data_2GBT
# 
_entry.id   2GBT 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.351 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   2GBT         pdb_00002gbt 10.2210/pdb2gbt/pdb 
RCSB  RCSB036930   ?            ?                   
WWPDB D_1000036930 ?            ?                   
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.details 
_pdbx_database_related.content_type 
PDB 1HL4 'apo CuZn Superoxide dismutase'                       unspecified 
PDB 2GBU 'C6A/C111A/C57A/C146A apo CuZn Superoxide dismutase'  unspecified 
PDB 2GBV 'C6A/C111A/C57A/C146A holo CuZn Superoxide dismutase' unspecified 
# 
_pdbx_database_status.entry_id                        2GBT 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.recvd_initial_deposition_date   2006-03-11 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Hornberg, A.'   1 
'Logan, D.T.'    2 
'Marklund, S.L.' 3 
'Oliveberg, M.'  4 
# 
_citation.id                        primary 
_citation.title                     
'The Coupling between Disulphide Status, Metallation and Dimer Interface Strength in Cu/Zn Superoxide Dismutase' 
_citation.journal_abbrev            J.Mol.Biol. 
_citation.journal_volume            365 
_citation.page_first                333 
_citation.page_last                 342 
_citation.year                      2007 
_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   17070542 
_citation.pdbx_database_id_DOI      10.1016/j.jmb.2006.09.048 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Hornberg, A.'   1 ? 
primary 'Logan, D.T.'    2 ? 
primary 'Marklund, S.L.' 3 ? 
primary 'Oliveberg, M.'  4 ? 
# 
_cell.length_a           156.618 
_cell.length_b           35.257 
_cell.length_c           114.971 
_cell.angle_alpha        90.00 
_cell.angle_beta         112.17 
_cell.angle_gamma        90.00 
_cell.entry_id           2GBT 
_cell.pdbx_unique_axis   ? 
_cell.Z_PDB              16 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.entry_id                         2GBT 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.Int_Tables_number                5 
_symmetry.cell_setting                     ? 
_symmetry.space_group_name_Hall            ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Superoxide dismutase [Cu-Zn]' 15763.430 4   1.15.1.1 C6A/C111A ? ? 
2 non-polymer syn 'COPPER (I) ION'               63.546    2   ?        ?         ? ? 
3 non-polymer syn 'ZINC ION'                     65.409    2   ?        ?         ? ? 
4 water       nat water                          18.015    537 ?        ?         ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Cu/Zn superoxide dismutase' 
# 
_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       
;ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHAIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHAIIGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B,C,D 
_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   ALA 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 ALA 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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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                   'Escherichia coli' 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               BL21/DE3 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       pACA 
_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 2GBT A 1 ? 153 ? P00441 1 ? 153 ? 1 153 
2 1 2GBT B 1 ? 153 ? P00441 1 ? 153 ? 1 153 
3 1 2GBT C 1 ? 153 ? P00441 1 ? 153 ? 1 153 
4 1 2GBT D 1 ? 153 ? P00441 1 ? 153 ? 1 153 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 2GBT ALA A 6   ? UNP P00441 CYS 6   'engineered mutation' 6   1 
1 2GBT ALA A 111 ? UNP P00441 CYS 111 'engineered mutation' 111 2 
2 2GBT ALA B 6   ? UNP P00441 CYS 6   'engineered mutation' 6   3 
2 2GBT ALA B 111 ? UNP P00441 CYS 111 'engineered mutation' 111 4 
3 2GBT ALA C 6   ? UNP P00441 CYS 6   'engineered mutation' 6   5 
3 2GBT ALA C 111 ? UNP P00441 CYS 111 'engineered mutation' 111 6 
4 2GBT ALA D 6   ? UNP P00441 CYS 6   'engineered mutation' 6   7 
4 2GBT ALA D 111 ? UNP P00441 CYS 111 'engineered mutation' 111 8 
# 
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 
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          2GBT 
_exptl.crystals_number   1 
_exptl.method            'X-RAY DIFFRACTION' 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.33 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_percent_sol   47.22 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              7.5 
_exptl_crystal_grow.temp            291 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pdbx_details    
'18% PEG8000, 50mM TRIS-HCL, 50mM NaAc, 1mM EDTA, pH 7.5, VAPOR DIFFUSION, HANGING DROP, temperature 291K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   2004-06-20 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.monochromator                    'SI 111 CHANNEL' 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.092 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'MAX II BEAMLINE I711' 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.092 
_diffrn_source.pdbx_synchrotron_site       'MAX II' 
_diffrn_source.pdbx_synchrotron_beamline   I711 
# 
_reflns.entry_id                     2GBT 
_reflns.observed_criterion_sigma_F   1 
_reflns.observed_criterion_sigma_I   1 
_reflns.d_resolution_high            1.7 
_reflns.d_resolution_low             20 
_reflns.number_all                   64389 
_reflns.number_obs                   64389 
_reflns.percent_possible_obs         99.4 
_reflns.pdbx_Rmerge_I_obs            0.059 
_reflns.pdbx_Rsym_value              ? 
_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_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             1.70 
_reflns_shell.d_res_low              1.79 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.percent_possible_all   99.9 
_reflns_shell.Rmerge_I_obs           0.378 
_reflns_shell.meanI_over_sigI_obs    1.8 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.pdbx_redundancy        ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.number_measured_all    ? 
_reflns_shell.number_measured_obs    ? 
_reflns_shell.number_unique_obs      ? 
_reflns_shell.pdbx_chi_squared       ? 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.pdbx_diffrn_id         1 
# 
_refine.ls_d_res_high                            1.700 
_refine.ls_d_res_low                             20.000 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.ls_percent_reflns_obs                    98.940 
_refine.ls_number_reflns_obs                     64189 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.ls_R_factor_all                          0.204 
_refine.ls_R_factor_R_work                       0.203 
_refine.ls_R_factor_R_free                       0.23 
_refine.ls_percent_reflns_R_free                 5.100 
_refine.ls_number_reflns_R_free                  3249 
_refine.B_iso_mean                               31.885 
_refine.aniso_B[1][1]                            -1.500 
_refine.aniso_B[2][2]                            2.160 
_refine.aniso_B[3][3]                            -1.220 
_refine.aniso_B[1][2]                            0.000 
_refine.aniso_B[1][3]                            -0.730 
_refine.aniso_B[2][3]                            0.000 
_refine.correlation_coeff_Fo_to_Fc               0.957 
_refine.correlation_coeff_Fo_to_Fc_free          0.944 
_refine.pdbx_overall_ESU_R                       0.115 
_refine.pdbx_overall_ESU_R_Free                  0.109 
_refine.overall_SU_ML                            0.098 
_refine.overall_SU_B                             5.979 
_refine.solvent_model_details                    'BABINET MODEL WITH MASK' 
_refine.pdbx_solvent_vdw_probe_radii             1.200 
_refine.pdbx_solvent_ion_probe_radii             0.800 
_refine.pdbx_solvent_shrinkage_radii             0.800 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.entry_id                                 2GBT 
_refine.pdbx_ls_sigma_I                          ? 
_refine.ls_number_reflns_all                     64389 
_refine.ls_R_factor_obs                          0.204 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      1HL4 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_TLS_residual_ADP_flag               'LIKELY RESIDUAL' 
_refine.pdbx_diffrn_id                           1 
_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_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4026 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         4 
_refine_hist.number_atoms_solvent             537 
_refine_hist.number_atoms_total               4567 
_refine_hist.d_res_high                       1.700 
_refine_hist.d_res_low                        20.000 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.number 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d         4094 0.006  0.021  ? 'X-RAY DIFFRACTION' ? 
r_bond_other_d           3650 0.002  0.020  ? 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      5532 1.031  1.941  ? 'X-RAY DIFFRACTION' ? 
r_angle_other_deg        8533 0.673  3.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   546  5.687  5.000  ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   173  37.789 25.491 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   657  10.404 15.000 ? 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   14   10.324 15.000 ? 'X-RAY DIFFRACTION' ? 
r_chiral_restr           621  0.062  0.200  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     4694 0.003  0.020  ? 'X-RAY DIFFRACTION' ? 
r_gen_planes_other       744  0.001  0.020  ? 'X-RAY DIFFRACTION' ? 
r_nbd_refined            637  0.181  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbd_other              3563 0.171  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbtor_refined          1962 0.156  0.200  ? 'X-RAY DIFFRACTION' ? 
r_nbtor_other            2344 0.079  0.200  ? 'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    438  0.113  0.200  ? 'X-RAY DIFFRACTION' ? 
r_metal_ion_refined      6    0.174  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   9    0.080  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other     36   0.182  0.200  ? 'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 14   0.104  0.200  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_it              3547 0.569  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcbond_other           1184 0.090  1.500  ? 'X-RAY DIFFRACTION' ? 
r_mcangle_it             4289 0.677  2.000  ? 'X-RAY DIFFRACTION' ? 
r_scbond_it              1678 1.201  3.000  ? 'X-RAY DIFFRACTION' ? 
r_scangle_it             1243 1.604  4.500  ? 'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.d_res_high                       1.700 
_refine_ls_shell.d_res_low                        1.744 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.percent_reflns_obs               99.150 
_refine_ls_shell.number_reflns_R_work             4458 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_R_work                  0.291 
_refine_ls_shell.R_factor_R_free                  0.323 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             235 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                4693 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  2GBT 
_struct.title                     'C6A/C111A CuZn Superoxide dismutase' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2GBT 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            'OXIDOREDUCTASE, HUMAN CU/ZN SUPEROXIDE DISMUTASE' 
# 
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 2 ? 
F N N 3 ? 
G N N 2 ? 
H N N 3 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
# 
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 ALA D 55  ? GLY D 61  ? ALA D 55  GLY D 61  5 ? 7 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 57  SG  ? ? ? 1_555 A CYS 146 SG ? ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.067 ? ? 
disulf2  disulf ? ? B CYS 57  SG  ? ? ? 1_555 B CYS 146 SG ? ? B CYS 57  B CYS 146 1_555 ? ? ? ? ? ? ? 2.079 ? ? 
disulf3  disulf ? ? C CYS 57  SG  ? ? ? 1_555 C CYS 146 SG ? ? C CYS 57  C CYS 146 1_555 ? ? ? ? ? ? ? 2.101 ? ? 
disulf4  disulf ? ? D CYS 57  SG  ? ? ? 1_555 D CYS 146 SG ? ? D CYS 57  D CYS 146 1_555 ? ? ? ? ? ? ? 2.083 ? ? 
metalc1  metalc ? ? A HIS 46  ND1 ? ? ? 1_555 E CU1 .   CU ? ? A HIS 46  A CU1 154 1_555 ? ? ? ? ? ? ? 2.409 ? ? 
metalc2  metalc ? ? A HIS 48  NE2 ? ? ? 1_555 E CU1 .   CU ? ? A HIS 48  A CU1 154 1_555 ? ? ? ? ? ? ? 2.049 ? ? 
metalc3  metalc ? ? A HIS 63  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? A HIS 63  A ZN  155 1_555 ? ? ? ? ? ? ? 2.102 ? ? 
metalc4  metalc ? ? A HIS 71  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? A HIS 71  A ZN  155 1_555 ? ? ? ? ? ? ? 2.315 ? ? 
metalc5  metalc ? ? A HIS 80  ND1 ? ? ? 1_555 F ZN  .   ZN ? ? A HIS 80  A ZN  155 1_555 ? ? ? ? ? ? ? 2.050 ? ? 
metalc6  metalc ? ? A ASP 83  OD1 ? ? ? 1_555 F ZN  .   ZN ? ? A ASP 83  A ZN  155 1_555 ? ? ? ? ? ? ? 1.793 ? ? 
metalc7  metalc ? ? A HIS 120 NE2 ? ? ? 1_555 E CU1 .   CU ? ? A HIS 120 A CU1 154 1_555 ? ? ? ? ? ? ? 1.828 ? ? 
metalc8  metalc ? ? B HIS 46  ND1 ? ? ? 1_555 G CU1 .   CU ? ? B HIS 46  B CU1 154 1_555 ? ? ? ? ? ? ? 2.249 ? ? 
metalc9  metalc ? ? B HIS 48  NE2 ? ? ? 1_555 G CU1 .   CU ? ? B HIS 48  B CU1 154 1_555 ? ? ? ? ? ? ? 2.052 ? ? 
metalc10 metalc ? ? B HIS 63  ND1 ? ? ? 1_555 H ZN  .   ZN ? ? B HIS 63  B ZN  155 1_555 ? ? ? ? ? ? ? 1.893 ? ? 
metalc11 metalc ? ? B HIS 71  ND1 ? ? ? 1_555 H ZN  .   ZN ? ? B HIS 71  B ZN  155 1_555 ? ? ? ? ? ? ? 2.251 ? ? 
metalc12 metalc ? ? B HIS 80  ND1 ? ? ? 1_555 H ZN  .   ZN ? ? B HIS 80  B ZN  155 1_555 ? ? ? ? ? ? ? 2.276 ? ? 
metalc13 metalc ? ? B ASP 83  OD1 ? ? ? 1_555 H ZN  .   ZN ? ? B ASP 83  B ZN  155 1_555 ? ? ? ? ? ? ? 1.905 ? ? 
metalc14 metalc ? ? B HIS 120 NE2 ? ? ? 1_555 G CU1 .   CU ? ? B HIS 120 B CU1 154 1_555 ? ? ? ? ? ? ? 1.809 ? ? 
# 
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 ? 
# 
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 
# 
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  ? GLU A 21  ? GLN A 15  GLU A 21  
A 4 LYS A 3   ? LEU A 8   ? LYS A 3   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  ? GLU B 21  ? GLN B 15  GLU B 21  
C 4 LYS B 3   ? LEU B 8   ? LYS B 3   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  ? GLN D 22  ? GLN D 15  GLN D 22  
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 
# 
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 ASP A 101 ? O ASP A 101 N VAL A 29  ? N VAL A 29  
A 2 3 O TRP A 32  ? O TRP A 32  N ASN A 19  ? N ASN A 19  
A 3 4 O ILE A 18  ? O ILE A 18  N ALA A 6   ? N ALA A 6   
A 4 5 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
B 1 2 O ALA A 89  ? O ALA A 89  N GLY A 41  ? N GLY A 41  
B 2 3 N HIS A 48  ? N HIS A 48  O THR A 116 ? O THR A 116 
B 3 4 N LEU A 117 ? N LEU A 117 O GLY A 147 ? O GLY A 147 
C 1 2 O ALA B 95  ? O ALA B 95  N ILE B 35  ? N ILE B 35  
C 2 3 O TRP B 32  ? O TRP B 32  N ASN B 19  ? N ASN B 19  
C 3 4 O PHE B 20  ? O PHE B 20  N ALA B 4   ? N ALA B 4   
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 VAL C 97  ? O VAL C 97  N GLY C 33  ? N GLY C 33  
E 2 3 O TRP C 32  ? O TRP C 32  N ASN C 19  ? N ASN C 19  
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 ILE D 99  ? O ILE D 99  N VAL D 31  ? N VAL D 31  
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 ALA D 6   ? N ALA 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 LEU D 117 ? N LEU D 117 O GLY D 147 ? O GLY D 147 
# 
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 A CU1 154 ? 4 'BINDING SITE FOR RESIDUE CU1 A 154' 
AC2 Software A ZN  155 ? 4 'BINDING SITE FOR RESIDUE ZN A 155'  
AC3 Software B CU1 154 ? 4 'BINDING SITE FOR RESIDUE CU1 B 154' 
AC4 Software B ZN  155 ? 4 'BINDING SITE FOR RESIDUE ZN B 155'  
# 
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 ? 
# 
_database_PDB_matrix.entry_id          2GBT 
_database_PDB_matrix.origx[1][1]       1.00000 
_database_PDB_matrix.origx[1][2]       0.00000 
_database_PDB_matrix.origx[1][3]       0.00000 
_database_PDB_matrix.origx[2][1]       0.00000 
_database_PDB_matrix.origx[2][2]       1.00000 
_database_PDB_matrix.origx[2][3]       0.00000 
_database_PDB_matrix.origx[3][1]       0.00000 
_database_PDB_matrix.origx[3][2]       0.00000 
_database_PDB_matrix.origx[3][3]       1.00000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    2GBT 
_atom_sites.fract_transf_matrix[1][1]   0.00638 
_atom_sites.fract_transf_matrix[1][2]   0.00000 
_atom_sites.fract_transf_matrix[1][3]   0.00260 
_atom_sites.fract_transf_matrix[2][1]   0.00000 
_atom_sites.fract_transf_matrix[2][2]   0.02836 
_atom_sites.fract_transf_matrix[2][3]   0.00000 
_atom_sites.fract_transf_matrix[3][1]   0.00000 
_atom_sites.fract_transf_matrix[3][2]   0.00000 
_atom_sites.fract_transf_matrix[3][3]   0.00939 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CU 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . THR A 1 2   ? 1.450   -9.473  28.824  1.00 37.54 ? 2   THR A N   1 
ATOM   2    C  CA  . THR A 1 2   ? 1.056   -10.728 28.110  1.00 37.31 ? 2   THR A CA  1 
ATOM   3    C  C   . THR A 1 2   ? -0.428  -11.075 28.234  1.00 36.77 ? 2   THR A C   1 
ATOM   4    O  O   . THR A 1 2   ? -0.955  -11.789 27.385  1.00 36.23 ? 2   THR A O   1 
ATOM   5    C  CB  . THR A 1 2   ? 1.873   -11.953 28.577  1.00 37.69 ? 2   THR A CB  1 
ATOM   6    O  OG1 . THR A 1 2   ? 1.625   -12.212 29.969  1.00 38.81 ? 2   THR A OG1 1 
ATOM   7    C  CG2 . THR A 1 2   ? 3.369   -11.738 28.359  1.00 38.25 ? 2   THR A CG2 1 
ATOM   8    N  N   . LYS A 1 3   ? -1.096  -10.584 29.279  1.00 36.37 ? 3   LYS A N   1 
ATOM   9    C  CA  . LYS A 1 3   ? -2.511  -10.888 29.493  1.00 36.26 ? 3   LYS A CA  1 
ATOM   10   C  C   . LYS A 1 3   ? -3.271  -9.714  30.109  1.00 35.74 ? 3   LYS A C   1 
ATOM   11   O  O   . LYS A 1 3   ? -2.769  -9.052  31.017  1.00 35.31 ? 3   LYS A O   1 
ATOM   12   C  CB  . LYS A 1 3   ? -2.638  -12.127 30.381  1.00 36.44 ? 3   LYS A CB  1 
ATOM   13   C  CG  . LYS A 1 3   ? -3.976  -12.820 30.287  1.00 36.83 ? 3   LYS A CG  1 
ATOM   14   C  CD  . LYS A 1 3   ? -3.900  -14.236 30.835  1.00 37.41 ? 3   LYS A CD  1 
ATOM   15   C  CE  . LYS A 1 3   ? -5.220  -14.970 30.673  1.00 38.26 ? 3   LYS A CE  1 
ATOM   16   N  NZ  . LYS A 1 3   ? -6.295  -14.425 31.553  1.00 40.10 ? 3   LYS A NZ  1 
ATOM   17   N  N   . ALA A 1 4   ? -4.483  -9.464  29.612  1.00 35.04 ? 4   ALA A N   1 
ATOM   18   C  CA  . ALA A 1 4   ? -5.315  -8.372  30.108  1.00 35.00 ? 4   ALA A CA  1 
ATOM   19   C  C   . ALA A 1 4   ? -6.795  -8.737  30.109  1.00 34.68 ? 4   ALA A C   1 
ATOM   20   O  O   . ALA A 1 4   ? -7.186  -9.760  29.555  1.00 34.15 ? 4   ALA A O   1 
ATOM   21   C  CB  . ALA A 1 4   ? -5.081  -7.115  29.275  1.00 34.90 ? 4   ALA A CB  1 
ATOM   22   N  N   . VAL A 1 5   ? -7.606  -7.894  30.738  1.00 34.62 ? 5   VAL A N   1 
ATOM   23   C  CA  . VAL A 1 5   ? -9.052  -8.121  30.807  1.00 34.78 ? 5   VAL A CA  1 
ATOM   24   C  C   . VAL A 1 5   ? -9.801  -6.787  30.843  1.00 34.98 ? 5   VAL A C   1 
ATOM   25   O  O   . VAL A 1 5   ? -9.281  -5.780  31.332  1.00 34.72 ? 5   VAL A O   1 
ATOM   26   C  CB  . VAL A 1 5   ? -9.436  -9.027  32.024  1.00 34.70 ? 5   VAL A CB  1 
ATOM   27   C  CG1 . VAL A 1 5   ? -9.130  -8.341  33.353  1.00 35.70 ? 5   VAL A CG1 1 
ATOM   28   C  CG2 . VAL A 1 5   ? -10.912 -9.466  31.955  1.00 34.74 ? 5   VAL A CG2 1 
ATOM   29   N  N   . ALA A 1 6   ? -11.011 -6.785  30.287  1.00 34.96 ? 6   ALA A N   1 
ATOM   30   C  CA  . ALA A 1 6   ? -11.896 -5.632  30.350  1.00 34.99 ? 6   ALA A CA  1 
ATOM   31   C  C   . ALA A 1 6   ? -13.262 -6.108  30.807  1.00 35.21 ? 6   ALA A C   1 
ATOM   32   O  O   . ALA A 1 6   ? -13.807 -7.051  30.238  1.00 35.26 ? 6   ALA A O   1 
ATOM   33   C  CB  . ALA A 1 6   ? -12.016 -4.975  28.985  1.00 35.01 ? 6   ALA A CB  1 
ATOM   34   N  N   . VAL A 1 7   ? -13.805 -5.453  31.827  1.00 35.24 ? 7   VAL A N   1 
ATOM   35   C  CA  . VAL A 1 7   ? -15.148 -5.750  32.320  1.00 35.62 ? 7   VAL A CA  1 
ATOM   36   C  C   . VAL A 1 7   ? -16.058 -4.629  31.844  1.00 36.13 ? 7   VAL A C   1 
ATOM   37   O  O   . VAL A 1 7   ? -15.876 -3.464  32.212  1.00 36.09 ? 7   VAL A O   1 
ATOM   38   C  CB  . VAL A 1 7   ? -15.167 -5.891  33.855  1.00 35.45 ? 7   VAL A CB  1 
ATOM   39   C  CG1 . VAL A 1 7   ? -16.569 -6.161  34.359  1.00 35.64 ? 7   VAL A CG1 1 
ATOM   40   C  CG2 . VAL A 1 7   ? -14.237 -7.018  34.275  1.00 35.88 ? 7   VAL A CG2 1 
ATOM   41   N  N   . LEU A 1 8   ? -17.015 -4.992  30.992  1.00 36.01 ? 8   LEU A N   1 
ATOM   42   C  CA  . LEU A 1 8   ? -17.845 -4.023  30.304  1.00 36.38 ? 8   LEU A CA  1 
ATOM   43   C  C   . LEU A 1 8   ? -19.109 -3.743  31.107  1.00 36.06 ? 8   LEU A C   1 
ATOM   44   O  O   . LEU A 1 8   ? -19.819 -4.670  31.496  1.00 35.91 ? 8   LEU A O   1 
ATOM   45   C  CB  . LEU A 1 8   ? -18.218 -4.547  28.912  1.00 36.63 ? 8   LEU A CB  1 
ATOM   46   C  CG  . LEU A 1 8   ? -17.053 -4.886  27.975  1.00 37.81 ? 8   LEU A CG  1 
ATOM   47   C  CD1 . LEU A 1 8   ? -17.571 -5.337  26.623  1.00 39.69 ? 8   LEU A CD1 1 
ATOM   48   C  CD2 . LEU A 1 8   ? -16.139 -3.702  27.818  1.00 39.50 ? 8   LEU A CD2 1 
ATOM   49   N  N   . LYS A 1 9   ? -19.382 -2.463  31.340  1.00 36.33 ? 9   LYS A N   1 
ATOM   50   C  CA  . LYS A 1 9   ? -20.542 -2.023  32.121  1.00 37.06 ? 9   LYS A CA  1 
ATOM   51   C  C   . LYS A 1 9   ? -21.067 -0.706  31.565  1.00 36.76 ? 9   LYS A C   1 
ATOM   52   O  O   . LYS A 1 9   ? -20.306 0.087   31.019  1.00 36.06 ? 9   LYS A O   1 
ATOM   53   C  CB  . LYS A 1 9   ? -20.161 -1.811  33.589  1.00 37.72 ? 9   LYS A CB  1 
ATOM   54   C  CG  . LYS A 1 9   ? -19.813 -3.069  34.351  1.00 39.09 ? 9   LYS A CG  1 
ATOM   55   C  CD  . LYS A 1 9   ? -19.351 -2.742  35.774  1.00 39.66 ? 9   LYS A CD  1 
ATOM   56   C  CE  . LYS A 1 9   ? -19.441 -3.953  36.711  1.00 41.98 ? 9   LYS A CE  1 
ATOM   57   N  NZ  . LYS A 1 9   ? -18.879 -5.195  36.100  1.00 44.76 ? 9   LYS A NZ  1 
ATOM   58   N  N   . GLY A 1 10  ? -22.366 -0.469  31.712  1.00 36.63 ? 10  GLY A N   1 
ATOM   59   C  CA  . GLY A 1 10  ? -22.965 0.791   31.281  1.00 37.07 ? 10  GLY A CA  1 
ATOM   60   C  C   . GLY A 1 10  ? -24.124 1.221   32.163  1.00 37.49 ? 10  GLY A C   1 
ATOM   61   O  O   . GLY A 1 10  ? -24.239 0.785   33.308  1.00 37.68 ? 10  GLY A O   1 
ATOM   62   N  N   . ASP A 1 11  ? -24.971 2.088   31.614  1.00 37.92 ? 11  ASP A N   1 
ATOM   63   C  CA  . ASP A 1 11  ? -26.145 2.607   32.312  1.00 38.21 ? 11  ASP A CA  1 
ATOM   64   C  C   . ASP A 1 11  ? -27.374 1.772   31.990  1.00 38.03 ? 11  ASP A C   1 
ATOM   65   O  O   . ASP A 1 11  ? -28.454 2.015   32.535  1.00 38.27 ? 11  ASP A O   1 
ATOM   66   C  CB  . ASP A 1 11  ? -26.402 4.064   31.911  1.00 38.82 ? 11  ASP A CB  1 
ATOM   67   C  CG  . ASP A 1 11  ? -25.304 5.005   32.381  1.00 40.85 ? 11  ASP A CG  1 
ATOM   68   O  OD1 . ASP A 1 11  ? -24.849 4.872   33.536  1.00 43.35 ? 11  ASP A OD1 1 
ATOM   69   O  OD2 . ASP A 1 11  ? -24.898 5.881   31.585  1.00 44.10 ? 11  ASP A OD2 1 
ATOM   70   N  N   . GLY A 1 12  ? -27.205 0.801   31.096  1.00 37.90 ? 12  GLY A N   1 
ATOM   71   C  CA  . GLY A 1 12  ? -28.282 -0.091  30.684  1.00 37.73 ? 12  GLY A CA  1 
ATOM   72   C  C   . GLY A 1 12  ? -27.979 -1.523  31.091  1.00 37.63 ? 12  GLY A C   1 
ATOM   73   O  O   . GLY A 1 12  ? -27.183 -1.743  32.013  1.00 37.62 ? 12  GLY A O   1 
ATOM   74   N  N   . PRO A 1 13  ? -28.585 -2.506  30.392  1.00 36.95 ? 13  PRO A N   1 
ATOM   75   C  CA  . PRO A 1 13  ? -28.432 -3.930  30.696  1.00 36.98 ? 13  PRO A CA  1 
ATOM   76   C  C   . PRO A 1 13  ? -27.187 -4.632  30.121  1.00 36.82 ? 13  PRO A C   1 
ATOM   77   O  O   . PRO A 1 13  ? -26.979 -5.818  30.384  1.00 36.55 ? 13  PRO A O   1 
ATOM   78   C  CB  . PRO A 1 13  ? -29.694 -4.536  30.073  1.00 36.73 ? 13  PRO A CB  1 
ATOM   79   C  CG  . PRO A 1 13  ? -29.938 -3.695  28.889  1.00 36.61 ? 13  PRO A CG  1 
ATOM   80   C  CD  . PRO A 1 13  ? -29.498 -2.301  29.250  1.00 37.01 ? 13  PRO A CD  1 
ATOM   81   N  N   . VAL A 1 14  ? -26.362 -3.929  29.357  1.00 37.06 ? 14  VAL A N   1 
ATOM   82   C  CA  . VAL A 1 14  ? -25.242 -4.587  28.690  1.00 37.28 ? 14  VAL A CA  1 
ATOM   83   C  C   . VAL A 1 14  ? -24.098 -4.799  29.675  1.00 37.64 ? 14  VAL A C   1 
ATOM   84   O  O   . VAL A 1 14  ? -23.604 -3.846  30.273  1.00 37.62 ? 14  VAL A O   1 
ATOM   85   C  CB  . VAL A 1 14  ? -24.751 -3.800  27.461  1.00 37.13 ? 14  VAL A CB  1 
ATOM   86   C  CG1 . VAL A 1 14  ? -23.570 -4.523  26.806  1.00 36.87 ? 14  VAL A CG1 1 
ATOM   87   C  CG2 . VAL A 1 14  ? -25.890 -3.633  26.460  1.00 37.31 ? 14  VAL A CG2 1 
ATOM   88   N  N   . GLN A 1 15  ? -23.702 -6.056  29.856  1.00 37.97 ? 15  GLN A N   1 
ATOM   89   C  CA  . GLN A 1 15  ? -22.516 -6.370  30.647  1.00 38.27 ? 15  GLN A CA  1 
ATOM   90   C  C   . GLN A 1 15  ? -21.705 -7.493  29.996  1.00 37.79 ? 15  GLN A C   1 
ATOM   91   O  O   . GLN A 1 15  ? -22.243 -8.333  29.282  1.00 37.54 ? 15  GLN A O   1 
ATOM   92   C  CB  . GLN A 1 15  ? -22.903 -6.710  32.089  1.00 38.89 ? 15  GLN A CB  1 
ATOM   93   C  CG  . GLN A 1 15  ? -23.623 -8.024  32.282  1.00 39.92 ? 15  GLN A CG  1 
ATOM   94   C  CD  . GLN A 1 15  ? -24.019 -8.268  33.734  1.00 40.87 ? 15  GLN A CD  1 
ATOM   95   O  OE1 . GLN A 1 15  ? -24.567 -7.387  34.402  1.00 45.31 ? 15  GLN A OE1 1 
ATOM   96   N  NE2 . GLN A 1 15  ? -23.754 -9.476  34.224  1.00 44.44 ? 15  GLN A NE2 1 
ATOM   97   N  N   . GLY A 1 16  ? -20.399 -7.492  30.218  1.00 37.36 ? 16  GLY A N   1 
ATOM   98   C  CA  . GLY A 1 16  ? -19.557 -8.536  29.653  1.00 37.00 ? 16  GLY A CA  1 
ATOM   99   C  C   . GLY A 1 16  ? -18.148 -8.539  30.202  1.00 36.90 ? 16  GLY A C   1 
ATOM   100  O  O   . GLY A 1 16  ? -17.751 -7.624  30.923  1.00 36.55 ? 16  GLY A O   1 
ATOM   101  N  N   . ILE A 1 17  ? -17.420 -9.601  29.870  1.00 36.19 ? 17  ILE A N   1 
ATOM   102  C  CA  . ILE A 1 17  ? -16.031 -9.766  30.254  1.00 36.05 ? 17  ILE A CA  1 
ATOM   103  C  C   . ILE A 1 17  ? -15.265 -10.209 29.025  1.00 35.75 ? 17  ILE A C   1 
ATOM   104  O  O   . ILE A 1 17  ? -15.606 -11.210 28.388  1.00 34.68 ? 17  ILE A O   1 
ATOM   105  C  CB  . ILE A 1 17  ? -15.841 -10.819 31.374  1.00 36.05 ? 17  ILE A CB  1 
ATOM   106  C  CG1 . ILE A 1 17  ? -16.613 -10.421 32.633  1.00 36.00 ? 17  ILE A CG1 1 
ATOM   107  C  CG2 . ILE A 1 17  ? -14.351 -10.973 31.706  1.00 36.01 ? 17  ILE A CG2 1 
ATOM   108  C  CD1 . ILE A 1 17  ? -16.663 -11.512 33.685  1.00 36.74 ? 17  ILE A CD1 1 
ATOM   109  N  N   . ILE A 1 18  ? -14.226 -9.454  28.698  1.00 35.35 ? 18  ILE A N   1 
ATOM   110  C  CA  . ILE A 1 18  ? -13.421 -9.720  27.522  1.00 35.30 ? 18  ILE A CA  1 
ATOM   111  C  C   . ILE A 1 18  ? -11.963 -9.860  27.935  1.00 35.14 ? 18  ILE A C   1 
ATOM   112  O  O   . ILE A 1 18  ? -11.410 -8.978  28.580  1.00 34.71 ? 18  ILE A O   1 
ATOM   113  C  CB  . ILE A 1 18  ? -13.544 -8.589  26.484  1.00 35.52 ? 18  ILE A CB  1 
ATOM   114  C  CG1 . ILE A 1 18  ? -15.004 -8.431  26.025  1.00 35.55 ? 18  ILE A CG1 1 
ATOM   115  C  CG2 . ILE A 1 18  ? -12.634 -8.864  25.289  1.00 35.30 ? 18  ILE A CG2 1 
ATOM   116  C  CD1 . ILE A 1 18  ? -15.537 -9.563  25.133  1.00 35.39 ? 18  ILE A CD1 1 
ATOM   117  N  N   . ASN A 1 19  ? -11.361 -10.980 27.547  1.00 34.92 ? 19  ASN A N   1 
ATOM   118  C  CA  . ASN A 1 19  ? -9.976  -11.293 27.854  1.00 34.94 ? 19  ASN A CA  1 
ATOM   119  C  C   . ASN A 1 19  ? -9.077  -11.030 26.658  1.00 34.85 ? 19  ASN A C   1 
ATOM   120  O  O   . ASN A 1 19  ? -9.515  -11.147 25.509  1.00 34.51 ? 19  ASN A O   1 
ATOM   121  C  CB  . ASN A 1 19  ? -9.865  -12.761 28.245  1.00 34.93 ? 19  ASN A CB  1 
ATOM   122  C  CG  . ASN A 1 19  ? -10.806 -13.133 29.375  1.00 35.23 ? 19  ASN A CG  1 
ATOM   123  O  OD1 . ASN A 1 19  ? -10.612 -12.716 30.515  1.00 36.39 ? 19  ASN A OD1 1 
ATOM   124  N  ND2 . ASN A 1 19  ? -11.839 -13.914 29.061  1.00 36.37 ? 19  ASN A ND2 1 
ATOM   125  N  N   . PHE A 1 20  ? -7.828  -10.671 26.940  1.00 35.04 ? 20  PHE A N   1 
ATOM   126  C  CA  . PHE A 1 20  ? -6.803  -10.452 25.918  1.00 35.27 ? 20  PHE A CA  1 
ATOM   127  C  C   . PHE A 1 20  ? -5.578  -11.255 26.292  1.00 35.41 ? 20  PHE A C   1 
ATOM   128  O  O   . PHE A 1 20  ? -5.158  -11.223 27.450  1.00 35.40 ? 20  PHE A O   1 
ATOM   129  C  CB  . PHE A 1 20  ? -6.384  -8.985  25.850  1.00 35.33 ? 20  PHE A CB  1 
ATOM   130  C  CG  . PHE A 1 20  ? -7.500  -8.022  25.546  1.00 35.12 ? 20  PHE A CG  1 
ATOM   131  C  CD1 . PHE A 1 20  ? -8.362  -7.598  26.547  1.00 35.35 ? 20  PHE A CD1 1 
ATOM   132  C  CD2 . PHE A 1 20  ? -7.652  -7.498  24.272  1.00 35.36 ? 20  PHE A CD2 1 
ATOM   133  C  CE1 . PHE A 1 20  ? -9.379  -6.696  26.274  1.00 35.74 ? 20  PHE A CE1 1 
ATOM   134  C  CE2 . PHE A 1 20  ? -8.660  -6.594  23.994  1.00 35.59 ? 20  PHE A CE2 1 
ATOM   135  C  CZ  . PHE A 1 20  ? -9.530  -6.196  24.995  1.00 35.36 ? 20  PHE A CZ  1 
ATOM   136  N  N   . GLU A 1 21  ? -4.993  -11.968 25.334  1.00 35.54 ? 21  GLU A N   1 
ATOM   137  C  CA  . GLU A 1 21  ? -3.707  -12.631 25.571  1.00 35.91 ? 21  GLU A CA  1 
ATOM   138  C  C   . GLU A 1 21  ? -2.767  -12.490 24.379  1.00 35.96 ? 21  GLU A C   1 
ATOM   139  O  O   . GLU A 1 21  ? -3.165  -12.689 23.233  1.00 35.48 ? 21  GLU A O   1 
ATOM   140  C  CB  . GLU A 1 21  ? -3.887  -14.114 25.928  1.00 35.75 ? 21  GLU A CB  1 
ATOM   141  C  CG  . GLU A 1 21  ? -2.569  -14.803 26.285  1.00 36.13 ? 21  GLU A CG  1 
ATOM   142  C  CD  . GLU A 1 21  ? -2.746  -16.190 26.876  1.00 36.96 ? 21  GLU A CD  1 
ATOM   143  O  OE1 . GLU A 1 21  ? -3.421  -17.039 26.245  1.00 40.76 ? 21  GLU A OE1 1 
ATOM   144  O  OE2 . GLU A 1 21  ? -2.185  -16.435 27.967  1.00 38.64 ? 21  GLU A OE2 1 
ATOM   145  N  N   . GLN A 1 22  ? -1.513  -12.162 24.673  1.00 36.23 ? 22  GLN A N   1 
ATOM   146  C  CA  . GLN A 1 22  ? -0.483  -11.990 23.651  1.00 36.95 ? 22  GLN A CA  1 
ATOM   147  C  C   . GLN A 1 22  ? 0.796   -12.700 24.095  1.00 37.51 ? 22  GLN A C   1 
ATOM   148  O  O   . GLN A 1 22  ? 1.470   -12.259 25.023  1.00 37.68 ? 22  GLN A O   1 
ATOM   149  C  CB  . GLN A 1 22  ? -0.215  -10.501 23.422  1.00 36.61 ? 22  GLN A CB  1 
ATOM   150  C  CG  . GLN A 1 22  ? 0.720   -10.204 22.266  1.00 36.37 ? 22  GLN A CG  1 
ATOM   151  C  CD  . GLN A 1 22  ? 0.912   -8.716  22.023  1.00 36.79 ? 22  GLN A CD  1 
ATOM   152  O  OE1 . GLN A 1 22  ? 0.779   -7.899  22.940  1.00 36.41 ? 22  GLN A OE1 1 
ATOM   153  N  NE2 . GLN A 1 22  ? 1.239   -8.358  20.786  1.00 35.48 ? 22  GLN A NE2 1 
ATOM   154  N  N   . LYS A 1 23  ? 1.122   -13.797 23.416  1.00 38.45 ? 23  LYS A N   1 
ATOM   155  C  CA  . LYS A 1 23  ? 2.257   -14.636 23.783  1.00 39.10 ? 23  LYS A CA  1 
ATOM   156  C  C   . LYS A 1 23  ? 3.593   -13.961 23.474  1.00 39.55 ? 23  LYS A C   1 
ATOM   157  O  O   . LYS A 1 23  ? 4.562   -14.133 24.216  1.00 39.87 ? 23  LYS A O   1 
ATOM   158  C  CB  . LYS A 1 23  ? 2.181   -15.979 23.052  1.00 39.50 ? 23  LYS A CB  1 
ATOM   159  C  CG  . LYS A 1 23  ? 0.905   -16.777 23.319  1.00 40.25 ? 23  LYS A CG  1 
ATOM   160  C  CD  . LYS A 1 23  ? 0.888   -17.387 24.712  1.00 40.78 ? 23  LYS A CD  1 
ATOM   161  C  CE  . LYS A 1 23  ? -0.310  -18.316 24.889  1.00 40.81 ? 23  LYS A CE  1 
ATOM   162  N  NZ  . LYS A 1 23  ? -0.153  -19.224 26.057  1.00 40.90 ? 23  LYS A NZ  1 
ATOM   163  N  N   . GLU A 1 24  ? 3.638   -13.197 22.382  1.00 40.06 ? 24  GLU A N   1 
ATOM   164  C  CA  . GLU A 1 24  ? 4.864   -12.524 21.944  1.00 40.45 ? 24  GLU A CA  1 
ATOM   165  C  C   . GLU A 1 24  ? 4.585   -11.083 21.523  1.00 40.57 ? 24  GLU A C   1 
ATOM   166  O  O   . GLU A 1 24  ? 3.532   -10.794 20.956  1.00 40.62 ? 24  GLU A O   1 
ATOM   167  C  CB  . GLU A 1 24  ? 5.481   -13.276 20.768  1.00 40.61 ? 24  GLU A CB  1 
ATOM   168  C  CG  . GLU A 1 24  ? 5.761   -14.737 21.041  1.00 41.18 ? 24  GLU A CG  1 
ATOM   169  C  CD  . GLU A 1 24  ? 6.440   -15.413 19.871  1.00 41.51 ? 24  GLU A CD  1 
ATOM   170  O  OE1 . GLU A 1 24  ? 5.908   -15.317 18.739  1.00 43.42 ? 24  GLU A OE1 1 
ATOM   171  O  OE2 . GLU A 1 24  ? 7.500   -16.039 20.082  1.00 42.68 ? 24  GLU A OE2 1 
ATOM   172  N  N   . SER A 1 25  ? 5.548   -10.193 21.772  1.00 40.68 ? 25  SER A N   1 
ATOM   173  C  CA  . SER A 1 25  ? 5.361   -8.754  21.534  1.00 40.71 ? 25  SER A CA  1 
ATOM   174  C  C   . SER A 1 25  ? 5.116   -8.396  20.064  1.00 40.70 ? 25  SER A C   1 
ATOM   175  O  O   . SER A 1 25  ? 4.392   -7.442  19.776  1.00 41.04 ? 25  SER A O   1 
ATOM   176  C  CB  . SER A 1 25  ? 6.548   -7.951  22.078  1.00 40.79 ? 25  SER A CB  1 
ATOM   177  O  OG  . SER A 1 25  ? 7.750   -8.281  21.408  1.00 40.84 ? 25  SER A OG  1 
ATOM   178  N  N   . ASN A 1 26  ? 5.709   -9.155  19.144  1.00 40.75 ? 26  ASN A N   1 
ATOM   179  C  CA  . ASN A 1 26  ? 5.419   -8.996  17.712  1.00 40.72 ? 26  ASN A CA  1 
ATOM   180  C  C   . ASN A 1 26  ? 4.460   -10.079 17.201  1.00 40.61 ? 26  ASN A C   1 
ATOM   181  O  O   . ASN A 1 26  ? 4.561   -10.523 16.050  1.00 41.07 ? 26  ASN A O   1 
ATOM   182  C  CB  . ASN A 1 26  ? 6.715   -8.999  16.890  1.00 41.11 ? 26  ASN A CB  1 
ATOM   183  C  CG  . ASN A 1 26  ? 7.539   -7.725  17.071  1.00 41.97 ? 26  ASN A CG  1 
ATOM   184  O  OD1 . ASN A 1 26  ? 8.769   -7.769  17.065  1.00 43.99 ? 26  ASN A OD1 1 
ATOM   185  N  ND2 . ASN A 1 26  ? 6.861   -6.585  17.213  1.00 43.36 ? 26  ASN A ND2 1 
ATOM   186  N  N   . GLY A 1 27  ? 3.528   -10.492 18.057  1.00 39.93 ? 27  GLY A N   1 
ATOM   187  C  CA  . GLY A 1 27  ? 2.595   -11.564 17.730  1.00 39.37 ? 27  GLY A CA  1 
ATOM   188  C  C   . GLY A 1 27  ? 1.160   -11.117 17.894  1.00 38.79 ? 27  GLY A C   1 
ATOM   189  O  O   . GLY A 1 27  ? 0.904   -10.045 18.447  1.00 38.78 ? 27  GLY A O   1 
ATOM   190  N  N   . PRO A 1 28  ? 0.207   -11.944 17.428  1.00 38.08 ? 28  PRO A N   1 
ATOM   191  C  CA  . PRO A 1 28  ? -1.206  -11.579 17.493  1.00 37.74 ? 28  PRO A CA  1 
ATOM   192  C  C   . PRO A 1 28  ? -1.765  -11.560 18.917  1.00 37.14 ? 28  PRO A C   1 
ATOM   193  O  O   . PRO A 1 28  ? -1.253  -12.255 19.799  1.00 37.08 ? 28  PRO A O   1 
ATOM   194  C  CB  . PRO A 1 28  ? -1.899  -12.679 16.667  1.00 37.62 ? 28  PRO A CB  1 
ATOM   195  C  CG  . PRO A 1 28  ? -0.803  -13.409 15.953  1.00 37.94 ? 28  PRO A CG  1 
ATOM   196  C  CD  . PRO A 1 28  ? 0.400   -13.269 16.813  1.00 38.22 ? 28  PRO A CD  1 
ATOM   197  N  N   . VAL A 1 29  ? -2.807  -10.758 19.118  1.00 36.64 ? 29  VAL A N   1 
ATOM   198  C  CA  . VAL A 1 29  ? -3.540  -10.721 20.378  1.00 36.34 ? 29  VAL A CA  1 
ATOM   199  C  C   . VAL A 1 29  ? -4.833  -11.518 20.226  1.00 36.09 ? 29  VAL A C   1 
ATOM   200  O  O   . VAL A 1 29  ? -5.646  -11.215 19.357  1.00 36.09 ? 29  VAL A O   1 
ATOM   201  C  CB  . VAL A 1 29  ? -3.894  -9.277  20.796  1.00 36.17 ? 29  VAL A CB  1 
ATOM   202  C  CG1 . VAL A 1 29  ? -4.566  -9.272  22.170  1.00 36.02 ? 29  VAL A CG1 1 
ATOM   203  C  CG2 . VAL A 1 29  ? -2.650  -8.398  20.813  1.00 36.35 ? 29  VAL A CG2 1 
ATOM   204  N  N   . LYS A 1 30  ? -5.002  -12.538 21.063  1.00 35.92 ? 30  LYS A N   1 
ATOM   205  C  CA  . LYS A 1 30  ? -6.255  -13.277 21.146  1.00 35.89 ? 30  LYS A CA  1 
ATOM   206  C  C   . LYS A 1 30  ? -7.214  -12.503 22.042  1.00 35.64 ? 30  LYS A C   1 
ATOM   207  O  O   . LYS A 1 30  ? -6.830  -12.037 23.117  1.00 35.35 ? 30  LYS A O   1 
ATOM   208  C  CB  . LYS A 1 30  ? -6.024  -14.678 21.712  1.00 35.95 ? 30  LYS A CB  1 
ATOM   209  C  CG  . LYS A 1 30  ? -5.097  -15.527 20.871  1.00 36.62 ? 30  LYS A CG  1 
ATOM   210  C  CD  . LYS A 1 30  ? -5.005  -16.954 21.389  1.00 36.63 ? 30  LYS A CD  1 
ATOM   211  C  CE  . LYS A 1 30  ? -4.227  -17.844 20.426  1.00 36.56 ? 30  LYS A CE  1 
ATOM   212  N  NZ  . LYS A 1 30  ? -4.278  -19.282 20.812  1.00 36.99 ? 30  LYS A NZ  1 
ATOM   213  N  N   . VAL A 1 31  ? -8.455  -12.358 21.584  1.00 35.47 ? 31  VAL A N   1 
ATOM   214  C  CA  . VAL A 1 31  ? -9.479  -11.605 22.292  1.00 35.58 ? 31  VAL A CA  1 
ATOM   215  C  C   . VAL A 1 31  ? -10.703 -12.502 22.418  1.00 35.56 ? 31  VAL A C   1 
ATOM   216  O  O   . VAL A 1 31  ? -11.257 -12.929 21.406  1.00 35.43 ? 31  VAL A O   1 
ATOM   217  C  CB  . VAL A 1 31  ? -9.849  -10.316 21.524  1.00 35.77 ? 31  VAL A CB  1 
ATOM   218  C  CG1 . VAL A 1 31  ? -10.807 -9.446  22.331  1.00 35.98 ? 31  VAL A CG1 1 
ATOM   219  C  CG2 . VAL A 1 31  ? -8.585  -9.537  21.158  1.00 36.02 ? 31  VAL A CG2 1 
ATOM   220  N  N   . TRP A 1 32  ? -11.113 -12.811 23.647  1.00 35.48 ? 32  TRP A N   1 
ATOM   221  C  CA  . TRP A 1 32  ? -12.257 -13.705 23.848  1.00 35.30 ? 32  TRP A CA  1 
ATOM   222  C  C   . TRP A 1 32  ? -13.047 -13.443 25.125  1.00 35.39 ? 32  TRP A C   1 
ATOM   223  O  O   . TRP A 1 32  ? -12.524 -12.932 26.109  1.00 35.12 ? 32  TRP A O   1 
ATOM   224  C  CB  . TRP A 1 32  ? -11.816 -15.173 23.798  1.00 34.88 ? 32  TRP A CB  1 
ATOM   225  C  CG  . TRP A 1 32  ? -11.163 -15.672 25.035  1.00 34.82 ? 32  TRP A CG  1 
ATOM   226  C  CD1 . TRP A 1 32  ? -11.730 -16.449 26.002  1.00 34.91 ? 32  TRP A CD1 1 
ATOM   227  C  CD2 . TRP A 1 32  ? -9.810  -15.444 25.450  1.00 34.58 ? 32  TRP A CD2 1 
ATOM   228  N  NE1 . TRP A 1 32  ? -10.818 -16.716 26.991  1.00 34.71 ? 32  TRP A NE1 1 
ATOM   229  C  CE2 . TRP A 1 32  ? -9.631  -16.112 26.679  1.00 34.66 ? 32  TRP A CE2 1 
ATOM   230  C  CE3 . TRP A 1 32  ? -8.732  -14.739 24.903  1.00 34.68 ? 32  TRP A CE3 1 
ATOM   231  C  CZ2 . TRP A 1 32  ? -8.420  -16.101 27.368  1.00 34.65 ? 32  TRP A CZ2 1 
ATOM   232  C  CZ3 . TRP A 1 32  ? -7.529  -14.728 25.589  1.00 34.85 ? 32  TRP A CZ3 1 
ATOM   233  C  CH2 . TRP A 1 32  ? -7.384  -15.399 26.811  1.00 34.99 ? 32  TRP A CH2 1 
ATOM   234  N  N   . GLY A 1 33  ? -14.319 -13.821 25.092  1.00 35.45 ? 33  GLY A N   1 
ATOM   235  C  CA  . GLY A 1 33  ? -15.215 -13.586 26.217  1.00 35.76 ? 33  GLY A CA  1 
ATOM   236  C  C   . GLY A 1 33  ? -16.666 -13.576 25.789  1.00 35.94 ? 33  GLY A C   1 
ATOM   237  O  O   . GLY A 1 33  ? -17.022 -14.113 24.736  1.00 36.35 ? 33  GLY A O   1 
ATOM   238  N  N   . SER A 1 34  ? -17.503 -12.954 26.610  1.00 36.49 ? 34  SER A N   1 
ATOM   239  C  CA  . SER A 1 34  ? -18.932 -12.893 26.352  1.00 36.53 ? 34  SER A CA  1 
ATOM   240  C  C   . SER A 1 34  ? -19.499 -11.528 26.726  1.00 36.77 ? 34  SER A C   1 
ATOM   241  O  O   . SER A 1 34  ? -19.029 -10.876 27.669  1.00 37.19 ? 34  SER A O   1 
ATOM   242  C  CB  . SER A 1 34  ? -19.655 -13.986 27.144  1.00 36.73 ? 34  SER A CB  1 
ATOM   243  O  OG  . SER A 1 34  ? -20.964 -14.193 26.645  1.00 37.48 ? 34  SER A OG  1 
ATOM   244  N  N   . ILE A 1 35  ? -20.502 -11.097 25.969  1.00 36.50 ? 35  ILE A N   1 
ATOM   245  C  CA  . ILE A 1 35  ? -21.273 -9.911  26.311  1.00 36.28 ? 35  ILE A CA  1 
ATOM   246  C  C   . ILE A 1 35  ? -22.748 -10.289 26.257  1.00 35.84 ? 35  ILE A C   1 
ATOM   247  O  O   . ILE A 1 35  ? -23.183 -10.972 25.328  1.00 35.67 ? 35  ILE A O   1 
ATOM   248  C  CB  . ILE A 1 35  ? -21.002 -8.741  25.341  1.00 35.79 ? 35  ILE A CB  1 
ATOM   249  C  CG1 . ILE A 1 35  ? -19.497 -8.498  25.170  1.00 36.31 ? 35  ILE A CG1 1 
ATOM   250  C  CG2 . ILE A 1 35  ? -21.659 -7.464  25.852  1.00 35.94 ? 35  ILE A CG2 1 
ATOM   251  C  CD1 . ILE A 1 35  ? -19.168 -7.559  24.044  1.00 36.61 ? 35  ILE A CD1 1 
ATOM   252  N  N   . LYS A 1 36  ? -23.515 -9.851  27.250  1.00 35.90 ? 36  LYS A N   1 
ATOM   253  C  CA  . LYS A 1 36  ? -24.951 -10.104 27.254  1.00 35.91 ? 36  LYS A CA  1 
ATOM   254  C  C   . LYS A 1 36  ? -25.743 -8.811  27.336  1.00 35.71 ? 36  LYS A C   1 
ATOM   255  O  O   . LYS A 1 36  ? -25.182 -7.749  27.564  1.00 35.92 ? 36  LYS A O   1 
ATOM   256  C  CB  . LYS A 1 36  ? -25.336 -11.057 28.387  1.00 36.39 ? 36  LYS A CB  1 
ATOM   257  C  CG  . LYS A 1 36  ? -24.974 -10.613 29.797  1.00 36.84 ? 36  LYS A CG  1 
ATOM   258  C  CD  . LYS A 1 36  ? -25.332 -11.722 30.775  1.00 37.25 ? 36  LYS A CD  1 
ATOM   259  C  CE  . LYS A 1 36  ? -24.849 -11.442 32.177  1.00 38.09 ? 36  LYS A CE  1 
ATOM   260  N  NZ  . LYS A 1 36  ? -25.261 -12.527 33.119  1.00 39.35 ? 36  LYS A NZ  1 
ATOM   261  N  N   . GLY A 1 37  ? -27.053 -8.904  27.121  1.00 35.24 ? 37  GLY A N   1 
ATOM   262  C  CA  . GLY A 1 37  ? -27.931 -7.739  27.221  1.00 35.34 ? 37  GLY A CA  1 
ATOM   263  C  C   . GLY A 1 37  ? -28.013 -6.898  25.962  1.00 35.03 ? 37  GLY A C   1 
ATOM   264  O  O   . GLY A 1 37  ? -28.489 -5.759  26.001  1.00 34.63 ? 37  GLY A O   1 
ATOM   265  N  N   . LEU A 1 38  ? -27.560 -7.471  24.848  1.00 35.29 ? 38  LEU A N   1 
ATOM   266  C  CA  . LEU A 1 38  ? -27.506 -6.788  23.558  1.00 35.20 ? 38  LEU A CA  1 
ATOM   267  C  C   . LEU A 1 38  ? -28.713 -7.132  22.697  1.00 35.26 ? 38  LEU A C   1 
ATOM   268  O  O   . LEU A 1 38  ? -29.304 -8.198  22.842  1.00 34.96 ? 38  LEU A O   1 
ATOM   269  C  CB  . LEU A 1 38  ? -26.246 -7.209  22.800  1.00 35.26 ? 38  LEU A CB  1 
ATOM   270  C  CG  . LEU A 1 38  ? -24.908 -6.808  23.423  1.00 34.68 ? 38  LEU A CG  1 
ATOM   271  C  CD1 . LEU A 1 38  ? -23.772 -7.604  22.794  1.00 35.28 ? 38  LEU A CD1 1 
ATOM   272  C  CD2 . LEU A 1 38  ? -24.669 -5.313  23.262  1.00 34.93 ? 38  LEU A CD2 1 
ATOM   273  N  N   . THR A 1 39  ? -29.066 -6.228  21.788  1.00 35.50 ? 39  THR A N   1 
ATOM   274  C  CA  . THR A 1 39  ? -30.052 -6.539  20.761  1.00 35.59 ? 39  THR A CA  1 
ATOM   275  C  C   . THR A 1 39  ? -29.432 -7.531  19.792  1.00 35.44 ? 39  THR A C   1 
ATOM   276  O  O   . THR A 1 39  ? -28.249 -7.421  19.447  1.00 34.70 ? 39  THR A O   1 
ATOM   277  C  CB  . THR A 1 39  ? -30.494 -5.298  19.957  1.00 35.87 ? 39  THR A CB  1 
ATOM   278  O  OG1 . THR A 1 39  ? -29.358 -4.703  19.313  1.00 37.13 ? 39  THR A OG1 1 
ATOM   279  C  CG2 . THR A 1 39  ? -31.179 -4.281  20.854  1.00 36.41 ? 39  THR A CG2 1 
ATOM   280  N  N   . GLU A 1 40  ? -30.231 -8.501  19.361  1.00 35.57 ? 40  GLU A N   1 
ATOM   281  C  CA  . GLU A 1 40  ? -29.800 -9.476  18.364  1.00 35.73 ? 40  GLU A CA  1 
ATOM   282  C  C   . GLU A 1 40  ? -29.171 -8.769  17.157  1.00 35.48 ? 40  GLU A C   1 
ATOM   283  O  O   . GLU A 1 40  ? -29.727 -7.797  16.646  1.00 35.87 ? 40  GLU A O   1 
ATOM   284  C  CB  . GLU A 1 40  ? -30.997 -10.321 17.924  1.00 35.93 ? 40  GLU A CB  1 
ATOM   285  C  CG  . GLU A 1 40  ? -30.661 -11.477 17.004  1.00 36.18 ? 40  GLU A CG  1 
ATOM   286  C  CD  . GLU A 1 40  ? -31.888 -12.256 16.559  1.00 36.81 ? 40  GLU A CD  1 
ATOM   287  O  OE1 . GLU A 1 40  ? -33.001 -12.026 17.094  1.00 38.58 ? 40  GLU A OE1 1 
ATOM   288  O  OE2 . GLU A 1 40  ? -31.744 -13.111 15.661  1.00 38.61 ? 40  GLU A OE2 1 
ATOM   289  N  N   . GLY A 1 41  ? -28.009 -9.249  16.721  1.00 35.15 ? 41  GLY A N   1 
ATOM   290  C  CA  . GLY A 1 41  ? -27.326 -8.694  15.550  1.00 35.03 ? 41  GLY A CA  1 
ATOM   291  C  C   . GLY A 1 41  ? -25.958 -8.109  15.835  1.00 35.10 ? 41  GLY A C   1 
ATOM   292  O  O   . GLY A 1 41  ? -25.359 -8.379  16.877  1.00 34.38 ? 41  GLY A O   1 
ATOM   293  N  N   . LEU A 1 42  ? -25.474 -7.294  14.899  1.00 34.96 ? 42  LEU A N   1 
ATOM   294  C  CA  . LEU A 1 42  ? -24.097 -6.788  14.935  1.00 35.15 ? 42  LEU A CA  1 
ATOM   295  C  C   . LEU A 1 42  ? -23.956 -5.527  15.778  1.00 34.98 ? 42  LEU A C   1 
ATOM   296  O  O   . LEU A 1 42  ? -24.813 -4.643  15.720  1.00 35.12 ? 42  LEU A O   1 
ATOM   297  C  CB  . LEU A 1 42  ? -23.609 -6.489  13.517  1.00 35.50 ? 42  LEU A CB  1 
ATOM   298  C  CG  . LEU A 1 42  ? -23.446 -7.659  12.548  1.00 36.77 ? 42  LEU A CG  1 
ATOM   299  C  CD1 . LEU A 1 42  ? -23.140 -7.125  11.160  1.00 37.61 ? 42  LEU A CD1 1 
ATOM   300  C  CD2 . LEU A 1 42  ? -22.343 -8.590  12.999  1.00 37.81 ? 42  LEU A CD2 1 
ATOM   301  N  N   . HIS A 1 43  ? -22.853 -5.447  16.529  1.00 34.78 ? 43  HIS A N   1 
ATOM   302  C  CA  . HIS A 1 43  ? -22.547 -4.308  17.384  1.00 34.36 ? 43  HIS A CA  1 
ATOM   303  C  C   . HIS A 1 43  ? -21.074 -3.937  17.264  1.00 34.45 ? 43  HIS A C   1 
ATOM   304  O  O   . HIS A 1 43  ? -20.208 -4.798  17.422  1.00 33.48 ? 43  HIS A O   1 
ATOM   305  C  CB  . HIS A 1 43  ? -22.853 -4.659  18.830  1.00 34.48 ? 43  HIS A CB  1 
ATOM   306  C  CG  . HIS A 1 43  ? -24.310 -4.848  19.096  1.00 33.87 ? 43  HIS A CG  1 
ATOM   307  N  ND1 . HIS A 1 43  ? -25.139 -3.803  19.441  1.00 35.09 ? 43  HIS A ND1 1 
ATOM   308  C  CD2 . HIS A 1 43  ? -25.096 -5.947  19.022  1.00 34.44 ? 43  HIS A CD2 1 
ATOM   309  C  CE1 . HIS A 1 43  ? -26.373 -4.256  19.583  1.00 34.10 ? 43  HIS A CE1 1 
ATOM   310  N  NE2 . HIS A 1 43  ? -26.373 -5.554  19.339  1.00 33.52 ? 43  HIS A NE2 1 
ATOM   311  N  N   . GLY A 1 44  ? -20.807 -2.658  17.013  1.00 34.16 ? 44  GLY A N   1 
ATOM   312  C  CA  . GLY A 1 44  ? -19.437 -2.161  16.909  1.00 34.65 ? 44  GLY A CA  1 
ATOM   313  C  C   . GLY A 1 44  ? -18.652 -2.503  18.158  1.00 34.86 ? 44  GLY A C   1 
ATOM   314  O  O   . GLY A 1 44  ? -19.202 -2.524  19.247  1.00 35.49 ? 44  GLY A O   1 
ATOM   315  N  N   . PHE A 1 45  ? -17.359 -2.772  17.983  1.00 35.34 ? 45  PHE A N   1 
ATOM   316  C  CA  . PHE A 1 45  ? -16.515 -3.299  19.047  1.00 35.54 ? 45  PHE A CA  1 
ATOM   317  C  C   . PHE A 1 45  ? -15.143 -2.663  18.871  1.00 35.94 ? 45  PHE A C   1 
ATOM   318  O  O   . PHE A 1 45  ? -14.395 -3.067  17.982  1.00 36.26 ? 45  PHE A O   1 
ATOM   319  C  CB  . PHE A 1 45  ? -16.450 -4.817  18.878  1.00 35.97 ? 45  PHE A CB  1 
ATOM   320  C  CG  . PHE A 1 45  ? -15.791 -5.546  20.007  1.00 35.90 ? 45  PHE A CG  1 
ATOM   321  C  CD1 . PHE A 1 45  ? -16.273 -5.438  21.302  1.00 37.15 ? 45  PHE A CD1 1 
ATOM   322  C  CD2 . PHE A 1 45  ? -14.726 -6.399  19.761  1.00 36.83 ? 45  PHE A CD2 1 
ATOM   323  C  CE1 . PHE A 1 45  ? -15.681 -6.145  22.341  1.00 37.24 ? 45  PHE A CE1 1 
ATOM   324  C  CE2 . PHE A 1 45  ? -14.124 -7.095  20.790  1.00 37.06 ? 45  PHE A CE2 1 
ATOM   325  C  CZ  . PHE A 1 45  ? -14.601 -6.977  22.077  1.00 37.49 ? 45  PHE A CZ  1 
ATOM   326  N  N   . HIS A 1 46  ? -14.834 -1.639  19.668  1.00 36.24 ? 46  HIS A N   1 
ATOM   327  C  CA  . HIS A 1 46  ? -13.623 -0.838  19.428  1.00 36.53 ? 46  HIS A CA  1 
ATOM   328  C  C   . HIS A 1 46  ? -12.856 -0.516  20.702  1.00 36.15 ? 46  HIS A C   1 
ATOM   329  O  O   . HIS A 1 46  ? -13.437 -0.413  21.774  1.00 36.09 ? 46  HIS A O   1 
ATOM   330  C  CB  . HIS A 1 46  ? -13.948 0.504   18.764  1.00 37.34 ? 46  HIS A CB  1 
ATOM   331  C  CG  . HIS A 1 46  ? -14.933 0.417   17.638  1.00 37.53 ? 46  HIS A CG  1 
ATOM   332  N  ND1 . HIS A 1 46  ? -16.117 1.121   17.637  1.00 38.14 ? 46  HIS A ND1 1 
ATOM   333  C  CD2 . HIS A 1 46  ? -14.917 -0.295  16.488  1.00 38.82 ? 46  HIS A CD2 1 
ATOM   334  C  CE1 . HIS A 1 46  ? -16.780 0.856   16.524  1.00 39.22 ? 46  HIS A CE1 1 
ATOM   335  N  NE2 . HIS A 1 46  ? -16.073 -0.002  15.811  1.00 38.93 ? 46  HIS A NE2 1 
ATOM   336  N  N   . VAL A 1 47  ? -11.556 -0.306  20.547  1.00 35.83 ? 47  VAL A N   1 
ATOM   337  C  CA  . VAL A 1 47  ? -10.732 0.256   21.613  1.00 36.04 ? 47  VAL A CA  1 
ATOM   338  C  C   . VAL A 1 47  ? -10.694 1.767   21.419  1.00 35.94 ? 47  VAL A C   1 
ATOM   339  O  O   . VAL A 1 47  ? -10.332 2.249   20.332  1.00 35.55 ? 47  VAL A O   1 
ATOM   340  C  CB  . VAL A 1 47  ? -9.313  -0.296  21.585  1.00 36.20 ? 47  VAL A CB  1 
ATOM   341  C  CG1 . VAL A 1 47  ? -8.511  0.261   22.765  1.00 35.46 ? 47  VAL A CG1 1 
ATOM   342  C  CG2 . VAL A 1 47  ? -9.347  -1.823  21.641  1.00 36.87 ? 47  VAL A CG2 1 
ATOM   343  N  N   . HIS A 1 48  ? -11.084 2.489   22.474  1.00 35.63 ? 48  HIS A N   1 
ATOM   344  C  CA  . HIS A 1 48  ? -11.065 3.949   22.505  1.00 35.74 ? 48  HIS A CA  1 
ATOM   345  C  C   . HIS A 1 48  ? -9.843  4.455   23.258  1.00 35.83 ? 48  HIS A C   1 
ATOM   346  O  O   . HIS A 1 48  ? -9.234  3.711   24.011  1.00 36.07 ? 48  HIS A O   1 
ATOM   347  C  CB  . HIS A 1 48  ? -12.359 4.476   23.117  1.00 35.96 ? 48  HIS A CB  1 
ATOM   348  C  CG  . HIS A 1 48  ? -13.543 4.306   22.216  1.00 35.53 ? 48  HIS A CG  1 
ATOM   349  N  ND1 . HIS A 1 48  ? -14.256 5.373   21.708  1.00 37.03 ? 48  HIS A ND1 1 
ATOM   350  C  CD2 . HIS A 1 48  ? -14.101 3.194   21.684  1.00 36.26 ? 48  HIS A CD2 1 
ATOM   351  C  CE1 . HIS A 1 48  ? -15.222 4.922   20.924  1.00 36.71 ? 48  HIS A CE1 1 
ATOM   352  N  NE2 . HIS A 1 48  ? -15.151 3.602   20.894  1.00 36.22 ? 48  HIS A NE2 1 
ATOM   353  N  N   . GLU A 1 49  ? -9.510  5.728   23.068  1.00 35.81 ? 49  GLU A N   1 
ATOM   354  C  CA  . GLU A 1 49  ? -8.171  6.227   23.401  1.00 35.85 ? 49  GLU A CA  1 
ATOM   355  C  C   . GLU A 1 49  ? -7.862  6.248   24.898  1.00 35.67 ? 49  GLU A C   1 
ATOM   356  O  O   . GLU A 1 49  ? -6.751  5.893   25.317  1.00 35.45 ? 49  GLU A O   1 
ATOM   357  C  CB  . GLU A 1 49  ? -7.962  7.636   22.827  1.00 36.13 ? 49  GLU A CB  1 
ATOM   358  C  CG  . GLU A 1 49  ? -6.534  8.143   22.986  1.00 36.15 ? 49  GLU A CG  1 
ATOM   359  C  CD  . GLU A 1 49  ? -6.273  9.457   22.276  1.00 36.65 ? 49  GLU A CD  1 
ATOM   360  O  OE1 . GLU A 1 49  ? -7.196  9.983   21.623  1.00 38.70 ? 49  GLU A OE1 1 
ATOM   361  O  OE2 . GLU A 1 49  ? -5.133  9.960   22.376  1.00 38.49 ? 49  GLU A OE2 1 
ATOM   362  N  N   . PHE A 1 50  ? -8.829  6.680   25.703  1.00 35.67 ? 50  PHE A N   1 
ATOM   363  C  CA  . PHE A 1 50  ? -8.562  6.935   27.119  1.00 35.79 ? 50  PHE A CA  1 
ATOM   364  C  C   . PHE A 1 50  ? -9.261  5.931   28.027  1.00 35.90 ? 50  PHE A C   1 
ATOM   365  O  O   . PHE A 1 50  ? -10.392 5.521   27.769  1.00 36.20 ? 50  PHE A O   1 
ATOM   366  C  CB  . PHE A 1 50  ? -8.975  8.363   27.492  1.00 36.01 ? 50  PHE A CB  1 
ATOM   367  C  CG  . PHE A 1 50  ? -8.317  9.428   26.651  1.00 36.03 ? 50  PHE A CG  1 
ATOM   368  C  CD1 . PHE A 1 50  ? -6.944  9.649   26.728  1.00 36.32 ? 50  PHE A CD1 1 
ATOM   369  C  CD2 . PHE A 1 50  ? -9.070  10.217  25.791  1.00 36.43 ? 50  PHE A CD2 1 
ATOM   370  C  CE1 . PHE A 1 50  ? -6.340  10.633  25.953  1.00 36.88 ? 50  PHE A CE1 1 
ATOM   371  C  CE2 . PHE A 1 50  ? -8.466  11.206  25.010  1.00 35.99 ? 50  PHE A CE2 1 
ATOM   372  C  CZ  . PHE A 1 50  ? -7.103  11.406  25.090  1.00 36.19 ? 50  PHE A CZ  1 
ATOM   373  N  N   . GLY A 1 51  ? -8.577  5.531   29.095  1.00 35.65 ? 51  GLY A N   1 
ATOM   374  C  CA  . GLY A 1 51  ? -9.167  4.678   30.120  1.00 35.95 ? 51  GLY A CA  1 
ATOM   375  C  C   . GLY A 1 51  ? -9.799  5.533   31.203  1.00 35.86 ? 51  GLY A C   1 
ATOM   376  O  O   . GLY A 1 51  ? -9.508  5.361   32.380  1.00 36.01 ? 51  GLY A O   1 
ATOM   377  N  N   . ASP A 1 52  ? -10.671 6.450   30.782  1.00 36.33 ? 52  ASP A N   1 
ATOM   378  C  CA  . ASP A 1 52  ? -11.259 7.473   31.643  1.00 36.12 ? 52  ASP A CA  1 
ATOM   379  C  C   . ASP A 1 52  ? -12.770 7.238   31.677  1.00 36.50 ? 52  ASP A C   1 
ATOM   380  O  O   . ASP A 1 52  ? -13.442 7.392   30.660  1.00 36.05 ? 52  ASP A O   1 
ATOM   381  C  CB  . ASP A 1 52  ? -10.930 8.858   31.067  1.00 36.06 ? 52  ASP A CB  1 
ATOM   382  C  CG  . ASP A 1 52  ? -11.418 10.004  31.938  1.00 36.32 ? 52  ASP A CG  1 
ATOM   383  O  OD1 . ASP A 1 52  ? -12.341 9.802   32.757  1.00 36.96 ? 52  ASP A OD1 1 
ATOM   384  O  OD2 . ASP A 1 52  ? -10.880 11.124  31.795  1.00 35.62 ? 52  ASP A OD2 1 
ATOM   385  N  N   . ASN A 1 53  ? -13.285 6.847   32.840  1.00 36.77 ? 53  ASN A N   1 
ATOM   386  C  CA  . ASN A 1 53  ? -14.716 6.577   33.015  1.00 36.82 ? 53  ASN A CA  1 
ATOM   387  C  C   . ASN A 1 53  ? -15.391 7.637   33.889  1.00 36.78 ? 53  ASN A C   1 
ATOM   388  O  O   . ASN A 1 53  ? -16.418 7.373   34.510  1.00 36.63 ? 53  ASN A O   1 
ATOM   389  C  CB  . ASN A 1 53  ? -14.905 5.178   33.631  1.00 37.13 ? 53  ASN A CB  1 
ATOM   390  C  CG  . ASN A 1 53  ? -16.358 4.708   33.616  1.00 38.19 ? 53  ASN A CG  1 
ATOM   391  O  OD1 . ASN A 1 53  ? -16.883 4.248   34.634  1.00 42.78 ? 53  ASN A OD1 1 
ATOM   392  N  ND2 . ASN A 1 53  ? -17.008 4.827   32.469  1.00 39.72 ? 53  ASN A ND2 1 
ATOM   393  N  N   . THR A 1 54  ? -14.827 8.841   33.931  1.00 36.62 ? 54  THR A N   1 
ATOM   394  C  CA  . THR A 1 54  ? -15.322 9.880   34.833  1.00 37.06 ? 54  THR A CA  1 
ATOM   395  C  C   . THR A 1 54  ? -16.694 10.427  34.439  1.00 37.37 ? 54  THR A C   1 
ATOM   396  O  O   . THR A 1 54  ? -17.398 10.968  35.287  1.00 37.73 ? 54  THR A O   1 
ATOM   397  C  CB  . THR A 1 54  ? -14.339 11.055  34.938  1.00 37.02 ? 54  THR A CB  1 
ATOM   398  O  OG1 . THR A 1 54  ? -14.055 11.557  33.635  1.00 36.99 ? 54  THR A OG1 1 
ATOM   399  C  CG2 . THR A 1 54  ? -13.045 10.613  35.602  1.00 37.19 ? 54  THR A CG2 1 
ATOM   400  N  N   . ALA A 1 55  ? -17.042 10.316  33.158  1.00 37.81 ? 55  ALA A N   1 
ATOM   401  C  CA  . ALA A 1 55  ? -18.375 10.687  32.663  1.00 38.08 ? 55  ALA A CA  1 
ATOM   402  C  C   . ALA A 1 55  ? -18.999 9.540   31.881  1.00 38.33 ? 55  ALA A C   1 
ATOM   403  O  O   . ALA A 1 55  ? -19.584 9.753   30.821  1.00 39.15 ? 55  ALA A O   1 
ATOM   404  C  CB  . ALA A 1 55  ? -18.290 11.936  31.792  1.00 38.18 ? 55  ALA A CB  1 
ATOM   405  N  N   . GLY A 1 56  ? -18.876 8.321   32.400  1.00 38.42 ? 56  GLY A N   1 
ATOM   406  C  CA  . GLY A 1 56  ? -19.350 7.139   31.687  1.00 38.47 ? 56  GLY A CA  1 
ATOM   407  C  C   . GLY A 1 56  ? -18.475 6.828   30.489  1.00 38.68 ? 56  GLY A C   1 
ATOM   408  O  O   . GLY A 1 56  ? -17.295 7.193   30.464  1.00 38.49 ? 56  GLY A O   1 
ATOM   409  N  N   . CYS A 1 57  ? -19.052 6.176   29.480  1.00 38.89 ? 57  CYS A N   1 
ATOM   410  C  CA  . CYS A 1 57  ? -18.285 5.748   28.309  1.00 39.11 ? 57  CYS A CA  1 
ATOM   411  C  C   . CYS A 1 57  ? -17.878 6.909   27.393  1.00 38.79 ? 57  CYS A C   1 
ATOM   412  O  O   . CYS A 1 57  ? -16.961 6.761   26.596  1.00 38.56 ? 57  CYS A O   1 
ATOM   413  C  CB  . CYS A 1 57  ? -19.036 4.657   27.528  1.00 39.49 ? 57  CYS A CB  1 
ATOM   414  S  SG  . CYS A 1 57  ? -19.305 3.117   28.496  1.00 42.92 ? 57  CYS A SG  1 
ATOM   415  N  N   . THR A 1 58  ? -18.529 8.064   27.532  1.00 38.89 ? 58  THR A N   1 
ATOM   416  C  CA  . THR A 1 58  ? -18.177 9.257   26.746  1.00 38.60 ? 58  THR A CA  1 
ATOM   417  C  C   . THR A 1 58  ? -16.739 9.725   27.000  1.00 38.21 ? 58  THR A C   1 
ATOM   418  O  O   . THR A 1 58  ? -16.065 10.209  26.085  1.00 37.78 ? 58  THR A O   1 
ATOM   419  C  CB  . THR A 1 58  ? -19.119 10.423  27.070  1.00 38.94 ? 58  THR A CB  1 
ATOM   420  O  OG1 . THR A 1 58  ? -20.469 10.026  26.816  1.00 40.14 ? 58  THR A OG1 1 
ATOM   421  C  CG2 . THR A 1 58  ? -18.800 11.641  26.214  1.00 39.27 ? 58  THR A CG2 1 
ATOM   422  N  N   . SER A 1 59  ? -16.296 9.573   28.248  1.00 37.49 ? 59  SER A N   1 
ATOM   423  C  CA  . SER A 1 59  ? -14.961 9.980   28.688  1.00 37.56 ? 59  SER A CA  1 
ATOM   424  C  C   . SER A 1 59  ? -13.813 9.192   28.041  1.00 37.13 ? 59  SER A C   1 
ATOM   425  O  O   . SER A 1 59  ? -12.663 9.623   28.097  1.00 37.04 ? 59  SER A O   1 
ATOM   426  C  CB  . SER A 1 59  ? -14.860 9.842   30.214  1.00 37.37 ? 59  SER A CB  1 
ATOM   427  O  OG  . SER A 1 59  ? -15.548 10.879  30.880  1.00 39.41 ? 59  SER A OG  1 
ATOM   428  N  N   . ALA A 1 60  ? -14.111 8.038   27.444  1.00 36.90 ? 60  ALA A N   1 
ATOM   429  C  CA  . ALA A 1 60  ? -13.090 7.226   26.786  1.00 37.19 ? 60  ALA A CA  1 
ATOM   430  C  C   . ALA A 1 60  ? -12.547 7.884   25.515  1.00 37.29 ? 60  ALA A C   1 
ATOM   431  O  O   . ALA A 1 60  ? -11.495 7.483   24.996  1.00 37.57 ? 60  ALA A O   1 
ATOM   432  C  CB  . ALA A 1 60  ? -13.640 5.837   26.474  1.00 36.75 ? 60  ALA A CB  1 
ATOM   433  N  N   . GLY A 1 61  ? -13.266 8.887   25.011  1.00 37.46 ? 61  GLY A N   1 
ATOM   434  C  CA  . GLY A 1 61  ? -12.800 9.671   23.883  1.00 37.26 ? 61  GLY A CA  1 
ATOM   435  C  C   . GLY A 1 61  ? -12.952 8.923   22.573  1.00 37.31 ? 61  GLY A C   1 
ATOM   436  O  O   . GLY A 1 61  ? -13.770 8.005   22.469  1.00 37.13 ? 61  GLY A O   1 
ATOM   437  N  N   . PRO A 1 62  ? -12.147 9.294   21.565  1.00 37.30 ? 62  PRO A N   1 
ATOM   438  C  CA  . PRO A 1 62  ? -12.310 8.746   20.227  1.00 37.28 ? 62  PRO A CA  1 
ATOM   439  C  C   . PRO A 1 62  ? -11.725 7.350   20.110  1.00 37.22 ? 62  PRO A C   1 
ATOM   440  O  O   . PRO A 1 62  ? -11.105 6.858   21.053  1.00 36.47 ? 62  PRO A O   1 
ATOM   441  C  CB  . PRO A 1 62  ? -11.520 9.728   19.360  1.00 37.56 ? 62  PRO A CB  1 
ATOM   442  C  CG  . PRO A 1 62  ? -10.431 10.208  20.257  1.00 37.66 ? 62  PRO A CG  1 
ATOM   443  C  CD  . PRO A 1 62  ? -11.014 10.237  21.640  1.00 37.57 ? 62  PRO A CD  1 
ATOM   444  N  N   . HIS A 1 63  ? -11.922 6.723   18.956  1.00 37.25 ? 63  HIS A N   1 
ATOM   445  C  CA  . HIS A 1 63  ? -11.255 5.466   18.635  1.00 37.70 ? 63  HIS A CA  1 
ATOM   446  C  C   . HIS A 1 63  ? -9.754  5.663   18.799  1.00 37.31 ? 63  HIS A C   1 
ATOM   447  O  O   . HIS A 1 63  ? -9.237  6.730   18.483  1.00 37.10 ? 63  HIS A O   1 
ATOM   448  C  CB  . HIS A 1 63  ? -11.525 5.043   17.191  1.00 38.42 ? 63  HIS A CB  1 
ATOM   449  C  CG  . HIS A 1 63  ? -12.929 4.600   16.934  1.00 39.23 ? 63  HIS A CG  1 
ATOM   450  N  ND1 . HIS A 1 63  ? -13.263 3.767   15.888  1.00 39.88 ? 63  HIS A ND1 1 
ATOM   451  C  CD2 . HIS A 1 63  ? -14.089 4.887   17.572  1.00 40.46 ? 63  HIS A CD2 1 
ATOM   452  C  CE1 . HIS A 1 63  ? -14.566 3.551   15.899  1.00 40.50 ? 63  HIS A CE1 1 
ATOM   453  N  NE2 . HIS A 1 63  ? -15.092 4.218   16.912  1.00 40.39 ? 63  HIS A NE2 1 
ATOM   454  N  N   . PHE A 1 64  ? -9.068  4.637   19.295  1.00 36.95 ? 64  PHE A N   1 
ATOM   455  C  CA  . PHE A 1 64  ? -7.612  4.678   19.432  1.00 36.84 ? 64  PHE A CA  1 
ATOM   456  C  C   . PHE A 1 64  ? -7.014  4.636   18.019  1.00 36.52 ? 64  PHE A C   1 
ATOM   457  O  O   . PHE A 1 64  ? -7.155  3.650   17.302  1.00 35.46 ? 64  PHE A O   1 
ATOM   458  C  CB  . PHE A 1 64  ? -7.117  3.520   20.318  1.00 36.89 ? 64  PHE A CB  1 
ATOM   459  C  CG  . PHE A 1 64  ? -5.624  3.493   20.529  1.00 36.91 ? 64  PHE A CG  1 
ATOM   460  C  CD1 . PHE A 1 64  ? -4.926  4.649   20.864  1.00 36.59 ? 64  PHE A CD1 1 
ATOM   461  C  CD2 . PHE A 1 64  ? -4.922  2.299   20.430  1.00 36.33 ? 64  PHE A CD2 1 
ATOM   462  C  CE1 . PHE A 1 64  ? -3.551  4.617   21.071  1.00 37.29 ? 64  PHE A CE1 1 
ATOM   463  C  CE2 . PHE A 1 64  ? -3.544  2.261   20.636  1.00 36.64 ? 64  PHE A CE2 1 
ATOM   464  C  CZ  . PHE A 1 64  ? -2.861  3.417   20.960  1.00 37.20 ? 64  PHE A CZ  1 
ATOM   465  N  N   . ASN A 1 65  ? -6.385  5.739   17.625  1.00 36.28 ? 65  ASN A N   1 
ATOM   466  C  CA  . ASN A 1 65  ? -5.950  5.939   16.256  1.00 36.63 ? 65  ASN A CA  1 
ATOM   467  C  C   . ASN A 1 65  ? -4.615  6.698   16.217  1.00 36.37 ? 65  ASN A C   1 
ATOM   468  O  O   . ASN A 1 65  ? -4.535  7.797   15.650  1.00 36.39 ? 65  ASN A O   1 
ATOM   469  C  CB  . ASN A 1 65  ? -7.045  6.692   15.478  1.00 36.31 ? 65  ASN A CB  1 
ATOM   470  C  CG  . ASN A 1 65  ? -6.749  6.807   13.992  1.00 36.77 ? 65  ASN A CG  1 
ATOM   471  O  OD1 . ASN A 1 65  ? -5.967  6.031   13.429  1.00 36.13 ? 65  ASN A OD1 1 
ATOM   472  N  ND2 . ASN A 1 65  ? -7.390  7.775   13.342  1.00 36.68 ? 65  ASN A ND2 1 
ATOM   473  N  N   . PRO A 1 66  ? -3.551  6.096   16.798  1.00 36.48 ? 66  PRO A N   1 
ATOM   474  C  CA  . PRO A 1 66  ? -2.243  6.756   16.898  1.00 36.71 ? 66  PRO A CA  1 
ATOM   475  C  C   . PRO A 1 66  ? -1.578  7.038   15.549  1.00 36.86 ? 66  PRO A C   1 
ATOM   476  O  O   . PRO A 1 66  ? -0.762  7.952   15.450  1.00 36.69 ? 66  PRO A O   1 
ATOM   477  C  CB  . PRO A 1 66  ? -1.405  5.759   17.715  1.00 36.49 ? 66  PRO A CB  1 
ATOM   478  C  CG  . PRO A 1 66  ? -2.047  4.454   17.499  1.00 36.75 ? 66  PRO A CG  1 
ATOM   479  C  CD  . PRO A 1 66  ? -3.511  4.737   17.369  1.00 36.39 ? 66  PRO A CD  1 
ATOM   480  N  N   . LEU A 1 67  ? -1.926  6.263   14.522  1.00 37.24 ? 67  LEU A N   1 
ATOM   481  C  CA  . LEU A 1 67  ? -1.349  6.444   13.193  1.00 37.28 ? 67  LEU A CA  1 
ATOM   482  C  C   . LEU A 1 67  ? -2.197  7.351   12.279  1.00 37.33 ? 67  LEU A C   1 
ATOM   483  O  O   . LEU A 1 67  ? -1.891  7.500   11.097  1.00 36.95 ? 67  LEU A O   1 
ATOM   484  C  CB  . LEU A 1 67  ? -1.120  5.082   12.529  1.00 37.41 ? 67  LEU A CB  1 
ATOM   485  C  CG  . LEU A 1 67  ? -0.182  4.112   13.251  1.00 37.86 ? 67  LEU A CG  1 
ATOM   486  C  CD1 . LEU A 1 67  ? -0.060  2.822   12.451  1.00 38.08 ? 67  LEU A CD1 1 
ATOM   487  C  CD2 . LEU A 1 67  ? 1.191   4.728   13.473  1.00 38.97 ? 67  LEU A CD2 1 
ATOM   488  N  N   . SER A 1 68  ? -3.255  7.946   12.831  1.00 37.47 ? 68  SER A N   1 
ATOM   489  C  CA  . SER A 1 68  ? -4.099  8.910   12.112  1.00 37.83 ? 68  SER A CA  1 
ATOM   490  C  C   . SER A 1 68  ? -4.621  8.397   10.771  1.00 37.85 ? 68  SER A C   1 
ATOM   491  O  O   . SER A 1 68  ? -4.492  9.062   9.737   1.00 38.08 ? 68  SER A O   1 
ATOM   492  C  CB  . SER A 1 68  ? -3.351  10.226  11.926  1.00 37.68 ? 68  SER A CB  1 
ATOM   493  O  OG  . SER A 1 68  ? -2.887  10.695  13.175  1.00 38.74 ? 68  SER A OG  1 
ATOM   494  N  N   . ARG A 1 69  ? -5.216  7.213   10.802  1.00 38.03 ? 69  ARG A N   1 
ATOM   495  C  CA  . ARG A 1 69  ? -5.782  6.598   9.609   1.00 38.54 ? 69  ARG A CA  1 
ATOM   496  C  C   . ARG A 1 69  ? -7.298  6.721   9.590   1.00 38.01 ? 69  ARG A C   1 
ATOM   497  O  O   . ARG A 1 69  ? -7.905  7.147   10.570  1.00 37.48 ? 69  ARG A O   1 
ATOM   498  C  CB  . ARG A 1 69  ? -5.357  5.135   9.539   1.00 38.77 ? 69  ARG A CB  1 
ATOM   499  C  CG  . ARG A 1 69  ? -3.845  4.986   9.442   1.00 40.90 ? 69  ARG A CG  1 
ATOM   500  C  CD  . ARG A 1 69  ? -3.436  3.632   8.919   1.00 41.43 ? 69  ARG A CD  1 
ATOM   501  N  NE  . ARG A 1 69  ? -1.982  3.502   8.823   1.00 42.44 ? 69  ARG A NE  1 
ATOM   502  C  CZ  . ARG A 1 69  ? -1.356  2.439   8.321   1.00 43.65 ? 69  ARG A CZ  1 
ATOM   503  N  NH1 . ARG A 1 69  ? -2.057  1.403   7.859   1.00 45.00 ? 69  ARG A NH1 1 
ATOM   504  N  NH2 . ARG A 1 69  ? -0.027  2.407   8.271   1.00 43.50 ? 69  ARG A NH2 1 
ATOM   505  N  N   . LYS A 1 70  ? -7.902  6.370   8.457   1.00 37.80 ? 70  LYS A N   1 
ATOM   506  C  CA  . LYS A 1 70  ? -9.359  6.318   8.363   1.00 37.65 ? 70  LYS A CA  1 
ATOM   507  C  C   . LYS A 1 70  ? -9.901  5.062   9.042   1.00 37.15 ? 70  LYS A C   1 
ATOM   508  O  O   . LYS A 1 70  ? -9.199  4.060   9.166   1.00 36.92 ? 70  LYS A O   1 
ATOM   509  C  CB  . LYS A 1 70  ? -9.805  6.368   6.901   1.00 37.67 ? 70  LYS A CB  1 
ATOM   510  C  CG  . LYS A 1 70  ? -9.534  7.709   6.253   1.00 38.16 ? 70  LYS A CG  1 
ATOM   511  C  CD  . LYS A 1 70  ? -10.222 7.845   4.910   1.00 38.56 ? 70  LYS A CD  1 
ATOM   512  C  CE  . LYS A 1 70  ? -9.977  9.222   4.307   1.00 39.27 ? 70  LYS A CE  1 
ATOM   513  N  NZ  . LYS A 1 70  ? -10.553 10.302  5.164   1.00 40.51 ? 70  LYS A NZ  1 
ATOM   514  N  N   . HIS A 1 71  ? -11.151 5.135   9.494   1.00 36.61 ? 71  HIS A N   1 
ATOM   515  C  CA  . HIS A 1 71  ? -11.830 4.000   10.089  1.00 36.45 ? 71  HIS A CA  1 
ATOM   516  C  C   . HIS A 1 71  ? -12.071 2.907   9.055   1.00 36.20 ? 71  HIS A C   1 
ATOM   517  O  O   . HIS A 1 71  ? -12.477 3.193   7.926   1.00 36.09 ? 71  HIS A O   1 
ATOM   518  C  CB  . HIS A 1 71  ? -13.179 4.424   10.680  1.00 36.07 ? 71  HIS A CB  1 
ATOM   519  C  CG  . HIS A 1 71  ? -13.972 3.283   11.226  1.00 36.26 ? 71  HIS A CG  1 
ATOM   520  N  ND1 . HIS A 1 71  ? -13.637 2.638   12.397  1.00 34.91 ? 71  HIS A ND1 1 
ATOM   521  C  CD2 . HIS A 1 71  ? -15.076 2.662   10.757  1.00 35.23 ? 71  HIS A CD2 1 
ATOM   522  C  CE1 . HIS A 1 71  ? -14.502 1.668   12.625  1.00 36.22 ? 71  HIS A CE1 1 
ATOM   523  N  NE2 . HIS A 1 71  ? -15.384 1.658   11.640  1.00 35.47 ? 71  HIS A NE2 1 
ATOM   524  N  N   . GLY A 1 72  ? -11.821 1.662   9.448   1.00 36.16 ? 72  GLY A N   1 
ATOM   525  C  CA  . GLY A 1 72  ? -12.075 0.503   8.592   1.00 36.35 ? 72  GLY A CA  1 
ATOM   526  C  C   . GLY A 1 72  ? -12.479 -0.715  9.402   1.00 36.37 ? 72  GLY A C   1 
ATOM   527  O  O   . GLY A 1 72  ? -12.765 -0.613  10.588  1.00 36.28 ? 72  GLY A O   1 
ATOM   528  N  N   . GLY A 1 73  ? -12.514 -1.869  8.746   1.00 36.44 ? 73  GLY A N   1 
ATOM   529  C  CA  . GLY A 1 73  ? -12.721 -3.138  9.435   1.00 36.72 ? 73  GLY A CA  1 
ATOM   530  C  C   . GLY A 1 73  ? -11.384 -3.717  9.864   1.00 36.88 ? 73  GLY A C   1 
ATOM   531  O  O   . GLY A 1 73  ? -10.342 -3.277  9.370   1.00 36.85 ? 73  GLY A O   1 
ATOM   532  N  N   . PRO A 1 74  ? -11.398 -4.703  10.785  1.00 37.35 ? 74  PRO A N   1 
ATOM   533  C  CA  . PRO A 1 74  ? -10.161 -5.293  11.305  1.00 37.63 ? 74  PRO A CA  1 
ATOM   534  C  C   . PRO A 1 74  ? -9.261  -5.920  10.241  1.00 37.86 ? 74  PRO A C   1 
ATOM   535  O  O   . PRO A 1 74  ? -8.049  -5.975  10.431  1.00 37.38 ? 74  PRO A O   1 
ATOM   536  C  CB  . PRO A 1 74  ? -10.660 -6.367  12.284  1.00 37.83 ? 74  PRO A CB  1 
ATOM   537  C  CG  . PRO A 1 74  ? -12.072 -6.620  11.910  1.00 37.72 ? 74  PRO A CG  1 
ATOM   538  C  CD  . PRO A 1 74  ? -12.586 -5.308  11.409  1.00 37.61 ? 74  PRO A CD  1 
ATOM   539  N  N   . LYS A 1 75  ? -9.846  -6.384  9.137   1.00 38.04 ? 75  LYS A N   1 
ATOM   540  C  CA  . LYS A 1 75  ? -9.080  -7.002  8.049   1.00 38.60 ? 75  LYS A CA  1 
ATOM   541  C  C   . LYS A 1 75  ? -8.411  -5.989  7.104   1.00 38.53 ? 75  LYS A C   1 
ATOM   542  O  O   . LYS A 1 75  ? -7.562  -6.366  6.293   1.00 38.65 ? 75  LYS A O   1 
ATOM   543  C  CB  . LYS A 1 75  ? -9.981  -7.928  7.229   1.00 38.70 ? 75  LYS A CB  1 
ATOM   544  C  CG  . LYS A 1 75  ? -10.548 -9.111  8.007   1.00 39.82 ? 75  LYS A CG  1 
ATOM   545  C  CD  . LYS A 1 75  ? -11.540 -9.929  7.167   1.00 40.32 ? 75  LYS A CD  1 
ATOM   546  C  CE  . LYS A 1 75  ? -10.885 -10.604 5.971   1.00 42.11 ? 75  LYS A CE  1 
ATOM   547  N  NZ  . LYS A 1 75  ? -9.702  -11.446 6.341   1.00 43.22 ? 75  LYS A NZ  1 
ATOM   548  N  N   . ASP A 1 76  ? -8.801  -4.719  7.200   1.00 38.60 ? 76  ASP A N   1 
ATOM   549  C  CA  . ASP A 1 76  ? -8.299  -3.681  6.297   1.00 38.85 ? 76  ASP A CA  1 
ATOM   550  C  C   . ASP A 1 76  ? -6.927  -3.185  6.712   1.00 38.95 ? 76  ASP A C   1 
ATOM   551  O  O   . ASP A 1 76  ? -6.645  -3.081  7.901   1.00 38.59 ? 76  ASP A O   1 
ATOM   552  C  CB  . ASP A 1 76  ? -9.252  -2.485  6.280   1.00 38.80 ? 76  ASP A CB  1 
ATOM   553  C  CG  . ASP A 1 76  ? -10.615 -2.828  5.721   1.00 38.80 ? 76  ASP A CG  1 
ATOM   554  O  OD1 . ASP A 1 76  ? -10.727 -3.801  4.949   1.00 38.71 ? 76  ASP A OD1 1 
ATOM   555  O  OD2 . ASP A 1 76  ? -11.577 -2.108  6.044   1.00 38.84 ? 76  ASP A OD2 1 
ATOM   556  N  N   . GLU A 1 77  ? -6.087  -2.863  5.731   1.00 39.47 ? 77  GLU A N   1 
ATOM   557  C  CA  . GLU A 1 77  ? -4.816  -2.189  6.006   1.00 39.59 ? 77  GLU A CA  1 
ATOM   558  C  C   . GLU A 1 77  ? -5.105  -0.779  6.526   1.00 39.49 ? 77  GLU A C   1 
ATOM   559  O  O   . GLU A 1 77  ? -4.482  -0.325  7.490   1.00 39.58 ? 77  GLU A O   1 
ATOM   560  C  CB  . GLU A 1 77  ? -3.932  -2.133  4.755   1.00 39.95 ? 77  GLU A CB  1 
ATOM   561  C  CG  . GLU A 1 77  ? -2.500  -1.682  5.029   1.00 40.55 ? 77  GLU A CG  1 
ATOM   562  C  CD  . GLU A 1 77  ? -1.640  -1.631  3.776   1.00 41.95 ? 77  GLU A CD  1 
ATOM   563  O  OE1 . GLU A 1 77  ? -1.436  -2.686  3.118   1.00 46.12 ? 77  GLU A OE1 1 
ATOM   564  O  OE2 . GLU A 1 77  ? -1.152  -0.526  3.438   1.00 46.23 ? 77  GLU A OE2 1 
ATOM   565  N  N   . GLU A 1 78  ? -6.070  -0.108  5.892   1.00 39.07 ? 78  GLU A N   1 
ATOM   566  C  CA  . GLU A 1 78  ? -6.528  1.218   6.319   1.00 38.39 ? 78  GLU A CA  1 
ATOM   567  C  C   . GLU A 1 78  ? -7.548  1.094   7.457   1.00 37.67 ? 78  GLU A C   1 
ATOM   568  O  O   . GLU A 1 78  ? -8.734  0.851   7.228   1.00 36.95 ? 78  GLU A O   1 
ATOM   569  C  CB  . GLU A 1 78  ? -7.134  1.976   5.128   1.00 38.91 ? 78  GLU A CB  1 
ATOM   570  C  CG  . GLU A 1 78  ? -7.402  3.463   5.375   1.00 39.53 ? 78  GLU A CG  1 
ATOM   571  C  CD  . GLU A 1 78  ? -6.137  4.296   5.534   1.00 40.84 ? 78  GLU A CD  1 
ATOM   572  O  OE1 . GLU A 1 78  ? -5.076  3.911   4.986   1.00 42.05 ? 78  GLU A OE1 1 
ATOM   573  O  OE2 . GLU A 1 78  ? -6.212  5.353   6.198   1.00 40.63 ? 78  GLU A OE2 1 
ATOM   574  N  N   . ARG A 1 79  ? -7.075  1.267   8.688   1.00 36.87 ? 79  ARG A N   1 
ATOM   575  C  CA  . ARG A 1 79  ? -7.928  1.146   9.875   1.00 36.61 ? 79  ARG A CA  1 
ATOM   576  C  C   . ARG A 1 79  ? -7.287  1.840   11.066  1.00 36.28 ? 79  ARG A C   1 
ATOM   577  O  O   . ARG A 1 79  ? -6.083  2.128   11.052  1.00 36.69 ? 79  ARG A O   1 
ATOM   578  C  CB  . ARG A 1 79  ? -8.149  -0.324  10.224  1.00 36.48 ? 79  ARG A CB  1 
ATOM   579  C  CG  . ARG A 1 79  ? -6.858  -1.099  10.487  1.00 36.37 ? 79  ARG A CG  1 
ATOM   580  C  CD  . ARG A 1 79  ? -7.136  -2.475  11.077  1.00 36.28 ? 79  ARG A CD  1 
ATOM   581  N  NE  . ARG A 1 79  ? -7.228  -2.433  12.538  1.00 36.01 ? 79  ARG A NE  1 
ATOM   582  C  CZ  . ARG A 1 79  ? -7.186  -3.502  13.329  1.00 35.85 ? 79  ARG A CZ  1 
ATOM   583  N  NH1 . ARG A 1 79  ? -7.080  -4.716  12.819  1.00 35.93 ? 79  ARG A NH1 1 
ATOM   584  N  NH2 . ARG A 1 79  ? -7.244  -3.351  14.646  1.00 36.44 ? 79  ARG A NH2 1 
ATOM   585  N  N   . HIS A 1 80  ? -8.092  2.102   12.091  1.00 35.89 ? 80  HIS A N   1 
ATOM   586  C  CA  . HIS A 1 80  ? -7.573  2.570   13.377  1.00 35.94 ? 80  HIS A CA  1 
ATOM   587  C  C   . HIS A 1 80  ? -6.968  1.382   14.105  1.00 35.65 ? 80  HIS A C   1 
ATOM   588  O  O   . HIS A 1 80  ? -7.392  0.249   13.901  1.00 35.46 ? 80  HIS A O   1 
ATOM   589  C  CB  . HIS A 1 80  ? -8.681  3.155   14.249  1.00 35.73 ? 80  HIS A CB  1 
ATOM   590  C  CG  . HIS A 1 80  ? -9.433  4.283   13.618  1.00 36.43 ? 80  HIS A CG  1 
ATOM   591  N  ND1 . HIS A 1 80  ? -10.720 4.613   13.984  1.00 35.97 ? 80  HIS A ND1 1 
ATOM   592  C  CD2 . HIS A 1 80  ? -9.084  5.152   12.643  1.00 36.10 ? 80  HIS A CD2 1 
ATOM   593  C  CE1 . HIS A 1 80  ? -11.129 5.640   13.261  1.00 36.52 ? 80  HIS A CE1 1 
ATOM   594  N  NE2 . HIS A 1 80  ? -10.153 5.991   12.445  1.00 35.81 ? 80  HIS A NE2 1 
ATOM   595  N  N   . VAL A 1 81  ? -6.007  1.625   14.991  1.00 35.73 ? 81  VAL A N   1 
ATOM   596  C  CA  . VAL A 1 81  ? -5.520  0.534   15.838  1.00 35.72 ? 81  VAL A CA  1 
ATOM   597  C  C   . VAL A 1 81  ? -6.696  -0.131  16.579  1.00 35.65 ? 81  VAL A C   1 
ATOM   598  O  O   . VAL A 1 81  ? -6.759  -1.359  16.687  1.00 36.02 ? 81  VAL A O   1 
ATOM   599  C  CB  . VAL A 1 81  ? -4.434  1.011   16.825  1.00 35.81 ? 81  VAL A CB  1 
ATOM   600  C  CG1 . VAL A 1 81  ? -4.121  -0.074  17.853  1.00 35.69 ? 81  VAL A CG1 1 
ATOM   601  C  CG2 . VAL A 1 81  ? -3.184  1.408   16.055  1.00 35.94 ? 81  VAL A CG2 1 
ATOM   602  N  N   . GLY A 1 82  ? -7.639  0.674   17.060  1.00 35.69 ? 82  GLY A N   1 
ATOM   603  C  CA  . GLY A 1 82  ? -8.767  0.167   17.833  1.00 36.01 ? 82  GLY A CA  1 
ATOM   604  C  C   . GLY A 1 82  ? -9.936  -0.436  17.076  1.00 36.34 ? 82  GLY A C   1 
ATOM   605  O  O   . GLY A 1 82  ? -10.936 -0.793  17.694  1.00 36.19 ? 82  GLY A O   1 
ATOM   606  N  N   . ASP A 1 83  ? -9.824  -0.569  15.757  1.00 36.18 ? 83  ASP A N   1 
ATOM   607  C  CA  . ASP A 1 83  ? -10.944 -1.041  14.929  1.00 36.38 ? 83  ASP A CA  1 
ATOM   608  C  C   . ASP A 1 83  ? -11.038 -2.562  14.954  1.00 36.33 ? 83  ASP A C   1 
ATOM   609  O  O   . ASP A 1 83  ? -10.450 -3.228  14.105  1.00 37.28 ? 83  ASP A O   1 
ATOM   610  C  CB  . ASP A 1 83  ? -10.783 -0.570  13.481  1.00 36.09 ? 83  ASP A CB  1 
ATOM   611  C  CG  . ASP A 1 83  ? -11.141 0.896   13.284  1.00 35.83 ? 83  ASP A CG  1 
ATOM   612  O  OD1 . ASP A 1 83  ? -11.786 1.499   14.167  1.00 35.96 ? 83  ASP A OD1 1 
ATOM   613  O  OD2 . ASP A 1 83  ? -10.795 1.445   12.214  1.00 37.29 ? 83  ASP A OD2 1 
ATOM   614  N  N   . LEU A 1 84  ? -11.789 -3.108  15.911  1.00 36.64 ? 84  LEU A N   1 
ATOM   615  C  CA  . LEU A 1 84  ? -11.960 -4.565  16.020  1.00 36.67 ? 84  LEU A CA  1 
ATOM   616  C  C   . LEU A 1 84  ? -13.281 -5.070  15.432  1.00 36.90 ? 84  LEU A C   1 
ATOM   617  O  O   . LEU A 1 84  ? -13.702 -6.192  15.713  1.00 37.52 ? 84  LEU A O   1 
ATOM   618  C  CB  . LEU A 1 84  ? -11.812 -5.018  17.477  1.00 36.90 ? 84  LEU A CB  1 
ATOM   619  C  CG  . LEU A 1 84  ? -10.455 -4.723  18.132  1.00 37.44 ? 84  LEU A CG  1 
ATOM   620  C  CD1 . LEU A 1 84  ? -10.510 -5.049  19.610  1.00 37.50 ? 84  LEU A CD1 1 
ATOM   621  C  CD2 . LEU A 1 84  ? -9.335  -5.498  17.457  1.00 38.10 ? 84  LEU A CD2 1 
ATOM   622  N  N   . GLY A 1 85  ? -13.932 -4.236  14.627  1.00 36.54 ? 85  GLY A N   1 
ATOM   623  C  CA  . GLY A 1 85  ? -15.086 -4.653  13.853  1.00 36.11 ? 85  GLY A CA  1 
ATOM   624  C  C   . GLY A 1 85  ? -16.366 -4.752  14.654  1.00 35.58 ? 85  GLY A C   1 
ATOM   625  O  O   . GLY A 1 85  ? -16.713 -3.826  15.389  1.00 35.22 ? 85  GLY A O   1 
ATOM   626  N  N   . ASN A 1 86  ? -17.062 -5.876  14.486  1.00 35.56 ? 86  ASN A N   1 
ATOM   627  C  CA  . ASN A 1 86  ? -18.350 -6.130  15.125  1.00 35.63 ? 86  ASN A CA  1 
ATOM   628  C  C   . ASN A 1 86  ? -18.340 -7.426  15.907  1.00 35.78 ? 86  ASN A C   1 
ATOM   629  O  O   . ASN A 1 86  ? -17.678 -8.385  15.521  1.00 36.06 ? 86  ASN A O   1 
ATOM   630  C  CB  . ASN A 1 86  ? -19.464 -6.239  14.070  1.00 35.42 ? 86  ASN A CB  1 
ATOM   631  C  CG  . ASN A 1 86  ? -19.837 -4.903  13.470  1.00 35.38 ? 86  ASN A CG  1 
ATOM   632  O  OD1 . ASN A 1 86  ? -20.291 -4.004  14.179  1.00 34.89 ? 86  ASN A OD1 1 
ATOM   633  N  ND2 . ASN A 1 86  ? -19.657 -4.765  12.151  1.00 34.45 ? 86  ASN A ND2 1 
ATOM   634  N  N   . VAL A 1 87  ? -19.102 -7.450  16.995  1.00 35.78 ? 87  VAL A N   1 
ATOM   635  C  CA  . VAL A 1 87  ? -19.473 -8.701  17.643  1.00 36.02 ? 87  VAL A CA  1 
ATOM   636  C  C   . VAL A 1 87  ? -20.927 -8.984  17.277  1.00 35.91 ? 87  VAL A C   1 
ATOM   637  O  O   . VAL A 1 87  ? -21.673 -8.063  16.945  1.00 35.88 ? 87  VAL A O   1 
ATOM   638  C  CB  . VAL A 1 87  ? -19.293 -8.662  19.172  1.00 36.32 ? 87  VAL A CB  1 
ATOM   639  C  CG1 . VAL A 1 87  ? -17.830 -8.421  19.512  1.00 37.07 ? 87  VAL A CG1 1 
ATOM   640  C  CG2 . VAL A 1 87  ? -20.183 -7.608  19.816  1.00 36.44 ? 87  VAL A CG2 1 
ATOM   641  N  N   . THR A 1 88  ? -21.317 -10.253 17.334  1.00 35.75 ? 88  THR A N   1 
ATOM   642  C  CA  . THR A 1 88  ? -22.662 -10.664 16.930  1.00 35.97 ? 88  THR A CA  1 
ATOM   643  C  C   . THR A 1 88  ? -23.414 -11.252 18.112  1.00 35.94 ? 88  THR A C   1 
ATOM   644  O  O   . THR A 1 88  ? -22.949 -12.211 18.722  1.00 36.05 ? 88  THR A O   1 
ATOM   645  C  CB  . THR A 1 88  ? -22.622 -11.724 15.803  1.00 35.99 ? 88  THR A CB  1 
ATOM   646  O  OG1 . THR A 1 88  ? -21.829 -11.244 14.708  1.00 36.24 ? 88  THR A OG1 1 
ATOM   647  C  CG2 . THR A 1 88  ? -24.026 -12.038 15.309  1.00 35.76 ? 88  THR A CG2 1 
ATOM   648  N  N   . ALA A 1 89  ? -24.574 -10.677 18.423  1.00 36.03 ? 89  ALA A N   1 
ATOM   649  C  CA  . ALA A 1 89  ? -25.436 -11.183 19.486  1.00 36.09 ? 89  ALA A CA  1 
ATOM   650  C  C   . ALA A 1 89  ? -26.508 -12.110 18.915  1.00 36.30 ? 89  ALA A C   1 
ATOM   651  O  O   . ALA A 1 89  ? -27.061 -11.855 17.843  1.00 36.12 ? 89  ALA A O   1 
ATOM   652  C  CB  . ALA A 1 89  ? -26.084 -10.031 20.238  1.00 36.17 ? 89  ALA A CB  1 
ATOM   653  N  N   . ASP A 1 90  ? -26.793 -13.187 19.636  1.00 36.51 ? 90  ASP A N   1 
ATOM   654  C  CA  . ASP A 1 90  ? -27.848 -14.120 19.241  1.00 36.67 ? 90  ASP A CA  1 
ATOM   655  C  C   . ASP A 1 90  ? -29.229 -13.585 19.633  1.00 36.87 ? 90  ASP A C   1 
ATOM   656  O  O   . ASP A 1 90  ? -29.343 -12.468 20.145  1.00 36.83 ? 90  ASP A O   1 
ATOM   657  C  CB  . ASP A 1 90  ? -27.590 -15.512 19.838  1.00 36.73 ? 90  ASP A CB  1 
ATOM   658  C  CG  . ASP A 1 90  ? -27.570 -15.520 21.354  1.00 36.77 ? 90  ASP A CG  1 
ATOM   659  O  OD1 . ASP A 1 90  ? -28.028 -14.544 21.986  1.00 37.75 ? 90  ASP A OD1 1 
ATOM   660  O  OD2 . ASP A 1 90  ? -27.085 -16.520 21.916  1.00 36.85 ? 90  ASP A OD2 1 
ATOM   661  N  N   . LYS A 1 91  ? -30.268 -14.383 19.387  1.00 36.98 ? 91  LYS A N   1 
ATOM   662  C  CA  . LYS A 1 91  ? -31.648 -14.007 19.705  1.00 37.24 ? 91  LYS A CA  1 
ATOM   663  C  C   . LYS A 1 91  ? -31.910 -13.810 21.201  1.00 37.25 ? 91  LYS A C   1 
ATOM   664  O  O   . LYS A 1 91  ? -32.905 -13.186 21.575  1.00 37.59 ? 91  LYS A O   1 
ATOM   665  C  CB  . LYS A 1 91  ? -32.622 -15.054 19.151  1.00 37.44 ? 91  LYS A CB  1 
ATOM   666  C  CG  . LYS A 1 91  ? -32.527 -16.417 19.829  1.00 37.90 ? 91  LYS A CG  1 
ATOM   667  C  CD  . LYS A 1 91  ? -33.544 -17.393 19.274  1.00 38.05 ? 91  LYS A CD  1 
ATOM   668  C  CE  . LYS A 1 91  ? -33.533 -18.706 20.046  1.00 38.99 ? 91  LYS A CE  1 
ATOM   669  N  NZ  . LYS A 1 91  ? -33.695 -18.502 21.514  1.00 39.26 ? 91  LYS A NZ  1 
ATOM   670  N  N   . ASP A 1 92  ? -31.042 -14.367 22.046  1.00 37.15 ? 92  ASP A N   1 
ATOM   671  C  CA  . ASP A 1 92  ? -31.128 -14.184 23.500  1.00 37.26 ? 92  ASP A CA  1 
ATOM   672  C  C   . ASP A 1 92  ? -30.266 -13.006 23.976  1.00 37.19 ? 92  ASP A C   1 
ATOM   673  O  O   . ASP A 1 92  ? -30.149 -12.758 25.180  1.00 36.73 ? 92  ASP A O   1 
ATOM   674  C  CB  . ASP A 1 92  ? -30.697 -15.464 24.223  1.00 37.41 ? 92  ASP A CB  1 
ATOM   675  C  CG  . ASP A 1 92  ? -31.499 -16.676 23.794  1.00 38.35 ? 92  ASP A CG  1 
ATOM   676  O  OD1 . ASP A 1 92  ? -32.738 -16.647 23.931  1.00 38.61 ? 92  ASP A OD1 1 
ATOM   677  O  OD2 . ASP A 1 92  ? -30.889 -17.661 23.324  1.00 40.43 ? 92  ASP A OD2 1 
ATOM   678  N  N   . GLY A 1 93  ? -29.656 -12.298 23.028  1.00 37.02 ? 93  GLY A N   1 
ATOM   679  C  CA  . GLY A 1 93  ? -28.885 -11.097 23.314  1.00 37.20 ? 93  GLY A CA  1 
ATOM   680  C  C   . GLY A 1 93  ? -27.467 -11.327 23.799  1.00 37.14 ? 93  GLY A C   1 
ATOM   681  O  O   . GLY A 1 93  ? -26.867 -10.425 24.376  1.00 37.15 ? 93  GLY A O   1 
ATOM   682  N  N   . VAL A 1 94  ? -26.931 -12.520 23.551  1.00 37.20 ? 94  VAL A N   1 
ATOM   683  C  CA  . VAL A 1 94  ? -25.605 -12.898 24.019  1.00 37.44 ? 94  VAL A CA  1 
ATOM   684  C  C   . VAL A 1 94  ? -24.636 -12.981 22.843  1.00 37.68 ? 94  VAL A C   1 
ATOM   685  O  O   . VAL A 1 94  ? -24.898 -13.668 21.853  1.00 37.56 ? 94  VAL A O   1 
ATOM   686  C  CB  . VAL A 1 94  ? -25.631 -14.252 24.772  1.00 37.50 ? 94  VAL A CB  1 
ATOM   687  C  CG1 . VAL A 1 94  ? -24.215 -14.678 25.182  1.00 37.50 ? 94  VAL A CG1 1 
ATOM   688  C  CG2 . VAL A 1 94  ? -26.520 -14.149 25.999  1.00 37.35 ? 94  VAL A CG2 1 
ATOM   689  N  N   . ALA A 1 95  ? -23.521 -12.276 22.970  1.00 37.67 ? 95  ALA A N   1 
ATOM   690  C  CA  . ALA A 1 95  ? -22.469 -12.275 21.960  1.00 38.03 ? 95  ALA A CA  1 
ATOM   691  C  C   . ALA A 1 95  ? -21.240 -12.984 22.502  1.00 38.34 ? 95  ALA A C   1 
ATOM   692  O  O   . ALA A 1 95  ? -20.595 -12.488 23.433  1.00 38.68 ? 95  ALA A O   1 
ATOM   693  C  CB  . ALA A 1 95  ? -22.118 -10.846 21.568  1.00 37.85 ? 95  ALA A CB  1 
ATOM   694  N  N   . ASP A 1 96  ? -20.927 -14.149 21.934  1.00 38.58 ? 96  ASP A N   1 
ATOM   695  C  CA  . ASP A 1 96  ? -19.676 -14.840 22.247  1.00 38.86 ? 96  ASP A CA  1 
ATOM   696  C  C   . ASP A 1 96  ? -18.588 -14.337 21.307  1.00 38.76 ? 96  ASP A C   1 
ATOM   697  O  O   . ASP A 1 96  ? -18.754 -14.353 20.089  1.00 38.45 ? 96  ASP A O   1 
ATOM   698  C  CB  . ASP A 1 96  ? -19.824 -16.358 22.123  1.00 39.09 ? 96  ASP A CB  1 
ATOM   699  C  CG  . ASP A 1 96  ? -20.633 -16.970 23.261  1.00 39.46 ? 96  ASP A CG  1 
ATOM   700  O  OD1 . ASP A 1 96  ? -20.656 -16.411 24.387  1.00 40.85 ? 96  ASP A OD1 1 
ATOM   701  O  OD2 . ASP A 1 96  ? -21.245 -18.033 23.027  1.00 39.97 ? 96  ASP A OD2 1 
ATOM   702  N  N   . VAL A 1 97  ? -17.480 -13.897 21.894  1.00 38.72 ? 97  VAL A N   1 
ATOM   703  C  CA  . VAL A 1 97  ? -16.384 -13.258 21.172  1.00 38.91 ? 97  VAL A CA  1 
ATOM   704  C  C   . VAL A 1 97  ? -15.169 -14.180 21.208  1.00 38.93 ? 97  VAL A C   1 
ATOM   705  O  O   . VAL A 1 97  ? -14.816 -14.695 22.271  1.00 38.22 ? 97  VAL A O   1 
ATOM   706  C  CB  . VAL A 1 97  ? -16.032 -11.907 21.832  1.00 39.05 ? 97  VAL A CB  1 
ATOM   707  C  CG1 . VAL A 1 97  ? -14.825 -11.248 21.155  1.00 38.22 ? 97  VAL A CG1 1 
ATOM   708  C  CG2 . VAL A 1 97  ? -17.246 -10.981 21.807  1.00 39.86 ? 97  VAL A CG2 1 
ATOM   709  N  N   . SER A 1 98  ? -14.550 -14.410 20.049  1.00 39.33 ? 98  SER A N   1 
ATOM   710  C  CA  . SER A 1 98  ? -13.355 -15.254 19.974  1.00 39.58 ? 98  SER A CA  1 
ATOM   711  C  C   . SER A 1 98  ? -12.511 -14.937 18.745  1.00 40.04 ? 98  SER A C   1 
ATOM   712  O  O   . SER A 1 98  ? -12.421 -15.752 17.816  1.00 40.50 ? 98  SER A O   1 
ATOM   713  C  CB  . SER A 1 98  ? -13.743 -16.730 19.965  1.00 39.88 ? 98  SER A CB  1 
ATOM   714  O  OG  . SER A 1 98  ? -12.591 -17.550 19.867  1.00 39.84 ? 98  SER A OG  1 
ATOM   715  N  N   . ILE A 1 99  ? -11.886 -13.761 18.751  1.00 40.03 ? 99  ILE A N   1 
ATOM   716  C  CA  . ILE A 1 99  ? -11.133 -13.277 17.594  1.00 40.17 ? 99  ILE A CA  1 
ATOM   717  C  C   . ILE A 1 99  ? -9.638  -13.201 17.876  1.00 40.00 ? 99  ILE A C   1 
ATOM   718  O  O   . ILE A 1 99  ? -9.184  -13.416 19.007  1.00 39.91 ? 99  ILE A O   1 
ATOM   719  C  CB  . ILE A 1 99  ? -11.627 -11.883 17.130  1.00 40.37 ? 99  ILE A CB  1 
ATOM   720  C  CG1 . ILE A 1 99  ? -11.341 -10.820 18.189  1.00 40.91 ? 99  ILE A CG1 1 
ATOM   721  C  CG2 . ILE A 1 99  ? -13.119 -11.935 16.800  1.00 41.14 ? 99  ILE A CG2 1 
ATOM   722  C  CD1 . ILE A 1 99  ? -11.479 -9.404  17.695  1.00 41.35 ? 99  ILE A CD1 1 
ATOM   723  N  N   . GLU A 1 100 ? -8.888  -12.892 16.824  1.00 39.67 ? 100 GLU A N   1 
ATOM   724  C  CA  . GLU A 1 100 ? -7.454  -12.704 16.904  1.00 39.43 ? 100 GLU A CA  1 
ATOM   725  C  C   . GLU A 1 100 ? -7.115  -11.463 16.089  1.00 38.90 ? 100 GLU A C   1 
ATOM   726  O  O   . GLU A 1 100 ? -7.673  -11.263 15.005  1.00 38.46 ? 100 GLU A O   1 
ATOM   727  C  CB  . GLU A 1 100 ? -6.750  -13.939 16.348  1.00 39.70 ? 100 GLU A CB  1 
ATOM   728  C  CG  . GLU A 1 100 ? -5.305  -14.105 16.788  1.00 40.10 ? 100 GLU A CG  1 
ATOM   729  C  CD  . GLU A 1 100 ? -4.817  -15.543 16.690  1.00 40.35 ? 100 GLU A CD  1 
ATOM   730  O  OE1 . GLU A 1 100 ? -5.494  -16.373 16.046  1.00 43.85 ? 100 GLU A OE1 1 
ATOM   731  O  OE2 . GLU A 1 100 ? -3.752  -15.849 17.264  1.00 42.17 ? 100 GLU A OE2 1 
ATOM   732  N  N   . ASP A 1 101 ? -6.226  -10.622 16.611  1.00 38.40 ? 101 ASP A N   1 
ATOM   733  C  CA  . ASP A 1 101 ? -5.845  -9.394  15.922  1.00 38.27 ? 101 ASP A CA  1 
ATOM   734  C  C   . ASP A 1 101 ? -4.344  -9.139  16.024  1.00 38.11 ? 101 ASP A C   1 
ATOM   735  O  O   . ASP A 1 101 ? -3.732  -9.394  17.060  1.00 37.71 ? 101 ASP A O   1 
ATOM   736  C  CB  . ASP A 1 101 ? -6.614  -8.198  16.480  1.00 38.31 ? 101 ASP A CB  1 
ATOM   737  C  CG  . ASP A 1 101 ? -6.613  -7.018  15.533  1.00 38.37 ? 101 ASP A CG  1 
ATOM   738  O  OD1 . ASP A 1 101 ? -7.302  -7.099  14.488  1.00 39.40 ? 101 ASP A OD1 1 
ATOM   739  O  OD2 . ASP A 1 101 ? -5.925  -6.016  15.819  1.00 37.26 ? 101 ASP A OD2 1 
ATOM   740  N  N   . SER A 1 102 ? -3.766  -8.635  14.936  1.00 37.85 ? 102 SER A N   1 
ATOM   741  C  CA  . SER A 1 102 ? -2.324  -8.419  14.850  1.00 37.80 ? 102 SER A CA  1 
ATOM   742  C  C   . SER A 1 102 ? -1.946  -6.939  14.765  1.00 37.40 ? 102 SER A C   1 
ATOM   743  O  O   . SER A 1 102 ? -0.778  -6.613  14.548  1.00 37.63 ? 102 SER A O   1 
ATOM   744  C  CB  . SER A 1 102 ? -1.766  -9.189  13.655  1.00 38.08 ? 102 SER A CB  1 
ATOM   745  O  OG  . SER A 1 102 ? -1.902  -10.588 13.860  1.00 39.24 ? 102 SER A OG  1 
ATOM   746  N  N   . VAL A 1 103 ? -2.920  -6.049  14.960  1.00 36.91 ? 103 VAL A N   1 
ATOM   747  C  CA  . VAL A 1 103 ? -2.665  -4.610  14.925  1.00 36.57 ? 103 VAL A CA  1 
ATOM   748  C  C   . VAL A 1 103 ? -2.649  -4.034  16.338  1.00 36.31 ? 103 VAL A C   1 
ATOM   749  O  O   . VAL A 1 103 ? -1.760  -3.254  16.673  1.00 36.17 ? 103 VAL A O   1 
ATOM   750  C  CB  . VAL A 1 103 ? -3.675  -3.873  14.027  1.00 36.93 ? 103 VAL A CB  1 
ATOM   751  C  CG1 . VAL A 1 103 ? -3.488  -2.355  14.128  1.00 36.87 ? 103 VAL A CG1 1 
ATOM   752  C  CG2 . VAL A 1 103 ? -3.505  -4.339  12.585  1.00 36.95 ? 103 VAL A CG2 1 
ATOM   753  N  N   . ILE A 1 104 ? -3.619  -4.417  17.166  1.00 35.56 ? 104 ILE A N   1 
ATOM   754  C  CA  . ILE A 1 104 ? -3.548  -4.099  18.598  1.00 35.58 ? 104 ILE A CA  1 
ATOM   755  C  C   . ILE A 1 104 ? -2.386  -4.849  19.234  1.00 34.84 ? 104 ILE A C   1 
ATOM   756  O  O   . ILE A 1 104 ? -1.922  -5.856  18.704  1.00 34.60 ? 104 ILE A O   1 
ATOM   757  C  CB  . ILE A 1 104 ? -4.855  -4.427  19.384  1.00 35.44 ? 104 ILE A CB  1 
ATOM   758  C  CG1 . ILE A 1 104 ? -5.211  -5.914  19.293  1.00 36.11 ? 104 ILE A CG1 1 
ATOM   759  C  CG2 . ILE A 1 104 ? -6.002  -3.569  18.897  1.00 36.45 ? 104 ILE A CG2 1 
ATOM   760  C  CD1 . ILE A 1 104 ? -6.343  -6.323  20.230  1.00 35.51 ? 104 ILE A CD1 1 
ATOM   761  N  N   . SER A 1 105 ? -1.926  -4.349  20.374  1.00 34.73 ? 105 SER A N   1 
ATOM   762  C  CA  . SER A 1 105 ? -0.845  -4.982  21.124  1.00 34.91 ? 105 SER A CA  1 
ATOM   763  C  C   . SER A 1 105 ? -1.065  -4.693  22.596  1.00 34.85 ? 105 SER A C   1 
ATOM   764  O  O   . SER A 1 105 ? -1.786  -3.756  22.936  1.00 35.23 ? 105 SER A O   1 
ATOM   765  C  CB  . SER A 1 105 ? 0.520   -4.446  20.675  1.00 34.76 ? 105 SER A CB  1 
ATOM   766  O  OG  . SER A 1 105 ? 1.592   -5.145  21.297  1.00 34.36 ? 105 SER A OG  1 
ATOM   767  N  N   . LEU A 1 106 ? -0.478  -5.519  23.459  1.00 34.91 ? 106 LEU A N   1 
ATOM   768  C  CA  . LEU A 1 106 ? -0.502  -5.279  24.902  1.00 35.09 ? 106 LEU A CA  1 
ATOM   769  C  C   . LEU A 1 106 ? 0.780   -4.615  25.384  1.00 35.48 ? 106 LEU A C   1 
ATOM   770  O  O   . LEU A 1 106 ? 0.939   -4.357  26.579  1.00 35.56 ? 106 LEU A O   1 
ATOM   771  C  CB  . LEU A 1 106 ? -0.720  -6.591  25.656  1.00 34.94 ? 106 LEU A CB  1 
ATOM   772  C  CG  . LEU A 1 106 ? -2.007  -7.340  25.293  1.00 34.11 ? 106 LEU A CG  1 
ATOM   773  C  CD1 . LEU A 1 106 ? -2.136  -8.583  26.160  1.00 33.90 ? 106 LEU A CD1 1 
ATOM   774  C  CD2 . LEU A 1 106 ? -3.235  -6.451  25.440  1.00 33.18 ? 106 LEU A CD2 1 
ATOM   775  N  N   . SER A 1 107 ? 1.701   -4.349  24.461  1.00 35.92 ? 107 SER A N   1 
ATOM   776  C  CA  . SER A 1 107 ? 2.941   -3.647  24.795  1.00 36.23 ? 107 SER A CA  1 
ATOM   777  C  C   . SER A 1 107 ? 3.361   -2.704  23.673  1.00 36.43 ? 107 SER A C   1 
ATOM   778  O  O   . SER A 1 107 ? 2.820   -2.760  22.563  1.00 36.02 ? 107 SER A O   1 
ATOM   779  C  CB  . SER A 1 107 ? 4.052   -4.646  25.094  1.00 36.22 ? 107 SER A CB  1 
ATOM   780  O  OG  . SER A 1 107 ? 4.391   -5.381  23.940  1.00 37.35 ? 107 SER A OG  1 
ATOM   781  N  N   . GLY A 1 108 ? 4.312   -1.824  23.976  1.00 36.99 ? 108 GLY A N   1 
ATOM   782  C  CA  . GLY A 1 108 ? 4.822   -0.869  22.991  1.00 37.59 ? 108 GLY A CA  1 
ATOM   783  C  C   . GLY A 1 108 ? 3.916   0.328   22.763  1.00 38.30 ? 108 GLY A C   1 
ATOM   784  O  O   . GLY A 1 108 ? 2.960   0.559   23.512  1.00 37.79 ? 108 GLY A O   1 
ATOM   785  N  N   . ASP A 1 109 ? 4.217   1.080   21.707  1.00 39.07 ? 109 ASP A N   1 
ATOM   786  C  CA  . ASP A 1 109 ? 3.452   2.281   21.335  1.00 39.75 ? 109 ASP A CA  1 
ATOM   787  C  C   . ASP A 1 109 ? 1.959   2.041   21.075  1.00 39.82 ? 109 ASP A C   1 
ATOM   788  O  O   . ASP A 1 109 ? 1.130   2.913   21.343  1.00 40.83 ? 109 ASP A O   1 
ATOM   789  C  CB  . ASP A 1 109 ? 4.074   2.934   20.091  1.00 40.03 ? 109 ASP A CB  1 
ATOM   790  C  CG  . ASP A 1 109 ? 5.334   3.718   20.396  1.00 41.11 ? 109 ASP A CG  1 
ATOM   791  O  OD1 . ASP A 1 109 ? 5.525   4.152   21.552  1.00 44.09 ? 109 ASP A OD1 1 
ATOM   792  O  OD2 . ASP A 1 109 ? 6.142   3.908   19.464  1.00 41.10 ? 109 ASP A OD2 1 
ATOM   793  N  N   . HIS A 1 110 ? 1.599   0.877   20.541  1.00 39.60 ? 110 HIS A N   1 
ATOM   794  C  CA  . HIS A 1 110 ? 0.183   0.579   20.280  1.00 39.32 ? 110 HIS A CA  1 
ATOM   795  C  C   . HIS A 1 110 ? -0.457  -0.256  21.397  1.00 38.54 ? 110 HIS A C   1 
ATOM   796  O  O   . HIS A 1 110 ? -1.475  -0.932  21.175  1.00 38.84 ? 110 HIS A O   1 
ATOM   797  C  CB  . HIS A 1 110 ? 0.012   -0.093  18.913  1.00 39.85 ? 110 HIS A CB  1 
ATOM   798  C  CG  . HIS A 1 110 ? 0.403   0.786   17.766  1.00 40.57 ? 110 HIS A CG  1 
ATOM   799  N  ND1 . HIS A 1 110 ? 0.482   0.330   16.465  1.00 40.54 ? 110 HIS A ND1 1 
ATOM   800  C  CD2 . HIS A 1 110 ? 0.761   2.094   17.730  1.00 41.41 ? 110 HIS A CD2 1 
ATOM   801  C  CE1 . HIS A 1 110 ? 0.847   1.324   15.677  1.00 41.17 ? 110 HIS A CE1 1 
ATOM   802  N  NE2 . HIS A 1 110 ? 1.028   2.404   16.420  1.00 40.95 ? 110 HIS A NE2 1 
ATOM   803  N  N   . ALA A 1 111 ? 0.122   -0.185  22.601  1.00 37.60 ? 111 ALA A N   1 
ATOM   804  C  CA  . ALA A 1 111 ? -0.417  -0.911  23.741  1.00 36.63 ? 111 ALA A CA  1 
ATOM   805  C  C   . ALA A 1 111 ? -1.801  -0.387  24.090  1.00 35.85 ? 111 ALA A C   1 
ATOM   806  O  O   . ALA A 1 111 ? -2.005  0.821   24.185  1.00 35.28 ? 111 ALA A O   1 
ATOM   807  C  CB  . ALA A 1 111 ? 0.500   -0.783  24.948  1.00 36.78 ? 111 ALA A CB  1 
ATOM   808  N  N   . ILE A 1 112 ? -2.735  -1.303  24.298  1.00 34.89 ? 112 ILE A N   1 
ATOM   809  C  CA  . ILE A 1 112 ? -4.109  -0.942  24.653  1.00 35.16 ? 112 ILE A CA  1 
ATOM   810  C  C   . ILE A 1 112 ? -4.383  -1.058  26.154  1.00 34.50 ? 112 ILE A C   1 
ATOM   811  O  O   . ILE A 1 112 ? -5.492  -0.783  26.611  1.00 34.13 ? 112 ILE A O   1 
ATOM   812  C  CB  . ILE A 1 112 ? -5.140  -1.766  23.844  1.00 35.03 ? 112 ILE A CB  1 
ATOM   813  C  CG1 . ILE A 1 112 ? -5.034  -3.274  24.133  1.00 35.11 ? 112 ILE A CG1 1 
ATOM   814  C  CG2 . ILE A 1 112 ? -4.952  -1.486  22.350  1.00 35.46 ? 112 ILE A CG2 1 
ATOM   815  C  CD1 . ILE A 1 112 ? -6.144  -4.106  23.503  1.00 35.61 ? 112 ILE A CD1 1 
ATOM   816  N  N   . ILE A 1 113 ? -3.372  -1.453  26.925  1.00 34.50 ? 113 ILE A N   1 
ATOM   817  C  CA  . ILE A 1 113 ? -3.492  -1.479  28.374  1.00 34.43 ? 113 ILE A CA  1 
ATOM   818  C  C   . ILE A 1 113 ? -3.748  -0.067  28.865  1.00 34.05 ? 113 ILE A C   1 
ATOM   819  O  O   . ILE A 1 113 ? -3.020  0.852   28.503  1.00 34.60 ? 113 ILE A O   1 
ATOM   820  C  CB  . ILE A 1 113 ? -2.199  -1.988  29.054  1.00 34.62 ? 113 ILE A CB  1 
ATOM   821  C  CG1 . ILE A 1 113 ? -1.858  -3.416  28.606  1.00 35.73 ? 113 ILE A CG1 1 
ATOM   822  C  CG2 . ILE A 1 113 ? -2.313  -1.910  30.582  1.00 34.85 ? 113 ILE A CG2 1 
ATOM   823  C  CD1 . ILE A 1 113 ? -2.874  -4.448  28.946  1.00 35.56 ? 113 ILE A CD1 1 
ATOM   824  N  N   . GLY A 1 114 ? -4.762  0.093   29.714  1.00 33.76 ? 114 GLY A N   1 
ATOM   825  C  CA  . GLY A 1 114 ? -5.108  1.402   30.267  1.00 33.81 ? 114 GLY A CA  1 
ATOM   826  C  C   . GLY A 1 114 ? -6.000  2.233   29.361  1.00 33.93 ? 114 GLY A C   1 
ATOM   827  O  O   . GLY A 1 114 ? -6.307  3.384   29.675  1.00 34.03 ? 114 GLY A O   1 
ATOM   828  N  N   . ARG A 1 115 ? -6.395  1.653   28.232  1.00 33.86 ? 115 ARG A N   1 
ATOM   829  C  CA  . ARG A 1 115 ? -7.356  2.270   27.327  1.00 33.92 ? 115 ARG A CA  1 
ATOM   830  C  C   . ARG A 1 115 ? -8.710  1.591   27.536  1.00 34.16 ? 115 ARG A C   1 
ATOM   831  O  O   . ARG A 1 115 ? -8.853  0.778   28.440  1.00 35.07 ? 115 ARG A O   1 
ATOM   832  C  CB  . ARG A 1 115 ? -6.845  2.187   25.893  1.00 34.03 ? 115 ARG A CB  1 
ATOM   833  C  CG  . ARG A 1 115 ? -5.425  2.752   25.786  1.00 33.75 ? 115 ARG A CG  1 
ATOM   834  C  CD  . ARG A 1 115 ? -5.008  3.081   24.385  1.00 34.17 ? 115 ARG A CD  1 
ATOM   835  N  NE  . ARG A 1 115 ? -3.623  3.543   24.331  1.00 32.92 ? 115 ARG A NE  1 
ATOM   836  C  CZ  . ARG A 1 115 ? -3.233  4.816   24.423  1.00 33.70 ? 115 ARG A CZ  1 
ATOM   837  N  NH1 . ARG A 1 115 ? -4.119  5.792   24.553  1.00 34.33 ? 115 ARG A NH1 1 
ATOM   838  N  NH2 . ARG A 1 115 ? -1.942  5.119   24.364  1.00 34.09 ? 115 ARG A NH2 1 
ATOM   839  N  N   . THR A 1 116 ? -9.715  1.944   26.741  1.00 34.23 ? 116 THR A N   1 
ATOM   840  C  CA  . THR A 1 116 ? -11.082 1.471   27.019  1.00 34.32 ? 116 THR A CA  1 
ATOM   841  C  C   . THR A 1 116 ? -11.631 0.634   25.870  1.00 34.59 ? 116 THR A C   1 
ATOM   842  O  O   . THR A 1 116 ? -11.491 1.012   24.718  1.00 34.68 ? 116 THR A O   1 
ATOM   843  C  CB  . THR A 1 116 ? -12.019 2.653   27.307  1.00 34.33 ? 116 THR A CB  1 
ATOM   844  O  OG1 . THR A 1 116 ? -11.602 3.297   28.511  1.00 34.18 ? 116 THR A OG1 1 
ATOM   845  C  CG2 . THR A 1 116 ? -13.453 2.198   27.469  1.00 34.16 ? 116 THR A CG2 1 
ATOM   846  N  N   . LEU A 1 117 ? -12.231 -0.509  26.194  1.00 34.88 ? 117 LEU A N   1 
ATOM   847  C  CA  . LEU A 1 117 ? -12.969 -1.311  25.228  1.00 35.08 ? 117 LEU A CA  1 
ATOM   848  C  C   . LEU A 1 117 ? -14.433 -0.892  25.289  1.00 34.70 ? 117 LEU A C   1 
ATOM   849  O  O   . LEU A 1 117 ? -14.993 -0.769  26.379  1.00 34.04 ? 117 LEU A O   1 
ATOM   850  C  CB  . LEU A 1 117 ? -12.853 -2.800  25.583  1.00 35.48 ? 117 LEU A CB  1 
ATOM   851  C  CG  . LEU A 1 117 ? -13.427 -3.833  24.605  1.00 35.85 ? 117 LEU A CG  1 
ATOM   852  C  CD1 . LEU A 1 117 ? -12.755 -3.769  23.253  1.00 36.45 ? 117 LEU A CD1 1 
ATOM   853  C  CD2 . LEU A 1 117 ? -13.267 -5.221  25.196  1.00 35.68 ? 117 LEU A CD2 1 
ATOM   854  N  N   . VAL A 1 118 ? -15.050 -0.670  24.127  1.00 35.05 ? 118 VAL A N   1 
ATOM   855  C  CA  . VAL A 1 118 ? -16.443 -0.215  24.061  1.00 35.00 ? 118 VAL A CA  1 
ATOM   856  C  C   . VAL A 1 118 ? -17.239 -1.102  23.114  1.00 35.00 ? 118 VAL A C   1 
ATOM   857  O  O   . VAL A 1 118 ? -16.754 -1.477  22.046  1.00 34.93 ? 118 VAL A O   1 
ATOM   858  C  CB  . VAL A 1 118 ? -16.546 1.251   23.548  1.00 35.19 ? 118 VAL A CB  1 
ATOM   859  C  CG1 . VAL A 1 118 ? -18.017 1.719   23.498  1.00 35.30 ? 118 VAL A CG1 1 
ATOM   860  C  CG2 . VAL A 1 118 ? -15.719 2.186   24.405  1.00 34.88 ? 118 VAL A CG2 1 
ATOM   861  N  N   . VAL A 1 119 ? -18.461 -1.438  23.515  1.00 35.26 ? 119 VAL A N   1 
ATOM   862  C  CA  . VAL A 1 119 ? -19.396 -2.113  22.621  1.00 35.29 ? 119 VAL A CA  1 
ATOM   863  C  C   . VAL A 1 119 ? -20.534 -1.145  22.357  1.00 35.29 ? 119 VAL A C   1 
ATOM   864  O  O   . VAL A 1 119 ? -21.041 -0.488  23.277  1.00 34.51 ? 119 VAL A O   1 
ATOM   865  C  CB  . VAL A 1 119 ? -19.893 -3.479  23.175  1.00 35.40 ? 119 VAL A CB  1 
ATOM   866  C  CG1 . VAL A 1 119 ? -20.704 -3.320  24.458  1.00 35.96 ? 119 VAL A CG1 1 
ATOM   867  C  CG2 . VAL A 1 119 ? -20.693 -4.226  22.115  1.00 35.41 ? 119 VAL A CG2 1 
ATOM   868  N  N   . HIS A 1 120 ? -20.929 -1.071  21.088  1.00 35.27 ? 120 HIS A N   1 
ATOM   869  C  CA  . HIS A 1 120 ? -21.786 -0.006  20.594  1.00 35.74 ? 120 HIS A CA  1 
ATOM   870  C  C   . HIS A 1 120 ? -23.221 -0.439  20.317  1.00 35.68 ? 120 HIS A C   1 
ATOM   871  O  O   . HIS A 1 120 ? -23.521 -1.625  20.222  1.00 35.10 ? 120 HIS A O   1 
ATOM   872  C  CB  . HIS A 1 120 ? -21.189 0.579   19.320  1.00 35.88 ? 120 HIS A CB  1 
ATOM   873  C  CG  . HIS A 1 120 ? -19.992 1.437   19.561  1.00 35.92 ? 120 HIS A CG  1 
ATOM   874  N  ND1 . HIS A 1 120 ? -20.084 2.799   19.749  1.00 36.02 ? 120 HIS A ND1 1 
ATOM   875  C  CD2 . HIS A 1 120 ? -18.677 1.130   19.667  1.00 37.95 ? 120 HIS A CD2 1 
ATOM   876  C  CE1 . HIS A 1 120 ? -18.875 3.297   19.937  1.00 37.58 ? 120 HIS A CE1 1 
ATOM   877  N  NE2 . HIS A 1 120 ? -18.004 2.304   19.900  1.00 36.61 ? 120 HIS A NE2 1 
ATOM   878  N  N   . GLU A 1 121 ? -24.076 0.572   20.190  1.00 36.08 ? 121 GLU A N   1 
ATOM   879  C  CA  . GLU A 1 121 ? -25.517 0.438   19.971  1.00 36.67 ? 121 GLU A CA  1 
ATOM   880  C  C   . GLU A 1 121 ? -25.834 -0.266  18.653  1.00 36.49 ? 121 GLU A C   1 
ATOM   881  O  O   . GLU A 1 121 ? -26.687 -1.158  18.603  1.00 36.22 ? 121 GLU A O   1 
ATOM   882  C  CB  . GLU A 1 121 ? -26.112 1.848   19.962  1.00 36.95 ? 121 GLU A CB  1 
ATOM   883  C  CG  . GLU A 1 121 ? -27.605 1.968   19.721  1.00 37.16 ? 121 GLU A CG  1 
ATOM   884  C  CD  . GLU A 1 121 ? -28.002 3.354   19.221  1.00 38.14 ? 121 GLU A CD  1 
ATOM   885  O  OE1 . GLU A 1 121 ? -27.104 4.175   18.911  1.00 39.36 ? 121 GLU A OE1 1 
ATOM   886  O  OE2 . GLU A 1 121 ? -29.221 3.615   19.118  1.00 40.76 ? 121 GLU A OE2 1 
ATOM   887  N  N   . LYS A 1 122 ? -25.131 0.142   17.599  1.00 36.50 ? 122 LYS A N   1 
ATOM   888  C  CA  . LYS A 1 122 ? -25.414 -0.305  16.233  1.00 36.93 ? 122 LYS A CA  1 
ATOM   889  C  C   . LYS A 1 122 ? -24.226 -1.024  15.599  1.00 36.24 ? 122 LYS A C   1 
ATOM   890  O  O   . LYS A 1 122 ? -23.121 -1.061  16.155  1.00 35.86 ? 122 LYS A O   1 
ATOM   891  C  CB  . LYS A 1 122 ? -25.802 0.895   15.359  1.00 37.21 ? 122 LYS A CB  1 
ATOM   892  C  CG  . LYS A 1 122 ? -26.991 1.669   15.866  1.00 38.42 ? 122 LYS A CG  1 
ATOM   893  C  CD  . LYS A 1 122 ? -27.300 2.884   15.002  1.00 38.57 ? 122 LYS A CD  1 
ATOM   894  C  CE  . LYS A 1 122 ? -28.557 3.587   15.510  1.00 40.09 ? 122 LYS A CE  1 
ATOM   895  N  NZ  . LYS A 1 122 ? -28.973 4.739   14.645  1.00 41.21 ? 122 LYS A NZ  1 
ATOM   896  N  N   . ALA A 1 123 ? -24.468 -1.593  14.421  1.00 36.29 ? 123 ALA A N   1 
ATOM   897  C  CA  . ALA A 1 123 ? -23.425 -2.264  13.663  1.00 36.17 ? 123 ALA A CA  1 
ATOM   898  C  C   . ALA A 1 123 ? -22.390 -1.253  13.175  1.00 36.19 ? 123 ALA A C   1 
ATOM   899  O  O   . ALA A 1 123 ? -22.724 -0.121  12.816  1.00 36.38 ? 123 ALA A O   1 
ATOM   900  C  CB  . ALA A 1 123 ? -24.022 -3.014  12.481  1.00 36.49 ? 123 ALA A CB  1 
ATOM   901  N  N   . ASP A 1 124 ? -21.130 -1.666  13.206  1.00 35.63 ? 124 ASP A N   1 
ATOM   902  C  CA  . ASP A 1 124 ? -20.040 -0.934  12.570  1.00 35.68 ? 124 ASP A CA  1 
ATOM   903  C  C   . ASP A 1 124 ? -20.126 -1.218  11.072  1.00 35.01 ? 124 ASP A C   1 
ATOM   904  O  O   . ASP A 1 124 ? -20.103 -2.384  10.656  1.00 34.63 ? 124 ASP A O   1 
ATOM   905  C  CB  . ASP A 1 124 ? -18.707 -1.424  13.146  1.00 35.53 ? 124 ASP A CB  1 
ATOM   906  C  CG  . ASP A 1 124 ? -17.502 -0.661  12.628  1.00 36.17 ? 124 ASP A CG  1 
ATOM   907  O  OD1 . ASP A 1 124 ? -17.599 0.084   11.630  1.00 34.20 ? 124 ASP A OD1 1 
ATOM   908  O  OD2 . ASP A 1 124 ? -16.427 -0.836  13.235  1.00 37.23 ? 124 ASP A OD2 1 
ATOM   909  N  N   . ASP A 1 125 ? -20.235 -0.160  10.265  1.00 34.60 ? 125 ASP A N   1 
ATOM   910  C  CA  . ASP A 1 125 ? -20.323 -0.328  8.802   1.00 34.43 ? 125 ASP A CA  1 
ATOM   911  C  C   . ASP A 1 125 ? -18.940 -0.474  8.147   1.00 34.02 ? 125 ASP A C   1 
ATOM   912  O  O   . ASP A 1 125 ? -18.836 -0.580  6.922   1.00 33.73 ? 125 ASP A O   1 
ATOM   913  C  CB  . ASP A 1 125 ? -21.163 0.781   8.137   1.00 34.33 ? 125 ASP A CB  1 
ATOM   914  C  CG  . ASP A 1 125 ? -20.503 2.155   8.175   1.00 34.06 ? 125 ASP A CG  1 
ATOM   915  O  OD1 . ASP A 1 125 ? -19.264 2.250   8.265   1.00 33.57 ? 125 ASP A OD1 1 
ATOM   916  O  OD2 . ASP A 1 125 ? -21.242 3.157   8.086   1.00 34.02 ? 125 ASP A OD2 1 
ATOM   917  N  N   . LEU A 1 126 ? -17.895 -0.480  8.977   1.00 34.29 ? 126 LEU A N   1 
ATOM   918  C  CA  . LEU A 1 126 ? -16.523 -0.787  8.555   1.00 34.52 ? 126 LEU A CA  1 
ATOM   919  C  C   . LEU A 1 126 ? -15.936 0.213   7.552   1.00 34.63 ? 126 LEU A C   1 
ATOM   920  O  O   . LEU A 1 126 ? -15.051 -0.136  6.765   1.00 34.59 ? 126 LEU A O   1 
ATOM   921  C  CB  . LEU A 1 126 ? -16.446 -2.213  7.987   1.00 34.44 ? 126 LEU A CB  1 
ATOM   922  C  CG  . LEU A 1 126 ? -17.118 -3.310  8.819   1.00 34.29 ? 126 LEU A CG  1 
ATOM   923  C  CD1 . LEU A 1 126 ? -16.991 -4.659  8.141   1.00 34.60 ? 126 LEU A CD1 1 
ATOM   924  C  CD2 . LEU A 1 126 ? -16.537 -3.375  10.219  1.00 34.94 ? 126 LEU A CD2 1 
ATOM   925  N  N   . GLY A 1 127 ? -16.419 1.453   7.587   1.00 34.71 ? 127 GLY A N   1 
ATOM   926  C  CA  . GLY A 1 127 ? -15.990 2.477   6.637   1.00 34.80 ? 127 GLY A CA  1 
ATOM   927  C  C   . GLY A 1 127 ? -16.639 2.382   5.261   1.00 34.82 ? 127 GLY A C   1 
ATOM   928  O  O   . GLY A 1 127 ? -16.247 3.100   4.340   1.00 34.72 ? 127 GLY A O   1 
ATOM   929  N  N   . LYS A 1 128 ? -17.644 1.514   5.127   1.00 34.81 ? 128 LYS A N   1 
ATOM   930  C  CA  . LYS A 1 128 ? -18.309 1.257   3.846   1.00 34.99 ? 128 LYS A CA  1 
ATOM   931  C  C   . LYS A 1 128 ? -19.763 1.727   3.848   1.00 34.73 ? 128 LYS A C   1 
ATOM   932  O  O   . LYS A 1 128 ? -20.583 1.210   3.093   1.00 34.61 ? 128 LYS A O   1 
ATOM   933  C  CB  . LYS A 1 128 ? -18.247 -0.245  3.523   1.00 35.49 ? 128 LYS A CB  1 
ATOM   934  C  CG  . LYS A 1 128 ? -17.127 -0.669  2.599   1.00 37.68 ? 128 LYS A CG  1 
ATOM   935  C  CD  . LYS A 1 128 ? -15.800 -0.043  2.921   1.00 39.42 ? 128 LYS A CD  1 
ATOM   936  C  CE  . LYS A 1 128 ? -14.712 -0.600  2.017   1.00 39.23 ? 128 LYS A CE  1 
ATOM   937  N  NZ  . LYS A 1 128 ? -13.380 -0.178  2.508   1.00 40.03 ? 128 LYS A NZ  1 
ATOM   938  N  N   . GLY A 1 129 ? -20.073 2.718   4.681   1.00 34.58 ? 129 GLY A N   1 
ATOM   939  C  CA  . GLY A 1 129 ? -21.439 3.229   4.809   1.00 34.40 ? 129 GLY A CA  1 
ATOM   940  C  C   . GLY A 1 129 ? -21.781 4.355   3.857   1.00 34.11 ? 129 GLY A C   1 
ATOM   941  O  O   . GLY A 1 129 ? -22.950 4.723   3.725   1.00 33.91 ? 129 GLY A O   1 
ATOM   942  N  N   . GLY A 1 130 ? -20.768 4.912   3.197   1.00 34.05 ? 130 GLY A N   1 
ATOM   943  C  CA  . GLY A 1 130 ? -20.986 5.906   2.148   1.00 34.38 ? 130 GLY A CA  1 
ATOM   944  C  C   . GLY A 1 130 ? -21.334 7.303   2.621   1.00 34.37 ? 130 GLY A C   1 
ATOM   945  O  O   . GLY A 1 130 ? -21.967 8.063   1.897   1.00 34.22 ? 130 GLY A O   1 
ATOM   946  N  N   . ASN A 1 131 ? -20.922 7.646   3.836   1.00 35.07 ? 131 ASN A N   1 
ATOM   947  C  CA  . ASN A 1 131 ? -21.049 9.017   4.334   1.00 35.22 ? 131 ASN A CA  1 
ATOM   948  C  C   . ASN A 1 131 ? -19.828 9.404   5.154   1.00 35.55 ? 131 ASN A C   1 
ATOM   949  O  O   . ASN A 1 131 ? -19.013 8.556   5.509   1.00 35.61 ? 131 ASN A O   1 
ATOM   950  C  CB  . ASN A 1 131 ? -22.354 9.208   5.127   1.00 34.94 ? 131 ASN A CB  1 
ATOM   951  C  CG  . ASN A 1 131 ? -22.528 8.191   6.236   1.00 34.36 ? 131 ASN A CG  1 
ATOM   952  O  OD1 . ASN A 1 131 ? -21.565 7.778   6.871   1.00 32.14 ? 131 ASN A OD1 1 
ATOM   953  N  ND2 . ASN A 1 131 ? -23.769 7.790   6.478   1.00 34.93 ? 131 ASN A ND2 1 
ATOM   954  N  N   . GLU A 1 132 ? -19.706 10.693  5.447   1.00 36.24 ? 132 GLU A N   1 
ATOM   955  C  CA  . GLU A 1 132 ? -18.541 11.221  6.156   1.00 36.79 ? 132 GLU A CA  1 
ATOM   956  C  C   . GLU A 1 132 ? -18.293 10.520  7.488   1.00 36.84 ? 132 GLU A C   1 
ATOM   957  O  O   . GLU A 1 132 ? -17.148 10.244  7.844   1.00 37.31 ? 132 GLU A O   1 
ATOM   958  C  CB  . GLU A 1 132 ? -18.699 12.725  6.382   1.00 37.00 ? 132 GLU A CB  1 
ATOM   959  C  CG  . GLU A 1 132 ? -18.636 13.552  5.116   1.00 37.83 ? 132 GLU A CG  1 
ATOM   960  C  CD  . GLU A 1 132 ? -19.094 14.980  5.336   1.00 37.87 ? 132 GLU A CD  1 
ATOM   961  O  OE1 . GLU A 1 132 ? -18.892 15.504  6.455   1.00 40.66 ? 132 GLU A OE1 1 
ATOM   962  O  OE2 . GLU A 1 132 ? -19.657 15.569  4.395   1.00 39.13 ? 132 GLU A OE2 1 
ATOM   963  N  N   . GLU A 1 133 ? -19.362 10.226  8.224   1.00 36.93 ? 133 GLU A N   1 
ATOM   964  C  CA  . GLU A 1 133 ? -19.243 9.574   9.530   1.00 36.90 ? 133 GLU A CA  1 
ATOM   965  C  C   . GLU A 1 133 ? -18.703 8.140   9.440   1.00 36.70 ? 133 GLU A C   1 
ATOM   966  O  O   . GLU A 1 133 ? -18.059 7.653   10.377  1.00 36.74 ? 133 GLU A O   1 
ATOM   967  C  CB  . GLU A 1 133 ? -20.599 9.582   10.251  1.00 37.12 ? 133 GLU A CB  1 
ATOM   968  C  CG  . GLU A 1 133 ? -20.548 9.191   11.726  1.00 37.67 ? 133 GLU A CG  1 
ATOM   969  C  CD  . GLU A 1 133 ? -19.651 10.096  12.561  1.00 39.08 ? 133 GLU A CD  1 
ATOM   970  O  OE1 . GLU A 1 133 ? -19.652 11.330  12.343  1.00 40.24 ? 133 GLU A OE1 1 
ATOM   971  O  OE2 . GLU A 1 133 ? -18.948 9.569   13.447  1.00 41.15 ? 133 GLU A OE2 1 
ATOM   972  N  N   . SER A 1 134 ? -18.961 7.470   8.318   1.00 36.40 ? 134 SER A N   1 
ATOM   973  C  CA  . SER A 1 134 ? -18.532 6.083   8.126   1.00 36.58 ? 134 SER A CA  1 
ATOM   974  C  C   . SER A 1 134 ? -17.024 5.904   8.292   1.00 36.48 ? 134 SER A C   1 
ATOM   975  O  O   . SER A 1 134 ? -16.580 4.930   8.894   1.00 36.39 ? 134 SER A O   1 
ATOM   976  C  CB  . SER A 1 134 ? -18.955 5.573   6.743   1.00 36.39 ? 134 SER A CB  1 
ATOM   977  O  OG  . SER A 1 134 ? -18.637 4.201   6.584   1.00 35.74 ? 134 SER A OG  1 
ATOM   978  N  N   . THR A 1 135 ? -16.246 6.842   7.760   1.00 37.03 ? 135 THR A N   1 
ATOM   979  C  CA  . THR A 1 135 ? -14.785 6.758   7.818   1.00 37.57 ? 135 THR A CA  1 
ATOM   980  C  C   . THR A 1 135 ? -14.207 7.393   9.090   1.00 37.89 ? 135 THR A C   1 
ATOM   981  O  O   . THR A 1 135 ? -12.994 7.550   9.205   1.00 37.55 ? 135 THR A O   1 
ATOM   982  C  CB  . THR A 1 135 ? -14.134 7.399   6.565   1.00 37.77 ? 135 THR A CB  1 
ATOM   983  O  OG1 . THR A 1 135 ? -14.529 8.773   6.458   1.00 38.83 ? 135 THR A OG1 1 
ATOM   984  C  CG2 . THR A 1 135 ? -14.563 6.661   5.305   1.00 38.03 ? 135 THR A CG2 1 
ATOM   985  N  N   . LYS A 1 136 ? -15.081 7.745   10.034  1.00 38.08 ? 136 LYS A N   1 
ATOM   986  C  CA  . LYS A 1 136 ? -14.679 8.272   11.342  1.00 38.72 ? 136 LYS A CA  1 
ATOM   987  C  C   . LYS A 1 136 ? -14.985 7.272   12.462  1.00 38.63 ? 136 LYS A C   1 
ATOM   988  O  O   . LYS A 1 136 ? -14.119 6.964   13.287  1.00 38.96 ? 136 LYS A O   1 
ATOM   989  C  CB  . LYS A 1 136 ? -15.406 9.595   11.610  1.00 39.00 ? 136 LYS A CB  1 
ATOM   990  C  CG  . LYS A 1 136 ? -15.228 10.641  10.517  1.00 39.91 ? 136 LYS A CG  1 
ATOM   991  C  CD  . LYS A 1 136 ? -16.038 11.891  10.820  1.00 39.95 ? 136 LYS A CD  1 
ATOM   992  C  CE  . LYS A 1 136 ? -15.897 12.931  9.727   1.00 40.78 ? 136 LYS A CE  1 
ATOM   993  N  NZ  . LYS A 1 136 ? -16.725 14.144  9.995   1.00 41.65 ? 136 LYS A NZ  1 
ATOM   994  N  N   . THR A 1 137 ? -16.224 6.781   12.503  1.00 38.61 ? 137 THR A N   1 
ATOM   995  C  CA  . THR A 1 137 ? -16.680 5.883   13.569  1.00 38.37 ? 137 THR A CA  1 
ATOM   996  C  C   . THR A 1 137 ? -17.403 4.617   13.094  1.00 38.22 ? 137 THR A C   1 
ATOM   997  O  O   . THR A 1 137 ? -17.782 3.774   13.917  1.00 38.84 ? 137 THR A O   1 
ATOM   998  C  CB  . THR A 1 137 ? -17.652 6.625   14.514  1.00 38.71 ? 137 THR A CB  1 
ATOM   999  O  OG1 . THR A 1 137 ? -18.849 6.971   13.798  1.00 38.65 ? 137 THR A OG1 1 
ATOM   1000 C  CG2 . THR A 1 137 ? -16.998 7.886   15.075  1.00 39.19 ? 137 THR A CG2 1 
ATOM   1001 N  N   . GLY A 1 138 ? -17.644 4.495   11.792  1.00 37.32 ? 138 GLY A N   1 
ATOM   1002 C  CA  . GLY A 1 138 ? -18.402 3.367   11.263  1.00 37.01 ? 138 GLY A CA  1 
ATOM   1003 C  C   . GLY A 1 138 ? -19.894 3.417   11.561  1.00 36.53 ? 138 GLY A C   1 
ATOM   1004 O  O   . GLY A 1 138 ? -20.605 2.425   11.354  1.00 36.27 ? 138 GLY A O   1 
ATOM   1005 N  N   . ASN A 1 139 ? -20.371 4.575   12.023  1.00 36.06 ? 139 ASN A N   1 
ATOM   1006 C  CA  . ASN A 1 139 ? -21.786 4.784   12.346  1.00 36.23 ? 139 ASN A CA  1 
ATOM   1007 C  C   . ASN A 1 139 ? -22.348 3.813   13.394  1.00 36.13 ? 139 ASN A C   1 
ATOM   1008 O  O   . ASN A 1 139 ? -23.540 3.511   13.399  1.00 35.72 ? 139 ASN A O   1 
ATOM   1009 C  CB  . ASN A 1 139 ? -22.624 4.759   11.059  1.00 36.13 ? 139 ASN A CB  1 
ATOM   1010 C  CG  . ASN A 1 139 ? -22.426 5.998   10.227  1.00 36.69 ? 139 ASN A CG  1 
ATOM   1011 O  OD1 . ASN A 1 139 ? -22.743 7.101   10.669  1.00 36.69 ? 139 ASN A OD1 1 
ATOM   1012 N  ND2 . ASN A 1 139 ? -21.887 5.834   9.018   1.00 35.77 ? 139 ASN A ND2 1 
ATOM   1013 N  N   . ALA A 1 140 ? -21.489 3.359   14.305  1.00 35.89 ? 140 ALA A N   1 
ATOM   1014 C  CA  . ALA A 1 140 ? -21.886 2.338   15.290  1.00 35.99 ? 140 ALA A CA  1 
ATOM   1015 C  C   . ALA A 1 140 ? -22.741 2.885   16.441  1.00 35.82 ? 140 ALA A C   1 
ATOM   1016 O  O   . ALA A 1 140 ? -23.278 2.121   17.245  1.00 35.09 ? 140 ALA A O   1 
ATOM   1017 C  CB  . ALA A 1 140 ? -20.665 1.629   15.830  1.00 36.15 ? 140 ALA A CB  1 
ATOM   1018 N  N   . GLY A 1 141 ? -22.847 4.208   16.526  1.00 35.89 ? 141 GLY A N   1 
ATOM   1019 C  CA  . GLY A 1 141 ? -23.806 4.844   17.411  1.00 36.12 ? 141 GLY A CA  1 
ATOM   1020 C  C   . GLY A 1 141 ? -23.290 4.974   18.824  1.00 36.01 ? 141 GLY A C   1 
ATOM   1021 O  O   . GLY A 1 141 ? -22.076 5.004   19.061  1.00 35.97 ? 141 GLY A O   1 
ATOM   1022 N  N   . SER A 1 142 ? -24.227 5.027   19.762  1.00 36.31 ? 142 SER A N   1 
ATOM   1023 C  CA  . SER A 1 142 ? -23.911 5.310   21.155  1.00 36.37 ? 142 SER A CA  1 
ATOM   1024 C  C   . SER A 1 142 ? -23.155 4.157   21.792  1.00 36.46 ? 142 SER A C   1 
ATOM   1025 O  O   . SER A 1 142 ? -23.112 3.047   21.261  1.00 36.69 ? 142 SER A O   1 
ATOM   1026 C  CB  . SER A 1 142 ? -25.184 5.602   21.945  1.00 36.69 ? 142 SER A CB  1 
ATOM   1027 O  OG  . SER A 1 142 ? -25.988 4.445   22.044  1.00 37.57 ? 142 SER A OG  1 
ATOM   1028 N  N   . ARG A 1 143 ? -22.561 4.439   22.942  1.00 36.13 ? 143 ARG A N   1 
ATOM   1029 C  CA  . ARG A 1 143 ? -21.728 3.477   23.640  1.00 36.10 ? 143 ARG A CA  1 
ATOM   1030 C  C   . ARG A 1 143 ? -22.577 2.824   24.721  1.00 35.58 ? 143 ARG A C   1 
ATOM   1031 O  O   . ARG A 1 143 ? -23.025 3.495   25.648  1.00 36.25 ? 143 ARG A O   1 
ATOM   1032 C  CB  . ARG A 1 143 ? -20.514 4.198   24.231  1.00 36.32 ? 143 ARG A CB  1 
ATOM   1033 C  CG  . ARG A 1 143 ? -19.787 5.010   23.175  1.00 37.10 ? 143 ARG A CG  1 
ATOM   1034 C  CD  . ARG A 1 143 ? -18.643 5.835   23.709  1.00 37.53 ? 143 ARG A CD  1 
ATOM   1035 N  NE  . ARG A 1 143 ? -18.131 6.707   22.655  1.00 37.37 ? 143 ARG A NE  1 
ATOM   1036 C  CZ  . ARG A 1 143 ? -17.022 7.434   22.729  1.00 37.90 ? 143 ARG A CZ  1 
ATOM   1037 N  NH1 . ARG A 1 143 ? -16.267 7.405   23.817  1.00 37.45 ? 143 ARG A NH1 1 
ATOM   1038 N  NH2 . ARG A 1 143 ? -16.663 8.182   21.689  1.00 38.31 ? 143 ARG A NH2 1 
ATOM   1039 N  N   . LEU A 1 144 ? -22.808 1.520   24.594  1.00 35.01 ? 144 LEU A N   1 
ATOM   1040 C  CA  . LEU A 1 144 ? -23.705 0.802   25.503  1.00 34.90 ? 144 LEU A CA  1 
ATOM   1041 C  C   . LEU A 1 144 ? -23.028 0.340   26.784  1.00 34.41 ? 144 LEU A C   1 
ATOM   1042 O  O   . LEU A 1 144 ? -23.656 0.305   27.840  1.00 34.16 ? 144 LEU A O   1 
ATOM   1043 C  CB  . LEU A 1 144 ? -24.302 -0.422  24.814  1.00 35.07 ? 144 LEU A CB  1 
ATOM   1044 C  CG  . LEU A 1 144 ? -25.210 -0.180  23.610  1.00 35.34 ? 144 LEU A CG  1 
ATOM   1045 C  CD1 . LEU A 1 144 ? -25.782 -1.511  23.152  1.00 36.31 ? 144 LEU A CD1 1 
ATOM   1046 C  CD2 . LEU A 1 144 ? -26.328 0.801   23.935  1.00 35.22 ? 144 LEU A CD2 1 
ATOM   1047 N  N   . ALA A 1 145 ? -21.764 -0.054  26.669  1.00 34.24 ? 145 ALA A N   1 
ATOM   1048 C  CA  . ALA A 1 145 ? -20.988 -0.517  27.815  1.00 34.25 ? 145 ALA A CA  1 
ATOM   1049 C  C   . ALA A 1 145 ? -19.513 -0.387  27.510  1.00 34.15 ? 145 ALA A C   1 
ATOM   1050 O  O   . ALA A 1 145 ? -19.094 -0.470  26.361  1.00 33.79 ? 145 ALA A O   1 
ATOM   1051 C  CB  . ALA A 1 145 ? -21.319 -1.960  28.143  1.00 34.22 ? 145 ALA A CB  1 
ATOM   1052 N  N   . CYS A 1 146 ? -18.718 -0.185  28.548  1.00 34.09 ? 146 CYS A N   1 
ATOM   1053 C  CA  . CYS A 1 146 ? -17.286 -0.060  28.362  1.00 34.63 ? 146 CYS A CA  1 
ATOM   1054 C  C   . CYS A 1 146 ? -16.529 -0.497  29.603  1.00 34.24 ? 146 CYS A C   1 
ATOM   1055 O  O   . CYS A 1 146 ? -17.114 -0.736  30.659  1.00 34.39 ? 146 CYS A O   1 
ATOM   1056 C  CB  . CYS A 1 146 ? -16.922 1.383   28.017  1.00 35.18 ? 146 CYS A CB  1 
ATOM   1057 S  SG  . CYS A 1 146 ? -17.436 2.618   29.223  1.00 39.75 ? 146 CYS A SG  1 
ATOM   1058 N  N   . GLY A 1 147 ? -15.219 -0.616  29.456  1.00 34.16 ? 147 GLY A N   1 
ATOM   1059 C  CA  . GLY A 1 147 ? -14.366 -0.979  30.572  1.00 34.01 ? 147 GLY A CA  1 
ATOM   1060 C  C   . GLY A 1 147 ? -12.921 -0.695  30.255  1.00 34.10 ? 147 GLY A C   1 
ATOM   1061 O  O   . GLY A 1 147 ? -12.494 -0.846  29.122  1.00 34.21 ? 147 GLY A O   1 
ATOM   1062 N  N   . VAL A 1 148 ? -12.171 -0.279  31.266  1.00 33.90 ? 148 VAL A N   1 
ATOM   1063 C  CA  . VAL A 1 148 ? -10.733 -0.070  31.110  1.00 34.19 ? 148 VAL A CA  1 
ATOM   1064 C  C   . VAL A 1 148 ? -10.044 -1.423  30.958  1.00 34.12 ? 148 VAL A C   1 
ATOM   1065 O  O   . VAL A 1 148 ? -10.354 -2.373  31.682  1.00 33.96 ? 148 VAL A O   1 
ATOM   1066 C  CB  . VAL A 1 148 ? -10.138 0.688   32.317  1.00 34.47 ? 148 VAL A CB  1 
ATOM   1067 C  CG1 . VAL A 1 148 ? -8.635  0.886   32.148  1.00 34.74 ? 148 VAL A CG1 1 
ATOM   1068 C  CG2 . VAL A 1 148 ? -10.842 2.029   32.494  1.00 34.98 ? 148 VAL A CG2 1 
ATOM   1069 N  N   . ILE A 1 149 ? -9.091  -1.490  30.037  1.00 34.20 ? 149 ILE A N   1 
ATOM   1070 C  CA  . ILE A 1 149 ? -8.348  -2.714  29.783  1.00 34.54 ? 149 ILE A CA  1 
ATOM   1071 C  C   . ILE A 1 149 ? -7.210  -2.786  30.796  1.00 34.75 ? 149 ILE A C   1 
ATOM   1072 O  O   . ILE A 1 149 ? -6.278  -1.984  30.751  1.00 34.63 ? 149 ILE A O   1 
ATOM   1073 C  CB  . ILE A 1 149 ? -7.813  -2.761  28.337  1.00 34.75 ? 149 ILE A CB  1 
ATOM   1074 C  CG1 . ILE A 1 149 ? -8.979  -2.690  27.346  1.00 35.53 ? 149 ILE A CG1 1 
ATOM   1075 C  CG2 . ILE A 1 149 ? -7.000  -4.039  28.095  1.00 34.11 ? 149 ILE A CG2 1 
ATOM   1076 C  CD1 . ILE A 1 149 ? -8.568  -2.335  25.945  1.00 35.47 ? 149 ILE A CD1 1 
ATOM   1077 N  N   . GLY A 1 150 ? -7.300  -3.758  31.695  1.00 34.60 ? 150 GLY A N   1 
ATOM   1078 C  CA  . GLY A 1 150 ? -6.352  -3.892  32.800  1.00 34.90 ? 150 GLY A CA  1 
ATOM   1079 C  C   . GLY A 1 150 ? -5.488  -5.132  32.727  1.00 35.35 ? 150 GLY A C   1 
ATOM   1080 O  O   . GLY A 1 150 ? -5.829  -6.107  32.062  1.00 34.80 ? 150 GLY A O   1 
ATOM   1081 N  N   . ILE A 1 151 ? -4.356  -5.084  33.425  1.00 35.39 ? 151 ILE A N   1 
ATOM   1082 C  CA  . ILE A 1 151 ? -3.440  -6.216  33.498  1.00 35.55 ? 151 ILE A CA  1 
ATOM   1083 C  C   . ILE A 1 151 ? -4.091  -7.355  34.286  1.00 35.92 ? 151 ILE A C   1 
ATOM   1084 O  O   . ILE A 1 151 ? -4.632  -7.143  35.379  1.00 35.88 ? 151 ILE A O   1 
ATOM   1085 C  CB  . ILE A 1 151 ? -2.089  -5.808  34.133  1.00 35.26 ? 151 ILE A CB  1 
ATOM   1086 C  CG1 . ILE A 1 151 ? -1.390  -4.773  33.244  1.00 35.37 ? 151 ILE A CG1 1 
ATOM   1087 C  CG2 . ILE A 1 151 ? -1.192  -7.037  34.345  1.00 35.28 ? 151 ILE A CG2 1 
ATOM   1088 C  CD1 . ILE A 1 151 ? -0.291  -3.990  33.938  1.00 35.16 ? 151 ILE A CD1 1 
ATOM   1089 N  N   . ALA A 1 152 ? -4.048  -8.554  33.713  1.00 36.14 ? 152 ALA A N   1 
ATOM   1090 C  CA  . ALA A 1 152 ? -4.674  -9.733  34.309  1.00 36.78 ? 152 ALA A CA  1 
ATOM   1091 C  C   . ALA A 1 152 ? -3.650  -10.824 34.576  1.00 37.28 ? 152 ALA A C   1 
ATOM   1092 O  O   . ALA A 1 152 ? -2.561  -10.827 33.996  1.00 37.17 ? 152 ALA A O   1 
ATOM   1093 C  CB  . ALA A 1 152 ? -5.771  -10.258 33.394  1.00 36.89 ? 152 ALA A CB  1 
ATOM   1094 N  N   . GLN A 1 153 ? -4.014  -11.753 35.456  1.00 37.98 ? 153 GLN A N   1 
ATOM   1095 C  CA  . GLN A 1 153 ? -3.166  -12.903 35.763  1.00 38.48 ? 153 GLN A CA  1 
ATOM   1096 C  C   . GLN A 1 153 ? -3.313  -13.963 34.676  1.00 38.95 ? 153 GLN A C   1 
ATOM   1097 O  O   . GLN A 1 153 ? -4.423  -14.264 34.214  1.00 39.18 ? 153 GLN A O   1 
ATOM   1098 C  CB  . GLN A 1 153 ? -3.537  -13.495 37.120  1.00 38.52 ? 153 GLN A CB  1 
ATOM   1099 C  CG  . GLN A 1 153 ? -2.638  -14.649 37.567  1.00 38.81 ? 153 GLN A CG  1 
ATOM   1100 C  CD  . GLN A 1 153 ? -3.111  -15.317 38.847  1.00 39.60 ? 153 GLN A CD  1 
ATOM   1101 O  OE1 . GLN A 1 153 ? -2.731  -16.455 39.144  1.00 42.00 ? 153 GLN A OE1 1 
ATOM   1102 N  NE2 . GLN A 1 153 ? -3.940  -14.617 39.614  1.00 41.52 ? 153 GLN A NE2 1 
ATOM   1103 O  OXT . GLN A 1 153 ? -2.317  -14.552 34.248  1.00 39.70 ? 153 GLN A OXT 1 
ATOM   1104 N  N   . THR B 1 2   ? 2.821   12.438  31.573  1.00 38.81 ? 2   THR B N   1 
ATOM   1105 C  CA  . THR B 1 2   ? 1.923   11.248  31.599  1.00 38.30 ? 2   THR B CA  1 
ATOM   1106 C  C   . THR B 1 2   ? 0.795   11.489  32.605  1.00 37.62 ? 2   THR B C   1 
ATOM   1107 O  O   . THR B 1 2   ? 1.032   11.991  33.699  1.00 37.18 ? 2   THR B O   1 
ATOM   1108 C  CB  . THR B 1 2   ? 2.721   9.966   31.940  1.00 38.70 ? 2   THR B CB  1 
ATOM   1109 O  OG1 . THR B 1 2   ? 3.884   9.899   31.109  1.00 41.64 ? 2   THR B OG1 1 
ATOM   1110 C  CG2 . THR B 1 2   ? 1.906   8.724   31.697  1.00 39.68 ? 2   THR B CG2 1 
ATOM   1111 N  N   . LYS B 1 3   ? -0.434  11.167  32.210  1.00 36.74 ? 3   LYS B N   1 
ATOM   1112 C  CA  . LYS B 1 3   ? -1.606  11.353  33.065  1.00 36.93 ? 3   LYS B CA  1 
ATOM   1113 C  C   . LYS B 1 3   ? -2.438  10.085  33.109  1.00 36.12 ? 3   LYS B C   1 
ATOM   1114 O  O   . LYS B 1 3   ? -2.528  9.353   32.116  1.00 36.42 ? 3   LYS B O   1 
ATOM   1115 C  CB  . LYS B 1 3   ? -2.491  12.481  32.551  1.00 36.88 ? 3   LYS B CB  1 
ATOM   1116 C  CG  . LYS B 1 3   ? -1.948  13.860  32.806  1.00 39.00 ? 3   LYS B CG  1 
ATOM   1117 C  CD  . LYS B 1 3   ? -2.902  14.928  32.300  1.00 38.72 ? 3   LYS B CD  1 
ATOM   1118 C  CE  . LYS B 1 3   ? -4.112  15.108  33.200  1.00 40.22 ? 3   LYS B CE  1 
ATOM   1119 N  NZ  . LYS B 1 3   ? -5.005  16.182  32.649  1.00 41.60 ? 3   LYS B NZ  1 
ATOM   1120 N  N   . ALA B 1 4   ? -3.052  9.848   34.260  1.00 35.54 ? 4   ALA B N   1 
ATOM   1121 C  CA  . ALA B 1 4   ? -3.961  8.727   34.424  1.00 35.21 ? 4   ALA B CA  1 
ATOM   1122 C  C   . ALA B 1 4   ? -5.096  9.083   35.363  1.00 34.73 ? 4   ALA B C   1 
ATOM   1123 O  O   . ALA B 1 4   ? -5.076  10.130  36.018  1.00 33.99 ? 4   ALA B O   1 
ATOM   1124 C  CB  . ALA B 1 4   ? -3.203  7.501   34.920  1.00 35.41 ? 4   ALA B CB  1 
ATOM   1125 N  N   . VAL B 1 5   ? -6.103  8.219   35.396  1.00 34.57 ? 5   VAL B N   1 
ATOM   1126 C  CA  . VAL B 1 5   ? -7.268  8.417   36.258  1.00 34.75 ? 5   VAL B CA  1 
ATOM   1127 C  C   . VAL B 1 5   ? -7.828  7.062   36.692  1.00 34.73 ? 5   VAL B C   1 
ATOM   1128 O  O   . VAL B 1 5   ? -7.753  6.084   35.948  1.00 35.36 ? 5   VAL B O   1 
ATOM   1129 C  CB  . VAL B 1 5   ? -8.339  9.262   35.546  1.00 35.01 ? 5   VAL B CB  1 
ATOM   1130 C  CG1 . VAL B 1 5   ? -8.965  8.488   34.402  1.00 35.03 ? 5   VAL B CG1 1 
ATOM   1131 C  CG2 . VAL B 1 5   ? -9.396  9.762   36.522  1.00 34.50 ? 5   VAL B CG2 1 
ATOM   1132 N  N   . ALA B 1 6   ? -8.367  7.010   37.906  1.00 34.72 ? 6   ALA B N   1 
ATOM   1133 C  CA  . ALA B 1 6   ? -9.085  5.841   38.390  1.00 34.54 ? 6   ALA B CA  1 
ATOM   1134 C  C   . ALA B 1 6   ? -10.415 6.319   38.942  1.00 34.59 ? 6   ALA B C   1 
ATOM   1135 O  O   . ALA B 1 6   ? -10.460 7.276   39.712  1.00 34.17 ? 6   ALA B O   1 
ATOM   1136 C  CB  . ALA B 1 6   ? -8.293  5.128   39.454  1.00 35.01 ? 6   ALA B CB  1 
ATOM   1137 N  N   . VAL B 1 7   ? -11.495 5.677   38.510  1.00 34.27 ? 7   VAL B N   1 
ATOM   1138 C  CA  . VAL B 1 7   ? -12.831 5.970   39.013  1.00 35.15 ? 7   VAL B CA  1 
ATOM   1139 C  C   . VAL B 1 7   ? -13.169 4.852   39.975  1.00 35.35 ? 7   VAL B C   1 
ATOM   1140 O  O   . VAL B 1 7   ? -13.250 3.695   39.578  1.00 35.51 ? 7   VAL B O   1 
ATOM   1141 C  CB  . VAL B 1 7   ? -13.862 6.063   37.864  1.00 35.11 ? 7   VAL B CB  1 
ATOM   1142 C  CG1 . VAL B 1 7   ? -15.259 6.179   38.407  1.00 35.52 ? 7   VAL B CG1 1 
ATOM   1143 C  CG2 . VAL B 1 7   ? -13.530 7.260   36.982  1.00 35.94 ? 7   VAL B CG2 1 
ATOM   1144 N  N   . LEU B 1 8   ? -13.320 5.200   41.249  1.00 35.91 ? 8   LEU B N   1 
ATOM   1145 C  CA  . LEU B 1 8   ? -13.533 4.218   42.298  1.00 36.22 ? 8   LEU B CA  1 
ATOM   1146 C  C   . LEU B 1 8   ? -15.021 3.955   42.486  1.00 36.37 ? 8   LEU B C   1 
ATOM   1147 O  O   . LEU B 1 8   ? -15.805 4.879   42.699  1.00 35.89 ? 8   LEU B O   1 
ATOM   1148 C  CB  . LEU B 1 8   ? -12.931 4.709   43.604  1.00 36.36 ? 8   LEU B CB  1 
ATOM   1149 C  CG  . LEU B 1 8   ? -11.434 5.020   43.582  1.00 37.31 ? 8   LEU B CG  1 
ATOM   1150 C  CD1 . LEU B 1 8   ? -11.013 5.594   44.916  1.00 38.38 ? 8   LEU B CD1 1 
ATOM   1151 C  CD2 . LEU B 1 8   ? -10.626 3.781   43.241  1.00 39.29 ? 8   LEU B CD2 1 
ATOM   1152 N  N   . LYS B 1 9   ? -15.398 2.686   42.392  1.00 37.21 ? 9   LYS B N   1 
ATOM   1153 C  CA  . LYS B 1 9   ? -16.780 2.260   42.609  1.00 38.01 ? 9   LYS B CA  1 
ATOM   1154 C  C   . LYS B 1 9   ? -16.782 0.943   43.365  1.00 38.12 ? 9   LYS B C   1 
ATOM   1155 O  O   . LYS B 1 9   ? -15.836 0.163   43.271  1.00 38.00 ? 9   LYS B O   1 
ATOM   1156 C  CB  . LYS B 1 9   ? -17.500 2.086   41.270  1.00 38.36 ? 9   LYS B CB  1 
ATOM   1157 C  CG  . LYS B 1 9   ? -17.671 3.378   40.464  1.00 40.09 ? 9   LYS B CG  1 
ATOM   1158 C  CD  . LYS B 1 9   ? -18.100 3.096   39.021  1.00 40.22 ? 9   LYS B CD  1 
ATOM   1159 C  CE  . LYS B 1 9   ? -18.525 4.380   38.297  1.00 41.45 ? 9   LYS B CE  1 
ATOM   1160 N  NZ  . LYS B 1 9   ? -19.070 4.129   36.931  1.00 43.12 ? 9   LYS B NZ  1 
ATOM   1161 N  N   . GLY B 1 10  ? -17.851 0.695   44.113  1.00 38.76 ? 10  GLY B N   1 
ATOM   1162 C  CA  . GLY B 1 10  ? -18.006 -0.568  44.818  1.00 39.53 ? 10  GLY B CA  1 
ATOM   1163 C  C   . GLY B 1 10  ? -19.465 -0.934  44.982  1.00 40.16 ? 10  GLY B C   1 
ATOM   1164 O  O   . GLY B 1 10  ? -20.308 -0.501  44.190  1.00 40.64 ? 10  GLY B O   1 
ATOM   1165 N  N   . ASP B 1 11  ? -19.752 -1.731  46.010  1.00 40.90 ? 11  ASP B N   1 
ATOM   1166 C  CA  . ASP B 1 11  ? -21.109 -2.209  46.294  1.00 41.53 ? 11  ASP B CA  1 
ATOM   1167 C  C   . ASP B 1 11  ? -21.846 -1.346  47.319  1.00 41.57 ? 11  ASP B C   1 
ATOM   1168 O  O   . ASP B 1 11  ? -22.890 -1.757  47.825  1.00 42.22 ? 11  ASP B O   1 
ATOM   1169 C  CB  . ASP B 1 11  ? -21.067 -3.652  46.823  1.00 41.86 ? 11  ASP B CB  1 
ATOM   1170 C  CG  . ASP B 1 11  ? -20.491 -4.633  45.822  1.00 43.21 ? 11  ASP B CG  1 
ATOM   1171 O  OD1 . ASP B 1 11  ? -20.696 -4.448  44.605  1.00 44.87 ? 11  ASP B OD1 1 
ATOM   1172 O  OD2 . ASP B 1 11  ? -19.841 -5.605  46.264  1.00 43.84 ? 11  ASP B OD2 1 
ATOM   1173 N  N   . GLY B 1 12  ? -21.319 -0.161  47.625  1.00 41.39 ? 12  GLY B N   1 
ATOM   1174 C  CA  . GLY B 1 12  ? -21.909 0.696   48.650  1.00 41.22 ? 12  GLY B CA  1 
ATOM   1175 C  C   . GLY B 1 12  ? -21.907 2.167   48.275  1.00 40.99 ? 12  GLY B C   1 
ATOM   1176 O  O   . GLY B 1 12  ? -21.926 2.506   47.098  1.00 41.01 ? 12  GLY B O   1 
ATOM   1177 N  N   . PRO B 1 13  ? -21.896 3.056   49.282  1.00 40.85 ? 13  PRO B N   1 
ATOM   1178 C  CA  . PRO B 1 13  ? -21.911 4.494   49.022  1.00 40.41 ? 13  PRO B CA  1 
ATOM   1179 C  C   . PRO B 1 13  ? -20.552 5.058   48.595  1.00 39.88 ? 13  PRO B C   1 
ATOM   1180 O  O   . PRO B 1 13  ? -20.479 6.215   48.170  1.00 39.71 ? 13  PRO B O   1 
ATOM   1181 C  CB  . PRO B 1 13  ? -22.333 5.082   50.370  1.00 40.60 ? 13  PRO B CB  1 
ATOM   1182 C  CG  . PRO B 1 13  ? -21.801 4.119   51.372  1.00 41.04 ? 13  PRO B CG  1 
ATOM   1183 C  CD  . PRO B 1 13  ? -21.865 2.758   50.725  1.00 40.91 ? 13  PRO B CD  1 
ATOM   1184 N  N   . VAL B 1 14  ? -19.493 4.255   48.691  1.00 39.36 ? 14  VAL B N   1 
ATOM   1185 C  CA  . VAL B 1 14  ? -18.143 4.756   48.438  1.00 39.17 ? 14  VAL B CA  1 
ATOM   1186 C  C   . VAL B 1 14  ? -17.893 4.956   46.947  1.00 39.02 ? 14  VAL B C   1 
ATOM   1187 O  O   . VAL B 1 14  ? -17.942 4.004   46.158  1.00 39.38 ? 14  VAL B O   1 
ATOM   1188 C  CB  . VAL B 1 14  ? -17.047 3.824   49.003  1.00 39.01 ? 14  VAL B CB  1 
ATOM   1189 C  CG1 . VAL B 1 14  ? -15.662 4.459   48.813  1.00 39.01 ? 14  VAL B CG1 1 
ATOM   1190 C  CG2 . VAL B 1 14  ? -17.295 3.531   50.470  1.00 39.07 ? 14  VAL B CG2 1 
ATOM   1191 N  N   . GLN B 1 15  ? -17.617 6.200   46.567  1.00 38.56 ? 15  GLN B N   1 
ATOM   1192 C  CA  . GLN B 1 15  ? -17.246 6.519   45.197  1.00 38.32 ? 15  GLN B CA  1 
ATOM   1193 C  C   . GLN B 1 15  ? -16.260 7.672   45.175  1.00 37.50 ? 15  GLN B C   1 
ATOM   1194 O  O   . GLN B 1 15  ? -16.255 8.517   46.068  1.00 37.45 ? 15  GLN B O   1 
ATOM   1195 C  CB  . GLN B 1 15  ? -18.478 6.868   44.364  1.00 38.27 ? 15  GLN B CB  1 
ATOM   1196 C  CG  . GLN B 1 15  ? -19.178 8.147   44.777  1.00 39.32 ? 15  GLN B CG  1 
ATOM   1197 C  CD  . GLN B 1 15  ? -20.402 8.434   43.927  1.00 39.66 ? 15  GLN B CD  1 
ATOM   1198 O  OE1 . GLN B 1 15  ? -21.485 7.905   44.175  1.00 42.02 ? 15  GLN B OE1 1 
ATOM   1199 N  NE2 . GLN B 1 15  ? -20.233 9.283   42.920  1.00 42.11 ? 15  GLN B NE2 1 
ATOM   1200 N  N   . GLY B 1 16  ? -15.434 7.710   44.143  1.00 37.00 ? 16  GLY B N   1 
ATOM   1201 C  CA  . GLY B 1 16  ? -14.459 8.779   44.011  1.00 36.60 ? 16  GLY B CA  1 
ATOM   1202 C  C   . GLY B 1 16  ? -13.759 8.780   42.672  1.00 36.24 ? 16  GLY B C   1 
ATOM   1203 O  O   . GLY B 1 16  ? -13.880 7.840   41.889  1.00 35.55 ? 16  GLY B O   1 
ATOM   1204 N  N   . ILE B 1 17  ? -13.054 9.873   42.411  1.00 35.85 ? 17  ILE B N   1 
ATOM   1205 C  CA  . ILE B 1 17  ? -12.226 10.013  41.227  1.00 35.49 ? 17  ILE B CA  1 
ATOM   1206 C  C   . ILE B 1 17  ? -10.847 10.438  41.695  1.00 35.13 ? 17  ILE B C   1 
ATOM   1207 O  O   . ILE B 1 17  ? -10.711 11.425  42.422  1.00 34.91 ? 17  ILE B O   1 
ATOM   1208 C  CB  . ILE B 1 17  ? -12.773 11.087  40.260  1.00 35.53 ? 17  ILE B CB  1 
ATOM   1209 C  CG1 . ILE B 1 17  ? -14.180 10.717  39.778  1.00 35.80 ? 17  ILE B CG1 1 
ATOM   1210 C  CG2 . ILE B 1 17  ? -11.833 11.256  39.069  1.00 35.56 ? 17  ILE B CG2 1 
ATOM   1211 C  CD1 . ILE B 1 17  ? -14.906 11.853  39.140  1.00 35.96 ? 17  ILE B CD1 1 
ATOM   1212 N  N   . ILE B 1 18  ? -9.838  9.674   41.291  1.00 34.76 ? 18  ILE B N   1 
ATOM   1213 C  CA  . ILE B 1 18  ? -8.447  9.961   41.629  1.00 34.79 ? 18  ILE B CA  1 
ATOM   1214 C  C   . ILE B 1 18  ? -7.642  10.132  40.356  1.00 34.61 ? 18  ILE B C   1 
ATOM   1215 O  O   . ILE B 1 18  ? -7.635  9.260   39.490  1.00 34.44 ? 18  ILE B O   1 
ATOM   1216 C  CB  . ILE B 1 18  ? -7.832  8.843   42.503  1.00 34.77 ? 18  ILE B CB  1 
ATOM   1217 C  CG1 . ILE B 1 18  ? -8.583  8.735   43.833  1.00 35.04 ? 18  ILE B CG1 1 
ATOM   1218 C  CG2 . ILE B 1 18  ? -6.343  9.087   42.744  1.00 34.74 ? 18  ILE B CG2 1 
ATOM   1219 C  CD1 . ILE B 1 18  ? -8.520  9.987   44.712  1.00 34.99 ? 18  ILE B CD1 1 
ATOM   1220 N  N   . ASN B 1 19  ? -6.967  11.274  40.265  1.00 34.35 ? 19  ASN B N   1 
ATOM   1221 C  CA  . ASN B 1 19  ? -6.129  11.633  39.141  1.00 34.56 ? 19  ASN B CA  1 
ATOM   1222 C  C   . ASN B 1 19  ? -4.673  11.363  39.458  1.00 34.67 ? 19  ASN B C   1 
ATOM   1223 O  O   . ASN B 1 19  ? -4.261  11.503  40.603  1.00 33.84 ? 19  ASN B O   1 
ATOM   1224 C  CB  . ASN B 1 19  ? -6.294  13.120  38.861  1.00 34.50 ? 19  ASN B CB  1 
ATOM   1225 C  CG  . ASN B 1 19  ? -7.745  13.513  38.699  1.00 35.61 ? 19  ASN B CG  1 
ATOM   1226 O  OD1 . ASN B 1 19  ? -8.334  14.167  39.568  1.00 36.93 ? 19  ASN B OD1 1 
ATOM   1227 N  ND2 . ASN B 1 19  ? -8.340  13.083  37.601  1.00 35.79 ? 19  ASN B ND2 1 
ATOM   1228 N  N   . PHE B 1 20  ? -3.905  10.991  38.435  1.00 34.98 ? 20  PHE B N   1 
ATOM   1229 C  CA  . PHE B 1 20  ? -2.455  10.821  38.552  1.00 35.40 ? 20  PHE B CA  1 
ATOM   1230 C  C   . PHE B 1 20  ? -1.785  11.670  37.479  1.00 35.86 ? 20  PHE B C   1 
ATOM   1231 O  O   . PHE B 1 20  ? -2.215  11.665  36.328  1.00 35.41 ? 20  PHE B O   1 
ATOM   1232 C  CB  . PHE B 1 20  ? -2.039  9.367   38.312  1.00 35.60 ? 20  PHE B CB  1 
ATOM   1233 C  CG  . PHE B 1 20  ? -2.694  8.368   39.221  1.00 35.37 ? 20  PHE B CG  1 
ATOM   1234 C  CD1 . PHE B 1 20  ? -4.019  7.984   39.028  1.00 36.09 ? 20  PHE B CD1 1 
ATOM   1235 C  CD2 . PHE B 1 20  ? -1.983  7.788   40.266  1.00 35.99 ? 20  PHE B CD2 1 
ATOM   1236 C  CE1 . PHE B 1 20  ? -4.618  7.048   39.865  1.00 35.69 ? 20  PHE B CE1 1 
ATOM   1237 C  CE2 . PHE B 1 20  ? -2.576  6.851   41.101  1.00 36.29 ? 20  PHE B CE2 1 
ATOM   1238 C  CZ  . PHE B 1 20  ? -3.899  6.487   40.907  1.00 35.93 ? 20  PHE B CZ  1 
ATOM   1239 N  N   . GLU B 1 21  ? -0.713  12.369  37.835  1.00 36.29 ? 21  GLU B N   1 
ATOM   1240 C  CA  . GLU B 1 21  ? 0.084   13.064  36.839  1.00 36.46 ? 21  GLU B CA  1 
ATOM   1241 C  C   . GLU B 1 21  ? 1.555   12.943  37.177  1.00 36.10 ? 21  GLU B C   1 
ATOM   1242 O  O   . GLU B 1 21  ? 1.947   13.068  38.342  1.00 35.77 ? 21  GLU B O   1 
ATOM   1243 C  CB  . GLU B 1 21  ? -0.315  14.537  36.738  1.00 36.99 ? 21  GLU B CB  1 
ATOM   1244 C  CG  . GLU B 1 21  ? 0.375   15.280  35.597  1.00 37.49 ? 21  GLU B CG  1 
ATOM   1245 C  CD  . GLU B 1 21  ? -0.349  16.555  35.172  1.00 38.53 ? 21  GLU B CD  1 
ATOM   1246 O  OE1 . GLU B 1 21  ? -1.486  16.799  35.644  1.00 42.43 ? 21  GLU B OE1 1 
ATOM   1247 O  OE2 . GLU B 1 21  ? 0.219   17.309  34.352  1.00 41.04 ? 21  GLU B OE2 1 
ATOM   1248 N  N   . GLN B 1 22  ? 2.354   12.691  36.149  1.00 35.75 ? 22  GLN B N   1 
ATOM   1249 C  CA  . GLN B 1 22  ? 3.792   12.556  36.302  1.00 35.95 ? 22  GLN B CA  1 
ATOM   1250 C  C   . GLN B 1 22  ? 4.488   13.378  35.213  1.00 35.95 ? 22  GLN B C   1 
ATOM   1251 O  O   . GLN B 1 22  ? 4.548   12.970  34.055  1.00 35.77 ? 22  GLN B O   1 
ATOM   1252 C  CB  . GLN B 1 22  ? 4.175   11.082  36.219  1.00 35.58 ? 22  GLN B CB  1 
ATOM   1253 C  CG  . GLN B 1 22  ? 5.617   10.799  36.578  1.00 35.33 ? 22  GLN B CG  1 
ATOM   1254 C  CD  . GLN B 1 22  ? 5.957   9.326   36.533  1.00 36.00 ? 22  GLN B CD  1 
ATOM   1255 O  OE1 . GLN B 1 22  ? 5.264   8.536   35.888  1.00 34.72 ? 22  GLN B OE1 1 
ATOM   1256 N  NE2 . GLN B 1 22  ? 7.054   8.952   37.189  1.00 34.67 ? 22  GLN B NE2 1 
ATOM   1257 N  N   . LYS B 1 23  ? 5.007   14.540  35.598  1.00 36.47 ? 23  LYS B N   1 
ATOM   1258 C  CA  . LYS B 1 23  ? 5.595   15.482  34.656  1.00 36.89 ? 23  LYS B CA  1 
ATOM   1259 C  C   . LYS B 1 23  ? 6.860   14.934  33.991  1.00 36.87 ? 23  LYS B C   1 
ATOM   1260 O  O   . LYS B 1 23  ? 7.129   15.230  32.821  1.00 36.94 ? 23  LYS B O   1 
ATOM   1261 C  CB  . LYS B 1 23  ? 5.933   16.796  35.367  1.00 37.45 ? 23  LYS B CB  1 
ATOM   1262 C  CG  . LYS B 1 23  ? 4.729   17.533  35.942  1.00 38.11 ? 23  LYS B CG  1 
ATOM   1263 C  CD  . LYS B 1 23  ? 5.151   18.905  36.459  1.00 38.49 ? 23  LYS B CD  1 
ATOM   1264 C  CE  . LYS B 1 23  ? 4.076   19.542  37.324  1.00 39.29 ? 23  LYS B CE  1 
ATOM   1265 N  NZ  . LYS B 1 23  ? 4.575   20.796  37.956  1.00 39.92 ? 23  LYS B NZ  1 
ATOM   1266 N  N   . GLU B 1 24  ? 7.639   14.160  34.750  1.00 36.66 ? 24  GLU B N   1 
ATOM   1267 C  CA  . GLU B 1 24  ? 8.866   13.531  34.243  1.00 36.31 ? 24  GLU B CA  1 
ATOM   1268 C  C   . GLU B 1 24  ? 8.893   12.046  34.598  1.00 35.38 ? 24  GLU B C   1 
ATOM   1269 O  O   . GLU B 1 24  ? 8.499   11.661  35.698  1.00 34.81 ? 24  GLU B O   1 
ATOM   1270 C  CB  . GLU B 1 24  ? 10.102  14.220  34.816  1.00 37.28 ? 24  GLU B CB  1 
ATOM   1271 C  CG  . GLU B 1 24  ? 10.469  15.516  34.122  1.00 39.81 ? 24  GLU B CG  1 
ATOM   1272 C  CD  . GLU B 1 24  ? 9.810   16.736  34.729  1.00 42.69 ? 24  GLU B CD  1 
ATOM   1273 O  OE1 . GLU B 1 24  ? 9.533   16.729  35.949  1.00 45.65 ? 24  GLU B OE1 1 
ATOM   1274 O  OE2 . GLU B 1 24  ? 9.594   17.721  33.982  1.00 43.74 ? 24  GLU B OE2 1 
ATOM   1275 N  N   . SER B 1 25  ? 9.395   11.228  33.674  1.00 34.70 ? 25  SER B N   1 
ATOM   1276 C  CA  . SER B 1 25  ? 9.393   9.769   33.826  1.00 34.38 ? 25  SER B CA  1 
ATOM   1277 C  C   . SER B 1 25  ? 10.214  9.275   35.027  1.00 33.92 ? 25  SER B C   1 
ATOM   1278 O  O   . SER B 1 25  ? 9.947   8.186   35.548  1.00 33.78 ? 25  SER B O   1 
ATOM   1279 C  CB  . SER B 1 25  ? 9.874   9.093   32.540  1.00 34.38 ? 25  SER B CB  1 
ATOM   1280 O  OG  . SER B 1 25  ? 11.126  9.603   32.137  1.00 34.30 ? 25  SER B OG  1 
ATOM   1281 N  N   . ASN B 1 26  ? 11.191  10.075  35.466  1.00 33.68 ? 26  ASN B N   1 
ATOM   1282 C  CA  . ASN B 1 26  ? 11.945  9.793   36.700  1.00 33.77 ? 26  ASN B CA  1 
ATOM   1283 C  C   . ASN B 1 26  ? 11.651  10.788  37.827  1.00 33.93 ? 26  ASN B C   1 
ATOM   1284 O  O   . ASN B 1 26  ? 12.477  11.007  38.721  1.00 34.57 ? 26  ASN B O   1 
ATOM   1285 C  CB  . ASN B 1 26  ? 13.453  9.709   36.414  1.00 33.18 ? 26  ASN B CB  1 
ATOM   1286 C  CG  . ASN B 1 26  ? 14.064  11.050  36.027  1.00 33.14 ? 26  ASN B CG  1 
ATOM   1287 O  OD1 . ASN B 1 26  ? 13.388  11.924  35.480  1.00 31.54 ? 26  ASN B OD1 1 
ATOM   1288 N  ND2 . ASN B 1 26  ? 15.359  11.210  36.299  1.00 32.39 ? 26  ASN B ND2 1 
ATOM   1289 N  N   . GLY B 1 27  ? 10.466  11.381  37.783  1.00 34.33 ? 27  GLY B N   1 
ATOM   1290 C  CA  . GLY B 1 27  ? 10.031  12.313  38.810  1.00 34.45 ? 27  GLY B CA  1 
ATOM   1291 C  C   . GLY B 1 27  ? 8.846   11.760  39.578  1.00 34.58 ? 27  GLY B C   1 
ATOM   1292 O  O   . GLY B 1 27  ? 8.346   10.672  39.267  1.00 34.54 ? 27  GLY B O   1 
ATOM   1293 N  N   . PRO B 1 28  ? 8.380   12.509  40.584  1.00 34.73 ? 28  PRO B N   1 
ATOM   1294 C  CA  . PRO B 1 28  ? 7.264   12.052  41.408  1.00 34.65 ? 28  PRO B CA  1 
ATOM   1295 C  C   . PRO B 1 28  ? 5.946   12.004  40.648  1.00 34.58 ? 28  PRO B C   1 
ATOM   1296 O  O   . PRO B 1 28  ? 5.777   12.720  39.654  1.00 34.40 ? 28  PRO B O   1 
ATOM   1297 C  CB  . PRO B 1 28  ? 7.186   13.108  42.526  1.00 34.83 ? 28  PRO B CB  1 
ATOM   1298 C  CG  . PRO B 1 28  ? 8.426   13.906  42.426  1.00 35.30 ? 28  PRO B CG  1 
ATOM   1299 C  CD  . PRO B 1 28  ? 8.869   13.830  41.011  1.00 35.04 ? 28  PRO B CD  1 
ATOM   1300 N  N   . VAL B 1 29  ? 5.038   11.149  41.118  1.00 34.41 ? 29  VAL B N   1 
ATOM   1301 C  CA  . VAL B 1 29  ? 3.658   11.099  40.628  1.00 35.06 ? 29  VAL B CA  1 
ATOM   1302 C  C   . VAL B 1 29  ? 2.779   11.870  41.613  1.00 35.28 ? 29  VAL B C   1 
ATOM   1303 O  O   . VAL B 1 29  ? 2.807   11.597  42.812  1.00 35.14 ? 29  VAL B O   1 
ATOM   1304 C  CB  . VAL B 1 29  ? 3.120   9.650   40.511  1.00 34.84 ? 29  VAL B CB  1 
ATOM   1305 C  CG1 . VAL B 1 29  ? 1.707   9.652   39.941  1.00 35.33 ? 29  VAL B CG1 1 
ATOM   1306 C  CG2 . VAL B 1 29  ? 4.022   8.795   39.647  1.00 35.29 ? 29  VAL B CG2 1 
ATOM   1307 N  N   . LYS B 1 30  ? 2.044   12.857  41.107  1.00 35.81 ? 30  LYS B N   1 
ATOM   1308 C  CA  . LYS B 1 30  ? 1.056   13.590  41.896  1.00 35.95 ? 30  LYS B CA  1 
ATOM   1309 C  C   . LYS B 1 30  ? -0.263  12.835  41.837  1.00 36.07 ? 30  LYS B C   1 
ATOM   1310 O  O   . LYS B 1 30  ? -0.738  12.500  40.749  1.00 35.80 ? 30  LYS B O   1 
ATOM   1311 C  CB  . LYS B 1 30  ? 0.883   15.010  41.358  1.00 36.15 ? 30  LYS B CB  1 
ATOM   1312 C  CG  . LYS B 1 30  ? -0.088  15.882  42.157  1.00 36.72 ? 30  LYS B CG  1 
ATOM   1313 C  CD  . LYS B 1 30  ? 0.046   17.363  41.777  1.00 37.72 ? 30  LYS B CD  1 
ATOM   1314 C  CE  . LYS B 1 30  ? -1.293  18.092  41.830  1.00 38.89 ? 30  LYS B CE  1 
ATOM   1315 N  NZ  . LYS B 1 30  ? -1.891  18.135  43.180  1.00 41.53 ? 30  LYS B NZ  1 
ATOM   1316 N  N   . VAL B 1 31  ? -0.838  12.561  43.007  1.00 35.98 ? 31  VAL B N   1 
ATOM   1317 C  CA  . VAL B 1 31  ? -2.092  11.827  43.110  1.00 36.12 ? 31  VAL B CA  1 
ATOM   1318 C  C   . VAL B 1 31  ? -3.102  12.685  43.861  1.00 36.10 ? 31  VAL B C   1 
ATOM   1319 O  O   . VAL B 1 31  ? -2.885  13.049  45.019  1.00 36.02 ? 31  VAL B O   1 
ATOM   1320 C  CB  . VAL B 1 31  ? -1.889  10.478  43.847  1.00 36.29 ? 31  VAL B CB  1 
ATOM   1321 C  CG1 . VAL B 1 31  ? -3.156  9.644   43.823  1.00 37.43 ? 31  VAL B CG1 1 
ATOM   1322 C  CG2 . VAL B 1 31  ? -0.726  9.701   43.232  1.00 36.42 ? 31  VAL B CG2 1 
ATOM   1323 N  N   . TRP B 1 32  ? -4.215  13.012  43.209  1.00 35.89 ? 32  TRP B N   1 
ATOM   1324 C  CA  . TRP B 1 32  ? -5.196  13.867  43.837  1.00 35.59 ? 32  TRP B CA  1 
ATOM   1325 C  C   . TRP B 1 32  ? -6.610  13.571  43.378  1.00 35.23 ? 32  TRP B C   1 
ATOM   1326 O  O   . TRP B 1 32  ? -6.831  12.993  42.316  1.00 34.31 ? 32  TRP B O   1 
ATOM   1327 C  CB  . TRP B 1 32  ? -4.844  15.344  43.611  1.00 36.12 ? 32  TRP B CB  1 
ATOM   1328 C  CG  . TRP B 1 32  ? -5.218  15.903  42.270  1.00 36.55 ? 32  TRP B CG  1 
ATOM   1329 C  CD1 . TRP B 1 32  ? -6.283  16.711  41.995  1.00 36.87 ? 32  TRP B CD1 1 
ATOM   1330 C  CD2 . TRP B 1 32  ? -4.528  15.715  41.031  1.00 36.32 ? 32  TRP B CD2 1 
ATOM   1331 N  NE1 . TRP B 1 32  ? -6.305  17.030  40.666  1.00 36.88 ? 32  TRP B NE1 1 
ATOM   1332 C  CE2 . TRP B 1 32  ? -5.239  16.432  40.047  1.00 37.24 ? 32  TRP B CE2 1 
ATOM   1333 C  CE3 . TRP B 1 32  ? -3.384  15.007  40.654  1.00 36.82 ? 32  TRP B CE3 1 
ATOM   1334 C  CZ2 . TRP B 1 32  ? -4.842  16.466  38.710  1.00 36.82 ? 32  TRP B CZ2 1 
ATOM   1335 C  CZ3 . TRP B 1 32  ? -2.991  15.035  39.329  1.00 37.02 ? 32  TRP B CZ3 1 
ATOM   1336 C  CH2 . TRP B 1 32  ? -3.720  15.765  38.368  1.00 37.07 ? 32  TRP B CH2 1 
ATOM   1337 N  N   . GLY B 1 33  ? -7.555  13.984  44.205  1.00 35.27 ? 33  GLY B N   1 
ATOM   1338 C  CA  . GLY B 1 33  ? -8.959  13.795  43.921  1.00 35.26 ? 33  GLY B CA  1 
ATOM   1339 C  C   . GLY B 1 33  ? -9.757  13.781  45.200  1.00 35.47 ? 33  GLY B C   1 
ATOM   1340 O  O   . GLY B 1 33  ? -9.343  14.346  46.219  1.00 35.08 ? 33  GLY B O   1 
ATOM   1341 N  N   . SER B 1 34  ? -10.908 13.128  45.147  1.00 35.75 ? 34  SER B N   1 
ATOM   1342 C  CA  . SER B 1 34  ? -11.797 13.069  46.293  1.00 35.76 ? 34  SER B CA  1 
ATOM   1343 C  C   . SER B 1 34  ? -12.524 11.733  46.326  1.00 35.87 ? 34  SER B C   1 
ATOM   1344 O  O   . SER B 1 34  ? -12.888 11.184  45.280  1.00 36.18 ? 34  SER B O   1 
ATOM   1345 C  CB  . SER B 1 34  ? -12.802 14.221  46.236  1.00 35.94 ? 34  SER B CB  1 
ATOM   1346 O  OG  . SER B 1 34  ? -13.612 14.249  47.392  1.00 36.46 ? 34  SER B OG  1 
ATOM   1347 N  N   . ILE B 1 35  ? -12.713 11.208  47.530  1.00 35.73 ? 35  ILE B N   1 
ATOM   1348 C  CA  . ILE B 1 35  ? -13.513 10.011  47.733  1.00 35.82 ? 35  ILE B CA  1 
ATOM   1349 C  C   . ILE B 1 35  ? -14.607 10.378  48.725  1.00 35.61 ? 35  ILE B C   1 
ATOM   1350 O  O   . ILE B 1 35  ? -14.336 11.052  49.721  1.00 35.30 ? 35  ILE B O   1 
ATOM   1351 C  CB  . ILE B 1 35  ? -12.672 8.847   48.272  1.00 35.52 ? 35  ILE B CB  1 
ATOM   1352 C  CG1 . ILE B 1 35  ? -11.440 8.617   47.387  1.00 35.78 ? 35  ILE B CG1 1 
ATOM   1353 C  CG2 . ILE B 1 35  ? -13.498 7.566   48.351  1.00 35.75 ? 35  ILE B CG2 1 
ATOM   1354 C  CD1 . ILE B 1 35  ? -10.427 7.653   47.990  1.00 36.23 ? 35  ILE B CD1 1 
ATOM   1355 N  N   . LYS B 1 36  ? -15.838 9.959   48.443  1.00 35.85 ? 36  LYS B N   1 
ATOM   1356 C  CA  . LYS B 1 36  ? -16.962 10.214  49.348  1.00 36.17 ? 36  LYS B CA  1 
ATOM   1357 C  C   . LYS B 1 36  ? -17.681 8.924   49.726  1.00 35.84 ? 36  LYS B C   1 
ATOM   1358 O  O   . LYS B 1 36  ? -17.420 7.868   49.162  1.00 35.56 ? 36  LYS B O   1 
ATOM   1359 C  CB  . LYS B 1 36  ? -17.949 11.220  48.737  1.00 36.56 ? 36  LYS B CB  1 
ATOM   1360 C  CG  . LYS B 1 36  ? -18.622 10.766  47.453  1.00 37.18 ? 36  LYS B CG  1 
ATOM   1361 C  CD  . LYS B 1 36  ? -19.572 11.841  46.941  1.00 37.65 ? 36  LYS B CD  1 
ATOM   1362 C  CE  . LYS B 1 36  ? -20.453 11.321  45.825  1.00 39.31 ? 36  LYS B CE  1 
ATOM   1363 N  NZ  . LYS B 1 36  ? -21.504 10.396  46.341  1.00 41.70 ? 36  LYS B NZ  1 
ATOM   1364 N  N   . GLY B 1 37  ? -18.584 9.021   50.696  1.00 35.67 ? 37  GLY B N   1 
ATOM   1365 C  CA  . GLY B 1 37  ? -19.338 7.865   51.164  1.00 35.87 ? 37  GLY B CA  1 
ATOM   1366 C  C   . GLY B 1 37  ? -18.601 7.019   52.185  1.00 35.86 ? 37  GLY B C   1 
ATOM   1367 O  O   . GLY B 1 37  ? -19.035 5.910   52.500  1.00 36.15 ? 37  GLY B O   1 
ATOM   1368 N  N   . LEU B 1 38  ? -17.504 7.550   52.722  1.00 35.96 ? 38  LEU B N   1 
ATOM   1369 C  CA  . LEU B 1 38  ? -16.674 6.834   53.692  1.00 35.95 ? 38  LEU B CA  1 
ATOM   1370 C  C   . LEU B 1 38  ? -17.071 7.162   55.121  1.00 36.26 ? 38  LEU B C   1 
ATOM   1371 O  O   . LEU B 1 38  ? -17.708 8.182   55.378  1.00 36.63 ? 38  LEU B O   1 
ATOM   1372 C  CB  . LEU B 1 38  ? -15.200 7.204   53.503  1.00 35.68 ? 38  LEU B CB  1 
ATOM   1373 C  CG  . LEU B 1 38  ? -14.551 6.756   52.198  1.00 35.13 ? 38  LEU B CG  1 
ATOM   1374 C  CD1 . LEU B 1 38  ? -13.263 7.521   51.964  1.00 34.01 ? 38  LEU B CD1 1 
ATOM   1375 C  CD2 . LEU B 1 38  ? -14.293 5.256   52.206  1.00 35.71 ? 38  LEU B CD2 1 
ATOM   1376 N  N   . THR B 1 39  ? -16.698 6.284   56.045  1.00 36.39 ? 39  THR B N   1 
ATOM   1377 C  CA  . THR B 1 39  ? -16.778 6.587   57.463  1.00 36.53 ? 39  THR B CA  1 
ATOM   1378 C  C   . THR B 1 39  ? -15.656 7.556   57.818  1.00 36.71 ? 39  THR B C   1 
ATOM   1379 O  O   . THR B 1 39  ? -14.573 7.497   57.226  1.00 36.89 ? 39  THR B O   1 
ATOM   1380 C  CB  . THR B 1 39  ? -16.617 5.322   58.332  1.00 36.77 ? 39  THR B CB  1 
ATOM   1381 O  OG1 . THR B 1 39  ? -15.425 4.623   57.949  1.00 36.42 ? 39  THR B OG1 1 
ATOM   1382 C  CG2 . THR B 1 39  ? -17.820 4.406   58.182  1.00 36.91 ? 39  THR B CG2 1 
ATOM   1383 N  N   . GLU B 1 40  ? -15.924 8.440   58.779  1.00 36.80 ? 40  GLU B N   1 
ATOM   1384 C  CA  . GLU B 1 40  ? -14.924 9.372   59.295  1.00 36.71 ? 40  GLU B CA  1 
ATOM   1385 C  C   . GLU B 1 40  ? -13.692 8.598   59.756  1.00 36.67 ? 40  GLU B C   1 
ATOM   1386 O  O   . GLU B 1 40  ? -13.818 7.582   60.444  1.00 36.82 ? 40  GLU B O   1 
ATOM   1387 C  CB  . GLU B 1 40  ? -15.504 10.181  60.468  1.00 36.97 ? 40  GLU B CB  1 
ATOM   1388 C  CG  . GLU B 1 40  ? -14.641 11.351  60.917  1.00 36.98 ? 40  GLU B CG  1 
ATOM   1389 C  CD  . GLU B 1 40  ? -15.241 12.150  62.068  1.00 37.24 ? 40  GLU B CD  1 
ATOM   1390 O  OE1 . GLU B 1 40  ? -16.384 11.871  62.496  1.00 37.89 ? 40  GLU B OE1 1 
ATOM   1391 O  OE2 . GLU B 1 40  ? -14.558 13.075  62.554  1.00 38.34 ? 40  GLU B OE2 1 
ATOM   1392 N  N   . GLY B 1 41  ? -12.512 9.070   59.366  1.00 36.39 ? 41  GLY B N   1 
ATOM   1393 C  CA  . GLY B 1 41  ? -11.250 8.457   59.785  1.00 36.26 ? 41  GLY B CA  1 
ATOM   1394 C  C   . GLY B 1 41  ? -10.367 7.951   58.658  1.00 35.96 ? 41  GLY B C   1 
ATOM   1395 O  O   . GLY B 1 41  ? -10.571 8.278   57.479  1.00 35.15 ? 41  GLY B O   1 
ATOM   1396 N  N   . LEU B 1 42  ? -9.383  7.135   59.028  1.00 35.78 ? 42  LEU B N   1 
ATOM   1397 C  CA  . LEU B 1 42  ? -8.366  6.662   58.089  1.00 35.88 ? 42  LEU B CA  1 
ATOM   1398 C  C   . LEU B 1 42  ? -8.824  5.436   57.323  1.00 35.54 ? 42  LEU B C   1 
ATOM   1399 O  O   . LEU B 1 42  ? -9.457  4.541   57.897  1.00 35.79 ? 42  LEU B O   1 
ATOM   1400 C  CB  . LEU B 1 42  ? -7.079  6.297   58.831  1.00 36.18 ? 42  LEU B CB  1 
ATOM   1401 C  CG  . LEU B 1 42  ? -6.344  7.393   59.589  1.00 37.37 ? 42  LEU B CG  1 
ATOM   1402 C  CD1 . LEU B 1 42  ? -5.208  6.762   60.388  1.00 38.52 ? 42  LEU B CD1 1 
ATOM   1403 C  CD2 . LEU B 1 42  ? -5.818  8.442   58.644  1.00 38.17 ? 42  LEU B CD2 1 
ATOM   1404 N  N   . HIS B 1 43  ? -8.481  5.402   56.037  1.00 35.31 ? 43  HIS B N   1 
ATOM   1405 C  CA  . HIS B 1 43  ? -8.804  4.284   55.152  1.00 35.00 ? 43  HIS B CA  1 
ATOM   1406 C  C   . HIS B 1 43  ? -7.600  3.911   54.298  1.00 34.56 ? 43  HIS B C   1 
ATOM   1407 O  O   . HIS B 1 43  ? -7.013  4.772   53.642  1.00 34.32 ? 43  HIS B O   1 
ATOM   1408 C  CB  . HIS B 1 43  ? -9.977  4.655   54.249  1.00 35.27 ? 43  HIS B CB  1 
ATOM   1409 C  CG  . HIS B 1 43  ? -11.248 4.871   54.995  1.00 35.10 ? 43  HIS B CG  1 
ATOM   1410 N  ND1 . HIS B 1 43  ? -12.101 3.840   55.313  1.00 36.07 ? 43  HIS B ND1 1 
ATOM   1411 C  CD2 . HIS B 1 43  ? -11.791 5.990   55.532  1.00 36.28 ? 43  HIS B CD2 1 
ATOM   1412 C  CE1 . HIS B 1 43  ? -13.129 4.315   55.994  1.00 36.02 ? 43  HIS B CE1 1 
ATOM   1413 N  NE2 . HIS B 1 43  ? -12.964 5.618   56.141  1.00 35.82 ? 43  HIS B NE2 1 
ATOM   1414 N  N   . GLY B 1 44  ? -7.248  2.627   54.296  1.00 34.48 ? 44  GLY B N   1 
ATOM   1415 C  CA  . GLY B 1 44  ? -6.122  2.133   53.494  1.00 34.58 ? 44  GLY B CA  1 
ATOM   1416 C  C   . GLY B 1 44  ? -6.294  2.471   52.026  1.00 34.76 ? 44  GLY B C   1 
ATOM   1417 O  O   . GLY B 1 44  ? -7.398  2.398   51.499  1.00 34.85 ? 44  GLY B O   1 
ATOM   1418 N  N   . PHE B 1 45  ? -5.192  2.835   51.368  1.00 35.12 ? 45  PHE B N   1 
ATOM   1419 C  CA  . PHE B 1 45  ? -5.222  3.390   50.015  1.00 34.97 ? 45  PHE B CA  1 
ATOM   1420 C  C   . PHE B 1 45  ? -4.034  2.796   49.280  1.00 35.34 ? 45  PHE B C   1 
ATOM   1421 O  O   . PHE B 1 45  ? -2.891  3.158   49.564  1.00 35.49 ? 45  PHE B O   1 
ATOM   1422 C  CB  . PHE B 1 45  ? -5.118  4.912   50.122  1.00 35.57 ? 45  PHE B CB  1 
ATOM   1423 C  CG  . PHE B 1 45  ? -5.342  5.662   48.830  1.00 35.58 ? 45  PHE B CG  1 
ATOM   1424 C  CD1 . PHE B 1 45  ? -6.582  5.657   48.208  1.00 36.72 ? 45  PHE B CD1 1 
ATOM   1425 C  CD2 . PHE B 1 45  ? -4.338  6.456   48.293  1.00 36.49 ? 45  PHE B CD2 1 
ATOM   1426 C  CE1 . PHE B 1 45  ? -6.800  6.382   47.040  1.00 36.64 ? 45  PHE B CE1 1 
ATOM   1427 C  CE2 . PHE B 1 45  ? -4.547  7.176   47.126  1.00 37.20 ? 45  PHE B CE2 1 
ATOM   1428 C  CZ  . PHE B 1 45  ? -5.789  7.140   46.502  1.00 36.67 ? 45  PHE B CZ  1 
ATOM   1429 N  N   . HIS B 1 46  ? -4.299  1.849   48.376  1.00 35.17 ? 46  HIS B N   1 
ATOM   1430 C  CA  . HIS B 1 46  ? -3.234  1.048   47.759  1.00 35.47 ? 46  HIS B CA  1 
ATOM   1431 C  C   . HIS B 1 46  ? -3.447  0.793   46.273  1.00 35.08 ? 46  HIS B C   1 
ATOM   1432 O  O   . HIS B 1 46  ? -4.577  0.757   45.795  1.00 35.31 ? 46  HIS B O   1 
ATOM   1433 C  CB  . HIS B 1 46  ? -3.130  -0.332  48.427  1.00 36.00 ? 46  HIS B CB  1 
ATOM   1434 C  CG  . HIS B 1 46  ? -3.136  -0.303  49.925  1.00 36.85 ? 46  HIS B CG  1 
ATOM   1435 N  ND1 . HIS B 1 46  ? -4.045  -1.016  50.678  1.00 36.90 ? 46  HIS B ND1 1 
ATOM   1436 C  CD2 . HIS B 1 46  ? -2.342  0.344   50.811  1.00 37.63 ? 46  HIS B CD2 1 
ATOM   1437 C  CE1 . HIS B 1 46  ? -3.808  -0.814  51.961  1.00 37.86 ? 46  HIS B CE1 1 
ATOM   1438 N  NE2 . HIS B 1 46  ? -2.786  0.015   52.068  1.00 37.80 ? 46  HIS B NE2 1 
ATOM   1439 N  N   . VAL B 1 47  ? -2.346  0.579   45.562  1.00 34.47 ? 47  VAL B N   1 
ATOM   1440 C  CA  . VAL B 1 47  ? -2.388  0.068   44.203  1.00 34.51 ? 47  VAL B CA  1 
ATOM   1441 C  C   . VAL B 1 47  ? -2.217  -1.448  44.303  1.00 34.54 ? 47  VAL B C   1 
ATOM   1442 O  O   . VAL B 1 47  ? -1.255  -1.940  44.913  1.00 33.96 ? 47  VAL B O   1 
ATOM   1443 C  CB  . VAL B 1 47  ? -1.295  0.678   43.309  1.00 34.54 ? 47  VAL B CB  1 
ATOM   1444 C  CG1 . VAL B 1 47  ? -1.422  0.157   41.891  1.00 35.16 ? 47  VAL B CG1 1 
ATOM   1445 C  CG2 . VAL B 1 47  ? -1.391  2.194   43.308  1.00 34.51 ? 47  VAL B CG2 1 
ATOM   1446 N  N   . HIS B 1 48  ? -3.183  -2.170  43.741  1.00 34.40 ? 48  HIS B N   1 
ATOM   1447 C  CA  . HIS B 1 48  ? -3.160  -3.627  43.704  1.00 34.71 ? 48  HIS B CA  1 
ATOM   1448 C  C   . HIS B 1 48  ? -2.694  -4.110  42.329  1.00 34.90 ? 48  HIS B C   1 
ATOM   1449 O  O   . HIS B 1 48  ? -2.770  -3.373  41.335  1.00 34.74 ? 48  HIS B O   1 
ATOM   1450 C  CB  . HIS B 1 48  ? -4.534  -4.185  44.094  1.00 34.91 ? 48  HIS B CB  1 
ATOM   1451 C  CG  . HIS B 1 48  ? -4.852  -4.018  45.551  1.00 35.27 ? 48  HIS B CG  1 
ATOM   1452 N  ND1 . HIS B 1 48  ? -5.061  -5.086  46.396  1.00 35.17 ? 48  HIS B ND1 1 
ATOM   1453 C  CD2 . HIS B 1 48  ? -4.959  -2.907  46.317  1.00 35.56 ? 48  HIS B CD2 1 
ATOM   1454 C  CE1 . HIS B 1 48  ? -5.311  -4.639  47.615  1.00 36.34 ? 48  HIS B CE1 1 
ATOM   1455 N  NE2 . HIS B 1 48  ? -5.245  -3.319  47.596  1.00 36.18 ? 48  HIS B NE2 1 
ATOM   1456 N  N   . GLU B 1 49  ? -2.210  -5.348  42.279  1.00 34.89 ? 49  GLU B N   1 
ATOM   1457 C  CA  . GLU B 1 49  ? -1.441  -5.840  41.131  1.00 34.97 ? 49  GLU B CA  1 
ATOM   1458 C  C   . GLU B 1 49  ? -2.220  -5.857  39.808  1.00 34.89 ? 49  GLU B C   1 
ATOM   1459 O  O   . GLU B 1 49  ? -1.685  -5.468  38.768  1.00 34.96 ? 49  GLU B O   1 
ATOM   1460 C  CB  . GLU B 1 49  ? -0.893  -7.244  41.411  1.00 34.88 ? 49  GLU B CB  1 
ATOM   1461 C  CG  . GLU B 1 49  ? 0.104   -7.723  40.359  1.00 35.32 ? 49  GLU B CG  1 
ATOM   1462 C  CD  . GLU B 1 49  ? 0.712   -9.075  40.679  1.00 35.96 ? 49  GLU B CD  1 
ATOM   1463 O  OE1 . GLU B 1 49  ? 0.398   -9.642  41.743  1.00 36.55 ? 49  GLU B OE1 1 
ATOM   1464 O  OE2 . GLU B 1 49  ? 1.503   -9.574  39.856  1.00 36.68 ? 49  GLU B OE2 1 
ATOM   1465 N  N   . PHE B 1 50  ? -3.471  -6.302  39.842  1.00 34.74 ? 50  PHE B N   1 
ATOM   1466 C  CA  . PHE B 1 50  ? -4.199  -6.595  38.606  1.00 34.98 ? 50  PHE B CA  1 
ATOM   1467 C  C   . PHE B 1 50  ? -5.348  -5.625  38.345  1.00 35.14 ? 50  PHE B C   1 
ATOM   1468 O  O   . PHE B 1 50  ? -6.098  -5.280  39.259  1.00 34.56 ? 50  PHE B O   1 
ATOM   1469 C  CB  . PHE B 1 50  ? -4.719  -8.034  38.635  1.00 35.44 ? 50  PHE B CB  1 
ATOM   1470 C  CG  . PHE B 1 50  ? -3.633  -9.065  38.778  1.00 35.38 ? 50  PHE B CG  1 
ATOM   1471 C  CD1 . PHE B 1 50  ? -2.647  -9.188  37.805  1.00 36.06 ? 50  PHE B CD1 1 
ATOM   1472 C  CD2 . PHE B 1 50  ? -3.597  -9.913  39.877  1.00 36.45 ? 50  PHE B CD2 1 
ATOM   1473 C  CE1 . PHE B 1 50  ? -1.641  -10.134 37.929  1.00 36.31 ? 50  PHE B CE1 1 
ATOM   1474 C  CE2 . PHE B 1 50  ? -2.589  -10.861 40.011  1.00 36.05 ? 50  PHE B CE2 1 
ATOM   1475 C  CZ  . PHE B 1 50  ? -1.612  -10.974 39.033  1.00 36.04 ? 50  PHE B CZ  1 
ATOM   1476 N  N   . GLY B 1 51  ? -5.479  -5.197  37.085  1.00 35.06 ? 51  GLY B N   1 
ATOM   1477 C  CA  . GLY B 1 51  ? -6.604  -4.368  36.647  1.00 35.40 ? 51  GLY B CA  1 
ATOM   1478 C  C   . GLY B 1 51  ? -7.780  -5.248  36.270  1.00 35.41 ? 51  GLY B C   1 
ATOM   1479 O  O   . GLY B 1 51  ? -8.328  -5.132  35.176  1.00 35.25 ? 51  GLY B O   1 
ATOM   1480 N  N   . ASP B 1 52  ? -8.165  -6.134  37.180  1.00 35.91 ? 52  ASP B N   1 
ATOM   1481 C  CA  . ASP B 1 52  ? -9.150  -7.176  36.904  1.00 35.99 ? 52  ASP B CA  1 
ATOM   1482 C  C   . ASP B 1 52  ? -10.330 -6.972  37.850  1.00 36.36 ? 52  ASP B C   1 
ATOM   1483 O  O   . ASP B 1 52  ? -10.165 -7.071  39.063  1.00 36.20 ? 52  ASP B O   1 
ATOM   1484 C  CB  . ASP B 1 52  ? -8.502  -8.551  37.128  1.00 36.03 ? 52  ASP B CB  1 
ATOM   1485 C  CG  . ASP B 1 52  ? -9.431  -9.711  36.812  1.00 36.38 ? 52  ASP B CG  1 
ATOM   1486 O  OD1 . ASP B 1 52  ? -10.664 -9.538  36.867  1.00 37.34 ? 52  ASP B OD1 1 
ATOM   1487 O  OD2 . ASP B 1 52  ? -8.916  -10.812 36.521  1.00 35.40 ? 52  ASP B OD2 1 
ATOM   1488 N  N   . ASN B 1 53  ? -11.503 -6.669  37.298  1.00 36.81 ? 53  ASN B N   1 
ATOM   1489 C  CA  . ASN B 1 53  ? -12.704 -6.443  38.110  1.00 37.20 ? 53  ASN B CA  1 
ATOM   1490 C  C   . ASN B 1 53  ? -13.769 -7.515  37.899  1.00 37.13 ? 53  ASN B C   1 
ATOM   1491 O  O   . ASN B 1 53  ? -14.943 -7.292  38.202  1.00 37.01 ? 53  ASN B O   1 
ATOM   1492 C  CB  . ASN B 1 53  ? -13.288 -5.050  37.824  1.00 37.65 ? 53  ASN B CB  1 
ATOM   1493 C  CG  . ASN B 1 53  ? -14.287 -4.599  38.883  1.00 38.35 ? 53  ASN B CG  1 
ATOM   1494 O  OD1 . ASN B 1 53  ? -15.348 -4.062  38.562  1.00 42.97 ? 53  ASN B OD1 1 
ATOM   1495 N  ND2 . ASN B 1 53  ? -13.963 -4.838  40.145  1.00 40.40 ? 53  ASN B ND2 1 
ATOM   1496 N  N   . THR B 1 54  ? -13.356 -8.685  37.412  1.00 37.24 ? 54  THR B N   1 
ATOM   1497 C  CA  . THR B 1 54  ? -14.287 -9.765  37.081  1.00 37.67 ? 54  THR B CA  1 
ATOM   1498 C  C   . THR B 1 54  ? -15.102 -10.232 38.279  1.00 37.91 ? 54  THR B C   1 
ATOM   1499 O  O   . THR B 1 54  ? -16.279 -10.533 38.134  1.00 37.92 ? 54  THR B O   1 
ATOM   1500 C  CB  . THR B 1 54  ? -13.565 -10.991 36.492  1.00 37.70 ? 54  THR B CB  1 
ATOM   1501 O  OG1 . THR B 1 54  ? -12.511 -11.398 37.369  1.00 37.81 ? 54  THR B OG1 1 
ATOM   1502 C  CG2 . THR B 1 54  ? -12.997 -10.676 35.124  1.00 37.42 ? 54  THR B CG2 1 
ATOM   1503 N  N   . ALA B 1 55  ? -14.473 -10.300 39.451  1.00 38.32 ? 55  ALA B N   1 
ATOM   1504 C  CA  . ALA B 1 55  ? -15.175 -10.648 40.691  1.00 38.67 ? 55  ALA B CA  1 
ATOM   1505 C  C   . ALA B 1 55  ? -15.068 -9.506  41.691  1.00 39.07 ? 55  ALA B C   1 
ATOM   1506 O  O   . ALA B 1 55  ? -14.715 -9.717  42.857  1.00 40.02 ? 55  ALA B O   1 
ATOM   1507 C  CB  . ALA B 1 55  ? -14.616 -11.935 41.289  1.00 38.75 ? 55  ALA B CB  1 
ATOM   1508 N  N   . GLY B 1 56  ? -15.367 -8.294  41.235  1.00 38.94 ? 56  GLY B N   1 
ATOM   1509 C  CA  . GLY B 1 56  ? -15.316 -7.121  42.095  1.00 38.90 ? 56  GLY B CA  1 
ATOM   1510 C  C   . GLY B 1 56  ? -13.893 -6.746  42.465  1.00 39.07 ? 56  GLY B C   1 
ATOM   1511 O  O   . GLY B 1 56  ? -12.949 -7.034  41.722  1.00 39.18 ? 56  GLY B O   1 
ATOM   1512 N  N   . CYS B 1 57  ? -13.735 -6.098  43.612  1.00 38.85 ? 57  CYS B N   1 
ATOM   1513 C  CA  . CYS B 1 57  ? -12.428 -5.618  44.033  1.00 38.95 ? 57  CYS B CA  1 
ATOM   1514 C  C   . CYS B 1 57  ? -11.483 -6.743  44.471  1.00 38.26 ? 57  CYS B C   1 
ATOM   1515 O  O   . CYS B 1 57  ? -10.273 -6.548  44.498  1.00 38.11 ? 57  CYS B O   1 
ATOM   1516 C  CB  . CYS B 1 57  ? -12.580 -4.555  45.126  1.00 39.38 ? 57  CYS B CB  1 
ATOM   1517 S  SG  . CYS B 1 57  ? -13.401 -3.018  44.546  1.00 43.70 ? 57  CYS B SG  1 
ATOM   1518 N  N   . THR B 1 58  ? -12.022 -7.924  44.774  1.00 37.85 ? 58  THR B N   1 
ATOM   1519 C  CA  . THR B 1 58  ? -11.185 -9.062  45.172  1.00 37.50 ? 58  THR B CA  1 
ATOM   1520 C  C   . THR B 1 58  ? -10.285 -9.549  44.021  1.00 37.01 ? 58  THR B C   1 
ATOM   1521 O  O   . THR B 1 58  ? -9.170  -10.027 44.253  1.00 36.28 ? 58  THR B O   1 
ATOM   1522 C  CB  . THR B 1 58  ? -12.034 -10.237 45.715  1.00 37.63 ? 58  THR B CB  1 
ATOM   1523 O  OG1 . THR B 1 58  ? -12.926 -10.704 44.700  1.00 39.71 ? 58  THR B OG1 1 
ATOM   1524 C  CG2 . THR B 1 58  ? -12.841 -9.802  46.920  1.00 37.20 ? 58  THR B CG2 1 
ATOM   1525 N  N   . SER B 1 59  ? -10.768 -9.385  42.786  1.00 36.16 ? 59  SER B N   1 
ATOM   1526 C  CA  . SER B 1 59  ? -10.044 -9.794  41.577  1.00 36.09 ? 59  SER B CA  1 
ATOM   1527 C  C   . SER B 1 59  ? -8.763  -8.998  41.311  1.00 35.57 ? 59  SER B C   1 
ATOM   1528 O  O   . SER B 1 59  ? -7.903  -9.441  40.548  1.00 35.56 ? 59  SER B O   1 
ATOM   1529 C  CB  . SER B 1 59  ? -10.963 -9.670  40.355  1.00 35.61 ? 59  SER B CB  1 
ATOM   1530 O  OG  . SER B 1 59  ? -11.974 -10.642 40.405  1.00 38.08 ? 59  SER B OG  1 
ATOM   1531 N  N   . ALA B 1 60  ? -8.648  -7.821  41.921  1.00 35.22 ? 60  ALA B N   1 
ATOM   1532 C  CA  . ALA B 1 60  ? -7.450  -6.993  41.793  1.00 35.35 ? 60  ALA B CA  1 
ATOM   1533 C  C   . ALA B 1 60  ? -6.216  -7.646  42.409  1.00 35.37 ? 60  ALA B C   1 
ATOM   1534 O  O   . ALA B 1 60  ? -5.090  -7.198  42.172  1.00 35.81 ? 60  ALA B O   1 
ATOM   1535 C  CB  . ALA B 1 60  ? -7.687  -5.625  42.415  1.00 35.24 ? 60  ALA B CB  1 
ATOM   1536 N  N   . GLY B 1 61  ? -6.423  -8.698  43.196  1.00 35.58 ? 61  GLY B N   1 
ATOM   1537 C  CA  . GLY B 1 61  ? -5.323  -9.456  43.763  1.00 35.62 ? 61  GLY B CA  1 
ATOM   1538 C  C   . GLY B 1 61  ? -4.614  -8.686  44.858  1.00 35.69 ? 61  GLY B C   1 
ATOM   1539 O  O   . GLY B 1 61  ? -5.197  -7.781  45.467  1.00 35.51 ? 61  GLY B O   1 
ATOM   1540 N  N   . PRO B 1 62  ? -3.345  -9.040  45.119  1.00 35.72 ? 62  PRO B N   1 
ATOM   1541 C  CA  . PRO B 1 62  ? -2.602  -8.470  46.234  1.00 35.85 ? 62  PRO B CA  1 
ATOM   1542 C  C   . PRO B 1 62  ? -2.066  -7.071  45.947  1.00 36.06 ? 62  PRO B C   1 
ATOM   1543 O  O   . PRO B 1 62  ? -2.187  -6.563  44.832  1.00 35.73 ? 62  PRO B O   1 
ATOM   1544 C  CB  . PRO B 1 62  ? -1.439  -9.447  46.394  1.00 35.75 ? 62  PRO B CB  1 
ATOM   1545 C  CG  . PRO B 1 62  ? -1.176  -9.905  45.003  1.00 36.00 ? 62  PRO B CG  1 
ATOM   1546 C  CD  . PRO B 1 62  ? -2.534  -10.017 44.367  1.00 35.63 ? 62  PRO B CD  1 
ATOM   1547 N  N   . HIS B 1 63  ? -1.466  -6.464  46.967  1.00 36.35 ? 63  HIS B N   1 
ATOM   1548 C  CA  . HIS B 1 63  ? -0.748  -5.207  46.807  1.00 36.15 ? 63  HIS B CA  1 
ATOM   1549 C  C   . HIS B 1 63  ? 0.282   -5.371  45.692  1.00 35.72 ? 63  HIS B C   1 
ATOM   1550 O  O   . HIS B 1 63  ? 0.942   -6.413  45.597  1.00 35.51 ? 63  HIS B O   1 
ATOM   1551 C  CB  . HIS B 1 63  ? -0.034  -4.831  48.112  1.00 36.56 ? 63  HIS B CB  1 
ATOM   1552 C  CG  . HIS B 1 63  ? -0.952  -4.389  49.209  1.00 36.93 ? 63  HIS B CG  1 
ATOM   1553 N  ND1 . HIS B 1 63  ? -0.520  -3.632  50.278  1.00 37.94 ? 63  HIS B ND1 1 
ATOM   1554 C  CD2 . HIS B 1 63  ? -2.274  -4.597  49.408  1.00 37.71 ? 63  HIS B CD2 1 
ATOM   1555 C  CE1 . HIS B 1 63  ? -1.537  -3.395  51.088  1.00 38.08 ? 63  HIS B CE1 1 
ATOM   1556 N  NE2 . HIS B 1 63  ? -2.614  -3.965  50.580  1.00 37.77 ? 63  HIS B NE2 1 
ATOM   1557 N  N   . PHE B 1 64  ? 0.407   -4.353  44.845  1.00 35.01 ? 64  PHE B N   1 
ATOM   1558 C  CA  . PHE B 1 64  ? 1.403   -4.366  43.773  1.00 35.06 ? 64  PHE B CA  1 
ATOM   1559 C  C   . PHE B 1 64  ? 2.788   -4.277  44.408  1.00 34.85 ? 64  PHE B C   1 
ATOM   1560 O  O   . PHE B 1 64  ? 3.130   -3.280  45.037  1.00 34.37 ? 64  PHE B O   1 
ATOM   1561 C  CB  . PHE B 1 64  ? 1.156   -3.218  42.786  1.00 34.94 ? 64  PHE B CB  1 
ATOM   1562 C  CG  . PHE B 1 64  ? 2.115   -3.182  41.626  1.00 34.89 ? 64  PHE B CG  1 
ATOM   1563 C  CD1 . PHE B 1 64  ? 2.401   -4.327  40.895  1.00 34.67 ? 64  PHE B CD1 1 
ATOM   1564 C  CD2 . PHE B 1 64  ? 2.708   -1.982  41.239  1.00 34.85 ? 64  PHE B CD2 1 
ATOM   1565 C  CE1 . PHE B 1 64  ? 3.287   -4.284  39.817  1.00 35.00 ? 64  PHE B CE1 1 
ATOM   1566 C  CE2 . PHE B 1 64  ? 3.589   -1.932  40.166  1.00 34.57 ? 64  PHE B CE2 1 
ATOM   1567 C  CZ  . PHE B 1 64  ? 3.877   -3.079  39.450  1.00 34.51 ? 64  PHE B CZ  1 
ATOM   1568 N  N   . ASN B 1 65  ? 3.569   -5.341  44.248  1.00 35.17 ? 65  ASN B N   1 
ATOM   1569 C  CA  . ASN B 1 65  ? 4.826   -5.493  44.961  1.00 35.61 ? 65  ASN B CA  1 
ATOM   1570 C  C   . ASN B 1 65  ? 5.877   -6.167  44.077  1.00 35.86 ? 65  ASN B C   1 
ATOM   1571 O  O   . ASN B 1 65  ? 6.340   -7.263  44.386  1.00 35.89 ? 65  ASN B O   1 
ATOM   1572 C  CB  . ASN B 1 65  ? 4.570   -6.313  46.229  1.00 35.10 ? 65  ASN B CB  1 
ATOM   1573 C  CG  . ASN B 1 65  ? 5.799   -6.446  47.114  1.00 35.22 ? 65  ASN B CG  1 
ATOM   1574 O  OD1 . ASN B 1 65  ? 6.725   -5.637  47.053  1.00 34.16 ? 65  ASN B OD1 1 
ATOM   1575 N  ND2 . ASN B 1 65  ? 5.798   -7.468  47.957  1.00 35.57 ? 65  ASN B ND2 1 
ATOM   1576 N  N   . PRO B 1 66  ? 6.259   -5.508  42.972  1.00 36.37 ? 66  PRO B N   1 
ATOM   1577 C  CA  . PRO B 1 66  ? 7.177   -6.125  42.013  1.00 36.83 ? 66  PRO B CA  1 
ATOM   1578 C  C   . PRO B 1 66  ? 8.590   -6.389  42.556  1.00 37.28 ? 66  PRO B C   1 
ATOM   1579 O  O   . PRO B 1 66  ? 9.282   -7.273  42.048  1.00 37.19 ? 66  PRO B O   1 
ATOM   1580 C  CB  . PRO B 1 66  ? 7.205   -5.119  40.853  1.00 36.84 ? 66  PRO B CB  1 
ATOM   1581 C  CG  . PRO B 1 66  ? 6.813   -3.826  41.449  1.00 36.85 ? 66  PRO B CG  1 
ATOM   1582 C  CD  . PRO B 1 66  ? 5.849   -4.154  42.553  1.00 36.53 ? 66  PRO B CD  1 
ATOM   1583 N  N   . LEU B 1 67  ? 9.002   -5.641  43.579  1.00 37.70 ? 67  LEU B N   1 
ATOM   1584 C  CA  . LEU B 1 67  ? 10.332  -5.811  44.189  1.00 38.21 ? 67  LEU B CA  1 
ATOM   1585 C  C   . LEU B 1 67  ? 10.341  -6.752  45.399  1.00 38.32 ? 67  LEU B C   1 
ATOM   1586 O  O   . LEU B 1 67  ? 11.375  -6.896  46.070  1.00 37.95 ? 67  LEU B O   1 
ATOM   1587 C  CB  . LEU B 1 67  ? 10.915  -4.446  44.575  1.00 38.46 ? 67  LEU B CB  1 
ATOM   1588 C  CG  . LEU B 1 67  ? 10.893  -3.384  43.465  1.00 40.05 ? 67  LEU B CG  1 
ATOM   1589 C  CD1 . LEU B 1 67  ? 11.582  -2.114  43.935  1.00 40.95 ? 67  LEU B CD1 1 
ATOM   1590 C  CD2 . LEU B 1 67  ? 11.538  -3.893  42.176  1.00 41.27 ? 67  LEU B CD2 1 
ATOM   1591 N  N   . SER B 1 68  ? 9.201   -7.387  45.677  1.00 38.47 ? 68  SER B N   1 
ATOM   1592 C  CA  . SER B 1 68  ? 9.095   -8.407  46.730  1.00 38.88 ? 68  SER B CA  1 
ATOM   1593 C  C   . SER B 1 68  ? 9.571   -7.907  48.092  1.00 39.03 ? 68  SER B C   1 
ATOM   1594 O  O   . SER B 1 68  ? 10.402  -8.540  48.743  1.00 39.00 ? 68  SER B O   1 
ATOM   1595 C  CB  . SER B 1 68  ? 9.866   -9.670  46.334  1.00 38.81 ? 68  SER B CB  1 
ATOM   1596 O  OG  . SER B 1 68  ? 9.464   -10.110 45.049  1.00 39.63 ? 68  SER B OG  1 
ATOM   1597 N  N   . ARG B 1 69  ? 9.038   -6.763  48.510  1.00 39.30 ? 69  ARG B N   1 
ATOM   1598 C  CA  . ARG B 1 69  ? 9.369   -6.173  49.805  1.00 39.70 ? 69  ARG B CA  1 
ATOM   1599 C  C   . ARG B 1 69  ? 8.243   -6.437  50.806  1.00 39.58 ? 69  ARG B C   1 
ATOM   1600 O  O   . ARG B 1 69  ? 7.174   -6.928  50.440  1.00 39.27 ? 69  ARG B O   1 
ATOM   1601 C  CB  . ARG B 1 69  ? 9.599   -4.663  49.673  1.00 40.23 ? 69  ARG B CB  1 
ATOM   1602 C  CG  . ARG B 1 69  ? 10.404  -4.226  48.451  1.00 42.41 ? 69  ARG B CG  1 
ATOM   1603 C  CD  . ARG B 1 69  ? 11.857  -4.634  48.540  1.00 45.71 ? 69  ARG B CD  1 
ATOM   1604 N  NE  . ARG B 1 69  ? 12.621  -3.787  49.457  1.00 47.03 ? 69  ARG B NE  1 
ATOM   1605 C  CZ  . ARG B 1 69  ? 13.080  -2.569  49.161  1.00 47.83 ? 69  ARG B CZ  1 
ATOM   1606 N  NH1 . ARG B 1 69  ? 12.860  -2.022  47.966  1.00 48.58 ? 69  ARG B NH1 1 
ATOM   1607 N  NH2 . ARG B 1 69  ? 13.771  -1.888  50.071  1.00 47.64 ? 69  ARG B NH2 1 
ATOM   1608 N  N   . LYS B 1 70  ? 8.494   -6.116  52.075  1.00 39.35 ? 70  LYS B N   1 
ATOM   1609 C  CA  . LYS B 1 70  ? 7.469   -6.233  53.114  1.00 39.44 ? 70  LYS B CA  1 
ATOM   1610 C  C   . LYS B 1 70  ? 6.569   -5.005  53.098  1.00 39.06 ? 70  LYS B C   1 
ATOM   1611 O  O   . LYS B 1 70  ? 6.982   -3.943  52.642  1.00 39.41 ? 70  LYS B O   1 
ATOM   1612 C  CB  . LYS B 1 70  ? 8.117   -6.382  54.487  1.00 39.33 ? 70  LYS B CB  1 
ATOM   1613 C  CG  . LYS B 1 70  ? 8.929   -7.657  54.643  1.00 39.92 ? 70  LYS B CG  1 
ATOM   1614 C  CD  . LYS B 1 70  ? 9.899   -7.566  55.809  1.00 39.89 ? 70  LYS B CD  1 
ATOM   1615 C  CE  . LYS B 1 70  ? 10.665  -8.868  55.985  1.00 40.23 ? 70  LYS B CE  1 
ATOM   1616 N  NZ  . LYS B 1 70  ? 11.536  -8.854  57.194  1.00 40.63 ? 70  LYS B NZ  1 
ATOM   1617 N  N   . HIS B 1 71  ? 5.345   -5.151  53.595  1.00 38.98 ? 71  HIS B N   1 
ATOM   1618 C  CA  . HIS B 1 71  ? 4.398   -4.043  53.631  1.00 38.72 ? 71  HIS B CA  1 
ATOM   1619 C  C   . HIS B 1 71  ? 4.849   -2.947  54.588  1.00 38.81 ? 71  HIS B C   1 
ATOM   1620 O  O   . HIS B 1 71  ? 5.349   -3.233  55.676  1.00 38.80 ? 71  HIS B O   1 
ATOM   1621 C  CB  . HIS B 1 71  ? 3.007   -4.525  54.051  1.00 38.76 ? 71  HIS B CB  1 
ATOM   1622 C  CG  . HIS B 1 71  ? 2.022   -3.415  54.244  1.00 38.92 ? 71  HIS B CG  1 
ATOM   1623 N  ND1 . HIS B 1 71  ? 1.445   -2.743  53.189  1.00 38.17 ? 71  HIS B ND1 1 
ATOM   1624 C  CD2 . HIS B 1 71  ? 1.533   -2.843  55.368  1.00 38.13 ? 71  HIS B CD2 1 
ATOM   1625 C  CE1 . HIS B 1 71  ? 0.629   -1.814  53.656  1.00 38.66 ? 71  HIS B CE1 1 
ATOM   1626 N  NE2 . HIS B 1 71  ? 0.667   -1.852  54.976  1.00 37.97 ? 71  HIS B NE2 1 
ATOM   1627 N  N   . GLY B 1 72  ? 4.658   -1.694  54.186  1.00 38.46 ? 72  GLY B N   1 
ATOM   1628 C  CA  . GLY B 1 72  ? 4.961   -0.555  55.049  1.00 38.41 ? 72  GLY B CA  1 
ATOM   1629 C  C   . GLY B 1 72  ? 4.155   0.675   54.687  1.00 38.35 ? 72  GLY B C   1 
ATOM   1630 O  O   . GLY B 1 72  ? 3.212   0.604   53.890  1.00 38.11 ? 72  GLY B O   1 
ATOM   1631 N  N   . GLY B 1 73  ? 4.526   1.806   55.282  1.00 38.18 ? 73  GLY B N   1 
ATOM   1632 C  CA  . GLY B 1 73  ? 3.933   3.096   54.934  1.00 38.24 ? 73  GLY B CA  1 
ATOM   1633 C  C   . GLY B 1 73  ? 4.653   3.723   53.754  1.00 38.09 ? 73  GLY B C   1 
ATOM   1634 O  O   . GLY B 1 73  ? 5.756   3.300   53.408  1.00 37.70 ? 73  GLY B O   1 
ATOM   1635 N  N   . PRO B 1 74  ? 4.036   4.738   53.120  1.00 38.33 ? 74  PRO B N   1 
ATOM   1636 C  CA  . PRO B 1 74  ? 4.638   5.372   51.941  1.00 38.63 ? 74  PRO B CA  1 
ATOM   1637 C  C   . PRO B 1 74  ? 6.003   6.009   52.195  1.00 38.77 ? 74  PRO B C   1 
ATOM   1638 O  O   . PRO B 1 74  ? 6.811   6.077   51.273  1.00 38.48 ? 74  PRO B O   1 
ATOM   1639 C  CB  . PRO B 1 74  ? 3.612   6.438   51.536  1.00 38.60 ? 74  PRO B CB  1 
ATOM   1640 C  CG  . PRO B 1 74  ? 2.755   6.635   52.714  1.00 38.56 ? 74  PRO B CG  1 
ATOM   1641 C  CD  . PRO B 1 74  ? 2.734   5.338   53.456  1.00 38.51 ? 74  PRO B CD  1 
ATOM   1642 N  N   . LYS B 1 75  ? 6.248   6.463   53.427  1.00 39.10 ? 75  LYS B N   1 
ATOM   1643 C  CA  . LYS B 1 75  ? 7.526   7.067   53.803  1.00 39.81 ? 75  LYS B CA  1 
ATOM   1644 C  C   . LYS B 1 75  ? 8.611   6.032   54.100  1.00 39.82 ? 75  LYS B C   1 
ATOM   1645 O  O   . LYS B 1 75  ? 9.784   6.387   54.199  1.00 39.62 ? 75  LYS B O   1 
ATOM   1646 C  CB  . LYS B 1 75  ? 7.359   7.972   55.026  1.00 40.06 ? 75  LYS B CB  1 
ATOM   1647 C  CG  . LYS B 1 75  ? 6.560   9.243   54.775  1.00 40.89 ? 75  LYS B CG  1 
ATOM   1648 C  CD  . LYS B 1 75  ? 6.540   10.128  56.023  1.00 41.01 ? 75  LYS B CD  1 
ATOM   1649 C  CE  . LYS B 1 75  ? 6.089   11.548  55.715  1.00 41.76 ? 75  LYS B CE  1 
ATOM   1650 N  NZ  . LYS B 1 75  ? 6.580   12.522  56.732  1.00 42.76 ? 75  LYS B NZ  1 
ATOM   1651 N  N   . ASP B 1 76  ? 8.230   4.763   54.252  1.00 39.98 ? 76  ASP B N   1 
ATOM   1652 C  CA  . ASP B 1 76  ? 9.183   3.717   54.616  1.00 40.57 ? 76  ASP B CA  1 
ATOM   1653 C  C   . ASP B 1 76  ? 10.026  3.289   53.422  1.00 40.61 ? 76  ASP B C   1 
ATOM   1654 O  O   . ASP B 1 76  ? 9.550   3.259   52.298  1.00 40.98 ? 76  ASP B O   1 
ATOM   1655 C  CB  . ASP B 1 76  ? 8.470   2.495   55.206  1.00 40.40 ? 76  ASP B CB  1 
ATOM   1656 C  CG  . ASP B 1 76  ? 7.777   2.797   56.527  1.00 41.06 ? 76  ASP B CG  1 
ATOM   1657 O  OD1 . ASP B 1 76  ? 8.235   3.696   57.272  1.00 42.40 ? 76  ASP B OD1 1 
ATOM   1658 O  OD2 . ASP B 1 76  ? 6.780   2.112   56.832  1.00 40.84 ? 76  ASP B OD2 1 
ATOM   1659 N  N   . GLU B 1 77  ? 11.287  2.960   53.681  1.00 41.21 ? 77  GLU B N   1 
ATOM   1660 C  CA  . GLU B 1 77  ? 12.158  2.423   52.642  1.00 41.24 ? 77  GLU B CA  1 
ATOM   1661 C  C   . GLU B 1 77  ? 11.697  1.009   52.291  1.00 41.04 ? 77  GLU B C   1 
ATOM   1662 O  O   . GLU B 1 77  ? 11.682  0.626   51.122  1.00 41.49 ? 77  GLU B O   1 
ATOM   1663 C  CB  . GLU B 1 77  ? 13.615  2.437   53.100  1.00 41.79 ? 77  GLU B CB  1 
ATOM   1664 C  CG  . GLU B 1 77  ? 14.628  2.172   51.985  1.00 42.14 ? 77  GLU B CG  1 
ATOM   1665 C  CD  . GLU B 1 77  ? 16.066  2.463   52.406  1.00 42.96 ? 77  GLU B CD  1 
ATOM   1666 O  OE1 . GLU B 1 77  ? 16.287  3.192   53.408  1.00 46.64 ? 77  GLU B OE1 1 
ATOM   1667 O  OE2 . GLU B 1 77  ? 16.996  1.956   51.737  1.00 45.59 ? 77  GLU B OE2 1 
ATOM   1668 N  N   . GLU B 1 78  ? 11.296  0.251   53.309  1.00 40.84 ? 78  GLU B N   1 
ATOM   1669 C  CA  . GLU B 1 78  ? 10.714  -1.074  53.115  1.00 40.27 ? 78  GLU B CA  1 
ATOM   1670 C  C   . GLU B 1 78  ? 9.207   -0.956  52.918  1.00 39.61 ? 78  GLU B C   1 
ATOM   1671 O  O   . GLU B 1 78  ? 8.454   -0.786  53.877  1.00 39.23 ? 78  GLU B O   1 
ATOM   1672 C  CB  . GLU B 1 78  ? 11.023  -1.978  54.317  1.00 41.03 ? 78  GLU B CB  1 
ATOM   1673 C  CG  . GLU B 1 78  ? 10.644  -3.458  54.127  1.00 41.92 ? 78  GLU B CG  1 
ATOM   1674 C  CD  . GLU B 1 78  ? 11.496  -4.182  53.077  1.00 44.60 ? 78  GLU B CD  1 
ATOM   1675 O  OE1 . GLU B 1 78  ? 12.470  -3.586  52.560  1.00 46.36 ? 78  GLU B OE1 1 
ATOM   1676 O  OE2 . GLU B 1 78  ? 11.192  -5.361  52.772  1.00 44.67 ? 78  GLU B OE2 1 
ATOM   1677 N  N   . ARG B 1 79  ? 8.769   -1.039  51.666  1.00 38.73 ? 79  ARG B N   1 
ATOM   1678 C  CA  . ARG B 1 79  ? 7.344   -0.971  51.348  1.00 38.34 ? 79  ARG B CA  1 
ATOM   1679 C  C   . ARG B 1 79  ? 7.068   -1.579  49.984  1.00 37.61 ? 79  ARG B C   1 
ATOM   1680 O  O   . ARG B 1 79  ? 7.984   -1.761  49.188  1.00 37.53 ? 79  ARG B O   1 
ATOM   1681 C  CB  . ARG B 1 79  ? 6.853   0.477   51.399  1.00 38.24 ? 79  ARG B CB  1 
ATOM   1682 C  CG  . ARG B 1 79  ? 7.427   1.398   50.326  1.00 38.38 ? 79  ARG B CG  1 
ATOM   1683 C  CD  . ARG B 1 79  ? 6.385   1.822   49.279  1.00 39.63 ? 79  ARG B CD  1 
ATOM   1684 N  NE  . ARG B 1 79  ? 6.332   3.264   49.240  1.00 40.66 ? 79  ARG B NE  1 
ATOM   1685 C  CZ  . ARG B 1 79  ? 5.657   4.014   48.391  1.00 37.78 ? 79  ARG B CZ  1 
ATOM   1686 N  NH1 . ARG B 1 79  ? 4.881   3.522   47.408  1.00 38.02 ? 79  ARG B NH1 1 
ATOM   1687 N  NH2 . ARG B 1 79  ? 5.770   5.314   48.551  1.00 39.07 ? 79  ARG B NH2 1 
ATOM   1688 N  N   . HIS B 1 80  ? 5.805   -1.907  49.731  1.00 37.13 ? 80  HIS B N   1 
ATOM   1689 C  CA  . HIS B 1 80  ? 5.382   -2.332  48.393  1.00 36.82 ? 80  HIS B CA  1 
ATOM   1690 C  C   . HIS B 1 80  ? 5.331   -1.099  47.500  1.00 36.33 ? 80  HIS B C   1 
ATOM   1691 O  O   . HIS B 1 80  ? 5.084   0.001   47.984  1.00 35.99 ? 80  HIS B O   1 
ATOM   1692 C  CB  . HIS B 1 80  ? 3.986   -2.964  48.432  1.00 36.61 ? 80  HIS B CB  1 
ATOM   1693 C  CG  . HIS B 1 80  ? 3.871   -4.136  49.352  1.00 36.78 ? 80  HIS B CG  1 
ATOM   1694 N  ND1 . HIS B 1 80  ? 2.680   -4.508  49.938  1.00 36.93 ? 80  HIS B ND1 1 
ATOM   1695 C  CD2 . HIS B 1 80  ? 4.799   -5.014  49.798  1.00 36.90 ? 80  HIS B CD2 1 
ATOM   1696 C  CE1 . HIS B 1 80  ? 2.877   -5.575  50.693  1.00 36.13 ? 80  HIS B CE1 1 
ATOM   1697 N  NE2 . HIS B 1 80  ? 4.154   -5.901  50.625  1.00 37.07 ? 80  HIS B NE2 1 
ATOM   1698 N  N   . VAL B 1 81  ? 5.522   -1.273  46.197  1.00 35.77 ? 81  VAL B N   1 
ATOM   1699 C  CA  . VAL B 1 81  ? 5.296   -0.171  45.259  1.00 35.99 ? 81  VAL B CA  1 
ATOM   1700 C  C   . VAL B 1 81  ? 3.893   0.426   45.482  1.00 35.75 ? 81  VAL B C   1 
ATOM   1701 O  O   . VAL B 1 81  ? 3.710   1.645   45.475  1.00 35.93 ? 81  VAL B O   1 
ATOM   1702 C  CB  . VAL B 1 81  ? 5.481   -0.627  43.782  1.00 35.77 ? 81  VAL B CB  1 
ATOM   1703 C  CG1 . VAL B 1 81  ? 4.927   0.397   42.800  1.00 36.14 ? 81  VAL B CG1 1 
ATOM   1704 C  CG2 . VAL B 1 81  ? 6.962   -0.868  43.479  1.00 35.63 ? 81  VAL B CG2 1 
ATOM   1705 N  N   . GLY B 1 82  ? 2.916   -0.440  45.719  1.00 35.72 ? 82  GLY B N   1 
ATOM   1706 C  CA  . GLY B 1 82  ? 1.530   -0.015  45.904  1.00 35.79 ? 82  GLY B CA  1 
ATOM   1707 C  C   . GLY B 1 82  ? 1.142   0.580   47.250  1.00 36.09 ? 82  GLY B C   1 
ATOM   1708 O  O   . GLY B 1 82  ? -0.030  0.900   47.461  1.00 35.83 ? 82  GLY B O   1 
ATOM   1709 N  N   . ASP B 1 83  ? 2.100   0.731   48.165  1.00 35.94 ? 83  ASP B N   1 
ATOM   1710 C  CA  . ASP B 1 83  ? 1.795   1.175   49.532  1.00 36.44 ? 83  ASP B CA  1 
ATOM   1711 C  C   . ASP B 1 83  ? 1.691   2.693   49.616  1.00 36.76 ? 83  ASP B C   1 
ATOM   1712 O  O   . ASP B 1 83  ? 2.664   3.375   49.966  1.00 37.23 ? 83  ASP B O   1 
ATOM   1713 C  CB  . ASP B 1 83  ? 2.850   0.671   50.528  1.00 36.11 ? 83  ASP B CB  1 
ATOM   1714 C  CG  . ASP B 1 83  ? 2.669   -0.791  50.900  1.00 36.43 ? 83  ASP B CG  1 
ATOM   1715 O  OD1 . ASP B 1 83  ? 1.555   -1.329  50.729  1.00 37.20 ? 83  ASP B OD1 1 
ATOM   1716 O  OD2 . ASP B 1 83  ? 3.649   -1.407  51.374  1.00 36.67 ? 83  ASP B OD2 1 
ATOM   1717 N  N   . LEU B 1 84  ? 0.499   3.212   49.323  1.00 36.71 ? 84  LEU B N   1 
ATOM   1718 C  CA  . LEU B 1 84  ? 0.240   4.650   49.397  1.00 37.07 ? 84  LEU B CA  1 
ATOM   1719 C  C   . LEU B 1 84  ? -0.408  5.082   50.721  1.00 37.32 ? 84  LEU B C   1 
ATOM   1720 O  O   . LEU B 1 84  ? -0.935  6.191   50.829  1.00 38.10 ? 84  LEU B O   1 
ATOM   1721 C  CB  . LEU B 1 84  ? -0.607  5.093   48.195  1.00 37.38 ? 84  LEU B CB  1 
ATOM   1722 C  CG  . LEU B 1 84  ? 0.052   4.880   46.828  1.00 38.05 ? 84  LEU B CG  1 
ATOM   1723 C  CD1 . LEU B 1 84  ? -0.925  5.238   45.715  1.00 38.79 ? 84  LEU B CD1 1 
ATOM   1724 C  CD2 . LEU B 1 84  ? 1.320   5.693   46.695  1.00 38.69 ? 84  LEU B CD2 1 
ATOM   1725 N  N   . GLY B 1 85  ? -0.358  4.220   51.735  1.00 37.01 ? 85  GLY B N   1 
ATOM   1726 C  CA  . GLY B 1 85  ? -0.769  4.605   53.079  1.00 36.68 ? 85  GLY B CA  1 
ATOM   1727 C  C   . GLY B 1 85  ? -2.269  4.724   53.280  1.00 36.38 ? 85  GLY B C   1 
ATOM   1728 O  O   . GLY B 1 85  ? -3.010  3.800   52.972  1.00 36.51 ? 85  GLY B O   1 
ATOM   1729 N  N   . ASN B 1 86  ? -2.694  5.861   53.827  1.00 36.29 ? 86  ASN B N   1 
ATOM   1730 C  CA  . ASN B 1 86  ? -4.085  6.100   54.183  1.00 36.33 ? 86  ASN B CA  1 
ATOM   1731 C  C   . ASN B 1 86  ? -4.591  7.416   53.624  1.00 36.39 ? 86  ASN B C   1 
ATOM   1732 O  O   . ASN B 1 86  ? -3.833  8.374   53.494  1.00 36.14 ? 86  ASN B O   1 
ATOM   1733 C  CB  . ASN B 1 86  ? -4.243  6.169   55.706  1.00 36.40 ? 86  ASN B CB  1 
ATOM   1734 C  CG  . ASN B 1 86  ? -4.071  4.832   56.375  1.00 35.97 ? 86  ASN B CG  1 
ATOM   1735 O  OD1 . ASN B 1 86  ? -4.824  3.900   56.115  1.00 36.48 ? 86  ASN B OD1 1 
ATOM   1736 N  ND2 . ASN B 1 86  ? -3.088  4.736   57.267  1.00 35.04 ? 86  ASN B ND2 1 
ATOM   1737 N  N   . VAL B 1 87  ? -5.885  7.457   53.322  1.00 35.98 ? 87  VAL B N   1 
ATOM   1738 C  CA  . VAL B 1 87  ? -6.584  8.714   53.089  1.00 36.38 ? 87  VAL B CA  1 
ATOM   1739 C  C   . VAL B 1 87  ? -7.484  8.960   54.290  1.00 36.24 ? 87  VAL B C   1 
ATOM   1740 O  O   . VAL B 1 87  ? -7.946  8.016   54.924  1.00 36.37 ? 87  VAL B O   1 
ATOM   1741 C  CB  . VAL B 1 87  ? -7.414  8.700   51.790  1.00 36.38 ? 87  VAL B CB  1 
ATOM   1742 C  CG1 . VAL B 1 87  ? -6.511  8.448   50.605  1.00 37.44 ? 87  VAL B CG1 1 
ATOM   1743 C  CG2 . VAL B 1 87  ? -8.544  7.661   51.858  1.00 36.61 ? 87  VAL B CG2 1 
ATOM   1744 N  N   . THR B 1 88  ? -7.717  10.230  54.597  1.00 36.55 ? 88  THR B N   1 
ATOM   1745 C  CA  . THR B 1 88  ? -8.486  10.625  55.767  1.00 36.51 ? 88  THR B CA  1 
ATOM   1746 C  C   . THR B 1 88  ? -9.818  11.225  55.329  1.00 36.50 ? 88  THR B C   1 
ATOM   1747 O  O   . THR B 1 88  ? -9.846  12.213  54.599  1.00 36.22 ? 88  THR B O   1 
ATOM   1748 C  CB  . THR B 1 88  ? -7.706  11.662  56.610  1.00 36.76 ? 88  THR B CB  1 
ATOM   1749 O  OG1 . THR B 1 88  ? -6.438  11.111  56.996  1.00 37.41 ? 88  THR B OG1 1 
ATOM   1750 C  CG2 . THR B 1 88  ? -8.472  12.046  57.860  1.00 36.90 ? 88  THR B CG2 1 
ATOM   1751 N  N   . ALA B 1 89  ? -10.910 10.614  55.783  1.00 36.57 ? 89  ALA B N   1 
ATOM   1752 C  CA  . ALA B 1 89  ? -12.261 11.124  55.549  1.00 36.68 ? 89  ALA B CA  1 
ATOM   1753 C  C   . ALA B 1 89  ? -12.706 12.007  56.705  1.00 36.67 ? 89  ALA B C   1 
ATOM   1754 O  O   . ALA B 1 89  ? -12.502 11.667  57.878  1.00 36.42 ? 89  ALA B O   1 
ATOM   1755 C  CB  . ALA B 1 89  ? -13.236 9.969   55.364  1.00 36.57 ? 89  ALA B CB  1 
ATOM   1756 N  N   . ASP B 1 90  ? -13.326 13.139  56.372  1.00 36.74 ? 90  ASP B N   1 
ATOM   1757 C  CA  . ASP B 1 90  ? -13.821 14.082  57.378  1.00 36.85 ? 90  ASP B CA  1 
ATOM   1758 C  C   . ASP B 1 90  ? -15.152 13.603  57.978  1.00 36.75 ? 90  ASP B C   1 
ATOM   1759 O  O   . ASP B 1 90  ? -15.624 12.509  57.659  1.00 36.60 ? 90  ASP B O   1 
ATOM   1760 C  CB  . ASP B 1 90  ? -13.931 15.503  56.786  1.00 36.72 ? 90  ASP B CB  1 
ATOM   1761 C  CG  . ASP B 1 90  ? -14.957 15.616  55.656  1.00 37.18 ? 90  ASP B CG  1 
ATOM   1762 O  OD1 . ASP B 1 90  ? -15.875 14.772  55.555  1.00 36.45 ? 90  ASP B OD1 1 
ATOM   1763 O  OD2 . ASP B 1 90  ? -14.838 16.571  54.861  1.00 37.34 ? 90  ASP B OD2 1 
ATOM   1764 N  N   . LYS B 1 91  ? -15.750 14.415  58.848  1.00 36.99 ? 91  LYS B N   1 
ATOM   1765 C  CA  . LYS B 1 91  ? -17.016 14.060  59.500  1.00 37.01 ? 91  LYS B CA  1 
ATOM   1766 C  C   . LYS B 1 91  ? -18.180 13.902  58.518  1.00 36.98 ? 91  LYS B C   1 
ATOM   1767 O  O   . LYS B 1 91  ? -19.196 13.283  58.856  1.00 37.18 ? 91  LYS B O   1 
ATOM   1768 C  CB  . LYS B 1 91  ? -17.379 15.087  60.580  1.00 37.02 ? 91  LYS B CB  1 
ATOM   1769 C  CG  . LYS B 1 91  ? -17.709 16.483  60.057  1.00 37.31 ? 91  LYS B CG  1 
ATOM   1770 C  CD  . LYS B 1 91  ? -17.952 17.460  61.197  1.00 37.59 ? 91  LYS B CD  1 
ATOM   1771 C  CE  . LYS B 1 91  ? -17.968 18.898  60.709  1.00 37.65 ? 91  LYS B CE  1 
ATOM   1772 N  NZ  . LYS B 1 91  ? -17.930 19.853  61.850  1.00 38.11 ? 91  LYS B NZ  1 
ATOM   1773 N  N   . ASP B 1 92  ? -18.034 14.479  57.324  1.00 36.83 ? 92  ASP B N   1 
ATOM   1774 C  CA  . ASP B 1 92  ? -19.020 14.341  56.249  1.00 36.84 ? 92  ASP B CA  1 
ATOM   1775 C  C   . ASP B 1 92  ? -18.746 13.126  55.363  1.00 36.49 ? 92  ASP B C   1 
ATOM   1776 O  O   . ASP B 1 92  ? -19.472 12.887  54.403  1.00 36.51 ? 92  ASP B O   1 
ATOM   1777 C  CB  . ASP B 1 92  ? -19.035 15.603  55.379  1.00 36.96 ? 92  ASP B CB  1 
ATOM   1778 C  CG  . ASP B 1 92  ? -19.343 16.859  56.174  1.00 38.03 ? 92  ASP B CG  1 
ATOM   1779 O  OD1 . ASP B 1 92  ? -20.200 16.801  57.076  1.00 38.07 ? 92  ASP B OD1 1 
ATOM   1780 O  OD2 . ASP B 1 92  ? -18.725 17.907  55.888  1.00 41.15 ? 92  ASP B OD2 1 
ATOM   1781 N  N   . GLY B 1 93  ? -17.695 12.370  55.674  1.00 36.38 ? 93  GLY B N   1 
ATOM   1782 C  CA  . GLY B 1 93  ? -17.348 11.168  54.916  1.00 36.22 ? 93  GLY B CA  1 
ATOM   1783 C  C   . GLY B 1 93  ? -16.586 11.397  53.620  1.00 36.03 ? 93  GLY B C   1 
ATOM   1784 O  O   . GLY B 1 93  ? -16.502 10.494  52.785  1.00 35.56 ? 93  GLY B O   1 
ATOM   1785 N  N   . VAL B 1 94  ? -16.012 12.590  53.464  1.00 36.12 ? 94  VAL B N   1 
ATOM   1786 C  CA  . VAL B 1 94  ? -15.276 12.959  52.255  1.00 36.08 ? 94  VAL B CA  1 
ATOM   1787 C  C   . VAL B 1 94  ? -13.774 12.999  52.523  1.00 36.23 ? 94  VAL B C   1 
ATOM   1788 O  O   . VAL B 1 94  ? -13.317 13.693  53.430  1.00 35.90 ? 94  VAL B O   1 
ATOM   1789 C  CB  . VAL B 1 94  ? -15.726 14.335  51.725  1.00 36.12 ? 94  VAL B CB  1 
ATOM   1790 C  CG1 . VAL B 1 94  ? -14.977 14.702  50.442  1.00 36.32 ? 94  VAL B CG1 1 
ATOM   1791 C  CG2 . VAL B 1 94  ? -17.221 14.336  51.479  1.00 36.12 ? 94  VAL B CG2 1 
ATOM   1792 N  N   . ALA B 1 95  ? -13.022 12.248  51.728  1.00 36.33 ? 95  ALA B N   1 
ATOM   1793 C  CA  . ALA B 1 95  ? -11.561 12.271  51.766  1.00 36.73 ? 95  ALA B CA  1 
ATOM   1794 C  C   . ALA B 1 95  ? -11.008 13.039  50.573  1.00 37.01 ? 95  ALA B C   1 
ATOM   1795 O  O   . ALA B 1 95  ? -11.070 12.569  49.438  1.00 37.20 ? 95  ALA B O   1 
ATOM   1796 C  CB  . ALA B 1 95  ? -11.015 10.865  51.781  1.00 36.56 ? 95  ALA B CB  1 
ATOM   1797 N  N   . ASP B 1 96  ? -10.480 14.229  50.842  1.00 37.80 ? 96  ASP B N   1 
ATOM   1798 C  CA  . ASP B 1 96  ? -9.738  14.989  49.858  1.00 37.88 ? 96  ASP B CA  1 
ATOM   1799 C  C   . ASP B 1 96  ? -8.346  14.386  49.794  1.00 37.85 ? 96  ASP B C   1 
ATOM   1800 O  O   . ASP B 1 96  ? -7.644  14.336  50.801  1.00 37.37 ? 96  ASP B O   1 
ATOM   1801 C  CB  . ASP B 1 96  ? -9.647  16.459  50.267  1.00 38.39 ? 96  ASP B CB  1 
ATOM   1802 C  CG  . ASP B 1 96  ? -8.884  17.300  49.257  1.00 39.50 ? 96  ASP B CG  1 
ATOM   1803 O  OD1 . ASP B 1 96  ? -9.061  17.076  48.042  1.00 43.17 ? 96  ASP B OD1 1 
ATOM   1804 O  OD2 . ASP B 1 96  ? -8.105  18.184  49.679  1.00 42.63 ? 96  ASP B OD2 1 
ATOM   1805 N  N   . VAL B 1 97  ? -7.961  13.908  48.617  1.00 37.77 ? 97  VAL B N   1 
ATOM   1806 C  CA  . VAL B 1 97  ? -6.671  13.262  48.432  1.00 37.90 ? 97  VAL B CA  1 
ATOM   1807 C  C   . VAL B 1 97  ? -5.706  14.216  47.741  1.00 37.90 ? 97  VAL B C   1 
ATOM   1808 O  O   . VAL B 1 97  ? -6.008  14.771  46.688  1.00 37.18 ? 97  VAL B O   1 
ATOM   1809 C  CB  . VAL B 1 97  ? -6.797  11.982  47.594  1.00 37.87 ? 97  VAL B CB  1 
ATOM   1810 C  CG1 . VAL B 1 97  ? -5.422  11.314  47.428  1.00 37.80 ? 97  VAL B CG1 1 
ATOM   1811 C  CG2 . VAL B 1 97  ? -7.806  11.026  48.225  1.00 38.28 ? 97  VAL B CG2 1 
ATOM   1812 N  N   . SER B 1 98  ? -4.541  14.407  48.347  1.00 38.71 ? 98  SER B N   1 
ATOM   1813 C  CA  . SER B 1 98  ? -3.484  15.181  47.722  1.00 39.12 ? 98  SER B CA  1 
ATOM   1814 C  C   . SER B 1 98  ? -2.140  14.669  48.201  1.00 39.47 ? 98  SER B C   1 
ATOM   1815 O  O   . SER B 1 98  ? -1.718  14.966  49.316  1.00 39.70 ? 98  SER B O   1 
ATOM   1816 C  CB  . SER B 1 98  ? -3.633  16.666  48.037  1.00 39.35 ? 98  SER B CB  1 
ATOM   1817 O  OG  . SER B 1 98  ? -2.800  17.430  47.178  1.00 39.71 ? 98  SER B OG  1 
ATOM   1818 N  N   . ILE B 1 99  ? -1.485  13.863  47.371  1.00 39.60 ? 99  ILE B N   1 
ATOM   1819 C  CA  . ILE B 1 99  ? -0.180  13.340  47.733  1.00 39.72 ? 99  ILE B CA  1 
ATOM   1820 C  C   . ILE B 1 99  ? 0.758   13.293  46.543  1.00 39.44 ? 99  ILE B C   1 
ATOM   1821 O  O   . ILE B 1 99  ? 0.327   13.343  45.384  1.00 38.85 ? 99  ILE B O   1 
ATOM   1822 C  CB  . ILE B 1 99  ? -0.275  11.931  48.377  1.00 40.07 ? 99  ILE B CB  1 
ATOM   1823 C  CG1 . ILE B 1 99  ? -0.790  10.900  47.384  1.00 40.55 ? 99  ILE B CG1 1 
ATOM   1824 C  CG2 . ILE B 1 99  ? -1.157  11.960  49.629  1.00 41.07 ? 99  ILE B CG2 1 
ATOM   1825 C  CD1 . ILE B 1 99  ? -0.623  9.470   47.864  1.00 41.13 ? 99  ILE B CD1 1 
ATOM   1826 N  N   . GLU B 1 100 ? 2.045   13.223  46.855  1.00 39.08 ? 100 GLU B N   1 
ATOM   1827 C  CA  . GLU B 1 100 ? 3.072   12.986  45.857  1.00 39.05 ? 100 GLU B CA  1 
ATOM   1828 C  C   . GLU B 1 100 ? 3.831   11.739  46.270  1.00 38.40 ? 100 GLU B C   1 
ATOM   1829 O  O   . GLU B 1 100 ? 4.101   11.538  47.460  1.00 37.86 ? 100 GLU B O   1 
ATOM   1830 C  CB  . GLU B 1 100 ? 4.003   14.192  45.724  1.00 39.61 ? 100 GLU B CB  1 
ATOM   1831 C  CG  . GLU B 1 100 ? 3.297   15.409  45.127  1.00 40.64 ? 100 GLU B CG  1 
ATOM   1832 C  CD  . GLU B 1 100 ? 4.237   16.447  44.535  1.00 41.23 ? 100 GLU B CD  1 
ATOM   1833 O  OE1 . GLU B 1 100 ? 5.478   16.275  44.595  1.00 44.15 ? 100 GLU B OE1 1 
ATOM   1834 O  OE2 . GLU B 1 100 ? 3.720   17.454  43.996  1.00 43.71 ? 100 GLU B OE2 1 
ATOM   1835 N  N   . ASP B 1 101 ? 4.148   10.897  45.288  1.00 37.71 ? 101 ASP B N   1 
ATOM   1836 C  CA  . ASP B 1 101 ? 4.884   9.666   45.530  1.00 37.30 ? 101 ASP B CA  1 
ATOM   1837 C  C   . ASP B 1 101 ? 5.968   9.451   44.481  1.00 36.64 ? 101 ASP B C   1 
ATOM   1838 O  O   . ASP B 1 101 ? 5.725   9.607   43.284  1.00 35.90 ? 101 ASP B O   1 
ATOM   1839 C  CB  . ASP B 1 101 ? 3.946   8.467   45.535  1.00 37.41 ? 101 ASP B CB  1 
ATOM   1840 C  CG  . ASP B 1 101 ? 4.557   7.272   46.219  1.00 37.87 ? 101 ASP B CG  1 
ATOM   1841 O  OD1 . ASP B 1 101 ? 4.622   7.301   47.464  1.00 39.26 ? 101 ASP B OD1 1 
ATOM   1842 O  OD2 . ASP B 1 101 ? 5.002   6.326   45.533  1.00 37.11 ? 101 ASP B OD2 1 
ATOM   1843 N  N   . SER B 1 102 ? 7.152   9.065   44.944  1.00 36.12 ? 102 SER B N   1 
ATOM   1844 C  CA  . SER B 1 102 ? 8.307   8.871   44.070  1.00 36.07 ? 102 SER B CA  1 
ATOM   1845 C  C   . SER B 1 102 ? 8.664   7.395   43.854  1.00 35.56 ? 102 SER B C   1 
ATOM   1846 O  O   . SER B 1 102 ? 9.658   7.080   43.183  1.00 35.81 ? 102 SER B O   1 
ATOM   1847 C  CB  . SER B 1 102 ? 9.503   9.623   44.642  1.00 36.46 ? 102 SER B CB  1 
ATOM   1848 O  OG  . SER B 1 102 ? 9.341   11.019  44.452  1.00 38.04 ? 102 SER B OG  1 
ATOM   1849 N  N   . VAL B 1 103 ? 7.874   6.490   44.424  1.00 34.99 ? 103 VAL B N   1 
ATOM   1850 C  CA  . VAL B 1 103 ? 8.075   5.061   44.209  1.00 34.82 ? 103 VAL B CA  1 
ATOM   1851 C  C   . VAL B 1 103 ? 7.225   4.542   43.047  1.00 34.36 ? 103 VAL B C   1 
ATOM   1852 O  O   . VAL B 1 103 ? 7.742   3.872   42.164  1.00 33.76 ? 103 VAL B O   1 
ATOM   1853 C  CB  . VAL B 1 103 ? 7.803   4.266   45.490  1.00 35.01 ? 103 VAL B CB  1 
ATOM   1854 C  CG1 . VAL B 1 103 ? 7.818   2.768   45.218  1.00 35.57 ? 103 VAL B CG1 1 
ATOM   1855 C  CG2 . VAL B 1 103 ? 8.849   4.628   46.534  1.00 35.13 ? 103 VAL B CG2 1 
ATOM   1856 N  N   . ILE B 1 104 ? 5.927   4.829   43.066  1.00 33.65 ? 104 ILE B N   1 
ATOM   1857 C  CA  . ILE B 1 104 ? 5.070   4.492   41.925  1.00 34.28 ? 104 ILE B CA  1 
ATOM   1858 C  C   . ILE B 1 104 ? 5.504   5.277   40.691  1.00 34.15 ? 104 ILE B C   1 
ATOM   1859 O  O   . ILE B 1 104 ? 6.086   6.363   40.803  1.00 33.35 ? 104 ILE B O   1 
ATOM   1860 C  CB  . ILE B 1 104 ? 3.570   4.764   42.182  1.00 34.21 ? 104 ILE B CB  1 
ATOM   1861 C  CG1 . ILE B 1 104 ? 3.308   6.247   42.463  1.00 34.83 ? 104 ILE B CG1 1 
ATOM   1862 C  CG2 . ILE B 1 104 ? 3.050   3.889   43.312  1.00 34.32 ? 104 ILE B CG2 1 
ATOM   1863 C  CD1 . ILE B 1 104 ? 1.827   6.607   42.505  1.00 34.68 ? 104 ILE B CD1 1 
ATOM   1864 N  N   . SER B 1 105 ? 5.198   4.725   39.519  1.00 34.46 ? 105 SER B N   1 
ATOM   1865 C  CA  . SER B 1 105 ? 5.393   5.435   38.263  1.00 34.58 ? 105 SER B CA  1 
ATOM   1866 C  C   . SER B 1 105 ? 4.251   5.126   37.310  1.00 34.91 ? 105 SER B C   1 
ATOM   1867 O  O   . SER B 1 105 ? 3.579   4.105   37.440  1.00 35.03 ? 105 SER B O   1 
ATOM   1868 C  CB  . SER B 1 105 ? 6.717   5.040   37.617  1.00 34.32 ? 105 SER B CB  1 
ATOM   1869 O  OG  . SER B 1 105 ? 6.976   5.844   36.474  1.00 34.32 ? 105 SER B OG  1 
ATOM   1870 N  N   . LEU B 1 106 ? 4.030   6.025   36.364  1.00 34.96 ? 106 LEU B N   1 
ATOM   1871 C  CA  . LEU B 1 106 ? 3.032   5.811   35.318  1.00 35.32 ? 106 LEU B CA  1 
ATOM   1872 C  C   . LEU B 1 106 ? 3.653   5.236   34.040  1.00 35.58 ? 106 LEU B C   1 
ATOM   1873 O  O   . LEU B 1 106 ? 2.948   4.959   33.067  1.00 35.88 ? 106 LEU B O   1 
ATOM   1874 C  CB  . LEU B 1 106 ? 2.327   7.125   35.004  1.00 35.29 ? 106 LEU B CB  1 
ATOM   1875 C  CG  . LEU B 1 106 ? 1.571   7.844   36.121  1.00 35.38 ? 106 LEU B CG  1 
ATOM   1876 C  CD1 . LEU B 1 106 ? 0.862   9.032   35.514  1.00 35.67 ? 106 LEU B CD1 1 
ATOM   1877 C  CD2 . LEU B 1 106 ? 0.575   6.942   36.843  1.00 35.89 ? 106 LEU B CD2 1 
ATOM   1878 N  N   . SER B 1 107 ? 4.974   5.075   34.017  1.00 35.41 ? 107 SER B N   1 
ATOM   1879 C  CA  . SER B 1 107 ? 5.647   4.478   32.862  1.00 35.94 ? 107 SER B CA  1 
ATOM   1880 C  C   . SER B 1 107 ? 6.746   3.505   33.285  1.00 36.00 ? 107 SER B C   1 
ATOM   1881 O  O   . SER B 1 107 ? 7.088   3.407   34.466  1.00 35.00 ? 107 SER B O   1 
ATOM   1882 C  CB  . SER B 1 107 ? 6.218   5.567   31.949  1.00 35.89 ? 107 SER B CB  1 
ATOM   1883 O  OG  . SER B 1 107 ? 7.185   6.351   32.629  1.00 35.73 ? 107 SER B OG  1 
ATOM   1884 N  N   . GLY B 1 108 ? 7.285   2.784   32.305  1.00 36.48 ? 108 GLY B N   1 
ATOM   1885 C  CA  . GLY B 1 108 ? 8.300   1.769   32.548  1.00 37.41 ? 108 GLY B CA  1 
ATOM   1886 C  C   . GLY B 1 108 ? 7.710   0.413   32.874  1.00 38.02 ? 108 GLY B C   1 
ATOM   1887 O  O   . GLY B 1 108 ? 6.485   0.253   32.931  1.00 38.52 ? 108 GLY B O   1 
ATOM   1888 N  N   . ASP B 1 109 ? 8.589   -0.557  33.106  1.00 38.94 ? 109 ASP B N   1 
ATOM   1889 C  CA  . ASP B 1 109 ? 8.180   -1.945  33.364  1.00 39.26 ? 109 ASP B CA  1 
ATOM   1890 C  C   . ASP B 1 109 ? 7.230   -2.084  34.544  1.00 39.10 ? 109 ASP B C   1 
ATOM   1891 O  O   . ASP B 1 109 ? 6.382   -2.976  34.541  1.00 39.12 ? 109 ASP B O   1 
ATOM   1892 C  CB  . ASP B 1 109 ? 9.401   -2.837  33.624  1.00 39.76 ? 109 ASP B CB  1 
ATOM   1893 C  CG  . ASP B 1 109 ? 10.286  -2.993  32.414  1.00 40.97 ? 109 ASP B CG  1 
ATOM   1894 O  OD1 . ASP B 1 109 ? 10.031  -2.330  31.385  1.00 44.45 ? 109 ASP B OD1 1 
ATOM   1895 O  OD2 . ASP B 1 109 ? 11.251  -3.786  32.489  1.00 40.94 ? 109 ASP B OD2 1 
ATOM   1896 N  N   . HIS B 1 110 ? 7.370   -1.220  35.552  1.00 38.74 ? 110 HIS B N   1 
ATOM   1897 C  CA  . HIS B 1 110 ? 6.548   -1.302  36.761  1.00 38.30 ? 110 HIS B CA  1 
ATOM   1898 C  C   . HIS B 1 110 ? 5.436   -0.237  36.828  1.00 37.68 ? 110 HIS B C   1 
ATOM   1899 O  O   . HIS B 1 110 ? 4.924   0.079   37.903  1.00 37.67 ? 110 HIS B O   1 
ATOM   1900 C  CB  . HIS B 1 110 ? 7.446   -1.236  37.996  1.00 38.79 ? 110 HIS B CB  1 
ATOM   1901 C  CG  . HIS B 1 110 ? 8.455   -2.340  38.059  1.00 39.68 ? 110 HIS B CG  1 
ATOM   1902 N  ND1 . HIS B 1 110 ? 8.116   -3.666  37.898  1.00 40.93 ? 110 HIS B ND1 1 
ATOM   1903 C  CD2 . HIS B 1 110 ? 9.792   -2.316  38.263  1.00 40.67 ? 110 HIS B CD2 1 
ATOM   1904 C  CE1 . HIS B 1 110 ? 9.202   -4.411  37.991  1.00 40.19 ? 110 HIS B CE1 1 
ATOM   1905 N  NE2 . HIS B 1 110 ? 10.233  -3.616  38.212  1.00 41.23 ? 110 HIS B NE2 1 
ATOM   1906 N  N   . ALA B 1 111 ? 5.041   0.297   35.676  1.00 36.61 ? 111 ALA B N   1 
ATOM   1907 C  CA  . ALA B 1 111 ? 3.995   1.315   35.620  1.00 36.16 ? 111 ALA B CA  1 
ATOM   1908 C  C   . ALA B 1 111 ? 2.737   0.804   36.307  1.00 35.56 ? 111 ALA B C   1 
ATOM   1909 O  O   . ALA B 1 111 ? 2.453   -0.385  36.236  1.00 35.52 ? 111 ALA B O   1 
ATOM   1910 C  CB  . ALA B 1 111 ? 3.673   1.648   34.177  1.00 36.16 ? 111 ALA B CB  1 
ATOM   1911 N  N   . ILE B 1 112 ? 1.989   1.695   36.948  1.00 34.78 ? 112 ILE B N   1 
ATOM   1912 C  CA  . ILE B 1 112 ? 0.707   1.309   37.580  1.00 34.99 ? 112 ILE B CA  1 
ATOM   1913 C  C   . ILE B 1 112 ? -0.500  1.462   36.645  1.00 34.56 ? 112 ILE B C   1 
ATOM   1914 O  O   . ILE B 1 112 ? -1.621  1.103   37.015  1.00 34.36 ? 112 ILE B O   1 
ATOM   1915 C  CB  . ILE B 1 112 ? 0.437   2.072   38.897  1.00 34.76 ? 112 ILE B CB  1 
ATOM   1916 C  CG1 . ILE B 1 112 ? 0.259   3.575   38.652  1.00 35.28 ? 112 ILE B CG1 1 
ATOM   1917 C  CG2 . ILE B 1 112 ? 1.557   1.785   39.905  1.00 34.58 ? 112 ILE B CG2 1 
ATOM   1918 C  CD1 . ILE B 1 112 ? -0.088  4.350   39.866  1.00 35.84 ? 112 ILE B CD1 1 
ATOM   1919 N  N   . ILE B 1 113 ? -0.283  2.009   35.455  1.00 35.01 ? 113 ILE B N   1 
ATOM   1920 C  CA  . ILE B 1 113 ? -1.338  2.018   34.442  1.00 35.03 ? 113 ILE B CA  1 
ATOM   1921 C  C   . ILE B 1 113 ? -1.769  0.570   34.135  1.00 34.67 ? 113 ILE B C   1 
ATOM   1922 O  O   . ILE B 1 113 ? -0.941  -0.301  33.910  1.00 34.54 ? 113 ILE B O   1 
ATOM   1923 C  CB  . ILE B 1 113 ? -0.935  2.837   33.187  1.00 35.57 ? 113 ILE B CB  1 
ATOM   1924 C  CG1 . ILE B 1 113 ? -1.053  4.344   33.519  1.00 35.26 ? 113 ILE B CG1 1 
ATOM   1925 C  CG2 . ILE B 1 113 ? -1.843  2.483   32.011  1.00 34.98 ? 113 ILE B CG2 1 
ATOM   1926 C  CD1 . ILE B 1 113 ? -0.519  5.281   32.491  1.00 36.71 ? 113 ILE B CD1 1 
ATOM   1927 N  N   . GLY B 1 114 ? -3.077  0.327   34.153  1.00 34.81 ? 114 GLY B N   1 
ATOM   1928 C  CA  . GLY B 1 114 ? -3.631  -1.017  33.944  1.00 34.49 ? 114 GLY B CA  1 
ATOM   1929 C  C   . GLY B 1 114 ? -3.769  -1.838  35.219  1.00 34.73 ? 114 GLY B C   1 
ATOM   1930 O  O   . GLY B 1 114 ? -4.220  -2.977  35.174  1.00 34.60 ? 114 GLY B O   1 
ATOM   1931 N  N   . ARG B 1 115 ? -3.380  -1.265  36.355  1.00 34.45 ? 115 ARG B N   1 
ATOM   1932 C  CA  . ARG B 1 115 ? -3.535  -1.916  37.652  1.00 34.68 ? 115 ARG B CA  1 
ATOM   1933 C  C   . ARG B 1 115 ? -4.707  -1.258  38.401  1.00 34.90 ? 115 ARG B C   1 
ATOM   1934 O  O   . ARG B 1 115 ? -5.391  -0.397  37.839  1.00 35.76 ? 115 ARG B O   1 
ATOM   1935 C  CB  . ARG B 1 115 ? -2.203  -1.876  38.407  1.00 34.64 ? 115 ARG B CB  1 
ATOM   1936 C  CG  . ARG B 1 115 ? -1.073  -2.466  37.552  1.00 34.38 ? 115 ARG B CG  1 
ATOM   1937 C  CD  . ARG B 1 115 ? 0.234   -2.660  38.290  1.00 34.97 ? 115 ARG B CD  1 
ATOM   1938 N  NE  . ARG B 1 115 ? 1.288   -3.117  37.381  1.00 34.60 ? 115 ARG B NE  1 
ATOM   1939 C  CZ  . ARG B 1 115 ? 1.507   -4.385  37.035  1.00 34.38 ? 115 ARG B CZ  1 
ATOM   1940 N  NH1 . ARG B 1 115 ? 0.770   -5.372  37.521  1.00 34.74 ? 115 ARG B NH1 1 
ATOM   1941 N  NH2 . ARG B 1 115 ? 2.491   -4.672  36.201  1.00 35.02 ? 115 ARG B NH2 1 
ATOM   1942 N  N   . THR B 1 116 ? -4.963  -1.661  39.642  1.00 34.75 ? 116 THR B N   1 
ATOM   1943 C  CA  . THR B 1 116 ? -6.180  -1.223  40.328  1.00 34.76 ? 116 THR B CA  1 
ATOM   1944 C  C   . THR B 1 116 ? -5.871  -0.404  41.571  1.00 35.29 ? 116 THR B C   1 
ATOM   1945 O  O   . THR B 1 116 ? -5.051  -0.811  42.390  1.00 36.06 ? 116 THR B O   1 
ATOM   1946 C  CB  . THR B 1 116 ? -7.056  -2.424  40.725  1.00 34.82 ? 116 THR B CB  1 
ATOM   1947 O  OG1 . THR B 1 116 ? -7.492  -3.111  39.546  1.00 34.84 ? 116 THR B OG1 1 
ATOM   1948 C  CG2 . THR B 1 116 ? -8.268  -1.976  41.522  1.00 34.57 ? 116 THR B CG2 1 
ATOM   1949 N  N   . LEU B 1 117 ? -6.538  0.738   41.707  1.00 35.05 ? 117 LEU B N   1 
ATOM   1950 C  CA  . LEU B 1 117 ? -6.513  1.525   42.932  1.00 35.05 ? 117 LEU B CA  1 
ATOM   1951 C  C   . LEU B 1 117 ? -7.679  1.104   43.820  1.00 35.03 ? 117 LEU B C   1 
ATOM   1952 O  O   . LEU B 1 117 ? -8.825  1.041   43.351  1.00 34.12 ? 117 LEU B O   1 
ATOM   1953 C  CB  . LEU B 1 117 ? -6.636  3.007   42.597  1.00 35.15 ? 117 LEU B CB  1 
ATOM   1954 C  CG  . LEU B 1 117 ? -6.507  4.018   43.730  1.00 35.08 ? 117 LEU B CG  1 
ATOM   1955 C  CD1 . LEU B 1 117 ? -5.098  3.991   44.336  1.00 36.30 ? 117 LEU B CD1 1 
ATOM   1956 C  CD2 . LEU B 1 117 ? -6.863  5.401   43.219  1.00 35.78 ? 117 LEU B CD2 1 
ATOM   1957 N  N   . VAL B 1 118 ? -7.385  0.807   45.090  1.00 35.05 ? 118 VAL B N   1 
ATOM   1958 C  CA  . VAL B 1 118 ? -8.401  0.378   46.058  1.00 35.30 ? 118 VAL B CA  1 
ATOM   1959 C  C   . VAL B 1 118 ? -8.406  1.265   47.305  1.00 35.36 ? 118 VAL B C   1 
ATOM   1960 O  O   . VAL B 1 118 ? -7.343  1.634   47.824  1.00 35.02 ? 118 VAL B O   1 
ATOM   1961 C  CB  . VAL B 1 118 ? -8.174  -1.090  46.517  1.00 35.54 ? 118 VAL B CB  1 
ATOM   1962 C  CG1 . VAL B 1 118 ? -9.311  -1.560  47.419  1.00 36.09 ? 118 VAL B CG1 1 
ATOM   1963 C  CG2 . VAL B 1 118 ? -8.032  -2.028  45.320  1.00 35.90 ? 118 VAL B CG2 1 
ATOM   1964 N  N   . VAL B 1 119 ? -9.605  1.576   47.796  1.00 35.46 ? 119 VAL B N   1 
ATOM   1965 C  CA  . VAL B 1 119 ? -9.763  2.202   49.104  1.00 35.63 ? 119 VAL B CA  1 
ATOM   1966 C  C   . VAL B 1 119 ? -10.435 1.202   50.047  1.00 35.73 ? 119 VAL B C   1 
ATOM   1967 O  O   . VAL B 1 119 ? -11.387 0.505   49.662  1.00 35.22 ? 119 VAL B O   1 
ATOM   1968 C  CB  . VAL B 1 119 ? -10.548 3.534   49.051  1.00 35.93 ? 119 VAL B CB  1 
ATOM   1969 C  CG1 . VAL B 1 119 ? -11.977 3.327   48.510  1.00 35.37 ? 119 VAL B CG1 1 
ATOM   1970 C  CG2 . VAL B 1 119 ? -10.572 4.193   50.432  1.00 35.88 ? 119 VAL B CG2 1 
ATOM   1971 N  N   . HIS B 1 120 ? -9.931  1.146   51.277  1.00 35.76 ? 120 HIS B N   1 
ATOM   1972 C  CA  . HIS B 1 120 ? -10.259 0.071   52.204  1.00 36.33 ? 120 HIS B CA  1 
ATOM   1973 C  C   . HIS B 1 120 ? -11.176 0.489   53.346  1.00 36.44 ? 120 HIS B C   1 
ATOM   1974 O  O   . HIS B 1 120 ? -11.327 1.678   53.652  1.00 36.51 ? 120 HIS B O   1 
ATOM   1975 C  CB  . HIS B 1 120 ? -8.972  -0.537  52.770  1.00 36.56 ? 120 HIS B CB  1 
ATOM   1976 C  CG  . HIS B 1 120 ? -8.216  -1.362  51.779  1.00 37.19 ? 120 HIS B CG  1 
ATOM   1977 N  ND1 . HIS B 1 120 ? -8.330  -2.734  51.712  1.00 37.17 ? 120 HIS B ND1 1 
ATOM   1978 C  CD2 . HIS B 1 120 ? -7.342  -1.009  50.809  1.00 37.77 ? 120 HIS B CD2 1 
ATOM   1979 C  CE1 . HIS B 1 120 ? -7.553  -3.191  50.749  1.00 37.84 ? 120 HIS B CE1 1 
ATOM   1980 N  NE2 . HIS B 1 120 ? -6.954  -2.163  50.174  1.00 37.93 ? 120 HIS B NE2 1 
ATOM   1981 N  N   . GLU B 1 121 ? -11.774 -0.527  53.968  1.00 36.76 ? 121 GLU B N   1 
ATOM   1982 C  CA  . GLU B 1 121 ? -12.698 -0.381  55.089  1.00 36.75 ? 121 GLU B CA  1 
ATOM   1983 C  C   . GLU B 1 121 ? -12.083 0.334   56.292  1.00 36.84 ? 121 GLU B C   1 
ATOM   1984 O  O   . GLU B 1 121 ? -12.728 1.179   56.924  1.00 36.29 ? 121 GLU B O   1 
ATOM   1985 C  CB  . GLU B 1 121 ? -13.136 -1.777  55.538  1.00 36.67 ? 121 GLU B CB  1 
ATOM   1986 C  CG  . GLU B 1 121 ? -14.125 -1.817  56.685  1.00 37.09 ? 121 GLU B CG  1 
ATOM   1987 C  CD  . GLU B 1 121 ? -14.235 -3.199  57.312  1.00 37.43 ? 121 GLU B CD  1 
ATOM   1988 O  OE1 . GLU B 1 121 ? -13.537 -4.135  56.860  1.00 38.57 ? 121 GLU B OE1 1 
ATOM   1989 O  OE2 . GLU B 1 121 ? -15.022 -3.348  58.263  1.00 37.76 ? 121 GLU B OE2 1 
ATOM   1990 N  N   . LYS B 1 122 ? -10.849 -0.047  56.617  1.00 36.57 ? 122 LYS B N   1 
ATOM   1991 C  CA  . LYS B 1 122 ? -10.191 0.383   57.843  1.00 36.77 ? 122 LYS B CA  1 
ATOM   1992 C  C   . LYS B 1 122 ? -8.871  1.066   57.519  1.00 36.34 ? 122 LYS B C   1 
ATOM   1993 O  O   . LYS B 1 122 ? -8.419  1.065   56.376  1.00 36.14 ? 122 LYS B O   1 
ATOM   1994 C  CB  . LYS B 1 122 ? -9.905  -0.821  58.755  1.00 36.95 ? 122 LYS B CB  1 
ATOM   1995 C  CG  . LYS B 1 122 ? -11.109 -1.610  59.234  1.00 37.91 ? 122 LYS B CG  1 
ATOM   1996 C  CD  . LYS B 1 122 ? -10.650 -2.771  60.125  1.00 37.69 ? 122 LYS B CD  1 
ATOM   1997 C  CE  . LYS B 1 122 ? -11.785 -3.721  60.453  1.00 39.27 ? 122 LYS B CE  1 
ATOM   1998 N  NZ  . LYS B 1 122 ? -11.281 -5.019  60.999  1.00 39.98 ? 122 LYS B NZ  1 
ATOM   1999 N  N   . ALA B 1 123 ? -8.243  1.625   58.549  1.00 36.50 ? 123 ALA B N   1 
ATOM   2000 C  CA  . ALA B 1 123 ? -6.904  2.197   58.435  1.00 36.12 ? 123 ALA B CA  1 
ATOM   2001 C  C   . ALA B 1 123 ? -5.858  1.132   58.104  1.00 36.06 ? 123 ALA B C   1 
ATOM   2002 O  O   . ALA B 1 123 ? -5.907  0.012   58.623  1.00 36.42 ? 123 ALA B O   1 
ATOM   2003 C  CB  . ALA B 1 123 ? -6.528  2.899   59.743  1.00 36.38 ? 123 ALA B CB  1 
ATOM   2004 N  N   . ASP B 1 124 ? -4.917  1.501   57.238  1.00 35.73 ? 124 ASP B N   1 
ATOM   2005 C  CA  . ASP B 1 124 ? -3.675  0.761   57.030  1.00 35.18 ? 124 ASP B CA  1 
ATOM   2006 C  C   . ASP B 1 124 ? -2.812  0.999   58.278  1.00 34.74 ? 124 ASP B C   1 
ATOM   2007 O  O   . ASP B 1 124 ? -2.518  2.147   58.601  1.00 34.76 ? 124 ASP B O   1 
ATOM   2008 C  CB  . ASP B 1 124 ? -2.994  1.300   55.763  1.00 35.24 ? 124 ASP B CB  1 
ATOM   2009 C  CG  . ASP B 1 124 ? -1.695  0.585   55.407  1.00 35.64 ? 124 ASP B CG  1 
ATOM   2010 O  OD1 . ASP B 1 124 ? -1.159  -0.204  56.208  1.00 34.23 ? 124 ASP B OD1 1 
ATOM   2011 O  OD2 . ASP B 1 124 ? -1.197  0.840   54.289  1.00 36.24 ? 124 ASP B OD2 1 
ATOM   2012 N  N   . ASP B 1 125 ? -2.426  -0.071  58.980  1.00 33.92 ? 125 ASP B N   1 
ATOM   2013 C  CA  . ASP B 1 125 ? -1.591  0.062   60.190  1.00 33.71 ? 125 ASP B CA  1 
ATOM   2014 C  C   . ASP B 1 125 ? -0.098  0.229   59.868  1.00 33.47 ? 125 ASP B C   1 
ATOM   2015 O  O   . ASP B 1 125 ? 0.731   0.346   60.777  1.00 32.83 ? 125 ASP B O   1 
ATOM   2016 C  CB  . ASP B 1 125 ? -1.820  -1.099  61.180  1.00 33.46 ? 125 ASP B CB  1 
ATOM   2017 C  CG  . ASP B 1 125 ? -1.314  -2.448  60.670  1.00 33.20 ? 125 ASP B CG  1 
ATOM   2018 O  OD1 . ASP B 1 125 ? -0.423  -2.493  59.796  1.00 32.81 ? 125 ASP B OD1 1 
ATOM   2019 O  OD2 . ASP B 1 125 ? -1.802  -3.482  61.175  1.00 33.38 ? 125 ASP B OD2 1 
ATOM   2020 N  N   . LEU B 1 126 ? 0.220   0.235   58.575  1.00 33.67 ? 126 LEU B N   1 
ATOM   2021 C  CA  . LEU B 1 126 ? 1.562   0.528   58.067  1.00 33.73 ? 126 LEU B CA  1 
ATOM   2022 C  C   . LEU B 1 126 ? 2.606   -0.514  58.472  1.00 33.62 ? 126 LEU B C   1 
ATOM   2023 O  O   . LEU B 1 126 ? 3.801   -0.223  58.500  1.00 33.61 ? 126 LEU B O   1 
ATOM   2024 C  CB  . LEU B 1 126 ? 2.003   1.944   58.473  1.00 33.89 ? 126 LEU B CB  1 
ATOM   2025 C  CG  . LEU B 1 126 ? 0.996   3.081   58.234  1.00 34.68 ? 126 LEU B CG  1 
ATOM   2026 C  CD1 . LEU B 1 126 ? 1.618   4.426   58.600  1.00 35.32 ? 126 LEU B CD1 1 
ATOM   2027 C  CD2 . LEU B 1 126 ? 0.476   3.110   56.804  1.00 34.89 ? 126 LEU B CD2 1 
ATOM   2028 N  N   . GLY B 1 127 ? 2.155   -1.735  58.751  1.00 33.24 ? 127 GLY B N   1 
ATOM   2029 C  CA  . GLY B 1 127 ? 3.045   -2.808  59.189  1.00 33.31 ? 127 GLY B CA  1 
ATOM   2030 C  C   . GLY B 1 127 ? 3.364   -2.817  60.674  1.00 33.11 ? 127 GLY B C   1 
ATOM   2031 O  O   . GLY B 1 127 ? 4.176   -3.629  61.128  1.00 33.56 ? 127 GLY B O   1 
ATOM   2032 N  N   . LYS B 1 128 ? 2.707   -1.948  61.446  1.00 32.94 ? 128 LYS B N   1 
ATOM   2033 C  CA  . LYS B 1 128 ? 2.983   -1.816  62.877  1.00 32.83 ? 128 LYS B CA  1 
ATOM   2034 C  C   . LYS B 1 128 ? 1.783   -2.202  63.751  1.00 32.24 ? 128 LYS B C   1 
ATOM   2035 O  O   . LYS B 1 128 ? 1.588   -1.636  64.826  1.00 31.70 ? 128 LYS B O   1 
ATOM   2036 C  CB  . LYS B 1 128 ? 3.432   -0.383  63.198  1.00 33.44 ? 128 LYS B CB  1 
ATOM   2037 C  CG  . LYS B 1 128 ? 4.683   0.071   62.439  1.00 34.59 ? 128 LYS B CG  1 
ATOM   2038 C  CD  . LYS B 1 128 ? 5.919   -0.731  62.829  1.00 36.56 ? 128 LYS B CD  1 
ATOM   2039 C  CE  . LYS B 1 128 ? 7.100   -0.422  61.918  1.00 37.00 ? 128 LYS B CE  1 
ATOM   2040 N  NZ  . LYS B 1 128 ? 6.885   -0.977  60.559  1.00 39.51 ? 128 LYS B NZ  1 
ATOM   2041 N  N   . GLY B 1 129 ? 1.013   -3.188  63.295  1.00 31.79 ? 129 GLY B N   1 
ATOM   2042 C  CA  . GLY B 1 129 ? -0.166  -3.671  64.021  1.00 31.52 ? 129 GLY B CA  1 
ATOM   2043 C  C   . GLY B 1 129 ? 0.064   -4.888  64.894  1.00 31.25 ? 129 GLY B C   1 
ATOM   2044 O  O   . GLY B 1 129 ? -0.853  -5.336  65.577  1.00 30.37 ? 129 GLY B O   1 
ATOM   2045 N  N   . GLY B 1 130 ? 1.284   -5.428  64.880  1.00 31.18 ? 130 GLY B N   1 
ATOM   2046 C  CA  . GLY B 1 130 ? 1.670   -6.491  65.806  1.00 31.26 ? 130 GLY B CA  1 
ATOM   2047 C  C   . GLY B 1 130 ? 1.157   -7.890  65.512  1.00 31.20 ? 130 GLY B C   1 
ATOM   2048 O  O   . GLY B 1 130 ? 0.972   -8.688  66.438  1.00 30.85 ? 130 GLY B O   1 
ATOM   2049 N  N   . ASN B 1 131 ? 0.939   -8.199  64.234  1.00 31.73 ? 131 ASN B N   1 
ATOM   2050 C  CA  . ASN B 1 131 ? 0.560   -9.551  63.813  1.00 32.19 ? 131 ASN B CA  1 
ATOM   2051 C  C   . ASN B 1 131 ? 1.010   -9.843  62.379  1.00 32.63 ? 131 ASN B C   1 
ATOM   2052 O  O   . ASN B 1 131 ? 1.500   -8.953  61.690  1.00 32.39 ? 131 ASN B O   1 
ATOM   2053 C  CB  . ASN B 1 131 ? -0.952  -9.780  63.979  1.00 32.07 ? 131 ASN B CB  1 
ATOM   2054 C  CG  . ASN B 1 131 ? -1.798  -8.780  63.204  1.00 31.24 ? 131 ASN B CG  1 
ATOM   2055 O  OD1 . ASN B 1 131 ? -1.400  -8.288  62.156  1.00 30.00 ? 131 ASN B OD1 1 
ATOM   2056 N  ND2 . ASN B 1 131 ? -2.983  -8.485  63.725  1.00 31.92 ? 131 ASN B ND2 1 
ATOM   2057 N  N   . GLU B 1 132 ? 0.847   -11.094 61.953  1.00 33.73 ? 132 GLU B N   1 
ATOM   2058 C  CA  . GLU B 1 132 ? 1.284   -11.554 60.631  1.00 34.29 ? 132 GLU B CA  1 
ATOM   2059 C  C   . GLU B 1 132 ? 0.656   -10.733 59.505  1.00 34.62 ? 132 GLU B C   1 
ATOM   2060 O  O   . GLU B 1 132 ? 1.338   -10.322 58.559  1.00 34.87 ? 132 GLU B O   1 
ATOM   2061 C  CB  . GLU B 1 132 ? 0.927   -13.038 60.451  1.00 34.83 ? 132 GLU B CB  1 
ATOM   2062 C  CG  . GLU B 1 132 ? 1.476   -13.697 59.174  1.00 35.45 ? 132 GLU B CG  1 
ATOM   2063 C  CD  . GLU B 1 132 ? 2.780   -14.446 59.399  1.00 37.83 ? 132 GLU B CD  1 
ATOM   2064 O  OE1 . GLU B 1 132 ? 3.573   -14.034 60.278  1.00 40.09 ? 132 GLU B OE1 1 
ATOM   2065 O  OE2 . GLU B 1 132 ? 3.015   -15.455 58.692  1.00 38.25 ? 132 GLU B OE2 1 
ATOM   2066 N  N   . GLU B 1 133 ? -0.645  -10.487 59.612  1.00 35.01 ? 133 GLU B N   1 
ATOM   2067 C  CA  . GLU B 1 133 ? -1.384  -9.786  58.563  1.00 35.34 ? 133 GLU B CA  1 
ATOM   2068 C  C   . GLU B 1 133 ? -0.932  -8.332  58.421  1.00 35.41 ? 133 GLU B C   1 
ATOM   2069 O  O   . GLU B 1 133 ? -0.954  -7.781  57.323  1.00 35.19 ? 133 GLU B O   1 
ATOM   2070 C  CB  . GLU B 1 133 ? -2.890  -9.857  58.838  1.00 35.55 ? 133 GLU B CB  1 
ATOM   2071 C  CG  . GLU B 1 133 ? -3.777  -9.429  57.683  1.00 36.00 ? 133 GLU B CG  1 
ATOM   2072 C  CD  . GLU B 1 133 ? -3.557  -10.260 56.424  1.00 37.97 ? 133 GLU B CD  1 
ATOM   2073 O  OE1 . GLU B 1 133 ? -3.341  -11.485 56.534  1.00 40.62 ? 133 GLU B OE1 1 
ATOM   2074 O  OE2 . GLU B 1 133 ? -3.597  -9.686  55.324  1.00 38.88 ? 133 GLU B OE2 1 
ATOM   2075 N  N   . SER B 1 134 ? -0.499  -7.721  59.522  1.00 35.44 ? 134 SER B N   1 
ATOM   2076 C  CA  . SER B 1 134 ? -0.013  -6.341  59.486  1.00 36.23 ? 134 SER B CA  1 
ATOM   2077 C  C   . SER B 1 134 ? 1.129   -6.138  58.482  1.00 36.89 ? 134 SER B C   1 
ATOM   2078 O  O   . SER B 1 134 ? 1.137   -5.157  57.740  1.00 36.30 ? 134 SER B O   1 
ATOM   2079 C  CB  . SER B 1 134 ? 0.460   -5.886  60.868  1.00 35.89 ? 134 SER B CB  1 
ATOM   2080 O  OG  . SER B 1 134 ? 0.957   -4.565  60.780  1.00 34.87 ? 134 SER B OG  1 
ATOM   2081 N  N   . THR B 1 135 ? 2.084   -7.067  58.471  1.00 38.31 ? 135 THR B N   1 
ATOM   2082 C  CA  . THR B 1 135 ? 3.266   -6.959  57.603  1.00 39.17 ? 135 THR B CA  1 
ATOM   2083 C  C   . THR B 1 135 ? 3.032   -7.527  56.195  1.00 40.05 ? 135 THR B C   1 
ATOM   2084 O  O   . THR B 1 135 ? 3.937   -7.533  55.359  1.00 40.61 ? 135 THR B O   1 
ATOM   2085 C  CB  . THR B 1 135 ? 4.496   -7.632  58.264  1.00 39.19 ? 135 THR B CB  1 
ATOM   2086 O  OG1 . THR B 1 135 ? 4.237   -9.023  58.484  1.00 39.81 ? 135 THR B OG1 1 
ATOM   2087 C  CG2 . THR B 1 135 ? 4.821   -6.972  59.604  1.00 39.57 ? 135 THR B CG2 1 
ATOM   2088 N  N   . LYS B 1 136 ? 1.806   -7.971  55.931  1.00 40.89 ? 136 LYS B N   1 
ATOM   2089 C  CA  . LYS B 1 136 ? 1.406   -8.501  54.632  1.00 41.16 ? 136 LYS B CA  1 
ATOM   2090 C  C   . LYS B 1 136 ? 0.482   -7.512  53.910  1.00 41.53 ? 136 LYS B C   1 
ATOM   2091 O  O   . LYS B 1 136 ? 0.681   -7.203  52.725  1.00 42.52 ? 136 LYS B O   1 
ATOM   2092 C  CB  . LYS B 1 136 ? 0.707   -9.850  54.855  1.00 41.54 ? 136 LYS B CB  1 
ATOM   2093 C  CG  . LYS B 1 136 ? 0.889   -10.876 53.750  1.00 41.53 ? 136 LYS B CG  1 
ATOM   2094 C  CD  . LYS B 1 136 ? 0.562   -12.271 54.276  1.00 41.64 ? 136 LYS B CD  1 
ATOM   2095 C  CE  . LYS B 1 136 ? 0.546   -13.319 53.167  1.00 42.19 ? 136 LYS B CE  1 
ATOM   2096 N  NZ  . LYS B 1 136 ? 0.567   -14.709 53.723  1.00 42.38 ? 136 LYS B NZ  1 
ATOM   2097 N  N   . THR B 1 137 ? -0.530  -7.014  54.620  1.00 41.54 ? 137 THR B N   1 
ATOM   2098 C  CA  . THR B 1 137 ? -1.520  -6.092  54.043  1.00 41.11 ? 137 THR B CA  1 
ATOM   2099 C  C   . THR B 1 137 ? -1.837  -4.838  54.880  1.00 40.80 ? 137 THR B C   1 
ATOM   2100 O  O   . THR B 1 137 ? -2.569  -3.956  54.417  1.00 41.41 ? 137 THR B O   1 
ATOM   2101 C  CB  . THR B 1 137 ? -2.858  -6.819  53.802  1.00 41.47 ? 137 THR B CB  1 
ATOM   2102 O  OG1 . THR B 1 137 ? -3.405  -7.240  55.057  1.00 41.63 ? 137 THR B OG1 1 
ATOM   2103 C  CG2 . THR B 1 137 ? -2.662  -8.025  52.887  1.00 42.18 ? 137 THR B CG2 1 
ATOM   2104 N  N   . GLY B 1 138 ? -1.320  -4.753  56.103  1.00 39.94 ? 138 GLY B N   1 
ATOM   2105 C  CA  . GLY B 1 138 ? -1.610  -3.612  56.966  1.00 39.28 ? 138 GLY B CA  1 
ATOM   2106 C  C   . GLY B 1 138 ? -2.957  -3.668  57.669  1.00 38.57 ? 138 GLY B C   1 
ATOM   2107 O  O   . GLY B 1 138 ? -3.365  -2.693  58.300  1.00 37.74 ? 138 GLY B O   1 
ATOM   2108 N  N   . ASN B 1 139 ? -3.645  -4.804  57.570  1.00 38.37 ? 139 ASN B N   1 
ATOM   2109 C  CA  . ASN B 1 139 ? -4.916  -5.025  58.272  1.00 38.41 ? 139 ASN B CA  1 
ATOM   2110 C  C   . ASN B 1 139 ? -5.996  -3.972  57.999  1.00 38.17 ? 139 ASN B C   1 
ATOM   2111 O  O   . ASN B 1 139 ? -6.736  -3.575  58.904  1.00 38.31 ? 139 ASN B O   1 
ATOM   2112 C  CB  . ASN B 1 139 ? -4.665  -5.148  59.780  1.00 38.75 ? 139 ASN B CB  1 
ATOM   2113 C  CG  . ASN B 1 139 ? -4.233  -6.530  60.182  1.00 39.79 ? 139 ASN B CG  1 
ATOM   2114 O  OD1 . ASN B 1 139 ? -4.945  -7.502  59.934  1.00 40.64 ? 139 ASN B OD1 1 
ATOM   2115 N  ND2 . ASN B 1 139 ? -3.070  -6.630  60.833  1.00 40.84 ? 139 ASN B ND2 1 
ATOM   2116 N  N   . ALA B 1 140 ? -6.103  -3.549  56.745  1.00 37.81 ? 140 ALA B N   1 
ATOM   2117 C  CA  . ALA B 1 140 ? -7.023  -2.475  56.361  1.00 37.65 ? 140 ALA B CA  1 
ATOM   2118 C  C   . ALA B 1 140 ? -8.441  -2.981  56.052  1.00 37.60 ? 140 ALA B C   1 
ATOM   2119 O  O   . ALA B 1 140 ? -9.319  -2.193  55.700  1.00 37.31 ? 140 ALA B O   1 
ATOM   2120 C  CB  . ALA B 1 140 ? -6.470  -1.715  55.189  1.00 37.55 ? 140 ALA B CB  1 
ATOM   2121 N  N   . GLY B 1 141 ? -8.648  -4.288  56.175  1.00 37.38 ? 141 GLY B N   1 
ATOM   2122 C  CA  . GLY B 1 141 ? -9.975  -4.878  56.071  1.00 37.44 ? 141 GLY B CA  1 
ATOM   2123 C  C   . GLY B 1 141 ? -10.443 -5.000  54.636  1.00 37.24 ? 141 GLY B C   1 
ATOM   2124 O  O   . GLY B 1 141 ? -9.641  -5.081  53.702  1.00 37.43 ? 141 GLY B O   1 
ATOM   2125 N  N   . SER B 1 142 ? -11.758 -4.997  54.461  1.00 37.23 ? 142 SER B N   1 
ATOM   2126 C  CA  . SER B 1 142 ? -12.346 -5.224  53.155  1.00 37.18 ? 142 SER B CA  1 
ATOM   2127 C  C   . SER B 1 142 ? -12.094 -4.064  52.194  1.00 37.09 ? 142 SER B C   1 
ATOM   2128 O  O   . SER B 1 142 ? -11.701 -2.963  52.584  1.00 37.26 ? 142 SER B O   1 
ATOM   2129 C  CB  . SER B 1 142 ? -13.846 -5.492  53.288  1.00 37.16 ? 142 SER B CB  1 
ATOM   2130 O  OG  . SER B 1 142 ? -14.523 -4.339  53.741  1.00 37.94 ? 142 SER B OG  1 
ATOM   2131 N  N   . ARG B 1 143 ? -12.322 -4.347  50.923  1.00 36.79 ? 143 ARG B N   1 
ATOM   2132 C  CA  . ARG B 1 143 ? -12.136 -3.389  49.868  1.00 36.93 ? 143 ARG B CA  1 
ATOM   2133 C  C   . ARG B 1 143 ? -13.481 -2.741  49.598  1.00 36.41 ? 143 ARG B C   1 
ATOM   2134 O  O   . ARG B 1 143 ? -14.426 -3.427  49.214  1.00 37.37 ? 143 ARG B O   1 
ATOM   2135 C  CB  . ARG B 1 143 ? -11.589 -4.112  48.637  1.00 37.08 ? 143 ARG B CB  1 
ATOM   2136 C  CG  . ARG B 1 143 ? -10.356 -4.950  48.988  1.00 37.74 ? 143 ARG B CG  1 
ATOM   2137 C  CD  . ARG B 1 143 ? -9.697  -5.631  47.804  1.00 38.06 ? 143 ARG B CD  1 
ATOM   2138 N  NE  . ARG B 1 143 ? -8.614  -6.504  48.266  1.00 38.55 ? 143 ARG B NE  1 
ATOM   2139 C  CZ  . ARG B 1 143 ? -7.808  -7.209  47.472  1.00 38.86 ? 143 ARG B CZ  1 
ATOM   2140 N  NH1 . ARG B 1 143 ? -7.948  -7.164  46.153  1.00 37.63 ? 143 ARG B NH1 1 
ATOM   2141 N  NH2 . ARG B 1 143 ? -6.856  -7.971  48.010  1.00 38.20 ? 143 ARG B NH2 1 
ATOM   2142 N  N   . LEU B 1 144 ? -13.579 -1.432  49.823  1.00 35.78 ? 144 LEU B N   1 
ATOM   2143 C  CA  . LEU B 1 144 ? -14.860 -0.722  49.703  1.00 35.70 ? 144 LEU B CA  1 
ATOM   2144 C  C   . LEU B 1 144 ? -15.158 -0.283  48.275  1.00 35.36 ? 144 LEU B C   1 
ATOM   2145 O  O   . LEU B 1 144 ? -16.305 -0.283  47.854  1.00 34.59 ? 144 LEU B O   1 
ATOM   2146 C  CB  . LEU B 1 144 ? -14.882 0.522   50.588  1.00 35.88 ? 144 LEU B CB  1 
ATOM   2147 C  CG  . LEU B 1 144 ? -14.655 0.359   52.086  1.00 36.91 ? 144 LEU B CG  1 
ATOM   2148 C  CD1 . LEU B 1 144 ? -14.635 1.735   52.748  1.00 37.71 ? 144 LEU B CD1 1 
ATOM   2149 C  CD2 . LEU B 1 144 ? -15.711 -0.535  52.707  1.00 37.38 ? 144 LEU B CD2 1 
ATOM   2150 N  N   . ALA B 1 145 ? -14.123 0.140   47.554  1.00 35.00 ? 145 ALA B N   1 
ATOM   2151 C  CA  . ALA B 1 145 ? -14.282 0.587   46.174  1.00 35.03 ? 145 ALA B CA  1 
ATOM   2152 C  C   . ALA B 1 145 ? -12.952 0.498   45.458  1.00 34.99 ? 145 ALA B C   1 
ATOM   2153 O  O   . ALA B 1 145 ? -11.898 0.565   46.087  1.00 34.69 ? 145 ALA B O   1 
ATOM   2154 C  CB  . ALA B 1 145 ? -14.809 2.014   46.126  1.00 34.90 ? 145 ALA B CB  1 
ATOM   2155 N  N   . CYS B 1 146 ? -13.016 0.331   44.143  1.00 34.94 ? 146 CYS B N   1 
ATOM   2156 C  CA  . CYS B 1 146 ? -11.816 0.224   43.324  1.00 35.45 ? 146 CYS B CA  1 
ATOM   2157 C  C   . CYS B 1 146 ? -12.076 0.673   41.893  1.00 34.85 ? 146 CYS B C   1 
ATOM   2158 O  O   . CYS B 1 146 ? -13.217 0.862   41.471  1.00 34.54 ? 146 CYS B O   1 
ATOM   2159 C  CB  . CYS B 1 146 ? -11.292 -1.211  43.310  1.00 35.99 ? 146 CYS B CB  1 
ATOM   2160 S  SG  . CYS B 1 146 ? -12.485 -2.466  42.763  1.00 41.13 ? 146 CYS B SG  1 
ATOM   2161 N  N   . GLY B 1 147 ? -10.993 0.820   41.145  1.00 34.42 ? 147 GLY B N   1 
ATOM   2162 C  CA  . GLY B 1 147 ? -11.077 1.192   39.736  1.00 34.33 ? 147 GLY B CA  1 
ATOM   2163 C  C   . GLY B 1 147 ? -9.747  0.961   39.060  1.00 34.39 ? 147 GLY B C   1 
ATOM   2164 O  O   . GLY B 1 147 ? -8.696  1.130   39.680  1.00 34.04 ? 147 GLY B O   1 
ATOM   2165 N  N   . VAL B 1 148 ? -9.797  0.561   37.791  1.00 34.11 ? 148 VAL B N   1 
ATOM   2166 C  CA  . VAL B 1 148 ? -8.578  0.324   37.021  1.00 34.86 ? 148 VAL B CA  1 
ATOM   2167 C  C   . VAL B 1 148 ? -7.966  1.679   36.707  1.00 34.89 ? 148 VAL B C   1 
ATOM   2168 O  O   . VAL B 1 148 ? -8.676  2.643   36.418  1.00 35.13 ? 148 VAL B O   1 
ATOM   2169 C  CB  . VAL B 1 148 ? -8.864  -0.471  35.720  1.00 34.88 ? 148 VAL B CB  1 
ATOM   2170 C  CG1 . VAL B 1 148 ? -7.572  -0.741  34.965  1.00 35.25 ? 148 VAL B CG1 1 
ATOM   2171 C  CG2 . VAL B 1 148 ? -9.554  -1.783  36.035  1.00 35.28 ? 148 VAL B CG2 1 
ATOM   2172 N  N   . ILE B 1 149 ? -6.642  1.760   36.774  1.00 35.13 ? 149 ILE B N   1 
ATOM   2173 C  CA  . ILE B 1 149 ? -5.949  3.003   36.499  1.00 35.46 ? 149 ILE B CA  1 
ATOM   2174 C  C   . ILE B 1 149 ? -5.744  3.123   34.993  1.00 35.22 ? 149 ILE B C   1 
ATOM   2175 O  O   . ILE B 1 149 ? -5.014  2.329   34.389  1.00 35.16 ? 149 ILE B O   1 
ATOM   2176 C  CB  . ILE B 1 149 ? -4.610  3.066   37.248  1.00 35.75 ? 149 ILE B CB  1 
ATOM   2177 C  CG1 . ILE B 1 149 ? -4.852  2.968   38.760  1.00 35.98 ? 149 ILE B CG1 1 
ATOM   2178 C  CG2 . ILE B 1 149 ? -3.864  4.356   36.891  1.00 35.77 ? 149 ILE B CG2 1 
ATOM   2179 C  CD1 . ILE B 1 149 ? -3.607  2.659   39.564  1.00 35.62 ? 149 ILE B CD1 1 
ATOM   2180 N  N   . GLY B 1 150 ? -6.391  4.117   34.391  1.00 35.57 ? 150 GLY B N   1 
ATOM   2181 C  CA  . GLY B 1 150 ? -6.413  4.258   32.942  1.00 35.58 ? 150 GLY B CA  1 
ATOM   2182 C  C   . GLY B 1 150 ? -5.713  5.502   32.453  1.00 35.82 ? 150 GLY B C   1 
ATOM   2183 O  O   . GLY B 1 150 ? -5.552  6.470   33.195  1.00 35.59 ? 150 GLY B O   1 
ATOM   2184 N  N   . ILE B 1 151 ? -5.275  5.454   31.198  1.00 35.67 ? 151 ILE B N   1 
ATOM   2185 C  CA  . ILE B 1 151 ? -4.664  6.599   30.543  1.00 35.96 ? 151 ILE B CA  1 
ATOM   2186 C  C   . ILE B 1 151 ? -5.694  7.723   30.416  1.00 36.33 ? 151 ILE B C   1 
ATOM   2187 O  O   . ILE B 1 151 ? -6.840  7.486   30.004  1.00 35.63 ? 151 ILE B O   1 
ATOM   2188 C  CB  . ILE B 1 151 ? -4.132  6.220   29.143  1.00 35.93 ? 151 ILE B CB  1 
ATOM   2189 C  CG1 . ILE B 1 151 ? -3.016  5.182   29.271  1.00 35.48 ? 151 ILE B CG1 1 
ATOM   2190 C  CG2 . ILE B 1 151 ? -3.647  7.471   28.393  1.00 35.96 ? 151 ILE B CG2 1 
ATOM   2191 C  CD1 . ILE B 1 151 ? -2.566  4.595   27.970  1.00 35.61 ? 151 ILE B CD1 1 
ATOM   2192 N  N   . ALA B 1 152 ? -5.276  8.939   30.767  1.00 36.72 ? 152 ALA B N   1 
ATOM   2193 C  CA  . ALA B 1 152 ? -6.140  10.112  30.722  1.00 37.94 ? 152 ALA B CA  1 
ATOM   2194 C  C   . ALA B 1 152 ? -5.555  11.187  29.818  1.00 38.65 ? 152 ALA B C   1 
ATOM   2195 O  O   . ALA B 1 152 ? -4.349  11.206  29.559  1.00 38.97 ? 152 ALA B O   1 
ATOM   2196 C  CB  . ALA B 1 152 ? -6.359  10.660  32.117  1.00 37.98 ? 152 ALA B CB  1 
ATOM   2197 N  N   . GLN B 1 153 ? -6.430  12.078  29.359  1.00 39.78 ? 153 GLN B N   1 
ATOM   2198 C  CA  . GLN B 1 153 ? -6.079  13.161  28.447  1.00 40.34 ? 153 GLN B CA  1 
ATOM   2199 C  C   . GLN B 1 153 ? -5.259  14.224  29.164  1.00 41.25 ? 153 GLN B C   1 
ATOM   2200 O  O   . GLN B 1 153 ? -4.194  14.624  28.699  1.00 42.55 ? 153 GLN B O   1 
ATOM   2201 C  CB  . GLN B 1 153 ? -7.360  13.789  27.893  1.00 40.74 ? 153 GLN B CB  1 
ATOM   2202 C  CG  . GLN B 1 153 ? -7.159  14.858  26.833  1.00 40.74 ? 153 GLN B CG  1 
ATOM   2203 C  CD  . GLN B 1 153 ? -8.477  15.305  26.220  1.00 41.01 ? 153 GLN B CD  1 
ATOM   2204 O  OE1 . GLN B 1 153 ? -9.528  15.215  26.853  1.00 44.59 ? 153 GLN B OE1 1 
ATOM   2205 N  NE2 . GLN B 1 153 ? -8.426  15.782  24.988  1.00 43.44 ? 153 GLN B NE2 1 
ATOM   2206 O  OXT . GLN B 1 153 ? -5.648  14.709  30.225  1.00 42.33 ? 153 GLN B OXT 1 
ATOM   2207 N  N   . ALA C 1 1   ? 16.116  -3.428  33.277  1.00 40.76 ? 1   ALA C N   1 
ATOM   2208 C  CA  . ALA C 1 1   ? 17.165  -2.368  33.334  1.00 40.22 ? 1   ALA C CA  1 
ATOM   2209 C  C   . ALA C 1 1   ? 17.509  -1.845  31.937  1.00 40.31 ? 1   ALA C C   1 
ATOM   2210 O  O   . ALA C 1 1   ? 17.525  -2.607  30.970  1.00 41.25 ? 1   ALA C O   1 
ATOM   2211 C  CB  . ALA C 1 1   ? 18.421  -2.900  34.028  1.00 40.58 ? 1   ALA C CB  1 
ATOM   2212 N  N   . THR C 1 2   ? 17.756  -0.541  31.840  1.00 39.31 ? 2   THR C N   1 
ATOM   2213 C  CA  . THR C 1 2   ? 18.156  0.100   30.598  1.00 38.69 ? 2   THR C CA  1 
ATOM   2214 C  C   . THR C 1 2   ? 19.631  0.432   30.729  1.00 37.73 ? 2   THR C C   1 
ATOM   2215 O  O   . THR C 1 2   ? 20.091  0.765   31.821  1.00 37.10 ? 2   THR C O   1 
ATOM   2216 C  CB  . THR C 1 2   ? 17.344  1.386   30.360  1.00 38.87 ? 2   THR C CB  1 
ATOM   2217 O  OG1 . THR C 1 2   ? 15.944  1.079   30.407  1.00 40.09 ? 2   THR C OG1 1 
ATOM   2218 C  CG2 . THR C 1 2   ? 17.659  2.003   29.019  1.00 39.63 ? 2   THR C CG2 1 
ATOM   2219 N  N   . LYS C 1 3   ? 20.359  0.313   29.624  1.00 36.95 ? 3   LYS C N   1 
ATOM   2220 C  CA  . LYS C 1 3   ? 21.806  0.516   29.601  1.00 36.93 ? 3   LYS C CA  1 
ATOM   2221 C  C   . LYS C 1 3   ? 22.230  1.382   28.430  1.00 36.20 ? 3   LYS C C   1 
ATOM   2222 O  O   . LYS C 1 3   ? 21.625  1.342   27.356  1.00 35.10 ? 3   LYS C O   1 
ATOM   2223 C  CB  . LYS C 1 3   ? 22.534  -0.826  29.515  1.00 36.72 ? 3   LYS C CB  1 
ATOM   2224 C  CG  . LYS C 1 3   ? 22.240  -1.747  30.677  1.00 38.69 ? 3   LYS C CG  1 
ATOM   2225 C  CD  . LYS C 1 3   ? 23.022  -3.038  30.589  1.00 38.81 ? 3   LYS C CD  1 
ATOM   2226 C  CE  . LYS C 1 3   ? 24.510  -2.799  30.763  1.00 40.23 ? 3   LYS C CE  1 
ATOM   2227 N  NZ  . LYS C 1 3   ? 25.210  -4.070  31.107  1.00 41.99 ? 3   LYS C NZ  1 
ATOM   2228 N  N   . ALA C 1 4   ? 23.273  2.171   28.653  1.00 35.84 ? 4   ALA C N   1 
ATOM   2229 C  CA  . ALA C 1 4   ? 23.869  2.978   27.606  1.00 35.59 ? 4   ALA C CA  1 
ATOM   2230 C  C   . ALA C 1 4   ? 25.385  2.999   27.774  1.00 35.36 ? 4   ALA C C   1 
ATOM   2231 O  O   . ALA C 1 4   ? 25.918  2.546   28.788  1.00 34.56 ? 4   ALA C O   1 
ATOM   2232 C  CB  . ALA C 1 4   ? 23.324  4.374   27.662  1.00 35.45 ? 4   ALA C CB  1 
ATOM   2233 N  N   . VAL C 1 5   ? 26.064  3.528   26.770  1.00 34.79 ? 5   VAL C N   1 
ATOM   2234 C  CA  . VAL C 1 5   ? 27.513  3.650   26.810  1.00 35.20 ? 5   VAL C CA  1 
ATOM   2235 C  C   . VAL C 1 5   ? 27.967  4.838   25.949  1.00 35.27 ? 5   VAL C C   1 
ATOM   2236 O  O   . VAL C 1 5   ? 27.320  5.200   24.953  1.00 35.20 ? 5   VAL C O   1 
ATOM   2237 C  CB  . VAL C 1 5   ? 28.187  2.344   26.344  1.00 35.36 ? 5   VAL C CB  1 
ATOM   2238 C  CG1 . VAL C 1 5   ? 27.855  2.045   24.879  1.00 35.39 ? 5   VAL C CG1 1 
ATOM   2239 C  CG2 . VAL C 1 5   ? 29.708  2.380   26.568  1.00 35.14 ? 5   VAL C CG2 1 
ATOM   2240 N  N   . ALA C 1 6   ? 29.067  5.466   26.364  1.00 35.38 ? 6   ALA C N   1 
ATOM   2241 C  CA  . ALA C 1 6   ? 29.727  6.486   25.572  1.00 35.41 ? 6   ALA C CA  1 
ATOM   2242 C  C   . ALA C 1 6   ? 31.220  6.207   25.490  1.00 35.64 ? 6   ALA C C   1 
ATOM   2243 O  O   . ALA C 1 6   ? 31.878  5.976   26.509  1.00 35.98 ? 6   ALA C O   1 
ATOM   2244 C  CB  . ALA C 1 6   ? 29.491  7.850   26.169  1.00 35.48 ? 6   ALA C CB  1 
ATOM   2245 N  N   . VAL C 1 7   ? 31.743  6.235   24.274  1.00 35.99 ? 7   VAL C N   1 
ATOM   2246 C  CA  . VAL C 1 7   ? 33.172  6.077   24.037  1.00 36.03 ? 7   VAL C CA  1 
ATOM   2247 C  C   . VAL C 1 7   ? 33.715  7.466   23.832  1.00 36.60 ? 7   VAL C C   1 
ATOM   2248 O  O   . VAL C 1 7   ? 33.319  8.148   22.893  1.00 36.38 ? 7   VAL C O   1 
ATOM   2249 C  CB  . VAL C 1 7   ? 33.460  5.195   22.822  1.00 36.60 ? 7   VAL C CB  1 
ATOM   2250 C  CG1 . VAL C 1 7   ? 34.962  5.122   22.533  1.00 36.18 ? 7   VAL C CG1 1 
ATOM   2251 C  CG2 . VAL C 1 7   ? 32.925  3.817   23.077  1.00 36.30 ? 7   VAL C CG2 1 
ATOM   2252 N  N   . LEU C 1 8   ? 34.634  7.869   24.708  1.00 36.54 ? 8   LEU C N   1 
ATOM   2253 C  CA  . LEU C 1 8   ? 35.152  9.231   24.714  1.00 36.74 ? 8   LEU C CA  1 
ATOM   2254 C  C   . LEU C 1 8   ? 36.426  9.337   23.879  1.00 36.81 ? 8   LEU C C   1 
ATOM   2255 O  O   . LEU C 1 8   ? 37.354  8.536   24.044  1.00 36.55 ? 8   LEU C O   1 
ATOM   2256 C  CB  . LEU C 1 8   ? 35.435  9.687   26.148  1.00 36.98 ? 8   LEU C CB  1 
ATOM   2257 C  CG  . LEU C 1 8   ? 34.237  9.679   27.108  1.00 38.02 ? 8   LEU C CG  1 
ATOM   2258 C  CD1 . LEU C 1 8   ? 34.699  9.941   28.531  1.00 40.00 ? 8   LEU C CD1 1 
ATOM   2259 C  CD2 . LEU C 1 8   ? 33.194  10.694  26.672  1.00 40.76 ? 8   LEU C CD2 1 
ATOM   2260 N  N   . LYS C 1 9   ? 36.445  10.316  22.976  1.00 36.91 ? 9   LYS C N   1 
ATOM   2261 C  CA  . LYS C 1 9   ? 37.597  10.610  22.127  1.00 37.47 ? 9   LYS C CA  1 
ATOM   2262 C  C   . LYS C 1 9   ? 37.647  12.107  21.861  1.00 37.21 ? 9   LYS C C   1 
ATOM   2263 O  O   . LYS C 1 9   ? 36.628  12.786  21.912  1.00 36.98 ? 9   LYS C O   1 
ATOM   2264 C  CB  . LYS C 1 9   ? 37.512  9.851   20.791  1.00 37.81 ? 9   LYS C CB  1 
ATOM   2265 C  CG  . LYS C 1 9   ? 37.644  8.343   20.941  1.00 39.63 ? 9   LYS C CG  1 
ATOM   2266 C  CD  . LYS C 1 9   ? 37.569  7.613   19.616  1.00 40.56 ? 9   LYS C CD  1 
ATOM   2267 C  CE  . LYS C 1 9   ? 37.519  6.093   19.815  1.00 41.39 ? 9   LYS C CE  1 
ATOM   2268 N  NZ  . LYS C 1 9   ? 37.191  5.385   18.536  1.00 44.05 ? 9   LYS C NZ  1 
ATOM   2269 N  N   . GLY C 1 10  ? 38.840  12.617  21.576  1.00 37.22 ? 10  GLY C N   1 
ATOM   2270 C  CA  . GLY C 1 10  ? 39.006  14.023  21.223  1.00 37.45 ? 10  GLY C CA  1 
ATOM   2271 C  C   . GLY C 1 10  ? 40.251  14.242  20.388  1.00 37.64 ? 10  GLY C C   1 
ATOM   2272 O  O   . GLY C 1 10  ? 40.784  13.307  19.794  1.00 37.87 ? 10  GLY C O   1 
ATOM   2273 N  N   . ASP C 1 11  ? 40.709  15.487  20.351  1.00 38.01 ? 11  ASP C N   1 
ATOM   2274 C  CA  . ASP C 1 11  ? 41.878  15.874  19.560  1.00 38.26 ? 11  ASP C CA  1 
ATOM   2275 C  C   . ASP C 1 11  ? 43.215  15.537  20.229  1.00 37.75 ? 11  ASP C C   1 
ATOM   2276 O  O   . ASP C 1 11  ? 44.271  15.569  19.578  1.00 37.72 ? 11  ASP C O   1 
ATOM   2277 C  CB  . ASP C 1 11  ? 41.827  17.374  19.287  1.00 38.69 ? 11  ASP C CB  1 
ATOM   2278 C  CG  . ASP C 1 11  ? 40.688  17.763  18.367  1.00 40.88 ? 11  ASP C CG  1 
ATOM   2279 O  OD1 . ASP C 1 11  ? 40.212  16.903  17.589  1.00 43.78 ? 11  ASP C OD1 1 
ATOM   2280 O  OD2 . ASP C 1 11  ? 40.281  18.947  18.414  1.00 41.41 ? 11  ASP C OD2 1 
ATOM   2281 N  N   . GLY C 1 12  ? 43.166  15.251  21.524  1.00 37.19 ? 12  GLY C N   1 
ATOM   2282 C  CA  . GLY C 1 12  ? 44.344  14.899  22.304  1.00 37.05 ? 12  GLY C CA  1 
ATOM   2283 C  C   . GLY C 1 12  ? 44.341  13.434  22.712  1.00 36.69 ? 12  GLY C C   1 
ATOM   2284 O  O   . GLY C 1 12  ? 43.682  12.608  22.071  1.00 36.24 ? 12  GLY C O   1 
ATOM   2285 N  N   . PRO C 1 13  ? 45.090  13.100  23.777  1.00 36.28 ? 13  PRO C N   1 
ATOM   2286 C  CA  . PRO C 1 13  ? 45.223  11.722  24.247  1.00 36.25 ? 13  PRO C CA  1 
ATOM   2287 C  C   . PRO C 1 13  ? 44.085  11.221  25.138  1.00 36.13 ? 13  PRO C C   1 
ATOM   2288 O  O   . PRO C 1 13  ? 44.107  10.062  25.554  1.00 36.43 ? 13  PRO C O   1 
ATOM   2289 C  CB  . PRO C 1 13  ? 46.515  11.776  25.056  1.00 36.11 ? 13  PRO C CB  1 
ATOM   2290 C  CG  . PRO C 1 13  ? 46.495  13.139  25.650  1.00 36.08 ? 13  PRO C CG  1 
ATOM   2291 C  CD  . PRO C 1 13  ? 45.898  14.028  24.595  1.00 36.31 ? 13  PRO C CD  1 
ATOM   2292 N  N   . VAL C 1 14  ? 43.109  12.069  25.441  1.00 35.79 ? 14  VAL C N   1 
ATOM   2293 C  CA  . VAL C 1 14  ? 42.061  11.681  26.383  1.00 36.19 ? 14  VAL C CA  1 
ATOM   2294 C  C   . VAL C 1 14  ? 41.119  10.679  25.726  1.00 36.62 ? 14  VAL C C   1 
ATOM   2295 O  O   . VAL C 1 14  ? 40.572  10.940  24.660  1.00 36.14 ? 14  VAL C O   1 
ATOM   2296 C  CB  . VAL C 1 14  ? 41.278  12.887  26.916  1.00 35.82 ? 14  VAL C CB  1 
ATOM   2297 C  CG1 . VAL C 1 14  ? 40.135  12.421  27.829  1.00 36.20 ? 14  VAL C CG1 1 
ATOM   2298 C  CG2 . VAL C 1 14  ? 42.198  13.819  27.679  1.00 36.32 ? 14  VAL C CG2 1 
ATOM   2299 N  N   . GLN C 1 15  ? 40.969  9.518   26.354  1.00 36.88 ? 15  GLN C N   1 
ATOM   2300 C  CA  . GLN C 1 15  ? 40.040  8.520   25.863  1.00 37.52 ? 15  GLN C CA  1 
ATOM   2301 C  C   . GLN C 1 15  ? 39.535  7.613   26.971  1.00 36.80 ? 15  GLN C C   1 
ATOM   2302 O  O   . GLN C 1 15  ? 40.211  7.379   27.965  1.00 36.90 ? 15  GLN C O   1 
ATOM   2303 C  CB  . GLN C 1 15  ? 40.676  7.703   24.746  1.00 37.92 ? 15  GLN C CB  1 
ATOM   2304 C  CG  . GLN C 1 15  ? 41.811  6.806   25.155  1.00 39.90 ? 15  GLN C CG  1 
ATOM   2305 C  CD  . GLN C 1 15  ? 42.357  6.038   23.969  1.00 40.24 ? 15  GLN C CD  1 
ATOM   2306 O  OE1 . GLN C 1 15  ? 42.861  6.625   23.012  1.00 46.33 ? 15  GLN C OE1 1 
ATOM   2307 N  NE2 . GLN C 1 15  ? 42.243  4.718   24.018  1.00 44.35 ? 15  GLN C NE2 1 
ATOM   2308 N  N   . GLY C 1 16  ? 38.323  7.109   26.795  1.00 36.52 ? 16  GLY C N   1 
ATOM   2309 C  CA  . GLY C 1 16  ? 37.735  6.264   27.808  1.00 36.07 ? 16  GLY C CA  1 
ATOM   2310 C  C   . GLY C 1 16  ? 36.398  5.715   27.393  1.00 35.82 ? 16  GLY C C   1 
ATOM   2311 O  O   . GLY C 1 16  ? 35.892  6.023   26.307  1.00 35.97 ? 16  GLY C O   1 
ATOM   2312 N  N   . ILE C 1 17  ? 35.851  4.886   28.269  1.00 35.51 ? 17  ILE C N   1 
ATOM   2313 C  CA  . ILE C 1 17  ? 34.546  4.271   28.084  1.00 35.23 ? 17  ILE C CA  1 
ATOM   2314 C  C   . ILE C 1 17  ? 33.749  4.503   29.352  1.00 35.03 ? 17  ILE C C   1 
ATOM   2315 O  O   . ILE C 1 17  ? 34.224  4.186   30.445  1.00 34.27 ? 17  ILE C O   1 
ATOM   2316 C  CB  . ILE C 1 17  ? 34.691  2.752   27.822  1.00 35.15 ? 17  ILE C CB  1 
ATOM   2317 C  CG1 . ILE C 1 17  ? 35.455  2.519   26.516  1.00 35.22 ? 17  ILE C CG1 1 
ATOM   2318 C  CG2 . ILE C 1 17  ? 33.323  2.079   27.790  1.00 35.74 ? 17  ILE C CG2 1 
ATOM   2319 C  CD1 . ILE C 1 17  ? 35.845  1.072   26.257  1.00 35.73 ? 17  ILE C CD1 1 
ATOM   2320 N  N   . ILE C 1 18  ? 32.536  5.038   29.206  1.00 34.80 ? 18  ILE C N   1 
ATOM   2321 C  CA  . ILE C 1 18  ? 31.662  5.301   30.340  1.00 34.55 ? 18  ILE C CA  1 
ATOM   2322 C  C   . ILE C 1 18  ? 30.341  4.584   30.114  1.00 34.29 ? 18  ILE C C   1 
ATOM   2323 O  O   . ILE C 1 18  ? 29.712  4.739   29.057  1.00 35.07 ? 18  ILE C O   1 
ATOM   2324 C  CB  . ILE C 1 18  ? 31.439  6.822   30.568  1.00 34.72 ? 18  ILE C CB  1 
ATOM   2325 C  CG1 . ILE C 1 18  ? 32.781  7.515   30.876  1.00 34.64 ? 18  ILE C CG1 1 
ATOM   2326 C  CG2 . ILE C 1 18  ? 30.432  7.079   31.686  1.00 34.98 ? 18  ILE C CG2 1 
ATOM   2327 C  CD1 . ILE C 1 18  ? 33.407  7.163   32.217  1.00 35.54 ? 18  ILE C CD1 1 
ATOM   2328 N  N   . ASN C 1 19  ? 29.978  3.758   31.096  1.00 34.32 ? 19  ASN C N   1 
ATOM   2329 C  CA  . ASN C 1 19  ? 28.756  2.980   31.079  1.00 34.37 ? 19  ASN C CA  1 
ATOM   2330 C  C   . ASN C 1 19  ? 27.702  3.617   31.948  1.00 34.25 ? 19  ASN C C   1 
ATOM   2331 O  O   . ASN C 1 19  ? 28.022  4.215   32.972  1.00 34.21 ? 19  ASN C O   1 
ATOM   2332 C  CB  . ASN C 1 19  ? 29.034  1.570   31.598  1.00 34.54 ? 19  ASN C CB  1 
ATOM   2333 C  CG  . ASN C 1 19  ? 30.187  0.906   30.883  1.00 35.13 ? 19  ASN C CG  1 
ATOM   2334 O  OD1 . ASN C 1 19  ? 30.035  0.430   29.759  1.00 35.74 ? 19  ASN C OD1 1 
ATOM   2335 N  ND2 . ASN C 1 19  ? 31.346  0.859   31.534  1.00 36.03 ? 19  ASN C ND2 1 
ATOM   2336 N  N   . PHE C 1 20  ? 26.446  3.457   31.534  1.00 34.85 ? 20  PHE C N   1 
ATOM   2337 C  CA  . PHE C 1 20  ? 25.283  3.930   32.272  1.00 35.01 ? 20  PHE C CA  1 
ATOM   2338 C  C   . PHE C 1 20  ? 24.338  2.743   32.455  1.00 35.30 ? 20  PHE C C   1 
ATOM   2339 O  O   . PHE C 1 20  ? 24.125  1.956   31.520  1.00 34.87 ? 20  PHE C O   1 
ATOM   2340 C  CB  . PHE C 1 20  ? 24.519  5.017   31.508  1.00 35.88 ? 20  PHE C CB  1 
ATOM   2341 C  CG  . PHE C 1 20  ? 25.342  6.208   31.111  1.00 35.74 ? 20  PHE C CG  1 
ATOM   2342 C  CD1 . PHE C 1 20  ? 26.214  6.144   30.033  1.00 36.43 ? 20  PHE C CD1 1 
ATOM   2343 C  CD2 . PHE C 1 20  ? 25.205  7.421   31.783  1.00 36.79 ? 20  PHE C CD2 1 
ATOM   2344 C  CE1 . PHE C 1 20  ? 26.948  7.241   29.652  1.00 36.58 ? 20  PHE C CE1 1 
ATOM   2345 C  CE2 . PHE C 1 20  ? 25.946  8.527   31.405  1.00 37.07 ? 20  PHE C CE2 1 
ATOM   2346 C  CZ  . PHE C 1 20  ? 26.820  8.430   30.339  1.00 36.54 ? 20  PHE C CZ  1 
ATOM   2347 N  N   . GLU C 1 21  ? 23.770  2.619   33.647  1.00 35.33 ? 21  GLU C N   1 
ATOM   2348 C  CA  . GLU C 1 21  ? 22.759  1.590   33.900  1.00 35.40 ? 21  GLU C CA  1 
ATOM   2349 C  C   . GLU C 1 21  ? 21.657  2.140   34.797  1.00 35.14 ? 21  GLU C C   1 
ATOM   2350 O  O   . GLU C 1 21  ? 21.928  2.765   35.815  1.00 34.53 ? 21  GLU C O   1 
ATOM   2351 C  CB  . GLU C 1 21  ? 23.387  0.323   34.490  1.00 35.93 ? 21  GLU C CB  1 
ATOM   2352 C  CG  . GLU C 1 21  ? 22.377  -0.759  34.756  1.00 36.33 ? 21  GLU C CG  1 
ATOM   2353 C  CD  . GLU C 1 21  ? 22.932  -2.176  34.666  1.00 37.74 ? 21  GLU C CD  1 
ATOM   2354 O  OE1 . GLU C 1 21  ? 24.099  -2.415  35.053  1.00 41.02 ? 21  GLU C OE1 1 
ATOM   2355 O  OE2 . GLU C 1 21  ? 22.172  -3.059  34.217  1.00 40.69 ? 21  GLU C OE2 1 
ATOM   2356 N  N   . GLN C 1 22  ? 20.410  1.906   34.397  1.00 34.66 ? 22  GLN C N   1 
ATOM   2357 C  CA  . GLN C 1 22  ? 19.248  2.377   35.142  1.00 35.23 ? 22  GLN C CA  1 
ATOM   2358 C  C   . GLN C 1 22  ? 18.270  1.213   35.332  1.00 35.41 ? 22  GLN C C   1 
ATOM   2359 O  O   . GLN C 1 22  ? 17.613  0.783   34.382  1.00 35.82 ? 22  GLN C O   1 
ATOM   2360 C  CB  . GLN C 1 22  ? 18.587  3.542   34.398  1.00 34.69 ? 22  GLN C CB  1 
ATOM   2361 C  CG  . GLN C 1 22  ? 17.490  4.250   35.180  1.00 35.00 ? 22  GLN C CG  1 
ATOM   2362 C  CD  . GLN C 1 22  ? 16.868  5.404   34.419  1.00 35.25 ? 22  GLN C CD  1 
ATOM   2363 O  OE1 . GLN C 1 22  ? 16.965  5.476   33.193  1.00 35.14 ? 22  GLN C OE1 1 
ATOM   2364 N  NE2 . GLN C 1 22  ? 16.214  6.309   35.142  1.00 33.96 ? 22  GLN C NE2 1 
ATOM   2365 N  N   . LYS C 1 23  ? 18.201  0.697   36.559  1.00 35.52 ? 23  LYS C N   1 
ATOM   2366 C  CA  . LYS C 1 23  ? 17.406  -0.498  36.861  1.00 35.80 ? 23  LYS C CA  1 
ATOM   2367 C  C   . LYS C 1 23  ? 15.903  -0.230  36.800  1.00 35.28 ? 23  LYS C C   1 
ATOM   2368 O  O   . LYS C 1 23  ? 15.136  -1.069  36.329  1.00 35.23 ? 23  LYS C O   1 
ATOM   2369 C  CB  . LYS C 1 23  ? 17.792  -1.069  38.229  1.00 36.41 ? 23  LYS C CB  1 
ATOM   2370 C  CG  . LYS C 1 23  ? 19.208  -1.641  38.263  1.00 37.63 ? 23  LYS C CG  1 
ATOM   2371 C  CD  . LYS C 1 23  ? 19.549  -2.247  39.612  1.00 37.79 ? 23  LYS C CD  1 
ATOM   2372 C  CE  . LYS C 1 23  ? 20.945  -2.875  39.603  1.00 39.04 ? 23  LYS C CE  1 
ATOM   2373 N  NZ  . LYS C 1 23  ? 21.329  -3.406  40.947  1.00 39.92 ? 23  LYS C NZ  1 
ATOM   2374 N  N   . GLU C 1 24  ? 15.494  0.939   37.286  1.00 34.91 ? 24  GLU C N   1 
ATOM   2375 C  CA  . GLU C 1 24  ? 14.086  1.349   37.281  1.00 34.71 ? 24  GLU C CA  1 
ATOM   2376 C  C   . GLU C 1 24  ? 13.962  2.644   36.498  1.00 33.62 ? 24  GLU C C   1 
ATOM   2377 O  O   . GLU C 1 24  ? 14.784  3.551   36.660  1.00 32.87 ? 24  GLU C O   1 
ATOM   2378 C  CB  . GLU C 1 24  ? 13.576  1.563   38.715  1.00 35.23 ? 24  GLU C CB  1 
ATOM   2379 C  CG  . GLU C 1 24  ? 12.741  0.446   39.274  1.00 38.46 ? 24  GLU C CG  1 
ATOM   2380 C  CD  . GLU C 1 24  ? 13.448  -0.886  39.334  1.00 40.88 ? 24  GLU C CD  1 
ATOM   2381 O  OE1 . GLU C 1 24  ? 14.611  -0.923  39.784  1.00 43.91 ? 24  GLU C OE1 1 
ATOM   2382 O  OE2 . GLU C 1 24  ? 12.821  -1.902  38.956  1.00 41.69 ? 24  GLU C OE2 1 
ATOM   2383 N  N   . SER C 1 25  ? 12.927  2.739   35.667  1.00 32.85 ? 25  SER C N   1 
ATOM   2384 C  CA  . SER C 1 25  ? 12.729  3.918   34.827  1.00 32.80 ? 25  SER C CA  1 
ATOM   2385 C  C   . SER C 1 25  ? 12.585  5.204   35.640  1.00 32.51 ? 25  SER C C   1 
ATOM   2386 O  O   . SER C 1 25  ? 12.928  6.276   35.151  1.00 32.27 ? 25  SER C O   1 
ATOM   2387 C  CB  . SER C 1 25  ? 11.524  3.738   33.895  1.00 32.59 ? 25  SER C CB  1 
ATOM   2388 O  OG  . SER C 1 25  ? 10.326  3.555   34.617  1.00 32.66 ? 25  SER C OG  1 
ATOM   2389 N  N   . ASN C 1 26  ? 12.104  5.097   36.882  1.00 32.66 ? 26  ASN C N   1 
ATOM   2390 C  CA  . ASN C 1 26  ? 12.021  6.256   37.782  1.00 32.62 ? 26  ASN C CA  1 
ATOM   2391 C  C   . ASN C 1 26  ? 13.069  6.218   38.889  1.00 33.14 ? 26  ASN C C   1 
ATOM   2392 O  O   . ASN C 1 26  ? 12.908  6.850   39.929  1.00 33.81 ? 26  ASN C O   1 
ATOM   2393 C  CB  . ASN C 1 26  ? 10.607  6.406   38.380  1.00 32.60 ? 26  ASN C CB  1 
ATOM   2394 C  CG  . ASN C 1 26  ? 10.236  5.272   39.314  1.00 31.58 ? 26  ASN C CG  1 
ATOM   2395 O  OD1 . ASN C 1 26  ? 10.725  4.157   39.170  1.00 30.54 ? 26  ASN C OD1 1 
ATOM   2396 N  ND2 . ASN C 1 26  ? 9.370   5.557   40.283  1.00 31.10 ? 26  ASN C ND2 1 
ATOM   2397 N  N   . GLY C 1 27  ? 14.139  5.471   38.657  1.00 33.49 ? 27  GLY C N   1 
ATOM   2398 C  CA  . GLY C 1 27  ? 15.206  5.322   39.629  1.00 33.57 ? 27  GLY C CA  1 
ATOM   2399 C  C   . GLY C 1 27  ? 16.515  5.926   39.149  1.00 33.75 ? 27  GLY C C   1 
ATOM   2400 O  O   . GLY C 1 27  ? 16.602  6.466   38.036  1.00 33.77 ? 27  GLY C O   1 
ATOM   2401 N  N   . PRO C 1 28  ? 17.553  5.833   39.995  1.00 34.30 ? 28  PRO C N   1 
ATOM   2402 C  CA  . PRO C 1 28  ? 18.839  6.435   39.690  1.00 34.51 ? 28  PRO C CA  1 
ATOM   2403 C  C   . PRO C 1 28  ? 19.576  5.730   38.556  1.00 34.88 ? 28  PRO C C   1 
ATOM   2404 O  O   . PRO C 1 28  ? 19.307  4.559   38.262  1.00 34.28 ? 28  PRO C O   1 
ATOM   2405 C  CB  . PRO C 1 28  ? 19.620  6.300   41.000  1.00 34.56 ? 28  PRO C CB  1 
ATOM   2406 C  CG  . PRO C 1 28  ? 18.967  5.208   41.730  1.00 34.80 ? 28  PRO C CG  1 
ATOM   2407 C  CD  . PRO C 1 28  ? 17.552  5.145   41.297  1.00 34.36 ? 28  PRO C CD  1 
ATOM   2408 N  N   . VAL C 1 29  ? 20.483  6.480   37.935  1.00 35.13 ? 29  VAL C N   1 
ATOM   2409 C  CA  . VAL C 1 29  ? 21.355  5.981   36.891  1.00 35.72 ? 29  VAL C CA  1 
ATOM   2410 C  C   . VAL C 1 29  ? 22.758  5.856   37.474  1.00 36.05 ? 29  VAL C C   1 
ATOM   2411 O  O   . VAL C 1 29  ? 23.308  6.831   37.982  1.00 36.35 ? 29  VAL C O   1 
ATOM   2412 C  CB  . VAL C 1 29  ? 21.425  6.940   35.682  1.00 36.15 ? 29  VAL C CB  1 
ATOM   2413 C  CG1 . VAL C 1 29  ? 22.324  6.355   34.599  1.00 36.33 ? 29  VAL C CG1 1 
ATOM   2414 C  CG2 . VAL C 1 29  ? 20.026  7.249   35.125  1.00 36.44 ? 29  VAL C CG2 1 
ATOM   2415 N  N   . LYS C 1 30  ? 23.322  4.656   37.402  1.00 36.27 ? 30  LYS C N   1 
ATOM   2416 C  CA  . LYS C 1 30  ? 24.714  4.428   37.793  1.00 36.45 ? 30  LYS C CA  1 
ATOM   2417 C  C   . LYS C 1 30  ? 25.605  4.702   36.596  1.00 36.39 ? 30  LYS C C   1 
ATOM   2418 O  O   . LYS C 1 30  ? 25.306  4.270   35.470  1.00 35.53 ? 30  LYS C O   1 
ATOM   2419 C  CB  . LYS C 1 30  ? 24.906  2.990   38.271  1.00 36.72 ? 30  LYS C CB  1 
ATOM   2420 C  CG  . LYS C 1 30  ? 24.169  2.665   39.547  1.00 38.22 ? 30  LYS C CG  1 
ATOM   2421 C  CD  . LYS C 1 30  ? 24.232  1.171   39.846  1.00 38.45 ? 30  LYS C CD  1 
ATOM   2422 C  CE  . LYS C 1 30  ? 23.859  0.857   41.280  1.00 38.88 ? 30  LYS C CE  1 
ATOM   2423 N  NZ  . LYS C 1 30  ? 23.838  -0.613  41.540  1.00 40.36 ? 30  LYS C NZ  1 
ATOM   2424 N  N   . VAL C 1 31  ? 26.686  5.441   36.840  1.00 35.99 ? 31  VAL C N   1 
ATOM   2425 C  CA  . VAL C 1 31  ? 27.605  5.860   35.803  1.00 36.28 ? 31  VAL C CA  1 
ATOM   2426 C  C   . VAL C 1 31  ? 28.977  5.391   36.238  1.00 36.13 ? 31  VAL C C   1 
ATOM   2427 O  O   . VAL C 1 31  ? 29.427  5.724   37.335  1.00 35.96 ? 31  VAL C O   1 
ATOM   2428 C  CB  . VAL C 1 31  ? 27.603  7.409   35.626  1.00 36.36 ? 31  VAL C CB  1 
ATOM   2429 C  CG1 . VAL C 1 31  ? 28.522  7.841   34.487  1.00 36.77 ? 31  VAL C CG1 1 
ATOM   2430 C  CG2 . VAL C 1 31  ? 26.182  7.936   35.397  1.00 36.84 ? 31  VAL C CG2 1 
ATOM   2431 N  N   . TRP C 1 32  ? 29.639  4.595   35.406  1.00 36.12 ? 32  TRP C N   1 
ATOM   2432 C  CA  . TRP C 1 32  ? 30.968  4.098   35.770  1.00 36.08 ? 32  TRP C CA  1 
ATOM   2433 C  C   . TRP C 1 32  ? 31.814  3.765   34.551  1.00 35.58 ? 32  TRP C C   1 
ATOM   2434 O  O   . TRP C 1 32  ? 31.302  3.490   33.468  1.00 35.11 ? 32  TRP C O   1 
ATOM   2435 C  CB  . TRP C 1 32  ? 30.860  2.863   36.672  1.00 36.82 ? 32  TRP C CB  1 
ATOM   2436 C  CG  . TRP C 1 32  ? 30.544  1.592   35.936  1.00 37.63 ? 32  TRP C CG  1 
ATOM   2437 C  CD1 . TRP C 1 32  ? 31.425  0.618   35.564  1.00 38.51 ? 32  TRP C CD1 1 
ATOM   2438 C  CD2 . TRP C 1 32  ? 29.256  1.166   35.476  1.00 37.69 ? 32  TRP C CD2 1 
ATOM   2439 N  NE1 . TRP C 1 32  ? 30.768  -0.383  34.893  1.00 38.64 ? 32  TRP C NE1 1 
ATOM   2440 C  CE2 . TRP C 1 32  ? 29.434  -0.076  34.832  1.00 38.18 ? 32  TRP C CE2 1 
ATOM   2441 C  CE3 . TRP C 1 32  ? 27.974  1.709   35.554  1.00 38.61 ? 32  TRP C CE3 1 
ATOM   2442 C  CZ2 . TRP C 1 32  ? 28.377  -0.784  34.267  1.00 38.45 ? 32  TRP C CZ2 1 
ATOM   2443 C  CZ3 . TRP C 1 32  ? 26.915  1.012   34.977  1.00 38.67 ? 32  TRP C CZ3 1 
ATOM   2444 C  CH2 . TRP C 1 32  ? 27.126  -0.227  34.347  1.00 38.88 ? 32  TRP C CH2 1 
ATOM   2445 N  N   . GLY C 1 33  ? 33.122  3.785   34.755  1.00 35.22 ? 33  GLY C N   1 
ATOM   2446 C  CA  . GLY C 1 33  ? 34.062  3.415   33.721  1.00 35.59 ? 33  GLY C CA  1 
ATOM   2447 C  C   . GLY C 1 33  ? 35.417  4.001   34.021  1.00 35.68 ? 33  GLY C C   1 
ATOM   2448 O  O   . GLY C 1 33  ? 35.727  4.301   35.171  1.00 35.25 ? 33  GLY C O   1 
ATOM   2449 N  N   . SER C 1 34  ? 36.227  4.149   32.984  1.00 36.21 ? 34  SER C N   1 
ATOM   2450 C  CA  . SER C 1 34  ? 37.573  4.691   33.131  1.00 36.22 ? 34  SER C CA  1 
ATOM   2451 C  C   . SER C 1 34  ? 37.908  5.617   31.970  1.00 36.54 ? 34  SER C C   1 
ATOM   2452 O  O   . SER C 1 34  ? 37.452  5.411   30.837  1.00 36.86 ? 34  SER C O   1 
ATOM   2453 C  CB  . SER C 1 34  ? 38.594  3.565   33.201  1.00 36.56 ? 34  SER C CB  1 
ATOM   2454 O  OG  . SER C 1 34  ? 39.846  4.045   33.680  1.00 37.43 ? 34  SER C OG  1 
ATOM   2455 N  N   . ILE C 1 35  ? 38.700  6.640   32.268  1.00 35.95 ? 35  ILE C N   1 
ATOM   2456 C  CA  . ILE C 1 35  ? 39.155  7.606   31.275  1.00 35.81 ? 35  ILE C CA  1 
ATOM   2457 C  C   . ILE C 1 35  ? 40.644  7.777   31.498  1.00 35.63 ? 35  ILE C C   1 
ATOM   2458 O  O   . ILE C 1 35  ? 41.086  7.910   32.641  1.00 35.05 ? 35  ILE C O   1 
ATOM   2459 C  CB  . ILE C 1 35  ? 38.485  8.993   31.464  1.00 35.82 ? 35  ILE C CB  1 
ATOM   2460 C  CG1 . ILE C 1 35  ? 36.962  8.885   31.524  1.00 36.16 ? 35  ILE C CG1 1 
ATOM   2461 C  CG2 . ILE C 1 35  ? 38.896  9.954   30.362  1.00 35.65 ? 35  ILE C CG2 1 
ATOM   2462 C  CD1 . ILE C 1 35  ? 36.292  10.158  32.007  1.00 36.43 ? 35  ILE C CD1 1 
ATOM   2463 N  N   . LYS C 1 36  ? 41.418  7.775   30.419  1.00 35.55 ? 36  LYS C N   1 
ATOM   2464 C  CA  . LYS C 1 36  ? 42.860  7.954   30.532  1.00 35.62 ? 36  LYS C CA  1 
ATOM   2465 C  C   . LYS C 1 36  ? 43.360  9.126   29.690  1.00 35.35 ? 36  LYS C C   1 
ATOM   2466 O  O   . LYS C 1 36  ? 42.605  9.729   28.921  1.00 34.80 ? 36  LYS C O   1 
ATOM   2467 C  CB  . LYS C 1 36  ? 43.595  6.658   30.177  1.00 36.00 ? 36  LYS C CB  1 
ATOM   2468 C  CG  . LYS C 1 36  ? 43.544  6.248   28.722  1.00 36.52 ? 36  LYS C CG  1 
ATOM   2469 C  CD  . LYS C 1 36  ? 44.147  4.856   28.556  1.00 36.90 ? 36  LYS C CD  1 
ATOM   2470 C  CE  . LYS C 1 36  ? 44.348  4.497   27.097  1.00 37.95 ? 36  LYS C CE  1 
ATOM   2471 N  NZ  . LYS C 1 36  ? 44.835  3.097   26.935  1.00 38.84 ? 36  LYS C NZ  1 
ATOM   2472 N  N   . GLY C 1 37  ? 44.640  9.453   29.863  1.00 34.86 ? 37  GLY C N   1 
ATOM   2473 C  CA  . GLY C 1 37  ? 45.260  10.562  29.141  1.00 35.06 ? 37  GLY C CA  1 
ATOM   2474 C  C   . GLY C 1 37  ? 44.970  11.928  29.740  1.00 34.93 ? 37  GLY C C   1 
ATOM   2475 O  O   . GLY C 1 37  ? 45.203  12.955  29.095  1.00 34.73 ? 37  GLY C O   1 
ATOM   2476 N  N   . LEU C 1 38  ? 44.476  11.942  30.980  1.00 35.14 ? 38  LEU C N   1 
ATOM   2477 C  CA  . LEU C 1 38  ? 44.128  13.184  31.667  1.00 34.90 ? 38  LEU C CA  1 
ATOM   2478 C  C   . LEU C 1 38  ? 45.290  13.688  32.511  1.00 34.77 ? 38  LEU C C   1 
ATOM   2479 O  O   . LEU C 1 38  ? 46.108  12.907  32.990  1.00 34.92 ? 38  LEU C O   1 
ATOM   2480 C  CB  . LEU C 1 38  ? 42.923  12.967  32.582  1.00 34.78 ? 38  LEU C CB  1 
ATOM   2481 C  CG  . LEU C 1 38  ? 41.585  12.694  31.897  1.00 34.81 ? 38  LEU C CG  1 
ATOM   2482 C  CD1 . LEU C 1 38  ? 40.594  12.079  32.873  1.00 35.73 ? 38  LEU C CD1 1 
ATOM   2483 C  CD2 . LEU C 1 38  ? 41.019  13.965  31.277  1.00 34.62 ? 38  LEU C CD2 1 
ATOM   2484 N  N   . THR C 1 39  ? 45.348  15.000  32.707  1.00 34.57 ? 39  THR C N   1 
ATOM   2485 C  CA  . THR C 1 39  ? 46.217  15.568  33.733  1.00 35.03 ? 39  THR C CA  1 
ATOM   2486 C  C   . THR C 1 39  ? 45.647  15.222  35.113  1.00 35.01 ? 39  THR C C   1 
ATOM   2487 O  O   . THR C 1 39  ? 44.429  15.140  35.285  1.00 34.76 ? 39  THR C O   1 
ATOM   2488 C  CB  . THR C 1 39  ? 46.333  17.097  33.603  1.00 34.94 ? 39  THR C CB  1 
ATOM   2489 O  OG1 . THR C 1 39  ? 45.036  17.694  33.738  1.00 36.32 ? 39  THR C OG1 1 
ATOM   2490 C  CG2 . THR C 1 39  ? 46.899  17.460  32.262  1.00 35.23 ? 39  THR C CG2 1 
ATOM   2491 N  N   . GLU C 1 40  ? 46.541  15.020  36.079  1.00 35.22 ? 40  GLU C N   1 
ATOM   2492 C  CA  . GLU C 1 40  ? 46.160  14.717  37.460  1.00 35.12 ? 40  GLU C CA  1 
ATOM   2493 C  C   . GLU C 1 40  ? 45.216  15.789  38.000  1.00 34.88 ? 40  GLU C C   1 
ATOM   2494 O  O   . GLU C 1 40  ? 45.462  16.979  37.819  1.00 34.99 ? 40  GLU C O   1 
ATOM   2495 C  CB  . GLU C 1 40  ? 47.412  14.637  38.335  1.00 35.49 ? 40  GLU C CB  1 
ATOM   2496 C  CG  . GLU C 1 40  ? 47.174  14.157  39.759  1.00 35.54 ? 40  GLU C CG  1 
ATOM   2497 C  CD  . GLU C 1 40  ? 48.457  13.989  40.545  1.00 36.04 ? 40  GLU C CD  1 
ATOM   2498 O  OE1 . GLU C 1 40  ? 49.547  14.296  40.009  1.00 36.63 ? 40  GLU C OE1 1 
ATOM   2499 O  OE2 . GLU C 1 40  ? 48.378  13.554  41.713  1.00 37.52 ? 40  GLU C OE2 1 
ATOM   2500 N  N   . GLY C 1 41  ? 44.129  15.362  38.636  1.00 34.50 ? 41  GLY C N   1 
ATOM   2501 C  CA  . GLY C 1 41  ? 43.191  16.281  39.271  1.00 34.22 ? 41  GLY C CA  1 
ATOM   2502 C  C   . GLY C 1 41  ? 41.774  16.190  38.750  1.00 33.84 ? 41  GLY C C   1 
ATOM   2503 O  O   . GLY C 1 41  ? 41.415  15.244  38.048  1.00 33.62 ? 41  GLY C O   1 
ATOM   2504 N  N   . LEU C 1 42  ? 40.976  17.196  39.093  1.00 33.69 ? 42  LEU C N   1 
ATOM   2505 C  CA  . LEU C 1 42  ? 39.543  17.209  38.779  1.00 33.88 ? 42  LEU C CA  1 
ATOM   2506 C  C   . LEU C 1 42  ? 39.286  17.717  37.367  1.00 33.74 ? 42  LEU C C   1 
ATOM   2507 O  O   . LEU C 1 42  ? 39.941  18.656  36.907  1.00 33.54 ? 42  LEU C O   1 
ATOM   2508 C  CB  . LEU C 1 42  ? 38.800  18.110  39.768  1.00 34.29 ? 42  LEU C CB  1 
ATOM   2509 C  CG  . LEU C 1 42  ? 38.778  17.696  41.239  1.00 34.69 ? 42  LEU C CG  1 
ATOM   2510 C  CD1 . LEU C 1 42  ? 38.328  18.868  42.109  1.00 36.09 ? 42  LEU C CD1 1 
ATOM   2511 C  CD2 . LEU C 1 42  ? 37.882  16.496  41.461  1.00 35.84 ? 42  LEU C CD2 1 
ATOM   2512 N  N   . HIS C 1 43  ? 38.321  17.095  36.694  1.00 33.61 ? 43  HIS C N   1 
ATOM   2513 C  CA  . HIS C 1 43  ? 37.898  17.497  35.356  1.00 33.82 ? 43  HIS C CA  1 
ATOM   2514 C  C   . HIS C 1 43  ? 36.382  17.500  35.291  1.00 33.84 ? 43  HIS C C   1 
ATOM   2515 O  O   . HIS C 1 43  ? 35.765  16.491  35.601  1.00 33.77 ? 43  HIS C O   1 
ATOM   2516 C  CB  . HIS C 1 43  ? 38.447  16.511  34.328  1.00 34.03 ? 43  HIS C CB  1 
ATOM   2517 C  CG  . HIS C 1 43  ? 39.939  16.506  34.258  1.00 34.14 ? 43  HIS C CG  1 
ATOM   2518 N  ND1 . HIS C 1 43  ? 40.644  17.389  33.470  1.00 35.63 ? 43  HIS C ND1 1 
ATOM   2519 C  CD2 . HIS C 1 43  ? 40.862  15.769  34.921  1.00 34.96 ? 43  HIS C CD2 1 
ATOM   2520 C  CE1 . HIS C 1 43  ? 41.938  17.183  33.636  1.00 34.86 ? 43  HIS C CE1 1 
ATOM   2521 N  NE2 . HIS C 1 43  ? 42.097  16.206  34.512  1.00 35.07 ? 43  HIS C NE2 1 
ATOM   2522 N  N   . GLY C 1 44  ? 35.792  18.626  34.890  1.00 33.72 ? 44  GLY C N   1 
ATOM   2523 C  CA  . GLY C 1 44  ? 34.331  18.713  34.712  1.00 33.86 ? 44  GLY C CA  1 
ATOM   2524 C  C   . GLY C 1 44  ? 33.784  17.580  33.859  1.00 33.84 ? 44  GLY C C   1 
ATOM   2525 O  O   . GLY C 1 44  ? 34.421  17.147  32.895  1.00 33.58 ? 44  GLY C O   1 
ATOM   2526 N  N   . PHE C 1 45  ? 32.585  17.110  34.208  1.00 34.15 ? 45  PHE C N   1 
ATOM   2527 C  CA  . PHE C 1 45  ? 31.994  15.918  33.598  1.00 34.27 ? 45  PHE C CA  1 
ATOM   2528 C  C   . PHE C 1 45  ? 30.518  16.225  33.353  1.00 34.15 ? 45  PHE C C   1 
ATOM   2529 O  O   . PHE C 1 45  ? 29.747  16.348  34.300  1.00 34.54 ? 45  PHE C O   1 
ATOM   2530 C  CB  . PHE C 1 45  ? 32.170  14.747  34.572  1.00 35.02 ? 45  PHE C CB  1 
ATOM   2531 C  CG  . PHE C 1 45  ? 32.039  13.380  33.959  1.00 34.86 ? 45  PHE C CG  1 
ATOM   2532 C  CD1 . PHE C 1 45  ? 32.671  13.057  32.762  1.00 36.39 ? 45  PHE C CD1 1 
ATOM   2533 C  CD2 . PHE C 1 45  ? 31.329  12.386  34.629  1.00 36.19 ? 45  PHE C CD2 1 
ATOM   2534 C  CE1 . PHE C 1 45  ? 32.569  11.784  32.225  1.00 35.83 ? 45  PHE C CE1 1 
ATOM   2535 C  CE2 . PHE C 1 45  ? 31.226  11.105  34.100  1.00 36.02 ? 45  PHE C CE2 1 
ATOM   2536 C  CZ  . PHE C 1 45  ? 31.856  10.804  32.893  1.00 36.62 ? 45  PHE C CZ  1 
ATOM   2537 N  N   . HIS C 1 46  ? 30.143  16.414  32.089  1.00 34.12 ? 46  HIS C N   1 
ATOM   2538 C  CA  . HIS C 1 46  ? 28.832  16.963  31.749  1.00 33.92 ? 46  HIS C CA  1 
ATOM   2539 C  C   . HIS C 1 46  ? 28.189  16.282  30.554  1.00 33.81 ? 46  HIS C C   1 
ATOM   2540 O  O   . HIS C 1 46  ? 28.871  15.919  29.595  1.00 33.87 ? 46  HIS C O   1 
ATOM   2541 C  CB  . HIS C 1 46  ? 28.952  18.459  31.426  1.00 34.31 ? 46  HIS C CB  1 
ATOM   2542 C  CG  . HIS C 1 46  ? 29.291  19.315  32.605  1.00 35.45 ? 46  HIS C CG  1 
ATOM   2543 N  ND1 . HIS C 1 46  ? 28.332  19.848  33.440  1.00 36.14 ? 46  HIS C ND1 1 
ATOM   2544 C  CD2 . HIS C 1 46  ? 30.484  19.741  33.081  1.00 36.06 ? 46  HIS C CD2 1 
ATOM   2545 C  CE1 . HIS C 1 46  ? 28.923  20.560  34.384  1.00 36.37 ? 46  HIS C CE1 1 
ATOM   2546 N  NE2 . HIS C 1 46  ? 30.230  20.504  34.192  1.00 35.42 ? 46  HIS C NE2 1 
ATOM   2547 N  N   . VAL C 1 47  ? 26.871  16.118  30.611  1.00 33.13 ? 47  VAL C N   1 
ATOM   2548 C  CA  . VAL C 1 47  ? 26.107  15.761  29.427  1.00 33.33 ? 47  VAL C CA  1 
ATOM   2549 C  C   . VAL C 1 47  ? 25.748  17.063  28.725  1.00 33.32 ? 47  VAL C C   1 
ATOM   2550 O  O   . VAL C 1 47  ? 25.174  17.991  29.332  1.00 33.70 ? 47  VAL C O   1 
ATOM   2551 C  CB  . VAL C 1 47  ? 24.816  14.976  29.743  1.00 33.44 ? 47  VAL C CB  1 
ATOM   2552 C  CG1 . VAL C 1 47  ? 24.060  14.669  28.456  1.00 33.40 ? 47  VAL C CG1 1 
ATOM   2553 C  CG2 . VAL C 1 47  ? 25.154  13.689  30.476  1.00 33.42 ? 47  VAL C CG2 1 
ATOM   2554 N  N   . HIS C 1 48  ? 26.103  17.125  27.442  1.00 33.48 ? 48  HIS C N   1 
ATOM   2555 C  CA  . HIS C 1 48  ? 25.764  18.244  26.584  1.00 33.17 ? 48  HIS C CA  1 
ATOM   2556 C  C   . HIS C 1 48  ? 24.586  17.882  25.680  1.00 33.45 ? 48  HIS C C   1 
ATOM   2557 O  O   . HIS C 1 48  ? 24.287  16.702  25.466  1.00 34.00 ? 48  HIS C O   1 
ATOM   2558 C  CB  . HIS C 1 48  ? 26.993  18.668  25.778  1.00 33.00 ? 48  HIS C CB  1 
ATOM   2559 C  CG  . HIS C 1 48  ? 28.040  19.324  26.618  1.00 32.55 ? 48  HIS C CG  1 
ATOM   2560 N  ND1 . HIS C 1 48  ? 28.381  20.652  26.473  1.00 31.17 ? 48  HIS C ND1 1 
ATOM   2561 C  CD2 . HIS C 1 48  ? 28.779  18.857  27.650  1.00 32.19 ? 48  HIS C CD2 1 
ATOM   2562 C  CE1 . HIS C 1 48  ? 29.314  20.961  27.356  1.00 32.70 ? 48  HIS C CE1 1 
ATOM   2563 N  NE2 . HIS C 1 48  ? 29.560  19.894  28.093  1.00 33.08 ? 48  HIS C NE2 1 
ATOM   2564 N  N   . GLU C 1 49  ? 23.927  18.903  25.147  1.00 33.43 ? 49  GLU C N   1 
ATOM   2565 C  CA  . GLU C 1 49  ? 22.603  18.729  24.550  1.00 33.58 ? 49  GLU C CA  1 
ATOM   2566 C  C   . GLU C 1 49  ? 22.564  17.875  23.278  1.00 33.99 ? 49  GLU C C   1 
ATOM   2567 O  O   . GLU C 1 49  ? 21.655  17.061  23.113  1.00 33.95 ? 49  GLU C O   1 
ATOM   2568 C  CB  . GLU C 1 49  ? 21.974  20.095  24.266  1.00 33.45 ? 49  GLU C CB  1 
ATOM   2569 C  CG  . GLU C 1 49  ? 20.510  20.022  23.827  1.00 33.57 ? 49  GLU C CG  1 
ATOM   2570 C  CD  . GLU C 1 49  ? 19.910  21.381  23.563  1.00 33.84 ? 49  GLU C CD  1 
ATOM   2571 O  OE1 . GLU C 1 49  ? 20.607  22.391  23.786  1.00 35.68 ? 49  GLU C OE1 1 
ATOM   2572 O  OE2 . GLU C 1 49  ? 18.739  21.441  23.127  1.00 34.93 ? 49  GLU C OE2 1 
ATOM   2573 N  N   . PHE C 1 50  ? 23.524  18.062  22.376  1.00 34.09 ? 50  PHE C N   1 
ATOM   2574 C  CA  . PHE C 1 50  ? 23.440  17.445  21.046  1.00 34.35 ? 50  PHE C CA  1 
ATOM   2575 C  C   . PHE C 1 50  ? 24.431  16.310  20.875  1.00 34.66 ? 50  PHE C C   1 
ATOM   2576 O  O   . PHE C 1 50  ? 25.582  16.411  21.302  1.00 33.94 ? 50  PHE C O   1 
ATOM   2577 C  CB  . PHE C 1 50  ? 23.636  18.501  19.954  1.00 34.36 ? 50  PHE C CB  1 
ATOM   2578 C  CG  . PHE C 1 50  ? 22.682  19.653  20.069  1.00 34.29 ? 50  PHE C CG  1 
ATOM   2579 C  CD1 . PHE C 1 50  ? 21.310  19.437  20.019  1.00 34.65 ? 50  PHE C CD1 1 
ATOM   2580 C  CD2 . PHE C 1 50  ? 23.144  20.944  20.260  1.00 34.97 ? 50  PHE C CD2 1 
ATOM   2581 C  CE1 . PHE C 1 50  ? 20.423  20.486  20.153  1.00 34.97 ? 50  PHE C CE1 1 
ATOM   2582 C  CE2 . PHE C 1 50  ? 22.260  21.993  20.393  1.00 34.18 ? 50  PHE C CE2 1 
ATOM   2583 C  CZ  . PHE C 1 50  ? 20.900  21.765  20.340  1.00 34.38 ? 50  PHE C CZ  1 
ATOM   2584 N  N   . GLY C 1 51  ? 23.970  15.233  20.235  1.00 35.42 ? 51  GLY C N   1 
ATOM   2585 C  CA  . GLY C 1 51  ? 24.818  14.108  19.897  1.00 35.99 ? 51  GLY C CA  1 
ATOM   2586 C  C   . GLY C 1 51  ? 25.504  14.340  18.569  1.00 36.53 ? 51  GLY C C   1 
ATOM   2587 O  O   . GLY C 1 51  ? 25.465  13.475  17.686  1.00 37.15 ? 51  GLY C O   1 
ATOM   2588 N  N   . ASP C 1 52  ? 26.121  15.515  18.424  1.00 36.74 ? 52  ASP C N   1 
ATOM   2589 C  CA  . ASP C 1 52  ? 26.651  15.986  17.150  1.00 36.64 ? 52  ASP C CA  1 
ATOM   2590 C  C   . ASP C 1 52  ? 28.162  16.151  17.280  1.00 36.88 ? 52  ASP C C   1 
ATOM   2591 O  O   . ASP C 1 52  ? 28.633  16.994  18.034  1.00 36.44 ? 52  ASP C O   1 
ATOM   2592 C  CB  . ASP C 1 52  ? 25.982  17.309  16.770  1.00 36.47 ? 52  ASP C CB  1 
ATOM   2593 C  CG  . ASP C 1 52  ? 26.400  17.824  15.396  1.00 36.34 ? 52  ASP C CG  1 
ATOM   2594 O  OD1 . ASP C 1 52  ? 27.481  17.449  14.885  1.00 33.71 ? 52  ASP C OD1 1 
ATOM   2595 O  OD2 . ASP C 1 52  ? 25.633  18.630  14.837  1.00 36.26 ? 52  ASP C OD2 1 
ATOM   2596 N  N   . ASN C 1 53  ? 28.906  15.319  16.555  1.00 37.28 ? 53  ASN C N   1 
ATOM   2597 C  CA  . ASN C 1 53  ? 30.370  15.350  16.566  1.00 37.66 ? 53  ASN C CA  1 
ATOM   2598 C  C   . ASN C 1 53  ? 30.950  15.811  15.227  1.00 37.82 ? 53  ASN C C   1 
ATOM   2599 O  O   . ASN C 1 53  ? 32.102  15.506  14.909  1.00 38.04 ? 53  ASN C O   1 
ATOM   2600 C  CB  . ASN C 1 53  ? 30.908  13.955  16.936  1.00 37.78 ? 53  ASN C CB  1 
ATOM   2601 C  CG  . ASN C 1 53  ? 32.399  13.953  17.239  1.00 38.92 ? 53  ASN C CG  1 
ATOM   2602 O  OD1 . ASN C 1 53  ? 32.897  14.756  18.040  1.00 41.42 ? 53  ASN C OD1 1 
ATOM   2603 N  ND2 . ASN C 1 53  ? 33.122  13.045  16.595  1.00 41.74 ? 53  ASN C ND2 1 
ATOM   2604 N  N   . THR C 1 54  ? 30.175  16.568  14.450  1.00 37.70 ? 54  THR C N   1 
ATOM   2605 C  CA  . THR C 1 54  ? 30.617  16.992  13.120  1.00 37.76 ? 54  THR C CA  1 
ATOM   2606 C  C   . THR C 1 54  ? 31.752  18.001  13.189  1.00 37.74 ? 54  THR C C   1 
ATOM   2607 O  O   . THR C 1 54  ? 32.577  18.051  12.285  1.00 37.80 ? 54  THR C O   1 
ATOM   2608 C  CB  . THR C 1 54  ? 29.482  17.612  12.290  1.00 37.74 ? 54  THR C CB  1 
ATOM   2609 O  OG1 . THR C 1 54  ? 28.888  18.684  13.024  1.00 37.36 ? 54  THR C OG1 1 
ATOM   2610 C  CG2 . THR C 1 54  ? 28.428  16.561  11.953  1.00 37.88 ? 54  THR C CG2 1 
ATOM   2611 N  N   . ALA C 1 55  ? 31.781  18.800  14.257  1.00 37.97 ? 55  ALA C N   1 
ATOM   2612 C  CA  . ALA C 1 55  ? 32.891  19.720  14.527  1.00 38.01 ? 55  ALA C CA  1 
ATOM   2613 C  C   . ALA C 1 55  ? 33.543  19.403  15.875  1.00 38.23 ? 55  ALA C C   1 
ATOM   2614 O  O   . ALA C 1 55  ? 33.765  20.296  16.693  1.00 38.58 ? 55  ALA C O   1 
ATOM   2615 C  CB  . ALA C 1 55  ? 32.394  21.158  14.502  1.00 38.12 ? 55  ALA C CB  1 
ATOM   2616 N  N   . GLY C 1 56  ? 33.834  18.124  16.111  1.00 38.06 ? 56  GLY C N   1 
ATOM   2617 C  CA  . GLY C 1 56  ? 34.432  17.693  17.367  1.00 37.99 ? 56  GLY C CA  1 
ATOM   2618 C  C   . GLY C 1 56  ? 33.490  17.859  18.545  1.00 38.02 ? 56  GLY C C   1 
ATOM   2619 O  O   . GLY C 1 56  ? 32.276  17.715  18.413  1.00 37.94 ? 56  GLY C O   1 
ATOM   2620 N  N   . CYS C 1 57  ? 34.047  18.188  19.703  1.00 37.75 ? 57  CYS C N   1 
ATOM   2621 C  CA  . CYS C 1 57  ? 33.236  18.351  20.900  1.00 37.95 ? 57  CYS C CA  1 
ATOM   2622 C  C   . CYS C 1 57  ? 32.479  19.677  20.927  1.00 37.17 ? 57  CYS C C   1 
ATOM   2623 O  O   . CYS C 1 57  ? 31.527  19.826  21.675  1.00 36.78 ? 57  CYS C O   1 
ATOM   2624 C  CB  . CYS C 1 57  ? 34.100  18.167  22.149  1.00 38.26 ? 57  CYS C CB  1 
ATOM   2625 S  SG  . CYS C 1 57  ? 34.844  16.490  22.219  1.00 41.70 ? 57  CYS C SG  1 
ATOM   2626 N  N   . THR C 1 58  ? 32.876  20.622  20.084  1.00 36.82 ? 58  THR C N   1 
ATOM   2627 C  CA  . THR C 1 58  ? 32.210  21.922  20.019  1.00 36.77 ? 58  THR C CA  1 
ATOM   2628 C  C   . THR C 1 58  ? 30.744  21.801  19.584  1.00 36.30 ? 58  THR C C   1 
ATOM   2629 O  O   . THR C 1 58  ? 29.876  22.516  20.089  1.00 35.30 ? 58  THR C O   1 
ATOM   2630 C  CB  . THR C 1 58  ? 32.947  22.861  19.058  1.00 36.78 ? 58  THR C CB  1 
ATOM   2631 O  OG1 . THR C 1 58  ? 34.326  22.931  19.435  1.00 38.07 ? 58  THR C OG1 1 
ATOM   2632 C  CG2 . THR C 1 58  ? 32.352  24.268  19.091  1.00 37.19 ? 58  THR C CG2 1 
ATOM   2633 N  N   . SER C 1 59  ? 30.473  20.882  18.659  1.00 35.79 ? 59  SER C N   1 
ATOM   2634 C  CA  . SER C 1 59  ? 29.135  20.744  18.094  1.00 35.75 ? 59  SER C CA  1 
ATOM   2635 C  C   . SER C 1 59  ? 28.141  20.047  19.047  1.00 35.46 ? 59  SER C C   1 
ATOM   2636 O  O   . SER C 1 59  ? 26.948  19.956  18.742  1.00 35.43 ? 59  SER C O   1 
ATOM   2637 C  CB  . SER C 1 59  ? 29.208  20.025  16.741  1.00 35.86 ? 59  SER C CB  1 
ATOM   2638 O  OG  . SER C 1 59  ? 30.057  18.893  16.814  1.00 37.97 ? 59  SER C OG  1 
ATOM   2639 N  N   . ALA C 1 60  ? 28.621  19.563  20.196  1.00 34.84 ? 60  ALA C N   1 
ATOM   2640 C  CA  . ALA C 1 60  ? 27.725  19.041  21.224  1.00 34.77 ? 60  ALA C CA  1 
ATOM   2641 C  C   . ALA C 1 60  ? 26.868  20.130  21.873  1.00 34.50 ? 60  ALA C C   1 
ATOM   2642 O  O   . ALA C 1 60  ? 25.886  19.824  22.546  1.00 34.86 ? 60  ALA C O   1 
ATOM   2643 C  CB  . ALA C 1 60  ? 28.506  18.270  22.286  1.00 35.02 ? 60  ALA C CB  1 
ATOM   2644 N  N   . GLY C 1 61  ? 27.226  21.396  21.670  1.00 34.24 ? 61  GLY C N   1 
ATOM   2645 C  CA  . GLY C 1 61  ? 26.424  22.512  22.168  1.00 34.31 ? 61  GLY C CA  1 
ATOM   2646 C  C   . GLY C 1 61  ? 26.573  22.707  23.668  1.00 34.19 ? 61  GLY C C   1 
ATOM   2647 O  O   . GLY C 1 61  ? 27.583  22.312  24.248  1.00 33.88 ? 61  GLY C O   1 
ATOM   2648 N  N   . PRO C 1 62  ? 25.548  23.288  24.315  1.00 34.01 ? 62  PRO C N   1 
ATOM   2649 C  CA  . PRO C 1 62  ? 25.674  23.665  25.716  1.00 34.15 ? 62  PRO C CA  1 
ATOM   2650 C  C   . PRO C 1 62  ? 25.403  22.499  26.650  1.00 34.35 ? 62  PRO C C   1 
ATOM   2651 O  O   . PRO C 1 62  ? 25.048  21.407  26.195  1.00 33.95 ? 62  PRO C O   1 
ATOM   2652 C  CB  . PRO C 1 62  ? 24.594  24.738  25.872  1.00 34.02 ? 62  PRO C CB  1 
ATOM   2653 C  CG  . PRO C 1 62  ? 23.513  24.293  24.948  1.00 34.16 ? 62  PRO C CG  1 
ATOM   2654 C  CD  . PRO C 1 62  ? 24.213  23.617  23.780  1.00 34.22 ? 62  PRO C CD  1 
ATOM   2655 N  N   . HIS C 1 63  ? 25.596  22.729  27.946  1.00 34.66 ? 63  HIS C N   1 
ATOM   2656 C  CA  . HIS C 1 63  ? 25.145  21.796  28.973  1.00 34.98 ? 63  HIS C CA  1 
ATOM   2657 C  C   . HIS C 1 63  ? 23.684  21.443  28.713  1.00 35.17 ? 63  HIS C C   1 
ATOM   2658 O  O   . HIS C 1 63  ? 22.890  22.307  28.381  1.00 34.52 ? 63  HIS C O   1 
ATOM   2659 C  CB  . HIS C 1 63  ? 25.240  22.428  30.360  1.00 34.95 ? 63  HIS C CB  1 
ATOM   2660 C  CG  . HIS C 1 63  ? 26.635  22.557  30.887  1.00 35.52 ? 63  HIS C CG  1 
ATOM   2661 N  ND1 . HIS C 1 63  ? 26.950  23.394  31.936  1.00 35.30 ? 63  HIS C ND1 1 
ATOM   2662 C  CD2 . HIS C 1 63  ? 27.796  21.972  30.510  1.00 36.05 ? 63  HIS C CD2 1 
ATOM   2663 C  CE1 . HIS C 1 63  ? 28.244  23.310  32.190  1.00 36.04 ? 63  HIS C CE1 1 
ATOM   2664 N  NE2 . HIS C 1 63  ? 28.780  22.454  31.339  1.00 35.63 ? 63  HIS C NE2 1 
ATOM   2665 N  N   . PHE C 1 64  ? 23.330  20.173  28.858  1.00 35.46 ? 64  PHE C N   1 
ATOM   2666 C  CA  . PHE C 1 64  ? 21.957  19.755  28.618  1.00 36.32 ? 64  PHE C CA  1 
ATOM   2667 C  C   . PHE C 1 64  ? 21.079  20.298  29.740  1.00 37.20 ? 64  PHE C C   1 
ATOM   2668 O  O   . PHE C 1 64  ? 21.377  20.109  30.920  1.00 37.11 ? 64  PHE C O   1 
ATOM   2669 C  CB  . PHE C 1 64  ? 21.880  18.227  28.528  1.00 36.11 ? 64  PHE C CB  1 
ATOM   2670 C  CG  . PHE C 1 64  ? 20.479  17.681  28.372  1.00 36.08 ? 64  PHE C CG  1 
ATOM   2671 C  CD1 . PHE C 1 64  ? 19.622  18.167  27.394  1.00 35.79 ? 64  PHE C CD1 1 
ATOM   2672 C  CD2 . PHE C 1 64  ? 20.047  16.636  29.178  1.00 35.51 ? 64  PHE C CD2 1 
ATOM   2673 C  CE1 . PHE C 1 64  ? 18.338  17.650  27.254  1.00 36.31 ? 64  PHE C CE1 1 
ATOM   2674 C  CE2 . PHE C 1 64  ? 18.779  16.111  29.041  1.00 36.45 ? 64  PHE C CE2 1 
ATOM   2675 C  CZ  . PHE C 1 64  ? 17.918  16.611  28.074  1.00 35.64 ? 64  PHE C CZ  1 
ATOM   2676 N  N   . ASN C 1 65  ? 20.018  21.006  29.368  1.00 38.27 ? 65  ASN C N   1 
ATOM   2677 C  CA  . ASN C 1 65  ? 19.094  21.546  30.351  1.00 39.26 ? 65  ASN C CA  1 
ATOM   2678 C  C   . ASN C 1 65  ? 17.725  21.792  29.731  1.00 40.13 ? 65  ASN C C   1 
ATOM   2679 O  O   . ASN C 1 65  ? 17.426  22.909  29.298  1.00 40.41 ? 65  ASN C O   1 
ATOM   2680 C  CB  . ASN C 1 65  ? 19.660  22.829  30.967  1.00 39.36 ? 65  ASN C CB  1 
ATOM   2681 C  CG  . ASN C 1 65  ? 19.121  23.091  32.360  1.00 39.18 ? 65  ASN C CG  1 
ATOM   2682 O  OD1 . ASN C 1 65  ? 18.910  22.159  33.149  1.00 40.11 ? 65  ASN C OD1 1 
ATOM   2683 N  ND2 . ASN C 1 65  ? 18.902  24.357  32.674  1.00 39.25 ? 65  ASN C ND2 1 
ATOM   2684 N  N   . PRO C 1 66  ? 16.885  20.746  29.689  1.00 41.05 ? 66  PRO C N   1 
ATOM   2685 C  CA  . PRO C 1 66  ? 15.582  20.825  29.029  1.00 41.76 ? 66  PRO C CA  1 
ATOM   2686 C  C   . PRO C 1 66  ? 14.567  21.700  29.764  1.00 42.49 ? 66  PRO C C   1 
ATOM   2687 O  O   . PRO C 1 66  ? 14.791  22.092  30.912  1.00 42.64 ? 66  PRO C O   1 
ATOM   2688 C  CB  . PRO C 1 66  ? 15.113  19.370  29.025  1.00 41.82 ? 66  PRO C CB  1 
ATOM   2689 C  CG  . PRO C 1 66  ? 15.787  18.760  30.197  1.00 41.45 ? 66  PRO C CG  1 
ATOM   2690 C  CD  . PRO C 1 66  ? 17.115  19.418  30.286  1.00 40.99 ? 66  PRO C CD  1 
ATOM   2691 N  N   . LEU C 1 67  ? 13.448  21.977  29.101  1.00 43.47 ? 67  LEU C N   1 
ATOM   2692 C  CA  . LEU C 1 67  ? 12.375  22.785  29.677  1.00 43.82 ? 67  LEU C CA  1 
ATOM   2693 C  C   . LEU C 1 67  ? 11.542  21.960  30.671  1.00 44.37 ? 67  LEU C C   1 
ATOM   2694 O  O   . LEU C 1 67  ? 10.347  21.738  30.461  1.00 44.75 ? 67  LEU C O   1 
ATOM   2695 C  CB  . LEU C 1 67  ? 11.493  23.360  28.559  1.00 43.99 ? 67  LEU C CB  1 
ATOM   2696 C  CG  . LEU C 1 67  ? 10.535  24.497  28.925  1.00 44.17 ? 67  LEU C CG  1 
ATOM   2697 C  CD1 . LEU C 1 67  ? 11.300  25.793  29.182  1.00 44.98 ? 67  LEU C CD1 1 
ATOM   2698 C  CD2 . LEU C 1 67  ? 9.483   24.711  27.835  1.00 44.12 ? 67  LEU C CD2 1 
ATOM   2699 N  N   . SER C 1 68  ? 12.181  21.516  31.757  1.00 44.84 ? 68  SER C N   1 
ATOM   2700 C  CA  . SER C 1 68  ? 11.493  20.793  32.834  1.00 44.91 ? 68  SER C CA  1 
ATOM   2701 C  C   . SER C 1 68  ? 10.642  21.757  33.649  1.00 45.26 ? 68  SER C C   1 
ATOM   2702 O  O   . SER C 1 68  ? 11.147  22.741  34.193  1.00 45.64 ? 68  SER C O   1 
ATOM   2703 C  CB  . SER C 1 68  ? 12.494  20.094  33.762  1.00 45.11 ? 68  SER C CB  1 
ATOM   2704 O  OG  . SER C 1 68  ? 13.083  18.961  33.146  1.00 45.41 ? 68  SER C OG  1 
ATOM   2705 N  N   . ARG C 1 79  ? 21.190  22.672  39.631  1.00 41.21 ? 79  ARG C N   1 
ATOM   2706 C  CA  . ARG C 1 79  ? 22.157  22.255  38.623  1.00 41.35 ? 79  ARG C CA  1 
ATOM   2707 C  C   . ARG C 1 79  ? 21.445  21.742  37.387  1.00 40.73 ? 79  ARG C C   1 
ATOM   2708 O  O   . ARG C 1 79  ? 20.316  21.255  37.469  1.00 40.69 ? 79  ARG C O   1 
ATOM   2709 C  CB  . ARG C 1 79  ? 23.090  21.170  39.174  1.00 41.71 ? 79  ARG C CB  1 
ATOM   2710 C  CG  . ARG C 1 79  ? 23.987  21.663  40.308  1.00 42.80 ? 79  ARG C CG  1 
ATOM   2711 C  CD  . ARG C 1 79  ? 25.156  20.724  40.567  1.00 43.13 ? 79  ARG C CD  1 
ATOM   2712 N  NE  . ARG C 1 79  ? 26.182  21.370  41.391  1.00 44.11 ? 79  ARG C NE  1 
ATOM   2713 C  CZ  . ARG C 1 79  ? 27.444  20.950  41.522  1.00 44.53 ? 79  ARG C CZ  1 
ATOM   2714 N  NH1 . ARG C 1 79  ? 27.882  19.863  40.891  1.00 45.48 ? 79  ARG C NH1 1 
ATOM   2715 N  NH2 . ARG C 1 79  ? 28.281  21.629  42.298  1.00 45.01 ? 79  ARG C NH2 1 
ATOM   2716 N  N   . HIS C 1 80  ? 22.104  21.847  36.237  1.00 40.13 ? 80  HIS C N   1 
ATOM   2717 C  CA  . HIS C 1 80  ? 21.498  21.402  34.990  1.00 39.99 ? 80  HIS C CA  1 
ATOM   2718 C  C   . HIS C 1 80  ? 21.430  19.881  34.980  1.00 39.48 ? 80  HIS C C   1 
ATOM   2719 O  O   . HIS C 1 80  ? 22.176  19.212  35.695  1.00 39.23 ? 80  HIS C O   1 
ATOM   2720 C  CB  . HIS C 1 80  ? 22.254  21.953  33.771  1.00 40.12 ? 80  HIS C CB  1 
ATOM   2721 C  CG  . HIS C 1 80  ? 23.521  21.228  33.454  1.00 40.19 ? 80  HIS C CG  1 
ATOM   2722 N  ND1 . HIS C 1 80  ? 23.581  20.209  32.527  1.00 41.03 ? 80  HIS C ND1 1 
ATOM   2723 C  CD2 . HIS C 1 80  ? 24.783  21.387  33.920  1.00 40.49 ? 80  HIS C CD2 1 
ATOM   2724 C  CE1 . HIS C 1 80  ? 24.824  19.766  32.442  1.00 41.21 ? 80  HIS C CE1 1 
ATOM   2725 N  NE2 . HIS C 1 80  ? 25.570  20.456  33.285  1.00 40.80 ? 80  HIS C NE2 1 
ATOM   2726 N  N   . VAL C 1 81  ? 20.527  19.336  34.173  1.00 39.37 ? 81  VAL C N   1 
ATOM   2727 C  CA  . VAL C 1 81  ? 20.301  17.893  34.149  1.00 39.47 ? 81  VAL C CA  1 
ATOM   2728 C  C   . VAL C 1 81  ? 21.610  17.126  33.875  1.00 39.81 ? 81  VAL C C   1 
ATOM   2729 O  O   . VAL C 1 81  ? 21.960  16.198  34.594  1.00 41.32 ? 81  VAL C O   1 
ATOM   2730 C  CB  . VAL C 1 81  ? 19.177  17.525  33.143  1.00 39.43 ? 81  VAL C CB  1 
ATOM   2731 C  CG1 . VAL C 1 81  ? 19.041  16.019  32.991  1.00 39.35 ? 81  VAL C CG1 1 
ATOM   2732 C  CG2 . VAL C 1 81  ? 17.849  18.122  33.606  1.00 39.21 ? 81  VAL C CG2 1 
ATOM   2733 N  N   . GLY C 1 82  ? 22.362  17.522  32.867  1.00 39.67 ? 82  GLY C N   1 
ATOM   2734 C  CA  . GLY C 1 82  ? 23.628  16.827  32.584  1.00 39.00 ? 82  GLY C CA  1 
ATOM   2735 C  C   . GLY C 1 82  ? 24.808  16.979  33.550  1.00 38.54 ? 82  GLY C C   1 
ATOM   2736 O  O   . GLY C 1 82  ? 25.883  16.439  33.288  1.00 37.91 ? 82  GLY C O   1 
ATOM   2737 N  N   . ASP C 1 83  ? 24.645  17.719  34.642  1.00 37.80 ? 83  ASP C N   1 
ATOM   2738 C  CA  . ASP C 1 83  ? 25.772  18.009  35.542  1.00 38.03 ? 83  ASP C CA  1 
ATOM   2739 C  C   . ASP C 1 83  ? 26.127  16.773  36.353  1.00 37.87 ? 83  ASP C C   1 
ATOM   2740 O  O   . ASP C 1 83  ? 25.395  16.409  37.274  1.00 38.23 ? 83  ASP C O   1 
ATOM   2741 C  CB  . ASP C 1 83  ? 25.424  19.163  36.487  1.00 37.90 ? 83  ASP C CB  1 
ATOM   2742 C  CG  . ASP C 1 83  ? 26.638  19.730  37.201  1.00 37.99 ? 83  ASP C CG  1 
ATOM   2743 O  OD1 . ASP C 1 83  ? 27.605  18.984  37.469  1.00 37.74 ? 83  ASP C OD1 1 
ATOM   2744 O  OD2 . ASP C 1 83  ? 26.616  20.935  37.516  1.00 38.31 ? 83  ASP C OD2 1 
ATOM   2745 N  N   . LEU C 1 84  ? 27.238  16.126  36.000  1.00 37.61 ? 84  LEU C N   1 
ATOM   2746 C  CA  . LEU C 1 84  ? 27.690  14.936  36.713  1.00 37.53 ? 84  LEU C CA  1 
ATOM   2747 C  C   . LEU C 1 84  ? 28.948  15.215  37.538  1.00 37.40 ? 84  LEU C C   1 
ATOM   2748 O  O   . LEU C 1 84  ? 29.724  14.303  37.830  1.00 38.07 ? 84  LEU C O   1 
ATOM   2749 C  CB  . LEU C 1 84  ? 27.918  13.790  35.734  1.00 37.60 ? 84  LEU C CB  1 
ATOM   2750 C  CG  . LEU C 1 84  ? 26.673  13.384  34.945  1.00 38.43 ? 84  LEU C CG  1 
ATOM   2751 C  CD1 . LEU C 1 84  ? 27.034  12.368  33.891  1.00 39.68 ? 84  LEU C CD1 1 
ATOM   2752 C  CD2 . LEU C 1 84  ? 25.597  12.845  35.883  1.00 38.56 ? 84  LEU C CD2 1 
ATOM   2753 N  N   . GLY C 1 85  ? 29.140  16.478  37.910  1.00 36.89 ? 85  GLY C N   1 
ATOM   2754 C  CA  . GLY C 1 85  ? 30.236  16.865  38.791  1.00 36.62 ? 85  GLY C CA  1 
ATOM   2755 C  C   . GLY C 1 85  ? 31.575  16.858  38.084  1.00 36.22 ? 85  GLY C C   1 
ATOM   2756 O  O   . GLY C 1 85  ? 31.709  17.413  36.994  1.00 36.17 ? 85  GLY C O   1 
ATOM   2757 N  N   . ASN C 1 86  ? 32.567  16.245  38.723  1.00 35.97 ? 86  ASN C N   1 
ATOM   2758 C  CA  . ASN C 1 86  ? 33.899  16.071  38.146  1.00 36.06 ? 86  ASN C CA  1 
ATOM   2759 C  C   . ASN C 1 86  ? 34.270  14.599  38.155  1.00 36.09 ? 86  ASN C C   1 
ATOM   2760 O  O   . ASN C 1 86  ? 33.646  13.798  38.850  1.00 36.42 ? 86  ASN C O   1 
ATOM   2761 C  CB  . ASN C 1 86  ? 34.954  16.831  38.954  1.00 35.83 ? 86  ASN C CB  1 
ATOM   2762 C  CG  . ASN C 1 86  ? 34.696  18.320  39.005  1.00 36.28 ? 86  ASN C CG  1 
ATOM   2763 O  OD1 . ASN C 1 86  ? 34.951  19.034  38.036  1.00 36.19 ? 86  ASN C OD1 1 
ATOM   2764 N  ND2 . ASN C 1 86  ? 34.212  18.804  40.151  1.00 37.03 ? 86  ASN C ND2 1 
ATOM   2765 N  N   . VAL C 1 87  ? 35.281  14.251  37.370  1.00 36.01 ? 87  VAL C N   1 
ATOM   2766 C  CA  . VAL C 1 87  ? 35.987  12.982  37.533  1.00 36.27 ? 87  VAL C CA  1 
ATOM   2767 C  C   . VAL C 1 87  ? 37.406  13.329  37.965  1.00 36.02 ? 87  VAL C C   1 
ATOM   2768 O  O   . VAL C 1 87  ? 37.855  14.446  37.744  1.00 35.68 ? 87  VAL C O   1 
ATOM   2769 C  CB  . VAL C 1 87  ? 35.985  12.122  36.255  1.00 36.67 ? 87  VAL C CB  1 
ATOM   2770 C  CG1 . VAL C 1 87  ? 34.572  11.728  35.909  1.00 38.17 ? 87  VAL C CG1 1 
ATOM   2771 C  CG2 . VAL C 1 87  ? 36.661  12.855  35.083  1.00 37.07 ? 87  VAL C CG2 1 
ATOM   2772 N  N   . THR C 1 88  ? 38.086  12.385  38.606  1.00 35.83 ? 88  THR C N   1 
ATOM   2773 C  CA  . THR C 1 88  ? 39.397  12.648  39.199  1.00 36.04 ? 88  THR C CA  1 
ATOM   2774 C  C   . THR C 1 88  ? 40.462  11.742  38.588  1.00 35.95 ? 88  THR C C   1 
ATOM   2775 O  O   . THR C 1 88  ? 40.390  10.521  38.715  1.00 35.84 ? 88  THR C O   1 
ATOM   2776 C  CB  . THR C 1 88  ? 39.366  12.439  40.735  1.00 36.27 ? 88  THR C CB  1 
ATOM   2777 O  OG1 . THR C 1 88  ? 38.322  13.232  41.320  1.00 36.47 ? 88  THR C OG1 1 
ATOM   2778 C  CG2 . THR C 1 88  ? 40.699  12.823  41.359  1.00 35.94 ? 88  THR C CG2 1 
ATOM   2779 N  N   . ALA C 1 89  ? 41.456  12.348  37.945  1.00 36.13 ? 89  ALA C N   1 
ATOM   2780 C  CA  . ALA C 1 89  ? 42.562  11.602  37.356  1.00 36.36 ? 89  ALA C CA  1 
ATOM   2781 C  C   . ALA C 1 89  ? 43.685  11.452  38.377  1.00 36.35 ? 89  ALA C C   1 
ATOM   2782 O  O   . ALA C 1 89  ? 44.013  12.401  39.104  1.00 36.17 ? 89  ALA C O   1 
ATOM   2783 C  CB  . ALA C 1 89  ? 43.077  12.310  36.122  1.00 36.41 ? 89  ALA C CB  1 
ATOM   2784 N  N   . ASP C 1 90  ? 44.274  10.260  38.427  1.00 36.61 ? 90  ASP C N   1 
ATOM   2785 C  CA  . ASP C 1 90  ? 45.407  10.002  39.318  1.00 37.20 ? 90  ASP C CA  1 
ATOM   2786 C  C   . ASP C 1 90  ? 46.706  10.512  38.686  1.00 37.10 ? 90  ASP C C   1 
ATOM   2787 O  O   . ASP C 1 90  ? 46.668  11.198  37.662  1.00 36.70 ? 90  ASP C O   1 
ATOM   2788 C  CB  . ASP C 1 90  ? 45.486  8.510   39.685  1.00 37.23 ? 90  ASP C CB  1 
ATOM   2789 C  CG  . ASP C 1 90  ? 45.826  7.615   38.502  1.00 38.49 ? 90  ASP C CG  1 
ATOM   2790 O  OD1 . ASP C 1 90  ? 46.323  8.113   37.467  1.00 39.23 ? 90  ASP C OD1 1 
ATOM   2791 O  OD2 . ASP C 1 90  ? 45.584  6.394   38.616  1.00 38.77 ? 90  ASP C OD2 1 
ATOM   2792 N  N   . LYS C 1 91  ? 47.842  10.187  39.310  1.00 37.11 ? 91  LYS C N   1 
ATOM   2793 C  CA  . LYS C 1 91  ? 49.165  10.592  38.825  1.00 37.62 ? 91  LYS C CA  1 
ATOM   2794 C  C   . LYS C 1 91  ? 49.559  9.986   37.478  1.00 37.63 ? 91  LYS C C   1 
ATOM   2795 O  O   . LYS C 1 91  ? 50.468  10.497  36.813  1.00 38.28 ? 91  LYS C O   1 
ATOM   2796 C  CB  . LYS C 1 91  ? 50.244  10.191  39.841  1.00 37.37 ? 91  LYS C CB  1 
ATOM   2797 C  CG  . LYS C 1 91  ? 50.161  10.906  41.173  1.00 38.46 ? 91  LYS C CG  1 
ATOM   2798 C  CD  . LYS C 1 91  ? 51.194  10.356  42.158  1.00 38.32 ? 91  LYS C CD  1 
ATOM   2799 C  CE  . LYS C 1 91  ? 51.005  10.967  43.545  1.00 38.66 ? 91  LYS C CE  1 
ATOM   2800 N  NZ  . LYS C 1 91  ? 51.722  10.224  44.621  1.00 39.56 ? 91  LYS C NZ  1 
ATOM   2801 N  N   . ASP C 1 92  ? 48.933  8.866   37.122  1.00 37.62 ? 92  ASP C N   1 
ATOM   2802 C  CA  . ASP C 1 92  ? 49.153  8.205   35.832  1.00 37.57 ? 92  ASP C CA  1 
ATOM   2803 C  C   . ASP C 1 92  ? 48.176  8.702   34.767  1.00 37.08 ? 92  ASP C C   1 
ATOM   2804 O  O   . ASP C 1 92  ? 48.214  8.241   33.622  1.00 37.10 ? 92  ASP C O   1 
ATOM   2805 C  CB  . ASP C 1 92  ? 49.005  6.686   35.984  1.00 37.60 ? 92  ASP C CB  1 
ATOM   2806 C  CG  . ASP C 1 92  ? 49.997  6.099   36.963  1.00 38.62 ? 92  ASP C CG  1 
ATOM   2807 O  OD1 . ASP C 1 92  ? 51.112  6.639   37.063  1.00 39.38 ? 92  ASP C OD1 1 
ATOM   2808 O  OD2 . ASP C 1 92  ? 49.657  5.101   37.638  1.00 39.20 ? 92  ASP C OD2 1 
ATOM   2809 N  N   . GLY C 1 93  ? 47.306  9.635   35.147  1.00 36.72 ? 93  GLY C N   1 
ATOM   2810 C  CA  . GLY C 1 93  ? 46.330  10.224  34.227  1.00 36.60 ? 93  GLY C CA  1 
ATOM   2811 C  C   . GLY C 1 93  ? 45.041  9.440   34.035  1.00 36.27 ? 93  GLY C C   1 
ATOM   2812 O  O   . GLY C 1 93  ? 44.293  9.702   33.097  1.00 36.04 ? 93  GLY C O   1 
ATOM   2813 N  N   . VAL C 1 94  ? 44.773  8.496   34.934  1.00 36.04 ? 94  VAL C N   1 
ATOM   2814 C  CA  . VAL C 1 94  ? 43.613  7.618   34.827  1.00 36.18 ? 94  VAL C CA  1 
ATOM   2815 C  C   . VAL C 1 94  ? 42.557  8.019   35.850  1.00 36.11 ? 94  VAL C C   1 
ATOM   2816 O  O   . VAL C 1 94  ? 42.847  8.107   37.044  1.00 35.31 ? 94  VAL C O   1 
ATOM   2817 C  CB  . VAL C 1 94  ? 44.006  6.143   35.056  1.00 36.14 ? 94  VAL C CB  1 
ATOM   2818 C  CG1 . VAL C 1 94  ? 42.801  5.223   34.904  1.00 36.53 ? 94  VAL C CG1 1 
ATOM   2819 C  CG2 . VAL C 1 94  ? 45.114  5.734   34.083  1.00 36.52 ? 94  VAL C CG2 1 
ATOM   2820 N  N   . ALA C 1 95  ? 41.341  8.265   35.368  1.00 36.24 ? 95  ALA C N   1 
ATOM   2821 C  CA  . ALA C 1 95  ? 40.200  8.504   36.230  1.00 36.54 ? 95  ALA C CA  1 
ATOM   2822 C  C   . ALA C 1 95  ? 39.297  7.285   36.194  1.00 36.75 ? 95  ALA C C   1 
ATOM   2823 O  O   . ALA C 1 95  ? 38.652  7.018   35.178  1.00 36.85 ? 95  ALA C O   1 
ATOM   2824 C  CB  . ALA C 1 95  ? 39.433  9.737   35.775  1.00 36.64 ? 95  ALA C CB  1 
ATOM   2825 N  N   . ASP C 1 96  ? 39.254  6.538   37.291  1.00 37.01 ? 96  ASP C N   1 
ATOM   2826 C  CA  . ASP C 1 96  ? 38.227  5.525   37.456  1.00 37.37 ? 96  ASP C CA  1 
ATOM   2827 C  C   . ASP C 1 96  ? 36.978  6.231   37.985  1.00 37.57 ? 96  ASP C C   1 
ATOM   2828 O  O   . ASP C 1 96  ? 37.025  6.972   38.972  1.00 37.68 ? 96  ASP C O   1 
ATOM   2829 C  CB  . ASP C 1 96  ? 38.695  4.390   38.361  1.00 38.26 ? 96  ASP C CB  1 
ATOM   2830 C  CG  . ASP C 1 96  ? 39.844  3.590   37.746  1.00 39.61 ? 96  ASP C CG  1 
ATOM   2831 O  OD1 . ASP C 1 96  ? 39.762  3.235   36.540  1.00 41.94 ? 96  ASP C OD1 1 
ATOM   2832 O  OD2 . ASP C 1 96  ? 40.838  3.314   38.461  1.00 43.52 ? 96  ASP C OD2 1 
ATOM   2833 N  N   . VAL C 1 97  ? 35.865  6.017   37.298  1.00 36.94 ? 97  VAL C N   1 
ATOM   2834 C  CA  . VAL C 1 97  ? 34.643  6.787   37.530  1.00 36.86 ? 97  VAL C CA  1 
ATOM   2835 C  C   . VAL C 1 97  ? 33.584  5.913   38.175  1.00 36.78 ? 97  VAL C C   1 
ATOM   2836 O  O   . VAL C 1 97  ? 33.339  4.799   37.721  1.00 36.56 ? 97  VAL C O   1 
ATOM   2837 C  CB  . VAL C 1 97  ? 34.083  7.345   36.193  1.00 36.56 ? 97  VAL C CB  1 
ATOM   2838 C  CG1 . VAL C 1 97  ? 32.790  8.121   36.421  1.00 36.88 ? 97  VAL C CG1 1 
ATOM   2839 C  CG2 . VAL C 1 97  ? 35.117  8.232   35.513  1.00 36.31 ? 97  VAL C CG2 1 
ATOM   2840 N  N   . SER C 1 98  ? 32.957  6.430   39.229  1.00 36.86 ? 98  SER C N   1 
ATOM   2841 C  CA  . SER C 1 98  ? 31.810  5.781   39.841  1.00 37.33 ? 98  SER C CA  1 
ATOM   2842 C  C   . SER C 1 98  ? 30.868  6.836   40.415  1.00 37.70 ? 98  SER C C   1 
ATOM   2843 O  O   . SER C 1 98  ? 31.179  7.498   41.406  1.00 37.54 ? 98  SER C O   1 
ATOM   2844 C  CB  . SER C 1 98  ? 32.245  4.796   40.920  1.00 37.70 ? 98  SER C CB  1 
ATOM   2845 O  OG  . SER C 1 98  ? 31.139  4.013   41.328  1.00 37.15 ? 98  SER C OG  1 
ATOM   2846 N  N   . ILE C 1 99  ? 29.723  6.992   39.758  1.00 37.68 ? 99  ILE C N   1 
ATOM   2847 C  CA  . ILE C 1 99  ? 28.777  8.057   40.043  1.00 37.96 ? 99  ILE C CA  1 
ATOM   2848 C  C   . ILE C 1 99  ? 27.383  7.424   40.076  1.00 38.03 ? 99  ILE C C   1 
ATOM   2849 O  O   . ILE C 1 99  ? 27.128  6.442   39.373  1.00 37.41 ? 99  ILE C O   1 
ATOM   2850 C  CB  . ILE C 1 99  ? 28.865  9.151   38.928  1.00 38.01 ? 99  ILE C CB  1 
ATOM   2851 C  CG1 . ILE C 1 99  ? 30.209  9.893   39.024  1.00 38.34 ? 99  ILE C CG1 1 
ATOM   2852 C  CG2 . ILE C 1 99  ? 27.704  10.139  38.997  1.00 38.35 ? 99  ILE C CG2 1 
ATOM   2853 C  CD1 . ILE C 1 99  ? 30.468  10.882  37.884  1.00 38.45 ? 99  ILE C CD1 1 
ATOM   2854 N  N   . GLU C 1 100 ? 26.501  7.966   40.907  1.00 38.53 ? 100 GLU C N   1 
ATOM   2855 C  CA  . GLU C 1 100 ? 25.076  7.646   40.822  1.00 38.91 ? 100 GLU C CA  1 
ATOM   2856 C  C   . GLU C 1 100 ? 24.319  8.962   40.782  1.00 38.73 ? 100 GLU C C   1 
ATOM   2857 O  O   . GLU C 1 100 ? 24.565  9.832   41.608  1.00 38.88 ? 100 GLU C O   1 
ATOM   2858 C  CB  . GLU C 1 100 ? 24.621  6.799   42.011  1.00 39.20 ? 100 GLU C CB  1 
ATOM   2859 C  CG  . GLU C 1 100 ? 23.140  6.432   41.965  1.00 40.04 ? 100 GLU C CG  1 
ATOM   2860 C  CD  . GLU C 1 100 ? 22.696  5.606   43.157  1.00 41.45 ? 100 GLU C CD  1 
ATOM   2861 O  OE1 . GLU C 1 100 ? 21.803  6.060   43.921  1.00 43.45 ? 100 GLU C OE1 1 
ATOM   2862 O  OE2 . GLU C 1 100 ? 23.249  4.498   43.336  1.00 46.55 ? 100 GLU C OE2 1 
ATOM   2863 N  N   . ASP C 1 101 ? 23.399  9.107   39.832  1.00 38.23 ? 101 ASP C N   1 
ATOM   2864 C  CA  . ASP C 1 101 ? 22.655  10.354  39.674  1.00 37.94 ? 101 ASP C CA  1 
ATOM   2865 C  C   . ASP C 1 101 ? 21.160  10.082  39.483  1.00 37.59 ? 101 ASP C C   1 
ATOM   2866 O  O   . ASP C 1 101 ? 20.784  9.157   38.764  1.00 37.13 ? 101 ASP C O   1 
ATOM   2867 C  CB  . ASP C 1 101 ? 23.205  11.149  38.485  1.00 38.22 ? 101 ASP C CB  1 
ATOM   2868 C  CG  . ASP C 1 101 ? 22.690  12.576  38.454  1.00 39.05 ? 101 ASP C CG  1 
ATOM   2869 O  OD1 . ASP C 1 101 ? 23.242  13.431  39.184  1.00 41.69 ? 101 ASP C OD1 1 
ATOM   2870 O  OD2 . ASP C 1 101 ? 21.718  12.840  37.716  1.00 38.63 ? 101 ASP C OD2 1 
ATOM   2871 N  N   . SER C 1 102 ? 20.327  10.904  40.115  1.00 37.14 ? 102 SER C N   1 
ATOM   2872 C  CA  . SER C 1 102 ? 18.874  10.727  40.081  1.00 37.13 ? 102 SER C CA  1 
ATOM   2873 C  C   . SER C 1 102 ? 18.150  11.804  39.272  1.00 36.50 ? 102 SER C C   1 
ATOM   2874 O  O   . SER C 1 102 ? 16.910  11.849  39.261  1.00 36.17 ? 102 SER C O   1 
ATOM   2875 C  CB  . SER C 1 102 ? 18.329  10.697  41.506  1.00 37.34 ? 102 SER C CB  1 
ATOM   2876 O  OG  . SER C 1 102 ? 18.585  9.439   42.104  1.00 39.28 ? 102 SER C OG  1 
ATOM   2877 N  N   . VAL C 1 103 ? 18.913  12.671  38.610  1.00 36.06 ? 103 VAL C N   1 
ATOM   2878 C  CA  . VAL C 1 103 ? 18.327  13.720  37.779  1.00 36.06 ? 103 VAL C CA  1 
ATOM   2879 C  C   . VAL C 1 103 ? 18.330  13.294  36.308  1.00 35.60 ? 103 VAL C C   1 
ATOM   2880 O  O   . VAL C 1 103 ? 17.323  13.457  35.614  1.00 35.04 ? 103 VAL C O   1 
ATOM   2881 C  CB  . VAL C 1 103 ? 19.046  15.072  37.978  1.00 36.13 ? 103 VAL C CB  1 
ATOM   2882 C  CG1 . VAL C 1 103 ? 18.454  16.134  37.063  1.00 36.50 ? 103 VAL C CG1 1 
ATOM   2883 C  CG2 . VAL C 1 103 ? 18.946  15.512  39.427  1.00 36.26 ? 103 VAL C CG2 1 
ATOM   2884 N  N   . ILE C 1 104 ? 19.452  12.757  35.831  1.00 35.09 ? 104 ILE C N   1 
ATOM   2885 C  CA  . ILE C 1 104 ? 19.494  12.167  34.492  1.00 35.48 ? 104 ILE C CA  1 
ATOM   2886 C  C   . ILE C 1 104 ? 18.640  10.904  34.405  1.00 35.33 ? 104 ILE C C   1 
ATOM   2887 O  O   . ILE C 1 104 ? 18.359  10.255  35.413  1.00 34.53 ? 104 ILE C O   1 
ATOM   2888 C  CB  . ILE C 1 104 ? 20.941  11.831  34.015  1.00 35.17 ? 104 ILE C CB  1 
ATOM   2889 C  CG1 . ILE C 1 104 ? 21.636  10.860  34.973  1.00 35.56 ? 104 ILE C CG1 1 
ATOM   2890 C  CG2 . ILE C 1 104 ? 21.740  13.104  33.854  1.00 35.96 ? 104 ILE C CG2 1 
ATOM   2891 C  CD1 . ILE C 1 104 ? 22.860  10.179  34.370  1.00 36.13 ? 104 ILE C CD1 1 
ATOM   2892 N  N   . SER C 1 105 ? 18.213  10.580  33.187  1.00 35.45 ? 105 SER C N   1 
ATOM   2893 C  CA  . SER C 1 105 ? 17.520  9.329   32.926  1.00 35.84 ? 105 SER C CA  1 
ATOM   2894 C  C   . SER C 1 105 ? 17.954  8.791   31.574  1.00 35.76 ? 105 SER C C   1 
ATOM   2895 O  O   . SER C 1 105 ? 18.447  9.540   30.724  1.00 36.23 ? 105 SER C O   1 
ATOM   2896 C  CB  . SER C 1 105 ? 16.002  9.530   32.949  1.00 35.42 ? 105 SER C CB  1 
ATOM   2897 O  OG  . SER C 1 105 ? 15.316  8.285   32.942  1.00 35.68 ? 105 SER C OG  1 
ATOM   2898 N  N   . LEU C 1 106 ? 17.790  7.489   31.388  1.00 35.95 ? 106 LEU C N   1 
ATOM   2899 C  CA  . LEU C 1 106 ? 18.060  6.858   30.100  1.00 36.17 ? 106 LEU C CA  1 
ATOM   2900 C  C   . LEU C 1 106 ? 16.790  6.704   29.273  1.00 36.54 ? 106 LEU C C   1 
ATOM   2901 O  O   . LEU C 1 106 ? 16.841  6.199   28.155  1.00 36.44 ? 106 LEU C O   1 
ATOM   2902 C  CB  . LEU C 1 106 ? 18.727  5.492   30.299  1.00 36.00 ? 106 LEU C CB  1 
ATOM   2903 C  CG  . LEU C 1 106 ? 20.047  5.508   31.089  1.00 36.13 ? 106 LEU C CG  1 
ATOM   2904 C  CD1 . LEU C 1 106 ? 20.618  4.115   31.171  1.00 36.68 ? 106 LEU C CD1 1 
ATOM   2905 C  CD2 . LEU C 1 106 ? 21.075  6.459   30.499  1.00 36.89 ? 106 LEU C CD2 1 
ATOM   2906 N  N   . SER C 1 107 ? 15.653  7.136   29.819  1.00 36.50 ? 107 SER C N   1 
ATOM   2907 C  CA  . SER C 1 107 ? 14.385  7.098   29.093  1.00 36.78 ? 107 SER C CA  1 
ATOM   2908 C  C   . SER C 1 107 ? 13.526  8.320   29.427  1.00 36.88 ? 107 SER C C   1 
ATOM   2909 O  O   . SER C 1 107 ? 13.860  9.109   30.307  1.00 35.92 ? 107 SER C O   1 
ATOM   2910 C  CB  . SER C 1 107 ? 13.631  5.797   29.397  1.00 37.06 ? 107 SER C CB  1 
ATOM   2911 O  OG  . SER C 1 107 ? 13.295  5.685   30.773  1.00 36.27 ? 107 SER C OG  1 
ATOM   2912 N  N   . GLY C 1 108 ? 12.426  8.475   28.700  1.00 37.59 ? 108 GLY C N   1 
ATOM   2913 C  CA  . GLY C 1 108 ? 11.536  9.618   28.876  1.00 38.60 ? 108 GLY C CA  1 
ATOM   2914 C  C   . GLY C 1 108 ? 11.918  10.738  27.934  1.00 39.47 ? 108 GLY C C   1 
ATOM   2915 O  O   . GLY C 1 108 ? 12.959  10.671  27.281  1.00 40.12 ? 108 GLY C O   1 
ATOM   2916 N  N   . ASP C 1 109 ? 11.084  11.775  27.878  1.00 40.23 ? 109 ASP C N   1 
ATOM   2917 C  CA  . ASP C 1 109 ? 11.308  12.914  26.973  1.00 40.58 ? 109 ASP C CA  1 
ATOM   2918 C  C   . ASP C 1 109 ? 12.647  13.627  27.180  1.00 40.66 ? 109 ASP C C   1 
ATOM   2919 O  O   . ASP C 1 109 ? 13.169  14.245  26.250  1.00 41.37 ? 109 ASP C O   1 
ATOM   2920 C  CB  . ASP C 1 109 ? 10.159  13.925  27.083  1.00 40.88 ? 109 ASP C CB  1 
ATOM   2921 C  CG  . ASP C 1 109 ? 8.889   13.441  26.408  1.00 41.53 ? 109 ASP C CG  1 
ATOM   2922 O  OD1 . ASP C 1 109 ? 8.984   12.705  25.400  1.00 44.18 ? 109 ASP C OD1 1 
ATOM   2923 O  OD2 . ASP C 1 109 ? 7.791   13.803  26.875  1.00 42.19 ? 109 ASP C OD2 1 
ATOM   2924 N  N   . HIS C 1 110 ? 13.207  13.538  28.383  1.00 40.63 ? 110 HIS C N   1 
ATOM   2925 C  CA  . HIS C 1 110 ? 14.462  14.219  28.690  1.00 40.04 ? 110 HIS C CA  1 
ATOM   2926 C  C   . HIS C 1 110 ? 15.681  13.280  28.794  1.00 39.83 ? 110 HIS C C   1 
ATOM   2927 O  O   . HIS C 1 110 ? 16.738  13.694  29.265  1.00 40.11 ? 110 HIS C O   1 
ATOM   2928 C  CB  . HIS C 1 110 ? 14.297  15.027  29.973  1.00 40.81 ? 110 HIS C CB  1 
ATOM   2929 C  CG  . HIS C 1 110 ? 13.195  16.038  29.914  1.00 41.92 ? 110 HIS C CG  1 
ATOM   2930 N  ND1 . HIS C 1 110 ? 13.082  16.959  28.894  1.00 43.47 ? 110 HIS C ND1 1 
ATOM   2931 C  CD2 . HIS C 1 110 ? 12.163  16.281  30.755  1.00 42.11 ? 110 HIS C CD2 1 
ATOM   2932 C  CE1 . HIS C 1 110 ? 12.023  17.720  29.106  1.00 42.28 ? 110 HIS C CE1 1 
ATOM   2933 N  NE2 . HIS C 1 110 ? 11.451  17.332  30.231  1.00 42.74 ? 110 HIS C NE2 1 
ATOM   2934 N  N   . ALA C 1 111 ? 15.541  12.037  28.328  1.00 38.78 ? 111 ALA C N   1 
ATOM   2935 C  CA  . ALA C 1 111 ? 16.619  11.048  28.324  1.00 37.67 ? 111 ALA C CA  1 
ATOM   2936 C  C   . ALA C 1 111 ? 17.921  11.606  27.749  1.00 36.89 ? 111 ALA C C   1 
ATOM   2937 O  O   . ALA C 1 111 ? 17.884  12.476  26.882  1.00 37.01 ? 111 ALA C O   1 
ATOM   2938 C  CB  . ALA C 1 111 ? 16.197  9.839   27.511  1.00 37.33 ? 111 ALA C CB  1 
ATOM   2939 N  N   . ILE C 1 112 ? 19.052  11.072  28.211  1.00 36.26 ? 112 ILE C N   1 
ATOM   2940 C  CA  . ILE C 1 112 ? 20.381  11.482  27.711  1.00 36.10 ? 112 ILE C CA  1 
ATOM   2941 C  C   . ILE C 1 112 ? 20.890  10.620  26.558  1.00 35.97 ? 112 ILE C C   1 
ATOM   2942 O  O   . ILE C 1 112 ? 21.961  10.883  26.012  1.00 35.44 ? 112 ILE C O   1 
ATOM   2943 C  CB  . ILE C 1 112 ? 21.453  11.519  28.837  1.00 35.69 ? 112 ILE C CB  1 
ATOM   2944 C  CG1 . ILE C 1 112 ? 21.673  10.123  29.452  1.00 36.20 ? 112 ILE C CG1 1 
ATOM   2945 C  CG2 . ILE C 1 112 ? 21.057  12.571  29.859  1.00 35.50 ? 112 ILE C CG2 1 
ATOM   2946 C  CD1 . ILE C 1 112 ? 22.815  10.019  30.461  1.00 36.50 ? 112 ILE C CD1 1 
ATOM   2947 N  N   . ILE C 1 113 ? 20.125  9.593   26.196  1.00 36.24 ? 113 ILE C N   1 
ATOM   2948 C  CA  . ILE C 1 113 ? 20.406  8.792   25.000  1.00 36.14 ? 113 ILE C CA  1 
ATOM   2949 C  C   . ILE C 1 113 ? 20.400  9.697   23.777  1.00 35.80 ? 113 ILE C C   1 
ATOM   2950 O  O   . ILE C 1 113 ? 19.466  10.471  23.573  1.00 36.08 ? 113 ILE C O   1 
ATOM   2951 C  CB  . ILE C 1 113 ? 19.354  7.675   24.780  1.00 36.83 ? 113 ILE C CB  1 
ATOM   2952 C  CG1 . ILE C 1 113 ? 19.272  6.746   25.991  1.00 37.32 ? 113 ILE C CG1 1 
ATOM   2953 C  CG2 . ILE C 1 113 ? 19.661  6.870   23.515  1.00 36.68 ? 113 ILE C CG2 1 
ATOM   2954 C  CD1 . ILE C 1 113 ? 20.514  6.017   26.307  1.00 36.51 ? 113 ILE C CD1 1 
ATOM   2955 N  N   . GLY C 1 114 ? 21.453  9.595   22.966  1.00 35.36 ? 114 GLY C N   1 
ATOM   2956 C  CA  . GLY C 1 114 ? 21.588  10.392  21.759  1.00 35.41 ? 114 GLY C CA  1 
ATOM   2957 C  C   . GLY C 1 114 ? 22.207  11.753  22.015  1.00 35.19 ? 114 GLY C C   1 
ATOM   2958 O  O   . GLY C 1 114 ? 22.324  12.567  21.102  1.00 35.27 ? 114 GLY C O   1 
ATOM   2959 N  N   . ARG C 1 115 ? 22.602  12.016  23.259  1.00 34.65 ? 115 ARG C N   1 
ATOM   2960 C  CA  . ARG C 1 115 ? 23.254  13.282  23.580  1.00 34.94 ? 115 ARG C CA  1 
ATOM   2961 C  C   . ARG C 1 115 ? 24.736  12.982  23.797  1.00 34.96 ? 115 ARG C C   1 
ATOM   2962 O  O   . ARG C 1 115 ? 25.167  11.860  23.549  1.00 35.27 ? 115 ARG C O   1 
ATOM   2963 C  CB  . ARG C 1 115 ? 22.575  13.947  24.775  1.00 34.81 ? 115 ARG C CB  1 
ATOM   2964 C  CG  . ARG C 1 115 ? 21.062  13.997  24.602  1.00 34.33 ? 115 ARG C CG  1 
ATOM   2965 C  CD  . ARG C 1 115 ? 20.380  14.968  25.533  1.00 35.31 ? 115 ARG C CD  1 
ATOM   2966 N  NE  . ARG C 1 115 ? 18.924  15.010  25.326  1.00 35.72 ? 115 ARG C NE  1 
ATOM   2967 C  CZ  . ARG C 1 115 ? 18.283  15.802  24.463  1.00 34.73 ? 115 ARG C CZ  1 
ATOM   2968 N  NH1 . ARG C 1 115 ? 18.935  16.655  23.675  1.00 35.55 ? 115 ARG C NH1 1 
ATOM   2969 N  NH2 . ARG C 1 115 ? 16.958  15.745  24.383  1.00 35.79 ? 115 ARG C NH2 1 
ATOM   2970 N  N   . THR C 1 116 ? 25.514  13.967  24.225  1.00 34.61 ? 116 THR C N   1 
ATOM   2971 C  CA  . THR C 1 116 ? 26.962  13.811  24.276  1.00 34.38 ? 116 THR C CA  1 
ATOM   2972 C  C   . THR C 1 116 ? 27.495  13.965  25.692  1.00 34.24 ? 116 THR C C   1 
ATOM   2973 O  O   . THR C 1 116 ? 27.147  14.905  26.391  1.00 34.14 ? 116 THR C O   1 
ATOM   2974 C  CB  . THR C 1 116 ? 27.665  14.819  23.355  1.00 33.97 ? 116 THR C CB  1 
ATOM   2975 O  OG1 . THR C 1 116 ? 27.304  14.548  21.998  1.00 34.73 ? 116 THR C OG1 1 
ATOM   2976 C  CG2 . THR C 1 116 ? 29.177  14.721  23.482  1.00 34.73 ? 116 THR C CG2 1 
ATOM   2977 N  N   . LEU C 1 117 ? 28.334  13.016  26.090  1.00 33.93 ? 117 LEU C N   1 
ATOM   2978 C  CA  . LEU C 1 117 ? 29.096  13.102  27.336  1.00 33.68 ? 117 LEU C CA  1 
ATOM   2979 C  C   . LEU C 1 117 ? 30.437  13.750  27.046  1.00 33.58 ? 117 LEU C C   1 
ATOM   2980 O  O   . LEU C 1 117 ? 31.155  13.315  26.144  1.00 32.53 ? 117 LEU C O   1 
ATOM   2981 C  CB  . LEU C 1 117 ? 29.334  11.702  27.888  1.00 33.92 ? 117 LEU C CB  1 
ATOM   2982 C  CG  . LEU C 1 117 ? 30.046  11.621  29.239  1.00 34.44 ? 117 LEU C CG  1 
ATOM   2983 C  CD1 . LEU C 1 117 ? 29.208  12.188  30.359  1.00 36.64 ? 117 LEU C CD1 1 
ATOM   2984 C  CD2 . LEU C 1 117 ? 30.417  10.182  29.542  1.00 34.94 ? 117 LEU C CD2 1 
ATOM   2985 N  N   . VAL C 1 118 ? 30.766  14.799  27.803  1.00 33.54 ? 118 VAL C N   1 
ATOM   2986 C  CA  . VAL C 1 118 ? 32.024  15.544  27.605  1.00 33.57 ? 118 VAL C CA  1 
ATOM   2987 C  C   . VAL C 1 118 ? 32.835  15.600  28.899  1.00 33.72 ? 118 VAL C C   1 
ATOM   2988 O  O   . VAL C 1 118 ? 32.279  15.856  29.963  1.00 33.55 ? 118 VAL C O   1 
ATOM   2989 C  CB  . VAL C 1 118 ? 31.739  17.000  27.141  1.00 33.01 ? 118 VAL C CB  1 
ATOM   2990 C  CG1 . VAL C 1 118 ? 33.042  17.782  26.901  1.00 33.03 ? 118 VAL C CG1 1 
ATOM   2991 C  CG2 . VAL C 1 118 ? 30.877  17.006  25.873  1.00 32.19 ? 118 VAL C CG2 1 
ATOM   2992 N  N   . VAL C 1 119 ? 34.145  15.370  28.788  1.00 34.44 ? 119 VAL C N   1 
ATOM   2993 C  CA  . VAL C 1 119 ? 35.076  15.599  29.889  1.00 35.12 ? 119 VAL C CA  1 
ATOM   2994 C  C   . VAL C 1 119 ? 35.875  16.863  29.580  1.00 35.47 ? 119 VAL C C   1 
ATOM   2995 O  O   . VAL C 1 119 ? 36.409  17.026  28.472  1.00 34.88 ? 119 VAL C O   1 
ATOM   2996 C  CB  . VAL C 1 119 ? 36.006  14.380  30.173  1.00 35.60 ? 119 VAL C CB  1 
ATOM   2997 C  CG1 . VAL C 1 119 ? 36.899  14.048  28.997  1.00 36.78 ? 119 VAL C CG1 1 
ATOM   2998 C  CG2 . VAL C 1 119 ? 36.847  14.636  31.446  1.00 35.19 ? 119 VAL C CG2 1 
ATOM   2999 N  N   . HIS C 1 120 ? 35.942  17.756  30.564  1.00 35.94 ? 120 HIS C N   1 
ATOM   3000 C  CA  . HIS C 1 120 ? 36.479  19.093  30.359  1.00 36.72 ? 120 HIS C CA  1 
ATOM   3001 C  C   . HIS C 1 120 ? 37.889  19.249  30.920  1.00 37.29 ? 120 HIS C C   1 
ATOM   3002 O  O   . HIS C 1 120 ? 38.328  18.487  31.780  1.00 36.90 ? 120 HIS C O   1 
ATOM   3003 C  CB  . HIS C 1 120 ? 35.543  20.125  30.985  1.00 36.46 ? 120 HIS C CB  1 
ATOM   3004 C  CG  . HIS C 1 120 ? 34.220  20.235  30.294  1.00 36.45 ? 120 HIS C CG  1 
ATOM   3005 N  ND1 . HIS C 1 120 ? 33.896  21.291  29.469  1.00 35.85 ? 120 HIS C ND1 1 
ATOM   3006 C  CD2 . HIS C 1 120 ? 33.137  19.423  30.310  1.00 35.58 ? 120 HIS C CD2 1 
ATOM   3007 C  CE1 . HIS C 1 120 ? 32.667  21.128  29.013  1.00 35.83 ? 120 HIS C CE1 1 
ATOM   3008 N  NE2 . HIS C 1 120 ? 32.188  19.996  29.498  1.00 35.35 ? 120 HIS C NE2 1 
ATOM   3009 N  N   . GLU C 1 121 ? 38.585  20.254  30.406  1.00 38.42 ? 121 GLU C N   1 
ATOM   3010 C  CA  . GLU C 1 121 ? 39.965  20.542  30.785  1.00 39.17 ? 121 GLU C CA  1 
ATOM   3011 C  C   . GLU C 1 121 ? 40.096  20.822  32.282  1.00 39.75 ? 121 GLU C C   1 
ATOM   3012 O  O   . GLU C 1 121 ? 40.985  20.283  32.951  1.00 40.05 ? 121 GLU C O   1 
ATOM   3013 C  CB  . GLU C 1 121 ? 40.445  21.747  29.981  1.00 38.94 ? 121 GLU C CB  1 
ATOM   3014 C  CG  . GLU C 1 121 ? 41.942  21.951  29.932  1.00 39.58 ? 121 GLU C CG  1 
ATOM   3015 C  CD  . GLU C 1 121 ? 42.301  23.183  29.129  1.00 40.99 ? 121 GLU C CD  1 
ATOM   3016 O  OE1 . GLU C 1 121 ? 41.676  24.243  29.364  1.00 43.69 ? 121 GLU C OE1 1 
ATOM   3017 O  OE2 . GLU C 1 121 ? 43.211  23.103  28.270  1.00 45.85 ? 121 GLU C OE2 1 
ATOM   3018 N  N   . LYS C 1 122 ? 39.203  21.661  32.803  1.00 40.29 ? 122 LYS C N   1 
ATOM   3019 C  CA  . LYS C 1 122 ? 39.296  22.126  34.182  1.00 40.95 ? 122 LYS C CA  1 
ATOM   3020 C  C   . LYS C 1 122 ? 38.120  21.639  35.011  1.00 41.55 ? 122 LYS C C   1 
ATOM   3021 O  O   . LYS C 1 122 ? 37.104  21.201  34.467  1.00 40.73 ? 122 LYS C O   1 
ATOM   3022 C  CB  . LYS C 1 122 ? 39.354  23.652  34.205  1.00 41.10 ? 122 LYS C CB  1 
ATOM   3023 C  CG  . LYS C 1 122 ? 40.568  24.228  33.477  1.00 41.02 ? 122 LYS C CG  1 
ATOM   3024 C  CD  . LYS C 1 122 ? 40.446  25.731  33.281  1.00 41.30 ? 122 LYS C CD  1 
ATOM   3025 C  CE  . LYS C 1 122 ? 41.695  26.293  32.622  1.00 41.44 ? 122 LYS C CE  1 
ATOM   3026 N  NZ  . LYS C 1 122 ? 41.745  27.784  32.662  1.00 42.09 ? 122 LYS C NZ  1 
ATOM   3027 N  N   . ALA C 1 123 ? 38.268  21.704  36.333  1.00 42.47 ? 123 ALA C N   1 
ATOM   3028 C  CA  . ALA C 1 123 ? 37.145  21.450  37.236  1.00 43.17 ? 123 ALA C CA  1 
ATOM   3029 C  C   . ALA C 1 123 ? 36.121  22.566  37.059  1.00 43.90 ? 123 ALA C C   1 
ATOM   3030 O  O   . ALA C 1 123 ? 36.490  23.740  36.958  1.00 44.22 ? 123 ALA C O   1 
ATOM   3031 C  CB  . ALA C 1 123 ? 37.620  21.394  38.673  1.00 43.26 ? 123 ALA C CB  1 
ATOM   3032 N  N   . ASP C 1 124 ? 34.841  22.209  37.024  1.00 44.96 ? 124 ASP C N   1 
ATOM   3033 C  CA  . ASP C 1 124 ? 33.788  23.195  36.774  1.00 45.50 ? 124 ASP C CA  1 
ATOM   3034 C  C   . ASP C 1 124 ? 33.530  24.033  38.022  1.00 45.79 ? 124 ASP C C   1 
ATOM   3035 O  O   . ASP C 1 124 ? 33.642  25.261  37.997  1.00 46.30 ? 124 ASP C O   1 
ATOM   3036 C  CB  . ASP C 1 124 ? 32.496  22.514  36.320  1.00 46.18 ? 124 ASP C CB  1 
ATOM   3037 C  CG  . ASP C 1 124 ? 31.817  21.766  37.439  1.00 48.06 ? 124 ASP C CG  1 
ATOM   3038 O  OD1 . ASP C 1 124 ? 32.441  20.820  37.969  1.00 50.99 ? 124 ASP C OD1 1 
ATOM   3039 O  OD2 . ASP C 1 124 ? 30.672  22.129  37.797  1.00 51.33 ? 124 ASP C OD2 1 
ATOM   3040 N  N   . SER C 1 142 ? 38.297  24.207  27.956  1.00 39.38 ? 142 SER C N   1 
ATOM   3041 C  CA  . SER C 1 142 ? 38.288  23.426  26.726  1.00 38.75 ? 142 SER C CA  1 
ATOM   3042 C  C   . SER C 1 142 ? 37.681  22.046  26.953  1.00 38.59 ? 142 SER C C   1 
ATOM   3043 O  O   . SER C 1 142 ? 37.677  21.534  28.072  1.00 39.03 ? 142 SER C O   1 
ATOM   3044 C  CB  . SER C 1 142 ? 39.714  23.297  26.178  1.00 39.03 ? 142 SER C CB  1 
ATOM   3045 O  OG  . SER C 1 142 ? 39.800  22.297  25.179  1.00 39.87 ? 142 SER C OG  1 
ATOM   3046 N  N   . ARG C 1 143 ? 37.161  21.458  25.877  1.00 37.74 ? 143 ARG C N   1 
ATOM   3047 C  CA  . ARG C 1 143 ? 36.557  20.135  25.914  1.00 37.41 ? 143 ARG C CA  1 
ATOM   3048 C  C   . ARG C 1 143 ? 37.569  19.107  25.440  1.00 37.09 ? 143 ARG C C   1 
ATOM   3049 O  O   . ARG C 1 143 ? 37.992  19.147  24.289  1.00 37.62 ? 143 ARG C O   1 
ATOM   3050 C  CB  . ARG C 1 143 ? 35.311  20.101  25.027  1.00 37.24 ? 143 ARG C CB  1 
ATOM   3051 C  CG  . ARG C 1 143 ? 34.288  21.137  25.436  1.00 37.29 ? 143 ARG C CG  1 
ATOM   3052 C  CD  . ARG C 1 143 ? 33.026  21.109  24.602  1.00 37.12 ? 143 ARG C CD  1 
ATOM   3053 N  NE  . ARG C 1 143 ? 32.148  22.201  25.012  1.00 36.57 ? 143 ARG C NE  1 
ATOM   3054 C  CZ  . ARG C 1 143 ? 30.913  22.409  24.568  1.00 36.48 ? 143 ARG C CZ  1 
ATOM   3055 N  NH1 . ARG C 1 143 ? 30.367  21.604  23.666  1.00 36.31 ? 143 ARG C NH1 1 
ATOM   3056 N  NH2 . ARG C 1 143 ? 30.225  23.446  25.033  1.00 36.55 ? 143 ARG C NH2 1 
ATOM   3057 N  N   . LEU C 1 144 ? 37.939  18.181  26.319  1.00 36.52 ? 144 LEU C N   1 
ATOM   3058 C  CA  . LEU C 1 144 ? 39.058  17.281  26.062  1.00 36.50 ? 144 LEU C CA  1 
ATOM   3059 C  C   . LEU C 1 144 ? 38.666  16.084  25.225  1.00 36.04 ? 144 LEU C C   1 
ATOM   3060 O  O   . LEU C 1 144 ? 39.421  15.656  24.359  1.00 35.49 ? 144 LEU C O   1 
ATOM   3061 C  CB  . LEU C 1 144 ? 39.664  16.785  27.374  1.00 36.70 ? 144 LEU C CB  1 
ATOM   3062 C  CG  . LEU C 1 144 ? 40.249  17.824  28.329  1.00 37.40 ? 144 LEU C CG  1 
ATOM   3063 C  CD1 . LEU C 1 144 ? 40.686  17.118  29.603  1.00 37.57 ? 144 LEU C CD1 1 
ATOM   3064 C  CD2 . LEU C 1 144 ? 41.404  18.565  27.695  1.00 38.13 ? 144 LEU C CD2 1 
ATOM   3065 N  N   . ALA C 1 145 ? 37.493  15.525  25.508  1.00 35.65 ? 145 ALA C N   1 
ATOM   3066 C  CA  . ALA C 1 145 ? 37.017  14.358  24.790  1.00 35.76 ? 145 ALA C CA  1 
ATOM   3067 C  C   . ALA C 1 145 ? 35.521  14.249  24.940  1.00 35.35 ? 145 ALA C C   1 
ATOM   3068 O  O   . ALA C 1 145 ? 34.939  14.805  25.866  1.00 34.90 ? 145 ALA C O   1 
ATOM   3069 C  CB  . ALA C 1 145 ? 37.682  13.095  25.306  1.00 35.67 ? 145 ALA C CB  1 
ATOM   3070 N  N   . CYS C 1 146 ? 34.905  13.527  24.018  1.00 35.67 ? 146 CYS C N   1 
ATOM   3071 C  CA  . CYS C 1 146 ? 33.462  13.360  24.051  1.00 35.76 ? 146 CYS C CA  1 
ATOM   3072 C  C   . CYS C 1 146 ? 33.011  12.103  23.321  1.00 35.32 ? 146 CYS C C   1 
ATOM   3073 O  O   . CYS C 1 146 ? 33.768  11.479  22.587  1.00 34.68 ? 146 CYS C O   1 
ATOM   3074 C  CB  . CYS C 1 146 ? 32.785  14.598  23.463  1.00 36.53 ? 146 CYS C CB  1 
ATOM   3075 S  SG  . CYS C 1 146 ? 33.329  15.093  21.811  1.00 39.85 ? 146 CYS C SG  1 
ATOM   3076 N  N   . GLY C 1 147 ? 31.760  11.733  23.538  1.00 35.15 ? 147 GLY C N   1 
ATOM   3077 C  CA  . GLY C 1 147 ? 31.190  10.565  22.878  1.00 35.07 ? 147 GLY C CA  1 
ATOM   3078 C  C   . GLY C 1 147 ? 29.683  10.663  22.923  1.00 34.69 ? 147 GLY C C   1 
ATOM   3079 O  O   . GLY C 1 147 ? 29.136  11.154  23.905  1.00 35.05 ? 147 GLY C O   1 
ATOM   3080 N  N   . VAL C 1 148 ? 29.020  10.234  21.855  1.00 34.97 ? 148 VAL C N   1 
ATOM   3081 C  CA  . VAL C 1 148 ? 27.556  10.211  21.856  1.00 35.40 ? 148 VAL C CA  1 
ATOM   3082 C  C   . VAL C 1 148 ? 27.126  9.062   22.758  1.00 35.42 ? 148 VAL C C   1 
ATOM   3083 O  O   . VAL C 1 148 ? 27.700  7.977   22.697  1.00 36.42 ? 148 VAL C O   1 
ATOM   3084 C  CB  . VAL C 1 148 ? 26.974  10.020  20.448  1.00 35.62 ? 148 VAL C CB  1 
ATOM   3085 C  CG1 . VAL C 1 148 ? 25.460  10.006  20.513  1.00 36.03 ? 148 VAL C CG1 1 
ATOM   3086 C  CG2 . VAL C 1 148 ? 27.462  11.128  19.510  1.00 36.52 ? 148 VAL C CG2 1 
ATOM   3087 N  N   . ILE C 1 149 ? 26.105  9.300   23.578  1.00 35.73 ? 149 ILE C N   1 
ATOM   3088 C  CA  . ILE C 1 149 ? 25.592  8.286   24.503  1.00 36.00 ? 149 ILE C CA  1 
ATOM   3089 C  C   . ILE C 1 149 ? 24.642  7.358   23.761  1.00 36.06 ? 149 ILE C C   1 
ATOM   3090 O  O   . ILE C 1 149 ? 23.566  7.774   23.318  1.00 36.01 ? 149 ILE C O   1 
ATOM   3091 C  CB  . ILE C 1 149 ? 24.892  8.948   25.716  1.00 36.17 ? 149 ILE C CB  1 
ATOM   3092 C  CG1 . ILE C 1 149 ? 25.889  9.837   26.479  1.00 36.13 ? 149 ILE C CG1 1 
ATOM   3093 C  CG2 . ILE C 1 149 ? 24.304  7.895   26.662  1.00 36.14 ? 149 ILE C CG2 1 
ATOM   3094 C  CD1 . ILE C 1 149 ? 25.238  10.869  27.358  1.00 36.31 ? 149 ILE C CD1 1 
ATOM   3095 N  N   . GLY C 1 150 ? 25.034  6.089   23.622  1.00 35.85 ? 150 GLY C N   1 
ATOM   3096 C  CA  . GLY C 1 150 ? 24.289  5.142   22.818  1.00 35.92 ? 150 GLY C CA  1 
ATOM   3097 C  C   . GLY C 1 150 ? 23.656  4.022   23.614  1.00 35.83 ? 150 GLY C C   1 
ATOM   3098 O  O   . GLY C 1 150 ? 24.075  3.726   24.725  1.00 35.04 ? 150 GLY C O   1 
ATOM   3099 N  N   . ILE C 1 151 ? 22.633  3.407   23.028  1.00 35.81 ? 151 ILE C N   1 
ATOM   3100 C  CA  . ILE C 1 151 ? 21.952  2.276   23.617  1.00 35.86 ? 151 ILE C CA  1 
ATOM   3101 C  C   . ILE C 1 151 ? 22.911  1.088   23.633  1.00 36.11 ? 151 ILE C C   1 
ATOM   3102 O  O   . ILE C 1 151 ? 23.503  0.740   22.603  1.00 34.66 ? 151 ILE C O   1 
ATOM   3103 C  CB  . ILE C 1 151 ? 20.659  1.931   22.813  1.00 35.58 ? 151 ILE C CB  1 
ATOM   3104 C  CG1 . ILE C 1 151 ? 19.644  3.076   22.923  1.00 35.69 ? 151 ILE C CG1 1 
ATOM   3105 C  CG2 . ILE C 1 151 ? 20.055  0.623   23.287  1.00 35.99 ? 151 ILE C CG2 1 
ATOM   3106 C  CD1 . ILE C 1 151 ? 18.449  2.941   22.022  1.00 36.17 ? 151 ILE C CD1 1 
ATOM   3107 N  N   . ALA C 1 152 ? 23.064  0.476   24.810  1.00 36.43 ? 152 ALA C N   1 
ATOM   3108 C  CA  . ALA C 1 152 ? 23.928  -0.683  24.976  1.00 37.17 ? 152 ALA C CA  1 
ATOM   3109 C  C   . ALA C 1 152 ? 23.090  -1.921  25.253  1.00 37.67 ? 152 ALA C C   1 
ATOM   3110 O  O   . ALA C 1 152 ? 21.954  -1.830  25.728  1.00 37.98 ? 152 ALA C O   1 
ATOM   3111 C  CB  . ALA C 1 152 ? 24.929  -0.450  26.120  1.00 37.10 ? 152 ALA C CB  1 
ATOM   3112 N  N   . GLN C 1 153 ? 23.662  -3.075  24.930  1.00 38.35 ? 153 GLN C N   1 
ATOM   3113 C  CA  . GLN C 1 153 ? 23.024  -4.363  25.146  1.00 38.73 ? 153 GLN C CA  1 
ATOM   3114 C  C   . GLN C 1 153 ? 22.975  -4.649  26.633  1.00 39.46 ? 153 GLN C C   1 
ATOM   3115 O  O   . GLN C 1 153 ? 21.900  -4.885  27.173  1.00 40.13 ? 153 GLN C O   1 
ATOM   3116 C  CB  . GLN C 1 153 ? 23.811  -5.456  24.429  1.00 38.78 ? 153 GLN C CB  1 
ATOM   3117 C  CG  . GLN C 1 153 ? 23.154  -6.831  24.425  1.00 38.67 ? 153 GLN C CG  1 
ATOM   3118 C  CD  . GLN C 1 153 ? 23.779  -7.761  23.402  1.00 38.74 ? 153 GLN C CD  1 
ATOM   3119 O  OE1 . GLN C 1 153 ? 23.081  -8.384  22.607  1.00 39.81 ? 153 GLN C OE1 1 
ATOM   3120 N  NE2 . GLN C 1 153 ? 25.104  -7.850  23.411  1.00 39.08 ? 153 GLN C NE2 1 
ATOM   3121 O  OXT . GLN C 1 153 ? 24.002  -4.634  27.318  1.00 40.25 ? 153 GLN C OXT 1 
ATOM   3122 N  N   . THR D 1 2   ? 13.356  15.863  16.000  1.00 38.43 ? 2   THR D N   1 
ATOM   3123 C  CA  . THR D 1 2   ? 13.089  16.053  14.539  1.00 38.00 ? 2   THR D CA  1 
ATOM   3124 C  C   . THR D 1 2   ? 14.344  15.942  13.671  1.00 37.47 ? 2   THR D C   1 
ATOM   3125 O  O   . THR D 1 2   ? 14.228  15.666  12.481  1.00 36.81 ? 2   THR D O   1 
ATOM   3126 C  CB  . THR D 1 2   ? 12.377  17.403  14.216  1.00 38.57 ? 2   THR D CB  1 
ATOM   3127 O  OG1 . THR D 1 2   ? 13.248  18.513  14.486  1.00 40.72 ? 2   THR D OG1 1 
ATOM   3128 C  CG2 . THR D 1 2   ? 11.089  17.560  15.017  1.00 38.59 ? 2   THR D CG2 1 
ATOM   3129 N  N   . LYS D 1 3   ? 15.525  16.167  14.258  1.00 36.85 ? 3   LYS D N   1 
ATOM   3130 C  CA  . LYS D 1 3   ? 16.793  16.032  13.537  1.00 36.71 ? 3   LYS D CA  1 
ATOM   3131 C  C   . LYS D 1 3   ? 17.803  15.157  14.286  1.00 36.51 ? 3   LYS D C   1 
ATOM   3132 O  O   . LYS D 1 3   ? 17.873  15.187  15.524  1.00 35.84 ? 3   LYS D O   1 
ATOM   3133 C  CB  . LYS D 1 3   ? 17.400  17.417  13.262  1.00 37.05 ? 3   LYS D CB  1 
ATOM   3134 C  CG  . LYS D 1 3   ? 16.540  18.284  12.355  1.00 37.66 ? 3   LYS D CG  1 
ATOM   3135 C  CD  . LYS D 1 3   ? 17.189  19.629  12.050  1.00 37.67 ? 3   LYS D CD  1 
ATOM   3136 C  CE  . LYS D 1 3   ? 16.183  20.587  11.412  1.00 38.67 ? 3   LYS D CE  1 
ATOM   3137 N  NZ  . LYS D 1 3   ? 16.781  21.856  10.888  1.00 39.14 ? 3   LYS D NZ  1 
ATOM   3138 N  N   . ALA D 1 4   ? 18.569  14.369  13.523  1.00 35.66 ? 4   ALA D N   1 
ATOM   3139 C  CA  . ALA D 1 4   ? 19.682  13.609  14.066  1.00 35.49 ? 4   ALA D CA  1 
ATOM   3140 C  C   . ALA D 1 4   ? 20.880  13.645  13.121  1.00 35.02 ? 4   ALA D C   1 
ATOM   3141 O  O   . ALA D 1 4   ? 20.771  14.082  11.977  1.00 34.52 ? 4   ALA D O   1 
ATOM   3142 C  CB  . ALA D 1 4   ? 19.260  12.181  14.323  1.00 35.11 ? 4   ALA D CB  1 
ATOM   3143 N  N   . VAL D 1 5   ? 22.024  13.185  13.612  1.00 34.83 ? 5   VAL D N   1 
ATOM   3144 C  CA  . VAL D 1 5   ? 23.235  13.114  12.805  1.00 34.94 ? 5   VAL D CA  1 
ATOM   3145 C  C   . VAL D 1 5   ? 24.102  11.927  13.229  1.00 35.33 ? 5   VAL D C   1 
ATOM   3146 O  O   . VAL D 1 5   ? 24.128  11.533  14.409  1.00 35.20 ? 5   VAL D O   1 
ATOM   3147 C  CB  . VAL D 1 5   ? 24.031  14.451  12.878  1.00 35.21 ? 5   VAL D CB  1 
ATOM   3148 C  CG1 . VAL D 1 5   ? 24.597  14.683  14.282  1.00 35.97 ? 5   VAL D CG1 1 
ATOM   3149 C  CG2 . VAL D 1 5   ? 25.140  14.492  11.827  1.00 34.97 ? 5   VAL D CG2 1 
ATOM   3150 N  N   . ALA D 1 6   ? 24.797  11.343  12.257  1.00 35.30 ? 6   ALA D N   1 
ATOM   3151 C  CA  . ALA D 1 6   ? 25.820  10.360  12.530  1.00 34.88 ? 6   ALA D CA  1 
ATOM   3152 C  C   . ALA D 1 6   ? 27.123  10.719  11.824  1.00 34.80 ? 6   ALA D C   1 
ATOM   3153 O  O   . ALA D 1 6   ? 27.125  11.050  10.631  1.00 35.50 ? 6   ALA D O   1 
ATOM   3154 C  CB  . ALA D 1 6   ? 25.352  8.985   12.090  1.00 34.76 ? 6   ALA D CB  1 
ATOM   3155 N  N   . VAL D 1 7   ? 28.221  10.676  12.579  1.00 34.38 ? 7   VAL D N   1 
ATOM   3156 C  CA  . VAL D 1 7   ? 29.555  10.880  12.030  1.00 34.77 ? 7   VAL D CA  1 
ATOM   3157 C  C   . VAL D 1 7   ? 30.174  9.508   11.898  1.00 35.23 ? 7   VAL D C   1 
ATOM   3158 O  O   . VAL D 1 7   ? 30.369  8.822   12.902  1.00 35.69 ? 7   VAL D O   1 
ATOM   3159 C  CB  . VAL D 1 7   ? 30.436  11.754  12.933  1.00 34.60 ? 7   VAL D CB  1 
ATOM   3160 C  CG1 . VAL D 1 7   ? 31.844  11.881  12.337  1.00 33.81 ? 7   VAL D CG1 1 
ATOM   3161 C  CG2 . VAL D 1 7   ? 29.831  13.133  13.078  1.00 34.43 ? 7   VAL D CG2 1 
ATOM   3162 N  N   . LEU D 1 8   ? 30.464  9.117   10.662  1.00 35.60 ? 8   LEU D N   1 
ATOM   3163 C  CA  . LEU D 1 8   ? 30.923  7.767   10.352  1.00 35.77 ? 8   LEU D CA  1 
ATOM   3164 C  C   . LEU D 1 8   ? 32.452  7.712   10.356  1.00 35.98 ? 8   LEU D C   1 
ATOM   3165 O  O   . LEU D 1 8   ? 33.116  8.500   9.678   1.00 35.35 ? 8   LEU D O   1 
ATOM   3166 C  CB  . LEU D 1 8   ? 30.382  7.318   8.988   1.00 35.99 ? 8   LEU D CB  1 
ATOM   3167 C  CG  . LEU D 1 8   ? 28.852  7.356   8.816   1.00 36.95 ? 8   LEU D CG  1 
ATOM   3168 C  CD1 . LEU D 1 8   ? 28.460  6.959   7.393   1.00 39.06 ? 8   LEU D CD1 1 
ATOM   3169 C  CD2 . LEU D 1 8   ? 28.163  6.465   9.819   1.00 38.60 ? 8   LEU D CD2 1 
ATOM   3170 N  N   . LYS D 1 9   ? 32.992  6.780   11.136  1.00 36.24 ? 9   LYS D N   1 
ATOM   3171 C  CA  . LYS D 1 9   ? 34.431  6.535   11.207  1.00 37.10 ? 9   LYS D CA  1 
ATOM   3172 C  C   . LYS D 1 9   ? 34.676  5.042   11.358  1.00 36.90 ? 9   LYS D C   1 
ATOM   3173 O  O   . LYS D 1 9   ? 33.814  4.318   11.844  1.00 36.52 ? 9   LYS D O   1 
ATOM   3174 C  CB  . LYS D 1 9   ? 35.034  7.273   12.401  1.00 37.41 ? 9   LYS D CB  1 
ATOM   3175 C  CG  . LYS D 1 9   ? 34.982  8.787   12.288  1.00 38.54 ? 9   LYS D CG  1 
ATOM   3176 C  CD  . LYS D 1 9   ? 35.951  9.454   13.271  1.00 39.21 ? 9   LYS D CD  1 
ATOM   3177 C  CE  . LYS D 1 9   ? 36.413  10.829  12.791  1.00 40.35 ? 9   LYS D CE  1 
ATOM   3178 N  NZ  . LYS D 1 9   ? 35.364  11.874  12.941  1.00 42.02 ? 9   LYS D NZ  1 
ATOM   3179 N  N   . GLY D 1 10  ? 35.853  4.587   10.938  1.00 37.33 ? 10  GLY D N   1 
ATOM   3180 C  CA  . GLY D 1 10  ? 36.220  3.181   11.071  1.00 37.76 ? 10  GLY D CA  1 
ATOM   3181 C  C   . GLY D 1 10  ? 37.721  3.014   11.150  1.00 38.18 ? 10  GLY D C   1 
ATOM   3182 O  O   . GLY D 1 10  ? 38.442  3.980   11.399  1.00 38.36 ? 10  GLY D O   1 
ATOM   3183 N  N   . ASP D 1 11  ? 38.184  1.787   10.927  1.00 38.55 ? 11  ASP D N   1 
ATOM   3184 C  CA  . ASP D 1 11  ? 39.604  1.451   11.028  1.00 39.04 ? 11  ASP D CA  1 
ATOM   3185 C  C   . ASP D 1 11  ? 40.395  1.774   9.760   1.00 38.80 ? 11  ASP D C   1 
ATOM   3186 O  O   . ASP D 1 11  ? 41.622  1.766   9.790   1.00 39.08 ? 11  ASP D O   1 
ATOM   3187 C  CB  . ASP D 1 11  ? 39.773  -0.032  11.381  1.00 39.35 ? 11  ASP D CB  1 
ATOM   3188 C  CG  . ASP D 1 11  ? 39.248  -0.369  12.772  1.00 40.95 ? 11  ASP D CG  1 
ATOM   3189 O  OD1 . ASP D 1 11  ? 39.188  0.536   13.636  1.00 43.62 ? 11  ASP D OD1 1 
ATOM   3190 O  OD2 . ASP D 1 11  ? 38.899  -1.546  13.007  1.00 41.01 ? 11  ASP D OD2 1 
ATOM   3191 N  N   . GLY D 1 12  ? 39.695  2.047   8.659   1.00 38.56 ? 12  GLY D N   1 
ATOM   3192 C  CA  . GLY D 1 12  ? 40.320  2.394   7.384   1.00 38.43 ? 12  GLY D CA  1 
ATOM   3193 C  C   . GLY D 1 12  ? 40.046  3.839   7.000   1.00 38.26 ? 12  GLY D C   1 
ATOM   3194 O  O   . GLY D 1 12  ? 39.850  4.682   7.878   1.00 38.23 ? 12  GLY D O   1 
ATOM   3195 N  N   . PRO D 1 13  ? 40.012  4.135   5.685   1.00 37.98 ? 13  PRO D N   1 
ATOM   3196 C  CA  . PRO D 1 13  ? 39.864  5.505   5.195   1.00 37.94 ? 13  PRO D CA  1 
ATOM   3197 C  C   . PRO D 1 13  ? 38.419  6.006   5.068   1.00 37.80 ? 13  PRO D C   1 
ATOM   3198 O  O   . PRO D 1 13  ? 38.211  7.171   4.729   1.00 37.89 ? 13  PRO D O   1 
ATOM   3199 C  CB  . PRO D 1 13  ? 40.499  5.431   3.807   1.00 37.84 ? 13  PRO D CB  1 
ATOM   3200 C  CG  . PRO D 1 13  ? 40.183  4.052   3.339   1.00 37.84 ? 13  PRO D CG  1 
ATOM   3201 C  CD  . PRO D 1 13  ? 40.118  3.174   4.569   1.00 38.09 ? 13  PRO D CD  1 
ATOM   3202 N  N   . VAL D 1 14  ? 37.438  5.148   5.327   1.00 37.72 ? 14  VAL D N   1 
ATOM   3203 C  CA  . VAL D 1 14  ? 36.035  5.506   5.098   1.00 37.91 ? 14  VAL D CA  1 
ATOM   3204 C  C   . VAL D 1 14  ? 35.520  6.436   6.202   1.00 37.92 ? 14  VAL D C   1 
ATOM   3205 O  O   . VAL D 1 14  ? 35.571  6.095   7.388   1.00 37.51 ? 14  VAL D O   1 
ATOM   3206 C  CB  . VAL D 1 14  ? 35.134  4.254   4.997   1.00 37.79 ? 14  VAL D CB  1 
ATOM   3207 C  CG1 . VAL D 1 14  ? 33.678  4.647   4.751   1.00 37.69 ? 14  VAL D CG1 1 
ATOM   3208 C  CG2 . VAL D 1 14  ? 35.620  3.338   3.883   1.00 38.21 ? 14  VAL D CG2 1 
ATOM   3209 N  N   . GLN D 1 15  ? 35.045  7.615   5.808   1.00 37.96 ? 15  GLN D N   1 
ATOM   3210 C  CA  . GLN D 1 15  ? 34.473  8.563   6.763   1.00 38.44 ? 15  GLN D CA  1 
ATOM   3211 C  C   . GLN D 1 15  ? 33.400  9.440   6.123   1.00 38.11 ? 15  GLN D C   1 
ATOM   3212 O  O   . GLN D 1 15  ? 33.394  9.648   4.911   1.00 38.06 ? 15  GLN D O   1 
ATOM   3213 C  CB  . GLN D 1 15  ? 35.566  9.426   7.410   1.00 38.96 ? 15  GLN D CB  1 
ATOM   3214 C  CG  . GLN D 1 15  ? 36.372  10.287  6.457   1.00 39.72 ? 15  GLN D CG  1 
ATOM   3215 C  CD  . GLN D 1 15  ? 37.573  10.942  7.133   1.00 40.74 ? 15  GLN D CD  1 
ATOM   3216 O  OE1 . GLN D 1 15  ? 37.495  12.087  7.590   1.00 44.95 ? 15  GLN D OE1 1 
ATOM   3217 N  NE2 . GLN D 1 15  ? 38.693  10.219  7.198   1.00 42.97 ? 15  GLN D NE2 1 
ATOM   3218 N  N   . GLY D 1 16  ? 32.479  9.935   6.944   1.00 37.78 ? 16  GLY D N   1 
ATOM   3219 C  CA  . GLY D 1 16  ? 31.404  10.774  6.430   1.00 37.34 ? 16  GLY D CA  1 
ATOM   3220 C  C   . GLY D 1 16  ? 30.488  11.343  7.494   1.00 36.99 ? 16  GLY D C   1 
ATOM   3221 O  O   . GLY D 1 16  ? 30.655  11.082  8.680   1.00 36.80 ? 16  GLY D O   1 
ATOM   3222 N  N   . ILE D 1 17  ? 29.529  12.144  7.047   1.00 36.21 ? 17  ILE D N   1 
ATOM   3223 C  CA  . ILE D 1 17  ? 28.516  12.724  7.912   1.00 35.88 ? 17  ILE D CA  1 
ATOM   3224 C  C   . ILE D 1 17  ? 27.167  12.465  7.262   1.00 35.40 ? 17  ILE D C   1 
ATOM   3225 O  O   . ILE D 1 17  ? 26.988  12.744  6.071   1.00 34.82 ? 17  ILE D O   1 
ATOM   3226 C  CB  . ILE D 1 17  ? 28.745  14.244  8.073   1.00 35.60 ? 17  ILE D CB  1 
ATOM   3227 C  CG1 . ILE D 1 17  ? 30.082  14.502  8.785   1.00 36.22 ? 17  ILE D CG1 1 
ATOM   3228 C  CG2 . ILE D 1 17  ? 27.605  14.876  8.842   1.00 35.56 ? 17  ILE D CG2 1 
ATOM   3229 C  CD1 . ILE D 1 17  ? 30.567  15.922  8.676   1.00 36.51 ? 17  ILE D CD1 1 
ATOM   3230 N  N   . ILE D 1 18  ? 26.233  11.914  8.031   1.00 35.20 ? 18  ILE D N   1 
ATOM   3231 C  CA  . ILE D 1 18  ? 24.891  11.639  7.534   1.00 35.06 ? 18  ILE D CA  1 
ATOM   3232 C  C   . ILE D 1 18  ? 23.877  12.297  8.454   1.00 34.99 ? 18  ILE D C   1 
ATOM   3233 O  O   . ILE D 1 18  ? 23.928  12.127  9.677   1.00 34.46 ? 18  ILE D O   1 
ATOM   3234 C  CB  . ILE D 1 18  ? 24.595  10.123  7.461   1.00 34.90 ? 18  ILE D CB  1 
ATOM   3235 C  CG1 . ILE D 1 18  ? 25.597  9.411   6.535   1.00 35.39 ? 18  ILE D CG1 1 
ATOM   3236 C  CG2 . ILE D 1 18  ? 23.178  9.887   6.977   1.00 35.27 ? 18  ILE D CG2 1 
ATOM   3237 C  CD1 . ILE D 1 18  ? 25.473  9.775   5.052   1.00 36.07 ? 18  ILE D CD1 1 
ATOM   3238 N  N   . ASN D 1 19  ? 22.958  13.041  7.843   1.00 34.61 ? 19  ASN D N   1 
ATOM   3239 C  CA  . ASN D 1 19  ? 21.938  13.787  8.548   1.00 34.98 ? 19  ASN D CA  1 
ATOM   3240 C  C   . ASN D 1 19  ? 20.594  13.113  8.396   1.00 35.23 ? 19  ASN D C   1 
ATOM   3241 O  O   . ASN D 1 19  ? 20.322  12.510  7.358   1.00 35.48 ? 19  ASN D O   1 
ATOM   3242 C  CB  . ASN D 1 19  ? 21.863  15.194  7.968   1.00 35.12 ? 19  ASN D CB  1 
ATOM   3243 C  CG  . ASN D 1 19  ? 23.197  15.905  8.013   1.00 36.15 ? 19  ASN D CG  1 
ATOM   3244 O  OD1 . ASN D 1 19  ? 23.618  16.379  9.067   1.00 37.43 ? 19  ASN D OD1 1 
ATOM   3245 N  ND2 . ASN D 1 19  ? 23.873  15.981  6.866   1.00 37.03 ? 19  ASN D ND2 1 
ATOM   3246 N  N   . PHE D 1 20  ? 19.763  13.240  9.425   1.00 35.66 ? 20  PHE D N   1 
ATOM   3247 C  CA  . PHE D 1 20  ? 18.402  12.706  9.435   1.00 36.15 ? 20  PHE D CA  1 
ATOM   3248 C  C   . PHE D 1 20  ? 17.454  13.835  9.801   1.00 36.43 ? 20  PHE D C   1 
ATOM   3249 O  O   . PHE D 1 20  ? 17.749  14.628  10.696  1.00 36.24 ? 20  PHE D O   1 
ATOM   3250 C  CB  . PHE D 1 20  ? 18.243  11.599  10.482  1.00 36.39 ? 20  PHE D CB  1 
ATOM   3251 C  CG  . PHE D 1 20  ? 19.128  10.407  10.276  1.00 36.23 ? 20  PHE D CG  1 
ATOM   3252 C  CD1 . PHE D 1 20  ? 20.457  10.423  10.713  1.00 36.24 ? 20  PHE D CD1 1 
ATOM   3253 C  CD2 . PHE D 1 20  ? 18.631  9.245   9.694   1.00 36.40 ? 20  PHE D CD2 1 
ATOM   3254 C  CE1 . PHE D 1 20  ? 21.274  9.311   10.546  1.00 37.23 ? 20  PHE D CE1 1 
ATOM   3255 C  CE2 . PHE D 1 20  ? 19.445  8.128   9.521   1.00 36.79 ? 20  PHE D CE2 1 
ATOM   3256 C  CZ  . PHE D 1 20  ? 20.776  8.167   9.947   1.00 36.50 ? 20  PHE D CZ  1 
ATOM   3257 N  N   . GLU D 1 21  ? 16.322  13.916  9.112   1.00 36.74 ? 21  GLU D N   1 
ATOM   3258 C  CA  . GLU D 1 21  ? 15.292  14.878  9.466   1.00 37.07 ? 21  GLU D CA  1 
ATOM   3259 C  C   . GLU D 1 21  ? 13.904  14.274  9.303   1.00 36.97 ? 21  GLU D C   1 
ATOM   3260 O  O   . GLU D 1 21  ? 13.611  13.651  8.285   1.00 36.42 ? 21  GLU D O   1 
ATOM   3261 C  CB  . GLU D 1 21  ? 15.410  16.147  8.623   1.00 37.33 ? 21  GLU D CB  1 
ATOM   3262 C  CG  . GLU D 1 21  ? 14.457  17.238  9.061   1.00 37.51 ? 21  GLU D CG  1 
ATOM   3263 C  CD  . GLU D 1 21  ? 14.671  18.542  8.328   1.00 38.65 ? 21  GLU D CD  1 
ATOM   3264 O  OE1 . GLU D 1 21  ? 15.676  18.676  7.596   1.00 42.20 ? 21  GLU D OE1 1 
ATOM   3265 O  OE2 . GLU D 1 21  ? 13.824  19.443  8.478   1.00 40.80 ? 21  GLU D OE2 1 
ATOM   3266 N  N   . GLN D 1 22  ? 13.066  14.474  10.316  1.00 37.05 ? 22  GLN D N   1 
ATOM   3267 C  CA  . GLN D 1 22  ? 11.704  13.957  10.330  1.00 37.62 ? 22  GLN D CA  1 
ATOM   3268 C  C   . GLN D 1 22  ? 10.749  15.089  10.692  1.00 38.19 ? 22  GLN D C   1 
ATOM   3269 O  O   . GLN D 1 22  ? 10.695  15.525  11.842  1.00 38.16 ? 22  GLN D O   1 
ATOM   3270 C  CB  . GLN D 1 22  ? 11.588  12.804  11.326  1.00 37.31 ? 22  GLN D CB  1 
ATOM   3271 C  CG  . GLN D 1 22  ? 10.249  12.081  11.290  1.00 37.13 ? 22  GLN D CG  1 
ATOM   3272 C  CD  . GLN D 1 22  ? 10.204  10.886  12.216  1.00 37.00 ? 22  GLN D CD  1 
ATOM   3273 O  OE1 . GLN D 1 22  ? 10.766  10.914  13.308  1.00 36.61 ? 22  GLN D OE1 1 
ATOM   3274 N  NE2 . GLN D 1 22  ? 9.532   9.826   11.783  1.00 36.34 ? 22  GLN D NE2 1 
ATOM   3275 N  N   . LYS D 1 23  ? 10.010  15.560  9.690   1.00 39.03 ? 23  LYS D N   1 
ATOM   3276 C  CA  . LYS D 1 23  ? 9.105   16.706  9.827   1.00 39.80 ? 23  LYS D CA  1 
ATOM   3277 C  C   . LYS D 1 23  ? 7.960   16.477  10.808  1.00 40.20 ? 23  LYS D C   1 
ATOM   3278 O  O   . LYS D 1 23  ? 7.556   17.405  11.505  1.00 40.45 ? 23  LYS D O   1 
ATOM   3279 C  CB  . LYS D 1 23  ? 8.506   17.074  8.466   1.00 40.06 ? 23  LYS D CB  1 
ATOM   3280 C  CG  . LYS D 1 23  ? 9.458   17.770  7.506   1.00 40.51 ? 23  LYS D CG  1 
ATOM   3281 C  CD  . LYS D 1 23  ? 8.789   17.964  6.142   1.00 40.71 ? 23  LYS D CD  1 
ATOM   3282 C  CE  . LYS D 1 23  ? 9.685   18.694  5.144   1.00 41.33 ? 23  LYS D CE  1 
ATOM   3283 N  NZ  . LYS D 1 23  ? 9.391   20.154  5.078   1.00 42.49 ? 23  LYS D NZ  1 
ATOM   3284 N  N   . GLU D 1 24  ? 7.423   15.259  10.844  1.00 40.64 ? 24  GLU D N   1 
ATOM   3285 C  CA  . GLU D 1 24  ? 6.270   14.948  11.694  1.00 41.14 ? 24  GLU D CA  1 
ATOM   3286 C  C   . GLU D 1 24  ? 6.406   13.568  12.329  1.00 41.32 ? 24  GLU D C   1 
ATOM   3287 O  O   . GLU D 1 24  ? 7.088   12.699  11.796  1.00 41.32 ? 24  GLU D O   1 
ATOM   3288 C  CB  . GLU D 1 24  ? 4.962   15.055  10.899  1.00 41.43 ? 24  GLU D CB  1 
ATOM   3289 C  CG  . GLU D 1 24  ? 4.953   14.267  9.597   1.00 41.88 ? 24  GLU D CG  1 
ATOM   3290 C  CD  . GLU D 1 24  ? 3.570   14.129  8.974   1.00 42.12 ? 24  GLU D CD  1 
ATOM   3291 O  OE1 . GLU D 1 24  ? 2.632   14.851  9.385   1.00 43.82 ? 24  GLU D OE1 1 
ATOM   3292 O  OE2 . GLU D 1 24  ? 3.426   13.291  8.054   1.00 43.34 ? 24  GLU D OE2 1 
ATOM   3293 N  N   . SER D 1 25  ? 5.726   13.383  13.458  1.00 41.65 ? 25  SER D N   1 
ATOM   3294 C  CA  . SER D 1 25  ? 5.962   12.258  14.376  1.00 41.78 ? 25  SER D CA  1 
ATOM   3295 C  C   . SER D 1 25  ? 6.147   10.897  13.707  1.00 41.80 ? 25  SER D C   1 
ATOM   3296 O  O   . SER D 1 25  ? 7.182   10.257  13.879  1.00 42.91 ? 25  SER D O   1 
ATOM   3297 C  CB  . SER D 1 25  ? 4.824   12.171  15.409  1.00 41.90 ? 25  SER D CB  1 
ATOM   3298 O  OG  . SER D 1 25  ? 5.102   11.179  16.384  1.00 42.22 ? 25  SER D OG  1 
ATOM   3299 N  N   . ASN D 1 26  ? 5.137   10.454  12.964  1.00 42.06 ? 26  ASN D N   1 
ATOM   3300 C  CA  . ASN D 1 26  ? 5.189   9.153   12.292  1.00 41.63 ? 26  ASN D CA  1 
ATOM   3301 C  C   . ASN D 1 26  ? 5.436   9.294   10.793  1.00 41.34 ? 26  ASN D C   1 
ATOM   3302 O  O   . ASN D 1 26  ? 5.073   8.410   10.012  1.00 41.69 ? 26  ASN D O   1 
ATOM   3303 C  CB  . ASN D 1 26  ? 3.883   8.389   12.525  1.00 41.87 ? 26  ASN D CB  1 
ATOM   3304 C  CG  . ASN D 1 26  ? 3.546   8.238   13.997  1.00 42.53 ? 26  ASN D CG  1 
ATOM   3305 O  OD1 . ASN D 1 26  ? 2.386   8.357   14.390  1.00 44.76 ? 26  ASN D OD1 1 
ATOM   3306 N  ND2 . ASN D 1 26  ? 4.562   7.982   14.821  1.00 44.03 ? 26  ASN D ND2 1 
ATOM   3307 N  N   . GLY D 1 27  ? 6.054   10.405  10.396  1.00 40.49 ? 27  GLY D N   1 
ATOM   3308 C  CA  . GLY D 1 27  ? 6.251   10.706  8.989   1.00 39.66 ? 27  GLY D CA  1 
ATOM   3309 C  C   . GLY D 1 27  ? 7.575   10.185  8.470   1.00 39.02 ? 27  GLY D C   1 
ATOM   3310 O  O   . GLY D 1 27  ? 8.390   9.662   9.241   1.00 38.76 ? 27  GLY D O   1 
ATOM   3311 N  N   . PRO D 1 28  ? 7.800   10.328  7.152   1.00 38.14 ? 28  PRO D N   1 
ATOM   3312 C  CA  . PRO D 1 28  ? 9.050   9.895   6.531   1.00 37.76 ? 28  PRO D CA  1 
ATOM   3313 C  C   . PRO D 1 28  ? 10.270  10.640  7.070   1.00 37.18 ? 28  PRO D C   1 
ATOM   3314 O  O   . PRO D 1 28  ? 10.168  11.798  7.472   1.00 36.44 ? 28  PRO D O   1 
ATOM   3315 C  CB  . PRO D 1 28  ? 8.840   10.224  5.047   1.00 37.87 ? 28  PRO D CB  1 
ATOM   3316 C  CG  . PRO D 1 28  ? 7.381   10.372  4.877   1.00 37.81 ? 28  PRO D CG  1 
ATOM   3317 C  CD  . PRO D 1 28  ? 6.873   10.908  6.162   1.00 38.02 ? 28  PRO D CD  1 
ATOM   3318 N  N   . VAL D 1 29  ? 11.408  9.959   7.061   1.00 36.84 ? 29  VAL D N   1 
ATOM   3319 C  CA  . VAL D 1 29  ? 12.676  10.532  7.501   1.00 36.87 ? 29  VAL D CA  1 
ATOM   3320 C  C   . VAL D 1 29  ? 13.572  10.726  6.283   1.00 36.94 ? 29  VAL D C   1 
ATOM   3321 O  O   . VAL D 1 29  ? 13.807  9.779   5.529   1.00 36.55 ? 29  VAL D O   1 
ATOM   3322 C  CB  . VAL D 1 29  ? 13.405  9.598   8.489   1.00 36.81 ? 29  VAL D CB  1 
ATOM   3323 C  CG1 . VAL D 1 29  ? 14.693  10.252  8.996   1.00 36.60 ? 29  VAL D CG1 1 
ATOM   3324 C  CG2 . VAL D 1 29  ? 12.508  9.222   9.654   1.00 36.98 ? 29  VAL D CG2 1 
ATOM   3325 N  N   . LYS D 1 30  ? 14.060  11.949  6.090   1.00 36.79 ? 30  LYS D N   1 
ATOM   3326 C  CA  . LYS D 1 30  ? 15.017  12.236  5.033   1.00 37.00 ? 30  LYS D CA  1 
ATOM   3327 C  C   . LYS D 1 30  ? 16.415  11.956  5.559   1.00 36.99 ? 30  LYS D C   1 
ATOM   3328 O  O   . LYS D 1 30  ? 16.755  12.359  6.672   1.00 36.44 ? 30  LYS D O   1 
ATOM   3329 C  CB  . LYS D 1 30  ? 14.907  13.689  4.578   1.00 37.10 ? 30  LYS D CB  1 
ATOM   3330 C  CG  . LYS D 1 30  ? 13.580  14.028  3.917   1.00 37.95 ? 30  LYS D CG  1 
ATOM   3331 C  CD  . LYS D 1 30  ? 13.526  15.496  3.482   1.00 38.34 ? 30  LYS D CD  1 
ATOM   3332 C  CE  . LYS D 1 30  ? 12.098  15.954  3.230   1.00 38.67 ? 30  LYS D CE  1 
ATOM   3333 N  NZ  . LYS D 1 30  ? 11.999  17.418  2.945   1.00 39.48 ? 30  LYS D NZ  1 
ATOM   3334 N  N   . VAL D 1 31  ? 17.205  11.247  4.758   1.00 36.83 ? 31  VAL D N   1 
ATOM   3335 C  CA  . VAL D 1 31  ? 18.562  10.852  5.118   1.00 36.94 ? 31  VAL D CA  1 
ATOM   3336 C  C   . VAL D 1 31  ? 19.488  11.382  4.028   1.00 36.94 ? 31  VAL D C   1 
ATOM   3337 O  O   . VAL D 1 31  ? 19.328  11.042  2.848   1.00 36.72 ? 31  VAL D O   1 
ATOM   3338 C  CB  . VAL D 1 31  ? 18.689  9.313   5.225   1.00 36.92 ? 31  VAL D CB  1 
ATOM   3339 C  CG1 . VAL D 1 31  ? 20.078  8.904   5.715   1.00 37.33 ? 31  VAL D CG1 1 
ATOM   3340 C  CG2 . VAL D 1 31  ? 17.611  8.742   6.148   1.00 37.29 ? 31  VAL D CG2 1 
ATOM   3341 N  N   . TRP D 1 32  ? 20.430  12.243  4.404   1.00 36.95 ? 32  TRP D N   1 
ATOM   3342 C  CA  . TRP D 1 32  ? 21.348  12.814  3.423   1.00 37.16 ? 32  TRP D CA  1 
ATOM   3343 C  C   . TRP D 1 32  ? 22.696  13.181  4.017   1.00 36.86 ? 32  TRP D C   1 
ATOM   3344 O  O   . TRP D 1 32  ? 22.812  13.467  5.213   1.00 36.51 ? 32  TRP D O   1 
ATOM   3345 C  CB  . TRP D 1 32  ? 20.729  14.045  2.768   1.00 37.86 ? 32  TRP D CB  1 
ATOM   3346 C  CG  . TRP D 1 32  ? 20.785  15.280  3.609   1.00 38.60 ? 32  TRP D CG  1 
ATOM   3347 C  CD1 . TRP D 1 32  ? 21.684  16.303  3.503   1.00 39.09 ? 32  TRP D CD1 1 
ATOM   3348 C  CD2 . TRP D 1 32  ? 19.899  15.633  4.675   1.00 38.51 ? 32  TRP D CD2 1 
ATOM   3349 N  NE1 . TRP D 1 32  ? 21.417  17.268  4.444   1.00 38.99 ? 32  TRP D NE1 1 
ATOM   3350 C  CE2 . TRP D 1 32  ? 20.321  16.886  5.172   1.00 39.29 ? 32  TRP D CE2 1 
ATOM   3351 C  CE3 . TRP D 1 32  ? 18.785  15.019  5.252   1.00 39.30 ? 32  TRP D CE3 1 
ATOM   3352 C  CZ2 . TRP D 1 32  ? 19.670  17.533  6.227   1.00 39.06 ? 32  TRP D CZ2 1 
ATOM   3353 C  CZ3 . TRP D 1 32  ? 18.138  15.661  6.302   1.00 39.18 ? 32  TRP D CZ3 1 
ATOM   3354 C  CH2 . TRP D 1 32  ? 18.584  16.907  6.779   1.00 39.23 ? 32  TRP D CH2 1 
ATOM   3355 N  N   . GLY D 1 33  ? 23.704  13.191  3.154   1.00 36.74 ? 33  GLY D N   1 
ATOM   3356 C  CA  . GLY D 1 33  ? 25.059  13.519  3.552   1.00 37.02 ? 33  GLY D CA  1 
ATOM   3357 C  C   . GLY D 1 33  ? 26.071  13.034  2.545   1.00 37.07 ? 33  GLY D C   1 
ATOM   3358 O  O   . GLY D 1 33  ? 25.747  12.807  1.372   1.00 36.86 ? 33  GLY D O   1 
ATOM   3359 N  N   . SER D 1 34  ? 27.308  12.889  3.003   1.00 37.25 ? 34  SER D N   1 
ATOM   3360 C  CA  . SER D 1 34  ? 28.422  12.519  2.134   1.00 37.57 ? 34  SER D CA  1 
ATOM   3361 C  C   . SER D 1 34  ? 29.309  11.516  2.849   1.00 37.39 ? 34  SER D C   1 
ATOM   3362 O  O   . SER D 1 34  ? 29.527  11.637  4.052   1.00 37.45 ? 34  SER D O   1 
ATOM   3363 C  CB  . SER D 1 34  ? 29.241  13.751  1.760   1.00 38.16 ? 34  SER D CB  1 
ATOM   3364 O  OG  . SER D 1 34  ? 28.434  14.736  1.134   1.00 40.93 ? 34  SER D OG  1 
ATOM   3365 N  N   . ILE D 1 35  ? 29.786  10.515  2.113   1.00 37.25 ? 35  ILE D N   1 
ATOM   3366 C  CA  . ILE D 1 35  ? 30.780  9.567   2.614   1.00 37.24 ? 35  ILE D CA  1 
ATOM   3367 C  C   . ILE D 1 35  ? 31.941  9.514   1.622   1.00 37.00 ? 35  ILE D C   1 
ATOM   3368 O  O   . ILE D 1 35  ? 31.723  9.460   0.414   1.00 36.78 ? 35  ILE D O   1 
ATOM   3369 C  CB  . ILE D 1 35  ? 30.200  8.143   2.786   1.00 37.09 ? 35  ILE D CB  1 
ATOM   3370 C  CG1 . ILE D 1 35  ? 28.865  8.175   3.541   1.00 37.63 ? 35  ILE D CG1 1 
ATOM   3371 C  CG2 . ILE D 1 35  ? 31.197  7.240   3.528   1.00 37.28 ? 35  ILE D CG2 1 
ATOM   3372 C  CD1 . ILE D 1 35  ? 28.201  6.813   3.671   1.00 37.14 ? 35  ILE D CD1 1 
ATOM   3373 N  N   . LYS D 1 36  ? 33.171  9.534   2.132   1.00 37.27 ? 36  LYS D N   1 
ATOM   3374 C  CA  . LYS D 1 36  ? 34.353  9.404   1.280   1.00 37.03 ? 36  LYS D CA  1 
ATOM   3375 C  C   . LYS D 1 36  ? 35.217  8.215   1.684   1.00 36.72 ? 36  LYS D C   1 
ATOM   3376 O  O   . LYS D 1 36  ? 34.979  7.586   2.708   1.00 36.17 ? 36  LYS D O   1 
ATOM   3377 C  CB  . LYS D 1 36  ? 35.180  10.699  1.283   1.00 37.46 ? 36  LYS D CB  1 
ATOM   3378 C  CG  . LYS D 1 36  ? 35.808  11.068  2.621   1.00 37.75 ? 36  LYS D CG  1 
ATOM   3379 C  CD  . LYS D 1 36  ? 36.511  12.420  2.526   1.00 37.92 ? 36  LYS D CD  1 
ATOM   3380 C  CE  . LYS D 1 36  ? 37.231  12.772  3.817   1.00 38.38 ? 36  LYS D CE  1 
ATOM   3381 N  NZ  . LYS D 1 36  ? 37.913  14.100  3.723   1.00 40.16 ? 36  LYS D NZ  1 
ATOM   3382 N  N   . GLY D 1 37  ? 36.217  7.912   0.856   1.00 36.54 ? 37  GLY D N   1 
ATOM   3383 C  CA  . GLY D 1 37  ? 37.149  6.813   1.116   1.00 36.64 ? 37  GLY D CA  1 
ATOM   3384 C  C   . GLY D 1 37  ? 36.679  5.436   0.677   1.00 36.73 ? 37  GLY D C   1 
ATOM   3385 O  O   . GLY D 1 37  ? 37.336  4.432   0.966   1.00 36.95 ? 37  GLY D O   1 
ATOM   3386 N  N   . LEU D 1 38  ? 35.563  5.387   -0.048  1.00 36.76 ? 38  LEU D N   1 
ATOM   3387 C  CA  . LEU D 1 38  ? 34.931  4.122   -0.433  1.00 36.73 ? 38  LEU D CA  1 
ATOM   3388 C  C   . LEU D 1 38  ? 35.435  3.595   -1.770  1.00 36.77 ? 38  LEU D C   1 
ATOM   3389 O  O   . LEU D 1 38  ? 35.799  4.370   -2.654  1.00 36.73 ? 38  LEU D O   1 
ATOM   3390 C  CB  . LEU D 1 38  ? 33.410  4.308   -0.529  1.00 36.64 ? 38  LEU D CB  1 
ATOM   3391 C  CG  . LEU D 1 38  ? 32.656  4.626   0.762   1.00 36.61 ? 38  LEU D CG  1 
ATOM   3392 C  CD1 . LEU D 1 38  ? 31.262  5.153   0.438   1.00 37.14 ? 38  LEU D CD1 1 
ATOM   3393 C  CD2 . LEU D 1 38  ? 32.573  3.405   1.652   1.00 35.67 ? 38  LEU D CD2 1 
ATOM   3394 N  N   . THR D 1 39  ? 35.445  2.272   -1.920  1.00 36.71 ? 39  THR D N   1 
ATOM   3395 C  CA  . THR D 1 39  ? 35.651  1.660   -3.226  1.00 36.78 ? 39  THR D CA  1 
ATOM   3396 C  C   . THR D 1 39  ? 34.434  1.964   -4.098  1.00 36.83 ? 39  THR D C   1 
ATOM   3397 O  O   . THR D 1 39  ? 33.307  2.047   -3.600  1.00 37.44 ? 39  THR D O   1 
ATOM   3398 C  CB  . THR D 1 39  ? 35.831  0.133   -3.136  1.00 36.74 ? 39  THR D CB  1 
ATOM   3399 O  OG1 . THR D 1 39  ? 34.732  -0.436  -2.420  1.00 36.68 ? 39  THR D OG1 1 
ATOM   3400 C  CG2 . THR D 1 39  ? 37.126  -0.223  -2.426  1.00 36.72 ? 39  THR D CG2 1 
ATOM   3401 N  N   . GLU D 1 40  ? 34.673  2.142   -5.389  1.00 36.95 ? 40  GLU D N   1 
ATOM   3402 C  CA  . GLU D 1 40  ? 33.618  2.478   -6.343  1.00 36.67 ? 40  GLU D CA  1 
ATOM   3403 C  C   . GLU D 1 40  ? 32.509  1.426   -6.322  1.00 36.36 ? 40  GLU D C   1 
ATOM   3404 O  O   . GLU D 1 40  ? 32.789  0.229   -6.281  1.00 36.29 ? 40  GLU D O   1 
ATOM   3405 C  CB  . GLU D 1 40  ? 34.213  2.579   -7.747  1.00 36.92 ? 40  GLU D CB  1 
ATOM   3406 C  CG  . GLU D 1 40  ? 33.318  3.245   -8.767  1.00 37.13 ? 40  GLU D CG  1 
ATOM   3407 C  CD  . GLU D 1 40  ? 33.999  3.425   -10.113 1.00 37.24 ? 40  GLU D CD  1 
ATOM   3408 O  OE1 . GLU D 1 40  ? 35.072  2.819   -10.337 1.00 37.64 ? 40  GLU D OE1 1 
ATOM   3409 O  OE2 . GLU D 1 40  ? 33.456  4.172   -10.955 1.00 38.82 ? 40  GLU D OE2 1 
ATOM   3410 N  N   . GLY D 1 41  ? 31.256  1.876   -6.332  1.00 36.06 ? 41  GLY D N   1 
ATOM   3411 C  CA  . GLY D 1 41  ? 30.108  0.971   -6.412  1.00 35.50 ? 41  GLY D CA  1 
ATOM   3412 C  C   . GLY D 1 41  ? 29.174  1.029   -5.218  1.00 35.12 ? 41  GLY D C   1 
ATOM   3413 O  O   . GLY D 1 41  ? 29.193  1.987   -4.449  1.00 34.81 ? 41  GLY D O   1 
ATOM   3414 N  N   . LEU D 1 42  ? 28.365  -0.018  -5.071  1.00 34.64 ? 42  LEU D N   1 
ATOM   3415 C  CA  . LEU D 1 42  ? 27.316  -0.080  -4.055  1.00 34.54 ? 42  LEU D CA  1 
ATOM   3416 C  C   . LEU D 1 42  ? 27.854  -0.580  -2.726  1.00 34.21 ? 42  LEU D C   1 
ATOM   3417 O  O   . LEU D 1 42  ? 28.672  -1.498  -2.691  1.00 33.83 ? 42  LEU D O   1 
ATOM   3418 C  CB  . LEU D 1 42  ? 26.203  -1.023  -4.500  1.00 34.38 ? 42  LEU D CB  1 
ATOM   3419 C  CG  . LEU D 1 42  ? 25.348  -0.598  -5.687  1.00 34.46 ? 42  LEU D CG  1 
ATOM   3420 C  CD1 . LEU D 1 42  ? 24.591  -1.806  -6.211  1.00 34.79 ? 42  LEU D CD1 1 
ATOM   3421 C  CD2 . LEU D 1 42  ? 24.391  0.517   -5.302  1.00 34.33 ? 42  LEU D CD2 1 
ATOM   3422 N  N   . HIS D 1 43  ? 27.361  0.021   -1.645  1.00 34.07 ? 43  HIS D N   1 
ATOM   3423 C  CA  . HIS D 1 43  ? 27.725  -0.341  -0.278  1.00 34.19 ? 43  HIS D CA  1 
ATOM   3424 C  C   . HIS D 1 43  ? 26.471  -0.389  0.593   1.00 34.08 ? 43  HIS D C   1 
ATOM   3425 O  O   . HIS D 1 43  ? 25.723  0.584   0.652   1.00 33.96 ? 43  HIS D O   1 
ATOM   3426 C  CB  . HIS D 1 43  ? 28.708  0.685   0.282   1.00 34.31 ? 43  HIS D CB  1 
ATOM   3427 C  CG  . HIS D 1 43  ? 30.042  0.666   -0.396  1.00 34.82 ? 43  HIS D CG  1 
ATOM   3428 N  ND1 . HIS D 1 43  ? 30.999  -0.287  -0.119  1.00 35.08 ? 43  HIS D ND1 1 
ATOM   3429 C  CD2 . HIS D 1 43  ? 30.570  1.463   -1.356  1.00 34.85 ? 43  HIS D CD2 1 
ATOM   3430 C  CE1 . HIS D 1 43  ? 32.062  -0.071  -0.873  1.00 34.70 ? 43  HIS D CE1 1 
ATOM   3431 N  NE2 . HIS D 1 43  ? 31.828  0.985   -1.632  1.00 34.70 ? 43  HIS D NE2 1 
ATOM   3432 N  N   . GLY D 1 44  ? 26.250  -1.517  1.268   1.00 34.09 ? 44  GLY D N   1 
ATOM   3433 C  CA  . GLY D 1 44  ? 25.120  -1.671  2.183   1.00 34.15 ? 44  GLY D CA  1 
ATOM   3434 C  C   . GLY D 1 44  ? 25.085  -0.581  3.238   1.00 34.20 ? 44  GLY D C   1 
ATOM   3435 O  O   . GLY D 1 44  ? 26.124  -0.147  3.728   1.00 33.69 ? 44  GLY D O   1 
ATOM   3436 N  N   . PHE D 1 45  ? 23.877  -0.155  3.595   1.00 34.56 ? 45  PHE D N   1 
ATOM   3437 C  CA  . PHE D 1 45  ? 23.681  1.015   4.437   1.00 34.82 ? 45  PHE D CA  1 
ATOM   3438 C  C   . PHE D 1 45  ? 22.585  0.670   5.440   1.00 34.72 ? 45  PHE D C   1 
ATOM   3439 O  O   . PHE D 1 45  ? 21.418  0.596   5.071   1.00 34.85 ? 45  PHE D O   1 
ATOM   3440 C  CB  . PHE D 1 45  ? 23.286  2.191   3.538   1.00 35.22 ? 45  PHE D CB  1 
ATOM   3441 C  CG  . PHE D 1 45  ? 23.475  3.552   4.151   1.00 34.93 ? 45  PHE D CG  1 
ATOM   3442 C  CD1 . PHE D 1 45  ? 24.664  3.905   4.780   1.00 36.47 ? 45  PHE D CD1 1 
ATOM   3443 C  CD2 . PHE D 1 45  ? 22.475  4.509   4.041   1.00 35.97 ? 45  PHE D CD2 1 
ATOM   3444 C  CE1 . PHE D 1 45  ? 24.832  5.171   5.313   1.00 36.39 ? 45  PHE D CE1 1 
ATOM   3445 C  CE2 . PHE D 1 45  ? 22.635  5.781   4.570   1.00 36.10 ? 45  PHE D CE2 1 
ATOM   3446 C  CZ  . PHE D 1 45  ? 23.828  6.116   5.202   1.00 35.72 ? 45  PHE D CZ  1 
ATOM   3447 N  N   . HIS D 1 46  ? 22.968  0.444   6.699   1.00 34.82 ? 46  HIS D N   1 
ATOM   3448 C  CA  . HIS D 1 46  ? 22.050  -0.098  7.704   1.00 35.00 ? 46  HIS D CA  1 
ATOM   3449 C  C   . HIS D 1 46  ? 22.154  0.580   9.069   1.00 35.29 ? 46  HIS D C   1 
ATOM   3450 O  O   . HIS D 1 46  ? 23.246  0.963   9.508   1.00 34.81 ? 46  HIS D O   1 
ATOM   3451 C  CB  . HIS D 1 46  ? 22.314  -1.595  7.924   1.00 35.22 ? 46  HIS D CB  1 
ATOM   3452 C  CG  . HIS D 1 46  ? 21.996  -2.453  6.741   1.00 35.65 ? 46  HIS D CG  1 
ATOM   3453 N  ND1 . HIS D 1 46  ? 20.742  -2.980  6.519   1.00 34.85 ? 46  HIS D ND1 1 
ATOM   3454 C  CD2 . HIS D 1 46  ? 22.775  -2.894  5.726   1.00 36.10 ? 46  HIS D CD2 1 
ATOM   3455 C  CE1 . HIS D 1 46  ? 20.762  -3.704  5.414   1.00 35.93 ? 46  HIS D CE1 1 
ATOM   3456 N  NE2 . HIS D 1 46  ? 21.983  -3.664  4.912   1.00 35.88 ? 46  HIS D NE2 1 
ATOM   3457 N  N   . VAL D 1 47  ? 21.009  0.696   9.744   1.00 34.83 ? 47  VAL D N   1 
ATOM   3458 C  CA  . VAL D 1 47  ? 20.994  0.995   11.169  1.00 34.78 ? 47  VAL D CA  1 
ATOM   3459 C  C   . VAL D 1 47  ? 21.119  -0.326  11.912  1.00 34.44 ? 47  VAL D C   1 
ATOM   3460 O  O   . VAL D 1 47  ? 20.376  -1.279  11.644  1.00 34.55 ? 47  VAL D O   1 
ATOM   3461 C  CB  . VAL D 1 47  ? 19.710  1.715   11.633  1.00 35.16 ? 47  VAL D CB  1 
ATOM   3462 C  CG1 . VAL D 1 47  ? 19.800  2.054   13.117  1.00 35.46 ? 47  VAL D CG1 1 
ATOM   3463 C  CG2 . VAL D 1 47  ? 19.483  2.996   10.810  1.00 35.77 ? 47  VAL D CG2 1 
ATOM   3464 N  N   . HIS D 1 48  ? 22.075  -0.359  12.837  1.00 33.82 ? 48  HIS D N   1 
ATOM   3465 C  CA  . HIS D 1 48  ? 22.307  -1.506  13.704  1.00 33.84 ? 48  HIS D CA  1 
ATOM   3466 C  C   . HIS D 1 48  ? 21.826  -1.196  15.113  1.00 33.76 ? 48  HIS D C   1 
ATOM   3467 O  O   . HIS D 1 48  ? 21.666  -0.051  15.481  1.00 34.30 ? 48  HIS D O   1 
ATOM   3468 C  CB  . HIS D 1 48  ? 23.788  -1.866  13.678  1.00 33.63 ? 48  HIS D CB  1 
ATOM   3469 C  CG  . HIS D 1 48  ? 24.216  -2.500  12.394  1.00 32.76 ? 48  HIS D CG  1 
ATOM   3470 N  ND1 . HIS D 1 48  ? 24.624  -3.816  12.314  1.00 32.89 ? 48  HIS D ND1 1 
ATOM   3471 C  CD2 . HIS D 1 48  ? 24.250  -2.020  11.128  1.00 33.37 ? 48  HIS D CD2 1 
ATOM   3472 C  CE1 . HIS D 1 48  ? 24.926  -4.105  11.061  1.00 34.45 ? 48  HIS D CE1 1 
ATOM   3473 N  NE2 . HIS D 1 48  ? 24.708  -3.034  10.320  1.00 34.09 ? 48  HIS D NE2 1 
ATOM   3474 N  N   . GLU D 1 49  ? 21.589  -2.233  15.907  1.00 33.56 ? 49  GLU D N   1 
ATOM   3475 C  CA  . GLU D 1 49  ? 20.795  -2.085  17.121  1.00 33.58 ? 49  GLU D CA  1 
ATOM   3476 C  C   . GLU D 1 49  ? 21.436  -1.240  18.228  1.00 33.61 ? 49  GLU D C   1 
ATOM   3477 O  O   . GLU D 1 49  ? 20.751  -0.466  18.893  1.00 33.86 ? 49  GLU D O   1 
ATOM   3478 C  CB  . GLU D 1 49  ? 20.442  -3.467  17.674  1.00 33.46 ? 49  GLU D CB  1 
ATOM   3479 C  CG  . GLU D 1 49  ? 19.419  -3.408  18.781  1.00 34.20 ? 49  GLU D CG  1 
ATOM   3480 C  CD  . GLU D 1 49  ? 19.114  -4.757  19.383  1.00 34.70 ? 49  GLU D CD  1 
ATOM   3481 O  OE1 . GLU D 1 49  ? 19.507  -5.787  18.797  1.00 38.59 ? 49  GLU D OE1 1 
ATOM   3482 O  OE2 . GLU D 1 49  ? 18.479  -4.786  20.458  1.00 36.56 ? 49  GLU D OE2 1 
ATOM   3483 N  N   . PHE D 1 50  ? 22.741  -1.378  18.437  1.00 33.80 ? 50  PHE D N   1 
ATOM   3484 C  CA  . PHE D 1 50  ? 23.365  -0.747  19.605  1.00 34.00 ? 50  PHE D CA  1 
ATOM   3485 C  C   . PHE D 1 50  ? 24.245  0.417   19.223  1.00 33.82 ? 50  PHE D C   1 
ATOM   3486 O  O   . PHE D 1 50  ? 24.987  0.333   18.249  1.00 33.48 ? 50  PHE D O   1 
ATOM   3487 C  CB  . PHE D 1 50  ? 24.179  -1.777  20.386  1.00 34.20 ? 50  PHE D CB  1 
ATOM   3488 C  CG  . PHE D 1 50  ? 23.376  -2.972  20.803  1.00 33.46 ? 50  PHE D CG  1 
ATOM   3489 C  CD1 . PHE D 1 50  ? 22.293  -2.831  21.661  1.00 34.03 ? 50  PHE D CD1 1 
ATOM   3490 C  CD2 . PHE D 1 50  ? 23.682  -4.237  20.323  1.00 34.68 ? 50  PHE D CD2 1 
ATOM   3491 C  CE1 . PHE D 1 50  ? 21.530  -3.936  22.035  1.00 34.90 ? 50  PHE D CE1 1 
ATOM   3492 C  CE2 . PHE D 1 50  ? 22.926  -5.333  20.696  1.00 34.74 ? 50  PHE D CE2 1 
ATOM   3493 C  CZ  . PHE D 1 50  ? 21.848  -5.177  21.550  1.00 34.36 ? 50  PHE D CZ  1 
ATOM   3494 N  N   . GLY D 1 51  ? 24.171  1.492   20.011  1.00 34.20 ? 51  GLY D N   1 
ATOM   3495 C  CA  . GLY D 1 51  ? 25.047  2.646   19.842  1.00 34.87 ? 51  GLY D CA  1 
ATOM   3496 C  C   . GLY D 1 51  ? 26.319  2.456   20.645  1.00 35.61 ? 51  GLY D C   1 
ATOM   3497 O  O   . GLY D 1 51  ? 26.705  3.322   21.413  1.00 35.84 ? 51  GLY D O   1 
ATOM   3498 N  N   . ASP D 1 52  ? 26.941  1.291   20.470  1.00 35.84 ? 52  ASP D N   1 
ATOM   3499 C  CA  . ASP D 1 52  ? 28.072  0.860   21.269  1.00 35.58 ? 52  ASP D CA  1 
ATOM   3500 C  C   . ASP D 1 52  ? 29.281  0.739   20.346  1.00 35.91 ? 52  ASP D C   1 
ATOM   3501 O  O   . ASP D 1 52  ? 29.323  -0.151  19.483  1.00 35.63 ? 52  ASP D O   1 
ATOM   3502 C  CB  . ASP D 1 52  ? 27.745  -0.485  21.925  1.00 35.54 ? 52  ASP D CB  1 
ATOM   3503 C  CG  . ASP D 1 52  ? 28.842  -0.974  22.855  1.00 35.73 ? 52  ASP D CG  1 
ATOM   3504 O  OD1 . ASP D 1 52  ? 30.024  -0.611  22.659  1.00 34.02 ? 52  ASP D OD1 1 
ATOM   3505 O  OD2 . ASP D 1 52  ? 28.523  -1.774  23.763  1.00 36.63 ? 52  ASP D OD2 1 
ATOM   3506 N  N   . ASN D 1 53  ? 30.249  1.643   20.521  1.00 35.93 ? 53  ASN D N   1 
ATOM   3507 C  CA  . ASN D 1 53  ? 31.472  1.657   19.715  1.00 36.13 ? 53  ASN D CA  1 
ATOM   3508 C  C   . ASN D 1 53  ? 32.692  1.191   20.509  1.00 35.85 ? 53  ASN D C   1 
ATOM   3509 O  O   . ASN D 1 53  ? 33.826  1.526   20.167  1.00 35.84 ? 53  ASN D O   1 
ATOM   3510 C  CB  . ASN D 1 53  ? 31.718  3.069   19.169  1.00 36.28 ? 53  ASN D CB  1 
ATOM   3511 C  CG  . ASN D 1 53  ? 32.839  3.120   18.138  1.00 37.24 ? 53  ASN D CG  1 
ATOM   3512 O  OD1 . ASN D 1 53  ? 32.882  2.318   17.199  1.00 40.53 ? 53  ASN D OD1 1 
ATOM   3513 N  ND2 . ASN D 1 53  ? 33.768  4.058   18.323  1.00 38.04 ? 53  ASN D ND2 1 
ATOM   3514 N  N   . THR D 1 54  ? 32.475  0.399   21.554  1.00 35.51 ? 54  THR D N   1 
ATOM   3515 C  CA  . THR D 1 54  ? 33.586  -0.046  22.398  1.00 35.99 ? 54  THR D CA  1 
ATOM   3516 C  C   . THR D 1 54  ? 34.511  -1.014  21.653  1.00 36.14 ? 54  THR D C   1 
ATOM   3517 O  O   . THR D 1 54  ? 35.711  -1.048  21.922  1.00 36.17 ? 54  THR D O   1 
ATOM   3518 C  CB  . THR D 1 54  ? 33.096  -0.700  23.711  1.00 35.88 ? 54  THR D CB  1 
ATOM   3519 O  OG1 . THR D 1 54  ? 32.199  -1.773  23.419  1.00 35.78 ? 54  THR D OG1 1 
ATOM   3520 C  CG2 . THR D 1 54  ? 32.398  0.325   24.600  1.00 35.41 ? 54  THR D CG2 1 
ATOM   3521 N  N   . ALA D 1 55  ? 33.953  -1.794  20.725  1.00 36.47 ? 55  ALA D N   1 
ATOM   3522 C  CA  . ALA D 1 55  ? 34.737  -2.709  19.894  1.00 36.88 ? 55  ALA D CA  1 
ATOM   3523 C  C   . ALA D 1 55  ? 34.603  -2.349  18.411  1.00 37.24 ? 55  ALA D C   1 
ATOM   3524 O  O   . ALA D 1 55  ? 34.327  -3.207  17.568  1.00 38.23 ? 55  ALA D O   1 
ATOM   3525 C  CB  . ALA D 1 55  ? 34.302  -4.148  20.142  1.00 36.88 ? 55  ALA D CB  1 
ATOM   3526 N  N   . GLY D 1 56  ? 34.806  -1.075  18.093  1.00 37.14 ? 56  GLY D N   1 
ATOM   3527 C  CA  . GLY D 1 56  ? 34.652  -0.593  16.726  1.00 37.15 ? 56  GLY D CA  1 
ATOM   3528 C  C   . GLY D 1 56  ? 33.227  -0.781  16.248  1.00 37.16 ? 56  GLY D C   1 
ATOM   3529 O  O   . GLY D 1 56  ? 32.287  -0.661  17.030  1.00 37.20 ? 56  GLY D O   1 
ATOM   3530 N  N   . CYS D 1 57  ? 33.064  -1.120  14.972  1.00 37.09 ? 57  CYS D N   1 
ATOM   3531 C  CA  . CYS D 1 57  ? 31.726  -1.278  14.397  1.00 37.20 ? 57  CYS D CA  1 
ATOM   3532 C  C   . CYS D 1 57  ? 31.095  -2.620  14.772  1.00 36.71 ? 57  CYS D C   1 
ATOM   3533 O  O   . CYS D 1 57  ? 29.886  -2.798  14.646  1.00 36.25 ? 57  CYS D O   1 
ATOM   3534 C  CB  . CYS D 1 57  ? 31.771  -1.077  12.880  1.00 37.57 ? 57  CYS D CB  1 
ATOM   3535 S  SG  . CYS D 1 57  ? 32.279  0.621   12.411  1.00 40.45 ? 57  CYS D SG  1 
ATOM   3536 N  N   . THR D 1 58  ? 31.912  -3.543  15.273  1.00 36.36 ? 58  THR D N   1 
ATOM   3537 C  CA  . THR D 1 58  ? 31.440  -4.868  15.686  1.00 36.31 ? 58  THR D CA  1 
ATOM   3538 C  C   . THR D 1 58  ? 30.419  -4.819  16.831  1.00 35.96 ? 58  THR D C   1 
ATOM   3539 O  O   . THR D 1 58  ? 29.461  -5.597  16.838  1.00 35.62 ? 58  THR D O   1 
ATOM   3540 C  CB  . THR D 1 58  ? 32.633  -5.757  16.088  1.00 36.48 ? 58  THR D CB  1 
ATOM   3541 O  OG1 . THR D 1 58  ? 33.581  -5.770  15.018  1.00 37.73 ? 58  THR D OG1 1 
ATOM   3542 C  CG2 . THR D 1 58  ? 32.201  -7.190  16.382  1.00 36.55 ? 58  THR D CG2 1 
ATOM   3543 N  N   . SER D 1 59  ? 30.619  -3.906  17.783  1.00 35.43 ? 59  SER D N   1 
ATOM   3544 C  CA  . SER D 1 59  ? 29.770  -3.841  18.976  1.00 35.18 ? 59  SER D CA  1 
ATOM   3545 C  C   . SER D 1 59  ? 28.412  -3.160  18.743  1.00 35.04 ? 59  SER D C   1 
ATOM   3546 O  O   . SER D 1 59  ? 27.571  -3.151  19.636  1.00 34.54 ? 59  SER D O   1 
ATOM   3547 C  CB  . SER D 1 59  ? 30.521  -3.193  20.146  1.00 35.18 ? 59  SER D CB  1 
ATOM   3548 O  OG  . SER D 1 59  ? 31.200  -2.024  19.737  1.00 34.98 ? 59  SER D OG  1 
ATOM   3549 N  N   . ALA D 1 60  ? 28.192  -2.603  17.547  1.00 34.63 ? 60  ALA D N   1 
ATOM   3550 C  CA  . ALA D 1 60  ? 26.849  -2.174  17.132  1.00 35.09 ? 60  ALA D CA  1 
ATOM   3551 C  C   . ALA D 1 60  ? 25.834  -3.318  17.052  1.00 35.07 ? 60  ALA D C   1 
ATOM   3552 O  O   . ALA D 1 60  ? 24.627  -3.084  17.074  1.00 35.76 ? 60  ALA D O   1 
ATOM   3553 C  CB  . ALA D 1 60  ? 26.912  -1.428  15.790  1.00 34.94 ? 60  ALA D CB  1 
ATOM   3554 N  N   . GLY D 1 61  ? 26.310  -4.553  16.946  1.00 35.04 ? 61  GLY D N   1 
ATOM   3555 C  CA  . GLY D 1 61  ? 25.420  -5.703  16.959  1.00 35.09 ? 61  GLY D CA  1 
ATOM   3556 C  C   . GLY D 1 61  ? 24.696  -5.882  15.633  1.00 34.85 ? 61  GLY D C   1 
ATOM   3557 O  O   . GLY D 1 61  ? 25.149  -5.375  14.602  1.00 34.73 ? 61  GLY D O   1 
ATOM   3558 N  N   . PRO D 1 62  ? 23.547  -6.581  15.653  1.00 34.85 ? 62  PRO D N   1 
ATOM   3559 C  CA  . PRO D 1 62  ? 22.852  -6.912  14.414  1.00 34.92 ? 62  PRO D CA  1 
ATOM   3560 C  C   . PRO D 1 62  ? 22.085  -5.728  13.818  1.00 34.90 ? 62  PRO D C   1 
ATOM   3561 O  O   . PRO D 1 62  ? 22.006  -4.657  14.421  1.00 34.14 ? 62  PRO D O   1 
ATOM   3562 C  CB  . PRO D 1 62  ? 21.881  -8.017  14.861  1.00 35.04 ? 62  PRO D CB  1 
ATOM   3563 C  CG  . PRO D 1 62  ? 21.530  -7.625  16.235  1.00 35.06 ? 62  PRO D CG  1 
ATOM   3564 C  CD  . PRO D 1 62  ? 22.812  -7.085  16.830  1.00 34.85 ? 62  PRO D CD  1 
ATOM   3565 N  N   . HIS D 1 63  ? 21.533  -5.935  12.627  1.00 35.23 ? 63  HIS D N   1 
ATOM   3566 C  CA  . HIS D 1 63  ? 20.551  -5.030  12.055  1.00 35.56 ? 63  HIS D CA  1 
ATOM   3567 C  C   . HIS D 1 63  ? 19.457  -4.750  13.090  1.00 35.54 ? 63  HIS D C   1 
ATOM   3568 O  O   . HIS D 1 63  ? 19.026  -5.644  13.802  1.00 34.50 ? 63  HIS D O   1 
ATOM   3569 C  CB  . HIS D 1 63  ? 19.901  -5.647  10.807  1.00 35.77 ? 63  HIS D CB  1 
ATOM   3570 C  CG  . HIS D 1 63  ? 20.811  -5.768  9.623   1.00 35.85 ? 63  HIS D CG  1 
ATOM   3571 N  ND1 . HIS D 1 63  ? 20.555  -6.637  8.583   1.00 36.18 ? 63  HIS D ND1 1 
ATOM   3572 C  CD2 . HIS D 1 63  ? 21.972  -5.145  9.313   1.00 36.63 ? 63  HIS D CD2 1 
ATOM   3573 C  CE1 . HIS D 1 63  ? 21.514  -6.536  7.681   1.00 36.18 ? 63  HIS D CE1 1 
ATOM   3574 N  NE2 . HIS D 1 63  ? 22.388  -5.641  8.102   1.00 36.68 ? 63  HIS D NE2 1 
ATOM   3575 N  N   . PHE D 1 64  ? 19.010  -3.504  13.160  1.00 35.81 ? 64  PHE D N   1 
ATOM   3576 C  CA  . PHE D 1 64  ? 17.990  -3.094  14.114  1.00 36.29 ? 64  PHE D CA  1 
ATOM   3577 C  C   . PHE D 1 64  ? 16.642  -3.681  13.719  1.00 37.01 ? 64  PHE D C   1 
ATOM   3578 O  O   . PHE D 1 64  ? 16.194  -3.514  12.586  1.00 36.86 ? 64  PHE D O   1 
ATOM   3579 C  CB  . PHE D 1 64  ? 17.927  -1.561  14.175  1.00 35.98 ? 64  PHE D CB  1 
ATOM   3580 C  CG  . PHE D 1 64  ? 16.836  -1.022  15.058  1.00 36.61 ? 64  PHE D CG  1 
ATOM   3581 C  CD1 . PHE D 1 64  ? 16.652  -1.507  16.348  1.00 36.70 ? 64  PHE D CD1 1 
ATOM   3582 C  CD2 . PHE D 1 64  ? 16.005  0.005   14.605  1.00 37.28 ? 64  PHE D CD2 1 
ATOM   3583 C  CE1 . PHE D 1 64  ? 15.642  -0.997  17.162  1.00 37.12 ? 64  PHE D CE1 1 
ATOM   3584 C  CE2 . PHE D 1 64  ? 14.994  0.523   15.418  1.00 36.76 ? 64  PHE D CE2 1 
ATOM   3585 C  CZ  . PHE D 1 64  ? 14.818  0.030   16.694  1.00 36.35 ? 64  PHE D CZ  1 
ATOM   3586 N  N   . ASN D 1 65  ? 16.019  -4.386  14.661  1.00 38.07 ? 65  ASN D N   1 
ATOM   3587 C  CA  . ASN D 1 65  ? 14.763  -5.081  14.424  1.00 38.81 ? 65  ASN D CA  1 
ATOM   3588 C  C   . ASN D 1 65  ? 13.928  -5.063  15.714  1.00 39.52 ? 65  ASN D C   1 
ATOM   3589 O  O   . ASN D 1 65  ? 13.951  -6.024  16.488  1.00 40.57 ? 65  ASN D O   1 
ATOM   3590 C  CB  . ASN D 1 65  ? 15.053  -6.523  13.960  1.00 38.88 ? 65  ASN D CB  1 
ATOM   3591 C  CG  . ASN D 1 65  ? 14.148  -6.980  12.825  1.00 39.19 ? 65  ASN D CG  1 
ATOM   3592 O  OD1 . ASN D 1 65  ? 13.635  -6.177  12.041  1.00 40.98 ? 65  ASN D OD1 1 
ATOM   3593 N  ND2 . ASN D 1 65  ? 13.959  -8.292  12.727  1.00 39.21 ? 65  ASN D ND2 1 
ATOM   3594 N  N   . PRO D 1 66  ? 13.184  -3.967  15.957  1.00 39.82 ? 66  PRO D N   1 
ATOM   3595 C  CA  . PRO D 1 66  ? 12.443  -3.800  17.214  1.00 39.77 ? 66  PRO D CA  1 
ATOM   3596 C  C   . PRO D 1 66  ? 11.177  -4.658  17.353  1.00 39.99 ? 66  PRO D C   1 
ATOM   3597 O  O   . PRO D 1 66  ? 10.988  -5.628  16.614  1.00 40.50 ? 66  PRO D O   1 
ATOM   3598 C  CB  . PRO D 1 66  ? 12.053  -2.322  17.176  1.00 40.08 ? 66  PRO D CB  1 
ATOM   3599 C  CG  . PRO D 1 66  ? 11.896  -2.034  15.735  1.00 39.87 ? 66  PRO D CG  1 
ATOM   3600 C  CD  . PRO D 1 66  ? 12.985  -2.816  15.058  1.00 39.89 ? 66  PRO D CD  1 
ATOM   3601 N  N   . GLU D 1 78  ? 8.791   -6.640  5.750   1.00 46.90 ? 78  GLU D N   1 
ATOM   3602 C  CA  . GLU D 1 78  ? 9.530   -7.110  4.582   1.00 46.76 ? 78  GLU D CA  1 
ATOM   3603 C  C   . GLU D 1 78  ? 11.030  -6.951  4.809   1.00 46.32 ? 78  GLU D C   1 
ATOM   3604 O  O   . GLU D 1 78  ? 11.797  -7.893  4.618   1.00 46.73 ? 78  GLU D O   1 
ATOM   3605 C  CB  . GLU D 1 78  ? 9.096   -6.339  3.331   1.00 46.96 ? 78  GLU D CB  1 
ATOM   3606 C  CG  . GLU D 1 78  ? 7.614   -6.486  3.002   1.00 47.66 ? 78  GLU D CG  1 
ATOM   3607 C  CD  . GLU D 1 78  ? 7.117   -5.470  1.980   1.00 47.82 ? 78  GLU D CD  1 
ATOM   3608 O  OE1 . GLU D 1 78  ? 7.933   -4.663  1.475   1.00 50.02 ? 78  GLU D OE1 1 
ATOM   3609 O  OE2 . GLU D 1 78  ? 5.900   -5.485  1.686   1.00 48.63 ? 78  GLU D OE2 1 
ATOM   3610 N  N   . ARG D 1 79  ? 11.439  -5.755  5.219   1.00 45.75 ? 79  ARG D N   1 
ATOM   3611 C  CA  . ARG D 1 79  ? 12.831  -5.478  5.562   1.00 45.21 ? 79  ARG D CA  1 
ATOM   3612 C  C   . ARG D 1 79  ? 12.920  -5.079  7.024   1.00 44.34 ? 79  ARG D C   1 
ATOM   3613 O  O   . ARG D 1 79  ? 11.947  -4.583  7.589   1.00 44.08 ? 79  ARG D O   1 
ATOM   3614 C  CB  . ARG D 1 79  ? 13.367  -4.336  4.706   1.00 45.43 ? 79  ARG D CB  1 
ATOM   3615 C  CG  . ARG D 1 79  ? 13.537  -4.664  3.235   1.00 46.04 ? 79  ARG D CG  1 
ATOM   3616 C  CD  . ARG D 1 79  ? 14.013  -3.426  2.493   1.00 46.58 ? 79  ARG D CD  1 
ATOM   3617 N  NE  . ARG D 1 79  ? 14.827  -3.752  1.324   1.00 47.54 ? 79  ARG D NE  1 
ATOM   3618 C  CZ  . ARG D 1 79  ? 15.738  -2.942  0.780   1.00 47.56 ? 79  ARG D CZ  1 
ATOM   3619 N  NH1 . ARG D 1 79  ? 15.985  -1.729  1.286   1.00 47.67 ? 79  ARG D NH1 1 
ATOM   3620 N  NH2 . ARG D 1 79  ? 16.420  -3.354  -0.281  1.00 47.45 ? 79  ARG D NH2 1 
ATOM   3621 N  N   . HIS D 1 80  ? 14.087  -5.266  7.637   1.00 43.43 ? 80  HIS D N   1 
ATOM   3622 C  CA  . HIS D 1 80  ? 14.280  -4.812  9.013   1.00 42.92 ? 80  HIS D CA  1 
ATOM   3623 C  C   . HIS D 1 80  ? 14.202  -3.290  9.039   1.00 42.24 ? 80  HIS D C   1 
ATOM   3624 O  O   . HIS D 1 80  ? 14.406  -2.641  8.014   1.00 41.72 ? 80  HIS D O   1 
ATOM   3625 C  CB  . HIS D 1 80  ? 15.602  -5.326  9.608   1.00 42.55 ? 80  HIS D CB  1 
ATOM   3626 C  CG  . HIS D 1 80  ? 16.795  -4.491  9.269   1.00 42.62 ? 80  HIS D CG  1 
ATOM   3627 N  ND1 . HIS D 1 80  ? 17.276  -3.508  10.107  1.00 42.42 ? 80  HIS D ND1 1 
ATOM   3628 C  CD2 . HIS D 1 80  ? 17.619  -4.507  8.195   1.00 42.55 ? 80  HIS D CD2 1 
ATOM   3629 C  CE1 . HIS D 1 80  ? 18.338  -2.945  9.556   1.00 42.54 ? 80  HIS D CE1 1 
ATOM   3630 N  NE2 . HIS D 1 80  ? 18.563  -3.530  8.393   1.00 41.98 ? 80  HIS D NE2 1 
ATOM   3631 N  N   . VAL D 1 81  ? 13.905  -2.731  10.209  1.00 41.77 ? 81  VAL D N   1 
ATOM   3632 C  CA  . VAL D 1 81  ? 13.638  -1.294  10.335  1.00 41.56 ? 81  VAL D CA  1 
ATOM   3633 C  C   . VAL D 1 81  ? 14.837  -0.437  9.880   1.00 41.89 ? 81  VAL D C   1 
ATOM   3634 O  O   . VAL D 1 81  ? 14.678  0.544   9.155   1.00 43.04 ? 81  VAL D O   1 
ATOM   3635 C  CB  . VAL D 1 81  ? 13.168  -0.943  11.773  1.00 41.27 ? 81  VAL D CB  1 
ATOM   3636 C  CG1 . VAL D 1 81  ? 13.097  0.564   11.999  1.00 40.93 ? 81  VAL D CG1 1 
ATOM   3637 C  CG2 . VAL D 1 81  ? 11.798  -1.587  12.044  1.00 41.12 ? 81  VAL D CG2 1 
ATOM   3638 N  N   . GLY D 1 82  ? 16.042  -0.809  10.267  1.00 41.57 ? 82  GLY D N   1 
ATOM   3639 C  CA  . GLY D 1 82  ? 17.209  -0.051  9.809   1.00 40.48 ? 82  GLY D CA  1 
ATOM   3640 C  C   . GLY D 1 82  ? 17.719  -0.222  8.378   1.00 39.66 ? 82  GLY D C   1 
ATOM   3641 O  O   . GLY D 1 82  ? 18.799  0.272   8.073   1.00 38.71 ? 82  GLY D O   1 
ATOM   3642 N  N   . ASP D 1 83  ? 16.979  -0.919  7.508   1.00 38.94 ? 83  ASP D N   1 
ATOM   3643 C  CA  . ASP D 1 83  ? 17.463  -1.238  6.161   1.00 38.61 ? 83  ASP D CA  1 
ATOM   3644 C  C   . ASP D 1 83  ? 17.293  -0.041  5.231   1.00 38.18 ? 83  ASP D C   1 
ATOM   3645 O  O   . ASP D 1 83  ? 16.187  0.229   4.761   1.00 38.24 ? 83  ASP D O   1 
ATOM   3646 C  CB  . ASP D 1 83  ? 16.717  -2.453  5.594   1.00 38.71 ? 83  ASP D CB  1 
ATOM   3647 C  CG  . ASP D 1 83  ? 17.379  -3.026  4.347   1.00 38.99 ? 83  ASP D CG  1 
ATOM   3648 O  OD1 . ASP D 1 83  ? 18.048  -2.270  3.606   1.00 39.80 ? 83  ASP D OD1 1 
ATOM   3649 O  OD2 . ASP D 1 83  ? 17.224  -4.242  4.105   1.00 39.03 ? 83  ASP D OD2 1 
ATOM   3650 N  N   . LEU D 1 84  ? 18.390  0.655   4.944   1.00 37.23 ? 84  LEU D N   1 
ATOM   3651 C  CA  . LEU D 1 84  ? 18.333  1.864   4.127   1.00 37.24 ? 84  LEU D CA  1 
ATOM   3652 C  C   . LEU D 1 84  ? 18.886  1.641   2.717   1.00 37.09 ? 84  LEU D C   1 
ATOM   3653 O  O   . LEU D 1 84  ? 19.283  2.594   2.041   1.00 37.88 ? 84  LEU D O   1 
ATOM   3654 C  CB  . LEU D 1 84  ? 19.075  3.009   4.822   1.00 37.45 ? 84  LEU D CB  1 
ATOM   3655 C  CG  . LEU D 1 84  ? 18.551  3.424   6.201   1.00 37.79 ? 84  LEU D CG  1 
ATOM   3656 C  CD1 . LEU D 1 84  ? 19.458  4.436   6.827   1.00 37.78 ? 84  LEU D CD1 1 
ATOM   3657 C  CD2 . LEU D 1 84  ? 17.143  3.979   6.076   1.00 38.11 ? 84  LEU D CD2 1 
ATOM   3658 N  N   . GLY D 1 85  ? 18.920  0.384   2.278   1.00 36.37 ? 85  GLY D N   1 
ATOM   3659 C  CA  . GLY D 1 85  ? 19.397  0.045   0.949   1.00 36.07 ? 85  GLY D CA  1 
ATOM   3660 C  C   . GLY D 1 85  ? 20.904  0.143   0.849   1.00 35.65 ? 85  GLY D C   1 
ATOM   3661 O  O   . GLY D 1 85  ? 21.616  -0.298  1.745   1.00 35.37 ? 85  GLY D O   1 
ATOM   3662 N  N   . ASN D 1 86  ? 21.379  0.715   -0.253  1.00 35.34 ? 86  ASN D N   1 
ATOM   3663 C  CA  . ASN D 1 86  ? 22.802  0.943   -0.477  1.00 35.41 ? 86  ASN D CA  1 
ATOM   3664 C  C   . ASN D 1 86  ? 23.083  2.420   -0.635  1.00 35.40 ? 86  ASN D C   1 
ATOM   3665 O  O   . ASN D 1 86  ? 22.179  3.204   -0.922  1.00 35.81 ? 86  ASN D O   1 
ATOM   3666 C  CB  . ASN D 1 86  ? 23.279  0.252   -1.754  1.00 35.13 ? 86  ASN D CB  1 
ATOM   3667 C  CG  . ASN D 1 86  ? 23.113  -1.245  -1.717  1.00 34.57 ? 86  ASN D CG  1 
ATOM   3668 O  OD1 . ASN D 1 86  ? 23.815  -1.934  -0.982  1.00 35.80 ? 86  ASN D OD1 1 
ATOM   3669 N  ND2 . ASN D 1 86  ? 22.212  -1.765  -2.544  1.00 34.77 ? 86  ASN D ND2 1 
ATOM   3670 N  N   . VAL D 1 87  ? 24.344  2.793   -0.454  1.00 35.41 ? 87  VAL D N   1 
ATOM   3671 C  CA  . VAL D 1 87  ? 24.846  4.065   -0.968  1.00 35.52 ? 87  VAL D CA  1 
ATOM   3672 C  C   . VAL D 1 87  ? 25.789  3.722   -2.119  1.00 35.47 ? 87  VAL D C   1 
ATOM   3673 O  O   . VAL D 1 87  ? 26.303  2.606   -2.181  1.00 35.19 ? 87  VAL D O   1 
ATOM   3674 C  CB  . VAL D 1 87  ? 25.541  4.922   0.120   1.00 35.46 ? 87  VAL D CB  1 
ATOM   3675 C  CG1 . VAL D 1 87  ? 24.550  5.260   1.235   1.00 36.02 ? 87  VAL D CG1 1 
ATOM   3676 C  CG2 . VAL D 1 87  ? 26.781  4.226   0.684   1.00 35.84 ? 87  VAL D CG2 1 
ATOM   3677 N  N   . THR D 1 88  ? 25.995  4.665   -3.036  1.00 35.86 ? 88  THR D N   1 
ATOM   3678 C  CA  . THR D 1 88  ? 26.867  4.439   -4.188  1.00 36.16 ? 88  THR D CA  1 
ATOM   3679 C  C   . THR D 1 88  ? 28.035  5.418   -4.204  1.00 36.48 ? 88  THR D C   1 
ATOM   3680 O  O   . THR D 1 88  ? 27.838  6.632   -4.213  1.00 36.19 ? 88  THR D O   1 
ATOM   3681 C  CB  . THR D 1 88  ? 26.108  4.572   -5.534  1.00 36.28 ? 88  THR D CB  1 
ATOM   3682 O  OG1 . THR D 1 88  ? 24.884  3.831   -5.480  1.00 36.67 ? 88  THR D OG1 1 
ATOM   3683 C  CG2 . THR D 1 88  ? 26.954  4.043   -6.680  1.00 36.27 ? 88  THR D CG2 1 
ATOM   3684 N  N   . ALA D 1 89  ? 29.250  4.874   -4.218  1.00 36.88 ? 89  ALA D N   1 
ATOM   3685 C  CA  . ALA D 1 89  ? 30.464  5.678   -4.330  1.00 36.97 ? 89  ALA D CA  1 
ATOM   3686 C  C   . ALA D 1 89  ? 30.836  5.855   -5.797  1.00 37.03 ? 89  ALA D C   1 
ATOM   3687 O  O   . ALA D 1 89  ? 30.797  4.898   -6.577  1.00 36.93 ? 89  ALA D O   1 
ATOM   3688 C  CB  . ALA D 1 89  ? 31.608  5.019   -3.571  1.00 36.89 ? 89  ALA D CB  1 
ATOM   3689 N  N   . ASP D 1 90  ? 31.201  7.081   -6.164  1.00 37.22 ? 90  ASP D N   1 
ATOM   3690 C  CA  . ASP D 1 90  ? 31.645  7.392   -7.524  1.00 37.61 ? 90  ASP D CA  1 
ATOM   3691 C  C   . ASP D 1 90  ? 33.108  6.974   -7.737  1.00 37.68 ? 90  ASP D C   1 
ATOM   3692 O  O   . ASP D 1 90  ? 33.715  6.349   -6.858  1.00 37.57 ? 90  ASP D O   1 
ATOM   3693 C  CB  . ASP D 1 90  ? 31.442  8.888   -7.818  1.00 37.52 ? 90  ASP D CB  1 
ATOM   3694 C  CG  . ASP D 1 90  ? 32.339  9.792   -6.977  1.00 38.02 ? 90  ASP D CG  1 
ATOM   3695 O  OD1 . ASP D 1 90  ? 33.250  9.288   -6.285  1.00 37.86 ? 90  ASP D OD1 1 
ATOM   3696 O  OD2 . ASP D 1 90  ? 32.130  11.021  -7.015  1.00 38.28 ? 90  ASP D OD2 1 
ATOM   3697 N  N   . LYS D 1 91  ? 33.661  7.330   -8.897  1.00 37.90 ? 91  LYS D N   1 
ATOM   3698 C  CA  . LYS D 1 91  ? 35.049  7.011   -9.263  1.00 38.10 ? 91  LYS D CA  1 
ATOM   3699 C  C   . LYS D 1 91  ? 36.101  7.522   -8.276  1.00 38.12 ? 91  LYS D C   1 
ATOM   3700 O  O   . LYS D 1 91  ? 37.183  6.940   -8.170  1.00 38.23 ? 91  LYS D O   1 
ATOM   3701 C  CB  . LYS D 1 91  ? 35.382  7.553   -10.667 1.00 38.12 ? 91  LYS D CB  1 
ATOM   3702 C  CG  . LYS D 1 91  ? 35.156  9.061   -10.846 1.00 38.40 ? 91  LYS D CG  1 
ATOM   3703 C  CD  . LYS D 1 91  ? 35.921  9.628   -12.029 1.00 38.61 ? 91  LYS D CD  1 
ATOM   3704 C  CE  . LYS D 1 91  ? 35.503  11.065  -12.304 1.00 38.76 ? 91  LYS D CE  1 
ATOM   3705 N  NZ  . LYS D 1 91  ? 36.588  11.851  -12.935 1.00 39.07 ? 91  LYS D NZ  1 
ATOM   3706 N  N   . ASP D 1 92  ? 35.792  8.618   -7.584  1.00 37.99 ? 92  ASP D N   1 
ATOM   3707 C  CA  . ASP D 1 92  ? 36.710  9.214   -6.616  1.00 38.00 ? 92  ASP D CA  1 
ATOM   3708 C  C   . ASP D 1 92  ? 36.479  8.693   -5.198  1.00 37.74 ? 92  ASP D C   1 
ATOM   3709 O  O   . ASP D 1 92  ? 37.147  9.134   -4.263  1.00 37.63 ? 92  ASP D O   1 
ATOM   3710 C  CB  . ASP D 1 92  ? 36.576  10.741  -6.639  1.00 38.17 ? 92  ASP D CB  1 
ATOM   3711 C  CG  . ASP D 1 92  ? 37.007  11.350  -7.963  1.00 38.79 ? 92  ASP D CG  1 
ATOM   3712 O  OD1 . ASP D 1 92  ? 37.841  10.743  -8.676  1.00 39.22 ? 92  ASP D OD1 1 
ATOM   3713 O  OD2 . ASP D 1 92  ? 36.515  12.454  -8.294  1.00 39.17 ? 92  ASP D OD2 1 
ATOM   3714 N  N   . GLY D 1 93  ? 35.534  7.763   -5.042  1.00 37.26 ? 93  GLY D N   1 
ATOM   3715 C  CA  . GLY D 1 93  ? 35.251  7.127   -3.759  1.00 37.25 ? 93  GLY D CA  1 
ATOM   3716 C  C   . GLY D 1 93  ? 34.269  7.886   -2.887  1.00 37.03 ? 93  GLY D C   1 
ATOM   3717 O  O   . GLY D 1 93  ? 34.176  7.633   -1.680  1.00 37.16 ? 93  GLY D O   1 
ATOM   3718 N  N   . VAL D 1 94  ? 33.518  8.799   -3.502  1.00 36.84 ? 94  VAL D N   1 
ATOM   3719 C  CA  . VAL D 1 94  ? 32.593  9.664   -2.782  1.00 36.89 ? 94  VAL D CA  1 
ATOM   3720 C  C   . VAL D 1 94  ? 31.142  9.256   -3.041  1.00 36.86 ? 94  VAL D C   1 
ATOM   3721 O  O   . VAL D 1 94  ? 30.722  9.110   -4.194  1.00 36.70 ? 94  VAL D O   1 
ATOM   3722 C  CB  . VAL D 1 94  ? 32.783  11.142  -3.183  1.00 36.79 ? 94  VAL D CB  1 
ATOM   3723 C  CG1 . VAL D 1 94  ? 31.704  12.021  -2.550  1.00 36.77 ? 94  VAL D CG1 1 
ATOM   3724 C  CG2 . VAL D 1 94  ? 34.164  11.625  -2.770  1.00 36.90 ? 94  VAL D CG2 1 
ATOM   3725 N  N   . ALA D 1 95  ? 30.385  9.103   -1.960  1.00 37.09 ? 95  ALA D N   1 
ATOM   3726 C  CA  . ALA D 1 95  ? 28.957  8.822   -2.037  1.00 37.53 ? 95  ALA D CA  1 
ATOM   3727 C  C   . ALA D 1 95  ? 28.175  10.042  -1.578  1.00 37.84 ? 95  ALA D C   1 
ATOM   3728 O  O   . ALA D 1 95  ? 28.282  10.466  -0.430  1.00 38.40 ? 95  ALA D O   1 
ATOM   3729 C  CB  . ALA D 1 95  ? 28.604  7.620   -1.197  1.00 37.46 ? 95  ALA D CB  1 
ATOM   3730 N  N   . ASP D 1 96  ? 27.402  10.601  -2.503  1.00 38.40 ? 96  ASP D N   1 
ATOM   3731 C  CA  . ASP D 1 96  ? 26.517  11.719  -2.240  1.00 38.48 ? 96  ASP D CA  1 
ATOM   3732 C  C   . ASP D 1 96  ? 25.167  11.100  -1.881  1.00 38.46 ? 96  ASP D C   1 
ATOM   3733 O  O   . ASP D 1 96  ? 24.444  10.641  -2.766  1.00 38.85 ? 96  ASP D O   1 
ATOM   3734 C  CB  . ASP D 1 96  ? 26.420  12.573  -3.509  1.00 38.92 ? 96  ASP D CB  1 
ATOM   3735 C  CG  . ASP D 1 96  ? 25.978  13.993  -3.242  1.00 39.36 ? 96  ASP D CG  1 
ATOM   3736 O  OD1 . ASP D 1 96  ? 25.156  14.207  -2.326  1.00 43.29 ? 96  ASP D OD1 1 
ATOM   3737 O  OD2 . ASP D 1 96  ? 26.450  14.897  -3.978  1.00 40.67 ? 96  ASP D OD2 1 
ATOM   3738 N  N   . VAL D 1 97  ? 24.837  11.076  -0.591  1.00 37.85 ? 97  VAL D N   1 
ATOM   3739 C  CA  . VAL D 1 97  ? 23.685  10.313  -0.090  1.00 37.51 ? 97  VAL D CA  1 
ATOM   3740 C  C   . VAL D 1 97  ? 22.401  11.148  -0.037  1.00 37.01 ? 97  VAL D C   1 
ATOM   3741 O  O   . VAL D 1 97  ? 22.386  12.244  0.509   1.00 35.90 ? 97  VAL D O   1 
ATOM   3742 C  CB  . VAL D 1 97  ? 23.960  9.717   1.319   1.00 37.59 ? 97  VAL D CB  1 
ATOM   3743 C  CG1 . VAL D 1 97  ? 22.741  8.944   1.833   1.00 37.50 ? 97  VAL D CG1 1 
ATOM   3744 C  CG2 . VAL D 1 97  ? 25.183  8.806   1.288   1.00 37.69 ? 97  VAL D CG2 1 
ATOM   3745 N  N   . SER D 1 98  ? 21.333  10.617  -0.628  1.00 37.10 ? 98  SER D N   1 
ATOM   3746 C  CA  . SER D 1 98  ? 19.998  11.188  -0.496  1.00 37.26 ? 98  SER D CA  1 
ATOM   3747 C  C   . SER D 1 98  ? 18.997  10.038  -0.478  1.00 37.32 ? 98  SER D C   1 
ATOM   3748 O  O   . SER D 1 98  ? 18.835  9.335   -1.482  1.00 36.79 ? 98  SER D O   1 
ATOM   3749 C  CB  . SER D 1 98  ? 19.692  12.155  -1.645  1.00 37.30 ? 98  SER D CB  1 
ATOM   3750 O  OG  . SER D 1 98  ? 18.441  12.802  -1.456  1.00 37.10 ? 98  SER D OG  1 
ATOM   3751 N  N   . ILE D 1 99  ? 18.354  9.845   0.670   1.00 37.32 ? 99  ILE D N   1 
ATOM   3752 C  CA  . ILE D 1 99  ? 17.398  8.763   0.878   1.00 37.63 ? 99  ILE D CA  1 
ATOM   3753 C  C   . ILE D 1 99  ? 16.168  9.309   1.614   1.00 37.70 ? 99  ILE D C   1 
ATOM   3754 O  O   . ILE D 1 99  ? 16.276  10.237  2.422   1.00 37.26 ? 99  ILE D O   1 
ATOM   3755 C  CB  . ILE D 1 99  ? 18.052  7.610   1.695   1.00 37.93 ? 99  ILE D CB  1 
ATOM   3756 C  CG1 . ILE D 1 99  ? 19.137  6.913   0.870   1.00 38.15 ? 99  ILE D CG1 1 
ATOM   3757 C  CG2 . ILE D 1 99  ? 17.020  6.581   2.154   1.00 37.90 ? 99  ILE D CG2 1 
ATOM   3758 C  CD1 . ILE D 1 99  ? 20.061  6.043   1.684   1.00 38.33 ? 99  ILE D CD1 1 
ATOM   3759 N  N   . GLU D 1 100 ? 15.000  8.745   1.314   1.00 37.74 ? 100 GLU D N   1 
ATOM   3760 C  CA  . GLU D 1 100 ? 13.804  8.977   2.115   1.00 38.15 ? 100 GLU D CA  1 
ATOM   3761 C  C   . GLU D 1 100 ? 13.258  7.618   2.554   1.00 37.97 ? 100 GLU D C   1 
ATOM   3762 O  O   . GLU D 1 100 ? 13.045  6.737   1.717   1.00 38.11 ? 100 GLU D O   1 
ATOM   3763 C  CB  . GLU D 1 100 ? 12.750  9.747   1.317   1.00 38.33 ? 100 GLU D CB  1 
ATOM   3764 C  CG  . GLU D 1 100 ? 11.659  10.350  2.190   1.00 38.98 ? 100 GLU D CG  1 
ATOM   3765 C  CD  . GLU D 1 100 ? 10.538  10.967  1.390   1.00 39.92 ? 100 GLU D CD  1 
ATOM   3766 O  OE1 . GLU D 1 100 ? 9.849   10.227  0.648   1.00 43.54 ? 100 GLU D OE1 1 
ATOM   3767 O  OE2 . GLU D 1 100 ? 10.328  12.194  1.516   1.00 43.33 ? 100 GLU D OE2 1 
ATOM   3768 N  N   . ASP D 1 101 ? 13.041  7.447   3.856   1.00 37.78 ? 101 ASP D N   1 
ATOM   3769 C  CA  . ASP D 1 101 ? 12.543  6.183   4.395   1.00 37.47 ? 101 ASP D CA  1 
ATOM   3770 C  C   . ASP D 1 101 ? 11.373  6.410   5.350   1.00 37.16 ? 101 ASP D C   1 
ATOM   3771 O  O   . ASP D 1 101 ? 11.426  7.284   6.208   1.00 36.95 ? 101 ASP D O   1 
ATOM   3772 C  CB  . ASP D 1 101 ? 13.651  5.426   5.125   1.00 37.87 ? 101 ASP D CB  1 
ATOM   3773 C  CG  . ASP D 1 101 ? 13.275  3.987   5.402   1.00 38.07 ? 101 ASP D CG  1 
ATOM   3774 O  OD1 . ASP D 1 101 ? 13.347  3.168   4.465   1.00 41.38 ? 101 ASP D OD1 1 
ATOM   3775 O  OD2 . ASP D 1 101 ? 12.872  3.675   6.534   1.00 37.72 ? 101 ASP D OD2 1 
ATOM   3776 N  N   . SER D 1 102 ? 10.325  5.603   5.195   1.00 36.95 ? 102 SER D N   1 
ATOM   3777 C  CA  . SER D 1 102 ? 9.118   5.728   6.012   1.00 36.90 ? 102 SER D CA  1 
ATOM   3778 C  C   . SER D 1 102 ? 8.965   4.629   7.077   1.00 36.63 ? 102 SER D C   1 
ATOM   3779 O  O   . SER D 1 102 ? 7.899   4.508   7.698   1.00 36.93 ? 102 SER D O   1 
ATOM   3780 C  CB  . SER D 1 102 ? 7.908   5.718   5.094   1.00 36.95 ? 102 SER D CB  1 
ATOM   3781 O  OG  . SER D 1 102 ? 7.904   4.526   4.333   1.00 38.38 ? 102 SER D OG  1 
ATOM   3782 N  N   . VAL D 1 103 ? 10.014  3.834   7.286   1.00 36.13 ? 103 VAL D N   1 
ATOM   3783 C  CA  . VAL D 1 103 ? 10.001  2.767   8.289   1.00 35.84 ? 103 VAL D CA  1 
ATOM   3784 C  C   . VAL D 1 103 ? 10.784  3.180   9.542   1.00 35.60 ? 103 VAL D C   1 
ATOM   3785 O  O   . VAL D 1 103 ? 10.321  2.961   10.662  1.00 35.23 ? 103 VAL D O   1 
ATOM   3786 C  CB  . VAL D 1 103 ? 10.556  1.445   7.716   1.00 36.03 ? 103 VAL D CB  1 
ATOM   3787 C  CG1 . VAL D 1 103 ? 10.582  0.359   8.790   1.00 36.74 ? 103 VAL D CG1 1 
ATOM   3788 C  CG2 . VAL D 1 103 ? 9.706   0.986   6.531   1.00 36.41 ? 103 VAL D CG2 1 
ATOM   3789 N  N   . ILE D 1 104 ? 11.970  3.758   9.359   1.00 35.07 ? 104 ILE D N   1 
ATOM   3790 C  CA  . ILE D 1 104 ? 12.699  4.342   10.494  1.00 35.02 ? 104 ILE D CA  1 
ATOM   3791 C  C   . ILE D 1 104 ? 11.958  5.552   11.051  1.00 34.72 ? 104 ILE D C   1 
ATOM   3792 O  O   . ILE D 1 104 ? 11.152  6.179   10.362  1.00 33.78 ? 104 ILE D O   1 
ATOM   3793 C  CB  . ILE D 1 104 ? 14.161  4.762   10.152  1.00 34.85 ? 104 ILE D CB  1 
ATOM   3794 C  CG1 . ILE D 1 104 ? 14.202  5.799   9.023   1.00 35.42 ? 104 ILE D CG1 1 
ATOM   3795 C  CG2 . ILE D 1 104 ? 14.985  3.545   9.813   1.00 35.36 ? 104 ILE D CG2 1 
ATOM   3796 C  CD1 . ILE D 1 104 ? 15.564  6.441   8.840   1.00 35.59 ? 104 ILE D CD1 1 
ATOM   3797 N  N   . SER D 1 105 ? 12.233  5.863   12.313  1.00 34.46 ? 105 SER D N   1 
ATOM   3798 C  CA  . SER D 1 105 ? 11.701  7.063   12.945  1.00 34.80 ? 105 SER D CA  1 
ATOM   3799 C  C   . SER D 1 105 ? 12.755  7.629   13.883  1.00 34.75 ? 105 SER D C   1 
ATOM   3800 O  O   . SER D 1 105 ? 13.738  6.952   14.208  1.00 34.50 ? 105 SER D O   1 
ATOM   3801 C  CB  . SER D 1 105 ? 10.402  6.751   13.699  1.00 34.75 ? 105 SER D CB  1 
ATOM   3802 O  OG  . SER D 1 105 ? 9.794   7.926   14.220  1.00 34.14 ? 105 SER D OG  1 
ATOM   3803 N  N   . LEU D 1 106 ? 12.564  8.881   14.282  1.00 34.91 ? 106 LEU D N   1 
ATOM   3804 C  CA  . LEU D 1 106 ? 13.404  9.506   15.296  1.00 35.55 ? 106 LEU D CA  1 
ATOM   3805 C  C   . LEU D 1 106 ? 12.711  9.508   16.659  1.00 35.89 ? 106 LEU D C   1 
ATOM   3806 O  O   . LEU D 1 106 ? 13.253  10.031  17.635  1.00 36.32 ? 106 LEU D O   1 
ATOM   3807 C  CB  . LEU D 1 106 ? 13.779  10.932  14.875  1.00 35.52 ? 106 LEU D CB  1 
ATOM   3808 C  CG  . LEU D 1 106 ? 14.533  11.054  13.545  1.00 35.86 ? 106 LEU D CG  1 
ATOM   3809 C  CD1 . LEU D 1 106 ? 14.928  12.498  13.290  1.00 36.23 ? 106 LEU D CD1 1 
ATOM   3810 C  CD2 . LEU D 1 106 ? 15.761  10.147  13.485  1.00 36.72 ? 106 LEU D CD2 1 
ATOM   3811 N  N   . SER D 1 107 ? 11.513  8.925   16.727  1.00 36.05 ? 107 SER D N   1 
ATOM   3812 C  CA  . SER D 1 107 ? 10.780  8.787   17.980  1.00 36.03 ? 107 SER D CA  1 
ATOM   3813 C  C   . SER D 1 107 ? 10.029  7.451   18.039  1.00 36.11 ? 107 SER D C   1 
ATOM   3814 O  O   . SER D 1 107 ? 9.894   6.755   17.034  1.00 35.77 ? 107 SER D O   1 
ATOM   3815 C  CB  . SER D 1 107 ? 9.805   9.957   18.158  1.00 36.33 ? 107 SER D CB  1 
ATOM   3816 O  OG  . SER D 1 107 ? 8.623   9.763   17.404  1.00 37.07 ? 107 SER D OG  1 
ATOM   3817 N  N   . GLY D 1 108 ? 9.560   7.093   19.231  1.00 36.24 ? 108 GLY D N   1 
ATOM   3818 C  CA  . GLY D 1 108 ? 8.780   5.873   19.428  1.00 36.51 ? 108 GLY D CA  1 
ATOM   3819 C  C   . GLY D 1 108 ? 9.575   4.581   19.337  1.00 36.74 ? 108 GLY D C   1 
ATOM   3820 O  O   . GLY D 1 108 ? 10.802  4.582   19.472  1.00 36.76 ? 108 GLY D O   1 
ATOM   3821 N  N   . ASP D 1 109 ? 8.863   3.483   19.088  1.00 37.18 ? 109 ASP D N   1 
ATOM   3822 C  CA  . ASP D 1 109 ? 9.453   2.132   19.026  1.00 37.33 ? 109 ASP D CA  1 
ATOM   3823 C  C   . ASP D 1 109 ? 10.460  1.929   17.893  1.00 37.25 ? 109 ASP D C   1 
ATOM   3824 O  O   . ASP D 1 109 ? 11.417  1.166   18.044  1.00 37.21 ? 109 ASP D O   1 
ATOM   3825 C  CB  . ASP D 1 109 ? 8.350   1.072   18.911  1.00 37.39 ? 109 ASP D CB  1 
ATOM   3826 C  CG  . ASP D 1 109 ? 7.497   0.978   20.161  1.00 38.11 ? 109 ASP D CG  1 
ATOM   3827 O  OD1 . ASP D 1 109 ? 7.968   1.402   21.238  1.00 39.71 ? 109 ASP D OD1 1 
ATOM   3828 O  OD2 . ASP D 1 109 ? 6.359   0.472   20.067  1.00 37.68 ? 109 ASP D OD2 1 
ATOM   3829 N  N   . HIS D 1 110 ? 10.256  2.615   16.768  1.00 37.10 ? 110 HIS D N   1 
ATOM   3830 C  CA  . HIS D 1 110 ? 11.189  2.543   15.648  1.00 37.01 ? 110 HIS D CA  1 
ATOM   3831 C  C   . HIS D 1 110 ? 12.316  3.579   15.740  1.00 36.63 ? 110 HIS D C   1 
ATOM   3832 O  O   . HIS D 1 110 ? 13.035  3.772   14.765  1.00 36.95 ? 110 HIS D O   1 
ATOM   3833 C  CB  . HIS D 1 110 ? 10.445  2.719   14.312  1.00 37.41 ? 110 HIS D CB  1 
ATOM   3834 C  CG  . HIS D 1 110 ? 9.618   1.535   13.911  1.00 37.57 ? 110 HIS D CG  1 
ATOM   3835 N  ND1 . HIS D 1 110 ? 9.160   1.354   12.623  1.00 37.57 ? 110 HIS D ND1 1 
ATOM   3836 C  CD2 . HIS D 1 110 ? 9.192   0.461   14.616  1.00 37.37 ? 110 HIS D CD2 1 
ATOM   3837 C  CE1 . HIS D 1 110 ? 8.474   0.227   12.556  1.00 37.56 ? 110 HIS D CE1 1 
ATOM   3838 N  NE2 . HIS D 1 110 ? 8.480   -0.336  13.751  1.00 37.87 ? 110 HIS D NE2 1 
ATOM   3839 N  N   . ALA D 1 111 ? 12.486  4.230   16.898  1.00 36.20 ? 111 ALA D N   1 
ATOM   3840 C  CA  . ALA D 1 111 ? 13.485  5.294   17.030  1.00 35.90 ? 111 ALA D CA  1 
ATOM   3841 C  C   . ALA D 1 111 ? 14.898  4.754   16.827  1.00 35.37 ? 111 ALA D C   1 
ATOM   3842 O  O   . ALA D 1 111 ? 15.264  3.726   17.408  1.00 34.90 ? 111 ALA D O   1 
ATOM   3843 C  CB  . ALA D 1 111 ? 13.392  5.968   18.379  1.00 35.89 ? 111 ALA D CB  1 
ATOM   3844 N  N   . ILE D 1 112 ? 15.672  5.463   16.012  1.00 34.95 ? 112 ILE D N   1 
ATOM   3845 C  CA  . ILE D 1 112 ? 17.058  5.093   15.720  1.00 35.27 ? 112 ILE D CA  1 
ATOM   3846 C  C   . ILE D 1 112 ? 18.063  5.960   16.481  1.00 34.80 ? 112 ILE D C   1 
ATOM   3847 O  O   . ILE D 1 112 ? 19.271  5.749   16.380  1.00 34.41 ? 112 ILE D O   1 
ATOM   3848 C  CB  . ILE D 1 112 ? 17.343  5.100   14.204  1.00 34.97 ? 112 ILE D CB  1 
ATOM   3849 C  CG1 . ILE D 1 112 ? 17.230  6.516   13.618  1.00 35.47 ? 112 ILE D CG1 1 
ATOM   3850 C  CG2 . ILE D 1 112 ? 16.412  4.093   13.503  1.00 35.13 ? 112 ILE D CG2 1 
ATOM   3851 C  CD1 . ILE D 1 112 ? 17.563  6.601   12.148  1.00 36.13 ? 112 ILE D CD1 1 
ATOM   3852 N  N   . ILE D 1 113 ? 17.550  6.922   17.244  1.00 34.79 ? 113 ILE D N   1 
ATOM   3853 C  CA  . ILE D 1 113 ? 18.374  7.750   18.119  1.00 35.10 ? 113 ILE D CA  1 
ATOM   3854 C  C   . ILE D 1 113 ? 19.087  6.846   19.126  1.00 34.70 ? 113 ILE D C   1 
ATOM   3855 O  O   . ILE D 1 113 ? 18.461  5.993   19.762  1.00 34.52 ? 113 ILE D O   1 
ATOM   3856 C  CB  . ILE D 1 113 ? 17.526  8.819   18.879  1.00 35.18 ? 113 ILE D CB  1 
ATOM   3857 C  CG1 . ILE D 1 113 ? 16.837  9.791   17.907  1.00 36.66 ? 113 ILE D CG1 1 
ATOM   3858 C  CG2 . ILE D 1 113 ? 18.384  9.582   19.905  1.00 35.36 ? 113 ILE D CG2 1 
ATOM   3859 C  CD1 . ILE D 1 113 ? 17.740  10.627  17.075  1.00 36.14 ? 113 ILE D CD1 1 
ATOM   3860 N  N   . GLY D 1 114 ? 20.405  7.016   19.247  1.00 34.61 ? 114 GLY D N   1 
ATOM   3861 C  CA  . GLY D 1 114 ? 21.199  6.202   20.165  1.00 34.35 ? 114 GLY D CA  1 
ATOM   3862 C  C   . GLY D 1 114 ? 21.614  4.852   19.607  1.00 34.40 ? 114 GLY D C   1 
ATOM   3863 O  O   . GLY D 1 114 ? 22.246  4.070   20.307  1.00 33.74 ? 114 GLY D O   1 
ATOM   3864 N  N   . ARG D 1 115 ? 21.239  4.567   18.359  1.00 34.68 ? 115 ARG D N   1 
ATOM   3865 C  CA  . ARG D 1 115 ? 21.662  3.337   17.682  1.00 34.80 ? 115 ARG D CA  1 
ATOM   3866 C  C   . ARG D 1 115 ? 22.796  3.695   16.702  1.00 34.97 ? 115 ARG D C   1 
ATOM   3867 O  O   . ARG D 1 115 ? 23.235  4.850   16.662  1.00 36.05 ? 115 ARG D O   1 
ATOM   3868 C  CB  . ARG D 1 115 ? 20.461  2.647   17.018  1.00 35.20 ? 115 ARG D CB  1 
ATOM   3869 C  CG  . ARG D 1 115 ? 19.302  2.434   18.023  1.00 34.73 ? 115 ARG D CG  1 
ATOM   3870 C  CD  . ARG D 1 115 ? 18.184  1.547   17.547  1.00 35.30 ? 115 ARG D CD  1 
ATOM   3871 N  NE  . ARG D 1 115 ? 17.120  1.460   18.553  1.00 34.67 ? 115 ARG D NE  1 
ATOM   3872 C  CZ  . ARG D 1 115 ? 17.088  0.610   19.580  1.00 35.01 ? 115 ARG D CZ  1 
ATOM   3873 N  NH1 . ARG D 1 115 ? 18.068  -0.258  19.781  1.00 34.80 ? 115 ARG D NH1 1 
ATOM   3874 N  NH2 . ARG D 1 115 ? 16.053  0.624   20.425  1.00 34.68 ? 115 ARG D NH2 1 
ATOM   3875 N  N   . THR D 1 116 ? 23.292  2.733   15.932  1.00 34.85 ? 116 THR D N   1 
ATOM   3876 C  CA  . THR D 1 116 ? 24.466  2.974   15.074  1.00 34.96 ? 116 THR D CA  1 
ATOM   3877 C  C   . THR D 1 116 ? 24.149  2.845   13.578  1.00 34.92 ? 116 THR D C   1 
ATOM   3878 O  O   . THR D 1 116 ? 23.500  1.907   13.159  1.00 33.93 ? 116 THR D O   1 
ATOM   3879 C  CB  . THR D 1 116 ? 25.605  2.023   15.426  1.00 35.11 ? 116 THR D CB  1 
ATOM   3880 O  OG1 . THR D 1 116 ? 26.033  2.298   16.760  1.00 35.93 ? 116 THR D OG1 1 
ATOM   3881 C  CG2 . THR D 1 116 ? 26.800  2.189   14.467  1.00 35.20 ? 116 THR D CG2 1 
ATOM   3882 N  N   . LEU D 1 117 ? 24.632  3.797   12.787  1.00 34.46 ? 117 LEU D N   1 
ATOM   3883 C  CA  . LEU D 1 117 ? 24.572  3.706   11.337  1.00 34.62 ? 117 LEU D CA  1 
ATOM   3884 C  C   . LEU D 1 117 ? 25.888  3.124   10.852  1.00 34.55 ? 117 LEU D C   1 
ATOM   3885 O  O   . LEU D 1 117 ? 26.961  3.574   11.266  1.00 34.15 ? 117 LEU D O   1 
ATOM   3886 C  CB  . LEU D 1 117 ? 24.388  5.101   10.742  1.00 34.78 ? 117 LEU D CB  1 
ATOM   3887 C  CG  . LEU D 1 117 ? 24.246  5.212   9.224   1.00 35.00 ? 117 LEU D CG  1 
ATOM   3888 C  CD1 . LEU D 1 117 ? 22.984  4.596   8.709   1.00 36.44 ? 117 LEU D CD1 1 
ATOM   3889 C  CD2 . LEU D 1 117 ? 24.305  6.678   8.838   1.00 35.36 ? 117 LEU D CD2 1 
ATOM   3890 N  N   . VAL D 1 118 ? 25.806  2.112   9.989   1.00 34.51 ? 118 VAL D N   1 
ATOM   3891 C  CA  . VAL D 1 118 ? 26.983  1.418   9.471   1.00 34.70 ? 118 VAL D CA  1 
ATOM   3892 C  C   . VAL D 1 118 ? 26.958  1.365   7.949   1.00 34.98 ? 118 VAL D C   1 
ATOM   3893 O  O   . VAL D 1 118 ? 25.929  1.075   7.354   1.00 34.65 ? 118 VAL D O   1 
ATOM   3894 C  CB  . VAL D 1 118 ? 27.046  -0.047  9.991   1.00 34.42 ? 118 VAL D CB  1 
ATOM   3895 C  CG1 . VAL D 1 118 ? 28.305  -0.755  9.467   1.00 35.31 ? 118 VAL D CG1 1 
ATOM   3896 C  CG2 . VAL D 1 118 ? 27.012  -0.080  11.506  1.00 34.35 ? 118 VAL D CG2 1 
ATOM   3897 N  N   . VAL D 1 119 ? 28.103  1.639   7.327   1.00 35.31 ? 119 VAL D N   1 
ATOM   3898 C  CA  . VAL D 1 119 ? 28.255  1.437   5.894   1.00 35.63 ? 119 VAL D CA  1 
ATOM   3899 C  C   . VAL D 1 119 ? 29.129  0.198   5.690   1.00 35.83 ? 119 VAL D C   1 
ATOM   3900 O  O   . VAL D 1 119 ? 30.187  0.070   6.317   1.00 35.63 ? 119 VAL D O   1 
ATOM   3901 C  CB  . VAL D 1 119 ? 28.823  2.691   5.176   1.00 36.16 ? 119 VAL D CB  1 
ATOM   3902 C  CG1 . VAL D 1 119 ? 30.169  3.134   5.749   1.00 36.41 ? 119 VAL D CG1 1 
ATOM   3903 C  CG2 . VAL D 1 119 ? 28.919  2.440   3.659   1.00 35.71 ? 119 VAL D CG2 1 
ATOM   3904 N  N   . HIS D 1 120 ? 28.670  -0.717  4.836   1.00 35.69 ? 120 HIS D N   1 
ATOM   3905 C  CA  . HIS D 1 120 ? 29.305  -2.024  4.673   1.00 35.75 ? 120 HIS D CA  1 
ATOM   3906 C  C   . HIS D 1 120 ? 30.190  -2.127  3.430   1.00 35.96 ? 120 HIS D C   1 
ATOM   3907 O  O   . HIS D 1 120 ? 30.083  -1.330  2.499   1.00 35.54 ? 120 HIS D O   1 
ATOM   3908 C  CB  . HIS D 1 120 ? 28.240  -3.122  4.652   1.00 35.31 ? 120 HIS D CB  1 
ATOM   3909 C  CG  . HIS D 1 120 ? 27.513  -3.277  5.952   1.00 34.81 ? 120 HIS D CG  1 
ATOM   3910 N  ND1 . HIS D 1 120 ? 27.737  -4.333  6.811   1.00 33.94 ? 120 HIS D ND1 1 
ATOM   3911 C  CD2 . HIS D 1 120 ? 26.563  -2.511  6.538   1.00 33.66 ? 120 HIS D CD2 1 
ATOM   3912 C  CE1 . HIS D 1 120 ? 26.960  -4.206  7.873   1.00 34.53 ? 120 HIS D CE1 1 
ATOM   3913 N  NE2 . HIS D 1 120 ? 26.240  -3.106  7.733   1.00 34.30 ? 120 HIS D NE2 1 
ATOM   3914 N  N   . GLU D 1 121 ? 31.051  -3.143  3.433   1.00 36.54 ? 121 GLU D N   1 
ATOM   3915 C  CA  . GLU D 1 121 ? 32.019  -3.369  2.363   1.00 37.26 ? 121 GLU D CA  1 
ATOM   3916 C  C   . GLU D 1 121 ? 31.347  -3.659  1.026   1.00 37.67 ? 121 GLU D C   1 
ATOM   3917 O  O   . GLU D 1 121 ? 31.710  -3.073  0.006   1.00 37.69 ? 121 GLU D O   1 
ATOM   3918 C  CB  . GLU D 1 121 ? 32.928  -4.540  2.733   1.00 37.21 ? 121 GLU D CB  1 
ATOM   3919 C  CG  . GLU D 1 121 ? 34.127  -4.743  1.817   1.00 37.28 ? 121 GLU D CG  1 
ATOM   3920 C  CD  . GLU D 1 121 ? 34.827  -6.061  2.078   1.00 37.65 ? 121 GLU D CD  1 
ATOM   3921 O  OE1 . GLU D 1 121 ? 34.603  -6.662  3.151   1.00 38.22 ? 121 GLU D OE1 1 
ATOM   3922 O  OE2 . GLU D 1 121 ? 35.605  -6.504  1.212   1.00 38.40 ? 121 GLU D OE2 1 
ATOM   3923 N  N   . LYS D 1 122 ? 30.383  -4.576  1.032   1.00 38.25 ? 122 LYS D N   1 
ATOM   3924 C  CA  . LYS D 1 122 ? 29.742  -5.019  -0.208  1.00 38.96 ? 122 LYS D CA  1 
ATOM   3925 C  C   . LYS D 1 122 ? 28.318  -4.507  -0.308  1.00 39.36 ? 122 LYS D C   1 
ATOM   3926 O  O   . LYS D 1 122 ? 27.735  -4.035  0.675   1.00 38.88 ? 122 LYS D O   1 
ATOM   3927 C  CB  . LYS D 1 122 ? 29.734  -6.547  -0.308  1.00 39.03 ? 122 LYS D CB  1 
ATOM   3928 C  CG  . LYS D 1 122 ? 31.103  -7.209  -0.201  1.00 39.56 ? 122 LYS D CG  1 
ATOM   3929 C  CD  . LYS D 1 122 ? 32.046  -6.800  -1.327  1.00 40.13 ? 122 LYS D CD  1 
ATOM   3930 C  CE  . LYS D 1 122 ? 33.374  -7.547  -1.224  1.00 40.08 ? 122 LYS D CE  1 
ATOM   3931 N  NZ  . LYS D 1 122 ? 34.436  -6.990  -2.116  1.00 40.60 ? 122 LYS D NZ  1 
ATOM   3932 N  N   . ALA D 1 123 ? 27.767  -4.621  -1.513  1.00 40.20 ? 123 ALA D N   1 
ATOM   3933 C  CA  . ALA D 1 123 ? 26.398  -4.217  -1.787  1.00 40.88 ? 123 ALA D CA  1 
ATOM   3934 C  C   . ALA D 1 123 ? 25.428  -5.073  -0.993  1.00 41.48 ? 123 ALA D C   1 
ATOM   3935 O  O   . ALA D 1 123 ? 25.689  -6.248  -0.736  1.00 41.66 ? 123 ALA D O   1 
ATOM   3936 C  CB  . ALA D 1 123 ? 26.101  -4.336  -3.271  1.00 40.94 ? 123 ALA D CB  1 
ATOM   3937 N  N   . ASP D 1 124 ? 24.310  -4.469  -0.616  1.00 42.49 ? 124 ASP D N   1 
ATOM   3938 C  CA  . ASP D 1 124 ? 23.243  -5.155  0.097   1.00 42.61 ? 124 ASP D CA  1 
ATOM   3939 C  C   . ASP D 1 124 ? 22.383  -5.975  -0.861  1.00 42.91 ? 124 ASP D C   1 
ATOM   3940 O  O   . ASP D 1 124 ? 22.867  -6.879  -1.543  1.00 43.34 ? 124 ASP D O   1 
ATOM   3941 C  CB  . ASP D 1 124 ? 22.368  -4.126  0.811   1.00 43.08 ? 124 ASP D CB  1 
ATOM   3942 C  CG  . ASP D 1 124 ? 21.501  -4.741  1.882   1.00 44.00 ? 124 ASP D CG  1 
ATOM   3943 O  OD1 . ASP D 1 124 ? 22.063  -5.372  2.807   1.00 45.79 ? 124 ASP D OD1 1 
ATOM   3944 O  OD2 . ASP D 1 124 ? 20.260  -4.578  1.803   1.00 48.08 ? 124 ASP D OD2 1 
ATOM   3945 N  N   . SER D 1 142 ? 32.519  -6.912  5.544   1.00 38.11 ? 142 SER D N   1 
ATOM   3946 C  CA  . SER D 1 142 ? 32.948  -6.201  6.741   1.00 37.78 ? 142 SER D CA  1 
ATOM   3947 C  C   . SER D 1 142 ? 32.298  -4.830  6.878   1.00 37.60 ? 142 SER D C   1 
ATOM   3948 O  O   . SER D 1 142 ? 31.730  -4.284  5.923   1.00 37.94 ? 142 SER D O   1 
ATOM   3949 C  CB  . SER D 1 142 ? 34.466  -6.028  6.742   1.00 38.17 ? 142 SER D CB  1 
ATOM   3950 O  OG  . SER D 1 142 ? 34.854  -4.943  5.912   1.00 39.23 ? 142 SER D OG  1 
ATOM   3951 N  N   . ARG D 1 143 ? 32.406  -4.280  8.081   1.00 36.95 ? 143 ARG D N   1 
ATOM   3952 C  CA  . ARG D 1 143 ? 31.816  -2.992  8.417   1.00 36.46 ? 143 ARG D CA  1 
ATOM   3953 C  C   . ARG D 1 143 ? 32.889  -1.920  8.289   1.00 36.30 ? 143 ARG D C   1 
ATOM   3954 O  O   . ARG D 1 143 ? 33.842  -1.895  9.065   1.00 37.03 ? 143 ARG D O   1 
ATOM   3955 C  CB  . ARG D 1 143 ? 31.245  -3.041  9.838   1.00 36.41 ? 143 ARG D CB  1 
ATOM   3956 C  CG  . ARG D 1 143 ? 30.316  -4.229  10.047  1.00 35.86 ? 143 ARG D CG  1 
ATOM   3957 C  CD  . ARG D 1 143 ? 29.612  -4.195  11.387  1.00 35.86 ? 143 ARG D CD  1 
ATOM   3958 N  NE  . ARG D 1 143 ? 28.669  -5.304  11.510  1.00 35.27 ? 143 ARG D NE  1 
ATOM   3959 C  CZ  . ARG D 1 143 ? 27.870  -5.515  12.555  1.00 35.52 ? 143 ARG D CZ  1 
ATOM   3960 N  NH1 . ARG D 1 143 ? 27.886  -4.698  13.599  1.00 34.72 ? 143 ARG D NH1 1 
ATOM   3961 N  NH2 . ARG D 1 143 ? 27.048  -6.557  12.549  1.00 34.58 ? 143 ARG D NH2 1 
ATOM   3962 N  N   . LEU D 1 144 ? 32.733  -1.040  7.302   1.00 35.84 ? 144 LEU D N   1 
ATOM   3963 C  CA  . LEU D 1 144 ? 33.785  -0.083  6.935   1.00 35.60 ? 144 LEU D CA  1 
ATOM   3964 C  C   . LEU D 1 144 ? 33.872  1.105   7.883   1.00 35.26 ? 144 LEU D C   1 
ATOM   3965 O  O   . LEU D 1 144 ? 34.961  1.580   8.196   1.00 35.35 ? 144 LEU D O   1 
ATOM   3966 C  CB  . LEU D 1 144 ? 33.561  0.431   5.510   1.00 35.45 ? 144 LEU D CB  1 
ATOM   3967 C  CG  . LEU D 1 144 ? 33.547  -0.616  4.391   1.00 35.44 ? 144 LEU D CG  1 
ATOM   3968 C  CD1 . LEU D 1 144 ? 33.154  0.043   3.075   1.00 35.50 ? 144 LEU D CD1 1 
ATOM   3969 C  CD2 . LEU D 1 144 ? 34.899  -1.305  4.268   1.00 35.83 ? 144 LEU D CD2 1 
ATOM   3970 N  N   . ALA D 1 145 ? 32.716  1.590   8.319   1.00 34.92 ? 145 ALA D N   1 
ATOM   3971 C  CA  . ALA D 1 145 ? 32.649  2.759   9.177   1.00 34.95 ? 145 ALA D CA  1 
ATOM   3972 C  C   . ALA D 1 145 ? 31.283  2.826   9.813   1.00 34.84 ? 145 ALA D C   1 
ATOM   3973 O  O   . ALA D 1 145 ? 30.318  2.258   9.295   1.00 34.43 ? 145 ALA D O   1 
ATOM   3974 C  CB  . ALA D 1 145 ? 32.929  4.030   8.387   1.00 35.03 ? 145 ALA D CB  1 
ATOM   3975 N  N   . CYS D 1 146 ? 31.221  3.519   10.941  1.00 35.15 ? 146 CYS D N   1 
ATOM   3976 C  CA  . CYS D 1 146 ? 29.999  3.616   11.711  1.00 35.23 ? 146 CYS D CA  1 
ATOM   3977 C  C   . CYS D 1 146 ? 29.997  4.844   12.595  1.00 34.85 ? 146 CYS D C   1 
ATOM   3978 O  O   . CYS D 1 146 ? 31.028  5.469   12.819  1.00 34.62 ? 146 CYS D O   1 
ATOM   3979 C  CB  . CYS D 1 146 ? 29.801  2.356   12.550  1.00 35.69 ? 146 CYS D CB  1 
ATOM   3980 S  SG  . CYS D 1 146 ? 31.179  1.901   13.632  1.00 39.64 ? 146 CYS D SG  1 
ATOM   3981 N  N   . GLY D 1 147 ? 28.812  5.183   13.083  1.00 34.63 ? 147 GLY D N   1 
ATOM   3982 C  CA  . GLY D 1 147 ? 28.651  6.318   13.973  1.00 34.91 ? 147 GLY D CA  1 
ATOM   3983 C  C   . GLY D 1 147 ? 27.374  6.165   14.764  1.00 34.85 ? 147 GLY D C   1 
ATOM   3984 O  O   . GLY D 1 147 ? 26.383  5.636   14.255  1.00 34.25 ? 147 GLY D O   1 
ATOM   3985 N  N   . VAL D 1 148 ? 27.407  6.607   16.016  1.00 35.31 ? 148 VAL D N   1 
ATOM   3986 C  CA  . VAL D 1 148 ? 26.197  6.623   16.831  1.00 35.89 ? 148 VAL D CA  1 
ATOM   3987 C  C   . VAL D 1 148 ? 25.291  7.736   16.348  1.00 35.84 ? 148 VAL D C   1 
ATOM   3988 O  O   . VAL D 1 148 ? 25.751  8.846   16.063  1.00 35.62 ? 148 VAL D O   1 
ATOM   3989 C  CB  . VAL D 1 148 ? 26.504  6.779   18.338  1.00 36.40 ? 148 VAL D CB  1 
ATOM   3990 C  CG1 . VAL D 1 148 ? 25.205  6.785   19.149  1.00 36.66 ? 148 VAL D CG1 1 
ATOM   3991 C  CG2 . VAL D 1 148 ? 27.400  5.639   18.813  1.00 37.27 ? 148 VAL D CG2 1 
ATOM   3992 N  N   . ILE D 1 149 ? 23.999  7.444   16.251  1.00 35.96 ? 149 ILE D N   1 
ATOM   3993 C  CA  . ILE D 1 149 ? 23.047  8.415   15.724  1.00 35.93 ? 149 ILE D CA  1 
ATOM   3994 C  C   . ILE D 1 149 ? 22.598  9.296   16.883  1.00 35.58 ? 149 ILE D C   1 
ATOM   3995 O  O   . ILE D 1 149 ? 21.915  8.846   17.795  1.00 34.53 ? 149 ILE D O   1 
ATOM   3996 C  CB  . ILE D 1 149 ? 21.830  7.721   15.062  1.00 36.41 ? 149 ILE D CB  1 
ATOM   3997 C  CG1 . ILE D 1 149 ? 22.289  6.814   13.902  1.00 36.33 ? 149 ILE D CG1 1 
ATOM   3998 C  CG2 . ILE D 1 149 ? 20.832  8.768   14.550  1.00 36.33 ? 149 ILE D CG2 1 
ATOM   3999 C  CD1 . ILE D 1 149 ? 21.310  5.730   13.529  1.00 36.73 ? 149 ILE D CD1 1 
ATOM   4000 N  N   . GLY D 1 150 ? 22.979  10.564  16.834  1.00 34.91 ? 150 GLY D N   1 
ATOM   4001 C  CA  . GLY D 1 150 ? 22.742  11.476  17.931  1.00 35.56 ? 150 GLY D CA  1 
ATOM   4002 C  C   . GLY D 1 150 ? 21.742  12.559  17.587  1.00 35.25 ? 150 GLY D C   1 
ATOM   4003 O  O   . GLY D 1 150 ? 21.497  12.844  16.421  1.00 35.38 ? 150 GLY D O   1 
ATOM   4004 N  N   . ILE D 1 151 ? 21.157  13.148  18.619  1.00 35.79 ? 151 ILE D N   1 
ATOM   4005 C  CA  . ILE D 1 151 ? 20.209  14.254  18.462  1.00 35.42 ? 151 ILE D CA  1 
ATOM   4006 C  C   . ILE D 1 151 ? 20.920  15.499  17.938  1.00 35.92 ? 151 ILE D C   1 
ATOM   4007 O  O   . ILE D 1 151 ? 21.915  15.945  18.529  1.00 35.08 ? 151 ILE D O   1 
ATOM   4008 C  CB  . ILE D 1 151 ? 19.526  14.594  19.811  1.00 35.27 ? 151 ILE D CB  1 
ATOM   4009 C  CG1 . ILE D 1 151 ? 18.739  13.388  20.325  1.00 34.71 ? 151 ILE D CG1 1 
ATOM   4010 C  CG2 . ILE D 1 151 ? 18.602  15.802  19.666  1.00 35.90 ? 151 ILE D CG2 1 
ATOM   4011 C  CD1 . ILE D 1 151 ? 18.187  13.551  21.703  1.00 34.48 ? 151 ILE D CD1 1 
ATOM   4012 N  N   . ALA D 1 152 ? 20.398  16.061  16.846  1.00 35.63 ? 152 ALA D N   1 
ATOM   4013 C  CA  . ALA D 1 152 ? 20.964  17.271  16.242  1.00 36.41 ? 152 ALA D CA  1 
ATOM   4014 C  C   . ALA D 1 152 ? 20.078  18.480  16.470  1.00 37.08 ? 152 ALA D C   1 
ATOM   4015 O  O   . ALA D 1 152 ? 18.876  18.362  16.726  1.00 37.50 ? 152 ALA D O   1 
ATOM   4016 C  CB  . ALA D 1 152 ? 21.191  17.070  14.763  1.00 36.28 ? 152 ALA D CB  1 
ATOM   4017 N  N   . GLN D 1 153 ? 20.700  19.647  16.362  1.00 37.29 ? 153 GLN D N   1 
ATOM   4018 C  CA  . GLN D 1 153 ? 20.049  20.926  16.620  1.00 37.74 ? 153 GLN D CA  1 
ATOM   4019 C  C   . GLN D 1 153 ? 19.091  21.291  15.494  1.00 38.11 ? 153 GLN D C   1 
ATOM   4020 O  O   . GLN D 1 153 ? 19.316  20.959  14.332  1.00 38.40 ? 153 GLN D O   1 
ATOM   4021 C  CB  . GLN D 1 153 ? 21.107  22.015  16.773  1.00 37.79 ? 153 GLN D CB  1 
ATOM   4022 C  CG  . GLN D 1 153 ? 20.554  23.358  17.215  1.00 37.69 ? 153 GLN D CG  1 
ATOM   4023 C  CD  . GLN D 1 153 ? 21.637  24.374  17.507  1.00 38.46 ? 153 GLN D CD  1 
ATOM   4024 O  OE1 . GLN D 1 153 ? 22.569  24.553  16.720  1.00 40.09 ? 153 GLN D OE1 1 
ATOM   4025 N  NE2 . GLN D 1 153 ? 21.511  25.062  18.637  1.00 38.52 ? 153 GLN D NE2 1 
ATOM   4026 O  OXT . GLN D 1 153 ? 18.072  21.943  15.726  1.00 39.18 ? 153 GLN D OXT 1 
HETATM 4027 CU CU  . CU1 E 2 .   ? -16.182 2.230   19.775  0.40 38.05 ? 154 CU1 A CU  1 
HETATM 4028 ZN ZN  . ZN  F 3 .   ? -12.231 3.236   14.136  0.75 38.87 ? 155 ZN  A ZN  1 
HETATM 4029 CU CU  . CU1 G 2 .   ? -5.391  -2.131  49.263  0.25 38.20 ? 154 CU1 B CU  1 
HETATM 4030 ZN ZN  . ZN  H 3 .   ? 1.170   -3.175  50.997  0.43 38.48 ? 155 ZN  B ZN  1 
HETATM 4031 O  O   . HOH I 4 .   ? -11.266 5.778   34.529  1.00 25.05 ? 156 HOH A O   1 
HETATM 4032 O  O   . HOH I 4 .   ? -28.846 -3.193  24.730  1.00 38.49 ? 157 HOH A O   1 
HETATM 4033 O  O   . HOH I 4 .   ? -4.184  4.244   14.117  1.00 28.00 ? 158 HOH A O   1 
HETATM 4034 O  O   . HOH I 4 .   ? -12.265 -3.448  33.252  1.00 20.73 ? 159 HOH A O   1 
HETATM 4035 O  O   . HOH I 4 .   ? -7.359  -0.712  3.298   1.00 33.56 ? 160 HOH A O   1 
HETATM 4036 O  O   . HOH I 4 .   ? -3.687  2.268   12.299  1.00 32.03 ? 161 HOH A O   1 
HETATM 4037 O  O   . HOH I 4 .   ? -24.792 1.374   11.892  1.00 30.86 ? 162 HOH A O   1 
HETATM 4038 O  O   . HOH I 4 .   ? -9.237  9.296   14.766  1.00 35.01 ? 163 HOH A O   1 
HETATM 4039 O  O   . HOH I 4 .   ? -13.849 -1.775  12.929  1.00 27.29 ? 164 HOH A O   1 
HETATM 4040 O  O   . HOH I 4 .   ? -12.685 -6.210  8.197   1.00 30.69 ? 165 HOH A O   1 
HETATM 4041 O  O   . HOH I 4 .   ? -24.328 -2.309  32.316  1.00 30.74 ? 166 HOH A O   1 
HETATM 4042 O  O   . HOH I 4 .   ? -0.121  2.688   23.943  1.00 33.76 ? 167 HOH A O   1 
HETATM 4043 O  O   . HOH I 4 .   ? -25.925 8.874   4.729   1.00 37.37 ? 168 HOH A O   1 
HETATM 4044 O  O   . HOH I 4 .   ? -13.759 -8.897  14.849  1.00 31.68 ? 169 HOH A O   1 
HETATM 4045 O  O   . HOH I 4 .   ? -3.418  8.804   24.042  1.00 34.29 ? 170 HOH A O   1 
HETATM 4046 O  O   . HOH I 4 .   ? -31.824 -8.949  22.986  1.00 38.31 ? 171 HOH A O   1 
HETATM 4047 O  O   . HOH I 4 .   ? -17.666 1.117   32.824  1.00 30.74 ? 172 HOH A O   1 
HETATM 4048 O  O   . HOH I 4 .   ? -5.457  -8.372  12.426  1.00 38.55 ? 173 HOH A O   1 
HETATM 4049 O  O   . HOH I 4 .   ? -5.766  7.775   19.262  1.00 36.13 ? 174 HOH A O   1 
HETATM 4050 O  O   . HOH I 4 .   ? 5.500   2.327   17.109  1.00 54.42 ? 175 HOH A O   1 
HETATM 4051 O  O   . HOH I 4 .   ? 0.020   -9.619  31.860  1.00 39.86 ? 176 HOH A O   1 
HETATM 4052 O  O   . HOH I 4 .   ? -13.332 -0.212  34.011  1.00 26.14 ? 177 HOH A O   1 
HETATM 4053 O  O   . HOH I 4 .   ? -8.871  -8.987  13.787  1.00 34.77 ? 178 HOH A O   1 
HETATM 4054 O  O   . HOH I 4 .   ? -27.192 -6.615  12.681  1.00 33.98 ? 179 HOH A O   1 
HETATM 4055 O  O   . HOH I 4 .   ? -14.751 1.883   32.708  1.00 35.37 ? 180 HOH A O   1 
HETATM 4056 O  O   . HOH I 4 .   ? -10.889 8.295   11.100  1.00 35.92 ? 181 HOH A O   1 
HETATM 4057 O  O   . HOH I 4 .   ? -0.471  1.469   27.912  1.00 29.24 ? 182 HOH A O   1 
HETATM 4058 O  O   . HOH I 4 .   ? -21.639 -3.928  8.952   1.00 43.37 ? 183 HOH A O   1 
HETATM 4059 O  O   . HOH I 4 .   ? -27.385 -4.276  14.932  1.00 35.95 ? 184 HOH A O   1 
HETATM 4060 O  O   . HOH I 4 .   ? -17.903 5.066   2.840   1.00 37.75 ? 185 HOH A O   1 
HETATM 4061 O  O   . HOH I 4 .   ? -32.978 -8.831  20.613  1.00 35.35 ? 186 HOH A O   1 
HETATM 4062 O  O   . HOH I 4 .   ? -4.400  12.536  22.384  1.00 46.37 ? 187 HOH A O   1 
HETATM 4063 O  O   . HOH I 4 .   ? -7.915  -12.252 31.088  1.00 37.15 ? 188 HOH A O   1 
HETATM 4064 O  O   . HOH I 4 .   ? -22.377 -11.571 35.890  1.00 53.90 ? 189 HOH A O   1 
HETATM 4065 O  O   . HOH I 4 .   ? 3.699   -10.744 24.853  1.00 45.16 ? 190 HOH A O   1 
HETATM 4066 O  O   . HOH I 4 .   ? 4.004   -4.908  20.581  1.00 36.72 ? 191 HOH A O   1 
HETATM 4067 O  O   . HOH I 4 .   ? 0.314   -7.280  17.795  1.00 38.87 ? 192 HOH A O   1 
HETATM 4068 O  O   . HOH I 4 .   ? -15.442 -17.034 23.226  1.00 44.42 ? 193 HOH A O   1 
HETATM 4069 O  O   . HOH I 4 .   ? -14.102 -14.949 30.840  1.00 42.54 ? 194 HOH A O   1 
HETATM 4070 O  O   . HOH I 4 .   ? -13.755 3.400   30.734  1.00 32.04 ? 195 HOH A O   1 
HETATM 4071 O  O   . HOH I 4 .   ? -9.210  11.686  29.751  1.00 31.54 ? 196 HOH A O   1 
HETATM 4072 O  O   . HOH I 4 .   ? -21.289 11.519  29.754  1.00 47.69 ? 197 HOH A O   1 
HETATM 4073 O  O   . HOH I 4 .   ? -16.548 11.051  23.553  1.00 38.82 ? 198 HOH A O   1 
HETATM 4074 O  O   . HOH I 4 .   ? -7.134  10.635  19.032  1.00 53.52 ? 199 HOH A O   1 
HETATM 4075 O  O   . HOH I 4 .   ? 0.039   9.632   17.617  1.00 44.21 ? 200 HOH A O   1 
HETATM 4076 O  O   . HOH I 4 .   ? -2.137  0.122   11.583  1.00 36.07 ? 201 HOH A O   1 
HETATM 4077 O  O   . HOH I 4 .   ? -3.123  -1.416  9.752   1.00 41.33 ? 202 HOH A O   1 
HETATM 4078 O  O   . HOH I 4 .   ? -13.976 -2.103  5.129   1.00 26.74 ? 203 HOH A O   1 
HETATM 4079 O  O   . HOH I 4 .   ? -6.844  -3.752  2.985   1.00 44.36 ? 204 HOH A O   1 
HETATM 4080 O  O   . HOH I 4 .   ? -18.804 -7.170  10.564  1.00 33.75 ? 205 HOH A O   1 
HETATM 4081 O  O   . HOH I 4 .   ? -15.722 -8.093  12.864  1.00 38.76 ? 206 HOH A O   1 
HETATM 4082 O  O   . HOH I 4 .   ? -19.347 -12.196 18.413  1.00 34.55 ? 207 HOH A O   1 
HETATM 4083 O  O   . HOH I 4 .   ? -21.700 -14.434 18.817  1.00 42.72 ? 208 HOH A O   1 
HETATM 4084 O  O   . HOH I 4 .   ? -27.629 -17.554 24.933  1.00 41.32 ? 209 HOH A O   1 
HETATM 4085 O  O   . HOH I 4 .   ? -29.899 -16.686 17.619  1.00 44.33 ? 210 HOH A O   1 
HETATM 4086 O  O   . HOH I 4 .   ? -11.575 -9.751  13.578  1.00 34.54 ? 211 HOH A O   1 
HETATM 4087 O  O   . HOH I 4 .   ? -17.671 -16.397 18.432  1.00 45.77 ? 212 HOH A O   1 
HETATM 4088 O  O   . HOH I 4 .   ? -21.453 6.786   15.024  1.00 42.39 ? 213 HOH A O   1 
HETATM 4089 O  O   . HOH I 4 .   ? -22.547 -13.048 28.751  1.00 49.82 ? 214 HOH A O   1 
HETATM 4090 O  O   . HOH I 4 .   ? -27.275 -13.226 15.568  1.00 34.83 ? 215 HOH A O   1 
HETATM 4091 O  O   . HOH I 4 .   ? -11.905 3.247   5.275   1.00 39.18 ? 216 HOH A O   1 
HETATM 4092 O  O   . HOH I 4 .   ? -12.689 -5.634  5.556   1.00 40.30 ? 217 HOH A O   1 
HETATM 4093 O  O   . HOH I 4 .   ? 2.909   -1.676  20.006  1.00 33.62 ? 218 HOH A O   1 
HETATM 4094 O  O   . HOH I 4 .   ? 2.897   -7.908  24.619  1.00 40.77 ? 219 HOH A O   1 
HETATM 4095 O  O   . HOH I 4 .   ? 5.369   -1.456  26.499  1.00 47.11 ? 220 HOH A O   1 
HETATM 4096 O  O   . HOH I 4 .   ? 3.482   1.075   26.476  1.00 44.81 ? 221 HOH A O   1 
HETATM 4097 O  O   . HOH I 4 .   ? 0.953   2.820   26.457  1.00 39.72 ? 222 HOH A O   1 
HETATM 4098 O  O   . HOH I 4 .   ? -21.911 12.308  4.356   1.00 44.78 ? 223 HOH A O   1 
HETATM 4099 O  O   . HOH I 4 .   ? -21.975 11.497  7.973   1.00 40.65 ? 224 HOH A O   1 
HETATM 4100 O  O   . HOH I 4 .   ? -13.100 7.778   15.832  1.00 44.42 ? 225 HOH A O   1 
HETATM 4101 O  O   . HOH I 4 .   ? 0.348   -14.564 29.458  1.00 51.61 ? 226 HOH A O   1 
HETATM 4102 O  O   . HOH I 4 .   ? -8.679  -16.089 32.352  1.00 51.35 ? 227 HOH A O   1 
HETATM 4103 O  O   . HOH I 4 .   ? -7.991  -13.386 33.418  1.00 49.96 ? 228 HOH A O   1 
HETATM 4104 O  O   . HOH I 4 .   ? -15.989 -1.731  34.098  1.00 47.15 ? 229 HOH A O   1 
HETATM 4105 O  O   . HOH I 4 .   ? -13.666 -2.036  35.459  1.00 46.05 ? 230 HOH A O   1 
HETATM 4106 O  O   . HOH I 4 .   ? -19.952 -6.353  33.802  0.50 27.48 ? 231 HOH A O   1 
HETATM 4107 O  O   . HOH I 4 .   ? -23.505 7.952   30.499  1.00 55.82 ? 232 HOH A O   1 
HETATM 4108 O  O   . HOH I 4 .   ? -24.982 2.421   28.959  1.00 40.56 ? 233 HOH A O   1 
HETATM 4109 O  O   . HOH I 4 .   ? -25.894 -0.723  28.809  1.00 37.23 ? 234 HOH A O   1 
HETATM 4110 O  O   . HOH I 4 .   ? -24.119 -3.083  34.813  1.00 40.46 ? 235 HOH A O   1 
HETATM 4111 O  O   . HOH I 4 .   ? -28.577 -7.256  31.784  1.00 39.27 ? 236 HOH A O   1 
HETATM 4112 O  O   . HOH I 4 .   ? -19.473 -8.013  33.513  0.50 25.00 ? 237 HOH A O   1 
HETATM 4113 O  O   . HOH I 4 .   ? -11.452 -13.217 33.107  1.00 37.14 ? 238 HOH A O   1 
HETATM 4114 O  O   . HOH I 4 .   ? -1.718  -14.880 21.657  1.00 45.39 ? 239 HOH A O   1 
HETATM 4115 O  O   . HOH I 4 .   ? -28.264 -3.450  22.166  1.00 32.15 ? 240 HOH A O   1 
HETATM 4116 O  O   . HOH I 4 .   ? -9.458  12.588  33.809  1.00 44.31 ? 241 HOH A O   1 
HETATM 4117 O  O   . HOH I 4 .   ? -15.070 5.439   29.781  1.00 28.02 ? 242 HOH A O   1 
HETATM 4118 O  O   . HOH I 4 .   ? -18.489 6.652   36.003  1.00 39.15 ? 243 HOH A O   1 
HETATM 4119 O  O   . HOH I 4 .   ? -19.754 13.938  28.973  1.00 53.54 ? 244 HOH A O   1 
HETATM 4120 O  O   . HOH I 4 .   ? -11.419 11.944  27.824  1.00 39.55 ? 245 HOH A O   1 
HETATM 4121 O  O   . HOH I 4 .   ? -15.100 11.032  21.329  1.00 40.64 ? 246 HOH A O   1 
HETATM 4122 O  O   . HOH I 4 .   ? -17.886 3.870   16.831  1.00 40.74 ? 247 HOH A O   1 
HETATM 4123 O  O   . HOH I 4 .   ? -3.297  8.493   19.811  1.00 44.30 ? 248 HOH A O   1 
HETATM 4124 O  O   . HOH I 4 .   ? -6.804  9.636   8.192   1.00 46.58 ? 249 HOH A O   1 
HETATM 4125 O  O   . HOH I 4 .   ? -19.373 -10.426 14.391  1.00 36.61 ? 250 HOH A O   1 
HETATM 4126 O  O   . HOH I 4 .   ? -28.790 -10.960 27.145  1.00 37.28 ? 251 HOH A O   1 
HETATM 4127 O  O   . HOH I 4 .   ? -16.610 -12.154 17.696  1.00 36.87 ? 252 HOH A O   1 
HETATM 4128 O  O   . HOH I 4 .   ? -4.436  -11.475 13.906  1.00 46.79 ? 253 HOH A O   1 
HETATM 4129 O  O   . HOH I 4 .   ? 1.797   -2.587  28.379  1.00 35.09 ? 254 HOH A O   1 
HETATM 4130 O  O   . HOH I 4 .   ? 1.218   -3.201  30.800  1.00 36.84 ? 255 HOH A O   1 
HETATM 4131 O  O   . HOH I 4 .   ? 4.768   -3.239  28.436  1.00 37.51 ? 256 HOH A O   1 
HETATM 4132 O  O   . HOH I 4 .   ? -13.892 2.770   3.169   1.00 35.72 ? 257 HOH A O   1 
HETATM 4133 O  O   . HOH I 4 .   ? -10.110 4.393   3.642   1.00 46.40 ? 258 HOH A O   1 
HETATM 4134 O  O   . HOH I 4 .   ? -11.478 9.845   13.235  1.00 46.45 ? 259 HOH A O   1 
HETATM 4135 O  O   . HOH I 4 .   ? -24.142 7.744   12.921  1.00 44.56 ? 260 HOH A O   1 
HETATM 4136 O  O   . HOH I 4 .   ? -23.916 9.278   9.678   1.00 42.73 ? 261 HOH A O   1 
HETATM 4137 O  O   . HOH I 4 .   ? -19.828 5.696   17.568  1.00 38.70 ? 262 HOH A O   1 
HETATM 4138 O  O   . HOH I 4 .   ? -22.721 7.036   23.844  1.00 36.92 ? 263 HOH A O   1 
HETATM 4139 O  O   . HOH I 4 .   ? -19.876 3.267   32.544  1.00 49.78 ? 264 HOH A O   1 
HETATM 4140 O  O   . HOH I 4 .   ? -27.864 0.571   27.134  1.00 38.11 ? 265 HOH A O   1 
HETATM 4141 O  O   . HOH I 4 .   ? -29.587 -0.859  25.700  1.00 38.42 ? 266 HOH A O   1 
HETATM 4142 O  O   . HOH I 4 .   ? -22.312 -5.356  35.428  1.00 54.04 ? 267 HOH A O   1 
HETATM 4143 O  O   . HOH I 4 .   ? 1.168   -13.307 20.295  1.00 37.26 ? 268 HOH A O   1 
HETATM 4144 O  O   . HOH I 4 .   ? 7.874   -11.449 23.380  1.00 61.99 ? 269 HOH A O   1 
HETATM 4145 O  O   . HOH I 4 .   ? 6.388   -11.396 25.633  1.00 53.52 ? 270 HOH A O   1 
HETATM 4146 O  O   . HOH I 4 .   ? -8.181  12.391  21.519  1.00 47.11 ? 271 HOH A O   1 
HETATM 4147 O  O   . HOH I 4 .   ? -8.774  9.249   17.327  1.00 40.20 ? 272 HOH A O   1 
HETATM 4148 O  O   . HOH I 4 .   ? -4.301  11.391  20.096  1.00 55.96 ? 273 HOH A O   1 
HETATM 4149 O  O   . HOH I 4 .   ? -1.939  10.491  18.951  1.00 50.45 ? 274 HOH A O   1 
HETATM 4150 O  O   . HOH I 4 .   ? -15.656 13.480  25.124  1.00 57.68 ? 275 HOH A O   1 
HETATM 4151 O  O   . HOH I 4 .   ? -6.768  10.704  11.406  1.00 46.25 ? 276 HOH A O   1 
HETATM 4152 O  O   . HOH I 4 .   ? -14.304 -8.037  9.391   1.00 43.50 ? 277 HOH A O   1 
HETATM 4153 O  O   . HOH I 4 .   ? -15.190 -4.312  4.460   1.00 41.52 ? 278 HOH A O   1 
HETATM 4154 O  O   . HOH I 4 .   ? -4.567  -4.004  9.182   1.00 39.19 ? 279 HOH A O   1 
HETATM 4155 O  O   . HOH I 4 .   ? -7.738  -9.967  5.249   1.00 54.41 ? 280 HOH A O   1 
HETATM 4156 O  O   . HOH I 4 .   ? -18.530 -12.806 14.928  1.00 49.75 ? 281 HOH A O   1 
HETATM 4157 O  O   . HOH I 4 .   ? -19.227 -9.638  11.607  1.00 42.95 ? 282 HOH A O   1 
HETATM 4158 O  O   . HOH I 4 .   ? -20.306 -6.281  8.467   1.00 45.75 ? 283 HOH A O   1 
HETATM 4159 O  O   . HOH I 4 .   ? -15.572 -9.833  16.685  1.00 45.03 ? 284 HOH A O   1 
HETATM 4160 O  O   . HOH I 4 .   ? -22.286 -12.235 12.202  1.00 43.99 ? 285 HOH A O   1 
HETATM 4161 O  O   . HOH I 4 .   ? -23.946 -10.634 10.244  1.00 57.90 ? 286 HOH A O   1 
HETATM 4162 O  O   . HOH I 4 .   ? -21.325 -10.805 9.995   1.00 47.58 ? 287 HOH A O   1 
HETATM 4163 O  O   . HOH I 4 .   ? 2.842   -3.186  17.866  1.00 52.71 ? 288 HOH A O   1 
HETATM 4164 O  O   . HOH I 4 .   ? 7.111   -3.316  27.287  1.00 52.35 ? 289 HOH A O   1 
HETATM 4165 O  O   . HOH I 4 .   ? 5.108   6.781   19.303  1.00 44.98 ? 290 HOH A O   1 
HETATM 4166 O  O   . HOH I 4 .   ? 1.622   6.834   23.730  1.00 48.09 ? 291 HOH A O   1 
HETATM 4167 O  O   . HOH I 4 .   ? -1.515  7.497   21.494  1.00 43.99 ? 292 HOH A O   1 
HETATM 4168 O  O   . HOH I 4 .   ? -0.379  7.485   25.649  1.00 47.24 ? 293 HOH A O   1 
HETATM 4169 O  O   . HOH I 4 .   ? -28.730 -1.486  20.335  1.00 41.07 ? 294 HOH A O   1 
HETATM 4170 O  O   . HOH I 4 .   ? -27.227 -2.108  13.641  1.00 47.29 ? 295 HOH A O   1 
HETATM 4171 O  O   . HOH I 4 .   ? -25.422 1.466   9.266   1.00 35.06 ? 296 HOH A O   1 
HETATM 4172 O  O   . HOH I 4 .   ? -24.376 -4.011  9.281   1.00 44.36 ? 297 HOH A O   1 
HETATM 4173 O  O   . HOH I 4 .   ? -20.585 -3.128  6.577   1.00 62.21 ? 298 HOH A O   1 
HETATM 4174 O  O   . HOH I 4 .   ? -15.619 15.402  7.836   1.00 60.40 ? 299 HOH A O   1 
HETATM 4175 O  O   . HOH I 4 .   ? -17.508 6.587   18.815  1.00 41.50 ? 300 HOH A O   1 
HETATM 4176 O  O   . HOH I 4 .   ? -24.065 10.876  11.761  1.00 58.25 ? 301 HOH A O   1 
HETATM 4177 O  O   . HOH I 4 .   ? 0.144   -11.505 33.601  1.00 51.37 ? 302 HOH A O   1 
HETATM 4178 O  O   . HOH I 4 .   ? -21.519 4.533   30.769  1.00 46.47 ? 303 HOH A O   1 
HETATM 4179 O  O   . HOH I 4 .   ? -22.840 3.759   28.557  1.00 51.65 ? 304 HOH A O   1 
HETATM 4180 O  O   . HOH I 4 .   ? -22.223 6.195   27.804  1.00 56.78 ? 305 HOH A O   1 
HETATM 4181 O  O   . HOH I 4 .   ? -16.236 -13.952 29.494  1.00 52.33 ? 306 HOH A O   1 
HETATM 4182 O  O   . HOH I 4 .   ? -18.466 -13.615 30.519  1.00 44.70 ? 307 HOH A O   1 
HETATM 4183 O  O   . HOH I 4 .   ? 7.761   -11.277 19.168  1.00 48.15 ? 308 HOH A O   1 
HETATM 4184 O  O   . HOH I 4 .   ? 7.077   -3.819  16.979  1.00 51.22 ? 309 HOH A O   1 
HETATM 4185 O  O   . HOH I 4 .   ? 5.553   -3.949  14.692  1.00 45.77 ? 310 HOH A O   1 
HETATM 4186 O  O   . HOH I 4 .   ? -34.859 -10.835 18.682  1.00 59.32 ? 311 HOH A O   1 
HETATM 4187 O  O   . HOH I 4 .   ? -29.884 -6.786  12.965  1.00 50.40 ? 312 HOH A O   1 
HETATM 4188 O  O   . HOH I 4 .   ? -8.517  12.995  18.827  1.00 59.05 ? 313 HOH A O   1 
HETATM 4189 O  O   . HOH I 4 .   ? -8.973  -9.105  10.658  1.00 54.59 ? 314 HOH A O   1 
HETATM 4190 O  O   . HOH I 4 .   ? -9.814  0.117   2.760   1.00 50.97 ? 315 HOH A O   1 
HETATM 4191 O  O   . HOH J 4 .   ? 5.186   1.973   39.711  1.00 28.30 ? 156 HOH B O   1 
HETATM 4192 O  O   . HOH J 4 .   ? -0.378  8.810   51.478  1.00 31.04 ? 157 HOH B O   1 
HETATM 4193 O  O   . HOH J 4 .   ? -11.145 3.731   36.448  1.00 21.00 ? 158 HOH B O   1 
HETATM 4194 O  O   . HOH J 4 .   ? 8.973   5.861   34.664  1.00 22.86 ? 159 HOH B O   1 
HETATM 4195 O  O   . HOH J 4 .   ? 8.451   1.490   36.095  1.00 31.28 ? 160 HOH B O   1 
HETATM 4196 O  O   . HOH J 4 .   ? -13.067 -6.806  50.225  1.00 36.18 ? 161 HOH B O   1 
HETATM 4197 O  O   . HOH J 4 .   ? 1.900   -8.410  37.449  1.00 32.87 ? 162 HOH B O   1 
HETATM 4198 O  O   . HOH J 4 .   ? 12.416  3.528   56.345  1.00 40.72 ? 163 HOH B O   1 
HETATM 4199 O  O   . HOH J 4 .   ? -16.225 3.639   54.990  1.00 31.62 ? 164 HOH B O   1 
HETATM 4200 O  O   . HOH J 4 .   ? 9.634   -0.189  41.205  1.00 43.85 ? 165 HOH B O   1 
HETATM 4201 O  O   . HOH J 4 .   ? 4.001   9.343   49.129  1.00 31.32 ? 166 HOH B O   1 
HETATM 4202 O  O   . HOH J 4 .   ? -1.453  7.092   57.940  1.00 35.60 ? 167 HOH B O   1 
HETATM 4203 O  O   . HOH J 4 .   ? 8.116   8.294   40.491  1.00 27.23 ? 168 HOH B O   1 
HETATM 4204 O  O   . HOH J 4 .   ? 7.605   8.698   47.817  1.00 33.80 ? 169 HOH B O   1 
HETATM 4205 O  O   . HOH J 4 .   ? 7.546   -3.723  45.389  1.00 30.23 ? 170 HOH B O   1 
HETATM 4206 O  O   . HOH J 4 .   ? 7.363   13.963  37.678  1.00 28.60 ? 171 HOH B O   1 
HETATM 4207 O  O   . HOH J 4 .   ? -1.153  10.346  29.608  1.00 38.80 ? 172 HOH B O   1 
HETATM 4208 O  O   . HOH J 4 .   ? 11.250  8.757   41.477  1.00 32.25 ? 173 HOH B O   1 
HETATM 4209 O  O   . HOH J 4 .   ? -6.712  12.225  52.555  1.00 38.04 ? 174 HOH B O   1 
HETATM 4210 O  O   . HOH J 4 .   ? -13.913 16.654  59.877  1.00 47.43 ? 175 HOH B O   1 
HETATM 4211 O  O   . HOH J 4 .   ? -19.810 11.331  52.100  1.00 33.92 ? 176 HOH B O   1 
HETATM 4212 O  O   . HOH J 4 .   ? 2.934   -7.483  42.581  1.00 36.50 ? 177 HOH B O   1 
HETATM 4213 O  O   . HOH J 4 .   ? 0.785   1.735   52.891  1.00 30.36 ? 178 HOH B O   1 
HETATM 4214 O  O   . HOH J 4 .   ? 4.407   15.211  38.644  1.00 37.82 ? 179 HOH B O   1 
HETATM 4215 O  O   . HOH J 4 .   ? -9.119  6.589   61.736  1.00 42.40 ? 180 HOH B O   1 
HETATM 4216 O  O   . HOH J 4 .   ? -8.863  14.640  53.826  1.00 46.49 ? 181 HOH B O   1 
HETATM 4217 O  O   . HOH J 4 .   ? -14.593 1.816   38.118  1.00 34.90 ? 182 HOH B O   1 
HETATM 4218 O  O   . HOH J 4 .   ? -2.203  -12.009 61.288  1.00 38.66 ? 183 HOH B O   1 
HETATM 4219 O  O   . HOH J 4 .   ? 2.966   -7.599  34.985  1.00 47.09 ? 184 HOH B O   1 
HETATM 4220 O  O   . HOH J 4 .   ? 6.186   11.523  32.697  1.00 31.59 ? 185 HOH B O   1 
HETATM 4221 O  O   . HOH J 4 .   ? -12.766 -1.736  38.171  1.00 32.11 ? 186 HOH B O   1 
HETATM 4222 O  O   . HOH J 4 .   ? -20.341 8.683   55.150  1.00 34.69 ? 187 HOH B O   1 
HETATM 4223 O  O   . HOH J 4 .   ? -18.620 8.701   59.720  1.00 38.84 ? 188 HOH B O   1 
HETATM 4224 O  O   . HOH J 4 .   ? 3.527   -5.719  63.029  1.00 34.70 ? 189 HOH B O   1 
HETATM 4225 O  O   . HOH J 4 .   ? 5.720   8.614   33.177  1.00 32.41 ? 190 HOH B O   1 
HETATM 4226 O  O   . HOH J 4 .   ? 6.355   5.617   58.032  1.00 40.24 ? 191 HOH B O   1 
HETATM 4227 O  O   . HOH J 4 .   ? -4.352  10.572  55.490  1.00 37.89 ? 192 HOH B O   1 
HETATM 4228 O  O   . HOH J 4 .   ? -2.391  9.593   57.398  1.00 42.11 ? 193 HOH B O   1 
HETATM 4229 O  O   . HOH J 4 .   ? -2.517  3.756   60.798  1.00 38.49 ? 194 HOH B O   1 
HETATM 4230 O  O   . HOH J 4 .   ? -3.984  -3.707  62.595  1.00 34.04 ? 195 HOH B O   1 
HETATM 4231 O  O   . HOH J 4 .   ? -16.181 -3.112  36.253  1.00 62.71 ? 196 HOH B O   1 
HETATM 4232 O  O   . HOH J 4 .   ? -18.545 3.392   53.790  1.00 31.82 ? 197 HOH B O   1 
HETATM 4233 O  O   . HOH J 4 .   ? -19.369 0.991   53.205  1.00 39.77 ? 198 HOH B O   1 
HETATM 4234 O  O   . HOH J 4 .   ? -11.029 -5.447  34.681  1.00 24.48 ? 199 HOH B O   1 
HETATM 4235 O  O   . HOH J 4 .   ? -10.455 -2.958  39.267  1.00 32.58 ? 200 HOH B O   1 
HETATM 4236 O  O   . HOH J 4 .   ? 1.831   -7.838  47.713  1.00 43.35 ? 201 HOH B O   1 
HETATM 4237 O  O   . HOH J 4 .   ? 10.143  4.161   49.934  1.00 44.83 ? 202 HOH B O   1 
HETATM 4238 O  O   . HOH J 4 .   ? -7.137  17.312  46.234  1.00 42.29 ? 203 HOH B O   1 
HETATM 4239 O  O   . HOH J 4 .   ? -4.382  12.407  51.078  1.00 32.01 ? 204 HOH B O   1 
HETATM 4240 O  O   . HOH J 4 .   ? -5.819  16.497  51.490  1.00 44.51 ? 205 HOH B O   1 
HETATM 4241 O  O   . HOH J 4 .   ? -5.533  -9.963  61.534  1.00 54.33 ? 206 HOH B O   1 
HETATM 4242 O  O   . HOH J 4 .   ? -24.261 -3.540  49.294  1.00 58.55 ? 207 HOH B O   1 
HETATM 4243 O  O   . HOH J 4 .   ? -12.325 0.533   36.379  1.00 28.96 ? 208 HOH B O   1 
HETATM 4244 O  O   . HOH J 4 .   ? -17.703 9.963   42.063  1.00 46.65 ? 209 HOH B O   1 
HETATM 4245 O  O   . HOH J 4 .   ? 10.133  12.485  31.094  1.00 35.59 ? 210 HOH B O   1 
HETATM 4246 O  O   . HOH J 4 .   ? -16.203 13.828  46.771  1.00 44.52 ? 211 HOH B O   1 
HETATM 4247 O  O   . HOH J 4 .   ? 4.470   -7.712  40.162  1.00 50.21 ? 212 HOH B O   1 
HETATM 4248 O  O   . HOH J 4 .   ? 4.703   6.095   56.017  1.00 35.05 ? 213 HOH B O   1 
HETATM 4249 O  O   . HOH J 4 .   ? 5.484   1.958   59.128  1.00 30.91 ? 214 HOH B O   1 
HETATM 4250 O  O   . HOH J 4 .   ? 11.770  0.953   56.179  1.00 36.76 ? 215 HOH B O   1 
HETATM 4251 O  O   . HOH J 4 .   ? 0.258   6.561   55.868  1.00 42.67 ? 216 HOH B O   1 
HETATM 4252 O  O   . HOH J 4 .   ? 1.988   9.840   50.908  1.00 34.73 ? 217 HOH B O   1 
HETATM 4253 O  O   . HOH J 4 .   ? 2.424   13.050  49.776  1.00 36.78 ? 218 HOH B O   1 
HETATM 4254 O  O   . HOH J 4 .   ? 5.254   13.250  49.841  1.00 45.03 ? 219 HOH B O   1 
HETATM 4255 O  O   . HOH J 4 .   ? 7.558   12.383  46.009  1.00 42.41 ? 220 HOH B O   1 
HETATM 4256 O  O   . HOH J 4 .   ? 2.520   3.922   30.774  1.00 37.71 ? 221 HOH B O   1 
HETATM 4257 O  O   . HOH J 4 .   ? 3.530   -2.259  34.516  1.00 34.12 ? 222 HOH B O   1 
HETATM 4258 O  O   . HOH J 4 .   ? -15.400 1.650   56.813  1.00 40.95 ? 223 HOH B O   1 
HETATM 4259 O  O   . HOH J 4 .   ? -8.937  1.467   61.446  1.00 39.13 ? 224 HOH B O   1 
HETATM 4260 O  O   . HOH J 4 .   ? -6.196  -1.019  60.930  1.00 50.23 ? 225 HOH B O   1 
HETATM 4261 O  O   . HOH J 4 .   ? -7.360  -6.890  57.082  1.00 40.90 ? 226 HOH B O   1 
HETATM 4262 O  O   . HOH J 4 .   ? -4.906  -3.774  52.186  1.00 40.91 ? 227 HOH B O   1 
HETATM 4263 O  O   . HOH J 4 .   ? -10.927 15.877  23.807  1.00 50.54 ? 228 HOH B O   1 
HETATM 4264 O  O   . HOH J 4 .   ? -18.091 -9.194  36.141  1.00 48.30 ? 229 HOH B O   1 
HETATM 4265 O  O   . HOH J 4 .   ? -6.297  -11.129 36.963  1.00 31.55 ? 230 HOH B O   1 
HETATM 4266 O  O   . HOH J 4 .   ? -6.740  12.645  35.386  1.00 35.96 ? 231 HOH B O   1 
HETATM 4267 O  O   . HOH J 4 .   ? -12.022 14.298  42.342  1.00 36.74 ? 232 HOH B O   1 
HETATM 4268 O  O   . HOH J 4 .   ? -10.634 13.576  36.200  1.00 34.47 ? 233 HOH B O   1 
HETATM 4269 O  O   . HOH J 4 .   ? 13.229  14.210  37.173  1.00 39.65 ? 234 HOH B O   1 
HETATM 4270 O  O   . HOH J 4 .   ? -12.348 16.364  48.692  1.00 44.81 ? 235 HOH B O   1 
HETATM 4271 O  O   . HOH J 4 .   ? -10.897 -5.168  40.887  1.00 30.06 ? 236 HOH B O   1 
HETATM 4272 O  O   . HOH J 4 .   ? -12.360 -13.674 38.124  1.00 45.09 ? 237 HOH B O   1 
HETATM 4273 O  O   . HOH J 4 .   ? -7.823  -10.635 46.730  1.00 38.61 ? 238 HOH B O   1 
HETATM 4274 O  O   . HOH J 4 .   ? 12.604  -7.660  51.368  1.00 49.14 ? 239 HOH B O   1 
HETATM 4275 O  O   . HOH J 4 .   ? 7.169   -9.736  50.956  1.00 63.73 ? 240 HOH B O   1 
HETATM 4276 O  O   . HOH J 4 .   ? 4.477   -8.154  52.105  1.00 42.33 ? 241 HOH B O   1 
HETATM 4277 O  O   . HOH J 4 .   ? 9.015   -1.709  46.541  1.00 32.04 ? 242 HOH B O   1 
HETATM 4278 O  O   . HOH J 4 .   ? 7.660   1.630   40.605  1.00 34.16 ? 243 HOH B O   1 
HETATM 4279 O  O   . HOH J 4 .   ? -0.610  8.332   54.105  1.00 35.72 ? 244 HOH B O   1 
HETATM 4280 O  O   . HOH J 4 .   ? -2.645  10.376  52.127  1.00 33.10 ? 245 HOH B O   1 
HETATM 4281 O  O   . HOH J 4 .   ? -5.043  12.226  59.009  1.00 45.17 ? 246 HOH B O   1 
HETATM 4282 O  O   . HOH J 4 .   ? -11.192 13.038  59.885  1.00 41.96 ? 247 HOH B O   1 
HETATM 4283 O  O   . HOH J 4 .   ? -16.981 17.689  53.081  1.00 47.95 ? 248 HOH B O   1 
HETATM 4284 O  O   . HOH J 4 .   ? -10.478 17.241  46.066  1.00 49.58 ? 249 HOH B O   1 
HETATM 4285 O  O   . HOH J 4 .   ? 7.355   14.835  45.799  1.00 36.59 ? 250 HOH B O   1 
HETATM 4286 O  O   . HOH J 4 .   ? 3.136   18.530  41.581  1.00 48.90 ? 251 HOH B O   1 
HETATM 4287 O  O   . HOH J 4 .   ? 11.944  5.385   43.623  1.00 36.95 ? 252 HOH B O   1 
HETATM 4288 O  O   . HOH J 4 .   ? 6.476   2.811   29.606  1.00 44.04 ? 253 HOH B O   1 
HETATM 4289 O  O   . HOH J 4 .   ? 11.341  0.281   32.275  1.00 42.24 ? 254 HOH B O   1 
HETATM 4290 O  O   . HOH J 4 .   ? 5.052   -0.961  30.908  1.00 41.75 ? 255 HOH B O   1 
HETATM 4291 O  O   . HOH J 4 .   ? 1.765   1.118   30.784  1.00 44.83 ? 256 HOH B O   1 
HETATM 4292 O  O   . HOH J 4 .   ? -0.269  -13.166 63.349  1.00 37.56 ? 257 HOH B O   1 
HETATM 4293 O  O   . HOH J 4 .   ? -7.238  -5.497  53.240  1.00 40.84 ? 258 HOH B O   1 
HETATM 4294 O  O   . HOH J 4 .   ? -5.159  -10.690 47.178  1.00 38.61 ? 259 HOH B O   1 
HETATM 4295 O  O   . HOH J 4 .   ? -15.951 -4.068  46.942  1.00 45.41 ? 260 HOH B O   1 
HETATM 4296 O  O   . HOH J 4 .   ? -14.870 -0.757  40.088  1.00 36.34 ? 261 HOH B O   1 
HETATM 4297 O  O   . HOH J 4 .   ? -21.338 3.050   34.865  1.00 47.88 ? 262 HOH B O   1 
HETATM 4298 O  O   . HOH J 4 .   ? -13.628 2.517   35.618  1.00 42.34 ? 263 HOH B O   1 
HETATM 4299 O  O   . HOH J 4 .   ? 4.581   7.847   29.307  1.00 45.78 ? 264 HOH B O   1 
HETATM 4300 O  O   . HOH J 4 .   ? 0.853   3.682   29.067  1.00 41.86 ? 265 HOH B O   1 
HETATM 4301 O  O   . HOH J 4 .   ? -7.757  14.403  31.508  1.00 46.79 ? 266 HOH B O   1 
HETATM 4302 O  O   . HOH J 4 .   ? -16.448 -0.117  38.177  1.00 49.14 ? 267 HOH B O   1 
HETATM 4303 O  O   . HOH J 4 .   ? -23.847 -5.762  47.949  1.00 52.69 ? 268 HOH B O   1 
HETATM 4304 O  O   . HOH J 4 .   ? -22.154 8.393   47.825  1.00 49.30 ? 269 HOH B O   1 
HETATM 4305 O  O   . HOH J 4 .   ? 6.094   17.046  39.628  1.00 41.05 ? 270 HOH B O   1 
HETATM 4306 O  O   . HOH J 4 .   ? 8.485   16.827  38.519  1.00 39.93 ? 271 HOH B O   1 
HETATM 4307 O  O   . HOH J 4 .   ? -11.280 16.675  43.567  1.00 47.35 ? 272 HOH B O   1 
HETATM 4308 O  O   . HOH J 4 .   ? -21.693 9.974   53.228  0.50 30.22 ? 273 HOH B O   1 
HETATM 4309 O  O   . HOH J 4 .   ? -20.907 12.830  50.190  1.00 45.97 ? 274 HOH B O   1 
HETATM 4310 O  O   . HOH J 4 .   ? -18.104 15.275  48.098  1.00 45.32 ? 275 HOH B O   1 
HETATM 4311 O  O   . HOH J 4 .   ? -12.924 14.628  61.225  1.00 48.82 ? 276 HOH B O   1 
HETATM 4312 O  O   . HOH J 4 .   ? -11.592 17.246  58.858  1.00 49.58 ? 277 HOH B O   1 
HETATM 4313 O  O   . HOH J 4 .   ? -9.692  11.408  61.141  1.00 56.49 ? 278 HOH B O   1 
HETATM 4314 O  O   . HOH J 4 .   ? -0.047  -12.170 42.332  1.00 47.35 ? 279 HOH B O   1 
HETATM 4315 O  O   . HOH J 4 .   ? 3.157   -11.701 39.831  1.00 62.64 ? 280 HOH B O   1 
HETATM 4316 O  O   . HOH J 4 .   ? 1.247   -10.004 35.533  1.00 52.32 ? 281 HOH B O   1 
HETATM 4317 O  O   . HOH J 4 .   ? 1.013   -12.551 35.976  1.00 46.73 ? 282 HOH B O   1 
HETATM 4318 O  O   . HOH J 4 .   ? -0.624  -7.581  49.840  1.00 42.06 ? 283 HOH B O   1 
HETATM 4319 O  O   . HOH J 4 .   ? 8.483   -8.024  39.564  1.00 46.78 ? 284 HOH B O   1 
HETATM 4320 O  O   . HOH J 4 .   ? 13.706  -8.030  47.890  1.00 54.58 ? 285 HOH B O   1 
HETATM 4321 O  O   . HOH J 4 .   ? 5.571   9.586   51.295  1.00 38.45 ? 286 HOH B O   1 
HETATM 4322 O  O   . HOH J 4 .   ? 4.849   4.003   60.519  1.00 48.69 ? 287 HOH B O   1 
HETATM 4323 O  O   . HOH J 4 .   ? -1.324  6.548   60.545  1.00 44.03 ? 288 HOH B O   1 
HETATM 4324 O  O   . HOH J 4 .   ? -4.318  12.915  54.881  1.00 52.59 ? 289 HOH B O   1 
HETATM 4325 O  O   . HOH J 4 .   ? -10.100 19.729  47.382  1.00 52.44 ? 290 HOH B O   1 
HETATM 4326 O  O   . HOH J 4 .   ? -3.891  18.662  45.064  1.00 58.81 ? 291 HOH B O   1 
HETATM 4327 O  O   . HOH J 4 .   ? 1.350   17.975  45.110  1.00 52.38 ? 292 HOH B O   1 
HETATM 4328 O  O   . HOH J 4 .   ? 1.229   -0.740  32.518  1.00 30.55 ? 293 HOH B O   1 
HETATM 4329 O  O   . HOH J 4 .   ? 0.548   2.491   62.392  1.00 45.81 ? 294 HOH B O   1 
HETATM 4330 O  O   . HOH J 4 .   ? 6.673   -3.650  60.278  1.00 40.92 ? 295 HOH B O   1 
HETATM 4331 O  O   . HOH J 4 .   ? -1.591  -13.305 57.395  1.00 59.27 ? 296 HOH B O   1 
HETATM 4332 O  O   . HOH J 4 .   ? 9.099   6.523   29.548  0.50 30.83 ? 297 HOH B O   1 
HETATM 4333 O  O   . HOH J 4 .   ? 3.250   -2.625  32.126  1.00 44.77 ? 298 HOH B O   1 
HETATM 4334 O  O   . HOH J 4 .   ? -12.719 14.592  37.387  1.00 43.31 ? 299 HOH B O   1 
HETATM 4335 O  O   . HOH J 4 .   ? -11.694 13.327  23.189  1.00 47.76 ? 300 HOH B O   1 
HETATM 4336 O  O   . HOH J 4 .   ? -16.986 7.900   40.879  1.00 43.36 ? 301 HOH B O   1 
HETATM 4337 O  O   . HOH J 4 .   ? -4.031  19.280  42.003  1.00 54.22 ? 302 HOH B O   1 
HETATM 4338 O  O   . HOH J 4 .   ? -16.217 11.938  44.970  1.00 48.83 ? 303 HOH B O   1 
HETATM 4339 O  O   . HOH J 4 .   ? -14.867 -13.041 44.657  1.00 58.76 ? 304 HOH B O   1 
HETATM 4340 O  O   . HOH J 4 .   ? -8.406  -13.579 46.669  1.00 46.20 ? 305 HOH B O   1 
HETATM 4341 O  O   . HOH J 4 .   ? -3.348  22.175  42.999  1.00 54.79 ? 306 HOH B O   1 
HETATM 4342 O  O   . HOH J 4 .   ? 11.031  1.998   48.783  1.00 48.65 ? 307 HOH B O   1 
HETATM 4343 O  O   . HOH J 4 .   ? -10.342 14.909  58.312  1.00 55.06 ? 308 HOH B O   1 
HETATM 4344 O  O   . HOH J 4 .   ? -1.573  12.525  53.568  1.00 47.18 ? 309 HOH B O   1 
HETATM 4345 O  O   . HOH J 4 .   ? 9.771   15.935  45.049  1.00 54.85 ? 310 HOH B O   1 
HETATM 4346 O  O   . HOH J 4 .   ? 4.511   -12.175 61.982  1.00 47.23 ? 311 HOH B O   1 
HETATM 4347 O  O   . HOH K 4 .   ? 41.311  11.112  22.105  1.00 25.97 ? 154 HOH C O   1 
HETATM 4348 O  O   . HOH K 4 .   ? 15.098  4.143   31.886  1.00 29.21 ? 155 HOH C O   1 
HETATM 4349 O  O   . HOH K 4 .   ? 29.993  6.662   22.075  1.00 20.46 ? 156 HOH C O   1 
HETATM 4350 O  O   . HOH K 4 .   ? 46.686  7.927   31.428  1.00 39.33 ? 157 HOH C O   1 
HETATM 4351 O  O   . HOH K 4 .   ? 12.744  7.556   32.816  1.00 23.49 ? 158 HOH C O   1 
HETATM 4352 O  O   . HOH K 4 .   ? 17.028  9.016   37.479  1.00 27.23 ? 159 HOH C O   1 
HETATM 4353 O  O   . HOH K 4 .   ? 27.286  12.966  15.817  1.00 23.96 ? 160 HOH C O   1 
HETATM 4354 O  O   . HOH K 4 .   ? 17.191  2.648   38.774  1.00 29.43 ? 161 HOH C O   1 
HETATM 4355 O  O   . HOH K 4 .   ? 31.188  13.627  39.973  1.00 28.66 ? 162 HOH C O   1 
HETATM 4356 O  O   . HOH K 4 .   ? 25.832  13.062  40.312  1.00 50.79 ? 163 HOH C O   1 
HETATM 4357 O  O   . HOH K 4 .   ? 22.518  15.690  36.953  1.00 32.71 ? 164 HOH C O   1 
HETATM 4358 O  O   . HOH K 4 .   ? 36.620  9.798   38.983  1.00 28.44 ? 165 HOH C O   1 
HETATM 4359 O  O   . HOH K 4 .   ? 44.919  15.524  28.495  1.00 36.88 ? 166 HOH C O   1 
HETATM 4360 O  O   . HOH K 4 .   ? 9.239   2.036   38.509  1.00 34.79 ? 167 HOH C O   1 
HETATM 4361 O  O   . HOH K 4 .   ? 46.662  11.998  42.775  1.00 46.62 ? 168 HOH C O   1 
HETATM 4362 O  O   . HOH K 4 .   ? 42.281  19.124  40.796  1.00 35.33 ? 169 HOH C O   1 
HETATM 4363 O  O   . HOH K 4 .   ? 48.738  12.721  33.685  1.00 31.95 ? 170 HOH C O   1 
HETATM 4364 O  O   . HOH K 4 .   ? 15.139  1.447   33.635  1.00 30.08 ? 171 HOH C O   1 
HETATM 4365 O  O   . HOH K 4 .   ? 17.307  18.952  22.378  1.00 36.11 ? 172 HOH C O   1 
HETATM 4366 O  O   . HOH K 4 .   ? 22.582  15.984  39.748  1.00 45.26 ? 173 HOH C O   1 
HETATM 4367 O  O   . HOH K 4 .   ? 16.833  10.523  23.534  1.00 28.36 ? 174 HOH C O   1 
HETATM 4368 O  O   . HOH K 4 .   ? 45.852  8.110   25.610  1.00 34.58 ? 175 HOH C O   1 
HETATM 4369 O  O   . HOH K 4 .   ? 14.821  13.594  39.212  1.00 44.04 ? 176 HOH C O   1 
HETATM 4370 O  O   . HOH K 4 .   ? 15.055  9.964   39.938  1.00 30.89 ? 177 HOH C O   1 
HETATM 4371 O  O   . HOH K 4 .   ? 29.514  13.219  41.813  1.00 39.87 ? 178 HOH C O   1 
HETATM 4372 O  O   . HOH K 4 .   ? 19.850  -3.585  29.124  1.00 55.71 ? 179 HOH C O   1 
HETATM 4373 O  O   . HOH K 4 .   ? 27.311  0.008   29.166  1.00 32.22 ? 180 HOH C O   1 
HETATM 4374 O  O   . HOH K 4 .   ? 35.695  1.554   31.275  1.00 38.59 ? 181 HOH C O   1 
HETATM 4375 O  O   . HOH K 4 .   ? 11.148  0.493   35.392  1.00 28.35 ? 182 HOH C O   1 
HETATM 4376 O  O   . HOH K 4 .   ? 12.125  -1.844  36.075  1.00 46.97 ? 183 HOH C O   1 
HETATM 4377 O  O   . HOH K 4 .   ? 30.467  9.080   19.595  1.00 29.37 ? 184 HOH C O   1 
HETATM 4378 O  O   . HOH K 4 .   ? 20.384  1.670   38.514  1.00 28.98 ? 185 HOH C O   1 
HETATM 4379 O  O   . HOH K 4 .   ? 43.897  16.819  30.874  1.00 31.71 ? 186 HOH C O   1 
HETATM 4380 O  O   . HOH K 4 .   ? 21.272  12.964  41.815  1.00 38.31 ? 187 HOH C O   1 
HETATM 4381 O  O   . HOH K 4 .   ? 40.078  17.372  22.164  1.00 45.01 ? 188 HOH C O   1 
HETATM 4382 O  O   . HOH K 4 .   ? 41.643  3.950   31.648  1.00 46.39 ? 189 HOH C O   1 
HETATM 4383 O  O   . HOH K 4 .   ? 43.550  19.477  31.178  1.00 44.29 ? 190 HOH C O   1 
HETATM 4384 O  O   . HOH K 4 .   ? 49.290  14.856  35.290  1.00 33.14 ? 191 HOH C O   1 
HETATM 4385 O  O   . HOH K 4 .   ? 26.967  25.198  28.545  1.00 41.46 ? 192 HOH C O   1 
HETATM 4386 O  O   . HOH K 4 .   ? 39.085  8.286   40.139  1.00 37.31 ? 193 HOH C O   1 
HETATM 4387 O  O   . HOH K 4 .   ? 37.118  22.857  23.242  1.00 38.65 ? 194 HOH C O   1 
HETATM 4388 O  O   . HOH K 4 .   ? 19.551  -1.161  27.300  1.00 35.13 ? 195 HOH C O   1 
HETATM 4389 O  O   . HOH K 4 .   ? 33.575  8.398   20.322  1.00 36.40 ? 196 HOH C O   1 
HETATM 4390 O  O   . HOH K 4 .   ? 31.337  6.915   19.541  1.00 33.17 ? 197 HOH C O   1 
HETATM 4391 O  O   . HOH K 4 .   ? 38.316  5.963   23.073  1.00 43.66 ? 198 HOH C O   1 
HETATM 4392 O  O   . HOH K 4 .   ? 43.964  11.603  19.453  1.00 41.97 ? 199 HOH C O   1 
HETATM 4393 O  O   . HOH K 4 .   ? 42.034  14.835  24.266  1.00 31.51 ? 200 HOH C O   1 
HETATM 4394 O  O   . HOH K 4 .   ? 31.352  -1.037  27.897  1.00 35.96 ? 201 HOH C O   1 
HETATM 4395 O  O   . HOH K 4 .   ? 33.951  -0.363  30.464  1.00 41.92 ? 202 HOH C O   1 
HETATM 4396 O  O   . HOH K 4 .   ? 16.769  -1.126  41.357  1.00 47.12 ? 203 HOH C O   1 
HETATM 4397 O  O   . HOH K 4 .   ? 17.042  1.419   41.221  1.00 35.18 ? 204 HOH C O   1 
HETATM 4398 O  O   . HOH K 4 .   ? 19.661  1.664   41.274  1.00 42.70 ? 205 HOH C O   1 
HETATM 4399 O  O   . HOH K 4 .   ? 44.481  18.690  36.190  1.00 45.98 ? 206 HOH C O   1 
HETATM 4400 O  O   . HOH K 4 .   ? 51.831  14.412  41.386  1.00 44.71 ? 207 HOH C O   1 
HETATM 4401 O  O   . HOH K 4 .   ? 44.254  12.455  41.880  1.00 41.78 ? 208 HOH C O   1 
HETATM 4402 O  O   . HOH K 4 .   ? 23.509  19.706  16.027  1.00 30.86 ? 209 HOH C O   1 
HETATM 4403 O  O   . HOH K 4 .   ? 30.438  16.299  20.003  1.00 31.62 ? 210 HOH C O   1 
HETATM 4404 O  O   . HOH K 4 .   ? 33.421  10.587  15.636  1.00 46.28 ? 211 HOH C O   1 
HETATM 4405 O  O   . HOH K 4 .   ? 35.716  14.080  18.942  1.00 43.99 ? 212 HOH C O   1 
HETATM 4406 O  O   . HOH K 4 .   ? 28.995  21.437  12.362  1.00 42.66 ? 213 HOH C O   1 
HETATM 4407 O  O   . HOH K 4 .   ? 33.366  20.351  10.829  1.00 48.34 ? 214 HOH C O   1 
HETATM 4408 O  O   . HOH K 4 .   ? 30.105  24.667  21.686  1.00 34.99 ? 215 HOH C O   1 
HETATM 4409 O  O   . HOH K 4 .   ? 25.261  21.658  17.364  1.00 35.63 ? 216 HOH C O   1 
HETATM 4410 O  O   . HOH K 4 .   ? 31.546  22.790  31.793  1.00 34.55 ? 217 HOH C O   1 
HETATM 4411 O  O   . HOH K 4 .   ? 19.787  22.032  26.666  1.00 38.53 ? 218 HOH C O   1 
HETATM 4412 O  O   . HOH K 4 .   ? 22.039  17.980  38.105  1.00 38.71 ? 219 HOH C O   1 
HETATM 4413 O  O   . HOH K 4 .   ? 19.305  19.130  38.918  1.00 44.02 ? 220 HOH C O   1 
HETATM 4414 O  O   . HOH K 4 .   ? 50.459  7.079   32.409  1.00 56.27 ? 221 HOH C O   1 
HETATM 4415 O  O   . HOH K 4 .   ? 41.540  6.871   39.101  1.00 40.44 ? 222 HOH C O   1 
HETATM 4416 O  O   . HOH K 4 .   ? 21.087  8.928   42.962  1.00 42.05 ? 223 HOH C O   1 
HETATM 4417 O  O   . HOH K 4 .   ? 22.358  11.352  43.798  1.00 49.47 ? 224 HOH C O   1 
HETATM 4418 O  O   . HOH K 4 .   ? 15.620  8.189   41.625  1.00 41.63 ? 225 HOH C O   1 
HETATM 4419 O  O   . HOH K 4 .   ? 15.587  6.051   25.821  1.00 38.48 ? 226 HOH C O   1 
HETATM 4420 O  O   . HOH K 4 .   ? 15.715  13.196  25.483  1.00 38.97 ? 227 HOH C O   1 
HETATM 4421 O  O   . HOH K 4 .   ? 15.722  8.242   24.056  1.00 41.47 ? 228 HOH C O   1 
HETATM 4422 O  O   . HOH K 4 .   ? 35.415  23.579  29.116  1.00 36.57 ? 229 HOH C O   1 
HETATM 4423 O  O   . HOH K 4 .   ? 37.375  23.583  31.216  1.00 36.72 ? 230 HOH C O   1 
HETATM 4424 O  O   . HOH K 4 .   ? 35.332  22.797  33.302  1.00 42.34 ? 231 HOH C O   1 
HETATM 4425 O  O   . HOH K 4 .   ? 39.434  24.429  23.025  1.00 46.31 ? 232 HOH C O   1 
HETATM 4426 O  O   . HOH K 4 .   ? 42.602  21.502  25.088  1.00 57.07 ? 233 HOH C O   1 
HETATM 4427 O  O   . HOH K 4 .   ? 34.120  11.651  19.876  1.00 32.41 ? 234 HOH C O   1 
HETATM 4428 O  O   . HOH K 4 .   ? 30.444  9.993   16.956  0.50 21.94 ? 235 HOH C O   1 
HETATM 4429 O  O   . HOH K 4 .   ? 29.580  26.728  19.651  1.00 42.16 ? 236 HOH C O   1 
HETATM 4430 O  O   . HOH K 4 .   ? 12.069  3.341   41.500  1.00 35.11 ? 237 HOH C O   1 
HETATM 4431 O  O   . HOH K 4 .   ? 14.557  2.901   42.227  1.00 35.13 ? 238 HOH C O   1 
HETATM 4432 O  O   . HOH K 4 .   ? 23.300  -6.035  29.437  1.00 52.74 ? 239 HOH C O   1 
HETATM 4433 O  O   . HOH K 4 .   ? 17.206  -0.251  25.986  1.00 49.96 ? 240 HOH C O   1 
HETATM 4434 O  O   . HOH K 4 .   ? 42.333  8.821   21.403  1.00 53.30 ? 241 HOH C O   1 
HETATM 4435 O  O   . HOH K 4 .   ? 41.912  19.307  23.398  1.00 45.15 ? 242 HOH C O   1 
HETATM 4436 O  O   . HOH K 4 .   ? 43.494  16.486  25.800  1.00 43.61 ? 243 HOH C O   1 
HETATM 4437 O  O   . HOH K 4 .   ? 33.870  -1.853  28.217  1.00 42.83 ? 244 HOH C O   1 
HETATM 4438 O  O   . HOH K 4 .   ? 21.770  -6.430  40.382  1.00 58.58 ? 245 HOH C O   1 
HETATM 4439 O  O   . HOH K 4 .   ? 20.323  -6.803  43.236  1.00 56.55 ? 246 HOH C O   1 
HETATM 4440 O  O   . HOH K 4 .   ? 26.726  -0.525  41.648  1.00 53.49 ? 247 HOH C O   1 
HETATM 4441 O  O   . HOH K 4 .   ? 43.740  2.393   31.897  1.00 50.60 ? 248 HOH C O   1 
HETATM 4442 O  O   . HOH K 4 .   ? 47.437  8.110   27.693  1.00 40.92 ? 249 HOH C O   1 
HETATM 4443 O  O   . HOH K 4 .   ? 45.067  19.434  40.815  1.00 46.55 ? 250 HOH C O   1 
HETATM 4444 O  O   . HOH K 4 .   ? 34.713  9.990   18.038  1.00 47.04 ? 251 HOH C O   1 
HETATM 4445 O  O   . HOH K 4 .   ? 33.297  15.271  11.194  1.00 48.28 ? 252 HOH C O   1 
HETATM 4446 O  O   . HOH K 4 .   ? 26.584  16.949  40.143  1.00 57.13 ? 253 HOH C O   1 
HETATM 4447 O  O   . HOH K 4 .   ? 46.550  4.360   37.363  1.00 49.75 ? 254 HOH C O   1 
HETATM 4448 O  O   . HOH K 4 .   ? 51.055  13.224  37.085  1.00 45.78 ? 255 HOH C O   1 
HETATM 4449 O  O   . HOH K 4 .   ? 34.646  2.627   38.309  1.00 41.03 ? 256 HOH C O   1 
HETATM 4450 O  O   . HOH K 4 .   ? 27.775  9.870   42.913  1.00 34.68 ? 257 HOH C O   1 
HETATM 4451 O  O   . HOH K 4 .   ? 30.406  9.513   43.238  1.00 34.47 ? 258 HOH C O   1 
HETATM 4452 O  O   . HOH K 4 .   ? 10.201  5.408   30.748  0.50 26.35 ? 259 HOH C O   1 
HETATM 4453 O  O   . HOH K 4 .   ? 29.601  13.864  20.230  1.00 35.72 ? 260 HOH C O   1 
HETATM 4454 O  O   . HOH K 4 .   ? 31.371  11.639  19.290  1.00 34.96 ? 261 HOH C O   1 
HETATM 4455 O  O   . HOH K 4 .   ? 34.593  23.324  22.650  1.00 61.57 ? 262 HOH C O   1 
HETATM 4456 O  O   . HOH K 4 .   ? 32.601  25.179  22.704  1.00 43.46 ? 263 HOH C O   1 
HETATM 4457 O  O   . HOH K 4 .   ? 7.058   12.504  30.361  1.00 45.64 ? 264 HOH C O   1 
HETATM 4458 O  O   . HOH K 4 .   ? 5.820   12.948  28.096  1.00 47.92 ? 265 HOH C O   1 
HETATM 4459 O  O   . HOH K 4 .   ? 53.416  12.310  45.196  1.00 53.30 ? 266 HOH C O   1 
HETATM 4460 O  O   . HOH K 4 .   ? 13.583  9.338   43.722  1.00 49.39 ? 267 HOH C O   1 
HETATM 4461 O  O   . HOH K 4 .   ? 46.821  16.814  19.525  1.00 42.22 ? 268 HOH C O   1 
HETATM 4462 O  O   . HOH K 4 .   ? 25.169  19.020  12.268  1.00 42.06 ? 269 HOH C O   1 
HETATM 4463 O  O   . HOH K 4 .   ? 16.358  5.112   23.779  1.00 42.97 ? 270 HOH C O   1 
HETATM 4464 O  O   . HOH K 4 .   ? 37.320  3.735   15.531  1.00 53.59 ? 271 HOH C O   1 
HETATM 4465 O  O   . HOH K 4 .   ? 39.892  5.382   17.999  1.00 59.64 ? 272 HOH C O   1 
HETATM 4466 O  O   . HOH K 4 .   ? 20.540  -8.550  22.920  1.00 44.27 ? 273 HOH C O   1 
HETATM 4467 O  O   . HOH L 4 .   ? 23.920  3.202   -7.892  1.00 29.62 ? 154 HOH D O   1 
HETATM 4468 O  O   . HOH L 4 .   ? 28.011  10.188  15.423  1.00 20.89 ? 155 HOH D O   1 
HETATM 4469 O  O   . HOH L 4 .   ? 8.022   13.542  8.366   1.00 33.60 ? 156 HOH D O   1 
HETATM 4470 O  O   . HOH L 4 .   ? 32.834  5.341   15.007  1.00 34.71 ? 157 HOH D O   1 
HETATM 4471 O  O   . HOH L 4 .   ? 29.290  3.868   21.983  1.00 23.24 ? 158 HOH D O   1 
HETATM 4472 O  O   . HOH L 4 .   ? 17.801  -2.671  21.772  1.00 40.05 ? 159 HOH D O   1 
HETATM 4473 O  O   . HOH L 4 .   ? 26.160  -3.144  23.770  1.00 30.49 ? 160 HOH D O   1 
HETATM 4474 O  O   . HOH L 4 .   ? 29.791  8.243   17.030  0.50 17.70 ? 161 HOH D O   1 
HETATM 4475 O  O   . HOH L 4 .   ? 37.253  9.430   -1.632  1.00 36.01 ? 162 HOH D O   1 
HETATM 4476 O  O   . HOH L 4 .   ? 12.497  0.609   4.176   1.00 43.43 ? 163 HOH D O   1 
HETATM 4477 O  O   . HOH L 4 .   ? 22.113  -8.435  11.688  1.00 42.78 ? 164 HOH D O   1 
HETATM 4478 O  O   . HOH L 4 .   ? 32.057  7.810   -11.018 1.00 41.38 ? 165 HOH D O   1 
HETATM 4479 O  O   . HOH L 4 .   ? 28.505  -2.045  -7.205  1.00 38.91 ? 166 HOH D O   1 
HETATM 4480 O  O   . HOH L 4 .   ? 19.377  3.322   -0.567  1.00 31.45 ? 167 HOH D O   1 
HETATM 4481 O  O   . HOH L 4 .   ? 24.795  7.291   -2.495  1.00 33.59 ? 168 HOH D O   1 
HETATM 4482 O  O   . HOH L 4 .   ? 37.272  2.463   7.118   1.00 36.72 ? 169 HOH D O   1 
HETATM 4483 O  O   . HOH L 4 .   ? 10.330  3.502   3.166   1.00 41.46 ? 170 HOH D O   1 
HETATM 4484 O  O   . HOH L 4 .   ? 7.369   7.185   14.802  1.00 35.42 ? 171 HOH D O   1 
HETATM 4485 O  O   . HOH L 4 .   ? 28.891  -7.428  9.362   1.00 39.30 ? 172 HOH D O   1 
HETATM 4486 O  O   . HOH L 4 .   ? 35.221  0.844   0.597   1.00 38.71 ? 173 HOH D O   1 
HETATM 4487 O  O   . HOH L 4 .   ? 17.620  -5.461  16.743  1.00 41.49 ? 174 HOH D O   1 
HETATM 4488 O  O   . HOH L 4 .   ? 25.222  6.016   -8.732  1.00 47.53 ? 175 HOH D O   1 
HETATM 4489 O  O   . HOH L 4 .   ? 16.252  17.489  16.904  1.00 38.59 ? 176 HOH D O   1 
HETATM 4490 O  O   . HOH L 4 .   ? 33.578  -5.932  10.155  1.00 48.99 ? 177 HOH D O   1 
HETATM 4491 O  O   . HOH L 4 .   ? 26.379  -9.896  11.429  1.00 53.63 ? 178 HOH D O   1 
HETATM 4492 O  O   . HOH L 4 .   ? 13.736  2.529   19.323  1.00 40.51 ? 179 HOH D O   1 
HETATM 4493 O  O   . HOH L 4 .   ? 12.096  5.719   21.794  1.00 42.94 ? 180 HOH D O   1 
HETATM 4494 O  O   . HOH L 4 .   ? 12.285  -0.287  20.007  1.00 37.87 ? 181 HOH D O   1 
HETATM 4495 O  O   . HOH L 4 .   ? 14.022  9.448   20.159  1.00 34.98 ? 182 HOH D O   1 
HETATM 4496 O  O   . HOH L 4 .   ? 16.059  5.970   20.987  1.00 35.97 ? 183 HOH D O   1 
HETATM 4497 O  O   . HOH L 4 .   ? 25.697  17.878  9.861   1.00 39.81 ? 184 HOH D O   1 
HETATM 4498 O  O   . HOH L 4 .   ? 28.973  3.016   17.014  1.00 32.92 ? 185 HOH D O   1 
HETATM 4499 O  O   . HOH L 4 .   ? 29.820  0.556   16.733  1.00 30.30 ? 186 HOH D O   1 
HETATM 4500 O  O   . HOH L 4 .   ? 31.823  -8.043  9.798   1.00 58.47 ? 187 HOH D O   1 
HETATM 4501 O  O   . HOH L 4 .   ? 26.949  -4.973  21.462  1.00 36.53 ? 188 HOH D O   1 
HETATM 4502 O  O   . HOH L 4 .   ? 11.171  5.208   0.456   1.00 45.83 ? 189 HOH D O   1 
HETATM 4503 O  O   . HOH L 4 .   ? 8.661   7.196   10.578  1.00 35.87 ? 190 HOH D O   1 
HETATM 4504 O  O   . HOH L 4 .   ? 28.415  -7.657  15.586  1.00 34.25 ? 191 HOH D O   1 
HETATM 4505 O  O   . HOH L 4 .   ? 16.226  -6.232  5.809   1.00 44.24 ? 192 HOH D O   1 
HETATM 4506 O  O   . HOH L 4 .   ? 29.757  -6.224  3.259   1.00 43.13 ? 193 HOH D O   1 
HETATM 4507 O  O   . HOH L 4 .   ? 21.819  16.908  11.023  1.00 38.20 ? 194 HOH D O   1 
HETATM 4508 O  O   . HOH L 4 .   ? 10.921  14.594  6.761   1.00 35.78 ? 195 HOH D O   1 
HETATM 4509 O  O   . HOH L 4 .   ? 37.677  1.848   1.260   1.00 39.21 ? 196 HOH D O   1 
HETATM 4510 O  O   . HOH L 4 .   ? 37.417  1.990   -6.330  1.00 40.10 ? 197 HOH D O   1 
HETATM 4511 O  O   . HOH L 4 .   ? 29.304  -2.151  26.242  1.00 43.14 ? 198 HOH D O   1 
HETATM 4512 O  O   . HOH L 4 .   ? 35.629  0.127   13.626  1.00 43.28 ? 199 HOH D O   1 
HETATM 4513 O  O   . HOH L 4 .   ? 31.869  8.437   14.948  1.00 37.80 ? 200 HOH D O   1 
HETATM 4514 O  O   . HOH L 4 .   ? 37.638  5.812   9.143   1.00 29.22 ? 201 HOH D O   1 
HETATM 4515 O  O   . HOH L 4 .   ? 36.875  0.113   9.625   1.00 38.64 ? 202 HOH D O   1 
HETATM 4516 O  O   . HOH L 4 .   ? 6.396   7.203   8.028   1.00 42.03 ? 203 HOH D O   1 
HETATM 4517 O  O   . HOH L 4 .   ? 27.502  -4.824  -6.288  1.00 44.79 ? 204 HOH D O   1 
HETATM 4518 O  O   . HOH L 4 .   ? 30.725  5.337   16.962  1.00 35.40 ? 205 HOH D O   1 
HETATM 4519 O  O   . HOH L 4 .   ? 34.472  6.378   18.971  1.00 46.60 ? 206 HOH D O   1 
HETATM 4520 O  O   . HOH L 4 .   ? 34.961  2.807   15.025  1.00 50.83 ? 207 HOH D O   1 
HETATM 4521 O  O   . HOH L 4 .   ? 28.730  -9.663  17.336  1.00 40.23 ? 208 HOH D O   1 
HETATM 4522 O  O   . HOH L 4 .   ? 17.925  -7.646  8.461   1.00 43.02 ? 209 HOH D O   1 
HETATM 4523 O  O   . HOH L 4 .   ? 14.108  0.975   6.823   1.00 36.89 ? 210 HOH D O   1 
HETATM 4524 O  O   . HOH L 4 .   ? 29.587  4.554   -8.918  1.00 41.53 ? 211 HOH D O   1 
HETATM 4525 O  O   . HOH L 4 .   ? 33.671  12.965  -6.622  1.00 46.74 ? 212 HOH D O   1 
HETATM 4526 O  O   . HOH L 4 .   ? 17.243  7.453   -2.587  1.00 28.80 ? 213 HOH D O   1 
HETATM 4527 O  O   . HOH L 4 .   ? 14.862  7.227   -1.133  1.00 33.25 ? 214 HOH D O   1 
HETATM 4528 O  O   . HOH L 4 .   ? 8.370   4.564   16.124  1.00 37.92 ? 215 HOH D O   1 
HETATM 4529 O  O   . HOH L 4 .   ? 10.320  8.945   21.312  1.00 57.07 ? 216 HOH D O   1 
HETATM 4530 O  O   . HOH L 4 .   ? 34.412  14.385  13.752  1.00 48.22 ? 217 HOH D O   1 
HETATM 4531 O  O   . HOH L 4 .   ? 15.327  19.670  15.778  1.00 48.11 ? 218 HOH D O   1 
HETATM 4532 O  O   . HOH L 4 .   ? 33.275  12.360  9.072   1.00 41.08 ? 219 HOH D O   1 
HETATM 4533 O  O   . HOH L 4 .   ? 26.911  16.475  5.396   1.00 49.01 ? 220 HOH D O   1 
HETATM 4534 O  O   . HOH L 4 .   ? 9.926   12.442  15.372  1.00 47.67 ? 221 HOH D O   1 
HETATM 4535 O  O   . HOH L 4 .   ? 5.600   19.392  8.487   1.00 54.96 ? 222 HOH D O   1 
HETATM 4536 O  O   . HOH L 4 .   ? 6.345   14.518  6.410   1.00 46.70 ? 223 HOH D O   1 
HETATM 4537 O  O   . HOH L 4 .   ? 28.965  14.195  -1.996  1.00 45.46 ? 224 HOH D O   1 
HETATM 4538 O  O   . HOH L 4 .   ? 19.047  -7.586  20.708  1.00 54.70 ? 225 HOH D O   1 
HETATM 4539 O  O   . HOH L 4 .   ? 29.588  -4.676  23.518  1.00 46.44 ? 226 HOH D O   1 
HETATM 4540 O  O   . HOH L 4 .   ? 36.399  2.760   19.920  1.00 42.37 ? 227 HOH D O   1 
HETATM 4541 O  O   . HOH L 4 .   ? 35.997  -5.850  17.336  1.00 59.24 ? 228 HOH D O   1 
HETATM 4542 O  O   . HOH L 4 .   ? 24.489  -5.868  6.352   1.00 35.27 ? 229 HOH D O   1 
HETATM 4543 O  O   . HOH L 4 .   ? 25.761  -7.215  9.771   1.00 39.24 ? 230 HOH D O   1 
HETATM 4544 O  O   . HOH L 4 .   ? 2.940   -4.413  3.155   1.00 55.26 ? 231 HOH D O   1 
HETATM 4545 O  O   . HOH L 4 .   ? 9.935   -3.238  5.174   1.00 58.12 ? 232 HOH D O   1 
HETATM 4546 O  O   . HOH L 4 .   ? 17.637  -5.329  1.898   1.00 47.17 ? 233 HOH D O   1 
HETATM 4547 O  O   . HOH L 4 .   ? 28.444  17.248  -3.814  1.00 58.53 ? 234 HOH D O   1 
HETATM 4548 O  O   . HOH L 4 .   ? 16.452  11.626  -3.130  1.00 41.10 ? 235 HOH D O   1 
HETATM 4549 O  O   . HOH L 4 .   ? 22.740  24.015  14.003  1.00 50.22 ? 236 HOH D O   1 
HETATM 4550 O  O   . HOH L 4 .   ? 38.034  0.357   5.550   1.00 42.81 ? 237 HOH D O   1 
HETATM 4551 O  O   . HOH L 4 .   ? 7.258   20.953  7.027   1.00 53.73 ? 238 HOH D O   1 
HETATM 4552 O  O   . HOH L 4 .   ? 13.401  19.397  2.015   1.00 50.31 ? 239 HOH D O   1 
HETATM 4553 O  O   . HOH L 4 .   ? 26.829  16.593  2.171   1.00 47.22 ? 240 HOH D O   1 
HETATM 4554 O  O   . HOH L 4 .   ? 27.867  17.159  -1.154  1.00 55.26 ? 241 HOH D O   1 
HETATM 4555 O  O   . HOH L 4 .   ? 34.939  -1.797  0.256   1.00 52.08 ? 242 HOH D O   1 
HETATM 4556 O  O   . HOH L 4 .   ? 28.125  1.865   -9.147  1.00 45.34 ? 243 HOH D O   1 
HETATM 4557 O  O   . HOH L 4 .   ? 30.711  -4.481  26.592  1.00 55.39 ? 244 HOH D O   1 
HETATM 4558 O  O   . HOH L 4 .   ? 34.872  -7.871  18.873  1.00 50.20 ? 245 HOH D O   1 
HETATM 4559 O  O   . HOH L 4 .   ? 26.311  -6.914  19.910  1.00 44.17 ? 246 HOH D O   1 
HETATM 4560 O  O   . HOH L 4 .   ? 19.113  -3.178  -0.803  1.00 39.51 ? 247 HOH D O   1 
HETATM 4561 O  O   . HOH L 4 .   ? 20.545  -4.170  -2.763  1.00 49.91 ? 248 HOH D O   1 
HETATM 4562 O  O   . HOH L 4 .   ? 28.477  10.620  -5.298  1.00 49.47 ? 249 HOH D O   1 
HETATM 4563 O  O   . HOH L 4 .   ? 16.677  12.880  1.362   1.00 48.55 ? 250 HOH D O   1 
HETATM 4564 O  O   . HOH L 4 .   ? 15.277  11.440  21.188  1.00 37.06 ? 251 HOH D O   1 
HETATM 4565 O  O   . HOH L 4 .   ? 6.784   1.634   23.623  1.00 55.85 ? 252 HOH D O   1 
HETATM 4566 O  O   . HOH L 4 .   ? 21.668  21.028  13.380  1.00 47.76 ? 253 HOH D O   1 
HETATM 4567 O  O   . HOH L 4 .   ? 14.172  -4.602  -1.998  1.00 50.01 ? 254 HOH D 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   ?   ?   ?   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   ALA 6   6   6   ALA ALA 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 ALA 111 111 111 ALA ALA 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   ?   ?   ?   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   ALA 6   6   6   ALA ALA 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 ALA 111 111 111 ALA ALA 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   ALA 6   6   6   ALA ALA 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  ?   ?   ?   C . n 
C 1 70  LYS 70  70  ?   ?   ?   C . n 
C 1 71  HIS 71  71  ?   ?   ?   C . n 
C 1 72  GLY 72  72  ?   ?   ?   C . n 
C 1 73  GLY 73  73  ?   ?   ?   C . n 
C 1 74  PRO 74  74  ?   ?   ?   C . n 
C 1 75  LYS 75  75  ?   ?   ?   C . n 
C 1 76  ASP 76  76  ?   ?   ?   C . n 
C 1 77  GLU 77  77  ?   ?   ?   C . n 
C 1 78  GLU 78  78  ?   ?   ?   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 ALA 111 111 111 ALA ALA 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 ?   ?   ?   C . n 
C 1 126 LEU 126 126 ?   ?   ?   C . n 
C 1 127 GLY 127 127 ?   ?   ?   C . n 
C 1 128 LYS 128 128 ?   ?   ?   C . n 
C 1 129 GLY 129 129 ?   ?   ?   C . n 
C 1 130 GLY 130 130 ?   ?   ?   C . n 
C 1 131 ASN 131 131 ?   ?   ?   C . n 
C 1 132 GLU 132 132 ?   ?   ?   C . n 
C 1 133 GLU 133 133 ?   ?   ?   C . n 
C 1 134 SER 134 134 ?   ?   ?   C . n 
C 1 135 THR 135 135 ?   ?   ?   C . n 
C 1 136 LYS 136 136 ?   ?   ?   C . n 
C 1 137 THR 137 137 ?   ?   ?   C . n 
C 1 138 GLY 138 138 ?   ?   ?   C . n 
C 1 139 ASN 139 139 ?   ?   ?   C . n 
C 1 140 ALA 140 140 ?   ?   ?   C . n 
C 1 141 GLY 141 141 ?   ?   ?   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   ?   ?   ?   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   ALA 6   6   6   ALA ALA 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  ?   ?   ?   D . n 
D 1 68  SER 68  68  ?   ?   ?   D . n 
D 1 69  ARG 69  69  ?   ?   ?   D . n 
D 1 70  LYS 70  70  ?   ?   ?   D . n 
D 1 71  HIS 71  71  ?   ?   ?   D . n 
D 1 72  GLY 72  72  ?   ?   ?   D . n 
D 1 73  GLY 73  73  ?   ?   ?   D . n 
D 1 74  PRO 74  74  ?   ?   ?   D . n 
D 1 75  LYS 75  75  ?   ?   ?   D . n 
D 1 76  ASP 76  76  ?   ?   ?   D . n 
D 1 77  GLU 77  77  ?   ?   ?   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 ALA 111 111 111 ALA ALA 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 ?   ?   ?   D . n 
D 1 126 LEU 126 126 ?   ?   ?   D . n 
D 1 127 GLY 127 127 ?   ?   ?   D . n 
D 1 128 LYS 128 128 ?   ?   ?   D . n 
D 1 129 GLY 129 129 ?   ?   ?   D . n 
D 1 130 GLY 130 130 ?   ?   ?   D . n 
D 1 131 ASN 131 131 ?   ?   ?   D . n 
D 1 132 GLU 132 132 ?   ?   ?   D . n 
D 1 133 GLU 133 133 ?   ?   ?   D . n 
D 1 134 SER 134 134 ?   ?   ?   D . n 
D 1 135 THR 135 135 ?   ?   ?   D . n 
D 1 136 LYS 136 136 ?   ?   ?   D . n 
D 1 137 THR 137 137 ?   ?   ?   D . n 
D 1 138 GLY 138 138 ?   ?   ?   D . n 
D 1 139 ASN 139 139 ?   ?   ?   D . n 
D 1 140 ALA 140 140 ?   ?   ?   D . n 
D 1 141 GLY 141 141 ?   ?   ?   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 
# 
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 
E 2 CU1 1   154 154 CU1 CU1 A . 
F 3 ZN  1   155 155 ZN  ZN  A . 
G 2 CU1 1   154 154 CU1 CU1 B . 
H 3 ZN  1   155 155 ZN  ZN  B . 
I 4 HOH 1   156 10  HOH HOH A . 
I 4 HOH 2   157 11  HOH HOH A . 
I 4 HOH 3   158 14  HOH HOH A . 
I 4 HOH 4   159 15  HOH HOH A . 
I 4 HOH 5   160 18  HOH HOH A . 
I 4 HOH 6   161 22  HOH HOH A . 
I 4 HOH 7   162 27  HOH HOH A . 
I 4 HOH 8   163 30  HOH HOH A . 
I 4 HOH 9   164 31  HOH HOH A . 
I 4 HOH 10  165 40  HOH HOH A . 
I 4 HOH 11  166 42  HOH HOH A . 
I 4 HOH 12  167 46  HOH HOH A . 
I 4 HOH 13  168 50  HOH HOH A . 
I 4 HOH 14  169 51  HOH HOH A . 
I 4 HOH 15  170 61  HOH HOH A . 
I 4 HOH 16  171 63  HOH HOH A . 
I 4 HOH 17  172 64  HOH HOH A . 
I 4 HOH 18  173 65  HOH HOH A . 
I 4 HOH 19  174 69  HOH HOH A . 
I 4 HOH 20  175 73  HOH HOH A . 
I 4 HOH 21  176 74  HOH HOH A . 
I 4 HOH 22  177 75  HOH HOH A . 
I 4 HOH 23  178 77  HOH HOH A . 
I 4 HOH 24  179 78  HOH HOH A . 
I 4 HOH 25  180 81  HOH HOH A . 
I 4 HOH 26  181 87  HOH HOH A . 
I 4 HOH 27  182 100 HOH HOH A . 
I 4 HOH 28  183 106 HOH HOH A . 
I 4 HOH 29  184 108 HOH HOH A . 
I 4 HOH 30  185 111 HOH HOH A . 
I 4 HOH 31  186 113 HOH HOH A . 
I 4 HOH 32  187 114 HOH HOH A . 
I 4 HOH 33  188 131 HOH HOH A . 
I 4 HOH 34  189 133 HOH HOH A . 
I 4 HOH 35  190 134 HOH HOH A . 
I 4 HOH 36  191 135 HOH HOH A . 
I 4 HOH 37  192 136 HOH HOH A . 
I 4 HOH 38  193 137 HOH HOH A . 
I 4 HOH 39  194 138 HOH HOH A . 
I 4 HOH 40  195 139 HOH HOH A . 
I 4 HOH 41  196 140 HOH HOH A . 
I 4 HOH 42  197 141 HOH HOH A . 
I 4 HOH 43  198 142 HOH HOH A . 
I 4 HOH 44  199 143 HOH HOH A . 
I 4 HOH 45  200 144 HOH HOH A . 
I 4 HOH 46  201 145 HOH HOH A . 
I 4 HOH 47  202 146 HOH HOH A . 
I 4 HOH 48  203 147 HOH HOH A . 
I 4 HOH 49  204 148 HOH HOH A . 
I 4 HOH 50  205 149 HOH HOH A . 
I 4 HOH 51  206 150 HOH HOH A . 
I 4 HOH 52  207 151 HOH HOH A . 
I 4 HOH 53  208 152 HOH HOH A . 
I 4 HOH 54  209 153 HOH HOH A . 
I 4 HOH 55  210 154 HOH HOH A . 
I 4 HOH 56  211 156 HOH HOH A . 
I 4 HOH 57  212 157 HOH HOH A . 
I 4 HOH 58  213 160 HOH HOH A . 
I 4 HOH 59  214 183 HOH HOH A . 
I 4 HOH 60  215 184 HOH HOH A . 
I 4 HOH 61  216 185 HOH HOH A . 
I 4 HOH 62  217 186 HOH HOH A . 
I 4 HOH 63  218 188 HOH HOH A . 
I 4 HOH 64  219 189 HOH HOH A . 
I 4 HOH 65  220 190 HOH HOH A . 
I 4 HOH 66  221 191 HOH HOH A . 
I 4 HOH 67  222 192 HOH HOH A . 
I 4 HOH 68  223 193 HOH HOH A . 
I 4 HOH 69  224 194 HOH HOH A . 
I 4 HOH 70  225 195 HOH HOH A . 
I 4 HOH 71  226 231 HOH HOH A . 
I 4 HOH 72  227 232 HOH HOH A . 
I 4 HOH 73  228 233 HOH HOH A . 
I 4 HOH 74  229 234 HOH HOH A . 
I 4 HOH 75  230 235 HOH HOH A . 
I 4 HOH 76  231 236 HOH HOH A . 
I 4 HOH 77  232 237 HOH HOH A . 
I 4 HOH 78  233 238 HOH HOH A . 
I 4 HOH 79  234 239 HOH HOH A . 
I 4 HOH 80  235 240 HOH HOH A . 
I 4 HOH 81  236 241 HOH HOH A . 
I 4 HOH 82  237 242 HOH HOH A . 
I 4 HOH 83  238 244 HOH HOH A . 
I 4 HOH 84  239 245 HOH HOH A . 
I 4 HOH 85  240 246 HOH HOH A . 
I 4 HOH 86  241 247 HOH HOH A . 
I 4 HOH 87  242 248 HOH HOH A . 
I 4 HOH 88  243 249 HOH HOH A . 
I 4 HOH 89  244 250 HOH HOH A . 
I 4 HOH 90  245 251 HOH HOH A . 
I 4 HOH 91  246 252 HOH HOH A . 
I 4 HOH 92  247 253 HOH HOH A . 
I 4 HOH 93  248 254 HOH HOH A . 
I 4 HOH 94  249 255 HOH HOH A . 
I 4 HOH 95  250 256 HOH HOH A . 
I 4 HOH 96  251 257 HOH HOH A . 
I 4 HOH 97  252 258 HOH HOH A . 
I 4 HOH 98  253 259 HOH HOH A . 
I 4 HOH 99  254 260 HOH HOH A . 
I 4 HOH 100 255 261 HOH HOH A . 
I 4 HOH 101 256 262 HOH HOH A . 
I 4 HOH 102 257 263 HOH HOH A . 
I 4 HOH 103 258 264 HOH HOH A . 
I 4 HOH 104 259 265 HOH HOH A . 
I 4 HOH 105 260 266 HOH HOH A . 
I 4 HOH 106 261 267 HOH HOH A . 
I 4 HOH 107 262 268 HOH HOH A . 
I 4 HOH 108 263 269 HOH HOH A . 
I 4 HOH 109 264 361 HOH HOH A . 
I 4 HOH 110 265 363 HOH HOH A . 
I 4 HOH 111 266 364 HOH HOH A . 
I 4 HOH 112 267 365 HOH HOH A . 
I 4 HOH 113 268 366 HOH HOH A . 
I 4 HOH 114 269 367 HOH HOH A . 
I 4 HOH 115 270 368 HOH HOH A . 
I 4 HOH 116 271 369 HOH HOH A . 
I 4 HOH 117 272 370 HOH HOH A . 
I 4 HOH 118 273 371 HOH HOH A . 
I 4 HOH 119 274 372 HOH HOH A . 
I 4 HOH 120 275 373 HOH HOH A . 
I 4 HOH 121 276 374 HOH HOH A . 
I 4 HOH 122 277 375 HOH HOH A . 
I 4 HOH 123 278 376 HOH HOH A . 
I 4 HOH 124 279 377 HOH HOH A . 
I 4 HOH 125 280 378 HOH HOH A . 
I 4 HOH 126 281 379 HOH HOH A . 
I 4 HOH 127 282 380 HOH HOH A . 
I 4 HOH 128 283 381 HOH HOH A . 
I 4 HOH 129 284 382 HOH HOH A . 
I 4 HOH 130 285 383 HOH HOH A . 
I 4 HOH 131 286 384 HOH HOH A . 
I 4 HOH 132 287 385 HOH HOH A . 
I 4 HOH 133 288 386 HOH HOH A . 
I 4 HOH 134 289 387 HOH HOH A . 
I 4 HOH 135 290 388 HOH HOH A . 
I 4 HOH 136 291 389 HOH HOH A . 
I 4 HOH 137 292 390 HOH HOH A . 
I 4 HOH 138 293 391 HOH HOH A . 
I 4 HOH 139 294 392 HOH HOH A . 
I 4 HOH 140 295 393 HOH HOH A . 
I 4 HOH 141 296 394 HOH HOH A . 
I 4 HOH 142 297 395 HOH HOH A . 
I 4 HOH 143 298 396 HOH HOH A . 
I 4 HOH 144 299 397 HOH HOH A . 
I 4 HOH 145 300 398 HOH HOH A . 
I 4 HOH 146 301 399 HOH HOH A . 
I 4 HOH 147 302 482 HOH HOH A . 
I 4 HOH 148 303 484 HOH HOH A . 
I 4 HOH 149 304 485 HOH HOH A . 
I 4 HOH 150 305 486 HOH HOH A . 
I 4 HOH 151 306 487 HOH HOH A . 
I 4 HOH 152 307 488 HOH HOH A . 
I 4 HOH 153 308 489 HOH HOH A . 
I 4 HOH 154 309 490 HOH HOH A . 
I 4 HOH 155 310 491 HOH HOH A . 
I 4 HOH 156 311 492 HOH HOH A . 
I 4 HOH 157 312 493 HOH HOH A . 
I 4 HOH 158 313 494 HOH HOH A . 
I 4 HOH 159 314 497 HOH HOH A . 
I 4 HOH 160 315 498 HOH HOH A . 
J 4 HOH 1   156 1   HOH HOH B . 
J 4 HOH 2   157 2   HOH HOH B . 
J 4 HOH 3   158 3   HOH HOH B . 
J 4 HOH 4   159 5   HOH HOH B . 
J 4 HOH 5   160 8   HOH HOH B . 
J 4 HOH 6   161 12  HOH HOH B . 
J 4 HOH 7   162 16  HOH HOH B . 
J 4 HOH 8   163 24  HOH HOH B . 
J 4 HOH 9   164 26  HOH HOH B . 
J 4 HOH 10  165 34  HOH HOH B . 
J 4 HOH 11  166 36  HOH HOH B . 
J 4 HOH 12  167 39  HOH HOH B . 
J 4 HOH 13  168 43  HOH HOH B . 
J 4 HOH 14  169 44  HOH HOH B . 
J 4 HOH 15  170 48  HOH HOH B . 
J 4 HOH 16  171 49  HOH HOH B . 
J 4 HOH 17  172 57  HOH HOH B . 
J 4 HOH 18  173 58  HOH HOH B . 
J 4 HOH 19  174 59  HOH HOH B . 
J 4 HOH 20  175 60  HOH HOH B . 
J 4 HOH 21  176 66  HOH HOH B . 
J 4 HOH 22  177 67  HOH HOH B . 
J 4 HOH 23  178 71  HOH HOH B . 
J 4 HOH 24  179 72  HOH HOH B . 
J 4 HOH 25  180 79  HOH HOH B . 
J 4 HOH 26  181 85  HOH HOH B . 
J 4 HOH 27  182 89  HOH HOH B . 
J 4 HOH 28  183 94  HOH HOH B . 
J 4 HOH 29  184 98  HOH HOH B . 
J 4 HOH 30  185 99  HOH HOH B . 
J 4 HOH 31  186 101 HOH HOH B . 
J 4 HOH 32  187 102 HOH HOH B . 
J 4 HOH 33  188 105 HOH HOH B . 
J 4 HOH 34  189 112 HOH HOH B . 
J 4 HOH 35  190 117 HOH HOH B . 
J 4 HOH 36  191 122 HOH HOH B . 
J 4 HOH 37  192 123 HOH HOH B . 
J 4 HOH 38  193 124 HOH HOH B . 
J 4 HOH 39  194 125 HOH HOH B . 
J 4 HOH 40  195 126 HOH HOH B . 
J 4 HOH 41  196 132 HOH HOH B . 
J 4 HOH 42  197 161 HOH HOH B . 
J 4 HOH 43  198 162 HOH HOH B . 
J 4 HOH 44  199 163 HOH HOH B . 
J 4 HOH 45  200 164 HOH HOH B . 
J 4 HOH 46  201 165 HOH HOH B . 
J 4 HOH 47  202 166 HOH HOH B . 
J 4 HOH 48  203 167 HOH HOH B . 
J 4 HOH 49  204 168 HOH HOH B . 
J 4 HOH 50  205 169 HOH HOH B . 
J 4 HOH 51  206 170 HOH HOH B . 
J 4 HOH 52  207 171 HOH HOH B . 
J 4 HOH 53  208 172 HOH HOH B . 
J 4 HOH 54  209 196 HOH HOH B . 
J 4 HOH 55  210 197 HOH HOH B . 
J 4 HOH 56  211 198 HOH HOH B . 
J 4 HOH 57  212 199 HOH HOH B . 
J 4 HOH 58  213 200 HOH HOH B . 
J 4 HOH 59  214 201 HOH HOH B . 
J 4 HOH 60  215 202 HOH HOH B . 
J 4 HOH 61  216 203 HOH HOH B . 
J 4 HOH 62  217 204 HOH HOH B . 
J 4 HOH 63  218 205 HOH HOH B . 
J 4 HOH 64  219 206 HOH HOH B . 
J 4 HOH 65  220 208 HOH HOH B . 
J 4 HOH 66  221 209 HOH HOH B . 
J 4 HOH 67  222 210 HOH HOH B . 
J 4 HOH 68  223 211 HOH HOH B . 
J 4 HOH 69  224 212 HOH HOH B . 
J 4 HOH 70  225 213 HOH HOH B . 
J 4 HOH 71  226 214 HOH HOH B . 
J 4 HOH 72  227 215 HOH HOH B . 
J 4 HOH 73  228 216 HOH HOH B . 
J 4 HOH 74  229 243 HOH HOH B . 
J 4 HOH 75  230 270 HOH HOH B . 
J 4 HOH 76  231 271 HOH HOH B . 
J 4 HOH 77  232 272 HOH HOH B . 
J 4 HOH 78  233 273 HOH HOH B . 
J 4 HOH 79  234 274 HOH HOH B . 
J 4 HOH 80  235 275 HOH HOH B . 
J 4 HOH 81  236 276 HOH HOH B . 
J 4 HOH 82  237 277 HOH HOH B . 
J 4 HOH 83  238 278 HOH HOH B . 
J 4 HOH 84  239 279 HOH HOH B . 
J 4 HOH 85  240 280 HOH HOH B . 
J 4 HOH 86  241 281 HOH HOH B . 
J 4 HOH 87  242 282 HOH HOH B . 
J 4 HOH 88  243 283 HOH HOH B . 
J 4 HOH 89  244 284 HOH HOH B . 
J 4 HOH 90  245 285 HOH HOH B . 
J 4 HOH 91  246 286 HOH HOH B . 
J 4 HOH 92  247 287 HOH HOH B . 
J 4 HOH 93  248 288 HOH HOH B . 
J 4 HOH 94  249 289 HOH HOH B . 
J 4 HOH 95  250 290 HOH HOH B . 
J 4 HOH 96  251 291 HOH HOH B . 
J 4 HOH 97  252 292 HOH HOH B . 
J 4 HOH 98  253 293 HOH HOH B . 
J 4 HOH 99  254 294 HOH HOH B . 
J 4 HOH 100 255 295 HOH HOH B . 
J 4 HOH 101 256 296 HOH HOH B . 
J 4 HOH 102 257 297 HOH HOH B . 
J 4 HOH 103 258 298 HOH HOH B . 
J 4 HOH 104 259 299 HOH HOH B . 
J 4 HOH 105 260 300 HOH HOH B . 
J 4 HOH 106 261 301 HOH HOH B . 
J 4 HOH 107 262 362 HOH HOH B . 
J 4 HOH 108 263 400 HOH HOH B . 
J 4 HOH 109 264 401 HOH HOH B . 
J 4 HOH 110 265 402 HOH HOH B . 
J 4 HOH 111 266 403 HOH HOH B . 
J 4 HOH 112 267 404 HOH HOH B . 
J 4 HOH 113 268 405 HOH HOH B . 
J 4 HOH 114 269 406 HOH HOH B . 
J 4 HOH 115 270 407 HOH HOH B . 
J 4 HOH 116 271 408 HOH HOH B . 
J 4 HOH 117 272 409 HOH HOH B . 
J 4 HOH 118 273 410 HOH HOH B . 
J 4 HOH 119 274 411 HOH HOH B . 
J 4 HOH 120 275 412 HOH HOH B . 
J 4 HOH 121 276 413 HOH HOH B . 
J 4 HOH 122 277 414 HOH HOH B . 
J 4 HOH 123 278 415 HOH HOH B . 
J 4 HOH 124 279 416 HOH HOH B . 
J 4 HOH 125 280 417 HOH HOH B . 
J 4 HOH 126 281 418 HOH HOH B . 
J 4 HOH 127 282 419 HOH HOH B . 
J 4 HOH 128 283 420 HOH HOH B . 
J 4 HOH 129 284 421 HOH HOH B . 
J 4 HOH 130 285 422 HOH HOH B . 
J 4 HOH 131 286 423 HOH HOH B . 
J 4 HOH 132 287 424 HOH HOH B . 
J 4 HOH 133 288 425 HOH HOH B . 
J 4 HOH 134 289 426 HOH HOH B . 
J 4 HOH 135 290 427 HOH HOH B . 
J 4 HOH 136 291 428 HOH HOH B . 
J 4 HOH 137 292 429 HOH HOH B . 
J 4 HOH 138 293 432 HOH HOH B . 
J 4 HOH 139 294 433 HOH HOH B . 
J 4 HOH 140 295 434 HOH HOH B . 
J 4 HOH 141 296 435 HOH HOH B . 
J 4 HOH 142 297 458 HOH HOH B . 
J 4 HOH 143 298 483 HOH HOH B . 
J 4 HOH 144 299 495 HOH HOH B . 
J 4 HOH 145 300 496 HOH HOH B . 
J 4 HOH 146 301 501 HOH HOH B . 
J 4 HOH 147 302 502 HOH HOH B . 
J 4 HOH 148 303 503 HOH HOH B . 
J 4 HOH 149 304 504 HOH HOH B . 
J 4 HOH 150 305 505 HOH HOH B . 
J 4 HOH 151 306 507 HOH HOH B . 
J 4 HOH 152 307 508 HOH HOH B . 
J 4 HOH 153 308 509 HOH HOH B . 
J 4 HOH 154 309 510 HOH HOH B . 
J 4 HOH 155 310 511 HOH HOH B . 
J 4 HOH 156 311 536 HOH HOH B . 
K 4 HOH 1   154 6   HOH HOH C . 
K 4 HOH 2   155 7   HOH HOH C . 
K 4 HOH 3   156 9   HOH HOH C . 
K 4 HOH 4   157 21  HOH HOH C . 
K 4 HOH 5   158 23  HOH HOH C . 
K 4 HOH 6   159 28  HOH HOH C . 
K 4 HOH 7   160 29  HOH HOH C . 
K 4 HOH 8   161 33  HOH HOH C . 
K 4 HOH 9   162 35  HOH HOH C . 
K 4 HOH 10  163 54  HOH HOH C . 
K 4 HOH 11  164 62  HOH HOH C . 
K 4 HOH 12  165 68  HOH HOH C . 
K 4 HOH 13  166 76  HOH HOH C . 
K 4 HOH 14  167 82  HOH HOH C . 
K 4 HOH 15  168 83  HOH HOH C . 
K 4 HOH 16  169 84  HOH HOH C . 
K 4 HOH 17  170 93  HOH HOH C . 
K 4 HOH 18  171 95  HOH HOH C . 
K 4 HOH 19  172 96  HOH HOH C . 
K 4 HOH 20  173 103 HOH HOH C . 
K 4 HOH 21  174 104 HOH HOH C . 
K 4 HOH 22  175 110 HOH HOH C . 
K 4 HOH 23  176 115 HOH HOH C . 
K 4 HOH 24  177 116 HOH HOH C . 
K 4 HOH 25  178 118 HOH HOH C . 
K 4 HOH 26  179 119 HOH HOH C . 
K 4 HOH 27  180 127 HOH HOH C . 
K 4 HOH 28  181 128 HOH HOH C . 
K 4 HOH 29  182 129 HOH HOH C . 
K 4 HOH 30  183 130 HOH HOH C . 
K 4 HOH 31  184 158 HOH HOH C . 
K 4 HOH 32  185 173 HOH HOH C . 
K 4 HOH 33  186 174 HOH HOH C . 
K 4 HOH 34  187 175 HOH HOH C . 
K 4 HOH 35  188 217 HOH HOH C . 
K 4 HOH 36  189 218 HOH HOH C . 
K 4 HOH 37  190 219 HOH HOH C . 
K 4 HOH 38  191 220 HOH HOH C . 
K 4 HOH 39  192 222 HOH HOH C . 
K 4 HOH 40  193 223 HOH HOH C . 
K 4 HOH 41  194 224 HOH HOH C . 
K 4 HOH 42  195 302 HOH HOH C . 
K 4 HOH 43  196 303 HOH HOH C . 
K 4 HOH 44  197 304 HOH HOH C . 
K 4 HOH 45  198 305 HOH HOH C . 
K 4 HOH 46  199 306 HOH HOH C . 
K 4 HOH 47  200 307 HOH HOH C . 
K 4 HOH 48  201 308 HOH HOH C . 
K 4 HOH 49  202 309 HOH HOH C . 
K 4 HOH 50  203 310 HOH HOH C . 
K 4 HOH 51  204 311 HOH HOH C . 
K 4 HOH 52  205 312 HOH HOH C . 
K 4 HOH 53  206 313 HOH HOH C . 
K 4 HOH 54  207 314 HOH HOH C . 
K 4 HOH 55  208 315 HOH HOH C . 
K 4 HOH 56  209 316 HOH HOH C . 
K 4 HOH 57  210 317 HOH HOH C . 
K 4 HOH 58  211 318 HOH HOH C . 
K 4 HOH 59  212 319 HOH HOH C . 
K 4 HOH 60  213 320 HOH HOH C . 
K 4 HOH 61  214 321 HOH HOH C . 
K 4 HOH 62  215 322 HOH HOH C . 
K 4 HOH 63  216 323 HOH HOH C . 
K 4 HOH 64  217 324 HOH HOH C . 
K 4 HOH 65  218 325 HOH HOH C . 
K 4 HOH 66  219 326 HOH HOH C . 
K 4 HOH 67  220 327 HOH HOH C . 
K 4 HOH 68  221 328 HOH HOH C . 
K 4 HOH 69  222 329 HOH HOH C . 
K 4 HOH 70  223 330 HOH HOH C . 
K 4 HOH 71  224 331 HOH HOH C . 
K 4 HOH 72  225 332 HOH HOH C . 
K 4 HOH 73  226 333 HOH HOH C . 
K 4 HOH 74  227 334 HOH HOH C . 
K 4 HOH 75  228 335 HOH HOH C . 
K 4 HOH 76  229 336 HOH HOH C . 
K 4 HOH 77  230 337 HOH HOH C . 
K 4 HOH 78  231 338 HOH HOH C . 
K 4 HOH 79  232 339 HOH HOH C . 
K 4 HOH 80  233 340 HOH HOH C . 
K 4 HOH 81  234 341 HOH HOH C . 
K 4 HOH 82  235 343 HOH HOH C . 
K 4 HOH 83  236 352 HOH HOH C . 
K 4 HOH 84  237 430 HOH HOH C . 
K 4 HOH 85  238 431 HOH HOH C . 
K 4 HOH 86  239 436 HOH HOH C . 
K 4 HOH 87  240 437 HOH HOH C . 
K 4 HOH 88  241 438 HOH HOH C . 
K 4 HOH 89  242 439 HOH HOH C . 
K 4 HOH 90  243 440 HOH HOH C . 
K 4 HOH 91  244 441 HOH HOH C . 
K 4 HOH 92  245 442 HOH HOH C . 
K 4 HOH 93  246 443 HOH HOH C . 
K 4 HOH 94  247 444 HOH HOH C . 
K 4 HOH 95  248 445 HOH HOH C . 
K 4 HOH 96  249 446 HOH HOH C . 
K 4 HOH 97  250 447 HOH HOH C . 
K 4 HOH 98  251 448 HOH HOH C . 
K 4 HOH 99  252 450 HOH HOH C . 
K 4 HOH 100 253 451 HOH HOH C . 
K 4 HOH 101 254 452 HOH HOH C . 
K 4 HOH 102 255 453 HOH HOH C . 
K 4 HOH 103 256 454 HOH HOH C . 
K 4 HOH 104 257 455 HOH HOH C . 
K 4 HOH 105 258 456 HOH HOH C . 
K 4 HOH 106 259 457 HOH HOH C . 
K 4 HOH 107 260 459 HOH HOH C . 
K 4 HOH 108 261 460 HOH HOH C . 
K 4 HOH 109 262 461 HOH HOH C . 
K 4 HOH 110 263 462 HOH HOH C . 
K 4 HOH 111 264 499 HOH HOH C . 
K 4 HOH 112 265 500 HOH HOH C . 
K 4 HOH 113 266 506 HOH HOH C . 
K 4 HOH 114 267 512 HOH HOH C . 
K 4 HOH 115 268 513 HOH HOH C . 
K 4 HOH 116 269 514 HOH HOH C . 
K 4 HOH 117 270 515 HOH HOH C . 
K 4 HOH 118 271 516 HOH HOH C . 
K 4 HOH 119 272 534 HOH HOH C . 
K 4 HOH 120 273 535 HOH HOH C . 
L 4 HOH 1   154 4   HOH HOH D . 
L 4 HOH 2   155 13  HOH HOH D . 
L 4 HOH 3   156 17  HOH HOH D . 
L 4 HOH 4   157 19  HOH HOH D . 
L 4 HOH 5   158 20  HOH HOH D . 
L 4 HOH 6   159 25  HOH HOH D . 
L 4 HOH 7   160 32  HOH HOH D . 
L 4 HOH 8   161 37  HOH HOH D . 
L 4 HOH 9   162 38  HOH HOH D . 
L 4 HOH 10  163 41  HOH HOH D . 
L 4 HOH 11  164 45  HOH HOH D . 
L 4 HOH 12  165 47  HOH HOH D . 
L 4 HOH 13  166 52  HOH HOH D . 
L 4 HOH 14  167 53  HOH HOH D . 
L 4 HOH 15  168 55  HOH HOH D . 
L 4 HOH 16  169 56  HOH HOH D . 
L 4 HOH 17  170 70  HOH HOH D . 
L 4 HOH 18  171 80  HOH HOH D . 
L 4 HOH 19  172 86  HOH HOH D . 
L 4 HOH 20  173 88  HOH HOH D . 
L 4 HOH 21  174 90  HOH HOH D . 
L 4 HOH 22  175 91  HOH HOH D . 
L 4 HOH 23  176 92  HOH HOH D . 
L 4 HOH 24  177 97  HOH HOH D . 
L 4 HOH 25  178 107 HOH HOH D . 
L 4 HOH 26  179 109 HOH HOH D . 
L 4 HOH 27  180 120 HOH HOH D . 
L 4 HOH 28  181 121 HOH HOH D . 
L 4 HOH 29  182 155 HOH HOH D . 
L 4 HOH 30  183 159 HOH HOH D . 
L 4 HOH 31  184 176 HOH HOH D . 
L 4 HOH 32  185 177 HOH HOH D . 
L 4 HOH 33  186 178 HOH HOH D . 
L 4 HOH 34  187 179 HOH HOH D . 
L 4 HOH 35  188 180 HOH HOH D . 
L 4 HOH 36  189 181 HOH HOH D . 
L 4 HOH 37  190 182 HOH HOH D . 
L 4 HOH 38  191 187 HOH HOH D . 
L 4 HOH 39  192 207 HOH HOH D . 
L 4 HOH 40  193 221 HOH HOH D . 
L 4 HOH 41  194 225 HOH HOH D . 
L 4 HOH 42  195 226 HOH HOH D . 
L 4 HOH 43  196 227 HOH HOH D . 
L 4 HOH 44  197 228 HOH HOH D . 
L 4 HOH 45  198 229 HOH HOH D . 
L 4 HOH 46  199 230 HOH HOH D . 
L 4 HOH 47  200 342 HOH HOH D . 
L 4 HOH 48  201 344 HOH HOH D . 
L 4 HOH 49  202 345 HOH HOH D . 
L 4 HOH 50  203 346 HOH HOH D . 
L 4 HOH 51  204 347 HOH HOH D . 
L 4 HOH 52  205 348 HOH HOH D . 
L 4 HOH 53  206 349 HOH HOH D . 
L 4 HOH 54  207 350 HOH HOH D . 
L 4 HOH 55  208 351 HOH HOH D . 
L 4 HOH 56  209 353 HOH HOH D . 
L 4 HOH 57  210 354 HOH HOH D . 
L 4 HOH 58  211 355 HOH HOH D . 
L 4 HOH 59  212 356 HOH HOH D . 
L 4 HOH 60  213 357 HOH HOH D . 
L 4 HOH 61  214 358 HOH HOH D . 
L 4 HOH 62  215 359 HOH HOH D . 
L 4 HOH 63  216 360 HOH HOH D . 
L 4 HOH 64  217 449 HOH HOH D . 
L 4 HOH 65  218 463 HOH HOH D . 
L 4 HOH 66  219 464 HOH HOH D . 
L 4 HOH 67  220 465 HOH HOH D . 
L 4 HOH 68  221 466 HOH HOH D . 
L 4 HOH 69  222 467 HOH HOH D . 
L 4 HOH 70  223 468 HOH HOH D . 
L 4 HOH 71  224 469 HOH HOH D . 
L 4 HOH 72  225 470 HOH HOH D . 
L 4 HOH 73  226 471 HOH HOH D . 
L 4 HOH 74  227 472 HOH HOH D . 
L 4 HOH 75  228 473 HOH HOH D . 
L 4 HOH 76  229 474 HOH HOH D . 
L 4 HOH 77  230 475 HOH HOH D . 
L 4 HOH 78  231 476 HOH HOH D . 
L 4 HOH 79  232 477 HOH HOH D . 
L 4 HOH 80  233 478 HOH HOH D . 
L 4 HOH 81  234 479 HOH HOH D . 
L 4 HOH 82  235 480 HOH HOH D . 
L 4 HOH 83  236 481 HOH HOH D . 
L 4 HOH 84  237 517 HOH HOH D . 
L 4 HOH 85  238 518 HOH HOH D . 
L 4 HOH 86  239 519 HOH HOH D . 
L 4 HOH 87  240 520 HOH HOH D . 
L 4 HOH 88  241 521 HOH HOH D . 
L 4 HOH 89  242 522 HOH HOH D . 
L 4 HOH 90  243 523 HOH HOH D . 
L 4 HOH 91  244 524 HOH HOH D . 
L 4 HOH 92  245 525 HOH HOH D . 
L 4 HOH 93  246 526 HOH HOH D . 
L 4 HOH 94  247 527 HOH HOH D . 
L 4 HOH 95  248 528 HOH HOH D . 
L 4 HOH 96  249 529 HOH HOH D . 
L 4 HOH 97  250 530 HOH HOH D . 
L 4 HOH 98  251 531 HOH HOH D . 
L 4 HOH 99  252 532 HOH HOH D . 
L 4 HOH 100 253 533 HOH HOH D . 
L 4 HOH 101 254 537 HOH HOH D . 
# 
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 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,F,G,H,I,J 
2 1 C,D,K,L         
# 
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)'  14230 ? 
2 'ABSA (A^2)' 1440  ? 
2 MORE         -11   ? 
2 'SSA (A^2)'  12120 ? 
# 
_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    B 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     273 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   J 
_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  ND1 ? A HIS 46 ? A HIS 46 ? 1_555 CU ? E CU1 . ? A CU1 154 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 141.2 ? 
2  ND1 ? A HIS 46 ? A HIS 46 ? 1_555 CU ? E CU1 . ? A CU1 154 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 96.1  ? 
3  NE2 ? A HIS 48 ? A HIS 48 ? 1_555 CU ? E CU1 . ? A CU1 154 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 115.9 ? 
4  ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? F ZN  . ? A ZN  155 ? 1_555 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 113.2 ? 
5  ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? F ZN  . ? A ZN  155 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 104.7 ? 
6  ND1 ? A HIS 71 ? A HIS 71 ? 1_555 ZN ? F ZN  . ? A ZN  155 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 124.4 ? 
7  ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? F ZN  . ? A ZN  155 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 110.6 ? 
8  ND1 ? A HIS 71 ? A HIS 71 ? 1_555 ZN ? F ZN  . ? A ZN  155 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 85.0  ? 
9  ND1 ? A HIS 80 ? A HIS 80 ? 1_555 ZN ? F ZN  . ? A ZN  155 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 118.0 ? 
10 ND1 ? B HIS 46 ? B HIS 46 ? 1_555 CU ? G CU1 . ? B CU1 154 ? 1_555 NE2 ? B HIS 48  ? B HIS 48  ? 1_555 139.1 ? 
11 ND1 ? B HIS 46 ? B HIS 46 ? 1_555 CU ? G CU1 . ? B CU1 154 ? 1_555 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 102.1 ? 
12 NE2 ? B HIS 48 ? B HIS 48 ? 1_555 CU ? G CU1 . ? B CU1 154 ? 1_555 NE2 ? B HIS 120 ? B HIS 120 ? 1_555 117.4 ? 
13 ND1 ? B HIS 63 ? B HIS 63 ? 1_555 ZN ? H ZN  . ? B ZN  155 ? 1_555 ND1 ? B HIS 71  ? B HIS 71  ? 1_555 121.7 ? 
14 ND1 ? B HIS 63 ? B HIS 63 ? 1_555 ZN ? H ZN  . ? B ZN  155 ? 1_555 ND1 ? B HIS 80  ? B HIS 80  ? 1_555 105.9 ? 
15 ND1 ? B HIS 71 ? B HIS 71 ? 1_555 ZN ? H ZN  . ? B ZN  155 ? 1_555 ND1 ? B HIS 80  ? B HIS 80  ? 1_555 119.0 ? 
16 ND1 ? B HIS 63 ? B HIS 63 ? 1_555 ZN ? H ZN  . ? B ZN  155 ? 1_555 OD1 ? B ASP 83  ? B ASP 83  ? 1_555 111.2 ? 
17 ND1 ? B HIS 71 ? B HIS 71 ? 1_555 ZN ? H ZN  . ? B ZN  155 ? 1_555 OD1 ? B ASP 83  ? B ASP 83  ? 1_555 85.8  ? 
18 ND1 ? B HIS 80 ? B HIS 80 ? 1_555 ZN ? H ZN  . ? B ZN  155 ? 1_555 OD1 ? B ASP 83  ? B ASP 83  ? 1_555 111.6 ? 
# 
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 2007-01-02 
2 'Structure model' 1 1 2008-05-01 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2018-05-23 
5 'Structure model' 1 4 2021-11-10 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
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' Advisory                    
3 3 'Structure model' 'Version format compliance' 
4 4 'Structure model' 'Data collection'           
5 5 'Structure model' 'Database references'       
6 5 'Structure model' 'Derived calculations'      
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' diffrn_source      
2 5 'Structure model' database_2         
3 5 'Structure model' struct_conn        
4 5 'Structure model' struct_ref_seq_dif 
5 5 'Structure model' struct_site        
# 
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' '_diffrn_source.pdbx_synchrotron_site' 
2  5 'Structure model' '_database_2.pdbx_DOI'                 
3  5 'Structure model' '_database_2.pdbx_database_accession'  
4  5 'Structure model' '_struct_conn.pdbx_dist_value'         
5  5 'Structure model' '_struct_conn.ptnr1_auth_comp_id'      
6  5 'Structure model' '_struct_conn.ptnr1_auth_seq_id'       
7  5 'Structure model' '_struct_conn.ptnr1_label_asym_id'     
8  5 'Structure model' '_struct_conn.ptnr1_label_atom_id'     
9  5 'Structure model' '_struct_conn.ptnr1_label_comp_id'     
10 5 'Structure model' '_struct_conn.ptnr1_label_seq_id'      
11 5 'Structure model' '_struct_conn.ptnr2_auth_comp_id'      
12 5 'Structure model' '_struct_conn.ptnr2_auth_seq_id'       
13 5 'Structure model' '_struct_conn.ptnr2_label_asym_id'     
14 5 'Structure model' '_struct_conn.ptnr2_label_atom_id'     
15 5 'Structure model' '_struct_conn.ptnr2_label_comp_id'     
16 5 'Structure model' '_struct_conn.ptnr2_label_seq_id'      
17 5 'Structure model' '_struct_ref_seq_dif.details'          
18 5 'Structure model' '_struct_site.pdbx_auth_asym_id'       
19 5 'Structure model' '_struct_site.pdbx_auth_comp_id'       
20 5 'Structure model' '_struct_site.pdbx_auth_seq_id'        
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.pdbx_refine_id 
1 ? refined -13.0429 -2.8992 20.8128 -0.2331 -0.0400 -0.2186 -0.0682 0.0042  0.0059  2.2893 1.5362 4.6842 0.1841  1.2149  0.2009  
0.0610 -0.0820 0.0210  0.1605  -0.1477 -0.0500 -0.0523 0.1859  -0.2844 'X-RAY DIFFRACTION' 
2 ? refined -3.7538  3.0887  46.3614 -0.2364 -0.0033 -0.2220 -0.0204 -0.0023 0.0104  2.2868 1.2758 3.6776 0.0207  0.1002  0.1389  
0.0247 0.0641  -0.0888 -0.3395 0.0131  -0.0042 0.1457  0.1141  -0.0202 'X-RAY DIFFRACTION' 
3 ? refined 29.1570  11.8112 30.5120 -0.2413 -0.1314 -0.2148 -0.0402 -0.0042 -0.0127 4.0533 1.3111 4.5178 0.3474  -0.0847 -0.0112 
0.0669 0.0191  -0.0860 -0.3993 0.2244  0.0109  -0.0139 -0.2011 0.1988  'X-RAY DIFFRACTION' 
4 ? refined 23.0501  5.0422  8.3858  -0.1985 -0.1429 -0.2157 -0.0352 -0.0102 0.0166  2.8302 2.2032 5.6411 -0.0465 0.3766  0.1322  
0.0162 0.0013  -0.0175 0.4500  -0.0564 0.0169  -0.1130 0.0903  0.0209  'X-RAY DIFFRACTION' 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.selection_details 
1 1 A 2 A 153 ALL A 2 A 153 'X-RAY DIFFRACTION' ? 
2 2 B 2 B 153 ALL B 2 B 153 'X-RAY DIFFRACTION' ? 
3 3 C 1 C 153 ALL C 1 C 153 'X-RAY DIFFRACTION' ? 
4 4 D 2 D 153 ALL D 2 D 153 'X-RAY DIFFRACTION' ? 
# 
loop_
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
_software.pdbx_ordinal 
SCALA       .         ?              program 'Phil Evans'      pre@mrc-lmb.cam.ac.uk    'data scaling'    
http://www.ccp4.ac.uk/dist/html/INDEX.html Fortran ? 1 
REFMAC      5.2.0005  ?              program 'Murshudov, G.N.' ccp4@dl.ac.uk            refinement        
http://www.ccp4.ac.uk/main.html            Fortran ? 2 
PDB_EXTRACT 1.701     'Nov. 1, 2005' package PDB               sw-help@rcsb.rutgers.edu 'data extraction' 
http://pdb.rutgers.edu/software/           C++     ? 3 
MOSFLM      .         ?              ?       ?                 ?                        'data reduction'  ? ?       ? 4 
CCP4        '(SCALA)' ?              ?       ?                 ?                        'data scaling'    ? ?       ? 5 
CNS         .         ?              ?       ?                 ?                        phasing           ? ?       ? 6 
# 
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 79 ? ? CZ B ARG 79 ? ? NH1 B ARG 79 ? ? 123.89 120.30 3.59  0.50 N 
2 1 NE B ARG 79 ? ? CZ B ARG 79 ? ? NH2 B ARG 79 ? ? 116.11 120.30 -4.19 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 A 98  ? ? -156.73 69.61  
2 1 ASN C 65  ? ? -156.53 84.99  
3 1 ALA C 111 ? ? -48.60  151.15 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A ALA 1   ? A ALA 1   
2  1 Y 1 B ALA 1   ? B ALA 1   
3  1 Y 1 C ARG 69  ? C ARG 69  
4  1 Y 1 C LYS 70  ? C LYS 70  
5  1 Y 1 C HIS 71  ? C HIS 71  
6  1 Y 1 C GLY 72  ? C GLY 72  
7  1 Y 1 C GLY 73  ? C GLY 73  
8  1 Y 1 C PRO 74  ? C PRO 74  
9  1 Y 1 C LYS 75  ? C LYS 75  
10 1 Y 1 C ASP 76  ? C ASP 76  
11 1 Y 1 C GLU 77  ? C GLU 77  
12 1 Y 1 C GLU 78  ? C GLU 78  
13 1 Y 1 C ASP 125 ? C ASP 125 
14 1 Y 1 C LEU 126 ? C LEU 126 
15 1 Y 1 C GLY 127 ? C GLY 127 
16 1 Y 1 C LYS 128 ? C LYS 128 
17 1 Y 1 C GLY 129 ? C GLY 129 
18 1 Y 1 C GLY 130 ? C GLY 130 
19 1 Y 1 C ASN 131 ? C ASN 131 
20 1 Y 1 C GLU 132 ? C GLU 132 
21 1 Y 1 C GLU 133 ? C GLU 133 
22 1 Y 1 C SER 134 ? C SER 134 
23 1 Y 1 C THR 135 ? C THR 135 
24 1 Y 1 C LYS 136 ? C LYS 136 
25 1 Y 1 C THR 137 ? C THR 137 
26 1 Y 1 C GLY 138 ? C GLY 138 
27 1 Y 1 C ASN 139 ? C ASN 139 
28 1 Y 1 C ALA 140 ? C ALA 140 
29 1 Y 1 C GLY 141 ? C GLY 141 
30 1 Y 1 D ALA 1   ? D ALA 1   
31 1 Y 1 D LEU 67  ? D LEU 67  
32 1 Y 1 D SER 68  ? D SER 68  
33 1 Y 1 D ARG 69  ? D ARG 69  
34 1 Y 1 D LYS 70  ? D LYS 70  
35 1 Y 1 D HIS 71  ? D HIS 71  
36 1 Y 1 D GLY 72  ? D GLY 72  
37 1 Y 1 D GLY 73  ? D GLY 73  
38 1 Y 1 D PRO 74  ? D PRO 74  
39 1 Y 1 D LYS 75  ? D LYS 75  
40 1 Y 1 D ASP 76  ? D ASP 76  
41 1 Y 1 D GLU 77  ? D GLU 77  
42 1 Y 1 D ASP 125 ? D ASP 125 
43 1 Y 1 D LEU 126 ? D LEU 126 
44 1 Y 1 D GLY 127 ? D GLY 127 
45 1 Y 1 D LYS 128 ? D LYS 128 
46 1 Y 1 D GLY 129 ? D GLY 129 
47 1 Y 1 D GLY 130 ? D GLY 130 
48 1 Y 1 D ASN 131 ? D ASN 131 
49 1 Y 1 D GLU 132 ? D GLU 132 
50 1 Y 1 D GLU 133 ? D GLU 133 
51 1 Y 1 D SER 134 ? D SER 134 
52 1 Y 1 D THR 135 ? D THR 135 
53 1 Y 1 D LYS 136 ? D LYS 136 
54 1 Y 1 D THR 137 ? D THR 137 
55 1 Y 1 D GLY 138 ? D GLY 138 
56 1 Y 1 D ASN 139 ? D ASN 139 
57 1 Y 1 D ALA 140 ? D ALA 140 
58 1 Y 1 D GLY 141 ? D GLY 141 
# 
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 water            HOH 
# 
