data_4A7U
# 
_entry.id   4A7U 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.279 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4A7U         
PDBE  EBI-50328    
WWPDB D_1290050328 
# 
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 4A7Q unspecified 
'STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 4 -(4-METHYL-1,4-DIAZEPAN-1-YL)QUINAZOLINE IN THE P21 SPACE GROUP.' 
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 4A7R unspecified 
;STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 4 -(4-METHYL-1,4-DIAZEPAN-1-YL)-2-(TRIFLUOROMETHYL) QUINAZOLINE IN THE P21 SPACE GROUP
;
PDB 4A7S unspecified 'STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 5 -FLUOROURIDINE IN THE P21 SPACE GROUP' 
PDB 2WZ5 unspecified 'L38V SOD1 MUTANT COMPLEXED WITH L-METHIONINE.' 
PDB 2XJL unspecified 'MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE WITHOUT CU LIGANDS' 
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 1PU0 unspecified 'STRUCTURE OF HUMAN CU,ZN SUPEROXIDE DISMUTASE' 
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 4A7V unspecified 'STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH DOPAMINE IN THE P21 SPACE GROUP' 
PDB 1RK7 unspecified 'SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE DISMUTASE: ROLEOF METAL IONS IN PROTEIN FOLDING' 
PDB 2VR7 unspecified 'CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.58 A RESOLUTION' 
PDB 2C9S unspecified '1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN-ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 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 2V0A unspecified 'ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN SUPEROXIDE DISMUTASE' 
PDB 4A7T unspecified 'STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH ISOPROTERANOL IN THE P21 SPACE GROUP' 
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 4A7G unspecified 
'STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 4 -METHYLPIPERAZIN-1-YL)QUINAZOLINE IN THE P21 SPACE GROUP.' 
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 1UXM unspecified 'A4V MUTANT OF HUMAN SOD1' 
PDB 1SPD unspecified 'SUPEROXIDE DISMUTASE' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4A7U 
_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                  ? 
_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 
'Antonyuk, S.V.' 3 
'Strange, R.W.'  4 
'ONeil, P.M.'    5 
'Hasnain, S.S.'  6 
# 
_citation.id                        primary 
_citation.title                     'Ligand Binding and Aggregation of Pathogenic Sod1.' 
_citation.journal_abbrev            Nat.Commun. 
_citation.journal_volume            4 
_citation.page_first                1758 
_citation.page_last                 ? 
_citation.year                      2013 
_citation.journal_id_ASTM           ? 
_citation.country                   UK 
_citation.journal_id_ISSN           2041-1723 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   23612299 
_citation.pdbx_database_id_DOI      10.1038/NCOMMS2750 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
primary 'Wright, G.S.A.' 1 
primary 'Antonyuk, S.V.' 2 
primary 'Kershaw, N.M.'  3 
primary 'Strange, R.W.'  4 
primary 'Hasnain, S.S.'  5 
# 
_cell.entry_id           4A7U 
_cell.length_a           38.300 
_cell.length_b           68.100 
_cell.length_c           50.200 
_cell.angle_alpha        90.00 
_cell.angle_beta         104.70 
_cell.angle_gamma        90.00 
_cell.Z_PDB              4 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         4A7U 
_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]' 15815.508 2   1.15.1.1 YES ? ? 
2 non-polymer syn L-EPINEPHRINE                  183.204   2   ?        ?   ? ? 
3 non-polymer syn 'SULFATE ION'                  96.063    4   ?        ?   ? ? 
4 non-polymer syn 'COPPER (II) ION'              63.546    2   ?        ?   ? ? 
5 non-polymer syn 'ZINC ION'                     65.409    2   ?        ?   ? ? 
6 non-polymer syn 'ACETATE ION'                  59.044    1   ?        ?   ? ? 
7 water       nat water                          18.015    283 ?        ?   ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'SUPEROXIDE DISMUTASE-1, SUPEROXIDE DISMUTASE 1, HSOD1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCITGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVCVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHEFGDNTAGCTSAGPHFNPLSRKHGGPKDEERH
VGDLGNVTADKDGVADVSIEDSVISLSGDHCITGRTLVVHEKADDLGKGGNEESTKTGNAGSRLACGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,F 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   THR n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   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  ILE n 
1 100 GLU n 
1 101 ASP n 
1 102 SER n 
1 103 VAL n 
1 104 ILE n 
1 105 SER n 
1 106 LEU n 
1 107 SER n 
1 108 GLY n 
1 109 ASP n 
1 110 HIS n 
1 111 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 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               HUMAN 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'HOMO SAPIENS' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'ESCHERICHIA COLI' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          PLASMID 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       PET303 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.pdbx_db_isoform            ? 
# 
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 4A7U A 1 ? 153 ? P00441 2 ? 154 ? 1 153 
2 1 4A7U 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 4A7U THR A 113 ? UNP P00441 ILE 114 'engineered mutation' 113 1 
2 4A7U THR F 113 ? UNP P00441 ILE 114 'engineered mutation' 113 2 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ACT non-polymer         . 'ACETATE ION'     ?          'C2 H3 O2 -1'    59.044  
ALA 'L-peptide linking' y ALANINE           ?          'C3 H7 N O2'     89.093  
ALE non-polymer         . L-EPINEPHRINE     ADRENALINE 'C9 H13 N O3'    183.204 
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          4A7U 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      1.84 
_exptl_crystal.density_percent_sol   33.17 
_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    '100 MM SODIUM ACETATE, 150 MM SODIUM CHLORIDE, 2.5 AMMONIUM SULPHATE PH 5' 
# 
_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 CCD' 
_diffrn_detector.pdbx_collection_date   2010-05-10 
_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   0.98 
_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             0.98 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     4A7U 
_reflns.observed_criterion_sigma_I   0.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             37.00 
_reflns.d_resolution_high            0.90 
_reflns.number_obs                   154810 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         84.3 
_reflns.pdbx_Rmerge_I_obs            0.04 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        14.70 
_reflns.B_iso_Wilson_estimate        14.1 
_reflns.pdbx_redundancy              3.6 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             0.90 
_reflns_shell.d_res_low              0.92 
_reflns_shell.percent_possible_all   25.3 
_reflns_shell.Rmerge_I_obs           0.57 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    1.60 
_reflns_shell.pdbx_redundancy        2.0 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4A7U 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     131250 
_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                             37.05 
_refine.ls_d_res_high                            0.98 
_refine.ls_percent_reflns_obs                    96.99 
_refine.ls_R_factor_obs                          0.13881 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.13803 
_refine.ls_R_factor_R_free                       0.15349 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_percent_reflns_R_free                 5.0 
_refine.ls_number_reflns_R_free                  6908 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               0.979 
_refine.correlation_coeff_Fo_to_Fc_free          0.973 
_refine.B_iso_mean                               13.466 
_refine.aniso_B[1][1]                            -0.20 
_refine.aniso_B[2][2]                            0.41 
_refine.aniso_B[3][3]                            -0.36 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -0.31 
_refine.aniso_B[2][3]                            0.00 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_ksol                 ? 
_refine.solvent_model_param_bsol                 ? 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS. 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                       0.022 
_refine.pdbx_overall_ESU_R_Free                  0.022 
_refine.overall_SU_ML                            0.013 
_refine.pdbx_overall_phase_error                 ? 
_refine.overall_SU_B                             0.531 
_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        2218 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         54 
_refine_hist.number_atoms_solvent             283 
_refine_hist.number_atoms_total               2555 
_refine_hist.d_res_high                       0.98 
_refine_hist.d_res_low                        37.05 
# 
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  0.019  ? 2435 'X-RAY DIFFRACTION' ? 
r_bond_other_d               0.003  0.020  ? 1587 'X-RAY DIFFRACTION' ? 
r_angle_refined_deg          1.711  1.964  ? 3308 'X-RAY DIFFRACTION' ? 
r_angle_other_deg            1.053  3.005  ? 3912 'X-RAY DIFFRACTION' ? 
r_dihedral_angle_1_deg       7.744  5.000  ? 331  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_2_deg       36.330 26.000 ? 105  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_3_deg       11.694 15.000 ? 388  'X-RAY DIFFRACTION' ? 
r_dihedral_angle_4_deg       11.116 15.000 ? 8    'X-RAY DIFFRACTION' ? 
r_chiral_restr               0.096  0.200  ? 360  'X-RAY DIFFRACTION' ? 
r_gen_planes_refined         0.008  0.020  ? 2854 'X-RAY DIFFRACTION' ? 
r_gen_planes_other           0.002  0.020  ? 442  '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                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_it                 ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_mcangle_other              ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_it                  ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scbond_other               ?      ?      ? ?    'X-RAY DIFFRACTION' ? 
r_scangle_it                 ?      ?      ? ?    '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           3.472  3.000  ? 4022 'X-RAY DIFFRACTION' ? 
r_sphericity_free            26.336 5.000  ? 54   'X-RAY DIFFRACTION' ? 
r_sphericity_bonded          9.907  5.000  ? 4210 '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                       0.980 
_refine_ls_shell.d_res_low                        1.005 
_refine_ls_shell.number_reflns_R_work             7078 
_refine_ls_shell.R_factor_R_work                  0.212 
_refine_ls_shell.percent_reflns_obs               71.66 
_refine_ls_shell.R_factor_R_free                  0.200 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.number_reflns_R_free             375 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.R_factor_all                     ? 
# 
_struct.entry_id                  4A7U 
_struct.title                     'Structure of human I113T SOD1 complexed with adrenaline 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        4A7U 
_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 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 3 ? 
J N N 3 ? 
K N N 3 ? 
L N N 4 ? 
M N N 5 ? 
N N N 7 ? 
O N N 7 ? 
# 
_struct_biol.id   1 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 1 GLY A 56  ? GLY A 61  ? GLY A 56  GLY A 61  5 ? 6 
HELX_P HELX_P2 2 SER A 107 ? HIS A 110 ? SER A 107 HIS A 110 5 ? 4 
HELX_P HELX_P3 3 ASN A 131 ? LYS A 136 ? ASN A 131 LYS A 136 5 ? 6 
HELX_P HELX_P4 4 GLY B 56  ? GLY B 61  ? GLY F 56  GLY F 61  5 ? 6 
HELX_P HELX_P5 5 GLU B 133 ? GLY B 138 ? GLU F 133 GLY F 138 1 ? 6 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
disulf1  disulf ? ? A CYS 57 SG ? ? ? 1_555 A CYS 146 SG  ? ? A CYS 57   A CYS 146 1_555 ? ? ? ? ? ? ? 2.097 ? 
disulf2  disulf ? ? B CYS 57 SG ? ? ? 1_555 B CYS 146 SG  ? ? F CYS 57   F CYS 146 1_555 ? ? ? ? ? ? ? 2.075 ? 
metalc1  metalc ? ? F CU  .  CU ? ? ? 1_555 A HIS 46  ND1 ? ? A CU  1157 A HIS 46  1_555 ? ? ? ? ? ? ? 2.061 ? 
metalc2  metalc ? ? F CU  .  CU ? ? ? 1_555 A HIS 48  NE2 ? ? A CU  1157 A HIS 48  1_555 ? ? ? ? ? ? ? 1.886 ? 
metalc3  metalc ? ? F CU  .  CU ? ? ? 1_555 A HIS 120 NE2 ? ? A CU  1157 A HIS 120 1_555 ? ? ? ? ? ? ? 1.927 ? 
metalc4  metalc ? ? G ZN  .  ZN ? ? ? 1_555 A ASP 83  OD1 ? ? A ZN  1158 A ASP 83  1_555 ? ? ? ? ? ? ? 1.961 ? 
metalc5  metalc ? ? G ZN  .  ZN ? ? ? 1_555 A HIS 80  ND1 ? ? A ZN  1158 A HIS 80  1_555 ? ? ? ? ? ? ? 2.022 ? 
metalc6  metalc ? ? G ZN  .  ZN ? ? ? 1_555 A HIS 63  ND1 ? ? A ZN  1158 A HIS 63  1_555 ? ? ? ? ? ? ? 2.000 ? 
metalc7  metalc ? ? G ZN  .  ZN ? ? ? 1_555 A HIS 71  ND1 ? ? A ZN  1158 A HIS 71  1_555 ? ? ? ? ? ? ? 2.027 ? 
metalc8  metalc ? ? L CU  .  CU ? ? ? 1_555 B HIS 46  ND1 ? ? F CU  1156 F HIS 46  1_555 ? ? ? ? ? ? ? 2.095 ? 
metalc9  metalc ? ? L CU  .  CU ? ? ? 1_555 B HIS 48  NE2 ? ? F CU  1156 F HIS 48  1_555 ? ? ? ? ? ? ? 1.866 ? 
metalc10 metalc ? ? L CU  .  CU ? ? ? 1_555 B HIS 120 NE2 ? ? F CU  1156 F HIS 120 1_555 ? ? ? ? ? ? ? 1.928 ? 
metalc11 metalc ? ? M ZN  .  ZN ? ? ? 1_555 B ASP 83  OD1 ? ? F ZN  1157 F ASP 83  1_555 ? ? ? ? ? ? ? 1.952 ? 
metalc12 metalc ? ? M ZN  .  ZN ? ? ? 1_555 B HIS 80  ND1 ? ? F ZN  1157 F HIS 80  1_555 ? ? ? ? ? ? ? 2.000 ? 
metalc13 metalc ? ? M ZN  .  ZN ? ? ? 1_555 B HIS 71  ND1 ? ? F ZN  1157 F HIS 71  1_555 ? ? ? ? ? ? ? 2.031 ? 
metalc14 metalc ? ? M ZN  .  ZN ? ? ? 1_555 B HIS 63  ND1 ? ? F ZN  1157 F HIS 63  1_555 ? ? ? ? ? ? ? 2.011 ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
disulf ? ? 
metalc ? ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 GLY 12 B . ? GLY 12 F PRO 13 B ? PRO 13 F 1 1.94  
2 GLY 12 B . ? GLY 12 F PRO 13 B ? PRO 13 F 1 -6.32 
# 
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 ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU A 1157'  
AC2 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN A 1158'  
AC3 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE SO4 F 1154' 
AC4 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE SO4 A 1154' 
AC5 Software ? ? ? ? 8 'BINDING SITE FOR RESIDUE ALE A 1000' 
AC6 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE CU F 1156'  
AC7 Software ? ? ? ? 4 'BINDING SITE FOR RESIDUE ZN F 1157'  
AC8 Software ? ? ? ? 7 'BINDING SITE FOR RESIDUE ALE A 1001' 
AC9 Software ? ? ? ? 6 'BINDING SITE FOR RESIDUE ACT A 1159' 
BC1 Software ? ? ? ? 5 'BINDING SITE FOR RESIDUE SO4 A 1160' 
BC2 Software ? ? ? ? 3 'BINDING SITE FOR RESIDUE SO4 F 1155' 
# 
loop_
_struct_site_gen.id 
_struct_site_gen.site_id 
_struct_site_gen.pdbx_num_res 
_struct_site_gen.label_comp_id 
_struct_site_gen.label_asym_id 
_struct_site_gen.label_seq_id 
_struct_site_gen.pdbx_auth_ins_code 
_struct_site_gen.auth_comp_id 
_struct_site_gen.auth_asym_id 
_struct_site_gen.auth_seq_id 
_struct_site_gen.label_atom_id 
_struct_site_gen.label_alt_id 
_struct_site_gen.symmetry 
_struct_site_gen.details 
1  AC1 4 HIS A 46  ? HIS A 46   . ? 1_555 ? 
2  AC1 4 HIS A 48  ? HIS A 48   . ? 1_555 ? 
3  AC1 4 HIS A 63  ? HIS A 63   . ? 1_555 ? 
4  AC1 4 HIS A 120 ? HIS A 120  . ? 1_555 ? 
5  AC2 4 HIS A 63  ? HIS A 63   . ? 1_555 ? 
6  AC2 4 HIS A 71  ? HIS A 71   . ? 1_555 ? 
7  AC2 4 HIS A 80  ? HIS A 80   . ? 1_555 ? 
8  AC2 4 ASP A 83  ? ASP A 83   . ? 1_555 ? 
9  AC3 7 GLU B 133 ? GLU F 133  . ? 1_555 ? 
10 AC3 7 THR B 137 ? THR F 137  . ? 1_555 ? 
11 AC3 7 ASN B 139 ? ASN F 139  . ? 1_555 ? 
12 AC3 7 GLY B 141 ? GLY F 141  . ? 1_555 ? 
13 AC3 7 HOH O .   ? HOH F 2098 . ? 1_555 ? 
14 AC3 7 HOH O .   ? HOH F 2101 . ? 1_555 ? 
15 AC3 7 HOH O .   ? HOH F 2115 . ? 1_555 ? 
16 AC4 6 GLU A 133 ? GLU A 133  . ? 1_555 ? 
17 AC4 6 THR A 137 ? THR A 137  . ? 1_555 ? 
18 AC4 6 ASN A 139 ? ASN A 139  . ? 1_555 ? 
19 AC4 6 ALA A 140 ? ALA A 140  . ? 1_555 ? 
20 AC4 6 GLY A 141 ? GLY A 141  . ? 1_555 ? 
21 AC4 6 HOH N .   ? HOH A 2143 . ? 1_555 ? 
22 AC5 8 ASN A 26  ? ASN A 26   . ? 1_555 ? 
23 AC5 8 GLY A 27  ? GLY A 27   . ? 1_555 ? 
24 AC5 8 LYS A 91  ? LYS A 91   . ? 1_655 ? 
25 AC5 8 ASP A 92  ? ASP A 92   . ? 1_655 ? 
26 AC5 8 SER A 102 ? SER A 102  . ? 1_555 ? 
27 AC5 8 VAL A 103 ? VAL A 103  . ? 1_555 ? 
28 AC5 8 HIS A 110 ? HIS A 110  . ? 1_555 ? 
29 AC5 8 HOH N .   ? HOH A 2037 . ? 1_555 ? 
30 AC6 4 HIS B 46  ? HIS F 46   . ? 1_555 ? 
31 AC6 4 HIS B 48  ? HIS F 48   . ? 1_555 ? 
32 AC6 4 HIS B 63  ? HIS F 63   . ? 1_555 ? 
33 AC6 4 HIS B 120 ? HIS F 120  . ? 1_555 ? 
34 AC7 4 HIS B 63  ? HIS F 63   . ? 1_555 ? 
35 AC7 4 HIS B 71  ? HIS F 71   . ? 1_555 ? 
36 AC7 4 HIS B 80  ? HIS F 80   . ? 1_555 ? 
37 AC7 4 ASP B 83  ? ASP F 83   . ? 1_555 ? 
38 AC8 7 GLU A 21  ? GLU A 21   . ? 1_555 ? 
39 AC8 7 GLN A 22  ? GLN A 22   . ? 1_555 ? 
40 AC8 7 LYS A 23  ? LYS A 23   . ? 1_555 ? 
41 AC8 7 PRO A 28  ? PRO A 28   . ? 1_555 ? 
42 AC8 7 TRP A 32  ? TRP A 32   . ? 1_555 ? 
43 AC8 7 GLU A 100 ? GLU A 100  . ? 1_555 ? 
44 AC8 7 HOH N .   ? HOH A 2034 . ? 1_555 ? 
45 AC9 6 THR A 39  ? THR A 39   . ? 1_555 ? 
46 AC9 6 GLU A 40  ? GLU A 40   . ? 1_555 ? 
47 AC9 6 LEU A 67  ? LEU A 67   . ? 1_455 ? 
48 AC9 6 LYS A 91  ? LYS A 91   . ? 1_555 ? 
49 AC9 6 HOH N .   ? HOH A 2140 . ? 1_455 ? 
50 AC9 6 HOH N .   ? HOH A 2160 . ? 1_555 ? 
51 BC1 5 THR A 58  ? THR A 58   . ? 1_555 ? 
52 BC1 5 SER A 142 ? SER A 142  . ? 1_555 ? 
53 BC1 5 ARG A 143 ? ARG A 143  . ? 1_555 ? 
54 BC1 5 HOH N .   ? HOH A 2153 . ? 1_555 ? 
55 BC1 5 HOH N .   ? HOH A 2161 . ? 1_555 ? 
56 BC2 3 THR B 58  ? THR F 58   . ? 1_555 ? 
57 BC2 3 SER B 142 ? SER F 142  . ? 1_555 ? 
58 BC2 3 ARG B 143 ? ARG F 143  . ? 1_555 ? 
# 
_database_PDB_matrix.entry_id          4A7U 
_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                    4A7U 
_atom_sites.fract_transf_matrix[1][1]   0.026110 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.006850 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.014684 
_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]   0.020594 
_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   ? 9.285   5.712   31.002  1.00 25.17  ? 1    ALA A N   1 
ATOM   2    C  CA  . ALA A 1 1   ? 8.583   4.535   30.456  1.00 18.79  ? 1    ALA A CA  1 
ATOM   3    C  C   . ALA A 1 1   ? 8.398   4.721   28.958  1.00 18.60  ? 1    ALA A C   1 
ATOM   4    O  O   . ALA A 1 1   ? 8.370   5.822   28.435  1.00 24.73  ? 1    ALA A O   1 
ATOM   5    C  CB  . ALA A 1 1   ? 7.227   4.357   31.132  1.00 21.14  ? 1    ALA A CB  1 
ATOM   6    N  N   . THR A 1 2   ? 8.223   3.605   28.290  1.00 13.65  ? 2    THR A N   1 
ATOM   7    C  CA  . THR A 1 2   ? 7.918   3.525   26.865  1.00 13.79  ? 2    THR A CA  1 
ATOM   8    C  C   . THR A 1 2   ? 6.498   2.955   26.758  1.00 11.38  ? 2    THR A C   1 
ATOM   9    O  O   . THR A 1 2   ? 6.142   2.094   27.559  1.00 11.79  ? 2    THR A O   1 
ATOM   10   C  CB  . THR A 1 2   ? 8.935   2.530   26.235  1.00 16.27  ? 2    THR A CB  1 
ATOM   11   O  OG1 . THR A 1 2   ? 10.271  3.012   26.468  1.00 21.85  ? 2    THR A OG1 1 
ATOM   12   C  CG2 . THR A 1 2   ? 8.702   2.325   24.798  1.00 16.86  ? 2    THR A CG2 1 
ATOM   13   N  N   . LYS A 1 3   ? 5.715   3.423   25.794  1.00 10.37  ? 3    LYS A N   1 
ATOM   14   C  CA  . LYS A 1 3   ? 4.326   3.023   25.654  1.00 9.77   ? 3    LYS A CA  1 
ATOM   15   C  C   . LYS A 1 3   ? 4.024   2.675   24.209  1.00 9.12   ? 3    LYS A C   1 
ATOM   16   O  O   . LYS A 1 3   ? 4.609   3.236   23.264  1.00 9.69   ? 3    LYS A O   1 
ATOM   17   C  CB  . LYS A 1 3   ? 3.390   4.148   26.128  1.00 11.54  ? 3    LYS A CB  1 
ATOM   18   C  CG  . LYS A 1 3   ? 3.540   4.428   27.613  1.00 14.38  ? 3    LYS A CG  1 
ATOM   19   C  CD  . LYS A 1 3   ? 2.866   5.712   28.055  1.00 17.96  ? 3    LYS A CD  1 
ATOM   20   C  CE  . LYS A 1 3   ? 3.265   6.050   29.485  1.00 23.97  ? 3    LYS A CE  1 
ATOM   21   N  NZ  . LYS A 1 3   ? 3.047   7.484   29.829  0.50 26.75  ? 3    LYS A NZ  1 
ATOM   22   N  N   . ALA A 1 4   ? 3.058   1.773   24.038  1.00 8.89   ? 4    ALA A N   1 
ATOM   23   C  CA  . ALA A 1 4   ? 2.554   1.408   22.742  1.00 8.93   ? 4    ALA A CA  1 
ATOM   24   C  C   . ALA A 1 4   ? 1.074   1.143   22.860  1.00 8.54   ? 4    ALA A C   1 
ATOM   25   O  O   . ALA A 1 4   ? 0.535   1.027   23.957  1.00 9.50   ? 4    ALA A O   1 
ATOM   26   C  CB  . ALA A 1 4   ? 3.326   0.216   22.146  1.00 9.74   ? 4    ALA A CB  1 
ATOM   27   N  N   . VAL A 1 5   ? 0.397   1.011   21.715  1.00 8.71   ? 5    VAL A N   1 
ATOM   28   C  CA  . VAL A 1 5   ? -1.046  0.892   21.705  1.00 8.49   ? 5    VAL A CA  1 
ATOM   29   C  C   . VAL A 1 5   ? -1.467  0.128   20.447  1.00 8.31   ? 5    VAL A C   1 
ATOM   30   O  O   . VAL A 1 5   ? -0.766  0.156   19.435  1.00 9.51   ? 5    VAL A O   1 
ATOM   31   C  CB  . VAL A 1 5   ? -1.705  2.294   21.765  1.00 9.75   ? 5    VAL A CB  1 
ATOM   32   C  CG1 . VAL A 1 5   ? -1.317  3.126   20.551  1.00 11.55  ? 5    VAL A CG1 1 
ATOM   33   C  CG2 . VAL A 1 5   ? -3.176  2.224   21.978  1.00 11.75  ? 5    VAL A CG2 1 
ATOM   34   N  N   . CYS A 1 6   ? -2.614  -0.523  20.518  1.00 8.65   ? 6    CYS A N   1 
ATOM   35   C  CA  . CYS A 1 6   ? -3.142  -1.266  19.385  1.00 8.57   ? 6    CYS A CA  1 
ATOM   36   C  C   . CYS A 1 6   ? -4.657  -1.205  19.370  1.00 8.41   ? 6    CYS A C   1 
ATOM   37   O  O   . CYS A 1 6   ? -5.287  -1.527  20.385  1.00 9.39   ? 6    CYS A O   1 
ATOM   38   C  CB  . CYS A 1 6   ? -2.681  -2.716  19.488  1.00 8.94   ? 6    CYS A CB  1 
ATOM   39   S  SG  . CYS A 1 6   ? -3.166  -3.715  18.060  1.00 10.66  ? 6    CYS A SG  1 
ATOM   40   N  N   . VAL A 1 7   ? -5.225  -0.834  18.234  1.00 8.46   ? 7    VAL A N   1 
ATOM   41   C  CA  . VAL A 1 7   ? -6.654  -0.859  18.012  1.00 8.84   ? 7    VAL A CA  1 
ATOM   42   C  C   . VAL A 1 7   ? -6.959  -2.135  17.220  1.00 9.12   ? 7    VAL A C   1 
ATOM   43   O  O   . VAL A 1 7   ? -6.438  -2.348  16.130  1.00 9.97   ? 7    VAL A O   1 
ATOM   44   C  CB  . VAL A 1 7   ? -7.121  0.378   17.221  1.00 10.89  ? 7    VAL A CB  1 
ATOM   45   C  CG1 . VAL A 1 7   ? -8.606  0.277   16.917  1.00 13.49  ? 7    VAL A CG1 1 
ATOM   46   C  CG2 . VAL A 1 7   ? -6.781  1.644   17.993  1.00 13.49  ? 7    VAL A CG2 1 
ATOM   47   N  N   . LEU A 1 8   ? -7.781  -3.005  17.805  1.00 9.47   ? 8    LEU A N   1 
ATOM   48   C  CA  . LEU A 1 8   ? -8.138  -4.277  17.185  1.00 9.95   ? 8    LEU A CA  1 
ATOM   49   C  C   . LEU A 1 8   ? -9.474  -4.153  16.434  1.00 10.37  ? 8    LEU A C   1 
ATOM   50   O  O   . LEU A 1 8   ? -10.475 -3.761  17.024  1.00 11.32  ? 8    LEU A O   1 
ATOM   51   C  CB  . LEU A 1 8   ? -8.253  -5.389  18.234  1.00 11.14  ? 8    LEU A CB  1 
ATOM   52   C  CG  . LEU A 1 8   ? -6.993  -5.760  19.045  1.00 11.72  ? 8    LEU A CG  1 
ATOM   53   C  CD1 . LEU A 1 8   ? -7.374  -6.594  20.286  1.00 13.90  ? 8    LEU A CD1 1 
ATOM   54   C  CD2 . LEU A 1 8   ? -5.982  -6.417  18.195  1.00 15.78  ? 8    LEU A CD2 1 
ATOM   55   N  N   . LYS A 1 9   ? -9.482  -4.509  15.166  1.00 11.39  ? 9    LYS A N   1 
ATOM   56   C  CA  . LYS A 1 9   ? -10.700 -4.556  14.352  1.00 13.39  ? 9    LYS A CA  1 
ATOM   57   C  C   . LYS A 1 9   ? -10.640 -5.751  13.444  1.00 11.85  ? 9    LYS A C   1 
ATOM   58   O  O   . LYS A 1 9   ? -9.576  -6.249  13.131  1.00 11.73  ? 9    LYS A O   1 
ATOM   59   C  CB  . LYS A 1 9   ? -10.853 -3.281  13.516  1.00 17.06  ? 9    LYS A CB  1 
ATOM   60   C  CG  . LYS A 1 9   ? -11.011 -1.998  14.313  1.00 18.58  ? 9    LYS A CG  1 
ATOM   61   C  CD  . LYS A 1 9   ? -11.155 -0.818  13.377  0.50 19.71  ? 9    LYS A CD  1 
ATOM   62   C  CE  . LYS A 1 9   ? -11.501 0.453   14.119  0.50 20.89  ? 9    LYS A CE  1 
ATOM   63   N  NZ  . LYS A 1 9   ? -11.654 1.573   13.161  0.50 25.46  ? 9    LYS A NZ  1 
ATOM   64   N  N   . GLY A 1 10  ? -11.788 -6.192  12.959  1.00 13.94  ? 10   GLY A N   1 
ATOM   65   C  CA  . GLY A 1 10  ? -11.839 -7.268  11.978  1.00 14.32  ? 10   GLY A CA  1 
ATOM   66   C  C   . GLY A 1 10  ? -13.084 -7.133  11.124  1.00 16.43  ? 10   GLY A C   1 
ATOM   67   O  O   . GLY A 1 10  ? -13.650 -6.040  10.994  1.00 21.64  ? 10   GLY A O   1 
ATOM   68   N  N   . ASP A 1 11  ? -13.477 -8.252  10.547  1.00 16.79  ? 11   ASP A N   1 
ATOM   69   C  CA  . ASP A 1 11  ? -14.601 -8.268  9.622   1.00 19.23  ? 11   ASP A CA  1 
ATOM   70   C  C   . ASP A 1 11  ? -15.934 -8.499  10.311  1.00 18.42  ? 11   ASP A C   1 
ATOM   71   O  O   . ASP A 1 11  ? -16.968 -8.331  9.687   1.00 24.13  ? 11   ASP A O   1 
ATOM   72   C  CB  . ASP A 1 11  ? -14.405 -9.361  8.559   1.00 23.17  ? 11   ASP A CB  1 
ATOM   73   C  CG  . ASP A 1 11  ? -13.264 -9.058  7.627   1.00 27.63  ? 11   ASP A CG  1 
ATOM   74   O  OD1 . ASP A 1 11  ? -13.072 -7.874  7.297   1.00 30.27  ? 11   ASP A OD1 1 
ATOM   75   O  OD2 . ASP A 1 11  ? -12.562 -10.008 7.222   1.00 38.39  ? 11   ASP A OD2 1 
ATOM   76   N  N   . GLY A 1 12  ? -15.921 -8.923  11.561  1.00 17.73  ? 12   GLY A N   1 
ATOM   77   C  CA  . GLY A 1 12  ? -17.103 -9.264  12.291  1.00 17.38  ? 12   GLY A CA  1 
ATOM   78   C  C   . GLY A 1 12  ? -17.244 -8.342  13.465  1.00 15.72  ? 12   GLY A C   1 
ATOM   79   O  O   . GLY A 1 12  ? -16.851 -7.171  13.402  1.00 17.41  ? 12   GLY A O   1 
ATOM   80   N  N   . PRO A 1 13  ? -17.769 -8.862  14.566  1.00 15.77  ? 13   PRO A N   1 
ATOM   81   C  CA  . PRO A 1 13  ? -18.135 -8.039  15.701  1.00 16.65  ? 13   PRO A CA  1 
ATOM   82   C  C   . PRO A 1 13  ? -17.005 -7.694  16.674  1.00 15.00  ? 13   PRO A C   1 
ATOM   83   O  O   . PRO A 1 13  ? -17.204 -6.911  17.603  1.00 15.96  ? 13   PRO A O   1 
ATOM   84   C  CB  . PRO A 1 13  ? -19.195 -8.912  16.401  1.00 19.06  ? 13   PRO A CB  1 
ATOM   85   C  CG  . PRO A 1 13  ? -18.742 -10.309 16.128  1.00 18.74  ? 13   PRO A CG  1 
ATOM   86   C  CD  . PRO A 1 13  ? -18.283 -10.238 14.699  1.00 16.17  ? 13   PRO A CD  1 
ATOM   87   N  N   . VAL A 1 14  ? -15.846 -8.293  16.501  1.00 12.54  ? 14   VAL A N   1 
ATOM   88   C  CA  . VAL A 1 14  ? -14.829 -8.188  17.522  1.00 11.88  ? 14   VAL A CA  1 
ATOM   89   C  C   . VAL A 1 14  ? -14.044 -6.904  17.352  1.00 12.21  ? 14   VAL A C   1 
ATOM   90   O  O   . VAL A 1 14  ? -13.516 -6.600  16.291  1.00 13.44  ? 14   VAL A O   1 
ATOM   91   C  CB  . VAL A 1 14  ? -13.876 -9.409  17.517  1.00 11.34  ? 14   VAL A CB  1 
ATOM   92   C  CG1 . VAL A 1 14  ? -12.803 -9.280  18.602  1.00 12.29  ? 14   VAL A CG1 1 
ATOM   93   C  CG2 . VAL A 1 14  ? -14.671 -10.688 17.693  1.00 13.47  ? 14   VAL A CG2 1 
ATOM   94   N  N   . GLN A 1 15  ? -13.931 -6.155  18.423  1.00 12.31  ? 15   GLN A N   1 
ATOM   95   C  CA  . GLN A 1 15  ? -13.147 -4.926  18.398  1.00 13.48  ? 15   GLN A CA  1 
ATOM   96   C  C   . GLN A 1 15  ? -12.573 -4.669  19.763  1.00 12.05  ? 15   GLN A C   1 
ATOM   97   O  O   . GLN A 1 15  ? -13.135 -5.066  20.794  1.00 14.27  ? 15   GLN A O   1 
ATOM   98   C  CB  . GLN A 1 15  ? -13.947 -3.759  17.910  1.00 18.43  ? 15   GLN A CB  1 
ATOM   99   C  CG  . GLN A 1 15  ? -15.167 -3.433  18.702  1.00 24.30  ? 15   GLN A CG  1 
ATOM   100  C  CD  . GLN A 1 15  ? -15.910 -2.268  18.080  1.00 29.92  ? 15   GLN A CD  1 
ATOM   101  O  OE1 . GLN A 1 15  ? -15.354 -1.182  17.930  1.00 36.70  ? 15   GLN A OE1 1 
ATOM   102  N  NE2 . GLN A 1 15  ? -17.158 -2.496  17.696  1.00 38.70  ? 15   GLN A NE2 1 
ATOM   103  N  N   . GLY A 1 16  ? -11.411 -4.040  19.797  1.00 11.70  ? 16   GLY A N   1 
ATOM   104  C  CA  . GLY A 1 16  ? -10.826 -3.775  21.053  1.00 13.30  ? 16   GLY A CA  1 
ATOM   105  C  C   . GLY A 1 16  ? -9.745  -2.728  21.027  1.00 10.26  ? 16   GLY A C   1 
ATOM   106  O  O   . GLY A 1 16  ? -9.392  -2.176  19.990  1.00 10.37  ? 16   GLY A O   1 
ATOM   107  N  N   A ILE A 1 17  ? -9.232  -2.436  22.213  0.50 10.03  ? 17   ILE A N   1 
ATOM   108  N  N   B ILE A 1 17  ? -9.213  -2.469  22.204  0.50 9.90   ? 17   ILE A N   1 
ATOM   109  C  CA  A ILE A 1 17  ? -8.174  -1.423  22.437  0.50 9.86   ? 17   ILE A CA  1 
ATOM   110  C  CA  B ILE A 1 17  ? -8.182  -1.451  22.397  0.50 9.65   ? 17   ILE A CA  1 
ATOM   111  C  C   A ILE A 1 17  ? -7.228  -2.009  23.478  0.50 9.47   ? 17   ILE A C   1 
ATOM   112  C  C   B ILE A 1 17  ? -7.231  -1.993  23.479  0.50 9.45   ? 17   ILE A C   1 
ATOM   113  O  O   A ILE A 1 17  ? -7.669  -2.399  24.565  0.50 10.71  ? 17   ILE A O   1 
ATOM   114  O  O   B ILE A 1 17  ? -7.673  -2.383  24.568  0.50 10.72  ? 17   ILE A O   1 
ATOM   115  C  CB  A ILE A 1 17  ? -8.723  -0.086  22.994  0.50 12.76  ? 17   ILE A CB  1 
ATOM   116  C  CB  B ILE A 1 17  ? -8.841  -0.086  22.730  0.50 10.75  ? 17   ILE A CB  1 
ATOM   117  C  CG1 A ILE A 1 17  ? -9.697  0.548   22.055  0.50 17.93  ? 17   ILE A CG1 1 
ATOM   118  C  CG1 B ILE A 1 17  ? -7.791  0.986   22.938  0.50 13.68  ? 17   ILE A CG1 1 
ATOM   119  C  CG2 A ILE A 1 17  ? -7.621  0.944   23.122  0.50 13.70  ? 17   ILE A CG2 1 
ATOM   120  C  CG2 B ILE A 1 17  ? -9.736  -0.193  23.963  0.50 10.68  ? 17   ILE A CG2 1 
ATOM   121  C  CD1 A ILE A 1 17  ? -8.979  1.153   20.880  0.50 19.31  ? 17   ILE A CD1 1 
ATOM   122  C  CD1 B ILE A 1 17  ? -6.997  1.321   21.693  0.50 12.42  ? 17   ILE A CD1 1 
ATOM   123  N  N   . ILE A 1 18  ? -5.937  -2.072  23.158  1.00 9.12   ? 18   ILE A N   1 
ATOM   124  C  CA  . ILE A 1 18  ? -4.933  -2.646  24.041  1.00 9.02   ? 18   ILE A CA  1 
ATOM   125  C  C   . ILE A 1 18  ? -3.760  -1.683  24.172  1.00 9.13   ? 18   ILE A C   1 
ATOM   126  O  O   . ILE A 1 18  ? -3.245  -1.187  23.166  1.00 10.29  ? 18   ILE A O   1 
ATOM   127  C  CB  . ILE A 1 18  ? -4.444  -4.021  23.536  1.00 9.47   ? 18   ILE A CB  1 
ATOM   128  C  CG1 . ILE A 1 18  ? -5.628  -5.030  23.444  1.00 10.92  ? 18   ILE A CG1 1 
ATOM   129  C  CG2 . ILE A 1 18  ? -3.318  -4.556  24.410  1.00 9.86   ? 18   ILE A CG2 1 
ATOM   130  C  CD1 . ILE A 1 18  ? -6.171  -5.486  24.793  1.00 12.73  ? 18   ILE A CD1 1 
ATOM   131  N  N   . ASN A 1 19  ? -3.362  -1.434  25.399  1.00 9.03   ? 19   ASN A N   1 
ATOM   132  C  CA  . ASN A 1 19  ? -2.243  -0.564  25.758  1.00 9.23   ? 19   ASN A CA  1 
ATOM   133  C  C   . ASN A 1 19  ? -1.093  -1.404  26.296  1.00 8.82   ? 19   ASN A C   1 
ATOM   134  O  O   . ASN A 1 19  ? -1.293  -2.419  26.937  1.00 9.66   ? 19   ASN A O   1 
ATOM   135  C  CB  . ASN A 1 19  ? -2.709  0.413   26.835  1.00 11.03  ? 19   ASN A CB  1 
ATOM   136  C  CG  . ASN A 1 19  ? -3.943  1.180   26.400  1.00 12.85  ? 19   ASN A CG  1 
ATOM   137  O  OD1 . ASN A 1 19  ? -3.859  2.027   25.546  1.00 15.49  ? 19   ASN A OD1 1 
ATOM   138  N  ND2 . ASN A 1 19  ? -5.064  0.886   26.959  1.00 16.11  ? 19   ASN A ND2 1 
ATOM   139  N  N   . PHE A 1 20  ? 0.122   -0.934  26.007  1.00 9.11   ? 20   PHE A N   1 
ATOM   140  C  CA  . PHE A 1 20  ? 1.354   -1.527  26.474  1.00 9.04   ? 20   PHE A CA  1 
ATOM   141  C  C   . PHE A 1 20  ? 2.201   -0.470  27.168  1.00 8.89   ? 20   PHE A C   1 
ATOM   142  O  O   . PHE A 1 20  ? 2.323   0.655   26.673  1.00 10.13  ? 20   PHE A O   1 
ATOM   143  C  CB  . PHE A 1 20  ? 2.214   -2.069  25.307  1.00 9.47   ? 20   PHE A CB  1 
ATOM   144  C  CG  . PHE A 1 20  ? 1.529   -3.107  24.459  1.00 9.24   ? 20   PHE A CG  1 
ATOM   145  C  CD1 . PHE A 1 20  ? 0.640   -2.754  23.454  1.00 10.54  ? 20   PHE A CD1 1 
ATOM   146  C  CD2 . PHE A 1 20  ? 1.759   -4.443  24.684  1.00 9.95   ? 20   PHE A CD2 1 
ATOM   147  C  CE1 . PHE A 1 20  ? 0.006   -3.733  22.697  1.00 11.82  ? 20   PHE A CE1 1 
ATOM   148  C  CE2 . PHE A 1 20  ? 1.138   -5.416  23.928  1.00 11.34  ? 20   PHE A CE2 1 
ATOM   149  C  CZ  . PHE A 1 20  ? 0.273   -5.062  22.919  1.00 11.71  ? 20   PHE A CZ  1 
ATOM   150  N  N   . GLU A 1 21  ? 2.840   -0.837  28.278  1.00 9.38   ? 21   GLU A N   1 
ATOM   151  C  CA  . GLU A 1 21  ? 3.763   0.094   28.941  1.00 9.68   ? 21   GLU A CA  1 
ATOM   152  C  C   . GLU A 1 21  ? 4.918   -0.688  29.518  1.00 9.35   ? 21   GLU A C   1 
ATOM   153  O  O   . GLU A 1 21  ? 4.745   -1.736  30.121  1.00 10.85  ? 21   GLU A O   1 
ATOM   154  C  CB  . GLU A 1 21  ? 3.050   0.884   30.038  1.00 11.75  ? 21   GLU A CB  1 
ATOM   155  C  CG  . GLU A 1 21  ? 3.948   1.938   30.683  1.00 13.63  ? 21   GLU A CG  1 
ATOM   156  C  CD  . GLU A 1 21  ? 3.182   3.033   31.397  1.00 18.01  ? 21   GLU A CD  1 
ATOM   157  O  OE1 . GLU A 1 21  ? 1.977   3.233   31.111  1.00 22.36  ? 21   GLU A OE1 1 
ATOM   158  O  OE2 . GLU A 1 21  ? 3.816   3.722   32.217  1.00 22.46  ? 21   GLU A OE2 1 
ATOM   159  N  N   . GLN A 1 22  ? 6.119   -0.162  29.305  1.00 9.91   ? 22   GLN A N   1 
ATOM   160  C  CA  . GLN A 1 22  ? 7.370   -0.798  29.751  1.00 10.35  ? 22   GLN A CA  1 
ATOM   161  C  C   . GLN A 1 22  ? 8.107   0.260   30.580  1.00 11.36  ? 22   GLN A C   1 
ATOM   162  O  O   . GLN A 1 22  ? 8.604   1.251   30.059  1.00 12.31  ? 22   GLN A O   1 
ATOM   163  C  CB  . GLN A 1 22  ? 8.185   -1.248  28.553  1.00 10.26  ? 22   GLN A CB  1 
ATOM   164  C  CG  . GLN A 1 22  ? 9.390   -2.065  28.937  1.00 10.75  ? 22   GLN A CG  1 
ATOM   165  C  CD  . GLN A 1 22  ? 10.090  -2.633  27.708  1.00 10.49  ? 22   GLN A CD  1 
ATOM   166  O  OE1 . GLN A 1 22  ? 10.093  -2.019  26.640  1.00 11.68  ? 22   GLN A OE1 1 
ATOM   167  N  NE2 . GLN A 1 22  ? 10.687  -3.813  27.849  1.00 11.26  ? 22   GLN A NE2 1 
ATOM   168  N  N   . LYS A 1 23  ? 8.136   0.040   31.889  1.00 12.27  ? 23   LYS A N   1 
ATOM   169  C  CA  . LYS A 1 23  ? 8.666   1.012   32.838  1.00 14.46  ? 23   LYS A CA  1 
ATOM   170  C  C   . LYS A 1 23  ? 10.152  1.218   32.639  1.00 14.85  ? 23   LYS A C   1 
ATOM   171  O  O   . LYS A 1 23  ? 10.618  2.332   32.779  1.00 17.83  ? 23   LYS A O   1 
ATOM   172  C  CB  . LYS A 1 23  ? 8.369   0.546   34.278  1.00 17.09  ? 23   LYS A CB  1 
ATOM   173  C  CG  . LYS A 1 23  ? 8.849   1.454   35.383  1.00 20.46  ? 23   LYS A CG  1 
ATOM   174  C  CD  . LYS A 1 23  ? 8.290   1.016   36.726  1.00 24.59  ? 23   LYS A CD  1 
ATOM   175  C  CE  . LYS A 1 23  ? 8.881   1.828   37.864  0.50 24.16  ? 23   LYS A CE  1 
ATOM   176  N  NZ  . LYS A 1 23  ? 8.046   1.765   39.092  0.50 31.31  ? 23   LYS A NZ  1 
ATOM   177  N  N   . GLU A 1 24  ? 10.902  0.168   32.346  1.00 14.63  ? 24   GLU A N   1 
ATOM   178  C  CA  . GLU A 1 24  ? 12.341  0.319   32.169  1.00 16.77  ? 24   GLU A CA  1 
ATOM   179  C  C   . GLU A 1 24  ? 12.830  -0.466  30.958  1.00 15.23  ? 24   GLU A C   1 
ATOM   180  O  O   . GLU A 1 24  ? 12.191  -1.431  30.548  1.00 14.44  ? 24   GLU A O   1 
ATOM   181  C  CB  . GLU A 1 24  ? 13.093  -0.120  33.428  1.00 20.86  ? 24   GLU A CB  1 
ATOM   182  C  CG  . GLU A 1 24  ? 13.067  -1.613  33.670  1.00 21.57  ? 24   GLU A CG  1 
ATOM   183  C  CD  . GLU A 1 24  ? 13.821  -2.060  34.913  1.00 27.72  ? 24   GLU A CD  1 
ATOM   184  O  OE1 . GLU A 1 24  ? 13.783  -1.325  35.920  1.00 34.57  ? 24   GLU A OE1 1 
ATOM   185  O  OE2 . GLU A 1 24  ? 14.433  -3.155  34.886  1.00 31.99  ? 24   GLU A OE2 1 
ATOM   186  N  N   . SER A 1 25  ? 13.987  -0.053  30.425  1.00 16.47  ? 25   SER A N   1 
ATOM   187  C  CA  . SER A 1 25  ? 14.570  -0.689  29.252  1.00 17.00  ? 25   SER A CA  1 
ATOM   188  C  C   . SER A 1 25  ? 14.724  -2.171  29.517  1.00 16.44  ? 25   SER A C   1 
ATOM   189  O  O   . SER A 1 25  ? 15.269  -2.570  30.546  1.00 17.13  ? 25   SER A O   1 
ATOM   190  C  CB  . SER A 1 25  ? 15.935  -0.120  28.928  1.00 20.46  ? 25   SER A CB  1 
ATOM   191  O  OG  . SER A 1 25  ? 16.485  -0.760  27.793  1.00 27.97  ? 25   SER A OG  1 
ATOM   192  N  N   . ASN A 1 26  ? 14.241  -2.979  28.578  1.00 15.13  ? 26   ASN A N   1 
ATOM   193  C  CA  . ASN A 1 26  ? 14.294  -4.418  28.615  1.00 14.71  ? 26   ASN A CA  1 
ATOM   194  C  C   . ASN A 1 26  ? 13.446  -5.059  29.726  1.00 13.26  ? 26   ASN A C   1 
ATOM   195  O  O   . ASN A 1 26  ? 13.543  -6.252  29.905  1.00 13.97  ? 26   ASN A O   1 
ATOM   196  C  CB  . ASN A 1 26  ? 15.729  -4.975  28.744  1.00 16.47  ? 26   ASN A CB  1 
ATOM   197  C  CG  . ASN A 1 26  ? 16.690  -4.493  27.662  1.00 16.82  ? 26   ASN A CG  1 
ATOM   198  O  OD1 . ASN A 1 26  ? 17.835  -4.151  27.978  1.00 19.93  ? 26   ASN A OD1 1 
ATOM   199  N  ND2 . ASN A 1 26  ? 16.285  -4.524  26.415  1.00 20.08  ? 26   ASN A ND2 1 
ATOM   200  N  N   . GLY A 1 27  ? 12.669  -4.274  30.481  1.00 13.68  ? 27   GLY A N   1 
ATOM   201  C  CA  . GLY A 1 27  ? 11.936  -4.779  31.632  1.00 13.02  ? 27   GLY A CA  1 
ATOM   202  C  C   . GLY A 1 27  ? 10.619  -5.411  31.253  1.00 11.49  ? 27   GLY A C   1 
ATOM   203  O  O   . GLY A 1 27  ? 10.273  -5.461  30.086  1.00 11.52  ? 27   GLY A O   1 
ATOM   204  N  N   . PRO A 1 28  ? 9.852   -5.897  32.253  1.00 11.49  ? 28   PRO A N   1 
ATOM   205  C  CA  . PRO A 1 28  ? 8.521   -6.439  31.924  1.00 10.80  ? 28   PRO A CA  1 
ATOM   206  C  C   . PRO A 1 28  ? 7.596   -5.351  31.339  1.00 10.02  ? 28   PRO A C   1 
ATOM   207  O  O   . PRO A 1 28  ? 7.768   -4.156  31.584  1.00 10.79  ? 28   PRO A O   1 
ATOM   208  C  CB  . PRO A 1 28  ? 8.001   -6.947  33.265  1.00 13.50  ? 28   PRO A CB  1 
ATOM   209  C  CG  . PRO A 1 28  ? 8.753   -6.136  34.261  1.00 15.47  ? 28   PRO A CG  1 
ATOM   210  C  CD  . PRO A 1 28  ? 10.120  -5.910  33.692  1.00 13.27  ? 28   PRO A CD  1 
ATOM   211  N  N   . VAL A 1 29  ? 6.628   -5.818  30.577  1.00 9.67   ? 29   VAL A N   1 
ATOM   212  C  CA  . VAL A 1 29  ? 5.658   -4.990  29.894  1.00 9.23   ? 29   VAL A CA  1 
ATOM   213  C  C   . VAL A 1 29  ? 4.270   -5.280  30.448  1.00 9.12   ? 29   VAL A C   1 
ATOM   214  O  O   . VAL A 1 29  ? 3.838   -6.430  30.492  1.00 10.23  ? 29   VAL A O   1 
ATOM   215  C  CB  . VAL A 1 29  ? 5.691   -5.252  28.376  1.00 9.31   ? 29   VAL A CB  1 
ATOM   216  C  CG1 . VAL A 1 29  ? 4.660   -4.379  27.652  1.00 10.20  ? 29   VAL A CG1 1 
ATOM   217  C  CG2 . VAL A 1 29  ? 7.085   -5.053  27.804  1.00 10.31  ? 29   VAL A CG2 1 
ATOM   218  N  N   . LYS A 1 30  ? 3.556   -4.232  30.863  1.00 9.28   ? 30   LYS A N   1 
ATOM   219  C  CA  . LYS A 1 30  ? 2.152   -4.321  31.226  1.00 9.93   ? 30   LYS A CA  1 
ATOM   220  C  C   . LYS A 1 30  ? 1.300   -4.174  29.971  1.00 9.48   ? 30   LYS A C   1 
ATOM   221  O  O   . LYS A 1 30  ? 1.552   -3.296  29.145  1.00 9.86   ? 30   LYS A O   1 
ATOM   222  C  CB  . LYS A 1 30  ? 1.802   -3.245  32.248  1.00 11.83  ? 30   LYS A CB  1 
ATOM   223  C  CG  . LYS A 1 30  ? 0.409   -3.330  32.817  1.00 17.52  ? 30   LYS A CG  1 
ATOM   224  C  CD  . LYS A 1 30  ? 0.330   -4.404  33.898  1.00 20.97  ? 30   LYS A CD  1 
ATOM   225  C  CE  . LYS A 1 30  ? -1.095  -4.667  34.342  1.00 26.10  ? 30   LYS A CE  1 
ATOM   226  N  NZ  . LYS A 1 30  ? -1.975  -5.052  33.206  1.00 30.99  ? 30   LYS A NZ  1 
ATOM   227  N  N   . VAL A 1 31  ? 0.289   -5.035  29.840  1.00 9.89   ? 31   VAL A N   1 
ATOM   228  C  CA  . VAL A 1 31  ? -0.618  -5.074  28.707  1.00 10.00  ? 31   VAL A CA  1 
ATOM   229  C  C   . VAL A 1 31  ? -2.025  -5.013  29.257  1.00 11.19  ? 31   VAL A C   1 
ATOM   230  O  O   . VAL A 1 31  ? -2.394  -5.839  30.086  1.00 13.30  ? 31   VAL A O   1 
ATOM   231  C  CB  . VAL A 1 31  ? -0.441  -6.387  27.915  1.00 11.10  ? 31   VAL A CB  1 
ATOM   232  C  CG1 . VAL A 1 31  ? -1.293  -6.380  26.656  1.00 12.37  ? 31   VAL A CG1 1 
ATOM   233  C  CG2 . VAL A 1 31  ? 1.031   -6.651  27.606  1.00 11.78  ? 31   VAL A CG2 1 
ATOM   234  N  N   . TRP A 1 32  ? -2.810  -4.009  28.862  1.00 10.16  ? 32   TRP A N   1 
ATOM   235  C  CA  . TRP A 1 32  ? -4.160  -3.877  29.425  1.00 11.62  ? 32   TRP A CA  1 
ATOM   236  C  C   . TRP A 1 32  ? -5.108  -3.243  28.459  1.00 9.88   ? 32   TRP A C   1 
ATOM   237  O  O   . TRP A 1 32  ? -4.705  -2.413  27.619  1.00 10.20  ? 32   TRP A O   1 
ATOM   238  C  CB  . TRP A 1 32  ? -4.127  -3.146  30.769  1.00 13.98  ? 32   TRP A CB  1 
ATOM   239  C  CG  . TRP A 1 32  ? -3.924  -1.686  30.654  1.00 14.29  ? 32   TRP A CG  1 
ATOM   240  C  CD1 . TRP A 1 32  ? -4.896  -0.718  30.745  1.00 17.59  ? 32   TRP A CD1 1 
ATOM   241  C  CD2 . TRP A 1 32  ? -2.686  -0.974  30.456  1.00 12.98  ? 32   TRP A CD2 1 
ATOM   242  N  NE1 . TRP A 1 32  ? -4.349  0.519   30.612  1.00 19.76  ? 32   TRP A NE1 1 
ATOM   243  C  CE2 . TRP A 1 32  ? -3.030  0.428   30.417  1.00 15.79  ? 32   TRP A CE2 1 
ATOM   244  C  CE3 . TRP A 1 32  ? -1.390  -1.346  30.273  1.00 14.23  ? 32   TRP A CE3 1 
ATOM   245  C  CZ2 . TRP A 1 32  ? -2.091  1.408   30.259  1.00 17.00  ? 32   TRP A CZ2 1 
ATOM   246  C  CZ3 . TRP A 1 32  ? -0.449  -0.348  30.087  1.00 14.46  ? 32   TRP A CZ3 1 
ATOM   247  C  CH2 . TRP A 1 32  ? -0.796  0.996   30.060  1.00 15.87  ? 32   TRP A CH2 1 
ATOM   248  N  N   . GLY A 1 33  ? -6.372  -3.559  28.582  1.00 10.23  ? 33   GLY A N   1 
ATOM   249  C  CA  . GLY A 1 33  ? -7.406  -2.948  27.762  1.00 10.34  ? 33   GLY A CA  1 
ATOM   250  C  C   . GLY A 1 33  ? -8.649  -3.800  27.726  1.00 10.33  ? 33   GLY A C   1 
ATOM   251  O  O   . GLY A 1 33  ? -8.926  -4.519  28.707  1.00 11.95  ? 33   GLY A O   1 
ATOM   252  N  N   . SER A 1 34  ? -9.395  -3.728  26.624  1.00 10.71  ? 34   SER A N   1 
ATOM   253  C  CA  . SER A 1 34  ? -10.697 -4.393  26.539  1.00 11.52  ? 34   SER A CA  1 
ATOM   254  C  C   . SER A 1 34  ? -10.947 -4.828  25.128  1.00 10.60  ? 34   SER A C   1 
ATOM   255  O  O   . SER A 1 34  ? -10.556 -4.153  24.203  1.00 12.08  ? 34   SER A O   1 
ATOM   256  C  CB  . SER A 1 34  ? -11.837 -3.422  26.977  1.00 13.95  ? 34   SER A CB  1 
ATOM   257  O  OG  . SER A 1 34  ? -13.022 -4.137  27.231  1.00 21.33  ? 34   SER A OG  1 
ATOM   258  N  N   . ILE A 1 35  ? -11.633 -5.955  24.983  1.00 10.62  ? 35   ILE A N   1 
ATOM   259  C  CA  . ILE A 1 35  ? -12.037 -6.478  23.693  1.00 10.56  ? 35   ILE A CA  1 
ATOM   260  C  C   . ILE A 1 35  ? -13.509 -6.886  23.843  1.00 11.42  ? 35   ILE A C   1 
ATOM   261  O  O   . ILE A 1 35  ? -13.829 -7.597  24.818  1.00 13.87  ? 35   ILE A O   1 
ATOM   262  C  CB  . ILE A 1 35  ? -11.183 -7.691  23.229  1.00 10.74  ? 35   ILE A CB  1 
ATOM   263  C  CG1 . ILE A 1 35  ? -9.706  -7.380  23.326  1.00 10.85  ? 35   ILE A CG1 1 
ATOM   264  C  CG2 . ILE A 1 35  ? -11.587 -8.098  21.835  1.00 11.86  ? 35   ILE A CG2 1 
ATOM   265  C  CD1 . ILE A 1 35  ? -8.809  -8.567  23.086  1.00 12.92  ? 35   ILE A CD1 1 
ATOM   266  N  N   . LYS A 1 36  ? -14.351 -6.489  22.896  1.00 11.39  ? 36   LYS A N   1 
ATOM   267  C  CA  . LYS A 1 36  ? -15.760 -6.838  22.897  1.00 11.45  ? 36   LYS A CA  1 
ATOM   268  C  C   . LYS A 1 36  ? -16.150 -7.608  21.670  1.00 11.09  ? 36   LYS A C   1 
ATOM   269  O  O   . LYS A 1 36  ? -15.388 -7.667  20.703  1.00 12.00  ? 36   LYS A O   1 
ATOM   270  C  CB  . LYS A 1 36  ? -16.615 -5.562  23.081  1.00 13.22  ? 36   LYS A CB  1 
ATOM   271  C  CG  . LYS A 1 36  ? -16.526 -4.545  21.977  1.00 14.62  ? 36   LYS A CG  1 
ATOM   272  C  CD  . LYS A 1 36  ? -17.318 -3.301  22.310  1.00 17.62  ? 36   LYS A CD  1 
ATOM   273  C  CE  . LYS A 1 36  ? -17.096 -2.200  21.321  1.00 20.34  ? 36   LYS A CE  1 
ATOM   274  N  NZ  . LYS A 1 36  ? -17.807 -1.002  21.829  1.00 25.45  ? 36   LYS A NZ  1 
ATOM   275  N  N   . GLY A 1 37  ? -17.352 -8.180  21.687  1.00 11.06  ? 37   GLY A N   1 
ATOM   276  C  CA  . GLY A 1 37  ? -17.848 -8.926  20.546  1.00 11.08  ? 37   GLY A CA  1 
ATOM   277  C  C   . GLY A 1 37  ? -17.429 -10.383 20.453  1.00 10.69  ? 37   GLY A C   1 
ATOM   278  O  O   . GLY A 1 37  ? -17.577 -11.002 19.397  1.00 12.32  ? 37   GLY A O   1 
ATOM   279  N  N   . LEU A 1 38  ? -16.878 -10.890 21.558  1.00 11.27  ? 38   LEU A N   1 
ATOM   280  C  CA  . LEU A 1 38  ? -16.335 -12.230 21.609  1.00 10.75  ? 38   LEU A CA  1 
ATOM   281  C  C   . LEU A 1 38  ? -17.326 -13.240 22.155  1.00 11.39  ? 38   LEU A C   1 
ATOM   282  O  O   . LEU A 1 38  ? -18.180 -12.916 22.984  1.00 12.49  ? 38   LEU A O   1 
ATOM   283  C  CB  . LEU A 1 38  ? -15.122 -12.255 22.553  1.00 10.54  ? 38   LEU A CB  1 
ATOM   284  C  CG  . LEU A 1 38  ? -13.879 -11.515 22.038  1.00 10.96  ? 38   LEU A CG  1 
ATOM   285  C  CD1 . LEU A 1 38  ? -12.922 -11.294 23.194  1.00 12.43  ? 38   LEU A CD1 1 
ATOM   286  C  CD2 . LEU A 1 38  ? -13.191 -12.272 20.909  1.00 11.85  ? 38   LEU A CD2 1 
ATOM   287  N  N   . THR A 1 39  ? -17.171 -14.485 21.754  1.00 11.53  ? 39   THR A N   1 
ATOM   288  C  CA  . THR A 1 39  ? -17.877 -15.568 22.409  1.00 11.67  ? 39   THR A CA  1 
ATOM   289  C  C   . THR A 1 39  ? -17.262 -15.790 23.809  1.00 11.09  ? 39   THR A C   1 
ATOM   290  O  O   . THR A 1 39  ? -16.064 -15.636 24.034  1.00 11.29  ? 39   THR A O   1 
ATOM   291  C  CB  . THR A 1 39  ? -17.778 -16.865 21.596  1.00 12.92  ? 39   THR A CB  1 
ATOM   292  O  OG1 . THR A 1 39  ? -16.393 -17.239 21.401  1.00 14.17  ? 39   THR A OG1 1 
ATOM   293  C  CG2 . THR A 1 39  ? -18.468 -16.734 20.251  1.00 14.63  ? 39   THR A CG2 1 
ATOM   294  N  N   . GLU A 1 40  ? -18.103 -16.211 24.748  1.00 11.86  ? 40   GLU A N   1 
ATOM   295  C  CA  . GLU A 1 40  ? -17.645 -16.463 26.074  1.00 11.49  ? 40   GLU A CA  1 
ATOM   296  C  C   . GLU A 1 40  ? -16.581 -17.584 26.070  1.00 11.35  ? 40   GLU A C   1 
ATOM   297  O  O   . GLU A 1 40  ? -16.721 -18.604 25.407  1.00 13.66  ? 40   GLU A O   1 
ATOM   298  C  CB  . GLU A 1 40  ? -18.834 -16.861 26.957  1.00 14.95  ? 40   GLU A CB  1 
ATOM   299  C  CG  . GLU A 1 40  ? -18.456 -17.031 28.408  1.00 20.04  ? 40   GLU A CG  1 
ATOM   300  C  CD  . GLU A 1 40  ? -19.294 -17.950 29.171  1.00 20.05  ? 40   GLU A CD  1 
ATOM   301  O  OE1 . GLU A 1 40  ? -19.982 -18.846 28.573  1.00 26.22  ? 40   GLU A OE1 1 
ATOM   302  O  OE2 . GLU A 1 40  ? -19.227 -17.791 30.406  1.00 19.44  ? 40   GLU A OE2 1 
ATOM   303  N  N   . GLY A 1 41  ? -15.522 -17.387 26.854  1.00 10.34  ? 41   GLY A N   1 
ATOM   304  C  CA  . GLY A 1 41  ? -14.439 -18.350 26.945  1.00 10.31  ? 41   GLY A CA  1 
ATOM   305  C  C   . GLY A 1 41  ? -13.104 -17.764 26.524  1.00 9.48   ? 41   GLY A C   1 
ATOM   306  O  O   . GLY A 1 41  ? -12.915 -16.554 26.445  1.00 9.97   ? 41   GLY A O   1 
ATOM   307  N  N   A LEU A 1 42  ? -12.156 -18.665 26.286  0.50 9.32   ? 42   LEU A N   1 
ATOM   308  N  N   B LEU A 1 42  ? -12.157 -18.668 26.282  0.50 9.33   ? 42   LEU A N   1 
ATOM   309  C  CA  A LEU A 1 42  ? -10.778 -18.308 25.979  0.50 9.01   ? 42   LEU A CA  1 
ATOM   310  C  CA  B LEU A 1 42  ? -10.779 -18.300 25.991  0.50 9.00   ? 42   LEU A CA  1 
ATOM   311  C  C   A LEU A 1 42  ? -10.608 -18.006 24.508  0.50 8.94   ? 42   LEU A C   1 
ATOM   312  C  C   B LEU A 1 42  ? -10.604 -18.006 24.518  0.50 8.93   ? 42   LEU A C   1 
ATOM   313  O  O   A LEU A 1 42  ? -11.136 -18.689 23.641  0.50 10.27  ? 42   LEU A O   1 
ATOM   314  O  O   B LEU A 1 42  ? -11.115 -18.704 23.662  0.50 10.33  ? 42   LEU A O   1 
ATOM   315  C  CB  A LEU A 1 42  ? -9.828  -19.463 26.325  0.50 9.77   ? 42   LEU A CB  1 
ATOM   316  C  CB  B LEU A 1 42  ? -9.821  -19.431 26.369  0.50 9.73   ? 42   LEU A CB  1 
ATOM   317  C  CG  A LEU A 1 42  ? -9.285  -19.593 27.725  0.50 12.61  ? 42   LEU A CG  1 
ATOM   318  C  CG  B LEU A 1 42  ? -9.653  -19.743 27.848  0.50 12.63  ? 42   LEU A CG  1 
ATOM   319  C  CD1 A LEU A 1 42  ? -10.412 -19.812 28.664  0.50 11.62  ? 42   LEU A CD1 1 
ATOM   320  C  CD1 B LEU A 1 42  ? -8.456  -20.705 27.964  0.50 14.95  ? 42   LEU A CD1 1 
ATOM   321  C  CD2 A LEU A 1 42  ? -8.318  -20.774 27.861  0.50 13.81  ? 42   LEU A CD2 1 
ATOM   322  C  CD2 B LEU A 1 42  ? -9.460  -18.556 28.781  0.50 13.28  ? 42   LEU A CD2 1 
ATOM   323  N  N   . HIS A 1 43  ? -9.757  -17.013 24.232  1.00 8.76   ? 43   HIS A N   1 
ATOM   324  C  CA  . HIS A 1 43  ? -9.384  -16.647 22.868  1.00 8.90   ? 43   HIS A CA  1 
ATOM   325  C  C   . HIS A 1 43  ? -7.894  -16.416 22.811  1.00 8.23   ? 43   HIS A C   1 
ATOM   326  O  O   . HIS A 1 43  ? -7.348  -15.588 23.545  1.00 8.50   ? 43   HIS A O   1 
ATOM   327  C  CB  . HIS A 1 43  ? -10.113 -15.368 22.449  1.00 9.09   ? 43   HIS A CB  1 
ATOM   328  C  CG  . HIS A 1 43  ? -11.573 -15.576 22.346  1.00 9.40   ? 43   HIS A CG  1 
ATOM   329  N  ND1 . HIS A 1 43  ? -12.167 -16.009 21.189  1.00 10.73  ? 43   HIS A ND1 1 
ATOM   330  C  CD2 . HIS A 1 43  ? -12.580 -15.476 23.292  1.00 9.99   ? 43   HIS A CD2 1 
ATOM   331  C  CE1 . HIS A 1 43  ? -13.477 -16.193 21.416  1.00 11.95  ? 43   HIS A CE1 1 
ATOM   332  N  NE2 . HIS A 1 43  ? -13.736 -15.872 22.684  1.00 11.31  ? 43   HIS A NE2 1 
ATOM   333  N  N   . GLY A 1 44  ? -7.222  -17.114 21.902  1.00 8.49   ? 44   GLY A N   1 
ATOM   334  C  CA  . GLY A 1 44  ? -5.793  -16.957 21.758  1.00 8.51   ? 44   GLY A CA  1 
ATOM   335  C  C   . GLY A 1 44  ? -5.427  -15.505 21.462  1.00 8.16   ? 44   GLY A C   1 
ATOM   336  O  O   . GLY A 1 44  ? -6.140  -14.799 20.753  1.00 8.78   ? 44   GLY A O   1 
ATOM   337  N  N   . PHE A 1 45  ? -4.277  -15.081 21.982  1.00 8.25   ? 45   PHE A N   1 
ATOM   338  C  CA  . PHE A 1 45  ? -3.880  -13.681 22.000  1.00 8.16   ? 45   PHE A CA  1 
ATOM   339  C  C   . PHE A 1 45  ? -2.398  -13.616 21.752  1.00 8.07   ? 45   PHE A C   1 
ATOM   340  O  O   . PHE A 1 45  ? -1.600  -14.002 22.623  1.00 9.02   ? 45   PHE A O   1 
ATOM   341  C  CB  . PHE A 1 45  ? -4.265  -13.109 23.361  1.00 8.46   ? 45   PHE A CB  1 
ATOM   342  C  CG  . PHE A 1 45  ? -4.126  -11.614 23.505  1.00 8.78   ? 45   PHE A CG  1 
ATOM   343  C  CD1 . PHE A 1 45  ? -4.842  -10.745 22.701  1.00 10.61  ? 45   PHE A CD1 1 
ATOM   344  C  CD2 . PHE A 1 45  ? -3.355  -11.074 24.522  1.00 9.78   ? 45   PHE A CD2 1 
ATOM   345  C  CE1 . PHE A 1 45  ? -4.787  -9.371  22.922  1.00 11.51  ? 45   PHE A CE1 1 
ATOM   346  C  CE2 . PHE A 1 45  ? -3.312  -9.712  24.738  1.00 11.32  ? 45   PHE A CE2 1 
ATOM   347  C  CZ  . PHE A 1 45  ? -4.054  -8.871  23.967  1.00 11.40  ? 45   PHE A CZ  1 
ATOM   348  N  N   . HIS A 1 46  ? -1.999  -13.166 20.550  1.00 7.94   ? 46   HIS A N   1 
ATOM   349  C  CA  . HIS A 1 46  ? -0.610  -13.250 20.157  1.00 8.29   ? 46   HIS A CA  1 
ATOM   350  C  C   . HIS A 1 46  ? -0.166  -12.040 19.376  1.00 7.94   ? 46   HIS A C   1 
ATOM   351  O  O   . HIS A 1 46  ? -0.939  -11.420 18.638  1.00 8.53   ? 46   HIS A O   1 
ATOM   352  C  CB  . HIS A 1 46  ? -0.297  -14.466 19.250  1.00 10.23  ? 46   HIS A CB  1 
ATOM   353  C  CG  . HIS A 1 46  ? -1.014  -15.687 19.638  1.00 9.69   ? 46   HIS A CG  1 
ATOM   354  N  ND1 . HIS A 1 46  ? -2.046  -16.112 18.919  1.00 11.57  ? 46   HIS A ND1 1 
ATOM   355  C  CD2 . HIS A 1 46  ? -0.868  -16.513 20.723  1.00 10.32  ? 46   HIS A CD2 1 
ATOM   356  C  CE1 . HIS A 1 46  ? -2.525  -17.204 19.509  1.00 11.80  ? 46   HIS A CE1 1 
ATOM   357  N  NE2 . HIS A 1 46  ? -1.802  -17.481 20.607  1.00 10.26  ? 46   HIS A NE2 1 
ATOM   358  N  N   . VAL A 1 47  ? 1.128   -11.758 19.476  1.00 8.05   ? 47   VAL A N   1 
ATOM   359  C  CA  . VAL A 1 47  ? 1.793   -10.863 18.529  1.00 8.13   ? 47   VAL A CA  1 
ATOM   360  C  C   . VAL A 1 47  ? 2.285   -11.720 17.353  1.00 8.17   ? 47   VAL A C   1 
ATOM   361  O  O   . VAL A 1 47  ? 3.019   -12.706 17.576  1.00 8.75   ? 47   VAL A O   1 
ATOM   362  C  CB  . VAL A 1 47  ? 2.957   -10.090 19.155  1.00 8.46   ? 47   VAL A CB  1 
ATOM   363  C  CG1 . VAL A 1 47  ? 3.578   -9.156  18.123  1.00 8.88   ? 47   VAL A CG1 1 
ATOM   364  C  CG2 . VAL A 1 47  ? 2.487   -9.305  20.384  1.00 9.52   ? 47   VAL A CG2 1 
ATOM   365  N  N   . HIS A 1 48  ? 1.856   -11.358 16.144  1.00 8.72   ? 48   HIS A N   1 
ATOM   366  C  CA  . HIS A 1 48  ? 2.280   -11.989 14.900  1.00 9.17   ? 48   HIS A CA  1 
ATOM   367  C  C   . HIS A 1 48  ? 3.372   -11.153 14.269  1.00 9.73   ? 48   HIS A C   1 
ATOM   368  O  O   . HIS A 1 48  ? 3.516   -9.969  14.537  1.00 11.71  ? 48   HIS A O   1 
ATOM   369  C  CB  . HIS A 1 48  ? 1.085   -12.174 13.982  1.00 9.42   ? 48   HIS A CB  1 
ATOM   370  C  CG  . HIS A 1 48  ? 0.097   -13.224 14.465  1.00 9.33   ? 48   HIS A CG  1 
ATOM   371  N  ND1 . HIS A 1 48  ? -0.173  -14.312 13.750  1.00 9.84   ? 48   HIS A ND1 1 
ATOM   372  C  CD2 . HIS A 1 48  ? -0.657  -13.327 15.614  1.00 10.18  ? 48   HIS A CD2 1 
ATOM   373  C  CE1 . HIS A 1 48  ? -1.101  -15.050 14.394  1.00 9.96   ? 48   HIS A CE1 1 
ATOM   374  N  NE2 . HIS A 1 48  ? -1.392  -14.473 15.538  1.00 10.45  ? 48   HIS A NE2 1 
ATOM   375  N  N   . GLU A 1 49  ? 4.142   -11.793 13.390  1.00 9.43   ? 49   GLU A N   1 
ATOM   376  C  CA  . GLU A 1 49  ? 5.400   -11.251 12.930  1.00 9.75   ? 49   GLU A CA  1 
ATOM   377  C  C   . GLU A 1 49  ? 5.270   -9.915  12.187  1.00 9.76   ? 49   GLU A C   1 
ATOM   378  O  O   . GLU A 1 49  ? 6.091   -8.997  12.413  1.00 11.29  ? 49   GLU A O   1 
ATOM   379  C  CB  . GLU A 1 49  ? 6.085   -12.275 12.021  1.00 11.22  ? 49   GLU A CB  1 
ATOM   380  C  CG  . GLU A 1 49  ? 7.463   -11.816 11.619  1.00 13.15  ? 49   GLU A CG  1 
ATOM   381  C  CD  . GLU A 1 49  ? 8.168   -12.779 10.748  1.00 16.16  ? 49   GLU A CD  1 
ATOM   382  O  OE1 . GLU A 1 49  ? 7.579   -13.830 10.403  1.00 17.45  ? 49   GLU A OE1 1 
ATOM   383  O  OE2 . GLU A 1 49  ? 9.335   -12.503 10.378  1.00 22.34  ? 49   GLU A OE2 1 
ATOM   384  N  N   . PHE A 1 50  ? 4.339   -9.812  11.273  1.00 9.38   ? 50   PHE A N   1 
ATOM   385  C  CA  . PHE A 1 50  ? 4.313   -8.679  10.386  1.00 9.64   ? 50   PHE A CA  1 
ATOM   386  C  C   . PHE A 1 50  ? 3.206   -7.707  10.793  1.00 9.19   ? 50   PHE A C   1 
ATOM   387  O  O   . PHE A 1 50  ? 2.094   -8.112  11.114  1.00 10.75  ? 50   PHE A O   1 
ATOM   388  C  CB  . PHE A 1 50  ? 4.084   -9.084  8.926   1.00 10.64  ? 50   PHE A CB  1 
ATOM   389  C  CG  . PHE A 1 50  ? 4.987   -10.160 8.447   1.00 12.00  ? 50   PHE A CG  1 
ATOM   390  C  CD1 . PHE A 1 50  ? 6.354   -10.009 8.490   1.00 13.90  ? 50   PHE A CD1 1 
ATOM   391  C  CD2 . PHE A 1 50  ? 4.456   -11.378 8.013   1.00 14.11  ? 50   PHE A CD2 1 
ATOM   392  C  CE1 . PHE A 1 50  ? 7.179   -11.074 8.082   1.00 15.37  ? 50   PHE A CE1 1 
ATOM   393  C  CE2 . PHE A 1 50  ? 5.258   -12.426 7.620   1.00 15.28  ? 50   PHE A CE2 1 
ATOM   394  C  CZ  . PHE A 1 50  ? 6.612   -12.258 7.678   1.00 15.93  ? 50   PHE A CZ  1 
ATOM   395  N  N   . GLY A 1 51  ? 3.513   -6.420  10.709  1.00 8.93   ? 51   GLY A N   1 
ATOM   396  C  CA  . GLY A 1 51  ? 2.492   -5.370  10.837  1.00 9.32   ? 51   GLY A CA  1 
ATOM   397  C  C   . GLY A 1 51  ? 1.811   -5.061  9.529   1.00 9.31   ? 51   GLY A C   1 
ATOM   398  O  O   . GLY A 1 51  ? 1.637   -3.903  9.156   1.00 11.17  ? 51   GLY A O   1 
ATOM   399  N  N   . ASP A 1 52  ? 1.409   -6.098  8.819   1.00 10.91  ? 52   ASP A N   1 
ATOM   400  C  CA  . ASP A 1 52  ? 0.829   -6.032  7.492   1.00 10.70  ? 52   ASP A CA  1 
ATOM   401  C  C   . ASP A 1 52  ? -0.590  -6.479  7.586   1.00 10.66  ? 52   ASP A C   1 
ATOM   402  O  O   . ASP A 1 52  ? -0.864  -7.634  7.889   1.00 12.00  ? 52   ASP A O   1 
ATOM   403  C  CB  . ASP A 1 52  ? 1.631   -6.906  6.516   1.00 11.87  ? 52   ASP A CB  1 
ATOM   404  C  CG  . ASP A 1 52  ? 1.198   -6.757  5.073   1.00 12.44  ? 52   ASP A CG  1 
ATOM   405  O  OD1 . ASP A 1 52  ? 0.108   -6.217  4.855   1.00 13.92  ? 52   ASP A OD1 1 
ATOM   406  O  OD2 . ASP A 1 52  ? 1.931   -7.223  4.182   1.00 16.03  ? 52   ASP A OD2 1 
ATOM   407  N  N   A ASN A 1 53  ? -1.499  -5.540  7.308   0.50 11.11  ? 53   ASN A N   1 
ATOM   408  N  N   B ASN A 1 53  ? -1.522  -5.562  7.378   0.50 11.09  ? 53   ASN A N   1 
ATOM   409  C  CA  A ASN A 1 53  ? -2.945  -5.781  7.303   0.50 13.06  ? 53   ASN A CA  1 
ATOM   410  C  CA  B ASN A 1 53  ? -2.919  -5.947  7.353   0.50 11.53  ? 53   ASN A CA  1 
ATOM   411  C  C   A ASN A 1 53  ? -3.549  -5.644  5.930   0.50 12.59  ? 53   ASN A C   1 
ATOM   412  C  C   B ASN A 1 53  ? -3.536  -5.647  5.969   0.50 12.53  ? 53   ASN A C   1 
ATOM   413  O  O   A ASN A 1 53  ? -4.757  -5.471  5.800   0.50 13.29  ? 53   ASN A O   1 
ATOM   414  O  O   B ASN A 1 53  ? -4.737  -5.403  5.869   0.50 14.38  ? 53   ASN A O   1 
ATOM   415  C  CB  A ASN A 1 53  ? -3.691  -4.781  8.171   0.50 16.10  ? 53   ASN A CB  1 
ATOM   416  C  CB  B ASN A 1 53  ? -3.724  -5.310  8.513   0.50 11.82  ? 53   ASN A CB  1 
ATOM   417  C  CG  A ASN A 1 53  ? -5.121  -5.212  8.439   0.50 18.17  ? 53   ASN A CG  1 
ATOM   418  C  CG  B ASN A 1 53  ? -3.174  -5.635  9.929   0.50 11.07  ? 53   ASN A CG  1 
ATOM   419  O  OD1 A ASN A 1 53  ? -5.350  -6.366  8.780   0.50 19.28  ? 53   ASN A OD1 1 
ATOM   420  O  OD1 B ASN A 1 53  ? -2.394  -6.591  10.163  0.50 12.01  ? 53   ASN A OD1 1 
ATOM   421  N  ND2 A ASN A 1 53  ? -6.079  -4.302  8.284   0.50 20.32  ? 53   ASN A ND2 1 
ATOM   422  N  ND2 B ASN A 1 53  ? -3.637  -4.897  10.881  0.50 11.24  ? 53   ASN A ND2 1 
ATOM   423  N  N   . THR A 1 54  ? -2.711  -5.736  4.919   1.00 12.46  ? 54   THR A N   1 
ATOM   424  C  CA  . THR A 1 54  ? -3.143  -5.436  3.550   1.00 13.14  ? 54   THR A CA  1 
ATOM   425  C  C   . THR A 1 54  ? -4.458  -6.137  3.211   1.00 13.01  ? 54   THR A C   1 
ATOM   426  O  O   . THR A 1 54  ? -5.393  -5.528  2.680   1.00 14.83  ? 54   THR A O   1 
ATOM   427  C  CB  . THR A 1 54  ? -2.039  -5.892  2.541   1.00 14.54  ? 54   THR A CB  1 
ATOM   428  O  OG1 . THR A 1 54  ? -0.870  -5.084  2.672   1.00 15.29  ? 54   THR A OG1 1 
ATOM   429  C  CG2 . THR A 1 54  ? -2.515  -5.696  1.109   1.00 15.12  ? 54   THR A CG2 1 
ATOM   430  N  N   . ALA A 1 55  ? -4.476  -7.423  3.458   1.00 13.33  ? 55   ALA A N   1 
ATOM   431  C  CA  . ALA A 1 55  ? -5.629  -8.250  3.116   1.00 15.09  ? 55   ALA A CA  1 
ATOM   432  C  C   . ALA A 1 55  ? -6.382  -8.724  4.344   1.00 15.61  ? 55   ALA A C   1 
ATOM   433  O  O   . ALA A 1 55  ? -7.031  -9.759  4.324   1.00 20.76  ? 55   ALA A O   1 
ATOM   434  C  CB  . ALA A 1 55  ? -5.183  -9.445  2.288   1.00 19.05  ? 55   ALA A CB  1 
ATOM   435  N  N   . GLY A 1 56  ? -6.280  -7.985  5.431   1.00 14.84  ? 56   GLY A N   1 
ATOM   436  C  CA  . GLY A 1 56  ? -6.813  -8.355  6.726   1.00 15.46  ? 56   GLY A CA  1 
ATOM   437  C  C   . GLY A 1 56  ? -5.794  -9.034  7.605   1.00 12.43  ? 56   GLY A C   1 
ATOM   438  O  O   . GLY A 1 56  ? -4.595  -8.985  7.354   1.00 13.34  ? 56   GLY A O   1 
ATOM   439  N  N   . CYS A 1 57  ? -6.283  -9.696  8.649   1.00 12.91  ? 57   CYS A N   1 
ATOM   440  C  CA  . CYS A 1 57  ? -5.406  -10.238 9.684   1.00 12.03  ? 57   CYS A CA  1 
ATOM   441  C  C   . CYS A 1 57  ? -4.491  -11.381 9.195   1.00 12.08  ? 57   CYS A C   1 
ATOM   442  O  O   . CYS A 1 57  ? -3.429  -11.638 9.775   1.00 12.07  ? 57   CYS A O   1 
ATOM   443  C  CB  . CYS A 1 57  ? -6.213  -10.717 10.885  1.00 13.35  ? 57   CYS A CB  1 
ATOM   444  S  SG  . CYS A 1 57  ? -7.207  -9.370  11.638  1.00 14.61  ? 57   CYS A SG  1 
ATOM   445  N  N   A THR A 1 58  ? -4.876  -12.047 8.116   0.50 12.88  ? 58   THR A N   1 
ATOM   446  N  N   B THR A 1 58  ? -4.856  -12.050 8.113   0.50 12.85  ? 58   THR A N   1 
ATOM   447  C  CA  A THR A 1 58  ? -4.068  -13.106 7.548   0.50 13.43  ? 58   THR A CA  1 
ATOM   448  C  CA  B THR A 1 58  ? -4.010  -13.098 7.576   0.50 13.15  ? 58   THR A CA  1 
ATOM   449  C  C   A THR A 1 58  ? -2.695  -12.584 7.124   0.50 12.85  ? 58   THR A C   1 
ATOM   450  C  C   B THR A 1 58  ? -2.663  -12.572 7.151   0.50 12.63  ? 58   THR A C   1 
ATOM   451  O  O   A THR A 1 58  ? -1.710  -13.325 7.191   0.50 13.60  ? 58   THR A O   1 
ATOM   452  O  O   B THR A 1 58  ? -1.668  -13.301 7.226   0.50 13.63  ? 58   THR A O   1 
ATOM   453  C  CB  A THR A 1 58  ? -4.796  -13.786 6.370   0.50 17.22  ? 58   THR A CB  1 
ATOM   454  C  CB  B THR A 1 58  ? -4.671  -13.798 6.395   0.50 16.74  ? 58   THR A CB  1 
ATOM   455  O  OG1 A THR A 1 58  ? -3.986  -14.842 5.832   0.50 19.47  ? 58   THR A OG1 1 
ATOM   456  O  OG1 B THR A 1 58  ? -5.090  -12.830 5.421   0.50 22.33  ? 58   THR A OG1 1 
ATOM   457  C  CG2 A THR A 1 58  ? -5.161  -12.759 5.275   0.50 19.36  ? 58   THR A CG2 1 
ATOM   458  C  CG2 B THR A 1 58  ? -5.857  -14.530 6.907   0.50 17.23  ? 58   THR A CG2 1 
ATOM   459  N  N   . SER A 1 59  ? -2.618  -11.327 6.690   1.00 11.77  ? 59   SER A N   1 
ATOM   460  C  CA  . SER A 1 59  ? -1.388  -10.768 6.163   1.00 11.66  ? 59   SER A CA  1 
ATOM   461  C  C   . SER A 1 59  ? -0.270  -10.657 7.240   1.00 11.60  ? 59   SER A C   1 
ATOM   462  O  O   . SER A 1 59  ? 0.883   -10.467 6.916   1.00 12.86  ? 59   SER A O   1 
ATOM   463  C  CB  . SER A 1 59  ? -1.671  -9.385  5.512   1.00 11.05  ? 59   SER A CB  1 
ATOM   464  O  OG  . SER A 1 59  ? -2.602  -9.486  4.409   1.00 13.77  ? 59   SER A OG  1 
ATOM   465  N  N   . ALA A 1 60  ? -0.642  -10.779 8.529   1.00 11.28  ? 60   ALA A N   1 
ATOM   466  C  CA  . ALA A 1 60  ? 0.289   -10.649 9.609   1.00 11.07  ? 60   ALA A CA  1 
ATOM   467  C  C   . ALA A 1 60  ? 1.254   -11.816 9.781   1.00 10.57  ? 60   ALA A C   1 
ATOM   468  O  O   . ALA A 1 60  ? 2.212   -11.731 10.545  1.00 11.10  ? 60   ALA A O   1 
ATOM   469  C  CB  . ALA A 1 60  ? -0.460  -10.381 10.912  1.00 11.52  ? 60   ALA A CB  1 
ATOM   470  N  N   . GLY A 1 61  ? 1.000   -12.929 9.110   1.00 10.43  ? 61   GLY A N   1 
ATOM   471  C  CA  . GLY A 1 61  ? 1.965   -14.022 9.188   1.00 10.93  ? 61   GLY A CA  1 
ATOM   472  C  C   . GLY A 1 61  ? 1.832   -14.797 10.482  1.00 10.11  ? 61   GLY A C   1 
ATOM   473  O  O   . GLY A 1 61  ? 0.811   -14.756 11.167  1.00 10.07  ? 61   GLY A O   1 
ATOM   474  N  N   . PRO A 1 62  ? 2.875   -15.574 10.814  1.00 10.40  ? 62   PRO A N   1 
ATOM   475  C  CA  . PRO A 1 62  ? 2.851   -16.484 11.969  1.00 10.80  ? 62   PRO A CA  1 
ATOM   476  C  C   . PRO A 1 62  ? 3.129   -15.711 13.259  1.00 9.59   ? 62   PRO A C   1 
ATOM   477  O  O   . PRO A 1 62  ? 3.368   -14.520 13.260  1.00 9.77   ? 62   PRO A O   1 
ATOM   478  C  CB  . PRO A 1 62  ? 3.965   -17.470 11.643  1.00 12.69  ? 62   PRO A CB  1 
ATOM   479  C  CG  . PRO A 1 62  ? 4.960   -16.648 10.912  1.00 13.34  ? 62   PRO A CG  1 
ATOM   480  C  CD  . PRO A 1 62  ? 4.167   -15.672 10.095  1.00 12.05  ? 62   PRO A CD  1 
ATOM   481  N  N   . HIS A 1 63  ? 3.084   -16.409 14.386  1.00 10.09  ? 63   HIS A N   1 
ATOM   482  C  CA  . HIS A 1 63  ? 3.439   -15.778 15.655  1.00 9.63   ? 63   HIS A CA  1 
ATOM   483  C  C   . HIS A 1 63  ? 4.850   -15.219 15.582  1.00 9.44   ? 63   HIS A C   1 
ATOM   484  O  O   . HIS A 1 63  ? 5.759   -15.832 14.995  1.00 10.49  ? 63   HIS A O   1 
ATOM   485  C  CB  . HIS A 1 63  ? 3.376   -16.764 16.833  1.00 10.03  ? 63   HIS A CB  1 
ATOM   486  C  CG  . HIS A 1 63  ? 2.025   -17.354 17.072  1.00 9.80   ? 63   HIS A CG  1 
ATOM   487  N  ND1 . HIS A 1 63  ? 1.814   -18.325 18.004  1.00 9.36   ? 63   HIS A ND1 1 
ATOM   488  C  CD2 . HIS A 1 63  ? 0.819   -17.083 16.472  1.00 12.13  ? 63   HIS A CD2 1 
ATOM   489  C  CE1 . HIS A 1 63  ? 0.519   -18.636 17.955  1.00 10.26  ? 63   HIS A CE1 1 
ATOM   490  N  NE2 . HIS A 1 63  ? -0.090  -17.909 17.013  1.00 11.72  ? 63   HIS A NE2 1 
ATOM   491  N  N   . PHE A 1 64  ? 5.075   -14.071 16.202  1.00 9.27   ? 64   PHE A N   1 
ATOM   492  C  CA  . PHE A 1 64  ? 6.400   -13.448 16.232  1.00 9.15   ? 64   PHE A CA  1 
ATOM   493  C  C   . PHE A 1 64  ? 7.361   -14.345 17.003  1.00 8.88   ? 64   PHE A C   1 
ATOM   494  O  O   . PHE A 1 64  ? 7.160   -14.650 18.178  1.00 9.26   ? 64   PHE A O   1 
ATOM   495  C  CB  . PHE A 1 64  ? 6.282   -12.063 16.873  1.00 9.17   ? 64   PHE A CB  1 
ATOM   496  C  CG  . PHE A 1 64  ? 7.583   -11.327 17.014  1.00 10.00  ? 64   PHE A CG  1 
ATOM   497  C  CD1 . PHE A 1 64  ? 8.509   -11.238 15.974  1.00 11.04  ? 64   PHE A CD1 1 
ATOM   498  C  CD2 . PHE A 1 64  ? 7.885   -10.685 18.219  1.00 10.98  ? 64   PHE A CD2 1 
ATOM   499  C  CE1 . PHE A 1 64  ? 9.696   -10.539 16.157  1.00 12.59  ? 64   PHE A CE1 1 
ATOM   500  C  CE2 . PHE A 1 64  ? 9.060   -9.956  18.361  1.00 12.42  ? 64   PHE A CE2 1 
ATOM   501  C  CZ  . PHE A 1 64  ? 9.969   -9.890  17.341  1.00 13.33  ? 64   PHE A CZ  1 
ATOM   502  N  N   . ASN A 1 65  ? 8.404   -14.792 16.308  1.00 10.26  ? 65   ASN A N   1 
ATOM   503  C  CA  . ASN A 1 65  ? 9.263   -15.878 16.802  1.00 10.45  ? 65   ASN A CA  1 
ATOM   504  C  C   . ASN A 1 65  ? 10.725  -15.615 16.416  1.00 11.21  ? 65   ASN A C   1 
ATOM   505  O  O   . ASN A 1 65  ? 11.342  -16.423 15.705  1.00 12.79  ? 65   ASN A O   1 
ATOM   506  C  CB  . ASN A 1 65  ? 8.772   -17.196 16.245  1.00 11.17  ? 65   ASN A CB  1 
ATOM   507  C  CG  . ASN A 1 65  ? 9.510   -18.402 16.808  1.00 11.68  ? 65   ASN A CG  1 
ATOM   508  O  OD1 . ASN A 1 65  ? 10.078  -18.359 17.912  1.00 11.83  ? 65   ASN A OD1 1 
ATOM   509  N  ND2 . ASN A 1 65  ? 9.447   -19.507 16.085  1.00 13.80  ? 65   ASN A ND2 1 
ATOM   510  N  N   . PRO A 1 66  ? 11.315  -14.501 16.884  1.00 11.13  ? 66   PRO A N   1 
ATOM   511  C  CA  . PRO A 1 66  ? 12.675  -14.165 16.458  1.00 12.53  ? 66   PRO A CA  1 
ATOM   512  C  C   . PRO A 1 66  ? 13.713  -15.176 16.931  1.00 13.17  ? 66   PRO A C   1 
ATOM   513  O  O   . PRO A 1 66  ? 14.798  -15.231 16.360  1.00 15.03  ? 66   PRO A O   1 
ATOM   514  C  CB  . PRO A 1 66  ? 12.892  -12.776 17.068  1.00 12.93  ? 66   PRO A CB  1 
ATOM   515  C  CG  . PRO A 1 66  ? 11.998  -12.763 18.283  1.00 11.84  ? 66   PRO A CG  1 
ATOM   516  C  CD  . PRO A 1 66  ? 10.764  -13.515 17.838  1.00 10.67  ? 66   PRO A CD  1 
ATOM   517  N  N   . LEU A 1 67  ? 13.410  -15.933 17.983  1.00 12.27  ? 67   LEU A N   1 
ATOM   518  C  CA  . LEU A 1 67  ? 14.344  -16.885 18.570  1.00 12.82  ? 67   LEU A CA  1 
ATOM   519  C  C   . LEU A 1 67  ? 14.091  -18.320 18.123  1.00 12.90  ? 67   LEU A C   1 
ATOM   520  O  O   . LEU A 1 67  ? 14.760  -19.246 18.631  1.00 14.49  ? 67   LEU A O   1 
ATOM   521  C  CB  . LEU A 1 67  ? 14.338  -16.746 20.098  1.00 13.99  ? 67   LEU A CB  1 
ATOM   522  C  CG  . LEU A 1 67  ? 14.779  -15.368 20.585  1.00 14.95  ? 67   LEU A CG  1 
ATOM   523  C  CD1 . LEU A 1 67  ? 14.450  -15.161 22.048  1.00 16.93  ? 67   LEU A CD1 1 
ATOM   524  C  CD2 . LEU A 1 67  ? 16.264  -15.187 20.377  1.00 20.63  ? 67   LEU A CD2 1 
ATOM   525  N  N   . SER A 1 68  ? 13.202  -18.545 17.158  1.00 13.77  ? 68   SER A N   1 
ATOM   526  C  CA  . SER A 1 68  ? 13.026  -19.888 16.567  1.00 14.65  ? 68   SER A CA  1 
ATOM   527  C  C   . SER A 1 68  ? 12.746  -20.963 17.604  1.00 14.65  ? 68   SER A C   1 
ATOM   528  O  O   . SER A 1 68  ? 13.384  -22.007 17.629  1.00 17.61  ? 68   SER A O   1 
ATOM   529  C  CB  . SER A 1 68  ? 14.240  -20.275 15.705  1.00 17.16  ? 68   SER A CB  1 
ATOM   530  O  OG  . SER A 1 68  ? 14.389  -19.357 14.639  1.00 18.09  ? 68   SER A OG  1 
ATOM   531  N  N   . ARG A 1 69  ? 11.782  -20.674 18.461  1.00 13.49  ? 69   ARG A N   1 
ATOM   532  C  CA  . ARG A 1 69  ? 11.295  -21.623 19.459  1.00 13.41  ? 69   ARG A CA  1 
ATOM   533  C  C   . ARG A 1 69  ? 9.959   -22.215 19.034  1.00 13.34  ? 69   ARG A C   1 
ATOM   534  O  O   . ARG A 1 69  ? 9.336   -21.751 18.067  1.00 13.91  ? 69   ARG A O   1 
ATOM   535  C  CB  . ARG A 1 69  ? 11.141  -20.933 20.826  1.00 14.24  ? 69   ARG A CB  1 
ATOM   536  C  CG  . ARG A 1 69  ? 12.340  -20.177 21.326  1.00 17.44  ? 69   ARG A CG  1 
ATOM   537  C  CD  . ARG A 1 69  ? 13.543  -21.041 21.428  1.00 19.72  ? 69   ARG A CD  1 
ATOM   538  N  NE  . ARG A 1 69  ? 13.336  -22.164 22.338  1.00 22.37  ? 69   ARG A NE  1 
ATOM   539  C  CZ  . ARG A 1 69  ? 13.400  -22.094 23.673  0.80 20.34  ? 69   ARG A CZ  1 
ATOM   540  N  NH1 . ARG A 1 69  ? 13.629  -20.939 24.295  0.80 25.96  ? 69   ARG A NH1 1 
ATOM   541  N  NH2 . ARG A 1 69  ? 13.208  -23.200 24.394  0.80 24.33  ? 69   ARG A NH2 1 
ATOM   542  N  N   . LYS A 1 70  ? 9.517   -23.210 19.778  1.00 13.71  ? 70   LYS A N   1 
ATOM   543  C  CA  . LYS A 1 70  ? 8.167   -23.764 19.624  1.00 12.91  ? 70   LYS A CA  1 
ATOM   544  C  C   . LYS A 1 70  ? 7.154   -22.900 20.383  1.00 11.64  ? 70   LYS A C   1 
ATOM   545  O  O   . LYS A 1 70  ? 7.500   -22.139 21.285  1.00 12.37  ? 70   LYS A O   1 
ATOM   546  C  CB  . LYS A 1 70  ? 8.094   -25.215 20.127  1.00 15.24  ? 70   LYS A CB  1 
ATOM   547  C  CG  . LYS A 1 70  ? 8.955   -26.174 19.312  1.00 18.57  ? 70   LYS A CG  1 
ATOM   548  C  CD  . LYS A 1 70  ? 8.930   -27.580 19.841  1.00 22.90  ? 70   LYS A CD  1 
ATOM   549  C  CE  . LYS A 1 70  ? 9.880   -27.753 21.018  0.50 28.16  ? 70   LYS A CE  1 
ATOM   550  N  NZ  . LYS A 1 70  ? 9.986   -29.179 21.451  0.50 34.33  ? 70   LYS A NZ  1 
ATOM   551  N  N   . HIS A 1 71  ? 5.895   -23.063 19.984  1.00 10.81  ? 71   HIS A N   1 
ATOM   552  C  CA  . HIS A 1 71  ? 4.781   -22.380 20.634  1.00 10.35  ? 71   HIS A CA  1 
ATOM   553  C  C   . HIS A 1 71  ? 4.591   -22.837 22.058  1.00 10.45  ? 71   HIS A C   1 
ATOM   554  O  O   . HIS A 1 71  ? 4.682   -24.026 22.356  1.00 11.90  ? 71   HIS A O   1 
ATOM   555  C  CB  . HIS A 1 71  ? 3.511   -22.626 19.821  1.00 10.38  ? 71   HIS A CB  1 
ATOM   556  C  CG  . HIS A 1 71  ? 2.316   -21.926 20.363  1.00 9.80   ? 71   HIS A CG  1 
ATOM   557  N  ND1 . HIS A 1 71  ? 2.106   -20.564 20.243  1.00 9.30   ? 71   HIS A ND1 1 
ATOM   558  C  CD2 . HIS A 1 71  ? 1.287   -22.438 21.127  1.00 10.11  ? 71   HIS A CD2 1 
ATOM   559  C  CE1 . HIS A 1 71  ? 0.992   -20.292 20.926  1.00 9.42   ? 71   HIS A CE1 1 
ATOM   560  N  NE2 . HIS A 1 71  ? 0.482   -21.414 21.444  1.00 10.00  ? 71   HIS A NE2 1 
ATOM   561  N  N   . GLY A 1 72  ? 4.264   -21.901 22.946  1.00 9.97   ? 72   GLY A N   1 
ATOM   562  C  CA  . GLY A 1 72  ? 3.922   -22.201 24.312  1.00 10.15  ? 72   GLY A CA  1 
ATOM   563  C  C   . GLY A 1 72  ? 3.025   -21.140 24.895  1.00 9.90   ? 72   GLY A C   1 
ATOM   564  O  O   . GLY A 1 72  ? 2.472   -20.291 24.176  1.00 10.82  ? 72   GLY A O   1 
ATOM   565  N  N   . GLY A 1 73  ? 2.879   -21.209 26.206  1.00 10.39  ? 73   GLY A N   1 
ATOM   566  C  CA  . GLY A 1 73  ? 2.180   -20.182 26.950  1.00 10.43  ? 73   GLY A CA  1 
ATOM   567  C  C   . GLY A 1 73  ? 3.135   -19.114 27.450  1.00 9.38   ? 73   GLY A C   1 
ATOM   568  O  O   . GLY A 1 73  ? 4.355   -19.268 27.436  1.00 10.16  ? 73   GLY A O   1 
ATOM   569  N  N   . PRO A 1 74  ? 2.564   -18.015 27.932  1.00 9.56   ? 74   PRO A N   1 
ATOM   570  C  CA  . PRO A 1 74  ? 3.399   -16.880 28.329  1.00 10.00  ? 74   PRO A CA  1 
ATOM   571  C  C   . PRO A 1 74  ? 4.284   -17.175 29.521  1.00 10.73  ? 74   PRO A C   1 
ATOM   572  O  O   . PRO A 1 74  ? 5.322   -16.542 29.670  1.00 13.31  ? 74   PRO A O   1 
ATOM   573  C  CB  . PRO A 1 74  ? 2.366   -15.781 28.640  1.00 10.87  ? 74   PRO A CB  1 
ATOM   574  C  CG  . PRO A 1 74  ? 1.076   -16.508 28.878  1.00 11.15  ? 74   PRO A CG  1 
ATOM   575  C  CD  . PRO A 1 74  ? 1.132   -17.687 27.958  1.00 10.15  ? 74   PRO A CD  1 
ATOM   576  N  N   . LYS A 1 75  ? 3.915   -18.153 30.346  1.00 10.38  ? 75   LYS A N   1 
ATOM   577  C  CA  . LYS A 1 75  ? 4.720   -18.511 31.496  1.00 11.62  ? 75   LYS A CA  1 
ATOM   578  C  C   . LYS A 1 75  ? 5.578   -19.752 31.269  1.00 11.51  ? 75   LYS A C   1 
ATOM   579  O  O   . LYS A 1 75  ? 6.087   -20.343 32.204  1.00 14.61  ? 75   LYS A O   1 
ATOM   580  C  CB  . LYS A 1 75  ? 3.857   -18.550 32.744  1.00 14.20  ? 75   LYS A CB  1 
ATOM   581  C  CG  . LYS A 1 75  ? 3.085   -17.242 33.006  1.00 14.98  ? 75   LYS A CG  1 
ATOM   582  C  CD  . LYS A 1 75  ? 3.937   -15.968 33.061  1.00 15.20  ? 75   LYS A CD  1 
ATOM   583  C  CE  . LYS A 1 75  ? 3.104   -14.737 33.343  1.00 17.87  ? 75   LYS A CE  1 
ATOM   584  N  NZ  . LYS A 1 75  ? 3.896   -13.480 33.430  1.00 19.17  ? 75   LYS A NZ  1 
ATOM   585  N  N   . ASP A 1 76  ? 5.783   -20.117 30.020  1.00 11.21  ? 76   ASP A N   1 
ATOM   586  C  CA  . ASP A 1 76  ? 6.698   -21.190 29.633  1.00 11.90  ? 76   ASP A CA  1 
ATOM   587  C  C   . ASP A 1 76  ? 8.015   -20.618 29.140  1.00 11.72  ? 76   ASP A C   1 
ATOM   588  O  O   . ASP A 1 76  ? 8.068   -19.574 28.511  1.00 12.67  ? 76   ASP A O   1 
ATOM   589  C  CB  . ASP A 1 76  ? 6.083   -22.009 28.505  1.00 11.93  ? 76   ASP A CB  1 
ATOM   590  C  CG  . ASP A 1 76  ? 4.821   -22.745 28.927  1.00 13.77  ? 76   ASP A CG  1 
ATOM   591  O  OD1 . ASP A 1 76  ? 4.640   -23.039 30.139  1.00 17.04  ? 76   ASP A OD1 1 
ATOM   592  O  OD2 . ASP A 1 76  ? 4.006   -23.062 28.026  1.00 14.45  ? 76   ASP A OD2 1 
ATOM   593  N  N   A GLU A 1 77  ? 9.088   -21.364 29.372  0.50 11.58  ? 77   GLU A N   1 
ATOM   594  N  N   B GLU A 1 77  ? 9.090   -21.353 29.380  0.50 11.57  ? 77   GLU A N   1 
ATOM   595  C  CA  A GLU A 1 77  ? 10.365  -21.017 28.780  0.50 12.13  ? 77   GLU A CA  1 
ATOM   596  C  CA  B GLU A 1 77  ? 10.369  -21.003 28.796  0.50 12.29  ? 77   GLU A CA  1 
ATOM   597  C  C   A GLU A 1 77  ? 10.353  -21.214 27.256  0.50 11.81  ? 77   GLU A C   1 
ATOM   598  C  C   B GLU A 1 77  ? 10.328  -21.208 27.281  0.50 11.91  ? 77   GLU A C   1 
ATOM   599  O  O   A GLU A 1 77  ? 10.820  -20.354 26.506  0.50 12.91  ? 77   GLU A O   1 
ATOM   600  O  O   B GLU A 1 77  ? 10.848  -20.404 26.503  0.50 13.30  ? 77   GLU A O   1 
ATOM   601  C  CB  A GLU A 1 77  ? 11.478  -21.851 29.422  0.50 13.62  ? 77   GLU A CB  1 
ATOM   602  C  CB  B GLU A 1 77  ? 11.445  -21.886 29.422  0.50 14.01  ? 77   GLU A CB  1 
ATOM   603  C  CG  A GLU A 1 77  ? 12.864  -21.415 29.017  0.50 15.69  ? 77   GLU A CG  1 
ATOM   604  C  CG  B GLU A 1 77  ? 12.860  -21.514 29.070  0.50 16.71  ? 77   GLU A CG  1 
ATOM   605  C  CD  A GLU A 1 77  ? 13.978  -22.067 29.823  0.50 17.14  ? 77   GLU A CD  1 
ATOM   606  C  CD  B GLU A 1 77  ? 13.301  -22.051 27.720  0.50 17.92  ? 77   GLU A CD  1 
ATOM   607  O  OE1 A GLU A 1 77  ? 13.921  -23.265 30.173  0.50 21.07  ? 77   GLU A OE1 1 
ATOM   608  O  OE1 B GLU A 1 77  ? 12.829  -23.123 27.279  0.50 19.46  ? 77   GLU A OE1 1 
ATOM   609  O  OE2 A GLU A 1 77  ? 14.957  -21.369 30.107  0.50 17.33  ? 77   GLU A OE2 1 
ATOM   610  O  OE2 B GLU A 1 77  ? 14.146  -21.393 27.089  0.50 20.31  ? 77   GLU A OE2 1 
ATOM   611  N  N   A GLU A 1 78  ? 9.833   -22.354 26.795  0.50 11.19  ? 78   GLU A N   1 
ATOM   612  N  N   B GLU A 1 78  ? 9.696   -22.308 26.881  0.50 11.91  ? 78   GLU A N   1 
ATOM   613  C  CA  A GLU A 1 78  ? 9.709   -22.621 25.372  0.50 10.81  ? 78   GLU A CA  1 
ATOM   614  C  CA  B GLU A 1 78  ? 9.547   -22.699 25.502  0.50 12.71  ? 78   GLU A CA  1 
ATOM   615  C  C   A GLU A 1 78  ? 8.407   -22.002 24.878  0.50 10.67  ? 78   GLU A C   1 
ATOM   616  C  C   B GLU A 1 78  ? 8.336   -21.998 24.891  0.50 11.57  ? 78   GLU A C   1 
ATOM   617  O  O   A GLU A 1 78  ? 7.323   -22.523 25.101  0.50 12.10  ? 78   GLU A O   1 
ATOM   618  O  O   B GLU A 1 78  ? 7.218   -22.469 25.027  0.50 12.00  ? 78   GLU A O   1 
ATOM   619  C  CB  A GLU A 1 78  ? 9.699   -24.128 25.115  0.50 10.03  ? 78   GLU A CB  1 
ATOM   620  C  CB  B GLU A 1 78  ? 9.335   -24.217 25.483  0.50 14.98  ? 78   GLU A CB  1 
ATOM   621  C  CG  A GLU A 1 78  ? 9.651   -24.473 23.652  0.50 11.96  ? 78   GLU A CG  1 
ATOM   622  C  CG  B GLU A 1 78  ? 10.279  -25.007 26.395  0.50 22.63  ? 78   GLU A CG  1 
ATOM   623  C  CD  A GLU A 1 78  ? 11.027  -24.483 23.060  0.50 17.32  ? 78   GLU A CD  1 
ATOM   624  C  CD  B GLU A 1 78  ? 9.968   -25.038 27.907  0.50 21.72  ? 78   GLU A CD  1 
ATOM   625  O  OE1 A GLU A 1 78  ? 11.960  -24.748 23.832  0.50 24.77  ? 78   GLU A OE1 1 
ATOM   626  O  OE1 B GLU A 1 78  ? 8.886   -24.591 28.449  0.50 13.76  ? 78   GLU A OE1 1 
ATOM   627  O  OE2 A GLU A 1 78  ? 11.199  -24.287 21.838  0.50 19.01  ? 78   GLU A OE2 1 
ATOM   628  O  OE2 B GLU A 1 78  ? 10.886  -25.581 28.570  0.50 26.85  ? 78   GLU A OE2 1 
ATOM   629  N  N   . ARG A 1 79  ? 8.553   -20.852 24.256  1.00 10.62  ? 79   ARG A N   1 
ATOM   630  C  CA  . ARG A 1 79  ? 7.458   -20.063 23.695  1.00 9.80   ? 79   ARG A CA  1 
ATOM   631  C  C   . ARG A 1 79  ? 8.026   -19.200 22.587  1.00 9.70   ? 79   ARG A C   1 
ATOM   632  O  O   . ARG A 1 79  ? 9.219   -18.916 22.551  1.00 10.53  ? 79   ARG A O   1 
ATOM   633  C  CB  . ARG A 1 79  ? 6.802   -19.176 24.765  1.00 9.68   ? 79   ARG A CB  1 
ATOM   634  C  CG  . ARG A 1 79  ? 7.766   -18.208 25.427  1.00 9.77   ? 79   ARG A CG  1 
ATOM   635  C  CD  . ARG A 1 79  ? 7.065   -17.211 26.333  1.00 9.62   ? 79   ARG A CD  1 
ATOM   636  N  NE  . ARG A 1 79  ? 6.576   -16.043 25.579  1.00 9.21   ? 79   ARG A NE  1 
ATOM   637  C  CZ  . ARG A 1 79  ? 6.118   -14.940 26.159  1.00 8.90   ? 79   ARG A CZ  1 
ATOM   638  N  NH1 . ARG A 1 79  ? 5.996   -14.874 27.475  1.00 9.58   ? 79   ARG A NH1 1 
ATOM   639  N  NH2 . ARG A 1 79  ? 5.799   -13.871 25.449  1.00 9.08   ? 79   ARG A NH2 1 
ATOM   640  N  N   . HIS A 1 80  ? 7.130   -18.735 21.732  1.00 9.27   ? 80   HIS A N   1 
ATOM   641  C  CA  . HIS A 1 80  ? 7.423   -17.636 20.821  1.00 9.33   ? 80   HIS A CA  1 
ATOM   642  C  C   . HIS A 1 80  ? 7.435   -16.328 21.620  1.00 9.00   ? 80   HIS A C   1 
ATOM   643  O  O   . HIS A 1 80  ? 6.654   -16.176 22.574  1.00 8.94   ? 80   HIS A O   1 
ATOM   644  C  CB  . HIS A 1 80  ? 6.323   -17.554 19.750  1.00 9.17   ? 80   HIS A CB  1 
ATOM   645  C  CG  . HIS A 1 80  ? 6.154   -18.818 18.975  1.00 9.62   ? 80   HIS A CG  1 
ATOM   646  N  ND1 . HIS A 1 80  ? 4.935   -19.299 18.558  1.00 9.83   ? 80   HIS A ND1 1 
ATOM   647  C  CD2 . HIS A 1 80  ? 7.106   -19.670 18.475  1.00 10.96  ? 80   HIS A CD2 1 
ATOM   648  C  CE1 . HIS A 1 80  ? 5.150   -20.369 17.786  1.00 10.35  ? 80   HIS A CE1 1 
ATOM   649  N  NE2 . HIS A 1 80  ? 6.458   -20.598 17.740  1.00 11.40  ? 80   HIS A NE2 1 
ATOM   650  N  N   . VAL A 1 81  ? 8.201   -15.335 21.181  1.00 8.95   ? 81   VAL A N   1 
ATOM   651  C  CA  . VAL A 1 81  ? 8.114   -14.031 21.827  1.00 9.07   ? 81   VAL A CA  1 
ATOM   652  C  C   . VAL A 1 81  ? 6.664   -13.540 21.808  1.00 8.76   ? 81   VAL A C   1 
ATOM   653  O  O   . VAL A 1 81  ? 6.213   -12.946 22.788  1.00 9.25   ? 81   VAL A O   1 
ATOM   654  C  CB  . VAL A 1 81  ? 9.096   -12.999 21.195  1.00 9.66   ? 81   VAL A CB  1 
ATOM   655  C  CG1 . VAL A 1 81  ? 8.820   -11.601 21.738  1.00 10.33  ? 81   VAL A CG1 1 
ATOM   656  C  CG2 . VAL A 1 81  ? 10.531  -13.419 21.514  1.00 10.75  ? 81   VAL A CG2 1 
ATOM   657  N  N   . GLY A 1 82  ? 5.944   -13.757 20.709  1.00 8.77   ? 82   GLY A N   1 
ATOM   658  C  CA  . GLY A 1 82  ? 4.576   -13.258 20.628  1.00 8.80   ? 82   GLY A CA  1 
ATOM   659  C  C   . GLY A 1 82  ? 3.514   -14.015 21.407  1.00 8.96   ? 82   GLY A C   1 
ATOM   660  O  O   . GLY A 1 82  ? 2.336   -13.645 21.290  1.00 9.53   ? 82   GLY A O   1 
ATOM   661  N  N   . ASP A 1 83  ? 3.878   -15.032 22.177  1.00 8.37   ? 83   ASP A N   1 
ATOM   662  C  CA  . ASP A 1 83  ? 2.884   -15.898 22.841  1.00 8.66   ? 83   ASP A CA  1 
ATOM   663  C  C   . ASP A 1 83  ? 2.367   -15.287 24.148  1.00 8.87   ? 83   ASP A C   1 
ATOM   664  O  O   . ASP A 1 83  ? 2.941   -15.493 25.209  1.00 11.21  ? 83   ASP A O   1 
ATOM   665  C  CB  . ASP A 1 83  ? 3.489   -17.255 23.100  1.00 8.85   ? 83   ASP A CB  1 
ATOM   666  C  CG  . ASP A 1 83  ? 3.645   -18.089 21.851  1.00 8.78   ? 83   ASP A CG  1 
ATOM   667  O  OD1 . ASP A 1 83  ? 3.033   -17.707 20.807  1.00 9.18   ? 83   ASP A OD1 1 
ATOM   668  O  OD2 . ASP A 1 83  ? 4.372   -19.119 21.896  1.00 9.52   ? 83   ASP A OD2 1 
ATOM   669  N  N   . LEU A 1 84  ? 1.221   -14.592 24.066  1.00 8.37   ? 84   LEU A N   1 
ATOM   670  C  CA  . LEU A 1 84  ? 0.598   -13.945 25.215  1.00 8.58   ? 84   LEU A CA  1 
ATOM   671  C  C   . LEU A 1 84  ? -0.589  -14.759 25.734  1.00 8.95   ? 84   LEU A C   1 
ATOM   672  O  O   . LEU A 1 84  ? -1.360  -14.256 26.568  1.00 10.59  ? 84   LEU A O   1 
ATOM   673  C  CB  . LEU A 1 84  ? 0.217   -12.508 24.915  1.00 8.72   ? 84   LEU A CB  1 
ATOM   674  C  CG  . LEU A 1 84  ? 1.428   -11.607 24.615  1.00 9.39   ? 84   LEU A CG  1 
ATOM   675  C  CD1 . LEU A 1 84  ? 0.921   -10.218 24.228  1.00 11.11  ? 84   LEU A CD1 1 
ATOM   676  C  CD2 . LEU A 1 84  ? 2.388   -11.537 25.795  1.00 11.32  ? 84   LEU A CD2 1 
ATOM   677  N  N   . GLY A 1 85  ? -0.730  -16.006 25.332  1.00 8.59   ? 85   GLY A N   1 
ATOM   678  C  CA  . GLY A 1 85  ? -1.707  -16.896 25.937  1.00 9.03   ? 85   GLY A CA  1 
ATOM   679  C  C   . GLY A 1 85  ? -3.105  -16.666 25.428  1.00 8.82   ? 85   GLY A C   1 
ATOM   680  O  O   . GLY A 1 85  ? -3.350  -16.670 24.231  1.00 10.20  ? 85   GLY A O   1 
ATOM   681  N  N   . ASN A 1 86  ? -4.040  -16.517 26.363  1.00 9.09   ? 86   ASN A N   1 
ATOM   682  C  CA  . ASN A 1 86  ? -5.436  -16.305 26.066  1.00 9.45   ? 86   ASN A CA  1 
ATOM   683  C  C   . ASN A 1 86  ? -5.954  -15.093 26.804  1.00 9.47   ? 86   ASN A C   1 
ATOM   684  O  O   . ASN A 1 86  ? -5.537  -14.811 27.935  1.00 11.62  ? 86   ASN A O   1 
ATOM   685  C  CB  . ASN A 1 86  ? -6.292  -17.493 26.550  1.00 9.73   ? 86   ASN A CB  1 
ATOM   686  C  CG  . ASN A 1 86  ? -6.043  -18.724 25.740  1.00 9.69   ? 86   ASN A CG  1 
ATOM   687  O  OD1 . ASN A 1 86  ? -6.495  -18.809 24.607  1.00 10.31  ? 86   ASN A OD1 1 
ATOM   688  N  ND2 . ASN A 1 86  ? -5.332  -19.683 26.320  1.00 11.88  ? 86   ASN A ND2 1 
ATOM   689  N  N   . VAL A 1 87  ? -6.935  -14.437 26.193  1.00 9.05   ? 87   VAL A N   1 
ATOM   690  C  CA  . VAL A 1 87  ? -7.836  -13.528 26.919  1.00 9.20   ? 87   VAL A CA  1 
ATOM   691  C  C   . VAL A 1 87  ? -9.145  -14.282 27.142  1.00 9.05   ? 87   VAL A C   1 
ATOM   692  O  O   . VAL A 1 87  ? -9.464  -15.238 26.438  1.00 10.47  ? 87   VAL A O   1 
ATOM   693  C  CB  . VAL A 1 87  ? -8.037  -12.209 26.190  1.00 10.64  ? 87   VAL A CB  1 
ATOM   694  C  CG1 . VAL A 1 87  ? -6.690  -11.496 26.053  1.00 14.06  ? 87   VAL A CG1 1 
ATOM   695  C  CG2 . VAL A 1 87  ? -8.726  -12.409 24.852  1.00 13.04  ? 87   VAL A CG2 1 
ATOM   696  N  N   . THR A 1 88  ? -9.896  -13.860 28.145  1.00 10.33  ? 88   THR A N   1 
ATOM   697  C  CA  . THR A 1 88  ? -11.142 -14.529 28.525  1.00 11.69  ? 88   THR A CA  1 
ATOM   698  C  C   . THR A 1 88  ? -12.303 -13.547 28.440  1.00 11.24  ? 88   THR A C   1 
ATOM   699  O  O   . THR A 1 88  ? -12.332 -12.495 29.087  1.00 14.49  ? 88   THR A O   1 
ATOM   700  C  CB  . THR A 1 88  ? -11.061 -15.091 29.924  1.00 17.25  ? 88   THR A CB  1 
ATOM   701  O  OG1 . THR A 1 88  ? -9.995  -16.029 29.974  1.00 20.92  ? 88   THR A OG1 1 
ATOM   702  C  CG2 . THR A 1 88  ? -12.363 -15.805 30.311  1.00 21.80  ? 88   THR A CG2 1 
ATOM   703  N  N   . ALA A 1 89  ? -13.298 -13.931 27.640  1.00 11.09  ? 89   ALA A N   1 
ATOM   704  C  CA  . ALA A 1 89  ? -14.533 -13.160 27.525  1.00 11.29  ? 89   ALA A CA  1 
ATOM   705  C  C   . ALA A 1 89  ? -15.585 -13.784 28.452  1.00 11.19  ? 89   ALA A C   1 
ATOM   706  O  O   . ALA A 1 89  ? -15.704 -15.027 28.529  1.00 11.42  ? 89   ALA A O   1 
ATOM   707  C  CB  . ALA A 1 89  ? -15.038 -13.152 26.113  1.00 12.22  ? 89   ALA A CB  1 
ATOM   708  N  N   . ASP A 1 90  ? -16.352 -12.919 29.096  1.00 10.99  ? 90   ASP A N   1 
ATOM   709  C  CA  . ASP A 1 90  ? -17.490 -13.350 29.894  1.00 11.03  ? 90   ASP A CA  1 
ATOM   710  C  C   . ASP A 1 90  ? -18.760 -13.361 29.056  0.70 8.78   ? 90   ASP A C   1 
ATOM   711  O  O   . ASP A 1 90  ? -18.711 -13.223 27.831  1.00 10.95  ? 90   ASP A O   1 
ATOM   712  C  CB  . ASP A 1 90  ? -17.606 -12.485 31.144  1.00 12.41  ? 90   ASP A CB  1 
ATOM   713  C  CG  . ASP A 1 90  ? -16.659 -12.904 32.225  1.00 14.21  ? 90   ASP A CG  1 
ATOM   714  O  OD1 . ASP A 1 90  ? -15.596 -13.472 31.890  0.70 14.55  ? 90   ASP A OD1 1 
ATOM   715  O  OD2 . ASP A 1 90  ? -16.883 -12.697 33.417  0.70 15.81  ? 90   ASP A OD2 1 
ATOM   716  N  N   . LYS A 1 91  ? -19.913 -13.552 29.713  1.00 11.45  ? 91   LYS A N   1 
ATOM   717  C  CA  . LYS A 1 91  ? -21.181 -13.600 28.998  1.00 11.17  ? 91   LYS A CA  1 
ATOM   718  C  C   . LYS A 1 91  ? -21.621 -12.240 28.430  1.00 11.59  ? 91   LYS A C   1 
ATOM   719  O  O   . LYS A 1 91  ? -22.636 -12.149 27.722  1.00 13.55  ? 91   LYS A O   1 
ATOM   720  C  CB  . LYS A 1 91  ? -22.278 -14.205 29.878  1.00 10.92  ? 91   LYS A CB  1 
ATOM   721  C  CG  . LYS A 1 91  ? -22.212 -15.707 30.079  1.00 13.07  ? 91   LYS A CG  1 
ATOM   722  C  CD  . LYS A 1 91  ? -22.436 -16.483 28.806  1.00 16.57  ? 91   LYS A CD  1 
ATOM   723  C  CE  . LYS A 1 91  ? -23.690 -17.274 28.729  1.00 21.89  ? 91   LYS A CE  1 
ATOM   724  N  NZ  . LYS A 1 91  ? -23.825 -17.706 27.312  1.00 21.95  ? 91   LYS A NZ  1 
ATOM   725  N  N   . ASP A 1 92  ? -20.929 -11.176 28.762  1.00 12.08  ? 92   ASP A N   1 
ATOM   726  C  CA  . ASP A 1 92  ? -21.107 -9.907  28.085  1.00 12.56  ? 92   ASP A CA  1 
ATOM   727  C  C   . ASP A 1 92  ? -20.360 -9.875  26.734  1.00 12.17  ? 92   ASP A C   1 
ATOM   728  O  O   . ASP A 1 92  ? -20.481 -8.889  26.006  1.00 14.01  ? 92   ASP A O   1 
ATOM   729  C  CB  . ASP A 1 92  ? -20.659 -8.732  28.986  1.00 13.32  ? 92   ASP A CB  1 
ATOM   730  C  CG  . ASP A 1 92  ? -19.218 -8.843  29.481  1.00 13.85  ? 92   ASP A CG  1 
ATOM   731  O  OD1 . ASP A 1 92  ? -18.570 -9.906  29.267  1.00 13.25  ? 92   ASP A OD1 1 
ATOM   732  O  OD2 . ASP A 1 92  ? -18.810 -7.834  30.105  1.00 15.71  ? 92   ASP A OD2 1 
ATOM   733  N  N   . GLY A 1 93  ? -19.567 -10.907 26.418  1.00 11.05  ? 93   GLY A N   1 
ATOM   734  C  CA  . GLY A 1 93  ? -18.725 -10.902 25.241  1.00 11.21  ? 93   GLY A CA  1 
ATOM   735  C  C   . GLY A 1 93  ? -17.508 -10.025 25.334  1.00 10.77  ? 93   GLY A C   1 
ATOM   736  O  O   . GLY A 1 93  ? -16.855 -9.760  24.332  1.00 11.35  ? 93   GLY A O   1 
ATOM   737  N  N   . VAL A 1 94  ? -17.180 -9.617  26.548  1.00 10.80  ? 94   VAL A N   1 
ATOM   738  C  CA  . VAL A 1 94  ? -16.063 -8.682  26.807  1.00 11.18  ? 94   VAL A CA  1 
ATOM   739  C  C   . VAL A 1 94  ? -14.946 -9.408  27.550  1.00 10.94  ? 94   VAL A C   1 
ATOM   740  O  O   . VAL A 1 94  ? -15.177 -10.098 28.551  1.00 11.39  ? 94   VAL A O   1 
ATOM   741  C  CB  . VAL A 1 94  ? -16.514 -7.455  27.626  1.00 13.44  ? 94   VAL A CB  1 
ATOM   742  C  CG1 . VAL A 1 94  ? -15.321 -6.536  27.960  1.00 15.67  ? 94   VAL A CG1 1 
ATOM   743  C  CG2 . VAL A 1 94  ? -17.606 -6.673  26.883  1.00 15.30  ? 94   VAL A CG2 1 
ATOM   744  N  N   . ALA A 1 95  ? -13.727 -9.218  27.059  1.00 10.80  ? 95   ALA A N   1 
ATOM   745  C  CA  . ALA A 1 95  ? -12.514 -9.617  27.744  1.00 11.79  ? 95   ALA A CA  1 
ATOM   746  C  C   . ALA A 1 95  ? -11.863 -8.373  28.311  1.00 12.15  ? 95   ALA A C   1 
ATOM   747  O  O   . ALA A 1 95  ? -11.519 -7.455  27.584  1.00 16.19  ? 95   ALA A O   1 
ATOM   748  C  CB  . ALA A 1 95  ? -11.555 -10.336 26.794  1.00 13.60  ? 95   ALA A CB  1 
ATOM   749  N  N   . ASP A 1 96  ? -11.691 -8.359  29.621  1.00 12.29  ? 96   ASP A N   1 
ATOM   750  C  CA  . ASP A 1 96  ? -10.964 -7.332  30.324  1.00 13.62  ? 96   ASP A CA  1 
ATOM   751  C  C   . ASP A 1 96  ? -9.531  -7.825  30.432  1.00 14.53  ? 96   ASP A C   1 
ATOM   752  O  O   . ASP A 1 96  ? -9.251  -8.812  31.084  1.00 23.28  ? 96   ASP A O   1 
ATOM   753  C  CB  . ASP A 1 96  ? -11.684 -7.076  31.651  1.00 16.98  ? 96   ASP A CB  1 
ATOM   754  C  CG  . ASP A 1 96  ? -12.648 -5.849  31.554  0.50 24.42  ? 96   ASP A CG  1 
ATOM   755  O  OD1 . ASP A 1 96  ? -12.799 -5.215  30.454  0.50 22.55  ? 96   ASP A OD1 1 
ATOM   756  O  OD2 . ASP A 1 96  ? -13.251 -5.503  32.590  0.50 30.42  ? 96   ASP A OD2 1 
ATOM   757  N  N   . VAL A 1 97  ? -8.622  -7.197  29.701  1.00 12.31  ? 97   VAL A N   1 
ATOM   758  C  CA  . VAL A 1 97  ? -7.278  -7.695  29.552  1.00 12.95  ? 97   VAL A CA  1 
ATOM   759  C  C   . VAL A 1 97  ? -6.373  -7.003  30.560  1.00 12.02  ? 97   VAL A C   1 
ATOM   760  O  O   . VAL A 1 97  ? -6.323  -5.757  30.662  1.00 11.05  ? 97   VAL A O   1 
ATOM   761  C  CB  . VAL A 1 97  ? -6.762  -7.464  28.110  1.00 13.89  ? 97   VAL A CB  1 
ATOM   762  C  CG1 . VAL A 1 97  ? -5.313  -7.937  27.963  1.00 15.15  ? 97   VAL A CG1 1 
ATOM   763  C  CG2 . VAL A 1 97  ? -7.719  -8.142  27.132  1.00 15.50  ? 97   VAL A CG2 1 
ATOM   764  N  N   . SER A 1 98  ? -5.638  -7.817  31.283  1.00 13.56  ? 98   SER A N   1 
ATOM   765  C  CA  . SER A 1 98  ? -4.663  -7.321  32.184  1.00 13.36  ? 98   SER A CA  1 
ATOM   766  C  C   . SER A 1 98  ? -3.562  -8.411  32.301  1.00 14.08  ? 98   SER A C   1 
ATOM   767  O  O   . SER A 1 98  ? -3.778  -9.464  32.896  1.00 16.80  ? 98   SER A O   1 
ATOM   768  C  CB  . SER A 1 98  ? -5.260  -7.025  33.549  1.00 17.04  ? 98   SER A CB  1 
ATOM   769  O  OG  . SER A 1 98  ? -4.271  -6.419  34.364  1.00 22.82  ? 98   SER A OG  1 
ATOM   770  N  N   . ILE A 1 99  ? -2.406  -8.133  31.706  1.00 13.08  ? 99   ILE A N   1 
ATOM   771  C  CA  . ILE A 1 99  ? -1.300  -9.087  31.522  1.00 13.81  ? 99   ILE A CA  1 
ATOM   772  C  C   . ILE A 1 99  ? -0.007  -8.333  31.964  1.00 12.77  ? 99   ILE A C   1 
ATOM   773  O  O   . ILE A 1 99  ? 0.137   -7.127  31.722  1.00 12.61  ? 99   ILE A O   1 
ATOM   774  C  CB  . ILE A 1 99  ? -1.181  -9.593  30.000  1.00 12.00  ? 99   ILE A CB  1 
ATOM   775  C  CG1 . ILE A 1 99  ? -2.377  -10.546 29.676  1.00 13.38  ? 99   ILE A CG1 1 
ATOM   776  C  CG2 . ILE A 1 99  ? 0.154   -10.243 29.665  1.00 15.88  ? 99   ILE A CG2 1 
ATOM   777  C  CD1 . ILE A 1 99  ? -2.596  -10.804 28.208  1.00 17.41  ? 99   ILE A CD1 1 
ATOM   778  N  N   . GLU A 1 100 ? 0.959   -9.032  32.570  1.00 11.91  ? 100  GLU A N   1 
ATOM   779  C  CA  . GLU A 1 100 ? 2.334   -8.545  32.645  1.00 10.51  ? 100  GLU A CA  1 
ATOM   780  C  C   . GLU A 1 100 ? 3.177   -9.634  32.004  1.00 9.60   ? 100  GLU A C   1 
ATOM   781  O  O   . GLU A 1 100 ? 3.002   -10.812 32.317  1.00 11.12  ? 100  GLU A O   1 
ATOM   782  C  CB  . GLU A 1 100 ? 2.756   -8.305  34.058  1.00 13.79  ? 100  GLU A CB  1 
ATOM   783  C  CG  . GLU A 1 100 ? 4.087   -7.643  34.144  1.00 17.17  ? 100  GLU A CG  1 
ATOM   784  C  CD  . GLU A 1 100 ? 4.420   -7.229  35.560  1.00 21.27  ? 100  GLU A CD  1 
ATOM   785  O  OE1 . GLU A 1 100 ? 3.790   -7.723  36.528  0.70 26.73  ? 100  GLU A OE1 1 
ATOM   786  O  OE2 . GLU A 1 100 ? 5.327   -6.386  35.713  1.00 20.15  ? 100  GLU A OE2 1 
ATOM   787  N  N   . ASP A 1 101 ? 4.071   -9.248  31.088  1.00 8.95   ? 101  ASP A N   1 
ATOM   788  C  CA  . ASP A 1 101 ? 4.886   -10.218 30.367  1.00 8.86   ? 101  ASP A CA  1 
ATOM   789  C  C   . ASP A 1 101 ? 6.329   -9.813  30.393  1.00 8.74   ? 101  ASP A C   1 
ATOM   790  O  O   . ASP A 1 101 ? 6.665   -8.642  30.221  1.00 9.92   ? 101  ASP A O   1 
ATOM   791  C  CB  . ASP A 1 101 ? 4.391   -10.377 28.932  1.00 8.97   ? 101  ASP A CB  1 
ATOM   792  C  CG  . ASP A 1 101 ? 5.000   -11.611 28.270  1.00 9.23   ? 101  ASP A CG  1 
ATOM   793  O  OD1 . ASP A 1 101 ? 4.573   -12.734 28.654  1.00 10.33  ? 101  ASP A OD1 1 
ATOM   794  O  OD2 . ASP A 1 101 ? 5.925   -11.470 27.416  1.00 9.37   ? 101  ASP A OD2 1 
ATOM   795  N  N   . SER A 1 102 ? 7.200   -10.804 30.552  1.00 9.52   ? 102  SER A N   1 
ATOM   796  C  CA  . SER A 1 102 ? 8.616   -10.597 30.675  1.00 10.69  ? 102  SER A CA  1 
ATOM   797  C  C   . SER A 1 102 ? 9.428   -10.935 29.411  1.00 9.80   ? 102  SER A C   1 
ATOM   798  O  O   . SER A 1 102 ? 10.651  -10.908 29.460  1.00 11.75  ? 102  SER A O   1 
ATOM   799  C  CB  . SER A 1 102 ? 9.153   -11.501 31.837  1.00 14.64  ? 102  SER A CB  1 
ATOM   800  O  OG  . SER A 1 102 ? 8.634   -11.026 33.048  1.00 20.48  ? 102  SER A OG  1 
ATOM   801  N  N   . VAL A 1 103 ? 8.768   -11.297 28.329  1.00 9.33   ? 103  VAL A N   1 
ATOM   802  C  CA  . VAL A 1 103 ? 9.459   -11.694 27.116  1.00 9.35   ? 103  VAL A CA  1 
ATOM   803  C  C   . VAL A 1 103 ? 9.244   -10.679 25.980  1.00 9.45   ? 103  VAL A C   1 
ATOM   804  O  O   . VAL A 1 103 ? 10.207  -10.314 25.287  1.00 10.69  ? 103  VAL A O   1 
ATOM   805  C  CB  . VAL A 1 103 ? 9.038   -13.115 26.707  1.00 9.46   ? 103  VAL A CB  1 
ATOM   806  C  CG1 . VAL A 1 103 ? 9.651   -13.490 25.381  1.00 11.17  ? 103  VAL A CG1 1 
ATOM   807  C  CG2 . VAL A 1 103 ? 9.457   -14.099 27.789  1.00 10.44  ? 103  VAL A CG2 1 
ATOM   808  N  N   . ILE A 1 104 ? 8.022   -10.186 25.763  1.00 9.05   ? 104  ILE A N   1 
ATOM   809  C  CA  . ILE A 1 104 ? 7.857   -9.107  24.822  1.00 8.99   ? 104  ILE A CA  1 
ATOM   810  C  C   . ILE A 1 104 ? 8.635   -7.873  25.328  1.00 8.87   ? 104  ILE A C   1 
ATOM   811  O  O   . ILE A 1 104 ? 8.882   -7.713  26.514  1.00 9.94   ? 104  ILE A O   1 
ATOM   812  C  CB  . ILE A 1 104 ? 6.366   -8.746  24.603  1.00 8.67   ? 104  ILE A CB  1 
ATOM   813  C  CG1 . ILE A 1 104 ? 5.695   -8.282  25.900  1.00 9.28   ? 104  ILE A CG1 1 
ATOM   814  C  CG2 . ILE A 1 104 ? 5.622   -9.899  23.933  1.00 9.77   ? 104  ILE A CG2 1 
ATOM   815  C  CD1 . ILE A 1 104 ? 4.313   -7.700  25.727  1.00 9.74   ? 104  ILE A CD1 1 
ATOM   816  N  N   . SER A 1 105 ? 8.932   -6.969  24.400  1.00 9.04   ? 105  SER A N   1 
ATOM   817  C  CA  . SER A 1 105 ? 9.562   -5.700  24.731  1.00 9.13   ? 105  SER A CA  1 
ATOM   818  C  C   . SER A 1 105 ? 9.034   -4.623  23.794  1.00 8.81   ? 105  SER A C   1 
ATOM   819  O  O   . SER A 1 105 ? 8.465   -4.920  22.749  1.00 9.55   ? 105  SER A O   1 
ATOM   820  C  CB  . SER A 1 105 ? 11.071  -5.808  24.617  1.00 9.70   ? 105  SER A CB  1 
ATOM   821  O  OG  . SER A 1 105 ? 11.661  -4.629  25.152  1.00 10.55  ? 105  SER A OG  1 
ATOM   822  N  N   . LEU A 1 106 ? 9.276   -3.382  24.167  1.00 9.35   ? 106  LEU A N   1 
ATOM   823  C  CA  . LEU A 1 106 ? 8.999   -2.218  23.319  1.00 9.91   ? 106  LEU A CA  1 
ATOM   824  C  C   . LEU A 1 106 ? 10.281  -1.593  22.741  1.00 10.73  ? 106  LEU A C   1 
ATOM   825  O  O   . LEU A 1 106 ? 10.261  -0.500  22.198  1.00 11.69  ? 106  LEU A O   1 
ATOM   826  C  CB  . LEU A 1 106 ? 8.142   -1.181  24.077  1.00 9.97   ? 106  LEU A CB  1 
ATOM   827  C  CG  . LEU A 1 106 ? 6.827   -1.726  24.636  1.00 10.02  ? 106  LEU A CG  1 
ATOM   828  C  CD1 . LEU A 1 106 ? 6.047   -0.583  25.304  1.00 11.32  ? 106  LEU A CD1 1 
ATOM   829  C  CD2 . LEU A 1 106 ? 5.969   -2.397  23.560  1.00 11.75  ? 106  LEU A CD2 1 
ATOM   830  N  N   . SER A 1 107 ? 11.387  -2.327  22.820  1.00 11.24  ? 107  SER A N   1 
ATOM   831  C  CA  . SER A 1 107 ? 12.618  -1.987  22.101  1.00 12.63  ? 107  SER A CA  1 
ATOM   832  C  C   . SER A 1 107 ? 13.400  -3.243  21.819  1.00 12.20  ? 107  SER A C   1 
ATOM   833  O  O   . SER A 1 107 ? 13.083  -4.309  22.312  1.00 13.03  ? 107  SER A O   1 
ATOM   834  C  CB  . SER A 1 107 ? 13.468  -1.001  22.889  1.00 15.22  ? 107  SER A CB  1 
ATOM   835  O  OG  . SER A 1 107 ? 14.055  -1.650  23.976  1.00 17.75  ? 107  SER A OG  1 
ATOM   836  N  N   . GLY A 1 108 ? 14.437  -3.124  20.999  1.00 13.99  ? 108  GLY A N   1 
ATOM   837  C  CA  . GLY A 1 108 ? 15.360  -4.205  20.772  1.00 13.79  ? 108  GLY A CA  1 
ATOM   838  C  C   . GLY A 1 108 ? 14.842  -5.322  19.913  1.00 13.44  ? 108  GLY A C   1 
ATOM   839  O  O   . GLY A 1 108 ? 13.830  -5.172  19.194  1.00 13.72  ? 108  GLY A O   1 
ATOM   840  N  N   . ASP A 1 109 ? 15.493  -6.494  19.982  1.00 13.14  ? 109  ASP A N   1 
ATOM   841  C  CA  . ASP A 1 109 ? 15.110  -7.596  19.107  1.00 13.20  ? 109  ASP A CA  1 
ATOM   842  C  C   . ASP A 1 109 ? 13.805  -8.258  19.505  1.00 12.20  ? 109  ASP A C   1 
ATOM   843  O  O   . ASP A 1 109 ? 13.216  -8.983  18.700  1.00 14.12  ? 109  ASP A O   1 
ATOM   844  C  CB  . ASP A 1 109 ? 16.251  -8.621  18.937  1.00 14.52  ? 109  ASP A CB  1 
ATOM   845  C  CG  . ASP A 1 109 ? 16.593  -9.371  20.183  1.00 14.69  ? 109  ASP A CG  1 
ATOM   846  O  OD1 . ASP A 1 109 ? 16.327  -8.884  21.307  1.00 15.51  ? 109  ASP A OD1 1 
ATOM   847  O  OD2 . ASP A 1 109 ? 17.167  -10.462 20.026  1.00 18.71  ? 109  ASP A OD2 1 
ATOM   848  N  N   . HIS A 1 110 ? 13.375  -8.052  20.747  1.00 11.28  ? 110  HIS A N   1 
ATOM   849  C  CA  . HIS A 1 110 ? 12.081  -8.537  21.216  1.00 10.87  ? 110  HIS A CA  1 
ATOM   850  C  C   . HIS A 1 110 ? 10.957  -7.523  20.991  1.00 10.43  ? 110  HIS A C   1 
ATOM   851  O  O   . HIS A 1 110 ? 9.832   -7.741  21.428  1.00 10.23  ? 110  HIS A O   1 
ATOM   852  C  CB  . HIS A 1 110 ? 12.150  -8.877  22.703  1.00 11.27  ? 110  HIS A CB  1 
ATOM   853  C  CG  . HIS A 1 110 ? 13.018  -10.056 23.038  1.00 11.91  ? 110  HIS A CG  1 
ATOM   854  N  ND1 . HIS A 1 110 ? 14.373  -10.138 22.829  1.00 13.13  ? 110  HIS A ND1 1 
ATOM   855  C  CD2 . HIS A 1 110 ? 12.666  -11.191 23.678  1.00 11.58  ? 110  HIS A CD2 1 
ATOM   856  C  CE1 . HIS A 1 110 ? 14.830  -11.280 23.336  1.00 13.24  ? 110  HIS A CE1 1 
ATOM   857  N  NE2 . HIS A 1 110 ? 13.785  -11.944 23.828  1.00 13.31  ? 110  HIS A NE2 1 
ATOM   858  N  N   . CYS A 1 111 ? 11.249  -6.418  20.291  1.00 10.66  ? 111  CYS A N   1 
ATOM   859  C  CA  . CYS A 1 111 ? 10.284  -5.360  20.122  1.00 10.40  ? 111  CYS A CA  1 
ATOM   860  C  C   . CYS A 1 111 ? 9.079   -5.827  19.307  1.00 9.78   ? 111  CYS A C   1 
ATOM   861  O  O   . CYS A 1 111 ? 9.207   -6.364  18.195  1.00 10.90  ? 111  CYS A O   1 
ATOM   862  C  CB  . CYS A 1 111 ? 10.928  -4.171  19.421  1.00 11.70  ? 111  CYS A CB  1 
ATOM   863  S  SG  . CYS A 1 111 ? 9.873   -2.708  19.419  1.00 13.17  ? 111  CYS A SG  1 
ATOM   864  N  N   . ILE A 1 112 ? 7.900   -5.561  19.852  1.00 9.32   ? 112  ILE A N   1 
ATOM   865  C  CA  . ILE A 1 112 ? 6.638   -5.884  19.196  1.00 9.19   ? 112  ILE A CA  1 
ATOM   866  C  C   . ILE A 1 112 ? 6.004   -4.713  18.449  1.00 9.05   ? 112  ILE A C   1 
ATOM   867  O  O   . ILE A 1 112 ? 5.037   -4.900  17.708  1.00 9.18   ? 112  ILE A O   1 
ATOM   868  C  CB  . ILE A 1 112 ? 5.646   -6.493  20.208  1.00 9.32   ? 112  ILE A CB  1 
ATOM   869  C  CG1 . ILE A 1 112 ? 5.302   -5.496  21.323  1.00 10.17  ? 112  ILE A CG1 1 
ATOM   870  C  CG2 . ILE A 1 112 ? 6.216   -7.812  20.735  1.00 10.59  ? 112  ILE A CG2 1 
ATOM   871  C  CD1 . ILE A 1 112 ? 4.160   -5.963  22.202  1.00 11.35  ? 112  ILE A CD1 1 
ATOM   872  N  N   . THR A 1 113 ? 6.545   -3.513  18.630  1.00 10.01  ? 113  THR A N   1 
ATOM   873  C  CA  . THR A 1 113 ? 5.996   -2.364  17.951  1.00 9.90   ? 113  THR A CA  1 
ATOM   874  C  C   . THR A 1 113 ? 6.211   -2.526  16.435  1.00 9.41   ? 113  THR A C   1 
ATOM   875  O  O   . THR A 1 113 ? 7.261   -2.998  15.981  1.00 10.62  ? 113  THR A O   1 
ATOM   876  C  CB  . THR A 1 113 ? 6.633   -1.112  18.516  1.00 11.77  ? 113  THR A CB  1 
ATOM   877  O  OG1 . THR A 1 113 ? 6.525   -1.199  19.951  1.00 13.83  ? 113  THR A OG1 1 
ATOM   878  C  CG2 . THR A 1 113 ? 5.990   0.098   17.954  1.00 16.30  ? 113  THR A CG2 1 
ATOM   879  N  N   . GLY A 1 114 ? 5.203   -2.136  15.661  1.00 8.77   ? 114  GLY A N   1 
ATOM   880  C  CA  . GLY A 1 114 ? 5.221   -2.354  14.235  1.00 9.10   ? 114  GLY A CA  1 
ATOM   881  C  C   . GLY A 1 114 ? 4.795   -3.732  13.781  1.00 8.34   ? 114  GLY A C   1 
ATOM   882  O  O   . GLY A 1 114 ? 4.798   -4.006  12.594  1.00 9.20   ? 114  GLY A O   1 
ATOM   883  N  N   . ARG A 1 115 ? 4.419   -4.589  14.722  1.00 8.24   ? 115  ARG A N   1 
ATOM   884  C  CA  . ARG A 1 115 ? 3.917   -5.924  14.437  1.00 8.16   ? 115  ARG A CA  1 
ATOM   885  C  C   . ARG A 1 115 ? 2.439   -5.958  14.732  1.00 8.22   ? 115  ARG A C   1 
ATOM   886  O  O   . ARG A 1 115 ? 1.868   -4.952  15.048  1.00 12.16  ? 115  ARG A O   1 
ATOM   887  C  CB  . ARG A 1 115 ? 4.746   -6.969  15.180  1.00 8.61   ? 115  ARG A CB  1 
ATOM   888  C  CG  . ARG A 1 115 ? 6.218   -6.785  14.904  1.00 9.36   ? 115  ARG A CG  1 
ATOM   889  C  CD  . ARG A 1 115 ? 7.083   -7.898  15.489  1.00 10.11  ? 115  ARG A CD  1 
ATOM   890  N  NE  . ARG A 1 115 ? 8.507   -7.606  15.383  1.00 11.77  ? 115  ARG A NE  1 
ATOM   891  C  CZ  . ARG A 1 115 ? 9.265   -7.899  14.324  1.00 11.78  ? 115  ARG A CZ  1 
ATOM   892  N  NH1 . ARG A 1 115 ? 8.746   -8.474  13.255  1.00 12.00  ? 115  ARG A NH1 1 
ATOM   893  N  NH2 . ARG A 1 115 ? 10.558  -7.622  14.338  1.00 13.55  ? 115  ARG A NH2 1 
ATOM   894  N  N   . THR A 1 116 ? 1.767   -7.091  14.531  1.00 8.58   ? 116  THR A N   1 
ATOM   895  C  CA  . THR A 1 116 ? 0.319   -7.161  14.648  1.00 8.39   ? 116  THR A CA  1 
ATOM   896  C  C   . THR A 1 116 ? -0.098  -7.949  15.881  1.00 8.05   ? 116  THR A C   1 
ATOM   897  O  O   . THR A 1 116 ? 0.354   -9.065  16.073  1.00 10.30  ? 116  THR A O   1 
ATOM   898  C  CB  . THR A 1 116 ? -0.313  -7.819  13.405  1.00 8.88   ? 116  THR A CB  1 
ATOM   899  O  OG1 . THR A 1 116 ? -0.043  -7.023  12.268  1.00 10.17  ? 116  THR A OG1 1 
ATOM   900  C  CG2 . THR A 1 116 ? -1.801  -7.996  13.525  1.00 9.32   ? 116  THR A CG2 1 
ATOM   901  N  N   . LEU A 1 117 ? -1.001  -7.393  16.671  1.00 7.84   ? 117  LEU A N   1 
ATOM   902  C  CA  . LEU A 1 117 ? -1.656  -8.120  17.757  1.00 7.74   ? 117  LEU A CA  1 
ATOM   903  C  C   . LEU A 1 117 ? -2.959  -8.737  17.203  1.00 7.81   ? 117  LEU A C   1 
ATOM   904  O  O   . LEU A 1 117 ? -3.709  -8.036  16.512  1.00 8.75   ? 117  LEU A O   1 
ATOM   905  C  CB  . LEU A 1 117 ? -1.971  -7.147  18.883  1.00 8.16   ? 117  LEU A CB  1 
ATOM   906  C  CG  . LEU A 1 117 ? -2.541  -7.744  20.157  1.00 8.72   ? 117  LEU A CG  1 
ATOM   907  C  CD1 . LEU A 1 117 ? -1.538  -8.661  20.868  1.00 10.10  ? 117  LEU A CD1 1 
ATOM   908  C  CD2 . LEU A 1 117 ? -2.985  -6.612  21.079  1.00 9.81   ? 117  LEU A CD2 1 
ATOM   909  N  N   . VAL A 1 118 ? -3.178  -10.014 17.505  1.00 7.69   ? 118  VAL A N   1 
ATOM   910  C  CA  . VAL A 1 118 ? -4.322  -10.755 16.988  1.00 8.19   ? 118  VAL A CA  1 
ATOM   911  C  C   . VAL A 1 118 ? -5.062  -11.428 18.134  1.00 7.88   ? 118  VAL A C   1 
ATOM   912  O  O   . VAL A 1 118 ? -4.443  -12.051 19.004  1.00 8.79   ? 118  VAL A O   1 
ATOM   913  C  CB  . VAL A 1 118 ? -3.880  -11.833 15.989  1.00 8.98   ? 118  VAL A CB  1 
ATOM   914  C  CG1 . VAL A 1 118 ? -5.086  -12.615 15.457  1.00 10.67  ? 118  VAL A CG1 1 
ATOM   915  C  CG2 . VAL A 1 118 ? -3.068  -11.214 14.848  1.00 9.78   ? 118  VAL A CG2 1 
ATOM   916  N  N   . VAL A 1 119 ? -6.381  -11.341 18.095  1.00 8.12   ? 119  VAL A N   1 
ATOM   917  C  CA  . VAL A 1 119 ? -7.241  -12.152 18.960  1.00 8.64   ? 119  VAL A CA  1 
ATOM   918  C  C   . VAL A 1 119 ? -7.955  -13.210 18.092  1.00 8.42   ? 119  VAL A C   1 
ATOM   919  O  O   . VAL A 1 119 ? -8.493  -12.906 17.027  1.00 9.16   ? 119  VAL A O   1 
ATOM   920  C  CB  . VAL A 1 119 ? -8.225  -11.302 19.801  1.00 9.06   ? 119  VAL A CB  1 
ATOM   921  C  CG1 . VAL A 1 119 ? -9.162  -10.463 18.976  1.00 10.52  ? 119  VAL A CG1 1 
ATOM   922  C  CG2 . VAL A 1 119 ? -8.973  -12.185 20.790  1.00 10.33  ? 119  VAL A CG2 1 
ATOM   923  N  N   . HIS A 1 120 ? -7.890  -14.446 18.558  1.00 8.74   ? 120  HIS A N   1 
ATOM   924  C  CA  . HIS A 1 120 ? -8.303  -15.598 17.777  1.00 9.22   ? 120  HIS A CA  1 
ATOM   925  C  C   . HIS A 1 120 ? -9.684  -16.131 18.162  1.00 9.75   ? 120  HIS A C   1 
ATOM   926  O  O   . HIS A 1 120 ? -10.260 -15.831 19.198  1.00 10.49  ? 120  HIS A O   1 
ATOM   927  C  CB  . HIS A 1 120 ? -7.256  -16.716 17.957  1.00 9.48   ? 120  HIS A CB  1 
ATOM   928  C  CG  . HIS A 1 120 ? -5.981  -16.454 17.221  1.00 9.59   ? 120  HIS A CG  1 
ATOM   929  N  ND1 . HIS A 1 120 ? -5.711  -16.987 15.994  1.00 10.54  ? 120  HIS A ND1 1 
ATOM   930  C  CD2 . HIS A 1 120 ? -4.889  -15.693 17.539  1.00 10.25  ? 120  HIS A CD2 1 
ATOM   931  C  CE1 . HIS A 1 120 ? -4.497  -16.571 15.583  1.00 11.25  ? 120  HIS A CE1 1 
ATOM   932  N  NE2 . HIS A 1 120 ? -3.994  -15.785 16.521  1.00 11.05  ? 120  HIS A NE2 1 
ATOM   933  N  N   . GLU A 1 121 ? -10.178 -16.977 17.272  1.00 10.83  ? 121  GLU A N   1 
ATOM   934  C  CA  . GLU A 1 121 ? -11.481 -17.628 17.366  1.00 11.61  ? 121  GLU A CA  1 
ATOM   935  C  C   . GLU A 1 121 ? -11.644 -18.515 18.586  1.00 11.55  ? 121  GLU A C   1 
ATOM   936  O  O   . GLU A 1 121 ? -12.705 -18.543 19.179  1.00 12.40  ? 121  GLU A O   1 
ATOM   937  C  CB  . GLU A 1 121 ? -11.618 -18.487 16.097  1.00 14.85  ? 121  GLU A CB  1 
ATOM   938  C  CG  . GLU A 1 121 ? -12.860 -19.314 15.944  1.00 18.24  ? 121  GLU A CG  1 
ATOM   939  C  CD  . GLU A 1 121 ? -12.689 -20.454 14.933  1.00 20.43  ? 121  GLU A CD  1 
ATOM   940  O  OE1 . GLU A 1 121 ? -11.630 -20.630 14.274  1.00 20.34  ? 121  GLU A OE1 1 
ATOM   941  O  OE2 . GLU A 1 121 ? -13.661 -21.196 14.781  1.00 29.42  ? 121  GLU A OE2 1 
ATOM   942  N  N   . LYS A 1 122 ? -10.606 -19.284 18.881  1.00 12.97  ? 122  LYS A N   1 
ATOM   943  C  CA  . LYS A 1 122 ? -10.647 -20.412 19.783  1.00 14.82  ? 122  LYS A CA  1 
ATOM   944  C  C   . LYS A 1 122 ? -9.582  -20.237 20.881  1.00 10.87  ? 122  LYS A C   1 
ATOM   945  O  O   . LYS A 1 122 ? -8.701  -19.377 20.788  1.00 11.07  ? 122  LYS A O   1 
ATOM   946  C  CB  . LYS A 1 122 ? -10.433 -21.824 19.012  1.00 16.60  ? 122  LYS A CB  1 
ATOM   947  C  CG  . LYS A 1 122 ? -11.233 -22.093 17.758  1.00 19.06  ? 122  LYS A CG  1 
ATOM   948  C  CD  . LYS A 1 122 ? -10.810 -23.450 17.189  1.00 24.17  ? 122  LYS A CD  1 
ATOM   949  C  CE  . LYS A 1 122 ? -11.534 -23.852 15.917  1.00 29.59  ? 122  LYS A CE  1 
ATOM   950  N  NZ  . LYS A 1 122 ? -10.883 -25.057 15.329  1.00 35.93  ? 122  LYS A NZ  1 
ATOM   951  N  N   . ALA A 1 123 ? -9.604  -21.126 21.855  1.00 11.00  ? 123  ALA A N   1 
ATOM   952  C  CA  . ALA A 1 123 ? -8.588  -21.144 22.895  1.00 11.02  ? 123  ALA A CA  1 
ATOM   953  C  C   . ALA A 1 123 ? -7.246  -21.577 22.325  1.00 10.64  ? 123  ALA A C   1 
ATOM   954  O  O   . ALA A 1 123 ? -7.154  -22.445 21.463  1.00 12.62  ? 123  ALA A O   1 
ATOM   955  C  CB  . ALA A 1 123 ? -9.014  -22.100 24.013  1.00 12.81  ? 123  ALA A CB  1 
ATOM   956  N  N   . ASP A 1 124 ? -6.206  -20.966 22.840  1.00 10.14  ? 124  ASP A N   1 
ATOM   957  C  CA  . ASP A 1 124 ? -4.834  -21.442 22.677  1.00 9.98   ? 124  ASP A CA  1 
ATOM   958  C  C   . ASP A 1 124 ? -4.566  -22.519 23.763  1.00 9.87   ? 124  ASP A C   1 
ATOM   959  O  O   . ASP A 1 124 ? -4.780  -22.276 24.962  1.00 10.46  ? 124  ASP A O   1 
ATOM   960  C  CB  . ASP A 1 124 ? -3.909  -20.229 22.844  1.00 9.89   ? 124  ASP A CB  1 
ATOM   961  C  CG  . ASP A 1 124 ? -2.438  -20.483 22.593  1.00 9.98   ? 124  ASP A CG  1 
ATOM   962  O  OD1 . ASP A 1 124 ? -2.014  -21.644 22.597  1.00 10.04  ? 124  ASP A OD1 1 
ATOM   963  O  OD2 . ASP A 1 124 ? -1.710  -19.480 22.441  1.00 11.07  ? 124  ASP A OD2 1 
ATOM   964  N  N   . ASP A 1 125 ? -4.161  -23.699 23.302  1.00 10.25  ? 125  ASP A N   1 
ATOM   965  C  CA  . ASP A 1 125 ? -3.835  -24.807 24.189  1.00 10.45  ? 125  ASP A CA  1 
ATOM   966  C  C   . ASP A 1 125 ? -2.420  -24.736 24.774  1.00 10.08  ? 125  ASP A C   1 
ATOM   967  O  O   . ASP A 1 125 ? -2.001  -25.641 25.484  1.00 10.27  ? 125  ASP A O   1 
ATOM   968  C  CB  . ASP A 1 125 ? -4.104  -26.135 23.505  1.00 11.46  ? 125  ASP A CB  1 
ATOM   969  C  CG  . ASP A 1 125 ? -3.188  -26.423 22.323  1.00 11.88  ? 125  ASP A CG  1 
ATOM   970  O  OD1 . ASP A 1 125 ? -2.061  -25.871 22.247  1.00 11.76  ? 125  ASP A OD1 1 
ATOM   971  O  OD2 . ASP A 1 125 ? -3.588  -27.281 21.474  1.00 14.32  ? 125  ASP A OD2 1 
ATOM   972  N  N   . LEU A 1 126 ? -1.717  -23.619 24.519  1.00 10.34  ? 126  LEU A N   1 
ATOM   973  C  CA  . LEU A 1 126 ? -0.438  -23.322 25.136  1.00 10.30  ? 126  LEU A CA  1 
ATOM   974  C  C   . LEU A 1 126 ? 0.603   -24.377 24.849  1.00 10.69  ? 126  LEU A C   1 
ATOM   975  O  O   . LEU A 1 126 ? 1.570   -24.527 25.587  1.00 11.77  ? 126  LEU A O   1 
ATOM   976  C  CB  . LEU A 1 126 ? -0.540  -22.976 26.638  1.00 10.37  ? 126  LEU A CB  1 
ATOM   977  C  CG  . LEU A 1 126 ? -1.634  -21.999 27.053  1.00 10.85  ? 126  LEU A CG  1 
ATOM   978  C  CD1 . LEU A 1 126 ? -1.489  -21.649 28.516  1.00 11.57  ? 126  LEU A CD1 1 
ATOM   979  C  CD2 . LEU A 1 126 ? -1.621  -20.743 26.215  1.00 10.75  ? 126  LEU A CD2 1 
ATOM   980  N  N   . GLY A 1 127 ? 0.463   -25.040 23.710  1.00 11.00  ? 127  GLY A N   1 
ATOM   981  C  CA  . GLY A 1 127 ? 1.434   -26.051 23.324  1.00 11.82  ? 127  GLY A CA  1 
ATOM   982  C  C   . GLY A 1 127 ? 1.232   -27.423 23.950  1.00 12.59  ? 127  GLY A C   1 
ATOM   983  O  O   . GLY A 1 127 ? 2.057   -28.317 23.789  1.00 14.43  ? 127  GLY A O   1 
ATOM   984  N  N   . LYS A 1 128 ? 0.112   -27.608 24.647  1.00 12.12  ? 128  LYS A N   1 
ATOM   985  C  CA  . LYS A 1 128 ? -0.160  -28.844 25.412  1.00 13.23  ? 128  LYS A CA  1 
ATOM   986  C  C   . LYS A 1 128 ? -1.234  -29.694 24.788  1.00 13.43  ? 128  LYS A C   1 
ATOM   987  O  O   . LYS A 1 128 ? -1.754  -30.632 25.408  1.00 15.47  ? 128  LYS A O   1 
ATOM   988  C  CB  . LYS A 1 128 ? -0.545  -28.491 26.840  1.00 13.59  ? 128  LYS A CB  1 
ATOM   989  C  CG  . LYS A 1 128 ? 0.538   -27.768 27.593  1.00 17.93  ? 128  LYS A CG  1 
ATOM   990  C  CD  . LYS A 1 128 ? 1.719   -28.667 27.949  0.50 20.22  ? 128  LYS A CD  1 
ATOM   991  C  CE  . LYS A 1 128 ? 2.653   -28.002 28.958  0.50 23.60  ? 128  LYS A CE  1 
ATOM   992  N  NZ  . LYS A 1 128 ? 3.865   -28.817 29.273  0.50 29.29  ? 128  LYS A NZ  1 
ATOM   993  N  N   . GLY A 1 129 ? -1.554  -29.410 23.546  1.00 13.63  ? 129  GLY A N   1 
ATOM   994  C  CA  . GLY A 1 129 ? -2.617  -30.127 22.880  1.00 14.71  ? 129  GLY A CA  1 
ATOM   995  C  C   . GLY A 1 129 ? -2.234  -31.476 22.298  1.00 16.10  ? 129  GLY A C   1 
ATOM   996  O  O   . GLY A 1 129 ? -3.106  -32.181 21.847  1.00 19.84  ? 129  GLY A O   1 
ATOM   997  N  N   . GLY A 1 130 ? -0.963  -31.821 22.253  1.00 16.37  ? 130  GLY A N   1 
ATOM   998  C  CA  . GLY A 1 130 ? -0.640  -33.144 21.730  1.00 21.03  ? 130  GLY A CA  1 
ATOM   999  C  C   . GLY A 1 130 ? -0.854  -33.455 20.223  1.00 23.70  ? 130  GLY A C   1 
ATOM   1000 O  O   . GLY A 1 130 ? -0.695  -34.585 19.836  1.00 31.28  ? 130  GLY A O   1 
ATOM   1001 N  N   . ASN A 1 131 ? -1.252  -32.492 19.370  1.00 41.62  ? 131  ASN A N   1 
ATOM   1002 C  CA  . ASN A 1 131 ? -1.086  -32.616 17.886  1.00 27.04  ? 131  ASN A CA  1 
ATOM   1003 C  C   . ASN A 1 131 ? 0.096   -31.726 17.461  1.00 22.82  ? 131  ASN A C   1 
ATOM   1004 O  O   . ASN A 1 131 ? 0.585   -30.911 18.236  1.00 24.26  ? 131  ASN A O   1 
ATOM   1005 C  CB  . ASN A 1 131 ? -2.398  -32.352 17.086  1.00 23.89  ? 131  ASN A CB  1 
ATOM   1006 C  CG  . ASN A 1 131 ? -2.894  -30.917 17.177  1.00 20.48  ? 131  ASN A CG  1 
ATOM   1007 O  OD1 . ASN A 1 131 ? -2.265  -30.103 17.794  1.00 17.61  ? 131  ASN A OD1 1 
ATOM   1008 N  ND2 . ASN A 1 131 ? -4.008  -30.597 16.510  1.00 27.69  ? 131  ASN A ND2 1 
ATOM   1009 N  N   . GLU A 1 132 ? 0.544   -31.835 16.225  1.00 21.71  ? 132  GLU A N   1 
ATOM   1010 C  CA  . GLU A 1 132 ? 1.670   -31.015 15.717  1.00 22.70  ? 132  GLU A CA  1 
ATOM   1011 C  C   . GLU A 1 132 ? 1.347   -29.533 15.768  1.00 18.53  ? 132  GLU A C   1 
ATOM   1012 O  O   . GLU A 1 132 ? 2.195   -28.681 16.074  1.00 22.46  ? 132  GLU A O   1 
ATOM   1013 C  CB  . GLU A 1 132 ? 2.033   -31.417 14.275  1.00 24.07  ? 132  GLU A CB  1 
ATOM   1014 C  CG  . GLU A 1 132 ? 2.566   -30.305 13.348  0.50 29.06  ? 132  GLU A CG  1 
ATOM   1015 C  CD  . GLU A 1 132 ? 1.475   -29.540 12.579  0.50 30.58  ? 132  GLU A CD  1 
ATOM   1016 O  OE1 . GLU A 1 132 ? 0.491   -30.178 12.133  0.50 35.18  ? 132  GLU A OE1 1 
ATOM   1017 O  OE2 . GLU A 1 132 ? 1.604   -28.300 12.390  0.50 29.81  ? 132  GLU A OE2 1 
ATOM   1018 N  N   . GLU A 1 133 ? 0.106   -29.216 15.445  1.00 15.54  ? 133  GLU A N   1 
ATOM   1019 C  CA  . GLU A 1 133 ? -0.241  -27.817 15.332  1.00 15.83  ? 133  GLU A CA  1 
ATOM   1020 C  C   . GLU A 1 133 ? -0.193  -27.136 16.707  1.00 13.74  ? 133  GLU A C   1 
ATOM   1021 O  O   . GLU A 1 133 ? 0.040   -25.923 16.805  1.00 14.04  ? 133  GLU A O   1 
ATOM   1022 C  CB  . GLU A 1 133 ? -1.611  -27.643 14.688  1.00 18.13  ? 133  GLU A CB  1 
ATOM   1023 C  CG  . GLU A 1 133 ? -1.967  -26.246 14.221  1.00 22.61  ? 133  GLU A CG  1 
ATOM   1024 C  CD  . GLU A 1 133 ? -1.235  -25.736 12.954  0.50 23.57  ? 133  GLU A CD  1 
ATOM   1025 O  OE1 . GLU A 1 133 ? -0.143  -26.234 12.600  0.50 28.26  ? 133  GLU A OE1 1 
ATOM   1026 O  OE2 . GLU A 1 133 ? -1.749  -24.794 12.286  0.50 28.18  ? 133  GLU A OE2 1 
ATOM   1027 N  N   . SER A 1 134 ? -0.375  -27.881 17.794  1.00 13.41  ? 134  SER A N   1 
ATOM   1028 C  CA  . SER A 1 134 ? -0.306  -27.278 19.135  1.00 12.98  ? 134  SER A CA  1 
ATOM   1029 C  C   . SER A 1 134 ? 1.002   -26.537 19.370  1.00 12.57  ? 134  SER A C   1 
ATOM   1030 O  O   . SER A 1 134 ? 0.989   -25.476 19.968  1.00 13.26  ? 134  SER A O   1 
ATOM   1031 C  CB  . SER A 1 134 ? -0.508  -28.338 20.205  1.00 13.11  ? 134  SER A CB  1 
ATOM   1032 O  OG  . SER A 1 134 ? -0.392  -27.799 21.487  1.00 13.26  ? 134  SER A OG  1 
ATOM   1033 N  N   . THR A 1 135 ? 2.114   -27.120 18.888  1.00 14.27  ? 135  THR A N   1 
ATOM   1034 C  CA  . THR A 1 135 ? 3.418   -26.477 19.105  1.00 14.91  ? 135  THR A CA  1 
ATOM   1035 C  C   . THR A 1 135 ? 3.808   -25.455 18.003  1.00 12.99  ? 135  THR A C   1 
ATOM   1036 O  O   . THR A 1 135 ? 4.945   -24.968 18.010  1.00 14.07  ? 135  THR A O   1 
ATOM   1037 C  CB  . THR A 1 135 ? 4.515   -27.452 19.472  1.00 19.16  ? 135  THR A CB  1 
ATOM   1038 O  OG1 . THR A 1 135 ? 4.518   -28.469 18.508  1.00 28.83  ? 135  THR A OG1 1 
ATOM   1039 C  CG2 . THR A 1 135 ? 4.305   -28.092 20.894  1.00 20.89  ? 135  THR A CG2 1 
ATOM   1040 N  N   . LYS A 1 136 ? 2.838   -25.058 17.169  1.00 13.28  ? 136  LYS A N   1 
ATOM   1041 C  CA  . LYS A 1 136 ? 3.007   -24.004 16.180  1.00 13.62  ? 136  LYS A CA  1 
ATOM   1042 C  C   . LYS A 1 136 ? 2.043   -22.844 16.454  1.00 12.47  ? 136  LYS A C   1 
ATOM   1043 O  O   . LYS A 1 136 ? 2.457   -21.703 16.555  1.00 13.22  ? 136  LYS A O   1 
ATOM   1044 C  CB  . LYS A 1 136 ? 2.792   -24.539 14.758  1.00 15.87  ? 136  LYS A CB  1 
ATOM   1045 C  CG  . LYS A 1 136 ? 3.724   -25.677 14.375  1.00 18.61  ? 136  LYS A CG  1 
ATOM   1046 C  CD  . LYS A 1 136 ? 5.189   -25.331 14.243  0.50 20.33  ? 136  LYS A CD  1 
ATOM   1047 C  CE  . LYS A 1 136 ? 5.983   -26.549 13.798  0.50 21.30  ? 136  LYS A CE  1 
ATOM   1048 N  NZ  . LYS A 1 136 ? 5.773   -26.832 12.358  0.50 22.88  ? 136  LYS A NZ  1 
ATOM   1049 N  N   . THR A 1 137 ? 0.755   -23.155 16.552  1.00 12.71  ? 137  THR A N   1 
ATOM   1050 C  CA  . THR A 1 137 ? -0.288  -22.125 16.696  1.00 12.34  ? 137  THR A CA  1 
ATOM   1051 C  C   . THR A 1 137 ? -1.091  -22.248 17.970  1.00 11.35  ? 137  THR A C   1 
ATOM   1052 O  O   . THR A 1 137 ? -1.884  -21.353 18.261  1.00 12.39  ? 137  THR A O   1 
ATOM   1053 C  CB  . THR A 1 137 ? -1.312  -22.204 15.549  1.00 13.91  ? 137  THR A CB  1 
ATOM   1054 O  OG1 . THR A 1 137 ? -1.995  -23.441 15.701  1.00 15.38  ? 137  THR A OG1 1 
ATOM   1055 C  CG2 . THR A 1 137 ? -0.673  -22.118 14.193  1.00 15.62  ? 137  THR A CG2 1 
ATOM   1056 N  N   . GLY A 1 138 ? -0.984  -23.350 18.713  1.00 11.10  ? 138  GLY A N   1 
ATOM   1057 C  CA  . GLY A 1 138 ? -1.827  -23.560 19.865  1.00 11.01  ? 138  GLY A CA  1 
ATOM   1058 C  C   . GLY A 1 138 ? -3.255  -23.938 19.516  1.00 10.57  ? 138  GLY A C   1 
ATOM   1059 O  O   . GLY A 1 138 ? -4.103  -23.980 20.401  1.00 11.42  ? 138  GLY A O   1 
ATOM   1060 N  N   . ASN A 1 139 ? -3.534  -24.206 18.246  1.00 11.64  ? 139  ASN A N   1 
ATOM   1061 C  CA  . ASN A 1 139 ? -4.875  -24.581 17.790  1.00 11.99  ? 139  ASN A CA  1 
ATOM   1062 C  C   . ASN A 1 139 ? -5.906  -23.496 18.077  1.00 11.95  ? 139  ASN A C   1 
ATOM   1063 O  O   . ASN A 1 139 ? -7.072  -23.786 18.296  1.00 13.68  ? 139  ASN A O   1 
ATOM   1064 C  CB  . ASN A 1 139 ? -5.328  -25.941 18.392  1.00 13.38  ? 139  ASN A CB  1 
ATOM   1065 C  CG  . ASN A 1 139 ? -4.526  -27.088 17.844  1.00 13.81  ? 139  ASN A CG  1 
ATOM   1066 O  OD1 . ASN A 1 139 ? -4.645  -27.397 16.676  1.00 16.07  ? 139  ASN A OD1 1 
ATOM   1067 N  ND2 . ASN A 1 139 ? -3.703  -27.706 18.662  1.00 14.47  ? 139  ASN A ND2 1 
ATOM   1068 N  N   . ALA A 1 140 ? -5.486  -22.236 18.027  1.00 11.35  ? 140  ALA A N   1 
ATOM   1069 C  CA  . ALA A 1 140 ? -6.384  -21.134 18.372  1.00 11.65  ? 140  ALA A CA  1 
ATOM   1070 C  C   . ALA A 1 140 ? -7.311  -20.690 17.228  1.00 12.35  ? 140  ALA A C   1 
ATOM   1071 O  O   . ALA A 1 140 ? -8.147  -19.813 17.412  1.00 12.15  ? 140  ALA A O   1 
ATOM   1072 C  CB  . ALA A 1 140 ? -5.574  -19.945 18.885  1.00 12.11  ? 140  ALA A CB  1 
ATOM   1073 N  N   . GLY A 1 141 ? -7.164  -21.295 16.050  1.00 13.70  ? 141  GLY A N   1 
ATOM   1074 C  CA  . GLY A 1 141 ? -8.090  -21.032 14.960  1.00 14.41  ? 141  GLY A CA  1 
ATOM   1075 C  C   . GLY A 1 141 ? -7.931  -19.673 14.320  1.00 12.92  ? 141  GLY A C   1 
ATOM   1076 O  O   . GLY A 1 141 ? -6.846  -19.060 14.319  1.00 13.69  ? 141  GLY A O   1 
ATOM   1077 N  N   . SER A 1 142 ? -9.035  -19.219 13.732  1.00 13.06  ? 142  SER A N   1 
ATOM   1078 C  CA  . SER A 1 142 ? -8.996  -18.063 12.860  1.00 13.16  ? 142  SER A CA  1 
ATOM   1079 C  C   . SER A 1 142 ? -8.770  -16.763 13.620  1.00 11.44  ? 142  SER A C   1 
ATOM   1080 O  O   . SER A 1 142 ? -8.746  -16.727 14.856  1.00 12.01  ? 142  SER A O   1 
ATOM   1081 C  CB  . SER A 1 142 ? -10.254 -18.003 12.018  1.00 14.50  ? 142  SER A CB  1 
ATOM   1082 O  OG  . SER A 1 142 ? -11.344 -17.598 12.773  1.00 17.80  ? 142  SER A OG  1 
ATOM   1083 N  N   . ARG A 1 143 ? -8.568  -15.704 12.853  1.00 10.97  ? 143  ARG A N   1 
ATOM   1084 C  CA  . ARG A 1 143 ? -8.197  -14.416 13.387  1.00 10.38  ? 143  ARG A CA  1 
ATOM   1085 C  C   . ARG A 1 143 ? -9.433  -13.524 13.373  1.00 11.01  ? 143  ARG A C   1 
ATOM   1086 O  O   . ARG A 1 143 ? -9.919  -13.147 12.327  1.00 15.56  ? 143  ARG A O   1 
ATOM   1087 C  CB  . ARG A 1 143 ? -7.081  -13.808 12.541  1.00 10.73  ? 143  ARG A CB  1 
ATOM   1088 C  CG  . ARG A 1 143 ? -5.884  -14.751 12.523  1.00 10.98  ? 143  ARG A CG  1 
ATOM   1089 C  CD  . ARG A 1 143 ? -4.734  -14.275 11.658  1.00 11.49  ? 143  ARG A CD  1 
ATOM   1090 N  NE  . ARG A 1 143 ? -3.746  -15.334 11.623  1.00 12.14  ? 143  ARG A NE  1 
ATOM   1091 C  CZ  . ARG A 1 143 ? -2.515  -15.226 11.164  1.00 11.51  ? 143  ARG A CZ  1 
ATOM   1092 N  NH1 . ARG A 1 143 ? -2.035  -14.065 10.752  1.00 11.46  ? 143  ARG A NH1 1 
ATOM   1093 N  NH2 . ARG A 1 143 ? -1.718  -16.265 11.225  1.00 12.01  ? 143  ARG A NH2 1 
ATOM   1094 N  N   . LEU A 1 144 ? -9.941  -13.166 14.540  1.00 9.87   ? 144  LEU A N   1 
ATOM   1095 C  CA  . LEU A 1 144 ? -11.184 -12.411 14.611  1.00 10.22  ? 144  LEU A CA  1 
ATOM   1096 C  C   . LEU A 1 144 ? -10.980 -10.921 14.513  1.00 10.22  ? 144  LEU A C   1 
ATOM   1097 O  O   . LEU A 1 144 ? -11.824 -10.203 13.962  1.00 11.27  ? 144  LEU A O   1 
ATOM   1098 C  CB  . LEU A 1 144 ? -11.905 -12.721 15.906  1.00 11.18  ? 144  LEU A CB  1 
ATOM   1099 C  CG  . LEU A 1 144 ? -12.260 -14.175 16.150  1.00 13.69  ? 144  LEU A CG  1 
ATOM   1100 C  CD1 . LEU A 1 144 ? -13.102 -14.253 17.410  1.00 17.78  ? 144  LEU A CD1 1 
ATOM   1101 C  CD2 . LEU A 1 144 ? -12.946 -14.792 14.928  1.00 16.93  ? 144  LEU A CD2 1 
ATOM   1102 N  N   . ALA A 1 145 ? -9.887  -10.413 15.067  1.00 9.64   ? 145  ALA A N   1 
ATOM   1103 C  CA  . ALA A 1 145 ? -9.585  -8.992  14.985  1.00 9.59   ? 145  ALA A CA  1 
ATOM   1104 C  C   . ALA A 1 145 ? -8.094  -8.816  15.202  1.00 9.08   ? 145  ALA A C   1 
ATOM   1105 O  O   . ALA A 1 145 ? -7.438  -9.664  15.836  1.00 9.55   ? 145  ALA A O   1 
ATOM   1106 C  CB  . ALA A 1 145 ? -10.374 -8.195  16.021  1.00 10.54  ? 145  ALA A CB  1 
ATOM   1107 N  N   . CYS A 1 146 ? -7.572  -7.704  14.701  1.00 9.20   ? 146  CYS A N   1 
ATOM   1108 C  CA  . CYS A 1 146 ? -6.146  -7.458  14.785  1.00 8.96   ? 146  CYS A CA  1 
ATOM   1109 C  C   . CYS A 1 146 ? -5.891  -5.976  14.590  1.00 8.78   ? 146  CYS A C   1 
ATOM   1110 O  O   . CYS A 1 146 ? -6.758  -5.224  14.151  1.00 9.75   ? 146  CYS A O   1 
ATOM   1111 C  CB  . CYS A 1 146 ? -5.374  -8.270  13.751  1.00 10.17  ? 146  CYS A CB  1 
ATOM   1112 S  SG  . CYS A 1 146 ? -5.796  -7.878  12.062  1.00 12.98  ? 146  CYS A SG  1 
ATOM   1113 N  N   . GLY A 1 147 ? -4.675  -5.571  14.898  1.00 8.90   ? 147  GLY A N   1 
ATOM   1114 C  CA  . GLY A 1 147 ? -4.207  -4.224  14.596  1.00 9.04   ? 147  GLY A CA  1 
ATOM   1115 C  C   . GLY A 1 147 ? -2.718  -4.172  14.671  1.00 8.75   ? 147  GLY A C   1 
ATOM   1116 O  O   . GLY A 1 147 ? -2.080  -5.042  15.274  1.00 9.20   ? 147  GLY A O   1 
ATOM   1117 N  N   . VAL A 1 148 ? -2.137  -3.123  14.097  1.00 8.68   ? 148  VAL A N   1 
ATOM   1118 C  CA  . VAL A 1 148 ? -0.714  -2.909  14.164  1.00 8.59   ? 148  VAL A CA  1 
ATOM   1119 C  C   . VAL A 1 148 ? -0.395  -2.185  15.469  1.00 8.84   ? 148  VAL A C   1 
ATOM   1120 O  O   . VAL A 1 148 ? -1.044  -1.204  15.825  1.00 10.77  ? 148  VAL A O   1 
ATOM   1121 C  CB  . VAL A 1 148 ? -0.220  -2.121  12.921  1.00 10.06  ? 148  VAL A CB  1 
ATOM   1122 C  CG1 . VAL A 1 148 ? 1.286   -1.932  12.994  1.00 10.85  ? 148  VAL A CG1 1 
ATOM   1123 C  CG2 . VAL A 1 148 ? -0.633  -2.824  11.639  1.00 11.93  ? 148  VAL A CG2 1 
ATOM   1124 N  N   . ILE A 1 149 ? 0.627   -2.645  16.171  1.00 8.74   ? 149  ILE A N   1 
ATOM   1125 C  CA  . ILE A 1 149 ? 1.031   -2.063  17.430  1.00 8.73   ? 149  ILE A CA  1 
ATOM   1126 C  C   . ILE A 1 149 ? 1.876   -0.813  17.132  1.00 8.66   ? 149  ILE A C   1 
ATOM   1127 O  O   . ILE A 1 149 ? 2.873   -0.869  16.420  1.00 9.74   ? 149  ILE A O   1 
ATOM   1128 C  CB  . ILE A 1 149 ? 1.835   -3.092  18.251  1.00 9.00   ? 149  ILE A CB  1 
ATOM   1129 C  CG1 . ILE A 1 149 ? 0.980   -4.349  18.520  1.00 9.76   ? 149  ILE A CG1 1 
ATOM   1130 C  CG2 . ILE A 1 149 ? 2.311   -2.457  19.555  1.00 10.04  ? 149  ILE A CG2 1 
ATOM   1131 C  CD1 . ILE A 1 149 ? 1.806   -5.524  19.023  1.00 11.20  ? 149  ILE A CD1 1 
ATOM   1132 N  N   . GLY A 1 150 ? 1.449   0.309   17.682  1.00 8.27   ? 150  GLY A N   1 
ATOM   1133 C  CA  . GLY A 1 150 ? 2.075   1.589   17.401  1.00 8.68   ? 150  GLY A CA  1 
ATOM   1134 C  C   . GLY A 1 150 ? 2.682   2.237   18.616  1.00 8.30   ? 150  GLY A C   1 
ATOM   1135 O  O   . GLY A 1 150 ? 2.301   1.980   19.760  1.00 9.27   ? 150  GLY A O   1 
ATOM   1136 N  N   . ILE A 1 151 ? 3.625   3.147   18.356  1.00 8.59   ? 151  ILE A N   1 
ATOM   1137 C  CA  . ILE A 1 151 ? 4.237   3.955   19.399  1.00 8.60   ? 151  ILE A CA  1 
ATOM   1138 C  C   . ILE A 1 151 ? 3.218   4.911   19.991  1.00 9.02   ? 151  ILE A C   1 
ATOM   1139 O  O   . ILE A 1 151 ? 2.520   5.604   19.242  1.00 10.02  ? 151  ILE A O   1 
ATOM   1140 C  CB  . ILE A 1 151 ? 5.421   4.749   18.786  1.00 9.73   ? 151  ILE A CB  1 
ATOM   1141 C  CG1 . ILE A 1 151 ? 6.513   3.795   18.292  1.00 10.34  ? 151  ILE A CG1 1 
ATOM   1142 C  CG2 . ILE A 1 151 ? 5.990   5.783   19.757  1.00 11.89  ? 151  ILE A CG2 1 
ATOM   1143 C  CD1 . ILE A 1 151 ? 7.597   4.456   17.448  1.00 12.59  ? 151  ILE A CD1 1 
ATOM   1144 N  N   . ALA A 1 152 ? 3.140   4.970   21.302  1.00 8.94   ? 152  ALA A N   1 
ATOM   1145 C  CA  . ALA A 1 152 ? 2.171   5.842   21.989  1.00 9.64   ? 152  ALA A CA  1 
ATOM   1146 C  C   . ALA A 1 152 ? 2.887   6.963   22.743  1.00 10.45  ? 152  ALA A C   1 
ATOM   1147 O  O   . ALA A 1 152 ? 4.070   6.887   23.044  1.00 12.00  ? 152  ALA A O   1 
ATOM   1148 C  CB  . ALA A 1 152 ? 1.283   5.023   22.919  1.00 11.01  ? 152  ALA A CB  1 
ATOM   1149 N  N   . GLN A 1 153 ? 2.118   8.005   23.005  1.00 11.57  ? 153  GLN A N   1 
ATOM   1150 C  CA  . GLN A 1 153 ? 2.580   9.197   23.656  1.00 13.14  ? 153  GLN A CA  1 
ATOM   1151 C  C   . GLN A 1 153 ? 2.879   8.928   25.102  0.60 13.19  ? 153  GLN A C   1 
ATOM   1152 O  O   . GLN A 1 153 ? 2.131   8.221   25.763  0.60 15.24  ? 153  GLN A O   1 
ATOM   1153 C  CB  . GLN A 1 153 ? 1.493   10.273  23.539  1.00 13.77  ? 153  GLN A CB  1 
ATOM   1154 C  CG  . GLN A 1 153 ? 1.772   11.610  24.172  1.00 13.32  ? 153  GLN A CG  1 
ATOM   1155 C  CD  . GLN A 1 153 ? 0.671   12.598  23.943  1.00 13.31  ? 153  GLN A CD  1 
ATOM   1156 O  OE1 . GLN A 1 153 ? 0.011   12.602  22.852  1.00 11.99  ? 153  GLN A OE1 1 
ATOM   1157 N  NE2 . GLN A 1 153 ? 0.479   13.461  24.931  1.00 15.95  ? 153  GLN A NE2 1 
ATOM   1158 O  OXT . GLN A 1 153 ? 3.863   9.520   25.612  0.60 16.83  ? 153  GLN A OXT 1 
ATOM   1159 N  N   . ALA B 1 1   ? 15.468  -4.612  0.895   1.00 28.80  ? 1    ALA F N   1 
ATOM   1160 C  CA  . ALA B 1 1   ? 16.189  -5.004  2.140   1.00 26.31  ? 1    ALA F CA  1 
ATOM   1161 C  C   . ALA B 1 1   ? 15.261  -5.050  3.333   1.00 23.20  ? 1    ALA F C   1 
ATOM   1162 O  O   . ALA B 1 1   ? 15.025  -6.098  3.910   1.00 29.64  ? 1    ALA F O   1 
ATOM   1163 C  CB  . ALA B 1 1   ? 17.364  -4.094  2.424   1.00 37.11  ? 1    ALA F CB  1 
ATOM   1164 N  N   . THR B 1 2   ? 14.755  -3.889  3.711   1.00 19.79  ? 2    THR F N   1 
ATOM   1165 C  CA  . THR B 1 2   ? 13.801  -3.775  4.792   1.00 18.57  ? 2    THR F CA  1 
ATOM   1166 C  C   . THR B 1 2   ? 12.533  -3.230  4.165   1.00 15.80  ? 2    THR F C   1 
ATOM   1167 O  O   . THR B 1 2   ? 12.602  -2.338  3.309   1.00 17.13  ? 2    THR F O   1 
ATOM   1168 C  CB  . THR B 1 2   ? 14.338  -2.756  5.812   1.00 21.53  ? 2    THR F CB  1 
ATOM   1169 O  OG1 . THR B 1 2   ? 15.614  -3.210  6.277   1.00 30.05  ? 2    THR F OG1 1 
ATOM   1170 C  CG2 . THR B 1 2   ? 13.430  -2.599  6.983   1.00 22.33  ? 2    THR F CG2 1 
ATOM   1171 N  N   . LYS B 1 3   ? 11.381  -3.715  4.620   1.00 14.71  ? 3    LYS F N   1 
ATOM   1172 C  CA  . LYS B 1 3   ? 10.090  -3.345  4.035   1.00 14.10  ? 3    LYS F CA  1 
ATOM   1173 C  C   . LYS B 1 3   ? 9.093   -2.997  5.115   1.00 12.41  ? 3    LYS F C   1 
ATOM   1174 O  O   . LYS B 1 3   ? 9.114   -3.558  6.205   1.00 12.78  ? 3    LYS F O   1 
ATOM   1175 C  CB  . LYS B 1 3   ? 9.552   -4.487  3.163   1.00 15.00  ? 3    LYS F CB  1 
ATOM   1176 C  CG  . LYS B 1 3   ? 10.432  -4.731  1.942   1.00 18.67  ? 3    LYS F CG  1 
ATOM   1177 C  CD  . LYS B 1 3   ? 9.994   -5.946  1.169   1.00 21.69  ? 3    LYS F CD  1 
ATOM   1178 C  CE  . LYS B 1 3   ? 11.010  -6.276  0.077   1.00 27.44  ? 3    LYS F CE  1 
ATOM   1179 N  NZ  . LYS B 1 3   ? 10.798  -7.611  -0.555  1.00 34.05  ? 3    LYS F NZ  1 
ATOM   1180 N  N   . ALA B 1 4   ? 8.168   -2.107  4.778   1.00 12.18  ? 4    ALA F N   1 
ATOM   1181 C  CA  . ALA B 1 4   ? 7.066   -1.743  5.673   1.00 11.14  ? 4    ALA F CA  1 
ATOM   1182 C  C   . ALA B 1 4   ? 5.838   -1.485  4.819   1.00 11.13  ? 4    ALA F C   1 
ATOM   1183 O  O   . ALA B 1 4   ? 5.929   -1.375  3.593   1.00 12.34  ? 4    ALA F O   1 
ATOM   1184 C  CB  . ALA B 1 4   ? 7.448   -0.550  6.554   1.00 11.37  ? 4    ALA F CB  1 
ATOM   1185 N  N   . VAL B 1 5   ? 4.684   -1.397  5.464   1.00 11.01  ? 5    VAL F N   1 
ATOM   1186 C  CA  . VAL B 1 5   ? 3.429   -1.265  4.758   1.00 11.07  ? 5    VAL F CA  1 
ATOM   1187 C  C   . VAL B 1 5   ? 2.442   -0.516  5.660   1.00 10.53  ? 5    VAL F C   1 
ATOM   1188 O  O   . VAL B 1 5   ? 2.554   -0.549  6.880   1.00 11.23  ? 5    VAL F O   1 
ATOM   1189 C  CB  . VAL B 1 5   ? 2.925   -2.650  4.357   1.00 12.68  ? 5    VAL F CB  1 
ATOM   1190 C  CG1 . VAL B 1 5   ? 2.614   -3.503  5.572   1.00 13.97  ? 5    VAL F CG1 1 
ATOM   1191 C  CG2 . VAL B 1 5   ? 1.750   -2.562  3.396   1.00 15.50  ? 5    VAL F CG2 1 
ATOM   1192 N  N   . CYS B 1 6   ? 1.495   0.153   5.030   1.00 10.85  ? 6    CYS F N   1 
ATOM   1193 C  CA  . CYS B 1 6   ? 0.483   0.888   5.741   1.00 10.71  ? 6    CYS F CA  1 
ATOM   1194 C  C   . CYS B 1 6   ? -0.840  0.808   4.982   1.00 11.44  ? 6    CYS F C   1 
ATOM   1195 O  O   . CYS B 1 6   ? -0.901  1.145   3.810   1.00 12.91  ? 6    CYS F O   1 
ATOM   1196 C  CB  . CYS B 1 6   ? 0.905   2.340   5.889   1.00 10.74  ? 6    CYS F CB  1 
ATOM   1197 S  SG  . CYS B 1 6   ? -0.234  3.320   6.875   1.00 12.14  ? 6    CYS F SG  1 
ATOM   1198 N  N   . VAL B 1 7   ? -1.886  0.415   5.705   1.00 11.26  ? 7    VAL F N   1 
ATOM   1199 C  CA  . VAL B 1 7   ? -3.273  0.422   5.196   1.00 12.25  ? 7    VAL F CA  1 
ATOM   1200 C  C   . VAL B 1 7   ? -3.956  1.687   5.690   1.00 12.77  ? 7    VAL F C   1 
ATOM   1201 O  O   . VAL B 1 7   ? -4.062  1.913   6.899   1.00 13.02  ? 7    VAL F O   1 
ATOM   1202 C  CB  . VAL B 1 7   ? -4.043  -0.825  5.675   1.00 14.15  ? 7    VAL F CB  1 
ATOM   1203 C  CG1 . VAL B 1 7   ? -5.488  -0.754  5.198   1.00 17.99  ? 7    VAL F CG1 1 
ATOM   1204 C  CG2 . VAL B 1 7   ? -3.316  -2.067  5.195   1.00 16.17  ? 7    VAL F CG2 1 
ATOM   1205 N  N   . LEU B 1 8   ? -4.345  2.561   4.764   1.00 14.63  ? 8    LEU F N   1 
ATOM   1206 C  CA  . LEU B 1 8   ? -5.009  3.819   5.113   1.00 14.51  ? 8    LEU F CA  1 
ATOM   1207 C  C   . LEU B 1 8   ? -6.536  3.668   5.106   1.00 15.51  ? 8    LEU F C   1 
ATOM   1208 O  O   . LEU B 1 8   ? -7.104  3.242   4.101   1.00 18.17  ? 8    LEU F O   1 
ATOM   1209 C  CB  . LEU B 1 8   ? -4.593  4.934   4.114   1.00 15.80  ? 8    LEU F CB  1 
ATOM   1210 C  CG  . LEU B 1 8   ? -3.111  5.346   4.020   1.00 15.83  ? 8    LEU F CG  1 
ATOM   1211 C  CD1 . LEU B 1 8   ? -2.810  6.210   2.781   1.00 17.71  ? 8    LEU F CD1 1 
ATOM   1212 C  CD2 . LEU B 1 8   ? -2.703  6.099   5.262   1.00 17.13  ? 8    LEU F CD2 1 
ATOM   1213 N  N   . LYS B 1 9   ? -7.185  4.033   6.212   1.00 16.69  ? 9    LYS F N   1 
ATOM   1214 C  CA  . LYS B 1 9   ? -8.656  4.014   6.333   1.00 18.96  ? 9    LYS F CA  1 
ATOM   1215 C  C   . LYS B 1 9   ? -9.097  5.214   7.165   1.00 20.71  ? 9    LYS F C   1 
ATOM   1216 O  O   . LYS B 1 9   ? -8.346  5.703   7.997   1.00 19.90  ? 9    LYS F O   1 
ATOM   1217 C  CB  . LYS B 1 9   ? -9.125  2.732   7.015   1.00 20.80  ? 9    LYS F CB  1 
ATOM   1218 C  CG  . LYS B 1 9   ? -8.785  1.443   6.291   1.00 22.80  ? 9    LYS F CG  1 
ATOM   1219 C  CD  . LYS B 1 9   ? -9.610  0.268   6.774   1.00 27.19  ? 9    LYS F CD  1 
ATOM   1220 C  CE  . LYS B 1 9   ? -10.823 0.022   5.890   0.50 32.53  ? 9    LYS F CE  1 
ATOM   1221 N  NZ  . LYS B 1 9   ? -11.769 -0.972  6.473   0.50 36.62  ? 9    LYS F NZ  1 
ATOM   1222 N  N   A GLY B 1 10  ? -10.363 5.543   6.832   0.50 24.52  ? 10   GLY F N   1 
ATOM   1223 N  N   B GLY B 1 10  ? -10.355 5.645   7.155   0.50 17.85  ? 10   GLY F N   1 
ATOM   1224 C  CA  A GLY B 1 10  ? -10.865 6.878   6.403   0.50 16.14  ? 10   GLY F CA  1 
ATOM   1225 C  CA  B GLY B 1 10  ? -10.848 6.656   8.125   0.50 14.58  ? 10   GLY F CA  1 
ATOM   1226 C  C   A GLY B 1 10  ? -12.142 6.982   5.513   0.50 19.30  ? 10   GLY F C   1 
ATOM   1227 C  C   B GLY B 1 10  ? -12.369 6.579   8.238   0.50 14.71  ? 10   GLY F C   1 
ATOM   1228 O  O   A GLY B 1 10  ? -12.295 6.325   4.479   0.50 17.54  ? 10   GLY F O   1 
ATOM   1229 O  O   B GLY B 1 10  ? -12.945 5.482   8.222   0.50 18.11  ? 10   GLY F O   1 
ATOM   1230 N  N   A ASP B 1 11  ? -13.070 7.844   5.893   0.50 16.29  ? 11   ASP F N   1 
ATOM   1231 N  N   B ASP B 1 11  ? -13.034 7.728   8.319   0.50 18.19  ? 11   ASP F N   1 
ATOM   1232 C  CA  A ASP B 1 11  ? -14.350 7.925   5.201   0.50 19.84  ? 11   ASP F CA  1 
ATOM   1233 C  CA  B ASP B 1 11  ? -14.471 7.791   8.008   0.50 26.27  ? 11   ASP F CA  1 
ATOM   1234 C  C   A ASP B 1 11  ? -14.279 8.467   3.760   0.50 16.54  ? 11   ASP F C   1 
ATOM   1235 C  C   B ASP B 1 11  ? -14.759 8.019   6.502   0.50 21.20  ? 11   ASP F C   1 
ATOM   1236 O  O   A ASP B 1 11  ? -13.507 9.360   3.437   0.50 18.13  ? 11   ASP F O   1 
ATOM   1237 O  O   B ASP B 1 11  ? -15.524 8.912   6.140   0.50 34.33  ? 11   ASP F O   1 
ATOM   1238 C  CB  A ASP B 1 11  ? -15.282 8.748   6.062   0.50 26.45  ? 11   ASP F CB  1 
ATOM   1239 C  CB  B ASP B 1 11  ? -15.159 8.899   8.804   0.50 30.77  ? 11   ASP F CB  1 
ATOM   1240 C  CG  A ASP B 1 11  ? -15.367 8.222   7.502   0.50 21.74  ? 11   ASP F CG  1 
ATOM   1241 C  CG  B ASP B 1 11  ? -14.467 9.193   10.109  0.50 29.14  ? 11   ASP F CG  1 
ATOM   1242 O  OD1 A ASP B 1 11  ? -14.335 8.112   8.211   0.50 32.30  ? 11   ASP F OD1 1 
ATOM   1243 O  OD1 B ASP B 1 11  ? -14.194 8.238   10.868  0.50 35.02  ? 11   ASP F OD1 1 
ATOM   1244 O  OD2 A ASP B 1 11  ? -16.504 7.963   7.933   0.50 25.51  ? 11   ASP F OD2 1 
ATOM   1245 O  OD2 B ASP B 1 11  ? -14.197 10.385  10.377  0.50 37.95  ? 11   ASP F OD2 1 
ATOM   1246 N  N   A GLY B 1 12  ? -15.109 7.903   2.890   0.50 16.34  ? 12   GLY F N   1 
ATOM   1247 N  N   B GLY B 1 12  ? -14.126 7.238   5.633   0.50 27.92  ? 12   GLY F N   1 
ATOM   1248 C  CA  A GLY B 1 12  ? -15.203 8.345   1.511   0.50 21.34  ? 12   GLY F CA  1 
ATOM   1249 C  CA  B GLY B 1 12  ? -14.649 6.980   4.282   0.50 23.35  ? 12   GLY F CA  1 
ATOM   1250 C  C   A GLY B 1 12  ? -15.781 7.245   0.647   0.50 21.66  ? 12   GLY F C   1 
ATOM   1251 C  C   B GLY B 1 12  ? -14.938 8.057   3.251   0.50 25.85  ? 12   GLY F C   1 
ATOM   1252 O  O   A GLY B 1 12  ? -16.809 7.442   -0.001  0.50 22.65  ? 12   GLY F O   1 
ATOM   1253 O  O   B GLY B 1 12  ? -15.297 9.185   3.588   0.50 34.91  ? 12   GLY F O   1 
ATOM   1254 N  N   A PRO B 1 13  ? -15.163 6.054   0.666   0.50 20.86  ? 13   PRO F N   1 
ATOM   1255 N  N   B PRO B 1 13  ? -14.818 7.688   1.964   0.50 25.08  ? 13   PRO F N   1 
ATOM   1256 C  CA  A PRO B 1 13  ? -14.007 5.749   1.490   0.50 22.55  ? 13   PRO F CA  1 
ATOM   1257 C  CA  B PRO B 1 13  ? -14.313 6.399   1.553   0.50 29.19  ? 13   PRO F CA  1 
ATOM   1258 C  C   A PRO B 1 13  ? -12.823 6.504   0.942   0.50 23.31  ? 13   PRO F C   1 
ATOM   1259 C  C   B PRO B 1 13  ? -12.903 6.520   1.023   0.50 23.48  ? 13   PRO F C   1 
ATOM   1260 O  O   A PRO B 1 13  ? -12.636 6.498   -0.273  0.50 24.94  ? 13   PRO F O   1 
ATOM   1261 O  O   B PRO B 1 13  ? -12.607 6.027   -0.054  0.50 23.54  ? 13   PRO F O   1 
ATOM   1262 C  CB  A PRO B 1 13  ? -13.829 4.235   1.286   0.50 24.58  ? 13   PRO F CB  1 
ATOM   1263 C  CB  B PRO B 1 13  ? -15.259 6.009   0.413   0.50 28.03  ? 13   PRO F CB  1 
ATOM   1264 C  CG  A PRO B 1 13  ? -15.116 3.747   0.723   0.50 25.56  ? 13   PRO F CG  1 
ATOM   1265 C  CG  B PRO B 1 13  ? -15.862 7.306   -0.064  0.50 30.24  ? 13   PRO F CG  1 
ATOM   1266 C  CD  A PRO B 1 13  ? -15.600 4.883   -0.116  0.50 22.48  ? 13   PRO F CD  1 
ATOM   1267 C  CD  B PRO B 1 13  ? -15.344 8.418   0.803   0.50 25.65  ? 13   PRO F CD  1 
ATOM   1268 N  N   . VAL B 1 14  ? -12.048 7.188   1.788   1.00 24.20  ? 14   VAL F N   1 
ATOM   1269 C  CA  . VAL B 1 14  ? -10.688 7.383   1.432   1.00 20.06  ? 14   VAL F CA  1 
ATOM   1270 C  C   . VAL B 1 14  ? -10.002 6.159   1.980   1.00 23.05  ? 14   VAL F C   1 
ATOM   1271 O  O   . VAL B 1 14  ? -10.089 5.857   3.174   1.00 26.81  ? 14   VAL F O   1 
ATOM   1272 C  CB  . VAL B 1 14  ? -10.058 8.660   1.981   1.00 17.01  ? 14   VAL F CB  1 
ATOM   1273 C  CG1 . VAL B 1 14  ? -8.585  8.691   1.598   1.00 15.99  ? 14   VAL F CG1 1 
ATOM   1274 C  CG2 . VAL B 1 14  ? -10.752 9.885   1.425   1.00 17.63  ? 14   VAL F CG2 1 
ATOM   1275 N  N   . GLN B 1 15  ? -9.384  5.422   1.075   1.00 22.55  ? 15   GLN F N   1 
ATOM   1276 C  CA  . GLN B 1 15  ? -8.729  4.172   1.420   1.00 24.35  ? 15   GLN F CA  1 
ATOM   1277 C  C   . GLN B 1 15  ? -7.512  4.055   0.583   1.00 23.04  ? 15   GLN F C   1 
ATOM   1278 O  O   . GLN B 1 15  ? -7.492  4.446   -0.605  1.00 27.49  ? 15   GLN F O   1 
ATOM   1279 C  CB  . GLN B 1 15  ? -9.561  2.941   1.055   1.00 27.20  ? 15   GLN F CB  1 
ATOM   1280 C  CG  . GLN B 1 15  ? -10.995 2.934   1.522   1.00 29.81  ? 15   GLN F CG  1 
ATOM   1281 C  CD  . GLN B 1 15  ? -11.559 1.539   1.728   1.00 35.52  ? 15   GLN F CD  1 
ATOM   1282 O  OE1 . GLN B 1 15  ? -12.438 1.333   2.569   1.00 46.28  ? 15   GLN F OE1 1 
ATOM   1283 N  NE2 . GLN B 1 15  ? -11.054 0.571   0.968   1.00 36.35  ? 15   GLN F NE2 1 
ATOM   1284 N  N   . GLY B 1 16  ? -6.506  3.458   1.163   1.00 21.53  ? 16   GLY F N   1 
ATOM   1285 C  CA  . GLY B 1 16  ? -5.329  3.280   0.425   1.00 23.03  ? 16   GLY F CA  1 
ATOM   1286 C  C   . GLY B 1 16  ? -4.486  2.216   1.004   1.00 19.19  ? 16   GLY F C   1 
ATOM   1287 O  O   . GLY B 1 16  ? -4.713  1.729   2.105   1.00 19.97  ? 16   GLY F O   1 
ATOM   1288 N  N   . ILE B 1 17  ? -3.451  1.941   0.262   1.00 17.09  ? 17   ILE F N   1 
ATOM   1289 C  CA  . ILE B 1 17  ? -2.437  0.993   0.645   1.00 17.62  ? 17   ILE F CA  1 
ATOM   1290 C  C   . ILE B 1 17  ? -1.082  1.567   0.198   1.00 15.87  ? 17   ILE F C   1 
ATOM   1291 O  O   . ILE B 1 17  ? -0.961  1.984   -0.971  1.00 19.28  ? 17   ILE F O   1 
ATOM   1292 C  CB  . ILE B 1 17  ? -2.735  -0.360  0.012   1.00 19.38  ? 17   ILE F CB  1 
ATOM   1293 C  CG1 . ILE B 1 17  ? -1.625  -1.341  0.325   1.00 18.62  ? 17   ILE F CG1 1 
ATOM   1294 C  CG2 . ILE B 1 17  ? -2.978  -0.190  -1.472  1.00 21.36  ? 17   ILE F CG2 1 
ATOM   1295 C  CD1 . ILE B 1 17  ? -1.618  -1.764  1.782   1.00 22.39  ? 17   ILE F CD1 1 
ATOM   1296 N  N   . ILE B 1 18  ? -0.096  1.677   1.100   1.00 13.80  ? 18   ILE F N   1 
ATOM   1297 C  CA  . ILE B 1 18  ? 1.217   2.299   0.832   1.00 13.40  ? 18   ILE F CA  1 
ATOM   1298 C  C   . ILE B 1 18  ? 2.332   1.341   1.278   1.00 13.26  ? 18   ILE F C   1 
ATOM   1299 O  O   . ILE B 1 18  ? 2.347   0.862   2.416   1.00 14.37  ? 18   ILE F O   1 
ATOM   1300 C  CB  . ILE B 1 18  ? 1.355   3.664   1.515   1.00 13.22  ? 18   ILE F CB  1 
ATOM   1301 C  CG1 . ILE B 1 18  ? 0.259   4.624   1.046   1.00 14.08  ? 18   ILE F CG1 1 
ATOM   1302 C  CG2 . ILE B 1 18  ? 2.737   4.228   1.288   1.00 13.45  ? 18   ILE F CG2 1 
ATOM   1303 C  CD1 . ILE B 1 18  ? 0.316   5.071   -0.406  1.00 15.51  ? 18   ILE F CD1 1 
ATOM   1304 N  N   . ASN B 1 19  ? 3.261   1.082   0.375   1.00 13.72  ? 19   ASN F N   1 
ATOM   1305 C  CA  . ASN B 1 19  ? 4.396   0.223   0.600   1.00 13.70  ? 19   ASN F CA  1 
ATOM   1306 C  C   . ASN B 1 19  ? 5.668   1.055   0.748   1.00 13.26  ? 19   ASN F C   1 
ATOM   1307 O  O   . ASN B 1 19  ? 5.822   2.094   0.101   1.00 14.54  ? 19   ASN F O   1 
ATOM   1308 C  CB  . ASN B 1 19  ? 4.514   -0.735  -0.584  1.00 17.37  ? 19   ASN F CB  1 
ATOM   1309 C  CG  . ASN B 1 19  ? 3.234   -1.529  -0.803  1.00 18.93  ? 19   ASN F CG  1 
ATOM   1310 O  OD1 . ASN B 1 19  ? 2.928   -2.436  -0.060  1.00 20.34  ? 19   ASN F OD1 1 
ATOM   1311 N  ND2 . ASN B 1 19  ? 2.468   -1.146  -1.818  1.00 23.05  ? 19   ASN F ND2 1 
ATOM   1312 N  N   . PHE B 1 20  ? 6.588   0.560   1.582   1.00 13.34  ? 20   PHE F N   1 
ATOM   1313 C  CA  . PHE B 1 20  ? 7.883   1.191   1.828   1.00 13.22  ? 20   PHE F CA  1 
ATOM   1314 C  C   . PHE B 1 20  ? 8.977   0.143   1.642   1.00 13.62  ? 20   PHE F C   1 
ATOM   1315 O  O   . PHE B 1 20  ? 8.851   -0.977  2.143   1.00 14.56  ? 20   PHE F O   1 
ATOM   1316 C  CB  . PHE B 1 20  ? 8.001   1.733   3.265   1.00 12.71  ? 20   PHE F CB  1 
ATOM   1317 C  CG  . PHE B 1 20  ? 6.943   2.725   3.661   1.00 12.16  ? 20   PHE F CG  1 
ATOM   1318 C  CD1 . PHE B 1 20  ? 5.669   2.345   4.048   1.00 13.44  ? 20   PHE F CD1 1 
ATOM   1319 C  CD2 . PHE B 1 20  ? 7.248   4.066   3.657   1.00 12.64  ? 20   PHE F CD2 1 
ATOM   1320 C  CE1 . PHE B 1 20  ? 4.723   3.296   4.425   1.00 14.34  ? 20   PHE F CE1 1 
ATOM   1321 C  CE2 . PHE B 1 20  ? 6.306   5.007   4.018   1.00 13.80  ? 20   PHE F CE2 1 
ATOM   1322 C  CZ  . PHE B 1 20  ? 5.045   4.632   4.401   1.00 13.81  ? 20   PHE F CZ  1 
ATOM   1323 N  N   . GLU B 1 21  ? 10.064  0.515   0.977   1.00 14.48  ? 21   GLU F N   1 
ATOM   1324 C  CA  . GLU B 1 21  ? 11.210  -0.373  0.865   1.00 15.74  ? 21   GLU F CA  1 
ATOM   1325 C  C   . GLU B 1 21  ? 12.496  0.396   0.962   1.00 16.04  ? 21   GLU F C   1 
ATOM   1326 O  O   . GLU B 1 21  ? 12.640  1.461   0.355   1.00 18.35  ? 21   GLU F O   1 
ATOM   1327 C  CB  . GLU B 1 21  ? 11.170  -1.166  -0.437  1.00 18.57  ? 21   GLU F CB  1 
ATOM   1328 C  CG  . GLU B 1 21  ? 12.258  -2.232  -0.577  1.00 20.57  ? 21   GLU F CG  1 
ATOM   1329 C  CD  . GLU B 1 21  ? 11.983  -3.224  -1.679  1.00 29.13  ? 21   GLU F CD  1 
ATOM   1330 O  OE1 . GLU B 1 21  ? 10.822  -3.363  -2.129  1.00 32.57  ? 21   GLU F OE1 1 
ATOM   1331 O  OE2 . GLU B 1 21  ? 12.949  -3.908  -2.056  1.00 35.32  ? 21   GLU F OE2 1 
ATOM   1332 N  N   . GLN B 1 22  ? 13.434  -0.126  1.739   1.00 16.23  ? 22   GLN F N   1 
ATOM   1333 C  CA  . GLN B 1 22  ? 14.744  0.496   1.965   1.00 16.97  ? 22   GLN F CA  1 
ATOM   1334 C  C   . GLN B 1 22  ? 15.801  -0.583  1.708   1.00 18.89  ? 22   GLN F C   1 
ATOM   1335 O  O   . GLN B 1 22  ? 15.947  -1.527  2.458   1.00 20.52  ? 22   GLN F O   1 
ATOM   1336 C  CB  . GLN B 1 22  ? 14.831  1.013   3.396   1.00 16.62  ? 22   GLN F CB  1 
ATOM   1337 C  CG  . GLN B 1 22  ? 16.037  1.888   3.666   1.00 17.42  ? 22   GLN F CG  1 
ATOM   1338 C  CD  . GLN B 1 22  ? 16.018  2.453   5.063   1.00 16.30  ? 22   GLN F CD  1 
ATOM   1339 O  OE1 . GLN B 1 22  ? 15.394  1.888   5.945   1.00 18.45  ? 22   GLN F OE1 1 
ATOM   1340 N  NE2 . GLN B 1 22  ? 16.666  3.591   5.272   1.00 16.09  ? 22   GLN F NE2 1 
ATOM   1341 N  N   . LYS B 1 23  ? 16.526  -0.436  0.607   1.00 20.60  ? 23   LYS F N   1 
ATOM   1342 C  CA  . LYS B 1 23  ? 17.516  -1.430  0.198   1.00 23.91  ? 23   LYS F CA  1 
ATOM   1343 C  C   . LYS B 1 23  ? 18.671  -1.572  1.193   1.00 25.46  ? 23   LYS F C   1 
ATOM   1344 O  O   . LYS B 1 23  ? 19.175  -2.682  1.377   1.00 29.55  ? 23   LYS F O   1 
ATOM   1345 C  CB  . LYS B 1 23  ? 18.033  -1.139  -1.204  1.00 27.49  ? 23   LYS F CB  1 
ATOM   1346 C  CG  . LYS B 1 23  ? 16.928  -1.167  -2.251  1.00 31.04  ? 23   LYS F CG  1 
ATOM   1347 C  CD  . LYS B 1 23  ? 17.489  -1.113  -3.662  1.00 36.64  ? 23   LYS F CD  1 
ATOM   1348 C  CE  . LYS B 1 23  ? 16.392  -1.239  -4.712  1.00 42.21  ? 23   LYS F CE  1 
ATOM   1349 N  NZ  . LYS B 1 23  ? 16.949  -1.293  -6.096  1.00 54.73  ? 23   LYS F NZ  1 
ATOM   1350 N  N   . GLU B 1 24  ? 19.086  -0.474  1.825   1.00 27.64  ? 24   GLU F N   1 
ATOM   1351 C  CA  . GLU B 1 24  ? 20.035  -0.542  2.957   1.00 32.52  ? 24   GLU F CA  1 
ATOM   1352 C  C   . GLU B 1 24  ? 19.705  0.506   4.007   1.00 27.00  ? 24   GLU F C   1 
ATOM   1353 O  O   . GLU B 1 24  ? 19.042  1.445   3.686   1.00 26.17  ? 24   GLU F O   1 
ATOM   1354 C  CB  . GLU B 1 24  ? 21.468  -0.402  2.467   1.00 34.07  ? 24   GLU F CB  1 
ATOM   1355 C  CG  . GLU B 1 24  ? 21.660  0.577   1.318   1.00 34.07  ? 24   GLU F CG  1 
ATOM   1356 C  CD  . GLU B 1 24  ? 22.814  0.184   0.407   1.00 41.89  ? 24   GLU F CD  1 
ATOM   1357 O  OE1 . GLU B 1 24  ? 23.746  -0.510  0.876   0.50 44.67  ? 24   GLU F OE1 1 
ATOM   1358 O  OE2 . GLU B 1 24  ? 22.785  0.564   -0.787  0.50 47.07  ? 24   GLU F OE2 1 
ATOM   1359 N  N   . SER B 1 25  ? 20.156  0.325   5.252   1.00 31.52  ? 25   SER F N   1 
ATOM   1360 C  CA  . SER B 1 25  ? 19.696  1.162   6.386   1.00 27.33  ? 25   SER F CA  1 
ATOM   1361 C  C   . SER B 1 25  ? 20.169  2.602   6.279   1.00 24.10  ? 25   SER F C   1 
ATOM   1362 O  O   . SER B 1 25  ? 19.544  3.538   6.780   1.00 34.85  ? 25   SER F O   1 
ATOM   1363 C  CB  . SER B 1 25  ? 20.165  0.568   7.716   1.00 32.99  ? 25   SER F CB  1 
ATOM   1364 O  OG  . SER B 1 25  ? 21.576  0.593   7.835   1.00 38.86  ? 25   SER F OG  1 
ATOM   1365 N  N   . ASN B 1 26  ? 21.290  2.759   5.619   1.00 28.16  ? 26   ASN F N   1 
ATOM   1366 C  CA  . ASN B 1 26  ? 21.813  4.075   5.366   1.00 28.86  ? 26   ASN F CA  1 
ATOM   1367 C  C   . ASN B 1 26  ? 21.225  4.658   4.068   1.00 27.57  ? 26   ASN F C   1 
ATOM   1368 O  O   . ASN B 1 26  ? 21.807  5.573   3.498   1.00 32.87  ? 26   ASN F O   1 
ATOM   1369 C  CB  . ASN B 1 26  ? 23.355  4.021   5.355   1.00 31.33  ? 26   ASN F CB  1 
ATOM   1370 C  CG  . ASN B 1 26  ? 23.911  2.824   4.611   0.50 32.32  ? 26   ASN F CG  1 
ATOM   1371 O  OD1 . ASN B 1 26  ? 23.241  2.215   3.776   0.50 32.49  ? 26   ASN F OD1 1 
ATOM   1372 N  ND2 . ASN B 1 26  ? 25.155  2.483   4.913   1.00 43.43  ? 26   ASN F ND2 1 
ATOM   1373 N  N   . GLY B 1 27  ? 20.055  4.198   3.603   1.00 25.02  ? 27   GLY F N   1 
ATOM   1374 C  CA  . GLY B 1 27  ? 19.764  4.585   2.227   1.00 22.80  ? 27   GLY F CA  1 
ATOM   1375 C  C   . GLY B 1 27  ? 18.361  5.099   2.070   1.00 18.16  ? 27   GLY F C   1 
ATOM   1376 O  O   . GLY B 1 27  ? 17.582  5.156   3.051   1.00 18.01  ? 27   GLY F O   1 
ATOM   1377 N  N   . PRO B 1 28  ? 18.009  5.503   0.839   1.00 19.60  ? 28   PRO F N   1 
ATOM   1378 C  CA  . PRO B 1 28  ? 16.695  6.049   0.596   1.00 20.44  ? 28   PRO F CA  1 
ATOM   1379 C  C   . PRO B 1 28  ? 15.592  5.014   0.729   1.00 17.64  ? 28   PRO F C   1 
ATOM   1380 O  O   . PRO B 1 28  ? 15.814  3.799   0.537   1.00 19.11  ? 28   PRO F O   1 
ATOM   1381 C  CB  . PRO B 1 28  ? 16.794  6.572   -0.846  1.00 24.52  ? 28   PRO F CB  1 
ATOM   1382 C  CG  . PRO B 1 28  ? 17.850  5.751   -1.474  1.00 26.90  ? 28   PRO F CG  1 
ATOM   1383 C  CD  . PRO B 1 28  ? 18.831  5.471   -0.388  1.00 23.17  ? 28   PRO F CD  1 
ATOM   1384 N  N   . VAL B 1 29  ? 14.406  5.516   1.012   1.00 16.87  ? 29   VAL F N   1 
ATOM   1385 C  CA  . VAL B 1 29  ? 13.222  4.700   1.132   1.00 15.28  ? 29   VAL F CA  1 
ATOM   1386 C  C   . VAL B 1 29  ? 12.314  5.008   -0.051  1.00 15.39  ? 29   VAL F C   1 
ATOM   1387 O  O   . VAL B 1 29  ? 11.992  6.175   -0.320  1.00 16.70  ? 29   VAL F O   1 
ATOM   1388 C  CB  . VAL B 1 29  ? 12.466  5.002   2.436   1.00 15.50  ? 29   VAL F CB  1 
ATOM   1389 C  CG1 . VAL B 1 29  ? 11.230  4.108   2.549   1.00 16.04  ? 29   VAL F CG1 1 
ATOM   1390 C  CG2 . VAL B 1 29  ? 13.366  4.803   3.634   1.00 17.06  ? 29   VAL F CG2 1 
ATOM   1391 N  N   . LYS B 1 30  ? 11.946  3.963   -0.778  1.00 15.90  ? 30   LYS F N   1 
ATOM   1392 C  CA  . LYS B 1 30  ? 10.940  4.061   -1.819  1.00 16.80  ? 30   LYS F CA  1 
ATOM   1393 C  C   . LYS B 1 30  ? 9.564   3.899   -1.182  1.00 15.53  ? 30   LYS F C   1 
ATOM   1394 O  O   . LYS B 1 30  ? 9.356   2.980   -0.374  1.00 16.07  ? 30   LYS F O   1 
ATOM   1395 C  CB  . LYS B 1 30  ? 11.191  3.006   -2.896  1.00 18.87  ? 30   LYS F CB  1 
ATOM   1396 C  CG  . LYS B 1 30  ? 12.527  3.222   -3.596  1.00 24.82  ? 30   LYS F CG  1 
ATOM   1397 C  CD  . LYS B 1 30  ? 12.703  2.297   -4.789  1.00 29.36  ? 30   LYS F CD  1 
ATOM   1398 C  CE  . LYS B 1 30  ? 14.116  2.352   -5.353  1.00 30.65  ? 30   LYS F CE  1 
ATOM   1399 N  NZ  . LYS B 1 30  ? 14.384  1.274   -6.349  1.00 42.54  ? 30   LYS F NZ  1 
ATOM   1400 N  N   . VAL B 1 31  ? 8.628   4.748   -1.569  1.00 15.99  ? 31   VAL F N   1 
ATOM   1401 C  CA  . VAL B 1 31  ? 7.281   4.794   -1.044  1.00 15.88  ? 31   VAL F CA  1 
ATOM   1402 C  C   . VAL B 1 31  ? 6.351   4.751   -2.232  1.00 17.48  ? 31   VAL F C   1 
ATOM   1403 O  O   . VAL B 1 31  ? 6.448   5.599   -3.119  1.00 21.13  ? 31   VAL F O   1 
ATOM   1404 C  CB  . VAL B 1 31  ? 7.019   6.080   -0.234  1.00 15.85  ? 31   VAL F CB  1 
ATOM   1405 C  CG1 . VAL B 1 31  ? 5.637   6.078   0.384   1.00 16.88  ? 31   VAL F CG1 1 
ATOM   1406 C  CG2 . VAL B 1 31  ? 8.109   6.300   0.793   1.00 16.69  ? 31   VAL F CG2 1 
ATOM   1407 N  N   . TRP B 1 32  ? 5.497   3.736   -2.301  1.00 16.79  ? 32   TRP F N   1 
ATOM   1408 C  CA  . TRP B 1 32  ? 4.626   3.661   -3.450  1.00 19.05  ? 32   TRP F CA  1 
ATOM   1409 C  C   . TRP B 1 32  ? 3.361   2.947   -3.131  1.00 16.19  ? 32   TRP F C   1 
ATOM   1410 O  O   . TRP B 1 32  ? 3.277   2.096   -2.209  1.00 15.56  ? 32   TRP F O   1 
ATOM   1411 C  CB  . TRP B 1 32  ? 5.348   3.021   -4.612  1.00 22.14  ? 32   TRP F CB  1 
ATOM   1412 C  CG  . TRP B 1 32  ? 5.420   1.543   -4.479  1.00 22.55  ? 32   TRP F CG  1 
ATOM   1413 C  CD1 . TRP B 1 32  ? 4.604   0.610   -5.081  1.00 25.63  ? 32   TRP F CD1 1 
ATOM   1414 C  CD2 . TRP B 1 32  ? 6.373   0.770   -3.694  1.00 21.32  ? 32   TRP F CD2 1 
ATOM   1415 N  NE1 . TRP B 1 32  ? 4.969   -0.656  -4.709  1.00 28.35  ? 32   TRP F NE1 1 
ATOM   1416 C  CE2 . TRP B 1 32  ? 6.021   -0.630  -3.876  1.00 23.83  ? 32   TRP F CE2 1 
ATOM   1417 C  CE3 . TRP B 1 32  ? 7.427   1.102   -2.848  1.00 21.86  ? 32   TRP F CE3 1 
ATOM   1418 C  CZ2 . TRP B 1 32  ? 6.728   -1.646  -3.258  1.00 26.90  ? 32   TRP F CZ2 1 
ATOM   1419 C  CZ3 . TRP B 1 32  ? 8.131   0.068   -2.217  1.00 21.90  ? 32   TRP F CZ3 1 
ATOM   1420 C  CH2 . TRP B 1 32  ? 7.798   -1.272  -2.433  1.00 24.11  ? 32   TRP F CH2 1 
ATOM   1421 N  N   . GLY B 1 33  ? 2.335   3.286   -3.878  1.00 17.97  ? 33   GLY F N   1 
ATOM   1422 C  CA  . GLY B 1 33  ? 1.039   2.679   -3.709  1.00 17.28  ? 33   GLY F CA  1 
ATOM   1423 C  C   . GLY B 1 33  ? -0.062  3.495   -4.336  1.00 19.25  ? 33   GLY F C   1 
ATOM   1424 O  O   . GLY B 1 33  ? 0.209   4.274   -5.243  1.00 23.97  ? 33   GLY F O   1 
ATOM   1425 N  N   . SER B 1 34  ? -1.290  3.346   -3.809  1.00 20.11  ? 34   SER F N   1 
ATOM   1426 C  CA  . SER B 1 34  ? -2.485  4.020   -4.348  1.00 20.07  ? 34   SER F CA  1 
ATOM   1427 C  C   . SER B 1 34  ? -3.418  4.426   -3.232  1.00 20.10  ? 34   SER F C   1 
ATOM   1428 O  O   . SER B 1 34  ? -3.558  3.723   -2.209  1.00 22.85  ? 34   SER F O   1 
ATOM   1429 C  CB  . SER B 1 34  ? -3.244  3.087   -5.311  1.00 20.35  ? 34   SER F CB  1 
ATOM   1430 O  OG  . SER B 1 34  ? -4.173  3.820   -6.097  1.00 30.05  ? 34   SER F OG  1 
ATOM   1431 N  N   . ILE B 1 35  ? -4.069  5.555   -3.462  1.00 19.99  ? 35   ILE F N   1 
ATOM   1432 C  CA  . ILE B 1 35  ? -5.091  6.053   -2.566  1.00 19.32  ? 35   ILE F CA  1 
ATOM   1433 C  C   . ILE B 1 35  ? -6.247  6.463   -3.437  1.00 19.80  ? 35   ILE F C   1 
ATOM   1434 O  O   . ILE B 1 35  ? -6.067  7.203   -4.419  1.00 21.47  ? 35   ILE F O   1 
ATOM   1435 C  CB  . ILE B 1 35  ? -4.651  7.265   -1.723  1.00 17.84  ? 35   ILE F CB  1 
ATOM   1436 C  CG1 . ILE B 1 35  ? -3.298  6.985   -1.068  1.00 17.12  ? 35   ILE F CG1 1 
ATOM   1437 C  CG2 . ILE B 1 35  ? -5.713  7.544   -0.676  1.00 18.72  ? 35   ILE F CG2 1 
ATOM   1438 C  CD1 . ILE B 1 35  ? -2.680  8.193   -0.397  1.00 19.29  ? 35   ILE F CD1 1 
ATOM   1439 N  N   . LYS B 1 36  ? -7.433  6.019   -3.044  1.00 19.23  ? 36   LYS F N   1 
ATOM   1440 C  CA  . LYS B 1 36  ? -8.672  6.348   -3.778  1.00 19.84  ? 36   LYS F CA  1 
ATOM   1441 C  C   . LYS B 1 36  ? -9.671  7.029   -2.874  1.00 19.78  ? 36   LYS F C   1 
ATOM   1442 O  O   . LYS B 1 36  ? -9.479  7.121   -1.656  1.00 20.42  ? 36   LYS F O   1 
ATOM   1443 C  CB  . LYS B 1 36  ? -9.292  5.090   -4.366  1.00 21.58  ? 36   LYS F CB  1 
ATOM   1444 C  CG  . LYS B 1 36  ? -9.793  4.056   -3.370  1.00 23.47  ? 36   LYS F CG  1 
ATOM   1445 C  CD  . LYS B 1 36  ? -10.179 2.774   -4.100  1.00 26.25  ? 36   LYS F CD  1 
ATOM   1446 C  CE  . LYS B 1 36  ? -10.567 1.643   -3.162  0.50 24.83  ? 36   LYS F CE  1 
ATOM   1447 N  NZ  . LYS B 1 36  ? -11.065 0.451   -3.916  0.50 29.33  ? 36   LYS F NZ  1 
ATOM   1448 N  N   . GLY B 1 37  ? -10.722 7.571   -3.493  1.00 21.27  ? 37   GLY F N   1 
ATOM   1449 C  CA  . GLY B 1 37  ? -11.764 8.267   -2.769  1.00 21.29  ? 37   GLY F CA  1 
ATOM   1450 C  C   . GLY B 1 37  ? -11.471 9.731   -2.469  1.00 18.94  ? 37   GLY F C   1 
ATOM   1451 O  O   . GLY B 1 37  ? -12.214 10.330  -1.720  1.00 22.56  ? 37   GLY F O   1 
ATOM   1452 N  N   . LEU B 1 38  ? -10.400 10.272  -3.053  1.00 19.06  ? 38   LEU F N   1 
ATOM   1453 C  CA  . LEU B 1 38  ? -9.950  11.627  -2.778  1.00 17.84  ? 38   LEU F CA  1 
ATOM   1454 C  C   . LEU B 1 38  ? -10.599 12.649  -3.705  1.00 18.00  ? 38   LEU F C   1 
ATOM   1455 O  O   . LEU B 1 38  ? -10.941 12.343  -4.835  1.00 22.26  ? 38   LEU F O   1 
ATOM   1456 C  CB  . LEU B 1 38  ? -8.448  11.732  -2.967  1.00 17.06  ? 38   LEU F CB  1 
ATOM   1457 C  CG  . LEU B 1 38  ? -7.610  10.946  -1.938  1.00 16.77  ? 38   LEU F CG  1 
ATOM   1458 C  CD1 . LEU B 1 38  ? -6.192  10.816  -2.453  1.00 18.46  ? 38   LEU F CD1 1 
ATOM   1459 C  CD2 . LEU B 1 38  ? -7.669  11.648  -0.581  1.00 15.96  ? 38   LEU F CD2 1 
ATOM   1460 N  N   . THR B 1 39  ? -10.743 13.876  -3.236  1.00 16.69  ? 39   THR F N   1 
ATOM   1461 C  CA  . THR B 1 39  ? -11.077 14.989  -4.132  1.00 16.45  ? 39   THR F CA  1 
ATOM   1462 C  C   . THR B 1 39  ? -9.876  15.310  -5.051  1.00 15.98  ? 39   THR F C   1 
ATOM   1463 O  O   . THR B 1 39  ? -8.728  15.105  -4.683  1.00 16.55  ? 39   THR F O   1 
ATOM   1464 C  CB  . THR B 1 39  ? -11.497 16.236  -3.335  1.00 17.73  ? 39   THR F CB  1 
ATOM   1465 O  OG1 . THR B 1 39  ? -10.434 16.600  -2.460  1.00 18.70  ? 39   THR F OG1 1 
ATOM   1466 C  CG2 . THR B 1 39  ? -12.768 16.000  -2.527  1.00 19.82  ? 39   THR F CG2 1 
ATOM   1467 N  N   . GLU B 1 40  ? -10.151 15.812  -6.251  1.00 17.30  ? 40   GLU F N   1 
ATOM   1468 C  CA  . GLU B 1 40  ? -9.108  16.165  -7.203  1.00 16.89  ? 40   GLU F CA  1 
ATOM   1469 C  C   . GLU B 1 40  ? -8.192  17.242  -6.610  1.00 16.60  ? 40   GLU F C   1 
ATOM   1470 O  O   . GLU B 1 40  ? -8.662  18.209  -6.026  1.00 19.08  ? 40   GLU F O   1 
ATOM   1471 C  CB  . GLU B 1 40  ? -9.762  16.685  -8.495  1.00 18.58  ? 40   GLU F CB  1 
ATOM   1472 C  CG  . GLU B 1 40  ? -8.771  17.096  -9.597  1.00 18.21  ? 40   GLU F CG  1 
ATOM   1473 C  CD  . GLU B 1 40  ? -9.409  17.719  -10.798 1.00 19.42  ? 40   GLU F CD  1 
ATOM   1474 O  OE1 . GLU B 1 40  ? -10.483 18.354  -10.660 1.00 23.96  ? 40   GLU F OE1 1 
ATOM   1475 O  OE2 . GLU B 1 40  ? -8.790  17.600  -11.860 1.00 21.00  ? 40   GLU F OE2 1 
ATOM   1476 N  N   . GLY B 1 41  ? -6.878  17.067  -6.747  1.00 15.05  ? 41   GLY F N   1 
ATOM   1477 C  CA  . GLY B 1 41  ? -5.917  18.050  -6.297  1.00 13.82  ? 41   GLY F CA  1 
ATOM   1478 C  C   . GLY B 1 41  ? -4.948  17.450  -5.287  1.00 14.01  ? 41   GLY F C   1 
ATOM   1479 O  O   . GLY B 1 41  ? -4.823  16.228  -5.150  1.00 14.14  ? 41   GLY F O   1 
ATOM   1480 N  N   . LEU B 1 42  ? -4.258  18.352  -4.618  1.00 13.56  ? 42   LEU F N   1 
ATOM   1481 C  CA  . LEU B 1 42  ? -3.225  17.957  -3.689  1.00 12.99  ? 42   LEU F CA  1 
ATOM   1482 C  C   . LEU B 1 42  ? -3.805  17.594  -2.333  1.00 11.95  ? 42   LEU F C   1 
ATOM   1483 O  O   . LEU B 1 42  ? -4.753  18.241  -1.851  1.00 12.89  ? 42   LEU F O   1 
ATOM   1484 C  CB  . LEU B 1 42  ? -2.225  19.103  -3.487  1.00 12.87  ? 42   LEU F CB  1 
ATOM   1485 C  CG  . LEU B 1 42  ? -1.071  19.300  -4.448  1.00 13.96  ? 42   LEU F CG  1 
ATOM   1486 C  CD1 . LEU B 1 42  ? -1.592  19.563  -5.819  1.00 15.71  ? 42   LEU F CD1 1 
ATOM   1487 C  CD2 . LEU B 1 42  ? -0.114  20.414  -4.041  1.00 14.29  ? 42   LEU F CD2 1 
ATOM   1488 N  N   . HIS B 1 43  ? -3.193  16.611  -1.704  1.00 11.77  ? 43   HIS F N   1 
ATOM   1489 C  CA  . HIS B 1 43  ? -3.510  16.217  -0.340  1.00 11.87  ? 43   HIS F CA  1 
ATOM   1490 C  C   . HIS B 1 43  ? -2.230  16.023  0.419   1.00 11.47  ? 43   HIS F C   1 
ATOM   1491 O  O   . HIS B 1 43  ? -1.381  15.209  0.031   1.00 12.04  ? 43   HIS F O   1 
ATOM   1492 C  CB  . HIS B 1 43  ? -4.319  14.914  -0.339  1.00 12.01  ? 43   HIS F CB  1 
ATOM   1493 C  CG  . HIS B 1 43  ? -5.661  15.084  -0.974  1.00 12.40  ? 43   HIS F CG  1 
ATOM   1494 N  ND1 . HIS B 1 43  ? -6.724  15.481  -0.276  1.00 13.78  ? 43   HIS F ND1 1 
ATOM   1495 C  CD2 . HIS B 1 43  ? -6.066  14.985  -2.300  1.00 13.87  ? 43   HIS F CD2 1 
ATOM   1496 C  CE1 . HIS B 1 43  ? -7.781  15.635  -1.106  1.00 15.95  ? 43   HIS F CE1 1 
ATOM   1497 N  NE2 . HIS B 1 43  ? -7.375  15.335  -2.338  1.00 15.89  ? 43   HIS F NE2 1 
ATOM   1498 N  N   . GLY B 1 44  ? -2.121  16.706  1.546   1.00 11.33  ? 44   GLY F N   1 
ATOM   1499 C  CA  . GLY B 1 44  ? -0.934  16.574  2.374   1.00 11.31  ? 44   GLY F CA  1 
ATOM   1500 C  C   . GLY B 1 44  ? -0.715  15.128  2.817   1.00 10.88  ? 44   GLY F C   1 
ATOM   1501 O  O   . GLY B 1 44  ? -1.675  14.410  3.077   1.00 11.46  ? 44   GLY F O   1 
ATOM   1502 N  N   . PHE B 1 45  ? 0.542   14.740  2.943   1.00 10.71  ? 45   PHE F N   1 
ATOM   1503 C  CA  . PHE B 1 45  ? 0.920   13.331  3.120   1.00 10.73  ? 45   PHE F CA  1 
ATOM   1504 C  C   . PHE B 1 45  ? 2.087   13.298  4.075   1.00 10.00  ? 45   PHE F C   1 
ATOM   1505 O  O   . PHE B 1 45  ? 3.205   13.703  3.715   1.00 11.06  ? 45   PHE F O   1 
ATOM   1506 C  CB  . PHE B 1 45  ? 1.281   12.767  1.734   1.00 11.51  ? 45   PHE F CB  1 
ATOM   1507 C  CG  . PHE B 1 45  ? 1.493   11.280  1.677   1.00 11.29  ? 45   PHE F CG  1 
ATOM   1508 C  CD1 . PHE B 1 45  ? 0.468   10.394  1.994   1.00 13.62  ? 45   PHE F CD1 1 
ATOM   1509 C  CD2 . PHE B 1 45  ? 2.671   10.753  1.194   1.00 12.79  ? 45   PHE F CD2 1 
ATOM   1510 C  CE1 . PHE B 1 45  ? 0.642   9.012   1.838   1.00 14.48  ? 45   PHE F CE1 1 
ATOM   1511 C  CE2 . PHE B 1 45  ? 2.846   9.388   1.044   1.00 14.21  ? 45   PHE F CE2 1 
ATOM   1512 C  CZ  . PHE B 1 45  ? 1.824   8.531   1.347   1.00 14.15  ? 45   PHE F CZ  1 
ATOM   1513 N  N   . HIS B 1 46  ? 1.838   12.809  5.305   1.00 9.50   ? 46   HIS F N   1 
ATOM   1514 C  CA  . HIS B 1 46  ? 2.866   12.924  6.341   1.00 9.53   ? 46   HIS F CA  1 
ATOM   1515 C  C   . HIS B 1 46  ? 2.885   11.699  7.222   1.00 8.88   ? 46   HIS F C   1 
ATOM   1516 O  O   . HIS B 1 46  ? 1.853   11.056  7.469   1.00 9.45   ? 46   HIS F O   1 
ATOM   1517 C  CB  . HIS B 1 46  ? 2.650   14.114  7.280   1.00 11.18  ? 46   HIS F CB  1 
ATOM   1518 C  CG  . HIS B 1 46  ? 2.194   15.335  6.595   1.00 10.60  ? 46   HIS F CG  1 
ATOM   1519 N  ND1 . HIS B 1 46  ? 0.940   15.733  6.699   1.00 12.33  ? 46   HIS F ND1 1 
ATOM   1520 C  CD2 . HIS B 1 46  ? 2.863   16.189  5.750   1.00 11.75  ? 46   HIS F CD2 1 
ATOM   1521 C  CE1 . HIS B 1 46  ? 0.794   16.824  5.953   1.00 12.64  ? 46   HIS F CE1 1 
ATOM   1522 N  NE2 . HIS B 1 46  ? 1.970   17.130  5.367   1.00 11.83  ? 46   HIS F NE2 1 
ATOM   1523 N  N   . VAL B 1 47  ? 4.053   11.435  7.780   1.00 8.63   ? 47   VAL F N   1 
ATOM   1524 C  CA  . VAL B 1 47  ? 4.156   10.550  8.931   1.00 8.30   ? 47   VAL F CA  1 
ATOM   1525 C  C   . VAL B 1 47  ? 4.001   11.387  10.203  1.00 8.16   ? 47   VAL F C   1 
ATOM   1526 O  O   . VAL B 1 47  ? 4.734   12.374  10.396  1.00 8.84   ? 47   VAL F O   1 
ATOM   1527 C  CB  . VAL B 1 47  ? 5.504   9.805   8.956   1.00 8.83   ? 47   VAL F CB  1 
ATOM   1528 C  CG1 . VAL B 1 47  ? 5.562   8.876   10.157  1.00 9.57   ? 47   VAL F CG1 1 
ATOM   1529 C  CG2 . VAL B 1 47  ? 5.736   9.043   7.658   1.00 10.64  ? 47   VAL F CG2 1 
ATOM   1530 N  N   . HIS B 1 48  ? 3.012   11.012  11.022  1.00 8.89   ? 48   HIS F N   1 
ATOM   1531 C  CA  . HIS B 1 48  ? 2.751   11.617  12.308  1.00 9.32   ? 48   HIS F CA  1 
ATOM   1532 C  C   . HIS B 1 48  ? 3.406   10.802  13.405  1.00 9.93   ? 48   HIS F C   1 
ATOM   1533 O  O   . HIS B 1 48  ? 3.712   9.640   13.227  1.00 13.15  ? 48   HIS F O   1 
ATOM   1534 C  CB  . HIS B 1 48  ? 1.250   11.772  12.529  1.00 9.87   ? 48   HIS F CB  1 
ATOM   1535 C  CG  . HIS B 1 48  ? 0.601   12.804  11.633  1.00 9.79   ? 48   HIS F CG  1 
ATOM   1536 N  ND1 . HIS B 1 48  ? -0.015  13.891  12.144  1.00 9.84   ? 48   HIS F ND1 1 
ATOM   1537 C  CD2 . HIS B 1 48  ? 0.521   12.932  10.255  1.00 10.71  ? 48   HIS F CD2 1 
ATOM   1538 C  CE1 . HIS B 1 48  ? -0.502  14.623  11.112  1.00 10.11  ? 48   HIS F CE1 1 
ATOM   1539 N  NE2 . HIS B 1 48  ? -0.176  14.057  9.965   1.00 10.77  ? 48   HIS F NE2 1 
ATOM   1540 N  N   A GLU B 1 49  ? 3.599   11.443  14.540  0.70 9.62   ? 49   GLU F N   1 
ATOM   1541 N  N   B GLU B 1 49  ? 3.622   11.473  14.543  0.30 10.30  ? 49   GLU F N   1 
ATOM   1542 C  CA  A GLU B 1 49  ? 4.454   10.901  15.570  0.70 10.22  ? 49   GLU F CA  1 
ATOM   1543 C  CA  B GLU B 1 49  ? 4.559   11.039  15.597  0.30 10.97  ? 49   GLU F CA  1 
ATOM   1544 C  C   A GLU B 1 49  ? 4.029   9.550   16.114  0.70 9.70   ? 49   GLU F C   1 
ATOM   1545 C  C   B GLU B 1 49  ? 4.119   9.730   16.322  0.30 10.59  ? 49   GLU F C   1 
ATOM   1546 O  O   A GLU B 1 49  ? 4.822   8.623   16.226  0.70 10.12  ? 49   GLU F O   1 
ATOM   1547 O  O   B GLU B 1 49  ? 5.026   8.962   16.681  0.30 11.05  ? 49   GLU F O   1 
ATOM   1548 C  CB  A GLU B 1 49  ? 4.511   11.921  16.706  0.70 10.00  ? 49   GLU F CB  1 
ATOM   1549 C  CB  B GLU B 1 49  ? 4.861   12.247  16.564  0.30 11.29  ? 49   GLU F CB  1 
ATOM   1550 C  CG  A GLU B 1 49  ? 5.494   11.475  17.751  0.70 10.73  ? 49   GLU F CG  1 
ATOM   1551 C  CG  B GLU B 1 49  ? 5.937   12.108  17.668  0.30 11.16  ? 49   GLU F CG  1 
ATOM   1552 C  CD  A GLU B 1 49  ? 5.633   12.487  18.810  0.70 11.83  ? 49   GLU F CD  1 
ATOM   1553 C  CD  B GLU B 1 49  ? 7.356   12.690  17.366  0.30 12.13  ? 49   GLU F CD  1 
ATOM   1554 O  OE1 A GLU B 1 49  ? 4.904   13.505  18.745  0.70 12.87  ? 49   GLU F OE1 1 
ATOM   1555 O  OE1 B GLU B 1 49  ? 7.561   13.872  16.737  0.30 10.49  ? 49   GLU F OE1 1 
ATOM   1556 O  OE2 A GLU B 1 49  ? 6.481   12.250  19.701  0.70 14.87  ? 49   GLU F OE2 1 
ATOM   1557 O  OE2 B GLU B 1 49  ? 8.292   11.960  17.886  0.30 13.28  ? 49   GLU F OE2 1 
ATOM   1558 N  N   . PHE B 1 50  ? 2.792   9.482   16.511  1.00 9.88   ? 50   PHE F N   1 
ATOM   1559 C  CA  . PHE B 1 50  ? 2.331   8.314   17.270  1.00 10.22  ? 50   PHE F CA  1 
ATOM   1560 C  C   . PHE B 1 50  ? 1.596   7.345   16.371  1.00 9.82   ? 50   PHE F C   1 
ATOM   1561 O  O   . PHE B 1 50  ? 0.772   7.749   15.538  1.00 11.87  ? 50   PHE F O   1 
ATOM   1562 C  CB  . PHE B 1 50  ? 1.426   8.724   18.433  1.00 10.95  ? 50   PHE F CB  1 
ATOM   1563 C  CG  . PHE B 1 50  ? 1.958   9.813   19.266  1.00 12.22  ? 50   PHE F CG  1 
ATOM   1564 C  CD1 . PHE B 1 50  ? 3.165   9.688   19.892  1.00 14.41  ? 50   PHE F CD1 1 
ATOM   1565 C  CD2 . PHE B 1 50  ? 1.265   11.023  19.390  1.00 13.06  ? 50   PHE F CD2 1 
ATOM   1566 C  CE1 . PHE B 1 50  ? 3.653   10.773  20.634  1.00 15.23  ? 50   PHE F CE1 1 
ATOM   1567 C  CE2 . PHE B 1 50  ? 1.743   12.072  20.140  1.00 14.34  ? 50   PHE F CE2 1 
ATOM   1568 C  CZ  . PHE B 1 50  ? 2.957   11.940  20.710  1.00 14.70  ? 50   PHE F CZ  1 
ATOM   1569 N  N   . GLY B 1 51  ? 1.839   6.070   16.588  1.00 9.15   ? 51   GLY F N   1 
ATOM   1570 C  CA  . GLY B 1 51  ? 1.045   5.012   15.965  1.00 9.13   ? 51   GLY F CA  1 
ATOM   1571 C  C   . GLY B 1 51  ? -0.209  4.673   16.763  1.00 9.59   ? 51   GLY F C   1 
ATOM   1572 O  O   . GLY B 1 51  ? -0.521  3.513   17.006  1.00 10.50  ? 51   GLY F O   1 
ATOM   1573 N  N   . ASP B 1 52  ? -0.913  5.714   17.190  1.00 11.12  ? 52   ASP F N   1 
ATOM   1574 C  CA  . ASP B 1 52  ? -2.084  5.639   18.051  1.00 10.56  ? 52   ASP F CA  1 
ATOM   1575 C  C   . ASP B 1 52  ? -3.284  6.065   17.267  1.00 10.74  ? 52   ASP F C   1 
ATOM   1576 O  O   . ASP B 1 52  ? -3.373  7.223   16.871  1.00 11.81  ? 52   ASP F O   1 
ATOM   1577 C  CB  . ASP B 1 52  ? -1.859  6.520   19.279  1.00 10.95  ? 52   ASP F CB  1 
ATOM   1578 C  CG  . ASP B 1 52  ? -2.918  6.337   20.325  1.00 11.21  ? 52   ASP F CG  1 
ATOM   1579 O  OD1 . ASP B 1 52  ? -3.987  5.773   20.015  1.00 12.14  ? 52   ASP F OD1 1 
ATOM   1580 O  OD2 . ASP B 1 52  ? -2.697  6.806   21.480  1.00 14.05  ? 52   ASP F OD2 1 
ATOM   1581 N  N   A ASN B 1 53  ? -4.203  5.139   17.030  0.50 11.27  ? 53   ASN F N   1 
ATOM   1582 N  N   B ASN B 1 53  ? -4.208  5.102   17.061  0.50 11.01  ? 53   ASN F N   1 
ATOM   1583 C  CA  A ASN B 1 53  ? -5.428  5.507   16.375  0.50 12.45  ? 53   ASN F CA  1 
ATOM   1584 C  CA  B ASN B 1 53  ? -5.500  5.292   16.371  0.50 12.11  ? 53   ASN F CA  1 
ATOM   1585 C  C   A ASN B 1 53  ? -6.648  5.191   17.290  0.50 11.47  ? 53   ASN F C   1 
ATOM   1586 C  C   B ASN B 1 53  ? -6.680  5.162   17.312  0.50 11.37  ? 53   ASN F C   1 
ATOM   1587 O  O   A ASN B 1 53  ? -7.757  4.947   16.814  0.50 12.66  ? 53   ASN F O   1 
ATOM   1588 O  O   B ASN B 1 53  ? -7.805  4.970   16.865  0.50 12.61  ? 53   ASN F O   1 
ATOM   1589 C  CB  A ASN B 1 53  ? -5.523  4.878   14.955  0.50 12.40  ? 53   ASN F CB  1 
ATOM   1590 C  CB  B ASN B 1 53  ? -5.726  4.255   15.241  0.50 14.07  ? 53   ASN F CB  1 
ATOM   1591 C  CG  A ASN B 1 53  ? -4.344  5.233   13.999  0.50 11.50  ? 53   ASN F CG  1 
ATOM   1592 C  CG  B ASN B 1 53  ? -6.841  4.665   14.256  0.50 14.06  ? 53   ASN F CG  1 
ATOM   1593 O  OD1 A ASN B 1 53  ? -3.557  6.192   14.193  0.50 12.39  ? 53   ASN F OD1 1 
ATOM   1594 O  OD1 B ASN B 1 53  ? -6.878  5.809   13.798  0.50 15.37  ? 53   ASN F OD1 1 
ATOM   1595 N  ND2 A ASN B 1 53  ? -4.259  4.459   12.935  0.50 11.53  ? 53   ASN F ND2 1 
ATOM   1596 N  ND2 B ASN B 1 53  ? -7.727  3.730   13.914  0.50 16.73  ? 53   ASN F ND2 1 
ATOM   1597 N  N   . THR B 1 54  ? -6.427  5.274   18.609  1.00 10.71  ? 54   THR F N   1 
ATOM   1598 C  CA  . THR B 1 54  ? -7.444  4.990   19.604  1.00 10.75  ? 54   THR F CA  1 
ATOM   1599 C  C   . THR B 1 54  ? -8.774  5.671   19.265  1.00 11.27  ? 54   THR F C   1 
ATOM   1600 O  O   . THR B 1 54  ? -9.838  5.036   19.289  1.00 13.02  ? 54   THR F O   1 
ATOM   1601 C  CB  . THR B 1 54  ? -6.987  5.419   21.018  1.00 11.43  ? 54   THR F CB  1 
ATOM   1602 O  OG1 . THR B 1 54  ? -5.864  4.636   21.438  1.00 12.82  ? 54   THR F OG1 1 
ATOM   1603 C  CG2 . THR B 1 54  ? -8.099  5.263   22.050  1.00 12.95  ? 54   THR F CG2 1 
ATOM   1604 N  N   . ALA B 1 55  ? -8.720  6.959   19.012  1.00 11.38  ? 55   ALA F N   1 
ATOM   1605 C  CA  . ALA B 1 55  ? -9.918  7.754   18.721  1.00 13.35  ? 55   ALA F CA  1 
ATOM   1606 C  C   . ALA B 1 55  ? -9.985  8.187   17.277  1.00 13.77  ? 55   ALA F C   1 
ATOM   1607 O  O   . ALA B 1 55  ? -10.588 9.196   16.979  1.00 17.94  ? 55   ALA F O   1 
ATOM   1608 C  CB  . ALA B 1 55  ? -9.988  8.958   19.641  1.00 15.99  ? 55   ALA F CB  1 
ATOM   1609 N  N   . GLY B 1 56  ? -9.348  7.440   16.391  1.00 13.35  ? 56   GLY F N   1 
ATOM   1610 C  CA  . GLY B 1 56  ? -9.190  7.806   15.001  1.00 13.65  ? 56   GLY F CA  1 
ATOM   1611 C  C   . GLY B 1 56  ? -7.863  8.489   14.738  1.00 12.24  ? 56   GLY F C   1 
ATOM   1612 O  O   . GLY B 1 56  ? -6.936  8.478   15.558  1.00 12.33  ? 56   GLY F O   1 
ATOM   1613 N  N   . CYS B 1 57  ? -7.759  9.090   13.564  1.00 12.86  ? 57   CYS F N   1 
ATOM   1614 C  CA  . CYS B 1 57  ? -6.496  9.666   13.121  1.00 12.18  ? 57   CYS F CA  1 
ATOM   1615 C  C   . CYS B 1 57  ? -5.977  10.825  13.976  1.00 11.89  ? 57   CYS F C   1 
ATOM   1616 O  O   . CYS B 1 57  ? -4.778  11.083  13.985  1.00 11.64  ? 57   CYS F O   1 
ATOM   1617 C  CB  . CYS B 1 57  ? -6.606  10.128  11.666  1.00 13.75  ? 57   CYS F CB  1 
ATOM   1618 S  SG  . CYS B 1 57  ? -7.083  8.768   10.516  1.00 14.62  ? 57   CYS F SG  1 
ATOM   1619 N  N   A THR B 1 58  ? -6.864  11.503  14.694  0.50 12.62  ? 58   THR F N   1 
ATOM   1620 N  N   B THR B 1 58  ? -6.860  11.496  14.707  0.50 12.58  ? 58   THR F N   1 
ATOM   1621 C  CA  A THR B 1 58  ? -6.447  12.570  15.562  0.50 13.27  ? 58   THR F CA  1 
ATOM   1622 C  CA  B THR B 1 58  ? -6.423  12.558  15.576  0.50 13.05  ? 58   THR F CA  1 
ATOM   1623 C  C   A THR B 1 58  ? -5.466  12.067  16.637  0.50 12.78  ? 58   THR F C   1 
ATOM   1624 C  C   B THR B 1 58  ? -5.452  12.060  16.641  0.50 12.64  ? 58   THR F C   1 
ATOM   1625 O  O   A THR B 1 58  ? -4.607  12.848  17.078  0.50 13.26  ? 58   THR F O   1 
ATOM   1626 O  O   B THR B 1 58  ? -4.590  12.837  17.078  0.50 13.26  ? 58   THR F O   1 
ATOM   1627 C  CB  A THR B 1 58  ? -7.687  13.231  16.196  0.50 16.46  ? 58   THR F CB  1 
ATOM   1628 C  CB  B THR B 1 58  ? -7.636  13.265  16.205  0.50 15.33  ? 58   THR F CB  1 
ATOM   1629 O  OG1 A THR B 1 58  ? -7.300  14.304  17.070  0.50 20.74  ? 58   THR F OG1 1 
ATOM   1630 O  OG1 B THR B 1 58  ? -8.530  12.271  16.730  0.50 19.64  ? 58   THR F OG1 1 
ATOM   1631 C  CG2 A THR B 1 58  ? -8.493  12.166  16.927  0.50 14.18  ? 58   THR F CG2 1 
ATOM   1632 C  CG2 B THR B 1 58  ? -8.329  14.045  15.109  0.50 15.46  ? 58   THR F CG2 1 
ATOM   1633 N  N   . SER B 1 59  ? -5.588  10.810  17.062  1.00 11.18  ? 59   SER F N   1 
ATOM   1634 C  CA  . SER B 1 59  ? -4.759  10.314  18.149  1.00 11.32  ? 59   SER F CA  1 
ATOM   1635 C  C   . SER B 1 59  ? -3.270  10.236  17.760  1.00 11.05  ? 59   SER F C   1 
ATOM   1636 O  O   . SER B 1 59  ? -2.413  10.067  18.625  1.00 11.69  ? 59   SER F O   1 
ATOM   1637 C  CB  . SER B 1 59  ? -5.283  8.941   18.593  1.00 10.76  ? 59   SER F CB  1 
ATOM   1638 O  OG  . SER B 1 59  ? -6.618  9.007   19.110  1.00 12.14  ? 59   SER F OG  1 
ATOM   1639 N  N   . ALA B 1 60  ? -2.947  10.348  16.460  1.00 10.27  ? 60   ALA F N   1 
ATOM   1640 C  CA  . ALA B 1 60  ? -1.602  10.218  16.005  1.00 10.08  ? 60   ALA F CA  1 
ATOM   1641 C  C   . ALA B 1 60  ? -0.705  11.421  16.324  1.00 9.95   ? 60   ALA F C   1 
ATOM   1642 O  O   . ALA B 1 60  ? 0.507   11.363  16.144  1.00 10.40  ? 60   ALA F O   1 
ATOM   1643 C  CB  . ALA B 1 60  ? -1.556  9.942   14.507  1.00 10.70  ? 60   ALA F CB  1 
ATOM   1644 N  N   . GLY B 1 61  ? -1.281  12.522  16.755  1.00 9.97   ? 61   GLY F N   1 
ATOM   1645 C  CA  . GLY B 1 61  ? -0.460  13.647  17.161  1.00 10.53  ? 61   GLY F CA  1 
ATOM   1646 C  C   . GLY B 1 61  ? 0.088   14.416  15.970  1.00 9.46   ? 61   GLY F C   1 
ATOM   1647 O  O   . GLY B 1 61  ? -0.444  14.351  14.861  1.00 9.75   ? 61   GLY F O   1 
ATOM   1648 N  N   . PRO B 1 62  ? 1.156   15.201  16.210  1.00 9.74   ? 62   PRO F N   1 
ATOM   1649 C  CA  . PRO B 1 62  ? 1.708   16.120  15.194  1.00 9.69   ? 62   PRO F CA  1 
ATOM   1650 C  C   . PRO B 1 62  ? 2.587   15.359  14.204  1.00 9.04   ? 62   PRO F C   1 
ATOM   1651 O  O   . PRO B 1 62  ? 2.789   14.159  14.320  1.00 8.80   ? 62   PRO F O   1 
ATOM   1652 C  CB  . PRO B 1 62  ? 2.500   17.109  16.056  1.00 11.41  ? 62   PRO F CB  1 
ATOM   1653 C  CG  . PRO B 1 62  ? 2.997   16.276  17.175  1.00 12.70  ? 62   PRO F CG  1 
ATOM   1654 C  CD  . PRO B 1 62  ? 1.885   15.312  17.480  1.00 11.37  ? 62   PRO F CD  1 
ATOM   1655 N  N   . HIS B 1 63  ? 3.098   16.065  13.211  1.00 9.91   ? 63   HIS F N   1 
ATOM   1656 C  CA  . HIS B 1 63  ? 4.041   15.447  12.284  1.00 9.30   ? 63   HIS F CA  1 
ATOM   1657 C  C   . HIS B 1 63  ? 5.240   14.911  13.059  1.00 8.82   ? 63   HIS F C   1 
ATOM   1658 O  O   . HIS B 1 63  ? 5.695   15.518  14.029  1.00 9.92   ? 63   HIS F O   1 
ATOM   1659 C  CB  . HIS B 1 63  ? 4.556   16.425  11.241  1.00 9.97   ? 63   HIS F CB  1 
ATOM   1660 C  CG  . HIS B 1 63  ? 3.478   17.004  10.369  1.00 10.09  ? 63   HIS F CG  1 
ATOM   1661 N  ND1 . HIS B 1 63  ? 3.743   17.953  9.423   1.00 9.82   ? 63   HIS F ND1 1 
ATOM   1662 C  CD2 . HIS B 1 63  ? 2.122   16.746  10.315  1.00 11.58  ? 63   HIS F CD2 1 
ATOM   1663 C  CE1 . HIS B 1 63  ? 2.590   18.256  8.827   1.00 10.72  ? 63   HIS F CE1 1 
ATOM   1664 N  NE2 . HIS B 1 63  ? 1.602   17.555  9.378   1.00 11.82  ? 63   HIS F NE2 1 
ATOM   1665 N  N   . PHE B 1 64  ? 5.785   13.768  12.618  1.00 8.64   ? 64   PHE F N   1 
ATOM   1666 C  CA  . PHE B 1 64  ? 6.964   13.186  13.250  1.00 8.65   ? 64   PHE F CA  1 
ATOM   1667 C  C   . PHE B 1 64  ? 8.166   14.153  13.051  1.00 8.42   ? 64   PHE F C   1 
ATOM   1668 O  O   . PHE B 1 64  ? 8.566   14.436  11.929  1.00 9.09   ? 64   PHE F O   1 
ATOM   1669 C  CB  . PHE B 1 64  ? 7.247   11.830  12.620  1.00 9.22   ? 64   PHE F CB  1 
ATOM   1670 C  CG  . PHE B 1 64  ? 8.456   11.134  13.181  1.00 9.78   ? 64   PHE F CG  1 
ATOM   1671 C  CD1 . PHE B 1 64  ? 8.739   11.074  14.531  1.00 10.82  ? 64   PHE F CD1 1 
ATOM   1672 C  CD2 . PHE B 1 64  ? 9.315   10.480  12.319  1.00 10.67  ? 64   PHE F CD2 1 
ATOM   1673 C  CE1 . PHE B 1 64  ? 9.863   10.414  15.015  1.00 12.76  ? 64   PHE F CE1 1 
ATOM   1674 C  CE2 . PHE B 1 64  ? 10.441  9.793   12.795  1.00 12.46  ? 64   PHE F CE2 1 
ATOM   1675 C  CZ  . PHE B 1 64  ? 10.717  9.785   14.148  1.00 13.39  ? 64   PHE F CZ  1 
ATOM   1676 N  N   . ASN B 1 65  ? 8.694   14.612  14.167  1.00 9.09   ? 65   ASN F N   1 
ATOM   1677 C  CA  . ASN B 1 65  ? 9.646   15.717  14.177  1.00 9.12   ? 65   ASN F CA  1 
ATOM   1678 C  C   . ASN B 1 65  ? 10.733  15.500  15.222  1.00 9.74   ? 65   ASN F C   1 
ATOM   1679 O  O   . ASN B 1 65  ? 10.882  16.281  16.160  1.00 10.19  ? 65   ASN F O   1 
ATOM   1680 C  CB  . ASN B 1 65  ? 8.896   17.031  14.442  1.00 9.68   ? 65   ASN F CB  1 
ATOM   1681 C  CG  . ASN B 1 65  ? 9.783   18.250  14.331  1.00 10.11  ? 65   ASN F CG  1 
ATOM   1682 O  OD1 . ASN B 1 65  ? 10.835  18.228  13.688  1.00 10.37  ? 65   ASN F OD1 1 
ATOM   1683 N  ND2 . ASN B 1 65  ? 9.322   19.334  14.936  1.00 11.05  ? 65   ASN F ND2 1 
ATOM   1684 N  N   . PRO B 1 66  ? 11.512  14.416  15.089  1.00 10.23  ? 66   PRO F N   1 
ATOM   1685 C  CA  . PRO B 1 66  ? 12.505  14.099  16.129  1.00 10.89  ? 66   PRO F CA  1 
ATOM   1686 C  C   . PRO B 1 66  ? 13.584  15.164  16.298  1.00 11.45  ? 66   PRO F C   1 
ATOM   1687 O  O   . PRO B 1 66  ? 14.166  15.242  17.365  1.00 12.47  ? 66   PRO F O   1 
ATOM   1688 C  CB  . PRO B 1 66  ? 13.099  12.763  15.636  1.00 12.04  ? 66   PRO F CB  1 
ATOM   1689 C  CG  . PRO B 1 66  ? 12.878  12.785  14.152  1.00 11.79  ? 66   PRO F CG  1 
ATOM   1690 C  CD  . PRO B 1 66  ? 11.535  13.459  13.966  1.00 10.39  ? 66   PRO F CD  1 
ATOM   1691 N  N   . LEU B 1 67  ? 13.830  15.950  15.251  1.00 10.96  ? 67   LEU F N   1 
ATOM   1692 C  CA  . LEU B 1 67  ? 14.914  16.933  15.255  1.00 11.47  ? 67   LEU F CA  1 
ATOM   1693 C  C   . LEU B 1 67  ? 14.434  18.341  15.597  1.00 10.61  ? 67   LEU F C   1 
ATOM   1694 O  O   . LEU B 1 67  ? 15.233  19.277  15.553  1.00 11.28  ? 67   LEU F O   1 
ATOM   1695 C  CB  . LEU B 1 67  ? 15.671  16.910  13.913  1.00 12.94  ? 67   LEU F CB  1 
ATOM   1696 C  CG  . LEU B 1 67  ? 16.578  15.709  13.676  1.00 17.33  ? 67   LEU F CG  1 
ATOM   1697 C  CD1 . LEU B 1 67  ? 16.922  15.549  12.210  1.00 18.64  ? 67   LEU F CD1 1 
ATOM   1698 C  CD2 . LEU B 1 67  ? 17.854  15.828  14.503  1.00 20.09  ? 67   LEU F CD2 1 
ATOM   1699 N  N   . SER B 1 68  ? 13.168  18.521  15.959  1.00 10.05  ? 68   SER F N   1 
ATOM   1700 C  CA  . SER B 1 68  ? 12.684  19.836  16.428  1.00 10.15  ? 68   SER F CA  1 
ATOM   1701 C  C   . SER B 1 68  ? 12.846  20.940  15.384  1.00 10.02  ? 68   SER F C   1 
ATOM   1702 O  O   . SER B 1 68  ? 13.295  22.031  15.701  1.00 11.52  ? 68   SER F O   1 
ATOM   1703 C  CB  . SER B 1 68  ? 13.355  20.231  17.759  1.00 10.30  ? 68   SER F CB  1 
ATOM   1704 O  OG  . SER B 1 68  ? 13.029  19.345  18.800  1.00 11.06  ? 68   SER F OG  1 
ATOM   1705 N  N   . ARG B 1 69  ? 12.432  20.644  14.158  1.00 11.30  ? 69   ARG F N   1 
ATOM   1706 C  CA  . ARG B 1 69  ? 12.434  21.605  13.072  1.00 12.00  ? 69   ARG F CA  1 
ATOM   1707 C  C   . ARG B 1 69  ? 11.056  22.118  12.753  1.00 12.03  ? 69   ARG F C   1 
ATOM   1708 O  O   . ARG B 1 69  ? 10.046  21.583  13.209  1.00 12.01  ? 69   ARG F O   1 
ATOM   1709 C  CB  . ARG B 1 69  ? 13.025  20.961  11.816  1.00 13.48  ? 69   ARG F CB  1 
ATOM   1710 C  CG  . ARG B 1 69  ? 14.376  20.313  11.972  1.00 15.60  ? 69   ARG F CG  1 
ATOM   1711 C  CD  . ARG B 1 69  ? 15.400  21.237  12.558  1.00 17.11  ? 69   ARG F CD  1 
ATOM   1712 N  NE  . ARG B 1 69  ? 15.679  22.351  11.672  0.70 16.83  ? 69   ARG F NE  1 
ATOM   1713 C  CZ  . ARG B 1 69  ? 16.470  22.294  10.599  0.70 17.94  ? 69   ARG F CZ  1 
ATOM   1714 N  NH1 . ARG B 1 69  ? 17.055  21.156  10.261  0.70 20.64  ? 69   ARG F NH1 1 
ATOM   1715 N  NH2 . ARG B 1 69  ? 16.692  23.389  9.856   0.70 20.65  ? 69   ARG F NH2 1 
ATOM   1716 N  N   . LYS B 1 70  ? 10.995  23.156  11.939  1.00 14.00  ? 70   LYS F N   1 
ATOM   1717 C  CA  . LYS B 1 70  ? 9.745   23.625  11.356  1.00 13.97  ? 70   LYS F CA  1 
ATOM   1718 C  C   . LYS B 1 70  ? 9.346   22.761  10.167  1.00 12.52  ? 70   LYS F C   1 
ATOM   1719 O  O   . LYS B 1 70  ? 10.160  22.084  9.545   1.00 13.17  ? 70   LYS F O   1 
ATOM   1720 C  CB  . LYS B 1 70  ? 9.868   25.097  10.926  1.00 16.24  ? 70   LYS F CB  1 
ATOM   1721 C  CG  . LYS B 1 70  ? 9.955   26.101  12.064  1.00 21.41  ? 70   LYS F CG  1 
ATOM   1722 C  CD  . LYS B 1 70  ? 10.124  27.480  11.461  1.00 24.77  ? 70   LYS F CD  1 
ATOM   1723 C  CE  . LYS B 1 70  ? 9.563   28.587  12.301  1.00 26.54  ? 70   LYS F CE  1 
ATOM   1724 N  NZ  . LYS B 1 70  ? 9.986   29.826  11.630  1.00 30.33  ? 70   LYS F NZ  1 
ATOM   1725 N  N   . HIS B 1 71  ? 8.067   22.838  9.843   1.00 12.61  ? 71   HIS F N   1 
ATOM   1726 C  CA  . HIS B 1 71  ? 7.492   22.110  8.727   1.00 11.95  ? 71   HIS F CA  1 
ATOM   1727 C  C   . HIS B 1 71  ? 8.069   22.587  7.390   1.00 12.43  ? 71   HIS F C   1 
ATOM   1728 O  O   . HIS B 1 71  ? 8.276   23.808  7.174   1.00 14.37  ? 71   HIS F O   1 
ATOM   1729 C  CB  . HIS B 1 71  ? 5.986   22.313  8.741   1.00 11.81  ? 71   HIS F CB  1 
ATOM   1730 C  CG  . HIS B 1 71  ? 5.278   21.606  7.650   1.00 11.54  ? 71   HIS F CG  1 
ATOM   1731 N  ND1 . HIS B 1 71  ? 5.066   20.256  7.638   1.00 10.76  ? 71   HIS F ND1 1 
ATOM   1732 C  CD2 . HIS B 1 71  ? 4.738   22.118  6.483   1.00 12.16  ? 71   HIS F CD2 1 
ATOM   1733 C  CE1 . HIS B 1 71  ? 4.469   19.957  6.499   1.00 10.85  ? 71   HIS F CE1 1 
ATOM   1734 N  NE2 . HIS B 1 71  ? 4.226   21.087  5.812   1.00 12.13  ? 71   HIS F NE2 1 
ATOM   1735 N  N   . GLY B 1 72  ? 8.252   21.645  6.455   1.00 12.65  ? 72   GLY F N   1 
ATOM   1736 C  CA  . GLY B 1 72  ? 8.697   21.984  5.095   1.00 13.01  ? 72   GLY F CA  1 
ATOM   1737 C  C   . GLY B 1 72  ? 8.220   20.934  4.119   1.00 12.81  ? 72   GLY F C   1 
ATOM   1738 O  O   . GLY B 1 72  ? 7.361   20.074  4.446   1.00 13.51  ? 72   GLY F O   1 
ATOM   1739 N  N   . GLY B 1 73  ? 8.749   21.009  2.900   1.00 14.13  ? 73   GLY F N   1 
ATOM   1740 C  CA  . GLY B 1 73  ? 8.556   19.967  1.898   1.00 14.49  ? 73   GLY F CA  1 
ATOM   1741 C  C   . GLY B 1 73  ? 9.694   18.973  1.951   1.00 13.50  ? 73   GLY F C   1 
ATOM   1742 O  O   . GLY B 1 73  ? 10.748  19.201  2.557   1.00 14.62  ? 73   GLY F O   1 
ATOM   1743 N  N   . PRO B 1 74  ? 9.492   17.838  1.289   1.00 13.92  ? 74   PRO F N   1 
ATOM   1744 C  CA  . PRO B 1 74  ? 10.478  16.793  1.382   1.00 14.73  ? 74   PRO F CA  1 
ATOM   1745 C  C   . PRO B 1 74  ? 11.847  17.189  0.829   1.00 14.74  ? 74   PRO F C   1 
ATOM   1746 O  O   . PRO B 1 74  ? 12.842  16.651  1.284   1.00 16.69  ? 74   PRO F O   1 
ATOM   1747 C  CB  . PRO B 1 74  ? 9.838   15.634  0.594   1.00 16.46  ? 74   PRO F CB  1 
ATOM   1748 C  CG  . PRO B 1 74  ? 8.755   16.223  -0.240  1.00 17.24  ? 74   PRO F CG  1 
ATOM   1749 C  CD  . PRO B 1 74  ? 8.299   17.437  0.520   1.00 15.11  ? 74   PRO F CD  1 
ATOM   1750 N  N   . LYS B 1 75  ? 11.897  18.124  -0.125  1.00 15.38  ? 75   LYS F N   1 
ATOM   1751 C  CA  . LYS B 1 75  ? 13.178  18.559  -0.680  1.00 17.40  ? 75   LYS F CA  1 
ATOM   1752 C  C   . LYS B 1 75  ? 13.949  19.553  0.187   1.00 18.86  ? 75   LYS F C   1 
ATOM   1753 O  O   . LYS B 1 75  ? 15.091  19.886  -0.115  1.00 22.88  ? 75   LYS F O   1 
ATOM   1754 C  CB  . LYS B 1 75  ? 12.957  19.219  -2.039  1.00 20.26  ? 75   LYS F CB  1 
ATOM   1755 C  CG  . LYS B 1 75  ? 12.427  18.282  -3.099  1.00 23.09  ? 75   LYS F CG  1 
ATOM   1756 C  CD  . LYS B 1 75  ? 12.471  18.888  -4.493  1.00 28.94  ? 75   LYS F CD  1 
ATOM   1757 C  CE  . LYS B 1 75  ? 11.330  19.844  -4.748  1.00 35.84  ? 75   LYS F CE  1 
ATOM   1758 N  NZ  . LYS B 1 75  ? 11.165  20.082  -6.212  1.00 43.47  ? 75   LYS F NZ  1 
ATOM   1759 N  N   . ASP B 1 76  ? 13.301  20.092  1.204   1.00 16.85  ? 76   ASP F N   1 
ATOM   1760 C  CA  . ASP B 1 76  ? 13.880  21.131  2.028   1.00 17.09  ? 76   ASP F CA  1 
ATOM   1761 C  C   . ASP B 1 76  ? 14.771  20.567  3.132   1.00 17.15  ? 76   ASP F C   1 
ATOM   1762 O  O   . ASP B 1 76  ? 14.501  19.524  3.686   1.00 18.56  ? 76   ASP F O   1 
ATOM   1763 C  CB  . ASP B 1 76  ? 12.773  21.943  2.665   1.00 18.08  ? 76   ASP F CB  1 
ATOM   1764 C  CG  . ASP B 1 76  ? 11.909  22.649  1.646   1.00 19.81  ? 76   ASP F CG  1 
ATOM   1765 O  OD1 . ASP B 1 76  ? 12.383  22.974  0.532   1.00 25.99  ? 76   ASP F OD1 1 
ATOM   1766 O  OD2 . ASP B 1 76  ? 10.746  22.894  1.986   1.00 21.17  ? 76   ASP F OD2 1 
ATOM   1767 N  N   A GLU B 1 77  ? 15.825  21.286  3.506   0.50 17.27  ? 77   GLU F N   1 
ATOM   1768 N  N   B GLU B 1 77  ? 15.858  21.288  3.376   0.50 18.11  ? 77   GLU F N   1 
ATOM   1769 C  CA  A GLU B 1 77  ? 16.600  20.916  4.696   0.50 16.38  ? 77   GLU F CA  1 
ATOM   1770 C  CA  B GLU B 1 77  ? 16.778  21.029  4.456   0.50 19.76  ? 77   GLU F CA  1 
ATOM   1771 C  C   A GLU B 1 77  ? 15.763  21.151  5.960   0.50 16.02  ? 77   GLU F C   1 
ATOM   1772 C  C   B GLU B 1 77  ? 16.030  21.135  5.788   0.50 18.15  ? 77   GLU F C   1 
ATOM   1773 O  O   A GLU B 1 77  ? 15.775  20.332  6.888   0.50 16.08  ? 77   GLU F O   1 
ATOM   1774 O  O   B GLU B 1 77  ? 16.127  20.279  6.674   0.50 19.36  ? 77   GLU F O   1 
ATOM   1775 C  CB  A GLU B 1 77  ? 17.920  21.705  4.754   0.50 16.68  ? 77   GLU F CB  1 
ATOM   1776 C  CB  B GLU B 1 77  ? 17.901  22.068  4.359   0.50 22.66  ? 77   GLU F CB  1 
ATOM   1777 C  CG  A GLU B 1 77  ? 18.893  21.233  5.822   0.50 18.43  ? 77   GLU F CG  1 
ATOM   1778 C  CG  B GLU B 1 77  ? 17.471  23.544  4.421   0.50 26.84  ? 77   GLU F CG  1 
ATOM   1779 C  CD  A GLU B 1 77  ? 18.613  21.830  7.187   0.50 21.39  ? 77   GLU F CD  1 
ATOM   1780 C  CD  B GLU B 1 77  ? 16.332  23.978  3.470   0.50 29.19  ? 77   GLU F CD  1 
ATOM   1781 O  OE1 A GLU B 1 77  ? 18.032  22.934  7.273   0.50 21.52  ? 77   GLU F OE1 1 
ATOM   1782 O  OE1 B GLU B 1 77  ? 16.506  23.940  2.210   0.50 42.83  ? 77   GLU F OE1 1 
ATOM   1783 O  OE2 A GLU B 1 77  ? 18.979  21.188  8.185   0.50 22.72  ? 77   GLU F OE2 1 
ATOM   1784 O  OE2 B GLU B 1 77  ? 15.261  24.407  4.000   0.50 20.04  ? 77   GLU F OE2 1 
ATOM   1785 N  N   A GLU B 1 78  ? 15.044  22.272  5.991   0.90 16.73  ? 78   GLU F N   1 
ATOM   1786 N  N   B GLU B 1 78  ? 15.261  22.223  5.905   0.10 16.78  ? 78   GLU F N   1 
ATOM   1787 C  CA  A GLU B 1 78  ? 14.213  22.582  7.128   0.90 16.37  ? 78   GLU F CA  1 
ATOM   1788 C  CA  B GLU B 1 78  ? 14.372  22.453  7.052   0.10 15.92  ? 78   GLU F CA  1 
ATOM   1789 C  C   A GLU B 1 78  ? 12.898  21.874  6.866   0.90 15.05  ? 78   GLU F C   1 
ATOM   1790 C  C   B GLU B 1 78  ? 12.997  21.831  6.802   0.10 14.26  ? 78   GLU F C   1 
ATOM   1791 O  O   A GLU B 1 78  ? 12.039  22.363  6.139   0.90 15.62  ? 78   GLU F O   1 
ATOM   1792 O  O   B GLU B 1 78  ? 12.193  22.348  6.029   0.10 15.23  ? 78   GLU F O   1 
ATOM   1793 C  CB  A GLU B 1 78  ? 14.022  24.082  7.282   0.90 18.13  ? 78   GLU F CB  1 
ATOM   1794 C  CB  B GLU B 1 78  ? 14.204  23.951  7.364   0.10 17.12  ? 78   GLU F CB  1 
ATOM   1795 C  CG  A GLU B 1 78  ? 13.143  24.475  8.460   0.90 19.77  ? 78   GLU F CG  1 
ATOM   1796 C  CG  B GLU B 1 78  ? 13.303  24.213  8.571   0.10 18.00  ? 78   GLU F CG  1 
ATOM   1797 C  CD  A GLU B 1 78  ? 13.924  24.730  9.721   0.90 25.15  ? 78   GLU F CD  1 
ATOM   1798 C  CD  B GLU B 1 78  ? 13.021  25.689  8.845   0.10 15.89  ? 78   GLU F CD  1 
ATOM   1799 O  OE1 A GLU B 1 78  ? 15.014  25.324  9.615   0.50 27.90  ? 78   GLU F OE1 1 
ATOM   1800 O  OE1 B GLU B 1 78  ? 12.316  26.346  8.049   0.10 14.42  ? 78   GLU F OE1 1 
ATOM   1801 O  OE2 A GLU B 1 78  ? 13.478  24.401  10.827  0.50 24.20  ? 78   GLU F OE2 1 
ATOM   1802 O  OE2 B GLU B 1 78  ? 13.478  26.187  9.893   0.10 14.87  ? 78   GLU F OE2 1 
ATOM   1803 N  N   . ARG B 1 79  ? 12.756  20.711  7.470   1.00 13.31  ? 79   ARG F N   1 
ATOM   1804 C  CA  . ARG B 1 79  ? 11.513  19.936  7.373   1.00 12.22  ? 79   ARG F CA  1 
ATOM   1805 C  C   . ARG B 1 79  ? 11.442  19.068  8.622   1.00 11.37  ? 79   ARG F C   1 
ATOM   1806 O  O   . ARG B 1 79  ? 12.439  18.830  9.295   1.00 12.48  ? 79   ARG F O   1 
ATOM   1807 C  CB  . ARG B 1 79  ? 11.502  19.033  6.134   1.00 12.14  ? 79   ARG F CB  1 
ATOM   1808 C  CG  . ARG B 1 79  ? 12.686  18.084  6.040   1.00 13.01  ? 79   ARG F CG  1 
ATOM   1809 C  CD  . ARG B 1 79  ? 12.547  17.107  4.896   1.00 13.28  ? 79   ARG F CD  1 
ATOM   1810 N  NE  . ARG B 1 79  ? 11.778  15.905  5.265   1.00 12.14  ? 79   ARG F NE  1 
ATOM   1811 C  CZ  . ARG B 1 79  ? 11.735  14.800  4.531   1.00 12.37  ? 79   ARG F CZ  1 
ATOM   1812 N  NH1 . ARG B 1 79  ? 12.329  14.768  3.353   1.00 13.91  ? 79   ARG F NH1 1 
ATOM   1813 N  NH2 . ARG B 1 79  ? 11.129  13.692  4.971   1.00 12.57  ? 79   ARG F NH2 1 
ATOM   1814 N  N   . HIS B 1 80  ? 10.238  18.566  8.869   1.00 10.67  ? 80   HIS F N   1 
ATOM   1815 C  CA  . HIS B 1 80  ? 10.036  17.462  9.796   1.00 10.34  ? 80   HIS F CA  1 
ATOM   1816 C  C   . HIS B 1 80  ? 10.488  16.170  9.103   1.00 9.86   ? 80   HIS F C   1 
ATOM   1817 O  O   . HIS B 1 80  ? 10.293  16.012  7.889   1.00 10.19  ? 80   HIS F O   1 
ATOM   1818 C  CB  . HIS B 1 80  ? 8.562   17.336  10.139  1.00 9.88   ? 80   HIS F CB  1 
ATOM   1819 C  CG  . HIS B 1 80  ? 7.974   18.573  10.730  1.00 9.64   ? 80   HIS F CG  1 
ATOM   1820 N  ND1 . HIS B 1 80  ? 6.689   18.993  10.493  1.00 9.76   ? 80   HIS F ND1 1 
ATOM   1821 C  CD2 . HIS B 1 80  ? 8.508   19.420  11.660  1.00 10.90  ? 80   HIS F CD2 1 
ATOM   1822 C  CE1 . HIS B 1 80  ? 6.460   20.052  11.284  1.00 10.61  ? 80   HIS F CE1 1 
ATOM   1823 N  NE2 . HIS B 1 80  ? 7.560   20.318  11.980  1.00 11.05  ? 80   HIS F NE2 1 
ATOM   1824 N  N   . VAL B 1 81  ? 10.966  15.187  9.870   1.00 9.84   ? 81   VAL F N   1 
ATOM   1825 C  CA  . VAL B 1 81  ? 11.256  13.877  9.257   1.00 10.26  ? 81   VAL F CA  1 
ATOM   1826 C  C   . VAL B 1 81  ? 9.999   13.352  8.541   1.00 9.71   ? 81   VAL F C   1 
ATOM   1827 O  O   . VAL B 1 81  ? 10.115  12.781  7.461   1.00 10.56  ? 81   VAL F O   1 
ATOM   1828 C  CB  . VAL B 1 81  ? 11.818  12.882  10.280  1.00 10.89  ? 81   VAL F CB  1 
ATOM   1829 C  CG1 . VAL B 1 81  ? 11.851  11.461  9.707   1.00 11.83  ? 81   VAL F CG1 1 
ATOM   1830 C  CG2 . VAL B 1 81  ? 13.211  13.312  10.701  1.00 12.13  ? 81   VAL F CG2 1 
ATOM   1831 N  N   . GLY B 1 82  ? 8.813   13.543  9.131   1.00 9.47   ? 82   GLY F N   1 
ATOM   1832 C  CA  . GLY B 1 82  ? 7.601   13.015  8.516   1.00 9.78   ? 82   GLY F CA  1 
ATOM   1833 C  C   . GLY B 1 82  ? 7.053   13.762  7.323   1.00 10.05  ? 82   GLY F C   1 
ATOM   1834 O  O   . GLY B 1 82  ? 5.984   13.369  6.844   1.00 11.00  ? 82   GLY F O   1 
ATOM   1835 N  N   . ASP B 1 83  ? 7.724   14.799  6.838   1.00 9.50   ? 83   ASP F N   1 
ATOM   1836 C  CA  . ASP B 1 83  ? 7.178   15.637  5.759   1.00 10.56  ? 83   ASP F CA  1 
ATOM   1837 C  C   . ASP B 1 83  ? 7.402   15.032  4.375   1.00 10.73  ? 83   ASP F C   1 
ATOM   1838 O  O   . ASP B 1 83  ? 8.451   15.207  3.769   1.00 14.02  ? 83   ASP F O   1 
ATOM   1839 C  CB  . ASP B 1 83  ? 7.800   17.029  5.831   1.00 10.69  ? 83   ASP F CB  1 
ATOM   1840 C  CG  . ASP B 1 83  ? 7.292   17.836  6.991   1.00 10.13  ? 83   ASP F CG  1 
ATOM   1841 O  OD1 . ASP B 1 83  ? 6.232   17.441  7.602   1.00 9.88   ? 83   ASP F OD1 1 
ATOM   1842 O  OD2 . ASP B 1 83  ? 7.919   18.855  7.329   1.00 11.10  ? 83   ASP F OD2 1 
ATOM   1843 N  N   . LEU B 1 84  ? 6.375   14.352  3.863   1.00 10.30  ? 84   LEU F N   1 
ATOM   1844 C  CA  . LEU B 1 84  ? 6.427   13.704  2.557   1.00 11.18  ? 84   LEU F CA  1 
ATOM   1845 C  C   . LEU B 1 84  ? 5.633   14.480  1.494   1.00 12.08  ? 84   LEU F C   1 
ATOM   1846 O  O   . LEU B 1 84  ? 5.387   13.964  0.396   1.00 14.30  ? 84   LEU F O   1 
ATOM   1847 C  CB  . LEU B 1 84  ? 5.974   12.256  2.623   1.00 11.39  ? 84   LEU F CB  1 
ATOM   1848 C  CG  . LEU B 1 84  ? 6.860   11.373  3.506   1.00 12.47  ? 84   LEU F CG  1 
ATOM   1849 C  CD1 . LEU B 1 84  ? 6.289   9.955   3.557   1.00 14.21  ? 84   LEU F CD1 1 
ATOM   1850 C  CD2 . LEU B 1 84  ? 8.307   11.359  2.997   1.00 14.80  ? 84   LEU F CD2 1 
ATOM   1851 N  N   . GLY B 1 85  ? 5.282   15.727  1.777   1.00 11.42  ? 85   GLY F N   1 
ATOM   1852 C  CA  . GLY B 1 85  ? 4.720   16.613  0.768   1.00 12.72  ? 85   GLY F CA  1 
ATOM   1853 C  C   . GLY B 1 85  ? 3.251   16.349  0.530   1.00 12.04  ? 85   GLY F C   1 
ATOM   1854 O  O   . GLY B 1 85  ? 2.418   16.379  1.456   1.00 12.98  ? 85   GLY F O   1 
ATOM   1855 N  N   . ASN B 1 86  ? 2.916   16.175  -0.751  1.00 12.97  ? 86   ASN F N   1 
ATOM   1856 C  CA  . ASN B 1 86  ? 1.550   15.954  -1.200  1.00 13.76  ? 86   ASN F CA  1 
ATOM   1857 C  C   . ASN B 1 86  ? 1.476   14.761  -2.116  1.00 13.64  ? 86   ASN F C   1 
ATOM   1858 O  O   . ASN B 1 86  ? 2.415   14.468  -2.849  1.00 16.60  ? 86   ASN F O   1 
ATOM   1859 C  CB  . ASN B 1 86  ? 1.018   17.128  -2.029  1.00 14.34  ? 86   ASN F CB  1 
ATOM   1860 C  CG  . ASN B 1 86  ? 0.823   18.361  -1.200  1.00 14.70  ? 86   ASN F CG  1 
ATOM   1861 O  OD1 . ASN B 1 86  ? -0.163  18.478  -0.468  1.00 14.94  ? 86   ASN F OD1 1 
ATOM   1862 N  ND2 . ASN B 1 86  ? 1.761   19.294  -1.291  1.00 17.55  ? 86   ASN F ND2 1 
ATOM   1863 N  N   . VAL B 1 87  ? 0.324   14.106  -2.100  1.00 12.93  ? 87   VAL F N   1 
ATOM   1864 C  CA  . VAL B 1 87  ? -0.113  13.221  -3.156  1.00 13.72  ? 87   VAL F CA  1 
ATOM   1865 C  C   . VAL B 1 87  ? -1.151  13.985  -3.959  1.00 13.79  ? 87   VAL F C   1 
ATOM   1866 O  O   . VAL B 1 87  ? -1.812  14.867  -3.459  1.00 14.38  ? 87   VAL F O   1 
ATOM   1867 C  CB  . VAL B 1 87  ? -0.625  11.868  -2.625  1.00 14.84  ? 87   VAL F CB  1 
ATOM   1868 C  CG1 . VAL B 1 87  ? 0.503   11.159  -1.869  1.00 16.86  ? 87   VAL F CG1 1 
ATOM   1869 C  CG2 . VAL B 1 87  ? -1.864  12.033  -1.769  1.00 17.03  ? 87   VAL F CG2 1 
ATOM   1870 N  N   . THR B 1 88  ? -1.252  13.674  -5.222  1.00 15.40  ? 88   THR F N   1 
ATOM   1871 C  CA  . THR B 1 88  ? -2.071  14.513  -6.086  1.00 14.67  ? 88   THR F CA  1 
ATOM   1872 C  C   . THR B 1 88  ? -3.075  13.580  -6.723  1.00 15.30  ? 88   THR F C   1 
ATOM   1873 O  O   . THR B 1 88  ? -2.669  12.678  -7.447  1.00 17.96  ? 88   THR F O   1 
ATOM   1874 C  CB  . THR B 1 88  ? -1.213  15.306  -7.147  1.00 14.96  ? 88   THR F CB  1 
ATOM   1875 O  OG1 . THR B 1 88  ? -0.381  16.251  -6.537  1.00 16.45  ? 88   THR F OG1 1 
ATOM   1876 C  CG2 . THR B 1 88  ? -2.154  16.067  -8.080  1.00 17.52  ? 88   THR F CG2 1 
ATOM   1877 N  N   . ALA B 1 89  ? -4.388  13.782  -6.498  1.00 16.44  ? 89   ALA F N   1 
ATOM   1878 C  CA  . ALA B 1 89  ? -5.473  12.979  -7.071  1.00 16.11  ? 89   ALA F CA  1 
ATOM   1879 C  C   . ALA B 1 89  ? -6.054  13.625  -8.329  1.00 16.63  ? 89   ALA F C   1 
ATOM   1880 O  O   . ALA B 1 89  ? -6.153  14.854  -8.449  1.00 17.34  ? 89   ALA F O   1 
ATOM   1881 C  CB  . ALA B 1 89  ? -6.602  12.782  -6.066  1.00 16.44  ? 89   ALA F CB  1 
ATOM   1882 N  N   A ASP B 1 90  ? -6.406  12.734  -9.252  0.50 19.41  ? 90   ASP F N   1 
ATOM   1883 N  N   B ASP B 1 90  ? -6.462  12.807  -9.262  0.50 20.23  ? 90   ASP F N   1 
ATOM   1884 C  CA  A ASP B 1 90  ? -7.085  13.112  -10.478 0.50 20.64  ? 90   ASP F CA  1 
ATOM   1885 C  CA  B ASP B 1 90  ? -7.097  13.345  -10.427 0.50 20.19  ? 90   ASP F CA  1 
ATOM   1886 C  C   A ASP B 1 90  ? -8.602  13.124  -10.277 0.50 18.90  ? 90   ASP F C   1 
ATOM   1887 C  C   B ASP B 1 90  ? -8.602  13.275  -10.236 0.50 17.72  ? 90   ASP F C   1 
ATOM   1888 O  O   A ASP B 1 90  ? -9.100  12.784  -9.198  0.50 20.62  ? 90   ASP F O   1 
ATOM   1889 O  O   B ASP B 1 90  ? -9.092  13.020  -9.132  0.50 18.60  ? 90   ASP F O   1 
ATOM   1890 C  CB  A ASP B 1 90  ? -6.672  12.180  -11.624 0.50 27.46  ? 90   ASP F CB  1 
ATOM   1891 C  CB  B ASP B 1 90  ? -6.677  12.505  -11.592 0.50 20.45  ? 90   ASP F CB  1 
ATOM   1892 C  CG  A ASP B 1 90  ? -5.300  12.535  -12.218 0.50 26.86  ? 90   ASP F CG  1 
ATOM   1893 C  CG  B ASP B 1 90  ? -6.967  11.076  -11.343 0.50 16.53  ? 90   ASP F CG  1 
ATOM   1894 O  OD1 A ASP B 1 90  ? -4.702  13.564  -11.822 0.50 31.35  ? 90   ASP F OD1 1 
ATOM   1895 O  OD1 B ASP B 1 90  ? -7.833  10.793  -10.490 0.50 24.46  ? 90   ASP F OD1 1 
ATOM   1896 O  OD2 A ASP B 1 90  ? -4.833  11.754  -13.085 0.50 29.24  ? 90   ASP F OD2 1 
ATOM   1897 O  OD2 B ASP B 1 90  ? -6.406  10.192  -12.026 0.50 24.12  ? 90   ASP F OD2 1 
ATOM   1898 N  N   . LYS B 1 91  ? -9.331  13.530  -11.314 1.00 18.93  ? 91   LYS F N   1 
ATOM   1899 C  CA  . LYS B 1 91  ? -10.800 13.537  -11.269 1.00 17.44  ? 91   LYS F CA  1 
ATOM   1900 C  C   . LYS B 1 91  ? -11.407 12.220  -10.881 1.00 19.02  ? 91   LYS F C   1 
ATOM   1901 O  O   . LYS B 1 91  ? -12.528 12.172  -10.384 1.00 21.84  ? 91   LYS F O   1 
ATOM   1902 C  CB  . LYS B 1 91  ? -11.371 13.918  -12.640 1.00 17.69  ? 91   LYS F CB  1 
ATOM   1903 C  CG  . LYS B 1 91  ? -11.331 15.399  -12.924 1.00 19.64  ? 91   LYS F CG  1 
ATOM   1904 C  CD  . LYS B 1 91  ? -12.380 16.166  -12.139 1.00 22.03  ? 91   LYS F CD  1 
ATOM   1905 C  CE  . LYS B 1 91  ? -12.686 17.492  -12.842 1.00 28.06  ? 91   LYS F CE  1 
ATOM   1906 N  NZ  . LYS B 1 91  ? -13.251 18.537  -11.946 1.00 37.11  ? 91   LYS F NZ  1 
ATOM   1907 N  N   . ASP B 1 92  ? -10.701 11.139  -11.156 1.00 19.94  ? 92   ASP F N   1 
ATOM   1908 C  CA  . ASP B 1 92  ? -11.202 9.845   -10.733 1.00 20.98  ? 92   ASP F CA  1 
ATOM   1909 C  C   . ASP B 1 92  ? -11.029 9.575   -9.228  1.00 21.15  ? 92   ASP F C   1 
ATOM   1910 O  O   . ASP B 1 92  ? -11.511 8.577   -8.722  1.00 24.31  ? 92   ASP F O   1 
ATOM   1911 C  CB  . ASP B 1 92  ? -10.658 8.690   -11.595 1.00 25.33  ? 92   ASP F CB  1 
ATOM   1912 C  CG  . ASP B 1 92  ? -9.187  8.377   -11.353 1.00 29.41  ? 92   ASP F CG  1 
ATOM   1913 O  OD1 . ASP B 1 92  ? -8.538  9.002   -10.484 1.00 32.96  ? 92   ASP F OD1 1 
ATOM   1914 O  OD2 . ASP B 1 92  ? -8.672  7.472   -12.051 1.00 41.81  ? 92   ASP F OD2 1 
ATOM   1915 N  N   . GLY B 1 93  ? -10.371 10.483  -8.523  1.00 19.78  ? 93   GLY F N   1 
ATOM   1916 C  CA  . GLY B 1 93  ? -10.218 10.364  -7.082  1.00 19.16  ? 93   GLY F CA  1 
ATOM   1917 C  C   . GLY B 1 93  ? -9.011  9.537   -6.646  1.00 19.30  ? 93   GLY F C   1 
ATOM   1918 O  O   . GLY B 1 93  ? -8.844  9.280   -5.450  1.00 20.50  ? 93   GLY F O   1 
ATOM   1919 N  N   . VAL B 1 94  ? -8.148  9.172   -7.593  1.00 20.24  ? 94   VAL F N   1 
ATOM   1920 C  CA  . VAL B 1 94  ? -6.996  8.307   -7.321  1.00 20.21  ? 94   VAL F CA  1 
ATOM   1921 C  C   . VAL B 1 94  ? -5.690  9.070   -7.384  1.00 18.77  ? 94   VAL F C   1 
ATOM   1922 O  O   . VAL B 1 94  ? -5.458  9.814   -8.329  1.00 20.37  ? 94   VAL F O   1 
ATOM   1923 C  CB  . VAL B 1 94  ? -6.925  7.161   -8.347  1.00 22.90  ? 94   VAL F CB  1 
ATOM   1924 C  CG1 . VAL B 1 94  ? -5.754  6.238   -8.063  1.00 26.64  ? 94   VAL F CG1 1 
ATOM   1925 C  CG2 . VAL B 1 94  ? -8.222  6.386   -8.308  1.00 23.69  ? 94   VAL F CG2 1 
ATOM   1926 N  N   . ALA B 1 95  ? -4.869  8.894   -6.348  1.00 18.06  ? 95   ALA F N   1 
ATOM   1927 C  CA  . ALA B 1 95  ? -3.503  9.382   -6.321  1.00 18.48  ? 95   ALA F CA  1 
ATOM   1928 C  C   . ALA B 1 95  ? -2.563  8.219   -6.456  1.00 19.36  ? 95   ALA F C   1 
ATOM   1929 O  O   . ALA B 1 95  ? -2.638  7.288   -5.687  1.00 20.45  ? 95   ALA F O   1 
ATOM   1930 C  CB  . ALA B 1 95  ? -3.232  10.096  -5.023  1.00 20.15  ? 95   ALA F CB  1 
ATOM   1931 N  N   . ASP B 1 96  ? -1.663  8.289   -7.424  1.00 20.39  ? 96   ASP F N   1 
ATOM   1932 C  CA  . ASP B 1 96  ? -0.610  7.314   -7.575  1.00 21.61  ? 96   ASP F CA  1 
ATOM   1933 C  C   . ASP B 1 96  ? 0.585   7.826   -6.824  1.00 19.72  ? 96   ASP F C   1 
ATOM   1934 O  O   . ASP B 1 96  ? 1.100   8.925   -7.071  1.00 25.96  ? 96   ASP F O   1 
ATOM   1935 C  CB  . ASP B 1 96  ? -0.289  7.098   -9.044  1.00 23.57  ? 96   ASP F CB  1 
ATOM   1936 C  CG  . ASP B 1 96  ? -0.994  5.873   -9.614  0.50 32.62  ? 96   ASP F CG  1 
ATOM   1937 O  OD1 . ASP B 1 96  ? -2.013  5.424   -9.025  1.00 34.78  ? 96   ASP F OD1 1 
ATOM   1938 O  OD2 . ASP B 1 96  ? -0.526  5.354   -10.649 0.50 40.04  ? 96   ASP F OD2 1 
ATOM   1939 N  N   . VAL B 1 97  ? 0.978   7.032   -5.835  1.00 22.37  ? 97   VAL F N   1 
ATOM   1940 C  CA  . VAL B 1 97  ? 2.043   7.443   -4.984  1.00 22.87  ? 97   VAL F CA  1 
ATOM   1941 C  C   . VAL B 1 97  ? 3.314   6.763   -5.451  1.00 20.68  ? 97   VAL F C   1 
ATOM   1942 O  O   . VAL B 1 97  ? 3.383   5.524   -5.569  1.00 20.27  ? 97   VAL F O   1 
ATOM   1943 C  CB  . VAL B 1 97  ? 1.727   7.131   -3.519  1.00 20.46  ? 97   VAL F CB  1 
ATOM   1944 C  CG1 . VAL B 1 97  ? 2.849   7.646   -2.640  1.00 22.62  ? 97   VAL F CG1 1 
ATOM   1945 C  CG2 . VAL B 1 97  ? 0.371   7.723   -3.139  1.00 22.47  ? 97   VAL F CG2 1 
ATOM   1946 N  N   . SER B 1 98  ? 4.304   7.599   -5.719  1.00 25.06  ? 98   SER F N   1 
ATOM   1947 C  CA  . SER B 1 98  ? 5.645   7.165   -6.055  1.00 23.29  ? 98   SER F CA  1 
ATOM   1948 C  C   . SER B 1 98  ? 6.610   8.255   -5.575  1.00 24.15  ? 98   SER F C   1 
ATOM   1949 O  O   . SER B 1 98  ? 6.726   9.327   -6.183  1.00 30.07  ? 98   SER F O   1 
ATOM   1950 C  CB  . SER B 1 98  ? 5.777   6.919   -7.549  1.00 26.74  ? 98   SER F CB  1 
ATOM   1951 O  OG  . SER B 1 98  ? 7.028   6.324   -7.816  1.00 32.68  ? 98   SER F OG  1 
ATOM   1952 N  N   . ILE B 1 99  ? 7.269   7.970   -4.464  1.00 21.59  ? 99   ILE F N   1 
ATOM   1953 C  CA  . ILE B 1 99  ? 8.096   8.914   -3.706  1.00 20.59  ? 99   ILE F CA  1 
ATOM   1954 C  C   . ILE B 1 99  ? 9.416   8.158   -3.429  1.00 19.89  ? 99   ILE F C   1 
ATOM   1955 O  O   . ILE B 1 99  ? 9.395   6.934   -3.194  1.00 21.44  ? 99   ILE F O   1 
ATOM   1956 C  CB  . ILE B 1 99  ? 7.361   9.329   -2.378  1.00 19.23  ? 99   ILE F CB  1 
ATOM   1957 C  CG1 . ILE B 1 99  ? 6.233   10.345  -2.667  1.00 20.79  ? 99   ILE F CG1 1 
ATOM   1958 C  CG2 . ILE B 1 99  ? 8.313   9.907   -1.353  1.00 24.07  ? 99   ILE F CG2 1 
ATOM   1959 C  CD1 . ILE B 1 99  ? 5.339   10.587  -1.472  1.00 24.66  ? 99   ILE F CD1 1 
ATOM   1960 N  N   . GLU B 1 100 ? 10.558  8.837   -3.472  1.00 19.09  ? 100  GLU F N   1 
ATOM   1961 C  CA  . GLU B 1 100 ? 11.776  8.324   -2.857  1.00 18.20  ? 100  GLU F CA  1 
ATOM   1962 C  C   . GLU B 1 100 ? 12.188  9.395   -1.885  1.00 16.22  ? 100  GLU F C   1 
ATOM   1963 O  O   . GLU B 1 100 ? 12.153  10.569  -2.226  1.00 17.98  ? 100  GLU F O   1 
ATOM   1964 C  CB  . GLU B 1 100 ? 12.881  8.041   -3.870  1.00 22.14  ? 100  GLU F CB  1 
ATOM   1965 C  CG  . GLU B 1 100 ? 14.099  7.375   -3.266  1.00 27.03  ? 100  GLU F CG  1 
ATOM   1966 C  CD  . GLU B 1 100 ? 15.245  7.242   -4.243  1.00 31.98  ? 100  GLU F CD  1 
ATOM   1967 O  OE1 . GLU B 1 100 ? 16.000  8.227   -4.449  1.00 40.40  ? 100  GLU F OE1 1 
ATOM   1968 O  OE2 . GLU B 1 100 ? 15.403  6.139   -4.791  1.00 36.56  ? 100  GLU F OE2 1 
ATOM   1969 N  N   . ASP B 1 101 ? 12.541  9.003   -0.668  1.00 15.47  ? 101  ASP F N   1 
ATOM   1970 C  CA  . ASP B 1 101 ? 12.877  9.966   0.365   1.00 14.98  ? 101  ASP F CA  1 
ATOM   1971 C  C   . ASP B 1 101 ? 14.088  9.482   1.126   1.00 15.24  ? 101  ASP F C   1 
ATOM   1972 O  O   . ASP B 1 101 ? 14.171  8.309   1.471   1.00 16.58  ? 101  ASP F O   1 
ATOM   1973 C  CB  . ASP B 1 101 ? 11.708  10.223  1.333   1.00 13.97  ? 101  ASP F CB  1 
ATOM   1974 C  CG  . ASP B 1 101 ? 11.946  11.445  2.195   1.00 14.12  ? 101  ASP F CG  1 
ATOM   1975 O  OD1 . ASP B 1 101 ? 11.858  12.562  1.632   1.00 16.39  ? 101  ASP F OD1 1 
ATOM   1976 O  OD2 . ASP B 1 101 ? 12.291  11.296  3.388   1.00 13.91  ? 101  ASP F OD2 1 
ATOM   1977 N  N   . SER B 1 102 ? 14.998  10.410  1.415   1.00 15.44  ? 102  SER F N   1 
ATOM   1978 C  CA  . SER B 1 102 ? 16.232  10.094  2.095   1.00 17.34  ? 102  SER F CA  1 
ATOM   1979 C  C   . SER B 1 102 ? 16.253  10.426  3.567   1.00 15.40  ? 102  SER F C   1 
ATOM   1980 O  O   . SER B 1 102 ? 17.235  10.105  4.238   1.00 18.93  ? 102  SER F O   1 
ATOM   1981 C  CB  . SER B 1 102 ? 17.392  10.814  1.425   1.00 23.26  ? 102  SER F CB  1 
ATOM   1982 O  OG  . SER B 1 102 ? 17.619  10.250  0.158   1.00 31.57  ? 102  SER F OG  1 
ATOM   1983 N  N   . VAL B 1 103 ? 15.186  11.030  4.077   1.00 14.45  ? 103  VAL F N   1 
ATOM   1984 C  CA  . VAL B 1 103 ? 15.164  11.442  5.462   1.00 13.78  ? 103  VAL F CA  1 
ATOM   1985 C  C   . VAL B 1 103 ? 14.414  10.458  6.368   1.00 13.38  ? 103  VAL F C   1 
ATOM   1986 O  O   . VAL B 1 103 ? 14.880  10.123  7.444   1.00 14.78  ? 103  VAL F O   1 
ATOM   1987 C  CB  . VAL B 1 103 ? 14.594  12.863  5.560   1.00 14.90  ? 103  VAL F CB  1 
ATOM   1988 C  CG1 . VAL B 1 103 ? 14.373  13.276  7.001   1.00 16.11  ? 103  VAL F CG1 1 
ATOM   1989 C  CG2 . VAL B 1 103 ? 15.523  13.863  4.859   1.00 17.43  ? 103  VAL F CG2 1 
ATOM   1990 N  N   . ILE B 1 104 ? 13.267  9.969   5.908   1.00 13.04  ? 104  ILE F N   1 
ATOM   1991 C  CA  . ILE B 1 104 ? 12.633  8.871   6.595   1.00 12.02  ? 104  ILE F CA  1 
ATOM   1992 C  C   . ILE B 1 104 ? 13.552  7.642   6.512   1.00 12.00  ? 104  ILE F C   1 
ATOM   1993 O  O   . ILE B 1 104 ? 14.394  7.524   5.638   1.00 13.69  ? 104  ILE F O   1 
ATOM   1994 C  CB  . ILE B 1 104 ? 11.241  8.534   6.027   1.00 11.25  ? 104  ILE F CB  1 
ATOM   1995 C  CG1 . ILE B 1 104 ? 11.317  8.113   4.535   1.00 12.38  ? 104  ILE F CG1 1 
ATOM   1996 C  CG2 . ILE B 1 104 ? 10.257  9.688   6.242   1.00 12.21  ? 104  ILE F CG2 1 
ATOM   1997 C  CD1 . ILE B 1 104 ? 10.026  7.539   3.994   1.00 13.22  ? 104  ILE F CD1 1 
ATOM   1998 N  N   . SER B 1 105 ? 13.366  6.735   7.455   1.00 12.21  ? 105  SER F N   1 
ATOM   1999 C  CA  . SER B 1 105 ? 14.084  5.476   7.461   1.00 12.88  ? 105  SER F CA  1 
ATOM   2000 C  C   . SER B 1 105 ? 13.169  4.384   8.002   1.00 12.11  ? 105  SER F C   1 
ATOM   2001 O  O   . SER B 1 105 ? 12.162  4.661   8.652   1.00 11.83  ? 105  SER F O   1 
ATOM   2002 C  CB  . SER B 1 105 ? 15.343  5.589   8.309   1.00 14.08  ? 105  SER F CB  1 
ATOM   2003 O  OG  . SER B 1 105 ? 16.135  4.440   8.107   1.00 16.23  ? 105  SER F OG  1 
ATOM   2004 N  N   . LEU B 1 106 ? 13.553  3.133   7.742   1.00 13.75  ? 106  LEU F N   1 
ATOM   2005 C  CA  . LEU B 1 106 ? 12.897  1.967   8.318   1.00 13.80  ? 106  LEU F CA  1 
ATOM   2006 C  C   . LEU B 1 106 ? 13.772  1.328   9.406   1.00 16.10  ? 106  LEU F C   1 
ATOM   2007 O  O   . LEU B 1 106 ? 13.489  0.234   9.860   1.00 18.06  ? 106  LEU F O   1 
ATOM   2008 C  CB  . LEU B 1 106 ? 12.530  0.955   7.229   1.00 14.28  ? 106  LEU F CB  1 
ATOM   2009 C  CG  . LEU B 1 106 ? 11.650  1.489   6.097   1.00 13.68  ? 106  LEU F CG  1 
ATOM   2010 C  CD1 . LEU B 1 106 ? 11.315  0.348   5.133   1.00 15.85  ? 106  LEU F CD1 1 
ATOM   2011 C  CD2 . LEU B 1 106 ? 10.364  2.143   6.613   1.00 15.38  ? 106  LEU F CD2 1 
ATOM   2012 N  N   . SER B 1 107 ? 14.813  2.042   9.831   1.00 18.30  ? 107  SER F N   1 
ATOM   2013 C  CA  . SER B 1 107 ? 15.598  1.687   11.010  1.00 22.07  ? 107  SER F CA  1 
ATOM   2014 C  C   . SER B 1 107 ? 16.137  2.978   11.671  1.00 21.18  ? 107  SER F C   1 
ATOM   2015 O  O   . SER B 1 107 ? 16.024  4.061   11.110  1.00 21.18  ? 107  SER F O   1 
ATOM   2016 C  CB  . SER B 1 107 ? 16.730  0.742   10.617  1.00 27.19  ? 107  SER F CB  1 
ATOM   2017 O  OG  . SER B 1 107 ? 17.713  1.365   9.804   1.00 32.99  ? 107  SER F OG  1 
ATOM   2018 N  N   . GLY B 1 108 ? 16.703  2.854   12.867  1.00 26.36  ? 108  GLY F N   1 
ATOM   2019 C  CA  . GLY B 1 108 ? 17.386  3.983   13.516  1.00 26.05  ? 108  GLY F CA  1 
ATOM   2020 C  C   . GLY B 1 108 ? 16.461  5.047   14.096  1.00 25.93  ? 108  GLY F C   1 
ATOM   2021 O  O   . GLY B 1 108 ? 15.256  4.802   14.268  1.00 24.06  ? 108  GLY F O   1 
ATOM   2022 N  N   . ASP B 1 109 ? 17.033  6.229   14.396  1.00 26.03  ? 109  ASP F N   1 
ATOM   2023 C  CA  . ASP B 1 109 ? 16.305  7.290   15.137  1.00 23.88  ? 109  ASP F CA  1 
ATOM   2024 C  C   . ASP B 1 109 ? 15.198  7.884   14.308  1.00 21.52  ? 109  ASP F C   1 
ATOM   2025 O  O   . ASP B 1 109 ? 14.235  8.401   14.824  1.00 23.52  ? 109  ASP F O   1 
ATOM   2026 C  CB  . ASP B 1 109 ? 17.231  8.463   15.649  1.00 25.25  ? 109  ASP F CB  1 
ATOM   2027 C  CG  . ASP B 1 109 ? 16.594  9.259   16.868  1.00 24.41  ? 109  ASP F CG  1 
ATOM   2028 O  OD1 . ASP B 1 109 ? 15.854  8.567   17.591  1.00 35.00  ? 109  ASP F OD1 1 
ATOM   2029 O  OD2 . ASP B 1 109 ? 16.771  10.487  17.148  1.00 22.48  ? 109  ASP F OD2 1 
ATOM   2030 N  N   . HIS B 1 110 ? 15.349  7.823   13.008  1.00 17.63  ? 110  HIS F N   1 
ATOM   2031 C  CA  . HIS B 1 110 ? 14.350  8.391   12.096  1.00 14.84  ? 110  HIS F CA  1 
ATOM   2032 C  C   . HIS B 1 110 ? 13.410  7.324   11.542  1.00 13.92  ? 110  HIS F C   1 
ATOM   2033 O  O   . HIS B 1 110 ? 12.711  7.533   10.555  1.00 13.41  ? 110  HIS F O   1 
ATOM   2034 C  CB  . HIS B 1 110 ? 15.044  9.166   11.010  1.00 15.06  ? 110  HIS F CB  1 
ATOM   2035 C  CG  . HIS B 1 110 ? 15.821  10.315  11.541  1.00 16.61  ? 110  HIS F CG  1 
ATOM   2036 N  ND1 . HIS B 1 110 ? 16.696  11.014  10.806  1.00 22.19  ? 110  HIS F ND1 1 
ATOM   2037 C  CD2 . HIS B 1 110 ? 15.853  10.846  12.815  1.00 17.76  ? 110  HIS F CD2 1 
ATOM   2038 C  CE1 . HIS B 1 110 ? 17.245  11.955  11.564  1.00 24.04  ? 110  HIS F CE1 1 
ATOM   2039 N  NE2 . HIS B 1 110 ? 16.737  11.835  12.802  1.00 19.69  ? 110  HIS F NE2 1 
ATOM   2040 N  N   . CYS B 1 111 ? 13.345  6.181   12.218  1.00 14.67  ? 111  CYS F N   1 
ATOM   2041 C  CA  . CYS B 1 111 ? 12.458  5.108   11.814  1.00 13.38  ? 111  CYS F CA  1 
ATOM   2042 C  C   . CYS B 1 111 ? 10.998  5.523   11.931  1.00 11.45  ? 111  CYS F C   1 
ATOM   2043 O  O   . CYS B 1 111 ? 10.567  6.039   12.949  1.00 12.42  ? 111  CYS F O   1 
ATOM   2044 C  CB  . CYS B 1 111 ? 12.688  3.875   12.680  1.00 15.23  ? 111  CYS F CB  1 
ATOM   2045 S  SG  . CYS B 1 111 ? 11.778  2.415   12.148  1.00 17.04  ? 111  CYS F SG  1 
ATOM   2046 N  N   . ILE B 1 112 ? 10.247  5.251   10.864  1.00 10.75  ? 112  ILE F N   1 
ATOM   2047 C  CA  . ILE B 1 112 ? 8.835   5.588   10.804  1.00 10.29  ? 112  ILE F CA  1 
ATOM   2048 C  C   . ILE B 1 112 ? 7.913   4.398   11.124  1.00 9.90   ? 112  ILE F C   1 
ATOM   2049 O  O   . ILE B 1 112 ? 6.710   4.571   11.271  1.00 9.94   ? 112  ILE F O   1 
ATOM   2050 C  CB  . ILE B 1 112 ? 8.462   6.204   9.459   1.00 10.09  ? 112  ILE F CB  1 
ATOM   2051 C  CG1 . ILE B 1 112 ? 8.731   5.260   8.299   1.00 11.10  ? 112  ILE F CG1 1 
ATOM   2052 C  CG2 . ILE B 1 112 ? 9.195   7.534   9.328   1.00 11.78  ? 112  ILE F CG2 1 
ATOM   2053 C  CD1 . ILE B 1 112 ? 8.159   5.748   6.988   1.00 12.66  ? 112  ILE F CD1 1 
ATOM   2054 N  N   . THR B 1 113 ? 8.467   3.196   11.231  1.00 11.03  ? 113  THR F N   1 
ATOM   2055 C  CA  . THR B 1 113 ? 7.656   2.048   11.546  1.00 10.91  ? 113  THR F CA  1 
ATOM   2056 C  C   . THR B 1 113 ? 7.089   2.210   12.967  1.00 9.69   ? 113  THR F C   1 
ATOM   2057 O  O   . THR B 1 113 ? 7.754   2.698   13.880  1.00 10.91  ? 113  THR F O   1 
ATOM   2058 C  CB  . THR B 1 113 ? 8.491   0.806   11.369  1.00 13.61  ? 113  THR F CB  1 
ATOM   2059 O  OG1 . THR B 1 113 ? 9.127   0.892   10.075  1.00 15.56  ? 113  THR F OG1 1 
ATOM   2060 C  CG2 . THR B 1 113 ? 7.685   -0.392  11.475  1.00 17.17  ? 113  THR F CG2 1 
ATOM   2061 N  N   . GLY B 1 114 ? 5.829   1.840   13.132  1.00 9.06   ? 114  GLY F N   1 
ATOM   2062 C  CA  . GLY B 1 114 ? 5.141   2.045   14.396  1.00 8.91   ? 114  GLY F CA  1 
ATOM   2063 C  C   . GLY B 1 114 ? 4.534   3.427   14.556  1.00 8.06   ? 114  GLY F C   1 
ATOM   2064 O  O   . GLY B 1 114 ? 3.938   3.696   15.590  1.00 8.75   ? 114  GLY F O   1 
ATOM   2065 N  N   . ARG B 1 115 ? 4.660   4.267   13.533  1.00 7.91   ? 115  ARG F N   1 
ATOM   2066 C  CA  . ARG B 1 115 ? 4.064   5.596   13.536  1.00 7.90   ? 115  ARG F CA  1 
ATOM   2067 C  C   . ARG B 1 115 ? 2.898   5.608   12.547  1.00 7.97   ? 115  ARG F C   1 
ATOM   2068 O  O   . ARG B 1 115 ? 2.590   4.602   11.959  1.00 12.32  ? 115  ARG F O   1 
ATOM   2069 C  CB  . ARG B 1 115 ? 5.134   6.652   13.254  1.00 8.10   ? 115  ARG F CB  1 
ATOM   2070 C  CG  . ARG B 1 115 ? 6.278   6.508   14.248  1.00 8.69   ? 115  ARG F CG  1 
ATOM   2071 C  CD  . ARG B 1 115 ? 7.302   7.626   14.110  1.00 9.79   ? 115  ARG F CD  1 
ATOM   2072 N  NE  . ARG B 1 115 ? 8.479   7.354   14.956  1.00 11.32  ? 115  ARG F NE  1 
ATOM   2073 C  CZ  . ARG B 1 115 ? 8.611   7.703   16.230  1.00 11.59  ? 115  ARG F CZ  1 
ATOM   2074 N  NH1 . ARG B 1 115 ? 7.636   8.268   16.902  1.00 12.71  ? 115  ARG F NH1 1 
ATOM   2075 N  NH2 . ARG B 1 115 ? 9.751   7.414   16.849  1.00 13.31  ? 115  ARG F NH2 1 
ATOM   2076 N  N   . THR B 1 116 ? 2.206   6.718   12.401  1.00 8.60   ? 116  THR F N   1 
ATOM   2077 C  CA  . THR B 1 116 ? 1.003   6.775   11.581  1.00 8.40   ? 116  THR F CA  1 
ATOM   2078 C  C   . THR B 1 116 ? 1.252   7.561   10.307  1.00 8.41   ? 116  THR F C   1 
ATOM   2079 O  O   . THR B 1 116 ? 1.721   8.700   10.365  1.00 10.79  ? 116  THR F O   1 
ATOM   2080 C  CB  . THR B 1 116 ? -0.162  7.438   12.352  1.00 8.73   ? 116  THR F CB  1 
ATOM   2081 O  OG1 . THR B 1 116 ? -0.492  6.630   13.479  1.00 9.96   ? 116  THR F OG1 1 
ATOM   2082 C  CG2 . THR B 1 116 ? -1.401  7.593   11.519  1.00 9.84   ? 116  THR F CG2 1 
ATOM   2083 N  N   . LEU B 1 117 ? 0.859   7.007   9.171   1.00 8.18   ? 117  LEU F N   1 
ATOM   2084 C  CA  . LEU B 1 117 ? 0.825   7.742   7.908   1.00 8.46   ? 117  LEU F CA  1 
ATOM   2085 C  C   . LEU B 1 117 ? -0.580  8.343   7.753   1.00 8.77   ? 117  LEU F C   1 
ATOM   2086 O  O   . LEU B 1 117 ? -1.573  7.637   7.974   1.00 9.34   ? 117  LEU F O   1 
ATOM   2087 C  CB  . LEU B 1 117 ? 1.126   6.789   6.772   1.00 9.08   ? 117  LEU F CB  1 
ATOM   2088 C  CG  . LEU B 1 117 ? 1.245   7.375   5.386   1.00 10.03  ? 117  LEU F CG  1 
ATOM   2089 C  CD1 . LEU B 1 117 ? 2.452   8.302   5.249   1.00 11.90  ? 117  LEU F CD1 1 
ATOM   2090 C  CD2 . LEU B 1 117 ? 1.329   6.259   4.361   1.00 11.26  ? 117  LEU F CD2 1 
ATOM   2091 N  N   . VAL B 1 118 ? -0.658  9.621   7.366   1.00 8.63   ? 118  VAL F N   1 
ATOM   2092 C  CA  . VAL B 1 118 ? -1.925  10.344  7.238   1.00 9.38   ? 118  VAL F CA  1 
ATOM   2093 C  C   . VAL B 1 118 ? -1.982  11.014  5.867   1.00 9.62   ? 118  VAL F C   1 
ATOM   2094 O  O   . VAL B 1 118 ? -1.015  11.648  5.438   1.00 10.40  ? 118  VAL F O   1 
ATOM   2095 C  CB  . VAL B 1 118 ? -2.063  11.412  8.331   1.00 9.86   ? 118  VAL F CB  1 
ATOM   2096 C  CG1 . VAL B 1 118 ? -3.401  12.152  8.200   1.00 11.48  ? 118  VAL F CG1 1 
ATOM   2097 C  CG2 . VAL B 1 118 ? -1.929  10.795  9.719   1.00 10.31  ? 118  VAL F CG2 1 
ATOM   2098 N  N   . VAL B 1 119 ? -3.163  10.896  5.224   1.00 10.24  ? 119  VAL F N   1 
ATOM   2099 C  CA  . VAL B 1 119 ? -3.478  11.713  4.061   1.00 10.47  ? 119  VAL F CA  1 
ATOM   2100 C  C   . VAL B 1 119 ? -4.526  12.738  4.471   1.00 10.66  ? 119  VAL F C   1 
ATOM   2101 O  O   . VAL B 1 119 ? -5.521  12.424  5.116   1.00 11.40  ? 119  VAL F O   1 
ATOM   2102 C  CB  . VAL B 1 119 ? -3.915  10.859  2.864   1.00 12.40  ? 119  VAL F CB  1 
ATOM   2103 C  CG1 . VAL B 1 119 ? -5.125  9.981   3.112   1.00 13.98  ? 119  VAL F CG1 1 
ATOM   2104 C  CG2 . VAL B 1 119 ? -4.120  11.729  1.612   1.00 13.63  ? 119  VAL F CG2 1 
ATOM   2105 N  N   . HIS B 1 120 ? -4.264  13.990  4.120   1.00 10.96  ? 120  HIS F N   1 
ATOM   2106 C  CA  . HIS B 1 120 ? -5.030  15.123  4.614   1.00 11.86  ? 120  HIS F CA  1 
ATOM   2107 C  C   . HIS B 1 120 ? -6.057  15.664  3.616   1.00 12.31  ? 120  HIS F C   1 
ATOM   2108 O  O   . HIS B 1 120 ? -6.006  15.395  2.412   1.00 13.55  ? 120  HIS F O   1 
ATOM   2109 C  CB  . HIS B 1 120 ? -4.074  16.265  5.004   1.00 11.49  ? 120  HIS F CB  1 
ATOM   2110 C  CG  . HIS B 1 120 ? -3.337  15.989  6.268   1.00 10.96  ? 120  HIS F CG  1 
ATOM   2111 N  ND1 . HIS B 1 120 ? -3.733  16.481  7.464   1.00 12.00  ? 120  HIS F ND1 1 
ATOM   2112 C  CD2 . HIS B 1 120 ? -2.193  15.255  6.521   1.00 11.58  ? 120  HIS F CD2 1 
ATOM   2113 C  CE1 . HIS B 1 120 ? -2.887  16.070  8.422   1.00 11.91  ? 120  HIS F CE1 1 
ATOM   2114 N  NE2 . HIS B 1 120 ? -1.943  15.344  7.848   1.00 11.81  ? 120  HIS F NE2 1 
ATOM   2115 N  N   . GLU B 1 121 ? -6.946  16.471  4.175   1.00 13.08  ? 121  GLU F N   1 
ATOM   2116 C  CA  . GLU B 1 121 ? -8.047  17.085  3.468   1.00 14.00  ? 121  GLU F CA  1 
ATOM   2117 C  C   . GLU B 1 121 ? -7.614  17.988  2.334   1.00 14.28  ? 121  GLU F C   1 
ATOM   2118 O  O   . GLU B 1 121 ? -8.241  17.996  1.263   1.00 15.22  ? 121  GLU F O   1 
ATOM   2119 C  CB  . GLU B 1 121 ? -8.820  17.899  4.510   1.00 16.92  ? 121  GLU F CB  1 
ATOM   2120 C  CG  . GLU B 1 121 ? -9.965  18.762  4.036   1.00 20.32  ? 121  GLU F CG  1 
ATOM   2121 C  CD  . GLU B 1 121 ? -10.327 19.872  5.025   1.00 22.74  ? 121  GLU F CD  1 
ATOM   2122 O  OE1 . GLU B 1 121 ? -9.709  20.052  6.109   1.00 22.31  ? 121  GLU F OE1 1 
ATOM   2123 O  OE2 . GLU B 1 121 ? -11.253 20.624  4.673   0.50 21.28  ? 121  GLU F OE2 1 
ATOM   2124 N  N   . LYS B 1 122 ? -6.607  18.813  2.614   1.00 16.44  ? 122  LYS F N   1 
ATOM   2125 C  CA  . LYS B 1 122 ? -6.205  19.907  1.791   1.00 17.43  ? 122  LYS F CA  1 
ATOM   2126 C  C   . LYS B 1 122 ? -4.721  19.769  1.336   1.00 14.17  ? 122  LYS F C   1 
ATOM   2127 O  O   . LYS B 1 122 ? -3.982  18.922  1.832   1.00 14.69  ? 122  LYS F O   1 
ATOM   2128 C  CB  . LYS B 1 122 ? -6.409  21.320  2.553   1.00 18.01  ? 122  LYS F CB  1 
ATOM   2129 C  CG  . LYS B 1 122 ? -7.715  21.568  3.284   1.00 20.28  ? 122  LYS F CG  1 
ATOM   2130 C  CD  . LYS B 1 122 ? -7.724  22.924  3.949   1.00 25.48  ? 122  LYS F CD  1 
ATOM   2131 C  CE  . LYS B 1 122 ? -9.040  23.154  4.672   1.00 28.12  ? 122  LYS F CE  1 
ATOM   2132 N  NZ  . LYS B 1 122 ? -9.042  24.462  5.378   1.00 39.48  ? 122  LYS F NZ  1 
ATOM   2133 N  N   . ALA B 1 123 ? -4.262  20.698  0.491   1.00 14.14  ? 123  ALA F N   1 
ATOM   2134 C  CA  . ALA B 1 123 ? -2.871  20.742  0.075   1.00 14.57  ? 123  ALA F CA  1 
ATOM   2135 C  C   . ALA B 1 123 ? -2.009  21.159  1.238   1.00 14.12  ? 123  ALA F C   1 
ATOM   2136 O  O   . ALA B 1 123 ? -2.378  22.004  2.057   1.00 15.26  ? 123  ALA F O   1 
ATOM   2137 C  CB  . ALA B 1 123 ? -2.672  21.725  -1.067  1.00 16.15  ? 123  ALA F CB  1 
ATOM   2138 N  N   . ASP B 1 124 ? -0.804  20.602  1.253   1.00 13.53  ? 124  ASP F N   1 
ATOM   2139 C  CA  . ASP B 1 124 ? 0.274   21.060  2.109   1.00 13.39  ? 124  ASP F CA  1 
ATOM   2140 C  C   . ASP B 1 124 ? 1.033   22.150  1.310   1.00 14.23  ? 124  ASP F C   1 
ATOM   2141 O  O   . ASP B 1 124 ? 1.508   21.880  0.176   1.00 15.48  ? 124  ASP F O   1 
ATOM   2142 C  CB  . ASP B 1 124 ? 1.156   19.860  2.415   1.00 13.14  ? 124  ASP F CB  1 
ATOM   2143 C  CG  . ASP B 1 124 ? 2.316   20.136  3.358   1.00 12.91  ? 124  ASP F CG  1 
ATOM   2144 O  OD1 . ASP B 1 124 ? 2.660   21.287  3.596   1.00 13.34  ? 124  ASP F OD1 1 
ATOM   2145 O  OD2 . ASP B 1 124 ? 2.920   19.141  3.823   1.00 12.92  ? 124  ASP F OD2 1 
ATOM   2146 N  N   . ASP B 1 125 ? 1.161   23.331  1.915   1.00 14.93  ? 125  ASP F N   1 
ATOM   2147 C  CA  . ASP B 1 125 ? 1.891   24.418  1.270   1.00 15.23  ? 125  ASP F CA  1 
ATOM   2148 C  C   . ASP B 1 125 ? 3.413   24.346  1.447   1.00 14.62  ? 125  ASP F C   1 
ATOM   2149 O  O   . ASP B 1 125 ? 4.129   25.263  1.034   1.00 15.35  ? 125  ASP F O   1 
ATOM   2150 C  CB  . ASP B 1 125 ? 1.321   25.743  1.693   1.00 16.95  ? 125  ASP F CB  1 
ATOM   2151 C  CG  . ASP B 1 125 ? 1.433   26.014  3.173   1.00 17.26  ? 125  ASP F CG  1 
ATOM   2152 O  OD1 . ASP B 1 125 ? 2.334   25.465  3.868   1.00 17.15  ? 125  ASP F OD1 1 
ATOM   2153 O  OD2 . ASP B 1 125 ? 0.622   26.826  3.701   1.00 18.97  ? 125  ASP F OD2 1 
ATOM   2154 N  N   . LEU B 1 126 ? 3.871   23.253  2.050   1.00 15.22  ? 126  LEU F N   1 
ATOM   2155 C  CA  . LEU B 1 126 ? 5.272   22.938  2.153   1.00 14.55  ? 126  LEU F CA  1 
ATOM   2156 C  C   . LEU B 1 126 ? 6.029   23.990  2.932   1.00 15.47  ? 126  LEU F C   1 
ATOM   2157 O  O   . LEU B 1 126 ? 7.238   24.174  2.810   1.00 17.34  ? 126  LEU F O   1 
ATOM   2158 C  CB  . LEU B 1 126 ? 5.933   22.623  0.799   1.00 14.77  ? 126  LEU F CB  1 
ATOM   2159 C  CG  . LEU B 1 126 ? 5.274   21.623  -0.125  1.00 15.39  ? 126  LEU F CG  1 
ATOM   2160 C  CD1 . LEU B 1 126 ? 6.187   21.266  -1.293  1.00 17.10  ? 126  LEU F CD1 1 
ATOM   2161 C  CD2 . LEU B 1 126 ? 4.878   20.378  0.621   1.00 15.58  ? 126  LEU F CD2 1 
ATOM   2162 N  N   . GLY B 1 127 ? 5.322   24.614  3.855   1.00 15.41  ? 127  GLY F N   1 
ATOM   2163 C  CA  . GLY B 1 127 ? 5.852   25.613  4.722   1.00 17.85  ? 127  GLY F CA  1 
ATOM   2164 C  C   . GLY B 1 127 ? 5.992   27.023  4.121   1.00 19.88  ? 127  GLY F C   1 
ATOM   2165 O  O   . GLY B 1 127 ? 6.609   27.871  4.737   1.00 25.17  ? 127  GLY F O   1 
ATOM   2166 N  N   . LYS B 1 128 ? 5.417   27.258  2.935   1.00 17.79  ? 128  LYS F N   1 
ATOM   2167 C  CA  . LYS B 1 128 ? 5.596   28.506  2.143   1.00 18.31  ? 128  LYS F CA  1 
ATOM   2168 C  C   . LYS B 1 128 ? 4.307   29.321  2.067   1.00 18.20  ? 128  LYS F C   1 
ATOM   2169 O  O   . LYS B 1 128 ? 4.229   30.242  1.281   1.00 21.16  ? 128  LYS F O   1 
ATOM   2170 C  CB  . LYS B 1 128 ? 6.088   28.142  0.751   1.00 19.10  ? 128  LYS F CB  1 
ATOM   2171 C  CG  . LYS B 1 128 ? 7.428   27.432  0.697   1.00 25.15  ? 128  LYS F CG  1 
ATOM   2172 C  CD  . LYS B 1 128 ? 8.605   28.319  1.032   1.00 30.16  ? 128  LYS F CD  1 
ATOM   2173 C  CE  . LYS B 1 128 ? 9.912   27.550  0.849   1.00 36.60  ? 128  LYS F CE  1 
ATOM   2174 N  NZ  . LYS B 1 128 ? 11.041  28.099  1.652   1.00 47.14  ? 128  LYS F NZ  1 
ATOM   2175 N  N   . GLY B 1 129 ? 3.330   29.033  2.920   1.00 20.25  ? 129  GLY F N   1 
ATOM   2176 C  CA  . GLY B 1 129 ? 1.998   29.674  2.865   1.00 21.74  ? 129  GLY F CA  1 
ATOM   2177 C  C   . GLY B 1 129 ? 1.885   31.037  3.505   1.00 25.04  ? 129  GLY F C   1 
ATOM   2178 O  O   . GLY B 1 129 ? 0.904   31.753  3.290   1.00 28.18  ? 129  GLY F O   1 
ATOM   2179 N  N   . GLY B 1 130 ? 2.871   31.415  4.312   1.00 25.46  ? 130  GLY F N   1 
ATOM   2180 C  CA  . GLY B 1 130 ? 2.898   32.760  4.878   1.00 23.53  ? 130  GLY F CA  1 
ATOM   2181 C  C   . GLY B 1 130 ? 2.232   33.048  6.224   1.00 26.61  ? 130  GLY F C   1 
ATOM   2182 O  O   . GLY B 1 130 ? 2.497   34.078  6.798   1.00 30.83  ? 130  GLY F O   1 
ATOM   2183 N  N   . ASN B 1 131 ? 1.365   32.148  6.707   1.00 23.86  ? 131  ASN F N   1 
ATOM   2184 C  CA  . ASN B 1 131 ? 0.853   32.186  8.134   1.00 19.76  ? 131  ASN F CA  1 
ATOM   2185 C  C   . ASN B 1 131 ? 1.695   31.298  9.038   1.00 21.98  ? 131  ASN F C   1 
ATOM   2186 O  O   . ASN B 1 131 ? 2.532   30.507  8.581   1.00 22.83  ? 131  ASN F O   1 
ATOM   2187 C  CB  . ASN B 1 131 ? -0.664  31.848  8.188   1.00 21.37  ? 131  ASN F CB  1 
ATOM   2188 C  CG  . ASN B 1 131 ? -0.954  30.395  7.912   1.00 21.36  ? 131  ASN F CG  1 
ATOM   2189 O  OD1 . ASN B 1 131 ? -0.047  29.652  7.625   1.00 22.27  ? 131  ASN F OD1 1 
ATOM   2190 N  ND2 . ASN B 1 131 ? -2.219  29.980  8.016   1.00 27.03  ? 131  ASN F ND2 1 
ATOM   2191 N  N   . GLU B 1 132 ? 1.445   31.390  10.332  1.00 20.13  ? 132  GLU F N   1 
ATOM   2192 C  CA  . GLU B 1 132 ? 2.189   30.637  11.313  1.00 23.23  ? 132  GLU F CA  1 
ATOM   2193 C  C   . GLU B 1 132 ? 1.950   29.129  11.132  1.00 19.01  ? 132  GLU F C   1 
ATOM   2194 O  O   . GLU B 1 132 ? 2.843   28.294  11.339  1.00 24.53  ? 132  GLU F O   1 
ATOM   2195 C  CB  . GLU B 1 132 ? 1.723   31.052  12.699  1.00 26.60  ? 132  GLU F CB  1 
ATOM   2196 C  CG  . GLU B 1 132 ? 2.411   30.343  13.857  1.00 30.30  ? 132  GLU F CG  1 
ATOM   2197 C  CD  . GLU B 1 132 ? 2.132   30.992  15.201  0.50 33.16  ? 132  GLU F CD  1 
ATOM   2198 O  OE1 . GLU B 1 132 ? 1.045   31.594  15.373  0.50 37.42  ? 132  GLU F OE1 1 
ATOM   2199 O  OE2 . GLU B 1 132 ? 3.003   30.898  16.092  0.50 37.33  ? 132  GLU F OE2 1 
ATOM   2200 N  N   . GLU B 1 133 ? 0.706   28.766  10.844  1.00 17.96  ? 133  GLU F N   1 
ATOM   2201 C  CA  . GLU B 1 133 ? 0.351   27.346  10.837  1.00 18.64  ? 133  GLU F CA  1 
ATOM   2202 C  C   . GLU B 1 133 ? 1.052   26.631  9.654   1.00 16.45  ? 133  GLU F C   1 
ATOM   2203 O  O   . GLU B 1 133 ? 1.283   25.393  9.799   1.00 17.55  ? 133  GLU F O   1 
ATOM   2204 C  CB  . GLU B 1 133 ? -1.192  27.092  11.024  1.00 20.69  ? 133  GLU F CB  1 
ATOM   2205 C  CG  . GLU B 1 133 ? -1.794  25.674  11.108  1.00 20.81  ? 133  GLU F CG  1 
ATOM   2206 C  CD  . GLU B 1 133 ? -1.732  24.851  12.448  0.50 18.93  ? 133  GLU F CD  1 
ATOM   2207 O  OE1 . GLU B 1 133 ? -0.866  25.074  13.343  0.80 21.79  ? 133  GLU F OE1 1 
ATOM   2208 O  OE2 . GLU B 1 133 ? -2.573  23.902  12.589  0.50 19.28  ? 133  GLU F OE2 1 
ATOM   2209 N  N   . SER B 1 134 ? 1.487   27.351  8.591   1.00 16.56  ? 134  SER F N   1 
ATOM   2210 C  CA  . SER B 1 134 ? 2.271   26.780  7.498   1.00 15.43  ? 134  SER F CA  1 
ATOM   2211 C  C   . SER B 1 134 ? 3.472   26.119  8.084   1.00 16.93  ? 134  SER F C   1 
ATOM   2212 O  O   . SER B 1 134 ? 3.818   25.088  7.595   1.00 17.04  ? 134  SER F O   1 
ATOM   2213 C  CB  . SER B 1 134 ? 2.724   27.814  6.431   1.00 14.47  ? 134  SER F CB  1 
ATOM   2214 O  OG  . SER B 1 134 ? 3.371   27.337  5.334   1.00 17.38  ? 134  SER F OG  1 
ATOM   2215 N  N   . THR B 1 135 ? 4.075   26.686  9.137   1.00 17.67  ? 135  THR F N   1 
ATOM   2216 C  CA  . THR B 1 135 ? 5.299   26.176  9.761   1.00 17.92  ? 135  THR F CA  1 
ATOM   2217 C  C   . THR B 1 135 ? 5.128   24.997  10.709  1.00 15.36  ? 135  THR F C   1 
ATOM   2218 O  O   . THR B 1 135 ? 6.138   24.502  11.220  1.00 15.62  ? 135  THR F O   1 
ATOM   2219 C  CB  . THR B 1 135 ? 6.051   27.282  10.563  1.00 21.24  ? 135  THR F CB  1 
ATOM   2220 O  OG1 . THR B 1 135 ? 5.422   27.557  11.838  1.00 22.30  ? 135  THR F OG1 1 
ATOM   2221 C  CG2 . THR B 1 135 ? 6.111   28.552  9.770   1.00 20.60  ? 135  THR F CG2 1 
ATOM   2222 N  N   . LYS B 1 136 ? 3.887   24.551  10.939  1.00 15.74  ? 136  LYS F N   1 
ATOM   2223 C  CA  . LYS B 1 136 ? 3.597   23.400  11.765  1.00 14.95  ? 136  LYS F CA  1 
ATOM   2224 C  C   . LYS B 1 136 ? 2.959   22.292  10.984  1.00 13.05  ? 136  LYS F C   1 
ATOM   2225 O  O   . LYS B 1 136 ? 3.399   21.157  11.066  1.00 13.80  ? 136  LYS F O   1 
ATOM   2226 C  CB  . LYS B 1 136 ? 2.740   23.780  12.963  1.00 16.21  ? 136  LYS F CB  1 
ATOM   2227 C  CG  . LYS B 1 136 ? 3.527   24.590  13.967  1.00 20.39  ? 136  LYS F CG  1 
ATOM   2228 C  CD  . LYS B 1 136 ? 2.687   25.455  14.865  1.00 27.13  ? 136  LYS F CD  1 
ATOM   2229 C  CE  . LYS B 1 136 ? 2.369   24.784  16.174  1.00 27.20  ? 136  LYS F CE  1 
ATOM   2230 N  NZ  . LYS B 1 136 ? 3.205   25.361  17.254  1.00 23.85  ? 136  LYS F NZ  1 
ATOM   2231 N  N   . THR B 1 137 ? 1.904   22.617  10.231  1.00 13.27  ? 137  THR F N   1 
ATOM   2232 C  CA  . THR B 1 137 ? 1.115   21.614  9.536   1.00 12.59  ? 137  THR F CA  1 
ATOM   2233 C  C   . THR B 1 137 ? 1.054   21.778  8.023   1.00 11.91  ? 137  THR F C   1 
ATOM   2234 O  O   . THR B 1 137 ? 0.496   20.925  7.343   1.00 12.93  ? 137  THR F O   1 
ATOM   2235 C  CB  . THR B 1 137 ? -0.331  21.607  10.026  1.00 13.76  ? 137  THR F CB  1 
ATOM   2236 O  OG1 . THR B 1 137 ? -0.912  22.844  9.634   1.00 15.67  ? 137  THR F OG1 1 
ATOM   2237 C  CG2 . THR B 1 137 ? -0.439  21.477  11.506  1.00 15.49  ? 137  THR F CG2 1 
ATOM   2238 N  N   . GLY B 1 138 ? 1.550   22.884  7.494   1.00 12.87  ? 138  GLY F N   1 
ATOM   2239 C  CA  . GLY B 1 138 ? 1.401   23.180  6.063   1.00 13.56  ? 138  GLY F CA  1 
ATOM   2240 C  C   . GLY B 1 138 ? -0.023  23.548  5.659   1.00 13.77  ? 138  GLY F C   1 
ATOM   2241 O  O   . GLY B 1 138 ? -0.354  23.591  4.474   1.00 15.38  ? 138  GLY F O   1 
ATOM   2242 N  N   . ASN B 1 139 ? -0.867  23.791  6.656   1.00 14.14  ? 139  ASN F N   1 
ATOM   2243 C  CA  . ASN B 1 139 ? -2.275  24.149  6.436   1.00 15.30  ? 139  ASN F CA  1 
ATOM   2244 C  C   . ASN B 1 139 ? -3.021  23.053  5.668   1.00 15.19  ? 139  ASN F C   1 
ATOM   2245 O  O   . ASN B 1 139 ? -3.940  23.326  4.902   1.00 16.75  ? 139  ASN F O   1 
ATOM   2246 C  CB  . ASN B 1 139 ? -2.418  25.493  5.717   1.00 17.44  ? 139  ASN F CB  1 
ATOM   2247 C  CG  . ASN B 1 139 ? -1.991  26.638  6.582   1.00 18.56  ? 139  ASN F CG  1 
ATOM   2248 O  OD1 . ASN B 1 139 ? -2.619  26.931  7.607   1.00 20.74  ? 139  ASN F OD1 1 
ATOM   2249 N  ND2 . ASN B 1 139 ? -0.916  27.305  6.200   1.00 19.09  ? 139  ASN F ND2 1 
ATOM   2250 N  N   . ALA B 1 140 ? -2.651  21.789  5.897   1.00 14.03  ? 140  ALA F N   1 
ATOM   2251 C  CA  . ALA B 1 140 ? -3.232  20.695  5.142   1.00 13.80  ? 140  ALA F CA  1 
ATOM   2252 C  C   . ALA B 1 140 ? -4.578  20.199  5.695   1.00 13.92  ? 140  ALA F C   1 
ATOM   2253 O  O   . ALA B 1 140 ? -5.181  19.314  5.106   1.00 14.13  ? 140  ALA F O   1 
ATOM   2254 C  CB  . ALA B 1 140 ? -2.227  19.543  5.012   1.00 13.55  ? 140  ALA F CB  1 
ATOM   2255 N  N   . GLY B 1 141 ? -5.068  20.766  6.794   1.00 14.63  ? 141  GLY F N   1 
ATOM   2256 C  CA  . GLY B 1 141 ? -6.410  20.485  7.255   1.00 15.55  ? 141  GLY F CA  1 
ATOM   2257 C  C   . GLY B 1 141 ? -6.556  19.106  7.886   1.00 14.06  ? 141  GLY F C   1 
ATOM   2258 O  O   . GLY B 1 141 ? -5.597  18.520  8.421   1.00 14.65  ? 141  GLY F O   1 
ATOM   2259 N  N   . SER B 1 142 ? -7.789  18.614  7.848   1.00 14.40  ? 142  SER F N   1 
ATOM   2260 C  CA  . SER B 1 142 ? -8.165  17.453  8.599   1.00 14.03  ? 142  SER F CA  1 
ATOM   2261 C  C   . SER B 1 142 ? -7.545  16.176  8.016   1.00 12.54  ? 142  SER F C   1 
ATOM   2262 O  O   . SER B 1 142 ? -6.891  16.155  6.980   1.00 13.60  ? 142  SER F O   1 
ATOM   2263 C  CB  . SER B 1 142 ? -9.672  17.340  8.680   1.00 16.82  ? 142  SER F CB  1 
ATOM   2264 O  OG  . SER B 1 142 ? -10.209 16.965  7.446   1.00 21.56  ? 142  SER F OG  1 
ATOM   2265 N  N   . ARG B 1 143 ? -7.775  15.097  8.747   1.00 12.38  ? 143  ARG F N   1 
ATOM   2266 C  CA  . ARG B 1 143 ? -7.153  13.804  8.460   1.00 12.20  ? 143  ARG F CA  1 
ATOM   2267 C  C   . ARG B 1 143 ? -8.185  12.883  7.817   1.00 13.13  ? 143  ARG F C   1 
ATOM   2268 O  O   . ARG B 1 143 ? -9.108  12.411  8.469   1.00 16.02  ? 143  ARG F O   1 
ATOM   2269 C  CB  . ARG B 1 143 ? -6.616  13.198  9.758   1.00 11.84  ? 143  ARG F CB  1 
ATOM   2270 C  CG  . ARG B 1 143 ? -5.645  14.152  10.421  1.00 11.47  ? 143  ARG F CG  1 
ATOM   2271 C  CD  . ARG B 1 143 ? -5.085  13.676  11.731  1.00 12.20  ? 143  ARG F CD  1 
ATOM   2272 N  NE  . ARG B 1 143 ? -4.275  14.774  12.262  1.00 13.66  ? 143  ARG F NE  1 
ATOM   2273 C  CZ  . ARG B 1 143 ? -3.363  14.643  13.214  1.00 11.53  ? 143  ARG F CZ  1 
ATOM   2274 N  NH1 . ARG B 1 143 ? -3.110  13.489  13.794  1.00 11.74  ? 143  ARG F NH1 1 
ATOM   2275 N  NH2 . ARG B 1 143 ? -2.664  15.711  13.531  1.00 12.02  ? 143  ARG F NH2 1 
ATOM   2276 N  N   . LEU B 1 144 ? -8.053  12.642  6.523   1.00 12.55  ? 144  LEU F N   1 
ATOM   2277 C  CA  . LEU B 1 144 ? -9.063  11.875  5.797   1.00 13.26  ? 144  LEU F CA  1 
ATOM   2278 C  C   . LEU B 1 144 ? -8.915  10.373  6.036   1.00 12.99  ? 144  LEU F C   1 
ATOM   2279 O  O   . LEU B 1 144 ? -9.904  9.650   6.089   1.00 15.39  ? 144  LEU F O   1 
ATOM   2280 C  CB  . LEU B 1 144 ? -8.974  12.127  4.305   1.00 14.20  ? 144  LEU F CB  1 
ATOM   2281 C  CG  . LEU B 1 144 ? -9.185  13.559  3.829   1.00 16.05  ? 144  LEU F CG  1 
ATOM   2282 C  CD1 . LEU B 1 144 ? -9.012  13.624  2.322   1.00 20.03  ? 144  LEU F CD1 1 
ATOM   2283 C  CD2 . LEU B 1 144 ? -10.541 14.054  4.300   1.00 20.77  ? 144  LEU F CD2 1 
ATOM   2284 N  N   . ALA B 1 145 ? -7.677  9.897   6.122   1.00 12.33  ? 145  ALA F N   1 
ATOM   2285 C  CA  . ALA B 1 145 ? -7.414  8.471   6.313   1.00 12.16  ? 145  ALA F CA  1 
ATOM   2286 C  C   . ALA B 1 145 ? -6.028  8.325   6.893   1.00 10.73  ? 145  ALA F C   1 
ATOM   2287 O  O   . ALA B 1 145 ? -5.152  9.167   6.689   1.00 11.00  ? 145  ALA F O   1 
ATOM   2288 C  CB  . ALA B 1 145 ? -7.529  7.687   5.007   1.00 15.41  ? 145  ALA F CB  1 
ATOM   2289 N  N   . CYS B 1 146 ? -5.830  7.230   7.603   1.00 10.47  ? 146  CYS F N   1 
ATOM   2290 C  CA  . CYS B 1 146 ? -4.561  6.989   8.243   1.00 9.82   ? 146  CYS F CA  1 
ATOM   2291 C  C   . CYS B 1 146 ? -4.392  5.511   8.512   1.00 9.81   ? 146  CYS F C   1 
ATOM   2292 O  O   . CYS B 1 146 ? -5.354  4.732   8.440   1.00 11.18  ? 146  CYS F O   1 
ATOM   2293 C  CB  . CYS B 1 146 ? -4.422  7.792   9.533   1.00 10.82  ? 146  CYS F CB  1 
ATOM   2294 S  SG  . CYS B 1 146 ? -5.603  7.341   10.800  1.00 13.09  ? 146  CYS F SG  1 
ATOM   2295 N  N   . GLY B 1 147 ? -3.179  5.123   8.871   1.00 9.50   ? 147  GLY F N   1 
ATOM   2296 C  CA  . GLY B 1 147 ? -2.912  3.772   9.358   1.00 9.52   ? 147  GLY F CA  1 
ATOM   2297 C  C   . GLY B 1 147 ? -1.570  3.744   10.019  1.00 9.00   ? 147  GLY F C   1 
ATOM   2298 O  O   . GLY B 1 147 ? -0.740  4.637   9.822   1.00 9.64   ? 147  GLY F O   1 
ATOM   2299 N  N   . VAL B 1 148 ? -1.330  2.717   10.818  1.00 9.06   ? 148  VAL F N   1 
ATOM   2300 C  CA  . VAL B 1 148 ? -0.059  2.528   11.467  1.00 8.92   ? 148  VAL F CA  1 
ATOM   2301 C  C   . VAL B 1 148 ? 0.889   1.810   10.498  1.00 9.18   ? 148  VAL F C   1 
ATOM   2302 O  O   . VAL B 1 148 ? 0.517   0.819   9.859   1.00 11.25  ? 148  VAL F O   1 
ATOM   2303 C  CB  . VAL B 1 148 ? -0.205  1.738   12.787  1.00 10.33  ? 148  VAL F CB  1 
ATOM   2304 C  CG1 . VAL B 1 148 ? 1.127   1.581   13.501  1.00 11.52  ? 148  VAL F CG1 1 
ATOM   2305 C  CG2 . VAL B 1 148 ? -1.227  2.439   13.705  1.00 12.56  ? 148  VAL F CG2 1 
ATOM   2306 N  N   . ILE B 1 149 ? 2.112   2.294   10.400  1.00 9.20   ? 149  ILE F N   1 
ATOM   2307 C  CA  . ILE B 1 149 ? 3.114   1.720   9.502   1.00 9.11   ? 149  ILE F CA  1 
ATOM   2308 C  C   . ILE B 1 149 ? 3.713   0.480   10.187  1.00 9.02   ? 149  ILE F C   1 
ATOM   2309 O  O   . ILE B 1 149 ? 4.218   0.548   11.292  1.00 10.13  ? 149  ILE F O   1 
ATOM   2310 C  CB  . ILE B 1 149 ? 4.206   2.770   9.181   1.00 9.58   ? 149  ILE F CB  1 
ATOM   2311 C  CG1 . ILE B 1 149 ? 3.591   4.012   8.521   1.00 10.10  ? 149  ILE F CG1 1 
ATOM   2312 C  CG2 . ILE B 1 149 ? 5.273   2.141   8.314   1.00 10.87  ? 149  ILE F CG2 1 
ATOM   2313 C  CD1 . ILE B 1 149 ? 4.556   5.185   8.489   1.00 12.13  ? 149  ILE F CD1 1 
ATOM   2314 N  N   . GLY B 1 150 ? 3.609   -0.654  9.507   1.00 8.97   ? 150  GLY F N   1 
ATOM   2315 C  CA  . GLY B 1 150 ? 4.026   -1.909  10.064  1.00 9.63   ? 150  GLY F CA  1 
ATOM   2316 C  C   . GLY B 1 150 ? 5.166   -2.562  9.313   1.00 9.30   ? 150  GLY F C   1 
ATOM   2317 O  O   . GLY B 1 150 ? 5.386   -2.320  8.124   1.00 10.35  ? 150  GLY F O   1 
ATOM   2318 N  N   . ILE B 1 151 ? 5.857   -3.447  10.004  1.00 9.33   ? 151  ILE F N   1 
ATOM   2319 C  CA  . ILE B 1 151 ? 6.935   -4.252  9.424   1.00 9.73   ? 151  ILE F CA  1 
ATOM   2320 C  C   . ILE B 1 151 ? 6.335   -5.232  8.420   1.00 9.76   ? 151  ILE F C   1 
ATOM   2321 O  O   . ILE B 1 151 ? 5.378   -5.934  8.742   1.00 10.74  ? 151  ILE F O   1 
ATOM   2322 C  CB  . ILE B 1 151 ? 7.675   -5.018  10.554  1.00 10.78  ? 151  ILE F CB  1 
ATOM   2323 C  CG1 . ILE B 1 151 ? 8.368   -4.032  11.496  1.00 11.49  ? 151  ILE F CG1 1 
ATOM   2324 C  CG2 . ILE B 1 151 ? 8.639   -6.033  9.950   1.00 13.21  ? 151  ILE F CG2 1 
ATOM   2325 C  CD1 . ILE B 1 151 ? 8.861   -4.684  12.776  1.00 13.76  ? 151  ILE F CD1 1 
ATOM   2326 N  N   . ALA B 1 152 ? 6.920   -5.298  7.236   1.00 10.24  ? 152  ALA F N   1 
ATOM   2327 C  CA  . ALA B 1 152 ? 6.430   -6.180  6.183   1.00 10.98  ? 152  ALA F CA  1 
ATOM   2328 C  C   . ALA B 1 152 ? 7.434   -7.283  5.903   1.00 11.54  ? 152  ALA F C   1 
ATOM   2329 O  O   . ALA B 1 152 ? 8.621   -7.193  6.215   1.00 13.09  ? 152  ALA F O   1 
ATOM   2330 C  CB  . ALA B 1 152 ? 6.120   -5.399  4.901   1.00 13.40  ? 152  ALA F CB  1 
ATOM   2331 N  N   . GLN B 1 153 ? 6.935   -8.350  5.293   1.00 12.47  ? 153  GLN F N   1 
ATOM   2332 C  CA  . GLN B 1 153 ? 7.687   -9.522  4.936   1.00 13.94  ? 153  GLN F CA  1 
ATOM   2333 C  C   . GLN B 1 153 ? 8.667   -9.239  3.823   0.60 13.88  ? 153  GLN F C   1 
ATOM   2334 O  O   . GLN B 1 153 ? 8.319   -8.558  2.860   0.60 16.21  ? 153  GLN F O   1 
ATOM   2335 C  CB  . GLN B 1 153 ? 6.689   -10.647 4.530   1.00 15.11  ? 153  GLN F CB  1 
ATOM   2336 C  CG  . GLN B 1 153 ? 7.286   -11.938 4.108   1.00 15.46  ? 153  GLN F CG  1 
ATOM   2337 C  CD  . GLN B 1 153 ? 6.204   -12.971 3.805   1.00 15.23  ? 153  GLN F CD  1 
ATOM   2338 O  OE1 . GLN B 1 153 ? 5.074   -12.931 4.398   1.00 15.10  ? 153  GLN F OE1 1 
ATOM   2339 N  NE2 . GLN B 1 153 ? 6.466   -13.806 2.829   1.00 18.11  ? 153  GLN F NE2 1 
ATOM   2340 O  OXT . GLN B 1 153 ? 9.796   -9.768  3.845   0.60 17.97  ? 153  GLN F OXT 1 
HETATM 2341 C  C1  . ALE C 2 .   ? 14.567  -9.469  31.443  1.00 11.56  ? 1000 ALE A C1  1 
HETATM 2342 C  C2  . ALE C 2 .   ? 15.257  -10.652 31.672  1.00 11.43  ? 1000 ALE A C2  1 
HETATM 2343 C  C3  . ALE C 2 .   ? 16.469  -10.688 32.363  1.00 12.45  ? 1000 ALE A C3  1 
HETATM 2344 C  C4  . ALE C 2 .   ? 17.002  -9.513  32.867  1.00 14.21  ? 1000 ALE A C4  1 
HETATM 2345 C  C5  . ALE C 2 .   ? 16.326  -8.328  32.663  1.00 14.09  ? 1000 ALE A C5  1 
HETATM 2346 C  C6  . ALE C 2 .   ? 15.122  -8.305  31.963  1.00 13.20  ? 1000 ALE A C6  1 
HETATM 2347 O  O1  . ALE C 2 .   ? 17.106  -11.888 32.488  1.00 13.39  ? 1000 ALE A O1  1 
HETATM 2348 O  O2  . ALE C 2 .   ? 18.184  -9.566  33.534  1.00 15.99  ? 1000 ALE A O2  1 
HETATM 2349 O  O3  . ALE C 2 .   ? 12.389  -8.429  30.972  1.00 12.20  ? 1000 ALE A O3  1 
HETATM 2350 C  C9  . ALE C 2 .   ? 12.928  -9.525  26.839  1.00 12.74  ? 1000 ALE A C9  1 
HETATM 2351 N  N1  . ALE C 2 .   ? 12.529  -9.425  28.257  1.00 11.98  ? 1000 ALE A N1  1 
HETATM 2352 C  C8  . ALE C 2 .   ? 13.708  -9.385  29.141  1.00 11.90  ? 1000 ALE A C8  1 
HETATM 2353 C  C7  . ALE C 2 .   ? 13.329  -9.448  30.645  1.00 11.79  ? 1000 ALE A C7  1 
HETATM 2354 C  C1  . ALE D 2 .   ? 3.555   -1.047  34.940  0.70 16.16  ? 1001 ALE A C1  1 
HETATM 2355 C  C2  . ALE D 2 .   ? 4.596   -1.043  34.001  0.70 15.85  ? 1001 ALE A C2  1 
HETATM 2356 C  C3  . ALE D 2 .   ? 5.302   -2.206  33.711  0.70 13.40  ? 1001 ALE A C3  1 
HETATM 2357 C  C4  . ALE D 2 .   ? 5.004   -3.396  34.378  0.70 14.53  ? 1001 ALE A C4  1 
HETATM 2358 C  C5  . ALE D 2 .   ? 3.961   -3.413  35.310  0.70 16.18  ? 1001 ALE A C5  1 
HETATM 2359 C  C6  . ALE D 2 .   ? 3.246   -2.248  35.606  0.70 16.87  ? 1001 ALE A C6  1 
HETATM 2360 O  O1  . ALE D 2 .   ? 6.341   -2.153  32.851  0.70 11.91  ? 1001 ALE A O1  1 
HETATM 2361 O  O2  . ALE D 2 .   ? 5.737   -4.490  34.045  0.70 15.57  ? 1001 ALE A O2  1 
HETATM 2362 O  O3  . ALE D 2 .   ? 3.695   1.260   35.420  0.70 22.11  ? 1001 ALE A O3  1 
HETATM 2363 C  C9  . ALE D 2 .   ? -0.074  1.736   33.601  0.70 26.99  ? 1001 ALE A C9  1 
HETATM 2364 N  N1  . ALE D 2 .   ? 0.970   1.542   34.601  0.70 22.33  ? 1001 ALE A N1  1 
HETATM 2365 C  C8  . ALE D 2 .   ? 1.809   0.454   34.116  0.70 20.09  ? 1001 ALE A C8  1 
HETATM 2366 C  C7  . ALE D 2 .   ? 2.822   0.133   35.233  0.70 18.56  ? 1001 ALE A C7  1 
HETATM 2367 S  S   . SO4 E 3 .   ? -4.997  -23.453 13.703  0.60 17.03  ? 1154 SO4 A S   1 
HETATM 2368 O  O1  . SO4 E 3 .   ? -6.036  -23.568 14.777  0.60 18.93  ? 1154 SO4 A O1  1 
HETATM 2369 O  O2  . SO4 E 3 .   ? -4.121  -22.404 14.043  0.60 23.71  ? 1154 SO4 A O2  1 
HETATM 2370 O  O3  . SO4 E 3 .   ? -5.572  -23.186 12.370  0.60 30.03  ? 1154 SO4 A O3  1 
HETATM 2371 O  O4  . SO4 E 3 .   ? -4.026  -24.546 13.732  0.60 21.99  ? 1154 SO4 A O4  1 
HETATM 2372 CU CU  . CU  F 4 .   ? -2.185  -15.341 17.013  0.30 9.82   ? 1157 CU  A CU  1 
HETATM 2373 ZN ZN  . ZN  G 5 .   ? 3.100   -19.032 19.363  1.00 9.32   ? 1158 ZN  A ZN  1 
HETATM 2374 C  C   . ACT H 6 .   ? -21.561 -15.588 24.777  1.00 16.00  ? 1159 ACT A C   1 
HETATM 2375 O  O   . ACT H 6 .   ? -20.830 -16.537 24.305  1.00 16.89  ? 1159 ACT A O   1 
HETATM 2376 O  OXT . ACT H 6 .   ? -21.249 -14.313 24.816  1.00 20.98  ? 1159 ACT A OXT 1 
HETATM 2377 C  CH3 . ACT H 6 .   ? -22.850 -15.944 25.271  1.00 14.74  ? 1159 ACT A CH3 1 
HETATM 2378 S  S   . SO4 I 3 .   ? -7.373  -16.178 9.228   0.50 30.23  ? 1160 SO4 A S   1 
HETATM 2379 O  O1  . SO4 I 3 .   ? -8.498  -15.625 10.028  0.50 42.20  ? 1160 SO4 A O1  1 
HETATM 2380 O  O2  . SO4 I 3 .   ? -6.313  -15.172 9.037   0.50 27.27  ? 1160 SO4 A O2  1 
HETATM 2381 O  O3  . SO4 I 3 .   ? -7.913  -16.540 7.885   0.50 31.66  ? 1160 SO4 A O3  1 
HETATM 2382 O  O4  . SO4 I 3 .   ? -6.834  -17.406 9.867   0.50 29.98  ? 1160 SO4 A O4  1 
HETATM 2383 S  S   . SO4 J 3 .   ? -4.718  22.755  9.893   0.70 17.63  ? 1154 SO4 F S   1 
HETATM 2384 O  O1  . SO4 J 3 .   ? -4.590  23.861  10.837  0.70 23.03  ? 1154 SO4 F O1  1 
HETATM 2385 O  O2  . SO4 J 3 .   ? -3.476  22.049  9.622   0.70 21.56  ? 1154 SO4 F O2  1 
HETATM 2386 O  O3  . SO4 J 3 .   ? -5.152  23.219  8.552   0.70 19.99  ? 1154 SO4 F O3  1 
HETATM 2387 O  O4  . SO4 J 3 .   ? -5.658  21.727  10.450  0.70 21.36  ? 1154 SO4 F O4  1 
HETATM 2388 S  S   . SO4 K 3 .   ? -8.733  15.481  12.465  0.50 29.11  ? 1155 SO4 F S   1 
HETATM 2389 O  O1  . SO4 K 3 .   ? -7.933  16.708  12.209  0.50 32.87  ? 1155 SO4 F O1  1 
HETATM 2390 O  O2  . SO4 K 3 .   ? -9.912  15.854  13.293  0.50 33.67  ? 1155 SO4 F O2  1 
HETATM 2391 O  O3  . SO4 K 3 .   ? -7.912  14.465  13.164  0.50 23.96  ? 1155 SO4 F O3  1 
HETATM 2392 O  O4  . SO4 K 3 .   ? -9.183  14.995  11.156  0.50 20.94  ? 1155 SO4 F O4  1 
HETATM 2393 CU CU  . CU  L 4 .   ? -0.122  14.901  8.302   0.30 10.96  ? 1156 CU  F CU  1 
HETATM 2394 ZN ZN  . ZN  M 5 .   ? 5.522   18.724  8.891   1.00 9.97   ? 1157 ZN  F ZN  1 
HETATM 2395 O  O   . HOH N 7 .   ? -8.213  -15.623 3.355   1.00 25.58  ? 2001 HOH A O   1 
HETATM 2396 O  O   . HOH N 7 .   ? 9.517   4.796   33.643  1.00 26.49  ? 2002 HOH A O   1 
HETATM 2397 O  O   . HOH N 7 .   ? 6.939   4.776   35.000  1.00 31.79  ? 2003 HOH A O   1 
HETATM 2398 O  O   . HOH N 7 .   ? 11.264  1.725   29.070  1.00 22.63  ? 2004 HOH A O   1 
HETATM 2399 O  O   . HOH N 7 .   ? 8.896   4.926   22.186  1.00 34.22  ? 2005 HOH A O   1 
HETATM 2400 O  O   . HOH N 7 .   ? 6.341   5.860   24.393  1.00 15.43  ? 2006 HOH A O   1 
HETATM 2401 O  O   . HOH N 7 .   ? 7.029   2.944   21.860  1.00 16.01  ? 2007 HOH A O   1 
HETATM 2402 O  O   . HOH N 7 .   ? 3.879   9.601   28.408  1.00 32.25  ? 2008 HOH A O   1 
HETATM 2403 O  O   . HOH N 7 .   ? -5.052  0.809   13.832  1.00 19.44  ? 2009 HOH A O   1 
HETATM 2404 O  O   . HOH N 7 .   ? -1.417  3.081   25.225  1.00 24.36  ? 2010 HOH A O   1 
HETATM 2405 O  O   . HOH N 7 .   ? 0.280   2.615   26.845  1.00 20.88  ? 2011 HOH A O   1 
HETATM 2406 O  O   . HOH N 7 .   ? -14.576 -12.578 11.154  1.00 38.00  ? 2012 HOH A O   1 
HETATM 2407 O  O   . HOH N 7 .   ? -15.462 -12.284 13.545  1.00 23.78  ? 2013 HOH A O   1 
HETATM 2408 O  O   . HOH N 7 .   ? -3.484  0.013   16.061  1.00 9.29   ? 2014 HOH A O   1 
HETATM 2409 O  O   . HOH N 7 .   ? -6.659  -1.522  13.578  1.00 20.63  ? 2015 HOH A O   1 
HETATM 2410 O  O   . HOH N 7 .   ? -11.786 -1.066  17.774  1.00 45.97  ? 2016 HOH A O   1 
HETATM 2411 O  O   . HOH N 7 .   ? -8.617  -1.350  30.856  1.00 28.41  ? 2017 HOH A O   1 
HETATM 2412 O  O   . HOH N 7 .   ? -7.519  -3.963  11.788  1.00 29.74  ? 2018 HOH A O   1 
HETATM 2413 O  O   . HOH N 7 .   ? -14.414 -5.744  14.038  1.00 19.28  ? 2019 HOH A O   1 
HETATM 2414 O  O   . HOH N 7 .   ? -12.900 -3.389  10.464  1.00 37.34  ? 2020 HOH A O   1 
HETATM 2415 O  O   . HOH N 7 .   ? 9.874   -2.706  35.616  1.00 23.60  ? 2021 HOH A O   1 
HETATM 2416 O  O   . HOH N 7 .   ? 17.975  -5.006  32.925  1.00 22.23  ? 2022 HOH A O   1 
HETATM 2417 O  O   . HOH N 7 .   ? -12.652 -10.752 11.328  1.00 19.83  ? 2023 HOH A O   1 
HETATM 2418 O  O   . HOH N 7 .   ? -14.652 -9.692  14.132  1.00 16.03  ? 2024 HOH A O   1 
HETATM 2419 O  O   . HOH N 7 .   ? -19.918 -14.353 17.387  1.00 20.29  ? 2025 HOH A O   1 
HETATM 2420 O  O   . HOH N 7 .   ? -16.775 -13.717 15.413  1.00 20.13  ? 2026 HOH A O   1 
HETATM 2421 O  O   . HOH N 7 .   ? -11.202 0.178   19.644  1.00 23.84  ? 2027 HOH A O   1 
HETATM 2422 O  O   . HOH N 7 .   ? -16.691 -19.625 17.970  1.00 29.28  ? 2028 HOH A O   1 
HETATM 2423 O  O   . HOH N 7 .   ? -15.991 -16.523 15.726  1.00 22.12  ? 2029 HOH A O   1 
HETATM 2424 O  O   . HOH N 7 .   ? -5.624  3.848   24.168  1.00 15.14  ? 2030 HOH A O   1 
HETATM 2425 O  O   . HOH N 7 .   ? -7.078  2.909   26.274  1.00 19.67  ? 2031 HOH A O   1 
HETATM 2426 O  O   . HOH N 7 .   ? -7.843  0.452   29.023  1.00 24.05  ? 2032 HOH A O   1 
HETATM 2427 O  O   . HOH N 7 .   ? 12.671  -10.686 13.888  1.00 23.68  ? 2033 HOH A O   1 
HETATM 2428 O  O   . HOH N 7 .   ? 5.582   2.522   33.864  1.00 23.62  ? 2034 HOH A O   1 
HETATM 2429 O  O   . HOH N 7 .   ? -3.871  -1.206  9.649   1.00 22.17  ? 2035 HOH A O   1 
HETATM 2430 O  O   . HOH N 7 .   ? 12.826  -1.567  26.345  1.00 19.15  ? 2036 HOH A O   1 
HETATM 2431 O  O   . HOH N 7 .   ? 11.088  -7.104  27.983  1.00 13.00  ? 2037 HOH A O   1 
HETATM 2432 O  O   . HOH N 7 .   ? 9.755   -2.542  32.820  1.00 13.82  ? 2038 HOH A O   1 
HETATM 2433 O  O   . HOH N 7 .   ? 0.539   -19.158 10.857  1.00 21.30  ? 2039 HOH A O   1 
HETATM 2434 O  O   . HOH N 7 .   ? 15.274  -4.590  32.637  1.00 20.79  ? 2040 HOH A O   1 
HETATM 2435 O  O   . HOH N 7 .   ? 17.961  -17.089 17.394  1.00 21.99  ? 2041 HOH A O   1 
HETATM 2436 O  O   . HOH N 7 .   ? 18.859  -13.839 14.441  1.00 29.95  ? 2042 HOH A O   1 
HETATM 2437 O  O   . HOH N 7 .   ? 16.002  -10.919 15.522  1.00 23.58  ? 2043 HOH A O   1 
HETATM 2438 O  O   . HOH N 7 .   ? 15.121  2.460   31.379  1.00 40.60  ? 2044 HOH A O   1 
HETATM 2439 O  O   . HOH N 7 .   ? 17.011  -1.221  32.244  1.00 34.72  ? 2045 HOH A O   1 
HETATM 2440 O  O   . HOH N 7 .   ? 11.756  -16.269 24.606  1.00 21.30  ? 2046 HOH A O   1 
HETATM 2441 O  O   . HOH N 7 .   ? 18.884  -5.297  30.383  1.00 21.43  ? 2047 HOH A O   1 
HETATM 2442 O  O   . HOH N 7 .   ? 19.847  -3.257  25.903  1.00 23.16  ? 2048 HOH A O   1 
HETATM 2443 O  O   . HOH N 7 .   ? 14.303  -4.478  24.855  1.00 20.15  ? 2049 HOH A O   1 
HETATM 2444 O  O   . HOH N 7 .   ? 17.845  -4.282  24.093  1.00 26.57  ? 2050 HOH A O   1 
HETATM 2445 O  O   . HOH N 7 .   ? 8.143   -26.922 23.898  1.00 31.61  ? 2051 HOH A O   1 
HETATM 2446 O  O   . HOH N 7 .   ? -0.740  -18.828 31.315  1.00 24.13  ? 2052 HOH A O   1 
HETATM 2447 O  O   . HOH N 7 .   ? 0.069   -13.820 31.067  1.00 13.04  ? 2053 HOH A O   1 
HETATM 2448 O  O   . HOH N 7 .   ? 4.970   -17.295 36.305  1.00 33.37  ? 2054 HOH A O   1 
HETATM 2449 O  O   . HOH N 7 .   ? -10.788 -2.993  30.720  1.00 28.60  ? 2055 HOH A O   1 
HETATM 2450 O  O   . HOH N 7 .   ? -8.012  -3.998  32.048  1.00 21.89  ? 2056 HOH A O   1 
HETATM 2451 O  O   . HOH N 7 .   ? -13.701 -2.811  23.775  1.00 39.55  ? 2057 HOH A O   1 
HETATM 2452 O  O   . HOH N 7 .   ? -19.855 -8.390  23.216  1.00 15.06  ? 2058 HOH A O   1 
HETATM 2453 O  O   . HOH N 7 .   ? -17.317 -13.299 17.954  1.00 15.69  ? 2059 HOH A O   1 
HETATM 2454 O  O   . HOH N 7 .   ? -15.570 -14.835 19.369  1.00 13.96  ? 2060 HOH A O   1 
HETATM 2455 O  O   . HOH N 7 .   ? -15.105 -17.393 18.314  1.00 17.24  ? 2061 HOH A O   1 
HETATM 2456 O  O   . HOH N 7 .   ? -15.808 -19.284 22.801  1.00 27.56  ? 2062 HOH A O   1 
HETATM 2457 O  O   . HOH N 7 .   ? -18.663 -20.767 26.134  1.00 28.33  ? 2063 HOH A O   1 
HETATM 2458 O  O   . HOH N 7 .   ? -19.399 -15.179 32.035  1.00 16.66  ? 2064 HOH A O   1 
HETATM 2459 O  O   . HOH N 7 .   ? -18.973 -17.234 32.124  1.00 29.81  ? 2065 HOH A O   1 
HETATM 2460 O  O   . HOH N 7 .   ? 9.560   1.397   18.535  1.00 24.35  ? 2066 HOH A O   1 
HETATM 2461 O  O   . HOH N 7 .   ? 11.861  -4.124  15.336  1.00 32.73  ? 2067 HOH A O   1 
HETATM 2462 O  O   . HOH N 7 .   ? -13.013 -19.106 21.752  1.00 23.75  ? 2068 HOH A O   1 
HETATM 2463 O  O   . HOH N 7 .   ? 11.132  -1.646  12.830  1.00 23.82  ? 2069 HOH A O   1 
HETATM 2464 O  O   . HOH N 7 .   ? 12.298  -5.117  9.622   1.00 37.08  ? 2070 HOH A O   1 
HETATM 2465 O  O   . HOH N 7 .   ? -7.583  -25.516 23.836  1.00 27.23  ? 2071 HOH A O   1 
HETATM 2466 O  O   . HOH N 7 .   ? -2.685  -19.054 16.840  1.00 12.50  ? 2072 HOH A O   1 
HETATM 2467 O  O   . HOH N 7 .   ? 10.121  -9.588  10.859  1.00 25.10  ? 2073 HOH A O   1 
HETATM 2468 O  O   . HOH N 7 .   ? 11.378  -12.895 13.230  1.00 27.50  ? 2074 HOH A O   1 
HETATM 2469 O  O   . HOH N 7 .   ? -0.466  -2.885  7.588   1.00 11.84  ? 2075 HOH A O   1 
HETATM 2470 O  O   . HOH N 7 .   ? 1.321   -9.727  2.947   1.00 21.60  ? 2076 HOH A O   1 
HETATM 2471 O  O   . HOH N 7 .   ? 4.166   -8.498  4.812   1.00 21.32  ? 2077 HOH A O   1 
HETATM 2472 O  O   . HOH N 7 .   ? 3.212   -6.020  1.808   1.00 31.45  ? 2078 HOH A O   1 
HETATM 2473 O  O   . HOH N 7 .   ? -5.346  -3.039  10.975  1.00 22.86  ? 2079 HOH A O   1 
HETATM 2474 O  O   . HOH N 7 .   ? -6.524  -1.415  8.916   1.00 26.82  ? 2080 HOH A O   1 
HETATM 2475 O  O   . HOH N 7 .   ? -5.049  -3.014  1.321   1.00 28.30  ? 2081 HOH A O   1 
HETATM 2476 O  O   . HOH N 7 .   ? 0.700   -4.381  0.417   1.00 19.98  ? 2082 HOH A O   1 
HETATM 2477 O  O   . HOH N 7 .   ? -8.954  -9.868  2.110   1.00 25.73  ? 2083 HOH A O   1 
HETATM 2478 O  O   . HOH N 7 .   ? -3.867  -15.477 3.223   1.00 28.60  ? 2084 HOH A O   1 
HETATM 2479 O  O   . HOH N 7 .   ? -3.174  -12.854 3.783   1.00 28.43  ? 2085 HOH A O   1 
HETATM 2480 O  O   . HOH N 7 .   ? 2.915   -10.993 4.916   1.00 15.03  ? 2086 HOH A O   1 
HETATM 2481 O  O   . HOH N 7 .   ? 0.612   -18.592 13.510  1.00 21.35  ? 2087 HOH A O   1 
HETATM 2482 O  O   . HOH N 7 .   ? 2.871   -19.548 14.577  1.00 17.79  ? 2088 HOH A O   1 
HETATM 2483 O  O   . HOH N 7 .   ? 5.788   -18.608 14.858  1.00 16.73  ? 2089 HOH A O   1 
HETATM 2484 O  O   . HOH N 7 .   ? 6.871   -17.734 13.150  1.00 23.17  ? 2090 HOH A O   1 
HETATM 2485 O  O   . HOH N 7 .   ? 10.803  -16.323 19.613  1.00 11.10  ? 2091 HOH A O   1 
HETATM 2486 O  O   . HOH N 7 .   ? 7.734   -19.481 14.013  1.00 67.83  ? 2092 HOH A O   1 
HETATM 2487 O  O   . HOH N 7 .   ? 16.132  -17.352 15.270  1.00 21.84  ? 2093 HOH A O   1 
HETATM 2488 O  O   . HOH N 7 .   ? 15.652  -13.550 14.454  1.00 26.35  ? 2094 HOH A O   1 
HETATM 2489 O  O   . HOH N 7 .   ? 17.319  -18.884 19.495  1.00 24.00  ? 2095 HOH A O   1 
HETATM 2490 O  O   . HOH N 7 .   ? 15.372  -20.614 12.480  1.00 40.69  ? 2096 HOH A O   1 
HETATM 2491 O  O   . HOH N 7 .   ? 13.976  -18.190 23.500  1.00 27.84  ? 2097 HOH A O   1 
HETATM 2492 O  O   . HOH N 7 .   ? 6.124   -24.963 24.503  1.00 18.06  ? 2098 HOH A O   1 
HETATM 2493 O  O   . HOH N 7 .   ? 0.390   -18.320 23.865  1.00 10.71  ? 2099 HOH A O   1 
HETATM 2494 O  O   . HOH N 7 .   ? 1.658   -19.958 30.263  1.00 13.12  ? 2100 HOH A O   1 
HETATM 2495 O  O   . HOH N 7 .   ? 8.079   -17.023 29.813  1.00 15.30  ? 2101 HOH A O   1 
HETATM 2496 O  O   . HOH N 7 .   ? 6.036   -13.433 31.156  1.00 12.88  ? 2102 HOH A O   1 
HETATM 2497 O  O   . HOH N 7 .   ? 5.625   -21.188 34.802  1.00 26.48  ? 2103 HOH A O   1 
HETATM 2498 O  O   . HOH N 7 .   ? 2.623   -12.968 30.605  1.00 12.68  ? 2104 HOH A O   1 
HETATM 2499 O  O   . HOH N 7 .   ? 1.886   -12.292 35.096  1.00 24.58  ? 2105 HOH A O   1 
HETATM 2500 O  O   . HOH N 7 .   ? 6.965   -12.434 34.423  1.00 32.17  ? 2106 HOH A O   1 
HETATM 2501 O  O   . HOH N 7 .   ? 1.981   -24.681 28.358  1.00 18.71  ? 2107 HOH A O   1 
HETATM 2502 O  O   . HOH N 7 .   ? 2.294   -22.391 31.416  1.00 19.94  ? 2108 HOH A O   1 
HETATM 2503 O  O   . HOH N 7 .   ? 4.079   -25.931 26.080  1.00 26.60  ? 2109 HOH A O   1 
HETATM 2504 O  O   . HOH N 7 .   ? 11.603  -17.772 26.974  1.00 14.83  ? 2110 HOH A O   1 
HETATM 2505 O  O   . HOH N 7 .   ? 12.828  -25.243 20.021  1.00 35.37  ? 2111 HOH A O   1 
HETATM 2506 O  O   . HOH N 7 .   ? 11.173  -17.042 22.195  1.00 14.46  ? 2112 HOH A O   1 
HETATM 2507 O  O   . HOH N 7 .   ? -1.969  -14.194 29.220  1.00 15.07  ? 2113 HOH A O   1 
HETATM 2508 O  O   . HOH N 7 .   ? -2.586  -17.282 29.481  1.00 14.77  ? 2114 HOH A O   1 
HETATM 2509 O  O   . HOH N 7 .   ? -7.424  -15.189 30.175  1.00 22.47  ? 2115 HOH A O   1 
HETATM 2510 O  O   . HOH N 7 .   ? -4.505  -13.170 29.912  1.00 18.07  ? 2116 HOH A O   1 
HETATM 2511 O  O   . HOH N 7 .   ? -4.622  -19.147 29.079  1.00 18.55  ? 2117 HOH A O   1 
HETATM 2512 O  O   . HOH N 7 .   ? -8.675  -11.504 29.679  1.00 14.64  ? 2118 HOH A O   1 
HETATM 2513 O  O   . HOH N 7 .   ? -12.414 -10.720 31.087  1.00 33.85  ? 2119 HOH A O   1 
HETATM 2514 O  O   . HOH N 7 .   ? -13.744 -13.656 33.724  1.00 16.96  ? 2120 HOH A O   1 
HETATM 2515 O  O   . HOH N 7 .   ? -25.232 -12.997 27.601  1.00 13.93  ? 2121 HOH A O   1 
HETATM 2516 O  O   . HOH N 7 .   ? -22.903 -7.469  25.780  1.00 20.10  ? 2122 HOH A O   1 
HETATM 2517 O  O   . HOH N 7 .   ? -15.138 -5.637  31.320  1.00 29.55  ? 2123 HOH A O   1 
HETATM 2518 O  O   . HOH N 7 .   ? -10.239 -5.335  32.331  1.00 20.63  ? 2124 HOH A O   1 
HETATM 2519 O  O   . HOH N 7 .   ? -11.176 -4.134  35.095  1.00 24.02  ? 2125 HOH A O   1 
HETATM 2520 O  O   . HOH N 7 .   ? -6.076  -10.924 30.541  1.00 16.14  ? 2126 HOH A O   1 
HETATM 2521 O  O   . HOH N 7 .   ? -2.736  -11.907 33.781  1.00 27.10  ? 2127 HOH A O   1 
HETATM 2522 O  O   . HOH N 7 .   ? -0.095  -11.843 33.137  1.00 15.91  ? 2128 HOH A O   1 
HETATM 2523 O  O   . HOH N 7 .   ? 8.229   0.767   20.823  1.00 13.52  ? 2129 HOH A O   1 
HETATM 2524 O  O   . HOH N 7 .   ? 11.646  1.925   21.987  1.00 27.30  ? 2130 HOH A O   1 
HETATM 2525 O  O   . HOH N 7 .   ? 14.570  -6.766  23.053  1.00 14.25  ? 2131 HOH A O   1 
HETATM 2526 O  O   . HOH N 7 .   ? 15.728  -1.151  20.004  1.00 76.47  ? 2132 HOH A O   1 
HETATM 2527 O  O   . HOH N 7 .   ? 11.601  -6.694  16.818  1.00 18.82  ? 2133 HOH A O   1 
HETATM 2528 O  O   . HOH N 7 .   ? 13.528  -2.949  17.411  1.00 28.35  ? 2134 HOH A O   1 
HETATM 2529 O  O   . HOH N 7 .   ? 18.986  -5.883  19.193  1.00 24.26  ? 2135 HOH A O   1 
HETATM 2530 O  O   . HOH N 7 .   ? 17.896  -6.076  21.886  1.00 19.77  ? 2136 HOH A O   1 
HETATM 2531 O  O   . HOH N 7 .   ? 13.715  -9.427  15.992  1.00 19.71  ? 2137 HOH A O   1 
HETATM 2532 O  O   . HOH N 7 .   ? 17.727  -11.694 22.383  1.00 23.85  ? 2138 HOH A O   1 
HETATM 2533 O  O   . HOH N 7 .   ? 16.625  -12.239 17.873  1.00 22.82  ? 2139 HOH A O   1 
HETATM 2534 O  O   . HOH N 7 .   ? 13.536  -14.251 25.219  1.00 13.90  ? 2140 HOH A O   1 
HETATM 2535 O  O   . HOH N 7 .   ? 8.824   -1.051  14.513  1.00 28.97  ? 2141 HOH A O   1 
HETATM 2536 O  O   . HOH N 7 .   ? 12.143  -7.787  11.761  1.00 35.33  ? 2142 HOH A O   1 
HETATM 2537 O  O   . HOH N 7 .   ? -4.196  -19.950 14.656  1.00 18.36  ? 2143 HOH A O   1 
HETATM 2538 O  O   . HOH N 7 .   ? -14.208 -20.456 20.781  1.00 22.60  ? 2144 HOH A O   1 
HETATM 2539 O  O   . HOH N 7 .   ? -15.195 -21.773 17.046  1.00 27.48  ? 2145 HOH A O   1 
HETATM 2540 O  O   . HOH N 7 .   ? -11.238 -23.713 21.932  1.00 24.67  ? 2146 HOH A O   1 
HETATM 2541 O  O   . HOH N 7 .   ? -8.392  -24.828 20.859  1.00 22.61  ? 2147 HOH A O   1 
HETATM 2542 O  O   . HOH N 7 .   ? -5.910  -28.640 21.637  1.00 26.99  ? 2148 HOH A O   1 
HETATM 2543 O  O   . HOH N 7 .   ? 1.529   -30.810 22.758  1.00 24.63  ? 2149 HOH A O   1 
HETATM 2544 O  O   . HOH N 7 .   ? -2.856  -34.885 19.562  1.00 27.74  ? 2150 HOH A O   1 
HETATM 2545 O  O   . HOH N 7 .   ? -1.704  -30.909 13.912  1.00 22.09  ? 2151 HOH A O   1 
HETATM 2546 O  O   . HOH N 7 .   ? 3.593   -27.629 10.855  1.00 39.91  ? 2152 HOH A O   1 
HETATM 2547 O  O   . HOH N 7 .   ? -4.879  -17.949 12.076  1.00 24.99  ? 2153 HOH A O   1 
HETATM 2548 O  O   . HOH N 7 .   ? -12.147 -15.273 11.531  1.00 35.08  ? 2154 HOH A O   1 
HETATM 2549 O  O   . HOH N 7 .   ? -2.107  -18.190 13.699  1.00 20.71  ? 2155 HOH A O   1 
HETATM 2550 O  O   . HOH N 7 .   ? 6.204   8.608   22.136  1.00 21.55  ? 2156 HOH A O   1 
HETATM 2551 O  O   . HOH N 7 .   ? -0.401  8.142   21.883  1.00 18.37  ? 2157 HOH A O   1 
HETATM 2552 O  O   . HOH N 7 .   ? -1.588  10.627  21.373  1.00 13.12  ? 2158 HOH A O   1 
HETATM 2553 O  O   . HOH N 7 .   ? 5.798   10.911  23.920  1.00 27.44  ? 2159 HOH A O   1 
HETATM 2554 O  O   . HOH N 7 .   ? -21.805 -18.591 24.113  1.00 24.11  ? 2160 HOH A O   1 
HETATM 2555 O  O   . HOH N 7 .   ? -8.558  -14.500 5.851   1.00 34.09  ? 2161 HOH A O   1 
HETATM 2556 O  O   . HOH O 7 .   ? -12.427 17.962  15.928  1.00 27.28  ? 2001 HOH F O   1 
HETATM 2557 O  O   . HOH O 7 .   ? 18.782  -5.055  -0.099  1.00 36.80  ? 2002 HOH F O   1 
HETATM 2558 O  O   . HOH O 7 .   ? 12.026  -7.913  4.133   1.00 29.98  ? 2003 HOH F O   1 
HETATM 2559 O  O   . HOH O 7 .   ? 17.569  -1.787  4.751   1.00 34.84  ? 2004 HOH F O   1 
HETATM 2560 O  O   . HOH O 7 .   ? 11.204  -6.157  6.122   1.00 18.39  ? 2005 HOH F O   1 
HETATM 2561 O  O   . HOH O 7 .   ? 10.562  -3.210  8.651   1.00 20.33  ? 2006 HOH F O   1 
HETATM 2562 O  O   . HOH O 7 .   ? 7.166   -8.235  -1.800  1.00 27.11  ? 2007 HOH F O   1 
HETATM 2563 O  O   . HOH O 7 .   ? 4.875   -3.415  1.441   1.00 28.34  ? 2008 HOH F O   1 
HETATM 2564 O  O   . HOH O 7 .   ? 7.196   -3.036  0.967   1.00 26.19  ? 2009 HOH F O   1 
HETATM 2565 O  O   . HOH O 7 .   ? -1.473  -0.420  8.458   1.00 10.23  ? 2010 HOH F O   1 
HETATM 2566 O  O   . HOH O 7 .   ? -5.459  1.198   9.091   1.00 23.55  ? 2011 HOH F O   1 
HETATM 2567 O  O   . HOH O 7 .   ? -6.999  3.448   10.232  1.00 28.16  ? 2012 HOH F O   1 
HETATM 2568 O  O   . HOH O 7 .   ? -8.853  5.880   11.612  1.00 33.30  ? 2013 HOH F O   1 
HETATM 2569 O  O   . HOH O 7 .   ? 19.569  2.223   -2.068  1.00 37.76  ? 2014 HOH F O   1 
HETATM 2570 O  O   . HOH O 7 .   ? -12.071 10.918  4.991   1.00 25.08  ? 2015 HOH F O   1 
HETATM 2571 O  O   . HOH O 7 .   ? -10.315 9.928   9.305   1.00 26.31  ? 2016 HOH F O   1 
HETATM 2572 O  O   . HOH O 7 .   ? -17.259 6.597   -2.824  1.00 36.40  ? 2017 HOH F O   1 
HETATM 2573 O  O   . HOH O 7 .   ? -11.557 4.466   -7.299  1.00 33.99  ? 2018 HOH F O   1 
HETATM 2574 O  O   . HOH O 7 .   ? -1.097  0.538   -3.530  1.00 25.37  ? 2019 HOH F O   1 
HETATM 2575 O  O   . HOH O 7 .   ? 15.333  1.702   -1.312  1.00 26.79  ? 2020 HOH F O   1 
HETATM 2576 O  O   . HOH O 7 .   ? 17.092  6.860   5.303   1.00 24.31  ? 2021 HOH F O   1 
HETATM 2577 O  O   . HOH O 7 .   ? 18.149  2.200   0.333   1.00 26.34  ? 2022 HOH F O   1 
HETATM 2578 O  O   . HOH O 7 .   ? 18.726  18.791  13.027  1.00 31.87  ? 2023 HOH F O   1 
HETATM 2579 O  O   . HOH O 7 .   ? 19.412  8.191   3.448   1.00 27.73  ? 2024 HOH F O   1 
HETATM 2580 O  O   . HOH O 7 .   ? 15.487  15.967  8.564   1.00 25.03  ? 2025 HOH F O   1 
HETATM 2581 O  O   . HOH O 7 .   ? 8.967   13.566  -2.615  1.00 19.99  ? 2026 HOH F O   1 
HETATM 2582 O  O   . HOH O 7 .   ? 4.493   -2.034  -7.801  1.00 37.46  ? 2027 HOH F O   1 
HETATM 2583 O  O   . HOH O 7 .   ? 2.567   3.862   -7.617  1.00 36.65  ? 2028 HOH F O   1 
HETATM 2584 O  O   . HOH O 7 .   ? -6.473  2.015   -3.305  1.00 39.12  ? 2029 HOH F O   1 
HETATM 2585 O  O   . HOH O 7 .   ? -11.603 7.099   -6.289  1.00 28.28  ? 2030 HOH F O   1 
HETATM 2586 O  O   . HOH O 7 .   ? -12.886 12.508  -0.220  1.00 24.49  ? 2031 HOH F O   1 
HETATM 2587 O  O   . HOH O 7 .   ? 9.814   15.827  -3.923  1.00 29.11  ? 2032 HOH F O   1 
HETATM 2588 O  O   . HOH O 7 .   ? -10.660 14.076  -0.386  1.00 18.56  ? 2033 HOH F O   1 
HETATM 2589 O  O   . HOH O 7 .   ? -10.683 16.741  0.712   1.00 19.35  ? 2034 HOH F O   1 
HETATM 2590 O  O   . HOH O 7 .   ? -9.272  18.517  -3.330  1.00 27.28  ? 2035 HOH F O   1 
HETATM 2591 O  O   . HOH O 7 .   ? -12.954 16.212  -6.872  1.00 31.41  ? 2036 HOH F O   1 
HETATM 2592 O  O   . HOH O 7 .   ? -8.816  19.754  -13.569 1.00 16.25  ? 2037 HOH F O   1 
HETATM 2593 O  O   . HOH O 7 .   ? -7.393  18.472  -1.143  1.00 28.05  ? 2038 HOH F O   1 
HETATM 2594 O  O   . HOH O 7 .   ? -0.774  18.562  8.178   1.00 12.80  ? 2039 HOH F O   1 
HETATM 2595 O  O   . HOH O 7 .   ? -4.215  28.128  3.984   1.00 34.13  ? 2040 HOH F O   1 
HETATM 2596 O  O   . HOH O 7 .   ? -3.037  20.515  14.536  1.00 31.64  ? 2041 HOH F O   1 
HETATM 2597 O  O   . HOH O 7 .   ? 7.507   9.441   19.662  1.00 21.32  ? 2042 HOH F O   1 
HETATM 2598 O  O   . HOH O 7 .   ? -3.102  2.471   17.345  1.00 10.85  ? 2043 HOH F O   1 
HETATM 2599 O  O   . HOH O 7 .   ? -3.970  9.319   22.266  1.00 18.64  ? 2044 HOH F O   1 
HETATM 2600 O  O   . HOH O 7 .   ? -2.492  5.650   24.077  1.00 28.67  ? 2045 HOH F O   1 
HETATM 2601 O  O   . HOH O 7 .   ? -10.277 3.735   16.023  1.00 26.82  ? 2046 HOH F O   1 
HETATM 2602 O  O   . HOH O 7 .   ? -5.278  2.750   12.094  1.00 24.97  ? 2047 HOH F O   1 
HETATM 2603 O  O   . HOH O 7 .   ? -7.645  1.067   13.329  1.00 25.41  ? 2048 HOH F O   1 
HETATM 2604 O  O   . HOH O 7 .   ? -10.216 2.547   20.591  1.00 18.37  ? 2049 HOH F O   1 
HETATM 2605 O  O   . HOH O 7 .   ? -13.295 9.577   17.882  1.00 23.61  ? 2050 HOH F O   1 
HETATM 2606 O  O   . HOH O 7 .   ? -11.323 11.996  16.406  1.00 27.39  ? 2051 HOH F O   1 
HETATM 2607 O  O   . HOH O 7 .   ? -4.811  15.476  16.289  1.00 16.70  ? 2052 HOH F O   1 
HETATM 2608 O  O   . HOH O 7 .   ? -7.540  12.301  19.258  1.00 21.08  ? 2053 HOH F O   1 
HETATM 2609 O  O   . HOH O 7 .   ? -6.714  16.703  17.893  1.00 28.60  ? 2054 HOH F O   1 
HETATM 2610 O  O   . HOH O 7 .   ? -6.443  10.329  21.520  1.00 17.52  ? 2055 HOH F O   1 
HETATM 2611 O  O   . HOH O 7 .   ? -2.258  16.517  16.461  1.00 16.00  ? 2056 HOH F O   1 
HETATM 2612 O  O   . HOH O 7 .   ? 0.478   18.224  12.845  1.00 25.17  ? 2057 HOH F O   1 
HETATM 2613 O  O   . HOH O 7 .   ? 2.992   19.086  13.059  1.00 14.70  ? 2058 HOH F O   1 
HETATM 2614 O  O   . HOH O 7 .   ? 5.523   18.355  14.193  1.00 14.95  ? 2059 HOH F O   1 
HETATM 2615 O  O   . HOH O 7 .   ? 12.385  16.251  12.488  1.00 11.16  ? 2060 HOH F O   1 
HETATM 2616 O  O   . HOH O 7 .   ? 14.799  17.269  19.058  1.00 11.50  ? 2061 HOH F O   1 
HETATM 2617 O  O   . HOH O 7 .   ? 17.917  18.719  16.303  1.00 16.77  ? 2062 HOH F O   1 
HETATM 2618 O  O   . HOH O 7 .   ? 13.939  24.680  15.072  1.00 21.12  ? 2063 HOH F O   1 
HETATM 2619 O  O   . HOH O 7 .   ? 6.587   22.065  14.004  1.00 13.91  ? 2064 HOH F O   1 
HETATM 2620 O  O   . HOH O 7 .   ? 16.784  18.430  11.054  1.00 22.67  ? 2065 HOH F O   1 
HETATM 2621 O  O   . HOH O 7 .   ? 7.938   26.468  7.723   1.00 27.68  ? 2066 HOH F O   1 
HETATM 2622 O  O   . HOH O 7 .   ? 10.688  24.752  5.937   1.00 22.40  ? 2067 HOH F O   1 
HETATM 2623 O  O   . HOH O 7 .   ? 5.483   18.043  3.628   1.00 13.25  ? 2068 HOH F O   1 
HETATM 2624 O  O   . HOH O 7 .   ? 9.765   19.756  -1.242  1.00 18.46  ? 2069 HOH F O   1 
HETATM 2625 O  O   . HOH O 7 .   ? 10.698  22.290  -1.709  1.00 27.73  ? 2070 HOH F O   1 
HETATM 2626 O  O   . HOH O 7 .   ? 9.031   24.355  0.697   1.00 25.69  ? 2071 HOH F O   1 
HETATM 2627 O  O   . HOH O 7 .   ? 9.620   25.642  3.595   1.00 31.52  ? 2072 HOH F O   1 
HETATM 2628 O  O   . HOH O 7 .   ? 16.417  17.605  6.638   1.00 26.71  ? 2073 HOH F O   1 
HETATM 2629 O  O   . HOH O 7 .   ? 17.259  25.527  6.066   1.00 35.30  ? 2074 HOH F O   1 
HETATM 2630 O  O   . HOH O 7 .   ? 14.135  17.074  10.564  1.00 15.73  ? 2075 HOH F O   1 
HETATM 2631 O  O   . HOH O 7 .   ? 6.241   14.025  -2.112  1.00 20.65  ? 2076 HOH F O   1 
HETATM 2632 O  O   . HOH O 7 .   ? 5.757   16.861  -2.696  1.00 21.38  ? 2077 HOH F O   1 
HETATM 2633 O  O   . HOH O 7 .   ? 1.938   15.212  -5.695  1.00 26.01  ? 2078 HOH F O   1 
HETATM 2634 O  O   . HOH O 7 .   ? 4.382   12.885  -3.951  1.00 24.47  ? 2079 HOH F O   1 
HETATM 2635 O  O   . HOH O 7 .   ? 0.671   11.547  -6.032  1.00 25.01  ? 2080 HOH F O   1 
HETATM 2636 O  O   . HOH O 7 .   ? -1.107  10.748  -8.733  1.00 28.76  ? 2081 HOH F O   1 
HETATM 2637 O  O   . HOH O 7 .   ? 0.779   18.091  -8.309  1.00 18.45  ? 2082 HOH F O   1 
HETATM 2638 O  O   . HOH O 7 .   ? -9.276  11.733  -13.921 1.00 29.99  ? 2083 HOH F O   1 
HETATM 2639 O  O   . HOH O 7 .   ? 3.274   10.668  -5.309  1.00 25.20  ? 2084 HOH F O   1 
HETATM 2640 O  O   . HOH O 7 .   ? 10.062  11.729  -4.926  1.00 60.20  ? 2085 HOH F O   1 
HETATM 2641 O  O   . HOH O 7 .   ? 13.034  12.320  -4.560  1.00 40.80  ? 2086 HOH F O   1 
HETATM 2642 O  O   . HOH O 7 .   ? 11.091  12.822  -1.017  1.00 19.62  ? 2087 HOH F O   1 
HETATM 2643 O  O   . HOH O 7 .   ? 15.676  9.979   -1.836  1.00 27.52  ? 2088 HOH F O   1 
HETATM 2644 O  O   . HOH O 7 .   ? 14.482  13.099  0.472   1.00 25.38  ? 2089 HOH F O   1 
HETATM 2645 O  O   . HOH O 7 .   ? 17.324  10.458  8.244   1.00 31.13  ? 2090 HOH F O   1 
HETATM 2646 O  O   . HOH O 7 .   ? 11.076  -1.014  10.119  1.00 17.79  ? 2091 HOH F O   1 
HETATM 2647 O  O   . HOH O 7 .   ? 17.210  6.606   11.186  1.00 25.66  ? 2092 HOH F O   1 
HETATM 2648 O  O   . HOH O 7 .   ? 14.039  2.444   15.607  1.00 37.26  ? 2093 HOH F O   1 
HETATM 2649 O  O   . HOH O 7 .   ? 11.984  6.545   15.269  1.00 18.15  ? 2094 HOH F O   1 
HETATM 2650 O  O   . HOH O 7 .   ? 16.904  12.702  15.445  1.00 20.21  ? 2095 HOH F O   1 
HETATM 2651 O  O   . HOH O 7 .   ? 17.611  14.058  8.966   1.00 29.91  ? 2096 HOH F O   1 
HETATM 2652 O  O   . HOH O 7 .   ? 10.251  2.856   14.861  1.00 26.97  ? 2097 HOH F O   1 
HETATM 2653 O  O   . HOH O 7 .   ? -3.162  19.454  9.394   1.00 17.22  ? 2098 HOH F O   1 
HETATM 2654 O  O   . HOH O 7 .   ? -8.830  19.962  -0.870  1.00 25.95  ? 2099 HOH F O   1 
HETATM 2655 O  O   . HOH O 7 .   ? -9.897  21.611  8.452   1.00 34.67  ? 2100 HOH F O   1 
HETATM 2656 O  O   . HOH O 7 .   ? -7.866  23.698  8.169   1.00 31.93  ? 2101 HOH F O   1 
HETATM 2657 O  O   . HOH O 7 .   ? -5.694  23.217  -0.370  1.00 27.71  ? 2102 HOH F O   1 
HETATM 2658 O  O   . HOH O 7 .   ? -3.677  24.390  1.970   1.00 23.60  ? 2103 HOH F O   1 
HETATM 2659 O  O   . HOH O 7 .   ? 1.251   23.378  -2.328  1.00 19.53  ? 2104 HOH F O   1 
HETATM 2660 O  O   . HOH O 7 .   ? -2.069  26.968  2.482   1.00 29.20  ? 2105 HOH F O   1 
HETATM 2661 O  O   . HOH O 7 .   ? 5.301   30.407  5.187   1.00 32.63  ? 2106 HOH F O   1 
HETATM 2662 O  O   . HOH O 7 .   ? -1.429  30.556  11.273  1.00 27.86  ? 2107 HOH F O   1 
HETATM 2663 O  O   . HOH O 7 .   ? -0.214  34.090  11.277  1.00 39.77  ? 2108 HOH F O   1 
HETATM 2664 O  O   . HOH O 7 .   ? -0.895  33.457  14.121  1.00 52.48  ? 2109 HOH F O   1 
HETATM 2665 O  O   . HOH O 7 .   ? 0.405   27.592  14.070  1.00 28.15  ? 2110 HOH F O   1 
HETATM 2666 O  O   . HOH O 7 .   ? -0.593  22.659  15.040  1.00 22.64  ? 2111 HOH F O   1 
HETATM 2667 O  O   . HOH O 7 .   ? -4.440  24.118  15.054  1.00 29.48  ? 2112 HOH F O   1 
HETATM 2668 O  O   . HOH O 7 .   ? -4.066  26.530  13.974  1.00 32.65  ? 2113 HOH F O   1 
HETATM 2669 O  O   . HOH O 7 .   ? 6.590   26.892  14.196  1.00 133.28 ? 2114 HOH F O   1 
HETATM 2670 O  O   . HOH O 7 .   ? -5.170  26.113  8.446   1.00 32.08  ? 2115 HOH F O   1 
HETATM 2671 O  O   . HOH O 7 .   ? -4.999  17.797  11.697  1.00 75.18  ? 2116 HOH F O   1 
HETATM 2672 O  O   . HOH O 7 .   ? -11.389 14.405  8.251   1.00 33.37  ? 2117 HOH F O   1 
HETATM 2673 O  O   . HOH O 7 .   ? -1.666  17.777  11.230  1.00 21.45  ? 2118 HOH F O   1 
HETATM 2674 O  O   . HOH O 7 .   ? -1.031  18.286  14.274  1.00 13.77  ? 2119 HOH F O   1 
HETATM 2675 O  O   . HOH O 7 .   ? 10.120  -8.853  8.072   1.00 21.66  ? 2120 HOH F O   1 
HETATM 2676 O  O   . HOH O 7 .   ? 10.703  -11.112 6.419   1.00 30.51  ? 2121 HOH F O   1 
HETATM 2677 O  O   . HOH O 7 .   ? -8.928  17.720  16.211  1.00 31.00  ? 2122 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  ILE 99  99  99  ILE ILE A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 SER 102 102 102 SER SER A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 ILE 104 104 104 ILE ILE A . n 
A 1 105 SER 105 105 105 SER SER A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 SER 107 107 107 SER SER A . n 
A 1 108 GLY 108 108 108 GLY GLY A . n 
A 1 109 ASP 109 109 109 ASP ASP A . n 
A 1 110 HIS 110 110 110 HIS HIS A . n 
A 1 111 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 1 1   ALA 1   1   1   ALA ALA F . n 
B 1 2   THR 2   2   2   THR THR F . n 
B 1 3   LYS 3   3   3   LYS LYS F . n 
B 1 4   ALA 4   4   4   ALA ALA F . n 
B 1 5   VAL 5   5   5   VAL VAL F . n 
B 1 6   CYS 6   6   6   CYS CYS F . n 
B 1 7   VAL 7   7   7   VAL VAL F . n 
B 1 8   LEU 8   8   8   LEU LEU F . n 
B 1 9   LYS 9   9   9   LYS LYS F . n 
B 1 10  GLY 10  10  10  GLY GLY F . n 
B 1 11  ASP 11  11  11  ASP ASP F . n 
B 1 12  GLY 12  12  12  GLY GLY F . n 
B 1 13  PRO 13  13  13  PRO PRO F . n 
B 1 14  VAL 14  14  14  VAL VAL F . n 
B 1 15  GLN 15  15  15  GLN GLN F . n 
B 1 16  GLY 16  16  16  GLY GLY F . n 
B 1 17  ILE 17  17  17  ILE ILE F . n 
B 1 18  ILE 18  18  18  ILE ILE F . n 
B 1 19  ASN 19  19  19  ASN ASN F . n 
B 1 20  PHE 20  20  20  PHE PHE F . n 
B 1 21  GLU 21  21  21  GLU GLU F . n 
B 1 22  GLN 22  22  22  GLN GLN F . n 
B 1 23  LYS 23  23  23  LYS LYS F . n 
B 1 24  GLU 24  24  24  GLU GLU F . n 
B 1 25  SER 25  25  25  SER SER F . n 
B 1 26  ASN 26  26  26  ASN ASN F . n 
B 1 27  GLY 27  27  27  GLY GLY F . n 
B 1 28  PRO 28  28  28  PRO PRO F . n 
B 1 29  VAL 29  29  29  VAL VAL F . n 
B 1 30  LYS 30  30  30  LYS LYS F . n 
B 1 31  VAL 31  31  31  VAL VAL F . n 
B 1 32  TRP 32  32  32  TRP TRP F . n 
B 1 33  GLY 33  33  33  GLY GLY F . n 
B 1 34  SER 34  34  34  SER SER F . n 
B 1 35  ILE 35  35  35  ILE ILE F . n 
B 1 36  LYS 36  36  36  LYS LYS F . n 
B 1 37  GLY 37  37  37  GLY GLY F . n 
B 1 38  LEU 38  38  38  LEU LEU F . n 
B 1 39  THR 39  39  39  THR THR F . n 
B 1 40  GLU 40  40  40  GLU GLU F . n 
B 1 41  GLY 41  41  41  GLY GLY F . n 
B 1 42  LEU 42  42  42  LEU LEU F . n 
B 1 43  HIS 43  43  43  HIS HIS F . n 
B 1 44  GLY 44  44  44  GLY GLY F . n 
B 1 45  PHE 45  45  45  PHE PHE F . n 
B 1 46  HIS 46  46  46  HIS HIS F . n 
B 1 47  VAL 47  47  47  VAL VAL F . n 
B 1 48  HIS 48  48  48  HIS HIS F . n 
B 1 49  GLU 49  49  49  GLU GLU F . n 
B 1 50  PHE 50  50  50  PHE PHE F . n 
B 1 51  GLY 51  51  51  GLY GLY F . n 
B 1 52  ASP 52  52  52  ASP ASP F . n 
B 1 53  ASN 53  53  53  ASN ASN F . n 
B 1 54  THR 54  54  54  THR THR F . n 
B 1 55  ALA 55  55  55  ALA ALA F . n 
B 1 56  GLY 56  56  56  GLY GLY F . n 
B 1 57  CYS 57  57  57  CYS CYS F . n 
B 1 58  THR 58  58  58  THR THR F . n 
B 1 59  SER 59  59  59  SER SER F . n 
B 1 60  ALA 60  60  60  ALA ALA F . n 
B 1 61  GLY 61  61  61  GLY GLY F . n 
B 1 62  PRO 62  62  62  PRO PRO F . n 
B 1 63  HIS 63  63  63  HIS HIS F . n 
B 1 64  PHE 64  64  64  PHE PHE F . n 
B 1 65  ASN 65  65  65  ASN ASN F . n 
B 1 66  PRO 66  66  66  PRO PRO F . n 
B 1 67  LEU 67  67  67  LEU LEU F . n 
B 1 68  SER 68  68  68  SER SER F . n 
B 1 69  ARG 69  69  69  ARG ARG F . n 
B 1 70  LYS 70  70  70  LYS LYS F . n 
B 1 71  HIS 71  71  71  HIS HIS F . n 
B 1 72  GLY 72  72  72  GLY GLY F . n 
B 1 73  GLY 73  73  73  GLY GLY F . n 
B 1 74  PRO 74  74  74  PRO PRO F . n 
B 1 75  LYS 75  75  75  LYS LYS F . n 
B 1 76  ASP 76  76  76  ASP ASP F . n 
B 1 77  GLU 77  77  77  GLU GLU F . n 
B 1 78  GLU 78  78  78  GLU GLU F . n 
B 1 79  ARG 79  79  79  ARG ARG F . n 
B 1 80  HIS 80  80  80  HIS HIS F . n 
B 1 81  VAL 81  81  81  VAL VAL F . n 
B 1 82  GLY 82  82  82  GLY GLY F . n 
B 1 83  ASP 83  83  83  ASP ASP F . n 
B 1 84  LEU 84  84  84  LEU LEU F . n 
B 1 85  GLY 85  85  85  GLY GLY F . n 
B 1 86  ASN 86  86  86  ASN ASN F . n 
B 1 87  VAL 87  87  87  VAL VAL F . n 
B 1 88  THR 88  88  88  THR THR F . n 
B 1 89  ALA 89  89  89  ALA ALA F . n 
B 1 90  ASP 90  90  90  ASP ASP F . n 
B 1 91  LYS 91  91  91  LYS LYS F . n 
B 1 92  ASP 92  92  92  ASP ASP F . n 
B 1 93  GLY 93  93  93  GLY GLY F . n 
B 1 94  VAL 94  94  94  VAL VAL F . n 
B 1 95  ALA 95  95  95  ALA ALA F . n 
B 1 96  ASP 96  96  96  ASP ASP F . n 
B 1 97  VAL 97  97  97  VAL VAL F . n 
B 1 98  SER 98  98  98  SER SER F . n 
B 1 99  ILE 99  99  99  ILE ILE F . n 
B 1 100 GLU 100 100 100 GLU GLU F . n 
B 1 101 ASP 101 101 101 ASP ASP F . n 
B 1 102 SER 102 102 102 SER SER F . n 
B 1 103 VAL 103 103 103 VAL VAL F . n 
B 1 104 ILE 104 104 104 ILE ILE F . n 
B 1 105 SER 105 105 105 SER SER F . n 
B 1 106 LEU 106 106 106 LEU LEU F . n 
B 1 107 SER 107 107 107 SER SER F . n 
B 1 108 GLY 108 108 108 GLY GLY F . n 
B 1 109 ASP 109 109 109 ASP ASP F . n 
B 1 110 HIS 110 110 110 HIS HIS F . n 
B 1 111 CYS 111 111 111 CYS CYS F . n 
B 1 112 ILE 112 112 112 ILE ILE F . n 
B 1 113 THR 113 113 113 THR THR F . n 
B 1 114 GLY 114 114 114 GLY GLY F . n 
B 1 115 ARG 115 115 115 ARG ARG F . n 
B 1 116 THR 116 116 116 THR THR F . n 
B 1 117 LEU 117 117 117 LEU LEU F . n 
B 1 118 VAL 118 118 118 VAL VAL F . n 
B 1 119 VAL 119 119 119 VAL VAL F . n 
B 1 120 HIS 120 120 120 HIS HIS F . n 
B 1 121 GLU 121 121 121 GLU GLU F . n 
B 1 122 LYS 122 122 122 LYS LYS F . n 
B 1 123 ALA 123 123 123 ALA ALA F . n 
B 1 124 ASP 124 124 124 ASP ASP F . n 
B 1 125 ASP 125 125 125 ASP ASP F . n 
B 1 126 LEU 126 126 126 LEU LEU F . n 
B 1 127 GLY 127 127 127 GLY GLY F . n 
B 1 128 LYS 128 128 128 LYS LYS F . n 
B 1 129 GLY 129 129 129 GLY GLY F . n 
B 1 130 GLY 130 130 130 GLY GLY F . n 
B 1 131 ASN 131 131 131 ASN ASN F . n 
B 1 132 GLU 132 132 132 GLU GLU F . n 
B 1 133 GLU 133 133 133 GLU GLU F . n 
B 1 134 SER 134 134 134 SER SER F . n 
B 1 135 THR 135 135 135 THR THR F . n 
B 1 136 LYS 136 136 136 LYS LYS F . n 
B 1 137 THR 137 137 137 THR THR F . n 
B 1 138 GLY 138 138 138 GLY GLY F . n 
B 1 139 ASN 139 139 139 ASN ASN F . n 
B 1 140 ALA 140 140 140 ALA ALA F . n 
B 1 141 GLY 141 141 141 GLY GLY F . n 
B 1 142 SER 142 142 142 SER SER F . n 
B 1 143 ARG 143 143 143 ARG ARG F . n 
B 1 144 LEU 144 144 144 LEU LEU F . n 
B 1 145 ALA 145 145 145 ALA ALA F . n 
B 1 146 CYS 146 146 146 CYS CYS F . n 
B 1 147 GLY 147 147 147 GLY GLY F . n 
B 1 148 VAL 148 148 148 VAL VAL F . n 
B 1 149 ILE 149 149 149 ILE ILE F . n 
B 1 150 GLY 150 150 150 GLY GLY F . n 
B 1 151 ILE 151 151 151 ILE ILE F . n 
B 1 152 ALA 152 152 152 ALA ALA F . n 
B 1 153 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 2 ALE 1   1000 1000 ALE ALE A . 
D 2 ALE 1   1001 1001 ALE ALE A . 
E 3 SO4 1   1154 1154 SO4 SO4 A . 
F 4 CU  1   1157 1157 CU  CU  A . 
G 5 ZN  1   1158 1158 ZN  ZN  A . 
H 6 ACT 1   1159 1159 ACT ACT A . 
I 3 SO4 1   1160 1160 SO4 SO4 A . 
J 3 SO4 1   1154 1154 SO4 SO4 F . 
K 3 SO4 1   1155 1155 SO4 SO4 F . 
L 4 CU  1   1156 1156 CU  CU  F . 
M 5 ZN  1   1157 1157 ZN  ZN  F . 
N 7 HOH 1   2001 2001 HOH HOH A . 
N 7 HOH 2   2002 2002 HOH HOH A . 
N 7 HOH 3   2003 2003 HOH HOH A . 
N 7 HOH 4   2004 2004 HOH HOH A . 
N 7 HOH 5   2005 2005 HOH HOH A . 
N 7 HOH 6   2006 2006 HOH HOH A . 
N 7 HOH 7   2007 2007 HOH HOH A . 
N 7 HOH 8   2008 2008 HOH HOH A . 
N 7 HOH 9   2009 2009 HOH HOH A . 
N 7 HOH 10  2010 2010 HOH HOH A . 
N 7 HOH 11  2011 2011 HOH HOH A . 
N 7 HOH 12  2012 2012 HOH HOH A . 
N 7 HOH 13  2013 2013 HOH HOH A . 
N 7 HOH 14  2014 2014 HOH HOH A . 
N 7 HOH 15  2015 2015 HOH HOH A . 
N 7 HOH 16  2016 2016 HOH HOH A . 
N 7 HOH 17  2017 2017 HOH HOH A . 
N 7 HOH 18  2018 2018 HOH HOH A . 
N 7 HOH 19  2019 2019 HOH HOH A . 
N 7 HOH 20  2020 2020 HOH HOH A . 
N 7 HOH 21  2021 2021 HOH HOH A . 
N 7 HOH 22  2022 2022 HOH HOH A . 
N 7 HOH 23  2023 2023 HOH HOH A . 
N 7 HOH 24  2024 2024 HOH HOH A . 
N 7 HOH 25  2025 2025 HOH HOH A . 
N 7 HOH 26  2026 2026 HOH HOH A . 
N 7 HOH 27  2027 2027 HOH HOH A . 
N 7 HOH 28  2028 2028 HOH HOH A . 
N 7 HOH 29  2029 2029 HOH HOH A . 
N 7 HOH 30  2030 2030 HOH HOH A . 
N 7 HOH 31  2031 2031 HOH HOH A . 
N 7 HOH 32  2032 2032 HOH HOH A . 
N 7 HOH 33  2033 2033 HOH HOH A . 
N 7 HOH 34  2034 2034 HOH HOH A . 
N 7 HOH 35  2035 2035 HOH HOH A . 
N 7 HOH 36  2036 2036 HOH HOH A . 
N 7 HOH 37  2037 2037 HOH HOH A . 
N 7 HOH 38  2038 2038 HOH HOH A . 
N 7 HOH 39  2039 2039 HOH HOH A . 
N 7 HOH 40  2040 2040 HOH HOH A . 
N 7 HOH 41  2041 2041 HOH HOH A . 
N 7 HOH 42  2042 2042 HOH HOH A . 
N 7 HOH 43  2043 2043 HOH HOH A . 
N 7 HOH 44  2044 2044 HOH HOH A . 
N 7 HOH 45  2045 2045 HOH HOH A . 
N 7 HOH 46  2046 2046 HOH HOH A . 
N 7 HOH 47  2047 2047 HOH HOH A . 
N 7 HOH 48  2048 2048 HOH HOH A . 
N 7 HOH 49  2049 2049 HOH HOH A . 
N 7 HOH 50  2050 2050 HOH HOH A . 
N 7 HOH 51  2051 2051 HOH HOH A . 
N 7 HOH 52  2052 2052 HOH HOH A . 
N 7 HOH 53  2053 2053 HOH HOH A . 
N 7 HOH 54  2054 2054 HOH HOH A . 
N 7 HOH 55  2055 2055 HOH HOH A . 
N 7 HOH 56  2056 2056 HOH HOH A . 
N 7 HOH 57  2057 2057 HOH HOH A . 
N 7 HOH 58  2058 2058 HOH HOH A . 
N 7 HOH 59  2059 2059 HOH HOH A . 
N 7 HOH 60  2060 2060 HOH HOH A . 
N 7 HOH 61  2061 2061 HOH HOH A . 
N 7 HOH 62  2062 2062 HOH HOH A . 
N 7 HOH 63  2063 2063 HOH HOH A . 
N 7 HOH 64  2064 2064 HOH HOH A . 
N 7 HOH 65  2065 2065 HOH HOH A . 
N 7 HOH 66  2066 2066 HOH HOH A . 
N 7 HOH 67  2067 2067 HOH HOH A . 
N 7 HOH 68  2068 2068 HOH HOH A . 
N 7 HOH 69  2069 2069 HOH HOH A . 
N 7 HOH 70  2070 2070 HOH HOH A . 
N 7 HOH 71  2071 2071 HOH HOH A . 
N 7 HOH 72  2072 2072 HOH HOH A . 
N 7 HOH 73  2073 2073 HOH HOH A . 
N 7 HOH 74  2074 2074 HOH HOH A . 
N 7 HOH 75  2075 2075 HOH HOH A . 
N 7 HOH 76  2076 2076 HOH HOH A . 
N 7 HOH 77  2077 2077 HOH HOH A . 
N 7 HOH 78  2078 2078 HOH HOH A . 
N 7 HOH 79  2079 2079 HOH HOH A . 
N 7 HOH 80  2080 2080 HOH HOH A . 
N 7 HOH 81  2081 2081 HOH HOH A . 
N 7 HOH 82  2082 2082 HOH HOH A . 
N 7 HOH 83  2083 2083 HOH HOH A . 
N 7 HOH 84  2084 2084 HOH HOH A . 
N 7 HOH 85  2085 2085 HOH HOH A . 
N 7 HOH 86  2086 2086 HOH HOH A . 
N 7 HOH 87  2087 2087 HOH HOH A . 
N 7 HOH 88  2088 2088 HOH HOH A . 
N 7 HOH 89  2089 2089 HOH HOH A . 
N 7 HOH 90  2090 2090 HOH HOH A . 
N 7 HOH 91  2091 2091 HOH HOH A . 
N 7 HOH 92  2092 2092 HOH HOH A . 
N 7 HOH 93  2093 2093 HOH HOH A . 
N 7 HOH 94  2094 2094 HOH HOH A . 
N 7 HOH 95  2095 2095 HOH HOH A . 
N 7 HOH 96  2096 2096 HOH HOH A . 
N 7 HOH 97  2097 2097 HOH HOH A . 
N 7 HOH 98  2098 2098 HOH HOH A . 
N 7 HOH 99  2099 2099 HOH HOH A . 
N 7 HOH 100 2100 2100 HOH HOH A . 
N 7 HOH 101 2101 2101 HOH HOH A . 
N 7 HOH 102 2102 2102 HOH HOH A . 
N 7 HOH 103 2103 2103 HOH HOH A . 
N 7 HOH 104 2104 2104 HOH HOH A . 
N 7 HOH 105 2105 2105 HOH HOH A . 
N 7 HOH 106 2106 2106 HOH HOH A . 
N 7 HOH 107 2107 2107 HOH HOH A . 
N 7 HOH 108 2108 2108 HOH HOH A . 
N 7 HOH 109 2109 2109 HOH HOH A . 
N 7 HOH 110 2110 2110 HOH HOH A . 
N 7 HOH 111 2111 2111 HOH HOH A . 
N 7 HOH 112 2112 2112 HOH HOH A . 
N 7 HOH 113 2113 2113 HOH HOH A . 
N 7 HOH 114 2114 2114 HOH HOH A . 
N 7 HOH 115 2115 2115 HOH HOH A . 
N 7 HOH 116 2116 2116 HOH HOH A . 
N 7 HOH 117 2117 2117 HOH HOH A . 
N 7 HOH 118 2118 2118 HOH HOH A . 
N 7 HOH 119 2119 2119 HOH HOH A . 
N 7 HOH 120 2120 2120 HOH HOH A . 
N 7 HOH 121 2121 2121 HOH HOH A . 
N 7 HOH 122 2122 2122 HOH HOH A . 
N 7 HOH 123 2123 2123 HOH HOH A . 
N 7 HOH 124 2124 2124 HOH HOH A . 
N 7 HOH 125 2125 2125 HOH HOH A . 
N 7 HOH 126 2126 2126 HOH HOH A . 
N 7 HOH 127 2127 2127 HOH HOH A . 
N 7 HOH 128 2128 2128 HOH HOH A . 
N 7 HOH 129 2129 2129 HOH HOH A . 
N 7 HOH 130 2130 2130 HOH HOH A . 
N 7 HOH 131 2131 2131 HOH HOH A . 
N 7 HOH 132 2132 2132 HOH HOH A . 
N 7 HOH 133 2133 2133 HOH HOH A . 
N 7 HOH 134 2134 2134 HOH HOH A . 
N 7 HOH 135 2135 2135 HOH HOH A . 
N 7 HOH 136 2136 2136 HOH HOH A . 
N 7 HOH 137 2137 2137 HOH HOH A . 
N 7 HOH 138 2138 2138 HOH HOH A . 
N 7 HOH 139 2139 2139 HOH HOH A . 
N 7 HOH 140 2140 2140 HOH HOH A . 
N 7 HOH 141 2141 2141 HOH HOH A . 
N 7 HOH 142 2142 2142 HOH HOH A . 
N 7 HOH 143 2143 2143 HOH HOH A . 
N 7 HOH 144 2144 2144 HOH HOH A . 
N 7 HOH 145 2145 2145 HOH HOH A . 
N 7 HOH 146 2146 2146 HOH HOH A . 
N 7 HOH 147 2147 2147 HOH HOH A . 
N 7 HOH 148 2148 2148 HOH HOH A . 
N 7 HOH 149 2149 2149 HOH HOH A . 
N 7 HOH 150 2150 2150 HOH HOH A . 
N 7 HOH 151 2151 2151 HOH HOH A . 
N 7 HOH 152 2152 2152 HOH HOH A . 
N 7 HOH 153 2153 2153 HOH HOH A . 
N 7 HOH 154 2154 2154 HOH HOH A . 
N 7 HOH 155 2155 2155 HOH HOH A . 
N 7 HOH 156 2156 2156 HOH HOH A . 
N 7 HOH 157 2157 2157 HOH HOH A . 
N 7 HOH 158 2158 2158 HOH HOH A . 
N 7 HOH 159 2159 2159 HOH HOH A . 
N 7 HOH 160 2160 2160 HOH HOH A . 
N 7 HOH 161 2161 2161 HOH HOH A . 
O 7 HOH 1   2001 2001 HOH HOH F . 
O 7 HOH 2   2002 2002 HOH HOH F . 
O 7 HOH 3   2003 2003 HOH HOH F . 
O 7 HOH 4   2004 2004 HOH HOH F . 
O 7 HOH 5   2005 2005 HOH HOH F . 
O 7 HOH 6   2006 2006 HOH HOH F . 
O 7 HOH 7   2007 2007 HOH HOH F . 
O 7 HOH 8   2008 2008 HOH HOH F . 
O 7 HOH 9   2009 2009 HOH HOH F . 
O 7 HOH 10  2010 2010 HOH HOH F . 
O 7 HOH 11  2011 2011 HOH HOH F . 
O 7 HOH 12  2012 2012 HOH HOH F . 
O 7 HOH 13  2013 2013 HOH HOH F . 
O 7 HOH 14  2014 2014 HOH HOH F . 
O 7 HOH 15  2015 2015 HOH HOH F . 
O 7 HOH 16  2016 2016 HOH HOH F . 
O 7 HOH 17  2017 2017 HOH HOH F . 
O 7 HOH 18  2018 2018 HOH HOH F . 
O 7 HOH 19  2019 2019 HOH HOH F . 
O 7 HOH 20  2020 2020 HOH HOH F . 
O 7 HOH 21  2021 2021 HOH HOH F . 
O 7 HOH 22  2022 2022 HOH HOH F . 
O 7 HOH 23  2023 2023 HOH HOH F . 
O 7 HOH 24  2024 2024 HOH HOH F . 
O 7 HOH 25  2025 2025 HOH HOH F . 
O 7 HOH 26  2026 2026 HOH HOH F . 
O 7 HOH 27  2027 2027 HOH HOH F . 
O 7 HOH 28  2028 2028 HOH HOH F . 
O 7 HOH 29  2029 2029 HOH HOH F . 
O 7 HOH 30  2030 2030 HOH HOH F . 
O 7 HOH 31  2031 2031 HOH HOH F . 
O 7 HOH 32  2032 2032 HOH HOH F . 
O 7 HOH 33  2033 2033 HOH HOH F . 
O 7 HOH 34  2034 2034 HOH HOH F . 
O 7 HOH 35  2035 2035 HOH HOH F . 
O 7 HOH 36  2036 2036 HOH HOH F . 
O 7 HOH 37  2037 2037 HOH HOH F . 
O 7 HOH 38  2038 2038 HOH HOH F . 
O 7 HOH 39  2039 2039 HOH HOH F . 
O 7 HOH 40  2040 2040 HOH HOH F . 
O 7 HOH 41  2041 2041 HOH HOH F . 
O 7 HOH 42  2042 2042 HOH HOH F . 
O 7 HOH 43  2043 2043 HOH HOH F . 
O 7 HOH 44  2044 2044 HOH HOH F . 
O 7 HOH 45  2045 2045 HOH HOH F . 
O 7 HOH 46  2046 2046 HOH HOH F . 
O 7 HOH 47  2047 2047 HOH HOH F . 
O 7 HOH 48  2048 2048 HOH HOH F . 
O 7 HOH 49  2049 2049 HOH HOH F . 
O 7 HOH 50  2050 2050 HOH HOH F . 
O 7 HOH 51  2051 2051 HOH HOH F . 
O 7 HOH 52  2052 2052 HOH HOH F . 
O 7 HOH 53  2053 2053 HOH HOH F . 
O 7 HOH 54  2054 2054 HOH HOH F . 
O 7 HOH 55  2055 2055 HOH HOH F . 
O 7 HOH 56  2056 2056 HOH HOH F . 
O 7 HOH 57  2057 2057 HOH HOH F . 
O 7 HOH 58  2058 2058 HOH HOH F . 
O 7 HOH 59  2059 2059 HOH HOH F . 
O 7 HOH 60  2060 2060 HOH HOH F . 
O 7 HOH 61  2061 2061 HOH HOH F . 
O 7 HOH 62  2062 2062 HOH HOH F . 
O 7 HOH 63  2063 2063 HOH HOH F . 
O 7 HOH 64  2064 2064 HOH HOH F . 
O 7 HOH 65  2065 2065 HOH HOH F . 
O 7 HOH 66  2066 2066 HOH HOH F . 
O 7 HOH 67  2067 2067 HOH HOH F . 
O 7 HOH 68  2068 2068 HOH HOH F . 
O 7 HOH 69  2069 2069 HOH HOH F . 
O 7 HOH 70  2070 2070 HOH HOH F . 
O 7 HOH 71  2071 2071 HOH HOH F . 
O 7 HOH 72  2072 2072 HOH HOH F . 
O 7 HOH 73  2073 2073 HOH HOH F . 
O 7 HOH 74  2074 2074 HOH HOH F . 
O 7 HOH 75  2075 2075 HOH HOH F . 
O 7 HOH 76  2076 2076 HOH HOH F . 
O 7 HOH 77  2077 2077 HOH HOH F . 
O 7 HOH 78  2078 2078 HOH HOH F . 
O 7 HOH 79  2079 2079 HOH HOH F . 
O 7 HOH 80  2080 2080 HOH HOH F . 
O 7 HOH 81  2081 2081 HOH HOH F . 
O 7 HOH 82  2082 2082 HOH HOH F . 
O 7 HOH 83  2083 2083 HOH HOH F . 
O 7 HOH 84  2084 2084 HOH HOH F . 
O 7 HOH 85  2085 2085 HOH HOH F . 
O 7 HOH 86  2086 2086 HOH HOH F . 
O 7 HOH 87  2087 2087 HOH HOH F . 
O 7 HOH 88  2088 2088 HOH HOH F . 
O 7 HOH 89  2089 2089 HOH HOH F . 
O 7 HOH 90  2090 2090 HOH HOH F . 
O 7 HOH 91  2091 2091 HOH HOH F . 
O 7 HOH 92  2092 2092 HOH HOH F . 
O 7 HOH 93  2093 2093 HOH HOH F . 
O 7 HOH 94  2094 2094 HOH HOH F . 
O 7 HOH 95  2095 2095 HOH HOH F . 
O 7 HOH 96  2096 2096 HOH HOH F . 
O 7 HOH 97  2097 2097 HOH HOH F . 
O 7 HOH 98  2098 2098 HOH HOH F . 
O 7 HOH 99  2099 2099 HOH HOH F . 
O 7 HOH 100 2100 2100 HOH HOH F . 
O 7 HOH 101 2101 2101 HOH HOH F . 
O 7 HOH 102 2102 2102 HOH HOH F . 
O 7 HOH 103 2103 2103 HOH HOH F . 
O 7 HOH 104 2104 2104 HOH HOH F . 
O 7 HOH 105 2105 2105 HOH HOH F . 
O 7 HOH 106 2106 2106 HOH HOH F . 
O 7 HOH 107 2107 2107 HOH HOH F . 
O 7 HOH 108 2108 2108 HOH HOH F . 
O 7 HOH 109 2109 2109 HOH HOH F . 
O 7 HOH 110 2110 2110 HOH HOH F . 
O 7 HOH 111 2111 2111 HOH HOH F . 
O 7 HOH 112 2112 2112 HOH HOH F . 
O 7 HOH 113 2113 2113 HOH HOH F . 
O 7 HOH 114 2114 2114 HOH HOH F . 
O 7 HOH 115 2115 2115 HOH HOH F . 
O 7 HOH 116 2116 2116 HOH HOH F . 
O 7 HOH 117 2117 2117 HOH HOH F . 
O 7 HOH 118 2118 2118 HOH HOH F . 
O 7 HOH 119 2119 2119 HOH HOH F . 
O 7 HOH 120 2120 2120 HOH HOH F . 
O 7 HOH 121 2121 2121 HOH HOH F . 
O 7 HOH 122 2122 2122 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 
# 
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)' 2180  ? 
1 MORE         -65.8 ? 
1 'SSA (A^2)'  14010 ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  ND1 ? A HIS 46 ? A HIS 46 ? 1_555 CU ? F CU . ? A CU 1157 ? 1_555 NE2 ? A HIS 48  ? A HIS 48  ? 1_555 150.1 ? 
2  ND1 ? A HIS 46 ? A HIS 46 ? 1_555 CU ? F CU . ? A CU 1157 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 102.3 ? 
3  NE2 ? A HIS 48 ? A HIS 48 ? 1_555 CU ? F CU . ? A CU 1157 ? 1_555 NE2 ? A HIS 120 ? A HIS 120 ? 1_555 107.5 ? 
4  OD1 ? A ASP 83 ? A ASP 83 ? 1_555 ZN ? G ZN . ? A ZN 1158 ? 1_555 ND1 ? A HIS 80  ? A HIS 80  ? 1_555 114.4 ? 
5  OD1 ? A ASP 83 ? A ASP 83 ? 1_555 ZN ? G ZN . ? A ZN 1158 ? 1_555 ND1 ? A HIS 63  ? A HIS 63  ? 1_555 103.9 ? 
6  ND1 ? A HIS 80 ? A HIS 80 ? 1_555 ZN ? G ZN . ? A ZN 1158 ? 1_555 ND1 ? A HIS 63  ? A HIS 63  ? 1_555 111.1 ? 
7  OD1 ? A ASP 83 ? A ASP 83 ? 1_555 ZN ? G ZN . ? A ZN 1158 ? 1_555 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 100.0 ? 
8  ND1 ? A HIS 80 ? A HIS 80 ? 1_555 ZN ? G ZN . ? A ZN 1158 ? 1_555 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 121.2 ? 
9  ND1 ? A HIS 63 ? A HIS 63 ? 1_555 ZN ? G ZN . ? A ZN 1158 ? 1_555 ND1 ? A HIS 71  ? A HIS 71  ? 1_555 104.3 ? 
10 ND1 ? B HIS 46 ? F HIS 46 ? 1_555 CU ? L CU . ? F CU 1156 ? 1_555 NE2 ? B HIS 48  ? F HIS 48  ? 1_555 151.2 ? 
11 ND1 ? B HIS 46 ? F HIS 46 ? 1_555 CU ? L CU . ? F CU 1156 ? 1_555 NE2 ? B HIS 120 ? F HIS 120 ? 1_555 102.0 ? 
12 NE2 ? B HIS 48 ? F HIS 48 ? 1_555 CU ? L CU . ? F CU 1156 ? 1_555 NE2 ? B HIS 120 ? F HIS 120 ? 1_555 106.6 ? 
13 OD1 ? B ASP 83 ? F ASP 83 ? 1_555 ZN ? M ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 80  ? F HIS 80  ? 1_555 113.9 ? 
14 OD1 ? B ASP 83 ? F ASP 83 ? 1_555 ZN ? M ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 71  ? F HIS 71  ? 1_555 99.8  ? 
15 ND1 ? B HIS 80 ? F HIS 80 ? 1_555 ZN ? M ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 71  ? F HIS 71  ? 1_555 121.6 ? 
16 OD1 ? B ASP 83 ? F ASP 83 ? 1_555 ZN ? M ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 63  ? F HIS 63  ? 1_555 104.2 ? 
17 ND1 ? B HIS 80 ? F HIS 80 ? 1_555 ZN ? M ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 63  ? F HIS 63  ? 1_555 110.8 ? 
18 ND1 ? B HIS 71 ? F HIS 71 ? 1_555 ZN ? M ZN . ? F ZN 1157 ? 1_555 ND1 ? B HIS 63  ? F HIS 63  ? 1_555 104.7 ? 
# 
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 2012-11-28 
2 'Structure model' 1 1 2013-04-24 
3 'Structure model' 1 2 2013-05-08 
# 
_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' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
REFMAC refinement       5.6.0117 ? 1 
XDS    'data reduction' .        ? 2 
XDS    'data scaling'   .        ? 3 
REFMAC phasing          .        ? 4 
# 
_pdbx_entry_details.entry_id             4A7U 
_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 OE2 A GLU 40   ? ? O   A HOH 2065 ? ? 1.82 
2 1 CD1 A ILE 17   ? A O   F HOH 2049 ? ? 1.89 
3 1 OD1 F ASP 90   ? B OD1 F ASP 92   ? ? 1.92 
4 1 O   A HOH 2068 ? ? O   A HOH 2144 ? ? 2.05 
5 1 O   F HOH 2057 ? ? O   F HOH 2119 ? ? 2.08 
6 1 O   F HOH 2038 ? ? O   F HOH 2099 ? ? 2.09 
7 1 O   A HOH 2064 ? ? O   A HOH 2065 ? ? 2.10 
8 1 O   A HOH 2090 ? ? O   A HOH 2092 ? ? 2.13 
9 1 ND2 F ASN 53   ? A O   F HOH 2047 ? ? 2.16 
# 
_pdbx_validate_symm_contact.id                1 
_pdbx_validate_symm_contact.PDB_model_num     1 
_pdbx_validate_symm_contact.auth_atom_id_1    OD2 
_pdbx_validate_symm_contact.auth_asym_id_1    A 
_pdbx_validate_symm_contact.auth_comp_id_1    ASP 
_pdbx_validate_symm_contact.auth_seq_id_1     96 
_pdbx_validate_symm_contact.PDB_ins_code_1    ? 
_pdbx_validate_symm_contact.label_alt_id_1    ? 
_pdbx_validate_symm_contact.site_symmetry_1   1_555 
_pdbx_validate_symm_contact.auth_atom_id_2    O 
_pdbx_validate_symm_contact.auth_asym_id_2    F 
_pdbx_validate_symm_contact.auth_comp_id_2    HOH 
_pdbx_validate_symm_contact.auth_seq_id_2     2110 
_pdbx_validate_symm_contact.PDB_ins_code_2    ? 
_pdbx_validate_symm_contact.label_alt_id_2    ? 
_pdbx_validate_symm_contact.site_symmetry_2   2_546 
_pdbx_validate_symm_contact.dist              2.13 
# 
_pdbx_validate_rmsd_bond.id                        1 
_pdbx_validate_rmsd_bond.PDB_model_num             1 
_pdbx_validate_rmsd_bond.auth_atom_id_1            CD 
_pdbx_validate_rmsd_bond.auth_asym_id_1            F 
_pdbx_validate_rmsd_bond.auth_comp_id_1            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_1             49 
_pdbx_validate_rmsd_bond.PDB_ins_code_1            ? 
_pdbx_validate_rmsd_bond.label_alt_id_1            B 
_pdbx_validate_rmsd_bond.auth_atom_id_2            OE1 
_pdbx_validate_rmsd_bond.auth_asym_id_2            F 
_pdbx_validate_rmsd_bond.auth_comp_id_2            GLU 
_pdbx_validate_rmsd_bond.auth_seq_id_2             49 
_pdbx_validate_rmsd_bond.PDB_ins_code_2            ? 
_pdbx_validate_rmsd_bond.label_alt_id_2            B 
_pdbx_validate_rmsd_bond.bond_value                1.355 
_pdbx_validate_rmsd_bond.bond_target_value         1.252 
_pdbx_validate_rmsd_bond.bond_deviation            0.103 
_pdbx_validate_rmsd_bond.bond_standard_deviation   0.011 
_pdbx_validate_rmsd_bond.linker_flag               N 
# 
_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                126.63 
_pdbx_validate_rmsd_angle.angle_target_value         118.30 
_pdbx_validate_rmsd_angle.angle_deviation            8.33 
_pdbx_validate_rmsd_angle.angle_standard_deviation   0.90 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP F 11 ? B -87.05  49.23 
2 1 PRO F 13 ? B -105.02 49.67 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   LYS 
_pdbx_validate_peptide_omega.auth_asym_id_1   F 
_pdbx_validate_peptide_omega.auth_seq_id_1    9 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   GLY 
_pdbx_validate_peptide_omega.auth_asym_id_2   F 
_pdbx_validate_peptide_omega.auth_seq_id_2    10 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   A 
_pdbx_validate_peptide_omega.omega            -126.46 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 L-EPINEPHRINE     ALE 
3 'SULFATE ION'     SO4 
4 'COPPER (II) ION' CU  
5 'ZINC ION'        ZN  
6 'ACETATE ION'     ACT 
7 water             HOH 
# 
