data_1MFM
# 
_entry.id   1MFM 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.351 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   1MFM         pdb_00001mfm 10.2210/pdb1mfm/pdb 
RCSB  RCSB000865   ?            ?                   
WWPDB D_1000000865 ?            ?                   
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        1MFM 
_pdbx_database_status.recvd_initial_deposition_date   1999-04-16 
_pdbx_database_status.deposit_site                    BNL 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.status_code_nmr_data            ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Ferraroni, M.'  1 
'Rypniewski, W.' 2 
'Wilson, K.S.'   3 
'Orioli, P.L.'   4 
'Viezzoli, M.S.' 5 
'Banci, L.'      6 
'Bertini, I.'    7 
'Mangani, S.'    8 
# 
_citation.id                        primary 
_citation.title                     
'The crystal structure of the monomeric human SOD mutant F50E/G51E/E133Q at atomic resolution. The enzyme mechanism revisited.' 
_citation.journal_abbrev            J.Mol.Biol. 
_citation.journal_volume            288 
_citation.page_first                413 
_citation.page_last                 426 
_citation.year                      1999 
_citation.journal_id_ASTM           JMOBAK 
_citation.country                   UK 
_citation.journal_id_ISSN           0022-2836 
_citation.journal_id_CSD            0070 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   10329151 
_citation.pdbx_database_id_DOI      10.1006/jmbi.1999.2681 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Ferraroni, M.'  1 ? 
primary 'Rypniewski, W.' 2 ? 
primary 'Wilson, K.S.'   3 ? 
primary 'Viezzoli, M.S.' 4 ? 
primary 'Banci, L.'      5 ? 
primary 'Bertini, I.'    6 ? 
primary 'Mangani, S.'    7 ? 
# 
_cell.entry_id           1MFM 
_cell.length_a           34.990 
_cell.length_b           48.110 
_cell.length_c           81.080 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         1MFM 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
# 
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 'PROTEIN (COPPER,ZINC SUPEROXIDE DISMUTASE)' 15832.447 1   1.15.1.1 C6A,F50E,G51E,C111S,E133Q ? ? 
2 non-polymer syn 'ZINC ION'                                   65.409    1   ?        ?                         ? ? 
3 non-polymer syn 'COPPER (II) ION'                            63.546    1   ?        ?                         ? ? 
4 non-polymer syn 'CADMIUM ION'                                112.411   9   ?        ?                         ? ? 
5 non-polymer syn 'CHLORIDE ION'                               35.453    2   ?        ?                         ? ? 
6 water       nat water                                        18.015    283 ?        ?                         ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        Q133M2SOD 
# 
_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       
;ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEEEDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEQSTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEEEDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHSIIGRTLVVHEKADDLGKGGNEQSTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   THR n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   ALA n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  GLY n 
1 11  ASP n 
1 12  GLY n 
1 13  PRO n 
1 14  VAL n 
1 15  GLN n 
1 16  GLY n 
1 17  ILE n 
1 18  ILE n 
1 19  ASN n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  ASN n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  LYS n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  SER n 
1 35  ILE n 
1 36  LYS n 
1 37  GLY n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU n 
1 43  HIS n 
1 44  GLY n 
1 45  PHE n 
1 46  HIS n 
1 47  VAL n 
1 48  HIS n 
1 49  GLU n 
1 50  GLU n 
1 51  GLU n 
1 52  ASP n 
1 53  ASN n 
1 54  THR n 
1 55  ALA n 
1 56  GLY n 
1 57  CYS n 
1 58  THR n 
1 59  SER n 
1 60  ALA n 
1 61  GLY n 
1 62  PRO n 
1 63  HIS n 
1 64  PHE n 
1 65  ASN n 
1 66  PRO n 
1 67  LEU n 
1 68  SER n 
1 69  ARG n 
1 70  LYS n 
1 71  HIS n 
1 72  GLY n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS n 
1 76  ASP n 
1 77  GLU n 
1 78  GLU n 
1 79  ARG n 
1 80  HIS n 
1 81  VAL n 
1 82  GLY n 
1 83  ASP n 
1 84  LEU n 
1 85  GLY n 
1 86  ASN n 
1 87  VAL n 
1 88  THR n 
1 89  ALA n 
1 90  ASP n 
1 91  LYS n 
1 92  ASP n 
1 93  GLY n 
1 94  VAL n 
1 95  ALA n 
1 96  ASP n 
1 97  VAL n 
1 98  SER n 
1 99  ILE n 
1 100 GLU n 
1 101 ASP n 
1 102 SER n 
1 103 VAL n 
1 104 ILE n 
1 105 SER n 
1 106 LEU n 
1 107 SER n 
1 108 GLY n 
1 109 ASP n 
1 110 HIS n 
1 111 SER n 
1 112 ILE n 
1 113 ILE n 
1 114 GLY n 
1 115 ARG n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 HIS n 
1 121 GLU n 
1 122 LYS n 
1 123 ALA n 
1 124 ASP n 
1 125 ASP n 
1 126 LEU n 
1 127 GLY n 
1 128 LYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 GLU n 
1 133 GLN n 
1 134 SER n 
1 135 THR n 
1 136 LYS n 
1 137 THR n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 ARG n 
1 144 LEU n 
1 145 ALA n 
1 146 CYS n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 ILE n 
1 152 ALA n 
1 153 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     Homo 
_entity_src_gen.pdbx_gene_src_gene                 SOD1 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    CYTOPLASM 
_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                 HSOD 
_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               'TOPP 1 (STRATAGENE)' 
_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    PERIPLASM 
_entity_src_gen.pdbx_host_org_vector_type          PBR322 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              1MFM 
_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                 153 
_struct_ref_seq.pdbx_seq_align_end_ins_code   ? 
_struct_ref_seq.pdbx_db_accession             P00441 
_struct_ref_seq.db_align_beg                  1 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  153 
_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       153 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 1MFM ALA A 6   ? UNP P00441 CYS 6   'engineered mutation' 6   1 
1 1MFM GLU A 50  ? UNP P00441 PHE 50  'engineered mutation' 50  2 
1 1MFM GLU A 51  ? UNP P00441 GLY 51  'engineered mutation' 51  3 
1 1MFM SER A 111 ? UNP P00441 CYS 111 'engineered mutation' 111 4 
1 1MFM GLN A 133 ? UNP P00441 GLU 133 'engineered mutation' 133 5 
# 
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 
CD  non-polymer         . 'CADMIUM ION'     ? 'Cd 2'           112.411 
CL  non-polymer         . 'CHLORIDE ION'    ? 'Cl -1'          35.453  
CU  non-polymer         . 'COPPER (II) ION' ? 'Cu 2'           63.546  
CYS 'L-peptide linking' y CYSTEINE          ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE         ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'   ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE           ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE         ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER             ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE        ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE           ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE            ? 'C6 H15 N2 O2 1' 147.195 
PHE 'L-peptide linking' y PHENYLALANINE     ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE           ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE            ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE         ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN        ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE            ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'        ? 'Zn 2'           65.409  
# 
_exptl.entry_id          1MFM 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.13 
_exptl_crystal.density_percent_sol   42 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              8.0 
_exptl_crystal_grow.pdbx_details    'PEG 6000 15%, CDCL2 200-400 MM, TRIS 100MM, PH=8, pH 8.0' 
_exptl_crystal_grow.pdbx_pH_range   ? 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               'IMAGE PLATE' 
_diffrn_detector.type                   'MAR scanner 180 mm plate' 
_diffrn_detector.pdbx_collection_date   1996-11-01 
_diffrn_detector.details                'SEGMENTED MIRROR' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'TRIANGULAR GE CRYSTAL' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.89 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'EMBL/DESY, HAMBURG BEAMLINE BW7B' 
_diffrn_source.pdbx_synchrotron_site       'EMBL/DESY, HAMBURG' 
_diffrn_source.pdbx_synchrotron_beamline   BW7B 
_diffrn_source.pdbx_wavelength             0.89 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.entry_id                     1MFM 
_reflns.observed_criterion_sigma_I   0. 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             20. 
_reflns.d_resolution_high            1.00 
_reflns.number_obs                   681833 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.1 
_reflns.pdbx_Rmerge_I_obs            ? 
_reflns.pdbx_Rsym_value              0.061 
_reflns.pdbx_netI_over_sigmaI        9.7 
_reflns.B_iso_Wilson_estimate        ? 
_reflns.pdbx_redundancy              4.5 
_reflns.R_free_details               ? 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
# 
_reflns_shell.d_res_high             1.02 
_reflns_shell.d_res_low              1.04 
_reflns_shell.percent_possible_all   98.0 
_reflns_shell.Rmerge_I_obs           ? 
_reflns_shell.pdbx_Rsym_value        0.513 
_reflns_shell.meanI_over_sigI_obs    2.2 
_reflns_shell.pdbx_redundancy        3.3 
_reflns_shell.percent_possible_obs   ? 
_reflns_shell.number_unique_all      ? 
_reflns_shell.pdbx_diffrn_id         ? 
_reflns_shell.pdbx_ordinal           1 
# 
_refine.entry_id                                 1MFM 
_refine.ls_number_reflns_obs                     ? 
_refine.ls_number_reflns_all                     69839 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             20.0 
_refine.ls_d_res_high                            1.02 
_refine.ls_percent_reflns_obs                    99.1 
_refine.ls_R_factor_obs                          0.118 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       ? 
_refine.ls_R_factor_R_free                       ? 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 ? 
_refine.ls_number_reflns_R_free                  ? 
_refine.ls_number_parameters                     12921 
_refine.ls_number_restraints                     15655 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.B_iso_mean                               ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    ? 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      1SOS 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            ? 
_refine.overall_SU_B                             ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.pdbx_solvent_vdw_probe_radii             ? 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_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                        1MFM 
_refine_analyze.Luzzati_coordinate_error_obs    ? 
_refine_analyze.Luzzati_sigma_a_obs             ? 
_refine_analyze.Luzzati_d_res_low_obs           ? 
_refine_analyze.Luzzati_coordinate_error_free   ? 
_refine_analyze.Luzzati_sigma_a_free            ? 
_refine_analyze.Luzzati_d_res_low_free          ? 
_refine_analyze.number_disordered_residues      19 
_refine_analyze.occupancy_sum_hydrogen          ? 
_refine_analyze.occupancy_sum_non_hydrogen      ? 
_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        1152 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         13 
_refine_hist.number_atoms_solvent             283 
_refine_hist.number_atoms_total               1448 
_refine_hist.d_res_high                       1.02 
_refine_hist.d_res_low                        20.0 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
s_bond_d               0.031 ? ? ? 'X-RAY DIFFRACTION' ? 
s_angle_d              0.035 ? ? ? 'X-RAY DIFFRACTION' ? 
s_similar_dist         ?     ? ? ? 'X-RAY DIFFRACTION' ? 
s_from_restr_planes    0.435 ? ? ? 'X-RAY DIFFRACTION' ? 
s_zero_chiral_vol      0.134 ? ? ? 'X-RAY DIFFRACTION' ? 
s_non_zero_chiral_vol  0.124 ? ? ? 'X-RAY DIFFRACTION' ? 
s_anti_bump_dis_restr  0.102 ? ? ? 'X-RAY DIFFRACTION' ? 
s_rigid_bond_adp_cmpnt 0.006 ? ? ? 'X-RAY DIFFRACTION' ? 
s_similar_adp_cmpnt    0.090 ? ? ? 'X-RAY DIFFRACTION' ? 
s_approx_iso_adps      0.114 ? ? ? 'X-RAY DIFFRACTION' ? 
# 
_pdbx_refine.entry_id                                    1MFM 
_pdbx_refine.R_factor_all_no_cutoff                      ? 
_pdbx_refine.R_factor_obs_no_cutoff                      0.118 
_pdbx_refine.free_R_factor_no_cutoff                     ? 
_pdbx_refine.free_R_val_test_set_size_perc_no_cutoff     ? 
_pdbx_refine.free_R_val_test_set_ct_no_cutoff            ? 
_pdbx_refine.R_factor_all_4sig_cutoff                    ? 
_pdbx_refine.R_factor_obs_4sig_cutoff                    ? 
_pdbx_refine.free_R_factor_4sig_cutoff                   ? 
_pdbx_refine.free_R_val_test_set_size_perc_4sig_cutoff   ? 
_pdbx_refine.free_R_val_test_set_ct_4sig_cutoff          ? 
_pdbx_refine.number_reflns_obs_4sig_cutoff               ? 
_pdbx_refine.number_reflns_obs_no_cutoff                 ? 
_pdbx_refine.pdbx_refine_id                              'X-RAY DIFFRACTION' 
_pdbx_refine.free_R_error_no_cutoff                      ? 
# 
_struct.entry_id                  1MFM 
_struct.title                     'MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q AT ATOMIC RESOLUTION' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        1MFM 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            'OXIDOREDUCTASE, SUPEROXIDE ACCEPTOR, MONOMERIC MUTANT' 
# 
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 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 4 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 4 ? 
L N N 4 ? 
M N N 5 ? 
N N N 5 ? 
O N N 6 ? 
# 
_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 GLY A 56  ? THR A 58  ? GLY A 56  THR A 58  5 ? 3 
HELX_P HELX_P2 2 GLU A 132 ? THR A 137 ? GLU A 132 THR A 137 5 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
disulf1  disulf ? ? A CYS 57  SG  ? ? ? 1_555 A CYS 146 SG A ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 1.957 ? ? 
disulf2  disulf ? ? A CYS 57  SG  ? ? ? 1_555 A CYS 146 SG B ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.660 ? ? 
disulf3  disulf ? ? A CYS 57  SG  ? ? ? 1_555 A CYS 146 SG C ? A CYS 57  A CYS 146 1_555 ? ? ? ? ? ? ? 2.654 ? ? 
metalc1  metalc ? ? A ALA 1   O   ? ? ? 4_556 D CD  .   CD ? ? A ALA 1   A CD  156 1_555 ? ? ? ? ? ? ? 2.497 ? ? 
metalc2  metalc ? ? A ALA 1   N   ? ? ? 4_556 D CD  .   CD ? ? A ALA 1   A CD  156 1_555 ? ? ? ? ? ? ? 2.249 ? ? 
metalc3  metalc ? ? A GLU 24  OE1 A ? ? 1_555 H CD  .   CD ? ? A GLU 24  A CD  160 1_555 ? ? ? ? ? ? ? 2.301 ? ? 
metalc4  metalc ? ? A GLU 24  OE2 A ? ? 1_555 H CD  .   CD ? ? A GLU 24  A CD  160 1_555 ? ? ? ? ? ? ? 2.423 ? ? 
metalc5  metalc ? ? A HIS 46  ND1 ? ? ? 1_555 C CU  .   CU ? ? A HIS 46  A CU  155 1_555 ? ? ? ? ? ? ? 1.988 ? ? 
metalc6  metalc ? ? A HIS 46  ND1 ? ? ? 1_555 L CD  .   CD ? ? A HIS 46  A CD  164 1_555 ? ? ? ? ? ? ? 2.486 ? ? 
metalc7  metalc ? ? A HIS 48  NE2 ? ? ? 1_555 C CU  .   CU ? ? A HIS 48  A CU  155 1_555 ? ? ? ? ? ? ? 2.045 ? ? 
metalc8  metalc ? ? A HIS 48  NE2 ? ? ? 1_555 L CD  .   CD ? ? A HIS 48  A CD  164 1_555 ? ? ? ? ? ? ? 2.394 ? ? 
metalc9  metalc ? ? A GLU 50  OE1 A ? ? 1_555 F CD  .   CD ? ? A GLU 50  A CD  158 1_555 ? ? ? ? ? ? ? 2.050 ? ? 
metalc10 metalc ? ? A GLU 50  OE1 B ? ? 1_555 F CD  .   CD ? ? A GLU 50  A CD  158 1_555 ? ? ? ? ? ? ? 2.590 ? ? 
metalc11 metalc ? ? A GLU 50  OE2 B ? ? 1_555 F CD  .   CD ? ? A GLU 50  A CD  158 1_555 ? ? ? ? ? ? ? 2.380 ? ? 
metalc12 metalc ? ? A GLU 51  OE2 A ? ? 1_555 D CD  .   CD ? ? A GLU 51  A CD  156 1_555 ? ? ? ? ? ? ? 2.289 ? ? 
metalc13 metalc ? ? A GLU 51  OE2 B ? ? 1_555 D CD  .   CD ? ? A GLU 51  A CD  156 1_555 ? ? ? ? ? ? ? 2.203 ? ? 
metalc14 metalc ? ? A ASP 52  OD2 ? ? ? 1_555 F CD  .   CD ? ? A ASP 52  A CD  158 1_555 ? ? ? ? ? ? ? 2.250 ? ? 
metalc15 metalc ? ? A HIS 63  ND1 ? ? ? 1_555 B ZN  .   ZN ? ? A HIS 63  A ZN  154 1_555 ? ? ? ? ? ? ? 1.997 ? ? 
metalc16 metalc ? ? A HIS 63  NE2 ? ? ? 1_555 L CD  .   CD ? ? A HIS 63  A CD  164 1_555 ? ? ? ? ? ? ? 2.267 ? ? 
metalc17 metalc ? ? A HIS 71  ND1 ? ? ? 1_555 B ZN  .   ZN ? ? A HIS 71  A ZN  154 1_555 ? ? ? ? ? ? ? 2.031 ? ? 
metalc18 metalc ? ? A ASP 76  OD1 ? ? ? 1_555 I CD  .   CD ? ? A ASP 76  A CD  161 1_555 ? ? ? ? ? ? ? 2.442 ? ? 
metalc19 metalc ? ? A HIS 80  ND1 ? ? ? 1_555 B ZN  .   ZN ? ? A HIS 80  A ZN  154 1_555 ? ? ? ? ? ? ? 1.995 ? ? 
metalc20 metalc ? ? A ASP 83  OD1 ? ? ? 1_555 B ZN  .   ZN ? ? A ASP 83  A ZN  154 1_555 ? ? ? ? ? ? ? 1.971 ? ? 
metalc21 metalc ? ? A ASP 90  OD2 ? ? ? 1_655 F CD  .   CD ? ? A ASP 90  A CD  158 1_555 ? ? ? ? ? ? ? 2.163 ? ? 
metalc22 metalc ? ? A ASP 92  OD1 ? ? ? 1_655 F CD  .   CD ? ? A ASP 92  A CD  158 1_555 ? ? ? ? ? ? ? 2.377 ? ? 
metalc23 metalc ? ? A ASP 92  OD2 ? ? ? 1_655 F CD  .   CD ? ? A ASP 92  A CD  158 1_555 ? ? ? ? ? ? ? 2.370 ? ? 
metalc24 metalc ? ? A ASP 96  OD2 ? ? ? 1_655 D CD  .   CD ? ? A ASP 96  A CD  156 1_555 ? ? ? ? ? ? ? 2.278 ? ? 
metalc25 metalc ? ? A ASP 96  OD1 ? ? ? 1_655 D CD  .   CD ? ? A ASP 96  A CD  156 1_555 ? ? ? ? ? ? ? 2.504 ? ? 
metalc26 metalc ? ? A ASP 109 O   ? ? ? 1_555 J CD  .   CD ? ? A ASP 109 A CD  162 1_555 ? ? ? ? ? ? ? 2.513 ? ? 
metalc27 metalc ? ? A ASP 109 OD2 ? ? ? 1_555 K CD  .   CD ? ? A ASP 109 A CD  163 1_555 ? ? ? ? ? ? ? 2.329 ? ? 
metalc28 metalc ? ? A HIS 110 NE2 A ? ? 1_555 G CD  .   CD ? ? A HIS 110 A CD  159 1_555 ? ? ? ? ? ? ? 2.168 ? ? 
metalc29 metalc ? ? A HIS 110 ND1 B ? ? 1_555 J CD  .   CD ? ? A HIS 110 A CD  162 1_555 ? ? ? ? ? ? ? 2.518 ? ? 
metalc30 metalc ? ? A HIS 120 NE2 ? ? ? 1_555 C CU  .   CU ? ? A HIS 120 A CU  155 1_555 ? ? ? ? ? ? ? 2.201 ? ? 
metalc31 metalc ? ? A HIS 120 NE2 ? ? ? 1_555 L CD  .   CD ? ? A HIS 120 A CD  164 1_555 ? ? ? ? ? ? ? 2.272 ? ? 
metalc32 metalc ? ? A GLU 121 OE1 ? ? ? 1_555 E CD  .   CD ? ? A GLU 121 A CD  157 1_555 ? ? ? ? ? ? ? 2.326 ? ? 
metalc33 metalc ? ? A SER 142 OG  ? ? ? 1_555 E CD  .   CD ? ? A SER 142 A CD  157 1_555 ? ? ? ? ? ? ? 2.421 ? ? 
metalc34 metalc ? ? A GLN 153 OXT ? ? ? 4_556 G CD  .   CD ? ? A GLN 153 A CD  159 1_555 ? ? ? ? ? ? ? 2.528 ? ? 
metalc35 metalc ? ? A GLN 153 O   ? ? ? 4_556 G CD  .   CD ? ? A GLN 153 A CD  159 1_555 ? ? ? ? ? ? ? 2.198 ? ? 
metalc36 metalc ? ? A GLN 153 OXT ? ? ? 4_556 J CD  .   CD ? ? A GLN 153 A CD  162 1_555 ? ? ? ? ? ? ? 2.691 ? ? 
metalc37 metalc ? ? C CU  .   CU  ? ? ? 1_555 L CD  .   CD ? ? A CU  155 A CD  164 1_555 ? ? ? ? ? ? ? 1.602 ? ? 
metalc38 metalc ? ? D CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  156 A HOH 178 1_555 ? ? ? ? ? ? ? 2.270 ? ? 
metalc39 metalc ? ? E CD  .   CD  ? ? ? 1_555 M CL  .   CL ? ? A CD  157 A CL  165 1_555 ? ? ? ? ? ? ? 2.423 ? ? 
metalc40 metalc ? ? E CD  .   CD  ? ? ? 1_555 N CL  .   CL ? ? A CD  157 A CL  166 1_555 ? ? ? ? ? ? ? 2.498 ? ? 
metalc41 metalc ? ? E CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  157 A HOH 257 1_555 ? ? ? ? ? ? ? 2.395 ? ? 
metalc42 metalc ? ? E CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  157 A HOH 275 1_555 ? ? ? ? ? ? ? 2.518 ? ? 
metalc43 metalc ? ? F CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  158 A HOH 186 1_655 ? ? ? ? ? ? ? 3.067 ? ? 
metalc44 metalc ? ? G CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  159 A HOH 210 1_555 ? ? ? ? ? ? ? 2.496 ? ? 
metalc45 metalc ? ? G CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  159 A HOH 244 1_555 ? ? ? ? ? ? ? 2.457 ? ? 
metalc46 metalc ? ? G CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  159 A HOH 396 1_555 ? ? ? ? ? ? ? 2.293 ? ? 
metalc47 metalc ? ? H CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  160 A HOH 179 1_555 ? ? ? ? ? ? ? 2.532 ? ? 
metalc48 metalc ? ? H CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  160 A HOH 200 4_556 ? ? ? ? ? ? ? 2.424 ? ? 
metalc49 metalc ? ? H CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  160 A HOH 228 4_456 ? ? ? ? ? ? ? 2.470 ? ? 
metalc50 metalc ? ? H CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  160 A HOH 319 1_555 ? ? ? ? ? ? ? 2.359 ? ? 
metalc51 metalc ? ? H CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  160 A HOH 435 1_555 ? ? ? ? ? ? ? 2.568 ? ? 
metalc52 metalc ? ? I CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  161 A HOH 206 1_555 ? ? ? ? ? ? ? 2.612 ? ? 
metalc53 metalc ? ? I CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  161 A HOH 234 1_555 ? ? ? ? ? ? ? 2.582 ? ? 
metalc54 metalc ? ? I CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  161 A HOH 384 1_555 ? ? ? ? ? ? ? 2.646 ? ? 
metalc55 metalc ? ? J CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  162 A HOH 182 1_555 ? ? ? ? ? ? ? 2.356 ? ? 
metalc56 metalc ? ? J CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  162 A HOH 339 1_555 ? ? ? ? ? ? ? 2.806 ? ? 
metalc57 metalc ? ? K CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  163 A HOH 209 1_555 ? ? ? ? ? ? ? 2.552 ? ? 
metalc58 metalc ? ? K CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  163 A HOH 295 1_555 ? ? ? ? ? ? ? 2.471 ? ? 
metalc59 metalc ? ? K CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  163 A HOH 306 1_555 ? ? ? ? ? ? ? 2.886 ? ? 
metalc60 metalc ? ? K CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  163 A HOH 343 1_555 ? ? ? ? ? ? ? 2.420 ? ? 
metalc61 metalc ? ? K CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  163 A HOH 376 1_555 ? ? ? ? ? ? ? 2.633 ? ? 
metalc62 metalc ? ? K CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  163 A HOH 419 1_555 ? ? ? ? ? ? ? 2.413 ? ? 
metalc63 metalc ? ? K CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  163 A HOH 421 1_555 ? ? ? ? ? ? ? 2.996 ? ? 
metalc64 metalc ? ? L CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  164 A HOH 176 1_555 ? ? ? ? ? ? ? 2.392 ? ? 
metalc65 metalc ? ? L CD  .   CD  ? ? ? 1_555 O HOH .   O  ? ? A CD  164 A HOH 224 1_555 ? ? ? ? ? ? ? 2.594 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
A ? 5 ? 
B ? 2 ? 
C ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
A 1 2 ? anti-parallel 
A 2 3 ? anti-parallel 
A 3 4 ? anti-parallel 
A 4 5 ? anti-parallel 
B 1 2 ? anti-parallel 
C 1 2 ? anti-parallel 
C 2 3 ? 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 ILE A 149 ? ILE A 151 ? ILE A 149 ILE A 151 
A 2 THR A 2   ? LEU A 8   ? THR A 2   LEU A 8   
A 3 GLY A 16  ? GLN A 22  ? GLY A 16  GLN A 22  
A 4 VAL A 29  ? ILE A 35  ? VAL A 29  ILE A 35  
A 5 ALA A 95  ? ASP A 101 ? ALA A 95  ASP A 101 
B 1 GLY A 41  ? GLY A 44  ? GLY A 41  GLY A 44  
B 2 ASN A 86  ? ALA A 89  ? ASN A 86  ALA A 89  
C 1 PHE A 45  ? HIS A 48  ? PHE A 45  HIS A 48  
C 2 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
C 3 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
A 1 2 O GLY A 150 ? O GLY A 150 N VAL A 5   ? N VAL A 5   
A 2 3 O THR A 2   ? O THR A 2   N GLN A 22  ? N GLN A 22  
A 3 4 O ASN A 19  ? O ASN A 19  N TRP A 32  ? N TRP A 32  
A 4 5 O VAL A 29  ? O VAL A 29  N ASP A 101 ? N ASP A 101 
B 1 2 O GLY A 41  ? O GLY A 41  N ALA A 89  ? N ALA A 89  
C 1 2 O HIS A 46  ? O HIS A 46  N VAL A 118 ? N VAL A 118 
C 2 3 O LEU A 117 ? O LEU A 117 N GLY A 147 ? N GLY A 147 
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
ZN  Author   ? ?  ?   ? 5 
;ZN BINDING SITE ZINC ION (ZN2+) IS COORDINATED BY THREE HISTIDINES AND BY AN ASPARTIC ACID RESIDUE. HIS 63, HIS 71 AND HIS 80 ARE METAL COORDINATED THROUGH THE ND1 ATOM. ASP 83 IS METAL COORDINATED THROUGH OD1. THE THREE HISTIDINES COORDINATED TO THE ZN ION ARE PROTONATED AT THE OTHER N POSITION OF THE IMIDAZOLE RING, I.E. HIS 63, HIS 71 AND HIS 80 ARE ALL HIS-E.
;
CU  Author   ? ?  ?   ? 4 
;CU BINDING SITE COPPER ION (CU2+) IS COORDINATED BY THREE HISTIDINES: HIS 46, METAL COORDINATED THROUGH ND1; HIS 48, METAL COORDINATED THROUGH NE2; HIS 120 METAL COORDINATED THROUGH NE2.
;
AC1 Software A ZN 154 ? 4 'BINDING SITE FOR RESIDUE ZN A 154' 
AC2 Software A CU 155 ? 5 'BINDING SITE FOR RESIDUE CU A 155' 
AC3 Software A CD 156 ? 4 'BINDING SITE FOR RESIDUE CD A 156' 
AC4 Software A CD 157 ? 6 'BINDING SITE FOR RESIDUE CD A 157' 
AC5 Software A CD 158 ? 5 'BINDING SITE FOR RESIDUE CD A 158' 
AC6 Software A CD 159 ? 6 'BINDING SITE FOR RESIDUE CD A 159' 
AC7 Software A CD 160 ? 7 'BINDING SITE FOR RESIDUE CD A 160' 
AC8 Software A CD 161 ? 4 'BINDING SITE FOR RESIDUE CD A 161' 
AC9 Software A CD 162 ? 6 'BINDING SITE FOR RESIDUE CD A 162' 
BC1 Software A CD 163 ? 8 'BINDING SITE FOR RESIDUE CD A 163' 
BC2 Software A CD 164 ? 7 'BINDING SITE FOR RESIDUE CD A 164' 
BC3 Software A CL 165 ? 5 'BINDING SITE FOR RESIDUE CL A 165' 
BC4 Software A CL 166 ? 5 'BINDING SITE FOR RESIDUE CL A 166' 
# 
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  ZN  5 ZN  B .   ? ZN  A 154 . ? 1_555 ? 
2  ZN  5 CU  C .   ? CU  A 155 . ? 1_555 ? 
3  ZN  5 HIS A 71  ? HIS A 71  . ? 1_555 ? 
4  ZN  5 HIS A 80  ? HIS A 80  . ? 1_555 ? 
5  ZN  5 ASP A 83  ? ASP A 83  . ? 1_555 ? 
6  CU  4 CU  C .   ? CU  A 155 . ? 1_555 ? 
7  CU  4 HIS A 46  ? HIS A 46  . ? 1_555 ? 
8  CU  4 HIS A 48  ? HIS A 48  . ? 1_555 ? 
9  CU  4 HIS A 120 ? HIS A 120 . ? 1_555 ? 
10 AC1 4 HIS A 63  ? HIS A 63  . ? 1_555 ? 
11 AC1 4 HIS A 71  ? HIS A 71  . ? 1_555 ? 
12 AC1 4 HIS A 80  ? HIS A 80  . ? 1_555 ? 
13 AC1 4 ASP A 83  ? ASP A 83  . ? 1_555 ? 
14 AC2 5 HIS A 46  ? HIS A 46  . ? 1_555 ? 
15 AC2 5 HIS A 48  ? HIS A 48  . ? 1_555 ? 
16 AC2 5 HIS A 63  ? HIS A 63  . ? 1_555 ? 
17 AC2 5 HIS A 120 ? HIS A 120 . ? 1_555 ? 
18 AC2 5 CD  L .   ? CD  A 164 . ? 1_555 ? 
19 AC3 4 ALA A 1   ? ALA A 1   . ? 4_556 ? 
20 AC3 4 GLU A 51  ? GLU A 51  . ? 1_555 ? 
21 AC3 4 ASP A 96  ? ASP A 96  . ? 1_655 ? 
22 AC3 4 HOH O .   ? HOH A 178 . ? 1_555 ? 
23 AC4 6 GLU A 121 ? GLU A 121 . ? 1_555 ? 
24 AC4 6 SER A 142 ? SER A 142 . ? 1_555 ? 
25 AC4 6 CL  M .   ? CL  A 165 . ? 1_555 ? 
26 AC4 6 CL  N .   ? CL  A 166 . ? 1_555 ? 
27 AC4 6 HOH O .   ? HOH A 257 . ? 1_555 ? 
28 AC4 6 HOH O .   ? HOH A 275 . ? 1_555 ? 
29 AC5 5 GLU A 50  ? GLU A 50  . ? 1_555 ? 
30 AC5 5 ASP A 52  ? ASP A 52  . ? 1_555 ? 
31 AC5 5 ASP A 90  ? ASP A 90  . ? 1_655 ? 
32 AC5 5 ASP A 92  ? ASP A 92  . ? 1_655 ? 
33 AC5 5 HOH O .   ? HOH A 186 . ? 1_655 ? 
34 AC6 6 HIS A 110 ? HIS A 110 . ? 1_555 ? 
35 AC6 6 GLN A 153 ? GLN A 153 . ? 4_556 ? 
36 AC6 6 CD  J .   ? CD  A 162 . ? 1_555 ? 
37 AC6 6 HOH O .   ? HOH A 210 . ? 1_555 ? 
38 AC6 6 HOH O .   ? HOH A 244 . ? 1_555 ? 
39 AC6 6 HOH O .   ? HOH A 396 . ? 1_555 ? 
40 AC7 7 GLU A 24  ? GLU A 24  . ? 1_555 ? 
41 AC7 7 ASN A 53  ? ASN A 53  . ? 4_456 ? 
42 AC7 7 HOH O .   ? HOH A 179 . ? 1_555 ? 
43 AC7 7 HOH O .   ? HOH A 200 . ? 4_556 ? 
44 AC7 7 HOH O .   ? HOH A 228 . ? 4_456 ? 
45 AC7 7 HOH O .   ? HOH A 319 . ? 1_555 ? 
46 AC7 7 HOH O .   ? HOH A 435 . ? 1_555 ? 
47 AC8 4 ASP A 76  ? ASP A 76  . ? 1_555 ? 
48 AC8 4 HOH O .   ? HOH A 206 . ? 1_555 ? 
49 AC8 4 HOH O .   ? HOH A 234 . ? 1_555 ? 
50 AC8 4 HOH O .   ? HOH A 384 . ? 1_555 ? 
51 AC9 6 ASP A 109 ? ASP A 109 . ? 1_555 ? 
52 AC9 6 HIS A 110 ? HIS A 110 . ? 1_555 ? 
53 AC9 6 GLN A 153 ? GLN A 153 . ? 4_556 ? 
54 AC9 6 CD  G .   ? CD  A 159 . ? 1_555 ? 
55 AC9 6 HOH O .   ? HOH A 182 . ? 1_555 ? 
56 AC9 6 HOH O .   ? HOH A 339 . ? 1_555 ? 
57 BC1 8 ASP A 109 ? ASP A 109 . ? 1_555 ? 
58 BC1 8 HOH O .   ? HOH A 209 . ? 1_555 ? 
59 BC1 8 HOH O .   ? HOH A 295 . ? 1_555 ? 
60 BC1 8 HOH O .   ? HOH A 306 . ? 1_555 ? 
61 BC1 8 HOH O .   ? HOH A 343 . ? 1_555 ? 
62 BC1 8 HOH O .   ? HOH A 376 . ? 1_555 ? 
63 BC1 8 HOH O .   ? HOH A 419 . ? 1_555 ? 
64 BC1 8 HOH O .   ? HOH A 421 . ? 1_555 ? 
65 BC2 7 HIS A 46  ? HIS A 46  . ? 1_555 ? 
66 BC2 7 HIS A 48  ? HIS A 48  . ? 1_555 ? 
67 BC2 7 HIS A 63  ? HIS A 63  . ? 1_555 ? 
68 BC2 7 HIS A 120 ? HIS A 120 . ? 1_555 ? 
69 BC2 7 CU  C .   ? CU  A 155 . ? 1_555 ? 
70 BC2 7 HOH O .   ? HOH A 176 . ? 1_555 ? 
71 BC2 7 HOH O .   ? HOH A 224 . ? 1_555 ? 
72 BC3 5 ARG A 69  ? ARG A 69  . ? 3_655 ? 
73 BC3 5 GLU A 121 ? GLU A 121 . ? 1_555 ? 
74 BC3 5 SER A 142 ? SER A 142 . ? 1_555 ? 
75 BC3 5 CD  E .   ? CD  A 157 . ? 1_555 ? 
76 BC3 5 HOH O .   ? HOH A 322 . ? 3_655 ? 
77 BC4 5 ARG A 69  ? ARG A 69  . ? 3_655 ? 
78 BC4 5 LYS A 70  ? LYS A 70  . ? 3_655 ? 
79 BC4 5 GLU A 78  ? GLU A 78  . ? 3_655 ? 
80 BC4 5 SER A 142 ? SER A 142 . ? 1_555 ? 
81 BC4 5 CD  E .   ? CD  A 157 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          1MFM 
_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                    1MFM 
_atom_sites.fract_transf_matrix[1][1]   0.028579 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.020786 
_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]   0.012333 
_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  
CD 
CL 
CU 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 1   ? 12.973 2.447  42.775 1.00 14.13 ? 1   ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 12.646 3.609  41.955 1.00 11.24 ? 1   ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 13.435 4.813  42.485 1.00 10.69 ? 1   ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? 13.617 4.916  43.713 1.00 11.86 ? 1   ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 11.182 3.932  41.921 1.00 12.79 ? 1   ALA A CB  1 
ATOM   6    N  N   . THR A 1 2   ? 13.771 5.721  41.583 1.00 10.11 ? 2   THR A N   1 
ATOM   7    C  CA  . THR A 1 2   ? 14.398 7.010  41.906 1.00 9.44  ? 2   THR A CA  1 
ATOM   8    C  C   . THR A 1 2   ? 13.423 8.126  41.663 1.00 8.75  ? 2   THR A C   1 
ATOM   9    O  O   . THR A 1 2   ? 12.706 8.079  40.662 1.00 9.34  ? 2   THR A O   1 
ATOM   10   C  CB  . THR A 1 2   ? 15.686 7.171  41.080 1.00 11.05 ? 2   THR A CB  1 
ATOM   11   O  OG1 . THR A 1 2   ? 16.594 6.080  41.387 1.00 16.77 ? 2   THR A OG1 1 
ATOM   12   C  CG2 . THR A 1 2   ? 16.461 8.430  41.391 1.00 13.21 ? 2   THR A CG2 1 
ATOM   13   N  N   . LYS A 1 3   ? 13.395 9.132  42.522 1.00 9.25  ? 3   LYS A N   1 
ATOM   14   C  CA  . LYS A 1 3   ? 12.459 10.244 42.467 1.00 9.88  ? 3   LYS A CA  1 
ATOM   15   C  C   . LYS A 1 3   ? 13.207 11.552 42.565 1.00 9.47  ? 3   LYS A C   1 
ATOM   16   O  O   . LYS A 1 3   ? 14.177 11.651 43.342 1.00 11.12 ? 3   LYS A O   1 
ATOM   17   C  CB  . LYS A 1 3   ? 11.419 10.143 43.589 1.00 11.33 ? 3   LYS A CB  1 
ATOM   18   C  CG  . LYS A 1 3   ? 10.497 8.953  43.581 1.00 14.44 ? 3   LYS A CG  1 
ATOM   19   C  CD  A LYS A 1 3   ? 11.182 7.629  44.022 0.76 22.06 ? 3   LYS A CD  1 
ATOM   20   C  CD  B LYS A 1 3   ? 10.956 7.663  44.211 0.24 16.45 ? 3   LYS A CD  1 
ATOM   21   C  CE  A LYS A 1 3   ? 11.330 7.563  45.523 0.76 19.00 ? 3   LYS A CE  1 
ATOM   22   C  CE  B LYS A 1 3   ? 11.908 7.809  45.383 0.24 15.25 ? 3   LYS A CE  1 
ATOM   23   N  NZ  A LYS A 1 3   ? 12.489 6.791  46.004 0.76 34.95 ? 3   LYS A NZ  1 
ATOM   24   N  NZ  B LYS A 1 3   ? 12.128 6.495  46.056 0.24 13.55 ? 3   LYS A NZ  1 
ATOM   25   N  N   . ALA A 1 4   ? 12.741 12.581 41.848 1.00 8.92  ? 4   ALA A N   1 
ATOM   26   C  CA  . ALA A 1 4   ? 13.330 13.895 41.916 1.00 8.67  ? 4   ALA A CA  1 
ATOM   27   C  C   . ALA A 1 4   ? 12.230 14.948 41.864 1.00 8.29  ? 4   ALA A C   1 
ATOM   28   O  O   . ALA A 1 4   ? 11.084 14.700 41.454 1.00 8.75  ? 4   ALA A O   1 
ATOM   29   C  CB  . ALA A 1 4   ? 14.313 14.095 40.775 1.00 10.31 ? 4   ALA A CB  1 
ATOM   30   N  N   . VAL A 1 5   ? 12.610 16.154 42.298 1.00 8.44  ? 5   VAL A N   1 
ATOM   31   C  CA  . VAL A 1 5   ? 11.731 17.309 42.296 1.00 8.54  ? 5   VAL A CA  1 
ATOM   32   C  C   . VAL A 1 5   ? 12.540 18.500 41.816 1.00 7.71  ? 5   VAL A C   1 
ATOM   33   O  O   . VAL A 1 5   ? 13.667 18.721 42.247 1.00 9.23  ? 5   VAL A O   1 
ATOM   34   C  CB  . VAL A 1 5   ? 11.151 17.590 43.690 1.00 9.40  ? 5   VAL A CB  1 
ATOM   35   C  CG1 . VAL A 1 5   ? 10.287 18.812 43.687 1.00 13.65 ? 5   VAL A CG1 1 
ATOM   36   C  CG2 . VAL A 1 5   ? 10.299 16.423 44.209 1.00 11.80 ? 5   VAL A CG2 1 
ATOM   37   N  N   . ALA A 1 6   ? 11.912 19.320 40.968 1.00 7.97  ? 6   ALA A N   1 
ATOM   38   C  CA  . ALA A 1 6   ? 12.439 20.633 40.596 1.00 8.35  ? 6   ALA A CA  1 
ATOM   39   C  C   . ALA A 1 6   ? 11.419 21.683 41.004 1.00 8.21  ? 6   ALA A C   1 
ATOM   40   O  O   . ALA A 1 6   ? 10.245 21.553 40.654 1.00 10.03 ? 6   ALA A O   1 
ATOM   41   C  CB  . ALA A 1 6   ? 12.713 20.757 39.097 1.00 9.45  ? 6   ALA A CB  1 
ATOM   42   N  N   . VAL A 1 7   ? 11.825 22.704 41.715 1.00 9.04  ? 7   VAL A N   1 
ATOM   43   C  CA  . VAL A 1 7   ? 10.982 23.816 42.110 1.00 9.99  ? 7   VAL A CA  1 
ATOM   44   C  C   . VAL A 1 7   ? 11.357 24.943 41.145 1.00 9.83  ? 7   VAL A C   1 
ATOM   45   O  O   . VAL A 1 7   ? 12.458 25.487 41.180 1.00 11.28 ? 7   VAL A O   1 
ATOM   46   C  CB  . VAL A 1 7   ? 11.208 24.199 43.581 1.00 12.20 ? 7   VAL A CB  1 
ATOM   47   C  CG1 . VAL A 1 7   ? 10.385 25.437 43.868 1.00 15.90 ? 7   VAL A CG1 1 
ATOM   48   C  CG2 . VAL A 1 7   ? 10.926 23.011 44.452 1.00 15.89 ? 7   VAL A CG2 1 
ATOM   49   N  N   . LEU A 1 8   ? 10.396 25.273 40.280 1.00 10.65 ? 8   LEU A N   1 
ATOM   50   C  CA  . LEU A 1 8   ? 10.623 26.337 39.289 1.00 11.13 ? 8   LEU A CA  1 
ATOM   51   C  C   . LEU A 1 8   ? 10.308 27.691 39.908 1.00 11.69 ? 8   LEU A C   1 
ATOM   52   O  O   . LEU A 1 8   ? 9.223  27.879 40.458 1.00 13.99 ? 8   LEU A O   1 
ATOM   53   C  CB  . LEU A 1 8   ? 9.743  26.120 38.081 1.00 11.26 ? 8   LEU A CB  1 
ATOM   54   C  CG  . LEU A 1 8   ? 9.992  24.851 37.215 1.00 11.55 ? 8   LEU A CG  1 
ATOM   55   C  CD1 . LEU A 1 8   ? 8.899  24.697 36.177 1.00 13.12 ? 8   LEU A CD1 1 
ATOM   56   C  CD2 . LEU A 1 8   ? 11.357 24.962 36.547 1.00 15.16 ? 8   LEU A CD2 1 
ATOM   57   N  N   . LYS A 1 9   ? 11.243 28.617 39.807 1.00 12.48 ? 9   LYS A N   1 
ATOM   58   C  CA  . LYS A 1 9   ? 10.934 30.003 40.111 1.00 16.38 ? 9   LYS A CA  1 
ATOM   59   C  C   . LYS A 1 9   ? 11.791 30.937 39.291 1.00 13.20 ? 9   LYS A C   1 
ATOM   60   O  O   . LYS A 1 9   ? 12.756 30.534 38.655 1.00 14.49 ? 9   LYS A O   1 
ATOM   61   C  CB  . LYS A 1 9   ? 11.191 30.244 41.595 1.00 28.07 ? 9   LYS A CB  1 
ATOM   62   C  CG  . LYS A 1 9   ? 10.499 29.212 42.487 1.00 49.36 ? 9   LYS A CG  1 
ATOM   63   C  CD  . LYS A 1 9   ? 11.228 29.014 43.821 1.00 60.32 ? 9   LYS A CD  1 
ATOM   64   C  CE  . LYS A 1 9   ? 10.298 28.514 44.935 1.00 50.62 ? 9   LYS A CE  1 
ATOM   65   N  NZ  . LYS A 1 9   ? 10.454 29.353 46.125 1.00 57.79 ? 9   LYS A NZ  1 
ATOM   66   N  N   . GLY A 1 10  ? 11.316 32.175 39.238 1.00 18.07 ? 10  GLY A N   1 
ATOM   67   C  CA  . GLY A 1 10  ? 11.973 33.140 38.392 1.00 17.66 ? 10  GLY A CA  1 
ATOM   68   C  C   . GLY A 1 10  ? 11.851 34.529 38.914 1.00 21.91 ? 10  GLY A C   1 
ATOM   69   O  O   . GLY A 1 10  ? 11.532 34.705 40.079 1.00 24.75 ? 10  GLY A O   1 
ATOM   70   N  N   . ASP A 1 11  ? 12.060 35.569 38.086 1.00 22.20 ? 11  ASP A N   1 
ATOM   71   C  CA  . ASP A 1 11  ? 11.916 36.913 38.600 1.00 25.76 ? 11  ASP A CA  1 
ATOM   72   C  C   . ASP A 1 11  ? 10.493 37.462 38.553 1.00 30.80 ? 11  ASP A C   1 
ATOM   73   O  O   . ASP A 1 11  ? 10.163 38.506 39.129 1.00 32.39 ? 11  ASP A O   1 
ATOM   74   C  CB  . ASP A 1 11  ? 12.858 37.840 37.830 1.00 35.16 ? 11  ASP A CB  1 
ATOM   75   C  CG  . ASP A 1 11  ? 14.321 37.589 38.080 1.00 44.58 ? 11  ASP A CG  1 
ATOM   76   O  OD1 . ASP A 1 11  ? 14.666 37.353 39.256 1.00 64.47 ? 11  ASP A OD1 1 
ATOM   77   O  OD2 . ASP A 1 11  ? 15.217 37.737 37.200 1.00 73.49 ? 11  ASP A OD2 1 
ATOM   78   N  N   . GLY A 1 12  ? 9.597  36.789 37.880 1.00 23.58 ? 12  GLY A N   1 
ATOM   79   C  CA  . GLY A 1 12  ? 8.206  37.093 37.636 1.00 23.85 ? 12  GLY A CA  1 
ATOM   80   C  C   . GLY A 1 12  ? 7.267  36.131 38.304 1.00 29.25 ? 12  GLY A C   1 
ATOM   81   O  O   . GLY A 1 12  ? 7.649  35.522 39.281 1.00 25.62 ? 12  GLY A O   1 
ATOM   82   N  N   . PRO A 1 13  ? 6.045  35.941 37.854 1.00 21.84 ? 13  PRO A N   1 
ATOM   83   C  CA  . PRO A 1 13  ? 5.032  35.111 38.507 1.00 24.15 ? 13  PRO A CA  1 
ATOM   84   C  C   . PRO A 1 13  ? 5.024  33.640 38.199 1.00 19.88 ? 13  PRO A C   1 
ATOM   85   O  O   . PRO A 1 13  ? 4.175  32.879 38.690 1.00 22.54 ? 13  PRO A O   1 
ATOM   86   C  CB  . PRO A 1 13  ? 3.744  35.679 37.880 1.00 27.61 ? 13  PRO A CB  1 
ATOM   87   C  CG  . PRO A 1 13  ? 4.200  36.074 36.521 1.00 26.91 ? 13  PRO A CG  1 
ATOM   88   C  CD  . PRO A 1 13  ? 5.488  36.768 36.774 1.00 27.75 ? 13  PRO A CD  1 
ATOM   89   N  N   . VAL A 1 14  ? 5.966  33.176 37.371 1.00 18.29 ? 14  VAL A N   1 
ATOM   90   C  CA  . VAL A 1 14  ? 5.988  31.790 36.972 1.00 16.13 ? 14  VAL A CA  1 
ATOM   91   C  C   . VAL A 1 14  ? 6.632  30.911 38.029 1.00 13.41 ? 14  VAL A C   1 
ATOM   92   O  O   . VAL A 1 14  ? 7.747  31.118 38.504 1.00 16.93 ? 14  VAL A O   1 
ATOM   93   C  CB  . VAL A 1 14  ? 6.710  31.637 35.615 1.00 15.72 ? 14  VAL A CB  1 
ATOM   94   C  CG1 . VAL A 1 14  ? 6.717  30.166 35.180 1.00 16.18 ? 14  VAL A CG1 1 
ATOM   95   C  CG2 . VAL A 1 14  ? 6.015  32.428 34.536 1.00 17.53 ? 14  VAL A CG2 1 
ATOM   96   N  N   . GLN A 1 15  ? 5.865  29.916 38.453 1.00 14.61 ? 15  GLN A N   1 
ATOM   97   C  CA  . GLN A 1 15  ? 6.361  29.009 39.467 1.00 15.44 ? 15  GLN A CA  1 
ATOM   98   C  C   . GLN A 1 15  ? 5.681  27.664 39.408 1.00 12.97 ? 15  GLN A C   1 
ATOM   99   O  O   . GLN A 1 15  ? 4.554  27.565 38.935 1.00 13.41 ? 15  GLN A O   1 
ATOM   100  C  CB  . GLN A 1 15  ? 6.142  29.525 40.848 1.00 18.95 ? 15  GLN A CB  1 
ATOM   101  C  CG  . GLN A 1 15  ? 4.663  29.689 41.150 1.00 29.51 ? 15  GLN A CG  1 
ATOM   102  C  CD  . GLN A 1 15  ? 4.470  30.661 42.303 1.00 52.93 ? 15  GLN A CD  1 
ATOM   103  O  OE1 . GLN A 1 15  ? 3.606  31.548 42.259 1.00 91.00 ? 15  GLN A OE1 1 
ATOM   104  N  NE2 . GLN A 1 15  ? 5.308  30.518 43.321 1.00 94.74 ? 15  GLN A NE2 1 
ATOM   105  N  N   . GLY A 1 16  ? 6.317  26.633 39.904 1.00 12.06 ? 16  GLY A N   1 
ATOM   106  C  CA  . GLY A 1 16  ? 5.691  25.357 40.039 1.00 13.02 ? 16  GLY A CA  1 
ATOM   107  C  C   . GLY A 1 16  ? 6.575  24.267 40.571 1.00 10.81 ? 16  GLY A C   1 
ATOM   108  O  O   . GLY A 1 16  ? 7.744  24.480 40.713 1.00 14.04 ? 16  GLY A O   1 
ATOM   109  N  N   . ILE A 1 17  ? 5.958  23.137 40.970 1.00 11.82 ? 17  ILE A N   1 
ATOM   110  C  CA  . ILE A 1 17  ? 6.649  21.988 41.519 1.00 10.68 ? 17  ILE A CA  1 
ATOM   111  C  C   . ILE A 1 17  ? 6.548  20.874 40.501 1.00 10.18 ? 17  ILE A C   1 
ATOM   112  O  O   . ILE A 1 17  ? 5.432  20.417 40.211 1.00 11.77 ? 17  ILE A O   1 
ATOM   113  C  CB  . ILE A 1 17  ? 6.050  21.567 42.879 1.00 13.36 ? 17  ILE A CB  1 
ATOM   114  C  CG1 . ILE A 1 17  ? 6.218  22.730 43.902 1.00 21.26 ? 17  ILE A CG1 1 
ATOM   115  C  CG2 . ILE A 1 17  ? 6.735  20.322 43.371 1.00 14.41 ? 17  ILE A CG2 1 
ATOM   116  C  CD1 . ILE A 1 17  ? 5.427  22.502 45.125 1.00 26.32 ? 17  ILE A CD1 1 
ATOM   117  N  N   . ILE A 1 18  ? 7.690  20.427 39.967 1.00 8.83  ? 18  ILE A N   1 
ATOM   118  C  CA  . ILE A 1 18  ? 7.713  19.363 38.967 1.00 8.46  ? 18  ILE A CA  1 
ATOM   119  C  C   . ILE A 1 18  ? 8.348  18.113 39.599 1.00 7.67  ? 18  ILE A C   1 
ATOM   120  O  O   . ILE A 1 18  ? 9.468  18.177 40.124 1.00 8.99  ? 18  ILE A O   1 
ATOM   121  C  CB  . ILE A 1 18  ? 8.464  19.789 37.727 1.00 8.33  ? 18  ILE A CB  1 
ATOM   122  C  CG1 . ILE A 1 18  ? 7.890  21.076 37.132 1.00 11.20 ? 18  ILE A CG1 1 
ATOM   123  C  CG2 . ILE A 1 18  ? 8.519  18.657 36.710 1.00 9.36  ? 18  ILE A CG2 1 
ATOM   124  C  CD1 . ILE A 1 18  ? 6.404  20.958 36.763 1.00 15.04 ? 18  ILE A CD1 1 
ATOM   125  N  N   . ASN A 1 19  ? 7.643  17.002 39.512 1.00 7.79  ? 19  ASN A N   1 
ATOM   126  C  CA  . ASN A 1 19  ? 8.071  15.709 39.977 1.00 7.43  ? 19  ASN A CA  1 
ATOM   127  C  C   . ASN A 1 19  ? 8.588  14.857 38.816 1.00 7.32  ? 19  ASN A C   1 
ATOM   128  O  O   . ASN A 1 19  ? 8.077  14.925 37.719 1.00 7.78  ? 19  ASN A O   1 
ATOM   129  C  CB  . ASN A 1 19  ? 6.939  14.928 40.647 1.00 7.98  ? 19  ASN A CB  1 
ATOM   130  C  CG  . ASN A 1 19  ? 6.719  15.367 42.086 1.00 8.28  ? 19  ASN A CG  1 
ATOM   131  O  OD1 . ASN A 1 19  ? 6.208  16.456 42.361 1.00 9.58  ? 19  ASN A OD1 1 
ATOM   132  N  ND2 . ASN A 1 19  ? 7.165  14.521 42.978 1.00 9.50  ? 19  ASN A ND2 1 
ATOM   133  N  N   . PHE A 1 20  ? 9.561  13.999 39.170 1.00 7.78  ? 20  PHE A N   1 
ATOM   134  C  CA  . PHE A 1 20  ? 10.126 13.009 38.307 1.00 7.92  ? 20  PHE A CA  1 
ATOM   135  C  C   . PHE A 1 20  ? 10.141 11.656 39.007 1.00 7.87  ? 20  PHE A C   1 
ATOM   136  O  O   . PHE A 1 20  ? 10.413 11.614 40.221 1.00 8.48  ? 20  PHE A O   1 
ATOM   137  C  CB  . PHE A 1 20  ? 11.606 13.316 37.917 1.00 7.98  ? 20  PHE A CB  1 
ATOM   138  C  CG  . PHE A 1 20  ? 11.830 14.626 37.247 1.00 8.14  ? 20  PHE A CG  1 
ATOM   139  C  CD1 . PHE A 1 20  ? 11.760 15.830 37.921 1.00 8.92  ? 20  PHE A CD1 1 
ATOM   140  C  CD2 . PHE A 1 20  ? 12.112 14.672 35.889 1.00 8.69  ? 20  PHE A CD2 1 
ATOM   141  C  CE1 . PHE A 1 20  ? 11.960 17.037 37.289 1.00 9.47  ? 20  PHE A CE1 1 
ATOM   142  C  CE2 . PHE A 1 20  ? 12.353 15.872 35.264 1.00 10.04 ? 20  PHE A CE2 1 
ATOM   143  C  CZ  . PHE A 1 20  ? 12.277 17.065 35.956 1.00 9.91  ? 20  PHE A CZ  1 
ATOM   144  N  N   . GLU A 1 21  ? 9.911  10.584 38.260 1.00 8.00  ? 21  GLU A N   1 
ATOM   145  C  CA  . GLU A 1 21  ? 10.069 9.237  38.796 1.00 8.45  ? 21  GLU A CA  1 
ATOM   146  C  C   . GLU A 1 21  ? 10.588 8.325  37.722 1.00 8.17  ? 21  GLU A C   1 
ATOM   147  O  O   . GLU A 1 21  ? 10.110 8.358  36.581 1.00 9.39  ? 21  GLU A O   1 
ATOM   148  C  CB  . GLU A 1 21  ? 8.776  8.673  39.403 1.00 10.93 ? 21  GLU A CB  1 
ATOM   149  C  CG  . GLU A 1 21  ? 9.029  7.307  40.045 1.00 13.92 ? 21  GLU A CG  1 
ATOM   150  C  CD  . GLU A 1 21  ? 7.954  6.635  40.797 1.00 27.21 ? 21  GLU A CD  1 
ATOM   151  O  OE1 . GLU A 1 21  ? 7.140  5.960  40.209 1.00 40.32 ? 21  GLU A OE1 1 
ATOM   152  O  OE2 . GLU A 1 21  ? 8.017  6.456  42.027 1.00 47.46 ? 21  GLU A OE2 1 
ATOM   153  N  N   . GLN A 1 22  ? 11.537 7.483  38.076 1.00 8.60  ? 22  GLN A N   1 
ATOM   154  C  CA  . GLN A 1 22  ? 12.120 6.495  37.189 1.00 8.28  ? 22  GLN A CA  1 
ATOM   155  C  C   . GLN A 1 22  ? 12.151 5.172  37.939 1.00 8.32  ? 22  GLN A C   1 
ATOM   156  O  O   . GLN A 1 22  ? 12.931 5.036  38.876 1.00 9.80  ? 22  GLN A O   1 
ATOM   157  C  CB  . GLN A 1 22  ? 13.455 6.910  36.657 1.00 7.97  ? 22  GLN A CB  1 
ATOM   158  C  CG  . GLN A 1 22  ? 14.002 6.039  35.565 1.00 8.36  ? 22  GLN A CG  1 
ATOM   159  C  CD  . GLN A 1 22  ? 15.358 6.362  35.125 1.00 8.12  ? 22  GLN A CD  1 
ATOM   160  O  OE1 . GLN A 1 22  ? 16.129 7.027  35.880 1.00 9.90  ? 22  GLN A OE1 1 
ATOM   161  N  NE2 . GLN A 1 22  ? 15.616 6.005  33.889 1.00 9.74  ? 22  GLN A NE2 1 
ATOM   162  N  N   . LYS A 1 23  ? 11.320 4.212  37.562 1.00 9.05  ? 23  LYS A N   1 
ATOM   163  C  CA  . LYS A 1 23  ? 11.241 2.960  38.307 1.00 9.85  ? 23  LYS A CA  1 
ATOM   164  C  C   . LYS A 1 23  ? 12.431 2.050  38.111 1.00 10.37 ? 23  LYS A C   1 
ATOM   165  O  O   . LYS A 1 23  ? 12.728 1.264  38.987 1.00 13.38 ? 23  LYS A O   1 
ATOM   166  C  CB  . LYS A 1 23  ? 9.908  2.254  38.088 1.00 10.89 ? 23  LYS A CB  1 
ATOM   167  C  CG  . LYS A 1 23  ? 8.754  3.000  38.735 1.00 11.59 ? 23  LYS A CG  1 
ATOM   168  C  CD  . LYS A 1 23  ? 7.444  2.309  38.687 1.00 14.38 ? 23  LYS A CD  1 
ATOM   169  C  CE  . LYS A 1 23  ? 6.267  3.001  39.323 1.00 15.18 ? 23  LYS A CE  1 
ATOM   170  N  NZ  . LYS A 1 23  ? 6.548  3.273  40.781 1.00 14.65 ? 23  LYS A NZ  1 
ATOM   171  N  N   . GLU A 1 24  ? 13.029 2.084  36.921 1.00 10.98 ? 24  GLU A N   1 
ATOM   172  C  CA  . GLU A 1 24  ? 14.185 1.248  36.633 1.00 12.05 ? 24  GLU A CA  1 
ATOM   173  C  C   . GLU A 1 24  ? 15.325 2.139  36.140 1.00 11.78 ? 24  GLU A C   1 
ATOM   174  O  O   . GLU A 1 24  ? 15.032 3.139  35.492 1.00 13.31 ? 24  GLU A O   1 
ATOM   175  C  CB  A GLU A 1 24  ? 13.919 0.272  35.490 0.48 11.82 ? 24  GLU A CB  1 
ATOM   176  C  CB  B GLU A 1 24  ? 13.939 0.130  35.640 0.52 18.64 ? 24  GLU A CB  1 
ATOM   177  C  CG  A GLU A 1 24  ? 12.796 -0.696 35.740 0.48 14.88 ? 24  GLU A CG  1 
ATOM   178  C  CG  B GLU A 1 24  ? 12.608 -0.582 35.824 0.52 27.07 ? 24  GLU A CG  1 
ATOM   179  C  CD  A GLU A 1 24  ? 12.959 -1.523 36.974 0.48 13.95 ? 24  GLU A CD  1 
ATOM   180  C  CD  B GLU A 1 24  ? 12.672 -1.936 35.144 0.52 35.03 ? 24  GLU A CD  1 
ATOM   181  O  OE1 A GLU A 1 24  ? 14.020 -1.680 37.630 0.48 17.56 ? 24  GLU A OE1 1 
ATOM   182  O  OE1 B GLU A 1 24  ? 12.417 -2.007 33.921 0.52 58.33 ? 24  GLU A OE1 1 
ATOM   183  O  OE2 A GLU A 1 24  ? 11.915 -2.177 37.280 0.48 18.18 ? 24  GLU A OE2 1 
ATOM   184  O  OE2 B GLU A 1 24  ? 12.982 -2.914 35.864 0.52 52.55 ? 24  GLU A OE2 1 
ATOM   185  N  N   . SER A 1 25  ? 16.579 1.751  36.380 1.00 13.48 ? 25  SER A N   1 
ATOM   186  C  CA  . SER A 1 25  ? 17.684 2.658  36.048 1.00 16.89 ? 25  SER A CA  1 
ATOM   187  C  C   . SER A 1 25  ? 17.749 2.971  34.549 1.00 17.49 ? 25  SER A C   1 
ATOM   188  O  O   . SER A 1 25  ? 18.279 4.011  34.209 1.00 22.92 ? 25  SER A O   1 
ATOM   189  C  CB  . SER A 1 25  ? 19.000 2.079  36.586 1.00 17.94 ? 25  SER A CB  1 
ATOM   190  O  OG  . SER A 1 25  ? 19.260 0.832  35.904 1.00 19.01 ? 25  SER A OG  1 
ATOM   191  N  N   . ASN A 1 26  ? 17.231 2.063  33.697 1.00 15.58 ? 26  ASN A N   1 
ATOM   192  C  CA  . ASN A 1 26  ? 17.158 2.268  32.263 1.00 18.75 ? 26  ASN A CA  1 
ATOM   193  C  C   . ASN A 1 26  ? 15.713 2.220  31.750 1.00 17.12 ? 26  ASN A C   1 
ATOM   194  O  O   . ASN A 1 26  ? 15.449 1.928  30.592 1.00 21.55 ? 26  ASN A O   1 
ATOM   195  C  CB  . ASN A 1 26  ? 18.014 1.185  31.575 1.00 22.93 ? 26  ASN A CB  1 
ATOM   196  C  CG  . ASN A 1 26  ? 17.395 -0.177 31.781 1.00 19.33 ? 26  ASN A CG  1 
ATOM   197  O  OD1 . ASN A 1 26  ? 16.432 -0.353 32.518 1.00 19.20 ? 26  ASN A OD1 1 
ATOM   198  N  ND2 . ASN A 1 26  ? 17.983 -1.171 31.091 1.00 25.51 ? 26  ASN A ND2 1 
ATOM   199  N  N   . GLY A 1 27  ? 14.778 2.616  32.634 1.00 13.85 ? 27  GLY A N   1 
ATOM   200  C  CA  . GLY A 1 27  ? 13.387 2.650  32.226 1.00 12.90 ? 27  GLY A CA  1 
ATOM   201  C  C   . GLY A 1 27  ? 12.961 4.084  31.933 1.00 9.92  ? 27  GLY A C   1 
ATOM   202  O  O   . GLY A 1 27  ? 13.726 5.041  32.107 1.00 9.98  ? 27  GLY A O   1 
ATOM   203  N  N   . PRO A 1 28  ? 11.715 4.270  31.481 1.00 10.18 ? 28  PRO A N   1 
ATOM   204  C  CA  . PRO A 1 28  ? 11.219 5.633  31.191 1.00 10.31 ? 28  PRO A CA  1 
ATOM   205  C  C   . PRO A 1 28  ? 11.173 6.458  32.459 1.00 9.04  ? 28  PRO A C   1 
ATOM   206  O  O   . PRO A 1 28  ? 10.979 5.967  33.573 1.00 10.08 ? 28  PRO A O   1 
ATOM   207  C  CB  . PRO A 1 28  ? 9.824  5.408  30.641 1.00 14.08 ? 28  PRO A CB  1 
ATOM   208  C  CG  . PRO A 1 28  ? 9.397  4.081  31.230 1.00 18.57 ? 28  PRO A CG  1 
ATOM   209  C  CD  . PRO A 1 28  ? 10.667 3.257  31.291 1.00 14.45 ? 28  PRO A CD  1 
ATOM   210  N  N   . VAL A 1 29  ? 11.291 7.771  32.251 1.00 9.31  ? 29  VAL A N   1 
ATOM   211  C  CA  . VAL A 1 29  ? 11.098 8.757  33.294 1.00 8.50  ? 29  VAL A CA  1 
ATOM   212  C  C   . VAL A 1 29  ? 9.738  9.411  33.103 1.00 8.73  ? 29  VAL A C   1 
ATOM   213  O  O   . VAL A 1 29  ? 9.411  9.834  31.999 1.00 10.68 ? 29  VAL A O   1 
ATOM   214  C  CB  . VAL A 1 29  ? 12.220 9.821  33.323 1.00 9.15  ? 29  VAL A CB  1 
ATOM   215  C  CG1 . VAL A 1 29  ? 11.996 10.835 34.450 1.00 9.89  ? 29  VAL A CG1 1 
ATOM   216  C  CG2 . VAL A 1 29  ? 13.604 9.191  33.401 1.00 9.90  ? 29  VAL A CG2 1 
ATOM   217  N  N   . LYS A 1 30  ? 8.968  9.447  34.163 1.00 8.65  ? 30  LYS A N   1 
ATOM   218  C  CA  . LYS A 1 30  ? 7.701  10.132 34.187 1.00 8.54  ? 30  LYS A CA  1 
ATOM   219  C  C   . LYS A 1 30  ? 7.840  11.465 34.890 1.00 8.11  ? 30  LYS A C   1 
ATOM   220  O  O   . LYS A 1 30  ? 8.531  11.564 35.897 1.00 8.89  ? 30  LYS A O   1 
ATOM   221  C  CB  . LYS A 1 30  ? 6.661  9.218  34.828 1.00 11.72 ? 30  LYS A CB  1 
ATOM   222  C  CG  . LYS A 1 30  ? 6.439  8.013  33.882 1.00 16.09 ? 30  LYS A CG  1 
ATOM   223  C  CD  . LYS A 1 30  ? 5.456  7.004  34.339 1.00 18.84 ? 30  LYS A CD  1 
ATOM   224  C  CE  . LYS A 1 30  ? 5.388  5.876  33.250 1.00 25.01 ? 30  LYS A CE  1 
ATOM   225  N  NZ  . LYS A 1 30  ? 4.310  4.948  33.590 1.00 33.20 ? 30  LYS A NZ  1 
ATOM   226  N  N   . VAL A 1 31  ? 7.211  12.503 34.339 1.00 8.20  ? 31  VAL A N   1 
ATOM   227  C  CA  . VAL A 1 31  ? 7.363  13.872 34.767 1.00 8.33  ? 31  VAL A CA  1 
ATOM   228  C  C   . VAL A 1 31  ? 5.972  14.503 34.913 1.00 8.23  ? 31  VAL A C   1 
ATOM   229  O  O   . VAL A 1 31  ? 5.160  14.349 33.982 1.00 9.47  ? 31  VAL A O   1 
ATOM   230  C  CB  . VAL A 1 31  ? 8.176  14.698 33.778 1.00 8.52  ? 31  VAL A CB  1 
ATOM   231  C  CG1 . VAL A 1 31  ? 8.534  16.051 34.377 1.00 9.98  ? 31  VAL A CG1 1 
ATOM   232  C  CG2 . VAL A 1 31  ? 9.439  13.986 33.353 1.00 10.25 ? 31  VAL A CG2 1 
ATOM   233  N  N   . TRP A 1 32  ? 5.670  15.147 36.014 1.00 8.32  ? 32  TRP A N   1 
ATOM   234  C  CA  . TRP A 1 32  ? 4.377  15.721 36.216 1.00 8.22  ? 32  TRP A CA  1 
ATOM   235  C  C   . TRP A 1 32  ? 4.426  16.922 37.136 1.00 8.23  ? 32  TRP A C   1 
ATOM   236  O  O   . TRP A 1 32  ? 5.379  17.142 37.865 1.00 9.73  ? 32  TRP A O   1 
ATOM   237  C  CB  . TRP A 1 32  ? 3.361  14.677 36.731 1.00 8.75  ? 32  TRP A CB  1 
ATOM   238  C  CG  . TRP A 1 32  ? 3.588  14.238 38.111 1.00 8.76  ? 32  TRP A CG  1 
ATOM   239  C  CD1 . TRP A 1 32  ? 3.025  14.742 39.248 1.00 9.73  ? 32  TRP A CD1 1 
ATOM   240  C  CD2 . TRP A 1 32  ? 4.438  13.190 38.549 1.00 8.59  ? 32  TRP A CD2 1 
ATOM   241  N  NE1 . TRP A 1 32  ? 3.465  14.048 40.347 1.00 10.52 ? 32  TRP A NE1 1 
ATOM   242  C  CE2 . TRP A 1 32  ? 4.344  13.087 39.965 1.00 9.59  ? 32  TRP A CE2 1 
ATOM   243  C  CE3 . TRP A 1 32  ? 5.300  12.294 37.892 1.00 9.59  ? 32  TRP A CE3 1 
ATOM   244  C  CZ2 . TRP A 1 32  ? 5.066  12.158 40.694 1.00 10.07 ? 32  TRP A CZ2 1 
ATOM   245  C  CZ3 . TRP A 1 32  ? 6.020  11.363 38.614 1.00 10.26 ? 32  TRP A CZ3 1 
ATOM   246  C  CH2 . TRP A 1 32  ? 5.902  11.304 40.030 1.00 10.55 ? 32  TRP A CH2 1 
ATOM   247  N  N   . GLY A 1 33  ? 3.360  17.683 37.113 1.00 9.40  ? 33  GLY A N   1 
ATOM   248  C  CA  . GLY A 1 33  ? 3.200  18.845 38.001 1.00 9.36  ? 33  GLY A CA  1 
ATOM   249  C  C   A GLY A 1 33  ? 2.730  20.061 37.245 0.40 8.19  ? 33  GLY A C   1 
ATOM   250  C  C   B GLY A 1 33  ? 2.386  19.918 37.330 0.60 9.47  ? 33  GLY A C   1 
ATOM   251  O  O   A GLY A 1 33  ? 2.789  20.235 36.042 0.40 9.27  ? 33  GLY A O   1 
ATOM   252  O  O   B GLY A 1 33  ? 1.900  19.674 36.255 0.60 14.74 ? 33  GLY A O   1 
ATOM   253  N  N   . SER A 1 34  ? 2.239  21.061 37.946 1.00 12.30 ? 34  SER A N   1 
ATOM   254  C  CA  . SER A 1 34  ? 1.624  22.215 37.371 1.00 12.05 ? 34  SER A CA  1 
ATOM   255  C  C   . SER A 1 34  ? 2.565  23.418 37.517 1.00 12.76 ? 34  SER A C   1 
ATOM   256  O  O   . SER A 1 34  ? 3.252  23.632 38.522 1.00 18.59 ? 34  SER A O   1 
ATOM   257  C  CB  . SER A 1 34  ? 0.228  22.486 37.976 1.00 17.72 ? 34  SER A CB  1 
ATOM   258  O  OG  . SER A 1 34  ? -0.698 21.408 37.704 1.00 18.27 ? 34  SER A OG  1 
ATOM   259  N  N   . ILE A 1 35  ? 2.511  24.274 36.505 1.00 11.23 ? 35  ILE A N   1 
ATOM   260  C  CA  . ILE A 1 35  ? 3.190  25.544 36.497 1.00 10.75 ? 35  ILE A CA  1 
ATOM   261  C  C   . ILE A 1 35  ? 2.170  26.628 36.402 1.00 12.02 ? 35  ILE A C   1 
ATOM   262  O  O   . ILE A 1 35  ? 1.320  26.598 35.503 1.00 14.39 ? 35  ILE A O   1 
ATOM   263  C  CB  . ILE A 1 35  ? 4.196  25.641 35.317 1.00 11.43 ? 35  ILE A CB  1 
ATOM   264  C  CG1 . ILE A 1 35  ? 5.122  24.402 35.246 1.00 11.50 ? 35  ILE A CG1 1 
ATOM   265  C  CG2 . ILE A 1 35  ? 4.988  26.913 35.381 1.00 12.61 ? 35  ILE A CG2 1 
ATOM   266  C  CD1 . ILE A 1 35  ? 5.976  24.320 34.000 1.00 13.42 ? 35  ILE A CD1 1 
ATOM   267  N  N   . LYS A 1 36  ? 2.260  27.648 37.259 1.00 12.41 ? 36  LYS A N   1 
ATOM   268  C  CA  . LYS A 1 36  ? 1.313  28.765 37.236 1.00 13.17 ? 36  LYS A CA  1 
ATOM   269  C  C   . LYS A 1 36  ? 2.040  30.018 36.758 1.00 14.09 ? 36  LYS A C   1 
ATOM   270  O  O   . LYS A 1 36  ? 3.286  30.108 36.764 1.00 14.76 ? 36  LYS A O   1 
ATOM   271  C  CB  . LYS A 1 36  ? 0.647  28.950 38.588 1.00 16.36 ? 36  LYS A CB  1 
ATOM   272  C  CG  . LYS A 1 36  ? 1.569  29.463 39.663 1.00 22.54 ? 36  LYS A CG  1 
ATOM   273  C  CD  . LYS A 1 36  ? 0.776  29.767 40.929 1.00 34.34 ? 36  LYS A CD  1 
ATOM   274  C  CE  . LYS A 1 36  ? 0.604  28.393 41.587 1.00 62.15 ? 36  LYS A CE  1 
ATOM   275  N  NZ  . LYS A 1 36  ? -0.170 28.488 42.852 1.00 98.80 ? 36  LYS A NZ  1 
ATOM   276  N  N   . GLY A 1 37  ? 1.241  31.061 36.503 1.00 15.08 ? 37  GLY A N   1 
ATOM   277  C  CA  . GLY A 1 37  ? 1.783  32.373 36.194 1.00 17.00 ? 37  GLY A CA  1 
ATOM   278  C  C   . GLY A 1 37  ? 2.150  32.577 34.719 1.00 16.23 ? 37  GLY A C   1 
ATOM   279  O  O   . GLY A 1 37  ? 2.730  33.582 34.343 1.00 18.56 ? 37  GLY A O   1 
ATOM   280  N  N   . LEU A 1 38  ? 1.805  31.646 33.838 1.00 16.12 ? 38  LEU A N   1 
ATOM   281  C  CA  . LEU A 1 38  ? 2.217  31.702 32.437 1.00 16.32 ? 38  LEU A CA  1 
ATOM   282  C  C   . LEU A 1 38  ? 1.205  32.422 31.565 1.00 18.56 ? 38  LEU A C   1 
ATOM   283  O  O   . LEU A 1 38  ? 0.014  32.356 31.801 1.00 18.85 ? 38  LEU A O   1 
ATOM   284  C  CB  . LEU A 1 38  ? 2.337  30.247 31.893 1.00 15.25 ? 38  LEU A CB  1 
ATOM   285  C  CG  . LEU A 1 38  ? 3.514  29.448 32.468 1.00 15.15 ? 38  LEU A CG  1 
ATOM   286  C  CD1 . LEU A 1 38  ? 3.299  27.957 32.168 1.00 16.60 ? 38  LEU A CD1 1 
ATOM   287  C  CD2 . LEU A 1 38  ? 4.838  29.910 31.871 1.00 16.74 ? 38  LEU A CD2 1 
ATOM   288  N  N   . THR A 1 39  ? 1.656  32.979 30.464 1.00 20.68 ? 39  THR A N   1 
ATOM   289  C  CA  . THR A 1 39  ? 0.701  33.438 29.445 1.00 21.71 ? 39  THR A CA  1 
ATOM   290  C  C   . THR A 1 39  ? 0.054  32.214 28.790 1.00 20.20 ? 39  THR A C   1 
ATOM   291  O  O   . THR A 1 39  ? 0.669  31.163 28.610 1.00 19.08 ? 39  THR A O   1 
ATOM   292  C  CB  . THR A 1 39  ? 1.382  34.283 28.374 1.00 22.68 ? 39  THR A CB  1 
ATOM   293  O  OG1 . THR A 1 39  ? 2.454  33.547 27.786 1.00 23.96 ? 39  THR A OG1 1 
ATOM   294  C  CG2 . THR A 1 39  ? 1.951  35.540 29.000 1.00 29.18 ? 39  THR A CG2 1 
ATOM   295  N  N   . GLU A 1 40  ? -1.176 32.426 28.332 1.00 20.98 ? 40  GLU A N   1 
ATOM   296  C  CA  . GLU A 1 40  ? -1.911 31.365 27.654 1.00 20.59 ? 40  GLU A CA  1 
ATOM   297  C  C   . GLU A 1 40  ? -1.170 30.879 26.410 1.00 21.36 ? 40  GLU A C   1 
ATOM   298  O  O   . GLU A 1 40  ? -0.653 31.692 25.633 1.00 28.69 ? 40  GLU A O   1 
ATOM   299  C  CB  . GLU A 1 40  ? -3.306 31.812 27.307 1.00 22.71 ? 40  GLU A CB  1 
ATOM   300  C  CG  . GLU A 1 40  ? -4.182 30.790 26.650 1.00 28.17 ? 40  GLU A CG  1 
ATOM   301  C  CD  . GLU A 1 40  ? -5.594 31.258 26.327 1.00 49.49 ? 40  GLU A CD  1 
ATOM   302  O  OE1 . GLU A 1 40  ? -5.975 32.321 26.823 1.00 53.36 ? 40  GLU A OE1 1 
ATOM   303  O  OE2 . GLU A 1 40  ? -6.226 30.540 25.537 1.00 52.90 ? 40  GLU A OE2 1 
ATOM   304  N  N   . GLY A 1 41  ? -1.095 29.540 26.222 1.00 21.34 ? 41  GLY A N   1 
ATOM   305  C  CA  . GLY A 1 41  ? -0.454 28.956 25.040 1.00 19.89 ? 41  GLY A CA  1 
ATOM   306  C  C   . GLY A 1 41  ? 0.780  28.147 25.375 1.00 18.27 ? 41  GLY A C   1 
ATOM   307  O  O   . GLY A 1 41  ? 0.960  27.725 26.540 1.00 16.70 ? 41  GLY A O   1 
ATOM   308  N  N   . LEU A 1 42  ? 1.539  27.829 24.320 1.00 19.61 ? 42  LEU A N   1 
ATOM   309  C  CA  . LEU A 1 42  ? 2.647  26.891 24.419 1.00 16.88 ? 42  LEU A CA  1 
ATOM   310  C  C   . LEU A 1 42  ? 3.884  27.580 24.971 1.00 15.30 ? 42  LEU A C   1 
ATOM   311  O  O   . LEU A 1 42  ? 4.265  28.681 24.591 1.00 17.42 ? 42  LEU A O   1 
ATOM   312  C  CB  A LEU A 1 42  ? 2.930  26.260 23.055 0.47 18.05 ? 42  LEU A CB  1 
ATOM   313  C  CB  B LEU A 1 42  ? 2.963  26.513 22.946 0.53 22.78 ? 42  LEU A CB  1 
ATOM   314  C  CG  A LEU A 1 42  ? 2.071  25.070 22.651 0.47 20.14 ? 42  LEU A CG  1 
ATOM   315  C  CG  B LEU A 1 42  ? 1.898  25.669 22.252 0.53 20.34 ? 42  LEU A CG  1 
ATOM   316  C  CD1 A LEU A 1 42  ? 0.613  25.451 22.436 0.47 22.09 ? 42  LEU A CD1 1 
ATOM   317  C  CD1 B LEU A 1 42  ? 2.230  25.408 20.774 0.53 25.41 ? 42  LEU A CD1 1 
ATOM   318  C  CD2 A LEU A 1 42  ? 2.588  24.398 21.382 0.47 23.47 ? 42  LEU A CD2 1 
ATOM   319  C  CD2 B LEU A 1 42  ? 1.774  24.367 23.039 0.53 22.79 ? 42  LEU A CD2 1 
ATOM   320  N  N   . HIS A 1 43  ? 4.620  26.835 25.809 1.00 13.87 ? 43  HIS A N   1 
ATOM   321  C  CA  . HIS A 1 43  ? 5.864  27.298 26.383 1.00 13.11 ? 43  HIS A CA  1 
ATOM   322  C  C   . HIS A 1 43  ? 6.879  26.168 26.322 1.00 12.84 ? 43  HIS A C   1 
ATOM   323  O  O   . HIS A 1 43  ? 6.643  25.072 26.828 1.00 12.03 ? 43  HIS A O   1 
ATOM   324  C  CB  . HIS A 1 43  ? 5.636  27.646 27.869 1.00 13.32 ? 43  HIS A CB  1 
ATOM   325  C  CG  . HIS A 1 43  ? 4.765  28.850 27.995 1.00 13.96 ? 43  HIS A CG  1 
ATOM   326  N  ND1 . HIS A 1 43  ? 5.262  30.138 27.987 1.00 16.01 ? 43  HIS A ND1 1 
ATOM   327  C  CD2 . HIS A 1 43  ? 3.408  28.990 28.102 1.00 16.03 ? 43  HIS A CD2 1 
ATOM   328  C  CE1 . HIS A 1 43  ? 4.258  31.015 28.133 1.00 18.02 ? 43  HIS A CE1 1 
ATOM   329  N  NE2 . HIS A 1 43  ? 3.114  30.323 28.142 1.00 20.69 ? 43  HIS A NE2 1 
ATOM   330  N  N   . GLY A 1 44  ? 8.052  26.437 25.776 1.00 11.02 ? 44  GLY A N   1 
ATOM   331  C  CA  . GLY A 1 44  ? 9.140  25.466 25.789 1.00 10.48 ? 44  GLY A CA  1 
ATOM   332  C  C   . GLY A 1 44  ? 9.527  24.998 27.194 1.00 10.46 ? 44  GLY A C   1 
ATOM   333  O  O   . GLY A 1 44  ? 9.459  25.771 28.162 1.00 10.57 ? 44  GLY A O   1 
ATOM   334  N  N   . PHE A 1 45  ? 9.928  23.741 27.307 1.00 10.18 ? 45  PHE A N   1 
ATOM   335  C  CA  . PHE A 1 45  ? 10.114 23.071 28.586 1.00 9.53  ? 45  PHE A CA  1 
ATOM   336  C  C   . PHE A 1 45  ? 11.269 22.072 28.418 1.00 9.16  ? 45  PHE A C   1 
ATOM   337  O  O   . PHE A 1 45  ? 11.118 21.077 27.719 1.00 10.61 ? 45  PHE A O   1 
ATOM   338  C  CB  . PHE A 1 45  ? 8.828  22.337 28.983 1.00 10.16 ? 45  PHE A CB  1 
ATOM   339  C  CG  . PHE A 1 45  ? 8.832  21.672 30.309 1.00 9.43  ? 45  PHE A CG  1 
ATOM   340  C  CD1 . PHE A 1 45  ? 8.853  22.417 31.496 1.00 10.93 ? 45  PHE A CD1 1 
ATOM   341  C  CD2 . PHE A 1 45  ? 8.772  20.309 30.438 1.00 9.92  ? 45  PHE A CD2 1 
ATOM   342  C  CE1 . PHE A 1 45  ? 8.807  21.763 32.713 1.00 11.82 ? 45  PHE A CE1 1 
ATOM   343  C  CE2 . PHE A 1 45  ? 8.742  19.665 31.661 1.00 10.83 ? 45  PHE A CE2 1 
ATOM   344  C  CZ  . PHE A 1 45  ? 8.717  20.402 32.797 1.00 10.65 ? 45  PHE A CZ  1 
ATOM   345  N  N   . HIS A 1 46  ? 12.433 22.407 29.001 1.00 8.93  ? 46  HIS A N   1 
ATOM   346  C  CA  . HIS A 1 46  ? 13.619 21.642 28.702 1.00 9.38  ? 46  HIS A CA  1 
ATOM   347  C  C   . HIS A 1 46  ? 14.518 21.488 29.946 1.00 9.03  ? 46  HIS A C   1 
ATOM   348  O  O   . HIS A 1 46  ? 14.477 22.279 30.883 1.00 8.97  ? 46  HIS A O   1 
ATOM   349  C  CB  . HIS A 1 46  ? 14.543 22.400 27.678 1.00 15.24 ? 46  HIS A CB  1 
ATOM   350  C  CG  . HIS A 1 46  ? 13.814 22.944 26.501 1.00 11.25 ? 46  HIS A CG  1 
ATOM   351  N  ND1 . HIS A 1 46  ? 13.855 24.253 26.179 1.00 12.26 ? 46  HIS A ND1 1 
ATOM   352  C  CD2 . HIS A 1 46  ? 12.976 22.343 25.635 1.00 12.41 ? 46  HIS A CD2 1 
ATOM   353  C  CE1 . HIS A 1 46  ? 13.100 24.428 25.122 1.00 11.61 ? 46  HIS A CE1 1 
ATOM   354  N  NE2 . HIS A 1 46  ? 12.573 23.294 24.739 1.00 10.36 ? 46  HIS A NE2 1 
ATOM   355  N  N   . VAL A 1 47  ? 15.357 20.461 29.883 1.00 8.76  ? 47  VAL A N   1 
ATOM   356  C  CA  . VAL A 1 47  ? 16.481 20.322 30.779 1.00 8.09  ? 47  VAL A CA  1 
ATOM   357  C  C   . VAL A 1 47  ? 17.683 20.995 30.118 1.00 8.12  ? 47  VAL A C   1 
ATOM   358  O  O   . VAL A 1 47  ? 18.111 20.630 29.030 1.00 9.03  ? 47  VAL A O   1 
ATOM   359  C  CB  . VAL A 1 47  ? 16.766 18.885 31.142 1.00 8.55  ? 47  VAL A CB  1 
ATOM   360  C  CG1 . VAL A 1 47  ? 17.925 18.829 32.165 1.00 9.26  ? 47  VAL A CG1 1 
ATOM   361  C  CG2 . VAL A 1 47  ? 15.523 18.153 31.607 1.00 9.59  ? 47  VAL A CG2 1 
ATOM   362  N  N   . HIS A 1 48  ? 18.271 21.957 30.827 1.00 8.79  ? 48  HIS A N   1 
ATOM   363  C  CA  . HIS A 1 48  ? 19.461 22.672 30.415 1.00 8.53  ? 48  HIS A CA  1 
ATOM   364  C  C   . HIS A 1 48  ? 20.677 22.129 31.141 1.00 8.86  ? 48  HIS A C   1 
ATOM   365  O  O   . HIS A 1 48  ? 20.605 21.488 32.165 1.00 9.76  ? 48  HIS A O   1 
ATOM   366  C  CB  . HIS A 1 48  ? 19.315 24.161 30.687 1.00 8.93  ? 48  HIS A CB  1 
ATOM   367  C  CG  . HIS A 1 48  ? 18.394 24.836 29.746 1.00 9.99  ? 48  HIS A CG  1 
ATOM   368  N  ND1 . HIS A 1 48  ? 18.619 26.092 29.306 1.00 18.08 ? 48  HIS A ND1 1 
ATOM   369  C  CD2 . HIS A 1 48  ? 17.217 24.474 29.161 1.00 14.71 ? 48  HIS A CD2 1 
ATOM   370  C  CE1 . HIS A 1 48  ? 17.618 26.442 28.457 1.00 17.48 ? 48  HIS A CE1 1 
ATOM   371  N  NE2 . HIS A 1 48  ? 16.773 25.495 28.350 1.00 13.25 ? 48  HIS A NE2 1 
ATOM   372  N  N   . GLU A 1 49  ? 21.823 22.403 30.534 1.00 10.12 ? 49  GLU A N   1 
ATOM   373  C  CA  . GLU A 1 49  ? 23.134 21.896 30.915 1.00 11.23 ? 49  GLU A CA  1 
ATOM   374  C  C   . GLU A 1 49  ? 23.552 22.399 32.308 1.00 10.95 ? 49  GLU A C   1 
ATOM   375  O  O   . GLU A 1 49  ? 24.242 21.724 33.047 1.00 11.50 ? 49  GLU A O   1 
ATOM   376  C  CB  . GLU A 1 49  ? 24.136 22.364 29.860 1.00 17.52 ? 49  GLU A CB  1 
ATOM   377  C  CG  . GLU A 1 49  ? 25.558 21.845 30.119 1.00 18.59 ? 49  GLU A CG  1 
ATOM   378  C  CD  . GLU A 1 49  ? 26.477 22.313 28.995 1.00 30.81 ? 49  GLU A CD  1 
ATOM   379  O  OE1 . GLU A 1 49  ? 26.483 21.688 27.946 1.00 30.82 ? 49  GLU A OE1 1 
ATOM   380  O  OE2 . GLU A 1 49  ? 27.182 23.312 29.189 1.00 29.62 ? 49  GLU A OE2 1 
ATOM   381  N  N   . GLU A 1 50  ? 23.152 23.579 32.700 1.00 10.94 ? 50  GLU A N   1 
ATOM   382  C  CA  . GLU A 1 50  ? 23.748 24.197 33.880 1.00 11.30 ? 50  GLU A CA  1 
ATOM   383  C  C   . GLU A 1 50  ? 23.619 23.353 35.144 1.00 10.48 ? 50  GLU A C   1 
ATOM   384  O  O   . GLU A 1 50  ? 22.530 22.886 35.505 1.00 10.34 ? 50  GLU A O   1 
ATOM   385  C  CB  A GLU A 1 50  ? 23.254 25.605 34.168 0.29 12.67 ? 50  GLU A CB  1 
ATOM   386  C  CB  B GLU A 1 50  ? 23.061 25.531 34.140 0.71 14.94 ? 50  GLU A CB  1 
ATOM   387  C  CG  A GLU A 1 50  ? 23.715 26.234 35.457 0.29 11.40 ? 50  GLU A CG  1 
ATOM   388  C  CG  B GLU A 1 50  ? 23.612 26.389 35.233 0.71 15.44 ? 50  GLU A CG  1 
ATOM   389  C  CD  A GLU A 1 50  ? 25.172 26.616 35.539 0.29 11.19 ? 50  GLU A CD  1 
ATOM   390  C  CD  B GLU A 1 50  ? 25.093 26.590 35.023 0.71 14.70 ? 50  GLU A CD  1 
ATOM   391  O  OE1 A GLU A 1 50  ? 26.057 25.907 35.015 0.29 9.67  ? 50  GLU A OE1 1 
ATOM   392  O  OE1 B GLU A 1 50  ? 25.535 26.825 33.875 0.71 16.27 ? 50  GLU A OE1 1 
ATOM   393  O  OE2 A GLU A 1 50  ? 25.498 27.682 36.112 0.29 14.11 ? 50  GLU A OE2 1 
ATOM   394  O  OE2 B GLU A 1 50  ? 25.845 26.549 36.015 0.71 16.05 ? 50  GLU A OE2 1 
ATOM   395  N  N   . GLU A 1 51  ? 24.739 23.146 35.794 1.00 12.04 ? 51  GLU A N   1 
ATOM   396  C  CA  . GLU A 1 51  ? 24.822 22.395 37.028 1.00 10.86 ? 51  GLU A CA  1 
ATOM   397  C  C   . GLU A 1 51  ? 25.679 23.083 38.067 1.00 11.67 ? 51  GLU A C   1 
ATOM   398  O  O   . GLU A 1 51  ? 25.901 22.526 39.140 1.00 12.94 ? 51  GLU A O   1 
ATOM   399  C  CB  A GLU A 1 51  ? 25.398 21.010 36.633 0.30 10.43 ? 51  GLU A CB  1 
ATOM   400  C  CB  B GLU A 1 51  ? 25.132 20.914 36.876 0.71 14.25 ? 51  GLU A CB  1 
ATOM   401  C  CG  A GLU A 1 51  ? 26.855 21.130 36.169 0.30 13.70 ? 51  GLU A CG  1 
ATOM   402  C  CG  B GLU A 1 51  ? 26.082 20.412 35.811 0.71 12.56 ? 51  GLU A CG  1 
ATOM   403  C  CD  A GLU A 1 51  ? 27.456 19.797 35.791 0.30 13.18 ? 51  GLU A CD  1 
ATOM   404  C  CD  B GLU A 1 51  ? 27.515 20.820 35.937 0.71 10.91 ? 51  GLU A CD  1 
ATOM   405  O  OE1 A GLU A 1 51  ? 26.645 18.851 35.788 0.30 11.71 ? 51  GLU A OE1 1 
ATOM   406  O  OE1 B GLU A 1 51  ? 27.770 21.913 36.491 0.71 14.64 ? 51  GLU A OE1 1 
ATOM   407  O  OE2 A GLU A 1 51  ? 28.677 19.630 35.527 0.30 14.07 ? 51  GLU A OE2 1 
ATOM   408  O  OE2 B GLU A 1 51  ? 28.456 20.046 35.590 0.71 13.59 ? 51  GLU A OE2 1 
ATOM   409  N  N   . ASP A 1 52  ? 26.109 24.322 37.831 1.00 12.49 ? 52  ASP A N   1 
ATOM   410  C  CA  . ASP A 1 52  ? 26.858 25.053 38.891 1.00 12.36 ? 52  ASP A CA  1 
ATOM   411  C  C   . ASP A 1 52  ? 25.812 25.739 39.765 1.00 16.35 ? 52  ASP A C   1 
ATOM   412  O  O   . ASP A 1 52  ? 24.626 25.646 39.645 1.00 19.78 ? 52  ASP A O   1 
ATOM   413  C  CB  . ASP A 1 52  ? 27.876 25.999 38.276 1.00 12.30 ? 52  ASP A CB  1 
ATOM   414  C  CG  . ASP A 1 52  ? 28.899 25.217 37.483 1.00 11.42 ? 52  ASP A CG  1 
ATOM   415  O  OD1 . ASP A 1 52  ? 29.566 24.431 38.162 1.00 14.39 ? 52  ASP A OD1 1 
ATOM   416  O  OD2 . ASP A 1 52  ? 29.059 25.386 36.264 1.00 12.92 ? 52  ASP A OD2 1 
ATOM   417  N  N   . ASN A 1 53  ? 26.248 26.335 40.867 1.00 20.02 ? 53  ASN A N   1 
ATOM   418  C  CA  . ASN A 1 53  ? 25.305 26.926 41.797 1.00 23.50 ? 53  ASN A CA  1 
ATOM   419  C  C   . ASN A 1 53  ? 25.190 28.435 41.470 1.00 30.77 ? 53  ASN A C   1 
ATOM   420  O  O   . ASN A 1 53  ? 25.382 29.355 42.287 1.00 34.73 ? 53  ASN A O   1 
ATOM   421  C  CB  A ASN A 1 53  ? 25.908 26.948 43.211 0.56 24.49 ? 53  ASN A CB  1 
ATOM   422  C  CB  B ASN A 1 53  ? 25.685 26.568 43.216 0.44 32.19 ? 53  ASN A CB  1 
ATOM   423  C  CG  A ASN A 1 53  ? 25.841 25.655 43.971 0.56 21.99 ? 53  ASN A CG  1 
ATOM   424  C  CG  B ASN A 1 53  ? 26.817 25.571 43.370 0.44 26.83 ? 53  ASN A CG  1 
ATOM   425  O  OD1 A ASN A 1 53  ? 26.802 25.124 44.552 0.56 27.86 ? 53  ASN A OD1 1 
ATOM   426  O  OD1 B ASN A 1 53  ? 27.733 25.364 42.564 0.44 33.87 ? 53  ASN A OD1 1 
ATOM   427  N  ND2 A ASN A 1 53  ? 24.674 25.060 43.941 0.56 19.36 ? 53  ASN A ND2 1 
ATOM   428  N  ND2 B ASN A 1 53  ? 26.867 24.974 44.578 0.44 31.92 ? 53  ASN A ND2 1 
ATOM   429  N  N   . THR A 1 54  ? 24.823 28.706 40.197 1.00 22.62 ? 54  THR A N   1 
ATOM   430  C  CA  . THR A 1 54  ? 24.618 30.062 39.713 1.00 34.05 ? 54  THR A CA  1 
ATOM   431  C  C   . THR A 1 54  ? 23.238 30.567 40.109 1.00 37.23 ? 54  THR A C   1 
ATOM   432  O  O   . THR A 1 54  ? 22.322 29.838 40.461 1.00 72.79 ? 54  THR A O   1 
ATOM   433  C  CB  . THR A 1 54  ? 24.695 30.155 38.179 1.00 38.70 ? 54  THR A CB  1 
ATOM   434  O  OG1 . THR A 1 54  ? 23.830 29.141 37.644 1.00 65.89 ? 54  THR A OG1 1 
ATOM   435  C  CG2 . THR A 1 54  ? 26.132 29.984 37.707 1.00 54.92 ? 54  THR A CG2 1 
ATOM   436  N  N   . ALA A 1 55  ? 23.105 31.895 40.074 1.00 45.31 ? 55  ALA A N   1 
ATOM   437  C  CA  . ALA A 1 55  ? 21.905 32.510 40.612 1.00 48.32 ? 55  ALA A CA  1 
ATOM   438  C  C   . ALA A 1 55  ? 20.829 32.408 39.519 1.00 55.41 ? 55  ALA A C   1 
ATOM   439  O  O   . ALA A 1 55  ? 21.116 32.893 38.416 1.00 66.16 ? 55  ALA A O   1 
ATOM   440  C  CB  . ALA A 1 55  ? 22.268 33.917 40.974 1.00 71.39 ? 55  ALA A CB  1 
ATOM   441  N  N   . GLY A 1 56  ? 19.782 31.658 39.825 1.00 56.37 ? 56  GLY A N   1 
ATOM   442  C  CA  . GLY A 1 56  ? 18.570 31.292 39.185 1.00 76.73 ? 56  GLY A CA  1 
ATOM   443  C  C   . GLY A 1 56  ? 18.832 30.941 37.719 1.00 68.23 ? 56  GLY A C   1 
ATOM   444  O  O   . GLY A 1 56  ? 19.671 30.097 37.412 1.00 75.19 ? 56  GLY A O   1 
ATOM   445  N  N   . CYS A 1 57  ? 18.113 31.642 36.847 1.00 49.83 ? 57  CYS A N   1 
ATOM   446  C  CA  . CYS A 1 57  ? 18.181 31.398 35.415 1.00 49.83 ? 57  CYS A CA  1 
ATOM   447  C  C   . CYS A 1 57  ? 19.057 32.472 34.760 1.00 62.19 ? 57  CYS A C   1 
ATOM   448  O  O   . CYS A 1 57  ? 18.458 33.031 33.848 1.00 70.20 ? 57  CYS A O   1 
ATOM   449  C  CB  . CYS A 1 57  ? 16.840 31.703 34.839 1.00 40.47 ? 57  CYS A CB  1 
ATOM   450  S  SG  . CYS A 1 57  ? 15.298 30.934 35.080 1.00 37.49 ? 57  CYS A SG  1 
ATOM   451  N  N   . THR A 1 58  ? 20.187 32.733 35.386 1.00 63.84 ? 58  THR A N   1 
ATOM   452  C  CA  . THR A 1 58  ? 21.175 33.633 34.797 1.00 57.40 ? 58  THR A CA  1 
ATOM   453  C  C   . THR A 1 58  ? 22.110 32.842 33.891 1.00 56.18 ? 58  THR A C   1 
ATOM   454  O  O   . THR A 1 58  ? 22.574 33.375 32.863 1.00 91.50 ? 58  THR A O   1 
ATOM   455  C  CB  . THR A 1 58  ? 21.896 34.455 35.881 1.00 69.81 ? 58  THR A CB  1 
ATOM   456  O  OG1 . THR A 1 58  ? 22.626 33.585 36.771 1.00 80.00 ? 58  THR A OG1 1 
ATOM   457  C  CG2 . THR A 1 58  ? 20.806 35.109 36.743 1.00 66.75 ? 58  THR A CG2 1 
ATOM   458  N  N   . SER A 1 59  ? 22.456 31.607 34.230 1.00 57.96 ? 59  SER A N   1 
ATOM   459  C  CA  . SER A 1 59  ? 23.274 30.826 33.298 1.00 53.54 ? 59  SER A CA  1 
ATOM   460  C  C   . SER A 1 59  ? 22.771 29.384 33.152 1.00 38.17 ? 59  SER A C   1 
ATOM   461  O  O   . SER A 1 59  ? 23.470 28.418 33.432 1.00 79.71 ? 59  SER A O   1 
ATOM   462  C  CB  . SER A 1 59  ? 24.716 30.818 33.811 1.00 57.08 ? 59  SER A CB  1 
ATOM   463  O  OG  . SER A 1 59  ? 25.296 29.536 33.563 1.00 29.79 ? 59  SER A OG  1 
ATOM   464  N  N   . ALA A 1 60  ? 21.494 29.257 32.723 1.00 29.59 ? 60  ALA A N   1 
ATOM   465  C  CA  . ALA A 1 60  ? 20.938 27.923 32.491 1.00 29.89 ? 60  ALA A CA  1 
ATOM   466  C  C   . ALA A 1 60  ? 21.720 27.158 31.406 1.00 28.06 ? 60  ALA A C   1 
ATOM   467  O  O   . ALA A 1 60  ? 21.802 25.937 31.406 1.00 31.68 ? 60  ALA A O   1 
ATOM   468  C  CB  . ALA A 1 60  ? 19.477 28.084 32.061 1.00 35.68 ? 60  ALA A CB  1 
ATOM   469  N  N   . GLY A 1 61  ? 22.312 27.987 30.532 1.00 20.29 ? 61  GLY A N   1 
ATOM   470  C  CA  . GLY A 1 61  ? 23.127 27.362 29.447 1.00 27.59 ? 61  GLY A CA  1 
ATOM   471  C  C   . GLY A 1 61  ? 22.339 26.976 28.241 1.00 24.41 ? 61  GLY A C   1 
ATOM   472  O  O   . GLY A 1 61  ? 21.119 27.174 28.137 1.00 22.75 ? 61  GLY A O   1 
ATOM   473  N  N   . PRO A 1 62  ? 23.046 26.229 27.387 1.00 16.19 ? 62  PRO A N   1 
ATOM   474  C  CA  . PRO A 1 62  ? 22.385 25.487 26.343 1.00 15.88 ? 62  PRO A CA  1 
ATOM   475  C  C   . PRO A 1 62  ? 21.594 24.337 26.934 1.00 10.90 ? 62  PRO A C   1 
ATOM   476  O  O   . PRO A 1 62  ? 21.648 24.023 28.117 1.00 12.10 ? 62  PRO A O   1 
ATOM   477  C  CB  . PRO A 1 62  ? 23.561 25.001 25.491 1.00 21.64 ? 62  PRO A CB  1 
ATOM   478  C  CG  . PRO A 1 62  ? 24.652 24.825 26.489 1.00 23.19 ? 62  PRO A CG  1 
ATOM   479  C  CD  . PRO A 1 62  ? 24.499 26.028 27.400 1.00 20.48 ? 62  PRO A CD  1 
ATOM   480  N  N   . HIS A 1 63  ? 20.853 23.674 26.045 1.00 11.39 ? 63  HIS A N   1 
ATOM   481  C  CA  . HIS A 1 63  ? 20.132 22.475 26.405 1.00 10.35 ? 63  HIS A CA  1 
ATOM   482  C  C   . HIS A 1 63  ? 21.117 21.388 26.819 1.00 10.17 ? 63  HIS A C   1 
ATOM   483  O  O   . HIS A 1 63  ? 22.219 21.288 26.303 1.00 12.09 ? 63  HIS A O   1 
ATOM   484  C  CB  . HIS A 1 63  ? 19.285 21.995 25.236 1.00 10.86 ? 63  HIS A CB  1 
ATOM   485  C  CG  . HIS A 1 63  ? 18.223 22.982 24.915 1.00 10.48 ? 63  HIS A CG  1 
ATOM   486  N  ND1 . HIS A 1 63  ? 17.274 22.748 23.926 1.00 9.78  ? 63  HIS A ND1 1 
ATOM   487  C  CD2 . HIS A 1 63  ? 17.913 24.153 25.501 1.00 11.59 ? 63  HIS A CD2 1 
ATOM   488  C  CE1 . HIS A 1 63  ? 16.470 23.794 23.942 1.00 10.52 ? 63  HIS A CE1 1 
ATOM   489  N  NE2 . HIS A 1 63  ? 16.795 24.669 24.867 1.00 11.70 ? 63  HIS A NE2 1 
ATOM   490  N  N   . PHE A 1 64  ? 20.643 20.522 27.708 1.00 9.00  ? 64  PHE A N   1 
ATOM   491  C  CA  . PHE A 1 64  ? 21.455 19.374 28.100 1.00 9.12  ? 64  PHE A CA  1 
ATOM   492  C  C   . PHE A 1 64  ? 21.572 18.421 26.909 1.00 8.82  ? 64  PHE A C   1 
ATOM   493  O  O   . PHE A 1 64  ? 20.581 17.920 26.366 1.00 9.45  ? 64  PHE A O   1 
ATOM   494  C  CB  . PHE A 1 64  ? 20.796 18.700 29.300 1.00 9.95  ? 64  PHE A CB  1 
ATOM   495  C  CG  . PHE A 1 64  ? 21.566 17.510 29.804 1.00 9.76  ? 64  PHE A CG  1 
ATOM   496  C  CD1 . PHE A 1 64  ? 22.936 17.618 30.127 1.00 11.36 ? 64  PHE A CD1 1 
ATOM   497  C  CD2 . PHE A 1 64  ? 20.946 16.278 30.044 1.00 10.94 ? 64  PHE A CD2 1 
ATOM   498  C  CE1 . PHE A 1 64  ? 23.620 16.522 30.598 1.00 12.21 ? 64  PHE A CE1 1 
ATOM   499  C  CE2 . PHE A 1 64  ? 21.637 15.203 30.539 1.00 12.34 ? 64  PHE A CE2 1 
ATOM   500  C  CZ  . PHE A 1 64  ? 22.959 15.334 30.812 1.00 12.95 ? 64  PHE A CZ  1 
ATOM   501  N  N   . ASN A 1 65  ? 22.806 18.257 26.459 1.00 10.38 ? 65  ASN A N   1 
ATOM   502  C  CA  . ASN A 1 65  ? 23.078 17.646 25.163 1.00 10.98 ? 65  ASN A CA  1 
ATOM   503  C  C   . ASN A 1 65  ? 24.352 16.815 25.213 1.00 11.24 ? 65  ASN A C   1 
ATOM   504  O  O   . ASN A 1 65  ? 25.294 17.065 24.444 1.00 13.50 ? 65  ASN A O   1 
ATOM   505  C  CB  . ASN A 1 65  ? 23.190 18.768 24.130 1.00 11.07 ? 65  ASN A CB  1 
ATOM   506  C  CG  . ASN A 1 65  ? 23.324 18.218 22.703 1.00 11.84 ? 65  ASN A CG  1 
ATOM   507  O  OD1 . ASN A 1 65  ? 22.877 17.124 22.363 1.00 11.21 ? 65  ASN A OD1 1 
ATOM   508  N  ND2 . ASN A 1 65  ? 23.803 19.085 21.815 1.00 13.25 ? 65  ASN A ND2 1 
ATOM   509  N  N   . PRO A 1 66  ? 24.422 15.809 26.057 1.00 11.49 ? 66  PRO A N   1 
ATOM   510  C  CA  . PRO A 1 66  ? 25.620 14.997 26.219 1.00 13.63 ? 66  PRO A CA  1 
ATOM   511  C  C   . PRO A 1 66  ? 25.968 14.208 24.990 1.00 17.35 ? 66  PRO A C   1 
ATOM   512  O  O   . PRO A 1 66  ? 27.090 13.762 24.860 1.00 22.90 ? 66  PRO A O   1 
ATOM   513  C  CB  . PRO A 1 66  ? 25.285 14.095 27.417 1.00 14.28 ? 66  PRO A CB  1 
ATOM   514  C  CG  . PRO A 1 66  ? 23.788 13.920 27.339 1.00 13.29 ? 66  PRO A CG  1 
ATOM   515  C  CD  . PRO A 1 66  ? 23.355 15.343 26.990 1.00 12.57 ? 66  PRO A CD  1 
ATOM   516  N  N   . LEU A 1 67  ? 25.049 13.940 24.081 1.00 15.24 ? 67  LEU A N   1 
ATOM   517  C  CA  . LEU A 1 67  ? 25.318 13.232 22.868 1.00 18.47 ? 67  LEU A CA  1 
ATOM   518  C  C   . LEU A 1 67  ? 25.619 14.117 21.651 1.00 18.95 ? 67  LEU A C   1 
ATOM   519  O  O   . LEU A 1 67  ? 25.793 13.602 20.551 1.00 24.47 ? 67  LEU A O   1 
ATOM   520  C  CB  . LEU A 1 67  ? 24.189 12.229 22.572 1.00 19.85 ? 67  LEU A CB  1 
ATOM   521  C  CG  . LEU A 1 67  ? 23.974 11.162 23.672 1.00 24.83 ? 67  LEU A CG  1 
ATOM   522  C  CD1 . LEU A 1 67  ? 22.831 10.250 23.269 1.00 29.39 ? 67  LEU A CD1 1 
ATOM   523  C  CD2 . LEU A 1 67  ? 25.248 10.377 23.914 1.00 31.63 ? 67  LEU A CD2 1 
ATOM   524  N  N   . SER A 1 68  ? 25.682 15.447 21.858 1.00 17.45 ? 68  SER A N   1 
ATOM   525  C  CA  . SER A 1 68  ? 26.034 16.374 20.798 1.00 19.14 ? 68  SER A CA  1 
ATOM   526  C  C   . SER A 1 68  ? 25.180 16.206 19.554 1.00 19.03 ? 68  SER A C   1 
ATOM   527  O  O   . SER A 1 68  ? 25.704 16.111 18.444 1.00 27.50 ? 68  SER A O   1 
ATOM   528  C  CB  . SER A 1 68  ? 27.505 16.247 20.410 1.00 23.54 ? 68  SER A CB  1 
ATOM   529  O  OG  . SER A 1 68  ? 28.344 16.372 21.572 1.00 32.11 ? 68  SER A OG  1 
ATOM   530  N  N   . ARG A 1 69  ? 23.918 16.292 19.762 1.00 13.09 ? 69  ARG A N   1 
ATOM   531  C  CA  . ARG A 1 69  ? 22.915 16.207 18.730 1.00 13.30 ? 69  ARG A CA  1 
ATOM   532  C  C   . ARG A 1 69  ? 22.267 17.571 18.496 1.00 12.48 ? 69  ARG A C   1 
ATOM   533  O  O   . ARG A 1 69  ? 22.520 18.545 19.201 1.00 13.31 ? 69  ARG A O   1 
ATOM   534  C  CB  . ARG A 1 69  ? 21.848 15.195 19.105 1.00 14.45 ? 69  ARG A CB  1 
ATOM   535  C  CG  . ARG A 1 69  ? 22.561 13.914 19.520 1.00 18.64 ? 69  ARG A CG  1 
ATOM   536  C  CD  . ARG A 1 69  ? 21.692 12.740 19.350 1.00 28.00 ? 69  ARG A CD  1 
ATOM   537  N  NE  . ARG A 1 69  ? 21.210 12.403 18.042 1.00 26.27 ? 69  ARG A NE  1 
ATOM   538  C  CZ  . ARG A 1 69  ? 20.122 11.722 17.717 1.00 18.58 ? 69  ARG A CZ  1 
ATOM   539  N  NH1 . ARG A 1 69  ? 19.290 11.293 18.683 1.00 30.96 ? 69  ARG A NH1 1 
ATOM   540  N  NH2 . ARG A 1 69  ? 19.880 11.500 16.424 1.00 21.06 ? 69  ARG A NH2 1 
ATOM   541  N  N   . LYS A 1 70  ? 21.392 17.626 17.477 1.00 13.80 ? 70  LYS A N   1 
ATOM   542  C  CA  . LYS A 1 70  ? 20.600 18.797 17.179 1.00 13.52 ? 70  LYS A CA  1 
ATOM   543  C  C   . LYS A 1 70  ? 19.302 18.780 18.001 1.00 10.72 ? 70  LYS A C   1 
ATOM   544  O  O   . LYS A 1 70  ? 18.828 17.777 18.464 1.00 12.72 ? 70  LYS A O   1 
ATOM   545  C  CB  . LYS A 1 70  ? 20.265 18.817 15.684 1.00 17.60 ? 70  LYS A CB  1 
ATOM   546  C  CG  . LYS A 1 70  ? 21.509 18.890 14.799 1.00 30.55 ? 70  LYS A CG  1 
ATOM   547  C  CD  . LYS A 1 70  ? 21.078 18.777 13.332 1.00 47.41 ? 70  LYS A CD  1 
ATOM   548  C  CE  . LYS A 1 70  ? 21.745 17.591 12.656 1.00 61.91 ? 70  LYS A CE  1 
ATOM   549  N  NZ  . LYS A 1 70  ? 21.051 17.087 11.432 1.00 67.95 ? 70  LYS A NZ  1 
ATOM   550  N  N   . HIS A 1 71  ? 18.712 19.980 18.107 1.00 10.58 ? 71  HIS A N   1 
ATOM   551  C  CA  . HIS A 1 71  ? 17.457 20.177 18.830 1.00 10.08 ? 71  HIS A CA  1 
ATOM   552  C  C   . HIS A 1 71  ? 16.283 19.550 18.075 1.00 10.64 ? 71  HIS A C   1 
ATOM   553  O  O   . HIS A 1 71  ? 16.210 19.663 16.861 1.00 11.93 ? 71  HIS A O   1 
ATOM   554  C  CB  . HIS A 1 71  ? 17.183 21.671 19.042 1.00 10.30 ? 71  HIS A CB  1 
ATOM   555  C  CG  . HIS A 1 71  ? 15.956 21.967 19.808 1.00 9.54  ? 71  HIS A CG  1 
ATOM   556  N  ND1 . HIS A 1 71  ? 15.856 21.770 21.185 1.00 9.55  ? 71  HIS A ND1 1 
ATOM   557  C  CD2 . HIS A 1 71  ? 14.760 22.340 19.355 1.00 10.27 ? 71  HIS A CD2 1 
ATOM   558  C  CE1 . HIS A 1 71  ? 14.621 22.085 21.508 1.00 9.72  ? 71  HIS A CE1 1 
ATOM   559  N  NE2 . HIS A 1 71  ? 13.906 22.433 20.450 1.00 10.42 ? 71  HIS A NE2 1 
ATOM   560  N  N   . GLY A 1 72  ? 15.359 18.955 18.824 1.00 10.33 ? 72  GLY A N   1 
ATOM   561  C  CA  . GLY A 1 72  ? 14.128 18.435 18.277 1.00 11.73 ? 72  GLY A CA  1 
ATOM   562  C  C   . GLY A 1 72  ? 13.027 18.490 19.303 1.00 10.79 ? 72  GLY A C   1 
ATOM   563  O  O   . GLY A 1 72  ? 13.212 18.898 20.445 1.00 11.42 ? 72  GLY A O   1 
ATOM   564  N  N   . GLY A 1 73  ? 11.828 18.050 18.919 1.00 12.83 ? 73  GLY A N   1 
ATOM   565  C  CA  . GLY A 1 73  ? 10.803 17.723 19.877 1.00 13.48 ? 73  GLY A CA  1 
ATOM   566  C  C   . GLY A 1 73  ? 11.100 16.374 20.539 1.00 13.25 ? 73  GLY A C   1 
ATOM   567  O  O   . GLY A 1 73  ? 11.933 15.568 20.093 1.00 14.01 ? 73  GLY A O   1 
ATOM   568  N  N   . PRO A 1 74  ? 10.353 16.111 21.615 1.00 13.62 ? 74  PRO A N   1 
ATOM   569  C  CA  . PRO A 1 74  ? 10.634 14.866 22.388 1.00 13.87 ? 74  PRO A CA  1 
ATOM   570  C  C   . PRO A 1 74  ? 10.449 13.587 21.596 1.00 14.80 ? 74  PRO A C   1 
ATOM   571  O  O   . PRO A 1 74  ? 11.103 12.573 21.924 1.00 16.59 ? 74  PRO A O   1 
ATOM   572  C  CB  . PRO A 1 74  ? 9.652  14.925 23.556 1.00 15.48 ? 74  PRO A CB  1 
ATOM   573  C  CG  . PRO A 1 74  ? 8.596  15.877 23.057 1.00 17.05 ? 74  PRO A CG  1 
ATOM   574  C  CD  . PRO A 1 74  ? 9.308  16.925 22.217 1.00 14.30 ? 74  PRO A CD  1 
ATOM   575  N  N   . LYS A 1 75  ? 9.526  13.613 20.621 1.00 16.47 ? 75  LYS A N   1 
ATOM   576  C  CA  . LYS A 1 75  ? 9.263  12.416 19.797 1.00 19.56 ? 75  LYS A CA  1 
ATOM   577  C  C   . LYS A 1 75  ? 10.190 12.328 18.596 1.00 19.98 ? 75  LYS A C   1 
ATOM   578  O  O   . LYS A 1 75  ? 10.098 11.342 17.827 1.00 22.15 ? 75  LYS A O   1 
ATOM   579  C  CB  . LYS A 1 75  ? 7.787  12.415 19.449 1.00 32.40 ? 75  LYS A CB  1 
ATOM   580  C  CG  . LYS A 1 75  ? 6.951  12.077 20.645 1.00 36.31 ? 75  LYS A CG  1 
ATOM   581  C  CD  . LYS A 1 75  ? 7.604  11.317 21.775 1.00 47.38 ? 75  LYS A CD  1 
ATOM   582  C  CE  . LYS A 1 75  ? 6.685  10.956 22.942 1.00 64.92 ? 75  LYS A CE  1 
ATOM   583  N  NZ  . LYS A 1 75  ? 7.412  10.222 24.022 1.00 72.27 ? 75  LYS A NZ  1 
ATOM   584  N  N   . ASP A 1 76  ? 11.028 13.331 18.324 1.00 20.37 ? 76  ASP A N   1 
ATOM   585  C  CA  . ASP A 1 76  ? 11.881 13.331 17.128 1.00 22.37 ? 76  ASP A CA  1 
ATOM   586  C  C   . ASP A 1 76  ? 13.068 12.419 17.436 1.00 26.25 ? 76  ASP A C   1 
ATOM   587  O  O   . ASP A 1 76  ? 13.540 12.346 18.604 1.00 21.42 ? 76  ASP A O   1 
ATOM   588  C  CB  . ASP A 1 76  ? 12.353 14.747 16.768 1.00 22.70 ? 76  ASP A CB  1 
ATOM   589  C  CG  . ASP A 1 76  ? 11.263 15.591 16.115 1.00 38.61 ? 76  ASP A CG  1 
ATOM   590  O  OD1 . ASP A 1 76  ? 10.669 15.164 15.123 1.00 39.86 ? 76  ASP A OD1 1 
ATOM   591  O  OD2 . ASP A 1 76  ? 10.983 16.733 16.575 1.00 25.63 ? 76  ASP A OD2 1 
ATOM   592  N  N   . GLU A 1 77  ? 13.454 11.686 16.399 1.00 29.49 ? 77  GLU A N   1 
ATOM   593  C  CA  . GLU A 1 77  ? 14.686 10.885 16.610 1.00 37.93 ? 77  GLU A CA  1 
ATOM   594  C  C   . GLU A 1 77  ? 15.915 11.752 16.945 1.00 23.93 ? 77  GLU A C   1 
ATOM   595  O  O   . GLU A 1 77  ? 16.708 11.354 17.807 1.00 29.68 ? 77  GLU A O   1 
ATOM   596  C  CB  . GLU A 1 77  ? 14.962 10.069 15.356 1.00 46.92 ? 77  GLU A CB  1 
ATOM   597  N  N   . GLU A 1 78  ? 16.088 12.866 16.236 1.00 18.62 ? 78  GLU A N   1 
ATOM   598  C  CA  . GLU A 1 78  ? 17.229 13.761 16.458 1.00 16.15 ? 78  GLU A CA  1 
ATOM   599  C  C   . GLU A 1 78  ? 16.716 14.833 17.445 1.00 13.66 ? 78  GLU A C   1 
ATOM   600  O  O   . GLU A 1 78  ? 15.824 15.620 17.171 1.00 14.83 ? 78  GLU A O   1 
ATOM   601  C  CB  . GLU A 1 78  ? 17.655 14.407 15.139 1.00 19.98 ? 78  GLU A CB  1 
ATOM   602  N  N   . ARG A 1 79  ? 17.278 14.762 18.653 1.00 12.37 ? 79  ARG A N   1 
ATOM   603  C  CA  . ARG A 1 79  ? 16.922 15.696 19.718 1.00 11.40 ? 79  ARG A CA  1 
ATOM   604  C  C   . ARG A 1 79  ? 18.077 15.703 20.736 1.00 10.73 ? 79  ARG A C   1 
ATOM   605  O  O   . ARG A 1 79  ? 18.880 14.796 20.761 1.00 11.89 ? 79  ARG A O   1 
ATOM   606  C  CB  . ARG A 1 79  ? 15.607 15.292 20.428 1.00 11.70 ? 79  ARG A CB  1 
ATOM   607  C  CG  . ARG A 1 79  ? 15.665 13.883 20.998 1.00 12.05 ? 79  ARG A CG  1 
ATOM   608  C  CD  . ARG A 1 79  ? 14.484 13.521 21.903 1.00 12.57 ? 79  ARG A CD  1 
ATOM   609  N  NE  . ARG A 1 79  ? 14.757 13.986 23.268 1.00 11.60 ? 79  ARG A NE  1 
ATOM   610  C  CZ  . ARG A 1 79  ? 13.995 13.605 24.281 1.00 11.29 ? 79  ARG A CZ  1 
ATOM   611  N  NH1 . ARG A 1 79  ? 12.899 12.866 24.077 1.00 12.29 ? 79  ARG A NH1 1 
ATOM   612  N  NH2 . ARG A 1 79  ? 14.347 13.932 25.531 1.00 11.14 ? 79  ARG A NH2 1 
ATOM   613  N  N   . HIS A 1 80  ? 18.089 16.755 21.541 1.00 10.26 ? 80  HIS A N   1 
ATOM   614  C  CA  . HIS A 1 80  ? 18.823 16.881 22.789 1.00 9.48  ? 80  HIS A CA  1 
ATOM   615  C  C   . HIS A 1 80  ? 18.277 15.925 23.825 1.00 9.58  ? 80  HIS A C   1 
ATOM   616  O  O   . HIS A 1 80  ? 17.075 15.722 23.944 1.00 9.88  ? 80  HIS A O   1 
ATOM   617  C  CB  . HIS A 1 80  ? 18.686 18.326 23.287 1.00 9.28  ? 80  HIS A CB  1 
ATOM   618  C  CG  . HIS A 1 80  ? 19.350 19.258 22.302 1.00 9.14  ? 80  HIS A CG  1 
ATOM   619  N  ND1 . HIS A 1 80  ? 18.950 20.537 22.097 1.00 9.62  ? 80  HIS A ND1 1 
ATOM   620  C  CD2 . HIS A 1 80  ? 20.433 18.995 21.467 1.00 10.05 ? 80  HIS A CD2 1 
ATOM   621  C  CE1 . HIS A 1 80  ? 19.783 21.032 21.156 1.00 9.26  ? 80  HIS A CE1 1 
ATOM   622  N  NE2 . HIS A 1 80  ? 20.683 20.128 20.761 1.00 10.43 ? 80  HIS A NE2 1 
ATOM   623  N  N   . VAL A 1 81  ? 19.132 15.449 24.755 1.00 9.09  ? 81  VAL A N   1 
ATOM   624  C  CA  . VAL A 1 81  ? 18.562 14.737 25.896 1.00 9.99  ? 81  VAL A CA  1 
ATOM   625  C  C   . VAL A 1 81  ? 17.536 15.592 26.605 1.00 9.52  ? 81  VAL A C   1 
ATOM   626  O  O   . VAL A 1 81  ? 16.487 15.107 27.012 1.00 10.34 ? 81  VAL A O   1 
ATOM   627  C  CB  . VAL A 1 81  ? 19.619 14.232 26.862 1.00 10.41 ? 81  VAL A CB  1 
ATOM   628  C  CG1 . VAL A 1 81  ? 19.078 13.760 28.180 1.00 11.12 ? 81  VAL A CG1 1 
ATOM   629  C  CG2 . VAL A 1 81  ? 20.427 13.149 26.207 1.00 11.65 ? 81  VAL A CG2 1 
ATOM   630  N  N   . GLY A 1 82  ? 17.810 16.885 26.776 1.00 9.28  ? 82  GLY A N   1 
ATOM   631  C  CA  . GLY A 1 82  ? 16.899 17.743 27.510 1.00 9.31  ? 82  GLY A CA  1 
ATOM   632  C  C   . GLY A 1 82  ? 15.653 18.182 26.799 1.00 9.64  ? 82  GLY A C   1 
ATOM   633  O  O   . GLY A 1 82  ? 14.934 18.993 27.392 1.00 10.55 ? 82  GLY A O   1 
ATOM   634  N  N   . ASP A 1 83  ? 15.359 17.727 25.595 1.00 9.20  ? 83  ASP A N   1 
ATOM   635  C  CA  . ASP A 1 83  ? 14.246 18.246 24.791 1.00 9.38  ? 83  ASP A CA  1 
ATOM   636  C  C   . ASP A 1 83  ? 12.918 17.637 25.141 1.00 10.13 ? 83  ASP A C   1 
ATOM   637  O  O   . ASP A 1 83  ? 12.488 16.633 24.556 1.00 12.25 ? 83  ASP A O   1 
ATOM   638  C  CB  . ASP A 1 83  ? 14.562 18.012 23.307 1.00 9.82  ? 83  ASP A CB  1 
ATOM   639  C  CG  . ASP A 1 83  ? 15.638 18.953 22.777 1.00 9.36  ? 83  ASP A CG  1 
ATOM   640  O  OD1 . ASP A 1 83  ? 15.994 19.910 23.549 1.00 9.62  ? 83  ASP A OD1 1 
ATOM   641  O  OD2 . ASP A 1 83  ? 16.122 18.715 21.653 1.00 10.09 ? 83  ASP A OD2 1 
ATOM   642  N  N   . LEU A 1 84  ? 12.231 18.274 26.075 1.00 9.50  ? 84  LEU A N   1 
ATOM   643  C  CA  . LEU A 1 84  ? 10.916 17.812 26.567 1.00 10.04 ? 84  LEU A CA  1 
ATOM   644  C  C   . LEU A 1 84  ? 9.764  18.570 25.952 1.00 12.13 ? 84  LEU A C   1 
ATOM   645  O  O   . LEU A 1 84  ? 8.623  18.432 26.412 1.00 15.69 ? 84  LEU A O   1 
ATOM   646  C  CB  . LEU A 1 84  ? 10.857 17.822 28.083 1.00 10.19 ? 84  LEU A CB  1 
ATOM   647  C  CG  . LEU A 1 84  ? 11.937 16.920 28.768 1.00 10.53 ? 84  LEU A CG  1 
ATOM   648  C  CD1 . LEU A 1 84  ? 11.816 17.035 30.300 1.00 12.57 ? 84  LEU A CD1 1 
ATOM   649  C  CD2 . LEU A 1 84  ? 11.874 15.453 28.348 1.00 14.44 ? 84  LEU A CD2 1 
ATOM   650  N  N   . GLY A 1 85  ? 9.963  19.319 24.897 1.00 10.93 ? 85  GLY A N   1 
ATOM   651  C  CA  . GLY A 1 85  ? 8.892  19.905 24.124 1.00 11.71 ? 85  GLY A CA  1 
ATOM   652  C  C   . GLY A 1 85  ? 8.274  21.148 24.754 1.00 11.29 ? 85  GLY A C   1 
ATOM   653  O  O   . GLY A 1 85  ? 8.976  22.069 25.165 1.00 12.23 ? 85  GLY A O   1 
ATOM   654  N  N   . ASN A 1 86  ? 6.949  21.171 24.676 1.00 11.98 ? 86  ASN A N   1 
ATOM   655  C  CA  . ASN A 1 86  ? 6.162  22.252 25.153 1.00 12.66 ? 86  ASN A CA  1 
ATOM   656  C  C   . ASN A 1 86  ? 5.168  21.822 26.226 1.00 13.14 ? 86  ASN A C   1 
ATOM   657  O  O   . ASN A 1 86  ? 4.671  20.702 26.225 1.00 14.87 ? 86  ASN A O   1 
ATOM   658  C  CB  . ASN A 1 86  ? 5.278  22.873 24.042 1.00 13.36 ? 86  ASN A CB  1 
ATOM   659  C  CG  . ASN A 1 86  ? 6.111  23.643 23.044 1.00 13.11 ? 86  ASN A CG  1 
ATOM   660  O  OD1 . ASN A 1 86  ? 6.733  24.648 23.394 1.00 13.90 ? 86  ASN A OD1 1 
ATOM   661  N  ND2 . ASN A 1 86  ? 6.159  23.173 21.810 1.00 15.82 ? 86  ASN A ND2 1 
ATOM   662  N  N   . VAL A 1 87  ? 4.898  22.743 27.124 1.00 13.05 ? 87  VAL A N   1 
ATOM   663  C  CA  . VAL A 1 87  ? 3.729  22.656 27.985 1.00 13.76 ? 87  VAL A CA  1 
ATOM   664  C  C   . VAL A 1 87  ? 2.738  23.702 27.544 1.00 14.09 ? 87  VAL A C   1 
ATOM   665  O  O   . VAL A 1 87  ? 3.081  24.699 26.948 1.00 18.11 ? 87  VAL A O   1 
ATOM   666  C  CB  . VAL A 1 87  ? 4.138  22.789 29.465 1.00 15.40 ? 87  VAL A CB  1 
ATOM   667  C  CG1 . VAL A 1 87  ? 5.104  21.700 29.859 1.00 18.74 ? 87  VAL A CG1 1 
ATOM   668  C  CG2 . VAL A 1 87  ? 4.663  24.152 29.800 1.00 17.80 ? 87  VAL A CG2 1 
ATOM   669  N  N   . THR A 1 88  ? 1.466  23.459 27.856 1.00 14.93 ? 88  THR A N   1 
ATOM   670  C  CA  . THR A 1 88  ? 0.379  24.350 27.423 1.00 15.48 ? 88  THR A CA  1 
ATOM   671  C  C   . THR A 1 88  ? -0.328 24.994 28.600 1.00 15.49 ? 88  THR A C   1 
ATOM   672  O  O   . THR A 1 88  ? -0.840 24.294 29.466 1.00 16.23 ? 88  THR A O   1 
ATOM   673  C  CB  . THR A 1 88  ? -0.611 23.611 26.527 1.00 18.17 ? 88  THR A CB  1 
ATOM   674  O  OG1 . THR A 1 88  ? 0.094  23.146 25.376 1.00 23.49 ? 88  THR A OG1 1 
ATOM   675  C  CG2 . THR A 1 88  ? -1.689 24.543 25.950 1.00 29.87 ? 88  THR A CG2 1 
ATOM   676  N  N   . ALA A 1 89  ? -0.264 26.335 28.685 1.00 15.25 ? 89  ALA A N   1 
ATOM   677  C  CA  . ALA A 1 89  ? -0.959 27.061 29.728 1.00 14.42 ? 89  ALA A CA  1 
ATOM   678  C  C   . ALA A 1 89  ? -2.340 27.499 29.277 1.00 16.29 ? 89  ALA A C   1 
ATOM   679  O  O   . ALA A 1 89  ? -2.545 27.938 28.155 1.00 16.89 ? 89  ALA A O   1 
ATOM   680  C  CB  . ALA A 1 89  ? -0.158 28.269 30.175 1.00 17.19 ? 89  ALA A CB  1 
ATOM   681  N  N   . ASP A 1 90  ? -3.273 27.419 30.222 1.00 16.19 ? 90  ASP A N   1 
ATOM   682  C  CA  . ASP A 1 90  ? -4.659 27.851 29.962 1.00 17.69 ? 90  ASP A CA  1 
ATOM   683  C  C   . ASP A 1 90  ? -4.790 29.350 30.198 1.00 17.31 ? 90  ASP A C   1 
ATOM   684  O  O   . ASP A 1 90  ? -3.805 30.064 30.501 1.00 17.28 ? 90  ASP A O   1 
ATOM   685  C  CB  . ASP A 1 90  ? -5.617 27.038 30.800 1.00 15.76 ? 90  ASP A CB  1 
ATOM   686  C  CG  . ASP A 1 90  ? -5.509 27.182 32.290 1.00 14.80 ? 90  ASP A CG  1 
ATOM   687  O  OD1 . ASP A 1 90  ? -4.858 28.122 32.804 1.00 17.09 ? 90  ASP A OD1 1 
ATOM   688  O  OD2 . ASP A 1 90  ? -6.123 26.310 32.974 1.00 16.79 ? 90  ASP A OD2 1 
ATOM   689  N  N   . LYS A 1 91  ? -6.022 29.858 30.164 1.00 19.00 ? 91  LYS A N   1 
ATOM   690  C  CA  . LYS A 1 91  ? -6.263 31.296 30.228 1.00 23.87 ? 91  LYS A CA  1 
ATOM   691  C  C   . LYS A 1 91  ? -5.880 31.853 31.587 1.00 20.78 ? 91  LYS A C   1 
ATOM   692  O  O   . LYS A 1 91  ? -5.439 33.011 31.720 1.00 27.52 ? 91  LYS A O   1 
ATOM   693  C  CB  . LYS A 1 91  ? -7.677 31.671 29.797 1.00 28.69 ? 91  LYS A CB  1 
ATOM   694  C  CG  . LYS A 1 91  ? -7.985 33.109 30.259 1.00 37.93 ? 91  LYS A CG  1 
ATOM   695  N  N   . ASP A 1 92  ? -6.023 31.070 32.655 1.00 17.47 ? 92  ASP A N   1 
ATOM   696  C  CA  . ASP A 1 92  ? -5.646 31.544 33.965 1.00 17.25 ? 92  ASP A CA  1 
ATOM   697  C  C   . ASP A 1 92  ? -4.177 31.267 34.289 1.00 16.12 ? 92  ASP A C   1 
ATOM   698  O  O   . ASP A 1 92  ? -3.760 31.547 35.404 1.00 18.03 ? 92  ASP A O   1 
ATOM   699  C  CB  . ASP A 1 92  ? -6.553 30.954 35.057 1.00 17.95 ? 92  ASP A CB  1 
ATOM   700  C  CG  . ASP A 1 92  ? -6.725 29.466 34.996 1.00 15.06 ? 92  ASP A CG  1 
ATOM   701  O  OD1 . ASP A 1 92  ? -7.439 28.951 34.077 1.00 18.91 ? 92  ASP A OD1 1 
ATOM   702  O  OD2 . ASP A 1 92  ? -6.269 28.731 35.884 1.00 17.32 ? 92  ASP A OD2 1 
ATOM   703  N  N   . GLY A 1 93  ? -3.384 30.812 33.312 1.00 15.87 ? 93  GLY A N   1 
ATOM   704  C  CA  . GLY A 1 93  ? -1.976 30.747 33.397 1.00 15.90 ? 93  GLY A CA  1 
ATOM   705  C  C   . GLY A 1 93  ? -1.394 29.433 33.905 1.00 14.72 ? 93  GLY A C   1 
ATOM   706  O  O   . GLY A 1 93  ? -0.216 29.419 34.257 1.00 14.14 ? 93  GLY A O   1 
ATOM   707  N  N   . VAL A 1 94  ? -2.201 28.398 33.990 1.00 13.57 ? 94  VAL A N   1 
ATOM   708  C  CA  . VAL A 1 94  ? -1.737 27.119 34.558 1.00 12.01 ? 94  VAL A CA  1 
ATOM   709  C  C   . VAL A 1 94  ? -1.474 26.136 33.425 1.00 11.98 ? 94  VAL A C   1 
ATOM   710  O  O   . VAL A 1 94  ? -2.320 25.938 32.573 1.00 12.60 ? 94  VAL A O   1 
ATOM   711  C  CB  . VAL A 1 94  ? -2.756 26.507 35.521 1.00 12.80 ? 94  VAL A CB  1 
ATOM   712  C  CG1 . VAL A 1 94  ? -2.267 25.168 36.060 1.00 12.33 ? 94  VAL A CG1 1 
ATOM   713  C  CG2 . VAL A 1 94  ? -3.041 27.504 36.637 1.00 14.38 ? 94  VAL A CG2 1 
ATOM   714  N  N   . ALA A 1 95  ? -0.266 25.572 33.470 1.00 11.98 ? 95  ALA A N   1 
ATOM   715  C  CA  . ALA A 1 95  ? 0.081  24.502 32.578 1.00 11.42 ? 95  ALA A CA  1 
ATOM   716  C  C   . ALA A 1 95  ? 0.298  23.204 33.380 1.00 11.10 ? 95  ALA A C   1 
ATOM   717  O  O   . ALA A 1 95  ? 1.085  23.199 34.303 1.00 14.40 ? 95  ALA A O   1 
ATOM   718  C  CB  . ALA A 1 95  ? 1.387  24.773 31.812 1.00 12.98 ? 95  ALA A CB  1 
ATOM   719  N  N   . ASP A 1 96  ? -0.374 22.156 33.007 1.00 11.30 ? 96  ASP A N   1 
ATOM   720  C  CA  . ASP A 1 96  ? -0.167 20.827 33.618 1.00 12.17 ? 96  ASP A CA  1 
ATOM   721  C  C   . ASP A 1 96  ? 0.868  20.066 32.829 1.00 12.50 ? 96  ASP A C   1 
ATOM   722  O  O   . ASP A 1 96  ? 0.764  19.826 31.641 1.00 20.65 ? 96  ASP A O   1 
ATOM   723  C  CB  . ASP A 1 96  ? -1.456 20.040 33.560 1.00 12.35 ? 96  ASP A CB  1 
ATOM   724  C  CG  . ASP A 1 96  ? -2.555 20.544 34.473 1.00 12.56 ? 96  ASP A CG  1 
ATOM   725  O  OD1 . ASP A 1 96  ? -2.278 21.248 35.461 1.00 13.40 ? 96  ASP A OD1 1 
ATOM   726  O  OD2 . ASP A 1 96  ? -3.715 20.205 34.278 1.00 14.30 ? 96  ASP A OD2 1 
ATOM   727  N  N   . VAL A 1 97  ? 1.860  19.561 33.515 1.00 12.08 ? 97  VAL A N   1 
ATOM   728  C  CA  . VAL A 1 97  ? 2.908  18.748 32.913 1.00 11.77 ? 97  VAL A CA  1 
ATOM   729  C  C   . VAL A 1 97  ? 2.516  17.309 33.080 1.00 10.46 ? 97  VAL A C   1 
ATOM   730  O  O   . VAL A 1 97  ? 2.215  16.848 34.195 1.00 10.75 ? 97  VAL A O   1 
ATOM   731  C  CB  . VAL A 1 97  ? 4.276  19.016 33.559 1.00 12.11 ? 97  VAL A CB  1 
ATOM   732  C  CG1 . VAL A 1 97  ? 5.338  18.154 32.928 1.00 14.28 ? 97  VAL A CG1 1 
ATOM   733  C  CG2 . VAL A 1 97  ? 4.644  20.512 33.417 1.00 16.54 ? 97  VAL A CG2 1 
ATOM   734  N  N   . SER A 1 98  ? 2.590  16.514 32.003 1.00 11.45 ? 98  SER A N   1 
ATOM   735  C  CA  . SER A 1 98  ? 2.448  15.088 32.061 1.00 11.35 ? 98  SER A CA  1 
ATOM   736  C  C   . SER A 1 98  ? 3.209  14.463 30.895 1.00 11.92 ? 98  SER A C   1 
ATOM   737  O  O   . SER A 1 98  ? 2.777  14.562 29.744 1.00 14.01 ? 98  SER A O   1 
ATOM   738  C  CB  . SER A 1 98  ? 0.984  14.666 32.053 1.00 17.31 ? 98  SER A CB  1 
ATOM   739  O  OG  . SER A 1 98  ? 0.981  13.242 32.120 1.00 21.03 ? 98  SER A OG  1 
ATOM   740  N  N   . ILE A 1 99  ? 4.412  13.958 31.184 1.00 10.99 ? 99  ILE A N   1 
ATOM   741  C  CA  . ILE A 1 99  ? 5.370  13.504 30.160 1.00 11.43 ? 99  ILE A CA  1 
ATOM   742  C  C   . ILE A 1 99  ? 5.887  12.151 30.572 1.00 11.39 ? 99  ILE A C   1 
ATOM   743  O  O   . ILE A 1 99  ? 6.156  11.855 31.759 1.00 12.78 ? 99  ILE A O   1 
ATOM   744  C  CB  . ILE A 1 99  ? 6.541  14.506 30.046 1.00 13.05 ? 99  ILE A CB  1 
ATOM   745  C  CG1 . ILE A 1 99  ? 6.027  15.855 29.480 1.00 13.75 ? 99  ILE A CG1 1 
ATOM   746  C  CG2 . ILE A 1 99  ? 7.677  13.951 29.220 1.00 14.80 ? 99  ILE A CG2 1 
ATOM   747  C  CD1 . ILE A 1 99  ? 6.997  16.979 29.627 1.00 19.32 ? 99  ILE A CD1 1 
ATOM   748  N  N   . GLU A 1 100 ? 6.041  11.257 29.602 1.00 10.40 ? 100 GLU A N   1 
ATOM   749  C  CA  . GLU A 1 100 ? 6.809  10.024 29.719 1.00 10.92 ? 100 GLU A CA  1 
ATOM   750  C  C   . GLU A 1 100 ? 7.902  10.072 28.691 1.00 9.33  ? 100 GLU A C   1 
ATOM   751  O  O   . GLU A 1 100 ? 7.625  10.392 27.527 1.00 12.52 ? 100 GLU A O   1 
ATOM   752  C  CB  . GLU A 1 100 ? 5.967  8.767  29.486 1.00 12.40 ? 100 GLU A CB  1 
ATOM   753  C  CG  . GLU A 1 100 ? 6.743  7.483  29.694 1.00 14.71 ? 100 GLU A CG  1 
ATOM   754  C  CD  . GLU A 1 100 ? 5.951  6.222  29.469 1.00 22.80 ? 100 GLU A CD  1 
ATOM   755  O  OE1 . GLU A 1 100 ? 4.707  6.216  29.567 1.00 29.37 ? 100 GLU A OE1 1 
ATOM   756  O  OE2 . GLU A 1 100 ? 6.517  5.152  29.273 1.00 25.46 ? 100 GLU A OE2 1 
ATOM   757  N  N   . ASP A 1 101 ? 9.156  9.961  29.096 1.00 9.71  ? 101 ASP A N   1 
ATOM   758  C  CA  . ASP A 1 101 ? 10.261 10.155 28.212 1.00 9.72  ? 101 ASP A CA  1 
ATOM   759  C  C   . ASP A 1 101 ? 11.230 8.983  28.332 1.00 9.21  ? 101 ASP A C   1 
ATOM   760  O  O   . ASP A 1 101 ? 11.554 8.494  29.411 1.00 10.36 ? 101 ASP A O   1 
ATOM   761  C  CB  . ASP A 1 101 ? 10.975 11.487 28.472 1.00 10.19 ? 101 ASP A CB  1 
ATOM   762  C  CG  . ASP A 1 101 ? 11.874 11.889 27.314 1.00 10.74 ? 101 ASP A CG  1 
ATOM   763  O  OD1 . ASP A 1 101 ? 11.283 12.323 26.272 1.00 12.57 ? 101 ASP A OD1 1 
ATOM   764  O  OD2 . ASP A 1 101 ? 13.110 11.759 27.413 1.00 10.34 ? 101 ASP A OD2 1 
ATOM   765  N  N   . SER A 1 102 ? 11.792 8.536  27.201 1.00 10.12 ? 102 SER A N   1 
ATOM   766  C  CA  . SER A 1 102 ? 12.730 7.466  27.082 1.00 10.47 ? 102 SER A CA  1 
ATOM   767  C  C   . SER A 1 102 ? 14.190 7.895  27.015 1.00 9.23  ? 102 SER A C   1 
ATOM   768  O  O   . SER A 1 102 ? 15.059 7.041  27.075 1.00 11.42 ? 102 SER A O   1 
ATOM   769  C  CB  A SER A 1 102 ? 12.455 6.667  25.820 0.74 15.53 ? 102 SER A CB  1 
ATOM   770  C  CB  B SER A 1 102 ? 12.399 6.645  25.832 0.26 11.88 ? 102 SER A CB  1 
ATOM   771  O  OG  A SER A 1 102 ? 11.203 6.024  25.901 0.74 17.18 ? 102 SER A OG  1 
ATOM   772  O  OG  B SER A 1 102 ? 12.413 7.407  24.626 0.26 11.90 ? 102 SER A OG  1 
ATOM   773  N  N   . VAL A 1 103 ? 14.429 9.174  26.814 1.00 8.66  ? 103 VAL A N   1 
ATOM   774  C  CA  . VAL A 1 103 ? 15.799 9.648  26.554 1.00 8.91  ? 103 VAL A CA  1 
ATOM   775  C  C   . VAL A 1 103 ? 16.460 10.170 27.832 1.00 8.47  ? 103 VAL A C   1 
ATOM   776  O  O   . VAL A 1 103 ? 17.615 9.862  28.070 1.00 9.68  ? 103 VAL A O   1 
ATOM   777  C  CB  . VAL A 1 103 ? 15.795 10.655 25.394 1.00 9.50  ? 103 VAL A CB  1 
ATOM   778  C  CG1 . VAL A 1 103 ? 17.167 11.215 25.127 1.00 12.94 ? 103 VAL A CG1 1 
ATOM   779  C  CG2 . VAL A 1 103 ? 15.259 10.028 24.135 1.00 12.85 ? 103 VAL A CG2 1 
ATOM   780  N  N   . ILE A 1 104 ? 15.724 10.981 28.610 1.00 8.57  ? 104 ILE A N   1 
ATOM   781  C  CA  . ILE A 1 104 ? 16.261 11.382 29.904 1.00 8.08  ? 104 ILE A CA  1 
ATOM   782  C  C   . ILE A 1 104 ? 16.369 10.161 30.825 1.00 7.95  ? 104 ILE A C   1 
ATOM   783  O  O   . ILE A 1 104 ? 15.610 9.193  30.683 1.00 8.42  ? 104 ILE A O   1 
ATOM   784  C  CB  . ILE A 1 104 ? 15.420 12.480 30.545 1.00 7.87  ? 104 ILE A CB  1 
ATOM   785  C  CG1 . ILE A 1 104 ? 13.963 12.095 30.779 1.00 9.15  ? 104 ILE A CG1 1 
ATOM   786  C  CG2 . ILE A 1 104 ? 15.507 13.781 29.776 1.00 9.46  ? 104 ILE A CG2 1 
ATOM   787  C  CD1 . ILE A 1 104 ? 13.180 13.037 31.659 1.00 9.70  ? 104 ILE A CD1 1 
ATOM   788  N  N   . SER A 1 105 ? 17.254 10.290 31.809 1.00 8.02  ? 105 SER A N   1 
ATOM   789  C  CA  . SER A 1 105 ? 17.414 9.299  32.862 1.00 7.88  ? 105 SER A CA  1 
ATOM   790  C  C   . SER A 1 105 ? 17.836 9.980  34.133 1.00 7.40  ? 105 SER A C   1 
ATOM   791  O  O   . SER A 1 105 ? 18.504 11.026 34.086 1.00 8.66  ? 105 SER A O   1 
ATOM   792  C  CB  . SER A 1 105 ? 18.440 8.250  32.462 1.00 8.78  ? 105 SER A CB  1 
ATOM   793  O  OG  . SER A 1 105 ? 18.580 7.272  33.466 1.00 8.99  ? 105 SER A OG  1 
ATOM   794  N  N   . LEU A 1 106 ? 17.485 9.400  35.267 1.00 7.95  ? 106 LEU A N   1 
ATOM   795  C  CA  . LEU A 1 106 ? 17.953 9.873  36.560 1.00 7.82  ? 106 LEU A CA  1 
ATOM   796  C  C   . LEU A 1 106 ? 19.248 9.186  36.981 1.00 8.22  ? 106 LEU A C   1 
ATOM   797  O  O   . LEU A 1 106 ? 19.874 9.644  37.948 1.00 8.79  ? 106 LEU A O   1 
ATOM   798  C  CB  . LEU A 1 106 ? 16.878 9.736  37.649 1.00 8.12  ? 106 LEU A CB  1 
ATOM   799  C  CG  . LEU A 1 106 ? 15.502 10.295 37.254 1.00 8.19  ? 106 LEU A CG  1 
ATOM   800  C  CD1 . LEU A 1 106 ? 14.524 10.168 38.446 1.00 9.68  ? 106 LEU A CD1 1 
ATOM   801  C  CD2 . LEU A 1 106 ? 15.584 11.742 36.789 1.00 9.20  ? 106 LEU A CD2 1 
ATOM   802  N  N   . SER A 1 107 ? 19.666 8.139  36.292 1.00 8.30  ? 107 SER A N   1 
ATOM   803  C  CA  . SER A 1 107 ? 20.832 7.342  36.643 1.00 9.33  ? 107 SER A CA  1 
ATOM   804  C  C   . SER A 1 107 ? 21.880 7.382  35.551 1.00 8.67  ? 107 SER A C   1 
ATOM   805  O  O   . SER A 1 107 ? 21.562 7.552  34.388 1.00 12.19 ? 107 SER A O   1 
ATOM   806  C  CB  A SER A 1 107 ? 20.447 5.913  37.057 0.59 10.22 ? 107 SER A CB  1 
ATOM   807  C  CB  B SER A 1 107 ? 20.291 5.870  36.621 0.41 13.20 ? 107 SER A CB  1 
ATOM   808  O  OG  A SER A 1 107 ? 19.804 5.904  38.351 0.59 12.45 ? 107 SER A OG  1 
ATOM   809  O  OG  B SER A 1 107 ? 21.231 4.854  36.876 0.41 14.13 ? 107 SER A OG  1 
ATOM   810  N  N   . GLY A 1 108 ? 23.105 7.091  35.937 1.00 9.10  ? 108 GLY A N   1 
ATOM   811  C  CA  . GLY A 1 108 ? 24.187 6.826  35.036 1.00 9.62  ? 108 GLY A CA  1 
ATOM   812  C  C   . GLY A 1 108 ? 24.933 8.060  34.615 1.00 8.86  ? 108 GLY A C   1 
ATOM   813  O  O   . GLY A 1 108 ? 24.824 9.157  35.204 1.00 9.68  ? 108 GLY A O   1 
ATOM   814  N  N   . ASP A 1 109 ? 25.741 7.923  33.567 1.00 10.04 ? 109 ASP A N   1 
ATOM   815  C  CA  . ASP A 1 109 ? 26.669 8.920  33.162 1.00 10.45 ? 109 ASP A CA  1 
ATOM   816  C  C   . ASP A 1 109 ? 26.039 10.234 32.724 1.00 9.90  ? 109 ASP A C   1 
ATOM   817  O  O   . ASP A 1 109 ? 26.688 11.271 32.768 1.00 12.00 ? 109 ASP A O   1 
ATOM   818  C  CB  . ASP A 1 109 ? 27.514 8.380  31.970 1.00 13.87 ? 109 ASP A CB  1 
ATOM   819  C  CG  . ASP A 1 109 ? 28.336 7.164  32.403 1.00 16.18 ? 109 ASP A CG  1 
ATOM   820  O  OD1 . ASP A 1 109 ? 29.368 7.400  33.017 1.00 20.03 ? 109 ASP A OD1 1 
ATOM   821  O  OD2 . ASP A 1 109 ? 27.943 6.065  32.019 1.00 36.01 ? 109 ASP A OD2 1 
ATOM   822  N  N   . HIS A 1 110 ? 24.808 10.175 32.254 1.00 8.96  ? 110 HIS A N   1 
ATOM   823  C  CA  . HIS A 1 110 ? 24.133 11.339 31.720 1.00 9.33  ? 110 HIS A CA  1 
ATOM   824  C  C   . HIS A 1 110 ? 22.916 11.720 32.541 1.00 8.55  ? 110 HIS A C   1 
ATOM   825  O  O   . HIS A 1 110 ? 21.967 12.301 32.035 1.00 9.92  ? 110 HIS A O   1 
ATOM   826  C  CB  A HIS A 1 110 ? 23.751 11.106 30.233 0.59 11.49 ? 110 HIS A CB  1 
ATOM   827  C  CB  B HIS A 1 110 ? 23.721 11.129 30.243 0.42 12.76 ? 110 HIS A CB  1 
ATOM   828  C  CG  A HIS A 1 110 ? 24.895 10.884 29.326 0.59 11.96 ? 110 HIS A CG  1 
ATOM   829  C  CG  B HIS A 1 110 ? 24.860 10.674 29.410 0.42 13.56 ? 110 HIS A CG  1 
ATOM   830  N  ND1 A HIS A 1 110 ? 24.687 10.489 28.031 0.59 12.03 ? 110 HIS A ND1 1 
ATOM   831  N  ND1 B HIS A 1 110 ? 26.120 11.220 29.456 0.42 16.76 ? 110 HIS A ND1 1 
ATOM   832  C  CD2 A HIS A 1 110 ? 26.233 11.042 29.461 0.59 11.71 ? 110 HIS A CD2 1 
ATOM   833  C  CD2 B HIS A 1 110 ? 24.926 9.729  28.472 0.42 15.66 ? 110 HIS A CD2 1 
ATOM   834  C  CE1 A HIS A 1 110 ? 25.844 10.381 27.427 0.59 16.82 ? 110 HIS A CE1 1 
ATOM   835  C  CE1 B HIS A 1 110 ? 26.907 10.641 28.567 0.42 17.70 ? 110 HIS A CE1 1 
ATOM   836  N  NE2 A HIS A 1 110 ? 26.812 10.725 28.247 0.59 13.37 ? 110 HIS A NE2 1 
ATOM   837  N  NE2 B HIS A 1 110 ? 26.198 9.699  27.964 0.42 17.01 ? 110 HIS A NE2 1 
ATOM   838  N  N   . SER A 1 111 ? 22.903 11.392 33.821 1.00 9.50  ? 111 SER A N   1 
ATOM   839  C  CA  . SER A 1 111 ? 21.778 11.732 34.679 1.00 8.55  ? 111 SER A CA  1 
ATOM   840  C  C   . SER A 1 111 ? 21.427 13.203 34.587 1.00 8.06  ? 111 SER A C   1 
ATOM   841  O  O   . SER A 1 111 ? 22.295 14.059 34.623 1.00 9.19  ? 111 SER A O   1 
ATOM   842  C  CB  . SER A 1 111 ? 22.208 11.458 36.130 1.00 8.67  ? 111 SER A CB  1 
ATOM   843  O  OG  . SER A 1 111 ? 21.238 11.824 37.038 1.00 9.23  ? 111 SER A OG  1 
ATOM   844  N  N   . ILE A 1 112 ? 20.112 13.476 34.571 1.00 7.75  ? 112 ILE A N   1 
ATOM   845  C  CA  . ILE A 1 112 ? 19.634 14.841 34.664 1.00 7.55  ? 112 ILE A CA  1 
ATOM   846  C  C   . ILE A 1 112 ? 19.556 15.383 36.069 1.00 7.80  ? 112 ILE A C   1 
ATOM   847  O  O   . ILE A 1 112 ? 19.328 16.594 36.252 1.00 7.95  ? 112 ILE A O   1 
ATOM   848  C  CB  . ILE A 1 112 ? 18.262 15.046 33.992 1.00 8.01  ? 112 ILE A CB  1 
ATOM   849  C  CG1 . ILE A 1 112 ? 17.159 14.238 34.680 1.00 8.70  ? 112 ILE A CG1 1 
ATOM   850  C  CG2 . ILE A 1 112 ? 18.338 14.741 32.479 1.00 9.48  ? 112 ILE A CG2 1 
ATOM   851  C  CD1 . ILE A 1 112 ? 15.784 14.593 34.220 1.00 9.69  ? 112 ILE A CD1 1 
ATOM   852  N  N   . ILE A 1 113 ? 19.720 14.586 37.081 1.00 8.55  ? 113 ILE A N   1 
ATOM   853  C  CA  . ILE A 1 113 ? 19.800 15.064 38.450 1.00 8.01  ? 113 ILE A CA  1 
ATOM   854  C  C   . ILE A 1 113 ? 20.977 16.072 38.572 1.00 8.46  ? 113 ILE A C   1 
ATOM   855  O  O   . ILE A 1 113 ? 22.100 15.786 38.157 1.00 10.66 ? 113 ILE A O   1 
ATOM   856  C  CB  . ILE A 1 113 ? 20.019 13.933 39.434 1.00 9.85  ? 113 ILE A CB  1 
ATOM   857  C  CG1 . ILE A 1 113 ? 18.987 12.900 39.380 1.00 12.07 ? 113 ILE A CG1 1 
ATOM   858  C  CG2 . ILE A 1 113 ? 20.207 14.479 40.850 1.00 10.53 ? 113 ILE A CG2 1 
ATOM   859  C  CD1 . ILE A 1 113 ? 17.683 13.364 39.771 1.00 13.07 ? 113 ILE A CD1 1 
ATOM   860  N  N   . GLY A 1 114 ? 20.667 17.225 39.136 1.00 8.52  ? 114 GLY A N   1 
ATOM   861  C  CA  . GLY A 1 114 ? 21.612 18.313 39.286 1.00 9.48  ? 114 GLY A CA  1 
ATOM   862  C  C   . GLY A 1 114 ? 21.576 19.319 38.145 1.00 8.85  ? 114 GLY A C   1 
ATOM   863  O  O   . GLY A 1 114 ? 22.159 20.380 38.306 1.00 10.34 ? 114 GLY A O   1 
ATOM   864  N  N   . ARG A 1 115 ? 20.933 18.982 37.048 1.00 8.52  ? 115 ARG A N   1 
ATOM   865  C  CA  . ARG A 1 115 ? 20.793 19.883 35.914 1.00 8.34  ? 115 ARG A CA  1 
ATOM   866  C  C   . ARG A 1 115 ? 19.624 20.813 36.181 1.00 7.98  ? 115 ARG A C   1 
ATOM   867  O  O   . ARG A 1 115 ? 18.957 20.746 37.222 1.00 9.27  ? 115 ARG A O   1 
ATOM   868  C  CB  . ARG A 1 115 ? 20.615 19.082 34.604 1.00 8.85  ? 115 ARG A CB  1 
ATOM   869  C  CG  . ARG A 1 115 ? 21.772 18.130 34.288 1.00 10.57 ? 115 ARG A CG  1 
ATOM   870  C  CD  . ARG A 1 115 ? 23.061 18.826 33.987 1.00 12.47 ? 115 ARG A CD  1 
ATOM   871  N  NE  . ARG A 1 115 ? 24.135 17.849 33.820 1.00 12.72 ? 115 ARG A NE  1 
ATOM   872  C  CZ  . ARG A 1 115 ? 25.231 17.991 33.180 1.00 12.29 ? 115 ARG A CZ  1 
ATOM   873  N  NH1 . ARG A 1 115 ? 25.499 19.128 32.592 1.00 13.88 ? 115 ARG A NH1 1 
ATOM   874  N  NH2 . ARG A 1 115 ? 26.112 16.988 33.149 1.00 15.18 ? 115 ARG A NH2 1 
ATOM   875  N  N   . THR A 1 116 ? 19.365 21.725 35.237 1.00 8.82  ? 116 THR A N   1 
ATOM   876  C  CA  . THR A 1 116 ? 18.436 22.808 35.447 1.00 8.79  ? 116 THR A CA  1 
ATOM   877  C  C   . THR A 1 116 ? 17.206 22.644 34.553 1.00 8.27  ? 116 THR A C   1 
ATOM   878  O  O   . THR A 1 116 ? 17.358 22.650 33.337 1.00 10.59 ? 116 THR A O   1 
ATOM   879  C  CB  . THR A 1 116 ? 19.121 24.159 35.161 1.00 10.46 ? 116 THR A CB  1 
ATOM   880  O  OG1 . THR A 1 116 ? 20.271 24.266 36.027 1.00 12.03 ? 116 THR A OG1 1 
ATOM   881  C  CG2 . THR A 1 116 ? 18.207 25.349 35.362 1.00 11.85 ? 116 THR A CG2 1 
ATOM   882  N  N   . LEU A 1 117 ? 16.033 22.561 35.144 1.00 8.38  ? 117 LEU A N   1 
ATOM   883  C  CA  . LEU A 1 117 ? 14.777 22.552 34.417 1.00 8.05  ? 117 LEU A CA  1 
ATOM   884  C  C   . LEU A 1 117 ? 14.356 23.987 34.156 1.00 8.13  ? 117 LEU A C   1 
ATOM   885  O  O   . LEU A 1 117 ? 14.453 24.854 35.027 1.00 9.17  ? 117 LEU A O   1 
ATOM   886  C  CB  . LEU A 1 117 ? 13.722 21.782 35.232 1.00 8.60  ? 117 LEU A CB  1 
ATOM   887  C  CG  . LEU A 1 117 ? 12.399 21.543 34.509 1.00 8.64  ? 117 LEU A CG  1 
ATOM   888  C  CD1 . LEU A 1 117 ? 12.563 20.577 33.353 1.00 9.34  ? 117 LEU A CD1 1 
ATOM   889  C  CD2 . LEU A 1 117 ? 11.384 21.005 35.530 1.00 9.62  ? 117 LEU A CD2 1 
ATOM   890  N  N   . VAL A 1 118 ? 13.880 24.246 32.926 1.00 8.34  ? 118 VAL A N   1 
ATOM   891  C  CA  . VAL A 1 118 ? 13.537 25.610 32.462 1.00 8.87  ? 118 VAL A CA  1 
ATOM   892  C  C   . VAL A 1 118 ? 12.201 25.566 31.752 1.00 8.84  ? 118 VAL A C   1 
ATOM   893  O  O   . VAL A 1 118 ? 11.931 24.707 30.918 1.00 9.96  ? 118 VAL A O   1 
ATOM   894  C  CB  . VAL A 1 118 ? 14.615 26.142 31.486 1.00 9.86  ? 118 VAL A CB  1 
ATOM   895  C  CG1 . VAL A 1 118 ? 14.264 27.491 30.916 1.00 11.98 ? 118 VAL A CG1 1 
ATOM   896  C  CG2 . VAL A 1 118 ? 15.952 26.143 32.197 1.00 12.61 ? 118 VAL A CG2 1 
ATOM   897  N  N   . VAL A 1 119 ? 11.376 26.585 32.047 1.00 9.99  ? 119 VAL A N   1 
ATOM   898  C  CA  . VAL A 1 119 ? 10.211 26.901 31.241 1.00 9.57  ? 119 VAL A CA  1 
ATOM   899  C  C   . VAL A 1 119 ? 10.379 28.257 30.600 1.00 10.34 ? 119 VAL A C   1 
ATOM   900  O  O   . VAL A 1 119 ? 10.879 29.199 31.225 1.00 10.70 ? 119 VAL A O   1 
ATOM   901  C  CB  . VAL A 1 119 ? 8.906  26.773 32.029 1.00 10.59 ? 119 VAL A CB  1 
ATOM   902  C  CG1 . VAL A 1 119 ? 8.803  27.761 33.151 1.00 11.95 ? 119 VAL A CG1 1 
ATOM   903  C  CG2 . VAL A 1 119 ? 7.694  26.919 31.124 1.00 13.45 ? 119 VAL A CG2 1 
ATOM   904  N  N   . HIS A 1 120 ? 10.052 28.359 29.321 1.00 10.78 ? 120 HIS A N   1 
ATOM   905  C  CA  . HIS A 1 120 ? 10.325 29.498 28.458 1.00 10.45 ? 120 HIS A CA  1 
ATOM   906  C  C   . HIS A 1 120 ? 9.139  30.403 28.201 1.00 11.55 ? 120 HIS A C   1 
ATOM   907  O  O   . HIS A 1 120 ? 7.982  30.030 28.339 1.00 13.72 ? 120 HIS A O   1 
ATOM   908  C  CB  . HIS A 1 120 ? 10.845 28.969 27.108 1.00 10.68 ? 120 HIS A CB  1 
ATOM   909  C  CG  . HIS A 1 120 ? 12.271 28.438 27.193 1.00 10.74 ? 120 HIS A CG  1 
ATOM   910  N  ND1 . HIS A 1 120 ? 13.348 29.277 27.134 1.00 12.99 ? 120 HIS A ND1 1 
ATOM   911  C  CD2 . HIS A 1 120 ? 12.748 27.183 27.349 1.00 11.69 ? 120 HIS A CD2 1 
ATOM   912  C  CE1 . HIS A 1 120 ? 14.436 28.564 27.256 1.00 13.85 ? 120 HIS A CE1 1 
ATOM   913  N  NE2 . HIS A 1 120 ? 14.125 27.303 27.374 1.00 13.38 ? 120 HIS A NE2 1 
ATOM   914  N  N   . GLU A 1 121 ? 9.478  31.603 27.737 1.00 12.84 ? 121 GLU A N   1 
ATOM   915  C  CA  . GLU A 1 121 ? 8.511  32.591 27.348 1.00 15.17 ? 121 GLU A CA  1 
ATOM   916  C  C   . GLU A 1 121 ? 7.689  32.206 26.118 1.00 15.69 ? 121 GLU A C   1 
ATOM   917  O  O   . GLU A 1 121 ? 6.518  32.547 26.129 1.00 17.00 ? 121 GLU A O   1 
ATOM   918  C  CB  . GLU A 1 121 ? 9.216  33.950 27.129 1.00 17.02 ? 121 GLU A CB  1 
ATOM   919  C  CG  . GLU A 1 121 ? 8.327  35.113 26.835 1.00 24.45 ? 121 GLU A CG  1 
ATOM   920  C  CD  . GLU A 1 121 ? 9.088  36.429 26.726 1.00 29.12 ? 121 GLU A CD  1 
ATOM   921  O  OE1 . GLU A 1 121 ? 10.269 36.509 27.104 1.00 27.37 ? 121 GLU A OE1 1 
ATOM   922  O  OE2 . GLU A 1 121 ? 8.408  37.418 26.353 1.00 50.40 ? 121 GLU A OE2 1 
ATOM   923  N  N   . LYS A 1 122 ? 8.264  31.587 25.144 1.00 15.91 ? 122 LYS A N   1 
ATOM   924  C  CA  . LYS A 1 122 ? 7.638  31.255 23.882 1.00 16.36 ? 122 LYS A CA  1 
ATOM   925  C  C   . LYS A 1 122 ? 7.594  29.770 23.658 1.00 14.07 ? 122 LYS A C   1 
ATOM   926  O  O   . LYS A 1 122 ? 8.221  28.990 24.362 1.00 13.86 ? 122 LYS A O   1 
ATOM   927  C  CB  . LYS A 1 122 ? 8.356  31.882 22.657 1.00 20.13 ? 122 LYS A CB  1 
ATOM   928  C  CG  . LYS A 1 122 ? 8.808  33.293 22.938 1.00 33.34 ? 122 LYS A CG  1 
ATOM   929  N  N   . ALA A 1 123 ? 6.851  29.395 22.629 1.00 15.18 ? 123 ALA A N   1 
ATOM   930  C  CA  . ALA A 1 123 ? 6.828  28.023 22.222 1.00 14.67 ? 123 ALA A CA  1 
ATOM   931  C  C   . ALA A 1 123 ? 8.165  27.532 21.651 1.00 13.10 ? 123 ALA A C   1 
ATOM   932  O  O   . ALA A 1 123 ? 8.860  28.265 20.961 1.00 14.14 ? 123 ALA A O   1 
ATOM   933  C  CB  . ALA A 1 123 ? 5.771  27.806 21.122 1.00 16.92 ? 123 ALA A CB  1 
ATOM   934  N  N   . ASP A 1 124 ? 8.441  26.268 21.873 1.00 12.68 ? 124 ASP A N   1 
ATOM   935  C  CA  . ASP A 1 124 ? 9.472  25.536 21.157 1.00 11.99 ? 124 ASP A CA  1 
ATOM   936  C  C   . ASP A 1 124 ? 8.970  25.110 19.790 1.00 13.08 ? 124 ASP A C   1 
ATOM   937  O  O   . ASP A 1 124 ? 7.923  24.453 19.726 1.00 14.69 ? 124 ASP A O   1 
ATOM   938  C  CB  . ASP A 1 124 ? 9.872  24.348 22.074 1.00 11.54 ? 124 ASP A CB  1 
ATOM   939  C  CG  . ASP A 1 124 ? 10.992 23.474 21.582 1.00 11.25 ? 124 ASP A CG  1 
ATOM   940  O  OD1 . ASP A 1 124 ? 11.407 23.560 20.392 1.00 11.47 ? 124 ASP A OD1 1 
ATOM   941  O  OD2 . ASP A 1 124 ? 11.480 22.644 22.381 1.00 11.54 ? 124 ASP A OD2 1 
ATOM   942  N  N   . ASP A 1 125 ? 9.668  25.487 18.742 1.00 12.14 ? 125 ASP A N   1 
ATOM   943  C  CA  . ASP A 1 125 ? 9.304  25.103 17.375 1.00 13.04 ? 125 ASP A CA  1 
ATOM   944  C  C   . ASP A 1 125 ? 9.744  23.686 17.002 1.00 12.96 ? 125 ASP A C   1 
ATOM   945  O  O   . ASP A 1 125 ? 9.553  23.248 15.842 1.00 13.71 ? 125 ASP A O   1 
ATOM   946  C  CB  . ASP A 1 125 ? 9.802  26.181 16.405 1.00 12.96 ? 125 ASP A CB  1 
ATOM   947  C  CG  . ASP A 1 125 ? 11.281 26.180 16.134 1.00 11.77 ? 125 ASP A CG  1 
ATOM   948  O  OD1 . ASP A 1 125 ? 11.999 25.237 16.504 1.00 12.04 ? 125 ASP A OD1 1 
ATOM   949  O  OD2 . ASP A 1 125 ? 11.748 27.195 15.574 1.00 13.53 ? 125 ASP A OD2 1 
ATOM   950  N  N   . LEU A 1 126 ? 10.295 22.952 17.955 1.00 12.22 ? 126 LEU A N   1 
ATOM   951  C  CA  . LEU A 1 126 ? 10.585 21.528 17.797 1.00 12.31 ? 126 LEU A CA  1 
ATOM   952  C  C   . LEU A 1 126 ? 11.658 21.280 16.762 1.00 12.37 ? 126 LEU A C   1 
ATOM   953  O  O   . LEU A 1 126 ? 11.824 20.173 16.274 1.00 14.29 ? 126 LEU A O   1 
ATOM   954  C  CB  . LEU A 1 126 ? 9.313  20.741 17.579 1.00 14.83 ? 126 LEU A CB  1 
ATOM   955  C  CG  . LEU A 1 126 ? 8.180  21.020 18.553 1.00 15.42 ? 126 LEU A CG  1 
ATOM   956  C  CD1 . LEU A 1 126 ? 6.959  20.171 18.109 1.00 22.84 ? 126 LEU A CD1 1 
ATOM   957  C  CD2 . LEU A 1 126 ? 8.569  20.714 20.013 1.00 19.05 ? 126 LEU A CD2 1 
ATOM   958  N  N   . GLY A 1 127 ? 12.488 22.303 16.504 1.00 11.96 ? 127 GLY A N   1 
ATOM   959  C  CA  . GLY A 1 127 ? 13.571 22.128 15.565 1.00 12.26 ? 127 GLY A CA  1 
ATOM   960  C  C   . GLY A 1 127 ? 13.156 22.212 14.122 1.00 13.91 ? 127 GLY A C   1 
ATOM   961  O  O   . GLY A 1 127 ? 13.972 21.981 13.214 1.00 17.85 ? 127 GLY A O   1 
ATOM   962  N  N   . LYS A 1 128 ? 11.924 22.625 13.867 1.00 13.96 ? 128 LYS A N   1 
ATOM   963  C  CA  . LYS A 1 128 ? 11.350 22.653 12.516 1.00 16.01 ? 128 LYS A CA  1 
ATOM   964  C  C   . LYS A 1 128 ? 11.261 24.046 11.936 1.00 16.49 ? 128 LYS A C   1 
ATOM   965  O  O   . LYS A 1 128 ? 10.648 24.238 10.905 1.00 25.79 ? 128 LYS A O   1 
ATOM   966  C  CB  A LYS A 1 128 ? 9.977  21.963 12.598 0.76 80.49 ? 128 LYS A CB  1 
ATOM   967  C  CB  B LYS A 1 128 ? 10.056 21.873 12.405 0.24 20.27 ? 128 LYS A CB  1 
ATOM   968  C  CG  A LYS A 1 128 ? 10.071 20.507 13.057 0.76 80.17 ? 128 LYS A CG  1 
ATOM   969  C  CG  B LYS A 1 128 ? 10.236 20.359 12.301 0.24 25.30 ? 128 LYS A CG  1 
ATOM   970  C  CD  A LYS A 1 128 ? 8.923  19.571 13.102 0.76 65.30 ? 128 LYS A CD  1 
ATOM   971  C  CD  B LYS A 1 128 ? 11.697 19.956 12.207 0.24 39.44 ? 128 LYS A CD  1 
ATOM   972  C  CE  A LYS A 1 128 ? 9.243  18.189 13.689 0.76 56.51 ? 128 LYS A CE  1 
ATOM   973  C  CE  B LYS A 1 128 ? 12.133 19.615 10.776 0.24 50.02 ? 128 LYS A CE  1 
ATOM   974  N  NZ  A LYS A 1 128 ? 9.543  18.336 15.146 0.76 44.27 ? 128 LYS A NZ  1 
ATOM   975  N  NZ  B LYS A 1 128 ? 13.626 19.409 10.735 0.24 55.67 ? 128 LYS A NZ  1 
ATOM   976  N  N   . GLY A 1 129 ? 11.877 25.035 12.569 1.00 15.69 ? 129 GLY A N   1 
ATOM   977  C  CA  . GLY A 1 129 ? 11.827 26.410 12.164 1.00 15.51 ? 129 GLY A CA  1 
ATOM   978  C  C   . GLY A 1 129 ? 12.817 26.675 11.058 1.00 15.01 ? 129 GLY A C   1 
ATOM   979  O  O   . GLY A 1 129 ? 13.643 25.867 10.703 1.00 23.61 ? 129 GLY A O   1 
ATOM   980  N  N   . GLY A 1 130 ? 12.835 27.946 10.653 1.00 16.02 ? 130 GLY A N   1 
ATOM   981  C  CA  . GLY A 1 130 ? 13.528 28.290 9.440  1.00 16.75 ? 130 GLY A CA  1 
ATOM   982  C  C   . GLY A 1 130 ? 14.868 28.893 9.639  1.00 11.98 ? 130 GLY A C   1 
ATOM   983  O  O   . GLY A 1 130 ? 15.292 29.556 8.744  1.00 16.25 ? 130 GLY A O   1 
ATOM   984  N  N   . ASN A 1 131 ? 15.478 28.745 10.792 1.00 12.92 ? 131 ASN A N   1 
ATOM   985  C  CA  . ASN A 1 131 ? 16.809 29.225 11.059 1.00 10.98 ? 131 ASN A CA  1 
ATOM   986  C  C   . ASN A 1 131 ? 17.646 28.197 11.780 1.00 10.92 ? 131 ASN A C   1 
ATOM   987  O  O   . ASN A 1 131 ? 17.174 27.202 12.279 1.00 11.85 ? 131 ASN A O   1 
ATOM   988  C  CB  . ASN A 1 131 ? 16.812 30.554 11.803 1.00 10.38 ? 131 ASN A CB  1 
ATOM   989  C  CG  . ASN A 1 131 ? 16.108 30.507 13.128 1.00 10.19 ? 131 ASN A CG  1 
ATOM   990  O  OD1 . ASN A 1 131 ? 15.701 29.476 13.610 1.00 11.92 ? 131 ASN A OD1 1 
ATOM   991  N  ND2 . ASN A 1 131 ? 16.084 31.647 13.818 1.00 11.14 ? 131 ASN A ND2 1 
ATOM   992  N  N   . GLU A 1 132 ? 18.961 28.463 11.864 1.00 10.83 ? 132 GLU A N   1 
ATOM   993  C  CA  . GLU A 1 132 ? 19.832 27.549 12.589 1.00 11.79 ? 132 GLU A CA  1 
ATOM   994  C  C   . GLU A 1 132 ? 19.515 27.535 14.086 1.00 10.68 ? 132 GLU A C   1 
ATOM   995  O  O   . GLU A 1 132 ? 19.607 26.509 14.763 1.00 11.34 ? 132 GLU A O   1 
ATOM   996  C  CB  . GLU A 1 132 ? 21.307 27.853 12.364 1.00 12.86 ? 132 GLU A CB  1 
ATOM   997  C  CG  . GLU A 1 132 ? 22.240 26.889 13.062 1.00 15.84 ? 132 GLU A CG  1 
ATOM   998  C  CD  . GLU A 1 132 ? 23.680 27.103 12.862 1.00 18.55 ? 132 GLU A CD  1 
ATOM   999  O  OE1 . GLU A 1 132 ? 24.098 28.278 12.794 1.00 20.35 ? 132 GLU A OE1 1 
ATOM   1000 O  OE2 . GLU A 1 132 ? 24.403 26.098 12.801 1.00 32.70 ? 132 GLU A OE2 1 
ATOM   1001 N  N   . GLN A 1 133 ? 19.025 28.640 14.618 1.00 10.33 ? 133 GLN A N   1 
ATOM   1002 C  CA  . GLN A 1 133 ? 18.703 28.659 16.034 1.00 10.69 ? 133 GLN A CA  1 
ATOM   1003 C  C   . GLN A 1 133 ? 17.557 27.702 16.369 1.00 9.91  ? 133 GLN A C   1 
ATOM   1004 O  O   . GLN A 1 133 ? 17.495 27.125 17.447 1.00 10.33 ? 133 GLN A O   1 
ATOM   1005 C  CB  . GLN A 1 133 ? 18.317 30.084 16.417 1.00 10.92 ? 133 GLN A CB  1 
ATOM   1006 C  CG  . GLN A 1 133 ? 18.228 30.273 17.932 1.00 13.28 ? 133 GLN A CG  1 
ATOM   1007 C  CD  . GLN A 1 133 ? 19.601 30.095 18.550 1.00 17.00 ? 133 GLN A CD  1 
ATOM   1008 O  OE1 . GLN A 1 133 ? 20.622 30.499 18.021 1.00 19.54 ? 133 GLN A OE1 1 
ATOM   1009 N  NE2 . GLN A 1 133 ? 19.583 29.462 19.742 1.00 27.19 ? 133 GLN A NE2 1 
ATOM   1010 N  N   . SER A 1 134 ? 16.699 27.363 15.406 1.00 11.04 ? 134 SER A N   1 
ATOM   1011 C  CA  . SER A 1 134 ? 15.689 26.341 15.678 1.00 10.70 ? 134 SER A CA  1 
ATOM   1012 C  C   . SER A 1 134 ? 16.305 25.028 16.088 1.00 10.78 ? 134 SER A C   1 
ATOM   1013 O  O   . SER A 1 134 ? 15.775 24.314 16.945 1.00 10.70 ? 134 SER A O   1 
ATOM   1014 C  CB  . SER A 1 134 ? 14.840 26.165 14.416 1.00 12.08 ? 134 SER A CB  1 
ATOM   1015 O  OG  . SER A 1 134 ? 13.923 25.074 14.617 1.00 12.37 ? 134 SER A OG  1 
ATOM   1016 N  N   . THR A 1 135 ? 17.454 24.711 15.454 1.00 11.15 ? 135 THR A N   1 
ATOM   1017 C  CA  . THR A 1 135 ? 18.163 23.458 15.668 1.00 12.91 ? 135 THR A CA  1 
ATOM   1018 C  C   . THR A 1 135 ? 19.069 23.534 16.889 1.00 10.39 ? 135 THR A C   1 
ATOM   1019 O  O   . THR A 1 135 ? 19.717 22.549 17.181 1.00 11.92 ? 135 THR A O   1 
ATOM   1020 C  CB  . THR A 1 135 ? 19.066 23.143 14.426 1.00 17.59 ? 135 THR A CB  1 
ATOM   1021 O  OG1 . THR A 1 135 ? 20.254 23.958 14.408 1.00 20.08 ? 135 THR A OG1 1 
ATOM   1022 C  CG2 . THR A 1 135 ? 18.349 23.333 13.132 1.00 20.14 ? 135 THR A CG2 1 
ATOM   1023 N  N   . LYS A 1 136 ? 19.094 24.636 17.605 1.00 10.15 ? 136 LYS A N   1 
ATOM   1024 C  CA  . LYS A 1 136 ? 19.800 24.822 18.873 1.00 10.24 ? 136 LYS A CA  1 
ATOM   1025 C  C   . LYS A 1 136 ? 18.853 24.914 20.066 1.00 9.63  ? 136 LYS A C   1 
ATOM   1026 O  O   . LYS A 1 136 ? 18.997 24.203 21.057 1.00 11.23 ? 136 LYS A O   1 
ATOM   1027 C  CB  . LYS A 1 136 ? 20.698 26.082 18.840 1.00 12.32 ? 136 LYS A CB  1 
ATOM   1028 C  CG  . LYS A 1 136 ? 21.794 26.043 17.791 1.00 15.03 ? 136 LYS A CG  1 
ATOM   1029 C  CD  . LYS A 1 136 ? 22.571 27.341 17.786 1.00 22.48 ? 136 LYS A CD  1 
ATOM   1030 C  CE  . LYS A 1 136 ? 23.805 27.261 16.943 1.00 33.21 ? 136 LYS A CE  1 
ATOM   1031 N  NZ  . LYS A 1 136 ? 24.531 28.576 17.046 1.00 73.22 ? 136 LYS A NZ  1 
ATOM   1032 N  N   . THR A 1 137 ? 17.854 25.796 20.002 1.00 10.49 ? 137 THR A N   1 
ATOM   1033 C  CA  . THR A 1 137 ? 16.984 26.082 21.133 1.00 10.08 ? 137 THR A CA  1 
ATOM   1034 C  C   . THR A 1 137 ? 15.502 25.964 20.815 1.00 9.80  ? 137 THR A C   1 
ATOM   1035 O  O   . THR A 1 137 ? 14.666 26.204 21.695 1.00 10.98 ? 137 THR A O   1 
ATOM   1036 C  CB  . THR A 1 137 ? 17.253 27.508 21.639 1.00 11.45 ? 137 THR A CB  1 
ATOM   1037 O  OG1 . THR A 1 137 ? 16.856 28.374 20.575 1.00 12.71 ? 137 THR A OG1 1 
ATOM   1038 C  CG2 . THR A 1 137 ? 18.700 27.732 22.078 1.00 16.92 ? 137 THR A CG2 1 
ATOM   1039 N  N   . GLY A 1 138 ? 15.121 25.736 19.563 1.00 10.10 ? 138 GLY A N   1 
ATOM   1040 C  CA  . GLY A 1 138 ? 13.735 25.776 19.169 1.00 10.92 ? 138 GLY A CA  1 
ATOM   1041 C  C   . GLY A 1 138 ? 13.124 27.161 19.217 1.00 10.71 ? 138 GLY A C   1 
ATOM   1042 O  O   . GLY A 1 138 ? 11.902 27.294 19.146 1.00 11.79 ? 138 GLY A O   1 
ATOM   1043 N  N   . ASN A 1 139 ? 13.894 28.211 19.321 1.00 11.05 ? 139 ASN A N   1 
ATOM   1044 C  CA  . ASN A 1 139 ? 13.410 29.592 19.285 1.00 11.36 ? 139 ASN A CA  1 
ATOM   1045 C  C   . ASN A 1 139 ? 12.415 29.860 20.413 1.00 11.72 ? 139 ASN A C   1 
ATOM   1046 O  O   . ASN A 1 139 ? 11.593 30.715 20.291 1.00 13.36 ? 139 ASN A O   1 
ATOM   1047 C  CB  . ASN A 1 139 ? 12.871 29.948 17.909 1.00 11.83 ? 139 ASN A CB  1 
ATOM   1048 C  CG  . ASN A 1 139 ? 13.909 30.048 16.840 1.00 11.07 ? 139 ASN A CG  1 
ATOM   1049 O  OD1 . ASN A 1 139 ? 14.825 30.897 16.925 1.00 13.98 ? 139 ASN A OD1 1 
ATOM   1050 N  ND2 . ASN A 1 139 ? 13.797 29.221 15.814 1.00 13.10 ? 139 ASN A ND2 1 
ATOM   1051 N  N   . ALA A 1 140 ? 12.588 29.199 21.568 1.00 12.70 ? 140 ALA A N   1 
ATOM   1052 C  CA  . ALA A 1 140 ? 11.647 29.334 22.646 1.00 13.28 ? 140 ALA A CA  1 
ATOM   1053 C  C   . ALA A 1 140 ? 11.877 30.586 23.490 1.00 13.12 ? 140 ALA A C   1 
ATOM   1054 O  O   . ALA A 1 140 ? 11.097 30.924 24.387 1.00 14.32 ? 140 ALA A O   1 
ATOM   1055 C  CB  . ALA A 1 140 ? 11.625 28.125 23.574 1.00 14.05 ? 140 ALA A CB  1 
ATOM   1056 N  N   . GLY A 1 141 ? 12.949 31.296 23.217 1.00 14.48 ? 141 GLY A N   1 
ATOM   1057 C  CA  . GLY A 1 141 ? 13.072 32.581 23.856 1.00 15.17 ? 141 GLY A CA  1 
ATOM   1058 C  C   . GLY A 1 141 ? 13.565 32.532 25.314 1.00 15.00 ? 141 GLY A C   1 
ATOM   1059 O  O   . GLY A 1 141 ? 14.225 31.611 25.774 1.00 14.95 ? 141 GLY A O   1 
ATOM   1060 N  N   . SER A 1 142 ? 13.265 33.598 26.056 1.00 14.13 ? 142 SER A N   1 
ATOM   1061 C  CA  . SER A 1 142 ? 13.749 33.797 27.417 1.00 15.74 ? 142 SER A CA  1 
ATOM   1062 C  C   . SER A 1 142 ? 13.250 32.686 28.374 1.00 13.12 ? 142 SER A C   1 
ATOM   1063 O  O   . SER A 1 142 ? 12.233 32.078 28.184 1.00 12.52 ? 142 SER A O   1 
ATOM   1064 C  CB  . SER A 1 142 ? 13.139 35.137 27.902 1.00 19.85 ? 142 SER A CB  1 
ATOM   1065 O  OG  . SER A 1 142 ? 13.436 36.174 26.988 1.00 25.19 ? 142 SER A OG  1 
ATOM   1066 N  N   . ARG A 1 143 ? 14.063 32.504 29.418 1.00 15.65 ? 143 ARG A N   1 
ATOM   1067 C  CA  . ARG A 1 143 ? 13.785 31.678 30.546 1.00 14.19 ? 143 ARG A CA  1 
ATOM   1068 C  C   . ARG A 1 143 ? 12.885 32.404 31.483 1.00 14.98 ? 143 ARG A C   1 
ATOM   1069 O  O   . ARG A 1 143 ? 13.175 33.503 31.937 1.00 24.11 ? 143 ARG A O   1 
ATOM   1070 C  CB  . ARG A 1 143 ? 15.099 31.349 31.243 1.00 18.81 ? 143 ARG A CB  1 
ATOM   1071 C  CG  . ARG A 1 143 ? 16.065 30.591 30.338 1.00 27.79 ? 143 ARG A CG  1 
ATOM   1072 C  CD  . ARG A 1 143 ? 17.435 30.400 30.997 1.00 51.30 ? 143 ARG A CD  1 
ATOM   1073 N  NE  . ARG A 1 143 ? 17.938 31.675 31.519 1.00 76.74 ? 143 ARG A NE  1 
ATOM   1074 C  CZ  . ARG A 1 143 ? 19.245 31.940 31.339 1.00 95.47 ? 143 ARG A CZ  1 
ATOM   1075 N  NH1 . ARG A 1 143 ? 20.016 31.071 30.710 1.00 98.67 ? 143 ARG A NH1 1 
ATOM   1076 N  NH2 . ARG A 1 143 ? 19.760 33.084 31.803 1.00 98.81 ? 143 ARG A NH2 1 
ATOM   1077 N  N   . LEU A 1 144 ? 11.710 31.891 31.814 1.00 12.86 ? 144 LEU A N   1 
ATOM   1078 C  CA  . LEU A 1 144 ? 10.829 32.549 32.778 1.00 13.74 ? 144 LEU A CA  1 
ATOM   1079 C  C   . LEU A 1 144 ? 10.970 31.996 34.188 1.00 13.30 ? 144 LEU A C   1 
ATOM   1080 O  O   . LEU A 1 144 ? 10.728 32.745 35.124 1.00 17.33 ? 144 LEU A O   1 
ATOM   1081 C  CB  A LEU A 1 144 ? 9.395  32.581 32.325 0.51 14.28 ? 144 LEU A CB  1 
ATOM   1082 C  CB  B LEU A 1 144 ? 9.365  32.304 32.419 0.49 15.88 ? 144 LEU A CB  1 
ATOM   1083 C  CG  A LEU A 1 144 ? 9.166  33.297 31.008 0.51 16.89 ? 144 LEU A CG  1 
ATOM   1084 C  CG  B LEU A 1 144 ? 8.762  32.771 31.126 0.49 20.91 ? 144 LEU A CG  1 
ATOM   1085 C  CD1 A LEU A 1 144 ? 7.655  33.456 30.846 0.51 20.82 ? 144 LEU A CD1 1 
ATOM   1086 C  CD1 B LEU A 1 144 ? 7.401  32.101 30.888 0.49 21.57 ? 144 LEU A CD1 1 
ATOM   1087 C  CD2 A LEU A 1 144 ? 9.832  34.652 30.913 0.51 15.45 ? 144 LEU A CD2 1 
ATOM   1088 C  CD2 B LEU A 1 144 ? 8.638  34.286 31.076 0.49 30.10 ? 144 LEU A CD2 1 
ATOM   1089 N  N   . ALA A 1 145 ? 11.293 30.727 34.340 1.00 12.60 ? 145 ALA A N   1 
ATOM   1090 C  CA  . ALA A 1 145 ? 11.494 30.108 35.619 1.00 11.50 ? 145 ALA A CA  1 
ATOM   1091 C  C   . ALA A 1 145 ? 12.408 28.919 35.444 1.00 11.17 ? 145 ALA A C   1 
ATOM   1092 O  O   . ALA A 1 145 ? 12.369 28.256 34.392 1.00 12.66 ? 145 ALA A O   1 
ATOM   1093 C  CB  . ALA A 1 145 ? 10.192 29.765 36.265 1.00 12.90 ? 145 ALA A CB  1 
ATOM   1094 N  N   . CYS A 1 146 ? 13.148 28.631 36.489 1.00 11.04 ? 146 CYS A N   1 
ATOM   1095 C  CA  . CYS A 1 146 ? 14.088 27.509 36.397 1.00 11.32 ? 146 CYS A CA  1 
ATOM   1096 C  C   . CYS A 1 146 ? 14.239 26.923 37.792 1.00 10.04 ? 146 CYS A C   1 
ATOM   1097 O  O   . CYS A 1 146 ? 13.910 27.535 38.816 1.00 11.03 ? 146 CYS A O   1 
ATOM   1098 C  CB  A CYS A 1 146 ? 15.472 28.069 36.034 0.50 19.20 ? 146 CYS A CB  1 
ATOM   1099 C  CB  B CYS A 1 146 ? 15.391 27.927 35.760 0.34 15.45 ? 146 CYS A CB  1 
ATOM   1100 C  CB  C CYS A 1 146 ? 15.385 27.914 35.733 0.16 12.69 ? 146 CYS A CB  1 
ATOM   1101 S  SG  A CYS A 1 146 ? 15.671 29.079 34.580 0.50 16.84 ? 146 CYS A SG  1 
ATOM   1102 S  SG  B CYS A 1 146 ? 16.243 29.134 36.795 0.34 24.46 ? 146 CYS A SG  1 
ATOM   1103 S  SG  C CYS A 1 146 ? 16.256 29.115 36.759 0.16 22.97 ? 146 CYS A SG  1 
ATOM   1104 N  N   . GLY A 1 147 ? 14.742 25.708 37.848 1.00 9.82  ? 147 GLY A N   1 
ATOM   1105 C  CA  . GLY A 1 147 ? 15.085 25.090 39.129 1.00 9.75  ? 147 GLY A CA  1 
ATOM   1106 C  C   . GLY A 1 147 ? 15.959 23.909 38.943 1.00 8.97  ? 147 GLY A C   1 
ATOM   1107 O  O   . GLY A 1 147 ? 15.873 23.193 37.942 1.00 10.79 ? 147 GLY A O   1 
ATOM   1108 N  N   . VAL A 1 148 ? 16.787 23.627 39.954 1.00 9.60  ? 148 VAL A N   1 
ATOM   1109 C  CA  . VAL A 1 148 ? 17.632 22.462 39.944 1.00 9.49  ? 148 VAL A CA  1 
ATOM   1110 C  C   . VAL A 1 148 ? 16.794 21.209 40.117 1.00 8.37  ? 148 VAL A C   1 
ATOM   1111 O  O   . VAL A 1 148 ? 15.854 21.156 40.916 1.00 10.34 ? 148 VAL A O   1 
ATOM   1112 C  CB  A VAL A 1 148 ? 18.688 22.623 41.059 0.53 17.11 ? 148 VAL A CB  1 
ATOM   1113 C  CB  B VAL A 1 148 ? 18.725 22.432 41.035 0.47 11.69 ? 148 VAL A CB  1 
ATOM   1114 C  CG1 A VAL A 1 148 ? 19.616 21.438 41.156 0.53 15.62 ? 148 VAL A CG1 1 
ATOM   1115 C  CG1 B VAL A 1 148 ? 18.149 22.368 42.429 0.47 15.38 ? 148 VAL A CG1 1 
ATOM   1116 C  CG2 A VAL A 1 148 ? 19.451 23.930 40.761 0.53 20.16 ? 148 VAL A CG2 1 
ATOM   1117 C  CG2 B VAL A 1 148 ? 19.713 21.309 40.737 0.47 17.86 ? 148 VAL A CG2 1 
ATOM   1118 N  N   . ILE A 1 149 ? 17.123 20.156 39.383 1.00 8.18  ? 149 ILE A N   1 
ATOM   1119 C  CA  . ILE A 1 149 ? 16.464 18.886 39.489 1.00 8.41  ? 149 ILE A CA  1 
ATOM   1120 C  C   . ILE A 1 149 ? 17.145 18.130 40.618 1.00 8.57  ? 149 ILE A C   1 
ATOM   1121 O  O   . ILE A 1 149 ? 18.284 17.701 40.454 1.00 12.08 ? 149 ILE A O   1 
ATOM   1122 C  CB  . ILE A 1 149 ? 16.503 18.117 38.157 1.00 8.30  ? 149 ILE A CB  1 
ATOM   1123 C  CG1 . ILE A 1 149 ? 15.816 18.926 37.056 1.00 8.85  ? 149 ILE A CG1 1 
ATOM   1124 C  CG2 . ILE A 1 149 ? 15.879 16.769 38.314 1.00 9.65  ? 149 ILE A CG2 1 
ATOM   1125 C  CD1 . ILE A 1 149 ? 16.110 18.423 35.672 1.00 10.47 ? 149 ILE A CD1 1 
ATOM   1126 N  N   . GLY A 1 150 ? 16.491 17.993 41.766 1.00 8.98  ? 150 GLY A N   1 
ATOM   1127 C  CA  . GLY A 1 150 ? 17.120 17.397 42.958 1.00 9.59  ? 150 GLY A CA  1 
ATOM   1128 C  C   . GLY A 1 150 ? 16.479 16.102 43.370 1.00 9.04  ? 150 GLY A C   1 
ATOM   1129 O  O   . GLY A 1 150 ? 15.285 15.927 43.207 1.00 10.25 ? 150 GLY A O   1 
ATOM   1130 N  N   . ILE A 1 151 ? 17.254 15.180 43.916 1.00 10.85 ? 151 ILE A N   1 
ATOM   1131 C  CA  . ILE A 1 151 ? 16.660 13.947 44.466 1.00 11.06 ? 151 ILE A CA  1 
ATOM   1132 C  C   . ILE A 1 151 ? 15.643 14.269 45.528 1.00 10.65 ? 151 ILE A C   1 
ATOM   1133 O  O   . ILE A 1 151 ? 15.859 15.179 46.354 1.00 12.39 ? 151 ILE A O   1 
ATOM   1134 C  CB  . ILE A 1 151 ? 17.731 13.010 45.014 1.00 11.84 ? 151 ILE A CB  1 
ATOM   1135 C  CG1 . ILE A 1 151 ? 18.611 12.543 43.903 1.00 15.15 ? 151 ILE A CG1 1 
ATOM   1136 C  CG2 . ILE A 1 151 ? 17.090 11.856 45.766 1.00 14.93 ? 151 ILE A CG2 1 
ATOM   1137 C  CD1 . ILE A 1 151 ? 17.949 11.549 42.949 1.00 15.88 ? 151 ILE A CD1 1 
ATOM   1138 N  N   . ALA A 1 152 ? 14.511 13.594 45.523 1.00 11.67 ? 152 ALA A N   1 
ATOM   1139 C  CA  . ALA A 1 152 ? 13.452 13.843 46.525 1.00 11.81 ? 152 ALA A CA  1 
ATOM   1140 C  C   . ALA A 1 152 ? 13.936 13.603 47.943 1.00 13.80 ? 152 ALA A C   1 
ATOM   1141 O  O   . ALA A 1 152 ? 14.609 12.588 48.206 1.00 16.08 ? 152 ALA A O   1 
ATOM   1142 C  CB  . ALA A 1 152 ? 12.229 13.063 46.163 1.00 14.15 ? 152 ALA A CB  1 
ATOM   1143 N  N   . GLN A 1 153 ? 13.594 14.515 48.863 1.00 14.88 ? 153 GLN A N   1 
ATOM   1144 C  CA  . GLN A 1 153 ? 14.028 14.426 50.227 1.00 16.90 ? 153 GLN A CA  1 
ATOM   1145 C  C   . GLN A 1 153 ? 13.044 13.758 51.178 1.00 29.37 ? 153 GLN A C   1 
ATOM   1146 O  O   . GLN A 1 153 ? 13.415 13.622 52.378 1.00 35.40 ? 153 GLN A O   1 
ATOM   1147 C  CB  . GLN A 1 153 ? 14.388 15.849 50.702 1.00 26.24 ? 153 GLN A CB  1 
ATOM   1148 C  CG  . GLN A 1 153 ? 15.559 16.340 49.811 1.00 36.08 ? 153 GLN A CG  1 
ATOM   1149 C  CD  . GLN A 1 153 ? 16.717 15.351 49.953 1.00 47.01 ? 153 GLN A CD  1 
ATOM   1150 O  OE1 . GLN A 1 153 ? 17.298 14.873 48.950 1.00 27.35 ? 153 GLN A OE1 1 
ATOM   1151 N  NE2 . GLN A 1 153 ? 17.133 15.118 51.196 1.00 75.76 ? 153 GLN A NE2 1 
ATOM   1152 O  OXT . GLN A 1 153 ? 11.945 13.476 50.765 1.00 29.52 ? 153 GLN A OXT 1 
HETATM 1153 ZN ZN  . ZN  B 2 .   ? 17.157 21.220 22.645 1.00 9.44  ? 154 ZN  A ZN  1 
HETATM 1154 CU CU  . CU  C 3 .   ? 14.914 25.254 27.532 0.41 9.96  ? 155 CU  A CU  1 
HETATM 1155 CD CD  . CD  D 4 .   ? 30.297 21.138 36.112 0.83 10.94 ? 156 CD  A CD  1 
HETATM 1156 CD CD  . CD  E 4 .   ? 11.900 37.803 26.066 0.58 15.55 ? 157 CD  A CD  1 
HETATM 1157 CD CD  . CD  F 4 .   ? 27.924 26.742 34.872 0.73 12.41 ? 158 CD  A CD  1 
HETATM 1158 CD CD  . CD  G 4 .   ? 28.937 10.913 27.860 0.59 16.23 ? 159 CD  A CD  1 
HETATM 1159 CD CD  . CD  H 4 .   ? 13.082 -3.070 39.206 0.33 10.34 ? 160 CD  A CD  1 
HETATM 1160 CD CD  . CD  I 4 .   ? 11.725 14.359 13.074 0.22 15.14 ? 161 CD  A CD  1 
HETATM 1161 CD CD  . CD  J 4 .   ? 27.711 12.564 30.872 0.31 8.82  ? 162 CD  A CD  1 
HETATM 1162 CD CD  . CD  K 4 .   ? 26.740 5.267  30.191 0.23 16.83 ? 163 CD  A CD  1 
HETATM 1163 CD CD  . CD  L 4 .   ? 15.634 25.985 26.302 0.45 90.85 ? 164 CD  A CD  1 
HETATM 1164 CL CL  . CL  M 5 .   ? 11.473 35.902 24.626 1.00 27.53 ? 165 CL  A CL  1 
HETATM 1165 CL CL  . CL  N 5 .   ? 13.865 38.865 24.948 1.00 23.33 ? 166 CL  A CL  1 
HETATM 1166 O  O   . HOH O 6 .   ? 15.863 31.089 21.520 1.00 8.41  ? 167 HOH A O   1 
HETATM 1167 O  O   . HOH O 6 .   ? 19.496 11.891 30.962 1.00 9.36  ? 168 HOH A O   1 
HETATM 1168 O  O   . HOH O 6 .   ? 18.510 31.375 28.881 1.00 10.26 ? 169 HOH A O   1 
HETATM 1169 O  O   . HOH O 6 .   ? 8.518  11.998 42.422 1.00 10.66 ? 170 HOH A O   1 
HETATM 1170 O  O   . HOH O 6 .   ? 14.608 22.792 42.615 1.00 11.87 ? 171 HOH A O   1 
HETATM 1171 O  O   . HOH O 6 .   ? 22.849 8.052  31.999 1.00 12.53 ? 172 HOH A O   1 
HETATM 1172 O  O   . HOH O 6 .   ? 20.278 10.289 28.829 1.00 12.54 ? 173 HOH A O   1 
HETATM 1173 O  O   . HOH O 6 .   ? 22.177 14.907 23.742 1.00 12.58 ? 174 HOH A O   1 
HETATM 1174 O  O   . HOH O 6 .   ? 11.871 19.993 22.737 1.00 12.63 ? 175 HOH A O   1 
HETATM 1175 O  O   . HOH O 6 .   ? 14.789 26.996 24.306 1.00 13.02 ? 176 HOH A O   1 
HETATM 1176 O  O   . HOH O 6 .   ? 17.062 5.766  38.151 1.00 13.20 ? 177 HOH A O   1 
HETATM 1177 O  O   . HOH O 6 .   ? 29.951 23.127 35.075 1.00 13.46 ? 178 HOH A O   1 
HETATM 1178 O  O   . HOH O 6 .   ? 11.182 -4.466 40.130 1.00 13.52 ? 179 HOH A O   1 
HETATM 1179 O  O   . HOH O 6 .   ? 21.534 28.284 37.939 1.00 14.44 ? 180 HOH A O   1 
HETATM 1180 O  O   . HOH O 6 .   ? 20.913 24.494 23.190 1.00 14.55 ? 181 HOH A O   1 
HETATM 1181 O  O   . HOH O 6 .   ? 26.300 14.445 31.025 1.00 15.33 ? 182 HOH A O   1 
HETATM 1182 O  O   . HOH O 6 .   ? 5.458  3.086  29.169 1.00 15.34 ? 183 HOH A O   1 
HETATM 1183 O  O   . HOH O 6 .   ? 15.610 29.625 24.398 1.00 15.68 ? 184 HOH A O   1 
HETATM 1184 O  O   . HOH O 6 .   ? 21.776 6.176  40.019 1.00 15.73 ? 185 HOH A O   1 
HETATM 1185 O  O   . HOH O 6 .   ? -6.768 24.065 33.406 1.00 15.97 ? 186 HOH A O   1 
HETATM 1186 O  O   . HOH O 6 .   ? 29.165 13.606 25.276 1.00 16.10 ? 187 HOH A O   1 
HETATM 1187 O  O   . HOH O 6 .   ? 14.956 6.518  30.255 1.00 16.17 ? 188 HOH A O   1 
HETATM 1188 O  O   . HOH O 6 .   ? 8.646  12.439 25.816 1.00 16.18 ? 189 HOH A O   1 
HETATM 1189 O  O   . HOH O 6 .   ? 11.343 3.395  34.689 1.00 16.36 ? 190 HOH A O   1 
HETATM 1190 O  O   . HOH O 6 .   ? 20.322 13.272 22.525 1.00 16.83 ? 191 HOH A O   1 
HETATM 1191 O  O   . HOH O 6 .   ? 14.928 8.597  44.996 1.00 17.14 ? 192 HOH A O   1 
HETATM 1192 O  O   . HOH O 6 .   ? 4.930  12.292 26.954 1.00 17.20 ? 193 HOH A O   1 
HETATM 1193 O  O   . HOH O 6 .   ? 3.085  22.989 41.158 1.00 17.36 ? 194 HOH A O   1 
HETATM 1194 O  O   . HOH O 6 .   ? 7.788  15.900 19.417 1.00 17.81 ? 195 HOH A O   1 
HETATM 1195 O  O   . HOH O 6 .   ? 19.960 16.035 44.365 1.00 17.83 ? 196 HOH A O   1 
HETATM 1196 O  O   . HOH O 6 .   ? -2.095 22.228 30.680 1.00 18.10 ? 197 HOH A O   1 
HETATM 1197 O  O   . HOH O 6 .   ? 26.823 26.979 14.063 1.00 18.33 ? 198 HOH A O   1 
HETATM 1198 O  O   . HOH O 6 .   ? 24.444 14.282 38.072 1.00 18.39 ? 199 HOH A O   1 
HETATM 1199 O  O   . HOH O 6 .   ? -2.495 27.193 40.393 1.00 18.42 ? 200 HOH A O   1 
HETATM 1200 O  O   . HOH O 6 .   ? 6.576  14.163 25.461 1.00 18.51 ? 201 HOH A O   1 
HETATM 1201 O  O   . HOH O 6 .   ? 25.149 19.305 27.684 1.00 18.62 ? 202 HOH A O   1 
HETATM 1202 O  O   . HOH O 6 .   ? 13.690 31.897 10.809 1.00 18.81 ? 203 HOH A O   1 
HETATM 1203 O  O   . HOH O 6 .   ? 15.474 17.528 15.218 1.00 19.02 ? 204 HOH A O   1 
HETATM 1204 O  O   . HOH O 6 .   ? 22.279 21.970 19.018 1.00 19.24 ? 205 HOH A O   1 
HETATM 1205 O  O   . HOH O 6 .   ? 14.272 14.288 13.648 1.00 19.37 ? 206 HOH A O   1 
HETATM 1206 O  O   . HOH O 6 .   ? -1.664 31.247 37.049 1.00 19.62 ? 207 HOH A O   1 
HETATM 1207 O  O   . HOH O 6 .   ? 6.430  16.916 25.938 1.00 19.77 ? 208 HOH A O   1 
HETATM 1208 O  O   . HOH O 6 .   ? 24.664 5.519  31.654 1.00 20.50 ? 209 HOH A O   1 
HETATM 1209 O  O   . HOH O 6 .   ? 29.098 11.007 25.371 1.00 20.52 ? 210 HOH A O   1 
HETATM 1210 O  O   . HOH O 6 .   ? 4.157  18.096 27.144 1.00 20.66 ? 211 HOH A O   1 
HETATM 1211 O  O   . HOH O 6 .   ? 2.778  18.095 29.469 1.00 20.93 ? 212 HOH A O   1 
HETATM 1212 O  O   . HOH O 6 .   ? 4.454  33.497 30.402 1.00 21.14 ? 213 HOH A O   1 
HETATM 1213 O  O   . HOH O 6 .   ? -5.514 29.682 38.362 1.00 21.71 ? 214 HOH A O   1 
HETATM 1214 O  O   . HOH O 6 .   ? 5.703  18.559 23.593 1.00 21.72 ? 215 HOH A O   1 
HETATM 1215 O  O   . HOH O 6 .   ? 4.364  20.913 21.008 1.00 22.09 ? 216 HOH A O   1 
HETATM 1216 O  O   . HOH O 6 .   ? 16.703 20.867 14.426 1.00 22.18 ? 217 HOH A O   1 
HETATM 1217 O  O   . HOH O 6 .   ? 28.393 23.516 27.574 1.00 22.29 ? 218 HOH A O   1 
HETATM 1218 O  O   . HOH O 6 .   ? 1.062  20.784 29.112 1.00 22.44 ? 219 HOH A O   1 
HETATM 1219 O  O   . HOH O 6 .   ? -0.827 17.746 30.422 1.00 22.62 ? 220 HOH A O   1 
HETATM 1220 O  O   . HOH O 6 .   ? 14.755 23.503 11.128 1.00 22.74 ? 221 HOH A O   1 
HETATM 1221 O  O   . HOH O 6 .   ? -0.356 16.870 35.325 1.00 22.82 ? 222 HOH A O   1 
HETATM 1222 O  O   . HOH O 6 .   ? -3.730 23.567 32.583 1.00 22.93 ? 223 HOH A O   1 
HETATM 1223 O  O   . HOH O 6 .   ? 17.265 27.953 25.857 1.00 23.08 ? 224 HOH A O   1 
HETATM 1224 O  O   . HOH O 6 .   ? 21.379 4.078  34.283 1.00 23.16 ? 225 HOH A O   1 
HETATM 1225 O  O   . HOH O 6 .   ? 24.717 14.999 35.022 1.00 23.22 ? 226 HOH A O   1 
HETATM 1226 O  O   . HOH O 6 .   ? 14.073 10.068 47.211 1.00 23.34 ? 227 HOH A O   1 
HETATM 1227 O  O   . HOH O 6 .   ? 29.547 25.094 40.917 1.00 23.46 ? 228 HOH A O   1 
HETATM 1228 O  O   . HOH O 6 .   ? 10.126 29.000 14.528 1.00 23.67 ? 229 HOH A O   1 
HETATM 1229 O  O   . HOH O 6 .   ? 24.690 21.753 22.609 1.00 24.00 ? 230 HOH A O   1 
HETATM 1230 O  O   . HOH O 6 .   ? 20.179 14.620 10.709 1.00 24.55 ? 231 HOH A O   1 
HETATM 1231 O  O   . HOH O 6 .   ? 27.036 13.529 34.426 1.00 24.61 ? 232 HOH A O   1 
HETATM 1232 O  O   . HOH O 6 .   ? -2.950 29.888 39.164 1.00 24.67 ? 233 HOH A O   1 
HETATM 1233 O  O   . HOH O 6 .   ? 11.286 11.903 13.737 1.00 24.91 ? 234 HOH A O   1 
HETATM 1234 O  O   . HOH O 6 .   ? 8.754  32.985 40.096 1.00 24.94 ? 235 HOH A O   1 
HETATM 1235 O  O   . HOH O 6 .   ? 21.997 9.765  26.626 1.00 25.09 ? 236 HOH A O   1 
HETATM 1236 O  O   . HOH O 6 .   ? 22.797 23.697 40.091 1.00 25.13 ? 237 HOH A O   1 
HETATM 1237 O  O   . HOH O 6 .   ? 14.463 19.322 44.911 1.00 25.18 ? 238 HOH A O   1 
HETATM 1238 O  O   . HOH O 6 .   ? 27.165 22.892 46.673 1.00 25.35 ? 239 HOH A O   1 
HETATM 1239 O  O   . HOH O 6 .   ? 0.960  29.202 21.690 1.00 25.50 ? 240 HOH A O   1 
HETATM 1240 O  O   . HOH O 6 .   ? -0.277 18.733 37.178 1.00 25.56 ? 241 HOH A O   1 
HETATM 1241 O  O   . HOH O 6 .   ? 8.649  34.320 36.319 1.00 26.02 ? 242 HOH A O   1 
HETATM 1242 O  O   . HOH O 6 .   ? 18.872 10.978 21.720 1.00 26.12 ? 243 HOH A O   1 
HETATM 1243 O  O   . HOH O 6 .   ? 29.012 13.364 28.018 1.00 26.14 ? 244 HOH A O   1 
HETATM 1244 O  O   . HOH O 6 .   ? 15.334 -4.632 32.400 1.00 26.21 ? 245 HOH A O   1 
HETATM 1245 O  O   . HOH O 6 .   ? 12.948 18.565 14.306 1.00 26.49 ? 246 HOH A O   1 
HETATM 1246 O  O   . HOH O 6 .   ? 9.080  5.296  35.735 1.00 26.94 ? 247 HOH A O   1 
HETATM 1247 O  O   . HOH O 6 .   ? 15.071 32.738 19.031 1.00 27.06 ? 248 HOH A O   1 
HETATM 1248 O  O   . HOH O 6 .   ? 4.178  35.007 32.580 1.00 27.33 ? 249 HOH A O   1 
HETATM 1249 O  O   . HOH O 6 .   ? 19.261 3.501  40.048 1.00 27.34 ? 250 HOH A O   1 
HETATM 1250 O  O   . HOH O 6 .   ? 26.582 29.098 13.239 1.00 27.37 ? 251 HOH A O   1 
HETATM 1251 O  O   . HOH O 6 .   ? 6.877  6.632  44.065 1.00 27.39 ? 252 HOH A O   1 
HETATM 1252 O  O   . HOH O 6 .   ? 20.806 1.256  33.647 1.00 27.43 ? 253 HOH A O   1 
HETATM 1253 O  O   . HOH O 6 .   ? 16.810 -0.756 37.954 1.00 27.43 ? 254 HOH A O   1 
HETATM 1254 O  O   . HOH O 6 .   ? 15.501 3.802  39.004 1.00 27.48 ? 255 HOH A O   1 
HETATM 1255 O  O   . HOH O 6 .   ? 16.158 25.281 42.383 1.00 28.68 ? 256 HOH A O   1 
HETATM 1256 O  O   . HOH O 6 .   ? 10.375 39.442 25.215 1.00 28.79 ? 257 HOH A O   1 
HETATM 1257 O  O   . HOH O 6 .   ? 16.581 36.118 39.482 1.00 28.81 ? 258 HOH A O   1 
HETATM 1258 O  O   . HOH O 6 .   ? 10.647 9.513  24.536 1.00 28.94 ? 259 HOH A O   1 
HETATM 1259 O  O   . HOH O 6 .   ? 14.219 27.112 42.290 1.00 29.19 ? 260 HOH A O   1 
HETATM 1260 O  O   . HOH O 6 .   ? 5.180  34.475 27.975 1.00 29.21 ? 261 HOH A O   1 
HETATM 1261 O  O   . HOH O 6 .   ? 12.075 30.660 12.723 1.00 29.31 ? 262 HOH A O   1 
HETATM 1262 O  O   . HOH O 6 .   ? 26.459 11.537 35.966 1.00 29.33 ? 263 HOH A O   1 
HETATM 1263 O  O   . HOH O 6 .   ? 16.976 36.225 37.366 1.00 29.79 ? 264 HOH A O   1 
HETATM 1264 O  O   . HOH O 6 .   ? 5.233  31.348 21.019 1.00 29.85 ? 265 HOH A O   1 
HETATM 1265 O  O   . HOH O 6 .   ? 1.882  20.949 25.310 1.00 29.95 ? 266 HOH A O   1 
HETATM 1266 O  O   . HOH O 6 .   ? 18.942 6.851  40.012 1.00 30.17 ? 267 HOH A O   1 
HETATM 1267 O  O   . HOH O 6 .   ? 26.970 24.543 31.711 1.00 30.34 ? 268 HOH A O   1 
HETATM 1268 O  O   . HOH O 6 .   ? 8.507  7.409  26.126 1.00 30.48 ? 269 HOH A O   1 
HETATM 1269 O  O   . HOH O 6 .   ? 19.779 27.691 25.451 1.00 30.52 ? 270 HOH A O   1 
HETATM 1270 O  O   . HOH O 6 .   ? 15.872 36.135 33.030 1.00 30.54 ? 271 HOH A O   1 
HETATM 1271 O  O   . HOH O 6 .   ? 8.311  39.732 26.376 1.00 30.60 ? 272 HOH A O   1 
HETATM 1272 O  O   . HOH O 6 .   ? 31.194 5.442  32.285 1.00 30.94 ? 273 HOH A O   1 
HETATM 1273 O  O   . HOH O 6 .   ? 27.034 17.464 28.670 1.00 31.03 ? 274 HOH A O   1 
HETATM 1274 O  O   . HOH O 6 .   ? 12.292 38.998 28.247 1.00 31.17 ? 275 HOH A O   1 
HETATM 1275 O  O   . HOH O 6 .   ? 13.670 -1.678 30.277 1.00 31.34 ? 276 HOH A O   1 
HETATM 1276 O  O   . HOH O 6 .   ? 10.898 27.728 7.315  1.00 31.44 ? 277 HOH A O   1 
HETATM 1277 O  O   . HOH O 6 .   ? 7.950  15.967 16.577 1.00 31.69 ? 278 HOH A O   1 
HETATM 1278 O  O   . HOH O 6 .   ? 5.573  24.267 18.131 1.00 31.91 ? 279 HOH A O   1 
HETATM 1279 O  O   . HOH O 6 .   ? 15.729 34.198 38.024 1.00 31.95 ? 280 HOH A O   1 
HETATM 1280 O  O   . HOH O 6 .   ? 27.020 25.969 11.804 1.00 32.03 ? 281 HOH A O   1 
HETATM 1281 O  O   . HOH O 6 .   ? 22.889 23.553 21.486 1.00 32.12 ? 282 HOH A O   1 
HETATM 1282 O  O   . HOH O 6 .   ? 8.918  30.503 19.024 1.00 32.13 ? 283 HOH A O   1 
HETATM 1283 O  O   . HOH O 6 .   ? 24.691 21.899 25.298 1.00 32.19 ? 284 HOH A O   1 
HETATM 1284 O  O   . HOH O 6 .   ? 16.465 17.703 46.458 1.00 32.29 ? 285 HOH A O   1 
HETATM 1285 O  O   . HOH O 6 .   ? 19.463 13.347 12.324 1.00 32.53 ? 286 HOH A O   1 
HETATM 1286 O  O   . HOH O 6 .   ? 14.226 17.336 13.252 1.00 32.64 ? 287 HOH A O   1 
HETATM 1287 O  O   . HOH O 6 .   ? 22.049 29.241 21.289 1.00 32.85 ? 288 HOH A O   1 
HETATM 1288 O  O   . HOH O 6 .   ? 5.572  2.797  31.674 1.00 32.91 ? 289 HOH A O   1 
HETATM 1289 O  O   . HOH O 6 .   ? 2.749  14.192 27.111 1.00 33.00 ? 290 HOH A O   1 
HETATM 1290 O  O   . HOH O 6 .   ? 4.749  6.254  38.006 1.00 33.00 ? 291 HOH A O   1 
HETATM 1291 O  O   . HOH O 6 .   ? 16.649 10.081 20.589 1.00 33.01 ? 292 HOH A O   1 
HETATM 1292 O  O   . HOH O 6 .   ? 0.031  4.676  33.892 1.00 33.03 ? 293 HOH A O   1 
HETATM 1293 O  O   . HOH O 6 .   ? 21.023 23.092 38.386 1.00 33.05 ? 294 HOH A O   1 
HETATM 1294 O  O   . HOH O 6 .   ? 25.803 7.210  28.985 1.00 33.07 ? 295 HOH A O   1 
HETATM 1295 O  O   . HOH O 6 .   ? 5.715  17.345 21.080 1.00 33.25 ? 296 HOH A O   1 
HETATM 1296 O  O   . HOH O 6 .   ? 11.232 -0.373 32.359 1.00 33.40 ? 297 HOH A O   1 
HETATM 1297 O  O   . HOH O 6 .   ? 25.355 26.480 31.165 1.00 33.46 ? 298 HOH A O   1 
HETATM 1298 O  O   . HOH O 6 .   ? 15.001 33.311 16.269 1.00 33.95 ? 299 HOH A O   1 
HETATM 1299 O  O   . HOH O 6 .   ? 17.245 29.347 28.885 1.00 34.00 ? 300 HOH A O   1 
HETATM 1300 O  O   . HOH O 6 .   ? 13.744 10.211 20.546 1.00 34.07 ? 301 HOH A O   1 
HETATM 1301 O  O   . HOH O 6 .   ? 5.020  9.922  25.613 1.00 34.52 ? 302 HOH A O   1 
HETATM 1302 O  O   . HOH O 6 .   ? 13.496 36.323 31.418 1.00 35.00 ? 303 HOH A O   1 
HETATM 1303 O  O   . HOH O 6 .   ? 7.248  6.254  37.246 1.00 35.00 ? 304 HOH A O   1 
HETATM 1304 O  O   . HOH O 6 .   ? -2.999 31.031 41.807 1.00 35.00 ? 305 HOH A O   1 
HETATM 1305 O  O   . HOH O 6 .   ? 28.325 3.805  32.109 1.00 35.51 ? 306 HOH A O   1 
HETATM 1306 O  O   . HOH O 6 .   ? 20.235 28.526 35.746 1.00 35.52 ? 307 HOH A O   1 
HETATM 1307 O  O   . HOH O 6 .   ? -2.537 33.471 31.311 1.00 35.55 ? 308 HOH A O   1 
HETATM 1308 O  O   . HOH O 6 .   ? 22.588 21.909 23.543 1.00 35.75 ? 309 HOH A O   1 
HETATM 1309 O  O   . HOH O 6 .   ? -2.222 35.179 28.788 1.00 35.83 ? 310 HOH A O   1 
HETATM 1310 O  O   . HOH O 6 .   ? -2.109 16.371 32.615 1.00 35.87 ? 311 HOH A O   1 
HETATM 1311 O  O   . HOH O 6 .   ? 15.129 -3.282 30.096 1.00 35.88 ? 312 HOH A O   1 
HETATM 1312 O  O   . HOH O 6 .   ? 11.497 9.863  22.297 1.00 36.00 ? 313 HOH A O   1 
HETATM 1313 O  O   . HOH O 6 .   ? 15.093 1.308  40.564 1.00 36.59 ? 314 HOH A O   1 
HETATM 1314 O  O   . HOH O 6 .   ? 3.815  22.274 18.516 1.00 36.59 ? 315 HOH A O   1 
HETATM 1315 O  O   . HOH O 6 .   ? 19.964 29.645 28.480 1.00 36.75 ? 316 HOH A O   1 
HETATM 1316 O  O   . HOH O 6 .   ? 17.995 25.201 44.435 1.00 36.76 ? 317 HOH A O   1 
HETATM 1317 O  O   . HOH O 6 .   ? 11.927 7.229  22.432 1.00 36.82 ? 318 HOH A O   1 
HETATM 1318 O  O   . HOH O 6 .   ? 13.819 -4.845 37.838 1.00 36.88 ? 319 HOH A O   1 
HETATM 1319 O  O   . HOH O 6 .   ? 10.852 25.222 8.368  1.00 36.89 ? 320 HOH A O   1 
HETATM 1320 O  O   . HOH O 6 .   ? 16.419 34.292 29.753 1.00 36.98 ? 321 HOH A O   1 
HETATM 1321 O  O   . HOH O 6 .   ? 23.743 11.306 18.750 1.00 37.00 ? 322 HOH A O   1 
HETATM 1322 O  O   . HOH O 6 .   ? 18.212 27.032 38.985 1.00 37.15 ? 323 HOH A O   1 
HETATM 1323 O  O   . HOH O 6 .   ? 8.520  23.843 47.234 1.00 37.23 ? 324 HOH A O   1 
HETATM 1324 O  O   . HOH O 6 .   ? 6.503  36.523 32.932 1.00 37.71 ? 325 HOH A O   1 
HETATM 1325 O  O   . HOH O 6 .   ? 20.730 26.342 37.814 1.00 37.85 ? 326 HOH A O   1 
HETATM 1326 O  O   . HOH O 6 .   ? 25.993 28.625 31.418 1.00 38.00 ? 327 HOH A O   1 
HETATM 1327 O  O   . HOH O 6 .   ? -8.243 28.313 29.284 1.00 38.41 ? 328 HOH A O   1 
HETATM 1328 O  O   . HOH O 6 .   ? 7.107  23.563 14.759 1.00 38.91 ? 329 HOH A O   1 
HETATM 1329 O  O   . HOH O 6 .   ? 8.591  28.479 43.194 1.00 38.96 ? 330 HOH A O   1 
HETATM 1330 O  O   . HOH O 6 .   ? 22.043 27.085 22.892 1.00 39.00 ? 331 HOH A O   1 
HETATM 1331 O  O   . HOH O 6 .   ? 9.497  11.065 23.310 1.00 39.00 ? 332 HOH A O   1 
HETATM 1332 O  O   . HOH O 6 .   ? 26.742 23.093 34.712 1.00 39.00 ? 333 HOH A O   1 
HETATM 1333 O  O   . HOH O 6 .   ? 1.839  32.782 25.348 1.00 39.38 ? 334 HOH A O   1 
HETATM 1334 O  O   . HOH O 6 .   ? 7.204  25.957 46.031 1.00 39.61 ? 335 HOH A O   1 
HETATM 1335 O  O   . HOH O 6 .   ? -1.532 22.651 23.158 1.00 39.63 ? 336 HOH A O   1 
HETATM 1336 O  O   . HOH O 6 .   ? 8.811  20.893 46.448 1.00 39.73 ? 337 HOH A O   1 
HETATM 1337 O  O   . HOH O 6 .   ? 23.921 30.602 20.918 1.00 39.99 ? 338 HOH A O   1 
HETATM 1338 O  O   . HOH O 6 .   ? 28.818 14.113 32.933 1.00 40.00 ? 339 HOH A O   1 
HETATM 1339 O  O   . HOH O 6 .   ? 20.744 35.361 29.898 1.00 40.00 ? 340 HOH A O   1 
HETATM 1340 O  O   . HOH O 6 .   ? 19.994 28.625 39.527 1.00 40.00 ? 341 HOH A O   1 
HETATM 1341 O  O   . HOH O 6 .   ? 12.746 20.687 46.621 1.00 40.00 ? 342 HOH A O   1 
HETATM 1342 O  O   . HOH O 6 .   ? 25.993 3.849  28.378 1.00 40.00 ? 343 HOH A O   1 
HETATM 1343 O  O   . HOH O 6 .   ? 8.145  36.005 34.236 1.00 40.14 ? 344 HOH A O   1 
HETATM 1344 O  O   . HOH O 6 .   ? 3.599  4.188  29.283 1.00 40.20 ? 345 HOH A O   1 
HETATM 1345 O  O   . HOH O 6 .   ? 13.151 -5.053 35.040 1.00 40.20 ? 346 HOH A O   1 
HETATM 1346 O  O   . HOH O 6 .   ? 16.161 11.566 49.991 1.00 40.22 ? 347 HOH A O   1 
HETATM 1347 O  O   . HOH O 6 .   ? 28.992 13.437 22.620 1.00 40.62 ? 348 HOH A O   1 
HETATM 1348 O  O   . HOH O 6 .   ? 16.864 8.181  17.672 1.00 40.65 ? 349 HOH A O   1 
HETATM 1349 O  O   . HOH O 6 .   ? 5.135  13.989 23.135 1.00 40.80 ? 350 HOH A O   1 
HETATM 1350 O  O   . HOH O 6 .   ? 10.381 6.979  13.739 1.00 40.85 ? 351 HOH A O   1 
HETATM 1351 O  O   . HOH O 6 .   ? -8.454 31.647 25.325 1.00 40.86 ? 352 HOH A O   1 
HETATM 1352 O  O   . HOH O 6 .   ? 22.613 24.968 42.580 1.00 40.99 ? 353 HOH A O   1 
HETATM 1353 O  O   . HOH O 6 .   ? 4.749  8.419  37.500 1.00 41.00 ? 354 HOH A O   1 
HETATM 1354 O  O   . HOH O 6 .   ? 7.498  37.526 30.658 1.00 41.00 ? 355 HOH A O   1 
HETATM 1355 O  O   . HOH O 6 .   ? 12.746 9.622  14.696 1.00 41.00 ? 356 HOH A O   1 
HETATM 1356 O  O   . HOH O 6 .   ? 15.474 13.139 11.321 1.00 41.20 ? 357 HOH A O   1 
HETATM 1357 O  O   . HOH O 6 .   ? 2.442  37.384 32.224 1.00 41.45 ? 358 HOH A O   1 
HETATM 1358 O  O   . HOH O 6 .   ? 11.519 6.962  49.052 1.00 41.76 ? 359 HOH A O   1 
HETATM 1359 O  O   . HOH O 6 .   ? -2.654 19.697 29.755 1.00 41.82 ? 360 HOH A O   1 
HETATM 1360 O  O   . HOH O 6 .   ? 0.516  16.163 28.739 1.00 41.85 ? 361 HOH A O   1 
HETATM 1361 O  O   . HOH O 6 .   ? -0.962 33.632 38.199 1.00 41.86 ? 362 HOH A O   1 
HETATM 1362 O  O   . HOH O 6 .   ? 6.726  26.617 43.317 1.00 41.94 ? 363 HOH A O   1 
HETATM 1363 O  O   . HOH O 6 .   ? 1.500  25.889 40.194 1.00 41.96 ? 364 HOH A O   1 
HETATM 1364 O  O   . HOH O 6 .   ? -1.189 34.134 24.784 1.00 41.98 ? 365 HOH A O   1 
HETATM 1365 O  O   . HOH O 6 .   ? 12.250 33.305 20.681 1.00 41.99 ? 366 HOH A O   1 
HETATM 1366 O  O   . HOH O 6 .   ? -4.999 34.880 29.645 1.00 42.00 ? 367 HOH A O   1 
HETATM 1367 O  O   . HOH O 6 .   ? 7.998  13.952 15.203 1.00 42.00 ? 368 HOH A O   1 
HETATM 1368 O  O   . HOH O 6 .   ? 14.423 34.624 34.561 1.00 42.05 ? 369 HOH A O   1 
HETATM 1369 O  O   . HOH O 6 .   ? 26.704 28.019 16.027 1.00 42.07 ? 370 HOH A O   1 
HETATM 1370 O  O   . HOH O 6 .   ? 3.136  31.000 23.742 1.00 42.39 ? 371 HOH A O   1 
HETATM 1371 O  O   . HOH O 6 .   ? 7.482  3.352  34.627 1.00 42.45 ? 372 HOH A O   1 
HETATM 1372 O  O   . HOH O 6 .   ? 15.203 29.278 40.603 1.00 42.71 ? 373 HOH A O   1 
HETATM 1373 O  O   . HOH O 6 .   ? 20.103 -0.779 38.126 1.00 42.95 ? 374 HOH A O   1 
HETATM 1374 O  O   . HOH O 6 .   ? 10.997 22.131 8.868  1.00 43.00 ? 375 HOH A O   1 
HETATM 1375 O  O   . HOH O 6 .   ? 28.492 6.735  28.885 1.00 43.00 ? 376 HOH A O   1 
HETATM 1376 O  O   . HOH O 6 .   ? 31.725 6.537  34.303 1.00 43.34 ? 377 HOH A O   1 
HETATM 1377 O  O   . HOH O 6 .   ? 18.333 15.165 12.451 1.00 43.55 ? 378 HOH A O   1 
HETATM 1378 O  O   . HOH O 6 .   ? 18.408 9.262  15.863 1.00 43.66 ? 379 HOH A O   1 
HETATM 1379 O  O   . HOH O 6 .   ? 26.030 19.983 19.524 1.00 43.91 ? 380 HOH A O   1 
HETATM 1380 O  O   . HOH O 6 .   ? 28.358 20.782 32.156 1.00 44.03 ? 381 HOH A O   1 
HETATM 1381 O  O   . HOH O 6 .   ? 14.983 21.679 44.975 1.00 44.19 ? 382 HOH A O   1 
HETATM 1382 O  O   . HOH O 6 .   ? 12.186 35.116 35.377 1.00 44.56 ? 383 HOH A O   1 
HETATM 1383 O  O   . HOH O 6 .   ? 12.330 13.731 10.576 1.00 45.13 ? 384 HOH A O   1 
HETATM 1384 O  O   . HOH O 6 .   ? 27.150 8.074  25.870 1.00 45.17 ? 385 HOH A O   1 
HETATM 1385 O  O   . HOH O 6 .   ? 18.622 20.322 45.049 1.00 45.23 ? 386 HOH A O   1 
HETATM 1386 O  O   . HOH O 6 .   ? 12.093 -6.677 38.941 1.00 45.29 ? 387 HOH A O   1 
HETATM 1387 O  O   . HOH O 6 .   ? 17.022 17.328 12.895 1.00 45.33 ? 388 HOH A O   1 
HETATM 1388 O  O   . HOH O 6 .   ? 3.334  11.345 33.484 1.00 45.79 ? 389 HOH A O   1 
HETATM 1389 O  O   . HOH O 6 .   ? 28.742 21.409 26.858 1.00 46.00 ? 390 HOH A O   1 
HETATM 1390 O  O   . HOH O 6 .   ? 14.996 8.900  12.922 1.00 46.00 ? 391 HOH A O   1 
HETATM 1391 O  O   . HOH O 6 .   ? -5.248 34.399 27.365 1.00 46.00 ? 392 HOH A O   1 
HETATM 1392 O  O   . HOH O 6 .   ? 21.244 26.461 43.581 1.00 46.00 ? 393 HOH A O   1 
HETATM 1393 O  O   . HOH O 6 .   ? 11.997 8.660  20.017 1.00 46.00 ? 394 HOH A O   1 
HETATM 1394 O  O   . HOH O 6 .   ? 27.742 15.395 16.976 1.00 46.00 ? 395 HOH A O   1 
HETATM 1395 O  O   . HOH O 6 .   ? 28.678 8.642  27.678 1.00 46.39 ? 396 HOH A O   1 
HETATM 1396 O  O   . HOH O 6 .   ? 8.539  22.382 9.049  1.00 46.48 ? 397 HOH A O   1 
HETATM 1397 O  O   . HOH O 6 .   ? 22.655 30.989 29.631 1.00 46.57 ? 398 HOH A O   1 
HETATM 1398 O  O   . HOH O 6 .   ? 18.595 35.602 40.400 1.00 46.66 ? 399 HOH A O   1 
HETATM 1399 O  O   . HOH O 6 .   ? 8.082  35.178 20.872 1.00 46.87 ? 400 HOH A O   1 
HETATM 1400 O  O   . HOH O 6 .   ? 28.459 15.879 29.665 1.00 46.99 ? 401 HOH A O   1 
HETATM 1401 O  O   . HOH O 6 .   ? 13.496 27.663 44.847 1.00 47.00 ? 402 HOH A O   1 
HETATM 1402 O  O   . HOH O 6 .   ? 5.248  7.216  26.098 1.00 47.00 ? 403 HOH A O   1 
HETATM 1403 O  O   . HOH O 6 .   ? 21.755 22.816 44.314 1.00 47.03 ? 404 HOH A O   1 
HETATM 1404 O  O   . HOH O 6 .   ? 20.760 31.344 22.742 1.00 47.27 ? 405 HOH A O   1 
HETATM 1405 O  O   . HOH O 6 .   ? 8.312  36.905 22.616 1.00 47.79 ? 406 HOH A O   1 
HETATM 1406 O  O   . HOH O 6 .   ? 19.842 17.534 9.399  1.00 47.86 ? 407 HOH A O   1 
HETATM 1407 O  O   . HOH O 6 .   ? -1.106 24.813 40.494 1.00 47.97 ? 408 HOH A O   1 
HETATM 1408 O  O   . HOH O 6 .   ? 19.128 12.747 51.822 1.00 47.97 ? 409 HOH A O   1 
HETATM 1409 O  O   . HOH O 6 .   ? 2.101  20.283 22.476 1.00 48.47 ? 410 HOH A O   1 
HETATM 1410 O  O   . HOH O 6 .   ? 25.440 23.319 21.335 1.00 49.13 ? 411 HOH A O   1 
HETATM 1411 O  O   . HOH O 6 .   ? 21.729 30.178 36.399 1.00 49.17 ? 412 HOH A O   1 
HETATM 1412 O  O   . HOH O 6 .   ? 8.619  20.155 9.048  1.00 49.58 ? 413 HOH A O   1 
HETATM 1413 O  O   . HOH O 6 .   ? 20.351 15.175 48.854 1.00 49.92 ? 414 HOH A O   1 
HETATM 1414 O  O   . HOH O 6 .   ? 17.305 34.395 32.050 1.00 50.42 ? 415 HOH A O   1 
HETATM 1415 O  O   . HOH O 6 .   ? 14.788 -2.339 32.630 1.00 50.46 ? 416 HOH A O   1 
HETATM 1416 O  O   . HOH O 6 .   ? 6.132  37.800 25.813 1.00 50.47 ? 417 HOH A O   1 
HETATM 1417 O  O   . HOH O 6 .   ? 27.406 30.015 17.416 1.00 50.81 ? 418 HOH A O   1 
HETATM 1418 O  O   . HOH O 6 .   ? 26.920 2.883  30.516 1.00 51.07 ? 419 HOH A O   1 
HETATM 1419 O  O   . HOH O 6 .   ? 2.495  33.174 40.705 1.00 51.23 ? 420 HOH A O   1 
HETATM 1420 O  O   . HOH O 6 .   ? 29.585 4.348  30.383 1.00 52.05 ? 421 HOH A O   1 
HETATM 1421 O  O   . HOH O 6 .   ? 11.648 -4.169 33.784 1.00 52.16 ? 422 HOH A O   1 
HETATM 1422 O  O   . HOH O 6 .   ? 0.017  19.363 26.823 1.00 52.17 ? 423 HOH A O   1 
HETATM 1423 O  O   . HOH O 6 .   ? 23.200 29.056 25.411 1.00 52.24 ? 424 HOH A O   1 
HETATM 1424 O  O   . HOH O 6 .   ? 4.141  26.763 42.894 1.00 52.26 ? 425 HOH A O   1 
HETATM 1425 O  O   . HOH O 6 .   ? -1.089 34.391 35.227 1.00 53.29 ? 426 HOH A O   1 
HETATM 1426 O  O   . HOH O 6 .   ? 21.931 22.729 12.565 1.00 53.32 ? 427 HOH A O   1 
HETATM 1427 O  O   . HOH O 6 .   ? 9.504  7.087  23.996 1.00 53.73 ? 428 HOH A O   1 
HETATM 1428 O  O   . HOH O 6 .   ? 6.754  7.757  24.574 1.00 53.93 ? 429 HOH A O   1 
HETATM 1429 O  O   . HOH O 6 .   ? 24.962 14.407 33.044 1.00 54.22 ? 430 HOH A O   1 
HETATM 1430 O  O   . HOH O 6 .   ? 22.971 23.599 14.589 1.00 55.85 ? 431 HOH A O   1 
HETATM 1431 O  O   . HOH O 6 .   ? 27.384 18.877 24.309 1.00 56.20 ? 432 HOH A O   1 
HETATM 1432 O  O   . HOH O 6 .   ? 13.143 -5.294 32.802 1.00 56.59 ? 433 HOH A O   1 
HETATM 1433 O  O   . HOH O 6 .   ? 24.859 23.617 48.125 1.00 57.36 ? 434 HOH A O   1 
HETATM 1434 O  O   . HOH O 6 .   ? 11.011 -3.999 38.006 1.00 57.45 ? 435 HOH A O   1 
HETATM 1435 O  O   . HOH O 6 .   ? 6.210  18.762 27.433 1.00 57.62 ? 436 HOH A O   1 
HETATM 1436 O  O   . HOH O 6 .   ? 12.609 6.626  13.352 1.00 59.26 ? 437 HOH A O   1 
HETATM 1437 O  O   . HOH O 6 .   ? 9.031  26.190 47.415 1.00 60.40 ? 438 HOH A O   1 
HETATM 1438 O  O   . HOH O 6 .   ? -4.028 27.303 25.644 1.00 60.51 ? 439 HOH A O   1 
HETATM 1439 O  O   . HOH O 6 .   ? 12.927 9.839  11.682 1.00 60.79 ? 440 HOH A O   1 
HETATM 1440 O  O   . HOH O 6 .   ? -3.125 25.516 22.723 1.00 61.85 ? 441 HOH A O   1 
HETATM 1441 O  O   . HOH O 6 .   ? -4.696 33.782 36.687 1.00 62.69 ? 442 HOH A O   1 
HETATM 1442 O  O   . HOH O 6 .   ? 10.028 38.388 30.119 1.00 64.23 ? 443 HOH A O   1 
HETATM 1443 O  O   . HOH O 6 .   ? 6.913  32.148 19.093 1.00 67.54 ? 444 HOH A O   1 
HETATM 1444 O  O   . HOH O 6 .   ? 1.808  35.339 24.711 1.00 67.72 ? 445 HOH A O   1 
HETATM 1445 O  O   . HOH O 6 .   ? 2.559  16.644 25.520 1.00 68.19 ? 446 HOH A O   1 
HETATM 1446 O  O   . HOH O 6 .   ? 22.676 22.177 16.563 1.00 69.90 ? 447 HOH A O   1 
HETATM 1447 O  O   . HOH O 6 .   ? -5.576 19.127 30.315 1.00 73.39 ? 448 HOH A O   1 
HETATM 1448 O  O   . HOH O 6 .   ? 13.847 37.862 41.791 1.00 78.94 ? 449 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   ALA 1   1   1   ALA ALA A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  GLU 50  50  50  GLU GLU A . n 
A 1 51  GLU 51  51  51  GLU GLU A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  CYS 57  57  57  CYS CYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLN 133 133 133 GLN GLN A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
# 
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 ZN  1   154 154 ZN  ZN  A . 
C 3 CU  1   155 155 CU  CU  A . 
D 4 CD  1   156 156 CD  CAD A . 
E 4 CD  1   157 157 CD  CAD A . 
F 4 CD  1   158 158 CD  CAD A . 
G 4 CD  1   159 159 CD  CAD A . 
H 4 CD  1   160 160 CD  CAD A . 
I 4 CD  1   161 161 CD  CAD A . 
J 4 CD  1   162 162 CD  CAD A . 
K 4 CD  1   163 163 CD  CAD A . 
L 4 CD  1   164 164 CD  CAD A . 
M 5 CL  1   165 165 CL  CL  A . 
N 5 CL  1   166 166 CL  CL  A . 
O 6 HOH 1   167 1   HOH HOH A . 
O 6 HOH 2   168 2   HOH HOH A . 
O 6 HOH 3   169 3   HOH HOH A . 
O 6 HOH 4   170 4   HOH HOH A . 
O 6 HOH 5   171 5   HOH HOH A . 
O 6 HOH 6   172 6   HOH HOH A . 
O 6 HOH 7   173 7   HOH HOH A . 
O 6 HOH 8   174 8   HOH HOH A . 
O 6 HOH 9   175 9   HOH HOH A . 
O 6 HOH 10  176 10  HOH HOH A . 
O 6 HOH 11  177 11  HOH HOH A . 
O 6 HOH 12  178 12  HOH HOH A . 
O 6 HOH 13  179 13  HOH HOH A . 
O 6 HOH 14  180 14  HOH HOH A . 
O 6 HOH 15  181 15  HOH HOH A . 
O 6 HOH 16  182 16  HOH HOH A . 
O 6 HOH 17  183 17  HOH HOH A . 
O 6 HOH 18  184 18  HOH HOH A . 
O 6 HOH 19  185 19  HOH HOH A . 
O 6 HOH 20  186 20  HOH HOH A . 
O 6 HOH 21  187 21  HOH HOH A . 
O 6 HOH 22  188 22  HOH HOH A . 
O 6 HOH 23  189 23  HOH HOH A . 
O 6 HOH 24  190 24  HOH HOH A . 
O 6 HOH 25  191 25  HOH HOH A . 
O 6 HOH 26  192 26  HOH HOH A . 
O 6 HOH 27  193 27  HOH HOH A . 
O 6 HOH 28  194 28  HOH HOH A . 
O 6 HOH 29  195 29  HOH HOH A . 
O 6 HOH 30  196 30  HOH HOH A . 
O 6 HOH 31  197 31  HOH HOH A . 
O 6 HOH 32  198 32  HOH HOH A . 
O 6 HOH 33  199 33  HOH HOH A . 
O 6 HOH 34  200 34  HOH HOH A . 
O 6 HOH 35  201 35  HOH HOH A . 
O 6 HOH 36  202 36  HOH HOH A . 
O 6 HOH 37  203 37  HOH HOH A . 
O 6 HOH 38  204 38  HOH HOH A . 
O 6 HOH 39  205 39  HOH HOH A . 
O 6 HOH 40  206 40  HOH HOH A . 
O 6 HOH 41  207 41  HOH HOH A . 
O 6 HOH 42  208 42  HOH HOH A . 
O 6 HOH 43  209 43  HOH HOH A . 
O 6 HOH 44  210 44  HOH HOH A . 
O 6 HOH 45  211 45  HOH HOH A . 
O 6 HOH 46  212 46  HOH HOH A . 
O 6 HOH 47  213 47  HOH HOH A . 
O 6 HOH 48  214 48  HOH HOH A . 
O 6 HOH 49  215 49  HOH HOH A . 
O 6 HOH 50  216 50  HOH HOH A . 
O 6 HOH 51  217 51  HOH HOH A . 
O 6 HOH 52  218 52  HOH HOH A . 
O 6 HOH 53  219 53  HOH HOH A . 
O 6 HOH 54  220 54  HOH HOH A . 
O 6 HOH 55  221 55  HOH HOH A . 
O 6 HOH 56  222 56  HOH HOH A . 
O 6 HOH 57  223 57  HOH HOH A . 
O 6 HOH 58  224 58  HOH HOH A . 
O 6 HOH 59  225 59  HOH HOH A . 
O 6 HOH 60  226 60  HOH HOH A . 
O 6 HOH 61  227 61  HOH HOH A . 
O 6 HOH 62  228 62  HOH HOH A . 
O 6 HOH 63  229 63  HOH HOH A . 
O 6 HOH 64  230 65  HOH HOH A . 
O 6 HOH 65  231 66  HOH HOH A . 
O 6 HOH 66  232 67  HOH HOH A . 
O 6 HOH 67  233 68  HOH HOH A . 
O 6 HOH 68  234 69  HOH HOH A . 
O 6 HOH 69  235 70  HOH HOH A . 
O 6 HOH 70  236 71  HOH HOH A . 
O 6 HOH 71  237 72  HOH HOH A . 
O 6 HOH 72  238 73  HOH HOH A . 
O 6 HOH 73  239 74  HOH HOH A . 
O 6 HOH 74  240 75  HOH HOH A . 
O 6 HOH 75  241 76  HOH HOH A . 
O 6 HOH 76  242 77  HOH HOH A . 
O 6 HOH 77  243 78  HOH HOH A . 
O 6 HOH 78  244 79  HOH HOH A . 
O 6 HOH 79  245 80  HOH HOH A . 
O 6 HOH 80  246 81  HOH HOH A . 
O 6 HOH 81  247 82  HOH HOH A . 
O 6 HOH 82  248 83  HOH HOH A . 
O 6 HOH 83  249 84  HOH HOH A . 
O 6 HOH 84  250 85  HOH HOH A . 
O 6 HOH 85  251 86  HOH HOH A . 
O 6 HOH 86  252 87  HOH HOH A . 
O 6 HOH 87  253 88  HOH HOH A . 
O 6 HOH 88  254 89  HOH HOH A . 
O 6 HOH 89  255 90  HOH HOH A . 
O 6 HOH 90  256 91  HOH HOH A . 
O 6 HOH 91  257 92  HOH HOH A . 
O 6 HOH 92  258 93  HOH HOH A . 
O 6 HOH 93  259 94  HOH HOH A . 
O 6 HOH 94  260 95  HOH HOH A . 
O 6 HOH 95  261 96  HOH HOH A . 
O 6 HOH 96  262 97  HOH HOH A . 
O 6 HOH 97  263 98  HOH HOH A . 
O 6 HOH 98  264 99  HOH HOH A . 
O 6 HOH 99  265 100 HOH HOH A . 
O 6 HOH 100 266 101 HOH HOH A . 
O 6 HOH 101 267 102 HOH HOH A . 
O 6 HOH 102 268 103 HOH HOH A . 
O 6 HOH 103 269 104 HOH HOH A . 
O 6 HOH 104 270 105 HOH HOH A . 
O 6 HOH 105 271 106 HOH HOH A . 
O 6 HOH 106 272 107 HOH HOH A . 
O 6 HOH 107 273 108 HOH HOH A . 
O 6 HOH 108 274 109 HOH HOH A . 
O 6 HOH 109 275 110 HOH HOH A . 
O 6 HOH 110 276 111 HOH HOH A . 
O 6 HOH 111 277 112 HOH HOH A . 
O 6 HOH 112 278 113 HOH HOH A . 
O 6 HOH 113 279 114 HOH HOH A . 
O 6 HOH 114 280 115 HOH HOH A . 
O 6 HOH 115 281 116 HOH HOH A . 
O 6 HOH 116 282 117 HOH HOH A . 
O 6 HOH 117 283 118 HOH HOH A . 
O 6 HOH 118 284 119 HOH HOH A . 
O 6 HOH 119 285 120 HOH HOH A . 
O 6 HOH 120 286 121 HOH HOH A . 
O 6 HOH 121 287 122 HOH HOH A . 
O 6 HOH 122 288 123 HOH HOH A . 
O 6 HOH 123 289 124 HOH HOH A . 
O 6 HOH 124 290 125 HOH HOH A . 
O 6 HOH 125 291 126 HOH HOH A . 
O 6 HOH 126 292 127 HOH HOH A . 
O 6 HOH 127 293 128 HOH HOH A . 
O 6 HOH 128 294 129 HOH HOH A . 
O 6 HOH 129 295 130 HOH HOH A . 
O 6 HOH 130 296 131 HOH HOH A . 
O 6 HOH 131 297 132 HOH HOH A . 
O 6 HOH 132 298 133 HOH HOH A . 
O 6 HOH 133 299 134 HOH HOH A . 
O 6 HOH 134 300 135 HOH HOH A . 
O 6 HOH 135 301 136 HOH HOH A . 
O 6 HOH 136 302 137 HOH HOH A . 
O 6 HOH 137 303 138 HOH HOH A . 
O 6 HOH 138 304 139 HOH HOH A . 
O 6 HOH 139 305 140 HOH HOH A . 
O 6 HOH 140 306 141 HOH HOH A . 
O 6 HOH 141 307 142 HOH HOH A . 
O 6 HOH 142 308 143 HOH HOH A . 
O 6 HOH 143 309 144 HOH HOH A . 
O 6 HOH 144 310 145 HOH HOH A . 
O 6 HOH 145 311 146 HOH HOH A . 
O 6 HOH 146 312 147 HOH HOH A . 
O 6 HOH 147 313 148 HOH HOH A . 
O 6 HOH 148 314 149 HOH HOH A . 
O 6 HOH 149 315 150 HOH HOH A . 
O 6 HOH 150 316 151 HOH HOH A . 
O 6 HOH 151 317 152 HOH HOH A . 
O 6 HOH 152 318 153 HOH HOH A . 
O 6 HOH 153 319 154 HOH HOH A . 
O 6 HOH 154 320 155 HOH HOH A . 
O 6 HOH 155 321 156 HOH HOH A . 
O 6 HOH 156 322 157 HOH HOH A . 
O 6 HOH 157 323 158 HOH HOH A . 
O 6 HOH 158 324 159 HOH HOH A . 
O 6 HOH 159 325 160 HOH HOH A . 
O 6 HOH 160 326 161 HOH HOH A . 
O 6 HOH 161 327 162 HOH HOH A . 
O 6 HOH 162 328 163 HOH HOH A . 
O 6 HOH 163 329 164 HOH HOH A . 
O 6 HOH 164 330 165 HOH HOH A . 
O 6 HOH 165 331 166 HOH HOH A . 
O 6 HOH 166 332 167 HOH HOH A . 
O 6 HOH 167 333 168 HOH HOH A . 
O 6 HOH 168 334 169 HOH HOH A . 
O 6 HOH 169 335 170 HOH HOH A . 
O 6 HOH 170 336 171 HOH HOH A . 
O 6 HOH 171 337 172 HOH HOH A . 
O 6 HOH 172 338 173 HOH HOH A . 
O 6 HOH 173 339 174 HOH HOH A . 
O 6 HOH 174 340 175 HOH HOH A . 
O 6 HOH 175 341 176 HOH HOH A . 
O 6 HOH 176 342 177 HOH HOH A . 
O 6 HOH 177 343 178 HOH HOH A . 
O 6 HOH 178 344 179 HOH HOH A . 
O 6 HOH 179 345 180 HOH HOH A . 
O 6 HOH 180 346 181 HOH HOH A . 
O 6 HOH 181 347 182 HOH HOH A . 
O 6 HOH 182 348 183 HOH HOH A . 
O 6 HOH 183 349 184 HOH HOH A . 
O 6 HOH 184 350 185 HOH HOH A . 
O 6 HOH 185 351 186 HOH HOH A . 
O 6 HOH 186 352 187 HOH HOH A . 
O 6 HOH 187 353 188 HOH HOH A . 
O 6 HOH 188 354 189 HOH HOH A . 
O 6 HOH 189 355 190 HOH HOH A . 
O 6 HOH 190 356 191 HOH HOH A . 
O 6 HOH 191 357 192 HOH HOH A . 
O 6 HOH 192 358 193 HOH HOH A . 
O 6 HOH 193 359 194 HOH HOH A . 
O 6 HOH 194 360 195 HOH HOH A . 
O 6 HOH 195 361 196 HOH HOH A . 
O 6 HOH 196 362 197 HOH HOH A . 
O 6 HOH 197 363 198 HOH HOH A . 
O 6 HOH 198 364 199 HOH HOH A . 
O 6 HOH 199 365 200 HOH HOH A . 
O 6 HOH 200 366 201 HOH HOH A . 
O 6 HOH 201 367 202 HOH HOH A . 
O 6 HOH 202 368 203 HOH HOH A . 
O 6 HOH 203 369 204 HOH HOH A . 
O 6 HOH 204 370 205 HOH HOH A . 
O 6 HOH 205 371 206 HOH HOH A . 
O 6 HOH 206 372 207 HOH HOH A . 
O 6 HOH 207 373 208 HOH HOH A . 
O 6 HOH 208 374 209 HOH HOH A . 
O 6 HOH 209 375 210 HOH HOH A . 
O 6 HOH 210 376 211 HOH HOH A . 
O 6 HOH 211 377 212 HOH HOH A . 
O 6 HOH 212 378 213 HOH HOH A . 
O 6 HOH 213 379 214 HOH HOH A . 
O 6 HOH 214 380 215 HOH HOH A . 
O 6 HOH 215 381 216 HOH HOH A . 
O 6 HOH 216 382 217 HOH HOH A . 
O 6 HOH 217 383 218 HOH HOH A . 
O 6 HOH 218 384 219 HOH HOH A . 
O 6 HOH 219 385 220 HOH HOH A . 
O 6 HOH 220 386 221 HOH HOH A . 
O 6 HOH 221 387 222 HOH HOH A . 
O 6 HOH 222 388 223 HOH HOH A . 
O 6 HOH 223 389 224 HOH HOH A . 
O 6 HOH 224 390 225 HOH HOH A . 
O 6 HOH 225 391 226 HOH HOH A . 
O 6 HOH 226 392 227 HOH HOH A . 
O 6 HOH 227 393 228 HOH HOH A . 
O 6 HOH 228 394 229 HOH HOH A . 
O 6 HOH 229 395 230 HOH HOH A . 
O 6 HOH 230 396 231 HOH HOH A . 
O 6 HOH 231 397 232 HOH HOH A . 
O 6 HOH 232 398 233 HOH HOH A . 
O 6 HOH 233 399 234 HOH HOH A . 
O 6 HOH 234 400 235 HOH HOH A . 
O 6 HOH 235 401 236 HOH HOH A . 
O 6 HOH 236 402 237 HOH HOH A . 
O 6 HOH 237 403 238 HOH HOH A . 
O 6 HOH 238 404 239 HOH HOH A . 
O 6 HOH 239 405 240 HOH HOH A . 
O 6 HOH 240 406 241 HOH HOH A . 
O 6 HOH 241 407 242 HOH HOH A . 
O 6 HOH 242 408 243 HOH HOH A . 
O 6 HOH 243 409 244 HOH HOH A . 
O 6 HOH 244 410 245 HOH HOH A . 
O 6 HOH 245 411 246 HOH HOH A . 
O 6 HOH 246 412 247 HOH HOH A . 
O 6 HOH 247 413 248 HOH HOH A . 
O 6 HOH 248 414 249 HOH HOH A . 
O 6 HOH 249 415 250 HOH HOH A . 
O 6 HOH 250 416 251 HOH HOH A . 
O 6 HOH 251 417 252 HOH HOH A . 
O 6 HOH 252 418 253 HOH HOH A . 
O 6 HOH 253 419 254 HOH HOH A . 
O 6 HOH 254 420 255 HOH HOH A . 
O 6 HOH 255 421 256 HOH HOH A . 
O 6 HOH 256 422 257 HOH HOH A . 
O 6 HOH 257 423 258 HOH HOH A . 
O 6 HOH 258 424 259 HOH HOH A . 
O 6 HOH 259 425 260 HOH HOH A . 
O 6 HOH 260 426 261 HOH HOH A . 
O 6 HOH 261 427 262 HOH HOH A . 
O 6 HOH 262 428 263 HOH HOH A . 
O 6 HOH 263 429 264 HOH HOH A . 
O 6 HOH 264 430 265 HOH HOH A . 
O 6 HOH 265 431 266 HOH HOH A . 
O 6 HOH 266 432 267 HOH HOH A . 
O 6 HOH 267 433 268 HOH HOH A . 
O 6 HOH 268 434 269 HOH HOH A . 
O 6 HOH 269 435 270 HOH HOH A . 
O 6 HOH 270 436 271 HOH HOH A . 
O 6 HOH 271 437 272 HOH HOH A . 
O 6 HOH 272 438 273 HOH HOH A . 
O 6 HOH 273 439 274 HOH HOH A . 
O 6 HOH 274 440 275 HOH HOH A . 
O 6 HOH 275 441 276 HOH HOH A . 
O 6 HOH 276 442 277 HOH HOH A . 
O 6 HOH 277 443 278 HOH HOH A . 
O 6 HOH 278 444 279 HOH HOH A . 
O 6 HOH 279 445 280 HOH HOH A . 
O 6 HOH 280 446 281 HOH HOH A . 
O 6 HOH 281 447 282 HOH HOH A . 
O 6 HOH 282 448 283 HOH HOH A . 
O 6 HOH 283 449 284 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   monomeric 
_pdbx_struct_assembly.oligomeric_count     1 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1   O   ? A ALA 1   ? A ALA 1   ? 4_556 CD ? D CD . ? A CD 156 ? 1_555 N   ? A ALA 1   ? A ALA 1   ? 4_556 69.7  ? 
2   O   ? A ALA 1   ? A ALA 1   ? 4_556 CD ? D CD . ? A CD 156 ? 1_555 OE2 A A GLU 51  ? A GLU 51  ? 1_555 80.3  ? 
3   N   ? A ALA 1   ? A ALA 1   ? 4_556 CD ? D CD . ? A CD 156 ? 1_555 OE2 A A GLU 51  ? A GLU 51  ? 1_555 116.1 ? 
4   O   ? A ALA 1   ? A ALA 1   ? 4_556 CD ? D CD . ? A CD 156 ? 1_555 OE2 B A GLU 51  ? A GLU 51  ? 1_555 89.7  ? 
5   N   ? A ALA 1   ? A ALA 1   ? 4_556 CD ? D CD . ? A CD 156 ? 1_555 OE2 B A GLU 51  ? A GLU 51  ? 1_555 113.5 ? 
6   OE2 A A GLU 51  ? A GLU 51  ? 1_555 CD ? D CD . ? A CD 156 ? 1_555 OE2 B A GLU 51  ? A GLU 51  ? 1_555 11.9  ? 
7   O   ? A ALA 1   ? A ALA 1   ? 4_556 CD ? D CD . ? A CD 156 ? 1_555 OD2 ? A ASP 96  ? A ASP 96  ? 1_655 86.4  ? 
8   N   ? A ALA 1   ? A ALA 1   ? 4_556 CD ? D CD . ? A CD 156 ? 1_555 OD2 ? A ASP 96  ? A ASP 96  ? 1_655 146.9 ? 
9   OE2 A A GLU 51  ? A GLU 51  ? 1_555 CD ? D CD . ? A CD 156 ? 1_555 OD2 ? A ASP 96  ? A ASP 96  ? 1_655 80.1  ? 
10  OE2 B A GLU 51  ? A GLU 51  ? 1_555 CD ? D CD . ? A CD 156 ? 1_555 OD2 ? A ASP 96  ? A ASP 96  ? 1_655 88.0  ? 
11  O   ? A ALA 1   ? A ALA 1   ? 4_556 CD ? D CD . ? A CD 156 ? 1_555 OD1 ? A ASP 96  ? A ASP 96  ? 1_655 81.4  ? 
12  N   ? A ALA 1   ? A ALA 1   ? 4_556 CD ? D CD . ? A CD 156 ? 1_555 OD1 ? A ASP 96  ? A ASP 96  ? 1_655 99.8  ? 
13  OE2 A A GLU 51  ? A GLU 51  ? 1_555 CD ? D CD . ? A CD 156 ? 1_555 OD1 ? A ASP 96  ? A ASP 96  ? 1_655 130.2 ? 
14  OE2 B A GLU 51  ? A GLU 51  ? 1_555 CD ? D CD . ? A CD 156 ? 1_555 OD1 ? A ASP 96  ? A ASP 96  ? 1_655 140.0 ? 
15  OD2 ? A ASP 96  ? A ASP 96  ? 1_655 CD ? D CD . ? A CD 156 ? 1_555 OD1 ? A ASP 96  ? A ASP 96  ? 1_655 52.7  ? 
16  O   ? A ALA 1   ? A ALA 1   ? 4_556 CD ? D CD . ? A CD 156 ? 1_555 O   ? O HOH .   ? A HOH 178 ? 1_555 168.8 ? 
17  N   ? A ALA 1   ? A ALA 1   ? 4_556 CD ? D CD . ? A CD 156 ? 1_555 O   ? O HOH .   ? A HOH 178 ? 1_555 105.9 ? 
18  OE2 A A GLU 51  ? A GLU 51  ? 1_555 CD ? D CD . ? A CD 156 ? 1_555 O   ? O HOH .   ? A HOH 178 ? 1_555 110.6 ? 
19  OE2 B A GLU 51  ? A GLU 51  ? 1_555 CD ? D CD . ? A CD 156 ? 1_555 O   ? O HOH .   ? A HOH 178 ? 1_555 101.5 ? 
20  OD2 ? A ASP 96  ? A ASP 96  ? 1_655 CD ? D CD . ? A CD 156 ? 1_555 O   ? O HOH .   ? A HOH 178 ? 1_555 93.2  ? 
21  OD1 ? A ASP 96  ? A ASP 96  ? 1_655 CD ? D CD . ? A CD 156 ? 1_555 O   ? O HOH .   ? A HOH 178 ? 1_555 89.4  ? 
22  OE1 A A GLU 24  ? A GLU 24  ? 1_555 CD ? H CD . ? A CD 160 ? 1_555 OE2 A A GLU 24  ? A GLU 24  ? 1_555 55.2  ? 
23  OE1 A A GLU 24  ? A GLU 24  ? 1_555 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 179 ? 1_555 152.7 ? 
24  OE2 A A GLU 24  ? A GLU 24  ? 1_555 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 179 ? 1_555 97.6  ? 
25  OE1 A A GLU 24  ? A GLU 24  ? 1_555 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 200 ? 4_556 96.5  ? 
26  OE2 A A GLU 24  ? A GLU 24  ? 1_555 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 200 ? 4_556 151.3 ? 
27  O   ? O HOH .   ? A HOH 179 ? 1_555 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 200 ? 4_556 110.8 ? 
28  OE1 A A GLU 24  ? A GLU 24  ? 1_555 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 228 ? 4_456 86.5  ? 
29  OE2 A A GLU 24  ? A GLU 24  ? 1_555 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 228 ? 4_456 78.7  ? 
30  O   ? O HOH .   ? A HOH 179 ? 1_555 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 228 ? 4_456 89.9  ? 
31  O   ? O HOH .   ? A HOH 200 ? 4_556 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 228 ? 4_456 96.7  ? 
32  OE1 A A GLU 24  ? A GLU 24  ? 1_555 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 319 ? 1_555 86.0  ? 
33  OE2 A A GLU 24  ? A GLU 24  ? 1_555 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 319 ? 1_555 88.1  ? 
34  O   ? O HOH .   ? A HOH 179 ? 1_555 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 319 ? 1_555 91.8  ? 
35  O   ? O HOH .   ? A HOH 200 ? 4_556 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 319 ? 1_555 94.9  ? 
36  O   ? O HOH .   ? A HOH 228 ? 4_456 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 319 ? 1_555 166.8 ? 
37  OE1 A A GLU 24  ? A GLU 24  ? 1_555 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 435 ? 1_555 103.1 ? 
38  OE2 A A GLU 24  ? A GLU 24  ? 1_555 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 435 ? 1_555 51.2  ? 
39  O   ? O HOH .   ? A HOH 179 ? 1_555 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 435 ? 1_555 50.6  ? 
40  O   ? O HOH .   ? A HOH 200 ? 4_556 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 435 ? 1_555 156.0 ? 
41  O   ? O HOH .   ? A HOH 228 ? 4_456 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 435 ? 1_555 98.2  ? 
42  O   ? O HOH .   ? A HOH 319 ? 1_555 CD ? H CD . ? A CD 160 ? 1_555 O   ? O HOH .   ? A HOH 435 ? 1_555 73.1  ? 
43  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 CU ? C CU . ? A CU 155 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 144.6 ? 
44  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 CU ? C CU . ? A CU 155 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 103.2 ? 
45  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 CU ? C CU . ? A CU 155 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 104.2 ? 
46  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 CU ? C CU . ? A CU 155 ? 1_555 CD  ? L CD  .   ? A CD  164 ? 1_555 86.9  ? 
47  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 CU ? C CU . ? A CU 155 ? 1_555 CD  ? L CD  .   ? A CD  164 ? 1_555 81.1  ? 
48  NE2 ? A HIS 120 ? A HIS 120 ? 1_555 CU ? C CU . ? A CU 155 ? 1_555 CD  ? L CD  .   ? A CD  164 ? 1_555 71.4  ? 
49  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 CD ? L CD . ? A CD 164 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 103.9 ? 
50  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 CD ? L CD . ? A CD 164 ? 1_555 NE2 ? A HIS 63  ? A HIS 63  ? 1_555 86.0  ? 
51  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 CD ? L CD . ? A CD 164 ? 1_555 NE2 ? A HIS 63  ? A HIS 63  ? 1_555 100.3 ? 
52  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 CD ? L CD . ? A CD 164 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 87.3  ? 
53  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 CD ? L CD . ? A CD 164 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 91.8  ? 
54  NE2 ? A HIS 63  ? A HIS 63  ? 1_555 CD ? L CD . ? A CD 164 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 167.3 ? 
55  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 CD ? L CD . ? A CD 164 ? 1_555 O   ? O HOH .   ? A HOH 176 ? 1_555 90.0  ? 
56  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 CD ? L CD . ? A CD 164 ? 1_555 O   ? O HOH .   ? A HOH 176 ? 1_555 165.6 ? 
57  NE2 ? A HIS 63  ? A HIS 63  ? 1_555 CD ? L CD . ? A CD 164 ? 1_555 O   ? O HOH .   ? A HOH 176 ? 1_555 84.1  ? 
58  NE2 ? A HIS 120 ? A HIS 120 ? 1_555 CD ? L CD . ? A CD 164 ? 1_555 O   ? O HOH .   ? A HOH 176 ? 1_555 85.1  ? 
59  ND1 ? A HIS 46  ? A HIS 46  ? 1_555 CD ? L CD . ? A CD 164 ? 1_555 O   ? O HOH .   ? A HOH 224 ? 1_555 165.9 ? 
60  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 CD ? L CD . ? A CD 164 ? 1_555 O   ? O HOH .   ? A HOH 224 ? 1_555 90.2  ? 
61  NE2 ? A HIS 63  ? A HIS 63  ? 1_555 CD ? L CD . ? A CD 164 ? 1_555 O   ? O HOH .   ? A HOH 224 ? 1_555 90.6  ? 
62  NE2 ? A HIS 120 ? A HIS 120 ? 1_555 CD ? L CD . ? A CD 164 ? 1_555 O   ? O HOH .   ? A HOH 224 ? 1_555 93.3  ? 
63  O   ? O HOH .   ? A HOH 176 ? 1_555 CD ? L CD . ? A CD 164 ? 1_555 O   ? O HOH .   ? A HOH 224 ? 1_555 76.0  ? 
64  OE1 A A GLU 50  ? A GLU 50  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 OE1 B A GLU 50  ? A GLU 50  ? 1_555 36.9  ? 
65  OE1 A A GLU 50  ? A GLU 50  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 OE2 B A GLU 50  ? A GLU 50  ? 1_555 30.5  ? 
66  OE1 B A GLU 50  ? A GLU 50  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 OE2 B A GLU 50  ? A GLU 50  ? 1_555 51.8  ? 
67  OE1 A A GLU 50  ? A GLU 50  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 OD2 ? A ASP 52  ? A ASP 52  ? 1_555 99.8  ? 
68  OE1 B A GLU 50  ? A GLU 50  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 OD2 ? A ASP 52  ? A ASP 52  ? 1_555 136.3 ? 
69  OE2 B A GLU 50  ? A GLU 50  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 OD2 ? A ASP 52  ? A ASP 52  ? 1_555 95.4  ? 
70  OE1 A A GLU 50  ? A GLU 50  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 OD2 ? A ASP 90  ? A ASP 90  ? 1_655 112.1 ? 
71  OE1 B A GLU 50  ? A GLU 50  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 OD2 ? A ASP 90  ? A ASP 90  ? 1_655 94.1  ? 
72  OE2 B A GLU 50  ? A GLU 50  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 OD2 ? A ASP 90  ? A ASP 90  ? 1_655 141.8 ? 
73  OD2 ? A ASP 52  ? A ASP 52  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 OD2 ? A ASP 90  ? A ASP 90  ? 1_655 101.7 ? 
74  OE1 A A GLU 50  ? A GLU 50  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 OD1 ? A ASP 92  ? A ASP 92  ? 1_655 105.0 ? 
75  OE1 B A GLU 50  ? A GLU 50  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 OD1 ? A ASP 92  ? A ASP 92  ? 1_655 72.3  ? 
76  OE2 B A GLU 50  ? A GLU 50  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 OD1 ? A ASP 92  ? A ASP 92  ? 1_655 95.7  ? 
77  OD2 ? A ASP 52  ? A ASP 52  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 OD1 ? A ASP 92  ? A ASP 92  ? 1_655 147.8 ? 
78  OD2 ? A ASP 90  ? A ASP 90  ? 1_655 CD ? F CD . ? A CD 158 ? 1_555 OD1 ? A ASP 92  ? A ASP 92  ? 1_655 87.7  ? 
79  OE1 A A GLU 50  ? A GLU 50  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 OD2 ? A ASP 92  ? A ASP 92  ? 1_655 128.2 ? 
80  OE1 B A GLU 50  ? A GLU 50  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 OD2 ? A ASP 92  ? A ASP 92  ? 1_655 116.6 ? 
81  OE2 B A GLU 50  ? A GLU 50  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 OD2 ? A ASP 92  ? A ASP 92  ? 1_655 99.0  ? 
82  OD2 ? A ASP 52  ? A ASP 52  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 OD2 ? A ASP 92  ? A ASP 92  ? 1_655 94.1  ? 
83  OD2 ? A ASP 90  ? A ASP 90  ? 1_655 CD ? F CD . ? A CD 158 ? 1_555 OD2 ? A ASP 92  ? A ASP 92  ? 1_655 113.3 ? 
84  OD1 ? A ASP 92  ? A ASP 92  ? 1_655 CD ? F CD . ? A CD 158 ? 1_555 OD2 ? A ASP 92  ? A ASP 92  ? 1_655 54.2  ? 
85  OE1 A A GLU 50  ? A GLU 50  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 O   ? O HOH .   ? A HOH 186 ? 1_655 76.5  ? 
86  OE1 B A GLU 50  ? A GLU 50  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 O   ? O HOH .   ? A HOH 186 ? 1_655 86.2  ? 
87  OE2 B A GLU 50  ? A GLU 50  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 O   ? O HOH .   ? A HOH 186 ? 1_655 104.1 ? 
88  OD2 ? A ASP 52  ? A ASP 52  ? 1_555 CD ? F CD . ? A CD 158 ? 1_555 O   ? O HOH .   ? A HOH 186 ? 1_655 73.8  ? 
89  OD2 ? A ASP 90  ? A ASP 90  ? 1_655 CD ? F CD . ? A CD 158 ? 1_555 O   ? O HOH .   ? A HOH 186 ? 1_655 50.5  ? 
90  OD1 ? A ASP 92  ? A ASP 92  ? 1_655 CD ? F CD . ? A CD 158 ? 1_555 O   ? O HOH .   ? A HOH 186 ? 1_655 131.8 ? 
91  OD2 ? A ASP 92  ? A ASP 92  ? 1_655 CD ? F CD . ? A CD 158 ? 1_555 O   ? O HOH .   ? A HOH 186 ? 1_655 154.7 ? 
92  ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? B ZN . ? A ZN 154 ? 1_555 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 106.9 ? 
93  ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? B ZN . ? A ZN 154 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 112.7 ? 
94  ND1 ? A HIS 71  ? A HIS 71  ? 1_555 ZN ? B ZN . ? A ZN 154 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 118.1 ? 
95  ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? B ZN . ? A ZN 154 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 104.4 ? 
96  ND1 ? A HIS 71  ? A HIS 71  ? 1_555 ZN ? B ZN . ? A ZN 154 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 97.6  ? 
97  ND1 ? A HIS 80  ? A HIS 80  ? 1_555 ZN ? B ZN . ? A ZN 154 ? 1_555 OD1 ? A ASP 83  ? A ASP 83  ? 1_555 115.4 ? 
98  OD1 ? A ASP 76  ? A ASP 76  ? 1_555 CD ? I CD . ? A CD 161 ? 1_555 O   ? O HOH .   ? A HOH 206 ? 1_555 104.3 ? 
99  OD1 ? A ASP 76  ? A ASP 76  ? 1_555 CD ? I CD . ? A CD 161 ? 1_555 O   ? O HOH .   ? A HOH 234 ? 1_555 91.4  ? 
100 O   ? O HOH .   ? A HOH 206 ? 1_555 CD ? I CD . ? A CD 161 ? 1_555 O   ? O HOH .   ? A HOH 234 ? 1_555 94.8  ? 
101 OD1 ? A ASP 76  ? A ASP 76  ? 1_555 CD ? I CD . ? A CD 161 ? 1_555 O   ? O HOH .   ? A HOH 384 ? 1_555 165.8 ? 
102 O   ? O HOH .   ? A HOH 206 ? 1_555 CD ? I CD . ? A CD 161 ? 1_555 O   ? O HOH .   ? A HOH 384 ? 1_555 88.7  ? 
103 O   ? O HOH .   ? A HOH 234 ? 1_555 CD ? I CD . ? A CD 161 ? 1_555 O   ? O HOH .   ? A HOH 384 ? 1_555 93.2  ? 
104 O   ? A ASP 109 ? A ASP 109 ? 1_555 CD ? J CD . ? A CD 162 ? 1_555 ND1 B A HIS 110 ? A HIS 110 ? 1_555 83.8  ? 
105 O   ? A ASP 109 ? A ASP 109 ? 1_555 CD ? J CD . ? A CD 162 ? 1_555 OXT ? A GLN 153 ? A GLN 153 ? 4_556 92.2  ? 
106 ND1 B A HIS 110 ? A HIS 110 ? 1_555 CD ? J CD . ? A CD 162 ? 1_555 OXT ? A GLN 153 ? A GLN 153 ? 4_556 84.0  ? 
107 O   ? A ASP 109 ? A ASP 109 ? 1_555 CD ? J CD . ? A CD 162 ? 1_555 O   ? O HOH .   ? A HOH 182 ? 1_555 96.8  ? 
108 ND1 B A HIS 110 ? A HIS 110 ? 1_555 CD ? J CD . ? A CD 162 ? 1_555 O   ? O HOH .   ? A HOH 182 ? 1_555 94.8  ? 
109 OXT ? A GLN 153 ? A GLN 153 ? 4_556 CD ? J CD . ? A CD 162 ? 1_555 O   ? O HOH .   ? A HOH 182 ? 1_555 170.8 ? 
110 O   ? A ASP 109 ? A ASP 109 ? 1_555 CD ? J CD . ? A CD 162 ? 1_555 O   ? O HOH .   ? A HOH 339 ? 1_555 83.7  ? 
111 ND1 B A HIS 110 ? A HIS 110 ? 1_555 CD ? J CD . ? A CD 162 ? 1_555 O   ? O HOH .   ? A HOH 339 ? 1_555 163.1 ? 
112 OXT ? A GLN 153 ? A GLN 153 ? 4_556 CD ? J CD . ? A CD 162 ? 1_555 O   ? O HOH .   ? A HOH 339 ? 1_555 107.8 ? 
113 O   ? O HOH .   ? A HOH 182 ? 1_555 CD ? J CD . ? A CD 162 ? 1_555 O   ? O HOH .   ? A HOH 339 ? 1_555 75.4  ? 
114 OD2 ? A ASP 109 ? A ASP 109 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 209 ? 1_555 86.4  ? 
115 OD2 ? A ASP 109 ? A ASP 109 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 295 ? 1_555 108.0 ? 
116 O   ? O HOH .   ? A HOH 209 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 295 ? 1_555 83.9  ? 
117 OD2 ? A ASP 109 ? A ASP 109 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 306 ? 1_555 50.8  ? 
118 O   ? O HOH .   ? A HOH 209 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 306 ? 1_555 96.6  ? 
119 O   ? O HOH .   ? A HOH 295 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 306 ? 1_555 158.6 ? 
120 OD2 ? A ASP 109 ? A ASP 109 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 343 ? 1_555 161.5 ? 
121 O   ? O HOH .   ? A HOH 209 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 343 ? 1_555 103.7 ? 
122 O   ? O HOH .   ? A HOH 295 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 343 ? 1_555 88.7  ? 
123 O   ? O HOH .   ? A HOH 306 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 343 ? 1_555 111.8 ? 
124 OD2 ? A ASP 109 ? A ASP 109 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 376 ? 1_555 81.6  ? 
125 O   ? O HOH .   ? A HOH 209 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 376 ? 1_555 140.4 ? 
126 O   ? O HOH .   ? A HOH 295 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 376 ? 1_555 64.6  ? 
127 O   ? O HOH .   ? A HOH 306 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 376 ? 1_555 104.3 ? 
128 O   ? O HOH .   ? A HOH 343 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 376 ? 1_555 99.2  ? 
129 OD2 ? A ASP 109 ? A ASP 109 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 419 ? 1_555 101.2 ? 
130 O   ? O HOH .   ? A HOH 209 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 419 ? 1_555 94.6  ? 
131 O   ? O HOH .   ? A HOH 295 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 419 ? 1_555 150.6 ? 
132 O   ? O HOH .   ? A HOH 306 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 419 ? 1_555 50.9  ? 
133 O   ? O HOH .   ? A HOH 343 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 419 ? 1_555 62.9  ? 
134 O   ? O HOH .   ? A HOH 376 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 419 ? 1_555 124.6 ? 
135 OD2 ? A ASP 109 ? A ASP 109 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 421 ? 1_555 64.2  ? 
136 O   ? O HOH .   ? A HOH 209 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 421 ? 1_555 140.0 ? 
137 O   ? O HOH .   ? A HOH 295 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 421 ? 1_555 129.2 ? 
138 O   ? O HOH .   ? A HOH 306 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 421 ? 1_555 44.0  ? 
139 O   ? O HOH .   ? A HOH 343 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 421 ? 1_555 99.3  ? 
140 O   ? O HOH .   ? A HOH 376 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 421 ? 1_555 64.6  ? 
141 O   ? O HOH .   ? A HOH 419 ? 1_555 CD ? K CD . ? A CD 163 ? 1_555 O   ? O HOH .   ? A HOH 421 ? 1_555 67.5  ? 
142 NE2 A A HIS 110 ? A HIS 110 ? 1_555 CD ? G CD . ? A CD 159 ? 1_555 OXT ? A GLN 153 ? A GLN 153 ? 4_556 90.6  ? 
143 NE2 A A HIS 110 ? A HIS 110 ? 1_555 CD ? G CD . ? A CD 159 ? 1_555 O   ? A GLN 153 ? A GLN 153 ? 4_556 142.4 ? 
144 OXT ? A GLN 153 ? A GLN 153 ? 4_556 CD ? G CD . ? A CD 159 ? 1_555 O   ? A GLN 153 ? A GLN 153 ? 4_556 54.6  ? 
145 NE2 A A HIS 110 ? A HIS 110 ? 1_555 CD ? G CD . ? A CD 159 ? 1_555 O   ? O HOH .   ? A HOH 210 ? 1_555 104.2 ? 
146 OXT ? A GLN 153 ? A GLN 153 ? 4_556 CD ? G CD . ? A CD 159 ? 1_555 O   ? O HOH .   ? A HOH 210 ? 1_555 163.8 ? 
147 O   ? A GLN 153 ? A GLN 153 ? 4_556 CD ? G CD . ? A CD 159 ? 1_555 O   ? O HOH .   ? A HOH 210 ? 1_555 109.4 ? 
148 NE2 A A HIS 110 ? A HIS 110 ? 1_555 CD ? G CD . ? A CD 159 ? 1_555 O   ? O HOH .   ? A HOH 244 ? 1_555 96.0  ? 
149 OXT ? A GLN 153 ? A GLN 153 ? 4_556 CD ? G CD . ? A CD 159 ? 1_555 O   ? O HOH .   ? A HOH 244 ? 1_555 93.6  ? 
150 O   ? A GLN 153 ? A GLN 153 ? 4_556 CD ? G CD . ? A CD 159 ? 1_555 O   ? O HOH .   ? A HOH 244 ? 1_555 99.5  ? 
151 O   ? O HOH .   ? A HOH 210 ? 1_555 CD ? G CD . ? A CD 159 ? 1_555 O   ? O HOH .   ? A HOH 244 ? 1_555 91.4  ? 
152 NE2 A A HIS 110 ? A HIS 110 ? 1_555 CD ? G CD . ? A CD 159 ? 1_555 O   ? O HOH .   ? A HOH 396 ? 1_555 79.5  ? 
153 OXT ? A GLN 153 ? A GLN 153 ? 4_556 CD ? G CD . ? A CD 159 ? 1_555 O   ? O HOH .   ? A HOH 396 ? 1_555 88.2  ? 
154 O   ? A GLN 153 ? A GLN 153 ? 4_556 CD ? G CD . ? A CD 159 ? 1_555 O   ? O HOH .   ? A HOH 396 ? 1_555 85.2  ? 
155 O   ? O HOH .   ? A HOH 210 ? 1_555 CD ? G CD . ? A CD 159 ? 1_555 O   ? O HOH .   ? A HOH 396 ? 1_555 88.0  ? 
156 O   ? O HOH .   ? A HOH 244 ? 1_555 CD ? G CD . ? A CD 159 ? 1_555 O   ? O HOH .   ? A HOH 396 ? 1_555 175.2 ? 
157 OE1 ? A GLU 121 ? A GLU 121 ? 1_555 CD ? E CD . ? A CD 157 ? 1_555 OG  ? A SER 142 ? A SER 142 ? 1_555 84.3  ? 
158 OE1 ? A GLU 121 ? A GLU 121 ? 1_555 CD ? E CD . ? A CD 157 ? 1_555 CL  ? M CL  .   ? A CL  165 ? 1_555 72.9  ? 
159 OG  ? A SER 142 ? A SER 142 ? 1_555 CD ? E CD . ? A CD 157 ? 1_555 CL  ? M CL  .   ? A CL  165 ? 1_555 79.1  ? 
160 OE1 ? A GLU 121 ? A GLU 121 ? 1_555 CD ? E CD . ? A CD 157 ? 1_555 CL  ? N CL  .   ? A CL  166 ? 1_555 171.0 ? 
161 OG  ? A SER 142 ? A SER 142 ? 1_555 CD ? E CD . ? A CD 157 ? 1_555 CL  ? N CL  .   ? A CL  166 ? 1_555 87.6  ? 
162 CL  ? M CL  .   ? A CL  165 ? 1_555 CD ? E CD . ? A CD 157 ? 1_555 CL  ? N CL  .   ? A CL  166 ? 1_555 101.9 ? 
163 OE1 ? A GLU 121 ? A GLU 121 ? 1_555 CD ? E CD . ? A CD 157 ? 1_555 O   ? O HOH .   ? A HOH 257 ? 1_555 95.3  ? 
164 OG  ? A SER 142 ? A SER 142 ? 1_555 CD ? E CD . ? A CD 157 ? 1_555 O   ? O HOH .   ? A HOH 257 ? 1_555 178.4 ? 
165 CL  ? M CL  .   ? A CL  165 ? 1_555 CD ? E CD . ? A CD 157 ? 1_555 O   ? O HOH .   ? A HOH 257 ? 1_555 102.3 ? 
166 CL  ? N CL  .   ? A CL  166 ? 1_555 CD ? E CD . ? A CD 157 ? 1_555 O   ? O HOH .   ? A HOH 257 ? 1_555 92.9  ? 
167 OE1 ? A GLU 121 ? A GLU 121 ? 1_555 CD ? E CD . ? A CD 157 ? 1_555 O   ? O HOH .   ? A HOH 275 ? 1_555 89.2  ? 
168 OG  ? A SER 142 ? A SER 142 ? 1_555 CD ? E CD . ? A CD 157 ? 1_555 O   ? O HOH .   ? A HOH 275 ? 1_555 83.7  ? 
169 CL  ? M CL  .   ? A CL  165 ? 1_555 CD ? E CD . ? A CD 157 ? 1_555 O   ? O HOH .   ? A HOH 275 ? 1_555 156.2 ? 
170 CL  ? N CL  .   ? A CL  166 ? 1_555 CD ? E CD . ? A CD 157 ? 1_555 O   ? O HOH .   ? A HOH 275 ? 1_555 93.6  ? 
171 O   ? O HOH .   ? A HOH 257 ? 1_555 CD ? E CD . ? A CD 157 ? 1_555 O   ? O HOH .   ? A HOH 275 ? 1_555 94.7  ? 
# 
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 1999-04-21 
2 'Structure model' 1 1 2007-10-16 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2017-10-04 
5 'Structure model' 1 4 2021-11-03 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_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' 'Version format compliance' 
3 4 'Structure model' 'Refinement description'    
4 5 'Structure model' 'Data collection'           
5 5 'Structure model' 'Database references'       
6 5 'Structure model' 'Derived calculations'      
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' software               
2 5 'Structure model' database_2             
3 5 'Structure model' diffrn_source          
4 5 'Structure model' pdbx_struct_conn_angle 
5 5 'Structure model' struct_conn            
6 5 'Structure model' struct_ref_seq_dif     
7 5 'Structure model' struct_site            
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  4 'Structure model' '_software.name'                              
2  5 'Structure model' '_database_2.pdbx_DOI'                        
3  5 'Structure model' '_database_2.pdbx_database_accession'         
4  5 'Structure model' '_diffrn_source.pdbx_synchrotron_site'        
5  5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_comp_id'  
6  5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_auth_seq_id'   
7  5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_alt_id'  
8  5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_asym_id' 
9  5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_atom_id' 
10 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_comp_id' 
11 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_label_seq_id'  
12 5 'Structure model' '_pdbx_struct_conn_angle.ptnr1_symmetry'      
13 5 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_comp_id'  
14 5 'Structure model' '_pdbx_struct_conn_angle.ptnr2_auth_seq_id'   
15 5 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_asym_id' 
16 5 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_atom_id' 
17 5 'Structure model' '_pdbx_struct_conn_angle.ptnr2_label_comp_id' 
18 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_comp_id'  
19 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_auth_seq_id'   
20 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_alt_id'  
21 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_asym_id' 
22 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_atom_id' 
23 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_comp_id' 
24 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_label_seq_id'  
25 5 'Structure model' '_pdbx_struct_conn_angle.ptnr3_symmetry'      
26 5 'Structure model' '_pdbx_struct_conn_angle.value'               
27 5 'Structure model' '_struct_conn.pdbx_dist_value'                
28 5 'Structure model' '_struct_conn.pdbx_ptnr1_label_alt_id'        
29 5 'Structure model' '_struct_conn.ptnr1_auth_comp_id'             
30 5 'Structure model' '_struct_conn.ptnr1_auth_seq_id'              
31 5 'Structure model' '_struct_conn.ptnr1_label_asym_id'            
32 5 'Structure model' '_struct_conn.ptnr1_label_atom_id'            
33 5 'Structure model' '_struct_conn.ptnr1_label_comp_id'            
34 5 'Structure model' '_struct_conn.ptnr1_label_seq_id'             
35 5 'Structure model' '_struct_conn.ptnr1_symmetry'                 
36 5 'Structure model' '_struct_conn.ptnr2_auth_comp_id'             
37 5 'Structure model' '_struct_conn.ptnr2_auth_seq_id'              
38 5 'Structure model' '_struct_conn.ptnr2_label_asym_id'            
39 5 'Structure model' '_struct_conn.ptnr2_label_atom_id'            
40 5 'Structure model' '_struct_conn.ptnr2_label_comp_id'            
41 5 'Structure model' '_struct_conn.ptnr2_label_seq_id'             
42 5 'Structure model' '_struct_conn.ptnr2_symmetry'                 
43 5 'Structure model' '_struct_ref_seq_dif.details'                 
44 5 'Structure model' '_struct_site.pdbx_auth_asym_id'              
45 5 'Structure model' '_struct_site.pdbx_auth_comp_id'              
46 5 'Structure model' '_struct_site.pdbx_auth_seq_id'               
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
DENZO     'data reduction' . ? 1 
SCALEPACK 'data scaling'   . ? 2 
AMoRE     phasing          . ? 3 
SHELXL    refinement       . ? 4 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 OE2 A GLU 49  ? ? O A HOH 218 ? ? 2.03 
2  1 O   A HOH 246 ? ? O A HOH 287 ? ? 2.06 
3  1 O   A HOH 226 ? ? O A HOH 430 ? ? 2.08 
4  1 OG  A SER 107 ? A O A HOH 267 ? ? 2.10 
5  1 O   A HOH 180 ? ? O A HOH 326 ? ? 2.11 
6  1 O   A HOH 422 ? ? O A HOH 433 ? ? 2.11 
7  1 O   A PRO 66  ? ? O A HOH 187 ? ? 2.12 
8  1 O   A HOH 286 ? ? O A HOH 378 ? ? 2.14 
9  1 O   A HOH 346 ? ? O A HOH 422 ? ? 2.15 
10 1 O   A HOH 230 ? ? O A HOH 411 ? ? 2.15 
11 1 O   A HOH 258 ? ? O A HOH 264 ? ? 2.16 
12 1 OE2 A GLU 24  ? A O A HOH 435 ? ? 2.16 
13 1 O   A HOH 325 ? ? O A HOH 344 ? ? 2.16 
14 1 CG  A LYS 9   ? ? O A HOH 330 ? ? 2.16 
15 1 O   A HOH 183 ? ? O A HOH 345 ? ? 2.16 
16 1 O   A HOH 276 ? ? O A HOH 312 ? ? 2.18 
17 1 O   A HOH 231 ? ? O A HOH 286 ? ? 2.18 
18 1 O   A HOH 211 ? ? O A HOH 436 ? ? 2.18 
19 1 O   A HOH 179 ? ? O A HOH 435 ? ? 2.18 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 285 ? ? 1_555 O A HOH 293 ? ? 4_556 2.11 
2 1 O A HOH 186 ? ? 1_555 O A HOH 268 ? ? 1_455 2.16 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 OE1 A GLU 21 ? ? CD A GLU 21 ? ? OE2 A GLU 21 ? ? 115.73 123.30 -7.57 1.20 N 
2 1 C   A ALA 55 ? ? N  A GLY 56 ? ? CA  A GLY 56 ? ? 135.86 122.30 13.56 2.10 Y 
3 1 CA  A CYS 57 ? ? CB A CYS 57 ? ? SG  A CYS 57 ? ? 130.78 114.20 16.58 1.10 N 
4 1 O   A CYS 57 ? ? C  A CYS 57 ? ? N   A THR 58 ? ? 133.00 122.70 10.30 1.60 Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 53 ? ? -95.75  56.79 
2 1 CYS A 57 ? ? -101.91 45.25 
3 1 ASN A 65 ? ? -144.86 59.78 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A GLU 77  ? CG  ? A GLU 77  CG  
2  1 Y 1 A GLU 77  ? CD  ? A GLU 77  CD  
3  1 Y 1 A GLU 77  ? OE1 ? A GLU 77  OE1 
4  1 Y 1 A GLU 77  ? OE2 ? A GLU 77  OE2 
5  1 Y 1 A GLU 78  ? CG  ? A GLU 78  CG  
6  1 Y 1 A GLU 78  ? CD  ? A GLU 78  CD  
7  1 Y 1 A GLU 78  ? OE1 ? A GLU 78  OE1 
8  1 Y 1 A GLU 78  ? OE2 ? A GLU 78  OE2 
9  1 Y 1 A LYS 91  ? CD  ? A LYS 91  CD  
10 1 Y 1 A LYS 91  ? CE  ? A LYS 91  CE  
11 1 Y 1 A LYS 91  ? NZ  ? A LYS 91  NZ  
12 1 Y 1 A LYS 122 ? CD  ? A LYS 122 CD  
13 1 Y 1 A LYS 122 ? CE  ? A LYS 122 CE  
14 1 Y 1 A LYS 122 ? NZ  ? A LYS 122 NZ  
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'        ZN  
3 'COPPER (II) ION' CU  
4 'CADMIUM ION'     CD  
5 'CHLORIDE ION'    CL  
6 water             HOH 
# 
