data_4A7G
# 
_entry.id   4A7G 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.315 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4A7G         
PDBE  EBI-50307    
WWPDB D_1290050307 
# 
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 1OZU unspecified 
'CRYSTAL STRUCTURE OF FAMILIAL ALS MUTANT S134N OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) TO 1.3A RESOLUTION' 
PDB 2VR6 unspecified 'CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.3 A RESOLUTION' 
PDB 2C9V unspecified 'ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 2WZ5 unspecified 'L38V SOD1 MUTANT COMPLEXED WITH L-METHIONINE.' 
PDB 2XJL unspecified 'MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE WITHOUT CU LIGANDS' 
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 2XJK unspecified 'MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE' 
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 1L3N unspecified 'THE SOLUTION STRUCTURE OF REDUCED DIMERIC COPPER ZINC SOD:THE STRUCTURAL EFFECTS OF DIMERIZATION' 
PDB 2WKO unspecified 'STRUCTURE OF METAL LOADED PATHOGENIC SOD1 MUTANT G93A.' 
PDB 2AF2 unspecified 'SOLUTION STRUCTURE OF DISULFIDE REDUCED AND COPPER DEPLETEDHUMAN SUPEROXIDE DISMUTASE' 
PDB 1UXL unspecified 'I113T MUTANT OF HUMAN SOD1' 
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 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 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 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' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4A7G 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2011-11-14 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  REL 
_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 
'Wright, G.S.A.' 1 
'Kershaw, N.M.'  2 
'Sharma, R.'     3 
'Antonyuk, S.V.' 4 
'Strange, R.W.'  5 
'Berry, N.G.'    6 
;O'Neil, P.M.
;
7 
'Hasnain, S.S.'  8 
# 
_citation.id                        primary 
_citation.title                     
'X-ray crystallography and computational docking for the detection and development of protein-ligand interactions.' 
_citation.journal_abbrev            Curr.Med.Chem. 
_citation.journal_volume            20 
_citation.page_first                569 
_citation.page_last                 575 
_citation.year                      2013 
_citation.journal_id_ASTM           ? 
_citation.country                   NE 
_citation.journal_id_ISSN           0929-8673 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   23278398 
_citation.pdbx_database_id_DOI      10.2174/0929867311320040008 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Kershaw, N.M.'  1 ? 
primary 'Wright, G.S.'   2 ? 
primary 'Sharma, R.'     3 ? 
primary 'Antonyuk, S.V.' 4 ? 
primary 'Strange, R.W.'  5 ? 
primary 'Berry, N.G.'    6 ? 
primary 
;O'Neill, P.M.
;
7 ? 
primary 'Hasnain, S.S.'  8 ? 
# 
_cell.entry_id           4A7G 
_cell.length_a           38.793 
_cell.length_b           68.352 
_cell.length_c           49.920 
_cell.angle_alpha        90.00 
_cell.angle_beta         104.49 
_cell.angle_gamma        90.00 
_cell.Z_PDB              2 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         4A7G 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
# 
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]'          15803.453 1   1.15.1.1 YES ? ? 
2 polymer     man 'SUPEROXIDE DISMUTASE [CU-ZN]'          15815.508 1   1.15.1.1 YES ? ? 
3 non-polymer syn 'SULFATE ION'                           96.063    5   ?        ?   ? ? 
4 non-polymer syn '4-(4-METHYLPIPERAZIN-1-YL)QUINAZOLINE' 228.293   3   ?        ?   ? ? 
5 non-polymer syn 'COPPER (II) ION'                       63.546    2   ?        ?   ? ? 
6 non-polymer syn 'ZINC ION'                              65.409    2   ?        ?   ? ? 
7 non-polymer syn 'ACETATE ION'                           59.044    1   ?        ?   ? ? 
8 water       nat water                                   18.015    388 ?        ?   ? ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 'SUPEROXIDE DISMUTASE-1, SUPEROXIDE DISMUTASE 1, HSOD1' 
2 'SUPEROXIDE DISMUTASE-1, SUPEROXIDE DISMUTASE 1, HSOD1' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSTEDSVISLSGDHCITGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSTEDSVISLSGDHCITGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
A ? 
2 'polypeptide(L)' no no 
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCITGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCITGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
F ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   THR n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   CYS n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  GLY n 
1 11  ASP n 
1 12  GLY n 
1 13  PRO n 
1 14  VAL n 
1 15  GLN n 
1 16  GLY n 
1 17  ILE n 
1 18  ILE n 
1 19  ASN n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  ASN n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  LYS n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  SER n 
1 35  ILE n 
1 36  LYS n 
1 37  GLY n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU n 
1 43  HIS n 
1 44  GLY n 
1 45  PHE n 
1 46  HIS n 
1 47  VAL n 
1 48  HIS n 
1 49  GLU n 
1 50  PHE n 
1 51  GLY n 
1 52  ASP n 
1 53  ASN n 
1 54  THR n 
1 55  ALA n 
1 56  GLY n 
1 57  CYS n 
1 58  THR n 
1 59  SER n 
1 60  ALA n 
1 61  GLY n 
1 62  PRO n 
1 63  HIS n 
1 64  PHE n 
1 65  ASN n 
1 66  PRO n 
1 67  LEU n 
1 68  SER n 
1 69  ARG n 
1 70  LYS n 
1 71  HIS n 
1 72  GLY n 
1 73  GLY n 
1 74  PRO n 
1 75  LYS n 
1 76  ASP n 
1 77  GLU n 
1 78  GLU n 
1 79  ARG n 
1 80  HIS n 
1 81  VAL n 
1 82  GLY n 
1 83  ASP n 
1 84  LEU n 
1 85  GLY n 
1 86  ASN n 
1 87  VAL n 
1 88  THR n 
1 89  ALA n 
1 90  ASP n 
1 91  LYS n 
1 92  ASP n 
1 93  GLY n 
1 94  VAL n 
1 95  ALA n 
1 96  ASP n 
1 97  VAL n 
1 98  SER n 
1 99  THR n 
1 100 GLU n 
1 101 ASP n 
1 102 SER n 
1 103 VAL n 
1 104 ILE n 
1 105 SER n 
1 106 LEU n 
1 107 SER n 
1 108 GLY n 
1 109 ASP n 
1 110 HIS n 
1 111 CYS n 
1 112 ILE n 
1 113 THR n 
1 114 GLY n 
1 115 ARG n 
1 116 THR n 
1 117 LEU n 
1 118 VAL n 
1 119 VAL n 
1 120 HIS n 
1 121 GLU n 
1 122 LYS n 
1 123 ALA n 
1 124 ASP n 
1 125 ASP n 
1 126 LEU n 
1 127 GLY n 
1 128 LYS n 
1 129 GLY n 
1 130 GLY n 
1 131 ASN n 
1 132 GLU n 
1 133 GLU n 
1 134 SER n 
1 135 THR n 
1 136 LYS n 
1 137 THR n 
1 138 GLY n 
1 139 ASN n 
1 140 ALA n 
1 141 GLY n 
1 142 SER n 
1 143 ARG n 
1 144 LEU n 
1 145 ALA n 
1 146 CYS n 
1 147 GLY n 
1 148 VAL n 
1 149 ILE n 
1 150 GLY n 
1 151 ILE n 
1 152 ALA n 
1 153 GLN n 
2 1   ALA n 
2 2   THR n 
2 3   LYS n 
2 4   ALA n 
2 5   VAL n 
2 6   CYS n 
2 7   VAL n 
2 8   LEU n 
2 9   LYS n 
2 10  GLY n 
2 11  ASP n 
2 12  GLY n 
2 13  PRO n 
2 14  VAL n 
2 15  GLN n 
2 16  GLY n 
2 17  ILE n 
2 18  ILE n 
2 19  ASN n 
2 20  PHE n 
2 21  GLU n 
2 22  GLN n 
2 23  LYS n 
2 24  GLU n 
2 25  SER n 
2 26  ASN n 
2 27  GLY n 
2 28  PRO n 
2 29  VAL n 
2 30  LYS n 
2 31  VAL n 
2 32  TRP n 
2 33  GLY n 
2 34  SER n 
2 35  ILE n 
2 36  LYS n 
2 37  GLY n 
2 38  LEU n 
2 39  THR n 
2 40  GLU n 
2 41  GLY n 
2 42  LEU n 
2 43  HIS n 
2 44  GLY n 
2 45  PHE n 
2 46  HIS n 
2 47  VAL n 
2 48  HIS n 
2 49  GLU n 
2 50  PHE n 
2 51  GLY n 
2 52  ASP n 
2 53  ASN n 
2 54  THR n 
2 55  ALA n 
2 56  GLY n 
2 57  CYS n 
2 58  THR n 
2 59  SER n 
2 60  ALA n 
2 61  GLY n 
2 62  PRO n 
2 63  HIS n 
2 64  PHE n 
2 65  ASN n 
2 66  PRO n 
2 67  LEU n 
2 68  SER n 
2 69  ARG n 
2 70  LYS n 
2 71  HIS n 
2 72  GLY n 
2 73  GLY n 
2 74  PRO n 
2 75  LYS n 
2 76  ASP n 
2 77  GLU n 
2 78  GLU n 
2 79  ARG n 
2 80  HIS n 
2 81  VAL n 
2 82  GLY n 
2 83  ASP n 
2 84  LEU n 
2 85  GLY n 
2 86  ASN n 
2 87  VAL n 
2 88  THR n 
2 89  ALA n 
2 90  ASP n 
2 91  LYS n 
2 92  ASP n 
2 93  GLY n 
2 94  VAL n 
2 95  ALA n 
2 96  ASP n 
2 97  VAL n 
2 98  SER n 
2 99  ILE n 
2 100 GLU n 
2 101 ASP n 
2 102 SER n 
2 103 VAL n 
2 104 ILE n 
2 105 SER n 
2 106 LEU n 
2 107 SER n 
2 108 GLY n 
2 109 ASP n 
2 110 HIS n 
2 111 CYS n 
2 112 ILE n 
2 113 THR n 
2 114 GLY n 
2 115 ARG n 
2 116 THR n 
2 117 LEU n 
2 118 VAL n 
2 119 VAL n 
2 120 HIS n 
2 121 GLU n 
2 122 LYS n 
2 123 ALA n 
2 124 ASP n 
2 125 ASP n 
2 126 LEU n 
2 127 GLY n 
2 128 LYS n 
2 129 GLY n 
2 130 GLY n 
2 131 ASN n 
2 132 GLU n 
2 133 GLU n 
2 134 SER n 
2 135 THR n 
2 136 LYS n 
2 137 THR n 
2 138 GLY n 
2 139 ASN n 
2 140 ALA n 
2 141 GLY n 
2 142 SER n 
2 143 ARG n 
2 144 LEU n 
2 145 ALA n 
2 146 CYS n 
2 147 GLY n 
2 148 VAL n 
2 149 ILE n 
2 150 GLY n 
2 151 ILE n 
2 152 ALA n 
2 153 GLN n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_entity_src_gen.pdbx_seq_type 
_entity_src_gen.pdbx_beg_seq_num 
_entity_src_gen.pdbx_end_seq_num 
_entity_src_gen.gene_src_common_name 
_entity_src_gen.gene_src_genus 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
_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 
1 1 sample ? ? ? HUMAN ? ? ? ? ? ? ? ? 'HOMO SAPIENS' 9606 ? ? ? ? ? ? ? ? 'ESCHERICHIA COLI BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? 
? ? ? ? PLASMID ? ? ? PET303 ? ? 
2 1 sample ? ? ? HUMAN ? ? ? ? ? ? ? ? 'HOMO SAPIENS' 9606 ? ? ? ? ? ? ? ? 'ESCHERICHIA COLI BL21(DE3)' 469008 ? ? ? ? ? ? ? ? ? ? 
? ? ? ? PLASMID ? ? ? PET303 ? ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
1 UNP SODC_HUMAN 1 ? ? P00441 ? 
2 UNP SODC_HUMAN 2 ? ? P00441 ? 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 4A7G A 1 ? 153 ? P00441 2 ? 154 ? 1 153 
2 2 4A7G F 1 ? 153 ? P00441 2 ? 154 ? 1 153 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 4A7G THR A 99  ? UNP P00441 ILE 100 conflict              99  1 
1 4A7G THR A 113 ? UNP P00441 ILE 114 'engineered mutation' 113 2 
2 4A7G THR F 113 ? UNP P00441 ILE 114 'engineered mutation' 113 3 
# 
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 
12I non-polymer         . '4-(4-METHYLPIPERAZIN-1-YL)QUINAZOLINE' ? 'C13 H16 N4'     228.293 
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 
CU  non-polymer         . 'COPPER (II) ION'                       ? 'Cu 2'           63.546  
CYS 'L-peptide linking' y CYSTEINE                                ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE                               ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID'                         ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE                                 ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE                               ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER                                   ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE                              ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE                                 ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE                                  ? 'C6 H15 N2 O2 1' 147.195 
PHE 'L-peptide linking' y PHENYLALANINE                           ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                                 ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                                  ? 'C3 H7 N O3'     105.093 
SO4 non-polymer         . 'SULFATE ION'                           ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE                               ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                              ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE                                  ? 'C5 H11 N O2'    117.146 
ZN  non-polymer         . 'ZINC ION'                              ? 'Zn 2'           65.409  
# 
_exptl.entry_id          4A7G 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      1.9 
_exptl_crystal.density_percent_sol   34 
_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    '100MM SODIUM ACETATE PH 5, 150 MM SODIUM CHLORIDE, 2.5 M AMMONIUM SULPHATE' 
# 
_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                   'ADSC QUANTUM 315r' 
_diffrn_detector.pdbx_collection_date   2010-04-06 
_diffrn_detector.details                MIRRORS 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    SI111 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.866 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'SOLEIL BEAMLINE PROXIMA 1' 
_diffrn_source.pdbx_synchrotron_site       SOLEIL 
_diffrn_source.pdbx_synchrotron_beamline   'PROXIMA 1' 
_diffrn_source.pdbx_wavelength             0.866 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     4A7G 
_reflns.observed_criterion_sigma_I   0.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             50.00 
_reflns.d_resolution_high            1.24 
_reflns.number_obs                   71339 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.9 
_reflns.pdbx_Rmerge_I_obs            0.08 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.00 
_reflns.B_iso_Wilson_estimate        10.4 
_reflns.pdbx_redundancy              4.1 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             1.24 
_reflns_shell.d_res_low              1.28 
_reflns_shell.percent_possible_all   99.9 
_reflns_shell.Rmerge_I_obs           0.69 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    1.70 
_reflns_shell.pdbx_redundancy        3.4 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4A7G 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     67694 
_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                             48.33 
_refine.ls_d_res_high                            1.24 
_refine.ls_percent_reflns_obs                    99.68 
_refine.ls_R_factor_obs                          0.14070 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.13884 
_refine.ls_R_factor_R_free                       0.17526 
_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                  3616 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.978 
_refine.correlation_coeff_Fo_to_Fc_free          0.966 
_refine.B_iso_mean                               12.052 
_refine.aniso_B[1][1]                            -0.19 
_refine.aniso_B[2][2]                            -0.12 
_refine.aniso_B[3][3]                            0.36 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.11 
_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. U VALUES REFINED INDIVIDUALLY' 
_refine.pdbx_starting_model                      NONE 
_refine.pdbx_method_to_determine_struct          OTHER 
_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                       0.046 
_refine.pdbx_overall_ESU_R_Free                  0.046 
_refine.overall_SU_ML                            0.029 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             1.485 
_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        2217 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         84 
_refine_hist.number_atoms_solvent             388 
_refine_hist.number_atoms_total               2689 
_refine_hist.d_res_high                       1.24 
_refine_hist.d_res_low                        48.33 
# 
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             0.014  0.021  ? 2533 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.001  0.020  ? 1654 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.612  1.978  ? 3456 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            0.902  3.000  ? 4089 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       6.805  5.000  ? 349  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       38.441 25.728 ? 103  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       11.751 15.000 ? 403  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       16.406 15.000 ? 9    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.090  0.200  ? 363  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 3012 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.002  0.020  ? 471  '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                  1.575  1.500  ? 1633 'X-RAY DIFFRACTION' ? 
r_mcbond_other               0.499  1.500  ? 699  'X-RAY DIFFRACTION' ? 
r_mcangle_it                 2.426  2.000  ? 2626 'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  3.361  3.000  ? 900  'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 4.736  4.500  ? 830  '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           1.272  3.000  ? 4187 '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                       1.239 
_refine_ls_shell.d_res_low                        1.271 
_refine_ls_shell.number_reflns_R_work             4882 
_refine_ls_shell.R_factor_R_work                  0.250 
_refine_ls_shell.percent_reflns_obs               97.44 
_refine_ls_shell.R_factor_R_free                  0.285 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             262 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  4A7G 
_struct.title                     
'Structure of human I113T SOD1 mutant complexed with 4-methylpiperazin- 1-yl)quinazoline in the p21 space group.' 
_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        4A7G 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            
'OXIDOREDUCTASE, AMYOTROPHIC LATERAL SCLEROSIS, ANTIOXIDANT, DISEASE MUTATION, METAL-BINDING, ZN SUPEROXIDE DISMUTASE' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 7 ? 
J N N 3 ? 
K N N 3 ? 
L N N 5 ? 
M N N 3 ? 
N N N 6 ? 
O N N 4 ? 
P N N 8 ? 
Q N N 8 ? 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 GLY A 56  ? GLY A 61  ? GLY A 56  GLY A 61  5 ? 6 
HELX_P HELX_P2 2 GLU A 132 ? LYS A 136 ? GLU A 132 LYS A 136 5 ? 5 
HELX_P HELX_P3 3 GLY B 56  ? GLY B 61  ? GLY F 56  GLY F 61  5 ? 6 
HELX_P HELX_P4 4 GLU B 132 ? LYS B 136 ? GLU F 132 LYS F 136 5 ? 5 
# 
_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 ? ? ? 1_555 A CYS 146 SG  ? ? A CYS 57   A CYS 146 1_555 ? ? ? ? ? ? ? 2.167 ? 
disulf2  disulf ? ? B CYS 57 SG ? ? ? 1_555 B CYS 146 SG  ? ? F CYS 57   F CYS 146 1_555 ? ? ? ? ? ? ? 2.170 ? 
metalc1  metalc ? ? G CU  .  CU ? ? ? 1_555 A HIS 48  NE2 ? ? A CU  1157 A HIS 48  1_555 ? ? ? ? ? ? ? 1.918 ? 
metalc2  metalc ? ? G CU  .  CU ? ? ? 1_555 A HIS 120 NE2 ? ? A CU  1157 A HIS 120 1_555 ? ? ? ? ? ? ? 1.935 ? 
metalc3  metalc ? ? G CU  .  CU ? ? ? 1_555 A HIS 46  ND1 ? ? A CU  1157 A HIS 46  1_555 ? ? ? ? ? ? ? 2.051 ? 
metalc4  metalc ? ? H ZN  .  ZN ? ? ? 1_555 A ASP 83  OD1 ? ? A ZN  1158 A ASP 83  1_555 ? ? ? ? ? ? ? 1.965 ? 
metalc5  metalc ? ? H ZN  .  ZN ? ? ? 1_555 A HIS 71  ND1 ? ? A ZN  1158 A HIS 71  1_555 ? ? ? ? ? ? ? 2.058 ? 
metalc6  metalc ? ? H ZN  .  ZN ? ? ? 1_555 A HIS 63  ND1 ? ? A ZN  1158 A HIS 63  1_555 ? ? ? ? ? ? ? 2.038 ? 
metalc7  metalc ? ? H ZN  .  ZN ? ? ? 1_555 A HIS 80  ND1 ? ? A ZN  1158 A HIS 80  1_555 ? ? ? ? ? ? ? 2.036 ? 
metalc8  metalc ? ? L CU  .  CU A ? ? 1_555 B HIS 120 NE2 ? ? F CU  1156 F HIS 120 1_555 ? ? ? ? ? ? ? 1.985 ? 
metalc9  metalc ? ? L CU  .  CU A ? ? 1_555 B HIS 48  NE2 ? ? F CU  1156 F HIS 48  1_555 ? ? ? ? ? ? ? 1.950 ? 
metalc10 metalc ? ? L CU  .  CU A ? ? 1_555 B HIS 46  ND1 ? ? F CU  1156 F HIS 46  1_555 ? ? ? ? ? ? ? 2.051 ? 
metalc11 metalc ? ? L CU  .  CU B ? ? 1_555 B HIS 46  ND1 ? ? F CU  1156 F HIS 46  1_555 ? ? ? ? ? ? ? 2.509 ? 
metalc12 metalc ? ? L CU  .  CU B ? ? 1_555 B HIS 48  NE2 ? ? F CU  1156 F HIS 48  1_555 ? ? ? ? ? ? ? 1.850 ? 
metalc13 metalc ? ? L CU  .  CU B ? ? 1_555 B HIS 120 NE2 ? ? F CU  1156 F HIS 120 1_555 ? ? ? ? ? ? ? 1.754 ? 
metalc14 metalc ? ? N ZN  .  ZN ? ? ? 1_555 B ASP 83  OD1 ? ? F ZN  1157 F ASP 83  1_555 ? ? ? ? ? ? ? 1.974 ? 
metalc15 metalc ? ? N ZN  .  ZN ? ? ? 1_555 B HIS 80  ND1 ? ? F ZN  1157 F HIS 80  1_555 ? ? ? ? ? ? ? 2.035 ? 
metalc16 metalc ? ? N ZN  .  ZN ? ? ? 1_555 B HIS 71  ND1 ? ? F ZN  1157 F HIS 71  1_555 ? ? ? ? ? ? ? 2.058 ? 
metalc17 metalc ? ? N ZN  .  ZN ? ? ? 1_555 B HIS 63  ND1 ? ? F ZN  1157 F HIS 63  1_555 ? ? ? ? ? ? ? 2.032 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
_struct_mon_prot_cis.pdbx_id                1 
_struct_mon_prot_cis.label_comp_id          GLY 
_struct_mon_prot_cis.label_seq_id           12 
_struct_mon_prot_cis.label_asym_id          B 
_struct_mon_prot_cis.label_alt_id           . 
_struct_mon_prot_cis.pdbx_PDB_ins_code      ? 
_struct_mon_prot_cis.auth_comp_id           GLY 
_struct_mon_prot_cis.auth_seq_id            12 
_struct_mon_prot_cis.auth_asym_id           F 
_struct_mon_prot_cis.pdbx_label_comp_id_2   PRO 
_struct_mon_prot_cis.pdbx_label_seq_id_2    13 
_struct_mon_prot_cis.pdbx_label_asym_id_2   B 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2    ? 
_struct_mon_prot_cis.pdbx_auth_comp_id_2    PRO 
_struct_mon_prot_cis.pdbx_auth_seq_id_2     13 
_struct_mon_prot_cis.pdbx_auth_asym_id_2    F 
_struct_mon_prot_cis.pdbx_PDB_model_num     1 
_struct_mon_prot_cis.pdbx_omega_angle       2.48 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 5 ? 
AB ? 4 ? 
FA ? 5 ? 
FB ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA 1 2 ? anti-parallel 
AA 2 3 ? anti-parallel 
AA 3 4 ? anti-parallel 
AA 4 5 ? anti-parallel 
AB 1 2 ? anti-parallel 
AB 2 3 ? anti-parallel 
AB 3 4 ? anti-parallel 
FA 1 2 ? anti-parallel 
FA 2 3 ? anti-parallel 
FA 3 4 ? anti-parallel 
FA 4 5 ? anti-parallel 
FB 1 2 ? anti-parallel 
FB 2 3 ? anti-parallel 
FB 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA 1 ALA A 95  ? ASP A 101 ? ALA A 95  ASP A 101 
AA 2 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
AA 3 GLN A 15  ? GLN A 22  ? GLN A 15  GLN A 22  
AA 4 THR A 2   ? LEU A 8   ? THR A 2   LEU A 8   
AA 5 GLY A 150 ? ILE A 151 ? GLY A 150 ILE A 151 
AB 1 ASP A 83  ? ALA A 89  ? ASP A 83  ALA A 89  
AB 2 GLY A 41  ? HIS A 48  ? GLY A 41  HIS A 48  
AB 3 THR A 116 ? HIS A 120 ? THR A 116 HIS A 120 
AB 4 ARG A 143 ? VAL A 148 ? ARG A 143 VAL A 148 
FA 1 ALA B 95  ? ASP B 101 ? ALA F 95  ASP F 101 
FA 2 VAL B 29  ? LYS B 36  ? VAL F 29  LYS F 36  
FA 3 VAL B 14  ? GLN B 22  ? VAL F 14  GLN F 22  
FA 4 THR B 2   ? GLY B 10  ? THR F 2   GLY F 10  
FA 5 GLY B 150 ? ILE B 151 ? GLY F 150 ILE F 151 
FB 1 ASP B 83  ? ALA B 89  ? ASP F 83  ALA F 89  
FB 2 GLY B 41  ? HIS B 48  ? GLY F 41  HIS F 48  
FB 3 THR B 116 ? HIS B 120 ? THR F 116 HIS F 120 
FB 4 ARG B 143 ? VAL B 148 ? ARG F 143 VAL F 148 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA 1 2 N ASP A 101 ? N ASP A 101 O VAL A 29  ? O VAL A 29  
AA 2 3 N LYS A 36  ? N LYS A 36  O GLN A 15  ? O GLN A 15  
AA 3 4 N GLN A 22  ? N GLN A 22  O THR A 2   ? O THR A 2   
AA 4 5 N VAL A 5   ? N VAL A 5   O GLY A 150 ? O GLY A 150 
AB 1 2 N ALA A 89  ? N ALA A 89  O GLY A 41  ? O GLY A 41  
AB 2 3 N HIS A 48  ? N HIS A 48  O THR A 116 ? O THR A 116 
AB 3 4 O VAL A 119 ? O VAL A 119 N LEU A 144 ? N LEU A 144 
FA 1 2 N ASP B 101 ? N ASP F 101 O VAL B 29  ? O VAL F 29  
FA 2 3 N LYS B 36  ? N LYS F 36  O GLN B 15  ? O GLN F 15  
FA 3 4 N GLN B 22  ? N GLN F 22  O THR B 2   ? O THR F 2   
FA 4 5 N VAL B 5   ? N VAL F 5   O GLY B 150 ? O GLY F 150 
FB 1 2 N ALA B 89  ? N ALA F 89  O GLY B 41  ? O GLY F 41  
FB 2 3 N HIS B 48  ? N HIS F 48  O THR B 116 ? O THR F 116 
FB 3 4 O VAL B 119 ? O VAL F 119 N LEU B 144 ? N LEU F 144 
# 
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 ? ? ? ? 15 'BINDING SITE FOR RESIDUE 12I A 1000' 
AC2 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE 12I A 1001' 
AC3 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 A 1154' 
AC4 Software ? ? ? ? 6  'BINDING SITE FOR RESIDUE SO4 A 1156' 
AC5 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE CU A 1157'  
AC6 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN A 1158'  
AC7 Software ? ? ? ? 5  'BINDING SITE FOR RESIDUE ACT A 1159' 
AC8 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE 12I F 1000' 
AC9 Software ? ? ? ? 7  'BINDING SITE FOR RESIDUE SO4 F 1154' 
BC1 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE CU F 1156'  
BC2 Software ? ? ? ? 4  'BINDING SITE FOR RESIDUE ZN F 1157'  
BC3 Software ? ? ? ? 8  'BINDING SITE FOR RESIDUE SO4 F 1155' 
BC4 Software ? ? ? ? 9  'BINDING SITE FOR RESIDUE SO4 F 1158' 
BC5 Software ? ? ? ? 1  'BINDING SITE FOR RESIDUE 12I F 1000' 
# 
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 15 SER A 25  ? SER A 25   . ? 1_555 ? 
2  AC1 15 ASN A 26  ? ASN A 26   . ? 1_555 ? 
3  AC1 15 GLY A 27  ? GLY A 27   . ? 1_555 ? 
4  AC1 15 LYS A 91  ? LYS A 91   . ? 1_655 ? 
5  AC1 15 ASP A 92  ? ASP A 92   . ? 1_655 ? 
6  AC1 15 GLY A 93  ? GLY A 93   . ? 1_655 ? 
7  AC1 15 SER A 102 ? SER A 102  . ? 1_555 ? 
8  AC1 15 VAL A 103 ? VAL A 103  . ? 1_555 ? 
9  AC1 15 SER A 105 ? SER A 105  . ? 1_555 ? 
10 AC1 15 SER A 107 ? SER A 107  . ? 1_555 ? 
11 AC1 15 ASP A 109 ? ASP A 109  . ? 1_555 ? 
12 AC1 15 HIS A 110 ? HIS A 110  . ? 1_555 ? 
13 AC1 15 ACT I .   ? ACT A 1159 . ? 1_555 ? 
14 AC1 15 HOH P .   ? HOH A 2060 . ? 1_555 ? 
15 AC1 15 HOH P .   ? HOH A 2156 . ? 1_555 ? 
16 AC2 6  GLU A 21  ? GLU A 21   . ? 1_555 ? 
17 AC2 6  LYS A 30  ? LYS A 30   . ? 1_555 ? 
18 AC2 6  TRP A 32  ? TRP A 32   . ? 1_555 ? 
19 AC2 6  SER A 98  ? SER A 98   . ? 1_555 ? 
20 AC2 6  HOH P .   ? HOH A 2062 . ? 1_555 ? 
21 AC2 6  HOH P .   ? HOH A 2214 . ? 1_555 ? 
22 AC3 8  GLU A 133 ? GLU A 133  . ? 1_555 ? 
23 AC3 8  THR A 137 ? THR A 137  . ? 1_555 ? 
24 AC3 8  ASN A 139 ? ASN A 139  . ? 1_555 ? 
25 AC3 8  ALA A 140 ? ALA A 140  . ? 1_555 ? 
26 AC3 8  GLY A 141 ? GLY A 141  . ? 1_555 ? 
27 AC3 8  HOH P .   ? HOH A 2172 . ? 1_555 ? 
28 AC3 8  HOH P .   ? HOH A 2175 . ? 1_555 ? 
29 AC3 8  HOH P .   ? HOH A 2192 . ? 1_555 ? 
30 AC4 6  THR A 58  ? THR A 58   . ? 1_555 ? 
31 AC4 6  SER A 142 ? SER A 142  . ? 1_555 ? 
32 AC4 6  ARG A 143 ? ARG A 143  . ? 1_555 ? 
33 AC4 6  HOH P .   ? HOH A 2196 . ? 1_555 ? 
34 AC4 6  HOH P .   ? HOH A 2199 . ? 1_555 ? 
35 AC4 6  HOH P .   ? HOH A 2212 . ? 1_555 ? 
36 AC5 4  HIS A 46  ? HIS A 46   . ? 1_555 ? 
37 AC5 4  HIS A 48  ? HIS A 48   . ? 1_555 ? 
38 AC5 4  HIS A 63  ? HIS A 63   . ? 1_555 ? 
39 AC5 4  HIS A 120 ? HIS A 120  . ? 1_555 ? 
40 AC6 4  HIS A 63  ? HIS A 63   . ? 1_555 ? 
41 AC6 4  HIS A 71  ? HIS A 71   . ? 1_555 ? 
42 AC6 4  HIS A 80  ? HIS A 80   . ? 1_555 ? 
43 AC6 4  ASP A 83  ? ASP A 83   . ? 1_555 ? 
44 AC7 5  ASN A 26  ? ASN A 26   . ? 1_555 ? 
45 AC7 5  GLY A 27  ? GLY A 27   . ? 1_555 ? 
46 AC7 5  PRO A 28  ? PRO A 28   . ? 1_555 ? 
47 AC7 5  SER A 102 ? SER A 102  . ? 1_555 ? 
48 AC7 5  12I D .   ? 12I A 1000 . ? 1_555 ? 
49 AC8 1  TRP B 32  ? TRP F 32   . ? 1_555 ? 
50 AC9 7  GLU B 133 ? GLU F 133  . ? 1_555 ? 
51 AC9 7  THR B 137 ? THR F 137  . ? 1_555 ? 
52 AC9 7  ASN B 139 ? ASN F 139  . ? 1_555 ? 
53 AC9 7  GLY B 141 ? GLY F 141  . ? 1_555 ? 
54 AC9 7  HOH Q .   ? HOH F 2143 . ? 1_555 ? 
55 AC9 7  HOH Q .   ? HOH F 2164 . ? 1_555 ? 
56 AC9 7  HOH Q .   ? HOH F 2177 . ? 1_555 ? 
57 BC1 4  HIS B 46  ? HIS F 46   . ? 1_555 ? 
58 BC1 4  HIS B 48  ? HIS F 48   . ? 1_555 ? 
59 BC1 4  HIS B 63  ? HIS F 63   . ? 1_555 ? 
60 BC1 4  HIS B 120 ? HIS F 120  . ? 1_555 ? 
61 BC2 4  HIS B 63  ? HIS F 63   . ? 1_555 ? 
62 BC2 4  HIS B 71  ? HIS F 71   . ? 1_555 ? 
63 BC2 4  HIS B 80  ? HIS F 80   . ? 1_555 ? 
64 BC2 4  ASP B 83  ? ASP F 83   . ? 1_555 ? 
65 BC3 8  THR B 58  ? THR F 58   . ? 1_555 ? 
66 BC3 8  SER B 142 ? SER F 142  . ? 1_555 ? 
67 BC3 8  ARG B 143 ? ARG F 143  . ? 1_555 ? 
68 BC3 8  SO4 M .   ? SO4 F 1158 . ? 1_555 ? 
69 BC3 8  HOH Q .   ? HOH F 2079 . ? 1_555 ? 
70 BC3 8  HOH Q .   ? HOH F 2163 . ? 1_555 ? 
71 BC3 8  HOH Q .   ? HOH F 2165 . ? 1_555 ? 
72 BC3 8  HOH Q .   ? HOH F 2166 . ? 1_555 ? 
73 BC4 9  ASP B 11  ? ASP F 11   . ? 1_555 ? 
74 BC4 9  GLY B 56  ? GLY F 56   . ? 1_555 ? 
75 BC4 9  CYS B 57  ? CYS F 57   . ? 1_555 ? 
76 BC4 9  THR B 58  ? THR F 58   . ? 1_555 ? 
77 BC4 9  ARG B 143 ? ARG F 143  . ? 1_555 ? 
78 BC4 9  SO4 K .   ? SO4 F 1155 . ? 1_555 ? 
79 BC4 9  HOH Q .   ? HOH F 2017 . ? 1_555 ? 
80 BC4 9  HOH Q .   ? HOH F 2074 . ? 1_555 ? 
81 BC4 9  HOH Q .   ? HOH F 2076 . ? 1_555 ? 
82 BC5 1  TRP B 32  ? TRP F 32   . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4A7G 
_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                    4A7G 
_atom_sites.fract_transf_matrix[1][1]   0.025778 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006662 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014630 
_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]   0.020690 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C  
CU 
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . ALA A 1 1   ? 9.915   5.784   30.612  1.00 21.29  ? 1    ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 9.207   4.528   30.195  1.00 18.78  ? 1    ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 8.875   4.612   28.726  1.00 18.11  ? 1    ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? 8.721   5.678   28.159  1.00 21.00  ? 1    ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 7.915   4.309   30.979  1.00 19.53  ? 1    ALA A CB  1 
ATOM   6    N  N   . THR A 1 2   ? 8.717   3.461   28.121  1.00 14.31  ? 2    THR A N   1 
ATOM   7    C  CA  . THR A 1 2   ? 8.321   3.346   26.735  1.00 13.55  ? 2    THR A CA  1 
ATOM   8    C  C   . THR A 1 2   ? 6.906   2.803   26.666  1.00 10.86  ? 2    THR A C   1 
ATOM   9    O  O   . THR A 1 2   ? 6.543   1.916   27.438  1.00 10.71  ? 2    THR A O   1 
ATOM   10   C  CB  . THR A 1 2   ? 9.305   2.414   26.050  1.00 15.03  ? 2    THR A CB  1 
ATOM   11   O  OG1 . THR A 1 2   ? 10.617  2.981   26.172  1.00 18.82  ? 2    THR A OG1 1 
ATOM   12   C  CG2 . THR A 1 2   ? 8.971   2.209   24.600  1.00 16.54  ? 2    THR A CG2 1 
ATOM   13   N  N   . LYS A 1 3   ? 6.093   3.352   25.764  1.00 10.12  ? 3    LYS A N   1 
ATOM   14   C  CA  . LYS A 1 3   ? 4.697   3.008   25.658  1.00 9.62   ? 3    LYS A CA  1 
ATOM   15   C  C   . LYS A 1 3   ? 4.329   2.658   24.239  1.00 9.26   ? 3    LYS A C   1 
ATOM   16   O  O   . LYS A 1 3   ? 4.861   3.214   23.284  1.00 8.97   ? 3    LYS A O   1 
ATOM   17   C  CB  . LYS A 1 3   ? 3.838   4.171   26.134  1.00 11.51  ? 3    LYS A CB  1 
ATOM   18   C  CG  . LYS A 1 3   ? 4.063   4.440   27.605  1.00 13.80  ? 3    LYS A CG  1 
ATOM   19   C  CD  . LYS A 1 3   ? 3.467   5.750   28.056  1.00 17.47  ? 3    LYS A CD  1 
ATOM   20   C  CE  . LYS A 1 3   ? 3.985   6.106   29.435  1.00 22.40  ? 3    LYS A CE  1 
ATOM   21   N  NZ  . LYS A 1 3   ? 3.468   7.408   29.910  1.00 27.40  ? 3    LYS A NZ  1 
ATOM   22   N  N   . ALA A 1 4   ? 3.345   1.773   24.112  1.00 8.80   ? 4    ALA A N   1 
ATOM   23   C  CA  . ALA A 1 4   ? 2.817   1.394   22.804  1.00 8.29   ? 4    ALA A CA  1 
ATOM   24   C  C   . ALA A 1 4   ? 1.343   1.093   22.942  1.00 7.98   ? 4    ALA A C   1 
ATOM   25   O  O   . ALA A 1 4   ? 0.838   0.946   24.054  1.00 9.25   ? 4    ALA A O   1 
ATOM   26   C  CB  . ALA A 1 4   ? 3.579   0.199   22.197  1.00 8.73   ? 4    ALA A CB  1 
ATOM   27   N  N   . VAL A 1 5   ? 0.661   0.993   21.812  1.00 8.94   ? 5    VAL A N   1 
ATOM   28   C  CA  . VAL A 1 5   ? -0.784  0.842   21.807  1.00 9.09   ? 5    VAL A CA  1 
ATOM   29   C  C   . VAL A 1 5   ? -1.204  0.088   20.544  1.00 8.20   ? 5    VAL A C   1 
ATOM   30   O  O   . VAL A 1 5   ? -0.519  0.153   19.532  1.00 8.97   ? 5    VAL A O   1 
ATOM   31   C  CB  . VAL A 1 5   ? -1.435  2.220   21.889  1.00 9.92   ? 5    VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 5   ? -1.142  3.044   20.658  1.00 12.92  ? 5    VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 5   ? -2.955  2.151   22.148  1.00 12.59  ? 5    VAL A CG2 1 
ATOM   34   N  N   . CYS A 1 6   ? -2.321  -0.626  20.622  1.00 8.34   ? 6    CYS A N   1 
ATOM   35   C  CA  . CYS A 1 6   ? -2.888  -1.332  19.505  1.00 8.07   ? 6    CYS A CA  1 
ATOM   36   C  C   . CYS A 1 6   ? -4.398  -1.213  19.516  1.00 7.82   ? 6    CYS A C   1 
ATOM   37   O  O   . CYS A 1 6   ? -5.021  -1.502  20.526  1.00 9.29   ? 6    CYS A O   1 
ATOM   38   C  CB  . CYS A 1 6   ? -2.493  -2.821  19.609  1.00 9.16   ? 6    CYS A CB  1 
ATOM   39   S  SG  . CYS A 1 6   ? -2.982  -3.751  18.167  1.00 11.48  ? 6    CYS A SG  1 
ATOM   40   N  N   . VAL A 1 7   ? -4.959  -0.830  18.379  1.00 8.27   ? 7    VAL A N   1 
ATOM   41   C  CA  . VAL A 1 7   ? -6.385  -0.814  18.185  1.00 9.09   ? 7    VAL A CA  1 
ATOM   42   C  C   . VAL A 1 7   ? -6.728  -2.080  17.393  1.00 9.18   ? 7    VAL A C   1 
ATOM   43   O  O   . VAL A 1 7   ? -6.299  -2.262  16.266  1.00 9.63   ? 7    VAL A O   1 
ATOM   44   C  CB  . VAL A 1 7   ? -6.842  0.443   17.420  1.00 10.24  ? 7    VAL A CB  1 
ATOM   45   C  CG1 . VAL A 1 7   ? -8.345  0.381   17.155  1.00 12.60  ? 7    VAL A CG1 1 
ATOM   46   C  CG2 . VAL A 1 7   ? -6.433  1.731   18.191  1.00 11.29  ? 7    VAL A CG2 1 
ATOM   47   N  N   A LEU A 1 8   ? -7.508  -2.964  17.999  0.80 9.37   ? 8    LEU A N   1 
ATOM   48   N  N   B LEU A 1 8   ? -7.495  -2.974  18.008  0.20 9.45   ? 8    LEU A N   1 
ATOM   49   C  CA  A LEU A 1 8   ? -7.909  -4.212  17.356  0.80 9.64   ? 8    LEU A CA  1 
ATOM   50   C  CA  B LEU A 1 8   ? -7.894  -4.207  17.338  0.20 9.56   ? 8    LEU A CA  1 
ATOM   51   C  C   A LEU A 1 8   ? -9.235  -4.079  16.662  0.80 9.75   ? 8    LEU A C   1 
ATOM   52   C  C   B LEU A 1 8   ? -9.226  -4.037  16.637  0.20 10.11  ? 8    LEU A C   1 
ATOM   53   O  O   A LEU A 1 8   ? -10.223 -3.716  17.300  0.80 10.57  ? 8    LEU A O   1 
ATOM   54   O  O   B LEU A 1 8   ? -10.189 -3.539  17.218  0.20 10.27  ? 8    LEU A O   1 
ATOM   55   C  CB  A LEU A 1 8   ? -8.036  -5.305  18.404  0.80 10.31  ? 8    LEU A CB  1 
ATOM   56   C  CB  B LEU A 1 8   ? -7.950  -5.370  18.321  0.20 9.54   ? 8    LEU A CB  1 
ATOM   57   C  CG  A LEU A 1 8   ? -6.800  -5.744  19.185  0.80 11.26  ? 8    LEU A CG  1 
ATOM   58   C  CG  B LEU A 1 8   ? -6.567  -5.753  18.840  0.20 8.54   ? 8    LEU A CG  1 
ATOM   59   C  CD1 A LEU A 1 8   ? -7.236  -6.618  20.367  0.80 13.70  ? 8    LEU A CD1 1 
ATOM   60   C  CD1 B LEU A 1 8   ? -6.134  -4.714  19.857  0.20 8.03   ? 8    LEU A CD1 1 
ATOM   61   C  CD2 A LEU A 1 8   ? -5.856  -6.495  18.290  0.80 15.07  ? 8    LEU A CD2 1 
ATOM   62   C  CD2 B LEU A 1 8   ? -6.541  -7.154  19.438  0.20 9.70   ? 8    LEU A CD2 1 
ATOM   63   N  N   . LYS A 1 9   ? -9.250  -4.442  15.370  1.00 10.42  ? 9    LYS A N   1 
ATOM   64   C  CA  . LYS A 1 9   ? -10.439 -4.401  14.537  1.00 12.50  ? 9    LYS A CA  1 
ATOM   65   C  C   . LYS A 1 9   ? -10.416 -5.579  13.590  1.00 11.99  ? 9    LYS A C   1 
ATOM   66   O  O   . LYS A 1 9   ? -9.357  -6.102  13.254  1.00 11.83  ? 9    LYS A O   1 
ATOM   67   C  CB  . LYS A 1 9   ? -10.518 -3.120  13.690  1.00 14.32  ? 9    LYS A CB  1 
ATOM   68   C  CG  . LYS A 1 9   ? -10.664 -1.832  14.467  1.00 18.44  ? 9    LYS A CG  1 
ATOM   69   C  CD  . LYS A 1 9   ? -10.834 -0.659  13.475  0.50 20.51  ? 9    LYS A CD  1 
ATOM   70   C  CE  . LYS A 1 9   ? -12.236 -0.607  12.852  0.50 22.79  ? 9    LYS A CE  1 
ATOM   71   N  NZ  . LYS A 1 9   ? -12.463 0.627   12.035  0.50 23.75  ? 9    LYS A NZ  1 
ATOM   72   N  N   . GLY A 1 10  ? -11.592 -5.979  13.138  1.00 13.65  ? 10   GLY A N   1 
ATOM   73   C  CA  . GLY A 1 10  ? -11.703 -7.033  12.128  1.00 13.73  ? 10   GLY A CA  1 
ATOM   74   C  C   . GLY A 1 10  ? -12.951 -6.888  11.306  1.00 15.77  ? 10   GLY A C   1 
ATOM   75   O  O   . GLY A 1 10  ? -13.574 -5.828  11.285  1.00 17.32  ? 10   GLY A O   1 
ATOM   76   N  N   . ASP A 1 11  ? -13.340 -7.967  10.655  1.00 17.53  ? 11   ASP A N   1 
ATOM   77   C  CA  . ASP A 1 11  ? -14.534 -7.938  9.800   1.00 19.29  ? 11   ASP A CA  1 
ATOM   78   C  C   . ASP A 1 11  ? -15.829 -8.179  10.542  1.00 19.17  ? 11   ASP A C   1 
ATOM   79   O  O   . ASP A 1 11  ? -16.910 -7.964  9.980   1.00 20.42  ? 11   ASP A O   1 
ATOM   80   C  CB  . ASP A 1 11  ? -14.391 -8.960  8.692   1.00 20.74  ? 11   ASP A CB  1 
ATOM   81   C  CG  . ASP A 1 11  ? -13.260 -8.635  7.736   1.00 24.36  ? 11   ASP A CG  1 
ATOM   82   O  OD1 . ASP A 1 11  ? -12.976 -7.434  7.518   1.00 30.95  ? 11   ASP A OD1 1 
ATOM   83   O  OD2 . ASP A 1 11  ? -12.651 -9.588  7.200   1.00 31.47  ? 11   ASP A OD2 1 
ATOM   84   N  N   . GLY A 1 12  ? -15.741 -8.646  11.773  1.00 18.31  ? 12   GLY A N   1 
ATOM   85   C  CA  . GLY A 1 12  ? -16.908 -8.916  12.591  1.00 17.28  ? 12   GLY A CA  1 
ATOM   86   C  C   . GLY A 1 12  ? -17.013 -7.969  13.765  1.00 16.52  ? 12   GLY A C   1 
ATOM   87   O  O   . GLY A 1 12  ? -16.552 -6.824  13.699  1.00 17.66  ? 12   GLY A O   1 
ATOM   88   N  N   . PRO A 1 13  ? -17.603 -8.446  14.867  1.00 15.58  ? 13   PRO A N   1 
ATOM   89   C  CA  . PRO A 1 13  ? -17.868 -7.561  16.001  1.00 15.71  ? 13   PRO A CA  1 
ATOM   90   C  C   . PRO A 1 13  ? -16.741 -7.380  17.013  1.00 14.40  ? 13   PRO A C   1 
ATOM   91   O  O   . PRO A 1 13  ? -16.876 -6.588  17.956  1.00 15.11  ? 13   PRO A O   1 
ATOM   92   C  CB  . PRO A 1 13  ? -19.052 -8.243  16.675  1.00 16.61  ? 13   PRO A CB  1 
ATOM   93   C  CG  . PRO A 1 13  ? -18.796 -9.679  16.444  1.00 15.58  ? 13   PRO A CG  1 
ATOM   94   C  CD  . PRO A 1 13  ? -18.287 -9.744  15.023  1.00 15.61  ? 13   PRO A CD  1 
ATOM   95   N  N   . VAL A 1 14  ? -15.646 -8.101  16.837  1.00 13.17  ? 14   VAL A N   1 
ATOM   96   C  CA  . VAL A 1 14  ? -14.603 -8.086  17.829  1.00 11.80  ? 14   VAL A CA  1 
ATOM   97   C  C   . VAL A 1 14  ? -13.754 -6.822  17.692  1.00 11.76  ? 14   VAL A C   1 
ATOM   98   O  O   . VAL A 1 14  ? -13.261 -6.488  16.620  1.00 12.83  ? 14   VAL A O   1 
ATOM   99   C  CB  . VAL A 1 14  ? -13.738 -9.346  17.742  1.00 11.00  ? 14   VAL A CB  1 
ATOM   100  C  CG1 . VAL A 1 14  ? -12.606 -9.259  18.780  1.00 11.88  ? 14   VAL A CG1 1 
ATOM   101  C  CG2 . VAL A 1 14  ? -14.589 -10.572 17.943  1.00 12.86  ? 14   VAL A CG2 1 
ATOM   102  N  N   . GLN A 1 15  ? -13.620 -6.088  18.772  1.00 12.25  ? 15   GLN A N   1 
ATOM   103  C  CA  . GLN A 1 15  ? -12.807 -4.887  18.736  1.00 13.20  ? 15   GLN A CA  1 
ATOM   104  C  C   . GLN A 1 15  ? -12.253 -4.612  20.101  1.00 12.07  ? 15   GLN A C   1 
ATOM   105  O  O   . GLN A 1 15  ? -12.837 -5.010  21.092  1.00 13.42  ? 15   GLN A O   1 
ATOM   106  C  CB  . GLN A 1 15  ? -13.607 -3.693  18.241  1.00 15.79  ? 15   GLN A CB  1 
ATOM   107  C  CG  . GLN A 1 15  ? -14.716 -3.306  19.082  1.00 18.75  ? 15   GLN A CG  1 
ATOM   108  C  CD  . GLN A 1 15  ? -15.350 -2.029  18.599  1.00 24.78  ? 15   GLN A CD  1 
ATOM   109  O  OE1 . GLN A 1 15  ? -14.929 -0.928  18.954  1.00 29.11  ? 15   GLN A OE1 1 
ATOM   110  N  NE2 . GLN A 1 15  ? -16.365 -2.169  17.773  1.00 29.03  ? 15   GLN A NE2 1 
ATOM   111  N  N   . GLY A 1 16  ? -11.102 -3.978  20.163  1.00 11.60  ? 16   GLY A N   1 
ATOM   112  C  CA  . GLY A 1 16  ? -10.539 -3.656  21.460  1.00 12.69  ? 16   GLY A CA  1 
ATOM   113  C  C   . GLY A 1 16  ? -9.401  -2.679  21.385  1.00 10.61  ? 16   GLY A C   1 
ATOM   114  O  O   . GLY A 1 16  ? -9.035  -2.264  20.291  1.00 12.35  ? 16   GLY A O   1 
ATOM   115  N  N   . ILE A 1 17  ? -8.902  -2.297  22.542  1.00 11.29  ? 17   ILE A N   1 
ATOM   116  C  CA  . ILE A 1 17  ? -7.775  -1.388  22.669  1.00 11.36  ? 17   ILE A CA  1 
ATOM   117  C  C   . ILE A 1 17  ? -6.852  -2.007  23.687  1.00 9.81   ? 17   ILE A C   1 
ATOM   118  O  O   . ILE A 1 17  ? -7.272  -2.328  24.808  1.00 10.95  ? 17   ILE A O   1 
ATOM   119  C  CB  . ILE A 1 17  ? -8.204  0.002   23.197  1.00 13.26  ? 17   ILE A CB  1 
ATOM   120  C  CG1 . ILE A 1 17  ? -9.241  0.679   22.307  1.00 17.42  ? 17   ILE A CG1 1 
ATOM   121  C  CG2 . ILE A 1 17  ? -7.011  0.899   23.380  1.00 14.30  ? 17   ILE A CG2 1 
ATOM   122  C  CD1 . ILE A 1 17  ? -8.720  1.185   21.024  1.00 18.21  ? 17   ILE A CD1 1 
ATOM   123  N  N   . ILE A 1 18  ? -5.591  -2.185  23.303  1.00 9.09   ? 18   ILE A N   1 
ATOM   124  C  CA  . ILE A 1 18  ? -4.586  -2.768  24.184  1.00 9.06   ? 18   ILE A CA  1 
ATOM   125  C  C   . ILE A 1 18  ? -3.412  -1.777  24.300  1.00 9.16   ? 18   ILE A C   1 
ATOM   126  O  O   . ILE A 1 18  ? -2.881  -1.291  23.299  1.00 9.96   ? 18   ILE A O   1 
ATOM   127  C  CB  . ILE A 1 18  ? -4.105  -4.130  23.655  1.00 9.20   ? 18   ILE A CB  1 
ATOM   128  C  CG1 . ILE A 1 18  ? -5.256  -5.115  23.527  1.00 11.24  ? 18   ILE A CG1 1 
ATOM   129  C  CG2 . ILE A 1 18  ? -2.990  -4.698  24.527  1.00 9.69   ? 18   ILE A CG2 1 
ATOM   130  C  CD1 . ILE A 1 18  ? -5.926  -5.488  24.824  1.00 12.98  ? 18   ILE A CD1 1 
ATOM   131  N  N   . ASN A 1 19  ? -3.016  -1.522  25.527  1.00 8.83   ? 19   ASN A N   1 
ATOM   132  C  CA  . ASN A 1 19  ? -1.899  -0.669  25.875  1.00 9.13   ? 19   ASN A CA  1 
ATOM   133  C  C   . ASN A 1 19  ? -0.719  -1.493  26.392  1.00 8.49   ? 19   ASN A C   1 
ATOM   134  O  O   . ASN A 1 19  ? -0.901  -2.529  27.042  1.00 8.97   ? 19   ASN A O   1 
ATOM   135  C  CB  . ASN A 1 19  ? -2.351  0.273   26.984  1.00 10.32  ? 19   ASN A CB  1 
ATOM   136  C  CG  . ASN A 1 19  ? -3.580  1.044   26.592  1.00 13.11  ? 19   ASN A CG  1 
ATOM   137  O  OD1 . ASN A 1 19  ? -3.507  1.900   25.745  1.00 14.85  ? 19   ASN A OD1 1 
ATOM   138  N  ND2 . ASN A 1 19  ? -4.709  0.720   27.172  1.00 15.59  ? 19   ASN A ND2 1 
ATOM   139  N  N   . PHE A 1 20  ? 0.483   -1.008  26.135  1.00 8.89   ? 20   PHE A N   1 
ATOM   140  C  CA  . PHE A 1 20  ? 1.745   -1.615  26.548  1.00 9.05   ? 20   PHE A CA  1 
ATOM   141  C  C   . PHE A 1 20  ? 2.596   -0.552  27.223  1.00 8.84   ? 20   PHE A C   1 
ATOM   142  O  O   . PHE A 1 20  ? 2.691   0.575   26.751  1.00 9.98   ? 20   PHE A O   1 
ATOM   143  C  CB  . PHE A 1 20  ? 2.553   -2.147  25.347  1.00 8.89   ? 20   PHE A CB  1 
ATOM   144  C  CG  . PHE A 1 20  ? 1.831   -3.149  24.487  1.00 9.66   ? 20   PHE A CG  1 
ATOM   145  C  CD1 . PHE A 1 20  ? 0.909   -2.756  23.538  1.00 10.52  ? 20   PHE A CD1 1 
ATOM   146  C  CD2 . PHE A 1 20  ? 2.068   -4.483  24.628  1.00 10.47  ? 20   PHE A CD2 1 
ATOM   147  C  CE1 . PHE A 1 20  ? 0.248   -3.683  22.754  1.00 11.66  ? 20   PHE A CE1 1 
ATOM   148  C  CE2 . PHE A 1 20  ? 1.424   -5.419  23.829  1.00 11.04  ? 20   PHE A CE2 1 
ATOM   149  C  CZ  . PHE A 1 20  ? 0.524   -5.021  22.923  1.00 10.89  ? 20   PHE A CZ  1 
ATOM   150  N  N   . GLU A 1 21  ? 3.278   -0.926  28.307  1.00 9.50   ? 21   GLU A N   1 
ATOM   151  C  CA  . GLU A 1 21  ? 4.243   -0.024  28.929  1.00 10.54  ? 21   GLU A CA  1 
ATOM   152  C  C   . GLU A 1 21  ? 5.397   -0.819  29.473  1.00 9.60   ? 21   GLU A C   1 
ATOM   153  O  O   . GLU A 1 21  ? 5.198   -1.842  30.100  1.00 11.08  ? 21   GLU A O   1 
ATOM   154  C  CB  . GLU A 1 21  ? 3.613   0.831   30.030  1.00 12.26  ? 21   GLU A CB  1 
ATOM   155  C  CG  . GLU A 1 21  ? 4.565   1.849   30.624  1.00 15.90  ? 21   GLU A CG  1 
ATOM   156  C  CD  . GLU A 1 21  ? 3.900   3.040   31.329  1.00 22.31  ? 21   GLU A CD  1 
ATOM   157  O  OE1 . GLU A 1 21  ? 2.685   3.211   31.210  1.00 25.44  ? 21   GLU A OE1 1 
ATOM   158  O  OE2 . GLU A 1 21  ? 4.624   3.832   31.982  1.00 27.98  ? 21   GLU A OE2 1 
ATOM   159  N  N   . GLN A 1 22  ? 6.596   -0.314  29.261  1.00 9.87   ? 22   GLN A N   1 
ATOM   160  C  CA  . GLN A 1 22  ? 7.824   -0.947  29.698  1.00 9.85   ? 22   GLN A CA  1 
ATOM   161  C  C   . GLN A 1 22  ? 8.666   0.115   30.385  1.00 11.87  ? 22   GLN A C   1 
ATOM   162  O  O   . GLN A 1 22  ? 9.146   1.052   29.752  1.00 12.59  ? 22   GLN A O   1 
ATOM   163  C  CB  . GLN A 1 22  ? 8.569   -1.528  28.521  1.00 10.20  ? 22   GLN A CB  1 
ATOM   164  C  CG  . GLN A 1 22  ? 9.733   -2.377  28.876  1.00 10.24  ? 22   GLN A CG  1 
ATOM   165  C  CD  . GLN A 1 22  ? 10.409  -2.991  27.659  1.00 9.79   ? 22   GLN A CD  1 
ATOM   166  O  OE1 . GLN A 1 22  ? 10.269  -2.470  26.563  1.00 11.62  ? 22   GLN A OE1 1 
ATOM   167  N  NE2 . GLN A 1 22  ? 11.150  -4.110  27.839  1.00 10.50  ? 22   GLN A NE2 1 
ATOM   168  N  N   . LYS A 1 23  ? 8.831   -0.052  31.686  1.00 14.33  ? 23   LYS A N   1 
ATOM   169  C  CA  . LYS A 1 23  ? 9.519   0.935   32.500  1.00 15.44  ? 23   LYS A CA  1 
ATOM   170  C  C   . LYS A 1 23  ? 11.014  0.999   32.157  1.00 15.85  ? 23   LYS A C   1 
ATOM   171  O  O   . LYS A 1 23  ? 11.608  2.093   32.146  1.00 17.94  ? 23   LYS A O   1 
ATOM   172  C  CB  . LYS A 1 23  ? 9.314   0.611   33.982  1.00 17.31  ? 23   LYS A CB  1 
ATOM   173  C  CG  . LYS A 1 23  ? 9.891   1.601   34.929  1.00 21.13  ? 23   LYS A CG  1 
ATOM   174  C  CD  . LYS A 1 23  ? 9.470   1.305   36.355  0.20 21.20  ? 23   LYS A CD  1 
ATOM   175  C  CE  . LYS A 1 23  ? 10.173  2.218   37.333  0.20 21.68  ? 23   LYS A CE  1 
ATOM   176  N  NZ  . LYS A 1 23  ? 9.846   1.868   38.742  0.20 21.69  ? 23   LYS A NZ  1 
ATOM   177  N  N   . GLU A 1 24  ? 11.627  -0.159  31.898  1.00 17.26  ? 24   GLU A N   1 
ATOM   178  C  CA  . GLU A 1 24  ? 13.070  -0.265  31.638  1.00 18.74  ? 24   GLU A CA  1 
ATOM   179  C  C   . GLU A 1 24  ? 13.256  -1.176  30.449  1.00 18.70  ? 24   GLU A C   1 
ATOM   180  O  O   . GLU A 1 24  ? 12.519  -2.137  30.330  1.00 17.83  ? 24   GLU A O   1 
ATOM   181  C  CB  . GLU A 1 24  ? 13.797  -0.858  32.877  1.00 20.50  ? 24   GLU A CB  1 
ATOM   182  C  CG  . GLU A 1 24  ? 13.547  -0.124  34.190  0.50 21.76  ? 24   GLU A CG  1 
ATOM   183  C  CD  . GLU A 1 24  ? 13.916  -0.950  35.402  0.50 24.01  ? 24   GLU A CD  1 
ATOM   184  O  OE1 . GLU A 1 24  ? 14.933  -1.679  35.359  0.50 23.13  ? 24   GLU A OE1 1 
ATOM   185  O  OE2 . GLU A 1 24  ? 13.176  -0.863  36.404  0.50 26.87  ? 24   GLU A OE2 1 
ATOM   186  N  N   . SER A 1 25  ? 14.253  -0.929  29.609  1.00 19.01  ? 25   SER A N   1 
ATOM   187  C  CA  . SER A 1 25  ? 14.446  -1.771  28.427  1.00 20.01  ? 25   SER A CA  1 
ATOM   188  C  C   . SER A 1 25  ? 14.741  -3.235  28.756  1.00 19.14  ? 25   SER A C   1 
ATOM   189  O  O   . SER A 1 25  ? 14.429  -4.102  27.972  1.00 18.97  ? 25   SER A O   1 
ATOM   190  C  CB  . SER A 1 25  ? 15.523  -1.208  27.498  1.00 21.35  ? 25   SER A CB  1 
ATOM   191  O  OG  . SER A 1 25  ? 16.802  -1.299  28.086  1.00 25.34  ? 25   SER A OG  1 
ATOM   192  N  N   . ASN A 1 26  ? 15.283  -3.520  29.936  1.00 17.34  ? 26   ASN A N   1 
ATOM   193  C  CA  . ASN A 1 26  ? 15.520  -4.894  30.363  1.00 16.65  ? 26   ASN A CA  1 
ATOM   194  C  C   . ASN A 1 26  ? 14.445  -5.414  31.298  1.00 15.75  ? 26   ASN A C   1 
ATOM   195  O  O   . ASN A 1 26  ? 14.617  -6.477  31.947  1.00 16.64  ? 26   ASN A O   1 
ATOM   196  C  CB  . ASN A 1 26  ? 16.911  -5.050  30.998  1.00 17.24  ? 26   ASN A CB  1 
ATOM   197  C  CG  . ASN A 1 26  ? 17.085  -4.290  32.288  1.00 17.00  ? 26   ASN A CG  1 
ATOM   198  O  OD1 . ASN A 1 26  ? 16.161  -3.669  32.832  1.00 18.90  ? 26   ASN A OD1 1 
ATOM   199  N  ND2 . ASN A 1 26  ? 18.328  -4.295  32.760  1.00 20.49  ? 26   ASN A ND2 1 
ATOM   200  N  N   . GLY A 1 27  ? 13.324  -4.706  31.345  1.00 14.36  ? 27   GLY A N   1 
ATOM   201  C  CA  . GLY A 1 27  ? 12.271  -5.061  32.283  1.00 13.97  ? 27   GLY A CA  1 
ATOM   202  C  C   . GLY A 1 27  ? 11.057  -5.629  31.569  1.00 11.90  ? 27   GLY A C   1 
ATOM   203  O  O   . GLY A 1 27  ? 10.986  -5.657  30.335  1.00 12.48  ? 27   GLY A O   1 
ATOM   204  N  N   . PRO A 1 28  ? 10.064  -6.035  32.349  1.00 11.96  ? 28   PRO A N   1 
ATOM   205  C  CA  . PRO A 1 28  ? 8.835   -6.567  31.795  1.00 11.17  ? 28   PRO A CA  1 
ATOM   206  C  C   . PRO A 1 28  ? 7.954   -5.518  31.162  1.00 10.62  ? 28   PRO A C   1 
ATOM   207  O  O   . PRO A 1 28  ? 8.090   -4.329  31.431  1.00 10.94  ? 28   PRO A O   1 
ATOM   208  C  CB  . PRO A 1 28  ? 8.143   -7.172  33.023  1.00 13.85  ? 28   PRO A CB  1 
ATOM   209  C  CG  . PRO A 1 28  ? 8.593   -6.329  34.120  1.00 15.57  ? 28   PRO A CG  1 
ATOM   210  C  CD  . PRO A 1 28  ? 10.008  -5.968  33.815  1.00 13.55  ? 28   PRO A CD  1 
ATOM   211  N  N   . VAL A 1 29  ? 7.086   -5.983  30.285  1.00 9.75   ? 29   VAL A N   1 
ATOM   212  C  CA  . VAL A 1 29  ? 6.104   -5.140  29.636  1.00 9.59   ? 29   VAL A CA  1 
ATOM   213  C  C   . VAL A 1 29  ? 4.753   -5.419  30.290  1.00 10.13  ? 29   VAL A C   1 
ATOM   214  O  O   . VAL A 1 29  ? 4.320   -6.572  30.342  1.00 11.00  ? 29   VAL A O   1 
ATOM   215  C  CB  . VAL A 1 29  ? 6.037   -5.412  28.131  1.00 9.58   ? 29   VAL A CB  1 
ATOM   216  C  CG1 . VAL A 1 29  ? 5.005   -4.508  27.423  1.00 10.77  ? 29   VAL A CG1 1 
ATOM   217  C  CG2 . VAL A 1 29  ? 7.422   -5.289  27.477  1.00 10.46  ? 29   VAL A CG2 1 
ATOM   218  N  N   . LYS A 1 30  ? 4.096   -4.369  30.762  1.00 9.99   ? 30   LYS A N   1 
ATOM   219  C  CA  . LYS A 1 30  ? 2.707   -4.482  31.197  1.00 11.26  ? 30   LYS A CA  1 
ATOM   220  C  C   . LYS A 1 30  ? 1.789   -4.298  29.987  1.00 9.80   ? 30   LYS A C   1 
ATOM   221  O  O   . LYS A 1 30  ? 2.019   -3.437  29.130  1.00 10.45  ? 30   LYS A O   1 
ATOM   222  C  CB  . LYS A 1 30  ? 2.369   -3.427  32.266  1.00 12.04  ? 30   LYS A CB  1 
ATOM   223  C  CG  . LYS A 1 30  ? 3.159   -3.601  33.556  1.00 17.22  ? 30   LYS A CG  1 
ATOM   224  C  CD  . LYS A 1 30  ? 2.526   -2.853  34.720  1.00 22.29  ? 30   LYS A CD  1 
ATOM   225  C  CE  . LYS A 1 30  ? 3.516   -2.572  35.846  1.00 25.79  ? 30   LYS A CE  1 
ATOM   226  N  NZ  . LYS A 1 30  ? 3.871   -1.121  35.899  0.50 26.59  ? 30   LYS A NZ  1 
ATOM   227  N  N   . VAL A 1 31  ? 0.758   -5.129  29.922  1.00 10.23  ? 31   VAL A N   1 
ATOM   228  C  CA  . VAL A 1 31  ? -0.178  -5.175  28.814  1.00 10.30  ? 31   VAL A CA  1 
ATOM   229  C  C   . VAL A 1 31  ? -1.582  -5.114  29.400  1.00 10.75  ? 31   VAL A C   1 
ATOM   230  O  O   . VAL A 1 31  ? -1.906  -5.938  30.223  1.00 12.62  ? 31   VAL A O   1 
ATOM   231  C  CB  . VAL A 1 31  ? 0.003   -6.450  27.983  1.00 11.30  ? 31   VAL A CB  1 
ATOM   232  C  CG1 . VAL A 1 31  ? -0.914  -6.457  26.763  1.00 12.93  ? 31   VAL A CG1 1 
ATOM   233  C  CG2 . VAL A 1 31  ? 1.486   -6.664  27.570  1.00 13.05  ? 31   VAL A CG2 1 
ATOM   234  N  N   . TRP A 1 32  ? -2.383  -4.137  29.006  1.00 10.31  ? 32   TRP A N   1 
ATOM   235  C  CA  . TRP A 1 32  ? -3.697  -4.021  29.574  1.00 11.13  ? 32   TRP A CA  1 
ATOM   236  C  C   . TRP A 1 32  ? -4.679  -3.398  28.596  1.00 10.11  ? 32   TRP A C   1 
ATOM   237  O  O   . TRP A 1 32  ? -4.333  -2.619  27.729  1.00 9.88   ? 32   TRP A O   1 
ATOM   238  C  CB  . TRP A 1 32  ? -3.682  -3.238  30.896  1.00 11.80  ? 32   TRP A CB  1 
ATOM   239  C  CG  . TRP A 1 32  ? -3.476  -1.776  30.749  1.00 12.12  ? 32   TRP A CG  1 
ATOM   240  C  CD1 . TRP A 1 32  ? -4.445  -0.815  30.701  1.00 13.11  ? 32   TRP A CD1 1 
ATOM   241  C  CD2 . TRP A 1 32  ? -2.239  -1.092  30.572  1.00 12.51  ? 32   TRP A CD2 1 
ATOM   242  N  NE1 . TRP A 1 32  ? -3.877  0.416   30.512  1.00 14.10  ? 32   TRP A NE1 1 
ATOM   243  C  CE2 . TRP A 1 32  ? -2.523  0.283   30.463  1.00 12.94  ? 32   TRP A CE2 1 
ATOM   244  C  CE3 . TRP A 1 32  ? -0.912  -1.504  30.527  1.00 14.77  ? 32   TRP A CE3 1 
ATOM   245  C  CZ2 . TRP A 1 32  ? -1.527  1.244   30.308  1.00 14.06  ? 32   TRP A CZ2 1 
ATOM   246  C  CZ3 . TRP A 1 32  ? 0.080   -0.557  30.364  1.00 15.62  ? 32   TRP A CZ3 1 
ATOM   247  C  CH2 . TRP A 1 32  ? -0.239  0.800   30.243  1.00 16.78  ? 32   TRP A CH2 1 
ATOM   248  N  N   . GLY A 1 33  ? -5.933  -3.745  28.776  1.00 9.91   ? 33   GLY A N   1 
ATOM   249  C  CA  . GLY A 1 33  ? -7.002  -3.165  27.998  1.00 10.38  ? 33   GLY A CA  1 
ATOM   250  C  C   . GLY A 1 33  ? -8.204  -4.040  28.005  1.00 11.68  ? 33   GLY A C   1 
ATOM   251  O  O   . GLY A 1 33  ? -8.406  -4.813  28.944  1.00 13.19  ? 33   GLY A O   1 
ATOM   252  N  N   A SER A 1 34  ? -9.008  -3.900  26.959  0.50 12.49  ? 34   SER A N   1 
ATOM   253  N  N   B SER A 1 34  ? -9.012  -3.936  26.967  0.50 12.72  ? 34   SER A N   1 
ATOM   254  C  CA  A SER A 1 34  ? -10.318 -4.544  26.871  0.50 13.46  ? 34   SER A CA  1 
ATOM   255  C  CA  B SER A 1 34  ? -10.239 -4.717  26.919  0.50 13.76  ? 34   SER A CA  1 
ATOM   256  C  C   A SER A 1 34  ? -10.545 -5.005  25.435  0.50 13.05  ? 34   SER A C   1 
ATOM   257  C  C   B SER A 1 34  ? -10.687 -4.942  25.487  0.50 13.40  ? 34   SER A C   1 
ATOM   258  O  O   A SER A 1 34  ? -10.049 -4.370  24.504  0.50 12.47  ? 34   SER A O   1 
ATOM   259  O  O   B SER A 1 34  ? -10.553 -4.065  24.629  0.50 13.18  ? 34   SER A O   1 
ATOM   260  C  CB  A SER A 1 34  ? -11.405 -3.548  27.306  0.50 14.00  ? 34   SER A CB  1 
ATOM   261  C  CB  B SER A 1 34  ? -11.351 -4.027  27.726  0.50 14.45  ? 34   SER A CB  1 
ATOM   262  O  OG  A SER A 1 34  ? -12.660 -4.177  27.467  0.50 17.14  ? 34   SER A OG  1 
ATOM   263  O  OG  B SER A 1 34  ? -11.794 -2.864  27.046  0.50 17.66  ? 34   SER A OG  1 
ATOM   264  N  N   . ILE A 1 35  ? -11.257 -6.121  25.268  1.00 12.30  ? 35   ILE A N   1 
ATOM   265  C  CA  . ILE A 1 35  ? -11.696 -6.591  23.970  1.00 11.65  ? 35   ILE A CA  1 
ATOM   266  C  C   . ILE A 1 35  ? -13.142 -7.007  24.145  1.00 11.51  ? 35   ILE A C   1 
ATOM   267  O  O   . ILE A 1 35  ? -13.478 -7.710  25.090  1.00 12.23  ? 35   ILE A O   1 
ATOM   268  C  CB  . ILE A 1 35  ? -10.869 -7.785  23.479  1.00 12.06  ? 35   ILE A CB  1 
ATOM   269  C  CG1 . ILE A 1 35  ? -9.383  -7.449  23.525  1.00 13.14  ? 35   ILE A CG1 1 
ATOM   270  C  CG2 . ILE A 1 35  ? -11.271 -8.185  22.075  1.00 11.86  ? 35   ILE A CG2 1 
ATOM   271  C  CD1 . ILE A 1 35  ? -8.483  -8.636  23.298  1.00 14.56  ? 35   ILE A CD1 1 
ATOM   272  N  N   . LYS A 1 36  ? -13.989 -6.534  23.254  1.00 11.31  ? 36   LYS A N   1 
ATOM   273  C  CA  . LYS A 1 36  ? -15.408 -6.803  23.311  1.00 11.97  ? 36   LYS A CA  1 
ATOM   274  C  C   . LYS A 1 36  ? -15.861 -7.530  22.050  1.00 11.32  ? 36   LYS A C   1 
ATOM   275  O  O   . LYS A 1 36  ? -15.143 -7.621  21.060  1.00 11.55  ? 36   LYS A O   1 
ATOM   276  C  CB  . LYS A 1 36  ? -16.208 -5.514  23.538  1.00 14.04  ? 36   LYS A CB  1 
ATOM   277  C  CG  . LYS A 1 36  ? -16.119 -4.508  22.456  1.00 17.05  ? 36   LYS A CG  1 
ATOM   278  C  CD  . LYS A 1 36  ? -16.907 -3.242  22.873  1.00 20.72  ? 36   LYS A CD  1 
ATOM   279  C  CE  . LYS A 1 36  ? -16.829 -2.150  21.818  1.00 22.78  ? 36   LYS A CE  1 
ATOM   280  N  NZ  . LYS A 1 36  ? -17.837 -1.091  22.143  1.00 25.32  ? 36   LYS A NZ  1 
ATOM   281  N  N   . GLY A 1 37  ? -17.094 -8.015  22.092  1.00 11.96  ? 37   GLY A N   1 
ATOM   282  C  CA  . GLY A 1 37  ? -17.715 -8.716  21.027  1.00 12.39  ? 37   GLY A CA  1 
ATOM   283  C  C   . GLY A 1 37  ? -17.275 -10.164 20.855  1.00 11.98  ? 37   GLY A C   1 
ATOM   284  O  O   . GLY A 1 37  ? -17.489 -10.763 19.801  1.00 13.14  ? 37   GLY A O   1 
ATOM   285  N  N   . LEU A 1 38  ? -16.682 -10.732 21.894  1.00 11.10  ? 38   LEU A N   1 
ATOM   286  C  CA  . LEU A 1 38  ? -16.140 -12.091 21.851  1.00 11.07  ? 38   LEU A CA  1 
ATOM   287  C  C   . LEU A 1 38  ? -17.163 -13.122 22.284  1.00 11.38  ? 38   LEU A C   1 
ATOM   288  O  O   . LEU A 1 38  ? -17.922 -12.892 23.198  1.00 12.94  ? 38   LEU A O   1 
ATOM   289  C  CB  . LEU A 1 38  ? -14.929 -12.197 22.776  1.00 11.28  ? 38   LEU A CB  1 
ATOM   290  C  CG  . LEU A 1 38  ? -13.670 -11.466 22.298  1.00 11.50  ? 38   LEU A CG  1 
ATOM   291  C  CD1 . LEU A 1 38  ? -12.672 -11.297 23.455  1.00 12.74  ? 38   LEU A CD1 1 
ATOM   292  C  CD2 . LEU A 1 38  ? -13.048 -12.196 21.116  1.00 11.58  ? 38   LEU A CD2 1 
ATOM   293  N  N   . THR A 1 39  ? -17.074 -14.306 21.710  1.00 10.32  ? 39   THR A N   1 
ATOM   294  C  CA  . THR A 1 39  ? -17.763 -15.470 22.274  1.00 10.72  ? 39   THR A CA  1 
ATOM   295  C  C   . THR A 1 39  ? -17.163 -15.840 23.651  1.00 10.36  ? 39   THR A C   1 
ATOM   296  O  O   . THR A 1 39  ? -15.979 -15.619 23.926  1.00 10.87  ? 39   THR A O   1 
ATOM   297  C  CB  . THR A 1 39  ? -17.731 -16.673 21.317  1.00 11.67  ? 39   THR A CB  1 
ATOM   298  O  OG1 . THR A 1 39  ? -16.370 -17.070 21.109  1.00 13.30  ? 39   THR A OG1 1 
ATOM   299  C  CG2 . THR A 1 39  ? -18.391 -16.376 20.012  1.00 13.90  ? 39   THR A CG2 1 
ATOM   300  N  N   . GLU A 1 40  ? -17.960 -16.455 24.494  1.00 10.23  ? 40   GLU A N   1 
ATOM   301  C  CA  . GLU A 1 40  ? -17.514 -16.810 25.842  1.00 10.64  ? 40   GLU A CA  1 
ATOM   302  C  C   . GLU A 1 40  ? -16.400 -17.860 25.772  1.00 10.68  ? 40   GLU A C   1 
ATOM   303  O  O   . GLU A 1 40  ? -16.481 -18.820 25.014  1.00 13.08  ? 40   GLU A O   1 
ATOM   304  C  CB  . GLU A 1 40  ? -18.688 -17.373 26.648  1.00 11.55  ? 40   GLU A CB  1 
ATOM   305  C  CG  . GLU A 1 40  ? -18.404 -17.645 28.078  1.00 12.96  ? 40   GLU A CG  1 
ATOM   306  C  CD  . GLU A 1 40  ? -19.544 -18.301 28.806  0.70 15.04  ? 40   GLU A CD  1 
ATOM   307  O  OE1 . GLU A 1 40  ? -20.431 -18.885 28.152  0.70 16.93  ? 40   GLU A OE1 1 
ATOM   308  O  OE2 . GLU A 1 40  ? -19.566 -18.205 30.051  0.70 14.86  ? 40   GLU A OE2 1 
ATOM   309  N  N   . GLY A 1 41  ? -15.364 -17.683 26.568  1.00 9.39   ? 41   GLY A N   1 
ATOM   310  C  CA  . GLY A 1 41  ? -14.271 -18.617 26.640  1.00 9.37   ? 41   GLY A CA  1 
ATOM   311  C  C   . GLY A 1 41  ? -12.946 -18.016 26.239  1.00 9.41   ? 41   GLY A C   1 
ATOM   312  O  O   . GLY A 1 41  ? -12.777 -16.782 26.227  1.00 9.64   ? 41   GLY A O   1 
ATOM   313  N  N   . LEU A 1 42  ? -11.998 -18.884 25.946  1.00 8.59   ? 42   LEU A N   1 
ATOM   314  C  CA  . LEU A 1 42  ? -10.637 -18.473 25.673  1.00 9.01   ? 42   LEU A CA  1 
ATOM   315  C  C   . LEU A 1 42  ? -10.458 -18.115 24.204  1.00 8.33   ? 42   LEU A C   1 
ATOM   316  O  O   . LEU A 1 42  ? -10.993 -18.777 23.336  1.00 9.57   ? 42   LEU A O   1 
ATOM   317  C  CB  . LEU A 1 42  ? -9.651  -19.612 25.995  1.00 8.73   ? 42   LEU A CB  1 
ATOM   318  C  CG  . LEU A 1 42  ? -9.255  -19.813 27.437  1.00 10.33  ? 42   LEU A CG  1 
ATOM   319  C  CD1 . LEU A 1 42  ? -10.389 -20.092 28.297  1.00 11.26  ? 42   LEU A CD1 1 
ATOM   320  C  CD2 . LEU A 1 42  ? -8.235  -20.948 27.547  1.00 11.72  ? 42   LEU A CD2 1 
ATOM   321  N  N   . HIS A 1 43  ? -9.614  -17.111 23.974  1.00 7.75   ? 43   HIS A N   1 
ATOM   322  C  CA  . HIS A 1 43  ? -9.252  -16.684 22.627  1.00 8.16   ? 43   HIS A CA  1 
ATOM   323  C  C   . HIS A 1 43  ? -7.760  -16.456 22.583  1.00 7.72   ? 43   HIS A C   1 
ATOM   324  O  O   . HIS A 1 43  ? -7.217  -15.643 23.362  1.00 8.63   ? 43   HIS A O   1 
ATOM   325  C  CB  . HIS A 1 43  ? -9.976  -15.390 22.315  1.00 8.08   ? 43   HIS A CB  1 
ATOM   326  C  CG  . HIS A 1 43  ? -11.453 -15.581 22.211  1.00 8.59   ? 43   HIS A CG  1 
ATOM   327  N  ND1 . HIS A 1 43  ? -12.058 -15.986 21.043  1.00 11.06  ? 43   HIS A ND1 1 
ATOM   328  C  CD2 . HIS A 1 43  ? -12.436 -15.522 23.149  1.00 10.36  ? 43   HIS A CD2 1 
ATOM   329  C  CE1 . HIS A 1 43  ? -13.360 -16.130 21.259  1.00 11.03  ? 43   HIS A CE1 1 
ATOM   330  N  NE2 . HIS A 1 43  ? -13.619 -15.868 22.526  1.00 10.70  ? 43   HIS A NE2 1 
ATOM   331  N  N   . GLY A 1 44  ? -7.096  -17.153 21.666  1.00 7.60   ? 44   GLY A N   1 
ATOM   332  C  CA  . GLY A 1 44  ? -5.646  -16.973 21.547  1.00 7.72   ? 44   GLY A CA  1 
ATOM   333  C  C   . GLY A 1 44  ? -5.266  -15.529 21.303  1.00 7.73   ? 44   GLY A C   1 
ATOM   334  O  O   . GLY A 1 44  ? -5.995  -14.829 20.617  1.00 8.32   ? 44   GLY A O   1 
ATOM   335  N  N   . PHE A 1 45  ? -4.108  -15.149 21.836  1.00 7.75   ? 45   PHE A N   1 
ATOM   336  C  CA  . PHE A 1 45  ? -3.697  -13.737 21.870  1.00 8.11   ? 45   PHE A CA  1 
ATOM   337  C  C   . PHE A 1 45  ? -2.208  -13.683 21.647  1.00 8.29   ? 45   PHE A C   1 
ATOM   338  O  O   . PHE A 1 45  ? -1.433  -14.103 22.506  1.00 9.16   ? 45   PHE A O   1 
ATOM   339  C  CB  . PHE A 1 45  ? -4.105  -13.195 23.226  1.00 8.89   ? 45   PHE A CB  1 
ATOM   340  C  CG  . PHE A 1 45  ? -3.917  -11.708 23.433  1.00 9.62   ? 45   PHE A CG  1 
ATOM   341  C  CD1 . PHE A 1 45  ? -4.602  -10.790 22.674  1.00 11.23  ? 45   PHE A CD1 1 
ATOM   342  C  CD2 . PHE A 1 45  ? -3.163  -11.234 24.500  1.00 10.80  ? 45   PHE A CD2 1 
ATOM   343  C  CE1 . PHE A 1 45  ? -4.471  -9.440  22.950  1.00 11.38  ? 45   PHE A CE1 1 
ATOM   344  C  CE2 . PHE A 1 45  ? -3.057  -9.903  24.752  1.00 11.69  ? 45   PHE A CE2 1 
ATOM   345  C  CZ  . PHE A 1 45  ? -3.698  -9.033  23.985  1.00 12.71  ? 45   PHE A CZ  1 
ATOM   346  N  N   . HIS A 1 46  ? -1.805  -13.235 20.437  1.00 8.01   ? 46   HIS A N   1 
ATOM   347  C  CA  . HIS A 1 46  ? -0.401  -13.297 20.022  1.00 8.25   ? 46   HIS A CA  1 
ATOM   348  C  C   . HIS A 1 46  ? 0.038   -12.072 19.267  1.00 7.33   ? 46   HIS A C   1 
ATOM   349  O  O   . HIS A 1 46  ? -0.756  -11.459 18.569  1.00 8.21   ? 46   HIS A O   1 
ATOM   350  C  CB  . HIS A 1 46  ? -0.079  -14.500 19.147  1.00 10.80  ? 46   HIS A CB  1 
ATOM   351  C  CG  . HIS A 1 46  ? -0.838  -15.725 19.503  1.00 9.71   ? 46   HIS A CG  1 
ATOM   352  N  ND1 . HIS A 1 46  ? -1.861  -16.185 18.720  1.00 11.92  ? 46   HIS A ND1 1 
ATOM   353  C  CD2 . HIS A 1 46  ? -0.724  -16.582 20.542  1.00 9.96   ? 46   HIS A CD2 1 
ATOM   354  C  CE1 . HIS A 1 46  ? -2.362  -17.266 19.273  1.00 12.26  ? 46   HIS A CE1 1 
ATOM   355  N  NE2 . HIS A 1 46  ? -1.696  -17.531 20.378  1.00 10.85  ? 46   HIS A NE2 1 
ATOM   356  N  N   . VAL A 1 47  ? 1.340   -11.814 19.348  1.00 7.53   ? 47   VAL A N   1 
ATOM   357  C  CA  . VAL A 1 47  ? 1.991   -10.930 18.426  1.00 6.92   ? 47   VAL A CA  1 
ATOM   358  C  C   . VAL A 1 47  ? 2.474   -11.756 17.235  1.00 7.17   ? 47   VAL A C   1 
ATOM   359  O  O   . VAL A 1 47  ? 3.222   -12.741 17.406  1.00 7.75   ? 47   VAL A O   1 
ATOM   360  C  CB  . VAL A 1 47  ? 3.171   -10.155 19.074  1.00 7.64   ? 47   VAL A CB  1 
ATOM   361  C  CG1 . VAL A 1 47  ? 3.811   -9.208  18.067  1.00 9.00   ? 47   VAL A CG1 1 
ATOM   362  C  CG2 . VAL A 1 47  ? 2.715   -9.399  20.314  1.00 9.17   ? 47   VAL A CG2 1 
ATOM   363  N  N   . HIS A 1 48  ? 2.055   -11.327 16.036  1.00 7.80   ? 48   HIS A N   1 
ATOM   364  C  CA  . HIS A 1 48  ? 2.459   -11.956 14.795  1.00 7.91   ? 48   HIS A CA  1 
ATOM   365  C  C   . HIS A 1 48  ? 3.564   -11.152 14.154  1.00 8.97   ? 48   HIS A C   1 
ATOM   366  O  O   . HIS A 1 48  ? 3.752   -9.982  14.475  1.00 11.59  ? 48   HIS A O   1 
ATOM   367  C  CB  . HIS A 1 48  ? 1.229   -12.120 13.865  1.00 8.41   ? 48   HIS A CB  1 
ATOM   368  C  CG  . HIS A 1 48  ? 0.251   -13.151 14.352  1.00 8.99   ? 48   HIS A CG  1 
ATOM   369  N  ND1 . HIS A 1 48  ? -0.075  -14.259 13.609  1.00 8.62   ? 48   HIS A ND1 1 
ATOM   370  C  CD2 . HIS A 1 48  ? -0.439  -13.268 15.513  1.00 10.13  ? 48   HIS A CD2 1 
ATOM   371  C  CE1 . HIS A 1 48  ? -0.977  -14.984 14.262  1.00 9.34   ? 48   HIS A CE1 1 
ATOM   372  N  NE2 . HIS A 1 48  ? -1.211  -14.408 15.425  1.00 9.37   ? 48   HIS A NE2 1 
ATOM   373  N  N   . GLU A 1 49  ? 4.287   -11.770 13.242  1.00 8.71   ? 49   GLU A N   1 
ATOM   374  C  CA  . GLU A 1 49  ? 5.532   -11.227 12.746  1.00 9.24   ? 49   GLU A CA  1 
ATOM   375  C  C   . GLU A 1 49  ? 5.412   -9.884  12.020  1.00 9.87   ? 49   GLU A C   1 
ATOM   376  O  O   . GLU A 1 49  ? 6.236   -9.001  12.220  1.00 10.45  ? 49   GLU A O   1 
ATOM   377  C  CB  . GLU A 1 49  ? 6.182   -12.250 11.816  1.00 11.63  ? 49   GLU A CB  1 
ATOM   378  C  CG  . GLU A 1 49  ? 7.586   -11.827 11.433  1.00 13.87  ? 49   GLU A CG  1 
ATOM   379  C  CD  . GLU A 1 49  ? 8.283   -12.789 10.485  1.00 17.54  ? 49   GLU A CD  1 
ATOM   380  O  OE1 . GLU A 1 49  ? 7.668   -13.821 10.075  1.00 19.54  ? 49   GLU A OE1 1 
ATOM   381  O  OE2 . GLU A 1 49  ? 9.458   -12.482 10.103  1.00 23.98  ? 49   GLU A OE2 1 
ATOM   382  N  N   . PHE A 1 50  ? 4.441   -9.761  11.125  1.00 8.59   ? 50   PHE A N   1 
ATOM   383  C  CA  . PHE A 1 50  ? 4.388   -8.605  10.247  1.00 8.55   ? 50   PHE A CA  1 
ATOM   384  C  C   . PHE A 1 50  ? 3.315   -7.641  10.699  1.00 8.54   ? 50   PHE A C   1 
ATOM   385  O  O   . PHE A 1 50  ? 2.214   -8.055  11.075  1.00 10.91  ? 50   PHE A O   1 
ATOM   386  C  CB  . PHE A 1 50  ? 4.123   -9.038  8.800   1.00 9.32   ? 50   PHE A CB  1 
ATOM   387  C  CG  . PHE A 1 50  ? 5.022   -10.106 8.332   1.00 10.92  ? 50   PHE A CG  1 
ATOM   388  C  CD1 . PHE A 1 50  ? 6.381   -9.913  8.312   1.00 13.54  ? 50   PHE A CD1 1 
ATOM   389  C  CD2 . PHE A 1 50  ? 4.506   -11.306 7.873   1.00 13.06  ? 50   PHE A CD2 1 
ATOM   390  C  CE1 . PHE A 1 50  ? 7.218   -10.946 7.889   1.00 15.58  ? 50   PHE A CE1 1 
ATOM   391  C  CE2 . PHE A 1 50  ? 5.337   -12.310 7.442   1.00 15.19  ? 50   PHE A CE2 1 
ATOM   392  C  CZ  . PHE A 1 50  ? 6.688   -12.139 7.462   1.00 14.57  ? 50   PHE A CZ  1 
ATOM   393  N  N   . GLY A 1 51  ? 3.606   -6.356  10.579  1.00 8.81   ? 51   GLY A N   1 
ATOM   394  C  CA  . GLY A 1 51  ? 2.625   -5.297  10.790  1.00 9.01   ? 51   GLY A CA  1 
ATOM   395  C  C   . GLY A 1 51  ? 1.924   -4.976  9.481   1.00 9.78   ? 51   GLY A C   1 
ATOM   396  O  O   . GLY A 1 51  ? 1.747   -3.830  9.121   1.00 11.87  ? 51   GLY A O   1 
ATOM   397  N  N   . ASP A 1 52  ? 1.509   -6.010  8.766   1.00 10.93  ? 52   ASP A N   1 
ATOM   398  C  CA  . ASP A 1 52  ? 0.921   -5.910  7.414   1.00 10.66  ? 52   ASP A CA  1 
ATOM   399  C  C   . ASP A 1 52  ? -0.520  -6.335  7.490   1.00 10.13  ? 52   ASP A C   1 
ATOM   400  O  O   . ASP A 1 52  ? -0.792  -7.504  7.795   1.00 11.97  ? 52   ASP A O   1 
ATOM   401  C  CB  . ASP A 1 52  ? 1.688   -6.786  6.437   1.00 11.47  ? 52   ASP A CB  1 
ATOM   402  C  CG  . ASP A 1 52  ? 1.274   -6.576  4.985   1.00 12.53  ? 52   ASP A CG  1 
ATOM   403  O  OD1 . ASP A 1 52  ? 0.200   -5.970  4.736   1.00 14.78  ? 52   ASP A OD1 1 
ATOM   404  O  OD2 . ASP A 1 52  ? 2.034   -7.030  4.106   1.00 15.77  ? 52   ASP A OD2 1 
ATOM   405  N  N   . ASN A 1 53  ? -1.433  -5.413  7.223   1.00 10.45  ? 53   ASN A N   1 
ATOM   406  C  CA  . ASN A 1 53  ? -2.863  -5.707  7.222   1.00 11.60  ? 53   ASN A CA  1 
ATOM   407  C  C   . ASN A 1 53  ? -3.463  -5.541  5.835   1.00 11.03  ? 53   ASN A C   1 
ATOM   408  O  O   . ASN A 1 53  ? -4.663  -5.392  5.698   1.00 12.24  ? 53   ASN A O   1 
ATOM   409  C  CB  . ASN A 1 53  ? -3.593  -4.776  8.194   1.00 13.43  ? 53   ASN A CB  1 
ATOM   410  C  CG  . ASN A 1 53  ? -5.015  -5.214  8.472   0.50 13.62  ? 53   ASN A CG  1 
ATOM   411  O  OD1 . ASN A 1 53  ? -5.246  -6.366  8.804   0.50 15.91  ? 53   ASN A OD1 1 
ATOM   412  N  ND2 . ASN A 1 53  ? -5.975  -4.287  8.353   0.50 17.87  ? 53   ASN A ND2 1 
ATOM   413  N  N   . THR A 1 54  ? -2.628  -5.630  4.812   1.00 12.38  ? 54   THR A N   1 
ATOM   414  C  CA  . THR A 1 54  ? -3.064  -5.394  3.455   1.00 13.71  ? 54   THR A CA  1 
ATOM   415  C  C   . THR A 1 54  ? -4.324  -6.132  3.092   1.00 14.49  ? 54   THR A C   1 
ATOM   416  O  O   . THR A 1 54  ? -5.312  -5.561  2.574   1.00 15.23  ? 54   THR A O   1 
ATOM   417  C  CB  . THR A 1 54  ? -1.963  -5.768  2.454   1.00 13.50  ? 54   THR A CB  1 
ATOM   418  O  OG1 . THR A 1 54  ? -0.836  -4.895  2.614   1.00 16.89  ? 54   THR A OG1 1 
ATOM   419  C  CG2 . THR A 1 54  ? -2.448  -5.618  0.994   1.00 15.92  ? 54   THR A CG2 1 
ATOM   420  N  N   . ALA A 1 55  ? -4.306  -7.426  3.360   1.00 14.02  ? 55   ALA A N   1 
ATOM   421  C  CA  . ALA A 1 55  ? -5.474  -8.279  3.064   1.00 15.25  ? 55   ALA A CA  1 
ATOM   422  C  C   . ALA A 1 55  ? -6.261  -8.718  4.288   1.00 15.71  ? 55   ALA A C   1 
ATOM   423  O  O   . ALA A 1 55  ? -6.935  -9.756  4.263   1.00 18.57  ? 55   ALA A O   1 
ATOM   424  C  CB  . ALA A 1 55  ? -5.058  -9.513  2.269   1.00 17.01  ? 55   ALA A CB  1 
ATOM   425  N  N   . GLY A 1 56  ? -6.190  -7.947  5.356   1.00 14.42  ? 56   GLY A N   1 
ATOM   426  C  CA  . GLY A 1 56  ? -6.715  -8.326  6.655   1.00 13.98  ? 56   GLY A CA  1 
ATOM   427  C  C   . GLY A 1 56  ? -5.670  -8.996  7.530   1.00 12.37  ? 56   GLY A C   1 
ATOM   428  O  O   . GLY A 1 56  ? -4.456  -8.913  7.260   1.00 13.19  ? 56   GLY A O   1 
ATOM   429  N  N   . CYS A 1 57  ? -6.153  -9.628  8.597   1.00 12.03  ? 57   CYS A N   1 
ATOM   430  C  CA  . CYS A 1 57  ? -5.266  -10.167 9.586   1.00 11.88  ? 57   CYS A CA  1 
ATOM   431  C  C   . CYS A 1 57  ? -4.371  -11.303 9.108   1.00 10.77  ? 57   CYS A C   1 
ATOM   432  O  O   . CYS A 1 57  ? -3.332  -11.541 9.725   1.00 11.14  ? 57   CYS A O   1 
ATOM   433  C  CB  . CYS A 1 57  ? -6.064  -10.637 10.808  1.00 13.29  ? 57   CYS A CB  1 
ATOM   434  S  SG  . CYS A 1 57  ? -7.067  -9.313  11.619  1.00 17.04  ? 57   CYS A SG  1 
ATOM   435  N  N   A THR A 1 58  ? -4.758  -11.969 8.020   0.50 10.99  ? 58   THR A N   1 
ATOM   436  N  N   B THR A 1 58  ? -4.722  -12.001 8.031   0.50 11.51  ? 58   THR A N   1 
ATOM   437  C  CA  A THR A 1 58  ? -3.952  -13.015 7.422   0.50 11.17  ? 58   THR A CA  1 
ATOM   438  C  CA  B THR A 1 58  ? -3.842  -13.058 7.560   0.50 12.07  ? 58   THR A CA  1 
ATOM   439  C  C   A THR A 1 58  ? -2.569  -12.522 7.020   0.50 10.20  ? 58   THR A C   1 
ATOM   440  C  C   B THR A 1 58  ? -2.504  -12.507 7.093   0.50 10.82  ? 58   THR A C   1 
ATOM   441  O  O   A THR A 1 58  ? -1.598  -13.263 7.101   0.50 10.90  ? 58   THR A O   1 
ATOM   442  O  O   B THR A 1 58  ? -1.487  -13.189 7.218   0.50 11.29  ? 58   THR A O   1 
ATOM   443  C  CB  A THR A 1 58  ? -4.678  -13.639 6.205   0.50 11.50  ? 58   THR A CB  1 
ATOM   444  C  CB  B THR A 1 58  ? -4.461  -13.887 6.448   0.50 12.85  ? 58   THR A CB  1 
ATOM   445  O  OG1 A THR A 1 58  ? -3.915  -14.749 5.668   0.50 12.74  ? 58   THR A OG1 1 
ATOM   446  O  OG1 B THR A 1 58  ? -4.478  -13.145 5.232   0.50 16.40  ? 58   THR A OG1 1 
ATOM   447  C  CG2 A THR A 1 58  ? -5.029  -12.579 5.116   0.50 12.85  ? 58   THR A CG2 1 
ATOM   448  C  CG2 B THR A 1 58  ? -5.864  -14.294 6.821   0.50 14.30  ? 58   THR A CG2 1 
ATOM   449  N  N   . SER A 1 59  ? -2.468  -11.250 6.629   1.00 9.97   ? 59   SER A N   1 
ATOM   450  C  CA  . SER A 1 59  ? -1.256  -10.682 6.121   1.00 11.38  ? 59   SER A CA  1 
ATOM   451  C  C   . SER A 1 59  ? -0.172  -10.565 7.214   1.00 10.09  ? 59   SER A C   1 
ATOM   452  O  O   . SER A 1 59  ? 1.012   -10.381 6.901   1.00 10.80  ? 59   SER A O   1 
ATOM   453  C  CB  . SER A 1 59  ? -1.522  -9.305  5.448   1.00 11.33  ? 59   SER A CB  1 
ATOM   454  O  OG  . SER A 1 59  ? -2.378  -9.420  4.303   1.00 13.55  ? 59   SER A OG  1 
ATOM   455  N  N   . ALA A 1 60  ? -0.553  -10.689 8.491   1.00 10.23  ? 60   ALA A N   1 
ATOM   456  C  CA  . ALA A 1 60  ? 0.365   -10.564 9.603   1.00 9.73   ? 60   ALA A CA  1 
ATOM   457  C  C   . ALA A 1 60  ? 1.328   -11.727 9.706   1.00 9.05   ? 60   ALA A C   1 
ATOM   458  O  O   . ALA A 1 60  ? 2.300   -11.660 10.462  1.00 9.66   ? 60   ALA A O   1 
ATOM   459  C  CB  . ALA A 1 60  ? -0.412  -10.384 10.888  1.00 10.31  ? 60   ALA A CB  1 
ATOM   460  N  N   . GLY A 1 61  ? 1.076   -12.830 9.007   1.00 8.73   ? 61   GLY A N   1 
ATOM   461  C  CA  . GLY A 1 61  ? 2.001   -13.956 9.037   1.00 9.15   ? 61   GLY A CA  1 
ATOM   462  C  C   . GLY A 1 61  ? 1.898   -14.753 10.327  1.00 9.03   ? 61   GLY A C   1 
ATOM   463  O  O   . GLY A 1 61  ? 0.893   -14.723 11.023  1.00 9.26   ? 61   GLY A O   1 
ATOM   464  N  N   . PRO A 1 62  ? 2.937   -15.554 10.600  1.00 9.56   ? 62   PRO A N   1 
ATOM   465  C  CA  . PRO A 1 62  ? 2.930   -16.449 11.751  1.00 9.34   ? 62   PRO A CA  1 
ATOM   466  C  C   . PRO A 1 62  ? 3.256   -15.705 13.057  1.00 9.28   ? 62   PRO A C   1 
ATOM   467  O  O   . PRO A 1 62  ? 3.500   -14.515 13.050  1.00 8.77   ? 62   PRO A O   1 
ATOM   468  C  CB  . PRO A 1 62  ? 4.043   -17.440 11.391  1.00 9.99   ? 62   PRO A CB  1 
ATOM   469  C  CG  . PRO A 1 62  ? 5.007   -16.599 10.662  1.00 10.96  ? 62   PRO A CG  1 
ATOM   470  C  CD  . PRO A 1 62  ? 4.225   -15.601 9.893   1.00 10.46  ? 62   PRO A CD  1 
ATOM   471  N  N   . HIS A 1 63  ? 3.228   -16.396 14.174  1.00 8.78   ? 63   HIS A N   1 
ATOM   472  C  CA  . HIS A 1 63  ? 3.609   -15.792 15.453  1.00 8.81   ? 63   HIS A CA  1 
ATOM   473  C  C   . HIS A 1 63  ? 5.041   -15.240 15.357  1.00 8.12   ? 63   HIS A C   1 
ATOM   474  O  O   . HIS A 1 63  ? 5.913   -15.841 14.728  1.00 8.85   ? 63   HIS A O   1 
ATOM   475  C  CB  . HIS A 1 63  ? 3.518   -16.778 16.610  1.00 8.82   ? 63   HIS A CB  1 
ATOM   476  C  CG  . HIS A 1 63  ? 2.163   -17.366 16.804  1.00 9.07   ? 63   HIS A CG  1 
ATOM   477  N  ND1 . HIS A 1 63  ? 1.899   -18.310 17.758  1.00 8.40   ? 63   HIS A ND1 1 
ATOM   478  C  CD2 . HIS A 1 63  ? 0.987   -17.105 16.199  1.00 10.18  ? 63   HIS A CD2 1 
ATOM   479  C  CE1 . HIS A 1 63  ? 0.619   -18.658 17.695  1.00 9.31   ? 63   HIS A CE1 1 
ATOM   480  N  NE2 . HIS A 1 63  ? 0.044   -17.948 16.745  1.00 11.26  ? 63   HIS A NE2 1 
ATOM   481  N  N   . PHE A 1 64  ? 5.278   -14.089 15.998  1.00 8.01   ? 64   PHE A N   1 
ATOM   482  C  CA  . PHE A 1 64  ? 6.610   -13.508 16.068  1.00 7.99   ? 64   PHE A CA  1 
ATOM   483  C  C   . PHE A 1 64  ? 7.548   -14.452 16.793  1.00 7.62   ? 64   PHE A C   1 
ATOM   484  O  O   . PHE A 1 64  ? 7.348   -14.775 17.954  1.00 7.95   ? 64   PHE A O   1 
ATOM   485  C  CB  . PHE A 1 64  ? 6.513   -12.112 16.708  1.00 8.62   ? 64   PHE A CB  1 
ATOM   486  C  CG  . PHE A 1 64  ? 7.833   -11.401 16.861  1.00 9.10   ? 64   PHE A CG  1 
ATOM   487  C  CD1 . PHE A 1 64  ? 8.728   -11.315 15.802  1.00 11.17  ? 64   PHE A CD1 1 
ATOM   488  C  CD2 . PHE A 1 64  ? 8.142   -10.756 18.031  1.00 10.35  ? 64   PHE A CD2 1 
ATOM   489  C  CE1 . PHE A 1 64  ? 9.934   -10.629 15.966  1.00 12.36  ? 64   PHE A CE1 1 
ATOM   490  C  CE2 . PHE A 1 64  ? 9.334   -10.063 18.158  1.00 10.36  ? 64   PHE A CE2 1 
ATOM   491  C  CZ  . PHE A 1 64  ? 10.211  -10.008 17.129  1.00 11.49  ? 64   PHE A CZ  1 
ATOM   492  N  N   . ASN A 1 65  ? 8.582   -14.875 16.098  1.00 8.72   ? 65   ASN A N   1 
ATOM   493  C  CA  . ASN A 1 65  ? 9.424   -15.966 16.553  1.00 9.86   ? 65   ASN A CA  1 
ATOM   494  C  C   . ASN A 1 65  ? 10.884  -15.772 16.172  1.00 10.67  ? 65   ASN A C   1 
ATOM   495  O  O   . ASN A 1 65  ? 11.463  -16.599 15.460  1.00 12.21  ? 65   ASN A O   1 
ATOM   496  C  CB  . ASN A 1 65  ? 8.887   -17.290 15.995  1.00 10.03  ? 65   ASN A CB  1 
ATOM   497  C  CG  . ASN A 1 65  ? 9.590   -18.513 16.531  1.00 11.20  ? 65   ASN A CG  1 
ATOM   498  O  OD1 . ASN A 1 65  ? 10.154  -18.492 17.632  1.00 11.17  ? 65   ASN A OD1 1 
ATOM   499  N  ND2 . ASN A 1 65  ? 9.489   -19.613 15.770  1.00 13.08  ? 65   ASN A ND2 1 
ATOM   500  N  N   . PRO A 1 66  ? 11.511  -14.698 16.651  1.00 10.93  ? 66   PRO A N   1 
ATOM   501  C  CA  . PRO A 1 66  ? 12.900  -14.443 16.234  1.00 11.72  ? 66   PRO A CA  1 
ATOM   502  C  C   . PRO A 1 66  ? 13.902  -15.506 16.703  1.00 12.70  ? 66   PRO A C   1 
ATOM   503  O  O   . PRO A 1 66  ? 14.977  -15.584 16.111  1.00 15.73  ? 66   PRO A O   1 
ATOM   504  C  CB  . PRO A 1 66  ? 13.202  -13.076 16.867  1.00 12.26  ? 66   PRO A CB  1 
ATOM   505  C  CG  . PRO A 1 66  ? 12.307  -13.012 18.021  1.00 10.99  ? 66   PRO A CG  1 
ATOM   506  C  CD  . PRO A 1 66  ? 11.036  -13.669 17.581  1.00 9.96   ? 66   PRO A CD  1 
ATOM   507  N  N   . LEU A 1 67  ? 13.587  -16.290 17.745  1.00 12.25  ? 67   LEU A N   1 
ATOM   508  C  CA  . LEU A 1 67  ? 14.511  -17.324 18.247  1.00 13.57  ? 67   LEU A CA  1 
ATOM   509  C  C   . LEU A 1 67  ? 14.242  -18.707 17.680  1.00 13.34  ? 67   LEU A C   1 
ATOM   510  O  O   . LEU A 1 67  ? 14.878  -19.676 18.056  1.00 14.36  ? 67   LEU A O   1 
ATOM   511  C  CB  . LEU A 1 67  ? 14.456  -17.391 19.780  1.00 15.25  ? 67   LEU A CB  1 
ATOM   512  C  CG  . LEU A 1 67  ? 15.012  -16.156 20.463  1.00 16.87  ? 67   LEU A CG  1 
ATOM   513  C  CD1 . LEU A 1 67  ? 14.744  -16.156 21.946  1.00 21.08  ? 67   LEU A CD1 1 
ATOM   514  C  CD2 . LEU A 1 67  ? 16.504  -16.120 20.206  1.00 20.17  ? 67   LEU A CD2 1 
ATOM   515  N  N   . SER A 1 68  ? 13.299  -18.827 16.759  1.00 12.85  ? 68   SER A N   1 
ATOM   516  C  CA  . SER A 1 68  ? 13.026  -20.117 16.080  1.00 13.95  ? 68   SER A CA  1 
ATOM   517  C  C   . SER A 1 68  ? 12.670  -21.223 17.083  1.00 13.93  ? 68   SER A C   1 
ATOM   518  O  O   . SER A 1 68  ? 13.197  -22.332 17.009  1.00 16.20  ? 68   SER A O   1 
ATOM   519  C  CB  . SER A 1 68  ? 14.179  -20.546 15.151  1.00 15.36  ? 68   SER A CB  1 
ATOM   520  O  OG  . SER A 1 68  ? 14.467  -19.523 14.217  1.00 17.85  ? 68   SER A OG  1 
ATOM   521  N  N   . ARG A 1 69  ? 11.781  -20.930 18.022  1.00 13.10  ? 69   ARG A N   1 
ATOM   522  C  CA  . ARG A 1 69  ? 11.311  -21.861 19.017  1.00 13.41  ? 69   ARG A CA  1 
ATOM   523  C  C   . ARG A 1 69  ? 9.974   -22.430 18.596  1.00 13.55  ? 69   ARG A C   1 
ATOM   524  O  O   . ARG A 1 69  ? 9.362   -21.965 17.638  1.00 13.58  ? 69   ARG A O   1 
ATOM   525  C  CB  . ARG A 1 69  ? 11.143  -21.172 20.364  1.00 14.16  ? 69   ARG A CB  1 
ATOM   526  C  CG  . ARG A 1 69  ? 12.400  -20.471 20.860  1.00 18.50  ? 69   ARG A CG  1 
ATOM   527  C  CD  . ARG A 1 69  ? 13.582  -21.397 21.087  1.00 24.57  ? 69   ARG A CD  1 
ATOM   528  N  NE  . ARG A 1 69  ? 13.753  -21.692 22.511  1.00 31.39  ? 69   ARG A NE  1 
ATOM   529  C  CZ  . ARG A 1 69  ? 14.171  -20.820 23.436  1.00 33.58  ? 69   ARG A CZ  1 
ATOM   530  N  NH1 . ARG A 1 69  ? 14.480  -19.557 23.120  0.50 35.13  ? 69   ARG A NH1 1 
ATOM   531  N  NH2 . ARG A 1 69  ? 14.268  -21.207 24.702  0.50 35.10  ? 69   ARG A NH2 1 
ATOM   532  N  N   . LYS A 1 70  ? 9.506   -23.417 19.357  1.00 12.84  ? 70   LYS A N   1 
ATOM   533  C  CA  . LYS A 1 70  ? 8.161   -23.936 19.234  1.00 13.33  ? 70   LYS A CA  1 
ATOM   534  C  C   . LYS A 1 70  ? 7.165   -23.076 19.999  1.00 11.82  ? 70   LYS A C   1 
ATOM   535  O  O   . LYS A 1 70  ? 7.524   -22.346 20.915  1.00 12.99  ? 70   LYS A O   1 
ATOM   536  C  CB  . LYS A 1 70  ? 8.105   -25.370 19.743  1.00 14.49  ? 70   LYS A CB  1 
ATOM   537  C  CG  . LYS A 1 70  ? 8.911   -26.319 18.861  1.00 18.51  ? 70   LYS A CG  1 
ATOM   538  C  CD  . LYS A 1 70  ? 8.852   -27.737 19.343  1.00 23.20  ? 70   LYS A CD  1 
ATOM   539  C  CE  . LYS A 1 70  ? 9.673   -27.953 20.608  0.20 22.00  ? 70   LYS A CE  1 
ATOM   540  N  NZ  . LYS A 1 70  ? 9.660   -29.383 21.025  0.20 22.76  ? 70   LYS A NZ  1 
ATOM   541  N  N   . HIS A 1 71  ? 5.899   -23.189 19.605  1.00 10.35  ? 71   HIS A N   1 
ATOM   542  C  CA  . HIS A 1 71  ? 4.854   -22.476 20.281  1.00 10.48  ? 71   HIS A CA  1 
ATOM   543  C  C   . HIS A 1 71  ? 4.647   -22.953 21.719  1.00 10.26  ? 71   HIS A C   1 
ATOM   544  O  O   . HIS A 1 71  ? 4.757   -24.162 22.010  1.00 11.47  ? 71   HIS A O   1 
ATOM   545  C  CB  . HIS A 1 71  ? 3.557   -22.663 19.498  1.00 9.87   ? 71   HIS A CB  1 
ATOM   546  C  CG  . HIS A 1 71  ? 2.382   -21.979 20.103  1.00 9.95   ? 71   HIS A CG  1 
ATOM   547  N  ND1 . HIS A 1 71  ? 2.181   -20.623 20.011  1.00 9.60   ? 71   HIS A ND1 1 
ATOM   548  C  CD2 . HIS A 1 71  ? 1.353   -22.471 20.828  1.00 10.28  ? 71   HIS A CD2 1 
ATOM   549  C  CE1 . HIS A 1 71  ? 1.081   -20.314 20.661  1.00 9.53   ? 71   HIS A CE1 1 
ATOM   550  N  NE2 . HIS A 1 71  ? 0.541   -21.416 21.149  1.00 9.68   ? 71   HIS A NE2 1 
ATOM   551  N  N   . GLY A 1 72  ? 4.385   -22.023 22.617  1.00 10.23  ? 72   GLY A N   1 
ATOM   552  C  CA  . GLY A 1 72  ? 4.062   -22.317 23.995  1.00 10.53  ? 72   GLY A CA  1 
ATOM   553  C  C   . GLY A 1 72  ? 3.167   -21.270 24.579  1.00 10.70  ? 72   GLY A C   1 
ATOM   554  O  O   . GLY A 1 72  ? 2.597   -20.442 23.875  1.00 11.53  ? 72   GLY A O   1 
ATOM   555  N  N   . GLY A 1 73  ? 3.029   -21.314 25.890  1.00 11.29  ? 73   GLY A N   1 
ATOM   556  C  CA  . GLY A 1 73  ? 2.337   -20.273 26.624  1.00 11.24  ? 73   GLY A CA  1 
ATOM   557  C  C   . GLY A 1 73  ? 3.303   -19.275 27.219  1.00 10.39  ? 73   GLY A C   1 
ATOM   558  O  O   . GLY A 1 73  ? 4.537   -19.481 27.227  1.00 11.08  ? 73   GLY A O   1 
ATOM   559  N  N   . PRO A 1 74  ? 2.754   -18.173 27.744  1.00 10.93  ? 74   PRO A N   1 
ATOM   560  C  CA  . PRO A 1 74  ? 3.616   -17.088 28.194  1.00 12.13  ? 74   PRO A CA  1 
ATOM   561  C  C   . PRO A 1 74  ? 4.510   -17.460 29.369  1.00 12.68  ? 74   PRO A C   1 
ATOM   562  O  O   . PRO A 1 74  ? 5.563   -16.877 29.514  1.00 15.08  ? 74   PRO A O   1 
ATOM   563  C  CB  . PRO A 1 74  ? 2.624   -15.971 28.541  1.00 13.02  ? 74   PRO A CB  1 
ATOM   564  C  CG  . PRO A 1 74  ? 1.306   -16.622 28.645  1.00 13.26  ? 74   PRO A CG  1 
ATOM   565  C  CD  . PRO A 1 74  ? 1.337   -17.777 27.750  1.00 10.69  ? 74   PRO A CD  1 
ATOM   566  N  N   . LYS A 1 75  ? 4.107   -18.432 30.181  1.00 12.30  ? 75   LYS A N   1 
ATOM   567  C  CA  . LYS A 1 75  ? 4.911   -18.877 31.327  1.00 13.64  ? 75   LYS A CA  1 
ATOM   568  C  C   . LYS A 1 75  ? 5.878   -19.986 30.992  1.00 12.97  ? 75   LYS A C   1 
ATOM   569  O  O   . LYS A 1 75  ? 6.512   -20.507 31.889  1.00 15.25  ? 75   LYS A O   1 
ATOM   570  C  CB  . LYS A 1 75  ? 4.030   -19.357 32.486  1.00 15.65  ? 75   LYS A CB  1 
ATOM   571  C  CG  . LYS A 1 75  ? 2.935   -18.373 32.921  1.00 19.81  ? 75   LYS A CG  1 
ATOM   572  C  CD  . LYS A 1 75  ? 2.219   -18.812 34.218  1.00 24.97  ? 75   LYS A CD  1 
ATOM   573  C  CE  . LYS A 1 75  ? 1.403   -20.071 34.015  1.00 28.39  ? 75   LYS A CE  1 
ATOM   574  N  NZ  . LYS A 1 75  ? 0.529   -20.358 35.185  1.00 30.80  ? 75   LYS A NZ  1 
ATOM   575  N  N   . ASP A 1 76  ? 5.997   -20.372 29.740  1.00 12.48  ? 76   ASP A N   1 
ATOM   576  C  CA  . ASP A 1 76  ? 6.922   -21.438 29.307  1.00 13.42  ? 76   ASP A CA  1 
ATOM   577  C  C   . ASP A 1 76  ? 8.236   -20.860 28.817  1.00 12.78  ? 76   ASP A C   1 
ATOM   578  O  O   . ASP A 1 76  ? 8.261   -19.768 28.237  1.00 13.75  ? 76   ASP A O   1 
ATOM   579  C  CB  . ASP A 1 76  ? 6.304   -22.229 28.171  1.00 13.99  ? 76   ASP A CB  1 
ATOM   580  C  CG  . ASP A 1 76  ? 5.052   -22.982 28.596  1.00 16.57  ? 76   ASP A CG  1 
ATOM   581  O  OD1 . ASP A 1 76  ? 4.904   -23.346 29.775  1.00 20.99  ? 76   ASP A OD1 1 
ATOM   582  O  OD2 . ASP A 1 76  ? 4.202   -23.196 27.721  1.00 18.12  ? 76   ASP A OD2 1 
ATOM   583  N  N   A GLU A 1 77  ? 9.334   -21.567 29.032  0.80 12.43  ? 77   GLU A N   1 
ATOM   584  N  N   B GLU A 1 77  ? 9.311   -21.610 29.041  0.20 12.51  ? 77   GLU A N   1 
ATOM   585  C  CA  A GLU A 1 77  ? 10.596  -21.177 28.424  0.80 13.25  ? 77   GLU A CA  1 
ATOM   586  C  CA  B GLU A 1 77  ? 10.620  -21.331 28.464  0.20 12.32  ? 77   GLU A CA  1 
ATOM   587  C  C   A GLU A 1 77  ? 10.550  -21.399 26.899  0.80 12.80  ? 77   GLU A C   1 
ATOM   588  C  C   B GLU A 1 77  ? 10.556  -21.433 26.941  0.20 12.16  ? 77   GLU A C   1 
ATOM   589  O  O   A GLU A 1 77  ? 11.032  -20.557 26.122  0.80 13.02  ? 77   GLU A O   1 
ATOM   590  O  O   B GLU A 1 77  ? 11.014  -20.542 26.220  0.20 12.29  ? 77   GLU A O   1 
ATOM   591  C  CB  A GLU A 1 77  ? 11.763  -21.959 29.011  0.80 14.19  ? 77   GLU A CB  1 
ATOM   592  C  CB  B GLU A 1 77  ? 11.635  -22.355 28.986  0.20 12.37  ? 77   GLU A CB  1 
ATOM   593  C  CG  A GLU A 1 77  ? 13.101  -21.458 28.493  0.80 17.03  ? 77   GLU A CG  1 
ATOM   594  C  CG  B GLU A 1 77  ? 13.081  -21.992 28.695  0.20 12.61  ? 77   GLU A CG  1 
ATOM   595  C  CD  A GLU A 1 77  ? 14.293  -22.123 29.196  0.80 20.25  ? 77   GLU A CD  1 
ATOM   596  C  CD  B GLU A 1 77  ? 13.507  -22.301 27.265  0.20 12.28  ? 77   GLU A CD  1 
ATOM   597  O  OE1 A GLU A 1 77  ? 14.238  -23.341 29.472  0.80 24.63  ? 77   GLU A OE1 1 
ATOM   598  O  OE1 B GLU A 1 77  ? 13.101  -23.359 26.732  0.20 12.59  ? 77   GLU A OE1 1 
ATOM   599  O  OE2 A GLU A 1 77  ? 15.278  -21.417 29.500  0.80 23.87  ? 77   GLU A OE2 1 
ATOM   600  O  OE2 B GLU A 1 77  ? 14.262  -21.491 26.674  0.20 12.81  ? 77   GLU A OE2 1 
ATOM   601  N  N   . GLU A 1 78  ? 9.983   -22.542 26.477  1.00 11.89  ? 78   GLU A N   1 
ATOM   602  C  CA  . GLU A 1 78  ? 9.817   -22.839 25.077  1.00 11.41  ? 78   GLU A CA  1 
ATOM   603  C  C   . GLU A 1 78  ? 8.525   -22.183 24.576  1.00 10.48  ? 78   GLU A C   1 
ATOM   604  O  O   . GLU A 1 78  ? 7.425   -22.696 24.734  1.00 12.45  ? 78   GLU A O   1 
ATOM   605  C  CB  . GLU A 1 78  ? 9.761   -24.353 24.861  1.00 12.11  ? 78   GLU A CB  1 
ATOM   606  C  CG  . GLU A 1 78  ? 9.796   -24.752 23.402  1.00 14.74  ? 78   GLU A CG  1 
ATOM   607  C  CD  . GLU A 1 78  ? 11.168  -24.586 22.712  1.00 19.85  ? 78   GLU A CD  1 
ATOM   608  O  OE1 . GLU A 1 78  ? 12.226  -24.511 23.399  0.70 22.38  ? 78   GLU A OE1 1 
ATOM   609  O  OE2 . GLU A 1 78  ? 11.185  -24.559 21.452  1.00 21.13  ? 78   GLU A OE2 1 
ATOM   610  N  N   . ARG A 1 79  ? 8.703   -21.057 23.923  1.00 9.69   ? 79   ARG A N   1 
ATOM   611  C  CA  . ARG A 1 79  ? 7.614   -20.262 23.373  1.00 9.54   ? 79   ARG A CA  1 
ATOM   612  C  C   . ARG A 1 79  ? 8.160   -19.406 22.269  1.00 9.22   ? 79   ARG A C   1 
ATOM   613  O  O   . ARG A 1 79  ? 9.340   -19.128 22.229  1.00 9.88   ? 79   ARG A O   1 
ATOM   614  C  CB  . ARG A 1 79  ? 6.963   -19.369 24.449  1.00 8.99   ? 79   ARG A CB  1 
ATOM   615  C  CG  . ARG A 1 79  ? 7.934   -18.414 25.116  1.00 9.22   ? 79   ARG A CG  1 
ATOM   616  C  CD  . ARG A 1 79  ? 7.284   -17.431 26.076  1.00 9.42   ? 79   ARG A CD  1 
ATOM   617  N  NE  . ARG A 1 79  ? 6.811   -16.258 25.352  1.00 9.21   ? 79   ARG A NE  1 
ATOM   618  C  CZ  . ARG A 1 79  ? 6.372   -15.169 25.963  1.00 9.41   ? 79   ARG A CZ  1 
ATOM   619  N  NH1 . ARG A 1 79  ? 6.261   -15.152 27.281  1.00 10.03  ? 79   ARG A NH1 1 
ATOM   620  N  NH2 . ARG A 1 79  ? 6.044   -14.088 25.280  1.00 9.42   ? 79   ARG A NH2 1 
ATOM   621  N  N   . HIS A 1 80  ? 7.260   -18.916 21.430  1.00 9.20   ? 80   HIS A N   1 
ATOM   622  C  CA  . HIS A 1 80  ? 7.560   -17.821 20.537  1.00 8.62   ? 80   HIS A CA  1 
ATOM   623  C  C   . HIS A 1 80  ? 7.570   -16.522 21.333  1.00 7.74   ? 80   HIS A C   1 
ATOM   624  O  O   . HIS A 1 80  ? 6.841   -16.365 22.307  1.00 8.25   ? 80   HIS A O   1 
ATOM   625  C  CB  . HIS A 1 80  ? 6.483   -17.706 19.473  1.00 8.57   ? 80   HIS A CB  1 
ATOM   626  C  CG  . HIS A 1 80  ? 6.296   -18.931 18.644  1.00 9.54   ? 80   HIS A CG  1 
ATOM   627  N  ND1 . HIS A 1 80  ? 5.049   -19.386 18.264  1.00 8.11   ? 80   HIS A ND1 1 
ATOM   628  C  CD2 . HIS A 1 80  ? 7.190   -19.813 18.145  1.00 10.90  ? 80   HIS A CD2 1 
ATOM   629  C  CE1 . HIS A 1 80  ? 5.196   -20.467 17.514  1.00 9.20   ? 80   HIS A CE1 1 
ATOM   630  N  NE2 . HIS A 1 80  ? 6.486   -20.750 17.432  1.00 11.80  ? 80   HIS A NE2 1 
ATOM   631  N  N   . VAL A 1 81  ? 8.355   -15.535 20.938  1.00 7.78   ? 81   VAL A N   1 
ATOM   632  C  CA  . VAL A 1 81  ? 8.321   -14.245 21.624  1.00 8.17   ? 81   VAL A CA  1 
ATOM   633  C  C   . VAL A 1 81  ? 6.883   -13.710 21.636  1.00 7.91   ? 81   VAL A C   1 
ATOM   634  O  O   . VAL A 1 81  ? 6.466   -13.142 22.633  1.00 9.22   ? 81   VAL A O   1 
ATOM   635  C  CB  . VAL A 1 81  ? 9.312   -13.194 20.992  1.00 8.78   ? 81   VAL A CB  1 
ATOM   636  C  CG1 . VAL A 1 81  ? 9.026   -11.788 21.513  1.00 9.59   ? 81   VAL A CG1 1 
ATOM   637  C  CG2 . VAL A 1 81  ? 10.747  -13.563 21.301  1.00 10.05  ? 81   VAL A CG2 1 
ATOM   638  N  N   . GLY A 1 82  ? 6.137   -13.900 20.531  1.00 8.00   ? 82   GLY A N   1 
ATOM   639  C  CA  . GLY A 1 82  ? 4.788   -13.368 20.460  1.00 8.52   ? 82   GLY A CA  1 
ATOM   640  C  C   . GLY A 1 82  ? 3.717   -14.100 21.238  1.00 7.84   ? 82   GLY A C   1 
ATOM   641  O  O   . GLY A 1 82  ? 2.539   -13.718 21.145  1.00 9.26   ? 82   GLY A O   1 
ATOM   642  N  N   . ASP A 1 83  ? 4.064   -15.149 21.965  1.00 8.42   ? 83   ASP A N   1 
ATOM   643  C  CA  . ASP A 1 83  ? 3.061   -16.007 22.627  1.00 8.68   ? 83   ASP A CA  1 
ATOM   644  C  C   . ASP A 1 83  ? 2.559   -15.418 23.959  1.00 8.67   ? 83   ASP A C   1 
ATOM   645  O  O   . ASP A 1 83  ? 3.155   -15.637 25.022  1.00 11.43  ? 83   ASP A O   1 
ATOM   646  C  CB  . ASP A 1 83  ? 3.652   -17.396 22.869  1.00 8.69   ? 83   ASP A CB  1 
ATOM   647  C  CG  . ASP A 1 83  ? 3.767   -18.186 21.616  1.00 8.63   ? 83   ASP A CG  1 
ATOM   648  O  OD1 . ASP A 1 83  ? 3.162   -17.788 20.566  1.00 8.00   ? 83   ASP A OD1 1 
ATOM   649  O  OD2 . ASP A 1 83  ? 4.480   -19.224 21.630  1.00 9.46   ? 83   ASP A OD2 1 
ATOM   650  N  N   . LEU A 1 84  ? 1.401   -14.738 23.897  1.00 8.51   ? 84   LEU A N   1 
ATOM   651  C  CA  . LEU A 1 84  ? 0.821   -14.119 25.072  1.00 8.67   ? 84   LEU A CA  1 
ATOM   652  C  C   . LEU A 1 84  ? -0.394  -14.882 25.622  1.00 9.64   ? 84   LEU A C   1 
ATOM   653  O  O   . LEU A 1 84  ? -1.148  -14.369 26.435  1.00 12.57  ? 84   LEU A O   1 
ATOM   654  C  CB  . LEU A 1 84  ? 0.456   -12.679 24.762  1.00 8.84   ? 84   LEU A CB  1 
ATOM   655  C  CG  . LEU A 1 84  ? 1.632   -11.749 24.435  1.00 10.00  ? 84   LEU A CG  1 
ATOM   656  C  CD1 . LEU A 1 84  ? 1.148   -10.348 24.087  1.00 12.28  ? 84   LEU A CD1 1 
ATOM   657  C  CD2 . LEU A 1 84  ? 2.646   -11.721 25.632  1.00 12.24  ? 84   LEU A CD2 1 
ATOM   658  N  N   . GLY A 1 85  ? -0.567  -16.112 25.164  1.00 9.13   ? 85   GLY A N   1 
ATOM   659  C  CA  . GLY A 1 85  ? -1.560  -16.991 25.753  1.00 9.55   ? 85   GLY A CA  1 
ATOM   660  C  C   . GLY A 1 85  ? -2.965  -16.783 25.231  1.00 9.04   ? 85   GLY A C   1 
ATOM   661  O  O   . GLY A 1 85  ? -3.198  -16.792 24.022  1.00 10.27  ? 85   GLY A O   1 
ATOM   662  N  N   . ASN A 1 86  ? -3.884  -16.634 26.166  1.00 9.71   ? 86   ASN A N   1 
ATOM   663  C  CA  . ASN A 1 86  ? -5.294  -16.433 25.892  1.00 9.53   ? 86   ASN A CA  1 
ATOM   664  C  C   . ASN A 1 86  ? -5.830  -15.238 26.617  1.00 9.96   ? 86   ASN A C   1 
ATOM   665  O  O   . ASN A 1 86  ? -5.381  -14.930 27.724  1.00 11.68  ? 86   ASN A O   1 
ATOM   666  C  CB  . ASN A 1 86  ? -6.126  -17.627 26.356  1.00 10.41  ? 86   ASN A CB  1 
ATOM   667  C  CG  . ASN A 1 86  ? -5.869  -18.878 25.541  1.00 10.16  ? 86   ASN A CG  1 
ATOM   668  O  OD1 . ASN A 1 86  ? -6.352  -18.982 24.431  1.00 11.06  ? 86   ASN A OD1 1 
ATOM   669  N  ND2 . ASN A 1 86  ? -5.065  -19.808 26.065  1.00 12.98  ? 86   ASN A ND2 1 
ATOM   670  N  N   . VAL A 1 87  ? -6.836  -14.601 26.026  1.00 9.67   ? 87   VAL A N   1 
ATOM   671  C  CA  . VAL A 1 87  ? -7.717  -13.708 26.776  1.00 10.28  ? 87   VAL A CA  1 
ATOM   672  C  C   . VAL A 1 87  ? -9.014  -14.482 26.980  1.00 9.70   ? 87   VAL A C   1 
ATOM   673  O  O   . VAL A 1 87  ? -9.327  -15.391 26.239  1.00 10.80  ? 87   VAL A O   1 
ATOM   674  C  CB  . VAL A 1 87  ? -7.918  -12.373 26.068  1.00 11.21  ? 87   VAL A CB  1 
ATOM   675  C  CG1 . VAL A 1 87  ? -6.560  -11.651 25.937  1.00 13.02  ? 87   VAL A CG1 1 
ATOM   676  C  CG2 . VAL A 1 87  ? -8.630  -12.550 24.725  1.00 12.58  ? 87   VAL A CG2 1 
ATOM   677  N  N   . THR A 1 88  ? -9.704  -14.203 28.054  1.00 10.67  ? 88   THR A N   1 
ATOM   678  C  CA  . THR A 1 88  ? -10.920 -14.941 28.369  1.00 10.78  ? 88   THR A CA  1 
ATOM   679  C  C   . THR A 1 88  ? -12.115 -14.010 28.477  1.00 10.37  ? 88   THR A C   1 
ATOM   680  O  O   . THR A 1 88  ? -12.109 -13.087 29.274  1.00 12.39  ? 88   THR A O   1 
ATOM   681  C  CB  . THR A 1 88  ? -10.761 -15.743 29.702  1.00 11.58  ? 88   THR A CB  1 
ATOM   682  O  OG1 . THR A 1 88  ? -9.667  -16.661 29.571  1.00 14.07  ? 88   THR A OG1 1 
ATOM   683  C  CG2 . THR A 1 88  ? -12.048 -16.532 30.066  1.00 12.18  ? 88   THR A CG2 1 
ATOM   684  N  N   . ALA A 1 89  ? -13.146 -14.298 27.691  1.00 10.67  ? 89   ALA A N   1 
ATOM   685  C  CA  . ALA A 1 89  ? -14.346 -13.515 27.647  1.00 10.41  ? 89   ALA A CA  1 
ATOM   686  C  C   . ALA A 1 89  ? -15.473 -14.190 28.422  1.00 10.63  ? 89   ALA A C   1 
ATOM   687  O  O   . ALA A 1 89  ? -15.600 -15.405 28.457  1.00 9.87   ? 89   ALA A O   1 
ATOM   688  C  CB  . ALA A 1 89  ? -14.787 -13.315 26.204  1.00 11.31  ? 89   ALA A CB  1 
ATOM   689  N  N   . ASP A 1 90  ? -16.297 -13.356 29.031  1.00 12.04  ? 90   ASP A N   1 
ATOM   690  C  CA  . ASP A 1 90  ? -17.474 -13.794 29.769  1.00 12.87  ? 90   ASP A CA  1 
ATOM   691  C  C   . ASP A 1 90  ? -18.694 -13.761 28.846  1.00 11.40  ? 90   ASP A C   1 
ATOM   692  O  O   . ASP A 1 90  ? -18.571 -13.483 27.649  1.00 11.55  ? 90   ASP A O   1 
ATOM   693  C  CB  . ASP A 1 90  ? -17.726 -12.844 30.978  1.00 13.95  ? 90   ASP A CB  1 
ATOM   694  C  CG  . ASP A 1 90  ? -16.750 -13.014 32.137  1.00 18.54  ? 90   ASP A CG  1 
ATOM   695  O  OD1 . ASP A 1 90  ? -16.064 -14.033 32.216  1.00 26.08  ? 90   ASP A OD1 1 
ATOM   696  O  OD2 . ASP A 1 90  ? -16.688 -12.093 33.003  1.00 23.84  ? 90   ASP A OD2 1 
ATOM   697  N  N   A LYS A 1 91  ? -19.881 -14.010 29.399  0.50 11.58  ? 91   LYS A N   1 
ATOM   698  N  N   B LYS A 1 91  ? -19.849 -14.034 29.447  0.50 12.30  ? 91   LYS A N   1 
ATOM   699  C  CA  A LYS A 1 91  ? -21.132 -13.882 28.647  0.50 11.28  ? 91   LYS A CA  1 
ATOM   700  C  CA  B LYS A 1 91  ? -21.142 -13.890 28.818  0.50 12.34  ? 91   LYS A CA  1 
ATOM   701  C  C   A LYS A 1 91  ? -21.569 -12.415 28.405  0.50 11.48  ? 91   LYS A C   1 
ATOM   702  C  C   B LYS A 1 91  ? -21.396 -12.484 28.241  0.50 12.88  ? 91   LYS A C   1 
ATOM   703  O  O   A LYS A 1 91  ? -22.659 -12.164 27.904  0.50 10.84  ? 91   LYS A O   1 
ATOM   704  O  O   B LYS A 1 91  ? -22.118 -12.372 27.248  0.50 14.17  ? 91   LYS A O   1 
ATOM   705  C  CB  A LYS A 1 91  ? -22.281 -14.575 29.388  0.50 11.85  ? 91   LYS A CB  1 
ATOM   706  C  CB  B LYS A 1 91  ? -22.241 -14.279 29.824  0.50 12.97  ? 91   LYS A CB  1 
ATOM   707  C  CG  A LYS A 1 91  ? -22.334 -16.101 29.400  0.50 13.34  ? 91   LYS A CG  1 
ATOM   708  C  CG  B LYS A 1 91  ? -22.431 -15.794 30.022  0.50 13.45  ? 91   LYS A CG  1 
ATOM   709  C  CD  A LYS A 1 91  ? -23.025 -16.664 28.172  0.50 14.15  ? 91   LYS A CD  1 
ATOM   710  C  CD  B LYS A 1 91  ? -22.705 -16.473 28.699  0.50 16.56  ? 91   LYS A CD  1 
ATOM   711  C  CE  A LYS A 1 91  ? -23.765 -17.939 28.507  0.50 14.80  ? 91   LYS A CE  1 
ATOM   712  C  CE  B LYS A 1 91  ? -23.338 -17.849 28.847  0.50 19.72  ? 91   LYS A CE  1 
ATOM   713  N  NZ  A LYS A 1 91  ? -22.918 -18.840 29.321  0.50 13.90  ? 91   LYS A NZ  1 
ATOM   714  N  NZ  B LYS A 1 91  ? -23.684 -18.381 27.500  0.50 22.73  ? 91   LYS A NZ  1 
ATOM   715  N  N   . ASP A 1 92  ? -20.747 -11.464 28.825  1.00 12.35  ? 92   ASP A N   1 
ATOM   716  C  CA  . ASP A 1 92  ? -20.877 -10.075 28.410  1.00 12.90  ? 92   ASP A CA  1 
ATOM   717  C  C   . ASP A 1 92  ? -20.068 -9.805  27.132  1.00 12.45  ? 92   ASP A C   1 
ATOM   718  O  O   . ASP A 1 92  ? -20.147 -8.695  26.598  1.00 13.95  ? 92   ASP A O   1 
ATOM   719  C  CB  . ASP A 1 92  ? -20.466 -9.104  29.537  1.00 14.05  ? 92   ASP A CB  1 
ATOM   720  C  CG  . ASP A 1 92  ? -19.033 -9.331  30.053  1.00 15.92  ? 92   ASP A CG  1 
ATOM   721  O  OD1 . ASP A 1 92  ? -18.280 -10.194 29.507  1.00 17.42  ? 92   ASP A OD1 1 
ATOM   722  O  OD2 . ASP A 1 92  ? -18.652 -8.632  31.035  1.00 18.81  ? 92   ASP A OD2 1 
ATOM   723  N  N   . GLY A 1 93  ? -19.311 -10.798 26.635  1.00 11.72  ? 93   GLY A N   1 
ATOM   724  C  CA  . GLY A 1 93  ? -18.509 -10.671 25.445  1.00 11.67  ? 93   GLY A CA  1 
ATOM   725  C  C   . GLY A 1 93  ? -17.194 -9.938  25.647  1.00 10.67  ? 93   GLY A C   1 
ATOM   726  O  O   . GLY A 1 93  ? -16.489 -9.670  24.664  1.00 11.59  ? 93   GLY A O   1 
ATOM   727  N  N   . VAL A 1 94  ? -16.867 -9.623  26.896  1.00 11.18  ? 94   VAL A N   1 
ATOM   728  C  CA  . VAL A 1 94  ? -15.709 -8.828  27.188  1.00 11.03  ? 94   VAL A CA  1 
ATOM   729  C  C   . VAL A 1 94  ? -14.627 -9.643  27.843  1.00 11.61  ? 94   VAL A C   1 
ATOM   730  O  O   . VAL A 1 94  ? -14.882 -10.372 28.792  1.00 11.89  ? 94   VAL A O   1 
ATOM   731  C  CB  . VAL A 1 94  ? -16.084 -7.646  28.115  1.00 12.08  ? 94   VAL A CB  1 
ATOM   732  C  CG1 . VAL A 1 94  ? -14.862 -6.800  28.476  1.00 14.02  ? 94   VAL A CG1 1 
ATOM   733  C  CG2 . VAL A 1 94  ? -17.151 -6.773  27.439  1.00 13.83  ? 94   VAL A CG2 1 
ATOM   734  N  N   . ALA A 1 95  ? -13.410 -9.449  27.348  1.00 11.06  ? 95   ALA A N   1 
ATOM   735  C  CA  . ALA A 1 95  ? -12.197 -9.929  27.988  1.00 12.51  ? 95   ALA A CA  1 
ATOM   736  C  C   . ALA A 1 95  ? -11.463 -8.714  28.530  1.00 12.92  ? 95   ALA A C   1 
ATOM   737  O  O   . ALA A 1 95  ? -11.069 -7.820  27.769  1.00 13.88  ? 95   ALA A O   1 
ATOM   738  C  CB  . ALA A 1 95  ? -11.322 -10.689 26.996  1.00 13.10  ? 95   ALA A CB  1 
ATOM   739  N  N   . ASP A 1 96  ? -11.258 -8.695  29.835  1.00 14.65  ? 96   ASP A N   1 
ATOM   740  C  CA  . ASP A 1 96  ? -10.387 -7.715  30.468  1.00 15.95  ? 96   ASP A CA  1 
ATOM   741  C  C   . ASP A 1 96  ? -8.970  -8.267  30.414  1.00 16.33  ? 96   ASP A C   1 
ATOM   742  O  O   . ASP A 1 96  ? -8.690  -9.413  30.793  1.00 19.45  ? 96   ASP A O   1 
ATOM   743  C  CB  . ASP A 1 96  ? -10.789 -7.491  31.917  1.00 17.91  ? 96   ASP A CB  1 
ATOM   744  C  CG  . ASP A 1 96  ? -12.080 -6.712  32.066  0.70 20.40  ? 96   ASP A CG  1 
ATOM   745  O  OD1 . ASP A 1 96  ? -12.463 -5.921  31.171  0.70 25.53  ? 96   ASP A OD1 1 
ATOM   746  O  OD2 . ASP A 1 96  ? -12.736 -6.884  33.121  0.70 24.95  ? 96   ASP A OD2 1 
ATOM   747  N  N   . VAL A 1 97  ? -8.048  -7.455  29.935  1.00 15.18  ? 97   VAL A N   1 
ATOM   748  C  CA  . VAL A 1 97  ? -6.679  -7.898  29.807  1.00 14.90  ? 97   VAL A CA  1 
ATOM   749  C  C   . VAL A 1 97  ? -5.834  -7.159  30.809  1.00 14.74  ? 97   VAL A C   1 
ATOM   750  O  O   . VAL A 1 97  ? -5.870  -5.946  30.868  1.00 14.09  ? 97   VAL A O   1 
ATOM   751  C  CB  . VAL A 1 97  ? -6.175  -7.655  28.369  1.00 14.87  ? 97   VAL A CB  1 
ATOM   752  C  CG1 . VAL A 1 97  ? -4.695  -8.025  28.245  1.00 16.61  ? 97   VAL A CG1 1 
ATOM   753  C  CG2 . VAL A 1 97  ? -7.055  -8.424  27.384  1.00 18.87  ? 97   VAL A CG2 1 
ATOM   754  N  N   . SER A 1 98  ? -5.079  -7.888  31.622  1.00 15.57  ? 98   SER A N   1 
ATOM   755  C  CA  . SER A 1 98  ? -4.094  -7.258  32.479  1.00 17.56  ? 98   SER A CA  1 
ATOM   756  C  C   . SER A 1 98  ? -3.024  -8.254  32.784  1.00 17.70  ? 98   SER A C   1 
ATOM   757  O  O   . SER A 1 98  ? -3.164  -9.051  33.726  1.00 20.48  ? 98   SER A O   1 
ATOM   758  C  CB  . SER A 1 98  ? -4.697  -6.749  33.798  1.00 18.50  ? 98   SER A CB  1 
ATOM   759  O  OG  . SER A 1 98  ? -3.714  -5.967  34.481  1.00 23.66  ? 98   SER A OG  1 
ATOM   760  N  N   . THR A 1 99  ? -1.940  -8.181  32.033  1.00 15.86  ? 99   THR A N   1 
ATOM   761  C  CA  . THR A 1 99  ? -0.838  -9.069  32.224  1.00 16.42  ? 99   THR A CA  1 
ATOM   762  C  C   . THR A 1 99  ? 0.500   -8.389  32.171  1.00 14.04  ? 99   THR A C   1 
ATOM   763  O  O   . THR A 1 99  ? 0.633   -7.213  31.842  1.00 14.80  ? 99   THR A O   1 
ATOM   764  C  CB  . THR A 1 99  ? -0.860  -10.168 31.237  1.00 16.73  ? 99   THR A CB  1 
ATOM   765  O  OG1 . THR A 1 99  ? -0.653  -9.668  29.912  1.00 19.54  ? 99   THR A OG1 1 
ATOM   766  C  CG2 . THR A 1 99  ? -2.219  -10.946 31.310  1.00 19.35  ? 99   THR A CG2 1 
ATOM   767  N  N   . GLU A 1 100 ? 1.501   -9.149  32.565  1.00 13.24  ? 100  GLU A N   1 
ATOM   768  C  CA  . GLU A 1 100 ? 2.852   -8.693  32.537  1.00 12.99  ? 100  GLU A CA  1 
ATOM   769  C  C   . GLU A 1 100 ? 3.661   -9.784  31.875  1.00 11.80  ? 100  GLU A C   1 
ATOM   770  O  O   . GLU A 1 100 ? 3.479   -10.954 32.184  1.00 13.84  ? 100  GLU A O   1 
ATOM   771  C  CB  . GLU A 1 100 ? 3.306   -8.445  33.962  1.00 15.44  ? 100  GLU A CB  1 
ATOM   772  C  CG  . GLU A 1 100 ? 4.578   -7.742  34.054  1.00 20.33  ? 100  GLU A CG  1 
ATOM   773  C  CD  . GLU A 1 100 ? 4.857   -7.223  35.442  1.00 26.50  ? 100  GLU A CD  1 
ATOM   774  O  OE1 . GLU A 1 100 ? 4.444   -7.883  36.417  1.00 31.64  ? 100  GLU A OE1 1 
ATOM   775  O  OE2 . GLU A 1 100 ? 5.501   -6.166  35.537  1.00 31.34  ? 100  GLU A OE2 1 
ATOM   776  N  N   . ASP A 1 101 ? 4.492   -9.409  30.919  1.00 9.97   ? 101  ASP A N   1 
ATOM   777  C  CA  . ASP A 1 101 ? 5.288   -10.364 30.189  1.00 10.15  ? 101  ASP A CA  1 
ATOM   778  C  C   . ASP A 1 101 ? 6.737   -9.942  30.142  1.00 9.84   ? 101  ASP A C   1 
ATOM   779  O  O   . ASP A 1 101 ? 7.059   -8.783  29.951  1.00 11.02  ? 101  ASP A O   1 
ATOM   780  C  CB  . ASP A 1 101 ? 4.739   -10.573 28.766  1.00 10.39  ? 101  ASP A CB  1 
ATOM   781  C  CG  . ASP A 1 101 ? 5.313   -11.831 28.111  1.00 11.56  ? 101  ASP A CG  1 
ATOM   782  O  OD1 . ASP A 1 101 ? 4.909   -12.948 28.542  1.00 12.80  ? 101  ASP A OD1 1 
ATOM   783  O  OD2 . ASP A 1 101 ? 6.240   -11.693 27.251  1.00 10.78  ? 101  ASP A OD2 1 
ATOM   784  N  N   A SER A 1 102 ? 7.602   -10.949 30.276  0.60 9.54   ? 102  SER A N   1 
ATOM   785  N  N   B SER A 1 102 ? 7.631   -10.912 30.323  0.40 10.25  ? 102  SER A N   1 
ATOM   786  C  CA  A SER A 1 102 ? 9.039   -10.761 30.414  0.60 9.84   ? 102  SER A CA  1 
ATOM   787  C  CA  B SER A 1 102 ? 9.060   -10.625 30.366  0.40 10.77  ? 102  SER A CA  1 
ATOM   788  C  C   A SER A 1 102 ? 9.819   -11.042 29.132  0.60 9.77   ? 102  SER A C   1 
ATOM   789  C  C   B SER A 1 102 ? 9.834   -11.145 29.168  0.40 10.10  ? 102  SER A C   1 
ATOM   790  O  O   A SER A 1 102 ? 11.013  -10.795 29.079  0.60 10.68  ? 102  SER A O   1 
ATOM   791  O  O   B SER A 1 102 ? 11.048  -11.217 29.228  0.40 10.22  ? 102  SER A O   1 
ATOM   792  C  CB  A SER A 1 102 ? 9.574   -11.664 31.537  0.60 10.26  ? 102  SER A CB  1 
ATOM   793  C  CB  B SER A 1 102 ? 9.688   -11.204 31.626  0.40 11.70  ? 102  SER A CB  1 
ATOM   794  O  OG  A SER A 1 102 ? 9.050   -11.223 32.771  0.60 12.45  ? 102  SER A OG  1 
ATOM   795  O  OG  B SER A 1 102 ? 9.442   -12.580 31.719  0.40 15.53  ? 102  SER A OG  1 
ATOM   796  N  N   . VAL A 1 103 ? 9.146   -11.526 28.102  1.00 9.30   ? 103  VAL A N   1 
ATOM   797  C  CA  . VAL A 1 103 ? 9.799   -11.927 26.869  1.00 9.37   ? 103  VAL A CA  1 
ATOM   798  C  C   . VAL A 1 103 ? 9.611   -10.937 25.724  1.00 9.15   ? 103  VAL A C   1 
ATOM   799  O  O   . VAL A 1 103 ? 10.551  -10.623 25.002  1.00 10.16  ? 103  VAL A O   1 
ATOM   800  C  CB  . VAL A 1 103 ? 9.374   -13.372 26.461  1.00 9.28   ? 103  VAL A CB  1 
ATOM   801  C  CG1 . VAL A 1 103 ? 9.962   -13.802 25.132  1.00 11.20  ? 103  VAL A CG1 1 
ATOM   802  C  CG2 . VAL A 1 103 ? 9.781   -14.368 27.572  1.00 9.40   ? 103  VAL A CG2 1 
ATOM   803  N  N   . ILE A 1 104 ? 8.390   -10.420 25.559  1.00 9.05   ? 104  ILE A N   1 
ATOM   804  C  CA  . ILE A 1 104 ? 8.168   -9.295  24.636  1.00 8.26   ? 104  ILE A CA  1 
ATOM   805  C  C   . ILE A 1 104 ? 8.978   -8.077  25.109  1.00 8.60   ? 104  ILE A C   1 
ATOM   806  O  O   . ILE A 1 104 ? 9.311   -7.963  26.291  1.00 9.53   ? 104  ILE A O   1 
ATOM   807  C  CB  . ILE A 1 104 ? 6.673   -8.977  24.458  1.00 8.32   ? 104  ILE A CB  1 
ATOM   808  C  CG1 . ILE A 1 104 ? 6.026   -8.546  25.761  1.00 8.85   ? 104  ILE A CG1 1 
ATOM   809  C  CG2 . ILE A 1 104 ? 5.926   -10.121 23.756  1.00 9.60   ? 104  ILE A CG2 1 
ATOM   810  C  CD1 . ILE A 1 104 ? 4.669   -7.929  25.555  1.00 9.98   ? 104  ILE A CD1 1 
ATOM   811  N  N   . SER A 1 105 ? 9.202   -7.136  24.204  1.00 9.10   ? 105  SER A N   1 
ATOM   812  C  CA  . SER A 1 105 ? 9.848   -5.862  24.539  1.00 8.26   ? 105  SER A CA  1 
ATOM   813  C  C   . SER A 1 105 ? 9.303   -4.782  23.622  1.00 8.51   ? 105  SER A C   1 
ATOM   814  O  O   . SER A 1 105 ? 8.711   -5.058  22.564  1.00 9.26   ? 105  SER A O   1 
ATOM   815  C  CB  . SER A 1 105 ? 11.353  -5.982  24.414  1.00 9.50   ? 105  SER A CB  1 
ATOM   816  O  OG  . SER A 1 105 ? 11.965  -4.872  25.017  1.00 11.27  ? 105  SER A OG  1 
ATOM   817  N  N   . LEU A 1 106 ? 9.529   -3.548  24.033  1.00 9.29   ? 106  LEU A N   1 
ATOM   818  C  CA  . LEU A 1 106 ? 9.227   -2.363  23.210  1.00 9.98   ? 106  LEU A CA  1 
ATOM   819  C  C   . LEU A 1 106 ? 10.491  -1.714  22.655  1.00 11.10  ? 106  LEU A C   1 
ATOM   820  O  O   . LEU A 1 106 ? 10.451  -0.619  22.119  1.00 12.30  ? 106  LEU A O   1 
ATOM   821  C  CB  . LEU A 1 106 ? 8.372   -1.370  23.992  1.00 10.38  ? 106  LEU A CB  1 
ATOM   822  C  CG  . LEU A 1 106 ? 7.065   -1.906  24.591  1.00 10.01  ? 106  LEU A CG  1 
ATOM   823  C  CD1 . LEU A 1 106 ? 6.314   -0.769  25.311  1.00 10.61  ? 106  LEU A CD1 1 
ATOM   824  C  CD2 . LEU A 1 106 ? 6.179   -2.521  23.508  1.00 11.64  ? 106  LEU A CD2 1 
ATOM   825  N  N   . SER A 1 107 ? 11.606  -2.422  22.731  1.00 12.18  ? 107  SER A N   1 
ATOM   826  C  CA  . SER A 1 107 ? 12.850  -2.030  22.064  1.00 14.26  ? 107  SER A CA  1 
ATOM   827  C  C   . SER A 1 107 ? 13.696  -3.276  21.821  1.00 13.19  ? 107  SER A C   1 
ATOM   828  O  O   . SER A 1 107 ? 13.336  -4.392  22.228  1.00 13.04  ? 107  SER A O   1 
ATOM   829  C  CB  . SER A 1 107 ? 13.618  -0.978  22.858  1.00 16.52  ? 107  SER A CB  1 
ATOM   830  O  OG  . SER A 1 107 ? 13.943  -1.462  24.139  1.00 18.08  ? 107  SER A OG  1 
ATOM   831  N  N   . GLY A 1 108 ? 14.793  -3.105  21.098  1.00 14.03  ? 108  GLY A N   1 
ATOM   832  C  CA  . GLY A 1 108 ? 15.686  -4.212  20.769  1.00 14.34  ? 108  GLY A CA  1 
ATOM   833  C  C   . GLY A 1 108 ? 15.146  -5.240  19.810  1.00 14.05  ? 108  GLY A C   1 
ATOM   834  O  O   . GLY A 1 108 ? 14.125  -5.044  19.187  1.00 14.86  ? 108  GLY A O   1 
ATOM   835  N  N   . ASP A 1 109 ? 15.801  -6.397  19.753  1.00 15.00  ? 109  ASP A N   1 
ATOM   836  C  CA  . ASP A 1 109 ? 15.464  -7.412  18.777  1.00 16.60  ? 109  ASP A CA  1 
ATOM   837  C  C   . ASP A 1 109 ? 14.132  -8.103  19.068  1.00 15.89  ? 109  ASP A C   1 
ATOM   838  O  O   . ASP A 1 109 ? 13.513  -8.665  18.176  1.00 18.51  ? 109  ASP A O   1 
ATOM   839  C  CB  . ASP A 1 109 ? 16.581  -8.464  18.713  1.00 18.05  ? 109  ASP A CB  1 
ATOM   840  C  CG  . ASP A 1 109 ? 16.463  -9.356  17.495  1.00 21.46  ? 109  ASP A CG  1 
ATOM   841  O  OD1 . ASP A 1 109 ? 16.318  -8.802  16.376  1.00 26.89  ? 109  ASP A OD1 1 
ATOM   842  O  OD2 . ASP A 1 109 ? 16.518  -10.593 17.655  1.00 27.04  ? 109  ASP A OD2 1 
ATOM   843  N  N   . HIS A 1 110 ? 13.688  -8.093  20.322  1.00 13.34  ? 110  HIS A N   1 
ATOM   844  C  CA  . HIS A 1 110 ? 12.368  -8.653  20.676  1.00 13.79  ? 110  HIS A CA  1 
ATOM   845  C  C   . HIS A 1 110 ? 11.267  -7.613  20.619  1.00 12.01  ? 110  HIS A C   1 
ATOM   846  O  O   . HIS A 1 110 ? 10.177  -7.881  21.119  1.00 12.02  ? 110  HIS A O   1 
ATOM   847  C  CB  . HIS A 1 110 ? 12.348  -9.248  22.078  1.00 15.67  ? 110  HIS A CB  1 
ATOM   848  C  CG  . HIS A 1 110 ? 13.099  -10.514 22.189  1.00 18.46  ? 110  HIS A CG  1 
ATOM   849  N  ND1 . HIS A 1 110 ? 12.944  -11.405 23.235  1.00 21.05  ? 110  HIS A ND1 1 
ATOM   850  C  CD2 . HIS A 1 110 ? 13.978  -11.072 21.336  1.00 18.64  ? 110  HIS A CD2 1 
ATOM   851  C  CE1 . HIS A 1 110 ? 13.746  -12.438 23.025  1.00 19.56  ? 110  HIS A CE1 1 
ATOM   852  N  NE2 . HIS A 1 110 ? 14.395  -12.250 21.892  1.00 20.57  ? 110  HIS A NE2 1 
ATOM   853  N  N   . CYS A 1 111 ? 11.546  -6.450  20.030  1.00 10.91  ? 111  CYS A N   1 
ATOM   854  C  CA  . CYS A 1 111 ? 10.543  -5.396  19.942  1.00 10.51  ? 111  CYS A CA  1 
ATOM   855  C  C   . CYS A 1 111 ? 9.323   -5.828  19.151  1.00 9.76   ? 111  CYS A C   1 
ATOM   856  O  O   . CYS A 1 111 ? 9.462   -6.331  18.025  1.00 10.33  ? 111  CYS A O   1 
ATOM   857  C  CB  . CYS A 1 111 ? 11.136  -4.176  19.275  1.00 10.93  ? 111  CYS A CB  1 
ATOM   858  S  SG  . CYS A 1 111 ? 10.109  -2.716  19.289  1.00 14.16  ? 111  CYS A SG  1 
ATOM   859  N  N   . ILE A 1 112 ? 8.157   -5.559  19.728  1.00 8.64   ? 112  ILE A N   1 
ATOM   860  C  CA  . ILE A 1 112 ? 6.898   -5.892  19.081  1.00 9.03   ? 112  ILE A CA  1 
ATOM   861  C  C   . ILE A 1 112 ? 6.240   -4.735  18.347  1.00 8.63   ? 112  ILE A C   1 
ATOM   862  O  O   . ILE A 1 112 ? 5.273   -4.917  17.636  1.00 9.07   ? 112  ILE A O   1 
ATOM   863  C  CB  . ILE A 1 112 ? 5.935   -6.537  20.105  1.00 8.58   ? 112  ILE A CB  1 
ATOM   864  C  CG1 . ILE A 1 112 ? 5.583   -5.599  21.269  1.00 10.75  ? 112  ILE A CG1 1 
ATOM   865  C  CG2 . ILE A 1 112 ? 6.510   -7.896  20.560  1.00 9.66   ? 112  ILE A CG2 1 
ATOM   866  C  CD1 . ILE A 1 112 ? 4.496   -6.124  22.174  1.00 11.40  ? 112  ILE A CD1 1 
ATOM   867  N  N   A THR A 1 113 ? 6.817   -3.549  18.510  0.50 8.74   ? 113  THR A N   1 
ATOM   868  N  N   B THR A 1 113 ? 6.730   -3.518  18.556  0.50 9.86   ? 113  THR A N   1 
ATOM   869  C  CA  A THR A 1 113 ? 6.287   -2.376  17.867  0.50 8.17   ? 113  THR A CA  1 
ATOM   870  C  CA  B THR A 1 113 ? 6.114   -2.383  17.898  0.50 10.16  ? 113  THR A CA  1 
ATOM   871  C  C   A THR A 1 113 ? 6.408   -2.534  16.343  0.50 8.20   ? 113  THR A C   1 
ATOM   872  C  C   B THR A 1 113 ? 6.389   -2.468  16.393  0.50 9.43   ? 113  THR A C   1 
ATOM   873  O  O   A THR A 1 113 ? 7.406   -3.054  15.863  0.50 9.39   ? 113  THR A O   1 
ATOM   874  O  O   B THR A 1 113 ? 7.482   -2.844  15.983  0.50 10.46  ? 113  THR A O   1 
ATOM   875  C  CB  A THR A 1 113 ? 6.977   -1.127  18.374  0.50 7.62   ? 113  THR A CB  1 
ATOM   876  C  CB  B THR A 1 113 ? 6.581   -1.076  18.495  0.50 11.36  ? 113  THR A CB  1 
ATOM   877  O  OG1 A THR A 1 113 ? 6.961   -1.189  19.804  0.50 10.26  ? 113  THR A OG1 1 
ATOM   878  O  OG1 B THR A 1 113 ? 7.939   -0.847  18.148  0.50 16.68  ? 113  THR A OG1 1 
ATOM   879  C  CG2 A THR A 1 113 ? 6.203   0.104   17.890  0.50 8.45   ? 113  THR A CG2 1 
ATOM   880  C  CG2 B THR A 1 113 ? 6.419   -1.165  19.986  0.50 9.43   ? 113  THR A CG2 1 
ATOM   881  N  N   . GLY A 1 114 ? 5.371   -2.149  15.592  1.00 8.27   ? 114  GLY A N   1 
ATOM   882  C  CA  . GLY A 1 114 ? 5.397   -2.350  14.169  1.00 8.06   ? 114  GLY A CA  1 
ATOM   883  C  C   . GLY A 1 114 ? 4.947   -3.723  13.711  1.00 7.70   ? 114  GLY A C   1 
ATOM   884  O  O   . GLY A 1 114 ? 4.955   -3.991  12.537  1.00 8.44   ? 114  GLY A O   1 
ATOM   885  N  N   . ARG A 1 115 ? 4.633   -4.582  14.666  1.00 7.64   ? 115  ARG A N   1 
ATOM   886  C  CA  . ARG A 1 115 ? 4.111   -5.927  14.387  1.00 7.59   ? 115  ARG A CA  1 
ATOM   887  C  C   . ARG A 1 115 ? 2.612   -5.953  14.704  1.00 7.67   ? 115  ARG A C   1 
ATOM   888  O  O   . ARG A 1 115 ? 2.069   -4.958  15.072  1.00 10.68  ? 115  ARG A O   1 
ATOM   889  C  CB  . ARG A 1 115 ? 4.931   -6.975  15.141  1.00 8.30   ? 115  ARG A CB  1 
ATOM   890  C  CG  . ARG A 1 115 ? 6.401   -6.842  14.821  1.00 9.14   ? 115  ARG A CG  1 
ATOM   891  C  CD  . ARG A 1 115 ? 7.244   -7.957  15.345  1.00 10.82  ? 115  ARG A CD  1 
ATOM   892  N  NE  . ARG A 1 115 ? 8.671   -7.692  15.225  1.00 10.82  ? 115  ARG A NE  1 
ATOM   893  C  CZ  . ARG A 1 115 ? 9.403   -8.000  14.159  1.00 10.28  ? 115  ARG A CZ  1 
ATOM   894  N  NH1 . ARG A 1 115 ? 8.851   -8.573  13.102  1.00 10.51  ? 115  ARG A NH1 1 
ATOM   895  N  NH2 . ARG A 1 115 ? 10.700  -7.741  14.142  1.00 11.83  ? 115  ARG A NH2 1 
ATOM   896  N  N   . THR A 1 116 ? 1.928   -7.067  14.485  1.00 8.21   ? 116  THR A N   1 
ATOM   897  C  CA  . THR A 1 116 ? 0.483   -7.138  14.617  1.00 8.18   ? 116  THR A CA  1 
ATOM   898  C  C   . THR A 1 116 ? 0.080   -7.938  15.845  1.00 8.05   ? 116  THR A C   1 
ATOM   899  O  O   . THR A 1 116 ? 0.549   -9.065  16.004  1.00 9.63   ? 116  THR A O   1 
ATOM   900  C  CB  . THR A 1 116 ? -0.156  -7.772  13.376  1.00 8.66   ? 116  THR A CB  1 
ATOM   901  O  OG1 . THR A 1 116 ? 0.095   -6.949  12.252  1.00 10.36  ? 116  THR A OG1 1 
ATOM   902  C  CG2 . THR A 1 116 ? -1.642  -7.930  13.535  1.00 9.50   ? 116  THR A CG2 1 
ATOM   903  N  N   . LEU A 1 117 ? -0.821  -7.393  16.659  1.00 7.35   ? 117  LEU A N   1 
ATOM   904  C  CA  . LEU A 1 117 ? -1.470  -8.147  17.711  1.00 7.86   ? 117  LEU A CA  1 
ATOM   905  C  C   . LEU A 1 117 ? -2.756  -8.738  17.179  1.00 7.77   ? 117  LEU A C   1 
ATOM   906  O  O   . LEU A 1 117 ? -3.504  -8.036  16.517  1.00 8.91   ? 117  LEU A O   1 
ATOM   907  C  CB  . LEU A 1 117 ? -1.774  -7.213  18.863  1.00 8.03   ? 117  LEU A CB  1 
ATOM   908  C  CG  . LEU A 1 117 ? -2.328  -7.829  20.136  1.00 8.63   ? 117  LEU A CG  1 
ATOM   909  C  CD1 . LEU A 1 117 ? -1.295  -8.776  20.802  1.00 10.02  ? 117  LEU A CD1 1 
ATOM   910  C  CD2 . LEU A 1 117 ? -2.711  -6.677  21.118  1.00 10.75  ? 117  LEU A CD2 1 
ATOM   911  N  N   . VAL A 1 118 ? -3.001  -10.020 17.458  1.00 7.33   ? 118  VAL A N   1 
ATOM   912  C  CA  . VAL A 1 118 ? -4.139  -10.755 16.922  1.00 8.47   ? 118  VAL A CA  1 
ATOM   913  C  C   . VAL A 1 118 ? -4.884  -11.456 18.038  1.00 8.08   ? 118  VAL A C   1 
ATOM   914  O  O   . VAL A 1 118 ? -4.283  -12.062 18.940  1.00 8.67   ? 118  VAL A O   1 
ATOM   915  C  CB  . VAL A 1 118 ? -3.709  -11.808 15.891  1.00 8.98   ? 118  VAL A CB  1 
ATOM   916  C  CG1 . VAL A 1 118 ? -4.909  -12.593 15.359  1.00 10.40  ? 118  VAL A CG1 1 
ATOM   917  C  CG2 . VAL A 1 118 ? -2.905  -11.178 14.781  1.00 9.14   ? 118  VAL A CG2 1 
ATOM   918  N  N   . VAL A 1 119 ? -6.209  -11.347 18.004  1.00 8.23   ? 119  VAL A N   1 
ATOM   919  C  CA  . VAL A 1 119 ? -7.085  -12.169 18.836  1.00 8.98   ? 119  VAL A CA  1 
ATOM   920  C  C   . VAL A 1 119 ? -7.825  -13.173 17.960  1.00 8.35   ? 119  VAL A C   1 
ATOM   921  O  O   . VAL A 1 119 ? -8.347  -12.837 16.917  1.00 8.99   ? 119  VAL A O   1 
ATOM   922  C  CB  . VAL A 1 119 ? -8.031  -11.317 19.743  1.00 9.80   ? 119  VAL A CB  1 
ATOM   923  C  CG1 . VAL A 1 119 ? -8.887  -10.437 18.970  1.00 11.92  ? 119  VAL A CG1 1 
ATOM   924  C  CG2 . VAL A 1 119 ? -8.840  -12.198 20.686  1.00 11.47  ? 119  VAL A CG2 1 
ATOM   925  N  N   . HIS A 1 120 ? -7.775  -14.415 18.411  1.00 8.43   ? 120  HIS A N   1 
ATOM   926  C  CA  . HIS A 1 120 ? -8.206  -15.540 17.631  1.00 8.83   ? 120  HIS A CA  1 
ATOM   927  C  C   . HIS A 1 120 ? -9.600  -16.066 18.008  1.00 9.01   ? 120  HIS A C   1 
ATOM   928  O  O   . HIS A 1 120 ? -10.151 -15.786 19.067  1.00 10.10  ? 120  HIS A O   1 
ATOM   929  C  CB  . HIS A 1 120 ? -7.194  -16.674 17.784  1.00 9.27   ? 120  HIS A CB  1 
ATOM   930  C  CG  . HIS A 1 120 ? -5.903  -16.434 17.075  1.00 9.25   ? 120  HIS A CG  1 
ATOM   931  N  ND1 . HIS A 1 120 ? -5.641  -16.926 15.811  1.00 10.60  ? 120  HIS A ND1 1 
ATOM   932  C  CD2 . HIS A 1 120 ? -4.783  -15.751 17.446  1.00 9.82   ? 120  HIS A CD2 1 
ATOM   933  C  CE1 . HIS A 1 120 ? -4.431  -16.539 15.430  1.00 10.70  ? 120  HIS A CE1 1 
ATOM   934  N  NE2 . HIS A 1 120 ? -3.883  -15.833 16.406  1.00 10.53  ? 120  HIS A NE2 1 
ATOM   935  N  N   . GLU A 1 121 ? -10.101 -16.927 17.127  1.00 10.25  ? 121  GLU A N   1 
ATOM   936  C  CA  . GLU A 1 121 ? -11.417 -17.561 17.230  1.00 11.68  ? 121  GLU A CA  1 
ATOM   937  C  C   . GLU A 1 121 ? -11.614 -18.482 18.438  1.00 11.14  ? 121  GLU A C   1 
ATOM   938  O  O   . GLU A 1 121 ? -12.683 -18.509 19.023  1.00 11.59  ? 121  GLU A O   1 
ATOM   939  C  CB  . GLU A 1 121 ? -11.602 -18.374 15.937  1.00 13.42  ? 121  GLU A CB  1 
ATOM   940  C  CG  . GLU A 1 121 ? -12.853 -19.198 15.739  1.00 17.51  ? 121  GLU A CG  1 
ATOM   941  C  CD  . GLU A 1 121 ? -12.669 -20.340 14.684  0.80 20.57  ? 121  GLU A CD  1 
ATOM   942  O  OE1 . GLU A 1 121 ? -11.563 -20.507 14.063  1.00 20.58  ? 121  GLU A OE1 1 
ATOM   943  O  OE2 . GLU A 1 121 ? -13.654 -21.106 14.500  0.70 22.90  ? 121  GLU A OE2 1 
ATOM   944  N  N   A LYS A 1 122 ? -10.584 -19.317 18.656  0.50 12.03  ? 122  LYS A N   1 
ATOM   945  N  N   B LYS A 1 122 ? -10.580 -19.148 18.913  0.50 10.72  ? 122  LYS A N   1 
ATOM   946  C  CA  A LYS A 1 122 ? -10.606 -20.476 19.569  0.50 11.67  ? 122  LYS A CA  1 
ATOM   947  C  CA  B LYS A 1 122 ? -10.805 -20.090 19.996  0.50 10.19  ? 122  LYS A CA  1 
ATOM   948  C  C   A LYS A 1 122 ? -9.484  -20.357 20.601  0.50 10.93  ? 122  LYS A C   1 
ATOM   949  C  C   B LYS A 1 122 ? -9.550  -20.212 20.802  0.50 9.91   ? 122  LYS A C   1 
ATOM   950  O  O   A LYS A 1 122 ? -8.598  -19.507 20.452  0.50 11.15  ? 122  LYS A O   1 
ATOM   951  O  O   B LYS A 1 122 ? -8.656  -19.362 20.736  0.50 10.10  ? 122  LYS A O   1 
ATOM   952  C  CB  A LYS A 1 122 ? -10.398 -21.793 18.795  0.50 12.33  ? 122  LYS A CB  1 
ATOM   953  C  CB  B LYS A 1 122 ? -11.311 -21.434 19.443  0.50 9.56   ? 122  LYS A CB  1 
ATOM   954  C  CG  A LYS A 1 122 ? -11.111 -21.938 17.466  0.50 13.27  ? 122  LYS A CG  1 
ATOM   955  C  CG  B LYS A 1 122 ? -10.376 -22.121 18.459  0.50 10.16  ? 122  LYS A CG  1 
ATOM   956  C  CD  A LYS A 1 122 ? -10.596 -23.171 16.755  0.50 15.64  ? 122  LYS A CD  1 
ATOM   957  C  CD  B LYS A 1 122 ? -11.101 -23.218 17.649  0.50 10.95  ? 122  LYS A CD  1 
ATOM   958  C  CE  A LYS A 1 122 ? -11.587 -23.738 15.822  0.50 18.19  ? 122  LYS A CE  1 
ATOM   959  C  CE  B LYS A 1 122 ? -10.090 -23.913 16.771  0.50 11.52  ? 122  LYS A CE  1 
ATOM   960  N  NZ  A LYS A 1 122 ? -10.957 -24.873 15.139  0.50 19.20  ? 122  LYS A NZ  1 
ATOM   961  N  NZ  B LYS A 1 122 ? -9.485  -25.026 17.578  0.50 17.31  ? 122  LYS A NZ  1 
ATOM   962  N  N   . ALA A 1 123 ? -9.505  -21.242 21.605  1.00 10.09  ? 123  ALA A N   1 
ATOM   963  C  CA  . ALA A 1 123 ? -8.479  -21.314 22.613  1.00 10.35  ? 123  ALA A CA  1 
ATOM   964  C  C   . ALA A 1 123 ? -7.125  -21.710 22.043  1.00 10.79  ? 123  ALA A C   1 
ATOM   965  O  O   . ALA A 1 123 ? -7.029  -22.544 21.162  1.00 11.58  ? 123  ALA A O   1 
ATOM   966  C  CB  . ALA A 1 123 ? -8.888  -22.285 23.682  1.00 11.43  ? 123  ALA A CB  1 
ATOM   967  N  N   . ASP A 1 124 ? -6.082  -21.103 22.591  1.00 10.24  ? 124  ASP A N   1 
ATOM   968  C  CA  . ASP A 1 124 ? -4.709  -21.527 22.407  1.00 10.64  ? 124  ASP A CA  1 
ATOM   969  C  C   . ASP A 1 124 ? -4.438  -22.595 23.471  1.00 10.24  ? 124  ASP A C   1 
ATOM   970  O  O   . ASP A 1 124 ? -4.615  -22.365 24.683  1.00 11.20  ? 124  ASP A O   1 
ATOM   971  C  CB  . ASP A 1 124 ? -3.823  -20.292 22.570  1.00 10.53  ? 124  ASP A CB  1 
ATOM   972  C  CG  . ASP A 1 124 ? -2.342  -20.540 22.351  1.00 11.21  ? 124  ASP A CG  1 
ATOM   973  O  OD1 . ASP A 1 124 ? -1.895  -21.698 22.312  1.00 10.70  ? 124  ASP A OD1 1 
ATOM   974  O  OD2 . ASP A 1 124 ? -1.618  -19.526 22.198  1.00 12.51  ? 124  ASP A OD2 1 
ATOM   975  N  N   . ASP A 1 125 ? -4.015  -23.762 23.010  1.00 11.01  ? 125  ASP A N   1 
ATOM   976  C  CA  . ASP A 1 125 ? -3.687  -24.872 23.926  1.00 11.58  ? 125  ASP A CA  1 
ATOM   977  C  C   . ASP A 1 125 ? -2.267  -24.805 24.513  1.00 10.88  ? 125  ASP A C   1 
ATOM   978  O  O   . ASP A 1 125 ? -1.815  -25.721 25.199  1.00 11.53  ? 125  ASP A O   1 
ATOM   979  C  CB  . ASP A 1 125 ? -3.951  -26.223 23.256  1.00 11.91  ? 125  ASP A CB  1 
ATOM   980  C  CG  . ASP A 1 125 ? -3.073  -26.477 22.036  1.00 11.97  ? 125  ASP A CG  1 
ATOM   981  O  OD1 . ASP A 1 125 ? -1.961  -25.915 21.980  1.00 12.95  ? 125  ASP A OD1 1 
ATOM   982  O  OD2 . ASP A 1 125 ? -3.453  -27.303 21.153  1.00 14.56  ? 125  ASP A OD2 1 
ATOM   983  N  N   . LEU A 1 126 ? -1.562  -23.699 24.237  1.00 11.14  ? 126  LEU A N   1 
ATOM   984  C  CA  . LEU A 1 126 ? -0.262  -23.389 24.838  1.00 11.14  ? 126  LEU A CA  1 
ATOM   985  C  C   . LEU A 1 126 ? 0.775   -24.426 24.511  1.00 12.36  ? 126  LEU A C   1 
ATOM   986  O  O   . LEU A 1 126 ? 1.720   -24.606 25.249  1.00 12.63  ? 126  LEU A O   1 
ATOM   987  C  CB  . LEU A 1 126 ? -0.359  -23.080 26.349  1.00 11.09  ? 126  LEU A CB  1 
ATOM   988  C  CG  . LEU A 1 126 ? -1.441  -22.081 26.800  1.00 11.14  ? 126  LEU A CG  1 
ATOM   989  C  CD1 . LEU A 1 126 ? -1.337  -21.746 28.270  1.00 13.47  ? 126  LEU A CD1 1 
ATOM   990  C  CD2 . LEU A 1 126 ? -1.465  -20.803 25.945  1.00 12.17  ? 126  LEU A CD2 1 
ATOM   991  N  N   . GLY A 1 127 ? 0.622   -25.072 23.364  1.00 11.77  ? 127  GLY A N   1 
ATOM   992  C  CA  . GLY A 1 127 ? 1.536   -26.097 22.918  1.00 13.39  ? 127  GLY A CA  1 
ATOM   993  C  C   . GLY A 1 127 ? 1.397   -27.425 23.597  1.00 13.67  ? 127  GLY A C   1 
ATOM   994  O  O   . GLY A 1 127 ? 2.278   -28.291 23.423  1.00 14.82  ? 127  GLY A O   1 
ATOM   995  N  N   . LYS A 1 128 ? 0.296   -27.620 24.344  1.00 12.50  ? 128  LYS A N   1 
ATOM   996  C  CA  . LYS A 1 128 ? 0.084   -28.853 25.132  1.00 13.75  ? 128  LYS A CA  1 
ATOM   997  C  C   . LYS A 1 128 ? -1.009  -29.703 24.554  1.00 14.22  ? 128  LYS A C   1 
ATOM   998  O  O   . LYS A 1 128 ? -1.489  -30.644 25.185  1.00 15.98  ? 128  LYS A O   1 
ATOM   999  C  CB  . LYS A 1 128 ? -0.262  -28.482 26.577  1.00 15.01  ? 128  LYS A CB  1 
ATOM   1000 C  CG  . LYS A 1 128 ? 0.780   -27.675 27.291  1.00 19.33  ? 128  LYS A CG  1 
ATOM   1001 C  CD  . LYS A 1 128 ? 1.971   -28.528 27.642  0.50 21.91  ? 128  LYS A CD  1 
ATOM   1002 C  CE  . LYS A 1 128 ? 2.799   -27.932 28.768  0.50 24.44  ? 128  LYS A CE  1 
ATOM   1003 N  NZ  . LYS A 1 128 ? 3.609   -28.974 29.461  0.50 26.69  ? 128  LYS A NZ  1 
ATOM   1004 N  N   . GLY A 1 129 ? -1.398  -29.413 23.319  1.00 13.92  ? 129  GLY A N   1 
ATOM   1005 C  CA  . GLY A 1 129 ? -2.467  -30.168 22.681  1.00 15.27  ? 129  GLY A CA  1 
ATOM   1006 C  C   . GLY A 1 129 ? -2.117  -31.540 22.141  1.00 16.28  ? 129  GLY A C   1 
ATOM   1007 O  O   . GLY A 1 129 ? -3.025  -32.286 21.822  1.00 18.03  ? 129  GLY A O   1 
ATOM   1008 N  N   . GLY A 1 130 ? -0.836  -31.876 22.002  1.00 15.95  ? 130  GLY A N   1 
ATOM   1009 C  CA  . GLY A 1 130 ? -0.429  -33.243 21.599  1.00 17.51  ? 130  GLY A CA  1 
ATOM   1010 C  C   . GLY A 1 130 ? -0.600  -33.511 20.114  1.00 18.51  ? 130  GLY A C   1 
ATOM   1011 O  O   . GLY A 1 130 ? -0.752  -34.658 19.682  1.00 21.30  ? 130  GLY A O   1 
ATOM   1012 N  N   A ASN A 1 131 ? -0.611  -32.450 19.313  0.50 18.89  ? 131  ASN A N   1 
ATOM   1013 N  N   B ASN A 1 131 ? -0.548  -32.452 19.320  0.50 18.45  ? 131  ASN A N   1 
ATOM   1014 C  CA  A ASN A 1 131 ? -0.535  -32.597 17.865  0.50 18.76  ? 131  ASN A CA  1 
ATOM   1015 C  CA  B ASN A 1 131 ? -0.529  -32.594 17.880  0.50 17.88  ? 131  ASN A CA  1 
ATOM   1016 C  C   A ASN A 1 131 ? 0.423   -31.575 17.280  0.50 18.62  ? 131  ASN A C   1 
ATOM   1017 C  C   B ASN A 1 131 ? 0.424   -31.572 17.280  0.50 18.15  ? 131  ASN A C   1 
ATOM   1018 O  O   A ASN A 1 131 ? 0.936   -30.691 17.980  0.50 18.22  ? 131  ASN A O   1 
ATOM   1019 O  O   B ASN A 1 131 ? 0.942   -30.687 17.976  0.50 17.76  ? 131  ASN A O   1 
ATOM   1020 C  CB  A ASN A 1 131 ? -1.927  -32.516 17.211  0.50 18.66  ? 131  ASN A CB  1 
ATOM   1021 C  CB  B ASN A 1 131 ? -1.951  -32.477 17.315  0.50 17.25  ? 131  ASN A CB  1 
ATOM   1022 C  CG  A ASN A 1 131 ? -2.571  -31.146 17.339  0.50 20.14  ? 131  ASN A CG  1 
ATOM   1023 C  CG  B ASN A 1 131 ? -2.686  -31.236 17.806  0.50 16.26  ? 131  ASN A CG  1 
ATOM   1024 O  OD1 A ASN A 1 131 ? -1.991  -30.235 17.910  0.50 20.27  ? 131  ASN A OD1 1 
ATOM   1025 O  OD1 B ASN A 1 131 ? -2.275  -30.118 17.504  0.50 15.12  ? 131  ASN A OD1 1 
ATOM   1026 N  ND2 A ASN A 1 131 ? -3.773  -30.994 16.787  0.50 21.49  ? 131  ASN A ND2 1 
ATOM   1027 N  ND2 B ASN A 1 131 ? -3.800  -31.426 18.520  0.50 17.03  ? 131  ASN A ND2 1 
ATOM   1028 N  N   . GLU A 1 132 ? 0.691   -31.713 15.989  1.00 18.25  ? 132  GLU A N   1 
ATOM   1029 C  CA  . GLU A 1 132 ? 1.718   -30.904 15.351  1.00 19.17  ? 132  GLU A CA  1 
ATOM   1030 C  C   . GLU A 1 132 ? 1.339   -29.427 15.334  1.00 17.79  ? 132  GLU A C   1 
ATOM   1031 O  O   . GLU A 1 132 ? 2.195   -28.541 15.570  1.00 18.47  ? 132  GLU A O   1 
ATOM   1032 C  CB  . GLU A 1 132 ? 1.994   -31.406 13.957  1.00 20.95  ? 132  GLU A CB  1 
ATOM   1033 C  CG  . GLU A 1 132 ? 3.007   -30.599 13.214  0.50 21.49  ? 132  GLU A CG  1 
ATOM   1034 C  CD  . GLU A 1 132 ? 2.377   -29.496 12.424  0.50 23.35  ? 132  GLU A CD  1 
ATOM   1035 O  OE1 . GLU A 1 132 ? 1.158   -29.553 12.172  0.50 24.80  ? 132  GLU A OE1 1 
ATOM   1036 O  OE2 . GLU A 1 132 ? 3.117   -28.580 12.038  0.50 25.31  ? 132  GLU A OE2 1 
ATOM   1037 N  N   . GLU A 1 133 ? 0.059   -29.145 15.104  1.00 16.09  ? 133  GLU A N   1 
ATOM   1038 C  CA  . GLU A 1 133 ? -0.392  -27.757 15.060  1.00 16.65  ? 133  GLU A CA  1 
ATOM   1039 C  C   . GLU A 1 133 ? -0.219  -27.093 16.417  1.00 15.01  ? 133  GLU A C   1 
ATOM   1040 O  O   . GLU A 1 133 ? 0.012   -25.878 16.501  1.00 14.69  ? 133  GLU A O   1 
ATOM   1041 C  CB  . GLU A 1 133 ? -1.848  -27.701 14.610  1.00 17.96  ? 133  GLU A CB  1 
ATOM   1042 C  CG  . GLU A 1 133 ? -2.051  -27.958 13.141  1.00 21.04  ? 133  GLU A CG  1 
ATOM   1043 C  CD  . GLU A 1 133 ? -2.420  -26.727 12.372  0.10 20.82  ? 133  GLU A CD  1 
ATOM   1044 O  OE1 . GLU A 1 133 ? -3.281  -25.957 12.847  0.10 21.09  ? 133  GLU A OE1 1 
ATOM   1045 O  OE2 . GLU A 1 133 ? -1.859  -26.538 11.275  0.10 21.53  ? 133  GLU A OE2 1 
ATOM   1046 N  N   . SER A 1 134 ? -0.348  -27.841 17.502  1.00 14.54  ? 134  SER A N   1 
ATOM   1047 C  CA  . SER A 1 134 ? -0.266  -27.262 18.816  1.00 13.59  ? 134  SER A CA  1 
ATOM   1048 C  C   . SER A 1 134 ? 1.069   -26.553 19.004  1.00 13.49  ? 134  SER A C   1 
ATOM   1049 O  O   . SER A 1 134 ? 1.110   -25.496 19.635  1.00 12.89  ? 134  SER A O   1 
ATOM   1050 C  CB  . SER A 1 134 ? -0.419  -28.322 19.886  1.00 12.75  ? 134  SER A CB  1 
ATOM   1051 O  OG  . SER A 1 134 ? -0.319  -27.791 21.183  1.00 14.12  ? 134  SER A OG  1 
ATOM   1052 N  N   . THR A 1 135 ? 2.152   -27.108 18.467  1.00 14.55  ? 135  THR A N   1 
ATOM   1053 C  CA  . THR A 1 135 ? 3.470   -26.485 18.672  1.00 15.31  ? 135  THR A CA  1 
ATOM   1054 C  C   . THR A 1 135 ? 3.833   -25.474 17.578  1.00 13.46  ? 135  THR A C   1 
ATOM   1055 O  O   . THR A 1 135 ? 4.976   -24.987 17.537  1.00 13.39  ? 135  THR A O   1 
ATOM   1056 C  CB  . THR A 1 135 ? 4.583   -27.490 18.989  1.00 17.24  ? 135  THR A CB  1 
ATOM   1057 O  OG1 . THR A 1 135 ? 4.429   -28.599 18.143  1.00 22.01  ? 135  THR A OG1 1 
ATOM   1058 C  CG2 . THR A 1 135 ? 4.436   -27.985 20.415  1.00 19.16  ? 135  THR A CG2 1 
ATOM   1059 N  N   A LYS A 1 136 ? 2.864   -25.112 16.740  0.60 13.41  ? 136  LYS A N   1 
ATOM   1060 N  N   B LYS A 1 136 ? 2.847   -25.100 16.763  0.40 13.48  ? 136  LYS A N   1 
ATOM   1061 C  CA  A LYS A 1 136 ? 3.050   -24.027 15.769  0.60 13.66  ? 136  LYS A CA  1 
ATOM   1062 C  CA  B LYS A 1 136 ? 2.997   -24.037 15.767  0.40 13.56  ? 136  LYS A CA  1 
ATOM   1063 C  C   A LYS A 1 136 ? 2.078   -22.842 16.045  0.60 12.92  ? 136  LYS A C   1 
ATOM   1064 C  C   B LYS A 1 136 ? 2.076   -22.846 16.067  0.40 13.05  ? 136  LYS A C   1 
ATOM   1065 O  O   A LYS A 1 136 ? 2.518   -21.680 16.159  0.60 12.54  ? 136  LYS A O   1 
ATOM   1066 O  O   B LYS A 1 136 ? 2.531   -21.698 16.179  0.40 12.92  ? 136  LYS A O   1 
ATOM   1067 C  CB  A LYS A 1 136 ? 2.971   -24.579 14.332  0.60 14.88  ? 136  LYS A CB  1 
ATOM   1068 C  CB  B LYS A 1 136 ? 2.707   -24.606 14.381  0.40 14.39  ? 136  LYS A CB  1 
ATOM   1069 C  CG  A LYS A 1 136 ? 4.157   -25.515 13.968  0.60 17.27  ? 136  LYS A CG  1 
ATOM   1070 C  CG  B LYS A 1 136 ? 3.602   -25.770 14.051  0.40 15.75  ? 136  LYS A CG  1 
ATOM   1071 C  CD  A LYS A 1 136 ? 4.083   -26.055 12.536  0.60 20.72  ? 136  LYS A CD  1 
ATOM   1072 C  CD  B LYS A 1 136 ? 3.356   -26.330 12.671  0.40 19.60  ? 136  LYS A CD  1 
ATOM   1073 C  CE  A LYS A 1 136 ? 4.560   -25.054 11.489  0.60 23.08  ? 136  LYS A CE  1 
ATOM   1074 C  CE  B LYS A 1 136 ? 4.411   -27.364 12.300  0.40 21.07  ? 136  LYS A CE  1 
ATOM   1075 N  NZ  A LYS A 1 136 ? 3.954   -25.244 10.170  0.60 23.91  ? 136  LYS A NZ  1 
ATOM   1076 N  NZ  B LYS A 1 136 ? 5.766   -26.772 12.171  0.40 21.24  ? 136  LYS A NZ  1 
ATOM   1077 N  N   . THR A 1 137 ? 0.786   -23.123 16.221  1.00 12.49  ? 137  THR A N   1 
ATOM   1078 C  CA  . THR A 1 137 ? -0.238  -22.083 16.381  1.00 12.92  ? 137  THR A CA  1 
ATOM   1079 C  C   . THR A 1 137 ? -1.036  -22.199 17.668  1.00 12.17  ? 137  THR A C   1 
ATOM   1080 O  O   . THR A 1 137 ? -1.830  -21.323 18.005  1.00 13.20  ? 137  THR A O   1 
ATOM   1081 C  CB  . THR A 1 137 ? -1.260  -22.134 15.235  1.00 14.25  ? 137  THR A CB  1 
ATOM   1082 O  OG1 . THR A 1 137 ? -1.952  -23.375 15.328  1.00 15.95  ? 137  THR A OG1 1 
ATOM   1083 C  CG2 . THR A 1 137 ? -0.600  -21.975 13.854  1.00 16.44  ? 137  THR A CG2 1 
ATOM   1084 N  N   . GLY A 1 138 ? -0.918  -23.321 18.363  1.00 11.36  ? 138  GLY A N   1 
ATOM   1085 C  CA  . GLY A 1 138 ? -1.732  -23.582 19.521  1.00 11.91  ? 138  GLY A CA  1 
ATOM   1086 C  C   . GLY A 1 138 ? -3.167  -23.954 19.217  1.00 11.58  ? 138  GLY A C   1 
ATOM   1087 O  O   . GLY A 1 138 ? -3.975  -23.976 20.118  1.00 11.91  ? 138  GLY A O   1 
ATOM   1088 N  N   . ASN A 1 139 ? -3.479  -24.212 17.957  1.00 12.13  ? 139  ASN A N   1 
ATOM   1089 C  CA  . ASN A 1 139 ? -4.835  -24.540 17.557  1.00 12.92  ? 139  ASN A CA  1 
ATOM   1090 C  C   . ASN A 1 139 ? -5.856  -23.455 17.857  1.00 12.49  ? 139  ASN A C   1 
ATOM   1091 O  O   . ASN A 1 139 ? -7.023  -23.750 18.058  1.00 13.56  ? 139  ASN A O   1 
ATOM   1092 C  CB  . ASN A 1 139 ? -5.287  -25.877 18.186  1.00 13.71  ? 139  ASN A CB  1 
ATOM   1093 C  CG  . ASN A 1 139 ? -4.554  -27.074 17.597  1.00 15.80  ? 139  ASN A CG  1 
ATOM   1094 O  OD1 . ASN A 1 139 ? -4.710  -27.397 16.421  1.00 20.19  ? 139  ASN A OD1 1 
ATOM   1095 N  ND2 . ASN A 1 139 ? -3.715  -27.701 18.392  1.00 17.49  ? 139  ASN A ND2 1 
ATOM   1096 N  N   . ALA A 1 140 ? -5.439  -22.196 17.825  1.00 11.94  ? 140  ALA A N   1 
ATOM   1097 C  CA  . ALA A 1 140 ? -6.320  -21.104 18.172  1.00 11.67  ? 140  ALA A CA  1 
ATOM   1098 C  C   . ALA A 1 140 ? -7.246  -20.667 17.027  1.00 11.89  ? 140  ALA A C   1 
ATOM   1099 O  O   . ALA A 1 140 ? -8.093  -19.809 17.233  1.00 11.85  ? 140  ALA A O   1 
ATOM   1100 C  CB  . ALA A 1 140 ? -5.499  -19.908 18.684  1.00 12.40  ? 140  ALA A CB  1 
ATOM   1101 N  N   . GLY A 1 141 ? -7.092  -21.217 15.834  1.00 12.98  ? 141  GLY A N   1 
ATOM   1102 C  CA  . GLY A 1 141 ? -8.043  -20.951 14.791  1.00 13.05  ? 141  GLY A CA  1 
ATOM   1103 C  C   . GLY A 1 141 ? -7.878  -19.595 14.128  1.00 12.59  ? 141  GLY A C   1 
ATOM   1104 O  O   . GLY A 1 141 ? -6.815  -19.002 14.130  1.00 12.11  ? 141  GLY A O   1 
ATOM   1105 N  N   . SER A 1 142 ? -8.965  -19.147 13.516  1.00 12.64  ? 142  SER A N   1 
ATOM   1106 C  CA  . SER A 1 142 ? -8.944  -17.954 12.677  1.00 12.31  ? 142  SER A CA  1 
ATOM   1107 C  C   . SER A 1 142 ? -8.712  -16.670 13.466  1.00 10.22  ? 142  SER A C   1 
ATOM   1108 O  O   . SER A 1 142 ? -8.727  -16.665 14.699  1.00 11.56  ? 142  SER A O   1 
ATOM   1109 C  CB  . SER A 1 142 ? -10.217 -17.860 11.845  1.00 13.35  ? 142  SER A CB  1 
ATOM   1110 O  OG  . SER A 1 142 ? -11.290 -17.509 12.661  1.00 18.30  ? 142  SER A OG  1 
ATOM   1111 N  N   . ARG A 1 143 ? -8.507  -15.584 12.720  1.00 11.15  ? 143  ARG A N   1 
ATOM   1112 C  CA  . ARG A 1 143 ? -8.143  -14.298 13.302  1.00 10.47  ? 143  ARG A CA  1 
ATOM   1113 C  C   . ARG A 1 143 ? -9.358  -13.390 13.326  1.00 10.76  ? 143  ARG A C   1 
ATOM   1114 O  O   . ARG A 1 143 ? -9.870  -13.016 12.259  1.00 13.86  ? 143  ARG A O   1 
ATOM   1115 C  CB  . ARG A 1 143 ? -7.000  -13.696 12.498  1.00 10.66  ? 143  ARG A CB  1 
ATOM   1116 C  CG  . ARG A 1 143 ? -5.856  -14.634 12.405  1.00 11.06  ? 143  ARG A CG  1 
ATOM   1117 C  CD  . ARG A 1 143 ? -4.683  -14.175 11.608  1.00 11.31  ? 143  ARG A CD  1 
ATOM   1118 N  NE  . ARG A 1 143 ? -3.694  -15.265 11.544  1.00 10.93  ? 143  ARG A NE  1 
ATOM   1119 C  CZ  . ARG A 1 143 ? -2.462  -15.159 11.071  1.00 9.79   ? 143  ARG A CZ  1 
ATOM   1120 N  NH1 . ARG A 1 143 ? -1.981  -14.002 10.641  1.00 11.13  ? 143  ARG A NH1 1 
ATOM   1121 N  NH2 . ARG A 1 143 ? -1.679  -16.209 11.079  1.00 10.94  ? 143  ARG A NH2 1 
ATOM   1122 N  N   . LEU A 1 144 ? -9.855  -13.053 14.505  1.00 9.89   ? 144  LEU A N   1 
ATOM   1123 C  CA  . LEU A 1 144 ? -11.080 -12.269 14.599  1.00 10.08  ? 144  LEU A CA  1 
ATOM   1124 C  C   . LEU A 1 144 ? -10.838 -10.777 14.510  1.00 9.65   ? 144  LEU A C   1 
ATOM   1125 O  O   . LEU A 1 144 ? -11.667 -10.049 13.974  1.00 10.54  ? 144  LEU A O   1 
ATOM   1126 C  CB  . LEU A 1 144 ? -11.831 -12.571 15.884  1.00 10.67  ? 144  LEU A CB  1 
ATOM   1127 C  CG  . LEU A 1 144 ? -12.167 -14.035 16.121  1.00 12.62  ? 144  LEU A CG  1 
ATOM   1128 C  CD1 . LEU A 1 144 ? -12.900 -14.134 17.401  1.00 16.83  ? 144  LEU A CD1 1 
ATOM   1129 C  CD2 . LEU A 1 144 ? -12.962 -14.617 14.995  1.00 16.64  ? 144  LEU A CD2 1 
ATOM   1130 N  N   . ALA A 1 145 ? -9.745  -10.285 15.065  1.00 8.63   ? 145  ALA A N   1 
ATOM   1131 C  CA  . ALA A 1 145 ? -9.423  -8.881  15.042  1.00 9.48   ? 145  ALA A CA  1 
ATOM   1132 C  C   . ALA A 1 145 ? -7.928  -8.745  15.222  1.00 8.14   ? 145  ALA A C   1 
ATOM   1133 O  O   . ALA A 1 145 ? -7.259  -9.623  15.795  1.00 8.75   ? 145  ALA A O   1 
ATOM   1134 C  CB  . ALA A 1 145 ? -10.164 -8.114  16.134  1.00 10.13  ? 145  ALA A CB  1 
ATOM   1135 N  N   . CYS A 1 146 ? -7.389  -7.644  14.718  1.00 8.41   ? 146  CYS A N   1 
ATOM   1136 C  CA  . CYS A 1 146 ? -5.966  -7.379  14.805  1.00 9.18   ? 146  CYS A CA  1 
ATOM   1137 C  C   . CYS A 1 146 ? -5.693  -5.903  14.649  1.00 8.74   ? 146  CYS A C   1 
ATOM   1138 O  O   . CYS A 1 146 ? -6.566  -5.148  14.260  1.00 9.31   ? 146  CYS A O   1 
ATOM   1139 C  CB  . CYS A 1 146 ? -5.232  -8.175  13.741  1.00 9.94   ? 146  CYS A CB  1 
ATOM   1140 S  SG  . CYS A 1 146 ? -5.623  -7.760  12.064  1.00 13.75  ? 146  CYS A SG  1 
ATOM   1141 N  N   . GLY A 1 147 ? -4.468  -5.515  14.955  1.00 8.48   ? 147  GLY A N   1 
ATOM   1142 C  CA  . GLY A 1 147 ? -4.003  -4.164  14.678  1.00 8.16   ? 147  GLY A CA  1 
ATOM   1143 C  C   . GLY A 1 147 ? -2.499  -4.121  14.753  1.00 7.67   ? 147  GLY A C   1 
ATOM   1144 O  O   . GLY A 1 147 ? -1.872  -4.992  15.360  1.00 8.85   ? 147  GLY A O   1 
ATOM   1145 N  N   . VAL A 1 148 ? -1.928  -3.085  14.149  1.00 7.57   ? 148  VAL A N   1 
ATOM   1146 C  CA  . VAL A 1 148 ? -0.498  -2.882  14.231  1.00 7.63   ? 148  VAL A CA  1 
ATOM   1147 C  C   . VAL A 1 148 ? -0.187  -2.204  15.555  1.00 8.18   ? 148  VAL A C   1 
ATOM   1148 O  O   . VAL A 1 148 ? -0.847  -1.220  15.936  1.00 10.46  ? 148  VAL A O   1 
ATOM   1149 C  CB  . VAL A 1 148 ? 0.009   -2.051  13.013  1.00 9.12   ? 148  VAL A CB  1 
ATOM   1150 C  CG1 . VAL A 1 148 ? 1.526   -1.892  13.061  1.00 10.73  ? 148  VAL A CG1 1 
ATOM   1151 C  CG2 . VAL A 1 148 ? -0.398  -2.694  11.700  1.00 11.69  ? 148  VAL A CG2 1 
ATOM   1152 N  N   . ILE A 1 149 ? 0.840   -2.680  16.238  1.00 7.81   ? 149  ILE A N   1 
ATOM   1153 C  CA  . ILE A 1 149 ? 1.264   -2.081  17.500  1.00 8.29   ? 149  ILE A CA  1 
ATOM   1154 C  C   . ILE A 1 149 ? 2.092   -0.834  17.200  1.00 8.35   ? 149  ILE A C   1 
ATOM   1155 O  O   . ILE A 1 149 ? 3.078   -0.901  16.472  1.00 9.04   ? 149  ILE A O   1 
ATOM   1156 C  CB  . ILE A 1 149 ? 2.071   -3.120  18.323  1.00 8.77   ? 149  ILE A CB  1 
ATOM   1157 C  CG1 . ILE A 1 149 ? 1.208   -4.363  18.613  1.00 9.25   ? 149  ILE A CG1 1 
ATOM   1158 C  CG2 . ILE A 1 149 ? 2.558   -2.488  19.595  1.00 9.97   ? 149  ILE A CG2 1 
ATOM   1159 C  CD1 . ILE A 1 149 ? 2.030   -5.615  19.019  1.00 10.37  ? 149  ILE A CD1 1 
ATOM   1160 N  N   . GLY A 1 150 ? 1.656   0.294   17.747  1.00 8.13   ? 150  GLY A N   1 
ATOM   1161 C  CA  . GLY A 1 150 ? 2.299   1.544   17.490  1.00 8.41   ? 150  GLY A CA  1 
ATOM   1162 C  C   . GLY A 1 150 ? 2.884   2.224   18.695  1.00 7.98   ? 150  GLY A C   1 
ATOM   1163 O  O   . GLY A 1 150 ? 2.501   1.970   19.834  1.00 9.83   ? 150  GLY A O   1 
ATOM   1164 N  N   . ILE A 1 151 ? 3.771   3.176   18.405  1.00 8.53   ? 151  ILE A N   1 
ATOM   1165 C  CA  . ILE A 1 151 ? 4.424   3.976   19.417  1.00 9.02   ? 151  ILE A CA  1 
ATOM   1166 C  C   . ILE A 1 151 ? 3.420   4.939   20.025  1.00 9.04   ? 151  ILE A C   1 
ATOM   1167 O  O   . ILE A 1 151 ? 2.683   5.598   19.323  1.00 10.10  ? 151  ILE A O   1 
ATOM   1168 C  CB  . ILE A 1 151 ? 5.608   4.755   18.824  1.00 9.68   ? 151  ILE A CB  1 
ATOM   1169 C  CG1 . ILE A 1 151 ? 6.691   3.805   18.334  1.00 10.24  ? 151  ILE A CG1 1 
ATOM   1170 C  CG2 . ILE A 1 151 ? 6.129   5.782   19.829  1.00 11.52  ? 151  ILE A CG2 1 
ATOM   1171 C  CD1 . ILE A 1 151 ? 7.740   4.439   17.500  1.00 13.91  ? 151  ILE A CD1 1 
ATOM   1172 N  N   . ALA A 1 152 ? 3.350   4.974   21.355  1.00 9.37   ? 152  ALA A N   1 
ATOM   1173 C  CA  . ALA A 1 152 ? 2.378   5.811   22.055  1.00 10.22  ? 152  ALA A CA  1 
ATOM   1174 C  C   . ALA A 1 152 ? 3.052   6.942   22.809  1.00 10.98  ? 152  ALA A C   1 
ATOM   1175 O  O   . ALA A 1 152 ? 4.240   6.879   23.138  1.00 11.91  ? 152  ALA A O   1 
ATOM   1176 C  CB  . ALA A 1 152 ? 1.516   4.961   23.013  1.00 11.27  ? 152  ALA A CB  1 
ATOM   1177 N  N   . GLN A 1 153 ? 2.243   7.960   23.071  1.00 11.75  ? 153  GLN A N   1 
ATOM   1178 C  CA  . GLN A 1 153 ? 2.636   9.141   23.811  1.00 13.15  ? 153  GLN A CA  1 
ATOM   1179 C  C   . GLN A 1 153 ? 2.874   8.855   25.252  0.70 14.01  ? 153  GLN A C   1 
ATOM   1180 O  O   . GLN A 1 153 ? 2.147   8.070   25.857  0.70 16.11  ? 153  GLN A O   1 
ATOM   1181 C  CB  . GLN A 1 153 ? 1.525   10.188  23.666  1.00 12.92  ? 153  GLN A CB  1 
ATOM   1182 C  CG  . GLN A 1 153 ? 1.821   11.531  24.282  1.00 14.21  ? 153  GLN A CG  1 
ATOM   1183 C  CD  . GLN A 1 153 ? 0.718   12.490  24.023  1.00 13.72  ? 153  GLN A CD  1 
ATOM   1184 O  OE1 . GLN A 1 153 ? 0.140   12.518  22.906  1.00 11.80  ? 153  GLN A OE1 1 
ATOM   1185 N  NE2 . GLN A 1 153 ? 0.447   13.338  25.020  1.00 14.01  ? 153  GLN A NE2 1 
ATOM   1186 O  OXT . GLN A 1 153 ? 3.801   9.448   25.810  0.70 17.44  ? 153  GLN A OXT 1 
ATOM   1187 N  N   . ALA B 2 1   ? 17.245  -6.137  2.120   1.00 23.01  ? 1    ALA F N   1 
ATOM   1188 C  CA  . ALA B 2 1   ? 16.436  -4.896  2.207   1.00 20.28  ? 1    ALA F CA  1 
ATOM   1189 C  C   . ALA B 2 1   ? 15.511  -5.017  3.389   1.00 19.04  ? 1    ALA F C   1 
ATOM   1190 O  O   . ALA B 2 1   ? 15.309  -6.107  3.916   1.00 21.26  ? 1    ALA F O   1 
ATOM   1191 C  CB  . ALA B 2 1   ? 15.630  -4.680  0.937   1.00 21.33  ? 1    ALA F CB  1 
ATOM   1192 N  N   . THR B 2 2   ? 14.959  -3.883  3.790   1.00 15.57  ? 2    THR F N   1 
ATOM   1193 C  CA  . THR B 2 2   ? 13.981  -3.786  4.857   1.00 15.53  ? 2    THR F CA  1 
ATOM   1194 C  C   . THR B 2 2   ? 12.713  -3.205  4.223   1.00 12.63  ? 2    THR F C   1 
ATOM   1195 O  O   . THR B 2 2   ? 12.784  -2.328  3.334   1.00 12.48  ? 2    THR F O   1 
ATOM   1196 C  CB  . THR B 2 2   ? 14.522  -2.813  5.918   1.00 17.17  ? 2    THR F CB  1 
ATOM   1197 O  OG1 . THR B 2 2   ? 15.744  -3.350  6.442   1.00 22.26  ? 2    THR F OG1 1 
ATOM   1198 C  CG2 . THR B 2 2   ? 13.556  -2.581  7.018   1.00 19.75  ? 2    THR F CG2 1 
ATOM   1199 N  N   . LYS B 2 3   ? 11.560  -3.708  4.632   1.00 11.60  ? 3    LYS F N   1 
ATOM   1200 C  CA  . LYS B 2 3   ? 10.289  -3.333  4.044   1.00 10.68  ? 3    LYS F CA  1 
ATOM   1201 C  C   . LYS B 2 3   ? 9.275   -2.995  5.093   1.00 9.85   ? 3    LYS F C   1 
ATOM   1202 O  O   . LYS B 2 3   ? 9.284   -3.568  6.169   1.00 10.28  ? 3    LYS F O   1 
ATOM   1203 C  CB  . LYS B 2 3   ? 9.751   -4.465  3.165   1.00 11.75  ? 3    LYS F CB  1 
ATOM   1204 C  CG  . LYS B 2 3   ? 10.634  -4.752  1.963   1.00 14.92  ? 3    LYS F CG  1 
ATOM   1205 C  CD  . LYS B 2 3   ? 10.283  -6.041  1.256   0.60 16.55  ? 3    LYS F CD  1 
ATOM   1206 C  CE  . LYS B 2 3   ? 11.370  -6.405  0.227   0.60 19.18  ? 3    LYS F CE  1 
ATOM   1207 N  NZ  . LYS B 2 3   ? 11.363  -7.859  -0.045  0.60 22.40  ? 3    LYS F NZ  1 
ATOM   1208 N  N   . ALA B 2 4   ? 8.363   -2.076  4.752   1.00 9.03   ? 4    ALA F N   1 
ATOM   1209 C  CA  . ALA B 2 4   ? 7.271   -1.715  5.649   1.00 8.61   ? 4    ALA F CA  1 
ATOM   1210 C  C   . ALA B 2 4   ? 6.041   -1.426  4.785   1.00 9.03   ? 4    ALA F C   1 
ATOM   1211 O  O   . ALA B 2 4   ? 6.132   -1.307  3.551   1.00 9.52   ? 4    ALA F O   1 
ATOM   1212 C  CB  . ALA B 2 4   ? 7.609   -0.518  6.525   1.00 9.46   ? 4    ALA F CB  1 
ATOM   1213 N  N   . VAL B 2 5   ? 4.892   -1.351  5.439   1.00 8.63   ? 5    VAL F N   1 
ATOM   1214 C  CA  . VAL B 2 5   ? 3.615   -1.183  4.737   1.00 8.60   ? 5    VAL F CA  1 
ATOM   1215 C  C   . VAL B 2 5   ? 2.644   -0.452  5.642   1.00 8.24   ? 5    VAL F C   1 
ATOM   1216 O  O   . VAL B 2 5   ? 2.756   -0.496  6.863   1.00 9.19   ? 5    VAL F O   1 
ATOM   1217 C  CB  . VAL B 2 5   ? 3.051   -2.581  4.323   1.00 9.93   ? 5    VAL F CB  1 
ATOM   1218 C  CG1 . VAL B 2 5   ? 2.750   -3.438  5.560   1.00 12.53  ? 5    VAL F CG1 1 
ATOM   1219 C  CG2 . VAL B 2 5   ? 1.852   -2.445  3.425   1.00 13.14  ? 5    VAL F CG2 1 
ATOM   1220 N  N   . CYS B 2 6   ? 1.714   0.255   5.029   1.00 8.23   ? 6    CYS F N   1 
ATOM   1221 C  CA  . CYS B 2 6   ? 0.681   0.968   5.736   1.00 8.20   ? 6    CYS F CA  1 
ATOM   1222 C  C   . CYS B 2 6   ? -0.631  0.909   4.995   1.00 8.73   ? 6    CYS F C   1 
ATOM   1223 O  O   . CYS B 2 6   ? -0.682  1.179   3.796   1.00 9.48   ? 6    CYS F O   1 
ATOM   1224 C  CB  . CYS B 2 6   ? 1.049   2.449   5.873   1.00 9.48   ? 6    CYS F CB  1 
ATOM   1225 S  SG  . CYS B 2 6   ? -0.039  3.428   6.857   1.00 11.33  ? 6    CYS F SG  1 
ATOM   1226 N  N   . VAL B 2 7   ? -1.672  0.510   5.706   1.00 8.58   ? 7    VAL F N   1 
ATOM   1227 C  CA  . VAL B 2 7   ? -3.035  0.516   5.195   1.00 9.83   ? 7    VAL F CA  1 
ATOM   1228 C  C   . VAL B 2 7   ? -3.714  1.784   5.712   1.00 9.87   ? 7    VAL F C   1 
ATOM   1229 O  O   . VAL B 2 7   ? -3.893  1.959   6.895   1.00 11.04  ? 7    VAL F O   1 
ATOM   1230 C  CB  . VAL B 2 7   ? -3.789  -0.743  5.629   1.00 10.41  ? 7    VAL F CB  1 
ATOM   1231 C  CG1 . VAL B 2 7   ? -5.232  -0.698  5.119   1.00 12.84  ? 7    VAL F CG1 1 
ATOM   1232 C  CG2 . VAL B 2 7   ? -3.071  -2.000  5.158   1.00 12.18  ? 7    VAL F CG2 1 
ATOM   1233 N  N   . LEU B 2 8   ? -4.044  2.674   4.778   1.00 10.36  ? 8    LEU F N   1 
ATOM   1234 C  CA  . LEU B 2 8   ? -4.693  3.948   5.133   1.00 10.78  ? 8    LEU F CA  1 
ATOM   1235 C  C   . LEU B 2 8   ? -6.180  3.787   5.043   1.00 11.46  ? 8    LEU F C   1 
ATOM   1236 O  O   . LEU B 2 8   ? -6.685  3.311   4.021   1.00 12.98  ? 8    LEU F O   1 
ATOM   1237 C  CB  . LEU B 2 8   ? -4.289  5.040   4.160   1.00 12.28  ? 8    LEU F CB  1 
ATOM   1238 C  CG  . LEU B 2 8   ? -2.826  5.465   4.099   1.00 12.48  ? 8    LEU F CG  1 
ATOM   1239 C  CD1 . LEU B 2 8   ? -2.586  6.365   2.849   1.00 14.05  ? 8    LEU F CD1 1 
ATOM   1240 C  CD2 . LEU B 2 8   ? -2.497  6.227   5.337   1.00 15.36  ? 8    LEU F CD2 1 
ATOM   1241 N  N   . LYS B 2 9   ? -6.877  4.189   6.097   1.00 12.16  ? 9    LYS F N   1 
ATOM   1242 C  CA  . LYS B 2 9   ? -8.353  4.133   6.142   1.00 15.02  ? 9    LYS F CA  1 
ATOM   1243 C  C   . LYS B 2 9   ? -8.891  5.365   6.821   1.00 15.95  ? 9    LYS F C   1 
ATOM   1244 O  O   . LYS B 2 9   ? -8.234  5.899   7.707   1.00 16.83  ? 9    LYS F O   1 
ATOM   1245 C  CB  . LYS B 2 9   ? -8.850  2.907   6.914   1.00 16.04  ? 9    LYS F CB  1 
ATOM   1246 C  CG  . LYS B 2 9   ? -8.532  1.630   6.226   1.00 19.52  ? 9    LYS F CG  1 
ATOM   1247 C  CD  . LYS B 2 9   ? -9.229  0.411   6.858   0.50 20.26  ? 9    LYS F CD  1 
ATOM   1248 C  CE  . LYS B 2 9   ? -9.164  -0.854  5.977   0.50 22.44  ? 9    LYS F CE  1 
ATOM   1249 N  NZ  . LYS B 2 9   ? -8.238  -1.939  6.469   0.50 22.21  ? 9    LYS F NZ  1 
ATOM   1250 N  N   A GLY B 2 10  ? -9.943  5.839   6.108   0.50 13.97  ? 10   GLY F N   1 
ATOM   1251 N  N   B GLY B 2 10  ? -10.171 5.712   6.720   0.50 18.41  ? 10   GLY F N   1 
ATOM   1252 C  CA  A GLY B 2 10  ? -10.774 6.977   6.441   0.50 12.44  ? 10   GLY F CA  1 
ATOM   1253 C  CA  B GLY B 2 10  ? -10.665 6.811   7.580   0.50 19.63  ? 10   GLY F CA  1 
ATOM   1254 C  C   A GLY B 2 10  ? -12.067 7.045   5.650   0.50 12.94  ? 10   GLY F C   1 
ATOM   1255 C  C   B GLY B 2 10  ? -12.091 6.774   8.090   0.50 20.41  ? 10   GLY F C   1 
ATOM   1256 O  O   A GLY B 2 10  ? -12.285 6.318   4.709   0.50 11.65  ? 10   GLY F O   1 
ATOM   1257 O  O   B GLY B 2 10  ? -12.711 5.714   8.162   0.50 19.79  ? 10   GLY F O   1 
ATOM   1258 N  N   A ASP B 2 11  ? -12.928 7.952   6.064   0.50 13.14  ? 11   ASP F N   1 
ATOM   1259 N  N   B ASP B 2 11  ? -12.603 7.944   8.475   0.50 21.98  ? 11   ASP F N   1 
ATOM   1260 C  CA  A ASP B 2 11  ? -14.263 8.084   5.506   0.50 15.00  ? 11   ASP F CA  1 
ATOM   1261 C  CA  B ASP B 2 11  ? -14.027 8.081   8.732   0.50 23.79  ? 11   ASP F CA  1 
ATOM   1262 C  C   A ASP B 2 11  ? -14.165 8.532   4.060   0.50 14.81  ? 11   ASP F C   1 
ATOM   1263 C  C   B ASP B 2 11  ? -14.811 7.908   7.412   0.50 24.16  ? 11   ASP F C   1 
ATOM   1264 O  O   A ASP B 2 11  ? -13.380 9.423   3.716   0.50 12.69  ? 11   ASP F O   1 
ATOM   1265 O  O   B ASP B 2 11  ? -16.029 7.673   7.425   0.50 24.71  ? 11   ASP F O   1 
ATOM   1266 C  CB  A ASP B 2 11  ? -15.050 9.067   6.349   0.50 16.35  ? 11   ASP F CB  1 
ATOM   1267 C  CB  B ASP B 2 11  ? -14.333 9.433   9.384   0.50 24.49  ? 11   ASP F CB  1 
ATOM   1268 C  CG  A ASP B 2 11  ? -15.298 8.549   7.748   0.50 20.48  ? 11   ASP F CG  1 
ATOM   1269 C  CG  B ASP B 2 11  ? -13.814 9.524   10.799  0.50 26.77  ? 11   ASP F CG  1 
ATOM   1270 O  OD1 A ASP B 2 11  ? -14.324 8.405   8.521   0.50 26.10  ? 11   ASP F OD1 1 
ATOM   1271 O  OD1 B ASP B 2 11  ? -13.974 8.531   11.547  0.50 29.66  ? 11   ASP F OD1 1 
ATOM   1272 O  OD2 A ASP B 2 11  ? -16.463 8.252   8.071   0.50 25.02  ? 11   ASP F OD2 1 
ATOM   1273 O  OD2 B ASP B 2 11  ? -13.257 10.585  11.168  0.50 31.71  ? 11   ASP F OD2 1 
ATOM   1274 N  N   A GLY B 2 12  ? -14.959 7.920   3.192   0.50 14.25  ? 12   GLY F N   1 
ATOM   1275 N  N   B GLY B 2 12  ? -14.111 8.040   6.286   0.50 24.22  ? 12   GLY F N   1 
ATOM   1276 C  CA  A GLY B 2 12  ? -15.050 8.328   1.798   0.50 15.94  ? 12   GLY F CA  1 
ATOM   1277 C  CA  B GLY B 2 12  ? -14.596 7.564   4.986   0.50 24.28  ? 12   GLY F CA  1 
ATOM   1278 C  C   A GLY B 2 12  ? -15.648 7.236   0.932   0.50 15.82  ? 12   GLY F C   1 
ATOM   1279 C  C   B GLY B 2 12  ? -14.343 8.462   3.796   0.50 23.92  ? 12   GLY F C   1 
ATOM   1280 O  O   A GLY B 2 12  ? -16.729 7.432   0.330   0.50 15.72  ? 12   GLY F O   1 
ATOM   1281 O  O   B GLY B 2 12  ? -14.015 9.649   3.961   0.50 24.99  ? 12   GLY F O   1 
ATOM   1282 N  N   A PRO B 2 13  ? -14.988 6.056   0.886   0.50 16.15  ? 13   PRO F N   1 
ATOM   1283 N  N   B PRO B 2 13  ? -14.370 7.906   2.570   0.50 22.72  ? 13   PRO F N   1 
ATOM   1284 C  CA  A PRO B 2 13  ? -13.770 5.747   1.653   0.50 16.36  ? 13   PRO F CA  1 
ATOM   1285 C  CA  B PRO B 2 13  ? -14.057 6.592   1.981   0.50 21.91  ? 13   PRO F CA  1 
ATOM   1286 C  C   A PRO B 2 13  ? -12.536 6.480   1.104   0.50 16.68  ? 13   PRO F C   1 
ATOM   1287 C  C   B PRO B 2 13  ? -12.702 6.620   1.240   0.50 19.99  ? 13   PRO F C   1 
ATOM   1288 O  O   A PRO B 2 13  ? -12.334 6.457   -0.110  0.50 17.91  ? 13   PRO F O   1 
ATOM   1289 O  O   B PRO B 2 13  ? -12.569 6.195   0.102   0.50 21.20  ? 13   PRO F O   1 
ATOM   1290 C  CB  A PRO B 2 13  ? -13.618 4.223   1.480   0.50 16.57  ? 13   PRO F CB  1 
ATOM   1291 C  CB  B PRO B 2 13  ? -15.186 6.369   0.976   0.50 22.13  ? 13   PRO F CB  1 
ATOM   1292 C  CG  A PRO B 2 13  ? -14.834 3.751   0.823   0.50 16.50  ? 13   PRO F CG  1 
ATOM   1293 C  CG  B PRO B 2 13  ? -15.846 7.704   0.801   0.50 23.03  ? 13   PRO F CG  1 
ATOM   1294 C  CD  A PRO B 2 13  ? -15.485 4.885   0.137   0.50 15.76  ? 13   PRO F CD  1 
ATOM   1295 C  CD  B PRO B 2 13  ? -15.136 8.730   1.629   0.50 23.12  ? 13   PRO F CD  1 
ATOM   1296 N  N   . VAL B 2 14  ? -11.721 7.141   1.953   1.00 17.93  ? 14   VAL F N   1 
ATOM   1297 C  CA  . VAL B 2 14  ? -10.371 7.453   1.518   1.00 15.96  ? 14   VAL F CA  1 
ATOM   1298 C  C   . VAL B 2 14  ? -9.586  6.240   1.992   1.00 15.61  ? 14   VAL F C   1 
ATOM   1299 O  O   . VAL B 2 14  ? -9.584  5.908   3.169   1.00 17.82  ? 14   VAL F O   1 
ATOM   1300 C  CB  . VAL B 2 14  ? -9.815  8.747   2.121   1.00 14.60  ? 14   VAL F CB  1 
ATOM   1301 C  CG1 . VAL B 2 14  ? -8.334  8.923   1.731   1.00 14.64  ? 14   VAL F CG1 1 
ATOM   1302 C  CG2 . VAL B 2 14  ? -10.625 9.912   1.675   1.00 16.19  ? 14   VAL F CG2 1 
ATOM   1303 N  N   . GLN B 2 15  ? -8.965  5.544   1.073   1.00 15.03  ? 15   GLN F N   1 
ATOM   1304 C  CA  . GLN B 2 15  ? -8.194  4.374   1.441   1.00 15.91  ? 15   GLN F CA  1 
ATOM   1305 C  C   . GLN B 2 15  ? -7.067  4.126   0.490   1.00 15.36  ? 15   GLN F C   1 
ATOM   1306 O  O   . GLN B 2 15  ? -7.114  4.523   -0.665  1.00 17.01  ? 15   GLN F O   1 
ATOM   1307 C  CB  . GLN B 2 15  ? -9.104  3.183   1.564   1.00 17.93  ? 15   GLN F CB  1 
ATOM   1308 C  CG  . GLN B 2 15  ? -9.760  2.783   0.335   0.60 18.30  ? 15   GLN F CG  1 
ATOM   1309 C  CD  . GLN B 2 15  ? -10.634 1.587   0.598   0.60 22.16  ? 15   GLN F CD  1 
ATOM   1310 O  OE1 . GLN B 2 15  ? -11.663 1.705   1.257   0.60 24.94  ? 15   GLN F OE1 1 
ATOM   1311 N  NE2 . GLN B 2 15  ? -10.204 0.417   0.141   0.60 24.18  ? 15   GLN F NE2 1 
ATOM   1312 N  N   . GLY B 2 16  ? -6.022  3.504   1.009   1.00 13.99  ? 16   GLY F N   1 
ATOM   1313 C  CA  . GLY B 2 16  ? -4.862  3.238   0.209   1.00 14.46  ? 16   GLY F CA  1 
ATOM   1314 C  C   . GLY B 2 16  ? -3.919  2.288   0.864   1.00 11.74  ? 16   GLY F C   1 
ATOM   1315 O  O   . GLY B 2 16  ? -4.085  2.015   2.042   1.00 14.30  ? 16   GLY F O   1 
ATOM   1316 N  N   . ILE B 2 17  ? -3.024  1.751   0.073   1.00 12.31  ? 17   ILE F N   1 
ATOM   1317 C  CA  . ILE B 2 17  ? -1.954  0.889   0.574   1.00 12.42  ? 17   ILE F CA  1 
ATOM   1318 C  C   . ILE B 2 17  ? -0.674  1.550   0.139   1.00 12.19  ? 17   ILE F C   1 
ATOM   1319 O  O   . ILE B 2 17  ? -0.483  1.837   -1.043  1.00 13.76  ? 17   ILE F O   1 
ATOM   1320 C  CB  . ILE B 2 17  ? -1.994  -0.539  -0.060  1.00 14.71  ? 17   ILE F CB  1 
ATOM   1321 C  CG1 . ILE B 2 17  ? -3.333  -1.262  0.160   1.00 17.08  ? 17   ILE F CG1 1 
ATOM   1322 C  CG2 . ILE B 2 17  ? -0.845  -1.377  0.453   1.00 17.52  ? 17   ILE F CG2 1 
ATOM   1323 C  CD1 . ILE B 2 17  ? -3.667  -1.503  1.565   1.00 17.41  ? 17   ILE F CD1 1 
ATOM   1324 N  N   . ILE B 2 18  ? 0.194   1.810   1.101   1.00 9.66   ? 18   ILE F N   1 
ATOM   1325 C  CA  . ILE B 2 18  ? 1.491   2.410   0.832   1.00 10.38  ? 18   ILE F CA  1 
ATOM   1326 C  C   . ILE B 2 18  ? 2.599   1.450   1.295   1.00 9.61   ? 18   ILE F C   1 
ATOM   1327 O  O   . ILE B 2 18  ? 2.591   0.963   2.424   1.00 10.52  ? 18   ILE F O   1 
ATOM   1328 C  CB  . ILE B 2 18  ? 1.634   3.771   1.532   1.00 9.95   ? 18   ILE F CB  1 
ATOM   1329 C  CG1 . ILE B 2 18  ? 0.515   4.746   1.113   1.00 12.14  ? 18   ILE F CG1 1 
ATOM   1330 C  CG2 . ILE B 2 18  ? 3.006   4.357   1.260   1.00 11.42  ? 18   ILE F CG2 1 
ATOM   1331 C  CD1 . ILE B 2 18  ? 0.481   5.112   -0.374  1.00 13.73  ? 18   ILE F CD1 1 
ATOM   1332 N  N   . ASN B 2 19  ? 3.532   1.198   0.389   1.00 10.21  ? 19   ASN F N   1 
ATOM   1333 C  CA  . ASN B 2 19  ? 4.664   0.320   0.601   1.00 9.29   ? 19   ASN F CA  1 
ATOM   1334 C  C   . ASN B 2 19  ? 5.916   1.129   0.755   1.00 9.71   ? 19   ASN F C   1 
ATOM   1335 O  O   . ASN B 2 19  ? 6.089   2.172   0.104   1.00 10.30  ? 19   ASN F O   1 
ATOM   1336 C  CB  . ASN B 2 19  ? 4.814   -0.621  -0.592  1.00 11.27  ? 19   ASN F CB  1 
ATOM   1337 C  CG  . ASN B 2 19  ? 3.550   -1.388  -0.864  1.00 13.95  ? 19   ASN F CG  1 
ATOM   1338 O  OD1 . ASN B 2 19  ? 3.203   -2.270  -0.126  1.00 16.77  ? 19   ASN F OD1 1 
ATOM   1339 N  ND2 . ASN B 2 19  ? 2.857   -1.041  -1.926  1.00 18.72  ? 19   ASN F ND2 1 
ATOM   1340 N  N   . PHE B 2 20  ? 6.840   0.619   1.564   1.00 9.86   ? 20   PHE F N   1 
ATOM   1341 C  CA  . PHE B 2 20  ? 8.124   1.258   1.837   1.00 9.36   ? 20   PHE F CA  1 
ATOM   1342 C  C   . PHE B 2 20  ? 9.211   0.209   1.669   1.00 10.83  ? 20   PHE F C   1 
ATOM   1343 O  O   . PHE B 2 20  ? 9.050   -0.921  2.136   1.00 10.93  ? 20   PHE F O   1 
ATOM   1344 C  CB  . PHE B 2 20  ? 8.224   1.763   3.280   1.00 10.04  ? 20   PHE F CB  1 
ATOM   1345 C  CG  . PHE B 2 20  ? 7.191   2.789   3.685   1.00 9.65   ? 20   PHE F CG  1 
ATOM   1346 C  CD1 . PHE B 2 20  ? 5.907   2.408   4.015   1.00 10.49  ? 20   PHE F CD1 1 
ATOM   1347 C  CD2 . PHE B 2 20  ? 7.501   4.134   3.708   1.00 10.95  ? 20   PHE F CD2 1 
ATOM   1348 C  CE1 . PHE B 2 20  ? 4.963   3.332   4.386   1.00 12.13  ? 20   PHE F CE1 1 
ATOM   1349 C  CE2 . PHE B 2 20  ? 6.558   5.083   4.075   1.00 12.29  ? 20   PHE F CE2 1 
ATOM   1350 C  CZ  . PHE B 2 20  ? 5.282   4.671   4.398   1.00 11.82  ? 20   PHE F CZ  1 
ATOM   1351 N  N   . GLU B 2 21  ? 10.310  0.569   1.003   1.00 11.06  ? 21   GLU F N   1 
ATOM   1352 C  CA  . GLU B 2 21  ? 11.471  -0.348  0.935   1.00 11.76  ? 21   GLU F CA  1 
ATOM   1353 C  C   . GLU B 2 21  ? 12.774  0.417   1.022   1.00 12.58  ? 21   GLU F C   1 
ATOM   1354 O  O   . GLU B 2 21  ? 12.921  1.459   0.413   1.00 13.24  ? 21   GLU F O   1 
ATOM   1355 C  CB  . GLU B 2 21  ? 11.431  -1.169  -0.351  1.00 13.28  ? 21   GLU F CB  1 
ATOM   1356 C  CG  . GLU B 2 21  ? 12.528  -2.223  -0.420  1.00 16.64  ? 21   GLU F CG  1 
ATOM   1357 C  CD  . GLU B 2 21  ? 12.213  -3.397  -1.350  1.00 22.66  ? 21   GLU F CD  1 
ATOM   1358 O  OE1 . GLU B 2 21  ? 11.071  -3.496  -1.847  0.50 22.74  ? 21   GLU F OE1 1 
ATOM   1359 O  OE2 . GLU B 2 21  ? 13.134  -4.223  -1.556  0.50 22.73  ? 21   GLU F OE2 1 
ATOM   1360 N  N   . GLN B 2 22  ? 13.707  -0.091  1.813   1.00 12.34  ? 22   GLN F N   1 
ATOM   1361 C  CA  . GLN B 2 22  ? 14.997  0.554   2.028   1.00 13.12  ? 22   GLN F CA  1 
ATOM   1362 C  C   . GLN B 2 22  ? 16.051  -0.530  1.804   1.00 15.45  ? 22   GLN F C   1 
ATOM   1363 O  O   . GLN B 2 22  ? 16.145  -1.502  2.562   1.00 14.90  ? 22   GLN F O   1 
ATOM   1364 C  CB  . GLN B 2 22  ? 15.072  1.114   3.452   1.00 11.87  ? 22   GLN F CB  1 
ATOM   1365 C  CG  . GLN B 2 22  ? 16.293  1.960   3.754   1.00 12.14  ? 22   GLN F CG  1 
ATOM   1366 C  CD  . GLN B 2 22  ? 16.284  2.516   5.162   1.00 12.49  ? 22   GLN F CD  1 
ATOM   1367 O  OE1 . GLN B 2 22  ? 15.641  1.966   6.037   1.00 14.21  ? 22   GLN F OE1 1 
ATOM   1368 N  NE2 . GLN B 2 22  ? 16.969  3.629   5.374   1.00 12.52  ? 22   GLN F NE2 1 
ATOM   1369 N  N   . LYS B 2 23  ? 16.801  -0.375  0.721   1.00 17.72  ? 23   LYS F N   1 
ATOM   1370 C  CA  . LYS B 2 23  ? 17.826  -1.355  0.376   1.00 19.90  ? 23   LYS F CA  1 
ATOM   1371 C  C   . LYS B 2 23  ? 18.892  -1.481  1.474   1.00 21.34  ? 23   LYS F C   1 
ATOM   1372 O  O   . LYS B 2 23  ? 19.355  -2.589  1.735   1.00 22.16  ? 23   LYS F O   1 
ATOM   1373 C  CB  . LYS B 2 23  ? 18.490  -0.987  -0.946  1.00 21.07  ? 23   LYS F CB  1 
ATOM   1374 C  CG  . LYS B 2 23  ? 17.730  -1.318  -2.204  0.60 23.59  ? 23   LYS F CG  1 
ATOM   1375 C  CD  . LYS B 2 23  ? 18.481  -0.824  -3.458  0.60 26.43  ? 23   LYS F CD  1 
ATOM   1376 C  CE  . LYS B 2 23  ? 17.587  -0.787  -4.698  0.60 28.21  ? 23   LYS F CE  1 
ATOM   1377 N  NZ  . LYS B 2 23  ? 17.891  0.389   -5.570  0.60 29.27  ? 23   LYS F NZ  1 
ATOM   1378 N  N   . GLU B 2 24  ? 19.340  -0.370  2.064   1.00 22.72  ? 24   GLU F N   1 
ATOM   1379 C  CA  . GLU B 2 24  ? 20.315  -0.419  3.181   1.00 23.59  ? 24   GLU F CA  1 
ATOM   1380 C  C   . GLU B 2 24  ? 20.033  0.635   4.245   1.00 23.38  ? 24   GLU F C   1 
ATOM   1381 O  O   . GLU B 2 24  ? 19.415  1.642   3.943   1.00 21.96  ? 24   GLU F O   1 
ATOM   1382 C  CB  . GLU B 2 24  ? 21.749  -0.309  2.653   1.00 24.73  ? 24   GLU F CB  1 
ATOM   1383 C  CG  . GLU B 2 24  ? 22.010  0.874   1.740   0.50 24.25  ? 24   GLU F CG  1 
ATOM   1384 C  CD  . GLU B 2 24  ? 23.201  0.654   0.815   0.10 24.10  ? 24   GLU F CD  1 
ATOM   1385 O  OE1 . GLU B 2 24  ? 24.178  -0.005  1.231   0.10 23.66  ? 24   GLU F OE1 1 
ATOM   1386 O  OE2 . GLU B 2 24  ? 23.155  1.134   -0.336  0.10 23.90  ? 24   GLU F OE2 1 
ATOM   1387 N  N   . SER B 2 25  ? 20.459  0.406   5.491   1.00 23.54  ? 25   SER F N   1 
ATOM   1388 C  CA  . SER B 2 25  ? 20.050  1.263   6.616   1.00 24.61  ? 25   SER F CA  1 
ATOM   1389 C  C   . SER B 2 25  ? 20.579  2.673   6.457   1.00 24.19  ? 25   SER F C   1 
ATOM   1390 O  O   . SER B 2 25  ? 20.009  3.627   6.977   1.00 25.23  ? 25   SER F O   1 
ATOM   1391 C  CB  . SER B 2 25  ? 20.473  0.676   7.966   1.00 25.57  ? 25   SER F CB  1 
ATOM   1392 O  OG  . SER B 2 25  ? 21.877  0.504   8.027   1.00 27.98  ? 25   SER F OG  1 
ATOM   1393 N  N   . ASN B 2 26  ? 21.661  2.803   5.703   1.00 23.22  ? 26   ASN F N   1 
ATOM   1394 C  CA  . ASN B 2 26  ? 22.231  4.120   5.425   1.00 23.12  ? 26   ASN F CA  1 
ATOM   1395 C  C   . ASN B 2 26  ? 21.633  4.763   4.153   1.00 21.44  ? 26   ASN F C   1 
ATOM   1396 O  O   . ASN B 2 26  ? 22.126  5.798   3.703   1.00 22.93  ? 26   ASN F O   1 
ATOM   1397 C  CB  . ASN B 2 26  ? 23.784  4.041   5.396   1.00 23.84  ? 26   ASN F CB  1 
ATOM   1398 C  CG  . ASN B 2 26  ? 24.326  2.798   4.693   1.00 25.79  ? 26   ASN F CG  1 
ATOM   1399 O  OD1 . ASN B 2 26  ? 23.726  1.724   4.717   0.50 25.45  ? 26   ASN F OD1 1 
ATOM   1400 N  ND2 . ASN B 2 26  ? 25.508  2.952   4.076   0.50 25.43  ? 26   ASN F ND2 1 
ATOM   1401 N  N   . GLY B 2 27  ? 20.567  4.189   3.582   1.00 18.56  ? 27   GLY F N   1 
ATOM   1402 C  CA  . GLY B 2 27  ? 20.139  4.610   2.249   1.00 17.12  ? 27   GLY F CA  1 
ATOM   1403 C  C   . GLY B 2 27  ? 18.720  5.146   2.174   1.00 16.56  ? 27   GLY F C   1 
ATOM   1404 O  O   . GLY B 2 27  ? 18.014  5.185   3.172   1.00 16.52  ? 27   GLY F O   1 
ATOM   1405 N  N   . PRO B 2 28  ? 18.327  5.593   0.992   1.00 16.26  ? 28   PRO F N   1 
ATOM   1406 C  CA  . PRO B 2 28  ? 16.993  6.133   0.842   1.00 15.92  ? 28   PRO F CA  1 
ATOM   1407 C  C   . PRO B 2 28  ? 15.895  5.080   0.907   1.00 14.29  ? 28   PRO F C   1 
ATOM   1408 O  O   . PRO B 2 28  ? 16.120  3.892   0.671   1.00 15.03  ? 28   PRO F O   1 
ATOM   1409 C  CB  . PRO B 2 28  ? 17.012  6.700   -0.564  1.00 17.58  ? 28   PRO F CB  1 
ATOM   1410 C  CG  . PRO B 2 28  ? 18.055  5.906   -1.275  1.00 19.52  ? 28   PRO F CG  1 
ATOM   1411 C  CD  . PRO B 2 28  ? 19.083  5.609   -0.274  1.00 17.30  ? 28   PRO F CD  1 
ATOM   1412 N  N   . VAL B 2 29  ? 14.689  5.571   1.165   1.00 13.43  ? 29   VAL F N   1 
ATOM   1413 C  CA  . VAL B 2 29  ? 13.497  4.747   1.244   1.00 12.17  ? 29   VAL F CA  1 
ATOM   1414 C  C   . VAL B 2 29  ? 12.618  5.060   0.042   1.00 11.96  ? 29   VAL F C   1 
ATOM   1415 O  O   . VAL B 2 29  ? 12.289  6.219   -0.212  1.00 13.61  ? 29   VAL F O   1 
ATOM   1416 C  CB  . VAL B 2 29  ? 12.725  5.017   2.564   1.00 12.05  ? 29   VAL F CB  1 
ATOM   1417 C  CG1 . VAL B 2 29  ? 11.416  4.165   2.659   1.00 12.59  ? 29   VAL F CG1 1 
ATOM   1418 C  CG2 . VAL B 2 29  ? 13.620  4.843   3.809   1.00 13.10  ? 29   VAL F CG2 1 
ATOM   1419 N  N   . LYS B 2 30  ? 12.239  4.024   -0.674  1.00 12.62  ? 30   LYS F N   1 
ATOM   1420 C  CA  . LYS B 2 30  ? 11.274  4.120   -1.748  1.00 13.16  ? 30   LYS F CA  1 
ATOM   1421 C  C   . LYS B 2 30  ? 9.882   3.917   -1.158  1.00 11.43  ? 30   LYS F C   1 
ATOM   1422 O  O   . LYS B 2 30  ? 9.688   3.045   -0.317  1.00 12.14  ? 30   LYS F O   1 
ATOM   1423 C  CB  . LYS B 2 30  ? 11.546  3.085   -2.856  1.00 15.29  ? 30   LYS F CB  1 
ATOM   1424 C  CG  . LYS B 2 30  ? 12.857  3.371   -3.581  1.00 20.01  ? 30   LYS F CG  1 
ATOM   1425 C  CD  . LYS B 2 30  ? 13.077  2.473   -4.792  1.00 24.36  ? 30   LYS F CD  1 
ATOM   1426 C  CE  . LYS B 2 30  ? 14.353  2.841   -5.534  1.00 27.87  ? 30   LYS F CE  1 
ATOM   1427 N  NZ  . LYS B 2 30  ? 14.791  1.726   -6.433  1.00 31.85  ? 30   LYS F NZ  1 
ATOM   1428 N  N   . VAL B 2 31  ? 8.958   4.780   -1.542  1.00 12.01  ? 31   VAL F N   1 
ATOM   1429 C  CA  . VAL B 2 31  ? 7.597   4.806   -1.041  1.00 11.88  ? 31   VAL F CA  1 
ATOM   1430 C  C   . VAL B 2 31  ? 6.670   4.775   -2.256  1.00 12.36  ? 31   VAL F C   1 
ATOM   1431 O  O   . VAL B 2 31  ? 6.785   5.635   -3.106  1.00 14.67  ? 31   VAL F O   1 
ATOM   1432 C  CB  . VAL B 2 31  ? 7.319   6.082   -0.220  1.00 12.51  ? 31   VAL F CB  1 
ATOM   1433 C  CG1 . VAL B 2 31  ? 5.924   6.025   0.384   1.00 12.95  ? 31   VAL F CG1 1 
ATOM   1434 C  CG2 . VAL B 2 31  ? 8.405   6.293   0.875   1.00 14.24  ? 31   VAL F CG2 1 
ATOM   1435 N  N   . TRP B 2 32  ? 5.754   3.819   -2.323  1.00 11.70  ? 32   TRP F N   1 
ATOM   1436 C  CA  . TRP B 2 32  ? 4.870   3.708   -3.472  1.00 13.04  ? 32   TRP F CA  1 
ATOM   1437 C  C   . TRP B 2 32  ? 3.546   3.087   -3.095  1.00 11.60  ? 32   TRP F C   1 
ATOM   1438 O  O   . TRP B 2 32  ? 3.426   2.296   -2.169  1.00 11.68  ? 32   TRP F O   1 
ATOM   1439 C  CB  . TRP B 2 32  ? 5.515   2.919   -4.625  1.00 13.74  ? 32   TRP F CB  1 
ATOM   1440 C  CG  . TRP B 2 32  ? 5.642   1.468   -4.409  1.00 14.30  ? 32   TRP F CG  1 
ATOM   1441 C  CD1 . TRP B 2 32  ? 4.778   0.501   -4.826  1.00 17.21  ? 32   TRP F CD1 1 
ATOM   1442 C  CD2 . TRP B 2 32  ? 6.649   0.808   -3.653  1.00 15.74  ? 32   TRP F CD2 1 
ATOM   1443 N  NE1 . TRP B 2 32  ? 5.193   -0.722  -4.395  1.00 16.76  ? 32   TRP F NE1 1 
ATOM   1444 C  CE2 . TRP B 2 32  ? 6.353   -0.571  -3.687  1.00 15.25  ? 32   TRP F CE2 1 
ATOM   1445 C  CE3 . TRP B 2 32  ? 7.784   1.239   -2.970  1.00 18.14  ? 32   TRP F CE3 1 
ATOM   1446 C  CZ2 . TRP B 2 32  ? 7.140   -1.506  -3.056  1.00 16.62  ? 32   TRP F CZ2 1 
ATOM   1447 C  CZ3 . TRP B 2 32  ? 8.567   0.311   -2.341  1.00 17.61  ? 32   TRP F CZ3 1 
ATOM   1448 C  CH2 . TRP B 2 32  ? 8.248   -1.050  -2.394  1.00 16.64  ? 32   TRP F CH2 1 
ATOM   1449 N  N   . GLY B 2 33  ? 2.542   3.454   -3.858  1.00 11.16  ? 33   GLY F N   1 
ATOM   1450 C  CA  . GLY B 2 33  ? 1.239   2.863   -3.713  1.00 12.20  ? 33   GLY F CA  1 
ATOM   1451 C  C   . GLY B 2 33  ? 0.218   3.759   -4.327  1.00 13.93  ? 33   GLY F C   1 
ATOM   1452 O  O   . GLY B 2 33  ? 0.543   4.535   -5.219  1.00 15.05  ? 33   GLY F O   1 
ATOM   1453 N  N   A SER B 2 34  ? -0.997  3.666   -3.803  0.50 15.37  ? 34   SER F N   1 
ATOM   1454 N  N   B SER B 2 34  ? -1.009  3.622   -3.879  0.50 14.96  ? 34   SER F N   1 
ATOM   1455 C  CA  A SER B 2 34  ? -2.195  4.240   -4.417  0.50 15.79  ? 34   SER F CA  1 
ATOM   1456 C  CA  B SER B 2 34  ? -2.074  4.462   -4.362  0.50 14.99  ? 34   SER F CA  1 
ATOM   1457 C  C   A SER B 2 34  ? -3.223  4.612   -3.337  0.50 15.71  ? 34   SER F C   1 
ATOM   1458 C  C   B SER B 2 34  ? -3.028  4.750   -3.227  0.50 15.16  ? 34   SER F C   1 
ATOM   1459 O  O   A SER B 2 34  ? -3.505  3.822   -2.437  0.50 15.70  ? 34   SER F O   1 
ATOM   1460 O  O   B SER B 2 34  ? -3.053  4.057   -2.197  0.50 14.38  ? 34   SER F O   1 
ATOM   1461 C  CB  A SER B 2 34  ? -2.797  3.228   -5.407  0.50 16.30  ? 34   SER F CB  1 
ATOM   1462 C  CB  B SER B 2 34  ? -2.821  3.795   -5.517  0.50 15.28  ? 34   SER F CB  1 
ATOM   1463 O  OG  A SER B 2 34  ? -3.976  3.714   -6.010  0.50 19.08  ? 34   SER F OG  1 
ATOM   1464 O  OG  B SER B 2 34  ? -3.496  2.641   -5.053  0.50 17.19  ? 34   SER F OG  1 
ATOM   1465 N  N   . ILE B 2 35  ? -3.786  5.817   -3.433  1.00 14.70  ? 35   ILE F N   1 
ATOM   1466 C  CA  . ILE B 2 35  ? -4.802  6.248   -2.495  1.00 13.59  ? 35   ILE F CA  1 
ATOM   1467 C  C   . ILE B 2 35  ? -6.003  6.664   -3.324  1.00 14.15  ? 35   ILE F C   1 
ATOM   1468 O  O   . ILE B 2 35  ? -5.886  7.481   -4.243  1.00 14.45  ? 35   ILE F O   1 
ATOM   1469 C  CB  . ILE B 2 35  ? -4.350  7.430   -1.636  1.00 13.44  ? 35   ILE F CB  1 
ATOM   1470 C  CG1 . ILE B 2 35  ? -2.996  7.152   -0.994  1.00 13.36  ? 35   ILE F CG1 1 
ATOM   1471 C  CG2 . ILE B 2 35  ? -5.435  7.754   -0.617  1.00 12.99  ? 35   ILE F CG2 1 
ATOM   1472 C  CD1 . ILE B 2 35  ? -2.412  8.326   -0.298  1.00 15.18  ? 35   ILE F CD1 1 
ATOM   1473 N  N   . LYS B 2 36  ? -7.165  6.139   -2.952  1.00 14.04  ? 36   LYS F N   1 
ATOM   1474 C  CA  . LYS B 2 36  ? -8.406  6.433   -3.676  1.00 15.30  ? 36   LYS F CA  1 
ATOM   1475 C  C   . LYS B 2 36  ? -9.381  7.182   -2.777  1.00 14.81  ? 36   LYS F C   1 
ATOM   1476 O  O   . LYS B 2 36  ? -9.221  7.253   -1.543  1.00 14.76  ? 36   LYS F O   1 
ATOM   1477 C  CB  . LYS B 2 36  ? -9.035  5.150   -4.238  1.00 16.04  ? 36   LYS F CB  1 
ATOM   1478 C  CG  . LYS B 2 36  ? -9.627  4.217   -3.223  1.00 19.58  ? 36   LYS F CG  1 
ATOM   1479 C  CD  . LYS B 2 36  ? -10.010 2.914   -3.949  1.00 23.70  ? 36   LYS F CD  1 
ATOM   1480 C  CE  . LYS B 2 36  ? -10.578 1.829   -3.039  1.00 27.15  ? 36   LYS F CE  1 
ATOM   1481 N  NZ  . LYS B 2 36  ? -11.202 0.723   -3.864  1.00 29.39  ? 36   LYS F NZ  1 
ATOM   1482 N  N   . GLY B 2 37  ? -10.411 7.750   -3.398  1.00 15.08  ? 37   GLY F N   1 
ATOM   1483 C  CA  . GLY B 2 37  ? -11.475 8.412   -2.680  1.00 15.13  ? 37   GLY F CA  1 
ATOM   1484 C  C   . GLY B 2 37  ? -11.199 9.859   -2.319  1.00 14.42  ? 37   GLY F C   1 
ATOM   1485 O  O   . GLY B 2 37  ? -11.963 10.471  -1.572  1.00 15.63  ? 37   GLY F O   1 
ATOM   1486 N  N   . LEU B 2 38  ? -10.121 10.419  -2.869  1.00 14.00  ? 38   LEU F N   1 
ATOM   1487 C  CA  . LEU B 2 38  ? -9.704  11.781  -2.598  1.00 13.61  ? 38   LEU F CA  1 
ATOM   1488 C  C   . LEU B 2 38  ? -10.377 12.800  -3.531  1.00 13.81  ? 38   LEU F C   1 
ATOM   1489 O  O   . LEU B 2 38  ? -10.683 12.514  -4.682  1.00 15.95  ? 38   LEU F O   1 
ATOM   1490 C  CB  . LEU B 2 38  ? -8.203  11.894  -2.806  1.00 14.24  ? 38   LEU F CB  1 
ATOM   1491 C  CG  . LEU B 2 38  ? -7.334  11.122  -1.810  1.00 13.28  ? 38   LEU F CG  1 
ATOM   1492 C  CD1 . LEU B 2 38  ? -5.906  11.072  -2.303  1.00 13.31  ? 38   LEU F CD1 1 
ATOM   1493 C  CD2 . LEU B 2 38  ? -7.369  11.823  -0.442  1.00 14.25  ? 38   LEU F CD2 1 
ATOM   1494 N  N   . THR B 2 39  ? -10.558 14.015  -3.047  1.00 13.66  ? 39   THR F N   1 
ATOM   1495 C  CA  . THR B 2 39  ? -10.949 15.130  -3.907  1.00 14.01  ? 39   THR F CA  1 
ATOM   1496 C  C   . THR B 2 39  ? -9.765  15.503  -4.817  1.00 14.03  ? 39   THR F C   1 
ATOM   1497 O  O   . THR B 2 39  ? -8.596  15.288  -4.480  1.00 14.63  ? 39   THR F O   1 
ATOM   1498 C  CB  . THR B 2 39  ? -11.367 16.389  -3.107  1.00 14.65  ? 39   THR F CB  1 
ATOM   1499 O  OG1 . THR B 2 39  ? -10.294 16.801  -2.252  1.00 16.77  ? 39   THR F OG1 1 
ATOM   1500 C  CG2 . THR B 2 39  ? -12.594 16.140  -2.238  1.00 16.74  ? 39   THR F CG2 1 
ATOM   1501 N  N   . GLU B 2 40  ? -10.063 16.046  -5.994  1.00 13.96  ? 40   GLU F N   1 
ATOM   1502 C  CA  . GLU B 2 40  ? -9.012  16.410  -6.958  1.00 13.58  ? 40   GLU F CA  1 
ATOM   1503 C  C   . GLU B 2 40  ? -8.110  17.482  -6.362  1.00 13.80  ? 40   GLU F C   1 
ATOM   1504 O  O   . GLU B 2 40  ? -8.594  18.450  -5.787  1.00 15.87  ? 40   GLU F O   1 
ATOM   1505 C  CB  . GLU B 2 40  ? -9.654  16.934  -8.251  1.00 14.25  ? 40   GLU F CB  1 
ATOM   1506 C  CG  . GLU B 2 40  ? -8.678  17.294  -9.383  1.00 15.84  ? 40   GLU F CG  1 
ATOM   1507 C  CD  . GLU B 2 40  ? -9.343  17.962  -10.537 0.70 15.34  ? 40   GLU F CD  1 
ATOM   1508 O  OE1 . GLU B 2 40  ? -10.411 18.602  -10.349 0.50 14.42  ? 40   GLU F OE1 1 
ATOM   1509 O  OE2 . GLU B 2 40  ? -8.778  17.844  -11.642 1.00 18.86  ? 40   GLU F OE2 1 
ATOM   1510 N  N   . GLY B 2 41  ? -6.810  17.314  -6.517  1.00 12.01  ? 41   GLY F N   1 
ATOM   1511 C  CA  . GLY B 2 41  ? -5.844  18.271  -6.040  1.00 11.74  ? 41   GLY F CA  1 
ATOM   1512 C  C   . GLY B 2 41  ? -4.857  17.684  -5.075  1.00 11.10  ? 41   GLY F C   1 
ATOM   1513 O  O   . GLY B 2 41  ? -4.680  16.456  -4.988  1.00 11.84  ? 41   GLY F O   1 
ATOM   1514 N  N   . LEU B 2 42  ? -4.159  18.574  -4.386  1.00 10.61  ? 42   LEU F N   1 
ATOM   1515 C  CA  . LEU B 2 42  ? -3.102  18.182  -3.478  1.00 10.61  ? 42   LEU F CA  1 
ATOM   1516 C  C   . LEU B 2 42  ? -3.641  17.806  -2.104  1.00 10.14  ? 42   LEU F C   1 
ATOM   1517 O  O   . LEU B 2 42  ? -4.516  18.466  -1.571  1.00 10.92  ? 42   LEU F O   1 
ATOM   1518 C  CB  . LEU B 2 42  ? -2.087  19.316  -3.297  1.00 11.10  ? 42   LEU F CB  1 
ATOM   1519 C  CG  . LEU B 2 42  ? -0.997  19.513  -4.335  1.00 11.86  ? 42   LEU F CG  1 
ATOM   1520 C  CD1 . LEU B 2 42  ? -1.557  19.771  -5.695  1.00 14.60  ? 42   LEU F CD1 1 
ATOM   1521 C  CD2 . LEU B 2 42  ? -0.057  20.625  -3.895  1.00 13.13  ? 42   LEU F CD2 1 
ATOM   1522 N  N   . HIS B 2 43  ? -3.004  16.802  -1.515  1.00 9.95   ? 43   HIS F N   1 
ATOM   1523 C  CA  . HIS B 2 43  ? -3.296  16.399  -0.141  1.00 9.47   ? 43   HIS F CA  1 
ATOM   1524 C  C   . HIS B 2 43  ? -1.993  16.188  0.611   1.00 9.38   ? 43   HIS F C   1 
ATOM   1525 O  O   . HIS B 2 43  ? -1.157  15.384  0.216   1.00 10.34  ? 43   HIS F O   1 
ATOM   1526 C  CB  . HIS B 2 43  ? -4.122  15.090  -0.157  1.00 10.38  ? 43   HIS F CB  1 
ATOM   1527 C  CG  . HIS B 2 43  ? -5.453  15.272  -0.808  1.00 10.66  ? 43   HIS F CG  1 
ATOM   1528 N  ND1 . HIS B 2 43  ? -6.552  15.667  -0.084  1.00 12.46  ? 43   HIS F ND1 1 
ATOM   1529 C  CD2 . HIS B 2 43  ? -5.846  15.213  -2.104  1.00 12.30  ? 43   HIS F CD2 1 
ATOM   1530 C  CE1 . HIS B 2 43  ? -7.576  15.843  -0.906  1.00 13.44  ? 43   HIS F CE1 1 
ATOM   1531 N  NE2 . HIS B 2 43  ? -7.181  15.567  -2.138  1.00 12.45  ? 43   HIS F NE2 1 
ATOM   1532 N  N   . GLY B 2 44  ? -1.856  16.857  1.741   1.00 9.75   ? 44   GLY F N   1 
ATOM   1533 C  CA  . GLY B 2 44  ? -0.662  16.688  2.585   1.00 9.77   ? 44   GLY F CA  1 
ATOM   1534 C  C   . GLY B 2 44  ? -0.470  15.240  2.977   1.00 8.79   ? 44   GLY F C   1 
ATOM   1535 O  O   . GLY B 2 44  ? -1.439  14.524  3.217   1.00 9.31   ? 44   GLY F O   1 
ATOM   1536 N  N   . PHE B 2 45  ? 0.788   14.834  3.058   1.00 9.23   ? 45   PHE F N   1 
ATOM   1537 C  CA  . PHE B 2 45  ? 1.146   13.436  3.267   1.00 9.02   ? 45   PHE F CA  1 
ATOM   1538 C  C   . PHE B 2 45  ? 2.334   13.385  4.193   1.00 8.81   ? 45   PHE F C   1 
ATOM   1539 O  O   . PHE B 2 45  ? 3.431   13.795  3.823   1.00 9.81   ? 45   PHE F O   1 
ATOM   1540 C  CB  . PHE B 2 45  ? 1.518   12.898  1.892   1.00 9.19   ? 45   PHE F CB  1 
ATOM   1541 C  CG  . PHE B 2 45  ? 1.731   11.403  1.798   1.00 9.32   ? 45   PHE F CG  1 
ATOM   1542 C  CD1 . PHE B 2 45  ? 0.721   10.522  2.105   1.00 11.15  ? 45   PHE F CD1 1 
ATOM   1543 C  CD2 . PHE B 2 45  ? 2.888   10.902  1.254   1.00 12.28  ? 45   PHE F CD2 1 
ATOM   1544 C  CE1 . PHE B 2 45  ? 0.917   9.155   1.984   1.00 13.00  ? 45   PHE F CE1 1 
ATOM   1545 C  CE2 . PHE B 2 45  ? 3.091   9.530   1.120   1.00 13.00  ? 45   PHE F CE2 1 
ATOM   1546 C  CZ  . PHE B 2 45  ? 2.097   8.676   1.433   1.00 12.88  ? 45   PHE F CZ  1 
ATOM   1547 N  N   . HIS B 2 46  ? 2.128   12.916  5.428   1.00 7.79   ? 46   HIS F N   1 
ATOM   1548 C  CA  . HIS B 2 46  ? 3.161   12.967  6.441   1.00 8.52   ? 46   HIS F CA  1 
ATOM   1549 C  C   . HIS B 2 46  ? 3.168   11.756  7.340   1.00 7.54   ? 46   HIS F C   1 
ATOM   1550 O  O   . HIS B 2 46  ? 2.149   11.144  7.570   1.00 8.47   ? 46   HIS F O   1 
ATOM   1551 C  CB  . HIS B 2 46  ? 3.012   14.170  7.382   1.00 10.08  ? 46   HIS F CB  1 
ATOM   1552 C  CG  . HIS B 2 46  ? 2.556   15.406  6.717   1.00 10.03  ? 46   HIS F CG  1 
ATOM   1553 N  ND1 . HIS B 2 46  ? 1.283   15.875  6.898   1.00 12.20  ? 46   HIS F ND1 1 
ATOM   1554 C  CD2 . HIS B 2 46  ? 3.176   16.259  5.878   1.00 10.43  ? 46   HIS F CD2 1 
ATOM   1555 C  CE1 . HIS B 2 46  ? 1.134   16.973  6.194   1.00 11.20  ? 46   HIS F CE1 1 
ATOM   1556 N  NE2 . HIS B 2 46  ? 2.262   17.227  5.554   1.00 11.13  ? 46   HIS F NE2 1 
ATOM   1557 N  N   . VAL B 2 47  ? 4.345   11.476  7.871   1.00 7.81   ? 47   VAL F N   1 
ATOM   1558 C  CA  . VAL B 2 47  ? 4.465   10.590  9.002   1.00 6.83   ? 47   VAL F CA  1 
ATOM   1559 C  C   . VAL B 2 47  ? 4.303   11.406  10.299  1.00 6.97   ? 47   VAL F C   1 
ATOM   1560 O  O   . VAL B 2 47  ? 5.036   12.399  10.495  1.00 8.42   ? 47   VAL F O   1 
ATOM   1561 C  CB  . VAL B 2 47  ? 5.802   9.832   9.020   1.00 7.42   ? 47   VAL F CB  1 
ATOM   1562 C  CG1 . VAL B 2 47  ? 5.872   8.858   10.194  1.00 9.24   ? 47   VAL F CG1 1 
ATOM   1563 C  CG2 . VAL B 2 47  ? 6.002   9.096   7.705   1.00 9.32   ? 47   VAL F CG2 1 
ATOM   1564 N  N   . HIS B 2 48  ? 3.360   11.001  11.155  1.00 7.78   ? 48   HIS F N   1 
ATOM   1565 C  CA  . HIS B 2 48  ? 3.114   11.639  12.425  1.00 7.98   ? 48   HIS F CA  1 
ATOM   1566 C  C   . HIS B 2 48  ? 3.797   10.843  13.502  1.00 9.12   ? 48   HIS F C   1 
ATOM   1567 O  O   . HIS B 2 48  ? 4.120   9.681   13.325  1.00 11.76  ? 48   HIS F O   1 
ATOM   1568 C  CB  . HIS B 2 48  ? 1.603   11.785  12.646  1.00 8.44   ? 48   HIS F CB  1 
ATOM   1569 C  CG  . HIS B 2 48  ? 0.993   12.830  11.778  1.00 7.92   ? 48   HIS F CG  1 
ATOM   1570 N  ND1 . HIS B 2 48  ? 0.321   13.914  12.279  1.00 8.83   ? 48   HIS F ND1 1 
ATOM   1571 C  CD2 . HIS B 2 48  ? 0.941   12.945  10.427  1.00 9.91   ? 48   HIS F CD2 1 
ATOM   1572 C  CE1 . HIS B 2 48  ? -0.115  14.660  11.271  1.00 8.58   ? 48   HIS F CE1 1 
ATOM   1573 N  NE2 . HIS B 2 48  ? 0.228   14.091  10.135  1.00 10.32  ? 48   HIS F NE2 1 
ATOM   1574 N  N   . GLU B 2 49  ? 3.965   11.449  14.673  1.00 9.22   ? 49   GLU F N   1 
ATOM   1575 C  CA  . GLU B 2 49  ? 4.836   10.921  15.732  1.00 9.93   ? 49   GLU F CA  1 
ATOM   1576 C  C   . GLU B 2 49  ? 4.352   9.590   16.315  1.00 9.70   ? 49   GLU F C   1 
ATOM   1577 O  O   . GLU B 2 49  ? 5.146   8.677   16.522  1.00 11.39  ? 49   GLU F O   1 
ATOM   1578 C  CB  . GLU B 2 49  ? 4.922   11.956  16.839  1.00 11.36  ? 49   GLU F CB  1 
ATOM   1579 C  CG  . GLU B 2 49  ? 5.850   11.532  17.902  1.00 13.53  ? 49   GLU F CG  1 
ATOM   1580 C  CD  . GLU B 2 49  ? 5.965   12.522  19.031  0.50 13.70  ? 49   GLU F CD  1 
ATOM   1581 O  OE1 . GLU B 2 49  ? 5.222   13.524  19.041  0.70 17.60  ? 49   GLU F OE1 1 
ATOM   1582 O  OE2 . GLU B 2 49  ? 6.809   12.289  19.914  0.50 15.06  ? 49   GLU F OE2 1 
ATOM   1583 N  N   . PHE B 2 50  ? 3.083   9.461   16.610  1.00 9.31   ? 50   PHE F N   1 
ATOM   1584 C  CA  . PHE B 2 50  ? 2.602   8.305   17.328  1.00 8.99   ? 50   PHE F CA  1 
ATOM   1585 C  C   . PHE B 2 50  ? 1.849   7.350   16.444  1.00 9.47   ? 50   PHE F C   1 
ATOM   1586 O  O   . PHE B 2 50  ? 1.125   7.747   15.553  1.00 11.23  ? 50   PHE F O   1 
ATOM   1587 C  CB  . PHE B 2 50  ? 1.697   8.720   18.468  1.00 9.79   ? 50   PHE F CB  1 
ATOM   1588 C  CG  . PHE B 2 50  ? 2.273   9.768   19.356  1.00 11.64  ? 50   PHE F CG  1 
ATOM   1589 C  CD1 . PHE B 2 50  ? 3.477   9.591   19.999  1.00 13.66  ? 50   PHE F CD1 1 
ATOM   1590 C  CD2 . PHE B 2 50  ? 1.589   10.964  19.533  1.00 12.51  ? 50   PHE F CD2 1 
ATOM   1591 C  CE1 . PHE B 2 50  ? 3.997   10.593  20.795  1.00 15.77  ? 50   PHE F CE1 1 
ATOM   1592 C  CE2 . PHE B 2 50  ? 2.123   11.970  20.319  1.00 14.52  ? 50   PHE F CE2 1 
ATOM   1593 C  CZ  . PHE B 2 50  ? 3.324   11.780  20.942  1.00 14.10  ? 50   PHE F CZ  1 
ATOM   1594 N  N   . GLY B 2 51  ? 2.030   6.072   16.702  1.00 8.90   ? 51   GLY F N   1 
ATOM   1595 C  CA  . GLY B 2 51  ? 1.267   5.026   16.039  1.00 9.54   ? 51   GLY F CA  1 
ATOM   1596 C  C   . GLY B 2 51  ? 0.019   4.678   16.826  1.00 10.33  ? 51   GLY F C   1 
ATOM   1597 O  O   . GLY B 2 51  ? -0.323  3.520   17.015  1.00 12.14  ? 51   GLY F O   1 
ATOM   1598 N  N   . ASP B 2 52  ? -0.656  5.699   17.295  1.00 11.80  ? 52   ASP F N   1 
ATOM   1599 C  CA  . ASP B 2 52  ? -1.826  5.587   18.165  1.00 11.23  ? 52   ASP F CA  1 
ATOM   1600 C  C   . ASP B 2 52  ? -3.042  6.037   17.403  1.00 10.69  ? 52   ASP F C   1 
ATOM   1601 O  O   . ASP B 2 52  ? -3.101  7.193   16.982  1.00 12.01  ? 52   ASP F O   1 
ATOM   1602 C  CB  . ASP B 2 52  ? -1.618  6.435   19.414  1.00 12.26  ? 52   ASP F CB  1 
ATOM   1603 C  CG  . ASP B 2 52  ? -2.704  6.255   20.454  1.00 12.79  ? 52   ASP F CG  1 
ATOM   1604 O  OD1 . ASP B 2 52  ? -3.739  5.629   20.149  1.00 13.74  ? 52   ASP F OD1 1 
ATOM   1605 O  OD2 . ASP B 2 52  ? -2.512  6.692   21.604  1.00 15.73  ? 52   ASP F OD2 1 
ATOM   1606 N  N   A ASN B 2 53  ? -3.980  5.135   17.163  0.50 11.44  ? 53   ASN F N   1 
ATOM   1607 N  N   B ASN B 2 53  ? -3.985  5.106   17.182  0.50 11.63  ? 53   ASN F N   1 
ATOM   1608 C  CA  A ASN B 2 53  ? -5.201  5.490   16.498  0.50 11.59  ? 53   ASN F CA  1 
ATOM   1609 C  CA  B ASN B 2 53  ? -5.261  5.330   16.486  0.50 11.66  ? 53   ASN F CA  1 
ATOM   1610 C  C   A ASN B 2 53  ? -6.413  5.206   17.420  0.50 11.33  ? 53   ASN F C   1 
ATOM   1611 C  C   B ASN B 2 53  ? -6.456  5.250   17.440  0.50 11.38  ? 53   ASN F C   1 
ATOM   1612 O  O   A ASN B 2 53  ? -7.508  4.954   16.932  0.50 12.65  ? 53   ASN F O   1 
ATOM   1613 O  O   B ASN B 2 53  ? -7.594  5.194   16.996  0.50 12.06  ? 53   ASN F O   1 
ATOM   1614 C  CB  A ASN B 2 53  ? -5.295  4.811   15.118  0.50 11.51  ? 53   ASN F CB  1 
ATOM   1615 C  CB  B ASN B 2 53  ? -5.468  4.316   15.345  0.50 12.54  ? 53   ASN F CB  1 
ATOM   1616 C  CG  A ASN B 2 53  ? -4.145  5.205   14.147  0.50 12.97  ? 53   ASN F CG  1 
ATOM   1617 C  CG  B ASN B 2 53  ? -6.637  4.694   14.417  0.50 14.04  ? 53   ASN F CG  1 
ATOM   1618 O  OD1 A ASN B 2 53  ? -3.351  6.129   14.391  0.50 15.23  ? 53   ASN F OD1 1 
ATOM   1619 O  OD1 B ASN B 2 53  ? -7.489  3.858   14.084  0.50 18.32  ? 53   ASN F OD1 1 
ATOM   1620 N  ND2 A ASN B 2 53  ? -4.065  4.502   13.039  0.50 14.74  ? 53   ASN F ND2 1 
ATOM   1621 N  ND2 B ASN B 2 53  ? -6.663  5.949   13.983  0.50 14.11  ? 53   ASN F ND2 1 
ATOM   1622 N  N   . THR B 2 54  ? -6.210  5.300   18.746  1.00 11.29  ? 54   THR F N   1 
ATOM   1623 C  CA  . THR B 2 54  ? -7.262  5.074   19.747  1.00 12.83  ? 54   THR F CA  1 
ATOM   1624 C  C   . THR B 2 54  ? -8.534  5.853   19.458  1.00 13.50  ? 54   THR F C   1 
ATOM   1625 O  O   . THR B 2 54  ? -9.641  5.297   19.468  1.00 15.22  ? 54   THR F O   1 
ATOM   1626 C  CB  . THR B 2 54  ? -6.767  5.419   21.166  1.00 12.84  ? 54   THR F CB  1 
ATOM   1627 O  OG1 . THR B 2 54  ? -5.709  4.526   21.511  1.00 15.32  ? 54   THR F OG1 1 
ATOM   1628 C  CG2 . THR B 2 54  ? -7.873  5.312   22.243  1.00 15.24  ? 54   THR F CG2 1 
ATOM   1629 N  N   . ALA B 2 55  ? -8.375  7.137   19.197  1.00 13.60  ? 55   ALA F N   1 
ATOM   1630 C  CA  . ALA B 2 55  ? -9.531  8.007   18.957  1.00 14.97  ? 55   ALA F CA  1 
ATOM   1631 C  C   . ALA B 2 55  ? -9.583  8.476   17.520  1.00 14.85  ? 55   ALA F C   1 
ATOM   1632 O  O   . ALA B 2 55  ? -10.146 9.515   17.235  1.00 18.57  ? 55   ALA F O   1 
ATOM   1633 C  CB  . ALA B 2 55  ? -9.500  9.187   19.917  1.00 16.77  ? 55   ALA F CB  1 
ATOM   1634 N  N   . GLY B 2 56  ? -8.976  7.706   16.632  1.00 14.01  ? 56   GLY F N   1 
ATOM   1635 C  CA  . GLY B 2 56  ? -8.834  8.026   15.224  1.00 13.67  ? 56   GLY F CA  1 
ATOM   1636 C  C   . GLY B 2 56  ? -7.492  8.702   14.942  1.00 11.67  ? 56   GLY F C   1 
ATOM   1637 O  O   . GLY B 2 56  ? -6.569  8.642   15.758  1.00 12.05  ? 56   GLY F O   1 
ATOM   1638 N  N   . CYS B 2 57  ? -7.418  9.346   13.774  1.00 11.82  ? 57   CYS F N   1 
ATOM   1639 C  CA  . CYS B 2 57  ? -6.158  9.898   13.303  1.00 11.46  ? 57   CYS F CA  1 
ATOM   1640 C  C   . CYS B 2 57  ? -5.617  11.023  14.156  1.00 10.67  ? 57   CYS F C   1 
ATOM   1641 O  O   . CYS B 2 57  ? -4.418  11.256  14.149  1.00 10.53  ? 57   CYS F O   1 
ATOM   1642 C  CB  . CYS B 2 57  ? -6.251  10.359  11.856  1.00 12.26  ? 57   CYS F CB  1 
ATOM   1643 S  SG  . CYS B 2 57  ? -6.779  9.081   10.675  1.00 16.62  ? 57   CYS F SG  1 
ATOM   1644 N  N   A THR B 2 58  ? -6.490  11.698  14.902  0.50 11.30  ? 58   THR F N   1 
ATOM   1645 N  N   B THR B 2 58  ? -6.450  11.723  14.917  0.50 11.83  ? 58   THR F N   1 
ATOM   1646 C  CA  A THR B 2 58  ? -6.072  12.732  15.830  0.50 11.20  ? 58   THR F CA  1 
ATOM   1647 C  CA  B THR B 2 58  ? -5.926  12.763  15.789  0.50 12.30  ? 58   THR F CA  1 
ATOM   1648 C  C   A THR B 2 58  ? -5.054  12.227  16.861  0.50 10.45  ? 58   THR F C   1 
ATOM   1649 C  C   B THR B 2 58  ? -4.942  12.203  16.816  0.50 10.87  ? 58   THR F C   1 
ATOM   1650 O  O   A THR B 2 58  ? -4.220  12.983  17.305  0.50 10.49  ? 58   THR F O   1 
ATOM   1651 O  O   B THR B 2 58  ? -3.996  12.885  17.193  0.50 10.35  ? 58   THR F O   1 
ATOM   1652 C  CB  A THR B 2 58  ? -7.275  13.382  16.551  0.50 11.63  ? 58   THR F CB  1 
ATOM   1653 C  CB  B THR B 2 58  ? -7.035  13.534  16.492  0.50 13.26  ? 58   THR F CB  1 
ATOM   1654 O  OG1 A THR B 2 58  ? -6.800  14.475  17.369  0.50 12.70  ? 58   THR F OG1 1 
ATOM   1655 O  OG1 B THR B 2 58  ? -7.555  12.760  17.571  0.50 16.54  ? 58   THR F OG1 1 
ATOM   1656 C  CG2 A THR B 2 58  ? -8.084  12.318  17.348  0.50 12.78  ? 58   THR F CG2 1 
ATOM   1657 C  CG2 B THR B 2 58  ? -8.124  13.843  15.500  0.50 14.51  ? 58   THR F CG2 1 
ATOM   1658 N  N   . SER B 2 59  ? -5.129  10.945  17.228  1.00 10.77  ? 59   SER F N   1 
ATOM   1659 C  CA  . SER B 2 59  ? -4.319  10.367  18.276  1.00 11.12  ? 59   SER F CA  1 
ATOM   1660 C  C   . SER B 2 59  ? -2.848  10.254  17.833  1.00 9.76   ? 59   SER F C   1 
ATOM   1661 O  O   . SER B 2 59  ? -1.962  10.081  18.659  1.00 11.19  ? 59   SER F O   1 
ATOM   1662 C  CB  . SER B 2 59  ? -4.894  8.985   18.682  1.00 10.49  ? 59   SER F CB  1 
ATOM   1663 O  OG  . SER B 2 59  ? -6.186  9.095   19.281  1.00 13.20  ? 59   SER F OG  1 
ATOM   1664 N  N   . ALA B 2 60  ? -2.589  10.354  16.521  1.00 10.01  ? 60   ALA F N   1 
ATOM   1665 C  CA  . ALA B 2 60  ? -1.226  10.248  15.985  1.00 9.43   ? 60   ALA F CA  1 
ATOM   1666 C  C   . ALA B 2 60  ? -0.335  11.438  16.328  1.00 8.46   ? 60   ALA F C   1 
ATOM   1667 O  O   . ALA B 2 60  ? 0.852   11.376  16.147  1.00 9.87   ? 60   ALA F O   1 
ATOM   1668 C  CB  . ALA B 2 60  ? -1.283  10.068  14.489  1.00 10.13  ? 60   ALA F CB  1 
ATOM   1669 N  N   . GLY B 2 61  ? -0.904  12.530  16.813  1.00 8.79   ? 61   GLY F N   1 
ATOM   1670 C  CA  . GLY B 2 61  ? -0.052  13.651  17.258  1.00 9.51   ? 61   GLY F CA  1 
ATOM   1671 C  C   . GLY B 2 61  ? 0.456   14.466  16.101  1.00 9.19   ? 61   GLY F C   1 
ATOM   1672 O  O   . GLY B 2 61  ? -0.083  14.416  14.981  1.00 9.06   ? 61   GLY F O   1 
ATOM   1673 N  N   . PRO B 2 62  ? 1.527   15.218  16.329  1.00 8.89   ? 62   PRO F N   1 
ATOM   1674 C  CA  . PRO B 2 62  ? 2.074   16.115  15.323  1.00 9.32   ? 62   PRO F CA  1 
ATOM   1675 C  C   . PRO B 2 62  ? 2.957   15.370  14.321  1.00 8.81   ? 62   PRO F C   1 
ATOM   1676 O  O   . PRO B 2 62  ? 3.135   14.166  14.454  1.00 8.68   ? 62   PRO F O   1 
ATOM   1677 C  CB  . PRO B 2 62  ? 2.912   17.061  16.163  1.00 10.30  ? 62   PRO F CB  1 
ATOM   1678 C  CG  . PRO B 2 62  ? 3.416   16.238  17.271  1.00 11.22  ? 62   PRO F CG  1 
ATOM   1679 C  CD  . PRO B 2 62  ? 2.287   15.300  17.590  1.00 10.65  ? 62   PRO F CD  1 
ATOM   1680 N  N   . HIS B 2 63  ? 3.502   16.074  13.336  1.00 8.23   ? 63   HIS F N   1 
ATOM   1681 C  CA  . HIS B 2 63  ? 4.428   15.454  12.421  1.00 8.40   ? 63   HIS F CA  1 
ATOM   1682 C  C   . HIS B 2 63  ? 5.622   14.883  13.185  1.00 7.72   ? 63   HIS F C   1 
ATOM   1683 O  O   . HIS B 2 63  ? 6.099   15.501  14.142  1.00 9.27   ? 63   HIS F O   1 
ATOM   1684 C  CB  . HIS B 2 63  ? 4.940   16.436  11.373  1.00 9.03   ? 63   HIS F CB  1 
ATOM   1685 C  CG  . HIS B 2 63  ? 3.857   17.030  10.545  1.00 9.07   ? 63   HIS F CG  1 
ATOM   1686 N  ND1 . HIS B 2 63  ? 4.095   18.013  9.626   1.00 8.72   ? 63   HIS F ND1 1 
ATOM   1687 C  CD2 . HIS B 2 63  ? 2.523   16.795  10.522  1.00 11.21  ? 63   HIS F CD2 1 
ATOM   1688 C  CE1 . HIS B 2 63  ? 2.954   18.350  9.061   1.00 9.70   ? 63   HIS F CE1 1 
ATOM   1689 N  NE2 . HIS B 2 63  ? 1.985   17.636  9.591   1.00 11.51  ? 63   HIS F NE2 1 
ATOM   1690 N  N   . PHE B 2 64  ? 6.149   13.736  12.708  1.00 8.26   ? 64   PHE F N   1 
ATOM   1691 C  CA  . PHE B 2 64  ? 7.320   13.145  13.318  1.00 8.02   ? 64   PHE F CA  1 
ATOM   1692 C  C   . PHE B 2 64  ? 8.504   14.100  13.135  1.00 7.98   ? 64   PHE F C   1 
ATOM   1693 O  O   . PHE B 2 64  ? 8.872   14.443  12.015  1.00 9.02   ? 64   PHE F O   1 
ATOM   1694 C  CB  . PHE B 2 64  ? 7.583   11.780  12.708  1.00 8.16   ? 64   PHE F CB  1 
ATOM   1695 C  CG  . PHE B 2 64  ? 8.822   11.079  13.244  1.00 8.98   ? 64   PHE F CG  1 
ATOM   1696 C  CD1 . PHE B 2 64  ? 9.082   11.009  14.600  1.00 9.99   ? 64   PHE F CD1 1 
ATOM   1697 C  CD2 . PHE B 2 64  ? 9.654   10.425  12.382  1.00 10.30  ? 64   PHE F CD2 1 
ATOM   1698 C  CE1 . PHE B 2 64  ? 10.206  10.355  15.056  1.00 10.95  ? 64   PHE F CE1 1 
ATOM   1699 C  CE2 . PHE B 2 64  ? 10.740  9.717   12.838  1.00 11.34  ? 64   PHE F CE2 1 
ATOM   1700 C  CZ  . PHE B 2 64  ? 11.036  9.719   14.158  1.00 11.67  ? 64   PHE F CZ  1 
ATOM   1701 N  N   . ASN B 2 65  ? 9.084   14.539  14.236  1.00 8.70   ? 65   ASN F N   1 
ATOM   1702 C  CA  . ASN B 2 65  ? 10.061  15.623  14.209  1.00 8.66   ? 65   ASN F CA  1 
ATOM   1703 C  C   . ASN B 2 65  ? 11.154  15.406  15.282  1.00 9.04   ? 65   ASN F C   1 
ATOM   1704 O  O   . ASN B 2 65  ? 11.291  16.184  16.234  1.00 9.82   ? 65   ASN F O   1 
ATOM   1705 C  CB  . ASN B 2 65  ? 9.334   16.929  14.477  1.00 8.57   ? 65   ASN F CB  1 
ATOM   1706 C  CG  . ASN B 2 65  ? 10.242  18.151  14.371  1.00 9.59   ? 65   ASN F CG  1 
ATOM   1707 O  OD1 . ASN B 2 65  ? 11.276  18.134  13.707  1.00 9.38   ? 65   ASN F OD1 1 
ATOM   1708 N  ND2 . ASN B 2 65  ? 9.800   19.261  14.984  1.00 10.54  ? 65   ASN F ND2 1 
ATOM   1709 N  N   . PRO B 2 66  ? 11.942  14.326  15.135  1.00 8.83   ? 66   PRO F N   1 
ATOM   1710 C  CA  . PRO B 2 66  ? 12.914  14.021  16.166  1.00 9.76   ? 66   PRO F CA  1 
ATOM   1711 C  C   . PRO B 2 66  ? 13.988  15.092  16.344  1.00 10.20  ? 66   PRO F C   1 
ATOM   1712 O  O   . PRO B 2 66  ? 14.568  15.158  17.412  1.00 11.33  ? 66   PRO F O   1 
ATOM   1713 C  CB  . PRO B 2 66  ? 13.520  12.696  15.681  1.00 10.07  ? 66   PRO F CB  1 
ATOM   1714 C  CG  . PRO B 2 66  ? 13.331  12.692  14.223  1.00 10.37  ? 66   PRO F CG  1 
ATOM   1715 C  CD  . PRO B 2 66  ? 11.986  13.319  14.057  1.00 9.11   ? 66   PRO F CD  1 
ATOM   1716 N  N   . LEU B 2 67  ? 14.245  15.895  15.329  1.00 9.78   ? 67   LEU F N   1 
ATOM   1717 C  CA  . LEU B 2 67  ? 15.305  16.888  15.353  1.00 10.02  ? 67   LEU F CA  1 
ATOM   1718 C  C   . LEU B 2 67  ? 14.828  18.300  15.738  1.00 9.67   ? 67   LEU F C   1 
ATOM   1719 O  O   . LEU B 2 67  ? 15.613  19.242  15.735  1.00 11.37  ? 67   LEU F O   1 
ATOM   1720 C  CB  . LEU B 2 67  ? 15.996  16.951  13.997  1.00 11.21  ? 67   LEU F CB  1 
ATOM   1721 C  CG  . LEU B 2 67  ? 16.866  15.725  13.704  1.00 12.93  ? 67   LEU F CG  1 
ATOM   1722 C  CD1 . LEU B 2 67  ? 17.333  15.737  12.253  1.00 15.69  ? 67   LEU F CD1 1 
ATOM   1723 C  CD2 . LEU B 2 67  ? 18.058  15.553  14.668  1.00 18.27  ? 67   LEU F CD2 1 
ATOM   1724 N  N   . SER B 2 68  ? 13.548  18.464  16.065  1.00 10.02  ? 68   SER F N   1 
ATOM   1725 C  CA  . SER B 2 68  ? 13.020  19.758  16.531  1.00 10.66  ? 68   SER F CA  1 
ATOM   1726 C  C   . SER B 2 68  ? 13.160  20.872  15.483  1.00 11.11  ? 68   SER F C   1 
ATOM   1727 O  O   . SER B 2 68  ? 13.451  22.008  15.815  1.00 13.18  ? 68   SER F O   1 
ATOM   1728 C  CB  . SER B 2 68  ? 13.667  20.167  17.872  1.00 12.08  ? 68   SER F CB  1 
ATOM   1729 O  OG  . SER B 2 68  ? 13.350  19.235  18.907  1.00 11.15  ? 68   SER F OG  1 
ATOM   1730 N  N   A ARG B 2 69  ? 12.898  20.540  14.232  0.50 11.85  ? 69   ARG F N   1 
ATOM   1731 N  N   B ARG B 2 69  ? 12.927  20.519  14.221  0.50 11.65  ? 69   ARG F N   1 
ATOM   1732 C  CA  A ARG B 2 69  ? 12.957  21.488  13.138  0.50 12.26  ? 69   ARG F CA  1 
ATOM   1733 C  CA  B ARG B 2 69  ? 12.944  21.437  13.080  0.50 11.71  ? 69   ARG F CA  1 
ATOM   1734 C  C   A ARG B 2 69  ? 11.554  21.990  12.796  0.50 12.22  ? 69   ARG F C   1 
ATOM   1735 C  C   B ARG B 2 69  ? 11.558  22.035  12.853  0.50 11.97  ? 69   ARG F C   1 
ATOM   1736 O  O   A ARG B 2 69  ? 10.553  21.528  13.346  0.50 12.56  ? 69   ARG F O   1 
ATOM   1737 O  O   B ARG B 2 69  ? 10.580  21.671  13.519  0.50 11.84  ? 69   ARG F O   1 
ATOM   1738 C  CB  A ARG B 2 69  ? 13.644  20.868  11.931  0.50 12.81  ? 69   ARG F CB  1 
ATOM   1739 C  CB  B ARG B 2 69  ? 13.366  20.722  11.800  0.50 12.25  ? 69   ARG F CB  1 
ATOM   1740 C  CG  A ARG B 2 69  ? 15.089  20.541  12.205  0.50 14.98  ? 69   ARG F CG  1 
ATOM   1741 C  CG  B ARG B 2 69  ? 14.643  19.937  11.920  0.50 13.48  ? 69   ARG F CG  1 
ATOM   1742 C  CD  A ARG B 2 69  ? 15.793  20.149  10.937  0.50 17.44  ? 69   ARG F CD  1 
ATOM   1743 C  CD  B ARG B 2 69  ? 15.831  20.833  12.228  0.50 14.42  ? 69   ARG F CD  1 
ATOM   1744 N  NE  A ARG B 2 69  ? 17.225  20.012  11.155  0.50 21.30  ? 69   ARG F NE  1 
ATOM   1745 N  NE  B ARG B 2 69  ? 17.080  20.108  12.017  0.50 16.04  ? 69   ARG F NE  1 
ATOM   1746 C  CZ  A ARG B 2 69  ? 18.091  19.592  10.241  0.50 22.35  ? 69   ARG F CZ  1 
ATOM   1747 C  CZ  B ARG B 2 69  ? 18.082  20.027  12.887  0.50 16.13  ? 69   ARG F CZ  1 
ATOM   1748 N  NH1 A ARG B 2 69  ? 17.693  19.258  9.023   0.50 23.94  ? 69   ARG F NH1 1 
ATOM   1749 N  NH1 B ARG B 2 69  ? 18.022  20.648  14.059  0.50 15.93  ? 69   ARG F NH1 1 
ATOM   1750 N  NH2 A ARG B 2 69  ? 19.371  19.511  10.560  0.50 23.53  ? 69   ARG F NH2 1 
ATOM   1751 N  NH2 B ARG B 2 69  ? 19.150  19.319  12.564  0.50 17.73  ? 69   ARG F NH2 1 
ATOM   1752 N  N   . LYS B 2 70  ? 11.506  22.987  11.920  1.00 12.57  ? 70   LYS F N   1 
ATOM   1753 C  CA  . LYS B 2 70  ? 10.244  23.505  11.418  1.00 12.79  ? 70   LYS F CA  1 
ATOM   1754 C  C   . LYS B 2 70  ? 9.796   22.677  10.220  1.00 12.33  ? 70   LYS F C   1 
ATOM   1755 O  O   . LYS B 2 70  ? 10.561  21.949  9.612   1.00 13.03  ? 70   LYS F O   1 
ATOM   1756 C  CB  . LYS B 2 70  ? 10.372  24.987  11.053  1.00 13.50  ? 70   LYS F CB  1 
ATOM   1757 C  CG  . LYS B 2 70  ? 10.337  25.902  12.288  1.00 16.38  ? 70   LYS F CG  1 
ATOM   1758 C  CD  . LYS B 2 70  ? 10.589  27.355  11.966  1.00 18.83  ? 70   LYS F CD  1 
ATOM   1759 C  CE  . LYS B 2 70  ? 10.430  28.233  13.200  1.00 19.94  ? 70   LYS F CE  1 
ATOM   1760 N  NZ  . LYS B 2 70  ? 10.693  29.683  12.889  1.00 21.59  ? 70   LYS F NZ  1 
ATOM   1761 N  N   . HIS B 2 71  ? 8.508   22.797  9.928   1.00 11.19  ? 71   HIS F N   1 
ATOM   1762 C  CA  . HIS B 2 71  ? 7.891   22.112  8.804   1.00 11.16  ? 71   HIS F CA  1 
ATOM   1763 C  C   . HIS B 2 71  ? 8.437   22.620  7.479   1.00 11.34  ? 71   HIS F C   1 
ATOM   1764 O  O   . HIS B 2 71  ? 8.617   23.824  7.299   1.00 12.63  ? 71   HIS F O   1 
ATOM   1765 C  CB  . HIS B 2 71  ? 6.381   22.321  8.885   1.00 10.49  ? 71   HIS F CB  1 
ATOM   1766 C  CG  . HIS B 2 71  ? 5.637   21.646  7.786   1.00 10.77  ? 71   HIS F CG  1 
ATOM   1767 N  ND1 . HIS B 2 71  ? 5.402   20.293  7.773   1.00 9.64   ? 71   HIS F ND1 1 
ATOM   1768 C  CD2 . HIS B 2 71  ? 5.121   22.142  6.633   1.00 10.91  ? 71   HIS F CD2 1 
ATOM   1769 C  CE1 . HIS B 2 71  ? 4.779   19.977  6.652   1.00 9.48   ? 71   HIS F CE1 1 
ATOM   1770 N  NE2 . HIS B 2 71  ? 4.578   21.086  5.951   1.00 10.99  ? 71   HIS F NE2 1 
ATOM   1771 N  N   . GLY B 2 72  ? 8.620   21.711  6.540   1.00 11.49  ? 72   GLY F N   1 
ATOM   1772 C  CA  . GLY B 2 72  ? 8.990   22.015  5.182   1.00 11.53  ? 72   GLY F CA  1 
ATOM   1773 C  C   . GLY B 2 72  ? 8.519   20.970  4.210   1.00 12.03  ? 72   GLY F C   1 
ATOM   1774 O  O   . GLY B 2 72  ? 7.683   20.151  4.541   1.00 11.86  ? 72   GLY F O   1 
ATOM   1775 N  N   . GLY B 2 73  ? 8.983   21.072  2.974   1.00 12.90  ? 73   GLY F N   1 
ATOM   1776 C  CA  . GLY B 2 73  ? 8.759   20.062  1.972   1.00 12.88  ? 73   GLY F CA  1 
ATOM   1777 C  C   . GLY B 2 73  ? 9.900   19.065  1.992   1.00 12.94  ? 73   GLY F C   1 
ATOM   1778 O  O   . GLY B 2 73  ? 10.959  19.292  2.614   1.00 14.10  ? 73   GLY F O   1 
ATOM   1779 N  N   . PRO B 2 74  ? 9.692   17.930  1.315   1.00 13.19  ? 74   PRO F N   1 
ATOM   1780 C  CA  . PRO B 2 74  ? 10.687  16.865  1.382   1.00 13.83  ? 74   PRO F CA  1 
ATOM   1781 C  C   . PRO B 2 74  ? 12.059  17.242  0.821   1.00 15.21  ? 74   PRO F C   1 
ATOM   1782 O  O   . PRO B 2 74  ? 13.066  16.709  1.276   1.00 16.37  ? 74   PRO F O   1 
ATOM   1783 C  CB  . PRO B 2 74  ? 10.039  15.724  0.614   1.00 15.33  ? 74   PRO F CB  1 
ATOM   1784 C  CG  . PRO B 2 74  ? 8.960   16.348  -0.181  1.00 15.17  ? 74   PRO F CG  1 
ATOM   1785 C  CD  . PRO B 2 74  ? 8.479   17.490  0.625   1.00 14.20  ? 74   PRO F CD  1 
ATOM   1786 N  N   . LYS B 2 75  ? 12.098  18.170  -0.127  1.00 15.98  ? 75   LYS F N   1 
ATOM   1787 C  CA  . LYS B 2 75  ? 13.369  18.632  -0.683  1.00 17.71  ? 75   LYS F CA  1 
ATOM   1788 C  C   . LYS B 2 75  ? 14.113  19.647  0.179   1.00 17.45  ? 75   LYS F C   1 
ATOM   1789 O  O   . LYS B 2 75  ? 15.253  20.008  -0.128  1.00 20.42  ? 75   LYS F O   1 
ATOM   1790 C  CB  . LYS B 2 75  ? 13.129  19.269  -2.046  1.00 17.50  ? 75   LYS F CB  1 
ATOM   1791 C  CG  . LYS B 2 75  ? 12.608  18.289  -3.053  1.00 20.85  ? 75   LYS F CG  1 
ATOM   1792 C  CD  . LYS B 2 75  ? 12.773  18.792  -4.474  1.00 26.03  ? 75   LYS F CD  1 
ATOM   1793 C  CE  . LYS B 2 75  ? 11.727  19.794  -4.809  1.00 27.42  ? 75   LYS F CE  1 
ATOM   1794 N  NZ  . LYS B 2 75  ? 11.591  19.988  -6.294  1.00 30.67  ? 75   LYS F NZ  1 
ATOM   1795 N  N   . ASP B 2 76  ? 13.477  20.168  1.210   1.00 16.88  ? 76   ASP F N   1 
ATOM   1796 C  CA  . ASP B 2 76  ? 14.090  21.197  2.059   1.00 17.85  ? 76   ASP F CA  1 
ATOM   1797 C  C   . ASP B 2 76  ? 14.989  20.588  3.124   1.00 18.22  ? 76   ASP F C   1 
ATOM   1798 O  O   . ASP B 2 76  ? 14.689  19.523  3.662   1.00 18.65  ? 76   ASP F O   1 
ATOM   1799 C  CB  . ASP B 2 76  ? 13.008  22.028  2.711   1.00 18.51  ? 76   ASP F CB  1 
ATOM   1800 C  CG  . ASP B 2 76  ? 12.160  22.763  1.693   1.00 21.81  ? 76   ASP F CG  1 
ATOM   1801 O  OD1 . ASP B 2 76  ? 12.700  23.166  0.626   1.00 26.97  ? 76   ASP F OD1 1 
ATOM   1802 O  OD2 . ASP B 2 76  ? 10.954  22.925  1.980   1.00 22.13  ? 76   ASP F OD2 1 
ATOM   1803 N  N   . GLU B 2 77  ? 16.100  21.249  3.424   1.00 18.75  ? 77   GLU F N   1 
ATOM   1804 C  CA  . GLU B 2 77  ? 16.910  20.837  4.559   1.00 18.74  ? 77   GLU F CA  1 
ATOM   1805 C  C   . GLU B 2 77  ? 16.159  21.062  5.857   1.00 17.23  ? 77   GLU F C   1 
ATOM   1806 O  O   . GLU B 2 77  ? 16.211  20.233  6.782   1.00 17.61  ? 77   GLU F O   1 
ATOM   1807 C  CB  . GLU B 2 77  ? 18.226  21.604  4.607   1.00 19.67  ? 77   GLU F CB  1 
ATOM   1808 C  CG  . GLU B 2 77  ? 19.136  21.141  5.774   1.00 22.59  ? 77   GLU F CG  1 
ATOM   1809 C  CD  . GLU B 2 77  ? 19.635  19.704  5.628   0.50 25.16  ? 77   GLU F CD  1 
ATOM   1810 O  OE1 . GLU B 2 77  ? 19.767  19.224  4.477   0.50 27.96  ? 77   GLU F OE1 1 
ATOM   1811 O  OE2 . GLU B 2 77  ? 19.897  19.046  6.666   0.50 28.72  ? 77   GLU F OE2 1 
ATOM   1812 N  N   . GLU B 2 78  ? 15.454  22.192  5.951   1.00 15.57  ? 78   GLU F N   1 
ATOM   1813 C  CA  . GLU B 2 78  ? 14.648  22.482  7.139   1.00 15.06  ? 78   GLU F CA  1 
ATOM   1814 C  C   . GLU B 2 78  ? 13.274  21.830  6.898   1.00 13.19  ? 78   GLU F C   1 
ATOM   1815 O  O   . GLU B 2 78  ? 12.408  22.347  6.159   1.00 14.39  ? 78   GLU F O   1 
ATOM   1816 C  CB  . GLU B 2 78  ? 14.484  23.987  7.349   1.00 15.59  ? 78   GLU F CB  1 
ATOM   1817 C  CG  . GLU B 2 78  ? 13.771  24.363  8.609   1.00 17.37  ? 78   GLU F CG  1 
ATOM   1818 C  CD  . GLU B 2 78  ? 14.583  24.096  9.864   0.80 16.76  ? 78   GLU F CD  1 
ATOM   1819 O  OE1 . GLU B 2 78  ? 15.836  23.932  9.782   0.80 23.78  ? 78   GLU F OE1 1 
ATOM   1820 O  OE2 . GLU B 2 78  ? 13.974  24.121  10.952  1.00 21.32  ? 78   GLU F OE2 1 
ATOM   1821 N  N   . ARG B 2 79  ? 13.075  20.699  7.551   1.00 11.98  ? 79   ARG F N   1 
ATOM   1822 C  CA  . ARG B 2 79  ? 11.819  19.931  7.458   1.00 11.23  ? 79   ARG F CA  1 
ATOM   1823 C  C   . ARG B 2 79  ? 11.753  19.049  8.668   1.00 10.68  ? 79   ARG F C   1 
ATOM   1824 O  O   . ARG B 2 79  ? 12.768  18.786  9.295   1.00 12.09  ? 79   ARG F O   1 
ATOM   1825 C  CB  . ARG B 2 79  ? 11.788  19.062  6.191   1.00 11.33  ? 79   ARG F CB  1 
ATOM   1826 C  CG  . ARG B 2 79  ? 12.956  18.075  6.073   1.00 11.83  ? 79   ARG F CG  1 
ATOM   1827 C  CD  . ARG B 2 79  ? 12.808  17.096  4.937   1.00 12.05  ? 79   ARG F CD  1 
ATOM   1828 N  NE  . ARG B 2 79  ? 12.047  15.920  5.338   1.00 11.40  ? 79   ARG F NE  1 
ATOM   1829 C  CZ  . ARG B 2 79  ? 11.997  14.831  4.589   1.00 11.75  ? 79   ARG F CZ  1 
ATOM   1830 N  NH1 . ARG B 2 79  ? 12.586  14.821  3.394   1.00 12.51  ? 79   ARG F NH1 1 
ATOM   1831 N  NH2 . ARG B 2 79  ? 11.363  13.751  5.016   1.00 11.79  ? 79   ARG F NH2 1 
ATOM   1832 N  N   . HIS B 2 80  ? 10.562  18.578  8.976   1.00 9.81   ? 80   HIS F N   1 
ATOM   1833 C  CA  . HIS B 2 80  ? 10.384  17.462  9.892   1.00 9.25   ? 80   HIS F CA  1 
ATOM   1834 C  C   . HIS B 2 80  ? 10.770  16.174  9.197   1.00 9.00   ? 80   HIS F C   1 
ATOM   1835 O  O   . HIS B 2 80  ? 10.581  16.052  7.996   1.00 10.01  ? 80   HIS F O   1 
ATOM   1836 C  CB  . HIS B 2 80  ? 8.911   17.377  10.298  1.00 9.34   ? 80   HIS F CB  1 
ATOM   1837 C  CG  . HIS B 2 80  ? 8.357   18.615  10.909  1.00 11.17  ? 80   HIS F CG  1 
ATOM   1838 N  ND1 . HIS B 2 80  ? 7.070   19.058  10.689  1.00 9.75   ? 80   HIS F ND1 1 
ATOM   1839 C  CD2 . HIS B 2 80  ? 8.896   19.456  11.807  1.00 10.88  ? 80   HIS F CD2 1 
ATOM   1840 C  CE1 . HIS B 2 80  ? 6.854   20.125  11.428  1.00 9.86   ? 80   HIS F CE1 1 
ATOM   1841 N  NE2 . HIS B 2 80  ? 7.952   20.393  12.108  1.00 11.38  ? 80   HIS F NE2 1 
ATOM   1842 N  N   . VAL B 2 81  ? 11.243  15.180  9.936   1.00 8.99   ? 81   VAL F N   1 
ATOM   1843 C  CA  . VAL B 2 81  ? 11.542  13.900  9.307   1.00 9.81   ? 81   VAL F CA  1 
ATOM   1844 C  C   . VAL B 2 81  ? 10.297  13.355  8.610   1.00 9.79   ? 81   VAL F C   1 
ATOM   1845 O  O   . VAL B 2 81  ? 10.384  12.806  7.518   1.00 9.93   ? 81   VAL F O   1 
ATOM   1846 C  CB  . VAL B 2 81  ? 12.094  12.866  10.311  1.00 8.78   ? 81   VAL F CB  1 
ATOM   1847 C  CG1 . VAL B 2 81  ? 12.097  11.449  9.694   1.00 10.47  ? 81   VAL F CG1 1 
ATOM   1848 C  CG2 . VAL B 2 81  ? 13.522  13.279  10.730  1.00 11.08  ? 81   VAL F CG2 1 
ATOM   1849 N  N   . GLY B 2 82  ? 9.115   13.559  9.206   1.00 9.20   ? 82   GLY F N   1 
ATOM   1850 C  CA  . GLY B 2 82  ? 7.876   13.045  8.619   1.00 9.95   ? 82   GLY F CA  1 
ATOM   1851 C  C   . GLY B 2 82  ? 7.328   13.774  7.394   1.00 8.97   ? 82   GLY F C   1 
ATOM   1852 O  O   . GLY B 2 82  ? 6.270   13.425  6.936   1.00 10.06  ? 82   GLY F O   1 
ATOM   1853 N  N   . ASP B 2 83  ? 7.983   14.832  6.927   1.00 9.80   ? 83   ASP F N   1 
ATOM   1854 C  CA  . ASP B 2 83  ? 7.465   15.702  5.867   1.00 9.80   ? 83   ASP F CA  1 
ATOM   1855 C  C   . ASP B 2 83  ? 7.661   15.110  4.481   1.00 10.78  ? 83   ASP F C   1 
ATOM   1856 O  O   . ASP B 2 83  ? 8.690   15.313  3.839   1.00 13.33  ? 83   ASP F O   1 
ATOM   1857 C  CB  . ASP B 2 83  ? 8.105   17.082  5.957   1.00 10.22  ? 83   ASP F CB  1 
ATOM   1858 C  CG  . ASP B 2 83  ? 7.614   17.861  7.133   1.00 9.60   ? 83   ASP F CG  1 
ATOM   1859 O  OD1 . ASP B 2 83  ? 6.566   17.458  7.730   1.00 9.53   ? 83   ASP F OD1 1 
ATOM   1860 O  OD2 . ASP B 2 83  ? 8.221   18.896  7.480   1.00 10.34  ? 83   ASP F OD2 1 
ATOM   1861 N  N   . LEU B 2 84  ? 6.631   14.440  3.980   1.00 9.89   ? 84   LEU F N   1 
ATOM   1862 C  CA  . LEU B 2 84  ? 6.697   13.814  2.671   1.00 10.59  ? 84   LEU F CA  1 
ATOM   1863 C  C   . LEU B 2 84  ? 5.898   14.576  1.621   1.00 10.69  ? 84   LEU F C   1 
ATOM   1864 O  O   . LEU B 2 84  ? 5.656   14.071  0.535   1.00 12.96  ? 84   LEU F O   1 
ATOM   1865 C  CB  . LEU B 2 84  ? 6.216   12.371  2.734   1.00 10.51  ? 84   LEU F CB  1 
ATOM   1866 C  CG  . LEU B 2 84  ? 7.086   11.447  3.618   1.00 11.66  ? 84   LEU F CG  1 
ATOM   1867 C  CD1 . LEU B 2 84  ? 6.491   10.073  3.730   1.00 13.39  ? 84   LEU F CD1 1 
ATOM   1868 C  CD2 . LEU B 2 84  ? 8.555   11.400  3.113   1.00 14.97  ? 84   LEU F CD2 1 
ATOM   1869 N  N   . GLY B 2 85  ? 5.532   15.806  1.918   1.00 10.67  ? 85   GLY F N   1 
ATOM   1870 C  CA  . GLY B 2 85  ? 4.970   16.688  0.888   1.00 10.85  ? 85   GLY F CA  1 
ATOM   1871 C  C   . GLY B 2 85  ? 3.482   16.475  0.645   1.00 11.10  ? 85   GLY F C   1 
ATOM   1872 O  O   . GLY B 2 85  ? 2.704   16.465  1.585   1.00 11.83  ? 85   GLY F O   1 
ATOM   1873 N  N   . ASN B 2 86  ? 3.111   16.354  -0.622  1.00 11.07  ? 86   ASN F N   1 
ATOM   1874 C  CA  . ASN B 2 86  ? 1.745   16.137  -1.042  1.00 11.03  ? 86   ASN F CA  1 
ATOM   1875 C  C   . ASN B 2 86  ? 1.639   14.931  -1.949  1.00 12.11  ? 86   ASN F C   1 
ATOM   1876 O  O   . ASN B 2 86  ? 2.553   14.634  -2.679  1.00 14.09  ? 86   ASN F O   1 
ATOM   1877 C  CB  . ASN B 2 86  ? 1.232   17.339  -1.848  1.00 12.23  ? 86   ASN F CB  1 
ATOM   1878 C  CG  . ASN B 2 86  ? 1.081   18.574  -1.002  1.00 12.50  ? 86   ASN F CG  1 
ATOM   1879 O  OD1 . ASN B 2 86  ? 0.115   18.690  -0.244  1.00 11.80  ? 86   ASN F OD1 1 
ATOM   1880 N  ND2 . ASN B 2 86  ? 2.035   19.507  -1.113  1.00 14.23  ? 86   ASN F ND2 1 
ATOM   1881 N  N   . VAL B 2 87  ? 0.484   14.294  -1.946  1.00 11.66  ? 87   VAL F N   1 
ATOM   1882 C  CA  . VAL B 2 87  ? 0.057   13.425  -3.027  1.00 12.19  ? 87   VAL F CA  1 
ATOM   1883 C  C   . VAL B 2 87  ? -0.979  14.188  -3.822  1.00 11.79  ? 87   VAL F C   1 
ATOM   1884 O  O   . VAL B 2 87  ? -1.620  15.079  -3.298  1.00 12.46  ? 87   VAL F O   1 
ATOM   1885 C  CB  . VAL B 2 87  ? -0.439  12.089  -2.515  1.00 12.66  ? 87   VAL F CB  1 
ATOM   1886 C  CG1 . VAL B 2 87  ? 0.704   11.371  -1.790  1.00 14.32  ? 87   VAL F CG1 1 
ATOM   1887 C  CG2 . VAL B 2 87  ? -1.698  12.224  -1.622  1.00 14.66  ? 87   VAL F CG2 1 
ATOM   1888 N  N   . THR B 2 88  ? -1.065  13.912  -5.110  1.00 12.74  ? 88   THR F N   1 
ATOM   1889 C  CA  . THR B 2 88  ? -1.961  14.688  -5.968  1.00 13.80  ? 88   THR F CA  1 
ATOM   1890 C  C   . THR B 2 88  ? -2.961  13.722  -6.585  1.00 12.92  ? 88   THR F C   1 
ATOM   1891 O  O   . THR B 2 88  ? -2.577  12.771  -7.271  1.00 14.05  ? 88   THR F O   1 
ATOM   1892 C  CB  . THR B 2 88  ? -1.168  15.475  -7.057  1.00 13.79  ? 88   THR F CB  1 
ATOM   1893 O  OG1 . THR B 2 88  ? -0.282  16.430  -6.450  1.00 15.87  ? 88   THR F OG1 1 
ATOM   1894 C  CG2 . THR B 2 88  ? -2.114  16.220  -7.981  1.00 14.78  ? 88   THR F CG2 1 
ATOM   1895 N  N   . ALA B 2 89  ? -4.245  13.975  -6.341  1.00 12.72  ? 89   ALA F N   1 
ATOM   1896 C  CA  . ALA B 2 89  ? -5.340  13.179  -6.886  1.00 14.50  ? 89   ALA F CA  1 
ATOM   1897 C  C   . ALA B 2 89  ? -5.916  13.830  -8.139  1.00 14.52  ? 89   ALA F C   1 
ATOM   1898 O  O   . ALA B 2 89  ? -6.023  15.051  -8.283  1.00 13.51  ? 89   ALA F O   1 
ATOM   1899 C  CB  . ALA B 2 89  ? -6.415  13.005  -5.867  1.00 14.21  ? 89   ALA F CB  1 
ATOM   1900 N  N   . ASP B 2 90  ? -6.333  12.976  -9.047  1.00 16.15  ? 90   ASP F N   1 
ATOM   1901 C  CA  . ASP B 2 90  ? -7.020  13.495  -10.229 1.00 17.59  ? 90   ASP F CA  1 
ATOM   1902 C  C   . ASP B 2 90  ? -8.534  13.436  -10.034 1.00 16.57  ? 90   ASP F C   1 
ATOM   1903 O  O   . ASP B 2 90  ? -9.007  13.106  -8.947  1.00 14.98  ? 90   ASP F O   1 
ATOM   1904 C  CB  . ASP B 2 90  ? -6.529  12.842  -11.532 1.00 20.06  ? 90   ASP F CB  1 
ATOM   1905 C  CG  . ASP B 2 90  ? -6.761  11.420  -11.569 1.00 23.51  ? 90   ASP F CG  1 
ATOM   1906 O  OD1 . ASP B 2 90  ? -7.026  10.858  -10.504 1.00 30.98  ? 90   ASP F OD1 1 
ATOM   1907 O  OD2 . ASP B 2 90  ? -6.689  10.876  -12.690 0.60 27.85  ? 90   ASP F OD2 1 
ATOM   1908 N  N   . LYS B 2 91  ? -9.297  13.790  -11.063 1.00 16.03  ? 91   LYS F N   1 
ATOM   1909 C  CA  . LYS B 2 91  ? -10.769 13.710  -10.991 1.00 16.26  ? 91   LYS F CA  1 
ATOM   1910 C  C   . LYS B 2 91  ? -11.329 12.356  -10.618 1.00 16.86  ? 91   LYS F C   1 
ATOM   1911 O  O   . LYS B 2 91  ? -12.415 12.280  -10.052 1.00 17.74  ? 91   LYS F O   1 
ATOM   1912 C  CB  . LYS B 2 91  ? -11.368 14.091  -12.350 1.00 16.92  ? 91   LYS F CB  1 
ATOM   1913 C  CG  . LYS B 2 91  ? -11.464 15.572  -12.631 1.00 19.37  ? 91   LYS F CG  1 
ATOM   1914 C  CD  . LYS B 2 91  ? -12.571 16.193  -11.799 1.00 22.88  ? 91   LYS F CD  1 
ATOM   1915 C  CE  . LYS B 2 91  ? -13.151 17.449  -12.414 1.00 24.57  ? 91   LYS F CE  1 
ATOM   1916 N  NZ  . LYS B 2 91  ? -12.217 18.570  -12.350 1.00 26.81  ? 91   LYS F NZ  1 
ATOM   1917 N  N   . ASP B 2 92  ? -10.614 11.299  -10.974 1.00 16.45  ? 92   ASP F N   1 
ATOM   1918 C  CA  . ASP B 2 92  ? -11.018 9.948   -10.586 1.00 17.37  ? 92   ASP F CA  1 
ATOM   1919 C  C   . ASP B 2 92  ? -10.853 9.685   -9.074  1.00 17.04  ? 92   ASP F C   1 
ATOM   1920 O  O   . ASP B 2 92  ? -11.258 8.639   -8.581  1.00 19.06  ? 92   ASP F O   1 
ATOM   1921 C  CB  . ASP B 2 92  ? -10.244 8.910   -11.404 1.00 18.64  ? 92   ASP F CB  1 
ATOM   1922 C  CG  . ASP B 2 92  ? -8.707  9.058   -11.287 0.80 20.38  ? 92   ASP F CG  1 
ATOM   1923 O  OD1 . ASP B 2 92  ? -8.240  9.754   -10.364 1.00 22.06  ? 92   ASP F OD1 1 
ATOM   1924 O  OD2 . ASP B 2 92  ? -7.946  8.485   -12.124 0.80 24.20  ? 92   ASP F OD2 1 
ATOM   1925 N  N   . GLY B 2 93  ? -10.276 10.634  -8.349  1.00 15.71  ? 93   GLY F N   1 
ATOM   1926 C  CA  . GLY B 2 93  ? -10.055 10.472  -6.909  1.00 15.20  ? 93   GLY F CA  1 
ATOM   1927 C  C   . GLY B 2 93  ? -8.845  9.655   -6.486  1.00 14.56  ? 93   GLY F C   1 
ATOM   1928 O  O   . GLY B 2 93  ? -8.635  9.425   -5.294  1.00 15.50  ? 93   GLY F O   1 
ATOM   1929 N  N   . VAL B 2 94  ? -7.993  9.318   -7.441  1.00 13.97  ? 94   VAL F N   1 
ATOM   1930 C  CA  . VAL B 2 94  ? -6.821  8.483   -7.205  1.00 14.36  ? 94   VAL F CA  1 
ATOM   1931 C  C   . VAL B 2 94  ? -5.535  9.269   -7.292  1.00 13.80  ? 94   VAL F C   1 
ATOM   1932 O  O   . VAL B 2 94  ? -5.301  10.014  -8.246  1.00 14.76  ? 94   VAL F O   1 
ATOM   1933 C  CB  . VAL B 2 94  ? -6.735  7.332   -8.218  1.00 14.81  ? 94   VAL F CB  1 
ATOM   1934 C  CG1 . VAL B 2 94  ? -5.517  6.483   -7.968  1.00 16.28  ? 94   VAL F CG1 1 
ATOM   1935 C  CG2 . VAL B 2 94  ? -8.043  6.497   -8.178  1.00 17.46  ? 94   VAL F CG2 1 
ATOM   1936 N  N   . ALA B 2 95  ? -4.725  9.118   -6.240  1.00 13.86  ? 95   ALA F N   1 
ATOM   1937 C  CA  . ALA B 2 95  ? -3.360  9.593   -6.216  1.00 14.81  ? 95   ALA F CA  1 
ATOM   1938 C  C   . ALA B 2 95  ? -2.395  8.422   -6.313  1.00 15.03  ? 95   ALA F C   1 
ATOM   1939 O  O   . ALA B 2 95  ? -2.445  7.491   -5.519  1.00 15.99  ? 95   ALA F O   1 
ATOM   1940 C  CB  . ALA B 2 95  ? -3.112  10.404  -4.958  1.00 15.24  ? 95   ALA F CB  1 
ATOM   1941 N  N   . ASP B 2 96  ? -1.507  8.483   -7.296  1.00 15.72  ? 96   ASP F N   1 
ATOM   1942 C  CA  . ASP B 2 96  ? -0.423  7.508   -7.424  1.00 16.91  ? 96   ASP F CA  1 
ATOM   1943 C  C   . ASP B 2 96  ? 0.776   8.069   -6.697  1.00 17.19  ? 96   ASP F C   1 
ATOM   1944 O  O   . ASP B 2 96  ? 1.232   9.192   -6.940  1.00 19.97  ? 96   ASP F O   1 
ATOM   1945 C  CB  . ASP B 2 96  ? -0.110  7.253   -8.890  1.00 17.93  ? 96   ASP F CB  1 
ATOM   1946 C  CG  . ASP B 2 96  ? -1.233  6.545   -9.596  1.00 20.84  ? 96   ASP F CG  1 
ATOM   1947 O  OD1 . ASP B 2 96  ? -1.813  5.588   -9.033  0.70 21.24  ? 96   ASP F OD1 1 
ATOM   1948 O  OD2 . ASP B 2 96  ? -1.537  6.929   -10.730 0.60 25.03  ? 96   ASP F OD2 1 
ATOM   1949 N  N   . VAL B 2 97  ? 1.265   7.283   -5.754  1.00 16.36  ? 97   VAL F N   1 
ATOM   1950 C  CA  . VAL B 2 97  ? 2.359   7.693   -4.900  1.00 17.03  ? 97   VAL F CA  1 
ATOM   1951 C  C   . VAL B 2 97  ? 3.601   6.987   -5.387  1.00 16.77  ? 97   VAL F C   1 
ATOM   1952 O  O   . VAL B 2 97  ? 3.625   5.751   -5.564  1.00 15.40  ? 97   VAL F O   1 
ATOM   1953 C  CB  . VAL B 2 97  ? 2.047   7.322   -3.450  1.00 16.95  ? 97   VAL F CB  1 
ATOM   1954 C  CG1 . VAL B 2 97  ? 3.189   7.753   -2.500  1.00 18.13  ? 97   VAL F CG1 1 
ATOM   1955 C  CG2 . VAL B 2 97  ? 0.722   7.971   -3.024  1.00 18.75  ? 97   VAL F CG2 1 
ATOM   1956 N  N   . SER B 2 98  ? 4.627   7.791   -5.634  1.00 18.54  ? 98   SER F N   1 
ATOM   1957 C  CA  . SER B 2 98  ? 5.959   7.324   -5.973  1.00 19.27  ? 98   SER F CA  1 
ATOM   1958 C  C   . SER B 2 98  ? 6.937   8.386   -5.474  1.00 20.07  ? 98   SER F C   1 
ATOM   1959 O  O   . SER B 2 98  ? 7.069   9.473   -6.057  1.00 21.25  ? 98   SER F O   1 
ATOM   1960 C  CB  . SER B 2 98  ? 6.102   7.095   -7.480  1.00 20.75  ? 98   SER F CB  1 
ATOM   1961 O  OG  . SER B 2 98  ? 7.369   6.535   -7.751  1.00 25.60  ? 98   SER F OG  1 
ATOM   1962 N  N   . ILE B 2 99  ? 7.639   8.070   -4.405  1.00 19.37  ? 99   ILE F N   1 
ATOM   1963 C  CA  . ILE B 2 99  ? 8.488   9.007   -3.697  1.00 18.49  ? 99   ILE F CA  1 
ATOM   1964 C  C   . ILE B 2 99  ? 9.770   8.216   -3.401  1.00 17.08  ? 99   ILE F C   1 
ATOM   1965 O  O   . ILE B 2 99  ? 9.737   6.989   -3.175  1.00 17.63  ? 99   ILE F O   1 
ATOM   1966 C  CB  . ILE B 2 99  ? 7.772   9.450   -2.345  1.00 18.98  ? 99   ILE F CB  1 
ATOM   1967 C  CG1 . ILE B 2 99  ? 6.623   10.436  -2.631  1.00 21.19  ? 99   ILE F CG1 1 
ATOM   1968 C  CG2 . ILE B 2 99  ? 8.710   10.077  -1.354  1.00 22.15  ? 99   ILE F CG2 1 
ATOM   1969 C  CD1 . ILE B 2 99  ? 5.687   10.695  -1.442  1.00 23.63  ? 99   ILE F CD1 1 
ATOM   1970 N  N   A GLU B 2 100 ? 10.903  8.895   -3.439  0.70 16.50  ? 100  GLU F N   1 
ATOM   1971 N  N   B GLU B 2 100 ? 10.911  8.892   -3.423  0.30 16.45  ? 100  GLU F N   1 
ATOM   1972 C  CA  A GLU B 2 100 ? 12.106  8.408   -2.820  0.70 16.77  ? 100  GLU F CA  1 
ATOM   1973 C  CA  B GLU B 2 100 ? 12.109  8.356   -2.799  0.30 16.10  ? 100  GLU F CA  1 
ATOM   1974 C  C   A GLU B 2 100 ? 12.454  9.474   -1.809  0.70 15.71  ? 100  GLU F C   1 
ATOM   1975 C  C   B GLU B 2 100 ? 12.629  9.435   -1.868  0.30 15.33  ? 100  GLU F C   1 
ATOM   1976 O  O   A GLU B 2 100 ? 12.370  10.679  -2.106  0.70 15.55  ? 100  GLU F O   1 
ATOM   1977 O  O   B GLU B 2 100 ? 12.829  10.589  -2.275  0.30 15.07  ? 100  GLU F O   1 
ATOM   1978 C  CB  A GLU B 2 100 ? 13.248  8.228   -3.840  0.70 18.31  ? 100  GLU F CB  1 
ATOM   1979 C  CB  B GLU B 2 100 ? 13.177  7.924   -3.819  0.30 16.66  ? 100  GLU F CB  1 
ATOM   1980 C  CG  A GLU B 2 100 ? 14.515  7.673   -3.233  0.70 22.04  ? 100  GLU F CG  1 
ATOM   1981 C  CG  B GLU B 2 100 ? 14.234  6.993   -3.227  0.30 17.98  ? 100  GLU F CG  1 
ATOM   1982 C  CD  A GLU B 2 100 ? 15.653  7.581   -4.228  0.70 25.20  ? 100  GLU F CD  1 
ATOM   1983 C  CD  B GLU B 2 100 ? 15.007  6.216   -4.275  0.30 19.60  ? 100  GLU F CD  1 
ATOM   1984 O  OE1 A GLU B 2 100 ? 15.539  6.766   -5.161  0.70 28.71  ? 100  GLU F OE1 1 
ATOM   1985 O  OE1 B GLU B 2 100 ? 14.490  6.089   -5.400  0.30 20.49  ? 100  GLU F OE1 1 
ATOM   1986 O  OE2 A GLU B 2 100 ? 16.648  8.336   -4.091  0.70 28.22  ? 100  GLU F OE2 1 
ATOM   1987 O  OE2 B GLU B 2 100 ? 16.117  5.721   -3.965  0.30 20.38  ? 100  GLU F OE2 1 
ATOM   1988 N  N   . ASP B 2 101 ? 12.853  9.054   -0.617  1.00 13.99  ? 101  ASP F N   1 
ATOM   1989 C  CA  . ASP B 2 101 ? 13.224  10.000  0.434   1.00 13.21  ? 101  ASP F CA  1 
ATOM   1990 C  C   . ASP B 2 101 ? 14.426  9.527   1.199   1.00 13.16  ? 101  ASP F C   1 
ATOM   1991 O  O   . ASP B 2 101 ? 14.517  8.352   1.545   1.00 14.48  ? 101  ASP F O   1 
ATOM   1992 C  CB  . ASP B 2 101 ? 12.058  10.244  1.397   1.00 13.14  ? 101  ASP F CB  1 
ATOM   1993 C  CG  . ASP B 2 101 ? 12.246  11.505  2.242   0.80 12.39  ? 101  ASP F CG  1 
ATOM   1994 O  OD1 . ASP B 2 101 ? 12.092  12.635  1.704   0.70 13.50  ? 101  ASP F OD1 1 
ATOM   1995 O  OD2 . ASP B 2 101 ? 12.569  11.368  3.441   1.00 13.36  ? 101  ASP F OD2 1 
ATOM   1996 N  N   A SER B 2 102 ? 15.307  10.489  1.478   0.60 13.85  ? 102  SER F N   1 
ATOM   1997 N  N   B SER B 2 102 ? 15.368  10.416  1.502   0.40 13.43  ? 102  SER F N   1 
ATOM   1998 C  CA  A SER B 2 102 ? 16.595  10.266  2.100   0.60 14.58  ? 102  SER F CA  1 
ATOM   1999 C  CA  B SER B 2 102 ? 16.557  10.009  2.253   0.40 13.95  ? 102  SER F CA  1 
ATOM   2000 C  C   A SER B 2 102 ? 16.605  10.600  3.592   0.60 12.98  ? 102  SER F C   1 
ATOM   2001 C  C   B SER B 2 102 ? 16.510  10.357  3.726   0.40 13.03  ? 102  SER F C   1 
ATOM   2002 O  O   A SER B 2 102 ? 17.665  10.489  4.217   0.60 14.04  ? 102  SER F O   1 
ATOM   2003 O  O   B SER B 2 102 ? 17.380  9.936   4.498   0.40 14.28  ? 102  SER F O   1 
ATOM   2004 C  CB  A SER B 2 102 ? 17.660  11.159  1.412   0.60 15.84  ? 102  SER F CB  1 
ATOM   2005 C  CB  B SER B 2 102 ? 17.809  10.636  1.661   0.40 14.35  ? 102  SER F CB  1 
ATOM   2006 O  OG  A SER B 2 102 ? 17.517  12.511  1.824   0.60 19.55  ? 102  SER F OG  1 
ATOM   2007 O  OG  B SER B 2 102 ? 17.892  10.360  0.280   0.40 17.04  ? 102  SER F OG  1 
ATOM   2008 N  N   . VAL B 2 103 ? 15.479  11.078  4.144   1.00 12.41  ? 103  VAL F N   1 
ATOM   2009 C  CA  . VAL B 2 103 ? 15.400  11.511  5.531   1.00 12.23  ? 103  VAL F CA  1 
ATOM   2010 C  C   . VAL B 2 103 ? 14.636  10.523  6.433   1.00 11.96  ? 103  VAL F C   1 
ATOM   2011 O  O   . VAL B 2 103 ? 15.107  10.177  7.522   1.00 13.04  ? 103  VAL F O   1 
ATOM   2012 C  CB  . VAL B 2 103 ? 14.842  12.960  5.601   1.00 11.77  ? 103  VAL F CB  1 
ATOM   2013 C  CG1 . VAL B 2 103 ? 14.676  13.407  7.024   1.00 13.46  ? 103  VAL F CG1 1 
ATOM   2014 C  CG2 . VAL B 2 103 ? 15.767  13.903  4.883   1.00 14.46  ? 103  VAL F CG2 1 
ATOM   2015 N  N   . ILE B 2 104 ? 13.488  10.028  5.987   1.00 11.66  ? 104  ILE F N   1 
ATOM   2016 C  CA  . ILE B 2 104 ? 12.879  8.901   6.678   1.00 10.91  ? 104  ILE F CA  1 
ATOM   2017 C  C   . ILE B 2 104 ? 13.810  7.685   6.611   1.00 11.31  ? 104  ILE F C   1 
ATOM   2018 O  O   . ILE B 2 104 ? 14.678  7.588   5.746   1.00 12.66  ? 104  ILE F O   1 
ATOM   2019 C  CB  . ILE B 2 104 ? 11.487  8.566   6.093   1.00 10.37  ? 104  ILE F CB  1 
ATOM   2020 C  CG1 . ILE B 2 104 ? 11.560  8.116   4.638   1.00 10.24  ? 104  ILE F CG1 1 
ATOM   2021 C  CG2 . ILE B 2 104 ? 10.515  9.722   6.317   1.00 11.23  ? 104  ILE F CG2 1 
ATOM   2022 C  CD1 . ILE B 2 104 ? 10.261  7.581   4.051   1.00 10.79  ? 104  ILE F CD1 1 
ATOM   2023 N  N   A SER B 2 105 ? 13.595  6.761   7.535   0.70 11.09  ? 105  SER F N   1 
ATOM   2024 N  N   B SER B 2 105 ? 13.582  6.729   7.496   0.30 11.88  ? 105  SER F N   1 
ATOM   2025 C  CA  A SER B 2 105 ? 14.300  5.479   7.555   0.70 10.24  ? 105  SER F CA  1 
ATOM   2026 C  CA  B SER B 2 105 ? 14.277  5.450   7.433   0.30 12.04  ? 105  SER F CA  1 
ATOM   2027 C  C   A SER B 2 105 ? 13.371  4.384   8.052   0.70 10.94  ? 105  SER F C   1 
ATOM   2028 C  C   B SER B 2 105 ? 13.385  4.385   8.029   0.30 11.84  ? 105  SER F C   1 
ATOM   2029 O  O   A SER B 2 105 ? 12.356  4.671   8.688   0.70 10.77  ? 105  SER F O   1 
ATOM   2030 O  O   B SER B 2 105 ? 12.399  4.693   8.696   0.30 11.70  ? 105  SER F O   1 
ATOM   2031 C  CB  A SER B 2 105 ? 15.531  5.560   8.438   0.70 10.82  ? 105  SER F CB  1 
ATOM   2032 C  CB  B SER B 2 105 ? 15.588  5.511   8.199   0.30 12.61  ? 105  SER F CB  1 
ATOM   2033 O  OG  A SER B 2 105 ? 16.324  4.421   8.197   0.70 10.38  ? 105  SER F OG  1 
ATOM   2034 O  OG  B SER B 2 105 ? 15.320  5.692   9.571   0.30 15.17  ? 105  SER F OG  1 
ATOM   2035 N  N   . LEU B 2 106 ? 13.748  3.131   7.783   1.00 11.38  ? 106  LEU F N   1 
ATOM   2036 C  CA  . LEU B 2 106 ? 13.063  1.998   8.376   1.00 12.35  ? 106  LEU F CA  1 
ATOM   2037 C  C   . LEU B 2 106 ? 13.924  1.324   9.443   1.00 13.84  ? 106  LEU F C   1 
ATOM   2038 O  O   . LEU B 2 106 ? 13.632  0.219   9.895   1.00 15.33  ? 106  LEU F O   1 
ATOM   2039 C  CB  . LEU B 2 106 ? 12.666  0.991   7.308   1.00 12.75  ? 106  LEU F CB  1 
ATOM   2040 C  CG  . LEU B 2 106 ? 11.819  1.532   6.148   1.00 11.65  ? 106  LEU F CG  1 
ATOM   2041 C  CD1 . LEU B 2 106 ? 11.494  0.446   5.130   1.00 13.04  ? 106  LEU F CD1 1 
ATOM   2042 C  CD2 . LEU B 2 106 ? 10.525  2.175   6.679   1.00 12.91  ? 106  LEU F CD2 1 
ATOM   2043 N  N   . SER B 2 107 ? 14.963  2.013   9.882   1.00 15.30  ? 107  SER F N   1 
ATOM   2044 C  CA  . SER B 2 107 ? 15.671  1.610   11.102  1.00 18.10  ? 107  SER F CA  1 
ATOM   2045 C  C   . SER B 2 107 ? 16.340  2.822   11.762  1.00 18.54  ? 107  SER F C   1 
ATOM   2046 O  O   . SER B 2 107 ? 16.294  3.932   11.235  1.00 18.33  ? 107  SER F O   1 
ATOM   2047 C  CB  . SER B 2 107 ? 16.662  0.487   10.802  1.00 19.98  ? 107  SER F CB  1 
ATOM   2048 O  OG  . SER B 2 107 ? 17.617  0.881   9.857   1.00 23.29  ? 107  SER F OG  1 
ATOM   2049 N  N   . GLY B 2 108 ? 16.925  2.639   12.941  1.00 19.32  ? 108  GLY F N   1 
ATOM   2050 C  CA  . GLY B 2 108 ? 17.575  3.766   13.627  1.00 20.00  ? 108  GLY F CA  1 
ATOM   2051 C  C   . GLY B 2 108 ? 16.684  4.874   14.200  1.00 20.60  ? 108  GLY F C   1 
ATOM   2052 O  O   . GLY B 2 108 ? 15.460  4.696   14.328  1.00 21.16  ? 108  GLY F O   1 
ATOM   2053 N  N   . ASP B 2 109 ? 17.285  6.037   14.528  1.00 21.30  ? 109  ASP F N   1 
ATOM   2054 C  CA  . ASP B 2 109 ? 16.581  7.112   15.278  1.00 21.65  ? 109  ASP F CA  1 
ATOM   2055 C  C   . ASP B 2 109 ? 15.455  7.723   14.451  1.00 20.23  ? 109  ASP F C   1 
ATOM   2056 O  O   . ASP B 2 109 ? 14.508  8.270   15.002  1.00 21.66  ? 109  ASP F O   1 
ATOM   2057 C  CB  . ASP B 2 109 ? 17.537  8.274   15.794  1.00 22.31  ? 109  ASP F CB  1 
ATOM   2058 C  CG  . ASP B 2 109 ? 16.945  9.077   17.059  0.60 22.35  ? 109  ASP F CG  1 
ATOM   2059 O  OD1 . ASP B 2 109 ? 16.297  8.402   17.892  0.30 21.66  ? 109  ASP F OD1 1 
ATOM   2060 O  OD2 . ASP B 2 109 ? 17.120  10.349  17.291  1.00 22.98  ? 109  ASP F OD2 1 
ATOM   2061 N  N   . HIS B 2 110 ? 15.589  7.667   13.126  1.00 16.59  ? 110  HIS F N   1 
ATOM   2062 C  CA  . HIS B 2 110 ? 14.599  8.276   12.237  1.00 14.75  ? 110  HIS F CA  1 
ATOM   2063 C  C   . HIS B 2 110 ? 13.636  7.245   11.652  1.00 13.14  ? 110  HIS F C   1 
ATOM   2064 O  O   . HIS B 2 110 ? 12.954  7.481   10.657  1.00 12.40  ? 110  HIS F O   1 
ATOM   2065 C  CB  . HIS B 2 110 ? 15.296  9.088   11.169  1.00 14.63  ? 110  HIS F CB  1 
ATOM   2066 C  CG  . HIS B 2 110 ? 16.048  10.253  11.727  1.00 16.68  ? 110  HIS F CG  1 
ATOM   2067 N  ND1 . HIS B 2 110 ? 16.884  11.034  10.960  1.00 20.74  ? 110  HIS F ND1 1 
ATOM   2068 C  CD2 . HIS B 2 110 ? 16.140  10.726  12.991  1.00 18.81  ? 110  HIS F CD2 1 
ATOM   2069 C  CE1 . HIS B 2 110 ? 17.421  11.971  11.721  1.00 21.13  ? 110  HIS F CE1 1 
ATOM   2070 N  NE2 . HIS B 2 110 ? 16.982  11.808  12.958  1.00 19.21  ? 110  HIS F NE2 1 
ATOM   2071 N  N   . CYS B 2 111 ? 13.573  6.085   12.284  1.00 12.95  ? 111  CYS F N   1 
ATOM   2072 C  CA  . CYS B 2 111 ? 12.702  4.992   11.850  1.00 12.73  ? 111  CYS F CA  1 
ATOM   2073 C  C   . CYS B 2 111 ? 11.242  5.442   11.982  1.00 11.04  ? 111  CYS F C   1 
ATOM   2074 O  O   . CYS B 2 111 ? 10.809  5.967   13.020  1.00 11.43  ? 111  CYS F O   1 
ATOM   2075 C  CB  . CYS B 2 111 ? 12.930  3.765   12.723  1.00 13.24  ? 111  CYS F CB  1 
ATOM   2076 S  SG  . CYS B 2 111 ? 11.976  2.369   12.227  1.00 16.24  ? 111  CYS F SG  1 
ATOM   2077 N  N   . ILE B 2 112 ? 10.493  5.191   10.923  1.00 10.20  ? 112  ILE F N   1 
ATOM   2078 C  CA  . ILE B 2 112 ? 9.081   5.545   10.881  1.00 9.15   ? 112  ILE F CA  1 
ATOM   2079 C  C   . ILE B 2 112 ? 8.140   4.380   11.171  1.00 9.01   ? 112  ILE F C   1 
ATOM   2080 O  O   . ILE B 2 112 ? 6.936   4.572   11.302  1.00 9.93   ? 112  ILE F O   1 
ATOM   2081 C  CB  . ILE B 2 112 ? 8.739   6.193   9.533   1.00 9.48   ? 112  ILE F CB  1 
ATOM   2082 C  CG1 . ILE B 2 112 ? 8.933   5.225   8.366   1.00 11.02  ? 112  ILE F CG1 1 
ATOM   2083 C  CG2 . ILE B 2 112 ? 9.522   7.527   9.385   1.00 10.77  ? 112  ILE F CG2 1 
ATOM   2084 C  CD1 . ILE B 2 112 ? 8.442   5.756   7.017   1.00 11.93  ? 112  ILE F CD1 1 
ATOM   2085 N  N   A THR B 2 113 ? 8.704   3.184   11.293  0.50 9.19   ? 113  THR F N   1 
ATOM   2086 N  N   B THR B 2 113 ? 8.662   3.154   11.225  0.50 9.61   ? 113  THR F N   1 
ATOM   2087 C  CA  A THR B 2 113 ? 7.896   2.032   11.610  0.50 9.53   ? 113  THR F CA  1 
ATOM   2088 C  CA  B THR B 2 113 ? 7.779   2.027   11.498  0.50 10.17  ? 113  THR F CA  1 
ATOM   2089 C  C   A THR B 2 113 ? 7.280   2.209   13.007  0.50 8.80   ? 113  THR F C   1 
ATOM   2090 C  C   B THR B 2 113 ? 7.299   2.127   12.957  0.50 9.29   ? 113  THR F C   1 
ATOM   2091 O  O   A THR B 2 113 ? 7.894   2.763   13.918  0.50 9.53   ? 113  THR F O   1 
ATOM   2092 O  O   B THR B 2 113 ? 8.049   2.507   13.854  0.50 10.53  ? 113  THR F O   1 
ATOM   2093 C  CB  A THR B 2 113 ? 8.750   0.780   11.508  0.50 9.69   ? 113  THR F CB  1 
ATOM   2094 C  CB  B THR B 2 113 ? 8.454   0.685   11.196  0.50 10.81  ? 113  THR F CB  1 
ATOM   2095 O  OG1 A THR B 2 113 ? 9.426   0.841   10.250  0.50 11.59  ? 113  THR F OG1 1 
ATOM   2096 O  OG1 B THR B 2 113 ? 9.432   0.385   12.192  0.50 15.37  ? 113  THR F OG1 1 
ATOM   2097 C  CG2 A THR B 2 113 ? 7.869   -0.462  11.605  0.50 11.05  ? 113  THR F CG2 1 
ATOM   2098 C  CG2 B THR B 2 113 ? 9.087   0.772   9.819   0.50 10.99  ? 113  THR F CG2 1 
ATOM   2099 N  N   . GLY B 2 114 ? 6.024   1.804   13.163  1.00 8.49   ? 114  GLY F N   1 
ATOM   2100 C  CA  . GLY B 2 114 ? 5.348   2.022   14.403  1.00 7.94   ? 114  GLY F CA  1 
ATOM   2101 C  C   . GLY B 2 114 ? 4.723   3.385   14.587  1.00 7.83   ? 114  GLY F C   1 
ATOM   2102 O  O   . GLY B 2 114 ? 4.167   3.665   15.606  1.00 8.41   ? 114  GLY F O   1 
ATOM   2103 N  N   . ARG B 2 115 ? 4.879   4.245   13.591  1.00 7.29   ? 115  ARG F N   1 
ATOM   2104 C  CA  . ARG B 2 115 ? 4.280   5.587   13.591  1.00 7.00   ? 115  ARG F CA  1 
ATOM   2105 C  C   . ARG B 2 115 ? 3.131   5.629   12.592  1.00 7.67   ? 115  ARG F C   1 
ATOM   2106 O  O   . ARG B 2 115 ? 2.842   4.645   11.958  1.00 11.61  ? 115  ARG F O   1 
ATOM   2107 C  CB  . ARG B 2 115 ? 5.365   6.636   13.318  1.00 7.74   ? 115  ARG F CB  1 
ATOM   2108 C  CG  . ARG B 2 115 ? 6.531   6.475   14.292  1.00 9.69   ? 115  ARG F CG  1 
ATOM   2109 C  CD  . ARG B 2 115 ? 7.501   7.616   14.216  1.00 9.59   ? 115  ARG F CD  1 
ATOM   2110 N  NE  . ARG B 2 115 ? 8.703   7.342   15.006  1.00 10.72  ? 115  ARG F NE  1 
ATOM   2111 C  CZ  . ARG B 2 115 ? 8.881   7.662   16.293  1.00 11.21  ? 115  ARG F CZ  1 
ATOM   2112 N  NH1 . ARG B 2 115 ? 7.924   8.257   16.972  1.00 12.39  ? 115  ARG F NH1 1 
ATOM   2113 N  NH2 . ARG B 2 115 ? 10.025  7.369   16.900  1.00 13.12  ? 115  ARG F NH2 1 
ATOM   2114 N  N   . THR B 2 116 ? 2.418   6.734   12.472  1.00 7.99   ? 116  THR F N   1 
ATOM   2115 C  CA  . THR B 2 116 ? 1.225   6.787   11.631  1.00 8.23   ? 116  THR F CA  1 
ATOM   2116 C  C   . THR B 2 116 ? 1.500   7.607   10.380  1.00 7.96   ? 116  THR F C   1 
ATOM   2117 O  O   . THR B 2 116 ? 2.022   8.717   10.467  1.00 10.15  ? 116  THR F O   1 
ATOM   2118 C  CB  . THR B 2 116 ? 0.084   7.443   12.408  1.00 8.43   ? 116  THR F CB  1 
ATOM   2119 O  OG1 . THR B 2 116 ? -0.252  6.644   13.539  1.00 10.05  ? 116  THR F OG1 1 
ATOM   2120 C  CG2 . THR B 2 116 ? -1.169  7.633   11.580  1.00 9.12   ? 116  THR F CG2 1 
ATOM   2121 N  N   . LEU B 2 117 ? 1.087   7.078   9.231   1.00 7.89   ? 117  LEU F N   1 
ATOM   2122 C  CA  . LEU B 2 117 ? 1.061   7.833   7.991   1.00 7.61   ? 117  LEU F CA  1 
ATOM   2123 C  C   . LEU B 2 117 ? -0.319  8.437   7.843   1.00 7.59   ? 117  LEU F C   1 
ATOM   2124 O  O   . LEU B 2 117 ? -1.319  7.748   8.087   1.00 8.76   ? 117  LEU F O   1 
ATOM   2125 C  CB  . LEU B 2 117 ? 1.375   6.880   6.850   1.00 8.00   ? 117  LEU F CB  1 
ATOM   2126 C  CG  . LEU B 2 117 ? 1.505   7.488   5.468   1.00 8.51   ? 117  LEU F CG  1 
ATOM   2127 C  CD1 . LEU B 2 117 ? 2.757   8.378   5.364   1.00 10.68  ? 117  LEU F CD1 1 
ATOM   2128 C  CD2 . LEU B 2 117 ? 1.561   6.350   4.402   1.00 10.70  ? 117  LEU F CD2 1 
ATOM   2129 N  N   . VAL B 2 118 ? -0.383  9.717   7.474   1.00 7.55   ? 118  VAL F N   1 
ATOM   2130 C  CA  . VAL B 2 118 ? -1.633  10.431  7.380   1.00 7.93   ? 118  VAL F CA  1 
ATOM   2131 C  C   . VAL B 2 118 ? -1.727  11.127  6.042   1.00 7.87   ? 118  VAL F C   1 
ATOM   2132 O  O   . VAL B 2 118 ? -0.756  11.773  5.588   1.00 8.73   ? 118  VAL F O   1 
ATOM   2133 C  CB  . VAL B 2 118 ? -1.730  11.512  8.462   1.00 7.74   ? 118  VAL F CB  1 
ATOM   2134 C  CG1 . VAL B 2 118 ? -3.051  12.321  8.354   1.00 10.25  ? 118  VAL F CG1 1 
ATOM   2135 C  CG2 . VAL B 2 118 ? -1.617  10.920  9.855   1.00 9.40   ? 118  VAL F CG2 1 
ATOM   2136 N  N   . VAL B 2 119 ? -2.904  11.066  5.420   1.00 8.13   ? 119  VAL F N   1 
ATOM   2137 C  CA  . VAL B 2 119 ? -3.217  11.894  4.253   1.00 8.46   ? 119  VAL F CA  1 
ATOM   2138 C  C   . VAL B 2 119 ? -4.276  12.910  4.660   1.00 9.30   ? 119  VAL F C   1 
ATOM   2139 O  O   . VAL B 2 119 ? -5.258  12.590  5.310   1.00 9.49   ? 119  VAL F O   1 
ATOM   2140 C  CB  . VAL B 2 119 ? -3.622  11.051  2.985   1.00 10.25  ? 119  VAL F CB  1 
ATOM   2141 C  CG1 . VAL B 2 119 ? -4.833  10.171  3.244   1.00 12.26  ? 119  VAL F CG1 1 
ATOM   2142 C  CG2 . VAL B 2 119 ? -3.789  11.936  1.748   1.00 11.59  ? 119  VAL F CG2 1 
ATOM   2143 N  N   . HIS B 2 120 ? -4.014  14.155  4.276   1.00 9.07   ? 120  HIS F N   1 
ATOM   2144 C  CA  . HIS B 2 120 ? -4.783  15.312  4.761   1.00 10.31  ? 120  HIS F CA  1 
ATOM   2145 C  C   . HIS B 2 120 ? -5.811  15.835  3.771   1.00 10.98  ? 120  HIS F C   1 
ATOM   2146 O  O   . HIS B 2 120 ? -5.795  15.534  2.581   1.00 11.91  ? 120  HIS F O   1 
ATOM   2147 C  CB  . HIS B 2 120 ? -3.825  16.433  5.139   1.00 10.22  ? 120  HIS F CB  1 
ATOM   2148 C  CG  . HIS B 2 120 ? -3.041  16.174  6.383   1.00 10.75  ? 120  HIS F CG  1 
ATOM   2149 N  ND1 . HIS B 2 120 ? -3.413  16.678  7.613   1.00 10.32  ? 120  HIS F ND1 1 
ATOM   2150 C  CD2 . HIS B 2 120 ? -1.934  15.426  6.610   1.00 10.42  ? 120  HIS F CD2 1 
ATOM   2151 C  CE1 . HIS B 2 120 ? -2.568  16.243  8.540   1.00 10.96  ? 120  HIS F CE1 1 
ATOM   2152 N  NE2 . HIS B 2 120 ? -1.656  15.492  7.957   1.00 10.77  ? 120  HIS F NE2 1 
ATOM   2153 N  N   A GLU B 2 121 ? -6.696  16.641  4.342   0.80 11.41  ? 121  GLU F N   1 
ATOM   2154 N  N   B GLU B 2 121 ? -6.721  16.656  4.279   0.20 11.84  ? 121  GLU F N   1 
ATOM   2155 C  CA  A GLU B 2 121 ? -7.793  17.312  3.636   0.80 12.95  ? 121  GLU F CA  1 
ATOM   2156 C  CA  B GLU B 2 121 ? -7.805  17.202  3.462   0.20 12.56  ? 121  GLU F CA  1 
ATOM   2157 C  C   A GLU B 2 121 ? -7.358  18.180  2.454   0.80 12.82  ? 121  GLU F C   1 
ATOM   2158 C  C   B GLU B 2 121 ? -7.353  18.197  2.392   0.20 13.03  ? 121  GLU F C   1 
ATOM   2159 O  O   A GLU B 2 121 ? -8.008  18.187  1.393   0.80 13.13  ? 121  GLU F O   1 
ATOM   2160 O  O   B GLU B 2 121 ? -7.957  18.271  1.317   0.20 13.27  ? 121  GLU F O   1 
ATOM   2161 C  CB  A GLU B 2 121 ? -8.486  18.196  4.689   0.80 13.94  ? 121  GLU F CB  1 
ATOM   2162 C  CB  B GLU B 2 121 ? -8.815  17.889  4.370   0.20 12.89  ? 121  GLU F CB  1 
ATOM   2163 C  CG  A GLU B 2 121 ? -9.687  19.005  4.244   0.80 17.52  ? 121  GLU F CG  1 
ATOM   2164 C  CG  B GLU B 2 121 ? -9.688  18.892  3.656   0.20 14.00  ? 121  GLU F CG  1 
ATOM   2165 C  CD  A GLU B 2 121 ? -10.037 20.155  5.214   0.80 18.75  ? 121  GLU F CD  1 
ATOM   2166 C  CD  B GLU B 2 121 ? -11.022 18.321  3.304   0.20 15.44  ? 121  GLU F CD  1 
ATOM   2167 O  OE1 A GLU B 2 121 ? -9.461  20.281  6.341   0.80 17.92  ? 121  GLU F OE1 1 
ATOM   2168 O  OE1 B GLU B 2 121 ? -11.356 17.250  3.843   0.20 15.52  ? 121  GLU F OE1 1 
ATOM   2169 O  OE2 A GLU B 2 121 ? -10.916 20.946  4.826   0.80 23.77  ? 121  GLU F OE2 1 
ATOM   2170 O  OE2 B GLU B 2 121 ? -11.741 18.930  2.485   0.20 16.87  ? 121  GLU F OE2 1 
ATOM   2171 N  N   . LYS B 2 122 ? -6.312  18.968  2.698   1.00 13.50  ? 122  LYS F N   1 
ATOM   2172 C  CA  . LYS B 2 122 ? -5.913  20.111  1.899   1.00 14.97  ? 122  LYS F CA  1 
ATOM   2173 C  C   . LYS B 2 122 ? -4.420  19.992  1.507   1.00 11.97  ? 122  LYS F C   1 
ATOM   2174 O  O   . LYS B 2 122 ? -3.684  19.090  1.971   1.00 12.58  ? 122  LYS F O   1 
ATOM   2175 C  CB  . LYS B 2 122 ? -6.144  21.491  2.715   1.00 16.37  ? 122  LYS F CB  1 
ATOM   2176 C  CG  . LYS B 2 122 ? -7.411  21.737  3.559   1.00 21.03  ? 122  LYS F CG  1 
ATOM   2177 C  CD  . LYS B 2 122 ? -7.287  23.048  4.431   1.00 22.55  ? 122  LYS F CD  1 
ATOM   2178 C  CE  . LYS B 2 122 ? -6.341  24.099  3.866   1.00 27.50  ? 122  LYS F CE  1 
ATOM   2179 N  NZ  . LYS B 2 122 ? -5.970  25.204  4.804   1.00 30.73  ? 122  LYS F NZ  1 
ATOM   2180 N  N   . ALA B 2 123 ? -3.968  20.918  0.687   1.00 11.95  ? 123  ALA F N   1 
ATOM   2181 C  CA  . ALA B 2 123 ? -2.581  20.977  0.286   1.00 11.79  ? 123  ALA F CA  1 
ATOM   2182 C  C   . ALA B 2 123 ? -1.685  21.380  1.445   1.00 11.85  ? 123  ALA F C   1 
ATOM   2183 O  O   . ALA B 2 123 ? -2.022  22.224  2.264   1.00 12.42  ? 123  ALA F O   1 
ATOM   2184 C  CB  . ALA B 2 123 ? -2.411  21.968  -0.882  1.00 13.13  ? 123  ALA F CB  1 
ATOM   2185 N  N   . ASP B 2 124 ? -0.516  20.758  1.463   1.00 11.52  ? 124  ASP F N   1 
ATOM   2186 C  CA  . ASP B 2 124 ? 0.598   21.191  2.284   1.00 11.89  ? 124  ASP F CA  1 
ATOM   2187 C  C   . ASP B 2 124 ? 1.350   22.270  1.496   1.00 12.35  ? 124  ASP F C   1 
ATOM   2188 O  O   . ASP B 2 124 ? 1.745   22.058  0.346   1.00 13.08  ? 124  ASP F O   1 
ATOM   2189 C  CB  . ASP B 2 124 ? 1.471   19.979  2.571   1.00 11.29  ? 124  ASP F CB  1 
ATOM   2190 C  CG  . ASP B 2 124 ? 2.642   20.238  3.496   1.00 11.22  ? 124  ASP F CG  1 
ATOM   2191 O  OD1 . ASP B 2 124 ? 3.040   21.395  3.752   1.00 12.82  ? 124  ASP F OD1 1 
ATOM   2192 O  OD2 . ASP B 2 124 ? 3.203   19.233  3.974   1.00 12.01  ? 124  ASP F OD2 1 
ATOM   2193 N  N   . ASP B 2 125 ? 1.496   23.427  2.107   1.00 12.11  ? 125  ASP F N   1 
ATOM   2194 C  CA  . ASP B 2 125 ? 2.185   24.545  1.456   1.00 12.45  ? 125  ASP F CA  1 
ATOM   2195 C  C   . ASP B 2 125 ? 3.712   24.464  1.599   1.00 12.14  ? 125  ASP F C   1 
ATOM   2196 O  O   . ASP B 2 125 ? 4.429   25.401  1.221   1.00 13.46  ? 125  ASP F O   1 
ATOM   2197 C  CB  . ASP B 2 125 ? 1.636   25.887  1.936   1.00 13.55  ? 125  ASP F CB  1 
ATOM   2198 C  CG  . ASP B 2 125 ? 1.873   26.157  3.429   1.00 13.85  ? 125  ASP F CG  1 
ATOM   2199 O  OD1 . ASP B 2 125 ? 2.825   25.595  4.030   1.00 14.29  ? 125  ASP F OD1 1 
ATOM   2200 O  OD2 . ASP B 2 125 ? 1.102   26.977  4.009   1.00 16.31  ? 125  ASP F OD2 1 
ATOM   2201 N  N   . LEU B 2 126 ? 4.209   23.363  2.183   1.00 12.63  ? 126  LEU F N   1 
ATOM   2202 C  CA  . LEU B 2 126 ? 5.644   23.057  2.277   1.00 13.30  ? 126  LEU F CA  1 
ATOM   2203 C  C   . LEU B 2 126 ? 6.402   24.106  3.058   1.00 13.28  ? 126  LEU F C   1 
ATOM   2204 O  O   . LEU B 2 126 ? 7.600   24.271  2.873   1.00 14.60  ? 126  LEU F O   1 
ATOM   2205 C  CB  . LEU B 2 126 ? 6.275   22.762  0.907   1.00 13.30  ? 126  LEU F CB  1 
ATOM   2206 C  CG  . LEU B 2 126 ? 5.523   21.780  -0.014  1.00 13.32  ? 126  LEU F CG  1 
ATOM   2207 C  CD1 . LEU B 2 126 ? 6.349   21.441  -1.271  1.00 16.08  ? 126  LEU F CD1 1 
ATOM   2208 C  CD2 . LEU B 2 126 ? 5.142   20.471  0.709   1.00 14.44  ? 126  LEU F CD2 1 
ATOM   2209 N  N   . GLY B 2 127 ? 5.719   24.740  4.008   1.00 12.82  ? 127  GLY F N   1 
ATOM   2210 C  CA  . GLY B 2 127 ? 6.302   25.777  4.861   1.00 14.17  ? 127  GLY F CA  1 
ATOM   2211 C  C   . GLY B 2 127 ? 6.484   27.120  4.181   1.00 14.36  ? 127  GLY F C   1 
ATOM   2212 O  O   . GLY B 2 127 ? 7.142   28.008  4.753   1.00 16.41  ? 127  GLY F O   1 
ATOM   2213 N  N   . LYS B 2 128 ? 5.913   27.290  2.984   1.00 14.41  ? 128  LYS F N   1 
ATOM   2214 C  CA  . LYS B 2 128 ? 6.111   28.497  2.156   1.00 15.26  ? 128  LYS F CA  1 
ATOM   2215 C  C   . LYS B 2 128 ? 4.871   29.378  2.159   1.00 15.67  ? 128  LYS F C   1 
ATOM   2216 O  O   . LYS B 2 128 ? 4.746   30.289  1.333   1.00 16.64  ? 128  LYS F O   1 
ATOM   2217 C  CB  . LYS B 2 128 ? 6.469   28.106  0.713   1.00 16.34  ? 128  LYS F CB  1 
ATOM   2218 C  CG  . LYS B 2 128 ? 7.781   27.378  0.540   1.00 20.05  ? 128  LYS F CG  1 
ATOM   2219 C  CD  . LYS B 2 128 ? 8.945   28.363  0.482   0.60 21.80  ? 128  LYS F CD  1 
ATOM   2220 C  CE  . LYS B 2 128 ? 10.310  27.677  0.540   0.60 22.43  ? 128  LYS F CE  1 
ATOM   2221 N  NZ  . LYS B 2 128 ? 10.728  27.373  1.946   0.60 23.86  ? 128  LYS F NZ  1 
ATOM   2222 N  N   . GLY B 2 129 ? 3.944   29.138  3.082   1.00 15.45  ? 129  GLY F N   1 
ATOM   2223 C  CA  . GLY B 2 129 ? 2.662   29.839  3.105   1.00 16.83  ? 129  GLY F CA  1 
ATOM   2224 C  C   . GLY B 2 129 ? 2.651   31.200  3.757   1.00 17.97  ? 129  GLY F C   1 
ATOM   2225 O  O   . GLY B 2 129 ? 1.665   31.926  3.599   1.00 20.40  ? 129  GLY F O   1 
ATOM   2226 N  N   . GLY B 2 130 ? 3.720   31.554  4.472   1.00 18.34  ? 130  GLY F N   1 
ATOM   2227 C  CA  . GLY B 2 130 ? 3.896   32.899  5.045   1.00 20.46  ? 130  GLY F CA  1 
ATOM   2228 C  C   . GLY B 2 130 ? 3.098   33.184  6.305   1.00 21.54  ? 130  GLY F C   1 
ATOM   2229 O  O   . GLY B 2 130 ? 2.800   34.345  6.617   1.00 23.99  ? 130  GLY F O   1 
ATOM   2230 N  N   . ASN B 2 131 ? 2.755   32.140  7.037   1.00 21.70  ? 131  ASN F N   1 
ATOM   2231 C  CA  . ASN B 2 131 ? 2.069   32.306  8.312   1.00 20.63  ? 131  ASN F CA  1 
ATOM   2232 C  C   . ASN B 2 131 ? 2.598   31.292  9.308   1.00 21.42  ? 131  ASN F C   1 
ATOM   2233 O  O   . ASN B 2 131 ? 3.396   30.411  8.967   1.00 21.26  ? 131  ASN F O   1 
ATOM   2234 C  CB  . ASN B 2 131 ? 0.558   32.210  8.135   1.00 20.29  ? 131  ASN F CB  1 
ATOM   2235 C  CG  . ASN B 2 131 ? 0.117   30.915  7.445   1.00 21.11  ? 131  ASN F CG  1 
ATOM   2236 O  OD1 . ASN B 2 131 ? 0.456   29.800  7.869   1.00 19.93  ? 131  ASN F OD1 1 
ATOM   2237 N  ND2 . ASN B 2 131 ? -0.652  31.065  6.361   1.00 24.45  ? 131  ASN F ND2 1 
ATOM   2238 N  N   . GLU B 2 132 ? 2.161   31.429  10.549  1.00 21.47  ? 132  GLU F N   1 
ATOM   2239 C  CA  . GLU B 2 132 ? 2.700   30.662  11.660  1.00 22.23  ? 132  GLU F CA  1 
ATOM   2240 C  C   . GLU B 2 132 ? 2.452   29.157  11.495  1.00 21.46  ? 132  GLU F C   1 
ATOM   2241 O  O   . GLU B 2 132 ? 3.344   28.297  11.702  1.00 21.99  ? 132  GLU F O   1 
ATOM   2242 C  CB  . GLU B 2 132 ? 2.026   31.139  12.939  1.00 23.32  ? 132  GLU F CB  1 
ATOM   2243 C  CG  . GLU B 2 132 ? 2.684   30.704  14.241  0.50 25.16  ? 132  GLU F CG  1 
ATOM   2244 C  CD  . GLU B 2 132 ? 2.065   31.395  15.452  0.50 28.39  ? 132  GLU F CD  1 
ATOM   2245 O  OE1 . GLU B 2 132 ? 0.940   31.925  15.321  0.50 30.10  ? 132  GLU F OE1 1 
ATOM   2246 O  OE2 . GLU B 2 132 ? 2.699   31.426  16.533  0.50 30.87  ? 132  GLU F OE2 1 
ATOM   2247 N  N   . GLU B 2 133 ? 1.232   28.837  11.104  1.00 20.34  ? 133  GLU F N   1 
ATOM   2248 C  CA  . GLU B 2 133 ? 0.880   27.433  10.974  1.00 18.85  ? 133  GLU F CA  1 
ATOM   2249 C  C   . GLU B 2 133 ? 1.621   26.787  9.777   1.00 16.86  ? 133  GLU F C   1 
ATOM   2250 O  O   . GLU B 2 133 ? 1.866   25.573  9.818   1.00 16.09  ? 133  GLU F O   1 
ATOM   2251 C  CB  . GLU B 2 133 ? -0.656  27.262  10.950  1.00 20.18  ? 133  GLU F CB  1 
ATOM   2252 C  CG  . GLU B 2 133 ? -1.232  25.807  11.099  1.00 21.85  ? 133  GLU F CG  1 
ATOM   2253 C  CD  . GLU B 2 133 ? -1.224  25.117  12.532  0.70 22.35  ? 133  GLU F CD  1 
ATOM   2254 O  OE1 . GLU B 2 133 ? -0.347  25.357  13.411  0.70 21.44  ? 133  GLU F OE1 1 
ATOM   2255 O  OE2 . GLU B 2 133 ? -2.108  24.229  12.755  0.70 22.89  ? 133  GLU F OE2 1 
ATOM   2256 N  N   . SER B 2 134 ? 2.051   27.538  8.759   1.00 15.08  ? 134  SER F N   1 
ATOM   2257 C  CA  . SER B 2 134 ? 2.738   26.958  7.633   1.00 14.66  ? 134  SER F CA  1 
ATOM   2258 C  C   . SER B 2 134 ? 3.966   26.214  8.075   1.00 14.38  ? 134  SER F C   1 
ATOM   2259 O  O   . SER B 2 134 ? 4.256   25.166  7.538   1.00 14.46  ? 134  SER F O   1 
ATOM   2260 C  CB  . SER B 2 134 ? 3.131   28.034  6.630   1.00 14.93  ? 134  SER F CB  1 
ATOM   2261 O  OG  . SER B 2 134 ? 3.830   27.528  5.517   1.00 15.91  ? 134  SER F OG  1 
ATOM   2262 N  N   . THR B 2 135 ? 4.719   26.781  9.014   1.00 14.34  ? 135  THR F N   1 
ATOM   2263 C  CA  . THR B 2 135 ? 5.953   26.140  9.465   1.00 14.89  ? 135  THR F CA  1 
ATOM   2264 C  C   . THR B 2 135 ? 5.752   25.148  10.626  1.00 13.66  ? 135  THR F C   1 
ATOM   2265 O  O   . THR B 2 135 ? 6.736   24.666  11.217  1.00 14.47  ? 135  THR F O   1 
ATOM   2266 C  CB  . THR B 2 135 ? 7.060   27.135  9.766   1.00 15.83  ? 135  THR F CB  1 
ATOM   2267 O  OG1 . THR B 2 135 ? 6.584   28.074  10.711  1.00 19.90  ? 135  THR F OG1 1 
ATOM   2268 C  CG2 . THR B 2 135 ? 7.520   27.814  8.450   1.00 18.88  ? 135  THR F CG2 1 
ATOM   2269 N  N   . LYS B 2 136 ? 4.500   24.794  10.912  1.00 14.07  ? 136  LYS F N   1 
ATOM   2270 C  CA  . LYS B 2 136 ? 4.167   23.733  11.857  1.00 14.82  ? 136  LYS F CA  1 
ATOM   2271 C  C   . LYS B 2 136 ? 3.436   22.550  11.182  1.00 13.85  ? 136  LYS F C   1 
ATOM   2272 O  O   . LYS B 2 136 ? 3.847   21.377  11.325  1.00 14.21  ? 136  LYS F O   1 
ATOM   2273 C  CB  . LYS B 2 136 ? 3.308   24.290  13.010  1.00 15.35  ? 136  LYS F CB  1 
ATOM   2274 C  CG  . LYS B 2 136 ? 4.092   25.276  13.923  1.00 17.98  ? 136  LYS F CG  1 
ATOM   2275 C  CD  . LYS B 2 136 ? 3.244   26.098  14.924  1.00 19.27  ? 136  LYS F CD  1 
ATOM   2276 C  CE  . LYS B 2 136 ? 2.613   25.287  16.058  1.00 18.75  ? 136  LYS F CE  1 
ATOM   2277 N  NZ  . LYS B 2 136 ? 3.584   24.448  16.848  1.00 18.65  ? 136  LYS F NZ  1 
ATOM   2278 N  N   . THR B 2 137 ? 2.379   22.840  10.426  1.00 13.04  ? 137  THR F N   1 
ATOM   2279 C  CA  . THR B 2 137 ? 1.578   21.801  9.769   1.00 13.39  ? 137  THR F CA  1 
ATOM   2280 C  C   . THR B 2 137 ? 1.498   21.925  8.253   1.00 12.92  ? 137  THR F C   1 
ATOM   2281 O  O   . THR B 2 137 ? 0.955   21.046  7.580   1.00 12.83  ? 137  THR F O   1 
ATOM   2282 C  CB  . THR B 2 137 ? 0.130   21.835  10.247  1.00 14.72  ? 137  THR F CB  1 
ATOM   2283 O  OG1 . THR B 2 137 ? -0.445  23.067  9.817   1.00 15.15  ? 137  THR F OG1 1 
ATOM   2284 C  CG2 . THR B 2 137 ? 0.027   21.681  11.746  1.00 15.67  ? 137  THR F CG2 1 
ATOM   2285 N  N   . GLY B 2 138 ? 1.956   23.042  7.697   1.00 11.73  ? 138  GLY F N   1 
ATOM   2286 C  CA  . GLY B 2 138 ? 1.831   23.276  6.261   1.00 12.32  ? 138  GLY F CA  1 
ATOM   2287 C  C   . GLY B 2 138 ? 0.413   23.635  5.849   1.00 12.57  ? 138  GLY F C   1 
ATOM   2288 O  O   . GLY B 2 138 ? 0.114   23.667  4.672   1.00 13.06  ? 138  GLY F O   1 
ATOM   2289 N  N   . ASN B 2 139 ? -0.453  23.901  6.814   1.00 13.67  ? 139  ASN F N   1 
ATOM   2290 C  CA  . ASN B 2 139 ? -1.856  24.244  6.539   1.00 13.80  ? 139  ASN F CA  1 
ATOM   2291 C  C   . ASN B 2 139 ? -2.628  23.178  5.763   1.00 13.46  ? 139  ASN F C   1 
ATOM   2292 O  O   . ASN B 2 139 ? -3.512  23.490  4.989   1.00 14.72  ? 139  ASN F O   1 
ATOM   2293 C  CB  . ASN B 2 139 ? -1.927  25.603  5.821   1.00 15.14  ? 139  ASN F CB  1 
ATOM   2294 C  CG  . ASN B 2 139 ? -1.547  26.780  6.745   1.00 16.35  ? 139  ASN F CG  1 
ATOM   2295 O  OD1 . ASN B 2 139 ? -2.210  27.047  7.761   1.00 20.57  ? 139  ASN F OD1 1 
ATOM   2296 N  ND2 . ASN B 2 139 ? -0.444  27.424  6.436   1.00 17.33  ? 139  ASN F ND2 1 
ATOM   2297 N  N   . ALA B 2 140 ? -2.295  21.905  5.977   1.00 12.37  ? 140  ALA F N   1 
ATOM   2298 C  CA  . ALA B 2 140 ? -2.897  20.807  5.227   1.00 12.24  ? 140  ALA F CA  1 
ATOM   2299 C  C   . ALA B 2 140 ? -4.239  20.368  5.784   1.00 11.95  ? 140  ALA F C   1 
ATOM   2300 O  O   . ALA B 2 140 ? -4.870  19.505  5.216   1.00 12.30  ? 140  ALA F O   1 
ATOM   2301 C  CB  . ALA B 2 140 ? -1.925  19.618  5.156   1.00 12.32  ? 140  ALA F CB  1 
ATOM   2302 N  N   . GLY B 2 141 ? -4.675  20.908  6.915   1.00 12.62  ? 141  GLY F N   1 
ATOM   2303 C  CA  . GLY B 2 141 ? -6.033  20.651  7.356   1.00 12.73  ? 141  GLY F CA  1 
ATOM   2304 C  C   . GLY B 2 141 ? -6.219  19.303  8.011   1.00 12.46  ? 141  GLY F C   1 
ATOM   2305 O  O   . GLY B 2 141 ? -5.281  18.709  8.553   1.00 13.00  ? 141  GLY F O   1 
ATOM   2306 N  N   A SER B 2 142 ? -7.466  18.851  8.036   0.80 12.24  ? 142  SER F N   1 
ATOM   2307 N  N   B SER B 2 142 ? -7.464  18.832  7.939   0.20 12.02  ? 142  SER F N   1 
ATOM   2308 C  CA  A SER B 2 142 ? -7.829  17.677  8.802   0.80 12.05  ? 142  SER F CA  1 
ATOM   2309 C  CA  B SER B 2 142 ? -7.935  17.667  8.673   0.20 11.55  ? 142  SER F CA  1 
ATOM   2310 C  C   A SER B 2 142 ? -7.262  16.390  8.197   0.80 10.73  ? 142  SER F C   1 
ATOM   2311 C  C   B SER B 2 142 ? -7.372  16.365  8.122   0.20 10.94  ? 142  SER F C   1 
ATOM   2312 O  O   A SER B 2 142 ? -6.607  16.387  7.145   0.80 11.22  ? 142  SER F O   1 
ATOM   2313 O  O   B SER B 2 142 ? -6.888  16.312  6.988   0.20 11.32  ? 142  SER F O   1 
ATOM   2314 C  CB  A SER B 2 142 ? -9.351  17.579  8.897   0.80 12.69  ? 142  SER F CB  1 
ATOM   2315 C  CB  B SER B 2 142 ? -9.463  17.620  8.610   0.20 11.46  ? 142  SER F CB  1 
ATOM   2316 O  OG  A SER B 2 142 ? -9.926  17.208  7.671   0.80 16.07  ? 142  SER F OG  1 
ATOM   2317 O  OG  B SER B 2 142 ? -10.017 18.912  8.796   0.20 11.92  ? 142  SER F OG  1 
ATOM   2318 N  N   . ARG B 2 143 ? -7.468  15.311  8.929   1.00 10.46  ? 143  ARG F N   1 
ATOM   2319 C  CA  . ARG B 2 143 ? -6.855  14.017  8.600   1.00 10.64  ? 143  ARG F CA  1 
ATOM   2320 C  C   . ARG B 2 143 ? -7.884  13.098  7.990   1.00 10.84  ? 143  ARG F C   1 
ATOM   2321 O  O   . ARG B 2 143 ? -8.789  12.611  8.662   1.00 13.61  ? 143  ARG F O   1 
ATOM   2322 C  CB  . ARG B 2 143 ? -6.258  13.419  9.876   1.00 11.12  ? 143  ARG F CB  1 
ATOM   2323 C  CG  . ARG B 2 143 ? -5.326  14.397  10.541  1.00 10.75  ? 143  ARG F CG  1 
ATOM   2324 C  CD  . ARG B 2 143 ? -4.685  13.921  11.828  1.00 10.83  ? 143  ARG F CD  1 
ATOM   2325 N  NE  . ARG B 2 143 ? -3.851  14.993  12.341  1.00 12.25  ? 143  ARG F NE  1 
ATOM   2326 C  CZ  . ARG B 2 143 ? -2.984  14.883  13.321  1.00 9.79   ? 143  ARG F CZ  1 
ATOM   2327 N  NH1 . ARG B 2 143 ? -2.787  13.735  13.926  1.00 10.60  ? 143  ARG F NH1 1 
ATOM   2328 N  NH2 . ARG B 2 143 ? -2.270  15.928  13.671  1.00 11.78  ? 143  ARG F NH2 1 
ATOM   2329 N  N   . LEU B 2 144 ? -7.752  12.846  6.702   1.00 10.18  ? 144  LEU F N   1 
ATOM   2330 C  CA  . LEU B 2 144 ? -8.783  12.082  5.999   1.00 10.67  ? 144  LEU F CA  1 
ATOM   2331 C  C   . LEU B 2 144 ? -8.638  10.590  6.210   1.00 10.51  ? 144  LEU F C   1 
ATOM   2332 O  O   . LEU B 2 144 ? -9.643  9.862   6.253   1.00 12.40  ? 144  LEU F O   1 
ATOM   2333 C  CB  . LEU B 2 144 ? -8.700  12.362  4.502   1.00 11.53  ? 144  LEU F CB  1 
ATOM   2334 C  CG  . LEU B 2 144 ? -8.949  13.782  4.044   1.00 13.92  ? 144  LEU F CG  1 
ATOM   2335 C  CD1 . LEU B 2 144 ? -8.787  13.824  2.525   1.00 16.48  ? 144  LEU F CD1 1 
ATOM   2336 C  CD2 . LEU B 2 144 ? -10.289 14.308  4.494   1.00 17.57  ? 144  LEU F CD2 1 
ATOM   2337 N  N   . ALA B 2 145 ? -7.402  10.098  6.306   1.00 10.17  ? 145  ALA F N   1 
ATOM   2338 C  CA  . ALA B 2 145 ? -7.139  8.672   6.457   1.00 9.87   ? 145  ALA F CA  1 
ATOM   2339 C  C   . ALA B 2 145 ? -5.762  8.494   7.034   1.00 9.33   ? 145  ALA F C   1 
ATOM   2340 O  O   . ALA B 2 145 ? -4.902  9.337   6.846   1.00 9.37   ? 145  ALA F O   1 
ATOM   2341 C  CB  . ALA B 2 145 ? -7.247  7.935   5.087   1.00 11.28  ? 145  ALA F CB  1 
ATOM   2342 N  N   . CYS B 2 146 ? -5.577  7.389   7.720   1.00 9.24   ? 146  CYS F N   1 
ATOM   2343 C  CA  . CYS B 2 146 ? -4.305  7.109   8.370   1.00 8.94   ? 146  CYS F CA  1 
ATOM   2344 C  C   . CYS B 2 146 ? -4.175  5.622   8.619   1.00 8.57   ? 146  CYS F C   1 
ATOM   2345 O  O   . CYS B 2 146 ? -5.134  4.864   8.489   1.00 9.34   ? 146  CYS F O   1 
ATOM   2346 C  CB  . CYS B 2 146 ? -4.165  7.890   9.680   1.00 8.93   ? 146  CYS F CB  1 
ATOM   2347 S  SG  . CYS B 2 146 ? -5.355  7.465   10.938  1.00 14.15  ? 146  CYS F SG  1 
ATOM   2348 N  N   . GLY B 2 147 ? -2.955  5.225   8.935   1.00 8.07   ? 147  GLY F N   1 
ATOM   2349 C  CA  . GLY B 2 147 ? -2.688  3.871   9.375   1.00 8.38   ? 147  GLY F CA  1 
ATOM   2350 C  C   . GLY B 2 147 ? -1.343  3.815   10.024  1.00 7.20   ? 147  GLY F C   1 
ATOM   2351 O  O   . GLY B 2 147 ? -0.509  4.697   9.839   1.00 8.93   ? 147  GLY F O   1 
ATOM   2352 N  N   . VAL B 2 148 ? -1.131  2.776   10.822  1.00 8.01   ? 148  VAL F N   1 
ATOM   2353 C  CA  . VAL B 2 148 ? 0.151   2.590   11.468  1.00 8.08   ? 148  VAL F CA  1 
ATOM   2354 C  C   . VAL B 2 148 ? 1.102   1.902   10.480  1.00 8.23   ? 148  VAL F C   1 
ATOM   2355 O  O   . VAL B 2 148 ? 0.731   0.938   9.808   1.00 9.89   ? 148  VAL F O   1 
ATOM   2356 C  CB  . VAL B 2 148 ? 0.015   1.764   12.768  1.00 8.67   ? 148  VAL F CB  1 
ATOM   2357 C  CG1 . VAL B 2 148 ? 1.332   1.611   13.491  1.00 11.52  ? 148  VAL F CG1 1 
ATOM   2358 C  CG2 . VAL B 2 148 ? -1.008  2.408   13.707  1.00 11.93  ? 148  VAL F CG2 1 
ATOM   2359 N  N   . ILE B 2 149 ? 2.335   2.370   10.375  1.00 7.90   ? 149  ILE F N   1 
ATOM   2360 C  CA  . ILE B 2 149 ? 3.325   1.779   9.504   1.00 8.32   ? 149  ILE F CA  1 
ATOM   2361 C  C   . ILE B 2 149 ? 3.894   0.520   10.170  1.00 8.05   ? 149  ILE F C   1 
ATOM   2362 O  O   . ILE B 2 149 ? 4.395   0.575   11.280  1.00 9.75   ? 149  ILE F O   1 
ATOM   2363 C  CB  . ILE B 2 149 ? 4.465   2.810   9.184   1.00 8.14   ? 149  ILE F CB  1 
ATOM   2364 C  CG1 . ILE B 2 149 ? 3.858   4.065   8.540   1.00 9.41   ? 149  ILE F CG1 1 
ATOM   2365 C  CG2 . ILE B 2 149 ? 5.544   2.172   8.283   1.00 10.62  ? 149  ILE F CG2 1 
ATOM   2366 C  CD1 . ILE B 2 149 ? 4.809   5.240   8.575   1.00 11.28  ? 149  ILE F CD1 1 
ATOM   2367 N  N   . GLY B 2 150 ? 3.819   -0.612  9.485   1.00 7.96   ? 150  GLY F N   1 
ATOM   2368 C  CA  . GLY B 2 150 ? 4.227   -1.877  10.041  1.00 8.39   ? 150  GLY F CA  1 
ATOM   2369 C  C   . GLY B 2 150 ? 5.318   -2.543  9.268   1.00 7.87   ? 150  GLY F C   1 
ATOM   2370 O  O   . GLY B 2 150 ? 5.524   -2.289  8.097   1.00 9.71   ? 150  GLY F O   1 
ATOM   2371 N  N   . ILE B 2 151 ? 5.975   -3.472  9.925   1.00 8.54   ? 151  ILE F N   1 
ATOM   2372 C  CA  . ILE B 2 151 ? 7.026   -4.267  9.330   1.00 9.20   ? 151  ILE F CA  1 
ATOM   2373 C  C   . ILE B 2 151 ? 6.458   -5.225  8.322   1.00 8.85   ? 151  ILE F C   1 
ATOM   2374 O  O   . ILE B 2 151 ? 5.477   -5.912  8.605   1.00 10.02  ? 151  ILE F O   1 
ATOM   2375 C  CB  . ILE B 2 151 ? 7.772   -5.063  10.422  1.00 9.93   ? 151  ILE F CB  1 
ATOM   2376 C  CG1 . ILE B 2 151 ? 8.492   -4.101  11.390  1.00 10.95  ? 151  ILE F CG1 1 
ATOM   2377 C  CG2 . ILE B 2 151 ? 8.817   -6.059  9.818   1.00 11.99  ? 151  ILE F CG2 1 
ATOM   2378 C  CD1 . ILE B 2 151 ? 9.043   -4.730  12.613  1.00 11.00  ? 151  ILE F CD1 1 
ATOM   2379 N  N   . ALA B 2 152 ? 7.043   -5.269  7.129   1.00 9.77   ? 152  ALA F N   1 
ATOM   2380 C  CA  . ALA B 2 152 ? 6.522   -6.117  6.057   1.00 10.33  ? 152  ALA F CA  1 
ATOM   2381 C  C   . ALA B 2 152 ? 7.490   -7.263  5.737   1.00 11.63  ? 152  ALA F C   1 
ATOM   2382 O  O   . ALA B 2 152 ? 8.679   -7.199  6.034   1.00 12.12  ? 152  ALA F O   1 
ATOM   2383 C  CB  . ALA B 2 152 ? 6.235   -5.303  4.806   1.00 11.63  ? 152  ALA F CB  1 
ATOM   2384 N  N   . GLN B 2 153 ? 6.930   -8.314  5.136   1.00 12.71  ? 153  GLN F N   1 
ATOM   2385 C  CA  . GLN B 2 153 ? 7.633   -9.504  4.710   1.00 15.05  ? 153  GLN F CA  1 
ATOM   2386 C  C   . GLN B 2 153 ? 8.596   -9.204  3.592   1.00 16.21  ? 153  GLN F C   1 
ATOM   2387 O  O   . GLN B 2 153 ? 8.262   -8.474  2.685   1.00 18.91  ? 153  GLN F O   1 
ATOM   2388 C  CB  . GLN B 2 153 ? 6.599   -10.529 4.216   1.00 14.80  ? 153  GLN F CB  1 
ATOM   2389 C  CG  . GLN B 2 153 ? 7.146   -11.897 3.820   1.00 15.89  ? 153  GLN F CG  1 
ATOM   2390 C  CD  . GLN B 2 153 ? 6.033   -12.873 3.519   1.00 16.00  ? 153  GLN F CD  1 
ATOM   2391 O  OE1 . GLN B 2 153 ? 4.940   -12.856 4.161   1.00 14.14  ? 153  GLN F OE1 1 
ATOM   2392 N  NE2 . GLN B 2 153 ? 6.282   -13.732 2.526   1.00 17.06  ? 153  GLN F NE2 1 
ATOM   2393 O  OXT . GLN B 2 153 ? 9.711   -9.753  3.571   0.50 16.24  ? 153  GLN F OXT 1 
HETATM 2394 S  S   . SO4 C 3 .   ? -5.040  -23.328 13.440  0.70 17.87  ? 1154 SO4 A S   1 
HETATM 2395 O  O1  . SO4 C 3 .   ? -4.146  -22.348 13.993  0.70 22.49  ? 1154 SO4 A O1  1 
HETATM 2396 O  O2  . SO4 C 3 .   ? -5.595  -22.815 12.198  0.70 25.45  ? 1154 SO4 A O2  1 
HETATM 2397 O  O3  . SO4 C 3 .   ? -4.213  -24.527 13.292  0.70 23.50  ? 1154 SO4 A O3  1 
HETATM 2398 O  O4  . SO4 C 3 .   ? -6.066  -23.573 14.477  0.70 21.15  ? 1154 SO4 A O4  1 
HETATM 2399 N  N1  . 12I D 4 .   ? 15.403  -7.654  22.684  1.00 16.73  ? 1000 12I A N1  1 
HETATM 2400 C  C2  . 12I D 4 .   ? 14.576  -6.897  23.377  1.00 16.75  ? 1000 12I A C2  1 
HETATM 2401 C  C3  . 12I D 4 .   ? 15.929  -8.782  23.240  1.00 15.96  ? 1000 12I A C3  1 
HETATM 2402 N  N3  . 12I D 4 .   ? 14.071  -8.453  26.606  1.00 16.96  ? 1000 12I A N3  1 
HETATM 2403 C  C4  . 12I D 4 .   ? 15.570  -9.145  24.623  1.00 15.18  ? 1000 12I A C4  1 
HETATM 2404 N  N4  . 12I D 4 .   ? 13.204  -8.985  29.240  1.00 16.77  ? 1000 12I A N4  1 
HETATM 2405 C  C5  . 12I D 4 .   ? 16.124  -10.290 25.167  1.00 15.63  ? 1000 12I A C5  1 
HETATM 2406 C  C6  . 12I D 4 .   ? 16.996  -11.072 24.425  1.00 14.91  ? 1000 12I A C6  1 
HETATM 2407 C  C7  . 12I D 4 .   ? 17.362  -10.732 23.130  1.00 15.75  ? 1000 12I A C7  1 
HETATM 2408 C  C8  . 12I D 4 .   ? 14.649  -8.254  25.345  1.00 16.09  ? 1000 12I A C8  1 
HETATM 2409 C  C9  . 12I D 4 .   ? 13.653  -7.321  27.422  1.00 16.07  ? 1000 12I A C9  1 
HETATM 2410 C  C10 . 12I D 4 .   ? 13.570  -7.634  28.909  1.00 15.37  ? 1000 12I A C10 1 
HETATM 2411 C  C11 . 12I D 4 .   ? 13.636  -10.095 28.362  1.00 16.54  ? 1000 12I A C11 1 
HETATM 2412 C  C17 . 12I D 4 .   ? 16.833  -9.585  22.553  1.00 16.95  ? 1000 12I A C17 1 
HETATM 2413 C  C12 . 12I D 4 .   ? 13.485  -9.761  26.882  1.00 16.81  ? 1000 12I A C12 1 
HETATM 2414 N  N9  . 12I D 4 .   ? 14.213  -7.188  24.657  1.00 16.20  ? 1000 12I A N9  1 
HETATM 2415 C  C13 . 12I D 4 .   ? 12.833  -9.174  30.646  1.00 16.26  ? 1000 12I A C13 1 
HETATM 2416 S  S   . SO4 E 3 .   ? -7.336  -16.080 9.085   0.60 24.23  ? 1156 SO4 A S   1 
HETATM 2417 O  O1  . SO4 E 3 .   ? -6.331  -15.032 8.979   0.60 25.13  ? 1156 SO4 A O1  1 
HETATM 2418 O  O2  . SO4 E 3 .   ? -7.769  -16.496 7.749   0.60 25.77  ? 1156 SO4 A O2  1 
HETATM 2419 O  O3  . SO4 E 3 .   ? -6.724  -17.222 9.792   0.60 24.12  ? 1156 SO4 A O3  1 
HETATM 2420 O  O4  . SO4 E 3 .   ? -8.462  -15.619 9.879   0.60 19.80  ? 1156 SO4 A O4  1 
HETATM 2421 N  N1  . 12I F 4 .   ? -4.706  0.977   33.656  1.00 33.62  ? 1001 12I A N1  1 
HETATM 2422 C  C2  . 12I F 4 .   ? -3.975  2.109   33.553  1.00 35.11  ? 1001 12I A C2  1 
HETATM 2423 C  C3  . 12I F 4 .   ? -4.127  -0.218  33.919  1.00 32.07  ? 1001 12I A C3  1 
HETATM 2424 N  N3  . 12I F 4 .   ? -0.514  1.178   34.123  1.00 39.54  ? 1001 12I A N3  1 
HETATM 2425 C  C4  . 12I F 4 .   ? -2.654  -0.286  34.104  1.00 33.40  ? 1001 12I A C4  1 
HETATM 2426 N  N4  . 12I F 4 .   ? 2.173   1.749   34.423  0.50 41.36  ? 1001 12I A N4  1 
HETATM 2427 C  C5  . 12I F 4 .   ? -2.089  -1.529  34.379  1.00 32.94  ? 1001 12I A C5  1 
HETATM 2428 C  C6  . 12I F 4 .   ? -2.905  -2.665  34.458  1.00 33.48  ? 1001 12I A C6  1 
HETATM 2429 C  C7  . 12I F 4 .   ? -4.291  -2.602  34.289  1.00 32.39  ? 1001 12I A C7  1 
HETATM 2430 C  C8  . 12I F 4 .   ? -1.906  1.004   33.974  1.00 36.46  ? 1001 12I A C8  1 
HETATM 2431 C  C9  . 12I F 4 .   ? 0.468   0.147   33.815  0.50 40.19  ? 1001 12I A C9  1 
HETATM 2432 C  C10 . 12I F 4 .   ? 1.738   0.856   33.350  0.50 40.98  ? 1001 12I A C10 1 
HETATM 2433 C  C11 . 12I F 4 .   ? 1.223   2.229   35.407  1.00 41.17  ? 1001 12I A C11 1 
HETATM 2434 C  C17 . 12I F 4 .   ? -4.901  -1.375  34.017  1.00 32.48  ? 1001 12I A C17 1 
HETATM 2435 C  C12 . 12I F 4 .   ? -0.058  2.477   34.622  1.00 40.83  ? 1001 12I A C12 1 
HETATM 2436 N  N9  . 12I F 4 .   ? -2.640  2.123   33.707  1.00 36.93  ? 1001 12I A N9  1 
HETATM 2437 C  C13 . 12I F 4 .   ? 3.560   2.175   34.517  0.50 42.31  ? 1001 12I A C13 1 
HETATM 2438 CU CU  . CU  G 5 .   ? -2.077  -15.318 16.874  0.50 10.95  ? 1157 CU  A CU  1 
HETATM 2439 ZN ZN  . ZN  H 6 .   ? 3.216   -19.095 19.100  1.00 9.13   ? 1158 ZN  A ZN  1 
HETATM 2440 C  C   . ACT I 7 .   ? 11.788  -9.193  34.015  1.00 70.86  ? 1159 ACT A C   1 
HETATM 2441 O  O   . ACT I 7 .   ? 11.213  -9.821  34.929  1.00 70.66  ? 1159 ACT A O   1 
HETATM 2442 O  OXT . ACT I 7 .   ? 12.985  -8.878  34.188  1.00 70.76  ? 1159 ACT A OXT 1 
HETATM 2443 C  CH3 . ACT I 7 .   ? 11.067  -8.822  32.765  1.00 70.88  ? 1159 ACT A CH3 1 
HETATM 2444 S  S   . SO4 J 3 .   ? -4.088  23.015  9.996   0.70 19.20  ? 1154 SO4 F S   1 
HETATM 2445 O  O1  . SO4 J 3 .   ? -2.969  22.122  9.834   0.70 23.14  ? 1154 SO4 F O1  1 
HETATM 2446 O  O2  . SO4 J 3 .   ? -4.607  23.291  8.654   0.70 22.20  ? 1154 SO4 F O2  1 
HETATM 2447 O  O3  . SO4 J 3 .   ? -5.114  22.294  10.752  0.70 24.74  ? 1154 SO4 F O3  1 
HETATM 2448 O  O4  . SO4 J 3 .   ? -3.644  24.214  10.673  0.70 23.67  ? 1154 SO4 F O4  1 
HETATM 2449 S  S   . SO4 K 3 .   ? -8.183  15.854  12.735  0.60 29.30  ? 1155 SO4 F S   1 
HETATM 2450 O  O1  . SO4 K 3 .   ? -7.467  17.095  12.418  0.60 29.08  ? 1155 SO4 F O1  1 
HETATM 2451 O  O2  . SO4 K 3 .   ? -8.709  15.287  11.497  0.60 22.46  ? 1155 SO4 F O2  1 
HETATM 2452 O  O3  . SO4 K 3 .   ? -7.273  14.931  13.411  0.60 29.33  ? 1155 SO4 F O3  1 
HETATM 2453 O  O4  . SO4 K 3 .   ? -9.290  16.196  13.639  0.60 31.18  ? 1155 SO4 F O4  1 
HETATM 2454 CU CU  A CU  L 5 .   ? 0.210   14.982  8.400   0.40 8.65   ? 1156 CU  F CU  1 
HETATM 2455 CU CU  B CU  L 5 .   ? -0.171  15.395  8.885   0.10 14.82  ? 1156 CU  F CU  1 
HETATM 2456 S  S   . SO4 M 3 .   ? -9.777  11.770  12.978  0.50 25.22  ? 1158 SO4 F S   1 
HETATM 2457 O  O1  . SO4 M 3 .   ? -8.828  12.596  12.244  0.50 23.24  ? 1158 SO4 F O1  1 
HETATM 2458 O  O2  . SO4 M 3 .   ? -11.135 12.263  12.850  0.50 27.42  ? 1158 SO4 F O2  1 
HETATM 2459 O  O3  . SO4 M 3 .   ? -9.699  10.421  12.397  0.50 23.31  ? 1158 SO4 F O3  1 
HETATM 2460 O  O4  . SO4 M 3 .   ? -9.381  11.769  14.397  0.50 22.53  ? 1158 SO4 F O4  1 
HETATM 2461 ZN ZN  . ZN  N 6 .   ? 5.896   18.760  9.054   1.00 9.51   ? 1157 ZN  F ZN  1 
HETATM 2462 N  N1  . 12I O 4 .   ? 5.704   -1.188  -7.775  1.00 39.29  ? 1000 12I F N1  1 
HETATM 2463 C  C2  . 12I O 4 .   ? 6.225   -2.351  -7.352  1.00 40.26  ? 1000 12I F C2  1 
HETATM 2464 C  C3  . 12I O 4 .   ? 6.389   -0.027  -7.658  1.00 37.82  ? 1000 12I F C3  1 
HETATM 2465 N  N3  . 12I O 4 .   ? 9.539   -1.649  -5.994  1.00 42.65  ? 1000 12I F N3  1 
HETATM 2466 C  C4  . 12I O 4 .   ? 7.752   -0.022  -7.056  1.00 38.12  ? 1000 12I F C4  1 
HETATM 2467 N  N4  . 12I O 4 .   ? 12.164  -2.371  -5.698  0.50 43.51  ? 1000 12I F N4  1 
HETATM 2468 C  C5  . 12I O 4 .   ? 8.396   1.214   -6.976  1.00 37.77  ? 1000 12I F C5  1 
HETATM 2469 C  C6  . 12I O 4 .   ? 7.770   2.378   -7.439  1.00 37.74  ? 1000 12I F C6  1 
HETATM 2470 C  C7  . 12I O 4 .   ? 6.497   2.361   -7.995  1.00 37.48  ? 1000 12I F C7  1 
HETATM 2471 C  C8  . 12I O 4 .   ? 8.286   -1.362  -6.610  1.00 40.45  ? 1000 12I F C8  1 
HETATM 2472 C  C9  . 12I O 4 .   ? 9.858   -3.045  -5.651  1.00 43.20  ? 1000 12I F C9  1 
HETATM 2473 C  C10 . 12I O 4 .   ? 11.232  -3.349  -6.240  0.50 43.40  ? 1000 12I F C10 1 
HETATM 2474 C  C11 . 12I O 4 .   ? 11.684  -1.260  -4.891  0.50 43.40  ? 1000 12I F C11 1 
HETATM 2475 C  C17 . 12I O 4 .   ? 5.808   1.156   -8.103  1.00 37.12  ? 1000 12I F C17 1 
HETATM 2476 C  C12 . 12I O 4 .   ? 10.522  -0.622  -5.653  0.50 43.14  ? 1000 12I F C12 1 
HETATM 2477 N  N9  . 12I O 4 .   ? 7.452   -2.425  -6.799  1.00 40.50  ? 1000 12I F N9  1 
HETATM 2478 C  C13 . 12I O 4 .   ? 13.589  -2.502  -5.973  0.50 43.60  ? 1000 12I F C13 1 
HETATM 2479 O  O   . HOH P 8 .   ? -8.240  -15.550 3.271   1.00 27.13  ? 2001 HOH A O   1 
HETATM 2480 O  O   . HOH P 8 .   ? -8.138  -0.252  33.142  1.00 36.16  ? 2002 HOH A O   1 
HETATM 2481 O  O   . HOH P 8 .   ? 10.605  4.632   33.237  1.00 33.85  ? 2003 HOH A O   1 
HETATM 2482 O  O   . HOH P 8 .   ? 11.816  1.142   28.545  1.00 25.02  ? 2004 HOH A O   1 
HETATM 2483 O  O   . HOH P 8 .   ? 8.935   5.190   22.181  1.00 37.75  ? 2005 HOH A O   1 
HETATM 2484 O  O   . HOH P 8 .   ? 6.607   5.850   24.335  1.00 15.80  ? 2006 HOH A O   1 
HETATM 2485 O  O   . HOH P 8 .   ? 7.292   2.889   21.891  1.00 17.52  ? 2007 HOH A O   1 
HETATM 2486 O  O   . HOH P 8 .   ? -4.831  0.828   13.893  1.00 23.50  ? 2008 HOH A O   1 
HETATM 2487 O  O   . HOH P 8 .   ? -1.107  3.156   25.478  1.00 26.83  ? 2009 HOH A O   1 
HETATM 2488 O  O   . HOH P 8 .   ? 0.718   2.678   27.048  1.00 21.86  ? 2010 HOH A O   1 
HETATM 2489 O  O   . HOH P 8 .   ? -14.375 -12.524 11.289  1.00 39.89  ? 2011 HOH A O   1 
HETATM 2490 O  O   . HOH P 8 .   ? -15.368 -11.923 13.855  1.00 29.60  ? 2012 HOH A O   1 
HETATM 2491 O  O   . HOH P 8 .   ? -3.261  -0.020  16.149  1.00 8.80   ? 2013 HOH A O   1 
HETATM 2492 O  O   . HOH P 8 .   ? -6.475  -1.439  13.708  1.00 20.93  ? 2014 HOH A O   1 
HETATM 2493 O  O   . HOH P 8 .   ? -11.403 -1.032  18.323  1.00 33.95  ? 2015 HOH A O   1 
HETATM 2494 O  O   . HOH P 8 .   ? 7.388   -2.993  35.428  1.00 48.29  ? 2016 HOH A O   1 
HETATM 2495 O  O   . HOH P 8 .   ? -8.912  -3.855  10.519  1.00 93.53  ? 2017 HOH A O   1 
HETATM 2496 O  O   . HOH P 8 .   ? -7.914  -6.454  10.077  1.00 41.40  ? 2018 HOH A O   1 
HETATM 2497 O  O   . HOH P 8 .   ? -11.298 1.464   15.276  1.00 52.76  ? 2019 HOH A O   1 
HETATM 2498 O  O   . HOH P 8 .   ? -14.177 -5.472  14.347  1.00 18.64  ? 2020 HOH A O   1 
HETATM 2499 O  O   . HOH P 8 .   ? -16.503 -4.984  11.510  1.00 37.42  ? 2021 HOH A O   1 
HETATM 2500 O  O   . HOH P 8 .   ? 16.522  2.196   31.850  1.00 69.97  ? 2022 HOH A O   1 
HETATM 2501 O  O   . HOH P 8 .   ? 18.656  -4.644  28.246  1.00 47.09  ? 2023 HOH A O   1 
HETATM 2502 O  O   . HOH P 8 .   ? -12.674 -10.592 11.420  1.00 22.30  ? 2024 HOH A O   1 
HETATM 2503 O  O   . HOH P 8 .   ? -14.453 -9.505  14.357  1.00 18.92  ? 2025 HOH A O   1 
HETATM 2504 O  O   . HOH P 8 .   ? -20.052 -7.040  13.275  1.00 54.60  ? 2026 HOH A O   1 
HETATM 2505 O  O   . HOH P 8 .   ? -18.989 -5.460  19.206  1.00 27.98  ? 2027 HOH A O   1 
HETATM 2506 O  O   . HOH P 8 .   ? -8.269  -1.503  31.035  1.00 35.43  ? 2028 HOH A O   1 
HETATM 2507 O  O   . HOH P 8 .   ? -12.799 -0.799  21.020  1.00 35.40  ? 2029 HOH A O   1 
HETATM 2508 O  O   . HOH P 8 .   ? -15.521 -3.071  14.557  1.00 42.57  ? 2030 HOH A O   1 
HETATM 2509 O  O   . HOH P 8 .   ? -19.043 -5.179  25.010  1.00 131.90 ? 2031 HOH A O   1 
HETATM 2510 O  O   . HOH P 8 .   ? -19.957 -13.967 17.708  1.00 26.76  ? 2032 HOH A O   1 
HETATM 2511 O  O   . HOH P 8 .   ? -16.829 -13.263 15.574  1.00 24.21  ? 2033 HOH A O   1 
HETATM 2512 O  O   . HOH P 8 .   ? -21.888 -14.750 24.057  1.00 26.20  ? 2034 HOH A O   1 
HETATM 2513 O  O   . HOH P 8 .   ? -16.240 -16.324 15.865  1.00 31.99  ? 2035 HOH A O   1 
HETATM 2514 O  O   . HOH P 8 .   ? -16.893 -19.344 18.031  1.00 61.41  ? 2036 HOH A O   1 
HETATM 2515 O  O   . HOH P 8 .   ? -20.454 -19.168 21.685  1.00 33.66  ? 2037 HOH A O   1 
HETATM 2516 O  O   . HOH P 8 .   ? -19.273 -13.219 14.034  1.00 60.99  ? 2038 HOH A O   1 
HETATM 2517 O  O   . HOH P 8 .   ? -8.663  -0.610  26.758  1.00 29.50  ? 2039 HOH A O   1 
HETATM 2518 O  O   . HOH P 8 .   ? -5.242  3.901   24.376  1.00 17.84  ? 2040 HOH A O   1 
HETATM 2519 O  O   . HOH P 8 .   ? -3.159  4.312   28.256  1.00 41.27  ? 2041 HOH A O   1 
HETATM 2520 O  O   . HOH P 8 .   ? 6.776   -2.085  32.968  1.00 21.73  ? 2042 HOH A O   1 
HETATM 2521 O  O   . HOH P 8 .   ? 1.002   4.128   29.304  1.00 46.48  ? 2043 HOH A O   1 
HETATM 2522 O  O   . HOH P 8 .   ? 6.555   2.394   33.573  1.00 52.81  ? 2044 HOH A O   1 
HETATM 2523 O  O   . HOH P 8 .   ? -3.770  -1.153  9.633   1.00 23.20  ? 2045 HOH A O   1 
HETATM 2524 O  O   . HOH P 8 .   ? 12.055  -0.527  25.933  1.00 25.54  ? 2046 HOH A O   1 
HETATM 2525 O  O   . HOH P 8 .   ? 10.033  -2.647  32.658  1.00 18.10  ? 2047 HOH A O   1 
HETATM 2526 O  O   . HOH P 8 .   ? 13.127  -2.372  38.359  1.00 42.01  ? 2048 HOH A O   1 
HETATM 2527 O  O   . HOH P 8 .   ? 10.638  -2.699  35.439  1.00 21.49  ? 2049 HOH A O   1 
HETATM 2528 O  O   . HOH P 8 .   ? 16.481  -16.430 12.006  1.00 53.73  ? 2050 HOH A O   1 
HETATM 2529 O  O   . HOH P 8 .   ? 18.523  -16.934 16.954  1.00 39.58  ? 2051 HOH A O   1 
HETATM 2530 O  O   . HOH P 8 .   ? 15.547  1.779   29.671  1.00 47.01  ? 2052 HOH A O   1 
HETATM 2531 O  O   . HOH P 8 .   ? 17.340  -1.419  31.102  1.00 39.76  ? 2053 HOH A O   1 
HETATM 2532 O  O   . HOH P 8 .   ? 14.451  -4.078  25.173  1.00 21.82  ? 2054 HOH A O   1 
HETATM 2533 O  O   . HOH P 8 .   ? 10.510  -25.561 15.553  1.00 43.52  ? 2055 HOH A O   1 
HETATM 2534 O  O   . HOH P 8 .   ? 16.089  -8.713  32.439  1.00 19.41  ? 2056 HOH A O   1 
HETATM 2535 O  O   . HOH P 8 .   ? 19.709  -2.111  30.280  1.00 77.33  ? 2057 HOH A O   1 
HETATM 2536 O  O   . HOH P 8 .   ? 20.210  -5.858  31.028  1.00 25.15  ? 2058 HOH A O   1 
HETATM 2537 O  O   . HOH P 8 .   ? -0.797  -19.060 30.911  1.00 32.82  ? 2059 HOH A O   1 
HETATM 2538 O  O   . HOH P 8 .   ? 10.479  -8.007  28.817  1.00 15.26  ? 2060 HOH A O   1 
HETATM 2539 O  O   . HOH P 8 .   ? 12.424  -16.734 24.407  1.00 22.13  ? 2061 HOH A O   1 
HETATM 2540 O  O   . HOH P 8 .   ? 5.085   -0.132  33.568  1.00 44.05  ? 2062 HOH A O   1 
HETATM 2541 O  O   . HOH P 8 .   ? 6.047   -0.791  36.865  1.00 55.21  ? 2063 HOH A O   1 
HETATM 2542 O  O   . HOH P 8 .   ? -0.873  -5.063  33.381  1.00 27.58  ? 2064 HOH A O   1 
HETATM 2543 O  O   . HOH P 8 .   ? 0.363   -13.922 30.854  1.00 20.69  ? 2065 HOH A O   1 
HETATM 2544 O  O   . HOH P 8 .   ? -5.190  3.014   30.397  1.00 44.02  ? 2066 HOH A O   1 
HETATM 2545 O  O   . HOH P 8 .   ? -7.763  -13.892 31.742  1.00 36.79  ? 2067 HOH A O   1 
HETATM 2546 O  O   . HOH P 8 .   ? -10.090 -4.340  31.751  1.00 93.20  ? 2068 HOH A O   1 
HETATM 2547 O  O   . HOH P 8 .   ? -7.581  -4.217  32.278  1.00 31.67  ? 2069 HOH A O   1 
HETATM 2548 O  O   . HOH P 8 .   ? -17.415 -3.685  26.471  1.00 154.20 ? 2070 HOH A O   1 
HETATM 2549 O  O   . HOH P 8 .   ? 3.548   -14.964 32.743  1.00 39.76  ? 2071 HOH A O   1 
HETATM 2550 O  O   . HOH P 8 .   ? -19.140 -7.373  24.251  1.00 17.85  ? 2072 HOH A O   1 
HETATM 2551 O  O   . HOH P 8 .   ? -17.425 -12.905 18.065  1.00 16.95  ? 2073 HOH A O   1 
HETATM 2552 O  O   . HOH P 8 .   ? -20.313 -12.686 20.105  1.00 42.36  ? 2074 HOH A O   1 
HETATM 2553 O  O   . HOH P 8 .   ? -20.269 -10.387 19.590  1.00 46.43  ? 2075 HOH A O   1 
HETATM 2554 O  O   . HOH P 8 .   ? 14.253  -14.835 25.018  1.00 23.80  ? 2076 HOH A O   1 
HETATM 2555 O  O   . HOH P 8 .   ? -19.696 -13.831 25.222  1.00 19.03  ? 2077 HOH A O   1 
HETATM 2556 O  O   . HOH P 8 .   ? -15.506 -14.456 19.338  1.00 15.54  ? 2078 HOH A O   1 
HETATM 2557 O  O   . HOH P 8 .   ? -15.108 -17.185 18.360  1.00 17.26  ? 2079 HOH A O   1 
HETATM 2558 O  O   . HOH P 8 .   ? -15.926 -19.301 22.381  1.00 23.97  ? 2080 HOH A O   1 
HETATM 2559 O  O   . HOH P 8 .   ? 12.041  -4.236  14.942  1.00 37.13  ? 2081 HOH A O   1 
HETATM 2560 O  O   . HOH P 8 .   ? -20.705 -17.157 23.612  1.00 18.61  ? 2082 HOH A O   1 
HETATM 2561 O  O   . HOH P 8 .   ? -21.657 -18.900 25.748  1.00 39.17  ? 2083 HOH A O   1 
HETATM 2562 O  O   . HOH P 8 .   ? -20.343 -20.776 26.673  1.00 40.15  ? 2084 HOH A O   1 
HETATM 2563 O  O   . HOH P 8 .   ? -19.603 -15.465 31.872  1.00 23.12  ? 2085 HOH A O   1 
HETATM 2564 O  O   . HOH P 8 .   ? -18.554 -20.580 24.825  1.00 97.08  ? 2086 HOH A O   1 
HETATM 2565 O  O   . HOH P 8 .   ? 13.025  -11.009 13.671  1.00 28.46  ? 2087 HOH A O   1 
HETATM 2566 O  O   . HOH P 8 .   ? 11.445  3.734   17.053  1.00 39.27  ? 2088 HOH A O   1 
HETATM 2567 O  O   . HOH P 8 .   ? 10.994  4.527   19.463  1.00 42.51  ? 2089 HOH A O   1 
HETATM 2568 O  O   . HOH P 8 .   ? -14.776 -22.592 19.221  1.00 28.43  ? 2090 HOH A O   1 
HETATM 2569 O  O   . HOH P 8 .   ? -2.598  -19.032 16.647  1.00 13.84  ? 2091 HOH A O   1 
HETATM 2570 O  O   . HOH P 8 .   ? 9.100   -14.210 13.403  1.00 15.78  ? 2092 HOH A O   1 
HETATM 2571 O  O   . HOH P 8 .   ? 10.257  -9.824  10.806  1.00 27.19  ? 2093 HOH A O   1 
HETATM 2572 O  O   . HOH P 8 .   ? -0.336  -2.759  7.576   1.00 11.34  ? 2094 HOH A O   1 
HETATM 2573 O  O   . HOH P 8 .   ? -2.608  -7.027  10.187  1.00 93.43  ? 2095 HOH A O   1 
HETATM 2574 O  O   . HOH P 8 .   ? 1.222   -9.691  2.932   1.00 27.26  ? 2096 HOH A O   1 
HETATM 2575 O  O   . HOH P 8 .   ? 4.155   -8.325  4.843   1.00 20.38  ? 2097 HOH A O   1 
HETATM 2576 O  O   . HOH P 8 .   ? 3.183   -5.918  1.950   1.00 47.74  ? 2098 HOH A O   1 
HETATM 2577 O  O   . HOH P 8 .   ? -2.080  -20.001 10.282  1.00 37.96  ? 2099 HOH A O   1 
HETATM 2578 O  O   A HOH P 8 .   ? -7.189  -4.019  5.303   0.50 21.88  ? 2100 HOH A O   1 
HETATM 2579 O  O   B HOH P 8 .   ? -6.680  -3.785  6.773   0.50 29.60  ? 2100 HOH A O   1 
HETATM 2580 O  O   . HOH P 8 .   ? -4.524  -3.163  11.149  1.00 31.20  ? 2101 HOH A O   1 
HETATM 2581 O  O   . HOH P 8 .   ? -6.267  -1.480  8.731   1.00 29.39  ? 2102 HOH A O   1 
HETATM 2582 O  O   . HOH P 8 .   ? -7.327  -4.274  2.629   1.00 63.59  ? 2103 HOH A O   1 
HETATM 2583 O  O   . HOH P 8 .   ? 1.033   -4.264  0.324   1.00 20.97  ? 2104 HOH A O   1 
HETATM 2584 O  O   . HOH P 8 .   ? -8.912  -9.856  2.094   1.00 31.72  ? 2105 HOH A O   1 
HETATM 2585 O  O   . HOH P 8 .   ? -9.585  -7.596  3.634   1.00 44.79  ? 2106 HOH A O   1 
HETATM 2586 O  O   . HOH P 8 .   ? -7.176  -11.900 6.820   1.00 69.08  ? 2107 HOH A O   1 
HETATM 2587 O  O   . HOH P 8 .   ? -9.034  -9.158  8.706   1.00 33.22  ? 2108 HOH A O   1 
HETATM 2588 O  O   . HOH P 8 .   ? -3.799  -16.727 8.226   1.00 36.74  ? 2109 HOH A O   1 
HETATM 2589 O  O   . HOH P 8 .   ? 2.867   -10.853 4.770   1.00 15.55  ? 2110 HOH A O   1 
HETATM 2590 O  O   . HOH P 8 .   ? 0.514   -18.484 13.156  1.00 19.43  ? 2111 HOH A O   1 
HETATM 2591 O  O   . HOH P 8 .   ? -1.926  -18.216 13.682  1.00 21.18  ? 2112 HOH A O   1 
HETATM 2592 O  O   . HOH P 8 .   ? 2.945   -19.546 14.237  1.00 16.09  ? 2113 HOH A O   1 
HETATM 2593 O  O   . HOH P 8 .   ? 5.913   -18.629 14.618  1.00 18.37  ? 2114 HOH A O   1 
HETATM 2594 O  O   . HOH P 8 .   ? 10.992  -16.535 19.392  1.00 10.00  ? 2115 HOH A O   1 
HETATM 2595 O  O   . HOH P 8 .   ? 16.314  -17.722 14.882  1.00 26.56  ? 2116 HOH A O   1 
HETATM 2596 O  O   . HOH P 8 .   ? 16.021  -13.859 14.299  1.00 60.43  ? 2117 HOH A O   1 
HETATM 2597 O  O   . HOH P 8 .   ? 17.740  -19.072 18.503  1.00 32.61  ? 2118 HOH A O   1 
HETATM 2598 O  O   . HOH P 8 .   ? 11.573  -23.040 14.708  1.00 43.25  ? 2119 HOH A O   1 
HETATM 2599 O  O   . HOH P 8 .   ? 6.711   -22.930 15.712  1.00 24.77  ? 2120 HOH A O   1 
HETATM 2600 O  O   . HOH P 8 .   ? 6.971   -30.763 20.223  1.00 80.96  ? 2121 HOH A O   1 
HETATM 2601 O  O   . HOH P 8 .   ? 6.212   -25.043 24.308  1.00 22.62  ? 2122 HOH A O   1 
HETATM 2602 O  O   . HOH P 8 .   ? 0.511   -18.434 23.586  1.00 11.07  ? 2123 HOH A O   1 
HETATM 2603 O  O   . HOH P 8 .   ? 1.800   -20.173 29.993  1.00 17.01  ? 2124 HOH A O   1 
HETATM 2604 O  O   . HOH P 8 .   ? 8.352   -17.293 29.488  1.00 17.83  ? 2125 HOH A O   1 
HETATM 2605 O  O   . HOH P 8 .   ? 9.071   -21.535 32.652  1.00 23.44  ? 2126 HOH A O   1 
HETATM 2606 O  O   . HOH P 8 .   ? 6.280   -21.625 34.296  1.00 74.20  ? 2127 HOH A O   1 
HETATM 2607 O  O   . HOH P 8 .   ? 2.407   -22.725 30.899  1.00 29.33  ? 2128 HOH A O   1 
HETATM 2608 O  O   . HOH P 8 .   ? 2.162   -24.790 27.980  1.00 28.01  ? 2129 HOH A O   1 
HETATM 2609 O  O   . HOH P 8 .   ? 5.932   -26.413 29.962  1.00 47.94  ? 2130 HOH A O   1 
HETATM 2610 O  O   . HOH P 8 .   ? 4.160   -25.999 25.834  1.00 31.97  ? 2131 HOH A O   1 
HETATM 2611 O  O   . HOH P 8 .   ? 9.180   -24.800 28.171  1.00 21.00  ? 2132 HOH A O   1 
HETATM 2612 O  O   . HOH P 8 .   ? 11.677  -17.940 26.684  1.00 21.36  ? 2133 HOH A O   1 
HETATM 2613 O  O   . HOH P 8 .   ? 12.053  -25.669 27.338  1.00 73.27  ? 2134 HOH A O   1 
HETATM 2614 O  O   . HOH P 8 .   ? 12.987  -25.350 19.560  1.00 44.69  ? 2135 HOH A O   1 
HETATM 2615 O  O   . HOH P 8 .   ? 11.232  -17.162 21.966  1.00 12.57  ? 2136 HOH A O   1 
HETATM 2616 O  O   . HOH P 8 .   ? -1.739  -14.338 29.063  1.00 22.85  ? 2137 HOH A O   1 
HETATM 2617 O  O   . HOH P 8 .   ? -2.451  -17.140 29.175  1.00 27.86  ? 2138 HOH A O   1 
HETATM 2618 O  O   . HOH P 8 .   ? -7.200  -15.589 29.944  1.00 22.41  ? 2139 HOH A O   1 
HETATM 2619 O  O   . HOH P 8 .   ? -4.143  -13.282 29.613  1.00 31.98  ? 2140 HOH A O   1 
HETATM 2620 O  O   . HOH P 8 .   ? -8.411  -12.033 29.717  1.00 17.97  ? 2141 HOH A O   1 
HETATM 2621 O  O   . HOH P 8 .   ? -13.484 -13.336 31.770  1.00 33.31  ? 2142 HOH A O   1 
HETATM 2622 O  O   . HOH P 8 .   ? -11.341 -11.103 31.124  1.00 74.27  ? 2143 HOH A O   1 
HETATM 2623 O  O   . HOH P 8 .   ? -15.852 -14.956 35.128  1.00 17.76  ? 2144 HOH A O   1 
HETATM 2624 O  O   . HOH P 8 .   ? -18.457 -15.857 34.050  1.00 18.46  ? 2145 HOH A O   1 
HETATM 2625 O  O   . HOH P 8 .   ? -25.064 -13.408 27.216  1.00 12.90  ? 2146 HOH A O   1 
HETATM 2626 O  O   . HOH P 8 .   ? -21.751 -6.533  27.329  1.00 27.46  ? 2147 HOH A O   1 
HETATM 2627 O  O   . HOH P 8 .   ? -23.356 -11.182 31.367  1.00 23.71  ? 2148 HOH A O   1 
HETATM 2628 O  O   . HOH P 8 .   ? -20.113 -8.879  33.422  1.00 24.54  ? 2149 HOH A O   1 
HETATM 2629 O  O   . HOH P 8 .   ? -11.249 -4.026  34.679  1.00 49.54  ? 2150 HOH A O   1 
HETATM 2630 O  O   . HOH P 8 .   ? 0.608   -11.846 33.823  1.00 63.09  ? 2151 HOH A O   1 
HETATM 2631 O  O   . HOH P 8 .   ? 2.986   -13.115 30.451  1.00 15.69  ? 2152 HOH A O   1 
HETATM 2632 O  O   . HOH P 8 .   ? 6.530   -10.497 33.565  1.00 29.97  ? 2153 HOH A O   1 
HETATM 2633 O  O   . HOH P 8 .   ? 6.660   -5.095  37.002  1.00 37.99  ? 2154 HOH A O   1 
HETATM 2634 O  O   . HOH P 8 .   ? 6.498   -13.556 30.880  1.00 16.19  ? 2155 HOH A O   1 
HETATM 2635 O  O   . HOH P 8 .   ? 12.807  -12.091 25.083  1.00 34.92  ? 2156 HOH A O   1 
HETATM 2636 O  O   . HOH P 8 .   ? 8.486   0.704   20.794  1.00 15.29  ? 2157 HOH A O   1 
HETATM 2637 O  O   . HOH P 8 .   ? 11.772  1.867   21.866  1.00 34.30  ? 2158 HOH A O   1 
HETATM 2638 O  O   . HOH P 8 .   ? 16.757  -0.794  24.192  1.00 46.76  ? 2159 HOH A O   1 
HETATM 2639 O  O   . HOH P 8 .   ? 16.007  -0.739  19.923  1.00 42.97  ? 2160 HOH A O   1 
HETATM 2640 O  O   . HOH P 8 .   ? 18.006  -1.613  21.784  1.00 56.95  ? 2161 HOH A O   1 
HETATM 2641 O  O   . HOH P 8 .   ? 13.820  -2.939  17.339  1.00 37.45  ? 2162 HOH A O   1 
HETATM 2642 O  O   A HOH P 8 .   ? 16.956  -6.039  16.067  0.50 34.36  ? 2163 HOH A O   1 
HETATM 2643 O  O   B HOH P 8 .   ? 17.789  -4.828  17.417  0.50 32.39  ? 2163 HOH A O   1 
HETATM 2644 O  O   . HOH P 8 .   ? 18.303  -6.576  21.415  1.00 21.41  ? 2165 HOH A O   1 
HETATM 2645 O  O   . HOH P 8 .   ? 13.612  -9.309  15.661  1.00 32.32  ? 2166 HOH A O   1 
HETATM 2646 O  O   . HOH P 8 .   ? 11.753  -6.694  16.581  1.00 16.66  ? 2167 HOH A O   1 
HETATM 2647 O  O   . HOH P 8 .   ? 16.037  -12.332 19.452  1.00 106.75 ? 2168 HOH A O   1 
HETATM 2648 O  O   . HOH P 8 .   ? 9.104   -1.095  14.503  1.00 33.25  ? 2169 HOH A O   1 
HETATM 2649 O  O   . HOH P 8 .   ? 9.837   1.377   18.510  1.00 24.60  ? 2170 HOH A O   1 
HETATM 2650 O  O   . HOH P 8 .   ? 12.035  -8.262  11.390  1.00 40.87  ? 2171 HOH A O   1 
HETATM 2651 O  O   . HOH P 8 .   ? -4.175  -19.835 14.506  1.00 18.06  ? 2172 HOH A O   1 
HETATM 2652 O  O   . HOH P 8 .   ? -14.806 -22.083 16.712  1.00 40.51  ? 2173 HOH A O   1 
HETATM 2653 O  O   . HOH P 8 .   ? -12.280 -27.049 17.446  1.00 45.72  ? 2174 HOH A O   1 
HETATM 2654 O  O   . HOH P 8 .   ? -8.805  -24.115 13.200  1.00 47.39  ? 2175 HOH A O   1 
HETATM 2655 O  O   . HOH P 8 .   ? -8.557  -24.753 20.524  1.00 25.08  ? 2176 HOH A O   1 
HETATM 2656 O  O   . HOH P 8 .   ? -11.168 -23.795 21.660  1.00 18.98  ? 2177 HOH A O   1 
HETATM 2657 O  O   . HOH P 8 .   ? -6.294  -23.995 26.560  1.00 19.74  ? 2178 HOH A O   1 
HETATM 2658 O  O   . HOH P 8 .   ? -5.929  -28.483 21.376  1.00 33.12  ? 2179 HOH A O   1 
HETATM 2659 O  O   . HOH P 8 .   ? 1.670   -30.815 22.510  1.00 24.17  ? 2180 HOH A O   1 
HETATM 2660 O  O   . HOH P 8 .   ? 4.905   -28.664 23.697  1.00 65.44  ? 2181 HOH A O   1 
HETATM 2661 O  O   . HOH P 8 .   ? 0.059   -32.051 27.022  1.00 30.20  ? 2182 HOH A O   1 
HETATM 2662 O  O   . HOH P 8 .   ? -4.764  -33.916 19.140  1.00 33.22  ? 2183 HOH A O   1 
HETATM 2663 O  O   . HOH P 8 .   ? -5.675  -31.419 21.844  1.00 22.11  ? 2184 HOH A O   1 
HETATM 2664 O  O   . HOH P 8 .   ? -4.586  -29.521 14.705  1.00 95.75  ? 2185 HOH A O   1 
HETATM 2665 O  O   . HOH P 8 .   ? -1.777  -30.930 13.955  1.00 26.92  ? 2186 HOH A O   1 
HETATM 2666 O  O   . HOH P 8 .   ? -0.214  -34.366 14.212  1.00 39.28  ? 2187 HOH A O   1 
HETATM 2667 O  O   . HOH P 8 .   ? 4.662   -27.983 16.467  1.00 27.03  ? 2188 HOH A O   1 
HETATM 2668 O  O   . HOH P 8 .   ? 3.505   -30.391 9.858   1.00 35.93  ? 2189 HOH A O   1 
HETATM 2669 O  O   . HOH P 8 .   ? 5.812   -29.707 11.136  1.00 41.55  ? 2190 HOH A O   1 
HETATM 2670 O  O   . HOH P 8 .   ? -3.503  -27.709 9.899   1.00 45.88  ? 2191 HOH A O   1 
HETATM 2671 O  O   . HOH P 8 .   ? -1.899  -24.403 11.589  1.00 30.84  ? 2192 HOH A O   1 
HETATM 2672 O  O   . HOH P 8 .   ? 0.218   -25.271 12.010  1.00 24.11  ? 2193 HOH A O   1 
HETATM 2673 O  O   . HOH P 8 .   ? 6.780   -27.711 15.619  1.00 41.28  ? 2194 HOH A O   1 
HETATM 2674 O  O   . HOH P 8 .   ? 7.921   -28.384 11.953  1.00 44.41  ? 2195 HOH A O   1 
HETATM 2675 O  O   . HOH P 8 .   ? -4.926  -17.894 11.862  1.00 26.38  ? 2196 HOH A O   1 
HETATM 2676 O  O   . HOH P 8 .   ? -11.956 -14.984 11.409  1.00 36.73  ? 2197 HOH A O   1 
HETATM 2677 O  O   . HOH P 8 .   ? -10.502 -10.866 10.411  1.00 43.48  ? 2198 HOH A O   1 
HETATM 2678 O  O   . HOH P 8 .   ? -8.512  -12.830 9.317   1.00 35.36  ? 2199 HOH A O   1 
HETATM 2679 O  O   . HOH P 8 .   ? 0.413   -19.095 10.750  1.00 30.00  ? 2200 HOH A O   1 
HETATM 2680 O  O   . HOH P 8 .   ? -6.881  -3.376  11.844  1.00 102.79 ? 2201 HOH A O   1 
HETATM 2681 O  O   . HOH P 8 .   ? -3.664  -1.088  12.923  1.00 21.21  ? 2202 HOH A O   1 
HETATM 2682 O  O   . HOH P 8 .   ? 6.409   8.495   22.270  1.00 28.67  ? 2203 HOH A O   1 
HETATM 2683 O  O   . HOH P 8 .   ? -0.326  8.057   22.050  1.00 18.96  ? 2204 HOH A O   1 
HETATM 2684 O  O   . HOH P 8 .   ? -0.558  7.594   24.859  1.00 91.80  ? 2205 HOH A O   1 
HETATM 2685 O  O   . HOH P 8 .   ? -1.405  10.535  21.411  1.00 12.81  ? 2206 HOH A O   1 
HETATM 2686 O  O   . HOH P 8 .   ? 1.662   13.782  27.755  1.00 21.00  ? 2207 HOH A O   1 
HETATM 2687 O  O   . HOH P 8 .   ? 6.367   7.833   26.278  1.00 36.88  ? 2208 HOH A O   1 
HETATM 2688 O  O   . HOH P 8 .   ? 6.044   10.781  24.600  1.00 69.27  ? 2209 HOH A O   1 
HETATM 2689 O  O   . HOH P 8 .   ? 0.896   9.462   27.860  1.00 29.75  ? 2210 HOH A O   1 
HETATM 2690 O  O   . HOH P 8 .   ? 17.128  -5.117  24.319  1.00 40.80  ? 2211 HOH A O   1 
HETATM 2691 O  O   . HOH P 8 .   ? -7.940  -19.071 9.114   1.00 44.85  ? 2212 HOH A O   1 
HETATM 2692 O  O   . HOH P 8 .   ? -8.400  -14.189 5.554   1.00 34.37  ? 2213 HOH A O   1 
HETATM 2693 O  O   . HOH P 8 .   ? -6.839  2.442   33.303  1.00 61.15  ? 2214 HOH A O   1 
HETATM 2694 O  O   . HOH Q 8 .   ? 19.174  -5.173  0.402   1.00 42.65  ? 2001 HOH F O   1 
HETATM 2695 O  O   . HOH Q 8 .   ? 17.800  -1.701  4.901   1.00 27.24  ? 2002 HOH F O   1 
HETATM 2696 O  O   . HOH Q 8 .   ? 16.793  -0.104  7.321   1.00 34.11  ? 2003 HOH F O   1 
HETATM 2697 O  O   . HOH Q 8 .   ? 11.295  -6.168  6.174   1.00 16.31  ? 2004 HOH F O   1 
HETATM 2698 O  O   . HOH Q 8 .   ? 10.742  -3.295  8.574   1.00 18.04  ? 2005 HOH F O   1 
HETATM 2699 O  O   . HOH Q 8 .   ? 5.114   -3.462  1.415   1.00 26.06  ? 2006 HOH F O   1 
HETATM 2700 O  O   . HOH Q 8 .   ? 7.551   -2.984  0.841   1.00 23.05  ? 2007 HOH F O   1 
HETATM 2701 O  O   . HOH Q 8 .   ? -13.038 12.789  7.249   1.00 64.68  ? 2008 HOH F O   1 
HETATM 2702 O  O   . HOH Q 8 .   ? -1.296  -0.313  8.468   1.00 9.03   ? 2009 HOH F O   1 
HETATM 2703 O  O   . HOH Q 8 .   ? -5.426  1.032   8.906   1.00 23.69  ? 2010 HOH F O   1 
HETATM 2704 O  O   . HOH Q 8 .   ? -7.570  0.842   3.289   1.00 87.13  ? 2011 HOH F O   1 
HETATM 2705 O  O   . HOH Q 8 .   ? 14.483  -0.327  -2.778  1.00 47.99  ? 2012 HOH F O   1 
HETATM 2706 O  O   . HOH Q 8 .   ? -9.050  7.572   9.679   1.00 40.73  ? 2013 HOH F O   1 
HETATM 2707 O  O   . HOH Q 8 .   ? -11.877 3.617   9.242   1.00 80.98  ? 2014 HOH F O   1 
HETATM 2708 O  O   . HOH Q 8 .   ? -11.991 11.086  5.405   1.00 22.72  ? 2015 HOH F O   1 
HETATM 2709 O  O   . HOH Q 8 .   ? -17.100 11.217  9.036   1.00 52.44  ? 2016 HOH F O   1 
HETATM 2710 O  O   . HOH Q 8 .   ? -10.089 10.251  9.612   1.00 25.25  ? 2017 HOH F O   1 
HETATM 2711 O  O   . HOH Q 8 .   ? -16.951 6.763   -2.274  1.00 54.27  ? 2018 HOH F O   1 
HETATM 2712 O  O   . HOH Q 8 .   ? -14.130 9.226   -1.224  1.00 39.60  ? 2019 HOH F O   1 
HETATM 2713 O  O   . HOH Q 8 .   ? -13.046 5.060   -2.390  1.00 55.28  ? 2020 HOH F O   1 
HETATM 2714 O  O   . HOH Q 8 .   ? 1.777   1.296   -7.093  1.00 32.80  ? 2021 HOH F O   1 
HETATM 2715 O  O   . HOH Q 8 .   ? -8.787  3.076   -7.605  1.00 46.28  ? 2022 HOH F O   1 
HETATM 2716 O  O   . HOH Q 8 .   ? -7.154  0.621   -0.608  1.00 36.87  ? 2023 HOH F O   1 
HETATM 2717 O  O   . HOH Q 8 .   ? -14.845 13.558  -1.238  1.00 41.15  ? 2024 HOH F O   1 
HETATM 2718 O  O   . HOH Q 8 .   ? -14.321 9.277   -5.239  1.00 51.50  ? 2025 HOH F O   1 
HETATM 2719 O  O   . HOH Q 8 .   ? -3.852  1.102   -2.824  1.00 28.96  ? 2026 HOH F O   1 
HETATM 2720 O  O   . HOH Q 8 .   ? -0.895  0.431   -3.499  1.00 30.69  ? 2027 HOH F O   1 
HETATM 2721 O  O   . HOH Q 8 .   ? 0.692   -3.271  -2.318  1.00 28.11  ? 2028 HOH F O   1 
HETATM 2722 O  O   . HOH Q 8 .   ? 15.708  1.636   -1.285  1.00 26.27  ? 2029 HOH F O   1 
HETATM 2723 O  O   . HOH Q 8 .   ? 15.569  -3.121  -1.883  1.00 38.97  ? 2030 HOH F O   1 
HETATM 2724 O  O   . HOH Q 8 .   ? 17.298  7.021   5.142   1.00 27.25  ? 2031 HOH F O   1 
HETATM 2725 O  O   . HOH Q 8 .   ? 18.461  2.265   0.589   1.00 21.90  ? 2032 HOH F O   1 
HETATM 2726 O  O   . HOH Q 8 .   ? 17.535  2.396   -3.257  1.00 41.01  ? 2033 HOH F O   1 
HETATM 2727 O  O   . HOH Q 8 .   ? 20.243  2.349   -1.681  1.00 39.03  ? 2034 HOH F O   1 
HETATM 2728 O  O   . HOH Q 8 .   ? 19.125  6.342   6.775   1.00 41.98  ? 2035 HOH F O   1 
HETATM 2729 O  O   . HOH Q 8 .   ? 18.759  4.227   9.521   1.00 33.89  ? 2036 HOH F O   1 
HETATM 2730 O  O   . HOH Q 8 .   ? 17.945  14.035  8.968   1.00 34.97  ? 2037 HOH F O   1 
HETATM 2731 O  O   . HOH Q 8 .   ? 21.119  16.088  12.297  1.00 48.06  ? 2038 HOH F O   1 
HETATM 2732 O  O   . HOH Q 8 .   ? 19.723  8.414   3.499   1.00 34.69  ? 2039 HOH F O   1 
HETATM 2733 O  O   . HOH Q 8 .   ? 13.584  26.236  4.002   1.00 42.41  ? 2040 HOH F O   1 
HETATM 2734 O  O   . HOH Q 8 .   ? 9.187   4.825   -5.454  1.00 34.17  ? 2041 HOH F O   1 
HETATM 2735 O  O   . HOH Q 8 .   ? 9.170   13.646  -2.610  1.00 24.56  ? 2042 HOH F O   1 
HETATM 2736 O  O   . HOH Q 8 .   ? 9.774   15.977  -3.938  1.00 29.48  ? 2043 HOH F O   1 
HETATM 2737 O  O   . HOH Q 8 .   ? 2.557   4.066   -7.681  1.00 38.17  ? 2044 HOH F O   1 
HETATM 2738 O  O   . HOH Q 8 .   ? -6.462  2.942   -5.764  1.00 57.18  ? 2045 HOH F O   1 
HETATM 2739 O  O   . HOH Q 8 .   ? -11.319 7.177   -6.208  1.00 20.76  ? 2046 HOH F O   1 
HETATM 2740 O  O   . HOH Q 8 .   ? -12.625 12.618  -0.018  1.00 20.28  ? 2047 HOH F O   1 
HETATM 2741 O  O   . HOH Q 8 .   ? -13.288 12.021  -5.508  1.00 40.46  ? 2048 HOH F O   1 
HETATM 2742 O  O   . HOH Q 8 .   ? -11.405 13.611  -7.307  1.00 37.12  ? 2049 HOH F O   1 
HETATM 2743 O  O   . HOH Q 8 .   ? -10.430 14.302  -0.145  1.00 18.62  ? 2050 HOH F O   1 
HETATM 2744 O  O   . HOH Q 8 .   ? -10.488 16.867  0.823   1.00 18.14  ? 2051 HOH F O   1 
HETATM 2745 O  O   . HOH Q 8 .   ? -8.683  18.702  -2.935  1.00 75.92  ? 2052 HOH F O   1 
HETATM 2746 O  O   . HOH Q 8 .   ? 12.828  -4.114  12.391  1.00 37.15  ? 2053 HOH F O   1 
HETATM 2747 O  O   . HOH Q 8 .   ? -12.903 16.325  -6.639  1.00 27.87  ? 2054 HOH F O   1 
HETATM 2748 O  O   . HOH Q 8 .   ? -10.406 20.246  -6.869  1.00 94.27  ? 2055 HOH F O   1 
HETATM 2749 O  O   . HOH Q 8 .   ? -13.053 18.070  -8.711  1.00 53.47  ? 2056 HOH F O   1 
HETATM 2750 O  O   A HOH Q 8 .   ? -8.080  15.290  -13.043 0.50 15.79  ? 2057 HOH F O   1 
HETATM 2751 O  O   B HOH Q 8 .   ? -7.857  14.019  -13.739 0.50 16.03  ? 2057 HOH F O   1 
HETATM 2752 O  O   . HOH Q 8 .   ? -7.004  16.473  -12.885 1.00 31.30  ? 2058 HOH F O   1 
HETATM 2753 O  O   . HOH Q 8 .   ? -0.387  18.729  8.355   1.00 14.10  ? 2059 HOH F O   1 
HETATM 2754 O  O   . HOH Q 8 .   ? 7.836   32.895  5.491   1.00 51.74  ? 2060 HOH F O   1 
HETATM 2755 O  O   A HOH Q 8 .   ? 8.309   13.857  16.843  0.50 11.61  ? 2061 HOH F O   1 
HETATM 2756 O  O   B HOH Q 8 .   ? 7.852   13.545  16.829  0.50 30.36  ? 2061 HOH F O   1 
HETATM 2757 O  O   . HOH Q 8 .   ? 7.860   9.211   19.911  1.00 26.39  ? 2062 HOH F O   1 
HETATM 2758 O  O   . HOH Q 8 .   ? 8.959   11.745  18.248  1.00 30.09  ? 2063 HOH F O   1 
HETATM 2759 O  O   . HOH Q 8 .   ? -2.882  2.451   17.406  1.00 11.40  ? 2064 HOH F O   1 
HETATM 2760 O  O   . HOH Q 8 .   ? -12.683 18.026  15.819  1.00 36.72  ? 2065 HOH F O   1 
HETATM 2761 O  O   . HOH Q 8 .   ? -4.004  7.515   14.333  1.00 28.65  ? 2066 HOH F O   1 
HETATM 2762 O  O   . HOH Q 8 .   ? -2.472  5.537   24.141  1.00 29.85  ? 2067 HOH F O   1 
HETATM 2763 O  O   . HOH Q 8 .   ? -3.720  9.413   22.223  1.00 28.62  ? 2068 HOH F O   1 
HETATM 2764 O  O   . HOH Q 8 .   ? -9.826  3.877   16.059  1.00 30.01  ? 2069 HOH F O   1 
HETATM 2765 O  O   . HOH Q 8 .   ? -4.996  2.862   12.244  1.00 30.48  ? 2070 HOH F O   1 
HETATM 2766 O  O   . HOH Q 8 .   ? -7.546  1.046   13.510  1.00 30.45  ? 2071 HOH F O   1 
HETATM 2767 O  O   . HOH Q 8 .   ? -8.569  6.233   11.910  1.00 31.49  ? 2072 HOH F O   1 
HETATM 2768 O  O   . HOH Q 8 .   ? 9.591   -11.634 0.014   1.00 34.82  ? 2073 HOH F O   1 
HETATM 2769 O  O   . HOH Q 8 .   ? -11.043 12.014  16.397  1.00 39.88  ? 2074 HOH F O   1 
HETATM 2770 O  O   . HOH Q 8 .   ? -12.988 9.604   18.052  1.00 29.01  ? 2075 HOH F O   1 
HETATM 2771 O  O   . HOH Q 8 .   ? -9.961  8.629   12.069  1.00 38.89  ? 2076 HOH F O   1 
HETATM 2772 O  O   . HOH Q 8 .   ? -3.005  15.534  16.690  1.00 15.11  ? 2077 HOH F O   1 
HETATM 2773 O  O   . HOH Q 8 .   ? -8.718  15.277  19.507  1.00 32.07  ? 2078 HOH F O   1 
HETATM 2774 O  O   . HOH Q 8 .   ? -5.475  16.517  15.349  1.00 35.97  ? 2079 HOH F O   1 
HETATM 2775 O  O   . HOH Q 8 .   ? 0.700   18.245  13.009  1.00 21.78  ? 2080 HOH F O   1 
HETATM 2776 O  O   . HOH Q 8 .   ? 6.607   16.828  16.546  1.00 147.83 ? 2081 HOH F O   1 
HETATM 2777 O  O   . HOH Q 8 .   ? 12.802  16.160  12.580  1.00 10.28  ? 2083 HOH F O   1 
HETATM 2778 O  O   . HOH Q 8 .   ? 8.613   21.871  16.456  1.00 23.95  ? 2084 HOH F O   1 
HETATM 2779 O  O   . HOH Q 8 .   ? 15.208  17.190  19.106  1.00 13.57  ? 2085 HOH F O   1 
HETATM 2780 O  O   . HOH Q 8 .   ? 18.274  18.602  16.570  1.00 18.04  ? 2086 HOH F O   1 
HETATM 2781 O  O   . HOH Q 8 .   ? 7.238   22.640  13.770  1.00 27.02  ? 2087 HOH F O   1 
HETATM 2782 O  O   . HOH Q 8 .   ? 16.523  17.412  6.237   1.00 25.92  ? 2088 HOH F O   1 
HETATM 2783 O  O   . HOH Q 8 .   ? 16.341  16.173  8.704   1.00 22.56  ? 2089 HOH F O   1 
HETATM 2784 O  O   . HOH Q 8 .   ? 20.381  18.210  14.650  1.00 39.41  ? 2090 HOH F O   1 
HETATM 2785 O  O   . HOH Q 8 .   ? 21.103  21.483  14.611  1.00 93.07  ? 2091 HOH F O   1 
HETATM 2786 O  O   . HOH Q 8 .   ? 9.534   30.726  10.421  1.00 63.17  ? 2092 HOH F O   1 
HETATM 2787 O  O   . HOH Q 8 .   ? 13.487  29.398  12.544  1.00 26.88  ? 2093 HOH F O   1 
HETATM 2788 O  O   . HOH Q 8 .   ? 5.762   18.135  3.763   1.00 12.16  ? 2094 HOH F O   1 
HETATM 2789 O  O   . HOH Q 8 .   ? 9.931   19.833  -1.210  1.00 19.81  ? 2095 HOH F O   1 
HETATM 2790 O  O   . HOH Q 8 .   ? 15.792  15.601  1.235   1.00 32.03  ? 2096 HOH F O   1 
HETATM 2791 O  O   . HOH Q 8 .   ? 16.140  17.236  3.311   1.00 54.98  ? 2097 HOH F O   1 
HETATM 2792 O  O   . HOH Q 8 .   ? 9.397   24.505  0.930   1.00 40.03  ? 2098 HOH F O   1 
HETATM 2793 O  O   . HOH Q 8 .   ? 9.895   25.747  3.635   1.00 25.17  ? 2099 HOH F O   1 
HETATM 2794 O  O   . HOH Q 8 .   ? 10.504  22.527  -1.301  1.00 31.89  ? 2100 HOH F O   1 
HETATM 2795 O  O   . HOH Q 8 .   ? 16.586  23.632  2.060   1.00 66.29  ? 2101 HOH F O   1 
HETATM 2796 O  O   . HOH Q 8 .   ? 15.627  24.538  4.083   1.00 30.43  ? 2102 HOH F O   1 
HETATM 2797 O  O   . HOH Q 8 .   ? 11.575  24.630  5.271   1.00 72.01  ? 2103 HOH F O   1 
HETATM 2798 O  O   . HOH Q 8 .   ? 18.083  22.886  8.697   1.00 45.22  ? 2104 HOH F O   1 
HETATM 2799 O  O   . HOH Q 8 .   ? 14.356  16.838  10.434  1.00 15.33  ? 2105 HOH F O   1 
HETATM 2800 O  O   . HOH Q 8 .   ? 6.461   14.047  -2.014  1.00 25.44  ? 2106 HOH F O   1 
HETATM 2801 O  O   . HOH Q 8 .   ? 4.337   18.752  -2.969  1.00 42.16  ? 2107 HOH F O   1 
HETATM 2802 O  O   . HOH Q 8 .   ? 5.903   16.891  -2.583  1.00 21.84  ? 2108 HOH F O   1 
HETATM 2803 O  O   . HOH Q 8 .   ? 2.015   15.422  -5.527  1.00 25.29  ? 2109 HOH F O   1 
HETATM 2804 O  O   . HOH Q 8 .   ? 4.547   12.997  -3.683  1.00 27.31  ? 2110 HOH F O   1 
HETATM 2805 O  O   . HOH Q 8 .   ? 0.946   11.812  -5.921  1.00 23.46  ? 2111 HOH F O   1 
HETATM 2806 O  O   . HOH Q 8 .   ? -2.797  13.027  -10.297 1.00 41.15  ? 2112 HOH F O   1 
HETATM 2807 O  O   . HOH Q 8 .   ? -0.905  11.020  -8.611  1.00 31.19  ? 2113 HOH F O   1 
HETATM 2808 O  O   . HOH Q 8 .   ? 0.852   18.384  -8.086  1.00 17.28  ? 2114 HOH F O   1 
HETATM 2809 O  O   . HOH Q 8 .   ? -0.253  17.130  -9.058  1.00 41.57  ? 2115 HOH F O   1 
HETATM 2810 O  O   . HOH Q 8 .   ? -9.286  11.891  -13.612 1.00 30.58  ? 2116 HOH F O   1 
HETATM 2811 O  O   . HOH Q 8 .   ? -7.903  8.873   -14.880 1.00 33.94  ? 2117 HOH F O   1 
HETATM 2812 O  O   . HOH Q 8 .   ? -14.003 20.702  -12.806 1.00 42.67  ? 2118 HOH F O   1 
HETATM 2813 O  O   . HOH Q 8 .   ? -11.627 21.280  -13.025 1.00 32.40  ? 2119 HOH F O   1 
HETATM 2814 O  O   A HOH Q 8 .   ? 3.544   10.906  -4.922  0.50 90.28  ? 2120 HOH F O   1 
HETATM 2815 O  O   B HOH Q 8 .   ? 3.086   11.047  -4.914  0.50 106.68 ? 2120 HOH F O   1 
HETATM 2816 O  O   . HOH Q 8 .   ? 7.608   12.116  -5.626  1.00 37.51  ? 2122 HOH F O   1 
HETATM 2817 O  O   . HOH Q 8 .   ? 10.536  11.686  -4.635  1.00 39.65  ? 2123 HOH F O   1 
HETATM 2818 O  O   . HOH Q 8 .   ? 11.386  12.916  -0.937  1.00 21.21  ? 2124 HOH F O   1 
HETATM 2819 O  O   . HOH Q 8 .   ? 19.540  8.283   -4.058  1.00 41.16  ? 2125 HOH F O   1 
HETATM 2820 O  O   . HOH Q 8 .   ? 16.139  10.016  -1.840  1.00 26.42  ? 2126 HOH F O   1 
HETATM 2821 O  O   . HOH Q 8 .   ? 14.920  13.130  0.602   1.00 29.87  ? 2127 HOH F O   1 
HETATM 2822 O  O   . HOH Q 8 .   ? 19.235  12.936  4.237   1.00 47.06  ? 2128 HOH F O   1 
HETATM 2823 O  O   . HOH Q 8 .   ? 20.211  9.178   0.630   1.00 35.65  ? 2129 HOH F O   1 
HETATM 2824 O  O   . HOH Q 8 .   ? 17.422  10.701  8.548   1.00 33.33  ? 2130 HOH F O   1 
HETATM 2825 O  O   . HOH Q 8 .   ? 17.442  6.526   11.391  1.00 23.13  ? 2131 HOH F O   1 
HETATM 2826 O  O   . HOH Q 8 .   ? 14.828  -2.048  11.601  1.00 113.29 ? 2132 HOH F O   1 
HETATM 2827 O  O   . HOH Q 8 .   ? 11.263  -1.060  10.103  1.00 17.57  ? 2133 HOH F O   1 
HETATM 2828 O  O   . HOH Q 8 .   ? 17.132  -0.167  14.139  1.00 43.43  ? 2134 HOH F O   1 
HETATM 2829 O  O   . HOH Q 8 .   ? 14.269  2.023   15.554  1.00 55.83  ? 2135 HOH F O   1 
HETATM 2830 O  O   . HOH Q 8 .   ? 20.318  6.098   13.835  1.00 49.61  ? 2136 HOH F O   1 
HETATM 2831 O  O   . HOH Q 8 .   ? 12.281  6.404   15.356  1.00 17.51  ? 2137 HOH F O   1 
HETATM 2832 O  O   . HOH Q 8 .   ? 13.692  9.146   17.357  1.00 40.46  ? 2138 HOH F O   1 
HETATM 2833 O  O   . HOH Q 8 .   ? 13.350  -0.204  14.040  1.00 43.77  ? 2139 HOH F O   1 
HETATM 2834 O  O   . HOH Q 8 .   ? 11.289  -1.761  12.749  1.00 26.53  ? 2140 HOH F O   1 
HETATM 2835 O  O   . HOH Q 8 .   ? 10.249  8.839   19.442  1.00 37.28  ? 2141 HOH F O   1 
HETATM 2836 O  O   . HOH Q 8 .   ? 10.196  6.767   20.172  1.00 39.44  ? 2142 HOH F O   1 
HETATM 2837 O  O   . HOH Q 8 .   ? -2.827  19.618  9.521   1.00 18.64  ? 2143 HOH F O   1 
HETATM 2838 O  O   . HOH Q 8 .   ? -9.720  21.900  8.407   1.00 51.05  ? 2144 HOH F O   1 
HETATM 2839 O  O   . HOH Q 8 .   ? -12.897 16.736  1.743   1.00 69.96  ? 2145 HOH F O   1 
HETATM 2840 O  O   . HOH Q 8 .   ? -14.233 17.832  4.242   1.00 61.50  ? 2146 HOH F O   1 
HETATM 2841 O  O   . HOH Q 8 .   ? -7.921  27.260  3.032   1.00 45.88  ? 2147 HOH F O   1 
HETATM 2842 O  O   . HOH Q 8 .   ? -5.377  23.601  -0.199  1.00 21.20  ? 2148 HOH F O   1 
HETATM 2843 O  O   . HOH Q 8 .   ? -3.568  24.461  2.093   1.00 24.97  ? 2149 HOH F O   1 
HETATM 2844 O  O   . HOH Q 8 .   ? 1.148   23.690  -2.126  1.00 20.14  ? 2150 HOH F O   1 
HETATM 2845 O  O   . HOH Q 8 .   ? -0.957  28.103  2.740   1.00 49.21  ? 2151 HOH F O   1 
HETATM 2846 O  O   . HOH Q 8 .   ? 6.157   30.436  5.291   1.00 25.69  ? 2152 HOH F O   1 
HETATM 2847 O  O   . HOH Q 8 .   ? 9.706   28.282  5.768   1.00 38.01  ? 2153 HOH F O   1 
HETATM 2848 O  O   . HOH Q 8 .   ? 6.789   31.882  0.567   1.00 41.03  ? 2154 HOH F O   1 
HETATM 2849 O  O   . HOH Q 8 .   ? -0.959  30.480  11.047  1.00 56.93  ? 2155 HOH F O   1 
HETATM 2850 O  O   . HOH Q 8 .   ? -2.636  29.584  8.465   1.00 60.03  ? 2156 HOH F O   1 
HETATM 2851 O  O   . HOH Q 8 .   ? 0.128   33.833  11.414  1.00 38.79  ? 2157 HOH F O   1 
HETATM 2852 O  O   . HOH Q 8 .   ? 4.995   29.216  13.780  1.00 30.11  ? 2158 HOH F O   1 
HETATM 2853 O  O   . HOH Q 8 .   ? 2.133   33.980  17.270  1.00 112.97 ? 2159 HOH F O   1 
HETATM 2854 O  O   . HOH Q 8 .   ? -4.179  26.619  13.736  1.00 38.42  ? 2160 HOH F O   1 
HETATM 2855 O  O   . HOH Q 8 .   ? -4.660  24.224  14.755  1.00 36.25  ? 2161 HOH F O   1 
HETATM 2856 O  O   . HOH Q 8 .   ? 6.735   27.523  13.115  1.00 41.00  ? 2162 HOH F O   1 
HETATM 2857 O  O   . HOH Q 8 .   ? -4.676  17.579  11.424  1.00 25.18  ? 2163 HOH F O   1 
HETATM 2858 O  O   . HOH Q 8 .   ? -7.462  21.174  10.372  1.00 49.51  ? 2164 HOH F O   1 
HETATM 2859 O  O   . HOH Q 8 .   ? -10.807 15.014  10.431  1.00 35.27  ? 2165 HOH F O   1 
HETATM 2860 O  O   . HOH Q 8 .   ? -10.845 17.722  12.089  1.00 58.40  ? 2166 HOH F O   1 
HETATM 2861 O  O   . HOH Q 8 .   ? -1.260  17.817  11.345  1.00 21.44  ? 2167 HOH F O   1 
HETATM 2862 O  O   . HOH Q 8 .   ? -0.623  18.853  15.078  1.00 27.40  ? 2168 HOH F O   1 
HETATM 2863 O  O   . HOH Q 8 .   ? -6.584  3.449   10.356  1.00 31.47  ? 2169 HOH F O   1 
HETATM 2864 O  O   . HOH Q 8 .   ? -3.223  0.774   11.105  1.00 21.40  ? 2170 HOH F O   1 
HETATM 2865 O  O   . HOH Q 8 .   ? 10.170  -8.914  7.804   1.00 26.07  ? 2171 HOH F O   1 
HETATM 2866 O  O   . HOH Q 8 .   ? 5.516   -8.324  1.819   1.00 87.53  ? 2172 HOH F O   1 
HETATM 2867 O  O   . HOH Q 8 .   ? 7.874   -9.732  0.188   1.00 30.87  ? 2173 HOH F O   1 
HETATM 2868 O  O   . HOH Q 8 .   ? 8.671   -14.089 0.694   1.00 24.26  ? 2174 HOH F O   1 
HETATM 2869 O  O   . HOH Q 8 .   ? 10.579  -11.378 6.065   1.00 34.72  ? 2175 HOH F O   1 
HETATM 2870 O  O   . HOH Q 8 .   ? 12.047  -7.990  4.280   1.00 31.68  ? 2176 HOH F O   1 
HETATM 2871 O  O   . HOH Q 8 .   ? -7.289  24.047  8.265   1.00 68.80  ? 2177 HOH F O   1 
# 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   1   ALA ALA A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   CYS 6   6   6   CYS CYS A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  PHE 50  50  50  PHE PHE A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ASP 52  52  52  ASP ASP A . n 
A 1 53  ASN 53  53  53  ASN ASN A . n 
A 1 54  THR 54  54  54  THR THR A . n 
A 1 55  ALA 55  55  55  ALA ALA A . n 
A 1 56  GLY 56  56  56  GLY GLY A . n 
A 1 57  CYS 57  57  57  CYS CYS A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  SER 59  59  59  SER SER A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  GLY 61  61  61  GLY GLY A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  HIS 63  63  63  HIS HIS A . n 
A 1 64  PHE 64  64  64  PHE PHE A . n 
A 1 65  ASN 65  65  65  ASN ASN A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  LEU 67  67  67  LEU LEU A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  LYS 70  70  70  LYS LYS A . n 
A 1 71  HIS 71  71  71  HIS HIS A . n 
A 1 72  GLY 72  72  72  GLY GLY A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LYS 75  75  75  LYS LYS A . n 
A 1 76  ASP 76  76  76  ASP ASP A . n 
A 1 77  GLU 77  77  77  GLU GLU A . n 
A 1 78  GLU 78  78  78  GLU GLU A . n 
A 1 79  ARG 79  79  79  ARG ARG A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  VAL 81  81  81  VAL VAL A . n 
A 1 82  GLY 82  82  82  GLY GLY A . n 
A 1 83  ASP 83  83  83  ASP ASP A . n 
A 1 84  LEU 84  84  84  LEU LEU A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  ASN 86  86  86  ASN ASN A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  THR 88  88  88  THR THR A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  ASP 90  90  90  ASP ASP A . n 
A 1 91  LYS 91  91  91  LYS LYS A . n 
A 1 92  ASP 92  92  92  ASP ASP A . n 
A 1 93  GLY 93  93  93  GLY GLY A . n 
A 1 94  VAL 94  94  94  VAL VAL A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  ASP 96  96  96  ASP ASP A . n 
A 1 97  VAL 97  97  97  VAL VAL A . n 
A 1 98  SER 98  98  98  SER SER A . n 
A 1 99  THR 99  99  99  THR THR A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 CYS 111 111 111 CYS CYS A . n 
A 1 112 ILE 112 112 112 ILE ILE A . n 
A 1 113 THR 113 113 113 THR THR A . n 
A 1 114 GLY 114 114 114 GLY GLY A . n 
A 1 115 ARG 115 115 115 ARG ARG A . n 
A 1 116 THR 116 116 116 THR THR A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 VAL 118 118 118 VAL VAL A . n 
A 1 119 VAL 119 119 119 VAL VAL A . n 
A 1 120 HIS 120 120 120 HIS HIS A . n 
A 1 121 GLU 121 121 121 GLU GLU A . n 
A 1 122 LYS 122 122 122 LYS LYS A . n 
A 1 123 ALA 123 123 123 ALA ALA A . n 
A 1 124 ASP 124 124 124 ASP ASP A . n 
A 1 125 ASP 125 125 125 ASP ASP A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 GLY 127 127 127 GLY GLY A . n 
A 1 128 LYS 128 128 128 LYS LYS A . n 
A 1 129 GLY 129 129 129 GLY GLY A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ASN 131 131 131 ASN ASN A . n 
A 1 132 GLU 132 132 132 GLU GLU A . n 
A 1 133 GLU 133 133 133 GLU GLU A . n 
A 1 134 SER 134 134 134 SER SER A . n 
A 1 135 THR 135 135 135 THR THR A . n 
A 1 136 LYS 136 136 136 LYS LYS A . n 
A 1 137 THR 137 137 137 THR THR A . n 
A 1 138 GLY 138 138 138 GLY GLY A . n 
A 1 139 ASN 139 139 139 ASN ASN A . n 
A 1 140 ALA 140 140 140 ALA ALA A . n 
A 1 141 GLY 141 141 141 GLY GLY A . n 
A 1 142 SER 142 142 142 SER SER A . n 
A 1 143 ARG 143 143 143 ARG ARG A . n 
A 1 144 LEU 144 144 144 LEU LEU A . n 
A 1 145 ALA 145 145 145 ALA ALA A . n 
A 1 146 CYS 146 146 146 CYS CYS A . n 
A 1 147 GLY 147 147 147 GLY GLY A . n 
A 1 148 VAL 148 148 148 VAL VAL A . n 
A 1 149 ILE 149 149 149 ILE ILE A . n 
A 1 150 GLY 150 150 150 GLY GLY A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ALA 152 152 152 ALA ALA A . n 
A 1 153 GLN 153 153 153 GLN GLN A . n 
B 2 1   ALA 1   1   1   ALA ALA F . n 
B 2 2   THR 2   2   2   THR THR F . n 
B 2 3   LYS 3   3   3   LYS LYS F . n 
B 2 4   ALA 4   4   4   ALA ALA F . n 
B 2 5   VAL 5   5   5   VAL VAL F . n 
B 2 6   CYS 6   6   6   CYS CYS F . n 
B 2 7   VAL 7   7   7   VAL VAL F . n 
B 2 8   LEU 8   8   8   LEU LEU F . n 
B 2 9   LYS 9   9   9   LYS LYS F . n 
B 2 10  GLY 10  10  10  GLY GLY F . n 
B 2 11  ASP 11  11  11  ASP ASP F . n 
B 2 12  GLY 12  12  12  GLY GLY F . n 
B 2 13  PRO 13  13  13  PRO PRO F . n 
B 2 14  VAL 14  14  14  VAL VAL F . n 
B 2 15  GLN 15  15  15  GLN GLN F . n 
B 2 16  GLY 16  16  16  GLY GLY F . n 
B 2 17  ILE 17  17  17  ILE ILE F . n 
B 2 18  ILE 18  18  18  ILE ILE F . n 
B 2 19  ASN 19  19  19  ASN ASN F . n 
B 2 20  PHE 20  20  20  PHE PHE F . n 
B 2 21  GLU 21  21  21  GLU GLU F . n 
B 2 22  GLN 22  22  22  GLN GLN F . n 
B 2 23  LYS 23  23  23  LYS LYS F . n 
B 2 24  GLU 24  24  24  GLU GLU F . n 
B 2 25  SER 25  25  25  SER SER F . n 
B 2 26  ASN 26  26  26  ASN ASN F . n 
B 2 27  GLY 27  27  27  GLY GLY F . n 
B 2 28  PRO 28  28  28  PRO PRO F . n 
B 2 29  VAL 29  29  29  VAL VAL F . n 
B 2 30  LYS 30  30  30  LYS LYS F . n 
B 2 31  VAL 31  31  31  VAL VAL F . n 
B 2 32  TRP 32  32  32  TRP TRP F . n 
B 2 33  GLY 33  33  33  GLY GLY F . n 
B 2 34  SER 34  34  34  SER SER F . n 
B 2 35  ILE 35  35  35  ILE ILE F . n 
B 2 36  LYS 36  36  36  LYS LYS F . n 
B 2 37  GLY 37  37  37  GLY GLY F . n 
B 2 38  LEU 38  38  38  LEU LEU F . n 
B 2 39  THR 39  39  39  THR THR F . n 
B 2 40  GLU 40  40  40  GLU GLU F . n 
B 2 41  GLY 41  41  41  GLY GLY F . n 
B 2 42  LEU 42  42  42  LEU LEU F . n 
B 2 43  HIS 43  43  43  HIS HIS F . n 
B 2 44  GLY 44  44  44  GLY GLY F . n 
B 2 45  PHE 45  45  45  PHE PHE F . n 
B 2 46  HIS 46  46  46  HIS HIS F . n 
B 2 47  VAL 47  47  47  VAL VAL F . n 
B 2 48  HIS 48  48  48  HIS HIS F . n 
B 2 49  GLU 49  49  49  GLU GLU F . n 
B 2 50  PHE 50  50  50  PHE PHE F . n 
B 2 51  GLY 51  51  51  GLY GLY F . n 
B 2 52  ASP 52  52  52  ASP ASP F . n 
B 2 53  ASN 53  53  53  ASN ASN F . n 
B 2 54  THR 54  54  54  THR THR F . n 
B 2 55  ALA 55  55  55  ALA ALA F . n 
B 2 56  GLY 56  56  56  GLY GLY F . n 
B 2 57  CYS 57  57  57  CYS CYS F . n 
B 2 58  THR 58  58  58  THR THR F . n 
B 2 59  SER 59  59  59  SER SER F . n 
B 2 60  ALA 60  60  60  ALA ALA F . n 
B 2 61  GLY 61  61  61  GLY GLY F . n 
B 2 62  PRO 62  62  62  PRO PRO F . n 
B 2 63  HIS 63  63  63  HIS HIS F . n 
B 2 64  PHE 64  64  64  PHE PHE F . n 
B 2 65  ASN 65  65  65  ASN ASN F . n 
B 2 66  PRO 66  66  66  PRO PRO F . n 
B 2 67  LEU 67  67  67  LEU LEU F . n 
B 2 68  SER 68  68  68  SER SER F . n 
B 2 69  ARG 69  69  69  ARG ARG F . n 
B 2 70  LYS 70  70  70  LYS LYS F . n 
B 2 71  HIS 71  71  71  HIS HIS F . n 
B 2 72  GLY 72  72  72  GLY GLY F . n 
B 2 73  GLY 73  73  73  GLY GLY F . n 
B 2 74  PRO 74  74  74  PRO PRO F . n 
B 2 75  LYS 75  75  75  LYS LYS F . n 
B 2 76  ASP 76  76  76  ASP ASP F . n 
B 2 77  GLU 77  77  77  GLU GLU F . n 
B 2 78  GLU 78  78  78  GLU GLU F . n 
B 2 79  ARG 79  79  79  ARG ARG F . n 
B 2 80  HIS 80  80  80  HIS HIS F . n 
B 2 81  VAL 81  81  81  VAL VAL F . n 
B 2 82  GLY 82  82  82  GLY GLY F . n 
B 2 83  ASP 83  83  83  ASP ASP F . n 
B 2 84  LEU 84  84  84  LEU LEU F . n 
B 2 85  GLY 85  85  85  GLY GLY F . n 
B 2 86  ASN 86  86  86  ASN ASN F . n 
B 2 87  VAL 87  87  87  VAL VAL F . n 
B 2 88  THR 88  88  88  THR THR F . n 
B 2 89  ALA 89  89  89  ALA ALA F . n 
B 2 90  ASP 90  90  90  ASP ASP F . n 
B 2 91  LYS 91  91  91  LYS LYS F . n 
B 2 92  ASP 92  92  92  ASP ASP F . n 
B 2 93  GLY 93  93  93  GLY GLY F . n 
B 2 94  VAL 94  94  94  VAL VAL F . n 
B 2 95  ALA 95  95  95  ALA ALA F . n 
B 2 96  ASP 96  96  96  ASP ASP F . n 
B 2 97  VAL 97  97  97  VAL VAL F . n 
B 2 98  SER 98  98  98  SER SER F . n 
B 2 99  ILE 99  99  99  ILE ILE F . n 
B 2 100 GLU 100 100 100 GLU GLU F . n 
B 2 101 ASP 101 101 101 ASP ASP F . n 
B 2 102 SER 102 102 102 SER SER F . n 
B 2 103 VAL 103 103 103 VAL VAL F . n 
B 2 104 ILE 104 104 104 ILE ILE F . n 
B 2 105 SER 105 105 105 SER SER F . n 
B 2 106 LEU 106 106 106 LEU LEU F . n 
B 2 107 SER 107 107 107 SER SER F . n 
B 2 108 GLY 108 108 108 GLY GLY F . n 
B 2 109 ASP 109 109 109 ASP ASP F . n 
B 2 110 HIS 110 110 110 HIS HIS F . n 
B 2 111 CYS 111 111 111 CYS CYS F . n 
B 2 112 ILE 112 112 112 ILE ILE F . n 
B 2 113 THR 113 113 113 THR THR F . n 
B 2 114 GLY 114 114 114 GLY GLY F . n 
B 2 115 ARG 115 115 115 ARG ARG F . n 
B 2 116 THR 116 116 116 THR THR F . n 
B 2 117 LEU 117 117 117 LEU LEU F . n 
B 2 118 VAL 118 118 118 VAL VAL F . n 
B 2 119 VAL 119 119 119 VAL VAL F . n 
B 2 120 HIS 120 120 120 HIS HIS F . n 
B 2 121 GLU 121 121 121 GLU GLU F . n 
B 2 122 LYS 122 122 122 LYS LYS F . n 
B 2 123 ALA 123 123 123 ALA ALA F . n 
B 2 124 ASP 124 124 124 ASP ASP F . n 
B 2 125 ASP 125 125 125 ASP ASP F . n 
B 2 126 LEU 126 126 126 LEU LEU F . n 
B 2 127 GLY 127 127 127 GLY GLY F . n 
B 2 128 LYS 128 128 128 LYS LYS F . n 
B 2 129 GLY 129 129 129 GLY GLY F . n 
B 2 130 GLY 130 130 130 GLY GLY F . n 
B 2 131 ASN 131 131 131 ASN ASN F . n 
B 2 132 GLU 132 132 132 GLU GLU F . n 
B 2 133 GLU 133 133 133 GLU GLU F . n 
B 2 134 SER 134 134 134 SER SER F . n 
B 2 135 THR 135 135 135 THR THR F . n 
B 2 136 LYS 136 136 136 LYS LYS F . n 
B 2 137 THR 137 137 137 THR THR F . n 
B 2 138 GLY 138 138 138 GLY GLY F . n 
B 2 139 ASN 139 139 139 ASN ASN F . n 
B 2 140 ALA 140 140 140 ALA ALA F . n 
B 2 141 GLY 141 141 141 GLY GLY F . n 
B 2 142 SER 142 142 142 SER SER F . n 
B 2 143 ARG 143 143 143 ARG ARG F . n 
B 2 144 LEU 144 144 144 LEU LEU F . n 
B 2 145 ALA 145 145 145 ALA ALA F . n 
B 2 146 CYS 146 146 146 CYS CYS F . n 
B 2 147 GLY 147 147 147 GLY GLY F . n 
B 2 148 VAL 148 148 148 VAL VAL F . n 
B 2 149 ILE 149 149 149 ILE ILE F . n 
B 2 150 GLY 150 150 150 GLY GLY F . n 
B 2 151 ILE 151 151 151 ILE ILE F . n 
B 2 152 ALA 152 152 152 ALA ALA F . n 
B 2 153 GLN 153 153 153 GLN GLN F . 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 
C 3 SO4 1   1154 1154 SO4 SO4 A . 
D 4 12I 1   1000 1000 12I 12I A . 
E 3 SO4 1   1156 1156 SO4 SO4 A . 
F 4 12I 1   1001 1001 12I 12I A . 
G 5 CU  1   1157 1157 CU  CU  A . 
H 6 ZN  1   1158 1158 ZN  ZN  A . 
I 7 ACT 1   1159 1159 ACT ACT A . 
J 3 SO4 1   1154 1154 SO4 SO4 F . 
K 3 SO4 1   1155 1155 SO4 SO4 F . 
L 5 CU  1   1156 1156 CU  CU  F . 
M 3 SO4 1   1158 1158 SO4 SO4 F . 
N 6 ZN  1   1157 1157 ZN  ZN  F . 
O 4 12I 1   1000 1000 12I 12I F . 
P 8 HOH 1   2001 2001 HOH HOH A . 
P 8 HOH 2   2002 2002 HOH HOH A . 
P 8 HOH 3   2003 2003 HOH HOH A . 
P 8 HOH 4   2004 2004 HOH HOH A . 
P 8 HOH 5   2005 2005 HOH HOH A . 
P 8 HOH 6   2006 2006 HOH HOH A . 
P 8 HOH 7   2007 2007 HOH HOH A . 
P 8 HOH 8   2008 2008 HOH HOH A . 
P 8 HOH 9   2009 2009 HOH HOH A . 
P 8 HOH 10  2010 2010 HOH HOH A . 
P 8 HOH 11  2011 2011 HOH HOH A . 
P 8 HOH 12  2012 2012 HOH HOH A . 
P 8 HOH 13  2013 2013 HOH HOH A . 
P 8 HOH 14  2014 2014 HOH HOH A . 
P 8 HOH 15  2015 2015 HOH HOH A . 
P 8 HOH 16  2016 2016 HOH HOH A . 
P 8 HOH 17  2017 2017 HOH HOH A . 
P 8 HOH 18  2018 2018 HOH HOH A . 
P 8 HOH 19  2019 2019 HOH HOH A . 
P 8 HOH 20  2020 2020 HOH HOH A . 
P 8 HOH 21  2021 2021 HOH HOH A . 
P 8 HOH 22  2022 2022 HOH HOH A . 
P 8 HOH 23  2023 2023 HOH HOH A . 
P 8 HOH 24  2024 2024 HOH HOH A . 
P 8 HOH 25  2025 2025 HOH HOH A . 
P 8 HOH 26  2026 2026 HOH HOH A . 
P 8 HOH 27  2027 2027 HOH HOH A . 
P 8 HOH 28  2028 2028 HOH HOH A . 
P 8 HOH 29  2029 2029 HOH HOH A . 
P 8 HOH 30  2030 2030 HOH HOH A . 
P 8 HOH 31  2031 2031 HOH HOH A . 
P 8 HOH 32  2032 2032 HOH HOH A . 
P 8 HOH 33  2033 2033 HOH HOH A . 
P 8 HOH 34  2034 2034 HOH HOH A . 
P 8 HOH 35  2035 2035 HOH HOH A . 
P 8 HOH 36  2036 2036 HOH HOH A . 
P 8 HOH 37  2037 2037 HOH HOH A . 
P 8 HOH 38  2038 2038 HOH HOH A . 
P 8 HOH 39  2039 2039 HOH HOH A . 
P 8 HOH 40  2040 2040 HOH HOH A . 
P 8 HOH 41  2041 2041 HOH HOH A . 
P 8 HOH 42  2042 2042 HOH HOH A . 
P 8 HOH 43  2043 2043 HOH HOH A . 
P 8 HOH 44  2044 2044 HOH HOH A . 
P 8 HOH 45  2045 2045 HOH HOH A . 
P 8 HOH 46  2046 2046 HOH HOH A . 
P 8 HOH 47  2047 2047 HOH HOH A . 
P 8 HOH 48  2048 2048 HOH HOH A . 
P 8 HOH 49  2049 2049 HOH HOH A . 
P 8 HOH 50  2050 2050 HOH HOH A . 
P 8 HOH 51  2051 2051 HOH HOH A . 
P 8 HOH 52  2052 2052 HOH HOH A . 
P 8 HOH 53  2053 2053 HOH HOH A . 
P 8 HOH 54  2054 2054 HOH HOH A . 
P 8 HOH 55  2055 2055 HOH HOH A . 
P 8 HOH 56  2056 2056 HOH HOH A . 
P 8 HOH 57  2057 2057 HOH HOH A . 
P 8 HOH 58  2058 2058 HOH HOH A . 
P 8 HOH 59  2059 2059 HOH HOH A . 
P 8 HOH 60  2060 2060 HOH HOH A . 
P 8 HOH 61  2061 2061 HOH HOH A . 
P 8 HOH 62  2062 2062 HOH HOH A . 
P 8 HOH 63  2063 2063 HOH HOH A . 
P 8 HOH 64  2064 2064 HOH HOH A . 
P 8 HOH 65  2065 2065 HOH HOH A . 
P 8 HOH 66  2066 2066 HOH HOH A . 
P 8 HOH 67  2067 2067 HOH HOH A . 
P 8 HOH 68  2068 2068 HOH HOH A . 
P 8 HOH 69  2069 2069 HOH HOH A . 
P 8 HOH 70  2070 2070 HOH HOH A . 
P 8 HOH 71  2071 2071 HOH HOH A . 
P 8 HOH 72  2072 2072 HOH HOH A . 
P 8 HOH 73  2073 2073 HOH HOH A . 
P 8 HOH 74  2074 2074 HOH HOH A . 
P 8 HOH 75  2075 2075 HOH HOH A . 
P 8 HOH 76  2076 2076 HOH HOH A . 
P 8 HOH 77  2077 2077 HOH HOH A . 
P 8 HOH 78  2078 2078 HOH HOH A . 
P 8 HOH 79  2079 2079 HOH HOH A . 
P 8 HOH 80  2080 2080 HOH HOH A . 
P 8 HOH 81  2081 2081 HOH HOH A . 
P 8 HOH 82  2082 2082 HOH HOH A . 
P 8 HOH 83  2083 2083 HOH HOH A . 
P 8 HOH 84  2084 2084 HOH HOH A . 
P 8 HOH 85  2085 2085 HOH HOH A . 
P 8 HOH 86  2086 2086 HOH HOH A . 
P 8 HOH 87  2087 2087 HOH HOH A . 
P 8 HOH 88  2088 2088 HOH HOH A . 
P 8 HOH 89  2089 2089 HOH HOH A . 
P 8 HOH 90  2090 2090 HOH HOH A . 
P 8 HOH 91  2091 2091 HOH HOH A . 
P 8 HOH 92  2092 2092 HOH HOH A . 
P 8 HOH 93  2093 2093 HOH HOH A . 
P 8 HOH 94  2094 2094 HOH HOH A . 
P 8 HOH 95  2095 2095 HOH HOH A . 
P 8 HOH 96  2096 2096 HOH HOH A . 
P 8 HOH 97  2097 2097 HOH HOH A . 
P 8 HOH 98  2098 2098 HOH HOH A . 
P 8 HOH 99  2099 2099 HOH HOH A . 
P 8 HOH 100 2100 2100 HOH HOH A . 
P 8 HOH 101 2101 2101 HOH HOH A . 
P 8 HOH 102 2102 2102 HOH HOH A . 
P 8 HOH 103 2103 2103 HOH HOH A . 
P 8 HOH 104 2104 2104 HOH HOH A . 
P 8 HOH 105 2105 2105 HOH HOH A . 
P 8 HOH 106 2106 2106 HOH HOH A . 
P 8 HOH 107 2107 2107 HOH HOH A . 
P 8 HOH 108 2108 2108 HOH HOH A . 
P 8 HOH 109 2109 2109 HOH HOH A . 
P 8 HOH 110 2110 2110 HOH HOH A . 
P 8 HOH 111 2111 2111 HOH HOH A . 
P 8 HOH 112 2112 2112 HOH HOH A . 
P 8 HOH 113 2113 2113 HOH HOH A . 
P 8 HOH 114 2114 2114 HOH HOH A . 
P 8 HOH 115 2115 2115 HOH HOH A . 
P 8 HOH 116 2116 2116 HOH HOH A . 
P 8 HOH 117 2117 2117 HOH HOH A . 
P 8 HOH 118 2118 2118 HOH HOH A . 
P 8 HOH 119 2119 2119 HOH HOH A . 
P 8 HOH 120 2120 2120 HOH HOH A . 
P 8 HOH 121 2121 2121 HOH HOH A . 
P 8 HOH 122 2122 2122 HOH HOH A . 
P 8 HOH 123 2123 2123 HOH HOH A . 
P 8 HOH 124 2124 2124 HOH HOH A . 
P 8 HOH 125 2125 2125 HOH HOH A . 
P 8 HOH 126 2126 2126 HOH HOH A . 
P 8 HOH 127 2127 2127 HOH HOH A . 
P 8 HOH 128 2128 2128 HOH HOH A . 
P 8 HOH 129 2129 2129 HOH HOH A . 
P 8 HOH 130 2130 2130 HOH HOH A . 
P 8 HOH 131 2131 2131 HOH HOH A . 
P 8 HOH 132 2132 2132 HOH HOH A . 
P 8 HOH 133 2133 2133 HOH HOH A . 
P 8 HOH 134 2134 2134 HOH HOH A . 
P 8 HOH 135 2135 2135 HOH HOH A . 
P 8 HOH 136 2136 2136 HOH HOH A . 
P 8 HOH 137 2137 2137 HOH HOH A . 
P 8 HOH 138 2138 2138 HOH HOH A . 
P 8 HOH 139 2139 2139 HOH HOH A . 
P 8 HOH 140 2140 2140 HOH HOH A . 
P 8 HOH 141 2141 2141 HOH HOH A . 
P 8 HOH 142 2142 2142 HOH HOH A . 
P 8 HOH 143 2143 2143 HOH HOH A . 
P 8 HOH 144 2144 2144 HOH HOH A . 
P 8 HOH 145 2145 2145 HOH HOH A . 
P 8 HOH 146 2146 2146 HOH HOH A . 
P 8 HOH 147 2147 2147 HOH HOH A . 
P 8 HOH 148 2148 2148 HOH HOH A . 
P 8 HOH 149 2149 2149 HOH HOH A . 
P 8 HOH 150 2150 2150 HOH HOH A . 
P 8 HOH 151 2151 2151 HOH HOH A . 
P 8 HOH 152 2152 2152 HOH HOH A . 
P 8 HOH 153 2153 2153 HOH HOH A . 
P 8 HOH 154 2154 2154 HOH HOH A . 
P 8 HOH 155 2155 2155 HOH HOH A . 
P 8 HOH 156 2156 2156 HOH HOH A . 
P 8 HOH 157 2157 2157 HOH HOH A . 
P 8 HOH 158 2158 2158 HOH HOH A . 
P 8 HOH 159 2159 2159 HOH HOH A . 
P 8 HOH 160 2160 2160 HOH HOH A . 
P 8 HOH 161 2161 2161 HOH HOH A . 
P 8 HOH 162 2162 2162 HOH HOH A . 
P 8 HOH 163 2163 2163 HOH HOH A . 
P 8 HOH 164 2165 2165 HOH HOH A . 
P 8 HOH 165 2166 2166 HOH HOH A . 
P 8 HOH 166 2167 2167 HOH HOH A . 
P 8 HOH 167 2168 2168 HOH HOH A . 
P 8 HOH 168 2169 2169 HOH HOH A . 
P 8 HOH 169 2170 2170 HOH HOH A . 
P 8 HOH 170 2171 2171 HOH HOH A . 
P 8 HOH 171 2172 2172 HOH HOH A . 
P 8 HOH 172 2173 2173 HOH HOH A . 
P 8 HOH 173 2174 2174 HOH HOH A . 
P 8 HOH 174 2175 2175 HOH HOH A . 
P 8 HOH 175 2176 2176 HOH HOH A . 
P 8 HOH 176 2177 2177 HOH HOH A . 
P 8 HOH 177 2178 2178 HOH HOH A . 
P 8 HOH 178 2179 2179 HOH HOH A . 
P 8 HOH 179 2180 2180 HOH HOH A . 
P 8 HOH 180 2181 2181 HOH HOH A . 
P 8 HOH 181 2182 2182 HOH HOH A . 
P 8 HOH 182 2183 2183 HOH HOH A . 
P 8 HOH 183 2184 2184 HOH HOH A . 
P 8 HOH 184 2185 2185 HOH HOH A . 
P 8 HOH 185 2186 2186 HOH HOH A . 
P 8 HOH 186 2187 2187 HOH HOH A . 
P 8 HOH 187 2188 2188 HOH HOH A . 
P 8 HOH 188 2189 2189 HOH HOH A . 
P 8 HOH 189 2190 2190 HOH HOH A . 
P 8 HOH 190 2191 2191 HOH HOH A . 
P 8 HOH 191 2192 2192 HOH HOH A . 
P 8 HOH 192 2193 2193 HOH HOH A . 
P 8 HOH 193 2194 2194 HOH HOH A . 
P 8 HOH 194 2195 2195 HOH HOH A . 
P 8 HOH 195 2196 2196 HOH HOH A . 
P 8 HOH 196 2197 2197 HOH HOH A . 
P 8 HOH 197 2198 2198 HOH HOH A . 
P 8 HOH 198 2199 2199 HOH HOH A . 
P 8 HOH 199 2200 2200 HOH HOH A . 
P 8 HOH 200 2201 2201 HOH HOH A . 
P 8 HOH 201 2202 2202 HOH HOH A . 
P 8 HOH 202 2203 2203 HOH HOH A . 
P 8 HOH 203 2204 2204 HOH HOH A . 
P 8 HOH 204 2205 2205 HOH HOH A . 
P 8 HOH 205 2206 2206 HOH HOH A . 
P 8 HOH 206 2207 2207 HOH HOH A . 
P 8 HOH 207 2208 2208 HOH HOH A . 
P 8 HOH 208 2209 2209 HOH HOH A . 
P 8 HOH 209 2210 2210 HOH HOH A . 
P 8 HOH 210 2211 2211 HOH HOH A . 
P 8 HOH 211 2212 2212 HOH HOH A . 
P 8 HOH 212 2213 2213 HOH HOH A . 
P 8 HOH 213 2214 2214 HOH HOH A . 
Q 8 HOH 1   2001 2001 HOH HOH F . 
Q 8 HOH 2   2002 2002 HOH HOH F . 
Q 8 HOH 3   2003 2003 HOH HOH F . 
Q 8 HOH 4   2004 2004 HOH HOH F . 
Q 8 HOH 5   2005 2005 HOH HOH F . 
Q 8 HOH 6   2006 2006 HOH HOH F . 
Q 8 HOH 7   2007 2007 HOH HOH F . 
Q 8 HOH 8   2008 2008 HOH HOH F . 
Q 8 HOH 9   2009 2009 HOH HOH F . 
Q 8 HOH 10  2010 2010 HOH HOH F . 
Q 8 HOH 11  2011 2011 HOH HOH F . 
Q 8 HOH 12  2012 2012 HOH HOH F . 
Q 8 HOH 13  2013 2013 HOH HOH F . 
Q 8 HOH 14  2014 2014 HOH HOH F . 
Q 8 HOH 15  2015 2015 HOH HOH F . 
Q 8 HOH 16  2016 2016 HOH HOH F . 
Q 8 HOH 17  2017 2017 HOH HOH F . 
Q 8 HOH 18  2018 2018 HOH HOH F . 
Q 8 HOH 19  2019 2019 HOH HOH F . 
Q 8 HOH 20  2020 2020 HOH HOH F . 
Q 8 HOH 21  2021 2021 HOH HOH F . 
Q 8 HOH 22  2022 2022 HOH HOH F . 
Q 8 HOH 23  2023 2023 HOH HOH F . 
Q 8 HOH 24  2024 2024 HOH HOH F . 
Q 8 HOH 25  2025 2025 HOH HOH F . 
Q 8 HOH 26  2026 2026 HOH HOH F . 
Q 8 HOH 27  2027 2027 HOH HOH F . 
Q 8 HOH 28  2028 2028 HOH HOH F . 
Q 8 HOH 29  2029 2029 HOH HOH F . 
Q 8 HOH 30  2030 2030 HOH HOH F . 
Q 8 HOH 31  2031 2031 HOH HOH F . 
Q 8 HOH 32  2032 2032 HOH HOH F . 
Q 8 HOH 33  2033 2033 HOH HOH F . 
Q 8 HOH 34  2034 2034 HOH HOH F . 
Q 8 HOH 35  2035 2035 HOH HOH F . 
Q 8 HOH 36  2036 2036 HOH HOH F . 
Q 8 HOH 37  2037 2037 HOH HOH F . 
Q 8 HOH 38  2038 2038 HOH HOH F . 
Q 8 HOH 39  2039 2039 HOH HOH F . 
Q 8 HOH 40  2040 2040 HOH HOH F . 
Q 8 HOH 41  2041 2041 HOH HOH F . 
Q 8 HOH 42  2042 2042 HOH HOH F . 
Q 8 HOH 43  2043 2043 HOH HOH F . 
Q 8 HOH 44  2044 2044 HOH HOH F . 
Q 8 HOH 45  2045 2045 HOH HOH F . 
Q 8 HOH 46  2046 2046 HOH HOH F . 
Q 8 HOH 47  2047 2047 HOH HOH F . 
Q 8 HOH 48  2048 2048 HOH HOH F . 
Q 8 HOH 49  2049 2049 HOH HOH F . 
Q 8 HOH 50  2050 2050 HOH HOH F . 
Q 8 HOH 51  2051 2051 HOH HOH F . 
Q 8 HOH 52  2052 2052 HOH HOH F . 
Q 8 HOH 53  2053 2053 HOH HOH F . 
Q 8 HOH 54  2054 2054 HOH HOH F . 
Q 8 HOH 55  2055 2055 HOH HOH F . 
Q 8 HOH 56  2056 2056 HOH HOH F . 
Q 8 HOH 57  2057 2057 HOH HOH F . 
Q 8 HOH 58  2058 2058 HOH HOH F . 
Q 8 HOH 59  2059 2059 HOH HOH F . 
Q 8 HOH 60  2060 2060 HOH HOH F . 
Q 8 HOH 61  2061 2061 HOH HOH F . 
Q 8 HOH 62  2062 2062 HOH HOH F . 
Q 8 HOH 63  2063 2063 HOH HOH F . 
Q 8 HOH 64  2064 2064 HOH HOH F . 
Q 8 HOH 65  2065 2065 HOH HOH F . 
Q 8 HOH 66  2066 2066 HOH HOH F . 
Q 8 HOH 67  2067 2067 HOH HOH F . 
Q 8 HOH 68  2068 2068 HOH HOH F . 
Q 8 HOH 69  2069 2069 HOH HOH F . 
Q 8 HOH 70  2070 2070 HOH HOH F . 
Q 8 HOH 71  2071 2071 HOH HOH F . 
Q 8 HOH 72  2072 2072 HOH HOH F . 
Q 8 HOH 73  2073 2073 HOH HOH F . 
Q 8 HOH 74  2074 2074 HOH HOH F . 
Q 8 HOH 75  2075 2075 HOH HOH F . 
Q 8 HOH 76  2076 2076 HOH HOH F . 
Q 8 HOH 77  2077 2077 HOH HOH F . 
Q 8 HOH 78  2078 2078 HOH HOH F . 
Q 8 HOH 79  2079 2079 HOH HOH F . 
Q 8 HOH 80  2080 2080 HOH HOH F . 
Q 8 HOH 81  2081 2081 HOH HOH F . 
Q 8 HOH 82  2083 2083 HOH HOH F . 
Q 8 HOH 83  2084 2084 HOH HOH F . 
Q 8 HOH 84  2085 2085 HOH HOH F . 
Q 8 HOH 85  2086 2086 HOH HOH F . 
Q 8 HOH 86  2087 2087 HOH HOH F . 
Q 8 HOH 87  2088 2088 HOH HOH F . 
Q 8 HOH 88  2089 2089 HOH HOH F . 
Q 8 HOH 89  2090 2090 HOH HOH F . 
Q 8 HOH 90  2091 2091 HOH HOH F . 
Q 8 HOH 91  2092 2092 HOH HOH F . 
Q 8 HOH 92  2093 2093 HOH HOH F . 
Q 8 HOH 93  2094 2094 HOH HOH F . 
Q 8 HOH 94  2095 2095 HOH HOH F . 
Q 8 HOH 95  2096 2096 HOH HOH F . 
Q 8 HOH 96  2097 2097 HOH HOH F . 
Q 8 HOH 97  2098 2098 HOH HOH F . 
Q 8 HOH 98  2099 2099 HOH HOH F . 
Q 8 HOH 99  2100 2100 HOH HOH F . 
Q 8 HOH 100 2101 2101 HOH HOH F . 
Q 8 HOH 101 2102 2102 HOH HOH F . 
Q 8 HOH 102 2103 2103 HOH HOH F . 
Q 8 HOH 103 2104 2104 HOH HOH F . 
Q 8 HOH 104 2105 2105 HOH HOH F . 
Q 8 HOH 105 2106 2106 HOH HOH F . 
Q 8 HOH 106 2107 2107 HOH HOH F . 
Q 8 HOH 107 2108 2108 HOH HOH F . 
Q 8 HOH 108 2109 2109 HOH HOH F . 
Q 8 HOH 109 2110 2110 HOH HOH F . 
Q 8 HOH 110 2111 2111 HOH HOH F . 
Q 8 HOH 111 2112 2112 HOH HOH F . 
Q 8 HOH 112 2113 2113 HOH HOH F . 
Q 8 HOH 113 2114 2114 HOH HOH F . 
Q 8 HOH 114 2115 2115 HOH HOH F . 
Q 8 HOH 115 2116 2116 HOH HOH F . 
Q 8 HOH 116 2117 2117 HOH HOH F . 
Q 8 HOH 117 2118 2118 HOH HOH F . 
Q 8 HOH 118 2119 2119 HOH HOH F . 
Q 8 HOH 119 2120 2120 HOH HOH F . 
Q 8 HOH 120 2122 2122 HOH HOH F . 
Q 8 HOH 121 2123 2123 HOH HOH F . 
Q 8 HOH 122 2124 2124 HOH HOH F . 
Q 8 HOH 123 2125 2125 HOH HOH F . 
Q 8 HOH 124 2126 2126 HOH HOH F . 
Q 8 HOH 125 2127 2127 HOH HOH F . 
Q 8 HOH 126 2128 2128 HOH HOH F . 
Q 8 HOH 127 2129 2129 HOH HOH F . 
Q 8 HOH 128 2130 2130 HOH HOH F . 
Q 8 HOH 129 2131 2131 HOH HOH F . 
Q 8 HOH 130 2132 2132 HOH HOH F . 
Q 8 HOH 131 2133 2133 HOH HOH F . 
Q 8 HOH 132 2134 2134 HOH HOH F . 
Q 8 HOH 133 2135 2135 HOH HOH F . 
Q 8 HOH 134 2136 2136 HOH HOH F . 
Q 8 HOH 135 2137 2137 HOH HOH F . 
Q 8 HOH 136 2138 2138 HOH HOH F . 
Q 8 HOH 137 2139 2139 HOH HOH F . 
Q 8 HOH 138 2140 2140 HOH HOH F . 
Q 8 HOH 139 2141 2141 HOH HOH F . 
Q 8 HOH 140 2142 2142 HOH HOH F . 
Q 8 HOH 141 2143 2143 HOH HOH F . 
Q 8 HOH 142 2144 2144 HOH HOH F . 
Q 8 HOH 143 2145 2145 HOH HOH F . 
Q 8 HOH 144 2146 2146 HOH HOH F . 
Q 8 HOH 145 2147 2147 HOH HOH F . 
Q 8 HOH 146 2148 2148 HOH HOH F . 
Q 8 HOH 147 2149 2149 HOH HOH F . 
Q 8 HOH 148 2150 2150 HOH HOH F . 
Q 8 HOH 149 2151 2151 HOH HOH F . 
Q 8 HOH 150 2152 2152 HOH HOH F . 
Q 8 HOH 151 2153 2153 HOH HOH F . 
Q 8 HOH 152 2154 2154 HOH HOH F . 
Q 8 HOH 153 2155 2155 HOH HOH F . 
Q 8 HOH 154 2156 2156 HOH HOH F . 
Q 8 HOH 155 2157 2157 HOH HOH F . 
Q 8 HOH 156 2158 2158 HOH HOH F . 
Q 8 HOH 157 2159 2159 HOH HOH F . 
Q 8 HOH 158 2160 2160 HOH HOH F . 
Q 8 HOH 159 2161 2161 HOH HOH F . 
Q 8 HOH 160 2162 2162 HOH HOH F . 
Q 8 HOH 161 2163 2163 HOH HOH F . 
Q 8 HOH 162 2164 2164 HOH HOH F . 
Q 8 HOH 163 2165 2165 HOH HOH F . 
Q 8 HOH 164 2166 2166 HOH HOH F . 
Q 8 HOH 165 2167 2167 HOH HOH F . 
Q 8 HOH 166 2168 2168 HOH HOH F . 
Q 8 HOH 167 2169 2169 HOH HOH F . 
Q 8 HOH 168 2170 2170 HOH HOH F . 
Q 8 HOH 169 2171 2171 HOH HOH F . 
Q 8 HOH 170 2172 2172 HOH HOH F . 
Q 8 HOH 171 2173 2173 HOH HOH F . 
Q 8 HOH 172 2174 2174 HOH HOH F . 
Q 8 HOH 173 2175 2175 HOH HOH F . 
Q 8 HOH 174 2176 2176 HOH HOH F . 
Q 8 HOH 175 2177 2177 HOH HOH F . 
# 
_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   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2480  ? 
1 MORE         -86.8 ? 
1 'SSA (A^2)'  14190 ? 
# 
_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  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 CU ? G CU . ? A CU 1157 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 111.4 ? 
2  NE2 ? A HIS 48  ? A HIS 48  ? 1_555 CU ? G CU . ? A CU 1157 ? 1_555 ND1 ? A HIS 46  ? A HIS 46  ? 1_555 146.4 ? 
3  NE2 ? A HIS 120 ? A HIS 120 ? 1_555 CU ? G CU . ? A CU 1157 ? 1_555 ND1 ? A HIS 46  ? A HIS 46  ? 1_555 101.7 ? 
4  OD1 ? A ASP 83  ? A ASP 83  ? 1_555 ZN ? H ZN . ? A ZN 1158 ? 1_555 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 98.6  ? 
5  OD1 ? A ASP 83  ? A ASP 83  ? 1_555 ZN ? H ZN . ? A ZN 1158 ? 1_555 ND1 ? A HIS 63  ? A HIS 63  ? 1_555 102.6 ? 
6  ND1 ? A HIS 71  ? A HIS 71  ? 1_555 ZN ? H ZN . ? A ZN 1158 ? 1_555 ND1 ? A HIS 63  ? A HIS 63  ? 1_555 104.6 ? 
7  OD1 ? A ASP 83  ? A ASP 83  ? 1_555 ZN ? H ZN . ? A ZN 1158 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 115.2 ? 
8  ND1 ? A HIS 71  ? A HIS 71  ? 1_555 ZN ? H ZN . ? A ZN 1158 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 121.9 ? 
9  ND1 ? A HIS 63  ? A HIS 63  ? 1_555 ZN ? H ZN . ? A ZN 1158 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 111.5 ? 
10 NE2 ? B HIS 120 ? F HIS 120 ? 1_555 CU A L CU . ? F CU 1156 ? 1_555 NE2 ? B HIS 48  ? F HIS 48  ? 1_555 108.9 ? 
11 NE2 ? B HIS 120 ? F HIS 120 ? 1_555 CU A L CU . ? F CU 1156 ? 1_555 ND1 ? B HIS 46  ? F HIS 46  ? 1_555 102.5 ? 
12 NE2 ? B HIS 48  ? F HIS 48  ? 1_555 CU A L CU . ? F CU 1156 ? 1_555 ND1 ? B HIS 46  ? F HIS 46  ? 1_555 147.7 ? 
13 ND1 ? B HIS 46  ? F HIS 46  ? 1_555 CU B L CU . ? F CU 1156 ? 1_555 NE2 ? B HIS 48  ? F HIS 48  ? 1_555 123.0 ? 
14 ND1 ? B HIS 46  ? F HIS 46  ? 1_555 CU B L CU . ? F CU 1156 ? 1_555 NE2 ? B HIS 120 ? F HIS 120 ? 1_555 93.5  ? 
15 NE2 ? B HIS 48  ? F HIS 48  ? 1_555 CU B L CU . ? F CU 1156 ? 1_555 NE2 ? B HIS 120 ? F HIS 120 ? 1_555 125.4 ? 
16 OD1 ? B ASP 83  ? F ASP 83  ? 1_555 ZN ? N ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 80  ? F HIS 80  ? 1_555 116.1 ? 
17 OD1 ? B ASP 83  ? F ASP 83  ? 1_555 ZN ? N ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 71  ? F HIS 71  ? 1_555 98.9  ? 
18 ND1 ? B HIS 80  ? F HIS 80  ? 1_555 ZN ? N ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 71  ? F HIS 71  ? 1_555 122.0 ? 
19 OD1 ? B ASP 83  ? F ASP 83  ? 1_555 ZN ? N ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 63  ? F HIS 63  ? 1_555 104.3 ? 
20 ND1 ? B HIS 80  ? F HIS 80  ? 1_555 ZN ? N ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 63  ? F HIS 63  ? 1_555 109.8 ? 
21 ND1 ? B HIS 71  ? F HIS 71  ? 1_555 ZN ? N ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 63  ? F HIS 63  ? 1_555 103.7 ? 
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
1 'Structure model' 1 0 2012-10-24 
2 'Structure model' 1 1 2013-03-13 
3 'Structure model' 1 2 2013-08-28 
4 'Structure model' 1 3 2018-11-14 
5 'Structure model' 1 4 2018-11-21 
6 'Structure model' 1 5 2019-10-09 
# 
_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' 'Database references' 
2 3 'Structure model' 'Database references' 
3 4 'Structure model' 'Data collection'     
4 4 'Structure model' 'Database references' 
5 5 'Structure model' 'Data collection'     
6 5 'Structure model' 'Source and taxonomy' 
7 6 'Structure model' 'Data collection'     
8 6 'Structure model' 'Database references' 
9 6 'Structure model' Other                 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 4 'Structure model' citation             
2 5 'Structure model' entity_src_gen       
3 6 'Structure model' citation             
4 6 'Structure model' pdbx_database_status 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1  4 'Structure model' '_citation.journal_abbrev'                      
2  4 'Structure model' '_citation.journal_id_ISSN'                     
3  4 'Structure model' '_citation.page_last'                           
4  4 'Structure model' '_citation.pdbx_database_id_DOI'                
5  4 'Structure model' '_citation.title'                               
6  5 'Structure model' '_entity_src_gen.pdbx_host_org_scientific_name' 
7  5 'Structure model' '_entity_src_gen.pdbx_host_org_strain'          
8  6 'Structure model' '_citation.journal_abbrev'                      
9  6 'Structure model' '_citation.journal_id_ISSN'                     
10 6 'Structure model' '_citation.pdbx_database_id_DOI'                
11 6 'Structure model' '_pdbx_database_status.status_code_sf'          
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC   refinement       5.5.0102 ? 1 
HKL-2000 'data reduction' .        ? 2 
HKL-2000 'data scaling'   .        ? 3 
REFMAC   phasing          .        ? 4 
# 
_pdbx_entry_details.entry_id             4A7G 
_pdbx_entry_details.compound_details     
;ENGINEERED RESIDUE IN CHAIN A, ILE 114 TO THR
ENGINEERED RESIDUE IN CHAIN F, ILE 114 TO THR
;
_pdbx_entry_details.source_details       ? 
_pdbx_entry_details.nonpolymer_details   ? 
_pdbx_entry_details.sequence_details     ? 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 OD1 F ASN 53   ? A O   F HOH 2066 ? ? 1.53 
2 1 OD1 F ASP 90   ? ? OD1 F ASP 92   ? ? 1.65 
3 1 OG1 A THR 135  ? ? O   A HOH 2188 ? ? 1.80 
4 1 O3  F SO4 1158 ? ? O   F HOH 2076 ? ? 1.84 
5 1 O   F HOH 2114 ? ? O   F HOH 2115 ? ? 1.93 
6 1 ND1 A HIS 110  ? ? O   A HOH 2156 ? ? 1.98 
7 1 ND2 F ASN 53   ? A O   F HOH 2070 ? ? 2.05 
8 1 OE2 A GLU 100  ? ? O   A HOH 2154 ? ? 2.15 
9 1 OE2 A GLU 133  ? ? O   A HOH 2192 ? ? 2.16 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O   A HOH 2085 ? ? 1_555 O F HOH 2081 ? ? 2_546 1.95 
2 1 OE2 A GLU 40   ? ? 1_555 O F HOH 2081 ? ? 2_546 1.99 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CB 
_pdbx_validate_rmsd_angle.auth_asym_id_1             F 
_pdbx_validate_rmsd_angle.auth_comp_id_1             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_1              109 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_2             F 
_pdbx_validate_rmsd_angle.auth_comp_id_2             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_2              109 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             OD2 
_pdbx_validate_rmsd_angle.auth_asym_id_3             F 
_pdbx_validate_rmsd_angle.auth_comp_id_3             ASP 
_pdbx_validate_rmsd_angle.auth_seq_id_3              109 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                125.19 
_pdbx_validate_rmsd_angle.angle_target_value         118.30 
_pdbx_validate_rmsd_angle.angle_deviation            6.89 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.90 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    PRO 
_pdbx_validate_torsion.auth_asym_id    F 
_pdbx_validate_torsion.auth_seq_id     13 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    B 
_pdbx_validate_torsion.phi             -103.42 
_pdbx_validate_torsion.psi             49.51 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_1   F 
_pdbx_validate_peptide_omega.auth_seq_id_1    12 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   B 
_pdbx_validate_peptide_omega.auth_comp_id_2   PRO 
_pdbx_validate_peptide_omega.auth_asym_id_2   F 
_pdbx_validate_peptide_omega.auth_seq_id_2    13 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   B 
_pdbx_validate_peptide_omega.omega            -30.87 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'SULFATE ION'                           SO4 
4 '4-(4-METHYLPIPERAZIN-1-YL)QUINAZOLINE' 12I 
5 'COPPER (II) ION'                       CU  
6 'ZINC ION'                              ZN  
7 'ACETATE ION'                           ACT 
8 water                                   HOH 
# 
