data_2XJL
# 
_entry.id   2XJL 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.287 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   2XJL         
PDBE  EBI-44424    
WWPDB D_1290044424 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
_pdbx_database_related.details 
PDB 2WZ6 unspecified 'G93A SOD1 MUTANT COMPLEXED WITH QUINAZOLINE.' 
PDB 1PTZ unspecified 
'CRYSTAL STRUCTURE OF THE HUMAN CU, ZN SUPEROXIDE DISMUTASE,FAMILIAL AMYOTROPHIC LATERAL SCLEROSIS (FALS) MUTANT H43R' 
PDB 1OEZ unspecified 'ZN HIS46ARG MUTANT OF HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
PDB 1AZV unspecified 'FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)' 
PDB 1HL4 unspecified 'THE STRUCTURE OF APO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
PDB 2WYZ unspecified 'L38V SOD1 MUTANT COMPLEXED WITH UMP' 
PDB 2VR6 unspecified 'CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.3 A RESOLUTION' 
PDB 1OZU unspecified 
'CRYSTAL STRUCTURE OF FAMILIAL ALS MUTANT S134N OF HUMAN CU,ZN SUPEROXIDE DISMUTASE ( CUZNSOD) TO 1.3A RESOLUTION' 
PDB 2C9V unspecified 'ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 2WZ5 unspecified 'L38V SOD1 MUTANT COMPLEXED WITH L-METHIONINE .' 
PDB 1PU0 unspecified 'STRUCTURE OF HUMAN CU,ZN SUPEROXIDE DISMUTASE' 
PDB 1FUN unspecified 
'SUPEROXIDE DISMUTASE MUTANT WITH LYS 136 REPLACED BY GLU, CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (K136E, C6A, C111S)' 
PDB 1SOS unspecified 'SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (C6A, C111S)' 
PDB 1N19 unspecified 'STRUCTURE OF THE HSOD A4V MUTANT' 
PDB 1P1V unspecified 'CRYSTAL STRUCTURE OF FALS-ASSOCIATED HUMAN COPPER-ZINCSUPEROXIDE DISMUTASE (CUZNSOD) MUTANT D125H TO 1.4A' 
PDB 2WZ0 unspecified 'L38V SOD1 MUTANT COMPLEXED WITH ANILINE.' 
PDB 2WKO unspecified 'STRUCTURE OF METAL LOADED PATHOGENIC SOD1 MUTANT G93A.' 
PDB 1L3N unspecified 'THE SOLUTION STRUCTURE OF REDUCED DIMERIC COPPER ZINC SOD:THE STRUCTURAL EFFECTS OF DIMERIZATION' 
PDB 1UXL unspecified 'I113T MUTANT OF HUMAN SOD1' 
PDB 2AF2 unspecified 'SOLUTION STRUCTURE OF DISULFIDE REDUCED AND COPPER DEPLETEDHUMAN SUPEROXIDE DISMUTASE' 
PDB 2VR8 unspecified 'CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.36 A RESOLUTION' 
PDB 1RK7 unspecified 'SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE DISMUTASE: ROLEOF METAL IONS IN PROTEIN FOLDING' 
PDB 2VR7 unspecified 'CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.58 A RESOLUTION' 
PDB 2C9S unspecified '1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN- ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 2V0A unspecified 'ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN SUPEROXIDE DISMUTASE' 
PDB 4SOD unspecified 
;CU,ZN SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (C6A,C111S) WITH AN 18-RESIDUE HEPARIN-BINDING PEPTIDE FUSED TO THE C- TERMINUS (THEORETICAL MODEL)
;
PDB 1MFM unspecified 'MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q AT ATOMIC RESOLUTION' 
PDB 2WYT unspecified '1.0 A RESOLUTION STRUCTURE OF L38V SOD1 MUTANT' 
PDB 1DSW unspecified 
;THE SOLUTION STRUCTURE OF A MONOMERIC, REDUCED FORM OFHUMAN COPPER, ZINC SUPEROXIDE DISMUTASE BEARING THE SAMECHARGE AS THE NATIVE PROTEIN
;
PDB 1KMG unspecified 'THE SOLUTION STRUCTURE OF MONOMERIC COPPER- FREE SUPEROXIDEDISMUTASE' 
PDB 1OZT unspecified 
'CRYSTAL STRUCTURE OF APO-H46R FAMILIAL ALS MUTANT HUMAN CU,ZN SUPEROXIDE DISMUTASE ( CUZNSOD) TO 2.5A RESOLUTION' 
PDB 1N18 unspecified 'THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE DISMUTASE, C6A,C111S' 
PDB 1BA9 unspecified 'THE SOLUTION STRUCTURE OF REDUCED MONOMERIC SUPEROXIDE DISMUTASE, NMR, 36 STRUCTURES' 
PDB 2C9U unspecified '1.24 ANGSTROMS RESOLUTION STRUCTURE OF AS- ISOLATED CU-ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 1HL5 unspecified 'THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
PDB 1SPD unspecified 'SUPEROXIDE DISMUTASE' 
PDB 1UXM unspecified 'A4V MUTANT OF HUMAN SOD1' 
PDB 2XJK unspecified 'MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        2XJL 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2010-07-07 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Saraboji, K.'    1 
'Leinartaite, L.' 2 
'Nordlund, A.'    3 
'Oliveberg, M.'   4 
'Logan, D.T.'     5 
# 
loop_
_citation.id 
_citation.title 
_citation.journal_abbrev 
_citation.journal_volume 
_citation.page_first 
_citation.page_last 
_citation.year 
_citation.journal_id_ASTM 
_citation.country 
_citation.journal_id_ISSN 
_citation.journal_id_CSD 
_citation.book_publisher 
_citation.pdbx_database_id_PubMed 
_citation.pdbx_database_id_DOI 
primary 
'Folding Catalysis by Transient Coordination of Zn2+ to the Cu Ligands of the Als-Associated Enzyme Cu/Zn Superoxide Dismutase 1.' 
J.Am.Chem.Soc.         132 13495 ? 2010 JACSAT US 0002-7863 0004 ? 20822138 10.1021/JA1057136       
1       'Functional Features Cause Misfolding of the Als-Provoking Enzyme Sod1.' Proc.Natl.Acad.Sci.USA 106 9667  ? 2009 PNASA6 US 
0027-8424 0040 ? 19497878 10.1073/PNAS.0812046106 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Leinartaite, L.' 1  
primary 'Saraboji, K.'    2  
primary 'Nordlund, A.'    3  
primary 'Logan, D.T.'     4  
primary 'Oliveberg, M.'   5  
1       'Nordlund, A.'    6  
1       'Leinartaite, L.' 7  
1       'Saraboji, K.'    8  
1       'Aisenbrey, C.'   9  
1       'Grobner, G.'     10 
1       'Zetterstrom, P.' 11 
1       'Danielsson, J.'  12 
1       'Logan, D.T.'     13 
1       'Oliveberg, M.'   14 
# 
_cell.entry_id           2XJL 
_cell.length_a           34.760 
_cell.length_b           49.220 
_cell.length_c           80.460 
_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                         2XJL 
_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 'SUPEROXIDE DISMUTASE [CU-ZN]' 15664.223 1   1.15.1.1 YES ? ? 
2 non-polymer syn 'ZINC ION'                     65.409    4   ?        ?   ? ? 
3 non-polymer syn 'DI(HYDROXYETHYL)ETHER'        106.120   1   ?        ?   ? ? 
4 non-polymer syn 'SODIUM ION'                   22.990    2   ?        ?   ? ? 
5 non-polymer syn 'ACETATE ION'                  59.044    1   ?        ?   ? ? 
6 water       nat water                          18.015    145 ?        ?   ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'CU, ZN SUPEROXIDE DISMUTASE' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFSVSEEEDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHAIIGRTLVVSEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFSVSEEEDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHAIIGRTLVVSEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_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  SER n 
1 47  VAL n 
1 48  SER 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 ALA n 
1 112 ILE n 
1 113 ILE n 
1 114 GLY n 
1 115 ARG n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 SER n 
1 121 GLU n 
1 122 LYS n 
1 123 ALA n 
1 124 ASP n 
1 125 ASP n 
1 126 LEU n 
1 127 GLY n 
1 128 LYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 GLU n 
1 133 GLU n 
1 134 SER n 
1 135 THR n 
1 136 LYS n 
1 137 THR n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 ARG n 
1 144 LEU n 
1 145 ALA n 
1 146 CYS n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 ILE n 
1 152 ALA n 
1 153 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               HUMAN 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'HOMO SAPIENS' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'ESCHERICHIA COLI' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_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_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.pdbx_db_isoform            ? 
# 
_struct_ref_seq.align_id                      1 
_struct_ref_seq.ref_id                        1 
_struct_ref_seq.pdbx_PDB_id_code              2XJL 
_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                  2 
_struct_ref_seq.pdbx_db_align_beg_ins_code    ? 
_struct_ref_seq.db_align_end                  154 
_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 2XJL ALA A 6   ? UNP P00441 CYS 7   'engineered mutation' 6   1 
1 2XJL SER A 46  ? UNP P00441 HIS 47  'engineered mutation' 46  2 
1 2XJL SER A 48  ? UNP P00441 HIS 49  'engineered mutation' 48  3 
1 2XJL GLU A 50  ? UNP P00441 PHE 51  'engineered mutation' 50  4 
1 2XJL GLU A 51  ? UNP P00441 GLY 52  'engineered mutation' 51  5 
1 2XJL ALA A 111 ? UNP P00441 CYS 112 'engineered mutation' 111 6 
1 2XJL SER A 120 ? UNP P00441 HIS 121 'engineered mutation' 120 7 
# 
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 
ACT non-polymer         . 'ACETATE ION'           ? 'C2 H3 O2 -1'    59.044  
ALA 'L-peptide linking' y ALANINE                 ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE                ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE              ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID'         ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE                ? 'C3 H7 N O2 S'   121.158 
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 
NA  non-polymer         . 'SODIUM ION'            ? 'Na 1'           22.990  
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ? 'C4 H10 O3'      106.120 
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          2XJL 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.21 
_exptl_crystal.density_percent_sol   44.3 
_exptl_crystal.description           NONE 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              5 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '25% PEG 6000, 0.1M SODIUM ACETATE (PH 5.0), 0.01M ZNCL2' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   MARRESEARCH 
_diffrn_detector.pdbx_collection_date   2007-10-19 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'BENT SI (220) CRYSTAL' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9085 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'MAX II BEAMLINE I911-5' 
_diffrn_source.pdbx_synchrotron_site       'MAX II' 
_diffrn_source.pdbx_synchrotron_beamline   I911-5 
_diffrn_source.pdbx_wavelength             0.9085 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     2XJL 
_reflns.observed_criterion_sigma_I   0.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             40.00 
_reflns.d_resolution_high            1.55 
_reflns.number_obs                   20574 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.4 
_reflns.pdbx_Rmerge_I_obs            0.08 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        17.60 
_reflns.B_iso_Wilson_estimate        14.3 
_reflns.pdbx_redundancy              8.3 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             1.55 
_reflns_shell.d_res_low              1.59 
_reflns_shell.percent_possible_all   98.6 
_reflns_shell.Rmerge_I_obs           0.62 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    3.30 
_reflns_shell.pdbx_redundancy        5.8 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 2XJL 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     19519 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          . 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             40.00 
_refine.ls_d_res_high                            1.55 
_refine.ls_percent_reflns_obs                    99.35 
_refine.ls_R_factor_obs                          0.15688 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.15551 
_refine.ls_R_factor_R_free                       0.18300 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.1 
_refine.ls_number_reflns_R_free                  1055 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.967 
_refine.correlation_coeff_Fo_to_Fc_free          0.961 
_refine.B_iso_mean                               13.056 
_refine.aniso_B[1][1]                            -0.28 
_refine.aniso_B[2][2]                            0.97 
_refine.aniso_B[3][3]                            -0.69 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.00 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.40 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  
'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. TLS ADDED WITH U VALUES. ATOM RECORD CONTAINS SUM OF TLS AND RESIDUAL B FACTORS.' 
_refine.pdbx_starting_model                      'MONOMERIC CU,ZN SOD1' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_overall_ESU_R                       0.102 
_refine.pdbx_overall_ESU_R_Free                  0.075 
_refine.overall_SU_ML                            0.048 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             3.018 
_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_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        1099 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         17 
_refine_hist.number_atoms_solvent             145 
_refine_hist.number_atoms_total               1261 
_refine_hist.d_res_high                       1.55 
_refine_hist.d_res_low                        40.00 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
r_bond_refined_d             0.010  0.021  ? 1178 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.002  0.020  ? 781  'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.258  1.964  ? 1586 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.943  3.000  ? 1939 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.001  5.000  ? 158  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       36.599 26.275 ? 51   'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       13.273 15.000 ? 202  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       14.931 15.000 ? 5    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.105  0.200  ? 177  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.004  0.020  ? 1353 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.001  0.020  ? 203  'X-RAY DIFFRACTION' ? 
r_nbd_refined                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbd_other                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_refined              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_nbtor_other                ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_refined        ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_xyhbond_nbd_other          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_refined          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_metal_ion_other            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_vdw_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_refined     ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_hbond_other       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_refined ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_symmetry_metal_ion_other   ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_it                  0.991  1.500  ? 776  'X-RAY DIFFRACTION' ? 
r_mcbond_other               0.249  1.500  ? 335  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 1.674  2.000  ? 1238 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  2.455  3.000  ? 402  'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 3.736  4.500  ? 348  'X-RAY DIFFRACTION' ? 
r_scangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_refined       ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_long_range_B_other         ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_rigid_bond_restr           0.946  3.000  ? 1959 'X-RAY DIFFRACTION' ? 
r_sphericity_free            ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.d_res_high                       1.550 
_refine_ls_shell.d_res_low                        1.590 
_refine_ls_shell.number_reflns_R_work             1397 
_refine_ls_shell.R_factor_R_work                  0.268 
_refine_ls_shell.percent_reflns_obs               98.53 
_refine_ls_shell.R_factor_R_free                  0.288 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             80 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  2XJL 
_struct.title                     'Monomeric Human Cu,Zn Superoxide dismutase without Cu ligands' 
_struct.pdbx_descriptor           'SUPEROXIDE DISMUTASE [CU-ZN] (E.C.1.15.1.1)' 
_struct.pdbx_model_details        ? 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        2XJL 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            'OXIDOREDUCTASE, CU/ZN SOD1, METAL-BINDING, NEURODEGENERATION' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
I N N 5 ? 
J N N 6 ? 
# 
_struct_biol.id   1 
# 
_struct_conf.conf_type_id            HELX_P 
_struct_conf.id                      HELX_P1 
_struct_conf.pdbx_PDB_helix_id       1 
_struct_conf.beg_label_comp_id       GLU 
_struct_conf.beg_label_asym_id       A 
_struct_conf.beg_label_seq_id        133 
_struct_conf.pdbx_beg_PDB_ins_code   ? 
_struct_conf.end_label_comp_id       GLY 
_struct_conf.end_label_asym_id       A 
_struct_conf.end_label_seq_id        138 
_struct_conf.pdbx_end_PDB_ins_code   ? 
_struct_conf.beg_auth_comp_id        GLU 
_struct_conf.beg_auth_asym_id        A 
_struct_conf.beg_auth_seq_id         133 
_struct_conf.end_auth_comp_id        GLY 
_struct_conf.end_auth_asym_id        A 
_struct_conf.end_auth_seq_id         138 
_struct_conf.pdbx_PDB_helix_class    1 
_struct_conf.details                 ? 
_struct_conf.pdbx_PDB_helix_length   6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 57 SG A ? ? 1_555 A CYS 146 SG  A ? A CYS 57  A CYS 146  1_555 ? ? ? ? ? ? ? 2.969 ? 
disulf2  disulf ? ? A CYS 57 SG B ? ? 1_555 A CYS 146 SG  B ? A CYS 57  A CYS 146  1_555 ? ? ? ? ? ? ? 2.889 ? 
metalc1  metalc ? ? B ZN  .  ZN ? ? ? 1_555 A HIS 63  ND1 ? ? A ZN  155 A HIS 63   1_555 ? ? ? ? ? ? ? 2.034 ? 
metalc2  metalc ? ? B ZN  .  ZN ? ? ? 1_555 A HIS 80  ND1 ? ? A ZN  155 A HIS 80   1_555 ? ? ? ? ? ? ? 2.049 ? 
metalc3  metalc ? ? B ZN  .  ZN ? ? ? 1_555 A ASP 83  OD1 ? ? A ZN  155 A ASP 83   1_555 ? ? ? ? ? ? ? 1.936 ? 
metalc4  metalc ? ? B ZN  .  ZN ? ? ? 1_555 A HIS 71  ND1 ? ? A ZN  155 A HIS 71   1_555 ? ? ? ? ? ? ? 2.038 ? 
metalc5  metalc ? ? C ZN  .  ZN ? ? ? 1_555 A ALA 1   O   ? ? A ZN  156 A ALA 1    4_445 ? ? ? ? ? ? ? 2.287 ? 
metalc6  metalc ? ? C ZN  .  ZN ? ? ? 1_555 A GLU 51  OE2 ? ? A ZN  156 A GLU 51   1_555 ? ? ? ? ? ? ? 1.967 ? 
metalc7  metalc ? ? C ZN  .  ZN ? ? ? 1_555 A ASP 96  OD2 ? ? A ZN  156 A ASP 96   1_455 ? ? ? ? ? ? ? 1.925 ? 
metalc8  metalc ? ? C ZN  .  ZN ? ? ? 1_555 J HOH .   O   ? ? A ZN  156 A HOH 2143 1_555 ? ? ? ? ? ? ? 2.066 ? 
metalc9  metalc ? ? D ZN  .  ZN ? ? ? 1_555 A ASP 90  OD2 ? ? A ZN  157 A ASP 90   1_455 ? ? ? ? ? ? ? 1.982 ? 
metalc10 metalc ? ? D ZN  .  ZN ? ? ? 1_555 A ASP 52  OD2 B ? A ZN  157 A ASP 52   1_555 ? ? ? ? ? ? ? 1.892 ? 
metalc11 metalc ? ? D ZN  .  ZN ? ? ? 1_555 A ASP 52  OD2 A ? A ZN  157 A ASP 52   1_555 ? ? ? ? ? ? ? 2.012 ? 
metalc12 metalc ? ? D ZN  .  ZN ? ? ? 1_555 A ASP 92  OD1 ? ? A ZN  157 A ASP 92   1_455 ? ? ? ? ? ? ? 1.882 ? 
metalc13 metalc ? ? D ZN  .  ZN ? ? ? 1_555 A GLU 50  OE2 ? ? A ZN  157 A GLU 50   1_555 ? ? ? ? ? ? ? 1.915 ? 
metalc14 metalc ? ? E ZN  .  ZN ? ? ? 1_555 A GLN 153 O   ? ? A ZN  158 A GLN 153  4_445 ? ? ? ? ? ? ? 1.933 ? 
metalc15 metalc ? ? E ZN  .  ZN ? ? ? 1_555 A GLN 153 OXT ? ? A ZN  158 A GLN 153  4_445 ? ? ? ? ? ? ? 2.506 ? 
metalc16 metalc ? ? E ZN  .  ZN ? ? ? 1_555 J HOH .   O   ? ? A ZN  158 A HOH 2144 1_555 ? ? ? ? ? ? ? 2.163 ? 
metalc17 metalc ? ? E ZN  .  ZN ? ? ? 1_555 A HIS 110 NE2 ? ? A ZN  158 A HIS 110  1_555 ? ? ? ? ? ? ? 1.957 ? 
metalc18 metalc ? ? G NA  .  NA ? ? ? 1_555 J HOH .   O   ? ? A NA  160 A HOH 2131 1_555 ? ? ? ? ? ? ? 2.958 ? 
metalc19 metalc ? ? G NA  .  NA ? ? ? 1_555 J HOH .   O   ? ? A NA  160 A HOH 2130 1_555 ? ? ? ? ? ? ? 2.843 ? 
metalc20 metalc ? ? H NA  .  NA ? ? ? 1_555 J HOH .   O   ? ? A NA  161 A HOH 2057 1_555 ? ? ? ? ? ? ? 3.031 ? 
metalc21 metalc ? ? H NA  .  NA ? ? ? 1_555 J HOH .   O   ? ? A NA  161 A HOH 2007 1_555 ? ? ? ? ? ? ? 2.996 ? 
metalc22 metalc ? ? H NA  .  NA ? ? ? 1_555 A CYS 146 O   ? ? A NA  161 A CYS 146  1_555 ? ? ? ? ? ? ? 2.683 ? 
metalc23 metalc ? ? H NA  .  NA ? ? ? 1_555 A ALA 55  O   A ? A NA  161 A ALA 55   1_555 ? ? ? ? ? ? ? 2.217 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
_struct_sheet.id               AA 
_struct_sheet.type             ? 
_struct_sheet.number_strands   9 
_struct_sheet.details          ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA 1 2 ? anti-parallel 
AA 2 3 ? anti-parallel 
AA 3 4 ? anti-parallel 
AA 4 5 ? anti-parallel 
AA 5 6 ? anti-parallel 
AA 6 7 ? anti-parallel 
AA 7 8 ? anti-parallel 
AA 8 9 ? 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 
AA 1 THR A 2   ? LYS A 9   ? THR A 2   LYS A 9   
AA 2 GLN A 15  ? GLN A 22  ? GLN A 15  GLN A 22  
AA 3 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
AA 4 ALA A 95  ? ASP A 101 ? ALA A 95  ASP A 101 
AA 5 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
AA 6 GLY A 41  ? SER A 48  ? GLY A 41  SER A 48  
AA 7 THR A 116 ? SER A 120 ? THR A 116 SER A 120 
AA 8 ARG A 143 ? ILE A 151 ? ARG A 143 ILE A 151 
AA 9 THR A 2   ? LYS A 9   ? THR A 2   LYS A 9   
# 
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 
AA 1 2 N LEU A 8   ? N LEU A 8   O GLY A 16  ? O GLY A 16  
AA 2 3 N GLU A 21  ? N GLU A 21  O LYS A 30  ? O LYS A 30  
AA 3 4 N ILE A 35  ? N ILE A 35  O ALA A 95  ? O ALA A 95  
AA 4 5 N ASP A 96  ? N ASP A 96  O THR A 88  ? O THR A 88  
AA 5 6 N ALA A 89  ? N ALA A 89  O GLY A 41  ? O GLY A 41  
AA 6 7 N SER A 48  ? N SER A 48  O THR A 116 ? O THR A 116 
AA 7 8 O VAL A 119 ? O VAL A 119 N LEU A 144 ? N LEU A 144 
AA 8 9 N GLY A 150 ? N GLY A 150 O VAL A 5   ? O VAL A 5   
# 
loop_
_struct_site.id 
_struct_site.pdbx_evidence_code 
_struct_site.pdbx_auth_asym_id 
_struct_site.pdbx_auth_comp_id 
_struct_site.pdbx_auth_seq_id 
_struct_site.pdbx_auth_ins_code 
_struct_site.pdbx_num_residues 
_struct_site.details 
AC1 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 155'  
AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 156'  
AC3 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 157'  
AC4 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE ZN A 158'  
AC5 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE PEG A 159' 
AC6 Software ? ? ? ? 2 'BINDING SITE FOR RESIDUE NA A 160'  
AC7 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE NA A 161'  
AC8 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE ACT A 162' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4 HIS A 63  ? HIS A 63   . ? 1_555 ? 
2  AC1 4 HIS A 71  ? HIS A 71   . ? 1_555 ? 
3  AC1 4 HIS A 80  ? HIS A 80   . ? 1_555 ? 
4  AC1 4 ASP A 83  ? ASP A 83   . ? 1_555 ? 
5  AC2 4 ALA A 1   ? ALA A 1    . ? 4_445 ? 
6  AC2 4 GLU A 51  ? GLU A 51   . ? 1_555 ? 
7  AC2 4 ASP A 96  ? ASP A 96   . ? 1_455 ? 
8  AC2 4 HOH J .   ? HOH A 2143 . ? 1_555 ? 
9  AC3 4 GLU A 50  ? GLU A 50   . ? 1_555 ? 
10 AC3 4 ASP A 52  ? ASP A 52   . ? 1_555 ? 
11 AC3 4 ASP A 90  ? ASP A 90   . ? 1_455 ? 
12 AC3 4 ASP A 92  ? ASP A 92   . ? 1_455 ? 
13 AC4 3 HIS A 110 ? HIS A 110  . ? 1_555 ? 
14 AC4 3 GLN A 153 ? GLN A 153  . ? 4_445 ? 
15 AC4 3 HOH J .   ? HOH A 2144 . ? 1_555 ? 
16 AC5 8 LEU A 67  ? LEU A 67   . ? 1_555 ? 
17 AC5 8 ASP A 76  ? ASP A 76   . ? 1_555 ? 
18 AC5 8 GLU A 77  ? GLU A 77   . ? 1_555 ? 
19 AC5 8 ARG A 79  ? ARG A 79   . ? 1_555 ? 
20 AC5 8 VAL A 103 ? VAL A 103  . ? 1_555 ? 
21 AC5 8 HOH J .   ? HOH A 2074 . ? 1_555 ? 
22 AC5 8 HOH J .   ? HOH A 2078 . ? 1_555 ? 
23 AC5 8 HOH J .   ? HOH A 2145 . ? 1_555 ? 
24 AC6 2 HOH J .   ? HOH A 2130 . ? 1_555 ? 
25 AC6 2 HOH J .   ? HOH A 2131 . ? 1_555 ? 
26 AC7 5 LYS A 9   ? LYS A 9    . ? 1_555 ? 
27 AC7 5 ALA A 55  ? ALA A 55   . ? 1_555 ? 
28 AC7 5 CYS A 146 ? CYS A 146  . ? 1_555 ? 
29 AC7 5 HOH J .   ? HOH A 2007 . ? 1_555 ? 
30 AC7 5 HOH J .   ? HOH A 2057 . ? 1_555 ? 
31 AC8 6 LYS A 30  ? LYS A 30   . ? 1_555 ? 
32 AC8 6 ILE A 113 ? ILE A 113  . ? 4_545 ? 
33 AC8 6 VAL A 148 ? VAL A 148  . ? 4_545 ? 
34 AC8 6 GLY A 150 ? GLY A 150  . ? 4_545 ? 
35 AC8 6 ILE A 151 ? ILE A 151  . ? 4_545 ? 
36 AC8 6 HOH J .   ? HOH A 2032 . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          2XJL 
_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                    2XJL 
_atom_sites.fract_transf_matrix[1][1]   0.028769 
_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]   0.020317 
_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]   0.012429 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
N  
NA 
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 1   ? -12.529 -21.910 -2.074  1.00 14.54  ? 1    ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? -12.394 -20.756 -1.138  1.00 12.95  ? 1    ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? -13.127 -19.541 -1.678  1.00 12.46  ? 1    ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? -13.279 -19.384 -2.895  1.00 12.65  ? 1    ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? -10.939 -20.410 -0.941  1.00 13.06  ? 1    ALA A CB  1 
ATOM   6    N  N   . THR A 1 2   ? -13.550 -18.677 -0.760  1.00 12.24  ? 2    THR A N   1 
ATOM   7    C  CA  . THR A 1 2   ? -14.219 -17.417 -1.081  1.00 12.02  ? 2    THR A CA  1 
ATOM   8    C  C   . THR A 1 2   ? -13.269 -16.262 -0.807  1.00 11.05  ? 2    THR A C   1 
ATOM   9    O  O   . THR A 1 2   ? -12.509 -16.291 0.147   1.00 11.04  ? 2    THR A O   1 
ATOM   10   C  CB  . THR A 1 2   ? -15.512 -17.273 -0.252  1.00 12.32  ? 2    THR A CB  1 
ATOM   11   O  OG1 . THR A 1 2   ? -16.361 -18.389 -0.537  1.00 15.59  ? 2    THR A OG1 1 
ATOM   12   C  CG2 . THR A 1 2   ? -16.247 -15.976 -0.579  1.00 12.33  ? 2    THR A CG2 1 
ATOM   13   N  N   . LYS A 1 3   ? -13.292 -15.271 -1.687  1.00 10.83  ? 3    LYS A N   1 
ATOM   14   C  CA  . LYS A 1 3   ? -12.389 -14.129 -1.604  1.00 11.01  ? 3    LYS A CA  1 
ATOM   15   C  C   . LYS A 1 3   ? -13.153 -12.839 -1.765  1.00 10.45  ? 3    LYS A C   1 
ATOM   16   O  O   . LYS A 1 3   ? -14.144 -12.794 -2.477  1.00 12.07  ? 3    LYS A O   1 
ATOM   17   C  CB  . LYS A 1 3   ? -11.323 -14.202 -2.687  1.00 11.79  ? 3    LYS A CB  1 
ATOM   18   C  CG  . LYS A 1 3   ? -10.345 -15.343 -2.497  1.00 15.53  ? 3    LYS A CG  1 
ATOM   19   C  CD  . LYS A 1 3   ? -10.013 -16.015 -3.780  1.00 20.91  ? 3    LYS A CD  1 
ATOM   20   C  CE  . LYS A 1 3   ? -11.198 -16.776 -4.326  1.00 22.15  ? 3    LYS A CE  1 
ATOM   21   N  NZ  . LYS A 1 3   ? -10.810 -17.507 -5.514  1.00 22.54  ? 3    LYS A NZ  1 
ATOM   22   N  N   . ALA A 1 4   ? -12.646 -11.789 -1.132  1.00 9.54   ? 4    ALA A N   1 
ATOM   23   C  CA  . ALA A 1 4   ? -13.190 -10.450 -1.271  1.00 9.14   ? 4    ALA A CA  1 
ATOM   24   C  C   . ALA A 1 4   ? -12.068 -9.415  -1.299  1.00 9.11   ? 4    ALA A C   1 
ATOM   25   O  O   . ALA A 1 4   ? -10.932 -9.681  -0.888  1.00 9.35   ? 4    ALA A O   1 
ATOM   26   C  CB  . ALA A 1 4   ? -14.175 -10.159 -0.153  1.00 9.10   ? 4    ALA A CB  1 
ATOM   27   N  N   . VAL A 1 5   ? -12.398 -8.245  -1.825  1.00 9.46   ? 5    VAL A N   1 
ATOM   28   C  CA  . VAL A 1 5   ? -11.490 -7.111  -1.884  1.00 9.41   ? 5    VAL A CA  1 
ATOM   29   C  C   . VAL A 1 5   ? -12.243 -5.845  -1.496  1.00 8.71   ? 5    VAL A C   1 
ATOM   30   O  O   . VAL A 1 5   ? -13.378 -5.638  -1.918  1.00 9.33   ? 5    VAL A O   1 
ATOM   31   C  CB  . VAL A 1 5   ? -10.910 -6.909  -3.319  1.00 9.75   ? 5    VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 5   ? -10.056 -5.654  -3.394  1.00 11.06  ? 5    VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 5   ? -10.084 -8.108  -3.746  1.00 11.94  ? 5    VAL A CG2 1 
ATOM   34   N  N   . ALA A 1 6   ? -11.611 -5.028  -0.669  1.00 8.44   ? 6    ALA A N   1 
ATOM   35   C  CA  . ALA A 1 6   ? -12.095 -3.701  -0.345  1.00 8.28   ? 6    ALA A CA  1 
ATOM   36   C  C   . ALA A 1 6   ? -11.047 -2.692  -0.793  1.00 8.49   ? 6    ALA A C   1 
ATOM   37   O  O   . ALA A 1 6   ? -9.861  -2.823  -0.459  1.00 9.30   ? 6    ALA A O   1 
ATOM   38   C  CB  . ALA A 1 6   ? -12.369 -3.564  1.141   1.00 8.55   ? 6    ALA A CB  1 
ATOM   39   N  N   . VAL A 1 7   ? -11.498 -1.693  -1.552  1.00 9.36   ? 7    VAL A N   1 
ATOM   40   C  CA  . VAL A 1 7   ? -10.658 -0.594  -1.983  1.00 10.42  ? 7    VAL A CA  1 
ATOM   41   C  C   . VAL A 1 7   ? -10.982 0.579   -1.078  1.00 10.51  ? 7    VAL A C   1 
ATOM   42   O  O   . VAL A 1 7   ? -12.104 1.119   -1.120  1.00 10.92  ? 7    VAL A O   1 
ATOM   43   C  CB  . VAL A 1 7   ? -10.950 -0.220  -3.442  1.00 11.29  ? 7    VAL A CB  1 
ATOM   44   C  CG1 . VAL A 1 7   ? -10.138 1.024   -3.848  1.00 12.74  ? 7    VAL A CG1 1 
ATOM   45   C  CG2 . VAL A 1 7   ? -10.674 -1.412  -4.364  1.00 12.43  ? 7    VAL A CG2 1 
ATOM   46   N  N   . LEU A 1 8   ? -10.023 0.955   -0.237  1.00 11.04  ? 8    LEU A N   1 
ATOM   47   C  CA  . LEU A 1 8   ? -10.231 2.018   0.749   1.00 11.08  ? 8    LEU A CA  1 
ATOM   48   C  C   . LEU A 1 8   ? -9.908  3.372   0.113   1.00 12.58  ? 8    LEU A C   1 
ATOM   49   O  O   . LEU A 1 8   ? -8.825  3.565   -0.455  1.00 13.45  ? 8    LEU A O   1 
ATOM   50   C  CB  . LEU A 1 8   ? -9.345  1.812   1.978   1.00 11.52  ? 8    LEU A CB  1 
ATOM   51   C  CG  . LEU A 1 8   ? -9.594  0.587   2.871   1.00 11.79  ? 8    LEU A CG  1 
ATOM   52   C  CD1 . LEU A 1 8   ? -8.542  0.440   3.988   1.00 14.12  ? 8    LEU A CD1 1 
ATOM   53   C  CD2 . LEU A 1 8   ? -10.954 0.645   3.477   1.00 13.83  ? 8    LEU A CD2 1 
ATOM   54   N  N   . LYS A 1 9   ? -10.862 4.291   0.185   1.00 13.65  ? 9    LYS A N   1 
ATOM   55   C  CA  . LYS A 1 9   ? -10.657 5.660   -0.291  1.00 15.16  ? 9    LYS A CA  1 
ATOM   56   C  C   . LYS A 1 9   ? -11.353 6.633   0.668   1.00 15.67  ? 9    LYS A C   1 
ATOM   57   O  O   . LYS A 1 9   ? -12.347 6.282   1.311   1.00 15.85  ? 9    LYS A O   1 
ATOM   58   C  CB  . LYS A 1 9   ? -11.233 5.881   -1.699  1.00 16.27  ? 9    LYS A CB  1 
ATOM   59   C  CG  . LYS A 1 9   ? -11.040 4.777   -2.721  0.50 17.82  ? 9    LYS A CG  1 
ATOM   60   C  CD  . LYS A 1 9   ? -11.947 5.030   -3.922  0.50 20.21  ? 9    LYS A CD  1 
ATOM   61   C  CE  . LYS A 1 9   ? -11.750 4.016   -5.037  0.50 21.14  ? 9    LYS A CE  1 
ATOM   62   N  NZ  . LYS A 1 9   ? -10.449 4.195   -5.734  0.50 22.33  ? 9    LYS A NZ  1 
ATOM   63   N  N   . GLY A 1 10  ? -10.848 7.863   0.727   1.00 17.88  ? 10   GLY A N   1 
ATOM   64   C  CA  . GLY A 1 10  ? -11.486 8.922   1.503   1.00 18.52  ? 10   GLY A CA  1 
ATOM   65   C  C   . GLY A 1 10  ? -11.256 10.297  0.902   1.00 20.67  ? 10   GLY A C   1 
ATOM   66   O  O   . GLY A 1 10  ? -10.828 10.419  -0.245  1.00 21.80  ? 10   GLY A O   1 
ATOM   67   N  N   . ASP A 1 11  ? -11.551 11.327  1.691   1.00 22.00  ? 11   ASP A N   1 
ATOM   68   C  CA  . ASP A 1 11  ? -11.371 12.728  1.267   1.00 23.47  ? 11   ASP A CA  1 
ATOM   69   C  C   . ASP A 1 11  ? -9.909  13.171  1.290   1.00 24.15  ? 11   ASP A C   1 
ATOM   70   O  O   . ASP A 1 11  ? -9.534  14.145  0.624   1.00 26.02  ? 11   ASP A O   1 
ATOM   71   C  CB  . ASP A 1 11  ? -12.212 13.655  2.148   1.00 24.59  ? 11   ASP A CB  1 
ATOM   72   C  CG  . ASP A 1 11  ? -13.694 13.399  2.005   0.50 25.35  ? 11   ASP A CG  1 
ATOM   73   O  OD1 . ASP A 1 11  ? -14.194 13.459  0.863   0.50 28.33  ? 11   ASP A OD1 1 
ATOM   74   O  OD2 . ASP A 1 11  ? -14.357 13.128  3.031   0.50 27.26  ? 11   ASP A OD2 1 
ATOM   75   N  N   . GLY A 1 12  ? -9.088  12.447  2.044   1.00 23.07  ? 12   GLY A N   1 
ATOM   76   C  CA  . GLY A 1 12  ? -7.687  12.764  2.203   1.00 23.22  ? 12   GLY A CA  1 
ATOM   77   C  C   . GLY A 1 12  ? -6.792  11.784  1.479   1.00 22.34  ? 12   GLY A C   1 
ATOM   78   O  O   . GLY A 1 12  ? -7.219  11.147  0.510   1.00 22.39  ? 12   GLY A O   1 
ATOM   79   N  N   . PRO A 1 13  ? -5.539  11.647  1.949   1.00 21.61  ? 13   PRO A N   1 
ATOM   80   C  CA  . PRO A 1 13  ? -4.537  10.834  1.263   1.00 20.89  ? 13   PRO A CA  1 
ATOM   81   C  C   . PRO A 1 13  ? -4.579  9.332   1.559   1.00 19.50  ? 13   PRO A C   1 
ATOM   82   O  O   . PRO A 1 13  ? -3.781  8.580   0.985   1.00 19.08  ? 13   PRO A O   1 
ATOM   83   C  CB  . PRO A 1 13  ? -3.219  11.422  1.787   1.00 21.91  ? 13   PRO A CB  1 
ATOM   84   C  CG  . PRO A 1 13  ? -3.540  11.873  3.153   1.00 21.91  ? 13   PRO A CG  1 
ATOM   85   C  CD  . PRO A 1 13  ? -4.966  12.341  3.118   1.00 22.01  ? 13   PRO A CD  1 
ATOM   86   N  N   . VAL A 1 14  ? -5.466  8.895   2.450   1.00 17.83  ? 14   VAL A N   1 
ATOM   87   C  CA  . VAL A 1 14  ? -5.469  7.505   2.886   1.00 16.60  ? 14   VAL A CA  1 
ATOM   88   C  C   . VAL A 1 14  ? -6.106  6.638   1.824   1.00 16.06  ? 14   VAL A C   1 
ATOM   89   O  O   . VAL A 1 14  ? -7.217  6.910   1.362   1.00 16.72  ? 14   VAL A O   1 
ATOM   90   C  CB  . VAL A 1 14  ? -6.166  7.307   4.247   1.00 16.15  ? 14   VAL A CB  1 
ATOM   91   C  CG1 . VAL A 1 14  ? -6.139  5.836   4.657   1.00 14.41  ? 14   VAL A CG1 1 
ATOM   92   C  CG2 . VAL A 1 14  ? -5.467  8.171   5.304   1.00 17.03  ? 14   VAL A CG2 1 
ATOM   93   N  N   . GLN A 1 15  ? -5.382  5.603   1.416   1.00 15.67  ? 15   GLN A N   1 
ATOM   94   C  CA  . GLN A 1 15  ? -5.893  4.658   0.442   1.00 15.36  ? 15   GLN A CA  1 
ATOM   95   C  C   . GLN A 1 15  ? -5.222  3.298   0.556   1.00 14.52  ? 15   GLN A C   1 
ATOM   96   O  O   . GLN A 1 15  ? -4.076  3.163   1.006   1.00 15.06  ? 15   GLN A O   1 
ATOM   97   C  CB  . GLN A 1 15  ? -5.734  5.214   -0.969  1.00 17.07  ? 15   GLN A CB  1 
ATOM   98   C  CG  . GLN A 1 15  ? -4.319  5.413   -1.427  1.00 20.18  ? 15   GLN A CG  1 
ATOM   99   C  CD  . GLN A 1 15  ? -4.243  6.079   -2.805  1.00 25.61  ? 15   GLN A CD  1 
ATOM   100  O  OE1 . GLN A 1 15  ? -4.980  5.725   -3.720  1.00 30.60  ? 15   GLN A OE1 1 
ATOM   101  N  NE2 . GLN A 1 15  ? -3.354  7.048   -2.947  1.00 27.82  ? 15   GLN A NE2 1 
ATOM   102  N  N   . GLY A 1 16  ? -5.942  2.267   0.154   1.00 13.84  ? 16   GLY A N   1 
ATOM   103  C  CA  . GLY A 1 16  ? -5.351  0.946   0.171   1.00 13.07  ? 16   GLY A CA  1 
ATOM   104  C  C   . GLY A 1 16  ? -6.263  -0.079  -0.433  1.00 12.11  ? 16   GLY A C   1 
ATOM   105  O  O   . GLY A 1 16  ? -7.420  0.206   -0.713  1.00 11.96  ? 16   GLY A O   1 
ATOM   106  N  N   . ILE A 1 17  ? -5.696  -1.252  -0.669  1.00 12.05  ? 17   ILE A N   1 
ATOM   107  C  CA  . ILE A 1 17  ? -6.395  -2.418  -1.194  1.00 11.24  ? 17   ILE A CA  1 
ATOM   108  C  C   . ILE A 1 17  ? -6.268  -3.522  -0.151  1.00 10.42  ? 17   ILE A C   1 
ATOM   109  O  O   . ILE A 1 17  ? -5.146  -3.959  0.186   1.00 11.53  ? 17   ILE A O   1 
ATOM   110  C  CB  . ILE A 1 17  ? -5.797  -2.899  -2.534  1.00 12.23  ? 17   ILE A CB  1 
ATOM   111  C  CG1 . ILE A 1 17  ? -5.789  -1.762  -3.581  1.00 14.89  ? 17   ILE A CG1 1 
ATOM   112  C  CG2 . ILE A 1 17  ? -6.527  -4.168  -3.025  1.00 13.18  ? 17   ILE A CG2 1 
ATOM   113  C  CD1 . ILE A 1 17  ? -7.120  -1.486  -4.239  1.00 16.79  ? 17   ILE A CD1 1 
ATOM   114  N  N   . ILE A 1 18  ? -7.406  -3.983  0.359   1.00 9.04   ? 18   ILE A N   1 
ATOM   115  C  CA  . ILE A 1 18  ? -7.424  -5.032  1.377   1.00 8.14   ? 18   ILE A CA  1 
ATOM   116  C  C   . ILE A 1 18  ? -8.094  -6.271  0.816   1.00 8.38   ? 18   ILE A C   1 
ATOM   117  O  O   . ILE A 1 18  ? -9.194  -6.181  0.265   1.00 9.36   ? 18   ILE A O   1 
ATOM   118  C  CB  . ILE A 1 18  ? -8.186  -4.553  2.652   1.00 8.21   ? 18   ILE A CB  1 
ATOM   119  C  CG1 . ILE A 1 18  ? -7.534  -3.273  3.226   1.00 9.11   ? 18   ILE A CG1 1 
ATOM   120  C  CG2 . ILE A 1 18  ? -8.268  -5.658  3.693   1.00 8.68   ? 18   ILE A CG2 1 
ATOM   121  C  CD1 . ILE A 1 18  ? -6.056  -3.410  3.598   1.00 10.96  ? 18   ILE A CD1 1 
ATOM   122  N  N   . ASN A 1 19  ? -7.424  -7.414  0.974   1.00 8.24   ? 19   ASN A N   1 
ATOM   123  C  CA  . ASN A 1 19  ? -7.911  -8.710  0.533   1.00 8.11   ? 19   ASN A CA  1 
ATOM   124  C  C   . ASN A 1 19  ? -8.424  -9.526  1.708   1.00 7.75   ? 19   ASN A C   1 
ATOM   125  O  O   . ASN A 1 19  ? -7.919  -9.403  2.834   1.00 8.16   ? 19   ASN A O   1 
ATOM   126  C  CB  . ASN A 1 19  ? -6.800  -9.494  -0.137  1.00 9.35   ? 19   ASN A CB  1 
ATOM   127  C  CG  . ASN A 1 19  ? -6.608  -9.125  -1.596  1.00 9.48   ? 19   ASN A CG  1 
ATOM   128  O  OD1 . ASN A 1 19  ? -6.118  -8.043  -1.910  1.00 13.06  ? 19   ASN A OD1 1 
ATOM   129  N  ND2 . ASN A 1 19  ? -6.987  -10.039 -2.506  1.00 9.46   ? 19   ASN A ND2 1 
ATOM   130  N  N   . PHE A 1 20  ? -9.401  -10.375 1.415   1.00 8.28   ? 20   PHE A N   1 
ATOM   131  C  CA  . PHE A 1 20  ? -9.970  -11.318 2.353   1.00 8.63   ? 20   PHE A CA  1 
ATOM   132  C  C   . PHE A 1 20  ? -9.983  -12.698 1.700   1.00 9.32   ? 20   PHE A C   1 
ATOM   133  O  O   . PHE A 1 20  ? -10.237 -12.815 0.503   1.00 9.07   ? 20   PHE A O   1 
ATOM   134  C  CB  . PHE A 1 20  ? -11.423 -10.961 2.710   1.00 8.93   ? 20   PHE A CB  1 
ATOM   135  C  CG  . PHE A 1 20  ? -11.601 -9.609  3.350   1.00 8.78   ? 20   PHE A CG  1 
ATOM   136  C  CD1 . PHE A 1 20  ? -11.551 -8.447  2.593   1.00 10.67  ? 20   PHE A CD1 1 
ATOM   137  C  CD2 . PHE A 1 20  ? -11.884 -9.509  4.696   1.00 10.74  ? 20   PHE A CD2 1 
ATOM   138  C  CE1 . PHE A 1 20  ? -11.726 -7.219  3.182   1.00 10.22  ? 20   PHE A CE1 1 
ATOM   139  C  CE2 . PHE A 1 20  ? -12.069 -8.278  5.286   1.00 9.59   ? 20   PHE A CE2 1 
ATOM   140  C  CZ  . PHE A 1 20  ? -11.989 -7.130  4.528   1.00 8.99   ? 20   PHE A CZ  1 
ATOM   141  N  N   . GLU A 1 21  ? -9.753  -13.746 2.480   1.00 9.71   ? 21   GLU A N   1 
ATOM   142  C  CA  . GLU A 1 21  ? -9.920  -15.113 1.974   1.00 10.49  ? 21   GLU A CA  1 
ATOM   143  C  C   . GLU A 1 21  ? -10.411 -16.008 3.082   1.00 10.69  ? 21   GLU A C   1 
ATOM   144  O  O   . GLU A 1 21  ? -9.930  -15.925 4.199   1.00 10.24  ? 21   GLU A O   1 
ATOM   145  C  CB  . GLU A 1 21  ? -8.619  -15.690 1.376   1.00 11.54  ? 21   GLU A CB  1 
ATOM   146  C  CG  . GLU A 1 21  ? -8.823  -17.081 0.729   1.00 15.02  ? 21   GLU A CG  1 
ATOM   147  C  CD  . GLU A 1 21  ? -7.771  -17.432 -0.310  1.00 19.64  ? 21   GLU A CD  1 
ATOM   148  O  OE1 . GLU A 1 21  ? -6.703  -16.790 -0.322  1.00 24.08  ? 21   GLU A OE1 1 
ATOM   149  O  OE2 . GLU A 1 21  ? -8.007  -18.350 -1.126  1.00 21.89  ? 21   GLU A OE2 1 
ATOM   150  N  N   . GLN A 1 22  ? -11.344 -16.890 2.738   1.00 11.08  ? 22   GLN A N   1 
ATOM   151  C  CA  . GLN A 1 22  ? -11.888 -17.862 3.670   1.00 11.85  ? 22   GLN A CA  1 
ATOM   152  C  C   . GLN A 1 22  ? -12.014 -19.185 2.933   1.00 14.05  ? 22   GLN A C   1 
ATOM   153  O  O   . GLN A 1 22  ? -12.736 -19.281 1.945   1.00 13.51  ? 22   GLN A O   1 
ATOM   154  C  CB  . GLN A 1 22  ? -13.242 -17.378 4.176   1.00 11.38  ? 22   GLN A CB  1 
ATOM   155  C  CG  . GLN A 1 22  ? -13.840 -18.221 5.277   1.00 11.23  ? 22   GLN A CG  1 
ATOM   156  C  CD  . GLN A 1 22  ? -15.216 -17.723 5.724   1.00 10.41  ? 22   GLN A CD  1 
ATOM   157  O  OE1 . GLN A 1 22  ? -15.940 -17.081 4.947   1.00 10.11  ? 22   GLN A OE1 1 
ATOM   158  N  NE2 . GLN A 1 22  ? -15.590 -18.031 6.975   1.00 10.09  ? 22   GLN A NE2 1 
ATOM   159  N  N   . LYS A 1 23  ? -11.306 -20.208 3.400   1.00 16.63  ? 23   LYS A N   1 
ATOM   160  C  CA  . LYS A 1 23  ? -11.270 -21.471 2.670   1.00 19.70  ? 23   LYS A CA  1 
ATOM   161  C  C   . LYS A 1 23  ? -12.539 -22.277 2.869   1.00 21.38  ? 23   LYS A C   1 
ATOM   162  O  O   . LYS A 1 23  ? -13.138 -22.707 1.888   1.00 24.28  ? 23   LYS A O   1 
ATOM   163  C  CB  . LYS A 1 23  ? -10.017 -22.264 3.027   1.00 20.70  ? 23   LYS A CB  1 
ATOM   164  C  CG  . LYS A 1 23  ? -8.761  -21.526 2.607   1.00 22.18  ? 23   LYS A CG  1 
ATOM   165  C  CD  . LYS A 1 23  ? -7.629  -22.437 2.132   1.00 23.53  ? 23   LYS A CD  1 
ATOM   166  C  CE  . LYS A 1 23  ? -6.367  -21.635 1.724   1.00 23.49  ? 23   LYS A CE  1 
ATOM   167  N  NZ  . LYS A 1 23  ? -6.110  -21.434 0.233   1.00 17.22  ? 23   LYS A NZ  1 
ATOM   168  N  N   . GLU A 1 24  ? -12.973 -22.448 4.111   1.00 21.98  ? 24   GLU A N   1 
ATOM   169  C  CA  . GLU A 1 24  ? -14.212 -23.162 4.407   1.00 23.02  ? 24   GLU A CA  1 
ATOM   170  C  C   . GLU A 1 24  ? -15.252 -22.133 4.825   1.00 21.61  ? 24   GLU A C   1 
ATOM   171  O  O   . GLU A 1 24  ? -14.894 -21.091 5.368   1.00 20.59  ? 24   GLU A O   1 
ATOM   172  C  CB  . GLU A 1 24  ? -14.010 -24.167 5.550   1.00 24.25  ? 24   GLU A CB  1 
ATOM   173  C  CG  A GLU A 1 24  ? -12.890 -25.185 5.321   0.50 25.90  ? 24   GLU A CG  1 
ATOM   174  C  CG  B GLU A 1 24  ? -13.023 -25.301 5.250   0.50 26.30  ? 24   GLU A CG  1 
ATOM   175  C  CD  A GLU A 1 24  ? -11.481 -24.623 5.581   0.50 26.65  ? 24   GLU A CD  1 
ATOM   176  C  CD  B GLU A 1 24  ? -13.603 -26.402 4.349   0.50 28.93  ? 24   GLU A CD  1 
ATOM   177  O  OE1 A GLU A 1 24  ? -11.336 -23.565 6.249   0.50 25.20  ? 24   GLU A OE1 1 
ATOM   178  O  OE1 B GLU A 1 24  ? -14.820 -26.702 4.427   0.50 29.91  ? 24   GLU A OE1 1 
ATOM   179  O  OE2 A GLU A 1 24  ? -10.508 -25.251 5.108   0.50 29.42  ? 24   GLU A OE2 1 
ATOM   180  O  OE2 B GLU A 1 24  ? -12.826 -26.981 3.561   0.50 31.06  ? 24   GLU A OE2 1 
ATOM   181  N  N   . SER A 1 25  ? -16.534 -22.432 4.610   1.00 21.41  ? 25   SER A N   1 
ATOM   182  C  CA  . SER A 1 25  ? -17.615 -21.479 4.903   1.00 20.57  ? 25   SER A CA  1 
ATOM   183  C  C   . SER A 1 25  ? -17.699 -21.100 6.389   1.00 19.59  ? 25   SER A C   1 
ATOM   184  O  O   . SER A 1 25  ? -18.252 -20.057 6.730   1.00 19.75  ? 25   SER A O   1 
ATOM   185  C  CB  . SER A 1 25  ? -18.965 -22.031 4.429   1.00 21.80  ? 25   SER A CB  1 
ATOM   186  O  OG  . SER A 1 25  ? -19.263 -23.243 5.096   1.00 23.87  ? 25   SER A OG  1 
ATOM   187  N  N   . ASN A 1 26  ? -17.164 -21.963 7.258   1.00 18.34  ? 26   ASN A N   1 
ATOM   188  C  CA  . ASN A 1 26  ? -17.050 -21.701 8.698   1.00 17.89  ? 26   ASN A CA  1 
ATOM   189  C  C   . ASN A 1 26  ? -15.576 -21.710 9.157   1.00 17.02  ? 26   ASN A C   1 
ATOM   190  O  O   . ASN A 1 26  ? -15.276 -21.980 10.315  1.00 18.13  ? 26   ASN A O   1 
ATOM   191  C  CB  . ASN A 1 26  ? -17.854 -22.740 9.496   1.00 18.62  ? 26   ASN A CB  1 
ATOM   192  C  CG  . ASN A 1 26  ? -17.408 -24.168 9.216   1.00 19.53  ? 26   ASN A CG  1 
ATOM   193  O  OD1 . ASN A 1 26  ? -16.542 -24.393 8.382   1.00 20.96  ? 26   ASN A OD1 1 
ATOM   194  N  ND2 . ASN A 1 26  ? -18.004 -25.138 9.909   1.00 21.24  ? 26   ASN A ND2 1 
ATOM   195  N  N   . GLY A 1 27  ? -14.672 -21.403 8.232   1.00 16.00  ? 27   GLY A N   1 
ATOM   196  C  CA  . GLY A 1 27  ? -13.245 -21.338 8.523   1.00 14.85  ? 27   GLY A CA  1 
ATOM   197  C  C   . GLY A 1 27  ? -12.830 -19.941 8.943   1.00 13.14  ? 27   GLY A C   1 
ATOM   198  O  O   . GLY A 1 27  ? -13.602 -18.985 8.825   1.00 11.38  ? 27   GLY A O   1 
ATOM   199  N  N   . PRO A 1 28  ? -11.594 -19.801 9.421   1.00 12.59  ? 28   PRO A N   1 
ATOM   200  C  CA  . PRO A 1 28  ? -11.091 -18.464 9.683   1.00 12.15  ? 28   PRO A CA  1 
ATOM   201  C  C   . PRO A 1 28  ? -10.985 -17.634 8.412   1.00 11.20  ? 28   PRO A C   1 
ATOM   202  O  O   . PRO A 1 28  ? -10.791 -18.175 7.308   1.00 11.02  ? 28   PRO A O   1 
ATOM   203  C  CB  . PRO A 1 28  ? -9.685  -18.715 10.224  1.00 12.30  ? 28   PRO A CB  1 
ATOM   204  C  CG  . PRO A 1 28  ? -9.302  -20.025 9.715   1.00 13.80  ? 28   PRO A CG  1 
ATOM   205  C  CD  . PRO A 1 28  ? -10.556 -20.829 9.605   1.00 14.27  ? 28   PRO A CD  1 
ATOM   206  N  N   . VAL A 1 29  ? -11.089 -16.320 8.571   1.00 10.79  ? 29   VAL A N   1 
ATOM   207  C  CA  . VAL A 1 29  ? -10.875 -15.392 7.471   1.00 10.45  ? 29   VAL A CA  1 
ATOM   208  C  C   . VAL A 1 29  ? -9.516  -14.754 7.619   1.00 10.65  ? 29   VAL A C   1 
ATOM   209  O  O   . VAL A 1 29  ? -9.181  -14.224 8.680   1.00 10.24  ? 29   VAL A O   1 
ATOM   210  C  CB  . VAL A 1 29  ? -11.951 -14.317 7.408   1.00 9.95   ? 29   VAL A CB  1 
ATOM   211  C  CG1 . VAL A 1 29  ? -11.685 -13.375 6.215   1.00 9.57   ? 29   VAL A CG1 1 
ATOM   212  C  CG2 . VAL A 1 29  ? -13.350 -14.957 7.330   1.00 11.15  ? 29   VAL A CG2 1 
ATOM   213  N  N   . LYS A 1 30  ? -8.746  -14.789 6.536   1.00 10.17  ? 30   LYS A N   1 
ATOM   214  C  CA  . LYS A 1 30  ? -7.460  -14.106 6.490   1.00 10.89  ? 30   LYS A CA  1 
ATOM   215  C  C   . LYS A 1 30  ? -7.643  -12.777 5.773   1.00 9.72   ? 30   LYS A C   1 
ATOM   216  O  O   . LYS A 1 30  ? -8.373  -12.695 4.785   1.00 10.36  ? 30   LYS A O   1 
ATOM   217  C  CB  . LYS A 1 30  ? -6.415  -14.982 5.817   1.00 11.72  ? 30   LYS A CB  1 
ATOM   218  C  CG  . LYS A 1 30  ? -6.030  -16.219 6.641   0.50 14.06  ? 30   LYS A CG  1 
ATOM   219  C  CD  . LYS A 1 30  ? -4.608  -16.643 6.345   0.50 17.63  ? 30   LYS A CD  1 
ATOM   220  C  CE  . LYS A 1 30  ? -4.226  -17.974 6.987   0.50 20.10  ? 30   LYS A CE  1 
ATOM   221  N  NZ  . LYS A 1 30  ? -2.805  -18.323 6.664   0.50 21.44  ? 30   LYS A NZ  1 
ATOM   222  N  N   . VAL A 1 31  ? -7.008  -11.736 6.311   1.00 9.60   ? 31   VAL A N   1 
ATOM   223  C  CA  . VAL A 1 31  ? -7.128  -10.362 5.808   1.00 9.66   ? 31   VAL A CA  1 
ATOM   224  C  C   . VAL A 1 31  ? -5.728  -9.781  5.628   1.00 10.08  ? 31   VAL A C   1 
ATOM   225  O  O   . VAL A 1 31  ? -4.869  -9.896  6.516   1.00 10.80  ? 31   VAL A O   1 
ATOM   226  C  CB  . VAL A 1 31  ? -7.940  -9.453  6.755   1.00 9.57   ? 31   VAL A CB  1 
ATOM   227  C  CG1 . VAL A 1 31  ? -8.262  -8.139  6.054   1.00 9.66   ? 31   VAL A CG1 1 
ATOM   228  C  CG2 . VAL A 1 31  ? -9.222  -10.147 7.220   1.00 9.45   ? 31   VAL A CG2 1 
ATOM   229  N  N   . TRP A 1 32  ? -5.481  -9.151  4.481   1.00 9.70   ? 32   TRP A N   1 
ATOM   230  C  CA  . TRP A 1 32  ? -4.161  -8.608  4.228   1.00 9.64   ? 32   TRP A CA  1 
ATOM   231  C  C   . TRP A 1 32  ? -4.198  -7.481  3.228   1.00 10.31  ? 32   TRP A C   1 
ATOM   232  O  O   . TRP A 1 32  ? -5.197  -7.281  2.562   1.00 11.04  ? 32   TRP A O   1 
ATOM   233  C  CB  . TRP A 1 32  ? -3.192  -9.692  3.748   1.00 9.96   ? 32   TRP A CB  1 
ATOM   234  C  CG  . TRP A 1 32  ? -3.389  -10.167 2.345   1.00 8.94   ? 32   TRP A CG  1 
ATOM   235  C  CD1 . TRP A 1 32  ? -2.763  -9.698  1.208   1.00 10.06  ? 32   TRP A CD1 1 
ATOM   236  C  CD2 . TRP A 1 32  ? -4.272  -11.201 1.911   1.00 9.08   ? 32   TRP A CD2 1 
ATOM   237  N  NE1 . TRP A 1 32  ? -3.210  -10.390 0.108   1.00 10.83  ? 32   TRP A NE1 1 
ATOM   238  C  CE2 . TRP A 1 32  ? -4.133  -11.317 0.506   1.00 10.21  ? 32   TRP A CE2 1 
ATOM   239  C  CE3 . TRP A 1 32  ? -5.165  -12.049 2.573   1.00 9.47   ? 32   TRP A CE3 1 
ATOM   240  C  CZ2 . TRP A 1 32  ? -4.848  -12.262 -0.240  1.00 9.79   ? 32   TRP A CZ2 1 
ATOM   241  C  CZ3 . TRP A 1 32  ? -5.888  -12.971 1.828   1.00 11.21  ? 32   TRP A CZ3 1 
ATOM   242  C  CH2 . TRP A 1 32  ? -5.726  -13.074 0.445   1.00 10.21  ? 32   TRP A CH2 1 
ATOM   243  N  N   . GLY A 1 33  ? -3.095  -6.747  3.154   1.00 11.08  ? 33   GLY A N   1 
ATOM   244  C  CA  . GLY A 1 33  ? -2.948  -5.642  2.218   1.00 11.74  ? 33   GLY A CA  1 
ATOM   245  C  C   . GLY A 1 33  ? -2.283  -4.453  2.880   1.00 13.03  ? 33   GLY A C   1 
ATOM   246  O  O   . GLY A 1 33  ? -1.969  -4.487  4.058   1.00 15.65  ? 33   GLY A O   1 
ATOM   247  N  N   . SER A 1 34  ? -2.021  -3.408  2.113   1.00 14.27  ? 34   SER A N   1 
ATOM   248  C  CA  . SER A 1 34  ? -1.344  -2.228  2.652   1.00 14.96  ? 34   SER A CA  1 
ATOM   249  C  C   . SER A 1 34  ? -2.234  -1.002  2.536   1.00 14.43  ? 34   SER A C   1 
ATOM   250  O  O   . SER A 1 34  ? -3.032  -0.893  1.608   1.00 15.44  ? 34   SER A O   1 
ATOM   251  C  CB  . SER A 1 34  ? -0.013  -1.984  1.934   1.00 16.30  ? 34   SER A CB  1 
ATOM   252  O  OG  . SER A 1 34  ? 0.915   -3.028  2.190   1.00 19.15  ? 34   SER A OG  1 
ATOM   253  N  N   . ILE A 1 35  ? -2.131  -0.115  3.518   1.00 13.10  ? 35   ILE A N   1 
ATOM   254  C  CA  . ILE A 1 35  ? -2.828  1.176   3.501   1.00 13.19  ? 35   ILE A CA  1 
ATOM   255  C  C   . ILE A 1 35  ? -1.743  2.228   3.581   1.00 13.48  ? 35   ILE A C   1 
ATOM   256  O  O   . ILE A 1 35  ? -0.848  2.138   4.440   1.00 13.50  ? 35   ILE A O   1 
ATOM   257  C  CB  . ILE A 1 35  ? -3.774  1.317   4.710   1.00 13.06  ? 35   ILE A CB  1 
ATOM   258  C  CG1 . ILE A 1 35  ? -4.659  0.070   4.844   1.00 12.09  ? 35   ILE A CG1 1 
ATOM   259  C  CG2 . ILE A 1 35  ? -4.595  2.612   4.610   1.00 13.20  ? 35   ILE A CG2 1 
ATOM   260  C  CD1 . ILE A 1 35  ? -5.599  0.118   6.022   1.00 12.90  ? 35   ILE A CD1 1 
ATOM   261  N  N   . LYS A 1 36  ? -1.801  3.220   2.686   1.00 13.67  ? 36   LYS A N   1 
ATOM   262  C  CA  . LYS A 1 36  ? -0.831  4.303   2.676   1.00 14.03  ? 36   LYS A CA  1 
ATOM   263  C  C   . LYS A 1 36  ? -1.498  5.632   2.996   1.00 14.09  ? 36   LYS A C   1 
ATOM   264  O  O   . LYS A 1 36  ? -2.726  5.737   3.028   1.00 14.01  ? 36   LYS A O   1 
ATOM   265  C  CB  . LYS A 1 36  ? -0.097  4.376   1.343   1.00 14.95  ? 36   LYS A CB  1 
ATOM   266  C  CG  . LYS A 1 36  ? -0.938  4.625   0.121   1.00 16.68  ? 36   LYS A CG  1 
ATOM   267  C  CD  . LYS A 1 36  ? -0.043  4.876   -1.086  1.00 21.28  ? 36   LYS A CD  1 
ATOM   268  C  CE  . LYS A 1 36  ? -0.745  4.583   -2.395  1.00 24.12  ? 36   LYS A CE  1 
ATOM   269  N  NZ  . LYS A 1 36  ? 0.220   4.636   -3.540  1.00 27.40  ? 36   LYS A NZ  1 
ATOM   270  N  N   . GLY A 1 37  ? -0.671  6.630   3.267   1.00 13.90  ? 37   GLY A N   1 
ATOM   271  C  CA  . GLY A 1 37  ? -1.152  7.961   3.561   1.00 15.47  ? 37   GLY A CA  1 
ATOM   272  C  C   . GLY A 1 37  ? -1.521  8.203   5.006   1.00 15.72  ? 37   GLY A C   1 
ATOM   273  O  O   . GLY A 1 37  ? -2.084  9.245   5.310   1.00 17.32  ? 37   GLY A O   1 
ATOM   274  N  N   . LEU A 1 38  ? -1.212  7.256   5.895   1.00 15.46  ? 38   LEU A N   1 
ATOM   275  C  CA  . LEU A 1 38  ? -1.577  7.347   7.314   1.00 15.14  ? 38   LEU A CA  1 
ATOM   276  C  C   . LEU A 1 38  ? -0.517  8.083   8.128   1.00 16.31  ? 38   LEU A C   1 
ATOM   277  O  O   . LEU A 1 38  ? 0.650   8.101   7.767   1.00 16.43  ? 38   LEU A O   1 
ATOM   278  C  CB  . LEU A 1 38  ? -1.728  5.954   7.918   1.00 14.75  ? 38   LEU A CB  1 
ATOM   279  C  CG  . LEU A 1 38  ? -2.897  5.130   7.398   1.00 14.13  ? 38   LEU A CG  1 
ATOM   280  C  CD1 . LEU A 1 38  ? -2.710  3.620   7.688   1.00 12.70  ? 38   LEU A CD1 1 
ATOM   281  C  CD2 . LEU A 1 38  ? -4.185  5.659   8.000   1.00 13.08  ? 38   LEU A CD2 1 
ATOM   282  N  N   . THR A 1 39  ? -0.928  8.665   9.247   1.00 16.43  ? 39   THR A N   1 
ATOM   283  C  CA  . THR A 1 39  ? 0.028   9.166   10.229  1.00 17.84  ? 39   THR A CA  1 
ATOM   284  C  C   . THR A 1 39  ? 0.668   7.974   10.933  1.00 17.73  ? 39   THR A C   1 
ATOM   285  O  O   . THR A 1 39  ? 0.020   6.955   11.144  1.00 17.13  ? 39   THR A O   1 
ATOM   286  C  CB  . THR A 1 39  ? -0.643  10.091  11.251  1.00 17.98  ? 39   THR A CB  1 
ATOM   287  O  OG1 . THR A 1 39  ? -1.741  9.419   11.881  1.00 18.98  ? 39   THR A OG1 1 
ATOM   288  C  CG2 . THR A 1 39  ? -1.141  11.342  10.556  1.00 18.96  ? 39   THR A CG2 1 
ATOM   289  N  N   . GLU A 1 40  ? 1.947   8.100   11.285  1.00 18.73  ? 40   GLU A N   1 
ATOM   290  C  CA  . GLU A 1 40  ? 2.652   7.038   12.000  1.00 18.99  ? 40   GLU A CA  1 
ATOM   291  C  C   . GLU A 1 40  ? 1.906   6.640   13.281  1.00 18.29  ? 40   GLU A C   1 
ATOM   292  O  O   . GLU A 1 40  ? 1.456   7.511   14.010  1.00 18.74  ? 40   GLU A O   1 
ATOM   293  C  CB  . GLU A 1 40  ? 4.057   7.511   12.359  1.00 20.39  ? 40   GLU A CB  1 
ATOM   294  C  CG  . GLU A 1 40  ? 4.938   6.424   12.923  1.00 21.82  ? 40   GLU A CG  1 
ATOM   295  C  CD  . GLU A 1 40  ? 6.327   6.926   13.286  1.00 25.21  ? 40   GLU A CD  1 
ATOM   296  O  OE1 . GLU A 1 40  ? 6.540   8.160   13.266  1.00 26.92  ? 40   GLU A OE1 1 
ATOM   297  O  OE2 . GLU A 1 40  ? 7.204   6.080   13.585  1.00 28.42  ? 40   GLU A OE2 1 
ATOM   298  N  N   . GLY A 1 41  ? 1.807   5.337   13.547  1.00 17.65  ? 41   GLY A N   1 
ATOM   299  C  CA  . GLY A 1 41  ? 1.161   4.821   14.744  1.00 17.54  ? 41   GLY A CA  1 
ATOM   300  C  C   . GLY A 1 41  ? -0.074  3.973   14.486  1.00 16.48  ? 41   GLY A C   1 
ATOM   301  O  O   . GLY A 1 41  ? -0.290  3.479   13.378  1.00 15.89  ? 41   GLY A O   1 
ATOM   302  N  N   . LEU A 1 42  ? -0.873  3.802   15.540  1.00 16.35  ? 42   LEU A N   1 
ATOM   303  C  CA  . LEU A 1 42  ? -2.032  2.917   15.536  1.00 15.33  ? 42   LEU A CA  1 
ATOM   304  C  C   . LEU A 1 42  ? -3.249  3.554   14.898  1.00 13.93  ? 42   LEU A C   1 
ATOM   305  O  O   . LEU A 1 42  ? -3.530  4.731   15.100  1.00 14.98  ? 42   LEU A O   1 
ATOM   306  C  CB  . LEU A 1 42  ? -2.405  2.521   16.970  1.00 15.69  ? 42   LEU A CB  1 
ATOM   307  C  CG  . LEU A 1 42  ? -1.416  1.653   17.733  1.00 18.02  ? 42   LEU A CG  1 
ATOM   308  C  CD1 . LEU A 1 42  ? -1.868  1.525   19.190  1.00 19.36  ? 42   LEU A CD1 1 
ATOM   309  C  CD2 . LEU A 1 42  ? -1.256  0.294   17.087  1.00 18.31  ? 42   LEU A CD2 1 
ATOM   310  N  N   . HIS A 1 43  ? -3.975  2.760   14.125  1.00 12.68  ? 43   HIS A N   1 
ATOM   311  C  CA  . HIS A 1 43  ? -5.233  3.205   13.510  1.00 11.87  ? 43   HIS A CA  1 
ATOM   312  C  C   . HIS A 1 43  ? -6.302  2.134   13.640  1.00 10.86  ? 43   HIS A C   1 
ATOM   313  O  O   . HIS A 1 43  ? -6.068  0.996   13.287  1.00 10.44  ? 43   HIS A O   1 
ATOM   314  C  CB  . HIS A 1 43  ? -5.010  3.550   12.043  1.00 11.88  ? 43   HIS A CB  1 
ATOM   315  C  CG  . HIS A 1 43  ? -4.130  4.736   11.857  1.00 13.18  ? 43   HIS A CG  1 
ATOM   316  N  ND1 . HIS A 1 43  ? -4.627  6.018   11.790  1.00 13.93  ? 43   HIS A ND1 1 
ATOM   317  C  CD2 . HIS A 1 43  ? -2.785  4.846   11.767  1.00 13.83  ? 43   HIS A CD2 1 
ATOM   318  C  CE1 . HIS A 1 43  ? -3.626  6.872   11.669  1.00 15.10  ? 43   HIS A CE1 1 
ATOM   319  N  NE2 . HIS A 1 43  ? -2.496  6.185   11.645  1.00 15.02  ? 43   HIS A NE2 1 
ATOM   320  N  N   . GLY A 1 44  ? -7.484  2.518   14.132  1.00 10.19  ? 44   GLY A N   1 
ATOM   321  C  CA  . GLY A 1 44  ? -8.601  1.596   14.264  1.00 9.84   ? 44   GLY A CA  1 
ATOM   322  C  C   . GLY A 1 44  ? -8.981  1.026   12.916  1.00 9.32   ? 44   GLY A C   1 
ATOM   323  O  O   . GLY A 1 44  ? -8.956  1.724   11.928  1.00 10.45  ? 44   GLY A O   1 
ATOM   324  N  N   . PHE A 1 45  ? -9.339  -0.245  12.891  1.00 9.50   ? 45   PHE A N   1 
ATOM   325  C  CA  . PHE A 1 45  ? -9.647  -0.975  11.669  1.00 9.15   ? 45   PHE A CA  1 
ATOM   326  C  C   . PHE A 1 45  ? -10.896 -1.793  11.981  1.00 9.44   ? 45   PHE A C   1 
ATOM   327  O  O   . PHE A 1 45  ? -10.901 -2.620  12.882  1.00 10.15  ? 45   PHE A O   1 
ATOM   328  C  CB  . PHE A 1 45  ? -8.454  -1.891  11.375  1.00 9.17   ? 45   PHE A CB  1 
ATOM   329  C  CG  . PHE A 1 45  ? -8.464  -2.538  10.020  1.00 9.20   ? 45   PHE A CG  1 
ATOM   330  C  CD1 . PHE A 1 45  ? -8.480  -1.768  8.858   1.00 10.75  ? 45   PHE A CD1 1 
ATOM   331  C  CD2 . PHE A 1 45  ? -8.404  -3.925  9.902   1.00 10.98  ? 45   PHE A CD2 1 
ATOM   332  C  CE1 . PHE A 1 45  ? -8.435  -2.365  7.596   1.00 13.26  ? 45   PHE A CE1 1 
ATOM   333  C  CE2 . PHE A 1 45  ? -8.368  -4.533  8.627   1.00 11.31  ? 45   PHE A CE2 1 
ATOM   334  C  CZ  . PHE A 1 45  ? -8.377  -3.742  7.483   1.00 10.49  ? 45   PHE A CZ  1 
ATOM   335  N  N   . SER A 1 46  ? -11.967 -1.534  11.241  1.00 8.56   ? 46   SER A N   1 
ATOM   336  C  CA  . SER A 1 46  ? -13.265 -2.116  11.559  1.00 9.15   ? 46   SER A CA  1 
ATOM   337  C  C   . SER A 1 46  ? -14.110 -2.339  10.322  1.00 8.57   ? 46   SER A C   1 
ATOM   338  O  O   . SER A 1 46  ? -13.881 -1.759  9.260   1.00 8.85   ? 46   SER A O   1 
ATOM   339  C  CB  . SER A 1 46  ? -14.041 -1.218  12.530  1.00 10.42  ? 46   SER A CB  1 
ATOM   340  O  OG  . SER A 1 46  ? -14.306 0.050   11.948  1.00 12.81  ? 46   SER A OG  1 
ATOM   341  N  N   . VAL A 1 47  ? -15.097 -3.205  10.490  1.00 8.94   ? 47   VAL A N   1 
ATOM   342  C  CA  . VAL A 1 47  ? -16.156 -3.393  9.515   1.00 9.12   ? 47   VAL A CA  1 
ATOM   343  C  C   . VAL A 1 47  ? -17.384 -2.688  10.065  1.00 9.19   ? 47   VAL A C   1 
ATOM   344  O  O   . VAL A 1 47  ? -17.880 -3.022  11.142  1.00 9.44   ? 47   VAL A O   1 
ATOM   345  C  CB  . VAL A 1 47  ? -16.471 -4.880  9.281   1.00 8.81   ? 47   VAL A CB  1 
ATOM   346  C  CG1 . VAL A 1 47  ? -17.563 -5.030  8.196   1.00 9.46   ? 47   VAL A CG1 1 
ATOM   347  C  CG2 . VAL A 1 47  ? -15.200 -5.638  8.883   1.00 10.25  ? 47   VAL A CG2 1 
ATOM   348  N  N   . SER A 1 48  ? -17.853 -1.694  9.323   1.00 9.82   ? 48   SER A N   1 
ATOM   349  C  CA  . SER A 1 48  ? -19.068 -0.960  9.659   1.00 10.90  ? 48   SER A CA  1 
ATOM   350  C  C   . SER A 1 48  ? -20.290 -1.701  9.130   1.00 10.81  ? 48   SER A C   1 
ATOM   351  O  O   . SER A 1 48  ? -20.209 -2.443  8.134   1.00 10.03  ? 48   SER A O   1 
ATOM   352  C  CB  . SER A 1 48  ? -19.021 0.448   9.048   1.00 11.90  ? 48   SER A CB  1 
ATOM   353  O  OG  . SER A 1 48  ? -18.617 1.425   9.998   1.00 16.55  ? 48   SER A OG  1 
ATOM   354  N  N   . GLU A 1 49  ? -21.440 -1.483  9.776   1.00 10.69  ? 49   GLU A N   1 
ATOM   355  C  CA  . GLU A 1 49  ? -22.677 -2.105  9.319   1.00 11.20  ? 49   GLU A CA  1 
ATOM   356  C  C   . GLU A 1 49  ? -23.158 -1.586  7.954   1.00 10.89  ? 49   GLU A C   1 
ATOM   357  O  O   . GLU A 1 49  ? -23.877 -2.291  7.255   1.00 12.46  ? 49   GLU A O   1 
ATOM   358  C  CB  . GLU A 1 49  ? -23.771 -1.988  10.380  1.00 12.02  ? 49   GLU A CB  1 
ATOM   359  C  CG  . GLU A 1 49  ? -24.320 -0.616  10.624  0.50 12.75  ? 49   GLU A CG  1 
ATOM   360  C  CD  . GLU A 1 49  ? -25.533 -0.649  11.549  0.50 14.85  ? 49   GLU A CD  1 
ATOM   361  O  OE1 . GLU A 1 49  ? -25.636 -1.571  12.393  0.50 15.59  ? 49   GLU A OE1 1 
ATOM   362  O  OE2 . GLU A 1 49  ? -26.385 0.246   11.434  0.50 16.56  ? 49   GLU A OE2 1 
ATOM   363  N  N   . GLU A 1 50  ? -22.756 -0.382  7.562   1.00 10.43  ? 50   GLU A N   1 
ATOM   364  C  CA  . GLU A 1 50  ? -23.336 0.258   6.388   1.00 10.94  ? 50   GLU A CA  1 
ATOM   365  C  C   . GLU A 1 50  ? -23.210 -0.616  5.144   1.00 10.23  ? 50   GLU A C   1 
ATOM   366  O  O   . GLU A 1 50  ? -22.120 -1.078  4.806   1.00 9.77   ? 50   GLU A O   1 
ATOM   367  C  CB  . GLU A 1 50  ? -22.686 1.611   6.119   1.00 11.11  ? 50   GLU A CB  1 
ATOM   368  C  CG  . GLU A 1 50  ? -23.353 2.401   5.017   1.00 13.66  ? 50   GLU A CG  1 
ATOM   369  C  CD  . GLU A 1 50  ? -24.825 2.606   5.308   1.00 15.52  ? 50   GLU A CD  1 
ATOM   370  O  OE1 . GLU A 1 50  ? -25.163 3.346   6.247   1.00 19.28  ? 50   GLU A OE1 1 
ATOM   371  O  OE2 . GLU A 1 50  ? -25.653 2.025   4.600   1.00 16.52  ? 50   GLU A OE2 1 
ATOM   372  N  N   . GLU A 1 51  ? -24.327 -0.832  4.461   1.00 10.84  ? 51   GLU A N   1 
ATOM   373  C  CA  . GLU A 1 51  ? -24.341 -1.644  3.246   1.00 11.86  ? 51   GLU A CA  1 
ATOM   374  C  C   . GLU A 1 51  ? -25.095 -1.002  2.077   1.00 14.23  ? 51   GLU A C   1 
ATOM   375  O  O   . GLU A 1 51  ? -25.322 -1.642  1.056   1.00 14.10  ? 51   GLU A O   1 
ATOM   376  C  CB  . GLU A 1 51  ? -24.911 -3.035  3.557   1.00 11.78  ? 51   GLU A CB  1 
ATOM   377  C  CG  . GLU A 1 51  ? -26.344 -3.023  4.079   1.00 12.27  ? 51   GLU A CG  1 
ATOM   378  C  CD  . GLU A 1 51  ? -26.902 -4.414  4.374   1.00 12.36  ? 51   GLU A CD  1 
ATOM   379  O  OE1 . GLU A 1 51  ? -26.108 -5.368  4.513   1.00 14.07  ? 51   GLU A OE1 1 
ATOM   380  O  OE2 . GLU A 1 51  ? -28.149 -4.545  4.479   1.00 12.63  ? 51   GLU A OE2 1 
ATOM   381  N  N   A ASP A 1 52  ? -25.450 0.269   2.250   0.50 15.29  ? 52   ASP A N   1 
ATOM   382  N  N   B ASP A 1 52  ? -25.484 0.259   2.206   0.50 15.50  ? 52   ASP A N   1 
ATOM   383  C  CA  A ASP A 1 52  ? -26.107 1.065   1.221   0.50 17.44  ? 52   ASP A CA  1 
ATOM   384  C  CA  B ASP A 1 52  ? -26.295 0.896   1.165   0.50 17.79  ? 52   ASP A CA  1 
ATOM   385  C  C   A ASP A 1 52  ? -25.108 2.075   0.649   0.50 19.63  ? 52   ASP A C   1 
ATOM   386  C  C   B ASP A 1 52  ? -25.453 1.704   0.176   0.50 20.24  ? 52   ASP A C   1 
ATOM   387  O  O   A ASP A 1 52  ? -24.570 1.865   -0.434  0.50 19.53  ? 52   ASP A O   1 
ATOM   388  O  O   B ASP A 1 52  ? -24.230 1.760   0.290   0.50 19.28  ? 52   ASP A O   1 
ATOM   389  C  CB  A ASP A 1 52  ? -27.319 1.755   1.835   0.50 17.53  ? 52   ASP A CB  1 
ATOM   390  C  CB  B ASP A 1 52  ? -27.388 1.725   1.826   0.50 17.96  ? 52   ASP A CB  1 
ATOM   391  C  CG  A ASP A 1 52  ? -28.158 0.797   2.655   0.50 16.52  ? 52   ASP A CG  1 
ATOM   392  C  CG  B ASP A 1 52  ? -28.264 0.875   2.725   0.50 17.19  ? 52   ASP A CG  1 
ATOM   393  O  OD1 A ASP A 1 52  ? -28.642 -0.193  2.081   0.50 14.98  ? 52   ASP A OD1 1 
ATOM   394  O  OD1 B ASP A 1 52  ? -28.844 -0.106  2.226   0.50 16.14  ? 52   ASP A OD1 1 
ATOM   395  O  OD2 A ASP A 1 52  ? -28.312 1.012   3.868   0.50 15.54  ? 52   ASP A OD2 1 
ATOM   396  O  OD2 B ASP A 1 52  ? -28.348 1.159   3.929   0.50 16.67  ? 52   ASP A OD2 1 
ATOM   397  N  N   A ASN A 1 53  ? -24.841 3.162   1.366   0.50 22.32  ? 53   ASN A N   1 
ATOM   398  N  N   B ASN A 1 53  ? -26.109 2.295   -0.816  0.50 23.86  ? 53   ASN A N   1 
ATOM   399  C  CA  A ASN A 1 53  ? -23.786 4.071   0.936   0.50 24.81  ? 53   ASN A CA  1 
ATOM   400  C  CA  B ASN A 1 53  ? -25.398 2.982   -1.893  0.50 26.68  ? 53   ASN A CA  1 
ATOM   401  C  C   A ASN A 1 53  ? -22.440 3.628   1.506   0.50 25.71  ? 53   ASN A C   1 
ATOM   402  C  C   B ASN A 1 53  ? -25.068 4.426   -1.548  0.50 28.47  ? 53   ASN A C   1 
ATOM   403  O  O   A ASN A 1 53  ? -22.026 4.068   2.578   0.50 25.30  ? 53   ASN A O   1 
ATOM   404  O  O   B ASN A 1 53  ? -25.715 5.353   -2.035  0.50 29.62  ? 53   ASN A O   1 
ATOM   405  C  CB  A ASN A 1 53  ? -24.079 5.518   1.333   0.50 25.62  ? 53   ASN A CB  1 
ATOM   406  C  CB  B ASN A 1 53  ? -26.230 2.935   -3.175  0.50 27.85  ? 53   ASN A CB  1 
ATOM   407  C  CG  A ASN A 1 53  ? -22.990 6.478   0.863   0.50 26.68  ? 53   ASN A CG  1 
ATOM   408  C  CG  B ASN A 1 53  ? -25.402 3.189   -4.414  0.50 28.93  ? 53   ASN A CG  1 
ATOM   409  O  OD1 A ASN A 1 53  ? -22.284 6.209   -0.120  0.50 26.75  ? 53   ASN A OD1 1 
ATOM   410  O  OD1 B ASN A 1 53  ? -24.331 3.793   -4.347  0.50 30.26  ? 53   ASN A OD1 1 
ATOM   411  N  ND2 A ASN A 1 53  ? -22.851 7.602   1.561   0.50 27.83  ? 53   ASN A ND2 1 
ATOM   412  N  ND2 B ASN A 1 53  ? -25.891 2.720   -5.557  0.50 30.36  ? 53   ASN A ND2 1 
ATOM   413  N  N   A THR A 1 54  ? -21.763 2.753   0.769   0.60 27.22  ? 54   THR A N   1 
ATOM   414  N  N   B THR A 1 54  ? -24.050 4.618   -0.718  0.40 29.49  ? 54   THR A N   1 
ATOM   415  C  CA  A THR A 1 54  ? -20.490 2.180   1.197   0.60 28.08  ? 54   THR A CA  1 
ATOM   416  C  CA  B THR A 1 54  ? -23.711 5.952   -0.249  0.40 30.90  ? 54   THR A CA  1 
ATOM   417  C  C   A THR A 1 54  ? -19.298 2.905   0.560   0.60 29.28  ? 54   THR A C   1 
ATOM   418  C  C   B THR A 1 54  ? -22.319 6.394   -0.694  0.40 31.47  ? 54   THR A C   1 
ATOM   419  O  O   A THR A 1 54  ? -18.140 2.580   0.847   0.60 28.92  ? 54   THR A O   1 
ATOM   420  O  O   B THR A 1 54  ? -21.563 5.623   -1.285  0.40 31.13  ? 54   THR A O   1 
ATOM   421  C  CB  A THR A 1 54  ? -20.430 0.697   0.809   0.60 27.84  ? 54   THR A CB  1 
ATOM   422  C  CB  B THR A 1 54  ? -23.805 6.034   1.283   0.40 30.76  ? 54   THR A CB  1 
ATOM   423  O  OG1 A THR A 1 54  ? -20.623 0.576   -0.607  0.60 28.32  ? 54   THR A OG1 1 
ATOM   424  O  OG1 B THR A 1 54  ? -23.381 4.790   1.859   0.40 30.10  ? 54   THR A OG1 1 
ATOM   425  C  CG2 A THR A 1 54  ? -21.525 -0.095  1.527   0.60 26.90  ? 54   THR A CG2 1 
ATOM   426  C  CG2 B THR A 1 54  ? -25.227 6.326   1.701   0.40 31.24  ? 54   THR A CG2 1 
ATOM   427  N  N   A ALA A 1 55  ? -19.584 3.882   -0.299  0.50 30.74  ? 55   ALA A N   1 
ATOM   428  N  N   B ALA A 1 55  ? -21.994 7.649   -0.400  0.50 32.57  ? 55   ALA A N   1 
ATOM   429  C  CA  A ALA A 1 55  ? -18.546 4.620   -1.011  0.50 31.72  ? 55   ALA A CA  1 
ATOM   430  C  CA  B ALA A 1 55  ? -20.712 8.222   -0.786  0.50 32.97  ? 55   ALA A CA  1 
ATOM   431  C  C   A ALA A 1 55  ? -17.835 5.586   -0.076  0.50 31.97  ? 55   ALA A C   1 
ATOM   432  C  C   B ALA A 1 55  ? -19.720 8.237   0.373   0.50 32.58  ? 55   ALA A C   1 
ATOM   433  O  O   A ALA A 1 55  ? -16.701 5.343   0.329   0.50 32.06  ? 55   ALA A O   1 
ATOM   434  O  O   B ALA A 1 55  ? -19.972 8.829   1.426   0.50 32.71  ? 55   ALA A O   1 
ATOM   435  C  CB  A ALA A 1 55  ? -19.140 5.370   -2.192  0.50 32.49  ? 55   ALA A CB  1 
ATOM   436  C  CB  B ALA A 1 55  ? -20.910 9.624   -1.319  0.50 33.91  ? 55   ALA A CB  1 
ATOM   437  N  N   A GLY A 1 56  ? -18.492 6.683   0.271   0.50 32.48  ? 56   GLY A N   1 
ATOM   438  N  N   B GLY A 1 56  ? -18.595 7.561   0.166   0.50 32.19  ? 56   GLY A N   1 
ATOM   439  C  CA  A GLY A 1 56  ? -17.872 7.670   1.145   0.50 32.26  ? 56   GLY A CA  1 
ATOM   440  C  CA  B GLY A 1 56  ? -17.448 7.647   1.068   0.50 31.57  ? 56   GLY A CA  1 
ATOM   441  C  C   A GLY A 1 56  ? -17.584 7.070   2.506   0.50 31.02  ? 56   GLY A C   1 
ATOM   442  C  C   B GLY A 1 56  ? -17.674 7.139   2.483   0.50 30.74  ? 56   GLY A C   1 
ATOM   443  O  O   A GLY A 1 56  ? -17.693 5.849   2.692   0.50 30.56  ? 56   GLY A O   1 
ATOM   444  O  O   B GLY A 1 56  ? -18.285 6.081   2.691   0.50 30.63  ? 56   GLY A O   1 
ATOM   445  N  N   . CYS A 1 57  ? -17.186 7.922   3.448   1.00 30.03  ? 57   CYS A N   1 
ATOM   446  C  CA  . CYS A 1 57  ? -17.094 7.528   4.859   1.00 28.23  ? 57   CYS A CA  1 
ATOM   447  C  C   . CYS A 1 57  ? -18.257 8.064   5.687   1.00 27.52  ? 57   CYS A C   1 
ATOM   448  O  O   . CYS A 1 57  ? -18.402 7.692   6.849   1.00 26.18  ? 57   CYS A O   1 
ATOM   449  C  CB  A CYS A 1 57  ? -15.777 8.038   5.463   0.50 28.45  ? 57   CYS A CB  1 
ATOM   450  C  CB  B CYS A 1 57  ? -15.755 7.978   5.465   0.50 27.85  ? 57   CYS A CB  1 
ATOM   451  S  SG  A CYS A 1 57  ? -14.274 7.595   4.530   0.50 29.26  ? 57   CYS A SG  1 
ATOM   452  S  SG  B CYS A 1 57  ? -14.371 6.831   5.132   0.50 24.23  ? 57   CYS A SG  1 
ATOM   453  N  N   . THR A 1 58  ? -19.097 8.908   5.090   1.00 27.31  ? 58   THR A N   1 
ATOM   454  C  CA  . THR A 1 58  ? -20.077 9.679   5.859   1.00 27.16  ? 58   THR A CA  1 
ATOM   455  C  C   . THR A 1 58  ? -21.106 8.818   6.600   1.00 26.20  ? 58   THR A C   1 
ATOM   456  O  O   . THR A 1 58  ? -21.461 9.108   7.751   1.00 25.72  ? 58   THR A O   1 
ATOM   457  C  CB  . THR A 1 58  ? -20.825 10.707  4.955   1.00 28.48  ? 58   THR A CB  1 
ATOM   458  O  OG1 . THR A 1 58  ? -19.873 11.599  4.352   1.00 29.50  ? 58   THR A OG1 1 
ATOM   459  C  CG2 . THR A 1 58  ? -21.831 11.525  5.773   1.00 29.11  ? 58   THR A CG2 1 
ATOM   460  N  N   . SER A 1 59  ? -21.568 7.756   5.944   1.00 24.97  ? 59   SER A N   1 
ATOM   461  C  CA  . SER A 1 59  ? -22.663 6.942   6.463   1.00 24.58  ? 59   SER A CA  1 
ATOM   462  C  C   . SER A 1 59  ? -22.164 5.762   7.297   1.00 23.73  ? 59   SER A C   1 
ATOM   463  O  O   . SER A 1 59  ? -22.942 5.136   8.022   1.00 23.52  ? 59   SER A O   1 
ATOM   464  C  CB  . SER A 1 59  ? -23.539 6.435   5.302   1.00 24.92  ? 59   SER A CB  1 
ATOM   465  O  OG  . SER A 1 59  ? -24.049 7.523   4.533   1.00 26.55  ? 59   SER A OG  1 
ATOM   466  N  N   . ALA A 1 60  ? -20.872 5.457   7.200   1.00 22.72  ? 60   ALA A N   1 
ATOM   467  C  CA  . ALA A 1 60  ? -20.294 4.405   8.020   1.00 22.70  ? 60   ALA A CA  1 
ATOM   468  C  C   . ALA A 1 60  ? -20.168 4.952   9.444   0.90 23.33  ? 60   ALA A C   1 
ATOM   469  O  O   . ALA A 1 60  ? -20.495 6.111   9.706   0.90 24.09  ? 60   ALA A O   1 
ATOM   470  C  CB  . ALA A 1 60  ? -18.941 3.969   7.455   1.00 21.42  ? 60   ALA A CB  1 
ATOM   471  N  N   . GLY A 1 61  ? -19.714 4.123   10.369  0.90 23.11  ? 61   GLY A N   1 
ATOM   472  C  CA  . GLY A 1 61  ? -19.590 4.555   11.765  0.90 22.63  ? 61   GLY A CA  1 
ATOM   473  C  C   . GLY A 1 61  ? -20.014 3.451   12.714  0.90 20.81  ? 61   GLY A C   1 
ATOM   474  O  O   . GLY A 1 61  ? -19.179 2.906   13.432  0.90 21.16  ? 61   GLY A O   1 
ATOM   475  N  N   . PRO A 1 62  ? -21.317 3.130   12.753  0.90 18.36  ? 62   PRO A N   1 
ATOM   476  C  CA  . PRO A 1 62  ? -21.705 2.030   13.630  1.00 16.36  ? 62   PRO A CA  1 
ATOM   477  C  C   . PRO A 1 62  ? -21.070 0.725   13.170  1.00 13.69  ? 62   PRO A C   1 
ATOM   478  O  O   . PRO A 1 62  ? -21.160 0.373   11.993  1.00 12.51  ? 62   PRO A O   1 
ATOM   479  C  CB  . PRO A 1 62  ? -23.234 1.985   13.495  1.00 17.07  ? 62   PRO A CB  1 
ATOM   480  C  CG  . PRO A 1 62  ? -23.611 3.337   13.042  1.00 18.72  ? 62   PRO A CG  1 
ATOM   481  C  CD  . PRO A 1 62  ? -22.478 3.868   12.236  1.00 19.30  ? 62   PRO A CD  1 
ATOM   482  N  N   . HIS A 1 63  ? -20.394 0.040   14.091  1.00 11.50  ? 63   HIS A N   1 
ATOM   483  C  CA  . HIS A 1 63  ? -19.722 -1.207  13.769  1.00 10.27  ? 63   HIS A CA  1 
ATOM   484  C  C   . HIS A 1 63  ? -20.733 -2.293  13.465  1.00 9.96   ? 63   HIS A C   1 
ATOM   485  O  O   . HIS A 1 63  ? -21.811 -2.315  14.036  1.00 11.05  ? 63   HIS A O   1 
ATOM   486  C  CB  . HIS A 1 63  ? -18.835 -1.665  14.919  1.00 10.12  ? 63   HIS A CB  1 
ATOM   487  C  CG  . HIS A 1 63  ? -17.691 -0.749  15.187  1.00 9.51   ? 63   HIS A CG  1 
ATOM   488  N  ND1 . HIS A 1 63  ? -16.873 -0.877  16.288  1.00 8.70   ? 63   HIS A ND1 1 
ATOM   489  C  CD2 . HIS A 1 63  ? -17.239 0.328   14.500  1.00 9.94   ? 63   HIS A CD2 1 
ATOM   490  C  CE1 . HIS A 1 63  ? -15.954 0.070   16.252  1.00 10.05  ? 63   HIS A CE1 1 
ATOM   491  N  NE2 . HIS A 1 63  ? -16.165 0.825   15.190  1.00 10.43  ? 63   HIS A NE2 1 
ATOM   492  N  N   . PHE A 1 64  ? -20.356 -3.210  12.583  1.00 9.54   ? 64   PHE A N   1 
ATOM   493  C  CA  . PHE A 1 64  ? -21.200 -4.336  12.265  1.00 9.36   ? 64   PHE A CA  1 
ATOM   494  C  C   . PHE A 1 64  ? -21.362 -5.229  13.498  1.00 9.80   ? 64   PHE A C   1 
ATOM   495  O  O   . PHE A 1 64  ? -20.386 -5.745  14.052  1.00 10.51  ? 64   PHE A O   1 
ATOM   496  C  CB  . PHE A 1 64  ? -20.623 -5.101  11.064  1.00 9.59   ? 64   PHE A CB  1 
ATOM   497  C  CG  . PHE A 1 64  ? -21.462 -6.284  10.630  1.00 10.51  ? 64   PHE A CG  1 
ATOM   498  C  CD1 . PHE A 1 64  ? -22.836 -6.173  10.474  1.00 11.86  ? 64   PHE A CD1 1 
ATOM   499  C  CD2 . PHE A 1 64  ? -20.868 -7.496  10.338  1.00 11.93  ? 64   PHE A CD2 1 
ATOM   500  C  CE1 . PHE A 1 64  ? -23.595 -7.265  10.070  1.00 12.68  ? 64   PHE A CE1 1 
ATOM   501  C  CE2 . PHE A 1 64  ? -21.629 -8.585  9.921   1.00 12.13  ? 64   PHE A CE2 1 
ATOM   502  C  CZ  . PHE A 1 64  ? -22.990 -8.464  9.799   1.00 11.71  ? 64   PHE A CZ  1 
ATOM   503  N  N   . ASN A 1 65  ? -22.598 -5.305  13.978  1.00 10.57  ? 65   ASN A N   1 
ATOM   504  C  CA  . ASN A 1 65  ? -22.901 -5.898  15.290  1.00 10.82  ? 65   ASN A CA  1 
ATOM   505  C  C   . ASN A 1 65  ? -24.208 -6.696  15.289  1.00 12.15  ? 65   ASN A C   1 
ATOM   506  O  O   . ASN A 1 65  ? -25.140 -6.396  16.037  1.00 12.77  ? 65   ASN A O   1 
ATOM   507  C  CB  . ASN A 1 65  ? -22.941 -4.771  16.325  1.00 10.76  ? 65   ASN A CB  1 
ATOM   508  C  CG  . ASN A 1 65  ? -23.049 -5.273  17.763  1.00 10.02  ? 65   ASN A CG  1 
ATOM   509  O  OD1 . ASN A 1 65  ? -22.657 -6.399  18.084  1.00 11.19  ? 65   ASN A OD1 1 
ATOM   510  N  ND2 . ASN A 1 65  ? -23.578 -4.418  18.652  1.00 12.21  ? 65   ASN A ND2 1 
ATOM   511  N  N   . PRO A 1 66  ? -24.273 -7.741  14.454  1.00 13.01  ? 66   PRO A N   1 
ATOM   512  C  CA  . PRO A 1 66  ? -25.518 -8.483  14.319  1.00 14.67  ? 66   PRO A CA  1 
ATOM   513  C  C   . PRO A 1 66  ? -25.907 -9.232  15.579  1.00 15.69  ? 66   PRO A C   1 
ATOM   514  O  O   . PRO A 1 66  ? -27.074 -9.613  15.713  1.00 17.86  ? 66   PRO A O   1 
ATOM   515  C  CB  . PRO A 1 66  ? -25.210 -9.475  13.187  1.00 14.48  ? 66   PRO A CB  1 
ATOM   516  C  CG  . PRO A 1 66  ? -23.753 -9.650  13.213  1.00 14.25  ? 66   PRO A CG  1 
ATOM   517  C  CD  . PRO A 1 66  ? -23.209 -8.307  13.609  1.00 13.00  ? 66   PRO A CD  1 
ATOM   518  N  N   . LEU A 1 67  ? -24.958 -9.463  16.493  1.00 16.02  ? 67   LEU A N   1 
ATOM   519  C  CA  . LEU A 1 67  ? -25.255 -10.201 17.731  1.00 16.97  ? 67   LEU A CA  1 
ATOM   520  C  C   . LEU A 1 67  ? -25.445 -9.297  18.952  1.00 16.97  ? 67   LEU A C   1 
ATOM   521  O  O   . LEU A 1 67  ? -25.549 -9.785  20.089  1.00 17.84  ? 67   LEU A O   1 
ATOM   522  C  CB  . LEU A 1 67  ? -24.167 -11.254 17.997  1.00 17.63  ? 67   LEU A CB  1 
ATOM   523  C  CG  . LEU A 1 67  ? -23.926 -12.285 16.885  1.00 19.98  ? 67   LEU A CG  1 
ATOM   524  C  CD1 . LEU A 1 67  ? -22.709 -13.155 17.182  1.00 21.76  ? 67   LEU A CD1 1 
ATOM   525  C  CD2 . LEU A 1 67  ? -25.169 -13.140 16.660  1.00 22.07  ? 67   LEU A CD2 1 
ATOM   526  N  N   . SER A 1 68  ? -25.540 -7.990  18.704  1.00 15.87  ? 68   SER A N   1 
ATOM   527  C  CA  . SER A 1 68  ? -25.853 -6.983  19.728  1.00 16.36  ? 68   SER A CA  1 
ATOM   528  C  C   . SER A 1 68  ? -24.952 -7.065  20.958  1.00 16.01  ? 68   SER A C   1 
ATOM   529  O  O   . SER A 1 68  ? -25.424 -7.122  22.101  1.00 16.15  ? 68   SER A O   1 
ATOM   530  C  CB  . SER A 1 68  ? -27.318 -7.079  20.135  1.00 17.38  ? 68   SER A CB  1 
ATOM   531  O  OG  . SER A 1 68  ? -28.148 -6.937  18.994  1.00 19.88  ? 68   SER A OG  1 
ATOM   532  N  N   . ARG A 1 69  ? -23.654 -7.083  20.701  1.00 14.88  ? 69   ARG A N   1 
ATOM   533  C  CA  . ARG A 1 69  ? -22.647 -7.179  21.746  1.00 14.89  ? 69   ARG A CA  1 
ATOM   534  C  C   . ARG A 1 69  ? -22.024 -5.812  21.966  1.00 13.56  ? 69   ARG A C   1 
ATOM   535  O  O   . ARG A 1 69  ? -22.310 -4.862  21.232  1.00 13.02  ? 69   ARG A O   1 
ATOM   536  C  CB  . ARG A 1 69  ? -21.542 -8.147  21.336  1.00 14.75  ? 69   ARG A CB  1 
ATOM   537  C  CG  A ARG A 1 69  ? -22.044 -9.481  20.800  0.50 15.30  ? 69   ARG A CG  1 
ATOM   538  C  CG  B ARG A 1 69  ? -22.041 -9.470  20.790  0.50 16.58  ? 69   ARG A CG  1 
ATOM   539  C  CD  A ARG A 1 69  ? -22.917 -10.207 21.805  0.50 16.39  ? 69   ARG A CD  1 
ATOM   540  C  CD  B ARG A 1 69  ? -21.765 -10.589 21.741  0.50 19.37  ? 69   ARG A CD  1 
ATOM   541  N  NE  A ARG A 1 69  ? -22.125 -10.747 22.902  0.50 18.60  ? 69   ARG A NE  1 
ATOM   542  N  NE  B ARG A 1 69  ? -22.374 -10.382 23.045  0.50 21.38  ? 69   ARG A NE  1 
ATOM   543  C  CZ  A ARG A 1 69  ? -22.651 -11.182 24.040  0.50 20.21  ? 69   ARG A CZ  1 
ATOM   544  C  CZ  B ARG A 1 69  ? -21.989 -11.033 24.138  0.50 23.30  ? 69   ARG A CZ  1 
ATOM   545  N  NH1 A ARG A 1 69  ? -23.957 -11.119 24.217  0.50 19.92  ? 69   ARG A NH1 1 
ATOM   546  N  NH1 B ARG A 1 69  ? -20.988 -11.905 24.070  0.50 23.86  ? 69   ARG A NH1 1 
ATOM   547  N  NH2 A ARG A 1 69  ? -21.870 -11.668 24.993  0.50 21.05  ? 69   ARG A NH2 1 
ATOM   548  N  NH2 B ARG A 1 69  ? -22.585 -10.795 25.297  0.50 23.18  ? 69   ARG A NH2 1 
ATOM   549  N  N   . LYS A 1 70  ? -21.161 -5.733  22.969  1.00 13.79  ? 70   LYS A N   1 
ATOM   550  C  CA  . LYS A 1 70  ? -20.369 -4.535  23.210  1.00 13.44  ? 70   LYS A CA  1 
ATOM   551  C  C   . LYS A 1 70  ? -19.042 -4.596  22.437  1.00 11.92  ? 70   LYS A C   1 
ATOM   552  O  O   . LYS A 1 70  ? -18.573 -5.666  22.036  1.00 11.97  ? 70   LYS A O   1 
ATOM   553  C  CB  . LYS A 1 70  ? -20.119 -4.327  24.706  1.00 14.66  ? 70   LYS A CB  1 
ATOM   554  C  CG  . LYS A 1 70  ? -21.399 -4.035  25.500  1.00 16.49  ? 70   LYS A CG  1 
ATOM   555  C  CD  . LYS A 1 70  ? -21.102 -3.377  26.843  1.00 21.25  ? 70   LYS A CD  1 
ATOM   556  C  CE  . LYS A 1 70  ? -22.371 -2.888  27.544  0.50 22.11  ? 70   LYS A CE  1 
ATOM   557  N  NZ  . LYS A 1 70  ? -22.885 -3.853  28.546  0.50 23.72  ? 70   LYS A NZ  1 
ATOM   558  N  N   . HIS A 1 71  ? -18.456 -3.427  22.233  1.00 11.18  ? 71   HIS A N   1 
ATOM   559  C  CA  . HIS A 1 71  ? -17.231 -3.282  21.496  1.00 10.01  ? 71   HIS A CA  1 
ATOM   560  C  C   . HIS A 1 71  ? -16.063 -3.885  22.274  1.00 10.44  ? 71   HIS A C   1 
ATOM   561  O  O   . HIS A 1 71  ? -15.993 -3.769  23.502  1.00 11.33  ? 71   HIS A O   1 
ATOM   562  C  CB  . HIS A 1 71  ? -16.956 -1.797  21.205  1.00 10.24  ? 71   HIS A CB  1 
ATOM   563  C  CG  . HIS A 1 71  ? -15.697 -1.557  20.447  1.00 9.46   ? 71   HIS A CG  1 
ATOM   564  N  ND1 . HIS A 1 71  ? -15.579 -1.783  19.094  1.00 8.36   ? 71   HIS A ND1 1 
ATOM   565  C  CD2 . HIS A 1 71  ? -14.478 -1.145  20.869  1.00 9.36   ? 71   HIS A CD2 1 
ATOM   566  C  CE1 . HIS A 1 71  ? -14.346 -1.500  18.711  1.00 8.76   ? 71   HIS A CE1 1 
ATOM   567  N  NE2 . HIS A 1 71  ? -13.659 -1.107  19.769  1.00 9.37   ? 71   HIS A NE2 1 
ATOM   568  N  N   . GLY A 1 72  ? -15.149 -4.509  21.541  1.00 9.62   ? 72   GLY A N   1 
ATOM   569  C  CA  . GLY A 1 72  ? -13.936 -5.079  22.126  1.00 10.31  ? 72   GLY A CA  1 
ATOM   570  C  C   . GLY A 1 72  ? -12.814 -5.172  21.115  1.00 10.90  ? 72   GLY A C   1 
ATOM   571  O  O   . GLY A 1 72  ? -12.964 -4.754  19.981  1.00 10.33  ? 72   GLY A O   1 
ATOM   572  N  N   . GLY A 1 73  ? -11.679 -5.691  21.552  1.00 11.57  ? 73   GLY A N   1 
ATOM   573  C  CA  . GLY A 1 73  ? -10.596 -6.041  20.640  1.00 11.69  ? 73   GLY A CA  1 
ATOM   574  C  C   . GLY A 1 73  ? -10.930 -7.347  19.948  1.00 12.00  ? 73   GLY A C   1 
ATOM   575  O  O   . GLY A 1 73  ? -11.840 -8.067  20.372  1.00 12.23  ? 73   GLY A O   1 
ATOM   576  N  N   . PRO A 1 74  ? -10.213 -7.661  18.864  1.00 12.42  ? 74   PRO A N   1 
ATOM   577  C  CA  . PRO A 1 74  ? -10.495 -8.865  18.078  1.00 13.26  ? 74   PRO A CA  1 
ATOM   578  C  C   . PRO A 1 74  ? -10.355 -10.155 18.871  1.00 14.06  ? 74   PRO A C   1 
ATOM   579  O  O   . PRO A 1 74  ? -11.027 -11.138 18.549  1.00 14.19  ? 74   PRO A O   1 
ATOM   580  C  CB  . PRO A 1 74  ? -9.470  -8.793  16.941  1.00 13.14  ? 74   PRO A CB  1 
ATOM   581  C  CG  . PRO A 1 74  ? -8.414  -7.902  17.445  1.00 13.67  ? 74   PRO A CG  1 
ATOM   582  C  CD  . PRO A 1 74  ? -9.096  -6.898  18.298  1.00 12.54  ? 74   PRO A CD  1 
ATOM   583  N  N   . LYS A 1 75  ? -9.503  -10.167 19.894  1.00 15.30  ? 75   LYS A N   1 
ATOM   584  C  CA  . LYS A 1 75  ? -9.305  -11.381 20.675  1.00 16.86  ? 75   LYS A CA  1 
ATOM   585  C  C   . LYS A 1 75  ? -10.148 -11.452 21.942  1.00 17.06  ? 75   LYS A C   1 
ATOM   586  O  O   . LYS A 1 75  ? -10.074 -12.446 22.675  1.00 17.89  ? 75   LYS A O   1 
ATOM   587  C  CB  . LYS A 1 75  ? -7.817  -11.565 20.996  1.00 18.45  ? 75   LYS A CB  1 
ATOM   588  C  CG  . LYS A 1 75  ? -6.918  -11.697 19.744  1.00 20.98  ? 75   LYS A CG  1 
ATOM   589  C  CD  . LYS A 1 75  ? -7.318  -12.875 18.816  1.00 25.29  ? 75   LYS A CD  1 
ATOM   590  C  CE  . LYS A 1 75  ? -6.861  -12.666 17.375  1.00 27.28  ? 75   LYS A CE  1 
ATOM   591  N  NZ  . LYS A 1 75  ? -7.467  -13.674 16.438  1.00 29.97  ? 75   LYS A NZ  1 
ATOM   592  N  N   . ASP A 1 76  ? -10.962 -10.422 22.184  1.00 16.81  ? 76   ASP A N   1 
ATOM   593  C  CA  . ASP A 1 76  ? -11.901 -10.426 23.308  1.00 17.12  ? 76   ASP A CA  1 
ATOM   594  C  C   . ASP A 1 76  ? -13.124 -11.280 23.018  1.00 17.47  ? 76   ASP A C   1 
ATOM   595  O  O   . ASP A 1 76  ? -13.619 -11.320 21.887  1.00 16.74  ? 76   ASP A O   1 
ATOM   596  C  CB  . ASP A 1 76  ? -12.357 -9.010  23.651  1.00 17.08  ? 76   ASP A CB  1 
ATOM   597  C  CG  . ASP A 1 76  ? -11.265 -8.184  24.272  1.00 18.35  ? 76   ASP A CG  1 
ATOM   598  O  OD1 . ASP A 1 76  ? -10.438 -8.751  25.039  1.00 22.45  ? 76   ASP A OD1 1 
ATOM   599  O  OD2 . ASP A 1 76  ? -11.240 -6.965  24.007  1.00 18.82  ? 76   ASP A OD2 1 
ATOM   600  N  N   . GLU A 1 77  ? -13.626 -11.932 24.064  1.00 17.74  ? 77   GLU A N   1 
ATOM   601  C  CA  . GLU A 1 77  ? -14.820 -12.751 23.961  1.00 18.52  ? 77   GLU A CA  1 
ATOM   602  C  C   . GLU A 1 77  ? -16.030 -11.880 23.654  1.00 17.38  ? 77   GLU A C   1 
ATOM   603  O  O   . GLU A 1 77  ? -16.861 -12.244 22.826  1.00 18.22  ? 77   GLU A O   1 
ATOM   604  C  CB  . GLU A 1 77  ? -15.046 -13.526 25.255  1.00 19.67  ? 77   GLU A CB  1 
ATOM   605  C  CG  . GLU A 1 77  ? -13.924 -14.499 25.588  1.00 21.49  ? 77   GLU A CG  1 
ATOM   606  C  CD  . GLU A 1 77  ? -14.150 -15.247 26.900  1.00 24.37  ? 77   GLU A CD  1 
ATOM   607  O  OE1 . GLU A 1 77  ? -14.982 -14.808 27.727  1.00 24.96  ? 77   GLU A OE1 1 
ATOM   608  O  OE2 . GLU A 1 77  ? -13.488 -16.277 27.110  1.00 27.11  ? 77   GLU A OE2 1 
ATOM   609  N  N   . GLU A 1 78  ? -16.107 -10.722 24.305  1.00 16.63  ? 78   GLU A N   1 
ATOM   610  C  CA  . GLU A 1 78  ? -17.141 -9.722  24.035  1.00 15.77  ? 78   GLU A CA  1 
ATOM   611  C  C   . GLU A 1 78  ? -16.634 -8.731  22.978  1.00 13.79  ? 78   GLU A C   1 
ATOM   612  O  O   . GLU A 1 78  ? -15.722 -7.963  23.237  1.00 13.34  ? 78   GLU A O   1 
ATOM   613  C  CB  . GLU A 1 78  ? -17.482 -8.962  25.321  1.00 16.79  ? 78   GLU A CB  1 
ATOM   614  C  CG  . GLU A 1 78  ? -18.588 -7.910  25.176  1.00 19.14  ? 78   GLU A CG  1 
ATOM   615  C  CD  . GLU A 1 78  ? -19.976 -8.498  25.283  1.00 22.21  ? 78   GLU A CD  1 
ATOM   616  O  OE1 . GLU A 1 78  ? -20.104 -9.659  25.739  1.00 26.84  ? 78   GLU A OE1 1 
ATOM   617  O  OE2 . GLU A 1 78  ? -20.945 -7.801  24.926  1.00 22.62  ? 78   GLU A OE2 1 
ATOM   618  N  N   . ARG A 1 79  ? -17.207 -8.785  21.780  1.00 12.89  ? 79   ARG A N   1 
ATOM   619  C  CA  . ARG A 1 79  ? -16.839 -7.877  20.702  1.00 11.33  ? 79   ARG A CA  1 
ATOM   620  C  C   . ARG A 1 79  ? -17.928 -7.849  19.650  1.00 11.05  ? 79   ARG A C   1 
ATOM   621  O  O   . ARG A 1 79  ? -18.755 -8.760  19.577  1.00 10.59  ? 79   ARG A O   1 
ATOM   622  C  CB  . ARG A 1 79  ? -15.538 -8.333  20.028  1.00 10.99  ? 79   ARG A CB  1 
ATOM   623  C  CG  . ARG A 1 79  ? -15.582 -9.760  19.474  1.00 11.85  ? 79   ARG A CG  1 
ATOM   624  C  CD  . ARG A 1 79  ? -14.386 -10.062 18.573  1.00 12.47  ? 79   ARG A CD  1 
ATOM   625  N  NE  . ARG A 1 79  ? -14.654 -9.731  17.166  1.00 12.15  ? 79   ARG A NE  1 
ATOM   626  C  CZ  . ARG A 1 79  ? -13.891 -10.093 16.140  1.00 12.16  ? 79   ARG A CZ  1 
ATOM   627  N  NH1 . ARG A 1 79  ? -12.775 -10.791 16.335  1.00 12.53  ? 79   ARG A NH1 1 
ATOM   628  N  NH2 . ARG A 1 79  ? -14.240 -9.754  14.907  1.00 11.82  ? 79   ARG A NH2 1 
ATOM   629  N  N   . HIS A 1 80  ? -17.912 -6.793  18.845  1.00 10.81  ? 80   HIS A N   1 
ATOM   630  C  CA  . HIS A 1 80  ? -18.719 -6.731  17.641  1.00 10.00  ? 80   HIS A CA  1 
ATOM   631  C  C   . HIS A 1 80  ? -18.082 -7.631  16.598  1.00 9.90   ? 80   HIS A C   1 
ATOM   632  O  O   . HIS A 1 80  ? -16.861 -7.833  16.595  1.00 10.31  ? 80   HIS A O   1 
ATOM   633  C  CB  . HIS A 1 80  ? -18.775 -5.302  17.078  1.00 9.28   ? 80   HIS A CB  1 
ATOM   634  C  CG  . HIS A 1 80  ? -19.292 -4.289  18.042  1.00 8.86   ? 80   HIS A CG  1 
ATOM   635  N  ND1 . HIS A 1 80  ? -18.796 -3.010  18.125  1.00 8.32   ? 80   HIS A ND1 1 
ATOM   636  C  CD2 . HIS A 1 80  ? -20.275 -4.376  18.969  1.00 9.61   ? 80   HIS A CD2 1 
ATOM   637  C  CE1 . HIS A 1 80  ? -19.473 -2.342  19.045  1.00 9.87   ? 80   HIS A CE1 1 
ATOM   638  N  NE2 . HIS A 1 80  ? -20.363 -3.154  19.584  1.00 11.06  ? 80   HIS A NE2 1 
ATOM   639  N  N   . VAL A 1 81  ? -18.893 -8.147  15.677  1.00 10.13  ? 81   VAL A N   1 
ATOM   640  C  CA  . VAL A 1 81  ? -18.356 -8.911  14.564  1.00 9.65   ? 81   VAL A CA  1 
ATOM   641  C  C   . VAL A 1 81  ? -17.325 -8.038  13.831  1.00 8.97   ? 81   VAL A C   1 
ATOM   642  O  O   . VAL A 1 81  ? -16.268 -8.529  13.426  1.00 9.38   ? 81   VAL A O   1 
ATOM   643  C  CB  . VAL A 1 81  ? -19.485 -9.432  13.607  1.00 9.20   ? 81   VAL A CB  1 
ATOM   644  C  CG1 . VAL A 1 81  ? -18.913 -9.967  12.266  1.00 10.09  ? 81   VAL A CG1 1 
ATOM   645  C  CG2 . VAL A 1 81  ? -20.332 -10.526 14.305  1.00 10.47  ? 81   VAL A CG2 1 
ATOM   646  N  N   . GLY A 1 82  ? -17.611 -6.745  13.691  1.00 8.53   ? 82   GLY A N   1 
ATOM   647  C  CA  . GLY A 1 82  ? -16.710 -5.848  12.940  1.00 8.65   ? 82   GLY A CA  1 
ATOM   648  C  C   . GLY A 1 82  ? -15.450 -5.356  13.626  1.00 9.24   ? 82   GLY A C   1 
ATOM   649  O  O   . GLY A 1 82  ? -14.763 -4.494  13.085  1.00 10.57  ? 82   GLY A O   1 
ATOM   650  N  N   . ASP A 1 83  ? -15.137 -5.892  14.803  1.00 9.42   ? 83   ASP A N   1 
ATOM   651  C  CA  . ASP A 1 83  ? -14.009 -5.398  15.598  1.00 9.65   ? 83   ASP A CA  1 
ATOM   652  C  C   . ASP A 1 83  ? -12.685 -6.059  15.226  1.00 9.65   ? 83   ASP A C   1 
ATOM   653  O  O   . ASP A 1 83  ? -12.359 -7.151  15.715  1.00 11.48  ? 83   ASP A O   1 
ATOM   654  C  CB  . ASP A 1 83  ? -14.287 -5.562  17.088  1.00 9.73   ? 83   ASP A CB  1 
ATOM   655  C  CG  . ASP A 1 83  ? -15.396 -4.669  17.575  1.00 8.43   ? 83   ASP A CG  1 
ATOM   656  O  OD1 . ASP A 1 83  ? -15.790 -3.724  16.830  1.00 7.87   ? 83   ASP A OD1 1 
ATOM   657  O  OD2 . ASP A 1 83  ? -15.900 -4.928  18.698  1.00 8.20   ? 83   ASP A OD2 1 
ATOM   658  N  N   . LEU A 1 84  ? -11.909 -5.371  14.388  1.00 9.25   ? 84   LEU A N   1 
ATOM   659  C  CA  . LEU A 1 84  ? -10.659 -5.940  13.892  1.00 9.82   ? 84   LEU A CA  1 
ATOM   660  C  C   . LEU A 1 84  ? -9.419  -5.250  14.460  1.00 9.77   ? 84   LEU A C   1 
ATOM   661  O  O   . LEU A 1 84  ? -8.319  -5.374  13.912  1.00 11.55  ? 84   LEU A O   1 
ATOM   662  C  CB  . LEU A 1 84  ? -10.668 -5.973  12.360  1.00 9.72   ? 84   LEU A CB  1 
ATOM   663  C  CG  . LEU A 1 84  ? -11.771 -6.829  11.709  1.00 10.99  ? 84   LEU A CG  1 
ATOM   664  C  CD1 . LEU A 1 84  ? -11.657 -6.705  10.196  1.00 12.44  ? 84   LEU A CD1 1 
ATOM   665  C  CD2 . LEU A 1 84  ? -11.720 -8.305  12.167  1.00 14.39  ? 84   LEU A CD2 1 
ATOM   666  N  N   . GLY A 1 85  ? -9.596  -4.537  15.566  1.00 10.19  ? 85   GLY A N   1 
ATOM   667  C  CA  . GLY A 1 85  ? -8.485  -3.950  16.301  1.00 10.47  ? 85   GLY A CA  1 
ATOM   668  C  C   . GLY A 1 85  ? -7.831  -2.773  15.623  1.00 10.86  ? 85   GLY A C   1 
ATOM   669  O  O   . GLY A 1 85  ? -8.511  -1.907  15.071  1.00 11.06  ? 85   GLY A O   1 
ATOM   670  N  N   . ASN A 1 86  ? -6.499  -2.746  15.704  1.00 11.31  ? 86   ASN A N   1 
ATOM   671  C  CA  . ASN A 1 86  ? -5.679  -1.692  15.124  1.00 11.51  ? 86   ASN A CA  1 
ATOM   672  C  C   . ASN A 1 86  ? -4.699  -2.188  14.088  1.00 12.14  ? 86   ASN A C   1 
ATOM   673  O  O   . ASN A 1 86  ? -4.180  -3.295  14.173  1.00 13.59  ? 86   ASN A O   1 
ATOM   674  C  CB  . ASN A 1 86  ? -4.886  -1.004  16.220  1.00 11.89  ? 86   ASN A CB  1 
ATOM   675  C  CG  . ASN A 1 86  ? -5.762  -0.199  17.123  1.00 11.30  ? 86   ASN A CG  1 
ATOM   676  O  OD1 . ASN A 1 86  ? -6.375  0.772   16.683  1.00 12.44  ? 86   ASN A OD1 1 
ATOM   677  N  ND2 . ASN A 1 86  ? -5.851  -0.599  18.393  1.00 13.03  ? 86   ASN A ND2 1 
ATOM   678  N  N   . VAL A 1 87  ? -4.408  -1.324  13.134  1.00 12.18  ? 87   VAL A N   1 
ATOM   679  C  CA  . VAL A 1 87  ? -3.284  -1.536  12.230  1.00 13.14  ? 87   VAL A CA  1 
ATOM   680  C  C   . VAL A 1 87  ? -2.242  -0.487  12.582  1.00 13.65  ? 87   VAL A C   1 
ATOM   681  O  O   . VAL A 1 87  ? -2.572  0.551   13.176  1.00 14.44  ? 87   VAL A O   1 
ATOM   682  C  CB  . VAL A 1 87  ? -3.714  -1.479  10.749  1.00 12.83  ? 87   VAL A CB  1 
ATOM   683  C  CG1 . VAL A 1 87  ? -4.748  -2.584  10.474  1.00 13.41  ? 87   VAL A CG1 1 
ATOM   684  C  CG2 . VAL A 1 87  ? -4.267  -0.093  10.368  1.00 13.20  ? 87   VAL A CG2 1 
ATOM   685  N  N   . THR A 1 88  ? -0.984  -0.766  12.257  1.00 13.88  ? 88   THR A N   1 
ATOM   686  C  CA  . THR A 1 88  ? 0.120   0.123   12.628  1.00 14.84  ? 88   THR A CA  1 
ATOM   687  C  C   . THR A 1 88  ? 0.797   0.679   11.379  1.00 14.86  ? 88   THR A C   1 
ATOM   688  O  O   . THR A 1 88  ? 1.278   -0.072  10.535  1.00 14.70  ? 88   THR A O   1 
ATOM   689  C  CB  . THR A 1 88  ? 1.138   -0.626  13.485  1.00 15.90  ? 88   THR A CB  1 
ATOM   690  O  OG1 . THR A 1 88  ? 0.504   -1.070  14.694  1.00 18.46  ? 88   THR A OG1 1 
ATOM   691  C  CG2 . THR A 1 88  ? 2.332   0.270   13.858  1.00 18.23  ? 88   THR A CG2 1 
ATOM   692  N  N   . ALA A 1 89  ? 0.774   1.997   11.247  1.00 14.91  ? 89   ALA A N   1 
ATOM   693  C  CA  . ALA A 1 89  ? 1.446   2.672   10.155  1.00 15.23  ? 89   ALA A CA  1 
ATOM   694  C  C   . ALA A 1 89  ? 2.875   2.994   10.559  1.00 16.60  ? 89   ALA A C   1 
ATOM   695  O  O   . ALA A 1 89  ? 3.131   3.455   11.669  1.00 17.26  ? 89   ALA A O   1 
ATOM   696  C  CB  . ALA A 1 89  ? 0.693   3.939   9.772   1.00 15.39  ? 89   ALA A CB  1 
ATOM   697  N  N   . ASP A 1 90  ? 3.807   2.774   9.640   1.00 17.04  ? 90   ASP A N   1 
ATOM   698  C  CA  . ASP A 1 90  ? 5.209   3.041   9.913   1.00 18.37  ? 90   ASP A CA  1 
ATOM   699  C  C   . ASP A 1 90  ? 5.523   4.508   9.648   1.00 19.13  ? 90   ASP A C   1 
ATOM   700  O  O   . ASP A 1 90  ? 4.616   5.338   9.485   1.00 19.03  ? 90   ASP A O   1 
ATOM   701  C  CB  . ASP A 1 90  ? 6.102   2.099   9.086   1.00 18.45  ? 90   ASP A CB  1 
ATOM   702  C  CG  . ASP A 1 90  ? 6.122   2.431   7.600   1.00 18.69  ? 90   ASP A CG  1 
ATOM   703  O  OD1 . ASP A 1 90  ? 5.404   3.346   7.144   1.00 17.98  ? 90   ASP A OD1 1 
ATOM   704  O  OD2 . ASP A 1 90  ? 6.870   1.740   6.874   1.00 20.48  ? 90   ASP A OD2 1 
ATOM   705  N  N   . LYS A 1 91  ? 6.810   4.835   9.611   1.00 21.18  ? 91   LYS A N   1 
ATOM   706  C  CA  . LYS A 1 91  ? 7.233   6.222   9.521   1.00 22.41  ? 91   LYS A CA  1 
ATOM   707  C  C   . LYS A 1 91  ? 6.804   6.943   8.251   1.00 21.93  ? 91   LYS A C   1 
ATOM   708  O  O   . LYS A 1 91  ? 6.525   8.142   8.300   1.00 22.83  ? 91   LYS A O   1 
ATOM   709  C  CB  . LYS A 1 91  ? 8.751   6.344   9.680   1.00 24.48  ? 91   LYS A CB  1 
ATOM   710  C  CG  . LYS A 1 91  ? 9.193   6.721   11.064  1.00 26.87  ? 91   LYS A CG  1 
ATOM   711  C  CD  . LYS A 1 91  ? 10.692  6.856   11.142  1.00 28.69  ? 91   LYS A CD  1 
ATOM   712  C  CE  . LYS A 1 91  ? 11.204  8.146   10.526  1.00 30.89  ? 91   LYS A CE  1 
ATOM   713  N  NZ  . LYS A 1 91  ? 12.701  8.220   10.615  1.00 32.67  ? 91   LYS A NZ  1 
ATOM   714  N  N   . ASP A 1 92  ? 6.750   6.238   7.121   1.00 20.24  ? 92   ASP A N   1 
ATOM   715  C  CA  . ASP A 1 92  ? 6.323   6.876   5.870   1.00 19.50  ? 92   ASP A CA  1 
ATOM   716  C  C   . ASP A 1 92  ? 4.844   6.639   5.540   1.00 17.79  ? 92   ASP A C   1 
ATOM   717  O  O   . ASP A 1 92  ? 4.421   6.810   4.399   1.00 17.93  ? 92   ASP A O   1 
ATOM   718  C  CB  . ASP A 1 92  ? 7.260   6.545   4.689   1.00 20.13  ? 92   ASP A CB  1 
ATOM   719  C  CG  . ASP A 1 92  ? 7.358   5.044   4.355   1.00 19.71  ? 92   ASP A CG  1 
ATOM   720  O  OD1 . ASP A 1 92  ? 6.721   4.198   4.991   1.00 20.79  ? 92   ASP A OD1 1 
ATOM   721  O  OD2 . ASP A 1 92  ? 8.113   4.698   3.416   1.00 22.89  ? 92   ASP A OD2 1 
ATOM   722  N  N   . GLY A 1 93  ? 4.076   6.255   6.559   1.00 16.03  ? 93   GLY A N   1 
ATOM   723  C  CA  . GLY A 1 93  ? 2.622   6.275   6.494   1.00 14.96  ? 93   GLY A CA  1 
ATOM   724  C  C   . GLY A 1 93  ? 1.965   5.038   5.924   1.00 13.81  ? 93   GLY A C   1 
ATOM   725  O  O   . GLY A 1 93  ? 0.796   5.084   5.527   1.00 14.52  ? 93   GLY A O   1 
ATOM   726  N  N   . VAL A 1 94  ? 2.701   3.932   5.896   1.00 13.22  ? 94   VAL A N   1 
ATOM   727  C  CA  . VAL A 1 94  ? 2.185   2.661   5.371   1.00 11.87  ? 94   VAL A CA  1 
ATOM   728  C  C   . VAL A 1 94  ? 1.915   1.675   6.509   1.00 11.72  ? 94   VAL A C   1 
ATOM   729  O  O   . VAL A 1 94  ? 2.792   1.395   7.330   1.00 12.84  ? 94   VAL A O   1 
ATOM   730  C  CB  . VAL A 1 94  ? 3.155   2.002   4.368   1.00 11.39  ? 94   VAL A CB  1 
ATOM   731  C  CG1 . VAL A 1 94  ? 2.568   0.657   3.842   1.00 11.75  ? 94   VAL A CG1 1 
ATOM   732  C  CG2 . VAL A 1 94  ? 3.509   2.985   3.218   1.00 11.61  ? 94   VAL A CG2 1 
ATOM   733  N  N   . ALA A 1 95  ? 0.688   1.166   6.546   1.00 11.67  ? 95   ALA A N   1 
ATOM   734  C  CA  . ALA A 1 95  ? 0.301   0.103   7.468   1.00 11.95  ? 95   ALA A CA  1 
ATOM   735  C  C   . ALA A 1 95  ? 0.050   -1.168  6.676   1.00 12.28  ? 95   ALA A C   1 
ATOM   736  O  O   . ALA A 1 95  ? -0.747  -1.192  5.720   1.00 12.84  ? 95   ALA A O   1 
ATOM   737  C  CB  . ALA A 1 95  ? -0.955  0.482   8.260   1.00 11.58  ? 95   ALA A CB  1 
ATOM   738  N  N   . ASP A 1 96  ? 0.747   -2.224  7.069   1.00 12.89  ? 96   ASP A N   1 
ATOM   739  C  CA  . ASP A 1 96  ? 0.508   -3.542  6.504   1.00 13.24  ? 96   ASP A CA  1 
ATOM   740  C  C   . ASP A 1 96  ? -0.493  -4.284  7.364   1.00 13.49  ? 96   ASP A C   1 
ATOM   741  O  O   . ASP A 1 96  ? -0.360  -4.358  8.591   1.00 15.92  ? 96   ASP A O   1 
ATOM   742  C  CB  . ASP A 1 96  ? 1.802   -4.331  6.409   1.00 13.91  ? 96   ASP A CB  1 
ATOM   743  C  CG  . ASP A 1 96  ? 2.747   -3.782  5.368   1.00 14.09  ? 96   ASP A CG  1 
ATOM   744  O  OD1 . ASP A 1 96  ? 2.320   -3.109  4.395   1.00 15.41  ? 96   ASP A OD1 1 
ATOM   745  O  OD2 . ASP A 1 96  ? 3.948   -4.042  5.524   1.00 13.65  ? 96   ASP A OD2 1 
ATOM   746  N  N   . VAL A 1 97  ? -1.507  -4.820  6.712   1.00 12.91  ? 97   VAL A N   1 
ATOM   747  C  CA  . VAL A 1 97  ? -2.535  -5.568  7.394   1.00 12.61  ? 97   VAL A CA  1 
ATOM   748  C  C   . VAL A 1 97  ? -2.186  -7.053  7.258   1.00 13.16  ? 97   VAL A C   1 
ATOM   749  O  O   . VAL A 1 97  ? -1.887  -7.542  6.163   1.00 12.60  ? 97   VAL A O   1 
ATOM   750  C  CB  . VAL A 1 97  ? -3.907  -5.285  6.793   1.00 12.20  ? 97   VAL A CB  1 
ATOM   751  C  CG1 . VAL A 1 97  ? -4.977  -6.101  7.535   1.00 12.41  ? 97   VAL A CG1 1 
ATOM   752  C  CG2 . VAL A 1 97  ? -4.214  -3.765  6.842   1.00 12.99  ? 97   VAL A CG2 1 
ATOM   753  N  N   . SER A 1 98  ? -2.218  -7.757  8.384   1.00 13.30  ? 98   SER A N   1 
ATOM   754  C  CA  . SER A 1 98  ? -2.137  -9.216  8.389   1.00 14.20  ? 98   SER A CA  1 
ATOM   755  C  C   . SER A 1 98  ? -2.919  -9.742  9.581   1.00 14.16  ? 98   SER A C   1 
ATOM   756  O  O   . SER A 1 98  ? -2.449  -9.690  10.717  1.00 15.24  ? 98   SER A O   1 
ATOM   757  C  CB  . SER A 1 98  ? -0.686  -9.704  8.437   1.00 15.62  ? 98   SER A CB  1 
ATOM   758  O  OG  . SER A 1 98  ? -0.636  -11.114 8.206   1.00 18.66  ? 98   SER A OG  1 
ATOM   759  N  N   . ILE A 1 99  ? -4.127  -10.217 9.308   1.00 13.17  ? 99   ILE A N   1 
ATOM   760  C  CA  . ILE A 1 99  ? -5.085  -10.610 10.342  1.00 12.86  ? 99   ILE A CA  1 
ATOM   761  C  C   . ILE A 1 99  ? -5.650  -11.985 10.002  1.00 12.85  ? 99   ILE A C   1 
ATOM   762  O  O   . ILE A 1 99  ? -5.879  -12.306 8.837   1.00 12.16  ? 99   ILE A O   1 
ATOM   763  C  CB  . ILE A 1 99  ? -6.247  -9.582  10.406  1.00 13.00  ? 99   ILE A CB  1 
ATOM   764  C  CG1 . ILE A 1 99  ? -5.733  -8.263  10.959  1.00 14.18  ? 99   ILE A CG1 1 
ATOM   765  C  CG2 . ILE A 1 99  ? -7.417  -10.096 11.235  1.00 14.27  ? 99   ILE A CG2 1 
ATOM   766  C  CD1 . ILE A 1 99  ? -6.719  -7.106  10.860  1.00 15.56  ? 99   ILE A CD1 1 
ATOM   767  N  N   . GLU A 1 100 ? -5.830  -12.809 11.027  1.00 13.34  ? 100  GLU A N   1 
ATOM   768  C  CA  . GLU A 1 100 ? -6.626  -14.011 10.909  1.00 13.62  ? 100  GLU A CA  1 
ATOM   769  C  C   . GLU A 1 100 ? -7.696  -13.866 11.966  1.00 12.94  ? 100  GLU A C   1 
ATOM   770  O  O   . GLU A 1 100 ? -7.381  -13.604 13.130  1.00 13.89  ? 100  GLU A O   1 
ATOM   771  C  CB  . GLU A 1 100 ? -5.797  -15.270 11.136  1.00 15.42  ? 100  GLU A CB  1 
ATOM   772  C  CG  . GLU A 1 100 ? -6.606  -16.534 10.945  1.00 18.73  ? 100  GLU A CG  1 
ATOM   773  C  CD  A GLU A 1 100 ? -5.787  -17.795 11.171  0.50 21.77  ? 100  GLU A CD  1 
ATOM   774  C  CD  B GLU A 1 100 ? -5.774  -17.793 11.019  0.50 21.08  ? 100  GLU A CD  1 
ATOM   775  O  OE1 A GLU A 1 100 ? -4.685  -17.915 10.580  0.50 23.74  ? 100  GLU A OE1 1 
ATOM   776  O  OE1 B GLU A 1 100 ? -6.154  -18.772 10.340  0.50 22.37  ? 100  GLU A OE1 1 
ATOM   777  O  OE2 A GLU A 1 100 ? -6.249  -18.668 11.951  0.50 23.48  ? 100  GLU A OE2 1 
ATOM   778  O  OE2 B GLU A 1 100 ? -4.741  -17.812 11.730  0.50 22.13  ? 100  GLU A OE2 1 
ATOM   779  N  N   . ASP A 1 101 ? -8.952  -14.021 11.556  1.00 11.25  ? 101  ASP A N   1 
ATOM   780  C  CA  . ASP A 1 101 ? -10.071 -13.777 12.451  1.00 11.23  ? 101  ASP A CA  1 
ATOM   781  C  C   . ASP A 1 101 ? -11.068 -14.901 12.406  1.00 11.13  ? 101  ASP A C   1 
ATOM   782  O  O   . ASP A 1 101 ? -11.357 -15.422 11.347  1.00 11.27  ? 101  ASP A O   1 
ATOM   783  C  CB  . ASP A 1 101 ? -10.774 -12.461 12.096  1.00 10.94  ? 101  ASP A CB  1 
ATOM   784  C  CG  . ASP A 1 101 ? -11.654 -11.973 13.224  1.00 11.81  ? 101  ASP A CG  1 
ATOM   785  O  OD1 . ASP A 1 101 ? -11.086 -11.498 14.241  1.00 14.83  ? 101  ASP A OD1 1 
ATOM   786  O  OD2 . ASP A 1 101 ? -12.890 -12.103 13.129  1.00 12.33  ? 101  ASP A OD2 1 
ATOM   787  N  N   . SER A 1 102 ? -11.607 -15.236 13.576  1.00 11.80  ? 102  SER A N   1 
ATOM   788  C  CA  . SER A 1 102 ? -12.537 -16.345 13.756  1.00 12.36  ? 102  SER A CA  1 
ATOM   789  C  C   . SER A 1 102 ? -14.003 -15.906 13.825  1.00 12.04  ? 102  SER A C   1 
ATOM   790  O  O   . SER A 1 102 ? -14.900 -16.742 13.831  1.00 12.79  ? 102  SER A O   1 
ATOM   791  C  CB  A SER A 1 102 ? -12.214 -17.123 15.035  0.50 13.62  ? 102  SER A CB  1 
ATOM   792  C  CB  B SER A 1 102 ? -12.161 -17.131 15.020  0.50 13.61  ? 102  SER A CB  1 
ATOM   793  O  OG  A SER A 1 102 ? -10.980 -17.790 14.937  0.50 14.71  ? 102  SER A OG  1 
ATOM   794  O  OG  B SER A 1 102 ? -12.032 -16.268 16.143  0.50 13.82  ? 102  SER A OG  1 
ATOM   795  N  N   . VAL A 1 103 ? -14.259 -14.609 13.904  1.00 10.44  ? 103  VAL A N   1 
ATOM   796  C  CA  . VAL A 1 103 ? -15.626 -14.132 14.090  1.00 10.21  ? 103  VAL A CA  1 
ATOM   797  C  C   . VAL A 1 103 ? -16.279 -13.608 12.797  1.00 9.58   ? 103  VAL A C   1 
ATOM   798  O  O   . VAL A 1 103 ? -17.439 -13.896 12.517  1.00 10.43  ? 103  VAL A O   1 
ATOM   799  C  CB  . VAL A 1 103 ? -15.659 -13.081 15.202  1.00 10.19  ? 103  VAL A CB  1 
ATOM   800  C  CG1 . VAL A 1 103 ? -17.041 -12.427 15.314  1.00 11.44  ? 103  VAL A CG1 1 
ATOM   801  C  CG2 . VAL A 1 103 ? -15.226 -13.739 16.522  1.00 11.40  ? 103  VAL A CG2 1 
ATOM   802  N  N   . ILE A 1 104 ? -15.531 -12.872 11.991  1.00 8.85   ? 104  ILE A N   1 
ATOM   803  C  CA  . ILE A 1 104 ? -16.025 -12.504 10.664  1.00 8.50   ? 104  ILE A CA  1 
ATOM   804  C  C   . ILE A 1 104 ? -16.134 -13.740 9.771   1.00 8.08   ? 104  ILE A C   1 
ATOM   805  O  O   . ILE A 1 104 ? -15.473 -14.767 10.006  1.00 8.85   ? 104  ILE A O   1 
ATOM   806  C  CB  . ILE A 1 104 ? -15.163 -11.412 9.972   1.00 8.31   ? 104  ILE A CB  1 
ATOM   807  C  CG1 . ILE A 1 104 ? -13.719 -11.895 9.744   1.00 9.21   ? 104  ILE A CG1 1 
ATOM   808  C  CG2 . ILE A 1 104 ? -15.174 -10.127 10.815  1.00 8.49   ? 104  ILE A CG2 1 
ATOM   809  C  CD1 . ILE A 1 104 ? -12.857 -10.914 8.917   1.00 9.99   ? 104  ILE A CD1 1 
ATOM   810  N  N   . SER A 1 105 ? -17.005 -13.640 8.764   1.00 8.22   ? 105  SER A N   1 
ATOM   811  C  CA  . SER A 1 105 ? -17.177 -14.686 7.752   1.00 8.11   ? 105  SER A CA  1 
ATOM   812  C  C   . SER A 1 105 ? -17.562 -14.008 6.442   1.00 8.03   ? 105  SER A C   1 
ATOM   813  O  O   . SER A 1 105 ? -18.180 -12.954 6.451   1.00 8.30   ? 105  SER A O   1 
ATOM   814  C  CB  . SER A 1 105 ? -18.266 -15.692 8.178   1.00 8.70   ? 105  SER A CB  1 
ATOM   815  O  OG  . SER A 1 105 ? -18.345 -16.765 7.250   1.00 10.21  ? 105  SER A OG  1 
ATOM   816  N  N   . LEU A 1 106 ? -17.205 -14.630 5.326   1.00 8.25   ? 106  LEU A N   1 
ATOM   817  C  CA  . LEU A 1 106 ? -17.625 -14.154 4.001   1.00 8.45   ? 106  LEU A CA  1 
ATOM   818  C  C   . LEU A 1 106 ? -18.876 -14.869 3.492   1.00 9.93   ? 106  LEU A C   1 
ATOM   819  O  O   . LEU A 1 106 ? -19.335 -14.558 2.397   1.00 10.73  ? 106  LEU A O   1 
ATOM   820  C  CB  . LEU A 1 106 ? -16.489 -14.347 2.979   1.00 8.41   ? 106  LEU A CB  1 
ATOM   821  C  CG  . LEU A 1 106 ? -15.101 -13.851 3.404   1.00 7.67   ? 106  LEU A CG  1 
ATOM   822  C  CD1 . LEU A 1 106 ? -14.067 -14.064 2.277   1.00 9.37   ? 106  LEU A CD1 1 
ATOM   823  C  CD2 . LEU A 1 106 ? -15.181 -12.376 3.841   1.00 9.27   ? 106  LEU A CD2 1 
ATOM   824  N  N   . SER A 1 107 ? -19.410 -15.809 4.283   1.00 11.04  ? 107  SER A N   1 
ATOM   825  C  CA  . SER A 1 107 ? -20.579 -16.592 3.914   1.00 12.81  ? 107  SER A CA  1 
ATOM   826  C  C   . SER A 1 107 ? -21.614 -16.638 5.026   1.00 12.85  ? 107  SER A C   1 
ATOM   827  O  O   . SER A 1 107 ? -21.298 -16.406 6.195   1.00 13.58  ? 107  SER A O   1 
ATOM   828  C  CB  . SER A 1 107 ? -20.158 -18.028 3.607   1.00 13.85  ? 107  SER A CB  1 
ATOM   829  O  OG  . SER A 1 107 ? -19.500 -18.093 2.377   1.00 16.89  ? 107  SER A OG  1 
ATOM   830  N  N   . GLY A 1 108 ? -22.849 -16.932 4.656   1.00 12.82  ? 108  GLY A N   1 
ATOM   831  C  CA  . GLY A 1 108 ? -23.925 -17.132 5.615   1.00 13.40  ? 108  GLY A CA  1 
ATOM   832  C  C   . GLY A 1 108 ? -24.648 -15.862 6.017   1.00 13.43  ? 108  GLY A C   1 
ATOM   833  O  O   . GLY A 1 108 ? -24.440 -14.796 5.434   1.00 12.66  ? 108  GLY A O   1 
ATOM   834  N  N   . ASP A 1 109 ? -25.492 -15.985 7.035   1.00 14.57  ? 109  ASP A N   1 
ATOM   835  C  CA  . ASP A 1 109 ? -26.431 -14.947 7.430   1.00 15.79  ? 109  ASP A CA  1 
ATOM   836  C  C   . ASP A 1 109 ? -25.800 -13.598 7.764   1.00 15.90  ? 109  ASP A C   1 
ATOM   837  O  O   . ASP A 1 109 ? -26.397 -12.529 7.521   1.00 17.84  ? 109  ASP A O   1 
ATOM   838  C  CB  . ASP A 1 109 ? -27.220 -15.415 8.659   1.00 16.43  ? 109  ASP A CB  1 
ATOM   839  C  CG  . ASP A 1 109 ? -28.106 -16.597 8.362   0.50 17.48  ? 109  ASP A CG  1 
ATOM   840  O  OD1 . ASP A 1 109 ? -28.838 -16.532 7.356   0.50 18.17  ? 109  ASP A OD1 1 
ATOM   841  O  OD2 . ASP A 1 109 ? -28.073 -17.584 9.131   0.50 19.28  ? 109  ASP A OD2 1 
ATOM   842  N  N   . HIS A 1 110 ? -24.612 -13.645 8.347   1.00 15.52  ? 110  HIS A N   1 
ATOM   843  C  CA  . HIS A 1 110 ? -23.938 -12.426 8.786   1.00 15.13  ? 110  HIS A CA  1 
ATOM   844  C  C   . HIS A 1 110 ? -22.665 -12.115 8.021   1.00 14.03  ? 110  HIS A C   1 
ATOM   845  O  O   . HIS A 1 110 ? -21.732 -11.546 8.584   1.00 13.53  ? 110  HIS A O   1 
ATOM   846  C  CB  . HIS A 1 110 ? -23.616 -12.542 10.264  1.00 15.93  ? 110  HIS A CB  1 
ATOM   847  C  CG  . HIS A 1 110 ? -24.821 -12.711 11.113  1.00 17.90  ? 110  HIS A CG  1 
ATOM   848  N  ND1 . HIS A 1 110 ? -24.796 -13.396 12.310  1.00 21.63  ? 110  HIS A ND1 1 
ATOM   849  C  CD2 . HIS A 1 110 ? -26.100 -12.311 10.928  1.00 19.17  ? 110  HIS A CD2 1 
ATOM   850  C  CE1 . HIS A 1 110 ? -26.008 -13.391 12.834  1.00 21.83  ? 110  HIS A CE1 1 
ATOM   851  N  NE2 . HIS A 1 110 ? -26.818 -12.746 12.012  1.00 20.55  ? 110  HIS A NE2 1 
ATOM   852  N  N   . ALA A 1 111 ? -22.635 -12.476 6.746   1.00 13.02  ? 111  ALA A N   1 
ATOM   853  C  CA  . ALA A 1 111 ? -21.442 -12.321 5.912   1.00 12.10  ? 111  ALA A CA  1 
ATOM   854  C  C   . ALA A 1 111 ? -21.032 -10.855 5.895   1.00 11.53  ? 111  ALA A C   1 
ATOM   855  O  O   . ALA A 1 111 ? -21.896 -9.987  5.851   1.00 12.60  ? 111  ALA A O   1 
ATOM   856  C  CB  . ALA A 1 111 ? -21.725 -12.808 4.513   1.00 12.94  ? 111  ALA A CB  1 
ATOM   857  N  N   . ILE A 1 112 ? -19.733 -10.580 5.943   1.00 10.70  ? 112  ILE A N   1 
ATOM   858  C  CA  . ILE A 1 112 ? -19.253 -9.187  5.857   1.00 9.96   ? 112  ILE A CA  1 
ATOM   859  C  C   . ILE A 1 112 ? -19.202 -8.635  4.431   1.00 10.21  ? 112  ILE A C   1 
ATOM   860  O  O   . ILE A 1 112 ? -19.003 -7.445  4.245   1.00 9.73   ? 112  ILE A O   1 
ATOM   861  C  CB  . ILE A 1 112 ? -17.895 -8.961  6.559   1.00 9.65   ? 112  ILE A CB  1 
ATOM   862  C  CG1 . ILE A 1 112 ? -16.762 -9.793  5.938   1.00 9.29   ? 112  ILE A CG1 1 
ATOM   863  C  CG2 . ILE A 1 112 ? -18.050 -9.196  8.061   1.00 10.90  ? 112  ILE A CG2 1 
ATOM   864  C  CD1 . ILE A 1 112 ? -15.372 -9.402  6.474   1.00 10.12  ? 112  ILE A CD1 1 
ATOM   865  N  N   . ILE A 1 113 ? -19.381 -9.493  3.429   1.00 10.75  ? 113  ILE A N   1 
ATOM   866  C  CA  . ILE A 1 113 ? -19.478 -9.017  2.057   1.00 11.72  ? 113  ILE A CA  1 
ATOM   867  C  C   . ILE A 1 113 ? -20.627 -8.035  1.935   1.00 11.83  ? 113  ILE A C   1 
ATOM   868  O  O   . ILE A 1 113 ? -21.736 -8.298  2.428   1.00 13.75  ? 113  ILE A O   1 
ATOM   869  C  CB  . ILE A 1 113 ? -19.760 -10.177 1.092   1.00 12.96  ? 113  ILE A CB  1 
ATOM   870  C  CG1 . ILE A 1 113 ? -18.645 -11.200 1.149   1.00 14.74  ? 113  ILE A CG1 1 
ATOM   871  C  CG2 . ILE A 1 113 ? -19.990 -9.659  -0.334  1.00 14.18  ? 113  ILE A CG2 1 
ATOM   872  C  CD1 . ILE A 1 113 ? -17.316 -10.661 0.926   1.00 15.01  ? 113  ILE A CD1 1 
ATOM   873  N  N   . GLY A 1 114 ? -20.375 -6.895  1.297   1.00 10.92  ? 114  GLY A N   1 
ATOM   874  C  CA  . GLY A 1 114 ? -21.387 -5.886  1.133   1.00 11.28  ? 114  GLY A CA  1 
ATOM   875  C  C   . GLY A 1 114 ? -21.325 -4.821  2.214   1.00 10.90  ? 114  GLY A C   1 
ATOM   876  O  O   . GLY A 1 114 ? -21.902 -3.756  2.041   1.00 11.06  ? 114  GLY A O   1 
ATOM   877  N  N   . ARG A 1 115 ? -20.645 -5.117  3.329   1.00 10.45  ? 115  ARG A N   1 
ATOM   878  C  CA  . ARG A 1 115 ? -20.474 -4.159  4.428   1.00 10.17  ? 115  ARG A CA  1 
ATOM   879  C  C   . ARG A 1 115 ? -19.279 -3.263  4.114   1.00 9.65   ? 115  ARG A C   1 
ATOM   880  O  O   . ARG A 1 115 ? -18.623 -3.439  3.096   1.00 10.50  ? 115  ARG A O   1 
ATOM   881  C  CB  . ARG A 1 115 ? -20.266 -4.880  5.761   1.00 10.18  ? 115  ARG A CB  1 
ATOM   882  C  CG  . ARG A 1 115 ? -21.327 -5.929  6.115   1.00 12.32  ? 115  ARG A CG  1 
ATOM   883  C  CD  . ARG A 1 115 ? -22.645 -5.311  6.446   1.00 12.72  ? 115  ARG A CD  1 
ATOM   884  N  NE  . ARG A 1 115 ? -23.696 -6.303  6.681   1.00 14.74  ? 115  ARG A NE  1 
ATOM   885  C  CZ  . ARG A 1 115 ? -24.862 -6.024  7.250   1.00 14.21  ? 115  ARG A CZ  1 
ATOM   886  N  NH1 . ARG A 1 115 ? -25.145 -4.778  7.637   1.00 14.71  ? 115  ARG A NH1 1 
ATOM   887  N  NH2 . ARG A 1 115 ? -25.764 -6.979  7.412   1.00 16.10  ? 115  ARG A NH2 1 
ATOM   888  N  N   . THR A 1 116 ? -18.985 -2.324  5.006   1.00 9.36   ? 116  THR A N   1 
ATOM   889  C  CA  . THR A 1 116 ? -18.005 -1.285  4.719   1.00 9.72   ? 116  THR A CA  1 
ATOM   890  C  C   . THR A 1 116 ? -16.778 -1.439  5.606   1.00 9.36   ? 116  THR A C   1 
ATOM   891  O  O   . THR A 1 116 ? -16.887 -1.443  6.818   1.00 10.35  ? 116  THR A O   1 
ATOM   892  C  CB  . THR A 1 116 ? -18.633 0.108   4.926   1.00 10.72  ? 116  THR A CB  1 
ATOM   893  O  OG1 . THR A 1 116 ? -19.773 0.244   4.063   1.00 13.07  ? 116  THR A OG1 1 
ATOM   894  C  CG2 . THR A 1 116 ? -17.615 1.189   4.606   1.00 10.94  ? 116  THR A CG2 1 
ATOM   895  N  N   . LEU A 1 117 ? -15.612 -1.609  4.987   1.00 9.07   ? 117  LEU A N   1 
ATOM   896  C  CA  . LEU A 1 117 ? -14.355 -1.606  5.720   1.00 8.32   ? 117  LEU A CA  1 
ATOM   897  C  C   . LEU A 1 117 ? -13.937 -0.173  5.979   1.00 8.65   ? 117  LEU A C   1 
ATOM   898  O  O   . LEU A 1 117 ? -14.039 0.677   5.072   1.00 9.62   ? 117  LEU A O   1 
ATOM   899  C  CB  . LEU A 1 117 ? -13.257 -2.329  4.926   1.00 7.58   ? 117  LEU A CB  1 
ATOM   900  C  CG  . LEU A 1 117 ? -11.984 -2.659  5.686   1.00 7.58   ? 117  LEU A CG  1 
ATOM   901  C  CD1 . LEU A 1 117 ? -12.254 -3.613  6.881   1.00 8.24   ? 117  LEU A CD1 1 
ATOM   902  C  CD2 . LEU A 1 117 ? -10.971 -3.243  4.711   1.00 10.18  ? 117  LEU A CD2 1 
ATOM   903  N  N   . VAL A 1 118 ? -13.427 0.078   7.190   1.00 8.52   ? 118  VAL A N   1 
ATOM   904  C  CA  . VAL A 1 118 ? -13.083 1.426   7.657   1.00 8.35   ? 118  VAL A CA  1 
ATOM   905  C  C   . VAL A 1 118 ? -11.721 1.460   8.368   1.00 8.80   ? 118  VAL A C   1 
ATOM   906  O  O   . VAL A 1 118 ? -11.434 0.625   9.225   1.00 9.48   ? 118  VAL A O   1 
ATOM   907  C  CB  . VAL A 1 118 ? -14.171 1.945   8.637   1.00 8.14   ? 118  VAL A CB  1 
ATOM   908  C  CG1 . VAL A 1 118 ? -13.794 3.283   9.200   1.00 9.85   ? 118  VAL A CG1 1 
ATOM   909  C  CG2 . VAL A 1 118 ? -15.521 2.070   7.961   1.00 10.18  ? 118  VAL A CG2 1 
ATOM   910  N  N   . VAL A 1 119 ? -10.879 2.425   7.997   1.00 9.05   ? 119  VAL A N   1 
ATOM   911  C  CA  . VAL A 1 119 ? -9.676  2.736   8.764   1.00 9.60   ? 119  VAL A CA  1 
ATOM   912  C  C   . VAL A 1 119 ? -9.844  4.139   9.357   1.00 10.20  ? 119  VAL A C   1 
ATOM   913  O  O   . VAL A 1 119 ? -10.270 5.084   8.676   1.00 9.74   ? 119  VAL A O   1 
ATOM   914  C  CB  . VAL A 1 119 ? -8.363  2.561   7.944   1.00 9.76   ? 119  VAL A CB  1 
ATOM   915  C  CG1 . VAL A 1 119 ? -8.323  3.515   6.782   1.00 10.89  ? 119  VAL A CG1 1 
ATOM   916  C  CG2 . VAL A 1 119 ? -7.150  2.752   8.849   1.00 11.06  ? 119  VAL A CG2 1 
ATOM   917  N  N   . SER A 1 120 ? -9.522  4.257   10.641  1.00 10.44  ? 120  SER A N   1 
ATOM   918  C  CA  . SER A 1 120 ? -9.820  5.445   11.426  1.00 10.58  ? 120  SER A CA  1 
ATOM   919  C  C   . SER A 1 120 ? -8.581  6.238   11.807  1.00 11.59  ? 120  SER A C   1 
ATOM   920  O  O   . SER A 1 120 ? -7.435  5.794   11.645  1.00 12.36  ? 120  SER A O   1 
ATOM   921  C  CB  . SER A 1 120 ? -10.620 5.072   12.684  1.00 10.70  ? 120  SER A CB  1 
ATOM   922  O  OG  . SER A 1 120 ? -11.887 4.541   12.324  1.00 11.92  ? 120  SER A OG  1 
ATOM   923  N  N   . GLU A 1 121 ? -8.846  7.427   12.323  1.00 12.79  ? 121  GLU A N   1 
ATOM   924  C  CA  . GLU A 1 121 ? -7.830  8.455   12.578  1.00 13.56  ? 121  GLU A CA  1 
ATOM   925  C  C   . GLU A 1 121 ? -6.886  8.119   13.728  1.00 13.98  ? 121  GLU A C   1 
ATOM   926  O  O   . GLU A 1 121 ? -5.702  8.492   13.703  1.00 14.93  ? 121  GLU A O   1 
ATOM   927  C  CB  . GLU A 1 121 ? -8.554  9.768   12.888  1.00 14.75  ? 121  GLU A CB  1 
ATOM   928  C  CG  . GLU A 1 121 ? -7.695  10.974  13.218  1.00 17.15  ? 121  GLU A CG  1 
ATOM   929  C  CD  . GLU A 1 121 ? -8.512  12.104  13.831  1.00 18.52  ? 121  GLU A CD  1 
ATOM   930  O  OE1 . GLU A 1 121 ? -9.711  11.894  14.111  1.00 17.55  ? 121  GLU A OE1 1 
ATOM   931  O  OE2 . GLU A 1 121 ? -7.958  13.204  14.031  1.00 23.66  ? 121  GLU A OE2 1 
ATOM   932  N  N   . LYS A 1 122 ? -7.433  7.455   14.744  1.00 13.77  ? 122  LYS A N   1 
ATOM   933  C  CA  . LYS A 1 122 ? -6.732  7.192   15.999  1.00 14.31  ? 122  LYS A CA  1 
ATOM   934  C  C   . LYS A 1 122 ? -6.819  5.728   16.325  1.00 13.11  ? 122  LYS A C   1 
ATOM   935  O  O   . LYS A 1 122 ? -7.531  4.972   15.655  1.00 12.38  ? 122  LYS A O   1 
ATOM   936  C  CB  . LYS A 1 122 ? -7.376  7.975   17.159  1.00 15.10  ? 122  LYS A CB  1 
ATOM   937  C  CG  . LYS A 1 122 ? -7.510  9.458   16.919  1.00 16.56  ? 122  LYS A CG  1 
ATOM   938  C  CD  . LYS A 1 122 ? -8.184  10.185  18.066  0.50 17.34  ? 122  LYS A CD  1 
ATOM   939  C  CE  . LYS A 1 122 ? -8.330  11.662  17.715  0.50 18.59  ? 122  LYS A CE  1 
ATOM   940  N  NZ  . LYS A 1 122 ? -8.670  12.557  18.867  1.00 19.85  ? 122  LYS A NZ  1 
ATOM   941  N  N   . ALA A 1 123 ? -6.119  5.338   17.382  1.00 13.13  ? 123  ALA A N   1 
ATOM   942  C  CA  . ALA A 1 123 ? -6.218  3.987   17.929  1.00 12.86  ? 123  ALA A CA  1 
ATOM   943  C  C   . ALA A 1 123 ? -7.619  3.649   18.415  1.00 12.79  ? 123  ALA A C   1 
ATOM   944  O  O   . ALA A 1 123 ? -8.270  4.450   19.079  1.00 13.58  ? 123  ALA A O   1 
ATOM   945  C  CB  . ALA A 1 123 ? -5.251  3.801   19.062  1.00 13.44  ? 123  ALA A CB  1 
ATOM   946  N  N   . ASP A 1 124 ? -8.061  2.444   18.089  1.00 12.33  ? 124  ASP A N   1 
ATOM   947  C  CA  . ASP A 1 124 ? -9.204  1.826   18.740  1.00 12.22  ? 124  ASP A CA  1 
ATOM   948  C  C   . ASP A 1 124 ? -8.762  1.460   20.159  1.00 12.80  ? 124  ASP A C   1 
ATOM   949  O  O   . ASP A 1 124 ? -7.753  0.785   20.331  1.00 13.33  ? 124  ASP A O   1 
ATOM   950  C  CB  . ASP A 1 124 ? -9.586  0.577   17.930  1.00 11.86  ? 124  ASP A CB  1 
ATOM   951  C  CG  . ASP A 1 124 ? -10.758 -0.214  18.508  1.00 12.41  ? 124  ASP A CG  1 
ATOM   952  O  OD1 . ASP A 1 124 ? -11.156 -0.070  19.689  1.00 12.71  ? 124  ASP A OD1 1 
ATOM   953  O  OD2 . ASP A 1 124 ? -11.272 -1.051  17.735  1.00 14.01  ? 124  ASP A OD2 1 
ATOM   954  N  N   . ASP A 1 125 ? -9.493  1.919   21.180  1.00 12.42  ? 125  ASP A N   1 
ATOM   955  C  CA  . ASP A 1 125 ? -9.111  1.624   22.572  1.00 13.64  ? 125  ASP A CA  1 
ATOM   956  C  C   . ASP A 1 125 ? -9.553  0.240   23.063  1.00 13.39  ? 125  ASP A C   1 
ATOM   957  O  O   . ASP A 1 125 ? -9.354  -0.115  24.239  1.00 14.06  ? 125  ASP A O   1 
ATOM   958  C  CB  . ASP A 1 125 ? -9.546  2.749   23.534  1.00 14.15  ? 125  ASP A CB  1 
ATOM   959  C  CG  . ASP A 1 125 ? -11.052 2.845   23.730  1.00 14.29  ? 125  ASP A CG  1 
ATOM   960  O  OD1 . ASP A 1 125 ? -11.781 1.869   23.455  1.00 13.03  ? 125  ASP A OD1 1 
ATOM   961  O  OD2 . ASP A 1 125 ? -11.506 3.908   24.211  1.00 15.26  ? 125  ASP A OD2 1 
ATOM   962  N  N   . LEU A 1 126 ? -10.140 -0.540  22.155  1.00 12.83  ? 126  LEU A N   1 
ATOM   963  C  CA  . LEU A 1 126 ? -10.464 -1.944  22.372  1.00 13.11  ? 126  LEU A CA  1 
ATOM   964  C  C   . LEU A 1 126 ? -11.526 -2.144  23.447  1.00 14.03  ? 126  LEU A C   1 
ATOM   965  O  O   . LEU A 1 126 ? -11.649 -3.233  24.033  1.00 14.58  ? 126  LEU A O   1 
ATOM   966  C  CB  . LEU A 1 126 ? -9.197  -2.769  22.658  1.00 13.26  ? 126  LEU A CB  1 
ATOM   967  C  CG  . LEU A 1 126 ? -8.025  -2.639  21.680  1.00 14.48  ? 126  LEU A CG  1 
ATOM   968  C  CD1 . LEU A 1 126 ? -6.936  -3.644  22.054  1.00 14.97  ? 126  LEU A CD1 1 
ATOM   969  C  CD2 . LEU A 1 126 ? -8.458  -2.836  20.234  1.00 14.11  ? 126  LEU A CD2 1 
ATOM   970  N  N   . GLY A 1 127 ? -12.307 -1.093  23.680  1.00 14.50  ? 127  GLY A N   1 
ATOM   971  C  CA  . GLY A 1 127 ? -13.397 -1.143  24.637  1.00 15.53  ? 127  GLY A CA  1 
ATOM   972  C  C   . GLY A 1 127 ? -12.946 -1.013  26.072  1.00 17.58  ? 127  GLY A C   1 
ATOM   973  O  O   . GLY A 1 127 ? -13.752 -1.227  26.978  1.00 18.88  ? 127  GLY A O   1 
ATOM   974  N  N   . LYS A 1 128 ? -11.682 -0.628  26.285  1.00 18.49  ? 128  LYS A N   1 
ATOM   975  C  CA  . LYS A 1 128 ? -11.082 -0.571  27.623  1.00 20.33  ? 128  LYS A CA  1 
ATOM   976  C  C   . LYS A 1 128 ? -10.952 0.872   28.126  1.00 20.53  ? 128  LYS A C   1 
ATOM   977  O  O   . LYS A 1 128 ? -10.323 1.124   29.155  1.00 22.28  ? 128  LYS A O   1 
ATOM   978  C  CB  . LYS A 1 128 ? -9.725  -1.295  27.650  1.00 21.08  ? 128  LYS A CB  1 
ATOM   979  C  CG  . LYS A 1 128 ? -9.794  -2.648  26.973  1.00 23.04  ? 128  LYS A CG  1 
ATOM   980  C  CD  A LYS A 1 128 ? -8.680  -3.562  27.512  0.50 24.71  ? 128  LYS A CD  1 
ATOM   981  C  CD  B LYS A 1 128 ? -8.785  -3.673  27.431  0.50 24.76  ? 128  LYS A CD  1 
ATOM   982  C  CE  A LYS A 1 128 ? -8.426  -4.792  26.636  0.50 24.42  ? 128  LYS A CE  1 
ATOM   983  C  CE  B LYS A 1 128 ? -9.294  -5.081  27.067  0.50 24.66  ? 128  LYS A CE  1 
ATOM   984  N  NZ  A LYS A 1 128 ? -7.317  -4.602  25.659  0.50 23.97  ? 128  LYS A NZ  1 
ATOM   985  N  NZ  B LYS A 1 128 ? -10.005 -5.128  25.731  0.50 23.53  ? 128  LYS A NZ  1 
ATOM   986  N  N   . GLY A 1 129 ? -11.559 1.807   27.395  1.00 19.70  ? 129  GLY A N   1 
ATOM   987  C  CA  . GLY A 1 129 ? -11.614 3.202   27.766  1.00 20.01  ? 129  GLY A CA  1 
ATOM   988  C  C   . GLY A 1 129 ? -12.602 3.465   28.896  1.00 20.28  ? 129  GLY A C   1 
ATOM   989  O  O   . GLY A 1 129 ? -13.335 2.567   29.351  1.00 21.41  ? 129  GLY A O   1 
ATOM   990  N  N   . GLY A 1 130 ? -12.640 4.714   29.328  1.00 19.78  ? 130  GLY A N   1 
ATOM   991  C  CA  . GLY A 1 130 ? -13.394 5.102   30.518  1.00 19.32  ? 130  GLY A CA  1 
ATOM   992  C  C   . GLY A 1 130 ? -14.752 5.736   30.292  1.00 17.98  ? 130  GLY A C   1 
ATOM   993  O  O   . GLY A 1 130 ? -15.233 6.434   31.154  1.00 18.72  ? 130  GLY A O   1 
ATOM   994  N  N   . ASN A 1 131 ? -15.368 5.503   29.140  1.00 15.51  ? 131  ASN A N   1 
ATOM   995  C  CA  . ASN A 1 131 ? -16.735 5.961   28.895  1.00 14.51  ? 131  ASN A CA  1 
ATOM   996  C  C   . ASN A 1 131 ? -17.547 4.949   28.109  1.00 13.96  ? 131  ASN A C   1 
ATOM   997  O  O   . ASN A 1 131 ? -17.006 3.963   27.590  1.00 13.68  ? 131  ASN A O   1 
ATOM   998  C  CB  . ASN A 1 131 ? -16.782 7.343   28.203  1.00 14.40  ? 131  ASN A CB  1 
ATOM   999  C  CG  . ASN A 1 131 ? -16.142 7.367   26.832  1.00 13.25  ? 131  ASN A CG  1 
ATOM   1000 O  OD1 . ASN A 1 131 ? -15.712 6.344   26.304  1.00 13.64  ? 131  ASN A OD1 1 
ATOM   1001 N  ND2 . ASN A 1 131 ? -16.075 8.570   26.238  1.00 13.06  ? 131  ASN A ND2 1 
ATOM   1002 N  N   . GLU A 1 132 ? -18.842 5.199   27.997  1.00 14.43  ? 132  GLU A N   1 
ATOM   1003 C  CA  . GLU A 1 132 ? -19.707 4.305   27.227  1.00 14.37  ? 132  GLU A CA  1 
ATOM   1004 C  C   . GLU A 1 132 ? -19.334 4.265   25.757  1.00 13.49  ? 132  GLU A C   1 
ATOM   1005 O  O   . GLU A 1 132 ? -19.436 3.223   25.125  1.00 11.88  ? 132  GLU A O   1 
ATOM   1006 C  CB  . GLU A 1 132 ? -21.181 4.653   27.380  1.00 15.33  ? 132  GLU A CB  1 
ATOM   1007 C  CG  . GLU A 1 132 ? -22.094 3.600   26.776  1.00 17.20  ? 132  GLU A CG  1 
ATOM   1008 C  CD  . GLU A 1 132 ? -23.557 3.860   27.004  1.00 20.85  ? 132  GLU A CD  1 
ATOM   1009 O  OE1 . GLU A 1 132 ? -23.938 5.036   27.078  1.00 21.67  ? 132  GLU A OE1 1 
ATOM   1010 O  OE2 . GLU A 1 132 ? -24.323 2.874   27.116  1.00 25.81  ? 132  GLU A OE2 1 
ATOM   1011 N  N   . GLU A 1 133 ? -18.896 5.398   25.204  1.00 13.41  ? 133  GLU A N   1 
ATOM   1012 C  CA  . GLU A 1 133 ? -18.484 5.425   23.823  1.00 13.83  ? 133  GLU A CA  1 
ATOM   1013 C  C   . GLU A 1 133 ? -17.372 4.417   23.525  1.00 12.35  ? 133  GLU A C   1 
ATOM   1014 O  O   . GLU A 1 133 ? -17.359 3.818   22.441  1.00 11.81  ? 133  GLU A O   1 
ATOM   1015 C  CB  . GLU A 1 133 ? -18.031 6.828   23.453  1.00 14.63  ? 133  GLU A CB  1 
ATOM   1016 C  CG  . GLU A 1 133 ? -18.104 7.114   21.977  1.00 18.27  ? 133  GLU A CG  1 
ATOM   1017 C  CD  . GLU A 1 133 ? -19.470 6.825   21.357  1.00 22.57  ? 133  GLU A CD  1 
ATOM   1018 O  OE1 . GLU A 1 133 ? -20.510 7.079   22.005  1.00 24.10  ? 133  GLU A OE1 1 
ATOM   1019 O  OE2 . GLU A 1 133 ? -19.482 6.324   20.216  1.00 27.80  ? 133  GLU A OE2 1 
ATOM   1020 N  N   . SER A 1 134 ? -16.464 4.186   24.480  1.00 12.54  ? 134  SER A N   1 
ATOM   1021 C  CA  . SER A 1 134 ? -15.437 3.152   24.298  1.00 12.34  ? 134  SER A CA  1 
ATOM   1022 C  C   . SER A 1 134 ? -16.079 1.802   23.955  1.00 11.63  ? 134  SER A C   1 
ATOM   1023 O  O   . SER A 1 134 ? -15.583 1.051   23.083  1.00 11.13  ? 134  SER A O   1 
ATOM   1024 C  CB  . SER A 1 134 ? -14.564 2.993   25.546  1.00 13.00  ? 134  SER A CB  1 
ATOM   1025 O  OG  . SER A 1 134 ? -13.620 1.945   25.354  1.00 13.69  ? 134  SER A OG  1 
ATOM   1026 N  N   . THR A 1 135 ? -17.179 1.501   24.648  1.00 11.52  ? 135  THR A N   1 
ATOM   1027 C  CA  . THR A 1 135 ? -17.928 0.252   24.464  1.00 12.09  ? 135  THR A CA  1 
ATOM   1028 C  C   . THR A 1 135 ? -18.808 0.234   23.217  1.00 11.48  ? 135  THR A C   1 
ATOM   1029 O  O   . THR A 1 135 ? -19.464 -0.772  22.949  1.00 10.40  ? 135  THR A O   1 
ATOM   1030 C  CB  . THR A 1 135 ? -18.822 -0.075  25.705  1.00 12.99  ? 135  THR A CB  1 
ATOM   1031 O  OG1 . THR A 1 135 ? -20.046 0.676   25.684  1.00 14.64  ? 135  THR A OG1 1 
ATOM   1032 C  CG2 . THR A 1 135 ? -18.053 0.186   27.015  1.00 14.50  ? 135  THR A CG2 1 
ATOM   1033 N  N   . LYS A 1 136 ? -18.827 1.334   22.456  1.00 11.66  ? 136  LYS A N   1 
ATOM   1034 C  CA  . LYS A 1 136 ? -19.574 1.377   21.195  1.00 12.20  ? 136  LYS A CA  1 
ATOM   1035 C  C   . LYS A 1 136 ? -18.634 1.423   19.987  1.00 11.85  ? 136  LYS A C   1 
ATOM   1036 O  O   . LYS A 1 136 ? -18.802 0.642   19.055  1.00 11.88  ? 136  LYS A O   1 
ATOM   1037 C  CB  . LYS A 1 136 ? -20.540 2.554   21.163  1.00 12.75  ? 136  LYS A CB  1 
ATOM   1038 C  CG  . LYS A 1 136 ? -21.568 2.570   22.271  1.00 14.33  ? 136  LYS A CG  1 
ATOM   1039 C  CD  . LYS A 1 136 ? -22.409 3.843   22.212  1.00 17.21  ? 136  LYS A CD  1 
ATOM   1040 C  CE  . LYS A 1 136 ? -23.547 3.860   23.224  0.50 19.27  ? 136  LYS A CE  1 
ATOM   1041 N  NZ  . LYS A 1 136 ? -24.325 2.587   23.261  0.50 21.08  ? 136  LYS A NZ  1 
ATOM   1042 N  N   . THR A 1 137 ? -17.637 2.310   20.015  1.00 11.66  ? 137  THR A N   1 
ATOM   1043 C  CA  . THR A 1 137 ? -16.755 2.539   18.858  1.00 11.99  ? 137  THR A CA  1 
ATOM   1044 C  C   . THR A 1 137 ? -15.264 2.428   19.138  1.00 11.91  ? 137  THR A C   1 
ATOM   1045 O  O   . THR A 1 137 ? -14.469 2.460   18.202  1.00 12.00  ? 137  THR A O   1 
ATOM   1046 C  CB  . THR A 1 137 ? -16.975 3.945   18.272  1.00 12.47  ? 137  THR A CB  1 
ATOM   1047 O  OG1 . THR A 1 137 ? -16.563 4.921   19.239  1.00 14.17  ? 137  THR A OG1 1 
ATOM   1048 C  CG2 . THR A 1 137 ? -18.459 4.140   17.902  1.00 14.42  ? 137  THR A CG2 1 
ATOM   1049 N  N   . GLY A 1 138 ? -14.861 2.332   20.406  1.00 11.83  ? 138  GLY A N   1 
ATOM   1050 C  CA  . GLY A 1 138 ? -13.440 2.322   20.735  1.00 12.33  ? 138  GLY A CA  1 
ATOM   1051 C  C   . GLY A 1 138 ? -12.753 3.683   20.643  1.00 12.77  ? 138  GLY A C   1 
ATOM   1052 O  O   . GLY A 1 138 ? -11.527 3.759   20.750  1.00 13.04  ? 138  GLY A O   1 
ATOM   1053 N  N   . ASN A 1 139 ? -13.525 4.751   20.419  1.00 12.89  ? 139  ASN A N   1 
ATOM   1054 C  CA  . ASN A 1 139 ? -12.985 6.125   20.398  1.00 13.66  ? 139  ASN A CA  1 
ATOM   1055 C  C   . ASN A 1 139 ? -11.820 6.331   19.428  1.00 13.65  ? 139  ASN A C   1 
ATOM   1056 O  O   . ASN A 1 139 ? -10.795 6.941   19.770  1.00 14.92  ? 139  ASN A O   1 
ATOM   1057 C  CB  . ASN A 1 139 ? -12.589 6.547   21.818  1.00 14.76  ? 139  ASN A CB  1 
ATOM   1058 C  CG  . ASN A 1 139 ? -13.785 6.645   22.741  1.00 15.40  ? 139  ASN A CG  1 
ATOM   1059 O  OD1 . ASN A 1 139 ? -14.800 7.234   22.373  1.00 17.41  ? 139  ASN A OD1 1 
ATOM   1060 N  ND2 . ASN A 1 139 ? -13.688 6.043   23.930  1.00 13.48  ? 139  ASN A ND2 1 
ATOM   1061 N  N   . ALA A 1 140 ? -11.997 5.832   18.209  1.00 12.70  ? 140  ALA A N   1 
ATOM   1062 C  CA  . ALA A 1 140 ? -10.925 5.826   17.204  1.00 12.84  ? 140  ALA A CA  1 
ATOM   1063 C  C   . ALA A 1 140 ? -10.934 7.075   16.322  1.00 13.46  ? 140  ALA A C   1 
ATOM   1064 O  O   . ALA A 1 140 ? -10.196 7.156   15.344  1.00 13.02  ? 140  ALA A O   1 
ATOM   1065 C  CB  . ALA A 1 140 ? -11.005 4.545   16.352  1.00 11.99  ? 140  ALA A CB  1 
ATOM   1066 N  N   . GLY A 1 141 ? -11.741 8.070   16.674  1.00 14.70  ? 141  GLY A N   1 
ATOM   1067 C  CA  . GLY A 1 141 ? -11.732 9.339   15.947  1.00 15.02  ? 141  GLY A CA  1 
ATOM   1068 C  C   . GLY A 1 141 ? -12.432 9.234   14.604  1.00 15.23  ? 141  GLY A C   1 
ATOM   1069 O  O   . GLY A 1 141 ? -13.305 8.373   14.395  1.00 14.97  ? 141  GLY A O   1 
ATOM   1070 N  N   . SER A 1 142 ? -12.024 10.102  13.686  1.00 15.70  ? 142  SER A N   1 
ATOM   1071 C  CA  . SER A 1 142 ? -12.685 10.208  12.391  1.00 16.10  ? 142  SER A CA  1 
ATOM   1072 C  C   . SER A 1 142 ? -12.400 8.993   11.510  1.00 14.94  ? 142  SER A C   1 
ATOM   1073 O  O   . SER A 1 142 ? -11.373 8.340   11.657  1.00 15.08  ? 142  SER A O   1 
ATOM   1074 C  CB  . SER A 1 142 ? -12.203 11.472  11.667  1.00 17.24  ? 142  SER A CB  1 
ATOM   1075 O  OG  . SER A 1 142 ? -12.585 12.645  12.365  1.00 21.22  ? 142  SER A OG  1 
ATOM   1076 N  N   . ARG A 1 143 ? -13.303 8.716   10.572  1.00 13.92  ? 143  ARG A N   1 
ATOM   1077 C  CA  . ARG A 1 143 ? -13.041 7.706   9.549   1.00 13.51  ? 143  ARG A CA  1 
ATOM   1078 C  C   . ARG A 1 143 ? -12.221 8.349   8.424   1.00 13.30  ? 143  ARG A C   1 
ATOM   1079 O  O   . ARG A 1 143 ? -12.629 9.366   7.849   1.00 15.19  ? 143  ARG A O   1 
ATOM   1080 C  CB  . ARG A 1 143 ? -14.362 7.128   9.038   1.00 13.94  ? 143  ARG A CB  1 
ATOM   1081 C  CG  . ARG A 1 143 ? -15.176 6.486   10.151  1.00 15.53  ? 143  ARG A CG  1 
ATOM   1082 C  CD  . ARG A 1 143 ? -16.532 5.968   9.676   1.00 16.94  ? 143  ARG A CD  1 
ATOM   1083 N  NE  . ARG A 1 143 ? -17.452 7.050   9.342   1.00 17.40  ? 143  ARG A NE  1 
ATOM   1084 C  CZ  . ARG A 1 143 ? -18.092 7.813   10.229  1.00 18.93  ? 143  ARG A CZ  1 
ATOM   1085 N  NH1 . ARG A 1 143 ? -17.934 7.614   11.532  1.00 19.24  ? 143  ARG A NH1 1 
ATOM   1086 N  NH2 . ARG A 1 143 ? -18.903 8.780   9.806   1.00 20.22  ? 143  ARG A NH2 1 
ATOM   1087 N  N   . LEU A 1 144 ? -11.052 7.778   8.137   1.00 12.11  ? 144  LEU A N   1 
ATOM   1088 C  CA  . LEU A 1 144 ? -10.140 8.344   7.139   1.00 12.64  ? 144  LEU A CA  1 
ATOM   1089 C  C   . LEU A 1 144 ? -10.355 7.798   5.725   1.00 12.17  ? 144  LEU A C   1 
ATOM   1090 O  O   . LEU A 1 144 ? -10.177 8.529   4.750   1.00 12.99  ? 144  LEU A O   1 
ATOM   1091 C  CB  . LEU A 1 144 ? -8.682  8.112   7.553   1.00 12.83  ? 144  LEU A CB  1 
ATOM   1092 C  CG  . LEU A 1 144 ? -8.258  8.766   8.877   1.00 14.78  ? 144  LEU A CG  1 
ATOM   1093 C  CD1 . LEU A 1 144 ? -6.770  8.552   9.099   1.00 16.67  ? 144  LEU A CD1 1 
ATOM   1094 C  CD2 . LEU A 1 144 ? -8.581  10.251  8.942   1.00 17.09  ? 144  LEU A CD2 1 
ATOM   1095 N  N   . ALA A 1 145 ? -10.694 6.518   5.624   1.00 11.33  ? 145  ALA A N   1 
ATOM   1096 C  CA  . ALA A 1 145 ? -10.928 5.875   4.331   1.00 11.29  ? 145  ALA A CA  1 
ATOM   1097 C  C   . ALA A 1 145 ? -11.816 4.666   4.541   1.00 11.28  ? 145  ALA A C   1 
ATOM   1098 O  O   . ALA A 1 145 ? -11.750 4.014   5.579   1.00 11.57  ? 145  ALA A O   1 
ATOM   1099 C  CB  . ALA A 1 145 ? -9.605  5.452   3.686   1.00 11.31  ? 145  ALA A CB  1 
ATOM   1100 N  N   . CYS A 1 146 ? -12.644 4.371   3.550   1.00 10.99  ? 146  CYS A N   1 
ATOM   1101 C  CA  . CYS A 1 146 ? -13.508 3.221   3.621   1.00 11.39  ? 146  CYS A CA  1 
ATOM   1102 C  C   . CYS A 1 146 ? -13.813 2.696   2.248   1.00 10.63  ? 146  CYS A C   1 
ATOM   1103 O  O   . CYS A 1 146 ? -13.514 3.346   1.234   1.00 11.30  ? 146  CYS A O   1 
ATOM   1104 C  CB  . CYS A 1 146 ? -14.821 3.520   4.320   1.00 12.09  ? 146  CYS A CB  1 
ATOM   1105 S  SG  A CYS A 1 146 ? -14.900 4.886   5.570   0.50 12.59  ? 146  CYS A SG  1 
ATOM   1106 S  SG  B CYS A 1 146 ? -15.734 4.832   3.554   0.50 17.95  ? 146  CYS A SG  1 
ATOM   1107 N  N   . GLY A 1 147 ? -14.413 1.513   2.226   1.00 10.61  ? 147  GLY A N   1 
ATOM   1108 C  CA  . GLY A 1 147 ? -14.832 0.906   0.988   1.00 10.04  ? 147  GLY A CA  1 
ATOM   1109 C  C   . GLY A 1 147 ? -15.629 -0.353  1.210   1.00 9.62   ? 147  GLY A C   1 
ATOM   1110 O  O   . GLY A 1 147 ? -15.491 -1.027  2.233   1.00 9.29   ? 147  GLY A O   1 
ATOM   1111 N  N   . VAL A 1 148 ? -16.484 -0.661  0.249   1.00 9.47   ? 148  VAL A N   1 
ATOM   1112 C  CA  . VAL A 1 148 ? -17.280 -1.878  0.335   1.00 9.79   ? 148  VAL A CA  1 
ATOM   1113 C  C   . VAL A 1 148 ? -16.402 -3.110  0.225   1.00 9.61   ? 148  VAL A C   1 
ATOM   1114 O  O   . VAL A 1 148 ? -15.446 -3.162  -0.570  1.00 10.08  ? 148  VAL A O   1 
ATOM   1115 C  CB  . VAL A 1 148 ? -18.337 -2.019  -0.799  1.00 10.92  ? 148  VAL A CB  1 
ATOM   1116 C  CG1 A VAL A 1 148 ? -17.868 -1.559  -2.194  0.50 9.67   ? 148  VAL A CG1 1 
ATOM   1117 C  CG1 B VAL A 1 148 ? -19.614 -2.637  -0.275  0.50 11.78  ? 148  VAL A CG1 1 
ATOM   1118 C  CG2 A VAL A 1 148 ? -19.287 -3.224  -0.631  0.50 9.36   ? 148  VAL A CG2 1 
ATOM   1119 C  CG2 B VAL A 1 148 ? -18.572 -0.724  -1.543  0.50 12.42  ? 148  VAL A CG2 1 
ATOM   1120 N  N   . ILE A 1 149 ? -16.753 -4.123  1.004   1.00 8.80   ? 149  ILE A N   1 
ATOM   1121 C  CA  . ILE A 1 149 ? -16.091 -5.410  0.915   1.00 8.89   ? 149  ILE A CA  1 
ATOM   1122 C  C   . ILE A 1 149 ? -16.795 -6.191  -0.188  1.00 9.45   ? 149  ILE A C   1 
ATOM   1123 O  O   . ILE A 1 149 ? -17.911 -6.681  -0.004  1.00 9.69   ? 149  ILE A O   1 
ATOM   1124 C  CB  . ILE A 1 149 ? -16.164 -6.127  2.267   1.00 8.50   ? 149  ILE A CB  1 
ATOM   1125 C  CG1 . ILE A 1 149 ? -15.440 -5.287  3.325   1.00 8.39   ? 149  ILE A CG1 1 
ATOM   1126 C  CG2 . ILE A 1 149 ? -15.565 -7.504  2.173   1.00 9.71   ? 149  ILE A CG2 1 
ATOM   1127 C  CD1 . ILE A 1 149 ? -15.745 -5.682  4.766   1.00 9.16   ? 149  ILE A CD1 1 
ATOM   1128 N  N   . GLY A 1 150 ? -16.173 -6.234  -1.368  1.00 9.84   ? 150  GLY A N   1 
ATOM   1129 C  CA  . GLY A 1 150 ? -16.785 -6.838  -2.547  1.00 10.72  ? 150  GLY A CA  1 
ATOM   1130 C  C   . GLY A 1 150 ? -16.236 -8.206  -2.873  1.00 11.52  ? 150  GLY A C   1 
ATOM   1131 O  O   . GLY A 1 150 ? -15.065 -8.477  -2.659  1.00 10.98  ? 150  GLY A O   1 
ATOM   1132 N  N   . ILE A 1 151 ? -17.075 -9.072  -3.429  1.00 13.11  ? 151  ILE A N   1 
ATOM   1133 C  CA  . ILE A 1 151 ? -16.596 -10.388 -3.851  1.00 14.80  ? 151  ILE A CA  1 
ATOM   1134 C  C   . ILE A 1 151 ? -15.564 -10.229 -4.957  1.00 16.04  ? 151  ILE A C   1 
ATOM   1135 O  O   . ILE A 1 151 ? -15.693 -9.362  -5.827  1.00 15.57  ? 151  ILE A O   1 
ATOM   1136 C  CB  . ILE A 1 151 ? -17.739 -11.300 -4.320  1.00 16.23  ? 151  ILE A CB  1 
ATOM   1137 C  CG1 . ILE A 1 151 ? -18.561 -11.775 -3.125  1.00 18.41  ? 151  ILE A CG1 1 
ATOM   1138 C  CG2 . ILE A 1 151 ? -17.181 -12.488 -5.101  1.00 18.07  ? 151  ILE A CG2 1 
ATOM   1139 C  CD1 . ILE A 1 151 ? -17.842 -12.756 -2.197  1.00 19.86  ? 151  ILE A CD1 1 
ATOM   1140 N  N   . ALA A 1 152 ? -14.507 -11.026 -4.917  1.00 18.16  ? 152  ALA A N   1 
ATOM   1141 C  CA  . ALA A 1 152 ? -13.429 -10.808 -5.880  1.00 20.76  ? 152  ALA A CA  1 
ATOM   1142 C  C   . ALA A 1 152 ? -13.891 -11.132 -7.307  0.70 23.59  ? 152  ALA A C   1 
ATOM   1143 O  O   . ALA A 1 152 ? -14.639 -12.092 -7.536  0.70 23.99  ? 152  ALA A O   1 
ATOM   1144 C  CB  . ALA A 1 152 ? -12.175 -11.575 -5.483  1.00 21.37  ? 152  ALA A CB  1 
ATOM   1145 N  N   . GLN A 1 153 ? -13.472 -10.288 -8.249  0.70 26.03  ? 153  GLN A N   1 
ATOM   1146 C  CA  . GLN A 1 153 ? -13.847 -10.411 -9.651  0.70 28.33  ? 153  GLN A CA  1 
ATOM   1147 C  C   . GLN A 1 153 ? -12.872 -11.288 -10.427 0.70 29.21  ? 153  GLN A C   1 
ATOM   1148 O  O   . GLN A 1 153 ? -13.017 -11.425 -11.646 0.70 30.24  ? 153  GLN A O   1 
ATOM   1149 C  CB  . GLN A 1 153 ? -13.900 -9.022  -10.303 0.70 29.20  ? 153  GLN A CB  1 
ATOM   1150 C  CG  . GLN A 1 153 ? -14.839 -8.024  -9.629  0.70 30.38  ? 153  GLN A CG  1 
ATOM   1151 C  CD  . GLN A 1 153 ? -16.302 -8.272  -9.958  0.70 32.72  ? 153  GLN A CD  1 
ATOM   1152 O  OE1 . GLN A 1 153 ? -16.724 -9.410  -10.184 0.70 35.31  ? 153  GLN A OE1 1 
ATOM   1153 N  NE2 . GLN A 1 153 ? -17.088 -7.200  -9.979  0.70 34.05  ? 153  GLN A NE2 1 
ATOM   1154 O  OXT . GLN A 1 153 ? -11.920 -11.868 -9.893  0.70 29.06  ? 153  GLN A OXT 1 
HETATM 1155 ZN ZN  . ZN  B 2 .   ? -16.903 -2.376  17.662  1.00 9.44   ? 155  ZN  A ZN  1 
HETATM 1156 ZN ZN  . ZN  C 2 .   ? -29.736 -3.471  4.034   1.00 12.50  ? 156  ZN  A ZN  1 
HETATM 1157 ZN ZN  . ZN  D 2 .   ? -27.474 2.404   5.054   1.00 17.46  ? 157  ZN  A ZN  1 
HETATM 1158 ZN ZN  . ZN  E 2 .   ? -28.731 -12.470 12.318  0.70 27.80  ? 158  ZN  A ZN  1 
HETATM 1159 C  C1  . PEG F 3 .   ? -18.288 -12.884 18.888  1.00 46.07  ? 159  PEG A C1  1 
HETATM 1160 O  O1  . PEG F 3 .   ? -19.697 -13.104 19.060  1.00 45.77  ? 159  PEG A O1  1 
HETATM 1161 C  C2  . PEG F 3 .   ? -17.478 -13.690 19.904  1.00 46.27  ? 159  PEG A C2  1 
HETATM 1162 O  O2  . PEG F 3 .   ? -16.153 -13.148 20.054  1.00 46.06  ? 159  PEG A O2  1 
HETATM 1163 C  C3  . PEG F 3 .   ? -15.126 -14.132 20.236  1.00 46.29  ? 159  PEG A C3  1 
HETATM 1164 C  C4  . PEG F 3 .   ? -13.768 -13.588 19.806  1.00 46.22  ? 159  PEG A C4  1 
HETATM 1165 O  O4  . PEG F 3 .   ? -12.714 -14.430 20.290  1.00 46.80  ? 159  PEG A O4  1 
HETATM 1166 NA NA  . NA  G 4 .   ? -22.022 3.267   17.297  1.00 51.07  ? 160  NA  A NA  1 
HETATM 1167 NA NA  . NA  H 4 .   ? -14.735 4.889   -0.590  1.00 44.46  ? 161  NA  A NA  1 
HETATM 1168 C  C   . ACT I 5 .   ? -3.487  -17.328 2.936   1.00 37.68  ? 162  ACT A C   1 
HETATM 1169 O  O   . ACT I 5 .   ? -2.565  -16.730 3.570   1.00 36.87  ? 162  ACT A O   1 
HETATM 1170 O  OXT . ACT I 5 .   ? -4.537  -16.680 2.678   1.00 37.78  ? 162  ACT A OXT 1 
HETATM 1171 C  CH3 . ACT I 5 .   ? -3.371  -18.760 2.512   1.00 37.50  ? 162  ACT A CH3 1 
HETATM 1172 O  O   . HOH J 6 .   ? -15.907 -20.457 1.180   1.00 28.68  ? 2001 HOH A O   1 
HETATM 1173 O  O   . HOH J 6 .   ? -16.722 -19.023 -2.977  1.00 35.02  ? 2002 HOH A O   1 
HETATM 1174 O  O   . HOH J 6 .   ? -14.585 -2.762  -4.719  1.00 35.33  ? 2003 HOH A O   1 
HETATM 1175 O  O   . HOH J 6 .   ? -14.603 -15.848 -4.288  1.00 24.76  ? 2004 HOH A O   1 
HETATM 1176 O  O   . HOH J 6 .   ? -14.202 -5.144  -4.550  1.00 28.90  ? 2005 HOH A O   1 
HETATM 1177 O  O   . HOH J 6 .   ? -7.839  8.005   -2.952  1.00 67.77  ? 2006 HOH A O   1 
HETATM 1178 O  O   . HOH J 6 .   ? -13.839 2.586   -2.284  1.00 33.69  ? 2007 HOH A O   1 
HETATM 1179 O  O   . HOH J 6 .   ? -12.391 9.175   -2.651  1.00 62.08  ? 2008 HOH A O   1 
HETATM 1180 O  O   . HOH J 6 .   ? -12.711 10.651  4.651   1.00 60.85  ? 2009 HOH A O   1 
HETATM 1181 O  O   . HOH J 6 .   ? -24.139 -20.552 7.515   1.00 42.12  ? 2010 HOH A O   1 
HETATM 1182 O  O   . HOH J 6 .   ? -1.672  8.569   -0.566  1.00 46.76  ? 2011 HOH A O   1 
HETATM 1183 O  O   . HOH J 6 .   ? -3.955  -22.178 4.076   1.00 34.70  ? 2012 HOH A O   1 
HETATM 1184 O  O   . HOH J 6 .   ? -4.981  -9.711  17.551  1.00 31.30  ? 2013 HOH A O   1 
HETATM 1185 O  O   . HOH J 6 .   ? -8.297  8.533   -0.232  1.00 24.71  ? 2014 HOH A O   1 
HETATM 1186 O  O   . HOH J 6 .   ? -1.462  12.953  7.475   1.00 44.77  ? 2015 HOH A O   1 
HETATM 1187 O  O   . HOH J 6 .   ? -2.206  5.635   20.134  1.00 38.53  ? 2016 HOH A O   1 
HETATM 1188 O  O   . HOH J 6 .   ? -8.344  -12.471 -1.743  1.00 14.61  ? 2017 HOH A O   1 
HETATM 1189 O  O   . HOH J 6 .   ? -4.234  -6.634  -0.658  1.00 18.86  ? 2018 HOH A O   1 
HETATM 1190 O  O   . HOH J 6 .   ? -27.060 -5.683  11.972  1.00 47.77  ? 2019 HOH A O   1 
HETATM 1191 O  O   . HOH J 6 .   ? -6.701  -18.168 -3.291  1.00 24.14  ? 2020 HOH A O   1 
HETATM 1192 O  O   . HOH J 6 .   ? -8.416  -18.612 4.712   1.00 59.39  ? 2021 HOH A O   1 
HETATM 1193 O  O   . HOH J 6 .   ? -9.756  12.577  6.274   1.00 69.96  ? 2022 HOH A O   1 
HETATM 1194 O  O   . HOH J 6 .   ? -14.733 -23.149 -0.380  1.00 42.10  ? 2023 HOH A O   1 
HETATM 1195 O  O   . HOH J 6 .   ? -23.010 0.442   19.350  1.00 45.89  ? 2024 HOH A O   1 
HETATM 1196 O  O   . HOH J 6 .   ? -20.988 -22.467 7.239   1.00 38.27  ? 2025 HOH A O   1 
HETATM 1197 O  O   . HOH J 6 .   ? -17.143 -25.006 3.020   1.00 47.06  ? 2026 HOH A O   1 
HETATM 1198 O  O   . HOH J 6 .   ? -21.137 -19.781 6.459   1.00 25.03  ? 2027 HOH A O   1 
HETATM 1199 O  O   . HOH J 6 .   ? -13.531 -24.523 10.950  1.00 50.45  ? 2028 HOH A O   1 
HETATM 1200 O  O   . HOH J 6 .   ? -18.030 -3.493  27.784  1.00 85.07  ? 2029 HOH A O   1 
HETATM 1201 O  O   . HOH J 6 .   ? -5.755  -5.813  19.316  1.00 44.26  ? 2030 HOH A O   1 
HETATM 1202 O  O   . HOH J 6 .   ? -10.482 -20.412 6.060   1.00 33.49  ? 2031 HOH A O   1 
HETATM 1203 O  O   . HOH J 6 .   ? -1.747  -20.038 4.603   1.00 64.48  ? 2032 HOH A O   1 
HETATM 1204 O  O   . HOH J 6 .   ? -6.448  -9.690  15.045  1.00 17.15  ? 2033 HOH A O   1 
HETATM 1205 O  O   . HOH J 6 .   ? -2.323  -3.734  17.394  1.00 39.86  ? 2034 HOH A O   1 
HETATM 1206 O  O   . HOH J 6 .   ? -3.627  -1.214  21.591  1.00 34.56  ? 2035 HOH A O   1 
HETATM 1207 O  O   . HOH J 6 .   ? -2.141  -3.911  -0.836  1.00 51.41  ? 2036 HOH A O   1 
HETATM 1208 O  O   . HOH J 6 .   ? -2.590  -1.255  -1.094  1.00 27.34  ? 2037 HOH A O   1 
HETATM 1209 O  O   . HOH J 6 .   ? -3.574  10.870  7.050   1.00 22.58  ? 2038 HOH A O   1 
HETATM 1210 O  O   . HOH J 6 .   ? -0.136  11.483  4.620   1.00 45.51  ? 2039 HOH A O   1 
HETATM 1211 O  O   . HOH J 6 .   ? -3.698  9.280   9.345   1.00 19.25  ? 2040 HOH A O   1 
HETATM 1212 O  O   . HOH J 6 .   ? 3.878   7.328   16.472  1.00 56.35  ? 2041 HOH A O   1 
HETATM 1213 O  O   . HOH J 6 .   ? 3.327   10.431  10.619  1.00 34.83  ? 2042 HOH A O   1 
HETATM 1214 O  O   . HOH J 6 .   ? 7.406   3.456   13.167  1.00 29.96  ? 2043 HOH A O   1 
HETATM 1215 O  O   . HOH J 6 .   ? -1.184  8.440   14.646  1.00 48.11  ? 2044 HOH A O   1 
HETATM 1216 O  O   . HOH J 6 .   ? 9.582   6.760   14.606  1.00 52.25  ? 2045 HOH A O   1 
HETATM 1217 O  O   . HOH J 6 .   ? -2.417  6.882   16.331  1.00 27.48  ? 2046 HOH A O   1 
HETATM 1218 O  O   . HOH J 6 .   ? -0.080  5.239   17.988  1.00 31.12  ? 2047 HOH A O   1 
HETATM 1219 O  O   . HOH J 6 .   ? -11.919 1.531   14.563  1.00 14.76  ? 2048 HOH A O   1 
HETATM 1220 O  O   . HOH J 6 .   ? -16.399 1.655   11.503  1.00 30.46  ? 2049 HOH A O   1 
HETATM 1221 O  O   . HOH J 6 .   ? -5.588  3.554   23.225  1.00 73.24  ? 2050 HOH A O   1 
HETATM 1222 O  O   . HOH J 6 .   ? -10.139 8.146   23.997  1.00 36.41  ? 2051 HOH A O   1 
HETATM 1223 O  O   . HOH J 6 .   ? -24.910 -4.092  12.896  1.00 19.82  ? 2052 HOH A O   1 
HETATM 1224 O  O   . HOH J 6 .   ? -25.933 2.574   11.034  1.00 63.93  ? 2053 HOH A O   1 
HETATM 1225 O  O   . HOH J 6 .   ? -24.218 0.511   -3.366  1.00 83.43  ? 2054 HOH A O   1 
HETATM 1226 O  O   . HOH J 6 .   ? -29.416 0.272   -0.525  1.00 41.10  ? 2055 HOH A O   1 
HETATM 1227 O  O   . HOH J 6 .   ? -7.286  11.608  5.844   1.00 63.84  ? 2056 HOH A O   1 
HETATM 1228 O  O   . HOH J 6 .   ? -14.615 7.856   -1.198  1.00 77.42  ? 2057 HOH A O   1 
HETATM 1229 O  O   . HOH J 6 .   ? -25.530 9.363   6.119   1.00 34.41  ? 2058 HOH A O   1 
HETATM 1230 O  O   . HOH J 6 .   ? -24.551 3.201   8.899   1.00 35.38  ? 2059 HOH A O   1 
HETATM 1231 O  O   . HOH J 6 .   ? -16.621 3.429   13.466  1.00 29.06  ? 2060 HOH A O   1 
HETATM 1232 O  O   . HOH J 6 .   ? -22.017 1.704   9.628   1.00 20.82  ? 2061 HOH A O   1 
HETATM 1233 O  O   . HOH J 6 .   ? -21.974 -1.283  16.717  1.00 42.23  ? 2062 HOH A O   1 
HETATM 1234 O  O   . HOH J 6 .   ? -22.071 -8.667  16.722  1.00 11.71  ? 2063 HOH A O   1 
HETATM 1235 O  O   . HOH J 6 .   ? -24.354 -1.656  17.796  1.00 23.64  ? 2064 HOH A O   1 
HETATM 1236 O  O   . HOH J 6 .   ? -24.741 -5.777  24.491  1.00 38.98  ? 2065 HOH A O   1 
HETATM 1237 O  O   . HOH J 6 .   ? -19.901 -2.263  29.505  1.00 77.77  ? 2066 HOH A O   1 
HETATM 1238 O  O   . HOH J 6 .   ? -16.614 -2.664  25.783  1.00 23.10  ? 2067 HOH A O   1 
HETATM 1239 O  O   . HOH J 6 .   ? -5.109  -14.237 14.874  1.00 32.21  ? 2068 HOH A O   1 
HETATM 1240 O  O   . HOH J 6 .   ? -7.755  -7.953  21.092  1.00 17.35  ? 2069 HOH A O   1 
HETATM 1241 O  O   . HOH J 6 .   ? -10.365 -13.853 16.004  1.00 28.13  ? 2070 HOH A O   1 
HETATM 1242 O  O   . HOH J 6 .   ? -14.120 -18.602 25.460  1.00 45.26  ? 2071 HOH A O   1 
HETATM 1243 O  O   . HOH J 6 .   ? -17.746 -13.471 27.689  1.00 34.91  ? 2072 HOH A O   1 
HETATM 1244 O  O   . HOH J 6 .   ? -12.201 -11.711 26.625  1.00 31.85  ? 2073 HOH A O   1 
HETATM 1245 O  O   . HOH J 6 .   ? -18.935 -11.463 21.548  1.00 36.22  ? 2074 HOH A O   1 
HETATM 1246 O  O   . HOH J 6 .   ? -15.555 -6.146  25.222  1.00 25.78  ? 2075 HOH A O   1 
HETATM 1247 O  O   . HOH J 6 .   ? -23.400 -7.550  25.823  1.00 28.65  ? 2076 HOH A O   1 
HETATM 1248 O  O   . HOH J 6 .   ? -14.515 -9.864  26.704  1.00 22.81  ? 2077 HOH A O   1 
HETATM 1249 O  O   . HOH J 6 .   ? -20.247 -10.353 17.961  1.00 15.21  ? 2078 HOH A O   1 
HETATM 1250 O  O   . HOH J 6 .   ? -21.944 -1.603  21.323  1.00 18.87  ? 2079 HOH A O   1 
HETATM 1251 O  O   . HOH J 6 .   ? -6.099  -6.835  14.418  1.00 17.60  ? 2080 HOH A O   1 
HETATM 1252 O  O   . HOH J 6 .   ? -5.297  -5.392  16.728  1.00 18.06  ? 2081 HOH A O   1 
HETATM 1253 O  O   . HOH J 6 .   ? -4.197  -2.915  19.256  1.00 22.34  ? 2082 HOH A O   1 
HETATM 1254 O  O   . HOH J 6 .   ? -4.011  -5.835  13.113  1.00 25.13  ? 2083 HOH A O   1 
HETATM 1255 O  O   . HOH J 6 .   ? -1.358  -2.928  15.055  1.00 33.37  ? 2084 HOH A O   1 
HETATM 1256 O  O   . HOH J 6 .   ? 2.556   -2.152  9.379   1.00 21.91  ? 2085 HOH A O   1 
HETATM 1257 O  O   . HOH J 6 .   ? 4.963   2.350   13.613  1.00 32.80  ? 2086 HOH A O   1 
HETATM 1258 O  O   . HOH J 6 .   ? 7.973   -0.641  6.435   1.00 20.47  ? 2087 HOH A O   1 
HETATM 1259 O  O   . HOH J 6 .   ? 2.202   6.800   2.877   1.00 21.46  ? 2088 HOH A O   1 
HETATM 1260 O  O   . HOH J 6 .   ? 5.931   5.366   0.955   1.00 44.77  ? 2089 HOH A O   1 
HETATM 1261 O  O   . HOH J 6 .   ? 4.174   -0.917  7.246   1.00 26.15  ? 2090 HOH A O   1 
HETATM 1262 O  O   . HOH J 6 .   ? -0.571  -3.443  11.134  1.00 25.83  ? 2091 HOH A O   1 
HETATM 1263 O  O   . HOH J 6 .   ? 0.267   -7.509  4.495   1.00 27.98  ? 2092 HOH A O   1 
HETATM 1264 O  O   . HOH J 6 .   ? -3.009  -13.009 7.017   1.00 39.89  ? 2093 HOH A O   1 
HETATM 1265 O  O   . HOH J 6 .   ? -2.381  -6.118  10.873  1.00 22.29  ? 2094 HOH A O   1 
HETATM 1266 O  O   . HOH J 6 .   ? -0.846  -7.844  12.151  1.00 56.81  ? 2095 HOH A O   1 
HETATM 1267 O  O   . HOH J 6 .   ? -4.737  -11.724 13.582  1.00 21.30  ? 2096 HOH A O   1 
HETATM 1268 O  O   . HOH J 6 .   ? -5.148  -20.858 9.592   1.00 50.63  ? 2097 HOH A O   1 
HETATM 1269 O  O   . HOH J 6 .   ? -3.664  -16.746 14.233  1.00 53.22  ? 2098 HOH A O   1 
HETATM 1270 O  O   . HOH J 6 .   ? -8.449  -11.409 14.663  1.00 17.48  ? 2099 HOH A O   1 
HETATM 1271 O  O   . HOH J 6 .   ? -8.331  -17.969 13.823  1.00 55.57  ? 2100 HOH A O   1 
HETATM 1272 O  O   . HOH J 6 .   ? -19.980 -13.468 11.678  1.00 18.93  ? 2101 HOH A O   1 
HETATM 1273 O  O   . HOH J 6 .   ? -14.854 -17.282 10.586  1.00 21.46  ? 2102 HOH A O   1 
HETATM 1274 O  O   . HOH J 6 .   ? -16.991 -18.307 2.790   1.00 20.44  ? 2103 HOH A O   1 
HETATM 1275 O  O   . HOH J 6 .   ? -22.525 -15.787 8.661   1.00 19.94  ? 2104 HOH A O   1 
HETATM 1276 O  O   . HOH J 6 .   ? -25.842 -12.306 4.582   1.00 35.14  ? 2105 HOH A O   1 
HETATM 1277 O  O   . HOH J 6 .   ? -30.483 -18.190 6.679   1.00 67.69  ? 2106 HOH A O   1 
HETATM 1278 O  O   . HOH J 6 .   ? -24.524 -18.270 8.802   1.00 103.17 ? 2107 HOH A O   1 
HETATM 1279 O  O   . HOH J 6 .   ? -21.988 -13.689 13.626  1.00 27.80  ? 2108 HOH A O   1 
HETATM 1280 O  O   . HOH J 6 .   ? -19.324 -12.001 9.534   1.00 12.71  ? 2109 HOH A O   1 
HETATM 1281 O  O   . HOH J 6 .   ? -24.404 -9.238  5.947   1.00 30.14  ? 2110 HOH A O   1 
HETATM 1282 O  O   . HOH J 6 .   ? -23.839 -10.123 2.737   1.00 29.70  ? 2111 HOH A O   1 
HETATM 1283 O  O   . HOH J 6 .   ? -26.724 -8.851  9.835   1.00 67.13  ? 2112 HOH A O   1 
HETATM 1284 O  O   . HOH J 6 .   ? -13.758 5.709   13.764  1.00 26.73  ? 2113 HOH A O   1 
HETATM 1285 O  O   . HOH J 6 .   ? -12.176 1.889   11.946  1.00 15.10  ? 2114 HOH A O   1 
HETATM 1286 O  O   . HOH J 6 .   ? -4.526  10.236  11.768  1.00 22.41  ? 2115 HOH A O   1 
HETATM 1287 O  O   . HOH J 6 .   ? -8.437  14.773  17.231  1.00 36.86  ? 2116 HOH A O   1 
HETATM 1288 O  O   . HOH J 6 .   ? -6.726  11.968  21.103  1.00 41.11  ? 2117 HOH A O   1 
HETATM 1289 O  O   . HOH J 6 .   ? -11.620 10.926  19.312  1.00 27.03  ? 2118 HOH A O   1 
HETATM 1290 O  O   . HOH J 6 .   ? -7.605  5.789   21.258  1.00 38.39  ? 2119 HOH A O   1 
HETATM 1291 O  O   . HOH J 6 .   ? -4.228  6.997   18.933  1.00 26.65  ? 2120 HOH A O   1 
HETATM 1292 O  O   . HOH J 6 .   ? -11.730 -1.224  15.146  1.00 18.79  ? 2121 HOH A O   1 
HETATM 1293 O  O   . HOH J 6 .   ? -5.415  0.876   22.022  1.00 30.01  ? 2122 HOH A O   1 
HETATM 1294 O  O   . HOH J 6 .   ? -11.419 -3.808  17.834  1.00 12.10  ? 2123 HOH A O   1 
HETATM 1295 O  O   . HOH J 6 .   ? -9.921  5.821   25.248  1.00 30.54  ? 2124 HOH A O   1 
HETATM 1296 O  O   . HOH J 6 .   ? -6.852  -0.034  25.114  1.00 38.33  ? 2125 HOH A O   1 
HETATM 1297 O  O   . HOH J 6 .   ? -8.027  -6.825  23.612  1.00 48.02  ? 2126 HOH A O   1 
HETATM 1298 O  O   . HOH J 6 .   ? -14.347 0.263   29.010  1.00 36.26  ? 2127 HOH A O   1 
HETATM 1299 O  O   . HOH J 6 .   ? -13.721 8.864   29.310  1.00 23.77  ? 2128 HOH A O   1 
HETATM 1300 O  O   . HOH J 6 .   ? -12.162 7.231   27.397  1.00 54.05  ? 2129 HOH A O   1 
HETATM 1301 O  O   . HOH J 6 .   ? -21.630 5.750   18.624  1.00 42.58  ? 2130 HOH A O   1 
HETATM 1302 O  O   . HOH J 6 .   ? -20.458 0.791   16.879  1.00 17.87  ? 2131 HOH A O   1 
HETATM 1303 O  O   . HOH J 6 .   ? -14.172 2.834   15.484  1.00 14.74  ? 2132 HOH A O   1 
HETATM 1304 O  O   . HOH J 6 .   ? -15.333 9.605   23.630  1.00 22.44  ? 2133 HOH A O   1 
HETATM 1305 O  O   . HOH J 6 .   ? -14.497 5.617   16.464  1.00 33.83  ? 2134 HOH A O   1 
HETATM 1306 O  O   . HOH J 6 .   ? -13.653 8.810   18.678  1.00 29.08  ? 2135 HOH A O   1 
HETATM 1307 O  O   . HOH J 6 .   ? -15.692 10.372  10.319  1.00 22.96  ? 2136 HOH A O   1 
HETATM 1308 O  O   . HOH J 6 .   ? -16.388 5.991   13.243  1.00 34.74  ? 2137 HOH A O   1 
HETATM 1309 O  O   . HOH J 6 .   ? -8.116  10.002  3.553   1.00 30.12  ? 2138 HOH A O   1 
HETATM 1310 O  O   . HOH J 6 .   ? -14.262 -1.593  -2.387  1.00 12.13  ? 2139 HOH A O   1 
HETATM 1311 O  O   . HOH J 6 .   ? -16.325 1.383   -1.994  1.00 65.29  ? 2140 HOH A O   1 
HETATM 1312 O  O   . HOH J 6 .   ? -13.571 -13.859 -5.813  1.00 42.30  ? 2141 HOH A O   1 
HETATM 1313 O  O   . HOH J 6 .   ? -11.396 -14.120 -7.875  1.00 44.21  ? 2142 HOH A O   1 
HETATM 1314 O  O   . HOH J 6 .   ? -29.413 -1.602  4.852   1.00 12.48  ? 2143 HOH A O   1 
HETATM 1315 O  O   . HOH J 6 .   ? -29.127 -11.874 14.359  1.00 43.92  ? 2144 HOH A O   1 
HETATM 1316 O  O   . HOH J 6 .   ? -11.171 -14.017 18.320  1.00 48.73  ? 2145 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  SER 46  46  46  SER SER A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  SER 48  48  48  SER SER 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 ALA 111 111 111 ALA ALA A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 ILE 113 113 113 ILE ILE A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 SER 120 120 120 SER SER A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
# 
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   155  155  ZN  ZN  A . 
C 2 ZN  1   156  156  ZN  ZN  A . 
D 2 ZN  1   157  157  ZN  ZN  A . 
E 2 ZN  1   158  158  ZN  ZN  A . 
F 3 PEG 1   159  159  PEG PEG A . 
G 4 NA  1   160  160  NA  NA  A . 
H 4 NA  1   161  161  NA  NA  A . 
I 5 ACT 1   162  162  ACT ACT A . 
J 6 HOH 1   2001 2001 HOH HOH A . 
J 6 HOH 2   2002 2002 HOH HOH A . 
J 6 HOH 3   2003 2003 HOH HOH A . 
J 6 HOH 4   2004 2004 HOH HOH A . 
J 6 HOH 5   2005 2005 HOH HOH A . 
J 6 HOH 6   2006 2006 HOH HOH A . 
J 6 HOH 7   2007 2007 HOH HOH A . 
J 6 HOH 8   2008 2008 HOH HOH A . 
J 6 HOH 9   2009 2009 HOH HOH A . 
J 6 HOH 10  2010 2010 HOH HOH A . 
J 6 HOH 11  2011 2011 HOH HOH A . 
J 6 HOH 12  2012 2012 HOH HOH A . 
J 6 HOH 13  2013 2013 HOH HOH A . 
J 6 HOH 14  2014 2014 HOH HOH A . 
J 6 HOH 15  2015 2015 HOH HOH A . 
J 6 HOH 16  2016 2016 HOH HOH A . 
J 6 HOH 17  2017 2017 HOH HOH A . 
J 6 HOH 18  2018 2018 HOH HOH A . 
J 6 HOH 19  2019 2019 HOH HOH A . 
J 6 HOH 20  2020 2020 HOH HOH A . 
J 6 HOH 21  2021 2021 HOH HOH A . 
J 6 HOH 22  2022 2022 HOH HOH A . 
J 6 HOH 23  2023 2023 HOH HOH A . 
J 6 HOH 24  2024 2024 HOH HOH A . 
J 6 HOH 25  2025 2025 HOH HOH A . 
J 6 HOH 26  2026 2026 HOH HOH A . 
J 6 HOH 27  2027 2027 HOH HOH A . 
J 6 HOH 28  2028 2028 HOH HOH A . 
J 6 HOH 29  2029 2029 HOH HOH A . 
J 6 HOH 30  2030 2030 HOH HOH A . 
J 6 HOH 31  2031 2031 HOH HOH A . 
J 6 HOH 32  2032 2032 HOH HOH A . 
J 6 HOH 33  2033 2033 HOH HOH A . 
J 6 HOH 34  2034 2034 HOH HOH A . 
J 6 HOH 35  2035 2035 HOH HOH A . 
J 6 HOH 36  2036 2036 HOH HOH A . 
J 6 HOH 37  2037 2037 HOH HOH A . 
J 6 HOH 38  2038 2038 HOH HOH A . 
J 6 HOH 39  2039 2039 HOH HOH A . 
J 6 HOH 40  2040 2040 HOH HOH A . 
J 6 HOH 41  2041 2041 HOH HOH A . 
J 6 HOH 42  2042 2042 HOH HOH A . 
J 6 HOH 43  2043 2043 HOH HOH A . 
J 6 HOH 44  2044 2044 HOH HOH A . 
J 6 HOH 45  2045 2045 HOH HOH A . 
J 6 HOH 46  2046 2046 HOH HOH A . 
J 6 HOH 47  2047 2047 HOH HOH A . 
J 6 HOH 48  2048 2048 HOH HOH A . 
J 6 HOH 49  2049 2049 HOH HOH A . 
J 6 HOH 50  2050 2050 HOH HOH A . 
J 6 HOH 51  2051 2051 HOH HOH A . 
J 6 HOH 52  2052 2052 HOH HOH A . 
J 6 HOH 53  2053 2053 HOH HOH A . 
J 6 HOH 54  2054 2054 HOH HOH A . 
J 6 HOH 55  2055 2055 HOH HOH A . 
J 6 HOH 56  2056 2056 HOH HOH A . 
J 6 HOH 57  2057 2057 HOH HOH A . 
J 6 HOH 58  2058 2058 HOH HOH A . 
J 6 HOH 59  2059 2059 HOH HOH A . 
J 6 HOH 60  2060 2060 HOH HOH A . 
J 6 HOH 61  2061 2061 HOH HOH A . 
J 6 HOH 62  2062 2062 HOH HOH A . 
J 6 HOH 63  2063 2063 HOH HOH A . 
J 6 HOH 64  2064 2064 HOH HOH A . 
J 6 HOH 65  2065 2065 HOH HOH A . 
J 6 HOH 66  2066 2066 HOH HOH A . 
J 6 HOH 67  2067 2067 HOH HOH A . 
J 6 HOH 68  2068 2068 HOH HOH A . 
J 6 HOH 69  2069 2069 HOH HOH A . 
J 6 HOH 70  2070 2070 HOH HOH A . 
J 6 HOH 71  2071 2071 HOH HOH A . 
J 6 HOH 72  2072 2072 HOH HOH A . 
J 6 HOH 73  2073 2073 HOH HOH A . 
J 6 HOH 74  2074 2074 HOH HOH A . 
J 6 HOH 75  2075 2075 HOH HOH A . 
J 6 HOH 76  2076 2076 HOH HOH A . 
J 6 HOH 77  2077 2077 HOH HOH A . 
J 6 HOH 78  2078 2078 HOH HOH A . 
J 6 HOH 79  2079 2079 HOH HOH A . 
J 6 HOH 80  2080 2080 HOH HOH A . 
J 6 HOH 81  2081 2081 HOH HOH A . 
J 6 HOH 82  2082 2082 HOH HOH A . 
J 6 HOH 83  2083 2083 HOH HOH A . 
J 6 HOH 84  2084 2084 HOH HOH A . 
J 6 HOH 85  2085 2085 HOH HOH A . 
J 6 HOH 86  2086 2086 HOH HOH A . 
J 6 HOH 87  2087 2087 HOH HOH A . 
J 6 HOH 88  2088 2088 HOH HOH A . 
J 6 HOH 89  2089 2089 HOH HOH A . 
J 6 HOH 90  2090 2090 HOH HOH A . 
J 6 HOH 91  2091 2091 HOH HOH A . 
J 6 HOH 92  2092 2092 HOH HOH A . 
J 6 HOH 93  2093 2093 HOH HOH A . 
J 6 HOH 94  2094 2094 HOH HOH A . 
J 6 HOH 95  2095 2095 HOH HOH A . 
J 6 HOH 96  2096 2096 HOH HOH A . 
J 6 HOH 97  2097 2097 HOH HOH A . 
J 6 HOH 98  2098 2098 HOH HOH A . 
J 6 HOH 99  2099 2099 HOH HOH A . 
J 6 HOH 100 2100 2100 HOH HOH A . 
J 6 HOH 101 2101 2101 HOH HOH A . 
J 6 HOH 102 2102 2102 HOH HOH A . 
J 6 HOH 103 2103 2103 HOH HOH A . 
J 6 HOH 104 2104 2104 HOH HOH A . 
J 6 HOH 105 2105 2105 HOH HOH A . 
J 6 HOH 106 2106 2106 HOH HOH A . 
J 6 HOH 107 2107 2107 HOH HOH A . 
J 6 HOH 108 2108 2108 HOH HOH A . 
J 6 HOH 109 2109 2109 HOH HOH A . 
J 6 HOH 110 2110 2110 HOH HOH A . 
J 6 HOH 111 2111 2111 HOH HOH A . 
J 6 HOH 112 2112 2112 HOH HOH A . 
J 6 HOH 113 2113 2113 HOH HOH A . 
J 6 HOH 114 2114 2114 HOH HOH A . 
J 6 HOH 115 2115 2115 HOH HOH A . 
J 6 HOH 116 2116 2116 HOH HOH A . 
J 6 HOH 117 2117 2117 HOH HOH A . 
J 6 HOH 118 2118 2118 HOH HOH A . 
J 6 HOH 119 2119 2119 HOH HOH A . 
J 6 HOH 120 2120 2120 HOH HOH A . 
J 6 HOH 121 2121 2121 HOH HOH A . 
J 6 HOH 122 2122 2122 HOH HOH A . 
J 6 HOH 123 2123 2123 HOH HOH A . 
J 6 HOH 124 2124 2124 HOH HOH A . 
J 6 HOH 125 2125 2125 HOH HOH A . 
J 6 HOH 126 2126 2126 HOH HOH A . 
J 6 HOH 127 2127 2127 HOH HOH A . 
J 6 HOH 128 2128 2128 HOH HOH A . 
J 6 HOH 129 2129 2129 HOH HOH A . 
J 6 HOH 130 2130 2130 HOH HOH A . 
J 6 HOH 131 2131 2131 HOH HOH A . 
J 6 HOH 132 2132 2132 HOH HOH A . 
J 6 HOH 133 2133 2133 HOH HOH A . 
J 6 HOH 134 2134 2134 HOH HOH A . 
J 6 HOH 135 2135 2135 HOH HOH A . 
J 6 HOH 136 2136 2136 HOH HOH A . 
J 6 HOH 137 2137 2137 HOH HOH A . 
J 6 HOH 138 2138 2138 HOH HOH A . 
J 6 HOH 139 2139 2139 HOH HOH A . 
J 6 HOH 140 2140 2140 HOH HOH A . 
J 6 HOH 141 2141 2141 HOH HOH A . 
J 6 HOH 142 2142 2142 HOH HOH A . 
J 6 HOH 143 2143 2143 HOH HOH A . 
J 6 HOH 144 2144 2144 HOH HOH A . 
J 6 HOH 145 2145 2145 HOH HOH A . 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_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 
# 
_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  ND1 ? A HIS 63  ? A HIS 63   ? 1_555 ZN ? B ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 80  ? A HIS 80   ? 1_555 113.2 ? 
2  ND1 ? A HIS 63  ? A HIS 63   ? 1_555 ZN ? B ZN . ? A ZN 155 ? 1_555 OD1 ? A ASP 83  ? A ASP 83   ? 1_555 102.4 ? 
3  ND1 ? A HIS 80  ? A HIS 80   ? 1_555 ZN ? B ZN . ? A ZN 155 ? 1_555 OD1 ? A ASP 83  ? A ASP 83   ? 1_555 114.4 ? 
4  ND1 ? A HIS 63  ? A HIS 63   ? 1_555 ZN ? B ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 71  ? A HIS 71   ? 1_555 104.5 ? 
5  ND1 ? A HIS 80  ? A HIS 80   ? 1_555 ZN ? B ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 71  ? A HIS 71   ? 1_555 122.1 ? 
6  OD1 ? A ASP 83  ? A ASP 83   ? 1_555 ZN ? B ZN . ? A ZN 155 ? 1_555 ND1 ? A HIS 71  ? A HIS 71   ? 1_555 97.5  ? 
7  O   ? A ALA 1   ? A ALA 1    ? 4_445 ZN ? C ZN . ? A ZN 156 ? 1_555 OE2 ? A GLU 51  ? A GLU 51   ? 1_555 91.1  ? 
8  O   ? A ALA 1   ? A ALA 1    ? 4_445 ZN ? C ZN . ? A ZN 156 ? 1_555 OD2 ? A ASP 96  ? A ASP 96   ? 1_455 86.1  ? 
9  OE2 ? A GLU 51  ? A GLU 51   ? 1_555 ZN ? C ZN . ? A ZN 156 ? 1_555 OD2 ? A ASP 96  ? A ASP 96   ? 1_455 96.5  ? 
10 O   ? A ALA 1   ? A ALA 1    ? 4_445 ZN ? C ZN . ? A ZN 156 ? 1_555 O   ? J HOH .   ? A HOH 2143 ? 1_555 162.7 ? 
11 OE2 ? A GLU 51  ? A GLU 51   ? 1_555 ZN ? C ZN . ? A ZN 156 ? 1_555 O   ? J HOH .   ? A HOH 2143 ? 1_555 106.2 ? 
12 OD2 ? A ASP 96  ? A ASP 96   ? 1_455 ZN ? C ZN . ? A ZN 156 ? 1_555 O   ? J HOH .   ? A HOH 2143 ? 1_555 92.8  ? 
13 OD2 ? A ASP 90  ? A ASP 90   ? 1_455 ZN ? D ZN . ? A ZN 157 ? 1_555 OD2 B A ASP 52  ? A ASP 52   ? 1_555 103.2 ? 
14 OD2 ? A ASP 90  ? A ASP 90   ? 1_455 ZN ? D ZN . ? A ZN 157 ? 1_555 OD2 A A ASP 52  ? A ASP 52   ? 1_555 102.8 ? 
15 OD2 B A ASP 52  ? A ASP 52   ? 1_555 ZN ? D ZN . ? A ZN 157 ? 1_555 OD2 A A ASP 52  ? A ASP 52   ? 1_555 3.3   ? 
16 OD2 ? A ASP 90  ? A ASP 90   ? 1_455 ZN ? D ZN . ? A ZN 157 ? 1_555 OD1 ? A ASP 92  ? A ASP 92   ? 1_455 106.7 ? 
17 OD2 B A ASP 52  ? A ASP 52   ? 1_555 ZN ? D ZN . ? A ZN 157 ? 1_555 OD1 ? A ASP 92  ? A ASP 92   ? 1_455 118.0 ? 
18 OD2 A A ASP 52  ? A ASP 52   ? 1_555 ZN ? D ZN . ? A ZN 157 ? 1_555 OD1 ? A ASP 92  ? A ASP 92   ? 1_455 121.0 ? 
19 OD2 ? A ASP 90  ? A ASP 90   ? 1_455 ZN ? D ZN . ? A ZN 157 ? 1_555 OE2 ? A GLU 50  ? A GLU 50   ? 1_555 110.6 ? 
20 OD2 B A ASP 52  ? A ASP 52   ? 1_555 ZN ? D ZN . ? A ZN 157 ? 1_555 OE2 ? A GLU 50  ? A GLU 50   ? 1_555 99.7  ? 
21 OD2 A A ASP 52  ? A ASP 52   ? 1_555 ZN ? D ZN . ? A ZN 157 ? 1_555 OE2 ? A GLU 50  ? A GLU 50   ? 1_555 96.9  ? 
22 OD1 ? A ASP 92  ? A ASP 92   ? 1_455 ZN ? D ZN . ? A ZN 157 ? 1_555 OE2 ? A GLU 50  ? A GLU 50   ? 1_555 117.8 ? 
23 O   ? A GLN 153 ? A GLN 153  ? 4_445 ZN ? E ZN . ? A ZN 158 ? 1_555 OXT ? A GLN 153 ? A GLN 153  ? 4_445 55.1  ? 
24 O   ? A GLN 153 ? A GLN 153  ? 4_445 ZN ? E ZN . ? A ZN 158 ? 1_555 O   ? J HOH .   ? A HOH 2144 ? 1_555 105.8 ? 
25 OXT ? A GLN 153 ? A GLN 153  ? 4_445 ZN ? E ZN . ? A ZN 158 ? 1_555 O   ? J HOH .   ? A HOH 2144 ? 1_555 154.4 ? 
26 O   ? A GLN 153 ? A GLN 153  ? 4_445 ZN ? E ZN . ? A ZN 158 ? 1_555 NE2 ? A HIS 110 ? A HIS 110  ? 1_555 137.4 ? 
27 OXT ? A GLN 153 ? A GLN 153  ? 4_445 ZN ? E ZN . ? A ZN 158 ? 1_555 NE2 ? A HIS 110 ? A HIS 110  ? 1_555 93.2  ? 
28 O   ? J HOH .   ? A HOH 2144 ? 1_555 ZN ? E ZN . ? A ZN 158 ? 1_555 NE2 ? A HIS 110 ? A HIS 110  ? 1_555 111.4 ? 
29 O   ? J HOH .   ? A HOH 2131 ? 1_555 NA ? G NA . ? A NA 160 ? 1_555 O   ? J HOH .   ? A HOH 2130 ? 1_555 136.4 ? 
30 O   ? J HOH .   ? A HOH 2057 ? 1_555 NA ? H NA . ? A NA 161 ? 1_555 O   ? J HOH .   ? A HOH 2007 ? 1_555 128.8 ? 
31 O   ? J HOH .   ? A HOH 2057 ? 1_555 NA ? H NA . ? A NA 161 ? 1_555 O   ? A CYS 146 ? A CYS 146  ? 1_555 132.9 ? 
32 O   ? J HOH .   ? A HOH 2007 ? 1_555 NA ? H NA . ? A NA 161 ? 1_555 O   ? A CYS 146 ? A CYS 146  ? 1_555 78.8  ? 
33 O   ? J HOH .   ? A HOH 2057 ? 1_555 NA ? H NA . ? A NA 161 ? 1_555 O   A A ALA 55  ? A ALA 55   ? 1_555 85.3  ? 
34 O   ? J HOH .   ? A HOH 2007 ? 1_555 NA ? H NA . ? A NA 161 ? 1_555 O   A A ALA 55  ? A ALA 55   ? 1_555 131.1 ? 
35 O   ? A CYS 146 ? A CYS 146  ? 1_555 NA ? H NA . ? A NA 161 ? 1_555 O   A A ALA 55  ? A ALA 55   ? 1_555 103.9 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2010-09-01 
2 'Structure model' 1 1 2011-05-08 
3 'Structure model' 1 2 2011-07-13 
4 'Structure model' 1 3 2018-01-17 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Version format compliance' 
2 3 'Structure model' 'Version format compliance' 
3 4 'Structure model' 'Data collection'           
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    4 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            diffrn_source 
# 
_pdbx_audit_revision_item.ordinal             1 
_pdbx_audit_revision_item.revision_ordinal    4 
_pdbx_audit_revision_item.data_content_type   'Structure model' 
_pdbx_audit_revision_item.item                '_diffrn_source.pdbx_synchrotron_site' 
# 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         -12.4916 
_pdbx_refine_tls.origin_y         -3.4731 
_pdbx_refine_tls.origin_z         10.1206 
_pdbx_refine_tls.T[1][1]          0.0058 
_pdbx_refine_tls.T[2][2]          0.0051 
_pdbx_refine_tls.T[3][3]          0.0056 
_pdbx_refine_tls.T[1][2]          0.0018 
_pdbx_refine_tls.T[1][3]          0.0026 
_pdbx_refine_tls.T[2][3]          -0.0007 
_pdbx_refine_tls.L[1][1]          0.9008 
_pdbx_refine_tls.L[2][2]          0.7031 
_pdbx_refine_tls.L[3][3]          1.2400 
_pdbx_refine_tls.L[1][2]          -0.1415 
_pdbx_refine_tls.L[1][3]          -0.2992 
_pdbx_refine_tls.L[2][3]          0.2801 
_pdbx_refine_tls.S[1][1]          0.0109 
_pdbx_refine_tls.S[1][2]          -0.0480 
_pdbx_refine_tls.S[1][3]          0.0498 
_pdbx_refine_tls.S[2][1]          0.0333 
_pdbx_refine_tls.S[2][2]          0.0093 
_pdbx_refine_tls.S[2][3]          -0.0114 
_pdbx_refine_tls.S[3][1]          0.0119 
_pdbx_refine_tls.S[3][2]          0.0477 
_pdbx_refine_tls.S[3][3]          -0.0202 
# 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.refine_tls_id       1 
_pdbx_refine_tls_group.beg_auth_asym_id    A 
_pdbx_refine_tls_group.beg_auth_seq_id     1 
_pdbx_refine_tls_group.beg_label_asym_id   ? 
_pdbx_refine_tls_group.beg_label_seq_id    ? 
_pdbx_refine_tls_group.end_auth_asym_id    A 
_pdbx_refine_tls_group.end_auth_seq_id     153 
_pdbx_refine_tls_group.end_label_asym_id   ? 
_pdbx_refine_tls_group.end_label_seq_id    ? 
_pdbx_refine_tls_group.selection           ? 
_pdbx_refine_tls_group.selection_details   ? 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC refinement       5.5.0109 ? 1 
XDS    'data reduction' .        ? 2 
XDS    'data scaling'   .        ? 3 
PHASER phasing          .        ? 4 
# 
_pdbx_database_remark.id     700 
_pdbx_database_remark.text   
;
SHEET
DETERMINATION METHOD: DSSP
THE SHEETS PRESENTED AS "AA" IN EACH CHAIN ON SHEET RECORDS
BELOW IS ACTUALLY AN  8-STRANDED BARREL THIS IS REPRESENTED BY
A  9-STRANDED SHEET IN WHICH THE FIRST AND LAST STRANDS
ARE IDENTICAL.
;
# 
_pdbx_entry_details.entry_id             2XJL 
_pdbx_entry_details.compound_details     
;ENGINEERED RESIDUE IN CHAIN A, CYS   7 TO ALA
ENGINEERED RESIDUE IN CHAIN A, HIS  47 TO SER
ENGINEERED RESIDUE IN CHAIN A, HIS  49 TO SER
ENGINEERED RESIDUE IN CHAIN A, PHE  51 TO GLU
ENGINEERED RESIDUE IN CHAIN A, GLY  52 TO GLU
ENGINEERED RESIDUE IN CHAIN A, CYS 112 TO ALA
ENGINEERED RESIDUE IN CHAIN A, HIS 121 TO SER
;
_pdbx_entry_details.source_details       ? 
_pdbx_entry_details.nonpolymer_details   ? 
_pdbx_entry_details.sequence_details     ? 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG1 
_pdbx_validate_rmsd_angle.auth_asym_id_1             A 
_pdbx_validate_rmsd_angle.auth_comp_id_1             VAL 
_pdbx_validate_rmsd_angle.auth_seq_id_1              148 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             A 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_2             A 
_pdbx_validate_rmsd_angle.auth_comp_id_2             VAL 
_pdbx_validate_rmsd_angle.auth_seq_id_2              148 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CG2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             A 
_pdbx_validate_rmsd_angle.auth_comp_id_3             VAL 
_pdbx_validate_rmsd_angle.auth_seq_id_3              148 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             A 
_pdbx_validate_rmsd_angle.angle_value                121.23 
_pdbx_validate_rmsd_angle.angle_target_value         110.90 
_pdbx_validate_rmsd_angle.angle_deviation            10.33 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.60 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP A 52 ? A -106.65 -77.57 
2 1 ALA A 55 ? A -73.89  -74.48 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'ZINC ION'              ZN  
3 'DI(HYDROXYETHYL)ETHER' PEG 
4 'SODIUM ION'            NA  
5 'ACETATE ION'           ACT 
6 water                   HOH 
# 
