.313  47.205  8.026  1.00 29.47  ? 126  LEU I CA  1 
ATOM   9840  C  C   . LEU I  1 126 ? 77.172  48.265  6.937  1.00 31.83  ? 126  LEU I C   1 
ATOM   9841  O  O   . LEU I  1 126 ? 76.785  47.925  5.813  1.00 37.35  ? 126  LEU I O   1 
ATOM   9842  C  CB  . LEU I  1 126 ? 76.289  46.091  7.733  1.00 32.63  ? 126  LEU I CB  1 
ATOM   9843  C  CG  . LEU I  1 126 ? 76.210  45.082  8.883  1.00 42.16  ? 126  LEU I CG  1 
ATOM   9844  C  CD1 . LEU I  1 126 ? 75.193  43.995  8.604  1.00 37.43  ? 126  LEU I CD1 1 
ATOM   9845  C  CD2 . LEU I  1 126 ? 77.604  44.506  9.114  1.00 30.99  ? 126  LEU I CD2 1 
ATOM   9846  N  N   . GLY I  1 127 ? 77.504  49.503  7.244  1.00 32.64  ? 127  GLY I N   1 
ATOM   9847  C  CA  . GLY I  1 127 ? 77.560  50.512  6.186  1.00 41.04  ? 127  GLY I CA  1 
ATOM   9848  C  C   . GLY I  1 127 ? 76.164  51.009  5.838  1.00 55.25  ? 127  GLY I C   1 
ATOM   9849  O  O   . GLY I  1 127 ? 75.924  51.475  4.727  1.00 49.85  ? 127  GLY I O   1 
ATOM   9850  N  N   . LYS I  1 128 ? 75.276  50.896  6.814  1.00 54.88  ? 128  LYS I N   1 
ATOM   9851  C  CA  . LYS I  1 128 ? 73.855  51.166  6.659  1.00 53.93  ? 128  LYS I CA  1 
ATOM   9852  C  C   . LYS I  1 128 ? 73.385  52.158  7.704  1.00 55.30  ? 128  LYS I C   1 
ATOM   9853  O  O   . LYS I  1 128 ? 72.210  52.487  7.831  1.00 73.00  ? 128  LYS I O   1 
ATOM   9854  C  CB  . LYS I  1 128 ? 73.096  49.838  6.769  1.00 53.54  ? 128  LYS I CB  1 
ATOM   9855  C  CG  . LYS I  1 128 ? 73.126  49.007  5.499  1.00 63.09  ? 128  LYS I CG  1 
ATOM   9856  C  CD  . LYS I  1 128 ? 73.927  47.728  5.653  1.00 76.54  ? 128  LYS I CD  1 
ATOM   9857  C  CE  . LYS I  1 128 ? 74.382  47.164  4.316  1.00 78.57  ? 128  LYS I CE  1 
ATOM   9858  N  NZ  . LYS I  1 128 ? 73.248  46.620  3.517  1.00 74.37  ? 128  LYS I NZ  1 
ATOM   9859  N  N   . GLY I  1 129 ? 74.346  52.654  8.487  1.00 55.33  ? 129  GLY I N   1 
ATOM   9860  C  CA  . GLY I  1 129 ? 74.033  53.607  9.530  1.00 51.06  ? 129  GLY I CA  1 
ATOM   9861  C  C   . GLY I  1 129 ? 73.547  54.935  8.987  1.00 55.72  ? 129  GLY I C   1 
ATOM   9862  O  O   . GLY I  1 129 ? 73.080  55.793  9.741  1.00 57.94  ? 129  GLY I O   1 
ATOM   9863  N  N   . GLY I  1 130 ? 73.655  55.144  7.671  1.00 54.49  ? 130  GLY I N   1 
ATOM   9864  C  CA  . GLY I  1 130 ? 73.208  56.423  7.139  1.00 64.40  ? 130  GLY I CA  1 
ATOM   9865  C  C   . GLY I  1 130 ? 74.057  57.588  7.607  1.00 68.16  ? 130  GLY I C   1 
ATOM   9866  O  O   . GLY I  1 130 ? 73.557  58.641  8.016  1.00 68.94  ? 130  GLY I O   1 
ATOM   9867  N  N   . ASN I  1 131 ? 75.375  57.409  7.543  1.00 63.50  ? 131  ASN I N   1 
ATOM   9868  C  CA  . ASN I  1 131 ? 76.291  58.495  7.888  1.00 57.07  ? 131  ASN I CA  1 
ATOM   9869  C  C   . ASN I  1 131 ? 77.677  58.157  7.347  1.00 60.48  ? 131  ASN I C   1 
ATOM   9870  O  O   . ASN I  1 131 ? 77.849  57.057  6.818  1.00 62.50  ? 131  ASN I O   1 
ATOM   9871  C  CB  . ASN I  1 131 ? 76.301  58.735  9.389  1.00 55.23  ? 131  ASN I CB  1 
ATOM   9872  C  CG  . ASN I  1 131 ? 76.561  57.454  10.161 1.00 64.42  ? 131  ASN I CG  1 
ATOM   9873  O  OD1 . ASN I  1 131 ? 75.654  56.914  10.787 1.00 82.74  ? 131  ASN I OD1 1 
ATOM   9874  N  ND2 . ASN I  1 131 ? 77.798  56.986  10.105 1.00 43.92  ? 131  ASN I ND2 1 
ATOM   9875  N  N   . GLU I  1 132 ? 78.615  59.088  7.457  1.00 60.66  ? 132  GLU I N   1 
ATOM   9876  C  CA  . GLU I  1 132 ? 79.929  58.951  6.843  1.00 55.63  ? 132  GLU I CA  1 
ATOM   9877  C  C   . GLU I  1 132 ? 80.763  57.860  7.518  1.00 40.73  ? 132  GLU I C   1 
ATOM   9878  O  O   . GLU I  1 132 ? 81.263  56.990  6.798  1.00 50.78  ? 132  GLU I O   1 
ATOM   9879  C  CB  . GLU I  1 132 ? 80.693  60.279  6.857  1.00 67.96  ? 132  GLU I CB  1 
ATOM   9880  C  CG  . GLU I  1 132 ? 80.835  60.914  5.482  1.00 83.76  ? 132  GLU I CG  1 
ATOM   9881  C  CD  . GLU I  1 132 ? 81.726  60.143  4.533  1.00 93.76  ? 132  GLU I CD  1 
ATOM   9882  O  OE1 . GLU I  1 132 ? 81.230  59.232  3.833  1.00 104.42 ? 132  GLU I OE1 1 
ATOM   9883  O  OE2 . GLU I  1 132 ? 82.939  60.448  4.463  1.00 103.86 ? 132  GLU I OE2 1 
ATOM   9884  N  N   . GLU I  1 133 ? 80.901  57.925  8.833  1.00 42.35  ? 133  GLU I N   1 
ATOM   9885  C  CA  . GLU I  1 133 ? 81.605  56.900  9.602  1.00 57.56  ? 133  GLU I CA  1 
ATOM   9886  C  C   . GLU I  1 133 ? 81.091  55.504  9.248  1.00 56.73  ? 133  GLU I C   1 
ATOM   9887  O  O   . GLU I  1 133 ? 81.875  54.571  9.069  1.00 51.42  ? 133  GLU I O   1 
ATOM   9888  C  CB  . GLU I  1 133 ? 81.465  57.145  11.103 1.00 73.75  ? 133  GLU I CB  1 
ATOM   9889  C  CG  . GLU I  1 133 ? 82.484  56.421  11.963 1.00 90.87  ? 133  GLU I CG  1 
ATOM   9890  C  CD  . GLU I  1 133 ? 83.881  57.010  11.937 1.00 96.01  ? 133  GLU I CD  1 
ATOM   9891  O  OE1 . GLU I  1 133 ? 84.043  58.226  12.178 1.00 96.10  ? 133  GLU I OE1 1 
ATOM   9892  O  OE2 . GLU I  1 133 ? 84.840  56.244  11.683 1.00 91.52  ? 133  GLU I OE2 1 
ATOM   9893  N  N   . SER I  1 134 ? 79.770  55.411  9.148  1.00 42.81  ? 134  SER I N   1 
ATOM   9894  C  CA  . SER I  1 134 ? 79.105  54.170  8.776  1.00 43.86  ? 134  SER I CA  1 
ATOM   9895  C  C   . SER I  1 134 ? 79.756  53.615  7.520  1.00 48.91  ? 134  SER I C   1 
ATOM   9896  O  O   . SER I  1 134 ? 79.981  52.411  7.433  1.00 45.69  ? 134  SER I O   1 
ATOM   9897  C  CB  . SER I  1 134 ? 77.613  54.418  8.569  1.00 44.34  ? 134  SER I CB  1 
ATOM   9898  O  OG  . SER I  1 134 ? 76.869  53.231  8.428  1.00 47.34  ? 134  SER I OG  1 
ATOM   9899  N  N   . THR I  1 135 ? 80.060  54.498  6.576  1.00 52.76  ? 135  THR I N   1 
ATOM   9900  C  CA  . THR I  1 135 ? 80.668  54.139  5.294  1.00 49.36  ? 135  THR I CA  1 
ATOM   9901  C  C   . THR I  1 135 ? 82.170  53.862  5.423  1.00 38.50  ? 135  THR I C   1 
ATOM   9902  O  O   . THR I  1 135 ? 82.773  53.307  4.508  1.00 41.52  ? 135  THR I O   1 
ATOM   9903  C  CB  . THR I  1 135 ? 80.432  55.242  4.240  1.00 60.00  ? 135  THR I CB  1 
ATOM   9904  O  OG1 . THR I  1 135 ? 81.489  56.214  4.228  1.00 59.22  ? 135  THR I OG1 1 
ATOM   9905  C  CG2 . THR I  1 135 ? 79.173  56.033  4.581  1.00 51.04  ? 135  THR I CG2 1 
ATOM   9906  N  N   . LYS I  1 136 ? 82.751  54.242  6.552  1.00 38.30  ? 136  LYS I N   1 
ATOM   9907  C  CA  . LYS I  1 136 ? 84.156  53.961  6.816  1.00 50.34  ? 136  LYS I CA  1 
ATOM   9908  C  C   . LYS I  1 136 ? 84.359  52.627  7.543  1.00 50.98  ? 136  LYS I C   1 
ATOM   9909  O  O   . LYS I  1 136 ? 84.971  51.684  7.033  1.00 40.21  ? 136  LYS I O   1 
ATOM   9910  C  CB  . LYS I  1 136 ? 84.778  55.075  7.677  1.00 44.04  ? 136  LYS I CB  1 
ATOM   9911  C  CG  . LYS I  1 136 ? 84.599  56.468  7.092  1.00 64.27  ? 136  LYS I CG  1 
ATOM   9912  C  CD  . LYS I  1 136 ? 85.640  57.450  7.591  1.00 68.92  ? 136  LYS I CD  1 
ATOM   9913  C  CE  . LYS I  1 136 ? 85.121  58.294  8.743  1.00 71.94  ? 136  LYS I CE  1 
ATOM   9914  N  NZ  . LYS I  1 136 ? 86.073  58.316  9.890  1.00 66.01  ? 136  LYS I NZ  1 
ATOM   9915  N  N   . THR I  1 137 ? 83.830  52.625  8.756  1.00 47.68  ? 137  THR I N   1 
ATOM   9916  C  CA  . THR I  1 137 ? 84.025  51.686  9.826  1.00 43.55  ? 137  THR I CA  1 
ATOM   9917  C  C   . THR I  1 137 ? 82.758  51.047  10.368 1.00 47.76  ? 137  THR I C   1 
ATOM   9918  O  O   . THR I  1 137 ? 82.830  50.290  11.347 1.00 48.98  ? 137  THR I O   1 
ATOM   9919  C  CB  . THR I  1 137 ? 84.615  52.416  11.058 1.00 46.68  ? 137  THR I CB  1 
ATOM   9920  O  OG1 . THR I  1 137 ? 83.545  53.226  11.564 1.00 36.50  ? 137  THR I OG1 1 
ATOM   9921  C  CG2 . THR I  1 137 ? 85.768  53.320  10.674 1.00 59.72  ? 137  THR I CG2 1 
ATOM   9922  N  N   . GLY I  1 138 ? 81.591  51.342  9.802  1.00 37.16  ? 138  GLY I N   1 
ATOM   9923  C  CA  . GLY I  1 138 ? 80.396  50.738  10.361 1.00 36.43  ? 138  GLY I CA  1 
ATOM   9924  C  C   . GLY I  1 138 ? 80.113  51.161  11.784 1.00 37.93  ? 138  GLY I C   1 
ATOM   9925  O  O   . GLY I  1 138 ? 79.258  50.530  12.425 1.00 37.11  ? 138  GLY I O   1 
ATOM   9926  N  N   . ASN I  1 139 ? 80.773  52.197  12.299 1.00 32.98  ? 139  ASN I N   1 
ATOM   9927  C  CA  . ASN I  1 139 ? 80.500  52.680  13.655 1.00 28.98  ? 139  ASN I CA  1 
ATOM   9928  C  C   . ASN I  1 139 ? 80.769  51.628  14.726 1.00 41.63  ? 139  ASN I C   1 
ATOM   9929  O  O   . ASN I  1 139 ? 80.204  51.656  15.832 1.00 35.61  ? 139  ASN I O   1 
ATOM   9930  C  CB  . ASN I  1 139 ? 79.044  53.181  13.743 1.00 36.32  ? 139  ASN I CB  1 
ATOM   9931  C  CG  . ASN I  1 139 ? 78.789  54.453  12.950 1.00 40.68  ? 139  ASN I CG  1 
ATOM   9932  O  OD1 . ASN I  1 139 ? 79.102  55.548  13.415 1.00 47.96  ? 139  ASN I OD1 1 
ATOM   9933  N  ND2 . ASN I  1 139 ? 78.236  54.340  11.748 1.00 48.58  ? 139  ASN I ND2 1 
ATOM   9934  N  N   . ALA I  1 140 ? 81.652  50.654  14.477 1.00 41.77  ? 140  ALA I N   1 
ATOM   9935  C  CA  . ALA I  1 140 ? 81.909  49.593  15.453 1.00 40.12  ? 140  ALA I CA  1 
ATOM   9936  C  C   . ALA I  1 140 ? 82.732  50.025  16.659 1.00 38.11  ? 140  ALA I C   1 
ATOM   9937  O  O   . ALA I  1 140 ? 83.029  49.209  17.538 1.00 34.22  ? 140  ALA I O   1 
ATOM   9938  C  CB  . ALA I  1 140 ? 82.635  48.427  14.773 1.00 37.04  ? 140  ALA I CB  1 
ATOM   9939  N  N   . GLY I  1 141 ? 83.124  51.293  16.731 1.00 35.80  ? 141  GLY I N   1 
ATOM   9940  C  CA  . GLY I  1 141 ? 83.851  51.786  17.888 1.00 36.44  ? 141  GLY I CA  1 
ATOM   9941  C  C   . GLY I  1 141 ? 85.263  51.204  17.972 1.00 30.24  ? 141  GLY I C   1 
ATOM   9942  O  O   . GLY I  1 141 ? 85.871  50.893  16.947 1.00 29.51  ? 141  GLY I O   1 
ATOM   9943  N  N   . SER I  1 142 ? 85.700  51.089  19.202 1.00 28.39  ? 142  SER I N   1 
ATOM   9944  C  CA  . SER I  1 142 ? 87.083  50.849  19.587 1.00 40.98  ? 142  SER I CA  1 
ATOM   9945  C  C   . SER I  1 142 ? 87.527  49.408  19.328 1.00 47.36  ? 142  SER I C   1 
ATOM   9946  O  O   . SER I  1 142 ? 86.677  48.519  19.256 1.00 37.36  ? 142  SER I O   1 
ATOM   9947  C  CB  . SER I  1 142 ? 87.267  51.253  21.052 1.00 36.15  ? 142  SER I CB  1 
ATOM   9948  O  OG  . SER I  1 142 ? 87.101  50.186  21.951 1.00 41.96  ? 142  SER I OG  1 
ATOM   9949  N  N   . ARG I  1 143 ? 88.841  49.237  19.178 1.00 33.21  ? 143  ARG I N   1 
ATOM   9950  C  CA  . ARG I  1 143 ? 89.481  47.948  18.922 1.00 33.57  ? 143  ARG I CA  1 
ATOM   9951  C  C   . ARG I  1 143 ? 89.807  47.220  20.213 1.00 39.18  ? 143  ARG I C   1 
ATOM   9952  O  O   . ARG I  1 143 ? 90.698  47.598  20.988 1.00 41.41  ? 143  ARG I O   1 
ATOM   9953  C  CB  . ARG I  1 143 ? 90.729  48.223  18.075 1.00 31.97  ? 143  ARG I CB  1 
ATOM   9954  C  CG  . ARG I  1 143 ? 90.398  49.084  16.857 1.00 38.38  ? 143  ARG I CG  1 
ATOM   9955  C  CD  . ARG I  1 143 ? 91.641  49.487  16.069 1.00 37.58  ? 143  ARG I CD  1 
ATOM   9956  N  NE  . ARG I  1 143 ? 91.300  50.397  14.983 1.00 33.63  ? 143  ARG I NE  1 
ATOM   9957  C  CZ  . ARG I  1 143 ? 91.980  50.707  13.897 1.00 48.04  ? 143  ARG I CZ  1 
ATOM   9958  N  NH1 . ARG I  1 143 ? 91.469  51.582  13.018 1.00 32.78  ? 143  ARG I NH1 1 
ATOM   9959  N  NH2 . ARG I  1 143 ? 93.171  50.176  13.631 1.00 35.12  ? 143  ARG I NH2 1 
ATOM   9960  N  N   . LEU I  1 144 ? 89.114  46.134  20.545 1.00 29.50  ? 144  LEU I N   1 
ATOM   9961  C  CA  . LEU I  1 144 ? 89.287  45.521  21.862 1.00 25.84  ? 144  LEU I CA  1 
ATOM   9962  C  C   . LEU I  1 144 ? 90.433  44.512  21.852 1.00 28.08  ? 144  LEU I C   1 
ATOM   9963  O  O   . LEU I  1 144 ? 91.131  44.283  22.834 1.00 31.23  ? 144  LEU I O   1 
ATOM   9964  C  CB  . LEU I  1 144 ? 88.027  44.792  22.326 1.00 32.06  ? 144  LEU I CB  1 
ATOM   9965  C  CG  . LEU I  1 144 ? 86.768  45.620  22.612 1.00 33.91  ? 144  LEU I CG  1 
ATOM   9966  C  CD1 . LEU I  1 144 ? 85.665  44.729  23.155 1.00 44.46  ? 144  LEU I CD1 1 
ATOM   9967  C  CD2 . LEU I  1 144 ? 87.086  46.751  23.573 1.00 41.43  ? 144  LEU I CD2 1 
ATOM   9968  N  N   . ALA I  1 145 ? 90.626  43.880  20.698 1.00 24.85  ? 145  ALA I N   1 
ATOM   9969  C  CA  . ALA I  1 145 ? 91.723  42.904  20.646 1.00 28.76  ? 145  ALA I CA  1 
ATOM   9970  C  C   . ALA I  1 145 ? 92.067  42.692  19.188 1.00 28.69  ? 145  ALA I C   1 
ATOM   9971  O  O   . ALA I  1 145 ? 91.237  42.950  18.320 1.00 27.25  ? 145  ALA I O   1 
ATOM   9972  C  CB  . ALA I  1 145 ? 91.378  41.613  21.361 1.00 35.27  ? 145  ALA I CB  1 
ATOM   9973  N  N   . CYS I  1 146 ? 93.291  42.247  18.924 1.00 25.94  ? 146  CYS I N   1 
ATOM   9974  C  CA  . CYS I  1 146 ? 93.732  42.139  17.540 1.00 26.25  ? 146  CYS I CA  1 
ATOM   9975  C  C   . CYS I  1 146 ? 94.919  41.197  17.449 1.00 25.26  ? 146  CYS I C   1 
ATOM   9976  O  O   . CYS I  1 146 ? 95.510  40.816  18.471 1.00 27.25  ? 146  CYS I O   1 
ATOM   9977  C  CB  A CYS I  1 146 ? 94.114  43.525  17.012 0.34 30.05  ? 146  CYS I CB  1 
ATOM   9978  C  CB  B CYS I  1 146 ? 94.063  43.538  17.016 0.66 31.04  ? 146  CYS I CB  1 
ATOM   9979  S  SG  A CYS I  1 146 ? 95.250  44.426  18.097 0.34 53.79  ? 146  CYS I SG  1 
ATOM   9980  S  SG  B CYS I  1 146 ? 95.581  44.282  17.641 0.66 34.29  ? 146  CYS I SG  1 
ATOM   9981  N  N   . GLY I  1 147 ? 95.268  40.810  16.230 1.00 24.63  ? 147  GLY I N   1 
ATOM   9982  C  CA  . GLY I  1 147 ? 96.403  39.902  16.077 1.00 24.67  ? 147  GLY I CA  1 
ATOM   9983  C  C   . GLY I  1 147 ? 96.834  39.923  14.628 1.00 26.65  ? 147  GLY I C   1 
ATOM   9984  O  O   . GLY I  1 147 ? 96.020  40.141  13.729 1.00 25.65  ? 147  GLY I O   1 
ATOM   9985  N  N   . VAL I  1 148 ? 98.116  39.683  14.372 1.00 23.37  ? 148  VAL I N   1 
ATOM   9986  C  CA  . VAL I  1 148 ? 98.575  39.573  13.001 1.00 23.56  ? 148  VAL I CA  1 
ATOM   9987  C  C   . VAL I  1 148 ? 98.275  38.186  12.448 1.00 28.00  ? 148  VAL I C   1 
ATOM   9988  O  O   . VAL I  1 148 ? 98.468  37.209  13.164 1.00 29.73  ? 148  VAL I O   1 
ATOM   9989  C  CB  . VAL I  1 148 ? 100.106 39.784  12.908 1.00 32.89  ? 148  VAL I CB  1 
ATOM   9990  C  CG1 . VAL I  1 148 ? 100.523 39.855  11.448 1.00 36.47  ? 148  VAL I CG1 1 
ATOM   9991  C  CG2 . VAL I  1 148 ? 100.518 41.023  13.684 1.00 29.62  ? 148  VAL I CG2 1 
ATOM   9992  N  N   . ILE I  1 149 ? 97.825  38.122  11.198 1.00 26.15  ? 149  ILE I N   1 
ATOM   9993  C  CA  . ILE I  1 149 ? 97.423  36.849  10.622 1.00 26.30  ? 149  ILE I CA  1 
ATOM   9994  C  C   . ILE I  1 149 ? 98.629  36.168  9.999  1.00 29.99  ? 149  ILE I C   1 
ATOM   9995  O  O   . ILE I  1 149 ? 99.260  36.692  9.086  1.00 31.38  ? 149  ILE I O   1 
ATOM   9996  C  CB  . ILE I  1 149 ? 96.289  37.053  9.588  1.00 34.94  ? 149  ILE I CB  1 
ATOM   9997  C  CG1 . ILE I  1 149 ? 95.059  37.750  10.187 1.00 30.38  ? 149  ILE I CG1 1 
ATOM   9998  C  CG2 . ILE I  1 149 ? 95.961  35.730  8.911  1.00 28.23  ? 149  ILE I CG2 1 
ATOM   9999  C  CD1 . ILE I  1 149 ? 93.988  38.142  9.179  1.00 29.08  ? 149  ILE I CD1 1 
ATOM   10000 N  N   . GLY I  1 150 ? 98.935  34.977  10.526 1.00 30.43  ? 150  GLY I N   1 
ATOM   10001 C  CA  . GLY I  1 150 ? 100.157 34.317  10.111 1.00 35.62  ? 150  GLY I CA  1 
ATOM   10002 C  C   . GLY I  1 150 ? 99.934  33.030  9.363  1.00 35.22  ? 150  GLY I C   1 
ATOM   10003 O  O   . GLY I  1 150 ? 98.893  32.390  9.508  1.00 30.83  ? 150  GLY I O   1 
ATOM   10004 N  N   . ILE I  1 151 ? 100.924 32.626  8.569  1.00 32.71  ? 151  ILE I N   1 
ATOM   10005 C  CA  . ILE I  1 151 ? 100.844 31.314  7.904  1.00 34.57  ? 151  ILE I CA  1 
ATOM   10006 C  C   . ILE I  1 151 ? 100.909 30.181  8.910  1.00 33.93  ? 151  ILE I C   1 
ATOM   10007 O  O   . ILE I  1 151 ? 101.659 30.173  9.892  1.00 31.97  ? 151  ILE I O   1 
ATOM   10008 C  CB  . ILE I  1 151 ? 101.965 31.210  6.854  1.00 35.61  ? 151  ILE I CB  1 
ATOM   10009 C  CG1 . ILE I  1 151 ? 101.934 32.400  5.886  1.00 38.85  ? 151  ILE I CG1 1 
ATOM   10010 C  CG2 . ILE I  1 151 ? 101.931 29.884  6.120  1.00 37.43  ? 151  ILE I CG2 1 
ATOM   10011 C  CD1 . ILE I  1 151 ? 103.283 32.864  5.393  1.00 47.74  ? 151  ILE I CD1 1 
ATOM   10012 N  N   . ALA I  1 152 ? 100.066 29.163  8.688  1.00 28.49  ? 152  ALA I N   1 
ATOM   10013 C  CA  . ALA I  1 152 ? 100.011 28.050  9.619  1.00 37.03  ? 152  ALA I CA  1 
ATOM   10014 C  C   . ALA I  1 152 ? 100.305 26.734  8.898  1.00 37.42  ? 152  ALA I C   1 
ATOM   10015 O  O   . ALA I  1 152 ? 100.185 26.637  7.676  1.00 37.67  ? 152  ALA I O   1 
ATOM   10016 C  CB  . ALA I  1 152 ? 98.648  28.005  10.309 1.00 39.85  ? 152  ALA I CB  1 
ATOM   10017 N  N   . GLN I  1 153 ? 100.680 25.720  9.677  1.00 29.38  ? 153  GLN I N   1 
ATOM   10018 C  CA  . GLN I  1 153 ? 100.991 24.431  9.064  1.00 42.74  ? 153  GLN I CA  1 
ATOM   10019 C  C   . GLN I  1 153 ? 99.721  23.786  8.517  1.00 56.48  ? 153  GLN I C   1 
ATOM   10020 O  O   . GLN I  1 153 ? 98.787  23.590  9.330  1.00 61.10  ? 153  GLN I O   1 
ATOM   10021 C  CB  . GLN I  1 153 ? 101.663 23.537  10.098 1.00 40.49  ? 153  GLN I CB  1 
ATOM   10022 C  CG  . GLN I  1 153 ? 102.226 22.247  9.522  1.00 46.79  ? 153  GLN I CG  1 
ATOM   10023 C  CD  . GLN I  1 153 ? 102.728 21.334  10.630 1.00 46.36  ? 153  GLN I CD  1 
ATOM   10024 O  OE1 . GLN I  1 153 ? 103.868 21.482  11.072 1.00 68.31  ? 153  GLN I OE1 1 
ATOM   10025 N  NE2 . GLN I  1 153 ? 101.881 20.408  11.065 1.00 83.43  ? 153  GLN I NE2 1 
ATOM   10026 O  OXT . GLN I  1 153 ? 99.649  23.491  7.306  1.00 58.35  ? 153  GLN I OXT 1 
ATOM   10027 N  N   . ALA J  1 1   ? 109.321 50.039  -2.589 1.00 69.84  ? 1    ALA J N   1 
ATOM   10028 C  CA  . ALA J  1 1   ? 109.823 49.505  -1.332 1.00 64.38  ? 1    ALA J CA  1 
ATOM   10029 C  C   . ALA J  1 1   ? 108.711 48.924  -0.459 1.00 60.54  ? 1    ALA J C   1 
ATOM   10030 O  O   . ALA J  1 1   ? 107.697 49.564  -0.189 1.00 78.74  ? 1    ALA J O   1 
ATOM   10031 C  CB  . ALA J  1 1   ? 110.574 50.572  -0.539 1.00 59.14  ? 1    ALA J CB  1 
ATOM   10032 N  N   . THR J  1 2   ? 108.927 47.698  -0.005 1.00 56.49  ? 2    THR J N   1 
ATOM   10033 C  CA  . THR J  1 2   ? 108.063 47.015  0.947  1.00 41.04  ? 2    THR J CA  1 
ATOM   10034 C  C   . THR J  1 2   ? 108.582 47.298  2.353  1.00 36.31  ? 2    THR J C   1 
ATOM   10035 O  O   . THR J  1 2   ? 109.791 47.449  2.546  1.00 38.63  ? 2    THR J O   1 
ATOM   10036 C  CB  . THR J  1 2   ? 108.014 45.499  0.696  1.00 47.26  ? 2    THR J CB  1 
ATOM   10037 O  OG1 . THR J  1 2   ? 108.713 45.180  -0.517 1.00 61.41  ? 2    THR J OG1 1 
ATOM   10038 C  CG2 . THR J  1 2   ? 106.592 45.008  0.496  1.00 47.62  ? 2    THR J CG2 1 
ATOM   10039 N  N   . LYS J  1 3   ? 107.682 47.374  3.306  1.00 36.76  ? 3    LYS J N   1 
ATOM   10040 C  CA  . LYS J  1 3   ? 107.941 47.538  4.721  1.00 32.68  ? 3    LYS J CA  1 
ATOM   10041 C  C   . LYS J  1 3   ? 107.180 46.483  5.532  1.00 36.15  ? 3    LYS J C   1 
ATOM   10042 O  O   . LYS J  1 3   ? 106.041 46.162  5.209  1.00 33.85  ? 3    LYS J O   1 
ATOM   10043 C  CB  . LYS J  1 3   ? 107.532 48.928  5.190  1.00 37.65  ? 3    LYS J CB  1 
ATOM   10044 C  CG  . LYS J  1 3   ? 108.330 50.066  4.554  1.00 42.25  ? 3    LYS J CG  1 
ATOM   10045 C  CD  . LYS J  1 3   ? 108.165 51.328  5.385  1.00 48.69  ? 3    LYS J CD  1 
ATOM   10046 C  CE  . LYS J  1 3   ? 109.270 51.453  6.423  1.00 70.43  ? 3    LYS J CE  1 
ATOM   10047 N  NZ  . LYS J  1 3   ? 108.782 52.040  7.708  1.00 91.69  ? 3    LYS J NZ  1 
ATOM   10048 N  N   . ALA J  1 4   ? 107.820 45.972  6.573  1.00 39.73  ? 4    ALA J N   1 
ATOM   10049 C  CA  . ALA J  1 4   ? 107.250 44.996  7.496  1.00 31.01  ? 4    ALA J CA  1 
ATOM   10050 C  C   . ALA J  1 4   ? 107.638 45.378  8.916  1.00 32.00  ? 4    ALA J C   1 
ATOM   10051 O  O   . ALA J  1 4   ? 108.478 46.250  9.184  1.00 32.34  ? 4    ALA J O   1 
ATOM   10052 C  CB  . ALA J  1 4   ? 107.678 43.581  7.108  1.00 27.53  ? 4    ALA J CB  1 
ATOM   10053 N  N   . VAL J  1 5   ? 107.003 44.723  9.886  1.00 29.43  ? 5    VAL J N   1 
ATOM   10054 C  CA  . VAL J  1 5   ? 107.246 45.084  11.285 1.00 26.73  ? 5    VAL J CA  1 
ATOM   10055 C  C   . VAL J  1 5   ? 106.825 43.908  12.155 1.00 30.26  ? 5    VAL J C   1 
ATOM   10056 O  O   . VAL J  1 5   ? 105.929 43.137  11.793 1.00 32.95  ? 5    VAL J O   1 
ATOM   10057 C  CB  . VAL J  1 5   ? 106.488 46.352  11.685 1.00 29.62  ? 5    VAL J CB  1 
ATOM   10058 C  CG1 . VAL J  1 5   ? 104.984 46.048  11.630 1.00 33.01  ? 5    VAL J CG1 1 
ATOM   10059 C  CG2 . VAL J  1 5   ? 106.893 46.854  13.048 1.00 24.32  ? 5    VAL J CG2 1 
ATOM   10060 N  N   . CYS J  1 6   ? 107.491 43.773  13.286 1.00 27.74  ? 6    CYS J N   1 
ATOM   10061 C  CA  . CYS J  1 6   ? 107.278 42.664  14.196 1.00 26.26  ? 6    CYS J CA  1 
ATOM   10062 C  C   . CYS J  1 6   ? 107.394 43.132  15.639 1.00 28.85  ? 6    CYS J C   1 
ATOM   10063 O  O   . CYS J  1 6   ? 108.338 43.786  16.077 1.00 30.59  ? 6    CYS J O   1 
ATOM   10064 C  CB  . CYS J  1 6   ? 108.277 41.538  13.928 1.00 25.08  ? 6    CYS J CB  1 
ATOM   10065 S  SG  . CYS J  1 6   ? 108.040 40.085  14.982 1.00 36.63  ? 6    CYS J SG  1 
ATOM   10066 N  N   . VAL J  1 7   ? 106.362 42.780  16.414 1.00 23.58  ? 7    VAL J N   1 
ATOM   10067 C  CA  . VAL J  1 7   ? 106.387 43.078  17.839 1.00 27.34  ? 7    VAL J CA  1 
ATOM   10068 C  C   . VAL J  1 7   ? 106.730 41.797  18.584 1.00 35.36  ? 7    VAL J C   1 
ATOM   10069 O  O   . VAL J  1 7   ? 106.007 40.799  18.523 1.00 30.81  ? 7    VAL J O   1 
ATOM   10070 C  CB  . VAL J  1 7   ? 105.038 43.655  18.297 1.00 27.73  ? 7    VAL J CB  1 
ATOM   10071 C  CG1 . VAL J  1 7   ? 105.008 43.759  19.810 1.00 26.67  ? 7    VAL J CG1 1 
ATOM   10072 C  CG2 . VAL J  1 7   ? 104.810 45.016  17.637 1.00 28.28  ? 7    VAL J CG2 1 
ATOM   10073 N  N   . LEU J  1 8   ? 107.864 41.764  19.285 1.00 27.38  ? 8    LEU J N   1 
ATOM   10074 C  CA  . LEU J  1 8   ? 108.226 40.516  19.947 1.00 31.78  ? 8    LEU J CA  1 
ATOM   10075 C  C   . LEU J  1 8   ? 107.756 40.485  21.390 1.00 29.98  ? 8    LEU J C   1 
ATOM   10076 O  O   . LEU J  1 8   ? 107.986 41.448  22.117 1.00 30.44  ? 8    LEU J O   1 
ATOM   10077 C  CB  . LEU J  1 8   ? 109.757 40.341  19.926 1.00 25.18  ? 8    LEU J CB  1 
ATOM   10078 C  CG  . LEU J  1 8   ? 110.355 40.359  18.518 1.00 27.46  ? 8    LEU J CG  1 
ATOM   10079 C  CD1 . LEU J  1 8   ? 111.850 40.622  18.583 1.00 38.04  ? 8    LEU J CD1 1 
ATOM   10080 C  CD2 . LEU J  1 8   ? 110.039 39.026  17.862 1.00 44.07  ? 8    LEU J CD2 1 
ATOM   10081 N  N   . LYS J  1 9   ? 107.107 39.409  21.792 1.00 28.36  ? 9    LYS J N   1 
ATOM   10082 C  CA  . LYS J  1 9   ? 106.602 39.224  23.147 1.00 32.72  ? 9    LYS J CA  1 
ATOM   10083 C  C   . LYS J  1 9   ? 106.748 37.770  23.575 1.00 31.01  ? 9    LYS J C   1 
ATOM   10084 O  O   . LYS J  1 9   ? 106.746 36.871  22.723 1.00 28.95  ? 9    LYS J O   1 
ATOM   10085 C  CB  . LYS J  1 9   ? 105.127 39.613  23.247 1.00 40.23  ? 9    LYS J CB  1 
ATOM   10086 C  CG  . LYS J  1 9   ? 104.748 40.951  22.651 1.00 47.87  ? 9    LYS J CG  1 
ATOM   10087 C  CD  . LYS J  1 9   ? 104.857 42.061  23.680 1.00 62.89  ? 9    LYS J CD  1 
ATOM   10088 C  CE  . LYS J  1 9   ? 104.640 43.439  23.071 1.00 66.86  ? 9    LYS J CE  1 
ATOM   10089 N  NZ  . LYS J  1 9   ? 103.246 43.621  22.572 1.00 60.65  ? 9    LYS J NZ  1 
ATOM   10090 N  N   . GLY J  1 10  ? 106.886 37.499  24.863 1.00 27.05  ? 10   GLY J N   1 
ATOM   10091 C  CA  . GLY J  1 10  ? 106.947 36.107  25.294 1.00 36.28  ? 10   GLY J CA  1 
ATOM   10092 C  C   . GLY J  1 10  ? 106.373 35.928  26.693 1.00 43.48  ? 10   GLY J C   1 
ATOM   10093 O  O   . GLY J  1 10  ? 105.659 36.817  27.158 1.00 37.19  ? 10   GLY J O   1 
ATOM   10094 N  N   . ASP J  1 11  ? 106.692 34.819  27.334 1.00 40.36  ? 11   ASP J N   1 
ATOM   10095 C  CA  . ASP J  1 11  ? 106.386 34.583  28.734 1.00 57.30  ? 11   ASP J CA  1 
ATOM   10096 C  C   . ASP J  1 11  ? 106.949 35.710  29.603 1.00 56.43  ? 11   ASP J C   1 
ATOM   10097 O  O   . ASP J  1 11  ? 106.218 36.499  30.185 1.00 68.46  ? 11   ASP J O   1 
ATOM   10098 C  CB  . ASP J  1 11  ? 107.007 33.294  29.268 1.00 67.06  ? 11   ASP J CB  1 
ATOM   10099 C  CG  . ASP J  1 11  ? 106.168 32.056  29.068 1.00 86.52  ? 11   ASP J CG  1 
ATOM   10100 O  OD1 . ASP J  1 11  ? 105.083 32.167  28.458 1.00 107.02 ? 11   ASP J OD1 1 
ATOM   10101 O  OD2 . ASP J  1 11  ? 106.604 30.972  29.525 1.00 116.14 ? 11   ASP J OD2 1 
ATOM   10102 N  N   . GLY J  1 12  ? 108.280 35.721  29.652 1.00 41.61  ? 12   GLY J N   1 
ATOM   10103 C  CA  . GLY J  1 12  ? 109.022 36.578  30.542 1.00 39.71  ? 12   GLY J CA  1 
ATOM   10104 C  C   . GLY J  1 12  ? 109.094 38.034  30.166 1.00 40.92  ? 12   GLY J C   1 
ATOM   10105 O  O   . GLY J  1 12  ? 108.221 38.572  29.485 1.00 48.37  ? 12   GLY J O   1 
ATOM   10106 N  N   . PRO J  1 13  ? 110.154 38.693  30.634 1.00 42.20  ? 13   PRO J N   1 
ATOM   10107 C  CA  . PRO J  1 13  ? 110.339 40.124  30.402 1.00 41.07  ? 13   PRO J CA  1 
ATOM   10108 C  C   . PRO J  1 13  ? 110.866 40.484  29.024 1.00 40.05  ? 13   PRO J C   1 
ATOM   10109 O  O   . PRO J  1 13  ? 110.964 41.680  28.735 1.00 34.76  ? 13   PRO J O   1 
ATOM   10110 C  CB  . PRO J  1 13  ? 111.413 40.503  31.433 1.00 43.66  ? 13   PRO J CB  1 
ATOM   10111 C  CG  . PRO J  1 13  ? 112.192 39.248  31.635 1.00 43.24  ? 13   PRO J CG  1 
ATOM   10112 C  CD  . PRO J  1 13  ? 111.231 38.102  31.446 1.00 37.51  ? 13   PRO J CD  1 
ATOM   10113 N  N   . VAL J  1 14  ? 111.215 39.516  28.172 1.00 36.54  ? 14   VAL J N   1 
ATOM   10114 C  CA  . VAL J  1 14  ? 111.828 39.910  26.894 1.00 31.34  ? 14   VAL J CA  1 
ATOM   10115 C  C   . VAL J  1 14  ? 110.798 40.479  25.940 1.00 36.43  ? 14   VAL J C   1 
ATOM   10116 O  O   . VAL J  1 14  ? 109.763 39.864  25.619 1.00 32.65  ? 14   VAL J O   1 
ATOM   10117 C  CB  . VAL J  1 14  ? 112.552 38.689  26.281 1.00 31.30  ? 14   VAL J CB  1 
ATOM   10118 C  CG1 . VAL J  1 14  ? 113.054 39.026  24.885 1.00 34.05  ? 14   VAL J CG1 1 
ATOM   10119 C  CG2 . VAL J  1 14  ? 113.699 38.225  27.171 1.00 26.21  ? 14   VAL J CG2 1 
ATOM   10120 N  N   . GLN J  1 15  ? 111.039 41.692  25.436 1.00 28.04  ? 15   GLN J N   1 
ATOM   10121 C  CA  . GLN J  1 15  ? 110.147 42.220  24.410 1.00 28.18  ? 15   GLN J CA  1 
ATOM   10122 C  C   . GLN J  1 15  ? 110.838 43.287  23.566 1.00 32.51  ? 15   GLN J C   1 
ATOM   10123 O  O   . GLN J  1 15  ? 111.874 43.785  24.000 1.00 32.64  ? 15   GLN J O   1 
ATOM   10124 C  CB  . GLN J  1 15  ? 108.896 42.815  25.057 1.00 46.62  ? 15   GLN J CB  1 
ATOM   10125 C  CG  . GLN J  1 15  ? 109.073 44.259  25.504 1.00 59.40  ? 15   GLN J CG  1 
ATOM   10126 C  CD  . GLN J  1 15  ? 107.875 44.717  26.325 1.00 73.25  ? 15   GLN J CD  1 
ATOM   10127 O  OE1 . GLN J  1 15  ? 106.894 45.208  25.762 1.00 75.03  ? 15   GLN J OE1 1 
ATOM   10128 N  NE2 . GLN J  1 15  ? 107.981 44.536  27.641 1.00 55.05  ? 15   GLN J NE2 1 
ATOM   10129 N  N   . GLY J  1 16  ? 110.254 43.621  22.412 1.00 35.68  ? 16   GLY J N   1 
ATOM   10130 C  CA  . GLY J  1 16  ? 110.850 44.631  21.554 1.00 33.79  ? 16   GLY J CA  1 
ATOM   10131 C  C   . GLY J  1 16  ? 110.171 44.796  20.223 1.00 36.21  ? 16   GLY J C   1 
ATOM   10132 O  O   . GLY J  1 16  ? 109.154 44.175  19.912 1.00 33.80  ? 16   GLY J O   1 
ATOM   10133 N  N   . ILE J  1 17  ? 110.699 45.662  19.361 1.00 28.40  ? 17   ILE J N   1 
ATOM   10134 C  CA  . ILE J  1 17  ? 110.063 45.914  18.084 1.00 24.83  ? 17   ILE J CA  1 
ATOM   10135 C  C   . ILE J  1 17  ? 111.093 45.873  16.969 1.00 31.24  ? 17   ILE J C   1 
ATOM   10136 O  O   . ILE J  1 17  ? 112.141 46.500  17.156 1.00 31.33  ? 17   ILE J O   1 
ATOM   10137 C  CB  . ILE J  1 17  ? 109.380 47.296  18.125 1.00 31.64  ? 17   ILE J CB  1 
ATOM   10138 C  CG1 . ILE J  1 17  ? 108.246 47.356  19.155 1.00 37.49  ? 17   ILE J CG1 1 
ATOM   10139 C  CG2 . ILE J  1 17  ? 108.895 47.723  16.760 1.00 28.60  ? 17   ILE J CG2 1 
ATOM   10140 C  CD1 . ILE J  1 17  ? 107.762 48.778  19.351 1.00 39.25  ? 17   ILE J CD1 1 
ATOM   10141 N  N   . ILE J  1 18  ? 110.786 45.160  15.887 1.00 28.43  ? 18   ILE J N   1 
ATOM   10142 C  CA  . ILE J  1 18  ? 111.741 45.042  14.788 1.00 27.68  ? 18   ILE J CA  1 
ATOM   10143 C  C   . ILE J  1 18  ? 111.104 45.415  13.461 1.00 32.87  ? 18   ILE J C   1 
ATOM   10144 O  O   . ILE J  1 18  ? 110.044 44.879  13.131 1.00 31.64  ? 18   ILE J O   1 
ATOM   10145 C  CB  . ILE J  1 18  ? 112.296 43.607  14.720 1.00 29.07  ? 18   ILE J CB  1 
ATOM   10146 C  CG1 . ILE J  1 18  ? 113.005 43.193  16.020 1.00 26.65  ? 18   ILE J CG1 1 
ATOM   10147 C  CG2 . ILE J  1 18  ? 113.192 43.410  13.505 1.00 25.51  ? 18   ILE J CG2 1 
ATOM   10148 C  CD1 . ILE J  1 18  ? 114.357 43.873  16.156 1.00 37.34  ? 18   ILE J CD1 1 
ATOM   10149 N  N   . ASN J  1 19  ? 111.759 46.316  12.735 1.00 34.73  ? 19   ASN J N   1 
ATOM   10150 C  CA  . ASN J  1 19  ? 111.341 46.779  11.420 1.00 27.67  ? 19   ASN J CA  1 
ATOM   10151 C  C   . ASN J  1 19  ? 112.148 46.167  10.294 1.00 29.38  ? 19   ASN J C   1 
ATOM   10152 O  O   . ASN J  1 19  ? 113.319 45.803  10.387 1.00 29.65  ? 19   ASN J O   1 
ATOM   10153 C  CB  . ASN J  1 19  ? 111.464 48.309  11.300 1.00 31.49  ? 19   ASN J CB  1 
ATOM   10154 C  CG  . ASN J  1 19  ? 110.889 49.009  12.515 1.00 39.12  ? 19   ASN J CG  1 
ATOM   10155 O  OD1 . ASN J  1 19  ? 109.674 49.217  12.594 1.00 33.12  ? 19   ASN J OD1 1 
ATOM   10156 N  ND2 . ASN J  1 19  ? 111.745 49.364  13.467 1.00 34.32  ? 19   ASN J ND2 1 
ATOM   10157 N  N   . PHE J  1 20  ? 111.464 46.059  9.165  1.00 25.38  ? 20   PHE J N   1 
ATOM   10158 C  CA  . PHE J  1 20  ? 112.053 45.516  7.960  1.00 24.45  ? 20   PHE J CA  1 
ATOM   10159 C  C   . PHE J  1 20  ? 111.784 46.482  6.810  1.00 33.07  ? 20   PHE J C   1 
ATOM   10160 O  O   . PHE J  1 20  ? 110.674 47.015  6.719  1.00 32.68  ? 20   PHE J O   1 
ATOM   10161 C  CB  . PHE J  1 20  ? 111.478 44.157  7.574  1.00 25.59  ? 20   PHE J CB  1 
ATOM   10162 C  CG  . PHE J  1 20  ? 111.576 43.052  8.604  1.00 26.36  ? 20   PHE J CG  1 
ATOM   10163 C  CD1 . PHE J  1 20  ? 112.521 42.046  8.434  1.00 29.17  ? 20   PHE J CD1 1 
ATOM   10164 C  CD2 . PHE J  1 20  ? 110.749 43.025  9.717  1.00 32.43  ? 20   PHE J CD2 1 
ATOM   10165 C  CE1 . PHE J  1 20  ? 112.609 41.024  9.361  1.00 27.14  ? 20   PHE J CE1 1 
ATOM   10166 C  CE2 . PHE J  1 20  ? 110.831 41.999  10.646 1.00 26.87  ? 20   PHE J CE2 1 
ATOM   10167 C  CZ  . PHE J  1 20  ? 111.786 41.017  10.475 1.00 28.19  ? 20   PHE J CZ  1 
ATOM   10168 N  N   . GLU J  1 21  ? 112.782 46.672  5.957  1.00 35.11  ? 21   GLU J N   1 
ATOM   10169 C  CA  . GLU J  1 21  ? 112.576 47.500  4.767  1.00 30.71  ? 21   GLU J CA  1 
ATOM   10170 C  C   . GLU J  1 21  ? 113.275 46.881  3.571  1.00 35.17  ? 21   GLU J C   1 
ATOM   10171 O  O   . GLU J  1 21  ? 114.443 46.473  3.681  1.00 37.98  ? 21   GLU J O   1 
ATOM   10172 C  CB  . GLU J  1 21  ? 113.071 48.923  5.049  1.00 33.99  ? 21   GLU J CB  1 
ATOM   10173 C  CG  . GLU J  1 21  ? 112.623 49.934  4.008  1.00 48.58  ? 21   GLU J CG  1 
ATOM   10174 C  CD  . GLU J  1 21  ? 113.146 51.344  4.177  1.00 50.87  ? 21   GLU J CD  1 
ATOM   10175 O  OE1 . GLU J  1 21  ? 112.905 52.163  3.254  1.00 78.99  ? 21   GLU J OE1 1 
ATOM   10176 O  OE2 . GLU J  1 21  ? 113.790 51.678  5.191  1.00 53.31  ? 21   GLU J OE2 1 
ATOM   10177 N  N   . GLN J  1 22  ? 112.611 46.788  2.427  1.00 32.80  ? 22   GLN J N   1 
ATOM   10178 C  CA  . GLN J  1 22  ? 113.284 46.318  1.205  1.00 35.92  ? 22   GLN J CA  1 
ATOM   10179 C  C   . GLN J  1 22  ? 112.907 47.271  0.063  1.00 51.15  ? 22   GLN J C   1 
ATOM   10180 O  O   . GLN J  1 22  ? 111.758 47.307  -0.397 1.00 40.13  ? 22   GLN J O   1 
ATOM   10181 C  CB  . GLN J  1 22  ? 112.938 44.882  0.892  1.00 29.58  ? 22   GLN J CB  1 
ATOM   10182 C  CG  . GLN J  1 22  ? 113.628 44.160  -0.234 1.00 35.55  ? 22   GLN J CG  1 
ATOM   10183 C  CD  . GLN J  1 22  ? 113.016 42.803  -0.521 1.00 34.25  ? 22   GLN J CD  1 
ATOM   10184 O  OE1 . GLN J  1 22  ? 111.816 42.617  -0.302 1.00 42.59  ? 22   GLN J OE1 1 
ATOM   10185 N  NE2 . GLN J  1 22  ? 113.794 41.836  -1.013 1.00 31.97  ? 22   GLN J NE2 1 
ATOM   10186 N  N   . LYS J  1 23  ? 113.892 48.049  -0.380 1.00 52.61  ? 23   LYS J N   1 
ATOM   10187 C  CA  . LYS J  1 23  ? 113.691 49.064  -1.410 1.00 62.94  ? 23   LYS J CA  1 
ATOM   10188 C  C   . LYS J  1 23  ? 113.537 48.482  -2.810 1.00 55.33  ? 23   LYS J C   1 
ATOM   10189 O  O   . LYS J  1 23  ? 112.713 48.931  -3.608 1.00 58.90  ? 23   LYS J O   1 
ATOM   10190 C  CB  . LYS J  1 23  ? 114.867 50.048  -1.376 1.00 79.70  ? 23   LYS J CB  1 
ATOM   10191 C  CG  . LYS J  1 23  ? 114.686 51.154  -0.344 1.00 97.66  ? 23   LYS J CG  1 
ATOM   10192 C  CD  . LYS J  1 23  ? 115.706 51.060  0.778  1.00 106.84 ? 23   LYS J CD  1 
ATOM   10193 C  CE  . LYS J  1 23  ? 115.406 52.059  1.889  1.00 108.38 ? 23   LYS J CE  1 
ATOM   10194 N  NZ  . LYS J  1 23  ? 115.963 51.616  3.201  1.00 112.53 ? 23   LYS J NZ  1 
ATOM   10195 N  N   . GLU J  1 24  ? 114.331 47.469  -3.107 1.00 54.97  ? 24   GLU J N   1 
ATOM   10196 C  CA  . GLU J  1 24  ? 114.406 46.854  -4.420 1.00 70.75  ? 24   GLU J CA  1 
ATOM   10197 C  C   . GLU J  1 24  ? 113.721 45.491  -4.397 1.00 68.96  ? 24   GLU J C   1 
ATOM   10198 O  O   . GLU J  1 24  ? 113.880 44.765  -3.416 1.00 55.85  ? 24   GLU J O   1 
ATOM   10199 C  CB  . GLU J  1 24  ? 115.865 46.718  -4.861 1.00 81.70  ? 24   GLU J CB  1 
ATOM   10200 C  CG  . GLU J  1 24  ? 116.794 47.746  -4.228 1.00 92.67  ? 24   GLU J CG  1 
ATOM   10201 C  CD  . GLU J  1 24  ? 117.934 47.153  -3.426 1.00 94.37  ? 24   GLU J CD  1 
ATOM   10202 O  OE1 . GLU J  1 24  ? 118.271 45.971  -3.652 1.00 109.20 ? 24   GLU J OE1 1 
ATOM   10203 O  OE2 . GLU J  1 24  ? 118.503 47.856  -2.553 1.00 56.04  ? 24   GLU J OE2 1 
ATOM   10204 N  N   . SER J  1 25  ? 112.987 45.198  -5.459 1.00 67.71  ? 25   SER J N   1 
ATOM   10205 C  CA  . SER J  1 25  ? 112.198 43.986  -5.598 1.00 74.31  ? 25   SER J CA  1 
ATOM   10206 C  C   . SER J  1 25  ? 112.955 42.755  -5.132 1.00 65.81  ? 25   SER J C   1 
ATOM   10207 O  O   . SER J  1 25  ? 112.496 41.978  -4.293 1.00 71.91  ? 25   SER J O   1 
ATOM   10208 C  CB  . SER J  1 25  ? 111.766 43.790  -7.057 1.00 80.44  ? 25   SER J CB  1 
ATOM   10209 O  OG  . SER J  1 25  ? 111.399 45.031  -7.641 1.00 83.93  ? 25   SER J OG  1 
ATOM   10210 N  N   . ASN J  1 26  ? 114.154 42.543  -5.676 1.00 60.19  ? 26   ASN J N   1 
ATOM   10211 C  CA  . ASN J  1 26  ? 114.855 41.341  -5.211 1.00 64.97  ? 26   ASN J CA  1 
ATOM   10212 C  C   . ASN J  1 26  ? 116.032 41.701  -4.314 1.00 55.90  ? 26   ASN J C   1 
ATOM   10213 O  O   . ASN J  1 26  ? 116.932 40.872  -4.172 1.00 52.50  ? 26   ASN J O   1 
ATOM   10214 C  CB  . ASN J  1 26  ? 115.337 40.530  -6.410 1.00 73.06  ? 26   ASN J CB  1 
ATOM   10215 C  CG  . ASN J  1 26  ? 114.623 39.204  -6.556 1.00 79.44  ? 26   ASN J CG  1 
ATOM   10216 O  OD1 . ASN J  1 26  ? 113.533 39.014  -6.016 1.00 90.83  ? 26   ASN J OD1 1 
ATOM   10217 N  ND2 . ASN J  1 26  ? 115.235 38.282  -7.290 1.00 99.59  ? 26   ASN J ND2 1 
ATOM   10218 N  N   . GLY J  1 27  ? 116.020 42.902  -3.748 1.00 46.31  ? 27   GLY J N   1 
ATOM   10219 C  CA  . GLY J  1 27  ? 117.136 43.485  -3.055 1.00 41.66  ? 27   GLY J CA  1 
ATOM   10220 C  C   . GLY J  1 27  ? 117.342 43.137  -1.605 1.00 45.17  ? 27   GLY J C   1 
ATOM   10221 O  O   . GLY J  1 27  ? 116.578 42.428  -0.947 1.00 39.92  ? 27   GLY J O   1 
ATOM   10222 N  N   . PRO J  1 28  ? 118.423 43.643  -1.016 1.00 44.36  ? 28   PRO J N   1 
ATOM   10223 C  CA  . PRO J  1 28  ? 118.667 43.379  0.408  1.00 38.66  ? 28   PRO J CA  1 
ATOM   10224 C  C   . PRO J  1 28  ? 117.533 43.927  1.270  1.00 42.33  ? 28   PRO J C   1 
ATOM   10225 O  O   . PRO J  1 28  ? 116.807 44.835  0.853  1.00 47.06  ? 28   PRO J O   1 
ATOM   10226 C  CB  . PRO J  1 28  ? 119.956 44.150  0.693  1.00 41.10  ? 28   PRO J CB  1 
ATOM   10227 C  CG  . PRO J  1 28  ? 119.965 45.206  -0.380 1.00 45.78  ? 28   PRO J CG  1 
ATOM   10228 C  CD  . PRO J  1 28  ? 119.477 44.489  -1.613 1.00 42.99  ? 28   PRO J CD  1 
ATOM   10229 N  N   . VAL J  1 29  ? 117.394 43.375  2.465  1.00 33.69  ? 29   VAL J N   1 
ATOM   10230 C  CA  . VAL J  1 29  ? 116.438 43.841  3.459  1.00 27.67  ? 29   VAL J CA  1 
ATOM   10231 C  C   . VAL J  1 29  ? 117.169 44.359  4.687  1.00 34.65  ? 29   VAL J C   1 
ATOM   10232 O  O   . VAL J  1 29  ? 118.043 43.658  5.202  1.00 31.06  ? 29   VAL J O   1 
ATOM   10233 C  CB  . VAL J  1 29  ? 115.487 42.697  3.872  1.00 28.16  ? 29   VAL J CB  1 
ATOM   10234 C  CG1 . VAL J  1 29  ? 114.515 43.153  4.942  1.00 27.14  ? 29   VAL J CG1 1 
ATOM   10235 C  CG2 . VAL J  1 29  ? 114.712 42.167  2.675  1.00 31.68  ? 29   VAL J CG2 1 
ATOM   10236 N  N   . LYS J  1 30  ? 116.833 45.553  5.150  1.00 28.48  ? 30   LYS J N   1 
ATOM   10237 C  CA  . LYS J  1 30  ? 117.327 46.100  6.394  1.00 30.09  ? 30   LYS J CA  1 
ATOM   10238 C  C   . LYS J  1 30  ? 116.384 45.669  7.519  1.00 36.78  ? 30   LYS J C   1 
ATOM   10239 O  O   . LYS J  1 30  ? 115.161 45.732  7.375  1.00 31.77  ? 30   LYS J O   1 
ATOM   10240 C  CB  . LYS J  1 30  ? 117.427 47.632  6.389  1.00 32.98  ? 30   LYS J CB  1 
ATOM   10241 C  CG  . LYS J  1 30  ? 118.151 48.156  5.157  1.00 54.55  ? 30   LYS J CG  1 
ATOM   10242 C  CD  . LYS J  1 30  ? 118.074 49.672  5.019  1.00 66.65  ? 30   LYS J CD  1 
ATOM   10243 C  CE  . LYS J  1 30  ? 119.147 50.150  4.044  1.00 74.37  ? 30   LYS J CE  1 
ATOM   10244 N  NZ  . LYS J  1 30  ? 118.933 51.555  3.603  1.00 88.43  ? 30   LYS J NZ  1 
ATOM   10245 N  N   . VAL J  1 31  ? 117.000 45.245  8.607  1.00 26.53  ? 31   VAL J N   1 
ATOM   10246 C  CA  . VAL J  1 31  ? 116.268 44.756  9.767  1.00 28.40  ? 31   VAL J CA  1 
ATOM   10247 C  C   . VAL J  1 31  ? 116.722 45.537  10.969 1.00 28.17  ? 31   VAL J C   1 
ATOM   10248 O  O   . VAL J  1 31  ? 117.915 45.447  11.292 1.00 29.70  ? 31   VAL J O   1 
ATOM   10249 C  CB  . VAL J  1 31  ? 116.575 43.257  9.983  1.00 27.42  ? 31   VAL J CB  1 
ATOM   10250 C  CG1 . VAL J  1 31  ? 115.836 42.682  11.174 1.00 27.28  ? 31   VAL J CG1 1 
ATOM   10251 C  CG2 . VAL J  1 31  ? 116.249 42.507  8.698  1.00 26.94  ? 31   VAL J CG2 1 
ATOM   10252 N  N   . TRP J  1 32  ? 115.865 46.303  11.628 1.00 23.28  ? 32   TRP J N   1 
ATOM   10253 C  CA  . TRP J  1 32  ? 116.376 47.090  12.735 1.00 27.89  ? 32   TRP J CA  1 
ATOM   10254 C  C   . TRP J  1 32  ? 115.278 47.358  13.761 1.00 31.00  ? 32   TRP J C   1 
ATOM   10255 O  O   . TRP J  1 32  ? 114.083 47.296  13.486 1.00 34.52  ? 32   TRP J O   1 
ATOM   10256 C  CB  . TRP J  1 32  ? 116.972 48.425  12.269 1.00 31.99  ? 32   TRP J CB  1 
ATOM   10257 C  CG  . TRP J  1 32  ? 115.936 49.486  12.030 1.00 38.75  ? 32   TRP J CG  1 
ATOM   10258 C  CD1 . TRP J  1 32  ? 115.542 50.508  12.838 1.00 38.21  ? 32   TRP J CD1 1 
ATOM   10259 C  CD2 . TRP J  1 32  ? 115.148 49.598  10.834 1.00 38.60  ? 32   TRP J CD2 1 
ATOM   10260 N  NE1 . TRP J  1 32  ? 114.558 51.250  12.225 1.00 41.74  ? 32   TRP J NE1 1 
ATOM   10261 C  CE2 . TRP J  1 32  ? 114.297 50.713  10.994 1.00 37.97  ? 32   TRP J CE2 1 
ATOM   10262 C  CE3 . TRP J  1 32  ? 115.093 48.855  9.655  1.00 32.94  ? 32   TRP J CE3 1 
ATOM   10263 C  CZ2 . TRP J  1 32  ? 113.393 51.104  10.008 1.00 35.96  ? 32   TRP J CZ2 1 
ATOM   10264 C  CZ3 . TRP J  1 32  ? 114.194 49.248  8.679  1.00 37.32  ? 32   TRP J CZ3 1 
ATOM   10265 C  CH2 . TRP J  1 32  ? 113.364 50.359  8.867  1.00 39.39  ? 32   TRP J CH2 1 
ATOM   10266 N  N   . GLY J  1 33  ? 115.760 47.645  14.962 1.00 28.84  ? 33   GLY J N   1 
ATOM   10267 C  CA  . GLY J  1 33  ? 114.900 47.960  16.084 1.00 25.31  ? 33   GLY J CA  1 
ATOM   10268 C  C   . GLY J  1 33  ? 115.617 47.682  17.379 1.00 28.78  ? 33   GLY J C   1 
ATOM   10269 O  O   . GLY J  1 33  ? 116.840 47.791  17.488 1.00 31.10  ? 33   GLY J O   1 
ATOM   10270 N  N   . SER J  1 34  ? 114.853 47.312  18.402 1.00 26.41  ? 34   SER J N   1 
ATOM   10271 C  CA  . SER J  1 34  ? 115.437 47.126  19.711 1.00 23.45  ? 34   SER J CA  1 
ATOM   10272 C  C   . SER J  1 34  ? 114.684 46.045  20.478 1.00 33.34  ? 34   SER J C   1 
ATOM   10273 O  O   . SER J  1 34  ? 113.473 45.911  20.301 1.00 34.08  ? 34   SER J O   1 
ATOM   10274 C  CB  . SER J  1 34  ? 115.384 48.439  20.501 1.00 33.29  ? 34   SER J CB  1 
ATOM   10275 O  OG  . SER J  1 34  ? 116.142 48.340  21.691 1.00 47.34  ? 34   SER J OG  1 
ATOM   10276 N  N   . ILE J  1 35  ? 115.416 45.323  21.317 1.00 27.90  ? 35   ILE J N   1 
ATOM   10277 C  CA  . ILE J  1 35  ? 114.810 44.325  22.184 1.00 30.75  ? 35   ILE J CA  1 
ATOM   10278 C  C   . ILE J  1 35  ? 115.281 44.564  23.603 1.00 33.39  ? 35   ILE J C   1 
ATOM   10279 O  O   . ILE J  1 35  ? 116.460 44.838  23.840 1.00 36.04  ? 35   ILE J O   1 
ATOM   10280 C  CB  . ILE J  1 35  ? 115.137 42.897  21.720 1.00 28.03  ? 35   ILE J CB  1 
ATOM   10281 C  CG1 . ILE J  1 35  ? 114.822 42.634  20.239 1.00 31.00  ? 35   ILE J CG1 1 
ATOM   10282 C  CG2 . ILE J  1 35  ? 114.426 41.863  22.587 1.00 27.61  ? 35   ILE J CG2 1 
ATOM   10283 C  CD1 . ILE J  1 35  ? 115.293 41.277  19.756 1.00 33.39  ? 35   ILE J CD1 1 
ATOM   10284 N  N   . LYS J  1 36  ? 114.372 44.479  24.572 1.00 29.92  ? 36   LYS J N   1 
ATOM   10285 C  CA  . LYS J  1 36  ? 114.845 44.683  25.950 1.00 32.57  ? 36   LYS J CA  1 
ATOM   10286 C  C   . LYS J  1 36  ? 114.510 43.501  26.840 1.00 32.61  ? 36   LYS J C   1 
ATOM   10287 O  O   . LYS J  1 36  ? 113.733 42.631  26.444 1.00 32.69  ? 36   LYS J O   1 
ATOM   10288 C  CB  . LYS J  1 36  ? 114.252 45.977  26.523 1.00 34.05  ? 36   LYS J CB  1 
ATOM   10289 C  CG  . LYS J  1 36  ? 112.733 46.004  26.505 1.00 38.58  ? 36   LYS J CG  1 
ATOM   10290 C  CD  . LYS J  1 36  ? 112.200 46.806  27.690 1.00 44.79  ? 36   LYS J CD  1 
ATOM   10291 C  CE  . LYS J  1 36  ? 110.681 46.825  27.687 1.00 50.04  ? 36   LYS J CE  1 
ATOM   10292 N  NZ  . LYS J  1 36  ? 110.128 48.183  27.421 1.00 72.65  ? 36   LYS J NZ  1 
ATOM   10293 N  N   . GLY J  1 37  ? 115.108 43.465  28.027 1.00 30.53  ? 37   GLY J N   1 
ATOM   10294 C  CA  . GLY J  1 37  ? 114.884 42.408  28.985 1.00 32.67  ? 37   GLY J CA  1 
ATOM   10295 C  C   . GLY J  1 37  ? 115.704 41.157  28.792 1.00 30.46  ? 37   GLY J C   1 
ATOM   10296 O  O   . GLY J  1 37  ? 115.457 40.130  29.419 1.00 30.33  ? 37   GLY J O   1 
ATOM   10297 N  N   . LEU J  1 38  ? 116.718 41.225  27.930 1.00 32.29  ? 38   LEU J N   1 
ATOM   10298 C  CA  . LEU J  1 38  ? 117.601 40.108  27.653 1.00 31.87  ? 38   LEU J CA  1 
ATOM   10299 C  C   . LEU J  1 38  ? 118.767 39.953  28.607 1.00 36.84  ? 38   LEU J C   1 
ATOM   10300 O  O   . LEU J  1 38  ? 119.172 40.921  29.243 1.00 35.39  ? 38   LEU J O   1 
ATOM   10301 C  CB  . LEU J  1 38  ? 118.168 40.347  26.245 1.00 31.87  ? 38   LEU J CB  1 
ATOM   10302 C  CG  . LEU J  1 38  ? 117.142 40.150  25.113 1.00 29.00  ? 38   LEU J CG  1 
ATOM   10303 C  CD1 . LEU J  1 38  ? 117.747 40.708  23.831 1.00 34.68  ? 38   LEU J CD1 1 
ATOM   10304 C  CD2 . LEU J  1 38  ? 116.755 38.692  25.000 1.00 24.51  ? 38   LEU J CD2 1 
ATOM   10305 N  N   . THR J  1 39  ? 119.373 38.769  28.731 1.00 30.07  ? 39   THR J N   1 
ATOM   10306 C  CA  . THR J  1 39  ? 120.630 38.744  29.486 1.00 40.07  ? 39   THR J CA  1 
ATOM   10307 C  C   . THR J  1 39  ? 121.740 39.293  28.586 1.00 40.77  ? 39   THR J C   1 
ATOM   10308 O  O   . THR J  1 39  ? 121.648 39.156  27.367 1.00 35.94  ? 39   THR J O   1 
ATOM   10309 C  CB  . THR J  1 39  ? 121.072 37.358  29.969 1.00 46.66  ? 39   THR J CB  1 
ATOM   10310 O  OG1 . THR J  1 39  ? 121.192 36.476  28.836 1.00 40.21  ? 39   THR J OG1 1 
ATOM   10311 C  CG2 . THR J  1 39  ? 120.039 36.763  30.919 1.00 44.81  ? 39   THR J CG2 1 
ATOM   10312 N  N   . GLU J  1 40  ? 122.749 39.899  29.181 1.00 32.07  ? 40   GLU J N   1 
ATOM   10313 C  CA  . GLU J  1 40  ? 123.847 40.479  28.419 1.00 33.16  ? 40   GLU J CA  1 
ATOM   10314 C  C   . GLU J  1 40  ? 124.503 39.439  27.525 1.00 27.62  ? 40   GLU J C   1 
ATOM   10315 O  O   . GLU J  1 40  ? 124.736 38.303  27.937 1.00 34.73  ? 40   GLU J O   1 
ATOM   10316 C  CB  . GLU J  1 40  ? 124.864 41.082  29.395 1.00 36.77  ? 40   GLU J CB  1 
ATOM   10317 C  CG  . GLU J  1 40  ? 125.989 41.822  28.702 1.00 40.84  ? 40   GLU J CG  1 
ATOM   10318 C  CD  . GLU J  1 40  ? 126.948 42.449  29.701 1.00 60.87  ? 40   GLU J CD  1 
ATOM   10319 O  OE1 . GLU J  1 40  ? 127.930 43.071  29.237 1.00 95.85  ? 40   GLU J OE1 1 
ATOM   10320 O  OE2 . GLU J  1 40  ? 126.733 42.329  30.927 1.00 50.15  ? 40   GLU J OE2 1 
ATOM   10321 N  N   . GLY J  1 41  ? 124.796 39.822  26.278 1.00 31.76  ? 41   GLY J N   1 
ATOM   10322 C  CA  . GLY J  1 41  ? 125.495 38.888  25.410 1.00 29.82  ? 41   GLY J CA  1 
ATOM   10323 C  C   . GLY J  1 41  ? 124.707 38.544  24.159 1.00 28.44  ? 41   GLY J C   1 
ATOM   10324 O  O   . GLY J  1 41  ? 123.747 39.231  23.830 1.00 27.36  ? 41   GLY J O   1 
ATOM   10325 N  N   . LEU J  1 42  ? 125.159 37.488  23.490 1.00 28.32  ? 42   LEU J N   1 
ATOM   10326 C  CA  . LEU J  1 42  ? 124.576 37.062  22.230 1.00 30.02  ? 42   LEU J CA  1 
ATOM   10327 C  C   . LEU J  1 42  ? 123.301 36.231  22.378 1.00 29.03  ? 42   LEU J C   1 
ATOM   10328 O  O   . LEU J  1 42  ? 123.258 35.357  23.244 1.00 32.59  ? 42   LEU J O   1 
ATOM   10329 C  CB  . LEU J  1 42  ? 125.586 36.176  21.488 1.00 31.10  ? 42   LEU J CB  1 
ATOM   10330 C  CG  . LEU J  1 42  ? 126.857 36.847  20.977 1.00 31.25  ? 42   LEU J CG  1 
ATOM   10331 C  CD1 . LEU J  1 42  ? 127.797 35.767  20.439 1.00 28.39  ? 42   LEU J CD1 1 
ATOM   10332 C  CD2 . LEU J  1 42  ? 126.519 37.913  19.938 1.00 30.79  ? 42   LEU J CD2 1 
ATOM   10333 N  N   . HIS J  1 43  ? 122.330 36.468  21.511 1.00 24.52  ? 43   HIS J N   1 
ATOM   10334 C  CA  . HIS J  1 43  ? 121.096 35.690  21.452 1.00 20.73  ? 43   HIS J CA  1 
ATOM   10335 C  C   . HIS J  1 43  ? 120.761 35.355  19.999 1.00 23.27  ? 43   HIS J C   1 
ATOM   10336 O  O   . HIS J  1 43  ? 120.747 36.249  19.153 1.00 22.08  ? 43   HIS J O   1 
ATOM   10337 C  CB  . HIS J  1 43  ? 119.917 36.464  22.071 1.00 24.34  ? 43   HIS J CB  1 
ATOM   10338 C  CG  . HIS J  1 43  ? 120.168 36.709  23.535 1.00 29.35  ? 43   HIS J CG  1 
ATOM   10339 N  ND1 . HIS J  1 43  ? 119.706 35.867  24.517 1.00 33.73  ? 43   HIS J ND1 1 
ATOM   10340 C  CD2 . HIS J  1 43  ? 120.859 37.689  24.163 1.00 27.93  ? 43   HIS J CD2 1 
ATOM   10341 C  CE1 . HIS J  1 43  ? 120.089 36.325  25.694 1.00 29.92  ? 43   HIS J CE1 1 
ATOM   10342 N  NE2 . HIS J  1 43  ? 120.791 37.436  25.520 1.00 29.01  ? 43   HIS J NE2 1 
ATOM   10343 N  N   . GLY J  1 44  ? 120.469 34.098  19.701 1.00 24.49  ? 44   GLY J N   1 
ATOM   10344 C  CA  . GLY J  1 44  ? 120.157 33.706  18.319 1.00 23.67  ? 44   GLY J CA  1 
ATOM   10345 C  C   . GLY J  1 44  ? 118.902 34.428  17.849 1.00 24.00  ? 44   GLY J C   1 
ATOM   10346 O  O   . GLY J  1 44  ? 118.022 34.749  18.641 1.00 22.68  ? 44   GLY J O   1 
ATOM   10347 N  N   . PHE J  1 45  ? 118.778 34.664  16.557 1.00 20.59  ? 45   PHE J N   1 
ATOM   10348 C  CA  . PHE J  1 45  ? 117.718 35.499  16.005 1.00 23.19  ? 45   PHE J CA  1 
ATOM   10349 C  C   . PHE J  1 45  ? 117.315 34.995  14.632 1.00 28.49  ? 45   PHE J C   1 
ATOM   10350 O  O   . PHE J  1 45  ? 118.163 35.065  13.731 1.00 23.63  ? 45   PHE J O   1 
ATOM   10351 C  CB  . PHE J  1 45  ? 118.307 36.897  15.902 1.00 23.80  ? 45   PHE J CB  1 
ATOM   10352 C  CG  . PHE J  1 45  ? 117.418 38.052  15.570 1.00 23.46  ? 45   PHE J CG  1 
ATOM   10353 C  CD1 . PHE J  1 45  ? 116.364 38.378  16.407 1.00 25.44  ? 45   PHE J CD1 1 
ATOM   10354 C  CD2 . PHE J  1 45  ? 117.656 38.806  14.431 1.00 26.43  ? 45   PHE J CD2 1 
ATOM   10355 C  CE1 . PHE J  1 45  ? 115.573 39.482  16.107 1.00 27.76  ? 45   PHE J CE1 1 
ATOM   10356 C  CE2 . PHE J  1 45  ? 116.868 39.913  14.132 1.00 26.98  ? 45   PHE J CE2 1 
ATOM   10357 C  CZ  . PHE J  1 45  ? 115.820 40.236  14.980 1.00 26.49  ? 45   PHE J CZ  1 
ATOM   10358 N  N   . HIS J  1 46  ? 116.109 34.442  14.437 1.00 20.08  ? 46   HIS J N   1 
ATOM   10359 C  CA  . HIS J  1 46  ? 115.813 33.784  13.169 1.00 21.05  ? 46   HIS J CA  1 
ATOM   10360 C  C   . HIS J  1 46  ? 114.348 33.995  12.785 1.00 20.95  ? 46   HIS J C   1 
ATOM   10361 O  O   . HIS J  1 46  ? 113.514 34.196  13.662 1.00 22.70  ? 46   HIS J O   1 
ATOM   10362 C  CB  . HIS J  1 46  ? 116.029 32.262  13.171 1.00 20.68  ? 46   HIS J CB  1 
ATOM   10363 C  CG  . HIS J  1 46  ? 117.146 31.777  14.035 1.00 26.12  ? 46   HIS J CG  1 
ATOM   10364 N  ND1 . HIS J  1 46  ? 116.963 31.292  15.317 1.00 23.04  ? 46   HIS J ND1 1 
ATOM   10365 C  CD2 . HIS J  1 46  ? 118.478 31.769  13.798 1.00 21.04  ? 46   HIS J CD2 1 
ATOM   10366 C  CE1 . HIS J  1 46  ? 118.142 30.971  15.822 1.00 29.52  ? 46   HIS J CE1 1 
ATOM   10367 N  NE2 . HIS J  1 46  ? 119.083 31.251  14.921 1.00 23.25  ? 46   HIS J NE2 1 
ATOM   10368 N  N   . VAL J  1 47  ? 114.074 33.885  11.499 1.00 24.28  ? 47   VAL J N   1 
ATOM   10369 C  CA  . VAL J  1 47  ? 112.687 33.738  11.032 1.00 24.00  ? 47   VAL J CA  1 
ATOM   10370 C  C   . VAL J  1 47  ? 112.327 32.260  11.044 1.00 21.45  ? 47   VAL J C   1 
ATOM   10371 O  O   . VAL J  1 47  ? 113.043 31.437  10.468 1.00 21.56  ? 47   VAL J O   1 
ATOM   10372 C  CB  . VAL J  1 47  ? 112.497 34.306  9.616  1.00 30.06  ? 47   VAL J CB  1 
ATOM   10373 C  CG1 . VAL J  1 47  ? 111.050 34.116  9.163  1.00 24.76  ? 47   VAL J CG1 1 
ATOM   10374 C  CG2 . VAL J  1 47  ? 112.903 35.779  9.580  1.00 26.00  ? 47   VAL J CG2 1 
ATOM   10375 N  N   . HIS J  1 48  ? 111.240 31.920  11.728 1.00 23.73  ? 48   HIS J N   1 
ATOM   10376 C  CA  . HIS J  1 48  ? 110.745 30.542  11.795 1.00 22.10  ? 48   HIS J CA  1 
ATOM   10377 C  C   . HIS J  1 48  ? 109.567 30.375  10.844 1.00 26.41  ? 48   HIS J C   1 
ATOM   10378 O  O   . HIS J  1 48  ? 108.919 31.345  10.426 1.00 27.09  ? 48   HIS J O   1 
ATOM   10379 C  CB  . HIS J  1 48  ? 110.351 30.196  13.232 1.00 18.88  ? 48   HIS J CB  1 
ATOM   10380 C  CG  . HIS J  1 48  ? 111.508 29.972  14.159 1.00 24.16  ? 48   HIS J CG  1 
ATOM   10381 N  ND1 . HIS J  1 48  ? 111.717 28.774  14.791 1.00 26.73  ? 48   HIS J ND1 1 
ATOM   10382 C  CD2 . HIS J  1 48  ? 112.540 30.779  14.564 1.00 23.47  ? 48   HIS J CD2 1 
ATOM   10383 C  CE1 . HIS J  1 48  ? 112.810 28.828  15.544 1.00 27.52  ? 48   HIS J CE1 1 
ATOM   10384 N  NE2 . HIS J  1 48  ? 113.317 30.037  15.425 1.00 24.47  ? 48   HIS J NE2 1 
ATOM   10385 N  N   . GLU J  1 49  ? 109.262 29.146  10.472 1.00 26.68  ? 49   GLU J N   1 
ATOM   10386 C  CA  . GLU J  1 49  ? 108.372 28.870  9.360  1.00 27.46  ? 49   GLU J CA  1 
ATOM   10387 C  C   . GLU J  1 49  ? 106.948 29.377  9.521  1.00 28.62  ? 49   GLU J C   1 
ATOM   10388 O  O   . GLU J  1 49  ? 106.357 29.877  8.556  1.00 27.82  ? 49   GLU J O   1 
ATOM   10389 C  CB  . GLU J  1 49  ? 108.310 27.339  9.183  1.00 25.20  ? 49   GLU J CB  1 
ATOM   10390 C  CG  . GLU J  1 49  ? 107.730 26.994  7.821  1.00 34.53  ? 49   GLU J CG  1 
ATOM   10391 C  CD  . GLU J  1 49  ? 107.673 25.505  7.550  1.00 39.05  ? 49   GLU J CD  1 
ATOM   10392 O  OE1 . GLU J  1 49  ? 107.078 25.152  6.509  1.00 40.57  ? 49   GLU J OE1 1 
ATOM   10393 O  OE2 . GLU J  1 49  ? 108.210 24.712  8.348  1.00 34.64  ? 49   GLU J OE2 1 
ATOM   10394 N  N   . PHE J  1 50  ? 106.383 29.210  10.717 1.00 24.59  ? 50   PHE J N   1 
ATOM   10395 C  CA  . PHE J  1 50  ? 104.943 29.437  10.846 1.00 33.20  ? 50   PHE J CA  1 
ATOM   10396 C  C   . PHE J  1 50  ? 104.577 30.668  11.651 1.00 30.40  ? 50   PHE J C   1 
ATOM   10397 O  O   . PHE J  1 50  ? 105.134 30.863  12.726 1.00 28.63  ? 50   PHE J O   1 
ATOM   10398 C  CB  . PHE J  1 50  ? 104.292 28.207  11.515 1.00 30.80  ? 50   PHE J CB  1 
ATOM   10399 C  CG  . PHE J  1 50  ? 104.525 26.918  10.741 1.00 31.45  ? 50   PHE J CG  1 
ATOM   10400 C  CD1 . PHE J  1 50  ? 104.095 26.816  9.422  1.00 38.68  ? 50   PHE J CD1 1 
ATOM   10401 C  CD2 . PHE J  1 50  ? 105.155 25.839  11.332 1.00 27.31  ? 50   PHE J CD2 1 
ATOM   10402 C  CE1 . PHE J  1 50  ? 104.320 25.639  8.721  1.00 40.27  ? 50   PHE J CE1 1 
ATOM   10403 C  CE2 . PHE J  1 50  ? 105.411 24.677  10.632 1.00 24.82  ? 50   PHE J CE2 1 
ATOM   10404 C  CZ  . PHE J  1 50  ? 104.994 24.598  9.316  1.00 33.33  ? 50   PHE J CZ  1 
ATOM   10405 N  N   . GLY J  1 51  ? 103.646 31.491  11.168 1.00 27.11  ? 51   GLY J N   1 
ATOM   10406 C  CA  . GLY J  1 51  ? 103.177 32.636  11.934 1.00 26.60  ? 51   GLY J CA  1 
ATOM   10407 C  C   . GLY J  1 51  ? 102.082 32.241  12.921 1.00 30.81  ? 51   GLY J C   1 
ATOM   10408 O  O   . GLY J  1 51  ? 101.019 32.856  13.022 1.00 33.94  ? 51   GLY J O   1 
ATOM   10409 N  N   . ASP J  1 52  ? 102.345 31.184  13.657 1.00 27.19  ? 52   ASP J N   1 
ATOM   10410 C  CA  . ASP J  1 52  ? 101.408 30.553  14.566 1.00 24.62  ? 52   ASP J CA  1 
ATOM   10411 C  C   . ASP J  1 52  ? 101.823 30.726  16.007 1.00 27.82  ? 52   ASP J C   1 
ATOM   10412 O  O   . ASP J  1 52  ? 102.748 30.081  16.495 1.00 29.23  ? 52   ASP J O   1 
ATOM   10413 C  CB  . ASP J  1 52  ? 101.345 29.040  14.294 1.00 30.64  ? 52   ASP J CB  1 
ATOM   10414 C  CG  . ASP J  1 52  ? 100.289 28.308  15.097 1.00 34.46  ? 52   ASP J CG  1 
ATOM   10415 O  OD1 . ASP J  1 52  ? 99.802  27.298  14.532 1.00 32.99  ? 52   ASP J OD1 1 
ATOM   10416 O  OD2 . ASP J  1 52  ? 99.944  28.690  16.239 1.00 27.82  ? 52   ASP J OD2 1 
ATOM   10417 N  N   . ASN J  1 53  ? 101.083 31.551  16.731 1.00 26.79  ? 53   ASN J N   1 
ATOM   10418 C  CA  . ASN J  1 53  ? 101.462 31.717  18.133 1.00 25.83  ? 53   ASN J CA  1 
ATOM   10419 C  C   . ASN J  1 53  ? 100.468 31.056  19.066 1.00 31.20  ? 53   ASN J C   1 
ATOM   10420 O  O   . ASN J  1 53  ? 100.409 31.434  20.242 1.00 31.75  ? 53   ASN J O   1 
ATOM   10421 C  CB  . ASN J  1 53  ? 101.575 33.235  18.354 1.00 30.22  ? 53   ASN J CB  1 
ATOM   10422 C  CG  . ASN J  1 53  ? 102.112 33.591  19.719 1.00 38.54  ? 53   ASN J CG  1 
ATOM   10423 O  OD1 . ASN J  1 53  ? 101.467 34.342  20.453 1.00 52.33  ? 53   ASN J OD1 1 
ATOM   10424 N  ND2 . ASN J  1 53  ? 103.280 33.053  20.058 1.00 40.91  ? 53   ASN J ND2 1 
ATOM   10425 N  N   . THR J  1 54  ? 99.687  30.086  18.596 1.00 29.02  ? 54   THR J N   1 
ATOM   10426 C  CA  . THR J  1 54  ? 98.628  29.508  19.429 1.00 33.29  ? 54   THR J CA  1 
ATOM   10427 C  C   . THR J  1 54  ? 99.173  28.840  20.686 1.00 42.27  ? 54   THR J C   1 
ATOM   10428 O  O   . THR J  1 54  ? 98.443  28.837  21.677 1.00 39.07  ? 54   THR J O   1 
ATOM   10429 C  CB  . THR J  1 54  ? 97.767  28.482  18.662 1.00 32.82  ? 54   THR J CB  1 
ATOM   10430 O  OG1 . THR J  1 54  ? 98.599  27.500  18.044 1.00 32.28  ? 54   THR J OG1 1 
ATOM   10431 C  CG2 . THR J  1 54  ? 97.030  29.180  17.530 1.00 36.49  ? 54   THR J CG2 1 
ATOM   10432 N  N   . ALA J  1 55  ? 100.394 28.316  20.619 1.00 37.72  ? 55   ALA J N   1 
ATOM   10433 C  CA  . ALA J  1 55  ? 101.039 27.672  21.756 1.00 39.01  ? 55   ALA J CA  1 
ATOM   10434 C  C   . ALA J  1 55  ? 102.228 28.489  22.242 1.00 41.94  ? 55   ALA J C   1 
ATOM   10435 O  O   . ALA J  1 55  ? 103.148 27.955  22.858 1.00 49.16  ? 55   ALA J O   1 
ATOM   10436 C  CB  . ALA J  1 55  ? 101.501 26.264  21.397 1.00 42.33  ? 55   ALA J CB  1 
ATOM   10437 N  N   . GLY J  1 56  ? 102.213 29.795  21.950 1.00 34.10  ? 56   GLY J N   1 
ATOM   10438 C  CA  . GLY J  1 56  ? 103.396 30.583  22.318 1.00 28.06  ? 56   GLY J CA  1 
ATOM   10439 C  C   . GLY J  1 56  ? 104.456 30.368  21.244 1.00 29.62  ? 56   GLY J C   1 
ATOM   10440 O  O   . GLY J  1 56  ? 104.121 29.875  20.164 1.00 29.66  ? 56   GLY J O   1 
ATOM   10441 N  N   . CYS J  1 57  ? 105.706 30.726  21.521 1.00 25.62  ? 57   CYS J N   1 
ATOM   10442 C  CA  . CYS J  1 57  ? 106.709 30.639  20.439 1.00 29.36  ? 57   CYS J CA  1 
ATOM   10443 C  C   . CYS J  1 57  ? 106.945 29.234  19.928 1.00 30.92  ? 57   CYS J C   1 
ATOM   10444 O  O   . CYS J  1 57  ? 107.437 29.018  18.818 1.00 29.08  ? 57   CYS J O   1 
ATOM   10445 C  CB  A CYS J  1 57  ? 108.041 31.160  20.993 0.43 29.96  ? 57   CYS J CB  1 
ATOM   10446 C  CB  B CYS J  1 57  ? 108.004 31.307  20.899 0.57 37.04  ? 57   CYS J CB  1 
ATOM   10447 S  SG  A CYS J  1 57  ? 108.056 32.918  21.392 0.43 42.50  ? 57   CYS J SG  1 
ATOM   10448 S  SG  B CYS J  1 57  ? 107.799 32.932  21.652 0.57 35.50  ? 57   CYS J SG  1 
ATOM   10449 N  N   . THR J  1 58  ? 106.592 28.205  20.696 1.00 28.16  ? 58   THR J N   1 
ATOM   10450 C  CA  . THR J  1 58  ? 106.724 26.832  20.234 1.00 26.96  ? 58   THR J CA  1 
ATOM   10451 C  C   . THR J  1 58  ? 105.994 26.538  18.941 1.00 28.67  ? 58   THR J C   1 
ATOM   10452 O  O   . THR J  1 58  ? 106.484 25.739  18.134 1.00 34.46  ? 58   THR J O   1 
ATOM   10453 C  CB  . THR J  1 58  ? 106.147 25.859  21.295 1.00 36.70  ? 58   THR J CB  1 
ATOM   10454 O  OG1 . THR J  1 58  ? 106.787 26.132  22.548 1.00 40.87  ? 58   THR J OG1 1 
ATOM   10455 C  CG2 . THR J  1 58  ? 106.449 24.433  20.874 1.00 38.16  ? 58   THR J CG2 1 
ATOM   10456 N  N   . SER J  1 59  ? 104.814 27.128  18.724 1.00 27.91  ? 59   SER J N   1 
ATOM   10457 C  CA  . SER J  1 59  ? 104.066 26.728  17.532 1.00 27.91  ? 59   SER J CA  1 
ATOM   10458 C  C   . SER J  1 59  ? 104.585 27.389  16.281 1.00 25.03  ? 59   SER J C   1 
ATOM   10459 O  O   . SER J  1 59  ? 104.054 27.152  15.197 1.00 27.71  ? 59   SER J O   1 
ATOM   10460 C  CB  . SER J  1 59  ? 102.557 27.026  17.647 1.00 31.51  ? 59   SER J CB  1 
ATOM   10461 O  OG  . SER J  1 59  ? 102.245 27.779  18.788 1.00 34.80  ? 59   SER J OG  1 
ATOM   10462 N  N   . ALA J  1 60  ? 105.638 28.212  16.377 1.00 24.44  ? 60   ALA J N   1 
ATOM   10463 C  CA  . ALA J  1 60  ? 106.186 28.811  15.162 1.00 24.24  ? 60   ALA J CA  1 
ATOM   10464 C  C   . ALA J  1 60  ? 106.982 27.841  14.305 1.00 27.38  ? 60   ALA J C   1 
ATOM   10465 O  O   . ALA J  1 60  ? 107.402 28.207  13.204 1.00 26.54  ? 60   ALA J O   1 
ATOM   10466 C  CB  . ALA J  1 60  ? 107.082 29.988  15.548 1.00 24.66  ? 60   ALA J CB  1 
ATOM   10467 N  N   . GLY J  1 61  ? 107.208 26.601  14.757 1.00 28.68  ? 61   GLY J N   1 
ATOM   10468 C  CA  . GLY J  1 61  ? 107.873 25.634  13.880 1.00 23.92  ? 61   GLY J CA  1 
ATOM   10469 C  C   . GLY J  1 61  ? 109.378 25.908  13.804 1.00 25.03  ? 61   GLY J C   1 
ATOM   10470 O  O   . GLY J  1 61  ? 109.907 26.722  14.565 1.00 25.55  ? 61   GLY J O   1 
ATOM   10471 N  N   . PRO J  1 62  ? 110.024 25.200  12.884 1.00 25.85  ? 62   PRO J N   1 
ATOM   10472 C  CA  . PRO J  1 62  ? 111.490 25.271  12.778 1.00 23.56  ? 62   PRO J CA  1 
ATOM   10473 C  C   . PRO J  1 62  ? 111.950 26.518  12.036 1.00 27.52  ? 62   PRO J C   1 
ATOM   10474 O  O   . PRO J  1 62  ? 111.137 27.353  11.626 1.00 28.95  ? 62   PRO J O   1 
ATOM   10475 C  CB  . PRO J  1 62  ? 111.805 24.009  11.974 1.00 29.10  ? 62   PRO J CB  1 
ATOM   10476 C  CG  . PRO J  1 62  ? 110.622 23.850  11.076 1.00 27.75  ? 62   PRO J CG  1 
ATOM   10477 C  CD  . PRO J  1 62  ? 109.426 24.290  11.891 1.00 27.38  ? 62   PRO J CD  1 
ATOM   10478 N  N   . HIS J  1 63  ? 113.272 26.672  11.858 1.00 23.51  ? 63   HIS J N   1 
ATOM   10479 C  CA  . HIS J  1 63  ? 113.724 27.817  11.084 1.00 22.49  ? 63   HIS J CA  1 
ATOM   10480 C  C   . HIS J  1 63  ? 113.131 27.796  9.676  1.00 22.94  ? 63   HIS J C   1 
ATOM   10481 O  O   . HIS J  1 63  ? 113.011 26.690  9.161  1.00 25.84  ? 63   HIS J O   1 
ATOM   10482 C  CB  . HIS J  1 63  ? 115.265 27.824  10.967 1.00 26.55  ? 63   HIS J CB  1 
ATOM   10483 C  CG  . HIS J  1 63  ? 115.947 27.977  12.290 1.00 26.25  ? 63   HIS J CG  1 
ATOM   10484 N  ND1 . HIS J  1 63  ? 117.317 27.990  12.464 1.00 25.46  ? 63   HIS J ND1 1 
ATOM   10485 C  CD2 . HIS J  1 63  ? 115.398 28.116  13.530 1.00 27.00  ? 63   HIS J CD2 1 
ATOM   10486 C  CE1 . HIS J  1 63  ? 117.576 28.136  13.755 1.00 26.35  ? 63   HIS J CE1 1 
ATOM   10487 N  NE2 . HIS J  1 63  ? 116.426 28.213  14.426 1.00 29.12  ? 63   HIS J NE2 1 
ATOM   10488 N  N   . PHE J  1 64  ? 112.805 28.925  9.081  1.00 23.81  ? 64   PHE J N   1 
ATOM   10489 C  CA  . PHE J  1 64  ? 112.279 28.983  7.715  1.00 23.64  ? 64   PHE J CA  1 
ATOM   10490 C  C   . PHE J  1 64  ? 113.336 28.495  6.736  1.00 25.58  ? 64   PHE J C   1 
ATOM   10491 O  O   . PHE J  1 64  ? 114.449 29.020  6.657  1.00 24.47  ? 64   PHE J O   1 
ATOM   10492 C  CB  . PHE J  1 64  ? 111.827 30.414  7.442  1.00 25.26  ? 64   PHE J CB  1 
ATOM   10493 C  CG  . PHE J  1 64  ? 111.210 30.607  6.062  1.00 32.46  ? 64   PHE J CG  1 
ATOM   10494 C  CD1 . PHE J  1 64  ? 111.546 31.703  5.292  1.00 32.85  ? 64   PHE J CD1 1 
ATOM   10495 C  CD2 . PHE J  1 64  ? 110.297 29.692  5.559  1.00 33.38  ? 64   PHE J CD2 1 
ATOM   10496 C  CE1 . PHE J  1 64  ? 111.004 31.928  4.030  1.00 30.67  ? 64   PHE J CE1 1 
ATOM   10497 C  CE2 . PHE J  1 64  ? 109.752 29.906  4.295  1.00 31.67  ? 64   PHE J CE2 1 
ATOM   10498 C  CZ  . PHE J  1 64  ? 110.092 31.002  3.540  1.00 28.29  ? 64   PHE J CZ  1 
ATOM   10499 N  N   . ASN J  1 65  ? 113.027 27.437  5.986  1.00 31.77  ? 65   ASN J N   1 
ATOM   10500 C  CA  . ASN J  1 65  ? 114.049 26.746  5.190  1.00 26.76  ? 65   ASN J CA  1 
ATOM   10501 C  C   . ASN J  1 65  ? 113.499 26.189  3.881  1.00 34.56  ? 65   ASN J C   1 
ATOM   10502 O  O   . ASN J  1 65  ? 113.538 24.966  3.662  1.00 33.88  ? 65   ASN J O   1 
ATOM   10503 C  CB  . ASN J  1 65  ? 114.596 25.590  6.032  1.00 24.88  ? 65   ASN J CB  1 
ATOM   10504 C  CG  . ASN J  1 65  ? 115.703 24.769  5.424  1.00 31.94  ? 65   ASN J CG  1 
ATOM   10505 O  OD1 . ASN J  1 65  ? 116.478 25.270  4.601  1.00 34.84  ? 65   ASN J OD1 1 
ATOM   10506 N  ND2 . ASN J  1 65  ? 115.848 23.525  5.872  1.00 29.69  ? 65   ASN J ND2 1 
ATOM   10507 N  N   . PRO J  1 66  ? 112.995 27.037  3.000  1.00 35.34  ? 66   PRO J N   1 
ATOM   10508 C  CA  . PRO J  1 66  ? 112.331 26.529  1.790  1.00 32.95  ? 66   PRO J CA  1 
ATOM   10509 C  C   . PRO J  1 66  ? 113.318 25.852  0.850  1.00 45.42  ? 66   PRO J C   1 
ATOM   10510 O  O   . PRO J  1 66  ? 112.926 25.086  -0.035 1.00 37.44  ? 66   PRO J O   1 
ATOM   10511 C  CB  . PRO J  1 66  ? 111.748 27.807  1.163  1.00 31.07  ? 66   PRO J CB  1 
ATOM   10512 C  CG  . PRO J  1 66  ? 112.675 28.895  1.623  1.00 32.20  ? 66   PRO J CG  1 
ATOM   10513 C  CD  . PRO J  1 66  ? 113.019 28.519  3.043  1.00 28.04  ? 66   PRO J CD  1 
ATOM   10514 N  N   . LEU J  1 67  ? 114.624 26.102  0.994  1.00 35.53  ? 67   LEU J N   1 
ATOM   10515 C  CA  . LEU J  1 67  ? 115.603 25.451  0.123  1.00 29.87  ? 67   LEU J CA  1 
ATOM   10516 C  C   . LEU J  1 67  ? 116.115 24.158  0.738  1.00 32.85  ? 67   LEU J C   1 
ATOM   10517 O  O   . LEU J  1 67  ? 116.936 23.448  0.159  1.00 46.18  ? 67   LEU J O   1 
ATOM   10518 C  CB  . LEU J  1 67  ? 116.769 26.404  -0.164 1.00 31.11  ? 67   LEU J CB  1 
ATOM   10519 C  CG  . LEU J  1 67  ? 116.397 27.831  -0.562 1.00 39.14  ? 67   LEU J CG  1 
ATOM   10520 C  CD1 . LEU J  1 67  ? 117.545 28.489  -1.325 1.00 46.16  ? 67   LEU J CD1 1 
ATOM   10521 C  CD2 . LEU J  1 67  ? 115.121 27.854  -1.387 1.00 53.36  ? 67   LEU J CD2 1 
ATOM   10522 N  N   . SER J  1 68  ? 115.642 23.824  1.938  1.00 29.98  ? 68   SER J N   1 
ATOM   10523 C  CA  . SER J  1 68  ? 116.020 22.561  2.557  1.00 30.44  ? 68   SER J CA  1 
ATOM   10524 C  C   . SER J  1 68  ? 117.525 22.463  2.709  1.00 35.77  ? 68   SER J C   1 
ATOM   10525 O  O   . SER J  1 68  ? 118.148 21.516  2.236  1.00 34.24  ? 68   SER J O   1 
ATOM   10526 C  CB  . SER J  1 68  ? 115.503 21.375  1.727  1.00 34.84  ? 68   SER J CB  1 
ATOM   10527 O  OG  . SER J  1 68  ? 114.229 21.689  1.194  1.00 44.02  ? 68   SER J OG  1 
ATOM   10528 N  N   . ARG J  1 69  ? 118.098 23.459  3.367  1.00 34.73  ? 69   ARG J N   1 
ATOM   10529 C  CA  . ARG J  1 69  ? 119.532 23.483  3.633  1.00 31.98  ? 69   ARG J CA  1 
ATOM   10530 C  C   . ARG J  1 69  ? 119.802 23.266  5.114  1.00 30.88  ? 69   ARG J C   1 
ATOM   10531 O  O   . ARG J  1 69  ? 118.837 23.191  5.882  1.00 32.34  ? 69   ARG J O   1 
ATOM   10532 C  CB  . ARG J  1 69  ? 120.131 24.802  3.115  1.00 30.70  ? 69   ARG J CB  1 
ATOM   10533 C  CG  . ARG J  1 69  ? 120.345 24.683  1.603  1.00 40.14  ? 69   ARG J CG  1 
ATOM   10534 C  CD  . ARG J  1 69  ? 121.038 25.881  0.982  1.00 45.58  ? 69   ARG J CD  1 
ATOM   10535 N  NE  . ARG J  1 69  ? 120.992 25.784  -0.475 1.00 58.04  ? 69   ARG J NE  1 
ATOM   10536 C  CZ  . ARG J  1 69  ? 121.339 26.685  -1.376 1.00 66.17  ? 69   ARG J CZ  1 
ATOM   10537 N  NH1 . ARG J  1 69  ? 121.220 26.395  -2.670 1.00 81.65  ? 69   ARG J NH1 1 
ATOM   10538 N  NH2 . ARG J  1 69  ? 121.803 27.875  -1.021 1.00 52.30  ? 69   ARG J NH2 1 
ATOM   10539 N  N   . LYS J  1 70  ? 121.064 23.148  5.505  1.00 32.43  ? 70   LYS J N   1 
ATOM   10540 C  CA  . LYS J  1 70  ? 121.382 23.013  6.933  1.00 29.50  ? 70   LYS J CA  1 
ATOM   10541 C  C   . LYS J  1 70  ? 121.527 24.388  7.580  1.00 26.84  ? 70   LYS J C   1 
ATOM   10542 O  O   . LYS J  1 70  ? 121.650 25.397  6.888  1.00 27.61  ? 70   LYS J O   1 
ATOM   10543 C  CB  . LYS J  1 70  ? 122.655 22.200  7.127  1.00 32.11  ? 70   LYS J CB  1 
ATOM   10544 C  CG  . LYS J  1 70  ? 122.483 20.708  6.854  1.00 33.03  ? 70   LYS J CG  1 
ATOM   10545 C  CD  . LYS J  1 70  ? 123.781 19.990  7.215  1.00 45.81  ? 70   LYS J CD  1 
ATOM   10546 C  CE  . LYS J  1 70  ? 124.989 20.858  6.904  1.00 55.20  ? 70   LYS J CE  1 
ATOM   10547 N  NZ  . LYS J  1 70  ? 126.236 20.352  7.537  1.00 80.91  ? 70   LYS J NZ  1 
ATOM   10548 N  N   . HIS J  1 71  ? 121.520 24.467  8.913  1.00 25.81  ? 71   HIS J N   1 
ATOM   10549 C  CA  . HIS J  1 71  ? 121.638 25.739  9.603  1.00 25.12  ? 71   HIS J CA  1 
ATOM   10550 C  C   . HIS J  1 71  ? 123.033 26.333  9.485  1.00 24.60  ? 71   HIS J C   1 
ATOM   10551 O  O   . HIS J  1 71  ? 124.054 25.639  9.553  1.00 24.62  ? 71   HIS J O   1 
ATOM   10552 C  CB  . HIS J  1 71  ? 121.281 25.530  11.089 1.00 25.47  ? 71   HIS J CB  1 
ATOM   10553 C  CG  . HIS J  1 71  ? 121.418 26.786  11.894 1.00 23.55  ? 71   HIS J CG  1 
ATOM   10554 N  ND1 . HIS J  1 71  ? 120.465 27.767  11.958 1.00 26.78  ? 71   HIS J ND1 1 
ATOM   10555 C  CD2 . HIS J  1 71  ? 122.444 27.209  12.682 1.00 21.91  ? 71   HIS J CD2 1 
ATOM   10556 C  CE1 . HIS J  1 71  ? 120.890 28.744  12.746 1.00 28.77  ? 71   HIS J CE1 1 
ATOM   10557 N  NE2 . HIS J  1 71  ? 122.106 28.428  13.208 1.00 22.22  ? 71   HIS J NE2 1 
ATOM   10558 N  N   . GLY J  1 72  ? 123.092 27.659  9.311  1.00 25.42  ? 72   GLY J N   1 
ATOM   10559 C  CA  . GLY J  1 72  ? 124.387 28.327  9.233  1.00 23.15  ? 72   GLY J CA  1 
ATOM   10560 C  C   . GLY J  1 72  ? 124.330 29.737  9.761  1.00 28.25  ? 72   GLY J C   1 
ATOM   10561 O  O   . GLY J  1 72  ? 123.286 30.151  10.278 1.00 24.65  ? 72   GLY J O   1 
ATOM   10562 N  N   . GLY J  1 73  ? 125.394 30.530  9.662  1.00 27.10  ? 73   GLY J N   1 
ATOM   10563 C  CA  . GLY J  1 73  ? 125.295 31.965  9.915  1.00 24.10  ? 73   GLY J CA  1 
ATOM   10564 C  C   . GLY J  1 73  ? 124.814 32.722  8.685  1.00 23.39  ? 73   GLY J C   1 
ATOM   10565 O  O   . GLY J  1 73  ? 124.806 32.170  7.573  1.00 26.23  ? 73   GLY J O   1 
ATOM   10566 N  N   . PRO J  1 74  ? 124.385 33.960  8.877  1.00 23.96  ? 74   PRO J N   1 
ATOM   10567 C  CA  . PRO J  1 74  ? 123.883 34.762  7.759  1.00 25.44  ? 74   PRO J CA  1 
ATOM   10568 C  C   . PRO J  1 74  ? 124.890 34.886  6.618  1.00 33.52  ? 74   PRO J C   1 
ATOM   10569 O  O   . PRO J  1 74  ? 124.493 35.029  5.448  1.00 29.24  ? 74   PRO J O   1 
ATOM   10570 C  CB  . PRO J  1 74  ? 123.593 36.121  8.376  1.00 31.61  ? 74   PRO J CB  1 
ATOM   10571 C  CG  . PRO J  1 74  ? 124.130 36.116  9.756  1.00 27.67  ? 74   PRO J CG  1 
ATOM   10572 C  CD  . PRO J  1 74  ? 124.307 34.681  10.157 1.00 24.71  ? 74   PRO J CD  1 
ATOM   10573 N  N   . LYS J  1 75  ? 126.195 34.813  6.889  1.00 32.99  ? 75   LYS J N   1 
ATOM   10574 C  CA  . LYS J  1 75  ? 127.161 34.937  5.792  1.00 39.12  ? 75   LYS J CA  1 
ATOM   10575 C  C   . LYS J  1 75  ? 127.459 33.616  5.094  1.00 41.11  ? 75   LYS J C   1 
ATOM   10576 O  O   . LYS J  1 75  ? 128.139 33.633  4.056  1.00 40.45  ? 75   LYS J O   1 
ATOM   10577 C  CB  . LYS J  1 75  ? 128.478 35.535  6.296  1.00 42.47  ? 75   LYS J CB  1 
ATOM   10578 C  CG  . LYS J  1 75  ? 128.346 36.784  7.148  1.00 50.43  ? 75   LYS J CG  1 
ATOM   10579 C  CD  . LYS J  1 75  ? 129.422 36.809  8.227  1.00 63.87  ? 75   LYS J CD  1 
ATOM   10580 C  CE  . LYS J  1 75  ? 130.538 37.783  7.871  1.00 70.23  ? 75   LYS J CE  1 
ATOM   10581 N  NZ  . LYS J  1 75  ? 130.186 39.161  8.325  1.00 76.72  ? 75   LYS J NZ  1 
ATOM   10582 N  N   . ASP J  1 76  ? 126.986 32.486  5.612  1.00 28.02  ? 76   ASP J N   1 
ATOM   10583 C  CA  . ASP J  1 76  ? 127.245 31.206  4.966  1.00 31.51  ? 76   ASP J CA  1 
ATOM   10584 C  C   . ASP J  1 76  ? 126.346 30.980  3.760  1.00 40.10  ? 76   ASP J C   1 
ATOM   10585 O  O   . ASP J  1 76  ? 125.188 31.396  3.753  1.00 34.80  ? 76   ASP J O   1 
ATOM   10586 C  CB  . ASP J  1 76  ? 127.075 30.052  5.956  1.00 31.87  ? 76   ASP J CB  1 
ATOM   10587 C  CG  . ASP J  1 76  ? 128.064 30.164  7.106  1.00 40.40  ? 76   ASP J CG  1 
ATOM   10588 O  OD1 . ASP J  1 76  ? 129.212 30.603  6.895  1.00 39.74  ? 76   ASP J OD1 1 
ATOM   10589 O  OD2 . ASP J  1 76  ? 127.714 29.815  8.252  1.00 33.78  ? 76   ASP J OD2 1 
ATOM   10590 N  N   . GLU J  1 77  ? 126.854 30.301  2.725  1.00 35.65  ? 77   GLU J N   1 
ATOM   10591 C  CA  . GLU J  1 77  ? 125.949 29.972  1.624  1.00 34.04  ? 77   GLU J CA  1 
ATOM   10592 C  C   . GLU J  1 77  ? 125.037 28.826  2.051  1.00 34.69  ? 77   GLU J C   1 
ATOM   10593 O  O   . GLU J  1 77  ? 123.884 28.768  1.639  1.00 37.53  ? 77   GLU J O   1 
ATOM   10594 C  CB  . GLU J  1 77  ? 126.686 29.599  0.338  1.00 51.74  ? 77   GLU J CB  1 
ATOM   10595 C  CG  . GLU J  1 77  ? 125.943 28.587  -0.520 1.00 69.10  ? 77   GLU J CG  1 
ATOM   10596 C  CD  . GLU J  1 77  ? 124.973 29.167  -1.527 1.00 81.59  ? 77   GLU J CD  1 
ATOM   10597 O  OE1 . GLU J  1 77  ? 124.827 30.407  -1.595 1.00 103.25 ? 77   GLU J OE1 1 
ATOM   10598 O  OE2 . GLU J  1 77  ? 124.338 28.383  -2.274 1.00 92.91  ? 77   GLU J OE2 1 
ATOM   10599 N  N   . GLU J  1 78  ? 125.540 27.908  2.866  1.00 30.50  ? 78   GLU J N   1 
ATOM   10600 C  CA  . GLU J  1 78  ? 124.710 26.848  3.426  1.00 27.97  ? 78   GLU J CA  1 
ATOM   10601 C  C   . GLU J  1 78  ? 124.114 27.410  4.717  1.00 31.17  ? 78   GLU J C   1 
ATOM   10602 O  O   . GLU J  1 78  ? 124.761 27.511  5.758  1.00 29.00  ? 78   GLU J O   1 
ATOM   10603 C  CB  . GLU J  1 78  ? 125.522 25.596  3.699  1.00 32.33  ? 78   GLU J CB  1 
ATOM   10604 C  CG  . GLU J  1 78  ? 124.745 24.395  4.202  1.00 37.56  ? 78   GLU J CG  1 
ATOM   10605 C  CD  . GLU J  1 78  ? 123.831 23.745  3.181  1.00 45.67  ? 78   GLU J CD  1 
ATOM   10606 O  OE1 . GLU J  1 78  ? 123.127 22.765  3.534  1.00 38.61  ? 78   GLU J OE1 1 
ATOM   10607 O  OE2 . GLU J  1 78  ? 123.777 24.180  2.010  1.00 52.80  ? 78   GLU J OE2 1 
ATOM   10608 N  N   . ARG J  1 79  ? 122.868 27.832  4.628  1.00 31.22  ? 79   ARG J N   1 
ATOM   10609 C  CA  . ARG J  1 79  ? 122.137 28.395  5.748  1.00 26.30  ? 79   ARG J CA  1 
ATOM   10610 C  C   . ARG J  1 79  ? 120.650 28.197  5.476  1.00 28.57  ? 79   ARG J C   1 
ATOM   10611 O  O   . ARG J  1 79  ? 120.272 27.983  4.323  1.00 26.24  ? 79   ARG J O   1 
ATOM   10612 C  CB  . ARG J  1 79  ? 122.433 29.886  5.925  1.00 24.58  ? 79   ARG J CB  1 
ATOM   10613 C  CG  . ARG J  1 79  ? 122.093 30.737  4.716  1.00 27.32  ? 79   ARG J CG  1 
ATOM   10614 C  CD  . ARG J  1 79  ? 122.158 32.232  4.933  1.00 25.57  ? 79   ARG J CD  1 
ATOM   10615 N  NE  . ARG J  1 79  ? 120.844 32.798  5.330  1.00 24.37  ? 79   ARG J NE  1 
ATOM   10616 C  CZ  . ARG J  1 79  ? 120.613 34.087  5.454  1.00 25.51  ? 79   ARG J CZ  1 
ATOM   10617 N  NH1 . ARG J  1 79  ? 119.418 34.570  5.807  1.00 22.50  ? 79   ARG J NH1 1 
ATOM   10618 N  NH2 . ARG J  1 79  ? 121.606 34.944  5.211  1.00 26.50  ? 79   ARG J NH2 1 
ATOM   10619 N  N   . HIS J  1 80  ? 119.827 28.269  6.513  1.00 24.42  ? 80   HIS J N   1 
ATOM   10620 C  CA  . HIS J  1 80  ? 118.398 28.418  6.277  1.00 22.96  ? 80   HIS J CA  1 
ATOM   10621 C  C   . HIS J  1 80  ? 118.065 29.819  5.790  1.00 26.93  ? 80   HIS J C   1 
ATOM   10622 O  O   . HIS J  1 80  ? 118.747 30.772  6.162  1.00 27.69  ? 80   HIS J O   1 
ATOM   10623 C  CB  . HIS J  1 80  ? 117.671 28.167  7.596  1.00 22.82  ? 80   HIS J CB  1 
ATOM   10624 C  CG  . HIS J  1 80  ? 117.915 26.824  8.193  1.00 24.38  ? 80   HIS J CG  1 
ATOM   10625 N  ND1 . HIS J  1 80  ? 118.102 26.627  9.544  1.00 23.27  ? 80   HIS J ND1 1 
ATOM   10626 C  CD2 . HIS J  1 80  ? 117.981 25.596  7.633  1.00 23.50  ? 80   HIS J CD2 1 
ATOM   10627 C  CE1 . HIS J  1 80  ? 118.275 25.343  9.766  1.00 23.57  ? 80   HIS J CE1 1 
ATOM   10628 N  NE2 . HIS J  1 80  ? 118.205 24.670  8.621  1.00 25.36  ? 80   HIS J NE2 1 
ATOM   10629 N  N   . VAL J  1 81  ? 117.027 30.052  4.995  1.00 24.27  ? 81   VAL J N   1 
ATOM   10630 C  CA  . VAL J  1 81  ? 116.646 31.431  4.670  1.00 24.88  ? 81   VAL J CA  1 
ATOM   10631 C  C   . VAL J  1 81  ? 116.425 32.273  5.911  1.00 25.09  ? 81   VAL J C   1 
ATOM   10632 O  O   . VAL J  1 81  ? 116.735 33.472  5.954  1.00 28.13  ? 81   VAL J O   1 
ATOM   10633 C  CB  . VAL J  1 81  ? 115.363 31.437  3.803  1.00 28.03  ? 81   VAL J CB  1 
ATOM   10634 C  CG1 . VAL J  1 81  ? 114.730 32.816  3.754  1.00 28.91  ? 81   VAL J CG1 1 
ATOM   10635 C  CG2 . VAL J  1 81  ? 115.690 30.951  2.394  1.00 27.16  ? 81   VAL J CG2 1 
ATOM   10636 N  N   . GLY J  1 82  ? 115.908 31.644  6.975  1.00 26.51  ? 82   GLY J N   1 
ATOM   10637 C  CA  . GLY J  1 82  ? 115.597 32.448  8.151  1.00 23.73  ? 82   GLY J CA  1 
ATOM   10638 C  C   . GLY J  1 82  ? 116.772 32.700  9.074  1.00 25.06  ? 82   GLY J C   1 
ATOM   10639 O  O   . GLY J  1 82  ? 116.618 33.301  10.159 1.00 22.89  ? 82   GLY J O   1 
ATOM   10640 N  N   . ASP J  1 83  ? 117.978 32.273  8.717  1.00 22.86  ? 83   ASP J N   1 
ATOM   10641 C  CA  . ASP J  1 83  ? 119.117 32.398  9.632  1.00 19.97  ? 83   ASP J CA  1 
ATOM   10642 C  C   . ASP J  1 83  ? 119.687 33.812  9.674  1.00 25.66  ? 83   ASP J C   1 
ATOM   10643 O  O   . ASP J  1 83  ? 120.458 34.215  8.799  1.00 25.61  ? 83   ASP J O   1 
ATOM   10644 C  CB  . ASP J  1 83  ? 120.212 31.400  9.240  1.00 22.40  ? 83   ASP J CB  1 
ATOM   10645 C  CG  . ASP J  1 83  ? 119.842 29.977  9.618  1.00 26.50  ? 83   ASP J CG  1 
ATOM   10646 O  OD1 . ASP J  1 83  ? 118.869 29.797  10.392 1.00 23.19  ? 83   ASP J OD1 1 
ATOM   10647 O  OD2 . ASP J  1 83  ? 120.478 29.016  9.157  1.00 23.42  ? 83   ASP J OD2 1 
ATOM   10648 N  N   . LEU J  1 84  ? 119.334 34.579  10.714 1.00 23.02  ? 84   LEU J N   1 
ATOM   10649 C  CA  . LEU J  1 84  ? 119.794 35.963  10.799 1.00 24.23  ? 84   LEU J CA  1 
ATOM   10650 C  C   . LEU J  1 84  ? 120.905 36.108  11.826 1.00 22.59  ? 84   LEU J C   1 
ATOM   10651 O  O   . LEU J  1 84  ? 121.263 37.233  12.189 1.00 30.14  ? 84   LEU J O   1 
ATOM   10652 C  CB  . LEU J  1 84  ? 118.617 36.888  11.136 1.00 25.34  ? 84   LEU J CB  1 
ATOM   10653 C  CG  . LEU J  1 84  ? 117.504 36.983  10.097 1.00 29.02  ? 84   LEU J CG  1 
ATOM   10654 C  CD1 . LEU J  1 84  ? 116.451 37.991  10.534 1.00 24.83  ? 84   LEU J CD1 1 
ATOM   10655 C  CD2 . LEU J  1 84  ? 118.058 37.356  8.729  1.00 33.62  ? 84   LEU J CD2 1 
ATOM   10656 N  N   . GLY J  1 85  ? 121.463 35.007  12.308 1.00 20.92  ? 85   GLY J N   1 
ATOM   10657 C  CA  . GLY J  1 85  ? 122.597 35.097  13.219 1.00 24.35  ? 85   GLY J CA  1 
ATOM   10658 C  C   . GLY J  1 85  ? 122.247 35.402  14.658 1.00 24.46  ? 85   GLY J C   1 
ATOM   10659 O  O   . GLY J  1 85  ? 121.366 34.756  15.233 1.00 25.08  ? 85   GLY J O   1 
ATOM   10660 N  N   . ASN J  1 86  ? 122.966 36.348  15.254 1.00 23.22  ? 86   ASN J N   1 
ATOM   10661 C  CA  . ASN J  1 86  ? 122.763 36.754  16.632 1.00 20.81  ? 86   ASN J CA  1 
ATOM   10662 C  C   . ASN J  1 86  ? 122.474 38.253  16.760 1.00 23.74  ? 86   ASN J C   1 
ATOM   10663 O  O   . ASN J  1 86  ? 122.902 39.059  15.936 1.00 24.89  ? 86   ASN J O   1 
ATOM   10664 C  CB  . ASN J  1 86  ? 124.004 36.472  17.489 1.00 23.37  ? 86   ASN J CB  1 
ATOM   10665 C  CG  . ASN J  1 86  ? 124.247 35.004  17.694 1.00 25.06  ? 86   ASN J CG  1 
ATOM   10666 O  OD1 . ASN J  1 86  ? 123.458 34.382  18.410 1.00 25.84  ? 86   ASN J OD1 1 
ATOM   10667 N  ND2 . ASN J  1 86  ? 125.319 34.457  17.113 1.00 23.03  ? 86   ASN J ND2 1 
ATOM   10668 N  N   . VAL J  1 87  ? 121.785 38.591  17.843 1.00 20.95  ? 87   VAL J N   1 
ATOM   10669 C  CA  . VAL J  1 87  ? 121.704 39.973  18.304 1.00 24.79  ? 87   VAL J CA  1 
ATOM   10670 C  C   . VAL J  1 87  ? 122.523 40.043  19.596 1.00 26.76  ? 87   VAL J C   1 
ATOM   10671 O  O   . VAL J  1 87  ? 122.745 39.033  20.268 1.00 24.23  ? 87   VAL J O   1 
ATOM   10672 C  CB  . VAL J  1 87  ? 120.276 40.505  18.515 1.00 22.01  ? 87   VAL J CB  1 
ATOM   10673 C  CG1 . VAL J  1 87  ? 119.509 40.504  17.197 1.00 28.79  ? 87   VAL J CG1 1 
ATOM   10674 C  CG2 . VAL J  1 87  ? 119.523 39.701  19.554 1.00 25.47  ? 87   VAL J CG2 1 
ATOM   10675 N  N   . THR J  1 88  ? 122.975 41.252  19.918 1.00 25.98  ? 88   THR J N   1 
ATOM   10676 C  CA  . THR J  1 88  ? 123.804 41.473  21.091 1.00 26.98  ? 88   THR J CA  1 
ATOM   10677 C  C   . THR J  1 88  ? 123.129 42.368  22.127 1.00 26.34  ? 88   THR J C   1 
ATOM   10678 O  O   . THR J  1 88  ? 122.807 43.508  21.798 1.00 27.50  ? 88   THR J O   1 
ATOM   10679 C  CB  . THR J  1 88  ? 125.138 42.141  20.656 1.00 30.16  ? 88   THR J CB  1 
ATOM   10680 O  OG1 . THR J  1 88  ? 125.788 41.309  19.684 1.00 28.07  ? 88   THR J OG1 1 
ATOM   10681 C  CG2 . THR J  1 88  ? 126.050 42.271  21.864 1.00 29.99  ? 88   THR J CG2 1 
ATOM   10682 N  N   . ALA J  1 89  ? 122.929 41.877  23.342 1.00 28.19  ? 89   ALA J N   1 
ATOM   10683 C  CA  . ALA J  1 89  ? 122.398 42.689  24.422 1.00 31.14  ? 89   ALA J CA  1 
ATOM   10684 C  C   . ALA J  1 89  ? 123.534 43.269  25.279 1.00 27.92  ? 89   ALA J C   1 
ATOM   10685 O  O   . ALA J  1 89  ? 124.435 42.536  25.650 1.00 27.12  ? 89   ALA J O   1 
ATOM   10686 C  CB  . ALA J  1 89  ? 121.477 41.901  25.332 1.00 28.48  ? 89   ALA J CB  1 
ATOM   10687 N  N   . ASP J  1 90  ? 123.435 44.552  25.589 1.00 38.42  ? 90   ASP J N   1 
ATOM   10688 C  CA  . ASP J  1 90  ? 124.360 45.253  26.471 1.00 39.29  ? 90   ASP J CA  1 
ATOM   10689 C  C   . ASP J  1 90  ? 124.093 44.895  27.931 1.00 45.53  ? 90   ASP J C   1 
ATOM   10690 O  O   . ASP J  1 90  ? 123.222 44.092  28.268 1.00 35.80  ? 90   ASP J O   1 
ATOM   10691 C  CB  . ASP J  1 90  ? 124.263 46.760  26.229 1.00 34.28  ? 90   ASP J CB  1 
ATOM   10692 C  CG  . ASP J  1 90  ? 122.923 47.371  26.594 1.00 44.92  ? 90   ASP J CG  1 
ATOM   10693 O  OD1 . ASP J  1 90  ? 122.282 47.003  27.602 1.00 58.90  ? 90   ASP J OD1 1 
ATOM   10694 O  OD2 . ASP J  1 90  ? 122.456 48.273  25.857 1.00 59.24  ? 90   ASP J OD2 1 
ATOM   10695 N  N   . LYS J  1 91  ? 124.882 45.488  28.824 1.00 46.30  ? 91   LYS J N   1 
ATOM   10696 C  CA  . LYS J  1 91  ? 124.791 45.231  30.253 1.00 40.21  ? 91   LYS J CA  1 
ATOM   10697 C  C   . LYS J  1 91  ? 123.394 45.574  30.743 1.00 33.45  ? 91   LYS J C   1 
ATOM   10698 O  O   . LYS J  1 91  ? 122.896 44.993  31.699 1.00 45.11  ? 91   LYS J O   1 
ATOM   10699 C  CB  . LYS J  1 91  ? 125.803 46.075  31.040 1.00 37.25  ? 91   LYS J CB  1 
ATOM   10700 C  CG  . LYS J  1 91  ? 125.839 47.528  30.576 1.00 51.78  ? 91   LYS J CG  1 
ATOM   10701 C  CD  . LYS J  1 91  ? 126.948 48.328  31.243 1.00 62.87  ? 91   LYS J CD  1 
ATOM   10702 C  CE  . LYS J  1 91  ? 126.408 49.439  32.126 1.00 59.48  ? 91   LYS J CE  1 
ATOM   10703 N  NZ  . LYS J  1 91  ? 127.457 50.045  32.988 1.00 64.29  ? 91   LYS J NZ  1 
ATOM   10704 N  N   . ASP J  1 92  ? 122.765 46.546  30.071 1.00 36.59  ? 92   ASP J N   1 
ATOM   10705 C  CA  . ASP J  1 92  ? 121.412 46.869  30.563 1.00 39.06  ? 92   ASP J CA  1 
ATOM   10706 C  C   . ASP J  1 92  ? 120.331 46.038  29.891 1.00 46.76  ? 92   ASP J C   1 
ATOM   10707 O  O   . ASP J  1 92  ? 119.137 46.364  29.940 1.00 41.19  ? 92   ASP J O   1 
ATOM   10708 C  CB  . ASP J  1 92  ? 121.172 48.369  30.394 1.00 41.14  ? 92   ASP J CB  1 
ATOM   10709 C  CG  . ASP J  1 92  ? 122.042 49.151  31.377 1.00 64.36  ? 92   ASP J CG  1 
ATOM   10710 O  OD1 . ASP J  1 92  ? 122.242 48.678  32.520 1.00 68.33  ? 92   ASP J OD1 1 
ATOM   10711 O  OD2 . ASP J  1 92  ? 122.524 50.241  30.998 1.00 90.14  ? 92   ASP J OD2 1 
ATOM   10712 N  N   . GLY J  1 93  ? 120.713 44.931  29.265 1.00 35.29  ? 93   GLY J N   1 
ATOM   10713 C  CA  . GLY J  1 93  ? 119.734 43.978  28.764 1.00 28.87  ? 93   GLY J CA  1 
ATOM   10714 C  C   . GLY J  1 93  ? 119.064 44.440  27.492 1.00 32.24  ? 93   GLY J C   1 
ATOM   10715 O  O   . GLY J  1 93  ? 118.093 43.810  27.056 1.00 36.70  ? 93   GLY J O   1 
ATOM   10716 N  N   . VAL J  1 94  ? 119.548 45.511  26.885 1.00 28.33  ? 94   VAL J N   1 
ATOM   10717 C  CA  . VAL J  1 94  ? 118.968 46.067  25.677 1.00 33.32  ? 94   VAL J CA  1 
ATOM   10718 C  C   . VAL J  1 94  ? 119.729 45.689  24.415 1.00 40.36  ? 94   VAL J C   1 
ATOM   10719 O  O   . VAL J  1 94  ? 120.936 45.933  24.340 1.00 38.60  ? 94   VAL J O   1 
ATOM   10720 C  CB  . VAL J  1 94  ? 118.939 47.611  25.717 1.00 38.28  ? 94   VAL J CB  1 
ATOM   10721 C  CG1 . VAL J  1 94  ? 118.550 48.148  24.351 1.00 37.92  ? 94   VAL J CG1 1 
ATOM   10722 C  CG2 . VAL J  1 94  ? 117.996 48.090  26.806 1.00 41.16  ? 94   VAL J CG2 1 
ATOM   10723 N  N   . ALA J  1 95  ? 119.052 45.120  23.427 1.00 30.27  ? 95   ALA J N   1 
ATOM   10724 C  CA  . ALA J  1 95  ? 119.754 44.830  22.182 1.00 26.62  ? 95   ALA J CA  1 
ATOM   10725 C  C   . ALA J  1 95  ? 119.276 45.819  21.137 1.00 33.94  ? 95   ALA J C   1 
ATOM   10726 O  O   . ALA J  1 95  ? 118.127 45.742  20.712 1.00 33.43  ? 95   ALA J O   1 
ATOM   10727 C  CB  . ALA J  1 95  ? 119.539 43.401  21.703 1.00 25.11  ? 95   ALA J CB  1 
ATOM   10728 N  N   . ASP J  1 96  ? 120.167 46.733  20.749 1.00 26.30  ? 96   ASP J N   1 
ATOM   10729 C  CA  . ASP J  1 96  ? 119.924 47.492  19.541 1.00 26.38  ? 96   ASP J CA  1 
ATOM   10730 C  C   . ASP J  1 96  ? 120.195 46.545  18.386 1.00 30.72  ? 96   ASP J C   1 
ATOM   10731 O  O   . ASP J  1 96  ? 121.200 45.829  18.363 1.00 33.17  ? 96   ASP J O   1 
ATOM   10732 C  CB  . ASP J  1 96  ? 120.800 48.743  19.506 1.00 35.55  ? 96   ASP J CB  1 
ATOM   10733 C  CG  . ASP J  1 96  ? 120.423 49.687  20.640 1.00 49.36  ? 96   ASP J CG  1 
ATOM   10734 O  OD1 . ASP J  1 96  ? 119.295 50.227  20.596 1.00 53.82  ? 96   ASP J OD1 1 
ATOM   10735 O  OD2 . ASP J  1 96  ? 121.238 49.874  21.567 1.00 70.16  ? 96   ASP J OD2 1 
ATOM   10736 N  N   . VAL J  1 97  ? 119.271 46.496  17.434 1.00 27.71  ? 97   VAL J N   1 
ATOM   10737 C  CA  . VAL J  1 97  ? 119.439 45.575  16.310 1.00 23.13  ? 97   VAL J CA  1 
ATOM   10738 C  C   . VAL J  1 97  ? 119.603 46.357  15.023 1.00 28.11  ? 97   VAL J C   1 
ATOM   10739 O  O   . VAL J  1 97  ? 118.892 47.333  14.763 1.00 27.14  ? 97   VAL J O   1 
ATOM   10740 C  CB  . VAL J  1 97  ? 118.236 44.619  16.213 1.00 27.40  ? 97   VAL J CB  1 
ATOM   10741 C  CG1 . VAL J  1 97  ? 118.349 43.721  14.987 1.00 27.39  ? 97   VAL J CG1 1 
ATOM   10742 C  CG2 . VAL J  1 97  ? 118.125 43.787  17.478 1.00 24.97  ? 97   VAL J CG2 1 
ATOM   10743 N  N   . SER J  1 98  ? 120.557 45.942  14.193 1.00 27.05  ? 98   SER J N   1 
ATOM   10744 C  CA  . SER J  1 98  ? 120.702 46.532  12.868 1.00 24.65  ? 98   SER J CA  1 
ATOM   10745 C  C   . SER J  1 98  ? 121.482 45.580  11.977 1.00 26.53  ? 98   SER J C   1 
ATOM   10746 O  O   . SER J  1 98  ? 122.685 45.393  12.151 1.00 31.28  ? 98   SER J O   1 
ATOM   10747 C  CB  . SER J  1 98  ? 121.385 47.912  12.929 1.00 25.92  ? 98   SER J CB  1 
ATOM   10748 O  OG  . SER J  1 98  ? 121.323 48.472  11.621 1.00 33.59  ? 98   SER J OG  1 
ATOM   10749 N  N   . ILE J  1 99  ? 120.754 44.945  11.066 1.00 21.84  ? 99   ILE J N   1 
ATOM   10750 C  CA  . ILE J  1 99  ? 121.241 43.867  10.237 1.00 24.07  ? 99   ILE J CA  1 
ATOM   10751 C  C   . ILE J  1 99  ? 120.842 44.179  8.809  1.00 30.56  ? 99   ILE J C   1 
ATOM   10752 O  O   . ILE J  1 99  ? 119.809 44.826  8.590  1.00 32.27  ? 99   ILE J O   1 
ATOM   10753 C  CB  . ILE J  1 99  ? 120.614 42.550  10.750 1.00 32.78  ? 99   ILE J CB  1 
ATOM   10754 C  CG1 . ILE J  1 99  ? 121.202 42.094  12.094 1.00 33.63  ? 99   ILE J CG1 1 
ATOM   10755 C  CG2 . ILE J  1 99  ? 120.680 41.426  9.738  1.00 30.57  ? 99   ILE J CG2 1 
ATOM   10756 C  CD1 . ILE J  1 99  ? 120.444 40.953  12.744 1.00 34.54  ? 99   ILE J CD1 1 
ATOM   10757 N  N   . GLU J  1 100 ? 121.644 43.727  7.858  1.00 29.46  ? 100  GLU J N   1 
ATOM   10758 C  CA  . GLU J  1 100 ? 121.207 43.721  6.471  1.00 31.71  ? 100  GLU J CA  1 
ATOM   10759 C  C   . GLU J  1 100 ? 121.401 42.331  5.875  1.00 30.66  ? 100  GLU J C   1 
ATOM   10760 O  O   . GLU J  1 100 ? 122.419 41.658  6.036  1.00 29.12  ? 100  GLU J O   1 
ATOM   10761 C  CB  . GLU J  1 100 ? 121.930 44.781  5.622  1.00 40.85  ? 100  GLU J CB  1 
ATOM   10762 C  CG  . GLU J  1 100 ? 121.352 44.832  4.208  1.00 45.92  ? 100  GLU J CG  1 
ATOM   10763 C  CD  . GLU J  1 100 ? 122.100 45.837  3.345  1.00 61.42  ? 100  GLU J CD  1 
ATOM   10764 O  OE1 . GLU J  1 100 ? 122.889 45.415  2.471  1.00 74.98  ? 100  GLU J OE1 1 
ATOM   10765 O  OE2 . GLU J  1 100 ? 121.887 47.046  3.562  1.00 55.81  ? 100  GLU J OE2 1 
ATOM   10766 N  N   . ASP J  1 101 ? 120.369 41.860  5.163  1.00 27.01  ? 101  ASP J N   1 
ATOM   10767 C  CA  . ASP J  1 101 ? 120.400 40.479  4.693  1.00 27.37  ? 101  ASP J CA  1 
ATOM   10768 C  C   . ASP J  1 101 ? 119.821 40.366  3.289  1.00 27.22  ? 101  ASP J C   1 
ATOM   10769 O  O   . ASP J  1 101 ? 118.802 40.991  2.975  1.00 33.10  ? 101  ASP J O   1 
ATOM   10770 C  CB  . ASP J  1 101 ? 119.626 39.578  5.672  1.00 29.30  ? 101  ASP J CB  1 
ATOM   10771 C  CG  . ASP J  1 101 ? 119.931 38.124  5.369  1.00 34.14  ? 101  ASP J CG  1 
ATOM   10772 O  OD1 . ASP J  1 101 ? 119.105 37.394  4.781  1.00 29.62  ? 101  ASP J OD1 1 
ATOM   10773 O  OD2 . ASP J  1 101 ? 121.058 37.704  5.714  1.00 34.33  ? 101  ASP J OD2 1 
ATOM   10774 N  N   . SER J  1 102 ? 120.460 39.584  2.437  1.00 31.64  ? 102  SER J N   1 
ATOM   10775 C  CA  . SER J  1 102 ? 119.996 39.541  1.050  1.00 38.65  ? 102  SER J CA  1 
ATOM   10776 C  C   . SER J  1 102 ? 119.380 38.196  0.730  1.00 33.67  ? 102  SER J C   1 
ATOM   10777 O  O   . SER J  1 102 ? 119.130 37.858  -0.423 1.00 39.55  ? 102  SER J O   1 
ATOM   10778 C  CB  . SER J  1 102 ? 121.181 39.850  0.123  1.00 44.72  ? 102  SER J CB  1 
ATOM   10779 O  OG  . SER J  1 102 ? 122.186 38.859  0.300  1.00 58.59  ? 102  SER J OG  1 
ATOM   10780 N  N   . VAL J  1 103 ? 119.122 37.386  1.760  1.00 26.38  ? 103  VAL J N   1 
ATOM   10781 C  CA  . VAL J  1 103 ? 118.546 36.081  1.497  1.00 23.65  ? 103  VAL J CA  1 
ATOM   10782 C  C   . VAL J  1 103 ? 117.061 36.109  1.851  1.00 32.58  ? 103  VAL J C   1 
ATOM   10783 O  O   . VAL J  1 103 ? 116.238 35.558  1.115  1.00 32.76  ? 103  VAL J O   1 
ATOM   10784 C  CB  . VAL J  1 103 ? 119.254 34.981  2.291  1.00 28.39  ? 103  VAL J CB  1 
ATOM   10785 C  CG1 . VAL J  1 103 ? 118.588 33.640  2.057  1.00 24.26  ? 103  VAL J CG1 1 
ATOM   10786 C  CG2 . VAL J  1 103 ? 120.734 34.968  1.890  1.00 35.50  ? 103  VAL J CG2 1 
ATOM   10787 N  N   . ILE J  1 104 ? 116.732 36.758  2.964  1.00 23.36  ? 104  ILE J N   1 
ATOM   10788 C  CA  . ILE J  1 104 ? 115.307 36.903  3.276  1.00 29.37  ? 104  ILE J CA  1 
ATOM   10789 C  C   . ILE J  1 104 ? 114.700 37.896  2.294  1.00 37.01  ? 104  ILE J C   1 
ATOM   10790 O  O   . ILE J  1 104 ? 115.467 38.741  1.819  1.00 31.58  ? 104  ILE J O   1 
ATOM   10791 C  CB  . ILE J  1 104 ? 115.037 37.455  4.683  1.00 29.83  ? 104  ILE J CB  1 
ATOM   10792 C  CG1 . ILE J  1 104 ? 115.683 38.825  4.898  1.00 28.65  ? 104  ILE J CG1 1 
ATOM   10793 C  CG2 . ILE J  1 104 ? 115.463 36.478  5.767  1.00 27.78  ? 104  ILE J CG2 1 
ATOM   10794 C  CD1 . ILE J  1 104 ? 115.361 39.503  6.198  1.00 30.11  ? 104  ILE J CD1 1 
ATOM   10795 N  N   . SER J  1 105 ? 113.399 37.819  2.036  1.00 33.51  ? 105  SER J N   1 
ATOM   10796 C  CA  . SER J  1 105 ? 112.730 38.866  1.273  1.00 33.58  ? 105  SER J CA  1 
ATOM   10797 C  C   . SER J  1 105 ? 111.342 39.185  1.823  1.00 32.52  ? 105  SER J C   1 
ATOM   10798 O  O   . SER J  1 105 ? 110.802 38.412  2.613  1.00 34.34  ? 105  SER J O   1 
ATOM   10799 C  CB  . SER J  1 105 ? 112.573 38.490  -0.207 1.00 43.68  ? 105  SER J CB  1 
ATOM   10800 O  OG  . SER J  1 105 ? 111.910 39.533  -0.918 1.00 42.12  ? 105  SER J OG  1 
ATOM   10801 N  N   . LEU J  1 106 ? 110.813 40.327  1.380  1.00 32.82  ? 106  LEU J N   1 
ATOM   10802 C  CA  . LEU J  1 106 ? 109.463 40.736  1.758  1.00 34.24  ? 106  LEU J CA  1 
ATOM   10803 C  C   . LEU J  1 106 ? 108.514 40.476  0.590  1.00 34.22  ? 106  LEU J C   1 
ATOM   10804 O  O   . LEU J  1 106 ? 107.374 40.940  0.604  1.00 40.45  ? 106  LEU J O   1 
ATOM   10805 C  CB  . LEU J  1 106 ? 109.380 42.185  2.213  1.00 31.55  ? 106  LEU J CB  1 
ATOM   10806 C  CG  . LEU J  1 106 ? 110.210 42.652  3.409  1.00 35.02  ? 106  LEU J CG  1 
ATOM   10807 C  CD1 . LEU J  1 106 ? 109.880 44.099  3.766  1.00 33.00  ? 106  LEU J CD1 1 
ATOM   10808 C  CD2 . LEU J  1 106 ? 110.038 41.797  4.660  1.00 28.30  ? 106  LEU J CD2 1 
ATOM   10809 N  N   . SER J  1 107 ? 108.979 39.723  -0.390 1.00 40.69  ? 107  SER J N   1 
ATOM   10810 C  CA  . SER J  1 107 ? 108.142 39.245  -1.490 1.00 50.98  ? 107  SER J CA  1 
ATOM   10811 C  C   . SER J  1 107 ? 108.781 38.043  -2.172 1.00 50.17  ? 107  SER J C   1 
ATOM   10812 O  O   . SER J  1 107 ? 109.950 37.761  -1.882 1.00 52.50  ? 107  SER J O   1 
ATOM   10813 C  CB  . SER J  1 107 ? 107.895 40.375  -2.493 1.00 63.26  ? 107  SER J CB  1 
ATOM   10814 O  OG  . SER J  1 107 ? 107.516 41.553  -1.789 1.00 66.79  ? 107  SER J OG  1 
ATOM   10815 N  N   . GLY J  1 108 ? 108.067 37.340  -3.043 1.00 49.66  ? 108  GLY J N   1 
ATOM   10816 C  CA  . GLY J  1 108 ? 108.573 36.184  -3.758 1.00 46.49  ? 108  GLY J CA  1 
ATOM   10817 C  C   . GLY J  1 108 ? 108.531 34.903  -2.948 1.00 58.75  ? 108  GLY J C   1 
ATOM   10818 O  O   . GLY J  1 108 ? 107.611 34.694  -2.155 1.00 68.01  ? 108  GLY J O   1 
ATOM   10819 N  N   . ASP J  1 109 ? 109.520 34.034  -3.132 1.00 62.09  ? 109  ASP J N   1 
ATOM   10820 C  CA  . ASP J  1 109 ? 109.523 32.694  -2.564 1.00 73.50  ? 109  ASP J CA  1 
ATOM   10821 C  C   . ASP J  1 109 ? 110.198 32.622  -1.200 1.00 65.92  ? 109  ASP J C   1 
ATOM   10822 O  O   . ASP J  1 109 ? 109.889 31.755  -0.384 1.00 59.88  ? 109  ASP J O   1 
ATOM   10823 C  CB  . ASP J  1 109 ? 110.224 31.716  -3.514 1.00 89.96  ? 109  ASP J CB  1 
ATOM   10824 C  CG  . ASP J  1 109 ? 110.132 32.107  -4.973 1.00 104.60 ? 109  ASP J CG  1 
ATOM   10825 O  OD1 . ASP J  1 109 ? 109.274 32.930  -5.359 1.00 117.13 ? 109  ASP J OD1 1 
ATOM   10826 O  OD2 . ASP J  1 109 ? 110.942 31.575  -5.770 1.00 128.63 ? 109  ASP J OD2 1 
ATOM   10827 N  N   . HIS J  1 110 ? 111.127 33.538  -0.959 1.00 58.61  ? 110  HIS J N   1 
ATOM   10828 C  CA  . HIS J  1 110 ? 111.779 33.641  0.340  1.00 49.53  ? 110  HIS J CA  1 
ATOM   10829 C  C   . HIS J  1 110 ? 111.032 34.645  1.200  1.00 42.37  ? 110  HIS J C   1 
ATOM   10830 O  O   . HIS J  1 110 ? 111.623 35.249  2.096  1.00 49.05  ? 110  HIS J O   1 
ATOM   10831 C  CB  . HIS J  1 110 ? 113.230 34.112  0.223  1.00 44.92  ? 110  HIS J CB  1 
ATOM   10832 C  CG  . HIS J  1 110 ? 114.113 33.211  -0.577 1.00 57.43  ? 110  HIS J CG  1 
ATOM   10833 N  ND1 . HIS J  1 110 ? 115.475 33.400  -0.674 1.00 66.89  ? 110  HIS J ND1 1 
ATOM   10834 C  CD2 . HIS J  1 110 ? 113.828 32.114  -1.314 1.00 55.16  ? 110  HIS J CD2 1 
ATOM   10835 C  CE1 . HIS J  1 110 ? 115.988 32.454  -1.440 1.00 73.04  ? 110  HIS J CE1 1 
ATOM   10836 N  NE2 . HIS J  1 110 ? 115.008 31.659  -1.843 1.00 66.19  ? 110  HIS J NE2 1 
ATOM   10837 N  N   . CYS J  1 111 ? 109.760 34.849  0.879  1.00 38.27  ? 111  CYS J N   1 
ATOM   10838 C  CA  . CYS J  1 111 ? 109.031 35.924  1.549  1.00 38.28  ? 111  CYS J CA  1 
ATOM   10839 C  C   . CYS J  1 111 ? 108.800 35.578  3.011  1.00 36.88  ? 111  CYS J C   1 
ATOM   10840 O  O   . CYS J  1 111 ? 108.434 34.436  3.302  1.00 36.23  ? 111  CYS J O   1 
ATOM   10841 C  CB  . CYS J  1 111 ? 107.709 36.161  0.822  1.00 44.34  ? 111  CYS J CB  1 
ATOM   10842 S  SG  . CYS J  1 111 ? 106.645 37.371  1.627  1.00 55.60  ? 111  CYS J SG  1 
ATOM   10843 N  N   . ILE J  1 112 ? 109.004 36.511  3.938  1.00 30.55  ? 112  ILE J N   1 
ATOM   10844 C  CA  . ILE J  1 112 ? 108.888 36.169  5.360  1.00 24.69  ? 112  ILE J CA  1 
ATOM   10845 C  C   . ILE J  1 112 ? 107.659 36.785  5.999  1.00 30.30  ? 112  ILE J C   1 
ATOM   10846 O  O   . ILE J  1 112 ? 107.451 36.682  7.213  1.00 25.32  ? 112  ILE J O   1 
ATOM   10847 C  CB  . ILE J  1 112 ? 110.124 36.650  6.151  1.00 25.85  ? 112  ILE J CB  1 
ATOM   10848 C  CG1 . ILE J  1 112 ? 110.284 38.168  6.087  1.00 29.69  ? 112  ILE J CG1 1 
ATOM   10849 C  CG2 . ILE J  1 112 ? 111.365 35.905  5.681  1.00 29.49  ? 112  ILE J CG2 1 
ATOM   10850 C  CD1 . ILE J  1 112 ? 111.498 38.754  6.785  1.00 33.08  ? 112  ILE J CD1 1 
ATOM   10851 N  N   . ILE J  1 113 ? 106.830 37.461  5.196  1.00 32.06  ? 113  ILE J N   1 
ATOM   10852 C  CA  . ILE J  1 113 ? 105.644 38.075  5.812  1.00 29.52  ? 113  ILE J CA  1 
ATOM   10853 C  C   . ILE J  1 113 ? 104.706 36.965  6.276  1.00 29.98  ? 113  ILE J C   1 
ATOM   10854 O  O   . ILE J  1 113 ? 104.549 35.969  5.576  1.00 27.65  ? 113  ILE J O   1 
ATOM   10855 C  CB  . ILE J  1 113 ? 104.925 39.039  4.859  1.00 38.33  ? 113  ILE J CB  1 
ATOM   10856 C  CG1 . ILE J  1 113 ? 105.852 40.169  4.374  1.00 41.60  ? 113  ILE J CG1 1 
ATOM   10857 C  CG2 . ILE J  1 113 ? 103.652 39.601  5.473  1.00 36.84  ? 113  ILE J CG2 1 
ATOM   10858 C  CD1 . ILE J  1 113 ? 106.535 40.873  5.530  1.00 35.04  ? 113  ILE J CD1 1 
ATOM   10859 N  N   . GLY J  1 114 ? 104.115 37.143  7.469  1.00 30.78  ? 114  GLY J N   1 
ATOM   10860 C  CA  . GLY J  1 114 ? 103.220 36.101  7.946  1.00 31.69  ? 114  GLY J CA  1 
ATOM   10861 C  C   . GLY J  1 114 ? 103.948 34.946  8.599  1.00 32.06  ? 114  GLY J C   1 
ATOM   10862 O  O   . GLY J  1 114 ? 103.322 33.983  9.050  1.00 29.91  ? 114  GLY J O   1 
ATOM   10863 N  N   . ARG J  1 115 ? 105.283 35.035  8.660  1.00 27.14  ? 115  ARG J N   1 
ATOM   10864 C  CA  . ARG J  1 115 ? 106.060 34.032  9.397  1.00 27.73  ? 115  ARG J CA  1 
ATOM   10865 C  C   . ARG J  1 115 ? 106.453 34.653  10.729 1.00 25.98  ? 115  ARG J C   1 
ATOM   10866 O  O   . ARG J  1 115 ? 105.937 35.702  11.092 1.00 27.47  ? 115  ARG J O   1 
ATOM   10867 C  CB  . ARG J  1 115 ? 107.239 33.515  8.573  1.00 28.71  ? 115  ARG J CB  1 
ATOM   10868 C  CG  . ARG J  1 115 ? 106.725 33.035  7.222  1.00 29.94  ? 115  ARG J CG  1 
ATOM   10869 C  CD  . ARG J  1 115 ? 107.760 32.285  6.421  1.00 30.71  ? 115  ARG J CD  1 
ATOM   10870 N  NE  . ARG J  1 115 ? 107.250 31.916  5.099  1.00 30.37  ? 115  ARG J NE  1 
ATOM   10871 C  CZ  . ARG J  1 115 ? 106.626 30.759  4.885  1.00 27.80  ? 115  ARG J CZ  1 
ATOM   10872 N  NH1 . ARG J  1 115 ? 106.185 30.460  3.671  1.00 33.76  ? 115  ARG J NH1 1 
ATOM   10873 N  NH2 . ARG J  1 115 ? 106.432 29.883  5.854  1.00 32.17  ? 115  ARG J NH2 1 
ATOM   10874 N  N   . THR J  1 116 ? 107.327 34.020  11.489 1.00 22.81  ? 116  THR J N   1 
ATOM   10875 C  CA  . THR J  1 116 ? 107.574 34.434  12.860 1.00 24.14  ? 116  THR J CA  1 
ATOM   10876 C  C   . THR J  1 116 ? 109.054 34.744  13.110 1.00 27.66  ? 116  THR J C   1 
ATOM   10877 O  O   . THR J  1 116 ? 109.887 33.926  12.733 1.00 25.45  ? 116  THR J O   1 
ATOM   10878 C  CB  . THR J  1 116 ? 107.166 33.306  13.829 1.00 28.67  ? 116  THR J CB  1 
ATOM   10879 O  OG1 . THR J  1 116 ? 105.723 33.225  13.856 1.00 25.82  ? 116  THR J OG1 1 
ATOM   10880 C  CG2 . THR J  1 116 ? 107.640 33.607  15.241 1.00 26.26  ? 116  THR J CG2 1 
ATOM   10881 N  N   . LEU J  1 117 ? 109.305 35.875  13.746 1.00 21.24  ? 117  LEU J N   1 
ATOM   10882 C  CA  . LEU J  1 117 ? 110.644 36.223  14.193 1.00 23.41  ? 117  LEU J CA  1 
ATOM   10883 C  C   . LEU J  1 117 ? 110.852 35.778  15.634 1.00 28.07  ? 117  LEU J C   1 
ATOM   10884 O  O   . LEU J  1 117 ? 110.017 36.095  16.490 1.00 27.58  ? 117  LEU J O   1 
ATOM   10885 C  CB  . LEU J  1 117 ? 110.852 37.728  14.105 1.00 26.27  ? 117  LEU J CB  1 
ATOM   10886 C  CG  . LEU J  1 117 ? 112.257 38.269  14.398 1.00 24.00  ? 117  LEU J CG  1 
ATOM   10887 C  CD1 . LEU J  1 117 ? 113.261 37.755  13.377 1.00 25.83  ? 117  LEU J CD1 1 
ATOM   10888 C  CD2 . LEU J  1 117 ? 112.206 39.792  14.406 1.00 22.64  ? 117  LEU J CD2 1 
ATOM   10889 N  N   . VAL J  1 118 ? 111.943 35.084  15.922 1.00 25.62  ? 118  VAL J N   1 
ATOM   10890 C  CA  . VAL J  1 118 ? 112.183 34.611  17.282 1.00 21.96  ? 118  VAL J CA  1 
ATOM   10891 C  C   . VAL J  1 118 ? 113.507 35.078  17.861 1.00 26.17  ? 118  VAL J C   1 
ATOM   10892 O  O   . VAL J  1 118 ? 114.465 35.052  17.097 1.00 22.33  ? 118  VAL J O   1 
ATOM   10893 C  CB  . VAL J  1 118 ? 112.177 33.068  17.277 1.00 23.79  ? 118  VAL J CB  1 
ATOM   10894 C  CG1 . VAL J  1 118 ? 112.586 32.530  18.632 1.00 27.29  ? 118  VAL J CG1 1 
ATOM   10895 C  CG2 . VAL J  1 118 ? 110.786 32.579  16.874 1.00 23.34  ? 118  VAL J CG2 1 
ATOM   10896 N  N   . VAL J  1 119 ? 113.583 35.480  19.122 1.00 24.71  ? 119  VAL J N   1 
ATOM   10897 C  CA  . VAL J  1 119 ? 114.879 35.776  19.743 1.00 22.52  ? 119  VAL J CA  1 
ATOM   10898 C  C   . VAL J  1 119 ? 115.071 34.761  20.857 1.00 25.17  ? 119  VAL J C   1 
ATOM   10899 O  O   . VAL J  1 119 ? 114.142 34.438  21.602 1.00 23.83  ? 119  VAL J O   1 
ATOM   10900 C  CB  . VAL J  1 119 ? 114.996 37.221  20.226 1.00 23.65  ? 119  VAL J CB  1 
ATOM   10901 C  CG1 . VAL J  1 119 ? 113.981 37.569  21.314 1.00 25.59  ? 119  VAL J CG1 1 
ATOM   10902 C  CG2 . VAL J  1 119 ? 116.398 37.478  20.776 1.00 30.51  ? 119  VAL J CG2 1 
ATOM   10903 N  N   . HIS J  1 120 ? 116.290 34.200  20.956 1.00 24.11  ? 120  HIS J N   1 
ATOM   10904 C  CA  . HIS J  1 120 ? 116.509 33.029  21.775 1.00 24.42  ? 120  HIS J CA  1 
ATOM   10905 C  C   . HIS J  1 120 ? 117.281 33.264  23.078 1.00 25.93  ? 120  HIS J C   1 
ATOM   10906 O  O   . HIS J  1 120 ? 117.904 34.294  23.336 1.00 26.79  ? 120  HIS J O   1 
ATOM   10907 C  CB  . HIS J  1 120 ? 117.306 31.935  21.027 1.00 22.54  ? 120  HIS J CB  1 
ATOM   10908 C  CG  . HIS J  1 120 ? 116.520 31.249  19.950 1.00 19.20  ? 120  HIS J CG  1 
ATOM   10909 N  ND1 . HIS J  1 120 ? 115.958 30.014  20.088 1.00 19.67  ? 120  HIS J ND1 1 
ATOM   10910 C  CD2 . HIS J  1 120 ? 116.228 31.647  18.680 1.00 22.01  ? 120  HIS J CD2 1 
ATOM   10911 C  CE1 . HIS J  1 120 ? 115.345 29.674  18.961 1.00 24.41  ? 120  HIS J CE1 1 
ATOM   10912 N  NE2 . HIS J  1 120 ? 115.484 30.654  18.082 1.00 22.56  ? 120  HIS J NE2 1 
ATOM   10913 N  N   . GLU J  1 121 ? 117.204 32.176  23.845 1.00 25.94  ? 121  GLU J N   1 
ATOM   10914 C  CA  . GLU J  1 121 ? 117.849 32.021  25.135 1.00 26.96  ? 121  GLU J CA  1 
ATOM   10915 C  C   . GLU J  1 121 ? 119.365 32.152  25.064 1.00 31.99  ? 121  GLU J C   1 
ATOM   10916 O  O   . GLU J  1 121 ? 119.951 32.878  25.874 1.00 29.70  ? 121  GLU J O   1 
ATOM   10917 C  CB  . GLU J  1 121 ? 117.486 30.649  25.701 1.00 25.25  ? 121  GLU J CB  1 
ATOM   10918 C  CG  . GLU J  1 121 ? 118.081 30.320  27.056 1.00 36.00  ? 121  GLU J CG  1 
ATOM   10919 C  CD  . GLU J  1 121 ? 118.063 28.834  27.380 1.00 51.89  ? 121  GLU J CD  1 
ATOM   10920 O  OE1 . GLU J  1 121 ? 118.502 28.490  28.505 1.00 70.30  ? 121  GLU J OE1 1 
ATOM   10921 O  OE2 . GLU J  1 121 ? 117.632 27.980  26.568 1.00 41.84  ? 121  GLU J OE2 1 
ATOM   10922 N  N   . LYS J  1 122 ? 119.975 31.447  24.123 1.00 27.47  ? 122  LYS J N   1 
ATOM   10923 C  CA  . LYS J  1 122 ? 121.428 31.401  24.016 1.00 30.85  ? 122  LYS J CA  1 
ATOM   10924 C  C   . LYS J  1 122 ? 121.927 31.889  22.660 1.00 30.05  ? 122  LYS J C   1 
ATOM   10925 O  O   . LYS J  1 122 ? 121.127 32.138  21.762 1.00 25.70  ? 122  LYS J O   1 
ATOM   10926 C  CB  . LYS J  1 122 ? 121.952 29.965  24.194 1.00 30.41  ? 122  LYS J CB  1 
ATOM   10927 C  CG  . LYS J  1 122 ? 121.423 29.277  25.439 1.00 33.49  ? 122  LYS J CG  1 
ATOM   10928 C  CD  . LYS J  1 122 ? 122.252 28.060  25.791 1.00 39.08  ? 122  LYS J CD  1 
ATOM   10929 C  CE  . LYS J  1 122 ? 121.821 26.859  24.963 1.00 50.03  ? 122  LYS J CE  1 
ATOM   10930 N  NZ  . LYS J  1 122 ? 121.961 25.578  25.716 1.00 48.70  ? 122  LYS J NZ  1 
ATOM   10931 N  N   . ALA J  1 123 ? 123.251 31.971  22.574 1.00 24.67  ? 123  ALA J N   1 
ATOM   10932 C  CA  . ALA J  1 123 ? 123.937 32.291  21.332 1.00 28.96  ? 123  ALA J CA  1 
ATOM   10933 C  C   . ALA J  1 123 ? 123.662 31.251  20.250 1.00 28.06  ? 123  ALA J C   1 
ATOM   10934 O  O   . ALA J  1 123 ? 123.580 30.061  20.529 1.00 27.86  ? 123  ALA J O   1 
ATOM   10935 C  CB  . ALA J  1 123 ? 125.439 32.365  21.588 1.00 31.90  ? 123  ALA J CB  1 
ATOM   10936 N  N   . ASP J  1 124 ? 123.551 31.704  19.010 1.00 24.43  ? 124  ASP J N   1 
ATOM   10937 C  CA  . ASP J  1 124 ? 123.549 30.810  17.852 1.00 22.44  ? 124  ASP J CA  1 
ATOM   10938 C  C   . ASP J  1 124 ? 124.994 30.499  17.494 1.00 20.58  ? 124  ASP J C   1 
ATOM   10939 O  O   . ASP J  1 124 ? 125.774 31.451  17.360 1.00 22.65  ? 124  ASP J O   1 
ATOM   10940 C  CB  . ASP J  1 124 ? 122.795 31.504  16.718 1.00 20.13  ? 124  ASP J CB  1 
ATOM   10941 C  CG  . ASP J  1 124 ? 122.665 30.716  15.443 1.00 25.05  ? 124  ASP J CG  1 
ATOM   10942 O  OD1 . ASP J  1 124 ? 121.702 31.036  14.701 1.00 21.41  ? 124  ASP J OD1 1 
ATOM   10943 O  OD2 . ASP J  1 124 ? 123.478 29.803  15.136 1.00 27.91  ? 124  ASP J OD2 1 
ATOM   10944 N  N   . ASP J  1 125 ? 125.369 29.236  17.363 1.00 19.82  ? 125  ASP J N   1 
ATOM   10945 C  CA  . ASP J  1 125 ? 126.774 28.903  17.110 1.00 26.40  ? 125  ASP J CA  1 
ATOM   10946 C  C   . ASP J  1 125 ? 127.052 28.917  15.601 1.00 23.50  ? 125  ASP J C   1 
ATOM   10947 O  O   . ASP J  1 125 ? 128.170 28.546  15.241 1.00 23.81  ? 125  ASP J O   1 
ATOM   10948 C  CB  . ASP J  1 125 ? 127.208 27.556  17.697 1.00 24.13  ? 125  ASP J CB  1 
ATOM   10949 C  CG  . ASP J  1 125 ? 126.553 26.326  17.128 1.00 28.36  ? 125  ASP J CG  1 
ATOM   10950 O  OD1 . ASP J  1 125 ? 126.549 25.267  17.815 1.00 24.39  ? 125  ASP J OD1 1 
ATOM   10951 O  OD2 . ASP J  1 125 ? 126.011 26.326  16.002 1.00 22.05  ? 125  ASP J OD2 1 
ATOM   10952 N  N   . LEU J  1 126 ? 126.072 29.342  14.822 1.00 20.93  ? 126  LEU J N   1 
ATOM   10953 C  CA  . LEU J  1 126 ? 126.224 29.543  13.369 1.00 21.05  ? 126  LEU J CA  1 
ATOM   10954 C  C   . LEU J  1 126 ? 126.638 28.266  12.653 1.00 22.04  ? 126  LEU J C   1 
ATOM   10955 O  O   . LEU J  1 126 ? 127.297 28.279  11.586 1.00 23.88  ? 126  LEU J O   1 
ATOM   10956 C  CB  . LEU J  1 126 ? 127.219 30.680  13.066 1.00 22.91  ? 126  LEU J CB  1 
ATOM   10957 C  CG  . LEU J  1 126 ? 127.089 31.944  13.928 1.00 23.49  ? 126  LEU J CG  1 
ATOM   10958 C  CD1 . LEU J  1 126 ? 128.131 32.989  13.576 1.00 24.71  ? 126  LEU J CD1 1 
ATOM   10959 C  CD2 . LEU J  1 126 ? 125.682 32.533  13.814 1.00 22.83  ? 126  LEU J CD2 1 
ATOM   10960 N  N   . GLY J  1 127 ? 126.245 27.107  13.197 1.00 20.14  ? 127  GLY J N   1 
ATOM   10961 C  CA  . GLY J  1 127 ? 126.513 25.834  12.525 1.00 18.87  ? 127  GLY J CA  1 
ATOM   10962 C  C   . GLY J  1 127 ? 127.904 25.288  12.810 1.00 21.98  ? 127  GLY J C   1 
ATOM   10963 O  O   . GLY J  1 127 ? 128.352 24.263  12.297 1.00 21.73  ? 127  GLY J O   1 
ATOM   10964 N  N   . LYS J  1 128 ? 128.662 25.932  13.695 1.00 19.20  ? 128  LYS J N   1 
ATOM   10965 C  CA  . LYS J  1 128 ? 130.039 25.498  13.941 1.00 17.59  ? 128  LYS J CA  1 
ATOM   10966 C  C   . LYS J  1 128 ? 130.221 24.745  15.248 1.00 24.28  ? 128  LYS J C   1 
ATOM   10967 O  O   . LYS J  1 128 ? 131.351 24.611  15.722 1.00 23.14  ? 128  LYS J O   1 
ATOM   10968 C  CB  . LYS J  1 128 ? 130.907 26.769  13.941 1.00 23.01  ? 128  LYS J CB  1 
ATOM   10969 C  CG  . LYS J  1 128 ? 130.719 27.592  12.653 1.00 24.24  ? 128  LYS J CG  1 
ATOM   10970 C  CD  . LYS J  1 128 ? 131.555 28.879  12.752 1.00 32.45  ? 128  LYS J CD  1 
ATOM   10971 C  CE  . LYS J  1 128 ? 133.051 28.590  12.722 1.00 31.41  ? 128  LYS J CE  1 
ATOM   10972 N  NZ  . LYS J  1 128 ? 133.849 29.833  12.942 1.00 43.35  ? 128  LYS J NZ  1 
ATOM   10973 N  N   . GLY J  1 129 ? 129.145 24.233  15.854 1.00 22.48  ? 129  GLY J N   1 
ATOM   10974 C  CA  . GLY J  1 129 ? 129.252 23.581  17.148 1.00 19.38  ? 129  GLY J CA  1 
ATOM   10975 C  C   . GLY J  1 129 ? 129.611 22.108  17.084 1.00 23.45  ? 129  GLY J C   1 
ATOM   10976 O  O   . GLY J  1 129 ? 129.912 21.531  18.128 1.00 22.95  ? 129  GLY J O   1 
ATOM   10977 N  N   . GLY J  1 130 ? 129.611 21.448  15.924 1.00 20.87  ? 130  GLY J N   1 
ATOM   10978 C  CA  . GLY J  1 130 ? 130.119 20.082  15.875 1.00 20.69  ? 130  GLY J CA  1 
ATOM   10979 C  C   . GLY J  1 130 ? 129.169 19.008  16.314 1.00 21.46  ? 130  GLY J C   1 
ATOM   10980 O  O   . GLY J  1 130 ? 129.488 17.816  16.316 1.00 26.65  ? 130  GLY J O   1 
ATOM   10981 N  N   . ASN J  1 131 ? 127.942 19.333  16.724 1.00 25.33  ? 131  ASN J N   1 
ATOM   10982 C  CA  . ASN J  1 131 ? 126.990 18.297  17.127 1.00 27.20  ? 131  ASN J CA  1 
ATOM   10983 C  C   . ASN J  1 131 ? 125.787 18.325  16.187 1.00 25.90  ? 131  ASN J C   1 
ATOM   10984 O  O   . ASN J  1 131 ? 125.642 19.184  15.313 1.00 27.29  ? 131  ASN J O   1 
ATOM   10985 C  CB  . ASN J  1 131 ? 126.546 18.468  18.582 1.00 22.96  ? 131  ASN J CB  1 
ATOM   10986 C  CG  . ASN J  1 131 ? 125.812 19.758  18.887 1.00 29.57  ? 131  ASN J CG  1 
ATOM   10987 O  OD1 . ASN J  1 131 ? 125.790 20.704  18.105 1.00 24.03  ? 131  ASN J OD1 1 
ATOM   10988 N  ND2 . ASN J  1 131 ? 125.177 19.818  20.059 1.00 25.57  ? 131  ASN J ND2 1 
ATOM   10989 N  N   . GLU J  1 132 ? 124.871 17.371  16.315 1.00 24.17  ? 132  GLU J N   1 
ATOM   10990 C  CA  . GLU J  1 132 ? 123.737 17.402  15.383 1.00 22.78  ? 132  GLU J CA  1 
ATOM   10991 C  C   . GLU J  1 132 ? 122.898 18.660  15.490 1.00 24.95  ? 132  GLU J C   1 
ATOM   10992 O  O   . GLU J  1 132 ? 122.389 19.217  14.524 1.00 29.21  ? 132  GLU J O   1 
ATOM   10993 C  CB  . GLU J  1 132 ? 122.845 16.188  15.704 1.00 29.75  ? 132  GLU J CB  1 
ATOM   10994 C  CG  . GLU J  1 132 ? 123.543 14.846  15.520 1.00 33.21  ? 132  GLU J CG  1 
ATOM   10995 C  CD  . GLU J  1 132 ? 122.550 13.713  15.758 1.00 43.03  ? 132  GLU J CD  1 
ATOM   10996 O  OE1 . GLU J  1 132 ? 121.898 13.730  16.818 1.00 58.07  ? 132  GLU J OE1 1 
ATOM   10997 O  OE2 . GLU J  1 132 ? 122.433 12.842  14.877 1.00 61.79  ? 132  GLU J OE2 1 
ATOM   10998 N  N   . GLU J  1 133 ? 122.719 19.136  16.728 1.00 21.39  ? 133  GLU J N   1 
ATOM   10999 C  CA  . GLU J  1 133 ? 121.833 20.270  16.911 1.00 25.63  ? 133  GLU J CA  1 
ATOM   11000 C  C   . GLU J  1 133 ? 122.399 21.526  16.267 1.00 25.68  ? 133  GLU J C   1 
ATOM   11001 O  O   . GLU J  1 133 ? 121.615 22.391  15.853 1.00 27.41  ? 133  GLU J O   1 
ATOM   11002 C  CB  . GLU J  1 133 ? 121.591 20.508  18.410 1.00 28.35  ? 133  GLU J CB  1 
ATOM   11003 C  CG  . GLU J  1 133 ? 120.590 21.627  18.669 1.00 34.19  ? 133  GLU J CG  1 
ATOM   11004 C  CD  . GLU J  1 133 ? 119.169 21.173  18.383 1.00 41.36  ? 133  GLU J CD  1 
ATOM   11005 O  OE1 . GLU J  1 133 ? 118.326 22.028  18.085 1.00 44.13  ? 133  GLU J OE1 1 
ATOM   11006 O  OE2 . GLU J  1 133 ? 118.919 19.951  18.452 1.00 39.66  ? 133  GLU J OE2 1 
ATOM   11007 N  N   . SER J  1 134 ? 123.721 21.642  16.170 1.00 25.76  ? 134  SER J N   1 
ATOM   11008 C  CA  . SER J  1 134 ? 124.278 22.882  15.583 1.00 21.37  ? 134  SER J CA  1 
ATOM   11009 C  C   . SER J  1 134 ? 123.784 23.128  14.162 1.00 23.64  ? 134  SER J C   1 
ATOM   11010 O  O   . SER J  1 134 ? 123.571 24.262  13.733 1.00 24.43  ? 134  SER J O   1 
ATOM   11011 C  CB  . SER J  1 134 ? 125.807 22.796  15.541 1.00 23.57  ? 134  SER J CB  1 
ATOM   11012 O  OG  . SER J  1 134 ? 126.345 23.983  14.995 1.00 26.09  ? 134  SER J OG  1 
ATOM   11013 N  N   . THR J  1 135 ? 123.628 22.035  13.411 1.00 25.40  ? 135  THR J N   1 
ATOM   11014 C  CA  . THR J  1 135 ? 123.167 22.046  12.044 1.00 22.77  ? 135  THR J CA  1 
ATOM   11015 C  C   . THR J  1 135 ? 121.645 22.209  11.917 1.00 26.30  ? 135  THR J C   1 
ATOM   11016 O  O   . THR J  1 135 ? 121.182 22.269  10.775 1.00 26.51  ? 135  THR J O   1 
ATOM   11017 C  CB  . THR J  1 135 ? 123.455 20.712  11.304 1.00 33.77  ? 135  THR J CB  1 
ATOM   11018 O  OG1 . THR J  1 135 ? 122.553 19.719  11.841 1.00 43.32  ? 135  THR J OG1 1 
ATOM   11019 C  CG2 . THR J  1 135 ? 124.850 20.206  11.547 1.00 42.90  ? 135  THR J CG2 1 
ATOM   11020 N  N   . LYS J  1 136 ? 120.929 22.234  13.027 1.00 24.62  ? 136  LYS J N   1 
ATOM   11021 C  CA  . LYS J  1 136 ? 119.477 22.422  12.986 1.00 28.66  ? 136  LYS J CA  1 
ATOM   11022 C  C   . LYS J  1 136 ? 119.113 23.801  13.526 1.00 27.14  ? 136  LYS J C   1 
ATOM   11023 O  O   . LYS J  1 136 ? 118.370 24.537  12.886 1.00 28.41  ? 136  LYS J O   1 
ATOM   11024 C  CB  . LYS J  1 136 ? 118.709 21.362  13.774 1.00 29.44  ? 136  LYS J CB  1 
ATOM   11025 C  CG  . LYS J  1 136 ? 119.141 19.943  13.462 1.00 40.63  ? 136  LYS J CG  1 
ATOM   11026 C  CD  . LYS J  1 136 ? 118.406 18.920  14.309 1.00 52.96  ? 136  LYS J CD  1 
ATOM   11027 C  CE  . LYS J  1 136 ? 119.294 17.744  14.690 1.00 57.03  ? 136  LYS J CE  1 
ATOM   11028 N  NZ  . LYS J  1 136 ? 118.500 16.548  15.102 1.00 46.90  ? 136  LYS J NZ  1 
ATOM   11029 N  N   . THR J  1 137 ? 119.647 24.114  14.712 1.00 21.66  ? 137  THR J N   1 
ATOM   11030 C  CA  . THR J  1 137 ? 119.239 25.319  15.393 1.00 23.36  ? 137  THR J CA  1 
ATOM   11031 C  C   . THR J  1 137 ? 120.387 26.197  15.860 1.00 25.43  ? 137  THR J C   1 
ATOM   11032 O  O   . THR J  1 137 ? 120.123 27.242  16.467 1.00 27.49  ? 137  THR J O   1 
ATOM   11033 C  CB  . THR J  1 137 ? 118.465 24.916  16.678 1.00 31.07  ? 137  THR J CB  1 
ATOM   11034 O  OG1 . THR J  1 137 ? 119.342 24.111  17.487 1.00 27.98  ? 137  THR J OG1 1 
ATOM   11035 C  CG2 . THR J  1 137 ? 117.247 24.067  16.342 1.00 26.97  ? 137  THR J CG2 1 
ATOM   11036 N  N   . GLY J  1 138 ? 121.619 25.738  15.635 1.00 23.47  ? 138  GLY J N   1 
ATOM   11037 C  CA  . GLY J  1 138 ? 122.768 26.446  16.178 1.00 21.96  ? 138  GLY J CA  1 
ATOM   11038 C  C   . GLY J  1 138 ? 122.874 26.367  17.692 1.00 29.28  ? 138  GLY J C   1 
ATOM   11039 O  O   . GLY J  1 138 ? 123.575 27.185  18.308 1.00 23.97  ? 138  GLY J O   1 
ATOM   11040 N  N   . ASN J  1 139 ? 122.202 25.407  18.326 1.00 24.46  ? 139  ASN J N   1 
ATOM   11041 C  CA  . ASN J  1 139 ? 122.211 25.355  19.791 1.00 25.35  ? 139  ASN J CA  1 
ATOM   11042 C  C   . ASN J  1 139 ? 121.729 26.640  20.447 1.00 25.95  ? 139  ASN J C   1 
ATOM   11043 O  O   . ASN J  1 139 ? 122.148 26.977  21.562 1.00 24.36  ? 139  ASN J O   1 
ATOM   11044 C  CB  . ASN J  1 139 ? 123.632 25.005  20.279 1.00 20.44  ? 139  ASN J CB  1 
ATOM   11045 C  CG  . ASN J  1 139 ? 123.924 23.558  19.894 1.00 27.34  ? 139  ASN J CG  1 
ATOM   11046 O  OD1 . ASN J  1 139 ? 123.427 22.591  20.498 1.00 29.64  ? 139  ASN J OD1 1 
ATOM   11047 N  ND2 . ASN J  1 139 ? 124.744 23.391  18.857 1.00 24.81  ? 139  ASN J ND2 1 
ATOM   11048 N  N   . ALA J  1 140 ? 120.797 27.385  19.842 1.00 21.89  ? 140  ALA J N   1 
ATOM   11049 C  CA  . ALA J  1 140 ? 120.377 28.645  20.469 1.00 23.07  ? 140  ALA J CA  1 
ATOM   11050 C  C   . ALA J  1 140 ? 119.424 28.474  21.645 1.00 29.67  ? 140  ALA J C   1 
ATOM   11051 O  O   . ALA J  1 140 ? 119.125 29.424  22.384 1.00 26.24  ? 140  ALA J O   1 
ATOM   11052 C  CB  . ALA J  1 140 ? 119.705 29.552  19.437 1.00 24.88  ? 140  ALA J CB  1 
ATOM   11053 N  N   . GLY J  1 141 ? 118.910 27.267  21.812 1.00 25.83  ? 141  GLY J N   1 
ATOM   11054 C  CA  . GLY J  1 141 ? 118.096 27.019  22.992 1.00 28.21  ? 141  GLY J CA  1 
ATOM   11055 C  C   . GLY J  1 141 ? 116.696 27.585  22.876 1.00 29.10  ? 141  GLY J C   1 
ATOM   11056 O  O   . GLY J  1 141 ? 116.101 27.765  21.810 1.00 26.51  ? 141  GLY J O   1 
ATOM   11057 N  N   . SER J  1 142 ? 116.125 27.881  24.055 1.00 27.29  ? 142  SER J N   1 
ATOM   11058 C  CA  . SER J  1 142 ? 114.681 28.136  24.084 1.00 26.61  ? 142  SER J CA  1 
ATOM   11059 C  C   . SER J  1 142 ? 114.332 29.467  23.462 1.00 29.44  ? 142  SER J C   1 
ATOM   11060 O  O   . SER J  1 142 ? 115.142 30.361  23.188 1.00 27.70  ? 142  SER J O   1 
ATOM   11061 C  CB  . SER J  1 142 ? 114.214 28.035  25.546 1.00 30.12  ? 142  SER J CB  1 
ATOM   11062 O  OG  . SER J  1 142 ? 114.550 29.201  26.264 1.00 38.88  ? 142  SER J OG  1 
ATOM   11063 N  N   . ARG J  1 143 ? 113.035 29.618  23.242 1.00 24.80  ? 143  ARG J N   1 
ATOM   11064 C  CA  . ARG J  1 143 ? 112.502 30.789  22.566 1.00 27.57  ? 143  ARG J CA  1 
ATOM   11065 C  C   . ARG J  1 143 ? 112.002 31.782  23.610 1.00 39.84  ? 143  ARG J C   1 
ATOM   11066 O  O   . ARG J  1 143 ? 111.018 31.480  24.294 1.00 33.81  ? 143  ARG J O   1 
ATOM   11067 C  CB  . ARG J  1 143 ? 111.395 30.380  21.579 1.00 21.46  ? 143  ARG J CB  1 
ATOM   11068 C  CG  . ARG J  1 143 ? 111.898 29.279  20.642 1.00 21.74  ? 143  ARG J CG  1 
ATOM   11069 C  CD  . ARG J  1 143 ? 110.841 28.753  19.683 1.00 27.59  ? 143  ARG J CD  1 
ATOM   11070 N  NE  . ARG J  1 143 ? 111.342 27.656  18.860 1.00 28.05  ? 143  ARG J NE  1 
ATOM   11071 C  CZ  . ARG J  1 143 ? 110.742 27.039  17.859 1.00 25.83  ? 143  ARG J CZ  1 
ATOM   11072 N  NH1 . ARG J  1 143 ? 111.386 26.053  17.230 1.00 25.64  ? 143  ARG J NH1 1 
ATOM   11073 N  NH2 . ARG J  1 143 ? 109.514 27.405  17.505 1.00 28.92  ? 143  ARG J NH2 1 
ATOM   11074 N  N   . LEU J  1 144 ? 112.662 32.935  23.722 1.00 25.68  ? 144  LEU J N   1 
ATOM   11075 C  CA  . LEU J  1 144 ? 112.295 33.917  24.736 1.00 26.13  ? 144  LEU J CA  1 
ATOM   11076 C  C   . LEU J  1 144 ? 111.145 34.825  24.323 1.00 34.23  ? 144  LEU J C   1 
ATOM   11077 O  O   . LEU J  1 144 ? 110.362 35.253  25.186 1.00 30.51  ? 144  LEU J O   1 
ATOM   11078 C  CB  . LEU J  1 144 ? 113.502 34.778  25.134 1.00 25.89  ? 144  LEU J CB  1 
ATOM   11079 C  CG  . LEU J  1 144 ? 114.698 34.000  25.704 1.00 36.11  ? 144  LEU J CG  1 
ATOM   11080 C  CD1 . LEU J  1 144 ? 115.711 34.976  26.294 1.00 34.42  ? 144  LEU J CD1 1 
ATOM   11081 C  CD2 . LEU J  1 144 ? 114.267 32.959  26.726 1.00 34.02  ? 144  LEU J CD2 1 
ATOM   11082 N  N   . ALA J  1 145 ? 111.036 35.154  23.040 1.00 26.50  ? 145  ALA J N   1 
ATOM   11083 C  CA  . ALA J  1 145 ? 109.973 36.076  22.621 1.00 25.05  ? 145  ALA J CA  1 
ATOM   11084 C  C   . ALA J  1 145 ? 109.870 35.966  21.111 1.00 27.73  ? 145  ALA J C   1 
ATOM   11085 O  O   . ALA J  1 145 ? 110.871 35.558  20.525 1.00 25.15  ? 145  ALA J O   1 
ATOM   11086 C  CB  . ALA J  1 145 ? 110.232 37.526  22.992 1.00 30.47  ? 145  ALA J CB  1 
ATOM   11087 N  N   . CYS J  1 146 ? 108.731 36.323  20.563 1.00 26.12  ? 146  CYS J N   1 
ATOM   11088 C  CA  . CYS J  1 146 ? 108.476 36.072  19.159 1.00 24.27  ? 146  CYS J CA  1 
ATOM   11089 C  C   . CYS J  1 146 ? 107.283 36.916  18.750 1.00 27.94  ? 146  CYS J C   1 
ATOM   11090 O  O   . CYS J  1 146 ? 106.540 37.432  19.595 1.00 28.88  ? 146  CYS J O   1 
ATOM   11091 C  CB  A CYS J  1 146 ? 108.223 34.596  18.851 0.43 24.21  ? 146  CYS J CB  1 
ATOM   11092 C  CB  B CYS J  1 146 ? 108.255 34.569  18.962 0.57 26.41  ? 146  CYS J CB  1 
ATOM   11093 S  SG  A CYS J  1 146 ? 106.982 33.805  19.904 0.43 39.15  ? 146  CYS J SG  1 
ATOM   11094 S  SG  B CYS J  1 146 ? 106.652 33.898  19.445 0.57 29.36  ? 146  CYS J SG  1 
ATOM   11095 N  N   . GLY J  1 147 ? 107.121 37.048  17.441 1.00 25.70  ? 147  GLY J N   1 
ATOM   11096 C  CA  . GLY J  1 147 ? 105.917 37.737  16.958 1.00 24.56  ? 147  GLY J CA  1 
ATOM   11097 C  C   . GLY J  1 147 ? 105.799 37.457  15.480 1.00 24.16  ? 147  GLY J C   1 
ATOM   11098 O  O   . GLY J  1 147 ? 106.779 37.068  14.839 1.00 28.86  ? 147  GLY J O   1 
ATOM   11099 N  N   . VAL J  1 148 ? 104.590 37.637  14.967 1.00 21.78  ? 148  VAL J N   1 
ATOM   11100 C  CA  . VAL J  1 148 ? 104.363 37.423  13.549 1.00 20.52  ? 148  VAL J CA  1 
ATOM   11101 C  C   . VAL J  1 148 ? 104.793 38.640  12.754 1.00 27.54  ? 148  VAL J C   1 
ATOM   11102 O  O   . VAL J  1 148 ? 104.498 39.752  13.182 1.00 27.54  ? 148  VAL J O   1 
ATOM   11103 C  CB  . VAL J  1 148 ? 102.856 37.132  13.332 1.00 23.62  ? 148  VAL J CB  1 
ATOM   11104 C  CG1 . VAL J  1 148 ? 102.574 36.783  11.897 1.00 23.58  ? 148  VAL J CG1 1 
ATOM   11105 C  CG2 . VAL J  1 148 ? 102.463 36.028  14.308 1.00 28.90  ? 148  VAL J CG2 1 
ATOM   11106 N  N   . ILE J  1 149 ? 105.476 38.438  11.631 1.00 28.41  ? 149  ILE J N   1 
ATOM   11107 C  CA  . ILE J  1 149 ? 105.957 39.560  10.809 1.00 24.72  ? 149  ILE J CA  1 
ATOM   11108 C  C   . ILE J  1 149 ? 104.839 40.086  9.935  1.00 29.81  ? 149  ILE J C   1 
ATOM   11109 O  O   . ILE J  1 149 ? 104.205 39.381  9.139  1.00 35.29  ? 149  ILE J O   1 
ATOM   11110 C  CB  . ILE J  1 149 ? 107.153 39.060  9.975  1.00 27.92  ? 149  ILE J CB  1 
ATOM   11111 C  CG1 . ILE J  1 149 ? 108.283 38.543  10.882 1.00 23.75  ? 149  ILE J CG1 1 
ATOM   11112 C  CG2 . ILE J  1 149 ? 107.646 40.098  8.991  1.00 26.90  ? 149  ILE J CG2 1 
ATOM   11113 C  CD1 . ILE J  1 149 ? 109.274 37.678  10.123 1.00 31.21  ? 149  ILE J CD1 1 
ATOM   11114 N  N   . GLY J  1 150 ? 104.500 41.368  10.060 1.00 29.51  ? 150  GLY J N   1 
ATOM   11115 C  CA  . GLY J  1 150 ? 103.328 41.791  9.293  1.00 23.84  ? 150  GLY J CA  1 
ATOM   11116 C  C   . GLY J  1 150 ? 103.648 42.975  8.413  1.00 35.62  ? 150  GLY J C   1 
ATOM   11117 O  O   . GLY J  1 150 ? 104.625 43.718  8.566  1.00 33.08  ? 150  GLY J O   1 
ATOM   11118 N  N   . ILE J  1 151 ? 102.767 43.138  7.427  1.00 34.25  ? 151  ILE J N   1 
ATOM   11119 C  CA  . ILE J  1 151 ? 102.904 44.270  6.508  1.00 32.34  ? 151  ILE J CA  1 
ATOM   11120 C  C   . ILE J  1 151 ? 102.822 45.590  7.248  1.00 40.79  ? 151  ILE J C   1 
ATOM   11121 O  O   . ILE J  1 151 ? 101.996 45.801  8.135  1.00 37.64  ? 151  ILE J O   1 
ATOM   11122 C  CB  . ILE J  1 151 ? 101.846 44.139  5.406  1.00 31.84  ? 151  ILE J CB  1 
ATOM   11123 C  CG1 . ILE J  1 151 ? 102.045 42.868  4.583  1.00 35.93  ? 151  ILE J CG1 1 
ATOM   11124 C  CG2 . ILE J  1 151 ? 101.836 45.374  4.514  1.00 37.44  ? 151  ILE J CG2 1 
ATOM   11125 C  CD1 . ILE J  1 151 ? 100.785 42.348  3.923  1.00 38.59  ? 151  ILE J CD1 1 
ATOM   11126 N  N   . ALA J  1 152 ? 103.727 46.514  6.897  1.00 37.33  ? 152  ALA J N   1 
ATOM   11127 C  CA  . ALA J  1 152 ? 103.712 47.849  7.466  1.00 31.82  ? 152  ALA J CA  1 
ATOM   11128 C  C   . ALA J  1 152 ? 103.455 48.914  6.386  1.00 31.01  ? 152  ALA J C   1 
ATOM   11129 O  O   . ALA J  1 152 ? 103.608 48.698  5.185  1.00 34.74  ? 152  ALA J O   1 
ATOM   11130 C  CB  . ALA J  1 152 ? 105.021 48.154  8.175  1.00 36.21  ? 152  ALA J CB  1 
ATOM   11131 N  N   . GLN J  1 153 ? 103.054 50.075  6.868  1.00 39.16  ? 153  GLN J N   1 
ATOM   11132 C  CA  . GLN J  1 153 ? 102.735 51.188  5.981  1.00 45.16  ? 153  GLN J CA  1 
ATOM   11133 C  C   . GLN J  1 153 ? 104.001 51.763  5.354  1.00 51.98  ? 153  GLN J C   1 
ATOM   11134 O  O   . GLN J  1 153 ? 104.926 52.069  6.139  1.00 53.50  ? 153  GLN J O   1 
ATOM   11135 C  CB  . GLN J  1 153 ? 102.000 52.260  6.769  1.00 39.87  ? 153  GLN J CB  1 
ATOM   11136 C  CG  . GLN J  1 153 ? 101.797 53.570  6.021  1.00 52.60  ? 153  GLN J CG  1 
ATOM   11137 C  CD  . GLN J  1 153 ? 100.672 54.358  6.684  1.00 57.60  ? 153  GLN J CD  1 
ATOM   11138 O  OE1 . GLN J  1 153 ? 99.598  54.495  6.096  1.00 61.46  ? 153  GLN J OE1 1 
ATOM   11139 N  NE2 . GLN J  1 153 ? 100.970 54.832  7.889  1.00 49.30  ? 153  GLN J NE2 1 
ATOM   11140 O  OXT . GLN J  1 153 ? 104.037 51.883  4.114  1.00 53.37  ? 153  GLN J OXT 1 
HETATM 11141 CU CU  . CU1 K  2 .   ? 63.095  46.486  18.660 1.00 24.40  ? 200  CU1 A CU  1 
HETATM 11142 ZN ZN  . ZN  L  3 .   ? 62.861  49.681  12.655 1.00 25.17  ? 201  ZN  A ZN  1 
HETATM 11143 CU CU  . CU1 M  2 .   ? 62.280  14.603  21.081 1.00 21.10  ? 200  CU1 B CU  1 
HETATM 11144 ZN ZN  . ZN  N  3 .   ? 61.272  10.517  15.732 1.00 20.34  ? 201  ZN  B ZN  1 
HETATM 11145 S  S   . SO4 O  4 .   ? 73.408  1.050   12.178 1.00 55.75  ? 300  SO4 B S   1 
HETATM 11146 O  O1  . SO4 O  4 .   ? 73.658  -0.397  12.380 1.00 85.23  ? 300  SO4 B O1  1 
HETATM 11147 O  O2  . SO4 O  4 .   ? 73.978  1.829   13.298 1.00 43.59  ? 300  SO4 B O2  1 
HETATM 11148 O  O3  . SO4 O  4 .   ? 71.953  1.251   12.044 1.00 58.22  ? 300  SO4 B O3  1 
HETATM 11149 O  O4  . SO4 O  4 .   ? 74.105  1.488   10.954 1.00 64.35  ? 300  SO4 B O4  1 
HETATM 11150 CU CU  . CU1 P  2 .   ? 118.633 -14.334 18.685 1.00 40.65  ? 200  CU1 C CU  1 
HETATM 11151 ZN ZN  . ZN  Q  3 .   ? 121.573 -15.605 12.648 1.00 46.57  ? 201  ZN  C ZN  1 
HETATM 11152 CU CU  . CU1 R  2 .   ? 91.036  1.590   21.003 1.00 22.95  ? 200  CU1 D CU  1 
HETATM 11153 ZN ZN  . ZN  S  3 .   ? 87.980  4.357   15.583 1.00 20.65  ? 201  ZN  D ZN  1 
HETATM 11154 CU CU  . CU1 T  2 .   ? 38.374  -33.253 18.859 1.00 22.47  ? 200  CU1 E CU  1 
HETATM 11155 ZN ZN  . ZN  U  3 .   ? 35.537  -34.859 12.843 1.00 22.71  ? 201  ZN  E ZN  1 
HETATM 11156 CU CU  . CU1 V  2 .   ? 65.585  -16.865 21.098 1.00 21.44  ? 200  CU1 F CU  1 
HETATM 11157 ZN ZN  . ZN  W  3 .   ? 69.415  -15.411 15.649 1.00 21.56  ? 201  ZN  F ZN  1 
HETATM 11158 CU CU  . CU1 X  2 .   ? 144.558 -13.683 17.278 1.00 35.64  ? 200  CU1 G CU  1 
HETATM 11159 ZN ZN  . ZN  Y  3 .   ? 145.875 -16.758 11.343 1.00 44.41  ? 201  ZN  G ZN  1 
HETATM 11160 CU CU  . CU1 Z  2 .   ? 143.799 18.277  19.984 1.00 25.94  ? 200  CU1 H CU  1 
HETATM 11161 ZN ZN  . ZN  AA 3 .   ? 145.517 22.378  14.829 1.00 24.85  ? 201  ZN  H ZN  1 
HETATM 11162 CU CU  . CU1 BA 2 .   ? 87.808  46.616  12.395 1.00 35.83  ? 200  CU1 I CU  1 
HETATM 11163 ZN ZN  . ZN  CA 3 .   ? 84.969  48.038  6.327  1.00 40.07  ? 201  ZN  I ZN  1 
HETATM 11164 CU CU  . CU1 DA 2 .   ? 115.084 30.679  16.051 1.00 24.85  ? 200  CU1 J CU  1 
HETATM 11165 ZN ZN  . ZN  EA 3 .   ? 118.656 27.945  10.970 1.00 23.22  ? 201  ZN  J ZN  1 
HETATM 11166 S  S   . SO4 FA 4 .   ? 133.768 31.582  9.562  1.00 56.36  ? 301  SO4 J S   1 
HETATM 11167 O  O1  . SO4 FA 4 .   ? 132.582 30.885  10.109 1.00 87.19  ? 301  SO4 J O1  1 
HETATM 11168 O  O2  . SO4 FA 4 .   ? 134.822 31.653  10.590 1.00 87.12  ? 301  SO4 J O2  1 
HETATM 11169 O  O3  . SO4 FA 4 .   ? 133.367 32.951  9.163  1.00 83.21  ? 301  SO4 J O3  1 
HETATM 11170 O  O4  . SO4 FA 4 .   ? 134.268 30.839  8.387  1.00 88.32  ? 301  SO4 J O4  1 
HETATM 11171 S  S   . SO4 GA 4 .   ? 122.385 39.290  32.811 1.00 106.83 ? 302  SO4 J S   1 
HETATM 11172 O  O1  . SO4 GA 4 .   ? 120.937 39.004  32.707 1.00 128.69 ? 302  SO4 J O1  1 
HETATM 11173 O  O2  . SO4 GA 4 .   ? 123.155 38.099  32.415 1.00 105.26 ? 302  SO4 J O2  1 
HETATM 11174 O  O3  . SO4 GA 4 .   ? 122.701 39.640  34.209 1.00 121.08 ? 302  SO4 J O3  1 
HETATM 11175 O  O4  . SO4 GA 4 .   ? 122.725 40.428  31.934 1.00 52.40  ? 302  SO4 J O4  1 
HETATM 11176 O  O   . HOH HA 5 .   ? 67.052  48.404  19.070 1.00 34.93  ? 400  HOH A O   1 
HETATM 11177 O  O   . HOH HA 5 .   ? 67.107  37.135  21.089 1.00 41.76  ? 409  HOH A O   1 
HETATM 11178 O  O   . HOH HA 5 .   ? 58.978  31.797  21.553 1.00 23.27  ? 419  HOH A O   1 
HETATM 11179 O  O   . HOH HA 5 .   ? 52.934  46.916  36.951 1.00 37.25  ? 452  HOH A O   1 
HETATM 11180 O  O   . HOH HA 5 .   ? 47.520  33.722  23.956 1.00 44.18  ? 453  HOH A O   1 
HETATM 11181 O  O   . HOH HA 5 .   ? 53.968  50.079  4.819  1.00 40.01  ? 456  HOH A O   1 
HETATM 11182 O  O   . HOH HA 5 .   ? 52.156  32.441  5.120  1.00 29.40  ? 460  HOH A O   1 
HETATM 11183 O  O   . HOH HA 5 .   ? 49.891  48.773  13.337 1.00 27.25  ? 462  HOH A O   1 
HETATM 11184 O  O   . HOH HA 5 .   ? 72.017  45.371  17.223 1.00 19.80  ? 464  HOH A O   1 
HETATM 11185 O  O   . HOH HA 5 .   ? 68.330  31.476  20.009 1.00 21.55  ? 470  HOH A O   1 
HETATM 11186 O  O   . HOH HA 5 .   ? 52.548  53.939  11.491 1.00 28.25  ? 501  HOH A O   1 
HETATM 11187 O  O   . HOH HA 5 .   ? 68.946  46.326  25.623 1.00 34.69  ? 511  HOH A O   1 
HETATM 11188 O  O   . HOH HA 5 .   ? 49.224  31.933  4.837  1.00 35.78  ? 526  HOH A O   1 
HETATM 11189 O  O   . HOH HA 5 .   ? 61.748  42.305  31.781 1.00 32.18  ? 534  HOH A O   1 
HETATM 11190 O  O   . HOH HA 5 .   ? 49.773  41.759  35.436 1.00 31.27  ? 543  HOH A O   1 
HETATM 11191 O  O   . HOH HA 5 .   ? 61.046  47.474  4.213  1.00 27.00  ? 550  HOH A O   1 
HETATM 11192 O  O   . HOH HA 5 .   ? 44.340  52.154  32.092 1.00 42.40  ? 577  HOH A O   1 
HETATM 11193 O  O   . HOH HA 5 .   ? 50.451  47.207  11.075 1.00 33.64  ? 579  HOH A O   1 
HETATM 11194 O  O   . HOH HA 5 .   ? 75.425  33.031  18.338 1.00 29.81  ? 585  HOH A O   1 
HETATM 11195 O  O   . HOH HA 5 .   ? 61.019  32.761  25.178 1.00 35.41  ? 587  HOH A O   1 
HETATM 11196 O  O   . HOH HA 5 .   ? 58.342  48.910  31.092 1.00 30.05  ? 588  HOH A O   1 
HETATM 11197 O  O   . HOH HA 5 .   ? 48.881  40.659  -1.827 1.00 35.74  ? 602  HOH A O   1 
HETATM 11198 O  O   . HOH HA 5 .   ? 54.649  58.968  13.063 1.00 40.41  ? 607  HOH A O   1 
HETATM 11199 O  O   . HOH HA 5 .   ? 51.814  51.614  16.398 1.00 28.93  ? 609  HOH A O   1 
HETATM 11200 O  O   . HOH HA 5 .   ? 62.175  31.883  22.497 1.00 28.32  ? 611  HOH A O   1 
HETATM 11201 O  O   . HOH HA 5 .   ? 54.239  34.986  2.019  1.00 30.32  ? 617  HOH A O   1 
HETATM 11202 O  O   . HOH HA 5 .   ? 73.396  35.342  15.380 1.00 27.62  ? 621  HOH A O   1 
HETATM 11203 O  O   . HOH HA 5 .   ? 47.746  31.020  0.700  1.00 43.90  ? 632  HOH A O   1 
HETATM 11204 O  O   . HOH HA 5 .   ? 51.493  40.285  4.764  1.00 29.58  ? 638  HOH A O   1 
HETATM 11205 O  O   . HOH HA 5 .   ? 60.799  38.164  31.868 1.00 30.01  ? 653  HOH A O   1 
HETATM 11206 O  O   . HOH HA 5 .   ? 58.971  46.843  32.952 1.00 27.66  ? 655  HOH A O   1 
HETATM 11207 O  O   . HOH HA 5 .   ? 48.446  46.786  19.913 1.00 29.77  ? 662  HOH A O   1 
HETATM 11208 O  O   . HOH HA 5 .   ? 76.400  33.407  20.395 1.00 34.23  ? 679  HOH A O   1 
HETATM 11209 O  O   . HOH HA 5 .   ? 60.171  51.037  30.732 1.00 36.22  ? 697  HOH A O   1 
HETATM 11210 O  O   . HOH HA 5 .   ? 49.965  48.463  18.297 1.00 36.72  ? 702  HOH A O   1 
HETATM 11211 O  O   . HOH HA 5 .   ? 58.135  36.708  2.335  1.00 38.04  ? 706  HOH A O   1 
HETATM 11212 O  O   . HOH HA 5 .   ? 56.778  54.956  27.424 1.00 41.48  ? 710  HOH A O   1 
HETATM 11213 O  O   . HOH HA 5 .   ? 51.289  43.820  34.657 1.00 30.87  ? 730  HOH A O   1 
HETATM 11214 O  O   . HOH HA 5 .   ? 45.464  46.567  28.404 1.00 46.91  ? 731  HOH A O   1 
HETATM 11215 O  O   . HOH HA 5 .   ? 61.925  45.363  32.990 1.00 39.11  ? 736  HOH A O   1 
HETATM 11216 O  O   . HOH HA 5 .   ? 47.261  47.418  13.332 1.00 47.69  ? 762  HOH A O   1 
HETATM 11217 O  O   . HOH HA 5 .   ? 55.126  40.074  35.299 1.00 35.12  ? 763  HOH A O   1 
HETATM 11218 O  O   . HOH HA 5 .   ? 58.624  56.548  26.460 1.00 43.47  ? 779  HOH A O   1 
HETATM 11219 O  O   . HOH HA 5 .   ? 53.344  52.028  35.386 1.00 35.28  ? 787  HOH A O   1 
HETATM 11220 O  O   . HOH HA 5 .   ? 44.660  45.120  33.200 1.00 51.01  ? 816  HOH A O   1 
HETATM 11221 O  O   . HOH HA 5 .   ? 73.388  42.925  11.945 1.00 30.49  ? 832  HOH A O   1 
HETATM 11222 O  O   . HOH HA 5 .   ? 68.504  46.956  10.431 1.00 39.25  ? 845  HOH A O   1 
HETATM 11223 O  O   . HOH HA 5 .   ? 68.101  41.015  6.097  1.00 56.77  ? 853  HOH A O   1 
HETATM 11224 O  O   . HOH HA 5 .   ? 68.938  37.282  8.122  1.00 36.23  ? 858  HOH A O   1 
HETATM 11225 O  O   . HOH HA 5 .   ? 53.166  49.073  35.459 1.00 30.04  ? 861  HOH A O   1 
HETATM 11226 O  O   . HOH HA 5 .   ? 48.455  30.899  25.109 1.00 52.08  ? 863  HOH A O   1 
HETATM 11227 O  O   . HOH HA 5 .   ? 48.663  47.639  22.580 1.00 30.32  ? 864  HOH A O   1 
HETATM 11228 O  O   . HOH HA 5 .   ? 73.282  46.584  15.007 1.00 43.82  ? 877  HOH A O   1 
HETATM 11229 O  O   . HOH HA 5 .   ? 65.244  36.632  26.495 1.00 55.58  ? 878  HOH A O   1 
HETATM 11230 O  O   . HOH HA 5 .   ? 49.641  31.161  18.149 1.00 35.26  ? 880  HOH A O   1 
HETATM 11231 O  O   . HOH HA 5 .   ? 54.999  34.104  29.034 1.00 38.89  ? 881  HOH A O   1 
HETATM 11232 O  O   . HOH HA 5 .   ? 52.975  35.381  30.160 1.00 48.09  ? 882  HOH A O   1 
HETATM 11233 O  O   . HOH HA 5 .   ? 48.373  35.947  24.974 1.00 34.51  ? 884  HOH A O   1 
HETATM 11234 O  O   . HOH HA 5 .   ? 49.262  30.872  22.110 1.00 38.79  ? 885  HOH A O   1 
HETATM 11235 O  O   . HOH HA 5 .   ? 46.184  36.647  5.234  1.00 32.76  ? 886  HOH A O   1 
HETATM 11236 O  O   . HOH HA 5 .   ? 45.016  36.578  8.537  1.00 45.26  ? 887  HOH A O   1 
HETATM 11237 O  O   . HOH HA 5 .   ? 44.591  40.801  15.671 1.00 45.78  ? 895  HOH A O   1 
HETATM 11238 O  O   . HOH HA 5 .   ? 51.836  37.648  36.565 1.00 36.33  ? 896  HOH A O   1 
HETATM 11239 O  O   . HOH HA 5 .   ? 48.098  39.995  33.429 1.00 38.07  ? 897  HOH A O   1 
HETATM 11240 O  O   . HOH HA 5 .   ? 48.453  37.779  35.811 1.00 51.38  ? 898  HOH A O   1 
HETATM 11241 O  O   . HOH HA 5 .   ? 53.075  44.181  36.440 1.00 31.59  ? 899  HOH A O   1 
HETATM 11242 O  O   . HOH HA 5 .   ? 48.384  53.638  28.899 1.00 65.42  ? 901  HOH A O   1 
HETATM 11243 O  O   . HOH HA 5 .   ? 49.484  51.059  20.976 1.00 44.57  ? 903  HOH A O   1 
HETATM 11244 O  O   . HOH HA 5 .   ? 52.319  54.502  18.094 1.00 30.06  ? 904  HOH A O   1 
HETATM 11245 O  O   . HOH HA 5 .   ? 55.613  59.471  15.487 1.00 38.87  ? 909  HOH A O   1 
HETATM 11246 O  O   . HOH HA 5 .   ? 55.689  58.362  24.807 1.00 53.25  ? 911  HOH A O   1 
HETATM 11247 O  O   . HOH HA 5 .   ? 67.869  42.846  8.411  1.00 41.06  ? 912  HOH A O   1 
HETATM 11248 O  O   . HOH HA 5 .   ? 72.065  42.756  9.650  1.00 41.21  ? 913  HOH A O   1 
HETATM 11249 O  O   . HOH HA 5 .   ? 69.862  33.099  27.188 1.00 48.85  ? 916  HOH A O   1 
HETATM 11250 O  O   . HOH HA 5 .   ? 72.092  31.711  26.810 1.00 42.39  ? 917  HOH A O   1 
HETATM 11251 O  O   . HOH HA 5 .   ? 65.650  31.198  25.890 1.00 40.05  ? 918  HOH A O   1 
HETATM 11252 O  O   . HOH HA 5 .   ? 67.506  48.869  13.935 1.00 29.89  ? 942  HOH A O   1 
HETATM 11253 O  O   . HOH HA 5 .   ? 66.246  50.419  20.853 1.00 35.26  ? 943  HOH A O   1 
HETATM 11254 O  O   . HOH HA 5 .   ? 63.175  35.456  5.964  1.00 46.59  ? 944  HOH A O   1 
HETATM 11255 O  O   . HOH HA 5 .   ? 57.145  48.945  3.302  1.00 51.51  ? 945  HOH A O   1 
HETATM 11256 O  O   . HOH HA 5 .   ? 50.605  46.972  7.797  1.00 33.71  ? 946  HOH A O   1 
HETATM 11257 O  O   . HOH HA 5 .   ? 49.245  51.319  13.345 1.00 37.23  ? 947  HOH A O   1 
HETATM 11258 O  O   . HOH HA 5 .   ? 51.415  48.845  15.781 1.00 27.61  ? 949  HOH A O   1 
HETATM 11259 O  O   . HOH HA 5 .   ? 51.588  53.606  14.340 1.00 35.49  ? 950  HOH A O   1 
HETATM 11260 O  O   . HOH HA 5 .   ? 46.881  47.837  25.437 1.00 50.86  ? 970  HOH A O   1 
HETATM 11261 O  O   . HOH HA 5 .   ? 45.598  43.577  34.941 1.00 56.09  ? 971  HOH A O   1 
HETATM 11262 O  O   . HOH HA 5 .   ? 52.885  44.310  1.311  1.00 59.73  ? 972  HOH A O   1 
HETATM 11263 O  O   . HOH HA 5 .   ? 58.240  29.652  3.377  1.00 48.99  ? 973  HOH A O   1 
HETATM 11264 O  O   . HOH HA 5 .   ? 61.093  57.431  22.860 1.00 41.23  ? 974  HOH A O   1 
HETATM 11265 O  O   . HOH HA 5 .   ? 72.039  63.869  15.518 1.00 78.11  ? 976  HOH A O   1 
HETATM 11266 O  O   . HOH HA 5 .   ? 68.134  48.391  21.375 1.00 50.24  ? 977  HOH A O   1 
HETATM 11267 O  O   . HOH HA 5 .   ? 70.790  49.164  19.324 1.00 58.04  ? 978  HOH A O   1 
HETATM 11268 O  O   . HOH HA 5 .   ? 70.552  48.150  17.278 1.00 47.04  ? 979  HOH A O   1 
HETATM 11269 O  O   . HOH HA 5 .   ? 67.959  48.034  16.667 1.00 38.66  ? 980  HOH A O   1 
HETATM 11270 O  O   . HOH HA 5 .   ? 53.490  56.749  26.391 1.00 40.21  ? 1084 HOH A O   1 
HETATM 11271 O  O   . HOH HA 5 .   ? 50.948  52.701  36.576 1.00 48.64  ? 1139 HOH A O   1 
HETATM 11272 O  O   . HOH HA 5 .   ? 60.452  30.709  26.464 1.00 42.04  ? 1150 HOH A O   1 
HETATM 11273 O  O   . HOH HA 5 .   ? 70.141  35.157  28.767 1.00 36.94  ? 1153 HOH A O   1 
HETATM 11274 O  O   . HOH HA 5 .   ? 59.386  42.312  2.631  1.00 43.09  ? 1260 HOH A O   1 
HETATM 11275 O  O   . HOH HA 5 .   ? 51.185  26.928  10.890 1.00 40.11  ? 1265 HOH A O   1 
HETATM 11276 O  O   . HOH HA 5 .   ? 67.148  39.378  27.786 1.00 40.36  ? 1285 HOH A O   1 
HETATM 11277 O  O   . HOH HA 5 .   ? 65.022  42.027  30.478 1.00 47.34  ? 1290 HOH A O   1 
HETATM 11278 O  O   . HOH HA 5 .   ? 63.264  61.778  12.199 1.00 39.80  ? 1291 HOH A O   1 
HETATM 11279 O  O   . HOH HA 5 .   ? 65.389  37.923  4.131  1.00 51.78  ? 1311 HOH A O   1 
HETATM 11280 O  O   . HOH HA 5 .   ? 51.786  49.006  5.816  1.00 45.38  ? 1317 HOH A O   1 
HETATM 11281 O  O   . HOH HA 5 .   ? 47.312  45.254  7.329  1.00 42.34  ? 1321 HOH A O   1 
HETATM 11282 O  O   . HOH HA 5 .   ? 55.485  57.590  19.226 1.00 38.35  ? 1323 HOH A O   1 
HETATM 11283 O  O   . HOH HA 5 .   ? 62.166  60.659  19.895 1.00 45.68  ? 1326 HOH A O   1 
HETATM 11284 O  O   . HOH HA 5 .   ? 49.203  35.976  32.419 1.00 54.47  ? 1333 HOH A O   1 
HETATM 11285 O  O   . HOH HA 5 .   ? 56.400  59.104  21.664 1.00 47.43  ? 1336 HOH A O   1 
HETATM 11286 O  O   . HOH HA 5 .   ? 57.982  50.742  14.287 1.00 26.13  ? 1342 HOH A O   1 
HETATM 11287 O  O   . HOH HA 5 .   ? 63.234  46.179  5.166  1.00 26.30  ? 1343 HOH A O   1 
HETATM 11288 O  O   . HOH HA 5 .   ? 58.239  39.042  6.634  1.00 33.22  ? 1362 HOH A O   1 
HETATM 11289 O  O   . HOH HA 5 .   ? 71.331  45.965  22.248 1.00 38.15  ? 1364 HOH A O   1 
HETATM 11290 O  O   . HOH HA 5 .   ? 54.289  58.769  17.661 1.00 40.20  ? 1365 HOH A O   1 
HETATM 11291 O  O   . HOH HA 5 .   ? 57.425  34.288  30.136 1.00 61.79  ? 1378 HOH A O   1 
HETATM 11292 O  O   . HOH HA 5 .   ? 48.654  31.718  16.150 1.00 55.17  ? 1382 HOH A O   1 
HETATM 11293 O  O   . HOH HA 5 .   ? 44.410  40.882  21.995 1.00 49.02  ? 1392 HOH A O   1 
HETATM 11294 O  O   . HOH HA 5 .   ? 63.452  34.782  25.511 1.00 40.34  ? 1408 HOH A O   1 
HETATM 11295 O  O   . HOH HA 5 .   ? 71.689  43.258  18.981 1.00 40.89  ? 1426 HOH A O   1 
HETATM 11296 O  O   . HOH HA 5 .   ? 44.589  46.482  21.956 1.00 39.46  ? 1434 HOH A O   1 
HETATM 11297 O  O   . HOH HA 5 .   ? 58.580  47.177  3.318  1.00 39.74  ? 1445 HOH A O   1 
HETATM 11298 O  O   . HOH HA 5 .   ? 69.997  44.763  24.340 1.00 45.03  ? 1458 HOH A O   1 
HETATM 11299 O  O   . HOH HA 5 .   ? 69.493  50.180  5.497  1.00 46.45  ? 1462 HOH A O   1 
HETATM 11300 O  O   . HOH HA 5 .   ? 69.314  49.140  11.571 1.00 39.82  ? 1466 HOH A O   1 
HETATM 11301 O  O   . HOH HA 5 .   ? 58.425  40.512  3.684  1.00 55.83  ? 1475 HOH A O   1 
HETATM 11302 O  O   . HOH HA 5 .   ? 59.451  33.874  -1.764 1.00 42.70  ? 1476 HOH A O   1 
HETATM 11303 O  O   . HOH HA 5 .   ? 57.002  56.514  4.344  1.00 51.74  ? 1477 HOH A O   1 
HETATM 11304 O  O   . HOH HA 5 .   ? 54.199  55.922  11.277 1.00 47.49  ? 1478 HOH A O   1 
HETATM 11305 O  O   . HOH HA 5 .   ? 50.104  36.261  27.584 1.00 45.60  ? 1544 HOH A O   1 
HETATM 11306 O  O   . HOH HA 5 .   ? 61.818  31.904  4.454  1.00 58.64  ? 1565 HOH A O   1 
HETATM 11307 O  O   . HOH IA 5 .   ? 58.848  12.807  22.160 1.00 31.42  ? 401  HOH B O   1 
HETATM 11308 O  O   . HOH IA 5 .   ? 59.987  25.541  22.343 1.00 35.70  ? 410  HOH B O   1 
HETATM 11309 O  O   . HOH IA 5 .   ? 66.498  29.544  20.966 1.00 20.88  ? 420  HOH B O   1 
HETATM 11310 O  O   . HOH IA 5 .   ? 61.321  11.142  21.998 1.00 39.62  ? 430  HOH B O   1 
HETATM 11311 O  O   . HOH IA 5 .   ? 74.936  11.742  7.537  1.00 58.16  ? 445  HOH B O   1 
HETATM 11312 O  O   . HOH IA 5 .   ? 67.941  12.154  32.719 1.00 29.69  ? 466  HOH B O   1 
HETATM 11313 O  O   . HOH IA 5 .   ? 60.973  -1.711  16.970 1.00 23.81  ? 468  HOH B O   1 
HETATM 11314 O  O   . HOH IA 5 .   ? 73.182  11.294  17.201 1.00 24.24  ? 472  HOH B O   1 
HETATM 11315 O  O   . HOH IA 5 .   ? 71.105  5.825   13.434 1.00 23.23  ? 473  HOH B O   1 
HETATM 11316 O  O   . HOH IA 5 .   ? 73.054  6.961   14.997 1.00 24.36  ? 474  HOH B O   1 
HETATM 11317 O  O   . HOH IA 5 .   ? 56.964  11.594  17.532 1.00 23.57  ? 476  HOH B O   1 
HETATM 11318 O  O   . HOH IA 5 .   ? 73.532  5.637   28.531 1.00 34.67  ? 488  HOH B O   1 
HETATM 11319 O  O   . HOH IA 5 .   ? 53.478  15.507  21.398 1.00 32.44  ? 493  HOH B O   1 
HETATM 11320 O  O   . HOH IA 5 .   ? 76.399  12.635  13.021 1.00 27.45  ? 495  HOH B O   1 
HETATM 11321 O  O   . HOH IA 5 .   ? 80.134  14.878  25.627 1.00 23.56  ? 497  HOH B O   1 
HETATM 11322 O  O   . HOH IA 5 .   ? 72.190  12.306  7.719  1.00 36.46  ? 500  HOH B O   1 
HETATM 11323 O  O   . HOH IA 5 .   ? 64.395  21.115  2.665  1.00 30.80  ? 503  HOH B O   1 
HETATM 11324 O  O   . HOH IA 5 .   ? 78.206  5.288   12.917 1.00 30.38  ? 506  HOH B O   1 
HETATM 11325 O  O   . HOH IA 5 .   ? 67.004  24.409  32.315 1.00 33.09  ? 507  HOH B O   1 
HETATM 11326 O  O   . HOH IA 5 .   ? 55.603  17.300  11.476 1.00 29.14  ? 510  HOH B O   1 
HETATM 11327 O  O   . HOH IA 5 .   ? 58.523  24.111  23.388 1.00 30.52  ? 512  HOH B O   1 
HETATM 11328 O  O   . HOH IA 5 .   ? 79.085  12.553  17.014 1.00 32.21  ? 514  HOH B O   1 
HETATM 11329 O  O   . HOH IA 5 .   ? 55.566  8.204   13.890 1.00 28.52  ? 523  HOH B O   1 
HETATM 11330 O  O   . HOH IA 5 .   ? 51.216  25.050  18.654 1.00 27.04  ? 530  HOH B O   1 
HETATM 11331 O  O   . HOH IA 5 .   ? 67.937  2.584   13.948 1.00 25.11  ? 531  HOH B O   1 
HETATM 11332 O  O   . HOH IA 5 .   ? 69.921  3.452   21.636 1.00 30.06  ? 532  HOH B O   1 
HETATM 11333 O  O   . HOH IA 5 .   ? 63.335  29.371  22.696 1.00 31.03  ? 537  HOH B O   1 
HETATM 11334 O  O   . HOH IA 5 .   ? 61.292  11.501  6.847  1.00 28.16  ? 546  HOH B O   1 
HETATM 11335 O  O   . HOH IA 5 .   ? 66.045  20.497  33.007 1.00 27.20  ? 548  HOH B O   1 
HETATM 11336 O  O   . HOH IA 5 .   ? 82.293  15.960  27.035 1.00 27.34  ? 551  HOH B O   1 
HETATM 11337 O  O   . HOH IA 5 .   ? 66.392  0.280   24.482 1.00 31.27  ? 560  HOH B O   1 
HETATM 11338 O  O   . HOH IA 5 .   ? 65.096  1.466   13.108 1.00 33.51  ? 563  HOH B O   1 
HETATM 11339 O  O   . HOH IA 5 .   ? 59.721  23.223  7.153  1.00 31.01  ? 564  HOH B O   1 
HETATM 11340 O  O   . HOH IA 5 .   ? 63.608  1.926   26.344 1.00 30.96  ? 566  HOH B O   1 
HETATM 11341 O  O   . HOH IA 5 .   ? 75.676  11.636  35.931 1.00 36.41  ? 574  HOH B O   1 
HETATM 11342 O  O   . HOH IA 5 .   ? 83.357  13.608  25.967 1.00 27.93  ? 584  HOH B O   1 
HETATM 11343 O  O   . HOH IA 5 .   ? 72.910  12.481  11.398 1.00 30.29  ? 586  HOH B O   1 
HETATM 11344 O  O   . HOH IA 5 .   ? 73.828  9.951   11.154 1.00 31.21  ? 593  HOH B O   1 
HETATM 11345 O  O   . HOH IA 5 .   ? 69.979  2.794   24.146 1.00 34.73  ? 603  HOH B O   1 
HETATM 11346 O  O   . HOH IA 5 .   ? 65.124  9.629   5.360  1.00 37.20  ? 608  HOH B O   1 
HETATM 11347 O  O   . HOH IA 5 .   ? 66.960  -3.642  19.955 1.00 36.09  ? 615  HOH B O   1 
HETATM 11348 O  O   . HOH IA 5 .   ? 68.794  1.158   19.977 1.00 28.73  ? 634  HOH B O   1 
HETATM 11349 O  O   . HOH IA 5 .   ? 52.893  -1.237  21.263 1.00 34.07  ? 641  HOH B O   1 
HETATM 11350 O  O   . HOH IA 5 .   ? 57.033  12.984  20.365 1.00 31.30  ? 642  HOH B O   1 
HETATM 11351 O  O   . HOH IA 5 .   ? 63.667  0.299   24.023 1.00 26.52  ? 646  HOH B O   1 
HETATM 11352 O  O   . HOH IA 5 .   ? 65.777  18.154  34.513 1.00 34.18  ? 665  HOH B O   1 
HETATM 11353 O  O   . HOH IA 5 .   ? 54.233  0.879   23.140 1.00 36.50  ? 666  HOH B O   1 
HETATM 11354 O  O   . HOH IA 5 .   ? 57.072  29.787  21.425 1.00 22.74  ? 668  HOH B O   1 
HETATM 11355 O  O   . HOH IA 5 .   ? 75.382  14.106  6.624  1.00 37.22  ? 672  HOH B O   1 
HETATM 11356 O  O   . HOH IA 5 .   ? 77.702  22.625  6.652  1.00 44.22  ? 676  HOH B O   1 
HETATM 11357 O  O   . HOH IA 5 .   ? 57.959  16.017  29.192 1.00 38.34  ? 685  HOH B O   1 
HETATM 11358 O  O   . HOH IA 5 .   ? 67.856  2.296   6.262  1.00 39.49  ? 689  HOH B O   1 
HETATM 11359 O  O   . HOH IA 5 .   ? 79.441  36.016  11.880 1.00 32.68  ? 693  HOH B O   1 
HETATM 11360 O  O   . HOH IA 5 .   ? 80.847  20.413  20.501 1.00 27.31  ? 696  HOH B O   1 
HETATM 11361 O  O   . HOH IA 5 .   ? 73.350  11.539  37.764 1.00 41.73  ? 703  HOH B O   1 
HETATM 11362 O  O   . HOH IA 5 .   ? 70.443  8.167   29.820 1.00 40.86  ? 713  HOH B O   1 
HETATM 11363 O  O   . HOH IA 5 .   ? 76.176  22.131  3.612  1.00 33.58  ? 719  HOH B O   1 
HETATM 11364 O  O   . HOH IA 5 .   ? 61.097  4.551   4.150  1.00 72.54  ? 728  HOH B O   1 
HETATM 11365 O  O   . HOH IA 5 .   ? 77.815  39.333  10.058 1.00 33.87  ? 732  HOH B O   1 
HETATM 11366 O  O   . HOH IA 5 .   ? 67.377  2.955   24.303 1.00 36.96  ? 734  HOH B O   1 
HETATM 11367 O  O   . HOH IA 5 .   ? 62.443  20.458  32.214 1.00 40.73  ? 741  HOH B O   1 
HETATM 11368 O  O   . HOH IA 5 .   ? 65.283  2.369   7.277  1.00 36.44  ? 748  HOH B O   1 
HETATM 11369 O  O   . HOH IA 5 .   ? 83.321  10.904  31.016 1.00 34.40  ? 749  HOH B O   1 
HETATM 11370 O  O   . HOH IA 5 .   ? 69.557  14.317  32.630 1.00 25.16  ? 765  HOH B O   1 
HETATM 11371 O  O   . HOH IA 5 .   ? 81.390  21.680  22.775 1.00 36.73  ? 772  HOH B O   1 
HETATM 11372 O  O   . HOH IA 5 .   ? 63.691  2.981   10.952 1.00 34.40  ? 778  HOH B O   1 
HETATM 11373 O  O   . HOH IA 5 .   ? 69.352  16.324  34.428 1.00 39.28  ? 783  HOH B O   1 
HETATM 11374 O  O   . HOH IA 5 .   ? 54.008  21.921  10.820 1.00 40.96  ? 790  HOH B O   1 
HETATM 11375 O  O   . HOH IA 5 .   ? 65.175  -4.721  17.455 1.00 39.07  ? 795  HOH B O   1 
HETATM 11376 O  O   . HOH IA 5 .   ? 72.604  -0.202  22.400 1.00 33.66  ? 798  HOH B O   1 
HETATM 11377 O  O   . HOH IA 5 .   ? 61.577  27.684  23.821 1.00 42.78  ? 801  HOH B O   1 
HETATM 11378 O  O   . HOH IA 5 .   ? 70.676  -0.710  26.136 1.00 48.89  ? 803  HOH B O   1 
HETATM 11379 O  O   . HOH IA 5 .   ? 62.878  27.163  26.028 1.00 41.49  ? 808  HOH B O   1 
HETATM 11380 O  O   . HOH IA 5 .   ? 67.051  4.101   28.383 1.00 38.11  ? 822  HOH B O   1 
HETATM 11381 O  O   . HOH IA 5 .   ? 68.250  -0.533  22.211 1.00 35.71  ? 823  HOH B O   1 
HETATM 11382 O  O   . HOH IA 5 .   ? 59.703  11.000  24.422 1.00 31.34  ? 826  HOH B O   1 
HETATM 11383 O  O   . HOH IA 5 .   ? 62.841  -0.182  13.097 1.00 55.28  ? 830  HOH B O   1 
HETATM 11384 O  O   . HOH IA 5 .   ? 71.072  2.983   26.740 1.00 43.69  ? 833  HOH B O   1 
HETATM 11385 O  O   . HOH IA 5 .   ? 53.593  16.963  23.516 1.00 37.75  ? 848  HOH B O   1 
HETATM 11386 O  O   . HOH IA 5 .   ? 68.352  8.756   6.549  1.00 42.32  ? 850  HOH B O   1 
HETATM 11387 O  O   . HOH IA 5 .   ? 65.319  4.188   26.189 1.00 29.16  ? 857  HOH B O   1 
HETATM 11388 O  O   . HOH IA 5 .   ? 77.856  25.920  22.767 1.00 34.40  ? 862  HOH B O   1 
HETATM 11389 O  O   . HOH IA 5 .   ? 64.307  12.983  3.201  1.00 50.11  ? 865  HOH B O   1 
HETATM 11390 O  O   . HOH IA 5 .   ? 67.469  -0.053  26.815 1.00 41.46  ? 868  HOH B O   1 
HETATM 11391 O  O   . HOH IA 5 .   ? 56.318  29.410  28.788 1.00 58.83  ? 883  HOH B O   1 
HETATM 11392 O  O   . HOH IA 5 .   ? 71.159  35.443  8.901  1.00 37.88  ? 914  HOH B O   1 
HETATM 11393 O  O   . HOH IA 5 .   ? 73.238  37.493  7.860  1.00 43.30  ? 915  HOH B O   1 
HETATM 11394 O  O   . HOH IA 5 .   ? 65.116  28.764  25.214 1.00 36.71  ? 919  HOH B O   1 
HETATM 11395 O  O   . HOH IA 5 .   ? 76.459  30.416  19.411 1.00 39.13  ? 920  HOH B O   1 
HETATM 11396 O  O   . HOH IA 5 .   ? 50.868  17.801  15.094 1.00 52.82  ? 923  HOH B O   1 
HETATM 11397 O  O   . HOH IA 5 .   ? 53.248  13.803  9.964  1.00 44.17  ? 924  HOH B O   1 
HETATM 11398 O  O   . HOH IA 5 .   ? 54.157  5.840   8.810  1.00 54.65  ? 925  HOH B O   1 
HETATM 11399 O  O   . HOH IA 5 .   ? 76.589  11.549  10.374 1.00 50.02  ? 961  HOH B O   1 
HETATM 11400 O  O   . HOH IA 5 .   ? 57.850  13.387  24.905 1.00 38.40  ? 967  HOH B O   1 
HETATM 11401 O  O   . HOH IA 5 .   ? 58.833  25.974  7.412  1.00 48.26  ? 981  HOH B O   1 
HETATM 11402 O  O   . HOH IA 5 .   ? 51.301  22.633  20.403 1.00 34.34  ? 982  HOH B O   1 
HETATM 11403 O  O   . HOH IA 5 .   ? 70.868  -3.750  13.586 1.00 40.84  ? 987  HOH B O   1 
HETATM 11404 O  O   . HOH IA 5 .   ? 76.964  19.496  34.029 1.00 34.97  ? 1001 HOH B O   1 
HETATM 11405 O  O   . HOH IA 5 .   ? 76.647  24.692  28.169 1.00 62.22  ? 1002 HOH B O   1 
HETATM 11406 O  O   . HOH IA 5 .   ? 76.603  26.239  26.170 1.00 45.21  ? 1003 HOH B O   1 
HETATM 11407 O  O   . HOH IA 5 .   ? 74.308  9.338   8.733  1.00 53.86  ? 1025 HOH B O   1 
HETATM 11408 O  O   . HOH IA 5 .   ? 68.339  5.854   29.122 1.00 40.87  ? 1030 HOH B O   1 
HETATM 11409 O  O   . HOH IA 5 .   ? 79.031  22.019  33.753 1.00 42.91  ? 1093 HOH B O   1 
HETATM 11410 O  O   . HOH IA 5 .   ? 79.649  23.114  31.056 1.00 38.88  ? 1094 HOH B O   1 
HETATM 11411 O  O   . HOH IA 5 .   ? 82.256  22.115  29.710 1.00 55.88  ? 1095 HOH B O   1 
HETATM 11412 O  O   . HOH IA 5 .   ? 83.459  19.748  28.462 1.00 44.37  ? 1096 HOH B O   1 
HETATM 11413 O  O   . HOH IA 5 .   ? 61.723  2.919   12.239 1.00 38.59  ? 1102 HOH B O   1 
HETATM 11414 O  O   . HOH IA 5 .   ? 61.593  -3.888  15.646 1.00 38.35  ? 1103 HOH B O   1 
HETATM 11415 O  O   . HOH IA 5 .   ? 50.421  -1.309  20.985 1.00 42.77  ? 1104 HOH B O   1 
HETATM 11416 O  O   . HOH IA 5 .   ? 78.785  31.158  15.052 1.00 32.55  ? 1143 HOH B O   1 
HETATM 11417 O  O   . HOH IA 5 .   ? 74.989  29.592  15.338 1.00 34.58  ? 1144 HOH B O   1 
HETATM 11418 O  O   . HOH IA 5 .   ? 72.075  32.408  8.391  1.00 33.21  ? 1145 HOH B O   1 
HETATM 11419 O  O   . HOH IA 5 .   ? 67.583  21.900  1.422  1.00 44.53  ? 1146 HOH B O   1 
HETATM 11420 O  O   . HOH IA 5 .   ? 67.561  17.275  3.138  1.00 69.05  ? 1147 HOH B O   1 
HETATM 11421 O  O   . HOH IA 5 .   ? 66.556  14.421  2.605  1.00 46.21  ? 1148 HOH B O   1 
HETATM 11422 O  O   . HOH IA 5 .   ? 55.687  13.206  14.203 1.00 45.43  ? 1159 HOH B O   1 
HETATM 11423 O  O   . HOH IA 5 .   ? 49.947  28.279  20.918 1.00 38.48  ? 1198 HOH B O   1 
HETATM 11424 O  O   . HOH IA 5 .   ? 83.158  17.991  30.945 1.00 34.33  ? 1211 HOH B O   1 
HETATM 11425 O  O   . HOH IA 5 .   ? 54.738  12.877  21.216 1.00 44.29  ? 1223 HOH B O   1 
HETATM 11426 O  O   . HOH IA 5 .   ? 67.217  10.148  35.009 1.00 44.57  ? 1263 HOH B O   1 
HETATM 11427 O  O   . HOH IA 5 .   ? 59.554  23.195  29.878 1.00 43.71  ? 1272 HOH B O   1 
HETATM 11428 O  O   . HOH IA 5 .   ? 55.027  18.562  8.990  1.00 44.43  ? 1307 HOH B O   1 
HETATM 11429 O  O   . HOH IA 5 .   ? 84.823  15.004  29.472 1.00 37.85  ? 1310 HOH B O   1 
HETATM 11430 O  O   . HOH IA 5 .   ? 70.345  -0.142  23.933 1.00 39.14  ? 1314 HOH B O   1 
HETATM 11431 O  O   . HOH IA 5 .   ? 65.801  13.444  34.793 1.00 50.90  ? 1322 HOH B O   1 
HETATM 11432 O  O   . HOH IA 5 .   ? 63.823  -2.833  13.848 1.00 35.52  ? 1325 HOH B O   1 
HETATM 11433 O  O   . HOH IA 5 .   ? 81.588  20.647  34.702 1.00 44.87  ? 1327 HOH B O   1 
HETATM 11434 O  O   . HOH IA 5 .   ? 74.045  8.075   34.199 1.00 46.83  ? 1331 HOH B O   1 
HETATM 11435 O  O   . HOH IA 5 .   ? 55.223  10.587  16.176 1.00 46.69  ? 1339 HOH B O   1 
HETATM 11436 O  O   . HOH IA 5 .   ? 54.924  15.662  25.930 1.00 42.49  ? 1341 HOH B O   1 
HETATM 11437 O  O   . HOH IA 5 .   ? 66.395  9.460   16.537 1.00 19.74  ? 1344 HOH B O   1 
HETATM 11438 O  O   . HOH IA 5 .   ? 59.543  12.959  8.030  1.00 22.46  ? 1345 HOH B O   1 
HETATM 11439 O  O   . HOH IA 5 .   ? 63.397  11.704  5.229  1.00 38.44  ? 1400 HOH B O   1 
HETATM 11440 O  O   . HOH IA 5 .   ? 53.431  9.373   10.856 1.00 53.63  ? 1420 HOH B O   1 
HETATM 11441 O  O   . HOH IA 5 .   ? 48.589  28.841  19.001 1.00 54.43  ? 1427 HOH B O   1 
HETATM 11442 O  O   . HOH IA 5 .   ? 71.714  16.924  2.220  1.00 44.95  ? 1455 HOH B O   1 
HETATM 11443 O  O   . HOH IA 5 .   ? 70.319  19.203  4.205  1.00 49.22  ? 1456 HOH B O   1 
HETATM 11444 O  O   . HOH IA 5 .   ? 70.395  26.443  3.264  1.00 48.31  ? 1460 HOH B O   1 
HETATM 11445 O  O   . HOH IA 5 .   ? 60.786  24.939  28.411 1.00 51.13  ? 1461 HOH B O   1 
HETATM 11446 O  O   . HOH IA 5 .   ? 58.773  8.102   25.093 1.00 51.06  ? 1528 HOH B O   1 
HETATM 11447 O  O   . HOH IA 5 .   ? 56.025  4.413   7.114  1.00 44.06  ? 1576 HOH B O   1 
HETATM 11448 O  O   . HOH JA 5 .   ? 118.557 -18.516 18.932 1.00 43.96  ? 402  HOH C O   1 
HETATM 11449 O  O   . HOH JA 5 .   ? 108.070 -11.121 20.978 1.00 35.07  ? 411  HOH C O   1 
HETATM 11450 O  O   . HOH JA 5 .   ? 107.666 -3.784  21.570 1.00 27.05  ? 421  HOH C O   1 
HETATM 11451 O  O   . HOH JA 5 .   ? 107.127 -9.655  23.072 1.00 37.98  ? 434  HOH C O   1 
HETATM 11452 O  O   . HOH JA 5 .   ? 102.984 -11.785 20.164 1.00 23.74  ? 489  HOH C O   1 
HETATM 11453 O  O   . HOH JA 5 .   ? 113.613 -21.507 17.326 1.00 37.37  ? 509  HOH C O   1 
HETATM 11454 O  O   . HOH JA 5 .   ? 112.962 -1.140  1.915  1.00 33.56  ? 624  HOH C O   1 
HETATM 11455 O  O   . HOH JA 5 .   ? 122.686 -11.380 30.941 1.00 44.77  ? 625  HOH C O   1 
HETATM 11456 O  O   . HOH JA 5 .   ? 108.480 -9.536  25.499 1.00 46.93  ? 631  HOH C O   1 
HETATM 11457 O  O   . HOH JA 5 .   ? 106.247 -6.562  22.549 1.00 27.35  ? 633  HOH C O   1 
HETATM 11458 O  O   . HOH JA 5 .   ? 121.884 -2.787  34.948 1.00 44.31  ? 637  HOH C O   1 
HETATM 11459 O  O   . HOH JA 5 .   ? 108.627 -13.677 21.539 1.00 34.67  ? 675  HOH C O   1 
HETATM 11460 O  O   . HOH JA 5 .   ? 107.224 5.415   11.044 1.00 46.45  ? 709  HOH C O   1 
HETATM 11461 O  O   . HOH JA 5 .   ? 105.684 6.210   18.390 1.00 33.22  ? 754  HOH C O   1 
HETATM 11462 O  O   . HOH JA 5 .   ? 111.334 5.483   22.179 1.00 41.59  ? 770  HOH C O   1 
HETATM 11463 O  O   . HOH JA 5 .   ? 115.458 -19.277 25.809 1.00 46.27  ? 793  HOH C O   1 
HETATM 11464 O  O   . HOH JA 5 .   ? 107.926 -6.222  25.073 1.00 40.59  ? 797  HOH C O   1 
HETATM 11465 O  O   . HOH JA 5 .   ? 111.491 5.136   18.033 1.00 40.69  ? 800  HOH C O   1 
HETATM 11466 O  O   . HOH JA 5 .   ? 129.889 -15.168 26.467 1.00 46.82  ? 802  HOH C O   1 
HETATM 11467 O  O   . HOH JA 5 .   ? 122.863 -6.385  35.835 1.00 35.41  ? 804  HOH C O   1 
HETATM 11468 O  O   . HOH JA 5 .   ? 125.767 -0.947  19.929 1.00 43.46  ? 815  HOH C O   1 
HETATM 11469 O  O   . HOH JA 5 .   ? 112.304 -21.453 19.779 1.00 49.50  ? 926  HOH C O   1 
HETATM 11470 O  O   . HOH JA 5 .   ? 107.910 -15.405 8.589  1.00 41.64  ? 953  HOH C O   1 
HETATM 11471 O  O   . HOH JA 5 .   ? 113.499 -14.882 36.113 1.00 49.44  ? 1029 HOH C O   1 
HETATM 11472 O  O   . HOH JA 5 .   ? 104.043 -9.848  25.843 1.00 37.13  ? 1062 HOH C O   1 
HETATM 11473 O  O   . HOH JA 5 .   ? 112.622 -8.386  32.087 1.00 32.61  ? 1064 HOH C O   1 
HETATM 11474 O  O   . HOH JA 5 .   ? 115.443 -11.146 31.655 1.00 36.80  ? 1065 HOH C O   1 
HETATM 11475 O  O   . HOH JA 5 .   ? 117.789 -13.002 32.512 1.00 42.94  ? 1066 HOH C O   1 
HETATM 11476 O  O   . HOH JA 5 .   ? 100.775 -18.463 18.055 1.00 37.21  ? 1069 HOH C O   1 
HETATM 11477 O  O   . HOH JA 5 .   ? 115.986 -4.526  35.247 1.00 35.61  ? 1224 HOH C O   1 
HETATM 11478 O  O   . HOH JA 5 .   ? 109.052 -9.345  6.021  1.00 37.52  ? 1254 HOH C O   1 
HETATM 11479 O  O   . HOH JA 5 .   ? 118.681 -1.626  4.606  1.00 44.45  ? 1262 HOH C O   1 
HETATM 11480 O  O   . HOH JA 5 .   ? 106.017 -19.861 16.973 1.00 37.95  ? 1266 HOH C O   1 
HETATM 11481 O  O   . HOH JA 5 .   ? 118.089 5.401   4.980  1.00 46.88  ? 1271 HOH C O   1 
HETATM 11482 O  O   . HOH JA 5 .   ? 113.782 -14.252 29.696 1.00 50.73  ? 1275 HOH C O   1 
HETATM 11483 O  O   . HOH JA 5 .   ? 109.368 -4.920  -1.967 1.00 60.02  ? 1296 HOH C O   1 
HETATM 11484 O  O   . HOH JA 5 .   ? 126.574 -1.897  22.658 1.00 39.84  ? 1306 HOH C O   1 
HETATM 11485 O  O   . HOH JA 5 .   ? 118.326 6.635   8.451  1.00 59.52  ? 1319 HOH C O   1 
HETATM 11486 O  O   . HOH JA 5 .   ? 117.540 -19.505 16.704 1.00 45.06  ? 1329 HOH C O   1 
HETATM 11487 O  O   . HOH JA 5 .   ? 131.830 -11.112 26.976 1.00 48.35  ? 1332 HOH C O   1 
HETATM 11488 O  O   . HOH JA 5 .   ? 124.913 -11.754 14.361 1.00 47.52  ? 1346 HOH C O   1 
HETATM 11489 O  O   . HOH JA 5 .   ? 118.242 -13.959 5.559  1.00 45.78  ? 1347 HOH C O   1 
HETATM 11490 O  O   . HOH JA 5 .   ? 114.502 -6.150  6.848  1.00 53.97  ? 1368 HOH C O   1 
HETATM 11491 O  O   . HOH JA 5 .   ? 111.452 1.750   4.718  1.00 36.84  ? 1373 HOH C O   1 
HETATM 11492 O  O   . HOH JA 5 .   ? 121.597 -8.261  36.149 1.00 39.78  ? 1374 HOH C O   1 
HETATM 11493 O  O   . HOH JA 5 .   ? 110.278 -6.610  32.022 1.00 42.29  ? 1401 HOH C O   1 
HETATM 11494 O  O   . HOH JA 5 .   ? 112.214 -5.475  2.349  1.00 45.36  ? 1416 HOH C O   1 
HETATM 11495 O  O   . HOH JA 5 .   ? 120.537 -12.675 4.527  1.00 46.17  ? 1450 HOH C O   1 
HETATM 11496 O  O   . HOH JA 5 .   ? 120.580 -0.991  35.537 1.00 51.41  ? 1464 HOH C O   1 
HETATM 11497 O  O   . HOH JA 5 .   ? 112.931 -6.053  -0.105 1.00 65.94  ? 1471 HOH C O   1 
HETATM 11498 O  O   . HOH JA 5 .   ? 118.337 -19.304 13.851 1.00 45.92  ? 1480 HOH C O   1 
HETATM 11499 O  O   . HOH JA 5 .   ? 103.686 -13.564 27.180 1.00 46.89  ? 1484 HOH C O   1 
HETATM 11500 O  O   . HOH JA 5 .   ? 111.970 5.232   5.035  1.00 49.36  ? 1510 HOH C O   1 
HETATM 11501 O  O   . HOH JA 5 .   ? 130.286 -8.024  12.279 1.00 60.33  ? 1541 HOH C O   1 
HETATM 11502 O  O   . HOH JA 5 .   ? 115.221 -18.120 0.224  1.00 57.43  ? 1556 HOH C O   1 
HETATM 11503 O  O   . HOH JA 5 .   ? 112.919 -16.653 8.596  1.00 44.53  ? 1581 HOH C O   1 
HETATM 11504 O  O   . HOH JA 5 .   ? 127.536 -0.077  25.840 1.00 49.87  ? 1586 HOH C O   1 
HETATM 11505 O  O   . HOH KA 5 .   ? 90.696  5.100   21.984 1.00 29.84  ? 403  HOH D O   1 
HETATM 11506 O  O   . HOH KA 5 .   ? 102.352 -3.421  23.810 1.00 58.15  ? 412  HOH D O   1 
HETATM 11507 O  O   . HOH KA 5 .   ? 102.146 -9.284  21.240 1.00 22.33  ? 422  HOH D O   1 
HETATM 11508 O  O   . HOH KA 5 .   ? 101.653 -0.970  22.648 1.00 47.10  ? 435  HOH D O   1 
HETATM 11509 O  O   . HOH KA 5 .   ? 84.774  16.732  23.577 1.00 35.81  ? 437  HOH D O   1 
HETATM 11510 O  O   . HOH KA 5 .   ? 94.877  -18.594 21.332 1.00 46.83  ? 447  HOH D O   1 
HETATM 11511 O  O   . HOH KA 5 .   ? 105.882 -4.749  25.933 1.00 45.42  ? 448  HOH D O   1 
HETATM 11512 O  O   . HOH KA 5 .   ? 76.393  2.323   8.266  1.00 56.42  ? 450  HOH D O   1 
HETATM 11513 O  O   . HOH KA 5 .   ? 102.754 -3.333  8.694  1.00 57.83  ? 451  HOH D O   1 
HETATM 11514 O  O   . HOH KA 5 .   ? 82.545  -16.540 27.275 1.00 39.54  ? 461  HOH D O   1 
HETATM 11515 O  O   . HOH KA 5 .   ? 82.838  14.781  23.359 1.00 24.39  ? 467  HOH D O   1 
HETATM 11516 O  O   . HOH KA 5 .   ? 91.032  7.537   17.551 1.00 24.40  ? 471  HOH D O   1 
HETATM 11517 O  O   . HOH KA 5 .   ? 82.960  -6.331  17.187 1.00 23.66  ? 475  HOH D O   1 
HETATM 11518 O  O   . HOH KA 5 .   ? 77.801  2.258   13.854 1.00 26.83  ? 483  HOH D O   1 
HETATM 11519 O  O   . HOH KA 5 .   ? 88.113  -13.119 34.294 1.00 26.30  ? 487  HOH D O   1 
HETATM 11520 O  O   . HOH KA 5 .   ? 87.062  -4.343  32.519 1.00 27.07  ? 494  HOH D O   1 
HETATM 11521 O  O   . HOH KA 5 .   ? 82.543  -10.117 13.018 1.00 27.89  ? 498  HOH D O   1 
HETATM 11522 O  O   . HOH KA 5 .   ? 77.870  7.163   23.780 1.00 23.15  ? 508  HOH D O   1 
HETATM 11523 O  O   . HOH KA 5 .   ? 79.124  -2.129  13.248 1.00 24.69  ? 519  HOH D O   1 
HETATM 11524 O  O   . HOH KA 5 .   ? 77.713  -3.612  28.153 1.00 26.80  ? 525  HOH D O   1 
HETATM 11525 O  O   . HOH KA 5 .   ? 86.884  -15.485 13.878 1.00 38.43  ? 549  HOH D O   1 
HETATM 11526 O  O   . HOH KA 5 .   ? 82.528  -14.008 25.810 1.00 24.48  ? 552  HOH D O   1 
HETATM 11527 O  O   . HOH KA 5 .   ? 90.803  -8.022  4.330  1.00 36.82  ? 556  HOH D O   1 
HETATM 11528 O  O   . HOH KA 5 .   ? 91.748  -3.131  34.418 1.00 32.60  ? 558  HOH D O   1 
HETATM 11529 O  O   . HOH KA 5 .   ? 104.027 -18.235 15.691 1.00 33.96  ? 559  HOH D O   1 
HETATM 11530 O  O   . HOH KA 5 .   ? 92.166  6.831   20.111 1.00 28.38  ? 565  HOH D O   1 
HETATM 11531 O  O   . HOH KA 5 .   ? 76.266  4.801   24.234 1.00 34.65  ? 572  HOH D O   1 
HETATM 11532 O  O   . HOH KA 5 .   ? 77.424  10.387  16.638 1.00 22.88  ? 573  HOH D O   1 
HETATM 11533 O  O   . HOH KA 5 .   ? 88.881  3.650   6.804  1.00 28.34  ? 580  HOH D O   1 
HETATM 11534 O  O   . HOH KA 5 .   ? 89.312  5.721   24.177 1.00 28.22  ? 582  HOH D O   1 
HETATM 11535 O  O   . HOH KA 5 .   ? 77.203  7.913   12.901 1.00 34.74  ? 583  HOH D O   1 
HETATM 11536 O  O   . HOH KA 5 .   ? 106.841 -1.178  21.262 1.00 29.04  ? 591  HOH D O   1 
HETATM 11537 O  O   . HOH KA 5 .   ? 83.933  -6.936  11.254 1.00 33.20  ? 612  HOH D O   1 
HETATM 11538 O  O   . HOH KA 5 .   ? 79.156  -4.177  14.871 1.00 32.52  ? 614  HOH D O   1 
HETATM 11539 O  O   . HOH KA 5 .   ? 103.662 -6.388  22.866 1.00 28.59  ? 628  HOH D O   1 
HETATM 11540 O  O   . HOH KA 5 .   ? 75.991  2.291   19.680 1.00 31.44  ? 630  HOH D O   1 
HETATM 11541 O  O   . HOH KA 5 .   ? 88.864  -4.891  34.489 1.00 27.58  ? 643  HOH D O   1 
HETATM 11542 O  O   . HOH KA 5 .   ? 77.063  0.490   23.714 1.00 34.68  ? 645  HOH D O   1 
HETATM 11543 O  O   . HOH KA 5 .   ? 94.285  4.713   29.005 1.00 33.60  ? 648  HOH D O   1 
HETATM 11544 O  O   . HOH KA 5 .   ? 96.597  6.100   11.426 1.00 32.68  ? 651  HOH D O   1 
HETATM 11545 O  O   . HOH KA 5 .   ? 89.114  -7.631  2.222  1.00 49.02  ? 682  HOH D O   1 
HETATM 11546 O  O   . HOH KA 5 .   ? 79.783  2.830   28.469 1.00 35.36  ? 688  HOH D O   1 
HETATM 11547 O  O   . HOH KA 5 .   ? 97.918  -16.749 16.032 1.00 40.65  ? 690  HOH D O   1 
HETATM 11548 O  O   . HOH KA 5 .   ? 88.494  10.558  13.850 1.00 36.19  ? 691  HOH D O   1 
HETATM 11549 O  O   . HOH KA 5 .   ? 70.656  3.076   13.898 1.00 28.80  ? 692  HOH D O   1 
HETATM 11550 O  O   . HOH KA 5 .   ? 96.716  -17.096 13.722 1.00 45.28  ? 701  HOH D O   1 
HETATM 11551 O  O   . HOH KA 5 .   ? 101.250 -4.477  26.765 1.00 35.48  ? 704  HOH D O   1 
HETATM 11552 O  O   . HOH KA 5 .   ? 84.121  -6.062  7.507  1.00 42.63  ? 716  HOH D O   1 
HETATM 11553 O  O   . HOH KA 5 .   ? 77.723  0.309   21.380 1.00 34.16  ? 721  HOH D O   1 
HETATM 11554 O  O   . HOH KA 5 .   ? 72.648  8.594   17.354 1.00 26.02  ? 727  HOH D O   1 
HETATM 11555 O  O   . HOH KA 5 .   ? 78.631  4.772   7.200  1.00 40.97  ? 735  HOH D O   1 
HETATM 11556 O  O   . HOH KA 5 .   ? 96.003  8.946   21.159 1.00 30.73  ? 739  HOH D O   1 
HETATM 11557 O  O   . HOH KA 5 .   ? 101.262 5.136   10.670 1.00 43.47  ? 745  HOH D O   1 
HETATM 11558 O  O   . HOH KA 5 .   ? 72.822  6.429   19.618 1.00 29.79  ? 753  HOH D O   1 
HETATM 11559 O  O   . HOH KA 5 .   ? 97.599  -19.530 22.048 1.00 46.18  ? 755  HOH D O   1 
HETATM 11560 O  O   . HOH KA 5 .   ? 95.735  -3.599  2.810  1.00 35.60  ? 784  HOH D O   1 
HETATM 11561 O  O   . HOH KA 5 .   ? 83.236  -1.020  6.265  1.00 60.24  ? 791  HOH D O   1 
HETATM 11562 O  O   . HOH KA 5 .   ? 98.114  5.821   9.280  1.00 60.50  ? 813  HOH D O   1 
HETATM 11563 O  O   . HOH KA 5 .   ? 103.397 7.168   19.993 1.00 33.37  ? 820  HOH D O   1 
HETATM 11564 O  O   . HOH KA 5 .   ? 77.717  2.359   5.639  1.00 45.53  ? 821  HOH D O   1 
HETATM 11565 O  O   . HOH KA 5 .   ? 73.755  1.782   26.246 1.00 49.31  ? 829  HOH D O   1 
HETATM 11566 O  O   . HOH KA 5 .   ? 80.607  4.067   26.101 1.00 28.73  ? 851  HOH D O   1 
HETATM 11567 O  O   . HOH KA 5 .   ? 78.291  2.595   24.303 1.00 36.22  ? 856  HOH D O   1 
HETATM 11568 O  O   . HOH KA 5 .   ? 74.760  8.885   13.454 1.00 29.78  ? 869  HOH D O   1 
HETATM 11569 O  O   . HOH KA 5 .   ? 90.954  -16.094 29.167 1.00 41.96  ? 873  HOH D O   1 
HETATM 11570 O  O   . HOH KA 5 .   ? 75.602  4.407   26.683 1.00 47.41  ? 875  HOH D O   1 
HETATM 11571 O  O   . HOH KA 5 .   ? 84.373  -10.015 6.751  1.00 39.40  ? 890  HOH D O   1 
HETATM 11572 O  O   . HOH KA 5 .   ? 91.082  -14.562 3.749  1.00 32.87  ? 891  HOH D O   1 
HETATM 11573 O  O   . HOH KA 5 .   ? 93.033  9.084   21.432 1.00 40.76  ? 927  HOH D O   1 
HETATM 11574 O  O   . HOH KA 5 .   ? 97.272  8.291   23.722 1.00 39.98  ? 964  HOH D O   1 
HETATM 11575 O  O   . HOH KA 5 .   ? 95.687  7.430   25.823 1.00 48.26  ? 965  HOH D O   1 
HETATM 11576 O  O   . HOH KA 5 .   ? 92.708  7.264   29.875 1.00 48.79  ? 966  HOH D O   1 
HETATM 11577 O  O   . HOH KA 5 .   ? 86.611  7.740   25.299 1.00 41.58  ? 975  HOH D O   1 
HETATM 11578 O  O   . HOH KA 5 .   ? 81.498  -11.269 15.545 1.00 44.09  ? 984  HOH D O   1 
HETATM 11579 O  O   . HOH KA 5 .   ? 74.894  3.687   21.895 1.00 38.40  ? 990  HOH D O   1 
HETATM 11580 O  O   . HOH KA 5 .   ? 74.262  1.654   23.997 1.00 54.74  ? 992  HOH D O   1 
HETATM 11581 O  O   . HOH KA 5 .   ? 76.375  -0.301  10.437 1.00 44.28  ? 1022 HOH D O   1 
HETATM 11582 O  O   . HOH KA 5 .   ? 80.083  5.750   10.967 1.00 36.29  ? 1023 HOH D O   1 
HETATM 11583 O  O   . HOH KA 5 .   ? 75.119  10.946  15.159 1.00 25.70  ? 1024 HOH D O   1 
HETATM 11584 O  O   . HOH KA 5 .   ? 104.263 -8.932  23.322 1.00 41.16  ? 1061 HOH D O   1 
HETATM 11585 O  O   . HOH KA 5 .   ? 102.254 -7.634  25.286 1.00 38.90  ? 1063 HOH D O   1 
HETATM 11586 O  O   . HOH KA 5 .   ? 81.108  -10.613 36.682 1.00 47.40  ? 1067 HOH D O   1 
HETATM 11587 O  O   . HOH KA 5 .   ? 98.202  -18.188 19.934 1.00 41.36  ? 1070 HOH D O   1 
HETATM 11588 O  O   . HOH KA 5 .   ? 93.575  -17.222 23.184 1.00 31.62  ? 1071 HOH D O   1 
HETATM 11589 O  O   . HOH KA 5 .   ? 94.152  -16.231 26.810 1.00 44.43  ? 1072 HOH D O   1 
HETATM 11590 O  O   . HOH KA 5 .   ? 92.937  -22.425 17.639 1.00 81.85  ? 1073 HOH D O   1 
HETATM 11591 O  O   . HOH KA 5 .   ? 90.293  -17.693 31.066 1.00 53.82  ? 1074 HOH D O   1 
HETATM 11592 O  O   . HOH KA 5 .   ? 94.002  -0.899  34.459 1.00 54.43  ? 1085 HOH D O   1 
HETATM 11593 O  O   . HOH KA 5 .   ? 81.354  -3.784  31.497 1.00 38.18  ? 1086 HOH D O   1 
HETATM 11594 O  O   . HOH KA 5 .   ? 80.830  -2.303  29.355 1.00 43.10  ? 1087 HOH D O   1 
HETATM 11595 O  O   . HOH KA 5 .   ? 81.335  -6.467  11.263 1.00 38.59  ? 1099 HOH D O   1 
HETATM 11596 O  O   . HOH KA 5 .   ? 79.784  -6.395  13.750 1.00 37.67  ? 1100 HOH D O   1 
HETATM 11597 O  O   . HOH KA 5 .   ? 85.428  1.194   5.484  1.00 37.43  ? 1133 HOH D O   1 
HETATM 11598 O  O   . HOH KA 5 .   ? 95.146  -6.562  1.631  1.00 43.30  ? 1134 HOH D O   1 
HETATM 11599 O  O   . HOH KA 5 .   ? 95.446  3.257   0.021  1.00 66.32  ? 1135 HOH D O   1 
HETATM 11600 O  O   . HOH KA 5 .   ? 94.278  -4.400  33.010 1.00 33.75  ? 1136 HOH D O   1 
HETATM 11601 O  O   . HOH KA 5 .   ? 96.178  -1.210  32.120 1.00 36.75  ? 1137 HOH D O   1 
HETATM 11602 O  O   . HOH KA 5 .   ? 97.189  -7.502  32.654 1.00 47.75  ? 1138 HOH D O   1 
HETATM 11603 O  O   . HOH KA 5 .   ? 79.218  6.463   26.017 1.00 33.46  ? 1151 HOH D O   1 
HETATM 11604 O  O   . HOH KA 5 .   ? 75.755  -4.726  26.963 1.00 39.79  ? 1168 HOH D O   1 
HETATM 11605 O  O   . HOH KA 5 .   ? 83.617  -17.945 31.399 1.00 44.67  ? 1169 HOH D O   1 
HETATM 11606 O  O   . HOH KA 5 .   ? 80.467  -17.933 30.071 1.00 47.53  ? 1171 HOH D O   1 
HETATM 11607 O  O   . HOH KA 5 .   ? 77.483  -14.855 31.211 1.00 38.16  ? 1172 HOH D O   1 
HETATM 11608 O  O   . HOH KA 5 .   ? 77.692  -17.101 30.777 1.00 58.47  ? 1173 HOH D O   1 
HETATM 11609 O  O   . HOH KA 5 .   ? 91.217  10.250  16.985 1.00 40.46  ? 1197 HOH D O   1 
HETATM 11610 O  O   . HOH KA 5 .   ? 86.678  14.527  22.210 1.00 43.02  ? 1210 HOH D O   1 
HETATM 11611 O  O   . HOH KA 5 .   ? 92.180  6.601   24.601 1.00 43.64  ? 1230 HOH D O   1 
HETATM 11612 O  O   . HOH KA 5 .   ? 99.871  -0.528  7.316  1.00 36.94  ? 1231 HOH D O   1 
HETATM 11613 O  O   . HOH KA 5 .   ? 88.931  -16.291 2.777  1.00 48.96  ? 1241 HOH D O   1 
HETATM 11614 O  O   . HOH KA 5 .   ? 109.229 5.970   20.850 1.00 49.69  ? 1243 HOH D O   1 
HETATM 11615 O  O   . HOH KA 5 .   ? 105.524 7.755   22.121 1.00 54.73  ? 1244 HOH D O   1 
HETATM 11616 O  O   . HOH KA 5 .   ? 94.500  0.000   0.000  0.50 51.82  ? 1252 HOH D O   1 
HETATM 11617 O  O   . HOH KA 5 .   ? 85.883  -1.726  32.699 1.00 30.57  ? 1256 HOH D O   1 
HETATM 11618 O  O   . HOH KA 5 .   ? 102.004 -15.742 8.749  1.00 34.25  ? 1261 HOH D O   1 
HETATM 11619 O  O   . HOH KA 5 .   ? 90.610  -15.827 6.784  1.00 45.28  ? 1281 HOH D O   1 
HETATM 11620 O  O   . HOH KA 5 .   ? 88.013  -18.390 22.966 1.00 41.51  ? 1283 HOH D O   1 
HETATM 11621 O  O   . HOH KA 5 .   ? 102.642 -5.691  2.756  1.00 53.86  ? 1297 HOH D O   1 
HETATM 11622 O  O   . HOH KA 5 .   ? 84.614  0.299   16.394 1.00 19.90  ? 1348 HOH D O   1 
HETATM 11623 O  O   . HOH KA 5 .   ? 91.033  4.671   8.010  1.00 23.90  ? 1349 HOH D O   1 
HETATM 11624 O  O   . HOH KA 5 .   ? 93.653  -11.829 35.392 1.00 35.77  ? 1367 HOH D O   1 
HETATM 11625 O  O   . HOH KA 5 .   ? 80.290  0.650   28.944 1.00 42.32  ? 1370 HOH D O   1 
HETATM 11626 O  O   . HOH KA 5 .   ? 72.483  4.004   20.339 1.00 39.58  ? 1388 HOH D O   1 
HETATM 11627 O  O   . HOH KA 5 .   ? 101.528 -2.670  30.937 1.00 70.55  ? 1411 HOH D O   1 
HETATM 11628 O  O   . HOH KA 5 .   ? 99.631  -0.172  30.113 1.00 57.96  ? 1412 HOH D O   1 
HETATM 11629 O  O   . HOH KA 5 .   ? 87.742  1.838   5.467  1.00 44.76  ? 1423 HOH D O   1 
HETATM 11630 O  O   . HOH KA 5 .   ? 88.243  -16.575 5.425  1.00 48.39  ? 1428 HOH D O   1 
HETATM 11631 O  O   . HOH KA 5 .   ? 98.711  9.980   14.795 1.00 43.99  ? 1440 HOH D O   1 
HETATM 11632 O  O   . HOH KA 5 .   ? 77.398  -10.921 28.960 1.00 54.43  ? 1454 HOH D O   1 
HETATM 11633 O  O   . HOH KA 5 .   ? 96.987  0.627   30.412 1.00 45.45  ? 1473 HOH D O   1 
HETATM 11634 O  O   . HOH KA 5 .   ? 92.932  -14.987 28.772 1.00 52.74  ? 1486 HOH D O   1 
HETATM 11635 O  O   . HOH KA 5 .   ? 97.093  -13.646 2.909  1.00 47.35  ? 1488 HOH D O   1 
HETATM 11636 O  O   . HOH KA 5 .   ? 92.821  8.294   13.983 1.00 68.08  ? 1507 HOH D O   1 
HETATM 11637 O  O   . HOH KA 5 .   ? 86.264  -9.951  1.953  1.00 69.58  ? 1548 HOH D O   1 
HETATM 11638 O  O   . HOH LA 5 .   ? 46.276  -25.408 21.226 1.00 38.74  ? 413  HOH E O   1 
HETATM 11639 O  O   . HOH LA 5 .   ? 52.924  -28.818 21.589 1.00 19.48  ? 423  HOH E O   1 
HETATM 11640 O  O   . HOH LA 5 .   ? 22.742  -33.306 17.855 1.00 32.70  ? 438  HOH E O   1 
HETATM 11641 O  O   . HOH LA 5 .   ? 32.715  -38.849 1.398  1.00 80.62  ? 459  HOH E O   1 
HETATM 11642 O  O   . HOH LA 5 .   ? 34.040  -30.484 14.216 1.00 24.48  ? 465  HOH E O   1 
HETATM 11643 O  O   . HOH LA 5 .   ? 20.341  -33.353 15.996 1.00 25.73  ? 480  HOH E O   1 
HETATM 11644 O  O   . HOH LA 5 .   ? 50.340  -41.720 -2.305 1.00 35.94  ? 485  HOH E O   1 
HETATM 11645 O  O   . HOH LA 5 .   ? 51.059  -26.219 22.511 1.00 24.66  ? 490  HOH E O   1 
HETATM 11646 O  O   . HOH LA 5 .   ? 48.109  -20.789 20.394 1.00 21.49  ? 491  HOH E O   1 
HETATM 11647 O  O   . HOH LA 5 .   ? 31.159  -31.241 9.987  1.00 33.52  ? 496  HOH E O   1 
HETATM 11648 O  O   . HOH LA 5 .   ? 34.507  -25.353 17.968 1.00 27.92  ? 504  HOH E O   1 
HETATM 11649 O  O   . HOH LA 5 .   ? 39.325  -38.722 31.542 1.00 26.02  ? 505  HOH E O   1 
HETATM 11650 O  O   . HOH LA 5 .   ? 49.448  -39.264 4.560  1.00 28.39  ? 518  HOH E O   1 
HETATM 11651 O  O   . HOH LA 5 .   ? 47.002  -26.927 6.199  1.00 36.68  ? 522  HOH E O   1 
HETATM 11652 O  O   . HOH LA 5 .   ? 43.002  -32.343 31.928 1.00 28.98  ? 524  HOH E O   1 
HETATM 11653 O  O   . HOH LA 5 .   ? 46.996  -31.139 32.073 1.00 28.28  ? 536  HOH E O   1 
HETATM 11654 O  O   . HOH LA 5 .   ? 43.825  -24.839 21.810 1.00 27.34  ? 538  HOH E O   1 
HETATM 11655 O  O   . HOH LA 5 .   ? 35.485  -28.378 26.109 1.00 34.40  ? 544  HOH E O   1 
HETATM 11656 O  O   . HOH LA 5 .   ? 24.653  -41.016 12.459 1.00 26.94  ? 545  HOH E O   1 
HETATM 11657 O  O   . HOH LA 5 .   ? 58.413  -36.337 17.546 1.00 29.31  ? 547  HOH E O   1 
HETATM 11658 O  O   . HOH LA 5 .   ? 30.261  -40.971 22.989 1.00 27.09  ? 553  HOH E O   1 
HETATM 11659 O  O   . HOH LA 5 .   ? 37.148  -46.039 11.635 1.00 25.26  ? 555  HOH E O   1 
HETATM 11660 O  O   . HOH LA 5 .   ? 60.908  -32.708 10.897 1.00 35.84  ? 557  HOH E O   1 
HETATM 11661 O  O   . HOH LA 5 .   ? 42.023  -44.353 16.471 1.00 30.07  ? 561  HOH E O   1 
HETATM 11662 O  O   . HOH LA 5 .   ? 55.254  -41.798 4.689  1.00 30.52  ? 569  HOH E O   1 
HETATM 11663 O  O   . HOH LA 5 .   ? 57.707  -36.588 4.553  1.00 32.40  ? 571  HOH E O   1 
HETATM 11664 O  O   . HOH LA 5 .   ? 35.560  -49.476 19.711 1.00 36.60  ? 575  HOH E O   1 
HETATM 11665 O  O   . HOH LA 5 .   ? 46.529  -47.939 25.856 1.00 29.31  ? 581  HOH E O   1 
HETATM 11666 O  O   . HOH LA 5 .   ? 55.681  -34.475 4.823  1.00 32.59  ? 589  HOH E O   1 
HETATM 11667 O  O   . HOH LA 5 .   ? 44.044  -43.860 10.796 1.00 29.90  ? 595  HOH E O   1 
HETATM 11668 O  O   . HOH LA 5 .   ? 48.042  -25.574 23.131 1.00 33.46  ? 596  HOH E O   1 
HETATM 11669 O  O   . HOH LA 5 .   ? 40.419  -33.967 33.042 1.00 32.81  ? 598  HOH E O   1 
HETATM 11670 O  O   . HOH LA 5 .   ? 50.531  -42.577 34.867 1.00 29.05  ? 600  HOH E O   1 
HETATM 11671 O  O   . HOH LA 5 .   ? 41.997  -23.166 8.625  1.00 40.00  ? 606  HOH E O   1 
HETATM 11672 O  O   . HOH LA 5 .   ? 44.147  -43.378 6.759  1.00 39.78  ? 613  HOH E O   1 
HETATM 11673 O  O   . HOH LA 5 .   ? 37.198  -46.321 17.786 1.00 32.28  ? 619  HOH E O   1 
HETATM 11674 O  O   . HOH LA 5 .   ? 52.319  -34.108 1.826  1.00 31.11  ? 622  HOH E O   1 
HETATM 11675 O  O   . HOH LA 5 .   ? 39.620  -19.811 17.242 1.00 35.37  ? 644  HOH E O   1 
HETATM 11676 O  O   . HOH LA 5 .   ? 36.984  -50.406 22.544 1.00 31.89  ? 650  HOH E O   1 
HETATM 11677 O  O   . HOH LA 5 .   ? 47.855  -26.731 25.730 1.00 41.15  ? 660  HOH E O   1 
HETATM 11678 O  O   . HOH LA 5 .   ? 47.840  -41.248 35.044 1.00 34.17  ? 674  HOH E O   1 
HETATM 11679 O  O   . HOH LA 5 .   ? 34.498  -29.757 17.033 1.00 31.73  ? 681  HOH E O   1 
HETATM 11680 O  O   . HOH LA 5 .   ? 39.007  -26.946 8.580  1.00 31.89  ? 695  HOH E O   1 
HETATM 11681 O  O   . HOH LA 5 .   ? 55.847  -42.775 7.963  1.00 37.09  ? 698  HOH E O   1 
HETATM 11682 O  O   . HOH LA 5 .   ? 45.001  -25.715 27.380 1.00 45.38  ? 700  HOH E O   1 
HETATM 11683 O  O   . HOH LA 5 .   ? 35.252  -24.493 20.351 1.00 33.40  ? 714  HOH E O   1 
HETATM 11684 O  O   . HOH LA 5 .   ? 35.087  -28.726 10.947 1.00 39.40  ? 718  HOH E O   1 
HETATM 11685 O  O   . HOH LA 5 .   ? 43.469  -52.254 31.311 1.00 47.05  ? 723  HOH E O   1 
HETATM 11686 O  O   . HOH LA 5 .   ? 49.821  -43.124 1.807  1.00 45.18  ? 726  HOH E O   1 
HETATM 11687 O  O   . HOH LA 5 .   ? 40.181  -25.473 6.242  1.00 52.89  ? 733  HOH E O   1 
HETATM 11688 O  O   . HOH LA 5 .   ? 38.164  -34.944 4.220  1.00 27.34  ? 737  HOH E O   1 
HETATM 11689 O  O   . HOH LA 5 .   ? 23.956  -46.200 13.419 1.00 51.39  ? 740  HOH E O   1 
HETATM 11690 O  O   . HOH LA 5 .   ? 33.496  -32.474 21.125 1.00 34.57  ? 742  HOH E O   1 
HETATM 11691 O  O   . HOH LA 5 .   ? 46.582  -29.435 35.460 1.00 43.34  ? 744  HOH E O   1 
HETATM 11692 O  O   . HOH LA 5 .   ? 34.278  -26.200 22.669 1.00 39.14  ? 764  HOH E O   1 
HETATM 11693 O  O   . HOH LA 5 .   ? 52.827  -46.098 21.935 1.00 42.77  ? 769  HOH E O   1 
HETATM 11694 O  O   . HOH LA 5 .   ? 30.733  -45.911 16.607 1.00 33.40  ? 773  HOH E O   1 
HETATM 11695 O  O   . HOH LA 5 .   ? 38.758  -46.516 13.341 1.00 44.46  ? 775  HOH E O   1 
HETATM 11696 O  O   . HOH LA 5 .   ? 41.947  -25.791 27.975 1.00 37.74  ? 776  HOH E O   1 
HETATM 11697 O  O   . HOH LA 5 .   ? 31.980  -43.107 4.325  1.00 50.08  ? 780  HOH E O   1 
HETATM 11698 O  O   . HOH LA 5 .   ? 59.209  -37.363 0.500  1.00 47.30  ? 792  HOH E O   1 
HETATM 11699 O  O   . HOH LA 5 .   ? 30.312  -33.757 21.749 1.00 39.56  ? 796  HOH E O   1 
HETATM 11700 O  O   . HOH LA 5 .   ? 25.467  -46.791 15.776 1.00 35.55  ? 799  HOH E O   1 
HETATM 11701 O  O   . HOH LA 5 .   ? 48.838  -31.795 2.365  1.00 37.46  ? 806  HOH E O   1 
HETATM 11702 O  O   . HOH LA 5 .   ? 34.612  -46.668 26.511 1.00 35.31  ? 807  HOH E O   1 
HETATM 11703 O  O   . HOH LA 5 .   ? 47.934  -45.348 6.899  1.00 50.31  ? 814  HOH E O   1 
HETATM 11704 O  O   . HOH LA 5 .   ? 33.703  -45.701 3.204  1.00 71.80  ? 819  HOH E O   1 
HETATM 11705 O  O   . HOH LA 5 .   ? 45.991  -47.068 12.666 1.00 49.51  ? 836  HOH E O   1 
HETATM 11706 O  O   . HOH LA 5 .   ? 41.786  -18.425 16.107 1.00 35.47  ? 840  HOH E O   1 
HETATM 11707 O  O   . HOH LA 5 .   ? 40.766  -37.419 33.391 1.00 31.65  ? 842  HOH E O   1 
HETATM 11708 O  O   . HOH LA 5 .   ? 39.705  -37.021 3.423  1.00 48.07  ? 859  HOH E O   1 
HETATM 11709 O  O   . HOH LA 5 .   ? 35.004  -47.259 18.270 1.00 39.08  ? 867  HOH E O   1 
HETATM 11710 O  O   . HOH LA 5 .   ? 39.387  -41.787 4.376  1.00 40.29  ? 871  HOH E O   1 
HETATM 11711 O  O   . HOH LA 5 .   ? 49.500  -25.190 6.246  1.00 49.10  ? 874  HOH E O   1 
HETATM 11712 O  O   . HOH LA 5 .   ? 55.825  -44.227 3.582  1.00 44.45  ? 892  HOH E O   1 
HETATM 11713 O  O   . HOH LA 5 .   ? 45.203  -27.863 37.952 1.00 48.38  ? 900  HOH E O   1 
HETATM 11714 O  O   . HOH LA 5 .   ? 36.041  -23.004 11.184 1.00 47.36  ? 928  HOH E O   1 
HETATM 11715 O  O   . HOH LA 5 .   ? 34.238  -29.747 21.797 1.00 39.96  ? 929  HOH E O   1 
HETATM 11716 O  O   . HOH LA 5 .   ? 32.042  -28.408 20.948 1.00 61.83  ? 930  HOH E O   1 
HETATM 11717 O  O   . HOH LA 5 .   ? 44.970  -22.925 6.465  1.00 75.52  ? 954  HOH E O   1 
HETATM 11718 O  O   . HOH LA 5 .   ? 34.396  -53.254 11.626 1.00 39.21  ? 1004 HOH E O   1 
HETATM 11719 O  O   . HOH LA 5 .   ? 40.210  -51.689 11.793 1.00 44.05  ? 1007 HOH E O   1 
HETATM 11720 O  O   . HOH LA 5 .   ? 37.166  -52.741 11.973 1.00 34.13  ? 1008 HOH E O   1 
HETATM 11721 O  O   . HOH LA 5 .   ? 35.661  -49.931 24.819 1.00 35.74  ? 1012 HOH E O   1 
HETATM 11722 O  O   . HOH LA 5 .   ? 45.388  -45.653 22.694 1.00 37.50  ? 1017 HOH E O   1 
HETATM 11723 O  O   . HOH LA 5 .   ? 41.268  -47.287 12.341 1.00 35.82  ? 1019 HOH E O   1 
HETATM 11724 O  O   . HOH LA 5 .   ? 42.329  -50.065 12.178 1.00 51.25  ? 1020 HOH E O   1 
HETATM 11725 O  O   . HOH LA 5 .   ? 30.908  -42.382 25.677 1.00 44.73  ? 1051 HOH E O   1 
HETATM 11726 O  O   . HOH LA 5 .   ? 36.630  -38.628 30.731 1.00 33.14  ? 1052 HOH E O   1 
HETATM 11727 O  O   . HOH LA 5 .   ? 35.309  -43.643 27.650 1.00 48.96  ? 1053 HOH E O   1 
HETATM 11728 O  O   . HOH LA 5 .   ? 42.041  -44.587 34.617 1.00 43.58  ? 1055 HOH E O   1 
HETATM 11729 O  O   . HOH LA 5 .   ? 50.722  -27.772 25.340 1.00 35.62  ? 1057 HOH E O   1 
HETATM 11730 O  O   . HOH LA 5 .   ? 49.697  -22.890 26.142 1.00 39.39  ? 1076 HOH E O   1 
HETATM 11731 O  O   . HOH LA 5 .   ? 41.653  -23.577 29.908 1.00 57.65  ? 1077 HOH E O   1 
HETATM 11732 O  O   . HOH LA 5 .   ? 24.730  -31.666 21.378 1.00 52.44  ? 1127 HOH E O   1 
HETATM 11733 O  O   . HOH LA 5 .   ? 23.009  -33.918 20.543 1.00 46.99  ? 1128 HOH E O   1 
HETATM 11734 O  O   . HOH LA 5 .   ? 34.960  -31.644 19.120 1.00 30.92  ? 1129 HOH E O   1 
HETATM 11735 O  O   . HOH LA 5 .   ? 32.638  -27.815 17.832 1.00 45.42  ? 1130 HOH E O   1 
HETATM 11736 O  O   . HOH LA 5 .   ? 43.003  -15.384 18.928 1.00 45.98  ? 1131 HOH E O   1 
HETATM 11737 O  O   . HOH LA 5 .   ? 55.301  -39.941 24.678 1.00 38.77  ? 1160 HOH E O   1 
HETATM 11738 O  O   . HOH LA 5 .   ? 59.129  -36.508 21.787 1.00 33.14  ? 1162 HOH E O   1 
HETATM 11739 O  O   . HOH LA 5 .   ? 57.483  -39.637 23.441 1.00 41.94  ? 1163 HOH E O   1 
HETATM 11740 O  O   . HOH LA 5 .   ? 53.442  -34.067 29.140 1.00 43.48  ? 1164 HOH E O   1 
HETATM 11741 O  O   . HOH LA 5 .   ? 52.193  -32.209 29.646 1.00 63.80  ? 1165 HOH E O   1 
HETATM 11742 O  O   . HOH LA 5 .   ? 53.550  -36.022 30.339 1.00 48.97  ? 1167 HOH E O   1 
HETATM 11743 O  O   . HOH LA 5 .   ? 46.379  -17.184 27.442 1.00 49.67  ? 1201 HOH E O   1 
HETATM 11744 O  O   . HOH LA 5 .   ? 58.872  -37.508 15.241 1.00 52.59  ? 1209 HOH E O   1 
HETATM 11745 O  O   . HOH LA 5 .   ? 55.662  -44.860 7.015  1.00 47.73  ? 1217 HOH E O   1 
HETATM 11746 O  O   . HOH LA 5 .   ? 33.121  -45.575 18.941 1.00 35.01  ? 1218 HOH E O   1 
HETATM 11747 O  O   . HOH LA 5 .   ? 32.107  -45.858 21.394 1.00 38.89  ? 1219 HOH E O   1 
HETATM 11748 O  O   . HOH LA 5 .   ? 35.761  -26.252 6.120  1.00 60.76  ? 1242 HOH E O   1 
HETATM 11749 O  O   . HOH LA 5 .   ? 38.689  -39.079 3.305  1.00 41.03  ? 1248 HOH E O   1 
HETATM 11750 O  O   . HOH LA 5 .   ? 41.595  -36.886 0.937  1.00 60.74  ? 1249 HOH E O   1 
HETATM 11751 O  O   . HOH LA 5 .   ? 41.169  -29.515 30.549 1.00 34.64  ? 1274 HOH E O   1 
HETATM 11752 O  O   . HOH LA 5 .   ? 40.618  -49.949 28.632 1.00 38.95  ? 1286 HOH E O   1 
HETATM 11753 O  O   . HOH LA 5 .   ? 47.855  -42.136 -2.231 1.00 39.26  ? 1288 HOH E O   1 
HETATM 11754 O  O   . HOH LA 5 .   ? 52.483  -42.834 32.891 1.00 36.05  ? 1292 HOH E O   1 
HETATM 11755 O  O   . HOH LA 5 .   ? 52.350  -45.455 15.064 1.00 44.33  ? 1302 HOH E O   1 
HETATM 11756 O  O   . HOH LA 5 .   ? 39.275  -45.076 35.346 1.00 40.56  ? 1304 HOH E O   1 
HETATM 11757 O  O   . HOH LA 5 .   ? 59.386  -37.236 24.382 1.00 53.60  ? 1330 HOH E O   1 
HETATM 11758 O  O   . HOH LA 5 .   ? 37.121  -39.668 14.307 1.00 26.06  ? 1350 HOH E O   1 
HETATM 11759 O  O   . HOH LA 5 .   ? 38.214  -32.443 5.413  1.00 27.78  ? 1351 HOH E O   1 
HETATM 11760 O  O   . HOH LA 5 .   ? 25.493  -46.206 11.270 1.00 47.01  ? 1372 HOH E O   1 
HETATM 11761 O  O   . HOH LA 5 .   ? 32.967  -42.856 26.586 1.00 59.86  ? 1380 HOH E O   1 
HETATM 11762 O  O   . HOH LA 5 .   ? 35.435  -50.094 10.008 1.00 49.90  ? 1386 HOH E O   1 
HETATM 11763 O  O   . HOH LA 5 .   ? 31.099  -40.684 7.969  1.00 32.21  ? 1389 HOH E O   1 
HETATM 11764 O  O   . HOH LA 5 .   ? 35.607  -26.538 24.749 1.00 52.11  ? 1396 HOH E O   1 
HETATM 11765 O  O   . HOH LA 5 .   ? 24.136  -36.031 21.103 1.00 55.75  ? 1399 HOH E O   1 
HETATM 11766 O  O   . HOH LA 5 .   ? 28.676  -50.559 10.784 1.00 49.51  ? 1430 HOH E O   1 
HETATM 11767 O  O   . HOH LA 5 .   ? 50.751  -48.589 21.837 1.00 40.05  ? 1452 HOH E O   1 
HETATM 11768 O  O   . HOH LA 5 .   ? 46.005  -20.370 27.865 1.00 63.30  ? 1518 HOH E O   1 
HETATM 11769 O  O   . HOH LA 5 .   ? 33.134  -49.949 21.460 1.00 44.91  ? 1562 HOH E O   1 
HETATM 11770 O  O   . HOH LA 5 .   ? 41.098  -29.292 37.644 1.00 48.61  ? 1582 HOH E O   1 
HETATM 11771 O  O   . HOH MA 5 .   ? 68.801  -18.485 21.903 1.00 28.26  ? 404  HOH F O   1 
HETATM 11772 O  O   . HOH MA 5 .   ? 59.671  -25.237 23.363 1.00 29.05  ? 414  HOH F O   1 
HETATM 11773 O  O   . HOH MA 5 .   ? 50.711  -21.237 21.244 1.00 20.10  ? 424  HOH F O   1 
HETATM 11774 O  O   . HOH MA 5 .   ? 73.740  -4.236  19.551 1.00 39.92  ? 446  HOH F O   1 
HETATM 11775 O  O   . HOH MA 5 .   ? 71.109  -22.219 24.329 1.00 69.84  ? 449  HOH F O   1 
HETATM 11776 O  O   . HOH MA 5 .   ? 55.162  -24.621 24.027 1.00 35.97  ? 463  HOH F O   1 
HETATM 11777 O  O   . HOH MA 5 .   ? 55.681  -29.236 21.249 1.00 19.90  ? 469  HOH F O   1 
HETATM 11778 O  O   . HOH MA 5 .   ? 67.422  -2.795  28.567 1.00 34.45  ? 484  HOH F O   1 
HETATM 11779 O  O   . HOH MA 5 .   ? 58.715  -17.343 33.093 1.00 31.94  ? 486  HOH F O   1 
HETATM 11780 O  O   . HOH MA 5 .   ? 62.246  -10.895 33.102 1.00 30.02  ? 492  HOH F O   1 
HETATM 11781 O  O   . HOH MA 5 .   ? 70.764  -19.955 17.491 1.00 28.68  ? 513  HOH F O   1 
HETATM 11782 O  O   . HOH MA 5 .   ? 45.988  -13.888 16.171 1.00 33.59  ? 516  HOH F O   1 
HETATM 11783 O  O   . HOH MA 5 .   ? 79.968  -9.596  16.670 1.00 22.80  ? 517  HOH F O   1 
HETATM 11784 O  O   . HOH MA 5 .   ? 77.036  -8.324  23.906 1.00 23.89  ? 528  HOH F O   1 
HETATM 11785 O  O   . HOH MA 5 .   ? 69.544  -24.897 21.065 1.00 29.65  ? 533  HOH F O   1 
HETATM 11786 O  O   . HOH MA 5 .   ? 53.511  -8.145  34.986 1.00 42.15  ? 540  HOH F O   1 
HETATM 11787 O  O   . HOH MA 5 .   ? 65.113  -11.173 32.919 1.00 30.94  ? 541  HOH F O   1 
HETATM 11788 O  O   . HOH MA 5 .   ? 60.571  -12.334 34.612 1.00 28.14  ? 542  HOH F O   1 
HETATM 11789 O  O   . HOH MA 5 .   ? 56.333  -1.950  25.914 1.00 29.50  ? 554  HOH F O   1 
HETATM 11790 O  O   . HOH MA 5 .   ? 78.781  -3.451  19.487 1.00 31.85  ? 594  HOH F O   1 
HETATM 11791 O  O   . HOH MA 5 .   ? 57.671  -24.900 22.281 1.00 31.45  ? 597  HOH F O   1 
HETATM 11792 O  O   . HOH MA 5 .   ? 54.815  -18.603 32.686 1.00 27.20  ? 599  HOH F O   1 
HETATM 11793 O  O   . HOH MA 5 .   ? 62.371  -5.753  17.722 1.00 30.36  ? 616  HOH F O   1 
HETATM 11794 O  O   . HOH MA 5 .   ? 57.925  2.626   31.970 1.00 43.38  ? 618  HOH F O   1 
HETATM 11795 O  O   . HOH MA 5 .   ? 58.748  -18.043 2.770  1.00 34.06  ? 623  HOH F O   1 
HETATM 11796 O  O   . HOH MA 5 .   ? 81.137  -16.443 23.603 1.00 28.66  ? 626  HOH F O   1 
HETATM 11797 O  O   . HOH MA 5 .   ? 69.751  -20.409 20.230 1.00 29.16  ? 629  HOH F O   1 
HETATM 11798 O  O   . HOH MA 5 .   ? 61.074  -15.705 34.526 1.00 28.50  ? 636  HOH F O   1 
HETATM 11799 O  O   . HOH MA 5 .   ? 66.670  -23.550 11.298 1.00 34.10  ? 649  HOH F O   1 
HETATM 11800 O  O   . HOH MA 5 .   ? 72.757  -5.879  13.882 1.00 34.10  ? 652  HOH F O   1 
HETATM 11801 O  O   . HOH MA 5 .   ? 51.523  -8.682  3.877  1.00 46.48  ? 657  HOH F O   1 
HETATM 11802 O  O   . HOH MA 5 .   ? 66.821  -21.504 28.905 1.00 33.07  ? 669  HOH F O   1 
HETATM 11803 O  O   . HOH MA 5 .   ? 62.608  -31.821 18.321 1.00 31.86  ? 670  HOH F O   1 
HETATM 11804 O  O   . HOH MA 5 .   ? 72.942  -9.032  26.405 1.00 27.31  ? 673  HOH F O   1 
HETATM 11805 O  O   . HOH MA 5 .   ? 75.846  -9.243  26.236 1.00 33.91  ? 680  HOH F O   1 
HETATM 11806 O  O   . HOH MA 5 .   ? 63.479  -27.327 10.683 1.00 45.23  ? 683  HOH F O   1 
HETATM 11807 O  O   . HOH MA 5 .   ? 47.854  -10.110 23.477 1.00 34.72  ? 687  HOH F O   1 
HETATM 11808 O  O   . HOH MA 5 .   ? 64.692  -30.376 19.812 1.00 34.10  ? 694  HOH F O   1 
HETATM 11809 O  O   . HOH MA 5 .   ? 44.827  -17.784 9.146  1.00 34.78  ? 712  HOH F O   1 
HETATM 11810 O  O   . HOH MA 5 .   ? 58.783  -5.531  36.042 1.00 39.50  ? 715  HOH F O   1 
HETATM 11811 O  O   . HOH MA 5 .   ? 68.500  -15.508 6.708  1.00 33.22  ? 724  HOH F O   1 
HETATM 11812 O  O   . HOH MA 5 .   ? 61.433  -6.225  11.671 1.00 35.58  ? 729  HOH F O   1 
HETATM 11813 O  O   . HOH MA 5 .   ? 61.923  -4.641  36.454 1.00 41.11  ? 738  HOH F O   1 
HETATM 11814 O  O   . HOH MA 5 .   ? 74.541  -18.774 13.828 1.00 49.60  ? 746  HOH F O   1 
HETATM 11815 O  O   . HOH MA 5 .   ? 71.689  -4.270  24.036 1.00 37.67  ? 751  HOH F O   1 
HETATM 11816 O  O   . HOH MA 5 .   ? 59.244  -3.327  13.253 1.00 36.82  ? 757  HOH F O   1 
HETATM 11817 O  O   . HOH MA 5 .   ? 58.216  -1.413  16.714 1.00 38.36  ? 758  HOH F O   1 
HETATM 11818 O  O   . HOH MA 5 .   ? 61.692  0.305   29.673 1.00 37.87  ? 761  HOH F O   1 
HETATM 11819 O  O   . HOH MA 5 .   ? 76.700  -2.417  19.909 1.00 46.46  ? 766  HOH F O   1 
HETATM 11820 O  O   . HOH MA 5 .   ? 80.702  -4.237  17.241 1.00 37.33  ? 768  HOH F O   1 
HETATM 11821 O  O   . HOH MA 5 .   ? 51.086  -3.980  21.354 1.00 38.75  ? 774  HOH F O   1 
HETATM 11822 O  O   . HOH MA 5 .   ? 57.168  -12.077 4.619  1.00 42.00  ? 785  HOH F O   1 
HETATM 11823 O  O   . HOH MA 5 .   ? 50.837  -7.092  34.334 1.00 31.01  ? 788  HOH F O   1 
HETATM 11824 O  O   . HOH MA 5 .   ? 60.615  -23.792 29.710 1.00 43.67  ? 794  HOH F O   1 
HETATM 11825 O  O   . HOH MA 5 .   ? 69.475  -20.285 24.175 1.00 51.57  ? 805  HOH F O   1 
HETATM 11826 O  O   . HOH MA 5 .   ? 81.651  -8.001  15.278 1.00 38.14  ? 809  HOH F O   1 
HETATM 11827 O  O   . HOH MA 5 .   ? 55.378  -23.049 26.457 1.00 37.51  ? 810  HOH F O   1 
HETATM 11828 O  O   . HOH MA 5 .   ? 57.439  -24.259 29.139 1.00 49.90  ? 811  HOH F O   1 
HETATM 11829 O  O   . HOH MA 5 .   ? 70.986  -4.463  21.422 1.00 38.95  ? 834  HOH F O   1 
HETATM 11830 O  O   . HOH MA 5 .   ? 75.431  -5.981  24.555 1.00 30.14  ? 835  HOH F O   1 
HETATM 11831 O  O   . HOH MA 5 .   ? 52.515  -4.765  14.252 1.00 37.85  ? 838  HOH F O   1 
HETATM 11832 O  O   . HOH MA 5 .   ? 56.439  -16.270 1.820  1.00 51.01  ? 839  HOH F O   1 
HETATM 11833 O  O   . HOH MA 5 .   ? 50.508  -7.939  6.875  1.00 50.41  ? 843  HOH F O   1 
HETATM 11834 O  O   . HOH MA 5 .   ? 70.057  -17.415 24.377 1.00 25.07  ? 844  HOH F O   1 
HETATM 11835 O  O   . HOH MA 5 .   ? 60.743  -20.267 32.121 1.00 44.56  ? 847  HOH F O   1 
HETATM 11836 O  O   . HOH MA 5 .   ? 86.998  -17.357 20.675 1.00 39.77  ? 849  HOH F O   1 
HETATM 11837 O  O   . HOH MA 5 .   ? 74.117  -2.483  23.904 1.00 55.01  ? 852  HOH F O   1 
HETATM 11838 O  O   . HOH MA 5 .   ? 64.190  0.187   29.040 1.00 45.18  ? 855  HOH F O   1 
HETATM 11839 O  O   . HOH MA 5 .   ? 44.543  -13.529 20.055 1.00 36.58  ? 879  HOH F O   1 
HETATM 11840 O  O   . HOH MA 5 .   ? 59.319  -23.160 7.138  1.00 35.74  ? 931  HOH F O   1 
HETATM 11841 O  O   . HOH MA 5 .   ? 65.202  -25.110 8.679  1.00 46.54  ? 932  HOH F O   1 
HETATM 11842 O  O   . HOH MA 5 .   ? 70.922  -22.374 21.218 1.00 37.98  ? 933  HOH F O   1 
HETATM 11843 O  O   . HOH MA 5 .   ? 73.400  -16.037 25.804 1.00 40.43  ? 934  HOH F O   1 
HETATM 11844 O  O   . HOH MA 5 .   ? 63.496  -25.678 29.290 1.00 48.86  ? 935  HOH F O   1 
HETATM 11845 O  O   . HOH MA 5 .   ? 68.480  -25.639 23.524 1.00 33.41  ? 963  HOH F O   1 
HETATM 11846 O  O   . HOH MA 5 .   ? 76.554  -11.960 14.526 1.00 33.03  ? 985  HOH F O   1 
HETATM 11847 O  O   . HOH MA 5 .   ? 74.659  -10.051 11.597 1.00 32.18  ? 986  HOH F O   1 
HETATM 11848 O  O   . HOH MA 5 .   ? 68.196  -4.366  13.645 1.00 23.61  ? 988  HOH F O   1 
HETATM 11849 O  O   . HOH MA 5 .   ? 66.264  -3.681  15.230 1.00 38.49  ? 989  HOH F O   1 
HETATM 11850 O  O   . HOH MA 5 .   ? 61.879  1.671   37.193 1.00 60.54  ? 994  HOH F O   1 
HETATM 11851 O  O   . HOH MA 5 .   ? 76.661  -0.151  13.846 1.00 36.87  ? 1021 HOH F O   1 
HETATM 11852 O  O   . HOH MA 5 .   ? 52.375  -19.496 32.947 1.00 42.64  ? 1028 HOH F O   1 
HETATM 11853 O  O   . HOH MA 5 .   ? 53.095  -27.020 26.515 1.00 43.25  ? 1056 HOH F O   1 
HETATM 11854 O  O   . HOH MA 5 .   ? 52.405  -23.780 22.729 1.00 27.54  ? 1058 HOH F O   1 
HETATM 11855 O  O   . HOH MA 5 .   ? 54.800  -20.420 35.979 1.00 45.34  ? 1079 HOH F O   1 
HETATM 11856 O  O   . HOH MA 5 .   ? 74.934  0.157   17.495 1.00 57.63  ? 1101 HOH F O   1 
HETATM 11857 O  O   . HOH MA 5 .   ? 77.919  -8.363  13.174 1.00 35.54  ? 1105 HOH F O   1 
HETATM 11858 O  O   . HOH MA 5 .   ? 75.296  -7.818  13.056 1.00 37.53  ? 1106 HOH F O   1 
HETATM 11859 O  O   . HOH MA 5 .   ? 45.904  -10.326 21.919 1.00 41.38  ? 1132 HOH F O   1 
HETATM 11860 O  O   . HOH MA 5 .   ? 74.384  -11.976 4.491  1.00 53.34  ? 1154 HOH F O   1 
HETATM 11861 O  O   . HOH MA 5 .   ? 46.358  -12.692 13.660 1.00 44.09  ? 1157 HOH F O   1 
HETATM 11862 O  O   . HOH MA 5 .   ? 60.842  -34.593 20.656 1.00 39.24  ? 1161 HOH F O   1 
HETATM 11863 O  O   . HOH MA 5 .   ? 80.254  -16.053 25.970 1.00 49.84  ? 1170 HOH F O   1 
HETATM 11864 O  O   . HOH MA 5 .   ? 72.018  -7.605  28.808 1.00 38.34  ? 1174 HOH F O   1 
HETATM 11865 O  O   . HOH MA 5 .   ? 74.879  -4.144  21.540 1.00 44.26  ? 1195 HOH F O   1 
HETATM 11866 O  O   . HOH MA 5 .   ? 73.085  -6.547  24.641 1.00 38.17  ? 1196 HOH F O   1 
HETATM 11867 O  O   . HOH MA 5 .   ? 69.093  -27.445 14.241 1.00 38.04  ? 1199 HOH F O   1 
HETATM 11868 O  O   . HOH MA 5 .   ? 52.134  -22.171 25.154 1.00 42.80  ? 1200 HOH F O   1 
HETATM 11869 O  O   . HOH MA 5 .   ? 49.226  -6.658  31.681 1.00 47.95  ? 1205 HOH F O   1 
HETATM 11870 O  O   . HOH MA 5 .   ? 58.060  -4.448  23.323 1.00 31.34  ? 1212 HOH F O   1 
HETATM 11871 O  O   . HOH MA 5 .   ? 67.769  -11.691 5.522  1.00 45.34  ? 1247 HOH F O   1 
HETATM 11872 O  O   . HOH MA 5 .   ? 58.597  -5.233  7.216  1.00 40.53  ? 1300 HOH F O   1 
HETATM 11873 O  O   . HOH MA 5 .   ? 62.526  -33.705 25.103 1.00 39.53  ? 1305 HOH F O   1 
HETATM 11874 O  O   . HOH MA 5 .   ? 53.536  -23.046 2.118  1.00 77.95  ? 1312 HOH F O   1 
HETATM 11875 O  O   . HOH MA 5 .   ? 68.957  -23.878 25.559 1.00 40.21  ? 1318 HOH F O   1 
HETATM 11876 O  O   . HOH MA 5 .   ? 62.051  -6.926  7.886  1.00 40.63  ? 1320 HOH F O   1 
HETATM 11877 O  O   . HOH MA 5 .   ? 67.196  -6.282  29.838 1.00 41.65  ? 1328 HOH F O   1 
HETATM 11878 O  O   . HOH MA 5 .   ? 50.669  -2.589  33.288 1.00 46.60  ? 1337 HOH F O   1 
HETATM 11879 O  O   . HOH MA 5 .   ? 67.477  -10.620 16.575 1.00 20.90  ? 1352 HOH F O   1 
HETATM 11880 O  O   . HOH MA 5 .   ? 68.289  -18.171 8.003  1.00 29.35  ? 1353 HOH F O   1 
HETATM 11881 O  O   . HOH MA 5 .   ? 51.256  -4.741  35.196 1.00 52.17  ? 1366 HOH F O   1 
HETATM 11882 O  O   . HOH MA 5 .   ? 74.454  -7.512  7.642  1.00 47.21  ? 1375 HOH F O   1 
HETATM 11883 O  O   . HOH MA 5 .   ? 67.254  -23.258 27.486 1.00 45.20  ? 1377 HOH F O   1 
HETATM 11884 O  O   . HOH MA 5 .   ? 43.792  -12.830 22.617 1.00 49.23  ? 1394 HOH F O   1 
HETATM 11885 O  O   . HOH MA 5 .   ? 77.072  -16.170 6.799  1.00 45.00  ? 1437 HOH F O   1 
HETATM 11886 O  O   . HOH MA 5 .   ? 78.671  -14.409 27.012 1.00 46.42  ? 1443 HOH F O   1 
HETATM 11887 O  O   . HOH MA 5 .   ? 43.599  -14.730 16.526 1.00 53.79  ? 1465 HOH F O   1 
HETATM 11888 O  O   . HOH MA 5 .   ? 54.605  -6.886  37.179 1.00 42.66  ? 1479 HOH F O   1 
HETATM 11889 O  O   . HOH MA 5 .   ? 72.511  -4.621  6.162  1.00 51.83  ? 1485 HOH F O   1 
HETATM 11890 O  O   . HOH MA 5 .   ? 36.540  -19.989 10.384 1.00 51.22  ? 1501 HOH F O   1 
HETATM 11891 O  O   . HOH MA 5 .   ? 50.031  -23.161 23.431 1.00 43.33  ? 1502 HOH F O   1 
HETATM 11892 O  O   . HOH MA 5 .   ? 71.659  -24.012 4.599  1.00 54.02  ? 1521 HOH F O   1 
HETATM 11893 O  O   . HOH MA 5 .   ? 73.170  -3.950  8.261  1.00 54.81  ? 1543 HOH F O   1 
HETATM 11894 O  O   . HOH MA 5 .   ? 56.781  -27.000 30.020 1.00 77.93  ? 1587 HOH F O   1 
HETATM 11895 O  O   . HOH MA 5 .   ? 64.163  -6.378  6.883  1.00 63.42  ? 1605 HOH F O   1 
HETATM 11896 O  O   . HOH MA 5 .   ? 60.118  -3.111  10.427 1.00 50.26  ? 1632 HOH F O   1 
HETATM 11897 O  O   . HOH NA 5 .   ? 140.960 -15.596 16.501 1.00 40.35  ? 405  HOH G O   1 
HETATM 11898 O  O   . HOH NA 5 .   ? 140.768 -3.104  19.175 1.00 39.35  ? 415  HOH G O   1 
HETATM 11899 O  O   . HOH NA 5 .   ? 147.590 1.144   21.023 1.00 31.71  ? 425  HOH G O   1 
HETATM 11900 O  O   . HOH NA 5 .   ? 144.188 0.821   21.373 1.00 38.89  ? 436  HOH G O   1 
HETATM 11901 O  O   . HOH NA 5 .   ? 138.632 1.083   18.031 1.00 28.54  ? 562  HOH G O   1 
HETATM 11902 O  O   . HOH NA 5 .   ? 142.898 -12.430 31.359 1.00 35.60  ? 567  HOH G O   1 
HETATM 11903 O  O   . HOH NA 5 .   ? 147.113 -16.011 30.644 1.00 37.07  ? 570  HOH G O   1 
HETATM 11904 O  O   . HOH NA 5 .   ? 137.601 -13.819 23.178 1.00 39.36  ? 605  HOH G O   1 
HETATM 11905 O  O   . HOH NA 5 .   ? 153.278 -10.669 35.306 1.00 40.94  ? 639  HOH G O   1 
HETATM 11906 O  O   . HOH NA 5 .   ? 160.723 -18.672 34.113 1.00 43.60  ? 722  HOH G O   1 
HETATM 11907 O  O   . HOH NA 5 .   ? 143.106 -9.668  30.303 1.00 36.89  ? 750  HOH G O   1 
HETATM 11908 O  O   . HOH NA 5 .   ? 151.173 -16.119 35.691 1.00 39.19  ? 812  HOH G O   1 
HETATM 11909 O  O   . HOH NA 5 .   ? 150.689 -26.363 20.871 1.00 41.30  ? 902  HOH G O   1 
HETATM 11910 O  O   . HOH NA 5 .   ? 152.226 -24.833 19.374 1.00 47.17  ? 905  HOH G O   1 
HETATM 11911 O  O   . HOH NA 5 .   ? 153.926 -25.817 17.449 1.00 36.22  ? 906  HOH G O   1 
HETATM 11912 O  O   . HOH NA 5 .   ? 155.364 -21.607 18.881 1.00 40.91  ? 907  HOH G O   1 
HETATM 11913 O  O   . HOH NA 5 .   ? 156.009 -18.795 16.943 1.00 36.15  ? 908  HOH G O   1 
HETATM 11914 O  O   . HOH NA 5 .   ? 156.586 -20.427 12.304 1.00 37.81  ? 910  HOH G O   1 
HETATM 11915 O  O   . HOH NA 5 .   ? 152.573 -26.591 14.754 1.00 37.10  ? 948  HOH G O   1 
HETATM 11916 O  O   . HOH NA 5 .   ? 138.985 -15.797 18.870 1.00 49.40  ? 962  HOH G O   1 
HETATM 11917 O  O   . HOH NA 5 .   ? 151.764 -18.607 35.861 1.00 38.60  ? 1078 HOH G O   1 
HETATM 11918 O  O   . HOH NA 5 .   ? 145.492 -18.586 29.691 1.00 44.03  ? 1080 HOH G O   1 
HETATM 11919 O  O   . HOH NA 5 .   ? 146.065 -13.873 32.114 1.00 41.55  ? 1081 HOH G O   1 
HETATM 11920 O  O   . HOH NA 5 .   ? 149.837 -21.881 27.106 1.00 52.43  ? 1082 HOH G O   1 
HETATM 11921 O  O   . HOH NA 5 .   ? 151.709 -23.898 26.420 1.00 57.80  ? 1083 HOH G O   1 
HETATM 11922 O  O   . HOH NA 5 .   ? 143.987 -5.556  30.862 1.00 30.50  ? 1089 HOH G O   1 
HETATM 11923 O  O   . HOH NA 5 .   ? 145.169 1.974   25.942 1.00 38.60  ? 1091 HOH G O   1 
HETATM 11924 O  O   . HOH NA 5 .   ? 144.802 -0.247  23.958 1.00 40.67  ? 1092 HOH G O   1 
HETATM 11925 O  O   . HOH NA 5 .   ? 132.299 -0.296  14.883 1.00 39.08  ? 1194 HOH G O   1 
HETATM 11926 O  O   . HOH NA 5 .   ? 154.574 -8.631  36.080 1.00 34.77  ? 1204 HOH G O   1 
HETATM 11927 O  O   . HOH NA 5 .   ? 139.619 1.167   24.042 1.00 49.50  ? 1215 HOH G O   1 
HETATM 11928 O  O   . HOH NA 5 .   ? 156.781 2.605   23.321 1.00 47.90  ? 1232 HOH G O   1 
HETATM 11929 O  O   . HOH NA 5 .   ? 157.221 1.791   18.928 1.00 36.51  ? 1234 HOH G O   1 
HETATM 11930 O  O   . HOH NA 5 .   ? 158.697 -13.419 21.181 1.00 35.15  ? 1235 HOH G O   1 
HETATM 11931 O  O   . HOH NA 5 .   ? 157.942 -14.486 23.692 1.00 37.63  ? 1236 HOH G O   1 
HETATM 11932 O  O   . HOH NA 5 .   ? 157.766 -20.247 29.985 1.00 41.43  ? 1246 HOH G O   1 
HETATM 11933 O  O   . HOH NA 5 .   ? 140.311 -4.659  6.086  1.00 42.98  ? 1269 HOH G O   1 
HETATM 11934 O  O   . HOH NA 5 .   ? 151.114 -2.975  -1.784 1.00 47.61  ? 1280 HOH G O   1 
HETATM 11935 O  O   . HOH NA 5 .   ? 140.005 -15.248 13.995 1.00 43.30  ? 1289 HOH G O   1 
HETATM 11936 O  O   . HOH NA 5 .   ? 150.775 -10.946 36.555 1.00 43.70  ? 1301 HOH G O   1 
HETATM 11937 O  O   . HOH NA 5 .   ? 135.216 -11.699 16.183 1.00 41.95  ? 1313 HOH G O   1 
HETATM 11938 O  O   . HOH NA 5 .   ? 138.132 -7.437  25.415 1.00 57.94  ? 1334 HOH G O   1 
HETATM 11939 O  O   . HOH NA 5 .   ? 145.753 -24.363 21.558 1.00 52.25  ? 1335 HOH G O   1 
HETATM 11940 O  O   . HOH NA 5 .   ? 150.277 -17.765 13.873 1.00 46.81  ? 1354 HOH G O   1 
HETATM 11941 O  O   . HOH NA 5 .   ? 146.473 -13.714 4.186  1.00 36.55  ? 1355 HOH G O   1 
HETATM 11942 O  O   . HOH NA 5 .   ? 151.970 -4.345  2.436  1.00 47.11  ? 1404 HOH G O   1 
HETATM 11943 O  O   . HOH NA 5 .   ? 136.412 -12.943 14.235 1.00 45.90  ? 1407 HOH G O   1 
HETATM 11944 O  O   . HOH NA 5 .   ? 141.071 -17.816 18.906 1.00 52.71  ? 1424 HOH G O   1 
HETATM 11945 O  O   . HOH NA 5 .   ? 156.786 -15.487 16.908 1.00 42.06  ? 1429 HOH G O   1 
HETATM 11946 O  O   . HOH NA 5 .   ? 148.919 -14.724 3.696  1.00 56.82  ? 1436 HOH G O   1 
HETATM 11947 O  O   . HOH NA 5 .   ? 146.038 -2.848  4.765  1.00 48.94  ? 1441 HOH G O   1 
HETATM 11948 O  O   . HOH NA 5 .   ? 143.326 -16.979 17.052 1.00 48.17  ? 1467 HOH G O   1 
HETATM 11949 O  O   . HOH NA 5 .   ? 163.121 -3.289  7.133  1.00 52.17  ? 1493 HOH G O   1 
HETATM 11950 O  O   . HOH NA 5 .   ? 142.056 -2.815  24.247 1.00 45.40  ? 1588 HOH G O   1 
HETATM 11951 O  O   . HOH NA 5 .   ? 158.004 -17.903 21.586 1.00 68.61  ? 1619 HOH G O   1 
HETATM 11952 O  O   . HOH OA 5 .   ? 147.120 20.112  21.759 1.00 42.82  ? 406  HOH H O   1 
HETATM 11953 O  O   . HOH OA 5 .   ? 147.418 8.813   22.973 1.00 45.24  ? 416  HOH H O   1 
HETATM 11954 O  O   . HOH OA 5 .   ? 140.326 3.204   19.290 1.00 25.94  ? 426  HOH H O   1 
HETATM 11955 O  O   . HOH OA 5 .   ? 145.600 21.951  23.909 1.00 39.96  ? 432  HOH H O   1 
HETATM 11956 O  O   . HOH OA 5 .   ? 148.223 34.033  16.388 1.00 41.92  ? 440  HOH H O   1 
HETATM 11957 O  O   . HOH OA 5 .   ? 135.508 29.779  21.659 1.00 36.19  ? 441  HOH H O   1 
HETATM 11958 O  O   . HOH OA 5 .   ? 155.104 10.534  21.124 1.00 48.24  ? 443  HOH H O   1 
HETATM 11959 O  O   . HOH OA 5 .   ? 128.818 27.146  9.483  1.00 44.60  ? 444  HOH H O   1 
HETATM 11960 O  O   . HOH OA 5 .   ? 136.031 26.755  10.966 1.00 23.46  ? 477  HOH H O   1 
HETATM 11961 O  O   . HOH OA 5 .   ? 141.379 32.564  22.643 1.00 26.33  ? 479  HOH H O   1 
HETATM 11962 O  O   . HOH OA 5 .   ? 145.269 34.573  16.130 1.00 27.00  ? 482  HOH H O   1 
HETATM 11963 O  O   . HOH OA 5 .   ? 134.668 18.300  30.255 1.00 26.43  ? 520  HOH H O   1 
HETATM 11964 O  O   . HOH OA 5 .   ? 149.365 3.282   21.288 1.00 35.53  ? 521  HOH H O   1 
HETATM 11965 O  O   . HOH OA 5 .   ? 133.453 21.248  14.440 1.00 24.98  ? 539  HOH H O   1 
HETATM 11966 O  O   . HOH OA 5 .   ? 138.194 12.128  31.156 1.00 30.00  ? 576  HOH H O   1 
HETATM 11967 O  O   . HOH OA 5 .   ? 130.849 19.879  9.771  1.00 28.10  ? 604  HOH H O   1 
HETATM 11968 O  O   . HOH OA 5 .   ? 152.037 16.144  11.745 1.00 35.66  ? 620  HOH H O   1 
HETATM 11969 O  O   . HOH OA 5 .   ? 134.296 16.403  32.216 1.00 33.35  ? 635  HOH H O   1 
HETATM 11970 O  O   . HOH OA 5 .   ? 135.874 29.090  19.353 1.00 34.77  ? 640  HOH H O   1 
HETATM 11971 O  O   . HOH OA 5 .   ? 155.377 8.042   19.576 1.00 34.82  ? 658  HOH H O   1 
HETATM 11972 O  O   . HOH OA 5 .   ? 136.058 27.035  26.821 1.00 38.63  ? 659  HOH H O   1 
HETATM 11973 O  O   . HOH OA 5 .   ? 128.620 6.442   19.063 1.00 39.15  ? 663  HOH H O   1 
HETATM 11974 O  O   . HOH OA 5 .   ? 137.847 30.075  22.670 1.00 33.88  ? 664  HOH H O   1 
HETATM 11975 O  O   . HOH OA 5 .   ? 137.796 28.497  26.470 1.00 46.65  ? 667  HOH H O   1 
HETATM 11976 O  O   . HOH OA 5 .   ? 149.508 21.265  17.605 1.00 29.89  ? 677  HOH H O   1 
HETATM 11977 O  O   . HOH OA 5 .   ? 123.303 16.145  22.733 1.00 34.29  ? 678  HOH H O   1 
HETATM 11978 O  O   . HOH OA 5 .   ? 137.155 31.523  17.875 1.00 30.26  ? 686  HOH H O   1 
HETATM 11979 O  O   . HOH OA 5 .   ? 131.059 1.500   16.063 1.00 46.16  ? 711  HOH H O   1 
HETATM 11980 O  O   . HOH OA 5 .   ? 126.094 7.740   18.759 1.00 49.42  ? 747  HOH H O   1 
HETATM 11981 O  O   . HOH OA 5 .   ? 136.136 20.592  5.798  1.00 46.03  ? 760  HOH H O   1 
HETATM 11982 O  O   . HOH OA 5 .   ? 146.784 16.996  28.585 1.00 38.95  ? 777  HOH H O   1 
HETATM 11983 O  O   . HOH OA 5 .   ? 128.450 4.321   17.490 1.00 35.24  ? 825  HOH H O   1 
HETATM 11984 O  O   . HOH OA 5 .   ? 142.357 30.507  5.760  1.00 42.24  ? 828  HOH H O   1 
HETATM 11985 O  O   . HOH OA 5 .   ? 136.864 16.848  33.719 1.00 45.34  ? 872  HOH H O   1 
HETATM 11986 O  O   . HOH OA 5 .   ? 131.886 10.180  2.799  1.00 46.21  ? 893  HOH H O   1 
HETATM 11987 O  O   . HOH OA 5 .   ? 151.504 20.085  14.240 1.00 52.02  ? 936  HOH H O   1 
HETATM 11988 O  O   . HOH OA 5 .   ? 152.523 17.560  21.545 1.00 34.80  ? 937  HOH H O   1 
HETATM 11989 O  O   . HOH OA 5 .   ? 141.904 12.184  30.945 1.00 40.38  ? 995  HOH H O   1 
HETATM 11990 O  O   . HOH OA 5 .   ? 138.210 14.591  32.634 1.00 36.49  ? 996  HOH H O   1 
HETATM 11991 O  O   . HOH OA 5 .   ? 137.857 19.038  32.875 1.00 40.71  ? 997  HOH H O   1 
HETATM 11992 O  O   . HOH OA 5 .   ? 136.254 20.516  30.560 1.00 32.87  ? 998  HOH H O   1 
HETATM 11993 O  O   . HOH OA 5 .   ? 128.182 20.806  32.566 1.00 33.70  ? 999  HOH H O   1 
HETATM 11994 O  O   . HOH OA 5 .   ? 130.003 24.152  31.350 1.00 56.69  ? 1000 HOH H O   1 
HETATM 11995 O  O   . HOH OA 5 .   ? 133.626 22.631  8.403  1.00 45.68  ? 1009 HOH H O   1 
HETATM 11996 O  O   . HOH OA 5 .   ? 131.264 26.697  25.532 1.00 33.20  ? 1010 HOH H O   1 
HETATM 11997 O  O   . HOH OA 5 .   ? 141.065 30.899  24.829 1.00 32.39  ? 1011 HOH H O   1 
HETATM 11998 O  O   . HOH OA 5 .   ? 134.136 29.888  24.165 1.00 41.49  ? 1013 HOH H O   1 
HETATM 11999 O  O   . HOH OA 5 .   ? 144.907 36.528  14.558 1.00 41.47  ? 1016 HOH H O   1 
HETATM 12000 O  O   . HOH OA 5 .   ? 146.288 31.525  26.517 1.00 52.78  ? 1018 HOH H O   1 
HETATM 12001 O  O   . HOH OA 5 .   ? 131.046 5.354   25.251 1.00 55.55  ? 1034 HOH H O   1 
HETATM 12002 O  O   . HOH OA 5 .   ? 125.535 10.192  29.370 1.00 47.62  ? 1036 HOH H O   1 
HETATM 12003 O  O   . HOH OA 5 .   ? 121.720 14.373  26.571 1.00 42.17  ? 1037 HOH H O   1 
HETATM 12004 O  O   . HOH OA 5 .   ? 121.206 21.134  26.745 1.00 41.86  ? 1041 HOH H O   1 
HETATM 12005 O  O   . HOH OA 5 .   ? 125.285 23.496  25.000 1.00 45.62  ? 1042 HOH H O   1 
HETATM 12006 O  O   . HOH OA 5 .   ? 133.326 4.074   24.709 1.00 44.90  ? 1088 HOH H O   1 
HETATM 12007 O  O   . HOH OA 5 .   ? 142.965 3.338   21.342 1.00 32.22  ? 1090 HOH H O   1 
HETATM 12008 O  O   . HOH OA 5 .   ? 137.592 7.912   30.191 1.00 35.88  ? 1140 HOH H O   1 
HETATM 12009 O  O   . HOH OA 5 .   ? 127.803 13.191  10.410 1.00 43.26  ? 1176 HOH H O   1 
HETATM 12010 O  O   . HOH OA 5 .   ? 127.064 14.819  8.413  1.00 64.58  ? 1177 HOH H O   1 
HETATM 12011 O  O   . HOH OA 5 .   ? 126.906 17.034  9.756  1.00 55.32  ? 1178 HOH H O   1 
HETATM 12012 O  O   . HOH OA 5 .   ? 127.700 19.894  13.273 1.00 35.07  ? 1179 HOH H O   1 
HETATM 12013 O  O   . HOH OA 5 .   ? 140.353 30.420  4.633  1.00 43.73  ? 1183 HOH H O   1 
HETATM 12014 O  O   . HOH OA 5 .   ? 146.934 21.509  6.038  1.00 31.04  ? 1184 HOH H O   1 
HETATM 12015 O  O   . HOH OA 5 .   ? 122.316 18.403  21.620 1.00 30.10  ? 1187 HOH H O   1 
HETATM 12016 O  O   . HOH OA 5 .   ? 123.553 9.892   22.718 1.00 55.60  ? 1191 HOH H O   1 
HETATM 12017 O  O   . HOH OA 5 .   ? 125.017 10.380  18.733 1.00 40.35  ? 1192 HOH H O   1 
HETATM 12018 O  O   . HOH OA 5 .   ? 125.929 11.754  16.223 1.00 41.14  ? 1193 HOH H O   1 
HETATM 12019 O  O   . HOH OA 5 .   ? 136.144 36.232  11.221 1.00 39.69  ? 1213 HOH H O   1 
HETATM 12020 O  O   . HOH OA 5 .   ? 133.994 38.366  11.028 1.00 33.80  ? 1214 HOH H O   1 
HETATM 12021 O  O   . HOH OA 5 .   ? 141.064 3.918   23.411 1.00 40.10  ? 1216 HOH H O   1 
HETATM 12022 O  O   . HOH OA 5 .   ? 156.535 4.774   22.061 1.00 41.30  ? 1233 HOH H O   1 
HETATM 12023 O  O   . HOH OA 5 .   ? 139.674 28.475  24.484 1.00 32.68  ? 1237 HOH H O   1 
HETATM 12024 O  O   . HOH OA 5 .   ? 148.327 19.898  24.342 1.00 61.37  ? 1239 HOH H O   1 
HETATM 12025 O  O   . HOH OA 5 .   ? 127.397 12.592  30.265 1.00 30.83  ? 1240 HOH H O   1 
HETATM 12026 O  O   . HOH OA 5 .   ? 134.561 20.115  8.528  1.00 36.24  ? 1251 HOH H O   1 
HETATM 12027 O  O   . HOH OA 5 .   ? 129.838 20.655  34.589 1.00 36.24  ? 1264 HOH H O   1 
HETATM 12028 O  O   . HOH OA 5 .   ? 146.107 25.120  25.126 1.00 44.92  ? 1270 HOH H O   1 
HETATM 12029 O  O   . HOH OA 5 .   ? 151.172 24.941  13.847 1.00 38.44  ? 1273 HOH H O   1 
HETATM 12030 O  O   . HOH OA 5 .   ? 133.643 10.607  0.364  1.00 32.47  ? 1277 HOH H O   1 
HETATM 12031 O  O   . HOH OA 5 .   ? 149.118 20.145  19.974 1.00 41.02  ? 1278 HOH H O   1 
HETATM 12032 O  O   . HOH OA 5 .   ? 136.489 -0.138  5.833  1.00 41.91  ? 1282 HOH H O   1 
HETATM 12033 O  O   . HOH OA 5 .   ? 137.703 16.015  -0.111 1.00 43.29  ? 1284 HOH H O   1 
HETATM 12034 O  O   . HOH OA 5 .   ? 132.550 2.962   12.337 1.00 35.55  ? 1298 HOH H O   1 
HETATM 12035 O  O   . HOH OA 5 .   ? 153.804 11.312  11.297 1.00 38.41  ? 1315 HOH H O   1 
HETATM 12036 O  O   . HOH OA 5 .   ? 144.562 7.459   27.684 1.00 43.21  ? 1324 HOH H O   1 
HETATM 12037 O  O   . HOH OA 5 .   ? 140.314 23.146  14.839 1.00 24.28  ? 1356 HOH H O   1 
HETATM 12038 O  O   . HOH OA 5 .   ? 148.850 20.096  7.743  1.00 35.20  ? 1357 HOH H O   1 
HETATM 12039 O  O   . HOH OA 5 .   ? 129.481 6.158   22.606 1.00 47.48  ? 1403 HOH H O   1 
HETATM 12040 O  O   . HOH OA 5 .   ? 134.546 -3.162  12.233 1.00 48.18  ? 1414 HOH H O   1 
HETATM 12041 O  O   . HOH OA 5 .   ? 146.308 7.428   21.514 1.00 38.15  ? 1415 HOH H O   1 
HETATM 12042 O  O   . HOH OA 5 .   ? 132.054 4.047   10.329 1.00 42.55  ? 1422 HOH H O   1 
HETATM 12043 O  O   . HOH OA 5 .   ? 149.081 31.246  26.379 1.00 55.84  ? 1447 HOH H O   1 
HETATM 12044 O  O   . HOH OA 5 .   ? 150.773 31.810  23.591 1.00 43.24  ? 1459 HOH H O   1 
HETATM 12045 O  O   . HOH OA 5 .   ? 143.323 29.680  9.722  1.00 42.52  ? 1463 HOH H O   1 
HETATM 12046 O  O   . HOH OA 5 .   ? 139.018 13.930  2.327  1.00 42.85  ? 1469 HOH H O   1 
HETATM 12047 O  O   . HOH OA 5 .   ? 143.225 6.408   25.472 1.00 45.87  ? 1474 HOH H O   1 
HETATM 12048 O  O   . HOH OA 5 .   ? 139.912 6.911   1.349  1.00 42.33  ? 1487 HOH H O   1 
HETATM 12049 O  O   . HOH OA 5 .   ? 152.307 16.278  23.964 1.00 49.99  ? 1490 HOH H O   1 
HETATM 12050 O  O   . HOH OA 5 .   ? 127.548 18.106  33.169 1.00 70.67  ? 1497 HOH H O   1 
HETATM 12051 O  O   . HOH OA 5 .   ? 131.967 8.320   31.493 1.00 59.59  ? 1522 HOH H O   1 
HETATM 12052 O  O   . HOH OA 5 .   ? 131.367 23.338  33.331 1.00 56.40  ? 1540 HOH H O   1 
HETATM 12053 O  O   . HOH OA 5 .   ? 156.211 6.692   26.622 1.00 53.17  ? 1553 HOH H O   1 
HETATM 12054 O  O   . HOH OA 5 .   ? 130.962 18.165  34.501 1.00 51.79  ? 1561 HOH H O   1 
HETATM 12055 O  O   . HOH OA 5 .   ? 126.845 8.442   24.864 1.00 67.19  ? 1592 HOH H O   1 
HETATM 12056 O  O   . HOH OA 5 .   ? 146.588 24.491  -0.576 1.00 70.86  ? 1609 HOH H O   1 
HETATM 12057 O  O   . HOH OA 5 .   ? 153.652 24.451  11.271 1.00 65.67  ? 1616 HOH H O   1 
HETATM 12058 O  O   . HOH OA 5 .   ? 145.577 9.956   29.071 1.00 47.12  ? 1618 HOH H O   1 
HETATM 12059 O  O   . HOH PA 5 .   ? 98.393  43.828  14.864 1.00 52.31  ? 417  HOH I O   1 
HETATM 12060 O  O   . HOH PA 5 .   ? 98.603  35.961  15.645 1.00 23.31  ? 427  HOH I O   1 
HETATM 12061 O  O   . HOH PA 5 .   ? 72.894  47.417  10.342 1.00 38.19  ? 439  HOH I O   1 
HETATM 12062 O  O   . HOH PA 5 .   ? 81.210  36.306  4.775  1.00 51.62  ? 455  HOH I O   1 
HETATM 12063 O  O   . HOH PA 5 .   ? 73.591  37.904  16.279 1.00 27.13  ? 478  HOH I O   1 
HETATM 12064 O  O   . HOH PA 5 .   ? 74.354  45.652  12.531 1.00 31.87  ? 481  HOH I O   1 
HETATM 12065 O  O   . HOH PA 5 .   ? 80.535  33.795  13.435 1.00 23.74  ? 499  HOH I O   1 
HETATM 12066 O  O   . HOH PA 5 .   ? 83.694  43.412  25.099 1.00 32.81  ? 502  HOH I O   1 
HETATM 12067 O  O   . HOH PA 5 .   ? 74.854  44.057  20.723 1.00 29.60  ? 535  HOH I O   1 
HETATM 12068 O  O   . HOH PA 5 .   ? 99.991  39.121  16.548 1.00 30.89  ? 590  HOH I O   1 
HETATM 12069 O  O   . HOH PA 5 .   ? 84.061  35.145  28.638 1.00 31.01  ? 592  HOH I O   1 
HETATM 12070 O  O   . HOH PA 5 .   ? 100.909 25.899  12.342 1.00 36.37  ? 647  HOH I O   1 
HETATM 12071 O  O   . HOH PA 5 .   ? 79.737  36.545  7.122  1.00 34.37  ? 656  HOH I O   1 
HETATM 12072 O  O   . HOH PA 5 .   ? 103.269 43.987  14.215 1.00 29.89  ? 699  HOH I O   1 
HETATM 12073 O  O   . HOH PA 5 .   ? 76.319  41.495  5.583  1.00 38.46  ? 708  HOH I O   1 
HETATM 12074 O  O   . HOH PA 5 .   ? 78.410  45.310  21.532 1.00 44.41  ? 752  HOH I O   1 
HETATM 12075 O  O   . HOH PA 5 .   ? 94.746  27.473  12.043 1.00 37.77  ? 759  HOH I O   1 
HETATM 12076 O  O   . HOH PA 5 .   ? 83.436  27.853  16.339 1.00 50.89  ? 767  HOH I O   1 
HETATM 12077 O  O   . HOH PA 5 .   ? 82.363  46.078  24.225 1.00 34.72  ? 771  HOH I O   1 
HETATM 12078 O  O   . HOH PA 5 .   ? 76.209  40.124  7.840  1.00 40.47  ? 781  HOH I O   1 
HETATM 12079 O  O   . HOH PA 5 .   ? 79.989  37.509  9.437  1.00 35.55  ? 786  HOH I O   1 
HETATM 12080 O  O   . HOH PA 5 .   ? 93.589  40.511  25.949 1.00 35.80  ? 824  HOH I O   1 
HETATM 12081 O  O   . HOH PA 5 .   ? 78.068  41.144  29.200 1.00 44.70  ? 854  HOH I O   1 
HETATM 12082 O  O   . HOH PA 5 .   ? 79.596  34.647  16.185 1.00 33.91  ? 876  HOH I O   1 
HETATM 12083 O  O   . HOH PA 5 .   ? 78.683  32.984  18.435 1.00 37.83  ? 921  HOH I O   1 
HETATM 12084 O  O   . HOH PA 5 .   ? 76.424  39.771  30.521 1.00 52.33  ? 922  HOH I O   1 
HETATM 12085 O  O   . HOH PA 5 .   ? 92.914  53.886  11.169 1.00 44.47  ? 938  HOH I O   1 
HETATM 12086 O  O   . HOH PA 5 .   ? 100.052 52.060  10.926 1.00 42.60  ? 960  HOH I O   1 
HETATM 12087 O  O   . HOH PA 5 .   ? 81.007  39.407  29.060 1.00 54.98  ? 968  HOH I O   1 
HETATM 12088 O  O   . HOH PA 5 .   ? 85.202  43.091  27.480 1.00 40.27  ? 969  HOH I O   1 
HETATM 12089 O  O   . HOH PA 5 .   ? 85.027  32.695  28.962 1.00 46.47  ? 1005 HOH I O   1 
HETATM 12090 O  O   . HOH PA 5 .   ? 86.665  30.968  23.910 1.00 47.04  ? 1097 HOH I O   1 
HETATM 12091 O  O   . HOH PA 5 .   ? 79.525  29.791  26.887 1.00 59.53  ? 1098 HOH I O   1 
HETATM 12092 O  O   . HOH PA 5 .   ? 94.758  26.988  15.792 1.00 40.83  ? 1108 HOH I O   1 
HETATM 12093 O  O   . HOH PA 5 .   ? 105.669 50.905  12.711 1.00 46.05  ? 1110 HOH I O   1 
HETATM 12094 O  O   . HOH PA 5 .   ? 101.898 41.795  20.273 1.00 43.81  ? 1115 HOH I O   1 
HETATM 12095 O  O   . HOH PA 5 .   ? 92.428  46.626  23.972 1.00 43.35  ? 1141 HOH I O   1 
HETATM 12096 O  O   . HOH PA 5 .   ? 73.988  43.451  27.940 1.00 47.61  ? 1152 HOH I O   1 
HETATM 12097 O  O   . HOH PA 5 .   ? 97.760  42.007  19.422 1.00 43.64  ? 1155 HOH I O   1 
HETATM 12098 O  O   . HOH PA 5 .   ? 99.062  41.787  17.033 1.00 47.30  ? 1156 HOH I O   1 
HETATM 12099 O  O   . HOH PA 5 .   ? 89.923  28.635  18.647 1.00 41.26  ? 1226 HOH I O   1 
HETATM 12100 O  O   . HOH PA 5 .   ? 87.355  27.230  18.739 1.00 46.28  ? 1227 HOH I O   1 
HETATM 12101 O  O   . HOH PA 5 .   ? 78.313  28.047  21.033 1.00 35.01  ? 1258 HOH I O   1 
HETATM 12102 O  O   . HOH PA 5 .   ? 99.371  26.896  4.897  1.00 46.69  ? 1287 HOH I O   1 
HETATM 12103 O  O   . HOH PA 5 .   ? 98.151  38.825  19.149 1.00 42.68  ? 1299 HOH I O   1 
HETATM 12104 O  O   . HOH PA 5 .   ? 95.752  47.247  21.677 1.00 42.75  ? 1303 HOH I O   1 
HETATM 12105 O  O   . HOH PA 5 .   ? 88.155  51.636  7.569  1.00 38.82  ? 1308 HOH I O   1 
HETATM 12106 O  O   . HOH PA 5 .   ? 81.662  44.387  7.996  1.00 30.97  ? 1358 HOH I O   1 
HETATM 12107 O  O   . HOH PA 5 .   ? 88.380  46.067  -1.229 1.00 40.50  ? 1359 HOH I O   1 
HETATM 12108 O  O   . HOH PA 5 .   ? 97.613  46.051  15.401 1.00 43.47  ? 1391 HOH I O   1 
HETATM 12109 O  O   . HOH PA 5 .   ? 93.788  48.715  2.334  1.00 49.84  ? 1405 HOH I O   1 
HETATM 12110 O  O   . HOH PA 5 .   ? 88.546  27.870  -1.118 1.00 52.18  ? 1418 HOH I O   1 
HETATM 12111 O  O   . HOH PA 5 .   ? 83.382  28.431  9.063  1.00 75.42  ? 1421 HOH I O   1 
HETATM 12112 O  O   . HOH PA 5 .   ? 77.144  50.356  16.109 1.00 43.87  ? 1442 HOH I O   1 
HETATM 12113 O  O   . HOH PA 5 .   ? 91.673  31.987  24.209 1.00 55.83  ? 1457 HOH I O   1 
HETATM 12114 O  O   . HOH PA 5 .   ? 81.158  35.825  0.909  1.00 54.88  ? 1472 HOH I O   1 
HETATM 12115 O  O   . HOH PA 5 .   ? 94.419  33.462  23.510 1.00 61.40  ? 1492 HOH I O   1 
HETATM 12116 O  O   . HOH PA 5 .   ? 93.775  27.103  9.637  1.00 52.03  ? 1526 HOH I O   1 
HETATM 12117 O  O   . HOH PA 5 .   ? 100.338 36.925  17.127 1.00 46.68  ? 1568 HOH I O   1 
HETATM 12118 O  O   . HOH PA 5 .   ? 97.240  42.106  -0.515 1.00 68.04  ? 1634 HOH I O   1 
HETATM 12119 O  O   . HOH QA 5 .   ? 114.982 27.029  16.994 1.00 39.34  ? 408  HOH J O   1 
HETATM 12120 O  O   . HOH QA 5 .   ? 104.716 31.747  17.666 1.00 37.22  ? 418  HOH J O   1 
HETATM 12121 O  O   . HOH QA 5 .   ? 104.046 41.430  15.335 1.00 26.42  ? 428  HOH J O   1 
HETATM 12122 O  O   . HOH QA 5 .   ? 117.519 28.202  17.283 1.00 49.62  ? 429  HOH J O   1 
HETATM 12123 O  O   . HOH QA 5 .   ? 114.054 25.440  14.981 1.00 36.59  ? 433  HOH J O   1 
HETATM 12124 O  O   . HOH QA 5 .   ? 133.593 28.521  17.575 1.00 36.65  ? 442  HOH J O   1 
HETATM 12125 O  O   . HOH QA 5 .   ? 102.569 38.872  16.848 1.00 30.87  ? 515  HOH J O   1 
HETATM 12126 O  O   . HOH QA 5 .   ? 115.489 24.692  12.536 1.00 29.59  ? 527  HOH J O   1 
HETATM 12127 O  O   . HOH QA 5 .   ? 128.002 25.205  20.200 1.00 24.79  ? 529  HOH J O   1 
HETATM 12128 O  O   . HOH QA 5 .   ? 129.319 22.045  13.106 1.00 26.66  ? 568  HOH J O   1 
HETATM 12129 O  O   . HOH QA 5 .   ? 109.958 23.192  15.783 1.00 31.29  ? 578  HOH J O   1 
HETATM 12130 O  O   . HOH QA 5 .   ? 127.658 34.469  9.577  1.00 29.17  ? 601  HOH J O   1 
HETATM 12131 O  O   . HOH QA 5 .   ? 133.832 25.416  12.387 1.00 29.22  ? 610  HOH J O   1 
HETATM 12132 O  O   . HOH QA 5 .   ? 99.429  33.318  15.314 1.00 26.73  ? 627  HOH J O   1 
HETATM 12133 O  O   . HOH QA 5 .   ? 122.232 43.286  18.260 1.00 36.45  ? 654  HOH J O   1 
HETATM 12134 O  O   . HOH QA 5 .   ? 131.024 28.777  18.545 1.00 34.19  ? 661  HOH J O   1 
HETATM 12135 O  O   . HOH QA 5 .   ? 129.197 30.000  10.269 1.00 35.09  ? 671  HOH J O   1 
HETATM 12136 O  O   . HOH QA 5 .   ? 119.193 24.442  20.921 1.00 43.33  ? 684  HOH J O   1 
HETATM 12137 O  O   . HOH QA 5 .   ? 110.758 27.076  23.425 1.00 38.79  ? 705  HOH J O   1 
HETATM 12138 O  O   . HOH QA 5 .   ? 132.182 23.671  10.741 1.00 34.57  ? 707  HOH J O   1 
HETATM 12139 O  O   . HOH QA 5 .   ? 125.505 30.134  24.901 1.00 45.17  ? 720  HOH J O   1 
HETATM 12140 O  O   . HOH QA 5 .   ? 126.992 27.018  7.107  1.00 46.05  ? 725  HOH J O   1 
HETATM 12141 O  O   . HOH QA 5 .   ? 112.280 49.528  18.174 1.00 48.04  ? 743  HOH J O   1 
HETATM 12142 O  O   . HOH QA 5 .   ? 117.696 36.614  28.040 1.00 30.97  ? 756  HOH J O   1 
HETATM 12143 O  O   . HOH QA 5 .   ? 127.333 47.068  27.704 1.00 44.78  ? 782  HOH J O   1 
HETATM 12144 O  O   . HOH QA 5 .   ? 124.207 42.727  8.737  1.00 34.82  ? 789  HOH J O   1 
HETATM 12145 O  O   . HOH QA 5 .   ? 133.332 26.207  16.838 1.00 32.12  ? 818  HOH J O   1 
HETATM 12146 O  O   . HOH QA 5 .   ? 102.271 50.421  9.466  1.00 44.93  ? 831  HOH J O   1 
HETATM 12147 O  O   . HOH QA 5 .   ? 124.805 25.447  0.083  1.00 51.38  ? 837  HOH J O   1 
HETATM 12148 O  O   . HOH QA 5 .   ? 131.846 21.568  12.115 1.00 29.48  ? 866  HOH J O   1 
HETATM 12149 O  O   . HOH QA 5 .   ? 105.462 27.012  5.074  1.00 49.25  ? 870  HOH J O   1 
HETATM 12150 O  O   . HOH QA 5 .   ? 116.178 46.379  -1.392 1.00 39.97  ? 894  HOH J O   1 
HETATM 12151 O  O   . HOH QA 5 .   ? 110.656 26.181  6.029  1.00 42.55  ? 939  HOH J O   1 
HETATM 12152 O  O   . HOH QA 5 .   ? 114.283 24.204  9.041  1.00 44.22  ? 940  HOH J O   1 
HETATM 12153 O  O   . HOH QA 5 .   ? 111.162 23.074  7.234  1.00 64.54  ? 941  HOH J O   1 
HETATM 12154 O  O   . HOH QA 5 .   ? 118.659 28.633  2.195  1.00 29.55  ? 951  HOH J O   1 
HETATM 12155 O  O   . HOH QA 5 .   ? 119.681 30.404  0.898  1.00 43.59  ? 952  HOH J O   1 
HETATM 12156 O  O   . HOH QA 5 .   ? 110.198 24.386  20.292 1.00 50.98  ? 957  HOH J O   1 
HETATM 12157 O  O   . HOH QA 5 .   ? 108.733 23.975  18.136 1.00 38.99  ? 958  HOH J O   1 
HETATM 12158 O  O   . HOH QA 5 .   ? 116.728 26.546  19.336 1.00 28.76  ? 959  HOH J O   1 
HETATM 12159 O  O   . HOH QA 5 .   ? 128.513 40.982  20.118 1.00 27.73  ? 1014 HOH J O   1 
HETATM 12160 O  O   . HOH QA 5 .   ? 118.952 49.819  15.826 1.00 43.47  ? 1015 HOH J O   1 
HETATM 12161 O  O   . HOH QA 5 .   ? 125.369 17.354  21.647 1.00 24.40  ? 1038 HOH J O   1 
HETATM 12162 O  O   . HOH QA 5 .   ? 123.093 17.377  19.086 1.00 28.21  ? 1039 HOH J O   1 
HETATM 12163 O  O   . HOH QA 5 .   ? 119.751 17.265  17.410 1.00 56.97  ? 1040 HOH J O   1 
HETATM 12164 O  O   . HOH QA 5 .   ? 127.416 35.997  24.725 1.00 37.55  ? 1044 HOH J O   1 
HETATM 12165 O  O   . HOH QA 5 .   ? 127.678 33.228  23.910 1.00 80.41  ? 1045 HOH J O   1 
HETATM 12166 O  O   . HOH QA 5 .   ? 128.252 32.307  17.898 1.00 33.92  ? 1046 HOH J O   1 
HETATM 12167 O  O   . HOH QA 5 .   ? 130.146 30.158  16.305 1.00 34.68  ? 1047 HOH J O   1 
HETATM 12168 O  O   . HOH QA 5 .   ? 128.694 32.259  20.499 1.00 37.80  ? 1048 HOH J O   1 
HETATM 12169 O  O   . HOH QA 5 .   ? 125.014 28.243  22.239 1.00 27.14  ? 1049 HOH J O   1 
HETATM 12170 O  O   . HOH QA 5 .   ? 129.247 34.744  16.385 1.00 41.61  ? 1054 HOH J O   1 
HETATM 12171 O  O   . HOH QA 5 .   ? 108.485 48.987  10.219 1.00 39.19  ? 1109 HOH J O   1 
HETATM 12172 O  O   . HOH QA 5 .   ? 107.651 50.497  14.565 1.00 49.93  ? 1111 HOH J O   1 
HETATM 12173 O  O   . HOH QA 5 .   ? 108.596 51.805  16.461 1.00 55.63  ? 1112 HOH J O   1 
HETATM 12174 O  O   . HOH QA 5 .   ? 110.964 51.310  15.702 1.00 56.03  ? 1113 HOH J O   1 
HETATM 12175 O  O   . HOH QA 5 .   ? 103.774 39.780  19.483 1.00 38.53  ? 1114 HOH J O   1 
HETATM 12176 O  O   . HOH QA 5 .   ? 104.033 36.507  20.223 1.00 51.59  ? 1116 HOH J O   1 
HETATM 12177 O  O   . HOH QA 5 .   ? 107.261 39.322  26.749 1.00 39.55  ? 1117 HOH J O   1 
HETATM 12178 O  O   . HOH QA 5 .   ? 110.187 36.555  27.586 1.00 47.15  ? 1118 HOH J O   1 
HETATM 12179 O  O   . HOH QA 5 .   ? 118.871 34.147  27.967 1.00 40.10  ? 1119 HOH J O   1 
HETATM 12180 O  O   . HOH QA 5 .   ? 105.473 38.903  30.333 1.00 62.06  ? 1120 HOH J O   1 
HETATM 12181 O  O   . HOH QA 5 .   ? 115.959 37.438  29.874 1.00 38.20  ? 1121 HOH J O   1 
HETATM 12182 O  O   . HOH QA 5 .   ? 113.919 35.495  30.011 1.00 51.22  ? 1122 HOH J O   1 
HETATM 12183 O  O   . HOH QA 5 .   ? 116.596 45.545  29.636 1.00 39.34  ? 1125 HOH J O   1 
HETATM 12184 O  O   . HOH QA 5 .   ? 115.249 47.971  29.351 1.00 55.68  ? 1126 HOH J O   1 
HETATM 12185 O  O   . HOH QA 5 .   ? 127.513 42.921  25.409 1.00 52.35  ? 1149 HOH J O   1 
HETATM 12186 O  O   . HOH QA 5 .   ? 118.194 21.982  9.205  1.00 36.41  ? 1175 HOH J O   1 
HETATM 12187 O  O   . HOH QA 5 .   ? 129.476 27.658  5.702  1.00 58.61  ? 1180 HOH J O   1 
HETATM 12188 O  O   . HOH QA 5 .   ? 129.807 29.712  2.557  1.00 49.47  ? 1181 HOH J O   1 
HETATM 12189 O  O   . HOH QA 5 .   ? 123.495 38.805  13.324 1.00 32.39  ? 1186 HOH J O   1 
HETATM 12190 O  O   . HOH QA 5 .   ? 121.424 11.389  18.178 1.00 64.56  ? 1190 HOH J O   1 
HETATM 12191 O  O   . HOH QA 5 .   ? 127.881 23.360  9.579  1.00 39.90  ? 1202 HOH J O   1 
HETATM 12192 O  O   . HOH QA 5 .   ? 128.562 20.060  9.649  1.00 46.66  ? 1203 HOH J O   1 
HETATM 12193 O  O   . HOH QA 5 .   ? 125.280 42.750  5.801  1.00 46.72  ? 1207 HOH J O   1 
HETATM 12194 O  O   . HOH QA 5 .   ? 122.862 36.317  -1.127 1.00 68.36  ? 1208 HOH J O   1 
HETATM 12195 O  O   . HOH QA 5 .   ? 113.602 26.015  20.063 1.00 41.14  ? 1220 HOH J O   1 
HETATM 12196 O  O   . HOH QA 5 .   ? 99.938  36.962  20.823 1.00 39.00  ? 1221 HOH J O   1 
HETATM 12197 O  O   . HOH QA 5 .   ? 133.876 23.800  14.757 1.00 36.08  ? 1222 HOH J O   1 
HETATM 12198 O  O   . HOH QA 5 .   ? 97.243  26.248  14.663 1.00 45.26  ? 1225 HOH J O   1 
HETATM 12199 O  O   . HOH QA 5 .   ? 102.929 24.822  14.054 1.00 49.70  ? 1228 HOH J O   1 
HETATM 12200 O  O   . HOH QA 5 .   ? 128.573 27.847  3.337  1.00 42.89  ? 1238 HOH J O   1 
HETATM 12201 O  O   . HOH QA 5 .   ? 122.955 46.398  21.408 1.00 33.19  ? 1257 HOH J O   1 
HETATM 12202 O  O   . HOH QA 5 .   ? 122.940 39.370  6.766  1.00 36.89  ? 1268 HOH J O   1 
HETATM 12203 O  O   . HOH QA 5 .   ? 122.255 31.332  1.022  1.00 40.85  ? 1276 HOH J O   1 
HETATM 12204 O  O   . HOH QA 5 .   ? 119.088 23.722  -1.826 1.00 46.33  ? 1293 HOH J O   1 
HETATM 12205 O  O   . HOH QA 5 .   ? 121.917 32.075  12.103 1.00 23.07  ? 1360 HOH J O   1 
HETATM 12206 O  O   . HOH QA 5 .   ? 116.319 27.625  3.119  1.00 28.46  ? 1361 HOH J O   1 
HETATM 12207 O  O   . HOH QA 5 .   ? 130.085 24.483  9.640  1.00 36.67  ? 1371 HOH J O   1 
HETATM 12208 O  O   . HOH QA 5 .   ? 121.240 15.440  18.637 1.00 44.27  ? 1376 HOH J O   1 
HETATM 12209 O  O   . HOH QA 5 .   ? 126.152 25.049  7.934  1.00 43.21  ? 1390 HOH J O   1 
HETATM 12210 O  O   . HOH QA 5 .   ? 104.258 34.089  16.561 1.00 44.87  ? 1395 HOH J O   1 
HETATM 12211 O  O   . HOH QA 5 .   ? 131.891 40.220  9.816  1.00 39.76  ? 1397 HOH J O   1 
HETATM 12212 O  O   . HOH QA 5 .   ? 107.370 32.681  1.522  1.00 40.08  ? 1402 HOH J O   1 
HETATM 12213 O  O   . HOH QA 5 .   ? 103.159 35.968  18.167 1.00 41.73  ? 1409 HOH J O   1 
HETATM 12214 O  O   . HOH QA 5 .   ? 122.739 38.186  2.877  1.00 48.02  ? 1425 HOH J O   1 
HETATM 12215 O  O   . HOH QA 5 .   ? 108.521 33.084  26.604 1.00 51.76  ? 1433 HOH J O   1 
HETATM 12216 O  O   . HOH QA 5 .   ? 124.567 25.888  23.912 1.00 51.27  ? 1446 HOH J O   1 
HETATM 12217 O  O   . HOH QA 5 .   ? 111.537 35.471  -2.489 1.00 52.82  ? 1468 HOH J O   1 
HETATM 12218 O  O   . HOH QA 5 .   ? 115.842 39.424  -1.103 1.00 46.17  ? 1470 HOH J O   1 
HETATM 12219 O  O   . HOH QA 5 .   ? 124.432 39.934  9.054  1.00 41.34  ? 1481 HOH J O   1 
HETATM 12220 O  O   . HOH QA 5 .   ? 105.856 32.095  24.215 1.00 44.97  ? 1482 HOH J O   1 
HETATM 12221 O  O   . HOH QA 5 .   ? 119.919 47.828  8.862  1.00 45.44  ? 1483 HOH J O   1 
HETATM 12222 O  O   . HOH QA 5 .   ? 127.612 29.628  20.491 1.00 49.24  ? 1511 HOH J 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 CYS 111 111 111 CYS CYS 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 CYS 111 111 111 CYS CYS 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 C . n 
C 1 2   THR 2   2   2   THR THR C . n 
C 1 3   LYS 3   3   3   LYS LYS C . n 
C 1 4   ALA 4   4   4   ALA ALA C . n 
C 1 5   VAL 5   5   5   VAL VAL C . n 
C 1 6   CYS 6   6   6   CYS CYS C . n 
C 1 7   VAL 7   7   7   VAL VAL C . n 
C 1 8   LEU 8   8   8   LEU LEU C . n 
C 1 9   LYS 9   9   9   LYS LYS C . n 
C 1 10  GLY 10  10  10  GLY GLY C . n 
C 1 11  ASP 11  11  11  ASP ASP C . n 
C 1 12  GLY 12  12  12  GLY GLY C . n 
C 1 13  PRO 13  13  13  PRO PRO C . n 
C 1 14  VAL 14  14  14  VAL VAL C . n 
C 1 15  GLN 15  15  15  GLN GLN C . n 
C 1 16  GLY 16  16  16  GLY GLY C . n 
C 1 17  ILE 17  17  17  ILE ILE C . n 
C 1 18  ILE 18  18  18  ILE ILE C . n 
C 1 19  ASN 19  19  19  ASN ASN C . n 
C 1 20  PHE 20  20  20  PHE PHE C . n 
C 1 21  GLU 21  21  21  GLU GLU C . n 
C 1 22  GLN 22  22  22  GLN GLN C . n 
C 1 23  LYS 23  23  23  LYS LYS C . n 
C 1 24  GLU 24  24  24  GLU GLU C . n 
C 1 25  SER 25  25  25  SER SER C . n 
C 1 26  ASN 26  26  26  ASN ASN C . n 
C 1 27  GLY 27  27  27  GLY GLY C . n 
C 1 28  PRO 28  28  28  PRO PRO C . n 
C 1 29  VAL 29  29  29  VAL VAL C . n 
C 1 30  LYS 30  30  30  LYS LYS C . n 
C 1 31  VAL 31  31  31  VAL VAL C . n 
C 1 32  TRP 32  32  32  TRP TRP C . n 
C 1 33  GLY 33  33  33  GLY GLY C . n 
C 1 34  SER 34  34  34  SER SER C . n 
C 1 35  ILE 35  35  35  ILE ILE C . n 
C 1 36  LYS 36  36  36  LYS LYS C . n 
C 1 37  GLY 37  37  37  GLY GLY C . n 
C 1 38  LEU 38  38  38  LEU LEU C . n 
C 1 39  THR 39  39  39  THR THR C . n 
C 1 40  GLU 40  40  40  GLU GLU C . n 
C 1 41  GLY 41  41  41  GLY GLY C . n 
C 1 42  LEU 42  42  42  LEU LEU C . n 
C 1 43  HIS 43  43  43  HIS HIS C . n 
C 1 44  GLY 44  44  44  GLY GLY C . n 
C 1 45  PHE 45  45  45  PHE PHE C . n 
C 1 46  HIS 46  46  46  HIS HIS C . n 
C 1 47  VAL 47  47  47  VAL VAL C . n 
C 1 48  HIS 48  48  48  HIS HIS C . n 
C 1 49  GLU 49  49  49  GLU GLU C . n 
C 1 50  PHE 50  50  50  PHE PHE C . n 
C 1 51  GLY 51  51  51  GLY GLY C . n 
C 1 52  ASP 52  52  52  ASP ASP C . n 
C 1 53  ASN 53  53  53  ASN ASN C . n 
C 1 54  THR 54  54  54  THR THR C . n 
C 1 55  ALA 55  55  55  ALA ALA C . n 
C 1 56  GLY 56  56  56  GLY GLY C . n 
C 1 57  CYS 57  57  57  CYS CYS C . n 
C 1 58  THR 58  58  58  THR THR C . n 
C 1 59  SER 59  59  59  SER SER C . n 
C 1 60  ALA 60  60  60  ALA ALA C . n 
C 1 61  GLY 61  61  61  GLY GLY C . n 
C 1 62  PRO 62  62  62  PRO PRO C . n 
C 1 63  HIS 63  63  63  HIS HIS C . n 
C 1 64  PHE 64  64  64  PHE PHE C . n 
C 1 65  ASN 65  65  65  ASN ASN C . n 
C 1 66  PRO 66  66  66  PRO PRO C . n 
C 1 67  LEU 67  67  67  LEU LEU C . n 
C 1 68  SER 68  68  68  SER SER C . n 
C 1 69  ARG 69  69  69  ARG ARG C . n 
C 1 70  LYS 70  70  70  LYS LYS C . n 
C 1 71  HIS 71  71  71  HIS HIS C . n 
C 1 72  GLY 72  72  72  GLY GLY C . n 
C 1 73  GLY 73  73  73  GLY GLY C . n 
C 1 74  PRO 74  74  74  PRO PRO C . n 
C 1 75  LYS 75  75  75  LYS LYS C . n 
C 1 76  ASP 76  76  76  ASP ASP C . n 
C 1 77  GLU 77  77  77  GLU GLU C . n 
C 1 78  GLU 78  78  78  GLU GLU C . n 
C 1 79  ARG 79  79  79  ARG ARG C . n 
C 1 80  HIS 80  80  80  HIS HIS C . n 
C 1 81  VAL 81  81  81  VAL VAL C . n 
C 1 82  GLY 82  82  82  GLY GLY C . n 
C 1 83  ASP 83  83  83  ASP ASP C . n 
C 1 84  LEU 84  84  84  LEU LEU C . n 
C 1 85  GLY 85  85  85  GLY GLY C . n 
C 1 86  ASN 86  86  86  ASN ASN C . n 
C 1 87  VAL 87  87  87  VAL VAL C . n 
C 1 88  THR 88  88  88  THR THR C . n 
C 1 89  ALA 89  89  89  ALA ALA C . n 
C 1 90  ASP 90  90  90  ASP ASP C . n 
C 1 91  LYS 91  91  91  LYS LYS C . n 
C 1 92  ASP 92  92  92  ASP ASP C . n 
C 1 93  GLY 93  93  93  GLY GLY C . n 
C 1 94  VAL 94  94  94  VAL VAL C . n 
C 1 95  ALA 95  95  95  ALA ALA C . n 
C 1 96  ASP 96  96  96  ASP ASP C . n 
C 1 97  VAL 97  97  97  VAL VAL C . n 
C 1 98  SER 98  98  98  SER SER C . n 
C 1 99  ILE 99  99  99  ILE ILE C . n 
C 1 100 GLU 100 100 100 GLU GLU C . n 
C 1 101 ASP 101 101 101 ASP ASP C . n 
C 1 102 SER 102 102 102 SER SER C . n 
C 1 103 VAL 103 103 103 VAL VAL C . n 
C 1 104 ILE 104 104 104 ILE ILE C . n 
C 1 105 SER 105 105 105 SER SER C . n 
C 1 106 LEU 106 106 106 LEU LEU C . n 
C 1 107 SER 107 107 107 SER SER C . n 
C 1 108 GLY 108 108 108 GLY GLY C . n 
C 1 109 ASP 109 109 109 ASP ASP C . n 
C 1 110 HIS 110 110 110 HIS HIS C . n 
C 1 111 CYS 111 111 111 CYS CYS C . n 
C 1 112 ILE 112 112 112 ILE ILE C . n 
C 1 113 ILE 113 113 113 ILE ILE C . n 
C 1 114 GLY 114 114 114 GLY GLY C . n 
C 1 115 ARG 115 115 115 ARG ARG C . n 
C 1 116 THR 116 116 116 THR THR C . n 
C 1 117 LEU 117 117 117 LEU LEU C . n 
C 1 118 VAL 118 118 118 VAL VAL C . n 
C 1 119 VAL 119 119 119 VAL VAL C . n 
C 1 120 HIS 120 120 120 HIS HIS C . n 
C 1 121 GLU 121 121 121 GLU GLU C . n 
C 1 122 LYS 122 122 122 LYS LYS C . n 
C 1 123 ALA 123 123 123 ALA ALA C . n 
C 1 124 ASP 124 124 124 ASP ASP C . n 
C 1 125 ASP 125 125 125 ASP ASP C . n 
C 1 126 LEU 126 126 126 LEU LEU C . n 
C 1 127 GLY 127 127 127 GLY GLY C . n 
C 1 128 LYS 128 128 128 LYS LYS C . n 
C 1 129 GLY 129 129 129 GLY GLY C . n 
C 1 130 GLY 130 130 130 GLY GLY C . n 
C 1 131 ASN 131 131 131 ASN ASN C . n 
C 1 132 GLU 132 132 132 GLU GLU C . n 
C 1 133 GLU 133 133 133 GLU GLU C . n 
C 1 134 SER 134 134 134 SER SER C . n 
C 1 135 THR 135 135 135 THR THR C . n 
C 1 136 LYS 136 136 136 LYS LYS C . n 
C 1 137 THR 137 137 137 THR THR C . n 
C 1 138 GLY 138 138 138 GLY GLY C . n 
C 1 139 ASN 139 139 139 ASN ASN C . n 
C 1 140 ALA 140 140 140 ALA ALA C . n 
C 1 141 GLY 141 141 141 GLY GLY C . n 
C 1 142 SER 142 142 142 SER SER C . n 
C 1 143 ARG 143 143 143 ARG ARG C . n 
C 1 144 LEU 144 144 144 LEU LEU C . n 
C 1 145 ALA 145 145 145 ALA ALA C . n 
C 1 146 CYS 146 146 146 CYS CYS C . n 
C 1 147 GLY 147 147 147 GLY GLY C . n 
C 1 148 VAL 148 148 148 VAL VAL C . n 
C 1 149 ILE 149 149 149 ILE ILE C . n 
C 1 150 GLY 150 150 150 GLY GLY C . n 
C 1 151 ILE 151 151 151 ILE ILE C . n 
C 1 152 ALA 152 152 152 ALA ALA C . n 
C 1 153 GLN 153 153 153 GLN GLN C . n 
D 1 1   ALA 1   1   1   ALA ALA D . n 
D 1 2   THR 2   2   2   THR THR D . n 
D 1 3   LYS 3   3   3   LYS LYS D . n 
D 1 4   ALA 4   4   4   ALA ALA D . n 
D 1 5   VAL 5   5   5   VAL VAL D . n 
D 1 6   CYS 6   6   6   CYS CYS D . n 
D 1 7   VAL 7   7   7   VAL VAL D . n 
D 1 8   LEU 8   8   8   LEU LEU D . n 
D 1 9   LYS 9   9   9   LYS LYS D . n 
D 1 10  GLY 10  10  10  GLY GLY D . n 
D 1 11  ASP 11  11  11  ASP ASP D . n 
D 1 12  GLY 12  12  12  GLY GLY D . n 
D 1 13  PRO 13  13  13  PRO PRO D . n 
D 1 14  VAL 14  14  14  VAL VAL D . n 
D 1 15  GLN 15  15  15  GLN GLN D . n 
D 1 16  GLY 16  16  16  GLY GLY D . n 
D 1 17  ILE 17  17  17  ILE ILE D . n 
D 1 18  ILE 18  18  18  ILE ILE D . n 
D 1 19  ASN 19  19  19  ASN ASN D . n 
D 1 20  PHE 20  20  20  PHE PHE D . n 
D 1 21  GLU 21  21  21  GLU GLU D . n 
D 1 22  GLN 22  22  22  GLN GLN D . n 
D 1 23  LYS 23  23  23  LYS LYS D . n 
D 1 24  GLU 24  24  24  GLU GLU D . n 
D 1 25  SER 25  25  25  SER SER D . n 
D 1 26  ASN 26  26  26  ASN ASN D . n 
D 1 27  GLY 27  27  27  GLY GLY D . n 
D 1 28  PRO 28  28  28  PRO PRO D . n 
D 1 29  VAL 29  29  29  VAL VAL D . n 
D 1 30  LYS 30  30  30  LYS LYS D . n 
D 1 31  VAL 31  31  31  VAL VAL D . n 
D 1 32  TRP 32  32  32  TRP TRP D . n 
D 1 33  GLY 33  33  33  GLY GLY D . n 
D 1 34  SER 34  34  34  SER SER D . n 
D 1 35  ILE 35  35  35  ILE ILE D . n 
D 1 36  LYS 36  36  36  LYS LYS D . n 
D 1 37  GLY 37  37  37  GLY GLY D . n 
D 1 38  LEU 38  38  38  LEU LEU D . n 
D 1 39  THR 39  39  39  THR THR D . n 
D 1 40  GLU 40  40  40  GLU GLU D . n 
D 1 41  GLY 41  41  41  GLY GLY D . n 
D 1 42  LEU 42  42  42  LEU LEU D . n 
D 1 43  HIS 43  43  43  HIS HIS D . n 
D 1 44  GLY 44  44  44  GLY GLY D . n 
D 1 45  PHE 45  45  45  PHE PHE D . n 
D 1 46  HIS 46  46  46  HIS HIS D . n 
D 1 47  VAL 47  47  47  VAL VAL D . n 
D 1 48  HIS 48  48  48  HIS HIS D . n 
D 1 49  GLU 49  49  49  GLU GLU D . n 
D 1 50  PHE 50  50  50  PHE PHE D . n 
D 1 51  GLY 51  51  51  GLY GLY D . n 
D 1 52  ASP 52  52  52  ASP ASP D . n 
D 1 53  ASN 53  53  53  ASN ASN D . n 
D 1 54  THR 54  54  54  THR THR D . n 
D 1 55  ALA 55  55  55  ALA ALA D . n 
D 1 56  GLY 56  56  56  GLY GLY D . n 
D 1 57  CYS 57  57  57  CYS CYS D . n 
D 1 58  THR 58  58  58  THR THR D . n 
D 1 59  SER 59  59  59  SER SER D . n 
D 1 60  ALA 60  60  60  ALA ALA D . n 
D 1 61  GLY 61  61  61  GLY GLY D . n 
D 1 62  PRO 62  62  62  PRO PRO D . n 
D 1 63  HIS 63  63  63  HIS HIS D . n 
D 1 64  PHE 64  64  64  PHE PHE D . n 
D 1 65  ASN 65  65  65  ASN ASN D . n 
D 1 66  PRO 66  66  66  PRO PRO D . n 
D 1 67  LEU 67  67  67  LEU LEU D . n 
D 1 68  SER 68  68  68  SER SER D . n 
D 1 69  ARG 69  69  69  ARG ARG D . n 
D 1 70  LYS 70  70  70  LYS LYS D . n 
D 1 71  HIS 71  71  71  HIS HIS D . n 
D 1 72  GLY 72  72  72  GLY GLY D . n 
D 1 73  GLY 73  73  73  GLY GLY D . n 
D 1 74  PRO 74  74  74  PRO PRO D . n 
D 1 75  LYS 75  75  75  LYS LYS D . n 
D 1 76  ASP 76  76  76  ASP ASP D . n 
D 1 77  GLU 77  77  77  GLU GLU D . n 
D 1 78  GLU 78  78  78  GLU GLU D . n 
D 1 79  ARG 79  79  79  ARG ARG D . n 
D 1 80  HIS 80  80  80  HIS HIS D . n 
D 1 81  VAL 81  81  81  VAL VAL D . n 
D 1 82  GLY 82  82  82  GLY GLY D . n 
D 1 83  ASP 83  83  83  ASP ASP D . n 
D 1 84  LEU 84  84  84  LEU LEU D . n 
D 1 85  GLY 85  85  85  GLY GLY D . n 
D 1 86  ASN 86  86  86  ASN ASN D . n 
D 1 87  VAL 87  87  87  VAL VAL D . n 
D 1 88  THR 88  88  88  THR THR D . n 
D 1 89  ALA 89  89  89  ALA ALA D . n 
D 1 90  ASP 90  90  90  ASP ASP D . n 
D 1 91  LYS 91  91  91  LYS LYS D . n 
D 1 92  ASP 92  92  92  ASP ASP D . n 
D 1 93  GLY 93  93  93  GLY GLY D . n 
D 1 94  VAL 94  94  94  VAL VAL D . n 
D 1 95  ALA 95  95  95  ALA ALA D . n 
D 1 96  ASP 96  96  96  ASP ASP D . n 
D 1 97  VAL 97  97  97  VAL VAL D . n 
D 1 98  SER 98  98  98  SER SER D . n 
D 1 99  ILE 99  99  99  ILE ILE D . n 
D 1 100 GLU 100 100 100 GLU GLU D . n 
D 1 101 ASP 101 101 101 ASP ASP D . n 
D 1 102 SER 102 102 102 SER SER D . n 
D 1 103 VAL 103 103 103 VAL VAL D . n 
D 1 104 ILE 104 104 104 ILE ILE D . n 
D 1 105 SER 105 105 105 SER SER D . n 
D 1 106 LEU 106 106 106 LEU LEU D . n 
D 1 107 SER 107 107 107 SER SER D . n 
D 1 108 GLY 108 108 108 GLY GLY D . n 
D 1 109 ASP 109 109 109 ASP ASP D . n 
D 1 110 HIS 110 110 110 HIS HIS D . n 
D 1 111 CYS 111 111 111 CYS CYS D . n 
D 1 112 ILE 112 112 112 ILE ILE D . n 
D 1 113 ILE 113 113 113 ILE ILE D . n 
D 1 114 GLY 114 114 114 GLY GLY D . n 
D 1 115 ARG 115 115 115 ARG ARG D . n 
D 1 116 THR 116 116 116 THR THR D . n 
D 1 117 LEU 117 117 117 LEU LEU D . n 
D 1 118 VAL 118 118 118 VAL VAL D . n 
D 1 119 VAL 119 119 119 VAL VAL D . n 
D 1 120 HIS 120 120 120 HIS HIS D . n 
D 1 121 GLU 121 121 121 GLU GLU D . n 
D 1 122 LYS 122 122 122 LYS LYS D . n 
D 1 123 ALA 123 123 123 ALA ALA D . n 
D 1 124 ASP 124 124 124 ASP ASP D . n 
D 1 125 ASP 125 125 125 ASP ASP D . n 
D 1 126 LEU 126 126 126 LEU LEU D . n 
D 1 127 GLY 127 127 127 GLY GLY D . n 
D 1 128 LYS 128 128 128 LYS LYS D . n 
D 1 129 GLY 129 129 129 GLY GLY D . n 
D 1 130 GLY 130 130 130 GLY GLY D . n 
D 1 131 ASN 131 131 131 ASN ASN D . n 
D 1 132 GLU 132 132 132 GLU GLU D . n 
D 1 133 GLU 133 133 133 GLU GLU D . n 
D 1 134 SER 134 134 134 SER SER D . n 
D 1 135 THR 135 135 135 THR THR D . n 
D 1 136 LYS 136 136 136 LYS LYS D . n 
D 1 137 THR 137 137 137 THR THR D . n 
D 1 138 GLY 138 138 138 GLY GLY D . n 
D 1 139 ASN 139 139 139 ASN ASN D . n 
D 1 140 ALA 140 140 140 ALA ALA D . n 
D 1 141 GLY 141 141 141 GLY GLY D . n 
D 1 142 SER 142 142 142 SER SER D . n 
D 1 143 ARG 143 143 143 ARG ARG D . n 
D 1 144 LEU 144 144 144 LEU LEU D . n 
D 1 145 ALA 145 145 145 ALA ALA D . n 
D 1 146 CYS 146 146 146 CYS CYS D . n 
D 1 147 GLY 147 147 147 GLY GLY D . n 
D 1 148 VAL 148 148 148 VAL VAL D . n 
D 1 149 ILE 149 149 149 ILE ILE D . n 
D 1 150 GLY 150 150 150 GLY GLY D . n 
D 1 151 ILE 151 151 151 ILE ILE D . n 
D 1 152 ALA 152 152 152 ALA ALA D . n 
D 1 153 GLN 153 153 153 GLN GLN D . n 
E 1 1   ALA 1   1   1   ALA ALA E . n 
E 1 2   THR 2   2   2   THR THR E . n 
E 1 3   LYS 3   3   3   LYS LYS E . n 
E 1 4   ALA 4   4   4   ALA ALA E . n 
E 1 5   VAL 5   5   5   VAL VAL E . n 
E 1 6   CYS 6   6   6   CYS CYS E . n 
E 1 7   VAL 7   7   7   VAL VAL E . n 
E 1 8   LEU 8   8   8   LEU LEU E . n 
E 1 9   LYS 9   9   9   LYS LYS E . n 
E 1 10  GLY 10  10  10  GLY GLY E . n 
E 1 11  ASP 11  11  11  ASP ASP E . n 
E 1 12  GLY 12  12  12  GLY GLY E . n 
E 1 13  PRO 13  13  13  PRO PRO E . n 
E 1 14  VAL 14  14  14  VAL VAL E . n 
E 1 15  GLN 15  15  15  GLN GLN E . n 
E 1 16  GLY 16  16  16  GLY GLY E . n 
E 1 17  ILE 17  17  17  ILE ILE E . n 
E 1 18  ILE 18  18  18  ILE ILE E . n 
E 1 19  ASN 19  19  19  ASN ASN E . n 
E 1 20  PHE 20  20  20  PHE PHE E . n 
E 1 21  GLU 21  21  21  GLU GLU E . n 
E 1 22  GLN 22  22  22  GLN GLN E . n 
E 1 23  LYS 23  23  23  LYS LYS E . n 
E 1 24  GLU 24  24  24  GLU GLU E . n 
E 1 25  SER 25  25  25  SER SER E . n 
E 1 26  ASN 26  26  26  ASN ASN E . n 
E 1 27  GLY 27  27  27  GLY GLY E . n 
E 1 28  PRO 28  28  28  PRO PRO E . n 
E 1 29  VAL 29  29  29  VAL VAL E . n 
E 1 30  LYS 30  30  30  LYS LYS E . n 
E 1 31  VAL 31  31  31  VAL VAL E . n 
E 1 32  TRP 32  32  32  TRP TRP E . n 
E 1 33  GLY 33  33  33  GLY GLY E . n 
E 1 34  SER 34  34  34  SER SER E . n 
E 1 35  ILE 35  35  35  ILE ILE E . n 
E 1 36  LYS 36  36  36  LYS LYS E . n 
E 1 37  GLY 37  37  37  GLY GLY E . n 
E 1 38  LEU 38  38  38  LEU LEU E . n 
E 1 39  THR 39  39  39  THR THR E . n 
E 1 40  GLU 40  40  40  GLU GLU E . n 
E 1 41  GLY 41  41  41  GLY GLY E . n 
E 1 42  LEU 42  42  42  LEU LEU E . n 
E 1 43  HIS 43  43  43  HIS HIS E . n 
E 1 44  GLY 44  44  44  GLY GLY E . n 
E 1 45  PHE 45  45  45  PHE PHE E . n 
E 1 46  HIS 46  46  46  HIS HIS E . n 
E 1 47  VAL 47  47  47  VAL VAL E . n 
E 1 48  HIS 48  48  48  HIS HIS E . n 
E 1 49  GLU 49  49  49  GLU GLU E . n 
E 1 50  PHE 50  50  50  PHE PHE E . n 
E 1 51  GLY 51  51  51  GLY GLY E . n 
E 1 52  ASP 52  52  52  ASP ASP E . n 
E 1 53  ASN 53  53  53  ASN ASN E . n 
E 1 54  THR 54  54  54  THR THR E . n 
E 1 55  ALA 55  55  55  ALA ALA E . n 
E 1 56  GLY 56  56  56  GLY GLY E . n 
E 1 57  CYS 57  57  57  CYS CYS E . n 
E 1 58  THR 58  58  58  THR THR E . n 
E 1 59  SER 59  59  59  SER SER E . n 
E 1 60  ALA 60  60  60  ALA ALA E . n 
E 1 61  GLY 61  61  61  GLY GLY E . n 
E 1 62  PRO 62  62  62  PRO PRO E . n 
E 1 63  HIS 63  63  63  HIS HIS E . n 
E 1 64  PHE 64  64  64  PHE PHE E . n 
E 1 65  ASN 65  65  65  ASN ASN E . n 
E 1 66  PRO 66  66  66  PRO PRO E . n 
E 1 67  LEU 67  67  67  LEU LEU E . n 
E 1 68  SER 68  68  68  SER SER E . n 
E 1 69  ARG 69  69  69  ARG ARG E . n 
E 1 70  LYS 70  70  70  LYS LYS E . n 
E 1 71  HIS 71  71  71  HIS HIS E . n 
E 1 72  GLY 72  72  72  GLY GLY E . n 
E 1 73  GLY 73  73  73  GLY GLY E . n 
E 1 74  PRO 74  74  74  PRO PRO E . n 
E 1 75  LYS 75  75  75  LYS LYS E . n 
E 1 76  ASP 76  76  76  ASP ASP E . n 
E 1 77  GLU 77  77  77  GLU GLU E . n 
E 1 78  GLU 78  78  78  GLU GLU E . n 
E 1 79  ARG 79  79  79  ARG ARG E . n 
E 1 80  HIS 80  80  80  HIS HIS E . n 
E 1 81  VAL 81  81  81  VAL VAL E . n 
E 1 82  GLY 82  82  82  GLY GLY E . n 
E 1 83  ASP 83  83  83  ASP ASP E . n 
E 1 84  LEU 84  84  84  LEU LEU E . n 
E 1 85  GLY 85  85  85  GLY GLY E . n 
E 1 86  ASN 86  86  86  ASN ASN E . n 
E 1 87  VAL 87  87  87  VAL VAL E . n 
E 1 88  THR 88  88  88  THR THR E . n 
E 1 89  ALA 89  89  89  ALA ALA E . n 
E 1 90  ASP 90  90  90  ASP ASP E . n 
E 1 91  LYS 91  91  91  LYS LYS E . n 
E 1 92  ASP 92  92  92  ASP ASP E . n 
E 1 93  GLY 93  93  93  GLY GLY E . n 
E 1 94  VAL 94  94  94  VAL VAL E . n 
E 1 95  ALA 95  95  95  ALA ALA E . n 
E 1 96  ASP 96  96  96  ASP ASP E . n 
E 1 97  VAL 97  97  97  VAL VAL E . n 
E 1 98  SER 98  98  98  SER SER E . n 
E 1 99  ILE 99  99  99  ILE ILE E . n 
E 1 100 GLU 100 100 100 GLU GLU E . n 
E 1 101 ASP 101 101 101 ASP ASP E . n 
E 1 102 SER 102 102 102 SER SER E . n 
E 1 103 VAL 103 103 103 VAL VAL E . n 
E 1 104 ILE 104 104 104 ILE ILE E . n 
E 1 105 SER 105 105 105 SER SER E . n 
E 1 106 LEU 106 106 106 LEU LEU E . n 
E 1 107 SER 107 107 107 SER SER E . n 
E 1 108 GLY 108 108 108 GLY GLY E . n 
E 1 109 ASP 109 109 109 ASP ASP E . n 
E 1 110 HIS 110 110 110 HIS HIS E . n 
E 1 111 CYS 111 111 111 CYS CYS E . n 
E 1 112 ILE 112 112 112 ILE ILE E . n 
E 1 113 ILE 113 113 113 ILE ILE E . n 
E 1 114 GLY 114 114 114 GLY GLY E . n 
E 1 115 ARG 115 115 115 ARG ARG E . n 
E 1 116 THR 116 116 116 THR THR E . n 
E 1 117 LEU 117 117 117 LEU LEU E . n 
E 1 118 VAL 118 118 118 VAL VAL E . n 
E 1 119 VAL 119 119 119 VAL VAL E . n 
E 1 120 HIS 120 120 120 HIS HIS E . n 
E 1 121 GLU 121 121 121 GLU GLU E . n 
E 1 122 LYS 122 122 122 LYS LYS E . n 
E 1 123 ALA 123 123 123 ALA ALA E . n 
E 1 124 ASP 124 124 124 ASP ASP E . n 
E 1 125 ASP 125 125 125 ASP ASP E . n 
E 1 126 LEU 126 126 126 LEU LEU E . n 
E 1 127 GLY 127 127 127 GLY GLY E . n 
E 1 128 LYS 128 128 128 LYS LYS E . n 
E 1 129 GLY 129 129 129 GLY GLY E . n 
E 1 130 GLY 130 130 130 GLY GLY E . n 
E 1 131 ASN 131 131 131 ASN ASN E . n 
E 1 132 GLU 132 132 132 GLU GLU E . n 
E 1 133 GLU 133 133 133 GLU GLU E . n 
E 1 134 SER 134 134 134 SER SER E . n 
E 1 135 THR 135 135 135 THR THR E . n 
E 1 136 LYS 136 136 136 LYS LYS E . n 
E 1 137 THR 137 137 137 THR THR E . n 
E 1 138 GLY 138 138 138 GLY GLY E . n 
E 1 139 ASN 139 139 139 ASN ASN E . n 
E 1 140 ALA 140 140 140 ALA ALA E . n 
E 1 141 GLY 141 141 141 GLY GLY E . n 
E 1 142 SER 142 142 142 SER SER E . n 
E 1 143 ARG 143 143 143 ARG ARG E . n 
E 1 144 LEU 144 144 144 LEU LEU E . n 
E 1 145 ALA 145 145 145 ALA ALA E . n 
E 1 146 CYS 146 146 146 CYS CYS E . n 
E 1 147 GLY 147 147 147 GLY GLY E . n 
E 1 148 VAL 148 148 148 VAL VAL E . n 
E 1 149 ILE 149 149 149 ILE ILE E . n 
E 1 150 GLY 150 150 150 GLY GLY E . n 
E 1 151 ILE 151 151 151 ILE ILE E . n 
E 1 152 ALA 152 152 152 ALA ALA E . n 
E 1 153 GLN 153 153 153 GLN GLN E . n 
F 1 1   ALA 1   1   1   ALA ALA F . n 
F 1 2   THR 2   2   2   THR THR F . n 
F 1 3   LYS 3   3   3   LYS LYS F . n 
F 1 4   ALA 4   4   4   ALA ALA F . n 
F 1 5   VAL 5   5   5   VAL VAL F . n 
F 1 6   CYS 6   6   6   CYS CYS F . n 
F 1 7   VAL 7   7   7   VAL VAL F . n 
F 1 8   LEU 8   8   8   LEU LEU F . n 
F 1 9   LYS 9   9   9   LYS LYS F . n 
F 1 10  GLY 10  10  10  GLY GLY F . n 
F 1 11  ASP 11  11  11  ASP ASP F . n 
F 1 12  GLY 12  12  12  GLY GLY F . n 
F 1 13  PRO 13  13  13  PRO PRO F . n 
F 1 14  VAL 14  14  14  VAL VAL F . n 
F 1 15  GLN 15  15  15  GLN GLN F . n 
F 1 16  GLY 16  16  16  GLY GLY F . n 
F 1 17  ILE 17  17  17  ILE ILE F . n 
F 1 18  ILE 18  18  18  ILE ILE F . n 
F 1 19  ASN 19  19  19  ASN ASN F . n 
F 1 20  PHE 20  20  20  PHE PHE F . n 
F 1 21  GLU 21  21  21  GLU GLU F . n 
F 1 22  GLN 22  22  22  GLN GLN F . n 
F 1 23  LYS 23  23  23  LYS LYS F . n 
F 1 24  GLU 24  24  24  GLU GLU F . n 
F 1 25  SER 25  25  25  SER SER F . n 
F 1 26  ASN 26  26  26  ASN ASN F . n 
F 1 27  GLY 27  27  27  GLY GLY F . n 
F 1 28  PRO 28  28  28  PRO PRO F . n 
F 1 29  VAL 29  29  29  VAL VAL F . n 
F 1 30  LYS 30  30  30  LYS LYS F . n 
F 1 31  VAL 31  31  31  VAL VAL F . n 
F 1 32  TRP 32  32  32  TRP TRP F . n 
F 1 33  GLY 33  33  33  GLY GLY F . n 
F 1 34  SER 34  34  34  SER SER F . n 
F 1 35  ILE 35  35  35  ILE ILE F . n 
F 1 36  LYS 36  36  36  LYS LYS F . n 
F 1 37  GLY 37  37  37  GLY GLY F . n 
F 1 38  LEU 38  38  38  LEU LEU F . n 
F 1 39  THR 39  39  39  THR THR F . n 
F 1 40  GLU 40  40  40  GLU GLU F . n 
F 1 41  GLY 41  41  41  GLY GLY F . n 
F 1 42  LEU 42  42  42  LEU LEU F . n 
F 1 43  HIS 43  43  43  HIS HIS F . n 
F 1 44  GLY 44  44  44  GLY GLY F . n 
F 1 45  PHE 45  45  45  PHE PHE F . n 
F 1 46  HIS 46  46  46  HIS HIS F . n 
F 1 47  VAL 47  47  47  VAL VAL F . n 
F 1 48  HIS 48  48  48  HIS HIS F . n 
F 1 49  GLU 49  49  49  GLU GLU F . n 
F 1 50  PHE 50  50  50  PHE PHE F . n 
F 1 51  GLY 51  51  51  GLY GLY F . n 
F 1 52  ASP 52  52  52  ASP ASP F . n 
F 1 53  ASN 53  53  53  ASN ASN F . n 
F 1 54  THR 54  54  54  THR THR F . n 
F 1 55  ALA 55  55  55  ALA ALA F . n 
F 1 56  GLY 56  56  56  GLY GLY F . n 
F 1 57  CYS 57  57  57  CYS CYS F . n 
F 1 58  THR 58  58  58  THR THR F . n 
F 1 59  SER 59  59  59  SER SER F . n 
F 1 60  ALA 60  60  60  ALA ALA F . n 
F 1 61  GLY 61  61  61  GLY GLY F . n 
F 1 62  PRO 62  62  62  PRO PRO F . n 
F 1 63  HIS 63  63  63  HIS HIS F . n 
F 1 64  PHE 64  64  64  PHE PHE F . n 
F 1 65  ASN 65  65  65  ASN ASN F . n 
F 1 66  PRO 66  66  66  PRO PRO F . n 
F 1 67  LEU 67  67  67  LEU LEU F . n 
F 1 68  SER 68  68  68  SER SER F . n 
F 1 69  ARG 69  69  69  ARG ARG F . n 
F 1 70  LYS 70  70  70  LYS LYS F . n 
F 1 71  HIS 71  71  71  HIS HIS F . n 
F 1 72  GLY 72  72  72  GLY GLY F . n 
F 1 73  GLY 73  73  73  GLY GLY F . n 
F 1 74  PRO 74  74  74  PRO PRO F . n 
F 1 75  LYS 75  75  75  LYS LYS F . n 
F 1 76  ASP 76  76  76  ASP ASP F . n 
F 1 77  GLU 77  77  77  GLU GLU F . n 
F 1 78  GLU 78  78  78  GLU GLU F . n 
F 1 79  ARG 79  79  79  ARG ARG F . n 
F 1 80  HIS 80  80  80  HIS HIS F . n 
F 1 81  VAL 81  81  81  VAL VAL F . n 
F 1 82  GLY 82  82  82  GLY GLY F . n 
F 1 83  ASP 83  83  83  ASP ASP F . n 
F 1 84  LEU 84  84  84  LEU LEU F . n 
F 1 85  GLY 85  85  85  GLY GLY F . n 
F 1 86  ASN 86  86  86  ASN ASN F . n 
F 1 87  VAL 87  87  87  VAL VAL F . n 
F 1 88  THR 88  88  88  THR THR F . n 
F 1 89  ALA 89  89  89  ALA ALA F . n 
F 1 90  ASP 90  90  90  ASP ASP F . n 
F 1 91  LYS 91  91  91  LYS LYS F . n 
F 1 92  ASP 92  92  92  ASP ASP F . n 
F 1 93  GLY 93  93  93  GLY GLY F . n 
F 1 94  VAL 94  94  94  VAL VAL F . n 
F 1 95  ALA 95  95  95  ALA ALA F . n 
F 1 96  ASP 96  96  96  ASP ASP F . n 
F 1 97  VAL 97  97  97  VAL VAL F . n 
F 1 98  SER 98  98  98  SER SER F . n 
F 1 99  ILE 99  99  99  ILE ILE F . n 
F 1 100 GLU 100 100 100 GLU GLU F . n 
F 1 101 ASP 101 101 101 ASP ASP F . n 
F 1 102 SER 102 102 102 SER SER F . n 
F 1 103 VAL 103 103 103 VAL VAL F . n 
F 1 104 ILE 104 104 104 ILE ILE F . n 
F 1 105 SER 105 105 105 SER SER F . n 
F 1 106 LEU 106 106 106 LEU LEU F . n 
F 1 107 SER 107 107 107 SER SER F . n 
F 1 108 GLY 108 108 108 GLY GLY F . n 
F 1 109 ASP 109 109 109 ASP ASP F . n 
F 1 110 HIS 110 110 110 HIS HIS F . n 
F 1 111 CYS 111 111 111 CYS CYS F . n 
F 1 112 ILE 112 112 112 ILE ILE F . n 
F 1 113 ILE 113 113 113 ILE ILE F . n 
F 1 114 GLY 114 114 114 GLY GLY F . n 
F 1 115 ARG 115 115 115 ARG ARG F . n 
F 1 116 THR 116 116 116 THR THR F . n 
F 1 117 LEU 117 117 117 LEU LEU F . n 
F 1 118 VAL 118 118 118 VAL VAL F . n 
F 1 119 VAL 119 119 119 VAL VAL F . n 
F 1 120 HIS 120 120 120 HIS HIS F . n 
F 1 121 GLU 121 121 121 GLU GLU F . n 
F 1 122 LYS 122 122 122 LYS LYS F . n 
F 1 123 ALA 123 123 123 ALA ALA F . n 
F 1 124 ASP 124 124 124 ASP ASP F . n 
F 1 125 ASP 125 125 125 ASP ASP F . n 
F 1 126 LEU 126 126 126 LEU LEU F . n 
F 1 127 GLY 127 127 127 GLY GLY F . n 
F 1 128 LYS 128 128 128 LYS LYS F . n 
F 1 129 GLY 129 129 129 GLY GLY F . n 
F 1 130 GLY 130 130 130 GLY GLY F . n 
F 1 131 ASN 131 131 131 ASN ASN F . n 
F 1 132 GLU 132 132 132 GLU GLU F . n 
F 1 133 GLU 133 133 133 GLU GLU F . n 
F 1 134 SER 134 134 134 SER SER F . n 
F 1 135 THR 135 135 135 THR THR F . n 
F 1 136 LYS 136 136 136 LYS LYS F . n 
F 1 137 THR 137 137 137 THR THR F . n 
F 1 138 GLY 138 138 138 GLY GLY F . n 
F 1 139 ASN 139 139 139 ASN ASN F . n 
F 1 140 ALA 140 140 140 ALA ALA F . n 
F 1 141 GLY 141 141 141 GLY GLY F . n 
F 1 142 SER 142 142 142 SER SER F . n 
F 1 143 ARG 143 143 143 ARG ARG F . n 
F 1 144 LEU 144 144 144 LEU LEU F . n 
F 1 145 ALA 145 145 145 ALA ALA F . n 
F 1 146 CYS 146 146 146 CYS CYS F . n 
F 1 147 GLY 147 147 147 GLY GLY F . n 
F 1 148 VAL 148 148 148 VAL VAL F . n 
F 1 149 ILE 149 149 149 ILE ILE F . n 
F 1 150 GLY 150 150 150 GLY GLY F . n 
F 1 151 ILE 151 151 151 ILE ILE F . n 
F 1 152 ALA 152 152 152 ALA ALA F . n 
F 1 153 GLN 153 153 153 GLN GLN F . n 
G 1 1   ALA 1   1   1   ALA ALA G . n 
G 1 2   THR 2   2   2   THR THR G . n 
G 1 3   LYS 3   3   3   LYS LYS G . n 
G 1 4   ALA 4   4   4   ALA ALA G . n 
G 1 5   VAL 5   5   5   VAL VAL G . n 
G 1 6   CYS 6   6   6   CYS CYS G . n 
G 1 7   VAL 7   7   7   VAL VAL G . n 
G 1 8   LEU 8   8   8   LEU LEU G . n 
G 1 9   LYS 9   9   9   LYS LYS G . n 
G 1 10  GLY 10  10  10  GLY GLY G . n 
G 1 11  ASP 11  11  11  ASP ASP G . n 
G 1 12  GLY 12  12  12  GLY GLY G . n 
G 1 13  PRO 13  13  13  PRO PRO G . n 
G 1 14  VAL 14  14  14  VAL VAL G . n 
G 1 15  GLN 15  15  15  GLN GLN G . n 
G 1 16  GLY 16  16  16  GLY GLY G . n 
G 1 17  ILE 17  17  17  ILE ILE G . n 
G 1 18  ILE 18  18  18  ILE ILE G . n 
G 1 19  ASN 19  19  19  ASN ASN G . n 
G 1 20  PHE 20  20  20  PHE PHE G . n 
G 1 21  GLU 21  21  21  GLU GLU G . n 
G 1 22  GLN 22  22  22  GLN GLN G . n 
G 1 23  LYS 23  23  23  LYS LYS G . n 
G 1 24  GLU 24  24  24  GLU GLU G . n 
G 1 25  SER 25  25  25  SER SER G . n 
G 1 26  ASN 26  26  26  ASN ASN G . n 
G 1 27  GLY 27  27  27  GLY GLY G . n 
G 1 28  PRO 28  28  28  PRO PRO G . n 
G 1 29  VAL 29  29  29  VAL VAL G . n 
G 1 30  LYS 30  30  30  LYS LYS G . n 
G 1 31  VAL 31  31  31  VAL VAL G . n 
G 1 32  TRP 32  32  32  TRP TRP G . n 
G 1 33  GLY 33  33  33  GLY GLY G . n 
G 1 34  SER 34  34  34  SER SER G . n 
G 1 35  ILE 35  35  35  ILE ILE G . n 
G 1 36  LYS 36  36  36  LYS LYS G . n 
G 1 37  GLY 37  37  37  GLY GLY G . n 
G 1 38  LEU 38  38  38  LEU LEU G . n 
G 1 39  THR 39  39  39  THR THR G . n 
G 1 40  GLU 40  40  40  GLU GLU G . n 
G 1 41  GLY 41  41  41  GLY GLY G . n 
G 1 42  LEU 42  42  42  LEU LEU G . n 
G 1 43  HIS 43  43  43  HIS HIS G . n 
G 1 44  GLY 44  44  44  GLY GLY G . n 
G 1 45  PHE 45  45  45  PHE PHE G . n 
G 1 46  HIS 46  46  46  HIS HIS G . n 
G 1 47  VAL 47  47  47  VAL VAL G . n 
G 1 48  HIS 48  48  48  HIS HIS G . n 
G 1 49  GLU 49  49  49  GLU GLU G . n 
G 1 50  PHE 50  50  50  PHE PHE G . n 
G 1 51  GLY 51  51  51  GLY GLY G . n 
G 1 52  ASP 52  52  52  ASP ASP G . n 
G 1 53  ASN 53  53  53  ASN ASN G . n 
G 1 54  THR 54  54  54  THR THR G . n 
G 1 55  ALA 55  55  55  ALA ALA G . n 
G 1 56  GLY 56  56  56  GLY GLY G . n 
G 1 57  CYS 57  57  57  CYS CYS G . n 
G 1 58  THR 58  58  58  THR THR G . n 
G 1 59  SER 59  59  59  SER SER G . n 
G 1 60  ALA 60  60  60  ALA ALA G . n 
G 1 61  GLY 61  61  61  GLY GLY G . n 
G 1 62  PRO 62  62  62  PRO PRO G . n 
G 1 63  HIS 63  63  63  HIS HIS G . n 
G 1 64  PHE 64  64  64  PHE PHE G . n 
G 1 65  ASN 65  65  65  ASN ASN G . n 
G 1 66  PRO 66  66  66  PRO PRO G . n 
G 1 67  LEU 67  67  67  LEU LEU G . n 
G 1 68  SER 68  68  68  SER SER G . n 
G 1 69  ARG 69  69  69  ARG ARG G . n 
G 1 70  LYS 70  70  70  LYS LYS G . n 
G 1 71  HIS 71  71  71  HIS HIS G . n 
G 1 72  GLY 72  72  72  GLY GLY G . n 
G 1 73  GLY 73  73  73  GLY GLY G . n 
G 1 74  PRO 74  74  74  PRO PRO G . n 
G 1 75  LYS 75  75  75  LYS LYS G . n 
G 1 76  ASP 76  76  76  ASP ASP G . n 
G 1 77  GLU 77  77  77  GLU GLU G . n 
G 1 78  GLU 78  78  78  GLU GLU G . n 
G 1 79  ARG 79  79  79  ARG ARG G . n 
G 1 80  HIS 80  80  80  HIS HIS G . n 
G 1 81  VAL 81  81  81  VAL VAL G . n 
G 1 82  GLY 82  82  82  GLY GLY G . n 
G 1 83  ASP 83  83  83  ASP ASP G . n 
G 1 84  LEU 84  84  84  LEU LEU G . n 
G 1 85  GLY 85  85  85  GLY GLY G . n 
G 1 86  ASN 86  86  86  ASN ASN G . n 
G 1 87  VAL 87  87  87  VAL VAL G . n 
G 1 88  THR 88  88  88  THR THR G . n 
G 1 89  ALA 89  89  89  ALA ALA G . n 
G 1 90  ASP 90  90  90  ASP ASP G . n 
G 1 91  LYS 91  91  91  LYS LYS G . n 
G 1 92  ASP 92  92  92  ASP ASP G . n 
G 1 93  GLY 93  93  93  GLY GLY G . n 
G 1 94  VAL 94  94  94  VAL VAL G . n 
G 1 95  ALA 95  95  95  ALA ALA G . n 
G 1 96  ASP 96  96  96  ASP ASP G . n 
G 1 97  VAL 97  97  97  VAL VAL G . n 
G 1 98  SER 98  98  98  SER SER G . n 
G 1 99  ILE 99  99  99  ILE ILE G . n 
G 1 100 GLU 100 100 100 GLU GLU G . n 
G 1 101 ASP 101 101 101 ASP ASP G . n 
G 1 102 SER 102 102 102 SER SER G . n 
G 1 103 VAL 103 103 103 VAL VAL G . n 
G 1 104 ILE 104 104 104 ILE ILE G . n 
G 1 105 SER 105 105 105 SER SER G . n 
G 1 106 LEU 106 106 106 LEU LEU G . n 
G 1 107 SER 107 107 107 SER SER G . n 
G 1 108 GLY 108 108 108 GLY GLY G . n 
G 1 109 ASP 109 109 109 ASP ASP G . n 
G 1 110 HIS 110 110 110 HIS HIS G . n 
G 1 111 CYS 111 111 111 CYS CYS G . n 
G 1 112 ILE 112 112 112 ILE ILE G . n 
G 1 113 ILE 113 113 113 ILE ILE G . n 
G 1 114 GLY 114 114 114 GLY GLY G . n 
G 1 115 ARG 115 115 115 ARG ARG G . n 
G 1 116 THR 116 116 116 THR THR G . n 
G 1 117 LEU 117 117 117 LEU LEU G . n 
G 1 118 VAL 118 118 118 VAL VAL G . n 
G 1 119 VAL 119 119 119 VAL VAL G . n 
G 1 120 HIS 120 120 120 HIS HIS G . n 
G 1 121 GLU 121 121 121 GLU GLU G . n 
G 1 122 LYS 122 122 122 LYS LYS G . n 
G 1 123 ALA 123 123 123 ALA ALA G . n 
G 1 124 ASP 124 124 124 ASP ASP G . n 
G 1 125 ASP 125 125 125 ASP ASP G . n 
G 1 126 LEU 126 126 126 LEU LEU G . n 
G 1 127 GLY 127 127 127 GLY GLY G . n 
G 1 128 LYS 128 128 128 LYS LYS G . n 
G 1 129 GLY 129 129 129 GLY GLY G . n 
G 1 130 GLY 130 130 130 GLY GLY G . n 
G 1 131 ASN 131 131 131 ASN ASN G . n 
G 1 132 GLU 132 132 132 GLU GLU G . n 
G 1 133 GLU 133 133 133 GLU GLU G . n 
G 1 134 SER 134 134 134 SER SER G . n 
G 1 135 THR 135 135 135 THR THR G . n 
G 1 136 LYS 136 136 136 LYS LYS G . n 
G 1 137 THR 137 137 137 THR THR G . n 
G 1 138 GLY 138 138 138 GLY GLY G . n 
G 1 139 ASN 139 139 139 ASN ASN G . n 
G 1 140 ALA 140 140 140 ALA ALA G . n 
G 1 141 GLY 141 141 141 GLY GLY G . n 
G 1 142 SER 142 142 142 SER SER G . n 
G 1 143 ARG 143 143 143 ARG ARG G . n 
G 1 144 LEU 144 144 144 LEU LEU G . n 
G 1 145 ALA 145 145 145 ALA ALA G . n 
G 1 146 CYS 146 146 146 CYS CYS G . n 
G 1 147 GLY 147 147 147 GLY GLY G . n 
G 1 148 VAL 148 148 148 VAL VAL G . n 
G 1 149 ILE 149 149 149 ILE ILE G . n 
G 1 150 GLY 150 150 150 GLY GLY G . n 
G 1 151 ILE 151 151 151 ILE ILE G . n 
G 1 152 ALA 152 152 152 ALA ALA G . n 
G 1 153 GLN 153 153 153 GLN GLN G . n 
H 1 1   ALA 1   1   1   ALA ALA H . n 
H 1 2   THR 2   2   2   THR THR H . n 
H 1 3   LYS 3   3   3   LYS LYS H . n 
H 1 4   ALA 4   4   4   ALA ALA H . n 
H 1 5   VAL 5   5   5   VAL VAL H . n 
H 1 6   CYS 6   6   6   CYS CYS H . n 
H 1 7   VAL 7   7   7   VAL VAL H . n 
H 1 8   LEU 8   8   8   LEU LEU H . n 
H 1 9   LYS 9   9   9   LYS LYS H . n 
H 1 10  GLY 10  10  10  GLY GLY H . n 
H 1 11  ASP 11  11  11  ASP ASP H . n 
H 1 12  GLY 12  12  12  GLY GLY H . n 
H 1 13  PRO 13  13  13  PRO PRO H . n 
H 1 14  VAL 14  14  14  VAL VAL H . n 
H 1 15  GLN 15  15  15  GLN GLN H . n 
H 1 16  GLY 16  16  16  GLY GLY H . n 
H 1 17  ILE 17  17  17  ILE ILE H . n 
H 1 18  ILE 18  18  18  ILE ILE H . n 
H 1 19  ASN 19  19  19  ASN ASN H . n 
H 1 20  PHE 20  20  20  PHE PHE H . n 
H 1 21  GLU 21  21  21  GLU GLU H . n 
H 1 22  GLN 22  22  22  GLN GLN H . n 
H 1 23  LYS 23  23  23  LYS LYS H . n 
H 1 24  GLU 24  24  24  GLU GLU H . n 
H 1 25  SER 25  25  25  SER SER H . n 
H 1 26  ASN 26  26  26  ASN ASN H . n 
H 1 27  GLY 27  27  27  GLY GLY H . n 
H 1 28  PRO 28  28  28  PRO PRO H . n 
H 1 29  VAL 29  29  29  VAL VAL H . n 
H 1 30  LYS 30  30  30  LYS LYS H . n 
H 1 31  VAL 31  31  31  VAL VAL H . n 
H 1 32  TRP 32  32  32  TRP TRP H . n 
H 1 33  GLY 33  33  33  GLY GLY H . n 
H 1 34  SER 34  34  34  SER SER H . n 
H 1 35  ILE 35  35  35  ILE ILE H . n 
H 1 36  LYS 36  36  36  LYS LYS H . n 
H 1 37  GLY 37  37  37  GLY GLY H . n 
H 1 38  LEU 38  38  38  LEU LEU H . n 
H 1 39  THR 39  39  39  THR THR H . n 
H 1 40  GLU 40  40  40  GLU GLU H . n 
H 1 41  GLY 41  41  41  GLY GLY H . n 
H 1 42  LEU 42  42  42  LEU LEU H . n 
H 1 43  HIS 43  43  43  HIS HIS H . n 
H 1 44  GLY 44  44  44  GLY GLY H . n 
H 1 45  PHE 45  45  45  PHE PHE H . n 
H 1 46  HIS 46  46  46  HIS HIS H . n 
H 1 47  VAL 47  47  47  VAL VAL H . n 
H 1 48  HIS 48  48  48  HIS HIS H . n 
H 1 49  GLU 49  49  49  GLU GLU H . n 
H 1 50  PHE 50  50  50  PHE PHE H . n 
H 1 51  GLY 51  51  51  GLY GLY H . n 
H 1 52  ASP 52  52  52  ASP ASP H . n 
H 1 53  ASN 53  53  53  ASN ASN H . n 
H 1 54  THR 54  54  54  THR THR H . n 
H 1 55  ALA 55  55  55  ALA ALA H . n 
H 1 56  GLY 56  56  56  GLY GLY H . n 
H 1 57  CYS 57  57  57  CYS CYS H . n 
H 1 58  THR 58  58  58  THR THR H . n 
H 1 59  SER 59  59  59  SER SER H . n 
H 1 60  ALA 60  60  60  ALA ALA H . n 
H 1 61  GLY 61  61  61  GLY GLY H . n 
H 1 62  PRO 62  62  62  PRO PRO H . n 
H 1 63  HIS 63  63  63  HIS HIS H . n 
H 1 64  PHE 64  64  64  PHE PHE H . n 
H 1 65  ASN 65  65  65  ASN ASN H . n 
H 1 66  PRO 66  66  66  PRO PRO H . n 
H 1 67  LEU 67  67  67  LEU LEU H . n 
H 1 68  SER 68  68  68  SER SER H . n 
H 1 69  ARG 69  69  69  ARG ARG H . n 
H 1 70  LYS 70  70  70  LYS LYS H . n 
H 1 71  HIS 71  71  71  HIS HIS H . n 
H 1 72  GLY 72  72  72  GLY GLY H . n 
H 1 73  GLY 73  73  73  GLY GLY H . n 
H 1 74  PRO 74  74  74  PRO PRO H . n 
H 1 75  LYS 75  75  75  LYS LYS H . n 
H 1 76  ASP 76  76  76  ASP ASP H . n 
H 1 77  GLU 77  77  77  GLU GLU H . n 
H 1 78  GLU 78  78  78  GLU GLU H . n 
H 1 79  ARG 79  79  79  ARG ARG H . n 
H 1 80  HIS 80  80  80  HIS HIS H . n 
H 1 81  VAL 81  81  81  VAL VAL H . n 
H 1 82  GLY 82  82  82  GLY GLY H . n 
H 1 83  ASP 83  83  83  ASP ASP H . n 
H 1 84  LEU 84  84  84  LEU LEU H . n 
H 1 85  GLY 85  85  85  GLY GLY H . n 
H 1 86  ASN 86  86  86  ASN ASN H . n 
H 1 87  VAL 87  87  87  VAL VAL H . n 
H 1 88  THR 88  88  88  THR THR H . n 
H 1 89  ALA 89  89  89  ALA ALA H . n 
H 1 90  ASP 90  90  90  ASP ASP H . n 
H 1 91  LYS 91  91  91  LYS LYS H . n 
H 1 92  ASP 92  92  92  ASP ASP H . n 
H 1 93  GLY 93  93  93  GLY GLY H . n 
H 1 94  VAL 94  94  94  VAL VAL H . n 
H 1 95  ALA 95  95  95  ALA ALA H . n 
H 1 96  ASP 96  96  96  ASP ASP H . n 
H 1 97  VAL 97  97  97  VAL VAL H . n 
H 1 98  SER 98  98  98  SER SER H . n 
H 1 99  ILE 99  99  99  ILE ILE H . n 
H 1 100 GLU 100 100 100 GLU GLU H . n 
H 1 101 ASP 101 101 101 ASP ASP H . n 
H 1 102 SER 102 102 102 SER SER H . n 
H 1 103 VAL 103 103 103 VAL VAL H . n 
H 1 104 ILE 104 104 104 ILE ILE H . n 
H 1 105 SER 105 105 105 SER SER H . n 
H 1 106 LEU 106 106 106 LEU LEU H . n 
H 1 107 SER 107 107 107 SER SER H . n 
H 1 108 GLY 108 108 108 GLY GLY H . n 
H 1 109 ASP 109 109 109 ASP ASP H . n 
H 1 110 HIS 110 110 110 HIS HIS H . n 
H 1 111 CYS 111 111 111 CYS CYS H . n 
H 1 112 ILE 112 112 112 ILE ILE H . n 
H 1 113 ILE 113 113 113 ILE ILE H . n 
H 1 114 GLY 114 114 114 GLY GLY H . n 
H 1 115 ARG 115 115 115 ARG ARG H . n 
H 1 116 THR 116 116 116 THR THR H . n 
H 1 117 LEU 117 117 117 LEU LEU H . n 
H 1 118 VAL 118 118 118 VAL VAL H . n 
H 1 119 VAL 119 119 119 VAL VAL H . n 
H 1 120 HIS 120 120 120 HIS HIS H . n 
H 1 121 GLU 121 121 121 GLU GLU H . n 
H 1 122 LYS 122 122 122 LYS LYS H . n 
H 1 123 ALA 123 123 123 ALA ALA H . n 
H 1 124 ASP 124 124 124 ASP ASP H . n 
H 1 125 ASP 125 125 125 ASP ASP H . n 
H 1 126 LEU 126 126 126 LEU LEU H . n 
H 1 127 GLY 127 127 127 GLY GLY H . n 
H 1 128 LYS 128 128 128 LYS LYS H . n 
H 1 129 GLY 129 129 129 GLY GLY H . n 
H 1 130 GLY 130 130 130 GLY GLY H . n 
H 1 131 ASN 131 131 131 ASN ASN H . n 
H 1 132 GLU 132 132 132 GLU GLU H . n 
H 1 133 GLU 133 133 133 GLU GLU H . n 
H 1 134 SER 134 134 134 SER SER H . n 
H 1 135 THR 135 135 135 THR THR H . n 
H 1 136 LYS 136 136 136 LYS LYS H . n 
H 1 137 THR 137 137 137 THR THR H . n 
H 1 138 GLY 138 138 138 GLY GLY H . n 
H 1 139 ASN 139 139 139 ASN ASN H . n 
H 1 140 ALA 140 140 140 ALA ALA H . n 
H 1 141 GLY 141 141 141 GLY GLY H . n 
H 1 142 SER 142 142 142 SER SER H . n 
H 1 143 ARG 143 143 143 ARG ARG H . n 
H 1 144 LEU 144 144 144 LEU LEU H . n 
H 1 145 ALA 145 145 145 ALA ALA H . n 
H 1 146 CYS 146 146 146 CYS CYS H . n 
H 1 147 GLY 147 147 147 GLY GLY H . n 
H 1 148 VAL 148 148 148 VAL VAL H . n 
H 1 149 ILE 149 149 149 ILE ILE H . n 
H 1 150 GLY 150 150 150 GLY GLY H . n 
H 1 151 ILE 151 151 151 ILE ILE H . n 
H 1 152 ALA 152 152 152 ALA ALA H . n 
H 1 153 GLN 153 153 153 GLN GLN H . n 
I 1 1   ALA 1   1   1   ALA ALA I . n 
I 1 2   THR 2   2   2   THR THR I . n 
I 1 3   LYS 3   3   3   LYS LYS I . n 
I 1 4   ALA 4   4   4   ALA ALA I . n 
I 1 5   VAL 5   5   5   VAL VAL I . n 
I 1 6   CYS 6   6   6   CYS CYS I . n 
I 1 7   VAL 7   7   7   VAL VAL I . n 
I 1 8   LEU 8   8   8   LEU LEU I . n 
I 1 9   LYS 9   9   9   LYS LYS I . n 
I 1 10  GLY 10  10  10  GLY GLY I . n 
I 1 11  ASP 11  11  11  ASP ASP I . n 
I 1 12  GLY 12  12  12  GLY GLY I . n 
I 1 13  PRO 13  13  13  PRO PRO I . n 
I 1 14  VAL 14  14  14  VAL VAL I . n 
I 1 15  GLN 15  15  15  GLN GLN I . n 
I 1 16  GLY 16  16  16  GLY GLY I . n 
I 1 17  ILE 17  17  17  ILE ILE I . n 
I 1 18  ILE 18  18  18  ILE ILE I . n 
I 1 19  ASN 19  19  19  ASN ASN I . n 
I 1 20  PHE 20  20  20  PHE PHE I . n 
I 1 21  GLU 21  21  21  GLU GLU I . n 
I 1 22  GLN 22  22  22  GLN GLN I . n 
I 1 23  LYS 23  23  23  LYS LYS I . n 
I 1 24  GLU 24  24  24  GLU GLU I . n 
I 1 25  SER 25  25  25  SER SER I . n 
I 1 26  ASN 26  26  26  ASN ASN I . n 
I 1 27  GLY 27  27  27  GLY GLY I . n 
I 1 28  PRO 28  28  28  PRO PRO I . n 
I 1 29  VAL 29  29  29  VAL VAL I . n 
I 1 30  LYS 30  30  30  LYS LYS I . n 
I 1 31  VAL 31  31  31  VAL VAL I . n 
I 1 32  TRP 32  32  32  TRP TRP I . n 
I 1 33  GLY 33  33  33  GLY GLY I . n 
I 1 34  SER 34  34  34  SER SER I . n 
I 1 35  ILE 35  35  35  ILE ILE I . n 
I 1 36  LYS 36  36  36  LYS LYS I . n 
I 1 37  GLY 37  37  37  GLY GLY I . n 
I 1 38  LEU 38  38  38  LEU LEU I . n 
I 1 39  THR 39  39  39  THR THR I . n 
I 1 40  GLU 40  40  40  GLU GLU I . n 
I 1 41  GLY 41  41  41  GLY GLY I . n 
I 1 42  LEU 42  42  42  LEU LEU I . n 
I 1 43  HIS 43  43  43  HIS HIS I . n 
I 1 44  GLY 44  44  44  GLY GLY I . n 
I 1 45  PHE 45  45  45  PHE PHE I . n 
I 1 46  HIS 46  46  46  HIS HIS I . n 
I 1 47  VAL 47  47  47  VAL VAL I . n 
I 1 48  HIS 48  48  48  HIS HIS I . n 
I 1 49  GLU 49  49  49  GLU GLU I . n 
I 1 50  PHE 50  50  50  PHE PHE I . n 
I 1 51  GLY 51  51  51  GLY GLY I . n 
I 1 52  ASP 52  52  52  ASP ASP I . n 
I 1 53  ASN 53  53  53  ASN ASN I . n 
I 1 54  THR 54  54  54  THR THR I . n 
I 1 55  ALA 55  55  55  ALA ALA I . n 
I 1 56  GLY 56  56  56  GLY GLY I . n 
I 1 57  CYS 57  57  57  CYS CYS I . n 
I 1 58  THR 58  58  58  THR THR I . n 
I 1 59  SER 59  59  59  SER SER I . n 
I 1 60  ALA 60  60  60  ALA ALA I . n 
I 1 61  GLY 61  61  61  GLY GLY I . n 
I 1 62  PRO 62  62  62  PRO PRO I . n 
I 1 63  HIS 63  63  63  HIS HIS I . n 
I 1 64  PHE 64  64  64  PHE PHE I . n 
I 1 65  ASN 65  65  65  ASN ASN I . n 
I 1 66  PRO 66  66  66  PRO PRO I . n 
I 1 67  LEU 67  67  67  LEU LEU I . n 
I 1 68  SER 68  68  68  SER SER I . n 
I 1 69  ARG 69  69  69  ARG ARG I . n 
I 1 70  LYS 70  70  70  LYS LYS I . n 
I 1 71  HIS 71  71  71  HIS HIS I . n 
I 1 72  GLY 72  72  72  GLY GLY I . n 
I 1 73  GLY 73  73  73  GLY GLY I . n 
I 1 74  PRO 74  74  74  PRO PRO I . n 
I 1 75  LYS 75  75  75  LYS LYS I . n 
I 1 76  ASP 76  76  76  ASP ASP I . n 
I 1 77  GLU 77  77  77  GLU GLU I . n 
I 1 78  GLU 78  78  78  GLU GLU I . n 
I 1 79  ARG 79  79  79  ARG ARG I . n 
I 1 80  HIS 80  80  80  HIS HIS I . n 
I 1 81  VAL 81  81  81  VAL VAL I . n 
I 1 82  GLY 82  82  82  GLY GLY I . n 
I 1 83  ASP 83  83  83  ASP ASP I . n 
I 1 84  LEU 84  84  84  LEU LEU I . n 
I 1 85  GLY 85  85  85  GLY GLY I . n 
I 1 86  ASN 86  86  86  ASN ASN I . n 
I 1 87  VAL 87  87  87  VAL VAL I . n 
I 1 88  THR 88  88  88  THR THR I . n 
I 1 89  ALA 89  89  89  ALA ALA I . n 
I 1 90  ASP 90  90  90  ASP ASP I . n 
I 1 91  LYS 91  91  91  LYS LYS I . n 
I 1 92  ASP 92  92  92  ASP ASP I . n 
I 1 93  GLY 93  93  93  GLY GLY I . n 
I 1 94  VAL 94  94  94  VAL VAL I . n 
I 1 95  ALA 95  95  95  ALA ALA I . n 
I 1 96  ASP 96  96  96  ASP ASP I . n 
I 1 97  VAL 97  97  97  VAL VAL I . n 
I 1 98  SER 98  98  98  SER SER I . n 
I 1 99  ILE 99  99  99  ILE ILE I . n 
I 1 100 GLU 100 100 100 GLU GLU I . n 
I 1 101 ASP 101 101 101 ASP ASP I . n 
I 1 102 SER 102 102 102 SER SER I . n 
I 1 103 VAL 103 103 103 VAL VAL I . n 
I 1 104 ILE 104 104 104 ILE ILE I . n 
I 1 105 SER 105 105 105 SER SER I . n 
I 1 106 LEU 106 106 106 LEU LEU I . n 
I 1 107 SER 107 107 107 SER SER I . n 
I 1 108 GLY 108 108 108 GLY GLY I . n 
I 1 109 ASP 109 109 109 ASP ASP I . n 
I 1 110 HIS 110 110 110 HIS HIS I . n 
I 1 111 CYS 111 111 111 CYS CYS I . n 
I 1 112 ILE 112 112 112 ILE ILE I . n 
I 1 113 ILE 113 113 113 ILE ILE I . n 
I 1 114 GLY 114 114 114 GLY GLY I . n 
I 1 115 ARG 115 115 115 ARG ARG I . n 
I 1 116 THR 116 116 116 THR THR I . n 
I 1 117 LEU 117 117 117 LEU LEU I . n 
I 1 118 VAL 118 118 118 VAL VAL I . n 
I 1 119 VAL 119 119 119 VAL VAL I . n 
I 1 120 HIS 120 120 120 HIS HIS I . n 
I 1 121 GLU 121 121 121 GLU GLU I . n 
I 1 122 LYS 122 122 122 LYS LYS I . n 
I 1 123 ALA 123 123 123 ALA ALA I . n 
I 1 124 ASP 124 124 124 ASP ASP I . n 
I 1 125 ASP 125 125 125 ASP ASP I . n 
I 1 126 LEU 126 126 126 LEU LEU I . n 
I 1 127 GLY 127 127 127 GLY GLY I . n 
I 1 128 LYS 128 128 128 LYS LYS I . n 
I 1 129 GLY 129 129 129 GLY GLY I . n 
I 1 130 GLY 130 130 130 GLY GLY I . n 
I 1 131 ASN 131 131 131 ASN ASN I . n 
I 1 132 GLU 132 132 132 GLU GLU I . n 
I 1 133 GLU 133 133 133 GLU GLU I . n 
I 1 134 SER 134 134 134 SER SER I . n 
I 1 135 THR 135 135 135 THR THR I . n 
I 1 136 LYS 136 136 136 LYS LYS I . n 
I 1 137 THR 137 137 137 THR THR I . n 
I 1 138 GLY 138 138 138 GLY GLY I . n 
I 1 139 ASN 139 139 139 ASN ASN I . n 
I 1 140 ALA 140 140 140 ALA ALA I . n 
I 1 141 GLY 141 141 141 GLY GLY I . n 
I 1 142 SER 142 142 142 SER SER I . n 
I 1 143 ARG 143 143 143 ARG ARG I . n 
I 1 144 LEU 144 144 144 LEU LEU I . n 
I 1 145 ALA 145 145 145 ALA ALA I . n 
I 1 146 CYS 146 146 146 CYS CYS I . n 
I 1 147 GLY 147 147 147 GLY GLY I . n 
I 1 148 VAL 148 148 148 VAL VAL I . n 
I 1 149 ILE 149 149 149 ILE ILE I . n 
I 1 150 GLY 150 150 150 GLY GLY I . n 
I 1 151 ILE 151 151 151 ILE ILE I . n 
I 1 152 ALA 152 152 152 ALA ALA I . n 
I 1 153 GLN 153 153 153 GLN GLN I . n 
J 1 1   ALA 1   1   1   ALA ALA J . n 
J 1 2   THR 2   2   2   THR THR J . n 
J 1 3   LYS 3   3   3   LYS LYS J . n 
J 1 4   ALA 4   4   4   ALA ALA J . n 
J 1 5   VAL 5   5   5   VAL VAL J . n 
J 1 6   CYS 6   6   6   CYS CYS J . n 
J 1 7   VAL 7   7   7   VAL VAL J . n 
J 1 8   LEU 8   8   8   LEU LEU J . n 
J 1 9   LYS 9   9   9   LYS LYS J . n 
J 1 10  GLY 10  10  10  GLY GLY J . n 
J 1 11  ASP 11  11  11  ASP ASP J . n 
J 1 12  GLY 12  12  12  GLY GLY J . n 
J 1 13  PRO 13  13  13  PRO PRO J . n 
J 1 14  VAL 14  14  14  VAL VAL J . n 
J 1 15  GLN 15  15  15  GLN GLN J . n 
J 1 16  GLY 16  16  16  GLY GLY J . n 
J 1 17  ILE 17  17  17  ILE ILE J . n 
J 1 18  ILE 18  18  18  ILE ILE J . n 
J 1 19  ASN 19  19  19  ASN ASN J . n 
J 1 20  PHE 20  20  20  PHE PHE J . n 
J 1 21  GLU 21  21  21  GLU GLU J . n 
J 1 22  GLN 22  22  22  GLN GLN J . n 
J 1 23  LYS 23  23  23  LYS LYS J . n 
J 1 24  GLU 24  24  24  GLU GLU J . n 
J 1 25  SER 25  25  25  SER SER J . n 
J 1 26  ASN 26  26  26  ASN ASN J . n 
J 1 27  GLY 27  27  27  GLY GLY J . n 
J 1 28  PRO 28  28  28  PRO PRO J . n 
J 1 29  VAL 29  29  29  VAL VAL J . n 
J 1 30  LYS 30  30  30  LYS LYS J . n 
J 1 31  VAL 31  31  31  VAL VAL J . n 
J 1 32  TRP 32  32  32  TRP TRP J . n 
J 1 33  GLY 33  33  33  GLY GLY J . n 
J 1 34  SER 34  34  34  SER SER J . n 
J 1 35  ILE 35  35  35  ILE ILE J . n 
J 1 36  LYS 36  36  36  LYS LYS J . n 
J 1 37  GLY 37  37  37  GLY GLY J . n 
J 1 38  LEU 38  38  38  LEU LEU J . n 
J 1 39  THR 39  39  39  THR THR J . n 
J 1 40  GLU 40  40  40  GLU GLU J . n 
J 1 41  GLY 41  41  41  GLY GLY J . n 
J 1 42  LEU 42  42  42  LEU LEU J . n 
J 1 43  HIS 43  43  43  HIS HIS J . n 
J 1 44  GLY 44  44  44  GLY GLY J . n 
J 1 45  PHE 45  45  45  PHE PHE J . n 
J 1 46  HIS 46  46  46  HIS HIS J . n 
J 1 47  VAL 47  47  47  VAL VAL J . n 
J 1 48  HIS 48  48  48  HIS HIS J . n 
J 1 49  GLU 49  49  49  GLU GLU J . n 
J 1 50  PHE 50  50  50  PHE PHE J . n 
J 1 51  GLY 51  51  51  GLY GLY J . n 
J 1 52  ASP 52  52  52  ASP ASP J . n 
J 1 53  ASN 53  53  53  ASN ASN J . n 
J 1 54  THR 54  54  54  THR THR J . n 
J 1 55  ALA 55  55  55  ALA ALA J . n 
J 1 56  GLY 56  56  56  GLY GLY J . n 
J 1 57  CYS 57  57  57  CYS CYS J . n 
J 1 58  THR 58  58  58  THR THR J . n 
J 1 59  SER 59  59  59  SER SER J . n 
J 1 60  ALA 60  60  60  ALA ALA J . n 
J 1 61  GLY 61  61  61  GLY GLY J . n 
J 1 62  PRO 62  62  62  PRO PRO J . n 
J 1 63  HIS 63  63  63  HIS HIS J . n 
J 1 64  PHE 64  64  64  PHE PHE J . n 
J 1 65  ASN 65  65  65  ASN ASN J . n 
J 1 66  PRO 66  66  66  PRO PRO J . n 
J 1 67  LEU 67  67  67  LEU LEU J . n 
J 1 68  SER 68  68  68  SER SER J . n 
J 1 69  ARG 69  69  69  ARG ARG J . n 
J 1 70  LYS 70  70  70  LYS LYS J . n 
J 1 71  HIS 71  71  71  HIS HIS J . n 
J 1 72  GLY 72  72  72  GLY GLY J . n 
J 1 73  GLY 73  73  73  GLY GLY J . n 
J 1 74  PRO 74  74  74  PRO PRO J . n 
J 1 75  LYS 75  75  75  LYS LYS J . n 
J 1 76  ASP 76  76  76  ASP ASP J . n 
J 1 77  GLU 77  77  77  GLU GLU J . n 
J 1 78  GLU 78  78  78  GLU GLU J . n 
J 1 79  ARG 79  79  79  ARG ARG J . n 
J 1 80  HIS 80  80  80  HIS HIS J . n 
J 1 81  VAL 81  81  81  VAL VAL J . n 
J 1 82  GLY 82  82  82  GLY GLY J . n 
J 1 83  ASP 83  83  83  ASP ASP J . n 
J 1 84  LEU 84  84  84  LEU LEU J . n 
J 1 85  GLY 85  85  85  GLY GLY J . n 
J 1 86  ASN 86  86  86  ASN ASN J . n 
J 1 87  VAL 87  87  87  VAL VAL J . n 
J 1 88  THR 88  88  88  THR THR J . n 
J 1 89  ALA 89  89  89  ALA ALA J . n 
J 1 90  ASP 90  90  90  ASP ASP J . n 
J 1 91  LYS 91  91  91  LYS LYS J . n 
J 1 92  ASP 92  92  92  ASP ASP J . n 
J 1 93  GLY 93  93  93  GLY GLY J . n 
J 1 94  VAL 94  94  94  VAL VAL J . n 
J 1 95  ALA 95  95  95  ALA ALA J . n 
J 1 96  ASP 96  96  96  ASP ASP J . n 
J 1 97  VAL 97  97  97  VAL VAL J . n 
J 1 98  SER 98  98  98  SER SER J . n 
J 1 99  ILE 99  99  99  ILE ILE J . n 
J 1 100 GLU 100 100 100 GLU GLU J . n 
J 1 101 ASP 101 101 101 ASP ASP J . n 
J 1 102 SER 102 102 102 SER SER J . n 
J 1 103 VAL 103 103 103 VAL VAL J . n 
J 1 104 ILE 104 104 104 ILE ILE J . n 
J 1 105 SER 105 105 105 SER SER J . n 
J 1 106 LEU 106 106 106 LEU LEU J . n 
J 1 107 SER 107 107 107 SER SER J . n 
J 1 108 GLY 108 108 108 GLY GLY J . n 
J 1 109 ASP 109 109 109 ASP ASP J . n 
J 1 110 HIS 110 110 110 HIS HIS J . n 
J 1 111 CYS 111 111 111 CYS CYS J . n 
J 1 112 ILE 112 112 112 ILE ILE J . n 
J 1 113 ILE 113 113 113 ILE ILE J . n 
J 1 114 GLY 114 114 114 GLY GLY J . n 
J 1 115 ARG 115 115 115 ARG ARG J . n 
J 1 116 THR 116 116 116 THR THR J . n 
J 1 117 LEU 117 117 117 LEU LEU J . n 
J 1 118 VAL 118 118 118 VAL VAL J . n 
J 1 119 VAL 119 119 119 VAL VAL J . n 
J 1 120 HIS 120 120 120 HIS HIS J . n 
J 1 121 GLU 121 121 121 GLU GLU J . n 
J 1 122 LYS 122 122 122 LYS LYS J . n 
J 1 123 ALA 123 123 123 ALA ALA J . n 
J 1 124 ASP 124 124 124 ASP ASP J . n 
J 1 125 ASP 125 125 125 ASP ASP J . n 
J 1 126 LEU 126 126 126 LEU LEU J . n 
J 1 127 GLY 127 127 127 GLY GLY J . n 
J 1 128 LYS 128 128 128 LYS LYS J . n 
J 1 129 GLY 129 129 129 GLY GLY J . n 
J 1 130 GLY 130 130 130 GLY GLY J . n 
J 1 131 ASN 131 131 131 ASN ASN J . n 
J 1 132 GLU 132 132 132 GLU GLU J . n 
J 1 133 GLU 133 133 133 GLU GLU J . n 
J 1 134 SER 134 134 134 SER SER J . n 
J 1 135 THR 135 135 135 THR THR J . n 
J 1 136 LYS 136 136 136 LYS LYS J . n 
J 1 137 THR 137 137 137 THR THR J . n 
J 1 138 GLY 138 138 138 GLY GLY J . n 
J 1 139 ASN 139 139 139 ASN ASN J . n 
J 1 140 ALA 140 140 140 ALA ALA J . n 
J 1 141 GLY 141 141 141 GLY GLY J . n 
J 1 142 SER 142 142 142 SER SER J . n 
J 1 143 ARG 143 143 143 ARG ARG J . n 
J 1 144 LEU 144 144 144 LEU LEU J . n 
J 1 145 ALA 145 145 145 ALA ALA J . n 
J 1 146 CYS 146 146 146 CYS CYS J . n 
J 1 147 GLY 147 147 147 GLY GLY J . n 
J 1 148 VAL 148 148 148 VAL VAL J . n 
J 1 149 ILE 149 149 149 ILE ILE J . n 
J 1 150 GLY 150 150 150 GLY GLY J . n 
J 1 151 ILE 151 151 151 ILE ILE J . n 
J 1 152 ALA 152 152 152 ALA ALA J . n 
J 1 153 GLN 153 153 153 GLN GLN J . n 
# 
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 
K  2 CU1 1   200  200  CU1 CU1 A . 
L  3 ZN  1   201  201  ZN  ZN2 A . 
M  2 CU1 1   200  200  CU1 CU1 B . 
N  3 ZN  1   201  201  ZN  ZN2 B . 
O  4 SO4 1   300  300  SO4 SO4 B . 
P  2 CU1 1   200  200  CU1 CU1 C . 
Q  3 ZN  1   201  201  ZN  ZN2 C . 
R  2 CU1 1   200  200  CU1 CU1 D . 
S  3 ZN  1   201  201  ZN  ZN2 D . 
T  2 CU1 1   200  200  CU1 CU1 E . 
U  3 ZN  1   201  201  ZN  ZN2 E . 
V  2 CU1 1   200  200  CU1 CU1 F . 
W  3 ZN  1   201  201  ZN  ZN2 F . 
X  2 CU1 1   200  200  CU1 CU1 G . 
Y  3 ZN  1   201  201  ZN  ZN2 G . 
Z  2 CU1 1   200  200  CU1 CU1 H . 
AA 3 ZN  1   201  201  ZN  ZN2 H . 
BA 2 CU1 1   200  200  CU1 CU1 I . 
CA 3 ZN  1   201  201  ZN  ZN2 I . 
DA 2 CU1 1   200  200  CU1 CU1 J . 
EA 3 ZN  1   201  201  ZN  ZN2 J . 
FA 4 SO4 1   301  301  SO4 SO4 J . 
GA 4 SO4 1   302  302  SO4 SO4 J . 
HA 5 HOH 1   400  400  HOH HOH A . 
HA 5 HOH 2   409  409  HOH HOH A . 
HA 5 HOH 3   419  419  HOH HOH A . 
HA 5 HOH 4   452  452  HOH HOH A . 
HA 5 HOH 5   453  453  HOH HOH A . 
HA 5 HOH 6   456  456  HOH HOH A . 
HA 5 HOH 7   460  460  HOH HOH A . 
HA 5 HOH 8   462  462  HOH HOH A . 
HA 5 HOH 9   464  464  HOH HOH A . 
HA 5 HOH 10  470  470  HOH HOH A . 
HA 5 HOH 11  501  501  HOH HOH A . 
HA 5 HOH 12  511  511  HOH HOH A . 
HA 5 HOH 13  526  526  HOH HOH A . 
HA 5 HOH 14  534  534  HOH HOH A . 
HA 5 HOH 15  543  543  HOH HOH A . 
HA 5 HOH 16  550  550  HOH HOH A . 
HA 5 HOH 17  577  577  HOH HOH A . 
HA 5 HOH 18  579  579  HOH HOH A . 
HA 5 HOH 19  585  585  HOH HOH A . 
HA 5 HOH 20  587  587  HOH HOH A . 
HA 5 HOH 21  588  588  HOH HOH A . 
HA 5 HOH 22  602  602  HOH HOH A . 
HA 5 HOH 23  607  607  HOH HOH A . 
HA 5 HOH 24  609  609  HOH HOH A . 
HA 5 HOH 25  611  611  HOH HOH A . 
HA 5 HOH 26  617  617  HOH HOH A . 
HA 5 HOH 27  621  621  HOH HOH A . 
HA 5 HOH 28  632  632  HOH HOH A . 
HA 5 HOH 29  638  638  HOH HOH A . 
HA 5 HOH 30  653  653  HOH HOH A . 
HA 5 HOH 31  655  655  HOH HOH A . 
HA 5 HOH 32  662  662  HOH HOH A . 
HA 5 HOH 33  679  679  HOH HOH A . 
HA 5 HOH 34  697  697  HOH HOH A . 
HA 5 HOH 35  702  702  HOH HOH A . 
HA 5 HOH 36  706  706  HOH HOH A . 
HA 5 HOH 37  710  710  HOH HOH A . 
HA 5 HOH 38  730  730  HOH HOH A . 
HA 5 HOH 39  731  731  HOH HOH A . 
HA 5 HOH 40  736  736  HOH HOH A . 
HA 5 HOH 41  762  762  HOH HOH A . 
HA 5 HOH 42  763  763  HOH HOH A . 
HA 5 HOH 43  779  779  HOH HOH A . 
HA 5 HOH 44  787  787  HOH HOH A . 
HA 5 HOH 45  816  816  HOH HOH A . 
HA 5 HOH 46  832  832  HOH HOH A . 
HA 5 HOH 47  845  845  HOH HOH A . 
HA 5 HOH 48  853  853  HOH HOH A . 
HA 5 HOH 49  858  858  HOH HOH A . 
HA 5 HOH 50  861  861  HOH HOH A . 
HA 5 HOH 51  863  863  HOH HOH A . 
HA 5 HOH 52  864  864  HOH HOH A . 
HA 5 HOH 53  877  877  HOH HOH A . 
HA 5 HOH 54  878  878  HOH HOH A . 
HA 5 HOH 55  880  880  HOH HOH A . 
HA 5 HOH 56  881  881  HOH HOH A . 
HA 5 HOH 57  882  882  HOH HOH A . 
HA 5 HOH 58  884  884  HOH HOH A . 
HA 5 HOH 59  885  885  HOH HOH A . 
HA 5 HOH 60  886  886  HOH HOH A . 
HA 5 HOH 61  887  887  HOH HOH A . 
HA 5 HOH 62  895  895  HOH HOH A . 
HA 5 HOH 63  896  896  HOH HOH A . 
HA 5 HOH 64  897  897  HOH HOH A . 
HA 5 HOH 65  898  898  HOH HOH A . 
HA 5 HOH 66  899  899  HOH HOH A . 
HA 5 HOH 67  901  901  HOH HOH A . 
HA 5 HOH 68  903  903  HOH HOH A . 
HA 5 HOH 69  904  904  HOH HOH A . 
HA 5 HOH 70  909  909  HOH HOH A . 
HA 5 HOH 71  911  911  HOH HOH A . 
HA 5 HOH 72  912  912  HOH HOH A . 
HA 5 HOH 73  913  913  HOH HOH A . 
HA 5 HOH 74  916  916  HOH HOH A . 
HA 5 HOH 75  917  917  HOH HOH A . 
HA 5 HOH 76  918  918  HOH HOH A . 
HA 5 HOH 77  942  942  HOH HOH A . 
HA 5 HOH 78  943  943  HOH HOH A . 
HA 5 HOH 79  944  944  HOH HOH A . 
HA 5 HOH 80  945  945  HOH HOH A . 
HA 5 HOH 81  946  946  HOH HOH A . 
HA 5 HOH 82  947  947  HOH HOH A . 
HA 5 HOH 83  949  949  HOH HOH A . 
HA 5 HOH 84  950  950  HOH HOH A . 
HA 5 HOH 85  970  970  HOH HOH A . 
HA 5 HOH 86  971  971  HOH HOH A . 
HA 5 HOH 87  972  972  HOH HOH A . 
HA 5 HOH 88  973  973  HOH HOH A . 
HA 5 HOH 89  974  974  HOH HOH A . 
HA 5 HOH 90  976  976  HOH HOH A . 
HA 5 HOH 91  977  977  HOH HOH A . 
HA 5 HOH 92  978  978  HOH HOH A . 
HA 5 HOH 93  979  979  HOH HOH A . 
HA 5 HOH 94  980  980  HOH HOH A . 
HA 5 HOH 95  1084 1084 HOH HOH A . 
HA 5 HOH 96  1139 1139 HOH HOH A . 
HA 5 HOH 97  1150 1150 HOH HOH A . 
HA 5 HOH 98  1153 1153 HOH HOH A . 
HA 5 HOH 99  1260 1260 HOH HOH A . 
HA 5 HOH 100 1265 1265 HOH HOH A . 
HA 5 HOH 101 1285 1285 HOH HOH A . 
HA 5 HOH 102 1290 1290 HOH HOH A . 
HA 5 HOH 103 1291 1291 HOH HOH A . 
HA 5 HOH 104 1311 1311 HOH HOH A . 
HA 5 HOH 105 1317 1317 HOH HOH A . 
HA 5 HOH 106 1321 1321 HOH HOH A . 
HA 5 HOH 107 1323 1323 HOH HOH A . 
HA 5 HOH 108 1326 1326 HOH HOH A . 
HA 5 HOH 109 1333 1333 HOH HOH A . 
HA 5 HOH 110 1336 1336 HOH HOH A . 
HA 5 HOH 111 1342 1342 HOH HOH A . 
HA 5 HOH 112 1343 1343 HOH HOH A . 
HA 5 HOH 113 1362 1362 HOH HOH A . 
HA 5 HOH 114 1364 1364 HOH HOH A . 
HA 5 HOH 115 1365 1365 HOH HOH A . 
HA 5 HOH 116 1378 1378 HOH HOH A . 
HA 5 HOH 117 1382 1382 HOH HOH A . 
HA 5 HOH 118 1392 1392 HOH HOH A . 
HA 5 HOH 119 1408 1408 HOH HOH A . 
HA 5 HOH 120 1426 1426 HOH HOH A . 
HA 5 HOH 121 1434 1434 HOH HOH A . 
HA 5 HOH 122 1445 1445 HOH HOH A . 
HA 5 HOH 123 1458 1458 HOH HOH A . 
HA 5 HOH 124 1462 1462 HOH HOH A . 
HA 5 HOH 125 1466 1466 HOH HOH A . 
HA 5 HOH 126 1475 1475 HOH HOH A . 
HA 5 HOH 127 1476 1476 HOH HOH A . 
HA 5 HOH 128 1477 1477 HOH HOH A . 
HA 5 HOH 129 1478 1478 HOH HOH A . 
HA 5 HOH 130 1544 1544 HOH HOH A . 
HA 5 HOH 131 1565 1565 HOH HOH A . 
IA 5 HOH 1   401  401  HOH HOH B . 
IA 5 HOH 2   410  410  HOH HOH B . 
IA 5 HOH 3   420  420  HOH HOH B . 
IA 5 HOH 4   430  430  HOH HOH B . 
IA 5 HOH 5   445  445  HOH HOH B . 
IA 5 HOH 6   466  466  HOH HOH B . 
IA 5 HOH 7   468  468  HOH HOH B . 
IA 5 HOH 8   472  472  HOH HOH B . 
IA 5 HOH 9   473  473  HOH HOH B . 
IA 5 HOH 10  474  474  HOH HOH B . 
IA 5 HOH 11  476  476  HOH HOH B . 
IA 5 HOH 12  488  488  HOH HOH B . 
IA 5 HOH 13  493  493  HOH HOH B . 
IA 5 HOH 14  495  495  HOH HOH B . 
IA 5 HOH 15  497  497  HOH HOH B . 
IA 5 HOH 16  500  500  HOH HOH B . 
IA 5 HOH 17  503  503  HOH HOH B . 
IA 5 HOH 18  506  506  HOH HOH B . 
IA 5 HOH 19  507  507  HOH HOH B . 
IA 5 HOH 20  510  510  HOH HOH B . 
IA 5 HOH 21  512  512  HOH HOH B . 
IA 5 HOH 22  514  514  HOH HOH B . 
IA 5 HOH 23  523  523  HOH HOH B . 
IA 5 HOH 24  530  530  HOH HOH B . 
IA 5 HOH 25  531  531  HOH HOH B . 
IA 5 HOH 26  532  532  HOH HOH B . 
IA 5 HOH 27  537  537  HOH HOH B . 
IA 5 HOH 28  546  546  HOH HOH B . 
IA 5 HOH 29  548  548  HOH HOH B . 
IA 5 HOH 30  551  551  HOH HOH B . 
IA 5 HOH 31  560  560  HOH HOH B . 
IA 5 HOH 32  563  563  HOH HOH B . 
IA 5 HOH 33  564  564  HOH HOH B . 
IA 5 HOH 34  566  566  HOH HOH B . 
IA 5 HOH 35  574  574  HOH HOH B . 
IA 5 HOH 36  584  584  HOH HOH B . 
IA 5 HOH 37  586  586  HOH HOH B . 
IA 5 HOH 38  593  593  HOH HOH B . 
IA 5 HOH 39  603  603  HOH HOH B . 
IA 5 HOH 40  608  608  HOH HOH B . 
IA 5 HOH 41  615  615  HOH HOH B . 
IA 5 HOH 42  634  634  HOH HOH B . 
IA 5 HOH 43  641  641  HOH HOH B . 
IA 5 HOH 44  642  642  HOH HOH B . 
IA 5 HOH 45  646  646  HOH HOH B . 
IA 5 HOH 46  665  665  HOH HOH B . 
IA 5 HOH 47  666  666  HOH HOH B . 
IA 5 HOH 48  668  668  HOH HOH B . 
IA 5 HOH 49  672  672  HOH HOH B . 
IA 5 HOH 50  676  676  HOH HOH B . 
IA 5 HOH 51  685  685  HOH HOH B . 
IA 5 HOH 52  689  689  HOH HOH B . 
IA 5 HOH 53  693  693  HOH HOH B . 
IA 5 HOH 54  696  696  HOH HOH B . 
IA 5 HOH 55  703  703  HOH HOH B . 
IA 5 HOH 56  713  713  HOH HOH B . 
IA 5 HOH 57  719  719  HOH HOH B . 
IA 5 HOH 58  728  728  HOH HOH B . 
IA 5 HOH 59  732  732  HOH HOH B . 
IA 5 HOH 60  734  734  HOH HOH B . 
IA 5 HOH 61  741  741  HOH HOH B . 
IA 5 HOH 62  748  748  HOH HOH B . 
IA 5 HOH 63  749  749  HOH HOH B . 
IA 5 HOH 64  765  765  HOH HOH B . 
IA 5 HOH 65  772  772  HOH HOH B . 
IA 5 HOH 66  778  778  HOH HOH B . 
IA 5 HOH 67  783  783  HOH HOH B . 
IA 5 HOH 68  790  790  HOH HOH B . 
IA 5 HOH 69  795  795  HOH HOH B . 
IA 5 HOH 70  798  798  HOH HOH B . 
IA 5 HOH 71  801  801  HOH HOH B . 
IA 5 HOH 72  803  803  HOH HOH B . 
IA 5 HOH 73  808  808  HOH HOH B . 
IA 5 HOH 74  822  822  HOH HOH B . 
IA 5 HOH 75  823  823  HOH HOH B . 
IA 5 HOH 76  826  826  HOH HOH B . 
IA 5 HOH 77  830  830  HOH HOH B . 
IA 5 HOH 78  833  833  HOH HOH B . 
IA 5 HOH 79  848  848  HOH HOH B . 
IA 5 HOH 80  850  850  HOH HOH B . 
IA 5 HOH 81  857  857  HOH HOH B . 
IA 5 HOH 82  862  862  HOH HOH B . 
IA 5 HOH 83  865  865  HOH HOH B . 
IA 5 HOH 84  868  868  HOH HOH B . 
IA 5 HOH 85  883  883  HOH HOH B . 
IA 5 HOH 86  914  914  HOH HOH B . 
IA 5 HOH 87  915  915  HOH HOH B . 
IA 5 HOH 88  919  919  HOH HOH B . 
IA 5 HOH 89  920  920  HOH HOH B . 
IA 5 HOH 90  923  923  HOH HOH B . 
IA 5 HOH 91  924  924  HOH HOH B . 
IA 5 HOH 92  925  925  HOH HOH B . 
IA 5 HOH 93  961  961  HOH HOH B . 
IA 5 HOH 94  967  967  HOH HOH B . 
IA 5 HOH 95  981  981  HOH HOH B . 
IA 5 HOH 96  982  982  HOH HOH B . 
IA 5 HOH 97  987  987  HOH HOH B . 
IA 5 HOH 98  1001 1001 HOH HOH B . 
IA 5 HOH 99  1002 1002 HOH HOH B . 
IA 5 HOH 100 1003 1003 HOH HOH B . 
IA 5 HOH 101 1025 1025 HOH HOH B . 
IA 5 HOH 102 1030 1030 HOH HOH B . 
IA 5 HOH 103 1093 1093 HOH HOH B . 
IA 5 HOH 104 1094 1094 HOH HOH B . 
IA 5 HOH 105 1095 1095 HOH HOH B . 
IA 5 HOH 106 1096 1096 HOH HOH B . 
IA 5 HOH 107 1102 1102 HOH HOH B . 
IA 5 HOH 108 1103 1103 HOH HOH B . 
IA 5 HOH 109 1104 1104 HOH HOH B . 
IA 5 HOH 110 1143 1143 HOH HOH B . 
IA 5 HOH 111 1144 1144 HOH HOH B . 
IA 5 HOH 112 1145 1145 HOH HOH B . 
IA 5 HOH 113 1146 1146 HOH HOH B . 
IA 5 HOH 114 1147 1147 HOH HOH B . 
IA 5 HOH 115 1148 1148 HOH HOH B . 
IA 5 HOH 116 1159 1159 HOH HOH B . 
IA 5 HOH 117 1198 1198 HOH HOH B . 
IA 5 HOH 118 1211 1211 HOH HOH B . 
IA 5 HOH 119 1223 1223 HOH HOH B . 
IA 5 HOH 120 1263 1263 HOH HOH B . 
IA 5 HOH 121 1272 1272 HOH HOH B . 
IA 5 HOH 122 1307 1307 HOH HOH B . 
IA 5 HOH 123 1310 1310 HOH HOH B . 
IA 5 HOH 124 1314 1314 HOH HOH B . 
IA 5 HOH 125 1322 1322 HOH HOH B . 
IA 5 HOH 126 1325 1325 HOH HOH B . 
IA 5 HOH 127 1327 1327 HOH HOH B . 
IA 5 HOH 128 1331 1331 HOH HOH B . 
IA 5 HOH 129 1339 1339 HOH HOH B . 
IA 5 HOH 130 1341 1341 HOH HOH B . 
IA 5 HOH 131 1344 1344 HOH HOH B . 
IA 5 HOH 132 1345 1345 HOH HOH B . 
IA 5 HOH 133 1400 1400 HOH HOH B . 
IA 5 HOH 134 1420 1420 HOH HOH B . 
IA 5 HOH 135 1427 1427 HOH HOH B . 
IA 5 HOH 136 1455 1455 HOH HOH B . 
IA 5 HOH 137 1456 1456 HOH HOH B . 
IA 5 HOH 138 1460 1460 HOH HOH B . 
IA 5 HOH 139 1461 1461 HOH HOH B . 
IA 5 HOH 140 1528 1528 HOH HOH B . 
IA 5 HOH 141 1576 1576 HOH HOH B . 
JA 5 HOH 1   402  402  HOH HOH C . 
JA 5 HOH 2   411  411  HOH HOH C . 
JA 5 HOH 3   421  421  HOH HOH C . 
JA 5 HOH 4   434  434  HOH HOH C . 
JA 5 HOH 5   489  489  HOH HOH C . 
JA 5 HOH 6   509  509  HOH HOH C . 
JA 5 HOH 7   624  624  HOH HOH C . 
JA 5 HOH 8   625  625  HOH HOH C . 
JA 5 HOH 9   631  631  HOH HOH C . 
JA 5 HOH 10  633  633  HOH HOH C . 
JA 5 HOH 11  637  637  HOH HOH C . 
JA 5 HOH 12  675  675  HOH HOH C . 
JA 5 HOH 13  709  709  HOH HOH C . 
JA 5 HOH 14  754  754  HOH HOH C . 
JA 5 HOH 15  770  770  HOH HOH C . 
JA 5 HOH 16  793  793  HOH HOH C . 
JA 5 HOH 17  797  797  HOH HOH C . 
JA 5 HOH 18  800  800  HOH HOH C . 
JA 5 HOH 19  802  802  HOH HOH C . 
JA 5 HOH 20  804  804  HOH HOH C . 
JA 5 HOH 21  815  815  HOH HOH C . 
JA 5 HOH 22  926  926  HOH HOH C . 
JA 5 HOH 23  953  953  HOH HOH C . 
JA 5 HOH 24  1029 1029 HOH HOH C . 
JA 5 HOH 25  1062 1062 HOH HOH C . 
JA 5 HOH 26  1064 1064 HOH HOH C . 
JA 5 HOH 27  1065 1065 HOH HOH C . 
JA 5 HOH 28  1066 1066 HOH HOH C . 
JA 5 HOH 29  1069 1069 HOH HOH C . 
JA 5 HOH 30  1224 1224 HOH HOH C . 
JA 5 HOH 31  1254 1254 HOH HOH C . 
JA 5 HOH 32  1262 1262 HOH HOH C . 
JA 5 HOH 33  1266 1266 HOH HOH C . 
JA 5 HOH 34  1271 1271 HOH HOH C . 
JA 5 HOH 35  1275 1275 HOH HOH C . 
JA 5 HOH 36  1296 1296 HOH HOH C . 
JA 5 HOH 37  1306 1306 HOH HOH C . 
JA 5 HOH 38  1319 1319 HOH HOH C . 
JA 5 HOH 39  1329 1329 HOH HOH C . 
JA 5 HOH 40  1332 1332 HOH HOH C . 
JA 5 HOH 41  1346 1346 HOH HOH C . 
JA 5 HOH 42  1347 1347 HOH HOH C . 
JA 5 HOH 43  1368 1368 HOH HOH C . 
JA 5 HOH 44  1373 1373 HOH HOH C . 
JA 5 HOH 45  1374 1374 HOH HOH C . 
JA 5 HOH 46  1401 1401 HOH HOH C . 
JA 5 HOH 47  1416 1416 HOH HOH C . 
JA 5 HOH 48  1450 1450 HOH HOH C . 
JA 5 HOH 49  1464 1464 HOH HOH C . 
JA 5 HOH 50  1471 1471 HOH HOH C . 
JA 5 HOH 51  1480 1480 HOH HOH C . 
JA 5 HOH 52  1484 1484 HOH HOH C . 
JA 5 HOH 53  1510 1510 HOH HOH C . 
JA 5 HOH 54  1541 1541 HOH HOH C . 
JA 5 HOH 55  1556 1556 HOH HOH C . 
JA 5 HOH 56  1581 1581 HOH HOH C . 
JA 5 HOH 57  1586 1586 HOH HOH C . 
KA 5 HOH 1   403  403  HOH HOH D . 
KA 5 HOH 2   412  412  HOH HOH D . 
KA 5 HOH 3   422  422  HOH HOH D . 
KA 5 HOH 4   435  435  HOH HOH D . 
KA 5 HOH 5   437  437  HOH HOH D . 
KA 5 HOH 6   447  447  HOH HOH D . 
KA 5 HOH 7   448  448  HOH HOH D . 
KA 5 HOH 8   450  450  HOH HOH D . 
KA 5 HOH 9   451  451  HOH HOH D . 
KA 5 HOH 10  461  461  HOH HOH D . 
KA 5 HOH 11  467  467  HOH HOH D . 
KA 5 HOH 12  471  471  HOH HOH D . 
KA 5 HOH 13  475  475  HOH HOH D . 
KA 5 HOH 14  483  483  HOH HOH D . 
KA 5 HOH 15  487  487  HOH HOH D . 
KA 5 HOH 16  494  494  HOH HOH D . 
KA 5 HOH 17  498  498  HOH HOH D . 
KA 5 HOH 18  508  508  HOH HOH D . 
KA 5 HOH 19  519  519  HOH HOH D . 
KA 5 HOH 20  525  525  HOH HOH D . 
KA 5 HOH 21  549  549  HOH HOH D . 
KA 5 HOH 22  552  552  HOH HOH D . 
KA 5 HOH 23  556  556  HOH HOH D . 
KA 5 HOH 24  558  558  HOH HOH D . 
KA 5 HOH 25  559  559  HOH HOH D . 
KA 5 HOH 26  565  565  HOH HOH D . 
KA 5 HOH 27  572  572  HOH HOH D . 
KA 5 HOH 28  573  573  HOH HOH D . 
KA 5 HOH 29  580  580  HOH HOH D . 
KA 5 HOH 30  582  582  HOH HOH D . 
KA 5 HOH 31  583  583  HOH HOH D . 
KA 5 HOH 32  591  591  HOH HOH D . 
KA 5 HOH 33  612  612  HOH HOH D . 
KA 5 HOH 34  614  614  HOH HOH D . 
KA 5 HOH 35  628  628  HOH HOH D . 
KA 5 HOH 36  630  630  HOH HOH D . 
KA 5 HOH 37  643  643  HOH HOH D . 
KA 5 HOH 38  645  645  HOH HOH D . 
KA 5 HOH 39  648  648  HOH HOH D . 
KA 5 HOH 40  651  651  HOH HOH D . 
KA 5 HOH 41  682  682  HOH HOH D . 
KA 5 HOH 42  688  688  HOH HOH D . 
KA 5 HOH 43  690  690  HOH HOH D . 
KA 5 HOH 44  691  691  HOH HOH D . 
KA 5 HOH 45  692  692  HOH HOH D . 
KA 5 HOH 46  701  701  HOH HOH D . 
KA 5 HOH 47  704  704  HOH HOH D . 
KA 5 HOH 48  716  716  HOH HOH D . 
KA 5 HOH 49  721  721  HOH HOH D . 
KA 5 HOH 50  727  727  HOH HOH D . 
KA 5 HOH 51  735  735  HOH HOH D . 
KA 5 HOH 52  739  739  HOH HOH D . 
KA 5 HOH 53  745  745  HOH HOH D . 
KA 5 HOH 54  753  753  HOH HOH D . 
KA 5 HOH 55  755  755  HOH HOH D . 
KA 5 HOH 56  784  784  HOH HOH D . 
KA 5 HOH 57  791  791  HOH HOH D . 
KA 5 HOH 58  813  813  HOH HOH D . 
KA 5 HOH 59  820  820  HOH HOH D . 
KA 5 HOH 60  821  821  HOH HOH D . 
KA 5 HOH 61  829  829  HOH HOH D . 
KA 5 HOH 62  851  851  HOH HOH D . 
KA 5 HOH 63  856  856  HOH HOH D . 
KA 5 HOH 64  869  869  HOH HOH D . 
KA 5 HOH 65  873  873  HOH HOH D . 
KA 5 HOH 66  875  875  HOH HOH D . 
KA 5 HOH 67  890  890  HOH HOH D . 
KA 5 HOH 68  891  891  HOH HOH D . 
KA 5 HOH 69  927  927  HOH HOH D . 
KA 5 HOH 70  964  964  HOH HOH D . 
KA 5 HOH 71  965  965  HOH HOH D . 
KA 5 HOH 72  966  966  HOH HOH D . 
KA 5 HOH 73  975  975  HOH HOH D . 
KA 5 HOH 74  984  984  HOH HOH D . 
KA 5 HOH 75  990  990  HOH HOH D . 
KA 5 HOH 76  992  992  HOH HOH D . 
KA 5 HOH 77  1022 1022 HOH HOH D . 
KA 5 HOH 78  1023 1023 HOH HOH D . 
KA 5 HOH 79  1024 1024 HOH HOH D . 
KA 5 HOH 80  1061 1061 HOH HOH D . 
KA 5 HOH 81  1063 1063 HOH HOH D . 
KA 5 HOH 82  1067 1067 HOH HOH D . 
KA 5 HOH 83  1070 1070 HOH HOH D . 
KA 5 HOH 84  1071 1071 HOH HOH D . 
KA 5 HOH 85  1072 1072 HOH HOH D . 
KA 5 HOH 86  1073 1073 HOH HOH D . 
KA 5 HOH 87  1074 1074 HOH HOH D . 
KA 5 HOH 88  1085 1085 HOH HOH D . 
KA 5 HOH 89  1086 1086 HOH HOH D . 
KA 5 HOH 90  1087 1087 HOH HOH D . 
KA 5 HOH 91  1099 1099 HOH HOH D . 
KA 5 HOH 92  1100 1100 HOH HOH D . 
KA 5 HOH 93  1133 1133 HOH HOH D . 
KA 5 HOH 94  1134 1134 HOH HOH D . 
KA 5 HOH 95  1135 1135 HOH HOH D . 
KA 5 HOH 96  1136 1136 HOH HOH D . 
KA 5 HOH 97  1137 1137 HOH HOH D . 
KA 5 HOH 98  1138 1138 HOH HOH D . 
KA 5 HOH 99  1151 1151 HOH HOH D . 
KA 5 HOH 100 1168 1168 HOH HOH D . 
KA 5 HOH 101 1169 1169 HOH HOH D . 
KA 5 HOH 102 1171 1171 HOH HOH D . 
KA 5 HOH 103 1172 1172 HOH HOH D . 
KA 5 HOH 104 1173 1173 HOH HOH D . 
KA 5 HOH 105 1197 1197 HOH HOH D . 
KA 5 HOH 106 1210 1210 HOH HOH D . 
KA 5 HOH 107 1230 1230 HOH HOH D . 
KA 5 HOH 108 1231 1231 HOH HOH D . 
KA 5 HOH 109 1241 1241 HOH HOH D . 
KA 5 HOH 110 1243 1243 HOH HOH D . 
KA 5 HOH 111 1244 1244 HOH HOH D . 
KA 5 HOH 112 1252 1252 HOH HOH D . 
KA 5 HOH 113 1256 1256 HOH HOH D . 
KA 5 HOH 114 1261 1261 HOH HOH D . 
KA 5 HOH 115 1281 1281 HOH HOH D . 
KA 5 HOH 116 1283 1283 HOH HOH D . 
KA 5 HOH 117 1297 1297 HOH HOH D . 
KA 5 HOH 118 1348 1348 HOH HOH D . 
KA 5 HOH 119 1349 1349 HOH HOH D . 
KA 5 HOH 120 1367 1367 HOH HOH D . 
KA 5 HOH 121 1370 1370 HOH HOH D . 
KA 5 HOH 122 1388 1388 HOH HOH D . 
KA 5 HOH 123 1411 1411 HOH HOH D . 
KA 5 HOH 124 1412 1412 HOH HOH D . 
KA 5 HOH 125 1423 1423 HOH HOH D . 
KA 5 HOH 126 1428 1428 HOH HOH D . 
KA 5 HOH 127 1440 1440 HOH HOH D . 
KA 5 HOH 128 1454 1454 HOH HOH D . 
KA 5 HOH 129 1473 1473 HOH HOH D . 
KA 5 HOH 130 1486 1486 HOH HOH D . 
KA 5 HOH 131 1488 1488 HOH HOH D . 
KA 5 HOH 132 1507 1507 HOH HOH D . 
KA 5 HOH 133 1548 1548 HOH HOH D . 
LA 5 HOH 1   413  413  HOH HOH E . 
LA 5 HOH 2   423  423  HOH HOH E . 
LA 5 HOH 3   438  438  HOH HOH E . 
LA 5 HOH 4   459  459  HOH HOH E . 
LA 5 HOH 5   465  465  HOH HOH E . 
LA 5 HOH 6   480  480  HOH HOH E . 
LA 5 HOH 7   485  485  HOH HOH E . 
LA 5 HOH 8   490  490  HOH HOH E . 
LA 5 HOH 9   491  491  HOH HOH E . 
LA 5 HOH 10  496  496  HOH HOH E . 
LA 5 HOH 11  504  504  HOH HOH E . 
LA 5 HOH 12  505  505  HOH HOH E . 
LA 5 HOH 13  518  518  HOH HOH E . 
LA 5 HOH 14  522  522  HOH HOH E . 
LA 5 HOH 15  524  524  HOH HOH E . 
LA 5 HOH 16  536  536  HOH HOH E . 
LA 5 HOH 17  538  538  HOH HOH E . 
LA 5 HOH 18  544  544  HOH HOH E . 
LA 5 HOH 19  545  545  HOH HOH E . 
LA 5 HOH 20  547  547  HOH HOH E . 
LA 5 HOH 21  553  553  HOH HOH E . 
LA 5 HOH 22  555  555  HOH HOH E . 
LA 5 HOH 23  557  557  HOH HOH E . 
LA 5 HOH 24  561  561  HOH HOH E . 
LA 5 HOH 25  569  569  HOH HOH E . 
LA 5 HOH 26  571  571  HOH HOH E . 
LA 5 HOH 27  575  575  HOH HOH E . 
LA 5 HOH 28  581  581  HOH HOH E . 
LA 5 HOH 29  589  589  HOH HOH E . 
LA 5 HOH 30  595  595  HOH HOH E . 
LA 5 HOH 31  596  596  HOH HOH E . 
LA 5 HOH 32  598  598  HOH HOH E . 
LA 5 HOH 33  600  600  HOH HOH E . 
LA 5 HOH 34  606  606  HOH HOH E . 
LA 5 HOH 35  613  613  HOH HOH E . 
LA 5 HOH 36  619  619  HOH HOH E . 
LA 5 HOH 37  622  622  HOH HOH E . 
LA 5 HOH 38  644  644  HOH HOH E . 
LA 5 HOH 39  650  650  HOH HOH E . 
LA 5 HOH 40  660  660  HOH HOH E . 
LA 5 HOH 41  674  674  HOH HOH E . 
LA 5 HOH 42  681  681  HOH HOH E . 
LA 5 HOH 43  695  695  HOH HOH E . 
LA 5 HOH 44  698  698  HOH HOH E . 
LA 5 HOH 45  700  700  HOH HOH E . 
LA 5 HOH 46  714  714  HOH HOH E . 
LA 5 HOH 47  718  718  HOH HOH E . 
LA 5 HOH 48  723  723  HOH HOH E . 
LA 5 HOH 49  726  726  HOH HOH E . 
LA 5 HOH 50  733  733  HOH HOH E . 
LA 5 HOH 51  737  737  HOH HOH E . 
LA 5 HOH 52  740  740  HOH HOH E . 
LA 5 HOH 53  742  742  HOH HOH E . 
LA 5 HOH 54  744  744  HOH HOH E . 
LA 5 HOH 55  764  764  HOH HOH E . 
LA 5 HOH 56  769  769  HOH HOH E . 
LA 5 HOH 57  773  773  HOH HOH E . 
LA 5 HOH 58  775  775  HOH HOH E . 
LA 5 HOH 59  776  776  HOH HOH E . 
LA 5 HOH 60  780  780  HOH HOH E . 
LA 5 HOH 61  792  792  HOH HOH E . 
LA 5 HOH 62  796  796  HOH HOH E . 
LA 5 HOH 63  799  799  HOH HOH E . 
LA 5 HOH 64  806  806  HOH HOH E . 
LA 5 HOH 65  807  807  HOH HOH E . 
LA 5 HOH 66  814  814  HOH HOH E . 
LA 5 HOH 67  819  819  HOH HOH E . 
LA 5 HOH 68  836  836  HOH HOH E . 
LA 5 HOH 69  840  840  HOH HOH E . 
LA 5 HOH 70  842  842  HOH HOH E . 
LA 5 HOH 71  859  859  HOH HOH E . 
LA 5 HOH 72  867  867  HOH HOH E . 
LA 5 HOH 73  871  871  HOH HOH E . 
LA 5 HOH 74  874  874  HOH HOH E . 
LA 5 HOH 75  892  892  HOH HOH E . 
LA 5 HOH 76  900  900  HOH HOH E . 
LA 5 HOH 77  928  928  HOH HOH E . 
LA 5 HOH 78  929  929  HOH HOH E . 
LA 5 HOH 79  930  930  HOH HOH E . 
LA 5 HOH 80  954  954  HOH HOH E . 
LA 5 HOH 81  1004 1004 HOH HOH E . 
LA 5 HOH 82  1007 1007 HOH HOH E . 
LA 5 HOH 83  1008 1008 HOH HOH E . 
LA 5 HOH 84  1012 1012 HOH HOH E . 
LA 5 HOH 85  1017 1017 HOH HOH E . 
LA 5 HOH 86  1019 1019 HOH HOH E . 
LA 5 HOH 87  1020 1020 HOH HOH E . 
LA 5 HOH 88  1051 1051 HOH HOH E . 
LA 5 HOH 89  1052 1052 HOH HOH E . 
LA 5 HOH 90  1053 1053 HOH HOH E . 
LA 5 HOH 91  1055 1055 HOH HOH E . 
LA 5 HOH 92  1057 1057 HOH HOH E . 
LA 5 HOH 93  1076 1076 HOH HOH E . 
LA 5 HOH 94  1077 1077 HOH HOH E . 
LA 5 HOH 95  1127 1127 HOH HOH E . 
LA 5 HOH 96  1128 1128 HOH HOH E . 
LA 5 HOH 97  1129 1129 HOH HOH E . 
LA 5 HOH 98  1130 1130 HOH HOH E . 
LA 5 HOH 99  1131 1131 HOH HOH E . 
LA 5 HOH 100 1160 1160 HOH HOH E . 
LA 5 HOH 101 1162 1162 HOH HOH E . 
LA 5 HOH 102 1163 1163 HOH HOH E . 
LA 5 HOH 103 1164 1164 HOH HOH E . 
LA 5 HOH 104 1165 1165 HOH HOH E . 
LA 5 HOH 105 1167 1167 HOH HOH E . 
LA 5 HOH 106 1201 1201 HOH HOH E . 
LA 5 HOH 107 1209 1209 HOH HOH E . 
LA 5 HOH 108 1217 1217 HOH HOH E . 
LA 5 HOH 109 1218 1218 HOH HOH E . 
LA 5 HOH 110 1219 1219 HOH HOH E . 
LA 5 HOH 111 1242 1242 HOH HOH E . 
LA 5 HOH 112 1248 1248 HOH HOH E . 
LA 5 HOH 113 1249 1249 HOH HOH E . 
LA 5 HOH 114 1274 1274 HOH HOH E . 
LA 5 HOH 115 1286 1286 HOH HOH E . 
LA 5 HOH 116 1288 1288 HOH HOH E . 
LA 5 HOH 117 1292 1292 HOH HOH E . 
LA 5 HOH 118 1302 1302 HOH HOH E . 
LA 5 HOH 119 1304 1304 HOH HOH E . 
LA 5 HOH 120 1330 1330 HOH HOH E . 
LA 5 HOH 121 1350 1350 HOH HOH E . 
LA 5 HOH 122 1351 1351 HOH HOH E . 
LA 5 HOH 123 1372 1372 HOH HOH E . 
LA 5 HOH 124 1380 1380 HOH HOH E . 
LA 5 HOH 125 1386 1386 HOH HOH E . 
LA 5 HOH 126 1389 1389 HOH HOH E . 
LA 5 HOH 127 1396 1396 HOH HOH E . 
LA 5 HOH 128 1399 1399 HOH HOH E . 
LA 5 HOH 129 1430 1430 HOH HOH E . 
LA 5 HOH 130 1452 1452 HOH HOH E . 
LA 5 HOH 131 1518 1518 HOH HOH E . 
LA 5 HOH 132 1562 1562 HOH HOH E . 
LA 5 HOH 133 1582 1582 HOH HOH E . 
MA 5 HOH 1   404  404  HOH HOH F . 
MA 5 HOH 2   414  414  HOH HOH F . 
MA 5 HOH 3   424  424  HOH HOH F . 
MA 5 HOH 4   446  446  HOH HOH F . 
MA 5 HOH 5   449  449  HOH HOH F . 
MA 5 HOH 6   463  463  HOH HOH F . 
MA 5 HOH 7   469  469  HOH HOH F . 
MA 5 HOH 8   484  484  HOH HOH F . 
MA 5 HOH 9   486  486  HOH HOH F . 
MA 5 HOH 10  492  492  HOH HOH F . 
MA 5 HOH 11  513  513  HOH HOH F . 
MA 5 HOH 12  516  516  HOH HOH F . 
MA 5 HOH 13  517  517  HOH HOH F . 
MA 5 HOH 14  528  528  HOH HOH F . 
MA 5 HOH 15  533  533  HOH HOH F . 
MA 5 HOH 16  540  540  HOH HOH F . 
MA 5 HOH 17  541  541  HOH HOH F . 
MA 5 HOH 18  542  542  HOH HOH F . 
MA 5 HOH 19  554  554  HOH HOH F . 
MA 5 HOH 20  594  594  HOH HOH F . 
MA 5 HOH 21  597  597  HOH HOH F . 
MA 5 HOH 22  599  599  HOH HOH F . 
MA 5 HOH 23  616  616  HOH HOH F . 
MA 5 HOH 24  618  618  HOH HOH F . 
MA 5 HOH 25  623  623  HOH HOH F . 
MA 5 HOH 26  626  626  HOH HOH F . 
MA 5 HOH 27  629  629  HOH HOH F . 
MA 5 HOH 28  636  636  HOH HOH F . 
MA 5 HOH 29  649  649  HOH HOH F . 
MA 5 HOH 30  652  652  HOH HOH F . 
MA 5 HOH 31  657  657  HOH HOH F . 
MA 5 HOH 32  669  669  HOH HOH F . 
MA 5 HOH 33  670  670  HOH HOH F . 
MA 5 HOH 34  673  673  HOH HOH F . 
MA 5 HOH 35  680  680  HOH HOH F . 
MA 5 HOH 36  683  683  HOH HOH F . 
MA 5 HOH 37  687  687  HOH HOH F . 
MA 5 HOH 38  694  694  HOH HOH F . 
MA 5 HOH 39  712  712  HOH HOH F . 
MA 5 HOH 40  715  715  HOH HOH F . 
MA 5 HOH 41  724  724  HOH HOH F . 
MA 5 HOH 42  729  729  HOH HOH F . 
MA 5 HOH 43  738  738  HOH HOH F . 
MA 5 HOH 44  746  746  HOH HOH F . 
MA 5 HOH 45  751  751  HOH HOH F . 
MA 5 HOH 46  757  757  HOH HOH F . 
MA 5 HOH 47  758  758  HOH HOH F . 
MA 5 HOH 48  761  761  HOH HOH F . 
MA 5 HOH 49  766  766  HOH HOH F . 
MA 5 HOH 50  768  768  HOH HOH F . 
MA 5 HOH 51  774  774  HOH HOH F . 
MA 5 HOH 52  785  785  HOH HOH F . 
MA 5 HOH 53  788  788  HOH HOH F . 
MA 5 HOH 54  794  794  HOH HOH F . 
MA 5 HOH 55  805  805  HOH HOH F . 
MA 5 HOH 56  809  809  HOH HOH F . 
MA 5 HOH 57  810  810  HOH HOH F . 
MA 5 HOH 58  811  811  HOH HOH F . 
MA 5 HOH 59  834  834  HOH HOH F . 
MA 5 HOH 60  835  835  HOH HOH F . 
MA 5 HOH 61  838  838  HOH HOH F . 
MA 5 HOH 62  839  839  HOH HOH F . 
MA 5 HOH 63  843  843  HOH HOH F . 
MA 5 HOH 64  844  844  HOH HOH F . 
MA 5 HOH 65  847  847  HOH HOH F . 
MA 5 HOH 66  849  849  HOH HOH F . 
MA 5 HOH 67  852  852  HOH HOH F . 
MA 5 HOH 68  855  855  HOH HOH F . 
MA 5 HOH 69  879  879  HOH HOH F . 
MA 5 HOH 70  931  931  HOH HOH F . 
MA 5 HOH 71  932  932  HOH HOH F . 
MA 5 HOH 72  933  933  HOH HOH F . 
MA 5 HOH 73  934  934  HOH HOH F . 
MA 5 HOH 74  935  935  HOH HOH F . 
MA 5 HOH 75  963  963  HOH HOH F . 
MA 5 HOH 76  985  985  HOH HOH F . 
MA 5 HOH 77  986  986  HOH HOH F . 
MA 5 HOH 78  988  988  HOH HOH F . 
MA 5 HOH 79  989  989  HOH HOH F . 
MA 5 HOH 80  994  994  HOH HOH F . 
MA 5 HOH 81  1021 1021 HOH HOH F . 
MA 5 HOH 82  1028 1028 HOH HOH F . 
MA 5 HOH 83  1056 1056 HOH HOH F . 
MA 5 HOH 84  1058 1058 HOH HOH F . 
MA 5 HOH 85  1079 1079 HOH HOH F . 
MA 5 HOH 86  1101 1101 HOH HOH F . 
MA 5 HOH 87  1105 1105 HOH HOH F . 
MA 5 HOH 88  1106 1106 HOH HOH F . 
MA 5 HOH 89  1132 1132 HOH HOH F . 
MA 5 HOH 90  1154 1154 HOH HOH F . 
MA 5 HOH 91  1157 1157 HOH HOH F . 
MA 5 HOH 92  1161 1161 HOH HOH F . 
MA 5 HOH 93  1170 1170 HOH HOH F . 
MA 5 HOH 94  1174 1174 HOH HOH F . 
MA 5 HOH 95  1195 1195 HOH HOH F . 
MA 5 HOH 96  1196 1196 HOH HOH F . 
MA 5 HOH 97  1199 1199 HOH HOH F . 
MA 5 HOH 98  1200 1200 HOH HOH F . 
MA 5 HOH 99  1205 1205 HOH HOH F . 
MA 5 HOH 100 1212 1212 HOH HOH F . 
MA 5 HOH 101 1247 1247 HOH HOH F . 
MA 5 HOH 102 1300 1300 HOH HOH F . 
MA 5 HOH 103 1305 1305 HOH HOH F . 
MA 5 HOH 104 1312 1312 HOH HOH F . 
MA 5 HOH 105 1318 1318 HOH HOH F . 
MA 5 HOH 106 1320 1320 HOH HOH F . 
MA 5 HOH 107 1328 1328 HOH HOH F . 
MA 5 HOH 108 1337 1337 HOH HOH F . 
MA 5 HOH 109 1352 1352 HOH HOH F . 
MA 5 HOH 110 1353 1353 HOH HOH F . 
MA 5 HOH 111 1366 1366 HOH HOH F . 
MA 5 HOH 112 1375 1375 HOH HOH F . 
MA 5 HOH 113 1377 1377 HOH HOH F . 
MA 5 HOH 114 1394 1394 HOH HOH F . 
MA 5 HOH 115 1437 1437 HOH HOH F . 
MA 5 HOH 116 1443 1443 HOH HOH F . 
MA 5 HOH 117 1465 1465 HOH HOH F . 
MA 5 HOH 118 1479 1479 HOH HOH F . 
MA 5 HOH 119 1485 1485 HOH HOH F . 
MA 5 HOH 120 1501 1501 HOH HOH F . 
MA 5 HOH 121 1502 1502 HOH HOH F . 
MA 5 HOH 122 1521 1521 HOH HOH F . 
MA 5 HOH 123 1543 1543 HOH HOH F . 
MA 5 HOH 124 1587 1587 HOH HOH F . 
MA 5 HOH 125 1605 1605 HOH HOH F . 
MA 5 HOH 126 1632 1632 HOH HOH F . 
NA 5 HOH 1   405  405  HOH HOH G . 
NA 5 HOH 2   415  415  HOH HOH G . 
NA 5 HOH 3   425  425  HOH HOH G . 
NA 5 HOH 4   436  436  HOH HOH G . 
NA 5 HOH 5   562  562  HOH HOH G . 
NA 5 HOH 6   567  567  HOH HOH G . 
NA 5 HOH 7   570  570  HOH HOH G . 
NA 5 HOH 8   605  605  HOH HOH G . 
NA 5 HOH 9   639  639  HOH HOH G . 
NA 5 HOH 10  722  722  HOH HOH G . 
NA 5 HOH 11  750  750  HOH HOH G . 
NA 5 HOH 12  812  812  HOH HOH G . 
NA 5 HOH 13  902  902  HOH HOH G . 
NA 5 HOH 14  905  905  HOH HOH G . 
NA 5 HOH 15  906  906  HOH HOH G . 
NA 5 HOH 16  907  907  HOH HOH G . 
NA 5 HOH 17  908  908  HOH HOH G . 
NA 5 HOH 18  910  910  HOH HOH G . 
NA 5 HOH 19  948  948  HOH HOH G . 
NA 5 HOH 20  962  962  HOH HOH G . 
NA 5 HOH 21  1078 1078 HOH HOH G . 
NA 5 HOH 22  1080 1080 HOH HOH G . 
NA 5 HOH 23  1081 1081 HOH HOH G . 
NA 5 HOH 24  1082 1082 HOH HOH G . 
NA 5 HOH 25  1083 1083 HOH HOH G . 
NA 5 HOH 26  1089 1089 HOH HOH G . 
NA 5 HOH 27  1091 1091 HOH HOH G . 
NA 5 HOH 28  1092 1092 HOH HOH G . 
NA 5 HOH 29  1194 1194 HOH HOH G . 
NA 5 HOH 30  1204 1204 HOH HOH G . 
NA 5 HOH 31  1215 1215 HOH HOH G . 
NA 5 HOH 32  1232 1232 HOH HOH G . 
NA 5 HOH 33  1234 1234 HOH HOH G . 
NA 5 HOH 34  1235 1235 HOH HOH G . 
NA 5 HOH 35  1236 1236 HOH HOH G . 
NA 5 HOH 36  1246 1246 HOH HOH G . 
NA 5 HOH 37  1269 1269 HOH HOH G . 
NA 5 HOH 38  1280 1280 HOH HOH G . 
NA 5 HOH 39  1289 1289 HOH HOH G . 
NA 5 HOH 40  1301 1301 HOH HOH G . 
NA 5 HOH 41  1313 1313 HOH HOH G . 
NA 5 HOH 42  1334 1334 HOH HOH G . 
NA 5 HOH 43  1335 1335 HOH HOH G . 
NA 5 HOH 44  1354 1354 HOH HOH G . 
NA 5 HOH 45  1355 1355 HOH HOH G . 
NA 5 HOH 46  1404 1404 HOH HOH G . 
NA 5 HOH 47  1407 1407 HOH HOH G . 
NA 5 HOH 48  1424 1424 HOH HOH G . 
NA 5 HOH 49  1429 1429 HOH HOH G . 
NA 5 HOH 50  1436 1436 HOH HOH G . 
NA 5 HOH 51  1441 1441 HOH HOH G . 
NA 5 HOH 52  1467 1467 HOH HOH G . 
NA 5 HOH 53  1493 1493 HOH HOH G . 
NA 5 HOH 54  1588 1588 HOH HOH G . 
NA 5 HOH 55  1619 1619 HOH HOH G . 
OA 5 HOH 1   406  406  HOH HOH H . 
OA 5 HOH 2   416  416  HOH HOH H . 
OA 5 HOH 3   426  426  HOH HOH H . 
OA 5 HOH 4   432  432  HOH HOH H . 
OA 5 HOH 5   440  440  HOH HOH H . 
OA 5 HOH 6   441  441  HOH HOH H . 
OA 5 HOH 7   443  443  HOH HOH H . 
OA 5 HOH 8   444  444  HOH HOH H . 
OA 5 HOH 9   477  477  HOH HOH H . 
OA 5 HOH 10  479  479  HOH HOH H . 
OA 5 HOH 11  482  482  HOH HOH H . 
OA 5 HOH 12  520  520  HOH HOH H . 
OA 5 HOH 13  521  521  HOH HOH H . 
OA 5 HOH 14  539  539  HOH HOH H . 
OA 5 HOH 15  576  576  HOH HOH H . 
OA 5 HOH 16  604  604  HOH HOH H . 
OA 5 HOH 17  620  620  HOH HOH H . 
OA 5 HOH 18  635  635  HOH HOH H . 
OA 5 HOH 19  640  640  HOH HOH H . 
OA 5 HOH 20  658  658  HOH HOH H . 
OA 5 HOH 21  659  659  HOH HOH H . 
OA 5 HOH 22  663  663  HOH HOH H . 
OA 5 HOH 23  664  664  HOH HOH H . 
OA 5 HOH 24  667  667  HOH HOH H . 
OA 5 HOH 25  677  677  HOH HOH H . 
OA 5 HOH 26  678  678  HOH HOH H . 
OA 5 HOH 27  686  686  HOH HOH H . 
OA 5 HOH 28  711  711  HOH HOH H . 
OA 5 HOH 29  747  747  HOH HOH H . 
OA 5 HOH 30  760  760  HOH HOH H . 
OA 5 HOH 31  777  777  HOH HOH H . 
OA 5 HOH 32  825  825  HOH HOH H . 
OA 5 HOH 33  828  828  HOH HOH H . 
OA 5 HOH 34  872  872  HOH HOH H . 
OA 5 HOH 35  893  893  HOH HOH H . 
OA 5 HOH 36  936  936  HOH HOH H . 
OA 5 HOH 37  937  937  HOH HOH H . 
OA 5 HOH 38  995  995  HOH HOH H . 
OA 5 HOH 39  996  996  HOH HOH H . 
OA 5 HOH 40  997  997  HOH HOH H . 
OA 5 HOH 41  998  998  HOH HOH H . 
OA 5 HOH 42  999  999  HOH HOH H . 
OA 5 HOH 43  1000 1000 HOH HOH H . 
OA 5 HOH 44  1009 1009 HOH HOH H . 
OA 5 HOH 45  1010 1010 HOH HOH H . 
OA 5 HOH 46  1011 1011 HOH HOH H . 
OA 5 HOH 47  1013 1013 HOH HOH H . 
OA 5 HOH 48  1016 1016 HOH HOH H . 
OA 5 HOH 49  1018 1018 HOH HOH H . 
OA 5 HOH 50  1034 1034 HOH HOH H . 
OA 5 HOH 51  1036 1036 HOH HOH H . 
OA 5 HOH 52  1037 1037 HOH HOH H . 
OA 5 HOH 53  1041 1041 HOH HOH H . 
OA 5 HOH 54  1042 1042 HOH HOH H . 
OA 5 HOH 55  1088 1088 HOH HOH H . 
OA 5 HOH 56  1090 1090 HOH HOH H . 
OA 5 HOH 57  1140 1140 HOH HOH H . 
OA 5 HOH 58  1176 1176 HOH HOH H . 
OA 5 HOH 59  1177 1177 HOH HOH H . 
OA 5 HOH 60  1178 1178 HOH HOH H . 
OA 5 HOH 61  1179 1179 HOH HOH H . 
OA 5 HOH 62  1183 1183 HOH HOH H . 
OA 5 HOH 63  1184 1184 HOH HOH H . 
OA 5 HOH 64  1187 1187 HOH HOH H . 
OA 5 HOH 65  1191 1191 HOH HOH H . 
OA 5 HOH 66  1192 1192 HOH HOH H . 
OA 5 HOH 67  1193 1193 HOH HOH H . 
OA 5 HOH 68  1213 1213 HOH HOH H . 
OA 5 HOH 69  1214 1214 HOH HOH H . 
OA 5 HOH 70  1216 1216 HOH HOH H . 
OA 5 HOH 71  1233 1233 HOH HOH H . 
OA 5 HOH 72  1237 1237 HOH HOH H . 
OA 5 HOH 73  1239 1239 HOH HOH H . 
OA 5 HOH 74  1240 1240 HOH HOH H . 
OA 5 HOH 75  1251 1251 HOH HOH H . 
OA 5 HOH 76  1264 1264 HOH HOH H . 
OA 5 HOH 77  1270 1270 HOH HOH H . 
OA 5 HOH 78  1273 1273 HOH HOH H . 
OA 5 HOH 79  1277 1277 HOH HOH H . 
OA 5 HOH 80  1278 1278 HOH HOH H . 
OA 5 HOH 81  1282 1282 HOH HOH H . 
OA 5 HOH 82  1284 1284 HOH HOH H . 
OA 5 HOH 83  1298 1298 HOH HOH H . 
OA 5 HOH 84  1315 1315 HOH HOH H . 
OA 5 HOH 85  1324 1324 HOH HOH H . 
OA 5 HOH 86  1356 1356 HOH HOH H . 
OA 5 HOH 87  1357 1357 HOH HOH H . 
OA 5 HOH 88  1403 1403 HOH HOH H . 
OA 5 HOH 89  1414 1414 HOH HOH H . 
OA 5 HOH 90  1415 1415 HOH HOH H . 
OA 5 HOH 91  1422 1422 HOH HOH H . 
OA 5 HOH 92  1447 1447 HOH HOH H . 
OA 5 HOH 93  1459 1459 HOH HOH H . 
OA 5 HOH 94  1463 1463 HOH HOH H . 
OA 5 HOH 95  1469 1469 HOH HOH H . 
OA 5 HOH 96  1474 1474 HOH HOH H . 
OA 5 HOH 97  1487 1487 HOH HOH H . 
OA 5 HOH 98  1490 1490 HOH HOH H . 
OA 5 HOH 99  1497 1497 HOH HOH H . 
OA 5 HOH 100 1522 1522 HOH HOH H . 
OA 5 HOH 101 1540 1540 HOH HOH H . 
OA 5 HOH 102 1553 1553 HOH HOH H . 
OA 5 HOH 103 1561 1561 HOH HOH H . 
OA 5 HOH 104 1592 1592 HOH HOH H . 
OA 5 HOH 105 1609 1609 HOH HOH H . 
OA 5 HOH 106 1616 1616 HOH HOH H . 
OA 5 HOH 107 1618 1618 HOH HOH H . 
PA 5 HOH 1   417  417  HOH HOH I . 
PA 5 HOH 2   427  427  HOH HOH I . 
PA 5 HOH 3   439  439  HOH HOH I . 
PA 5 HOH 4   455  455  HOH HOH I . 
PA 5 HOH 5   478  478  HOH HOH I . 
PA 5 HOH 6   481  481  HOH HOH I . 
PA 5 HOH 7   499  499  HOH HOH I . 
PA 5 HOH 8   502  502  HOH HOH I . 
PA 5 HOH 9   535  535  HOH HOH I . 
PA 5 HOH 10  590  590  HOH HOH I . 
PA 5 HOH 11  592  592  HOH HOH I . 
PA 5 HOH 12  647  647  HOH HOH I . 
PA 5 HOH 13  656  656  HOH HOH I . 
PA 5 HOH 14  699  699  HOH HOH I . 
PA 5 HOH 15  708  708  HOH HOH I . 
PA 5 HOH 16  752  752  HOH HOH I . 
PA 5 HOH 17  759  759  HOH HOH I . 
PA 5 HOH 18  767  767  HOH HOH I . 
PA 5 HOH 19  771  771  HOH HOH I . 
PA 5 HOH 20  781  781  HOH HOH I . 
PA 5 HOH 21  786  786  HOH HOH I . 
PA 5 HOH 22  824  824  HOH HOH I . 
PA 5 HOH 23  854  854  HOH HOH I . 
PA 5 HOH 24  876  876  HOH HOH I . 
PA 5 HOH 25  921  921  HOH HOH I . 
PA 5 HOH 26  922  922  HOH HOH I . 
PA 5 HOH 27  938  938  HOH HOH I . 
PA 5 HOH 28  960  960  HOH HOH I . 
PA 5 HOH 29  968  968  HOH HOH I . 
PA 5 HOH 30  969  969  HOH HOH I . 
PA 5 HOH 31  1005 1005 HOH HOH I . 
PA 5 HOH 32  1097 1097 HOH HOH I . 
PA 5 HOH 33  1098 1098 HOH HOH I . 
PA 5 HOH 34  1108 1108 HOH HOH I . 
PA 5 HOH 35  1110 1110 HOH HOH I . 
PA 5 HOH 36  1115 1115 HOH HOH I . 
PA 5 HOH 37  1141 1141 HOH HOH I . 
PA 5 HOH 38  1152 1152 HOH HOH I . 
PA 5 HOH 39  1155 1155 HOH HOH I . 
PA 5 HOH 40  1156 1156 HOH HOH I . 
PA 5 HOH 41  1226 1226 HOH HOH I . 
PA 5 HOH 42  1227 1227 HOH HOH I . 
PA 5 HOH 43  1258 1258 HOH HOH I . 
PA 5 HOH 44  1287 1287 HOH HOH I . 
PA 5 HOH 45  1299 1299 HOH HOH I . 
PA 5 HOH 46  1303 1303 HOH HOH I . 
PA 5 HOH 47  1308 1308 HOH HOH I . 
PA 5 HOH 48  1358 1358 HOH HOH I . 
PA 5 HOH 49  1359 1359 HOH HOH I . 
PA 5 HOH 50  1391 1391 HOH HOH I . 
PA 5 HOH 51  1405 1405 HOH HOH I . 
PA 5 HOH 52  1418 1418 HOH HOH I . 
PA 5 HOH 53  1421 1421 HOH HOH I . 
PA 5 HOH 54  1442 1442 HOH HOH I . 
PA 5 HOH 55  1457 1457 HOH HOH I . 
PA 5 HOH 56  1472 1472 HOH HOH I . 
PA 5 HOH 57  1492 1492 HOH HOH I . 
PA 5 HOH 58  1526 1526 HOH HOH I . 
PA 5 HOH 59  1568 1568 HOH HOH I . 
PA 5 HOH 60  1634 1634 HOH HOH I . 
QA 5 HOH 1   408  408  HOH HOH J . 
QA 5 HOH 2   418  418  HOH HOH J . 
QA 5 HOH 3   428  428  HOH HOH J . 
QA 5 HOH 4   429  429  HOH HOH J . 
QA 5 HOH 5   433  433  HOH HOH J . 
QA 5 HOH 6   442  442  HOH HOH J . 
QA 5 HOH 7   515  515  HOH HOH J . 
QA 5 HOH 8   527  527  HOH HOH J . 
QA 5 HOH 9   529  529  HOH HOH J . 
QA 5 HOH 10  568  568  HOH HOH J . 
QA 5 HOH 11  578  578  HOH HOH J . 
QA 5 HOH 12  601  601  HOH HOH J . 
QA 5 HOH 13  610  610  HOH HOH J . 
QA 5 HOH 14  627  627  HOH HOH J . 
QA 5 HOH 15  654  654  HOH HOH J . 
QA 5 HOH 16  661  661  HOH HOH J . 
QA 5 HOH 17  671  671  HOH HOH J . 
QA 5 HOH 18  684  684  HOH HOH J . 
QA 5 HOH 19  705  705  HOH HOH J . 
QA 5 HOH 20  707  707  HOH HOH J . 
QA 5 HOH 21  720  720  HOH HOH J . 
QA 5 HOH 22  725  725  HOH HOH J . 
QA 5 HOH 23  743  743  HOH HOH J . 
QA 5 HOH 24  756  756  HOH HOH J . 
QA 5 HOH 25  782  782  HOH HOH J . 
QA 5 HOH 26  789  789  HOH HOH J . 
QA 5 HOH 27  818  818  HOH HOH J . 
QA 5 HOH 28  831  831  HOH HOH J . 
QA 5 HOH 29  837  837  HOH HOH J . 
QA 5 HOH 30  866  866  HOH HOH J . 
QA 5 HOH 31  870  870  HOH HOH J . 
QA 5 HOH 32  894  894  HOH HOH J . 
QA 5 HOH 33  939  939  HOH HOH J . 
QA 5 HOH 34  940  940  HOH HOH J . 
QA 5 HOH 35  941  941  HOH HOH J . 
QA 5 HOH 36  951  951  HOH HOH J . 
QA 5 HOH 37  952  952  HOH HOH J . 
QA 5 HOH 38  957  957  HOH HOH J . 
QA 5 HOH 39  958  958  HOH HOH J . 
QA 5 HOH 40  959  959  HOH HOH J . 
QA 5 HOH 41  1014 1014 HOH HOH J . 
QA 5 HOH 42  1015 1015 HOH HOH J . 
QA 5 HOH 43  1038 1038 HOH HOH J . 
QA 5 HOH 44  1039 1039 HOH HOH J . 
QA 5 HOH 45  1040 1040 HOH HOH J . 
QA 5 HOH 46  1044 1044 HOH HOH J . 
QA 5 HOH 47  1045 1045 HOH HOH J . 
QA 5 HOH 48  1046 1046 HOH HOH J . 
QA 5 HOH 49  1047 1047 HOH HOH J . 
QA 5 HOH 50  1048 1048 HOH HOH J . 
QA 5 HOH 51  1049 1049 HOH HOH J . 
QA 5 HOH 52  1054 1054 HOH HOH J . 
QA 5 HOH 53  1109 1109 HOH HOH J . 
QA 5 HOH 54  1111 1111 HOH HOH J . 
QA 5 HOH 55  1112 1112 HOH HOH J . 
QA 5 HOH 56  1113 1113 HOH HOH J . 
QA 5 HOH 57  1114 1114 HOH HOH J . 
QA 5 HOH 58  1116 1116 HOH HOH J . 
QA 5 HOH 59  1117 1117 HOH HOH J . 
QA 5 HOH 60  1118 1118 HOH HOH J . 
QA 5 HOH 61  1119 1119 HOH HOH J . 
QA 5 HOH 62  1120 1120 HOH HOH J . 
QA 5 HOH 63  1121 1121 HOH HOH J . 
QA 5 HOH 64  1122 1122 HOH HOH J . 
QA 5 HOH 65  1125 1125 HOH HOH J . 
QA 5 HOH 66  1126 1126 HOH HOH J . 
QA 5 HOH 67  1149 1149 HOH HOH J . 
QA 5 HOH 68  1175 1175 HOH HOH J . 
QA 5 HOH 69  1180 1180 HOH HOH J . 
QA 5 HOH 70  1181 1181 HOH HOH J . 
QA 5 HOH 71  1186 1186 HOH HOH J . 
QA 5 HOH 72  1190 1190 HOH HOH J . 
QA 5 HOH 73  1202 1202 HOH HOH J . 
QA 5 HOH 74  1203 1203 HOH HOH J . 
QA 5 HOH 75  1207 1207 HOH HOH J . 
QA 5 HOH 76  1208 1208 HOH HOH J . 
QA 5 HOH 77  1220 1220 HOH HOH J . 
QA 5 HOH 78  1221 1221 HOH HOH J . 
QA 5 HOH 79  1222 1222 HOH HOH J . 
QA 5 HOH 80  1225 1225 HOH HOH J . 
QA 5 HOH 81  1228 1228 HOH HOH J . 
QA 5 HOH 82  1238 1238 HOH HOH J . 
QA 5 HOH 83  1257 1257 HOH HOH J . 
QA 5 HOH 84  1268 1268 HOH HOH J . 
QA 5 HOH 85  1276 1276 HOH HOH J . 
QA 5 HOH 86  1293 1293 HOH HOH J . 
QA 5 HOH 87  1360 1360 HOH HOH J . 
QA 5 HOH 88  1361 1361 HOH HOH J . 
QA 5 HOH 89  1371 1371 HOH HOH J . 
QA 5 HOH 90  1376 1376 HOH HOH J . 
QA 5 HOH 91  1390 1390 HOH HOH J . 
QA 5 HOH 92  1395 1395 HOH HOH J . 
QA 5 HOH 93  1397 1397 HOH HOH J . 
QA 5 HOH 94  1402 1402 HOH HOH J . 
QA 5 HOH 95  1409 1409 HOH HOH J . 
QA 5 HOH 96  1425 1425 HOH HOH J . 
QA 5 HOH 97  1433 1433 HOH HOH J . 
QA 5 HOH 98  1446 1446 HOH HOH J . 
QA 5 HOH 99  1468 1468 HOH HOH J . 
QA 5 HOH 100 1470 1470 HOH HOH J . 
QA 5 HOH 101 1481 1481 HOH HOH J . 
QA 5 HOH 102 1482 1482 HOH HOH J . 
QA 5 HOH 103 1483 1483 HOH HOH J . 
QA 5 HOH 104 1511 1511 HOH HOH J . 
# 
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 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,K,L,M,N,O,HA,IA         
2 1 C,D,P,Q,R,S,JA,KA           
3 1 E,F,T,U,V,W,LA,MA           
4 1 G,H,X,Y,Z,AA,NA,OA          
5 1 I,J,BA,CA,DA,EA,FA,GA,PA,QA 
# 
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)' 1430  ? 
1 MORE         -11   ? 
1 'SSA (A^2)'  13730 ? 
2 'ABSA (A^2)' 1560  ? 
2 MORE         -17   ? 
2 'SSA (A^2)'  13920 ? 
3 'ABSA (A^2)' 1390  ? 
3 MORE         -11   ? 
3 'SSA (A^2)'  13700 ? 
4 'ABSA (A^2)' 1540  ? 
4 MORE         -20   ? 
4 'SSA (A^2)'  13800 ? 
5 'ABSA (A^2)' 1540  ? 
5 MORE         -21   ? 
5 'SSA (A^2)'  13660 ? 
# 
_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 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    D 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     1252 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   KA 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
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 ? A ASP 83 ? A ASP 83 ? 1_555 ZN ? L  ZN  . ? A ZN  201 ? 1_555 ND1 ? A HIS 63  ? A HIS 63  ? 1_555 103.3 ? 
2   OD1 ? A ASP 83 ? A ASP 83 ? 1_555 ZN ? L  ZN  . ? A ZN  201 ? 1_555 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 96.0  ? 
3   ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? L  ZN  . ? A ZN  201 ? 1_555 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 102.0 ? 
4   OD1 ? A ASP 83 ? A ASP 83 ? 1_555 ZN ? L  ZN  . ? A ZN  201 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 120.2 ? 
5   ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? L  ZN  . ? A ZN  201 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 109.1 ? 
6   ND1 ? A HIS 71 ? A HIS 71 ? 1_555 ZN ? L  ZN  . ? A ZN  201 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 123.3 ? 
7   OD1 ? A ASP 83 ? A ASP 83 ? 1_555 ZN ? L  ZN  . ? A ZN  201 ? 1_555 OD2 ? A ASP 83  ? A ASP 83  ? 1_555 52.3  ? 
8   ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? L  ZN  . ? A ZN  201 ? 1_555 OD2 ? A ASP 83  ? A ASP 83  ? 1_555 155.0 ? 
9   ND1 ? A HIS 71 ? A HIS 71 ? 1_555 ZN ? L  ZN  . ? A ZN  201 ? 1_555 OD2 ? A ASP 83  ? A ASP 83  ? 1_555 78.4  ? 
10  ND1 ? A HIS 80 ? A HIS 80 ? 1_555 ZN ? L  ZN  . ? A ZN  201 ? 1_555 OD2 ? A ASP 83  ? A ASP 83  ? 1_555 90.6  ? 
11  ND1 ? A HIS 46 ? A HIS 46 ? 1_555 CU ? K  CU1 . ? A CU1 200 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 135.1 ? 
12  ND1 ? A HIS 46 ? A HIS 46 ? 1_555 CU ? K  CU1 . ? A CU1 200 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 104.3 ? 
13  NE2 ? A HIS 48 ? A HIS 48 ? 1_555 CU ? K  CU1 . ? A CU1 200 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 120.2 ? 
14  OD1 ? B ASP 83 ? B ASP 83 ? 1_555 ZN ? N  ZN  . ? B ZN  201 ? 1_555 ND1 ? B HIS 63  ? B HIS 63  ? 1_555 105.8 ? 
15  OD1 ? B ASP 83 ? B ASP 83 ? 1_555 ZN ? N  ZN  . ? B ZN  201 ? 1_555 ND1 ? B HIS 71  ? B HIS 71  ? 1_555 102.1 ? 
16  ND1 ? B HIS 63 ? B HIS 63 ? 1_555 ZN ? N  ZN  . ? B ZN  201 ? 1_555 ND1 ? B HIS 71  ? B HIS 71  ? 1_555 106.4 ? 
17  OD1 ? B ASP 83 ? B ASP 83 ? 1_555 ZN ? N  ZN  . ? B ZN  201 ? 1_555 ND1 ? B HIS 80  ? B HIS 80  ? 1_555 112.4 ? 
18  ND1 ? B HIS 63 ? B HIS 63 ? 1_555 ZN ? N  ZN  . ? B ZN  201 ? 1_555 ND1 ? B HIS 80  ? B HIS 80  ? 1_555 108.2 ? 
19  ND1 ? B HIS 71 ? B HIS 71 ? 1_555 ZN ? N  ZN  . ? B ZN  201 ? 1_555 ND1 ? B HIS 80  ? B HIS 80  ? 1_555 120.9 ? 
20  ND1 ? B HIS 46 ? B HIS 46 ? 1_555 CU ? M  CU1 . ? B CU1 200 ? 1_555 NE2 ? B HIS 48  ? B HIS 48  ? 1_555 137.4 ? 
21  ND1 ? B HIS 46 ? B HIS 46 ? 1_555 CU ? M  CU1 . ? B CU1 200 ? 1_555 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 98.5  ? 
22  NE2 ? B HIS 48 ? B HIS 48 ? 1_555 CU ? M  CU1 . ? B CU1 200 ? 1_555 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 124.0 ? 
23  OD1 ? C ASP 83 ? C ASP 83 ? 1_555 ZN ? Q  ZN  . ? C ZN  201 ? 1_555 ND1 ? C HIS 63  ? C HIS 63  ? 1_555 90.7  ? 
24  OD1 ? C ASP 83 ? C ASP 83 ? 1_555 ZN ? Q  ZN  . ? C ZN  201 ? 1_555 ND1 ? C HIS 71  ? C HIS 71  ? 1_555 95.5  ? 
25  ND1 ? C HIS 63 ? C HIS 63 ? 1_555 ZN ? Q  ZN  . ? C ZN  201 ? 1_555 ND1 ? C HIS 71  ? C HIS 71  ? 1_555 103.9 ? 
26  OD1 ? C ASP 83 ? C ASP 83 ? 1_555 ZN ? Q  ZN  . ? C ZN  201 ? 1_555 ND1 ? C HIS 80  ? C HIS 80  ? 1_555 117.5 ? 
27  ND1 ? C HIS 63 ? C HIS 63 ? 1_555 ZN ? Q  ZN  . ? C ZN  201 ? 1_555 ND1 ? C HIS 80  ? C HIS 80  ? 1_555 116.4 ? 
28  ND1 ? C HIS 71 ? C HIS 71 ? 1_555 ZN ? Q  ZN  . ? C ZN  201 ? 1_555 ND1 ? C HIS 80  ? C HIS 80  ? 1_555 125.8 ? 
29  OD1 ? C ASP 83 ? C ASP 83 ? 1_555 ZN ? Q  ZN  . ? C ZN  201 ? 1_555 OD2 ? C ASP 83  ? C ASP 83  ? 1_555 54.6  ? 
30  ND1 ? C HIS 63 ? C HIS 63 ? 1_555 ZN ? Q  ZN  . ? C ZN  201 ? 1_555 OD2 ? C ASP 83  ? C ASP 83  ? 1_555 143.7 ? 
31  ND1 ? C HIS 71 ? C HIS 71 ? 1_555 ZN ? Q  ZN  . ? C ZN  201 ? 1_555 OD2 ? C ASP 83  ? C ASP 83  ? 1_555 72.8  ? 
32  ND1 ? C HIS 80 ? C HIS 80 ? 1_555 ZN ? Q  ZN  . ? C ZN  201 ? 1_555 OD2 ? C ASP 83  ? C ASP 83  ? 1_555 92.0  ? 
33  ND1 ? C HIS 46 ? C HIS 46 ? 1_555 CU ? P  CU1 . ? C CU1 200 ? 1_555 NE2 ? C HIS 48  ? C HIS 48  ? 1_555 141.6 ? 
34  ND1 ? C HIS 46 ? C HIS 46 ? 1_555 CU ? P  CU1 . ? C CU1 200 ? 1_555 NE2 ? C HIS 120 ? C HIS 120 ? 1_555 99.5  ? 
35  NE2 ? C HIS 48 ? C HIS 48 ? 1_555 CU ? P  CU1 . ? C CU1 200 ? 1_555 NE2 ? C HIS 120 ? C HIS 120 ? 1_555 118.8 ? 
36  OD1 ? D ASP 83 ? D ASP 83 ? 1_555 ZN ? S  ZN  . ? D ZN  201 ? 1_555 ND1 ? D HIS 63  ? D HIS 63  ? 1_555 104.6 ? 
37  OD1 ? D ASP 83 ? D ASP 83 ? 1_555 ZN ? S  ZN  . ? D ZN  201 ? 1_555 ND1 ? D HIS 71  ? D HIS 71  ? 1_555 99.5  ? 
38  ND1 ? D HIS 63 ? D HIS 63 ? 1_555 ZN ? S  ZN  . ? D ZN  201 ? 1_555 ND1 ? D HIS 71  ? D HIS 71  ? 1_555 106.0 ? 
39  OD1 ? D ASP 83 ? D ASP 83 ? 1_555 ZN ? S  ZN  . ? D ZN  201 ? 1_555 ND1 ? D HIS 80  ? D HIS 80  ? 1_555 117.3 ? 
40  ND1 ? D HIS 63 ? D HIS 63 ? 1_555 ZN ? S  ZN  . ? D ZN  201 ? 1_555 ND1 ? D HIS 80  ? D HIS 80  ? 1_555 108.7 ? 
41  ND1 ? D HIS 71 ? D HIS 71 ? 1_555 ZN ? S  ZN  . ? D ZN  201 ? 1_555 ND1 ? D HIS 80  ? D HIS 80  ? 1_555 119.3 ? 
42  ND1 ? D HIS 46 ? D HIS 46 ? 1_555 CU ? R  CU1 . ? D CU1 200 ? 1_555 NE2 ? D HIS 48  ? D HIS 48  ? 1_555 141.5 ? 
43  ND1 ? D HIS 46 ? D HIS 46 ? 1_555 CU ? R  CU1 . ? D CU1 200 ? 1_555 NE2 ? D HIS 120 ? D HIS 120 ? 1_555 99.9  ? 
44  NE2 ? D HIS 48 ? D HIS 48 ? 1_555 CU ? R  CU1 . ? D CU1 200 ? 1_555 NE2 ? D HIS 120 ? D HIS 120 ? 1_555 118.4 ? 
45  OD1 ? E ASP 83 ? E ASP 83 ? 1_555 ZN ? U  ZN  . ? E ZN  201 ? 1_555 ND1 ? E HIS 63  ? E HIS 63  ? 1_555 104.1 ? 
46  OD1 ? E ASP 83 ? E ASP 83 ? 1_555 ZN ? U  ZN  . ? E ZN  201 ? 1_555 ND1 ? E HIS 71  ? E HIS 71  ? 1_555 96.1  ? 
47  ND1 ? E HIS 63 ? E HIS 63 ? 1_555 ZN ? U  ZN  . ? E ZN  201 ? 1_555 ND1 ? E HIS 71  ? E HIS 71  ? 1_555 106.1 ? 
48  OD1 ? E ASP 83 ? E ASP 83 ? 1_555 ZN ? U  ZN  . ? E ZN  201 ? 1_555 ND1 ? E HIS 80  ? E HIS 80  ? 1_555 114.7 ? 
49  ND1 ? E HIS 63 ? E HIS 63 ? 1_555 ZN ? U  ZN  . ? E ZN  201 ? 1_555 ND1 ? E HIS 80  ? E HIS 80  ? 1_555 112.1 ? 
50  ND1 ? E HIS 71 ? E HIS 71 ? 1_555 ZN ? U  ZN  . ? E ZN  201 ? 1_555 ND1 ? E HIS 80  ? E HIS 80  ? 1_555 121.5 ? 
51  ND1 ? E HIS 46 ? E HIS 46 ? 1_555 CU ? T  CU1 . ? E CU1 200 ? 1_555 NE2 ? E HIS 48  ? E HIS 48  ? 1_555 141.2 ? 
52  ND1 ? E HIS 46 ? E HIS 46 ? 1_555 CU ? T  CU1 . ? E CU1 200 ? 1_555 NE2 ? E HIS 120 ? E HIS 120 ? 1_555 98.8  ? 
53  NE2 ? E HIS 48 ? E HIS 48 ? 1_555 CU ? T  CU1 . ? E CU1 200 ? 1_555 NE2 ? E HIS 120 ? E HIS 120 ? 1_555 119.4 ? 
54  OD1 ? F ASP 83 ? F ASP 83 ? 1_555 ZN ? W  ZN  . ? F ZN  201 ? 1_555 ND1 ? F HIS 63  ? F HIS 63  ? 1_555 102.7 ? 
55  OD1 ? F ASP 83 ? F ASP 83 ? 1_555 ZN ? W  ZN  . ? F ZN  201 ? 1_555 ND1 ? F HIS 71  ? F HIS 71  ? 1_555 100.7 ? 
56  ND1 ? F HIS 63 ? F HIS 63 ? 1_555 ZN ? W  ZN  . ? F ZN  201 ? 1_555 ND1 ? F HIS 71  ? F HIS 71  ? 1_555 104.9 ? 
57  OD1 ? F ASP 83 ? F ASP 83 ? 1_555 ZN ? W  ZN  . ? F ZN  201 ? 1_555 ND1 ? F HIS 80  ? F HIS 80  ? 1_555 112.9 ? 
58  ND1 ? F HIS 63 ? F HIS 63 ? 1_555 ZN ? W  ZN  . ? F ZN  201 ? 1_555 ND1 ? F HIS 80  ? F HIS 80  ? 1_555 112.2 ? 
59  ND1 ? F HIS 71 ? F HIS 71 ? 1_555 ZN ? W  ZN  . ? F ZN  201 ? 1_555 ND1 ? F HIS 80  ? F HIS 80  ? 1_555 121.3 ? 
60  ND1 ? F HIS 46 ? F HIS 46 ? 1_555 CU ? V  CU1 . ? F CU1 200 ? 1_555 NE2 ? F HIS 48  ? F HIS 48  ? 1_555 139.2 ? 
61  ND1 ? F HIS 46 ? F HIS 46 ? 1_555 CU ? V  CU1 . ? F CU1 200 ? 1_555 NE2 ? F HIS 120 ? F HIS 120 ? 1_555 98.5  ? 
62  NE2 ? F HIS 48 ? F HIS 48 ? 1_555 CU ? V  CU1 . ? F CU1 200 ? 1_555 NE2 ? F HIS 120 ? F HIS 120 ? 1_555 122.0 ? 
63  OD1 ? G ASP 83 ? G ASP 83 ? 1_555 ZN ? Y  ZN  . ? G ZN  201 ? 1_555 ND1 ? G HIS 63  ? G HIS 63  ? 1_555 104.9 ? 
64  OD1 ? G ASP 83 ? G ASP 83 ? 1_555 ZN ? Y  ZN  . ? G ZN  201 ? 1_555 ND1 ? G HIS 71  ? G HIS 71  ? 1_555 98.2  ? 
65  ND1 ? G HIS 63 ? G HIS 63 ? 1_555 ZN ? Y  ZN  . ? G ZN  201 ? 1_555 ND1 ? G HIS 71  ? G HIS 71  ? 1_555 101.0 ? 
66  OD1 ? G ASP 83 ? G ASP 83 ? 1_555 ZN ? Y  ZN  . ? G ZN  201 ? 1_555 ND1 ? G HIS 80  ? G HIS 80  ? 1_555 119.7 ? 
67  ND1 ? G HIS 63 ? G HIS 63 ? 1_555 ZN ? Y  ZN  . ? G ZN  201 ? 1_555 ND1 ? G HIS 80  ? G HIS 80  ? 1_555 109.6 ? 
68  ND1 ? G HIS 71 ? G HIS 71 ? 1_555 ZN ? Y  ZN  . ? G ZN  201 ? 1_555 ND1 ? G HIS 80  ? G HIS 80  ? 1_555 120.9 ? 
69  OD1 ? G ASP 83 ? G ASP 83 ? 1_555 ZN ? Y  ZN  . ? G ZN  201 ? 1_555 OD2 ? G ASP 83  ? G ASP 83  ? 1_555 52.7  ? 
70  ND1 ? G HIS 63 ? G HIS 63 ? 1_555 ZN ? Y  ZN  . ? G ZN  201 ? 1_555 OD2 ? G ASP 83  ? G ASP 83  ? 1_555 157.3 ? 
71  ND1 ? G HIS 71 ? G HIS 71 ? 1_555 ZN ? Y  ZN  . ? G ZN  201 ? 1_555 OD2 ? G ASP 83  ? G ASP 83  ? 1_555 81.1  ? 
72  ND1 ? G HIS 80 ? G HIS 80 ? 1_555 ZN ? Y  ZN  . ? G ZN  201 ? 1_555 OD2 ? G ASP 83  ? G ASP 83  ? 1_555 87.8  ? 
73  ND1 ? G HIS 46 ? G HIS 46 ? 1_555 CU ? X  CU1 . ? G CU1 200 ? 1_555 NE2 ? G HIS 48  ? G HIS 48  ? 1_555 138.2 ? 
74  ND1 ? G HIS 46 ? G HIS 46 ? 1_555 CU ? X  CU1 . ? G CU1 200 ? 1_555 NE2 ? G HIS 120 ? G HIS 120 ? 1_555 103.0 ? 
75  NE2 ? G HIS 48 ? G HIS 48 ? 1_555 CU ? X  CU1 . ? G CU1 200 ? 1_555 NE2 ? G HIS 120 ? G HIS 120 ? 1_555 117.1 ? 
76  OD1 ? H ASP 83 ? H ASP 83 ? 1_555 ZN ? AA ZN  . ? H ZN  201 ? 1_555 ND1 ? H HIS 63  ? H HIS 63  ? 1_555 104.0 ? 
77  OD1 ? H ASP 83 ? H ASP 83 ? 1_555 ZN ? AA ZN  . ? H ZN  201 ? 1_555 ND1 ? H HIS 71  ? H HIS 71  ? 1_555 103.3 ? 
78  ND1 ? H HIS 63 ? H HIS 63 ? 1_555 ZN ? AA ZN  . ? H ZN  201 ? 1_555 ND1 ? H HIS 71  ? H HIS 71  ? 1_555 105.4 ? 
79  OD1 ? H ASP 83 ? H ASP 83 ? 1_555 ZN ? AA ZN  . ? H ZN  201 ? 1_555 ND1 ? H HIS 80  ? H HIS 80  ? 1_555 115.9 ? 
80  ND1 ? H HIS 63 ? H HIS 63 ? 1_555 ZN ? AA ZN  . ? H ZN  201 ? 1_555 ND1 ? H HIS 80  ? H HIS 80  ? 1_555 107.9 ? 
81  ND1 ? H HIS 71 ? H HIS 71 ? 1_555 ZN ? AA ZN  . ? H ZN  201 ? 1_555 ND1 ? H HIS 80  ? H HIS 80  ? 1_555 119.0 ? 
82  ND1 ? H HIS 46 ? H HIS 46 ? 1_555 CU ? Z  CU1 . ? H CU1 200 ? 1_555 NE2 ? H HIS 48  ? H HIS 48  ? 1_555 137.1 ? 
83  ND1 ? H HIS 46 ? H HIS 46 ? 1_555 CU ? Z  CU1 . ? H CU1 200 ? 1_555 NE2 ? H HIS 120 ? H HIS 120 ? 1_555 104.9 ? 
84  NE2 ? H HIS 48 ? H HIS 48 ? 1_555 CU ? Z  CU1 . ? H CU1 200 ? 1_555 NE2 ? H HIS 120 ? H HIS 120 ? 1_555 117.8 ? 
85  OD1 ? I ASP 83 ? I ASP 83 ? 1_555 ZN ? CA ZN  . ? I ZN  201 ? 1_555 ND1 ? I HIS 63  ? I HIS 63  ? 1_555 101.2 ? 
86  OD1 ? I ASP 83 ? I ASP 83 ? 1_555 ZN ? CA ZN  . ? I ZN  201 ? 1_555 ND1 ? I HIS 71  ? I HIS 71  ? 1_555 99.2  ? 
87  ND1 ? I HIS 63 ? I HIS 63 ? 1_555 ZN ? CA ZN  . ? I ZN  201 ? 1_555 ND1 ? I HIS 71  ? I HIS 71  ? 1_555 109.9 ? 
88  OD1 ? I ASP 83 ? I ASP 83 ? 1_555 ZN ? CA ZN  . ? I ZN  201 ? 1_555 ND1 ? I HIS 80  ? I HIS 80  ? 1_555 117.0 ? 
89  ND1 ? I HIS 63 ? I HIS 63 ? 1_555 ZN ? CA ZN  . ? I ZN  201 ? 1_555 ND1 ? I HIS 80  ? I HIS 80  ? 1_555 109.4 ? 
90  ND1 ? I HIS 71 ? I HIS 71 ? 1_555 ZN ? CA ZN  . ? I ZN  201 ? 1_555 ND1 ? I HIS 80  ? I HIS 80  ? 1_555 118.5 ? 
91  OD1 ? I ASP 83 ? I ASP 83 ? 1_555 ZN ? CA ZN  . ? I ZN  201 ? 1_555 OD2 ? I ASP 83  ? I ASP 83  ? 1_555 54.5  ? 
92  ND1 ? I HIS 63 ? I HIS 63 ? 1_555 ZN ? CA ZN  . ? I ZN  201 ? 1_555 OD2 ? I ASP 83  ? I ASP 83  ? 1_555 155.7 ? 
93  ND1 ? I HIS 71 ? I HIS 71 ? 1_555 ZN ? CA ZN  . ? I ZN  201 ? 1_555 OD2 ? I ASP 83  ? I ASP 83  ? 1_555 76.6  ? 
94  ND1 ? I HIS 80 ? I HIS 80 ? 1_555 ZN ? CA ZN  . ? I ZN  201 ? 1_555 OD2 ? I ASP 83  ? I ASP 83  ? 1_555 85.9  ? 
95  ND1 ? I HIS 46 ? I HIS 46 ? 1_555 CU ? BA CU1 . ? I CU1 200 ? 1_555 NE2 ? I HIS 48  ? I HIS 48  ? 1_555 137.5 ? 
96  ND1 ? I HIS 46 ? I HIS 46 ? 1_555 CU ? BA CU1 . ? I CU1 200 ? 1_555 NE2 ? I HIS 120 ? I HIS 120 ? 1_555 98.4  ? 
97  NE2 ? I HIS 48 ? I HIS 48 ? 1_555 CU ? BA CU1 . ? I CU1 200 ? 1_555 NE2 ? I HIS 120 ? I HIS 120 ? 1_555 123.5 ? 
98  OD1 ? J ASP 83 ? J ASP 83 ? 1_555 ZN ? EA ZN  . ? J ZN  201 ? 1_555 ND1 ? J HIS 63  ? J HIS 63  ? 1_555 105.8 ? 
99  OD1 ? J ASP 83 ? J ASP 83 ? 1_555 ZN ? EA ZN  . ? J ZN  201 ? 1_555 ND1 ? J HIS 71  ? J HIS 71  ? 1_555 97.3  ? 
100 ND1 ? J HIS 63 ? J HIS 63 ? 1_555 ZN ? EA ZN  . ? J ZN  201 ? 1_555 ND1 ? J HIS 71  ? J HIS 71  ? 1_555 103.3 ? 
101 OD1 ? J ASP 83 ? J ASP 83 ? 1_555 ZN ? EA ZN  . ? J ZN  201 ? 1_555 ND1 ? J HIS 80  ? J HIS 80  ? 1_555 116.1 ? 
102 ND1 ? J HIS 63 ? J HIS 63 ? 1_555 ZN ? EA ZN  . ? J ZN  201 ? 1_555 ND1 ? J HIS 80  ? J HIS 80  ? 1_555 110.9 ? 
103 ND1 ? J HIS 71 ? J HIS 71 ? 1_555 ZN ? EA ZN  . ? J ZN  201 ? 1_555 ND1 ? J HIS 80  ? J HIS 80  ? 1_555 121.4 ? 
104 ND1 ? J HIS 46 ? J HIS 46 ? 1_555 CU ? DA CU1 . ? J CU1 200 ? 1_555 NE2 ? J HIS 48  ? J HIS 48  ? 1_555 141.2 ? 
105 ND1 ? J HIS 46 ? J HIS 46 ? 1_555 CU ? DA CU1 . ? J CU1 200 ? 1_555 NE2 ? J HIS 120 ? J HIS 120 ? 1_555 100.0 ? 
106 NE2 ? J HIS 48 ? J HIS 48 ? 1_555 CU ? DA CU1 . ? J CU1 200 ? 1_555 NE2 ? J HIS 120 ? J HIS 120 ? 1_555 118.6 ? 
# 
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 2003-09-09 
2 'Structure model' 1 1 2008-04-29 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2017-10-11 
# 
_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         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' 'Refinement description'    
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    4 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            software 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 4 'Structure model' '_software.classification' 
2 4 'Structure model' '_software.name'           
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
AMoRE     phasing           . ? 1 
SHELXL-97 refinement        . ? 2 
MAR345    'data collection' . ? 3 
SCALEPACK 'data scaling'    . ? 4 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 NE B ARG 115 ? ? CZ B ARG 115 ? ? NH2 B ARG 115 ? ? 125.28 120.30 4.98  0.50 N 
2 1 NE D ARG 115 ? ? CZ D ARG 115 ? ? NH1 D ARG 115 ? ? 116.93 120.30 -3.37 0.50 N 
3 1 NE D ARG 115 ? ? CZ D ARG 115 ? ? NH2 D ARG 115 ? ? 124.01 120.30 3.71  0.50 N 
4 1 CB D ASP 125 ? ? CG D ASP 125 ? ? OD2 D ASP 125 ? ? 123.85 118.30 5.55  0.90 N 
5 1 NE E ARG 115 ? ? CZ E ARG 115 ? ? NH1 E ARG 115 ? ? 116.76 120.30 -3.54 0.50 N 
6 1 NE E ARG 115 ? ? CZ E ARG 115 ? ? NH2 E ARG 115 ? ? 124.50 120.30 4.20  0.50 N 
7 1 NE H ARG 79  ? ? CZ H ARG 79  ? ? NH1 H ARG 79  ? ? 115.24 120.30 -5.06 0.50 N 
8 1 NE H ARG 79  ? ? CZ H ARG 79  ? ? NH2 H ARG 79  ? ? 123.53 120.30 3.23  0.50 N 
9 1 NE H ARG 143 ? ? CZ H ARG 143 ? ? NH2 H ARG 143 ? ? 123.91 120.30 3.61  0.50 N 
# 
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 SER B 25  ? ? -12.70  -65.22  
2  1 SER C 68  ? ? 35.01   54.69   
3  1 ARG C 69  ? ? -99.94  -142.04 
4  1 LYS C 128 ? ? -105.53 51.73   
5  1 ALA D 55  ? ? -119.22 53.26   
6  1 SER G 25  ? ? -14.18  -63.84  
7  1 SER G 98  ? ? -152.82 84.12   
8  1 GLU G 132 ? ? -39.00  -27.30  
9  1 LYS I 136 ? ? -90.98  -64.67  
10 1 ARG J 115 ? ? -102.20 -169.98 
# 
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 
# 
