data_2G64
# 
_entry.id   2G64 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.377 
_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   2G64         pdb_00002g64 10.2210/pdb2g64/pdb 
RCSB  RCSB036735   ?            ?                   
WWPDB D_1000036735 ?            ?                   
# 
_pdbx_database_related.db_name        TargetDB 
_pdbx_database_related.db_id          NYSGXRC-T2216 
_pdbx_database_related.details        . 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2G64 
_pdbx_database_status.recvd_initial_deposition_date   2006-02-24 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.SG_entry                        Y 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Wengerter, B.C.'                                                1 ?                   
'Patskovsky, Y.'                                                 2 ?                   
'Zhan, C.'                                                       3 ?                   
'Ramagopal, U.'                                                  4 ?                   
'Milstein, S.'                                                   5 ?                   
'Vidal, M.'                                                      6 ?                   
'Almo, S.C.'                                                     7 ?                   
'Burley, S.K.'                                                   8 0000-0002-2487-9713 
'New York SGX Research Center for Structural Genomics (NYSGXRC)' 9 ?                   
# 
_citation.id                        primary 
_citation.title                     'Crystal Structure of Caenorhabditis Elegans 6-Pyruvoyl Tetrahydropterin Synthase' 
_citation.journal_abbrev            'To be Published' 
_citation.journal_volume            ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.year                      ? 
_citation.journal_id_ASTM           ? 
_citation.country                   ? 
_citation.journal_id_ISSN           ? 
_citation.journal_id_CSD            0353 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_DOI      ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Wengerter, B.C.' 1 ? 
primary 'Patskovsky, Y.'  2 ? 
primary 'Zhan, C.'        3 ? 
primary 'Ramagopal, U.'   4 ? 
primary 'Milstein, S.'    5 ? 
primary 'Vidal, M.'       6 ? 
primary 'Almo, S.C.'      7 ? 
# 
_cell.entry_id           2G64 
_cell.length_a           69.792 
_cell.length_b           69.792 
_cell.length_c           160.188 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              18 
_cell.pdbx_unique_axis   ? 
_cell.length_a_esd       ? 
_cell.length_b_esd       ? 
_cell.length_c_esd       ? 
_cell.angle_alpha_esd    ? 
_cell.angle_beta_esd     ? 
_cell.angle_gamma_esd    ? 
# 
_symmetry.entry_id                         2G64 
_symmetry.space_group_name_H-M             'H 3 2' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                155 
_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 'Putative 6-pyruvoyl tetrahydrobiopterin synthase' 16055.360 1   4.2.3.12 C140S ? ? 
2 non-polymer syn 'SODIUM ION'                                       22.990    2   ?        ?     ? ? 
3 non-polymer syn 'ZINC ION'                                         65.409    1   ?        ?     ? ? 
4 non-polymer syn GLYCEROL                                           92.094    1   ?        ?     ? ? 
5 water       nat water                                              18.015    167 ?        ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'PTPS, PTP synthase' 
# 
_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       
;MFRMPIVTMERVDSFSAAHRLHSEKLSDAENKETFGKCNNSNGHGHNYVWKVKLRGEVDPTSGMVYDLAKLKKEMSLVLD
TVDHRNLDKDVEFFKTTVSTSENVAIYMFEKLKSVMSNPSVLYKVTIEETPKNIFTYKGS
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MFRMPIVTMERVDSFSAAHRLHSEKLSDAENKETFGKCNNSNGHGHNYVWKVKLRGEVDPTSGMVYDLAKLKKEMSLVLD
TVDHRNLDKDVEFFKTTVSTSENVAIYMFEKLKSVMSNPSVLYKVTIEETPKNIFTYKGS
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         NYSGXRC-T2216 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   PHE n 
1 3   ARG n 
1 4   MET n 
1 5   PRO n 
1 6   ILE n 
1 7   VAL n 
1 8   THR n 
1 9   MET n 
1 10  GLU n 
1 11  ARG n 
1 12  VAL n 
1 13  ASP n 
1 14  SER n 
1 15  PHE n 
1 16  SER n 
1 17  ALA n 
1 18  ALA n 
1 19  HIS n 
1 20  ARG n 
1 21  LEU n 
1 22  HIS n 
1 23  SER n 
1 24  GLU n 
1 25  LYS n 
1 26  LEU n 
1 27  SER n 
1 28  ASP n 
1 29  ALA n 
1 30  GLU n 
1 31  ASN n 
1 32  LYS n 
1 33  GLU n 
1 34  THR n 
1 35  PHE n 
1 36  GLY n 
1 37  LYS n 
1 38  CYS n 
1 39  ASN n 
1 40  ASN n 
1 41  SER n 
1 42  ASN n 
1 43  GLY n 
1 44  HIS n 
1 45  GLY n 
1 46  HIS n 
1 47  ASN n 
1 48  TYR n 
1 49  VAL n 
1 50  TRP n 
1 51  LYS n 
1 52  VAL n 
1 53  LYS n 
1 54  LEU n 
1 55  ARG n 
1 56  GLY n 
1 57  GLU n 
1 58  VAL n 
1 59  ASP n 
1 60  PRO n 
1 61  THR n 
1 62  SER n 
1 63  GLY n 
1 64  MET n 
1 65  VAL n 
1 66  TYR n 
1 67  ASP n 
1 68  LEU n 
1 69  ALA n 
1 70  LYS n 
1 71  LEU n 
1 72  LYS n 
1 73  LYS n 
1 74  GLU n 
1 75  MET n 
1 76  SER n 
1 77  LEU n 
1 78  VAL n 
1 79  LEU n 
1 80  ASP n 
1 81  THR n 
1 82  VAL n 
1 83  ASP n 
1 84  HIS n 
1 85  ARG n 
1 86  ASN n 
1 87  LEU n 
1 88  ASP n 
1 89  LYS n 
1 90  ASP n 
1 91  VAL n 
1 92  GLU n 
1 93  PHE n 
1 94  PHE n 
1 95  LYS n 
1 96  THR n 
1 97  THR n 
1 98  VAL n 
1 99  SER n 
1 100 THR n 
1 101 SER n 
1 102 GLU n 
1 103 ASN n 
1 104 VAL n 
1 105 ALA n 
1 106 ILE n 
1 107 TYR n 
1 108 MET n 
1 109 PHE n 
1 110 GLU n 
1 111 LYS n 
1 112 LEU n 
1 113 LYS n 
1 114 SER n 
1 115 VAL n 
1 116 MET n 
1 117 SER n 
1 118 ASN n 
1 119 PRO n 
1 120 SER n 
1 121 VAL n 
1 122 LEU n 
1 123 TYR n 
1 124 LYS n 
1 125 VAL n 
1 126 THR n 
1 127 ILE n 
1 128 GLU n 
1 129 GLU n 
1 130 THR n 
1 131 PRO n 
1 132 LYS n 
1 133 ASN n 
1 134 ILE n 
1 135 PHE n 
1 136 THR n 
1 137 TYR n 
1 138 LYS n 
1 139 GLY n 
1 140 SER 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               ? 
_entity_src_gen.gene_src_genus                     Caenorhabditis 
_entity_src_gen.pdbx_gene_src_gene                 B0041.6 
_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      'Caenorhabditis elegans' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     6239 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     Escherichia 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21 AI' 
_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                       pET3a 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    PTPS_CAEEL 
_struct_ref.pdbx_db_accession          O02058 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MFRMPIVTMERVDSFSAAHRLHSEKLSDAENKETFGKCNNSNGHGHNYVWKVKLRGEVDPTSGMVYDLAKLKKEMSLVLD
TVDHRNLDKDVEFFKTTVSTSENVAIYMFEKLKSVMSNPSVLYKVTIEETPKNIFTYKGC
;
_struct_ref.pdbx_align_begin           1 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              2G64 
_struct_ref_seq.pdbx_strand_id                A 
_struct_ref_seq.seq_align_beg                 1 
_struct_ref_seq.pdbx_seq_align_beg_ins_code   ? 
_struct_ref_seq.seq_align_end                 140 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             O02058 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  140 
_struct_ref_seq.pdbx_db_align_end_ins_code    ? 
_struct_ref_seq.pdbx_auth_seq_align_beg       1 
_struct_ref_seq.pdbx_auth_seq_align_end       140 
# 
_struct_ref_seq_dif.align_id                     1 
_struct_ref_seq_dif.pdbx_pdb_id_code             2G64 
_struct_ref_seq_dif.mon_id                       SER 
_struct_ref_seq_dif.pdbx_pdb_strand_id           A 
_struct_ref_seq_dif.seq_num                      140 
_struct_ref_seq_dif.pdbx_pdb_ins_code            ? 
_struct_ref_seq_dif.pdbx_seq_db_name             UNP 
_struct_ref_seq_dif.pdbx_seq_db_accession_code   O02058 
_struct_ref_seq_dif.db_mon_id                    CYS 
_struct_ref_seq_dif.pdbx_seq_db_seq_num          140 
_struct_ref_seq_dif.details                      'engineered mutation' 
_struct_ref_seq_dif.pdbx_auth_seq_num            140 
_struct_ref_seq_dif.pdbx_ordinal                 1 
# 
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 
CYS 'L-peptide linking' y CYSTEINE        ?                               'C3 H7 N O2 S'   121.158 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
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 
MET 'L-peptide linking' y METHIONINE      ?                               'C5 H11 N O2 S'  149.211 
NA  non-polymer         . 'SODIUM ION'    ?                               'Na 1'           22.990  
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 
TYR 'L-peptide linking' y TYROSINE        ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                               'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'      ?                               'Zn 2'           65.409  
# 
_exptl.entry_id          2G64 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.34 
_exptl_crystal.density_percent_sol   47.38 
_exptl_crystal.description           ? 
_exptl_crystal.F_000                 ? 
_exptl_crystal.preparation           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.temp            290 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              7.00 
_exptl_crystal_grow.pdbx_details    
'100 MM HEPES, 1 M SODIUM SUCCINATE, PH 7.00, 1% PEG 2000ME, VAPOR DIFFUSION, SITTING DROP, temperature 290K' 
_exptl_crystal_grow.pdbx_pH_range   . 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100.0 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'RIGAKU RAXIS IV' 
_diffrn_detector.pdbx_collection_date   2006-01-31 
_diffrn_detector.details                MIRRORS 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    MIRRORS 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.5418 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      'ROTATING ANODE' 
_diffrn_source.type                        'RIGAKU RU200' 
_diffrn_source.pdbx_synchrotron_site       ? 
_diffrn_source.pdbx_synchrotron_beamline   ? 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_wavelength_list        1.5418 
# 
_reflns.entry_id                     2G64 
_reflns.observed_criterion_sigma_I   0.000 
_reflns.observed_criterion_sigma_F   0.000 
_reflns.d_resolution_low             50.000 
_reflns.d_resolution_high            1.800 
_reflns.number_obs                   14091 
_reflns.number_all                   14091 
_reflns.percent_possible_obs         98.7 
_reflns.pdbx_Rmerge_I_obs            0.031 
_reflns.pdbx_Rsym_value              0.03 
_reflns.pdbx_netI_over_sigmaI        38.9000 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              10.400 
_reflns.R_free_details               ? 
_reflns.limit_h_max                  ? 
_reflns.limit_h_min                  ? 
_reflns.limit_k_max                  ? 
_reflns.limit_k_min                  ? 
_reflns.limit_l_max                  ? 
_reflns.limit_l_min                  ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.pdbx_chi_squared             ? 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_ordinal                 1 
_reflns.pdbx_diffrn_id               1 
# 
_reflns_shell.d_res_high             1.80 
_reflns_shell.d_res_low              1.86 
_reflns_shell.percent_possible_all   97.9 
_reflns_shell.Rmerge_I_obs           0.094 
_reflns_shell.pdbx_Rsym_value        0.103 
_reflns_shell.meanI_over_sigI_obs    14.600 
_reflns_shell.pdbx_redundancy        5.20 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      1380 
_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.entry_id                                 2G64 
_refine.ls_number_reflns_obs                     13641 
_refine.ls_number_reflns_all                     13641 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.00 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             20.00 
_refine.ls_d_res_high                            1.80 
_refine.ls_percent_reflns_obs                    98.70 
_refine.ls_R_factor_obs                          0.16238 
_refine.ls_R_factor_all                          0.163 
_refine.ls_R_factor_R_work                       0.16058 
_refine.ls_R_factor_R_free                       0.21902 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 3.1 
_refine.ls_number_reflns_R_free                  442 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.960 
_refine.correlation_coeff_Fo_to_Fc_free          0.925 
_refine.B_iso_mean                               22.347 
_refine.aniso_B[1][1]                            0.11 
_refine.aniso_B[2][2]                            0.11 
_refine.aniso_B[3][3]                            -0.16 
_refine.aniso_B[1][2]                            0.05 
_refine.aniso_B[1][3]                            0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.pdbx_starting_model                      1B66 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             isotropic 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.120 
_refine.pdbx_overall_ESU_R_Free                  0.126 
_refine.overall_SU_ML                            0.081 
_refine.overall_SU_B                             2.541 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.B_iso_min                                ? 
_refine.B_iso_max                                ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.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_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
# 
_refine_analyze.entry_id                        2G64 
_refine_analyze.Luzzati_coordinate_error_obs    0.171 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           5.0 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      ? 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_refine_analyze.pdbx_Luzzati_d_res_high_obs     ? 
_refine_analyze.pdbx_refine_id                  'X-RAY DIFFRACTION' 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1124 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         9 
_refine_hist.number_atoms_solvent             167 
_refine_hist.number_atoms_total               1300 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        20.00 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d         0.011  0.022  ? 1226 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg      1.251  1.965  ? 1666 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg   6.227  5.000  ? 163  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg   36.923 24.340 ? 53   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg   14.944 15.000 ? 246  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg   23.580 15.000 ? 6    'X-RAY DIFFRACTION' ? 
r_chiral_restr           0.113  0.200  ? 189  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined     0.005  0.020  ? 903  'X-RAY DIFFRACTION' ? 
r_nbd_refined            0.232  0.300  ? 560  'X-RAY DIFFRACTION' ? 
r_nbtor_refined          0.310  0.500  ? 833  'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined    0.189  0.500  ? 233  'X-RAY DIFFRACTION' ? 
r_metal_ion_refined      0.193  0.500  ? 1    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined   0.187  0.300  ? 89   'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined 0.280  0.500  ? 33   'X-RAY DIFFRACTION' ? 
r_mcbond_it              4.136  2.000  ? 737  'X-RAY DIFFRACTION' ? 
r_mcangle_it             5.346  3.000  ? 1217 'X-RAY DIFFRACTION' ? 
r_scbond_it              9.172  3.000  ? 499  'X-RAY DIFFRACTION' ? 
r_scangle_it             10.877 5.000  ? 436  'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.800 
_refine_ls_shell.d_res_low                        1.847 
_refine_ls_shell.number_reflns_R_work             981 
_refine_ls_shell.R_factor_R_work                  0.208 
_refine_ls_shell.percent_reflns_obs               97.40 
_refine_ls_shell.R_factor_R_free                  0.333 
_refine_ls_shell.R_factor_R_free_error            0.02 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             30 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.number_reflns_obs                981 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  2G64 
_struct.title                     'Structure of Caenorhabditis elegans 6-pyruvoyl tetrahydropterin synthase' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2G64 
_struct_keywords.pdbx_keywords   LYASE 
_struct_keywords.text            
;TETRAHYDROBIOPTERIN BIOSYNTHESIS, PHOSPHATE ELIMINATION, PTERINE SYNTHESIS, Structural Genomics, PSI, Protein Structure Initiative, New York SGX Research Center for Structural Genomics, NYSGXRC, Lyase
;
# 
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 2 ? 
C N N 2 ? 
D N N 3 ? 
E N N 4 ? 
F N N 5 ? 
# 
_struct_biol.id   1 
# 
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 SER A 27  ? GLY A 36  ? SER A 27  GLY A 36  1 ? 10 
HELX_P HELX_P2 2 LYS A 37  ? ASN A 40  ? LYS A 37  ASN A 40  5 ? 4  
HELX_P HELX_P3 3 ASP A 67  ? THR A 81  ? ASP A 67  THR A 81  1 ? 15 
HELX_P HELX_P4 4 LEU A 87  ? VAL A 91  ? LEU A 87  VAL A 91  1 ? 5  
HELX_P HELX_P5 5 GLU A 92  ? THR A 96  ? GLU A 92  THR A 96  5 ? 5  
HELX_P HELX_P6 6 THR A 100 ? MET A 116 ? THR A 100 MET A 116 1 ? 17 
HELX_P HELX_P7 7 ASN A 118 ? SER A 120 ? ASN A 118 SER A 120 5 ? 3  
# 
_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 
metalc1  metalc ? ? A HIS 19 NE2 ? ? ? 1_555 D ZN  . ZN ? ? A HIS 19   A ZN  2001 1_555  ? ? ? ? ? ? ? 2.128 ? ? 
metalc2  metalc ? ? A CYS 38 O   ? ? ? 1_555 C NA  . NA ? ? A CYS 38   A NA  1002 1_555  ? ? ? ? ? ? ? 2.731 ? ? 
metalc3  metalc ? ? A ASN 40 O   ? ? ? 1_555 C NA  . NA ? ? A ASN 40   A NA  1002 1_555  ? ? ? ? ? ? ? 2.833 ? ? 
metalc4  metalc ? ? A HIS 44 ND1 ? ? ? 1_555 C NA  . NA ? ? A HIS 44   A NA  1002 1_555  ? ? ? ? ? ? ? 2.867 ? ? 
metalc5  metalc ? ? A HIS 44 NE2 ? ? ? 1_555 D ZN  . ZN ? ? A HIS 44   A ZN  2001 1_555  ? ? ? ? ? ? ? 2.137 ? ? 
metalc6  metalc ? ? A HIS 46 NE2 ? ? ? 1_555 D ZN  . ZN ? ? A HIS 46   A ZN  2001 1_555  ? ? ? ? ? ? ? 2.097 ? ? 
metalc7  metalc ? ? A ASN 47 O   ? ? ? 1_555 B NA  . NA ? ? A ASN 47   A NA  1001 1_555  ? ? ? ? ? ? ? 2.986 ? ? 
metalc8  metalc ? ? B NA  .  NA  ? ? ? 1_555 F HOH . O  ? ? A NA  1001 A HOH 3019 1_555  ? ? ? ? ? ? ? 2.652 ? ? 
metalc9  metalc ? ? B NA  .  NA  ? ? ? 1_555 F HOH . O  ? ? A NA  1001 A HOH 3117 1_555  ? ? ? ? ? ? ? 2.777 ? ? 
metalc10 metalc ? ? D ZN  .  ZN  ? ? ? 1_555 F HOH . O  ? ? A ZN  2001 A HOH 3084 11_566 ? ? ? ? ? ? ? 2.727 ? ? 
metalc11 metalc ? ? D ZN  .  ZN  ? ? ? 1_555 F HOH . O  ? ? A ZN  2001 A HOH 3139 1_555  ? ? ? ? ? ? ? 1.827 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
_struct_sheet.id               A 
_struct_sheet.type             ? 
_struct_sheet.number_strands   5 
_struct_sheet.details          ? 
# 
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 ? parallel      
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
A 4 5 ? 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 ARG A 85  ? ASN A 86  ? ARG A 85  ASN A 86  
A 2 ILE A 6   ? HIS A 19  ? ILE A 6   HIS A 19  
A 3 HIS A 44  ? GLU A 57  ? HIS A 44  GLU A 57  
A 4 LEU A 122 ? THR A 130 ? LEU A 122 THR A 130 
A 5 ASN A 133 ? TYR A 137 ? ASN A 133 TYR A 137 
# 
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 ARG A 85  ? O ARG A 85  N ALA A 18  ? N ALA A 18  
A 2 3 N MET A 9   ? N MET A 9   O LEU A 54  ? O LEU A 54  
A 3 4 N LYS A 53  ? N LYS A 53  O LYS A 124 ? O LYS A 124 
A 4 5 N ILE A 127 ? N ILE A 127 O PHE A 135 ? O PHE A 135 
# 
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 NA  1001 ? 7 'BINDING SITE FOR RESIDUE NA A 1001'  
AC2 Software A NA  1002 ? 5 'BINDING SITE FOR RESIDUE NA A 1002'  
AC3 Software A ZN  2001 ? 5 'BINDING SITE FOR RESIDUE ZN A 2001'  
AC4 Software A GOL 3001 ? 5 'BINDING SITE FOR RESIDUE GOL A 3001' 
# 
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 7 ASN A 47  ? ASN A 47   . ? 1_555  ? 
2  AC1 7 GLU A 128 ? GLU A 128  . ? 1_555  ? 
3  AC1 7 GLU A 129 ? GLU A 129  . ? 1_555  ? 
4  AC1 7 THR A 130 ? THR A 130  . ? 1_555  ? 
5  AC1 7 PRO A 131 ? PRO A 131  . ? 1_555  ? 
6  AC1 7 HOH F .   ? HOH A 3019 . ? 1_555  ? 
7  AC1 7 HOH F .   ? HOH A 3117 . ? 1_555  ? 
8  AC2 5 ARG A 20  ? ARG A 20   . ? 1_555  ? 
9  AC2 5 CYS A 38  ? CYS A 38   . ? 1_555  ? 
10 AC2 5 ASN A 40  ? ASN A 40   . ? 1_555  ? 
11 AC2 5 GLY A 43  ? GLY A 43   . ? 1_555  ? 
12 AC2 5 HIS A 44  ? HIS A 44   . ? 1_555  ? 
13 AC3 5 HIS A 19  ? HIS A 19   . ? 1_555  ? 
14 AC3 5 HIS A 44  ? HIS A 44   . ? 1_555  ? 
15 AC3 5 HIS A 46  ? HIS A 46   . ? 1_555  ? 
16 AC3 5 HOH F .   ? HOH A 3084 . ? 11_566 ? 
17 AC3 5 HOH F .   ? HOH A 3139 . ? 1_555  ? 
18 AC4 5 LYS A 53  ? LYS A 53   . ? 1_555  ? 
19 AC4 5 TYR A 123 ? TYR A 123  . ? 1_555  ? 
20 AC4 5 LYS A 124 ? LYS A 124  . ? 1_555  ? 
21 AC4 5 HOH F .   ? HOH A 3116 . ? 2_665  ? 
22 AC4 5 HOH F .   ? HOH A 3121 . ? 1_555  ? 
# 
_database_PDB_matrix.entry_id          2G64 
_database_PDB_matrix.origx[1][1]       1.000000 
_database_PDB_matrix.origx[1][2]       0.000000 
_database_PDB_matrix.origx[1][3]       0.000000 
_database_PDB_matrix.origx[2][1]       0.000000 
_database_PDB_matrix.origx[2][2]       1.000000 
_database_PDB_matrix.origx[2][3]       0.000000 
_database_PDB_matrix.origx[3][1]       0.000000 
_database_PDB_matrix.origx[3][2]       0.000000 
_database_PDB_matrix.origx[3][3]       1.000000 
_database_PDB_matrix.origx_vector[1]   0.00000 
_database_PDB_matrix.origx_vector[2]   0.00000 
_database_PDB_matrix.origx_vector[3]   0.00000 
# 
_atom_sites.entry_id                    2G64 
_atom_sites.fract_transf_matrix[1][1]   0.014328 
_atom_sites.fract_transf_matrix[1][2]   0.008272 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.016545 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.006243 
_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  
N  
NA 
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   . MET A 1 1   ? -6.597  14.507 71.508  1.00 16.02 ? 1    MET A N   1 
ATOM   2    C  CA  A MET A 1 1   ? -6.034  15.550 72.411  0.50 14.95 ? 1    MET A CA  1 
ATOM   3    C  CA  B MET A 1 1   ? -6.077  15.488 72.491  0.50 15.32 ? 1    MET A CA  1 
ATOM   4    C  C   . MET A 1 1   ? -7.073  16.593 72.819  1.00 15.96 ? 1    MET A C   1 
ATOM   5    O  O   . MET A 1 1   ? -7.950  16.947 72.029  1.00 13.47 ? 1    MET A O   1 
ATOM   6    C  CB  A MET A 1 1   ? -4.845  16.243 71.741  0.50 25.45 ? 1    MET A CB  1 
ATOM   7    C  CB  B MET A 1 1   ? -4.738  16.081 72.040  0.50 12.49 ? 1    MET A CB  1 
ATOM   8    C  CG  A MET A 1 1   ? -5.183  16.961 70.434  0.50 12.59 ? 1    MET A CG  1 
ATOM   9    C  CG  B MET A 1 1   ? -4.851  17.269 71.101  0.50 36.39 ? 1    MET A CG  1 
ATOM   10   S  SD  A MET A 1 1   ? -3.691  17.480 69.575  0.50 10.25 ? 1    MET A SD  1 
ATOM   11   S  SD  B MET A 1 1   ? -4.802  16.744 69.384  0.50 29.39 ? 1    MET A SD  1 
ATOM   12   C  CE  A MET A 1 1   ? -4.394  18.200 68.088  0.50 9.50  ? 1    MET A CE  1 
ATOM   13   C  CE  B MET A 1 1   ? -4.814  18.309 68.510  0.50 27.43 ? 1    MET A CE  1 
ATOM   14   N  N   . PHE A 1 2   ? -6.949  17.123 74.029  1.00 19.02 ? 2    PHE A N   1 
ATOM   15   C  CA  . PHE A 1 2   ? -7.886  18.124 74.509  1.00 17.28 ? 2    PHE A CA  1 
ATOM   16   C  C   . PHE A 1 2   ? -7.080  19.050 75.412  1.00 16.80 ? 2    PHE A C   1 
ATOM   17   O  O   . PHE A 1 2   ? -6.567  18.617 76.441  1.00 15.11 ? 2    PHE A O   1 
ATOM   18   C  CB  . PHE A 1 2   ? -8.962  17.440 75.353  1.00 12.13 ? 2    PHE A CB  1 
ATOM   19   C  CG  . PHE A 1 2   ? -10.014 18.383 75.892  1.00 14.54 ? 2    PHE A CG  1 
ATOM   20   C  CD1 . PHE A 1 2   ? -11.105 18.782 75.094  1.00 17.77 ? 2    PHE A CD1 1 
ATOM   21   C  CD2 . PHE A 1 2   ? -9.934  18.855 77.208  1.00 20.18 ? 2    PHE A CD2 1 
ATOM   22   C  CE1 . PHE A 1 2   ? -12.092 19.655 75.596  1.00 19.45 ? 2    PHE A CE1 1 
ATOM   23   C  CE2 . PHE A 1 2   ? -10.919 19.720 77.717  1.00 21.16 ? 2    PHE A CE2 1 
ATOM   24   C  CZ  . PHE A 1 2   ? -12.001 20.120 76.907  1.00 18.93 ? 2    PHE A CZ  1 
ATOM   25   N  N   . ARG A 1 3   ? -6.945  20.307 75.035  1.00 12.98 ? 3    ARG A N   1 
ATOM   26   C  CA  A ARG A 1 3   ? -6.201  21.216 75.891  0.50 17.31 ? 3    ARG A CA  1 
ATOM   27   C  CA  B ARG A 1 3   ? -6.217  21.276 75.870  0.50 13.47 ? 3    ARG A CA  1 
ATOM   28   C  C   . ARG A 1 3   ? -6.994  21.556 77.155  1.00 16.84 ? 3    ARG A C   1 
ATOM   29   O  O   . ARG A 1 3   ? -8.188  21.888 77.107  1.00 14.91 ? 3    ARG A O   1 
ATOM   30   C  CB  A ARG A 1 3   ? -5.732  22.461 75.145  0.50 18.07 ? 3    ARG A CB  1 
ATOM   31   C  CB  B ARG A 1 3   ? -5.992  22.588 75.120  0.50 11.30 ? 3    ARG A CB  1 
ATOM   32   C  CG  A ARG A 1 3   ? -4.399  22.972 75.676  0.50 14.79 ? 3    ARG A CG  1 
ATOM   33   C  CG  B ARG A 1 3   ? -5.265  23.644 75.974  0.50 10.79 ? 3    ARG A CG  1 
ATOM   34   C  CD  A ARG A 1 3   ? -3.900  24.165 74.918  0.50 22.30 ? 3    ARG A CD  1 
ATOM   35   C  CD  B ARG A 1 3   ? -5.024  24.915 75.215  0.50 14.12 ? 3    ARG A CD  1 
ATOM   36   N  NE  A ARG A 1 3   ? -4.550  25.382 75.380  0.50 41.45 ? 3    ARG A NE  1 
ATOM   37   N  NE  B ARG A 1 3   ? -6.253  25.670 74.989  0.50 29.71 ? 3    ARG A NE  1 
ATOM   38   C  CZ  A ARG A 1 3   ? -3.901  26.459 75.804  0.50 19.09 ? 3    ARG A CZ  1 
ATOM   39   C  CZ  B ARG A 1 3   ? -6.454  26.485 73.955  0.50 23.81 ? 3    ARG A CZ  1 
ATOM   40   N  NH1 A ARG A 1 3   ? -2.574  26.475 75.825  0.50 42.59 ? 3    ARG A NH1 1 
ATOM   41   N  NH1 B ARG A 1 3   ? -7.603  27.126 73.834  0.50 25.18 ? 3    ARG A NH1 1 
ATOM   42   N  NH2 A ARG A 1 3   ? -4.583  27.522 76.209  0.50 37.45 ? 3    ARG A NH2 1 
ATOM   43   N  NH2 B ARG A 1 3   ? -5.505  26.662 73.048  0.50 39.90 ? 3    ARG A NH2 1 
ATOM   44   N  N   . MET A 1 4   ? -6.313  21.434 78.292  1.00 13.74 ? 4    MET A N   1 
ATOM   45   C  CA  . MET A 1 4   ? -6.927  21.628 79.578  1.00 14.75 ? 4    MET A CA  1 
ATOM   46   C  C   . MET A 1 4   ? -6.848  23.117 79.987  1.00 13.88 ? 4    MET A C   1 
ATOM   47   O  O   . MET A 1 4   ? -6.075  23.887 79.412  1.00 15.89 ? 4    MET A O   1 
ATOM   48   C  CB  . MET A 1 4   ? -6.213  20.740 80.606  1.00 14.35 ? 4    MET A CB  1 
ATOM   49   C  CG  . MET A 1 4   ? -6.509  19.228 80.465  1.00 16.10 ? 4    MET A CG  1 
ATOM   50   S  SD  . MET A 1 4   ? -8.244  18.856 80.884  1.00 22.11 ? 4    MET A SD  1 
ATOM   51   C  CE  . MET A 1 4   ? -8.079  18.907 82.683  1.00 22.42 ? 4    MET A CE  1 
ATOM   52   N  N   . PRO A 1 5   ? -7.642  23.512 81.002  1.00 14.57 ? 5    PRO A N   1 
ATOM   53   C  CA  . PRO A 1 5   ? -7.574  24.895 81.499  1.00 18.03 ? 5    PRO A CA  1 
ATOM   54   C  C   . PRO A 1 5   ? -6.154  25.241 81.928  1.00 14.01 ? 5    PRO A C   1 
ATOM   55   O  O   . PRO A 1 5   ? -5.451  24.386 82.472  1.00 15.06 ? 5    PRO A O   1 
ATOM   56   C  CB  . PRO A 1 5   ? -8.487  24.871 82.729  1.00 17.50 ? 5    PRO A CB  1 
ATOM   57   C  CG  . PRO A 1 5   ? -9.442  23.747 82.471  1.00 19.80 ? 5    PRO A CG  1 
ATOM   58   C  CD  . PRO A 1 5   ? -8.645  22.703 81.721  1.00 15.68 ? 5    PRO A CD  1 
ATOM   59   N  N   . ILE A 1 6   ? -5.768  26.494 81.712  1.00 14.73 ? 6    ILE A N   1 
ATOM   60   C  CA  . ILE A 1 6   ? -4.463  26.990 82.128  1.00 15.03 ? 6    ILE A CA  1 
ATOM   61   C  C   . ILE A 1 6   ? -4.625  27.714 83.480  1.00 15.83 ? 6    ILE A C   1 
ATOM   62   O  O   . ILE A 1 6   ? -5.453  28.611 83.630  1.00 13.21 ? 6    ILE A O   1 
ATOM   63   C  CB  . ILE A 1 6   ? -3.882  27.978 81.097  1.00 17.54 ? 6    ILE A CB  1 
ATOM   64   C  CG1 . ILE A 1 6   ? -3.786  27.329 79.709  1.00 26.32 ? 6    ILE A CG1 1 
ATOM   65   C  CG2 . ILE A 1 6   ? -2.505  28.492 81.539  1.00 20.74 ? 6    ILE A CG2 1 
ATOM   66   C  CD1 . ILE A 1 6   ? -3.061  26.010 79.697  1.00 24.34 ? 6    ILE A CD1 1 
ATOM   67   N  N   . VAL A 1 7   ? -3.849  27.288 84.461  1.00 14.78 ? 7    VAL A N   1 
ATOM   68   C  CA  . VAL A 1 7   ? -3.959  27.849 85.814  1.00 13.29 ? 7    VAL A CA  1 
ATOM   69   C  C   . VAL A 1 7   ? -2.524  28.161 86.272  1.00 16.20 ? 7    VAL A C   1 
ATOM   70   O  O   . VAL A 1 7   ? -1.555  27.560 85.783  1.00 15.76 ? 7    VAL A O   1 
ATOM   71   C  CB  . VAL A 1 7   ? -4.638  26.815 86.765  1.00 11.95 ? 7    VAL A CB  1 
ATOM   72   C  CG1 . VAL A 1 7   ? -4.442  27.144 88.260  1.00 22.15 ? 7    VAL A CG1 1 
ATOM   73   C  CG2 . VAL A 1 7   ? -6.114  26.616 86.398  1.00 14.19 ? 7    VAL A CG2 1 
ATOM   74   N  N   . THR A 1 8   ? -2.380  29.096 87.205  1.00 14.49 ? 8    THR A N   1 
ATOM   75   C  CA  . THR A 1 8   ? -1.068  29.331 87.803  1.00 12.80 ? 8    THR A CA  1 
ATOM   76   C  C   . THR A 1 8   ? -1.012  28.724 89.207  1.00 11.23 ? 8    THR A C   1 
ATOM   77   O  O   . THR A 1 8   ? -2.033  28.605 89.892  1.00 12.00 ? 8    THR A O   1 
ATOM   78   C  CB  . THR A 1 8   ? -0.701  30.845 87.915  1.00 13.98 ? 8    THR A CB  1 
ATOM   79   O  OG1 . THR A 1 8   ? -1.588  31.499 88.817  1.00 12.92 ? 8    THR A OG1 1 
ATOM   80   C  CG2 . THR A 1 8   ? -0.757  31.552 86.542  1.00 16.19 ? 8    THR A CG2 1 
ATOM   81   N  N   . MET A 1 9   ? 0.189   28.332 89.599  1.00 13.03 ? 9    MET A N   1 
ATOM   82   C  CA  . MET A 1 9   ? 0.443   27.762 90.919  1.00 14.25 ? 9    MET A CA  1 
ATOM   83   C  C   . MET A 1 9   ? 1.706   28.447 91.445  1.00 13.55 ? 9    MET A C   1 
ATOM   84   O  O   . MET A 1 9   ? 2.768   28.459 90.774  1.00 15.43 ? 9    MET A O   1 
ATOM   85   C  CB  . MET A 1 9   ? 0.691   26.260 90.771  1.00 15.09 ? 9    MET A CB  1 
ATOM   86   C  CG  . MET A 1 9   ? 1.348   25.589 91.962  1.00 22.67 ? 9    MET A CG  1 
ATOM   87   S  SD  . MET A 1 9   ? 1.778   23.895 91.507  1.00 27.42 ? 9    MET A SD  1 
ATOM   88   C  CE  . MET A 1 9   ? 2.662   23.411 92.988  1.00 24.33 ? 9    MET A CE  1 
ATOM   89   N  N   . GLU A 1 10  ? 1.590   29.021 92.640  1.00 14.26 ? 10   GLU A N   1 
ATOM   90   C  CA  . GLU A 1 10  ? 2.682   29.810 93.193  1.00 11.54 ? 10   GLU A CA  1 
ATOM   91   C  C   . GLU A 1 10  ? 2.970   29.325 94.595  1.00 15.21 ? 10   GLU A C   1 
ATOM   92   O  O   . GLU A 1 10  ? 2.057   29.085 95.370  1.00 15.51 ? 10   GLU A O   1 
ATOM   93   C  CB  . GLU A 1 10  ? 2.317   31.295 93.200  1.00 15.28 ? 10   GLU A CB  1 
ATOM   94   C  CG  . GLU A 1 10  ? 3.421   32.206 93.742  1.00 14.85 ? 10   GLU A CG  1 
ATOM   95   C  CD  . GLU A 1 10  ? 3.064   33.673 93.574  1.00 20.16 ? 10   GLU A CD  1 
ATOM   96   O  OE1 . GLU A 1 10  ? 1.958   34.097 93.997  1.00 17.17 ? 10   GLU A OE1 1 
ATOM   97   O  OE2 . GLU A 1 10  ? 3.876   34.410 92.997  1.00 17.59 ? 10   GLU A OE2 1 
ATOM   98   N  N   . ARG A 1 11  ? 4.255   29.194 94.910  1.00 13.74 ? 11   ARG A N   1 
ATOM   99   C  CA  . ARG A 1 11  ? 4.681   28.666 96.192  1.00 13.24 ? 11   ARG A CA  1 
ATOM   100  C  C   . ARG A 1 11  ? 5.646   29.684 96.820  1.00 12.78 ? 11   ARG A C   1 
ATOM   101  O  O   . ARG A 1 11  ? 6.538   30.207 96.143  1.00 17.81 ? 11   ARG A O   1 
ATOM   102  C  CB  . ARG A 1 11  ? 5.368   27.319 95.976  1.00 17.31 ? 11   ARG A CB  1 
ATOM   103  C  CG  . ARG A 1 11  ? 6.138   26.801 97.185  1.00 21.52 ? 11   ARG A CG  1 
ATOM   104  C  CD  . ARG A 1 11  ? 5.192   26.485 98.310  1.00 26.30 ? 11   ARG A CD  1 
ATOM   105  N  NE  . ARG A 1 11  ? 5.904   25.906 99.449  1.00 33.68 ? 11   ARG A NE  1 
ATOM   106  C  CZ  . ARG A 1 11  ? 5.310   25.263 100.445 1.00 43.99 ? 11   ARG A CZ  1 
ATOM   107  N  NH1 . ARG A 1 11  ? 3.994   25.112 100.436 1.00 29.90 ? 11   ARG A NH1 1 
ATOM   108  N  NH2 . ARG A 1 11  ? 6.031   24.768 101.444 1.00 32.87 ? 11   ARG A NH2 1 
ATOM   109  N  N   . VAL A 1 12  ? 5.426   29.983 98.095  1.00 12.60 ? 12   VAL A N   1 
ATOM   110  C  CA  . VAL A 1 12  ? 6.137   31.079 98.785  1.00 14.22 ? 12   VAL A CA  1 
ATOM   111  C  C   . VAL A 1 12  ? 7.054   30.452 99.831  1.00 17.86 ? 12   VAL A C   1 
ATOM   112  O  O   . VAL A 1 12  ? 6.632   29.587 100.600 1.00 17.82 ? 12   VAL A O   1 
ATOM   113  C  CB  . VAL A 1 12  ? 5.150   32.041 99.513  1.00 13.83 ? 12   VAL A CB  1 
ATOM   114  C  CG1 . VAL A 1 12  ? 5.920   33.191 100.227 1.00 12.72 ? 12   VAL A CG1 1 
ATOM   115  C  CG2 . VAL A 1 12  ? 4.078   32.617 98.526  1.00 15.26 ? 12   VAL A CG2 1 
ATOM   116  N  N   . ASP A 1 13  ? 8.313   30.871 99.852  1.00 15.42 ? 13   ASP A N   1 
ATOM   117  C  CA  . ASP A 1 13  ? 9.232   30.435 100.912 1.00 16.31 ? 13   ASP A CA  1 
ATOM   118  C  C   . ASP A 1 13  ? 10.107  31.659 101.217 1.00 20.89 ? 13   ASP A C   1 
ATOM   119  O  O   . ASP A 1 13  ? 9.803   32.754 100.755 1.00 16.11 ? 13   ASP A O   1 
ATOM   120  C  CB  . ASP A 1 13  ? 10.058  29.247 100.426 1.00 12.34 ? 13   ASP A CB  1 
ATOM   121  C  CG  . ASP A 1 13  ? 10.528  28.341 101.553 1.00 33.92 ? 13   ASP A CG  1 
ATOM   122  O  OD1 . ASP A 1 13  ? 10.875  28.841 102.645 1.00 29.62 ? 13   ASP A OD1 1 
ATOM   123  O  OD2 . ASP A 1 13  ? 10.563  27.114 101.338 1.00 29.29 ? 13   ASP A OD2 1 
ATOM   124  N  N   . SER A 1 14  ? 11.149  31.491 102.028 1.00 15.13 ? 14   SER A N   1 
ATOM   125  C  CA  A SER A 1 14  ? 11.987  32.628 102.421 0.50 12.64 ? 14   SER A CA  1 
ATOM   126  C  CA  B SER A 1 14  ? 11.980  32.627 102.445 0.50 13.77 ? 14   SER A CA  1 
ATOM   127  C  C   . SER A 1 14  ? 13.402  32.152 102.719 1.00 16.74 ? 14   SER A C   1 
ATOM   128  O  O   . SER A 1 14  ? 13.632  30.960 102.941 1.00 20.52 ? 14   SER A O   1 
ATOM   129  C  CB  A SER A 1 14  ? 11.419  33.282 103.670 0.50 16.62 ? 14   SER A CB  1 
ATOM   130  C  CB  B SER A 1 14  ? 11.409  33.279 103.707 0.50 13.35 ? 14   SER A CB  1 
ATOM   131  O  OG  A SER A 1 14  ? 11.366  32.338 104.720 0.50 14.03 ? 14   SER A OG  1 
ATOM   132  O  OG  B SER A 1 14  ? 10.291  34.100 103.410 0.50 32.69 ? 14   SER A OG  1 
ATOM   133  N  N   . PHE A 1 15  ? 14.343  33.093 102.729 1.00 13.07 ? 15   PHE A N   1 
ATOM   134  C  CA  . PHE A 1 15  ? 15.720  32.810 103.159 1.00 13.61 ? 15   PHE A CA  1 
ATOM   135  C  C   . PHE A 1 15  ? 16.340  34.043 103.817 1.00 15.74 ? 15   PHE A C   1 
ATOM   136  O  O   . PHE A 1 15  ? 15.987  35.172 103.504 1.00 17.46 ? 15   PHE A O   1 
ATOM   137  C  CB  . PHE A 1 15  ? 16.588  32.268 102.006 1.00 12.88 ? 15   PHE A CB  1 
ATOM   138  C  CG  . PHE A 1 15  ? 16.773  33.235 100.834 1.00 15.61 ? 15   PHE A CG  1 
ATOM   139  C  CD1 . PHE A 1 15  ? 17.908  34.037 100.747 1.00 17.20 ? 15   PHE A CD1 1 
ATOM   140  C  CD2 . PHE A 1 15  ? 15.826  33.298 99.799  1.00 14.56 ? 15   PHE A CD2 1 
ATOM   141  C  CE1 . PHE A 1 15  ? 18.088  34.920 99.670  1.00 16.26 ? 15   PHE A CE1 1 
ATOM   142  C  CE2 . PHE A 1 15  ? 15.983  34.173 98.716  1.00 16.92 ? 15   PHE A CE2 1 
ATOM   143  C  CZ  . PHE A 1 15  ? 17.126  34.987 98.644  1.00 15.30 ? 15   PHE A CZ  1 
ATOM   144  N  N   . SER A 1 16  ? 17.245  33.817 104.755 1.00 13.00 ? 16   SER A N   1 
ATOM   145  C  CA  A SER A 1 16  ? 17.891  34.925 105.432 0.50 12.21 ? 16   SER A CA  1 
ATOM   146  C  CA  B SER A 1 16  ? 17.913  34.904 105.468 0.50 13.43 ? 16   SER A CA  1 
ATOM   147  C  C   . SER A 1 16  ? 19.325  35.027 104.918 1.00 14.14 ? 16   SER A C   1 
ATOM   148  O  O   . SER A 1 16  ? 20.031  34.025 104.804 1.00 19.88 ? 16   SER A O   1 
ATOM   149  C  CB  A SER A 1 16  ? 17.819  34.729 106.949 0.50 16.00 ? 16   SER A CB  1 
ATOM   150  C  CB  B SER A 1 16  ? 17.984  34.579 106.962 0.50 14.34 ? 16   SER A CB  1 
ATOM   151  O  OG  A SER A 1 16  ? 16.471  34.784 107.398 0.50 15.60 ? 16   SER A OG  1 
ATOM   152  O  OG  B SER A 1 16  ? 19.252  34.953 107.482 0.50 18.35 ? 16   SER A OG  1 
ATOM   153  N  N   . ALA A 1 17  ? 19.739  36.232 104.534 1.00 14.35 ? 17   ALA A N   1 
ATOM   154  C  CA  . ALA A 1 17  ? 21.087  36.362 103.993 1.00 13.10 ? 17   ALA A CA  1 
ATOM   155  C  C   . ALA A 1 17  ? 21.652  37.742 104.272 1.00 13.55 ? 17   ALA A C   1 
ATOM   156  O  O   . ALA A 1 17  ? 20.908  38.726 104.421 1.00 13.15 ? 17   ALA A O   1 
ATOM   157  C  CB  . ALA A 1 17  ? 21.113  36.068 102.476 1.00 13.94 ? 17   ALA A CB  1 
ATOM   158  N  N   . ALA A 1 18  ? 22.978  37.806 104.327 1.00 12.28 ? 18   ALA A N   1 
ATOM   159  C  CA  . ALA A 1 18  ? 23.682  39.074 104.378 1.00 12.58 ? 18   ALA A CA  1 
ATOM   160  C  C   . ALA A 1 18  ? 24.115  39.476 102.968 1.00 14.23 ? 18   ALA A C   1 
ATOM   161  O  O   . ALA A 1 18  ? 24.362  38.623 102.109 1.00 15.39 ? 18   ALA A O   1 
ATOM   162  C  CB  . ALA A 1 18  ? 24.935  38.939 105.296 1.00 13.48 ? 18   ALA A CB  1 
ATOM   163  N  N   . HIS A 1 19  ? 24.259  40.769 102.747 1.00 13.58 ? 19   HIS A N   1 
ATOM   164  C  CA  . HIS A 1 19  ? 24.933  41.243 101.539 1.00 12.00 ? 19   HIS A CA  1 
ATOM   165  C  C   . HIS A 1 19  ? 25.453  42.661 101.705 1.00 16.95 ? 19   HIS A C   1 
ATOM   166  O  O   . HIS A 1 19  ? 25.180  43.327 102.716 1.00 14.84 ? 19   HIS A O   1 
ATOM   167  C  CB  . HIS A 1 19  ? 24.014  41.078 100.298 1.00 14.66 ? 19   HIS A CB  1 
ATOM   168  C  CG  . HIS A 1 19  ? 22.983  42.156 100.128 1.00 12.95 ? 19   HIS A CG  1 
ATOM   169  N  ND1 . HIS A 1 19  ? 22.610  42.626 98.883  1.00 10.68 ? 19   HIS A ND1 1 
ATOM   170  C  CD2 . HIS A 1 19  ? 22.207  42.818 101.024 1.00 14.00 ? 19   HIS A CD2 1 
ATOM   171  C  CE1 . HIS A 1 19  ? 21.675  43.552 99.016  1.00 16.11 ? 19   HIS A CE1 1 
ATOM   172  N  NE2 . HIS A 1 19  ? 21.399  43.675 100.307 1.00 16.81 ? 19   HIS A NE2 1 
ATOM   173  N  N   . ARG A 1 20  ? 26.250  43.090 100.733 1.00 13.43 ? 20   ARG A N   1 
ATOM   174  C  CA  . ARG A 1 20  ? 26.661  44.485 100.619 1.00 12.66 ? 20   ARG A CA  1 
ATOM   175  C  C   . ARG A 1 20  ? 26.612  44.829 99.131  1.00 20.40 ? 20   ARG A C   1 
ATOM   176  O  O   . ARG A 1 20  ? 27.098  44.054 98.291  1.00 16.30 ? 20   ARG A O   1 
ATOM   177  C  CB  . ARG A 1 20  ? 28.084  44.643 101.158 1.00 14.45 ? 20   ARG A CB  1 
ATOM   178  C  CG  . ARG A 1 20  ? 28.660  46.032 100.874 1.00 14.44 ? 20   ARG A CG  1 
ATOM   179  C  CD  . ARG A 1 20  ? 30.167  46.053 101.121 1.00 18.59 ? 20   ARG A CD  1 
ATOM   180  N  NE  . ARG A 1 20  ? 30.641  47.432 101.096 1.00 21.02 ? 20   ARG A NE  1 
ATOM   181  C  CZ  . ARG A 1 20  ? 31.855  47.810 100.706 1.00 23.59 ? 20   ARG A CZ  1 
ATOM   182  N  NH1 . ARG A 1 20  ? 32.731  46.917 100.253 1.00 21.68 ? 20   ARG A NH1 1 
ATOM   183  N  NH2 . ARG A 1 20  ? 32.180  49.098 100.756 1.00 18.46 ? 20   ARG A NH2 1 
ATOM   184  N  N   . LEU A 1 21  ? 26.001  45.962 98.790  1.00 12.85 ? 21   LEU A N   1 
ATOM   185  C  CA  . LEU A 1 21  ? 25.945  46.383 97.393  1.00 14.96 ? 21   LEU A CA  1 
ATOM   186  C  C   . LEU A 1 21  ? 27.243  47.129 97.077  1.00 18.04 ? 21   LEU A C   1 
ATOM   187  O  O   . LEU A 1 21  ? 27.523  48.190 97.654  1.00 17.45 ? 21   LEU A O   1 
ATOM   188  C  CB  . LEU A 1 21  ? 24.718  47.264 97.143  1.00 22.28 ? 21   LEU A CB  1 
ATOM   189  C  CG  . LEU A 1 21  ? 23.391  46.509 97.332  1.00 14.88 ? 21   LEU A CG  1 
ATOM   190  C  CD1 . LEU A 1 21  ? 22.252  47.450 96.961  1.00 17.11 ? 21   LEU A CD1 1 
ATOM   191  C  CD2 . LEU A 1 21  ? 23.395  45.245 96.427  1.00 15.34 ? 21   LEU A CD2 1 
ATOM   192  N  N   . HIS A 1 22  ? 28.064  46.526 96.216  1.00 16.54 ? 22   HIS A N   1 
ATOM   193  C  CA  . HIS A 1 22  ? 29.371  47.098 95.875  1.00 13.18 ? 22   HIS A CA  1 
ATOM   194  C  C   . HIS A 1 22  ? 29.724  46.548 94.494  1.00 14.33 ? 22   HIS A C   1 
ATOM   195  O  O   . HIS A 1 22  ? 29.838  45.330 94.323  1.00 17.93 ? 22   HIS A O   1 
ATOM   196  C  CB  . HIS A 1 22  ? 30.438  46.702 96.913  1.00 17.06 ? 22   HIS A CB  1 
ATOM   197  C  CG  . HIS A 1 22  ? 31.718  47.479 96.794  1.00 23.07 ? 22   HIS A CG  1 
ATOM   198  N  ND1 . HIS A 1 22  ? 32.810  47.021 96.085  1.00 32.56 ? 22   HIS A ND1 1 
ATOM   199  C  CD2 . HIS A 1 22  ? 32.070  48.694 97.280  1.00 14.39 ? 22   HIS A CD2 1 
ATOM   200  C  CE1 . HIS A 1 22  ? 33.782  47.918 96.145  1.00 18.56 ? 22   HIS A CE1 1 
ATOM   201  N  NE2 . HIS A 1 22  ? 33.361  48.938 96.873  1.00 28.05 ? 22   HIS A NE2 1 
ATOM   202  N  N   . SER A 1 23  ? 29.882  47.442 93.514  1.00 18.40 ? 23   SER A N   1 
ATOM   203  C  CA  . SER A 1 23  ? 30.268  47.022 92.164  1.00 16.02 ? 23   SER A CA  1 
ATOM   204  C  C   . SER A 1 23  ? 31.783  47.097 91.971  1.00 24.41 ? 23   SER A C   1 
ATOM   205  O  O   . SER A 1 23  ? 32.402  48.118 92.259  1.00 20.55 ? 23   SER A O   1 
ATOM   206  C  CB  . SER A 1 23  ? 29.608  47.893 91.096  1.00 15.71 ? 23   SER A CB  1 
ATOM   207  O  OG  . SER A 1 23  ? 30.161  47.580 89.811  1.00 17.09 ? 23   SER A OG  1 
ATOM   208  N  N   . GLU A 1 24  ? 32.377  46.033 91.445  1.00 19.19 ? 24   GLU A N   1 
ATOM   209  C  CA  . GLU A 1 24  ? 33.792  46.101 91.066  1.00 24.40 ? 24   GLU A CA  1 
ATOM   210  C  C   . GLU A 1 24  ? 34.081  47.052 89.883  1.00 26.80 ? 24   GLU A C   1 
ATOM   211  O  O   . GLU A 1 24  ? 35.236  47.378 89.623  1.00 28.53 ? 24   GLU A O   1 
ATOM   212  C  CB  . GLU A 1 24  ? 34.337  44.691 90.801  1.00 26.34 ? 24   GLU A CB  1 
ATOM   213  C  CG  . GLU A 1 24  ? 34.430  43.854 92.063  1.00 24.90 ? 24   GLU A CG  1 
ATOM   214  C  CD  . GLU A 1 24  ? 35.251  44.538 93.133  1.00 49.02 ? 24   GLU A CD  1 
ATOM   215  O  OE1 . GLU A 1 24  ? 36.302  45.115 92.786  1.00 40.82 ? 24   GLU A OE1 1 
ATOM   216  O  OE2 . GLU A 1 24  ? 34.846  44.509 94.314  1.00 26.17 ? 24   GLU A OE2 1 
ATOM   217  N  N   . LYS A 1 25  ? 33.039  47.500 89.180  1.00 20.25 ? 25   LYS A N   1 
ATOM   218  C  CA  . LYS A 1 25  ? 33.200  48.440 88.058  1.00 24.15 ? 25   LYS A CA  1 
ATOM   219  C  C   . LYS A 1 25  ? 33.052  49.921 88.480  1.00 36.60 ? 25   LYS A C   1 
ATOM   220  O  O   . LYS A 1 25  ? 33.067  50.827 87.631  1.00 27.84 ? 25   LYS A O   1 
ATOM   221  C  CB  . LYS A 1 25  ? 32.213  48.118 86.925  1.00 28.80 ? 25   LYS A CB  1 
ATOM   222  C  CG  . LYS A 1 25  ? 32.213  46.654 86.482  1.00 51.78 ? 25   LYS A CG  1 
ATOM   223  C  CD  . LYS A 1 25  ? 32.947  46.445 85.173  1.00 34.77 ? 25   LYS A CD  1 
ATOM   224  C  CE  . LYS A 1 25  ? 33.025  44.961 84.799  1.00 25.97 ? 25   LYS A CE  1 
ATOM   225  N  NZ  . LYS A 1 25  ? 32.007  44.573 83.773  1.00 27.29 ? 25   LYS A NZ  1 
ATOM   226  N  N   . LEU A 1 26  ? 32.888  50.151 89.784  1.00 22.63 ? 26   LEU A N   1 
ATOM   227  C  CA  . LEU A 1 26  ? 32.781  51.494 90.339  1.00 20.72 ? 26   LEU A CA  1 
ATOM   228  C  C   . LEU A 1 26  ? 33.919  51.759 91.328  1.00 22.99 ? 26   LEU A C   1 
ATOM   229  O  O   . LEU A 1 26  ? 34.407  50.846 92.002  1.00 20.64 ? 26   LEU A O   1 
ATOM   230  C  CB  . LEU A 1 26  ? 31.418  51.698 91.041  1.00 20.13 ? 26   LEU A CB  1 
ATOM   231  C  CG  . LEU A 1 26  ? 30.158  51.700 90.162  1.00 23.42 ? 26   LEU A CG  1 
ATOM   232  C  CD1 . LEU A 1 26  ? 28.865  51.799 90.994  1.00 19.23 ? 26   LEU A CD1 1 
ATOM   233  C  CD2 . LEU A 1 26  ? 30.245  52.843 89.148  1.00 29.11 ? 26   LEU A CD2 1 
ATOM   234  N  N   . SER A 1 27  ? 34.318  53.026 91.437  1.00 24.42 ? 27   SER A N   1 
ATOM   235  C  CA  . SER A 1 27  ? 35.266  53.434 92.469  1.00 23.97 ? 27   SER A CA  1 
ATOM   236  C  C   . SER A 1 27  ? 34.625  53.385 93.846  1.00 24.97 ? 27   SER A C   1 
ATOM   237  O  O   . SER A 1 27  ? 33.399  53.265 93.967  1.00 19.48 ? 27   SER A O   1 
ATOM   238  C  CB  . SER A 1 27  ? 35.774  54.858 92.195  1.00 24.98 ? 27   SER A CB  1 
ATOM   239  O  OG  . SER A 1 27  ? 34.770  55.833 92.460  1.00 22.06 ? 27   SER A OG  1 
ATOM   240  N  N   . ASP A 1 28  ? 35.439  53.496 94.887  1.00 18.82 ? 28   ASP A N   1 
ATOM   241  C  CA  . ASP A 1 28  ? 34.876  53.548 96.244  1.00 25.93 ? 28   ASP A CA  1 
ATOM   242  C  C   . ASP A 1 28  ? 33.842  54.662 96.414  1.00 18.78 ? 28   ASP A C   1 
ATOM   243  O  O   . ASP A 1 28  ? 32.763  54.441 96.985  1.00 18.15 ? 28   ASP A O   1 
ATOM   244  C  CB  . ASP A 1 28  ? 35.970  53.698 97.296  1.00 21.62 ? 28   ASP A CB  1 
ATOM   245  C  CG  . ASP A 1 28  ? 36.825  52.445 97.432  1.00 23.81 ? 28   ASP A CG  1 
ATOM   246  O  OD1 . ASP A 1 28  ? 36.456  51.389 96.869  1.00 25.16 ? 28   ASP A OD1 1 
ATOM   247  O  OD2 . ASP A 1 28  ? 37.851  52.520 98.120  1.00 33.50 ? 28   ASP A OD2 1 
ATOM   248  N  N   . ALA A 1 29  ? 34.193  55.862 95.951  1.00 19.73 ? 29   ALA A N   1 
ATOM   249  C  CA  . ALA A 1 29  ? 33.290  57.013 96.015  1.00 17.01 ? 29   ALA A CA  1 
ATOM   250  C  C   . ALA A 1 29  ? 32.012  56.796 95.213  1.00 22.00 ? 29   ALA A C   1 
ATOM   251  O  O   . ALA A 1 29  ? 30.924  57.108 95.680  1.00 22.02 ? 29   ALA A O   1 
ATOM   252  C  CB  . ALA A 1 29  ? 34.006  58.288 95.548  1.00 20.39 ? 29   ALA A CB  1 
ATOM   253  N  N   . GLU A 1 30  ? 32.149  56.263 94.002  1.00 19.00 ? 30   GLU A N   1 
ATOM   254  C  CA  . GLU A 1 30  ? 30.990  55.973 93.152  1.00 22.49 ? 30   GLU A CA  1 
ATOM   255  C  C   . GLU A 1 30  ? 30.058  54.939 93.803  1.00 21.42 ? 30   GLU A C   1 
ATOM   256  O  O   . GLU A 1 30  ? 28.824  55.072 93.775  1.00 19.77 ? 30   GLU A O   1 
ATOM   257  C  CB  . GLU A 1 30  ? 31.481  55.474 91.791  1.00 17.68 ? 30   GLU A CB  1 
ATOM   258  C  CG  . GLU A 1 30  ? 31.986  56.606 90.898  1.00 23.36 ? 30   GLU A CG  1 
ATOM   259  C  CD  . GLU A 1 30  ? 32.793  56.138 89.694  1.00 37.31 ? 30   GLU A CD  1 
ATOM   260  O  OE1 . GLU A 1 30  ? 33.180  54.942 89.612  1.00 25.85 ? 30   GLU A OE1 1 
ATOM   261  O  OE2 . GLU A 1 30  ? 33.050  56.990 88.821  1.00 37.39 ? 30   GLU A OE2 1 
ATOM   262  N  N   . ASN A 1 31  ? 30.657  53.921 94.406  1.00 17.31 ? 31   ASN A N   1 
ATOM   263  C  CA  . ASN A 1 31  ? 29.875  52.893 95.124  1.00 15.44 ? 31   ASN A CA  1 
ATOM   264  C  C   . ASN A 1 31  ? 29.112  53.473 96.296  1.00 19.93 ? 31   ASN A C   1 
ATOM   265  O  O   . ASN A 1 31  ? 27.954  53.163 96.517  1.00 16.32 ? 31   ASN A O   1 
ATOM   266  C  CB  . ASN A 1 31  ? 30.795  51.794 95.641  1.00 13.59 ? 31   ASN A CB  1 
ATOM   267  C  CG  . ASN A 1 31  ? 30.961  50.688 94.649  1.00 23.45 ? 31   ASN A CG  1 
ATOM   268  O  OD1 . ASN A 1 31  ? 29.972  50.089 94.231  1.00 16.38 ? 31   ASN A OD1 1 
ATOM   269  N  ND2 . ASN A 1 31  ? 32.210  50.407 94.253  1.00 15.72 ? 31   ASN A ND2 1 
ATOM   270  N  N   . LYS A 1 32  ? 29.773  54.338 97.052  1.00 19.95 ? 32   LYS A N   1 
ATOM   271  C  CA  . LYS A 1 32  ? 29.090  55.043 98.131  1.00 18.63 ? 32   LYS A CA  1 
ATOM   272  C  C   . LYS A 1 32  ? 27.938  55.893 97.597  1.00 15.62 ? 32   LYS A C   1 
ATOM   273  O  O   . LYS A 1 32  ? 26.833  55.893 98.162  1.00 23.06 ? 32   LYS A O   1 
ATOM   274  C  CB  . LYS A 1 32  ? 30.105  55.887 98.922  1.00 24.08 ? 32   LYS A CB  1 
ATOM   275  C  CG  . LYS A 1 32  ? 29.531  56.659 100.129 1.00 33.85 ? 32   LYS A CG  1 
ATOM   276  C  CD  . LYS A 1 32  ? 28.591  55.840 101.005 1.00 40.40 ? 32   LYS A CD  1 
ATOM   277  C  CE  . LYS A 1 32  ? 27.978  56.707 102.112 1.00 68.15 ? 32   LYS A CE  1 
ATOM   278  N  NZ  . LYS A 1 32  ? 26.619  56.251 102.556 1.00 54.87 ? 32   LYS A NZ  1 
ATOM   279  N  N   . GLU A 1 33  ? 28.186  56.598 96.501  1.00 18.96 ? 33   GLU A N   1 
ATOM   280  C  CA  A GLU A 1 33  ? 27.172  57.465 95.921  0.50 24.22 ? 33   GLU A CA  1 
ATOM   281  C  CA  B GLU A 1 33  ? 27.183  57.479 95.884  0.50 23.11 ? 33   GLU A CA  1 
ATOM   282  C  C   . GLU A 1 33  ? 25.999  56.692 95.309  1.00 25.85 ? 33   GLU A C   1 
ATOM   283  O  O   . GLU A 1 33  ? 24.841  57.075 95.477  1.00 22.35 ? 33   GLU A O   1 
ATOM   284  C  CB  A GLU A 1 33  ? 27.822  58.394 94.908  0.50 20.76 ? 33   GLU A CB  1 
ATOM   285  C  CB  B GLU A 1 33  ? 27.828  58.316 94.777  0.50 21.67 ? 33   GLU A CB  1 
ATOM   286  C  CG  A GLU A 1 33  ? 28.651  59.459 95.583  0.50 18.10 ? 33   GLU A CG  1 
ATOM   287  C  CG  B GLU A 1 33  ? 26.831  59.045 93.864  0.50 19.07 ? 33   GLU A CG  1 
ATOM   288  C  CD  A GLU A 1 33  ? 29.883  59.856 94.806  0.50 22.74 ? 33   GLU A CD  1 
ATOM   289  C  CD  B GLU A 1 33  ? 26.796  60.538 94.107  0.50 17.54 ? 33   GLU A CD  1 
ATOM   290  O  OE1 A GLU A 1 33  ? 30.121  59.339 93.693  0.50 35.75 ? 33   GLU A OE1 1 
ATOM   291  O  OE1 B GLU A 1 33  ? 27.717  61.058 94.757  0.50 27.39 ? 33   GLU A OE1 1 
ATOM   292  O  OE2 A GLU A 1 33  ? 30.626  60.695 95.328  0.50 8.19  ? 33   GLU A OE2 1 
ATOM   293  O  OE2 B GLU A 1 33  ? 25.853  61.191 93.632  0.50 21.33 ? 33   GLU A OE2 1 
ATOM   294  N  N   . THR A 1 34  ? 26.299  55.596 94.621  1.00 17.50 ? 34   THR A N   1 
ATOM   295  C  CA  . THR A 1 34  ? 25.268  54.787 93.953  1.00 15.78 ? 34   THR A CA  1 
ATOM   296  C  C   . THR A 1 34  ? 24.438  54.030 94.973  1.00 26.09 ? 34   THR A C   1 
ATOM   297  O  O   . THR A 1 34  ? 23.211  53.975 94.869  1.00 21.08 ? 34   THR A O   1 
ATOM   298  C  CB  . THR A 1 34  ? 25.922  53.822 92.947  1.00 22.54 ? 34   THR A CB  1 
ATOM   299  O  OG1 . THR A 1 34  ? 26.633  54.594 91.964  1.00 21.67 ? 34   THR A OG1 1 
ATOM   300  C  CG2 . THR A 1 34  ? 24.882  52.923 92.239  1.00 19.42 ? 34   THR A CG2 1 
ATOM   301  N  N   . PHE A 1 35  ? 25.102  53.483 95.988  1.00 17.59 ? 35   PHE A N   1 
ATOM   302  C  CA  . PHE A 1 35  ? 24.470  52.482 96.841  1.00 19.39 ? 35   PHE A CA  1 
ATOM   303  C  C   . PHE A 1 35  ? 24.122  53.008 98.234  1.00 19.11 ? 35   PHE A C   1 
ATOM   304  O  O   . PHE A 1 35  ? 23.317  52.406 98.947  1.00 18.18 ? 35   PHE A O   1 
ATOM   305  C  CB  . PHE A 1 35  ? 25.339  51.224 96.898  1.00 15.98 ? 35   PHE A CB  1 
ATOM   306  C  CG  . PHE A 1 35  ? 25.399  50.483 95.582  1.00 14.28 ? 35   PHE A CG  1 
ATOM   307  C  CD1 . PHE A 1 35  ? 24.213  50.070 94.934  1.00 15.11 ? 35   PHE A CD1 1 
ATOM   308  C  CD2 . PHE A 1 35  ? 26.617  50.217 94.972  1.00 19.75 ? 35   PHE A CD2 1 
ATOM   309  C  CE1 . PHE A 1 35  ? 24.257  49.399 93.717  1.00 22.24 ? 35   PHE A CE1 1 
ATOM   310  C  CE2 . PHE A 1 35  ? 26.664  49.543 93.753  1.00 20.41 ? 35   PHE A CE2 1 
ATOM   311  C  CZ  . PHE A 1 35  ? 25.473  49.129 93.133  1.00 17.66 ? 35   PHE A CZ  1 
ATOM   312  N  N   . GLY A 1 36  ? 24.698  54.154 98.600  1.00 21.22 ? 36   GLY A N   1 
ATOM   313  C  CA  . GLY A 1 36  ? 24.427  54.782 99.901  1.00 18.62 ? 36   GLY A CA  1 
ATOM   314  C  C   . GLY A 1 36  ? 24.693  53.856 101.082 1.00 15.95 ? 36   GLY A C   1 
ATOM   315  O  O   . GLY A 1 36  ? 25.712  53.160 101.120 1.00 20.69 ? 36   GLY A O   1 
ATOM   316  N  N   . LYS A 1 37  ? 23.761  53.830 102.037 1.00 20.18 ? 37   LYS A N   1 
ATOM   317  C  CA  . LYS A 1 37  ? 23.906  52.961 103.212 1.00 21.08 ? 37   LYS A CA  1 
ATOM   318  C  C   . LYS A 1 37  ? 24.008  51.471 102.830 1.00 20.71 ? 37   LYS A C   1 
ATOM   319  O  O   . LYS A 1 37  ? 24.564  50.663 103.576 1.00 17.60 ? 37   LYS A O   1 
ATOM   320  C  CB  . LYS A 1 37  ? 22.743  53.164 104.182 1.00 26.07 ? 37   LYS A CB  1 
ATOM   321  C  CG  . LYS A 1 37  ? 22.869  54.424 105.033 1.00 35.88 ? 37   LYS A CG  1 
ATOM   322  C  CD  . LYS A 1 37  ? 21.752  54.481 106.083 1.00 52.04 ? 37   LYS A CD  1 
ATOM   323  C  CE  . LYS A 1 37  ? 21.864  55.724 106.961 1.00 50.27 ? 37   LYS A CE  1 
ATOM   324  N  NZ  . LYS A 1 37  ? 22.726  55.484 108.150 1.00 87.86 ? 37   LYS A NZ  1 
ATOM   325  N  N   . CYS A 1 38  ? 23.486  51.112 101.661 1.00 17.56 ? 38   CYS A N   1 
ATOM   326  C  CA  . CYS A 1 38  ? 23.619  49.727 101.200 1.00 22.96 ? 38   CYS A CA  1 
ATOM   327  C  C   . CYS A 1 38  ? 25.070  49.309 100.916 1.00 17.64 ? 38   CYS A C   1 
ATOM   328  O  O   . CYS A 1 38  ? 25.382  48.117 100.877 1.00 17.28 ? 38   CYS A O   1 
ATOM   329  C  CB  . CYS A 1 38  ? 22.734  49.460 99.994  1.00 19.69 ? 38   CYS A CB  1 
ATOM   330  S  SG  . CYS A 1 38  ? 20.963  49.550 100.377 1.00 27.97 ? 38   CYS A SG  1 
ATOM   331  N  N   . ASN A 1 39  ? 25.959  50.290 100.793 1.00 13.93 ? 39   ASN A N   1 
ATOM   332  C  CA  . ASN A 1 39  ? 27.375  50.006 100.612 1.00 17.01 ? 39   ASN A CA  1 
ATOM   333  C  C   . ASN A 1 39  ? 28.145  49.856 101.949 1.00 22.76 ? 39   ASN A C   1 
ATOM   334  O  O   . ASN A 1 39  ? 29.374  49.725 101.952 1.00 19.51 ? 39   ASN A O   1 
ATOM   335  C  CB  . ASN A 1 39  ? 27.984  51.113 99.721  1.00 19.94 ? 39   ASN A CB  1 
ATOM   336  C  CG  . ASN A 1 39  ? 29.422  50.849 99.343  1.00 20.25 ? 39   ASN A CG  1 
ATOM   337  O  OD1 . ASN A 1 39  ? 30.325  51.578 99.777  1.00 18.34 ? 39   ASN A OD1 1 
ATOM   338  N  ND2 . ASN A 1 39  ? 29.652  49.823 98.521  1.00 18.25 ? 39   ASN A ND2 1 
ATOM   339  N  N   . ASN A 1 40  ? 27.434  49.860 103.083 1.00 20.02 ? 40   ASN A N   1 
ATOM   340  C  CA  . ASN A 1 40  ? 28.100  49.747 104.403 1.00 21.94 ? 40   ASN A CA  1 
ATOM   341  C  C   . ASN A 1 40  ? 29.116  48.631 104.323 1.00 16.16 ? 40   ASN A C   1 
ATOM   342  O  O   . ASN A 1 40  ? 28.775  47.509 103.926 1.00 20.48 ? 40   ASN A O   1 
ATOM   343  C  CB  . ASN A 1 40  ? 27.093  49.383 105.531 1.00 31.91 ? 40   ASN A CB  1 
ATOM   344  C  CG  . ASN A 1 40  ? 27.780  49.131 106.898 1.00 41.09 ? 40   ASN A CG  1 
ATOM   345  O  OD1 . ASN A 1 40  ? 28.400  50.036 107.442 1.00 29.99 ? 40   ASN A OD1 1 
ATOM   346  N  ND2 . ASN A 1 40  ? 27.649  47.905 107.458 1.00 17.76 ? 40   ASN A ND2 1 
ATOM   347  N  N   . SER A 1 41  ? 30.354  48.916 104.719 1.00 22.97 ? 41   SER A N   1 
ATOM   348  C  CA  . SER A 1 41  ? 31.443  47.988 104.443 1.00 19.53 ? 41   SER A CA  1 
ATOM   349  C  C   . SER A 1 41  ? 31.276  46.617 105.072 1.00 17.24 ? 41   SER A C   1 
ATOM   350  O  O   . SER A 1 41  ? 31.699  45.617 104.487 1.00 21.65 ? 41   SER A O   1 
ATOM   351  C  CB  . SER A 1 41  ? 32.812  48.603 104.774 1.00 32.38 ? 41   SER A CB  1 
ATOM   352  O  OG  . SER A 1 41  ? 33.089  48.525 106.154 1.00 39.86 ? 41   SER A OG  1 
ATOM   353  N  N   . ASN A 1 42  ? 30.662  46.545 106.257 1.00 16.70 ? 42   ASN A N   1 
ATOM   354  C  CA  . ASN A 1 42  ? 30.443  45.236 106.859 1.00 14.47 ? 42   ASN A CA  1 
ATOM   355  C  C   . ASN A 1 42  ? 29.093  44.604 106.493 1.00 17.07 ? 42   ASN A C   1 
ATOM   356  O  O   . ASN A 1 42  ? 28.729  43.549 107.024 1.00 16.35 ? 42   ASN A O   1 
ATOM   357  C  CB  . ASN A 1 42  ? 30.645  45.265 108.377 1.00 15.14 ? 42   ASN A CB  1 
ATOM   358  C  CG  . ASN A 1 42  ? 32.091  45.504 108.759 1.00 16.46 ? 42   ASN A CG  1 
ATOM   359  O  OD1 . ASN A 1 42  ? 32.985  44.898 108.188 1.00 21.41 ? 42   ASN A OD1 1 
ATOM   360  N  ND2 . ASN A 1 42  ? 32.320  46.386 109.713 1.00 17.12 ? 42   ASN A ND2 1 
ATOM   361  N  N   . GLY A 1 43  ? 28.368  45.255 105.594 1.00 19.68 ? 43   GLY A N   1 
ATOM   362  C  CA  . GLY A 1 43  ? 27.161  44.655 105.057 1.00 18.99 ? 43   GLY A CA  1 
ATOM   363  C  C   . GLY A 1 43  ? 25.929  44.898 105.927 1.00 13.19 ? 43   GLY A C   1 
ATOM   364  O  O   . GLY A 1 43  ? 25.952  45.654 106.929 1.00 15.20 ? 43   GLY A O   1 
ATOM   365  N  N   . HIS A 1 44  ? 24.838  44.278 105.504 1.00 15.29 ? 44   HIS A N   1 
ATOM   366  C  CA  . HIS A 1 44  ? 23.566  44.331 106.209 1.00 11.57 ? 44   HIS A CA  1 
ATOM   367  C  C   . HIS A 1 44  ? 22.853  43.091 105.676 1.00 13.24 ? 44   HIS A C   1 
ATOM   368  O  O   . HIS A 1 44  ? 23.508  42.204 105.097 1.00 13.82 ? 44   HIS A O   1 
ATOM   369  C  CB  . HIS A 1 44  ? 22.793  45.635 105.901 1.00 12.41 ? 44   HIS A CB  1 
ATOM   370  C  CG  . HIS A 1 44  ? 22.424  45.811 104.451 1.00 16.76 ? 44   HIS A CG  1 
ATOM   371  N  ND1 . HIS A 1 44  ? 23.342  46.173 103.484 1.00 15.76 ? 44   HIS A ND1 1 
ATOM   372  C  CD2 . HIS A 1 44  ? 21.241  45.652 103.802 1.00 17.20 ? 44   HIS A CD2 1 
ATOM   373  C  CE1 . HIS A 1 44  ? 22.742  46.228 102.305 1.00 22.38 ? 44   HIS A CE1 1 
ATOM   374  N  NE2 . HIS A 1 44  ? 21.468  45.917 102.471 1.00 22.04 ? 44   HIS A NE2 1 
ATOM   375  N  N   . GLY A 1 45  ? 21.545  42.995 105.885 1.00 12.85 ? 45   GLY A N   1 
ATOM   376  C  CA  . GLY A 1 45  ? 20.872  41.742 105.559 1.00 17.80 ? 45   GLY A CA  1 
ATOM   377  C  C   . GLY A 1 45  ? 19.371  41.847 105.444 1.00 15.47 ? 45   GLY A C   1 
ATOM   378  O  O   . GLY A 1 45  ? 18.792  42.893 105.724 1.00 13.58 ? 45   GLY A O   1 
ATOM   379  N  N   . HIS A 1 46  ? 18.746  40.757 105.009 1.00 13.22 ? 46   HIS A N   1 
ATOM   380  C  CA  . HIS A 1 46  ? 17.303  40.757 104.766 1.00 17.18 ? 46   HIS A CA  1 
ATOM   381  C  C   . HIS A 1 46  ? 16.779  39.365 105.027 1.00 14.52 ? 46   HIS A C   1 
ATOM   382  O  O   . HIS A 1 46  ? 17.508  38.384 104.852 1.00 13.67 ? 46   HIS A O   1 
ATOM   383  C  CB  . HIS A 1 46  ? 16.956  41.149 103.310 1.00 14.46 ? 46   HIS A CB  1 
ATOM   384  C  CG  . HIS A 1 46  ? 17.434  42.509 102.911 1.00 12.58 ? 46   HIS A CG  1 
ATOM   385  N  ND1 . HIS A 1 46  ? 16.881  43.665 103.412 1.00 14.91 ? 46   HIS A ND1 1 
ATOM   386  C  CD2 . HIS A 1 46  ? 18.432  42.897 102.080 1.00 11.04 ? 46   HIS A CD2 1 
ATOM   387  C  CE1 . HIS A 1 46  ? 17.513  44.710 102.902 1.00 16.38 ? 46   HIS A CE1 1 
ATOM   388  N  NE2 . HIS A 1 46  ? 18.456  44.270 102.090 1.00 13.87 ? 46   HIS A NE2 1 
ATOM   389  N  N   . ASN A 1 47  ? 15.509  39.264 105.436 1.00 13.00 ? 47   ASN A N   1 
ATOM   390  C  CA  . ASN A 1 47  ? 14.743  38.045 105.172 1.00 12.25 ? 47   ASN A CA  1 
ATOM   391  C  C   . ASN A 1 47  ? 14.112  38.221 103.803 1.00 14.40 ? 47   ASN A C   1 
ATOM   392  O  O   . ASN A 1 47  ? 13.278  39.096 103.618 1.00 17.40 ? 47   ASN A O   1 
ATOM   393  C  CB  . ASN A 1 47  ? 13.635  37.877 106.204 1.00 15.02 ? 47   ASN A CB  1 
ATOM   394  C  CG  . ASN A 1 47  ? 14.160  37.914 107.618 1.00 18.42 ? 47   ASN A CG  1 
ATOM   395  O  OD1 . ASN A 1 47  ? 15.094  37.190 107.969 1.00 14.84 ? 47   ASN A OD1 1 
ATOM   396  N  ND2 . ASN A 1 47  ? 13.545  38.752 108.443 1.00 13.70 ? 47   ASN A ND2 1 
ATOM   397  N  N   . TYR A 1 48  ? 14.565  37.438 102.831 1.00 12.24 ? 48   TYR A N   1 
ATOM   398  C  CA  . TYR A 1 48  ? 14.056  37.596 101.484 1.00 11.64 ? 48   TYR A CA  1 
ATOM   399  C  C   . TYR A 1 48  ? 12.856  36.654 101.352 1.00 16.52 ? 48   TYR A C   1 
ATOM   400  O  O   . TYR A 1 48  ? 12.961  35.482 101.694 1.00 19.55 ? 48   TYR A O   1 
ATOM   401  C  CB  . TYR A 1 48  ? 15.136  37.172 100.486 1.00 11.59 ? 48   TYR A CB  1 
ATOM   402  C  CG  . TYR A 1 48  ? 16.299  38.118 100.324 1.00 15.95 ? 48   TYR A CG  1 
ATOM   403  C  CD1 . TYR A 1 48  ? 16.256  39.146 99.380  1.00 16.02 ? 48   TYR A CD1 1 
ATOM   404  C  CD2 . TYR A 1 48  ? 17.475  37.950 101.073 1.00 11.77 ? 48   TYR A CD2 1 
ATOM   405  C  CE1 . TYR A 1 48  ? 17.347  40.016 99.193  1.00 15.16 ? 48   TYR A CE1 1 
ATOM   406  C  CE2 . TYR A 1 48  ? 18.568  38.797 100.883 1.00 13.75 ? 48   TYR A CE2 1 
ATOM   407  C  CZ  . TYR A 1 48  ? 18.495  39.830 99.960  1.00 13.43 ? 48   TYR A CZ  1 
ATOM   408  O  OH  . TYR A 1 48  ? 19.572  40.649 99.793  1.00 14.64 ? 48   TYR A OH  1 
ATOM   409  N  N   . VAL A 1 49  ? 11.726  37.161 100.872 1.00 12.17 ? 49   VAL A N   1 
ATOM   410  C  CA  . VAL A 1 49  ? 10.629  36.260 100.515 1.00 11.42 ? 49   VAL A CA  1 
ATOM   411  C  C   . VAL A 1 49  ? 10.812  35.845 99.039  1.00 13.45 ? 49   VAL A C   1 
ATOM   412  O  O   . VAL A 1 49  ? 11.004  36.699 98.167  1.00 15.39 ? 49   VAL A O   1 
ATOM   413  C  CB  . VAL A 1 49  ? 9.258   36.937 100.702 1.00 14.71 ? 49   VAL A CB  1 
ATOM   414  C  CG1 . VAL A 1 49  ? 8.146   35.988 100.294 1.00 15.69 ? 49   VAL A CG1 1 
ATOM   415  C  CG2 . VAL A 1 49  ? 9.057   37.350 102.183 1.00 13.20 ? 49   VAL A CG2 1 
ATOM   416  N  N   . TRP A 1 50  ? 10.746  34.553 98.773  1.00 11.43 ? 50   TRP A N   1 
ATOM   417  C  CA  . TRP A 1 50  ? 10.883  34.061 97.400  1.00 13.78 ? 50   TRP A CA  1 
ATOM   418  C  C   . TRP A 1 50  ? 9.549   33.449 96.958  1.00 16.45 ? 50   TRP A C   1 
ATOM   419  O  O   . TRP A 1 50  ? 9.070   32.511 97.584  1.00 14.05 ? 50   TRP A O   1 
ATOM   420  C  CB  . TRP A 1 50  ? 11.939  32.955 97.368  1.00 14.51 ? 50   TRP A CB  1 
ATOM   421  C  CG  . TRP A 1 50  ? 12.291  32.473 95.991  1.00 14.03 ? 50   TRP A CG  1 
ATOM   422  C  CD1 . TRP A 1 50  ? 12.228  33.187 94.824  1.00 13.51 ? 50   TRP A CD1 1 
ATOM   423  C  CD2 . TRP A 1 50  ? 12.795  31.172 95.645  1.00 14.49 ? 50   TRP A CD2 1 
ATOM   424  N  NE1 . TRP A 1 50  ? 12.670  32.393 93.756  1.00 12.31 ? 50   TRP A NE1 1 
ATOM   425  C  CE2 . TRP A 1 50  ? 13.033  31.165 94.240  1.00 12.19 ? 50   TRP A CE2 1 
ATOM   426  C  CE3 . TRP A 1 50  ? 13.098  30.018 96.389  1.00 14.74 ? 50   TRP A CE3 1 
ATOM   427  C  CZ2 . TRP A 1 50  ? 13.543  30.034 93.559  1.00 11.66 ? 50   TRP A CZ2 1 
ATOM   428  C  CZ3 . TRP A 1 50  ? 13.585  28.870 95.697  1.00 14.90 ? 50   TRP A CZ3 1 
ATOM   429  C  CH2 . TRP A 1 50  ? 13.813  28.906 94.303  1.00 13.53 ? 50   TRP A CH2 1 
ATOM   430  N  N   . LYS A 1 51  ? 8.936   33.959 95.894  1.00 11.18 ? 51   LYS A N   1 
ATOM   431  C  CA  . LYS A 1 51  ? 7.729   33.265 95.409  1.00 13.22 ? 51   LYS A CA  1 
ATOM   432  C  C   . LYS A 1 51  ? 8.007   32.705 94.023  1.00 15.68 ? 51   LYS A C   1 
ATOM   433  O  O   . LYS A 1 51  ? 8.534   33.399 93.175  1.00 14.46 ? 51   LYS A O   1 
ATOM   434  C  CB  . LYS A 1 51  ? 6.533   34.216 95.340  1.00 14.22 ? 51   LYS A CB  1 
ATOM   435  C  CG  . LYS A 1 51  ? 6.334   35.080 96.590  1.00 15.02 ? 51   LYS A CG  1 
ATOM   436  C  CD  . LYS A 1 51  ? 5.048   35.874 96.466  1.00 23.25 ? 51   LYS A CD  1 
ATOM   437  C  CE  . LYS A 1 51  ? 4.791   36.698 97.733  1.00 26.77 ? 51   LYS A CE  1 
ATOM   438  N  NZ  . LYS A 1 51  ? 3.558   37.546 97.567  1.00 24.11 ? 51   LYS A NZ  1 
ATOM   439  N  N   . VAL A 1 52  ? 7.623   31.459 93.812  1.00 11.44 ? 52   VAL A N   1 
ATOM   440  C  CA  . VAL A 1 52  ? 7.893   30.753 92.560  1.00 17.41 ? 52   VAL A CA  1 
ATOM   441  C  C   . VAL A 1 52  ? 6.549   30.456 91.927  1.00 12.87 ? 52   VAL A C   1 
ATOM   442  O  O   . VAL A 1 52  ? 5.738   29.723 92.503  1.00 12.95 ? 52   VAL A O   1 
ATOM   443  C  CB  . VAL A 1 52  ? 8.639   29.430 92.825  1.00 15.45 ? 52   VAL A CB  1 
ATOM   444  C  CG1 . VAL A 1 52  ? 8.662   28.541 91.557  1.00 14.61 ? 52   VAL A CG1 1 
ATOM   445  C  CG2 . VAL A 1 52  ? 10.038  29.746 93.327  1.00 13.66 ? 52   VAL A CG2 1 
ATOM   446  N  N   . LYS A 1 53  ? 6.318   31.048 90.757  1.00 12.94 ? 53   LYS A N   1 
ATOM   447  C  CA  . LYS A 1 53  ? 5.026   30.939 90.089  1.00 16.47 ? 53   LYS A CA  1 
ATOM   448  C  C   . LYS A 1 53  ? 5.156   30.124 88.795  1.00 14.94 ? 53   LYS A C   1 
ATOM   449  O  O   . LYS A 1 53  ? 6.013   30.391 87.957  1.00 12.60 ? 53   LYS A O   1 
ATOM   450  C  CB  . LYS A 1 53  ? 4.466   32.342 89.790  1.00 16.57 ? 53   LYS A CB  1 
ATOM   451  C  CG  . LYS A 1 53  ? 3.017   32.379 89.260  1.00 16.80 ? 53   LYS A CG  1 
ATOM   452  C  CD  . LYS A 1 53  ? 2.574   33.838 89.171  1.00 18.25 ? 53   LYS A CD  1 
ATOM   453  C  CE  . LYS A 1 53  ? 1.134   33.967 88.725  1.00 15.28 ? 53   LYS A CE  1 
ATOM   454  N  NZ  . LYS A 1 53  ? 0.561   35.315 89.019  1.00 22.10 ? 53   LYS A NZ  1 
ATOM   455  N  N   . LEU A 1 54  ? 4.289   29.130 88.668  1.00 16.41 ? 54   LEU A N   1 
ATOM   456  C  CA  . LEU A 1 54  ? 4.286   28.219 87.528  1.00 16.74 ? 54   LEU A CA  1 
ATOM   457  C  C   . LEU A 1 54  ? 2.985   28.466 86.779  1.00 15.60 ? 54   LEU A C   1 
ATOM   458  O  O   . LEU A 1 54  ? 1.999   28.912 87.377  1.00 15.15 ? 54   LEU A O   1 
ATOM   459  C  CB  . LEU A 1 54  ? 4.315   26.773 88.035  1.00 14.04 ? 54   LEU A CB  1 
ATOM   460  C  CG  . LEU A 1 54  ? 5.399   26.423 89.074  1.00 16.19 ? 54   LEU A CG  1 
ATOM   461  C  CD1 . LEU A 1 54  ? 5.357   24.900 89.325  1.00 20.52 ? 54   LEU A CD1 1 
ATOM   462  C  CD2 . LEU A 1 54  ? 6.790   26.841 88.592  1.00 17.37 ? 54   LEU A CD2 1 
ATOM   463  N  N   . ARG A 1 55  ? 2.971   28.202 85.477  1.00 14.27 ? 55   ARG A N   1 
ATOM   464  C  CA  . ARG A 1 55  ? 1.722   28.318 84.720  1.00 15.30 ? 55   ARG A CA  1 
ATOM   465  C  C   . ARG A 1 55  ? 1.652   27.164 83.716  1.00 15.49 ? 55   ARG A C   1 
ATOM   466  O  O   . ARG A 1 55  ? 2.643   26.855 83.037  1.00 17.98 ? 55   ARG A O   1 
ATOM   467  C  CB  . ARG A 1 55  ? 1.691   29.661 83.981  1.00 13.14 ? 55   ARG A CB  1 
ATOM   468  C  CG  . ARG A 1 55  ? 0.431   29.904 83.168  1.00 14.53 ? 55   ARG A CG  1 
ATOM   469  C  CD  . ARG A 1 55  ? 0.477   31.298 82.560  1.00 26.55 ? 55   ARG A CD  1 
ATOM   470  N  NE  . ARG A 1 55  ? -0.799  31.657 81.959  1.00 40.11 ? 55   ARG A NE  1 
ATOM   471  C  CZ  . ARG A 1 55  ? -1.121  31.414 80.692  1.00 59.94 ? 55   ARG A CZ  1 
ATOM   472  N  NH1 . ARG A 1 55  ? -0.259  30.802 79.893  1.00 40.54 ? 55   ARG A NH1 1 
ATOM   473  N  NH2 . ARG A 1 55  ? -2.310  31.776 80.226  1.00 46.37 ? 55   ARG A NH2 1 
ATOM   474  N  N   . GLY A 1 56  ? 0.502   26.519 83.618  1.00 13.85 ? 56   GLY A N   1 
ATOM   475  C  CA  . GLY A 1 56  ? 0.409   25.367 82.716  1.00 14.20 ? 56   GLY A CA  1 
ATOM   476  C  C   . GLY A 1 56  ? -0.962  24.748 82.759  1.00 14.88 ? 56   GLY A C   1 
ATOM   477  O  O   . GLY A 1 56  ? -1.817  25.153 83.559  1.00 15.23 ? 56   GLY A O   1 
ATOM   478  N  N   . GLU A 1 57  ? -1.179  23.771 81.882  1.00 12.65 ? 57   GLU A N   1 
ATOM   479  C  CA  . GLU A 1 57  ? -2.430  23.022 81.902  1.00 12.77 ? 57   GLU A CA  1 
ATOM   480  C  C   . GLU A 1 57  ? -2.612  22.227 83.187  1.00 14.95 ? 57   GLU A C   1 
ATOM   481  O  O   . GLU A 1 57  ? -1.679  21.550 83.658  1.00 15.54 ? 57   GLU A O   1 
ATOM   482  C  CB  . GLU A 1 57  ? -2.473  22.024 80.745  1.00 17.73 ? 57   GLU A CB  1 
ATOM   483  C  CG  . GLU A 1 57  ? -2.638  22.660 79.385  1.00 16.46 ? 57   GLU A CG  1 
ATOM   484  C  CD  . GLU A 1 57  ? -2.562  21.608 78.305  1.00 23.53 ? 57   GLU A CD  1 
ATOM   485  O  OE1 . GLU A 1 57  ? -3.435  20.717 78.268  1.00 23.37 ? 57   GLU A OE1 1 
ATOM   486  O  OE2 . GLU A 1 57  ? -1.617  21.666 77.504  1.00 29.17 ? 57   GLU A OE2 1 
ATOM   487  N  N   . VAL A 1 58  ? -3.840  22.235 83.700  1.00 11.79 ? 58   VAL A N   1 
ATOM   488  C  CA  A VAL A 1 58  ? -4.221  21.345 84.799  0.50 13.06 ? 58   VAL A CA  1 
ATOM   489  C  CA  B VAL A 1 58  ? -4.200  21.341 84.800  0.50 15.28 ? 58   VAL A CA  1 
ATOM   490  C  C   . VAL A 1 58  ? -4.223  19.888 84.309  1.00 18.52 ? 58   VAL A C   1 
ATOM   491  O  O   . VAL A 1 58  ? -4.804  19.574 83.278  1.00 17.39 ? 58   VAL A O   1 
ATOM   492  C  CB  A VAL A 1 58  ? -5.621  21.712 85.346  0.50 9.17  ? 58   VAL A CB  1 
ATOM   493  C  CB  B VAL A 1 58  ? -5.549  21.732 85.469  0.50 18.12 ? 58   VAL A CB  1 
ATOM   494  C  CG1 A VAL A 1 58  ? -6.030  20.782 86.490  0.50 10.36 ? 58   VAL A CG1 1 
ATOM   495  C  CG1 B VAL A 1 58  ? -5.493  23.160 86.013  0.50 18.87 ? 58   VAL A CG1 1 
ATOM   496  C  CG2 A VAL A 1 58  ? -5.681  23.189 85.772  0.50 10.92 ? 58   VAL A CG2 1 
ATOM   497  C  CG2 B VAL A 1 58  ? -6.718  21.585 84.498  0.50 23.19 ? 58   VAL A CG2 1 
ATOM   498  N  N   . ASP A 1 59  ? -3.557  18.996 85.035  1.00 14.57 ? 59   ASP A N   1 
ATOM   499  C  CA  . ASP A 1 59  ? -3.596  17.580 84.676  1.00 14.62 ? 59   ASP A CA  1 
ATOM   500  C  C   . ASP A 1 59  ? -4.985  16.993 85.005  1.00 17.05 ? 59   ASP A C   1 
ATOM   501  O  O   . ASP A 1 59  ? -5.521  17.197 86.109  1.00 16.95 ? 59   ASP A O   1 
ATOM   502  C  CB  . ASP A 1 59  ? -2.512  16.826 85.455  1.00 20.48 ? 59   ASP A CB  1 
ATOM   503  C  CG  . ASP A 1 59  ? -2.390  15.386 85.014  1.00 26.81 ? 59   ASP A CG  1 
ATOM   504  O  OD1 . ASP A 1 59  ? -1.674  15.135 84.034  1.00 21.00 ? 59   ASP A OD1 1 
ATOM   505  O  OD2 . ASP A 1 59  ? -3.037  14.518 85.622  1.00 19.36 ? 59   ASP A OD2 1 
ATOM   506  N  N   . PRO A 1 60  ? -5.573  16.244 84.059  1.00 17.77 ? 60   PRO A N   1 
ATOM   507  C  CA  . PRO A 1 60  ? -6.928  15.749 84.304  1.00 15.63 ? 60   PRO A CA  1 
ATOM   508  C  C   . PRO A 1 60  ? -6.975  14.706 85.420  1.00 21.08 ? 60   PRO A C   1 
ATOM   509  O  O   . PRO A 1 60  ? -8.010  14.554 86.047  1.00 17.80 ? 60   PRO A O   1 
ATOM   510  C  CB  . PRO A 1 60  ? -7.337  15.105 82.958  1.00 19.61 ? 60   PRO A CB  1 
ATOM   511  C  CG  . PRO A 1 60  ? -6.056  14.798 82.260  1.00 19.80 ? 60   PRO A CG  1 
ATOM   512  C  CD  . PRO A 1 60  ? -5.056  15.845 82.732  1.00 18.73 ? 60   PRO A CD  1 
ATOM   513  N  N   . THR A 1 61  ? -5.875  13.991 85.661  1.00 16.41 ? 61   THR A N   1 
ATOM   514  C  CA  . THR A 1 61  ? -5.894  12.946 86.676  1.00 14.15 ? 61   THR A CA  1 
ATOM   515  C  C   . THR A 1 61  ? -5.539  13.462 88.081  1.00 17.21 ? 61   THR A C   1 
ATOM   516  O  O   . THR A 1 61  ? -6.280  13.240 89.045  1.00 19.00 ? 61   THR A O   1 
ATOM   517  C  CB  . THR A 1 61  ? -4.990  11.761 86.273  1.00 21.39 ? 61   THR A CB  1 
ATOM   518  O  OG1 . THR A 1 61  ? -5.407  11.267 84.988  1.00 20.16 ? 61   THR A OG1 1 
ATOM   519  C  CG2 . THR A 1 61  ? -5.110  10.626 87.286  1.00 26.99 ? 61   THR A CG2 1 
ATOM   520  N  N   . SER A 1 62  ? -4.418  14.169 88.182  1.00 15.68 ? 62   SER A N   1 
ATOM   521  C  CA  . SER A 1 62  ? -3.956  14.661 89.468  1.00 15.22 ? 62   SER A CA  1 
ATOM   522  C  C   . SER A 1 62  ? -4.614  15.983 89.854  1.00 19.22 ? 62   SER A C   1 
ATOM   523  O  O   . SER A 1 62  ? -4.592  16.358 91.013  1.00 19.83 ? 62   SER A O   1 
ATOM   524  C  CB  . SER A 1 62  ? -2.434  14.845 89.471  1.00 17.57 ? 62   SER A CB  1 
ATOM   525  O  OG  . SER A 1 62  ? -2.058  15.895 88.598  1.00 16.59 ? 62   SER A OG  1 
ATOM   526  N  N   . GLY A 1 63  ? -5.167  16.701 88.876  1.00 12.54 ? 63   GLY A N   1 
ATOM   527  C  CA  . GLY A 1 63  ? -5.703  18.050 89.134  1.00 15.79 ? 63   GLY A CA  1 
ATOM   528  C  C   . GLY A 1 63  ? -4.661  19.125 89.426  1.00 13.23 ? 63   GLY A C   1 
ATOM   529  O  O   . GLY A 1 63  ? -5.006  20.204 89.909  1.00 14.03 ? 63   GLY A O   1 
ATOM   530  N  N   . MET A 1 64  ? -3.400  18.841 89.096  1.00 15.80 ? 64   MET A N   1 
ATOM   531  C  CA  A MET A 1 64  ? -2.313  19.760 89.431  0.50 11.02 ? 64   MET A CA  1 
ATOM   532  C  CA  B MET A 1 64  ? -2.261  19.708 89.439  0.50 16.64 ? 64   MET A CA  1 
ATOM   533  C  C   . MET A 1 64  ? -1.615  20.323 88.201  1.00 15.47 ? 64   MET A C   1 
ATOM   534  O  O   . MET A 1 64  ? -1.455  19.643 87.181  1.00 16.96 ? 64   MET A O   1 
ATOM   535  C  CB  A MET A 1 64  ? -1.289  19.061 90.317  0.50 25.31 ? 64   MET A CB  1 
ATOM   536  C  CB  B MET A 1 64  ? -1.181  18.881 90.137  0.50 14.95 ? 64   MET A CB  1 
ATOM   537  C  CG  A MET A 1 64  ? -1.838  18.675 91.666  0.50 10.09 ? 64   MET A CG  1 
ATOM   538  C  CG  B MET A 1 64  ? -1.666  18.099 91.331  0.50 25.59 ? 64   MET A CG  1 
ATOM   539  S  SD  A MET A 1 64  ? -0.620  17.786 92.659  0.50 46.36 ? 64   MET A SD  1 
ATOM   540  S  SD  B MET A 1 64  ? -0.333  17.074 91.969  0.50 17.56 ? 64   MET A SD  1 
ATOM   541  C  CE  A MET A 1 64  ? 0.250   16.816 91.422  0.50 17.44 ? 64   MET A CE  1 
ATOM   542  C  CE  B MET A 1 64  ? -1.138  16.269 93.349  0.50 12.77 ? 64   MET A CE  1 
ATOM   543  N  N   . VAL A 1 65  ? -1.193  21.577 88.311  1.00 17.19 ? 65   VAL A N   1 
ATOM   544  C  CA  . VAL A 1 65  ? -0.278  22.190 87.322  1.00 15.86 ? 65   VAL A CA  1 
ATOM   545  C  C   . VAL A 1 65  ? 1.140   21.579 87.420  1.00 15.90 ? 65   VAL A C   1 
ATOM   546  O  O   . VAL A 1 65  ? 1.870   21.430 86.418  1.00 16.17 ? 65   VAL A O   1 
ATOM   547  C  CB  . VAL A 1 65  ? -0.205  23.732 87.552  1.00 19.37 ? 65   VAL A CB  1 
ATOM   548  C  CG1 . VAL A 1 65  ? 0.965   24.329 86.800  1.00 19.75 ? 65   VAL A CG1 1 
ATOM   549  C  CG2 . VAL A 1 65  ? -1.518  24.414 87.139  1.00 21.55 ? 65   VAL A CG2 1 
ATOM   550  N  N   . TYR A 1 66  ? 1.515   21.201 88.634  1.00 17.82 ? 66   TYR A N   1 
ATOM   551  C  CA  . TYR A 1 66  ? 2.841   20.661 88.911  1.00 20.04 ? 66   TYR A CA  1 
ATOM   552  C  C   . TYR A 1 66  ? 2.761   19.950 90.253  1.00 19.53 ? 66   TYR A C   1 
ATOM   553  O  O   . TYR A 1 66  ? 1.961   20.308 91.119  1.00 25.35 ? 66   TYR A O   1 
ATOM   554  C  CB  . TYR A 1 66  ? 3.865   21.818 88.997  1.00 16.96 ? 66   TYR A CB  1 
ATOM   555  C  CG  . TYR A 1 66  ? 5.352   21.480 88.843  1.00 18.35 ? 66   TYR A CG  1 
ATOM   556  C  CD1 . TYR A 1 66  ? 5.944   21.381 87.586  1.00 20.33 ? 66   TYR A CD1 1 
ATOM   557  C  CD2 . TYR A 1 66  ? 6.175   21.340 89.962  1.00 21.07 ? 66   TYR A CD2 1 
ATOM   558  C  CE1 . TYR A 1 66  ? 7.324   21.123 87.441  1.00 34.68 ? 66   TYR A CE1 1 
ATOM   559  C  CE2 . TYR A 1 66  ? 7.563   21.077 89.829  1.00 19.73 ? 66   TYR A CE2 1 
ATOM   560  C  CZ  . TYR A 1 66  ? 8.124   20.969 88.572  1.00 18.71 ? 66   TYR A CZ  1 
ATOM   561  O  OH  . TYR A 1 66  ? 9.480   20.725 88.433  1.00 25.71 ? 66   TYR A OH  1 
ATOM   562  N  N   . ASP A 1 67  ? 3.626   18.961 90.439  1.00 18.55 ? 67   ASP A N   1 
ATOM   563  C  CA  . ASP A 1 67  ? 3.685   18.242 91.708  1.00 19.69 ? 67   ASP A CA  1 
ATOM   564  C  C   . ASP A 1 67  ? 4.349   19.100 92.801  1.00 24.84 ? 67   ASP A C   1 
ATOM   565  O  O   . ASP A 1 67  ? 5.537   19.404 92.706  1.00 24.04 ? 67   ASP A O   1 
ATOM   566  C  CB  . ASP A 1 67  ? 4.461   16.946 91.485  1.00 26.48 ? 67   ASP A CB  1 
ATOM   567  C  CG  . ASP A 1 67  ? 4.669   16.158 92.762  1.00 39.27 ? 67   ASP A CG  1 
ATOM   568  O  OD1 . ASP A 1 67  ? 3.689   15.923 93.484  1.00 39.33 ? 67   ASP A OD1 1 
ATOM   569  O  OD2 . ASP A 1 67  ? 5.819   15.772 93.037  1.00 53.07 ? 67   ASP A OD2 1 
ATOM   570  N  N   . LEU A 1 68  ? 3.583   19.506 93.811  1.00 22.83 ? 68   LEU A N   1 
ATOM   571  C  CA  . LEU A 1 68  ? 4.115   20.404 94.845  1.00 32.04 ? 68   LEU A CA  1 
ATOM   572  C  C   . LEU A 1 68  ? 5.266   19.764 95.614  1.00 33.02 ? 68   LEU A C   1 
ATOM   573  O  O   . LEU A 1 68  ? 6.219   20.451 95.997  1.00 25.12 ? 68   LEU A O   1 
ATOM   574  C  CB  . LEU A 1 68  ? 3.023   20.907 95.806  1.00 22.38 ? 68   LEU A CB  1 
ATOM   575  C  CG  . LEU A 1 68  ? 3.508   21.763 96.995  1.00 32.71 ? 68   LEU A CG  1 
ATOM   576  C  CD1 . LEU A 1 68  ? 4.184   23.051 96.543  1.00 36.35 ? 68   LEU A CD1 1 
ATOM   577  C  CD2 . LEU A 1 68  ? 2.409   22.078 97.996  1.00 30.75 ? 68   LEU A CD2 1 
ATOM   578  N  N   . ALA A 1 69  ? 5.188   18.451 95.829  1.00 26.93 ? 69   ALA A N   1 
ATOM   579  C  CA  . ALA A 1 69  ? 6.259   17.742 96.522  1.00 26.59 ? 69   ALA A CA  1 
ATOM   580  C  C   . ALA A 1 69  ? 7.581   17.878 95.767  1.00 29.42 ? 69   ALA A C   1 
ATOM   581  O  O   . ALA A 1 69  ? 8.632   18.123 96.374  1.00 28.46 ? 69   ALA A O   1 
ATOM   582  C  CB  . ALA A 1 69  ? 5.900   16.272 96.706  1.00 35.59 ? 69   ALA A CB  1 
ATOM   583  N  N   . LYS A 1 70  ? 7.515   17.724 94.444  1.00 22.63 ? 70   LYS A N   1 
ATOM   584  C  CA  . LYS A 1 70  ? 8.670   17.889 93.563  1.00 18.70 ? 70   LYS A CA  1 
ATOM   585  C  C   . LYS A 1 70  ? 9.193   19.328 93.554  1.00 25.11 ? 70   LYS A C   1 
ATOM   586  O  O   . LYS A 1 70  ? 10.407  19.554 93.628  1.00 22.56 ? 70   LYS A O   1 
ATOM   587  C  CB  . LYS A 1 70  ? 8.314   17.490 92.137  1.00 26.31 ? 70   LYS A CB  1 
ATOM   588  C  CG  . LYS A 1 70  ? 8.871   16.147 91.700  1.00 62.25 ? 70   LYS A CG  1 
ATOM   589  C  CD  . LYS A 1 70  ? 8.285   15.709 90.362  1.00 67.83 ? 70   LYS A CD  1 
ATOM   590  C  CE  . LYS A 1 70  ? 7.752   14.273 90.416  1.00 71.33 ? 70   LYS A CE  1 
ATOM   591  N  NZ  . LYS A 1 70  ? 6.283   14.201 90.727  1.00 41.11 ? 70   LYS A NZ  1 
ATOM   592  N  N   . LEU A 1 71  ? 8.279   20.290 93.445  1.00 21.41 ? 71   LEU A N   1 
ATOM   593  C  CA  . LEU A 1 71  ? 8.660   21.715 93.501  1.00 18.04 ? 71   LEU A CA  1 
ATOM   594  C  C   . LEU A 1 71  ? 9.357   22.025 94.829  1.00 17.59 ? 71   LEU A C   1 
ATOM   595  O  O   . LEU A 1 71  ? 10.361  22.738 94.851  1.00 18.86 ? 71   LEU A O   1 
ATOM   596  C  CB  . LEU A 1 71  ? 7.427   22.618 93.341  1.00 20.47 ? 71   LEU A CB  1 
ATOM   597  C  CG  . LEU A 1 71  ? 7.706   24.122 93.179  1.00 25.27 ? 71   LEU A CG  1 
ATOM   598  C  CD1 . LEU A 1 71  ? 8.632   24.357 91.990  1.00 20.38 ? 71   LEU A CD1 1 
ATOM   599  C  CD2 . LEU A 1 71  ? 6.420   24.953 93.044  1.00 19.13 ? 71   LEU A CD2 1 
ATOM   600  N  N   . LYS A 1 72  ? 8.822   21.505 95.935  1.00 16.88 ? 72   LYS A N   1 
ATOM   601  C  CA  A LYS A 1 72  ? 9.425   21.769 97.242  0.50 21.84 ? 72   LYS A CA  1 
ATOM   602  C  CA  B LYS A 1 72  ? 9.416   21.742 97.257  0.50 25.51 ? 72   LYS A CA  1 
ATOM   603  C  C   . LYS A 1 72  ? 10.888  21.344 97.289  1.00 26.91 ? 72   LYS A C   1 
ATOM   604  O  O   . LYS A 1 72  ? 11.730  22.096 97.792  1.00 21.43 ? 72   LYS A O   1 
ATOM   605  C  CB  A LYS A 1 72  ? 8.610   21.136 98.372  0.50 21.23 ? 72   LYS A CB  1 
ATOM   606  C  CB  B LYS A 1 72  ? 8.632   21.007 98.351  0.50 27.76 ? 72   LYS A CB  1 
ATOM   607  C  CG  A LYS A 1 72  ? 7.392   21.949 98.750  0.50 17.94 ? 72   LYS A CG  1 
ATOM   608  C  CG  B LYS A 1 72  ? 7.400   21.750 98.825  0.50 34.04 ? 72   LYS A CG  1 
ATOM   609  C  CD  A LYS A 1 72  ? 6.477   21.175 99.695  0.50 42.81 ? 72   LYS A CD  1 
ATOM   610  C  CD  B LYS A 1 72  ? 6.591   20.933 99.828  0.50 35.77 ? 72   LYS A CD  1 
ATOM   611  C  CE  A LYS A 1 72  ? 7.139   20.938 101.042 0.50 39.57 ? 72   LYS A CE  1 
ATOM   612  C  CE  B LYS A 1 72  ? 5.426   21.748 100.368 0.50 36.07 ? 72   LYS A CE  1 
ATOM   613  N  NZ  A LYS A 1 72  ? 6.440   19.885 101.833 0.50 46.16 ? 72   LYS A NZ  1 
ATOM   614  N  NZ  B LYS A 1 72  ? 4.395   20.918 101.058 0.50 27.79 ? 72   LYS A NZ  1 
ATOM   615  N  N   . LYS A 1 73  ? 11.178  20.161 96.735  1.00 22.84 ? 73   LYS A N   1 
ATOM   616  C  CA  A LYS A 1 73  ? 12.544  19.632 96.679  0.50 23.37 ? 73   LYS A CA  1 
ATOM   617  C  CA  B LYS A 1 73  ? 12.540  19.599 96.636  0.50 24.43 ? 73   LYS A CA  1 
ATOM   618  C  C   . LYS A 1 73  ? 13.467  20.480 95.805  1.00 24.20 ? 73   LYS A C   1 
ATOM   619  O  O   . LYS A 1 73  ? 14.619  20.756 96.188  1.00 18.51 ? 73   LYS A O   1 
ATOM   620  C  CB  A LYS A 1 73  ? 12.536  18.175 96.195  0.50 20.76 ? 73   LYS A CB  1 
ATOM   621  C  CB  B LYS A 1 73  ? 12.468  18.204 95.991  0.50 27.51 ? 73   LYS A CB  1 
ATOM   622  C  CG  A LYS A 1 73  ? 12.184  17.157 97.273  0.50 20.29 ? 73   LYS A CG  1 
ATOM   623  C  CG  B LYS A 1 73  ? 13.780  17.414 95.949  0.50 28.62 ? 73   LYS A CG  1 
ATOM   624  C  CD  A LYS A 1 73  ? 12.308  15.724 96.752  0.50 26.27 ? 73   LYS A CD  1 
ATOM   625  C  CD  B LYS A 1 73  ? 14.843  18.027 95.027  0.50 48.14 ? 73   LYS A CD  1 
ATOM   626  C  CE  A LYS A 1 73  ? 13.466  15.577 95.774  0.50 27.27 ? 73   LYS A CE  1 
ATOM   627  C  CE  B LYS A 1 73  ? 14.570  17.751 93.558  0.50 18.40 ? 73   LYS A CE  1 
ATOM   628  N  NZ  A LYS A 1 73  ? 13.745  14.149 95.453  0.50 56.43 ? 73   LYS A NZ  1 
ATOM   629  N  NZ  B LYS A 1 73  ? 15.555  18.409 92.654  0.50 30.15 ? 73   LYS A NZ  1 
ATOM   630  N  N   . GLU A 1 74  ? 12.965  20.898 94.642  1.00 17.03 ? 74   GLU A N   1 
ATOM   631  C  CA  . GLU A 1 74  ? 13.727  21.693 93.704  1.00 21.64 ? 74   GLU A CA  1 
ATOM   632  C  C   . GLU A 1 74  ? 13.989  23.070 94.301  1.00 19.68 ? 74   GLU A C   1 
ATOM   633  O  O   . GLU A 1 74  ? 15.108  23.569 94.218  1.00 18.87 ? 74   GLU A O   1 
ATOM   634  C  CB  . GLU A 1 74  ? 12.983  21.810 92.370  1.00 19.94 ? 74   GLU A CB  1 
ATOM   635  C  CG  . GLU A 1 74  ? 13.002  20.496 91.593  1.00 22.57 ? 74   GLU A CG  1 
ATOM   636  C  CD  . GLU A 1 74  ? 11.808  20.305 90.659  1.00 33.33 ? 74   GLU A CD  1 
ATOM   637  O  OE1 . GLU A 1 74  ? 10.954  21.210 90.522  1.00 22.09 ? 74   GLU A OE1 1 
ATOM   638  O  OE2 . GLU A 1 74  ? 11.726  19.225 90.053  1.00 28.74 ? 74   GLU A OE2 1 
ATOM   639  N  N   . MET A 1 75  ? 12.962  23.677 94.896  1.00 16.65 ? 75   MET A N   1 
ATOM   640  C  CA  . MET A 1 75  ? 13.148  24.979 95.555  1.00 14.97 ? 75   MET A CA  1 
ATOM   641  C  C   . MET A 1 75  ? 14.148  24.884 96.723  1.00 24.55 ? 75   MET A C   1 
ATOM   642  O  O   . MET A 1 75  ? 14.946  25.797 96.930  1.00 19.68 ? 75   MET A O   1 
ATOM   643  C  CB  . MET A 1 75  ? 11.812  25.550 96.031  1.00 18.80 ? 75   MET A CB  1 
ATOM   644  C  CG  . MET A 1 75  ? 10.960  26.077 94.875  1.00 18.97 ? 75   MET A CG  1 
ATOM   645  S  SD  . MET A 1 75  ? 9.350   26.688 95.405  1.00 19.12 ? 75   MET A SD  1 
ATOM   646  C  CE  . MET A 1 75  ? 9.785   28.076 96.484  1.00 18.60 ? 75   MET A CE  1 
ATOM   647  N  N   . SER A 1 76  ? 14.103  23.784 97.474  1.00 19.01 ? 76   SER A N   1 
ATOM   648  C  CA  A SER A 1 76  ? 15.056  23.553 98.572  0.50 16.58 ? 76   SER A CA  1 
ATOM   649  C  CA  B SER A 1 76  ? 15.050  23.574 98.567  0.50 18.52 ? 76   SER A CA  1 
ATOM   650  C  C   . SER A 1 76  ? 16.498  23.581 98.077  1.00 19.23 ? 76   SER A C   1 
ATOM   651  O  O   . SER A 1 76  ? 17.380  24.154 98.722  1.00 18.88 ? 76   SER A O   1 
ATOM   652  C  CB  A SER A 1 76  ? 14.776  22.220 99.280  0.50 20.06 ? 76   SER A CB  1 
ATOM   653  C  CB  B SER A 1 76  ? 14.727  22.279 99.314  0.50 25.62 ? 76   SER A CB  1 
ATOM   654  O  OG  A SER A 1 76  ? 15.434  22.169 100.541 0.50 18.30 ? 76   SER A OG  1 
ATOM   655  O  OG  B SER A 1 76  ? 13.666  22.496 100.231 0.50 22.72 ? 76   SER A OG  1 
ATOM   656  N  N   . LEU A 1 77  ? 16.738  22.962 96.929  1.00 19.98 ? 77   LEU A N   1 
ATOM   657  C  CA  . LEU A 1 77  ? 18.072  22.918 96.332  1.00 18.72 ? 77   LEU A CA  1 
ATOM   658  C  C   . LEU A 1 77  ? 18.601  24.319 96.051  1.00 25.52 ? 77   LEU A C   1 
ATOM   659  O  O   . LEU A 1 77  ? 19.773  24.627 96.322  1.00 19.68 ? 77   LEU A O   1 
ATOM   660  C  CB  . LEU A 1 77  ? 18.038  22.113 95.043  1.00 23.51 ? 77   LEU A CB  1 
ATOM   661  C  CG  . LEU A 1 77  ? 18.000  20.600 95.198  1.00 25.53 ? 77   LEU A CG  1 
ATOM   662  C  CD1 . LEU A 1 77  ? 17.945  19.981 93.820  1.00 23.34 ? 77   LEU A CD1 1 
ATOM   663  C  CD2 . LEU A 1 77  ? 19.241  20.103 95.977  1.00 30.59 ? 77   LEU A CD2 1 
ATOM   664  N  N   . VAL A 1 78  ? 17.725  25.185 95.547  1.00 18.33 ? 78   VAL A N   1 
ATOM   665  C  CA  . VAL A 1 78  ? 18.100  26.569 95.297  1.00 17.96 ? 78   VAL A CA  1 
ATOM   666  C  C   . VAL A 1 78  ? 18.316  27.317 96.625  1.00 18.74 ? 78   VAL A C   1 
ATOM   667  O  O   . VAL A 1 78  ? 19.295  28.057 96.782  1.00 18.27 ? 78   VAL A O   1 
ATOM   668  C  CB  . VAL A 1 78  ? 17.032  27.301 94.430  1.00 19.11 ? 78   VAL A CB  1 
ATOM   669  C  CG1 . VAL A 1 78  ? 17.475  28.710 94.094  1.00 16.80 ? 78   VAL A CG1 1 
ATOM   670  C  CG2 . VAL A 1 78  ? 16.727  26.500 93.138  1.00 20.57 ? 78   VAL A CG2 1 
ATOM   671  N  N   . LEU A 1 79  ? 17.392  27.134 97.567  1.00 19.15 ? 79   LEU A N   1 
ATOM   672  C  CA  . LEU A 1 79  ? 17.441  27.851 98.840  1.00 16.69 ? 79   LEU A CA  1 
ATOM   673  C  C   . LEU A 1 79  ? 18.704  27.484 99.634  1.00 21.89 ? 79   LEU A C   1 
ATOM   674  O  O   . LEU A 1 79  ? 19.246  28.301 100.372 1.00 18.01 ? 79   LEU A O   1 
ATOM   675  C  CB  . LEU A 1 79  ? 16.179  27.569 99.657  1.00 16.96 ? 79   LEU A CB  1 
ATOM   676  C  CG  . LEU A 1 79  ? 14.935  28.327 99.170  1.00 14.59 ? 79   LEU A CG  1 
ATOM   677  C  CD1 . LEU A 1 79  ? 13.689  27.666 99.796  1.00 23.70 ? 79   LEU A CD1 1 
ATOM   678  C  CD2 . LEU A 1 79  ? 15.019  29.806 99.540  1.00 16.06 ? 79   LEU A CD2 1 
ATOM   679  N  N   . ASP A 1 80  ? 19.180  26.256 99.456  1.00 19.08 ? 80   ASP A N   1 
ATOM   680  C  CA  . ASP A 1 80  ? 20.383  25.789 100.158 1.00 15.80 ? 80   ASP A CA  1 
ATOM   681  C  C   . ASP A 1 80  ? 21.594  26.653 99.798  1.00 23.00 ? 80   ASP A C   1 
ATOM   682  O  O   . ASP A 1 80  ? 22.513  26.820 100.604 1.00 19.92 ? 80   ASP A O   1 
ATOM   683  C  CB  . ASP A 1 80  ? 20.696  24.345 99.747  1.00 16.25 ? 80   ASP A CB  1 
ATOM   684  C  CG  . ASP A 1 80  ? 19.872  23.320 100.500 1.00 23.99 ? 80   ASP A CG  1 
ATOM   685  O  OD1 . ASP A 1 80  ? 19.163  23.674 101.466 1.00 24.67 ? 80   ASP A OD1 1 
ATOM   686  O  OD2 . ASP A 1 80  ? 19.923  22.141 100.091 1.00 34.44 ? 80   ASP A OD2 1 
ATOM   687  N  N   . THR A 1 81  ? 21.599  27.170 98.572  1.00 15.55 ? 81   THR A N   1 
ATOM   688  C  CA  . THR A 1 81  ? 22.691  28.016 98.088  1.00 18.27 ? 81   THR A CA  1 
ATOM   689  C  C   . THR A 1 81  ? 22.770  29.408 98.737  1.00 23.54 ? 81   THR A C   1 
ATOM   690  O  O   . THR A 1 81  ? 23.823  30.057 98.696  1.00 17.23 ? 81   THR A O   1 
ATOM   691  C  CB  . THR A 1 81  ? 22.678  28.185 96.550  1.00 17.94 ? 81   THR A CB  1 
ATOM   692  O  OG1 . THR A 1 81  ? 21.647  29.103 96.122  1.00 17.51 ? 81   THR A OG1 1 
ATOM   693  C  CG2 . THR A 1 81  ? 22.536  26.829 95.830  1.00 20.61 ? 81   THR A CG2 1 
ATOM   694  N  N   . VAL A 1 82  ? 21.654  29.876 99.291  1.00 17.16 ? 82   VAL A N   1 
ATOM   695  C  CA  . VAL A 1 82  ? 21.560  31.262 99.766  1.00 16.26 ? 82   VAL A CA  1 
ATOM   696  C  C   . VAL A 1 82  ? 21.114  31.398 101.233 1.00 19.44 ? 82   VAL A C   1 
ATOM   697  O  O   . VAL A 1 82  ? 21.389  32.404 101.887 1.00 17.63 ? 82   VAL A O   1 
ATOM   698  C  CB  . VAL A 1 82  ? 20.632  32.114 98.859  1.00 16.79 ? 82   VAL A CB  1 
ATOM   699  C  CG1 . VAL A 1 82  ? 21.232  32.248 97.469  1.00 16.19 ? 82   VAL A CG1 1 
ATOM   700  C  CG2 . VAL A 1 82  ? 19.229  31.476 98.753  1.00 16.28 ? 82   VAL A CG2 1 
ATOM   701  N  N   . ASP A 1 83  ? 20.428  30.401 101.772 1.00 17.47 ? 83   ASP A N   1 
ATOM   702  C  CA  . ASP A 1 83  ? 19.917  30.588 103.108 1.00 20.48 ? 83   ASP A CA  1 
ATOM   703  C  C   . ASP A 1 83  ? 21.003  30.602 104.196 1.00 16.80 ? 83   ASP A C   1 
ATOM   704  O  O   . ASP A 1 83  ? 21.884  29.738 104.211 1.00 19.51 ? 83   ASP A O   1 
ATOM   705  C  CB  . ASP A 1 83  ? 18.847  29.571 103.466 1.00 23.18 ? 83   ASP A CB  1 
ATOM   706  C  CG  . ASP A 1 83  ? 18.282  29.832 104.834 1.00 27.02 ? 83   ASP A CG  1 
ATOM   707  O  OD1 . ASP A 1 83  ? 17.752  30.942 105.053 1.00 18.14 ? 83   ASP A OD1 1 
ATOM   708  O  OD2 . ASP A 1 83  ? 18.434  28.962 105.714 1.00 43.21 ? 83   ASP A OD2 1 
ATOM   709  N  N   . HIS A 1 84  ? 20.898  31.557 105.120 1.00 15.20 ? 84   HIS A N   1 
ATOM   710  C  CA  . HIS A 1 84  ? 21.925  31.748 106.162 1.00 17.98 ? 84   HIS A CA  1 
ATOM   711  C  C   . HIS A 1 84  ? 23.350  31.910 105.613 1.00 18.18 ? 84   HIS A C   1 
ATOM   712  O  O   . HIS A 1 84  ? 24.333  31.507 106.237 1.00 17.33 ? 84   HIS A O   1 
ATOM   713  C  CB  . HIS A 1 84  ? 21.825  30.645 107.207 1.00 17.35 ? 84   HIS A CB  1 
ATOM   714  C  CG  . HIS A 1 84  ? 20.682  30.852 108.150 1.00 29.01 ? 84   HIS A CG  1 
ATOM   715  N  ND1 . HIS A 1 84  ? 19.386  30.510 107.831 1.00 27.87 ? 84   HIS A ND1 1 
ATOM   716  C  CD2 . HIS A 1 84  ? 20.624  31.451 109.364 1.00 37.33 ? 84   HIS A CD2 1 
ATOM   717  C  CE1 . HIS A 1 84  ? 18.583  30.848 108.825 1.00 32.43 ? 84   HIS A CE1 1 
ATOM   718  N  NE2 . HIS A 1 84  ? 19.310  31.422 109.768 1.00 31.94 ? 84   HIS A NE2 1 
ATOM   719  N  N   . ARG A 1 85  ? 23.440  32.542 104.450 1.00 17.98 ? 85   ARG A N   1 
ATOM   720  C  CA  . ARG A 1 85  ? 24.707  32.818 103.807 1.00 14.61 ? 85   ARG A CA  1 
ATOM   721  C  C   . ARG A 1 85  ? 24.910  34.314 103.573 1.00 17.67 ? 85   ARG A C   1 
ATOM   722  O  O   . ARG A 1 85  ? 23.993  35.130 103.732 1.00 15.20 ? 85   ARG A O   1 
ATOM   723  C  CB  . ARG A 1 85  ? 24.783  32.078 102.465 1.00 18.79 ? 85   ARG A CB  1 
ATOM   724  C  CG  . ARG A 1 85  ? 24.552  30.561 102.600 1.00 22.82 ? 85   ARG A CG  1 
ATOM   725  C  CD  . ARG A 1 85  ? 25.492  29.806 101.682 1.00 44.59 ? 85   ARG A CD  1 
ATOM   726  N  NE  . ARG A 1 85  ? 25.083  28.420 101.483 1.00 81.34 ? 85   ARG A NE  1 
ATOM   727  C  CZ  . ARG A 1 85  ? 25.627  27.383 102.112 1.00 97.88 ? 85   ARG A CZ  1 
ATOM   728  N  NH1 . ARG A 1 85  ? 26.604  27.571 102.990 1.00 95.32 ? 85   ARG A NH1 1 
ATOM   729  N  NH2 . ARG A 1 85  ? 25.193  26.154 101.863 1.00 91.63 ? 85   ARG A NH2 1 
ATOM   730  N  N   . ASN A 1 86  ? 26.131  34.653 103.185 1.00 16.59 ? 86   ASN A N   1 
ATOM   731  C  CA  . ASN A 1 86  ? 26.463  35.980 102.705 1.00 14.72 ? 86   ASN A CA  1 
ATOM   732  C  C   . ASN A 1 86  ? 26.528  35.928 101.162 1.00 17.27 ? 86   ASN A C   1 
ATOM   733  O  O   . ASN A 1 86  ? 27.383  35.227 100.583 1.00 15.76 ? 86   ASN A O   1 
ATOM   734  C  CB  . ASN A 1 86  ? 27.823  36.371 103.296 1.00 13.61 ? 86   ASN A CB  1 
ATOM   735  C  CG  . ASN A 1 86  ? 28.255  37.757 102.890 1.00 16.71 ? 86   ASN A CG  1 
ATOM   736  O  OD1 . ASN A 1 86  ? 28.224  38.098 101.711 1.00 17.38 ? 86   ASN A OD1 1 
ATOM   737  N  ND2 . ASN A 1 86  ? 28.687  38.559 103.860 1.00 17.81 ? 86   ASN A ND2 1 
ATOM   738  N  N   . LEU A 1 87  ? 25.609  36.632 100.497 1.00 14.92 ? 87   LEU A N   1 
ATOM   739  C  CA  . LEU A 1 87  ? 25.456  36.481 99.042  1.00 12.69 ? 87   LEU A CA  1 
ATOM   740  C  C   . LEU A 1 87  ? 26.768  36.755 98.294  1.00 18.05 ? 87   LEU A C   1 
ATOM   741  O  O   . LEU A 1 87  ? 27.178  35.977 97.439  1.00 14.11 ? 87   LEU A O   1 
ATOM   742  C  CB  . LEU A 1 87  ? 24.332  37.362 98.505  1.00 11.75 ? 87   LEU A CB  1 
ATOM   743  C  CG  . LEU A 1 87  ? 22.926  37.141 99.091  1.00 13.22 ? 87   LEU A CG  1 
ATOM   744  C  CD1 . LEU A 1 87  ? 21.912  38.024 98.323  1.00 15.09 ? 87   LEU A CD1 1 
ATOM   745  C  CD2 . LEU A 1 87  ? 22.554  35.681 98.967  1.00 16.00 ? 87   LEU A CD2 1 
ATOM   746  N  N   . ASP A 1 88  ? 27.425  37.852 98.642  1.00 10.17 ? 88   ASP A N   1 
ATOM   747  C  CA  . ASP A 1 88  ? 28.597  38.312 97.898  1.00 13.29 ? 88   ASP A CA  1 
ATOM   748  C  C   . ASP A 1 88  ? 29.832  37.467 98.160  1.00 15.45 ? 88   ASP A C   1 
ATOM   749  O  O   . ASP A 1 88  ? 30.701  37.374 97.299  1.00 16.66 ? 88   ASP A O   1 
ATOM   750  C  CB  . ASP A 1 88  ? 28.881  39.767 98.241  1.00 14.31 ? 88   ASP A CB  1 
ATOM   751  C  CG  . ASP A 1 88  ? 27.630  40.602 98.208  1.00 15.49 ? 88   ASP A CG  1 
ATOM   752  O  OD1 . ASP A 1 88  ? 27.097  40.856 97.109  1.00 13.16 ? 88   ASP A OD1 1 
ATOM   753  O  OD2 . ASP A 1 88  ? 27.154  40.961 99.291  1.00 15.92 ? 88   ASP A OD2 1 
ATOM   754  N  N   . LYS A 1 89  ? 29.909  36.872 99.349  1.00 17.02 ? 89   LYS A N   1 
ATOM   755  C  CA  . LYS A 1 89  ? 31.091  36.120 99.764  1.00 19.19 ? 89   LYS A CA  1 
ATOM   756  C  C   . LYS A 1 89  ? 30.962  34.605 99.643  1.00 23.54 ? 89   LYS A C   1 
ATOM   757  O  O   . LYS A 1 89  ? 31.958  33.894 99.469  1.00 20.94 ? 89   LYS A O   1 
ATOM   758  C  CB  . LYS A 1 89  ? 31.498  36.497 101.190 1.00 21.52 ? 89   LYS A CB  1 
ATOM   759  C  CG  . LYS A 1 89  ? 31.889  37.975 101.303 1.00 21.40 ? 89   LYS A CG  1 
ATOM   760  C  CD  . LYS A 1 89  ? 32.323  38.320 102.696 1.00 27.09 ? 89   LYS A CD  1 
ATOM   761  C  CE  . LYS A 1 89  ? 32.537  39.821 102.827 1.00 29.18 ? 89   LYS A CE  1 
ATOM   762  N  NZ  . LYS A 1 89  ? 33.095  40.164 104.162 1.00 37.74 ? 89   LYS A NZ  1 
ATOM   763  N  N   . ASP A 1 90  ? 29.745  34.101 99.758  1.00 17.16 ? 90   ASP A N   1 
ATOM   764  C  CA  . ASP A 1 90  ? 29.515  32.642 99.797  1.00 20.46 ? 90   ASP A CA  1 
ATOM   765  C  C   . ASP A 1 90  ? 28.928  32.066 98.511  1.00 20.12 ? 90   ASP A C   1 
ATOM   766  O  O   . ASP A 1 90  ? 28.887  30.835 98.321  1.00 22.99 ? 90   ASP A O   1 
ATOM   767  C  CB  . ASP A 1 90  ? 28.552  32.284 100.935 1.00 18.80 ? 90   ASP A CB  1 
ATOM   768  C  CG  . ASP A 1 90  ? 29.109  32.622 102.297 1.00 25.57 ? 90   ASP A CG  1 
ATOM   769  O  OD1 . ASP A 1 90  ? 30.343  32.536 102.480 1.00 21.16 ? 90   ASP A OD1 1 
ATOM   770  O  OD2 . ASP A 1 90  ? 28.304  32.995 103.181 1.00 18.53 ? 90   ASP A OD2 1 
ATOM   771  N  N   . VAL A 1 91  ? 28.407  32.936 97.660  1.00 17.56 ? 91   VAL A N   1 
ATOM   772  C  CA  . VAL A 1 91  ? 27.734  32.500 96.456  1.00 16.08 ? 91   VAL A CA  1 
ATOM   773  C  C   . VAL A 1 91  ? 28.522  32.985 95.236  1.00 15.21 ? 91   VAL A C   1 
ATOM   774  O  O   . VAL A 1 91  ? 28.679  34.188 95.005  1.00 15.11 ? 91   VAL A O   1 
ATOM   775  C  CB  . VAL A 1 91  ? 26.246  32.991 96.401  1.00 20.56 ? 91   VAL A CB  1 
ATOM   776  C  CG1 . VAL A 1 91  ? 25.508  32.384 95.193  1.00 18.35 ? 91   VAL A CG1 1 
ATOM   777  C  CG2 . VAL A 1 91  ? 25.520  32.609 97.699  1.00 18.87 ? 91   VAL A CG2 1 
ATOM   778  N  N   . GLU A 1 92  ? 29.034  32.027 94.468  1.00 18.64 ? 92   GLU A N   1 
ATOM   779  C  CA  . GLU A 1 92  ? 29.986  32.354 93.431  1.00 17.44 ? 92   GLU A CA  1 
ATOM   780  C  C   . GLU A 1 92  ? 29.418  33.389 92.472  1.00 14.46 ? 92   GLU A C   1 
ATOM   781  O  O   . GLU A 1 92  ? 30.120  34.336 92.067  1.00 16.29 ? 92   GLU A O   1 
ATOM   782  C  CB  . GLU A 1 92  ? 30.436  31.103 92.682  1.00 18.22 ? 92   GLU A CB  1 
ATOM   783  C  CG  . GLU A 1 92  ? 31.615  31.346 91.782  1.00 28.09 ? 92   GLU A CG  1 
ATOM   784  C  CD  . GLU A 1 92  ? 32.916  31.619 92.551  1.00 43.55 ? 92   GLU A CD  1 
ATOM   785  O  OE1 . GLU A 1 92  ? 32.994  31.330 93.774  1.00 35.87 ? 92   GLU A OE1 1 
ATOM   786  O  OE2 . GLU A 1 92  ? 33.872  32.117 91.917  1.00 41.16 ? 92   GLU A OE2 1 
ATOM   787  N  N   . PHE A 1 93  ? 28.144  33.225 92.142  1.00 16.32 ? 93   PHE A N   1 
ATOM   788  C  CA  . PHE A 1 93  ? 27.474  34.099 91.179  1.00 13.54 ? 93   PHE A CA  1 
ATOM   789  C  C   . PHE A 1 93  ? 27.644  35.594 91.510  1.00 16.41 ? 93   PHE A C   1 
ATOM   790  O  O   . PHE A 1 93  ? 27.831  36.446 90.618  1.00 15.84 ? 93   PHE A O   1 
ATOM   791  C  CB  . PHE A 1 93  ? 25.982  33.756 91.104  1.00 12.43 ? 93   PHE A CB  1 
ATOM   792  C  CG  . PHE A 1 93  ? 25.211  34.661 90.184  1.00 14.29 ? 93   PHE A CG  1 
ATOM   793  C  CD1 . PHE A 1 93  ? 25.205  34.450 88.811  1.00 19.57 ? 93   PHE A CD1 1 
ATOM   794  C  CD2 . PHE A 1 93  ? 24.497  35.738 90.700  1.00 12.79 ? 93   PHE A CD2 1 
ATOM   795  C  CE1 . PHE A 1 93  ? 24.482  35.304 87.962  1.00 19.86 ? 93   PHE A CE1 1 
ATOM   796  C  CE2 . PHE A 1 93  ? 23.791  36.596 89.879  1.00 13.47 ? 93   PHE A CE2 1 
ATOM   797  C  CZ  . PHE A 1 93  ? 23.774  36.380 88.493  1.00 20.87 ? 93   PHE A CZ  1 
ATOM   798  N  N   . PHE A 1 94  ? 27.544  35.915 92.797  1.00 13.26 ? 94   PHE A N   1 
ATOM   799  C  CA  . PHE A 1 94  ? 27.557  37.321 93.216  1.00 14.04 ? 94   PHE A CA  1 
ATOM   800  C  C   . PHE A 1 94  ? 28.944  37.932 93.331  1.00 18.37 ? 94   PHE A C   1 
ATOM   801  O  O   . PHE A 1 94  ? 29.097  39.140 93.557  1.00 14.15 ? 94   PHE A O   1 
ATOM   802  C  CB  . PHE A 1 94  ? 26.721  37.507 94.499  1.00 13.80 ? 94   PHE A CB  1 
ATOM   803  C  CG  . PHE A 1 94  ? 25.262  37.219 94.288  1.00 11.49 ? 94   PHE A CG  1 
ATOM   804  C  CD1 . PHE A 1 94  ? 24.459  38.111 93.546  1.00 12.69 ? 94   PHE A CD1 1 
ATOM   805  C  CD2 . PHE A 1 94  ? 24.699  36.042 94.770  1.00 14.80 ? 94   PHE A CD2 1 
ATOM   806  C  CE1 . PHE A 1 94  ? 23.105  37.832 93.306  1.00 19.27 ? 94   PHE A CE1 1 
ATOM   807  C  CE2 . PHE A 1 94  ? 23.351  35.762 94.534  1.00 19.44 ? 94   PHE A CE2 1 
ATOM   808  C  CZ  . PHE A 1 94  ? 22.553  36.664 93.805  1.00 20.36 ? 94   PHE A CZ  1 
ATOM   809  N  N   . LYS A 1 95  ? 29.976  37.121 93.142  1.00 14.82 ? 95   LYS A N   1 
ATOM   810  C  CA  . LYS A 1 95  ? 31.326  37.705 93.009  1.00 16.18 ? 95   LYS A CA  1 
ATOM   811  C  C   . LYS A 1 95  ? 31.463  38.630 91.785  1.00 19.21 ? 95   LYS A C   1 
ATOM   812  O  O   . LYS A 1 95  ? 32.305  39.533 91.763  1.00 17.93 ? 95   LYS A O   1 
ATOM   813  C  CB  . LYS A 1 95  ? 32.382  36.587 92.952  1.00 21.22 ? 95   LYS A CB  1 
ATOM   814  C  CG  . LYS A 1 95  ? 32.492  35.806 94.262  1.00 32.44 ? 95   LYS A CG  1 
ATOM   815  C  CD  . LYS A 1 95  ? 33.702  34.880 94.255  1.00 36.23 ? 95   LYS A CD  1 
ATOM   816  C  CE  . LYS A 1 95  ? 33.965  34.296 95.640  1.00 64.89 ? 95   LYS A CE  1 
ATOM   817  N  NZ  . LYS A 1 95  ? 32.810  33.514 96.169  1.00 65.98 ? 95   LYS A NZ  1 
ATOM   818  N  N   . THR A 1 96  ? 30.641  38.400 90.767  1.00 17.20 ? 96   THR A N   1 
ATOM   819  C  CA  . THR A 1 96  ? 30.792  39.109 89.491  1.00 14.16 ? 96   THR A CA  1 
ATOM   820  C  C   . THR A 1 96  ? 29.513  39.799 88.999  1.00 16.25 ? 96   THR A C   1 
ATOM   821  O  O   . THR A 1 96  ? 29.513  40.448 87.943  1.00 16.11 ? 96   THR A O   1 
ATOM   822  C  CB  . THR A 1 96  ? 31.335  38.152 88.385  1.00 14.31 ? 96   THR A CB  1 
ATOM   823  O  OG1 . THR A 1 96  ? 30.511  36.980 88.334  1.00 17.07 ? 96   THR A OG1 1 
ATOM   824  C  CG2 . THR A 1 96  ? 32.788  37.730 88.722  1.00 19.91 ? 96   THR A CG2 1 
ATOM   825  N  N   . THR A 1 97  ? 28.426  39.685 89.774  1.00 14.57 ? 97   THR A N   1 
ATOM   826  C  CA  . THR A 1 97  ? 27.203  40.403 89.463  1.00 12.11 ? 97   THR A CA  1 
ATOM   827  C  C   . THR A 1 97  ? 26.707  40.961 90.800  1.00 14.20 ? 97   THR A C   1 
ATOM   828  O  O   . THR A 1 97  ? 26.659  40.217 91.798  1.00 14.22 ? 97   THR A O   1 
ATOM   829  C  CB  . THR A 1 97  ? 26.136  39.451 88.846  1.00 13.75 ? 97   THR A CB  1 
ATOM   830  O  OG1 . THR A 1 97  ? 26.604  38.938 87.576  1.00 15.56 ? 97   THR A OG1 1 
ATOM   831  C  CG2 . THR A 1 97  ? 24.784  40.185 88.663  1.00 12.72 ? 97   THR A CG2 1 
ATOM   832  N  N   . VAL A 1 98  ? 26.415  42.263 90.834  1.00 12.68 ? 98   VAL A N   1 
ATOM   833  C  CA  A VAL A 1 98  ? 26.022  42.947 92.068  0.50 15.37 ? 98   VAL A CA  1 
ATOM   834  C  CA  B VAL A 1 98  ? 26.041  42.908 92.096  0.50 11.93 ? 98   VAL A CA  1 
ATOM   835  C  C   . VAL A 1 98  ? 24.776  42.307 92.683  1.00 13.79 ? 98   VAL A C   1 
ATOM   836  O  O   . VAL A 1 98  ? 23.850  41.938 91.968  1.00 14.72 ? 98   VAL A O   1 
ATOM   837  C  CB  A VAL A 1 98  ? 25.787  44.464 91.807  0.50 19.41 ? 98   VAL A CB  1 
ATOM   838  C  CB  B VAL A 1 98  ? 25.934  44.466 92.003  0.50 15.23 ? 98   VAL A CB  1 
ATOM   839  C  CG1 A VAL A 1 98  ? 24.509  44.715 90.975  0.50 8.52  ? 98   VAL A CG1 1 
ATOM   840  C  CG1 B VAL A 1 98  ? 27.317  45.086 92.024  0.50 23.25 ? 98   VAL A CG1 1 
ATOM   841  C  CG2 A VAL A 1 98  ? 25.773  45.241 93.109  0.50 18.29 ? 98   VAL A CG2 1 
ATOM   842  C  CG2 B VAL A 1 98  ? 25.122  44.941 90.773  0.50 5.91  ? 98   VAL A CG2 1 
ATOM   843  N  N   . SER A 1 99  ? 24.743  42.183 94.005  1.00 12.38 ? 99   SER A N   1 
ATOM   844  C  CA  . SER A 1 99  ? 23.634  41.481 94.664  1.00 15.10 ? 99   SER A CA  1 
ATOM   845  C  C   . SER A 1 99  ? 22.387  42.366 94.945  1.00 16.42 ? 99   SER A C   1 
ATOM   846  O  O   . SER A 1 99  ? 21.744  42.260 96.005  1.00 13.42 ? 99   SER A O   1 
ATOM   847  C  CB  . SER A 1 99  ? 24.144  40.849 95.970  1.00 15.05 ? 99   SER A CB  1 
ATOM   848  O  OG  . SER A 1 99  ? 24.597  41.873 96.856  1.00 15.05 ? 99   SER A OG  1 
ATOM   849  N  N   . THR A 1 100 ? 22.037  43.234 94.006  1.00 11.65 ? 100  THR A N   1 
ATOM   850  C  CA  . THR A 1 100 ? 20.756  43.970 94.100  1.00 13.90 ? 100  THR A CA  1 
ATOM   851  C  C   . THR A 1 100 ? 19.648  42.948 94.031  1.00 16.72 ? 100  THR A C   1 
ATOM   852  O  O   . THR A 1 100 ? 19.832  41.872 93.477  1.00 14.00 ? 100  THR A O   1 
ATOM   853  C  CB  . THR A 1 100 ? 20.538  44.933 92.908  1.00 16.38 ? 100  THR A CB  1 
ATOM   854  O  OG1 . THR A 1 100 ? 20.722  44.215 91.672  1.00 12.62 ? 100  THR A OG1 1 
ATOM   855  C  CG2 . THR A 1 100 ? 21.502  46.088 92.977  1.00 14.44 ? 100  THR A CG2 1 
ATOM   856  N  N   . SER A 1 101 ? 18.466  43.284 94.543  1.00 11.44 ? 101  SER A N   1 
ATOM   857  C  CA  . SER A 1 101 ? 17.384  42.300 94.514  1.00 11.13 ? 101  SER A CA  1 
ATOM   858  C  C   . SER A 1 101 ? 16.909  41.970 93.087  1.00 11.54 ? 101  SER A C   1 
ATOM   859  O  O   . SER A 1 101 ? 16.433  40.871 92.832  1.00 13.13 ? 101  SER A O   1 
ATOM   860  C  CB  . SER A 1 101 ? 16.224  42.746 95.408  1.00 17.23 ? 101  SER A CB  1 
ATOM   861  O  OG  . SER A 1 101 ? 16.674  42.851 96.751  1.00 19.23 ? 101  SER A OG  1 
ATOM   862  N  N   . GLU A 1 102 ? 17.070  42.910 92.163  1.00 14.60 ? 102  GLU A N   1 
ATOM   863  C  CA  . GLU A 1 102 ? 16.862  42.629 90.722  1.00 14.12 ? 102  GLU A CA  1 
ATOM   864  C  C   . GLU A 1 102 ? 17.707  41.428 90.321  1.00 14.30 ? 102  GLU A C   1 
ATOM   865  O  O   . GLU A 1 102 ? 17.217  40.466 89.717  1.00 13.72 ? 102  GLU A O   1 
ATOM   866  C  CB  . GLU A 1 102 ? 17.275  43.852 89.868  1.00 12.68 ? 102  GLU A CB  1 
ATOM   867  C  CG  . GLU A 1 102 ? 16.338  45.071 89.967  1.00 15.43 ? 102  GLU A CG  1 
ATOM   868  C  CD  . GLU A 1 102 ? 16.709  46.045 91.084  1.00 15.12 ? 102  GLU A CD  1 
ATOM   869  O  OE1 . GLU A 1 102 ? 17.318  45.632 92.115  1.00 15.74 ? 102  GLU A OE1 1 
ATOM   870  O  OE2 . GLU A 1 102 ? 16.352  47.228 90.935  1.00 16.89 ? 102  GLU A OE2 1 
ATOM   871  N  N   . ASN A 1 103 ? 18.988  41.469 90.668  1.00 11.06 ? 103  ASN A N   1 
ATOM   872  C  CA  . ASN A 1 103 ? 19.904  40.390 90.262  1.00 12.86 ? 103  ASN A CA  1 
ATOM   873  C  C   . ASN A 1 103 ? 19.719  39.104 91.060  1.00 13.28 ? 103  ASN A C   1 
ATOM   874  O  O   . ASN A 1 103 ? 19.988  38.002 90.555  1.00 14.52 ? 103  ASN A O   1 
ATOM   875  C  CB  . ASN A 1 103 ? 21.372  40.865 90.279  1.00 12.77 ? 103  ASN A CB  1 
ATOM   876  C  CG  . ASN A 1 103 ? 21.729  41.703 89.065  1.00 16.46 ? 103  ASN A CG  1 
ATOM   877  O  OD1 . ASN A 1 103 ? 21.342  41.377 87.928  1.00 16.13 ? 103  ASN A OD1 1 
ATOM   878  N  ND2 . ASN A 1 103 ? 22.439  42.819 89.296  1.00 13.49 ? 103  ASN A ND2 1 
ATOM   879  N  N   . VAL A 1 104 ? 19.219  39.233 92.285  1.00 14.17 ? 104  VAL A N   1 
ATOM   880  C  CA  . VAL A 1 104 ? 18.856  38.056 93.083  1.00 15.27 ? 104  VAL A CA  1 
ATOM   881  C  C   . VAL A 1 104 ? 17.668  37.352 92.425  1.00 11.98 ? 104  VAL A C   1 
ATOM   882  O  O   . VAL A 1 104 ? 17.638  36.138 92.318  1.00 14.92 ? 104  VAL A O   1 
ATOM   883  C  CB  . VAL A 1 104 ? 18.527  38.435 94.558  1.00 14.57 ? 104  VAL A CB  1 
ATOM   884  C  CG1 . VAL A 1 104 ? 18.049  37.204 95.350  1.00 14.43 ? 104  VAL A CG1 1 
ATOM   885  C  CG2 . VAL A 1 104 ? 19.786  39.054 95.247  1.00 16.47 ? 104  VAL A CG2 1 
ATOM   886  N  N   . ALA A 1 105 ? 16.690  38.129 91.960  1.00 12.02 ? 105  ALA A N   1 
ATOM   887  C  CA  . ALA A 1 105 ? 15.517  37.520 91.325  1.00 10.34 ? 105  ALA A CA  1 
ATOM   888  C  C   . ALA A 1 105 ? 15.954  36.715 90.094  1.00 14.42 ? 105  ALA A C   1 
ATOM   889  O  O   . ALA A 1 105 ? 15.482  35.597 89.851  1.00 12.11 ? 105  ALA A O   1 
ATOM   890  C  CB  . ALA A 1 105 ? 14.531  38.600 90.947  1.00 12.00 ? 105  ALA A CB  1 
ATOM   891  N  N   . ILE A 1 106 ? 16.873  37.287 89.329  1.00 13.94 ? 106  ILE A N   1 
ATOM   892  C  CA  . ILE A 1 106 ? 17.383  36.627 88.133  1.00 13.21 ? 106  ILE A CA  1 
ATOM   893  C  C   . ILE A 1 106 ? 18.144  35.351 88.516  1.00 16.22 ? 106  ILE A C   1 
ATOM   894  O  O   . ILE A 1 106 ? 17.917  34.274 87.949  1.00 14.39 ? 106  ILE A O   1 
ATOM   895  C  CB  . ILE A 1 106 ? 18.274  37.587 87.260  1.00 15.58 ? 106  ILE A CB  1 
ATOM   896  C  CG1 . ILE A 1 106 ? 17.436  38.735 86.683  1.00 11.95 ? 106  ILE A CG1 1 
ATOM   897  C  CG2 . ILE A 1 106 ? 18.943  36.810 86.100  1.00 15.19 ? 106  ILE A CG2 1 
ATOM   898  C  CD1 . ILE A 1 106 ? 18.278  39.875 86.102  1.00 16.17 ? 106  ILE A CD1 1 
ATOM   899  N  N   . TYR A 1 107 ? 19.044  35.475 89.486  1.00 12.75 ? 107  TYR A N   1 
ATOM   900  C  CA  . TYR A 1 107 ? 19.784  34.330 90.004  1.00 14.69 ? 107  TYR A CA  1 
ATOM   901  C  C   . TYR A 1 107 ? 18.866  33.182 90.413  1.00 15.93 ? 107  TYR A C   1 
ATOM   902  O  O   . TYR A 1 107 ? 19.072  32.046 90.004  1.00 14.39 ? 107  TYR A O   1 
ATOM   903  C  CB  . TYR A 1 107 ? 20.710  34.753 91.177  1.00 11.29 ? 107  TYR A CB  1 
ATOM   904  C  CG  . TYR A 1 107 ? 21.269  33.550 91.888  1.00 14.36 ? 107  TYR A CG  1 
ATOM   905  C  CD1 . TYR A 1 107 ? 22.350  32.843 91.354  1.00 19.56 ? 107  TYR A CD1 1 
ATOM   906  C  CD2 . TYR A 1 107 ? 20.687  33.087 93.068  1.00 15.39 ? 107  TYR A CD2 1 
ATOM   907  C  CE1 . TYR A 1 107 ? 22.843  31.717 92.007  1.00 18.84 ? 107  TYR A CE1 1 
ATOM   908  C  CE2 . TYR A 1 107 ? 21.177  31.986 93.716  1.00 14.14 ? 107  TYR A CE2 1 
ATOM   909  C  CZ  . TYR A 1 107 ? 22.243  31.292 93.175  1.00 24.18 ? 107  TYR A CZ  1 
ATOM   910  O  OH  . TYR A 1 107 ? 22.719  30.179 93.834  1.00 18.39 ? 107  TYR A OH  1 
ATOM   911  N  N   . MET A 1 108 ? 17.838  33.468 91.213  1.00 13.28 ? 108  MET A N   1 
ATOM   912  C  CA  . MET A 1 108 ? 16.982  32.417 91.744  1.00 15.68 ? 108  MET A CA  1 
ATOM   913  C  C   . MET A 1 108 ? 16.156  31.768 90.623  1.00 14.46 ? 108  MET A C   1 
ATOM   914  O  O   . MET A 1 108 ? 15.986  30.555 90.595  1.00 13.77 ? 108  MET A O   1 
ATOM   915  C  CB  . MET A 1 108 ? 16.057  32.960 92.832  1.00 12.08 ? 108  MET A CB  1 
ATOM   916  C  CG  . MET A 1 108 ? 16.823  33.556 94.024  1.00 11.85 ? 108  MET A CG  1 
ATOM   917  S  SD  . MET A 1 108 ? 17.683  32.343 95.048  1.00 15.77 ? 108  MET A SD  1 
ATOM   918  C  CE  . MET A 1 108 ? 16.297  31.583 95.932  1.00 15.58 ? 108  MET A CE  1 
ATOM   919  N  N   . PHE A 1 109 ? 15.635  32.594 89.730  1.00 14.67 ? 109  PHE A N   1 
ATOM   920  C  CA  . PHE A 1 109 ? 14.924  32.102 88.539  1.00 19.12 ? 109  PHE A CA  1 
ATOM   921  C  C   . PHE A 1 109 ? 15.821  31.138 87.751  1.00 22.15 ? 109  PHE A C   1 
ATOM   922  O  O   . PHE A 1 109 ? 15.421  30.017 87.426  1.00 15.50 ? 109  PHE A O   1 
ATOM   923  C  CB  . PHE A 1 109 ? 14.538  33.293 87.667  1.00 14.02 ? 109  PHE A CB  1 
ATOM   924  C  CG  . PHE A 1 109 ? 13.673  32.951 86.484  1.00 15.13 ? 109  PHE A CG  1 
ATOM   925  C  CD1 . PHE A 1 109 ? 12.295  33.077 86.556  1.00 17.57 ? 109  PHE A CD1 1 
ATOM   926  C  CD2 . PHE A 1 109 ? 14.250  32.523 85.285  1.00 19.01 ? 109  PHE A CD2 1 
ATOM   927  C  CE1 . PHE A 1 109 ? 11.487  32.782 85.441  1.00 17.39 ? 109  PHE A CE1 1 
ATOM   928  C  CE2 . PHE A 1 109 ? 13.457  32.232 84.171  1.00 17.66 ? 109  PHE A CE2 1 
ATOM   929  C  CZ  . PHE A 1 109 ? 12.068  32.363 84.257  1.00 18.07 ? 109  PHE A CZ  1 
ATOM   930  N  N   . GLU A 1 110 ? 17.031  31.574 87.432  1.00 14.97 ? 110  GLU A N   1 
ATOM   931  C  CA  . GLU A 1 110 ? 17.901  30.753 86.591  1.00 21.72 ? 110  GLU A CA  1 
ATOM   932  C  C   . GLU A 1 110 ? 18.387  29.482 87.295  1.00 16.16 ? 110  GLU A C   1 
ATOM   933  O  O   . GLU A 1 110 ? 18.443  28.407 86.682  1.00 18.51 ? 110  GLU A O   1 
ATOM   934  C  CB  . GLU A 1 110 ? 19.070  31.580 86.042  1.00 22.17 ? 110  GLU A CB  1 
ATOM   935  C  CG  . GLU A 1 110 ? 18.652  32.638 85.008  1.00 19.15 ? 110  GLU A CG  1 
ATOM   936  C  CD  . GLU A 1 110 ? 17.987  32.035 83.757  1.00 36.11 ? 110  GLU A CD  1 
ATOM   937  O  OE1 . GLU A 1 110 ? 18.255  30.859 83.434  1.00 40.41 ? 110  GLU A OE1 1 
ATOM   938  O  OE2 . GLU A 1 110 ? 17.192  32.740 83.093  1.00 41.28 ? 110  GLU A OE2 1 
ATOM   939  N  N   . LYS A 1 111 ? 18.737  29.593 88.580  1.00 17.63 ? 111  LYS A N   1 
ATOM   940  C  CA  . LYS A 1 111 ? 19.168  28.424 89.353  1.00 18.76 ? 111  LYS A CA  1 
ATOM   941  C  C   . LYS A 1 111 ? 18.022  27.406 89.499  1.00 22.29 ? 111  LYS A C   1 
ATOM   942  O  O   . LYS A 1 111 ? 18.216  26.189 89.368  1.00 20.48 ? 111  LYS A O   1 
ATOM   943  C  CB  . LYS A 1 111 ? 19.703  28.842 90.727  1.00 20.37 ? 111  LYS A CB  1 
ATOM   944  C  CG  . LYS A 1 111 ? 20.122  27.679 91.608  1.00 26.95 ? 111  LYS A CG  1 
ATOM   945  C  CD  . LYS A 1 111 ? 21.492  27.149 91.167  1.00 28.56 ? 111  LYS A CD  1 
ATOM   946  C  CE  . LYS A 1 111 ? 21.796  25.805 91.814  1.00 42.43 ? 111  LYS A CE  1 
ATOM   947  N  NZ  . LYS A 1 111 ? 22.937  25.132 91.129  1.00 51.87 ? 111  LYS A NZ  1 
ATOM   948  N  N   . LEU A 1 112 ? 16.817  27.904 89.737  1.00 14.15 ? 112  LEU A N   1 
ATOM   949  C  CA  . LEU A 1 112 ? 15.666  27.006 89.848  1.00 15.73 ? 112  LEU A CA  1 
ATOM   950  C  C   . LEU A 1 112 ? 15.434  26.340 88.510  1.00 17.13 ? 112  LEU A C   1 
ATOM   951  O  O   . LEU A 1 112 ? 15.278  25.127 88.440  1.00 19.63 ? 112  LEU A O   1 
ATOM   952  C  CB  . LEU A 1 112 ? 14.405  27.738 90.277  1.00 12.88 ? 112  LEU A CB  1 
ATOM   953  C  CG  . LEU A 1 112 ? 13.162  26.859 90.357  1.00 14.04 ? 112  LEU A CG  1 
ATOM   954  C  CD1 . LEU A 1 112 ? 13.411  25.666 91.301  1.00 18.59 ? 112  LEU A CD1 1 
ATOM   955  C  CD2 . LEU A 1 112 ? 11.924  27.675 90.790  1.00 14.28 ? 112  LEU A CD2 1 
ATOM   956  N  N   . LYS A 1 113 ? 15.418  27.133 87.451  1.00 18.69 ? 113  LYS A N   1 
ATOM   957  C  CA  . LYS A 1 113 ? 15.192  26.554 86.119  1.00 24.50 ? 113  LYS A CA  1 
ATOM   958  C  C   . LYS A 1 113 ? 16.177  25.401 85.843  1.00 32.27 ? 113  LYS A C   1 
ATOM   959  O  O   . LYS A 1 113 ? 15.801  24.360 85.280  1.00 24.38 ? 113  LYS A O   1 
ATOM   960  C  CB  . LYS A 1 113 ? 15.251  27.641 85.062  1.00 19.95 ? 113  LYS A CB  1 
ATOM   961  C  CG  . LYS A 1 113 ? 14.438  27.366 83.816  1.00 30.99 ? 113  LYS A CG  1 
ATOM   962  C  CD  . LYS A 1 113 ? 14.232  28.663 83.054  1.00 34.35 ? 113  LYS A CD  1 
ATOM   963  C  CE  . LYS A 1 113 ? 14.384  28.468 81.558  1.00 69.02 ? 113  LYS A CE  1 
ATOM   964  N  NZ  . LYS A 1 113 ? 14.439  29.777 80.842  1.00 41.29 ? 113  LYS A NZ  1 
ATOM   965  N  N   . SER A 1 114 ? 17.414  25.575 86.308  1.00 19.30 ? 114  SER A N   1 
ATOM   966  C  CA  . SER A 1 114 ? 18.494  24.607 86.165  1.00 26.13 ? 114  SER A CA  1 
ATOM   967  C  C   . SER A 1 114 ? 18.298  23.282 86.912  1.00 31.36 ? 114  SER A C   1 
ATOM   968  O  O   . SER A 1 114 ? 18.921  22.288 86.566  1.00 30.70 ? 114  SER A O   1 
ATOM   969  C  CB  . SER A 1 114 ? 19.837  25.249 86.552  1.00 22.00 ? 114  SER A CB  1 
ATOM   970  O  OG  . SER A 1 114 ? 20.134  25.051 87.919  1.00 25.05 ? 114  SER A OG  1 
ATOM   971  N  N   . VAL A 1 115 ? 17.442  23.257 87.930  1.00 22.24 ? 115  VAL A N   1 
ATOM   972  C  CA  A VAL A 1 115 ? 17.253  22.042 88.721  0.50 20.07 ? 115  VAL A CA  1 
ATOM   973  C  CA  B VAL A 1 115 ? 17.253  22.066 88.746  0.50 21.34 ? 115  VAL A CA  1 
ATOM   974  C  C   . VAL A 1 115 ? 15.871  21.423 88.547  1.00 25.65 ? 115  VAL A C   1 
ATOM   975  O  O   . VAL A 1 115 ? 15.593  20.347 89.073  1.00 22.20 ? 115  VAL A O   1 
ATOM   976  C  CB  A VAL A 1 115 ? 17.587  22.218 90.238  0.50 23.07 ? 115  VAL A CB  1 
ATOM   977  C  CB  B VAL A 1 115 ? 17.487  22.378 90.241  0.50 25.83 ? 115  VAL A CB  1 
ATOM   978  C  CG1 A VAL A 1 115 ? 19.045  22.630 90.434  0.50 29.02 ? 115  VAL A CG1 1 
ATOM   979  C  CG1 B VAL A 1 115 ? 17.224  21.160 91.085  0.50 25.72 ? 115  VAL A CG1 1 
ATOM   980  C  CG2 A VAL A 1 115 ? 16.623  23.190 90.939  0.50 9.83  ? 115  VAL A CG2 1 
ATOM   981  C  CG2 B VAL A 1 115 ? 18.913  22.869 90.467  0.50 32.50 ? 115  VAL A CG2 1 
ATOM   982  N  N   . MET A 1 116 ? 15.004  22.088 87.792  1.00 25.38 ? 116  MET A N   1 
ATOM   983  C  CA  . MET A 1 116 ? 13.612  21.644 87.713  1.00 27.40 ? 116  MET A CA  1 
ATOM   984  C  C   . MET A 1 116 ? 13.412  20.405 86.859  1.00 25.80 ? 116  MET A C   1 
ATOM   985  O  O   . MET A 1 116 ? 13.954  20.316 85.763  1.00 29.67 ? 116  MET A O   1 
ATOM   986  C  CB  . MET A 1 116 ? 12.712  22.758 87.191  1.00 25.74 ? 116  MET A CB  1 
ATOM   987  C  CG  . MET A 1 116 ? 12.277  23.724 88.257  1.00 22.60 ? 116  MET A CG  1 
ATOM   988  S  SD  . MET A 1 116 ? 11.277  25.025 87.544  1.00 23.12 ? 116  MET A SD  1 
ATOM   989  C  CE  . MET A 1 116 ? 9.655   24.220 87.547  1.00 20.94 ? 116  MET A CE  1 
ATOM   990  N  N   . SER A 1 117 ? 12.595  19.484 87.364  1.00 31.50 ? 117  SER A N   1 
ATOM   991  C  CA  . SER A 1 117 ? 12.137  18.324 86.581  1.00 46.22 ? 117  SER A CA  1 
ATOM   992  C  C   . SER A 1 117 ? 11.360  18.711 85.316  1.00 49.03 ? 117  SER A C   1 
ATOM   993  O  O   . SER A 1 117 ? 11.534  18.095 84.264  1.00 50.86 ? 117  SER A O   1 
ATOM   994  C  CB  . SER A 1 117 ? 11.366  17.304 87.453  1.00 37.65 ? 117  SER A CB  1 
ATOM   995  O  OG  . SER A 1 117 ? 10.241  17.863 88.136  1.00 28.37 ? 117  SER A OG  1 
ATOM   996  N  N   . ASN A 1 118 ? 10.532  19.748 85.412  1.00 37.78 ? 118  ASN A N   1 
ATOM   997  C  CA  . ASN A 1 118 ? 9.829   20.292 84.241  1.00 40.83 ? 118  ASN A CA  1 
ATOM   998  C  C   . ASN A 1 118 ? 9.920   21.825 84.171  1.00 24.31 ? 118  ASN A C   1 
ATOM   999  O  O   . ASN A 1 118 ? 9.002   22.536 84.614  1.00 32.04 ? 118  ASN A O   1 
ATOM   1000 C  CB  . ASN A 1 118 ? 8.359   19.820 84.232  1.00 39.42 ? 118  ASN A CB  1 
ATOM   1001 C  CG  . ASN A 1 118 ? 7.541   20.428 83.091  1.00 65.30 ? 118  ASN A CG  1 
ATOM   1002 O  OD1 . ASN A 1 118 ? 8.073   20.748 82.026  1.00 57.36 ? 118  ASN A OD1 1 
ATOM   1003 N  ND2 . ASN A 1 118 ? 6.237   20.580 83.314  1.00 58.40 ? 118  ASN A ND2 1 
ATOM   1004 N  N   . PRO A 1 119 ? 11.033  22.338 83.641  1.00 30.36 ? 119  PRO A N   1 
ATOM   1005 C  CA  . PRO A 1 119 ? 11.295  23.778 83.713  1.00 37.64 ? 119  PRO A CA  1 
ATOM   1006 C  C   . PRO A 1 119 ? 10.412  24.600 82.777  1.00 35.90 ? 119  PRO A C   1 
ATOM   1007 O  O   . PRO A 1 119 ? 10.319  25.820 82.935  1.00 23.35 ? 119  PRO A O   1 
ATOM   1008 C  CB  . PRO A 1 119 ? 12.772  23.894 83.327  1.00 31.81 ? 119  PRO A CB  1 
ATOM   1009 C  CG  . PRO A 1 119 ? 13.063  22.652 82.541  1.00 29.52 ? 119  PRO A CG  1 
ATOM   1010 C  CD  . PRO A 1 119 ? 12.124  21.592 82.990  1.00 38.90 ? 119  PRO A CD  1 
ATOM   1011 N  N   . SER A 1 120 ? 9.754   23.941 81.826  1.00 23.26 ? 120  SER A N   1 
ATOM   1012 C  CA  . SER A 1 120 ? 8.893   24.652 80.872  1.00 25.83 ? 120  SER A CA  1 
ATOM   1013 C  C   . SER A 1 120 ? 7.726   25.411 81.541  1.00 23.97 ? 120  SER A C   1 
ATOM   1014 O  O   . SER A 1 120 ? 7.302   26.448 81.041  1.00 24.59 ? 120  SER A O   1 
ATOM   1015 C  CB  . SER A 1 120 ? 8.364   23.694 79.788  1.00 25.14 ? 120  SER A CB  1 
ATOM   1016 O  OG  . SER A 1 120 ? 7.386   22.821 80.334  1.00 40.95 ? 120  SER A OG  1 
ATOM   1017 N  N   . VAL A 1 121 ? 7.229   24.905 82.671  1.00 20.22 ? 121  VAL A N   1 
ATOM   1018 C  CA  . VAL A 1 121 ? 6.159   25.605 83.399  1.00 26.27 ? 121  VAL A CA  1 
ATOM   1019 C  C   . VAL A 1 121 ? 6.602   26.770 84.301  1.00 18.58 ? 121  VAL A C   1 
ATOM   1020 O  O   . VAL A 1 121 ? 5.747   27.467 84.842  1.00 16.16 ? 121  VAL A O   1 
ATOM   1021 C  CB  . VAL A 1 121 ? 5.230   24.655 84.209  1.00 29.86 ? 121  VAL A CB  1 
ATOM   1022 C  CG1 . VAL A 1 121 ? 4.459   23.721 83.278  1.00 30.44 ? 121  VAL A CG1 1 
ATOM   1023 C  CG2 . VAL A 1 121 ? 6.010   23.889 85.259  1.00 24.87 ? 121  VAL A CG2 1 
ATOM   1024 N  N   . LEU A 1 122 ? 7.909   26.993 84.458  1.00 17.51 ? 122  LEU A N   1 
ATOM   1025 C  CA  . LEU A 1 122 ? 8.346   28.117 85.297  1.00 19.73 ? 122  LEU A CA  1 
ATOM   1026 C  C   . LEU A 1 122 ? 7.927   29.417 84.636  1.00 18.85 ? 122  LEU A C   1 
ATOM   1027 O  O   . LEU A 1 122 ? 8.247   29.674 83.465  1.00 18.68 ? 122  LEU A O   1 
ATOM   1028 C  CB  . LEU A 1 122 ? 9.869   28.100 85.545  1.00 14.18 ? 122  LEU A CB  1 
ATOM   1029 C  CG  . LEU A 1 122 ? 10.429  29.294 86.338  1.00 16.47 ? 122  LEU A CG  1 
ATOM   1030 C  CD1 . LEU A 1 122 ? 9.780   29.372 87.749  1.00 16.95 ? 122  LEU A CD1 1 
ATOM   1031 C  CD2 . LEU A 1 122 ? 11.950  29.195 86.412  1.00 25.80 ? 122  LEU A CD2 1 
ATOM   1032 N  N   . TYR A 1 123 ? 7.212   30.252 85.381  1.00 15.75 ? 123  TYR A N   1 
ATOM   1033 C  CA  . TYR A 1 123 ? 6.614   31.412 84.780  1.00 14.34 ? 123  TYR A CA  1 
ATOM   1034 C  C   . TYR A 1 123 ? 7.177   32.722 85.375  1.00 17.05 ? 123  TYR A C   1 
ATOM   1035 O  O   . TYR A 1 123 ? 7.497   33.655 84.650  1.00 15.91 ? 123  TYR A O   1 
ATOM   1036 C  CB  . TYR A 1 123 ? 5.087   31.314 84.886  1.00 13.60 ? 123  TYR A CB  1 
ATOM   1037 C  CG  . TYR A 1 123 ? 4.378   32.554 84.406  1.00 16.44 ? 123  TYR A CG  1 
ATOM   1038 C  CD1 . TYR A 1 123 ? 4.308   32.857 83.054  1.00 19.89 ? 123  TYR A CD1 1 
ATOM   1039 C  CD2 . TYR A 1 123 ? 3.807   33.441 85.312  1.00 23.46 ? 123  TYR A CD2 1 
ATOM   1040 C  CE1 . TYR A 1 123 ? 3.677   34.009 82.622  1.00 27.43 ? 123  TYR A CE1 1 
ATOM   1041 C  CE2 . TYR A 1 123 ? 3.190   34.595 84.890  1.00 32.54 ? 123  TYR A CE2 1 
ATOM   1042 C  CZ  . TYR A 1 123 ? 3.122   34.870 83.546  1.00 39.06 ? 123  TYR A CZ  1 
ATOM   1043 O  OH  . TYR A 1 123 ? 2.498   36.022 83.135  1.00 41.40 ? 123  TYR A OH  1 
ATOM   1044 N  N   . LYS A 1 124 ? 7.300   32.790 86.695  1.00 15.53 ? 124  LYS A N   1 
ATOM   1045 C  CA  . LYS A 1 124 ? 7.751   34.040 87.302  1.00 16.40 ? 124  LYS A CA  1 
ATOM   1046 C  C   . LYS A 1 124 ? 8.391   33.788 88.660  1.00 17.76 ? 124  LYS A C   1 
ATOM   1047 O  O   . LYS A 1 124 ? 7.935   32.922 89.424  1.00 15.02 ? 124  LYS A O   1 
ATOM   1048 C  CB  . LYS A 1 124 ? 6.589   35.010 87.450  1.00 11.41 ? 124  LYS A CB  1 
ATOM   1049 C  CG  . LYS A 1 124 ? 7.024   36.365 88.022  1.00 18.22 ? 124  LYS A CG  1 
ATOM   1050 C  CD  . LYS A 1 124 ? 5.890   37.352 88.029  1.00 22.75 ? 124  LYS A CD  1 
ATOM   1051 C  CE  . LYS A 1 124 ? 5.225   37.392 89.389  1.00 21.23 ? 124  LYS A CE  1 
ATOM   1052 N  NZ  . LYS A 1 124 ? 4.024   38.308 89.433  1.00 22.57 ? 124  LYS A NZ  1 
ATOM   1053 N  N   . VAL A 1 125 ? 9.435   34.551 88.966  1.00 13.59 ? 125  VAL A N   1 
ATOM   1054 C  CA  . VAL A 1 125 ? 9.986   34.569 90.325  1.00 13.51 ? 125  VAL A CA  1 
ATOM   1055 C  C   . VAL A 1 125 ? 9.771   35.957 90.922  1.00 11.14 ? 125  VAL A C   1 
ATOM   1056 O  O   . VAL A 1 125 ? 9.941   36.971 90.240  1.00 11.88 ? 125  VAL A O   1 
ATOM   1057 C  CB  . VAL A 1 125 ? 11.513  34.229 90.301  1.00 17.10 ? 125  VAL A CB  1 
ATOM   1058 C  CG1 . VAL A 1 125 ? 12.245  34.848 91.494  1.00 24.07 ? 125  VAL A CG1 1 
ATOM   1059 C  CG2 . VAL A 1 125 ? 11.726  32.719 90.266  1.00 13.55 ? 125  VAL A CG2 1 
ATOM   1060 N  N   . THR A 1 126 ? 9.410   35.991 92.196  1.00 13.19 ? 126  THR A N   1 
ATOM   1061 C  CA  . THR A 1 126 ? 9.307   37.223 92.950  1.00 14.56 ? 126  THR A CA  1 
ATOM   1062 C  C   . THR A 1 126 ? 10.326  37.169 94.094  1.00 12.28 ? 126  THR A C   1 
ATOM   1063 O  O   . THR A 1 126 ? 10.452  36.142 94.757  1.00 13.64 ? 126  THR A O   1 
ATOM   1064 C  CB  . THR A 1 126 ? 7.882   37.367 93.551  1.00 12.50 ? 126  THR A CB  1 
ATOM   1065 O  OG1 . THR A 1 126 ? 6.934   37.388 92.480  1.00 13.26 ? 126  THR A OG1 1 
ATOM   1066 C  CG2 . THR A 1 126 ? 7.754   38.681 94.353  1.00 9.98  ? 126  THR A CG2 1 
ATOM   1067 N  N   . ILE A 1 127 ? 11.020  38.281 94.327  1.00 12.92 ? 127  ILE A N   1 
ATOM   1068 C  CA  . ILE A 1 127 ? 11.825  38.436 95.538  1.00 12.84 ? 127  ILE A CA  1 
ATOM   1069 C  C   . ILE A 1 127 ? 11.303  39.665 96.272  1.00 15.19 ? 127  ILE A C   1 
ATOM   1070 O  O   . ILE A 1 127 ? 11.224  40.735 95.691  1.00 14.77 ? 127  ILE A O   1 
ATOM   1071 C  CB  . ILE A 1 127 ? 13.323  38.651 95.189  1.00 17.13 ? 127  ILE A CB  1 
ATOM   1072 C  CG1 . ILE A 1 127 ? 13.951  37.326 94.691  1.00 14.96 ? 127  ILE A CG1 1 
ATOM   1073 C  CG2 . ILE A 1 127 ? 14.089  39.213 96.403  1.00 12.88 ? 127  ILE A CG2 1 
ATOM   1074 C  CD1 . ILE A 1 127 ? 14.009  36.208 95.752  1.00 11.86 ? 127  ILE A CD1 1 
ATOM   1075 N  N   . GLU A 1 128 ? 10.934  39.503 97.539  1.00 12.47 ? 128  GLU A N   1 
ATOM   1076 C  CA  . GLU A 1 128 ? 10.636  40.669 98.375  1.00 13.20 ? 128  GLU A CA  1 
ATOM   1077 C  C   . GLU A 1 128 ? 11.827  40.861 99.298  1.00 12.60 ? 128  GLU A C   1 
ATOM   1078 O  O   . GLU A 1 128 ? 12.068  40.066 100.204 1.00 15.34 ? 128  GLU A O   1 
ATOM   1079 C  CB  . GLU A 1 128 ? 9.336   40.475 99.165  1.00 15.72 ? 128  GLU A CB  1 
ATOM   1080 C  CG  . GLU A 1 128 ? 8.137   40.029 98.306  1.00 14.34 ? 128  GLU A CG  1 
ATOM   1081 C  CD  . GLU A 1 128 ? 6.802   40.020 99.038  1.00 28.72 ? 128  GLU A CD  1 
ATOM   1082 O  OE1 . GLU A 1 128 ? 6.791   40.039 100.287 1.00 26.51 ? 128  GLU A OE1 1 
ATOM   1083 O  OE2 . GLU A 1 128 ? 5.755   39.980 98.347  1.00 23.34 ? 128  GLU A OE2 1 
ATOM   1084 N  N   . GLU A 1 129 ? 12.581  41.909 99.037  1.00 13.03 ? 129  GLU A N   1 
ATOM   1085 C  CA  . GLU A 1 129 ? 13.748  42.242 99.829  1.00 10.03 ? 129  GLU A CA  1 
ATOM   1086 C  C   . GLU A 1 129 ? 13.330  42.702 101.232 1.00 17.56 ? 129  GLU A C   1 
ATOM   1087 O  O   . GLU A 1 129 ? 13.967  42.343 102.222 1.00 17.37 ? 129  GLU A O   1 
ATOM   1088 C  CB  . GLU A 1 129 ? 14.470  43.343 99.082  1.00 18.88 ? 129  GLU A CB  1 
ATOM   1089 C  CG  . GLU A 1 129 ? 15.562  44.033 99.787  1.00 25.08 ? 129  GLU A CG  1 
ATOM   1090 C  CD  . GLU A 1 129 ? 15.939  45.266 99.000  1.00 30.78 ? 129  GLU A CD  1 
ATOM   1091 O  OE1 . GLU A 1 129 ? 15.535  46.373 99.404  1.00 29.13 ? 129  GLU A OE1 1 
ATOM   1092 O  OE2 . GLU A 1 129 ? 16.571  45.111 97.937  1.00 26.26 ? 129  GLU A OE2 1 
ATOM   1093 N  N   . THR A 1 130 ? 12.266  43.504 101.285 1.00 14.72 ? 130  THR A N   1 
ATOM   1094 C  CA  . THR A 1 130 ? 11.506  43.775 102.504 1.00 17.91 ? 130  THR A CA  1 
ATOM   1095 C  C   . THR A 1 130 ? 10.037  43.787 102.088 1.00 21.08 ? 130  THR A C   1 
ATOM   1096 O  O   . THR A 1 130 ? 9.725   43.699 100.901 1.00 17.16 ? 130  THR A O   1 
ATOM   1097 C  CB  . THR A 1 130 ? 11.839  45.157 103.101 1.00 17.06 ? 130  THR A CB  1 
ATOM   1098 O  OG1 . THR A 1 130 ? 11.232  46.162 102.300 1.00 17.16 ? 130  THR A OG1 1 
ATOM   1099 C  CG2 . THR A 1 130 ? 13.371  45.395 103.162 1.00 16.85 ? 130  THR A CG2 1 
ATOM   1100 N  N   . PRO A 1 131 ? 9.129   43.876 103.060 1.00 17.94 ? 131  PRO A N   1 
ATOM   1101 C  CA  . PRO A 1 131 ? 7.705   43.942 102.718 1.00 26.07 ? 131  PRO A CA  1 
ATOM   1102 C  C   . PRO A 1 131 ? 7.334   45.112 101.814 1.00 20.11 ? 131  PRO A C   1 
ATOM   1103 O  O   . PRO A 1 131 ? 6.256   45.112 101.216 1.00 27.85 ? 131  PRO A O   1 
ATOM   1104 C  CB  . PRO A 1 131 ? 7.007   44.018 104.095 1.00 22.60 ? 131  PRO A CB  1 
ATOM   1105 C  CG  . PRO A 1 131 ? 8.010   43.314 105.035 1.00 20.75 ? 131  PRO A CG  1 
ATOM   1106 C  CD  . PRO A 1 131 ? 9.349   43.836 104.522 1.00 21.32 ? 131  PRO A CD  1 
ATOM   1107 N  N   . LYS A 1 132 ? 8.225   46.080 101.679 1.00 14.94 ? 132  LYS A N   1 
ATOM   1108 C  CA  . LYS A 1 132 ? 7.944   47.289 100.923 1.00 23.39 ? 132  LYS A CA  1 
ATOM   1109 C  C   . LYS A 1 132 ? 8.627   47.363 99.558  1.00 15.68 ? 132  LYS A C   1 
ATOM   1110 O  O   . LYS A 1 132 ? 8.315   48.265 98.777  1.00 15.03 ? 132  LYS A O   1 
ATOM   1111 C  CB  . LYS A 1 132 ? 8.348   48.534 101.717 1.00 29.86 ? 132  LYS A CB  1 
ATOM   1112 C  CG  . LYS A 1 132 ? 7.452   48.842 102.916 1.00 33.71 ? 132  LYS A CG  1 
ATOM   1113 C  CD  . LYS A 1 132 ? 8.157   49.774 103.903 1.00 40.39 ? 132  LYS A CD  1 
ATOM   1114 C  CE  . LYS A 1 132 ? 8.576   51.092 103.262 1.00 59.91 ? 132  LYS A CE  1 
ATOM   1115 N  NZ  . LYS A 1 132 ? 7.446   52.067 103.170 1.00 62.16 ? 132  LYS A NZ  1 
ATOM   1116 N  N   . ASN A 1 133 ? 9.562   46.448 99.288  1.00 14.72 ? 133  ASN A N   1 
ATOM   1117 C  CA  . ASN A 1 133 ? 10.406  46.501 98.081  1.00 12.09 ? 133  ASN A CA  1 
ATOM   1118 C  C   . ASN A 1 133 ? 10.337  45.132 97.403  1.00 12.59 ? 133  ASN A C   1 
ATOM   1119 O  O   . ASN A 1 133 ? 10.902  44.158 97.916  1.00 14.74 ? 133  ASN A O   1 
ATOM   1120 C  CB  . ASN A 1 133 ? 11.875  46.781 98.443  1.00 15.57 ? 133  ASN A CB  1 
ATOM   1121 C  CG  . ASN A 1 133 ? 12.091  48.158 99.056  1.00 28.00 ? 133  ASN A CG  1 
ATOM   1122 O  OD1 . ASN A 1 133 ? 11.502  49.138 98.621  1.00 21.98 ? 133  ASN A OD1 1 
ATOM   1123 N  ND2 . ASN A 1 133 ? 12.969  48.237 100.049 1.00 29.26 ? 133  ASN A ND2 1 
ATOM   1124 N  N   . ILE A 1 134 ? 9.639   45.066 96.269  1.00 10.89 ? 134  ILE A N   1 
ATOM   1125 C  CA  A ILE A 1 134 ? 9.271   43.797 95.637  0.50 11.38 ? 134  ILE A CA  1 
ATOM   1126 C  CA  B ILE A 1 134 ? 9.312   43.787 95.642  0.50 8.99  ? 134  ILE A CA  1 
ATOM   1127 C  C   . ILE A 1 134 ? 9.780   43.756 94.192  1.00 13.49 ? 134  ILE A C   1 
ATOM   1128 O  O   . ILE A 1 134 ? 9.556   44.701 93.435  1.00 15.93 ? 134  ILE A O   1 
ATOM   1129 C  CB  A ILE A 1 134 ? 7.731   43.633 95.634  0.50 13.86 ? 134  ILE A CB  1 
ATOM   1130 C  CB  B ILE A 1 134 ? 7.798   43.526 95.698  0.50 12.74 ? 134  ILE A CB  1 
ATOM   1131 C  CG1 A ILE A 1 134 ? 7.184   43.636 97.068  0.50 29.79 ? 134  ILE A CG1 1 
ATOM   1132 C  CG1 B ILE A 1 134 ? 7.328   43.497 97.154  0.50 5.89  ? 134  ILE A CG1 1 
ATOM   1133 C  CG2 A ILE A 1 134 ? 7.317   42.351 94.915  0.50 18.84 ? 134  ILE A CG2 1 
ATOM   1134 C  CG2 B ILE A 1 134 ? 7.443   42.207 95.012  0.50 9.64  ? 134  ILE A CG2 1 
ATOM   1135 C  CD1 A ILE A 1 134 ? 6.649   44.985 97.542  0.50 8.15  ? 134  ILE A CD1 1 
ATOM   1136 C  CD1 B ILE A 1 134 ? 5.951   44.103 97.357  0.50 23.09 ? 134  ILE A CD1 1 
ATOM   1137 N  N   . PHE A 1 135 ? 10.421  42.648 93.811  1.00 12.90 ? 135  PHE A N   1 
ATOM   1138 C  CA  . PHE A 1 135 ? 10.990  42.490 92.453  1.00 13.94 ? 135  PHE A CA  1 
ATOM   1139 C  C   . PHE A 1 135 ? 10.508  41.221 91.766  1.00 15.33 ? 135  PHE A C   1 
ATOM   1140 O  O   . PHE A 1 135 ? 10.364  40.171 92.418  1.00 12.68 ? 135  PHE A O   1 
ATOM   1141 C  CB  . PHE A 1 135 ? 12.515  42.470 92.547  1.00 12.35 ? 135  PHE A CB  1 
ATOM   1142 C  CG  . PHE A 1 135 ? 13.056  43.663 93.275  1.00 17.26 ? 135  PHE A CG  1 
ATOM   1143 C  CD1 . PHE A 1 135 ? 13.530  44.756 92.572  1.00 16.10 ? 135  PHE A CD1 1 
ATOM   1144 C  CD2 . PHE A 1 135 ? 13.018  43.715 94.670  1.00 14.58 ? 135  PHE A CD2 1 
ATOM   1145 C  CE1 . PHE A 1 135 ? 13.989  45.898 93.238  1.00 16.08 ? 135  PHE A CE1 1 
ATOM   1146 C  CE2 . PHE A 1 135 ? 13.474  44.865 95.347  1.00 15.92 ? 135  PHE A CE2 1 
ATOM   1147 C  CZ  . PHE A 1 135 ? 13.959  45.947 94.621  1.00 13.68 ? 135  PHE A CZ  1 
ATOM   1148 N  N   . THR A 1 136 ? 10.282  41.299 90.448  1.00 10.12 ? 136  THR A N   1 
ATOM   1149 C  CA  . THR A 1 136 ? 9.865   40.098 89.731  1.00 10.81 ? 136  THR A CA  1 
ATOM   1150 C  C   . THR A 1 136 ? 10.623  39.956 88.433  1.00 15.50 ? 136  THR A C   1 
ATOM   1151 O  O   . THR A 1 136 ? 11.115  40.943 87.858  1.00 14.82 ? 136  THR A O   1 
ATOM   1152 C  CB  . THR A 1 136 ? 8.349   40.041 89.458  1.00 14.80 ? 136  THR A CB  1 
ATOM   1153 O  OG1 . THR A 1 136 ? 8.018   40.836 88.312  1.00 14.21 ? 136  THR A OG1 1 
ATOM   1154 C  CG2 . THR A 1 136 ? 7.526   40.481 90.713  1.00 14.50 ? 136  THR A CG2 1 
ATOM   1155 N  N   . TYR A 1 137 ? 10.702  38.723 87.979  1.00 12.63 ? 137  TYR A N   1 
ATOM   1156 C  CA  . TYR A 1 137 ? 11.478  38.408 86.779  1.00 15.29 ? 137  TYR A CA  1 
ATOM   1157 C  C   . TYR A 1 137 ? 10.798  37.226 86.108  1.00 14.73 ? 137  TYR A C   1 
ATOM   1158 O  O   . TYR A 1 137 ? 10.384  36.280 86.789  1.00 15.84 ? 137  TYR A O   1 
ATOM   1159 C  CB  . TYR A 1 137 ? 12.909  38.054 87.147  1.00 11.34 ? 137  TYR A CB  1 
ATOM   1160 C  CG  . TYR A 1 137 ? 13.767  37.700 85.953  1.00 13.27 ? 137  TYR A CG  1 
ATOM   1161 C  CD1 . TYR A 1 137 ? 13.936  38.597 84.909  1.00 13.30 ? 137  TYR A CD1 1 
ATOM   1162 C  CD2 . TYR A 1 137 ? 14.400  36.457 85.877  1.00 21.05 ? 137  TYR A CD2 1 
ATOM   1163 C  CE1 . TYR A 1 137 ? 14.733  38.259 83.798  1.00 16.28 ? 137  TYR A CE1 1 
ATOM   1164 C  CE2 . TYR A 1 137 ? 15.186  36.118 84.799  1.00 17.12 ? 137  TYR A CE2 1 
ATOM   1165 C  CZ  . TYR A 1 137 ? 15.358  37.029 83.771  1.00 19.60 ? 137  TYR A CZ  1 
ATOM   1166 O  OH  . TYR A 1 137 ? 16.150  36.698 82.709  1.00 26.94 ? 137  TYR A OH  1 
ATOM   1167 N  N   . LYS A 1 138 ? 10.651  37.315 84.785  1.00 12.68 ? 138  LYS A N   1 
ATOM   1168 C  CA  . LYS A 1 138 ? 10.005  36.255 83.999  1.00 14.28 ? 138  LYS A CA  1 
ATOM   1169 C  C   . LYS A 1 138 ? 10.915  35.576 82.976  1.00 23.53 ? 138  LYS A C   1 
ATOM   1170 O  O   . LYS A 1 138 ? 10.451  34.798 82.126  1.00 18.80 ? 138  LYS A O   1 
ATOM   1171 C  CB  . LYS A 1 138 ? 8.755   36.775 83.286  1.00 20.24 ? 138  LYS A CB  1 
ATOM   1172 C  CG  . LYS A 1 138 ? 7.593   37.121 84.207  1.00 21.74 ? 138  LYS A CG  1 
ATOM   1173 C  CD  . LYS A 1 138 ? 6.509   37.830 83.388  1.00 26.50 ? 138  LYS A CD  1 
ATOM   1174 C  CE  . LYS A 1 138 ? 5.206   37.929 84.130  1.00 39.18 ? 138  LYS A CE  1 
ATOM   1175 N  NZ  . LYS A 1 138 ? 4.079   38.224 83.167  1.00 33.52 ? 138  LYS A NZ  1 
ATOM   1176 N  N   . GLY A 1 139 ? 12.203  35.854 83.064  1.00 17.01 ? 139  GLY A N   1 
ATOM   1177 C  CA  . GLY A 1 139 ? 13.181  35.169 82.215  1.00 21.01 ? 139  GLY A CA  1 
ATOM   1178 C  C   . GLY A 1 139 ? 13.362  35.904 80.898  1.00 41.74 ? 139  GLY A C   1 
ATOM   1179 O  O   . GLY A 1 139 ? 12.851  37.009 80.714  1.00 30.13 ? 139  GLY A O   1 
ATOM   1180 N  N   . SER A 1 140 ? 14.093  35.281 79.980  1.00 34.44 ? 140  SER A N   1 
ATOM   1181 C  CA  . SER A 1 140 ? 14.239  35.797 78.622  1.00 63.60 ? 140  SER A CA  1 
ATOM   1182 C  C   . SER A 1 140 ? 12.992  35.502 77.789  1.00 67.79 ? 140  SER A C   1 
ATOM   1183 O  O   . SER A 1 140 ? 12.028  34.890 78.258  1.00 89.58 ? 140  SER A O   1 
ATOM   1184 C  CB  . SER A 1 140 ? 15.468  35.179 77.948  1.00 64.08 ? 140  SER A CB  1 
ATOM   1185 O  OG  . SER A 1 140 ? 16.666  35.609 78.572  1.00 89.29 ? 140  SER A OG  1 
ATOM   1186 O  OXT . SER A 1 140 ? 12.922  35.862 76.616  1.00 75.81 ? 140  SER A OXT 1 
HETATM 1187 NA NA  . NA  B 2 .   ? 10.802  40.605 102.906 1.00 29.42 ? 1001 NA  A NA  1 
HETATM 1188 NA NA  . NA  C 2 .   ? 26.102  46.900 103.213 1.00 30.42 ? 1002 NA  A NA  1 
HETATM 1189 ZN ZN  . ZN  D 3 .   ? 20.059  45.146 101.061 0.80 19.71 ? 2001 ZN  A ZN  1 
HETATM 1190 C  C1  . GOL E 4 .   ? 1.591   37.461 87.567  1.00 29.28 ? 3001 GOL A C1  1 
HETATM 1191 O  O1  . GOL E 4 .   ? 2.662   36.728 88.042  1.00 29.91 ? 3001 GOL A O1  1 
HETATM 1192 C  C2  . GOL E 4 .   ? 1.967   37.985 86.222  1.00 27.22 ? 3001 GOL A C2  1 
HETATM 1193 O  O2  . GOL E 4 .   ? 1.107   37.352 85.311  1.00 47.61 ? 3001 GOL A O2  1 
HETATM 1194 C  C3  . GOL E 4 .   ? 1.746   39.485 86.278  1.00 66.65 ? 3001 GOL A C3  1 
HETATM 1195 O  O3  . GOL E 4 .   ? 2.944   40.210 86.112  1.00 38.37 ? 3001 GOL A O3  1 
HETATM 1196 O  O   . HOH F 5 .   ? -0.611  31.552 91.197  1.00 16.00 ? 3002 HOH A O   1 
HETATM 1197 O  O   . HOH F 5 .   ? 28.258  41.302 94.767  1.00 17.24 ? 3003 HOH A O   1 
HETATM 1198 O  O   . HOH F 5 .   ? -8.380  17.347 87.429  1.00 14.97 ? 3004 HOH A O   1 
HETATM 1199 O  O   . HOH F 5 .   ? -0.017  33.989 92.162  1.00 17.51 ? 3005 HOH A O   1 
HETATM 1200 O  O   . HOH F 5 .   ? 19.395  42.016 97.453  1.00 14.52 ? 3006 HOH A O   1 
HETATM 1201 O  O   . HOH F 5 .   ? -9.730  22.487 74.883  1.00 16.39 ? 3007 HOH A O   1 
HETATM 1202 O  O   . HOH F 5 .   ? 27.828  36.556 87.939  1.00 18.02 ? 3008 HOH A O   1 
HETATM 1203 O  O   . HOH F 5 .   ? 26.942  30.731 92.219  1.00 18.22 ? 3009 HOH A O   1 
HETATM 1204 O  O   . HOH F 5 .   ? 6.271   34.880 91.680  1.00 15.19 ? 3010 HOH A O   1 
HETATM 1205 O  O   . HOH F 5 .   ? 28.941  40.907 101.484 1.00 17.16 ? 3011 HOH A O   1 
HETATM 1206 O  O   . HOH F 5 .   ? 1.074   22.094 83.859  1.00 19.15 ? 3012 HOH A O   1 
HETATM 1207 O  O   . HOH F 5 .   ? 2.910   36.748 92.233  1.00 26.56 ? 3013 HOH A O   1 
HETATM 1208 O  O   . HOH F 5 .   ? 34.220  40.962 90.103  1.00 24.17 ? 3014 HOH A O   1 
HETATM 1209 O  O   . HOH F 5 .   ? 7.812   33.629 81.983  1.00 21.11 ? 3015 HOH A O   1 
HETATM 1210 O  O   . HOH F 5 .   ? 4.576   38.609 92.634  1.00 22.57 ? 3016 HOH A O   1 
HETATM 1211 O  O   . HOH F 5 .   ? 27.120  43.725 95.522  1.00 17.24 ? 3017 HOH A O   1 
HETATM 1212 O  O   . HOH F 5 .   ? 31.266  34.836 89.591  1.00 23.62 ? 3018 HOH A O   1 
HETATM 1213 O  O   . HOH F 5 .   ? 8.176   40.701 102.550 1.00 22.09 ? 3019 HOH A O   1 
HETATM 1214 O  O   . HOH F 5 .   ? 30.684  48.805 108.147 1.00 23.26 ? 3020 HOH A O   1 
HETATM 1215 O  O   . HOH F 5 .   ? 27.736  53.355 102.997 1.00 29.83 ? 3021 HOH A O   1 
HETATM 1216 O  O   . HOH F 5 .   ? 31.606  41.190 86.377  1.00 18.70 ? 3022 HOH A O   1 
HETATM 1217 O  O   . HOH F 5 .   ? -7.047  25.893 77.802  1.00 24.22 ? 3023 HOH A O   1 
HETATM 1218 O  O   . HOH F 5 .   ? 21.478  38.587 87.729  1.00 19.38 ? 3024 HOH A O   1 
HETATM 1219 O  O   . HOH F 5 .   ? 29.638  43.207 98.172  1.00 21.19 ? 3025 HOH A O   1 
HETATM 1220 O  O   . HOH F 5 .   ? 21.971  23.213 96.139  1.00 26.53 ? 3026 HOH A O   1 
HETATM 1221 O  O   . HOH F 5 .   ? -9.091  25.184 75.734  1.00 23.51 ? 3027 HOH A O   1 
HETATM 1222 O  O   . HOH F 5 .   ? 26.196  28.960 98.432  1.00 29.66 ? 3028 HOH A O   1 
HETATM 1223 O  O   . HOH F 5 .   ? 1.027   23.195 80.214  1.00 25.23 ? 3029 HOH A O   1 
HETATM 1224 O  O   . HOH F 5 .   ? 29.195  45.169 84.145  1.00 25.26 ? 3030 HOH A O   1 
HETATM 1225 O  O   . HOH F 5 .   ? -3.691  18.604 76.772  1.00 25.66 ? 3031 HOH A O   1 
HETATM 1226 O  O   . HOH F 5 .   ? -10.022 23.272 78.699  1.00 25.55 ? 3032 HOH A O   1 
HETATM 1227 O  O   . HOH F 5 .   ? 38.709  54.892 98.964  1.00 25.28 ? 3033 HOH A O   1 
HETATM 1228 O  O   . HOH F 5 .   ? 22.160  27.200 103.250 1.00 25.10 ? 3034 HOH A O   1 
HETATM 1229 O  O   . HOH F 5 .   ? -12.501 23.068 74.917  1.00 17.27 ? 3035 HOH A O   1 
HETATM 1230 O  O   . HOH F 5 .   ? 9.911   38.530 105.589 1.00 20.67 ? 3036 HOH A O   1 
HETATM 1231 O  O   . HOH F 5 .   ? 31.251  41.805 100.084 1.00 24.52 ? 3037 HOH A O   1 
HETATM 1232 O  O   . HOH F 5 .   ? 15.924  19.222 97.808  1.00 27.14 ? 3038 HOH A O   1 
HETATM 1233 O  O   . HOH F 5 .   ? -8.225  11.465 83.845  1.00 23.98 ? 3039 HOH A O   1 
HETATM 1234 O  O   . HOH F 5 .   ? -7.474  28.311 80.322  1.00 22.83 ? 3040 HOH A O   1 
HETATM 1235 O  O   . HOH F 5 .   ? 17.723  20.628 99.757  1.00 28.52 ? 3041 HOH A O   1 
HETATM 1236 O  O   . HOH F 5 .   ? 32.819  52.284 98.599  1.00 22.52 ? 3042 HOH A O   1 
HETATM 1237 O  O   . HOH F 5 .   ? -1.092  12.375 85.896  1.00 36.74 ? 3043 HOH A O   1 
HETATM 1238 O  O   . HOH F 5 .   ? -1.639  21.062 74.958  1.00 23.55 ? 3044 HOH A O   1 
HETATM 1239 O  O   . HOH F 5 .   ? 33.749  40.246 94.043  1.00 26.52 ? 3045 HOH A O   1 
HETATM 1240 O  O   . HOH F 5 .   ? 0.495   15.830 88.204  1.00 31.01 ? 3046 HOH A O   1 
HETATM 1241 O  O   . HOH F 5 .   ? 4.621   39.957 95.987  1.00 29.03 ? 3047 HOH A O   1 
HETATM 1242 O  O   . HOH F 5 .   ? 11.025  23.827 99.708  1.00 31.30 ? 3048 HOH A O   1 
HETATM 1243 O  O   . HOH F 5 .   ? 11.277  39.077 82.649  1.00 28.16 ? 3049 HOH A O   1 
HETATM 1244 O  O   . HOH F 5 .   ? 26.937  52.594 105.441 1.00 29.77 ? 3050 HOH A O   1 
HETATM 1245 O  O   . HOH F 5 .   ? 7.369   39.122 104.875 1.00 24.39 ? 3051 HOH A O   1 
HETATM 1246 O  O   . HOH F 5 .   ? 33.440  42.647 87.932  1.00 26.08 ? 3052 HOH A O   1 
HETATM 1247 O  O   . HOH F 5 .   ? 21.795  21.268 98.298  1.00 30.85 ? 3053 HOH A O   1 
HETATM 1248 O  O   . HOH F 5 .   ? 25.109  28.944 93.741  1.00 23.59 ? 3054 HOH A O   1 
HETATM 1249 O  O   . HOH F 5 .   ? 31.438  42.795 104.417 1.00 32.70 ? 3055 HOH A O   1 
HETATM 1250 O  O   . HOH F 5 .   ? 30.876  59.688 97.762  1.00 30.87 ? 3056 HOH A O   1 
HETATM 1251 O  O   . HOH F 5 .   ? 29.060  41.860 103.959 1.00 23.37 ? 3057 HOH A O   1 
HETATM 1252 O  O   . HOH F 5 .   ? 33.208  31.306 98.606  1.00 40.78 ? 3058 HOH A O   1 
HETATM 1253 O  O   . HOH F 5 .   ? -6.781  16.249 78.508  1.00 29.36 ? 3059 HOH A O   1 
HETATM 1254 O  O   . HOH F 5 .   ? 30.810  44.079 80.760  1.00 26.16 ? 3060 HOH A O   1 
HETATM 1255 O  O   . HOH F 5 .   ? 32.902  58.887 99.169  1.00 32.07 ? 3061 HOH A O   1 
HETATM 1256 O  O   . HOH F 5 .   ? 10.462  35.893 105.586 1.00 26.56 ? 3062 HOH A O   1 
HETATM 1257 O  O   . HOH F 5 .   ? 35.869  43.604 86.808  1.00 29.35 ? 3063 HOH A O   1 
HETATM 1258 O  O   . HOH F 5 .   ? 28.862  29.201 95.149  1.00 23.49 ? 3064 HOH A O   1 
HETATM 1259 O  O   . HOH F 5 .   ? 36.295  58.125 92.529  1.00 26.34 ? 3065 HOH A O   1 
HETATM 1260 O  O   . HOH F 5 .   ? 5.876   39.807 106.801 0.50 19.31 ? 3066 HOH A O   1 
HETATM 1261 O  O   . HOH F 5 .   ? 2.520   29.893 80.370  1.00 32.29 ? 3067 HOH A O   1 
HETATM 1262 O  O   . HOH F 5 .   ? 16.255  49.216 92.907  1.00 31.08 ? 3068 HOH A O   1 
HETATM 1263 O  O   . HOH F 5 .   ? 33.200  40.573 98.808  1.00 26.85 ? 3069 HOH A O   1 
HETATM 1264 O  O   . HOH F 5 .   ? 4.426   28.882 81.742  1.00 28.89 ? 3070 HOH A O   1 
HETATM 1265 O  O   . HOH F 5 .   ? 33.127  42.580 95.336  1.00 34.01 ? 3071 HOH A O   1 
HETATM 1266 O  O   . HOH F 5 .   ? 25.210  28.941 106.644 1.00 30.47 ? 3072 HOH A O   1 
HETATM 1267 O  O   . HOH F 5 .   ? -13.999 23.178 77.174  1.00 31.74 ? 3073 HOH A O   1 
HETATM 1268 O  O   . HOH F 5 .   ? 34.520  56.576 99.285  1.00 29.99 ? 3074 HOH A O   1 
HETATM 1269 O  O   . HOH F 5 .   ? 5.078   17.901 88.288  1.00 31.02 ? 3075 HOH A O   1 
HETATM 1270 O  O   . HOH F 5 .   ? 30.560  43.062 95.661  1.00 23.51 ? 3076 HOH A O   1 
HETATM 1271 O  O   . HOH F 5 .   ? 32.379  38.468 106.351 1.00 36.16 ? 3077 HOH A O   1 
HETATM 1272 O  O   . HOH F 5 .   ? 1.330   35.955 95.752  1.00 27.39 ? 3078 HOH A O   1 
HETATM 1273 O  O   . HOH F 5 .   ? 30.424  52.947 102.195 1.00 29.37 ? 3079 HOH A O   1 
HETATM 1274 O  O   . HOH F 5 .   ? 11.724  48.681 103.024 1.00 34.71 ? 3080 HOH A O   1 
HETATM 1275 O  O   . HOH F 5 .   ? 8.293   34.764 105.128 1.00 28.23 ? 3081 HOH A O   1 
HETATM 1276 O  O   . HOH F 5 .   ? 15.198  28.640 103.180 1.00 29.58 ? 3082 HOH A O   1 
HETATM 1277 O  O   . HOH F 5 .   ? 18.912  27.991 84.192  1.00 34.62 ? 3083 HOH A O   1 
HETATM 1278 O  O   . HOH F 5 .   ? 18.677  33.167 111.935 1.00 31.89 ? 3084 HOH A O   1 
HETATM 1279 O  O   . HOH F 5 .   ? 6.776   29.436 81.110  1.00 27.27 ? 3085 HOH A O   1 
HETATM 1280 O  O   . HOH F 5 .   ? 8.970   25.489 99.198  1.00 38.10 ? 3086 HOH A O   1 
HETATM 1281 O  O   . HOH F 5 .   ? 8.391   40.302 85.479  1.00 28.21 ? 3087 HOH A O   1 
HETATM 1282 O  O   . HOH F 5 .   ? 6.377   36.732 104.561 1.00 36.10 ? 3088 HOH A O   1 
HETATM 1283 O  O   . HOH F 5 .   ? 10.465  21.184 80.416  1.00 40.74 ? 3089 HOH A O   1 
HETATM 1284 O  O   . HOH F 5 .   ? -3.394  13.533 80.002  1.00 32.26 ? 3090 HOH A O   1 
HETATM 1285 O  O   . HOH F 5 .   ? 0.826   19.402 94.076  1.00 29.09 ? 3091 HOH A O   1 
HETATM 1286 O  O   . HOH F 5 .   ? 32.966  43.751 100.969 1.00 35.45 ? 3092 HOH A O   1 
HETATM 1287 O  O   . HOH F 5 .   ? 11.931  34.471 107.071 1.00 29.54 ? 3093 HOH A O   1 
HETATM 1288 O  O   . HOH F 5 .   ? -3.098  18.357 80.818  1.00 27.26 ? 3094 HOH A O   1 
HETATM 1289 O  O   . HOH F 5 .   ? -9.759  25.718 78.347  1.00 42.03 ? 3095 HOH A O   1 
HETATM 1290 O  O   . HOH F 5 .   ? -4.022  31.216 84.194  1.00 43.80 ? 3096 HOH A O   1 
HETATM 1291 O  O   . HOH F 5 .   ? 14.327  33.866 106.486 1.00 41.56 ? 3097 HOH A O   1 
HETATM 1292 O  O   . HOH F 5 .   ? 35.370  50.314 94.308  1.00 41.83 ? 3098 HOH A O   1 
HETATM 1293 O  O   . HOH F 5 .   ? 28.883  58.909 91.301  1.00 36.34 ? 3099 HOH A O   1 
HETATM 1294 O  O   . HOH F 5 .   ? -10.068 27.407 80.145  1.00 36.89 ? 3100 HOH A O   1 
HETATM 1295 O  O   . HOH F 5 .   ? -1.893  33.968 83.473  1.00 46.61 ? 3101 HOH A O   1 
HETATM 1296 O  O   . HOH F 5 .   ? 7.561   33.080 103.324 1.00 40.07 ? 3102 HOH A O   1 
HETATM 1297 O  O   . HOH F 5 .   ? 8.103   33.425 107.447 1.00 37.35 ? 3103 HOH A O   1 
HETATM 1298 O  O   . HOH F 5 .   ? 39.860  51.122 97.933  1.00 28.63 ? 3104 HOH A O   1 
HETATM 1299 O  O   . HOH F 5 .   ? 36.964  49.006 97.894  1.00 45.45 ? 3105 HOH A O   1 
HETATM 1300 O  O   . HOH F 5 .   ? 38.095  47.641 96.232  1.00 50.99 ? 3106 HOH A O   1 
HETATM 1301 O  O   . HOH F 5 .   ? 36.300  47.487 94.207  1.00 47.35 ? 3107 HOH A O   1 
HETATM 1302 O  O   . HOH F 5 .   ? 6.987   31.765 80.341  1.00 40.38 ? 3108 HOH A O   1 
HETATM 1303 O  O   . HOH F 5 .   ? 2.421   15.661 95.890  1.00 55.15 ? 3109 HOH A O   1 
HETATM 1304 O  O   . HOH F 5 .   ? 3.984   18.796 99.310  1.00 44.23 ? 3110 HOH A O   1 
HETATM 1305 O  O   . HOH F 5 .   ? 26.489  28.213 95.799  1.00 34.26 ? 3111 HOH A O   1 
HETATM 1306 O  O   . HOH F 5 .   ? 28.523  29.582 103.548 1.00 50.52 ? 3112 HOH A O   1 
HETATM 1307 O  O   . HOH F 5 .   ? 14.374  49.226 95.502  1.00 34.16 ? 3113 HOH A O   1 
HETATM 1308 O  O   . HOH F 5 .   ? 17.942  47.140 94.338  1.00 39.11 ? 3114 HOH A O   1 
HETATM 1309 O  O   . HOH F 5 .   ? 22.024  28.564 87.490  1.00 36.76 ? 3115 HOH A O   1 
HETATM 1310 O  O   . HOH F 5 .   ? -1.956  35.540 87.910  1.00 26.16 ? 3116 HOH A O   1 
HETATM 1311 O  O   . HOH F 5 .   ? 11.254  40.753 105.642 1.00 35.15 ? 3117 HOH A O   1 
HETATM 1312 O  O   . HOH F 5 .   ? 19.685  26.016 104.094 1.00 57.35 ? 3118 HOH A O   1 
HETATM 1313 O  O   . HOH F 5 .   ? 15.041  24.402 102.257 1.00 46.45 ? 3119 HOH A O   1 
HETATM 1314 O  O   . HOH F 5 .   ? 33.650  34.161 90.094  1.00 37.42 ? 3120 HOH A O   1 
HETATM 1315 O  O   . HOH F 5 .   ? 0.540   38.634 83.025  1.00 49.46 ? 3121 HOH A O   1 
HETATM 1316 O  O   . HOH F 5 .   ? 4.876   42.688 100.564 1.00 42.48 ? 3122 HOH A O   1 
HETATM 1317 O  O   . HOH F 5 .   ? 9.145   17.205 98.664  1.00 38.25 ? 3123 HOH A O   1 
HETATM 1318 O  O   . HOH F 5 .   ? 21.345  55.433 101.859 1.00 35.03 ? 3124 HOH A O   1 
HETATM 1319 O  O   . HOH F 5 .   ? 32.126  30.881 101.543 1.00 37.62 ? 3125 HOH A O   1 
HETATM 1320 O  O   . HOH F 5 .   ? 8.831   28.554 79.370  1.00 49.92 ? 3126 HOH A O   1 
HETATM 1321 O  O   . HOH F 5 .   ? 31.109  29.444 96.791  1.00 48.25 ? 3127 HOH A O   1 
HETATM 1322 O  O   . HOH F 5 .   ? 27.226  41.528 105.739 1.00 33.57 ? 3128 HOH A O   1 
HETATM 1323 O  O   . HOH F 5 .   ? 1.052   18.062 86.995  1.00 34.79 ? 3129 HOH A O   1 
HETATM 1324 O  O   . HOH F 5 .   ? 12.987  17.111 90.975  1.00 36.98 ? 3130 HOH A O   1 
HETATM 1325 O  O   . HOH F 5 .   ? 15.697  30.590 107.060 1.00 37.93 ? 3131 HOH A O   1 
HETATM 1326 O  O   . HOH F 5 .   ? 18.080  35.031 82.883  1.00 38.04 ? 3132 HOH A O   1 
HETATM 1327 O  O   . HOH F 5 .   ? 9.156   30.693 104.647 1.00 47.22 ? 3133 HOH A O   1 
HETATM 1328 O  O   . HOH F 5 .   ? 4.707   38.377 101.329 1.00 34.07 ? 3134 HOH A O   1 
HETATM 1329 O  O   . HOH F 5 .   ? 24.270  58.118 98.199  1.00 35.67 ? 3135 HOH A O   1 
HETATM 1330 O  O   . HOH F 5 .   ? 22.125  23.898 88.947  1.00 40.63 ? 3136 HOH A O   1 
HETATM 1331 O  O   . HOH F 5 .   ? 30.935  51.452 105.301 1.00 36.04 ? 3137 HOH A O   1 
HETATM 1332 O  O   . HOH F 5 .   ? 4.813   40.582 81.747  1.00 51.37 ? 3138 HOH A O   1 
HETATM 1333 O  O   . HOH F 5 .   ? 19.701  46.357 99.741  1.00 26.05 ? 3139 HOH A O   1 
HETATM 1334 O  O   . HOH F 5 .   ? 34.586  45.739 103.662 1.00 53.25 ? 3140 HOH A O   1 
HETATM 1335 O  O   . HOH F 5 .   ? 35.432  43.581 109.556 1.00 49.92 ? 3141 HOH A O   1 
HETATM 1336 O  O   . HOH F 5 .   ? 21.627  31.274 88.554  1.00 34.25 ? 3142 HOH A O   1 
HETATM 1337 O  O   . HOH F 5 .   ? 1.755   14.019 92.672  1.00 31.47 ? 3143 HOH A O   1 
HETATM 1338 O  O   . HOH F 5 .   ? 32.866  38.757 96.768  1.00 29.29 ? 3144 HOH A O   1 
HETATM 1339 O  O   . HOH F 5 .   ? 16.028  47.663 101.623 1.00 32.52 ? 3145 HOH A O   1 
HETATM 1340 O  O   . HOH F 5 .   ? 15.954  32.647 109.438 1.00 39.99 ? 3146 HOH A O   1 
HETATM 1341 O  O   . HOH F 5 .   ? 35.000  46.533 110.874 1.00 35.44 ? 3147 HOH A O   1 
HETATM 1342 O  O   . HOH F 5 .   ? 24.922  26.587 92.334  1.00 41.18 ? 3148 HOH A O   1 
HETATM 1343 O  O   . HOH F 5 .   ? 3.879   19.742 85.283  1.00 44.05 ? 3149 HOH A O   1 
HETATM 1344 O  O   . HOH F 5 .   ? 3.143   25.430 80.786  1.00 44.22 ? 3150 HOH A O   1 
HETATM 1345 O  O   . HOH F 5 .   ? 11.509  49.273 95.797  1.00 31.72 ? 3151 HOH A O   1 
HETATM 1346 O  O   . HOH F 5 .   ? 4.068   46.418 102.743 1.00 37.17 ? 3152 HOH A O   1 
HETATM 1347 O  O   . HOH F 5 .   ? 34.699  50.539 99.795  1.00 34.97 ? 3153 HOH A O   1 
HETATM 1348 O  O   . HOH F 5 .   ? 3.438   36.178 100.332 1.00 37.98 ? 3154 HOH A O   1 
HETATM 1349 O  O   . HOH F 5 .   ? 34.979  46.626 107.000 1.00 37.72 ? 3155 HOH A O   1 
HETATM 1350 O  O   . HOH F 5 .   ? 10.120  47.680 105.058 1.00 37.36 ? 3156 HOH A O   1 
HETATM 1351 O  O   . HOH F 5 .   ? 15.458  32.568 80.996  1.00 55.65 ? 3157 HOH A O   1 
HETATM 1352 O  O   . HOH F 5 .   ? 12.388  24.948 101.837 1.00 34.86 ? 3158 HOH A O   1 
HETATM 1353 O  O   . HOH F 5 .   ? -2.564  13.159 82.300  1.00 47.72 ? 3159 HOH A O   1 
HETATM 1354 O  O   . HOH F 5 .   ? 17.853  19.889 84.652  1.00 51.59 ? 3160 HOH A O   1 
HETATM 1355 O  O   . HOH F 5 .   ? 26.202  58.443 100.054 1.00 43.61 ? 3161 HOH A O   1 
HETATM 1356 O  O   . HOH F 5 .   ? 2.100   22.970 101.746 1.00 46.94 ? 3162 HOH A O   1 
HETATM 1357 O  O   . HOH F 5 .   ? 4.521   23.479 79.983  1.00 51.28 ? 3163 HOH A O   1 
HETATM 1358 O  O   . HOH F 5 .   ? 13.595  31.385 106.037 1.00 54.46 ? 3164 HOH A O   1 
HETATM 1359 O  O   . HOH F 5 .   ? 11.272  39.101 79.665  1.00 68.33 ? 3165 HOH A O   1 
HETATM 1360 O  O   . HOH F 5 .   ? 1.093   35.833 98.570  1.00 43.18 ? 3166 HOH A O   1 
HETATM 1361 O  O   . HOH F 5 .   ? 12.275  31.151 81.128  1.00 44.32 ? 3167 HOH A O   1 
HETATM 1362 O  O   . HOH F 5 .   ? 18.853  45.448 96.739  1.00 34.79 ? 3168 HOH A 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   MET 1   1   1   MET MET A . n 
A 1 2   PHE 2   2   2   PHE PHE A . n 
A 1 3   ARG 3   3   3   ARG ARG A . n 
A 1 4   MET 4   4   4   MET MET A . n 
A 1 5   PRO 5   5   5   PRO PRO A . n 
A 1 6   ILE 6   6   6   ILE ILE A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   THR 8   8   8   THR THR A . n 
A 1 9   MET 9   9   9   MET MET A . n 
A 1 10  GLU 10  10  10  GLU GLU A . n 
A 1 11  ARG 11  11  11  ARG ARG A . n 
A 1 12  VAL 12  12  12  VAL VAL A . n 
A 1 13  ASP 13  13  13  ASP ASP A . n 
A 1 14  SER 14  14  14  SER SER A . n 
A 1 15  PHE 15  15  15  PHE PHE A . n 
A 1 16  SER 16  16  16  SER SER A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  ALA 18  18  18  ALA ALA A . n 
A 1 19  HIS 19  19  19  HIS HIS A . n 
A 1 20  ARG 20  20  20  ARG ARG A . n 
A 1 21  LEU 21  21  21  LEU LEU A . n 
A 1 22  HIS 22  22  22  HIS HIS A . n 
A 1 23  SER 23  23  23  SER SER A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  LYS 25  25  25  LYS LYS A . n 
A 1 26  LEU 26  26  26  LEU LEU A . n 
A 1 27  SER 27  27  27  SER SER A . n 
A 1 28  ASP 28  28  28  ASP ASP A . n 
A 1 29  ALA 29  29  29  ALA ALA A . n 
A 1 30  GLU 30  30  30  GLU GLU A . n 
A 1 31  ASN 31  31  31  ASN ASN A . n 
A 1 32  LYS 32  32  32  LYS LYS A . n 
A 1 33  GLU 33  33  33  GLU GLU A . n 
A 1 34  THR 34  34  34  THR THR A . n 
A 1 35  PHE 35  35  35  PHE PHE A . n 
A 1 36  GLY 36  36  36  GLY GLY A . n 
A 1 37  LYS 37  37  37  LYS LYS A . n 
A 1 38  CYS 38  38  38  CYS CYS A . n 
A 1 39  ASN 39  39  39  ASN ASN A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  SER 41  41  41  SER SER A . n 
A 1 42  ASN 42  42  42  ASN ASN A . n 
A 1 43  GLY 43  43  43  GLY GLY A . n 
A 1 44  HIS 44  44  44  HIS HIS A . n 
A 1 45  GLY 45  45  45  GLY GLY A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  ASN 47  47  47  ASN ASN A . n 
A 1 48  TYR 48  48  48  TYR TYR A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  TRP 50  50  50  TRP TRP A . n 
A 1 51  LYS 51  51  51  LYS LYS A . n 
A 1 52  VAL 52  52  52  VAL VAL A . n 
A 1 53  LYS 53  53  53  LYS LYS A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  ARG 55  55  55  ARG ARG A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  VAL 58  58  58  VAL VAL A . n 
A 1 59  ASP 59  59  59  ASP ASP A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  THR 61  61  61  THR THR A . n 
A 1 62  SER 62  62  62  SER SER A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  MET 64  64  64  MET MET A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  TYR 66  66  66  TYR TYR A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  LEU 68  68  68  LEU LEU A . n 
A 1 69  ALA 69  69  69  ALA ALA A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  LEU 71  71  71  LEU LEU A . n 
A 1 72  LYS 72  72  72  LYS LYS A . n 
A 1 73  LYS 73  73  73  LYS LYS A . n 
A 1 74  GLU 74  74  74  GLU GLU A . n 
A 1 75  MET 75  75  75  MET MET A . n 
A 1 76  SER 76  76  76  SER SER A . n 
A 1 77  LEU 77  77  77  LEU LEU A . n 
A 1 78  VAL 78  78  78  VAL VAL A . n 
A 1 79  LEU 79  79  79  LEU LEU A . n 
A 1 80  ASP 80  80  80  ASP ASP A . n 
A 1 81  THR 81  81  81  THR THR A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  HIS 84  84  84  HIS HIS A . n 
A 1 85  ARG 85  85  85  ARG ARG A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  ASP 88  88  88  ASP ASP A . n 
A 1 89  LYS 89  89  89  LYS LYS A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  VAL 91  91  91  VAL VAL A . n 
A 1 92  GLU 92  92  92  GLU GLU A . n 
A 1 93  PHE 93  93  93  PHE PHE A . n 
A 1 94  PHE 94  94  94  PHE PHE A . n 
A 1 95  LYS 95  95  95  LYS LYS A . n 
A 1 96  THR 96  96  96  THR THR A . n 
A 1 97  THR 97  97  97  THR THR A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 THR 100 100 100 THR THR A . n 
A 1 101 SER 101 101 101 SER SER A . n 
A 1 102 GLU 102 102 102 GLU GLU A . n 
A 1 103 ASN 103 103 103 ASN ASN A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 ALA 105 105 105 ALA ALA A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 TYR 107 107 107 TYR TYR A . n 
A 1 108 MET 108 108 108 MET MET A . n 
A 1 109 PHE 109 109 109 PHE PHE A . n 
A 1 110 GLU 110 110 110 GLU GLU A . n 
A 1 111 LYS 111 111 111 LYS LYS A . n 
A 1 112 LEU 112 112 112 LEU LEU A . n 
A 1 113 LYS 113 113 113 LYS LYS A . n 
A 1 114 SER 114 114 114 SER SER A . n 
A 1 115 VAL 115 115 115 VAL VAL A . n 
A 1 116 MET 116 116 116 MET MET A . n 
A 1 117 SER 117 117 117 SER SER A . n 
A 1 118 ASN 118 118 118 ASN ASN A . n 
A 1 119 PRO 119 119 119 PRO PRO A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 TYR 123 123 123 TYR TYR A . n 
A 1 124 LYS 124 124 124 LYS LYS A . n 
A 1 125 VAL 125 125 125 VAL VAL A . n 
A 1 126 THR 126 126 126 THR THR A . n 
A 1 127 ILE 127 127 127 ILE ILE A . n 
A 1 128 GLU 128 128 128 GLU GLU A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 THR 130 130 130 THR THR A . n 
A 1 131 PRO 131 131 131 PRO PRO A . n 
A 1 132 LYS 132 132 132 LYS LYS A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 ILE 134 134 134 ILE ILE A . n 
A 1 135 PHE 135 135 135 PHE PHE A . n 
A 1 136 THR 136 136 136 THR THR A . n 
A 1 137 TYR 137 137 137 TYR TYR A . n 
A 1 138 LYS 138 138 138 LYS LYS A . n 
A 1 139 GLY 139 139 139 GLY GLY A . n 
A 1 140 SER 140 140 140 SER SER A . n 
# 
_pdbx_SG_project.id                    1 
_pdbx_SG_project.project_name          'PSI, Protein Structure Initiative' 
_pdbx_SG_project.full_name_of_center   'New York SGX Research Center for Structural Genomics' 
_pdbx_SG_project.initial_of_center     NYSGXRC 
# 
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 
B 2 NA  1   1001 1   NA  NA  A . 
C 2 NA  1   1002 2   NA  NA  A . 
D 3 ZN  1   2001 1   ZN  ZN  A . 
E 4 GOL 1   3001 1   GOL GOL A . 
F 5 HOH 1   3002 3   HOH HOH A . 
F 5 HOH 2   3003 4   HOH HOH A . 
F 5 HOH 3   3004 5   HOH HOH A . 
F 5 HOH 4   3005 6   HOH HOH A . 
F 5 HOH 5   3006 7   HOH HOH A . 
F 5 HOH 6   3007 8   HOH HOH A . 
F 5 HOH 7   3008 9   HOH HOH A . 
F 5 HOH 8   3009 10  HOH HOH A . 
F 5 HOH 9   3010 12  HOH HOH A . 
F 5 HOH 10  3011 13  HOH HOH A . 
F 5 HOH 11  3012 14  HOH HOH A . 
F 5 HOH 12  3013 15  HOH HOH A . 
F 5 HOH 13  3014 16  HOH HOH A . 
F 5 HOH 14  3015 18  HOH HOH A . 
F 5 HOH 15  3016 19  HOH HOH A . 
F 5 HOH 16  3017 20  HOH HOH A . 
F 5 HOH 17  3018 21  HOH HOH A . 
F 5 HOH 18  3019 22  HOH HOH A . 
F 5 HOH 19  3020 23  HOH HOH A . 
F 5 HOH 20  3021 24  HOH HOH A . 
F 5 HOH 21  3022 25  HOH HOH A . 
F 5 HOH 22  3023 26  HOH HOH A . 
F 5 HOH 23  3024 27  HOH HOH A . 
F 5 HOH 24  3025 28  HOH HOH A . 
F 5 HOH 25  3026 29  HOH HOH A . 
F 5 HOH 26  3027 30  HOH HOH A . 
F 5 HOH 27  3028 31  HOH HOH A . 
F 5 HOH 28  3029 32  HOH HOH A . 
F 5 HOH 29  3030 33  HOH HOH A . 
F 5 HOH 30  3031 34  HOH HOH A . 
F 5 HOH 31  3032 35  HOH HOH A . 
F 5 HOH 32  3033 36  HOH HOH A . 
F 5 HOH 33  3034 38  HOH HOH A . 
F 5 HOH 34  3035 39  HOH HOH A . 
F 5 HOH 35  3036 40  HOH HOH A . 
F 5 HOH 36  3037 42  HOH HOH A . 
F 5 HOH 37  3038 43  HOH HOH A . 
F 5 HOH 38  3039 44  HOH HOH A . 
F 5 HOH 39  3040 45  HOH HOH A . 
F 5 HOH 40  3041 46  HOH HOH A . 
F 5 HOH 41  3042 47  HOH HOH A . 
F 5 HOH 42  3043 49  HOH HOH A . 
F 5 HOH 43  3044 50  HOH HOH A . 
F 5 HOH 44  3045 51  HOH HOH A . 
F 5 HOH 45  3046 52  HOH HOH A . 
F 5 HOH 46  3047 53  HOH HOH A . 
F 5 HOH 47  3048 54  HOH HOH A . 
F 5 HOH 48  3049 56  HOH HOH A . 
F 5 HOH 49  3050 57  HOH HOH A . 
F 5 HOH 50  3051 58  HOH HOH A . 
F 5 HOH 51  3052 59  HOH HOH A . 
F 5 HOH 52  3053 60  HOH HOH A . 
F 5 HOH 53  3054 61  HOH HOH A . 
F 5 HOH 54  3055 62  HOH HOH A . 
F 5 HOH 55  3056 63  HOH HOH A . 
F 5 HOH 56  3057 64  HOH HOH A . 
F 5 HOH 57  3058 65  HOH HOH A . 
F 5 HOH 58  3059 67  HOH HOH A . 
F 5 HOH 59  3060 69  HOH HOH A . 
F 5 HOH 60  3061 70  HOH HOH A . 
F 5 HOH 61  3062 71  HOH HOH A . 
F 5 HOH 62  3063 72  HOH HOH A . 
F 5 HOH 63  3064 73  HOH HOH A . 
F 5 HOH 64  3065 74  HOH HOH A . 
F 5 HOH 65  3066 75  HOH HOH A . 
F 5 HOH 66  3067 76  HOH HOH A . 
F 5 HOH 67  3068 77  HOH HOH A . 
F 5 HOH 68  3069 78  HOH HOH A . 
F 5 HOH 69  3070 79  HOH HOH A . 
F 5 HOH 70  3071 80  HOH HOH A . 
F 5 HOH 71  3072 81  HOH HOH A . 
F 5 HOH 72  3073 83  HOH HOH A . 
F 5 HOH 73  3074 84  HOH HOH A . 
F 5 HOH 74  3075 85  HOH HOH A . 
F 5 HOH 75  3076 86  HOH HOH A . 
F 5 HOH 76  3077 91  HOH HOH A . 
F 5 HOH 77  3078 93  HOH HOH A . 
F 5 HOH 78  3079 94  HOH HOH A . 
F 5 HOH 79  3080 95  HOH HOH A . 
F 5 HOH 80  3081 96  HOH HOH A . 
F 5 HOH 81  3082 97  HOH HOH A . 
F 5 HOH 82  3083 98  HOH HOH A . 
F 5 HOH 83  3084 99  HOH HOH A . 
F 5 HOH 84  3085 100 HOH HOH A . 
F 5 HOH 85  3086 101 HOH HOH A . 
F 5 HOH 86  3087 102 HOH HOH A . 
F 5 HOH 87  3088 103 HOH HOH A . 
F 5 HOH 88  3089 104 HOH HOH A . 
F 5 HOH 89  3090 105 HOH HOH A . 
F 5 HOH 90  3091 106 HOH HOH A . 
F 5 HOH 91  3092 107 HOH HOH A . 
F 5 HOH 92  3093 108 HOH HOH A . 
F 5 HOH 93  3094 109 HOH HOH A . 
F 5 HOH 94  3095 110 HOH HOH A . 
F 5 HOH 95  3096 111 HOH HOH A . 
F 5 HOH 96  3097 112 HOH HOH A . 
F 5 HOH 97  3098 113 HOH HOH A . 
F 5 HOH 98  3099 114 HOH HOH A . 
F 5 HOH 99  3100 115 HOH HOH A . 
F 5 HOH 100 3101 116 HOH HOH A . 
F 5 HOH 101 3102 117 HOH HOH A . 
F 5 HOH 102 3103 118 HOH HOH A . 
F 5 HOH 103 3104 119 HOH HOH A . 
F 5 HOH 104 3105 120 HOH HOH A . 
F 5 HOH 105 3106 121 HOH HOH A . 
F 5 HOH 106 3107 122 HOH HOH A . 
F 5 HOH 107 3108 124 HOH HOH A . 
F 5 HOH 108 3109 125 HOH HOH A . 
F 5 HOH 109 3110 126 HOH HOH A . 
F 5 HOH 110 3111 127 HOH HOH A . 
F 5 HOH 111 3112 128 HOH HOH A . 
F 5 HOH 112 3113 129 HOH HOH A . 
F 5 HOH 113 3114 130 HOH HOH A . 
F 5 HOH 114 3115 131 HOH HOH A . 
F 5 HOH 115 3116 136 HOH HOH A . 
F 5 HOH 116 3117 138 HOH HOH A . 
F 5 HOH 117 3118 139 HOH HOH A . 
F 5 HOH 118 3119 2   HOH HOH A . 
F 5 HOH 119 3120 3   HOH HOH A . 
F 5 HOH 120 3121 4   HOH HOH A . 
F 5 HOH 121 3122 5   HOH HOH A . 
F 5 HOH 122 3123 6   HOH HOH A . 
F 5 HOH 123 3124 7   HOH HOH A . 
F 5 HOH 124 3125 8   HOH HOH A . 
F 5 HOH 125 3126 9   HOH HOH A . 
F 5 HOH 126 3127 10  HOH HOH A . 
F 5 HOH 127 3128 11  HOH HOH A . 
F 5 HOH 128 3129 12  HOH HOH A . 
F 5 HOH 129 3130 13  HOH HOH A . 
F 5 HOH 130 3131 14  HOH HOH A . 
F 5 HOH 131 3132 15  HOH HOH A . 
F 5 HOH 132 3133 16  HOH HOH A . 
F 5 HOH 133 3134 17  HOH HOH A . 
F 5 HOH 134 3135 18  HOH HOH A . 
F 5 HOH 135 3136 19  HOH HOH A . 
F 5 HOH 136 3137 20  HOH HOH A . 
F 5 HOH 137 3138 21  HOH HOH A . 
F 5 HOH 138 3139 22  HOH HOH A . 
F 5 HOH 139 3140 23  HOH HOH A . 
F 5 HOH 140 3141 24  HOH HOH A . 
F 5 HOH 141 3142 25  HOH HOH A . 
F 5 HOH 142 3143 26  HOH HOH A . 
F 5 HOH 143 3144 27  HOH HOH A . 
F 5 HOH 144 3145 28  HOH HOH A . 
F 5 HOH 145 3146 29  HOH HOH A . 
F 5 HOH 146 3147 30  HOH HOH A . 
F 5 HOH 147 3148 31  HOH HOH A . 
F 5 HOH 148 3149 32  HOH HOH A . 
F 5 HOH 149 3150 33  HOH HOH A . 
F 5 HOH 150 3151 34  HOH HOH A . 
F 5 HOH 151 3152 35  HOH HOH A . 
F 5 HOH 152 3153 36  HOH HOH A . 
F 5 HOH 153 3154 37  HOH HOH A . 
F 5 HOH 154 3155 38  HOH HOH A . 
F 5 HOH 155 3156 39  HOH HOH A . 
F 5 HOH 156 3157 40  HOH HOH A . 
F 5 HOH 157 3158 41  HOH HOH A . 
F 5 HOH 158 3159 42  HOH HOH A . 
F 5 HOH 159 3160 43  HOH HOH A . 
F 5 HOH 160 3161 44  HOH HOH A . 
F 5 HOH 161 3162 45  HOH HOH A . 
F 5 HOH 162 3163 46  HOH HOH A . 
F 5 HOH 163 3164 47  HOH HOH A . 
F 5 HOH 164 3165 48  HOH HOH A . 
F 5 HOH 165 3166 49  HOH HOH A . 
F 5 HOH 166 3167 50  HOH HOH A . 
F 5 HOH 167 3168 51  HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA,PQS 
_pdbx_struct_assembly.oligomeric_details   hexameric 
_pdbx_struct_assembly.oligomeric_count     6 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2,3,4,5,6 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F 
# 
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)' 14840 ? 
1 MORE         -352  ? 
1 'SSA (A^2)'  37860 ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555  x,y,z                  1.0000000000  0.0000000000  0.0000000000 0.0000000000   0.0000000000  
1.0000000000  0.0000000000 0.0000000000  0.0000000000 0.0000000000 1.0000000000  0.0000000000   
2 'crystal symmetry operation' 2_665  -y+1,x-y+1,z           -0.5000000000 -0.8660254038 0.0000000000 34.8960000000  0.8660254038  
-0.5000000000 0.0000000000 60.4416449809 0.0000000000 0.0000000000 1.0000000000  0.0000000000   
3 'crystal symmetry operation' 3_565  -x+y,-x+1,z            -0.5000000000 0.8660254038  0.0000000000 -34.8960000000 -0.8660254038 
-0.5000000000 0.0000000000 60.4416449809 0.0000000000 0.0000000000 1.0000000000  0.0000000000   
4 'crystal symmetry operation' 10_456 y-1/3,x+1/3,-z+4/3     -0.5000000000 0.8660254038  0.0000000000 -34.8960000000 0.8660254038  
0.5000000000  0.0000000000 20.1472149936 0.0000000000 0.0000000000 -1.0000000000 213.5840000000 
5 'crystal symmetry operation' 11_566 x-y+2/3,-y+4/3,-z+4/3  1.0000000000  0.0000000000  0.0000000000 0.0000000000   0.0000000000  
-1.0000000000 0.0000000000 80.5888599746 0.0000000000 0.0000000000 -1.0000000000 213.5840000000 
6 'crystal symmetry operation' 12_556 -x+2/3,-x+y+1/3,-z+4/3 -0.5000000000 -0.8660254038 0.0000000000 34.8960000000  -0.8660254038 
0.5000000000  0.0000000000 20.1472149936 0.0000000000 0.0000000000 -1.0000000000 213.5840000000 
# 
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  NE2 ? A HIS 19 ? A HIS 19   ? 1_555  ZN ? D ZN . ? A ZN 2001 ? 1_555 NE2 ? A HIS 44 ? A HIS 44   ? 1_555  93.9  ? 
2  NE2 ? A HIS 19 ? A HIS 19   ? 1_555  ZN ? D ZN . ? A ZN 2001 ? 1_555 NE2 ? A HIS 46 ? A HIS 46   ? 1_555  111.5 ? 
3  NE2 ? A HIS 44 ? A HIS 44   ? 1_555  ZN ? D ZN . ? A ZN 2001 ? 1_555 NE2 ? A HIS 46 ? A HIS 46   ? 1_555  109.3 ? 
4  NE2 ? A HIS 19 ? A HIS 19   ? 1_555  ZN ? D ZN . ? A ZN 2001 ? 1_555 O   ? F HOH .  ? A HOH 3084 ? 11_566 166.5 ? 
5  NE2 ? A HIS 44 ? A HIS 44   ? 1_555  ZN ? D ZN . ? A ZN 2001 ? 1_555 O   ? F HOH .  ? A HOH 3084 ? 11_566 83.7  ? 
6  NE2 ? A HIS 46 ? A HIS 46   ? 1_555  ZN ? D ZN . ? A ZN 2001 ? 1_555 O   ? F HOH .  ? A HOH 3084 ? 11_566 81.7  ? 
7  NE2 ? A HIS 19 ? A HIS 19   ? 1_555  ZN ? D ZN . ? A ZN 2001 ? 1_555 O   ? F HOH .  ? A HOH 3139 ? 1_555  109.0 ? 
8  NE2 ? A HIS 44 ? A HIS 44   ? 1_555  ZN ? D ZN . ? A ZN 2001 ? 1_555 O   ? F HOH .  ? A HOH 3139 ? 1_555  111.5 ? 
9  NE2 ? A HIS 46 ? A HIS 46   ? 1_555  ZN ? D ZN . ? A ZN 2001 ? 1_555 O   ? F HOH .  ? A HOH 3139 ? 1_555  118.8 ? 
10 O   ? F HOH .  ? A HOH 3084 ? 11_566 ZN ? D ZN . ? A ZN 2001 ? 1_555 O   ? F HOH .  ? A HOH 3139 ? 1_555  60.2  ? 
11 O   ? A CYS 38 ? A CYS 38   ? 1_555  NA ? C NA . ? A NA 1002 ? 1_555 O   ? A ASN 40 ? A ASN 40   ? 1_555  111.6 ? 
12 O   ? A CYS 38 ? A CYS 38   ? 1_555  NA ? C NA . ? A NA 1002 ? 1_555 ND1 ? A HIS 44 ? A HIS 44   ? 1_555  86.6  ? 
13 O   ? A ASN 40 ? A ASN 40   ? 1_555  NA ? C NA . ? A NA 1002 ? 1_555 ND1 ? A HIS 44 ? A HIS 44   ? 1_555  159.9 ? 
14 O   ? A ASN 47 ? A ASN 47   ? 1_555  NA ? B NA . ? A NA 1001 ? 1_555 O   ? F HOH .  ? A HOH 3019 ? 1_555  150.6 ? 
15 O   ? A ASN 47 ? A ASN 47   ? 1_555  NA ? B NA . ? A NA 1001 ? 1_555 O   ? F HOH .  ? A HOH 3117 ? 1_555  69.9  ? 
16 O   ? F HOH .  ? A HOH 3019 ? 1_555  NA ? B NA . ? A NA 1001 ? 1_555 O   ? F HOH .  ? A HOH 3117 ? 1_555  106.9 ? 
# 
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 2006-03-14 
2 'Structure model' 1 1 2008-05-01 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2021-02-03 
5 'Structure model' 1 4 2021-10-20 
6 'Structure model' 1 5 2023-08-30 
# 
_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' 'Derived calculations'      
3 3 'Structure model' 'Version format compliance' 
4 4 'Structure model' 'Derived calculations'      
5 4 'Structure model' 'Structure summary'         
6 5 'Structure model' 'Database references'       
7 6 'Structure model' 'Data collection'           
8 6 'Structure model' 'Refinement description'    
# 
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' audit_author                  
2 4 'Structure model' pdbx_struct_conn_angle        
3 4 'Structure model' struct_conn                   
4 4 'Structure model' struct_site                   
5 5 'Structure model' database_2                    
6 5 'Structure model' struct_ref_seq_dif            
7 6 'Structure model' chem_comp_atom                
8 6 'Structure model' chem_comp_bond                
9 6 'Structure model' pdbx_initial_refinement_model 
# 
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' '_audit_author.identifier_ORCID'             
2  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'  
3  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id' 
4  4 'Structure model' '_pdbx_struct_conn_angle.ptnr1_symmetry'     
5  4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'  
6  4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id' 
7  4 'Structure model' '_pdbx_struct_conn_angle.ptnr3_symmetry'     
8  4 'Structure model' '_pdbx_struct_conn_angle.value'              
9  4 'Structure model' '_struct_conn.pdbx_dist_value'               
10 4 'Structure model' '_struct_conn.ptnr1_auth_comp_id'            
11 4 'Structure model' '_struct_conn.ptnr1_auth_seq_id'             
12 4 'Structure model' '_struct_conn.ptnr1_label_asym_id'           
13 4 'Structure model' '_struct_conn.ptnr1_label_atom_id'           
14 4 'Structure model' '_struct_conn.ptnr1_label_comp_id'           
15 4 'Structure model' '_struct_conn.ptnr1_label_seq_id'            
16 4 'Structure model' '_struct_conn.ptnr2_auth_comp_id'            
17 4 'Structure model' '_struct_conn.ptnr2_auth_seq_id'             
18 4 'Structure model' '_struct_conn.ptnr2_label_asym_id'           
19 4 'Structure model' '_struct_conn.ptnr2_label_atom_id'           
20 4 'Structure model' '_struct_conn.ptnr2_label_comp_id'           
21 4 'Structure model' '_struct_conn.ptnr2_label_seq_id'            
22 4 'Structure model' '_struct_conn.ptnr2_symmetry'                
23 4 'Structure model' '_struct_site.pdbx_auth_asym_id'             
24 4 'Structure model' '_struct_site.pdbx_auth_comp_id'             
25 4 'Structure model' '_struct_site.pdbx_auth_seq_id'              
26 5 'Structure model' '_database_2.pdbx_DOI'                       
27 5 'Structure model' '_database_2.pdbx_database_accession'        
28 5 'Structure model' '_struct_ref_seq_dif.details'                
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
DENZO     'data reduction' .        ? 1 
SCALEPACK 'data scaling'   .        ? 2 
MOLREP    phasing          .        ? 3 
REFMAC    refinement       5.2.0005 ? 4 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    SER 
_pdbx_validate_torsion.auth_asym_id    A 
_pdbx_validate_torsion.auth_seq_id     99 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             -85.25 
_pdbx_validate_torsion.psi             39.95 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLU N    N  N N 88  
GLU CA   C  N S 89  
GLU C    C  N N 90  
GLU O    O  N N 91  
GLU CB   C  N N 92  
GLU CG   C  N N 93  
GLU CD   C  N N 94  
GLU OE1  O  N N 95  
GLU OE2  O  N N 96  
GLU OXT  O  N N 97  
GLU H    H  N N 98  
GLU H2   H  N N 99  
GLU HA   H  N N 100 
GLU HB2  H  N N 101 
GLU HB3  H  N N 102 
GLU HG2  H  N N 103 
GLU HG3  H  N N 104 
GLU HE2  H  N N 105 
GLU HXT  H  N N 106 
GLY N    N  N N 107 
GLY CA   C  N N 108 
GLY C    C  N N 109 
GLY O    O  N N 110 
GLY OXT  O  N N 111 
GLY H    H  N N 112 
GLY H2   H  N N 113 
GLY HA2  H  N N 114 
GLY HA3  H  N N 115 
GLY HXT  H  N N 116 
GOL C1   C  N N 117 
GOL O1   O  N N 118 
GOL C2   C  N N 119 
GOL O2   O  N N 120 
GOL C3   C  N N 121 
GOL O3   O  N N 122 
GOL H11  H  N N 123 
GOL H12  H  N N 124 
GOL HO1  H  N N 125 
GOL H2   H  N N 126 
GOL HO2  H  N N 127 
GOL H31  H  N N 128 
GOL H32  H  N N 129 
GOL HO3  H  N N 130 
HIS N    N  N N 131 
HIS CA   C  N S 132 
HIS C    C  N N 133 
HIS O    O  N N 134 
HIS CB   C  N N 135 
HIS CG   C  Y N 136 
HIS ND1  N  Y N 137 
HIS CD2  C  Y N 138 
HIS CE1  C  Y N 139 
HIS NE2  N  Y N 140 
HIS OXT  O  N N 141 
HIS H    H  N N 142 
HIS H2   H  N N 143 
HIS HA   H  N N 144 
HIS HB2  H  N N 145 
HIS HB3  H  N N 146 
HIS HD1  H  N N 147 
HIS HD2  H  N N 148 
HIS HE1  H  N N 149 
HIS HE2  H  N N 150 
HIS HXT  H  N N 151 
HOH O    O  N N 152 
HOH H1   H  N N 153 
HOH H2   H  N N 154 
ILE N    N  N N 155 
ILE CA   C  N S 156 
ILE C    C  N N 157 
ILE O    O  N N 158 
ILE CB   C  N S 159 
ILE CG1  C  N N 160 
ILE CG2  C  N N 161 
ILE CD1  C  N N 162 
ILE OXT  O  N N 163 
ILE H    H  N N 164 
ILE H2   H  N N 165 
ILE HA   H  N N 166 
ILE HB   H  N N 167 
ILE HG12 H  N N 168 
ILE HG13 H  N N 169 
ILE HG21 H  N N 170 
ILE HG22 H  N N 171 
ILE HG23 H  N N 172 
ILE HD11 H  N N 173 
ILE HD12 H  N N 174 
ILE HD13 H  N N 175 
ILE HXT  H  N N 176 
LEU N    N  N N 177 
LEU CA   C  N S 178 
LEU C    C  N N 179 
LEU O    O  N N 180 
LEU CB   C  N N 181 
LEU CG   C  N N 182 
LEU CD1  C  N N 183 
LEU CD2  C  N N 184 
LEU OXT  O  N N 185 
LEU H    H  N N 186 
LEU H2   H  N N 187 
LEU HA   H  N N 188 
LEU HB2  H  N N 189 
LEU HB3  H  N N 190 
LEU HG   H  N N 191 
LEU HD11 H  N N 192 
LEU HD12 H  N N 193 
LEU HD13 H  N N 194 
LEU HD21 H  N N 195 
LEU HD22 H  N N 196 
LEU HD23 H  N N 197 
LEU HXT  H  N N 198 
LYS N    N  N N 199 
LYS CA   C  N S 200 
LYS C    C  N N 201 
LYS O    O  N N 202 
LYS CB   C  N N 203 
LYS CG   C  N N 204 
LYS CD   C  N N 205 
LYS CE   C  N N 206 
LYS NZ   N  N N 207 
LYS OXT  O  N N 208 
LYS H    H  N N 209 
LYS H2   H  N N 210 
LYS HA   H  N N 211 
LYS HB2  H  N N 212 
LYS HB3  H  N N 213 
LYS HG2  H  N N 214 
LYS HG3  H  N N 215 
LYS HD2  H  N N 216 
LYS HD3  H  N N 217 
LYS HE2  H  N N 218 
LYS HE3  H  N N 219 
LYS HZ1  H  N N 220 
LYS HZ2  H  N N 221 
LYS HZ3  H  N N 222 
LYS HXT  H  N N 223 
MET N    N  N N 224 
MET CA   C  N S 225 
MET C    C  N N 226 
MET O    O  N N 227 
MET CB   C  N N 228 
MET CG   C  N N 229 
MET SD   S  N N 230 
MET CE   C  N N 231 
MET OXT  O  N N 232 
MET H    H  N N 233 
MET H2   H  N N 234 
MET HA   H  N N 235 
MET HB2  H  N N 236 
MET HB3  H  N N 237 
MET HG2  H  N N 238 
MET HG3  H  N N 239 
MET HE1  H  N N 240 
MET HE2  H  N N 241 
MET HE3  H  N N 242 
MET HXT  H  N N 243 
NA  NA   NA N N 244 
PHE N    N  N N 245 
PHE CA   C  N S 246 
PHE C    C  N N 247 
PHE O    O  N N 248 
PHE CB   C  N N 249 
PHE CG   C  Y N 250 
PHE CD1  C  Y N 251 
PHE CD2  C  Y N 252 
PHE CE1  C  Y N 253 
PHE CE2  C  Y N 254 
PHE CZ   C  Y N 255 
PHE OXT  O  N N 256 
PHE H    H  N N 257 
PHE H2   H  N N 258 
PHE HA   H  N N 259 
PHE HB2  H  N N 260 
PHE HB3  H  N N 261 
PHE HD1  H  N N 262 
PHE HD2  H  N N 263 
PHE HE1  H  N N 264 
PHE HE2  H  N N 265 
PHE HZ   H  N N 266 
PHE HXT  H  N N 267 
PRO N    N  N N 268 
PRO CA   C  N S 269 
PRO C    C  N N 270 
PRO O    O  N N 271 
PRO CB   C  N N 272 
PRO CG   C  N N 273 
PRO CD   C  N N 274 
PRO OXT  O  N N 275 
PRO H    H  N N 276 
PRO HA   H  N N 277 
PRO HB2  H  N N 278 
PRO HB3  H  N N 279 
PRO HG2  H  N N 280 
PRO HG3  H  N N 281 
PRO HD2  H  N N 282 
PRO HD3  H  N N 283 
PRO HXT  H  N N 284 
SER N    N  N N 285 
SER CA   C  N S 286 
SER C    C  N N 287 
SER O    O  N N 288 
SER CB   C  N N 289 
SER OG   O  N N 290 
SER OXT  O  N N 291 
SER H    H  N N 292 
SER H2   H  N N 293 
SER HA   H  N N 294 
SER HB2  H  N N 295 
SER HB3  H  N N 296 
SER HG   H  N N 297 
SER HXT  H  N N 298 
THR N    N  N N 299 
THR CA   C  N S 300 
THR C    C  N N 301 
THR O    O  N N 302 
THR CB   C  N R 303 
THR OG1  O  N N 304 
THR CG2  C  N N 305 
THR OXT  O  N N 306 
THR H    H  N N 307 
THR H2   H  N N 308 
THR HA   H  N N 309 
THR HB   H  N N 310 
THR HG1  H  N N 311 
THR HG21 H  N N 312 
THR HG22 H  N N 313 
THR HG23 H  N N 314 
THR HXT  H  N N 315 
TRP N    N  N N 316 
TRP CA   C  N S 317 
TRP C    C  N N 318 
TRP O    O  N N 319 
TRP CB   C  N N 320 
TRP CG   C  Y N 321 
TRP CD1  C  Y N 322 
TRP CD2  C  Y N 323 
TRP NE1  N  Y N 324 
TRP CE2  C  Y N 325 
TRP CE3  C  Y N 326 
TRP CZ2  C  Y N 327 
TRP CZ3  C  Y N 328 
TRP CH2  C  Y N 329 
TRP OXT  O  N N 330 
TRP H    H  N N 331 
TRP H2   H  N N 332 
TRP HA   H  N N 333 
TRP HB2  H  N N 334 
TRP HB3  H  N N 335 
TRP HD1  H  N N 336 
TRP HE1  H  N N 337 
TRP HE3  H  N N 338 
TRP HZ2  H  N N 339 
TRP HZ3  H  N N 340 
TRP HH2  H  N N 341 
TRP HXT  H  N N 342 
TYR N    N  N N 343 
TYR CA   C  N S 344 
TYR C    C  N N 345 
TYR O    O  N N 346 
TYR CB   C  N N 347 
TYR CG   C  Y N 348 
TYR CD1  C  Y N 349 
TYR CD2  C  Y N 350 
TYR CE1  C  Y N 351 
TYR CE2  C  Y N 352 
TYR CZ   C  Y N 353 
TYR OH   O  N N 354 
TYR OXT  O  N N 355 
TYR H    H  N N 356 
TYR H2   H  N N 357 
TYR HA   H  N N 358 
TYR HB2  H  N N 359 
TYR HB3  H  N N 360 
TYR HD1  H  N N 361 
TYR HD2  H  N N 362 
TYR HE1  H  N N 363 
TYR HE2  H  N N 364 
TYR HH   H  N N 365 
TYR HXT  H  N N 366 
VAL N    N  N N 367 
VAL CA   C  N S 368 
VAL C    C  N N 369 
VAL O    O  N N 370 
VAL CB   C  N N 371 
VAL CG1  C  N N 372 
VAL CG2  C  N N 373 
VAL OXT  O  N N 374 
VAL H    H  N N 375 
VAL H2   H  N N 376 
VAL HA   H  N N 377 
VAL HB   H  N N 378 
VAL HG11 H  N N 379 
VAL HG12 H  N N 380 
VAL HG13 H  N N 381 
VAL HG21 H  N N 382 
VAL HG22 H  N N 383 
VAL HG23 H  N N 384 
VAL HXT  H  N N 385 
ZN  ZN   ZN N N 386 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLU N   CA   sing N N 83  
GLU N   H    sing N N 84  
GLU N   H2   sing N N 85  
GLU CA  C    sing N N 86  
GLU CA  CB   sing N N 87  
GLU CA  HA   sing N N 88  
GLU C   O    doub N N 89  
GLU C   OXT  sing N N 90  
GLU CB  CG   sing N N 91  
GLU CB  HB2  sing N N 92  
GLU CB  HB3  sing N N 93  
GLU CG  CD   sing N N 94  
GLU CG  HG2  sing N N 95  
GLU CG  HG3  sing N N 96  
GLU CD  OE1  doub N N 97  
GLU CD  OE2  sing N N 98  
GLU OE2 HE2  sing N N 99  
GLU OXT HXT  sing N N 100 
GLY N   CA   sing N N 101 
GLY N   H    sing N N 102 
GLY N   H2   sing N N 103 
GLY CA  C    sing N N 104 
GLY CA  HA2  sing N N 105 
GLY CA  HA3  sing N N 106 
GLY C   O    doub N N 107 
GLY C   OXT  sing N N 108 
GLY OXT HXT  sing N N 109 
GOL C1  O1   sing N N 110 
GOL C1  C2   sing N N 111 
GOL C1  H11  sing N N 112 
GOL C1  H12  sing N N 113 
GOL O1  HO1  sing N N 114 
GOL C2  O2   sing N N 115 
GOL C2  C3   sing N N 116 
GOL C2  H2   sing N N 117 
GOL O2  HO2  sing N N 118 
GOL C3  O3   sing N N 119 
GOL C3  H31  sing N N 120 
GOL C3  H32  sing N N 121 
GOL O3  HO3  sing N N 122 
HIS N   CA   sing N N 123 
HIS N   H    sing N N 124 
HIS N   H2   sing N N 125 
HIS CA  C    sing N N 126 
HIS CA  CB   sing N N 127 
HIS CA  HA   sing N N 128 
HIS C   O    doub N N 129 
HIS C   OXT  sing N N 130 
HIS CB  CG   sing N N 131 
HIS CB  HB2  sing N N 132 
HIS CB  HB3  sing N N 133 
HIS CG  ND1  sing Y N 134 
HIS CG  CD2  doub Y N 135 
HIS ND1 CE1  doub Y N 136 
HIS ND1 HD1  sing N N 137 
HIS CD2 NE2  sing Y N 138 
HIS CD2 HD2  sing N N 139 
HIS CE1 NE2  sing Y N 140 
HIS CE1 HE1  sing N N 141 
HIS NE2 HE2  sing N N 142 
HIS OXT HXT  sing N N 143 
HOH O   H1   sing N N 144 
HOH O   H2   sing N N 145 
ILE N   CA   sing N N 146 
ILE N   H    sing N N 147 
ILE N   H2   sing N N 148 
ILE CA  C    sing N N 149 
ILE CA  CB   sing N N 150 
ILE CA  HA   sing N N 151 
ILE C   O    doub N N 152 
ILE C   OXT  sing N N 153 
ILE CB  CG1  sing N N 154 
ILE CB  CG2  sing N N 155 
ILE CB  HB   sing N N 156 
ILE CG1 CD1  sing N N 157 
ILE CG1 HG12 sing N N 158 
ILE CG1 HG13 sing N N 159 
ILE CG2 HG21 sing N N 160 
ILE CG2 HG22 sing N N 161 
ILE CG2 HG23 sing N N 162 
ILE CD1 HD11 sing N N 163 
ILE CD1 HD12 sing N N 164 
ILE CD1 HD13 sing N N 165 
ILE OXT HXT  sing N N 166 
LEU N   CA   sing N N 167 
LEU N   H    sing N N 168 
LEU N   H2   sing N N 169 
LEU CA  C    sing N N 170 
LEU CA  CB   sing N N 171 
LEU CA  HA   sing N N 172 
LEU C   O    doub N N 173 
LEU C   OXT  sing N N 174 
LEU CB  CG   sing N N 175 
LEU CB  HB2  sing N N 176 
LEU CB  HB3  sing N N 177 
LEU CG  CD1  sing N N 178 
LEU CG  CD2  sing N N 179 
LEU CG  HG   sing N N 180 
LEU CD1 HD11 sing N N 181 
LEU CD1 HD12 sing N N 182 
LEU CD1 HD13 sing N N 183 
LEU CD2 HD21 sing N N 184 
LEU CD2 HD22 sing N N 185 
LEU CD2 HD23 sing N N 186 
LEU OXT HXT  sing N N 187 
LYS N   CA   sing N N 188 
LYS N   H    sing N N 189 
LYS N   H2   sing N N 190 
LYS CA  C    sing N N 191 
LYS CA  CB   sing N N 192 
LYS CA  HA   sing N N 193 
LYS C   O    doub N N 194 
LYS C   OXT  sing N N 195 
LYS CB  CG   sing N N 196 
LYS CB  HB2  sing N N 197 
LYS CB  HB3  sing N N 198 
LYS CG  CD   sing N N 199 
LYS CG  HG2  sing N N 200 
LYS CG  HG3  sing N N 201 
LYS CD  CE   sing N N 202 
LYS CD  HD2  sing N N 203 
LYS CD  HD3  sing N N 204 
LYS CE  NZ   sing N N 205 
LYS CE  HE2  sing N N 206 
LYS CE  HE3  sing N N 207 
LYS NZ  HZ1  sing N N 208 
LYS NZ  HZ2  sing N N 209 
LYS NZ  HZ3  sing N N 210 
LYS OXT HXT  sing N N 211 
MET N   CA   sing N N 212 
MET N   H    sing N N 213 
MET N   H2   sing N N 214 
MET CA  C    sing N N 215 
MET CA  CB   sing N N 216 
MET CA  HA   sing N N 217 
MET C   O    doub N N 218 
MET C   OXT  sing N N 219 
MET CB  CG   sing N N 220 
MET CB  HB2  sing N N 221 
MET CB  HB3  sing N N 222 
MET CG  SD   sing N N 223 
MET CG  HG2  sing N N 224 
MET CG  HG3  sing N N 225 
MET SD  CE   sing N N 226 
MET CE  HE1  sing N N 227 
MET CE  HE2  sing N N 228 
MET CE  HE3  sing N N 229 
MET OXT HXT  sing N N 230 
PHE N   CA   sing N N 231 
PHE N   H    sing N N 232 
PHE N   H2   sing N N 233 
PHE CA  C    sing N N 234 
PHE CA  CB   sing N N 235 
PHE CA  HA   sing N N 236 
PHE C   O    doub N N 237 
PHE C   OXT  sing N N 238 
PHE CB  CG   sing N N 239 
PHE CB  HB2  sing N N 240 
PHE CB  HB3  sing N N 241 
PHE CG  CD1  doub Y N 242 
PHE CG  CD2  sing Y N 243 
PHE CD1 CE1  sing Y N 244 
PHE CD1 HD1  sing N N 245 
PHE CD2 CE2  doub Y N 246 
PHE CD2 HD2  sing N N 247 
PHE CE1 CZ   doub Y N 248 
PHE CE1 HE1  sing N N 249 
PHE CE2 CZ   sing Y N 250 
PHE CE2 HE2  sing N N 251 
PHE CZ  HZ   sing N N 252 
PHE OXT HXT  sing N N 253 
PRO N   CA   sing N N 254 
PRO N   CD   sing N N 255 
PRO N   H    sing N N 256 
PRO CA  C    sing N N 257 
PRO CA  CB   sing N N 258 
PRO CA  HA   sing N N 259 
PRO C   O    doub N N 260 
PRO C   OXT  sing N N 261 
PRO CB  CG   sing N N 262 
PRO CB  HB2  sing N N 263 
PRO CB  HB3  sing N N 264 
PRO CG  CD   sing N N 265 
PRO CG  HG2  sing N N 266 
PRO CG  HG3  sing N N 267 
PRO CD  HD2  sing N N 268 
PRO CD  HD3  sing N N 269 
PRO OXT HXT  sing N N 270 
SER N   CA   sing N N 271 
SER N   H    sing N N 272 
SER N   H2   sing N N 273 
SER CA  C    sing N N 274 
SER CA  CB   sing N N 275 
SER CA  HA   sing N N 276 
SER C   O    doub N N 277 
SER C   OXT  sing N N 278 
SER CB  OG   sing N N 279 
SER CB  HB2  sing N N 280 
SER CB  HB3  sing N N 281 
SER OG  HG   sing N N 282 
SER OXT HXT  sing N N 283 
THR N   CA   sing N N 284 
THR N   H    sing N N 285 
THR N   H2   sing N N 286 
THR CA  C    sing N N 287 
THR CA  CB   sing N N 288 
THR CA  HA   sing N N 289 
THR C   O    doub N N 290 
THR C   OXT  sing N N 291 
THR CB  OG1  sing N N 292 
THR CB  CG2  sing N N 293 
THR CB  HB   sing N N 294 
THR OG1 HG1  sing N N 295 
THR CG2 HG21 sing N N 296 
THR CG2 HG22 sing N N 297 
THR CG2 HG23 sing N N 298 
THR OXT HXT  sing N N 299 
TRP N   CA   sing N N 300 
TRP N   H    sing N N 301 
TRP N   H2   sing N N 302 
TRP CA  C    sing N N 303 
TRP CA  CB   sing N N 304 
TRP CA  HA   sing N N 305 
TRP C   O    doub N N 306 
TRP C   OXT  sing N N 307 
TRP CB  CG   sing N N 308 
TRP CB  HB2  sing N N 309 
TRP CB  HB3  sing N N 310 
TRP CG  CD1  doub Y N 311 
TRP CG  CD2  sing Y N 312 
TRP CD1 NE1  sing Y N 313 
TRP CD1 HD1  sing N N 314 
TRP CD2 CE2  doub Y N 315 
TRP CD2 CE3  sing Y N 316 
TRP NE1 CE2  sing Y N 317 
TRP NE1 HE1  sing N N 318 
TRP CE2 CZ2  sing Y N 319 
TRP CE3 CZ3  doub Y N 320 
TRP CE3 HE3  sing N N 321 
TRP CZ2 CH2  doub Y N 322 
TRP CZ2 HZ2  sing N N 323 
TRP CZ3 CH2  sing Y N 324 
TRP CZ3 HZ3  sing N N 325 
TRP CH2 HH2  sing N N 326 
TRP OXT HXT  sing N N 327 
TYR N   CA   sing N N 328 
TYR N   H    sing N N 329 
TYR N   H2   sing N N 330 
TYR CA  C    sing N N 331 
TYR CA  CB   sing N N 332 
TYR CA  HA   sing N N 333 
TYR C   O    doub N N 334 
TYR C   OXT  sing N N 335 
TYR CB  CG   sing N N 336 
TYR CB  HB2  sing N N 337 
TYR CB  HB3  sing N N 338 
TYR CG  CD1  doub Y N 339 
TYR CG  CD2  sing Y N 340 
TYR CD1 CE1  sing Y N 341 
TYR CD1 HD1  sing N N 342 
TYR CD2 CE2  doub Y N 343 
TYR CD2 HD2  sing N N 344 
TYR CE1 CZ   doub Y N 345 
TYR CE1 HE1  sing N N 346 
TYR CE2 CZ   sing Y N 347 
TYR CE2 HE2  sing N N 348 
TYR CZ  OH   sing N N 349 
TYR OH  HH   sing N N 350 
TYR OXT HXT  sing N N 351 
VAL N   CA   sing N N 352 
VAL N   H    sing N N 353 
VAL N   H2   sing N N 354 
VAL CA  C    sing N N 355 
VAL CA  CB   sing N N 356 
VAL CA  HA   sing N N 357 
VAL C   O    doub N N 358 
VAL C   OXT  sing N N 359 
VAL CB  CG1  sing N N 360 
VAL CB  CG2  sing N N 361 
VAL CB  HB   sing N N 362 
VAL CG1 HG11 sing N N 363 
VAL CG1 HG12 sing N N 364 
VAL CG1 HG13 sing N N 365 
VAL CG2 HG21 sing N N 366 
VAL CG2 HG22 sing N N 367 
VAL CG2 HG23 sing N N 368 
VAL OXT HXT  sing N N 369 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'SODIUM ION' NA  
3 'ZINC ION'   ZN  
4 GLYCEROL     GOL 
5 water        HOH 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1B66 
_pdbx_initial_refinement_model.details          ? 
# 
