data_9ARR
# 
_entry.id   9ARR 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9ARR         pdb_00009arr 10.2210/pdb9arr/pdb 
WWPDB D_1000281844 ?            ?                   
# 
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 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-01-22 ? 
2 'Structure model' 1 1 2025-04-23 ? 
3 'Structure model' 1 2 2025-04-30 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
loop_
_pdbx_audit_revision_group.ordinal 
_pdbx_audit_revision_group.revision_ordinal 
_pdbx_audit_revision_group.data_content_type 
_pdbx_audit_revision_group.group 
1 2 'Structure model' 'Database references' 
2 3 'Structure model' 'Database references' 
# 
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 2 'Structure model' citation        
2 2 'Structure model' citation_author 
3 3 'Structure model' citation        
4 3 'Structure model' citation_author 
# 
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  2 'Structure model' '_citation.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.pdbx_database_id_DOI'    
6  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
7  2 'Structure model' '_citation.title'                   
8  2 'Structure model' '_citation.year'                    
9  3 'Structure model' '_citation.journal_volume'          
10 3 'Structure model' '_citation.page_first'              
11 3 'Structure model' '_citation.page_last'               
12 3 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9ARR 
_pdbx_database_status.recvd_initial_deposition_date   2024-02-23 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_database_related.db_name        PDB 
_pdbx_database_related.details        'Crystal structure of AF9 YEATS domain in complex with acetylated at K1007 MOZ' 
_pdbx_database_related.db_id          9ARO 
_pdbx_database_related.content_type   unspecified 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              tatiana.kutateladze@cuanschutz.edu 
_pdbx_contact_author.name_first         Tatiana 
_pdbx_contact_author.name_last          Kutateladze 
_pdbx_contact_author.name_mi            G 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0001-7375-6990 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Selvam, K.'        1 ? 
'Kutateladze, T.G.' 2 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Nat.Struct.Mol.Biol. 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           1545-9985 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            32 
_citation.language                  ? 
_citation.page_first                709 
_citation.page_last                 718 
_citation.title                     'A multivalent engagement of ENL with MOZ.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41594-024-01455-8 
_citation.pdbx_database_id_PubMed   39794553 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Becht, D.C.'       1  ? 
primary 'Selvam, K.'        2  ? 
primary 'Lachance, C.'      3  ? 
primary 'Cote, V.'          4  ? 
primary 'Li, K.'            5  ? 
primary 'Nguyen, M.C.'      6  ? 
primary 'Pareek, A.'        7  ? 
primary 'Shi, X.'           8  ? 
primary 'Wen, H.'           9  ? 
primary 'Blanco, M.A.'      10 ? 
primary 'Cote, J.'          11 ? 
primary 'Kutateladze, T.G.' 12 ? 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Protein AF-9'                    16328.885 2   ?        ? 'YEATS domain'                           ? 
2 polymer     syn 'Histone acetyltransferase KAT6A' 1709.146  1   2.3.1.48 ? 'residues 1005-1017 (Uniprot numbering)' 
'residues K1007 and K1014 crotonylated (Uniprot numbering)' 
3 non-polymer syn 'LITHIUM ION'                     6.941     2   ?        ? ?                                        ? 
4 non-polymer syn 'NITRATE ION'                     62.005    4   ?        ? ?                                        ? 
5 non-polymer syn 'DI(HYDROXYETHYL)ETHER'           106.120   1   ?        ? ?                                        ? 
6 non-polymer syn GLYCEROL                          92.094    4   ?        ? ?                                        ? 
7 water       nat water                             18.015    127 ?        ? ?                                        ? 
# 
loop_
_entity_name_com.entity_id 
_entity_name_com.name 
1 
;ALL1-fused gene from chromosome 9 protein,Myeloid/lymphoid or mixed-lineage leukemia translocated to chromosome 3 protein,YEATS domain-containing protein 3
;
2 
;MOZ,YBF2/SAS3,SAS2 and TIP60 protein 3,MYST-3,Monocytic leukemia zinc finger protein,Runt-related transcription factor-binding protein 2,Zinc finger protein 220
;
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;MASSCAVQVKLELGHRAQVRKKPTVEGFTHDWMVFVRGPEHSNIQHFVEKVVFHLHESFPRPKRVCKDPPYKVEESGYAG
FILPIEVYFKNKEEPRKVRFDYDLFLHLEGHPPVNHLRCEKLTFNNPTEDFRRKLLKA
;
;MASSCAVQVKLELGHRAQVRKKPTVEGFTHDWMVFVRGPEHSNIQHFVEKVVFHLHESFPRPKRVCKDPPYKVEESGYAG
FILPIEVYFKNKEEPRKVRFDYDLFLHLEGHPPVNHLRCEKLTFNNPTEDFRRKLLKA
;
A,B ? 
2 'polypeptide(L)' no yes 'LT(KCR)PTLKRK(KCR)PFL' LTXPTLKRKXPFL C   ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'LITHIUM ION'           LI  
4 'NITRATE ION'           NO3 
5 'DI(HYDROXYETHYL)ETHER' PEG 
6 GLYCEROL                GOL 
7 water                   HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   ALA n 
1 3   SER n 
1 4   SER n 
1 5   CYS n 
1 6   ALA n 
1 7   VAL n 
1 8   GLN n 
1 9   VAL n 
1 10  LYS n 
1 11  LEU n 
1 12  GLU n 
1 13  LEU n 
1 14  GLY n 
1 15  HIS n 
1 16  ARG n 
1 17  ALA n 
1 18  GLN n 
1 19  VAL n 
1 20  ARG n 
1 21  LYS n 
1 22  LYS n 
1 23  PRO n 
1 24  THR n 
1 25  VAL n 
1 26  GLU n 
1 27  GLY n 
1 28  PHE n 
1 29  THR n 
1 30  HIS n 
1 31  ASP n 
1 32  TRP n 
1 33  MET n 
1 34  VAL n 
1 35  PHE n 
1 36  VAL n 
1 37  ARG n 
1 38  GLY n 
1 39  PRO n 
1 40  GLU n 
1 41  HIS n 
1 42  SER n 
1 43  ASN n 
1 44  ILE n 
1 45  GLN n 
1 46  HIS n 
1 47  PHE n 
1 48  VAL n 
1 49  GLU n 
1 50  LYS n 
1 51  VAL n 
1 52  VAL n 
1 53  PHE n 
1 54  HIS n 
1 55  LEU n 
1 56  HIS n 
1 57  GLU n 
1 58  SER n 
1 59  PHE n 
1 60  PRO n 
1 61  ARG n 
1 62  PRO n 
1 63  LYS n 
1 64  ARG n 
1 65  VAL n 
1 66  CYS n 
1 67  LYS n 
1 68  ASP n 
1 69  PRO n 
1 70  PRO n 
1 71  TYR n 
1 72  LYS n 
1 73  VAL n 
1 74  GLU n 
1 75  GLU n 
1 76  SER n 
1 77  GLY n 
1 78  TYR n 
1 79  ALA n 
1 80  GLY n 
1 81  PHE n 
1 82  ILE n 
1 83  LEU n 
1 84  PRO n 
1 85  ILE n 
1 86  GLU n 
1 87  VAL n 
1 88  TYR n 
1 89  PHE n 
1 90  LYS n 
1 91  ASN n 
1 92  LYS n 
1 93  GLU n 
1 94  GLU n 
1 95  PRO n 
1 96  ARG n 
1 97  LYS n 
1 98  VAL n 
1 99  ARG n 
1 100 PHE n 
1 101 ASP n 
1 102 TYR n 
1 103 ASP n 
1 104 LEU n 
1 105 PHE n 
1 106 LEU n 
1 107 HIS n 
1 108 LEU n 
1 109 GLU n 
1 110 GLY n 
1 111 HIS n 
1 112 PRO n 
1 113 PRO n 
1 114 VAL n 
1 115 ASN n 
1 116 HIS n 
1 117 LEU n 
1 118 ARG n 
1 119 CYS n 
1 120 GLU n 
1 121 LYS n 
1 122 LEU n 
1 123 THR n 
1 124 PHE n 
1 125 ASN n 
1 126 ASN n 
1 127 PRO n 
1 128 THR n 
1 129 GLU n 
1 130 ASP n 
1 131 PHE n 
1 132 ARG n 
1 133 ARG n 
1 134 LYS n 
1 135 LEU n 
1 136 LEU n 
1 137 LYS n 
1 138 ALA n 
2 1   LEU n 
2 2   THR n 
2 3   KCR n 
2 4   PRO n 
2 5   THR n 
2 6   LEU n 
2 7   LYS n 
2 8   ARG n 
2 9   LYS n 
2 10  KCR n 
2 11  PRO n 
2 12  PHE n 
2 13  LEU 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                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   138 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'MLLT3, AF9, YEATS3' 
_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     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       13 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   human 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.details                ? 
# 
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  
GOL non-polymer         . GLYCEROL                'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
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 
KCR 'L-peptide linking' n N-6-crotonyl-L-lysine   ?                               'C10 H18 N2 O3'  214.262 
LEU 'L-peptide linking' y LEUCINE                 ?                               'C6 H13 N O2'    131.173 
LI  non-polymer         . 'LITHIUM ION'           ?                               'Li 1'           6.941   
LYS 'L-peptide linking' y LYSINE                  ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE              ?                               'C5 H11 N O2 S'  149.211 
NO3 non-polymer         . 'NITRATE ION'           ?                               'N O3 -1'        62.005  
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER' ?                               'C4 H10 O3'      106.120 
PHE 'L-peptide linking' y PHENYLALANINE           ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE                 ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE                  ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE               ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN              ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE                ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE                  ?                               'C5 H11 N O2'    117.146 
# 
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   MET 1   1   1   MET MET A . n 
A 1 2   ALA 2   2   2   ALA ALA A . n 
A 1 3   SER 3   3   3   SER SER A . n 
A 1 4   SER 4   4   4   SER SER A . n 
A 1 5   CYS 5   5   5   CYS CYS 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   GLN 8   8   8   GLN GLN A . n 
A 1 9   VAL 9   9   9   VAL VAL A . n 
A 1 10  LYS 10  10  10  LYS LYS A . n 
A 1 11  LEU 11  11  11  LEU LEU A . n 
A 1 12  GLU 12  12  12  GLU GLU A . n 
A 1 13  LEU 13  13  13  LEU LEU A . n 
A 1 14  GLY 14  14  14  GLY GLY A . n 
A 1 15  HIS 15  15  15  HIS HIS A . n 
A 1 16  ARG 16  16  16  ARG ARG A . n 
A 1 17  ALA 17  17  17  ALA ALA A . n 
A 1 18  GLN 18  18  18  GLN GLN A . n 
A 1 19  VAL 19  19  19  VAL VAL A . n 
A 1 20  ARG 20  20  20  ARG ARG A . n 
A 1 21  LYS 21  21  21  LYS LYS A . n 
A 1 22  LYS 22  22  22  LYS LYS A . n 
A 1 23  PRO 23  23  23  PRO PRO A . n 
A 1 24  THR 24  24  24  THR THR A . n 
A 1 25  VAL 25  25  25  VAL VAL A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  GLY 27  27  27  GLY GLY A . n 
A 1 28  PHE 28  28  28  PHE PHE A . n 
A 1 29  THR 29  29  29  THR THR A . n 
A 1 30  HIS 30  30  30  HIS HIS A . n 
A 1 31  ASP 31  31  31  ASP ASP A . n 
A 1 32  TRP 32  32  32  TRP TRP A . n 
A 1 33  MET 33  33  33  MET MET A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  PHE 35  35  35  PHE PHE A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ARG 37  37  37  ARG ARG A . n 
A 1 38  GLY 38  38  38  GLY GLY A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  GLU 40  40  40  GLU GLU A . n 
A 1 41  HIS 41  41  41  HIS HIS A . n 
A 1 42  SER 42  42  42  SER SER A . n 
A 1 43  ASN 43  43  43  ASN ASN A . n 
A 1 44  ILE 44  44  44  ILE ILE A . n 
A 1 45  GLN 45  45  45  GLN GLN A . n 
A 1 46  HIS 46  46  46  HIS HIS A . n 
A 1 47  PHE 47  47  47  PHE PHE A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  GLU 49  49  49  GLU GLU A . n 
A 1 50  LYS 50  50  50  LYS LYS A . n 
A 1 51  VAL 51  51  51  VAL VAL A . n 
A 1 52  VAL 52  52  52  VAL VAL A . n 
A 1 53  PHE 53  53  53  PHE PHE A . n 
A 1 54  HIS 54  54  54  HIS HIS A . n 
A 1 55  LEU 55  55  55  LEU LEU A . n 
A 1 56  HIS 56  56  56  HIS HIS A . n 
A 1 57  GLU 57  57  57  GLU GLU A . n 
A 1 58  SER 58  58  58  SER SER A . n 
A 1 59  PHE 59  59  59  PHE PHE A . n 
A 1 60  PRO 60  60  60  PRO PRO A . n 
A 1 61  ARG 61  61  61  ARG ARG A . n 
A 1 62  PRO 62  62  62  PRO PRO A . n 
A 1 63  LYS 63  63  63  LYS LYS A . n 
A 1 64  ARG 64  64  64  ARG ARG A . n 
A 1 65  VAL 65  65  65  VAL VAL A . n 
A 1 66  CYS 66  66  66  CYS CYS A . n 
A 1 67  LYS 67  67  67  LYS LYS A . n 
A 1 68  ASP 68  68  68  ASP ASP A . n 
A 1 69  PRO 69  69  69  PRO PRO A . n 
A 1 70  PRO 70  70  70  PRO PRO A . n 
A 1 71  TYR 71  71  71  TYR TYR A . n 
A 1 72  LYS 72  72  72  LYS LYS A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  GLU 74  74  74  GLU GLU A . n 
A 1 75  GLU 75  75  75  GLU GLU A . n 
A 1 76  SER 76  76  76  SER SER A . n 
A 1 77  GLY 77  77  77  GLY GLY A . n 
A 1 78  TYR 78  78  78  TYR TYR A . n 
A 1 79  ALA 79  79  79  ALA ALA A . n 
A 1 80  GLY 80  80  80  GLY GLY A . n 
A 1 81  PHE 81  81  81  PHE PHE A . n 
A 1 82  ILE 82  82  82  ILE ILE A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  PRO 84  84  84  PRO PRO A . n 
A 1 85  ILE 85  85  85  ILE ILE A . n 
A 1 86  GLU 86  86  86  GLU GLU A . n 
A 1 87  VAL 87  87  87  VAL VAL A . n 
A 1 88  TYR 88  88  88  TYR TYR A . n 
A 1 89  PHE 89  89  89  PHE PHE A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  ASN 91  91  91  ASN ASN A . n 
A 1 92  LYS 92  92  92  LYS LYS A . n 
A 1 93  GLU 93  93  93  GLU GLU A . n 
A 1 94  GLU 94  94  94  GLU GLU A . n 
A 1 95  PRO 95  95  95  PRO PRO A . n 
A 1 96  ARG 96  96  96  ARG ARG A . n 
A 1 97  LYS 97  97  97  LYS LYS A . n 
A 1 98  VAL 98  98  98  VAL VAL A . n 
A 1 99  ARG 99  99  99  ARG ARG A . n 
A 1 100 PHE 100 100 100 PHE PHE A . n 
A 1 101 ASP 101 101 101 ASP ASP A . n 
A 1 102 TYR 102 102 102 TYR TYR A . n 
A 1 103 ASP 103 103 103 ASP ASP A . n 
A 1 104 LEU 104 104 104 LEU LEU A . n 
A 1 105 PHE 105 105 105 PHE PHE A . n 
A 1 106 LEU 106 106 106 LEU LEU A . n 
A 1 107 HIS 107 107 107 HIS HIS A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 GLU 109 109 109 GLU GLU A . n 
A 1 110 GLY 110 110 110 GLY GLY A . n 
A 1 111 HIS 111 111 111 HIS HIS A . n 
A 1 112 PRO 112 112 112 PRO PRO A . n 
A 1 113 PRO 113 113 113 PRO PRO A . n 
A 1 114 VAL 114 114 114 VAL VAL A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 HIS 116 116 116 HIS HIS A . n 
A 1 117 LEU 117 117 117 LEU LEU A . n 
A 1 118 ARG 118 118 118 ARG ARG A . n 
A 1 119 CYS 119 119 119 CYS CYS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 LYS 121 121 121 LYS LYS A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 THR 123 123 123 THR THR A . n 
A 1 124 PHE 124 124 124 PHE PHE A . n 
A 1 125 ASN 125 125 125 ASN ASN A . n 
A 1 126 ASN 126 126 126 ASN ASN A . n 
A 1 127 PRO 127 127 127 PRO PRO A . n 
A 1 128 THR 128 128 128 THR THR A . n 
A 1 129 GLU 129 129 129 GLU GLU A . n 
A 1 130 ASP 130 130 130 ASP ASP A . n 
A 1 131 PHE 131 131 131 PHE PHE A . n 
A 1 132 ARG 132 132 132 ARG ARG A . n 
A 1 133 ARG 133 133 133 ARG ARG A . n 
A 1 134 LYS 134 134 134 LYS LYS A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 ALA 138 138 138 ALA ALA A . n 
B 1 1   MET 1   1   1   MET MET B . n 
B 1 2   ALA 2   2   2   ALA ALA B . n 
B 1 3   SER 3   3   3   SER SER B . n 
B 1 4   SER 4   4   4   SER SER B . n 
B 1 5   CYS 5   5   5   CYS CYS 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   GLN 8   8   8   GLN GLN B . n 
B 1 9   VAL 9   9   9   VAL VAL B . n 
B 1 10  LYS 10  10  10  LYS LYS B . n 
B 1 11  LEU 11  11  11  LEU LEU B . n 
B 1 12  GLU 12  12  12  GLU GLU B . n 
B 1 13  LEU 13  13  13  LEU LEU B . n 
B 1 14  GLY 14  14  14  GLY GLY B . n 
B 1 15  HIS 15  15  15  HIS HIS B . n 
B 1 16  ARG 16  16  16  ARG ARG B . n 
B 1 17  ALA 17  17  17  ALA ALA B . n 
B 1 18  GLN 18  18  18  GLN GLN B . n 
B 1 19  VAL 19  19  19  VAL VAL B . n 
B 1 20  ARG 20  20  20  ARG ARG B . n 
B 1 21  LYS 21  21  21  LYS LYS B . n 
B 1 22  LYS 22  22  22  LYS LYS B . n 
B 1 23  PRO 23  23  23  PRO PRO B . n 
B 1 24  THR 24  24  24  THR THR B . n 
B 1 25  VAL 25  25  25  VAL VAL B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  GLY 27  27  27  GLY GLY B . n 
B 1 28  PHE 28  28  28  PHE PHE B . n 
B 1 29  THR 29  29  29  THR THR B . n 
B 1 30  HIS 30  30  30  HIS HIS B . n 
B 1 31  ASP 31  31  31  ASP ASP B . n 
B 1 32  TRP 32  32  32  TRP TRP B . n 
B 1 33  MET 33  33  33  MET MET B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  PHE 35  35  35  PHE PHE B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ARG 37  37  37  ARG ARG B . n 
B 1 38  GLY 38  38  38  GLY GLY B . n 
B 1 39  PRO 39  39  39  PRO PRO B . n 
B 1 40  GLU 40  40  40  GLU GLU B . n 
B 1 41  HIS 41  41  41  HIS HIS B . n 
B 1 42  SER 42  42  42  SER SER B . n 
B 1 43  ASN 43  43  43  ASN ASN B . n 
B 1 44  ILE 44  44  44  ILE ILE B . n 
B 1 45  GLN 45  45  45  GLN GLN B . n 
B 1 46  HIS 46  46  46  HIS HIS B . n 
B 1 47  PHE 47  47  47  PHE PHE B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  GLU 49  49  49  GLU GLU B . n 
B 1 50  LYS 50  50  50  LYS LYS B . n 
B 1 51  VAL 51  51  51  VAL VAL B . n 
B 1 52  VAL 52  52  52  VAL VAL B . n 
B 1 53  PHE 53  53  53  PHE PHE B . n 
B 1 54  HIS 54  54  54  HIS HIS B . n 
B 1 55  LEU 55  55  55  LEU LEU B . n 
B 1 56  HIS 56  56  56  HIS HIS B . n 
B 1 57  GLU 57  57  57  GLU GLU B . n 
B 1 58  SER 58  58  58  SER SER B . n 
B 1 59  PHE 59  59  59  PHE PHE B . n 
B 1 60  PRO 60  60  60  PRO PRO B . n 
B 1 61  ARG 61  61  61  ARG ARG B . n 
B 1 62  PRO 62  62  62  PRO PRO B . n 
B 1 63  LYS 63  63  63  LYS LYS B . n 
B 1 64  ARG 64  64  64  ARG ARG B . n 
B 1 65  VAL 65  65  65  VAL VAL B . n 
B 1 66  CYS 66  66  66  CYS CYS B . n 
B 1 67  LYS 67  67  67  LYS LYS B . n 
B 1 68  ASP 68  68  68  ASP ASP B . n 
B 1 69  PRO 69  69  69  PRO PRO B . n 
B 1 70  PRO 70  70  70  PRO PRO B . n 
B 1 71  TYR 71  71  71  TYR TYR B . n 
B 1 72  LYS 72  72  72  LYS LYS B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  GLU 74  74  74  GLU GLU B . n 
B 1 75  GLU 75  75  75  GLU GLU B . n 
B 1 76  SER 76  76  76  SER SER B . n 
B 1 77  GLY 77  77  77  GLY GLY B . n 
B 1 78  TYR 78  78  78  TYR TYR B . n 
B 1 79  ALA 79  79  79  ALA ALA B . n 
B 1 80  GLY 80  80  80  GLY GLY B . n 
B 1 81  PHE 81  81  81  PHE PHE B . n 
B 1 82  ILE 82  82  82  ILE ILE B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  PRO 84  84  84  PRO PRO B . n 
B 1 85  ILE 85  85  85  ILE ILE B . n 
B 1 86  GLU 86  86  86  GLU GLU B . n 
B 1 87  VAL 87  87  87  VAL VAL B . n 
B 1 88  TYR 88  88  88  TYR TYR B . n 
B 1 89  PHE 89  89  89  PHE PHE B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  ASN 91  91  91  ASN ASN B . n 
B 1 92  LYS 92  92  92  LYS LYS B . n 
B 1 93  GLU 93  93  93  GLU GLU B . n 
B 1 94  GLU 94  94  94  GLU GLU B . n 
B 1 95  PRO 95  95  95  PRO PRO B . n 
B 1 96  ARG 96  96  96  ARG ARG B . n 
B 1 97  LYS 97  97  97  LYS LYS B . n 
B 1 98  VAL 98  98  98  VAL VAL B . n 
B 1 99  ARG 99  99  99  ARG ARG B . n 
B 1 100 PHE 100 100 100 PHE PHE B . n 
B 1 101 ASP 101 101 101 ASP ASP B . n 
B 1 102 TYR 102 102 102 TYR TYR B . n 
B 1 103 ASP 103 103 103 ASP ASP B . n 
B 1 104 LEU 104 104 104 LEU LEU B . n 
B 1 105 PHE 105 105 105 PHE PHE B . n 
B 1 106 LEU 106 106 106 LEU LEU B . n 
B 1 107 HIS 107 107 107 HIS HIS B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 GLU 109 109 109 GLU GLU B . n 
B 1 110 GLY 110 110 110 GLY GLY B . n 
B 1 111 HIS 111 111 111 HIS HIS B . n 
B 1 112 PRO 112 112 112 PRO PRO B . n 
B 1 113 PRO 113 113 113 PRO PRO B . n 
B 1 114 VAL 114 114 114 VAL VAL B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 HIS 116 116 116 HIS HIS B . n 
B 1 117 LEU 117 117 117 LEU LEU B . n 
B 1 118 ARG 118 118 118 ARG ARG B . n 
B 1 119 CYS 119 119 119 CYS CYS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 LYS 121 121 121 LYS LYS B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 THR 123 123 123 THR THR B . n 
B 1 124 PHE 124 124 124 PHE PHE B . n 
B 1 125 ASN 125 125 125 ASN ASN B . n 
B 1 126 ASN 126 126 126 ASN ASN B . n 
B 1 127 PRO 127 127 127 PRO PRO B . n 
B 1 128 THR 128 128 128 THR THR B . n 
B 1 129 GLU 129 129 129 GLU GLU B . n 
B 1 130 ASP 130 130 130 ASP ASP B . n 
B 1 131 PHE 131 131 131 PHE PHE B . n 
B 1 132 ARG 132 132 132 ARG ARG B . n 
B 1 133 ARG 133 133 133 ARG ARG B . n 
B 1 134 LYS 134 134 134 LYS LYS B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 LEU 136 136 136 LEU LEU B . n 
B 1 137 LYS 137 137 137 LYS LYS B . n 
B 1 138 ALA 138 138 138 ALA ALA B . n 
C 2 1   LEU 1   1   1   LEU LEU C . n 
C 2 2   THR 2   2   2   THR THR C . n 
C 2 3   KCR 3   3   3   KCR KCR C . n 
C 2 4   PRO 4   4   4   PRO PRO C . n 
C 2 5   THR 5   5   5   THR THR C . n 
C 2 6   LEU 6   6   6   LEU LEU C . n 
C 2 7   LYS 7   7   7   LYS LYS C . n 
C 2 8   ARG 8   8   8   ARG ARG C . n 
C 2 9   LYS 9   9   9   LYS LYS C . n 
C 2 10  KCR 10  10  10  KCR KCR C . n 
C 2 11  PRO 11  11  11  PRO PRO C . n 
C 2 12  PHE 12  12  12  PHE PHE C . n 
C 2 13  LEU 13  13  13  LEU LEU C . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        KCR 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   KCR 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
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 
D 3 LI  1  201 201 LI  LI  A . 
E 4 NO3 1  202 202 NO3 NO3 A . 
F 4 NO3 1  203 203 NO3 NO3 A . 
G 5 PEG 1  204 205 PEG PEG A . 
H 6 GOL 1  205 206 GOL GOL A . 
I 6 GOL 1  206 207 GOL GOL A . 
J 6 GOL 1  207 208 GOL GOL A . 
K 3 LI  1  201 201 LI  LI  B . 
L 4 NO3 1  202 202 NO3 NO3 B . 
M 4 NO3 1  203 203 NO3 NO3 B . 
N 6 GOL 1  204 204 GOL GOL B . 
O 7 HOH 1  301 68  HOH HOH A . 
O 7 HOH 2  302 105 HOH HOH A . 
O 7 HOH 3  303 63  HOH HOH A . 
O 7 HOH 4  304 33  HOH HOH A . 
O 7 HOH 5  305 108 HOH HOH A . 
O 7 HOH 6  306 107 HOH HOH A . 
O 7 HOH 7  307 102 HOH HOH A . 
O 7 HOH 8  308 10  HOH HOH A . 
O 7 HOH 9  309 100 HOH HOH A . 
O 7 HOH 10 310 6   HOH HOH A . 
O 7 HOH 11 311 103 HOH HOH A . 
O 7 HOH 12 312 13  HOH HOH A . 
O 7 HOH 13 313 84  HOH HOH A . 
O 7 HOH 14 314 60  HOH HOH A . 
O 7 HOH 15 315 77  HOH HOH A . 
O 7 HOH 16 316 59  HOH HOH A . 
O 7 HOH 17 317 52  HOH HOH A . 
O 7 HOH 18 318 31  HOH HOH A . 
O 7 HOH 19 319 88  HOH HOH A . 
O 7 HOH 20 320 18  HOH HOH A . 
O 7 HOH 21 321 76  HOH HOH A . 
O 7 HOH 22 322 73  HOH HOH A . 
O 7 HOH 23 323 53  HOH HOH A . 
O 7 HOH 24 324 74  HOH HOH A . 
O 7 HOH 25 325 40  HOH HOH A . 
O 7 HOH 26 326 8   HOH HOH A . 
O 7 HOH 27 327 55  HOH HOH A . 
O 7 HOH 28 328 19  HOH HOH A . 
O 7 HOH 29 329 99  HOH HOH A . 
O 7 HOH 30 330 4   HOH HOH A . 
O 7 HOH 31 331 70  HOH HOH A . 
O 7 HOH 32 332 86  HOH HOH A . 
O 7 HOH 33 333 46  HOH HOH A . 
O 7 HOH 34 334 25  HOH HOH A . 
O 7 HOH 35 335 36  HOH HOH A . 
O 7 HOH 36 336 80  HOH HOH A . 
O 7 HOH 37 337 106 HOH HOH A . 
O 7 HOH 38 338 28  HOH HOH A . 
O 7 HOH 39 339 126 HOH HOH A . 
O 7 HOH 40 340 27  HOH HOH A . 
O 7 HOH 41 341 44  HOH HOH A . 
O 7 HOH 42 342 98  HOH HOH A . 
O 7 HOH 43 343 123 HOH HOH A . 
O 7 HOH 44 344 110 HOH HOH A . 
O 7 HOH 45 345 89  HOH HOH A . 
O 7 HOH 46 346 127 HOH HOH A . 
O 7 HOH 47 347 50  HOH HOH A . 
O 7 HOH 48 348 92  HOH HOH A . 
O 7 HOH 49 349 38  HOH HOH A . 
O 7 HOH 50 350 67  HOH HOH A . 
O 7 HOH 51 351 78  HOH HOH A . 
O 7 HOH 52 352 61  HOH HOH A . 
O 7 HOH 53 353 121 HOH HOH A . 
O 7 HOH 54 354 65  HOH HOH A . 
O 7 HOH 55 355 91  HOH HOH A . 
O 7 HOH 56 356 101 HOH HOH A . 
P 7 HOH 1  301 64  HOH HOH B . 
P 7 HOH 2  302 58  HOH HOH B . 
P 7 HOH 3  303 12  HOH HOH B . 
P 7 HOH 4  304 118 HOH HOH B . 
P 7 HOH 5  305 83  HOH HOH B . 
P 7 HOH 6  306 37  HOH HOH B . 
P 7 HOH 7  307 41  HOH HOH B . 
P 7 HOH 8  308 43  HOH HOH B . 
P 7 HOH 9  309 96  HOH HOH B . 
P 7 HOH 10 310 117 HOH HOH B . 
P 7 HOH 11 311 51  HOH HOH B . 
P 7 HOH 12 312 79  HOH HOH B . 
P 7 HOH 13 313 35  HOH HOH B . 
P 7 HOH 14 314 16  HOH HOH B . 
P 7 HOH 15 315 104 HOH HOH B . 
P 7 HOH 16 316 29  HOH HOH B . 
P 7 HOH 17 317 24  HOH HOH B . 
P 7 HOH 18 318 75  HOH HOH B . 
P 7 HOH 19 319 124 HOH HOH B . 
P 7 HOH 20 320 72  HOH HOH B . 
P 7 HOH 21 321 85  HOH HOH B . 
P 7 HOH 22 322 87  HOH HOH B . 
P 7 HOH 23 323 66  HOH HOH B . 
P 7 HOH 24 324 71  HOH HOH B . 
P 7 HOH 25 325 113 HOH HOH B . 
P 7 HOH 26 326 5   HOH HOH B . 
P 7 HOH 27 327 49  HOH HOH B . 
P 7 HOH 28 328 94  HOH HOH B . 
P 7 HOH 29 329 11  HOH HOH B . 
P 7 HOH 30 330 125 HOH HOH B . 
P 7 HOH 31 331 17  HOH HOH B . 
P 7 HOH 32 332 14  HOH HOH B . 
P 7 HOH 33 333 22  HOH HOH B . 
P 7 HOH 34 334 42  HOH HOH B . 
P 7 HOH 35 335 48  HOH HOH B . 
P 7 HOH 36 336 69  HOH HOH B . 
P 7 HOH 37 337 45  HOH HOH B . 
P 7 HOH 38 338 114 HOH HOH B . 
P 7 HOH 39 339 56  HOH HOH B . 
P 7 HOH 40 340 9   HOH HOH B . 
P 7 HOH 41 341 93  HOH HOH B . 
P 7 HOH 42 342 57  HOH HOH B . 
P 7 HOH 43 343 26  HOH HOH B . 
P 7 HOH 44 344 34  HOH HOH B . 
P 7 HOH 45 345 2   HOH HOH B . 
P 7 HOH 46 346 3   HOH HOH B . 
P 7 HOH 47 347 95  HOH HOH B . 
P 7 HOH 48 348 62  HOH HOH B . 
P 7 HOH 49 349 119 HOH HOH B . 
P 7 HOH 50 350 54  HOH HOH B . 
P 7 HOH 51 351 39  HOH HOH B . 
P 7 HOH 52 352 81  HOH HOH B . 
P 7 HOH 53 353 21  HOH HOH B . 
P 7 HOH 54 354 32  HOH HOH B . 
P 7 HOH 55 355 122 HOH HOH B . 
P 7 HOH 56 356 90  HOH HOH B . 
P 7 HOH 57 357 23  HOH HOH B . 
P 7 HOH 58 358 1   HOH HOH B . 
P 7 HOH 59 359 120 HOH HOH B . 
P 7 HOH 60 360 30  HOH HOH B . 
P 7 HOH 61 361 82  HOH HOH B . 
Q 7 HOH 1  101 115 HOH HOH C . 
Q 7 HOH 2  102 15  HOH HOH C . 
Q 7 HOH 3  103 7   HOH HOH C . 
Q 7 HOH 4  104 97  HOH HOH C . 
Q 7 HOH 5  105 116 HOH HOH C . 
Q 7 HOH 6  106 20  HOH HOH C . 
Q 7 HOH 7  107 111 HOH HOH C . 
Q 7 HOH 8  108 47  HOH HOH C . 
Q 7 HOH 9  109 109 HOH HOH C . 
Q 7 HOH 10 110 112 HOH HOH C . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1 1 Y 1 B GLU 57 ? CG  ? B GLU 57 CG  
2 1 Y 1 B GLU 57 ? CD  ? B GLU 57 CD  
3 1 Y 1 B GLU 57 ? OE1 ? B GLU 57 OE1 
4 1 Y 1 B GLU 57 ? OE2 ? B GLU 57 OE2 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0415 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   113.64 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9ARR 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     143.364 
_cell.length_a_esd                 ? 
_cell.length_b                     49.021 
_cell.length_b_esd                 ? 
_cell.length_c                     78.133 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9ARR 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                5 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 1 2 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9ARR 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             3.66 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          66.39 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          MICROBATCH 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    '0.2 M Lithium nitrate pH 7.1, 20% w/v PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            291 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CMOS 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RDI CMOS_8M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-06-09 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   1.0722 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ALS BEAMLINE 4.2.2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.0722 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   4.2.2 
_diffrn_source.pdbx_synchrotron_site       ALS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9ARR 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.10 
_reflns.d_resolution_low                               45.97 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     27648 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           94.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.7 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.51 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.066 
_reflns.pdbx_Rpim_I_all                                0.034 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.056 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    2.10 
_reflns_shell.d_res_low                                     2.16 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           7865 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2370 
_reflns_shell.percent_possible_obs                          99.6 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               3.3 
_reflns_shell.pdbx_chi_squared                              0.47 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.7 
_reflns_shell.pdbx_Rrim_I_all                               0.754 
_reflns_shell.pdbx_Rpim_I_all                               0.407 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.867 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.632 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -3.71 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            -0.37 
_refine.aniso_B[2][2]                            5.99 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            -1.42 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               48.129 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.957 
_refine.correlation_coeff_Fo_to_Fc_free          0.936 
_refine.details                                  'HYDROGENS HAVE BEEN ADDED IN THE RIDING POSITIONS' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9ARR 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            2.10 
_refine.ls_d_res_low                             45.97 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     25539 
_refine.ls_number_reflns_R_free                  1318 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    91.47 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.20529 
_refine.ls_R_factor_R_free                       0.24748 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.20307 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.185 
_refine.pdbx_overall_ESU_R_Free                  0.174 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             5.758 
_refine.overall_SU_ML                            0.139 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       2.10 
_refine_hist.d_res_low                        45.97 
_refine_hist.number_atoms_solvent             127 
_refine_hist.number_atoms_total               2598 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        2422 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         49 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.010  0.012  2534 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.002  0.016  2415 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.649  1.682  3400 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.626  1.593  5583 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 7.516  5.000  286  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 7.645  5.000  27   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 15.840 10.000 436  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.072  0.200  350  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.011  0.020  2894 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.005  0.020  598  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 5.318  4.545  1153 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 5.280  4.546  1153 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 7.093  8.122  1436 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 7.092  8.125  1437 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 7.085  5.317  1381 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 7.082  5.318  1382 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 10.165 9.314  1965 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 12.879 48.79  2686 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 12.899 48.37  2676 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       2.100 
_refine_ls_shell.d_res_low                        2.154 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             109 
_refine_ls_shell.number_reflns_R_work             2026 
_refine_ls_shell.percent_reflns_obs               99.49 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.329 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.309 
# 
_struct.entry_id                     9ARR 
_struct.title                        'Crystal structure of AF9 YEATS domain in complex with dicrotonylated at K1007 and K1014 MOZ' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9ARR 
_struct_keywords.text            'AF9, MOZ, YEATS, crotonylation, Chromatin, TRANSCRIPTION' 
_struct_keywords.pdbx_keywords   TRANSCRIPTION 
# 
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 3 ? 
E N N 4 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 6 ? 
J N N 6 ? 
K N N 3 ? 
L N N 4 ? 
M N N 4 ? 
N N N 6 ? 
O N N 7 ? 
P N N 7 ? 
Q N N 7 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP AF9_HUMAN   P42568 ? 1 
;MASSCAVQVKLELGHRAQVRKKPTVEGFTHDWMVFVRGPEHSNIQHFVEKVVFHLHESFPRPKRVCKDPPYKVEESGYAG
FILPIEVYFKNKEEPRKVRFDYDLFLHLEGHPPVNHLRCEKLTFNNPTEDFRRKLLKA
;
1    
2 UNP KAT6A_HUMAN Q92794 ? 2 LTKPTLKRKKPFL 1005 
# 
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 9ARR A 1 ? 138 ? P42568 1    ? 138  ? 1 138 
2 1 9ARR B 1 ? 138 ? P42568 1    ? 138  ? 1 138 
3 2 9ARR C 1 ? 13  ? Q92794 1005 ? 1017 ? 1 13  
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   trimeric 
_pdbx_struct_assembly.oligomeric_count     3 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 4320  ? 
1 MORE         -24   ? 
1 'SSA (A^2)'  17240 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P,Q 
# 
_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_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 GLY A 38  ? SER A 42  ? GLY A 38  SER A 42  5 ? 5  
HELX_P HELX_P2 AA2 ASN A 43  ? HIS A 46  ? ASN A 43  HIS A 46  5 ? 4  
HELX_P HELX_P3 AA3 THR A 128 ? ALA A 138 ? THR A 128 ALA A 138 1 ? 11 
HELX_P HELX_P4 AA4 GLY B 38  ? SER B 42  ? GLY B 38  SER B 42  5 ? 5  
HELX_P HELX_P5 AA5 ASN B 43  ? HIS B 46  ? ASN B 43  HIS B 46  5 ? 4  
HELX_P HELX_P6 AA6 THR B 128 ? LYS B 137 ? THR B 128 LYS B 137 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale both ? C THR 2  C  ? ? ? 1_555 C KCR 3  N  ? ? C THR 2  C KCR 3   1_555 ? ? ? ? ? ? ? 1.320 ? ? 
covale2 covale both ? C KCR 3  C  ? ? ? 1_555 C PRO 4  N  ? ? C KCR 3  C PRO 4   1_555 ? ? ? ? ? ? ? 1.304 ? ? 
covale3 covale both ? C LYS 9  C  ? ? ? 1_555 C KCR 10 N  ? ? C LYS 9  C KCR 10  1_555 ? ? ? ? ? ? ? 1.304 ? ? 
covale4 covale both ? C KCR 10 C  ? ? ? 1_555 C PRO 11 N  ? ? C KCR 10 C PRO 11  1_555 ? ? ? ? ? ? ? 1.337 ? ? 
metalc1 metalc ?    ? A LYS 67 O  ? ? ? 1_555 D LI  .  LI ? ? A LYS 67 A LI  201 1_555 ? ? ? ? ? ? ? 2.217 ? ? 
metalc2 metalc ?    ? A TYR 71 OH ? ? ? 1_555 D LI  .  LI ? ? A TYR 71 A LI  201 1_555 ? ? ? ? ? ? ? 2.558 ? ? 
metalc3 metalc ?    ? B LYS 67 O  ? ? ? 1_555 K LI  .  LI ? ? B LYS 67 B LI  201 1_555 ? ? ? ? ? ? ? 2.559 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
_pdbx_struct_conn_angle.id                    1 
_pdbx_struct_conn_angle.ptnr1_label_atom_id   O 
_pdbx_struct_conn_angle.ptnr1_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr1_label_asym_id   A 
_pdbx_struct_conn_angle.ptnr1_label_comp_id   LYS 
_pdbx_struct_conn_angle.ptnr1_label_seq_id    67 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id    LYS 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id     67 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr1_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr2_label_atom_id   LI 
_pdbx_struct_conn_angle.ptnr2_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr2_label_asym_id   D 
_pdbx_struct_conn_angle.ptnr2_label_comp_id   LI 
_pdbx_struct_conn_angle.ptnr2_label_seq_id    . 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id    LI 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id     201 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr2_symmetry        1_555 
_pdbx_struct_conn_angle.ptnr3_label_atom_id   OH 
_pdbx_struct_conn_angle.ptnr3_label_alt_id    ? 
_pdbx_struct_conn_angle.ptnr3_label_asym_id   A 
_pdbx_struct_conn_angle.ptnr3_label_comp_id   TYR 
_pdbx_struct_conn_angle.ptnr3_label_seq_id    71 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id    ? 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id    A 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id    TYR 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id     71 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code    ? 
_pdbx_struct_conn_angle.ptnr3_symmetry        1_555 
_pdbx_struct_conn_angle.value                 113.7 
_pdbx_struct_conn_angle.value_esd             ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 KCR C 3  ? . . . . KCR C 3  ? 1_555 . . . . . . . LYS 1 KCR Crotonylation 'Named protein modification' 
2 KCR C 10 ? . . . . KCR C 10 ? 1_555 . . . . . . . LYS 1 KCR Crotonylation 'Named protein modification' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PRO 69 A . ? PRO 69 A PRO 70 A ? PRO 70 A 1 1.76   
2 GLU 94 A . ? GLU 94 A PRO 95 A ? PRO 95 A 1 -13.24 
3 PRO 69 B . ? PRO 69 B PRO 70 B ? PRO 70 B 1 -0.78  
4 GLU 94 B . ? GLU 94 B PRO 95 B ? PRO 95 B 1 -13.66 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 6 ? 
AA2 ? 4 ? 
AA3 ? 4 ? 
AA4 ? 4 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 TYR A 71  ? GLY A 77  ? TYR A 71  GLY A 77  
AA1 2 HIS A 30  ? ARG A 37  ? HIS A 30  ARG A 37  
AA1 3 SER A 3   ? VAL A 19  ? SER A 3   VAL A 19  
AA1 4 SER B 3   ? VAL B 19  ? SER B 3   VAL B 19  
AA1 5 HIS B 30  ? ARG B 37  ? HIS B 30  ARG B 37  
AA1 6 TYR B 71  ? GLY B 77  ? TYR B 71  GLY B 77  
AA2 1 VAL A 114 ? ASN A 125 ? VAL A 114 ASN A 125 
AA2 2 SER A 3   ? VAL A 19  ? SER A 3   VAL A 19  
AA2 3 SER B 3   ? VAL B 19  ? SER B 3   VAL B 19  
AA2 4 VAL B 114 ? ASN B 125 ? VAL B 114 ASN B 125 
AA3 1 LYS A 63  ? CYS A 66  ? LYS A 63  CYS A 66  
AA3 2 VAL A 48  ? HIS A 54  ? VAL A 48  HIS A 54  
AA3 3 PHE A 81  ? PHE A 89  ? PHE A 81  PHE A 89  
AA3 4 LYS A 97  ? LEU A 104 ? LYS A 97  LEU A 104 
AA4 1 LYS B 63  ? CYS B 66  ? LYS B 63  CYS B 66  
AA4 2 VAL B 48  ? HIS B 54  ? VAL B 48  HIS B 54  
AA4 3 PHE B 81  ? PHE B 89  ? PHE B 81  PHE B 89  
AA4 4 LYS B 97  ? LEU B 104 ? LYS B 97  LEU B 104 
# 
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 
AA1 1 2 O GLU A 75  ? O GLU A 75  N TRP A 32  ? N TRP A 32  
AA1 2 3 O ARG A 37  ? O ARG A 37  N GLU A 12  ? N GLU A 12  
AA1 3 4 N SER A 4   ? N SER A 4   O GLN B 8   ? O GLN B 8   
AA1 4 5 N GLU B 12  ? N GLU B 12  O ARG B 37  ? O ARG B 37  
AA1 5 6 N TRP B 32  ? N TRP B 32  O GLU B 75  ? O GLU B 75  
AA2 1 2 O PHE A 124 ? O PHE A 124 N VAL A 7   ? N VAL A 7   
AA2 2 3 N SER A 4   ? N SER A 4   O GLN B 8   ? O GLN B 8   
AA2 3 4 N VAL B 7   ? N VAL B 7   O PHE B 124 ? O PHE B 124 
AA3 1 2 O ARG A 64  ? O ARG A 64  N PHE A 53  ? N PHE A 53  
AA3 2 3 N HIS A 54  ? N HIS A 54  O PRO A 84  ? O PRO A 84  
AA3 3 4 N LEU A 83  ? N LEU A 83  O TYR A 102 ? O TYR A 102 
AA4 1 2 O ARG B 64  ? O ARG B 64  N PHE B 53  ? N PHE B 53  
AA4 2 3 N HIS B 54  ? N HIS B 54  O PRO B 84  ? O PRO B 84  
AA4 3 4 N ILE B 85  ? N ILE B 85  O PHE B 100 ? O PHE B 100 
# 
_pdbx_entry_details.entry_id                   9ARR 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_rmsd_angle.id 
_pdbx_validate_rmsd_angle.PDB_model_num 
_pdbx_validate_rmsd_angle.auth_atom_id_1 
_pdbx_validate_rmsd_angle.auth_asym_id_1 
_pdbx_validate_rmsd_angle.auth_comp_id_1 
_pdbx_validate_rmsd_angle.auth_seq_id_1 
_pdbx_validate_rmsd_angle.PDB_ins_code_1 
_pdbx_validate_rmsd_angle.label_alt_id_1 
_pdbx_validate_rmsd_angle.auth_atom_id_2 
_pdbx_validate_rmsd_angle.auth_asym_id_2 
_pdbx_validate_rmsd_angle.auth_comp_id_2 
_pdbx_validate_rmsd_angle.auth_seq_id_2 
_pdbx_validate_rmsd_angle.PDB_ins_code_2 
_pdbx_validate_rmsd_angle.label_alt_id_2 
_pdbx_validate_rmsd_angle.auth_atom_id_3 
_pdbx_validate_rmsd_angle.auth_asym_id_3 
_pdbx_validate_rmsd_angle.auth_comp_id_3 
_pdbx_validate_rmsd_angle.auth_seq_id_3 
_pdbx_validate_rmsd_angle.PDB_ins_code_3 
_pdbx_validate_rmsd_angle.label_alt_id_3 
_pdbx_validate_rmsd_angle.angle_value 
_pdbx_validate_rmsd_angle.angle_target_value 
_pdbx_validate_rmsd_angle.angle_deviation 
_pdbx_validate_rmsd_angle.angle_standard_deviation 
_pdbx_validate_rmsd_angle.linker_flag 
1 1 C  C KCR 3  ? ? N C PRO 4  ? ? CD C PRO 4  ? ? 111.99 128.40 -16.41 2.10 Y 
2 1 C  C KCR 10 ? ? N C PRO 11 ? ? CD C PRO 11 ? ? 105.33 128.40 -23.07 2.10 Y 
3 1 CA C PRO 11 ? ? N C PRO 11 ? ? CD C PRO 11 ? ? 101.37 111.70 -10.33 1.40 N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 HIS B 41 ? ? 59.05   19.18  
2 1 LYS B 92 ? ? -142.43 51.18  
3 1 PRO C 11 ? ? -44.86  150.37 
# 
_pdbx_validate_planes.id              1 
_pdbx_validate_planes.PDB_model_num   1 
_pdbx_validate_planes.auth_comp_id    ARG 
_pdbx_validate_planes.auth_asym_id    A 
_pdbx_validate_planes.auth_seq_id     61 
_pdbx_validate_planes.PDB_ins_code    ? 
_pdbx_validate_planes.label_alt_id    ? 
_pdbx_validate_planes.rmsd            0.086 
_pdbx_validate_planes.type            'SIDE CHAIN' 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 C KCR 3  C KCR 3  ? LYS 'modified residue' 
2 C KCR 10 C KCR 10 ? LYS 'modified residue' 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CYS N    N  N N 74  
CYS CA   C  N R 75  
CYS C    C  N N 76  
CYS O    O  N N 77  
CYS CB   C  N N 78  
CYS SG   S  N N 79  
CYS OXT  O  N N 80  
CYS H    H  N N 81  
CYS H2   H  N N 82  
CYS HA   H  N N 83  
CYS HB2  H  N N 84  
CYS HB3  H  N N 85  
CYS HG   H  N N 86  
CYS HXT  H  N N 87  
GLN N    N  N N 88  
GLN CA   C  N S 89  
GLN C    C  N N 90  
GLN O    O  N N 91  
GLN CB   C  N N 92  
GLN CG   C  N N 93  
GLN CD   C  N N 94  
GLN OE1  O  N N 95  
GLN NE2  N  N N 96  
GLN OXT  O  N N 97  
GLN H    H  N N 98  
GLN H2   H  N N 99  
GLN HA   H  N N 100 
GLN HB2  H  N N 101 
GLN HB3  H  N N 102 
GLN HG2  H  N N 103 
GLN HG3  H  N N 104 
GLN HE21 H  N N 105 
GLN HE22 H  N N 106 
GLN HXT  H  N N 107 
GLU N    N  N N 108 
GLU CA   C  N S 109 
GLU C    C  N N 110 
GLU O    O  N N 111 
GLU CB   C  N N 112 
GLU CG   C  N N 113 
GLU CD   C  N N 114 
GLU OE1  O  N N 115 
GLU OE2  O  N N 116 
GLU OXT  O  N N 117 
GLU H    H  N N 118 
GLU H2   H  N N 119 
GLU HA   H  N N 120 
GLU HB2  H  N N 121 
GLU HB3  H  N N 122 
GLU HG2  H  N N 123 
GLU HG3  H  N N 124 
GLU HE2  H  N N 125 
GLU HXT  H  N N 126 
GLY N    N  N N 127 
GLY CA   C  N N 128 
GLY C    C  N N 129 
GLY O    O  N N 130 
GLY OXT  O  N N 131 
GLY H    H  N N 132 
GLY H2   H  N N 133 
GLY HA2  H  N N 134 
GLY HA3  H  N N 135 
GLY HXT  H  N N 136 
GOL C1   C  N N 137 
GOL O1   O  N N 138 
GOL C2   C  N N 139 
GOL O2   O  N N 140 
GOL C3   C  N N 141 
GOL O3   O  N N 142 
GOL H11  H  N N 143 
GOL H12  H  N N 144 
GOL HO1  H  N N 145 
GOL H2   H  N N 146 
GOL HO2  H  N N 147 
GOL H31  H  N N 148 
GOL H32  H  N N 149 
GOL HO3  H  N N 150 
HIS N    N  N N 151 
HIS CA   C  N S 152 
HIS C    C  N N 153 
HIS O    O  N N 154 
HIS CB   C  N N 155 
HIS CG   C  Y N 156 
HIS ND1  N  Y N 157 
HIS CD2  C  Y N 158 
HIS CE1  C  Y N 159 
HIS NE2  N  Y N 160 
HIS OXT  O  N N 161 
HIS H    H  N N 162 
HIS H2   H  N N 163 
HIS HA   H  N N 164 
HIS HB2  H  N N 165 
HIS HB3  H  N N 166 
HIS HD1  H  N N 167 
HIS HD2  H  N N 168 
HIS HE1  H  N N 169 
HIS HE2  H  N N 170 
HIS HXT  H  N N 171 
HOH O    O  N N 172 
HOH H1   H  N N 173 
HOH H2   H  N N 174 
ILE N    N  N N 175 
ILE CA   C  N S 176 
ILE C    C  N N 177 
ILE O    O  N N 178 
ILE CB   C  N S 179 
ILE CG1  C  N N 180 
ILE CG2  C  N N 181 
ILE CD1  C  N N 182 
ILE OXT  O  N N 183 
ILE H    H  N N 184 
ILE H2   H  N N 185 
ILE HA   H  N N 186 
ILE HB   H  N N 187 
ILE HG12 H  N N 188 
ILE HG13 H  N N 189 
ILE HG21 H  N N 190 
ILE HG22 H  N N 191 
ILE HG23 H  N N 192 
ILE HD11 H  N N 193 
ILE HD12 H  N N 194 
ILE HD13 H  N N 195 
ILE HXT  H  N N 196 
KCR N    N  N N 197 
KCR CA   C  N S 198 
KCR CB   C  N N 199 
KCR CG   C  N N 200 
KCR CD   C  N N 201 
KCR CE   C  N N 202 
KCR NZ   N  N N 203 
KCR CH   C  N N 204 
KCR OH   O  N N 205 
KCR CX   C  N N 206 
KCR CY   C  N N 207 
KCR CH3  C  N N 208 
KCR C    C  N N 209 
KCR O    O  N N 210 
KCR OXT  O  N N 211 
KCR H    H  N N 212 
KCR H2   H  N N 213 
KCR HA   H  N N 214 
KCR H5   H  N N 215 
KCR H6   H  N N 216 
KCR H7   H  N N 217 
KCR H8   H  N N 218 
KCR H9   H  N N 219 
KCR H10  H  N N 220 
KCR H11  H  N N 221 
KCR H12  H  N N 222 
KCR H13  H  N N 223 
KCR H14  H  N N 224 
KCR H15  H  N N 225 
KCR H16  H  N N 226 
KCR H17  H  N N 227 
KCR H18  H  N N 228 
KCR HXT  H  N N 229 
LEU N    N  N N 230 
LEU CA   C  N S 231 
LEU C    C  N N 232 
LEU O    O  N N 233 
LEU CB   C  N N 234 
LEU CG   C  N N 235 
LEU CD1  C  N N 236 
LEU CD2  C  N N 237 
LEU OXT  O  N N 238 
LEU H    H  N N 239 
LEU H2   H  N N 240 
LEU HA   H  N N 241 
LEU HB2  H  N N 242 
LEU HB3  H  N N 243 
LEU HG   H  N N 244 
LEU HD11 H  N N 245 
LEU HD12 H  N N 246 
LEU HD13 H  N N 247 
LEU HD21 H  N N 248 
LEU HD22 H  N N 249 
LEU HD23 H  N N 250 
LEU HXT  H  N N 251 
LI  LI   LI N N 252 
LYS N    N  N N 253 
LYS CA   C  N S 254 
LYS C    C  N N 255 
LYS O    O  N N 256 
LYS CB   C  N N 257 
LYS CG   C  N N 258 
LYS CD   C  N N 259 
LYS CE   C  N N 260 
LYS NZ   N  N N 261 
LYS OXT  O  N N 262 
LYS H    H  N N 263 
LYS H2   H  N N 264 
LYS HA   H  N N 265 
LYS HB2  H  N N 266 
LYS HB3  H  N N 267 
LYS HG2  H  N N 268 
LYS HG3  H  N N 269 
LYS HD2  H  N N 270 
LYS HD3  H  N N 271 
LYS HE2  H  N N 272 
LYS HE3  H  N N 273 
LYS HZ1  H  N N 274 
LYS HZ2  H  N N 275 
LYS HZ3  H  N N 276 
LYS HXT  H  N N 277 
MET N    N  N N 278 
MET CA   C  N S 279 
MET C    C  N N 280 
MET O    O  N N 281 
MET CB   C  N N 282 
MET CG   C  N N 283 
MET SD   S  N N 284 
MET CE   C  N N 285 
MET OXT  O  N N 286 
MET H    H  N N 287 
MET H2   H  N N 288 
MET HA   H  N N 289 
MET HB2  H  N N 290 
MET HB3  H  N N 291 
MET HG2  H  N N 292 
MET HG3  H  N N 293 
MET HE1  H  N N 294 
MET HE2  H  N N 295 
MET HE3  H  N N 296 
MET HXT  H  N N 297 
NO3 N    N  N N 298 
NO3 O1   O  N N 299 
NO3 O2   O  N N 300 
NO3 O3   O  N N 301 
PEG C1   C  N N 302 
PEG O1   O  N N 303 
PEG C2   C  N N 304 
PEG O2   O  N N 305 
PEG C3   C  N N 306 
PEG C4   C  N N 307 
PEG O4   O  N N 308 
PEG H11  H  N N 309 
PEG H12  H  N N 310 
PEG HO1  H  N N 311 
PEG H21  H  N N 312 
PEG H22  H  N N 313 
PEG H31  H  N N 314 
PEG H32  H  N N 315 
PEG H41  H  N N 316 
PEG H42  H  N N 317 
PEG HO4  H  N N 318 
PHE N    N  N N 319 
PHE CA   C  N S 320 
PHE C    C  N N 321 
PHE O    O  N N 322 
PHE CB   C  N N 323 
PHE CG   C  Y N 324 
PHE CD1  C  Y N 325 
PHE CD2  C  Y N 326 
PHE CE1  C  Y N 327 
PHE CE2  C  Y N 328 
PHE CZ   C  Y N 329 
PHE OXT  O  N N 330 
PHE H    H  N N 331 
PHE H2   H  N N 332 
PHE HA   H  N N 333 
PHE HB2  H  N N 334 
PHE HB3  H  N N 335 
PHE HD1  H  N N 336 
PHE HD2  H  N N 337 
PHE HE1  H  N N 338 
PHE HE2  H  N N 339 
PHE HZ   H  N N 340 
PHE HXT  H  N N 341 
PRO N    N  N N 342 
PRO CA   C  N S 343 
PRO C    C  N N 344 
PRO O    O  N N 345 
PRO CB   C  N N 346 
PRO CG   C  N N 347 
PRO CD   C  N N 348 
PRO OXT  O  N N 349 
PRO H    H  N N 350 
PRO HA   H  N N 351 
PRO HB2  H  N N 352 
PRO HB3  H  N N 353 
PRO HG2  H  N N 354 
PRO HG3  H  N N 355 
PRO HD2  H  N N 356 
PRO HD3  H  N N 357 
PRO HXT  H  N N 358 
SER N    N  N N 359 
SER CA   C  N S 360 
SER C    C  N N 361 
SER O    O  N N 362 
SER CB   C  N N 363 
SER OG   O  N N 364 
SER OXT  O  N N 365 
SER H    H  N N 366 
SER H2   H  N N 367 
SER HA   H  N N 368 
SER HB2  H  N N 369 
SER HB3  H  N N 370 
SER HG   H  N N 371 
SER HXT  H  N N 372 
THR N    N  N N 373 
THR CA   C  N S 374 
THR C    C  N N 375 
THR O    O  N N 376 
THR CB   C  N R 377 
THR OG1  O  N N 378 
THR CG2  C  N N 379 
THR OXT  O  N N 380 
THR H    H  N N 381 
THR H2   H  N N 382 
THR HA   H  N N 383 
THR HB   H  N N 384 
THR HG1  H  N N 385 
THR HG21 H  N N 386 
THR HG22 H  N N 387 
THR HG23 H  N N 388 
THR HXT  H  N N 389 
TRP N    N  N N 390 
TRP CA   C  N S 391 
TRP C    C  N N 392 
TRP O    O  N N 393 
TRP CB   C  N N 394 
TRP CG   C  Y N 395 
TRP CD1  C  Y N 396 
TRP CD2  C  Y N 397 
TRP NE1  N  Y N 398 
TRP CE2  C  Y N 399 
TRP CE3  C  Y N 400 
TRP CZ2  C  Y N 401 
TRP CZ3  C  Y N 402 
TRP CH2  C  Y N 403 
TRP OXT  O  N N 404 
TRP H    H  N N 405 
TRP H2   H  N N 406 
TRP HA   H  N N 407 
TRP HB2  H  N N 408 
TRP HB3  H  N N 409 
TRP HD1  H  N N 410 
TRP HE1  H  N N 411 
TRP HE3  H  N N 412 
TRP HZ2  H  N N 413 
TRP HZ3  H  N N 414 
TRP HH2  H  N N 415 
TRP HXT  H  N N 416 
TYR N    N  N N 417 
TYR CA   C  N S 418 
TYR C    C  N N 419 
TYR O    O  N N 420 
TYR CB   C  N N 421 
TYR CG   C  Y N 422 
TYR CD1  C  Y N 423 
TYR CD2  C  Y N 424 
TYR CE1  C  Y N 425 
TYR CE2  C  Y N 426 
TYR CZ   C  Y N 427 
TYR OH   O  N N 428 
TYR OXT  O  N N 429 
TYR H    H  N N 430 
TYR H2   H  N N 431 
TYR HA   H  N N 432 
TYR HB2  H  N N 433 
TYR HB3  H  N N 434 
TYR HD1  H  N N 435 
TYR HD2  H  N N 436 
TYR HE1  H  N N 437 
TYR HE2  H  N N 438 
TYR HH   H  N N 439 
TYR HXT  H  N N 440 
VAL N    N  N N 441 
VAL CA   C  N S 442 
VAL C    C  N N 443 
VAL O    O  N N 444 
VAL CB   C  N N 445 
VAL CG1  C  N N 446 
VAL CG2  C  N N 447 
VAL OXT  O  N N 448 
VAL H    H  N N 449 
VAL H2   H  N N 450 
VAL HA   H  N N 451 
VAL HB   H  N N 452 
VAL HG11 H  N N 453 
VAL HG12 H  N N 454 
VAL HG13 H  N N 455 
VAL HG21 H  N N 456 
VAL HG22 H  N N 457 
VAL HG23 H  N N 458 
VAL HXT  H  N N 459 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
KCR CH3 CY   sing N N 186 
KCR CY  CX   doub N E 187 
KCR CX  CH   sing N N 188 
KCR OH  CH   doub N N 189 
KCR CH  NZ   sing N N 190 
KCR NZ  CE   sing N N 191 
KCR CE  CD   sing N N 192 
KCR CG  CD   sing N N 193 
KCR CG  CB   sing N N 194 
KCR CB  CA   sing N N 195 
KCR N   CA   sing N N 196 
KCR CA  C    sing N N 197 
KCR O   C    doub N N 198 
KCR C   OXT  sing N N 199 
KCR N   H    sing N N 200 
KCR N   H2   sing N N 201 
KCR CA  HA   sing N N 202 
KCR CB  H5   sing N N 203 
KCR CB  H6   sing N N 204 
KCR CG  H7   sing N N 205 
KCR CG  H8   sing N N 206 
KCR CD  H9   sing N N 207 
KCR CD  H10  sing N N 208 
KCR CE  H11  sing N N 209 
KCR CE  H12  sing N N 210 
KCR NZ  H13  sing N N 211 
KCR CX  H14  sing N N 212 
KCR CY  H15  sing N N 213 
KCR CH3 H16  sing N N 214 
KCR CH3 H17  sing N N 215 
KCR CH3 H18  sing N N 216 
KCR OXT HXT  sing N N 217 
LEU N   CA   sing N N 218 
LEU N   H    sing N N 219 
LEU N   H2   sing N N 220 
LEU CA  C    sing N N 221 
LEU CA  CB   sing N N 222 
LEU CA  HA   sing N N 223 
LEU C   O    doub N N 224 
LEU C   OXT  sing N N 225 
LEU CB  CG   sing N N 226 
LEU CB  HB2  sing N N 227 
LEU CB  HB3  sing N N 228 
LEU CG  CD1  sing N N 229 
LEU CG  CD2  sing N N 230 
LEU CG  HG   sing N N 231 
LEU CD1 HD11 sing N N 232 
LEU CD1 HD12 sing N N 233 
LEU CD1 HD13 sing N N 234 
LEU CD2 HD21 sing N N 235 
LEU CD2 HD22 sing N N 236 
LEU CD2 HD23 sing N N 237 
LEU OXT HXT  sing N N 238 
LYS N   CA   sing N N 239 
LYS N   H    sing N N 240 
LYS N   H2   sing N N 241 
LYS CA  C    sing N N 242 
LYS CA  CB   sing N N 243 
LYS CA  HA   sing N N 244 
LYS C   O    doub N N 245 
LYS C   OXT  sing N N 246 
LYS CB  CG   sing N N 247 
LYS CB  HB2  sing N N 248 
LYS CB  HB3  sing N N 249 
LYS CG  CD   sing N N 250 
LYS CG  HG2  sing N N 251 
LYS CG  HG3  sing N N 252 
LYS CD  CE   sing N N 253 
LYS CD  HD2  sing N N 254 
LYS CD  HD3  sing N N 255 
LYS CE  NZ   sing N N 256 
LYS CE  HE2  sing N N 257 
LYS CE  HE3  sing N N 258 
LYS NZ  HZ1  sing N N 259 
LYS NZ  HZ2  sing N N 260 
LYS NZ  HZ3  sing N N 261 
LYS OXT HXT  sing N N 262 
MET N   CA   sing N N 263 
MET N   H    sing N N 264 
MET N   H2   sing N N 265 
MET CA  C    sing N N 266 
MET CA  CB   sing N N 267 
MET CA  HA   sing N N 268 
MET C   O    doub N N 269 
MET C   OXT  sing N N 270 
MET CB  CG   sing N N 271 
MET CB  HB2  sing N N 272 
MET CB  HB3  sing N N 273 
MET CG  SD   sing N N 274 
MET CG  HG2  sing N N 275 
MET CG  HG3  sing N N 276 
MET SD  CE   sing N N 277 
MET CE  HE1  sing N N 278 
MET CE  HE2  sing N N 279 
MET CE  HE3  sing N N 280 
MET OXT HXT  sing N N 281 
NO3 N   O1   doub N N 282 
NO3 N   O2   sing N N 283 
NO3 N   O3   sing N N 284 
PEG C1  O1   sing N N 285 
PEG C1  C2   sing N N 286 
PEG C1  H11  sing N N 287 
PEG C1  H12  sing N N 288 
PEG O1  HO1  sing N N 289 
PEG C2  O2   sing N N 290 
PEG C2  H21  sing N N 291 
PEG C2  H22  sing N N 292 
PEG O2  C3   sing N N 293 
PEG C3  C4   sing N N 294 
PEG C3  H31  sing N N 295 
PEG C3  H32  sing N N 296 
PEG C4  O4   sing N N 297 
PEG C4  H41  sing N N 298 
PEG C4  H42  sing N N 299 
PEG O4  HO4  sing N N 300 
PHE N   CA   sing N N 301 
PHE N   H    sing N N 302 
PHE N   H2   sing N N 303 
PHE CA  C    sing N N 304 
PHE CA  CB   sing N N 305 
PHE CA  HA   sing N N 306 
PHE C   O    doub N N 307 
PHE C   OXT  sing N N 308 
PHE CB  CG   sing N N 309 
PHE CB  HB2  sing N N 310 
PHE CB  HB3  sing N N 311 
PHE CG  CD1  doub Y N 312 
PHE CG  CD2  sing Y N 313 
PHE CD1 CE1  sing Y N 314 
PHE CD1 HD1  sing N N 315 
PHE CD2 CE2  doub Y N 316 
PHE CD2 HD2  sing N N 317 
PHE CE1 CZ   doub Y N 318 
PHE CE1 HE1  sing N N 319 
PHE CE2 CZ   sing Y N 320 
PHE CE2 HE2  sing N N 321 
PHE CZ  HZ   sing N N 322 
PHE OXT HXT  sing N N 323 
PRO N   CA   sing N N 324 
PRO N   CD   sing N N 325 
PRO N   H    sing N N 326 
PRO CA  C    sing N N 327 
PRO CA  CB   sing N N 328 
PRO CA  HA   sing N N 329 
PRO C   O    doub N N 330 
PRO C   OXT  sing N N 331 
PRO CB  CG   sing N N 332 
PRO CB  HB2  sing N N 333 
PRO CB  HB3  sing N N 334 
PRO CG  CD   sing N N 335 
PRO CG  HG2  sing N N 336 
PRO CG  HG3  sing N N 337 
PRO CD  HD2  sing N N 338 
PRO CD  HD3  sing N N 339 
PRO OXT HXT  sing N N 340 
SER N   CA   sing N N 341 
SER N   H    sing N N 342 
SER N   H2   sing N N 343 
SER CA  C    sing N N 344 
SER CA  CB   sing N N 345 
SER CA  HA   sing N N 346 
SER C   O    doub N N 347 
SER C   OXT  sing N N 348 
SER CB  OG   sing N N 349 
SER CB  HB2  sing N N 350 
SER CB  HB3  sing N N 351 
SER OG  HG   sing N N 352 
SER OXT HXT  sing N N 353 
THR N   CA   sing N N 354 
THR N   H    sing N N 355 
THR N   H2   sing N N 356 
THR CA  C    sing N N 357 
THR CA  CB   sing N N 358 
THR CA  HA   sing N N 359 
THR C   O    doub N N 360 
THR C   OXT  sing N N 361 
THR CB  OG1  sing N N 362 
THR CB  CG2  sing N N 363 
THR CB  HB   sing N N 364 
THR OG1 HG1  sing N N 365 
THR CG2 HG21 sing N N 366 
THR CG2 HG22 sing N N 367 
THR CG2 HG23 sing N N 368 
THR OXT HXT  sing N N 369 
TRP N   CA   sing N N 370 
TRP N   H    sing N N 371 
TRP N   H2   sing N N 372 
TRP CA  C    sing N N 373 
TRP CA  CB   sing N N 374 
TRP CA  HA   sing N N 375 
TRP C   O    doub N N 376 
TRP C   OXT  sing N N 377 
TRP CB  CG   sing N N 378 
TRP CB  HB2  sing N N 379 
TRP CB  HB3  sing N N 380 
TRP CG  CD1  doub Y N 381 
TRP CG  CD2  sing Y N 382 
TRP CD1 NE1  sing Y N 383 
TRP CD1 HD1  sing N N 384 
TRP CD2 CE2  doub Y N 385 
TRP CD2 CE3  sing Y N 386 
TRP NE1 CE2  sing Y N 387 
TRP NE1 HE1  sing N N 388 
TRP CE2 CZ2  sing Y N 389 
TRP CE3 CZ3  doub Y N 390 
TRP CE3 HE3  sing N N 391 
TRP CZ2 CH2  doub Y N 392 
TRP CZ2 HZ2  sing N N 393 
TRP CZ3 CH2  sing Y N 394 
TRP CZ3 HZ3  sing N N 395 
TRP CH2 HH2  sing N N 396 
TRP OXT HXT  sing N N 397 
TYR N   CA   sing N N 398 
TYR N   H    sing N N 399 
TYR N   H2   sing N N 400 
TYR CA  C    sing N N 401 
TYR CA  CB   sing N N 402 
TYR CA  HA   sing N N 403 
TYR C   O    doub N N 404 
TYR C   OXT  sing N N 405 
TYR CB  CG   sing N N 406 
TYR CB  HB2  sing N N 407 
TYR CB  HB3  sing N N 408 
TYR CG  CD1  doub Y N 409 
TYR CG  CD2  sing Y N 410 
TYR CD1 CE1  sing Y N 411 
TYR CD1 HD1  sing N N 412 
TYR CD2 CE2  doub Y N 413 
TYR CD2 HD2  sing N N 414 
TYR CE1 CZ   doub Y N 415 
TYR CE1 HE1  sing N N 416 
TYR CE2 CZ   sing Y N 417 
TYR CE2 HE2  sing N N 418 
TYR CZ  OH   sing N N 419 
TYR OH  HH   sing N N 420 
TYR OXT HXT  sing N N 421 
VAL N   CA   sing N N 422 
VAL N   H    sing N N 423 
VAL N   H2   sing N N 424 
VAL CA  C    sing N N 425 
VAL CA  CB   sing N N 426 
VAL CA  HA   sing N N 427 
VAL C   O    doub N N 428 
VAL C   OXT  sing N N 429 
VAL CB  CG1  sing N N 430 
VAL CB  CG2  sing N N 431 
VAL CB  HB   sing N N 432 
VAL CG1 HG11 sing N N 433 
VAL CG1 HG12 sing N N 434 
VAL CG1 HG13 sing N N 435 
VAL CG2 HG21 sing N N 436 
VAL CG2 HG22 sing N N 437 
VAL CG2 HG23 sing N N 438 
VAL OXT HXT  sing N N 439 
# 
_pdbx_audit_support.funding_organization   'National Institutes of Health/National Heart, Lung, and Blood Institute (NIH/NHLBI)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           HL151334 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   6MIL 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9ARR 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.006975 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.003054 
_atom_sites.fract_transf_matrix[2][1]   -0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.020399 
_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]   0.013972 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
LI 
N  
O  
S  
# 
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   . MET A 1 1   ? -4.515  20.607 30.126  1.00 65.28  ? 1   MET A N   1 
ATOM   2    C  CA  . MET A 1 1   ? -4.662  19.180 29.748  1.00 51.12  ? 1   MET A CA  1 
ATOM   3    C  C   . MET A 1 1   ? -5.588  19.051 28.520  1.00 42.31  ? 1   MET A C   1 
ATOM   4    O  O   . MET A 1 1   ? -5.327  18.205 27.689  1.00 40.22  ? 1   MET A O   1 
ATOM   5    C  CB  . MET A 1 1   ? -5.183  18.349 30.928  1.00 52.47  ? 1   MET A CB  1 
ATOM   6    C  CG  . MET A 1 1   ? -5.078  16.856 30.777  1.00 46.98  ? 1   MET A CG  1 
ATOM   7    S  SD  . MET A 1 1   ? -3.542  16.196 31.503  1.00 73.74  ? 1   MET A SD  1 
ATOM   8    C  CE  . MET A 1 1   ? -4.180  14.947 32.628  1.00 58.51  ? 1   MET A CE  1 
ATOM   9    N  N   . ALA A 1 2   ? -6.685  19.804 28.358  1.00 45.85  ? 2   ALA A N   1 
ATOM   10   C  CA  . ALA A 1 2   ? -7.527  19.603 27.171  1.00 49.29  ? 2   ALA A CA  1 
ATOM   11   C  C   . ALA A 1 2   ? -6.789  20.049 25.895  1.00 53.08  ? 2   ALA A C   1 
ATOM   12   O  O   . ALA A 1 2   ? -6.861  19.425 24.821  1.00 42.40  ? 2   ALA A O   1 
ATOM   13   C  CB  . ALA A 1 2   ? -8.846  20.339 27.266  1.00 46.73  ? 2   ALA A CB  1 
ATOM   14   N  N   . SER A 1 3   ? -6.069  21.155 26.027  1.00 40.42  ? 3   SER A N   1 
ATOM   15   C  CA  . SER A 1 3   ? -5.438  21.797 24.893  1.00 48.60  ? 3   SER A CA  1 
ATOM   16   C  C   . SER A 1 3   ? -4.010  21.305 24.696  1.00 46.97  ? 3   SER A C   1 
ATOM   17   O  O   . SER A 1 3   ? -3.351  20.875 25.636  1.00 47.50  ? 3   SER A O   1 
ATOM   18   C  CB  . SER A 1 3   ? -5.449  23.273 25.059  1.00 45.32  ? 3   SER A CB  1 
ATOM   19   O  OG  . SER A 1 3   ? -4.549  23.622 26.066  1.00 43.59  ? 3   SER A OG  1 
ATOM   20   N  N   . SER A 1 4   ? -3.554  21.394 23.450  1.00 47.94  ? 4   SER A N   1 
ATOM   21   C  CA  . SER A 1 4   ? -2.160  21.190 23.095  1.00 45.77  ? 4   SER A CA  1 
ATOM   22   C  C   . SER A 1 4   ? -1.861  22.064 21.876  1.00 49.71  ? 4   SER A C   1 
ATOM   23   O  O   . SER A 1 4   ? -2.776  22.518 21.181  1.00 42.23  ? 4   SER A O   1 
ATOM   24   C  CB  . SER A 1 4   ? -1.936  19.740 22.782  1.00 41.89  ? 4   SER A CB  1 
ATOM   25   O  OG  . SER A 1 4   ? -2.674  19.448 21.602  1.00 49.09  ? 4   SER A OG  1 
ATOM   26   N  N   . CYS A 1 5   ? -0.584  22.283 21.573  1.00 51.69  ? 5   CYS A N   1 
ATOM   27   C  CA  . CYS A 1 5   ? -0.258  23.006 20.361  1.00 55.00  ? 5   CYS A CA  1 
ATOM   28   C  C   . CYS A 1 5   ? 1.072   22.563 19.768  1.00 52.13  ? 5   CYS A C   1 
ATOM   29   O  O   . CYS A 1 5   ? 1.929   21.982 20.415  1.00 55.70  ? 5   CYS A O   1 
ATOM   30   C  CB  . CYS A 1 5   ? -0.272  24.512 20.571  1.00 64.62  ? 5   CYS A CB  1 
ATOM   31   S  SG  . CYS A 1 5   ? 1.113   25.085 21.560  1.00 63.72  ? 5   CYS A SG  1 
ATOM   32   N  N   . ALA A 1 6   ? 1.162   22.819 18.475  1.00 56.85  ? 6   ALA A N   1 
ATOM   33   C  CA  . ALA A 1 6   ? 2.346   22.600 17.664  1.00 50.97  ? 6   ALA A CA  1 
ATOM   34   C  C   . ALA A 1 6   ? 2.708   23.958 17.089  1.00 53.00  ? 6   ALA A C   1 
ATOM   35   O  O   . ALA A 1 6   ? 1.851   24.633 16.497  1.00 48.05  ? 6   ALA A O   1 
ATOM   36   C  CB  . ALA A 1 6   ? 2.084   21.550 16.585  1.00 49.38  ? 6   ALA A CB  1 
ATOM   37   N  N   . VAL A 1 7   ? 3.952   24.397 17.343  1.00 53.46  ? 7   VAL A N   1 
ATOM   38   C  CA  . VAL A 1 7   ? 4.456   25.599 16.705  1.00 50.28  ? 7   VAL A CA  1 
ATOM   39   C  C   . VAL A 1 7   ? 5.488   25.188 15.663  1.00 50.59  ? 7   VAL A C   1 
ATOM   40   O  O   . VAL A 1 7   ? 6.371   24.376 15.930  1.00 52.17  ? 7   VAL A O   1 
ATOM   41   C  CB  . VAL A 1 7   ? 5.004   26.617 17.706  1.00 53.51  ? 7   VAL A CB  1 
ATOM   42   C  CG1 . VAL A 1 7   ? 5.559   27.832 16.997  1.00 54.55  ? 7   VAL A CG1 1 
ATOM   43   C  CG2 . VAL A 1 7   ? 3.931   27.028 18.701  1.00 57.76  ? 7   VAL A CG2 1 
ATOM   44   N  N   . GLN A 1 8   ? 5.299   25.713 14.453  1.00 49.14  ? 8   GLN A N   1 
ATOM   45   C  CA  . GLN A 1 8   ? 6.233   25.541 13.354  1.00 55.29  ? 8   GLN A CA  1 
ATOM   46   C  C   . GLN A 1 8   ? 6.954   26.850 13.035  1.00 57.36  ? 8   GLN A C   1 
ATOM   47   O  O   . GLN A 1 8   ? 6.322   27.933 12.990  1.00 42.30  ? 8   GLN A O   1 
ATOM   48   C  CB  . GLN A 1 8   ? 5.466   25.133 12.104  1.00 58.91  ? 8   GLN A CB  1 
ATOM   49   C  CG  . GLN A 1 8   ? 6.362   24.588 11.026  1.00 79.56  ? 8   GLN A CG  1 
ATOM   50   C  CD  . GLN A 1 8   ? 5.543   23.631 10.203  1.00 90.17  ? 8   GLN A CD  1 
ATOM   51   O  OE1 . GLN A 1 8   ? 4.872   22.754 10.752  1.00 88.58  ? 8   GLN A OE1 1 
ATOM   52   N  NE2 . GLN A 1 8   ? 5.571   23.827 8.894   1.00 80.56  ? 8   GLN A NE2 1 
ATOM   53   N  N   . VAL A 1 9   ? 8.276   26.735 12.786  1.00 47.11  ? 9   VAL A N   1 
ATOM   54   C  CA  . VAL A 1 9   ? 9.014   27.863 12.240  1.00 50.42  ? 9   VAL A CA  1 
ATOM   55   C  C   . VAL A 1 9   ? 9.846   27.422 11.040  1.00 43.88  ? 9   VAL A C   1 
ATOM   56   O  O   . VAL A 1 9   ? 10.253  26.264 10.875  1.00 39.09  ? 9   VAL A O   1 
ATOM   57   C  CB  . VAL A 1 9   ? 9.881   28.583 13.287  1.00 54.10  ? 9   VAL A CB  1 
ATOM   58   C  CG1 . VAL A 1 9   ? 9.069   29.538 14.141  1.00 60.79  ? 9   VAL A CG1 1 
ATOM   59   C  CG2 . VAL A 1 9   ? 10.629  27.602 14.147  1.00 52.47  ? 9   VAL A CG2 1 
ATOM   60   N  N   . LYS A 1 10  ? 10.011  28.401 10.178  1.00 46.89  ? 10  LYS A N   1 
ATOM   61   C  CA  . LYS A 1 10  ? 10.686  28.221 8.916   1.00 62.70  ? 10  LYS A CA  1 
ATOM   62   C  C   . LYS A 1 10  ? 12.057  28.866 9.042   1.00 55.51  ? 10  LYS A C   1 
ATOM   63   O  O   . LYS A 1 10  ? 12.179  29.980 9.553   1.00 52.10  ? 10  LYS A O   1 
ATOM   64   C  CB  . LYS A 1 10  ? 9.862   28.848 7.789   1.00 73.03  ? 10  LYS A CB  1 
ATOM   65   C  CG  . LYS A 1 10  ? 8.567   28.119 7.459   1.00 87.65  ? 10  LYS A CG  1 
ATOM   66   C  CD  . LYS A 1 10  ? 7.772   28.738 6.318   1.00 91.14  ? 10  LYS A CD  1 
ATOM   67   C  CE  . LYS A 1 10  ? 6.685   27.802 5.834   1.00 103.24 ? 10  LYS A CE  1 
ATOM   68   N  NZ  . LYS A 1 10  ? 5.826   28.457 4.827   1.00 110.90 ? 10  LYS A NZ  1 
ATOM   69   N  N   . LEU A 1 11  ? 13.066  28.124 8.596   1.00 46.70  ? 11  LEU A N   1 
ATOM   70   C  CA  . LEU A 1 11  ? 14.408  28.649 8.440   1.00 48.31  ? 11  LEU A CA  1 
ATOM   71   C  C   . LEU A 1 11  ? 14.855  28.482 6.996   1.00 50.51  ? 11  LEU A C   1 
ATOM   72   O  O   . LEU A 1 11  ? 14.490  27.513 6.326   1.00 41.63  ? 11  LEU A O   1 
ATOM   73   C  CB  . LEU A 1 11  ? 15.385  27.873 9.324   1.00 44.03  ? 11  LEU A CB  1 
ATOM   74   C  CG  . LEU A 1 11  ? 15.277  28.133 10.822  1.00 49.75  ? 11  LEU A CG  1 
ATOM   75   C  CD1 . LEU A 1 11  ? 16.309  27.299 11.551  1.00 50.22  ? 11  LEU A CD1 1 
ATOM   76   C  CD2 . LEU A 1 11  ? 15.417  29.625 11.136  1.00 50.98  ? 11  LEU A CD2 1 
ATOM   77   N  N   . GLU A 1 12  ? 15.731  29.394 6.582   1.00 43.57  ? 12  GLU A N   1 
ATOM   78   C  CA  . GLU A 1 12  ? 16.399  29.271 5.299   1.00 45.17  ? 12  GLU A CA  1 
ATOM   79   C  C   . GLU A 1 12  ? 17.879  29.229 5.578   1.00 39.66  ? 12  GLU A C   1 
ATOM   80   O  O   . GLU A 1 12  ? 18.400  30.103 6.281   1.00 38.60  ? 12  GLU A O   1 
ATOM   81   C  CB  . GLU A 1 12  ? 16.092  30.470 4.413   1.00 47.35  ? 12  GLU A CB  1 
ATOM   82   C  CG  . GLU A 1 12  ? 14.703  30.424 3.834   1.00 50.58  ? 12  GLU A CG  1 
ATOM   83   C  CD  . GLU A 1 12  ? 14.320  31.680 3.072   1.00 67.93  ? 12  GLU A CD  1 
ATOM   84   O  OE1 . GLU A 1 12  ? 15.181  32.592 2.991   1.00 58.49  ? 12  GLU A OE1 1 
ATOM   85   O  OE2 . GLU A 1 12  ? 13.148  31.769 2.611   1.00 68.62  ? 12  GLU A OE2 1 
ATOM   86   N  N   . LEU A 1 13  ? 18.476  28.143 5.113   1.00 31.65  ? 13  LEU A N   1 
ATOM   87   C  CA  . LEU A 1 13  ? 19.902  27.986 5.057   1.00 32.69  ? 13  LEU A CA  1 
ATOM   88   C  C   . LEU A 1 13  ? 20.313  28.190 3.616   1.00 37.78  ? 13  LEU A C   1 
ATOM   89   O  O   . LEU A 1 13  ? 19.543  27.856 2.715   1.00 41.95  ? 13  LEU A O   1 
ATOM   90   C  CB  . LEU A 1 13  ? 20.269  26.563 5.464   1.00 40.40  ? 13  LEU A CB  1 
ATOM   91   C  CG  . LEU A 1 13  ? 20.283  26.226 6.948   1.00 41.30  ? 13  LEU A CG  1 
ATOM   92   C  CD1 . LEU A 1 13  ? 19.014  26.643 7.652   1.00 48.26  ? 13  LEU A CD1 1 
ATOM   93   C  CD2 . LEU A 1 13  ? 20.503  24.750 7.087   1.00 45.17  ? 13  LEU A CD2 1 
ATOM   94   N  N   . GLY A 1 14  ? 21.536  28.685 3.408   1.00 36.52  ? 14  GLY A N   1 
ATOM   95   C  CA  . GLY A 1 14  ? 21.986  28.866 2.049   1.00 36.28  ? 14  GLY A CA  1 
ATOM   96   C  C   . GLY A 1 14  ? 23.422  29.319 1.944   1.00 33.22  ? 14  GLY A C   1 
ATOM   97   O  O   . GLY A 1 14  ? 24.079  29.544 2.959   1.00 35.64  ? 14  GLY A O   1 
ATOM   98   N  N   . HIS A 1 15  ? 23.878  29.452 0.691   1.00 33.29  ? 15  HIS A N   1 
ATOM   99   C  CA  . HIS A 1 15  ? 25.225  29.906 0.458   1.00 32.23  ? 15  HIS A CA  1 
ATOM   100  C  C   . HIS A 1 15  ? 25.356  30.408 -0.949  1.00 29.68  ? 15  HIS A C   1 
ATOM   101  O  O   . HIS A 1 15  ? 24.593  30.011 -1.813  1.00 30.18  ? 15  HIS A O   1 
ATOM   102  C  CB  . HIS A 1 15  ? 26.288  28.852 0.789   1.00 35.28  ? 15  HIS A CB  1 
ATOM   103  C  CG  . HIS A 1 15  ? 26.568  27.860 -0.290  1.00 35.77  ? 15  HIS A CG  1 
ATOM   104  N  ND1 . HIS A 1 15  ? 25.653  26.926 -0.698  1.00 33.99  ? 15  HIS A ND1 1 
ATOM   105  C  CD2 . HIS A 1 15  ? 27.669  27.653 -1.026  1.00 34.27  ? 15  HIS A CD2 1 
ATOM   106  C  CE1 . HIS A 1 15  ? 26.216  26.143 -1.606  1.00 38.85  ? 15  HIS A CE1 1 
ATOM   107  N  NE2 . HIS A 1 15  ? 27.445  26.585 -1.843  1.00 33.20  ? 15  HIS A NE2 1 
ATOM   108  N  N   . ARG A 1 16  ? 26.331  31.311 -1.095  1.00 29.46  ? 16  ARG A N   1 
ATOM   109  C  CA  . ARG A 1 16  ? 26.753  31.855 -2.362  1.00 32.86  ? 16  ARG A CA  1 
ATOM   110  C  C   . ARG A 1 16  ? 28.214  31.494 -2.500  1.00 29.57  ? 16  ARG A C   1 
ATOM   111  O  O   . ARG A 1 16  ? 28.959  31.430 -1.522  1.00 29.47  ? 16  ARG A O   1 
ATOM   112  C  CB  . ARG A 1 16  ? 26.581  33.378 -2.439  1.00 38.36  ? 16  ARG A CB  1 
ATOM   113  C  CG  . ARG A 1 16  ? 25.138  33.847 -2.500  1.00 42.26  ? 16  ARG A CG  1 
ATOM   114  C  CD  . ARG A 1 16  ? 25.049  35.333 -2.672  1.00 52.71  ? 16  ARG A CD  1 
ATOM   115  N  NE  . ARG A 1 16  ? 23.755  35.710 -3.212  1.00 82.39  ? 16  ARG A NE  1 
ATOM   116  C  CZ  . ARG A 1 16  ? 22.584  35.625 -2.563  1.00 103.93 ? 16  ARG A CZ  1 
ATOM   117  N  NH1 . ARG A 1 16  ? 22.520  35.220 -1.300  1.00 101.38 ? 16  ARG A NH1 1 
ATOM   118  N  NH2 . ARG A 1 16  ? 21.465  35.969 -3.184  1.00 94.61  ? 16  ARG A NH2 1 
ATOM   119  N  N   . ALA A 1 17  ? 28.635  31.218 -3.721  1.00 29.53  ? 17  ALA A N   1 
ATOM   120  C  CA  . ALA A 1 17  ? 30.036  30.899 -3.926  1.00 31.95  ? 17  ALA A CA  1 
ATOM   121  C  C   . ALA A 1 17  ? 30.433  31.327 -5.314  1.00 30.77  ? 17  ALA A C   1 
ATOM   122  O  O   . ALA A 1 17  ? 29.735  31.038 -6.279  1.00 32.70  ? 17  ALA A O   1 
ATOM   123  C  CB  . ALA A 1 17  ? 30.318  29.432 -3.775  1.00 31.47  ? 17  ALA A CB  1 
ATOM   124  N  N   . GLN A 1 18  ? 31.551  32.029 -5.373  1.00 31.15  ? 18  GLN A N   1 
ATOM   125  C  CA  . GLN A 1 18  ? 31.969  32.664 -6.596  1.00 36.57  ? 18  GLN A CA  1 
ATOM   126  C  C   . GLN A 1 18  ? 33.461  32.455 -6.770  1.00 34.73  ? 18  GLN A C   1 
ATOM   127  O  O   . GLN A 1 18  ? 34.259  32.689 -5.860  1.00 35.54  ? 18  GLN A O   1 
ATOM   128  C  CB  . GLN A 1 18  ? 31.632  34.148 -6.548  1.00 50.50  ? 18  GLN A CB  1 
ATOM   129  C  CG  . GLN A 1 18  ? 31.903  34.832 -7.868  1.00 65.59  ? 18  GLN A CG  1 
ATOM   130  C  CD  . GLN A 1 18  ? 31.389  36.234 -7.744  1.00 75.41  ? 18  GLN A CD  1 
ATOM   131  O  OE1 . GLN A 1 18  ? 32.109  37.125 -7.312  1.00 95.83  ? 18  GLN A OE1 1 
ATOM   132  N  NE2 . GLN A 1 18  ? 30.107  36.404 -8.004  1.00 74.45  ? 18  GLN A NE2 1 
ATOM   133  N  N   . VAL A 1 19  ? 33.805  32.006 -7.975  1.00 39.51  ? 19  VAL A N   1 
ATOM   134  C  CA  . VAL A 1 19  ? 35.178  31.900 -8.372  1.00 42.31  ? 19  VAL A CA  1 
ATOM   135  C  C   . VAL A 1 19  ? 35.717  33.317 -8.422  1.00 36.87  ? 19  VAL A C   1 
ATOM   136  O  O   . VAL A 1 19  ? 35.136  34.157 -9.073  1.00 42.52  ? 19  VAL A O   1 
ATOM   137  C  CB  . VAL A 1 19  ? 35.317  31.190 -9.725  1.00 45.72  ? 19  VAL A CB  1 
ATOM   138  C  CG1 . VAL A 1 19  ? 36.743  31.278 -10.218 1.00 45.76  ? 19  VAL A CG1 1 
ATOM   139  C  CG2 . VAL A 1 19  ? 34.893  29.734 -9.605  1.00 49.40  ? 19  VAL A CG2 1 
ATOM   140  N  N   . ARG A 1 20  ? 36.788  33.562 -7.688  1.00 33.58  ? 20  ARG A N   1 
ATOM   141  C  CA  . ARG A 1 20  ? 37.414  34.879 -7.678  1.00 41.30  ? 20  ARG A CA  1 
ATOM   142  C  C   . ARG A 1 20  ? 38.147  35.145 -8.997  1.00 47.54  ? 20  ARG A C   1 
ATOM   143  O  O   . ARG A 1 20  ? 38.714  34.230 -9.592  1.00 44.72  ? 20  ARG A O   1 
ATOM   144  C  CB  . ARG A 1 20  ? 38.509  34.940 -6.627  1.00 36.18  ? 20  ARG A CB  1 
ATOM   145  C  CG  . ARG A 1 20  ? 38.040  34.823 -5.194  1.00 38.80  ? 20  ARG A CG  1 
ATOM   146  C  CD  . ARG A 1 20  ? 39.275  34.417 -4.433  1.00 48.43  ? 20  ARG A CD  1 
ATOM   147  N  NE  . ARG A 1 20  ? 40.231  35.530 -4.424  1.00 50.87  ? 20  ARG A NE  1 
ATOM   148  C  CZ  . ARG A 1 20  ? 40.162  36.563 -3.588  1.00 49.50  ? 20  ARG A CZ  1 
ATOM   149  N  NH1 . ARG A 1 20  ? 39.336  36.536 -2.554  1.00 45.42  ? 20  ARG A NH1 1 
ATOM   150  N  NH2 . ARG A 1 20  ? 40.988  37.578 -3.725  1.00 46.71  ? 20  ARG A NH2 1 
ATOM   151  N  N   . LYS A 1 21  ? 38.194  36.425 -9.380  1.00 52.94  ? 21  LYS A N   1 
ATOM   152  C  CA  . LYS A 1 21  ? 38.910  36.910 -10.554 1.00 58.20  ? 21  LYS A CA  1 
ATOM   153  C  C   . LYS A 1 21  ? 40.341  36.401 -10.496 1.00 48.46  ? 21  LYS A C   1 
ATOM   154  O  O   . LYS A 1 21  ? 40.884  36.009 -11.501 1.00 49.47  ? 21  LYS A O   1 
ATOM   155  C  CB  . LYS A 1 21  ? 38.887  38.448 -10.630 1.00 66.90  ? 21  LYS A CB  1 
ATOM   156  C  CG  . LYS A 1 21  ? 37.519  39.096 -10.856 1.00 81.45  ? 21  LYS A CG  1 
ATOM   157  C  CD  . LYS A 1 21  ? 37.561  40.621 -11.090 1.00 92.17  ? 21  LYS A CD  1 
ATOM   158  C  CE  . LYS A 1 21  ? 38.043  41.432 -9.899  1.00 107.69 ? 21  LYS A CE  1 
ATOM   159  N  NZ  . LYS A 1 21  ? 37.033  41.471 -8.809  1.00 117.94 ? 21  LYS A NZ  1 
ATOM   160  N  N   . LYS A 1 22  ? 40.913  36.340 -9.300  1.00 51.35  ? 22  LYS A N   1 
ATOM   161  C  CA  . LYS A 1 22  ? 42.291  35.981 -9.116  1.00 51.90  ? 22  LYS A CA  1 
ATOM   162  C  C   . LYS A 1 22  ? 42.430  35.242 -7.792  1.00 49.25  ? 22  LYS A C   1 
ATOM   163  O  O   . LYS A 1 22  ? 41.991  35.729 -6.767  1.00 47.17  ? 22  LYS A O   1 
ATOM   164  C  CB  . LYS A 1 22  ? 43.064  37.304 -9.065  1.00 63.70  ? 22  LYS A CB  1 
ATOM   165  C  CG  . LYS A 1 22  ? 44.569  37.199 -9.180  1.00 75.80  ? 22  LYS A CG  1 
ATOM   166  C  CD  . LYS A 1 22  ? 45.016  36.891 -10.601 1.00 94.12  ? 22  LYS A CD  1 
ATOM   167  C  CE  . LYS A 1 22  ? 46.378  37.467 -10.934 1.00 98.79  ? 22  LYS A CE  1 
ATOM   168  N  NZ  . LYS A 1 22  ? 46.296  38.888 -11.349 1.00 92.96  ? 22  LYS A NZ  1 
ATOM   169  N  N   . PRO A 1 23  ? 43.059  34.052 -7.747  1.00 50.14  ? 23  PRO A N   1 
ATOM   170  C  CA  . PRO A 1 23  ? 43.261  33.358 -6.482  1.00 46.32  ? 23  PRO A CA  1 
ATOM   171  C  C   . PRO A 1 23  ? 43.982  34.228 -5.462  1.00 55.98  ? 23  PRO A C   1 
ATOM   172  O  O   . PRO A 1 23  ? 44.781  35.080 -5.814  1.00 53.37  ? 23  PRO A O   1 
ATOM   173  C  CB  . PRO A 1 23  ? 44.132  32.134 -6.798  1.00 48.23  ? 23  PRO A CB  1 
ATOM   174  C  CG  . PRO A 1 23  ? 44.026  31.974 -8.323  1.00 55.72  ? 23  PRO A CG  1 
ATOM   175  C  CD  . PRO A 1 23  ? 43.552  33.294 -8.909  1.00 49.95  ? 23  PRO A CD  1 
ATOM   176  N  N   . THR A 1 24  ? 43.692  34.004 -4.184  1.00 59.21  ? 24  THR A N   1 
ATOM   177  C  CA  . THR A 1 24  ? 44.451  34.662 -3.147  1.00 57.37  ? 24  THR A CA  1 
ATOM   178  C  C   . THR A 1 24  ? 45.824  34.000 -3.061  1.00 57.38  ? 24  THR A C   1 
ATOM   179  O  O   . THR A 1 24  ? 46.112  32.993 -3.730  1.00 46.04  ? 24  THR A O   1 
ATOM   180  C  CB  . THR A 1 24  ? 43.745  34.572 -1.793  1.00 47.65  ? 24  THR A CB  1 
ATOM   181  O  OG1 . THR A 1 24  ? 43.869  33.218 -1.399  1.00 43.83  ? 24  THR A OG1 1 
ATOM   182  C  CG2 . THR A 1 24  ? 42.298  34.967 -1.825  1.00 56.74  ? 24  THR A CG2 1 
ATOM   183  N  N   . VAL A 1 25  ? 46.606  34.549 -2.132  1.00 60.62  ? 25  VAL A N   1 
ATOM   184  C  CA  . VAL A 1 25  ? 48.004  34.213 -1.972  1.00 59.01  ? 25  VAL A CA  1 
ATOM   185  C  C   . VAL A 1 25  ? 48.083  32.767 -1.543  1.00 60.98  ? 25  VAL A C   1 
ATOM   186  O  O   . VAL A 1 25  ? 48.988  32.067 -1.948  1.00 53.49  ? 25  VAL A O   1 
ATOM   187  C  CB  . VAL A 1 25  ? 48.711  35.069 -0.904  1.00 74.22  ? 25  VAL A CB  1 
ATOM   188  C  CG1 . VAL A 1 25  ? 50.219  34.963 -1.065  1.00 67.42  ? 25  VAL A CG1 1 
ATOM   189  C  CG2 . VAL A 1 25  ? 48.264  36.530 -0.886  1.00 74.60  ? 25  VAL A CG2 1 
ATOM   190  N  N   . GLU A 1 26  ? 47.146  32.332 -0.701  1.00 61.09  ? 26  GLU A N   1 
ATOM   191  C  CA  . GLU A 1 26  ? 47.192  30.968 -0.206  1.00 60.61  ? 26  GLU A CA  1 
ATOM   192  C  C   . GLU A 1 26  ? 46.708  30.018 -1.298  1.00 55.53  ? 26  GLU A C   1 
ATOM   193  O  O   . GLU A 1 26  ? 46.696  28.817 -1.077  1.00 59.22  ? 26  GLU A O   1 
ATOM   194  C  CB  . GLU A 1 26  ? 46.373  30.822 1.073   1.00 62.26  ? 26  GLU A CB  1 
ATOM   195  C  CG  . GLU A 1 26  ? 46.578  31.953 2.065   1.00 61.80  ? 26  GLU A CG  1 
ATOM   196  C  CD  . GLU A 1 26  ? 45.710  33.182 1.852   1.00 71.02  ? 26  GLU A CD  1 
ATOM   197  O  OE1 . GLU A 1 26  ? 45.209  33.396 0.720   1.00 75.71  ? 26  GLU A OE1 1 
ATOM   198  O  OE2 . GLU A 1 26  ? 45.507  33.912 2.836   1.00 78.40  ? 26  GLU A OE2 1 
ATOM   199  N  N   . GLY A 1 27  ? 46.299  30.568 -2.455  1.00 43.71  ? 27  GLY A N   1 
ATOM   200  C  CA  . GLY A 1 27  ? 45.675  29.776 -3.501  1.00 47.58  ? 27  GLY A CA  1 
ATOM   201  C  C   . GLY A 1 27  ? 44.168  29.562 -3.305  1.00 53.13  ? 27  GLY A C   1 
ATOM   202  O  O   . GLY A 1 27  ? 43.621  28.619 -3.848  1.00 50.89  ? 27  GLY A O   1 
ATOM   203  N  N   . PHE A 1 28  ? 43.476  30.415 -2.524  1.00 43.58  ? 28  PHE A N   1 
ATOM   204  C  CA  . PHE A 1 28  ? 42.032  30.294 -2.416  1.00 39.82  ? 28  PHE A CA  1 
ATOM   205  C  C   . PHE A 1 28  ? 41.383  30.815 -3.689  1.00 46.79  ? 28  PHE A C   1 
ATOM   206  O  O   . PHE A 1 28  ? 41.581  31.979 -4.016  1.00 42.90  ? 28  PHE A O   1 
ATOM   207  C  CB  . PHE A 1 28  ? 41.493  31.045 -1.201  1.00 31.50  ? 28  PHE A CB  1 
ATOM   208  C  CG  . PHE A 1 28  ? 42.086  30.608 0.104   1.00 35.29  ? 28  PHE A CG  1 
ATOM   209  C  CD1 . PHE A 1 28  ? 42.599  29.323 0.254   1.00 38.01  ? 28  PHE A CD1 1 
ATOM   210  C  CD2 . PHE A 1 28  ? 42.185  31.512 1.161   1.00 40.66  ? 28  PHE A CD2 1 
ATOM   211  C  CE1 . PHE A 1 28  ? 43.151  28.931 1.458   1.00 42.37  ? 28  PHE A CE1 1 
ATOM   212  C  CE2 . PHE A 1 28  ? 42.754  31.123 2.368   1.00 36.12  ? 28  PHE A CE2 1 
ATOM   213  C  CZ  . PHE A 1 28  ? 43.215  29.828 2.516   1.00 47.59  ? 28  PHE A CZ  1 
ATOM   214  N  N   . THR A 1 29  ? 40.516  29.987 -4.301  1.00 35.77  ? 29  THR A N   1 
ATOM   215  C  CA  . THR A 1 29  ? 39.986  30.233 -5.634  1.00 30.54  ? 29  THR A CA  1 
ATOM   216  C  C   . THR A 1 29  ? 38.601  30.829 -5.564  1.00 29.42  ? 29  THR A C   1 
ATOM   217  O  O   . THR A 1 29  ? 38.114  31.353 -6.543  1.00 33.29  ? 29  THR A O   1 
ATOM   218  C  CB  . THR A 1 29  ? 39.864  28.915 -6.422  1.00 42.55  ? 29  THR A CB  1 
ATOM   219  O  OG1 . THR A 1 29  ? 39.161  27.965 -5.598  1.00 39.56  ? 29  THR A OG1 1 
ATOM   220  C  CG2 . THR A 1 29  ? 41.220  28.353 -6.816  1.00 36.37  ? 29  THR A CG2 1 
ATOM   221  N  N   . HIS A 1 30  ? 37.947  30.701 -4.402  1.00 27.70  ? 30  HIS A N   1 
ATOM   222  C  CA  . HIS A 1 30  ? 36.559  31.067 -4.304  1.00 26.89  ? 30  HIS A CA  1 
ATOM   223  C  C   . HIS A 1 30  ? 36.342  31.923 -3.077  1.00 27.12  ? 30  HIS A C   1 
ATOM   224  O  O   . HIS A 1 30  ? 37.020  31.738 -2.070  1.00 26.58  ? 30  HIS A O   1 
ATOM   225  C  CB  . HIS A 1 30  ? 35.655  29.856 -4.101  1.00 31.46  ? 30  HIS A CB  1 
ATOM   226  C  CG  . HIS A 1 30  ? 35.504  28.993 -5.290  1.00 29.91  ? 30  HIS A CG  1 
ATOM   227  N  ND1 . HIS A 1 30  ? 36.530  28.317 -5.885  1.00 32.98  ? 30  HIS A ND1 1 
ATOM   228  C  CD2 . HIS A 1 30  ? 34.395  28.724 -6.006  1.00 35.71  ? 30  HIS A CD2 1 
ATOM   229  C  CE1 . HIS A 1 30  ? 36.049  27.645 -6.916  1.00 36.13  ? 30  HIS A CE1 1 
ATOM   230  N  NE2 . HIS A 1 30  ? 34.749  27.901 -7.008  1.00 33.83  ? 30  HIS A NE2 1 
ATOM   231  N  N   . ASP A 1 31  ? 35.352  32.812 -3.221  1.00 25.49  ? 31  ASP A N   1 
ATOM   232  C  CA  . ASP A 1 31  ? 34.735  33.448 -2.090  1.00 29.88  ? 31  ASP A CA  1 
ATOM   233  C  C   . ASP A 1 31  ? 33.384  32.797 -1.908  1.00 28.09  ? 31  ASP A C   1 
ATOM   234  O  O   . ASP A 1 31  ? 32.674  32.524 -2.867  1.00 30.08  ? 31  ASP A O   1 
ATOM   235  C  CB  . ASP A 1 31  ? 34.556  34.963 -2.324  1.00 34.06  ? 31  ASP A CB  1 
ATOM   236  C  CG  . ASP A 1 31  ? 35.896  35.641 -2.571  1.00 38.02  ? 31  ASP A CG  1 
ATOM   237  O  OD1 . ASP A 1 31  ? 36.925  35.222 -1.927  1.00 30.90  ? 31  ASP A OD1 1 
ATOM   238  O  OD2 . ASP A 1 31  ? 35.915  36.526 -3.430  1.00 43.34  ? 31  ASP A OD2 1 
ATOM   239  N  N   . TRP A 1 32  ? 33.034  32.574 -0.653  1.00 25.89  ? 32  TRP A N   1 
ATOM   240  C  CA  . TRP A 1 32  ? 31.699  32.104 -0.365  1.00 26.47  ? 32  TRP A CA  1 
ATOM   241  C  C   . TRP A 1 32  ? 31.183  32.700 0.920   1.00 26.18  ? 32  TRP A C   1 
ATOM   242  O  O   . TRP A 1 32  ? 31.921  33.200 1.761   1.00 34.03  ? 32  TRP A O   1 
ATOM   243  C  CB  . TRP A 1 32  ? 31.653  30.561 -0.306  1.00 28.40  ? 32  TRP A CB  1 
ATOM   244  C  CG  . TRP A 1 32  ? 32.654  29.922 0.614   1.00 21.54  ? 32  TRP A CG  1 
ATOM   245  C  CD1 . TRP A 1 32  ? 33.802  29.286 0.255   1.00 29.29  ? 32  TRP A CD1 1 
ATOM   246  C  CD2 . TRP A 1 32  ? 32.535  29.711 2.032   1.00 26.51  ? 32  TRP A CD2 1 
ATOM   247  N  NE1 . TRP A 1 32  ? 34.426  28.715 1.335   1.00 26.44  ? 32  TRP A NE1 1 
ATOM   248  C  CE2 . TRP A 1 32  ? 33.659  28.948 2.436   1.00 25.67  ? 32  TRP A CE2 1 
ATOM   249  C  CE3 . TRP A 1 32  ? 31.573  30.052 2.995   1.00 28.71  ? 32  TRP A CE3 1 
ATOM   250  C  CZ2 . TRP A 1 32  ? 33.856  28.547 3.748   1.00 26.27  ? 32  TRP A CZ2 1 
ATOM   251  C  CZ3 . TRP A 1 32  ? 31.814  29.695 4.309   1.00 26.15  ? 32  TRP A CZ3 1 
ATOM   252  C  CH2 . TRP A 1 32  ? 32.919  28.942 4.662   1.00 24.87  ? 32  TRP A CH2 1 
ATOM   253  N  N   . MET A 1 33  ? 29.867  32.601 1.012   1.00 27.63  ? 33  MET A N   1 
ATOM   254  C  CA  . MET A 1 33  ? 29.145  33.036 2.161   1.00 30.69  ? 33  MET A CA  1 
ATOM   255  C  C   . MET A 1 33  ? 28.037  32.044 2.443   1.00 26.79  ? 33  MET A C   1 
ATOM   256  O  O   . MET A 1 33  ? 27.288  31.662 1.553   1.00 30.10  ? 33  MET A O   1 
ATOM   257  C  CB  . MET A 1 33  ? 28.582  34.438 1.903   1.00 39.12  ? 33  MET A CB  1 
ATOM   258  C  CG  . MET A 1 33  ? 27.941  35.053 3.101   1.00 48.10  ? 33  MET A CG  1 
ATOM   259  S  SD  . MET A 1 33  ? 26.221  34.656 3.106   1.00 57.25  ? 33  MET A SD  1 
ATOM   260  C  CE  . MET A 1 33  ? 25.712  35.358 1.536   1.00 55.44  ? 33  MET A CE  1 
ATOM   261  N  N   . VAL A 1 34  ? 27.873  31.736 3.733   1.00 28.43  ? 34  VAL A N   1 
ATOM   262  C  CA  . VAL A 1 34  ? 26.829  30.841 4.183   1.00 27.48  ? 34  VAL A CA  1 
ATOM   263  C  C   . VAL A 1 34  ? 26.047  31.528 5.284   1.00 30.40  ? 34  VAL A C   1 
ATOM   264  O  O   . VAL A 1 34  ? 26.611  32.281 6.077   1.00 32.31  ? 34  VAL A O   1 
ATOM   265  C  CB  . VAL A 1 34  ? 27.466  29.521 4.663   1.00 28.48  ? 34  VAL A CB  1 
ATOM   266  C  CG1 . VAL A 1 34  ? 28.352  29.682 5.898   1.00 27.83  ? 34  VAL A CG1 1 
ATOM   267  C  CG2 . VAL A 1 34  ? 26.428  28.470 4.928   1.00 33.07  ? 34  VAL A CG2 1 
ATOM   268  N  N   . PHE A 1 35  ? 24.757  31.186 5.357   1.00 32.90  ? 35  PHE A N   1 
ATOM   269  C  CA  . PHE A 1 35  ? 23.854  31.886 6.215   1.00 32.63  ? 35  PHE A CA  1 
ATOM   270  C  C   . PHE A 1 35  ? 22.719  30.987 6.678   1.00 34.36  ? 35  PHE A C   1 
ATOM   271  O  O   . PHE A 1 35  ? 22.332  29.995 6.037   1.00 32.03  ? 35  PHE A O   1 
ATOM   272  C  CB  . PHE A 1 35  ? 23.284  33.080 5.447   1.00 39.21  ? 35  PHE A CB  1 
ATOM   273  C  CG  . PHE A 1 35  ? 22.421  32.716 4.265   1.00 40.12  ? 35  PHE A CG  1 
ATOM   274  C  CD1 . PHE A 1 35  ? 21.084  32.367 4.422   1.00 43.00  ? 35  PHE A CD1 1 
ATOM   275  C  CD2 . PHE A 1 35  ? 22.945  32.724 2.987   1.00 40.38  ? 35  PHE A CD2 1 
ATOM   276  C  CE1 . PHE A 1 35  ? 20.289  32.079 3.324   1.00 43.98  ? 35  PHE A CE1 1 
ATOM   277  C  CE2 . PHE A 1 35  ? 22.159  32.405 1.887   1.00 41.89  ? 35  PHE A CE2 1 
ATOM   278  C  CZ  . PHE A 1 35  ? 20.831  32.108 2.056   1.00 41.43  ? 35  PHE A CZ  1 
ATOM   279  N  N   . VAL A 1 36  ? 22.194  31.432 7.814   1.00 31.06  ? 36  VAL A N   1 
ATOM   280  C  CA  . VAL A 1 36  ? 20.911  31.034 8.338   1.00 34.28  ? 36  VAL A CA  1 
ATOM   281  C  C   . VAL A 1 36  ? 20.086  32.294 8.511   1.00 35.96  ? 36  VAL A C   1 
ATOM   282  O  O   . VAL A 1 36  ? 20.554  33.290 9.104   1.00 38.42  ? 36  VAL A O   1 
ATOM   283  C  CB  . VAL A 1 36  ? 21.066  30.351 9.701   1.00 33.61  ? 36  VAL A CB  1 
ATOM   284  C  CG1 . VAL A 1 36  ? 19.713  30.093 10.314  1.00 39.27  ? 36  VAL A CG1 1 
ATOM   285  C  CG2 . VAL A 1 36  ? 21.892  29.082 9.619   1.00 33.81  ? 36  VAL A CG2 1 
ATOM   286  N  N   . ARG A 1 37  ? 18.859  32.220 8.014   1.00 36.05  ? 37  ARG A N   1 
ATOM   287  C  CA  . ARG A 1 37  ? 17.917  33.292 8.253   1.00 40.79  ? 37  ARG A CA  1 
ATOM   288  C  C   . ARG A 1 37  ? 16.495  32.749 8.217   1.00 36.00  ? 37  ARG A C   1 
ATOM   289  O  O   . ARG A 1 37  ? 16.246  31.572 7.932   1.00 44.31  ? 37  ARG A O   1 
ATOM   290  C  CB  . ARG A 1 37  ? 18.078  34.365 7.174   1.00 36.87  ? 37  ARG A CB  1 
ATOM   291  C  CG  . ARG A 1 37  ? 17.634  33.847 5.813   1.00 46.04  ? 37  ARG A CG  1 
ATOM   292  C  CD  . ARG A 1 37  ? 17.988  34.773 4.661   1.00 50.23  ? 37  ARG A CD  1 
ATOM   293  N  NE  . ARG A 1 37  ? 17.452  34.205 3.436   1.00 48.86  ? 37  ARG A NE  1 
ATOM   294  C  CZ  . ARG A 1 37  ? 17.974  34.301 2.213   1.00 50.99  ? 37  ARG A CZ  1 
ATOM   295  N  NH1 . ARG A 1 37  ? 17.409  33.618 1.241   1.00 51.83  ? 37  ARG A NH1 1 
ATOM   296  N  NH2 . ARG A 1 37  ? 19.048  35.031 1.954   1.00 59.94  ? 37  ARG A NH2 1 
ATOM   297  N  N   . GLY A 1 38  ? 15.564  33.664 8.445   1.00 47.96  ? 38  GLY A N   1 
ATOM   298  C  CA  . GLY A 1 38  ? 14.148  33.392 8.298   1.00 53.41  ? 38  GLY A CA  1 
ATOM   299  C  C   . GLY A 1 38  ? 13.721  33.785 6.895   1.00 51.75  ? 38  GLY A C   1 
ATOM   300  O  O   . GLY A 1 38  ? 14.296  34.687 6.318   1.00 51.89  ? 38  GLY A O   1 
ATOM   301  N  N   . PRO A 1 39  ? 12.676  33.175 6.305   1.00 65.38  ? 39  PRO A N   1 
ATOM   302  C  CA  . PRO A 1 39  ? 12.189  33.630 5.000   1.00 59.52  ? 39  PRO A CA  1 
ATOM   303  C  C   . PRO A 1 39  ? 11.730  35.081 5.070   1.00 52.68  ? 39  PRO A C   1 
ATOM   304  O  O   . PRO A 1 39  ? 11.317  35.542 6.121   1.00 53.87  ? 39  PRO A O   1 
ATOM   305  C  CB  . PRO A 1 39  ? 11.040  32.669 4.690   1.00 58.31  ? 39  PRO A CB  1 
ATOM   306  C  CG  . PRO A 1 39  ? 10.590  32.193 6.046   1.00 63.42  ? 39  PRO A CG  1 
ATOM   307  C  CD  . PRO A 1 39  ? 11.853  32.098 6.882   1.00 64.85  ? 39  PRO A CD  1 
ATOM   308  N  N   . GLU A 1 40  ? 11.973  35.819 3.985   1.00 66.96  ? 40  GLU A N   1 
ATOM   309  C  CA  . GLU A 1 40  ? 11.405  37.137 3.740   1.00 80.74  ? 40  GLU A CA  1 
ATOM   310  C  C   . GLU A 1 40  ? 11.543  38.061 4.943   1.00 82.30  ? 40  GLU A C   1 
ATOM   311  O  O   . GLU A 1 40  ? 10.548  38.605 5.424   1.00 73.51  ? 40  GLU A O   1 
ATOM   312  C  CB  . GLU A 1 40  ? 9.946   36.987 3.318   1.00 87.19  ? 40  GLU A CB  1 
ATOM   313  C  CG  . GLU A 1 40  ? 9.841   36.149 2.057   1.00 100.10 ? 40  GLU A CG  1 
ATOM   314  C  CD  . GLU A 1 40  ? 8.488   36.104 1.380   1.00 109.94 ? 40  GLU A CD  1 
ATOM   315  O  OE1 . GLU A 1 40  ? 7.544   35.544 1.974   1.00 115.81 ? 40  GLU A OE1 1 
ATOM   316  O  OE2 . GLU A 1 40  ? 8.400   36.592 0.236   1.00 115.71 ? 40  GLU A OE2 1 
ATOM   317  N  N   . HIS A 1 41  ? 12.793  38.248 5.378   1.00 87.65  ? 41  HIS A N   1 
ATOM   318  C  CA  . HIS A 1 41  ? 13.168  39.249 6.368   1.00 94.75  ? 41  HIS A CA  1 
ATOM   319  C  C   . HIS A 1 41  ? 12.523  38.974 7.731   1.00 88.44  ? 41  HIS A C   1 
ATOM   320  O  O   . HIS A 1 41  ? 12.545  39.862 8.574   1.00 88.66  ? 41  HIS A O   1 
ATOM   321  C  CB  . HIS A 1 41  ? 12.866  40.681 5.881   1.00 106.54 ? 41  HIS A CB  1 
ATOM   322  C  CG  . HIS A 1 41  ? 13.585  41.143 4.650   1.00 120.15 ? 41  HIS A CG  1 
ATOM   323  N  ND1 . HIS A 1 41  ? 14.958  41.283 4.566   1.00 118.48 ? 41  HIS A ND1 1 
ATOM   324  C  CD2 . HIS A 1 41  ? 13.106  41.581 3.473   1.00 113.09 ? 41  HIS A CD2 1 
ATOM   325  C  CE1 . HIS A 1 41  ? 15.289  41.735 3.368   1.00 106.02 ? 41  HIS A CE1 1 
ATOM   326  N  NE2 . HIS A 1 41  ? 14.179  41.927 2.689   1.00 115.21 ? 41  HIS A NE2 1 
ATOM   327  N  N   . SER A 1 42  ? 11.982  37.760 7.966   1.00 75.57  ? 42  SER A N   1 
ATOM   328  C  CA  . SER A 1 42  ? 11.365  37.446 9.248   1.00 67.35  ? 42  SER A CA  1 
ATOM   329  C  C   . SER A 1 42  ? 12.435  37.403 10.341  1.00 63.09  ? 42  SER A C   1 
ATOM   330  O  O   . SER A 1 42  ? 13.584  37.040 10.107  1.00 66.18  ? 42  SER A O   1 
ATOM   331  C  CB  . SER A 1 42  ? 10.584  36.150 9.199   1.00 71.69  ? 42  SER A CB  1 
ATOM   332  O  OG  . SER A 1 42  ? 11.428  35.030 8.965   1.00 64.10  ? 42  SER A OG  1 
ATOM   333  N  N   . ASN A 1 43  ? 12.064  37.737 11.566  1.00 51.73  ? 43  ASN A N   1 
ATOM   334  C  CA  . ASN A 1 43  ? 13.065  37.870 12.601  1.00 58.39  ? 43  ASN A CA  1 
ATOM   335  C  C   . ASN A 1 43  ? 13.168  36.608 13.465  1.00 56.49  ? 43  ASN A C   1 
ATOM   336  O  O   . ASN A 1 43  ? 12.385  36.460 14.386  1.00 64.34  ? 43  ASN A O   1 
ATOM   337  C  CB  . ASN A 1 43  ? 12.794  39.100 13.462  1.00 67.46  ? 43  ASN A CB  1 
ATOM   338  C  CG  . ASN A 1 43  ? 13.938  39.346 14.423  1.00 75.90  ? 43  ASN A CG  1 
ATOM   339  O  OD1 . ASN A 1 43  ? 14.987  38.688 14.349  1.00 75.26  ? 43  ASN A OD1 1 
ATOM   340  N  ND2 . ASN A 1 43  ? 13.730  40.262 15.352  1.00 85.44  ? 43  ASN A ND2 1 
ATOM   341  N  N   . ILE A 1 44  ? 14.190  35.760 13.236  1.00 47.12  ? 44  ILE A N   1 
ATOM   342  C  CA  . ILE A 1 44  ? 14.328  34.513 13.972  1.00 47.13  ? 44  ILE A CA  1 
ATOM   343  C  C   . ILE A 1 44  ? 15.092  34.741 15.267  1.00 43.07  ? 44  ILE A C   1 
ATOM   344  O  O   . ILE A 1 44  ? 15.102  33.874 16.151  1.00 40.65  ? 44  ILE A O   1 
ATOM   345  C  CB  . ILE A 1 44  ? 14.969  33.432 13.094  1.00 53.22  ? 44  ILE A CB  1 
ATOM   346  C  CG1 . ILE A 1 44  ? 16.378  33.827 12.625  1.00 52.98  ? 44  ILE A CG1 1 
ATOM   347  C  CG2 . ILE A 1 44  ? 14.057  33.095 11.916  1.00 54.15  ? 44  ILE A CG2 1 
ATOM   348  C  CD1 . ILE A 1 44  ? 17.170  32.661 12.124  1.00 50.18  ? 44  ILE A CD1 1 
ATOM   349  N  N   . GLN A 1 45  ? 15.666  35.940 15.410  1.00 35.98  ? 45  GLN A N   1 
ATOM   350  C  CA  . GLN A 1 45  ? 16.404  36.278 16.616  1.00 43.98  ? 45  GLN A CA  1 
ATOM   351  C  C   . GLN A 1 45  ? 15.537  36.114 17.871  1.00 50.48  ? 45  GLN A C   1 
ATOM   352  O  O   . GLN A 1 45  ? 16.077  35.840 18.950  1.00 47.79  ? 45  GLN A O   1 
ATOM   353  C  CB  . GLN A 1 45  ? 16.982  37.702 16.590  1.00 40.90  ? 45  GLN A CB  1 
ATOM   354  C  CG  . GLN A 1 45  ? 17.659  38.044 17.909  1.00 51.41  ? 45  GLN A CG  1 
ATOM   355  C  CD  . GLN A 1 45  ? 18.629  39.196 17.860  1.00 62.04  ? 45  GLN A CD  1 
ATOM   356  O  OE1 . GLN A 1 45  ? 18.366  40.198 17.203  1.00 65.82  ? 45  GLN A OE1 1 
ATOM   357  N  NE2 . GLN A 1 45  ? 19.773  39.039 18.521  1.00 61.81  ? 45  GLN A NE2 1 
ATOM   358  N  N   . HIS A 1 46  ? 14.211  36.293 17.732  1.00 48.89  ? 46  HIS A N   1 
ATOM   359  C  CA  . HIS A 1 46  ? 13.274  36.126 18.838  1.00 47.00  ? 46  HIS A CA  1 
ATOM   360  C  C   . HIS A 1 46  ? 13.445  34.763 19.510  1.00 45.34  ? 46  HIS A C   1 
ATOM   361  O  O   . HIS A 1 46  ? 13.353  34.651 20.729  1.00 50.69  ? 46  HIS A O   1 
ATOM   362  C  CB  . HIS A 1 46  ? 11.835  36.320 18.350  1.00 48.83  ? 46  HIS A CB  1 
ATOM   363  C  CG  . HIS A 1 46  ? 11.466  37.719 18.007  1.00 58.54  ? 46  HIS A CG  1 
ATOM   364  N  ND1 . HIS A 1 46  ? 11.559  38.766 18.909  1.00 61.60  ? 46  HIS A ND1 1 
ATOM   365  C  CD2 . HIS A 1 46  ? 10.975  38.245 16.865  1.00 61.64  ? 46  HIS A CD2 1 
ATOM   366  C  CE1 . HIS A 1 46  ? 11.132  39.885 18.324  1.00 55.71  ? 46  HIS A CE1 1 
ATOM   367  N  NE2 . HIS A 1 46  ? 10.770  39.593 17.085  1.00 54.12  ? 46  HIS A NE2 1 
ATOM   368  N  N   . PHE A 1 47  ? 13.733  33.712 18.747  1.00 40.86  ? 47  PHE A N   1 
ATOM   369  C  CA  . PHE A 1 47  ? 13.876  32.411 19.383  1.00 43.38  ? 47  PHE A CA  1 
ATOM   370  C  C   . PHE A 1 47  ? 15.252  31.781 19.175  1.00 40.98  ? 47  PHE A C   1 
ATOM   371  O  O   . PHE A 1 47  ? 15.504  30.676 19.662  1.00 39.31  ? 47  PHE A O   1 
ATOM   372  C  CB  . PHE A 1 47  ? 12.822  31.424 18.859  1.00 45.67  ? 47  PHE A CB  1 
ATOM   373  C  CG  . PHE A 1 47  ? 12.888  31.139 17.385  1.00 47.44  ? 47  PHE A CG  1 
ATOM   374  C  CD1 . PHE A 1 47  ? 12.306  31.998 16.462  1.00 45.88  ? 47  PHE A CD1 1 
ATOM   375  C  CD2 . PHE A 1 47  ? 13.533  30.009 16.921  1.00 47.55  ? 47  PHE A CD2 1 
ATOM   376  C  CE1 . PHE A 1 47  ? 12.372  31.734 15.109  1.00 43.71  ? 47  PHE A CE1 1 
ATOM   377  C  CE2 . PHE A 1 47  ? 13.604  29.747 15.563  1.00 45.98  ? 47  PHE A CE2 1 
ATOM   378  C  CZ  . PHE A 1 47  ? 13.034  30.614 14.662  1.00 44.89  ? 47  PHE A CZ  1 
ATOM   379  N  N   . VAL A 1 48  ? 16.096  32.414 18.365  1.00 43.14  ? 48  VAL A N   1 
ATOM   380  C  CA  . VAL A 1 48  ? 17.422  31.864 18.133  1.00 43.00  ? 48  VAL A CA  1 
ATOM   381  C  C   . VAL A 1 48  ? 18.426  32.558 19.047  1.00 39.11  ? 48  VAL A C   1 
ATOM   382  O  O   . VAL A 1 48  ? 18.547  33.791 19.025  1.00 37.64  ? 48  VAL A O   1 
ATOM   383  C  CB  . VAL A 1 48  ? 17.854  32.010 16.665  1.00 47.97  ? 48  VAL A CB  1 
ATOM   384  C  CG1 . VAL A 1 48  ? 19.347  31.704 16.545  1.00 46.45  ? 48  VAL A CG1 1 
ATOM   385  C  CG2 . VAL A 1 48  ? 17.023  31.126 15.735  1.00 42.33  ? 48  VAL A CG2 1 
ATOM   386  N  N   . GLU A 1 49  ? 19.146  31.740 19.820  1.00 36.93  ? 49  GLU A N   1 
ATOM   387  C  CA  . GLU A 1 49  ? 20.114  32.236 20.784  1.00 42.80  ? 49  GLU A CA  1 
ATOM   388  C  C   . GLU A 1 49  ? 21.418  32.546 20.056  1.00 40.02  ? 49  GLU A C   1 
ATOM   389  O  O   . GLU A 1 49  ? 22.006  33.598 20.268  1.00 40.41  ? 49  GLU A O   1 
ATOM   390  C  CB  . GLU A 1 49  ? 20.337  31.199 21.879  1.00 50.31  ? 49  GLU A CB  1 
ATOM   391  C  CG  . GLU A 1 49  ? 21.412  31.557 22.888  1.00 60.92  ? 49  GLU A CG  1 
ATOM   392  C  CD  . GLU A 1 49  ? 22.102  30.324 23.460  1.00 66.13  ? 49  GLU A CD  1 
ATOM   393  O  OE1 . GLU A 1 49  ? 21.412  29.502 24.033  1.00 63.34  ? 49  GLU A OE1 1 
ATOM   394  O  OE2 . GLU A 1 49  ? 23.338  30.169 23.297  1.00 97.63  ? 49  GLU A OE2 1 
ATOM   395  N  N   . LYS A 1 50  ? 21.873  31.601 19.235  1.00 34.78  ? 50  LYS A N   1 
ATOM   396  C  CA  . LYS A 1 50  ? 23.060  31.784 18.423  1.00 35.92  ? 50  LYS A CA  1 
ATOM   397  C  C   . LYS A 1 50  ? 23.093  30.683 17.369  1.00 38.83  ? 50  LYS A C   1 
ATOM   398  O  O   . LYS A 1 50  ? 22.372  29.689 17.479  1.00 35.98  ? 50  LYS A O   1 
ATOM   399  C  CB  . LYS A 1 50  ? 24.320  31.708 19.274  1.00 35.27  ? 50  LYS A CB  1 
ATOM   400  C  CG  . LYS A 1 50  ? 24.575  30.317 19.847  1.00 37.85  ? 50  LYS A CG  1 
ATOM   401  C  CD  . LYS A 1 50  ? 25.543  30.238 21.001  1.00 37.93  ? 50  LYS A CD  1 
ATOM   402  C  CE  . LYS A 1 50  ? 25.854  28.788 21.282  1.00 44.71  ? 50  LYS A CE  1 
ATOM   403  N  NZ  . LYS A 1 50  ? 26.253  28.527 22.672  1.00 54.18  ? 50  LYS A NZ  1 
ATOM   404  N  N   . VAL A 1 51  ? 23.952  30.905 16.370  1.00 36.94  ? 51  VAL A N   1 
ATOM   405  C  CA  . VAL A 1 51  ? 24.232  29.964 15.317  1.00 30.84  ? 51  VAL A CA  1 
ATOM   406  C  C   . VAL A 1 51  ? 25.735  29.737 15.329  1.00 30.60  ? 51  VAL A C   1 
ATOM   407  O  O   . VAL A 1 51  ? 26.521  30.692 15.367  1.00 35.40  ? 51  VAL A O   1 
ATOM   408  C  CB  . VAL A 1 51  ? 23.745  30.454 13.947  1.00 34.38  ? 51  VAL A CB  1 
ATOM   409  C  CG1 . VAL A 1 51  ? 24.091  29.459 12.840  1.00 36.43  ? 51  VAL A CG1 1 
ATOM   410  C  CG2 . VAL A 1 51  ? 22.253  30.754 13.964  1.00 36.68  ? 51  VAL A CG2 1 
ATOM   411  N  N   . VAL A 1 52  ? 26.102  28.457 15.305  1.00 27.03  ? 52  VAL A N   1 
ATOM   412  C  CA  . VAL A 1 52  ? 27.481  28.049 15.239  1.00 28.90  ? 52  VAL A CA  1 
ATOM   413  C  C   . VAL A 1 52  ? 27.668  27.366 13.899  1.00 32.94  ? 52  VAL A C   1 
ATOM   414  O  O   . VAL A 1 52  ? 26.972  26.397 13.614  1.00 36.42  ? 52  VAL A O   1 
ATOM   415  C  CB  . VAL A 1 52  ? 27.869  27.150 16.430  1.00 30.72  ? 52  VAL A CB  1 
ATOM   416  C  CG1 . VAL A 1 52  ? 29.313  26.705 16.357  1.00 32.40  ? 52  VAL A CG1 1 
ATOM   417  C  CG2 . VAL A 1 52  ? 27.618  27.829 17.771  1.00 32.96  ? 52  VAL A CG2 1 
ATOM   418  N  N   . PHE A 1 53  ? 28.641  27.867 13.130  1.00 31.67  ? 53  PHE A N   1 
ATOM   419  C  CA  . PHE A 1 53  ? 29.006  27.337 11.846  1.00 29.26  ? 53  PHE A CA  1 
ATOM   420  C  C   . PHE A 1 53  ? 30.300  26.598 12.060  1.00 32.81  ? 53  PHE A C   1 
ATOM   421  O  O   . PHE A 1 53  ? 31.272  27.227 12.462  1.00 37.14  ? 53  PHE A O   1 
ATOM   422  C  CB  . PHE A 1 53  ? 29.205  28.442 10.810  1.00 31.91  ? 53  PHE A CB  1 
ATOM   423  C  CG  . PHE A 1 53  ? 27.989  29.256 10.500  1.00 26.79  ? 53  PHE A CG  1 
ATOM   424  C  CD1 . PHE A 1 53  ? 27.642  30.320 11.309  1.00 29.46  ? 53  PHE A CD1 1 
ATOM   425  C  CD2 . PHE A 1 53  ? 27.160  28.916 9.435   1.00 25.42  ? 53  PHE A CD2 1 
ATOM   426  C  CE1 . PHE A 1 53  ? 26.530  31.104 10.994  1.00 32.92  ? 53  PHE A CE1 1 
ATOM   427  C  CE2 . PHE A 1 53  ? 26.016  29.638 9.173   1.00 32.55  ? 53  PHE A CE2 1 
ATOM   428  C  CZ  . PHE A 1 53  ? 25.711  30.754 9.941   1.00 36.33  ? 53  PHE A CZ  1 
ATOM   429  N  N   . HIS A 1 54  ? 30.301  25.283 11.801  1.00 31.92  ? 54  HIS A N   1 
ATOM   430  C  CA  . HIS A 1 54  ? 31.494  24.490 11.991  1.00 30.65  ? 54  HIS A CA  1 
ATOM   431  C  C   . HIS A 1 54  ? 32.211  24.323 10.665  1.00 34.19  ? 54  HIS A C   1 
ATOM   432  O  O   . HIS A 1 54  ? 31.903  23.430 9.856   1.00 39.57  ? 54  HIS A O   1 
ATOM   433  C  CB  . HIS A 1 54  ? 31.158  23.116 12.601  1.00 35.46  ? 54  HIS A CB  1 
ATOM   434  C  CG  . HIS A 1 54  ? 30.506  23.194 13.946  1.00 36.93  ? 54  HIS A CG  1 
ATOM   435  N  ND1 . HIS A 1 54  ? 31.194  22.978 15.114  1.00 41.37  ? 54  HIS A ND1 1 
ATOM   436  C  CD2 . HIS A 1 54  ? 29.254  23.512 14.317  1.00 41.33  ? 54  HIS A CD2 1 
ATOM   437  C  CE1 . HIS A 1 54  ? 30.363  23.122 16.149  1.00 43.25  ? 54  HIS A CE1 1 
ATOM   438  N  NE2 . HIS A 1 54  ? 29.175  23.427 15.685  1.00 40.22  ? 54  HIS A NE2 1 
ATOM   439  N  N   . LEU A 1 55  ? 33.236  25.140 10.484  1.00 32.80  ? 55  LEU A N   1 
ATOM   440  C  CA  . LEU A 1 55  ? 33.977  25.171 9.243   1.00 34.37  ? 55  LEU A CA  1 
ATOM   441  C  C   . LEU A 1 55  ? 34.900  23.973 9.208   1.00 34.77  ? 55  LEU A C   1 
ATOM   442  O  O   . LEU A 1 55  ? 35.268  23.477 10.251  1.00 38.98  ? 55  LEU A O   1 
ATOM   443  C  CB  . LEU A 1 55  ? 34.768  26.483 9.183   1.00 39.17  ? 55  LEU A CB  1 
ATOM   444  C  CG  . LEU A 1 55  ? 34.132  27.596 8.356   1.00 40.65  ? 55  LEU A CG  1 
ATOM   445  C  CD1 . LEU A 1 55  ? 32.722  27.890 8.792   1.00 42.92  ? 55  LEU A CD1 1 
ATOM   446  C  CD2 . LEU A 1 55  ? 34.992  28.837 8.415   1.00 36.85  ? 55  LEU A CD2 1 
ATOM   447  N  N   . HIS A 1 56  ? 35.289  23.531 8.018   1.00 38.20  ? 56  HIS A N   1 
ATOM   448  C  CA  . HIS A 1 56  ? 36.262  22.467 7.929   1.00 35.74  ? 56  HIS A CA  1 
ATOM   449  C  C   . HIS A 1 56  ? 37.495  22.874 8.717   1.00 43.63  ? 56  HIS A C   1 
ATOM   450  O  O   . HIS A 1 56  ? 37.841  24.067 8.841   1.00 33.13  ? 56  HIS A O   1 
ATOM   451  C  CB  . HIS A 1 56  ? 36.625  22.185 6.486   1.00 35.52  ? 56  HIS A CB  1 
ATOM   452  C  CG  . HIS A 1 56  ? 37.400  20.955 6.289   1.00 42.56  ? 56  HIS A CG  1 
ATOM   453  N  ND1 . HIS A 1 56  ? 38.777  20.948 6.225   1.00 35.11  ? 56  HIS A ND1 1 
ATOM   454  C  CD2 . HIS A 1 56  ? 36.970  19.680 5.966   1.00 41.70  ? 56  HIS A CD2 1 
ATOM   455  C  CE1 . HIS A 1 56  ? 39.176  19.703 5.954   1.00 42.42  ? 56  HIS A CE1 1 
ATOM   456  N  NE2 . HIS A 1 56  ? 38.098  18.925 5.800   1.00 42.03  ? 56  HIS A NE2 1 
ATOM   457  N  N   . GLU A 1 57  ? 38.113  21.857 9.303   1.00 39.10  ? 57  GLU A N   1 
ATOM   458  C  CA  . GLU A 1 57  ? 39.196  22.054 10.239  1.00 42.59  ? 57  GLU A CA  1 
ATOM   459  C  C   . GLU A 1 57  ? 40.441  22.514 9.497   1.00 40.90  ? 57  GLU A C   1 
ATOM   460  O  O   . GLU A 1 57  ? 41.411  22.867 10.149  1.00 45.43  ? 57  GLU A O   1 
ATOM   461  C  CB  . GLU A 1 57  ? 39.540  20.733 10.919  1.00 60.52  ? 57  GLU A CB  1 
ATOM   462  C  CG  . GLU A 1 57  ? 40.130  19.790 9.896   1.00 73.81  ? 57  GLU A CG  1 
ATOM   463  C  CD  . GLU A 1 57  ? 40.347  18.378 10.377  1.00 93.89  ? 57  GLU A CD  1 
ATOM   464  O  OE1 . GLU A 1 57  ? 40.688  17.533 9.521   1.00 86.48  ? 57  GLU A OE1 1 
ATOM   465  O  OE2 . GLU A 1 57  ? 40.194  18.151 11.603  1.00 114.38 ? 57  GLU A OE2 1 
ATOM   466  N  N   . SER A 1 58  ? 40.449  22.515 8.144   1.00 40.98  ? 58  SER A N   1 
ATOM   467  C  CA  . SER A 1 58  ? 41.500  23.208 7.401   1.00 37.72  ? 58  SER A CA  1 
ATOM   468  C  C   . SER A 1 58  ? 41.452  24.725 7.676   1.00 35.91  ? 58  SER A C   1 
ATOM   469  O  O   . SER A 1 58  ? 42.434  25.425 7.502   1.00 39.34  ? 58  SER A O   1 
ATOM   470  C  CB  . SER A 1 58  ? 41.428  22.923 5.927   1.00 32.37  ? 58  SER A CB  1 
ATOM   471  O  OG  . SER A 1 58  ? 40.125  23.218 5.422   1.00 38.92  ? 58  SER A OG  1 
ATOM   472  N  N   . PHE A 1 59  ? 40.309  25.266 8.085   1.00 39.10  ? 59  PHE A N   1 
ATOM   473  C  CA  . PHE A 1 59  ? 40.225  26.687 8.388   1.00 33.49  ? 59  PHE A CA  1 
ATOM   474  C  C   . PHE A 1 59  ? 40.719  26.985 9.795   1.00 33.62  ? 59  PHE A C   1 
ATOM   475  O  O   . PHE A 1 59  ? 40.388  26.301 10.736  1.00 37.42  ? 59  PHE A O   1 
ATOM   476  C  CB  . PHE A 1 59  ? 38.798  27.192 8.297   1.00 30.74  ? 59  PHE A CB  1 
ATOM   477  C  CG  . PHE A 1 59  ? 38.268  27.288 6.910   1.00 33.45  ? 59  PHE A CG  1 
ATOM   478  C  CD1 . PHE A 1 59  ? 37.731  26.177 6.267   1.00 38.05  ? 59  PHE A CD1 1 
ATOM   479  C  CD2 . PHE A 1 59  ? 38.361  28.496 6.225   1.00 31.11  ? 59  PHE A CD2 1 
ATOM   480  C  CE1 . PHE A 1 59  ? 37.267  26.279 4.965   1.00 34.28  ? 59  PHE A CE1 1 
ATOM   481  C  CE2 . PHE A 1 59  ? 37.906  28.594 4.928   1.00 35.09  ? 59  PHE A CE2 1 
ATOM   482  C  CZ  . PHE A 1 59  ? 37.363  27.474 4.299   1.00 42.40  ? 59  PHE A CZ  1 
ATOM   483  N  N   . PRO A 1 60  ? 41.432  28.103 10.007  1.00 38.76  ? 60  PRO A N   1 
ATOM   484  C  CA  . PRO A 1 60  ? 41.828  28.491 11.357  1.00 39.08  ? 60  PRO A CA  1 
ATOM   485  C  C   . PRO A 1 60  ? 40.550  28.857 12.108  1.00 33.09  ? 60  PRO A C   1 
ATOM   486  O  O   . PRO A 1 60  ? 39.610  29.332 11.497  1.00 33.33  ? 60  PRO A O   1 
ATOM   487  C  CB  . PRO A 1 60  ? 42.737  29.722 11.127  1.00 44.81  ? 60  PRO A CB  1 
ATOM   488  C  CG  . PRO A 1 60  ? 42.253  30.283 9.786   1.00 46.94  ? 60  PRO A CG  1 
ATOM   489  C  CD  . PRO A 1 60  ? 41.841  29.071 8.974   1.00 42.96  ? 60  PRO A CD  1 
ATOM   490  N  N   . ARG A 1 61  ? 40.504  28.602 13.415  1.00 34.34  ? 61  ARG A N   1 
ATOM   491  C  CA  . ARG A 1 61  ? 39.400  29.049 14.257  1.00 35.07  ? 61  ARG A CA  1 
ATOM   492  C  C   . ARG A 1 61  ? 38.077  28.615 13.640  1.00 29.85  ? 61  ARG A C   1 
ATOM   493  O  O   . ARG A 1 61  ? 37.211  29.396 13.324  1.00 33.28  ? 61  ARG A O   1 
ATOM   494  C  CB  . ARG A 1 61  ? 39.499  30.573 14.401  1.00 40.79  ? 61  ARG A CB  1 
ATOM   495  C  CG  . ARG A 1 61  ? 40.833  31.071 14.950  1.00 47.05  ? 61  ARG A CG  1 
ATOM   496  C  CD  . ARG A 1 61  ? 40.854  32.623 15.081  1.00 47.20  ? 61  ARG A CD  1 
ATOM   497  N  NE  . ARG A 1 61  ? 41.218  33.292 13.829  1.00 47.12  ? 61  ARG A NE  1 
ATOM   498  C  CZ  . ARG A 1 61  ? 42.395  33.159 13.200  1.00 44.64  ? 61  ARG A CZ  1 
ATOM   499  N  NH1 . ARG A 1 61  ? 42.507  33.495 11.929  1.00 40.80  ? 61  ARG A NH1 1 
ATOM   500  N  NH2 . ARG A 1 61  ? 43.441  32.608 13.810  1.00 44.85  ? 61  ARG A NH2 1 
ATOM   501  N  N   . PRO A 1 62  ? 37.889  27.305 13.383  1.00 39.01  ? 62  PRO A N   1 
ATOM   502  C  CA  . PRO A 1 62  ? 36.844  26.858 12.463  1.00 36.60  ? 62  PRO A CA  1 
ATOM   503  C  C   . PRO A 1 62  ? 35.422  27.029 12.997  1.00 34.23  ? 62  PRO A C   1 
ATOM   504  O  O   . PRO A 1 62  ? 34.465  26.985 12.235  1.00 38.38  ? 62  PRO A O   1 
ATOM   505  C  CB  . PRO A 1 62  ? 37.237  25.382 12.234  1.00 44.56  ? 62  PRO A CB  1 
ATOM   506  C  CG  . PRO A 1 62  ? 37.936  24.982 13.525  1.00 38.66  ? 62  PRO A CG  1 
ATOM   507  C  CD  . PRO A 1 62  ? 38.716  26.211 13.914  1.00 38.69  ? 62  PRO A CD  1 
ATOM   508  N  N   . LYS A 1 63  ? 35.269  27.182 14.309  1.00 32.31  ? 63  LYS A N   1 
ATOM   509  C  CA  . LYS A 1 63  ? 33.950  27.113 14.922  1.00 34.62  ? 63  LYS A CA  1 
ATOM   510  C  C   . LYS A 1 63  ? 33.450  28.527 15.133  1.00 34.10  ? 63  LYS A C   1 
ATOM   511  O  O   . LYS A 1 63  ? 33.788  29.116 16.165  1.00 39.31  ? 63  LYS A O   1 
ATOM   512  C  CB  . LYS A 1 63  ? 33.990  26.336 16.245  1.00 33.57  ? 63  LYS A CB  1 
ATOM   513  C  CG  . LYS A 1 63  ? 34.043  24.834 16.103  1.00 48.87  ? 63  LYS A CG  1 
ATOM   514  C  CD  . LYS A 1 63  ? 34.439  24.132 17.370  1.00 64.91  ? 63  LYS A CD  1 
ATOM   515  C  CE  . LYS A 1 63  ? 35.818  24.609 17.783  1.00 89.10  ? 63  LYS A CE  1 
ATOM   516  N  NZ  . LYS A 1 63  ? 36.469  23.716 18.758  1.00 100.86 ? 63  LYS A NZ  1 
ATOM   517  N  N   . ARG A 1 64  ? 32.636  29.033 14.189  1.00 35.20  ? 64  ARG A N   1 
ATOM   518  C  CA  . ARG A 1 64  ? 32.325  30.459 14.119  1.00 35.03  ? 64  ARG A CA  1 
ATOM   519  C  C   . ARG A 1 64  ? 30.925  30.679 14.646  1.00 36.84  ? 64  ARG A C   1 
ATOM   520  O  O   . ARG A 1 64  ? 29.992  30.014 14.192  1.00 36.56  ? 64  ARG A O   1 
ATOM   521  C  CB  . ARG A 1 64  ? 32.334  31.017 12.692  1.00 33.53  ? 64  ARG A CB  1 
ATOM   522  C  CG  . ARG A 1 64  ? 33.595  30.711 11.904  1.00 38.71  ? 64  ARG A CG  1 
ATOM   523  C  CD  . ARG A 1 64  ? 34.672  31.712 12.185  1.00 37.06  ? 64  ARG A CD  1 
ATOM   524  N  NE  . ARG A 1 64  ? 35.941  31.200 11.707  1.00 32.04  ? 64  ARG A NE  1 
ATOM   525  C  CZ  . ARG A 1 64  ? 36.434  31.442 10.518  1.00 30.80  ? 64  ARG A CZ  1 
ATOM   526  N  NH1 . ARG A 1 64  ? 37.634  30.988 10.204  1.00 30.36  ? 64  ARG A NH1 1 
ATOM   527  N  NH2 . ARG A 1 64  ? 35.767  32.192 9.669   1.00 28.63  ? 64  ARG A NH2 1 
ATOM   528  N  N   . VAL A 1 65  ? 30.789  31.596 15.609  1.00 33.13  ? 65  VAL A N   1 
ATOM   529  C  CA  . VAL A 1 65  ? 29.506  31.811 16.253  1.00 28.87  ? 65  VAL A CA  1 
ATOM   530  C  C   . VAL A 1 65  ? 28.984  33.194 15.887  1.00 32.85  ? 65  VAL A C   1 
ATOM   531  O  O   . VAL A 1 65  ? 29.729  34.128 15.907  1.00 36.16  ? 65  VAL A O   1 
ATOM   532  C  CB  . VAL A 1 65  ? 29.581  31.657 17.775  1.00 33.76  ? 65  VAL A CB  1 
ATOM   533  C  CG1 . VAL A 1 65  ? 30.629  32.552 18.387  1.00 36.45  ? 65  VAL A CG1 1 
ATOM   534  C  CG2 . VAL A 1 65  ? 28.247  31.904 18.421  1.00 37.20  ? 65  VAL A CG2 1 
ATOM   535  N  N   . CYS A 1 66  ? 27.690  33.293 15.583  1.00 31.53  ? 66  CYS A N   1 
ATOM   536  C  CA  . CYS A 1 66  ? 26.976  34.549 15.492  1.00 36.25  ? 66  CYS A CA  1 
ATOM   537  C  C   . CYS A 1 66  ? 25.844  34.544 16.518  1.00 39.55  ? 66  CYS A C   1 
ATOM   538  O  O   . CYS A 1 66  ? 24.965  33.695 16.437  1.00 45.42  ? 66  CYS A O   1 
ATOM   539  C  CB  . CYS A 1 66  ? 26.371  34.738 14.112  1.00 36.46  ? 66  CYS A CB  1 
ATOM   540  S  SG  . CYS A 1 66  ? 27.575  34.598 12.769  1.00 39.44  ? 66  CYS A SG  1 
ATOM   541  N  N   . LYS A 1 67  ? 25.899  35.461 17.497  1.00 41.37  ? 67  LYS A N   1 
ATOM   542  C  CA  . LYS A 1 67  ? 24.893  35.556 18.544  1.00 47.22  ? 67  LYS A CA  1 
ATOM   543  C  C   . LYS A 1 67  ? 23.735  36.410 18.039  1.00 39.20  ? 67  LYS A C   1 
ATOM   544  O  O   . LYS A 1 67  ? 22.604  36.270 18.479  1.00 49.76  ? 67  LYS A O   1 
ATOM   545  C  CB  . LYS A 1 67  ? 25.426  36.181 19.834  1.00 52.36  ? 67  LYS A CB  1 
ATOM   546  C  CG  . LYS A 1 67  ? 25.602  35.260 21.041  1.00 61.55  ? 67  LYS A CG  1 
ATOM   547  C  CD  . LYS A 1 67  ? 25.289  35.997 22.366  1.00 75.30  ? 67  LYS A CD  1 
ATOM   548  C  CE  . LYS A 1 67  ? 25.732  35.300 23.638  1.00 89.36  ? 67  LYS A CE  1 
ATOM   549  N  NZ  . LYS A 1 67  ? 25.168  33.935 23.755  1.00 94.86  ? 67  LYS A NZ  1 
ATOM   550  N  N   . ASP A 1 68  ? 24.050  37.257 17.075  1.00 37.64  ? 68  ASP A N   1 
ATOM   551  C  CA  . ASP A 1 68  ? 23.146  38.259 16.552  1.00 44.96  ? 68  ASP A CA  1 
ATOM   552  C  C   . ASP A 1 68  ? 23.087  38.148 15.036  1.00 41.12  ? 68  ASP A C   1 
ATOM   553  O  O   . ASP A 1 68  ? 24.079  37.869 14.394  1.00 41.37  ? 68  ASP A O   1 
ATOM   554  C  CB  . ASP A 1 68  ? 23.635  39.654 16.935  1.00 47.00  ? 68  ASP A CB  1 
ATOM   555  C  CG  . ASP A 1 68  ? 23.583  39.855 18.442  1.00 52.32  ? 68  ASP A CG  1 
ATOM   556  O  OD1 . ASP A 1 68  ? 22.477  39.814 18.971  1.00 66.39  ? 68  ASP A OD1 1 
ATOM   557  O  OD2 . ASP A 1 68  ? 24.653  39.967 19.076  1.00 56.68  ? 68  ASP A OD2 1 
ATOM   558  N  N   . PRO A 1 69  ? 21.936  38.431 14.412  1.00 43.51  ? 69  PRO A N   1 
ATOM   559  C  CA  . PRO A 1 69  ? 21.857  38.442 12.960  1.00 47.24  ? 69  PRO A CA  1 
ATOM   560  C  C   . PRO A 1 69  ? 22.727  39.559 12.406  1.00 50.17  ? 69  PRO A C   1 
ATOM   561  O  O   . PRO A 1 69  ? 22.945  40.549 13.073  1.00 58.16  ? 69  PRO A O   1 
ATOM   562  C  CB  . PRO A 1 69  ? 20.378  38.705 12.641  1.00 47.16  ? 69  PRO A CB  1 
ATOM   563  C  CG  . PRO A 1 69  ? 19.772  39.234 13.932  1.00 48.63  ? 69  PRO A CG  1 
ATOM   564  C  CD  . PRO A 1 69  ? 20.674  38.811 15.069  1.00 42.05  ? 69  PRO A CD  1 
ATOM   565  N  N   . PRO A 1 70  ? 23.243  39.463 11.173  1.00 48.89  ? 70  PRO A N   1 
ATOM   566  C  CA  . PRO A 1 70  ? 22.956  38.314 10.323  1.00 44.21  ? 70  PRO A CA  1 
ATOM   567  C  C   . PRO A 1 70  ? 23.771  37.086 10.726  1.00 40.74  ? 70  PRO A C   1 
ATOM   568  O  O   . PRO A 1 70  ? 24.900  37.205 11.138  1.00 35.36  ? 70  PRO A O   1 
ATOM   569  C  CB  . PRO A 1 70  ? 23.288  38.830 8.925   1.00 47.29  ? 70  PRO A CB  1 
ATOM   570  C  CG  . PRO A 1 70  ? 24.369  39.896 9.180   1.00 54.01  ? 70  PRO A CG  1 
ATOM   571  C  CD  . PRO A 1 70  ? 24.106  40.479 10.557  1.00 45.72  ? 70  PRO A CD  1 
ATOM   572  N  N   . TYR A 1 71  ? 23.139  35.908 10.697  1.00 37.38  ? 71  TYR A N   1 
ATOM   573  C  CA  . TYR A 1 71  ? 23.795  34.659 11.056  1.00 34.01  ? 71  TYR A CA  1 
ATOM   574  C  C   . TYR A 1 71  ? 24.468  34.166 9.791   1.00 37.25  ? 71  TYR A C   1 
ATOM   575  O  O   . TYR A 1 71  ? 23.808  33.558 8.926   1.00 34.69  ? 71  TYR A O   1 
ATOM   576  C  CB  . TYR A 1 71  ? 22.802  33.634 11.610  1.00 36.88  ? 71  TYR A CB  1 
ATOM   577  C  CG  . TYR A 1 71  ? 21.922  34.154 12.734  1.00 37.61  ? 71  TYR A CG  1 
ATOM   578  C  CD1 . TYR A 1 71  ? 22.445  34.314 14.010  1.00 38.43  ? 71  TYR A CD1 1 
ATOM   579  C  CD2 . TYR A 1 71  ? 20.597  34.529 12.519  1.00 38.73  ? 71  TYR A CD2 1 
ATOM   580  C  CE1 . TYR A 1 71  ? 21.677  34.780 15.061  1.00 41.66  ? 71  TYR A CE1 1 
ATOM   581  C  CE2 . TYR A 1 71  ? 19.821  35.014 13.565  1.00 48.42  ? 71  TYR A CE2 1 
ATOM   582  C  CZ  . TYR A 1 71  ? 20.358  35.131 14.842  1.00 43.36  ? 71  TYR A CZ  1 
ATOM   583  O  OH  . TYR A 1 71  ? 19.628  35.580 15.894  1.00 42.42  ? 71  TYR A OH  1 
ATOM   584  N  N   . LYS A 1 72  ? 25.757  34.502 9.662   1.00 31.18  ? 72  LYS A N   1 
ATOM   585  C  CA  . LYS A 1 72  ? 26.463  34.186 8.431   1.00 34.95  ? 72  LYS A CA  1 
ATOM   586  C  C   . LYS A 1 72  ? 27.964  34.192 8.647   1.00 34.16  ? 72  LYS A C   1 
ATOM   587  O  O   . LYS A 1 72  ? 28.491  34.841 9.549   1.00 41.47  ? 72  LYS A O   1 
ATOM   588  C  CB  . LYS A 1 72  ? 26.090  35.166 7.320   1.00 42.75  ? 72  LYS A CB  1 
ATOM   589  C  CG  . LYS A 1 72  ? 26.670  36.566 7.445   1.00 50.51  ? 72  LYS A CG  1 
ATOM   590  C  CD  . LYS A 1 72  ? 26.234  37.421 6.261   1.00 65.15  ? 72  LYS A CD  1 
ATOM   591  C  CE  . LYS A 1 72  ? 26.666  38.867 6.319   1.00 74.54  ? 72  LYS A CE  1 
ATOM   592  N  NZ  . LYS A 1 72  ? 28.093  39.002 6.712   1.00 87.20  ? 72  LYS A NZ  1 
ATOM   593  N  N   . VAL A 1 73  ? 28.647  33.509 7.733   1.00 31.82  ? 73  VAL A N   1 
ATOM   594  C  CA  . VAL A 1 73  ? 30.093  33.484 7.694   1.00 31.47  ? 73  VAL A CA  1 
ATOM   595  C  C   . VAL A 1 73  ? 30.500  33.718 6.249   1.00 33.81  ? 73  VAL A C   1 
ATOM   596  O  O   . VAL A 1 73  ? 29.969  33.094 5.337   1.00 33.10  ? 73  VAL A O   1 
ATOM   597  C  CB  . VAL A 1 73  ? 30.618  32.123 8.175   1.00 34.55  ? 73  VAL A CB  1 
ATOM   598  C  CG1 . VAL A 1 73  ? 32.103  31.981 7.922   1.00 36.82  ? 73  VAL A CG1 1 
ATOM   599  C  CG2 . VAL A 1 73  ? 30.279  31.872 9.643   1.00 40.87  ? 73  VAL A CG2 1 
ATOM   600  N  N   . GLU A 1 74  ? 31.497  34.563 6.065   1.00 34.97  ? 74  GLU A N   1 
ATOM   601  C  CA  . GLU A 1 74  ? 32.063  34.830 4.766   1.00 37.90  ? 74  GLU A CA  1 
ATOM   602  C  C   . GLU A 1 74  ? 33.499  34.402 4.799   1.00 33.55  ? 74  GLU A C   1 
ATOM   603  O  O   . GLU A 1 74  ? 34.208  34.764 5.713   1.00 42.90  ? 74  GLU A O   1 
ATOM   604  C  CB  . GLU A 1 74  ? 32.050  36.318 4.458   1.00 38.53  ? 74  GLU A CB  1 
ATOM   605  C  CG  . GLU A 1 74  ? 30.672  36.821 4.157   1.00 47.37  ? 74  GLU A CG  1 
ATOM   606  C  CD  . GLU A 1 74  ? 30.630  38.330 4.038   1.00 56.40  ? 74  GLU A CD  1 
ATOM   607  O  OE1 . GLU A 1 74  ? 30.586  38.978 5.090   1.00 58.66  ? 74  GLU A OE1 1 
ATOM   608  O  OE2 . GLU A 1 74  ? 30.773  38.822 2.899   1.00 81.47  ? 74  GLU A OE2 1 
ATOM   609  N  N   . GLU A 1 75  ? 33.913  33.707 3.756   1.00 31.42  ? 75  GLU A N   1 
ATOM   610  C  CA  . GLU A 1 75  ? 35.212  33.079 3.742   1.00 29.91  ? 75  GLU A CA  1 
ATOM   611  C  C   . GLU A 1 75  ? 35.656  32.945 2.303   1.00 28.70  ? 75  GLU A C   1 
ATOM   612  O  O   . GLU A 1 75  ? 34.908  33.227 1.374   1.00 34.53  ? 75  GLU A O   1 
ATOM   613  C  CB  . GLU A 1 75  ? 35.100  31.692 4.403   1.00 35.92  ? 75  GLU A CB  1 
ATOM   614  C  CG  . GLU A 1 75  ? 35.474  31.696 5.846   1.00 41.13  ? 75  GLU A CG  1 
ATOM   615  C  CD  . GLU A 1 75  ? 36.901  32.159 6.074   1.00 42.57  ? 75  GLU A CD  1 
ATOM   616  O  OE1 . GLU A 1 75  ? 37.648  32.201 5.078   1.00 47.01  ? 75  GLU A OE1 1 
ATOM   617  O  OE2 . GLU A 1 75  ? 37.217  32.566 7.204   1.00 40.95  ? 75  GLU A OE2 1 
ATOM   618  N  N   . SER A 1 76  ? 36.918  32.564 2.168   1.00 28.30  ? 76  SER A N   1 
ATOM   619  C  CA  . SER A 1 76  ? 37.527  32.238 0.904   1.00 31.85  ? 76  SER A CA  1 
ATOM   620  C  C   . SER A 1 76  ? 38.123  30.848 1.084   1.00 29.52  ? 76  SER A C   1 
ATOM   621  O  O   . SER A 1 76  ? 38.565  30.532 2.167   1.00 28.90  ? 76  SER A O   1 
ATOM   622  C  CB  . SER A 1 76  ? 38.569  33.256 0.499   1.00 33.67  ? 76  SER A CB  1 
ATOM   623  O  OG  . SER A 1 76  ? 37.944  34.413 -0.082  1.00 34.84  ? 76  SER A OG  1 
ATOM   624  N  N   . GLY A 1 77  ? 38.169  30.069 0.017   1.00 29.38  ? 77  GLY A N   1 
ATOM   625  C  CA  . GLY A 1 77  ? 38.731  28.733 0.097   1.00 35.06  ? 77  GLY A CA  1 
ATOM   626  C  C   . GLY A 1 77  ? 38.864  28.093 -1.285  1.00 32.80  ? 77  GLY A C   1 
ATOM   627  O  O   . GLY A 1 77  ? 38.742  28.794 -2.281  1.00 30.84  ? 77  GLY A O   1 
ATOM   628  N  N   . TYR A 1 78  ? 39.156  26.783 -1.316  1.00 34.61  ? 78  TYR A N   1 
ATOM   629  C  CA  . TYR A 1 78  ? 39.473  26.134 -2.577  1.00 38.95  ? 78  TYR A CA  1 
ATOM   630  C  C   . TYR A 1 78  ? 38.588  24.913 -2.813  1.00 34.43  ? 78  TYR A C   1 
ATOM   631  O  O   . TYR A 1 78  ? 38.604  24.388 -3.905  1.00 35.71  ? 78  TYR A O   1 
ATOM   632  C  CB  . TYR A 1 78  ? 40.973  25.829 -2.606  1.00 38.11  ? 78  TYR A CB  1 
ATOM   633  C  CG  . TYR A 1 78  ? 41.473  24.911 -1.502  1.00 40.30  ? 78  TYR A CG  1 
ATOM   634  C  CD1 . TYR A 1 78  ? 41.270  23.546 -1.553  1.00 44.50  ? 78  TYR A CD1 1 
ATOM   635  C  CD2 . TYR A 1 78  ? 42.120  25.418 -0.395  1.00 43.48  ? 78  TYR A CD2 1 
ATOM   636  C  CE1 . TYR A 1 78  ? 41.696  22.712 -0.531  1.00 44.38  ? 78  TYR A CE1 1 
ATOM   637  C  CE2 . TYR A 1 78  ? 42.541  24.605 0.643   1.00 41.68  ? 78  TYR A CE2 1 
ATOM   638  C  CZ  . TYR A 1 78  ? 42.332  23.237 0.570   1.00 47.51  ? 78  TYR A CZ  1 
ATOM   639  O  OH  . TYR A 1 78  ? 42.773  22.389 1.551   1.00 53.06  ? 78  TYR A OH  1 
ATOM   640  N  N   . ALA A 1 79  ? 37.813  24.488 -1.823  1.00 36.50  ? 79  ALA A N   1 
ATOM   641  C  CA  . ALA A 1 79  ? 37.072  23.235 -1.895  1.00 40.97  ? 79  ALA A CA  1 
ATOM   642  C  C   . ALA A 1 79  ? 35.775  23.332 -1.101  1.00 34.80  ? 79  ALA A C   1 
ATOM   643  O  O   . ALA A 1 79  ? 35.804  23.770 0.041   1.00 35.77  ? 79  ALA A O   1 
ATOM   644  C  CB  . ALA A 1 79  ? 37.892  22.075 -1.361  1.00 38.00  ? 79  ALA A CB  1 
ATOM   645  N  N   . GLY A 1 80  ? 34.688  22.819 -1.703  1.00 36.17  ? 80  GLY A N   1 
ATOM   646  C  CA  . GLY A 1 80  ? 33.441  22.516 -1.027  1.00 33.59  ? 80  GLY A CA  1 
ATOM   647  C  C   . GLY A 1 80  ? 33.653  21.513 0.097   1.00 29.19  ? 80  GLY A C   1 
ATOM   648  O  O   . GLY A 1 80  ? 34.658  20.822 0.116   1.00 33.41  ? 80  GLY A O   1 
ATOM   649  N  N   . PHE A 1 81  ? 32.737  21.504 1.062   1.00 34.61  ? 81  PHE A N   1 
ATOM   650  C  CA  . PHE A 1 81  ? 32.789  20.503 2.122   1.00 39.11  ? 81  PHE A CA  1 
ATOM   651  C  C   . PHE A 1 81  ? 31.487  20.554 2.884   1.00 35.67  ? 81  PHE A C   1 
ATOM   652  O  O   . PHE A 1 81  ? 30.649  21.378 2.549   1.00 31.54  ? 81  PHE A O   1 
ATOM   653  C  CB  . PHE A 1 81  ? 33.914  20.794 3.099   1.00 40.32  ? 81  PHE A CB  1 
ATOM   654  C  CG  . PHE A 1 81  ? 33.834  22.179 3.686   1.00 42.43  ? 81  PHE A CG  1 
ATOM   655  C  CD1 . PHE A 1 81  ? 34.363  23.271 3.007   1.00 40.66  ? 81  PHE A CD1 1 
ATOM   656  C  CD2 . PHE A 1 81  ? 33.184  22.402 4.901   1.00 35.70  ? 81  PHE A CD2 1 
ATOM   657  C  CE1 . PHE A 1 81  ? 34.316  24.535 3.580   1.00 33.75  ? 81  PHE A CE1 1 
ATOM   658  C  CE2 . PHE A 1 81  ? 33.097  23.673 5.445   1.00 36.81  ? 81  PHE A CE2 1 
ATOM   659  C  CZ  . PHE A 1 81  ? 33.658  24.738 4.776   1.00 37.17  ? 81  PHE A CZ  1 
ATOM   660  N  N   . ILE A 1 82  ? 31.335  19.671 3.872   1.00 40.06  ? 82  ILE A N   1 
ATOM   661  C  CA  . ILE A 1 82  ? 30.098  19.590 4.633   1.00 41.27  ? 82  ILE A CA  1 
ATOM   662  C  C   . ILE A 1 82  ? 30.293  20.456 5.865   1.00 36.80  ? 82  ILE A C   1 
ATOM   663  O  O   . ILE A 1 82  ? 31.255  20.287 6.596   1.00 38.77  ? 82  ILE A O   1 
ATOM   664  C  CB  . ILE A 1 82  ? 29.733  18.118 4.992   1.00 53.04  ? 82  ILE A CB  1 
ATOM   665  C  CG1 . ILE A 1 82  ? 29.464  17.214 3.766   1.00 48.51  ? 82  ILE A CG1 1 
ATOM   666  C  CG2 . ILE A 1 82  ? 28.560  18.091 5.959   1.00 45.33  ? 82  ILE A CG2 1 
ATOM   667  C  CD1 . ILE A 1 82  ? 28.440  17.760 2.773   1.00 57.92  ? 82  ILE A CD1 1 
ATOM   668  N  N   . LEU A 1 83  ? 29.353  21.370 6.103   1.00 34.38  ? 83  LEU A N   1 
ATOM   669  C  CA  . LEU A 1 83  ? 29.518  22.402 7.108   1.00 31.56  ? 83  LEU A CA  1 
ATOM   670  C  C   . LEU A 1 83  ? 28.397  22.287 8.116   1.00 25.71  ? 83  LEU A C   1 
ATOM   671  O  O   . LEU A 1 83  ? 27.280  22.642 7.814   1.00 31.76  ? 83  LEU A O   1 
ATOM   672  C  CB  . LEU A 1 83  ? 29.520  23.742 6.364   1.00 36.60  ? 83  LEU A CB  1 
ATOM   673  C  CG  . LEU A 1 83  ? 29.962  24.950 7.185   1.00 34.02  ? 83  LEU A CG  1 
ATOM   674  C  CD1 . LEU A 1 83  ? 30.059  26.190 6.296   1.00 37.13  ? 83  LEU A CD1 1 
ATOM   675  C  CD2 . LEU A 1 83  ? 28.991  25.173 8.317   1.00 34.90  ? 83  LEU A CD2 1 
ATOM   676  N  N   . PRO A 1 84  ? 28.615  21.613 9.251   1.00 31.16  ? 84  PRO A N   1 
ATOM   677  C  CA  . PRO A 1 84  ? 27.586  21.495 10.271  1.00 34.66  ? 84  PRO A CA  1 
ATOM   678  C  C   . PRO A 1 84  ? 27.223  22.881 10.784  1.00 32.76  ? 84  PRO A C   1 
ATOM   679  O  O   . PRO A 1 84  ? 28.098  23.687 11.062  1.00 36.48  ? 84  PRO A O   1 
ATOM   680  C  CB  . PRO A 1 84  ? 28.223  20.612 11.376  1.00 40.69  ? 84  PRO A CB  1 
ATOM   681  C  CG  . PRO A 1 84  ? 29.351  19.844 10.659  1.00 39.48  ? 84  PRO A CG  1 
ATOM   682  C  CD  . PRO A 1 84  ? 29.797  20.779 9.547   1.00 37.10  ? 84  PRO A CD  1 
ATOM   683  N  N   . ILE A 1 85  ? 25.926  23.130 10.857  1.00 30.83  ? 85  ILE A N   1 
ATOM   684  C  CA  . ILE A 1 85  ? 25.373  24.369 11.365  1.00 38.74  ? 85  ILE A CA  1 
ATOM   685  C  C   . ILE A 1 85  ? 24.499  24.001 12.539  1.00 41.61  ? 85  ILE A C   1 
ATOM   686  O  O   . ILE A 1 85  ? 23.635  23.140 12.415  1.00 42.56  ? 85  ILE A O   1 
ATOM   687  C  CB  . ILE A 1 85  ? 24.566  25.116 10.299  1.00 33.81  ? 85  ILE A CB  1 
ATOM   688  C  CG1 . ILE A 1 85  ? 25.412  25.388 9.056   1.00 37.92  ? 85  ILE A CG1 1 
ATOM   689  C  CG2 . ILE A 1 85  ? 23.958  26.342 10.923  1.00 34.28  ? 85  ILE A CG2 1 
ATOM   690  C  CD1 . ILE A 1 85  ? 24.753  26.190 7.968   1.00 39.65  ? 85  ILE A CD1 1 
ATOM   691  N  N   . GLU A 1 86  ? 24.745  24.677 13.662  1.00 41.85  ? 86  GLU A N   1 
ATOM   692  C  CA  . GLU A 1 86  ? 23.984  24.463 14.868  1.00 36.90  ? 86  GLU A CA  1 
ATOM   693  C  C   . GLU A 1 86  ? 23.242  25.727 15.187  1.00 38.30  ? 86  GLU A C   1 
ATOM   694  O  O   . GLU A 1 86  ? 23.869  26.759 15.434  1.00 38.70  ? 86  GLU A O   1 
ATOM   695  C  CB  . GLU A 1 86  ? 24.846  24.115 16.067  1.00 43.11  ? 86  GLU A CB  1 
ATOM   696  C  CG  . GLU A 1 86  ? 25.498  22.761 15.912  1.00 46.98  ? 86  GLU A CG  1 
ATOM   697  C  CD  . GLU A 1 86  ? 26.270  22.269 17.119  1.00 55.22  ? 86  GLU A CD  1 
ATOM   698  O  OE1 . GLU A 1 86  ? 27.175  22.998 17.612  1.00 66.40  ? 86  GLU A OE1 1 
ATOM   699  O  OE2 . GLU A 1 86  ? 26.000  21.132 17.508  1.00 53.27  ? 86  GLU A OE2 1 
ATOM   700  N  N   . VAL A 1 87  ? 21.917  25.579 15.220  1.00 36.06  ? 87  VAL A N   1 
ATOM   701  C  CA  . VAL A 1 87  ? 21.036  26.639 15.631  1.00 40.59  ? 87  VAL A CA  1 
ATOM   702  C  C   . VAL A 1 87  ? 20.548  26.331 17.034  1.00 41.69  ? 87  VAL A C   1 
ATOM   703  O  O   . VAL A 1 87  ? 19.843  25.339 17.234  1.00 44.02  ? 87  VAL A O   1 
ATOM   704  C  CB  . VAL A 1 87  ? 19.864  26.755 14.658  1.00 40.65  ? 87  VAL A CB  1 
ATOM   705  C  CG1 . VAL A 1 87  ? 18.933  27.873 15.087  1.00 40.95  ? 87  VAL A CG1 1 
ATOM   706  C  CG2 . VAL A 1 87  ? 20.358  26.938 13.231  1.00 40.91  ? 87  VAL A CG2 1 
ATOM   707  N  N   . TYR A 1 88  ? 20.952  27.188 17.968  1.00 36.74  ? 88  TYR A N   1 
ATOM   708  C  CA  . TYR A 1 88  ? 20.596  27.102 19.375  1.00 38.70  ? 88  TYR A CA  1 
ATOM   709  C  C   . TYR A 1 88  ? 19.386  27.983 19.621  1.00 43.01  ? 88  TYR A C   1 
ATOM   710  O  O   . TYR A 1 88  ? 19.338  29.124 19.141  1.00 36.88  ? 88  TYR A O   1 
ATOM   711  C  CB  . TYR A 1 88  ? 21.676  27.648 20.321  1.00 41.60  ? 88  TYR A CB  1 
ATOM   712  C  CG  . TYR A 1 88  ? 22.894  26.755 20.413  1.00 42.68  ? 88  TYR A CG  1 
ATOM   713  C  CD1 . TYR A 1 88  ? 23.733  26.556 19.311  1.00 47.22  ? 88  TYR A CD1 1 
ATOM   714  C  CD2 . TYR A 1 88  ? 23.173  26.049 21.587  1.00 43.71  ? 88  TYR A CD2 1 
ATOM   715  C  CE1 . TYR A 1 88  ? 24.827  25.700 19.369  1.00 42.31  ? 88  TYR A CE1 1 
ATOM   716  C  CE2 . TYR A 1 88  ? 24.285  25.219 21.672  1.00 44.82  ? 88  TYR A CE2 1 
ATOM   717  C  CZ  . TYR A 1 88  ? 25.091  25.025 20.552  1.00 48.38  ? 88  TYR A CZ  1 
ATOM   718  O  OH  . TYR A 1 88  ? 26.163  24.195 20.604  1.00 44.60  ? 88  TYR A OH  1 
ATOM   719  N  N   . PHE A 1 89  ? 18.484  27.485 20.468  1.00 35.90  ? 89  PHE A N   1 
ATOM   720  C  CA  . PHE A 1 89  ? 17.226  28.162 20.715  1.00 40.70  ? 89  PHE A CA  1 
ATOM   721  C  C   . PHE A 1 89  ? 17.266  28.851 22.067  1.00 44.53  ? 89  PHE A C   1 
ATOM   722  O  O   . PHE A 1 89  ? 17.945  28.390 22.963  1.00 45.51  ? 89  PHE A O   1 
ATOM   723  C  CB  . PHE A 1 89  ? 16.097  27.134 20.700  1.00 44.13  ? 89  PHE A CB  1 
ATOM   724  C  CG  . PHE A 1 89  ? 16.021  26.331 19.421  1.00 43.97  ? 89  PHE A CG  1 
ATOM   725  C  CD1 . PHE A 1 89  ? 15.907  26.959 18.206  1.00 42.11  ? 89  PHE A CD1 1 
ATOM   726  C  CD2 . PHE A 1 89  ? 16.045  24.951 19.447  1.00 43.93  ? 89  PHE A CD2 1 
ATOM   727  C  CE1 . PHE A 1 89  ? 15.814  26.227 17.033  1.00 40.70  ? 89  PHE A CE1 1 
ATOM   728  C  CE2 . PHE A 1 89  ? 15.988  24.221 18.277  1.00 42.16  ? 89  PHE A CE2 1 
ATOM   729  C  CZ  . PHE A 1 89  ? 15.872  24.863 17.076  1.00 43.46  ? 89  PHE A CZ  1 
ATOM   730  N  N   . LYS A 1 90  ? 16.502  29.932 22.201  1.00 47.96  ? 90  LYS A N   1 
ATOM   731  C  CA  . LYS A 1 90  ? 16.343  30.633 23.456  1.00 47.79  ? 90  LYS A CA  1 
ATOM   732  C  C   . LYS A 1 90  ? 15.312  29.920 24.322  1.00 50.81  ? 90  LYS A C   1 
ATOM   733  O  O   . LYS A 1 90  ? 14.289  30.467 24.667  1.00 51.62  ? 90  LYS A O   1 
ATOM   734  C  CB  . LYS A 1 90  ? 15.896  32.051 23.163  1.00 47.45  ? 90  LYS A CB  1 
ATOM   735  C  CG  . LYS A 1 90  ? 17.006  32.958 22.667  1.00 46.30  ? 90  LYS A CG  1 
ATOM   736  C  CD  . LYS A 1 90  ? 16.452  34.311 22.349  1.00 50.50  ? 90  LYS A CD  1 
ATOM   737  C  CE  . LYS A 1 90  ? 17.514  35.367 22.188  1.00 47.76  ? 90  LYS A CE  1 
ATOM   738  N  NZ  . LYS A 1 90  ? 16.970  36.445 21.349  1.00 52.33  ? 90  LYS A NZ  1 
ATOM   739  N  N   . ASN A 1 91  ? 15.699  28.730 24.740  1.00 59.54  ? 91  ASN A N   1 
ATOM   740  C  CA  . ASN A 1 91  ? 14.850  27.654 25.158  1.00 60.57  ? 91  ASN A CA  1 
ATOM   741  C  C   . ASN A 1 91  ? 15.391  27.167 26.492  1.00 62.90  ? 91  ASN A C   1 
ATOM   742  O  O   . ASN A 1 91  ? 16.568  27.363 26.734  1.00 64.88  ? 91  ASN A O   1 
ATOM   743  C  CB  . ASN A 1 91  ? 15.026  26.533 24.144  1.00 62.03  ? 91  ASN A CB  1 
ATOM   744  C  CG  . ASN A 1 91  ? 13.803  25.676 24.112  1.00 73.57  ? 91  ASN A CG  1 
ATOM   745  O  OD1 . ASN A 1 91  ? 12.820  26.035 24.750  1.00 76.37  ? 91  ASN A OD1 1 
ATOM   746  N  ND2 . ASN A 1 91  ? 13.840  24.593 23.359  1.00 86.83  ? 91  ASN A ND2 1 
ATOM   747  N  N   . LYS A 1 92  ? 14.594  26.470 27.299  1.00 61.89  ? 92  LYS A N   1 
ATOM   748  C  CA  . LYS A 1 92  ? 15.034  26.106 28.630  1.00 71.57  ? 92  LYS A CA  1 
ATOM   749  C  C   . LYS A 1 92  ? 14.679  24.652 28.887  1.00 72.16  ? 92  LYS A C   1 
ATOM   750  O  O   . LYS A 1 92  ? 14.290  24.302 29.980  1.00 107.16 ? 92  LYS A O   1 
ATOM   751  C  CB  . LYS A 1 92  ? 14.392  27.076 29.625  1.00 78.62  ? 92  LYS A CB  1 
ATOM   752  C  CG  . LYS A 1 92  ? 15.376  27.710 30.602  1.00 92.16  ? 92  LYS A CG  1 
ATOM   753  C  CD  . LYS A 1 92  ? 16.349  28.649 29.917  1.00 92.90  ? 92  LYS A CD  1 
ATOM   754  C  CE  . LYS A 1 92  ? 17.752  28.584 30.484  1.00 104.66 ? 92  LYS A CE  1 
ATOM   755  N  NZ  . LYS A 1 92  ? 18.699  29.330 29.623  1.00 107.83 ? 92  LYS A NZ  1 
ATOM   756  N  N   . GLU A 1 93  ? 14.825  23.817 27.858  1.00 73.96  ? 93  GLU A N   1 
ATOM   757  C  CA  . GLU A 1 93  ? 14.174  22.526 27.776  1.00 69.78  ? 93  GLU A CA  1 
ATOM   758  C  C   . GLU A 1 93  ? 14.611  21.905 26.459  1.00 73.95  ? 93  GLU A C   1 
ATOM   759  O  O   . GLU A 1 93  ? 15.045  22.631 25.575  1.00 68.75  ? 93  GLU A O   1 
ATOM   760  C  CB  . GLU A 1 93  ? 12.651  22.678 27.815  1.00 88.52  ? 93  GLU A CB  1 
ATOM   761  C  CG  . GLU A 1 93  ? 12.108  23.694 26.812  1.00 104.44 ? 93  GLU A CG  1 
ATOM   762  C  CD  . GLU A 1 93  ? 10.638  23.558 26.431  1.00 118.64 ? 93  GLU A CD  1 
ATOM   763  O  OE1 . GLU A 1 93  ? 9.962   22.681 27.028  1.00 135.34 ? 93  GLU A OE1 1 
ATOM   764  O  OE2 . GLU A 1 93  ? 10.148  24.347 25.542  1.00 78.82  ? 93  GLU A OE2 1 
ATOM   765  N  N   . GLU A 1 94  ? 14.515  20.577 26.327  1.00 77.12  ? 94  GLU A N   1 
ATOM   766  C  CA  . GLU A 1 94  ? 14.904  19.958 25.073  1.00 76.73  ? 94  GLU A CA  1 
ATOM   767  C  C   . GLU A 1 94  ? 13.852  20.283 24.022  1.00 83.38  ? 94  GLU A C   1 
ATOM   768  O  O   . GLU A 1 94  ? 12.714  20.557 24.387  1.00 98.31  ? 94  GLU A O   1 
ATOM   769  C  CB  . GLU A 1 94  ? 15.102  18.451 25.213  1.00 74.09  ? 94  GLU A CB  1 
ATOM   770  C  CG  . GLU A 1 94  ? 16.434  18.100 25.843  1.00 80.50  ? 94  GLU A CG  1 
ATOM   771  C  CD  . GLU A 1 94  ? 17.601  18.949 25.359  1.00 93.72  ? 94  GLU A CD  1 
ATOM   772  O  OE1 . GLU A 1 94  ? 17.778  19.083 24.122  1.00 92.35  ? 94  GLU A OE1 1 
ATOM   773  O  OE2 . GLU A 1 94  ? 18.339  19.472 26.220  1.00 87.75  ? 94  GLU A OE2 1 
ATOM   774  N  N   . PRO A 1 95  ? 14.218  20.377 22.718  1.00 80.83  ? 95  PRO A N   1 
ATOM   775  C  CA  . PRO A 1 95  ? 15.617  20.460 22.294  1.00 77.34  ? 95  PRO A CA  1 
ATOM   776  C  C   . PRO A 1 95  ? 16.164  21.886 22.433  1.00 56.36  ? 95  PRO A C   1 
ATOM   777  O  O   . PRO A 1 95  ? 15.432  22.844 22.259  1.00 58.26  ? 95  PRO A O   1 
ATOM   778  C  CB  . PRO A 1 95  ? 15.525  19.996 20.836  1.00 81.22  ? 95  PRO A CB  1 
ATOM   779  C  CG  . PRO A 1 95  ? 14.199  20.556 20.366  1.00 78.45  ? 95  PRO A CG  1 
ATOM   780  C  CD  . PRO A 1 95  ? 13.292  20.415 21.572  1.00 85.69  ? 95  PRO A CD  1 
ATOM   781  N  N   . ARG A 1 96  ? 17.435  22.014 22.818  1.00 56.18  ? 96  ARG A N   1 
ATOM   782  C  CA  . ARG A 1 96  ? 18.082  23.312 22.996  1.00 56.85  ? 96  ARG A CA  1 
ATOM   783  C  C   . ARG A 1 96  ? 18.631  23.825 21.662  1.00 50.34  ? 96  ARG A C   1 
ATOM   784  O  O   . ARG A 1 96  ? 18.945  24.989 21.514  1.00 44.20  ? 96  ARG A O   1 
ATOM   785  C  CB  . ARG A 1 96  ? 19.251  23.205 23.987  1.00 59.04  ? 96  ARG A CB  1 
ATOM   786  C  CG  . ARG A 1 96  ? 18.840  22.806 25.397  1.00 70.79  ? 96  ARG A CG  1 
ATOM   787  C  CD  . ARG A 1 96  ? 17.981  23.885 26.005  1.00 73.59  ? 96  ARG A CD  1 
ATOM   788  N  NE  . ARG A 1 96  ? 18.830  24.988 26.400  1.00 82.39  ? 96  ARG A NE  1 
ATOM   789  C  CZ  . ARG A 1 96  ? 18.977  25.411 27.658  1.00 107.50 ? 96  ARG A CZ  1 
ATOM   790  N  NH1 . ARG A 1 96  ? 18.424  24.747 28.665  1.00 100.68 ? 96  ARG A NH1 1 
ATOM   791  N  NH2 . ARG A 1 96  ? 19.690  26.500 27.910  1.00 111.15 ? 96  ARG A NH2 1 
ATOM   792  N  N   . LYS A 1 97  ? 18.771  22.940 20.690  1.00 45.14  ? 97  LYS A N   1 
ATOM   793  C  CA  . LYS A 1 97  ? 19.371  23.298 19.416  1.00 52.72  ? 97  LYS A CA  1 
ATOM   794  C  C   . LYS A 1 97  ? 19.028  22.231 18.388  1.00 44.22  ? 97  LYS A C   1 
ATOM   795  O  O   . LYS A 1 97  ? 18.504  21.177 18.731  1.00 53.31  ? 97  LYS A O   1 
ATOM   796  C  CB  . LYS A 1 97  ? 20.893  23.349 19.517  1.00 48.94  ? 97  LYS A CB  1 
ATOM   797  C  CG  . LYS A 1 97  ? 21.550  21.973 19.611  1.00 51.29  ? 97  LYS A CG  1 
ATOM   798  C  CD  . LYS A 1 97  ? 22.974  22.035 20.018  1.00 60.78  ? 97  LYS A CD  1 
ATOM   799  C  CE  . LYS A 1 97  ? 23.628  20.685 20.147  1.00 58.71  ? 97  LYS A CE  1 
ATOM   800  N  NZ  . LYS A 1 97  ? 25.047  20.870 20.534  1.00 69.08  ? 97  LYS A NZ  1 
ATOM   801  N  N   . VAL A 1 98  ? 19.363  22.531 17.145  1.00 43.82  ? 98  VAL A N   1 
ATOM   802  C  CA  . VAL A 1 98  ? 19.208  21.618 16.039  1.00 42.59  ? 98  VAL A CA  1 
ATOM   803  C  C   . VAL A 1 98  ? 20.427  21.786 15.152  1.00 45.89  ? 98  VAL A C   1 
ATOM   804  O  O   . VAL A 1 98  ? 20.985  22.872 15.039  1.00 47.97  ? 98  VAL A O   1 
ATOM   805  C  CB  . VAL A 1 98  ? 17.916  21.885 15.250  1.00 46.06  ? 98  VAL A CB  1 
ATOM   806  C  CG1 . VAL A 1 98  ? 17.891  23.315 14.726  1.00 45.90  ? 98  VAL A CG1 1 
ATOM   807  C  CG2 . VAL A 1 98  ? 17.711  20.884 14.107  1.00 44.15  ? 98  VAL A CG2 1 
ATOM   808  N  N   . ARG A 1 99  ? 20.801  20.678 14.527  1.00 40.62  ? 99  ARG A N   1 
ATOM   809  C  CA  . ARG A 1 99  ? 21.956  20.618 13.687  1.00 46.89  ? 99  ARG A CA  1 
ATOM   810  C  C   . ARG A 1 99  ? 21.535  20.304 12.255  1.00 47.43  ? 99  ARG A C   1 
ATOM   811  O  O   . ARG A 1 99  ? 20.729  19.427 12.024  1.00 48.89  ? 99  ARG A O   1 
ATOM   812  C  CB  . ARG A 1 99  ? 22.888  19.569 14.260  1.00 43.30  ? 99  ARG A CB  1 
ATOM   813  C  CG  . ARG A 1 99  ? 24.036  19.268 13.322  1.00 51.22  ? 99  ARG A CG  1 
ATOM   814  C  CD  . ARG A 1 99  ? 24.916  18.310 14.038  1.00 57.75  ? 99  ARG A CD  1 
ATOM   815  N  NE  . ARG A 1 99  ? 25.733  17.722 13.016  1.00 57.25  ? 99  ARG A NE  1 
ATOM   816  C  CZ  . ARG A 1 99  ? 27.025  17.548 13.135  1.00 58.29  ? 99  ARG A CZ  1 
ATOM   817  N  NH1 . ARG A 1 99  ? 27.619  17.992 14.231  1.00 57.28  ? 99  ARG A NH1 1 
ATOM   818  N  NH2 . ARG A 1 99  ? 27.697  16.978 12.139  1.00 57.69  ? 99  ARG A NH2 1 
ATOM   819  N  N   . PHE A 1 100 ? 22.083  21.063 11.310  1.00 45.26  ? 100 PHE A N   1 
ATOM   820  C  CA  . PHE A 1 100 ? 21.961  20.772 9.900   1.00 41.08  ? 100 PHE A CA  1 
ATOM   821  C  C   . PHE A 1 100 ? 23.346  20.520 9.361   1.00 42.66  ? 100 PHE A C   1 
ATOM   822  O  O   . PHE A 1 100 ? 24.258  21.298 9.641   1.00 50.84  ? 100 PHE A O   1 
ATOM   823  C  CB  . PHE A 1 100 ? 21.360  21.961 9.161   1.00 39.53  ? 100 PHE A CB  1 
ATOM   824  C  CG  . PHE A 1 100 ? 20.006  22.346 9.671   1.00 42.28  ? 100 PHE A CG  1 
ATOM   825  C  CD1 . PHE A 1 100 ? 18.915  21.527 9.423   1.00 43.09  ? 100 PHE A CD1 1 
ATOM   826  C  CD2 . PHE A 1 100 ? 19.847  23.469 10.476  1.00 39.17  ? 100 PHE A CD2 1 
ATOM   827  C  CE1 . PHE A 1 100 ? 17.672  21.871 9.917   1.00 47.91  ? 100 PHE A CE1 1 
ATOM   828  C  CE2 . PHE A 1 100 ? 18.614  23.791 10.993  1.00 34.27  ? 100 PHE A CE2 1 
ATOM   829  C  CZ  . PHE A 1 100 ? 17.514  23.022 10.667  1.00 45.58  ? 100 PHE A CZ  1 
ATOM   830  N  N   . ASP A 1 101 ? 23.479  19.470 8.562   1.00 41.81  ? 101 ASP A N   1 
ATOM   831  C  CA  . ASP A 1 101 ? 24.706  19.251 7.840   1.00 43.42  ? 101 ASP A CA  1 
ATOM   832  C  C   . ASP A 1 101 ? 24.602  19.932 6.479   1.00 44.04  ? 101 ASP A C   1 
ATOM   833  O  O   . ASP A 1 101 ? 23.953  19.431 5.571   1.00 46.85  ? 101 ASP A O   1 
ATOM   834  C  CB  . ASP A 1 101 ? 25.007  17.769 7.749   1.00 47.51  ? 101 ASP A CB  1 
ATOM   835  C  CG  . ASP A 1 101 ? 25.502  17.196 9.060   1.00 53.34  ? 101 ASP A CG  1 
ATOM   836  O  OD1 . ASP A 1 101 ? 25.969  17.967 9.897   1.00 57.38  ? 101 ASP A OD1 1 
ATOM   837  O  OD2 . ASP A 1 101 ? 25.384  15.986 9.244   1.00 69.40  ? 101 ASP A OD2 1 
ATOM   838  N  N   . TYR A 1 102 ? 25.280  21.067 6.332   1.00 39.04  ? 102 TYR A N   1 
ATOM   839  C  CA  . TYR A 1 102 ? 25.022  21.893 5.158   1.00 35.95  ? 102 TYR A CA  1 
ATOM   840  C  C   . TYR A 1 102 ? 26.090  21.585 4.126   1.00 31.14  ? 102 TYR A C   1 
ATOM   841  O  O   . TYR A 1 102 ? 27.284  21.645 4.385   1.00 38.27  ? 102 TYR A O   1 
ATOM   842  C  CB  . TYR A 1 102 ? 25.009  23.383 5.497   1.00 34.82  ? 102 TYR A CB  1 
ATOM   843  C  CG  . TYR A 1 102 ? 24.636  24.177 4.270   1.00 35.14  ? 102 TYR A CG  1 
ATOM   844  C  CD1 . TYR A 1 102 ? 23.303  24.354 3.935   1.00 34.42  ? 102 TYR A CD1 1 
ATOM   845  C  CD2 . TYR A 1 102 ? 25.611  24.677 3.405   1.00 33.36  ? 102 TYR A CD2 1 
ATOM   846  C  CE1 . TYR A 1 102 ? 22.945  25.081 2.813   1.00 30.93  ? 102 TYR A CE1 1 
ATOM   847  C  CE2 . TYR A 1 102 ? 25.255  25.365 2.258   1.00 30.71  ? 102 TYR A CE2 1 
ATOM   848  C  CZ  . TYR A 1 102 ? 23.924  25.561 1.960   1.00 28.78  ? 102 TYR A CZ  1 
ATOM   849  O  OH  . TYR A 1 102 ? 23.570  26.220 0.838   1.00 33.56  ? 102 TYR A OH  1 
ATOM   850  N  N   . ASP A 1 103 ? 25.648  21.321 2.911   1.00 37.91  ? 103 ASP A N   1 
ATOM   851  C  CA  . ASP A 1 103 ? 26.538  20.999 1.816   1.00 36.49  ? 103 ASP A CA  1 
ATOM   852  C  C   . ASP A 1 103 ? 27.019  22.305 1.175   1.00 33.06  ? 103 ASP A C   1 
ATOM   853  O  O   . ASP A 1 103 ? 26.337  22.909 0.373   1.00 30.64  ? 103 ASP A O   1 
ATOM   854  C  CB  . ASP A 1 103 ? 25.798  20.139 0.776   1.00 32.26  ? 103 ASP A CB  1 
ATOM   855  C  CG  . ASP A 1 103 ? 26.680  19.682 -0.372  1.00 34.46  ? 103 ASP A CG  1 
ATOM   856  O  OD1 . ASP A 1 103 ? 27.858  19.816 -0.259  1.00 36.22  ? 103 ASP A OD1 1 
ATOM   857  O  OD2 . ASP A 1 103 ? 26.152  19.133 -1.338  1.00 58.09  ? 103 ASP A OD2 1 
ATOM   858  N  N   . LEU A 1 104 ? 28.242  22.683 1.480   1.00 38.21  ? 104 LEU A N   1 
ATOM   859  C  CA  . LEU A 1 104 ? 28.808  23.932 0.987   1.00 36.49  ? 104 LEU A CA  1 
ATOM   860  C  C   . LEU A 1 104 ? 29.619  23.580 -0.251  1.00 32.11  ? 104 LEU A C   1 
ATOM   861  O  O   . LEU A 1 104 ? 30.804  23.250 -0.147  1.00 27.80  ? 104 LEU A O   1 
ATOM   862  C  CB  . LEU A 1 104 ? 29.672  24.534 2.100   1.00 35.95  ? 104 LEU A CB  1 
ATOM   863  C  CG  . LEU A 1 104 ? 30.341  25.889 1.874   1.00 41.67  ? 104 LEU A CG  1 
ATOM   864  C  CD1 . LEU A 1 104 ? 31.043  25.984 0.540   1.00 44.30  ? 104 LEU A CD1 1 
ATOM   865  C  CD2 . LEU A 1 104 ? 29.345  27.041 2.061   1.00 39.89  ? 104 LEU A CD2 1 
ATOM   866  N  N   . PHE A 1 105 ? 28.959  23.611 -1.405  1.00 28.21  ? 105 PHE A N   1 
ATOM   867  C  CA  . PHE A 1 105 ? 29.610  23.232 -2.631  1.00 36.57  ? 105 PHE A CA  1 
ATOM   868  C  C   . PHE A 1 105 ? 29.990  24.487 -3.434  1.00 30.78  ? 105 PHE A C   1 
ATOM   869  O  O   . PHE A 1 105 ? 29.334  25.531 -3.348  1.00 34.05  ? 105 PHE A O   1 
ATOM   870  C  CB  . PHE A 1 105 ? 28.726  22.258 -3.426  1.00 34.81  ? 105 PHE A CB  1 
ATOM   871  C  CG  . PHE A 1 105 ? 27.393  22.826 -3.819  1.00 31.73  ? 105 PHE A CG  1 
ATOM   872  C  CD1 . PHE A 1 105 ? 27.211  23.467 -5.032  1.00 36.25  ? 105 PHE A CD1 1 
ATOM   873  C  CD2 . PHE A 1 105 ? 26.295  22.641 -3.004  1.00 37.99  ? 105 PHE A CD2 1 
ATOM   874  C  CE1 . PHE A 1 105 ? 25.983  24.007 -5.380  1.00 37.00  ? 105 PHE A CE1 1 
ATOM   875  C  CE2 . PHE A 1 105 ? 25.057  23.111 -3.383  1.00 37.52  ? 105 PHE A CE2 1 
ATOM   876  C  CZ  . PHE A 1 105 ? 24.904  23.820 -4.555  1.00 36.89  ? 105 PHE A CZ  1 
ATOM   877  N  N   . LEU A 1 106 ? 31.038  24.269 -4.234  1.00 29.82  ? 106 LEU A N   1 
ATOM   878  C  CA  . LEU A 1 106 ? 31.641  25.190 -5.164  1.00 40.89  ? 106 LEU A CA  1 
ATOM   879  C  C   . LEU A 1 106 ? 31.441  24.636 -6.557  1.00 39.19  ? 106 LEU A C   1 
ATOM   880  O  O   . LEU A 1 106 ? 31.551  23.451 -6.731  1.00 42.72  ? 106 LEU A O   1 
ATOM   881  C  CB  . LEU A 1 106 ? 33.137  25.217 -4.837  1.00 39.02  ? 106 LEU A CB  1 
ATOM   882  C  CG  . LEU A 1 106 ? 33.477  25.654 -3.407  1.00 39.27  ? 106 LEU A CG  1 
ATOM   883  C  CD1 . LEU A 1 106 ? 34.968  25.816 -3.238  1.00 41.32  ? 106 LEU A CD1 1 
ATOM   884  C  CD2 . LEU A 1 106 ? 32.774  26.946 -3.002  1.00 40.04  ? 106 LEU A CD2 1 
ATOM   885  N  N   . HIS A 1 107 ? 31.197  25.498 -7.529  1.00 40.11  ? 107 HIS A N   1 
ATOM   886  C  CA  . HIS A 1 107 ? 31.281  25.140 -8.933  1.00 41.34  ? 107 HIS A CA  1 
ATOM   887  C  C   . HIS A 1 107 ? 32.569  25.704 -9.531  1.00 37.41  ? 107 HIS A C   1 
ATOM   888  O  O   . HIS A 1 107 ? 33.260  26.499 -8.915  1.00 39.09  ? 107 HIS A O   1 
ATOM   889  C  CB  . HIS A 1 107 ? 30.028  25.585 -9.694  1.00 43.78  ? 107 HIS A CB  1 
ATOM   890  C  CG  . HIS A 1 107 ? 28.785  24.809 -9.379  1.00 38.81  ? 107 HIS A CG  1 
ATOM   891  N  ND1 . HIS A 1 107 ? 27.532  25.256 -9.739  1.00 36.83  ? 107 HIS A ND1 1 
ATOM   892  C  CD2 . HIS A 1 107 ? 28.603  23.656 -8.708  1.00 41.94  ? 107 HIS A CD2 1 
ATOM   893  C  CE1 . HIS A 1 107 ? 26.634  24.408 -9.299  1.00 41.20  ? 107 HIS A CE1 1 
ATOM   894  N  NE2 . HIS A 1 107 ? 27.258  23.407 -8.698  1.00 48.32  ? 107 HIS A NE2 1 
ATOM   895  N  N   . LEU A 1 108 ? 32.942  25.161 -10.677 1.00 35.18  ? 108 LEU A N   1 
ATOM   896  C  CA  . LEU A 1 108 ? 34.233  25.433 -11.290 1.00 40.97  ? 108 LEU A CA  1 
ATOM   897  C  C   . LEU A 1 108 ? 34.174  26.761 -12.039 1.00 35.45  ? 108 LEU A C   1 
ATOM   898  O  O   . LEU A 1 108 ? 33.101  27.260 -12.388 1.00 35.68  ? 108 LEU A O   1 
ATOM   899  C  CB  . LEU A 1 108 ? 34.519  24.313 -12.295 1.00 49.44  ? 108 LEU A CB  1 
ATOM   900  C  CG  . LEU A 1 108 ? 34.618  22.897 -11.731 1.00 48.08  ? 108 LEU A CG  1 
ATOM   901  C  CD1 . LEU A 1 108 ? 34.830  21.912 -12.869 1.00 41.90  ? 108 LEU A CD1 1 
ATOM   902  C  CD2 . LEU A 1 108 ? 35.738  22.835 -10.709 1.00 40.42  ? 108 LEU A CD2 1 
ATOM   903  N  N   . GLU A 1 109 ? 35.334  27.320 -12.310 1.00 47.37  ? 109 GLU A N   1 
ATOM   904  C  CA  . GLU A 1 109 ? 35.427  28.454 -13.216 1.00 53.77  ? 109 GLU A CA  1 
ATOM   905  C  C   . GLU A 1 109 ? 34.718  28.060 -14.513 1.00 50.60  ? 109 GLU A C   1 
ATOM   906  O  O   . GLU A 1 109 ? 34.804  26.913 -14.950 1.00 53.55  ? 109 GLU A O   1 
ATOM   907  C  CB  . GLU A 1 109 ? 36.902  28.801 -13.409 1.00 59.89  ? 109 GLU A CB  1 
ATOM   908  C  CG  . GLU A 1 109 ? 37.126  30.109 -14.155 1.00 82.81  ? 109 GLU A CG  1 
ATOM   909  C  CD  . GLU A 1 109 ? 38.545  30.658 -14.040 1.00 99.07  ? 109 GLU A CD  1 
ATOM   910  O  OE1 . GLU A 1 109 ? 39.455  30.108 -14.725 1.00 94.53  ? 109 GLU A OE1 1 
ATOM   911  O  OE2 . GLU A 1 109 ? 38.756  31.625 -13.237 1.00 83.40  ? 109 GLU A OE2 1 
ATOM   912  N  N   . GLY A 1 110 ? 33.934  28.973 -15.065 1.00 43.71  ? 110 GLY A N   1 
ATOM   913  C  CA  . GLY A 1 110 ? 33.231  28.705 -16.301 1.00 46.04  ? 110 GLY A CA  1 
ATOM   914  C  C   . GLY A 1 110 ? 31.747  28.617 -16.036 1.00 44.74  ? 110 GLY A C   1 
ATOM   915  O  O   . GLY A 1 110 ? 30.938  28.872 -16.922 1.00 41.40  ? 110 GLY A O   1 
ATOM   916  N  N   . HIS A 1 111 ? 31.433  28.227 -14.788 1.00 43.42  ? 111 HIS A N   1 
ATOM   917  C  CA  . HIS A 1 111 ? 30.062  28.126 -14.356 1.00 40.41  ? 111 HIS A CA  1 
ATOM   918  C  C   . HIS A 1 111 ? 29.694  29.410 -13.669 1.00 37.86  ? 111 HIS A C   1 
ATOM   919  O  O   . HIS A 1 111 ? 30.540  30.045 -13.073 1.00 39.30  ? 111 HIS A O   1 
ATOM   920  C  CB  . HIS A 1 111 ? 29.872  26.916 -13.441 1.00 46.15  ? 111 HIS A CB  1 
ATOM   921  C  CG  . HIS A 1 111 ? 30.127  25.641 -14.155 1.00 51.98  ? 111 HIS A CG  1 
ATOM   922  N  ND1 . HIS A 1 111 ? 31.389  25.260 -14.583 1.00 52.27  ? 111 HIS A ND1 1 
ATOM   923  C  CD2 . HIS A 1 111 ? 29.265  24.679 -14.561 1.00 50.73  ? 111 HIS A CD2 1 
ATOM   924  C  CE1 . HIS A 1 111 ? 31.298  24.061 -15.150 1.00 48.47  ? 111 HIS A CE1 1 
ATOM   925  N  NE2 . HIS A 1 111 ? 30.011  23.699 -15.160 1.00 47.35  ? 111 HIS A NE2 1 
ATOM   926  N  N   . PRO A 1 112 ? 28.422  29.812 -13.720 1.00 41.29  ? 112 PRO A N   1 
ATOM   927  C  CA  . PRO A 1 112 ? 27.965  30.979 -12.965 1.00 48.08  ? 112 PRO A CA  1 
ATOM   928  C  C   . PRO A 1 112 ? 28.104  30.733 -11.473 1.00 43.70  ? 112 PRO A C   1 
ATOM   929  O  O   . PRO A 1 112 ? 28.298  29.613 -11.029 1.00 34.84  ? 112 PRO A O   1 
ATOM   930  C  CB  . PRO A 1 112 ? 26.473  31.107 -13.286 1.00 50.10  ? 112 PRO A CB  1 
ATOM   931  C  CG  . PRO A 1 112 ? 26.101  29.764 -13.864 1.00 47.77  ? 112 PRO A CG  1 
ATOM   932  C  CD  . PRO A 1 112 ? 27.349  29.147 -14.465 1.00 42.33  ? 112 PRO A CD  1 
ATOM   933  N  N   . PRO A 1 113 ? 28.058  31.781 -10.642 1.00 44.99  ? 113 PRO A N   1 
ATOM   934  C  CA  . PRO A 1 113 ? 28.191  31.581 -9.208  1.00 43.74  ? 113 PRO A CA  1 
ATOM   935  C  C   . PRO A 1 113 ? 27.126  30.634 -8.661  1.00 39.84  ? 113 PRO A C   1 
ATOM   936  O  O   . PRO A 1 113 ? 26.033  30.534 -9.175  1.00 45.72  ? 113 PRO A O   1 
ATOM   937  C  CB  . PRO A 1 113 ? 28.106  32.980 -8.600  1.00 45.57  ? 113 PRO A CB  1 
ATOM   938  C  CG  . PRO A 1 113 ? 27.687  33.905 -9.720  1.00 44.09  ? 113 PRO A CG  1 
ATOM   939  C  CD  . PRO A 1 113 ? 27.877  33.181 -11.029 1.00 43.54  ? 113 PRO A CD  1 
ATOM   940  N  N   . VAL A 1 114 ? 27.455  29.991 -7.560  1.00 42.49  ? 114 VAL A N   1 
ATOM   941  C  CA  . VAL A 1 114 ? 26.482  29.278 -6.771  1.00 40.31  ? 114 VAL A CA  1 
ATOM   942  C  C   . VAL A 1 114 ? 25.670  30.276 -5.957  1.00 38.01  ? 114 VAL A C   1 
ATOM   943  O  O   . VAL A 1 114 ? 26.212  31.158 -5.282  1.00 37.89  ? 114 VAL A O   1 
ATOM   944  C  CB  . VAL A 1 114 ? 27.183  28.255 -5.863  1.00 40.50  ? 114 VAL A CB  1 
ATOM   945  C  CG1 . VAL A 1 114 ? 26.204  27.588 -4.910  1.00 43.89  ? 114 VAL A CG1 1 
ATOM   946  C  CG2 . VAL A 1 114 ? 27.956  27.223 -6.669  1.00 43.66  ? 114 VAL A CG2 1 
ATOM   947  N  N   . ASN A 1 115 ? 24.358  30.049 -5.997  1.00 35.40  ? 115 ASN A N   1 
ATOM   948  C  CA  . ASN A 1 115 ? 23.397  30.706 -5.158  1.00 42.59  ? 115 ASN A CA  1 
ATOM   949  C  C   . ASN A 1 115 ? 22.370  29.662 -4.738  1.00 43.52  ? 115 ASN A C   1 
ATOM   950  O  O   . ASN A 1 115 ? 21.478  29.311 -5.502  1.00 45.61  ? 115 ASN A O   1 
ATOM   951  C  CB  . ASN A 1 115 ? 22.733  31.853 -5.909  1.00 37.79  ? 115 ASN A CB  1 
ATOM   952  C  CG  . ASN A 1 115 ? 21.863  32.696 -5.003  1.00 46.70  ? 115 ASN A CG  1 
ATOM   953  O  OD1 . ASN A 1 115 ? 21.866  32.546 -3.789  1.00 47.47  ? 115 ASN A OD1 1 
ATOM   954  N  ND2 . ASN A 1 115 ? 21.148  33.633 -5.593  1.00 51.24  ? 115 ASN A ND2 1 
ATOM   955  N  N   . HIS A 1 116 ? 22.554  29.083 -3.556  1.00 39.19  ? 116 HIS A N   1 
ATOM   956  C  CA  . HIS A 1 116 ? 21.761  27.928 -3.173  1.00 37.06  ? 116 HIS A CA  1 
ATOM   957  C  C   . HIS A 1 116 ? 20.905  28.334 -1.980  1.00 42.98  ? 116 HIS A C   1 
ATOM   958  O  O   . HIS A 1 116 ? 21.323  29.130 -1.141  1.00 43.25  ? 116 HIS A O   1 
ATOM   959  C  CB  . HIS A 1 116 ? 22.628  26.746 -2.774  1.00 36.32  ? 116 HIS A CB  1 
ATOM   960  C  CG  . HIS A 1 116 ? 21.831  25.508 -2.550  1.00 53.44  ? 116 HIS A CG  1 
ATOM   961  N  ND1 . HIS A 1 116 ? 21.348  24.736 -3.592  1.00 45.47  ? 116 HIS A ND1 1 
ATOM   962  C  CD2 . HIS A 1 116 ? 21.442  24.904 -1.405  1.00 47.07  ? 116 HIS A CD2 1 
ATOM   963  C  CE1 . HIS A 1 116 ? 20.677  23.718 -3.086  1.00 53.88  ? 116 HIS A CE1 1 
ATOM   964  N  NE2 . HIS A 1 116 ? 20.713  23.803 -1.766  1.00 55.57  ? 116 HIS A NE2 1 
ATOM   965  N  N   . LEU A 1 117 ? 19.699  27.784 -1.929  1.00 46.36  ? 117 LEU A N   1 
ATOM   966  C  CA  . LEU A 1 117 ? 18.779  28.020 -0.837  1.00 43.80  ? 117 LEU A CA  1 
ATOM   967  C  C   . LEU A 1 117 ? 18.148  26.692 -0.449  1.00 40.68  ? 117 LEU A C   1 
ATOM   968  O  O   . LEU A 1 117 ? 17.700  25.969 -1.303  1.00 41.86  ? 117 LEU A O   1 
ATOM   969  C  CB  . LEU A 1 117 ? 17.720  29.021 -1.269  1.00 46.61  ? 117 LEU A CB  1 
ATOM   970  C  CG  . LEU A 1 117 ? 16.700  29.405 -0.193  1.00 57.24  ? 117 LEU A CG  1 
ATOM   971  C  CD1 . LEU A 1 117 ? 17.334  30.094 0.995   1.00 56.40  ? 117 LEU A CD1 1 
ATOM   972  C  CD2 . LEU A 1 117 ? 15.650  30.321 -0.811  1.00 58.09  ? 117 LEU A CD2 1 
ATOM   973  N  N   . ARG A 1 118 ? 18.137  26.416 0.851   1.00 38.38  ? 118 ARG A N   1 
ATOM   974  C  CA  . ARG A 1 118 ? 17.579  25.210 1.417   1.00 42.40  ? 118 ARG A CA  1 
ATOM   975  C  C   . ARG A 1 118 ? 16.635  25.614 2.555   1.00 48.31  ? 118 ARG A C   1 
ATOM   976  O  O   . ARG A 1 118 ? 17.052  26.236 3.543   1.00 44.25  ? 118 ARG A O   1 
ATOM   977  C  CB  . ARG A 1 118 ? 18.746  24.340 1.879   1.00 39.71  ? 118 ARG A CB  1 
ATOM   978  C  CG  . ARG A 1 118 ? 18.364  23.192 2.794   1.00 38.15  ? 118 ARG A CG  1 
ATOM   979  C  CD  . ARG A 1 118 ? 19.633  22.577 3.337   1.00 39.14  ? 118 ARG A CD  1 
ATOM   980  N  NE  . ARG A 1 118 ? 19.314  21.664 4.402   1.00 40.70  ? 118 ARG A NE  1 
ATOM   981  C  CZ  . ARG A 1 118 ? 20.165  20.847 4.990   1.00 44.09  ? 118 ARG A CZ  1 
ATOM   982  N  NH1 . ARG A 1 118 ? 21.407  20.728 4.542   1.00 45.04  ? 118 ARG A NH1 1 
ATOM   983  N  NH2 . ARG A 1 118 ? 19.748  20.124 6.017   1.00 46.96  ? 118 ARG A NH2 1 
ATOM   984  N  N   . CYS A 1 119 ? 15.348  25.293 2.374   1.00 45.52  ? 119 CYS A N   1 
ATOM   985  C  CA  . CYS A 1 119 ? 14.319  25.624 3.352   1.00 49.94  ? 119 CYS A CA  1 
ATOM   986  C  C   . CYS A 1 119 ? 14.202  24.482 4.355   1.00 48.02  ? 119 CYS A C   1 
ATOM   987  O  O   . CYS A 1 119 ? 14.317  23.309 4.010   1.00 46.65  ? 119 CYS A O   1 
ATOM   988  C  CB  . CYS A 1 119 ? 12.991  25.927 2.676   1.00 46.27  ? 119 CYS A CB  1 
ATOM   989  S  SG  . CYS A 1 119 ? 13.129  27.391 1.622   1.00 69.57  ? 119 CYS A SG  1 
ATOM   990  N  N   . GLU A 1 120 ? 14.034  24.853 5.613   1.00 44.56  ? 120 GLU A N   1 
ATOM   991  C  CA  . GLU A 1 120 ? 13.926  23.888 6.697   1.00 50.64  ? 120 GLU A CA  1 
ATOM   992  C  C   . GLU A 1 120 ? 12.748  24.293 7.569   1.00 44.33  ? 120 GLU A C   1 
ATOM   993  O  O   . GLU A 1 120 ? 12.502  25.490 7.741   1.00 50.04  ? 120 GLU A O   1 
ATOM   994  C  CB  . GLU A 1 120 ? 15.245  23.831 7.472   1.00 50.17  ? 120 GLU A CB  1 
ATOM   995  C  CG  . GLU A 1 120 ? 16.352  23.161 6.673   1.00 52.67  ? 120 GLU A CG  1 
ATOM   996  C  CD  . GLU A 1 120 ? 16.251  21.650 6.566   1.00 53.37  ? 120 GLU A CD  1 
ATOM   997  O  OE1 . GLU A 1 120 ? 15.440  21.105 7.301   1.00 58.94  ? 120 GLU A OE1 1 
ATOM   998  O  OE2 . GLU A 1 120 ? 17.005  21.028 5.773   1.00 56.12  ? 120 GLU A OE2 1 
ATOM   999  N  N   . LYS A 1 121 ? 11.994  23.299 8.046   1.00 49.59  ? 121 LYS A N   1 
ATOM   1000 C  CA  . LYS A 1 121 ? 10.857  23.563 8.913   1.00 57.76  ? 121 LYS A CA  1 
ATOM   1001 C  C   . LYS A 1 121 ? 11.126  22.924 10.256  1.00 45.42  ? 121 LYS A C   1 
ATOM   1002 O  O   . LYS A 1 121 ? 11.452  21.755 10.336  1.00 47.18  ? 121 LYS A O   1 
ATOM   1003 C  CB  . LYS A 1 121 ? 9.539   23.039 8.341   1.00 65.48  ? 121 LYS A CB  1 
ATOM   1004 C  CG  . LYS A 1 121 ? 8.797   24.062 7.491   1.00 85.12  ? 121 LYS A CG  1 
ATOM   1005 C  CD  . LYS A 1 121 ? 7.720   23.476 6.581   1.00 100.80 ? 121 LYS A CD  1 
ATOM   1006 C  CE  . LYS A 1 121 ? 8.270   22.663 5.424   1.00 108.04 ? 121 LYS A CE  1 
ATOM   1007 N  NZ  . LYS A 1 121 ? 7.191   22.023 4.638   1.00 108.44 ? 121 LYS A NZ  1 
ATOM   1008 N  N   . LEU A 1 122 ? 10.972  23.709 11.307  1.00 44.22  ? 122 LEU A N   1 
ATOM   1009 C  CA  . LEU A 1 122 ? 11.075  23.188 12.664  1.00 50.46  ? 122 LEU A CA  1 
ATOM   1010 C  C   . LEU A 1 122 ? 9.683   23.070 13.263  1.00 49.66  ? 122 LEU A C   1 
ATOM   1011 O  O   . LEU A 1 122 ? 8.909   24.018 13.144  1.00 40.92  ? 122 LEU A O   1 
ATOM   1012 C  CB  . LEU A 1 122 ? 11.892  24.200 13.473  1.00 59.13  ? 122 LEU A CB  1 
ATOM   1013 C  CG  . LEU A 1 122 ? 13.277  24.458 12.877  1.00 63.51  ? 122 LEU A CG  1 
ATOM   1014 C  CD1 . LEU A 1 122 ? 13.992  25.539 13.645  1.00 59.82  ? 122 LEU A CD1 1 
ATOM   1015 C  CD2 . LEU A 1 122 ? 14.086  23.162 12.846  1.00 60.10  ? 122 LEU A CD2 1 
ATOM   1016 N  N   . THR A 1 123 ? 9.415   21.967 13.977  1.00 53.96  ? 123 THR A N   1 
ATOM   1017 C  CA  . THR A 1 123 ? 8.149   21.800 14.678  1.00 55.91  ? 123 THR A CA  1 
ATOM   1018 C  C   . THR A 1 123 ? 8.427   21.655 16.167  1.00 52.63  ? 123 THR A C   1 
ATOM   1019 O  O   . THR A 1 123 ? 9.161   20.760 16.571  1.00 43.73  ? 123 THR A O   1 
ATOM   1020 C  CB  . THR A 1 123 ? 7.340   20.640 14.084  1.00 56.55  ? 123 THR A CB  1 
ATOM   1021 O  OG1 . THR A 1 123 ? 7.096   21.037 12.738  1.00 63.04  ? 123 THR A OG1 1 
ATOM   1022 C  CG2 . THR A 1 123 ? 6.003   20.392 14.756  1.00 56.27  ? 123 THR A CG2 1 
ATOM   1023 N  N   . PHE A 1 124 ? 7.833   22.527 16.981  1.00 47.37  ? 124 PHE A N   1 
ATOM   1024 C  CA  . PHE A 1 124 ? 7.930   22.336 18.421  1.00 53.39  ? 124 PHE A CA  1 
ATOM   1025 C  C   . PHE A 1 124 ? 6.558   21.981 18.990  1.00 49.62  ? 124 PHE A C   1 
ATOM   1026 O  O   . PHE A 1 124 ? 5.622   22.767 18.838  1.00 38.20  ? 124 PHE A O   1 
ATOM   1027 C  CB  . PHE A 1 124 ? 8.440   23.593 19.113  1.00 46.52  ? 124 PHE A CB  1 
ATOM   1028 C  CG  . PHE A 1 124 ? 9.786   24.048 18.642  1.00 55.70  ? 124 PHE A CG  1 
ATOM   1029 C  CD1 . PHE A 1 124 ? 9.896   24.855 17.513  1.00 55.01  ? 124 PHE A CD1 1 
ATOM   1030 C  CD2 . PHE A 1 124 ? 10.934  23.651 19.315  1.00 48.97  ? 124 PHE A CD2 1 
ATOM   1031 C  CE1 . PHE A 1 124 ? 11.138  25.274 17.073  1.00 52.03  ? 124 PHE A CE1 1 
ATOM   1032 C  CE2 . PHE A 1 124 ? 12.180  24.080 18.872  1.00 58.26  ? 124 PHE A CE2 1 
ATOM   1033 C  CZ  . PHE A 1 124 ? 12.279  24.875 17.748  1.00 54.94  ? 124 PHE A CZ  1 
ATOM   1034 N  N   . ASN A 1 125 ? 6.469   20.810 19.627  1.00 50.68  ? 125 ASN A N   1 
ATOM   1035 C  CA  . ASN A 1 125 ? 5.230   20.347 20.240  1.00 57.03  ? 125 ASN A CA  1 
ATOM   1036 C  C   . ASN A 1 125 ? 5.176   20.777 21.702  1.00 56.21  ? 125 ASN A C   1 
ATOM   1037 O  O   . ASN A 1 125 ? 6.097   20.519 22.453  1.00 59.82  ? 125 ASN A O   1 
ATOM   1038 C  CB  . ASN A 1 125 ? 5.071   18.840 20.095  1.00 55.97  ? 125 ASN A CB  1 
ATOM   1039 C  CG  . ASN A 1 125 ? 4.894   18.445 18.644  1.00 56.39  ? 125 ASN A CG  1 
ATOM   1040 O  OD1 . ASN A 1 125 ? 4.137   19.056 17.899  1.00 66.08  ? 125 ASN A OD1 1 
ATOM   1041 N  ND2 . ASN A 1 125 ? 5.624   17.444 18.213  1.00 58.74  ? 125 ASN A ND2 1 
ATOM   1042 N  N   . ASN A 1 126 ? 4.118   21.508 22.056  1.00 53.59  ? 126 ASN A N   1 
ATOM   1043 C  CA  . ASN A 1 126 ? 3.864   21.934 23.414  1.00 53.89  ? 126 ASN A CA  1 
ATOM   1044 C  C   . ASN A 1 126 ? 5.103   22.585 23.994  1.00 58.52  ? 126 ASN A C   1 
ATOM   1045 O  O   . ASN A 1 126 ? 5.596   22.176 25.027  1.00 57.99  ? 126 ASN A O   1 
ATOM   1046 C  CB  . ASN A 1 126 ? 3.406   20.755 24.264  1.00 48.99  ? 126 ASN A CB  1 
ATOM   1047 C  CG  . ASN A 1 126 ? 2.090   20.236 23.734  1.00 51.47  ? 126 ASN A CG  1 
ATOM   1048 O  OD1 . ASN A 1 126 ? 1.122   20.992 23.628  1.00 42.76  ? 126 ASN A OD1 1 
ATOM   1049 N  ND2 . ASN A 1 126 ? 2.056   18.976 23.342  1.00 44.71  ? 126 ASN A ND2 1 
ATOM   1050 N  N   . PRO A 1 127 ? 5.642   23.632 23.352  1.00 60.94  ? 127 PRO A N   1 
ATOM   1051 C  CA  . PRO A 1 127 ? 6.692   24.424 23.980  1.00 55.23  ? 127 PRO A CA  1 
ATOM   1052 C  C   . PRO A 1 127 ? 6.159   25.055 25.265  1.00 52.06  ? 127 PRO A C   1 
ATOM   1053 O  O   . PRO A 1 127 ? 4.958   25.240 25.408  1.00 52.57  ? 127 PRO A O   1 
ATOM   1054 C  CB  . PRO A 1 127 ? 7.016   25.505 22.938  1.00 50.03  ? 127 PRO A CB  1 
ATOM   1055 C  CG  . PRO A 1 127 ? 5.762   25.571 22.074  1.00 51.82  ? 127 PRO A CG  1 
ATOM   1056 C  CD  . PRO A 1 127 ? 5.236   24.153 22.044  1.00 52.79  ? 127 PRO A CD  1 
ATOM   1057 N  N   . THR A 1 128 ? 7.074   25.458 26.141  1.00 45.77  ? 128 THR A N   1 
ATOM   1058 C  CA  . THR A 1 128 ? 6.731   26.219 27.323  1.00 49.73  ? 128 THR A CA  1 
ATOM   1059 C  C   . THR A 1 128 ? 6.101   27.516 26.868  1.00 50.71  ? 128 THR A C   1 
ATOM   1060 O  O   . THR A 1 128 ? 6.252   27.892 25.713  1.00 46.07  ? 128 THR A O   1 
ATOM   1061 C  CB  . THR A 1 128 ? 7.947   26.664 28.147  1.00 57.20  ? 128 THR A CB  1 
ATOM   1062 O  OG1 . THR A 1 128 ? 8.722   27.546 27.331  1.00 62.86  ? 128 THR A OG1 1 
ATOM   1063 C  CG2 . THR A 1 128 ? 8.821   25.533 28.634  1.00 51.08  ? 128 THR A CG2 1 
ATOM   1064 N  N   . GLU A 1 129 ? 5.473   28.212 27.810  1.00 53.27  ? 129 GLU A N   1 
ATOM   1065 C  CA  . GLU A 1 129 ? 4.804   29.465 27.520  1.00 55.29  ? 129 GLU A CA  1 
ATOM   1066 C  C   . GLU A 1 129 ? 5.836   30.469 27.018  1.00 52.08  ? 129 GLU A C   1 
ATOM   1067 O  O   . GLU A 1 129 ? 5.602   31.151 26.021  1.00 58.80  ? 129 GLU A O   1 
ATOM   1068 C  CB  . GLU A 1 129 ? 4.044   29.979 28.743  1.00 48.87  ? 129 GLU A CB  1 
ATOM   1069 C  CG  . GLU A 1 129 ? 3.377   31.315 28.514  1.00 57.38  ? 129 GLU A CG  1 
ATOM   1070 C  CD  . GLU A 1 129 ? 2.502   31.783 29.662  1.00 66.34  ? 129 GLU A CD  1 
ATOM   1071 O  OE1 . GLU A 1 129 ? 1.513   31.101 29.962  1.00 66.59  ? 129 GLU A OE1 1 
ATOM   1072 O  OE2 . GLU A 1 129 ? 2.783   32.860 30.215  1.00 83.17  ? 129 GLU A OE2 1 
ATOM   1073 N  N   . ASP A 1 130 ? 6.970   30.553 27.716  1.00 56.61  ? 130 ASP A N   1 
ATOM   1074 C  CA  . ASP A 1 130 ? 7.982   31.557 27.426  1.00 62.22  ? 130 ASP A CA  1 
ATOM   1075 C  C   . ASP A 1 130 ? 8.474   31.410 25.985  1.00 50.64  ? 130 ASP A C   1 
ATOM   1076 O  O   . ASP A 1 130 ? 8.511   32.364 25.198  1.00 53.57  ? 130 ASP A O   1 
ATOM   1077 C  CB  . ASP A 1 130 ? 9.152   31.425 28.405  1.00 68.36  ? 130 ASP A CB  1 
ATOM   1078 C  CG  . ASP A 1 130 ? 9.835   32.763 28.603  1.00 94.80  ? 130 ASP A CG  1 
ATOM   1079 O  OD1 . ASP A 1 130 ? 9.191   33.668 29.208  1.00 104.91 ? 130 ASP A OD1 1 
ATOM   1080 O  OD2 . ASP A 1 130 ? 10.969  32.910 28.091  1.00 87.98  ? 130 ASP A OD2 1 
ATOM   1081 N  N   . PHE A 1 131 ? 8.826   30.172 25.667  1.00 42.22  ? 131 PHE A N   1 
ATOM   1082 C  CA  . PHE A 1 131 ? 9.364   29.813 24.368  1.00 49.66  ? 131 PHE A CA  1 
ATOM   1083 C  C   . PHE A 1 131 ? 8.300   29.957 23.286  1.00 55.12  ? 131 PHE A C   1 
ATOM   1084 O  O   . PHE A 1 131 ? 8.595   30.460 22.194  1.00 50.39  ? 131 PHE A O   1 
ATOM   1085 C  CB  . PHE A 1 131 ? 9.917   28.388 24.413  1.00 44.24  ? 131 PHE A CB  1 
ATOM   1086 C  CG  . PHE A 1 131 ? 10.750  28.043 23.207  1.00 46.73  ? 131 PHE A CG  1 
ATOM   1087 C  CD1 . PHE A 1 131 ? 11.616  28.980 22.648  1.00 44.13  ? 131 PHE A CD1 1 
ATOM   1088 C  CD2 . PHE A 1 131 ? 10.687  26.769 22.649  1.00 43.21  ? 131 PHE A CD2 1 
ATOM   1089 C  CE1 . PHE A 1 131 ? 12.362  28.670 21.519  1.00 44.74  ? 131 PHE A CE1 1 
ATOM   1090 C  CE2 . PHE A 1 131 ? 11.429  26.470 21.520  1.00 47.70  ? 131 PHE A CE2 1 
ATOM   1091 C  CZ  . PHE A 1 131 ? 12.276  27.412 20.964  1.00 45.23  ? 131 PHE A CZ  1 
ATOM   1092 N  N   . ARG A 1 132 ? 7.059   29.558 23.616  1.00 48.13  ? 132 ARG A N   1 
ATOM   1093 C  CA  . ARG A 1 132 ? 5.979   29.605 22.651  1.00 39.90  ? 132 ARG A CA  1 
ATOM   1094 C  C   . ARG A 1 132 ? 5.858   31.048 22.198  1.00 42.61  ? 132 ARG A C   1 
ATOM   1095 O  O   . ARG A 1 132 ? 5.698   31.304 21.003  1.00 39.41  ? 132 ARG A O   1 
ATOM   1096 C  CB  . ARG A 1 132 ? 4.665   29.057 23.233  1.00 44.19  ? 132 ARG A CB  1 
ATOM   1097 C  CG  . ARG A 1 132 ? 3.516   29.001 22.232  1.00 49.77  ? 132 ARG A CG  1 
ATOM   1098 C  CD  . ARG A 1 132 ? 2.196   28.545 22.827  1.00 50.31  ? 132 ARG A CD  1 
ATOM   1099 N  NE  . ARG A 1 132 ? 1.767   29.475 23.872  1.00 50.86  ? 132 ARG A NE  1 
ATOM   1100 C  CZ  . ARG A 1 132 ? 1.613   29.141 25.150  1.00 46.49  ? 132 ARG A CZ  1 
ATOM   1101 N  NH1 . ARG A 1 132 ? 1.834   27.912 25.548  1.00 39.87  ? 132 ARG A NH1 1 
ATOM   1102 N  NH2 . ARG A 1 132 ? 1.254   30.045 26.034  1.00 51.80  ? 132 ARG A NH2 1 
ATOM   1103 N  N   . ARG A 1 133 ? 5.957   31.980 23.160  1.00 39.26  ? 133 ARG A N   1 
ATOM   1104 C  CA  . ARG A 1 133 ? 5.775   33.383 22.824  1.00 49.12  ? 133 ARG A CA  1 
ATOM   1105 C  C   . ARG A 1 133 ? 6.938   33.890 21.988  1.00 52.95  ? 133 ARG A C   1 
ATOM   1106 O  O   . ARG A 1 133 ? 6.744   34.709 21.103  1.00 61.81  ? 133 ARG A O   1 
ATOM   1107 C  CB  . ARG A 1 133 ? 5.563   34.207 24.089  1.00 55.81  ? 133 ARG A CB  1 
ATOM   1108 C  CG  . ARG A 1 133 ? 4.189   33.922 24.675  1.00 63.99  ? 133 ARG A CG  1 
ATOM   1109 C  CD  . ARG A 1 133 ? 3.926   34.632 25.960  1.00 63.20  ? 133 ARG A CD  1 
ATOM   1110 N  NE  . ARG A 1 133 ? 2.732   34.098 26.582  1.00 70.81  ? 133 ARG A NE  1 
ATOM   1111 C  CZ  . ARG A 1 133 ? 2.129   34.669 27.621  1.00 74.56  ? 133 ARG A CZ  1 
ATOM   1112 N  NH1 . ARG A 1 133 ? 2.616   35.787 28.129  1.00 64.87  ? 133 ARG A NH1 1 
ATOM   1113 N  NH2 . ARG A 1 133 ? 1.043   34.127 28.155  1.00 77.88  ? 133 ARG A NH2 1 
ATOM   1114 N  N   . LYS A 1 134 ? 8.136   33.377 22.255  1.00 48.62  ? 134 LYS A N   1 
ATOM   1115 C  CA  . LYS A 1 134 ? 9.303   33.758 21.481  1.00 49.38  ? 134 LYS A CA  1 
ATOM   1116 C  C   . LYS A 1 134 ? 9.117   33.293 20.043  1.00 46.53  ? 134 LYS A C   1 
ATOM   1117 O  O   . LYS A 1 134 ? 9.201   34.109 19.133  1.00 40.90  ? 134 LYS A O   1 
ATOM   1118 C  CB  . LYS A 1 134 ? 10.569  33.158 22.105  1.00 52.57  ? 134 LYS A CB  1 
ATOM   1119 C  CG  . LYS A 1 134 ? 11.003  33.787 23.412  1.00 54.43  ? 134 LYS A CG  1 
ATOM   1120 C  CD  . LYS A 1 134 ? 12.365  33.326 23.880  1.00 63.56  ? 134 LYS A CD  1 
ATOM   1121 C  CE  . LYS A 1 134 ? 12.963  34.309 24.854  1.00 60.78  ? 134 LYS A CE  1 
ATOM   1122 N  NZ  . LYS A 1 134 ? 12.122  34.382 26.064  1.00 72.71  ? 134 LYS A NZ  1 
ATOM   1123 N  N   . LEU A 1 135 ? 8.840   31.984 19.864  1.00 40.04  ? 135 LEU A N   1 
ATOM   1124 C  CA  . LEU A 1 135 ? 8.624   31.429 18.543  1.00 46.11  ? 135 LEU A CA  1 
ATOM   1125 C  C   . LEU A 1 135 ? 7.591   32.254 17.776  1.00 50.09  ? 135 LEU A C   1 
ATOM   1126 O  O   . LEU A 1 135 ? 7.724   32.468 16.577  1.00 51.09  ? 135 LEU A O   1 
ATOM   1127 C  CB  . LEU A 1 135 ? 8.172   29.971 18.636  1.00 45.46  ? 135 LEU A CB  1 
ATOM   1128 C  CG  . LEU A 1 135 ? 9.179   29.007 19.242  1.00 47.80  ? 135 LEU A CG  1 
ATOM   1129 C  CD1 . LEU A 1 135 ? 8.506   27.721 19.693  1.00 48.95  ? 135 LEU A CD1 1 
ATOM   1130 C  CD2 . LEU A 1 135 ? 10.299  28.707 18.251  1.00 49.99  ? 135 LEU A CD2 1 
ATOM   1131 N  N   . LEU A 1 136 ? 6.553   32.718 18.465  1.00 56.01  ? 136 LEU A N   1 
ATOM   1132 C  CA  . LEU A 1 136 ? 5.399   33.265 17.763  1.00 52.28  ? 136 LEU A CA  1 
ATOM   1133 C  C   . LEU A 1 136 ? 5.548   34.763 17.573  1.00 55.51  ? 136 LEU A C   1 
ATOM   1134 O  O   . LEU A 1 136 ? 4.785   35.357 16.832  1.00 62.80  ? 136 LEU A O   1 
ATOM   1135 C  CB  . LEU A 1 136 ? 4.120   32.864 18.501  1.00 51.32  ? 136 LEU A CB  1 
ATOM   1136 C  CG  . LEU A 1 136 ? 3.709   31.406 18.263  1.00 50.01  ? 136 LEU A CG  1 
ATOM   1137 C  CD1 . LEU A 1 136 ? 2.547   30.995 19.151  1.00 56.01  ? 136 LEU A CD1 1 
ATOM   1138 C  CD2 . LEU A 1 136 ? 3.346   31.198 16.803  1.00 50.33  ? 136 LEU A CD2 1 
ATOM   1139 N  N   . LYS A 1 137 ? 6.596   35.354 18.149  1.00 58.16  ? 137 LYS A N   1 
ATOM   1140 C  CA  . LYS A 1 137 ? 7.002   36.684 17.736  1.00 65.42  ? 137 LYS A CA  1 
ATOM   1141 C  C   . LYS A 1 137 ? 7.703   36.633 16.372  1.00 68.22  ? 137 LYS A C   1 
ATOM   1142 O  O   . LYS A 1 137 ? 7.833   37.687 15.771  1.00 66.74  ? 137 LYS A O   1 
ATOM   1143 C  CB  . LYS A 1 137 ? 7.893   37.344 18.792  1.00 69.28  ? 137 LYS A CB  1 
ATOM   1144 C  CG  . LYS A 1 137 ? 7.140   38.053 19.904  1.00 79.09  ? 137 LYS A CG  1 
ATOM   1145 C  CD  . LYS A 1 137 ? 8.020   38.557 21.010  1.00 88.53  ? 137 LYS A CD  1 
ATOM   1146 C  CE  . LYS A 1 137 ? 8.310   37.466 22.019  1.00 105.92 ? 137 LYS A CE  1 
ATOM   1147 N  NZ  . LYS A 1 137 ? 9.352   37.869 22.989  1.00 114.68 ? 137 LYS A NZ  1 
ATOM   1148 N  N   . ALA A 1 138 ? 8.123   35.448 15.869  1.00 78.49  ? 138 ALA A N   1 
ATOM   1149 C  CA  . ALA A 1 138 ? 8.970   35.335 14.672  1.00 85.16  ? 138 ALA A CA  1 
ATOM   1150 C  C   . ALA A 1 138 ? 8.183   35.133 13.364  1.00 98.29  ? 138 ALA A C   1 
ATOM   1151 O  O   . ALA A 1 138 ? 7.109   34.492 13.409  1.00 115.31 ? 138 ALA A O   1 
ATOM   1152 C  CB  . ALA A 1 138 ? 9.949   34.195 14.817  1.00 72.61  ? 138 ALA A CB  1 
ATOM   1153 O  OXT . ALA A 1 138 ? 8.725   35.562 12.311  1.00 96.80  ? 138 ALA A OXT 1 
ATOM   1154 N  N   . MET B 1 1   ? 6.283   37.099 8.426   1.00 87.90  ? 1   MET B N   1 
ATOM   1155 C  CA  . MET B 1 1   ? 6.024   36.271 9.639   1.00 96.24  ? 1   MET B CA  1 
ATOM   1156 C  C   . MET B 1 1   ? 6.179   34.782 9.309   1.00 90.47  ? 1   MET B C   1 
ATOM   1157 O  O   . MET B 1 1   ? 5.399   34.238 8.535   1.00 103.65 ? 1   MET B O   1 
ATOM   1158 C  CB  . MET B 1 1   ? 4.617   36.546 10.184  1.00 103.33 ? 1   MET B CB  1 
ATOM   1159 C  CG  . MET B 1 1   ? 4.580   37.635 11.249  1.00 104.91 ? 1   MET B CG  1 
ATOM   1160 S  SD  . MET B 1 1   ? 4.676   36.991 12.945  1.00 120.47 ? 1   MET B SD  1 
ATOM   1161 C  CE  . MET B 1 1   ? 3.169   36.022 13.060  1.00 127.12 ? 1   MET B CE  1 
ATOM   1162 N  N   . ALA B 1 2   ? 7.188   34.131 9.912   1.00 89.32  ? 2   ALA B N   1 
ATOM   1163 C  CA  . ALA B 1 2   ? 7.647   32.802 9.521   1.00 87.53  ? 2   ALA B CA  1 
ATOM   1164 C  C   . ALA B 1 2   ? 7.276   31.728 10.543  1.00 94.74  ? 2   ALA B C   1 
ATOM   1165 O  O   . ALA B 1 2   ? 7.771   30.604 10.445  1.00 92.96  ? 2   ALA B O   1 
ATOM   1166 C  CB  . ALA B 1 2   ? 9.154   32.820 9.379   1.00 99.96  ? 2   ALA B CB  1 
ATOM   1167 N  N   . SER B 1 3   ? 6.509   32.088 11.575  1.00 84.52  ? 3   SER B N   1 
ATOM   1168 C  CA  . SER B 1 3   ? 6.043   31.107 12.543  1.00 76.70  ? 3   SER B CA  1 
ATOM   1169 C  C   . SER B 1 3   ? 4.569   30.839 12.287  1.00 69.58  ? 3   SER B C   1 
ATOM   1170 O  O   . SER B 1 3   ? 3.859   31.707 11.788  1.00 67.38  ? 3   SER B O   1 
ATOM   1171 C  CB  . SER B 1 3   ? 6.229   31.570 13.956  1.00 74.01  ? 3   SER B CB  1 
ATOM   1172 O  OG  . SER B 1 3   ? 5.398   32.693 14.195  1.00 68.36  ? 3   SER B OG  1 
ATOM   1173 N  N   . SER B 1 4   ? 4.124   29.644 12.665  1.00 55.26  ? 4   SER B N   1 
ATOM   1174 C  CA  . SER B 1 4   ? 2.708   29.335 12.690  1.00 57.23  ? 4   SER B CA  1 
ATOM   1175 C  C   . SER B 1 4   ? 2.417   28.378 13.848  1.00 52.42  ? 4   SER B C   1 
ATOM   1176 O  O   . SER B 1 4   ? 3.331   27.779 14.386  1.00 47.49  ? 4   SER B O   1 
ATOM   1177 C  CB  . SER B 1 4   ? 2.311   28.758 11.373  1.00 49.86  ? 4   SER B CB  1 
ATOM   1178 O  OG  . SER B 1 4   ? 2.921   27.492 11.252  1.00 55.44  ? 4   SER B OG  1 
ATOM   1179 N  N   . CYS B 1 5   ? 1.135   28.214 14.182  1.00 51.77  ? 5   CYS B N   1 
ATOM   1180 C  CA  . CYS B 1 5   ? 0.676   27.564 15.402  1.00 51.74  ? 5   CYS B CA  1 
ATOM   1181 C  C   . CYS B 1 5   ? -0.602  26.796 15.085  1.00 51.87  ? 5   CYS B C   1 
ATOM   1182 O  O   . CYS B 1 5   ? -1.506  27.401 14.510  1.00 54.05  ? 5   CYS B O   1 
ATOM   1183 C  CB  . CYS B 1 5   ? 0.318   28.625 16.435  1.00 53.81  ? 5   CYS B CB  1 
ATOM   1184 S  SG  . CYS B 1 5   ? 0.000   27.919 18.069  1.00 77.17  ? 5   CYS B SG  1 
ATOM   1185 N  N   . ALA B 1 6   ? -0.666  25.490 15.377  1.00 46.65  ? 6   ALA B N   1 
ATOM   1186 C  CA  . ALA B 1 6   ? -1.948  24.795 15.420  1.00 53.00  ? 6   ALA B CA  1 
ATOM   1187 C  C   . ALA B 1 6   ? -2.277  24.464 16.888  1.00 54.16  ? 6   ALA B C   1 
ATOM   1188 O  O   . ALA B 1 6   ? -1.459  23.851 17.575  1.00 51.61  ? 6   ALA B O   1 
ATOM   1189 C  CB  . ALA B 1 6   ? -1.925  23.562 14.526  1.00 43.38  ? 6   ALA B CB  1 
ATOM   1190 N  N   . VAL B 1 7   ? -3.440  24.913 17.369  1.00 51.53  ? 7   VAL B N   1 
ATOM   1191 C  CA  . VAL B 1 7   ? -3.919  24.538 18.692  1.00 52.89  ? 7   VAL B CA  1 
ATOM   1192 C  C   . VAL B 1 7   ? -5.048  23.518 18.553  1.00 47.41  ? 7   VAL B C   1 
ATOM   1193 O  O   . VAL B 1 7   ? -5.988  23.721 17.783  1.00 54.11  ? 7   VAL B O   1 
ATOM   1194 C  CB  . VAL B 1 7   ? -4.371  25.765 19.494  1.00 53.26  ? 7   VAL B CB  1 
ATOM   1195 C  CG1 . VAL B 1 7   ? -4.883  25.351 20.860  1.00 49.85  ? 7   VAL B CG1 1 
ATOM   1196 C  CG2 . VAL B 1 7   ? -3.262  26.796 19.619  1.00 58.94  ? 7   VAL B CG2 1 
ATOM   1197 N  N   . GLN B 1 8   ? -4.883  22.399 19.263  1.00 44.04  ? 8   GLN B N   1 
ATOM   1198 C  CA  . GLN B 1 8   ? -5.882  21.340 19.371  1.00 47.07  ? 8   GLN B CA  1 
ATOM   1199 C  C   . GLN B 1 8   ? -6.534  21.358 20.752  1.00 48.60  ? 8   GLN B C   1 
ATOM   1200 O  O   . GLN B 1 8   ? -5.843  21.588 21.747  1.00 37.40  ? 8   GLN B O   1 
ATOM   1201 C  CB  . GLN B 1 8   ? -5.283  19.960 19.191  1.00 48.66  ? 8   GLN B CB  1 
ATOM   1202 C  CG  . GLN B 1 8   ? -4.757  19.721 17.794  1.00 65.93  ? 8   GLN B CG  1 
ATOM   1203 C  CD  . GLN B 1 8   ? -4.612  18.240 17.574  1.00 83.86  ? 8   GLN B CD  1 
ATOM   1204 O  OE1 . GLN B 1 8   ? -5.165  17.424 18.311  1.00 94.88  ? 8   GLN B OE1 1 
ATOM   1205 N  NE2 . GLN B 1 8   ? -3.884  17.881 16.532  1.00 100.19 ? 8   GLN B NE2 1 
ATOM   1206 N  N   . VAL B 1 9   ? -7.859  21.116 20.801  1.00 42.52  ? 9   VAL B N   1 
ATOM   1207 C  CA  . VAL B 1 9   ? -8.550  20.968 22.065  1.00 43.87  ? 9   VAL B CA  1 
ATOM   1208 C  C   . VAL B 1 9   ? -9.467  19.781 21.935  1.00 43.35  ? 9   VAL B C   1 
ATOM   1209 O  O   . VAL B 1 9   ? -10.131 19.583 20.910  1.00 45.13  ? 9   VAL B O   1 
ATOM   1210 C  CB  . VAL B 1 9   ? -9.328  22.202 22.572  1.00 51.47  ? 9   VAL B CB  1 
ATOM   1211 C  CG1 . VAL B 1 9   ? -8.422  23.331 23.022  1.00 60.92  ? 9   VAL B CG1 1 
ATOM   1212 C  CG2 . VAL B 1 9   ? -10.283 22.731 21.538  1.00 61.07  ? 9   VAL B CG2 1 
ATOM   1213 N  N   . LYS B 1 10  ? -9.463  19.011 23.017  1.00 45.86  ? 10  LYS B N   1 
ATOM   1214 C  CA  . LYS B 1 10  ? -10.238 17.793 23.088  1.00 44.48  ? 10  LYS B CA  1 
ATOM   1215 C  C   . LYS B 1 10  ? -11.521 18.083 23.859  1.00 42.51  ? 10  LYS B C   1 
ATOM   1216 O  O   . LYS B 1 10  ? -11.494 18.755 24.882  1.00 45.26  ? 10  LYS B O   1 
ATOM   1217 C  CB  . LYS B 1 10  ? -9.373  16.740 23.758  1.00 45.40  ? 10  LYS B CB  1 
ATOM   1218 C  CG  . LYS B 1 10  ? -8.222  16.225 22.913  1.00 51.64  ? 10  LYS B CG  1 
ATOM   1219 C  CD  . LYS B 1 10  ? -7.673  14.855 23.336  1.00 60.27  ? 10  LYS B CD  1 
ATOM   1220 C  CE  . LYS B 1 10  ? -7.285  14.761 24.800  1.00 73.88  ? 10  LYS B CE  1 
ATOM   1221 N  NZ  . LYS B 1 10  ? -6.462  15.917 25.249  1.00 75.60  ? 10  LYS B NZ  1 
ATOM   1222 N  N   . LEU B 1 11  ? -12.647 17.647 23.306  1.00 44.51  ? 11  LEU B N   1 
ATOM   1223 C  CA  . LEU B 1 11  ? -13.927 17.728 23.981  1.00 42.80  ? 11  LEU B CA  1 
ATOM   1224 C  C   . LEU B 1 11  ? -14.484 16.324 24.130  1.00 38.84  ? 11  LEU B C   1 
ATOM   1225 O  O   . LEU B 1 11  ? -14.264 15.454 23.290  1.00 38.01  ? 11  LEU B O   1 
ATOM   1226 C  CB  . LEU B 1 11  ? -14.921 18.553 23.175  1.00 40.22  ? 11  LEU B CB  1 
ATOM   1227 C  CG  . LEU B 1 11  ? -14.662 20.044 23.077  1.00 46.19  ? 11  LEU B CG  1 
ATOM   1228 C  CD1 . LEU B 1 11  ? -15.764 20.671 22.232  1.00 43.92  ? 11  LEU B CD1 1 
ATOM   1229 C  CD2 . LEU B 1 11  ? -14.612 20.666 24.445  1.00 43.39  ? 11  LEU B CD2 1 
ATOM   1230 N  N   . GLU B 1 12  ? -15.328 16.207 25.145  1.00 36.48  ? 12  GLU B N   1 
ATOM   1231 C  CA  . GLU B 1 12  ? -16.168 15.051 25.310  1.00 40.16  ? 12  GLU B CA  1 
ATOM   1232 C  C   . GLU B 1 12  ? -17.608 15.519 25.220  1.00 37.66  ? 12  GLU B C   1 
ATOM   1233 O  O   . GLU B 1 12  ? -18.012 16.443 25.924  1.00 37.76  ? 12  GLU B O   1 
ATOM   1234 C  CB  . GLU B 1 12  ? -15.902 14.453 26.685  1.00 41.17  ? 12  GLU B CB  1 
ATOM   1235 C  CG  . GLU B 1 12  ? -14.590 13.714 26.768  1.00 44.03  ? 12  GLU B CG  1 
ATOM   1236 C  CD  . GLU B 1 12  ? -14.425 12.976 28.095  1.00 53.12  ? 12  GLU B CD  1 
ATOM   1237 O  OE1 . GLU B 1 12  ? -15.164 13.307 29.070  1.00 57.52  ? 12  GLU B OE1 1 
ATOM   1238 O  OE2 . GLU B 1 12  ? -13.566 12.069 28.167  1.00 60.29  ? 12  GLU B OE2 1 
ATOM   1239 N  N   . LEU B 1 13  ? -18.340 14.879 24.319  1.00 37.12  ? 13  LEU B N   1 
ATOM   1240 C  CA  . LEU B 1 13  ? -19.783 14.953 24.264  1.00 34.80  ? 13  LEU B CA  1 
ATOM   1241 C  C   . LEU B 1 13  ? -20.276 13.604 24.751  1.00 42.45  ? 13  LEU B C   1 
ATOM   1242 O  O   . LEU B 1 13  ? -19.610 12.592 24.542  1.00 38.38  ? 13  LEU B O   1 
ATOM   1243 C  CB  . LEU B 1 13  ? -20.270 15.158 22.827  1.00 38.34  ? 13  LEU B CB  1 
ATOM   1244 C  CG  . LEU B 1 13  ? -20.138 16.546 22.228  1.00 47.02  ? 13  LEU B CG  1 
ATOM   1245 C  CD1 . LEU B 1 13  ? -18.690 17.019 22.263  1.00 51.26  ? 13  LEU B CD1 1 
ATOM   1246 C  CD2 . LEU B 1 13  ? -20.660 16.533 20.784  1.00 52.71  ? 13  LEU B CD2 1 
ATOM   1247 N  N   . GLY B 1 14  ? -21.475 13.574 25.312  1.00 36.99  ? 14  GLY B N   1 
ATOM   1248 C  CA  . GLY B 1 14  ? -22.021 12.284 25.696  1.00 37.45  ? 14  GLY B CA  1 
ATOM   1249 C  C   . GLY B 1 14  ? -23.432 12.404 26.234  1.00 32.79  ? 14  GLY B C   1 
ATOM   1250 O  O   . GLY B 1 14  ? -23.977 13.499 26.374  1.00 35.64  ? 14  GLY B O   1 
ATOM   1251 N  N   . HIS B 1 15  ? -23.977 11.260 26.607  1.00 34.50  ? 15  HIS B N   1 
ATOM   1252 C  CA  . HIS B 1 15  ? -25.279 11.238 27.243  1.00 37.05  ? 15  HIS B CA  1 
ATOM   1253 C  C   . HIS B 1 15  ? -25.472 9.942  28.012  1.00 36.79  ? 15  HIS B C   1 
ATOM   1254 O  O   . HIS B 1 15  ? -24.836 8.938  27.693  1.00 38.09  ? 15  HIS B O   1 
ATOM   1255 C  CB  . HIS B 1 15  ? -26.392 11.446 26.215  1.00 34.37  ? 15  HIS B CB  1 
ATOM   1256 C  CG  . HIS B 1 15  ? -26.785 10.258 25.433  1.00 36.81  ? 15  HIS B CG  1 
ATOM   1257 N  ND1 . HIS B 1 15  ? -25.976 9.670  24.487  1.00 33.91  ? 15  HIS B ND1 1 
ATOM   1258 C  CD2 . HIS B 1 15  ? -27.943 9.593  25.432  1.00 39.19  ? 15  HIS B CD2 1 
ATOM   1259 C  CE1 . HIS B 1 15  ? -26.657 8.692  23.914  1.00 38.22  ? 15  HIS B CE1 1 
ATOM   1260 N  NE2 . HIS B 1 15  ? -27.844 8.630  24.470  1.00 40.97  ? 15  HIS B NE2 1 
ATOM   1261 N  N   . ARG B 1 16  ? -26.362 10.043 28.999  1.00 39.06  ? 16  ARG B N   1 
ATOM   1262 C  CA  . ARG B 1 16  ? -26.861 8.923  29.779  1.00 47.83  ? 16  ARG B CA  1 
ATOM   1263 C  C   . ARG B 1 16  ? -28.359 8.852  29.511  1.00 48.24  ? 16  ARG B C   1 
ATOM   1264 O  O   . ARG B 1 16  ? -29.013 9.883  29.322  1.00 39.66  ? 16  ARG B O   1 
ATOM   1265 C  CB  . ARG B 1 16  ? -26.569 9.112  31.276  1.00 46.33  ? 16  ARG B CB  1 
ATOM   1266 C  CG  . ARG B 1 16  ? -25.110 8.865  31.652  1.00 61.58  ? 16  ARG B CG  1 
ATOM   1267 C  CD  . ARG B 1 16  ? -24.680 9.138  33.093  1.00 70.50  ? 16  ARG B CD  1 
ATOM   1268 N  NE  . ARG B 1 16  ? -23.833 10.327 33.301  1.00 84.17  ? 16  ARG B NE  1 
ATOM   1269 C  CZ  . ARG B 1 16  ? -22.505 10.389 33.118  1.00 93.91  ? 16  ARG B CZ  1 
ATOM   1270 N  NH1 . ARG B 1 16  ? -21.889 11.565 33.115  1.00 76.14  ? 16  ARG B NH1 1 
ATOM   1271 N  NH2 . ARG B 1 16  ? -21.789 9.292  32.904  1.00 95.03  ? 16  ARG B NH2 1 
ATOM   1272 N  N   . ALA B 1 17  ? -28.905 7.647  29.512  1.00 40.34  ? 17  ALA B N   1 
ATOM   1273 C  CA  . ALA B 1 17  ? -30.345 7.518  29.349  1.00 47.68  ? 17  ALA B CA  1 
ATOM   1274 C  C   . ALA B 1 17  ? -30.814 6.256  30.058  1.00 48.38  ? 17  ALA B C   1 
ATOM   1275 O  O   . ALA B 1 17  ? -30.236 5.185  29.884  1.00 47.23  ? 17  ALA B O   1 
ATOM   1276 C  CB  . ALA B 1 17  ? -30.750 7.473  27.895  1.00 40.74  ? 17  ALA B CB  1 
ATOM   1277 N  N   . GLN B 1 18  ? -31.918 6.405  30.777  1.00 52.61  ? 18  GLN B N   1 
ATOM   1278 C  CA  . GLN B 1 18  ? -32.393 5.388  31.691  1.00 64.70  ? 18  GLN B CA  1 
ATOM   1279 C  C   . GLN B 1 18  ? -33.902 5.270  31.539  1.00 55.29  ? 18  GLN B C   1 
ATOM   1280 O  O   . GLN B 1 18  ? -34.609 6.273  31.590  1.00 47.51  ? 18  GLN B O   1 
ATOM   1281 C  CB  . GLN B 1 18  ? -32.074 5.858  33.106  1.00 72.28  ? 18  GLN B CB  1 
ATOM   1282 C  CG  . GLN B 1 18  ? -32.427 4.850  34.176  1.00 88.63  ? 18  GLN B CG  1 
ATOM   1283 C  CD  . GLN B 1 18  ? -31.228 4.005  34.516  1.00 103.72 ? 18  GLN B CD  1 
ATOM   1284 O  OE1 . GLN B 1 18  ? -30.118 4.256  34.051  1.00 115.97 ? 18  GLN B OE1 1 
ATOM   1285 N  NE2 . GLN B 1 18  ? -31.439 3.002  35.349  1.00 106.25 ? 18  GLN B NE2 1 
ATOM   1286 N  N   . VAL B 1 19  ? -34.388 4.051  31.353  1.00 51.58  ? 19  VAL B N   1 
ATOM   1287 C  CA  . VAL B 1 19  ? -35.812 3.793  31.465  1.00 52.52  ? 19  VAL B CA  1 
ATOM   1288 C  C   . VAL B 1 19  ? -36.268 4.101  32.886  1.00 47.05  ? 19  VAL B C   1 
ATOM   1289 O  O   . VAL B 1 19  ? -35.696 3.576  33.819  1.00 48.25  ? 19  VAL B O   1 
ATOM   1290 C  CB  . VAL B 1 19  ? -36.135 2.337  31.102  1.00 64.38  ? 19  VAL B CB  1 
ATOM   1291 C  CG1 . VAL B 1 19  ? -37.613 2.060  31.317  1.00 67.73  ? 19  VAL B CG1 1 
ATOM   1292 C  CG2 . VAL B 1 19  ? -35.718 2.022  29.677  1.00 61.00  ? 19  VAL B CG2 1 
ATOM   1293 N  N   . ARG B 1 20  ? -37.249 4.991  33.034  1.00 46.21  ? 20  ARG B N   1 
ATOM   1294 C  CA  . ARG B 1 20  ? -37.821 5.317  34.331  1.00 57.89  ? 20  ARG B CA  1 
ATOM   1295 C  C   . ARG B 1 20  ? -38.598 4.153  34.939  1.00 66.92  ? 20  ARG B C   1 
ATOM   1296 O  O   . ARG B 1 20  ? -39.268 3.417  34.217  1.00 63.35  ? 20  ARG B O   1 
ATOM   1297 C  CB  . ARG B 1 20  ? -38.886 6.401  34.221  1.00 57.10  ? 20  ARG B CB  1 
ATOM   1298 C  CG  . ARG B 1 20  ? -38.334 7.733  33.794  1.00 60.55  ? 20  ARG B CG  1 
ATOM   1299 C  CD  . ARG B 1 20  ? -39.509 8.573  33.376  1.00 71.64  ? 20  ARG B CD  1 
ATOM   1300 N  NE  . ARG B 1 20  ? -40.345 8.872  34.520  1.00 70.63  ? 20  ARG B NE  1 
ATOM   1301 C  CZ  . ARG B 1 20  ? -40.103 9.820  35.415  1.00 77.82  ? 20  ARG B CZ  1 
ATOM   1302 N  NH1 . ARG B 1 20  ? -39.061 10.626 35.282  1.00 74.69  ? 20  ARG B NH1 1 
ATOM   1303 N  NH2 . ARG B 1 20  ? -40.936 9.970  36.435  1.00 79.00  ? 20  ARG B NH2 1 
ATOM   1304 N  N   . LYS B 1 21  ? -38.584 4.077  36.279  1.00 79.67  ? 21  LYS B N   1 
ATOM   1305 C  CA  . LYS B 1 21  ? -39.302 3.027  36.991  1.00 88.79  ? 21  LYS B CA  1 
ATOM   1306 C  C   . LYS B 1 21  ? -40.782 3.129  36.637  1.00 76.81  ? 21  LYS B C   1 
ATOM   1307 O  O   . LYS B 1 21  ? -41.439 2.118  36.440  1.00 71.08  ? 21  LYS B O   1 
ATOM   1308 C  CB  . LYS B 1 21  ? -39.085 3.090  38.510  1.00 98.85  ? 21  LYS B CB  1 
ATOM   1309 C  CG  . LYS B 1 21  ? -37.639 3.052  39.017  1.00 106.36 ? 21  LYS B CG  1 
ATOM   1310 C  CD  . LYS B 1 21  ? -36.575 2.505  38.050  1.00 113.66 ? 21  LYS B CD  1 
ATOM   1311 C  CE  . LYS B 1 21  ? -36.791 1.084  37.559  1.00 111.44 ? 21  LYS B CE  1 
ATOM   1312 N  NZ  . LYS B 1 21  ? -36.511 0.083  38.611  1.00 103.25 ? 21  LYS B NZ  1 
ATOM   1313 N  N   . LYS B 1 22  ? -41.266 4.357  36.464  1.00 69.50  ? 22  LYS B N   1 
ATOM   1314 C  CA  . LYS B 1 22  ? -42.643 4.564  36.077  1.00 73.18  ? 22  LYS B CA  1 
ATOM   1315 C  C   . LYS B 1 22  ? -42.741 5.736  35.104  1.00 66.79  ? 22  LYS B C   1 
ATOM   1316 O  O   . LYS B 1 22  ? -42.259 6.816  35.416  1.00 60.34  ? 22  LYS B O   1 
ATOM   1317 C  CB  . LYS B 1 22  ? -43.468 4.816  37.338  1.00 74.37  ? 22  LYS B CB  1 
ATOM   1318 C  CG  . LYS B 1 22  ? -44.955 4.601  37.117  1.00 84.47  ? 22  LYS B CG  1 
ATOM   1319 C  CD  . LYS B 1 22  ? -45.811 4.735  38.337  1.00 87.77  ? 22  LYS B CD  1 
ATOM   1320 C  CE  . LYS B 1 22  ? -47.217 5.116  37.930  1.00 96.35  ? 22  LYS B CE  1 
ATOM   1321 N  NZ  . LYS B 1 22  ? -47.978 5.627  39.086  1.00 106.79 ? 22  LYS B NZ  1 
ATOM   1322 N  N   . PRO B 1 23  ? -43.387 5.578  33.924  1.00 62.52  ? 23  PRO B N   1 
ATOM   1323 C  CA  . PRO B 1 23  ? -43.630 6.699  33.019  1.00 62.93  ? 23  PRO B CA  1 
ATOM   1324 C  C   . PRO B 1 23  ? -44.254 7.895  33.713  1.00 61.23  ? 23  PRO B C   1 
ATOM   1325 O  O   . PRO B 1 23  ? -44.965 7.759  34.686  1.00 69.55  ? 23  PRO B O   1 
ATOM   1326 C  CB  . PRO B 1 23  ? -44.643 6.197  31.990  1.00 63.08  ? 23  PRO B CB  1 
ATOM   1327 C  CG  . PRO B 1 23  ? -44.546 4.676  32.072  1.00 60.38  ? 23  PRO B CG  1 
ATOM   1328 C  CD  . PRO B 1 23  ? -43.905 4.315  33.391  1.00 57.60  ? 23  PRO B CD  1 
ATOM   1329 N  N   . THR B 1 24  ? -43.959 9.079  33.199  1.00 66.17  ? 24  THR B N   1 
ATOM   1330 C  CA  . THR B 1 24  ? -44.590 10.270 33.707  1.00 63.04  ? 24  THR B CA  1 
ATOM   1331 C  C   . THR B 1 24  ? -46.007 10.336 33.164  1.00 75.46  ? 24  THR B C   1 
ATOM   1332 O  O   . THR B 1 24  ? -46.418 9.470  32.386  1.00 65.01  ? 24  THR B O   1 
ATOM   1333 C  CB  . THR B 1 24  ? -43.820 11.523 33.292  1.00 62.81  ? 24  THR B CB  1 
ATOM   1334 O  OG1 . THR B 1 24  ? -44.051 11.658 31.891  1.00 58.12  ? 24  THR B OG1 1 
ATOM   1335 C  CG2 . THR B 1 24  ? -42.354 11.439 33.653  1.00 69.78  ? 24  THR B CG2 1 
ATOM   1336 N  N   . VAL B 1 25  ? -46.689 11.428 33.537  1.00 74.08  ? 25  VAL B N   1 
ATOM   1337 C  CA  . VAL B 1 25  ? -48.067 11.677 33.174  1.00 78.30  ? 25  VAL B CA  1 
ATOM   1338 C  C   . VAL B 1 25  ? -48.148 11.757 31.662  1.00 81.49  ? 25  VAL B C   1 
ATOM   1339 O  O   . VAL B 1 25  ? -49.087 11.243 31.070  1.00 76.15  ? 25  VAL B O   1 
ATOM   1340 C  CB  . VAL B 1 25  ? -48.582 12.993 33.792  1.00 80.94  ? 25  VAL B CB  1 
ATOM   1341 C  CG1 . VAL B 1 25  ? -50.039 13.258 33.432  1.00 82.90  ? 25  VAL B CG1 1 
ATOM   1342 C  CG2 . VAL B 1 25  ? -48.380 13.015 35.299  1.00 79.10  ? 25  VAL B CG2 1 
ATOM   1343 N  N   . GLU B 1 26  ? -47.188 12.464 31.057  1.00 78.61  ? 26  GLU B N   1 
ATOM   1344 C  CA  . GLU B 1 26  ? -47.326 12.832 29.657  1.00 63.66  ? 26  GLU B CA  1 
ATOM   1345 C  C   . GLU B 1 26  ? -46.937 11.636 28.787  1.00 49.16  ? 26  GLU B C   1 
ATOM   1346 O  O   . GLU B 1 26  ? -46.948 11.732 27.572  1.00 56.69  ? 26  GLU B O   1 
ATOM   1347 C  CB  . GLU B 1 26  ? -46.491 14.065 29.322  1.00 64.73  ? 26  GLU B CB  1 
ATOM   1348 C  CG  . GLU B 1 26  ? -46.576 15.182 30.349  1.00 68.77  ? 26  GLU B CG  1 
ATOM   1349 C  CD  . GLU B 1 26  ? -45.651 15.059 31.553  1.00 80.04  ? 26  GLU B CD  1 
ATOM   1350 O  OE1 . GLU B 1 26  ? -45.190 13.935 31.881  1.00 75.79  ? 26  GLU B OE1 1 
ATOM   1351 O  OE2 . GLU B 1 26  ? -45.367 16.100 32.150  1.00 85.16  ? 26  GLU B OE2 1 
ATOM   1352 N  N   . GLY B 1 27  ? -46.584 10.510 29.405  1.00 48.61  ? 27  GLY B N   1 
ATOM   1353 C  CA  . GLY B 1 27  ? -46.116 9.351  28.668  1.00 48.41  ? 27  GLY B CA  1 
ATOM   1354 C  C   . GLY B 1 27  ? -44.590 9.299  28.524  1.00 61.15  ? 27  GLY B C   1 
ATOM   1355 O  O   . GLY B 1 27  ? -44.125 8.420  27.801  1.00 57.16  ? 27  GLY B O   1 
ATOM   1356 N  N   . PHE B 1 28  ? -43.807 10.153 29.232  1.00 57.28  ? 28  PHE B N   1 
ATOM   1357 C  CA  . PHE B 1 28  ? -42.346 10.133 29.102  1.00 46.77  ? 28  PHE B CA  1 
ATOM   1358 C  C   . PHE B 1 28  ? -41.779 8.913  29.817  1.00 45.30  ? 28  PHE B C   1 
ATOM   1359 O  O   . PHE B 1 28  ? -42.000 8.736  31.021  1.00 52.99  ? 28  PHE B O   1 
ATOM   1360 C  CB  . PHE B 1 28  ? -41.721 11.407 29.676  1.00 46.89  ? 28  PHE B CB  1 
ATOM   1361 C  CG  . PHE B 1 28  ? -42.246 12.693 29.084  1.00 41.87  ? 28  PHE B CG  1 
ATOM   1362 C  CD1 . PHE B 1 28  ? -42.843 12.722 27.830  1.00 43.41  ? 28  PHE B CD1 1 
ATOM   1363 C  CD2 . PHE B 1 28  ? -42.264 13.860 29.840  1.00 44.21  ? 28  PHE B CD2 1 
ATOM   1364 C  CE1 . PHE B 1 28  ? -43.343 13.914 27.313  1.00 50.85  ? 28  PHE B CE1 1 
ATOM   1365 C  CE2 . PHE B 1 28  ? -42.773 15.050 29.328  1.00 44.81  ? 28  PHE B CE2 1 
ATOM   1366 C  CZ  . PHE B 1 28  ? -43.281 15.086 28.049  1.00 49.02  ? 28  PHE B CZ  1 
ATOM   1367 N  N   . THR B 1 29  ? -41.062 8.064  29.063  1.00 37.86  ? 29  THR B N   1 
ATOM   1368 C  CA  . THR B 1 29  ? -40.653 6.741  29.542  1.00 42.67  ? 29  THR B CA  1 
ATOM   1369 C  C   . THR B 1 29  ? -39.216 6.713  30.059  1.00 47.50  ? 29  THR B C   1 
ATOM   1370 O  O   . THR B 1 29  ? -38.775 5.732  30.677  1.00 48.31  ? 29  THR B O   1 
ATOM   1371 C  CB  . THR B 1 29  ? -40.759 5.728  28.396  1.00 48.28  ? 29  THR B CB  1 
ATOM   1372 O  OG1 . THR B 1 29  ? -40.028 6.274  27.291  1.00 47.17  ? 29  THR B OG1 1 
ATOM   1373 C  CG2 . THR B 1 29  ? -42.202 5.451  27.974  1.00 44.38  ? 29  THR B CG2 1 
ATOM   1374 N  N   . HIS B 1 30  ? -38.444 7.745  29.696  1.00 40.95  ? 30  HIS B N   1 
ATOM   1375 C  CA  . HIS B 1 30  ? -37.013 7.704  29.930  1.00 41.54  ? 30  HIS B CA  1 
ATOM   1376 C  C   . HIS B 1 30  ? -36.540 9.029  30.511  1.00 39.91  ? 30  HIS B C   1 
ATOM   1377 O  O   . HIS B 1 30  ? -37.094 10.093 30.207  1.00 40.85  ? 30  HIS B O   1 
ATOM   1378 C  CB  . HIS B 1 30  ? -36.217 7.512  28.638  1.00 41.42  ? 30  HIS B CB  1 
ATOM   1379 C  CG  . HIS B 1 30  ? -36.299 6.174  28.037  1.00 40.81  ? 30  HIS B CG  1 
ATOM   1380 N  ND1 . HIS B 1 30  ? -37.443 5.728  27.411  1.00 43.41  ? 30  HIS B ND1 1 
ATOM   1381 C  CD2 . HIS B 1 30  ? -35.365 5.244  27.850  1.00 42.76  ? 30  HIS B CD2 1 
ATOM   1382 C  CE1 . HIS B 1 30  ? -37.198 4.534  26.886  1.00 44.02  ? 30  HIS B CE1 1 
ATOM   1383 N  NE2 . HIS B 1 30  ? -35.945 4.217  27.157  1.00 48.35  ? 30  HIS B NE2 1 
ATOM   1384 N  N   . ASP B 1 31  ? -35.485 8.929  31.318  1.00 40.61  ? 31  ASP B N   1 
ATOM   1385 C  CA  . ASP B 1 31  ? -34.731 10.095 31.753  1.00 53.76  ? 31  ASP B CA  1 
ATOM   1386 C  C   . ASP B 1 31  ? -33.386 10.077 31.039  1.00 50.27  ? 31  ASP B C   1 
ATOM   1387 O  O   . ASP B 1 31  ? -32.719 9.030  30.948  1.00 39.22  ? 31  ASP B O   1 
ATOM   1388 C  CB  . ASP B 1 31  ? -34.482 10.084 33.266  1.00 51.38  ? 31  ASP B CB  1 
ATOM   1389 C  CG  . ASP B 1 31  ? -35.781 10.015 34.043  1.00 57.48  ? 31  ASP B CG  1 
ATOM   1390 O  OD1 . ASP B 1 31  ? -36.748 10.704 33.611  1.00 51.64  ? 31  ASP B OD1 1 
ATOM   1391 O  OD2 . ASP B 1 31  ? -35.819 9.265  35.050  1.00 56.51  ? 31  ASP B OD2 1 
ATOM   1392 N  N   . TRP B 1 32  ? -32.958 11.260 30.615  1.00 34.24  ? 32  TRP B N   1 
ATOM   1393 C  CA  . TRP B 1 32  ? -31.650 11.340 29.998  1.00 38.72  ? 32  TRP B CA  1 
ATOM   1394 C  C   . TRP B 1 32  ? -30.974 12.657 30.332  1.00 36.03  ? 32  TRP B C   1 
ATOM   1395 O  O   . TRP B 1 32  ? -31.606 13.656 30.735  1.00 39.52  ? 32  TRP B O   1 
ATOM   1396 C  CB  . TRP B 1 32  ? -31.723 11.147 28.478  1.00 37.06  ? 32  TRP B CB  1 
ATOM   1397 C  CG  . TRP B 1 32  ? -32.667 12.045 27.735  1.00 35.14  ? 32  TRP B CG  1 
ATOM   1398 C  CD1 . TRP B 1 32  ? -33.873 11.656 27.228  1.00 38.24  ? 32  TRP B CD1 1 
ATOM   1399 C  CD2 . TRP B 1 32  ? -32.472 13.408 27.301  1.00 39.23  ? 32  TRP B CD2 1 
ATOM   1400 N  NE1 . TRP B 1 32  ? -34.454 12.692 26.535  1.00 38.64  ? 32  TRP B NE1 1 
ATOM   1401 C  CE2 . TRP B 1 32  ? -33.622 13.774 26.561  1.00 40.00  ? 32  TRP B CE2 1 
ATOM   1402 C  CE3 . TRP B 1 32  ? -31.454 14.357 27.449  1.00 43.05  ? 32  TRP B CE3 1 
ATOM   1403 C  CZ2 . TRP B 1 32  ? -33.769 15.025 25.980  1.00 38.29  ? 32  TRP B CZ2 1 
ATOM   1404 C  CZ3 . TRP B 1 32  ? -31.600 15.599 26.869  1.00 41.32  ? 32  TRP B CZ3 1 
ATOM   1405 C  CH2 . TRP B 1 32  ? -32.740 15.921 26.127  1.00 43.52  ? 32  TRP B CH2 1 
ATOM   1406 N  N   . MET B 1 33  ? -29.670 12.603 30.119  1.00 35.51  ? 33  MET B N   1 
ATOM   1407 C  CA  . MET B 1 33  ? -28.830 13.779 30.259  1.00 44.52  ? 33  MET B CA  1 
ATOM   1408 C  C   . MET B 1 33  ? -27.789 13.769 29.137  1.00 36.26  ? 33  MET B C   1 
ATOM   1409 O  O   . MET B 1 33  ? -27.214 12.747 28.815  1.00 33.36  ? 33  MET B O   1 
ATOM   1410 C  CB  . MET B 1 33  ? -28.190 13.753 31.653  1.00 40.29  ? 33  MET B CB  1 
ATOM   1411 C  CG  . MET B 1 33  ? -27.320 14.943 31.922  1.00 56.97  ? 33  MET B CG  1 
ATOM   1412 S  SD  . MET B 1 33  ? -25.611 14.566 31.412  1.00 61.42  ? 33  MET B SD  1 
ATOM   1413 C  CE  . MET B 1 33  ? -25.019 13.665 32.842  1.00 60.02  ? 33  MET B CE  1 
ATOM   1414 N  N   . VAL B 1 34  ? -27.537 14.934 28.565  1.00 32.76  ? 34  VAL B N   1 
ATOM   1415 C  CA  . VAL B 1 34  ? -26.515 15.111 27.550  1.00 31.16  ? 34  VAL B CA  1 
ATOM   1416 C  C   . VAL B 1 34  ? -25.622 16.267 28.004  1.00 33.48  ? 34  VAL B C   1 
ATOM   1417 O  O   . VAL B 1 34  ? -26.103 17.245 28.594  1.00 29.54  ? 34  VAL B O   1 
ATOM   1418 C  CB  . VAL B 1 34  ? -27.167 15.399 26.164  1.00 31.91  ? 34  VAL B CB  1 
ATOM   1419 C  CG1 . VAL B 1 34  ? -27.924 16.695 26.119  1.00 31.46  ? 34  VAL B CG1 1 
ATOM   1420 C  CG2 . VAL B 1 34  ? -26.177 15.398 25.036  1.00 34.23  ? 34  VAL B CG2 1 
ATOM   1421 N  N   . PHE B 1 35  ? -24.362 16.180 27.600  1.00 31.39  ? 35  PHE B N   1 
ATOM   1422 C  CA  . PHE B 1 35  ? -23.338 17.067 28.108  1.00 36.96  ? 35  PHE B CA  1 
ATOM   1423 C  C   . PHE B 1 35  ? -22.234 17.240 27.072  1.00 35.18  ? 35  PHE B C   1 
ATOM   1424 O  O   . PHE B 1 35  ? -22.010 16.404 26.208  1.00 30.65  ? 35  PHE B O   1 
ATOM   1425 C  CB  . PHE B 1 35  ? -22.777 16.474 29.402  1.00 35.65  ? 35  PHE B CB  1 
ATOM   1426 C  CG  . PHE B 1 35  ? -22.057 15.152 29.219  1.00 34.49  ? 35  PHE B CG  1 
ATOM   1427 C  CD1 . PHE B 1 35  ? -20.742 15.120 28.769  1.00 35.40  ? 35  PHE B CD1 1 
ATOM   1428 C  CD2 . PHE B 1 35  ? -22.695 13.943 29.461  1.00 36.83  ? 35  PHE B CD2 1 
ATOM   1429 C  CE1 . PHE B 1 35  ? -20.071 13.917 28.619  1.00 39.63  ? 35  PHE B CE1 1 
ATOM   1430 C  CE2 . PHE B 1 35  ? -22.034 12.724 29.278  1.00 40.04  ? 35  PHE B CE2 1 
ATOM   1431 C  CZ  . PHE B 1 35  ? -20.724 12.712 28.863  1.00 41.52  ? 35  PHE B CZ  1 
ATOM   1432 N  N   . VAL B 1 36  ? -21.605 18.392 27.187  1.00 34.01  ? 36  VAL B N   1 
ATOM   1433 C  CA  . VAL B 1 36  ? -20.315 18.721 26.622  1.00 32.45  ? 36  VAL B CA  1 
ATOM   1434 C  C   . VAL B 1 36  ? -19.378 19.082 27.777  1.00 32.50  ? 36  VAL B C   1 
ATOM   1435 O  O   . VAL B 1 36  ? -19.713 19.906 28.658  1.00 31.45  ? 36  VAL B O   1 
ATOM   1436 C  CB  . VAL B 1 36  ? -20.425 19.937 25.693  1.00 32.23  ? 36  VAL B CB  1 
ATOM   1437 C  CG1 . VAL B 1 36  ? -19.045 20.405 25.271  1.00 32.38  ? 36  VAL B CG1 1 
ATOM   1438 C  CG2 . VAL B 1 36  ? -21.283 19.625 24.485  1.00 36.51  ? 36  VAL B CG2 1 
ATOM   1439 N  N   . ARG B 1 37  ? -18.181 18.503 27.722  1.00 29.76  ? 37  ARG B N   1 
ATOM   1440 C  CA  . ARG B 1 37  ? -17.153 18.900 28.671  1.00 35.40  ? 37  ARG B CA  1 
ATOM   1441 C  C   . ARG B 1 37  ? -15.780 18.619 28.107  1.00 30.58  ? 37  ARG B C   1 
ATOM   1442 O  O   . ARG B 1 37  ? -15.607 18.078 27.002  1.00 33.65  ? 37  ARG B O   1 
ATOM   1443 C  CB  . ARG B 1 37  ? -17.275 18.137 29.990  1.00 31.23  ? 37  ARG B CB  1 
ATOM   1444 C  CG  . ARG B 1 37  ? -17.064 16.647 29.755  1.00 39.19  ? 37  ARG B CG  1 
ATOM   1445 C  CD  . ARG B 1 37  ? -17.537 15.799 30.904  1.00 40.24  ? 37  ARG B CD  1 
ATOM   1446 N  NE  . ARG B 1 37  ? -17.341 14.397 30.538  1.00 46.86  ? 37  ARG B NE  1 
ATOM   1447 C  CZ  . ARG B 1 37  ? -17.981 13.383 31.125  1.00 45.71  ? 37  ARG B CZ  1 
ATOM   1448 N  NH1 . ARG B 1 37  ? -17.556 12.148 30.936  1.00 46.52  ? 37  ARG B NH1 1 
ATOM   1449 N  NH2 . ARG B 1 37  ? -19.026 13.602 31.913  1.00 46.83  ? 37  ARG B NH2 1 
ATOM   1450 N  N   . GLY B 1 38  ? -14.811 19.023 28.931  1.00 31.08  ? 38  GLY B N   1 
ATOM   1451 C  CA  . GLY B 1 38  ? -13.407 18.765 28.713  1.00 31.11  ? 38  GLY B CA  1 
ATOM   1452 C  C   . GLY B 1 38  ? -13.087 17.351 29.219  1.00 32.32  ? 38  GLY B C   1 
ATOM   1453 O  O   . GLY B 1 38  ? -13.612 16.944 30.213  1.00 30.87  ? 38  GLY B O   1 
ATOM   1454 N  N   . PRO B 1 39  ? -12.148 16.606 28.624  1.00 35.23  ? 39  PRO B N   1 
ATOM   1455 C  CA  . PRO B 1 39  ? -11.674 15.371 29.254  1.00 39.60  ? 39  PRO B CA  1 
ATOM   1456 C  C   . PRO B 1 39  ? -11.008 15.682 30.596  1.00 40.59  ? 39  PRO B C   1 
ATOM   1457 O  O   . PRO B 1 39  ? -10.478 16.771 30.845  1.00 31.99  ? 39  PRO B O   1 
ATOM   1458 C  CB  . PRO B 1 39  ? -10.694 14.783 28.215  1.00 42.82  ? 39  PRO B CB  1 
ATOM   1459 C  CG  . PRO B 1 39  ? -10.179 16.041 27.495  1.00 41.38  ? 39  PRO B CG  1 
ATOM   1460 C  CD  . PRO B 1 39  ? -11.406 16.948 27.397  1.00 37.51  ? 39  PRO B CD  1 
ATOM   1461 N  N   . GLU B 1 40  ? -11.129 14.703 31.488  1.00 43.53  ? 40  GLU B N   1 
ATOM   1462 C  CA  . GLU B 1 40  ? -10.451 14.681 32.769  1.00 49.06  ? 40  GLU B CA  1 
ATOM   1463 C  C   . GLU B 1 40  ? -10.571 15.997 33.520  1.00 37.94  ? 40  GLU B C   1 
ATOM   1464 O  O   . GLU B 1 40  ? -9.585  16.478 33.969  1.00 39.39  ? 40  GLU B O   1 
ATOM   1465 C  CB  . GLU B 1 40  ? -8.997  14.302 32.523  1.00 50.45  ? 40  GLU B CB  1 
ATOM   1466 C  CG  . GLU B 1 40  ? -8.887  12.915 31.884  1.00 59.40  ? 40  GLU B CG  1 
ATOM   1467 C  CD  . GLU B 1 40  ? -7.499  12.713 31.317  1.00 71.50  ? 40  GLU B CD  1 
ATOM   1468 O  OE1 . GLU B 1 40  ? -7.345  12.917 30.102  1.00 87.41  ? 40  GLU B OE1 1 
ATOM   1469 O  OE2 . GLU B 1 40  ? -6.571  12.471 32.120  1.00 77.25  ? 40  GLU B OE2 1 
ATOM   1470 N  N   . HIS B 1 41  ? -11.785 16.490 33.703  1.00 33.78  ? 41  HIS B N   1 
ATOM   1471 C  CA  . HIS B 1 41  ? -12.145 17.627 34.540  1.00 42.25  ? 41  HIS B CA  1 
ATOM   1472 C  C   . HIS B 1 41  ? -11.424 18.897 34.104  1.00 37.32  ? 41  HIS B C   1 
ATOM   1473 O  O   . HIS B 1 41  ? -11.402 19.853 34.871  1.00 46.37  ? 41  HIS B O   1 
ATOM   1474 C  CB  . HIS B 1 41  ? -11.971 17.324 36.035  1.00 41.54  ? 41  HIS B CB  1 
ATOM   1475 C  CG  . HIS B 1 41  ? -12.745 16.130 36.419  1.00 45.19  ? 41  HIS B CG  1 
ATOM   1476 N  ND1 . HIS B 1 41  ? -14.070 16.238 36.795  1.00 45.03  ? 41  HIS B ND1 1 
ATOM   1477 C  CD2 . HIS B 1 41  ? -12.458 14.805 36.293  1.00 40.49  ? 41  HIS B CD2 1 
ATOM   1478 C  CE1 . HIS B 1 41  ? -14.544 15.012 36.993  1.00 42.11  ? 41  HIS B CE1 1 
ATOM   1479 N  NE2 . HIS B 1 41  ? -13.585 14.132 36.702  1.00 47.29  ? 41  HIS B NE2 1 
ATOM   1480 N  N   . SER B 1 42  ? -10.924 18.915 32.870  1.00 36.50  ? 42  SER B N   1 
ATOM   1481 C  CA  . SER B 1 42  ? -10.344 20.114 32.306  1.00 36.91  ? 42  SER B CA  1 
ATOM   1482 C  C   . SER B 1 42  ? -11.425 21.173 32.176  1.00 33.02  ? 42  SER B C   1 
ATOM   1483 O  O   . SER B 1 42  ? -12.608 20.912 32.188  1.00 35.11  ? 42  SER B O   1 
ATOM   1484 C  CB  . SER B 1 42  ? -9.671  19.836 30.991  1.00 39.40  ? 42  SER B CB  1 
ATOM   1485 O  OG  . SER B 1 42  ? -10.600 19.327 30.042  1.00 40.46  ? 42  SER B OG  1 
ATOM   1486 N  N   . ASN B 1 43  ? -10.976 22.407 32.196  1.00 36.93  ? 43  ASN B N   1 
ATOM   1487 C  CA  . ASN B 1 43  ? -11.826 23.573 32.211  1.00 32.47  ? 43  ASN B CA  1 
ATOM   1488 C  C   . ASN B 1 43  ? -11.875 24.184 30.804  1.00 33.15  ? 43  ASN B C   1 
ATOM   1489 O  O   . ASN B 1 43  ? -10.983 24.922 30.417  1.00 37.14  ? 43  ASN B O   1 
ATOM   1490 C  CB  . ASN B 1 43  ? -11.203 24.523 33.223  1.00 32.16  ? 43  ASN B CB  1 
ATOM   1491 C  CG  . ASN B 1 43  ? -12.009 25.775 33.404  1.00 38.61  ? 43  ASN B CG  1 
ATOM   1492 O  OD1 . ASN B 1 43  ? -12.880 26.065 32.594  1.00 40.20  ? 43  ASN B OD1 1 
ATOM   1493 N  ND2 . ASN B 1 43  ? -11.710 26.517 34.458  1.00 39.68  ? 43  ASN B ND2 1 
ATOM   1494 N  N   . ILE B 1 44  ? -12.955 23.950 30.063  1.00 32.50  ? 44  ILE B N   1 
ATOM   1495 C  CA  . ILE B 1 44  ? -13.096 24.452 28.698  1.00 31.75  ? 44  ILE B CA  1 
ATOM   1496 C  C   . ILE B 1 44  ? -13.715 25.845 28.725  1.00 32.13  ? 44  ILE B C   1 
ATOM   1497 O  O   . ILE B 1 44  ? -13.702 26.585 27.744  1.00 33.56  ? 44  ILE B O   1 
ATOM   1498 C  CB  . ILE B 1 44  ? -13.900 23.482 27.831  1.00 34.43  ? 44  ILE B CB  1 
ATOM   1499 C  CG1 . ILE B 1 44  ? -15.301 23.223 28.370  1.00 31.05  ? 44  ILE B CG1 1 
ATOM   1500 C  CG2 . ILE B 1 44  ? -13.136 22.169 27.659  1.00 34.08  ? 44  ILE B CG2 1 
ATOM   1501 C  CD1 . ILE B 1 44  ? -16.204 22.579 27.328  1.00 35.63  ? 44  ILE B CD1 1 
ATOM   1502 N  N   . GLN B 1 45  ? -14.145 26.258 29.898  1.00 29.54  ? 45  GLN B N   1 
ATOM   1503 C  CA  . GLN B 1 45  ? -14.826 27.541 30.000  1.00 34.30  ? 45  GLN B CA  1 
ATOM   1504 C  C   . GLN B 1 45  ? -13.881 28.688 29.676  1.00 33.82  ? 45  GLN B C   1 
ATOM   1505 O  O   . GLN B 1 45  ? -14.331 29.761 29.295  1.00 43.22  ? 45  GLN B O   1 
ATOM   1506 C  CB  . GLN B 1 45  ? -15.433 27.736 31.389  1.00 31.47  ? 45  GLN B CB  1 
ATOM   1507 C  CG  . GLN B 1 45  ? -16.063 29.109 31.516  1.00 34.35  ? 45  GLN B CG  1 
ATOM   1508 C  CD  . GLN B 1 45  ? -16.913 29.237 32.762  1.00 42.82  ? 45  GLN B CD  1 
ATOM   1509 O  OE1 . GLN B 1 45  ? -16.594 28.680 33.803  1.00 40.19  ? 45  GLN B OE1 1 
ATOM   1510 N  NE2 . GLN B 1 45  ? -17.982 30.015 32.695  1.00 42.32  ? 45  GLN B NE2 1 
ATOM   1511 N  N   . HIS B 1 46  ? -12.570 28.453 29.812  1.00 39.69  ? 46  HIS B N   1 
ATOM   1512 C  CA  . HIS B 1 46  ? -11.545 29.402 29.409  1.00 40.10  ? 46  HIS B CA  1 
ATOM   1513 C  C   . HIS B 1 46  ? -11.752 29.878 27.969  1.00 43.22  ? 46  HIS B C   1 
ATOM   1514 O  O   . HIS B 1 46  ? -11.560 31.054 27.665  1.00 35.86  ? 46  HIS B O   1 
ATOM   1515 C  CB  . HIS B 1 46  ? -10.165 28.772 29.567  1.00 39.37  ? 46  HIS B CB  1 
ATOM   1516 C  CG  . HIS B 1 46  ? -9.734  28.586 30.973  1.00 40.62  ? 46  HIS B CG  1 
ATOM   1517 N  ND1 . HIS B 1 46  ? -9.675  29.608 31.897  1.00 40.94  ? 46  HIS B ND1 1 
ATOM   1518 C  CD2 . HIS B 1 46  ? -9.298  27.449 31.621  1.00 39.27  ? 46  HIS B CD2 1 
ATOM   1519 C  CE1 . HIS B 1 46  ? -9.249  29.103 33.056  1.00 45.37  ? 46  HIS B CE1 1 
ATOM   1520 N  NE2 . HIS B 1 46  ? -9.001  27.802 32.901  1.00 40.53  ? 46  HIS B NE2 1 
ATOM   1521 N  N   . PHE B 1 47  ? -12.191 28.990 27.076  1.00 38.77  ? 47  PHE B N   1 
ATOM   1522 C  CA  . PHE B 1 47  ? -12.357 29.416 25.684  1.00 42.27  ? 47  PHE B CA  1 
ATOM   1523 C  C   . PHE B 1 47  ? -13.786 29.227 25.173  1.00 39.94  ? 47  PHE B C   1 
ATOM   1524 O  O   . PHE B 1 47  ? -14.083 29.509 24.010  1.00 35.37  ? 47  PHE B O   1 
ATOM   1525 C  CB  . PHE B 1 47  ? -11.407 28.629 24.772  1.00 42.64  ? 47  PHE B CB  1 
ATOM   1526 C  CG  . PHE B 1 47  ? -11.629 27.140 24.732  1.00 37.06  ? 47  PHE B CG  1 
ATOM   1527 C  CD1 . PHE B 1 47  ? -11.083 26.298 25.701  1.00 47.30  ? 47  PHE B CD1 1 
ATOM   1528 C  CD2 . PHE B 1 47  ? -12.383 26.567 23.728  1.00 39.23  ? 47  PHE B CD2 1 
ATOM   1529 C  CE1 . PHE B 1 47  ? -11.290 24.916 25.658  1.00 41.52  ? 47  PHE B CE1 1 
ATOM   1530 C  CE2 . PHE B 1 47  ? -12.585 25.193 23.692  1.00 34.69  ? 47  PHE B CE2 1 
ATOM   1531 C  CZ  . PHE B 1 47  ? -12.049 24.371 24.667  1.00 38.68  ? 47  PHE B CZ  1 
ATOM   1532 N  N   . VAL B 1 48  ? -14.651 28.641 25.999  1.00 38.72  ? 48  VAL B N   1 
ATOM   1533 C  CA  . VAL B 1 48  ? -16.026 28.430 25.581  1.00 38.48  ? 48  VAL B CA  1 
ATOM   1534 C  C   . VAL B 1 48  ? -16.909 29.535 26.152  1.00 40.17  ? 48  VAL B C   1 
ATOM   1535 O  O   . VAL B 1 48  ? -16.940 29.737 27.365  1.00 33.06  ? 48  VAL B O   1 
ATOM   1536 C  CB  . VAL B 1 48  ? -16.535 27.042 25.995  1.00 35.99  ? 48  VAL B CB  1 
ATOM   1537 C  CG1 . VAL B 1 48  ? -18.028 26.950 25.852  1.00 36.77  ? 48  VAL B CG1 1 
ATOM   1538 C  CG2 . VAL B 1 48  ? -15.859 25.916 25.199  1.00 38.66  ? 48  VAL B CG2 1 
ATOM   1539 N  N   . GLU B 1 49  ? -17.640 30.215 25.254  1.00 38.19  ? 49  GLU B N   1 
ATOM   1540 C  CA  . GLU B 1 49  ? -18.596 31.242 25.637  1.00 41.44  ? 49  GLU B CA  1 
ATOM   1541 C  C   . GLU B 1 49  ? -19.884 30.585 26.150  1.00 35.35  ? 49  GLU B C   1 
ATOM   1542 O  O   . GLU B 1 49  ? -20.418 30.927 27.200  1.00 35.01  ? 49  GLU B O   1 
ATOM   1543 C  CB  . GLU B 1 49  ? -18.936 32.135 24.435  1.00 43.04  ? 49  GLU B CB  1 
ATOM   1544 C  CG  . GLU B 1 49  ? -19.901 33.256 24.803  1.00 50.72  ? 49  GLU B CG  1 
ATOM   1545 C  CD  . GLU B 1 49  ? -20.463 33.974 23.581  1.00 67.48  ? 49  GLU B CD  1 
ATOM   1546 O  OE1 . GLU B 1 49  ? -19.686 34.341 22.628  1.00 63.81  ? 49  GLU B OE1 1 
ATOM   1547 O  OE2 . GLU B 1 49  ? -21.688 34.164 23.569  1.00 72.04  ? 49  GLU B OE2 1 
ATOM   1548 N  N   . LYS B 1 50  ? -20.392 29.618 25.376  1.00 32.86  ? 50  LYS B N   1 
ATOM   1549 C  CA  . LYS B 1 50  ? -21.636 28.958 25.705  1.00 33.98  ? 50  LYS B CA  1 
ATOM   1550 C  C   . LYS B 1 50  ? -21.771 27.695 24.878  1.00 31.47  ? 50  LYS B C   1 
ATOM   1551 O  O   . LYS B 1 50  ? -21.084 27.536 23.867  1.00 29.11  ? 50  LYS B O   1 
ATOM   1552 C  CB  . LYS B 1 50  ? -22.834 29.854 25.437  1.00 39.40  ? 50  LYS B CB  1 
ATOM   1553 C  CG  . LYS B 1 50  ? -23.007 30.266 23.991  1.00 41.24  ? 50  LYS B CG  1 
ATOM   1554 C  CD  . LYS B 1 50  ? -24.180 31.193 23.778  1.00 42.44  ? 50  LYS B CD  1 
ATOM   1555 C  CE  . LYS B 1 50  ? -24.079 31.890 22.429  1.00 44.87  ? 50  LYS B CE  1 
ATOM   1556 N  NZ  . LYS B 1 50  ? -25.220 32.811 22.280  1.00 49.86  ? 50  LYS B NZ  1 
ATOM   1557 N  N   . VAL B 1 51  ? -22.651 26.818 25.366  1.00 34.28  ? 51  VAL B N   1 
ATOM   1558 C  CA  . VAL B 1 51  ? -23.086 25.649 24.617  1.00 35.34  ? 51  VAL B CA  1 
ATOM   1559 C  C   . VAL B 1 51  ? -24.593 25.762 24.456  1.00 32.11  ? 51  VAL B C   1 
ATOM   1560 O  O   . VAL B 1 51  ? -25.314 26.175 25.375  1.00 34.66  ? 51  VAL B O   1 
ATOM   1561 C  CB  . VAL B 1 51  ? -22.671 24.333 25.297  1.00 32.72  ? 51  VAL B CB  1 
ATOM   1562 C  CG1 . VAL B 1 51  ? -23.117 23.106 24.534  1.00 34.24  ? 51  VAL B CG1 1 
ATOM   1563 C  CG2 . VAL B 1 51  ? -21.185 24.282 25.530  1.00 30.12  ? 51  VAL B CG2 1 
ATOM   1564 N  N   . VAL B 1 52  ? -25.033 25.541 23.223  1.00 30.27  ? 52  VAL B N   1 
ATOM   1565 C  CA  . VAL B 1 52  ? -26.451 25.579 22.903  1.00 29.27  ? 52  VAL B CA  1 
ATOM   1566 C  C   . VAL B 1 52  ? -26.822 24.159 22.494  1.00 30.63  ? 52  VAL B C   1 
ATOM   1567 O  O   . VAL B 1 52  ? -26.209 23.615 21.571  1.00 30.81  ? 52  VAL B O   1 
ATOM   1568 C  CB  . VAL B 1 52  ? -26.753 26.555 21.758  1.00 29.64  ? 52  VAL B CB  1 
ATOM   1569 C  CG1 . VAL B 1 52  ? -28.236 26.546 21.426  1.00 28.45  ? 52  VAL B CG1 1 
ATOM   1570 C  CG2 . VAL B 1 52  ? -26.254 27.969 22.069  1.00 30.00  ? 52  VAL B CG2 1 
ATOM   1571 N  N   . PHE B 1 53  ? -27.806 23.588 23.189  1.00 30.78  ? 53  PHE B N   1 
ATOM   1572 C  CA  . PHE B 1 53  ? -28.336 22.285 22.848  1.00 31.59  ? 53  PHE B CA  1 
ATOM   1573 C  C   . PHE B 1 53  ? -29.673 22.531 22.173  1.00 34.30  ? 53  PHE B C   1 
ATOM   1574 O  O   . PHE B 1 53  ? -30.558 23.128 22.788  1.00 35.79  ? 53  PHE B O   1 
ATOM   1575 C  CB  . PHE B 1 53  ? -28.524 21.436 24.102  1.00 29.31  ? 53  PHE B CB  1 
ATOM   1576 C  CG  . PHE B 1 53  ? -27.262 21.156 24.861  1.00 34.24  ? 53  PHE B CG  1 
ATOM   1577 C  CD1 . PHE B 1 53  ? -26.772 22.082 25.779  1.00 36.45  ? 53  PHE B CD1 1 
ATOM   1578 C  CD2 . PHE B 1 53  ? -26.600 19.952 24.711  1.00 33.13  ? 53  PHE B CD2 1 
ATOM   1579 C  CE1 . PHE B 1 53  ? -25.621 21.811 26.498  1.00 32.20  ? 53  PHE B CE1 1 
ATOM   1580 C  CE2 . PHE B 1 53  ? -25.412 19.708 25.395  1.00 37.28  ? 53  PHE B CE2 1 
ATOM   1581 C  CZ  . PHE B 1 53  ? -24.936 20.636 26.295  1.00 37.23  ? 53  PHE B CZ  1 
ATOM   1582 N  N   . HIS B 1 54  ? -29.819 22.058 20.936  1.00 35.50  ? 54  HIS B N   1 
ATOM   1583 C  CA  . HIS B 1 54  ? -31.085 22.209 20.221  1.00 33.69  ? 54  HIS B CA  1 
ATOM   1584 C  C   . HIS B 1 54  ? -31.881 20.927 20.323  1.00 32.30  ? 54  HIS B C   1 
ATOM   1585 O  O   . HIS B 1 54  ? -31.675 19.999 19.571  1.00 39.71  ? 54  HIS B O   1 
ATOM   1586 C  CB  . HIS B 1 54  ? -30.894 22.570 18.745  1.00 35.24  ? 54  HIS B CB  1 
ATOM   1587 C  CG  . HIS B 1 54  ? -30.123 23.815 18.517  1.00 34.67  ? 54  HIS B CG  1 
ATOM   1588 N  ND1 . HIS B 1 54  ? -30.739 25.012 18.220  1.00 35.99  ? 54  HIS B ND1 1 
ATOM   1589 C  CD2 . HIS B 1 54  ? -28.790 24.061 18.594  1.00 39.30  ? 54  HIS B CD2 1 
ATOM   1590 C  CE1 . HIS B 1 54  ? -29.795 25.968 18.077  1.00 36.80  ? 54  HIS B CE1 1 
ATOM   1591 N  NE2 . HIS B 1 54  ? -28.595 25.409 18.292  1.00 36.10  ? 54  HIS B NE2 1 
ATOM   1592 N  N   . LEU B 1 55  ? -32.828 20.923 21.240  1.00 33.54  ? 55  LEU B N   1 
ATOM   1593 C  CA  . LEU B 1 55  ? -33.653 19.776 21.542  1.00 35.98  ? 55  LEU B CA  1 
ATOM   1594 C  C   . LEU B 1 55  ? -34.691 19.614 20.446  1.00 34.95  ? 55  LEU B C   1 
ATOM   1595 O  O   . LEU B 1 55  ? -34.979 20.556 19.725  1.00 25.11  ? 55  LEU B O   1 
ATOM   1596 C  CB  . LEU B 1 55  ? -34.329 20.031 22.888  1.00 42.50  ? 55  LEU B CB  1 
ATOM   1597 C  CG  . LEU B 1 55  ? -33.695 19.393 24.116  1.00 48.60  ? 55  LEU B CG  1 
ATOM   1598 C  CD1 . LEU B 1 55  ? -32.223 19.715 24.220  1.00 48.07  ? 55  LEU B CD1 1 
ATOM   1599 C  CD2 . LEU B 1 55  ? -34.474 19.798 25.369  1.00 43.57  ? 55  LEU B CD2 1 
ATOM   1600 N  N   . HIS B 1 56  ? -35.232 18.395 20.284  1.00 33.76  ? 56  HIS B N   1 
ATOM   1601 C  CA  . HIS B 1 56  ? -36.268 18.210 19.283  1.00 35.65  ? 56  HIS B CA  1 
ATOM   1602 C  C   . HIS B 1 56  ? -37.397 19.198 19.561  1.00 39.67  ? 56  HIS B C   1 
ATOM   1603 O  O   . HIS B 1 56  ? -37.628 19.586 20.728  1.00 38.76  ? 56  HIS B O   1 
ATOM   1604 C  CB  . HIS B 1 56  ? -36.782 16.791 19.309  1.00 37.93  ? 56  HIS B CB  1 
ATOM   1605 C  CG  . HIS B 1 56  ? -37.698 16.442 18.191  1.00 46.61  ? 56  HIS B CG  1 
ATOM   1606 N  ND1 . HIS B 1 56  ? -39.068 16.498 18.326  1.00 41.44  ? 56  HIS B ND1 1 
ATOM   1607 C  CD2 . HIS B 1 56  ? -37.434 15.836 16.991  1.00 46.66  ? 56  HIS B CD2 1 
ATOM   1608 C  CE1 . HIS B 1 56  ? -39.605 16.011 17.208  1.00 44.68  ? 56  HIS B CE1 1 
ATOM   1609 N  NE2 . HIS B 1 56  ? -38.634 15.595 16.393  1.00 44.62  ? 56  HIS B NE2 1 
ATOM   1610 N  N   . GLU B 1 57  ? -38.055 19.620 18.470  1.00 38.74  ? 57  GLU B N   1 
ATOM   1611 C  CA  . GLU B 1 57  ? -39.069 20.662 18.538  1.00 40.04  ? 57  GLU B CA  1 
ATOM   1612 C  C   . GLU B 1 57  ? -40.279 20.193 19.339  1.00 43.18  ? 57  GLU B C   1 
ATOM   1613 O  O   . GLU B 1 57  ? -41.031 21.041 19.756  1.00 36.46  ? 57  GLU B O   1 
ATOM   1614 C  CB  . GLU B 1 57  ? -39.567 21.135 17.175  1.00 42.17  ? 57  GLU B CB  1 
ATOM   1615 N  N   . SER B 1 58  ? -40.415 18.880 19.613  1.00 40.87  ? 58  SER B N   1 
ATOM   1616 C  CA  . SER B 1 58  ? -41.419 18.397 20.534  1.00 41.73  ? 58  SER B CA  1 
ATOM   1617 C  C   . SER B 1 58  ? -41.210 18.931 21.955  1.00 46.34  ? 58  SER B C   1 
ATOM   1618 O  O   . SER B 1 58  ? -42.120 18.905 22.767  1.00 51.00  ? 58  SER B O   1 
ATOM   1619 C  CB  . SER B 1 58  ? -41.456 16.874 20.551  1.00 41.19  ? 58  SER B CB  1 
ATOM   1620 O  OG  . SER B 1 58  ? -40.181 16.315 20.838  1.00 41.46  ? 58  SER B OG  1 
ATOM   1621 N  N   . PHE B 1 59  ? -40.004 19.333 22.325  1.00 42.03  ? 59  PHE B N   1 
ATOM   1622 C  CA  . PHE B 1 59  ? -39.809 19.837 23.680  1.00 41.80  ? 59  PHE B CA  1 
ATOM   1623 C  C   . PHE B 1 59  ? -40.185 21.302 23.817  1.00 36.87  ? 59  PHE B C   1 
ATOM   1624 O  O   . PHE B 1 59  ? -39.855 22.086 22.953  1.00 46.74  ? 59  PHE B O   1 
ATOM   1625 C  CB  . PHE B 1 59  ? -38.354 19.736 24.134  1.00 37.72  ? 59  PHE B CB  1 
ATOM   1626 C  CG  . PHE B 1 59  ? -37.982 18.323 24.451  1.00 38.56  ? 59  PHE B CG  1 
ATOM   1627 C  CD1 . PHE B 1 59  ? -37.541 17.481 23.461  1.00 38.16  ? 59  PHE B CD1 1 
ATOM   1628 C  CD2 . PHE B 1 59  ? -38.057 17.861 25.754  1.00 39.17  ? 59  PHE B CD2 1 
ATOM   1629 C  CE1 . PHE B 1 59  ? -37.182 16.177 23.765  1.00 42.74  ? 59  PHE B CE1 1 
ATOM   1630 C  CE2 . PHE B 1 59  ? -37.734 16.557 26.043  1.00 37.48  ? 59  PHE B CE2 1 
ATOM   1631 C  CZ  . PHE B 1 59  ? -37.281 15.723 25.048  1.00 38.62  ? 59  PHE B CZ  1 
ATOM   1632 N  N   . PRO B 1 60  ? -40.728 21.730 24.981  1.00 49.35  ? 60  PRO B N   1 
ATOM   1633 C  CA  . PRO B 1 60  ? -40.898 23.158 25.263  1.00 59.30  ? 60  PRO B CA  1 
ATOM   1634 C  C   . PRO B 1 60  ? -39.519 23.819 25.282  1.00 59.41  ? 60  PRO B C   1 
ATOM   1635 O  O   . PRO B 1 60  ? -38.557 23.193 25.704  1.00 53.61  ? 60  PRO B O   1 
ATOM   1636 C  CB  . PRO B 1 60  ? -41.519 23.178 26.675  1.00 57.86  ? 60  PRO B CB  1 
ATOM   1637 C  CG  . PRO B 1 60  ? -41.021 21.883 27.316  1.00 55.74  ? 60  PRO B CG  1 
ATOM   1638 C  CD  . PRO B 1 60  ? -41.021 20.894 26.163  1.00 52.68  ? 60  PRO B CD  1 
ATOM   1639 N  N   . ARG B 1 61  ? -39.414 25.062 24.807  1.00 61.21  ? 61  ARG B N   1 
ATOM   1640 C  CA  . ARG B 1 61  ? -38.189 25.840 24.951  1.00 69.18  ? 61  ARG B CA  1 
ATOM   1641 C  C   . ARG B 1 61  ? -37.022 24.996 24.434  1.00 65.80  ? 61  ARG B C   1 
ATOM   1642 O  O   . ARG B 1 61  ? -36.068 24.719 25.151  1.00 54.74  ? 61  ARG B O   1 
ATOM   1643 C  CB  . ARG B 1 61  ? -37.928 26.232 26.415  1.00 67.14  ? 61  ARG B CB  1 
ATOM   1644 C  CG  . ARG B 1 61  ? -39.148 26.501 27.292  1.00 83.90  ? 61  ARG B CG  1 
ATOM   1645 C  CD  . ARG B 1 61  ? -38.852 26.508 28.796  1.00 87.01  ? 61  ARG B CD  1 
ATOM   1646 N  NE  . ARG B 1 61  ? -37.994 25.439 29.328  1.00 90.42  ? 61  ARG B NE  1 
ATOM   1647 C  CZ  . ARG B 1 61  ? -36.713 25.579 29.696  1.00 83.86  ? 61  ARG B CZ  1 
ATOM   1648 N  NH1 . ARG B 1 61  ? -36.075 24.598 30.311  1.00 69.76  ? 61  ARG B NH1 1 
ATOM   1649 N  NH2 . ARG B 1 61  ? -36.056 26.703 29.464  1.00 82.72  ? 61  ARG B NH2 1 
ATOM   1650 N  N   . PRO B 1 62  ? -37.070 24.498 23.186  1.00 58.63  ? 62  PRO B N   1 
ATOM   1651 C  CA  . PRO B 1 62  ? -36.146 23.441 22.767  1.00 49.52  ? 62  PRO B CA  1 
ATOM   1652 C  C   . PRO B 1 62  ? -34.684 23.871 22.738  1.00 43.01  ? 62  PRO B C   1 
ATOM   1653 O  O   . PRO B 1 62  ? -33.788 23.047 22.855  1.00 41.53  ? 62  PRO B O   1 
ATOM   1654 C  CB  . PRO B 1 62  ? -36.647 23.056 21.364  1.00 50.46  ? 62  PRO B CB  1 
ATOM   1655 C  CG  . PRO B 1 62  ? -37.376 24.322 20.877  1.00 50.41  ? 62  PRO B CG  1 
ATOM   1656 C  CD  . PRO B 1 62  ? -37.992 24.928 22.122  1.00 52.13  ? 62  PRO B CD  1 
ATOM   1657 N  N   . LYS B 1 63  ? -34.440 25.173 22.624  1.00 41.22  ? 63  LYS B N   1 
ATOM   1658 C  CA  . LYS B 1 63  ? -33.109 25.703 22.507  1.00 42.40  ? 63  LYS B CA  1 
ATOM   1659 C  C   . LYS B 1 63  ? -32.568 26.022 23.901  1.00 41.58  ? 63  LYS B C   1 
ATOM   1660 O  O   . LYS B 1 63  ? -32.908 27.061 24.474  1.00 45.30  ? 63  LYS B O   1 
ATOM   1661 C  CB  . LYS B 1 63  ? -33.157 26.943 21.620  1.00 42.88  ? 63  LYS B CB  1 
ATOM   1662 C  CG  . LYS B 1 63  ? -31.808 27.636 21.493  1.00 49.65  ? 63  LYS B CG  1 
ATOM   1663 C  CD  . LYS B 1 63  ? -31.784 28.750 20.494  1.00 55.80  ? 63  LYS B CD  1 
ATOM   1664 C  CE  . LYS B 1 63  ? -30.482 29.504 20.558  1.00 59.07  ? 63  LYS B CE  1 
ATOM   1665 N  NZ  . LYS B 1 63  ? -30.508 30.665 19.654  1.00 66.32  ? 63  LYS B NZ  1 
ATOM   1666 N  N   . ARG B 1 64  ? -31.715 25.132 24.419  1.00 37.41  ? 64  ARG B N   1 
ATOM   1667 C  CA  . ARG B 1 64  ? -31.194 25.220 25.784  1.00 42.01  ? 64  ARG B CA  1 
ATOM   1668 C  C   . ARG B 1 64  ? -29.781 25.789 25.739  1.00 35.43  ? 64  ARG B C   1 
ATOM   1669 O  O   . ARG B 1 64  ? -28.929 25.207 25.102  1.00 40.75  ? 64  ARG B O   1 
ATOM   1670 C  CB  . ARG B 1 64  ? -31.188 23.839 26.451  1.00 40.82  ? 64  ARG B CB  1 
ATOM   1671 C  CG  . ARG B 1 64  ? -32.544 23.162 26.496  1.00 44.61  ? 64  ARG B CG  1 
ATOM   1672 C  CD  . ARG B 1 64  ? -33.517 23.992 27.320  1.00 45.16  ? 64  ARG B CD  1 
ATOM   1673 N  NE  . ARG B 1 64  ? -34.878 23.537 27.257  1.00 42.97  ? 64  ARG B NE  1 
ATOM   1674 C  CZ  . ARG B 1 64  ? -35.363 22.418 27.776  1.00 41.65  ? 64  ARG B CZ  1 
ATOM   1675 N  NH1 . ARG B 1 64  ? -36.547 21.985 27.385  1.00 49.45  ? 64  ARG B NH1 1 
ATOM   1676 N  NH2 . ARG B 1 64  ? -34.650 21.688 28.604  1.00 40.71  ? 64  ARG B NH2 1 
ATOM   1677 N  N   . VAL B 1 65  ? -29.557 26.922 26.398  1.00 35.25  ? 65  VAL B N   1 
ATOM   1678 C  CA  . VAL B 1 65  ? -28.286 27.600 26.442  1.00 35.61  ? 65  VAL B CA  1 
ATOM   1679 C  C   . VAL B 1 65  ? -27.649 27.386 27.810  1.00 43.12  ? 65  VAL B C   1 
ATOM   1680 O  O   . VAL B 1 65  ? -28.325 27.527 28.817  1.00 46.53  ? 65  VAL B O   1 
ATOM   1681 C  CB  . VAL B 1 65  ? -28.496 29.099 26.152  1.00 38.86  ? 65  VAL B CB  1 
ATOM   1682 C  CG1 . VAL B 1 65  ? -27.165 29.815 26.033  1.00 39.83  ? 65  VAL B CG1 1 
ATOM   1683 C  CG2 . VAL B 1 65  ? -29.314 29.361 24.894  1.00 34.06  ? 65  VAL B CG2 1 
ATOM   1684 N  N   . CYS B 1 66  ? -26.376 26.989 27.845  1.00 42.05  ? 66  CYS B N   1 
ATOM   1685 C  CA  . CYS B 1 66  ? -25.581 26.939 29.070  1.00 37.07  ? 66  CYS B CA  1 
ATOM   1686 C  C   . CYS B 1 66  ? -24.398 27.892 28.956  1.00 38.58  ? 66  CYS B C   1 
ATOM   1687 O  O   . CYS B 1 66  ? -23.540 27.675 28.096  1.00 37.46  ? 66  CYS B O   1 
ATOM   1688 C  CB  . CYS B 1 66  ? -24.997 25.553 29.271  1.00 46.14  ? 66  CYS B CB  1 
ATOM   1689 S  SG  . CYS B 1 66  ? -26.251 24.316 29.674  1.00 47.61  ? 66  CYS B SG  1 
ATOM   1690 N  N   . LYS B 1 67  ? -24.390 28.965 29.768  1.00 39.90  ? 67  LYS B N   1 
ATOM   1691 C  CA  . LYS B 1 67  ? -23.335 29.970 29.712  1.00 42.78  ? 67  LYS B CA  1 
ATOM   1692 C  C   . LYS B 1 67  ? -22.175 29.553 30.586  1.00 33.60  ? 67  LYS B C   1 
ATOM   1693 O  O   . LYS B 1 67  ? -21.065 29.993 30.350  1.00 41.02  ? 67  LYS B O   1 
ATOM   1694 C  CB  . LYS B 1 67  ? -23.827 31.348 30.184  1.00 49.29  ? 67  LYS B CB  1 
ATOM   1695 C  CG  . LYS B 1 67  ? -24.830 32.043 29.275  1.00 58.08  ? 67  LYS B CG  1 
ATOM   1696 C  CD  . LYS B 1 67  ? -24.256 32.567 27.978  1.00 74.65  ? 67  LYS B CD  1 
ATOM   1697 C  CE  . LYS B 1 67  ? -25.297 33.151 27.034  1.00 82.97  ? 67  LYS B CE  1 
ATOM   1698 N  NZ  . LYS B 1 67  ? -25.885 34.401 27.550  1.00 72.96  ? 67  LYS B NZ  1 
ATOM   1699 N  N   . ASP B 1 68  ? -22.463 28.699 31.561  1.00 34.94  ? 68  ASP B N   1 
ATOM   1700 C  CA  . ASP B 1 68  ? -21.522 28.220 32.546  1.00 46.64  ? 68  ASP B CA  1 
ATOM   1701 C  C   . ASP B 1 68  ? -21.582 26.696 32.625  1.00 41.51  ? 68  ASP B C   1 
ATOM   1702 O  O   . ASP B 1 68  ? -22.653 26.113 32.489  1.00 43.44  ? 68  ASP B O   1 
ATOM   1703 C  CB  . ASP B 1 68  ? -21.868 28.770 33.938  1.00 44.15  ? 68  ASP B CB  1 
ATOM   1704 C  CG  . ASP B 1 68  ? -21.618 30.247 34.034  1.00 50.93  ? 68  ASP B CG  1 
ATOM   1705 O  OD1 . ASP B 1 68  ? -20.480 30.639 33.829  1.00 53.70  ? 68  ASP B OD1 1 
ATOM   1706 O  OD2 . ASP B 1 68  ? -22.579 30.992 34.212  1.00 65.63  ? 68  ASP B OD2 1 
ATOM   1707 N  N   . PRO B 1 69  ? -20.457 26.018 32.943  1.00 35.05  ? 69  PRO B N   1 
ATOM   1708 C  CA  . PRO B 1 69  ? -20.475 24.573 33.171  1.00 35.67  ? 69  PRO B CA  1 
ATOM   1709 C  C   . PRO B 1 69  ? -21.330 24.247 34.405  1.00 29.88  ? 69  PRO B C   1 
ATOM   1710 O  O   . PRO B 1 69  ? -21.443 25.031 35.299  1.00 37.67  ? 69  PRO B O   1 
ATOM   1711 C  CB  . PRO B 1 69  ? -19.008 24.154 33.393  1.00 34.75  ? 69  PRO B CB  1 
ATOM   1712 C  CG  . PRO B 1 69  ? -18.240 25.437 33.617  1.00 41.38  ? 69  PRO B CG  1 
ATOM   1713 C  CD  . PRO B 1 69  ? -19.126 26.594 33.139  1.00 40.56  ? 69  PRO B CD  1 
ATOM   1714 N  N   . PRO B 1 70  ? -21.860 23.027 34.560  1.00 40.01  ? 70  PRO B N   1 
ATOM   1715 C  CA  . PRO B 1 70  ? -21.658 21.978 33.559  1.00 32.63  ? 70  PRO B CA  1 
ATOM   1716 C  C   . PRO B 1 70  ? -22.541 22.244 32.325  1.00 32.81  ? 70  PRO B C   1 
ATOM   1717 O  O   . PRO B 1 70  ? -23.667 22.699 32.417  1.00 33.29  ? 70  PRO B O   1 
ATOM   1718 C  CB  . PRO B 1 70  ? -22.047 20.713 34.322  1.00 40.83  ? 70  PRO B CB  1 
ATOM   1719 C  CG  . PRO B 1 70  ? -23.064 21.174 35.361  1.00 37.25  ? 70  PRO B CG  1 
ATOM   1720 C  CD  . PRO B 1 70  ? -22.643 22.585 35.732  1.00 36.33  ? 70  PRO B CD  1 
ATOM   1721 N  N   . TYR B 1 71  ? -21.982 22.036 31.137  1.00 31.32  ? 71  TYR B N   1 
ATOM   1722 C  CA  . TYR B 1 71  ? -22.692 22.245 29.884  1.00 32.26  ? 71  TYR B CA  1 
ATOM   1723 C  C   . TYR B 1 71  ? -23.510 21.004 29.619  1.00 32.01  ? 71  TYR B C   1 
ATOM   1724 O  O   . TYR B 1 71  ? -22.968 20.021 29.137  1.00 34.12  ? 71  TYR B O   1 
ATOM   1725 C  CB  . TYR B 1 71  ? -21.703 22.548 28.761  1.00 35.58  ? 71  TYR B CB  1 
ATOM   1726 C  CG  . TYR B 1 71  ? -20.775 23.727 29.038  1.00 36.15  ? 71  TYR B CG  1 
ATOM   1727 C  CD1 . TYR B 1 71  ? -21.249 25.032 29.023  1.00 31.48  ? 71  TYR B CD1 1 
ATOM   1728 C  CD2 . TYR B 1 71  ? -19.438 23.520 29.296  1.00 32.83  ? 71  TYR B CD2 1 
ATOM   1729 C  CE1 . TYR B 1 71  ? -20.413 26.120 29.238  1.00 37.97  ? 71  TYR B CE1 1 
ATOM   1730 C  CE2 . TYR B 1 71  ? -18.595 24.585 29.556  1.00 36.88  ? 71  TYR B CE2 1 
ATOM   1731 C  CZ  . TYR B 1 71  ? -19.078 25.878 29.517  1.00 40.03  ? 71  TYR B CZ  1 
ATOM   1732 O  OH  . TYR B 1 71  ? -18.203 26.881 29.707  1.00 37.32  ? 71  TYR B OH  1 
ATOM   1733 N  N   . LYS B 1 72  ? -24.784 21.064 30.010  1.00 31.47  ? 72  LYS B N   1 
ATOM   1734 C  CA  . LYS B 1 72  ? -25.632 19.893 29.967  1.00 35.59  ? 72  LYS B CA  1 
ATOM   1735 C  C   . LYS B 1 72  ? -27.112 20.256 30.001  1.00 36.08  ? 72  LYS B C   1 
ATOM   1736 O  O   . LYS B 1 72  ? -27.514 21.344 30.437  1.00 36.19  ? 72  LYS B O   1 
ATOM   1737 C  CB  . LYS B 1 72  ? -25.306 18.974 31.141  1.00 34.91  ? 72  LYS B CB  1 
ATOM   1738 C  CG  . LYS B 1 72  ? -25.852 19.427 32.493  1.00 40.78  ? 72  LYS B CG  1 
ATOM   1739 C  CD  . LYS B 1 72  ? -25.725 18.307 33.511  1.00 43.76  ? 72  LYS B CD  1 
ATOM   1740 C  CE  . LYS B 1 72  ? -26.049 18.799 34.908  1.00 55.29  ? 72  LYS B CE  1 
ATOM   1741 N  NZ  . LYS B 1 72  ? -26.053 17.655 35.852  1.00 54.77  ? 72  LYS B NZ  1 
ATOM   1742 N  N   . VAL B 1 73  ? -27.912 19.291 29.548  1.00 35.31  ? 73  VAL B N   1 
ATOM   1743 C  CA  . VAL B 1 73  ? -29.370 19.350 29.614  1.00 33.57  ? 73  VAL B CA  1 
ATOM   1744 C  C   . VAL B 1 73  ? -29.864 18.023 30.177  1.00 34.66  ? 73  VAL B C   1 
ATOM   1745 O  O   . VAL B 1 73  ? -29.359 16.982 29.790  1.00 32.11  ? 73  VAL B O   1 
ATOM   1746 C  CB  . VAL B 1 73  ? -29.966 19.563 28.221  1.00 38.77  ? 73  VAL B CB  1 
ATOM   1747 C  CG1 . VAL B 1 73  ? -31.488 19.369 28.227  1.00 43.12  ? 73  VAL B CG1 1 
ATOM   1748 C  CG2 . VAL B 1 73  ? -29.563 20.923 27.651  1.00 39.11  ? 73  VAL B CG2 1 
ATOM   1749 N  N   . GLU B 1 74  ? -30.791 18.096 31.133  1.00 39.19  ? 74  GLU B N   1 
ATOM   1750 C  CA  . GLU B 1 74  ? -31.386 16.910 31.722  1.00 48.37  ? 74  GLU B CA  1 
ATOM   1751 C  C   . GLU B 1 74  ? -32.865 16.962 31.400  1.00 41.06  ? 74  GLU B C   1 
ATOM   1752 O  O   . GLU B 1 74  ? -33.494 17.981 31.615  1.00 37.50  ? 74  GLU B O   1 
ATOM   1753 C  CB  . GLU B 1 74  ? -31.229 16.897 33.236  1.00 46.54  ? 74  GLU B CB  1 
ATOM   1754 C  CG  . GLU B 1 74  ? -29.821 16.653 33.672  1.00 60.07  ? 74  GLU B CG  1 
ATOM   1755 C  CD  . GLU B 1 74  ? -29.619 16.820 35.167  1.00 76.52  ? 74  GLU B CD  1 
ATOM   1756 O  OE1 . GLU B 1 74  ? -29.956 17.898 35.699  1.00 80.78  ? 74  GLU B OE1 1 
ATOM   1757 O  OE2 . GLU B 1 74  ? -29.106 15.876 35.795  1.00 97.41  ? 74  GLU B OE2 1 
ATOM   1758 N  N   . GLU B 1 75  ? -33.390 15.867 30.902  1.00 41.51  ? 75  GLU B N   1 
ATOM   1759 C  CA  . GLU B 1 75  ? -34.743 15.857 30.393  1.00 41.66  ? 75  GLU B CA  1 
ATOM   1760 C  C   . GLU B 1 75  ? -35.305 14.453 30.538  1.00 37.22  ? 75  GLU B C   1 
ATOM   1761 O  O   . GLU B 1 75  ? -34.608 13.519 30.894  1.00 34.95  ? 75  GLU B O   1 
ATOM   1762 C  CB  . GLU B 1 75  ? -34.781 16.320 28.941  1.00 47.20  ? 75  GLU B CB  1 
ATOM   1763 C  CG  . GLU B 1 75  ? -35.072 17.788 28.788  1.00 49.30  ? 75  GLU B CG  1 
ATOM   1764 C  CD  . GLU B 1 75  ? -36.448 18.151 29.315  1.00 52.61  ? 75  GLU B CD  1 
ATOM   1765 O  OE1 . GLU B 1 75  ? -37.195 17.243 29.658  1.00 60.13  ? 75  GLU B OE1 1 
ATOM   1766 O  OE2 . GLU B 1 75  ? -36.786 19.319 29.332  1.00 51.25  ? 75  GLU B OE2 1 
ATOM   1767 N  N   . SER B 1 76  ? -36.616 14.380 30.369  1.00 43.28  ? 76  SER B N   1 
ATOM   1768 C  CA  . SER B 1 76  ? -37.351 13.128 30.301  1.00 46.52  ? 76  SER B CA  1 
ATOM   1769 C  C   . SER B 1 76  ? -38.132 13.191 28.996  1.00 50.96  ? 76  SER B C   1 
ATOM   1770 O  O   . SER B 1 76  ? -38.530 14.287 28.551  1.00 40.61  ? 76  SER B O   1 
ATOM   1771 C  CB  . SER B 1 76  ? -38.291 12.971 31.481  1.00 49.19  ? 76  SER B CB  1 
ATOM   1772 O  OG  . SER B 1 76  ? -37.596 12.556 32.648  1.00 48.32  ? 76  SER B OG  1 
ATOM   1773 N  N   . GLY B 1 77  ? -38.365 12.020 28.404  1.00 38.67  ? 77  GLY B N   1 
ATOM   1774 C  CA  . GLY B 1 77  ? -39.059 11.972 27.128  1.00 40.59  ? 77  GLY B CA  1 
ATOM   1775 C  C   . GLY B 1 77  ? -39.299 10.534 26.690  1.00 40.44  ? 77  GLY B C   1 
ATOM   1776 O  O   . GLY B 1 77  ? -39.094 9.613  27.484  1.00 36.20  ? 77  GLY B O   1 
ATOM   1777 N  N   . TYR B 1 78  ? -39.697 10.340 25.431  1.00 40.72  ? 78  TYR B N   1 
ATOM   1778 C  CA  . TYR B 1 78  ? -40.156 9.013  25.030  1.00 45.69  ? 78  TYR B CA  1 
ATOM   1779 C  C   . TYR B 1 78  ? -39.333 8.474  23.873  1.00 41.39  ? 78  TYR B C   1 
ATOM   1780 O  O   . TYR B 1 78  ? -39.470 7.312  23.533  1.00 50.13  ? 78  TYR B O   1 
ATOM   1781 C  CB  . TYR B 1 78  ? -41.666 9.091  24.730  1.00 41.95  ? 78  TYR B CB  1 
ATOM   1782 C  CG  . TYR B 1 78  ? -42.053 10.089 23.648  1.00 37.74  ? 78  TYR B CG  1 
ATOM   1783 C  CD1 . TYR B 1 78  ? -41.916 9.747  22.313  1.00 45.27  ? 78  TYR B CD1 1 
ATOM   1784 C  CD2 . TYR B 1 78  ? -42.368 11.410 23.936  1.00 41.13  ? 78  TYR B CD2 1 
ATOM   1785 C  CE1 . TYR B 1 78  ? -42.209 10.639 21.297  1.00 40.38  ? 78  TYR B CE1 1 
ATOM   1786 C  CE2 . TYR B 1 78  ? -42.618 12.322 22.929  1.00 36.79  ? 78  TYR B CE2 1 
ATOM   1787 C  CZ  . TYR B 1 78  ? -42.556 11.931 21.605  1.00 39.24  ? 78  TYR B CZ  1 
ATOM   1788 O  OH  . TYR B 1 78  ? -42.814 12.784 20.573  1.00 38.26  ? 78  TYR B OH  1 
ATOM   1789 N  N   . ALA B 1 79  ? -38.467 9.303  23.280  1.00 45.17  ? 79  ALA B N   1 
ATOM   1790 C  CA  . ALA B 1 79  ? -37.726 8.837  22.117  1.00 43.47  ? 79  ALA B CA  1 
ATOM   1791 C  C   . ALA B 1 79  ? -36.404 9.596  21.992  1.00 41.63  ? 79  ALA B C   1 
ATOM   1792 O  O   . ALA B 1 79  ? -36.314 10.768 22.340  1.00 37.34  ? 79  ALA B O   1 
ATOM   1793 C  CB  . ALA B 1 79  ? -38.605 9.026  20.883  1.00 37.77  ? 79  ALA B CB  1 
ATOM   1794 N  N   . GLY B 1 80  ? -35.403 8.903  21.458  1.00 41.20  ? 80  GLY B N   1 
ATOM   1795 C  CA  . GLY B 1 80  ? -34.186 9.524  20.981  1.00 45.47  ? 80  GLY B CA  1 
ATOM   1796 C  C   . GLY B 1 80  ? -34.451 10.448 19.792  1.00 40.61  ? 80  GLY B C   1 
ATOM   1797 O  O   . GLY B 1 80  ? -35.515 10.468 19.210  1.00 39.87  ? 80  GLY B O   1 
ATOM   1798 N  N   . PHE B 1 81  ? -33.426 11.180 19.413  1.00 36.51  ? 81  PHE B N   1 
ATOM   1799 C  CA  . PHE B 1 81  ? -33.447 12.043 18.264  1.00 33.33  ? 81  PHE B CA  1 
ATOM   1800 C  C   . PHE B 1 81  ? -32.055 12.611 18.073  1.00 34.63  ? 81  PHE B C   1 
ATOM   1801 O  O   . PHE B 1 81  ? -31.204 12.455 18.929  1.00 34.20  ? 81  PHE B O   1 
ATOM   1802 C  CB  . PHE B 1 81  ? -34.407 13.209 18.427  1.00 37.00  ? 81  PHE B CB  1 
ATOM   1803 C  CG  . PHE B 1 81  ? -34.186 13.986 19.690  1.00 40.18  ? 81  PHE B CG  1 
ATOM   1804 C  CD1 . PHE B 1 81  ? -34.742 13.557 20.894  1.00 42.12  ? 81  PHE B CD1 1 
ATOM   1805 C  CD2 . PHE B 1 81  ? -33.389 15.120 19.684  1.00 41.19  ? 81  PHE B CD2 1 
ATOM   1806 C  CE1 . PHE B 1 81  ? -34.527 14.276 22.065  1.00 45.77  ? 81  PHE B CE1 1 
ATOM   1807 C  CE2 . PHE B 1 81  ? -33.182 15.824 20.855  1.00 38.42  ? 81  PHE B CE2 1 
ATOM   1808 C  CZ  . PHE B 1 81  ? -33.747 15.411 22.040  1.00 42.69  ? 81  PHE B CZ  1 
ATOM   1809 N  N   . ILE B 1 82  ? -31.869 13.306 16.957  1.00 30.00  ? 82  ILE B N   1 
ATOM   1810 C  CA  . ILE B 1 82  ? -30.626 13.953 16.636  1.00 35.05  ? 82  ILE B CA  1 
ATOM   1811 C  C   . ILE B 1 82  ? -30.690 15.373 17.225  1.00 35.83  ? 82  ILE B C   1 
ATOM   1812 O  O   . ILE B 1 82  ? -31.675 16.100 17.032  1.00 33.01  ? 82  ILE B O   1 
ATOM   1813 C  CB  . ILE B 1 82  ? -30.407 13.948 15.107  1.00 36.94  ? 82  ILE B CB  1 
ATOM   1814 C  CG1 . ILE B 1 82  ? -30.274 12.550 14.504  1.00 37.24  ? 82  ILE B CG1 1 
ATOM   1815 C  CG2 . ILE B 1 82  ? -29.224 14.819 14.757  1.00 41.11  ? 82  ILE B CG2 1 
ATOM   1816 C  CD1 . ILE B 1 82  ? -29.096 11.755 14.989  1.00 42.36  ? 82  ILE B CD1 1 
ATOM   1817 N  N   . LEU B 1 83  ? -29.650 15.733 17.982  1.00 31.95  ? 83  LEU B N   1 
ATOM   1818 C  CA  . LEU B 1 83  ? -29.702 16.869 18.885  1.00 31.00  ? 83  LEU B CA  1 
ATOM   1819 C  C   . LEU B 1 83  ? -28.515 17.750 18.532  1.00 35.30  ? 83  LEU B C   1 
ATOM   1820 O  O   . LEU B 1 83  ? -27.371 17.421 18.829  1.00 34.28  ? 83  LEU B O   1 
ATOM   1821 C  CB  . LEU B 1 83  ? -29.645 16.351 20.320  1.00 34.81  ? 83  LEU B CB  1 
ATOM   1822 C  CG  . LEU B 1 83  ? -29.874 17.409 21.407  1.00 34.46  ? 83  LEU B CG  1 
ATOM   1823 C  CD1 . LEU B 1 83  ? -29.859 16.777 22.779  1.00 35.63  ? 83  LEU B CD1 1 
ATOM   1824 C  CD2 . LEU B 1 83  ? -28.830 18.490 21.341  1.00 36.35  ? 83  LEU B CD2 1 
ATOM   1825 N  N   . PRO B 1 84  ? -28.715 18.767 17.673  1.00 34.05  ? 84  PRO B N   1 
ATOM   1826 C  CA  . PRO B 1 84  ? -27.618 19.651 17.285  1.00 31.75  ? 84  PRO B CA  1 
ATOM   1827 C  C   . PRO B 1 84  ? -27.076 20.341 18.516  1.00 27.54  ? 84  PRO B C   1 
ATOM   1828 O  O   . PRO B 1 84  ? -27.868 20.885 19.308  1.00 29.32  ? 84  PRO B O   1 
ATOM   1829 C  CB  . PRO B 1 84  ? -28.276 20.673 16.324  1.00 34.58  ? 84  PRO B CB  1 
ATOM   1830 C  CG  . PRO B 1 84  ? -29.454 19.895 15.763  1.00 37.63  ? 84  PRO B CG  1 
ATOM   1831 C  CD  . PRO B 1 84  ? -29.942 19.027 16.920  1.00 34.51  ? 84  PRO B CD  1 
ATOM   1832 N  N   . ILE B 1 85  ? -25.753 20.344 18.635  1.00 27.69  ? 85  ILE B N   1 
ATOM   1833 C  CA  . ILE B 1 85  ? -25.067 21.014 19.735  1.00 32.02  ? 85  ILE B CA  1 
ATOM   1834 C  C   . ILE B 1 85  ? -24.128 22.037 19.132  1.00 28.32  ? 85  ILE B C   1 
ATOM   1835 O  O   . ILE B 1 85  ? -23.342 21.700 18.264  1.00 28.49  ? 85  ILE B O   1 
ATOM   1836 C  CB  . ILE B 1 85  ? -24.275 20.006 20.597  1.00 32.46  ? 85  ILE B CB  1 
ATOM   1837 C  CG1 . ILE B 1 85  ? -25.199 18.955 21.209  1.00 31.79  ? 85  ILE B CG1 1 
ATOM   1838 C  CG2 . ILE B 1 85  ? -23.418 20.712 21.651  1.00 30.59  ? 85  ILE B CG2 1 
ATOM   1839 C  CD1 . ILE B 1 85  ? -24.497 17.983 22.123  1.00 32.20  ? 85  ILE B CD1 1 
ATOM   1840 N  N   . GLU B 1 86  ? -24.195 23.254 19.643  1.00 33.63  ? 86  GLU B N   1 
ATOM   1841 C  CA  . GLU B 1 86  ? -23.350 24.318 19.155  1.00 36.46  ? 86  GLU B CA  1 
ATOM   1842 C  C   . GLU B 1 86  ? -22.474 24.806 20.297  1.00 33.98  ? 86  GLU B C   1 
ATOM   1843 O  O   . GLU B 1 86  ? -22.985 25.273 21.329  1.00 31.76  ? 86  GLU B O   1 
ATOM   1844 C  CB  . GLU B 1 86  ? -24.148 25.517 18.687  1.00 43.19  ? 86  GLU B CB  1 
ATOM   1845 C  CG  . GLU B 1 86  ? -25.007 25.324 17.458  1.00 52.04  ? 86  GLU B CG  1 
ATOM   1846 C  CD  . GLU B 1 86  ? -25.616 26.674 17.069  1.00 50.69  ? 86  GLU B CD  1 
ATOM   1847 O  OE1 . GLU B 1 86  ? -26.538 27.165 17.769  1.00 48.89  ? 86  GLU B OE1 1 
ATOM   1848 O  OE2 . GLU B 1 86  ? -25.043 27.317 16.190  1.00 60.92  ? 86  GLU B OE2 1 
ATOM   1849 N  N   . VAL B 1 87  ? -21.165 24.738 20.059  1.00 30.27  ? 87  VAL B N   1 
ATOM   1850 C  CA  . VAL B 1 87  ? -20.208 25.220 21.031  1.00 33.31  ? 87  VAL B CA  1 
ATOM   1851 C  C   . VAL B 1 87  ? -19.621 26.516 20.492  1.00 32.94  ? 87  VAL B C   1 
ATOM   1852 O  O   . VAL B 1 87  ? -18.922 26.496 19.487  1.00 38.39  ? 87  VAL B O   1 
ATOM   1853 C  CB  . VAL B 1 87  ? -19.102 24.198 21.305  1.00 32.59  ? 87  VAL B CB  1 
ATOM   1854 C  CG1 . VAL B 1 87  ? -18.084 24.750 22.295  1.00 31.50  ? 87  VAL B CG1 1 
ATOM   1855 C  CG2 . VAL B 1 87  ? -19.665 22.855 21.726  1.00 30.88  ? 87  VAL B CG2 1 
ATOM   1856 N  N   . TYR B 1 88  ? -19.949 27.615 21.172  1.00 30.67  ? 88  TYR B N   1 
ATOM   1857 C  CA  . TYR B 1 88  ? -19.493 28.954 20.828  1.00 34.25  ? 88  TYR B CA  1 
ATOM   1858 C  C   . TYR B 1 88  ? -18.218 29.311 21.590  1.00 37.95  ? 88  TYR B C   1 
ATOM   1859 O  O   . TYR B 1 88  ? -18.092 29.009 22.780  1.00 38.22  ? 88  TYR B O   1 
ATOM   1860 C  CB  . TYR B 1 88  ? -20.533 29.999 21.243  1.00 32.18  ? 88  TYR B CB  1 
ATOM   1861 C  CG  . TYR B 1 88  ? -21.677 30.072 20.247  1.00 35.90  ? 88  TYR B CG  1 
ATOM   1862 C  CD1 . TYR B 1 88  ? -22.623 29.048 20.206  1.00 39.29  ? 88  TYR B CD1 1 
ATOM   1863 C  CD2 . TYR B 1 88  ? -21.773 31.110 19.299  1.00 40.41  ? 88  TYR B CD2 1 
ATOM   1864 C  CE1 . TYR B 1 88  ? -23.669 29.064 19.288  1.00 46.77  ? 88  TYR B CE1 1 
ATOM   1865 C  CE2 . TYR B 1 88  ? -22.805 31.125 18.365  1.00 39.02  ? 88  TYR B CE2 1 
ATOM   1866 C  CZ  . TYR B 1 88  ? -23.743 30.094 18.353  1.00 49.25  ? 88  TYR B CZ  1 
ATOM   1867 O  OH  . TYR B 1 88  ? -24.761 30.024 17.447  1.00 44.01  ? 88  TYR B OH  1 
ATOM   1868 N  N   . PHE B 1 89  ? -17.297 29.980 20.897  1.00 32.66  ? 89  PHE B N   1 
ATOM   1869 C  CA  . PHE B 1 89  ? -15.975 30.257 21.429  1.00 31.08  ? 89  PHE B CA  1 
ATOM   1870 C  C   . PHE B 1 89  ? -15.834 31.693 21.901  1.00 37.08  ? 89  PHE B C   1 
ATOM   1871 O  O   . PHE B 1 89  ? -16.540 32.569 21.437  1.00 42.67  ? 89  PHE B O   1 
ATOM   1872 C  CB  . PHE B 1 89  ? -14.955 29.968 20.352  1.00 31.28  ? 89  PHE B CB  1 
ATOM   1873 C  CG  . PHE B 1 89  ? -15.018 28.554 19.833  1.00 39.36  ? 89  PHE B CG  1 
ATOM   1874 C  CD1 . PHE B 1 89  ? -14.958 27.477 20.693  1.00 36.81  ? 89  PHE B CD1 1 
ATOM   1875 C  CD2 . PHE B 1 89  ? -15.108 28.308 18.481  1.00 38.88  ? 89  PHE B CD2 1 
ATOM   1876 C  CE1 . PHE B 1 89  ? -15.032 26.191 20.202  1.00 38.78  ? 89  PHE B CE1 1 
ATOM   1877 C  CE2 . PHE B 1 89  ? -15.153 27.014 17.992  1.00 37.88  ? 89  PHE B CE2 1 
ATOM   1878 C  CZ  . PHE B 1 89  ? -15.162 25.963 18.863  1.00 37.71  ? 89  PHE B CZ  1 
ATOM   1879 N  N   . LYS B 1 90  ? -14.902 31.927 22.823  1.00 37.96  ? 90  LYS B N   1 
ATOM   1880 C  CA  . LYS B 1 90  ? -14.649 33.267 23.328  1.00 47.43  ? 90  LYS B CA  1 
ATOM   1881 C  C   . LYS B 1 90  ? -13.647 33.997 22.441  1.00 55.03  ? 90  LYS B C   1 
ATOM   1882 O  O   . LYS B 1 90  ? -12.562 34.336 22.877  1.00 53.00  ? 90  LYS B O   1 
ATOM   1883 C  CB  . LYS B 1 90  ? -14.089 33.178 24.734  1.00 43.76  ? 90  LYS B CB  1 
ATOM   1884 C  CG  . LYS B 1 90  ? -15.139 32.967 25.797  1.00 48.24  ? 90  LYS B CG  1 
ATOM   1885 C  CD  . LYS B 1 90  ? -14.515 32.829 27.150  1.00 50.98  ? 90  LYS B CD  1 
ATOM   1886 C  CE  . LYS B 1 90  ? -15.515 32.979 28.273  1.00 45.00  ? 90  LYS B CE  1 
ATOM   1887 N  NZ  . LYS B 1 90  ? -15.027 32.252 29.454  1.00 47.08  ? 90  LYS B NZ  1 
ATOM   1888 N  N   . ASN B 1 91  ? -14.006 34.228 21.187  1.00 65.23  ? 91  ASN B N   1 
ATOM   1889 C  CA  . ASN B 1 91  ? -13.110 34.890 20.250  1.00 59.32  ? 91  ASN B CA  1 
ATOM   1890 C  C   . ASN B 1 91  ? -13.963 35.866 19.450  1.00 58.10  ? 91  ASN B C   1 
ATOM   1891 O  O   . ASN B 1 91  ? -15.148 36.049 19.743  1.00 62.18  ? 91  ASN B O   1 
ATOM   1892 C  CB  . ASN B 1 91  ? -12.383 33.876 19.369  1.00 52.16  ? 91  ASN B CB  1 
ATOM   1893 C  CG  . ASN B 1 91  ? -13.384 33.121 18.540  1.00 58.92  ? 91  ASN B CG  1 
ATOM   1894 O  OD1 . ASN B 1 91  ? -14.553 33.484 18.551  1.00 55.30  ? 91  ASN B OD1 1 
ATOM   1895 N  ND2 . ASN B 1 91  ? -12.961 32.114 17.793  1.00 60.88  ? 91  ASN B ND2 1 
ATOM   1896 N  N   . LYS B 1 92  ? -13.349 36.523 18.475  1.00 67.73  ? 92  LYS B N   1 
ATOM   1897 C  CA  . LYS B 1 92  ? -14.007 37.594 17.749  1.00 73.75  ? 92  LYS B CA  1 
ATOM   1898 C  C   . LYS B 1 92  ? -13.562 37.473 16.302  1.00 68.46  ? 92  LYS B C   1 
ATOM   1899 O  O   . LYS B 1 92  ? -13.074 38.416 15.695  1.00 85.77  ? 92  LYS B O   1 
ATOM   1900 C  CB  . LYS B 1 92  ? -13.613 38.939 18.364  1.00 83.19  ? 92  LYS B CB  1 
ATOM   1901 C  CG  . LYS B 1 92  ? -13.845 39.085 19.860  1.00 90.23  ? 92  LYS B CG  1 
ATOM   1902 C  CD  . LYS B 1 92  ? -12.646 39.707 20.536  1.00 98.51  ? 92  LYS B CD  1 
ATOM   1903 C  CE  . LYS B 1 92  ? -12.976 40.358 21.856  1.00 104.20 ? 92  LYS B CE  1 
ATOM   1904 N  NZ  . LYS B 1 92  ? -13.762 41.593 21.642  1.00 109.45 ? 92  LYS B NZ  1 
ATOM   1905 N  N   . GLU B 1 93  ? -13.698 36.272 15.766  1.00 63.10  ? 93  GLU B N   1 
ATOM   1906 C  CA  . GLU B 1 93  ? -13.027 35.909 14.537  1.00 67.42  ? 93  GLU B CA  1 
ATOM   1907 C  C   . GLU B 1 93  ? -13.513 34.525 14.177  1.00 69.73  ? 93  GLU B C   1 
ATOM   1908 O  O   . GLU B 1 93  ? -13.947 33.810 15.069  1.00 74.07  ? 93  GLU B O   1 
ATOM   1909 C  CB  . GLU B 1 93  ? -11.509 35.884 14.726  1.00 81.40  ? 93  GLU B CB  1 
ATOM   1910 C  CG  . GLU B 1 93  ? -11.044 35.066 15.938  1.00 103.37 ? 93  GLU B CG  1 
ATOM   1911 C  CD  . GLU B 1 93  ? -9.695  34.364 15.787  1.00 118.19 ? 93  GLU B CD  1 
ATOM   1912 O  OE1 . GLU B 1 93  ? -9.185  34.369 14.650  1.00 136.88 ? 93  GLU B OE1 1 
ATOM   1913 O  OE2 . GLU B 1 93  ? -9.148  33.794 16.785  1.00 97.12  ? 93  GLU B OE2 1 
ATOM   1914 N  N   . GLU B 1 94  ? -13.445 34.157 12.897  1.00 66.15  ? 94  GLU B N   1 
ATOM   1915 C  CA  . GLU B 1 94  ? -13.915 32.839 12.522  1.00 71.01  ? 94  GLU B CA  1 
ATOM   1916 C  C   . GLU B 1 94  ? -12.886 31.823 12.985  1.00 75.86  ? 94  GLU B C   1 
ATOM   1917 O  O   . GLU B 1 94  ? -11.732 32.197 13.162  1.00 75.19  ? 94  GLU B O   1 
ATOM   1918 C  CB  . GLU B 1 94  ? -14.191 32.715 11.026  1.00 75.37  ? 94  GLU B CB  1 
ATOM   1919 C  CG  . GLU B 1 94  ? -15.525 33.315 10.632  1.00 71.40  ? 94  GLU B CG  1 
ATOM   1920 C  CD  . GLU B 1 94  ? -16.650 33.093 11.637  1.00 84.50  ? 94  GLU B CD  1 
ATOM   1921 O  OE1 . GLU B 1 94  ? -16.889 31.920 11.994  1.00 70.20  ? 94  GLU B OE1 1 
ATOM   1922 O  OE2 . GLU B 1 94  ? -17.293 34.091 12.072  1.00 98.07  ? 94  GLU B OE2 1 
ATOM   1923 N  N   . PRO B 1 95  ? -13.292 30.570 13.323  1.00 71.34  ? 95  PRO B N   1 
ATOM   1924 C  CA  . PRO B 1 95  ? -14.696 30.222 13.544  1.00 58.02  ? 95  PRO B CA  1 
ATOM   1925 C  C   . PRO B 1 95  ? -15.183 30.645 14.934  1.00 53.41  ? 95  PRO B C   1 
ATOM   1926 O  O   . PRO B 1 95  ? -14.430 30.639 15.900  1.00 53.85  ? 95  PRO B O   1 
ATOM   1927 C  CB  . PRO B 1 95  ? -14.674 28.696 13.399  1.00 63.66  ? 95  PRO B CB  1 
ATOM   1928 C  CG  . PRO B 1 95  ? -13.343 28.310 13.983  1.00 63.38  ? 95  PRO B CG  1 
ATOM   1929 C  CD  . PRO B 1 95  ? -12.407 29.411 13.524  1.00 69.76  ? 95  PRO B CD  1 
ATOM   1930 N  N   . ARG B 1 96  ? -16.446 31.075 15.009  1.00 48.44  ? 96  ARG B N   1 
ATOM   1931 C  CA  . ARG B 1 96  ? -17.072 31.535 16.227  1.00 43.74  ? 96  ARG B CA  1 
ATOM   1932 C  C   . ARG B 1 96  ? -17.637 30.351 17.012  1.00 38.56  ? 96  ARG B C   1 
ATOM   1933 O  O   . ARG B 1 96  ? -17.926 30.465 18.192  1.00 35.90  ? 96  ARG B O   1 
ATOM   1934 C  CB  . ARG B 1 96  ? -18.143 32.560 15.861  1.00 48.81  ? 96  ARG B CB  1 
ATOM   1935 C  CG  . ARG B 1 96  ? -17.555 33.925 15.504  1.00 58.13  ? 96  ARG B CG  1 
ATOM   1936 C  CD  . ARG B 1 96  ? -17.062 34.663 16.756  1.00 60.11  ? 96  ARG B CD  1 
ATOM   1937 N  NE  . ARG B 1 96  ? -18.067 34.811 17.845  1.00 74.73  ? 96  ARG B NE  1 
ATOM   1938 C  CZ  . ARG B 1 96  ? -18.205 34.009 18.924  1.00 81.86  ? 96  ARG B CZ  1 
ATOM   1939 N  NH1 . ARG B 1 96  ? -17.327 33.066 19.191  1.00 99.62  ? 96  ARG B NH1 1 
ATOM   1940 N  NH2 . ARG B 1 96  ? -19.219 34.137 19.765  1.00 79.92  ? 96  ARG B NH2 1 
ATOM   1941 N  N   . LYS B 1 97  ? -17.814 29.221 16.346  1.00 36.93  ? 97  LYS B N   1 
ATOM   1942 C  CA  . LYS B 1 97  ? -18.464 28.086 16.964  1.00 36.78  ? 97  LYS B CA  1 
ATOM   1943 C  C   . LYS B 1 97  ? -18.221 26.850 16.110  1.00 38.75  ? 97  LYS B C   1 
ATOM   1944 O  O   . LYS B 1 97  ? -17.735 26.933 14.989  1.00 41.99  ? 97  LYS B O   1 
ATOM   1945 C  CB  . LYS B 1 97  ? -19.978 28.276 17.092  1.00 40.95  ? 97  LYS B CB  1 
ATOM   1946 C  CG  . LYS B 1 97  ? -20.812 28.119 15.816  1.00 43.16  ? 97  LYS B CG  1 
ATOM   1947 C  CD  . LYS B 1 97  ? -21.271 29.427 15.205  1.00 55.90  ? 97  LYS B CD  1 
ATOM   1948 C  CE  . LYS B 1 97  ? -22.638 29.383 14.541  1.00 74.11  ? 97  LYS B CE  1 
ATOM   1949 N  NZ  . LYS B 1 97  ? -22.953 28.093 13.875  1.00 80.89  ? 97  LYS B NZ  1 
ATOM   1950 N  N   . VAL B 1 98  ? -18.626 25.727 16.671  1.00 34.63  ? 98  VAL B N   1 
ATOM   1951 C  CA  . VAL B 1 98  ? -18.628 24.455 15.985  1.00 41.96  ? 98  VAL B CA  1 
ATOM   1952 C  C   . VAL B 1 98  ? -19.932 23.736 16.334  1.00 37.62  ? 98  VAL B C   1 
ATOM   1953 O  O   . VAL B 1 98  ? -20.480 23.927 17.413  1.00 40.25  ? 98  VAL B O   1 
ATOM   1954 C  CB  . VAL B 1 98  ? -17.411 23.616 16.365  1.00 40.09  ? 98  VAL B CB  1 
ATOM   1955 C  CG1 . VAL B 1 98  ? -17.396 23.401 17.881  1.00 43.02  ? 98  VAL B CG1 1 
ATOM   1956 C  CG2 . VAL B 1 98  ? -17.395 22.279 15.594  1.00 47.45  ? 98  VAL B CG2 1 
ATOM   1957 N  N   . ARG B 1 99  ? -20.434 22.969 15.367  1.00 37.12  ? 99  ARG B N   1 
ATOM   1958 C  CA  . ARG B 1 99  ? -21.709 22.312 15.496  1.00 34.91  ? 99  ARG B CA  1 
ATOM   1959 C  C   . ARG B 1 99  ? -21.458 20.814 15.412  1.00 36.75  ? 99  ARG B C   1 
ATOM   1960 O  O   . ARG B 1 99  ? -20.760 20.350 14.529  1.00 44.43  ? 99  ARG B O   1 
ATOM   1961 C  CB  . ARG B 1 99  ? -22.660 22.826 14.423  1.00 39.85  ? 99  ARG B CB  1 
ATOM   1962 C  CG  . ARG B 1 99  ? -23.897 21.964 14.253  1.00 44.74  ? 99  ARG B CG  1 
ATOM   1963 C  CD  . ARG B 1 99  ? -24.959 22.628 13.399  1.00 47.09  ? 99  ARG B CD  1 
ATOM   1964 N  NE  . ARG B 1 99  ? -25.923 21.589 13.116  1.00 46.59  ? 99  ARG B NE  1 
ATOM   1965 C  CZ  . ARG B 1 99  ? -27.177 21.768 12.751  1.00 42.63  ? 99  ARG B CZ  1 
ATOM   1966 N  NH1 . ARG B 1 99  ? -27.650 22.965 12.474  1.00 50.36  ? 99  ARG B NH1 1 
ATOM   1967 N  NH2 . ARG B 1 99  ? -27.944 20.712 12.593  1.00 44.82  ? 99  ARG B NH2 1 
ATOM   1968 N  N   . PHE B 1 100 ? -22.038 20.078 16.349  1.00 37.13  ? 100 PHE B N   1 
ATOM   1969 C  CA  . PHE B 1 100 ? -22.053 18.625 16.300  1.00 37.42  ? 100 PHE B CA  1 
ATOM   1970 C  C   . PHE B 1 100 ? -23.502 18.180 16.250  1.00 40.62  ? 100 PHE B C   1 
ATOM   1971 O  O   . PHE B 1 100 ? -24.317 18.700 17.001  1.00 46.34  ? 100 PHE B O   1 
ATOM   1972 C  CB  . PHE B 1 100 ? -21.403 18.049 17.554  1.00 35.41  ? 100 PHE B CB  1 
ATOM   1973 C  CG  . PHE B 1 100 ? -19.971 18.474 17.738  1.00 39.04  ? 100 PHE B CG  1 
ATOM   1974 C  CD1 . PHE B 1 100 ? -18.982 18.007 16.878  1.00 42.92  ? 100 PHE B CD1 1 
ATOM   1975 C  CD2 . PHE B 1 100 ? -19.635 19.407 18.709  1.00 42.81  ? 100 PHE B CD2 1 
ATOM   1976 C  CE1 . PHE B 1 100 ? -17.665 18.411 17.034  1.00 40.43  ? 100 PHE B CE1 1 
ATOM   1977 C  CE2 . PHE B 1 100 ? -18.316 19.798 18.889  1.00 39.71  ? 100 PHE B CE2 1 
ATOM   1978 C  CZ  . PHE B 1 100 ? -17.343 19.308 18.035  1.00 41.99  ? 100 PHE B CZ  1 
ATOM   1979 N  N   . ASP B 1 101 ? -23.814 17.226 15.384  1.00 37.55  ? 101 ASP B N   1 
ATOM   1980 C  CA  . ASP B 1 101 ? -25.125 16.610 15.419  1.00 40.99  ? 101 ASP B CA  1 
ATOM   1981 C  C   . ASP B 1 101 ? -25.049 15.372 16.314  1.00 42.03  ? 101 ASP B C   1 
ATOM   1982 O  O   . ASP B 1 101 ? -24.501 14.326 15.937  1.00 38.94  ? 101 ASP B O   1 
ATOM   1983 C  CB  . ASP B 1 101 ? -25.606 16.278 14.015  1.00 37.77  ? 101 ASP B CB  1 
ATOM   1984 C  CG  . ASP B 1 101 ? -26.026 17.504 13.220  1.00 49.92  ? 101 ASP B CG  1 
ATOM   1985 O  OD1 . ASP B 1 101 ? -26.242 18.603 13.801  1.00 42.70  ? 101 ASP B OD1 1 
ATOM   1986 O  OD2 . ASP B 1 101 ? -26.134 17.342 12.019  1.00 64.48  ? 101 ASP B OD2 1 
ATOM   1987 N  N   . TYR B 1 102 ? -25.616 15.514 17.508  1.00 37.04  ? 102 TYR B N   1 
ATOM   1988 C  CA  . TYR B 1 102 ? -25.418 14.498 18.515  1.00 36.87  ? 102 TYR B CA  1 
ATOM   1989 C  C   . TYR B 1 102 ? -26.555 13.488 18.426  1.00 37.83  ? 102 TYR B C   1 
ATOM   1990 O  O   . TYR B 1 102 ? -27.737 13.837 18.469  1.00 36.25  ? 102 TYR B O   1 
ATOM   1991 C  CB  . TYR B 1 102 ? -25.321 15.098 19.914  1.00 36.39  ? 102 TYR B CB  1 
ATOM   1992 C  CG  . TYR B 1 102 ? -24.930 14.008 20.895  1.00 33.65  ? 102 TYR B CG  1 
ATOM   1993 C  CD1 . TYR B 1 102 ? -23.604 13.630 21.053  1.00 33.40  ? 102 TYR B CD1 1 
ATOM   1994 C  CD2 . TYR B 1 102 ? -25.895 13.290 21.591  1.00 32.58  ? 102 TYR B CD2 1 
ATOM   1995 C  CE1 . TYR B 1 102 ? -23.242 12.577 21.880  1.00 34.76  ? 102 TYR B CE1 1 
ATOM   1996 C  CE2 . TYR B 1 102 ? -25.543 12.249 22.444  1.00 35.31  ? 102 TYR B CE2 1 
ATOM   1997 C  CZ  . TYR B 1 102 ? -24.212 11.889 22.579  1.00 35.98  ? 102 TYR B CZ  1 
ATOM   1998 O  OH  . TYR B 1 102 ? -23.841 10.881 23.392  1.00 41.64  ? 102 TYR B OH  1 
ATOM   1999 N  N   . ASP B 1 103 ? -26.189 12.206 18.378  1.00 38.32  ? 103 ASP B N   1 
ATOM   2000 C  CA  . ASP B 1 103 ? -27.205 11.167 18.318  1.00 38.03  ? 103 ASP B CA  1 
ATOM   2001 C  C   . ASP B 1 103 ? -27.629 10.839 19.739  1.00 33.96  ? 103 ASP B C   1 
ATOM   2002 O  O   . ASP B 1 103 ? -26.972 10.069 20.408  1.00 34.59  ? 103 ASP B O   1 
ATOM   2003 C  CB  . ASP B 1 103 ? -26.694 9.903  17.631  1.00 36.80  ? 103 ASP B CB  1 
ATOM   2004 C  CG  . ASP B 1 103 ? -27.748 8.818  17.417  1.00 45.80  ? 103 ASP B CG  1 
ATOM   2005 O  OD1 . ASP B 1 103 ? -28.865 8.915  17.962  1.00 44.12  ? 103 ASP B OD1 1 
ATOM   2006 O  OD2 . ASP B 1 103 ? -27.456 7.873  16.673  1.00 52.56  ? 103 ASP B OD2 1 
ATOM   2007 N  N   . LEU B 1 104 ? -28.748 11.396 20.184  1.00 35.66  ? 104 LEU B N   1 
ATOM   2008 C  CA  . LEU B 1 104 ? -29.266 11.082 21.505  1.00 36.33  ? 104 LEU B CA  1 
ATOM   2009 C  C   . LEU B 1 104 ? -30.183 9.868  21.396  1.00 37.20  ? 104 LEU B C   1 
ATOM   2010 O  O   . LEU B 1 104 ? -31.345 10.018 21.055  1.00 36.55  ? 104 LEU B O   1 
ATOM   2011 C  CB  . LEU B 1 104 ? -30.058 12.257 22.071  1.00 33.23  ? 104 LEU B CB  1 
ATOM   2012 C  CG  . LEU B 1 104 ? -30.496 12.016 23.506  1.00 41.45  ? 104 LEU B CG  1 
ATOM   2013 C  CD1 . LEU B 1 104 ? -29.318 12.265 24.408  1.00 50.00  ? 104 LEU B CD1 1 
ATOM   2014 C  CD2 . LEU B 1 104 ? -31.630 12.911 23.902  1.00 48.71  ? 104 LEU B CD2 1 
ATOM   2015 N  N   . PHE B 1 105 ? -29.621 8.685  21.628  1.00 35.40  ? 105 PHE B N   1 
ATOM   2016 C  CA  . PHE B 1 105 ? -30.396 7.471  21.518  1.00 41.62  ? 105 PHE B CA  1 
ATOM   2017 C  C   . PHE B 1 105 ? -30.728 6.947  22.911  1.00 41.91  ? 105 PHE B C   1 
ATOM   2018 O  O   . PHE B 1 105 ? -29.977 7.164  23.867  1.00 41.85  ? 105 PHE B O   1 
ATOM   2019 C  CB  . PHE B 1 105 ? -29.663 6.450  20.647  1.00 38.95  ? 105 PHE B CB  1 
ATOM   2020 C  CG  . PHE B 1 105 ? -28.303 6.071  21.153  1.00 41.76  ? 105 PHE B CG  1 
ATOM   2021 C  CD1 . PHE B 1 105 ? -28.148 4.963  21.977  1.00 46.37  ? 105 PHE B CD1 1 
ATOM   2022 C  CD2 . PHE B 1 105 ? -27.170 6.770  20.759  1.00 39.82  ? 105 PHE B CD2 1 
ATOM   2023 C  CE1 . PHE B 1 105 ? -26.902 4.614  22.467  1.00 44.93  ? 105 PHE B CE1 1 
ATOM   2024 C  CE2 . PHE B 1 105 ? -25.913 6.387  21.214  1.00 42.35  ? 105 PHE B CE2 1 
ATOM   2025 C  CZ  . PHE B 1 105 ? -25.777 5.314  22.056  1.00 39.38  ? 105 PHE B CZ  1 
ATOM   2026 N  N   . LEU B 1 106 ? -31.848 6.221  22.968  1.00 37.37  ? 106 LEU B N   1 
ATOM   2027 C  CA  . LEU B 1 106 ? -32.348 5.499  24.137  1.00 44.93  ? 106 LEU B CA  1 
ATOM   2028 C  C   . LEU B 1 106 ? -32.210 4.000  23.906  1.00 43.62  ? 106 LEU B C   1 
ATOM   2029 O  O   . LEU B 1 106 ? -32.039 3.585  22.779  1.00 52.08  ? 106 LEU B O   1 
ATOM   2030 C  CB  . LEU B 1 106 ? -33.816 5.864  24.375  1.00 43.24  ? 106 LEU B CB  1 
ATOM   2031 C  CG  . LEU B 1 106 ? -34.089 7.370  24.392  1.00 42.24  ? 106 LEU B CG  1 
ATOM   2032 C  CD1 . LEU B 1 106 ? -35.546 7.674  24.635  1.00 43.07  ? 106 LEU B CD1 1 
ATOM   2033 C  CD2 . LEU B 1 106 ? -33.253 8.044  25.440  1.00 42.73  ? 106 LEU B CD2 1 
ATOM   2034 N  N   . HIS B 1 107 ? -32.178 3.221  24.984  1.00 55.31  ? 107 HIS B N   1 
ATOM   2035 C  CA  . HIS B 1 107 ? -32.331 1.776  24.911  1.00 61.84  ? 107 HIS B CA  1 
ATOM   2036 C  C   . HIS B 1 107 ? -33.695 1.446  25.499  1.00 66.02  ? 107 HIS B C   1 
ATOM   2037 O  O   . HIS B 1 107 ? -34.198 2.212  26.329  1.00 60.63  ? 107 HIS B O   1 
ATOM   2038 C  CB  . HIS B 1 107 ? -31.209 1.035  25.646  1.00 59.18  ? 107 HIS B CB  1 
ATOM   2039 C  CG  . HIS B 1 107 ? -29.875 1.039  24.937  1.00 70.34  ? 107 HIS B CG  1 
ATOM   2040 N  ND1 . HIS B 1 107 ? -28.706 0.588  25.525  1.00 60.92  ? 107 HIS B ND1 1 
ATOM   2041 C  CD2 . HIS B 1 107 ? -29.518 1.476  23.706  1.00 61.70  ? 107 HIS B CD2 1 
ATOM   2042 C  CE1 . HIS B 1 107 ? -27.706 0.704  24.662  1.00 53.11  ? 107 HIS B CE1 1 
ATOM   2043 N  NE2 . HIS B 1 107 ? -28.170 1.256  23.561  1.00 61.74  ? 107 HIS B NE2 1 
ATOM   2044 N  N   . LEU B 1 108 ? -34.287 0.319  25.080  1.00 77.94  ? 108 LEU B N   1 
ATOM   2045 C  CA  . LEU B 1 108 ? -35.576 -0.088 25.627  1.00 82.48  ? 108 LEU B CA  1 
ATOM   2046 C  C   . LEU B 1 108 ? -35.341 -0.847 26.920  1.00 84.47  ? 108 LEU B C   1 
ATOM   2047 O  O   . LEU B 1 108 ? -34.243 -1.340 27.138  1.00 96.96  ? 108 LEU B O   1 
ATOM   2048 C  CB  . LEU B 1 108 ? -36.347 -0.947 24.624  1.00 79.93  ? 108 LEU B CB  1 
ATOM   2049 C  CG  . LEU B 1 108 ? -36.856 -0.231 23.367  1.00 88.05  ? 108 LEU B CG  1 
ATOM   2050 C  CD1 . LEU B 1 108 ? -37.840 -1.118 22.612  1.00 94.40  ? 108 LEU B CD1 1 
ATOM   2051 C  CD2 . LEU B 1 108 ? -37.529 1.113  23.658  1.00 90.71  ? 108 LEU B CD2 1 
ATOM   2052 N  N   . GLU B 1 109 ? -36.380 -0.945 27.756  1.00 93.08  ? 109 GLU B N   1 
ATOM   2053 C  CA  . GLU B 1 109 ? -36.244 -1.722 28.972  1.00 93.65  ? 109 GLU B CA  1 
ATOM   2054 C  C   . GLU B 1 109 ? -35.904 -3.151 28.577  1.00 79.08  ? 109 GLU B C   1 
ATOM   2055 O  O   . GLU B 1 109 ? -36.305 -3.617 27.523  1.00 69.44  ? 109 GLU B O   1 
ATOM   2056 C  CB  . GLU B 1 109 ? -37.476 -1.674 29.871  1.00 101.48 ? 109 GLU B CB  1 
ATOM   2057 C  CG  . GLU B 1 109 ? -37.190 -2.275 31.244  1.00 119.04 ? 109 GLU B CG  1 
ATOM   2058 C  CD  . GLU B 1 109 ? -37.533 -1.414 32.450  1.00 135.00 ? 109 GLU B CD  1 
ATOM   2059 O  OE1 . GLU B 1 109 ? -38.733 -1.216 32.723  1.00 151.48 ? 109 GLU B OE1 1 
ATOM   2060 O  OE2 . GLU B 1 109 ? -36.587 -0.937 33.109  1.00 129.50 ? 109 GLU B OE2 1 
ATOM   2061 N  N   . GLY B 1 110 ? -35.096 -3.797 29.415  1.00 83.70  ? 110 GLY B N   1 
ATOM   2062 C  CA  . GLY B 1 110 ? -34.558 -5.106 29.113  1.00 81.87  ? 110 GLY B CA  1 
ATOM   2063 C  C   . GLY B 1 110 ? -33.096 -4.978 28.722  1.00 88.48  ? 110 GLY B C   1 
ATOM   2064 O  O   . GLY B 1 110 ? -32.296 -5.843 29.036  1.00 103.53 ? 110 GLY B O   1 
ATOM   2065 N  N   . HIS B 1 111 ? -32.768 -3.865 28.066  1.00 94.44  ? 111 HIS B N   1 
ATOM   2066 C  CA  . HIS B 1 111 ? -31.407 -3.565 27.667  1.00 90.13  ? 111 HIS B CA  1 
ATOM   2067 C  C   . HIS B 1 111 ? -30.818 -2.637 28.716  1.00 79.07  ? 111 HIS B C   1 
ATOM   2068 O  O   . HIS B 1 111 ? -31.552 -1.922 29.395  1.00 69.84  ? 111 HIS B O   1 
ATOM   2069 C  CB  . HIS B 1 111 ? -31.380 -2.895 26.287  1.00 97.09  ? 111 HIS B CB  1 
ATOM   2070 C  CG  . HIS B 1 111 ? -31.978 -3.738 25.225  1.00 92.79  ? 111 HIS B CG  1 
ATOM   2071 N  ND1 . HIS B 1 111 ? -33.331 -3.997 25.177  1.00 92.14  ? 111 HIS B ND1 1 
ATOM   2072 C  CD2 . HIS B 1 111 ? -31.423 -4.372 24.195  1.00 87.51  ? 111 HIS B CD2 1 
ATOM   2073 C  CE1 . HIS B 1 111 ? -33.578 -4.777 24.141  1.00 87.66  ? 111 HIS B CE1 1 
ATOM   2074 N  NE2 . HIS B 1 111 ? -32.433 -5.023 23.541  1.00 90.88  ? 111 HIS B NE2 1 
ATOM   2075 N  N   . PRO B 1 112 ? -29.479 -2.586 28.853  1.00 74.50  ? 112 PRO B N   1 
ATOM   2076 C  CA  . PRO B 1 112 ? -28.867 -1.738 29.871  1.00 76.46  ? 112 PRO B CA  1 
ATOM   2077 C  C   . PRO B 1 112 ? -29.027 -0.253 29.549  1.00 68.49  ? 112 PRO B C   1 
ATOM   2078 O  O   . PRO B 1 112 ? -29.258 0.151  28.409  1.00 58.39  ? 112 PRO B O   1 
ATOM   2079 C  CB  . PRO B 1 112 ? -27.386 -2.131 29.870  1.00 76.24  ? 112 PRO B CB  1 
ATOM   2080 C  CG  . PRO B 1 112 ? -27.165 -2.727 28.479  1.00 74.30  ? 112 PRO B CG  1 
ATOM   2081 C  CD  . PRO B 1 112 ? -28.494 -3.301 28.026  1.00 71.50  ? 112 PRO B CD  1 
ATOM   2082 N  N   . PRO B 1 113 ? -28.902 0.611  30.568  1.00 68.99  ? 113 PRO B N   1 
ATOM   2083 C  CA  . PRO B 1 113 ? -28.988 2.050  30.351  1.00 61.67  ? 113 PRO B CA  1 
ATOM   2084 C  C   . PRO B 1 113 ? -27.894 2.527  29.403  1.00 52.83  ? 113 PRO B C   1 
ATOM   2085 O  O   . PRO B 1 113 ? -26.860 1.901  29.215  1.00 51.13  ? 113 PRO B O   1 
ATOM   2086 C  CB  . PRO B 1 113 ? -28.778 2.685  31.735  1.00 64.05  ? 113 PRO B CB  1 
ATOM   2087 C  CG  . PRO B 1 113 ? -28.884 1.554  32.728  1.00 70.39  ? 113 PRO B CG  1 
ATOM   2088 C  CD  . PRO B 1 113 ? -28.664 0.254  31.971  1.00 77.06  ? 113 PRO B CD  1 
ATOM   2089 N  N   . VAL B 1 114 ? -28.157 3.651  28.758  1.00 56.28  ? 114 VAL B N   1 
ATOM   2090 C  CA  . VAL B 1 114 ? -27.173 4.229  27.873  1.00 48.95  ? 114 VAL B CA  1 
ATOM   2091 C  C   . VAL B 1 114 ? -26.199 5.051  28.708  1.00 46.64  ? 114 VAL B C   1 
ATOM   2092 O  O   . VAL B 1 114 ? -26.603 5.885  29.539  1.00 46.84  ? 114 VAL B O   1 
ATOM   2093 C  CB  . VAL B 1 114 ? -27.840 5.063  26.781  1.00 44.56  ? 114 VAL B CB  1 
ATOM   2094 C  CG1 . VAL B 1 114 ? -26.800 5.718  25.905  1.00 47.92  ? 114 VAL B CG1 1 
ATOM   2095 C  CG2 . VAL B 1 114 ? -28.766 4.213  25.943  1.00 47.41  ? 114 VAL B CG2 1 
ATOM   2096 N  N   . ASN B 1 115 ? -24.914 4.833  28.435  1.00 48.44  ? 115 ASN B N   1 
ATOM   2097 C  CA  . ASN B 1 115 ? -23.865 5.742  28.887  1.00 53.68  ? 115 ASN B CA  1 
ATOM   2098 C  C   . ASN B 1 115 ? -22.891 5.872  27.736  1.00 50.62  ? 115 ASN B C   1 
ATOM   2099 O  O   . ASN B 1 115 ? -22.113 4.972  27.500  1.00 52.14  ? 115 ASN B O   1 
ATOM   2100 C  CB  . ASN B 1 115 ? -23.179 5.258  30.159  1.00 59.06  ? 115 ASN B CB  1 
ATOM   2101 C  CG  . ASN B 1 115 ? -22.185 6.245  30.724  1.00 72.21  ? 115 ASN B CG  1 
ATOM   2102 O  OD1 . ASN B 1 115 ? -22.067 7.380  30.272  1.00 79.35  ? 115 ASN B OD1 1 
ATOM   2103 N  ND2 . ASN B 1 115 ? -21.453 5.818  31.731  1.00 77.40  ? 115 ASN B ND2 1 
ATOM   2104 N  N   . HIS B 1 116 ? -23.043 6.927  26.943  1.00 48.76  ? 116 HIS B N   1 
ATOM   2105 C  CA  . HIS B 1 116 ? -22.280 7.027  25.716  1.00 45.66  ? 116 HIS B CA  1 
ATOM   2106 C  C   . HIS B 1 116 ? -21.295 8.179  25.845  1.00 43.46  ? 116 HIS B C   1 
ATOM   2107 O  O   . HIS B 1 116 ? -21.587 9.186  26.481  1.00 39.12  ? 116 HIS B O   1 
ATOM   2108 C  CB  . HIS B 1 116 ? -23.184 7.305  24.519  1.00 45.08  ? 116 HIS B CB  1 
ATOM   2109 C  CG  . HIS B 1 116 ? -22.472 7.260  23.216  1.00 43.39  ? 116 HIS B CG  1 
ATOM   2110 N  ND1 . HIS B 1 116 ? -22.082 6.080  22.618  1.00 42.01  ? 116 HIS B ND1 1 
ATOM   2111 C  CD2 . HIS B 1 116 ? -22.091 8.259  22.396  1.00 40.74  ? 116 HIS B CD2 1 
ATOM   2112 C  CE1 . HIS B 1 116 ? -21.526 6.357  21.442  1.00 43.99  ? 116 HIS B CE1 1 
ATOM   2113 N  NE2 . HIS B 1 116 ? -21.491 7.677  21.300  1.00 47.01  ? 116 HIS B NE2 1 
ATOM   2114 N  N   . LEU B 1 117 ? -20.139 8.010  25.205  1.00 47.11  ? 117 LEU B N   1 
ATOM   2115 C  CA  . LEU B 1 117 ? -19.127 9.044  25.180  1.00 50.28  ? 117 LEU B CA  1 
ATOM   2116 C  C   . LEU B 1 117 ? -18.622 9.178  23.758  1.00 44.00  ? 117 LEU B C   1 
ATOM   2117 O  O   . LEU B 1 117 ? -18.280 8.202  23.131  1.00 41.43  ? 117 LEU B O   1 
ATOM   2118 C  CB  . LEU B 1 117 ? -17.994 8.678  26.140  1.00 51.04  ? 117 LEU B CB  1 
ATOM   2119 C  CG  . LEU B 1 117 ? -16.875 9.717  26.221  1.00 63.29  ? 117 LEU B CG  1 
ATOM   2120 C  CD1 . LEU B 1 117 ? -17.360 11.009 26.862  1.00 59.50  ? 117 LEU B CD1 1 
ATOM   2121 C  CD2 . LEU B 1 117 ? -15.673 9.147  26.956  1.00 64.63  ? 117 LEU B CD2 1 
ATOM   2122 N  N   . ARG B 1 118 ? -18.568 10.413 23.287  1.00 37.94  ? 118 ARG B N   1 
ATOM   2123 C  CA  . ARG B 1 118 ? -18.042 10.736 21.984  1.00 38.00  ? 118 ARG B CA  1 
ATOM   2124 C  C   . ARG B 1 118 ? -16.969 11.797 22.156  1.00 45.59  ? 118 ARG B C   1 
ATOM   2125 O  O   . ARG B 1 118 ? -17.235 12.898 22.653  1.00 45.09  ? 118 ARG B O   1 
ATOM   2126 C  CB  . ARG B 1 118 ? -19.235 11.188 21.148  1.00 42.79  ? 118 ARG B CB  1 
ATOM   2127 C  CG  . ARG B 1 118 ? -18.868 11.831 19.826  1.00 39.55  ? 118 ARG B CG  1 
ATOM   2128 C  CD  . ARG B 1 118 ? -20.136 12.354 19.190  1.00 40.72  ? 118 ARG B CD  1 
ATOM   2129 N  NE  . ARG B 1 118 ? -19.815 13.166 18.049  1.00 37.23  ? 118 ARG B NE  1 
ATOM   2130 C  CZ  . ARG B 1 118 ? -20.677 13.653 17.186  1.00 38.89  ? 118 ARG B CZ  1 
ATOM   2131 N  NH1 . ARG B 1 118 ? -21.966 13.357 17.261  1.00 38.59  ? 118 ARG B NH1 1 
ATOM   2132 N  NH2 . ARG B 1 118 ? -20.227 14.478 16.258  1.00 40.66  ? 118 ARG B NH2 1 
ATOM   2133 N  N   . CYS B 1 119 ? -15.755 11.436 21.752  1.00 44.01  ? 119 CYS B N   1 
ATOM   2134 C  CA  . CYS B 1 119 ? -14.612 12.324 21.790  1.00 44.09  ? 119 CYS B CA  1 
ATOM   2135 C  C   . CYS B 1 119 ? -14.563 13.114 20.501  1.00 41.72  ? 119 CYS B C   1 
ATOM   2136 O  O   . CYS B 1 119 ? -14.833 12.595 19.443  1.00 39.77  ? 119 CYS B O   1 
ATOM   2137 C  CB  . CYS B 1 119 ? -13.324 11.534 21.971  1.00 48.31  ? 119 CYS B CB  1 
ATOM   2138 S  SG  . CYS B 1 119 ? -13.305 10.671 23.561  1.00 56.17  ? 119 CYS B SG  1 
ATOM   2139 N  N   . GLU B 1 120 ? -14.236 14.392 20.617  1.00 41.56  ? 120 GLU B N   1 
ATOM   2140 C  CA  . GLU B 1 120 ? -14.103 15.251 19.460  1.00 44.02  ? 120 GLU B CA  1 
ATOM   2141 C  C   . GLU B 1 120 ? -12.835 16.067 19.659  1.00 49.77  ? 120 GLU B C   1 
ATOM   2142 O  O   . GLU B 1 120 ? -12.511 16.403 20.788  1.00 53.47  ? 120 GLU B O   1 
ATOM   2143 C  CB  . GLU B 1 120 ? -15.346 16.128 19.323  1.00 41.10  ? 120 GLU B CB  1 
ATOM   2144 C  CG  . GLU B 1 120 ? -16.579 15.352 18.877  1.00 49.51  ? 120 GLU B CG  1 
ATOM   2145 C  CD  . GLU B 1 120 ? -16.607 14.959 17.411  1.00 43.69  ? 120 GLU B CD  1 
ATOM   2146 O  OE1 . GLU B 1 120 ? -15.748 15.425 16.665  1.00 52.78  ? 120 GLU B OE1 1 
ATOM   2147 O  OE2 . GLU B 1 120 ? -17.493 14.191 17.018  1.00 59.64  ? 120 GLU B OE2 1 
ATOM   2148 N  N   . LYS B 1 121 ? -12.110 16.344 18.578  1.00 50.06  ? 121 LYS B N   1 
ATOM   2149 C  CA  . LYS B 1 121 ? -10.920 17.169 18.640  1.00 49.56  ? 121 LYS B CA  1 
ATOM   2150 C  C   . LYS B 1 121 ? -11.167 18.398 17.796  1.00 47.13  ? 121 LYS B C   1 
ATOM   2151 O  O   . LYS B 1 121 ? -11.521 18.265 16.648  1.00 50.76  ? 121 LYS B O   1 
ATOM   2152 C  CB  . LYS B 1 121 ? -9.728  16.491 17.983  1.00 64.73  ? 121 LYS B CB  1 
ATOM   2153 C  CG  . LYS B 1 121 ? -9.020  15.430 18.806  1.00 80.96  ? 121 LYS B CG  1 
ATOM   2154 C  CD  . LYS B 1 121 ? -7.794  14.913 18.074  1.00 97.51  ? 121 LYS B CD  1 
ATOM   2155 C  CE  . LYS B 1 121 ? -6.727  14.386 19.005  1.00 111.07 ? 121 LYS B CE  1 
ATOM   2156 N  NZ  . LYS B 1 121 ? -6.152  15.484 19.817  1.00 122.20 ? 121 LYS B NZ  1 
ATOM   2157 N  N   . LEU B 1 122 ? -11.014 19.581 18.365  1.00 38.69  ? 122 LEU B N   1 
ATOM   2158 C  CA  . LEU B 1 122 ? -11.008 20.777 17.552  1.00 41.99  ? 122 LEU B CA  1 
ATOM   2159 C  C   . LEU B 1 122 ? -9.571  21.181 17.228  1.00 45.24  ? 122 LEU B C   1 
ATOM   2160 O  O   . LEU B 1 122 ? -8.695  21.070 18.089  1.00 45.76  ? 122 LEU B O   1 
ATOM   2161 C  CB  . LEU B 1 122 ? -11.645 21.872 18.389  1.00 47.20  ? 122 LEU B CB  1 
ATOM   2162 C  CG  . LEU B 1 122 ? -13.038 21.550 18.914  1.00 52.31  ? 122 LEU B CG  1 
ATOM   2163 C  CD1 . LEU B 1 122 ? -13.580 22.732 19.690  1.00 51.93  ? 122 LEU B CD1 1 
ATOM   2164 C  CD2 . LEU B 1 122 ? -13.970 21.195 17.778  1.00 57.61  ? 122 LEU B CD2 1 
ATOM   2165 N  N   . THR B 1 123 ? -9.368  21.707 16.018  1.00 44.72  ? 123 THR B N   1 
ATOM   2166 C  CA  . THR B 1 123 ? -8.087  22.245 15.590  1.00 41.56  ? 123 THR B CA  1 
ATOM   2167 C  C   . THR B 1 123 ? -8.271  23.711 15.237  1.00 43.97  ? 123 THR B C   1 
ATOM   2168 O  O   . THR B 1 123 ? -9.101  24.039 14.415  1.00 44.58  ? 123 THR B O   1 
ATOM   2169 C  CB  . THR B 1 123 ? -7.514  21.417 14.442  1.00 50.71  ? 123 THR B CB  1 
ATOM   2170 O  OG1 . THR B 1 123 ? -7.491  20.056 14.910  1.00 50.02  ? 123 THR B OG1 1 
ATOM   2171 C  CG2 . THR B 1 123 ? -6.114  21.858 14.046  1.00 51.86  ? 123 THR B CG2 1 
ATOM   2172 N  N   . PHE B 1 124 ? -7.524  24.608 15.886  1.00 42.16  ? 124 PHE B N   1 
ATOM   2173 C  CA  . PHE B 1 124 ? -7.533  25.993 15.455  1.00 44.03  ? 124 PHE B CA  1 
ATOM   2174 C  C   . PHE B 1 124 ? -6.168  26.352 14.879  1.00 52.71  ? 124 PHE B C   1 
ATOM   2175 O  O   . PHE B 1 124 ? -5.151  26.198 15.563  1.00 48.62  ? 124 PHE B O   1 
ATOM   2176 C  CB  . PHE B 1 124 ? -7.856  26.916 16.605  1.00 41.22  ? 124 PHE B CB  1 
ATOM   2177 C  CG  . PHE B 1 124 ? -9.170  26.633 17.263  1.00 48.74  ? 124 PHE B CG  1 
ATOM   2178 C  CD1 . PHE B 1 124 ? -9.266  25.676 18.259  1.00 45.11  ? 124 PHE B CD1 1 
ATOM   2179 C  CD2 . PHE B 1 124 ? -10.315 27.294 16.854  1.00 51.97  ? 124 PHE B CD2 1 
ATOM   2180 C  CE1 . PHE B 1 124 ? -10.484 25.396 18.863  1.00 46.25  ? 124 PHE B CE1 1 
ATOM   2181 C  CE2 . PHE B 1 124 ? -11.530 27.022 17.468  1.00 54.36  ? 124 PHE B CE2 1 
ATOM   2182 C  CZ  . PHE B 1 124 ? -11.609 26.067 18.469  1.00 51.62  ? 124 PHE B CZ  1 
ATOM   2183 N  N   . ASN B 1 125 ? -6.155  26.798 13.610  1.00 48.78  ? 125 ASN B N   1 
ATOM   2184 C  CA  . ASN B 1 125 ? -4.915  27.171 12.926  1.00 45.25  ? 125 ASN B CA  1 
ATOM   2185 C  C   . ASN B 1 125 ? -4.689  28.670 13.070  1.00 44.08  ? 125 ASN B C   1 
ATOM   2186 O  O   . ASN B 1 125 ? -5.556  29.464 12.756  1.00 48.16  ? 125 ASN B O   1 
ATOM   2187 C  CB  . ASN B 1 125 ? -4.928  26.729 11.469  1.00 46.76  ? 125 ASN B CB  1 
ATOM   2188 C  CG  . ASN B 1 125 ? -4.914  25.213 11.374  1.00 52.54  ? 125 ASN B CG  1 
ATOM   2189 O  OD1 . ASN B 1 125 ? -4.139  24.538 12.042  1.00 57.84  ? 125 ASN B OD1 1 
ATOM   2190 N  ND2 . ASN B 1 125 ? -5.801  24.646 10.582  1.00 65.42  ? 125 ASN B ND2 1 
ATOM   2191 N  N   . ASN B 1 126 ? -3.551  29.032 13.637  1.00 42.43  ? 126 ASN B N   1 
ATOM   2192 C  CA  . ASN B 1 126 ? -3.150  30.416 13.815  1.00 50.20  ? 126 ASN B CA  1 
ATOM   2193 C  C   . ASN B 1 126 ? -4.259  31.236 14.415  1.00 46.58  ? 126 ASN B C   1 
ATOM   2194 O  O   . ASN B 1 126 ? -4.659  32.229 13.840  1.00 68.70  ? 126 ASN B O   1 
ATOM   2195 C  CB  . ASN B 1 126 ? -2.698  31.008 12.486  1.00 54.12  ? 126 ASN B CB  1 
ATOM   2196 C  CG  . ASN B 1 126 ? -1.566  30.170 11.949  1.00 54.79  ? 126 ASN B CG  1 
ATOM   2197 O  OD1 . ASN B 1 126 ? -0.515  30.077 12.588  1.00 56.11  ? 126 ASN B OD1 1 
ATOM   2198 N  ND2 . ASN B 1 126 ? -1.830  29.476 10.858  1.00 53.61  ? 126 ASN B ND2 1 
ATOM   2199 N  N   . PRO B 1 127 ? -4.773  30.871 15.598  1.00 51.38  ? 127 PRO B N   1 
ATOM   2200 C  CA  . PRO B 1 127 ? -5.728  31.742 16.276  1.00 48.58  ? 127 PRO B CA  1 
ATOM   2201 C  C   . PRO B 1 127 ? -5.052  33.060 16.610  1.00 40.38  ? 127 PRO B C   1 
ATOM   2202 O  O   . PRO B 1 127 ? -3.847  33.094 16.716  1.00 50.27  ? 127 PRO B O   1 
ATOM   2203 C  CB  . PRO B 1 127 ? -6.073  30.970 17.567  1.00 51.14  ? 127 PRO B CB  1 
ATOM   2204 C  CG  . PRO B 1 127 ? -4.947  29.954 17.727  1.00 52.35  ? 127 PRO B CG  1 
ATOM   2205 C  CD  . PRO B 1 127 ? -4.499  29.614 16.321  1.00 48.12  ? 127 PRO B CD  1 
ATOM   2206 N  N   . THR B 1 128 ? -5.833  34.079 16.914  1.00 41.07  ? 128 THR B N   1 
ATOM   2207 C  CA  . THR B 1 128 ? -5.319  35.321 17.434  1.00 52.11  ? 128 THR B CA  1 
ATOM   2208 C  C   . THR B 1 128 ? -4.609  35.041 18.738  1.00 60.15  ? 128 THR B C   1 
ATOM   2209 O  O   . THR B 1 128 ? -4.808  33.995 19.347  1.00 59.05  ? 128 THR B O   1 
ATOM   2210 C  CB  . THR B 1 128 ? -6.390  36.347 17.819  1.00 52.62  ? 128 THR B CB  1 
ATOM   2211 O  OG1 . THR B 1 128 ? -7.174  35.731 18.847  1.00 56.55  ? 128 THR B OG1 1 
ATOM   2212 C  CG2 . THR B 1 128 ? -7.218  36.805 16.642  1.00 52.65  ? 128 THR B CG2 1 
ATOM   2213 N  N   . GLU B 1 129 ? -3.863  36.049 19.178  1.00 60.05  ? 129 GLU B N   1 
ATOM   2214 C  CA  . GLU B 1 129 ? -3.131  35.940 20.419  1.00 66.51  ? 129 GLU B CA  1 
ATOM   2215 C  C   . GLU B 1 129 ? -4.096  35.711 21.583  1.00 56.11  ? 129 GLU B C   1 
ATOM   2216 O  O   . GLU B 1 129 ? -3.870  34.820 22.399  1.00 53.59  ? 129 GLU B O   1 
ATOM   2217 C  CB  . GLU B 1 129 ? -2.269  37.183 20.605  1.00 60.65  ? 129 GLU B CB  1 
ATOM   2218 C  CG  . GLU B 1 129 ? -1.391  37.077 21.832  1.00 72.02  ? 129 GLU B CG  1 
ATOM   2219 C  CD  . GLU B 1 129 ? -0.355  38.181 21.925  1.00 86.36  ? 129 GLU B CD  1 
ATOM   2220 O  OE1 . GLU B 1 129 ? 0.493   38.266 21.012  1.00 88.60  ? 129 GLU B OE1 1 
ATOM   2221 O  OE2 . GLU B 1 129 ? -0.438  38.979 22.873  1.00 81.72  ? 129 GLU B OE2 1 
ATOM   2222 N  N   . ASP B 1 130 ? -5.160  36.518 21.650  1.00 58.65  ? 130 ASP B N   1 
ATOM   2223 C  CA  . ASP B 1 130 ? -6.108  36.478 22.767  1.00 59.39  ? 130 ASP B CA  1 
ATOM   2224 C  C   . ASP B 1 130 ? -6.704  35.087 22.917  1.00 53.81  ? 130 ASP B C   1 
ATOM   2225 O  O   . ASP B 1 130 ? -6.730  34.511 24.006  1.00 50.26  ? 130 ASP B O   1 
ATOM   2226 C  CB  . ASP B 1 130 ? -7.319  37.388 22.568  1.00 68.25  ? 130 ASP B CB  1 
ATOM   2227 C  CG  . ASP B 1 130 ? -6.915  38.720 21.989  1.00 85.80  ? 130 ASP B CG  1 
ATOM   2228 O  OD1 . ASP B 1 130 ? -6.288  39.485 22.735  1.00 81.78  ? 130 ASP B OD1 1 
ATOM   2229 O  OD2 . ASP B 1 130 ? -7.156  38.933 20.773  1.00 112.68 ? 130 ASP B OD2 1 
ATOM   2230 N  N   . PHE B 1 131 ? -7.165  34.577 21.774  1.00 48.59  ? 131 PHE B N   1 
ATOM   2231 C  CA  . PHE B 1 131 ? -7.833  33.304 21.717  1.00 49.60  ? 131 PHE B CA  1 
ATOM   2232 C  C   . PHE B 1 131 ? -6.850  32.182 22.007  1.00 48.63  ? 131 PHE B C   1 
ATOM   2233 O  O   . PHE B 1 131 ? -7.192  31.227 22.710  1.00 56.05  ? 131 PHE B O   1 
ATOM   2234 C  CB  . PHE B 1 131 ? -8.515  33.143 20.355  1.00 48.64  ? 131 PHE B CB  1 
ATOM   2235 C  CG  . PHE B 1 131 ? -9.464  31.976 20.313  1.00 50.28  ? 131 PHE B CG  1 
ATOM   2236 C  CD1 . PHE B 1 131 ? -10.299 31.705 21.393  1.00 46.37  ? 131 PHE B CD1 1 
ATOM   2237 C  CD2 . PHE B 1 131 ? -9.514  31.145 19.200  1.00 47.57  ? 131 PHE B CD2 1 
ATOM   2238 C  CE1 . PHE B 1 131 ? -11.126 30.595 21.360  1.00 46.98  ? 131 PHE B CE1 1 
ATOM   2239 C  CE2 . PHE B 1 131 ? -10.388 30.076 19.152  1.00 45.01  ? 131 PHE B CE2 1 
ATOM   2240 C  CZ  . PHE B 1 131 ? -11.173 29.791 20.238  1.00 46.42  ? 131 PHE B CZ  1 
ATOM   2241 N  N   . ARG B 1 132 ? -5.633  32.310 21.460  1.00 49.70  ? 132 ARG B N   1 
ATOM   2242 C  CA  . ARG B 1 132 ? -4.629  31.276 21.597  1.00 47.02  ? 132 ARG B CA  1 
ATOM   2243 C  C   . ARG B 1 132 ? -4.382  31.093 23.087  1.00 42.50  ? 132 ARG B C   1 
ATOM   2244 O  O   . ARG B 1 132 ? -4.273  29.960 23.570  1.00 41.19  ? 132 ARG B O   1 
ATOM   2245 C  CB  . ARG B 1 132 ? -3.331  31.616 20.842  1.00 56.03  ? 132 ARG B CB  1 
ATOM   2246 C  CG  . ARG B 1 132 ? -2.255  30.530 20.915  1.00 59.58  ? 132 ARG B CG  1 
ATOM   2247 C  CD  . ARG B 1 132 ? -0.920  30.885 20.257  1.00 53.56  ? 132 ARG B CD  1 
ATOM   2248 N  NE  . ARG B 1 132 ? -0.346  32.124 20.757  1.00 58.66  ? 132 ARG B NE  1 
ATOM   2249 C  CZ  . ARG B 1 132 ? -0.202  33.238 20.051  1.00 51.25  ? 132 ARG B CZ  1 
ATOM   2250 N  NH1 . ARG B 1 132 ? -0.628  33.330 18.806  1.00 55.12  ? 132 ARG B NH1 1 
ATOM   2251 N  NH2 . ARG B 1 132 ? 0.361   34.282 20.606  1.00 48.74  ? 132 ARG B NH2 1 
ATOM   2252 N  N   . ARG B 1 133 ? -4.357  32.208 23.820  1.00 38.27  ? 133 ARG B N   1 
ATOM   2253 C  CA  . ARG B 1 133 ? -4.066  32.121 25.246  1.00 51.95  ? 133 ARG B CA  1 
ATOM   2254 C  C   . ARG B 1 133 ? -5.235  31.475 25.982  1.00 47.36  ? 133 ARG B C   1 
ATOM   2255 O  O   . ARG B 1 133 ? -5.034  30.726 26.942  1.00 43.79  ? 133 ARG B O   1 
ATOM   2256 C  CB  . ARG B 1 133 ? -3.704  33.496 25.810  1.00 53.01  ? 133 ARG B CB  1 
ATOM   2257 C  CG  . ARG B 1 133 ? -2.333  33.934 25.326  1.00 61.71  ? 133 ARG B CG  1 
ATOM   2258 C  CD  . ARG B 1 133 ? -1.971  35.347 25.725  1.00 60.46  ? 133 ARG B CD  1 
ATOM   2259 N  NE  . ARG B 1 133 ? -0.806  35.774 24.966  1.00 73.62  ? 133 ARG B NE  1 
ATOM   2260 C  CZ  . ARG B 1 133 ? 0.130   36.612 25.394  1.00 78.35  ? 133 ARG B CZ  1 
ATOM   2261 N  NH1 . ARG B 1 133 ? 0.115   37.030 26.644  1.00 82.81  ? 133 ARG B NH1 1 
ATOM   2262 N  NH2 . ARG B 1 133 ? 1.066   37.046 24.561  1.00 77.64  ? 133 ARG B NH2 1 
ATOM   2263 N  N   . LYS B 1 134 ? -6.458  31.776 25.524  1.00 44.48  ? 134 LYS B N   1 
ATOM   2264 C  CA  . LYS B 1 134 ? -7.639  31.212 26.155  1.00 44.31  ? 134 LYS B CA  1 
ATOM   2265 C  C   . LYS B 1 134 ? -7.618  29.701 25.959  1.00 42.01  ? 134 LYS B C   1 
ATOM   2266 O  O   . LYS B 1 134 ? -7.733  28.953 26.932  1.00 43.66  ? 134 LYS B O   1 
ATOM   2267 C  CB  . LYS B 1 134 ? -8.900  31.895 25.626  1.00 44.93  ? 134 LYS B CB  1 
ATOM   2268 C  CG  . LYS B 1 134 ? -9.144  33.292 26.193  1.00 49.33  ? 134 LYS B CG  1 
ATOM   2269 C  CD  . LYS B 1 134 ? -10.500 33.832 25.759  1.00 50.46  ? 134 LYS B CD  1 
ATOM   2270 C  CE  . LYS B 1 134 ? -10.805 35.174 26.364  1.00 58.75  ? 134 LYS B CE  1 
ATOM   2271 N  NZ  . LYS B 1 134 ? -10.042 36.212 25.651  1.00 66.55  ? 134 LYS B NZ  1 
ATOM   2272 N  N   . LEU B 1 135 ? -7.372  29.268 24.714  1.00 39.88  ? 135 LEU B N   1 
ATOM   2273 C  CA  . LEU B 1 135 ? -7.391  27.851 24.417  1.00 37.84  ? 135 LEU B CA  1 
ATOM   2274 C  C   . LEU B 1 135 ? -6.389  27.157 25.319  1.00 42.08  ? 135 LEU B C   1 
ATOM   2275 O  O   . LEU B 1 135 ? -6.611  26.004 25.754  1.00 43.23  ? 135 LEU B O   1 
ATOM   2276 C  CB  . LEU B 1 135 ? -7.056  27.620 22.939  1.00 41.15  ? 135 LEU B CB  1 
ATOM   2277 C  CG  . LEU B 1 135 ? -8.103  28.135 21.944  1.00 39.94  ? 135 LEU B CG  1 
ATOM   2278 C  CD1 . LEU B 1 135 ? -7.545  28.234 20.542  1.00 35.61  ? 135 LEU B CD1 1 
ATOM   2279 C  CD2 . LEU B 1 135 ? -9.337  27.245 21.919  1.00 37.12  ? 135 LEU B CD2 1 
ATOM   2280 N  N   . LEU B 1 136 ? -5.240  27.827 25.531  1.00 40.34  ? 136 LEU B N   1 
ATOM   2281 C  CA  . LEU B 1 136 ? -4.112  27.105 26.085  1.00 47.04  ? 136 LEU B CA  1 
ATOM   2282 C  C   . LEU B 1 136 ? -4.147  27.174 27.611  1.00 49.24  ? 136 LEU B C   1 
ATOM   2283 O  O   . LEU B 1 136 ? -3.453  26.408 28.257  1.00 48.40  ? 136 LEU B O   1 
ATOM   2284 C  CB  . LEU B 1 136 ? -2.828  27.618 25.440  1.00 50.46  ? 136 LEU B CB  1 
ATOM   2285 C  CG  . LEU B 1 136 ? -2.585  27.056 24.034  1.00 51.54  ? 136 LEU B CG  1 
ATOM   2286 C  CD1 . LEU B 1 136 ? -1.380  27.696 23.362  1.00 50.02  ? 136 LEU B CD1 1 
ATOM   2287 C  CD2 . LEU B 1 136 ? -2.402  25.537 24.072  1.00 50.04  ? 136 LEU B CD2 1 
ATOM   2288 N  N   . LYS B 1 137 ? -5.087  27.942 28.168  1.00 44.62  ? 137 LYS B N   1 
ATOM   2289 C  CA  . LYS B 1 137 ? -5.418  27.778 29.571  1.00 45.29  ? 137 LYS B CA  1 
ATOM   2290 C  C   . LYS B 1 137 ? -6.222  26.512 29.837  1.00 43.27  ? 137 LYS B C   1 
ATOM   2291 O  O   . LYS B 1 137 ? -6.267  26.141 30.998  1.00 50.70  ? 137 LYS B O   1 
ATOM   2292 C  CB  . LYS B 1 137 ? -6.201  28.970 30.112  1.00 46.97  ? 137 LYS B CB  1 
ATOM   2293 C  CG  . LYS B 1 137 ? -5.369  30.186 30.454  1.00 51.87  ? 137 LYS B CG  1 
ATOM   2294 C  CD  . LYS B 1 137 ? -6.272  31.358 30.754  1.00 62.05  ? 137 LYS B CD  1 
ATOM   2295 C  CE  . LYS B 1 137 ? -5.565  32.470 31.501  1.00 80.83  ? 137 LYS B CE  1 
ATOM   2296 N  NZ  . LYS B 1 137 ? -6.021  33.804 31.032  1.00 84.55  ? 137 LYS B NZ  1 
ATOM   2297 N  N   . ALA B 1 138 ? -6.763  25.821 28.802  1.00 45.62  ? 138 ALA B N   1 
ATOM   2298 C  CA  . ALA B 1 138 ? -7.645  24.665 29.007  1.00 48.12  ? 138 ALA B CA  1 
ATOM   2299 C  C   . ALA B 1 138 ? -6.921  23.311 28.987  1.00 57.02  ? 138 ALA B C   1 
ATOM   2300 O  O   . ALA B 1 138 ? -5.963  23.176 28.214  1.00 59.47  ? 138 ALA B O   1 
ATOM   2301 C  CB  . ALA B 1 138 ? -8.747  24.624 27.973  1.00 55.56  ? 138 ALA B CB  1 
ATOM   2302 O  OXT . ALA B 1 138 ? -7.413  22.387 29.697  1.00 58.51  ? 138 ALA B OXT 1 
ATOM   2303 N  N   . LEU C 2 1   ? 35.319  28.372 20.108  1.00 34.60  ? 1   LEU C N   1 
ATOM   2304 C  CA  . LEU C 2 1   ? 34.321  29.273 19.444  1.00 36.53  ? 1   LEU C CA  1 
ATOM   2305 C  C   . LEU C 2 1   ? 34.958  30.624 19.119  1.00 39.11  ? 1   LEU C C   1 
ATOM   2306 O  O   . LEU C 2 1   ? 35.657  31.123 19.986  1.00 36.01  ? 1   LEU C O   1 
ATOM   2307 C  CB  . LEU C 2 1   ? 33.098  29.476 20.349  1.00 42.47  ? 1   LEU C CB  1 
ATOM   2308 C  CG  . LEU C 2 1   ? 31.756  28.811 19.990  1.00 50.62  ? 1   LEU C CG  1 
ATOM   2309 C  CD1 . LEU C 2 1   ? 31.900  27.380 19.514  1.00 48.71  ? 1   LEU C CD1 1 
ATOM   2310 C  CD2 . LEU C 2 1   ? 30.764  28.859 21.166  1.00 39.76  ? 1   LEU C CD2 1 
ATOM   2311 N  N   . THR C 2 2   ? 34.570  31.241 17.968  1.00 35.89  ? 2   THR C N   1 
ATOM   2312 C  CA  . THR C 2 2   ? 35.173  32.439 17.429  1.00 39.86  ? 2   THR C CA  1 
ATOM   2313 C  C   . THR C 2 2   ? 34.107  33.402 16.936  1.00 33.92  ? 2   THR C C   1 
ATOM   2314 O  O   . THR C 2 2   ? 33.311  33.029 16.068  1.00 37.85  ? 2   THR C O   1 
ATOM   2315 C  CB  . THR C 2 2   ? 36.066  32.098 16.229  1.00 41.41  ? 2   THR C CB  1 
ATOM   2316 O  OG1 . THR C 2 2   ? 36.979  31.109 16.675  1.00 40.11  ? 2   THR C OG1 1 
ATOM   2317 C  CG2 . THR C 2 2   ? 36.831  33.273 15.677  1.00 43.94  ? 2   THR C CG2 1 
HETATM 2318 N  N   . KCR C 2 3   ? 34.137  34.632 17.413  1.00 41.59  ? 3   KCR C N   1 
HETATM 2319 C  CA  . KCR C 2 3   ? 33.298  35.606 16.767  1.00 39.27  ? 3   KCR C CA  1 
HETATM 2320 C  CB  . KCR C 2 3   ? 33.186  36.897 17.566  1.00 40.71  ? 3   KCR C CB  1 
HETATM 2321 C  CG  . KCR C 2 3   ? 32.814  36.635 19.008  1.00 44.31  ? 3   KCR C CG  1 
HETATM 2322 C  CD  . KCR C 2 3   ? 32.861  37.838 19.867  1.00 45.65  ? 3   KCR C CD  1 
HETATM 2323 C  CE  . KCR C 2 3   ? 32.772  37.417 21.319  1.00 43.39  ? 3   KCR C CE  1 
HETATM 2324 N  NZ  . KCR C 2 3   ? 32.149  38.468 22.094  1.00 43.32  ? 3   KCR C NZ  1 
HETATM 2325 C  CH  . KCR C 2 3   ? 31.889  38.312 23.363  1.00 43.58  ? 3   KCR C CH  1 
HETATM 2326 O  OH  . KCR C 2 3   ? 32.333  37.344 23.971  1.00 40.15  ? 3   KCR C OH  1 
HETATM 2327 C  CX  . KCR C 2 3   ? 31.204  39.352 23.891  1.00 46.78  ? 3   KCR C CX  1 
HETATM 2328 C  CY  . KCR C 2 3   ? 31.107  39.630 25.170  1.00 58.09  ? 3   KCR C CY  1 
HETATM 2329 C  CH3 . KCR C 2 3   ? 30.568  40.915 25.715  1.00 64.95  ? 3   KCR C CH3 1 
HETATM 2330 C  C   . KCR C 2 3   ? 33.932  35.921 15.436  1.00 37.22  ? 3   KCR C C   1 
HETATM 2331 O  O   . KCR C 2 3   ? 35.128  35.973 15.355  1.00 45.62  ? 3   KCR C O   1 
ATOM   2332 N  N   . PRO C 2 4   ? 33.156  36.413 14.510  1.00 48.15  ? 4   PRO C N   1 
ATOM   2333 C  CA  . PRO C 2 4   ? 33.761  36.677 13.235  1.00 49.21  ? 4   PRO C CA  1 
ATOM   2334 C  C   . PRO C 2 4   ? 34.122  38.168 13.264  1.00 46.21  ? 4   PRO C C   1 
ATOM   2335 O  O   . PRO C 2 4   ? 33.492  38.971 13.942  1.00 42.05  ? 4   PRO C O   1 
ATOM   2336 C  CB  . PRO C 2 4   ? 32.737  36.317 12.153  1.00 47.08  ? 4   PRO C CB  1 
ATOM   2337 C  CG  . PRO C 2 4   ? 31.497  36.045 12.899  1.00 47.11  ? 4   PRO C CG  1 
ATOM   2338 C  CD  . PRO C 2 4   ? 32.028  35.522 14.207  1.00 48.33  ? 4   PRO C CD  1 
ATOM   2339 N  N   . THR C 2 5   ? 35.128  38.539 12.477  1.00 51.78  ? 5   THR C N   1 
ATOM   2340 C  CA  . THR C 2 5   ? 35.577  39.919 12.383  1.00 45.91  ? 5   THR C CA  1 
ATOM   2341 C  C   . THR C 2 5   ? 34.538  40.804 11.711  1.00 44.99  ? 5   THR C C   1 
ATOM   2342 O  O   . THR C 2 5   ? 33.686  40.389 10.956  1.00 54.60  ? 5   THR C O   1 
ATOM   2343 C  CB  . THR C 2 5   ? 36.840  40.042 11.543  1.00 64.58  ? 5   THR C CB  1 
ATOM   2344 O  OG1 . THR C 2 5   ? 36.261  39.676 10.291  1.00 67.27  ? 5   THR C OG1 1 
ATOM   2345 C  CG2 . THR C 2 5   ? 37.980  39.154 12.021  1.00 67.14  ? 5   THR C CG2 1 
ATOM   2346 N  N   . LEU C 2 6   ? 34.578  42.069 12.050  1.00 50.12  ? 6   LEU C N   1 
ATOM   2347 C  CA  . LEU C 2 6   ? 33.614  43.012 11.557  1.00 57.02  ? 6   LEU C CA  1 
ATOM   2348 C  C   . LEU C 2 6   ? 34.090  43.627 10.243  1.00 62.23  ? 6   LEU C C   1 
ATOM   2349 O  O   . LEU C 2 6   ? 33.431  44.552 9.771   1.00 71.34  ? 6   LEU C O   1 
ATOM   2350 C  CB  . LEU C 2 6   ? 33.384  44.064 12.646  1.00 59.57  ? 6   LEU C CB  1 
ATOM   2351 C  CG  . LEU C 2 6   ? 32.110  43.849 13.479  1.00 83.80  ? 6   LEU C CG  1 
ATOM   2352 C  CD1 . LEU C 2 6   ? 32.303  42.863 14.642  1.00 69.15  ? 6   LEU C CD1 1 
ATOM   2353 C  CD2 . LEU C 2 6   ? 31.583  45.181 13.993  1.00 94.72  ? 6   LEU C CD2 1 
ATOM   2354 N  N   . LYS C 2 7   ? 35.174  43.106 9.638   1.00 60.06  ? 7   LYS C N   1 
ATOM   2355 C  CA  . LYS C 2 7   ? 35.639  43.553 8.318   1.00 62.07  ? 7   LYS C CA  1 
ATOM   2356 C  C   . LYS C 2 7   ? 34.579  43.381 7.213   1.00 57.76  ? 7   LYS C C   1 
ATOM   2357 O  O   . LYS C 2 7   ? 34.194  42.265 6.869   1.00 54.56  ? 7   LYS C O   1 
ATOM   2358 C  CB  . LYS C 2 7   ? 36.937  42.839 7.920   1.00 71.16  ? 7   LYS C CB  1 
ATOM   2359 C  CG  . LYS C 2 7   ? 37.656  43.420 6.700   1.00 77.32  ? 7   LYS C CG  1 
ATOM   2360 C  CD  . LYS C 2 7   ? 39.085  42.915 6.470   1.00 77.01  ? 7   LYS C CD  1 
ATOM   2361 C  CE  . LYS C 2 7   ? 39.215  41.450 6.088   1.00 77.51  ? 7   LYS C CE  1 
ATOM   2362 N  NZ  . LYS C 2 7   ? 38.403  41.099 4.897   1.00 89.61  ? 7   LYS C NZ  1 
ATOM   2363 N  N   . ARG C 2 8   ? 34.156  44.503 6.586   1.00 49.72  ? 8   ARG C N   1 
ATOM   2364 C  CA  . ARG C 2 8   ? 33.085  44.494 5.581   1.00 45.13  ? 8   ARG C CA  1 
ATOM   2365 C  C   . ARG C 2 8   ? 33.620  44.052 4.215   1.00 38.03  ? 8   ARG C C   1 
ATOM   2366 O  O   . ARG C 2 8   ? 34.777  44.292 3.873   1.00 37.92  ? 8   ARG C O   1 
ATOM   2367 C  CB  . ARG C 2 8   ? 32.416  45.866 5.516   1.00 47.62  ? 8   ARG C CB  1 
ATOM   2368 C  CG  . ARG C 2 8   ? 31.170  45.925 4.647   1.00 64.10  ? 8   ARG C CG  1 
ATOM   2369 C  CD  . ARG C 2 8   ? 29.891  45.287 5.179   1.00 59.16  ? 8   ARG C CD  1 
ATOM   2370 N  NE  . ARG C 2 8   ? 28.745  45.545 4.291   1.00 62.93  ? 8   ARG C NE  1 
ATOM   2371 C  CZ  . ARG C 2 8   ? 28.213  46.753 4.047   1.00 69.81  ? 8   ARG C CZ  1 
ATOM   2372 N  NH1 . ARG C 2 8   ? 27.257  46.918 3.140   1.00 68.17  ? 8   ARG C NH1 1 
ATOM   2373 N  NH2 . ARG C 2 8   ? 28.667  47.816 4.691   1.00 70.80  ? 8   ARG C NH2 1 
ATOM   2374 N  N   . LYS C 2 9   ? 32.806  43.290 3.483   1.00 42.98  ? 9   LYS C N   1 
ATOM   2375 C  CA  . LYS C 2 9   ? 33.223  42.717 2.222   1.00 46.81  ? 9   LYS C CA  1 
ATOM   2376 C  C   . LYS C 2 9   ? 32.249  43.111 1.107   1.00 41.78  ? 9   LYS C C   1 
ATOM   2377 O  O   . LYS C 2 9   ? 31.089  43.402 1.327   1.00 39.24  ? 9   LYS C O   1 
ATOM   2378 C  CB  . LYS C 2 9   ? 33.403  41.203 2.354   1.00 53.30  ? 9   LYS C CB  1 
ATOM   2379 C  CG  . LYS C 2 9   ? 34.843  40.818 2.630   1.00 57.71  ? 9   LYS C CG  1 
ATOM   2380 C  CD  . LYS C 2 9   ? 35.080  39.345 2.778   1.00 68.29  ? 9   LYS C CD  1 
ATOM   2381 C  CE  . LYS C 2 9   ? 34.984  38.895 4.220   1.00 80.93  ? 9   LYS C CE  1 
ATOM   2382 N  NZ  . LYS C 2 9   ? 35.832  37.706 4.454   1.00 80.82  ? 9   LYS C NZ  1 
HETATM 2383 N  N   . KCR C 2 10  ? 32.771  43.163 -0.087  1.00 37.68  ? 10  KCR C N   1 
HETATM 2384 C  CA  . KCR C 2 10  ? 31.902  43.504 -1.190  1.00 45.92  ? 10  KCR C CA  1 
HETATM 2385 C  CB  . KCR C 2 10  ? 32.769  43.834 -2.413  1.00 46.41  ? 10  KCR C CB  1 
HETATM 2386 C  CG  . KCR C 2 10  ? 33.580  45.108 -2.241  1.00 45.64  ? 10  KCR C CG  1 
HETATM 2387 C  CD  . KCR C 2 10  ? 32.732  46.228 -2.688  1.00 45.93  ? 10  KCR C CD  1 
HETATM 2388 C  CE  . KCR C 2 10  ? 33.407  47.548 -2.463  1.00 47.21  ? 10  KCR C CE  1 
HETATM 2389 N  NZ  . KCR C 2 10  ? 32.554  48.578 -2.966  1.00 45.00  ? 10  KCR C NZ  1 
HETATM 2390 C  CH  . KCR C 2 10  ? 32.262  49.697 -2.336  1.00 45.96  ? 10  KCR C CH  1 
HETATM 2391 O  OH  . KCR C 2 10  ? 32.881  50.086 -1.338  1.00 35.41  ? 10  KCR C OH  1 
HETATM 2392 C  CX  . KCR C 2 10  ? 31.352  50.331 -3.067  1.00 55.90  ? 10  KCR C CX  1 
HETATM 2393 C  CY  . KCR C 2 10  ? 30.846  51.527 -3.180  1.00 58.68  ? 10  KCR C CY  1 
HETATM 2394 C  CH3 . KCR C 2 10  ? 30.018  51.908 -4.375  1.00 54.58  ? 10  KCR C CH3 1 
HETATM 2395 C  C   . KCR C 2 10  ? 30.971  42.331 -1.469  1.00 42.47  ? 10  KCR C C   1 
HETATM 2396 O  O   . KCR C 2 10  ? 31.410  41.209 -1.335  1.00 47.57  ? 10  KCR C O   1 
ATOM   2397 N  N   . PRO C 2 11  ? 29.678  42.599 -1.676  1.00 52.38  ? 11  PRO C N   1 
ATOM   2398 C  CA  . PRO C 2 11  ? 28.721  41.659 -2.281  1.00 55.20  ? 11  PRO C CA  1 
ATOM   2399 C  C   . PRO C 2 11  ? 29.185  40.902 -3.533  1.00 52.34  ? 11  PRO C C   1 
ATOM   2400 O  O   . PRO C 2 11  ? 29.993  41.361 -4.341  1.00 51.14  ? 11  PRO C O   1 
ATOM   2401 C  CB  . PRO C 2 11  ? 27.544  42.588 -2.635  1.00 60.54  ? 11  PRO C CB  1 
ATOM   2402 C  CG  . PRO C 2 11  ? 28.230  43.831 -3.180  1.00 55.14  ? 11  PRO C CG  1 
ATOM   2403 C  CD  . PRO C 2 11  ? 29.660  43.716 -2.667  1.00 52.59  ? 11  PRO C CD  1 
ATOM   2404 N  N   . PHE C 2 12  ? 28.642  39.706 -3.691  1.00 59.72  ? 12  PHE C N   1 
ATOM   2405 C  CA  . PHE C 2 12  ? 28.987  38.867 -4.824  1.00 67.92  ? 12  PHE C CA  1 
ATOM   2406 C  C   . PHE C 2 12  ? 27.864  37.850 -4.972  1.00 68.87  ? 12  PHE C C   1 
ATOM   2407 O  O   . PHE C 2 12  ? 27.165  37.598 -3.999  1.00 71.79  ? 12  PHE C O   1 
ATOM   2408 C  CB  . PHE C 2 12  ? 30.368  38.242 -4.589  1.00 68.27  ? 12  PHE C CB  1 
ATOM   2409 C  CG  . PHE C 2 12  ? 30.411  37.239 -3.455  1.00 84.10  ? 12  PHE C CG  1 
ATOM   2410 C  CD1 . PHE C 2 12  ? 29.795  35.990 -3.607  1.00 57.01  ? 12  PHE C CD1 1 
ATOM   2411 C  CD2 . PHE C 2 12  ? 31.025  37.550 -2.234  1.00 74.29  ? 12  PHE C CD2 1 
ATOM   2412 C  CE1 . PHE C 2 12  ? 29.833  35.060 -2.586  1.00 53.65  ? 12  PHE C CE1 1 
ATOM   2413 C  CE2 . PHE C 2 12  ? 31.016  36.627 -1.193  1.00 75.38  ? 12  PHE C CE2 1 
ATOM   2414 C  CZ  . PHE C 2 12  ? 30.416  35.387 -1.376  1.00 61.71  ? 12  PHE C CZ  1 
ATOM   2415 N  N   . LEU C 2 13  ? 27.772  37.223 -6.152  1.00 89.93  ? 13  LEU C N   1 
ATOM   2416 C  CA  . LEU C 2 13  ? 26.650  36.383 -6.549  1.00 84.06  ? 13  LEU C CA  1 
ATOM   2417 C  C   . LEU C 2 13  ? 26.976  34.891 -6.328  1.00 77.67  ? 13  LEU C C   1 
ATOM   2418 O  O   . LEU C 2 13  ? 26.010  34.100 -5.969  1.00 56.11  ? 13  LEU C O   1 
ATOM   2419 C  CB  . LEU C 2 13  ? 26.352  36.730 -8.017  1.00 83.61  ? 13  LEU C CB  1 
ATOM   2420 C  CG  . LEU C 2 13  ? 26.122  38.220 -8.307  1.00 78.02  ? 13  LEU C CG  1 
ATOM   2421 C  CD1 . LEU C 2 13  ? 26.151  38.513 -9.799  1.00 74.27  ? 13  LEU C CD1 1 
ATOM   2422 C  CD2 . LEU C 2 13  ? 24.811  38.702 -7.692  1.00 78.93  ? 13  LEU C CD2 1 
HETATM 2423 LI LI  . LI  D 3 .   ? 20.460  35.731 18.308  1.00 9.22   ? 201 LI  A LI  1 
HETATM 2424 N  N   . NO3 E 4 .   ? 32.619  31.593 -13.864 1.00 93.18  ? 202 NO3 A N   1 
HETATM 2425 O  O1  . NO3 E 4 .   ? 32.448  31.333 -15.057 1.00 105.75 ? 202 NO3 A O1  1 
HETATM 2426 O  O2  . NO3 E 4 .   ? 33.690  31.323 -13.329 1.00 80.19  ? 202 NO3 A O2  1 
HETATM 2427 O  O3  . NO3 E 4 .   ? 31.719  32.141 -13.215 1.00 95.97  ? 202 NO3 A O3  1 
HETATM 2428 N  N   . NO3 F 4 .   ? 21.707  36.504 4.678   1.00 78.24  ? 203 NO3 A N   1 
HETATM 2429 O  O1  . NO3 F 4 .   ? 20.796  36.400 3.818   1.00 69.49  ? 203 NO3 A O1  1 
HETATM 2430 O  O2  . NO3 F 4 .   ? 22.867  36.558 4.287   1.00 76.00  ? 203 NO3 A O2  1 
HETATM 2431 O  O3  . NO3 F 4 .   ? 21.461  36.557 5.920   1.00 61.14  ? 203 NO3 A O3  1 
HETATM 2432 C  C1  . PEG G 5 .   ? 31.477  28.962 -8.106  1.00 61.17  ? 204 PEG A C1  1 
HETATM 2433 O  O1  . PEG G 5 .   ? 31.258  28.147 -7.076  1.00 43.85  ? 204 PEG A O1  1 
HETATM 2434 C  C2  . PEG G 5 .   ? 30.502  28.689 -9.224  1.00 74.09  ? 204 PEG A C2  1 
HETATM 2435 O  O2  . PEG G 5 .   ? 31.137  28.724 -10.500 1.00 50.53  ? 204 PEG A O2  1 
HETATM 2436 C  C3  . PEG G 5 .   ? 31.864  29.924 -10.736 1.00 62.94  ? 204 PEG A C3  1 
HETATM 2437 C  C4  . PEG G 5 .   ? 31.145  31.156 -10.195 1.00 52.27  ? 204 PEG A C4  1 
HETATM 2438 O  O4  . PEG G 5 .   ? 32.016  32.157 -9.873  1.00 52.60  ? 204 PEG A O4  1 
HETATM 2439 C  C1  . GOL H 6 .   ? 36.967  35.093 12.021  1.00 74.16  ? 205 GOL A C1  1 
HETATM 2440 O  O1  . GOL H 6 .   ? 36.359  35.916 11.016  1.00 59.56  ? 205 GOL A O1  1 
HETATM 2441 C  C2  . GOL H 6 .   ? 38.477  34.951 11.891  1.00 69.12  ? 205 GOL A C2  1 
HETATM 2442 O  O2  . GOL H 6 .   ? 39.086  35.153 13.162  1.00 76.54  ? 205 GOL A O2  1 
HETATM 2443 C  C3  . GOL H 6 .   ? 38.937  33.604 11.366  1.00 66.69  ? 205 GOL A C3  1 
HETATM 2444 O  O3  . GOL H 6 .   ? 40.121  33.687 10.567  1.00 67.25  ? 205 GOL A O3  1 
HETATM 2445 C  C1  . GOL I 6 .   ? 40.073  31.342 7.123   1.00 72.88  ? 206 GOL A C1  1 
HETATM 2446 O  O1  . GOL I 6 .   ? 39.866  32.138 8.287   1.00 52.62  ? 206 GOL A O1  1 
HETATM 2447 C  C2  . GOL I 6 .   ? 41.272  31.754 6.283   1.00 68.53  ? 206 GOL A C2  1 
HETATM 2448 O  O2  . GOL I 6 .   ? 42.093  30.609 6.064   1.00 65.69  ? 206 GOL A O2  1 
HETATM 2449 C  C3  . GOL I 6 .   ? 40.919  32.425 4.957   1.00 74.42  ? 206 GOL A C3  1 
HETATM 2450 O  O3  . GOL I 6 .   ? 40.050  31.663 4.112   1.00 57.38  ? 206 GOL A O3  1 
HETATM 2451 C  C1  . GOL J 6 .   ? -0.956  18.531 18.595  1.00 87.10  ? 207 GOL A C1  1 
HETATM 2452 O  O1  . GOL J 6 .   ? -1.439  19.847 18.314  1.00 81.61  ? 207 GOL A O1  1 
HETATM 2453 C  C2  . GOL J 6 .   ? 0.500   18.553 19.007  1.00 91.50  ? 207 GOL A C2  1 
HETATM 2454 O  O2  . GOL J 6 .   ? 0.668   19.515 20.045  1.00 98.04  ? 207 GOL A O2  1 
HETATM 2455 C  C3  . GOL J 6 .   ? 1.036   17.215 19.473  1.00 82.86  ? 207 GOL A C3  1 
HETATM 2456 O  O3  . GOL J 6 .   ? 0.624   16.933 20.807  1.00 82.67  ? 207 GOL A O3  1 
HETATM 2457 LI LI  . LI  K 3 .   ? -18.883 29.394 29.155  1.00 4.76   ? 201 LI  B LI  1 
HETATM 2458 N  N   . NO3 L 4 .   ? -26.432 2.912  19.160  1.00 111.12 ? 202 NO3 B N   1 
HETATM 2459 O  O1  . NO3 L 4 .   ? -27.274 3.638  18.627  1.00 94.33  ? 202 NO3 B O1  1 
HETATM 2460 O  O2  . NO3 L 4 .   ? -25.314 2.818  18.665  1.00 113.52 ? 202 NO3 B O2  1 
HETATM 2461 O  O3  . NO3 L 4 .   ? -26.700 2.285  20.193  1.00 104.25 ? 202 NO3 B O3  1 
HETATM 2462 N  N   . NO3 M 4 .   ? -21.231 16.783 32.516  1.00 66.00  ? 203 NO3 B N   1 
HETATM 2463 O  O1  . NO3 M 4 .   ? -20.596 17.766 32.082  1.00 62.32  ? 203 NO3 B O1  1 
HETATM 2464 O  O2  . NO3 M 4 .   ? -20.739 15.639 32.512  1.00 66.41  ? 203 NO3 B O2  1 
HETATM 2465 O  O3  . NO3 M 4 .   ? -22.360 16.946 32.954  1.00 66.12  ? 203 NO3 B O3  1 
HETATM 2466 C  C1  . GOL N 6 .   ? -12.651 12.069 32.067  1.00 66.28  ? 204 GOL B C1  1 
HETATM 2467 O  O1  . GOL N 6 .   ? -12.303 12.169 30.678  1.00 50.32  ? 204 GOL B O1  1 
HETATM 2468 C  C2  . GOL N 6 .   ? -14.050 12.575 32.389  1.00 59.84  ? 204 GOL B C2  1 
HETATM 2469 O  O2  . GOL N 6 .   ? -14.245 12.551 33.808  1.00 68.59  ? 204 GOL B O2  1 
HETATM 2470 C  C3  . GOL N 6 .   ? -14.404 13.940 31.778  1.00 74.44  ? 204 GOL B C3  1 
HETATM 2471 O  O3  . GOL N 6 .   ? -13.988 15.119 32.494  1.00 49.10  ? 204 GOL B O3  1 
HETATM 2472 O  O   . HOH O 7 .   ? 27.634  26.546 22.475  1.00 69.10  ? 301 HOH A O   1 
HETATM 2473 O  O   . HOH O 7 .   ? 39.495  25.362 -6.004  1.00 41.31  ? 302 HOH A O   1 
HETATM 2474 O  O   . HOH O 7 .   ? 21.371  35.620 21.652  1.00 42.27  ? 303 HOH A O   1 
HETATM 2475 O  O   . HOH O 7 .   ? 19.497  21.979 -0.496  1.00 49.55  ? 304 HOH A O   1 
HETATM 2476 O  O   . HOH O 7 .   ? 21.216  31.646 -1.486  1.00 39.18  ? 305 HOH A O   1 
HETATM 2477 O  O   . HOH O 7 .   ? 17.563  29.695 26.927  1.00 61.61  ? 306 HOH A O   1 
HETATM 2478 O  O   . HOH O 7 .   ? 20.795  35.826 9.117   1.00 40.47  ? 307 HOH A O   1 
HETATM 2479 O  O   . HOH O 7 .   ? 27.022  27.405 -11.328 1.00 44.08  ? 308 HOH A O   1 
HETATM 2480 O  O   . HOH O 7 .   ? 23.789  22.828 -0.122  1.00 36.28  ? 309 HOH A O   1 
HETATM 2481 O  O   . HOH O 7 .   ? 2.741   25.319 24.045  1.00 45.93  ? 310 HOH A O   1 
HETATM 2482 O  O   . HOH O 7 .   ? -5.266  18.787 22.847  1.00 49.39  ? 311 HOH A O   1 
HETATM 2483 O  O   . HOH O 7 .   ? 33.111  21.453 8.589   1.00 41.50  ? 312 HOH A O   1 
HETATM 2484 O  O   . HOH O 7 .   ? 4.872   27.042 30.120  1.00 57.37  ? 313 HOH A O   1 
HETATM 2485 O  O   . HOH O 7 .   ? 0.618   28.767 29.029  1.00 58.87  ? 314 HOH A O   1 
HETATM 2486 O  O   . HOH O 7 .   ? 36.999  35.201 7.582   1.00 63.93  ? 315 HOH A O   1 
HETATM 2487 O  O   . HOH O 7 .   ? 19.457  37.501 20.694  1.00 74.94  ? 316 HOH A O   1 
HETATM 2488 O  O   . HOH O 7 .   ? 21.535  25.844 -6.054  1.00 59.05  ? 317 HOH A O   1 
HETATM 2489 O  O   . HOH O 7 .   ? 19.603  18.464 15.543  1.00 47.47  ? 318 HOH A O   1 
HETATM 2490 O  O   . HOH O 7 .   ? 13.206  34.448 28.559  1.00 68.60  ? 319 HOH A O   1 
HETATM 2491 O  O   . HOH O 7 .   ? 43.308  35.219 1.404   1.00 73.05  ? 320 HOH A O   1 
HETATM 2492 O  O   . HOH O 7 .   ? 48.715  27.272 -2.060  1.00 66.95  ? 321 HOH A O   1 
HETATM 2493 O  O   . HOH O 7 .   ? 11.884  20.988 6.584   1.00 64.77  ? 322 HOH A O   1 
HETATM 2494 O  O   . HOH O 7 .   ? 37.754  38.101 -7.236  1.00 57.26  ? 323 HOH A O   1 
HETATM 2495 O  O   . HOH O 7 .   ? 34.239  36.241 -5.795  1.00 68.79  ? 324 HOH A O   1 
HETATM 2496 O  O   . HOH O 7 .   ? 36.926  19.364 9.525   1.00 46.32  ? 325 HOH A O   1 
HETATM 2497 O  O   . HOH O 7 .   ? 29.718  19.613 15.067  1.00 62.10  ? 326 HOH A O   1 
HETATM 2498 O  O   . HOH O 7 .   ? 18.483  27.032 -4.348  1.00 40.90  ? 327 HOH A O   1 
HETATM 2499 O  O   . HOH O 7 .   ? 34.010  34.365 10.030  1.00 44.43  ? 328 HOH A O   1 
HETATM 2500 O  O   . HOH O 7 .   ? 22.879  21.495 2.230   1.00 35.02  ? 329 HOH A O   1 
HETATM 2501 O  O   . HOH O 7 .   ? 45.731  36.989 -0.942  1.00 65.99  ? 330 HOH A O   1 
HETATM 2502 O  O   . HOH O 7 .   ? 7.340   29.297 30.266  1.00 57.12  ? 331 HOH A O   1 
HETATM 2503 O  O   . HOH O 7 .   ? 24.581  17.165 3.921   1.00 64.45  ? 332 HOH A O   1 
HETATM 2504 O  O   . HOH O 7 .   ? 40.036  31.838 -8.701  1.00 45.33  ? 333 HOH A O   1 
HETATM 2505 O  O   . HOH O 7 .   ? 21.066  18.087 7.570   1.00 41.36  ? 334 HOH A O   1 
HETATM 2506 O  O   . HOH O 7 .   ? 32.344  21.709 -4.015  1.00 38.05  ? 335 HOH A O   1 
HETATM 2507 O  O   . HOH O 7 .   ? 6.520   40.222 16.203  1.00 63.82  ? 336 HOH A O   1 
HETATM 2508 O  O   . HOH O 7 .   ? 32.441  35.945 8.418   1.00 42.17  ? 337 HOH A O   1 
HETATM 2509 O  O   . HOH O 7 .   ? 18.058  18.683 11.126  1.00 64.41  ? 338 HOH A O   1 
HETATM 2510 O  O   . HOH O 7 .   ? 8.697   35.274 25.854  1.00 58.85  ? 339 HOH A O   1 
HETATM 2511 O  O   . HOH O 7 .   ? 33.246  17.370 4.082   1.00 38.10  ? 340 HOH A O   1 
HETATM 2512 O  O   . HOH O 7 .   ? 34.631  22.498 13.029  1.00 61.02  ? 341 HOH A O   1 
HETATM 2513 O  O   . HOH O 7 .   ? 30.946  23.014 -11.589 1.00 43.03  ? 342 HOH A O   1 
HETATM 2514 O  O   . HOH O 7 .   ? 14.852  23.481 -0.075  1.00 58.68  ? 343 HOH A O   1 
HETATM 2515 O  O   . HOH O 7 .   ? 44.526  23.037 10.247  1.00 65.30  ? 344 HOH A O   1 
HETATM 2516 O  O   . HOH O 7 .   ? 33.371  35.977 1.303   1.00 53.59  ? 345 HOH A O   1 
HETATM 2517 O  O   . HOH O 7 .   ? 0.885   32.513 24.006  1.00 38.37  ? 346 HOH A O   1 
HETATM 2518 O  O   . HOH O 7 .   ? 23.544  27.203 -7.356  1.00 51.27  ? 347 HOH A O   1 
HETATM 2519 O  O   . HOH O 7 .   ? 25.579  25.947 24.707  1.00 60.20  ? 348 HOH A O   1 
HETATM 2520 O  O   . HOH O 7 .   ? 15.880  40.803 8.923   1.00 69.78  ? 349 HOH A O   1 
HETATM 2521 O  O   . HOH O 7 .   ? 18.054  30.073 -4.655  1.00 63.75  ? 350 HOH A O   1 
HETATM 2522 O  O   . HOH O 7 .   ? 35.591  17.597 3.539   1.00 53.24  ? 351 HOH A O   1 
HETATM 2523 O  O   . HOH O 7 .   ? 43.078  34.378 5.562   1.00 65.92  ? 352 HOH A O   1 
HETATM 2524 O  O   . HOH O 7 .   ? 22.810  20.695 -1.700  1.00 52.14  ? 353 HOH A O   1 
HETATM 2525 O  O   . HOH O 7 .   ? 39.924  29.532 -10.392 1.00 56.34  ? 354 HOH A O   1 
HETATM 2526 O  O   . HOH O 7 .   ? 35.022  30.346 -18.632 1.00 59.93  ? 355 HOH A O   1 
HETATM 2527 O  O   . HOH O 7 .   ? 31.445  19.591 -2.313  1.00 43.58  ? 356 HOH A O   1 
HETATM 2528 O  O   . HOH P 7 .   ? -10.197 31.738 31.675  1.00 62.23  ? 301 HOH B O   1 
HETATM 2529 O  O   . HOH P 7 .   ? -21.344 9.310  29.169  1.00 54.77  ? 302 HOH B O   1 
HETATM 2530 O  O   . HOH P 7 .   ? -19.892 20.269 31.077  1.00 40.81  ? 303 HOH B O   1 
HETATM 2531 O  O   . HOH P 7 .   ? -31.323 9.194  18.183  1.00 48.23  ? 304 HOH B O   1 
HETATM 2532 O  O   . HOH P 7 .   ? -45.092 8.220  25.513  1.00 66.63  ? 305 HOH B O   1 
HETATM 2533 O  O   . HOH P 7 .   ? -23.577 4.589  18.980  1.00 60.81  ? 306 HOH B O   1 
HETATM 2534 O  O   . HOH P 7 .   ? -25.374 12.309 14.690  1.00 52.91  ? 307 HOH B O   1 
HETATM 2535 O  O   . HOH P 7 .   ? -40.494 23.369 18.925  1.00 58.82  ? 308 HOH B O   1 
HETATM 2536 O  O   . HOH P 7 .   ? -28.279 5.570  17.336  1.00 46.03  ? 309 HOH B O   1 
HETATM 2537 O  O   . HOH P 7 .   ? -11.058 32.984 29.276  1.00 54.64  ? 310 HOH B O   1 
HETATM 2538 O  O   . HOH P 7 .   ? -22.086 2.594  28.477  1.00 69.40  ? 311 HOH B O   1 
HETATM 2539 O  O   . HOH P 7 .   ? -18.394 30.110 13.035  1.00 64.57  ? 312 HOH B O   1 
HETATM 2540 O  O   . HOH P 7 .   ? -39.806 16.416 29.304  1.00 46.30  ? 313 HOH B O   1 
HETATM 2541 O  O   . HOH P 7 .   ? -34.397 22.893 18.690  1.00 44.26  ? 314 HOH B O   1 
HETATM 2542 O  O   . HOH P 7 .   ? -6.750  35.945 26.223  1.00 50.27  ? 315 HOH B O   1 
HETATM 2543 O  O   . HOH P 7 .   ? -12.026 14.045 23.463  1.00 61.64  ? 316 HOH B O   1 
HETATM 2544 O  O   . HOH P 7 .   ? -20.414 8.779  19.118  1.00 55.05  ? 317 HOH B O   1 
HETATM 2545 O  O   . HOH P 7 .   ? -12.588 9.683  28.887  1.00 73.73  ? 318 HOH B O   1 
HETATM 2546 O  O   . HOH P 7 .   ? -33.393 25.246 18.495  1.00 46.39  ? 319 HOH B O   1 
HETATM 2547 O  O   . HOH P 7 .   ? -41.551 26.239 23.695  1.00 62.70  ? 320 HOH B O   1 
HETATM 2548 O  O   . HOH P 7 .   ? -40.715 4.212  31.733  1.00 51.93  ? 321 HOH B O   1 
HETATM 2549 O  O   . HOH P 7 .   ? -2.528  30.678 27.944  1.00 50.98  ? 322 HOH B O   1 
HETATM 2550 O  O   . HOH P 7 .   ? -37.361 8.473  37.144  1.00 65.82  ? 323 HOH B O   1 
HETATM 2551 O  O   . HOH P 7 .   ? -29.900 25.726 30.112  1.00 55.45  ? 324 HOH B O   1 
HETATM 2552 O  O   . HOH P 7 .   ? -8.070  22.515 32.336  1.00 37.78  ? 325 HOH B O   1 
HETATM 2553 O  O   . HOH P 7 .   ? -19.400 5.434  24.671  1.00 50.37  ? 326 HOH B O   1 
HETATM 2554 O  O   . HOH P 7 .   ? -3.134  37.857 17.256  1.00 65.45  ? 327 HOH B O   1 
HETATM 2555 O  O   . HOH P 7 .   ? -23.394 11.312 18.410  1.00 34.24  ? 328 HOH B O   1 
HETATM 2556 O  O   . HOH P 7 .   ? -1.608  31.521 16.975  1.00 51.02  ? 329 HOH B O   1 
HETATM 2557 O  O   . HOH P 7 .   ? -28.017 30.964 20.798  1.00 56.43  ? 330 HOH B O   1 
HETATM 2558 O  O   . HOH P 7 .   ? -15.206 8.748  21.455  1.00 61.18  ? 331 HOH B O   1 
HETATM 2559 O  O   . HOH P 7 .   ? -22.559 3.687  23.914  1.00 59.62  ? 332 HOH B O   1 
HETATM 2560 O  O   . HOH P 7 .   ? -26.585 25.361 13.349  1.00 49.59  ? 333 HOH B O   1 
HETATM 2561 O  O   . HOH P 7 .   ? -17.125 36.140 21.692  1.00 77.37  ? 334 HOH B O   1 
HETATM 2562 O  O   . HOH P 7 .   ? -26.726 29.456 31.216  1.00 51.70  ? 335 HOH B O   1 
HETATM 2563 O  O   . HOH P 7 .   ? -12.320 14.736 16.264  1.00 55.28  ? 336 HOH B O   1 
HETATM 2564 O  O   . HOH P 7 .   ? -21.442 15.938 14.162  1.00 38.78  ? 337 HOH B O   1 
HETATM 2565 O  O   . HOH P 7 .   ? -34.083 15.826 15.568  1.00 44.94  ? 338 HOH B O   1 
HETATM 2566 O  O   . HOH P 7 .   ? -19.343 23.410 12.780  1.00 50.97  ? 339 HOH B O   1 
HETATM 2567 O  O   . HOH P 7 .   ? -24.024 3.339  26.173  1.00 66.23  ? 340 HOH B O   1 
HETATM 2568 O  O   . HOH P 7 .   ? -24.209 9.357  20.397  1.00 36.78  ? 341 HOH B O   1 
HETATM 2569 O  O   . HOH P 7 .   ? -31.391 20.661 32.235  1.00 50.69  ? 342 HOH B O   1 
HETATM 2570 O  O   . HOH P 7 .   ? -33.037 13.332 33.291  1.00 44.49  ? 343 HOH B O   1 
HETATM 2571 O  O   . HOH P 7 .   ? -33.284 18.435 17.608  1.00 43.28  ? 344 HOH B O   1 
HETATM 2572 O  O   . HOH P 7 .   ? -17.590 35.458 24.337  1.00 70.24  ? 345 HOH B O   1 
HETATM 2573 O  O   . HOH P 7 .   ? -36.188 27.500 23.035  1.00 61.54  ? 346 HOH B O   1 
HETATM 2574 O  O   . HOH P 7 .   ? -24.575 7.592  16.128  1.00 48.47  ? 347 HOH B O   1 
HETATM 2575 O  O   . HOH P 7 .   ? -13.166 34.520 29.753  1.00 58.99  ? 348 HOH B O   1 
HETATM 2576 O  O   . HOH P 7 .   ? -32.198 3.749  27.895  1.00 48.82  ? 349 HOH B O   1 
HETATM 2577 O  O   . HOH P 7 .   ? -10.852 39.046 25.327  1.00 66.87  ? 350 HOH B O   1 
HETATM 2578 O  O   . HOH P 7 .   ? -32.301 22.416 30.274  1.00 45.86  ? 351 HOH B O   1 
HETATM 2579 O  O   . HOH P 7 .   ? -8.858  27.423 12.441  1.00 59.41  ? 352 HOH B O   1 
HETATM 2580 O  O   . HOH P 7 .   ? -37.731 17.894 32.634  1.00 58.48  ? 353 HOH B O   1 
HETATM 2581 O  O   . HOH P 7 .   ? -8.197  29.172 14.342  1.00 55.56  ? 354 HOH B O   1 
HETATM 2582 O  O   . HOH P 7 .   ? -1.770  28.626 29.684  1.00 58.63  ? 355 HOH B O   1 
HETATM 2583 O  O   . HOH P 7 .   ? -31.474 27.847 29.116  1.00 56.04  ? 356 HOH B O   1 
HETATM 2584 O  O   . HOH P 7 .   ? -29.966 17.909 38.905  1.00 57.83  ? 357 HOH B O   1 
HETATM 2585 O  O   . HOH P 7 .   ? -14.392 36.852 23.678  1.00 69.95  ? 358 HOH B O   1 
HETATM 2586 O  O   . HOH P 7 .   ? -8.373  12.567 26.832  1.00 62.04  ? 359 HOH B O   1 
HETATM 2587 O  O   . HOH P 7 .   ? -23.772 7.165  18.571  1.00 52.65  ? 360 HOH B O   1 
HETATM 2588 O  O   . HOH P 7 .   ? -17.999 5.504  27.612  1.00 75.01  ? 361 HOH B O   1 
HETATM 2589 O  O   . HOH Q 7 .   ? 38.136  30.452 20.538  1.00 41.44  ? 101 HOH C O   1 
HETATM 2590 O  O   . HOH Q 7 .   ? 36.591  46.167 4.412   1.00 32.63  ? 102 HOH C O   1 
HETATM 2591 O  O   . HOH Q 7 .   ? 30.722  42.238 4.795   1.00 46.88  ? 103 HOH C O   1 
HETATM 2592 O  O   . HOH Q 7 .   ? 35.484  50.827 -1.057  1.00 31.32  ? 104 HOH C O   1 
HETATM 2593 O  O   . HOH Q 7 .   ? 39.170  31.425 18.354  1.00 42.81  ? 105 HOH C O   1 
HETATM 2594 O  O   . HOH Q 7 .   ? 35.498  42.934 -0.628  1.00 43.76  ? 106 HOH C O   1 
HETATM 2595 O  O   . HOH Q 7 .   ? 35.073  37.086 24.562  1.00 32.67  ? 107 HOH C O   1 
HETATM 2596 O  O   . HOH Q 7 .   ? 37.515  37.518 15.110  1.00 41.88  ? 108 HOH C O   1 
HETATM 2597 O  O   . HOH Q 7 .   ? 35.518  47.064 6.756   1.00 44.15  ? 109 HOH C O   1 
HETATM 2598 O  O   . HOH Q 7 .   ? 27.038  40.485 -6.390  1.00 62.85  ? 110 HOH C O   1 
# 
