data_4BCZ
# 
_entry.id   4BCZ 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.308 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
PDB   4BCZ         
PDBE  EBI-54310    
WWPDB D_1290054310 
# 
loop_
_pdbx_database_related.db_name 
_pdbx_database_related.db_id 
_pdbx_database_related.content_type 
_pdbx_database_related.details 
PDB 1AZV unspecified 'FAMILIAL ALS MUTANT G37R CUZNSOD (HUMAN)' 
PDB 1BA9 unspecified 'THE SOLUTION STRUCTURE OF REDUCED MONOMERIC SUPEROXIDE DISMUTASE, NMR, 36 STRUCTURES' 
PDB 1DSW unspecified 
;THE SOLUTION STRUCTURE OF A MONOMERIC, REDUCED FORM OFHUMAN COPPER, ZINC SUPEROXIDE DISMUTASE BEARING THE SAMECHARGE AS THE NATIVE PROTEIN
;
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 1HL4 unspecified 'THE STRUCTURE OF APO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
PDB 1HL5 unspecified 'THE STRUCTURE OF HOLO TYPE HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
PDB 1KMG unspecified 'THE SOLUTION STRUCTURE OF MONOMERIC COPPER-FREE SUPEROXIDEDISMUTASE' 
PDB 1L3N unspecified 'THE SOLUTION STRUCTURE OF REDUCED DIMERIC COPPER ZINC SOD:THE STRUCTURAL EFFECTS OF DIMERIZATION' 
PDB 1MFM unspecified 'MONOMERIC HUMAN SOD MUTANT F50E/G51E/E133Q AT ATOMIC RESOLUTION' 
PDB 1N18 unspecified 'THERMOSTABLE MUTANT OF HUMAN SUPEROXIDE DISMUTASE, C6A, C111S' 
PDB 1N19 unspecified 'STRUCTURE OF THE HSOD A4V MUTANT' 
PDB 1OEZ unspecified 'ZN HIS46ARG MUTANT OF HUMAN CU, ZN SUPEROXIDE DISMUTASE' 
PDB 1OZT unspecified 
'CRYSTAL STRUCTURE OF APO-H46R FAMILIAL ALS MUTANT HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) TO 2.5A RESOLUTION' 
PDB 1OZU unspecified 
'CRYSTAL STRUCTURE OF FAMILIAL ALS MUTANT S134N OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) TO 1.3A RESOLUTION' 
PDB 1P1V unspecified 'CRYSTAL STRUCTURE OF FALS-ASSOCIATED HUMAN COPPER- ZINCSUPEROXIDE DISMUTASE (CUZNSOD) MUTANT D125H TO 1.4A' 
PDB 1PTZ unspecified 
'CRYSTAL STRUCTURE OF THE HUMAN CU, ZN SUPEROXIDE DISMUTASE,FAMILIAL AMYOTROPHIC LATERAL SCLEROSIS (FALS) MUTANT H43R' 
PDB 1PU0 unspecified 'STRUCTURE OF HUMAN CU,ZN SUPEROXIDE DISMUTASE' 
PDB 1RK7 unspecified 'SOLUTION STRUCTURE OF APO CU,ZN SUPEROXIDE DISMUTASE: ROLEOF METAL IONS IN PROTEIN FOLDING' 
PDB 1SOS unspecified 'SUPEROXIDE DISMUTASE MUTANT WITH CYS 6 REPLACED BY ALA AND CYS 111 REPLACED BY SER (C6A, C111S)' 
PDB 1SPD unspecified 'SUPEROXIDE DISMUTASE' 
PDB 1UXL unspecified 'I113T MUTANT OF HUMAN SOD1' 
PDB 1UXM unspecified 'A4V MUTANT OF HUMAN SOD1' 
PDB 2AF2 unspecified 'SOLUTION STRUCTURE OF DISULFIDE REDUCED AND COPPER DEPLETEDHUMAN SUPEROXIDE DISMUTASE' 
PDB 2C9S unspecified '1.24 ANGSTROMS RESOLUTION STRUCTURE OF ZN-ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 2C9U unspecified '1.24 ANGSTROMS RESOLUTION STRUCTURE OF AS-ISOLATED CU -ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 2C9V unspecified 'ATOMIC RESOLUTION STRUCTURE OF CU-ZN HUMAN SUPEROXIDE DISMUTASE' 
PDB 2V0A unspecified 'ATOMIC RESOLUTION CRYSTAL STRUCTURE OF HUMAN SUPEROXIDE DISMUTASE' 
PDB 2VR6 unspecified 'CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.3 A RESOLUTION' 
PDB 2VR7 unspecified 'CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.58 A RESOLUTION' 
PDB 2VR8 unspecified 'CRYSTAL STRUCTURE OF G85R ALS MUTANT OF HUMAN CU,ZN SUPEROXIDE DISMUTASE (CUZNSOD) AT 1.36 A RESOLUTION' 
PDB 2WKO unspecified 'STRUCTURE OF METAL LOADED PATHOGENIC SOD1 MUTANT G93A.' 
PDB 2WYT unspecified '1.0 A RESOLUTION STRUCTURE OF L38V SOD1 MUTANT' 
PDB 2WYZ unspecified 'L38V SOD1 MUTANT COMPLEXED WITH UMP' 
PDB 2WZ0 unspecified 'L38V SOD1 MUTANT COMPLEXED WITH ANILINE.' 
PDB 2WZ5 unspecified 'L38V SOD1 MUTANT COMPLEXED WITH L-METHIONINE.' 
PDB 2WZ6 unspecified 'G93A SOD1 MUTANT COMPLEXED WITH QUINAZOLINE.' 
PDB 2XJK unspecified 'MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE' 
PDB 2XJL unspecified 'MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE WITHOUT CU LIGANDS' 
PDB 4A7G unspecified 
'STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH 4 -METHYLPIPERAZIN-1-YL)QUINAZOLINE IN THE P21 SPACE GROUP.' 
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 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 4A7T unspecified 'STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH ISOPROTERANOL IN THE P21 SPACE GROUP' 
PDB 4A7U unspecified 'STRUCTURE OF HUMAN I113T SOD1 COMPLEXED WITH ADRENALINE IN THE P21 SPACE GROUP.' 
PDB 4A7V unspecified 'STRUCTURE OF HUMAN I113T SOD1 MUTANT COMPLEXED WITH DOPAMINE IN THE P21 SPACE GROUP' 
PDB 4B3E unspecified 'STRUCTURE OF COPPER-ZINC SUPEROXIDE DISMUTASE COMPLEXED WITH BICARBONATE.' 
PDB 4BCY unspecified 'MONOMERIC HUMAN CU,ZN SUPEROXIDE DISMUTASE, MUTATION H43F' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.entry_id                        4BCZ 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.SG_entry                        . 
_pdbx_database_status.recvd_initial_deposition_date   2012-10-03 
_pdbx_database_status.pdb_format_compatible           Y 
_pdbx_database_status.status_code_sf                  ? 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.methods_development_category    ? 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
'Saraboji, K.'   1 
'Awad, W.'       2 
'Danielsson, J.' 3 
'Lang, L.'       4 
'Kurnik, M.'     5 
'Marklund, S.L.' 6 
'Oliveberg, M.'  7 
'Logan, D.T.'    8 
# 
_citation.id                        primary 
_citation.title                     'Global Structural Motions from the Strain of a Single Hydrogen Bond.' 
_citation.journal_abbrev            Proc.Natl.Acad.Sci.USA 
_citation.journal_volume            110 
_citation.page_first                3829 
_citation.page_last                 ? 
_citation.year                      2013 
_citation.journal_id_ASTM           PNASA6 
_citation.country                   US 
_citation.journal_id_ISSN           0027-8424 
_citation.journal_id_CSD            0040 
_citation.book_publisher            ? 
_citation.pdbx_database_id_PubMed   23431167 
_citation.pdbx_database_id_DOI      10.1073/PNAS.1217306110 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Danielsson, J.'  1 ? 
primary 'Awad, W.'        2 ? 
primary 'Saraboji, K.'    3 ? 
primary 'Kurnik, M.'      4 ? 
primary 'Lang, L.'        5 ? 
primary 'Leinartaite, L.' 6 ? 
primary 'Marklund, S.L.'  7 ? 
primary 'Logan, D.T.'     8 ? 
primary 'Oliveberg, M.'   9 ? 
# 
_cell.entry_id           4BCZ 
_cell.length_a           74.430 
_cell.length_b           74.430 
_cell.length_c           59.270 
_cell.angle_alpha        90.00 
_cell.angle_beta         90.00 
_cell.angle_gamma        120.00 
_cell.Z_PDB              12 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         4BCZ 
_symmetry.space_group_name_H-M             'P 65' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                170 
# 
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]' 10990.290 2   1.15.1.1 YES 'RESIDUES 2049,83-124,141-154' ? 
2 water   nat water                          18.015    147 ?        ?   ?                              ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '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       
;ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHGAGGDLGNVTADKDGVADVSIEDSVISLSGDH
SIIGRTLVVHEKAGAGAGSRLASGVIGIAQ
;
_entity_poly.pdbx_seq_one_letter_code_can   
;ATKAVAVLKGDGPVQGIINFEQKESNGPVKVWGSIKGLTEGLHGFHVHGAGGDLGNVTADKDGVADVSIEDSVISLSGDH
SIIGRTLVVHEKAGAGAGSRLASGVIGIAQ
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   ALA n 
1 2   THR n 
1 3   LYS n 
1 4   ALA n 
1 5   VAL n 
1 6   ALA n 
1 7   VAL n 
1 8   LEU n 
1 9   LYS n 
1 10  GLY n 
1 11  ASP n 
1 12  GLY n 
1 13  PRO n 
1 14  VAL n 
1 15  GLN n 
1 16  GLY n 
1 17  ILE n 
1 18  ILE n 
1 19  ASN n 
1 20  PHE n 
1 21  GLU n 
1 22  GLN n 
1 23  LYS n 
1 24  GLU n 
1 25  SER n 
1 26  ASN n 
1 27  GLY n 
1 28  PRO n 
1 29  VAL n 
1 30  LYS n 
1 31  VAL n 
1 32  TRP n 
1 33  GLY n 
1 34  SER n 
1 35  ILE n 
1 36  LYS n 
1 37  GLY n 
1 38  LEU n 
1 39  THR n 
1 40  GLU n 
1 41  GLY n 
1 42  LEU n 
1 43  HIS n 
1 44  GLY n 
1 45  PHE n 
1 46  HIS n 
1 47  VAL n 
1 48  HIS n 
1 49  GLY n 
1 50  ALA n 
1 51  GLY n 
1 52  GLY n 
1 53  ASP n 
1 54  LEU n 
1 55  GLY n 
1 56  ASN n 
1 57  VAL n 
1 58  THR n 
1 59  ALA n 
1 60  ASP n 
1 61  LYS n 
1 62  ASP n 
1 63  GLY n 
1 64  VAL n 
1 65  ALA n 
1 66  ASP n 
1 67  VAL n 
1 68  SER n 
1 69  ILE n 
1 70  GLU n 
1 71  ASP n 
1 72  SER n 
1 73  VAL n 
1 74  ILE n 
1 75  SER n 
1 76  LEU n 
1 77  SER n 
1 78  GLY n 
1 79  ASP n 
1 80  HIS n 
1 81  SER n 
1 82  ILE n 
1 83  ILE n 
1 84  GLY n 
1 85  ARG n 
1 86  THR n 
1 87  LEU n 
1 88  VAL n 
1 89  VAL n 
1 90  HIS n 
1 91  GLU n 
1 92  LYS n 
1 93  ALA n 
1 94  GLY n 
1 95  ALA n 
1 96  GLY n 
1 97  ALA n 
1 98  GLY n 
1 99  SER n 
1 100 ARG n 
1 101 LEU n 
1 102 ALA n 
1 103 SER n 
1 104 GLY n 
1 105 VAL n 
1 106 ILE n 
1 107 GLY n 
1 108 ILE n 
1 109 ALA n 
1 110 GLN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               HUMAN 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'HOMO SAPIENS' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'ESCHERICHIA COLI' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               'BL21(DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    SODC_HUMAN 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   ? 
_struct_ref.pdbx_align_begin           ? 
_struct_ref.pdbx_db_accession          P00441 
_struct_ref.pdbx_db_isoform            ? 
# 
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 4BCZ A 1  ? 48  ? P00441 2   ? 49  ? 1  48  
2 1 4BCZ A 52 ? 93  ? P00441 83  ? 124 ? 52 93  
3 1 4BCZ A 97 ? 110 ? P00441 141 ? 154 ? 97 110 
4 1 4BCZ B 1  ? 48  ? P00441 2   ? 49  ? 1  48  
5 1 4BCZ B 52 ? 93  ? P00441 83  ? 124 ? 52 93  
6 1 4BCZ B 97 ? 110 ? P00441 141 ? 154 ? 97 110 
# 
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 4BCZ ALA A 6   ? UNP P00441 CYS 7   'engineered mutation' 6   1  
1 4BCZ GLY A 49  ? PDB ?      ?   ?   linker                49  2  
1 4BCZ ALA A 50  ? PDB ?      ?   ?   linker                50  3  
1 4BCZ GLY A 51  ? PDB ?      ?   ?   linker                51  4  
1 4BCZ SER A 81  ? UNP P00441 CYS 112 'engineered mutation' 81  5  
1 4BCZ GLY A 94  ? PDB ?      ?   ?   linker                94  6  
1 4BCZ ALA A 95  ? PDB ?      ?   ?   linker                95  7  
1 4BCZ GLY A 96  ? PDB ?      ?   ?   linker                96  8  
1 4BCZ SER A 103 ? UNP P00441 CYS 147 'engineered mutation' 103 9  
4 4BCZ ALA B 6   ? UNP P00441 CYS 7   'engineered mutation' 6   10 
4 4BCZ GLY B 49  ? PDB ?      ?   ?   linker                49  11 
4 4BCZ ALA B 50  ? PDB ?      ?   ?   linker                50  12 
4 4BCZ GLY B 51  ? PDB ?      ?   ?   linker                51  13 
4 4BCZ SER B 81  ? UNP P00441 CYS 112 'engineered mutation' 81  14 
4 4BCZ GLY B 94  ? PDB ?      ?   ?   linker                94  15 
4 4BCZ ALA B 95  ? PDB ?      ?   ?   linker                95  16 
4 4BCZ GLY B 96  ? PDB ?      ?   ?   linker                96  17 
4 4BCZ SER B 103 ? UNP P00441 CYS 147 'engineered mutation' 103 18 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
HIS 'L-peptide linking' y HISTIDINE       ? 'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ? 'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ? 'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ? 'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ? 'C6 H15 N2 O2 1' 147.195 
PHE 'L-peptide linking' y PHENYLALANINE   ? 'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ? 'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ? 'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
_exptl.entry_id          4BCZ 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_meas          ? 
_exptl_crystal.density_Matthews      2.17 
_exptl_crystal.density_percent_sol   43.4 
_exptl_crystal.description           NONE 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          ? 
_exptl_crystal_grow.temp            293 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.pdbx_details    '30% PEG 1500, 0.1M MIB BUFFER, PH 4.0, 20 C' 
# 
_diffrn.id                     1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
_diffrn.crystal_id             1 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               CCD 
_diffrn_detector.type                   'MARRESEARCH 165MM' 
_diffrn_detector.pdbx_collection_date   2011-03-15 
_diffrn_detector.details                'HORIZONTALLY FOCUSING MIRROR' 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    'BENT SI(111) CRYSTAL' 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0379 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'MAX II BEAMLINE I911-2' 
_diffrn_source.pdbx_synchrotron_site       'MAX II' 
_diffrn_source.pdbx_synchrotron_beamline   I911-2 
_diffrn_source.pdbx_wavelength             1.0379 
_diffrn_source.pdbx_wavelength_list        ? 
# 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.entry_id                     4BCZ 
_reflns.observed_criterion_sigma_I   0.0 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             30.00 
_reflns.d_resolution_high            1.93 
_reflns.number_obs                   14115 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.8 
_reflns.pdbx_Rmerge_I_obs            0.06 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        21.40 
_reflns.B_iso_Wilson_estimate        28.83 
_reflns.pdbx_redundancy              6.7 
# 
_reflns_shell.pdbx_diffrn_id         1 
_reflns_shell.pdbx_ordinal           1 
_reflns_shell.d_res_high             1.93 
_reflns_shell.d_res_low              1.98 
_reflns_shell.percent_possible_all   99.9 
_reflns_shell.Rmerge_I_obs           0.65 
_reflns_shell.pdbx_Rsym_value        ? 
_reflns_shell.meanI_over_sigI_obs    3.50 
_reflns_shell.pdbx_redundancy        6.7 
# 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.entry_id                                 4BCZ 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.ls_number_reflns_obs                     14115 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          0.0 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_d_res_low                             30.0 
_refine.ls_d_res_high                            1.93 
_refine.ls_percent_reflns_obs                    99.8 
_refine.ls_R_factor_obs                          0.1718 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_R_work                       0.1693 
_refine.ls_R_factor_R_free                       0.2195 
_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                  707 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.occupancy_min                            ? 
_refine.occupancy_max                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.B_iso_mean                               36.60 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_ksol                 0.0 
_refine.solvent_model_param_bsol                 0.0 
_refine.pdbx_solvent_vdw_probe_radii             1.11 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_ls_cross_valid_method               ? 
_refine.details                                  ? 
_refine.pdbx_starting_model                      'PDB ENTRY 2XJK' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.20 
_refine.pdbx_overall_phase_error                 23.59 
_refine.overall_SU_B                             ? 
_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        1543 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.number_atoms_solvent             147 
_refine_hist.number_atoms_total               1690 
_refine_hist.d_res_high                       1.93 
_refine_hist.d_res_low                        30.0 
# 
loop_
_refine_ls_restr.type 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.weight 
_refine_ls_restr.number 
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.pdbx_restraint_function 
f_bond_d           0.008  ? ? 1563 'X-RAY DIFFRACTION' ? 
f_angle_d          1.121  ? ? 2111 'X-RAY DIFFRACTION' ? 
f_dihedral_angle_d 12.668 ? ? 543  'X-RAY DIFFRACTION' ? 
f_chiral_restr     0.079  ? ? 245  'X-RAY DIFFRACTION' ? 
f_plane_restr      0.003  ? ? 279  'X-RAY DIFFRACTION' ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.R_factor_all 
'X-RAY DIFFRACTION' . 1.9301 2.0791  2669 0.2025 100.00 0.2882 . . 141 . . 
'X-RAY DIFFRACTION' . 2.0791 2.2883  2679 0.1923 100.00 0.2573 . . 139 . . 
'X-RAY DIFFRACTION' . 2.2883 2.6192  2664 0.1919 100.00 0.2387 . . 146 . . 
'X-RAY DIFFRACTION' . 2.6192 3.2991  2690 0.1845 100.00 0.2733 . . 142 . . 
'X-RAY DIFFRACTION' . 3.2991 28.3169 2706 0.1445 99.00  0.1689 . . 139 . . 
# 
_struct_ncs_oper.id             1 
_struct_ncs_oper.code           given 
_struct_ncs_oper.details        ? 
_struct_ncs_oper.matrix[1][1]   0.338000 
_struct_ncs_oper.matrix[1][2]   -0.940800 
_struct_ncs_oper.matrix[1][3]   -0.025390 
_struct_ncs_oper.matrix[2][1]   -0.940800 
_struct_ncs_oper.matrix[2][2]   -0.338500 
_struct_ncs_oper.matrix[2][3]   0.017530 
_struct_ncs_oper.matrix[3][1]   -0.025090 
_struct_ncs_oper.matrix[3][2]   0.017960 
_struct_ncs_oper.matrix[3][3]   -0.999500 
_struct_ncs_oper.vector[1]      -0.48290 
_struct_ncs_oper.vector[2]      0.42940 
_struct_ncs_oper.vector[3]      -31.93000 
# 
_struct.entry_id                  4BCZ 
_struct.title                     'Monomeric Human Cu,Zn Superoxide dismutase, loops IV and VII deleted, apo form.' 
_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        4BCZ 
_struct_keywords.pdbx_keywords   OXIDOREDUCTASE 
_struct_keywords.text            
'OXIDOREDUCTASE, CU/ZN SOD1, MONOMERIC MUTANT, DISEASE MUTATION, METAL BINDING, NEURODEGENERATION, ALS' 
# 
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 ? 
# 
_struct_biol.id   1 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA ? 8 ? 
BA ? 8 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA 1 2 ? anti-parallel 
AA 2 3 ? anti-parallel 
AA 3 4 ? anti-parallel 
AA 4 5 ? anti-parallel 
AA 5 6 ? anti-parallel 
AA 6 7 ? anti-parallel 
AA 7 8 ? anti-parallel 
BA 1 2 ? anti-parallel 
BA 2 3 ? anti-parallel 
BA 3 4 ? anti-parallel 
BA 4 5 ? anti-parallel 
BA 5 6 ? anti-parallel 
BA 6 7 ? anti-parallel 
BA 7 8 ? 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 ASP A 53  ? ALA A 59  ? ASP A 53  ALA A 59  
AA 2 GLY A 41  ? VAL A 47  ? GLY A 41  VAL A 47  
AA 3 THR A 86  ? HIS A 90  ? THR A 86  HIS A 90  
AA 4 LEU A 101 ? GLN A 110 ? LEU A 101 GLN A 110 
AA 5 LYS A 3   ? LYS A 9   ? LYS A 3   LYS A 9   
AA 6 GLN A 15  ? GLU A 21  ? GLN A 15  GLU A 21  
AA 7 VAL A 29  ? LYS A 36  ? VAL A 29  LYS A 36  
AA 8 ALA A 65  ? ASP A 71  ? ALA A 65  ASP A 71  
BA 1 ASP B 53  ? ALA B 59  ? ASP B 53  ALA B 59  
BA 2 GLY B 41  ? VAL B 47  ? GLY B 41  VAL B 47  
BA 3 THR B 86  ? HIS B 90  ? THR B 86  HIS B 90  
BA 4 LEU B 101 ? ALA B 109 ? LEU B 101 ALA B 109 
BA 5 LYS B 3   ? LYS B 9   ? LYS B 3   LYS B 9   
BA 6 GLN B 15  ? GLN B 22  ? GLN B 15  GLN B 22  
BA 7 VAL B 29  ? LYS B 36  ? VAL B 29  LYS B 36  
BA 8 ALA B 65  ? ASP B 71  ? ALA B 65  ASP B 71  
# 
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 ALA A 59  ? N ALA A 59  O GLY A 41  ? O GLY A 41  
AA 2 3 N HIS A 46  ? N HIS A 46  O VAL A 88  ? O VAL A 88  
AA 3 4 N VAL A 89  ? N VAL A 89  O ALA A 102 ? O ALA A 102 
AA 4 5 N ALA A 109 ? N ALA A 109 O LYS A 3   ? O LYS A 3   
AA 5 6 N LEU A 8   ? N LEU A 8   O GLY A 16  ? O GLY A 16  
AA 6 7 N GLU A 21  ? N GLU A 21  O LYS A 30  ? O LYS A 30  
AA 7 8 N ILE A 35  ? N ILE A 35  O ALA A 65  ? O ALA A 65  
BA 1 2 N ALA B 59  ? N ALA B 59  O GLY B 41  ? O GLY B 41  
BA 2 3 N HIS B 46  ? N HIS B 46  O VAL B 88  ? O VAL B 88  
BA 3 4 N VAL B 89  ? N VAL B 89  O ALA B 102 ? O ALA B 102 
BA 4 5 N ALA B 109 ? N ALA B 109 O LYS B 3   ? O LYS B 3   
BA 5 6 N LEU B 8   ? N LEU B 8   O GLY B 16  ? O GLY B 16  
BA 6 7 N GLU B 21  ? N GLU B 21  O LYS B 30  ? O LYS B 30  
BA 7 8 N ILE B 35  ? N ILE B 35  O ALA B 65  ? O ALA B 65  
# 
_database_PDB_matrix.entry_id          4BCZ 
_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                    4BCZ 
_atom_sites.fract_transf_matrix[1][1]   0.013435 
_atom_sites.fract_transf_matrix[1][2]   0.007757 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.015514 
_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]   0.016872 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
# 
loop_
_atom_type.symbol 
C 
N 
O 
# 
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   ? 21.614 -32.152 -14.799 1.00 57.33  ? 1    ALA A N   1 
ATOM   2    C CA  . ALA A 1 1   ? 21.807 -30.889 -15.511 1.00 59.29  ? 1    ALA A CA  1 
ATOM   3    C C   . ALA A 1 1   ? 23.209 -30.305 -15.317 1.00 54.87  ? 1    ALA A C   1 
ATOM   4    O O   . ALA A 1 1   ? 23.865 -30.552 -14.306 1.00 59.74  ? 1    ALA A O   1 
ATOM   5    C CB  . ALA A 1 1   ? 20.741 -29.873 -15.100 1.00 56.45  ? 1    ALA A CB  1 
ATOM   6    N N   . THR A 1 2   ? 23.668 -29.532 -16.293 1.00 42.37  ? 2    THR A N   1 
ATOM   7    C CA  . THR A 1 2   ? 24.969 -28.890 -16.187 1.00 43.13  ? 2    THR A CA  1 
ATOM   8    C C   . THR A 1 2   ? 24.850 -27.391 -15.871 1.00 35.43  ? 2    THR A C   1 
ATOM   9    O O   . THR A 1 2   ? 25.728 -26.834 -15.220 1.00 33.47  ? 2    THR A O   1 
ATOM   10   C CB  . THR A 1 2   ? 25.849 -29.142 -17.434 1.00 51.48  ? 2    THR A CB  1 
ATOM   11   O OG1 . THR A 1 2   ? 27.182 -28.690 -17.177 1.00 71.30  ? 2    THR A OG1 1 
ATOM   12   C CG2 . THR A 1 2   ? 25.308 -28.416 -18.644 1.00 44.83  ? 2    THR A CG2 1 
ATOM   13   N N   . LYS A 1 3   ? 23.771 -26.757 -16.331 1.00 27.36  ? 3    LYS A N   1 
ATOM   14   C CA  . LYS A 1 3   ? 23.460 -25.365 -15.981 1.00 24.58  ? 3    LYS A CA  1 
ATOM   15   C C   . LYS A 1 3   ? 22.002 -25.179 -15.572 1.00 25.42  ? 3    LYS A C   1 
ATOM   16   O O   . LYS A 1 3   ? 21.095 -25.831 -16.111 1.00 29.19  ? 3    LYS A O   1 
ATOM   17   C CB  . LYS A 1 3   ? 23.748 -24.425 -17.154 1.00 24.75  ? 3    LYS A CB  1 
ATOM   18   C CG  . LYS A 1 3   ? 25.186 -24.392 -17.595 1.00 27.32  ? 3    LYS A CG  1 
ATOM   19   C CD  . LYS A 1 3   ? 25.390 -23.336 -18.680 1.00 28.24  ? 3    LYS A CD  1 
ATOM   20   C CE  . LYS A 1 3   ? 26.685 -23.574 -19.450 1.00 46.36  ? 3    LYS A CE  1 
ATOM   21   N NZ  . LYS A 1 3   ? 27.899 -23.455 -18.589 1.00 55.09  ? 3    LYS A NZ  1 
ATOM   22   N N   . ALA A 1 4   ? 21.781 -24.265 -14.630 1.00 20.99  ? 4    ALA A N   1 
ATOM   23   C CA  . ALA A 1 4   ? 20.449 -23.929 -14.148 1.00 21.87  ? 4    ALA A CA  1 
ATOM   24   C C   . ALA A 1 4   ? 20.351 -22.439 -13.849 1.00 18.71  ? 4    ALA A C   1 
ATOM   25   O O   . ALA A 1 4   ? 21.360 -21.780 -13.648 1.00 22.36  ? 4    ALA A O   1 
ATOM   26   C CB  . ALA A 1 4   ? 20.117 -24.735 -12.886 1.00 18.19  ? 4    ALA A CB  1 
ATOM   27   N N   . VAL A 1 5   ? 19.129 -21.916 -13.819 1.00 16.37  ? 5    VAL A N   1 
ATOM   28   C CA  . VAL A 1 5   ? 18.879 -20.497 -13.545 1.00 17.97  ? 5    VAL A CA  1 
ATOM   29   C C   . VAL A 1 5   ? 17.656 -20.331 -12.628 1.00 20.70  ? 5    VAL A C   1 
ATOM   30   O O   . VAL A 1 5   ? 16.635 -20.981 -12.845 1.00 15.91  ? 5    VAL A O   1 
ATOM   31   C CB  . VAL A 1 5   ? 18.599 -19.717 -14.857 1.00 17.70  ? 5    VAL A CB  1 
ATOM   32   C CG1 . VAL A 1 5   ? 18.363 -18.208 -14.572 1.00 18.11  ? 5    VAL A CG1 1 
ATOM   33   C CG2 . VAL A 1 5   ? 19.756 -19.889 -15.849 1.00 24.93  ? 5    VAL A CG2 1 
ATOM   34   N N   . ALA A 1 6   ? 17.761 -19.470 -11.610 1.00 16.53  ? 6    ALA A N   1 
ATOM   35   C CA  . ALA A 1 6   ? 16.596 -19.037 -10.836 1.00 14.46  ? 6    ALA A CA  1 
ATOM   36   C C   . ALA A 1 6   ? 16.322 -17.563 -11.096 1.00 17.81  ? 6    ALA A C   1 
ATOM   37   O O   . ALA A 1 6   ? 17.214 -16.713 -10.975 1.00 17.83  ? 6    ALA A O   1 
ATOM   38   C CB  . ALA A 1 6   ? 16.793 -19.268 -9.334  1.00 12.03  ? 6    ALA A CB  1 
ATOM   39   N N   . VAL A 1 7   ? 15.079 -17.269 -11.449 1.00 13.65  ? 7    VAL A N   1 
ATOM   40   C CA  . VAL A 1 7   ? 14.626 -15.884 -11.573 1.00 17.72  ? 7    VAL A CA  1 
ATOM   41   C C   . VAL A 1 7   ? 13.928 -15.530 -10.262 1.00 17.92  ? 7    VAL A C   1 
ATOM   42   O O   . VAL A 1 7   ? 12.865 -16.069 -9.943  1.00 15.79  ? 7    VAL A O   1 
ATOM   43   C CB  . VAL A 1 7   ? 13.685 -15.690 -12.790 1.00 18.48  ? 7    VAL A CB  1 
ATOM   44   C CG1 . VAL A 1 7   ? 13.142 -14.242 -12.854 1.00 19.25  ? 7    VAL A CG1 1 
ATOM   45   C CG2 . VAL A 1 7   ? 14.405 -16.049 -14.088 1.00 23.85  ? 7    VAL A CG2 1 
ATOM   46   N N   . LEU A 1 8   ? 14.552 -14.647 -9.486  1.00 14.92  ? 8    LEU A N   1 
ATOM   47   C CA  . LEU A 1 8   ? 14.028 -14.281 -8.184  1.00 17.75  ? 8    LEU A CA  1 
ATOM   48   C C   . LEU A 1 8   ? 13.069 -13.123 -8.315  1.00 20.66  ? 8    LEU A C   1 
ATOM   49   O O   . LEU A 1 8   ? 13.378 -12.094 -8.937  1.00 15.84  ? 8    LEU A O   1 
ATOM   50   C CB  . LEU A 1 8   ? 15.164 -13.902 -7.224  1.00 20.38  ? 8    LEU A CB  1 
ATOM   51   C CG  . LEU A 1 8   ? 16.165 -14.999 -6.843  1.00 22.60  ? 8    LEU A CG  1 
ATOM   52   C CD1 . LEU A 1 8   ? 17.262 -14.429 -5.950  1.00 28.65  ? 8    LEU A CD1 1 
ATOM   53   C CD2 . LEU A 1 8   ? 15.459 -16.130 -6.130  1.00 26.47  ? 8    LEU A CD2 1 
ATOM   54   N N   . LYS A 1 9   ? 11.890 -13.299 -7.738  1.00 18.78  ? 9    LYS A N   1 
ATOM   55   C CA  . LYS A 1 9   ? 10.925 -12.230 -7.731  1.00 18.91  ? 9    LYS A CA  1 
ATOM   56   C C   . LYS A 1 9   ? 10.415 -12.029 -6.319  1.00 23.03  ? 9    LYS A C   1 
ATOM   57   O O   . LYS A 1 9   ? 10.040 -12.989 -5.645  1.00 15.49  ? 9    LYS A O   1 
ATOM   58   C CB  . LYS A 1 9   ? 9.776  -12.544 -8.679  1.00 20.86  ? 9    LYS A CB  1 
ATOM   59   C CG  . LYS A 1 9   ? 8.752  -11.410 -8.787  1.00 39.81  ? 9    LYS A CG  1 
ATOM   60   C CD  . LYS A 1 9   ? 9.397  -10.099 -9.257  1.00 37.95  ? 9    LYS A CD  1 
ATOM   61   C CE  . LYS A 1 9   ? 8.345  -9.058  -9.651  1.00 39.78  ? 9    LYS A CE  1 
ATOM   62   N NZ  . LYS A 1 9   ? 7.535  -8.588  -8.484  1.00 43.65  ? 9    LYS A NZ  1 
ATOM   63   N N   . GLY A 1 10  ? 10.402 -10.774 -5.876  1.00 21.57  ? 10   GLY A N   1 
ATOM   64   C CA  . GLY A 1 10  ? 9.898  -10.441 -4.560  1.00 19.33  ? 10   GLY A CA  1 
ATOM   65   C C   . GLY A 1 10  ? 9.024  -9.206  -4.591  1.00 32.73  ? 10   GLY A C   1 
ATOM   66   O O   . GLY A 1 10  ? 8.552  -8.805  -5.649  1.00 31.60  ? 10   GLY A O   1 
ATOM   67   N N   . ASP A 1 11  ? 8.805  -8.608  -3.421  1.00 28.59  ? 11   ASP A N   1 
ATOM   68   C CA  . ASP A 1 11  ? 7.950  -7.431  -3.301  1.00 29.43  ? 11   ASP A CA  1 
ATOM   69   C C   . ASP A 1 11  ? 8.661  -6.184  -3.788  1.00 31.36  ? 11   ASP A C   1 
ATOM   70   O O   . ASP A 1 11  ? 9.887  -6.080  -3.696  1.00 27.52  ? 11   ASP A O   1 
ATOM   71   C CB  . ASP A 1 11  ? 7.542  -7.202  -1.845  1.00 30.30  ? 11   ASP A CB  1 
ATOM   72   C CG  . ASP A 1 11  ? 6.845  -8.392  -1.247  1.00 43.34  ? 11   ASP A CG  1 
ATOM   73   O OD1 . ASP A 1 11  ? 5.601  -8.475  -1.367  1.00 48.38  ? 11   ASP A OD1 1 
ATOM   74   O OD2 . ASP A 1 11  ? 7.548  -9.249  -0.661  1.00 45.03  ? 11   ASP A OD2 1 
ATOM   75   N N   . GLY A 1 12  ? 7.875  -5.225  -4.264  1.00 32.19  ? 12   GLY A N   1 
ATOM   76   C CA  . GLY A 1 12  ? 8.397  -3.941  -4.682  1.00 33.36  ? 12   GLY A CA  1 
ATOM   77   C C   . GLY A 1 12  ? 9.439  -4.128  -5.763  1.00 39.73  ? 12   GLY A C   1 
ATOM   78   O O   . GLY A 1 12  ? 9.192  -4.805  -6.762  1.00 34.52  ? 12   GLY A O   1 
ATOM   79   N N   . PRO A 1 13  ? 10.627 -3.556  -5.552  1.00 37.75  ? 13   PRO A N   1 
ATOM   80   C CA  . PRO A 1 13  ? 11.673 -3.618  -6.574  1.00 38.17  ? 13   PRO A CA  1 
ATOM   81   C C   . PRO A 1 13  ? 12.557 -4.865  -6.464  1.00 26.96  ? 13   PRO A C   1 
ATOM   82   O O   . PRO A 1 13  ? 13.494 -4.983  -7.260  1.00 26.84  ? 13   PRO A O   1 
ATOM   83   C CB  . PRO A 1 13  ? 12.498 -2.359  -6.280  1.00 41.72  ? 13   PRO A CB  1 
ATOM   84   C CG  . PRO A 1 13  ? 12.422 -2.236  -4.777  1.00 43.57  ? 13   PRO A CG  1 
ATOM   85   C CD  . PRO A 1 13  ? 11.052 -2.783  -4.370  1.00 43.14  ? 13   PRO A CD  1 
ATOM   86   N N   . VAL A 1 14  ? 12.294 -5.773  -5.519  1.00 23.14  ? 14   VAL A N   1 
ATOM   87   C CA  . VAL A 1 14  ? 13.197 -6.931  -5.358  1.00 20.25  ? 14   VAL A CA  1 
ATOM   88   C C   . VAL A 1 14  ? 13.111 -7.918  -6.527  1.00 24.69  ? 14   VAL A C   1 
ATOM   89   O O   . VAL A 1 14  ? 12.050 -8.462  -6.827  1.00 25.02  ? 14   VAL A O   1 
ATOM   90   C CB  . VAL A 1 14  ? 12.983 -7.693  -4.036  1.00 24.40  ? 14   VAL A CB  1 
ATOM   91   C CG1 . VAL A 1 14  ? 13.949 -8.857  -3.963  1.00 23.86  ? 14   VAL A CG1 1 
ATOM   92   C CG2 . VAL A 1 14  ? 13.197 -6.754  -2.844  1.00 19.33  ? 14   VAL A CG2 1 
ATOM   93   N N   . GLN A 1 15  ? 14.231 -8.128  -7.199  1.00 20.73  ? 15   GLN A N   1 
ATOM   94   C CA  . GLN A 1 15  ? 14.290 -9.084  -8.302  1.00 17.51  ? 15   GLN A CA  1 
ATOM   95   C C   . GLN A 1 15  ? 15.733 -9.423  -8.598  1.00 18.59  ? 15   GLN A C   1 
ATOM   96   O O   . GLN A 1 15  ? 16.654 -8.635  -8.331  1.00 17.37  ? 15   GLN A O   1 
ATOM   97   C CB  . GLN A 1 15  ? 13.576 -8.566  -9.561  1.00 22.88  ? 15   GLN A CB  1 
ATOM   98   C CG  . GLN A 1 15  ? 14.060 -7.208  -10.038 1.00 26.00  ? 15   GLN A CG  1 
ATOM   99   C CD  . GLN A 1 15  ? 15.238 -7.312  -10.983 0.30 27.40  ? 15   GLN A CD  1 
ATOM   100  O OE1 . GLN A 1 15  ? 15.503 -8.373  -11.554 0.48 22.67  ? 15   GLN A OE1 1 
ATOM   101  N NE2 . GLN A 1 15  ? 15.955 -6.209  -11.155 0.77 31.90  ? 15   GLN A NE2 1 
ATOM   102  N N   . GLY A 1 16  ? 15.942 -10.617 -9.126  1.00 14.35  ? 16   GLY A N   1 
ATOM   103  C CA  . GLY A 1 16  ? 17.298 -11.050 -9.360  1.00 18.13  ? 16   GLY A CA  1 
ATOM   104  C C   . GLY A 1 16  ? 17.401 -12.211 -10.313 1.00 17.72  ? 16   GLY A C   1 
ATOM   105  O O   . GLY A 1 16  ? 16.399 -12.822 -10.671 1.00 18.27  ? 16   GLY A O   1 
ATOM   106  N N   . ILE A 1 17  ? 18.620 -12.495 -10.747 1.00 14.33  ? 17   ILE A N   1 
ATOM   107  C CA  . ILE A 1 17  ? 18.863 -13.653 -11.595 1.00 16.22  ? 17   ILE A CA  1 
ATOM   108  C C   . ILE A 1 17  ? 20.100 -14.333 -11.070 1.00 13.21  ? 17   ILE A C   1 
ATOM   109  O O   . ILE A 1 17  ? 21.178 -13.706 -10.957 1.00 16.52  ? 17   ILE A O   1 
ATOM   110  C CB  . ILE A 1 17  ? 19.096 -13.252 -13.058 1.00 18.70  ? 17   ILE A CB  1 
ATOM   111  C CG1 . ILE A 1 17  ? 17.798 -12.738 -13.668 1.00 25.29  ? 17   ILE A CG1 1 
ATOM   112  C CG2 . ILE A 1 17  ? 19.532 -14.451 -13.875 1.00 19.71  ? 17   ILE A CG2 1 
ATOM   113  C CD1 . ILE A 1 17  ? 17.994 -12.108 -15.008 1.00 34.65  ? 17   ILE A CD1 1 
ATOM   114  N N   . ILE A 1 18  ? 19.925 -15.596 -10.690 1.00 12.26  ? 18   ILE A N   1 
ATOM   115  C CA  . ILE A 1 18  ? 21.023 -16.390 -10.181 1.00 12.47  ? 18   ILE A CA  1 
ATOM   116  C C   . ILE A 1 18  ? 21.294 -17.619 -11.065 1.00 16.51  ? 18   ILE A C   1 
ATOM   117  O O   . ILE A 1 18  ? 20.392 -18.391 -11.358 1.00 16.97  ? 18   ILE A O   1 
ATOM   118  C CB  . ILE A 1 18  ? 20.726 -16.851 -8.729  1.00 19.30  ? 18   ILE A CB  1 
ATOM   119  C CG1 . ILE A 1 18  ? 20.608 -15.638 -7.795  1.00 19.71  ? 18   ILE A CG1 1 
ATOM   120  C CG2 . ILE A 1 18  ? 21.823 -17.776 -8.248  1.00 19.54  ? 18   ILE A CG2 1 
ATOM   121  C CD1 . ILE A 1 18  ? 21.932 -14.811 -7.710  1.00 19.12  ? 18   ILE A CD1 1 
ATOM   122  N N   . ASN A 1 19  ? 22.547 -17.802 -11.460 1.00 14.17  ? 19   ASN A N   1 
ATOM   123  C CA  . ASN A 1 19  ? 22.970 -18.907 -12.308 1.00 18.15  ? 19   ASN A CA  1 
ATOM   124  C C   . ASN A 1 19  ? 23.717 -19.974 -11.512 1.00 21.18  ? 19   ASN A C   1 
ATOM   125  O O   . ASN A 1 19  ? 24.436 -19.646 -10.569 1.00 22.68  ? 19   ASN A O   1 
ATOM   126  C CB  . ASN A 1 19  ? 23.875 -18.383 -13.428 1.00 18.89  ? 19   ASN A CB  1 
ATOM   127  C CG  . ASN A 1 19  ? 23.190 -17.313 -14.267 1.00 17.96  ? 19   ASN A CG  1 
ATOM   128  O OD1 . ASN A 1 19  ? 22.172 -17.574 -14.906 1.00 17.66  ? 19   ASN A OD1 1 
ATOM   129  N ND2 . ASN A 1 19  ? 23.746 -16.104 -14.267 1.00 18.35  ? 19   ASN A ND2 1 
ATOM   130  N N   . PHE A 1 20  ? 23.535 -21.238 -11.901 1.00 17.55  ? 20   PHE A N   1 
ATOM   131  C CA  . PHE A 1 20  ? 24.215 -22.388 -11.296 1.00 19.42  ? 20   PHE A CA  1 
ATOM   132  C C   . PHE A 1 20  ? 24.888 -23.162 -12.429 1.00 22.65  ? 20   PHE A C   1 
ATOM   133  O O   . PHE A 1 20  ? 24.257 -23.394 -13.454 1.00 30.97  ? 20   PHE A O   1 
ATOM   134  C CB  . PHE A 1 20  ? 23.208 -23.316 -10.577 1.00 18.98  ? 20   PHE A CB  1 
ATOM   135  C CG  . PHE A 1 20  ? 22.418 -22.644 -9.456  1.00 21.58  ? 20   PHE A CG  1 
ATOM   136  C CD1 . PHE A 1 20  ? 21.298 -21.883 -9.739  1.00 18.36  ? 20   PHE A CD1 1 
ATOM   137  C CD2 . PHE A 1 20  ? 22.803 -22.789 -8.123  1.00 23.16  ? 20   PHE A CD2 1 
ATOM   138  C CE1 . PHE A 1 20  ? 20.557 -21.256 -8.710  1.00 18.63  ? 20   PHE A CE1 1 
ATOM   139  C CE2 . PHE A 1 20  ? 22.082 -22.167 -7.089  1.00 27.54  ? 20   PHE A CE2 1 
ATOM   140  C CZ  . PHE A 1 20  ? 20.952 -21.401 -7.388  1.00 21.84  ? 20   PHE A CZ  1 
ATOM   141  N N   . GLU A 1 21  ? 26.159 -23.541 -12.264 1.00 24.25  ? 21   GLU A N   1 
ATOM   142  C CA  . GLU A 1 21  ? 26.855 -24.374 -13.247 1.00 26.84  ? 21   GLU A CA  1 
ATOM   143  C C   . GLU A 1 21  ? 27.670 -25.471 -12.572 1.00 29.63  ? 21   GLU A C   1 
ATOM   144  O O   . GLU A 1 21  ? 28.339 -25.231 -11.572 1.00 30.18  ? 21   GLU A O   1 
ATOM   145  C CB  . GLU A 1 21  ? 27.773 -23.535 -14.144 1.00 30.15  ? 21   GLU A CB  1 
ATOM   146  C CG  . GLU A 1 21  ? 26.999 -22.622 -15.081 1.00 39.42  ? 21   GLU A CG  1 
ATOM   147  C CD  . GLU A 1 21  ? 27.880 -21.660 -15.857 1.00 39.69  ? 21   GLU A CD  1 
ATOM   148  O OE1 . GLU A 1 21  ? 28.578 -22.098 -16.795 1.00 39.36  ? 21   GLU A OE1 1 
ATOM   149  O OE2 . GLU A 1 21  ? 27.848 -20.460 -15.529 1.00 36.65  ? 21   GLU A OE2 1 
ATOM   150  N N   . GLN A 1 22  ? 27.623 -26.668 -13.143 1.00 31.74  ? 22   GLN A N   1 
ATOM   151  C CA  . GLN A 1 22  ? 28.364 -27.804 -12.612 1.00 34.97  ? 22   GLN A CA  1 
ATOM   152  C C   . GLN A 1 22  ? 28.911 -28.602 -13.786 1.00 38.25  ? 22   GLN A C   1 
ATOM   153  O O   . GLN A 1 22  ? 28.143 -29.103 -14.609 1.00 38.08  ? 22   GLN A O   1 
ATOM   154  C CB  . GLN A 1 22  ? 27.434 -28.659 -11.752 1.00 34.33  ? 22   GLN A CB  1 
ATOM   155  C CG  . GLN A 1 22  ? 28.076 -29.827 -11.019 1.00 37.73  ? 22   GLN A CG  1 
ATOM   156  C CD  . GLN A 1 22  ? 27.049 -30.613 -10.199 1.00 41.35  ? 22   GLN A CD  1 
ATOM   157  O OE1 . GLN A 1 22  ? 25.903 -30.816 -10.632 1.00 35.41  ? 22   GLN A OE1 1 
ATOM   158  N NE2 . GLN A 1 22  ? 27.450 -31.042 -9.008  1.00 38.73  ? 22   GLN A NE2 1 
ATOM   159  N N   . LYS A 1 23  ? 30.237 -28.708 -13.875 1.00 41.54  ? 23   LYS A N   1 
ATOM   160  C CA  . LYS A 1 23  ? 30.858 -29.402 -14.990 1.00 45.21  ? 23   LYS A CA  1 
ATOM   161  C C   . LYS A 1 23  ? 30.591 -30.900 -14.928 1.00 47.72  ? 23   LYS A C   1 
ATOM   162  O O   . LYS A 1 23  ? 30.298 -31.522 -15.943 1.00 49.19  ? 23   LYS A O   1 
ATOM   163  C CB  . LYS A 1 23  ? 32.374 -29.160 -15.024 1.00 48.65  ? 23   LYS A CB  1 
ATOM   164  C CG  . LYS A 1 23  ? 33.082 -29.892 -16.174 1.00 53.11  ? 23   LYS A CG  1 
ATOM   165  C CD  . LYS A 1 23  ? 34.583 -30.103 -15.932 1.00 60.04  ? 23   LYS A CD  1 
ATOM   166  C CE  . LYS A 1 23  ? 35.365 -28.788 -15.906 1.00 57.19  ? 23   LYS A CE  1 
ATOM   167  N NZ  . LYS A 1 23  ? 36.834 -29.017 -16.092 1.00 62.50  ? 23   LYS A NZ  1 
ATOM   168  N N   . GLU A 1 24  ? 30.703 -31.477 -13.733 1.00 48.53  ? 24   GLU A N   1 
ATOM   169  C CA  . GLU A 1 24  ? 30.629 -32.927 -13.573 1.00 51.71  ? 24   GLU A CA  1 
ATOM   170  C C   . GLU A 1 24  ? 29.678 -33.353 -12.465 1.00 49.85  ? 24   GLU A C   1 
ATOM   171  O O   . GLU A 1 24  ? 29.508 -32.635 -11.477 1.00 47.32  ? 24   GLU A O   1 
ATOM   172  C CB  . GLU A 1 24  ? 32.017 -33.494 -13.287 1.00 56.67  ? 24   GLU A CB  1 
ATOM   173  C CG  . GLU A 1 24  ? 33.058 -33.009 -14.250 1.00 58.94  ? 24   GLU A CG  1 
ATOM   174  C CD  . GLU A 1 24  ? 34.439 -33.511 -13.912 1.00 64.13  ? 24   GLU A CD  1 
ATOM   175  O OE1 . GLU A 1 24  ? 34.641 -33.989 -12.777 1.00 65.39  ? 24   GLU A OE1 1 
ATOM   176  O OE2 . GLU A 1 24  ? 35.320 -33.425 -14.787 1.00 68.95  ? 24   GLU A OE2 1 
ATOM   177  N N   . SER A 1 25  ? 29.113 -34.552 -12.622 1.00 51.62  ? 25   SER A N   1 
ATOM   178  C CA  . SER A 1 25  ? 28.003 -35.038 -11.795 1.00 69.10  ? 25   SER A CA  1 
ATOM   179  C C   . SER A 1 25  ? 28.157 -34.857 -10.277 1.00 66.83  ? 25   SER A C   1 
ATOM   180  O O   . SER A 1 25  ? 27.182 -34.565 -9.583  1.00 66.39  ? 25   SER A O   1 
ATOM   181  C CB  . SER A 1 25  ? 27.698 -36.504 -12.121 1.00 64.71  ? 25   SER A CB  1 
ATOM   182  O OG  . SER A 1 25  ? 28.744 -37.346 -11.682 1.00 74.70  ? 25   SER A OG  1 
ATOM   183  N N   . ASN A 1 26  ? 29.369 -35.033 -9.764  1.00 67.19  ? 26   ASN A N   1 
ATOM   184  C CA  . ASN A 1 26  ? 29.608 -34.898 -8.329  1.00 72.16  ? 26   ASN A CA  1 
ATOM   185  C C   . ASN A 1 26  ? 30.425 -33.659 -7.987  1.00 63.16  ? 26   ASN A C   1 
ATOM   186  O O   . ASN A 1 26  ? 30.836 -33.479 -6.841  1.00 57.10  ? 26   ASN A O   1 
ATOM   187  C CB  . ASN A 1 26  ? 30.320 -36.143 -7.782  1.00 89.21  ? 26   ASN A CB  1 
ATOM   188  C CG  . ASN A 1 26  ? 29.369 -37.116 -7.101  1.00 98.95  ? 26   ASN A CG  1 
ATOM   189  O OD1 . ASN A 1 26  ? 28.801 -38.004 -7.741  1.00 103.34 ? 26   ASN A OD1 1 
ATOM   190  N ND2 . ASN A 1 26  ? 29.202 -36.961 -5.792  1.00 100.60 ? 26   ASN A ND2 1 
ATOM   191  N N   . GLY A 1 27  ? 30.660 -32.812 -8.984  1.00 50.13  ? 27   GLY A N   1 
ATOM   192  C CA  . GLY A 1 27  ? 31.595 -31.707 -8.847  1.00 50.55  ? 27   GLY A CA  1 
ATOM   193  C C   . GLY A 1 27  ? 31.043 -30.443 -8.205  1.00 45.53  ? 27   GLY A C   1 
ATOM   194  O O   . GLY A 1 27  ? 29.857 -30.358 -7.903  1.00 42.51  ? 27   GLY A O   1 
ATOM   195  N N   . PRO A 1 28  ? 31.911 -29.445 -7.991  1.00 49.38  ? 28   PRO A N   1 
ATOM   196  C CA  . PRO A 1 28  ? 31.485 -28.221 -7.308  1.00 43.49  ? 28   PRO A CA  1 
ATOM   197  C C   . PRO A 1 28  ? 30.530 -27.435 -8.193  1.00 42.97  ? 28   PRO A C   1 
ATOM   198  O O   . PRO A 1 28  ? 30.584 -27.571 -9.411  1.00 41.86  ? 28   PRO A O   1 
ATOM   199  C CB  . PRO A 1 28  ? 32.793 -27.457 -7.116  1.00 47.08  ? 28   PRO A CB  1 
ATOM   200  C CG  . PRO A 1 28  ? 33.674 -27.936 -8.230  1.00 48.67  ? 28   PRO A CG  1 
ATOM   201  C CD  . PRO A 1 28  ? 33.317 -29.380 -8.433  1.00 54.24  ? 28   PRO A CD  1 
ATOM   202  N N   . VAL A 1 29  ? 29.654 -26.641 -7.587  1.00 38.29  ? 29   VAL A N   1 
ATOM   203  C CA  . VAL A 1 29  ? 28.694 -25.855 -8.345  1.00 34.38  ? 29   VAL A CA  1 
ATOM   204  C C   . VAL A 1 29  ? 28.987 -24.376 -8.182  1.00 39.45  ? 29   VAL A C   1 
ATOM   205  O O   . VAL A 1 29  ? 29.043 -23.861 -7.064  1.00 42.38  ? 29   VAL A O   1 
ATOM   206  C CB  . VAL A 1 29  ? 27.245 -26.108 -7.886  1.00 35.37  ? 29   VAL A CB  1 
ATOM   207  C CG1 . VAL A 1 29  ? 26.285 -25.136 -8.589  1.00 26.16  ? 29   VAL A CG1 1 
ATOM   208  C CG2 . VAL A 1 29  ? 26.839 -27.559 -8.121  1.00 37.06  ? 29   VAL A CG2 1 
ATOM   209  N N   . LYS A 1 30  ? 29.183 -23.697 -9.303  1.00 36.74  ? 30   LYS A N   1 
ATOM   210  C CA  . LYS A 1 30  ? 29.384 -22.259 -9.294  1.00 38.83  ? 30   LYS A CA  1 
ATOM   211  C C   . LYS A 1 30  ? 28.017 -21.570 -9.306  1.00 33.09  ? 30   LYS A C   1 
ATOM   212  O O   . LYS A 1 30  ? 27.159 -21.906 -10.119 1.00 26.15  ? 30   LYS A O   1 
ATOM   213  C CB  . LYS A 1 30  ? 30.232 -21.845 -10.501 1.00 46.89  ? 30   LYS A CB  1 
ATOM   214  C CG  . LYS A 1 30  ? 30.682 -20.394 -10.494 1.00 57.70  ? 30   LYS A CG  1 
ATOM   215  C CD  . LYS A 1 30  ? 31.547 -20.088 -9.287  1.00 72.61  ? 30   LYS A CD  1 
ATOM   216  C CE  . LYS A 1 30  ? 32.180 -18.714 -9.415  1.00 81.75  ? 30   LYS A CE  1 
ATOM   217  N NZ  . LYS A 1 30  ? 31.165 -17.693 -9.795  1.00 80.43  ? 30   LYS A NZ  1 
ATOM   218  N N   . VAL A 1 31  ? 27.819 -20.631 -8.382  1.00 27.10  ? 31   VAL A N   1 
ATOM   219  C CA  . VAL A 1 31  ? 26.575 -19.883 -8.238  1.00 25.28  ? 31   VAL A CA  1 
ATOM   220  C C   . VAL A 1 31  ? 26.923 -18.411 -8.424  1.00 23.67  ? 31   VAL A C   1 
ATOM   221  O O   . VAL A 1 31  ? 27.804 -17.881 -7.736  1.00 25.89  ? 31   VAL A O   1 
ATOM   222  C CB  . VAL A 1 31  ? 25.978 -20.075 -6.827  1.00 29.78  ? 31   VAL A CB  1 
ATOM   223  C CG1 . VAL A 1 31  ? 24.623 -19.385 -6.705  1.00 20.43  ? 31   VAL A CG1 1 
ATOM   224  C CG2 . VAL A 1 31  ? 25.849 -21.577 -6.490  1.00 26.28  ? 31   VAL A CG2 1 
ATOM   225  N N   . TRP A 1 32  ? 26.276 -17.747 -9.371  1.00 19.11  ? 32   TRP A N   1 
ATOM   226  C CA  . TRP A 1 32  ? 26.648 -16.361 -9.648  1.00 20.59  ? 32   TRP A CA  1 
ATOM   227  C C   . TRP A 1 32  ? 25.502 -15.572 -10.233 1.00 25.27  ? 32   TRP A C   1 
ATOM   228  O O   . TRP A 1 32  ? 24.646 -16.114 -10.900 1.00 22.01  ? 32   TRP A O   1 
ATOM   229  C CB  . TRP A 1 32  ? 27.875 -16.288 -10.571 1.00 25.86  ? 32   TRP A CB  1 
ATOM   230  C CG  . TRP A 1 32  ? 27.658 -16.847 -11.953 1.00 23.58  ? 32   TRP A CG  1 
ATOM   231  C CD1 . TRP A 1 32  ? 27.758 -18.161 -12.344 1.00 21.63  ? 32   TRP A CD1 1 
ATOM   232  C CD2 . TRP A 1 32  ? 27.312 -16.104 -13.124 1.00 25.75  ? 32   TRP A CD2 1 
ATOM   233  N NE1 . TRP A 1 32  ? 27.496 -18.273 -13.695 1.00 27.50  ? 32   TRP A NE1 1 
ATOM   234  C CE2 . TRP A 1 32  ? 27.228 -17.023 -14.196 1.00 22.84  ? 32   TRP A CE2 1 
ATOM   235  C CE3 . TRP A 1 32  ? 27.059 -14.748 -13.372 1.00 21.57  ? 32   TRP A CE3 1 
ATOM   236  C CZ2 . TRP A 1 32  ? 26.899 -16.627 -15.493 1.00 34.09  ? 32   TRP A CZ2 1 
ATOM   237  C CZ3 . TRP A 1 32  ? 26.731 -14.356 -14.669 1.00 27.58  ? 32   TRP A CZ3 1 
ATOM   238  C CH2 . TRP A 1 32  ? 26.653 -15.291 -15.709 1.00 31.85  ? 32   TRP A CH2 1 
ATOM   239  N N   . GLY A 1 33  ? 25.476 -14.277 -9.979  1.00 20.61  ? 33   GLY A N   1 
ATOM   240  C CA  . GLY A 1 33  ? 24.402 -13.480 -10.551 1.00 20.35  ? 33   GLY A CA  1 
ATOM   241  C C   . GLY A 1 33  ? 24.253 -12.247 -9.704  1.00 21.85  ? 33   GLY A C   1 
ATOM   242  O O   . GLY A 1 33  ? 25.232 -11.767 -9.105  1.00 19.06  ? 33   GLY A O   1 
ATOM   243  N N   . SER A 1 34  ? 23.046 -11.717 -9.643  1.00 20.13  ? 34   SER A N   1 
ATOM   244  C CA  . SER A 1 34  ? 22.858 -10.545 -8.794  1.00 20.37  ? 34   SER A CA  1 
ATOM   245  C C   . SER A 1 34  ? 21.397 -10.401 -8.418  1.00 20.49  ? 34   SER A C   1 
ATOM   246  O O   . SER A 1 34  ? 20.504 -10.965 -9.068  1.00 21.38  ? 34   SER A O   1 
ATOM   247  C CB  . SER A 1 34  ? 23.361 -9.272  -9.468  1.00 25.65  ? 34   SER A CB  1 
ATOM   248  O OG  . SER A 1 34  ? 22.535 -8.947  -10.576 1.00 24.96  ? 34   SER A OG  1 
ATOM   249  N N   . ILE A 1 35  ? 21.171 -9.660  -7.340  1.00 20.25  ? 35   ILE A N   1 
ATOM   250  C CA  . ILE A 1 35  ? 19.824 -9.408  -6.843  1.00 19.62  ? 35   ILE A CA  1 
ATOM   251  C C   . ILE A 1 35  ? 19.745 -7.922  -6.566  1.00 19.88  ? 35   ILE A C   1 
ATOM   252  O O   . ILE A 1 35  ? 20.669 -7.333  -6.004  1.00 25.29  ? 35   ILE A O   1 
ATOM   253  C CB  . ILE A 1 35  ? 19.544 -10.186 -5.542  1.00 16.23  ? 35   ILE A CB  1 
ATOM   254  C CG1 . ILE A 1 35  ? 19.940 -11.657 -5.692  1.00 21.58  ? 35   ILE A CG1 1 
ATOM   255  C CG2 . ILE A 1 35  ? 18.073 -10.073 -5.137  1.00 15.62  ? 35   ILE A CG2 1 
ATOM   256  C CD1 . ILE A 1 35  ? 20.084 -12.394 -4.355  1.00 24.31  ? 35   ILE A CD1 1 
ATOM   257  N N   . LYS A 1 36  ? 18.650 -7.305  -6.967  1.00 16.09  ? 36   LYS A N   1 
ATOM   258  C CA  . LYS A 1 36  ? 18.534 -5.877  -6.805  1.00 22.51  ? 36   LYS A CA  1 
ATOM   259  C C   . LYS A 1 36  ? 17.265 -5.569  -6.025  1.00 26.41  ? 36   LYS A C   1 
ATOM   260  O O   . LYS A 1 36  ? 16.428 -6.459  -5.810  1.00 22.19  ? 36   LYS A O   1 
ATOM   261  C CB  . LYS A 1 36  ? 18.564 -5.205  -8.190  1.00 30.91  ? 36   LYS A CB  1 
ATOM   262  C CG  . LYS A 1 36  ? 19.770 -5.700  -9.026  1.00 35.70  ? 36   LYS A CG  1 
ATOM   263  C CD  . LYS A 1 36  ? 19.936 -5.022  -10.384 1.00 37.47  ? 36   LYS A CD  1 
ATOM   264  C CE  . LYS A 1 36  ? 21.114 -5.659  -11.145 1.00 40.12  ? 36   LYS A CE  1 
ATOM   265  N NZ  . LYS A 1 36  ? 21.526 -4.876  -12.360 1.00 49.82  ? 36   LYS A NZ  1 
ATOM   266  N N   . GLY A 1 37  ? 17.135 -4.321  -5.580  1.00 16.20  ? 37   GLY A N   1 
ATOM   267  C CA  . GLY A 1 37  ? 15.930 -3.874  -4.907  1.00 19.12  ? 37   GLY A CA  1 
ATOM   268  C C   . GLY A 1 37  ? 15.960 -4.194  -3.420  1.00 26.45  ? 37   GLY A C   1 
ATOM   269  O O   . GLY A 1 37  ? 14.959 -4.017  -2.724  1.00 23.34  ? 37   GLY A O   1 
ATOM   270  N N   . LEU A 1 38  ? 17.110 -4.653  -2.928  1.00 17.46  ? 38   LEU A N   1 
ATOM   271  C CA  . LEU A 1 38  ? 17.238 -5.066  -1.521  1.00 18.91  ? 38   LEU A CA  1 
ATOM   272  C C   . LEU A 1 38  ? 17.541 -3.899  -0.599  1.00 24.63  ? 38   LEU A C   1 
ATOM   273  O O   . LEU A 1 38  ? 18.045 -2.877  -1.036  1.00 27.93  ? 38   LEU A O   1 
ATOM   274  C CB  . LEU A 1 38  ? 18.348 -6.101  -1.371  1.00 16.57  ? 38   LEU A CB  1 
ATOM   275  C CG  . LEU A 1 38  ? 18.099 -7.461  -2.023  1.00 16.97  ? 38   LEU A CG  1 
ATOM   276  C CD1 . LEU A 1 38  ? 19.418 -8.228  -2.085  1.00 19.95  ? 38   LEU A CD1 1 
ATOM   277  C CD2 . LEU A 1 38  ? 17.045 -8.210  -1.222  1.00 20.10  ? 38   LEU A CD2 1 
ATOM   278  N N   . THR A 1 39  ? 17.254 -4.056  0.685   1.00 21.51  ? 39   THR A N   1 
ATOM   279  C CA  . THR A 1 39  ? 17.712 -3.078  1.655   1.00 28.47  ? 39   THR A CA  1 
ATOM   280  C C   . THR A 1 39  ? 19.204 -3.302  1.847   1.00 29.11  ? 39   THR A C   1 
ATOM   281  O O   . THR A 1 39  ? 19.697 -4.402  1.645   1.00 22.62  ? 39   THR A O   1 
ATOM   282  C CB  . THR A 1 39  ? 17.007 -3.259  3.013   1.00 35.50  ? 39   THR A CB  1 
ATOM   283  O OG1 . THR A 1 39  ? 16.969 -4.655  3.329   1.00 23.45  ? 39   THR A OG1 1 
ATOM   284  C CG2 . THR A 1 39  ? 15.573 -2.722  2.961   1.00 29.09  ? 39   THR A CG2 1 
ATOM   285  N N   . GLU A 1 40  ? 19.928 -2.262  2.235   1.00 30.57  ? 40   GLU A N   1 
ATOM   286  C CA  . GLU A 1 40  ? 21.368 -2.406  2.448   1.00 27.54  ? 40   GLU A CA  1 
ATOM   287  C C   . GLU A 1 40  ? 21.705 -3.408  3.569   1.00 28.75  ? 40   GLU A C   1 
ATOM   288  O O   . GLU A 1 40  ? 21.078 -3.405  4.629   1.00 30.11  ? 40   GLU A O   1 
ATOM   289  C CB  . GLU A 1 40  ? 21.995 -1.047  2.756   1.00 27.26  ? 40   GLU A CB  1 
ATOM   290  C CG  . GLU A 1 40  ? 23.500 -1.106  2.924   1.00 30.74  ? 40   GLU A CG  1 
ATOM   291  C CD  . GLU A 1 40  ? 24.087 0.242   3.284   1.00 50.84  ? 40   GLU A CD  1 
ATOM   292  O OE1 . GLU A 1 40  ? 23.307 1.132   3.699   1.00 48.38  ? 40   GLU A OE1 1 
ATOM   293  O OE2 . GLU A 1 40  ? 25.324 0.403   3.152   1.00 55.97  ? 40   GLU A OE2 1 
ATOM   294  N N   . GLY A 1 41  ? 22.699 -4.257  3.331   1.00 24.40  ? 41   GLY A N   1 
ATOM   295  C CA  . GLY A 1 41  ? 23.202 -5.128  4.377   1.00 25.35  ? 41   GLY A CA  1 
ATOM   296  C C   . GLY A 1 41  ? 23.044 -6.591  4.024   1.00 23.66  ? 41   GLY A C   1 
ATOM   297  O O   . GLY A 1 41  ? 22.915 -6.934  2.843   1.00 26.16  ? 41   GLY A O   1 
ATOM   298  N N   . LEU A 1 42  ? 23.053 -7.447  5.043   1.00 24.65  ? 42   LEU A N   1 
ATOM   299  C CA  . LEU A 1 42  ? 23.101 -8.891  4.845   1.00 23.68  ? 42   LEU A CA  1 
ATOM   300  C C   . LEU A 1 42  ? 21.712 -9.462  4.649   1.00 22.37  ? 42   LEU A C   1 
ATOM   301  O O   . LEU A 1 42  ? 20.794 -9.114  5.392   1.00 23.49  ? 42   LEU A O   1 
ATOM   302  C CB  . LEU A 1 42  ? 23.735 -9.574  6.055   1.00 25.80  ? 42   LEU A CB  1 
ATOM   303  C CG  . LEU A 1 42  ? 25.173 -9.141  6.354   1.00 27.61  ? 42   LEU A CG  1 
ATOM   304  C CD1 . LEU A 1 42  ? 25.693 -9.815  7.623   1.00 35.45  ? 42   LEU A CD1 1 
ATOM   305  C CD2 . LEU A 1 42  ? 26.008 -9.512  5.158   1.00 32.65  ? 42   LEU A CD2 1 
ATOM   306  N N   . HIS A 1 43  ? 21.567 -10.362 3.681   1.00 22.28  ? 43   HIS A N   1 
ATOM   307  C CA  . HIS A 1 43  ? 20.305 -11.070 3.464   1.00 22.92  ? 43   HIS A CA  1 
ATOM   308  C C   . HIS A 1 43  ? 20.517 -12.580 3.307   1.00 21.85  ? 43   HIS A C   1 
ATOM   309  O O   . HIS A 1 43  ? 21.315 -13.018 2.457   1.00 22.08  ? 43   HIS A O   1 
ATOM   310  C CB  . HIS A 1 43  ? 19.619 -10.532 2.210   1.00 21.54  ? 43   HIS A CB  1 
ATOM   311  C CG  . HIS A 1 43  ? 19.269 -9.077  2.292   1.00 28.97  ? 43   HIS A CG  1 
ATOM   312  N ND1 . HIS A 1 43  ? 18.004 -8.637  2.615   1.00 21.78  ? 43   HIS A ND1 1 
ATOM   313  C CD2 . HIS A 1 43  ? 20.018 -7.964  2.092   1.00 19.18  ? 43   HIS A CD2 1 
ATOM   314  C CE1 . HIS A 1 43  ? 17.988 -7.315  2.608   1.00 23.50  ? 43   HIS A CE1 1 
ATOM   315  N NE2 . HIS A 1 43  ? 19.199 -6.881  2.300   1.00 21.65  ? 43   HIS A NE2 1 
ATOM   316  N N   . GLY A 1 44  ? 19.798 -13.360 4.110   1.00 23.36  ? 44   GLY A N   1 
ATOM   317  C CA  . GLY A 1 44  ? 19.871 -14.811 4.072   1.00 25.72  ? 44   GLY A CA  1 
ATOM   318  C C   . GLY A 1 44  ? 19.523 -15.354 2.698   1.00 18.44  ? 44   GLY A C   1 
ATOM   319  O O   . GLY A 1 44  ? 18.577 -14.892 2.070   1.00 19.37  ? 44   GLY A O   1 
ATOM   320  N N   . PHE A 1 45  ? 20.273 -16.351 2.240   1.00 18.32  ? 45   PHE A N   1 
ATOM   321  C CA  . PHE A 1 45  ? 20.224 -16.789 0.834   1.00 20.14  ? 45   PHE A CA  1 
ATOM   322  C C   . PHE A 1 45  ? 20.376 -18.307 0.797   1.00 18.63  ? 45   PHE A C   1 
ATOM   323  O O   . PHE A 1 45  ? 21.419 -18.839 1.194   1.00 23.24  ? 45   PHE A O   1 
ATOM   324  C CB  . PHE A 1 45  ? 21.380 -16.121 0.091   1.00 22.45  ? 45   PHE A CB  1 
ATOM   325  C CG  . PHE A 1 45  ? 21.449 -16.423 -1.388  1.00 17.64  ? 45   PHE A CG  1 
ATOM   326  C CD1 . PHE A 1 45  ? 20.360 -16.224 -2.210  1.00 23.17  ? 45   PHE A CD1 1 
ATOM   327  C CD2 . PHE A 1 45  ? 22.654 -16.850 -1.952  1.00 18.81  ? 45   PHE A CD2 1 
ATOM   328  C CE1 . PHE A 1 45  ? 20.447 -16.474 -3.581  1.00 28.03  ? 45   PHE A CE1 1 
ATOM   329  C CE2 . PHE A 1 45  ? 22.759 -17.096 -3.318  1.00 22.63  ? 45   PHE A CE2 1 
ATOM   330  C CZ  . PHE A 1 45  ? 21.652 -16.902 -4.137  1.00 17.29  ? 45   PHE A CZ  1 
ATOM   331  N N   . HIS A 1 46  ? 19.347 -19.019 0.355   1.00 24.82  ? 46   HIS A N   1 
ATOM   332  C CA  . HIS A 1 46  ? 19.475 -20.480 0.403   1.00 25.69  ? 46   HIS A CA  1 
ATOM   333  C C   . HIS A 1 46  ? 18.413 -21.200 -0.392  1.00 19.66  ? 46   HIS A C   1 
ATOM   334  O O   . HIS A 1 46  ? 17.400 -20.611 -0.777  1.00 18.77  ? 46   HIS A O   1 
ATOM   335  C CB  . HIS A 1 46  ? 19.456 -20.980 1.849   1.00 39.82  ? 46   HIS A CB  1 
ATOM   336  C CG  . HIS A 1 46  ? 18.493 -20.243 2.723   1.00 35.26  ? 46   HIS A CG  1 
ATOM   337  N ND1 . HIS A 1 46  ? 18.901 -19.358 3.700   1.00 30.40  ? 46   HIS A ND1 1 
ATOM   338  C CD2 . HIS A 1 46  ? 17.140 -20.258 2.766   1.00 34.58  ? 46   HIS A CD2 1 
ATOM   339  C CE1 . HIS A 1 46  ? 17.839 -18.866 4.312   1.00 36.86  ? 46   HIS A CE1 1 
ATOM   340  N NE2 . HIS A 1 46  ? 16.758 -19.388 3.759   1.00 36.84  ? 46   HIS A NE2 1 
ATOM   341  N N   . VAL A 1 47  ? 18.659 -22.481 -0.652  1.00 19.77  ? 47   VAL A N   1 
ATOM   342  C CA  . VAL A 1 47  ? 17.681 -23.307 -1.340  1.00 17.70  ? 47   VAL A CA  1 
ATOM   343  C C   . VAL A 1 47  ? 16.753 -23.870 -0.286  1.00 28.93  ? 47   VAL A C   1 
ATOM   344  O O   . VAL A 1 47  ? 17.216 -24.406 0.728   1.00 26.01  ? 47   VAL A O   1 
ATOM   345  C CB  . VAL A 1 47  ? 18.346 -24.447 -2.129  1.00 22.48  ? 47   VAL A CB  1 
ATOM   346  C CG1 . VAL A 1 47  ? 17.287 -25.364 -2.728  1.00 28.81  ? 47   VAL A CG1 1 
ATOM   347  C CG2 . VAL A 1 47  ? 19.234 -23.876 -3.252  1.00 20.48  ? 47   VAL A CG2 1 
ATOM   348  N N   . HIS A 1 48  ? 15.447 -23.739 -0.517  1.00 24.99  ? 48   HIS A N   1 
ATOM   349  C CA  . HIS A 1 48  ? 14.446 -24.246 0.423   1.00 22.95  ? 48   HIS A CA  1 
ATOM   350  C C   . HIS A 1 48  ? 14.635 -25.735 0.645   1.00 28.03  ? 48   HIS A C   1 
ATOM   351  O O   . HIS A 1 48  ? 14.755 -26.502 -0.314  1.00 38.24  ? 48   HIS A O   1 
ATOM   352  C CB  . HIS A 1 48  ? 13.022 -23.960 -0.081  1.00 28.25  ? 48   HIS A CB  1 
ATOM   353  C CG  . HIS A 1 48  ? 11.943 -24.615 0.737   1.00 31.76  ? 48   HIS A CG  1 
ATOM   354  N ND1 . HIS A 1 48  ? 11.598 -24.179 1.999   1.00 30.51  ? 48   HIS A ND1 1 
ATOM   355  C CD2 . HIS A 1 48  ? 11.125 -25.659 0.463   1.00 35.42  ? 48   HIS A CD2 1 
ATOM   356  C CE1 . HIS A 1 48  ? 10.618 -24.931 2.470   1.00 30.86  ? 48   HIS A CE1 1 
ATOM   357  N NE2 . HIS A 1 48  ? 10.315 -25.840 1.561   1.00 31.44  ? 48   HIS A NE2 1 
ATOM   358  N N   . GLY A 1 49  ? 14.646 -26.137 1.912   1.00 33.84  ? 49   GLY A N   1 
ATOM   359  C CA  . GLY A 1 49  ? 14.857 -27.526 2.269   1.00 38.73  ? 49   GLY A CA  1 
ATOM   360  C C   . GLY A 1 49  ? 16.220 -27.723 2.902   1.00 52.18  ? 49   GLY A C   1 
ATOM   361  O O   . GLY A 1 49  ? 16.889 -26.755 3.277   1.00 52.19  ? 49   GLY A O   1 
ATOM   362  N N   . ALA A 1 50  ? 16.630 -28.983 3.015   1.00 59.25  ? 50   ALA A N   1 
ATOM   363  C CA  . ALA A 1 50  ? 17.925 -29.336 3.584   1.00 60.66  ? 50   ALA A CA  1 
ATOM   364  C C   . ALA A 1 50  ? 19.050 -29.269 2.546   1.00 63.46  ? 50   ALA A C   1 
ATOM   365  O O   . ALA A 1 50  ? 18.816 -29.448 1.351   1.00 64.64  ? 50   ALA A O   1 
ATOM   366  C CB  . ALA A 1 50  ? 17.859 -30.732 4.205   1.00 61.48  ? 50   ALA A CB  1 
ATOM   367  N N   . GLY A 1 51  ? 20.267 -29.003 3.015   1.00 68.70  ? 51   GLY A N   1 
ATOM   368  C CA  . GLY A 1 51  ? 21.463 -29.109 2.192   1.00 63.81  ? 51   GLY A CA  1 
ATOM   369  C C   . GLY A 1 51  ? 21.698 -27.965 1.226   1.00 62.27  ? 51   GLY A C   1 
ATOM   370  O O   . GLY A 1 51  ? 22.565 -28.043 0.357   1.00 67.72  ? 51   GLY A O   1 
ATOM   371  N N   . GLY A 1 52  ? 20.941 -26.888 1.383   1.00 43.55  ? 52   GLY A N   1 
ATOM   372  C CA  . GLY A 1 52  ? 20.991 -25.802 0.419   1.00 41.21  ? 52   GLY A CA  1 
ATOM   373  C C   . GLY A 1 52  ? 21.385 -24.429 0.938   1.00 40.79  ? 52   GLY A C   1 
ATOM   374  O O   . GLY A 1 52  ? 21.052 -23.422 0.313   1.00 29.27  ? 52   GLY A O   1 
ATOM   375  N N   . ASP A 1 53  ? 22.101 -24.370 2.062   1.00 47.16  ? 53   ASP A N   1 
ATOM   376  C CA  . ASP A 1 53  ? 22.497 -23.073 2.616   1.00 48.29  ? 53   ASP A CA  1 
ATOM   377  C C   . ASP A 1 53  ? 23.557 -22.387 1.749   1.00 39.00  ? 53   ASP A C   1 
ATOM   378  O O   . ASP A 1 53  ? 24.612 -22.950 1.469   1.00 47.07  ? 53   ASP A O   1 
ATOM   379  C CB  . ASP A 1 53  ? 23.000 -23.210 4.057   1.00 52.36  ? 53   ASP A CB  1 
ATOM   380  C CG  . ASP A 1 53  ? 22.944 -21.895 4.823   1.00 60.04  ? 53   ASP A CG  1 
ATOM   381  O OD1 . ASP A 1 53  ? 23.183 -20.830 4.218   1.00 55.14  ? 53   ASP A OD1 1 
ATOM   382  O OD2 . ASP A 1 53  ? 22.650 -21.924 6.036   1.00 71.19  ? 53   ASP A OD2 1 
ATOM   383  N N   . LEU A 1 54  ? 23.276 -21.164 1.329   1.00 32.00  ? 54   LEU A N   1 
ATOM   384  C CA  . LEU A 1 54  ? 24.257 -20.409 0.570   1.00 29.36  ? 54   LEU A CA  1 
ATOM   385  C C   . LEU A 1 54  ? 24.749 -19.193 1.358   1.00 30.69  ? 54   LEU A C   1 
ATOM   386  O O   . LEU A 1 54  ? 25.294 -18.259 0.790   1.00 34.85  ? 54   LEU A O   1 
ATOM   387  C CB  . LEU A 1 54  ? 23.689 -20.011 -0.792  1.00 28.22  ? 54   LEU A CB  1 
ATOM   388  C CG  . LEU A 1 54  ? 23.178 -21.195 -1.612  1.00 33.31  ? 54   LEU A CG  1 
ATOM   389  C CD1 . LEU A 1 54  ? 22.498 -20.708 -2.876  1.00 27.07  ? 54   LEU A CD1 1 
ATOM   390  C CD2 . LEU A 1 54  ? 24.313 -22.159 -1.937  1.00 41.57  ? 54   LEU A CD2 1 
ATOM   391  N N   . GLY A 1 55  ? 24.548 -19.214 2.673   1.00 27.20  ? 55   GLY A N   1 
ATOM   392  C CA  . GLY A 1 55  ? 25.027 -18.145 3.528   1.00 30.38  ? 55   GLY A CA  1 
ATOM   393  C C   . GLY A 1 55  ? 24.226 -16.864 3.392   1.00 35.82  ? 55   GLY A C   1 
ATOM   394  O O   . GLY A 1 55  ? 22.995 -16.888 3.352   1.00 28.97  ? 55   GLY A O   1 
ATOM   395  N N   . ASN A 1 56  ? 24.931 -15.740 3.347   1.00 23.25  ? 56   ASN A N   1 
ATOM   396  C CA  . ASN A 1 56  ? 24.303 -14.441 3.173   1.00 28.03  ? 56   ASN A CA  1 
ATOM   397  C C   . ASN A 1 56  ? 24.825 -13.787 1.916   1.00 29.64  ? 56   ASN A C   1 
ATOM   398  O O   . ASN A 1 56  ? 25.983 -13.992 1.535   1.00 25.09  ? 56   ASN A O   1 
ATOM   399  C CB  . ASN A 1 56  ? 24.619 -13.520 4.356   1.00 28.87  ? 56   ASN A CB  1 
ATOM   400  C CG  . ASN A 1 56  ? 23.957 -13.967 5.639   1.00 37.42  ? 56   ASN A CG  1 
ATOM   401  O OD1 . ASN A 1 56  ? 22.769 -14.294 5.659   1.00 33.78  ? 56   ASN A OD1 1 
ATOM   402  N ND2 . ASN A 1 56  ? 24.725 -13.984 6.727   1.00 33.26  ? 56   ASN A ND2 1 
ATOM   403  N N   . VAL A 1 57  ? 23.975 -13.003 1.267   1.00 26.16  ? 57   VAL A N   1 
ATOM   404  C CA  . VAL A 1 57  ? 24.476 -12.067 0.271   1.00 32.40  ? 57   VAL A CA  1 
ATOM   405  C C   . VAL A 1 57  ? 24.516 -10.670 0.875   1.00 31.25  ? 57   VAL A C   1 
ATOM   406  O O   . VAL A 1 57  ? 23.808 -10.379 1.845   1.00 24.69  ? 57   VAL A O   1 
ATOM   407  C CB  . VAL A 1 57  ? 23.639 -12.058 -1.007  1.00 26.41  ? 57   VAL A CB  1 
ATOM   408  C CG1 . VAL A 1 57  ? 23.581 -13.460 -1.592  1.00 30.01  ? 57   VAL A CG1 1 
ATOM   409  C CG2 . VAL A 1 57  ? 22.216 -11.487 -0.757  1.00 17.33  ? 57   VAL A CG2 1 
ATOM   410  N N   . THR A 1 58  ? 25.347 -9.807  0.303   1.00 25.11  ? 58   THR A N   1 
ATOM   411  C CA  . THR A 1 58  ? 25.489 -8.452  0.827   1.00 26.76  ? 58   THR A CA  1 
ATOM   412  C C   . THR A 1 58  ? 24.979 -7.444  -0.184  1.00 25.12  ? 58   THR A C   1 
ATOM   413  O O   . THR A 1 58  ? 25.508 -7.340  -1.288  1.00 23.72  ? 58   THR A O   1 
ATOM   414  C CB  . THR A 1 58  ? 26.957 -8.140  1.173   1.00 28.11  ? 58   THR A CB  1 
ATOM   415  O OG1 . THR A 1 58  ? 27.393 -9.035  2.198   1.00 27.84  ? 58   THR A OG1 1 
ATOM   416  C CG2 . THR A 1 58  ? 27.114 -6.698  1.665   1.00 29.43  ? 58   THR A CG2 1 
ATOM   417  N N   . ALA A 1 59  ? 23.928 -6.721  0.181   1.00 24.26  ? 59   ALA A N   1 
ATOM   418  C CA  . ALA A 1 59  ? 23.409 -5.664  -0.663  1.00 19.61  ? 59   ALA A CA  1 
ATOM   419  C C   . ALA A 1 59  ? 24.092 -4.351  -0.312  1.00 25.33  ? 59   ALA A C   1 
ATOM   420  O O   . ALA A 1 59  ? 24.242 -4.026  0.867   1.00 23.41  ? 59   ALA A O   1 
ATOM   421  C CB  . ALA A 1 59  ? 21.891 -5.555  -0.511  1.00 21.19  ? 59   ALA A CB  1 
ATOM   422  N N   . ASP A 1 60  ? 24.525 -3.621  -1.339  1.00 22.77  ? 60   ASP A N   1 
ATOM   423  C CA  . ASP A 1 60  ? 25.210 -2.346  -1.159  1.00 26.14  ? 60   ASP A CA  1 
ATOM   424  C C   . ASP A 1 60  ? 24.223 -1.174  -1.011  1.00 30.12  ? 60   ASP A C   1 
ATOM   425  O O   . ASP A 1 60  ? 23.019 -1.386  -0.871  1.00 27.62  ? 60   ASP A O   1 
ATOM   426  C CB  . ASP A 1 60  ? 26.232 -2.099  -2.291  1.00 25.80  ? 60   ASP A CB  1 
ATOM   427  C CG  . ASP A 1 60  ? 25.589 -1.919  -3.671  1.00 31.95  ? 60   ASP A CG  1 
ATOM   428  O OD1 . ASP A 1 60  ? 24.391 -1.574  -3.779  1.00 27.57  ? 60   ASP A OD1 1 
ATOM   429  O OD2 . ASP A 1 60  ? 26.304 -2.111  -4.678  1.00 35.67  ? 60   ASP A OD2 1 
ATOM   430  N N   . LYS A 1 61  ? 24.732 0.057   -1.052  1.00 25.87  ? 61   LYS A N   1 
ATOM   431  C CA  . LYS A 1 61  ? 23.899 1.239   -0.821  1.00 27.31  ? 61   LYS A CA  1 
ATOM   432  C C   . LYS A 1 61  ? 22.922 1.536   -1.951  1.00 26.49  ? 61   LYS A C   1 
ATOM   433  O O   . LYS A 1 61  ? 22.048 2.380   -1.804  1.00 29.97  ? 61   LYS A O   1 
ATOM   434  C CB  . LYS A 1 61  ? 24.762 2.482   -0.508  1.00 30.02  ? 61   LYS A CB  1 
ATOM   435  C CG  . LYS A 1 61  ? 25.292 2.507   0.912   1.00 50.17  ? 61   LYS A CG  1 
ATOM   436  C CD  . LYS A 1 61  ? 25.478 3.925   1.435   1.00 52.72  ? 61   LYS A CD  1 
ATOM   437  C CE  . LYS A 1 61  ? 25.578 3.935   2.946   1.00 54.19  ? 61   LYS A CE  1 
ATOM   438  N NZ  . LYS A 1 61  ? 26.792 3.224   3.433   1.00 53.23  ? 61   LYS A NZ  1 
ATOM   439  N N   . ASP A 1 62  ? 23.073 0.846   -3.076  1.00 24.75  ? 62   ASP A N   1 
ATOM   440  C CA  . ASP A 1 62  ? 22.116 0.929   -4.171  1.00 25.90  ? 62   ASP A CA  1 
ATOM   441  C C   . ASP A 1 62  ? 21.151 -0.266  -4.148  1.00 22.11  ? 62   ASP A C   1 
ATOM   442  O O   . ASP A 1 62  ? 20.357 -0.458  -5.074  1.00 22.97  ? 62   ASP A O   1 
ATOM   443  C CB  . ASP A 1 62  ? 22.828 0.960   -5.531  1.00 28.05  ? 62   ASP A CB  1 
ATOM   444  C CG  . ASP A 1 62  ? 23.811 2.102   -5.665  1.00 33.40  ? 62   ASP A CG  1 
ATOM   445  O OD1 . ASP A 1 62  ? 23.597 3.169   -5.044  1.00 32.14  ? 62   ASP A OD1 1 
ATOM   446  O OD2 . ASP A 1 62  ? 24.808 1.932   -6.404  1.00 34.96  ? 62   ASP A OD2 1 
ATOM   447  N N   . GLY A 1 63  ? 21.223 -1.076  -3.101  1.00 22.85  ? 63   GLY A N   1 
ATOM   448  C CA  . GLY A 1 63  ? 20.323 -2.209  -2.980  1.00 19.81  ? 63   GLY A CA  1 
ATOM   449  C C   . GLY A 1 63  ? 20.699 -3.381  -3.864  1.00 25.02  ? 63   GLY A C   1 
ATOM   450  O O   . GLY A 1 63  ? 19.878 -4.262  -4.126  1.00 21.22  ? 63   GLY A O   1 
ATOM   451  N N   . VAL A 1 64  ? 21.953 -3.403  -4.306  1.00 22.63  ? 64   VAL A N   1 
ATOM   452  C CA  . VAL A 1 64  ? 22.417 -4.443  -5.212  1.00 22.28  ? 64   VAL A CA  1 
ATOM   453  C C   . VAL A 1 64  ? 23.382 -5.398  -4.521  1.00 22.97  ? 64   VAL A C   1 
ATOM   454  O O   . VAL A 1 64  ? 24.333 -4.976  -3.858  1.00 21.28  ? 64   VAL A O   1 
ATOM   455  C CB  . VAL A 1 64  ? 23.061 -3.847  -6.489  1.00 25.46  ? 64   VAL A CB  1 
ATOM   456  C CG1 . VAL A 1 64  ? 23.558 -4.973  -7.405  1.00 23.03  ? 64   VAL A CG1 1 
ATOM   457  C CG2 . VAL A 1 64  ? 22.043 -2.964  -7.233  1.00 23.01  ? 64   VAL A CG2 1 
ATOM   458  N N   . ALA A 1 65  ? 23.106 -6.691  -4.663  1.00 22.90  ? 65   ALA A N   1 
ATOM   459  C CA  . ALA A 1 65  ? 23.956 -7.735  -4.112  1.00 26.27  ? 65   ALA A CA  1 
ATOM   460  C C   . ALA A 1 65  ? 24.509 -8.557  -5.256  1.00 26.99  ? 65   ALA A C   1 
ATOM   461  O O   . ALA A 1 65  ? 23.756 -9.204  -5.985  1.00 26.17  ? 65   ALA A O   1 
ATOM   462  C CB  . ALA A 1 65  ? 23.157 -8.633  -3.140  1.00 18.64  ? 65   ALA A CB  1 
ATOM   463  N N   . ASP A 1 66  ? 25.823 -8.519  -5.432  1.00 17.08  ? 66   ASP A N   1 
ATOM   464  C CA  . ASP A 1 66  ? 26.446 -9.363  -6.430  1.00 19.07  ? 66   ASP A CA  1 
ATOM   465  C C   . ASP A 1 66  ? 26.755 -10.706 -5.789  1.00 26.97  ? 66   ASP A C   1 
ATOM   466  O O   . ASP A 1 66  ? 27.162 -10.766 -4.623  1.00 29.10  ? 66   ASP A O   1 
ATOM   467  C CB  . ASP A 1 66  ? 27.704 -8.705  -6.968  1.00 18.77  ? 66   ASP A CB  1 
ATOM   468  C CG  . ASP A 1 66  ? 27.379 -7.568  -7.910  1.00 32.42  ? 66   ASP A CG  1 
ATOM   469  O OD1 . ASP A 1 66  ? 26.494 -7.764  -8.769  1.00 34.97  ? 66   ASP A OD1 1 
ATOM   470  O OD2 . ASP A 1 66  ? 27.968 -6.479  -7.769  1.00 36.64  ? 66   ASP A OD2 1 
ATOM   471  N N   . VAL A 1 67  ? 26.540 -11.779 -6.542  1.00 23.83  ? 67   VAL A N   1 
ATOM   472  C CA  . VAL A 1 67  ? 26.749 -13.122 -6.023  1.00 23.09  ? 67   VAL A CA  1 
ATOM   473  C C   . VAL A 1 67  ? 27.790 -13.865 -6.833  1.00 25.20  ? 67   VAL A C   1 
ATOM   474  O O   . VAL A 1 67  ? 27.696 -13.922 -8.060  1.00 27.60  ? 67   VAL A O   1 
ATOM   475  C CB  . VAL A 1 67  ? 25.427 -13.927 -6.009  1.00 24.85  ? 67   VAL A CB  1 
ATOM   476  C CG1 . VAL A 1 67  ? 25.625 -15.279 -5.309  1.00 23.72  ? 67   VAL A CG1 1 
ATOM   477  C CG2 . VAL A 1 67  ? 24.337 -13.135 -5.317  1.00 19.63  ? 67   VAL A CG2 1 
ATOM   478  N N   . SER A 1 68  ? 28.796 -14.420 -6.149  1.00 26.07  ? 68   SER A N   1 
ATOM   479  C CA  . SER A 1 68  ? 29.803 -15.243 -6.801  1.00 31.47  ? 68   SER A CA  1 
ATOM   480  C C   . SER A 1 68  ? 30.432 -16.246 -5.842  1.00 38.54  ? 68   SER A C   1 
ATOM   481  O O   . SER A 1 68  ? 31.467 -15.963 -5.233  1.00 35.12  ? 68   SER A O   1 
ATOM   482  C CB  . SER A 1 68  ? 30.910 -14.384 -7.404  1.00 40.49  ? 68   SER A CB  1 
ATOM   483  O OG  . SER A 1 68  ? 31.673 -15.169 -8.299  1.00 39.32  ? 68   SER A OG  1 
ATOM   484  N N   . ILE A 1 69  ? 29.820 -17.424 -5.776  1.00 34.42  ? 69   ILE A N   1 
ATOM   485  C CA  . ILE A 1 69  ? 30.077 -18.467 -4.782  1.00 34.97  ? 69   ILE A CA  1 
ATOM   486  C C   . ILE A 1 69  ? 30.445 -19.746 -5.499  1.00 42.02  ? 69   ILE A C   1 
ATOM   487  O O   . ILE A 1 69  ? 29.884 -20.050 -6.541  1.00 37.29  ? 69   ILE A O   1 
ATOM   488  C CB  . ILE A 1 69  ? 28.760 -18.803 -4.047  1.00 41.69  ? 69   ILE A CB  1 
ATOM   489  C CG1 . ILE A 1 69  ? 28.352 -17.701 -3.081  1.00 47.96  ? 69   ILE A CG1 1 
ATOM   490  C CG2 . ILE A 1 69  ? 28.839 -20.124 -3.303  1.00 56.37  ? 69   ILE A CG2 1 
ATOM   491  C CD1 . ILE A 1 69  ? 26.972 -17.946 -2.515  1.00 52.46  ? 69   ILE A CD1 1 
ATOM   492  N N   . GLU A 1 70  ? 31.370 -20.520 -4.948  1.00 46.59  ? 70   GLU A N   1 
ATOM   493  C CA  . GLU A 1 70  ? 31.477 -21.907 -5.360  1.00 45.30  ? 70   GLU A CA  1 
ATOM   494  C C   . GLU A 1 70  ? 31.060 -22.765 -4.176  1.00 48.83  ? 70   GLU A C   1 
ATOM   495  O O   . GLU A 1 70  ? 31.526 -22.560 -3.058  1.00 51.06  ? 70   GLU A O   1 
ATOM   496  C CB  . GLU A 1 70  ? 32.889 -22.254 -5.832  1.00 49.43  ? 70   GLU A CB  1 
ATOM   497  C CG  . GLU A 1 70  ? 33.008 -23.655 -6.402  1.00 60.13  ? 70   GLU A CG  1 
ATOM   498  C CD  . GLU A 1 70  ? 33.969 -23.738 -7.578  1.00 77.46  ? 70   GLU A CD  1 
ATOM   499  O OE1 . GLU A 1 70  ? 33.903 -22.864 -8.469  1.00 82.40  ? 70   GLU A OE1 1 
ATOM   500  O OE2 . GLU A 1 70  ? 34.796 -24.676 -7.610  1.00 85.20  ? 70   GLU A OE2 1 
ATOM   501  N N   . ASP A 1 71  ? 30.153 -23.702 -4.414  1.00 42.84  ? 71   ASP A N   1 
ATOM   502  C CA  . ASP A 1 71  ? 29.667 -24.551 -3.345  1.00 41.94  ? 71   ASP A CA  1 
ATOM   503  C C   . ASP A 1 71  ? 29.743 -26.023 -3.744  1.00 44.71  ? 71   ASP A C   1 
ATOM   504  O O   . ASP A 1 71  ? 29.299 -26.406 -4.825  1.00 38.90  ? 71   ASP A O   1 
ATOM   505  C CB  . ASP A 1 71  ? 28.240 -24.159 -2.965  1.00 46.55  ? 71   ASP A CB  1 
ATOM   506  C CG  . ASP A 1 71  ? 27.731 -24.930 -1.775  1.00 53.75  ? 71   ASP A CG  1 
ATOM   507  O OD1 . ASP A 1 71  ? 27.345 -26.095 -1.969  1.00 50.67  ? 71   ASP A OD1 1 
ATOM   508  O OD2 . ASP A 1 71  ? 27.726 -24.386 -0.648  1.00 65.05  ? 71   ASP A OD2 1 
ATOM   509  N N   . SER A 1 72  ? 30.304 -26.849 -2.869  1.00 49.19  ? 72   SER A N   1 
ATOM   510  C CA  . SER A 1 72  ? 30.513 -28.259 -3.186  1.00 53.91  ? 72   SER A CA  1 
ATOM   511  C C   . SER A 1 72  ? 29.499 -29.174 -2.497  1.00 53.77  ? 72   SER A C   1 
ATOM   512  O O   . SER A 1 72  ? 29.547 -30.397 -2.641  1.00 58.48  ? 72   SER A O   1 
ATOM   513  C CB  . SER A 1 72  ? 31.939 -28.664 -2.826  1.00 53.95  ? 72   SER A CB  1 
ATOM   514  O OG  . SER A 1 72  ? 32.862 -27.713 -3.340  1.00 58.76  ? 72   SER A OG  1 
ATOM   515  N N   . VAL A 1 73  ? 28.592 -28.558 -1.748  1.00 45.03  ? 73   VAL A N   1 
ATOM   516  C CA  . VAL A 1 73  ? 27.493 -29.238 -1.070  1.00 48.19  ? 73   VAL A CA  1 
ATOM   517  C C   . VAL A 1 73  ? 26.316 -29.510 -2.012  1.00 44.20  ? 73   VAL A C   1 
ATOM   518  O O   . VAL A 1 73  ? 25.817 -30.632 -2.088  1.00 48.48  ? 73   VAL A O   1 
ATOM   519  C CB  . VAL A 1 73  ? 26.963 -28.363 0.089   1.00 52.79  ? 73   VAL A CB  1 
ATOM   520  C CG1 . VAL A 1 73  ? 25.656 -28.912 0.635   1.00 52.11  ? 73   VAL A CG1 1 
ATOM   521  C CG2 . VAL A 1 73  ? 28.008 -28.209 1.170   1.00 52.26  ? 73   VAL A CG2 1 
ATOM   522  N N   . ILE A 1 74  ? 25.872 -28.473 -2.722  1.00 34.29  ? 74   ILE A N   1 
ATOM   523  C CA  . ILE A 1 74  ? 24.711 -28.578 -3.601  1.00 33.22  ? 74   ILE A CA  1 
ATOM   524  C C   . ILE A 1 74  ? 25.111 -29.273 -4.893  1.00 34.49  ? 74   ILE A C   1 
ATOM   525  O O   . ILE A 1 74  ? 26.294 -29.364 -5.215  1.00 33.81  ? 74   ILE A O   1 
ATOM   526  C CB  . ILE A 1 74  ? 24.102 -27.189 -3.938  1.00 35.83  ? 74   ILE A CB  1 
ATOM   527  C CG1 . ILE A 1 74  ? 25.194 -26.231 -4.434  1.00 30.31  ? 74   ILE A CG1 1 
ATOM   528  C CG2 . ILE A 1 74  ? 23.381 -26.609 -2.732  1.00 32.24  ? 74   ILE A CG2 1 
ATOM   529  C CD1 . ILE A 1 74  ? 24.650 -24.933 -5.011  1.00 25.34  ? 74   ILE A CD1 1 
ATOM   530  N N   . SER A 1 75  ? 24.120 -29.756 -5.630  1.00 30.79  ? 75   SER A N   1 
ATOM   531  C CA  . SER A 1 75  ? 24.379 -30.429 -6.892  1.00 35.64  ? 75   SER A CA  1 
ATOM   532  C C   . SER A 1 75  ? 23.252 -30.172 -7.876  1.00 34.34  ? 75   SER A C   1 
ATOM   533  O O   . SER A 1 75  ? 22.124 -29.911 -7.470  1.00 30.00  ? 75   SER A O   1 
ATOM   534  C CB  . SER A 1 75  ? 24.528 -31.931 -6.663  1.00 35.59  ? 75   SER A CB  1 
ATOM   535  O OG  . SER A 1 75  ? 24.921 -32.575 -7.861  1.00 39.99  ? 75   SER A OG  1 
ATOM   536  N N   . LEU A 1 76  ? 23.556 -30.253 -9.167  1.00 36.02  ? 76   LEU A N   1 
ATOM   537  C CA  . LEU A 1 76  ? 22.535 -30.108 -10.199 1.00 34.30  ? 76   LEU A CA  1 
ATOM   538  C C   . LEU A 1 76  ? 22.116 -31.469 -10.758 1.00 40.97  ? 76   LEU A C   1 
ATOM   539  O O   . LEU A 1 76  ? 21.324 -31.556 -11.703 1.00 38.57  ? 76   LEU A O   1 
ATOM   540  C CB  . LEU A 1 76  ? 23.043 -29.213 -11.333 1.00 34.33  ? 76   LEU A CB  1 
ATOM   541  C CG  . LEU A 1 76  ? 23.565 -27.835 -10.947 1.00 36.02  ? 76   LEU A CG  1 
ATOM   542  C CD1 . LEU A 1 76  ? 23.810 -26.992 -12.201 1.00 30.74  ? 76   LEU A CD1 1 
ATOM   543  C CD2 . LEU A 1 76  ? 22.584 -27.143 -10.025 1.00 36.26  ? 76   LEU A CD2 1 
ATOM   544  N N   . SER A 1 77  ? 22.674 -32.531 -10.183 1.00 33.68  ? 77   SER A N   1 
ATOM   545  C CA  . SER A 1 77  ? 22.304 -33.881 -10.554 1.00 36.24  ? 77   SER A CA  1 
ATOM   546  C C   . SER A 1 77  ? 22.195 -34.692 -9.269  1.00 48.82  ? 77   SER A C   1 
ATOM   547  O O   . SER A 1 77  ? 22.533 -34.193 -8.193  1.00 50.59  ? 77   SER A O   1 
ATOM   548  C CB  . SER A 1 77  ? 23.360 -34.483 -11.478 1.00 55.18  ? 77   SER A CB  1 
ATOM   549  O OG  . SER A 1 77  ? 24.624 -34.528 -10.837 1.00 52.00  ? 77   SER A OG  1 
ATOM   550  N N   . GLY A 1 78  ? 21.723 -35.931 -9.376  1.00 58.01  ? 78   GLY A N   1 
ATOM   551  C CA  . GLY A 1 78  ? 21.638 -36.814 -8.224  1.00 58.95  ? 78   GLY A CA  1 
ATOM   552  C C   . GLY A 1 78  ? 20.352 -36.641 -7.443  1.00 60.62  ? 78   GLY A C   1 
ATOM   553  O O   . GLY A 1 78  ? 19.448 -35.910 -7.868  1.00 55.61  ? 78   GLY A O   1 
ATOM   554  N N   . ASP A 1 79  ? 20.277 -37.303 -6.292  1.00 72.04  ? 79   ASP A N   1 
ATOM   555  C CA  . ASP A 1 79  ? 19.052 -37.348 -5.494  1.00 77.40  ? 79   ASP A CA  1 
ATOM   556  C C   . ASP A 1 79  ? 18.672 -36.003 -4.878  1.00 69.97  ? 79   ASP A C   1 
ATOM   557  O O   . ASP A 1 79  ? 17.511 -35.608 -4.918  1.00 69.37  ? 79   ASP A O   1 
ATOM   558  C CB  . ASP A 1 79  ? 19.135 -38.444 -4.419  1.00 94.52  ? 79   ASP A CB  1 
ATOM   559  C CG  . ASP A 1 79  ? 20.429 -38.390 -3.616  1.00 105.37 ? 79   ASP A CG  1 
ATOM   560  O OD1 . ASP A 1 79  ? 21.438 -37.863 -4.133  1.00 105.07 ? 79   ASP A OD1 1 
ATOM   561  O OD2 . ASP A 1 79  ? 20.437 -38.889 -2.468  1.00 111.00 ? 79   ASP A OD2 1 
ATOM   562  N N   . HIS A 1 80  ? 19.641 -35.295 -4.313  1.00 67.15  ? 80   HIS A N   1 
ATOM   563  C CA  . HIS A 1 80  ? 19.349 -33.980 -3.748  1.00 68.72  ? 80   HIS A CA  1 
ATOM   564  C C   . HIS A 1 80  ? 19.682 -32.844 -4.716  1.00 57.32  ? 80   HIS A C   1 
ATOM   565  O O   . HIS A 1 80  ? 20.121 -31.770 -4.298  1.00 55.48  ? 80   HIS A O   1 
ATOM   566  C CB  . HIS A 1 80  ? 20.056 -33.782 -2.404  1.00 79.33  ? 80   HIS A CB  1 
ATOM   567  C CG  . HIS A 1 80  ? 19.523 -34.655 -1.311  1.00 88.44  ? 80   HIS A CG  1 
ATOM   568  N ND1 . HIS A 1 80  ? 19.821 -35.998 -1.220  0.48 93.27  ? 80   HIS A ND1 1 
ATOM   569  C CD2 . HIS A 1 80  ? 18.703 -34.380 -0.269  1.00 89.41  ? 80   HIS A CD2 1 
ATOM   570  C CE1 . HIS A 1 80  ? 19.212 -36.512 -0.166  1.00 96.80  ? 80   HIS A CE1 1 
ATOM   571  N NE2 . HIS A 1 80  ? 18.528 -35.551 0.429   1.00 94.47  ? 80   HIS A NE2 1 
ATOM   572  N N   . SER A 1 81  ? 19.472 -33.095 -6.007  1.00 47.78  ? 81   SER A N   1 
ATOM   573  C CA  . SER A 1 81  ? 19.617 -32.062 -7.029  1.00 37.95  ? 81   SER A CA  1 
ATOM   574  C C   . SER A 1 81  ? 18.764 -30.876 -6.647  1.00 33.00  ? 81   SER A C   1 
ATOM   575  O O   . SER A 1 81  ? 17.639 -31.050 -6.182  1.00 42.82  ? 81   SER A O   1 
ATOM   576  C CB  . SER A 1 81  ? 19.165 -32.589 -8.388  1.00 32.89  ? 81   SER A CB  1 
ATOM   577  O OG  . SER A 1 81  ? 19.170 -31.550 -9.354  1.00 33.97  ? 81   SER A OG  1 
ATOM   578  N N   . ILE A 1 82  ? 19.282 -29.668 -6.842  1.00 31.03  ? 82   ILE A N   1 
ATOM   579  C CA  . ILE A 1 82  ? 18.497 -28.478 -6.530  1.00 25.95  ? 82   ILE A CA  1 
ATOM   580  C C   . ILE A 1 82  ? 17.568 -28.102 -7.681  1.00 22.89  ? 82   ILE A C   1 
ATOM   581  O O   . ILE A 1 82  ? 16.752 -27.187 -7.560  1.00 21.66  ? 82   ILE A O   1 
ATOM   582  C CB  . ILE A 1 82  ? 19.380 -27.301 -6.118  1.00 23.57  ? 82   ILE A CB  1 
ATOM   583  C CG1 . ILE A 1 82  ? 20.218 -26.810 -7.289  1.00 22.33  ? 82   ILE A CG1 1 
ATOM   584  C CG2 . ILE A 1 82  ? 20.300 -27.724 -4.973  1.00 32.70  ? 82   ILE A CG2 1 
ATOM   585  C CD1 . ILE A 1 82  ? 20.973 -25.571 -6.968  1.00 27.37  ? 82   ILE A CD1 1 
ATOM   586  N N   . ILE A 1 83  ? 17.675 -28.823 -8.794  1.00 25.67  ? 83   ILE A N   1 
ATOM   587  C CA  . ILE A 1 83  ? 16.805 -28.545 -9.932  1.00 23.92  ? 83   ILE A CA  1 
ATOM   588  C C   . ILE A 1 83  ? 15.368 -28.771 -9.484  1.00 20.33  ? 83   ILE A C   1 
ATOM   589  O O   . ILE A 1 83  ? 15.041 -29.827 -8.948  1.00 21.94  ? 83   ILE A O   1 
ATOM   590  C CB  . ILE A 1 83  ? 17.090 -29.479 -11.113 1.00 29.98  ? 83   ILE A CB  1 
ATOM   591  C CG1 . ILE A 1 83  ? 18.549 -29.344 -11.564 1.00 32.20  ? 83   ILE A CG1 1 
ATOM   592  C CG2 . ILE A 1 83  ? 16.124 -29.189 -12.266 1.00 26.36  ? 83   ILE A CG2 1 
ATOM   593  C CD1 . ILE A 1 83  ? 18.879 -27.971 -12.081 1.00 21.60  ? 83   ILE A CD1 1 
ATOM   594  N N   . GLY A 1 84  ? 14.525 -27.768 -9.692  1.00 18.34  ? 84   GLY A N   1 
ATOM   595  C CA  . GLY A 1 84  ? 13.120 -27.849 -9.317  1.00 20.39  ? 84   GLY A CA  1 
ATOM   596  C C   . GLY A 1 84  ? 12.842 -27.404 -7.888  1.00 20.69  ? 84   GLY A C   1 
ATOM   597  O O   . GLY A 1 84  ? 11.692 -27.409 -7.428  1.00 18.31  ? 84   GLY A O   1 
ATOM   598  N N   . ARG A 1 85  ? 13.894 -27.041 -7.166  1.00 17.86  ? 85   ARG A N   1 
ATOM   599  C CA  . ARG A 1 85  ? 13.724 -26.566 -5.794  1.00 17.54  ? 85   ARG A CA  1 
ATOM   600  C C   . ARG A 1 85  ? 13.677 -25.051 -5.830  1.00 17.86  ? 85   ARG A C   1 
ATOM   601  O O   . ARG A 1 85  ? 14.005 -24.445 -6.853  1.00 15.30  ? 85   ARG A O   1 
ATOM   602  C CB  . ARG A 1 85  ? 14.841 -27.100 -4.876  1.00 22.09  ? 85   ARG A CB  1 
ATOM   603  C CG  . ARG A 1 85  ? 14.646 -28.590 -4.548  1.00 27.79  ? 85   ARG A CG  1 
ATOM   604  C CD  . ARG A 1 85  ? 15.831 -29.205 -3.809  1.00 41.55  ? 85   ARG A CD  1 
ATOM   605  N NE  . ARG A 1 85  ? 16.086 -28.588 -2.509  1.00 52.07  ? 85   ARG A NE  1 
ATOM   606  C CZ  . ARG A 1 85  ? 17.076 -28.943 -1.692  1.00 55.60  ? 85   ARG A CZ  1 
ATOM   607  N NH1 . ARG A 1 85  ? 17.910 -29.919 -2.043  1.00 51.99  ? 85   ARG A NH1 1 
ATOM   608  N NH2 . ARG A 1 85  ? 17.233 -28.325 -0.524  1.00 54.81  ? 85   ARG A NH2 1 
ATOM   609  N N   . THR A 1 86  ? 13.252 -24.442 -4.727  1.00 15.60  ? 86   THR A N   1 
ATOM   610  C CA  . THR A 1 86  ? 13.030 -22.991 -4.698  1.00 14.30  ? 86   THR A CA  1 
ATOM   611  C C   . THR A 1 86  ? 14.209 -22.288 -4.025  1.00 15.32  ? 86   THR A C   1 
ATOM   612  O O   . THR A 1 86  ? 14.620 -22.655 -2.914  1.00 18.13  ? 86   THR A O   1 
ATOM   613  C CB  . THR A 1 86  ? 11.708 -22.635 -3.959  1.00 22.64  ? 86   THR A CB  1 
ATOM   614  O OG1 . THR A 1 86  ? 10.597 -23.148 -4.704  1.00 22.77  ? 86   THR A OG1 1 
ATOM   615  C CG2 . THR A 1 86  ? 11.546 -21.119 -3.800  1.00 19.79  ? 86   THR A CG2 1 
ATOM   616  N N   . LEU A 1 87  ? 14.754 -21.304 -4.729  1.00 14.27  ? 87   LEU A N   1 
ATOM   617  C CA  . LEU A 1 87  ? 15.813 -20.442 -4.217  1.00 15.09  ? 87   LEU A CA  1 
ATOM   618  C C   . LEU A 1 87  ? 15.138 -19.240 -3.553  1.00 15.54  ? 87   LEU A C   1 
ATOM   619  O O   . LEU A 1 87  ? 14.208 -18.642 -4.121  1.00 16.40  ? 87   LEU A O   1 
ATOM   620  C CB  . LEU A 1 87  ? 16.705 -19.969 -5.358  1.00 15.81  ? 87   LEU A CB  1 
ATOM   621  C CG  . LEU A 1 87  ? 17.896 -19.095 -4.923  1.00 18.86  ? 87   LEU A CG  1 
ATOM   622  C CD1 . LEU A 1 87  ? 18.860 -19.889 -4.057  1.00 18.35  ? 87   LEU A CD1 1 
ATOM   623  C CD2 . LEU A 1 87  ? 18.636 -18.531 -6.124  1.00 14.62  ? 87   LEU A CD2 1 
ATOM   624  N N   . VAL A 1 88  ? 15.556 -18.922 -2.331  1.00 15.57  ? 88   VAL A N   1 
ATOM   625  C CA  . VAL A 1 88  ? 14.964 -17.786 -1.634  1.00 13.40  ? 88   VAL A CA  1 
ATOM   626  C C   . VAL A 1 88  ? 16.026 -16.838 -1.094  1.00 14.04  ? 88   VAL A C   1 
ATOM   627  O O   . VAL A 1 88  ? 17.166 -17.255 -0.794  1.00 18.56  ? 88   VAL A O   1 
ATOM   628  C CB  . VAL A 1 88  ? 14.064 -18.239 -0.467  1.00 24.41  ? 88   VAL A CB  1 
ATOM   629  C CG1 . VAL A 1 88  ? 12.928 -19.168 -0.968  1.00 24.20  ? 88   VAL A CG1 1 
ATOM   630  C CG2 . VAL A 1 88  ? 14.890 -18.917 0.598   1.00 26.98  ? 88   VAL A CG2 1 
ATOM   631  N N   . VAL A 1 89  ? 15.643 -15.560 -1.008  1.00 14.80  ? 89   VAL A N   1 
ATOM   632  C CA  . VAL A 1 89  ? 16.421 -14.542 -0.284  1.00 18.39  ? 89   VAL A CA  1 
ATOM   633  C C   . VAL A 1 89  ? 15.480 -13.768 0.651   1.00 15.23  ? 89   VAL A C   1 
ATOM   634  O O   . VAL A 1 89  ? 14.373 -13.385 0.266   1.00 16.05  ? 89   VAL A O   1 
ATOM   635  C CB  . VAL A 1 89  ? 17.181 -13.571 -1.238  1.00 21.83  ? 89   VAL A CB  1 
ATOM   636  C CG1 . VAL A 1 89  ? 16.226 -12.905 -2.211  1.00 24.77  ? 89   VAL A CG1 1 
ATOM   637  C CG2 . VAL A 1 89  ? 17.980 -12.502 -0.440  1.00 17.19  ? 89   VAL A CG2 1 
ATOM   638  N N   . HIS A 1 90  ? 15.911 -13.597 1.892   1.00 18.61  ? 90   HIS A N   1 
ATOM   639  C CA  . HIS A 1 90  ? 15.152 -12.835 2.876   1.00 23.28  ? 90   HIS A CA  1 
ATOM   640  C C   . HIS A 1 90  ? 15.182 -11.368 2.499   1.00 27.43  ? 90   HIS A C   1 
ATOM   641  O O   . HIS A 1 90  ? 16.255 -10.808 2.300   1.00 23.77  ? 90   HIS A O   1 
ATOM   642  C CB  . HIS A 1 90  ? 15.755 -13.018 4.260   1.00 21.36  ? 90   HIS A CB  1 
ATOM   643  C CG  . HIS A 1 90  ? 15.417 -14.329 4.882   1.00 21.07  ? 90   HIS A CG  1 
ATOM   644  N ND1 . HIS A 1 90  ? 15.307 -14.500 6.243   1.00 30.50  ? 90   HIS A ND1 1 
ATOM   645  C CD2 . HIS A 1 90  ? 15.129 -15.528 4.327   1.00 20.77  ? 90   HIS A CD2 1 
ATOM   646  C CE1 . HIS A 1 90  ? 14.969 -15.750 6.502   1.00 35.85  ? 90   HIS A CE1 1 
ATOM   647  N NE2 . HIS A 1 90  ? 14.855 -16.397 5.357   1.00 26.07  ? 90   HIS A NE2 1 
ATOM   648  N N   . GLU A 1 91  ? 14.012 -10.741 2.403   1.00 18.57  ? 91   GLU A N   1 
ATOM   649  C CA  . GLU A 1 91  ? 13.967 -9.313  2.095   1.00 22.47  ? 91   GLU A CA  1 
ATOM   650  C C   . GLU A 1 91  ? 14.371 -8.484  3.296   1.00 24.11  ? 91   GLU A C   1 
ATOM   651  O O   . GLU A 1 91  ? 14.912 -7.395  3.143   1.00 28.76  ? 91   GLU A O   1 
ATOM   652  C CB  . GLU A 1 91  ? 12.589 -8.902  1.572   1.00 19.87  ? 91   GLU A CB  1 
ATOM   653  C CG  . GLU A 1 91  ? 12.327 -9.552  0.227   1.00 17.58  ? 91   GLU A CG  1 
ATOM   654  C CD  . GLU A 1 91  ? 11.001 -9.172  -0.399  1.00 28.07  ? 91   GLU A CD  1 
ATOM   655  O OE1 . GLU A 1 91  ? 10.044 -8.862  0.332   1.00 33.67  ? 91   GLU A OE1 1 
ATOM   656  O OE2 . GLU A 1 91  ? 10.928 -9.196  -1.640  1.00 23.63  ? 91   GLU A OE2 1 
ATOM   657  N N   . LYS A 1 92  ? 14.123 -9.014  4.493   1.00 23.25  ? 92   LYS A N   1 
ATOM   658  C CA  . LYS A 1 92  ? 14.567 -8.356  5.718   1.00 24.75  ? 92   LYS A CA  1 
ATOM   659  C C   . LYS A 1 92  ? 16.076 -8.545  5.876   1.00 24.29  ? 92   LYS A C   1 
ATOM   660  O O   . LYS A 1 92  ? 16.570 -9.669  5.836   1.00 30.06  ? 92   LYS A O   1 
ATOM   661  C CB  . LYS A 1 92  ? 13.834 -8.941  6.933   1.00 26.89  ? 92   LYS A CB  1 
ATOM   662  C CG  . LYS A 1 92  ? 14.112 -8.225  8.259   1.00 38.74  ? 92   LYS A CG  1 
ATOM   663  C CD  . LYS A 1 92  ? 13.349 -8.913  9.409   1.00 41.93  ? 92   LYS A CD  1 
ATOM   664  C CE  . LYS A 1 92  ? 13.145 -7.984  10.605  1.00 58.05  ? 92   LYS A CE  1 
ATOM   665  N NZ  . LYS A 1 92  ? 14.412 -7.619  11.303  1.00 65.49  ? 92   LYS A NZ  1 
ATOM   666  N N   . ALA A 1 93  ? 16.806 -7.452  6.060   1.00 31.72  ? 93   ALA A N   1 
ATOM   667  C CA  . ALA A 1 93  ? 18.242 -7.542  6.297   1.00 29.50  ? 93   ALA A CA  1 
ATOM   668  C C   . ALA A 1 93  ? 18.514 -8.181  7.646   1.00 31.87  ? 93   ALA A C   1 
ATOM   669  O O   . ALA A 1 93  ? 17.720 -8.039  8.579   1.00 30.46  ? 93   ALA A O   1 
ATOM   670  C CB  . ALA A 1 93  ? 18.882 -6.163  6.227   1.00 34.63  ? 93   ALA A CB  1 
ATOM   671  N N   . GLY A 1 94  ? 19.629 -8.895  7.749   1.00 32.29  ? 94   GLY A N   1 
ATOM   672  C CA  . GLY A 1 94  ? 20.066 -9.431  9.023   1.00 32.61  ? 94   GLY A CA  1 
ATOM   673  C C   . GLY A 1 94  ? 19.745 -10.893 9.243   1.00 38.42  ? 94   GLY A C   1 
ATOM   674  O O   . GLY A 1 94  ? 19.144 -11.548 8.402   1.00 40.38  ? 94   GLY A O   1 
ATOM   675  N N   . ALA A 1 95  ? 20.149 -11.406 10.398  1.00 35.66  ? 95   ALA A N   1 
ATOM   676  C CA  . ALA A 1 95  ? 19.982 -12.823 10.725  1.00 41.32  ? 95   ALA A CA  1 
ATOM   677  C C   . ALA A 1 95  ? 18.607 -13.132 11.301  1.00 39.11  ? 95   ALA A C   1 
ATOM   678  O O   . ALA A 1 95  ? 17.815 -12.230 11.585  1.00 42.86  ? 95   ALA A O   1 
ATOM   679  C CB  . ALA A 1 95  ? 21.077 -13.280 11.708  1.00 43.15  ? 95   ALA A CB  1 
ATOM   680  N N   . GLY A 1 96  ? 18.339 -14.419 11.485  1.00 35.11  ? 96   GLY A N   1 
ATOM   681  C CA  . GLY A 1 96  ? 17.061 -14.867 12.008  1.00 48.62  ? 96   GLY A CA  1 
ATOM   682  C C   . GLY A 1 96  ? 16.041 -15.209 10.935  1.00 49.23  ? 96   GLY A C   1 
ATOM   683  O O   . GLY A 1 96  ? 16.314 -15.118 9.725   1.00 36.75  ? 96   GLY A O   1 
ATOM   684  N N   . ALA A 1 97  ? 14.853 -15.605 11.380  1.00 48.96  ? 97   ALA A N   1 
ATOM   685  C CA  . ALA A 1 97  ? 13.765 -15.906 10.459  1.00 44.76  ? 97   ALA A CA  1 
ATOM   686  C C   . ALA A 1 97  ? 13.265 -14.652 9.737   1.00 45.84  ? 97   ALA A C   1 
ATOM   687  O O   . ALA A 1 97  ? 13.482 -13.526 10.184  1.00 50.26  ? 97   ALA A O   1 
ATOM   688  C CB  . ALA A 1 97  ? 12.608 -16.600 11.194  1.00 44.55  ? 97   ALA A CB  1 
ATOM   689  N N   . GLY A 1 98  ? 12.597 -14.867 8.612   1.00 42.95  ? 98   GLY A N   1 
ATOM   690  C CA  . GLY A 1 98  ? 11.940 -13.803 7.885   1.00 42.49  ? 98   GLY A CA  1 
ATOM   691  C C   . GLY A 1 98  ? 10.752 -14.393 7.154   1.00 49.18  ? 98   GLY A C   1 
ATOM   692  O O   . GLY A 1 98  ? 10.761 -15.579 6.809   1.00 44.71  ? 98   GLY A O   1 
ATOM   693  N N   . SER A 1 99  ? 9.728  -13.576 6.923   1.00 49.40  ? 99   SER A N   1 
ATOM   694  C CA  . SER A 1 99  ? 8.531  -14.045 6.231   1.00 45.50  ? 99   SER A CA  1 
ATOM   695  C C   . SER A 1 99  ? 8.452  -13.480 4.816   1.00 39.28  ? 99   SER A C   1 
ATOM   696  O O   . SER A 1 99  ? 7.854  -14.091 3.930   1.00 36.95  ? 99   SER A O   1 
ATOM   697  C CB  . SER A 1 99  ? 7.265  -13.703 7.029   1.00 47.28  ? 99   SER A CB  1 
ATOM   698  O OG  . SER A 1 99  ? 7.230  -12.326 7.377   1.00 53.62  ? 99   SER A OG  1 
ATOM   699  N N   . ARG A 1 100 ? 9.056  -12.315 4.605   1.00 34.29  ? 100  ARG A N   1 
ATOM   700  C CA  . ARG A 1 100 ? 9.042  -11.707 3.280   1.00 30.41  ? 100  ARG A CA  1 
ATOM   701  C C   . ARG A 1 100 ? 10.259 -12.157 2.506   1.00 22.58  ? 100  ARG A C   1 
ATOM   702  O O   . ARG A 1 100 ? 11.400 -11.860 2.887   1.00 24.19  ? 100  ARG A O   1 
ATOM   703  C CB  . ARG A 1 100 ? 9.007  -10.189 3.368   1.00 31.97  ? 100  ARG A CB  1 
ATOM   704  C CG  . ARG A 1 100 ? 7.732  -9.668  3.995   1.00 36.12  ? 100  ARG A CG  1 
ATOM   705  C CD  . ARG A 1 100 ? 7.796  -8.168  4.194   1.00 47.44  ? 100  ARG A CD  1 
ATOM   706  N NE  . ARG A 1 100 ? 7.187  -7.448  3.080   1.00 59.48  ? 100  ARG A NE  1 
ATOM   707  C CZ  . ARG A 1 100 ? 7.860  -6.778  2.147   1.00 63.05  ? 100  ARG A CZ  1 
ATOM   708  N NH1 . ARG A 1 100 ? 9.188  -6.715  2.179   1.00 61.62  ? 100  ARG A NH1 1 
ATOM   709  N NH2 . ARG A 1 100 ? 7.194  -6.159  1.183   1.00 69.37  ? 100  ARG A NH2 1 
ATOM   710  N N   . LEU A 1 101 ? 9.999  -12.876 1.422   1.00 19.09  ? 101  LEU A N   1 
ATOM   711  C CA  . LEU A 1 101 ? 11.038 -13.467 0.619   1.00 17.05  ? 101  LEU A CA  1 
ATOM   712  C C   . LEU A 1 101 ? 10.938 -12.972 -0.799  1.00 23.36  ? 101  LEU A C   1 
ATOM   713  O O   . LEU A 1 101 ? 9.871  -12.589 -1.276  1.00 18.42  ? 101  LEU A O   1 
ATOM   714  C CB  . LEU A 1 101 ? 10.844 -14.977 0.554   1.00 18.73  ? 101  LEU A CB  1 
ATOM   715  C CG  . LEU A 1 101 ? 10.629 -15.729 1.861   1.00 24.64  ? 101  LEU A CG  1 
ATOM   716  C CD1 . LEU A 1 101 ? 10.308 -17.195 1.536   1.00 24.77  ? 101  LEU A CD1 1 
ATOM   717  C CD2 . LEU A 1 101 ? 11.860 -15.597 2.738   1.00 24.20  ? 101  LEU A CD2 1 
ATOM   718  N N   . ALA A 1 102 ? 12.060 -13.019 -1.484  1.00 16.52  ? 102  ALA A N   1 
ATOM   719  C CA  . ALA A 1 102 ? 12.035 -13.023 -2.926  1.00 19.70  ? 102  ALA A CA  1 
ATOM   720  C C   . ALA A 1 102 ? 12.404 -14.446 -3.265  1.00 24.60  ? 102  ALA A C   1 
ATOM   721  O O   . ALA A 1 102 ? 13.288 -15.028 -2.622  1.00 19.71  ? 102  ALA A O   1 
ATOM   722  C CB  . ALA A 1 102 ? 13.065 -12.087 -3.459  1.00 19.14  ? 102  ALA A CB  1 
ATOM   723  N N   . SER A 1 103 ? 11.741 -15.029 -4.253  1.00 18.88  ? 103  SER A N   1 
ATOM   724  C CA  . SER A 1 103 ? 12.067 -16.407 -4.594  1.00 18.03  ? 103  SER A CA  1 
ATOM   725  C C   . SER A 1 103 ? 11.856 -16.761 -6.060  1.00 17.88  ? 103  SER A C   1 
ATOM   726  O O   . SER A 1 103 ? 11.224 -16.008 -6.821  1.00 16.65  ? 103  SER A O   1 
ATOM   727  C CB  . SER A 1 103 ? 11.263 -17.356 -3.703  1.00 23.54  ? 103  SER A CB  1 
ATOM   728  O OG  . SER A 1 103 ? 9.886  -17.225 -3.950  1.00 21.55  ? 103  SER A OG  1 
ATOM   729  N N   . GLY A 1 104 ? 12.395 -17.917 -6.442  1.00 14.70  ? 104  GLY A N   1 
ATOM   730  C CA  . GLY A 1 104 ? 12.158 -18.440 -7.777  1.00 16.78  ? 104  GLY A CA  1 
ATOM   731  C C   . GLY A 1 104 ? 12.552 -19.902 -7.852  1.00 20.63  ? 104  GLY A C   1 
ATOM   732  O O   . GLY A 1 104 ? 13.427 -20.356 -7.112  1.00 17.49  ? 104  GLY A O   1 
ATOM   733  N N   . VAL A 1 105 ? 11.909 -20.658 -8.737  1.00 15.64  ? 105  VAL A N   1 
ATOM   734  C CA  . VAL A 1 105 ? 12.226 -22.077 -8.874  1.00 15.57  ? 105  VAL A CA  1 
ATOM   735  C C   . VAL A 1 105 ? 13.476 -22.217 -9.731  1.00 13.74  ? 105  VAL A C   1 
ATOM   736  O O   . VAL A 1 105 ? 13.653 -21.509 -10.714 1.00 16.46  ? 105  VAL A O   1 
ATOM   737  C CB  . VAL A 1 105 ? 11.062 -22.863 -9.501  1.00 17.81  ? 105  VAL A CB  1 
ATOM   738  C CG1 . VAL A 1 105 ? 11.388 -24.345 -9.568  1.00 18.17  ? 105  VAL A CG1 1 
ATOM   739  C CG2 . VAL A 1 105 ? 9.784  -22.628 -8.701  1.00 26.82  ? 105  VAL A CG2 1 
ATOM   740  N N   . ILE A 1 106 ? 14.369 -23.108 -9.328  1.00 19.12  ? 106  ILE A N   1 
ATOM   741  C CA  . ILE A 1 106 ? 15.591 -23.318 -10.078 1.00 18.22  ? 106  ILE A CA  1 
ATOM   742  C C   . ILE A 1 106 ? 15.284 -24.174 -11.321 1.00 14.48  ? 106  ILE A C   1 
ATOM   743  O O   . ILE A 1 106 ? 14.921 -25.340 -11.198 1.00 20.43  ? 106  ILE A O   1 
ATOM   744  C CB  . ILE A 1 106 ? 16.640 -24.003 -9.178  1.00 18.87  ? 106  ILE A CB  1 
ATOM   745  C CG1 . ILE A 1 106 ? 16.988 -23.081 -7.987  1.00 14.55  ? 106  ILE A CG1 1 
ATOM   746  C CG2 . ILE A 1 106 ? 17.880 -24.372 -9.984  1.00 18.59  ? 106  ILE A CG2 1 
ATOM   747  C CD1 . ILE A 1 106 ? 17.613 -23.808 -6.790  1.00 21.35  ? 106  ILE A CD1 1 
ATOM   748  N N   . GLY A 1 107 ? 15.417 -23.584 -12.505 1.00 14.29  ? 107  GLY A N   1 
ATOM   749  C CA  . GLY A 1 107 ? 15.075 -24.277 -13.737 1.00 16.76  ? 107  GLY A CA  1 
ATOM   750  C C   . GLY A 1 107 ? 16.289 -24.684 -14.550 1.00 18.59  ? 107  GLY A C   1 
ATOM   751  O O   . GLY A 1 107 ? 17.316 -24.012 -14.508 1.00 22.91  ? 107  GLY A O   1 
ATOM   752  N N   . ILE A 1 108 ? 16.166 -25.785 -15.293 1.00 20.92  ? 108  ILE A N   1 
ATOM   753  C CA  . ILE A 1 108 ? 17.261 -26.293 -16.110 1.00 22.31  ? 108  ILE A CA  1 
ATOM   754  C C   . ILE A 1 108 ? 17.583 -25.266 -17.182 1.00 24.02  ? 108  ILE A C   1 
ATOM   755  O O   . ILE A 1 108 ? 16.675 -24.730 -17.817 1.00 23.51  ? 108  ILE A O   1 
ATOM   756  C CB  . ILE A 1 108 ? 16.867 -27.604 -16.829 1.00 26.58  ? 108  ILE A CB  1 
ATOM   757  C CG1 . ILE A 1 108 ? 16.483 -28.677 -15.809 1.00 32.75  ? 108  ILE A CG1 1 
ATOM   758  C CG2 . ILE A 1 108 ? 17.991 -28.071 -17.747 1.00 31.06  ? 108  ILE A CG2 1 
ATOM   759  C CD1 . ILE A 1 108 ? 15.786 -29.901 -16.415 1.00 36.33  ? 108  ILE A CD1 1 
ATOM   760  N N   . ALA A 1 109 ? 18.862 -24.977 -17.376 1.00 23.59  ? 109  ALA A N   1 
ATOM   761  C CA  . ALA A 1 109 ? 19.269 -24.153 -18.500 1.00 28.46  ? 109  ALA A CA  1 
ATOM   762  C C   . ALA A 1 109 ? 19.955 -25.047 -19.527 1.00 39.27  ? 109  ALA A C   1 
ATOM   763  O O   . ALA A 1 109 ? 19.626 -24.999 -20.715 1.00 37.70  ? 109  ALA A O   1 
ATOM   764  C CB  . ALA A 1 109 ? 20.190 -23.055 -18.049 1.00 27.44  ? 109  ALA A CB  1 
ATOM   765  N N   . GLN A 1 110 ? 20.900 -25.861 -19.053 1.00 39.06  ? 110  GLN A N   1 
ATOM   766  C CA  . GLN A 1 110 ? 21.593 -26.835 -19.896 1.00 56.03  ? 110  GLN A CA  1 
ATOM   767  C C   . GLN A 1 110 ? 21.716 -28.194 -19.206 1.00 58.23  ? 110  GLN A C   1 
ATOM   768  O O   . GLN A 1 110 ? 21.963 -28.257 -18.003 1.00 47.95  ? 110  GLN A O   1 
ATOM   769  C CB  . GLN A 1 110 ? 22.992 -26.338 -20.266 1.00 65.22  ? 110  GLN A CB  1 
ATOM   770  C CG  . GLN A 1 110 ? 23.058 -25.354 -21.414 1.00 66.84  ? 110  GLN A CG  1 
ATOM   771  C CD  . GLN A 1 110 ? 24.491 -25.053 -21.805 1.00 76.92  ? 110  GLN A CD  1 
ATOM   772  O OE1 . GLN A 1 110 ? 24.770 -24.049 -22.457 1.00 81.67  ? 110  GLN A OE1 1 
ATOM   773  N NE2 . GLN A 1 110 ? 25.413 -25.929 -21.404 1.00 80.32  ? 110  GLN A NE2 1 
ATOM   774  O OXT . GLN A 1 110 ? 21.589 -29.257 -19.828 1.00 61.37  ? 110  GLN A OXT 1 
ATOM   775  N N   . THR B 1 2   ? 36.502 -14.720 -16.667 1.00 33.17  ? 2    THR B N   1 
ATOM   776  C CA  . THR B 1 2   ? 35.650 -13.542 -16.784 1.00 29.26  ? 2    THR B CA  1 
ATOM   777  C C   . THR B 1 2   ? 34.239 -13.973 -17.170 1.00 29.99  ? 2    THR B C   1 
ATOM   778  O O   . THR B 1 2   ? 34.042 -14.990 -17.854 1.00 35.69  ? 2    THR B O   1 
ATOM   779  C CB  . THR B 1 2   ? 36.178 -12.554 -17.852 1.00 48.12  ? 2    THR B CB  1 
ATOM   780  O OG1 . THR B 1 2   ? 37.606 -12.624 -17.916 1.00 58.48  ? 2    THR B OG1 1 
ATOM   781  C CG2 . THR B 1 2   ? 35.760 -11.127 -17.529 1.00 48.88  ? 2    THR B CG2 1 
ATOM   782  N N   . LYS B 1 3   ? 33.252 -13.218 -16.710 1.00 25.84  ? 3    LYS B N   1 
ATOM   783  C CA  . LYS B 1 3   ? 31.864 -13.477 -17.079 1.00 22.15  ? 3    LYS B CA  1 
ATOM   784  C C   . LYS B 1 3   ? 31.210 -12.155 -17.462 1.00 30.42  ? 3    LYS B C   1 
ATOM   785  O O   . LYS B 1 3   ? 31.580 -11.097 -16.956 1.00 25.83  ? 3    LYS B O   1 
ATOM   786  C CB  . LYS B 1 3   ? 31.100 -14.149 -15.933 1.00 22.00  ? 3    LYS B CB  1 
ATOM   787  C CG  . LYS B 1 3   ? 31.772 -15.413 -15.389 1.00 32.22  ? 3    LYS B CG  1 
ATOM   788  C CD  . LYS B 1 3   ? 30.866 -16.155 -14.406 1.00 38.47  ? 3    LYS B CD  1 
ATOM   789  C CE  . LYS B 1 3   ? 30.665 -15.357 -13.127 1.00 42.11  ? 3    LYS B CE  1 
ATOM   790  N NZ  . LYS B 1 3   ? 31.903 -15.288 -12.287 1.00 48.93  ? 3    LYS B NZ  1 
ATOM   791  N N   . ALA B 1 4   ? 30.257 -12.214 -18.380 1.00 20.75  ? 4    ALA B N   1 
ATOM   792  C CA  . ALA B 1 4   ? 29.527 -11.017 -18.788 1.00 23.16  ? 4    ALA B CA  1 
ATOM   793  C C   . ALA B 1 4   ? 28.089 -11.405 -19.076 1.00 26.77  ? 4    ALA B C   1 
ATOM   794  O O   . ALA B 1 4   ? 27.805 -12.578 -19.296 1.00 22.97  ? 4    ALA B O   1 
ATOM   795  C CB  . ALA B 1 4   ? 30.172 -10.398 -20.019 1.00 17.10  ? 4    ALA B CB  1 
ATOM   796  N N   . VAL B 1 5   ? 27.174 -10.435 -19.036 1.00 19.56  ? 5    VAL B N   1 
ATOM   797  C CA  . VAL B 1 5   ? 25.760 -10.704 -19.259 1.00 15.38  ? 5    VAL B CA  1 
ATOM   798  C C   . VAL B 1 5   ? 25.160 -9.574  -20.103 1.00 18.69  ? 5    VAL B C   1 
ATOM   799  O O   . VAL B 1 5   ? 25.416 -8.406  -19.843 1.00 15.02  ? 5    VAL B O   1 
ATOM   800  C CB  . VAL B 1 5   ? 24.965 -10.747 -17.924 1.00 16.32  ? 5    VAL B CB  1 
ATOM   801  C CG1 . VAL B 1 5   ? 23.479 -11.012 -18.196 1.00 14.72  ? 5    VAL B CG1 1 
ATOM   802  C CG2 . VAL B 1 5   ? 25.543 -11.791 -16.963 1.00 19.85  ? 5    VAL B CG2 1 
ATOM   803  N N   . ALA B 1 6   ? 24.380 -9.924  -21.118 1.00 21.25  ? 6    ALA B N   1 
ATOM   804  C CA  . ALA B 1 6   ? 23.610 -8.938  -21.859 1.00 20.09  ? 6    ALA B CA  1 
ATOM   805  C C   . ALA B 1 6   ? 22.139 -9.214  -21.632 1.00 17.07  ? 6    ALA B C   1 
ATOM   806  O O   . ALA B 1 6   ? 21.674 -10.355 -21.829 1.00 17.93  ? 6    ALA B O   1 
ATOM   807  C CB  . ALA B 1 6   ? 23.932 -9.013  -23.357 1.00 18.45  ? 6    ALA B CB  1 
ATOM   808  N N   . VAL B 1 7   ? 21.413 -8.172  -21.223 1.00 12.19  ? 7    VAL B N   1 
ATOM   809  C CA  . VAL B 1 7   ? 19.965 -8.245  -21.070 1.00 15.04  ? 7    VAL B CA  1 
ATOM   810  C C   . VAL B 1 7   ? 19.345 -7.690  -22.345 1.00 17.04  ? 7    VAL B C   1 
ATOM   811  O O   . VAL B 1 7   ? 19.470 -6.501  -22.649 1.00 19.20  ? 7    VAL B O   1 
ATOM   812  C CB  . VAL B 1 7   ? 19.470 -7.438  -19.840 1.00 16.71  ? 7    VAL B CB  1 
ATOM   813  C CG1 . VAL B 1 7   ? 17.931 -7.439  -19.762 1.00 15.29  ? 7    VAL B CG1 1 
ATOM   814  C CG2 . VAL B 1 7   ? 20.083 -8.016  -18.553 1.00 20.98  ? 7    VAL B CG2 1 
ATOM   815  N N   . LEU B 1 8   ? 18.695 -8.556  -23.107 1.00 17.78  ? 8    LEU B N   1 
ATOM   816  C CA  . LEU B 1 8   ? 18.153 -8.148  -24.393 1.00 21.54  ? 8    LEU B CA  1 
ATOM   817  C C   . LEU B 1 8   ? 16.709 -7.698  -24.230 1.00 21.15  ? 8    LEU B C   1 
ATOM   818  O O   . LEU B 1 8   ? 15.890 -8.395  -23.619 1.00 22.55  ? 8    LEU B O   1 
ATOM   819  C CB  . LEU B 1 8   ? 18.224 -9.292  -25.396 1.00 21.01  ? 8    LEU B CB  1 
ATOM   820  C CG  . LEU B 1 8   ? 19.594 -9.924  -25.656 1.00 25.10  ? 8    LEU B CG  1 
ATOM   821  C CD1 . LEU B 1 8   ? 19.435 -11.143 -26.540 1.00 29.92  ? 8    LEU B CD1 1 
ATOM   822  C CD2 . LEU B 1 8   ? 20.551 -8.915  -26.308 1.00 23.51  ? 8    LEU B CD2 1 
ATOM   823  N N   . LYS B 1 9   ? 16.415 -6.528  -24.780 1.00 23.39  ? 9    LYS B N   1 
ATOM   824  C CA  . LYS B 1 9   ? 15.082 -5.968  -24.757 1.00 27.61  ? 9    LYS B CA  1 
ATOM   825  C C   . LYS B 1 9   ? 14.723 -5.545  -26.183 1.00 25.60  ? 9    LYS B C   1 
ATOM   826  O O   . LYS B 1 9   ? 15.505 -4.870  -26.854 1.00 24.66  ? 9    LYS B O   1 
ATOM   827  C CB  . LYS B 1 9   ? 15.046 -4.764  -23.817 1.00 30.29  ? 9    LYS B CB  1 
ATOM   828  C CG  . LYS B 1 9   ? 13.675 -4.123  -23.670 1.00 42.20  ? 9    LYS B CG  1 
ATOM   829  C CD  . LYS B 1 9   ? 12.696 -5.046  -22.939 1.00 46.10  ? 9    LYS B CD  1 
ATOM   830  C CE  . LYS B 1 9   ? 11.454 -4.298  -22.492 1.00 43.65  ? 9    LYS B CE  1 
ATOM   831  N NZ  . LYS B 1 9   ? 10.660 -3.763  -23.634 1.00 45.62  ? 9    LYS B NZ  1 
ATOM   832  N N   . GLY B 1 10  ? 13.541 -5.954  -26.639 1.00 25.83  ? 10   GLY B N   1 
ATOM   833  C CA  . GLY B 1 10  ? 13.080 -5.620  -27.970 1.00 37.05  ? 10   GLY B CA  1 
ATOM   834  C C   . GLY B 1 10  ? 11.638 -5.158  -27.949 1.00 42.68  ? 10   GLY B C   1 
ATOM   835  O O   . GLY B 1 10  ? 11.107 -4.810  -26.895 1.00 37.73  ? 10   GLY B O   1 
ATOM   836  N N   . ASP B 1 11  ? 11.005 -5.153  -29.119 1.00 36.47  ? 11   ASP B N   1 
ATOM   837  C CA  . ASP B 1 11  ? 9.602  -4.766  -29.225 1.00 40.80  ? 11   ASP B CA  1 
ATOM   838  C C   . ASP B 1 11  ? 8.696  -5.899  -28.771 1.00 41.50  ? 11   ASP B C   1 
ATOM   839  O O   . ASP B 1 11  ? 9.071  -7.073  -28.838 1.00 37.67  ? 11   ASP B O   1 
ATOM   840  C CB  . ASP B 1 11  ? 9.265  -4.385  -30.664 1.00 46.33  ? 11   ASP B CB  1 
ATOM   841  C CG  . ASP B 1 11  ? 10.232 -3.373  -31.229 1.00 53.84  ? 11   ASP B CG  1 
ATOM   842  O OD1 . ASP B 1 11  ? 11.351 -3.778  -31.617 1.00 53.56  ? 11   ASP B OD1 1 
ATOM   843  O OD2 . ASP B 1 11  ? 9.880  -2.175  -31.277 1.00 57.71  ? 11   ASP B OD2 1 
ATOM   844  N N   . GLY B 1 12  ? 7.499  -5.539  -28.322 1.00 51.51  ? 12   GLY B N   1 
ATOM   845  C CA  . GLY B 1 12  ? 6.529  -6.512  -27.861 1.00 52.07  ? 12   GLY B CA  1 
ATOM   846  C C   . GLY B 1 12  ? 7.098  -7.431  -26.796 1.00 48.56  ? 12   GLY B C   1 
ATOM   847  O O   . GLY B 1 12  ? 7.699  -6.968  -25.819 1.00 40.37  ? 12   GLY B O   1 
ATOM   848  N N   . PRO B 1 13  ? 6.928  -8.748  -26.991 1.00 44.92  ? 13   PRO B N   1 
ATOM   849  C CA  . PRO B 1 13  ? 7.339  -9.746  -25.995 1.00 40.52  ? 13   PRO B CA  1 
ATOM   850  C C   . PRO B 1 13  ? 8.818  -10.135 -26.092 1.00 33.92  ? 13   PRO B C   1 
ATOM   851  O O   . PRO B 1 13  ? 9.280  -10.913 -25.259 1.00 32.35  ? 13   PRO B O   1 
ATOM   852  C CB  . PRO B 1 13  ? 6.463  -10.947 -26.341 1.00 38.31  ? 13   PRO B CB  1 
ATOM   853  C CG  . PRO B 1 13  ? 6.297  -10.840 -27.846 1.00 39.01  ? 13   PRO B CG  1 
ATOM   854  C CD  . PRO B 1 13  ? 6.258  -9.361  -28.153 1.00 42.62  ? 13   PRO B CD  1 
ATOM   855  N N   . VAL B 1 14  ? 9.551  -9.618  -27.074 1.00 31.87  ? 14   VAL B N   1 
ATOM   856  C CA  . VAL B 1 14  ? 10.949 -10.042 -27.231 1.00 31.60  ? 14   VAL B CA  1 
ATOM   857  C C   . VAL B 1 14  ? 11.841 -9.614  -26.069 1.00 32.60  ? 14   VAL B C   1 
ATOM   858  O O   . VAL B 1 14  ? 11.989 -8.431  -25.777 1.00 29.80  ? 14   VAL B O   1 
ATOM   859  C CB  . VAL B 1 14  ? 11.572 -9.565  -28.543 1.00 31.74  ? 14   VAL B CB  1 
ATOM   860  C CG1 . VAL B 1 14  ? 12.980 -10.092 -28.649 1.00 29.61  ? 14   VAL B CG1 1 
ATOM   861  C CG2 . VAL B 1 14  ? 10.752 -10.060 -29.722 1.00 31.17  ? 14   VAL B CG2 1 
ATOM   862  N N   . GLN B 1 15  ? 12.425 -10.592 -25.393 1.00 25.97  ? 15   GLN B N   1 
ATOM   863  C CA  . GLN B 1 15  ? 13.331 -10.287 -24.298 1.00 26.81  ? 15   GLN B CA  1 
ATOM   864  C C   . GLN B 1 15  ? 14.150 -11.513 -23.999 1.00 21.65  ? 15   GLN B C   1 
ATOM   865  O O   . GLN B 1 15  ? 13.732 -12.637 -24.280 1.00 20.24  ? 15   GLN B O   1 
ATOM   866  C CB  . GLN B 1 15  ? 12.573 -9.823  -23.053 1.00 31.73  ? 15   GLN B CB  1 
ATOM   867  C CG  . GLN B 1 15  ? 11.535 -10.810 -22.567 1.00 29.70  ? 15   GLN B CG  1 
ATOM   868  C CD  . GLN B 1 15  ? 12.088 -11.760 -21.540 0.42 31.54  ? 15   GLN B CD  1 
ATOM   869  O OE1 . GLN B 1 15  ? 13.174 -11.540 -20.995 0.50 28.09  ? 15   GLN B OE1 1 
ATOM   870  N NE2 . GLN B 1 15  ? 11.345 -12.827 -21.261 0.72 35.56  ? 15   GLN B NE2 1 
ATOM   871  N N   . GLY B 1 16  ? 15.330 -11.311 -23.439 1.00 21.48  ? 16   GLY B N   1 
ATOM   872  C CA  . GLY B 1 16  ? 16.138 -12.462 -23.104 1.00 23.91  ? 16   GLY B CA  1 
ATOM   873  C C   . GLY B 1 16  ? 17.355 -12.129 -22.278 1.00 22.35  ? 16   GLY B C   1 
ATOM   874  O O   . GLY B 1 16  ? 17.624 -10.966 -21.961 1.00 19.50  ? 16   GLY B O   1 
ATOM   875  N N   . ILE B 1 17  ? 18.095 -13.171 -21.927 1.00 16.50  ? 17   ILE B N   1 
ATOM   876  C CA  . ILE B 1 17  ? 19.315 -12.997 -21.173 1.00 17.52  ? 17   ILE B CA  1 
ATOM   877  C C   . ILE B 1 17  ? 20.367 -13.915 -21.743 1.00 18.42  ? 17   ILE B C   1 
ATOM   878  O O   . ILE B 1 17  ? 20.135 -15.120 -21.940 1.00 24.21  ? 17   ILE B O   1 
ATOM   879  C CB  . ILE B 1 17  ? 19.119 -13.320 -19.677 1.00 23.26  ? 17   ILE B CB  1 
ATOM   880  C CG1 . ILE B 1 17  ? 18.135 -12.346 -19.061 1.00 25.65  ? 17   ILE B CG1 1 
ATOM   881  C CG2 . ILE B 1 17  ? 20.453 -13.230 -18.937 1.00 13.27  ? 17   ILE B CG2 1 
ATOM   882  C CD1 . ILE B 1 17  ? 17.133 -13.013 -18.250 1.00 34.88  ? 17   ILE B CD1 1 
ATOM   883  N N   . ILE B 1 18  ? 21.524 -13.327 -22.036 1.00 14.37  ? 18   ILE B N   1 
ATOM   884  C CA  . ILE B 1 18  ? 22.617 -14.080 -22.604 1.00 14.02  ? 18   ILE B CA  1 
ATOM   885  C C   . ILE B 1 18  ? 23.862 -13.891 -21.753 1.00 16.99  ? 18   ILE B C   1 
ATOM   886  O O   . ILE B 1 18  ? 24.288 -12.773 -21.460 1.00 19.82  ? 18   ILE B O   1 
ATOM   887  C CB  . ILE B 1 18  ? 22.916 -13.658 -24.063 1.00 21.39  ? 18   ILE B CB  1 
ATOM   888  C CG1 . ILE B 1 18  ? 21.689 -13.845 -24.966 1.00 26.62  ? 18   ILE B CG1 1 
ATOM   889  C CG2 . ILE B 1 18  ? 24.087 -14.433 -24.595 1.00 22.50  ? 18   ILE B CG2 1 
ATOM   890  C CD1 . ILE B 1 18  ? 21.213 -15.296 -25.118 1.00 27.59  ? 18   ILE B CD1 1 
ATOM   891  N N   . ASN B 1 19  ? 24.440 -15.010 -21.369 1.00 17.51  ? 19   ASN B N   1 
ATOM   892  C CA  . ASN B 1 19  ? 25.621 -15.064 -20.539 1.00 22.57  ? 19   ASN B CA  1 
ATOM   893  C C   . ASN B 1 19  ? 26.835 -15.408 -21.383 1.00 20.79  ? 19   ASN B C   1 
ATOM   894  O O   . ASN B 1 19  ? 26.740 -16.159 -22.357 1.00 25.97  ? 19   ASN B O   1 
ATOM   895  C CB  . ASN B 1 19  ? 25.411 -16.114 -19.446 1.00 27.25  ? 19   ASN B CB  1 
ATOM   896  C CG  . ASN B 1 19  ? 24.199 -15.807 -18.589 1.00 26.59  ? 19   ASN B CG  1 
ATOM   897  O OD1 . ASN B 1 19  ? 24.166 -14.780 -17.912 1.00 22.06  ? 19   ASN B OD1 1 
ATOM   898  N ND2 . ASN B 1 19  ? 23.193 -16.688 -18.619 1.00 15.77  ? 19   ASN B ND2 1 
ATOM   899  N N   . PHE B 1 20  ? 27.976 -14.840 -21.009 1.00 20.52  ? 20   PHE B N   1 
ATOM   900  C CA  . PHE B 1 20  ? 29.227 -15.069 -21.706 1.00 23.27  ? 20   PHE B CA  1 
ATOM   901  C C   . PHE B 1 20  ? 30.206 -15.502 -20.632 1.00 33.30  ? 20   PHE B C   1 
ATOM   902  O O   . PHE B 1 20  ? 30.271 -14.878 -19.569 1.00 27.86  ? 20   PHE B O   1 
ATOM   903  C CB  . PHE B 1 20  ? 29.747 -13.766 -22.336 1.00 21.42  ? 20   PHE B CB  1 
ATOM   904  C CG  . PHE B 1 20  ? 28.892 -13.223 -23.458 1.00 21.90  ? 20   PHE B CG  1 
ATOM   905  C CD1 . PHE B 1 20  ? 27.764 -12.458 -23.189 1.00 24.88  ? 20   PHE B CD1 1 
ATOM   906  C CD2 . PHE B 1 20  ? 29.247 -13.447 -24.784 1.00 26.27  ? 20   PHE B CD2 1 
ATOM   907  C CE1 . PHE B 1 20  ? 26.988 -11.944 -24.232 1.00 24.32  ? 20   PHE B CE1 1 
ATOM   908  C CE2 . PHE B 1 20  ? 28.478 -12.946 -25.831 1.00 24.63  ? 20   PHE B CE2 1 
ATOM   909  C CZ  . PHE B 1 20  ? 27.356 -12.197 -25.563 1.00 21.25  ? 20   PHE B CZ  1 
ATOM   910  N N   . GLU B 1 21  ? 30.961 -16.566 -20.892 1.00 24.66  ? 21   GLU B N   1 
ATOM   911  C CA  . GLU B 1 21  ? 31.982 -17.025 -19.947 1.00 26.86  ? 21   GLU B CA  1 
ATOM   912  C C   . GLU B 1 21  ? 33.259 -17.451 -20.659 1.00 31.84  ? 21   GLU B C   1 
ATOM   913  O O   . GLU B 1 21  ? 33.239 -18.185 -21.642 1.00 32.39  ? 21   GLU B O   1 
ATOM   914  C CB  . GLU B 1 21  ? 31.465 -18.168 -19.077 1.00 32.98  ? 21   GLU B CB  1 
ATOM   915  C CG  . GLU B 1 21  ? 30.381 -17.723 -18.119 1.00 37.87  ? 21   GLU B CG  1 
ATOM   916  C CD  . GLU B 1 21  ? 29.805 -18.858 -17.329 1.00 47.93  ? 21   GLU B CD  1 
ATOM   917  O OE1 . GLU B 1 21  ? 30.544 -19.433 -16.499 1.00 48.61  ? 21   GLU B OE1 1 
ATOM   918  O OE2 . GLU B 1 21  ? 28.611 -19.162 -17.550 1.00 50.09  ? 21   GLU B OE2 1 
ATOM   919  N N   . GLN B 1 22  ? 34.379 -16.983 -20.146 1.00 31.66  ? 22   GLN B N   1 
ATOM   920  C CA  . GLN B 1 22  ? 35.653 -17.258 -20.780 1.00 34.43  ? 22   GLN B CA  1 
ATOM   921  C C   . GLN B 1 22  ? 36.612 -17.752 -19.717 1.00 38.50  ? 22   GLN B C   1 
ATOM   922  O O   . GLN B 1 22  ? 36.948 -17.019 -18.782 1.00 36.85  ? 22   GLN B O   1 
ATOM   923  C CB  . GLN B 1 22  ? 36.193 -15.999 -21.467 1.00 33.76  ? 22   GLN B CB  1 
ATOM   924  C CG  . GLN B 1 22  ? 37.399 -16.256 -22.366 1.00 37.19  ? 22   GLN B CG  1 
ATOM   925  C CD  . GLN B 1 22  ? 37.914 -14.983 -23.025 1.00 36.65  ? 22   GLN B CD  1 
ATOM   926  O OE1 . GLN B 1 22  ? 37.752 -13.889 -22.490 1.00 34.46  ? 22   GLN B OE1 1 
ATOM   927  N NE2 . GLN B 1 22  ? 38.540 -15.126 -24.196 1.00 38.94  ? 22   GLN B NE2 1 
ATOM   928  N N   . LYS B 1 23  ? 37.024 -19.009 -19.859 1.00 40.59  ? 23   LYS B N   1 
ATOM   929  C CA  . LYS B 1 23  ? 37.948 -19.641 -18.928 1.00 54.92  ? 23   LYS B CA  1 
ATOM   930  C C   . LYS B 1 23  ? 39.353 -19.061 -19.084 1.00 55.22  ? 23   LYS B C   1 
ATOM   931  O O   . LYS B 1 23  ? 40.005 -18.715 -18.096 1.00 51.11  ? 23   LYS B O   1 
ATOM   932  C CB  . LYS B 1 23  ? 37.971 -21.157 -19.159 1.00 59.93  ? 23   LYS B CB  1 
ATOM   933  C CG  . LYS B 1 23  ? 38.478 -21.982 -17.979 1.00 66.35  ? 23   LYS B CG  1 
ATOM   934  C CD  . LYS B 1 23  ? 38.521 -23.466 -18.325 1.00 75.66  ? 23   LYS B CD  1 
ATOM   935  C CE  . LYS B 1 23  ? 38.861 -24.326 -17.110 1.00 82.08  ? 23   LYS B CE  1 
ATOM   936  N NZ  . LYS B 1 23  ? 37.723 -24.427 -16.145 1.00 79.28  ? 23   LYS B NZ  1 
ATOM   937  N N   . GLU B 1 24  ? 39.804 -18.945 -20.331 1.00 56.11  ? 24   GLU B N   1 
ATOM   938  C CA  . GLU B 1 24  ? 41.162 -18.486 -20.633 1.00 60.18  ? 24   GLU B CA  1 
ATOM   939  C C   . GLU B 1 24  ? 41.130 -17.260 -21.525 1.00 51.95  ? 24   GLU B C   1 
ATOM   940  O O   . GLU B 1 24  ? 40.365 -17.215 -22.483 1.00 46.42  ? 24   GLU B O   1 
ATOM   941  C CB  . GLU B 1 24  ? 41.949 -19.589 -21.342 1.00 60.74  ? 24   GLU B CB  1 
ATOM   942  C CG  . GLU B 1 24  ? 42.157 -20.836 -20.514 1.00 73.81  ? 24   GLU B CG  1 
ATOM   943  C CD  . GLU B 1 24  ? 43.034 -20.588 -19.306 1.00 87.90  ? 24   GLU B CD  1 
ATOM   944  O OE1 . GLU B 1 24  ? 43.946 -19.738 -19.396 1.00 98.04  ? 24   GLU B OE1 1 
ATOM   945  O OE2 . GLU B 1 24  ? 42.808 -21.241 -18.267 1.00 88.10  ? 24   GLU B OE2 1 
ATOM   946  N N   . SER B 1 25  ? 41.982 -16.282 -21.230 1.00 53.13  ? 25   SER B N   1 
ATOM   947  C CA  . SER B 1 25  ? 41.990 -15.036 -21.987 1.00 52.42  ? 25   SER B CA  1 
ATOM   948  C C   . SER B 1 25  ? 42.243 -15.258 -23.482 1.00 48.50  ? 25   SER B C   1 
ATOM   949  O O   . SER B 1 25  ? 41.765 -14.484 -24.315 1.00 47.69  ? 25   SER B O   1 
ATOM   950  C CB  . SER B 1 25  ? 42.983 -14.031 -21.398 1.00 47.85  ? 25   SER B CB  1 
ATOM   951  O OG  . SER B 1 25  ? 44.299 -14.276 -21.847 1.00 53.81  ? 25   SER B OG  1 
ATOM   952  N N   . ASN B 1 26  ? 42.960 -16.329 -23.821 1.00 52.70  ? 26   ASN B N   1 
ATOM   953  C CA  . ASN B 1 26  ? 43.197 -16.671 -25.222 1.00 54.88  ? 26   ASN B CA  1 
ATOM   954  C C   . ASN B 1 26  ? 42.250 -17.751 -25.737 1.00 55.04  ? 26   ASN B C   1 
ATOM   955  O O   . ASN B 1 26  ? 42.394 -18.234 -26.863 1.00 56.88  ? 26   ASN B O   1 
ATOM   956  C CB  . ASN B 1 26  ? 44.660 -17.092 -25.452 1.00 60.40  ? 26   ASN B CB  1 
ATOM   957  C CG  . ASN B 1 26  ? 45.035 -18.393 -24.732 1.00 64.65  ? 26   ASN B CG  1 
ATOM   958  O OD1 . ASN B 1 26  ? 44.182 -19.096 -24.194 1.00 64.07  ? 26   ASN B OD1 1 
ATOM   959  N ND2 . ASN B 1 26  ? 46.326 -18.714 -24.733 1.00 75.09  ? 26   ASN B ND2 1 
ATOM   960  N N   . GLY B 1 27  ? 41.293 -18.136 -24.899 1.00 52.00  ? 27   GLY B N   1 
ATOM   961  C CA  . GLY B 1 27  ? 40.445 -19.274 -25.191 1.00 52.13  ? 27   GLY B CA  1 
ATOM   962  C C   . GLY B 1 27  ? 39.067 -18.901 -25.694 1.00 48.46  ? 27   GLY B C   1 
ATOM   963  O O   . GLY B 1 27  ? 38.736 -17.719 -25.817 1.00 44.95  ? 27   GLY B O   1 
ATOM   964  N N   . PRO B 1 28  ? 38.245 -19.920 -25.986 1.00 52.98  ? 28   PRO B N   1 
ATOM   965  C CA  . PRO B 1 28  ? 36.893 -19.696 -26.497 1.00 44.74  ? 28   PRO B CA  1 
ATOM   966  C C   . PRO B 1 28  ? 35.983 -19.080 -25.444 1.00 44.21  ? 28   PRO B C   1 
ATOM   967  O O   . PRO B 1 28  ? 36.207 -19.213 -24.235 1.00 40.51  ? 28   PRO B O   1 
ATOM   968  C CB  . PRO B 1 28  ? 36.408 -21.108 -26.835 1.00 50.84  ? 28   PRO B CB  1 
ATOM   969  C CG  . PRO B 1 28  ? 37.170 -21.993 -25.910 1.00 61.51  ? 28   PRO B CG  1 
ATOM   970  C CD  . PRO B 1 28  ? 38.528 -21.350 -25.775 1.00 59.05  ? 28   PRO B CD  1 
ATOM   971  N N   . VAL B 1 29  ? 34.953 -18.398 -25.918 1.00 39.03  ? 29   VAL B N   1 
ATOM   972  C CA  . VAL B 1 29  ? 33.928 -17.868 -25.041 1.00 34.62  ? 29   VAL B CA  1 
ATOM   973  C C   . VAL B 1 29  ? 32.673 -18.714 -25.192 1.00 35.91  ? 29   VAL B C   1 
ATOM   974  O O   . VAL B 1 29  ? 32.162 -18.884 -26.304 1.00 40.53  ? 29   VAL B O   1 
ATOM   975  C CB  . VAL B 1 29  ? 33.590 -16.416 -25.387 1.00 32.35  ? 29   VAL B CB  1 
ATOM   976  C CG1 . VAL B 1 29  ? 32.534 -15.861 -24.402 1.00 27.71  ? 29   VAL B CG1 1 
ATOM   977  C CG2 . VAL B 1 29  ? 34.851 -15.556 -25.389 1.00 32.29  ? 29   VAL B CG2 1 
ATOM   978  N N   . LYS B 1 30  ? 32.194 -19.256 -24.075 1.00 39.69  ? 30   LYS B N   1 
ATOM   979  C CA  . LYS B 1 30  ? 30.905 -19.944 -24.020 1.00 43.07  ? 30   LYS B CA  1 
ATOM   980  C C   . LYS B 1 30  ? 29.785 -18.915 -23.921 1.00 32.48  ? 30   LYS B C   1 
ATOM   981  O O   . LYS B 1 30  ? 29.809 -18.052 -23.061 1.00 25.54  ? 30   LYS B O   1 
ATOM   982  C CB  . LYS B 1 30  ? 30.836 -20.862 -22.798 1.00 40.10  ? 30   LYS B CB  1 
ATOM   983  C CG  . LYS B 1 30  ? 31.931 -21.906 -22.732 1.00 50.95  ? 30   LYS B CG  1 
ATOM   984  C CD  . LYS B 1 30  ? 31.821 -22.894 -23.882 1.00 57.13  ? 30   LYS B CD  1 
ATOM   985  C CE  . LYS B 1 30  ? 32.412 -24.245 -23.500 1.00 64.94  ? 30   LYS B CE  1 
ATOM   986  N NZ  . LYS B 1 30  ? 33.825 -24.124 -23.060 1.00 67.60  ? 30   LYS B NZ  1 
ATOM   987  N N   . VAL B 1 31  ? 28.807 -19.015 -24.809 1.00 27.18  ? 31   VAL B N   1 
ATOM   988  C CA  . VAL B 1 31  ? 27.694 -18.080 -24.828 1.00 25.33  ? 31   VAL B CA  1 
ATOM   989  C C   . VAL B 1 31  ? 26.423 -18.892 -24.605 1.00 26.93  ? 31   VAL B C   1 
ATOM   990  O O   . VAL B 1 31  ? 26.164 -19.839 -25.342 1.00 26.66  ? 31   VAL B O   1 
ATOM   991  C CB  . VAL B 1 31  ? 27.627 -17.344 -26.176 1.00 29.78  ? 31   VAL B CB  1 
ATOM   992  C CG1 . VAL B 1 31  ? 26.546 -16.283 -26.146 1.00 30.74  ? 31   VAL B CG1 1 
ATOM   993  C CG2 . VAL B 1 31  ? 28.972 -16.708 -26.501 1.00 27.93  ? 31   VAL B CG2 1 
ATOM   994  N N   . TRP B 1 32  ? 25.643 -18.559 -23.584 1.00 23.23  ? 32   TRP B N   1 
ATOM   995  C CA  . TRP B 1 32  ? 24.428 -19.332 -23.330 1.00 26.89  ? 32   TRP B CA  1 
ATOM   996  C C   . TRP B 1 32  ? 23.291 -18.533 -22.714 1.00 25.87  ? 32   TRP B C   1 
ATOM   997  O O   . TRP B 1 32  ? 23.501 -17.489 -22.115 1.00 19.40  ? 32   TRP B O   1 
ATOM   998  C CB  . TRP B 1 32  ? 24.733 -20.550 -22.454 1.00 28.99  ? 32   TRP B CB  1 
ATOM   999  C CG  . TRP B 1 32  ? 25.222 -20.194 -21.084 1.00 25.73  ? 32   TRP B CG  1 
ATOM   1000 C CD1 . TRP B 1 32  ? 26.498 -19.831 -20.732 1.00 38.23  ? 32   TRP B CD1 1 
ATOM   1001 C CD2 . TRP B 1 32  ? 24.453 -20.171 -19.878 1.00 23.92  ? 32   TRP B CD2 1 
ATOM   1002 N NE1 . TRP B 1 32  ? 26.566 -19.591 -19.378 1.00 30.92  ? 32   TRP B NE1 1 
ATOM   1003 C CE2 . TRP B 1 32  ? 25.325 -19.789 -18.833 1.00 25.59  ? 32   TRP B CE2 1 
ATOM   1004 C CE3 . TRP B 1 32  ? 23.116 -20.442 -19.578 1.00 24.12  ? 32   TRP B CE3 1 
ATOM   1005 C CZ2 . TRP B 1 32  ? 24.900 -19.673 -17.515 1.00 29.47  ? 32   TRP B CZ2 1 
ATOM   1006 C CZ3 . TRP B 1 32  ? 22.692 -20.323 -18.263 1.00 29.07  ? 32   TRP B CZ3 1 
ATOM   1007 C CH2 . TRP B 1 32  ? 23.580 -19.948 -17.248 1.00 31.83  ? 32   TRP B CH2 1 
ATOM   1008 N N   . GLY B 1 33  ? 22.071 -19.027 -22.864 1.00 22.11  ? 33   GLY B N   1 
ATOM   1009 C CA  . GLY B 1 33  ? 20.942 -18.369 -22.228 1.00 21.18  ? 33   GLY B CA  1 
ATOM   1010 C C   . GLY B 1 33  ? 19.710 -18.569 -23.081 1.00 23.32  ? 33   GLY B C   1 
ATOM   1011 O O   . GLY B 1 33  ? 19.570 -19.590 -23.754 1.00 21.60  ? 33   GLY B O   1 
ATOM   1012 N N   . SER B 1 34  ? 18.814 -17.598 -23.071 1.00 22.29  ? 34   SER B N   1 
ATOM   1013 C CA  . SER B 1 34  ? 17.648 -17.750 -23.925 1.00 22.35  ? 34   SER B CA  1 
ATOM   1014 C C   . SER B 1 34  ? 16.997 -16.423 -24.284 1.00 25.09  ? 34   SER B C   1 
ATOM   1015 O O   . SER B 1 34  ? 17.191 -15.409 -23.612 1.00 22.75  ? 34   SER B O   1 
ATOM   1016 C CB  . SER B 1 34  ? 16.623 -18.706 -23.320 1.00 22.38  ? 34   SER B CB  1 
ATOM   1017 O OG  . SER B 1 34  ? 16.005 -18.118 -22.197 1.00 24.80  ? 34   SER B OG  1 
ATOM   1018 N N   . ILE B 1 35  ? 16.278 -16.442 -25.399 1.00 26.42  ? 35   ILE B N   1 
ATOM   1019 C CA  . ILE B 1 35  ? 15.515 -15.297 -25.851 1.00 25.01  ? 35   ILE B CA  1 
ATOM   1020 C C   . ILE B 1 35  ? 14.095 -15.776 -26.116 1.00 28.64  ? 35   ILE B C   1 
ATOM   1021 O O   . ILE B 1 35  ? 13.885 -16.827 -26.721 1.00 29.86  ? 35   ILE B O   1 
ATOM   1022 C CB  . ILE B 1 35  ? 16.086 -14.737 -27.150 1.00 24.12  ? 35   ILE B CB  1 
ATOM   1023 C CG1 . ILE B 1 35  ? 17.616 -14.689 -27.081 1.00 28.98  ? 35   ILE B CG1 1 
ATOM   1024 C CG2 . ILE B 1 35  ? 15.510 -13.349 -27.417 1.00 22.16  ? 35   ILE B CG2 1 
ATOM   1025 C CD1 . ILE B 1 35  ? 18.270 -14.482 -28.428 1.00 33.61  ? 35   ILE B CD1 1 
ATOM   1026 N N   . LYS B 1 36  ? 13.127 -14.999 -25.656 1.00 21.92  ? 36   LYS B N   1 
ATOM   1027 C CA  . LYS B 1 36  ? 11.724 -15.339 -25.777 1.00 23.56  ? 36   LYS B CA  1 
ATOM   1028 C C   . LYS B 1 36  ? 10.998 -14.227 -26.530 1.00 26.36  ? 36   LYS B C   1 
ATOM   1029 O O   . LYS B 1 36  ? 11.515 -13.109 -26.663 1.00 23.29  ? 36   LYS B O   1 
ATOM   1030 C CB  . LYS B 1 36  ? 11.130 -15.508 -24.383 1.00 26.47  ? 36   LYS B CB  1 
ATOM   1031 C CG  . LYS B 1 36  ? 11.895 -16.529 -23.532 1.00 44.61  ? 36   LYS B CG  1 
ATOM   1032 C CD  . LYS B 1 36  ? 11.358 -16.625 -22.106 1.00 54.64  ? 36   LYS B CD  1 
ATOM   1033 C CE  . LYS B 1 36  ? 11.651 -17.993 -21.485 1.00 63.18  ? 36   LYS B CE  1 
ATOM   1034 N NZ  . LYS B 1 36  ? 13.077 -18.420 -21.637 1.00 64.85  ? 36   LYS B NZ  1 
ATOM   1035 N N   . GLY B 1 37  ? 9.795  -14.533 -27.005 1.00 26.20  ? 37   GLY B N   1 
ATOM   1036 C CA  . GLY B 1 37  ? 8.955  -13.549 -27.671 1.00 33.57  ? 37   GLY B CA  1 
ATOM   1037 C C   . GLY B 1 37  ? 9.208  -13.428 -29.166 1.00 34.37  ? 37   GLY B C   1 
ATOM   1038 O O   . GLY B 1 37  ? 8.654  -12.552 -29.825 1.00 31.22  ? 37   GLY B O   1 
ATOM   1039 N N   . LEU B 1 38  ? 10.037 -14.319 -29.700 1.00 27.23  ? 38   LEU B N   1 
ATOM   1040 C CA  . LEU B 1 38  ? 10.434 -14.256 -31.097 1.00 26.17  ? 38   LEU B CA  1 
ATOM   1041 C C   . LEU B 1 38  ? 9.438  -14.951 -32.007 1.00 39.80  ? 38   LEU B C   1 
ATOM   1042 O O   . LEU B 1 38  ? 8.638  -15.772 -31.563 1.00 45.43  ? 38   LEU B O   1 
ATOM   1043 C CB  . LEU B 1 38  ? 11.814 -14.899 -31.285 1.00 28.73  ? 38   LEU B CB  1 
ATOM   1044 C CG  . LEU B 1 38  ? 12.975 -14.196 -30.572 1.00 31.01  ? 38   LEU B CG  1 
ATOM   1045 C CD1 . LEU B 1 38  ? 14.160 -15.143 -30.391 1.00 26.88  ? 38   LEU B CD1 1 
ATOM   1046 C CD2 . LEU B 1 38  ? 13.386 -12.924 -31.322 1.00 29.49  ? 38   LEU B CD2 1 
ATOM   1047 N N   . THR B 1 39  ? 9.491  -14.627 -33.291 1.00 31.87  ? 39   THR B N   1 
ATOM   1048 C CA  . THR B 1 39  ? 8.742  -15.405 -34.267 1.00 33.41  ? 39   THR B CA  1 
ATOM   1049 C C   . THR B 1 39  ? 9.502  -16.710 -34.499 1.00 36.58  ? 39   THR B C   1 
ATOM   1050 O O   . THR B 1 39  ? 10.731 -16.753 -34.345 1.00 32.07  ? 39   THR B O   1 
ATOM   1051 C CB  . THR B 1 39  ? 8.582  -14.644 -35.586 1.00 41.31  ? 39   THR B CB  1 
ATOM   1052 O OG1 . THR B 1 39  ? 9.864  -14.165 -36.012 1.00 38.80  ? 39   THR B OG1 1 
ATOM   1053 C CG2 . THR B 1 39  ? 7.643  -13.461 -35.398 1.00 39.14  ? 39   THR B CG2 1 
ATOM   1054 N N   . GLU B 1 40  ? 8.774  -17.772 -34.844 1.00 40.27  ? 40   GLU B N   1 
ATOM   1055 C CA  . GLU B 1 40  ? 9.384  -19.080 -35.052 1.00 35.94  ? 40   GLU B CA  1 
ATOM   1056 C C   . GLU B 1 40  ? 10.393 -19.035 -36.191 1.00 41.90  ? 40   GLU B C   1 
ATOM   1057 O O   . GLU B 1 40  ? 10.176 -18.353 -37.194 1.00 46.86  ? 40   GLU B O   1 
ATOM   1058 C CB  . GLU B 1 40  ? 8.319  -20.151 -35.339 1.00 39.49  ? 40   GLU B CB  1 
ATOM   1059 C CG  . GLU B 1 40  ? 8.899  -21.560 -35.370 1.00 43.81  ? 40   GLU B CG  1 
ATOM   1060 C CD  . GLU B 1 40  ? 7.863  -22.641 -35.600 1.00 57.60  ? 40   GLU B CD  1 
ATOM   1061 O OE1 . GLU B 1 40  ? 6.649  -22.333 -35.585 1.00 59.27  ? 40   GLU B OE1 1 
ATOM   1062 O OE2 . GLU B 1 40  ? 8.275  -23.805 -35.791 1.00 60.71  ? 40   GLU B OE2 1 
ATOM   1063 N N   . GLY B 1 41  ? 11.496 -19.758 -36.037 1.00 46.13  ? 41   GLY B N   1 
ATOM   1064 C CA  . GLY B 1 41  ? 12.482 -19.856 -37.100 1.00 45.44  ? 41   GLY B CA  1 
ATOM   1065 C C   . GLY B 1 41  ? 13.804 -19.217 -36.725 1.00 41.48  ? 41   GLY B C   1 
ATOM   1066 O O   . GLY B 1 41  ? 14.034 -18.893 -35.564 1.00 36.25  ? 41   GLY B O   1 
ATOM   1067 N N   . LEU B 1 42  ? 14.658 -19.023 -37.722 1.00 38.92  ? 42   LEU B N   1 
ATOM   1068 C CA  . LEU B 1 42  ? 16.018 -18.522 -37.534 1.00 42.76  ? 42   LEU B CA  1 
ATOM   1069 C C   . LEU B 1 42  ? 16.079 -17.005 -37.312 1.00 42.45  ? 42   LEU B C   1 
ATOM   1070 O O   . LEU B 1 42  ? 15.336 -16.244 -37.932 1.00 41.64  ? 42   LEU B O   1 
ATOM   1071 C CB  . LEU B 1 42  ? 16.875 -18.892 -38.753 1.00 40.97  ? 42   LEU B CB  1 
ATOM   1072 C CG  . LEU B 1 42  ? 17.618 -20.234 -38.792 1.00 42.50  ? 42   LEU B CG  1 
ATOM   1073 C CD1 . LEU B 1 42  ? 16.871 -21.352 -38.101 1.00 42.03  ? 42   LEU B CD1 1 
ATOM   1074 C CD2 . LEU B 1 42  ? 17.894 -20.611 -40.243 1.00 54.97  ? 42   LEU B CD2 1 
ATOM   1075 N N   . HIS B 1 43  ? 16.977 -16.569 -36.436 1.00 33.45  ? 43   HIS B N   1 
ATOM   1076 C CA  . HIS B 1 43  ? 17.147 -15.147 -36.167 1.00 31.90  ? 43   HIS B CA  1 
ATOM   1077 C C   . HIS B 1 43  ? 18.630 -14.832 -36.067 1.00 31.34  ? 43   HIS B C   1 
ATOM   1078 O O   . HIS B 1 43  ? 19.360 -15.511 -35.340 1.00 30.27  ? 43   HIS B O   1 
ATOM   1079 C CB  . HIS B 1 43  ? 16.439 -14.745 -34.869 1.00 29.70  ? 43   HIS B CB  1 
ATOM   1080 C CG  . HIS B 1 43  ? 14.945 -14.823 -34.943 1.00 29.79  ? 43   HIS B CG  1 
ATOM   1081 N ND1 . HIS B 1 43  ? 14.156 -13.728 -35.229 1.00 31.38  ? 43   HIS B ND1 1 
ATOM   1082 C CD2 . HIS B 1 43  ? 14.095 -15.866 -34.780 1.00 30.33  ? 43   HIS B CD2 1 
ATOM   1083 C CE1 . HIS B 1 43  ? 12.885 -14.094 -35.238 1.00 33.44  ? 43   HIS B CE1 1 
ATOM   1084 N NE2 . HIS B 1 43  ? 12.821 -15.385 -34.963 1.00 31.23  ? 43   HIS B NE2 1 
ATOM   1085 N N   . GLY B 1 44  ? 19.065 -13.815 -36.812 1.00 34.71  ? 44   GLY B N   1 
ATOM   1086 C CA  . GLY B 1 44  ? 20.446 -13.360 -36.801 1.00 35.24  ? 44   GLY B CA  1 
ATOM   1087 C C   . GLY B 1 44  ? 20.843 -12.907 -35.408 1.00 32.41  ? 44   GLY B C   1 
ATOM   1088 O O   . GLY B 1 44  ? 20.064 -12.246 -34.719 1.00 32.03  ? 44   GLY B O   1 
ATOM   1089 N N   . PHE B 1 45  ? 22.055 -13.263 -35.001 1.00 28.61  ? 45   PHE B N   1 
ATOM   1090 C CA  . PHE B 1 45  ? 22.514 -13.082 -33.617 1.00 32.34  ? 45   PHE B CA  1 
ATOM   1091 C C   . PHE B 1 45  ? 23.947 -12.568 -33.698 1.00 32.40  ? 45   PHE B C   1 
ATOM   1092 O O   . PHE B 1 45  ? 24.856 -13.326 -34.083 1.00 32.72  ? 45   PHE B O   1 
ATOM   1093 C CB  . PHE B 1 45  ? 22.457 -14.441 -32.900 1.00 29.85  ? 45   PHE B CB  1 
ATOM   1094 C CG  . PHE B 1 45  ? 22.717 -14.380 -31.419 1.00 29.34  ? 45   PHE B CG  1 
ATOM   1095 C CD1 . PHE B 1 45  ? 22.176 -13.371 -30.635 1.00 24.83  ? 45   PHE B CD1 1 
ATOM   1096 C CD2 . PHE B 1 45  ? 23.482 -15.363 -30.805 1.00 35.25  ? 45   PHE B CD2 1 
ATOM   1097 C CE1 . PHE B 1 45  ? 22.419 -13.330 -29.263 1.00 28.60  ? 45   PHE B CE1 1 
ATOM   1098 C CE2 . PHE B 1 45  ? 23.718 -15.333 -29.436 1.00 34.21  ? 45   PHE B CE2 1 
ATOM   1099 C CZ  . PHE B 1 45  ? 23.185 -14.316 -28.664 1.00 31.08  ? 45   PHE B CZ  1 
ATOM   1100 N N   . HIS B 1 46  ? 24.147 -11.279 -33.403 1.00 31.04  ? 46   HIS B N   1 
ATOM   1101 C CA  . HIS B 1 46  ? 25.451 -10.625 -33.656 1.00 34.57  ? 46   HIS B CA  1 
ATOM   1102 C C   . HIS B 1 46  ? 25.903 -9.757  -32.496 1.00 23.95  ? 46   HIS B C   1 
ATOM   1103 O O   . HIS B 1 46  ? 25.093 -9.101  -31.874 1.00 24.31  ? 46   HIS B O   1 
ATOM   1104 C CB  . HIS B 1 46  ? 25.394 -9.684  -34.876 1.00 30.06  ? 46   HIS B CB  1 
ATOM   1105 C CG  . HIS B 1 46  ? 24.692 -10.250 -36.067 1.00 37.84  ? 46   HIS B CG  1 
ATOM   1106 N ND1 . HIS B 1 46  ? 24.736 -11.587 -36.396 1.00 52.06  ? 46   HIS B ND1 1 
ATOM   1107 C CD2 . HIS B 1 46  ? 23.941 -9.653  -37.019 1.00 44.50  ? 46   HIS B CD2 1 
ATOM   1108 C CE1 . HIS B 1 46  ? 24.034 -11.790 -37.499 1.00 58.28  ? 46   HIS B CE1 1 
ATOM   1109 N NE2 . HIS B 1 46  ? 23.540 -10.633 -37.897 1.00 53.17  ? 46   HIS B NE2 1 
ATOM   1110 N N   . VAL B 1 47  ? 27.202 -9.704  -32.235 1.00 33.22  ? 47   VAL B N   1 
ATOM   1111 C CA  . VAL B 1 47  ? 27.726 -8.584  -31.464 1.00 30.69  ? 47   VAL B CA  1 
ATOM   1112 C C   . VAL B 1 47  ? 27.906 -7.428  -32.450 1.00 25.89  ? 47   VAL B C   1 
ATOM   1113 O O   . VAL B 1 47  ? 28.545 -7.596  -33.483 1.00 28.36  ? 47   VAL B O   1 
ATOM   1114 C CB  . VAL B 1 47  ? 29.074 -8.900  -30.806 1.00 29.71  ? 47   VAL B CB  1 
ATOM   1115 C CG1 . VAL B 1 47  ? 29.618 -7.647  -30.114 1.00 30.63  ? 47   VAL B CG1 1 
ATOM   1116 C CG2 . VAL B 1 47  ? 28.932 -10.051 -29.811 1.00 27.19  ? 47   VAL B CG2 1 
ATOM   1117 N N   . HIS B 1 48  ? 27.336 -6.266  -32.148 1.00 23.26  ? 48   HIS B N   1 
ATOM   1118 C CA  . HIS B 1 48  ? 27.441 -5.133  -33.064 1.00 34.21  ? 48   HIS B CA  1 
ATOM   1119 C C   . HIS B 1 48  ? 28.893 -4.763  -33.347 1.00 41.68  ? 48   HIS B C   1 
ATOM   1120 O O   . HIS B 1 48  ? 29.700 -4.588  -32.435 1.00 46.54  ? 48   HIS B O   1 
ATOM   1121 C CB  . HIS B 1 48  ? 26.720 -3.886  -32.538 1.00 31.02  ? 48   HIS B CB  1 
ATOM   1122 C CG  . HIS B 1 48  ? 26.884 -2.691  -33.428 1.00 29.05  ? 48   HIS B CG  1 
ATOM   1123 N ND1 . HIS B 1 48  ? 26.225 -2.570  -34.633 1.00 34.31  ? 48   HIS B ND1 1 
ATOM   1124 C CD2 . HIS B 1 48  ? 27.674 -1.595  -33.318 1.00 28.53  ? 48   HIS B CD2 1 
ATOM   1125 C CE1 . HIS B 1 48  ? 26.583 -1.440  -35.216 1.00 34.92  ? 48   HIS B CE1 1 
ATOM   1126 N NE2 . HIS B 1 48  ? 27.459 -0.829  -34.438 1.00 39.45  ? 48   HIS B NE2 1 
ATOM   1127 N N   . GLY B 1 49  ? 29.211 -4.617  -34.620 1.00 49.88  ? 49   GLY B N   1 
ATOM   1128 C CA  . GLY B 1 49  ? 30.540 -4.217  -35.010 1.00 60.82  ? 49   GLY B CA  1 
ATOM   1129 C C   . GLY B 1 49  ? 31.168 -5.295  -35.854 1.00 69.91  ? 49   GLY B C   1 
ATOM   1130 O O   . GLY B 1 49  ? 30.474 -6.126  -36.444 1.00 72.94  ? 49   GLY B O   1 
ATOM   1131 N N   . ALA B 1 50  ? 32.492 -5.283  -35.899 1.00 72.45  ? 50   ALA B N   1 
ATOM   1132 C CA  . ALA B 1 50  ? 33.244 -6.224  -36.710 1.00 77.79  ? 50   ALA B CA  1 
ATOM   1133 C C   . ALA B 1 50  ? 33.478 -7.553  -35.975 1.00 78.09  ? 50   ALA B C   1 
ATOM   1134 O O   . ALA B 1 50  ? 33.847 -7.572  -34.796 1.00 74.73  ? 50   ALA B O   1 
ATOM   1135 C CB  . ALA B 1 50  ? 34.564 -5.588  -37.132 1.00 77.21  ? 50   ALA B CB  1 
ATOM   1136 N N   . GLY B 1 51  ? 33.252 -8.661  -36.677 1.00 77.72  ? 51   GLY B N   1 
ATOM   1137 C CA  . GLY B 1 51  ? 33.462 -9.981  -36.109 1.00 83.43  ? 51   GLY B CA  1 
ATOM   1138 C C   . GLY B 1 51  ? 32.332 -10.395 -35.198 1.00 81.32  ? 51   GLY B C   1 
ATOM   1139 O O   . GLY B 1 51  ? 32.496 -11.245 -34.322 1.00 82.27  ? 51   GLY B O   1 
ATOM   1140 N N   . GLY B 1 52  ? 31.171 -9.796  -35.417 1.00 77.50  ? 52   GLY B N   1 
ATOM   1141 C CA  . GLY B 1 52  ? 30.058 -9.978  -34.515 1.00 69.27  ? 52   GLY B CA  1 
ATOM   1142 C C   . GLY B 1 52  ? 29.274 -11.260 -34.684 1.00 65.46  ? 52   GLY B C   1 
ATOM   1143 O O   . GLY B 1 52  ? 28.508 -11.625 -33.790 1.00 57.34  ? 52   GLY B O   1 
ATOM   1144 N N   . ASP B 1 53  ? 29.459 -11.948 -35.809 1.00 62.55  ? 53   ASP B N   1 
ATOM   1145 C CA  . ASP B 1 53  ? 28.583 -13.070 -36.150 1.00 63.45  ? 53   ASP B CA  1 
ATOM   1146 C C   . ASP B 1 53  ? 28.739 -14.298 -35.256 1.00 61.04  ? 53   ASP B C   1 
ATOM   1147 O O   . ASP B 1 53  ? 29.745 -15.005 -35.308 1.00 62.72  ? 53   ASP B O   1 
ATOM   1148 C CB  . ASP B 1 53  ? 28.703 -13.462 -37.623 1.00 65.38  ? 53   ASP B CB  1 
ATOM   1149 C CG  . ASP B 1 53  ? 27.344 -13.648 -38.285 1.00 70.84  ? 53   ASP B CG  1 
ATOM   1150 O OD1 . ASP B 1 53  ? 26.355 -13.928 -37.563 1.00 69.53  ? 53   ASP B OD1 1 
ATOM   1151 O OD2 . ASP B 1 53  ? 27.263 -13.506 -39.524 1.00 72.78  ? 53   ASP B OD2 1 
ATOM   1152 N N   . LEU B 1 54  ? 27.717 -14.529 -34.440 1.00 50.63  ? 54   LEU B N   1 
ATOM   1153 C CA  . LEU B 1 54  ? 27.617 -15.722 -33.614 1.00 42.65  ? 54   LEU B CA  1 
ATOM   1154 C C   . LEU B 1 54  ? 26.613 -16.661 -34.264 1.00 41.27  ? 54   LEU B C   1 
ATOM   1155 O O   . LEU B 1 54  ? 26.109 -17.582 -33.632 1.00 43.66  ? 54   LEU B O   1 
ATOM   1156 C CB  . LEU B 1 54  ? 27.155 -15.351 -32.203 1.00 42.99  ? 54   LEU B CB  1 
ATOM   1157 C CG  . LEU B 1 54  ? 27.921 -14.181 -31.580 1.00 44.84  ? 54   LEU B CG  1 
ATOM   1158 C CD1 . LEU B 1 54  ? 27.320 -13.780 -30.236 1.00 34.93  ? 54   LEU B CD1 1 
ATOM   1159 C CD2 . LEU B 1 54  ? 29.398 -14.519 -31.451 1.00 48.62  ? 54   LEU B CD2 1 
ATOM   1160 N N   . GLY B 1 55  ? 26.317 -16.406 -35.535 1.00 50.90  ? 55   GLY B N   1 
ATOM   1161 C CA  . GLY B 1 55  ? 25.402 -17.239 -36.291 1.00 52.41  ? 55   GLY B CA  1 
ATOM   1162 C C   . GLY B 1 55  ? 23.938 -16.870 -36.126 1.00 52.53  ? 55   GLY B C   1 
ATOM   1163 O O   . GLY B 1 55  ? 23.575 -15.694 -36.058 1.00 49.82  ? 55   GLY B O   1 
ATOM   1164 N N   . ASN B 1 56  ? 23.092 -17.892 -36.091 1.00 40.83  ? 56   ASN B N   1 
ATOM   1165 C CA  . ASN B 1 56  ? 21.660 -17.703 -35.915 1.00 42.37  ? 56   ASN B CA  1 
ATOM   1166 C C   . ASN B 1 56  ? 21.210 -18.457 -34.683 1.00 40.39  ? 56   ASN B C   1 
ATOM   1167 O O   . ASN B 1 56  ? 21.771 -19.497 -34.349 1.00 41.20  ? 56   ASN B O   1 
ATOM   1168 C CB  . ASN B 1 56  ? 20.881 -18.244 -37.120 1.00 42.57  ? 56   ASN B CB  1 
ATOM   1169 C CG  . ASN B 1 56  ? 21.216 -17.528 -38.408 1.00 50.10  ? 56   ASN B CG  1 
ATOM   1170 O OD1 . ASN B 1 56  ? 21.378 -16.306 -38.435 1.00 53.10  ? 56   ASN B OD1 1 
ATOM   1171 N ND2 . ASN B 1 56  ? 21.320 -18.289 -39.493 1.00 47.15  ? 56   ASN B ND2 1 
ATOM   1172 N N   . VAL B 1 57  ? 20.202 -17.933 -34.001 1.00 31.72  ? 57   VAL B N   1 
ATOM   1173 C CA  . VAL B 1 57  ? 19.519 -18.724 -32.990 1.00 31.56  ? 57   VAL B CA  1 
ATOM   1174 C C   . VAL B 1 57  ? 18.223 -19.245 -33.621 1.00 35.49  ? 57   VAL B C   1 
ATOM   1175 O O   . VAL B 1 57  ? 17.756 -18.701 -34.620 1.00 36.24  ? 57   VAL B O   1 
ATOM   1176 C CB  . VAL B 1 57  ? 19.248 -17.905 -31.729 1.00 33.70  ? 57   VAL B CB  1 
ATOM   1177 C CG1 . VAL B 1 57  ? 20.570 -17.325 -31.190 1.00 29.01  ? 57   VAL B CG1 1 
ATOM   1178 C CG2 . VAL B 1 57  ? 18.242 -16.788 -32.011 1.00 32.40  ? 57   VAL B CG2 1 
ATOM   1179 N N   . THR B 1 58  ? 17.668 -20.325 -33.078 1.00 31.93  ? 58   THR B N   1 
ATOM   1180 C CA  . THR B 1 58  ? 16.424 -20.863 -33.605 1.00 31.56  ? 58   THR B CA  1 
ATOM   1181 C C   . THR B 1 58  ? 15.317 -20.714 -32.568 1.00 29.63  ? 58   THR B C   1 
ATOM   1182 O O   . THR B 1 58  ? 15.428 -21.239 -31.462 1.00 30.16  ? 58   THR B O   1 
ATOM   1183 C CB  . THR B 1 58  ? 16.569 -22.355 -33.997 1.00 45.86  ? 58   THR B CB  1 
ATOM   1184 O OG1 . THR B 1 58  ? 17.449 -22.469 -35.118 1.00 40.04  ? 58   THR B OG1 1 
ATOM   1185 C CG2 . THR B 1 58  ? 15.220 -22.956 -34.376 1.00 48.27  ? 58   THR B CG2 1 
ATOM   1186 N N   . ALA B 1 59  ? 14.252 -20.001 -32.928 1.00 34.48  ? 59   ALA B N   1 
ATOM   1187 C CA  . ALA B 1 59  ? 13.078 -19.884 -32.068 1.00 32.08  ? 59   ALA B CA  1 
ATOM   1188 C C   . ALA B 1 59  ? 12.062 -20.980 -32.383 1.00 38.31  ? 59   ALA B C   1 
ATOM   1189 O O   . ALA B 1 59  ? 11.736 -21.229 -33.546 1.00 36.03  ? 59   ALA B O   1 
ATOM   1190 C CB  . ALA B 1 59  ? 12.444 -18.509 -32.212 1.00 34.53  ? 59   ALA B CB  1 
ATOM   1191 N N   . ASP B 1 60  ? 11.563 -21.645 -31.346 1.00 38.87  ? 60   ASP B N   1 
ATOM   1192 C CA  . ASP B 1 60  ? 10.598 -22.715 -31.558 1.00 40.43  ? 60   ASP B CA  1 
ATOM   1193 C C   . ASP B 1 60  ? 9.187  -22.154 -31.724 1.00 41.01  ? 60   ASP B C   1 
ATOM   1194 O O   . ASP B 1 60  ? 8.992  -20.938 -31.797 1.00 34.05  ? 60   ASP B O   1 
ATOM   1195 C CB  . ASP B 1 60  ? 10.642 -23.732 -30.410 1.00 36.14  ? 60   ASP B CB  1 
ATOM   1196 C CG  . ASP B 1 60  ? 10.362 -23.109 -29.047 1.00 35.85  ? 60   ASP B CG  1 
ATOM   1197 O OD1 . ASP B 1 60  ? 9.707  -22.040 -28.957 1.00 33.56  ? 60   ASP B OD1 1 
ATOM   1198 O OD2 . ASP B 1 60  ? 10.808 -23.705 -28.041 1.00 40.88  ? 60   ASP B OD2 1 
ATOM   1199 N N   . LYS B 1 61  ? 8.210  -23.054 -31.748 1.00 36.78  ? 61   LYS B N   1 
ATOM   1200 C CA  . LYS B 1 61  ? 6.805  -22.686 -31.860 1.00 40.62  ? 61   LYS B CA  1 
ATOM   1201 C C   . LYS B 1 61  ? 6.273  -21.883 -30.666 1.00 35.89  ? 61   LYS B C   1 
ATOM   1202 O O   . LYS B 1 61  ? 5.171  -21.338 -30.732 1.00 37.80  ? 61   LYS B O   1 
ATOM   1203 C CB  . LYS B 1 61  ? 5.960  -23.946 -32.052 1.00 48.84  ? 61   LYS B CB  1 
ATOM   1204 C CG  . LYS B 1 61  ? 5.064  -23.882 -33.266 1.00 62.88  ? 61   LYS B CG  1 
ATOM   1205 C CD  . LYS B 1 61  ? 4.444  -25.239 -33.584 1.00 70.01  ? 61   LYS B CD  1 
ATOM   1206 C CE  . LYS B 1 61  ? 3.903  -25.260 -35.005 1.00 68.32  ? 61   LYS B CE  1 
ATOM   1207 N NZ  . LYS B 1 61  ? 4.950  -24.839 -35.981 1.00 65.32  ? 61   LYS B NZ  1 
ATOM   1208 N N   . ASP B 1 62  ? 7.037  -21.818 -29.575 1.00 31.49  ? 62   ASP B N   1 
ATOM   1209 C CA  . ASP B 1 62  ? 6.645  -20.992 -28.432 1.00 32.05  ? 62   ASP B CA  1 
ATOM   1210 C C   . ASP B 1 62  ? 7.365  -19.649 -28.482 1.00 31.35  ? 62   ASP B C   1 
ATOM   1211 O O   . ASP B 1 62  ? 7.222  -18.818 -27.585 1.00 31.40  ? 62   ASP B O   1 
ATOM   1212 C CB  . ASP B 1 62  ? 6.961  -21.685 -27.105 1.00 36.57  ? 62   ASP B CB  1 
ATOM   1213 C CG  . ASP B 1 62  ? 6.253  -23.016 -26.949 1.00 37.34  ? 62   ASP B CG  1 
ATOM   1214 O OD1 . ASP B 1 62  ? 5.151  -23.192 -27.509 1.00 38.36  ? 62   ASP B OD1 1 
ATOM   1215 O OD2 . ASP B 1 62  ? 6.809  -23.886 -26.252 1.00 39.97  ? 62   ASP B OD2 1 
ATOM   1216 N N   . GLY B 1 63  ? 8.145  -19.436 -29.536 1.00 28.52  ? 63   GLY B N   1 
ATOM   1217 C CA  . GLY B 1 63  ? 8.892  -18.202 -29.660 1.00 26.00  ? 63   GLY B CA  1 
ATOM   1218 C C   . GLY B 1 63  ? 10.126 -18.175 -28.776 1.00 25.17  ? 63   GLY B C   1 
ATOM   1219 O O   . GLY B 1 63  ? 10.709 -17.118 -28.528 1.00 28.55  ? 63   GLY B O   1 
ATOM   1220 N N   . VAL B 1 64  ? 10.543 -19.341 -28.304 1.00 26.36  ? 64   VAL B N   1 
ATOM   1221 C CA  . VAL B 1 64  ? 11.698 -19.411 -27.426 1.00 29.12  ? 64   VAL B CA  1 
ATOM   1222 C C   . VAL B 1 64  ? 12.923 -19.949 -28.149 1.00 30.73  ? 64   VAL B C   1 
ATOM   1223 O O   . VAL B 1 64  ? 12.863 -20.984 -28.813 1.00 31.26  ? 64   VAL B O   1 
ATOM   1224 C CB  . VAL B 1 64  ? 11.404 -20.269 -26.182 1.00 31.89  ? 64   VAL B CB  1 
ATOM   1225 C CG1 . VAL B 1 64  ? 12.641 -20.373 -25.302 1.00 26.79  ? 64   VAL B CG1 1 
ATOM   1226 C CG2 . VAL B 1 64  ? 10.247 -19.662 -25.396 1.00 32.39  ? 64   VAL B CG2 1 
ATOM   1227 N N   . ALA B 1 65  ? 14.033 -19.228 -28.034 1.00 32.09  ? 65   ALA B N   1 
ATOM   1228 C CA  . ALA B 1 65  ? 15.292 -19.712 -28.590 1.00 35.01  ? 65   ALA B CA  1 
ATOM   1229 C C   . ALA B 1 65  ? 16.284 -19.985 -27.463 1.00 29.31  ? 65   ALA B C   1 
ATOM   1230 O O   . ALA B 1 65  ? 16.653 -19.086 -26.711 1.00 32.89  ? 65   ALA B O   1 
ATOM   1231 C CB  . ALA B 1 65  ? 15.869 -18.708 -29.593 1.00 31.53  ? 65   ALA B CB  1 
ATOM   1232 N N   . ASP B 1 66  ? 16.696 -21.238 -27.337 1.00 27.25  ? 66   ASP B N   1 
ATOM   1233 C CA  . ASP B 1 66  ? 17.725 -21.592 -26.377 1.00 27.28  ? 66   ASP B CA  1 
ATOM   1234 C C   . ASP B 1 66  ? 19.065 -21.392 -27.070 1.00 32.10  ? 66   ASP B C   1 
ATOM   1235 O O   . ASP B 1 66  ? 19.230 -21.768 -28.224 1.00 35.85  ? 66   ASP B O   1 
ATOM   1236 C CB  . ASP B 1 66  ? 17.582 -23.045 -25.934 1.00 31.18  ? 66   ASP B CB  1 
ATOM   1237 C CG  . ASP B 1 66  ? 16.410 -23.250 -25.015 1.00 32.27  ? 66   ASP B CG  1 
ATOM   1238 O OD1 . ASP B 1 66  ? 16.297 -22.497 -24.023 1.00 31.78  ? 66   ASP B OD1 1 
ATOM   1239 O OD2 . ASP B 1 66  ? 15.598 -24.160 -25.287 1.00 43.36  ? 66   ASP B OD2 1 
ATOM   1240 N N   . VAL B 1 67  ? 20.009 -20.789 -26.359 1.00 25.37  ? 67   VAL B N   1 
ATOM   1241 C CA  . VAL B 1 67  ? 21.311 -20.478 -26.911 1.00 29.22  ? 67   VAL B CA  1 
ATOM   1242 C C   . VAL B 1 67  ? 22.391 -21.191 -26.119 1.00 29.65  ? 67   VAL B C   1 
ATOM   1243 O O   . VAL B 1 67  ? 22.438 -21.085 -24.893 1.00 27.77  ? 67   VAL B O   1 
ATOM   1244 C CB  . VAL B 1 67  ? 21.581 -18.967 -26.844 1.00 30.10  ? 67   VAL B CB  1 
ATOM   1245 C CG1 . VAL B 1 67  ? 22.959 -18.631 -27.482 1.00 25.31  ? 67   VAL B CG1 1 
ATOM   1246 C CG2 . VAL B 1 67  ? 20.459 -18.202 -27.521 1.00 22.71  ? 67   VAL B CG2 1 
ATOM   1247 N N   . SER B 1 68  ? 23.253 -21.919 -26.822 1.00 33.24  ? 68   SER B N   1 
ATOM   1248 C CA  . SER B 1 68  ? 24.418 -22.530 -26.202 1.00 27.76  ? 68   SER B CA  1 
ATOM   1249 C C   . SER B 1 68  ? 25.497 -22.750 -27.248 1.00 34.73  ? 68   SER B C   1 
ATOM   1250 O O   . SER B 1 68  ? 25.616 -23.842 -27.792 1.00 36.77  ? 68   SER B O   1 
ATOM   1251 C CB  . SER B 1 68  ? 24.057 -23.857 -25.543 1.00 49.98  ? 68   SER B CB  1 
ATOM   1252 O OG  . SER B 1 68  ? 25.157 -24.345 -24.796 1.00 51.07  ? 68   SER B OG  1 
ATOM   1253 N N   . ILE B 1 69  ? 26.265 -21.696 -27.506 1.00 34.78  ? 69   ILE B N   1 
ATOM   1254 C CA  . ILE B 1 69  ? 27.343 -21.664 -28.490 1.00 40.26  ? 69   ILE B CA  1 
ATOM   1255 C C   . ILE B 1 69  ? 28.701 -21.591 -27.790 1.00 46.80  ? 69   ILE B C   1 
ATOM   1256 O O   . ILE B 1 69  ? 28.785 -21.290 -26.601 1.00 38.20  ? 69   ILE B O   1 
ATOM   1257 C CB  . ILE B 1 69  ? 27.238 -20.374 -29.354 1.00 60.12  ? 69   ILE B CB  1 
ATOM   1258 C CG1 . ILE B 1 69  ? 25.784 -20.041 -29.672 1.00 65.63  ? 69   ILE B CG1 1 
ATOM   1259 C CG2 . ILE B 1 69  ? 28.033 -20.483 -30.647 1.00 68.47  ? 69   ILE B CG2 1 
ATOM   1260 C CD1 . ILE B 1 69  ? 25.623 -18.758 -30.474 1.00 62.06  ? 69   ILE B CD1 1 
ATOM   1261 N N   . GLU B 1 70  ? 29.762 -21.859 -28.549 1.00 43.46  ? 70   GLU B N   1 
ATOM   1262 C CA  . GLU B 1 70  ? 31.133 -21.564 -28.144 1.00 50.77  ? 70   GLU B CA  1 
ATOM   1263 C C   . GLU B 1 70  ? 31.838 -20.892 -29.322 1.00 49.62  ? 70   GLU B C   1 
ATOM   1264 O O   . GLU B 1 70  ? 31.939 -21.488 -30.393 1.00 59.29  ? 70   GLU B O   1 
ATOM   1265 C CB  . GLU B 1 70  ? 31.865 -22.847 -27.746 1.00 54.81  ? 70   GLU B CB  1 
ATOM   1266 C CG  . GLU B 1 70  ? 33.379 -22.734 -27.765 1.00 63.37  ? 70   GLU B CG  1 
ATOM   1267 C CD  . GLU B 1 70  ? 34.071 -24.027 -27.351 1.00 73.83  ? 70   GLU B CD  1 
ATOM   1268 O OE1 . GLU B 1 70  ? 33.682 -24.588 -26.305 1.00 73.41  ? 70   GLU B OE1 1 
ATOM   1269 O OE2 . GLU B 1 70  ? 35.004 -24.477 -28.063 1.00 77.61  ? 70   GLU B OE2 1 
ATOM   1270 N N   . ASP B 1 71  ? 32.304 -19.656 -29.131 1.00 43.35  ? 71   ASP B N   1 
ATOM   1271 C CA  . ASP B 1 71  ? 32.935 -18.879 -30.207 1.00 50.62  ? 71   ASP B CA  1 
ATOM   1272 C C   . ASP B 1 71  ? 34.407 -18.566 -29.922 1.00 51.05  ? 71   ASP B C   1 
ATOM   1273 O O   . ASP B 1 71  ? 34.757 -18.215 -28.798 1.00 41.13  ? 71   ASP B O   1 
ATOM   1274 C CB  . ASP B 1 71  ? 32.171 -17.565 -30.433 1.00 48.98  ? 71   ASP B CB  1 
ATOM   1275 C CG  . ASP B 1 71  ? 32.601 -16.845 -31.704 1.00 52.95  ? 71   ASP B CG  1 
ATOM   1276 O OD1 . ASP B 1 71  ? 32.047 -17.153 -32.779 1.00 64.06  ? 71   ASP B OD1 1 
ATOM   1277 O OD2 . ASP B 1 71  ? 33.488 -15.969 -31.634 1.00 44.27  ? 71   ASP B OD2 1 
ATOM   1278 N N   . SER B 1 72  ? 35.260 -18.667 -30.944 1.00 52.60  ? 72   SER B N   1 
ATOM   1279 C CA  . SER B 1 72  ? 36.703 -18.448 -30.769 1.00 51.81  ? 72   SER B CA  1 
ATOM   1280 C C   . SER B 1 72  ? 37.209 -17.102 -31.302 1.00 56.09  ? 72   SER B C   1 
ATOM   1281 O O   . SER B 1 72  ? 38.381 -16.762 -31.132 1.00 62.41  ? 72   SER B O   1 
ATOM   1282 C CB  . SER B 1 72  ? 37.510 -19.588 -31.403 1.00 59.73  ? 72   SER B CB  1 
ATOM   1283 O OG  . SER B 1 72  ? 37.624 -20.695 -30.523 1.00 61.13  ? 72   SER B OG  1 
ATOM   1284 N N   . VAL B 1 73  ? 36.334 -16.342 -31.953 1.00 52.32  ? 73   VAL B N   1 
ATOM   1285 C CA  . VAL B 1 73  ? 36.707 -15.029 -32.472 1.00 57.57  ? 73   VAL B CA  1 
ATOM   1286 C C   . VAL B 1 73  ? 36.533 -13.934 -31.413 1.00 51.99  ? 73   VAL B C   1 
ATOM   1287 O O   . VAL B 1 73  ? 37.329 -12.992 -31.335 1.00 56.42  ? 73   VAL B O   1 
ATOM   1288 C CB  . VAL B 1 73  ? 35.903 -14.681 -33.751 1.00 73.75  ? 73   VAL B CB  1 
ATOM   1289 C CG1 . VAL B 1 73  ? 36.164 -13.244 -34.197 1.00 70.37  ? 73   VAL B CG1 1 
ATOM   1290 C CG2 . VAL B 1 73  ? 36.244 -15.654 -34.864 1.00 75.40  ? 73   VAL B CG2 1 
ATOM   1291 N N   . ILE B 1 74  ? 35.498 -14.069 -30.592 1.00 50.77  ? 74   ILE B N   1 
ATOM   1292 C CA  . ILE B 1 74  ? 35.216 -13.093 -29.543 1.00 44.03  ? 74   ILE B CA  1 
ATOM   1293 C C   . ILE B 1 74  ? 36.014 -13.382 -28.272 1.00 37.42  ? 74   ILE B C   1 
ATOM   1294 O O   . ILE B 1 74  ? 36.441 -14.511 -28.042 1.00 36.43  ? 74   ILE B O   1 
ATOM   1295 C CB  . ILE B 1 74  ? 33.717 -13.074 -29.187 1.00 42.18  ? 74   ILE B CB  1 
ATOM   1296 C CG1 . ILE B 1 74  ? 33.257 -14.469 -28.756 1.00 39.45  ? 74   ILE B CG1 1 
ATOM   1297 C CG2 . ILE B 1 74  ? 32.897 -12.579 -30.369 1.00 41.22  ? 74   ILE B CG2 1 
ATOM   1298 C CD1 . ILE B 1 74  ? 31.905 -14.478 -28.075 1.00 38.40  ? 74   ILE B CD1 1 
ATOM   1299 N N   . SER B 1 75  ? 36.209 -12.349 -27.457 1.00 32.57  ? 75   SER B N   1 
ATOM   1300 C CA  . SER B 1 75  ? 36.905 -12.478 -26.178 1.00 32.97  ? 75   SER B CA  1 
ATOM   1301 C C   . SER B 1 75  ? 36.268 -11.540 -25.158 1.00 30.76  ? 75   SER B C   1 
ATOM   1302 O O   . SER B 1 75  ? 35.535 -10.619 -25.532 1.00 29.54  ? 75   SER B O   1 
ATOM   1303 C CB  . SER B 1 75  ? 38.389 -12.132 -26.336 1.00 37.06  ? 75   SER B CB  1 
ATOM   1304 O OG  . SER B 1 75  ? 39.076 -12.332 -25.114 1.00 36.76  ? 75   SER B OG  1 
ATOM   1305 N N   . LEU B 1 76  ? 36.541 -11.770 -23.876 1.00 31.78  ? 76   LEU B N   1 
ATOM   1306 C CA  . LEU B 1 76  ? 36.018 -10.908 -22.817 1.00 31.64  ? 76   LEU B CA  1 
ATOM   1307 C C   . LEU B 1 76  ? 37.133 -10.066 -22.188 1.00 36.49  ? 76   LEU B C   1 
ATOM   1308 O O   . LEU B 1 76  ? 36.925 -9.409  -21.168 1.00 33.10  ? 76   LEU B O   1 
ATOM   1309 C CB  . LEU B 1 76  ? 35.324 -11.726 -21.721 1.00 31.10  ? 76   LEU B CB  1 
ATOM   1310 C CG  . LEU B 1 76  ? 34.151 -12.613 -22.148 1.00 29.38  ? 76   LEU B CG  1 
ATOM   1311 C CD1 . LEU B 1 76  ? 33.558 -13.358 -20.953 1.00 29.41  ? 76   LEU B CD1 1 
ATOM   1312 C CD2 . LEU B 1 76  ? 33.096 -11.778 -22.837 1.00 25.12  ? 76   LEU B CD2 1 
ATOM   1313 N N   . SER B 1 77  ? 38.316 -10.096 -22.791 1.00 31.21  ? 77   SER B N   1 
ATOM   1314 C CA  . SER B 1 77  ? 39.408 -9.226  -22.355 1.00 41.66  ? 77   SER B CA  1 
ATOM   1315 C C   . SER B 1 77  ? 40.266 -8.842  -23.553 1.00 41.86  ? 77   SER B C   1 
ATOM   1316 O O   . SER B 1 77  ? 39.984 -9.270  -24.669 1.00 40.51  ? 77   SER B O   1 
ATOM   1317 C CB  . SER B 1 77  ? 40.261 -9.910  -21.283 1.00 48.23  ? 77   SER B CB  1 
ATOM   1318 O OG  . SER B 1 77  ? 40.846 -11.104 -21.772 1.00 54.72  ? 77   SER B OG  1 
ATOM   1319 N N   . GLY B 1 78  ? 41.298 -8.029  -23.332 1.00 44.16  ? 78   GLY B N   1 
ATOM   1320 C CA  . GLY B 1 78  ? 42.218 -7.672  -24.401 1.00 38.55  ? 78   GLY B CA  1 
ATOM   1321 C C   . GLY B 1 78  ? 41.597 -6.679  -25.358 1.00 46.30  ? 78   GLY B C   1 
ATOM   1322 O O   . GLY B 1 78  ? 40.525 -6.146  -25.077 1.00 37.54  ? 78   GLY B O   1 
ATOM   1323 N N   . ASP B 1 79  ? 42.259 -6.427  -26.488 1.00 51.39  ? 79   ASP B N   1 
ATOM   1324 C CA  . ASP B 1 79  ? 41.777 -5.438  -27.459 1.00 51.03  ? 79   ASP B CA  1 
ATOM   1325 C C   . ASP B 1 79  ? 40.503 -5.869  -28.193 1.00 53.47  ? 79   ASP B C   1 
ATOM   1326 O O   . ASP B 1 79  ? 39.679 -5.030  -28.547 1.00 67.03  ? 79   ASP B O   1 
ATOM   1327 C CB  . ASP B 1 79  ? 42.870 -5.081  -28.469 1.00 66.88  ? 79   ASP B CB  1 
ATOM   1328 C CG  . ASP B 1 79  ? 44.084 -4.443  -27.816 1.00 72.34  ? 79   ASP B CG  1 
ATOM   1329 O OD1 . ASP B 1 79  ? 43.946 -3.888  -26.703 1.00 73.27  ? 79   ASP B OD1 1 
ATOM   1330 O OD2 . ASP B 1 79  ? 45.175 -4.496  -28.422 1.00 71.94  ? 79   ASP B OD2 1 
ATOM   1331 N N   . HIS B 1 80  ? 40.335 -7.169  -28.416 1.00 51.69  ? 80   HIS B N   1 
ATOM   1332 C CA  . HIS B 1 80  ? 39.123 -7.685  -29.062 1.00 57.16  ? 80   HIS B CA  1 
ATOM   1333 C C   . HIS B 1 80  ? 37.885 -7.678  -28.153 1.00 48.14  ? 80   HIS B C   1 
ATOM   1334 O O   . HIS B 1 80  ? 36.784 -7.940  -28.631 1.00 47.10  ? 80   HIS B O   1 
ATOM   1335 C CB  . HIS B 1 80  ? 39.326 -9.128  -29.551 1.00 74.64  ? 80   HIS B CB  1 
ATOM   1336 C CG  . HIS B 1 80  ? 40.028 -9.247  -30.869 1.00 86.01  ? 80   HIS B CG  1 
ATOM   1337 N ND1 . HIS B 1 80  ? 40.652 -10.410 -31.271 1.00 88.08  ? 80   HIS B ND1 1 
ATOM   1338 C CD2 . HIS B 1 80  ? 40.189 -8.364  -31.883 1.00 90.13  ? 80   HIS B CD2 1 
ATOM   1339 C CE1 . HIS B 1 80  ? 41.177 -10.234 -32.470 1.00 91.56  ? 80   HIS B CE1 1 
ATOM   1340 N NE2 . HIS B 1 80  ? 40.910 -9.002  -32.864 1.00 93.39  ? 80   HIS B NE2 1 
ATOM   1341 N N   . SER B 1 81  ? 38.065 -7.405  -26.859 1.00 43.90  ? 81   SER B N   1 
ATOM   1342 C CA  . SER B 1 81  ? 36.990 -7.580  -25.860 1.00 35.53  ? 81   SER B CA  1 
ATOM   1343 C C   . SER B 1 81  ? 35.617 -7.066  -26.285 1.00 30.45  ? 81   SER B C   1 
ATOM   1344 O O   . SER B 1 81  ? 35.491 -5.952  -26.785 1.00 30.49  ? 81   SER B O   1 
ATOM   1345 C CB  . SER B 1 81  ? 37.363 -6.951  -24.511 1.00 30.98  ? 81   SER B CB  1 
ATOM   1346 O OG  . SER B 1 81  ? 36.326 -7.185  -23.559 1.00 33.53  ? 81   SER B OG  1 
ATOM   1347 N N   . ILE B 1 82  ? 34.585 -7.882  -26.075 1.00 24.41  ? 82   ILE B N   1 
ATOM   1348 C CA  . ILE B 1 82  ? 33.218 -7.472  -26.402 1.00 22.41  ? 82   ILE B CA  1 
ATOM   1349 C C   . ILE B 1 82  ? 32.473 -6.826  -25.242 1.00 21.51  ? 82   ILE B C   1 
ATOM   1350 O O   . ILE B 1 82  ? 31.300 -6.474  -25.382 1.00 24.42  ? 82   ILE B O   1 
ATOM   1351 C CB  . ILE B 1 82  ? 32.368 -8.643  -26.908 1.00 22.72  ? 82   ILE B CB  1 
ATOM   1352 C CG1 . ILE B 1 82  ? 32.169 -9.665  -25.799 1.00 24.64  ? 82   ILE B CG1 1 
ATOM   1353 C CG2 . ILE B 1 82  ? 33.025 -9.280  -28.132 1.00 34.15  ? 82   ILE B CG2 1 
ATOM   1354 C CD1 . ILE B 1 82  ? 31.348 -10.884 -26.231 1.00 30.88  ? 82   ILE B CD1 1 
ATOM   1355 N N   . ILE B 1 83  ? 33.130 -6.681  -24.094 1.00 28.25  ? 83   ILE B N   1 
ATOM   1356 C CA  . ILE B 1 83  ? 32.506 -6.001  -22.957 1.00 28.26  ? 83   ILE B CA  1 
ATOM   1357 C C   . ILE B 1 83  ? 32.187 -4.567  -23.370 1.00 20.68  ? 83   ILE B C   1 
ATOM   1358 O O   . ILE B 1 83  ? 33.054 -3.884  -23.888 1.00 19.21  ? 83   ILE B O   1 
ATOM   1359 C CB  . ILE B 1 83  ? 33.464 -5.920  -21.748 1.00 33.55  ? 83   ILE B CB  1 
ATOM   1360 C CG1 . ILE B 1 83  ? 33.928 -7.315  -21.319 1.00 35.57  ? 83   ILE B CG1 1 
ATOM   1361 C CG2 . ILE B 1 83  ? 32.796 -5.176  -20.582 1.00 20.23  ? 83   ILE B CG2 1 
ATOM   1362 C CD1 . ILE B 1 83  ? 32.816 -8.181  -20.802 1.00 32.52  ? 83   ILE B CD1 1 
ATOM   1363 N N   . GLY B 1 84  ? 30.958 -4.112  -23.124 1.00 18.50  ? 84   GLY B N   1 
ATOM   1364 C CA  . GLY B 1 84  ? 30.566 -2.754  -23.483 1.00 22.67  ? 84   GLY B CA  1 
ATOM   1365 C C   . GLY B 1 84  ? 30.072 -2.627  -24.913 1.00 24.32  ? 84   GLY B C   1 
ATOM   1366 O O   . GLY B 1 84  ? 29.653 -1.546  -25.371 1.00 19.40  ? 84   GLY B O   1 
ATOM   1367 N N   . ARG B 1 85  ? 30.148 -3.733  -25.643 1.00 23.75  ? 85   ARG B N   1 
ATOM   1368 C CA  . ARG B 1 85  ? 29.599 -3.773  -26.989 1.00 22.94  ? 85   ARG B CA  1 
ATOM   1369 C C   . ARG B 1 85  ? 28.133 -4.193  -26.900 1.00 22.06  ? 85   ARG B C   1 
ATOM   1370 O O   . ARG B 1 85  ? 27.678 -4.755  -25.891 1.00 20.62  ? 85   ARG B O   1 
ATOM   1371 C CB  . ARG B 1 85  ? 30.368 -4.763  -27.862 1.00 21.48  ? 85   ARG B CB  1 
ATOM   1372 C CG  . ARG B 1 85  ? 31.847 -4.454  -28.030 1.00 30.82  ? 85   ARG B CG  1 
ATOM   1373 C CD  . ARG B 1 85  ? 32.094 -3.326  -28.992 1.00 38.17  ? 85   ARG B CD  1 
ATOM   1374 N NE  . ARG B 1 85  ? 33.524 -3.188  -29.279 1.00 50.07  ? 85   ARG B NE  1 
ATOM   1375 C CZ  . ARG B 1 85  ? 34.078 -2.109  -29.819 1.00 51.80  ? 85   ARG B CZ  1 
ATOM   1376 N NH1 . ARG B 1 85  ? 33.327 -1.058  -30.135 1.00 51.54  ? 85   ARG B NH1 1 
ATOM   1377 N NH2 . ARG B 1 85  ? 35.385 -2.076  -30.035 1.00 56.38  ? 85   ARG B NH2 1 
ATOM   1378 N N   . THR B 1 86  ? 27.382 -3.936  -27.960 1.00 22.85  ? 86   THR B N   1 
ATOM   1379 C CA  . THR B 1 86  ? 25.969 -4.286  -27.936 1.00 20.83  ? 86   THR B CA  1 
ATOM   1380 C C   . THR B 1 86  ? 25.702 -5.620  -28.632 1.00 17.67  ? 86   THR B C   1 
ATOM   1381 O O   . THR B 1 86  ? 26.145 -5.860  -29.754 1.00 23.23  ? 86   THR B O   1 
ATOM   1382 C CB  . THR B 1 86  ? 25.112 -3.159  -28.548 1.00 29.34  ? 86   THR B CB  1 
ATOM   1383 O OG1 . THR B 1 86  ? 25.255 -1.981  -27.743 1.00 28.31  ? 86   THR B OG1 1 
ATOM   1384 C CG2 . THR B 1 86  ? 23.642 -3.561  -28.595 1.00 22.52  ? 86   THR B CG2 1 
ATOM   1385 N N   . LEU B 1 87  ? 24.980 -6.484  -27.934 1.00 23.42  ? 87   LEU B N   1 
ATOM   1386 C CA  . LEU B 1 87  ? 24.523 -7.743  -28.476 1.00 24.33  ? 87   LEU B CA  1 
ATOM   1387 C C   . LEU B 1 87  ? 23.162 -7.494  -29.102 1.00 26.38  ? 87   LEU B C   1 
ATOM   1388 O O   . LEU B 1 87  ? 22.311 -6.805  -28.528 1.00 22.12  ? 87   LEU B O   1 
ATOM   1389 C CB  . LEU B 1 87  ? 24.398 -8.786  -27.357 1.00 17.48  ? 87   LEU B CB  1 
ATOM   1390 C CG  . LEU B 1 87  ? 23.987 -10.195 -27.808 1.00 19.52  ? 87   LEU B CG  1 
ATOM   1391 C CD1 . LEU B 1 87  ? 25.000 -10.784 -28.810 1.00 20.95  ? 87   LEU B CD1 1 
ATOM   1392 C CD2 . LEU B 1 87  ? 23.801 -11.130 -26.625 1.00 15.91  ? 87   LEU B CD2 1 
ATOM   1393 N N   . VAL B 1 88  ? 22.966 -8.081  -30.276 1.00 25.03  ? 88   VAL B N   1 
ATOM   1394 C CA  . VAL B 1 88  ? 21.785 -7.839  -31.080 1.00 24.01  ? 88   VAL B CA  1 
ATOM   1395 C C   . VAL B 1 88  ? 21.185 -9.164  -31.570 1.00 27.03  ? 88   VAL B C   1 
ATOM   1396 O O   . VAL B 1 88  ? 21.920 -10.102 -31.899 1.00 26.39  ? 88   VAL B O   1 
ATOM   1397 C CB  . VAL B 1 88  ? 22.182 -6.919  -32.269 1.00 38.68  ? 88   VAL B CB  1 
ATOM   1398 C CG1 . VAL B 1 88  ? 21.521 -7.337  -33.553 1.00 43.79  ? 88   VAL B CG1 1 
ATOM   1399 C CG2 . VAL B 1 88  ? 21.903 -5.458  -31.928 1.00 39.86  ? 88   VAL B CG2 1 
ATOM   1400 N N   . VAL B 1 89  ? 19.854 -9.254  -31.576 1.00 21.45  ? 89   VAL B N   1 
ATOM   1401 C CA  . VAL B 1 89  ? 19.164 -10.331 -32.287 1.00 23.79  ? 89   VAL B CA  1 
ATOM   1402 C C   . VAL B 1 89  ? 18.139 -9.717  -33.242 1.00 25.20  ? 89   VAL B C   1 
ATOM   1403 O O   . VAL B 1 89  ? 17.393 -8.801  -32.850 1.00 26.06  ? 89   VAL B O   1 
ATOM   1404 C CB  . VAL B 1 89  ? 18.507 -11.364 -31.303 1.00 34.70  ? 89   VAL B CB  1 
ATOM   1405 C CG1 . VAL B 1 89  ? 17.569 -10.685 -30.347 1.00 25.86  ? 89   VAL B CG1 1 
ATOM   1406 C CG2 . VAL B 1 89  ? 17.771 -12.473 -32.054 1.00 22.68  ? 89   VAL B CG2 1 
ATOM   1407 N N   . HIS B 1 90  ? 18.124 -10.188 -34.498 1.00 26.46  ? 90   HIS B N   1 
ATOM   1408 C CA  . HIS B 1 90  ? 17.104 -9.761  -35.459 1.00 28.78  ? 90   HIS B CA  1 
ATOM   1409 C C   . HIS B 1 90  ? 15.741 -10.299 -35.057 1.00 30.84  ? 90   HIS B C   1 
ATOM   1410 O O   . HIS B 1 90  ? 15.595 -11.499 -34.795 1.00 35.55  ? 90   HIS B O   1 
ATOM   1411 C CB  . HIS B 1 90  ? 17.411 -10.240 -36.886 1.00 31.82  ? 90   HIS B CB  1 
ATOM   1412 C CG  . HIS B 1 90  ? 18.524 -9.497  -37.553 1.00 34.04  ? 90   HIS B CG  1 
ATOM   1413 N ND1 . HIS B 1 90  ? 18.649 -9.425  -38.924 1.00 43.91  ? 90   HIS B ND1 1 
ATOM   1414 C CD2 . HIS B 1 90  ? 19.577 -8.818  -37.042 1.00 31.98  ? 90   HIS B CD2 1 
ATOM   1415 C CE1 . HIS B 1 90  ? 19.725 -8.722  -39.228 1.00 41.26  ? 90   HIS B CE1 1 
ATOM   1416 N NE2 . HIS B 1 90  ? 20.307 -8.342  -38.106 1.00 34.96  ? 90   HIS B NE2 1 
ATOM   1417 N N   . GLU B 1 91  ? 14.745 -9.419  -35.011 1.00 31.04  ? 91   GLU B N   1 
ATOM   1418 C CA  . GLU B 1 91  ? 13.382 -9.835  -34.702 1.00 30.63  ? 91   GLU B CA  1 
ATOM   1419 C C   . GLU B 1 91  ? 12.685 -10.436 -35.926 1.00 32.95  ? 91   GLU B C   1 
ATOM   1420 O O   . GLU B 1 91  ? 11.802 -11.282 -35.791 1.00 33.52  ? 91   GLU B O   1 
ATOM   1421 C CB  . GLU B 1 91  ? 12.578 -8.672  -34.117 1.00 34.52  ? 91   GLU B CB  1 
ATOM   1422 C CG  . GLU B 1 91  ? 13.109 -8.204  -32.761 1.00 30.55  ? 91   GLU B CG  1 
ATOM   1423 C CD  . GLU B 1 91  ? 12.339 -7.026  -32.181 1.00 36.13  ? 91   GLU B CD  1 
ATOM   1424 O OE1 . GLU B 1 91  ? 11.730 -6.266  -32.964 1.00 42.43  ? 91   GLU B OE1 1 
ATOM   1425 O OE2 . GLU B 1 91  ? 12.333 -6.869  -30.935 1.00 30.52  ? 91   GLU B OE2 1 
ATOM   1426 N N   . LYS B 1 92  ? 13.091 -10.012 -37.118 1.00 35.15  ? 92   LYS B N   1 
ATOM   1427 C CA  . LYS B 1 92  ? 12.576 -10.632 -38.336 1.00 38.51  ? 92   LYS B CA  1 
ATOM   1428 C C   . LYS B 1 92  ? 13.298 -11.953 -38.575 1.00 38.47  ? 92   LYS B C   1 
ATOM   1429 O O   . LYS B 1 92  ? 14.528 -11.999 -38.613 1.00 43.49  ? 92   LYS B O   1 
ATOM   1430 C CB  . LYS B 1 92  ? 12.733 -9.697  -39.540 1.00 42.16  ? 92   LYS B CB  1 
ATOM   1431 C CG  . LYS B 1 92  ? 12.181 -10.249 -40.848 1.00 47.14  ? 92   LYS B CG  1 
ATOM   1432 C CD  . LYS B 1 92  ? 11.962 -9.129  -41.871 1.00 51.78  ? 92   LYS B CD  1 
ATOM   1433 C CE  . LYS B 1 92  ? 12.813 -9.313  -43.120 1.00 67.94  ? 92   LYS B CE  1 
ATOM   1434 N NZ  . LYS B 1 92  ? 14.262 -9.099  -42.842 1.00 75.41  ? 92   LYS B NZ  1 
ATOM   1435 N N   . ALA B 1 93  ? 12.529 -13.029 -38.711 1.00 42.49  ? 93   ALA B N   1 
ATOM   1436 C CA  . ALA B 1 93  ? 13.097 -14.347 -38.982 1.00 44.72  ? 93   ALA B CA  1 
ATOM   1437 C C   . ALA B 1 93  ? 13.769 -14.397 -40.356 1.00 56.41  ? 93   ALA B C   1 
ATOM   1438 O O   . ALA B 1 93  ? 13.442 -13.609 -41.244 1.00 60.44  ? 93   ALA B O   1 
ATOM   1439 C CB  . ALA B 1 93  ? 12.022 -15.418 -38.876 1.00 41.01  ? 93   ALA B CB  1 
ATOM   1440 N N   . GLY B 1 94  ? 14.719 -15.313 -40.519 1.00 43.64  ? 94   GLY B N   1 
ATOM   1441 C CA  . GLY B 1 94  ? 15.355 -15.518 -41.807 1.00 47.11  ? 94   GLY B CA  1 
ATOM   1442 C C   . GLY B 1 94  ? 16.738 -14.909 -41.893 1.00 46.54  ? 94   GLY B C   1 
ATOM   1443 O O   . GLY B 1 94  ? 17.281 -14.439 -40.894 1.00 43.30  ? 94   GLY B O   1 
ATOM   1444 N N   . ALA B 1 95  ? 17.307 -14.910 -43.094 1.00 49.97  ? 95   ALA B N   1 
ATOM   1445 C CA  . ALA B 1 95  ? 18.674 -14.450 -43.299 1.00 50.09  ? 95   ALA B CA  1 
ATOM   1446 C C   . ALA B 1 95  ? 18.760 -13.027 -43.848 1.00 51.03  ? 95   ALA B C   1 
ATOM   1447 O O   . ALA B 1 95  ? 19.854 -12.526 -44.104 1.00 59.01  ? 95   ALA B O   1 
ATOM   1448 C CB  . ALA B 1 95  ? 19.416 -15.408 -44.225 1.00 56.19  ? 95   ALA B CB  1 
ATOM   1449 N N   . GLY B 1 96  ? 17.619 -12.383 -44.054 1.00 51.90  ? 96   GLY B N   1 
ATOM   1450 C CA  . GLY B 1 96  ? 17.617 -11.039 -44.604 1.00 69.69  ? 96   GLY B CA  1 
ATOM   1451 C C   . GLY B 1 96  ? 18.189 -10.037 -43.619 1.00 74.44  ? 96   GLY B C   1 
ATOM   1452 O O   . GLY B 1 96  ? 18.185 -10.281 -42.411 1.00 70.05  ? 96   GLY B O   1 
ATOM   1453 N N   . ALA B 1 97  ? 18.709 -8.921  -44.124 1.00 73.66  ? 97   ALA B N   1 
ATOM   1454 C CA  . ALA B 1 97  ? 19.092 -7.819  -43.250 1.00 67.51  ? 97   ALA B CA  1 
ATOM   1455 C C   . ALA B 1 97  ? 17.838 -7.351  -42.522 1.00 67.93  ? 97   ALA B C   1 
ATOM   1456 O O   . ALA B 1 97  ? 16.740 -7.377  -43.084 1.00 76.08  ? 97   ALA B O   1 
ATOM   1457 C CB  . ALA B 1 97  ? 19.694 -6.686  -44.052 1.00 68.00  ? 97   ALA B CB  1 
ATOM   1458 N N   . GLY B 1 98  ? 17.990 -6.934  -41.272 1.00 60.16  ? 98   GLY B N   1 
ATOM   1459 C CA  . GLY B 1 98  ? 16.837 -6.566  -40.471 1.00 63.32  ? 98   GLY B CA  1 
ATOM   1460 C C   . GLY B 1 98  ? 16.911 -5.181  -39.854 1.00 58.27  ? 98   GLY B C   1 
ATOM   1461 O O   . GLY B 1 98  ? 17.994 -4.629  -39.647 1.00 55.55  ? 98   GLY B O   1 
ATOM   1462 N N   . SER B 1 99  ? 15.743 -4.624  -39.552 1.00 50.85  ? 99   SER B N   1 
ATOM   1463 C CA  . SER B 1 99  ? 15.652 -3.291  -38.978 1.00 46.94  ? 99   SER B CA  1 
ATOM   1464 C C   . SER B 1 99  ? 15.296 -3.402  -37.511 1.00 42.37  ? 99   SER B C   1 
ATOM   1465 O O   . SER B 1 99  ? 15.911 -2.757  -36.658 1.00 46.23  ? 99   SER B O   1 
ATOM   1466 C CB  . SER B 1 99  ? 14.587 -2.465  -39.710 1.00 45.48  ? 99   SER B CB  1 
ATOM   1467 O OG  . SER B 1 99  ? 14.985 -2.179  -41.036 1.00 64.69  ? 99   SER B OG  1 
ATOM   1468 N N   . ARG B 1 100 ? 14.310 -4.240  -37.213 1.00 40.52  ? 100  ARG B N   1 
ATOM   1469 C CA  . ARG B 1 100 ? 13.845 -4.391  -35.837 1.00 37.39  ? 100  ARG B CA  1 
ATOM   1470 C C   . ARG B 1 100 ? 14.724 -5.347  -35.021 1.00 36.64  ? 100  ARG B C   1 
ATOM   1471 O O   . ARG B 1 100 ? 14.948 -6.500  -35.402 1.00 32.60  ? 100  ARG B O   1 
ATOM   1472 C CB  . ARG B 1 100 ? 12.381 -4.829  -35.835 1.00 45.24  ? 100  ARG B CB  1 
ATOM   1473 C CG  . ARG B 1 100 ? 11.468 -3.876  -36.607 1.00 49.06  ? 100  ARG B CG  1 
ATOM   1474 C CD  . ARG B 1 100 ? 10.032 -4.398  -36.695 1.00 62.63  ? 100  ARG B CD  1 
ATOM   1475 N NE  . ARG B 1 100 ? 9.520  -4.835  -35.393 1.00 70.72  ? 100  ARG B NE  1 
ATOM   1476 C CZ  . ARG B 1 100 ? 9.153  -6.083  -35.109 1.00 71.82  ? 100  ARG B CZ  1 
ATOM   1477 N NH1 . ARG B 1 100 ? 9.226  -7.033  -36.036 1.00 73.37  ? 100  ARG B NH1 1 
ATOM   1478 N NH2 . ARG B 1 100 ? 8.705  -6.383  -33.897 1.00 71.28  ? 100  ARG B NH2 1 
ATOM   1479 N N   . LEU B 1 101 ? 15.226 -4.861  -33.893 1.00 34.87  ? 101  LEU B N   1 
ATOM   1480 C CA  . LEU B 1 101 ? 16.175 -5.630  -33.108 1.00 33.29  ? 101  LEU B CA  1 
ATOM   1481 C C   . LEU B 1 101 ? 15.743 -5.762  -31.672 1.00 32.53  ? 101  LEU B C   1 
ATOM   1482 O O   . LEU B 1 101 ? 15.061 -4.893  -31.128 1.00 37.38  ? 101  LEU B O   1 
ATOM   1483 C CB  . LEU B 1 101 ? 17.533 -4.929  -33.085 1.00 34.79  ? 101  LEU B CB  1 
ATOM   1484 C CG  . LEU B 1 101 ? 18.195 -4.571  -34.403 1.00 36.51  ? 101  LEU B CG  1 
ATOM   1485 C CD1 . LEU B 1 101 ? 19.398 -3.684  -34.101 1.00 32.71  ? 101  LEU B CD1 1 
ATOM   1486 C CD2 . LEU B 1 101 ? 18.601 -5.836  -35.146 1.00 32.85  ? 101  LEU B CD2 1 
ATOM   1487 N N   . ALA B 1 102 ? 16.169 -6.842  -31.037 1.00 23.68  ? 102  ALA B N   1 
ATOM   1488 C CA  . ALA B 1 102 ? 16.256 -6.815  -29.585 1.00 22.39  ? 102  ALA B CA  1 
ATOM   1489 C C   . ALA B 1 102 ? 17.736 -6.652  -29.264 1.00 28.66  ? 102  ALA B C   1 
ATOM   1490 O O   . ALA B 1 102 ? 18.580 -7.259  -29.926 1.00 30.03  ? 102  ALA B O   1 
ATOM   1491 C CB  . ALA B 1 102 ? 15.725 -8.064  -28.986 1.00 23.12  ? 102  ALA B CB  1 
ATOM   1492 N N   . SER B 1 103 ? 18.062 -5.813  -28.283 1.00 25.76  ? 103  SER B N   1 
ATOM   1493 C CA  . SER B 1 103 ? 19.466 -5.585  -27.985 1.00 20.60  ? 103  SER B CA  1 
ATOM   1494 C C   . SER B 1 103 ? 19.764 -5.296  -26.518 1.00 24.72  ? 103  SER B C   1 
ATOM   1495 O O   . SER B 1 103 ? 18.859 -5.092  -25.688 1.00 18.60  ? 103  SER B O   1 
ATOM   1496 C CB  . SER B 1 103 ? 20.064 -4.501  -28.898 1.00 27.23  ? 103  SER B CB  1 
ATOM   1497 O OG  . SER B 1 103 ? 19.465 -3.244  -28.678 1.00 31.28  ? 103  SER B OG  1 
ATOM   1498 N N   . GLY B 1 104 ? 21.055 -5.300  -26.209 1.00 23.34  ? 104  GLY B N   1 
ATOM   1499 C CA  . GLY B 1 104 ? 21.481 -5.054  -24.846 1.00 17.36  ? 104  GLY B CA  1 
ATOM   1500 C C   . GLY B 1 104 ? 22.983 -4.902  -24.787 1.00 20.14  ? 104  GLY B C   1 
ATOM   1501 O O   . GLY B 1 104 ? 23.729 -5.562  -25.522 1.00 21.94  ? 104  GLY B O   1 
ATOM   1502 N N   . VAL B 1 105 ? 23.441 -4.007  -23.924 1.00 15.92  ? 105  VAL B N   1 
ATOM   1503 C CA  . VAL B 1 105 ? 24.882 -3.837  -23.739 1.00 16.41  ? 105  VAL B CA  1 
ATOM   1504 C C   . VAL B 1 105 ? 25.443 -4.994  -22.905 1.00 22.27  ? 105  VAL B C   1 
ATOM   1505 O O   . VAL B 1 105 ? 24.831 -5.415  -21.906 1.00 17.54  ? 105  VAL B O   1 
ATOM   1506 C CB  . VAL B 1 105 ? 25.194 -2.464  -23.099 1.00 17.94  ? 105  VAL B CB  1 
ATOM   1507 C CG1 . VAL B 1 105 ? 26.692 -2.273  -22.964 1.00 19.43  ? 105  VAL B CG1 1 
ATOM   1508 C CG2 . VAL B 1 105 ? 24.604 -1.346  -23.968 1.00 18.29  ? 105  VAL B CG2 1 
ATOM   1509 N N   . ILE B 1 106 ? 26.579 -5.529  -23.350 1.00 23.89  ? 106  ILE B N   1 
ATOM   1510 C CA  . ILE B 1 106 ? 27.260 -6.620  -22.664 1.00 20.68  ? 106  ILE B CA  1 
ATOM   1511 C C   . ILE B 1 106 ? 27.972 -6.061  -21.429 1.00 20.51  ? 106  ILE B C   1 
ATOM   1512 O O   . ILE B 1 106 ? 28.943 -5.314  -21.549 1.00 24.63  ? 106  ILE B O   1 
ATOM   1513 C CB  . ILE B 1 106 ? 28.271 -7.304  -23.619 1.00 22.99  ? 106  ILE B CB  1 
ATOM   1514 C CG1 . ILE B 1 106 ? 27.529 -7.992  -24.767 1.00 18.45  ? 106  ILE B CG1 1 
ATOM   1515 C CG2 . ILE B 1 106 ? 29.146 -8.312  -22.879 1.00 27.29  ? 106  ILE B CG2 1 
ATOM   1516 C CD1 . ILE B 1 106 ? 28.400 -8.333  -25.978 1.00 19.78  ? 106  ILE B CD1 1 
ATOM   1517 N N   . GLY B 1 107 ? 27.460 -6.392  -20.240 1.00 18.44  ? 107  GLY B N   1 
ATOM   1518 C CA  . GLY B 1 107 ? 28.023 -5.866  -19.009 1.00 18.11  ? 107  GLY B CA  1 
ATOM   1519 C C   . GLY B 1 107 ? 28.858 -6.870  -18.239 1.00 23.96  ? 107  GLY B C   1 
ATOM   1520 O O   . GLY B 1 107 ? 28.595 -8.065  -18.298 1.00 22.10  ? 107  GLY B O   1 
ATOM   1521 N N   . ILE B 1 108 ? 29.864 -6.383  -17.514 1.00 21.95  ? 108  ILE B N   1 
ATOM   1522 C CA  . ILE B 1 108 ? 30.692 -7.251  -16.678 1.00 20.49  ? 108  ILE B CA  1 
ATOM   1523 C C   . ILE B 1 108 ? 29.856 -7.899  -15.589 1.00 30.35  ? 108  ILE B C   1 
ATOM   1524 O O   . ILE B 1 108 ? 29.005 -7.245  -14.979 1.00 21.47  ? 108  ILE B O   1 
ATOM   1525 C CB  . ILE B 1 108 ? 31.810 -6.454  -15.989 1.00 21.65  ? 108  ILE B CB  1 
ATOM   1526 C CG1 . ILE B 1 108 ? 32.547 -5.608  -17.026 1.00 29.11  ? 108  ILE B CG1 1 
ATOM   1527 C CG2 . ILE B 1 108 ? 32.760 -7.401  -15.255 1.00 30.12  ? 108  ILE B CG2 1 
ATOM   1528 C CD1 . ILE B 1 108 ? 33.587 -4.656  -16.454 1.00 38.92  ? 108  ILE B CD1 1 
ATOM   1529 N N   . ALA B 1 109 ? 30.088 -9.183  -15.336 1.00 25.88  ? 109  ALA B N   1 
ATOM   1530 C CA  . ALA B 1 109 ? 29.442 -9.833  -14.206 1.00 22.10  ? 109  ALA B CA  1 
ATOM   1531 C C   . ALA B 1 109 ? 30.504 -10.218 -13.181 1.00 33.12  ? 109  ALA B C   1 
ATOM   1532 O O   . ALA B 1 109 ? 31.631 -10.579 -13.542 1.00 28.02  ? 109  ALA B O   1 
ATOM   1533 C CB  . ALA B 1 109 ? 28.683 -11.062 -14.653 1.00 21.02  ? 109  ALA B CB  1 
ATOM   1534 N N   . GLN B 1 110 ? 30.123 -10.098 -11.911 1.00 36.99  ? 110  GLN B N   1 
ATOM   1535 C CA  . GLN B 1 110 ? 30.849 -10.610 -10.746 1.00 58.09  ? 110  GLN B CA  1 
ATOM   1536 C C   . GLN B 1 110 ? 31.643 -11.902 -10.993 1.00 67.63  ? 110  GLN B C   1 
ATOM   1537 O O   . GLN B 1 110 ? 31.123 -13.019 -10.909 1.00 69.21  ? 110  GLN B O   1 
ATOM   1538 C CB  . GLN B 1 110 ? 29.860 -10.813 -9.581  1.00 63.08  ? 110  GLN B CB  1 
ATOM   1539 C CG  . GLN B 1 110 ? 28.542 -11.557 -9.942  1.00 40.32  ? 110  GLN B CG  1 
ATOM   1540 C CD  . GLN B 1 110 ? 27.556 -10.724 -10.795 1.00 49.47  ? 110  GLN B CD  1 
ATOM   1541 O OE1 . GLN B 1 110 ? 27.581 -9.489  -10.791 1.00 40.70  ? 110  GLN B OE1 1 
ATOM   1542 N NE2 . GLN B 1 110 ? 26.695 -11.414 -11.535 1.00 55.80  ? 110  GLN B NE2 1 
ATOM   1543 O OXT . GLN B 1 110 ? 32.842 -11.856 -11.276 1.00 70.89  ? 110  GLN B OXT 1 
HETATM 1544 O O   . HOH C 2 .   ? 14.650 -18.230 -17.236 1.00 46.53  ? 2001 HOH A O   1 
HETATM 1545 O O   . HOH C 2 .   ? 9.574  -15.400 -12.472 1.00 42.72  ? 2002 HOH A O   1 
HETATM 1546 O O   . HOH C 2 .   ? 14.587 -20.382 -14.670 1.00 37.36  ? 2003 HOH A O   1 
HETATM 1547 O O   . HOH C 2 .   ? 13.097 -19.240 -11.948 1.00 16.16  ? 2004 HOH A O   1 
HETATM 1548 O O   . HOH C 2 .   ? 10.195 -16.442 -10.250 1.00 28.42  ? 2005 HOH A O   1 
HETATM 1549 O O   . HOH C 2 .   ? 17.840 -8.903  -15.413 1.00 37.75  ? 2006 HOH A O   1 
HETATM 1550 O O   . HOH C 2 .   ? 20.166 -9.471  -14.875 1.00 33.96  ? 2007 HOH A O   1 
HETATM 1551 O O   . HOH C 2 .   ? 14.446 -11.283 -15.556 1.00 40.92  ? 2008 HOH A O   1 
HETATM 1552 O O   . HOH C 2 .   ? 7.978  -14.867 -6.261  1.00 35.68  ? 2009 HOH A O   1 
HETATM 1553 O O   . HOH C 2 .   ? 6.471  -5.888  -7.856  1.00 50.88  ? 2010 HOH A O   1 
HETATM 1554 O O   . HOH C 2 .   ? 10.314 -6.889  -8.166  1.00 37.09  ? 2011 HOH A O   1 
HETATM 1555 O O   . HOH C 2 .   ? 18.636 -16.858 -18.215 1.00 36.26  ? 2012 HOH A O   1 
HETATM 1556 O O   . HOH C 2 .   ? 22.180 -11.695 -14.840 1.00 24.14  ? 2013 HOH A O   1 
HETATM 1557 O O   . HOH C 2 .   ? 10.723 -5.026  -0.980  1.00 37.35  ? 2014 HOH A O   1 
HETATM 1558 O O   . HOH C 2 .   ? 27.220 -34.292 -16.531 1.00 48.93  ? 2015 HOH A O   1 
HETATM 1559 O O   . HOH C 2 .   ? 15.194 -3.843  -9.250  1.00 46.90  ? 2016 HOH A O   1 
HETATM 1560 O O   . HOH C 2 .   ? 17.312 -8.586  -12.794 1.00 47.73  ? 2017 HOH A O   1 
HETATM 1561 O O   . HOH C 2 .   ? 14.722 -10.846 -12.512 1.00 29.86  ? 2018 HOH A O   1 
HETATM 1562 O O   . HOH C 2 .   ? 12.719 -4.830  5.807   1.00 41.39  ? 2019 HOH A O   1 
HETATM 1563 O O   . HOH C 2 .   ? 16.529 -2.644  7.058   1.00 48.18  ? 2020 HOH A O   1 
HETATM 1564 O O   . HOH C 2 .   ? 20.870 -16.248 -16.768 1.00 18.28  ? 2021 HOH A O   1 
HETATM 1565 O O   . HOH C 2 .   ? 22.494 -14.087 -15.963 1.00 16.51  ? 2022 HOH A O   1 
HETATM 1566 O O   . HOH C 2 .   ? 27.481 -13.659 -2.155  1.00 38.73  ? 2023 HOH A O   1 
HETATM 1567 O O   . HOH C 2 .   ? 31.568 -29.586 -11.175 1.00 39.74  ? 2024 HOH A O   1 
HETATM 1568 O O   . HOH C 2 .   ? 29.801 -8.573  -3.146  1.00 53.36  ? 2025 HOH A O   1 
HETATM 1569 O O   . HOH C 2 .   ? 29.098 -6.089  -1.607  1.00 46.60  ? 2026 HOH A O   1 
HETATM 1570 O O   . HOH C 2 .   ? 29.200 -35.943 -15.183 1.00 48.89  ? 2027 HOH A O   1 
HETATM 1571 O O   . HOH C 2 .   ? 28.542 -38.814 -14.591 1.00 38.60  ? 2028 HOH A O   1 
HETATM 1572 O O   . HOH C 2 .   ? 21.145 -1.999  -11.410 1.00 34.01  ? 2029 HOH A O   1 
HETATM 1573 O O   . HOH C 2 .   ? 18.232 -1.757  -6.211  1.00 22.57  ? 2030 HOH A O   1 
HETATM 1574 O O   . HOH C 2 .   ? 13.363 -4.064  -0.522  1.00 39.11  ? 2031 HOH A O   1 
HETATM 1575 O O   . HOH C 2 .   ? 15.132 -6.008  0.798   1.00 23.22  ? 2032 HOH A O   1 
HETATM 1576 O O   . HOH C 2 .   ? 15.642 -4.893  5.834   1.00 27.63  ? 2033 HOH A O   1 
HETATM 1577 O O   . HOH C 2 .   ? 18.311 0.048   3.244   1.00 35.45  ? 2034 HOH A O   1 
HETATM 1578 O O   . HOH C 2 .   ? 18.902 -2.029  5.868   1.00 50.27  ? 2035 HOH A O   1 
HETATM 1579 O O   . HOH C 2 .   ? 23.045 -6.346  7.671   1.00 29.74  ? 2036 HOH A O   1 
HETATM 1580 O O   . HOH C 2 .   ? 18.391 -11.798 6.003   1.00 25.20  ? 2037 HOH A O   1 
HETATM 1581 O O   . HOH C 2 .   ? 18.084 -20.697 -19.697 1.00 38.31  ? 2038 HOH A O   1 
HETATM 1582 O O   . HOH C 2 .   ? 21.329 -18.745 4.379   1.00 29.61  ? 2039 HOH A O   1 
HETATM 1583 O O   . HOH C 2 .   ? 18.580 -24.475 3.593   1.00 49.99  ? 2040 HOH A O   1 
HETATM 1584 O O   . HOH C 2 .   ? 12.030 -26.129 -2.630  1.00 31.63  ? 2041 HOH A O   1 
HETATM 1585 O O   . HOH C 2 .   ? 15.194 -31.360 1.483   1.00 60.33  ? 2042 HOH A O   1 
HETATM 1586 O O   . HOH C 2 .   ? 21.039 -30.212 -1.834  1.00 52.99  ? 2043 HOH A O   1 
HETATM 1587 O O   . HOH C 2 .   ? 25.537 -25.344 0.237   1.00 48.30  ? 2044 HOH A O   1 
HETATM 1588 O O   . HOH C 2 .   ? 21.182 -20.952 7.998   1.00 55.04  ? 2045 HOH A O   1 
HETATM 1589 O O   . HOH C 2 .   ? 26.709 -16.220 -0.006  1.00 42.22  ? 2046 HOH A O   1 
HETATM 1590 O O   . HOH C 2 .   ? 21.823 -17.227 6.668   1.00 44.95  ? 2047 HOH A O   1 
HETATM 1591 O O   . HOH C 2 .   ? 27.365 -15.815 3.974   1.00 44.85  ? 2048 HOH A O   1 
HETATM 1592 O O   . HOH C 2 .   ? 28.245 -11.901 1.451   1.00 45.94  ? 2049 HOH A O   1 
HETATM 1593 O O   . HOH C 2 .   ? 20.817 -15.026 7.577   1.00 45.19  ? 2050 HOH A O   1 
HETATM 1594 O O   . HOH C 2 .   ? 26.810 -10.864 -1.806  1.00 28.84  ? 2051 HOH A O   1 
HETATM 1595 O O   . HOH C 2 .   ? 27.471 -7.375  -3.246  1.00 33.67  ? 2052 HOH A O   1 
HETATM 1596 O O   . HOH C 2 .   ? 29.292 -1.445  -4.396  1.00 49.37  ? 2053 HOH A O   1 
HETATM 1597 O O   . HOH C 2 .   ? 27.442 0.553   -0.623  1.00 38.16  ? 2054 HOH A O   1 
HETATM 1598 O O   . HOH C 2 .   ? 25.821 -5.984  -10.726 1.00 37.26  ? 2055 HOH A O   1 
HETATM 1599 O O   . HOH C 2 .   ? 29.444 -13.882 -3.571  1.00 44.94  ? 2056 HOH A O   1 
HETATM 1600 O O   . HOH C 2 .   ? 33.779 -16.075 -2.971  1.00 42.56  ? 2057 HOH A O   1 
HETATM 1601 O O   . HOH C 2 .   ? 30.101 -21.966 -0.849  1.00 47.65  ? 2058 HOH A O   1 
HETATM 1602 O O   . HOH C 2 .   ? 22.026 -30.736 -3.983  1.00 55.43  ? 2059 HOH A O   1 
HETATM 1603 O O   . HOH C 2 .   ? 18.326 -32.977 -11.542 1.00 39.24  ? 2060 HOH A O   1 
HETATM 1604 O O   . HOH C 2 .   ? 22.164 -35.020 -5.281  1.00 43.88  ? 2061 HOH A O   1 
HETATM 1605 O O   . HOH C 2 .   ? 15.393 -32.462 -8.812  1.00 47.68  ? 2062 HOH A O   1 
HETATM 1606 O O   . HOH C 2 .   ? 8.281  -21.830 -5.029  1.00 34.63  ? 2063 HOH A O   1 
HETATM 1607 O O   . HOH C 2 .   ? 15.787 -12.374 8.015   1.00 30.34  ? 2064 HOH A O   1 
HETATM 1608 O O   . HOH C 2 .   ? 18.363 -14.660 7.715   1.00 42.37  ? 2065 HOH A O   1 
HETATM 1609 O O   . HOH C 2 .   ? 12.820 -11.614 5.290   1.00 21.42  ? 2066 HOH A O   1 
HETATM 1610 O O   . HOH C 2 .   ? 10.946 -8.314  5.151   1.00 50.74  ? 2067 HOH A O   1 
HETATM 1611 O O   . HOH C 2 .   ? 16.949 -5.963  9.463   1.00 37.87  ? 2068 HOH A O   1 
HETATM 1612 O O   . HOH C 2 .   ? 21.153 -9.617  12.539  1.00 41.64  ? 2069 HOH A O   1 
HETATM 1613 O O   . HOH C 2 .   ? 11.846 -11.923 11.672  1.00 51.13  ? 2070 HOH A O   1 
HETATM 1614 O O   . HOH C 2 .   ? 9.457  -16.552 9.266   1.00 33.27  ? 2071 HOH A O   1 
HETATM 1615 O O   . HOH C 2 .   ? 8.418  -13.140 10.207  1.00 44.92  ? 2072 HOH A O   1 
HETATM 1616 O O   . HOH C 2 .   ? 10.430 -10.571 6.963   1.00 22.67  ? 2073 HOH A O   1 
HETATM 1617 O O   . HOH C 2 .   ? 7.064  -13.041 0.651   1.00 37.51  ? 2074 HOH A O   1 
HETATM 1618 O O   . HOH C 2 .   ? 6.784  -15.778 1.046   1.00 31.48  ? 2075 HOH A O   1 
HETATM 1619 O O   . HOH C 2 .   ? 5.701  -12.400 9.598   1.00 41.01  ? 2076 HOH A O   1 
HETATM 1620 O O   . HOH C 2 .   ? 4.640  -7.670  4.187   1.00 51.78  ? 2077 HOH A O   1 
HETATM 1621 O O   . HOH C 2 .   ? 9.045  -18.802 -6.004  1.00 36.98  ? 2078 HOH A O   1 
HETATM 1622 O O   . HOH C 2 .   ? 8.637  -16.317 -8.253  1.00 47.64  ? 2079 HOH A O   1 
HETATM 1623 O O   . HOH C 2 .   ? 7.817  -17.173 -1.228  1.00 31.95  ? 2080 HOH A O   1 
HETATM 1624 O O   . HOH C 2 .   ? 10.007 -19.139 -10.418 1.00 28.14  ? 2081 HOH A O   1 
HETATM 1625 O O   . HOH C 2 .   ? 13.152 -24.118 -17.110 1.00 26.05  ? 2082 HOH A O   1 
HETATM 1626 O O   . HOH C 2 .   ? 14.670 -25.873 -20.003 1.00 48.93  ? 2083 HOH A O   1 
HETATM 1627 O O   . HOH C 2 .   ? 15.202 -22.156 -16.868 1.00 46.78  ? 2084 HOH A O   1 
HETATM 1628 O O   . HOH C 2 .   ? 18.363 -22.108 -21.940 1.00 37.64  ? 2085 HOH A O   1 
HETATM 1629 O O   . HOH C 2 .   ? 20.824 -22.543 -22.825 1.00 36.49  ? 2086 HOH A O   1 
HETATM 1630 O O   . HOH D 2 .   ? 38.871 -13.150 -20.523 1.00 42.91  ? 2001 HOH B O   1 
HETATM 1631 O O   . HOH D 2 .   ? 33.811 -11.459 -14.413 1.00 35.56  ? 2002 HOH B O   1 
HETATM 1632 O O   . HOH D 2 .   ? 24.142 -6.702  -18.370 1.00 40.66  ? 2003 HOH B O   1 
HETATM 1633 O O   . HOH D 2 .   ? 22.636 -5.699  -20.460 1.00 16.31  ? 2004 HOH B O   1 
HETATM 1634 O O   . HOH D 2 .   ? 19.033 -3.914  -22.394 1.00 27.60  ? 2005 HOH B O   1 
HETATM 1635 O O   . HOH D 2 .   ? 14.264 -13.337 -17.049 1.00 46.61  ? 2006 HOH B O   1 
HETATM 1636 O O   . HOH D 2 .   ? 15.468 -9.586  -17.398 1.00 41.46  ? 2007 HOH B O   1 
HETATM 1637 O O   . HOH D 2 .   ? 12.014 -14.565 -16.868 1.00 38.75  ? 2008 HOH B O   1 
HETATM 1638 O O   . HOH D 2 .   ? 15.779 -15.793 -17.643 1.00 40.40  ? 2009 HOH B O   1 
HETATM 1639 O O   . HOH D 2 .   ? 7.708  -3.935  -24.735 1.00 52.18  ? 2010 HOH B O   1 
HETATM 1640 O O   . HOH D 2 .   ? 9.821  -7.374  -24.342 1.00 40.85  ? 2011 HOH B O   1 
HETATM 1641 O O   . HOH D 2 .   ? 14.251 -13.309 -19.964 1.00 53.10  ? 2012 HOH B O   1 
HETATM 1642 O O   . HOH D 2 .   ? 15.293 -10.122 -20.207 1.00 33.49  ? 2013 HOH B O   1 
HETATM 1643 O O   . HOH D 2 .   ? 12.120 -15.655 -19.243 1.00 46.76  ? 2014 HOH B O   1 
HETATM 1644 O O   . HOH D 2 .   ? 15.727 -15.361 -20.784 1.00 37.44  ? 2015 HOH B O   1 
HETATM 1645 O O   . HOH D 2 .   ? 20.110 -23.395 -32.656 1.00 59.48  ? 2016 HOH B O   1 
HETATM 1646 O O   . HOH D 2 .   ? 38.142 -19.820 -22.733 1.00 36.90  ? 2017 HOH B O   1 
HETATM 1647 O O   . HOH D 2 .   ? 41.922 -11.845 -24.971 1.00 52.53  ? 2018 HOH B O   1 
HETATM 1648 O O   . HOH D 2 .   ? 38.866 -15.844 -28.105 1.00 44.09  ? 2019 HOH B O   1 
HETATM 1649 O O   . HOH D 2 .   ? 17.606 -18.414 -19.406 1.00 48.63  ? 2020 HOH B O   1 
HETATM 1650 O O   . HOH D 2 .   ? 7.924  -16.607 -26.458 1.00 25.99  ? 2021 HOH B O   1 
HETATM 1651 O O   . HOH D 2 .   ? 8.330  -10.866 -31.940 1.00 43.97  ? 2022 HOH B O   1 
HETATM 1652 O O   . HOH D 2 .   ? 12.564 -5.489  -42.460 1.00 62.70  ? 2023 HOH B O   1 
HETATM 1653 O O   . HOH D 2 .   ? 10.583 -12.012 -33.458 1.00 28.34  ? 2024 HOH B O   1 
HETATM 1654 O O   . HOH D 2 .   ? 9.625  -12.736 -38.287 1.00 35.86  ? 2025 HOH B O   1 
HETATM 1655 O O   . HOH D 2 .   ? 5.492  -16.988 -35.719 1.00 45.37  ? 2026 HOH B O   1 
HETATM 1656 O O   . HOH D 2 .   ? 13.433 -19.139 -40.469 1.00 40.27  ? 2027 HOH B O   1 
HETATM 1657 O O   . HOH D 2 .   ? 16.981 -12.984 -38.834 1.00 32.96  ? 2028 HOH B O   1 
HETATM 1658 O O   . HOH D 2 .   ? 28.739 -2.485  -29.885 1.00 29.18  ? 2029 HOH B O   1 
HETATM 1659 O O   . HOH D 2 .   ? 23.407 -14.159 -39.263 1.00 69.22  ? 2030 HOH B O   1 
HETATM 1660 O O   . HOH D 2 .   ? 19.940 -22.019 -34.770 1.00 35.52  ? 2031 HOH B O   1 
HETATM 1661 O O   . HOH D 2 .   ? 19.328 -21.444 -31.026 1.00 31.09  ? 2032 HOH B O   1 
HETATM 1662 O O   . HOH D 2 .   ? 16.464 -23.212 -29.796 1.00 46.01  ? 2033 HOH B O   1 
HETATM 1663 O O   . HOH D 2 .   ? 14.628 -23.814 -28.172 1.00 37.58  ? 2034 HOH B O   1 
HETATM 1664 O O   . HOH D 2 .   ? 19.812 -24.691 -29.167 1.00 50.44  ? 2035 HOH B O   1 
HETATM 1665 O O   . HOH D 2 .   ? 14.445 -22.129 -22.154 1.00 42.48  ? 2036 HOH B O   1 
HETATM 1666 O O   . HOH D 2 .   ? 22.668 -22.755 -29.366 1.00 36.54  ? 2037 HOH B O   1 
HETATM 1667 O O   . HOH D 2 .   ? 26.605 -26.184 -29.614 1.00 53.69  ? 2038 HOH B O   1 
HETATM 1668 O O   . HOH D 2 .   ? 27.906 -22.817 -24.087 1.00 46.18  ? 2039 HOH B O   1 
HETATM 1669 O O   . HOH D 2 .   ? 29.119 -23.681 -30.912 1.00 34.70  ? 2040 HOH B O   1 
HETATM 1670 O O   . HOH D 2 .   ? 41.005 -9.488  -27.051 1.00 42.21  ? 2041 HOH B O   1 
HETATM 1671 O O   . HOH D 2 .   ? 35.134 -5.595  -29.325 1.00 47.50  ? 2042 HOH B O   1 
HETATM 1672 O O   . HOH D 2 .   ? 36.141 -3.064  -23.238 1.00 58.97  ? 2043 HOH B O   1 
HETATM 1673 O O   . HOH D 2 .   ? 23.229 -0.293  -27.184 1.00 53.01  ? 2044 HOH B O   1 
HETATM 1674 O O   . HOH D 2 .   ? 16.774 -10.481 -40.583 1.00 54.19  ? 2045 HOH B O   1 
HETATM 1675 O O   . HOH D 2 .   ? 20.262 -12.092 -40.366 1.00 49.55  ? 2046 HOH B O   1 
HETATM 1676 O O   . HOH D 2 .   ? 14.824 -7.749  -37.872 1.00 27.12  ? 2047 HOH B O   1 
HETATM 1677 O O   . HOH D 2 .   ? 15.046 -7.108  -44.629 1.00 47.74  ? 2048 HOH B O   1 
HETATM 1678 O O   . HOH D 2 .   ? 10.549 -13.096 -42.382 1.00 42.69  ? 2049 HOH B O   1 
HETATM 1679 O O   . HOH D 2 .   ? 15.095 -16.169 -45.101 1.00 44.20  ? 2050 HOH B O   1 
HETATM 1680 O O   . HOH D 2 .   ? 16.059 -4.018  -43.236 1.00 43.65  ? 2051 HOH B O   1 
HETATM 1681 O O   . HOH D 2 .   ? 18.438 -3.167  -41.801 1.00 47.06  ? 2052 HOH B O   1 
HETATM 1682 O O   . HOH D 2 .   ? 13.191 -6.012  -39.586 1.00 31.67  ? 2053 HOH B O   1 
HETATM 1683 O O   . HOH D 2 .   ? 16.476 -2.724  -29.837 1.00 35.66  ? 2054 HOH B O   1 
HETATM 1684 O O   . HOH D 2 .   ? 18.986 -1.541  -30.906 1.00 48.45  ? 2055 HOH B O   1 
HETATM 1685 O O   . HOH D 2 .   ? 20.942 -1.844  -26.480 1.00 37.52  ? 2056 HOH B O   1 
HETATM 1686 O O   . HOH D 2 .   ? 21.496 -2.791  -22.186 1.00 24.56  ? 2057 HOH B O   1 
HETATM 1687 O O   . HOH D 2 .   ? 26.096 -6.411  -15.413 1.00 53.49  ? 2058 HOH B O   1 
HETATM 1688 O O   . HOH D 2 .   ? 27.451 -3.997  -15.610 1.00 18.79  ? 2059 HOH B O   1 
HETATM 1689 O O   . HOH D 2 .   ? 28.862 -5.421  -12.800 1.00 49.06  ? 2060 HOH B O   1 
HETATM 1690 O O   . HOH D 2 .   ? 25.200 -10.517 -13.174 1.00 38.56  ? 2061 HOH B O   1 
# 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   ALA 1   1   1   ALA ALA A . n 
A 1 2   THR 2   2   2   THR THR A . n 
A 1 3   LYS 3   3   3   LYS LYS A . n 
A 1 4   ALA 4   4   4   ALA ALA A . n 
A 1 5   VAL 5   5   5   VAL VAL A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   VAL 7   7   7   VAL VAL A . n 
A 1 8   LEU 8   8   8   LEU LEU A . n 
A 1 9   LYS 9   9   9   LYS LYS A . n 
A 1 10  GLY 10  10  10  GLY GLY A . n 
A 1 11  ASP 11  11  11  ASP ASP A . n 
A 1 12  GLY 12  12  12  GLY GLY A . n 
A 1 13  PRO 13  13  13  PRO PRO A . n 
A 1 14  VAL 14  14  14  VAL VAL A . n 
A 1 15  GLN 15  15  15  GLN GLN A . n 
A 1 16  GLY 16  16  16  GLY GLY A . n 
A 1 17  ILE 17  17  17  ILE ILE A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  ASN 19  19  19  ASN ASN A . n 
A 1 20  PHE 20  20  20  PHE PHE A . n 
A 1 21  GLU 21  21  21  GLU GLU A . n 
A 1 22  GLN 22  22  22  GLN GLN A . n 
A 1 23  LYS 23  23  23  LYS LYS A . n 
A 1 24  GLU 24  24  24  GLU GLU A . n 
A 1 25  SER 25  25  25  SER SER A . n 
A 1 26  ASN 26  26  26  ASN ASN A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PRO 28  28  28  PRO PRO A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  LYS 30  30  30  LYS LYS A . n 
A 1 31  VAL 31  31  31  VAL VAL A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  GLY 33  33  33  GLY GLY A . n 
A 1 34  SER 34  34  34  SER SER A . n 
A 1 35  ILE 35  35  35  ILE ILE A . n 
A 1 36  LYS 36  36  36  LYS LYS A . n 
A 1 37  GLY 37  37  37  GLY GLY A . n 
A 1 38  LEU 38  38  38  LEU LEU A . n 
A 1 39  THR 39  39  39  THR THR A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  LEU 42  42  42  LEU LEU A . n 
A 1 43  HIS 43  43  43  HIS HIS A . n 
A 1 44  GLY 44  44  44  GLY GLY A . n 
A 1 45  PHE 45  45  45  PHE PHE A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  VAL 47  47  47  VAL VAL A . n 
A 1 48  HIS 48  48  48  HIS HIS A . n 
A 1 49  GLY 49  49  49  GLY GLY A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  GLY 52  52  52  GLY GLY A . n 
A 1 53  ASP 53  53  53  ASP ASP A . n 
A 1 54  LEU 54  54  54  LEU LEU A . n 
A 1 55  GLY 55  55  55  GLY GLY A . n 
A 1 56  ASN 56  56  56  ASN ASN A . n 
A 1 57  VAL 57  57  57  VAL VAL A . n 
A 1 58  THR 58  58  58  THR THR A . n 
A 1 59  ALA 59  59  59  ALA ALA A . n 
A 1 60  ASP 60  60  60  ASP ASP A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  ASP 62  62  62  ASP ASP A . n 
A 1 63  GLY 63  63  63  GLY GLY A . n 
A 1 64  VAL 64  64  64  VAL VAL A . n 
A 1 65  ALA 65  65  65  ALA ALA A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  VAL 67  67  67  VAL VAL A . n 
A 1 68  SER 68  68  68  SER SER A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  GLU 70  70  70  GLU GLU A . n 
A 1 71  ASP 71  71  71  ASP ASP A . n 
A 1 72  SER 72  72  72  SER SER A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  ILE 74  74  74  ILE ILE A . n 
A 1 75  SER 75  75  75  SER SER A . n 
A 1 76  LEU 76  76  76  LEU LEU A . n 
A 1 77  SER 77  77  77  SER SER A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  ASP 79  79  79  ASP ASP A . n 
A 1 80  HIS 80  80  80  HIS HIS A . n 
A 1 81  SER 81  81  81  SER SER A . n 
A 1 82  ILE 82  82  82  ILE ILE A . n 
A 1 83  ILE 83  83  83  ILE ILE A . n 
A 1 84  GLY 84  84  84  GLY GLY A . n 
A 1 85  ARG 85  85  85  ARG ARG A . n 
A 1 86  THR 86  86  86  THR THR A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  VAL 88  88  88  VAL VAL A . n 
A 1 89  VAL 89  89  89  VAL VAL A . n 
A 1 90  HIS 90  90  90  HIS HIS A . n 
A 1 91  GLU 91  91  91  GLU GLU A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  GLY 94  94  94  GLY GLY A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  GLY 96  96  96  GLY GLY A . n 
A 1 97  ALA 97  97  97  ALA ALA A . n 
A 1 98  GLY 98  98  98  GLY GLY A . n 
A 1 99  SER 99  99  99  SER SER A . n 
A 1 100 ARG 100 100 100 ARG ARG A . n 
A 1 101 LEU 101 101 101 LEU LEU A . n 
A 1 102 ALA 102 102 102 ALA ALA A . n 
A 1 103 SER 103 103 103 SER SER A . n 
A 1 104 GLY 104 104 104 GLY GLY A . n 
A 1 105 VAL 105 105 105 VAL VAL A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLY 107 107 107 GLY GLY A . n 
A 1 108 ILE 108 108 108 ILE ILE A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 GLN 110 110 110 GLN GLN A . n 
B 1 1   ALA 1   1   ?   ?   ?   B . n 
B 1 2   THR 2   2   2   THR THR B . n 
B 1 3   LYS 3   3   3   LYS LYS B . n 
B 1 4   ALA 4   4   4   ALA ALA B . n 
B 1 5   VAL 5   5   5   VAL VAL B . n 
B 1 6   ALA 6   6   6   ALA ALA B . n 
B 1 7   VAL 7   7   7   VAL VAL B . n 
B 1 8   LEU 8   8   8   LEU LEU B . n 
B 1 9   LYS 9   9   9   LYS LYS B . n 
B 1 10  GLY 10  10  10  GLY GLY B . n 
B 1 11  ASP 11  11  11  ASP ASP B . n 
B 1 12  GLY 12  12  12  GLY GLY B . n 
B 1 13  PRO 13  13  13  PRO PRO B . n 
B 1 14  VAL 14  14  14  VAL VAL B . n 
B 1 15  GLN 15  15  15  GLN GLN B . n 
B 1 16  GLY 16  16  16  GLY GLY B . n 
B 1 17  ILE 17  17  17  ILE ILE B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  ASN 19  19  19  ASN ASN B . n 
B 1 20  PHE 20  20  20  PHE PHE B . n 
B 1 21  GLU 21  21  21  GLU GLU B . n 
B 1 22  GLN 22  22  22  GLN GLN B . n 
B 1 23  LYS 23  23  23  LYS LYS B . n 
B 1 24  GLU 24  24  24  GLU GLU B . n 
B 1 25  SER 25  25  25  SER SER B . n 
B 1 26  ASN 26  26  26  ASN ASN B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  PRO 28  28  28  PRO PRO B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  LYS 30  30  30  LYS LYS B . n 
B 1 31  VAL 31  31  31  VAL VAL B . n 
B 1 32  TRP 32  32  32  TRP TRP B . n 
B 1 33  GLY 33  33  33  GLY GLY B . n 
B 1 34  SER 34  34  34  SER SER B . n 
B 1 35  ILE 35  35  35  ILE ILE B . n 
B 1 36  LYS 36  36  36  LYS LYS B . n 
B 1 37  GLY 37  37  37  GLY GLY B . n 
B 1 38  LEU 38  38  38  LEU LEU B . n 
B 1 39  THR 39  39  39  THR THR B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  LEU 42  42  42  LEU LEU B . n 
B 1 43  HIS 43  43  43  HIS HIS B . n 
B 1 44  GLY 44  44  44  GLY GLY B . n 
B 1 45  PHE 45  45  45  PHE PHE B . n 
B 1 46  HIS 46  46  46  HIS HIS B . n 
B 1 47  VAL 47  47  47  VAL VAL B . n 
B 1 48  HIS 48  48  48  HIS HIS B . n 
B 1 49  GLY 49  49  49  GLY GLY B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  GLY 52  52  52  GLY GLY B . n 
B 1 53  ASP 53  53  53  ASP ASP B . n 
B 1 54  LEU 54  54  54  LEU LEU B . n 
B 1 55  GLY 55  55  55  GLY GLY B . n 
B 1 56  ASN 56  56  56  ASN ASN B . n 
B 1 57  VAL 57  57  57  VAL VAL B . n 
B 1 58  THR 58  58  58  THR THR B . n 
B 1 59  ALA 59  59  59  ALA ALA B . n 
B 1 60  ASP 60  60  60  ASP ASP B . n 
B 1 61  LYS 61  61  61  LYS LYS B . n 
B 1 62  ASP 62  62  62  ASP ASP B . n 
B 1 63  GLY 63  63  63  GLY GLY B . n 
B 1 64  VAL 64  64  64  VAL VAL B . n 
B 1 65  ALA 65  65  65  ALA ALA B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  VAL 67  67  67  VAL VAL B . n 
B 1 68  SER 68  68  68  SER SER B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  GLU 70  70  70  GLU GLU B . n 
B 1 71  ASP 71  71  71  ASP ASP B . n 
B 1 72  SER 72  72  72  SER SER B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  ILE 74  74  74  ILE ILE B . n 
B 1 75  SER 75  75  75  SER SER B . n 
B 1 76  LEU 76  76  76  LEU LEU B . n 
B 1 77  SER 77  77  77  SER SER B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  ASP 79  79  79  ASP ASP B . n 
B 1 80  HIS 80  80  80  HIS HIS B . n 
B 1 81  SER 81  81  81  SER SER B . n 
B 1 82  ILE 82  82  82  ILE ILE B . n 
B 1 83  ILE 83  83  83  ILE ILE B . n 
B 1 84  GLY 84  84  84  GLY GLY B . n 
B 1 85  ARG 85  85  85  ARG ARG B . n 
B 1 86  THR 86  86  86  THR THR B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  VAL 88  88  88  VAL VAL B . n 
B 1 89  VAL 89  89  89  VAL VAL B . n 
B 1 90  HIS 90  90  90  HIS HIS B . n 
B 1 91  GLU 91  91  91  GLU GLU B . n 
B 1 92  LYS 92  92  92  LYS LYS B . n 
B 1 93  ALA 93  93  93  ALA ALA B . n 
B 1 94  GLY 94  94  94  GLY GLY B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  GLY 96  96  96  GLY GLY B . n 
B 1 97  ALA 97  97  97  ALA ALA B . n 
B 1 98  GLY 98  98  98  GLY GLY B . n 
B 1 99  SER 99  99  99  SER SER B . n 
B 1 100 ARG 100 100 100 ARG ARG B . n 
B 1 101 LEU 101 101 101 LEU LEU B . n 
B 1 102 ALA 102 102 102 ALA ALA B . n 
B 1 103 SER 103 103 103 SER SER B . n 
B 1 104 GLY 104 104 104 GLY GLY B . n 
B 1 105 VAL 105 105 105 VAL VAL B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLY 107 107 107 GLY GLY B . n 
B 1 108 ILE 108 108 108 ILE ILE B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 GLN 110 110 110 GLN GLN B . 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 HOH 1  2001 2001 HOH HOH A . 
C 2 HOH 2  2002 2002 HOH HOH A . 
C 2 HOH 3  2003 2003 HOH HOH A . 
C 2 HOH 4  2004 2004 HOH HOH A . 
C 2 HOH 5  2005 2005 HOH HOH A . 
C 2 HOH 6  2006 2006 HOH HOH A . 
C 2 HOH 7  2007 2007 HOH HOH A . 
C 2 HOH 8  2008 2008 HOH HOH A . 
C 2 HOH 9  2009 2009 HOH HOH A . 
C 2 HOH 10 2010 2010 HOH HOH A . 
C 2 HOH 11 2011 2011 HOH HOH A . 
C 2 HOH 12 2012 2012 HOH HOH A . 
C 2 HOH 13 2013 2013 HOH HOH A . 
C 2 HOH 14 2014 2014 HOH HOH A . 
C 2 HOH 15 2015 2015 HOH HOH A . 
C 2 HOH 16 2016 2016 HOH HOH A . 
C 2 HOH 17 2017 2017 HOH HOH A . 
C 2 HOH 18 2018 2018 HOH HOH A . 
C 2 HOH 19 2019 2019 HOH HOH A . 
C 2 HOH 20 2020 2020 HOH HOH A . 
C 2 HOH 21 2021 2021 HOH HOH A . 
C 2 HOH 22 2022 2022 HOH HOH A . 
C 2 HOH 23 2023 2023 HOH HOH A . 
C 2 HOH 24 2024 2024 HOH HOH A . 
C 2 HOH 25 2025 2025 HOH HOH A . 
C 2 HOH 26 2026 2026 HOH HOH A . 
C 2 HOH 27 2027 2027 HOH HOH A . 
C 2 HOH 28 2028 2028 HOH HOH A . 
C 2 HOH 29 2029 2029 HOH HOH A . 
C 2 HOH 30 2030 2030 HOH HOH A . 
C 2 HOH 31 2031 2031 HOH HOH A . 
C 2 HOH 32 2032 2032 HOH HOH A . 
C 2 HOH 33 2033 2033 HOH HOH A . 
C 2 HOH 34 2034 2034 HOH HOH A . 
C 2 HOH 35 2035 2035 HOH HOH A . 
C 2 HOH 36 2036 2036 HOH HOH A . 
C 2 HOH 37 2037 2037 HOH HOH A . 
C 2 HOH 38 2038 2038 HOH HOH A . 
C 2 HOH 39 2039 2039 HOH HOH A . 
C 2 HOH 40 2040 2040 HOH HOH A . 
C 2 HOH 41 2041 2041 HOH HOH A . 
C 2 HOH 42 2042 2042 HOH HOH A . 
C 2 HOH 43 2043 2043 HOH HOH A . 
C 2 HOH 44 2044 2044 HOH HOH A . 
C 2 HOH 45 2045 2045 HOH HOH A . 
C 2 HOH 46 2046 2046 HOH HOH A . 
C 2 HOH 47 2047 2047 HOH HOH A . 
C 2 HOH 48 2048 2048 HOH HOH A . 
C 2 HOH 49 2049 2049 HOH HOH A . 
C 2 HOH 50 2050 2050 HOH HOH A . 
C 2 HOH 51 2051 2051 HOH HOH A . 
C 2 HOH 52 2052 2052 HOH HOH A . 
C 2 HOH 53 2053 2053 HOH HOH A . 
C 2 HOH 54 2054 2054 HOH HOH A . 
C 2 HOH 55 2055 2055 HOH HOH A . 
C 2 HOH 56 2056 2056 HOH HOH A . 
C 2 HOH 57 2057 2057 HOH HOH A . 
C 2 HOH 58 2058 2058 HOH HOH A . 
C 2 HOH 59 2059 2059 HOH HOH A . 
C 2 HOH 60 2060 2060 HOH HOH A . 
C 2 HOH 61 2061 2061 HOH HOH A . 
C 2 HOH 62 2062 2062 HOH HOH A . 
C 2 HOH 63 2063 2063 HOH HOH A . 
C 2 HOH 64 2064 2064 HOH HOH A . 
C 2 HOH 65 2065 2065 HOH HOH A . 
C 2 HOH 66 2066 2066 HOH HOH A . 
C 2 HOH 67 2067 2067 HOH HOH A . 
C 2 HOH 68 2068 2068 HOH HOH A . 
C 2 HOH 69 2069 2069 HOH HOH A . 
C 2 HOH 70 2070 2070 HOH HOH A . 
C 2 HOH 71 2071 2071 HOH HOH A . 
C 2 HOH 72 2072 2072 HOH HOH A . 
C 2 HOH 73 2073 2073 HOH HOH A . 
C 2 HOH 74 2074 2074 HOH HOH A . 
C 2 HOH 75 2075 2075 HOH HOH A . 
C 2 HOH 76 2076 2076 HOH HOH A . 
C 2 HOH 77 2077 2077 HOH HOH A . 
C 2 HOH 78 2078 2078 HOH HOH A . 
C 2 HOH 79 2079 2079 HOH HOH A . 
C 2 HOH 80 2080 2080 HOH HOH A . 
C 2 HOH 81 2081 2081 HOH HOH A . 
C 2 HOH 82 2082 2082 HOH HOH A . 
C 2 HOH 83 2083 2083 HOH HOH A . 
C 2 HOH 84 2084 2084 HOH HOH A . 
C 2 HOH 85 2085 2085 HOH HOH A . 
C 2 HOH 86 2086 2086 HOH HOH A . 
D 2 HOH 1  2001 2001 HOH HOH B . 
D 2 HOH 2  2002 2002 HOH HOH B . 
D 2 HOH 3  2003 2003 HOH HOH B . 
D 2 HOH 4  2004 2004 HOH HOH B . 
D 2 HOH 5  2005 2005 HOH HOH B . 
D 2 HOH 6  2006 2006 HOH HOH B . 
D 2 HOH 7  2007 2007 HOH HOH B . 
D 2 HOH 8  2008 2008 HOH HOH B . 
D 2 HOH 9  2009 2009 HOH HOH B . 
D 2 HOH 10 2010 2010 HOH HOH B . 
D 2 HOH 11 2011 2011 HOH HOH B . 
D 2 HOH 12 2012 2012 HOH HOH B . 
D 2 HOH 13 2013 2013 HOH HOH B . 
D 2 HOH 14 2014 2014 HOH HOH B . 
D 2 HOH 15 2015 2015 HOH HOH B . 
D 2 HOH 16 2016 2016 HOH HOH B . 
D 2 HOH 17 2017 2017 HOH HOH B . 
D 2 HOH 18 2018 2018 HOH HOH B . 
D 2 HOH 19 2019 2019 HOH HOH B . 
D 2 HOH 20 2020 2020 HOH HOH B . 
D 2 HOH 21 2021 2021 HOH HOH B . 
D 2 HOH 22 2022 2022 HOH HOH B . 
D 2 HOH 23 2023 2023 HOH HOH B . 
D 2 HOH 24 2024 2024 HOH HOH B . 
D 2 HOH 25 2025 2025 HOH HOH B . 
D 2 HOH 26 2026 2026 HOH HOH B . 
D 2 HOH 27 2027 2027 HOH HOH B . 
D 2 HOH 28 2028 2028 HOH HOH B . 
D 2 HOH 29 2029 2029 HOH HOH B . 
D 2 HOH 30 2030 2030 HOH HOH B . 
D 2 HOH 31 2031 2031 HOH HOH B . 
D 2 HOH 32 2032 2032 HOH HOH B . 
D 2 HOH 33 2033 2033 HOH HOH B . 
D 2 HOH 34 2034 2034 HOH HOH B . 
D 2 HOH 35 2035 2035 HOH HOH B . 
D 2 HOH 36 2036 2036 HOH HOH B . 
D 2 HOH 37 2037 2037 HOH HOH B . 
D 2 HOH 38 2038 2038 HOH HOH B . 
D 2 HOH 39 2039 2039 HOH HOH B . 
D 2 HOH 40 2040 2040 HOH HOH B . 
D 2 HOH 41 2041 2041 HOH HOH B . 
D 2 HOH 42 2042 2042 HOH HOH B . 
D 2 HOH 43 2043 2043 HOH HOH B . 
D 2 HOH 44 2044 2044 HOH HOH B . 
D 2 HOH 45 2045 2045 HOH HOH B . 
D 2 HOH 46 2046 2046 HOH HOH B . 
D 2 HOH 47 2047 2047 HOH HOH B . 
D 2 HOH 48 2048 2048 HOH HOH B . 
D 2 HOH 49 2049 2049 HOH HOH B . 
D 2 HOH 50 2050 2050 HOH HOH B . 
D 2 HOH 51 2051 2051 HOH HOH B . 
D 2 HOH 52 2052 2052 HOH HOH B . 
D 2 HOH 53 2053 2053 HOH HOH B . 
D 2 HOH 54 2054 2054 HOH HOH B . 
D 2 HOH 55 2055 2055 HOH HOH B . 
D 2 HOH 56 2056 2056 HOH HOH B . 
D 2 HOH 57 2057 2057 HOH HOH B . 
D 2 HOH 58 2058 2058 HOH HOH B . 
D 2 HOH 59 2059 2059 HOH HOH B . 
D 2 HOH 60 2060 2060 HOH HOH B . 
D 2 HOH 61 2061 2061 HOH HOH B . 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C 
2 1 B,D 
# 
_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_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 2013-02-27 
2 'Structure model' 1 1 2013-03-20 
3 'Structure model' 1 2 2018-01-17 
4 'Structure model' 1 3 2019-05-08 
# 
_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' 'Data collection'          
3 4 'Structure model' 'Data collection'          
4 4 'Structure model' 'Experimental preparation' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 3 'Structure model' diffrn_source      
2 4 'Structure model' exptl_crystal_grow 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 3 'Structure model' '_diffrn_source.pdbx_synchrotron_site' 
2 4 'Structure model' '_exptl_crystal_grow.temp'             
# 
loop_
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][3] 
'X-RAY DIFFRACTION' 1 ? refined 20.5296 -18.1824 -4.9221  0.0988 0.1736 0.2148 0.0124  -0.0329 0.1005  3.0008 4.1223 4.0315 1.9262 
0.6155  0.2449  0.1178  -0.2082 -0.3741 0.3019  -0.3031 -0.5497 0.2012 0.2040  0.1535 
'X-RAY DIFFRACTION' 2 ? refined 23.8863 -12.9932 -28.0034 0.2656 0.2081 0.2139 -0.0322 0.1552  -0.0497 3.4203 4.1187 3.0880 2.9674 
-0.5707 -0.1387 -0.4227 0.5057  -0.4410 -0.7590 0.2489  -0.6841 0.2759 -0.0630 0.0728 
# 
loop_
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
'X-RAY DIFFRACTION' 1 1 ? ? ? ? ? ? ? ? ? '(CHAIN A AND RESSEQ 1:110)' 
'X-RAY DIFFRACTION' 2 2 ? ? ? ? ? ? ? ? ? '(CHAIN B AND RESSEQ 2:110)' 
# 
loop_
_software.name 
_software.classification 
_software.version 
_software.citation_id 
_software.pdbx_ordinal 
PHENIX refinement       '(PHENIX.REFINE)' ? 1 
XDS    'data reduction' .                 ? 2 
XSCALE 'data scaling'   .                 ? 3 
PHASER phasing          .                 ? 4 
# 
_pdbx_entry_details.entry_id             4BCZ 
_pdbx_entry_details.compound_details     ? 
_pdbx_entry_details.source_details       ? 
_pdbx_entry_details.nonpolymer_details   ? 
_pdbx_entry_details.sequence_details     
;MUTATIONS C6A, C111A, C146S DELETION OF
RESIDUES 49-81 AND 124-139) AND REPLACEMENT BY GAG
TRIPEPTIDE LINKERS.
;
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   O 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   HIS 
_pdbx_validate_close_contact.auth_seq_id_1    80 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   ? 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    2059 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             2.19 
# 
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 HIS A 80 ? ? -96.89  35.05 
2 1 SER B 68 ? ? -155.17 83.42 
# 
_pdbx_unobs_or_zero_occ_residues.id               1 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num    1 
_pdbx_unobs_or_zero_occ_residues.polymer_flag     Y 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag   1 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id     B 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id     ALA 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id      1 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code     ? 
_pdbx_unobs_or_zero_occ_residues.label_asym_id    B 
_pdbx_unobs_or_zero_occ_residues.label_comp_id    ALA 
_pdbx_unobs_or_zero_occ_residues.label_seq_id     1 
# 
_pdbx_entity_nonpoly.entity_id   2 
_pdbx_entity_nonpoly.name        water 
_pdbx_entity_nonpoly.comp_id     HOH 
# 
