data_7HCR
# 
_entry.id   7HCR 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.404 
_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   7HCR         pdb_00007hcr 10.2210/pdb7hcr/pdb 
WWPDB D_1001407309 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-06-11 
_pdbx_audit_revision_history.part_number         ? 
# 
_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             ? 
# 
_pdbx_database_status.entry_id                        7HCR 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-15 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.SG_entry                        ? 
_pdbx_database_status.pdb_format_compatible           N 
_pdbx_database_status.methods_development_category    ? 
# 
_pdbx_contact_author.id                 1 
_pdbx_contact_author.name_last          Fraser 
_pdbx_contact_author.name_first         James 
_pdbx_contact_author.name_mi            S. 
_pdbx_contact_author.email              jaimefraser@gmail.com 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-5080-2859 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Correy, G.J.' 1 ? 
'Fraser, J.S.' 2 ? 
# 
_citation.id                        primary 
_citation.title                     
;Exploration of structure-activity relationships for the SARS-CoV-2 macrodomain from shape-based fragment linking and active learning.
;
_citation.journal_abbrev            'Sci Adv' 
_citation.journal_volume            11 
_citation.page_first                eads7187 
_citation.page_last                 eads7187 
_citation.year                      2025 
_citation.pdbx_database_id_PubMed   40435250 
_citation.pdbx_database_id_DOI      10.1126/sciadv.ads7187 
_citation.journal_id_ASTM           ? 
_citation.country                   US 
_citation.journal_id_ISSN           2375-2548 
_citation.journal_id_CSD            ? 
_citation.book_publisher            ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.identifier_ORCID 
_citation_author.ordinal 
primary 'Correy, G.J.'    0000-0001-5155-7325 1  
primary 'Rachman, M.M.'   0000-0003-3671-8885 2  
primary 'Togo, T.'        0000-0003-0243-0760 3  
primary 'Gahbauer, S.'    0000-0002-3115-9757 4  
primary 'Doruk, Y.U.'     0000-0002-3388-7803 5  
primary 'Stevens, M.G.V.' 0009-0004-9732-0349 6  
primary 'Jaishankar, P.'  0009-0005-2013-8941 7  
primary 'Kelley, B.'      ?                   8  
primary 'Goldman, B.'     0009-0006-6465-6959 9  
primary 'Schmidt, M.'     ?                   10 
primary 'Kramer, T.'      0009-0002-5932-7406 11 
primary 'Radchenko, D.S.' 0000-0001-5444-7754 12 
primary 'Moroz, Y.S.'     0000-0001-6073-002X 13 
primary 'Ashworth, A.'    0000-0003-1446-7878 14 
primary 'Riley, P.'       0000-0003-0797-0272 15 
primary 'Shoichet, B.K.'  0000-0002-6098-7367 16 
primary 'Renslo, A.R.'    0000-0002-1240-2846 17 
primary 'Walters, W.P.'   0000-0003-2860-7958 18 
primary 'Fraser, J.S.'    0000-0002-5080-2859 19 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Non-structural protein 3'                                                    18178.766 2   
'3.4.19.121, 3.4.22.-' ? ? 'HIS6 purification tag and linker (MHHHHHHSSGVDLGTENLYFQ) cleaved with TEV protease' 
2 non-polymer syn 'DIMETHYL SULFOXIDE'                                                          78.133    1   ? ? ? ? 
3 non-polymer syn '(3S)-3-hydroxy-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidine-3-carboxamide' 247.253   1   ? ? ? ? 
4 non-polymer syn '(3R)-3-hydroxy-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidine-3-carboxamide' 247.253   1   ? ? ? ? 
5 non-polymer syn 'CHLORIDE ION'                                                                35.453    1   ? ? ? ? 
6 water       nat water                                                                         18.015    426 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'nsp3, PL2-PRO, Papain-like protease, Papain-like proteinase, PL-PRO' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_seq_one_letter_code_can   
;SMVNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGS
CVLSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNL
YDKLVSSFL
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 'DIMETHYL SULFOXIDE'                                                          DMS   
3 '(3S)-3-hydroxy-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidine-3-carboxamide' A1A56 
4 '(3R)-3-hydroxy-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidine-3-carboxamide' A1A57 
5 'CHLORIDE ION'                                                                CL    
6 water                                                                         HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   SER n 
1 2   MET n 
1 3   VAL n 
1 4   ASN n 
1 5   SER n 
1 6   PHE n 
1 7   SER n 
1 8   GLY n 
1 9   TYR n 
1 10  LEU n 
1 11  LYS n 
1 12  LEU n 
1 13  THR n 
1 14  ASP n 
1 15  ASN n 
1 16  VAL n 
1 17  TYR n 
1 18  ILE n 
1 19  LYS n 
1 20  ASN n 
1 21  ALA n 
1 22  ASP n 
1 23  ILE n 
1 24  VAL n 
1 25  GLU n 
1 26  GLU n 
1 27  ALA n 
1 28  LYS n 
1 29  LYS n 
1 30  VAL n 
1 31  LYS n 
1 32  PRO n 
1 33  THR n 
1 34  VAL n 
1 35  VAL n 
1 36  VAL n 
1 37  ASN n 
1 38  ALA n 
1 39  ALA n 
1 40  ASN n 
1 41  VAL n 
1 42  TYR n 
1 43  LEU n 
1 44  LYS n 
1 45  HIS n 
1 46  GLY n 
1 47  GLY n 
1 48  GLY n 
1 49  VAL n 
1 50  ALA n 
1 51  GLY n 
1 52  ALA n 
1 53  LEU n 
1 54  ASN n 
1 55  LYS n 
1 56  ALA n 
1 57  THR n 
1 58  ASN n 
1 59  ASN n 
1 60  ALA n 
1 61  MET n 
1 62  GLN n 
1 63  VAL n 
1 64  GLU n 
1 65  SER n 
1 66  ASP n 
1 67  ASP n 
1 68  TYR n 
1 69  ILE n 
1 70  ALA n 
1 71  THR n 
1 72  ASN n 
1 73  GLY n 
1 74  PRO n 
1 75  LEU n 
1 76  LYS n 
1 77  VAL n 
1 78  GLY n 
1 79  GLY n 
1 80  SER n 
1 81  CYS n 
1 82  VAL n 
1 83  LEU n 
1 84  SER n 
1 85  GLY n 
1 86  HIS n 
1 87  ASN n 
1 88  LEU n 
1 89  ALA n 
1 90  LYS n 
1 91  HIS n 
1 92  CYS n 
1 93  LEU n 
1 94  HIS n 
1 95  VAL n 
1 96  VAL n 
1 97  GLY n 
1 98  PRO n 
1 99  ASN n 
1 100 VAL n 
1 101 ASN n 
1 102 LYS n 
1 103 GLY n 
1 104 GLU n 
1 105 ASP n 
1 106 ILE n 
1 107 GLN n 
1 108 LEU n 
1 109 LEU n 
1 110 LYS n 
1 111 SER n 
1 112 ALA n 
1 113 TYR n 
1 114 GLU n 
1 115 ASN n 
1 116 PHE n 
1 117 ASN n 
1 118 GLN n 
1 119 HIS n 
1 120 GLU n 
1 121 VAL n 
1 122 LEU n 
1 123 LEU n 
1 124 ALA n 
1 125 PRO n 
1 126 LEU n 
1 127 LEU n 
1 128 SER n 
1 129 ALA n 
1 130 GLY n 
1 131 ILE n 
1 132 PHE n 
1 133 GLY n 
1 134 ALA n 
1 135 ASP n 
1 136 PRO n 
1 137 ILE n 
1 138 HIS n 
1 139 SER n 
1 140 LEU n 
1 141 ARG n 
1 142 VAL n 
1 143 CYS n 
1 144 VAL n 
1 145 ASP n 
1 146 THR n 
1 147 VAL n 
1 148 ARG n 
1 149 THR n 
1 150 ASN n 
1 151 VAL n 
1 152 TYR n 
1 153 LEU n 
1 154 ALA n 
1 155 VAL n 
1 156 PHE n 
1 157 ASP n 
1 158 LYS n 
1 159 ASN n 
1 160 LEU n 
1 161 TYR n 
1 162 ASP n 
1 163 LYS n 
1 164 LEU n 
1 165 VAL n 
1 166 SER n 
1 167 SER n 
1 168 PHE n 
1 169 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                   169 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'rep, 1a-1b' 
_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      'Severe acute respiratory syndrome coronavirus 2' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     2697049 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          plasmid 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       'pET22b(+)' 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
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 
A1A56 non-polymer         . '(3S)-3-hydroxy-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidine-3-carboxamide' ? 'C11 H13 N5 O2'  
247.253 
A1A57 non-polymer         . '(3R)-3-hydroxy-1-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)pyrrolidine-3-carboxamide' ? 'C11 H13 N5 O2'  
247.253 
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 
CL    non-polymer         . 'CHLORIDE ION'                                                                ? 'Cl -1'          
35.453  
CYS   'L-peptide linking' y CYSTEINE                                                                      ? 'C3 H7 N O2 S'   
121.158 
DMS   non-polymer         . 'DIMETHYL SULFOXIDE'                                                          ? 'C2 H6 O S'      
78.133  
GLN   'L-peptide linking' y GLUTAMINE                                                                     ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                               ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                       ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                     ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                         ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                    ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                       ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                        ? 'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                                                                    ? 'C5 H11 N O2 S'  
149.211 
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 
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   SER 1   1   ?   ?   ?   A . n 
A 1 2   MET 2   2   ?   ?   ?   A . n 
A 1 3   VAL 3   3   3   VAL VAL A . n 
A 1 4   ASN 4   4   4   ASN ASN A . n 
A 1 5   SER 5   5   5   SER SER A . n 
A 1 6   PHE 6   6   6   PHE PHE A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   GLY 8   8   8   GLY GLY A . n 
A 1 9   TYR 9   9   9   TYR TYR A . n 
A 1 10  LEU 10  10  10  LEU LEU A . n 
A 1 11  LYS 11  11  11  LYS LYS A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  THR 13  13  13  THR THR A . n 
A 1 14  ASP 14  14  14  ASP ASP A . n 
A 1 15  ASN 15  15  15  ASN ASN A . n 
A 1 16  VAL 16  16  16  VAL VAL A . n 
A 1 17  TYR 17  17  17  TYR TYR A . n 
A 1 18  ILE 18  18  18  ILE ILE A . n 
A 1 19  LYS 19  19  19  LYS LYS A . n 
A 1 20  ASN 20  20  20  ASN ASN A . n 
A 1 21  ALA 21  21  21  ALA ALA A . n 
A 1 22  ASP 22  22  22  ASP ASP A . n 
A 1 23  ILE 23  23  23  ILE ILE A . n 
A 1 24  VAL 24  24  24  VAL VAL A . n 
A 1 25  GLU 25  25  25  GLU GLU A . n 
A 1 26  GLU 26  26  26  GLU GLU A . n 
A 1 27  ALA 27  27  27  ALA ALA A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  LYS 29  29  29  LYS LYS A . n 
A 1 30  VAL 30  30  30  VAL VAL A . n 
A 1 31  LYS 31  31  31  LYS LYS A . n 
A 1 32  PRO 32  32  32  PRO PRO A . n 
A 1 33  THR 33  33  33  THR THR A . n 
A 1 34  VAL 34  34  34  VAL VAL A . n 
A 1 35  VAL 35  35  35  VAL VAL A . n 
A 1 36  VAL 36  36  36  VAL VAL A . n 
A 1 37  ASN 37  37  37  ASN ASN A . n 
A 1 38  ALA 38  38  38  ALA ALA A . n 
A 1 39  ALA 39  39  39  ALA ALA A . n 
A 1 40  ASN 40  40  40  ASN ASN A . n 
A 1 41  VAL 41  41  41  VAL VAL A . n 
A 1 42  TYR 42  42  42  TYR TYR A . n 
A 1 43  LEU 43  43  43  LEU LEU A . n 
A 1 44  LYS 44  44  44  LYS LYS A . n 
A 1 45  HIS 45  45  45  HIS HIS A . n 
A 1 46  GLY 46  46  46  GLY GLY A . n 
A 1 47  GLY 47  47  47  GLY GLY A . n 
A 1 48  GLY 48  48  48  GLY GLY A . n 
A 1 49  VAL 49  49  49  VAL VAL A . n 
A 1 50  ALA 50  50  50  ALA ALA A . n 
A 1 51  GLY 51  51  51  GLY GLY A . n 
A 1 52  ALA 52  52  52  ALA ALA A . n 
A 1 53  LEU 53  53  53  LEU LEU A . n 
A 1 54  ASN 54  54  54  ASN ASN A . n 
A 1 55  LYS 55  55  55  LYS LYS A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  THR 57  57  57  THR THR A . n 
A 1 58  ASN 58  58  58  ASN ASN A . n 
A 1 59  ASN 59  59  59  ASN ASN A . n 
A 1 60  ALA 60  60  60  ALA ALA A . n 
A 1 61  MET 61  61  61  MET MET A . n 
A 1 62  GLN 62  62  62  GLN GLN A . n 
A 1 63  VAL 63  63  63  VAL VAL A . n 
A 1 64  GLU 64  64  64  GLU GLU A . n 
A 1 65  SER 65  65  65  SER SER A . n 
A 1 66  ASP 66  66  66  ASP ASP A . n 
A 1 67  ASP 67  67  67  ASP ASP A . n 
A 1 68  TYR 68  68  68  TYR TYR A . n 
A 1 69  ILE 69  69  69  ILE ILE A . n 
A 1 70  ALA 70  70  70  ALA ALA A . n 
A 1 71  THR 71  71  71  THR THR A . n 
A 1 72  ASN 72  72  72  ASN ASN A . n 
A 1 73  GLY 73  73  73  GLY GLY A . n 
A 1 74  PRO 74  74  74  PRO PRO A . n 
A 1 75  LEU 75  75  75  LEU LEU A . n 
A 1 76  LYS 76  76  76  LYS LYS A . n 
A 1 77  VAL 77  77  77  VAL VAL A . n 
A 1 78  GLY 78  78  78  GLY GLY A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  SER 80  80  80  SER SER A . n 
A 1 81  CYS 81  81  81  CYS CYS A . n 
A 1 82  VAL 82  82  82  VAL VAL A . n 
A 1 83  LEU 83  83  83  LEU LEU A . n 
A 1 84  SER 84  84  84  SER SER A . n 
A 1 85  GLY 85  85  85  GLY GLY A . n 
A 1 86  HIS 86  86  86  HIS HIS A . n 
A 1 87  ASN 87  87  87  ASN ASN A . n 
A 1 88  LEU 88  88  88  LEU LEU A . n 
A 1 89  ALA 89  89  89  ALA ALA A . n 
A 1 90  LYS 90  90  90  LYS LYS A . n 
A 1 91  HIS 91  91  91  HIS HIS A . n 
A 1 92  CYS 92  92  92  CYS CYS A . n 
A 1 93  LEU 93  93  93  LEU LEU A . n 
A 1 94  HIS 94  94  94  HIS HIS A . n 
A 1 95  VAL 95  95  95  VAL VAL A . n 
A 1 96  VAL 96  96  96  VAL VAL A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  PRO 98  98  98  PRO PRO A . n 
A 1 99  ASN 99  99  99  ASN ASN A . n 
A 1 100 VAL 100 100 100 VAL VAL A . n 
A 1 101 ASN 101 101 101 ASN ASN A . n 
A 1 102 LYS 102 102 102 LYS LYS A . n 
A 1 103 GLY 103 103 103 GLY GLY A . n 
A 1 104 GLU 104 104 104 GLU GLU A . n 
A 1 105 ASP 105 105 105 ASP ASP A . n 
A 1 106 ILE 106 106 106 ILE ILE A . n 
A 1 107 GLN 107 107 107 GLN GLN A . n 
A 1 108 LEU 108 108 108 LEU LEU A . n 
A 1 109 LEU 109 109 109 LEU LEU A . n 
A 1 110 LYS 110 110 110 LYS LYS A . n 
A 1 111 SER 111 111 111 SER SER A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 TYR 113 113 113 TYR TYR A . n 
A 1 114 GLU 114 114 114 GLU GLU A . n 
A 1 115 ASN 115 115 115 ASN ASN A . n 
A 1 116 PHE 116 116 116 PHE PHE A . n 
A 1 117 ASN 117 117 117 ASN ASN A . n 
A 1 118 GLN 118 118 118 GLN GLN A . n 
A 1 119 HIS 119 119 119 HIS HIS A . n 
A 1 120 GLU 120 120 120 GLU GLU A . n 
A 1 121 VAL 121 121 121 VAL VAL A . n 
A 1 122 LEU 122 122 122 LEU LEU A . n 
A 1 123 LEU 123 123 123 LEU LEU A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 PRO 125 125 125 PRO PRO A . n 
A 1 126 LEU 126 126 126 LEU LEU A . n 
A 1 127 LEU 127 127 127 LEU LEU A . n 
A 1 128 SER 128 128 128 SER SER A . n 
A 1 129 ALA 129 129 129 ALA ALA A . n 
A 1 130 GLY 130 130 130 GLY GLY A . n 
A 1 131 ILE 131 131 131 ILE ILE A . n 
A 1 132 PHE 132 132 132 PHE PHE A . n 
A 1 133 GLY 133 133 133 GLY GLY A . n 
A 1 134 ALA 134 134 134 ALA ALA A . n 
A 1 135 ASP 135 135 135 ASP ASP A . n 
A 1 136 PRO 136 136 136 PRO PRO A . n 
A 1 137 ILE 137 137 137 ILE ILE A . n 
A 1 138 HIS 138 138 138 HIS HIS A . n 
A 1 139 SER 139 139 139 SER SER A . n 
A 1 140 LEU 140 140 140 LEU LEU A . n 
A 1 141 ARG 141 141 141 ARG ARG A . n 
A 1 142 VAL 142 142 142 VAL VAL A . n 
A 1 143 CYS 143 143 143 CYS CYS A . n 
A 1 144 VAL 144 144 144 VAL VAL A . n 
A 1 145 ASP 145 145 145 ASP ASP A . n 
A 1 146 THR 146 146 146 THR THR A . n 
A 1 147 VAL 147 147 147 VAL VAL A . n 
A 1 148 ARG 148 148 148 ARG ARG A . n 
A 1 149 THR 149 149 149 THR THR A . n 
A 1 150 ASN 150 150 150 ASN ASN A . n 
A 1 151 VAL 151 151 151 VAL VAL A . n 
A 1 152 TYR 152 152 152 TYR TYR A . n 
A 1 153 LEU 153 153 153 LEU LEU A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 VAL 155 155 155 VAL VAL A . n 
A 1 156 PHE 156 156 156 PHE PHE A . n 
A 1 157 ASP 157 157 157 ASP ASP A . n 
A 1 158 LYS 158 158 158 LYS LYS A . n 
A 1 159 ASN 159 159 159 ASN ASN A . n 
A 1 160 LEU 160 160 160 LEU LEU A . n 
A 1 161 TYR 161 161 161 TYR TYR A . n 
A 1 162 ASP 162 162 162 ASP ASP A . n 
A 1 163 LYS 163 163 163 LYS LYS A . n 
A 1 164 LEU 164 164 164 LEU LEU A . n 
A 1 165 VAL 165 165 165 VAL VAL A . n 
A 1 166 SER 166 166 166 SER SER A . n 
A 1 167 SER 167 167 167 SER SER A . n 
A 1 168 PHE 168 168 168 PHE PHE A . n 
A 1 169 LEU 169 169 169 LEU LEU A . n 
B 1 1   SER 1   1   1   SER SER B . n 
B 1 2   MET 2   2   2   MET MET B . n 
B 1 3   VAL 3   3   3   VAL VAL B . n 
B 1 4   ASN 4   4   4   ASN ASN B . n 
B 1 5   SER 5   5   5   SER SER B . n 
B 1 6   PHE 6   6   6   PHE PHE B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   GLY 8   8   8   GLY GLY B . n 
B 1 9   TYR 9   9   9   TYR TYR B . n 
B 1 10  LEU 10  10  10  LEU LEU B . n 
B 1 11  LYS 11  11  11  LYS LYS B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  THR 13  13  13  THR THR B . n 
B 1 14  ASP 14  14  14  ASP ASP B . n 
B 1 15  ASN 15  15  15  ASN ASN B . n 
B 1 16  VAL 16  16  16  VAL VAL B . n 
B 1 17  TYR 17  17  17  TYR TYR B . n 
B 1 18  ILE 18  18  18  ILE ILE B . n 
B 1 19  LYS 19  19  19  LYS LYS B . n 
B 1 20  ASN 20  20  20  ASN ASN B . n 
B 1 21  ALA 21  21  21  ALA ALA B . n 
B 1 22  ASP 22  22  22  ASP ASP B . n 
B 1 23  ILE 23  23  23  ILE ILE B . n 
B 1 24  VAL 24  24  24  VAL VAL B . n 
B 1 25  GLU 25  25  25  GLU GLU B . n 
B 1 26  GLU 26  26  26  GLU GLU B . n 
B 1 27  ALA 27  27  27  ALA ALA B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  LYS 29  29  29  LYS LYS B . n 
B 1 30  VAL 30  30  30  VAL VAL B . n 
B 1 31  LYS 31  31  31  LYS LYS B . n 
B 1 32  PRO 32  32  32  PRO PRO B . n 
B 1 33  THR 33  33  33  THR THR B . n 
B 1 34  VAL 34  34  34  VAL VAL B . n 
B 1 35  VAL 35  35  35  VAL VAL B . n 
B 1 36  VAL 36  36  36  VAL VAL B . n 
B 1 37  ASN 37  37  37  ASN ASN B . n 
B 1 38  ALA 38  38  38  ALA ALA B . n 
B 1 39  ALA 39  39  39  ALA ALA B . n 
B 1 40  ASN 40  40  40  ASN ASN B . n 
B 1 41  VAL 41  41  41  VAL VAL B . n 
B 1 42  TYR 42  42  42  TYR TYR B . n 
B 1 43  LEU 43  43  43  LEU LEU B . n 
B 1 44  LYS 44  44  44  LYS LYS B . n 
B 1 45  HIS 45  45  45  HIS HIS B . n 
B 1 46  GLY 46  46  46  GLY GLY B . n 
B 1 47  GLY 47  47  47  GLY GLY B . n 
B 1 48  GLY 48  48  48  GLY GLY B . n 
B 1 49  VAL 49  49  49  VAL VAL B . n 
B 1 50  ALA 50  50  50  ALA ALA B . n 
B 1 51  GLY 51  51  51  GLY GLY B . n 
B 1 52  ALA 52  52  52  ALA ALA B . n 
B 1 53  LEU 53  53  53  LEU LEU B . n 
B 1 54  ASN 54  54  54  ASN ASN B . n 
B 1 55  LYS 55  55  55  LYS LYS B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  THR 57  57  57  THR THR B . n 
B 1 58  ASN 58  58  58  ASN ASN B . n 
B 1 59  ASN 59  59  59  ASN ASN B . n 
B 1 60  ALA 60  60  60  ALA ALA B . n 
B 1 61  MET 61  61  61  MET MET B . n 
B 1 62  GLN 62  62  62  GLN GLN B . n 
B 1 63  VAL 63  63  63  VAL VAL B . n 
B 1 64  GLU 64  64  64  GLU GLU B . n 
B 1 65  SER 65  65  65  SER SER B . n 
B 1 66  ASP 66  66  66  ASP ASP B . n 
B 1 67  ASP 67  67  67  ASP ASP B . n 
B 1 68  TYR 68  68  68  TYR TYR B . n 
B 1 69  ILE 69  69  69  ILE ILE B . n 
B 1 70  ALA 70  70  70  ALA ALA B . n 
B 1 71  THR 71  71  71  THR THR B . n 
B 1 72  ASN 72  72  72  ASN ASN B . n 
B 1 73  GLY 73  73  73  GLY GLY B . n 
B 1 74  PRO 74  74  74  PRO PRO B . n 
B 1 75  LEU 75  75  75  LEU LEU B . n 
B 1 76  LYS 76  76  76  LYS LYS B . n 
B 1 77  VAL 77  77  77  VAL VAL B . n 
B 1 78  GLY 78  78  78  GLY GLY B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  SER 80  80  80  SER SER B . n 
B 1 81  CYS 81  81  81  CYS CYS B . n 
B 1 82  VAL 82  82  82  VAL VAL B . n 
B 1 83  LEU 83  83  83  LEU LEU B . n 
B 1 84  SER 84  84  84  SER SER B . n 
B 1 85  GLY 85  85  85  GLY GLY B . n 
B 1 86  HIS 86  86  86  HIS HIS B . n 
B 1 87  ASN 87  87  87  ASN ASN B . n 
B 1 88  LEU 88  88  88  LEU LEU B . n 
B 1 89  ALA 89  89  89  ALA ALA B . n 
B 1 90  LYS 90  90  90  LYS LYS B . n 
B 1 91  HIS 91  91  91  HIS HIS B . n 
B 1 92  CYS 92  92  92  CYS CYS B . n 
B 1 93  LEU 93  93  93  LEU LEU B . n 
B 1 94  HIS 94  94  94  HIS HIS B . n 
B 1 95  VAL 95  95  95  VAL VAL B . n 
B 1 96  VAL 96  96  96  VAL VAL B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  PRO 98  98  98  PRO PRO B . n 
B 1 99  ASN 99  99  99  ASN ASN B . n 
B 1 100 VAL 100 100 100 VAL VAL B . n 
B 1 101 ASN 101 101 101 ASN ASN B . n 
B 1 102 LYS 102 102 102 LYS LYS B . n 
B 1 103 GLY 103 103 103 GLY GLY B . n 
B 1 104 GLU 104 104 104 GLU GLU B . n 
B 1 105 ASP 105 105 105 ASP ASP B . n 
B 1 106 ILE 106 106 106 ILE ILE B . n 
B 1 107 GLN 107 107 107 GLN GLN B . n 
B 1 108 LEU 108 108 108 LEU LEU B . n 
B 1 109 LEU 109 109 109 LEU LEU B . n 
B 1 110 LYS 110 110 110 LYS LYS B . n 
B 1 111 SER 111 111 111 SER SER B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 TYR 113 113 113 TYR TYR B . n 
B 1 114 GLU 114 114 114 GLU GLU B . n 
B 1 115 ASN 115 115 115 ASN ASN B . n 
B 1 116 PHE 116 116 116 PHE PHE B . n 
B 1 117 ASN 117 117 117 ASN ASN B . n 
B 1 118 GLN 118 118 118 GLN GLN B . n 
B 1 119 HIS 119 119 119 HIS HIS B . n 
B 1 120 GLU 120 120 120 GLU GLU B . n 
B 1 121 VAL 121 121 121 VAL VAL B . n 
B 1 122 LEU 122 122 122 LEU LEU B . n 
B 1 123 LEU 123 123 123 LEU LEU B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 PRO 125 125 125 PRO PRO B . n 
B 1 126 LEU 126 126 126 LEU LEU B . n 
B 1 127 LEU 127 127 127 LEU LEU B . n 
B 1 128 SER 128 128 128 SER SER B . n 
B 1 129 ALA 129 129 129 ALA ALA B . n 
B 1 130 GLY 130 130 130 GLY GLY B . n 
B 1 131 ILE 131 131 131 ILE ILE B . n 
B 1 132 PHE 132 132 132 PHE PHE B . n 
B 1 133 GLY 133 133 133 GLY GLY B . n 
B 1 134 ALA 134 134 134 ALA ALA B . n 
B 1 135 ASP 135 135 135 ASP ASP B . n 
B 1 136 PRO 136 136 136 PRO PRO B . n 
B 1 137 ILE 137 137 137 ILE ILE B . n 
B 1 138 HIS 138 138 138 HIS HIS B . n 
B 1 139 SER 139 139 139 SER SER B . n 
B 1 140 LEU 140 140 140 LEU LEU B . n 
B 1 141 ARG 141 141 141 ARG ARG B . n 
B 1 142 VAL 142 142 142 VAL VAL B . n 
B 1 143 CYS 143 143 143 CYS CYS B . n 
B 1 144 VAL 144 144 144 VAL VAL B . n 
B 1 145 ASP 145 145 145 ASP ASP B . n 
B 1 146 THR 146 146 146 THR THR B . n 
B 1 147 VAL 147 147 147 VAL VAL B . n 
B 1 148 ARG 148 148 148 ARG ARG B . n 
B 1 149 THR 149 149 149 THR THR B . n 
B 1 150 ASN 150 150 150 ASN ASN B . n 
B 1 151 VAL 151 151 151 VAL VAL B . n 
B 1 152 TYR 152 152 152 TYR TYR B . n 
B 1 153 LEU 153 153 153 LEU LEU B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 VAL 155 155 155 VAL VAL B . n 
B 1 156 PHE 156 156 156 PHE PHE B . n 
B 1 157 ASP 157 157 157 ASP ASP B . n 
B 1 158 LYS 158 158 158 LYS LYS B . n 
B 1 159 ASN 159 159 159 ASN ASN B . n 
B 1 160 LEU 160 160 160 LEU LEU B . n 
B 1 161 TYR 161 161 161 TYR TYR B . n 
B 1 162 ASP 162 162 162 ASP ASP B . n 
B 1 163 LYS 163 163 163 LYS LYS B . n 
B 1 164 LEU 164 164 164 LEU LEU B . n 
B 1 165 VAL 165 165 165 VAL VAL B . n 
B 1 166 SER 166 166 166 SER SER B . n 
B 1 167 SER 167 167 167 SER SER B . n 
B 1 168 PHE 168 168 168 PHE PHE B . n 
B 1 169 LEU 169 169 169 LEU LEU B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 DMS   1   401 401  DMS   DMS A . 
D 3 A1A56 1   402 201  A1A56 LA1 A . 
E 4 A1A57 1   403 301  A1A57 LA2 A . 
F 5 CL    1   404 1    CL    CL  A . 
G 6 HOH   1   501 36   HOH   HOH A . 
G 6 HOH   2   502 19   HOH   HOH A . 
G 6 HOH   3   503 229  HOH   HOH A . 
G 6 HOH   4   504 292  HOH   HOH A . 
G 6 HOH   5   505 493  HOH   HOH A . 
G 6 HOH   6   506 1313 HOH   HOH A . 
G 6 HOH   7   507 209  HOH   HOH A . 
G 6 HOH   8   508 1290 HOH   HOH A . 
G 6 HOH   9   509 109  HOH   HOH A . 
G 6 HOH   10  510 1296 HOH   HOH A . 
G 6 HOH   11  511 625  HOH   HOH A . 
G 6 HOH   12  512 153  HOH   HOH A . 
G 6 HOH   13  513 196  HOH   HOH A . 
G 6 HOH   14  514 247  HOH   HOH A . 
G 6 HOH   15  515 337  HOH   HOH A . 
G 6 HOH   16  516 7    HOH   HOH A . 
G 6 HOH   17  517 151  HOH   HOH A . 
G 6 HOH   18  518 105  HOH   HOH A . 
G 6 HOH   19  519 2    HOH   HOH A . 
G 6 HOH   20  520 124  HOH   HOH A . 
G 6 HOH   21  521 1295 HOH   HOH A . 
G 6 HOH   22  522 192  HOH   HOH A . 
G 6 HOH   23  523 136  HOH   HOH A . 
G 6 HOH   24  524 17   HOH   HOH A . 
G 6 HOH   25  525 49   HOH   HOH A . 
G 6 HOH   26  526 409  HOH   HOH A . 
G 6 HOH   27  527 1300 HOH   HOH A . 
G 6 HOH   28  528 76   HOH   HOH A . 
G 6 HOH   29  529 57   HOH   HOH A . 
G 6 HOH   30  530 35   HOH   HOH A . 
G 6 HOH   31  531 1301 HOH   HOH A . 
G 6 HOH   32  532 1283 HOH   HOH A . 
G 6 HOH   33  533 964  HOH   HOH A . 
G 6 HOH   34  534 661  HOH   HOH A . 
G 6 HOH   35  535 469  HOH   HOH A . 
G 6 HOH   36  536 236  HOH   HOH A . 
G 6 HOH   37  537 195  HOH   HOH A . 
G 6 HOH   38  538 164  HOH   HOH A . 
G 6 HOH   39  539 96   HOH   HOH A . 
G 6 HOH   40  540 86   HOH   HOH A . 
G 6 HOH   41  541 218  HOH   HOH A . 
G 6 HOH   42  542 461  HOH   HOH A . 
G 6 HOH   43  543 34   HOH   HOH A . 
G 6 HOH   44  544 165  HOH   HOH A . 
G 6 HOH   45  545 33   HOH   HOH A . 
G 6 HOH   46  546 10   HOH   HOH A . 
G 6 HOH   47  547 393  HOH   HOH A . 
G 6 HOH   48  548 199  HOH   HOH A . 
G 6 HOH   49  549 155  HOH   HOH A . 
G 6 HOH   50  550 42   HOH   HOH A . 
G 6 HOH   51  551 296  HOH   HOH A . 
G 6 HOH   52  552 241  HOH   HOH A . 
G 6 HOH   53  553 140  HOH   HOH A . 
G 6 HOH   54  554 320  HOH   HOH A . 
G 6 HOH   55  555 630  HOH   HOH A . 
G 6 HOH   56  556 225  HOH   HOH A . 
G 6 HOH   57  557 26   HOH   HOH A . 
G 6 HOH   58  558 21   HOH   HOH A . 
G 6 HOH   59  559 102  HOH   HOH A . 
G 6 HOH   60  560 132  HOH   HOH A . 
G 6 HOH   61  561 351  HOH   HOH A . 
G 6 HOH   62  562 92   HOH   HOH A . 
G 6 HOH   63  563 93   HOH   HOH A . 
G 6 HOH   64  564 354  HOH   HOH A . 
G 6 HOH   65  565 1308 HOH   HOH A . 
G 6 HOH   66  566 169  HOH   HOH A . 
G 6 HOH   67  567 66   HOH   HOH A . 
G 6 HOH   68  568 39   HOH   HOH A . 
G 6 HOH   69  569 8    HOH   HOH A . 
G 6 HOH   70  570 2    HOH   HOH A . 
G 6 HOH   71  571 939  HOH   HOH A . 
G 6 HOH   72  572 18   HOH   HOH A . 
G 6 HOH   73  573 5    HOH   HOH A . 
G 6 HOH   74  574 17   HOH   HOH A . 
G 6 HOH   75  575 19   HOH   HOH A . 
G 6 HOH   76  576 78   HOH   HOH A . 
G 6 HOH   77  577 186  HOH   HOH A . 
G 6 HOH   78  578 81   HOH   HOH A . 
G 6 HOH   79  579 139  HOH   HOH A . 
G 6 HOH   80  580 56   HOH   HOH A . 
G 6 HOH   81  581 396  HOH   HOH A . 
G 6 HOH   82  582 5    HOH   HOH A . 
G 6 HOH   83  583 159  HOH   HOH A . 
G 6 HOH   84  584 154  HOH   HOH A . 
G 6 HOH   85  585 46   HOH   HOH A . 
G 6 HOH   86  586 138  HOH   HOH A . 
G 6 HOH   87  587 162  HOH   HOH A . 
G 6 HOH   88  588 45   HOH   HOH A . 
G 6 HOH   89  589 1275 HOH   HOH A . 
G 6 HOH   90  590 9    HOH   HOH A . 
G 6 HOH   91  591 278  HOH   HOH A . 
G 6 HOH   92  592 366  HOH   HOH A . 
G 6 HOH   93  593 15   HOH   HOH A . 
G 6 HOH   94  594 116  HOH   HOH A . 
G 6 HOH   95  595 134  HOH   HOH A . 
G 6 HOH   96  596 27   HOH   HOH A . 
G 6 HOH   97  597 14   HOH   HOH A . 
G 6 HOH   98  598 83   HOH   HOH A . 
G 6 HOH   99  599 58   HOH   HOH A . 
G 6 HOH   100 600 405  HOH   HOH A . 
G 6 HOH   101 601 381  HOH   HOH A . 
G 6 HOH   102 602 85   HOH   HOH A . 
G 6 HOH   103 603 67   HOH   HOH A . 
G 6 HOH   104 604 12   HOH   HOH A . 
G 6 HOH   105 605 74   HOH   HOH A . 
G 6 HOH   106 606 662  HOH   HOH A . 
G 6 HOH   107 607 115  HOH   HOH A . 
G 6 HOH   108 608 4    HOH   HOH A . 
G 6 HOH   109 609 24   HOH   HOH A . 
G 6 HOH   110 610 1315 HOH   HOH A . 
G 6 HOH   111 611 25   HOH   HOH A . 
G 6 HOH   112 612 148  HOH   HOH A . 
G 6 HOH   113 613 1309 HOH   HOH A . 
G 6 HOH   114 614 6    HOH   HOH A . 
G 6 HOH   115 615 281  HOH   HOH A . 
G 6 HOH   116 616 1068 HOH   HOH A . 
G 6 HOH   117 617 3    HOH   HOH A . 
G 6 HOH   118 618 123  HOH   HOH A . 
G 6 HOH   119 619 68   HOH   HOH A . 
G 6 HOH   120 620 303  HOH   HOH A . 
G 6 HOH   121 621 1310 HOH   HOH A . 
G 6 HOH   122 622 53   HOH   HOH A . 
G 6 HOH   123 623 8    HOH   HOH A . 
G 6 HOH   124 624 51   HOH   HOH A . 
G 6 HOH   125 625 333  HOH   HOH A . 
G 6 HOH   126 626 121  HOH   HOH A . 
G 6 HOH   127 627 125  HOH   HOH A . 
G 6 HOH   128 628 582  HOH   HOH A . 
G 6 HOH   129 629 944  HOH   HOH A . 
G 6 HOH   130 630 1238 HOH   HOH A . 
G 6 HOH   131 631 397  HOH   HOH A . 
G 6 HOH   132 632 122  HOH   HOH A . 
G 6 HOH   133 633 3    HOH   HOH A . 
G 6 HOH   134 634 212  HOH   HOH A . 
G 6 HOH   135 635 95   HOH   HOH A . 
G 6 HOH   136 636 18   HOH   HOH A . 
G 6 HOH   137 637 1289 HOH   HOH A . 
G 6 HOH   138 638 1279 HOH   HOH A . 
G 6 HOH   139 639 156  HOH   HOH A . 
G 6 HOH   140 640 576  HOH   HOH A . 
G 6 HOH   141 641 1222 HOH   HOH A . 
G 6 HOH   142 642 16   HOH   HOH A . 
G 6 HOH   143 643 73   HOH   HOH A . 
G 6 HOH   144 644 80   HOH   HOH A . 
G 6 HOH   145 645 71   HOH   HOH A . 
G 6 HOH   146 646 94   HOH   HOH A . 
G 6 HOH   147 647 70   HOH   HOH A . 
G 6 HOH   148 648 1094 HOH   HOH A . 
G 6 HOH   149 649 7    HOH   HOH A . 
G 6 HOH   150 650 188  HOH   HOH A . 
G 6 HOH   151 651 952  HOH   HOH A . 
G 6 HOH   152 652 40   HOH   HOH A . 
G 6 HOH   153 653 1189 HOH   HOH A . 
G 6 HOH   154 654 104  HOH   HOH A . 
G 6 HOH   155 655 79   HOH   HOH A . 
G 6 HOH   156 656 97   HOH   HOH A . 
G 6 HOH   157 657 1286 HOH   HOH A . 
G 6 HOH   158 658 509  HOH   HOH A . 
G 6 HOH   159 659 1134 HOH   HOH A . 
G 6 HOH   160 660 107  HOH   HOH A . 
G 6 HOH   161 661 330  HOH   HOH A . 
G 6 HOH   162 662 726  HOH   HOH A . 
G 6 HOH   163 663 163  HOH   HOH A . 
G 6 HOH   164 664 11   HOH   HOH A . 
G 6 HOH   165 665 1119 HOH   HOH A . 
G 6 HOH   166 666 280  HOH   HOH A . 
G 6 HOH   167 667 1    HOH   HOH A . 
G 6 HOH   168 668 756  HOH   HOH A . 
G 6 HOH   169 669 408  HOH   HOH A . 
G 6 HOH   170 670 319  HOH   HOH A . 
G 6 HOH   171 671 801  HOH   HOH A . 
G 6 HOH   172 672 126  HOH   HOH A . 
G 6 HOH   173 673 556  HOH   HOH A . 
G 6 HOH   174 674 361  HOH   HOH A . 
G 6 HOH   175 675 342  HOH   HOH A . 
G 6 HOH   176 676 370  HOH   HOH A . 
G 6 HOH   177 677 250  HOH   HOH A . 
G 6 HOH   178 678 63   HOH   HOH A . 
G 6 HOH   179 679 1307 HOH   HOH A . 
G 6 HOH   180 680 1284 HOH   HOH A . 
G 6 HOH   181 681 1276 HOH   HOH A . 
G 6 HOH   182 682 20   HOH   HOH A . 
G 6 HOH   183 683 1287 HOH   HOH A . 
G 6 HOH   184 684 1306 HOH   HOH A . 
G 6 HOH   185 685 135  HOH   HOH A . 
G 6 HOH   186 686 224  HOH   HOH A . 
G 6 HOH   187 687 202  HOH   HOH A . 
G 6 HOH   188 688 695  HOH   HOH A . 
G 6 HOH   189 689 674  HOH   HOH A . 
G 6 HOH   190 690 711  HOH   HOH A . 
G 6 HOH   191 691 318  HOH   HOH A . 
G 6 HOH   192 692 521  HOH   HOH A . 
G 6 HOH   193 693 941  HOH   HOH A . 
G 6 HOH   194 694 267  HOH   HOH A . 
G 6 HOH   195 695 981  HOH   HOH A . 
G 6 HOH   196 696 331  HOH   HOH A . 
G 6 HOH   197 697 309  HOH   HOH A . 
G 6 HOH   198 698 315  HOH   HOH A . 
G 6 HOH   199 699 1299 HOH   HOH A . 
G 6 HOH   200 700 208  HOH   HOH A . 
G 6 HOH   201 701 152  HOH   HOH A . 
G 6 HOH   202 702 4    HOH   HOH A . 
G 6 HOH   203 703 1314 HOH   HOH A . 
G 6 HOH   204 704 919  HOH   HOH A . 
G 6 HOH   205 705 805  HOH   HOH A . 
G 6 HOH   206 706 13   HOH   HOH A . 
G 6 HOH   207 707 263  HOH   HOH A . 
G 6 HOH   208 708 180  HOH   HOH A . 
G 6 HOH   209 709 1071 HOH   HOH A . 
G 6 HOH   210 710 356  HOH   HOH A . 
G 6 HOH   211 711 363  HOH   HOH A . 
G 6 HOH   212 712 326  HOH   HOH A . 
G 6 HOH   213 713 371  HOH   HOH A . 
G 6 HOH   214 714 313  HOH   HOH A . 
G 6 HOH   215 715 16   HOH   HOH A . 
G 6 HOH   216 716 185  HOH   HOH A . 
G 6 HOH   217 717 429  HOH   HOH A . 
G 6 HOH   218 718 772  HOH   HOH A . 
G 6 HOH   219 719 376  HOH   HOH A . 
G 6 HOH   220 720 1074 HOH   HOH A . 
G 6 HOH   221 721 1292 HOH   HOH A . 
G 6 HOH   222 722 346  HOH   HOH A . 
G 6 HOH   223 723 12   HOH   HOH A . 
G 6 HOH   224 724 1078 HOH   HOH A . 
H 6 HOH   1   201 64   HOH   HOH B . 
H 6 HOH   2   202 240  HOH   HOH B . 
H 6 HOH   3   203 1249 HOH   HOH B . 
H 6 HOH   4   204 549  HOH   HOH B . 
H 6 HOH   5   205 205  HOH   HOH B . 
H 6 HOH   6   206 398  HOH   HOH B . 
H 6 HOH   7   207 364  HOH   HOH B . 
H 6 HOH   8   208 232  HOH   HOH B . 
H 6 HOH   9   209 50   HOH   HOH B . 
H 6 HOH   10  210 120  HOH   HOH B . 
H 6 HOH   11  211 353  HOH   HOH B . 
H 6 HOH   12  212 531  HOH   HOH B . 
H 6 HOH   13  213 358  HOH   HOH B . 
H 6 HOH   14  214 743  HOH   HOH B . 
H 6 HOH   15  215 758  HOH   HOH B . 
H 6 HOH   16  216 264  HOH   HOH B . 
H 6 HOH   17  217 900  HOH   HOH B . 
H 6 HOH   18  218 452  HOH   HOH B . 
H 6 HOH   19  219 332  HOH   HOH B . 
H 6 HOH   20  220 15   HOH   HOH B . 
H 6 HOH   21  221 1140 HOH   HOH B . 
H 6 HOH   22  222 82   HOH   HOH B . 
H 6 HOH   23  223 343  HOH   HOH B . 
H 6 HOH   24  224 75   HOH   HOH B . 
H 6 HOH   25  225 1278 HOH   HOH B . 
H 6 HOH   26  226 54   HOH   HOH B . 
H 6 HOH   27  227 444  HOH   HOH B . 
H 6 HOH   28  228 69   HOH   HOH B . 
H 6 HOH   29  229 41   HOH   HOH B . 
H 6 HOH   30  230 654  HOH   HOH B . 
H 6 HOH   31  231 128  HOH   HOH B . 
H 6 HOH   32  232 723  HOH   HOH B . 
H 6 HOH   33  233 110  HOH   HOH B . 
H 6 HOH   34  234 131  HOH   HOH B . 
H 6 HOH   35  235 300  HOH   HOH B . 
H 6 HOH   36  236 103  HOH   HOH B . 
H 6 HOH   37  237 391  HOH   HOH B . 
H 6 HOH   38  238 129  HOH   HOH B . 
H 6 HOH   39  239 1    HOH   HOH B . 
H 6 HOH   40  240 1312 HOH   HOH B . 
H 6 HOH   41  241 60   HOH   HOH B . 
H 6 HOH   42  242 166  HOH   HOH B . 
H 6 HOH   43  243 52   HOH   HOH B . 
H 6 HOH   44  244 325  HOH   HOH B . 
H 6 HOH   45  245 77   HOH   HOH B . 
H 6 HOH   46  246 127  HOH   HOH B . 
H 6 HOH   47  247 272  HOH   HOH B . 
H 6 HOH   48  248 181  HOH   HOH B . 
H 6 HOH   49  249 172  HOH   HOH B . 
H 6 HOH   50  250 221  HOH   HOH B . 
H 6 HOH   51  251 133  HOH   HOH B . 
H 6 HOH   52  252 9    HOH   HOH B . 
H 6 HOH   53  253 276  HOH   HOH B . 
H 6 HOH   54  254 14   HOH   HOH B . 
H 6 HOH   55  255 30   HOH   HOH B . 
H 6 HOH   56  256 144  HOH   HOH B . 
H 6 HOH   57  257 72   HOH   HOH B . 
H 6 HOH   58  258 31   HOH   HOH B . 
H 6 HOH   59  259 47   HOH   HOH B . 
H 6 HOH   60  260 150  HOH   HOH B . 
H 6 HOH   61  261 416  HOH   HOH B . 
H 6 HOH   62  262 10   HOH   HOH B . 
H 6 HOH   63  263 117  HOH   HOH B . 
H 6 HOH   64  264 231  HOH   HOH B . 
H 6 HOH   65  265 62   HOH   HOH B . 
H 6 HOH   66  266 143  HOH   HOH B . 
H 6 HOH   67  267 243  HOH   HOH B . 
H 6 HOH   68  268 59   HOH   HOH B . 
H 6 HOH   69  269 1277 HOH   HOH B . 
H 6 HOH   70  270 271  HOH   HOH B . 
H 6 HOH   71  271 287  HOH   HOH B . 
H 6 HOH   72  272 347  HOH   HOH B . 
H 6 HOH   73  273 11   HOH   HOH B . 
H 6 HOH   74  274 147  HOH   HOH B . 
H 6 HOH   75  275 20   HOH   HOH B . 
H 6 HOH   76  276 252  HOH   HOH B . 
H 6 HOH   77  277 1106 HOH   HOH B . 
H 6 HOH   78  278 1285 HOH   HOH B . 
H 6 HOH   79  279 242  HOH   HOH B . 
H 6 HOH   80  280 302  HOH   HOH B . 
H 6 HOH   81  281 1305 HOH   HOH B . 
H 6 HOH   82  282 282  HOH   HOH B . 
H 6 HOH   83  283 84   HOH   HOH B . 
H 6 HOH   84  284 61   HOH   HOH B . 
H 6 HOH   85  285 114  HOH   HOH B . 
H 6 HOH   86  286 22   HOH   HOH B . 
H 6 HOH   87  287 207  HOH   HOH B . 
H 6 HOH   88  288 175  HOH   HOH B . 
H 6 HOH   89  289 43   HOH   HOH B . 
H 6 HOH   90  290 960  HOH   HOH B . 
H 6 HOH   91  291 235  HOH   HOH B . 
H 6 HOH   92  292 220  HOH   HOH B . 
H 6 HOH   93  293 88   HOH   HOH B . 
H 6 HOH   94  294 106  HOH   HOH B . 
H 6 HOH   95  295 13   HOH   HOH B . 
H 6 HOH   96  296 89   HOH   HOH B . 
H 6 HOH   97  297 160  HOH   HOH B . 
H 6 HOH   98  298 137  HOH   HOH B . 
H 6 HOH   99  299 1066 HOH   HOH B . 
H 6 HOH   100 300 99   HOH   HOH B . 
H 6 HOH   101 301 216  HOH   HOH B . 
H 6 HOH   102 302 112  HOH   HOH B . 
H 6 HOH   103 303 182  HOH   HOH B . 
H 6 HOH   104 304 297  HOH   HOH B . 
H 6 HOH   105 305 38   HOH   HOH B . 
H 6 HOH   106 306 118  HOH   HOH B . 
H 6 HOH   107 307 142  HOH   HOH B . 
H 6 HOH   108 308 316  HOH   HOH B . 
H 6 HOH   109 309 101  HOH   HOH B . 
H 6 HOH   110 310 170  HOH   HOH B . 
H 6 HOH   111 311 635  HOH   HOH B . 
H 6 HOH   112 312 44   HOH   HOH B . 
H 6 HOH   113 313 32   HOH   HOH B . 
H 6 HOH   114 314 23   HOH   HOH B . 
H 6 HOH   115 315 177  HOH   HOH B . 
H 6 HOH   116 316 311  HOH   HOH B . 
H 6 HOH   117 317 37   HOH   HOH B . 
H 6 HOH   118 318 215  HOH   HOH B . 
H 6 HOH   119 319 1291 HOH   HOH B . 
H 6 HOH   120 320 55   HOH   HOH B . 
H 6 HOH   121 321 48   HOH   HOH B . 
H 6 HOH   122 322 91   HOH   HOH B . 
H 6 HOH   123 323 197  HOH   HOH B . 
H 6 HOH   124 324 299  HOH   HOH B . 
H 6 HOH   125 325 28   HOH   HOH B . 
H 6 HOH   126 326 341  HOH   HOH B . 
H 6 HOH   127 327 387  HOH   HOH B . 
H 6 HOH   128 328 445  HOH   HOH B . 
H 6 HOH   129 329 100  HOH   HOH B . 
H 6 HOH   130 330 98   HOH   HOH B . 
H 6 HOH   131 331 704  HOH   HOH B . 
H 6 HOH   132 332 1294 HOH   HOH B . 
H 6 HOH   133 333 29   HOH   HOH B . 
H 6 HOH   134 334 1274 HOH   HOH B . 
H 6 HOH   135 335 717  HOH   HOH B . 
H 6 HOH   136 336 141  HOH   HOH B . 
H 6 HOH   137 337 87   HOH   HOH B . 
H 6 HOH   138 338 334  HOH   HOH B . 
H 6 HOH   139 339 161  HOH   HOH B . 
H 6 HOH   140 340 65   HOH   HOH B . 
H 6 HOH   141 341 1293 HOH   HOH B . 
H 6 HOH   142 342 234  HOH   HOH B . 
H 6 HOH   143 343 619  HOH   HOH B . 
H 6 HOH   144 344 1126 HOH   HOH B . 
H 6 HOH   145 345 178  HOH   HOH B . 
H 6 HOH   146 346 362  HOH   HOH B . 
H 6 HOH   147 347 90   HOH   HOH B . 
H 6 HOH   148 348 1304 HOH   HOH B . 
H 6 HOH   149 349 339  HOH   HOH B . 
H 6 HOH   150 350 623  HOH   HOH B . 
H 6 HOH   151 351 1280 HOH   HOH B . 
H 6 HOH   152 352 463  HOH   HOH B . 
H 6 HOH   153 353 191  HOH   HOH B . 
H 6 HOH   154 354 335  HOH   HOH B . 
H 6 HOH   155 355 1077 HOH   HOH B . 
H 6 HOH   156 356 203  HOH   HOH B . 
H 6 HOH   157 357 1046 HOH   HOH B . 
H 6 HOH   158 358 304  HOH   HOH B . 
H 6 HOH   159 359 290  HOH   HOH B . 
H 6 HOH   160 360 718  HOH   HOH B . 
H 6 HOH   161 361 541  HOH   HOH B . 
H 6 HOH   162 362 389  HOH   HOH B . 
H 6 HOH   163 363 283  HOH   HOH B . 
H 6 HOH   164 364 1072 HOH   HOH B . 
H 6 HOH   165 365 291  HOH   HOH B . 
H 6 HOH   166 366 479  HOH   HOH B . 
H 6 HOH   167 367 615  HOH   HOH B . 
H 6 HOH   168 368 340  HOH   HOH B . 
H 6 HOH   169 369 898  HOH   HOH B . 
H 6 HOH   170 370 1316 HOH   HOH B . 
H 6 HOH   171 371 667  HOH   HOH B . 
H 6 HOH   172 372 373  HOH   HOH B . 
H 6 HOH   173 373 418  HOH   HOH B . 
H 6 HOH   174 374 310  HOH   HOH B . 
H 6 HOH   175 375 1303 HOH   HOH B . 
H 6 HOH   176 376 190  HOH   HOH B . 
H 6 HOH   177 377 431  HOH   HOH B . 
H 6 HOH   178 378 183  HOH   HOH B . 
H 6 HOH   179 379 149  HOH   HOH B . 
H 6 HOH   180 380 1000 HOH   HOH B . 
H 6 HOH   181 381 1173 HOH   HOH B . 
H 6 HOH   182 382 1311 HOH   HOH B . 
H 6 HOH   183 383 1163 HOH   HOH B . 
H 6 HOH   184 384 424  HOH   HOH B . 
H 6 HOH   185 385 491  HOH   HOH B . 
H 6 HOH   186 386 176  HOH   HOH B . 
H 6 HOH   187 387 1298 HOH   HOH B . 
H 6 HOH   188 388 248  HOH   HOH B . 
H 6 HOH   189 389 265  HOH   HOH B . 
H 6 HOH   190 390 470  HOH   HOH B . 
H 6 HOH   191 391 360  HOH   HOH B . 
H 6 HOH   192 392 350  HOH   HOH B . 
H 6 HOH   193 393 184  HOH   HOH B . 
H 6 HOH   194 394 410  HOH   HOH B . 
H 6 HOH   195 395 355  HOH   HOH B . 
H 6 HOH   196 396 274  HOH   HOH B . 
H 6 HOH   197 397 157  HOH   HOH B . 
H 6 HOH   198 398 314  HOH   HOH B . 
H 6 HOH   199 399 566  HOH   HOH B . 
H 6 HOH   200 400 792  HOH   HOH B . 
H 6 HOH   201 401 321  HOH   HOH B . 
H 6 HOH   202 402 558  HOH   HOH B . 
# 
loop_
_software.pdbx_ordinal 
_software.name 
_software.version 
_software.date 
_software.type 
_software.contact_author 
_software.contact_author_email 
_software.classification 
_software.location 
_software.language 
_software.citation_id 
1 PHENIX      1.21.1_5286    ?               package 'Paul D. Adams'   PDAdams@lbl.gov                         refinement        
http://www.phenix-online.org/                                                C++ ? 
2 Aimless     0.7.15         02/11/23        program 'Phil Evans'      ?                                       'data scaling'    
http://www.mrc-lmb.cam.ac.uk/harry/pre/aimless.html                          ?   ? 
3 PDB_EXTRACT 3.28           'Apr. 15, 2021' package PDB               deposit@deposit.rcsb.org                'data extraction' 
http://sw-tools.pdb.org/apps/PDB_EXTRACT/                                    C++ ? 
4 XDS         'Jun 30, 2023' 'Jun. 30, 2023' program 'Wolfgang Kabsch' Wolfgang.Kabsch@mpimf-heidelberg.mpg.de 'data reduction'  
http://xds.mpimf-heidelberg.mpg.de                                           ?   ? 
5 PHASER      2.8.3          'May 17, 2020'  program 'Randy J. Read'   cimr-phaser@lists.cam.ac.uk             phasing           
https://www.phaser.cimr.cam.ac.uk/index.php/Phaser_Crystallographic_Software ?   ? 
# 
_cell.entry_id           7HCR 
_cell.length_a           88.714 
_cell.length_b           88.714 
_cell.length_c           39.413 
_cell.angle_alpha        90.000 
_cell.angle_beta         90.000 
_cell.angle_gamma        90.000 
_cell.Z_PDB              8 
_cell.pdbx_unique_axis   ? 
# 
_symmetry.entry_id                         7HCR 
_symmetry.space_group_name_H-M             'P 43' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                78 
# 
_exptl.method            'X-RAY DIFFRACTION' 
_exptl.crystals_number   1 
_exptl.entry_id          7HCR 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.13 
_exptl_crystal.density_percent_sol   42.42 
_exptl_crystal.density_meas          ? 
_exptl_crystal.description           ? 
# 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, HANGING DROP' 
_exptl_crystal_grow.pH              9.5 
_exptl_crystal_grow.temp            292 
_exptl_crystal_grow.pdbx_details    '100 mM CHES, 28% PEG 3000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp_details    ? 
# 
_diffrn.id                     1 
_diffrn.crystal_id             1 
_diffrn.ambient_temp           100 
_diffrn.ambient_temp_details   ? 
# 
_diffrn_detector.diffrn_id              1 
_diffrn_detector.detector               PIXEL 
_diffrn_detector.type                   'DECTRIS PILATUS3 6M' 
_diffrn_detector.pdbx_collection_date   2023-03-04 
_diffrn_detector.details                ? 
# 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.pdbx_scattering_type             x-ray 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.monochromator                    ? 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.88557 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.diffrn_id                   1 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.type                        'ALS BEAMLINE 8.3.1' 
_diffrn_source.pdbx_wavelength_list        0.88557 
_diffrn_source.pdbx_synchrotron_site       ALS 
_diffrn_source.pdbx_synchrotron_beamline   8.3.1 
_diffrn_source.pdbx_wavelength             ? 
# 
_reflns.entry_id                     7HCR 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.360 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   164461 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.400 
_reflns.pdbx_Rmerge_I_obs            0.048 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        13.500 
_reflns.B_iso_Wilson_estimate        12.290 
_reflns.pdbx_redundancy              6.300 
_reflns.pdbx_Rrim_I_all              0.052 
_reflns.pdbx_Rpim_I_all              0.020 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1042792 
_reflns.pdbx_scaling_rejects         ? 
_reflns.pdbx_chi_squared             ? 
_reflns.Rmerge_F_all                 ? 
_reflns.Rmerge_F_obs                 ? 
_reflns.observed_criterion_F_max     ? 
_reflns.observed_criterion_F_min     ? 
_reflns.observed_criterion_I_max     ? 
_reflns.observed_criterion_I_min     ? 
_reflns.pdbx_d_res_high_opt          ? 
_reflns.pdbx_d_res_low_opt           ? 
_reflns.details                      ? 
_reflns.pdbx_CC_star                 ? 
# 
loop_
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_ordinal 
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.number_measured_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_unique_obs 
_reflns_shell.pdbx_rejects 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_redundancy 
_reflns_shell.percent_possible_obs 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.Rmerge_I_all 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.percent_possible_all 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
1 1 1.000 1.020  ? 33133 7295 ? 2.060 ? ? ? 4.500 ? 0.500  ? ? ? ? ? ? 89.300 2.322 1.041 0.408 ? 
1 2 5.480 44.360 ? 7463  1091 ? 0.023 ? ? ? 6.800 ? 54.800 ? ? ? ? ? ? 99.900 0.025 0.009 0.999 ? 
# 
_refine.entry_id                                 7HCR 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             44.3600 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.2500 
_refine.ls_number_reflns_obs                     164181 
_refine.ls_number_reflns_all                     ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.ls_matrix_type                           ? 
_refine.pdbx_R_Free_selection_details            ? 
_refine.details                                  ? 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1494 
_refine.ls_R_factor_R_work                       0.1487 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1646 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7908 
_refine.ls_number_reflns_R_work                  156273 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               19.6346 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.overall_SU_R_free                        ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.overall_SU_ML                            0.1200 
_refine.overall_SU_B                             ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.pdbx_solvent_vdw_probe_radii             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.ls_number_parameters                     ? 
_refine.ls_number_restraints                     ? 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.B_iso_max                                78.840 
_refine.B_iso_min                                7.660 
_refine.pdbx_overall_phase_error                 19.0500 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.pdbx_diffrn_id                           1 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.ls_R_factor_R_free_error_details         ? 
# 
_refine_hist.cycle_id                         final 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.d_res_high                       1.0000 
_refine_hist.d_res_low                        44.3600 
_refine_hist.pdbx_number_atoms_ligand         73 
_refine_hist.number_atoms_solvent             426 
_refine_hist.number_atoms_total               3041 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           16.53 
_refine_hist.pdbx_B_iso_mean_solvent          31.57 
_refine_hist.pdbx_number_atoms_protein        2542 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
# 
loop_
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.R_factor_R_free 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.R_factor_obs 
1.0000 1.0100  30 84.0000  4443 . 0.4477 0.4391 . 226 0.0000 4669 . 'X-RAY DIFFRACTION' . 
1.0100 1.0200  30 95.0000  4945 . 0.3901 0.4043 . 214 0.0000 5159 . 'X-RAY DIFFRACTION' . 
1.0200 1.0400  30 100.0000 5260 . 0.3291 0.3027 . 266 0.0000 5526 . 'X-RAY DIFFRACTION' . 
1.0400 1.0500  30 100.0000 5147 . 0.2875 0.2936 . 271 0.0000 5418 . 'X-RAY DIFFRACTION' . 
1.0500 1.0600  30 100.0000 5201 . 0.2638 0.2936 . 319 0.0000 5520 . 'X-RAY DIFFRACTION' . 
1.0600 1.0800  30 100.0000 5217 . 0.2475 0.2585 . 253 0.0000 5470 . 'X-RAY DIFFRACTION' . 
1.0800 1.0900  30 100.0000 5247 . 0.2198 0.2437 . 254 0.0000 5501 . 'X-RAY DIFFRACTION' . 
1.0900 1.1100  30 100.0000 5204 . 0.1987 0.2215 . 252 0.0000 5456 . 'X-RAY DIFFRACTION' . 
1.1100 1.1300  30 100.0000 5223 . 0.1882 0.1892 . 270 0.0000 5493 . 'X-RAY DIFFRACTION' . 
1.1300 1.1400  30 100.0000 5207 . 0.1696 0.1916 . 246 0.0000 5453 . 'X-RAY DIFFRACTION' . 
1.1500 1.1600  30 100.0000 5244 . 0.1589 0.1931 . 272 0.0000 5516 . 'X-RAY DIFFRACTION' . 
1.1600 1.1900  30 100.0000 5247 . 0.1510 0.1858 . 268 0.0000 5515 . 'X-RAY DIFFRACTION' . 
1.1900 1.2100  30 100.0000 5143 . 0.1385 0.1621 . 283 0.0000 5426 . 'X-RAY DIFFRACTION' . 
1.2100 1.2300  30 100.0000 5322 . 0.1315 0.1615 . 217 0.0000 5539 . 'X-RAY DIFFRACTION' . 
1.2300 1.2600  30 100.0000 5189 . 0.1329 0.1556 . 264 0.0000 5453 . 'X-RAY DIFFRACTION' . 
1.2600 1.2900  30 100.0000 5243 . 0.1311 0.1531 . 270 0.0000 5513 . 'X-RAY DIFFRACTION' . 
1.2900 1.3200  30 100.0000 5209 . 0.1302 0.1524 . 287 0.0000 5496 . 'X-RAY DIFFRACTION' . 
1.3200 1.3600  30 100.0000 5233 . 0.1338 0.1603 . 276 0.0000 5509 . 'X-RAY DIFFRACTION' . 
1.3600 1.4000  30 100.0000 5249 . 0.1370 0.1622 . 255 0.0000 5504 . 'X-RAY DIFFRACTION' . 
1.4000 1.4400  30 100.0000 5218 . 0.1326 0.1601 . 263 0.0000 5481 . 'X-RAY DIFFRACTION' . 
1.4400 1.4900  30 100.0000 5285 . 0.1274 0.1336 . 245 0.0000 5530 . 'X-RAY DIFFRACTION' . 
1.4900 1.5500  30 100.0000 5206 . 0.1205 0.1372 . 285 0.0000 5491 . 'X-RAY DIFFRACTION' . 
1.5500 1.6200  30 100.0000 5262 . 0.1216 0.1433 . 272 0.0000 5534 . 'X-RAY DIFFRACTION' . 
1.6200 1.7100  30 100.0000 5279 . 0.1295 0.1474 . 245 0.0000 5524 . 'X-RAY DIFFRACTION' . 
1.7100 1.8200  30 100.0000 5255 . 0.1365 0.1445 . 253 0.0000 5508 . 'X-RAY DIFFRACTION' . 
1.8200 1.9600  30 100.0000 5264 . 0.1334 0.1316 . 283 0.0000 5547 . 'X-RAY DIFFRACTION' . 
1.9600 2.1500  30 100.0000 5280 . 0.1356 0.1459 . 287 0.0000 5567 . 'X-RAY DIFFRACTION' . 
2.1600 2.4700  30 100.0000 5274 . 0.1359 0.1434 . 288 0.0000 5562 . 'X-RAY DIFFRACTION' . 
2.4700 3.1100  30 100.0000 5312 . 0.1484 0.1660 . 254 0.0000 5566 . 'X-RAY DIFFRACTION' . 
3.1100 44.3600 30 100.0000 5465 . 0.1526 0.1777 . 270 0.0000 5735 . 'X-RAY DIFFRACTION' . 
# 
_struct.entry_id                  7HCR 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0000611' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HCR 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN, Hydrolase' 
_struct_keywords.text            'Macrodomain, ADP-ribose, SARS-CoV-2, fragment-based drug discovery, VIRAL PROTEIN, Hydrolase' 
# 
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 5 ? 
G N N 6 ? 
H N N 6 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    R1AB_SARS2 
_struct_ref.pdbx_db_accession          P0DTD1 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;VNSFSGYLKLTDNVYIKNADIVEEAKKVKPTVVVNAANVYLKHGGGVAGALNKATNNAMQVESDDYIATNGPLKVGGSCV
LSGHNLAKHCLHVVGPNVNKGEDIQLLKSAYENFNQHEVLLAPLLSAGIFGADPIHSLRVCVDTVRTNVYLAVFDKNLYD
KLVSSFL
;
_struct_ref.pdbx_align_begin           1025 
# 
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 7HCR A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HCR B 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 7HCR SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HCR MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HCR SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HCR MET B 2 ? UNP P0DTD1 ? ? 'expression tag' 2 4 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G 
2 1 B,H         
# 
_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 ASP A 22  ? LYS A 31  ? ASP A 22  LYS A 31  1 ? 10 
HELX_P HELX_P2  AA2 GLY A 47  ? THR A 57  ? GLY A 47  THR A 57  1 ? 11 
HELX_P HELX_P3  AA3 ASN A 59  ? GLY A 73  ? ASN A 59  GLY A 73  1 ? 15 
HELX_P HELX_P4  AA4 ASN A 99  ? GLY A 103 ? ASN A 99  GLY A 103 5 ? 5  
HELX_P HELX_P5  AA5 GLN A 107 ? ASN A 115 ? GLN A 107 ASN A 115 1 ? 9  
HELX_P HELX_P6  AA6 PHE A 116 ? HIS A 119 ? PHE A 116 HIS A 119 5 ? 4  
HELX_P HELX_P7  AA7 ALA A 129 ? GLY A 133 ? ALA A 129 GLY A 133 5 ? 5  
HELX_P HELX_P8  AA8 ASP A 135 ? VAL A 147 ? ASP A 135 VAL A 147 1 ? 13 
HELX_P HELX_P9  AA9 ASP A 157 ? SER A 167 ? ASP A 157 SER A 167 1 ? 11 
HELX_P HELX_P10 AB1 ASP B 22  ? LYS B 31  ? ASP B 22  LYS B 31  1 ? 10 
HELX_P HELX_P11 AB2 GLY B 47  ? THR B 57  ? GLY B 47  THR B 57  1 ? 11 
HELX_P HELX_P12 AB3 ASN B 59  ? GLY B 73  ? ASN B 59  GLY B 73  1 ? 15 
HELX_P HELX_P13 AB4 ASN B 99  ? GLY B 103 ? ASN B 99  GLY B 103 5 ? 5  
HELX_P HELX_P14 AB5 ASP B 105 ? GLN B 107 ? ASP B 105 GLN B 107 5 ? 3  
HELX_P HELX_P15 AB6 LEU B 108 ? ASN B 115 ? LEU B 108 ASN B 115 1 ? 8  
HELX_P HELX_P16 AB7 PHE B 116 ? HIS B 119 ? PHE B 116 HIS B 119 5 ? 4  
HELX_P HELX_P17 AB8 ALA B 129 ? GLY B 133 ? ALA B 129 GLY B 133 5 ? 5  
HELX_P HELX_P18 AB9 ASP B 135 ? VAL B 147 ? ASP B 135 VAL B 147 1 ? 13 
HELX_P HELX_P19 AC1 ASP B 157 ? LEU B 169 ? ASP B 157 LEU B 169 1 ? 13 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 3 ? 
AA3 ? 4 ? 
AA4 ? 3 ? 
# 
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 ? parallel      
AA1 3 4 ? parallel      
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA4 1 2 ? parallel      
AA4 2 3 ? 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 LEU A 10  ? LYS A 11  ? LEU A 10  LYS A 11  
AA1 2 VAL A 16  ? ASN A 20  ? VAL A 16  ASN A 20  
AA1 3 ASN A 150 ? VAL A 155 ? ASN A 150 VAL A 155 
AA1 4 VAL A 121 ? ALA A 124 ? VAL A 121 ALA A 124 
AA2 1 VAL A 34  ? ALA A 38  ? VAL A 34  ALA A 38  
AA2 2 HIS A 91  ? VAL A 95  ? HIS A 91  VAL A 95  
AA2 3 SER A 80  ? SER A 84  ? SER A 80  SER A 84  
AA3 1 LEU B 10  ? LYS B 11  ? LEU B 10  LYS B 11  
AA3 2 VAL B 16  ? ASN B 20  ? VAL B 16  ASN B 20  
AA3 3 ASN B 150 ? VAL B 155 ? ASN B 150 VAL B 155 
AA3 4 VAL B 121 ? ALA B 124 ? VAL B 121 ALA B 124 
AA4 1 VAL B 34  ? ALA B 38  ? VAL B 34  ALA B 38  
AA4 2 HIS B 91  ? VAL B 95  ? HIS B 91  VAL B 95  
AA4 3 SER B 80  ? SER B 84  ? SER B 80  SER B 84  
# 
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 N LEU A 10  ? N LEU A 10  O ILE A 18  ? O ILE A 18  
AA1 2 3 N TYR A 17  ? N TYR A 17  O LEU A 153 ? O LEU A 153 
AA1 3 4 O TYR A 152 ? O TYR A 152 N LEU A 122 ? N LEU A 122 
AA2 1 2 N ASN A 37  ? N ASN A 37  O VAL A 95  ? O VAL A 95  
AA2 2 3 O CYS A 92  ? O CYS A 92  N LEU A 83  ? N LEU A 83  
AA3 1 2 N LEU B 10  ? N LEU B 10  O ILE B 18  ? O ILE B 18  
AA3 2 3 N TYR B 17  ? N TYR B 17  O LEU B 153 ? O LEU B 153 
AA3 3 4 O TYR B 152 ? O TYR B 152 N LEU B 122 ? N LEU B 122 
AA4 1 2 N ASN B 37  ? N ASN B 37  O LEU B 93  ? O LEU B 93  
AA4 2 3 O CYS B 92  ? O CYS B 92  N LEU B 83  ? N LEU B 83  
# 
_pdbx_entry_details.entry_id                   7HCR 
_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   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 A 86  ? ? 55.72  -132.71 
2 1 SER A 128 ? B 73.40  -8.56   
3 1 ALA A 129 ? B -90.92 -158.16 
4 1 HIS B 86  ? ? 57.34  -127.79 
# 
_phasing.method   MR 
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 721 ? 5.84 . 
2 1 O ? A HOH 722 ? 6.07 . 
3 1 O B A HOH 723 ? 6.70 . 
4 1 O ? A HOH 724 ? 7.68 . 
5 1 O ? B HOH 402 ? 6.48 . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1 1 Y 1 A SER 1 ? A SER 1 
2 1 Y 1 A MET 2 ? A MET 2 
# 
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 
A1A56 N2   N  N N 1   
A1A56 C3   C  N N 2   
A1A56 C6   C  Y N 3   
A1A56 C9   C  Y N 4   
A1A56 C1   C  N N 5   
A1A56 C10  C  Y N 6   
A1A56 C11  C  N N 7   
A1A56 C2   C  N S 8   
A1A56 C4   C  N N 9   
A1A56 C5   C  Y N 10  
A1A56 C7   C  Y N 11  
A1A56 C8   C  Y N 12  
A1A56 N1   N  N N 13  
A1A56 N3   N  Y N 14  
A1A56 N4   N  Y N 15  
A1A56 N5   N  Y N 16  
A1A56 O1   O  N N 17  
A1A56 O2   O  N N 18  
A1A56 H4   H  N N 19  
A1A56 H5   H  N N 20  
A1A56 H8   H  N N 21  
A1A56 H9   H  N N 22  
A1A56 H10  H  N N 23  
A1A56 H13  H  N N 24  
A1A56 H12  H  N N 25  
A1A56 H7   H  N N 26  
A1A56 H6   H  N N 27  
A1A56 H2   H  N N 28  
A1A56 H1   H  N N 29  
A1A56 H11  H  N N 30  
A1A56 H3   H  N N 31  
A1A57 O1   O  N N 32  
A1A57 C1   C  N N 33  
A1A57 C2   C  N R 34  
A1A57 C3   C  N N 35  
A1A57 C4   C  N N 36  
A1A57 C5   C  Y N 37  
A1A57 C6   C  Y N 38  
A1A57 C7   C  Y N 39  
A1A57 C8   C  Y N 40  
A1A57 C10  C  Y N 41  
A1A57 C11  C  N N 42  
A1A57 C9   C  Y N 43  
A1A57 N1   N  N N 44  
A1A57 N2   N  N N 45  
A1A57 N3   N  Y N 46  
A1A57 N4   N  Y N 47  
A1A57 N5   N  Y N 48  
A1A57 O2   O  N N 49  
A1A57 H4   H  N N 50  
A1A57 H5   H  N N 51  
A1A57 H6   H  N N 52  
A1A57 H7   H  N N 53  
A1A57 H8   H  N N 54  
A1A57 H10  H  N N 55  
A1A57 H12  H  N N 56  
A1A57 H13  H  N N 57  
A1A57 H9   H  N N 58  
A1A57 H2   H  N N 59  
A1A57 H1   H  N N 60  
A1A57 H11  H  N N 61  
A1A57 H3   H  N N 62  
ALA   N    N  N N 63  
ALA   CA   C  N S 64  
ALA   C    C  N N 65  
ALA   O    O  N N 66  
ALA   CB   C  N N 67  
ALA   OXT  O  N N 68  
ALA   H    H  N N 69  
ALA   H2   H  N N 70  
ALA   HA   H  N N 71  
ALA   HB1  H  N N 72  
ALA   HB2  H  N N 73  
ALA   HB3  H  N N 74  
ALA   HXT  H  N N 75  
ARG   N    N  N N 76  
ARG   CA   C  N S 77  
ARG   C    C  N N 78  
ARG   O    O  N N 79  
ARG   CB   C  N N 80  
ARG   CG   C  N N 81  
ARG   CD   C  N N 82  
ARG   NE   N  N N 83  
ARG   CZ   C  N N 84  
ARG   NH1  N  N N 85  
ARG   NH2  N  N N 86  
ARG   OXT  O  N N 87  
ARG   H    H  N N 88  
ARG   H2   H  N N 89  
ARG   HA   H  N N 90  
ARG   HB2  H  N N 91  
ARG   HB3  H  N N 92  
ARG   HG2  H  N N 93  
ARG   HG3  H  N N 94  
ARG   HD2  H  N N 95  
ARG   HD3  H  N N 96  
ARG   HE   H  N N 97  
ARG   HH11 H  N N 98  
ARG   HH12 H  N N 99  
ARG   HH21 H  N N 100 
ARG   HH22 H  N N 101 
ARG   HXT  H  N N 102 
ASN   N    N  N N 103 
ASN   CA   C  N S 104 
ASN   C    C  N N 105 
ASN   O    O  N N 106 
ASN   CB   C  N N 107 
ASN   CG   C  N N 108 
ASN   OD1  O  N N 109 
ASN   ND2  N  N N 110 
ASN   OXT  O  N N 111 
ASN   H    H  N N 112 
ASN   H2   H  N N 113 
ASN   HA   H  N N 114 
ASN   HB2  H  N N 115 
ASN   HB3  H  N N 116 
ASN   HD21 H  N N 117 
ASN   HD22 H  N N 118 
ASN   HXT  H  N N 119 
ASP   N    N  N N 120 
ASP   CA   C  N S 121 
ASP   C    C  N N 122 
ASP   O    O  N N 123 
ASP   CB   C  N N 124 
ASP   CG   C  N N 125 
ASP   OD1  O  N N 126 
ASP   OD2  O  N N 127 
ASP   OXT  O  N N 128 
ASP   H    H  N N 129 
ASP   H2   H  N N 130 
ASP   HA   H  N N 131 
ASP   HB2  H  N N 132 
ASP   HB3  H  N N 133 
ASP   HD2  H  N N 134 
ASP   HXT  H  N N 135 
CL    CL   CL N N 136 
CYS   N    N  N N 137 
CYS   CA   C  N R 138 
CYS   C    C  N N 139 
CYS   O    O  N N 140 
CYS   CB   C  N N 141 
CYS   SG   S  N N 142 
CYS   OXT  O  N N 143 
CYS   H    H  N N 144 
CYS   H2   H  N N 145 
CYS   HA   H  N N 146 
CYS   HB2  H  N N 147 
CYS   HB3  H  N N 148 
CYS   HG   H  N N 149 
CYS   HXT  H  N N 150 
DMS   S    S  N N 151 
DMS   O    O  N N 152 
DMS   C1   C  N N 153 
DMS   C2   C  N N 154 
DMS   H11  H  N N 155 
DMS   H12  H  N N 156 
DMS   H13  H  N N 157 
DMS   H21  H  N N 158 
DMS   H22  H  N N 159 
DMS   H23  H  N N 160 
GLN   N    N  N N 161 
GLN   CA   C  N S 162 
GLN   C    C  N N 163 
GLN   O    O  N N 164 
GLN   CB   C  N N 165 
GLN   CG   C  N N 166 
GLN   CD   C  N N 167 
GLN   OE1  O  N N 168 
GLN   NE2  N  N N 169 
GLN   OXT  O  N N 170 
GLN   H    H  N N 171 
GLN   H2   H  N N 172 
GLN   HA   H  N N 173 
GLN   HB2  H  N N 174 
GLN   HB3  H  N N 175 
GLN   HG2  H  N N 176 
GLN   HG3  H  N N 177 
GLN   HE21 H  N N 178 
GLN   HE22 H  N N 179 
GLN   HXT  H  N N 180 
GLU   N    N  N N 181 
GLU   CA   C  N S 182 
GLU   C    C  N N 183 
GLU   O    O  N N 184 
GLU   CB   C  N N 185 
GLU   CG   C  N N 186 
GLU   CD   C  N N 187 
GLU   OE1  O  N N 188 
GLU   OE2  O  N N 189 
GLU   OXT  O  N N 190 
GLU   H    H  N N 191 
GLU   H2   H  N N 192 
GLU   HA   H  N N 193 
GLU   HB2  H  N N 194 
GLU   HB3  H  N N 195 
GLU   HG2  H  N N 196 
GLU   HG3  H  N N 197 
GLU   HE2  H  N N 198 
GLU   HXT  H  N N 199 
GLY   N    N  N N 200 
GLY   CA   C  N N 201 
GLY   C    C  N N 202 
GLY   O    O  N N 203 
GLY   OXT  O  N N 204 
GLY   H    H  N N 205 
GLY   H2   H  N N 206 
GLY   HA2  H  N N 207 
GLY   HA3  H  N N 208 
GLY   HXT  H  N N 209 
HIS   N    N  N N 210 
HIS   CA   C  N S 211 
HIS   C    C  N N 212 
HIS   O    O  N N 213 
HIS   CB   C  N N 214 
HIS   CG   C  Y N 215 
HIS   ND1  N  Y N 216 
HIS   CD2  C  Y N 217 
HIS   CE1  C  Y N 218 
HIS   NE2  N  Y N 219 
HIS   OXT  O  N N 220 
HIS   H    H  N N 221 
HIS   H2   H  N N 222 
HIS   HA   H  N N 223 
HIS   HB2  H  N N 224 
HIS   HB3  H  N N 225 
HIS   HD1  H  N N 226 
HIS   HD2  H  N N 227 
HIS   HE1  H  N N 228 
HIS   HE2  H  N N 229 
HIS   HXT  H  N N 230 
HOH   O    O  N N 231 
HOH   H1   H  N N 232 
HOH   H2   H  N N 233 
ILE   N    N  N N 234 
ILE   CA   C  N S 235 
ILE   C    C  N N 236 
ILE   O    O  N N 237 
ILE   CB   C  N S 238 
ILE   CG1  C  N N 239 
ILE   CG2  C  N N 240 
ILE   CD1  C  N N 241 
ILE   OXT  O  N N 242 
ILE   H    H  N N 243 
ILE   H2   H  N N 244 
ILE   HA   H  N N 245 
ILE   HB   H  N N 246 
ILE   HG12 H  N N 247 
ILE   HG13 H  N N 248 
ILE   HG21 H  N N 249 
ILE   HG22 H  N N 250 
ILE   HG23 H  N N 251 
ILE   HD11 H  N N 252 
ILE   HD12 H  N N 253 
ILE   HD13 H  N N 254 
ILE   HXT  H  N N 255 
LEU   N    N  N N 256 
LEU   CA   C  N S 257 
LEU   C    C  N N 258 
LEU   O    O  N N 259 
LEU   CB   C  N N 260 
LEU   CG   C  N N 261 
LEU   CD1  C  N N 262 
LEU   CD2  C  N N 263 
LEU   OXT  O  N N 264 
LEU   H    H  N N 265 
LEU   H2   H  N N 266 
LEU   HA   H  N N 267 
LEU   HB2  H  N N 268 
LEU   HB3  H  N N 269 
LEU   HG   H  N N 270 
LEU   HD11 H  N N 271 
LEU   HD12 H  N N 272 
LEU   HD13 H  N N 273 
LEU   HD21 H  N N 274 
LEU   HD22 H  N N 275 
LEU   HD23 H  N N 276 
LEU   HXT  H  N N 277 
LYS   N    N  N N 278 
LYS   CA   C  N S 279 
LYS   C    C  N N 280 
LYS   O    O  N N 281 
LYS   CB   C  N N 282 
LYS   CG   C  N N 283 
LYS   CD   C  N N 284 
LYS   CE   C  N N 285 
LYS   NZ   N  N N 286 
LYS   OXT  O  N N 287 
LYS   H    H  N N 288 
LYS   H2   H  N N 289 
LYS   HA   H  N N 290 
LYS   HB2  H  N N 291 
LYS   HB3  H  N N 292 
LYS   HG2  H  N N 293 
LYS   HG3  H  N N 294 
LYS   HD2  H  N N 295 
LYS   HD3  H  N N 296 
LYS   HE2  H  N N 297 
LYS   HE3  H  N N 298 
LYS   HZ1  H  N N 299 
LYS   HZ2  H  N N 300 
LYS   HZ3  H  N N 301 
LYS   HXT  H  N N 302 
MET   N    N  N N 303 
MET   CA   C  N S 304 
MET   C    C  N N 305 
MET   O    O  N N 306 
MET   CB   C  N N 307 
MET   CG   C  N N 308 
MET   SD   S  N N 309 
MET   CE   C  N N 310 
MET   OXT  O  N N 311 
MET   H    H  N N 312 
MET   H2   H  N N 313 
MET   HA   H  N N 314 
MET   HB2  H  N N 315 
MET   HB3  H  N N 316 
MET   HG2  H  N N 317 
MET   HG3  H  N N 318 
MET   HE1  H  N N 319 
MET   HE2  H  N N 320 
MET   HE3  H  N N 321 
MET   HXT  H  N N 322 
PHE   N    N  N N 323 
PHE   CA   C  N S 324 
PHE   C    C  N N 325 
PHE   O    O  N N 326 
PHE   CB   C  N N 327 
PHE   CG   C  Y N 328 
PHE   CD1  C  Y N 329 
PHE   CD2  C  Y N 330 
PHE   CE1  C  Y N 331 
PHE   CE2  C  Y N 332 
PHE   CZ   C  Y N 333 
PHE   OXT  O  N N 334 
PHE   H    H  N N 335 
PHE   H2   H  N N 336 
PHE   HA   H  N N 337 
PHE   HB2  H  N N 338 
PHE   HB3  H  N N 339 
PHE   HD1  H  N N 340 
PHE   HD2  H  N N 341 
PHE   HE1  H  N N 342 
PHE   HE2  H  N N 343 
PHE   HZ   H  N N 344 
PHE   HXT  H  N N 345 
PRO   N    N  N N 346 
PRO   CA   C  N S 347 
PRO   C    C  N N 348 
PRO   O    O  N N 349 
PRO   CB   C  N N 350 
PRO   CG   C  N N 351 
PRO   CD   C  N N 352 
PRO   OXT  O  N N 353 
PRO   H    H  N N 354 
PRO   HA   H  N N 355 
PRO   HB2  H  N N 356 
PRO   HB3  H  N N 357 
PRO   HG2  H  N N 358 
PRO   HG3  H  N N 359 
PRO   HD2  H  N N 360 
PRO   HD3  H  N N 361 
PRO   HXT  H  N N 362 
SER   N    N  N N 363 
SER   CA   C  N S 364 
SER   C    C  N N 365 
SER   O    O  N N 366 
SER   CB   C  N N 367 
SER   OG   O  N N 368 
SER   OXT  O  N N 369 
SER   H    H  N N 370 
SER   H2   H  N N 371 
SER   HA   H  N N 372 
SER   HB2  H  N N 373 
SER   HB3  H  N N 374 
SER   HG   H  N N 375 
SER   HXT  H  N N 376 
THR   N    N  N N 377 
THR   CA   C  N S 378 
THR   C    C  N N 379 
THR   O    O  N N 380 
THR   CB   C  N R 381 
THR   OG1  O  N N 382 
THR   CG2  C  N N 383 
THR   OXT  O  N N 384 
THR   H    H  N N 385 
THR   H2   H  N N 386 
THR   HA   H  N N 387 
THR   HB   H  N N 388 
THR   HG1  H  N N 389 
THR   HG21 H  N N 390 
THR   HG22 H  N N 391 
THR   HG23 H  N N 392 
THR   HXT  H  N N 393 
TYR   N    N  N N 394 
TYR   CA   C  N S 395 
TYR   C    C  N N 396 
TYR   O    O  N N 397 
TYR   CB   C  N N 398 
TYR   CG   C  Y N 399 
TYR   CD1  C  Y N 400 
TYR   CD2  C  Y N 401 
TYR   CE1  C  Y N 402 
TYR   CE2  C  Y N 403 
TYR   CZ   C  Y N 404 
TYR   OH   O  N N 405 
TYR   OXT  O  N N 406 
TYR   H    H  N N 407 
TYR   H2   H  N N 408 
TYR   HA   H  N N 409 
TYR   HB2  H  N N 410 
TYR   HB3  H  N N 411 
TYR   HD1  H  N N 412 
TYR   HD2  H  N N 413 
TYR   HE1  H  N N 414 
TYR   HE2  H  N N 415 
TYR   HH   H  N N 416 
TYR   HXT  H  N N 417 
VAL   N    N  N N 418 
VAL   CA   C  N S 419 
VAL   C    C  N N 420 
VAL   O    O  N N 421 
VAL   CB   C  N N 422 
VAL   CG1  C  N N 423 
VAL   CG2  C  N N 424 
VAL   OXT  O  N N 425 
VAL   H    H  N N 426 
VAL   H2   H  N N 427 
VAL   HA   H  N N 428 
VAL   HB   H  N N 429 
VAL   HG11 H  N N 430 
VAL   HG12 H  N N 431 
VAL   HG13 H  N N 432 
VAL   HG21 H  N N 433 
VAL   HG22 H  N N 434 
VAL   HG23 H  N N 435 
VAL   HXT  H  N N 436 
# 
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 
A1A56 N1  C1   sing N N 1   
A1A56 O2  C2   sing N N 2   
A1A56 C1  C2   sing N N 3   
A1A56 C1  O1   doub N N 4   
A1A56 C2  C3   sing N N 5   
A1A56 C2  C11  sing N N 6   
A1A56 C3  C4   sing N N 7   
A1A56 C11 N2   sing N N 8   
A1A56 C4  N2   sing N N 9   
A1A56 N2  C5   sing N N 10  
A1A56 C5  N3   doub Y N 11  
A1A56 C5  C8   sing Y N 12  
A1A56 C9  C8   sing Y N 13  
A1A56 C9  C10  doub Y N 14  
A1A56 N3  C6   sing Y N 15  
A1A56 C8  C7   doub Y N 16  
A1A56 C10 N5   sing Y N 17  
A1A56 C6  N4   doub Y N 18  
A1A56 C7  N5   sing Y N 19  
A1A56 C7  N4   sing Y N 20  
A1A56 C3  H4   sing N N 21  
A1A56 C3  H5   sing N N 22  
A1A56 C6  H8   sing N N 23  
A1A56 C9  H9   sing N N 24  
A1A56 C10 H10  sing N N 25  
A1A56 C11 H13  sing N N 26  
A1A56 C11 H12  sing N N 27  
A1A56 C4  H7   sing N N 28  
A1A56 C4  H6   sing N N 29  
A1A56 N1  H2   sing N N 30  
A1A56 N1  H1   sing N N 31  
A1A56 N5  H11  sing N N 32  
A1A56 O2  H3   sing N N 33  
A1A57 C6  N4   doub Y N 34  
A1A57 C6  N3   sing Y N 35  
A1A57 N4  C7   sing Y N 36  
A1A57 N3  C5   doub Y N 37  
A1A57 C7  N5   sing Y N 38  
A1A57 C7  C8   doub Y N 39  
A1A57 N5  C10  sing Y N 40  
A1A57 C5  C8   sing Y N 41  
A1A57 C5  N2   sing N N 42  
A1A57 C4  C3   sing N N 43  
A1A57 C4  N2   sing N N 44  
A1A57 C8  C9   sing Y N 45  
A1A57 C3  C2   sing N N 46  
A1A57 N2  C11  sing N N 47  
A1A57 C10 C9   doub Y N 48  
A1A57 C2  C11  sing N N 49  
A1A57 C2  C1   sing N N 50  
A1A57 C2  O2   sing N N 51  
A1A57 O1  C1   doub N N 52  
A1A57 C1  N1   sing N N 53  
A1A57 C3  H4   sing N N 54  
A1A57 C3  H5   sing N N 55  
A1A57 C4  H6   sing N N 56  
A1A57 C4  H7   sing N N 57  
A1A57 C6  H8   sing N N 58  
A1A57 C10 H10  sing N N 59  
A1A57 C11 H12  sing N N 60  
A1A57 C11 H13  sing N N 61  
A1A57 C9  H9   sing N N 62  
A1A57 N1  H2   sing N N 63  
A1A57 N1  H1   sing N N 64  
A1A57 N5  H11  sing N N 65  
A1A57 O2  H3   sing N N 66  
ALA   N   CA   sing N N 67  
ALA   N   H    sing N N 68  
ALA   N   H2   sing N N 69  
ALA   CA  C    sing N N 70  
ALA   CA  CB   sing N N 71  
ALA   CA  HA   sing N N 72  
ALA   C   O    doub N N 73  
ALA   C   OXT  sing N N 74  
ALA   CB  HB1  sing N N 75  
ALA   CB  HB2  sing N N 76  
ALA   CB  HB3  sing N N 77  
ALA   OXT HXT  sing N N 78  
ARG   N   CA   sing N N 79  
ARG   N   H    sing N N 80  
ARG   N   H2   sing N N 81  
ARG   CA  C    sing N N 82  
ARG   CA  CB   sing N N 83  
ARG   CA  HA   sing N N 84  
ARG   C   O    doub N N 85  
ARG   C   OXT  sing N N 86  
ARG   CB  CG   sing N N 87  
ARG   CB  HB2  sing N N 88  
ARG   CB  HB3  sing N N 89  
ARG   CG  CD   sing N N 90  
ARG   CG  HG2  sing N N 91  
ARG   CG  HG3  sing N N 92  
ARG   CD  NE   sing N N 93  
ARG   CD  HD2  sing N N 94  
ARG   CD  HD3  sing N N 95  
ARG   NE  CZ   sing N N 96  
ARG   NE  HE   sing N N 97  
ARG   CZ  NH1  sing N N 98  
ARG   CZ  NH2  doub N N 99  
ARG   NH1 HH11 sing N N 100 
ARG   NH1 HH12 sing N N 101 
ARG   NH2 HH21 sing N N 102 
ARG   NH2 HH22 sing N N 103 
ARG   OXT HXT  sing N N 104 
ASN   N   CA   sing N N 105 
ASN   N   H    sing N N 106 
ASN   N   H2   sing N N 107 
ASN   CA  C    sing N N 108 
ASN   CA  CB   sing N N 109 
ASN   CA  HA   sing N N 110 
ASN   C   O    doub N N 111 
ASN   C   OXT  sing N N 112 
ASN   CB  CG   sing N N 113 
ASN   CB  HB2  sing N N 114 
ASN   CB  HB3  sing N N 115 
ASN   CG  OD1  doub N N 116 
ASN   CG  ND2  sing N N 117 
ASN   ND2 HD21 sing N N 118 
ASN   ND2 HD22 sing N N 119 
ASN   OXT HXT  sing N N 120 
ASP   N   CA   sing N N 121 
ASP   N   H    sing N N 122 
ASP   N   H2   sing N N 123 
ASP   CA  C    sing N N 124 
ASP   CA  CB   sing N N 125 
ASP   CA  HA   sing N N 126 
ASP   C   O    doub N N 127 
ASP   C   OXT  sing N N 128 
ASP   CB  CG   sing N N 129 
ASP   CB  HB2  sing N N 130 
ASP   CB  HB3  sing N N 131 
ASP   CG  OD1  doub N N 132 
ASP   CG  OD2  sing N N 133 
ASP   OD2 HD2  sing N N 134 
ASP   OXT HXT  sing N N 135 
CYS   N   CA   sing N N 136 
CYS   N   H    sing N N 137 
CYS   N   H2   sing N N 138 
CYS   CA  C    sing N N 139 
CYS   CA  CB   sing N N 140 
CYS   CA  HA   sing N N 141 
CYS   C   O    doub N N 142 
CYS   C   OXT  sing N N 143 
CYS   CB  SG   sing N N 144 
CYS   CB  HB2  sing N N 145 
CYS   CB  HB3  sing N N 146 
CYS   SG  HG   sing N N 147 
CYS   OXT HXT  sing N N 148 
DMS   S   O    doub N N 149 
DMS   S   C1   sing N N 150 
DMS   S   C2   sing N N 151 
DMS   C1  H11  sing N N 152 
DMS   C1  H12  sing N N 153 
DMS   C1  H13  sing N N 154 
DMS   C2  H21  sing N N 155 
DMS   C2  H22  sing N N 156 
DMS   C2  H23  sing N N 157 
GLN   N   CA   sing N N 158 
GLN   N   H    sing N N 159 
GLN   N   H2   sing N N 160 
GLN   CA  C    sing N N 161 
GLN   CA  CB   sing N N 162 
GLN   CA  HA   sing N N 163 
GLN   C   O    doub N N 164 
GLN   C   OXT  sing N N 165 
GLN   CB  CG   sing N N 166 
GLN   CB  HB2  sing N N 167 
GLN   CB  HB3  sing N N 168 
GLN   CG  CD   sing N N 169 
GLN   CG  HG2  sing N N 170 
GLN   CG  HG3  sing N N 171 
GLN   CD  OE1  doub N N 172 
GLN   CD  NE2  sing N N 173 
GLN   NE2 HE21 sing N N 174 
GLN   NE2 HE22 sing N N 175 
GLN   OXT HXT  sing N N 176 
GLU   N   CA   sing N N 177 
GLU   N   H    sing N N 178 
GLU   N   H2   sing N N 179 
GLU   CA  C    sing N N 180 
GLU   CA  CB   sing N N 181 
GLU   CA  HA   sing N N 182 
GLU   C   O    doub N N 183 
GLU   C   OXT  sing N N 184 
GLU   CB  CG   sing N N 185 
GLU   CB  HB2  sing N N 186 
GLU   CB  HB3  sing N N 187 
GLU   CG  CD   sing N N 188 
GLU   CG  HG2  sing N N 189 
GLU   CG  HG3  sing N N 190 
GLU   CD  OE1  doub N N 191 
GLU   CD  OE2  sing N N 192 
GLU   OE2 HE2  sing N N 193 
GLU   OXT HXT  sing N N 194 
GLY   N   CA   sing N N 195 
GLY   N   H    sing N N 196 
GLY   N   H2   sing N N 197 
GLY   CA  C    sing N N 198 
GLY   CA  HA2  sing N N 199 
GLY   CA  HA3  sing N N 200 
GLY   C   O    doub N N 201 
GLY   C   OXT  sing N N 202 
GLY   OXT HXT  sing N N 203 
HIS   N   CA   sing N N 204 
HIS   N   H    sing N N 205 
HIS   N   H2   sing N N 206 
HIS   CA  C    sing N N 207 
HIS   CA  CB   sing N N 208 
HIS   CA  HA   sing N N 209 
HIS   C   O    doub N N 210 
HIS   C   OXT  sing N N 211 
HIS   CB  CG   sing N N 212 
HIS   CB  HB2  sing N N 213 
HIS   CB  HB3  sing N N 214 
HIS   CG  ND1  sing Y N 215 
HIS   CG  CD2  doub Y N 216 
HIS   ND1 CE1  doub Y N 217 
HIS   ND1 HD1  sing N N 218 
HIS   CD2 NE2  sing Y N 219 
HIS   CD2 HD2  sing N N 220 
HIS   CE1 NE2  sing Y N 221 
HIS   CE1 HE1  sing N N 222 
HIS   NE2 HE2  sing N N 223 
HIS   OXT HXT  sing N N 224 
HOH   O   H1   sing N N 225 
HOH   O   H2   sing N N 226 
ILE   N   CA   sing N N 227 
ILE   N   H    sing N N 228 
ILE   N   H2   sing N N 229 
ILE   CA  C    sing N N 230 
ILE   CA  CB   sing N N 231 
ILE   CA  HA   sing N N 232 
ILE   C   O    doub N N 233 
ILE   C   OXT  sing N N 234 
ILE   CB  CG1  sing N N 235 
ILE   CB  CG2  sing N N 236 
ILE   CB  HB   sing N N 237 
ILE   CG1 CD1  sing N N 238 
ILE   CG1 HG12 sing N N 239 
ILE   CG1 HG13 sing N N 240 
ILE   CG2 HG21 sing N N 241 
ILE   CG2 HG22 sing N N 242 
ILE   CG2 HG23 sing N N 243 
ILE   CD1 HD11 sing N N 244 
ILE   CD1 HD12 sing N N 245 
ILE   CD1 HD13 sing N N 246 
ILE   OXT HXT  sing N N 247 
LEU   N   CA   sing N N 248 
LEU   N   H    sing N N 249 
LEU   N   H2   sing N N 250 
LEU   CA  C    sing N N 251 
LEU   CA  CB   sing N N 252 
LEU   CA  HA   sing N N 253 
LEU   C   O    doub N N 254 
LEU   C   OXT  sing N N 255 
LEU   CB  CG   sing N N 256 
LEU   CB  HB2  sing N N 257 
LEU   CB  HB3  sing N N 258 
LEU   CG  CD1  sing N N 259 
LEU   CG  CD2  sing N N 260 
LEU   CG  HG   sing N N 261 
LEU   CD1 HD11 sing N N 262 
LEU   CD1 HD12 sing N N 263 
LEU   CD1 HD13 sing N N 264 
LEU   CD2 HD21 sing N N 265 
LEU   CD2 HD22 sing N N 266 
LEU   CD2 HD23 sing N N 267 
LEU   OXT HXT  sing N N 268 
LYS   N   CA   sing N N 269 
LYS   N   H    sing N N 270 
LYS   N   H2   sing N N 271 
LYS   CA  C    sing N N 272 
LYS   CA  CB   sing N N 273 
LYS   CA  HA   sing N N 274 
LYS   C   O    doub N N 275 
LYS   C   OXT  sing N N 276 
LYS   CB  CG   sing N N 277 
LYS   CB  HB2  sing N N 278 
LYS   CB  HB3  sing N N 279 
LYS   CG  CD   sing N N 280 
LYS   CG  HG2  sing N N 281 
LYS   CG  HG3  sing N N 282 
LYS   CD  CE   sing N N 283 
LYS   CD  HD2  sing N N 284 
LYS   CD  HD3  sing N N 285 
LYS   CE  NZ   sing N N 286 
LYS   CE  HE2  sing N N 287 
LYS   CE  HE3  sing N N 288 
LYS   NZ  HZ1  sing N N 289 
LYS   NZ  HZ2  sing N N 290 
LYS   NZ  HZ3  sing N N 291 
LYS   OXT HXT  sing N N 292 
MET   N   CA   sing N N 293 
MET   N   H    sing N N 294 
MET   N   H2   sing N N 295 
MET   CA  C    sing N N 296 
MET   CA  CB   sing N N 297 
MET   CA  HA   sing N N 298 
MET   C   O    doub N N 299 
MET   C   OXT  sing N N 300 
MET   CB  CG   sing N N 301 
MET   CB  HB2  sing N N 302 
MET   CB  HB3  sing N N 303 
MET   CG  SD   sing N N 304 
MET   CG  HG2  sing N N 305 
MET   CG  HG3  sing N N 306 
MET   SD  CE   sing N N 307 
MET   CE  HE1  sing N N 308 
MET   CE  HE2  sing N N 309 
MET   CE  HE3  sing N N 310 
MET   OXT HXT  sing N N 311 
PHE   N   CA   sing N N 312 
PHE   N   H    sing N N 313 
PHE   N   H2   sing N N 314 
PHE   CA  C    sing N N 315 
PHE   CA  CB   sing N N 316 
PHE   CA  HA   sing N N 317 
PHE   C   O    doub N N 318 
PHE   C   OXT  sing N N 319 
PHE   CB  CG   sing N N 320 
PHE   CB  HB2  sing N N 321 
PHE   CB  HB3  sing N N 322 
PHE   CG  CD1  doub Y N 323 
PHE   CG  CD2  sing Y N 324 
PHE   CD1 CE1  sing Y N 325 
PHE   CD1 HD1  sing N N 326 
PHE   CD2 CE2  doub Y N 327 
PHE   CD2 HD2  sing N N 328 
PHE   CE1 CZ   doub Y N 329 
PHE   CE1 HE1  sing N N 330 
PHE   CE2 CZ   sing Y N 331 
PHE   CE2 HE2  sing N N 332 
PHE   CZ  HZ   sing N N 333 
PHE   OXT HXT  sing N N 334 
PRO   N   CA   sing N N 335 
PRO   N   CD   sing N N 336 
PRO   N   H    sing N N 337 
PRO   CA  C    sing N N 338 
PRO   CA  CB   sing N N 339 
PRO   CA  HA   sing N N 340 
PRO   C   O    doub N N 341 
PRO   C   OXT  sing N N 342 
PRO   CB  CG   sing N N 343 
PRO   CB  HB2  sing N N 344 
PRO   CB  HB3  sing N N 345 
PRO   CG  CD   sing N N 346 
PRO   CG  HG2  sing N N 347 
PRO   CG  HG3  sing N N 348 
PRO   CD  HD2  sing N N 349 
PRO   CD  HD3  sing N N 350 
PRO   OXT HXT  sing N N 351 
SER   N   CA   sing N N 352 
SER   N   H    sing N N 353 
SER   N   H2   sing N N 354 
SER   CA  C    sing N N 355 
SER   CA  CB   sing N N 356 
SER   CA  HA   sing N N 357 
SER   C   O    doub N N 358 
SER   C   OXT  sing N N 359 
SER   CB  OG   sing N N 360 
SER   CB  HB2  sing N N 361 
SER   CB  HB3  sing N N 362 
SER   OG  HG   sing N N 363 
SER   OXT HXT  sing N N 364 
THR   N   CA   sing N N 365 
THR   N   H    sing N N 366 
THR   N   H2   sing N N 367 
THR   CA  C    sing N N 368 
THR   CA  CB   sing N N 369 
THR   CA  HA   sing N N 370 
THR   C   O    doub N N 371 
THR   C   OXT  sing N N 372 
THR   CB  OG1  sing N N 373 
THR   CB  CG2  sing N N 374 
THR   CB  HB   sing N N 375 
THR   OG1 HG1  sing N N 376 
THR   CG2 HG21 sing N N 377 
THR   CG2 HG22 sing N N 378 
THR   CG2 HG23 sing N N 379 
THR   OXT HXT  sing N N 380 
TYR   N   CA   sing N N 381 
TYR   N   H    sing N N 382 
TYR   N   H2   sing N N 383 
TYR   CA  C    sing N N 384 
TYR   CA  CB   sing N N 385 
TYR   CA  HA   sing N N 386 
TYR   C   O    doub N N 387 
TYR   C   OXT  sing N N 388 
TYR   CB  CG   sing N N 389 
TYR   CB  HB2  sing N N 390 
TYR   CB  HB3  sing N N 391 
TYR   CG  CD1  doub Y N 392 
TYR   CG  CD2  sing Y N 393 
TYR   CD1 CE1  sing Y N 394 
TYR   CD1 HD1  sing N N 395 
TYR   CD2 CE2  doub Y N 396 
TYR   CD2 HD2  sing N N 397 
TYR   CE1 CZ   doub Y N 398 
TYR   CE1 HE1  sing N N 399 
TYR   CE2 CZ   sing Y N 400 
TYR   CE2 HE2  sing N N 401 
TYR   CZ  OH   sing N N 402 
TYR   OH  HH   sing N N 403 
TYR   OXT HXT  sing N N 404 
VAL   N   CA   sing N N 405 
VAL   N   H    sing N N 406 
VAL   N   H2   sing N N 407 
VAL   CA  C    sing N N 408 
VAL   CA  CB   sing N N 409 
VAL   CA  HA   sing N N 410 
VAL   C   O    doub N N 411 
VAL   C   OXT  sing N N 412 
VAL   CB  CG1  sing N N 413 
VAL   CB  CG2  sing N N 414 
VAL   CB  HB   sing N N 415 
VAL   CG1 HG11 sing N N 416 
VAL   CG1 HG12 sing N N 417 
VAL   CG1 HG13 sing N N 418 
VAL   CG2 HG21 sing N N 419 
VAL   CG2 HG22 sing N N 420 
VAL   CG2 HG23 sing N N 421 
VAL   OXT HXT  sing N N 422 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           U19AI171110 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_deposit_group.group_title         
'PanDDA analysis group deposition of SARS-CoV-2 NSP3 macrodomain ligand screen - FrankenROCS hits and analogues of AVI-313' 
_pdbx_deposit_group.group_description   
'SARS-CoV-2 NSP3 macrodomain in complex with ligands identified by X-ray diffraction using ALS 8.3.1,  SSRL 9-2, and SSRL 12-2' 
_pdbx_deposit_group.group_type          'changed state' 
_pdbx_deposit_group.group_id            G_1002304 
# 
_atom_sites.entry_id                    7HCR 
_atom_sites.fract_transf_matrix[1][1]   0.011272 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.011272 
_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]   0.025372 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
# 
loop_
_atom_type.symbol 
C  
CL 
H  
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    A VAL   A 1 3   ? 19.629 -16.205 22.239  0.56 59.99 ?  3   VAL   A N    1 
ATOM   2    N  N    B VAL   A 1 3   ? 19.630 -15.815 22.368  0.44 58.46 ?  3   VAL   A N    1 
ATOM   3    C  CA   A VAL   A 1 3   ? 18.654 -15.132 22.393  0.56 59.50 ?  3   VAL   A CA   1 
ATOM   4    C  CA   B VAL   A 1 3   ? 18.607 -14.791 22.539  0.44 57.94 ?  3   VAL   A CA   1 
ATOM   5    C  C    A VAL   A 1 3   ? 19.305 -13.783 22.110  0.56 57.53 ?  3   VAL   A C    1 
ATOM   6    C  C    B VAL   A 1 3   ? 19.193 -13.412 22.256  0.44 55.81 ?  3   VAL   A C    1 
ATOM   7    O  O    A VAL   A 1 3   ? 20.418 -13.515 22.565  0.56 58.12 ?  3   VAL   A O    1 
ATOM   8    O  O    B VAL   A 1 3   ? 20.263 -13.070 22.761  0.44 56.39 ?  3   VAL   A O    1 
ATOM   9    C  CB   A VAL   A 1 3   ? 18.003 -15.163 23.792  0.56 60.53 ?  3   VAL   A CB   1 
ATOM   10   C  CB   B VAL   A 1 3   ? 17.981 -14.856 23.947  0.44 59.07 ?  3   VAL   A CB   1 
ATOM   11   C  CG1  A VAL   A 1 3   ? 16.969 -14.053 23.928  0.56 60.92 ?  3   VAL   A CG1  1 
ATOM   12   C  CG1  B VAL   A 1 3   ? 16.889 -13.806 24.092  0.44 59.49 ?  3   VAL   A CG1  1 
ATOM   13   C  CG2  A VAL   A 1 3   ? 17.366 -16.521 24.052  0.56 60.86 ?  3   VAL   A CG2  1 
ATOM   14   C  CG2  B VAL   A 1 3   ? 17.431 -16.250 24.223  0.44 59.44 ?  3   VAL   A CG2  1 
ATOM   15   H  HA   A VAL   A 1 3   ? 17.949 -15.256 21.743  0.56 71.42 ?  3   VAL   A HA   1 
ATOM   16   H  HA   B VAL   A 1 3   ? 17.897 -14.948 21.900  0.44 69.55 ?  3   VAL   A HA   1 
ATOM   17   H  HB   A VAL   A 1 3   ? 18.685 -15.019 24.467  0.56 72.66 ?  3   VAL   A HB   1 
ATOM   18   H  HB   B VAL   A 1 3   ? 18.665 -14.668 24.608  0.44 70.91 ?  3   VAL   A HB   1 
ATOM   19   H  HG11 A VAL   A 1 3   ? 16.456 -14.197 24.739  0.56 73.12 ?  3   VAL   A HG11 1 
ATOM   20   H  HG11 B VAL   A 1 3   ? 16.398 -13.974 24.911  0.44 71.41 ?  3   VAL   A HG11 1 
ATOM   21   H  HG12 A VAL   A 1 3   ? 17.425 -13.198 23.974  0.56 73.12 ?  3   VAL   A HG12 1 
ATOM   22   H  HG12 B VAL   A 1 3   ? 17.296 -12.926 24.126  0.44 71.41 ?  3   VAL   A HG12 1 
ATOM   23   H  HG13 A VAL   A 1 3   ? 16.380 -14.075 23.157  0.56 73.12 ?  3   VAL   A HG13 1 
ATOM   24   H  HG13 B VAL   A 1 3   ? 16.291 -13.866 23.331  0.44 71.41 ?  3   VAL   A HG13 1 
ATOM   25   H  HG21 A VAL   A 1 3   ? 16.900 -16.495 24.902  0.56 73.06 ?  3   VAL   A HG21 1 
ATOM   26   H  HG21 B VAL   A 1 3   ? 16.970 -16.245 25.077  0.44 71.35 ?  3   VAL   A HG21 1 
ATOM   27   H  HG22 A VAL   A 1 3   ? 16.740 -16.717 23.337  0.56 73.06 ?  3   VAL   A HG22 1 
ATOM   28   H  HG22 B VAL   A 1 3   ? 16.813 -16.491 23.515  0.44 71.35 ?  3   VAL   A HG22 1 
ATOM   29   H  HG23 A VAL   A 1 3   ? 18.062 -17.196 24.077  0.56 73.06 ?  3   VAL   A HG23 1 
ATOM   30   H  HG23 B VAL   A 1 3   ? 18.167 -16.881 24.249  0.44 71.35 ?  3   VAL   A HG23 1 
ATOM   31   N  N    A ASN   A 1 4   ? 18.612 -12.940 21.346  0.56 54.49 ?  4   ASN   A N    1 
ATOM   32   N  N    B ASN   A 1 4   ? 18.487 -12.624 21.443  0.44 52.66 ?  4   ASN   A N    1 
ATOM   33   C  CA   A ASN   A 1 4   ? 19.059 -11.582 21.062  0.56 51.15 ?  4   ASN   A CA   1 
ATOM   34   C  CA   B ASN   A 1 4   ? 18.916 -11.263 21.138  0.44 49.22 ?  4   ASN   A CA   1 
ATOM   35   C  C    A ASN   A 1 4   ? 17.904 -10.612 21.301  0.56 47.99 ?  4   ASN   A C    1 
ATOM   36   C  C    B ASN   A 1 4   ? 17.793 -10.266 21.401  0.44 45.92 ?  4   ASN   A C    1 
ATOM   37   O  O    A ASN   A 1 4   ? 16.791 -11.012 21.657  0.56 48.08 ?  4   ASN   A O    1 
ATOM   38   O  O    B ASN   A 1 4   ? 16.735 -10.638 21.921  0.44 45.95 ?  4   ASN   A O    1 
ATOM   39   C  CB   A ASN   A 1 4   ? 19.643 -11.460 19.647  0.56 50.73 ?  4   ASN   A CB   1 
ATOM   40   C  CB   B ASN   A 1 4   ? 19.439 -11.153 19.702  0.44 48.87 ?  4   ASN   A CB   1 
ATOM   41   C  CG   A ASN   A 1 4   ? 18.672 -11.897 18.570  0.56 50.30 ?  4   ASN   A CG   1 
ATOM   42   C  CG   B ASN   A 1 4   ? 18.432 -11.612 18.670  0.44 48.51 ?  4   ASN   A CG   1 
ATOM   43   O  OD1  A ASN   A 1 4   ? 17.508 -11.499 18.566  0.56 50.11 ?  4   ASN   A OD1  1 
ATOM   44   O  OD1  B ASN   A 1 4   ? 17.264 -11.224 18.705  0.44 48.36 ?  4   ASN   A OD1  1 
ATOM   45   N  ND2  A ASN   A 1 4   ? 19.151 -12.726 17.647  0.56 50.14 ?  4   ASN   A ND2  1 
ATOM   46   N  ND2  B ASN   A 1 4   ? 18.883 -12.447 17.740  0.44 48.38 ?  4   ASN   A ND2  1 
ATOM   47   H  H    A ASN   A 1 4   ? 17.861 -13.141 20.974  0.56 65.41 ?  4   ASN   A H    1 
ATOM   48   H  H    B ASN   A 1 4   ? 17.752 -12.858 21.063  0.44 63.21 ?  4   ASN   A H    1 
ATOM   49   H  HA   A ASN   A 1 4   ? 19.766 -11.358 21.682  0.56 61.40 ?  4   ASN   A HA   1 
ATOM   50   H  HA   B ASN   A 1 4   ? 19.652 -11.038 21.721  0.44 59.09 ?  4   ASN   A HA   1 
ATOM   51   H  HB2  A ASN   A 1 4   ? 19.879 -10.532 19.482  0.56 60.90 ?  4   ASN   A HB2  1 
ATOM   52   H  HB2  B ASN   A 1 4   ? 19.663 -10.226 19.514  0.44 58.66 ?  4   ASN   A HB2  1 
ATOM   53   H  HB3  A ASN   A 1 4   ? 20.434 -12.017 19.583  0.56 60.90 ?  4   ASN   A HB3  1 
ATOM   54   H  HB3  B ASN   A 1 4   ? 20.230 -11.705 19.613  0.44 58.66 ?  4   ASN   A HB3  1 
ATOM   55   H  HD21 A ASN   A 1 4   ? 18.642 -13.003 17.012  0.56 60.19 ?  4   ASN   A HD21 1 
ATOM   56   H  HD21 B ASN   A 1 4   ? 18.355 -12.737 17.127  0.44 58.08 ?  4   ASN   A HD21 1 
ATOM   57   H  HD22 A ASN   A 1 4   ? 19.971 -12.985 17.685  0.56 60.19 ?  4   ASN   A HD22 1 
ATOM   58   H  HD22 B ASN   A 1 4   ? 19.707 -12.699 17.751  0.44 58.08 ?  4   ASN   A HD22 1 
ATOM   59   N  N    A SER   A 1 5   ? 18.175 -9.323  21.096  0.56 44.52 ?  5   SER   A N    1 
ATOM   60   N  N    B SER   A 1 5   ? 18.010 -9.000  21.044  0.44 42.44 ?  5   SER   A N    1 
ATOM   61   C  CA   A SER   A 1 5   ? 17.256 -8.255  21.471  0.56 40.96 ?  5   SER   A CA   1 
ATOM   62   C  CA   B SER   A 1 5   ? 17.109 -7.916  21.413  0.44 38.91 ?  5   SER   A CA   1 
ATOM   63   C  C    A SER   A 1 5   ? 16.410 -7.748  20.308  0.56 36.47 ?  5   SER   A C    1 
ATOM   64   C  C    B SER   A 1 5   ? 16.240 -7.428  20.257  0.44 34.54 ?  5   SER   A C    1 
ATOM   65   O  O    A SER   A 1 5   ? 15.771 -6.699  20.435  0.56 36.59 ?  5   SER   A O    1 
ATOM   66   O  O    B SER   A 1 5   ? 15.594 -6.383  20.384  0.44 34.45 ?  5   SER   A O    1 
ATOM   67   C  CB   A SER   A 1 5   ? 18.026 -7.093  22.103  0.56 41.73 ?  5   SER   A CB   1 
ATOM   68   C  CB   B SER   A 1 5   ? 17.893 -6.747  22.014  0.44 39.61 ?  5   SER   A CB   1 
ATOM   69   O  OG   A SER   A 1 5   ? 19.053 -6.633  21.243  0.56 42.26 ?  5   SER   A OG   1 
ATOM   70   O  OG   B SER   A 1 5   ? 18.765 -6.167  21.061  0.44 40.07 ?  5   SER   A OG   1 
ATOM   71   H  H    A SER   A 1 5   ? 18.897 -9.042  20.729  0.56 53.44 ?  5   SER   A H    1 
ATOM   72   H  H    B SER   A 1 5   ? 18.684 -8.750  20.575  0.44 50.95 ?  5   SER   A H    1 
ATOM   73   H  HA   A SER   A 1 5   ? 16.653 -8.598  22.148  0.56 49.17 ?  5   SER   A HA   1 
ATOM   74   H  HA   B SER   A 1 5   ? 16.514 -8.242  22.102  0.44 46.71 ?  5   SER   A HA   1 
ATOM   75   H  HB2  A SER   A 1 5   ? 17.408 -6.363  22.275  0.56 50.10 ?  5   SER   A HB2  1 
ATOM   76   H  HB2  B SER   A 1 5   ? 17.265 -6.074  22.321  0.44 47.55 ?  5   SER   A HB2  1 
ATOM   77   H  HB3  A SER   A 1 5   ? 18.422 -7.392  22.937  0.56 50.10 ?  5   SER   A HB3  1 
ATOM   78   H  HB3  B SER   A 1 5   ? 18.419 -7.072  22.762  0.44 47.55 ?  5   SER   A HB3  1 
ATOM   79   H  HG   A SER   A 1 5   ? 19.465 -5.995  21.604  0.56 50.74 ?  5   SER   A HG   1 
ATOM   80   H  HG   B SER   A 1 5   ? 19.182 -5.524  21.408  0.44 48.11 ?  5   SER   A HG   1 
ATOM   81   N  N    A PHE   A 1 6   ? 16.390 -8.457  19.181  0.56 31.76 ?  6   PHE   A N    1 
ATOM   82   N  N    B PHE   A 1 6   ? 16.205 -8.150  19.140  0.44 30.17 ?  6   PHE   A N    1 
ATOM   83   C  CA   A PHE   A 1 6   ? 15.498 -8.088  18.089  0.56 27.40 ?  6   PHE   A CA   1 
ATOM   84   C  CA   B PHE   A 1 6   ? 15.265 -7.817  18.079  0.44 26.29 ?  6   PHE   A CA   1 
ATOM   85   C  C    A PHE   A 1 6   ? 14.060 -8.436  18.460  0.56 26.40 ?  6   PHE   A C    1 
ATOM   86   C  C    B PHE   A 1 6   ? 13.862 -8.238  18.499  0.44 25.69 ?  6   PHE   A C    1 
ATOM   87   O  O    A PHE   A 1 6   ? 13.784 -9.539  18.940  0.56 27.51 ?  6   PHE   A O    1 
ATOM   88   O  O    B PHE   A 1 6   ? 13.677 -9.282  19.128  0.44 26.52 ?  6   PHE   A O    1 
ATOM   89   C  CB   A PHE   A 1 6   ? 15.902 -8.818  16.811  0.56 24.63 ?  6   PHE   A CB   1 
ATOM   90   C  CB   B PHE   A 1 6   ? 15.653 -8.532  16.788  0.44 23.67 ?  6   PHE   A CB   1 
ATOM   91   C  CG   A PHE   A 1 6   ? 17.179 -8.308  16.197  0.56 22.72 ?  6   PHE   A CG   1 
ATOM   92   C  CG   B PHE   A 1 6   ? 16.963 -8.073  16.209  0.44 22.01 ?  6   PHE   A CG   1 
ATOM   93   C  CD1  A PHE   A 1 6   ? 17.191 -7.132  15.465  0.56 21.78 ?  6   PHE   A CD1  1 
ATOM   94   C  CD1  B PHE   A 1 6   ? 17.038 -6.905  15.468  0.44 21.23 ?  6   PHE   A CD1  1 
ATOM   95   C  CD2  A PHE   A 1 6   ? 18.363 -9.011  16.343  0.56 22.69 ?  6   PHE   A CD2  1 
ATOM   96   C  CD2  B PHE   A 1 6   ? 18.115 -8.815  16.398  0.44 22.09 ?  6   PHE   A CD2  1 
ATOM   97   C  CE1  A PHE   A 1 6   ? 18.361 -6.662  14.896  0.56 21.51 ?  6   PHE   A CE1  1 
ATOM   98   C  CE1  B PHE   A 1 6   ? 18.240 -6.482  14.933  0.44 21.02 ?  6   PHE   A CE1  1 
ATOM   99   C  CE2  A PHE   A 1 6   ? 19.536 -8.548  15.775  0.56 22.62 ?  6   PHE   A CE2  1 
ATOM   100  C  CE2  B PHE   A 1 6   ? 19.319 -8.400  15.864  0.44 22.08 ?  6   PHE   A CE2  1 
ATOM   101  C  CZ   A PHE   A 1 6   ? 19.535 -7.370  15.051  0.56 21.94 ?  6   PHE   A CZ   1 
ATOM   102  C  CZ   B PHE   A 1 6   ? 19.381 -7.231  15.130  0.44 21.55 ?  6   PHE   A CZ   1 
ATOM   103  H  H    A PHE   A 1 6   ? 16.880 -9.147  19.026  0.56 38.13 ?  6   PHE   A H    1 
ATOM   104  H  H    B PHE   A 1 6   ? 16.703 -8.833  18.976  0.44 36.23 ?  6   PHE   A H    1 
ATOM   105  H  HA   A PHE   A 1 6   ? 15.553 -7.136  17.935  0.56 32.91 ?  6   PHE   A HA   1 
ATOM   106  H  HA   B PHE   A 1 6   ? 15.269 -6.863  17.923  0.44 31.57 ?  6   PHE   A HA   1 
ATOM   107  H  HB2  A PHE   A 1 6   ? 16.023 -9.760  17.014  0.56 29.58 ?  6   PHE   A HB2  1 
ATOM   108  H  HB2  B PHE   A 1 6   ? 15.725 -9.483  16.966  0.44 28.43 ?  6   PHE   A HB2  1 
ATOM   109  H  HB3  A PHE   A 1 6   ? 15.194 -8.714  16.156  0.56 29.58 ?  6   PHE   A HB3  1 
ATOM   110  H  HB3  B PHE   A 1 6   ? 14.964 -8.374  16.124  0.44 28.43 ?  6   PHE   A HB3  1 
ATOM   111  H  HD1  A PHE   A 1 6   ? 16.403 -6.653  15.357  0.56 26.16 ?  6   PHE   A HD1  1 
ATOM   112  H  HD1  B PHE   A 1 6   ? 16.269 -6.397  15.332  0.44 25.50 ?  6   PHE   A HD1  1 
ATOM   113  H  HD2  A PHE   A 1 6   ? 18.369 -9.804  16.832  0.56 27.25 ?  6   PHE   A HD2  1 
ATOM   114  H  HD2  B PHE   A 1 6   ? 18.078 -9.602  16.893  0.44 26.52 ?  6   PHE   A HD2  1 
ATOM   115  H  HE1  A PHE   A 1 6   ? 18.357 -5.871  14.407  0.56 25.83 ?  6   PHE   A HE1  1 
ATOM   116  H  HE1  B PHE   A 1 6   ? 18.279 -5.695  14.437  0.44 25.24 ?  6   PHE   A HE1  1 
ATOM   117  H  HE2  A PHE   A 1 6   ? 20.328 -9.027  15.884  0.56 27.17 ?  6   PHE   A HE2  1 
ATOM   118  H  HE2  B PHE   A 1 6   ? 20.088 -8.905  16.000  0.44 26.52 ?  6   PHE   A HE2  1 
ATOM   119  H  HZ   A PHE   A 1 6   ? 20.323 -7.056  14.669  0.56 26.35 ?  6   PHE   A HZ   1 
ATOM   120  H  HZ   B PHE   A 1 6   ? 20.190 -6.948  14.771  0.44 25.88 ?  6   PHE   A HZ   1 
ATOM   121  N  N    A SER   A 1 7   ? 13.141 -7.497  18.229  0.56 24.71 ?  7   SER   A N    1 
ATOM   122  N  N    B SER   A 1 7   ? 12.867 -7.419  18.160  0.44 24.42 ?  7   SER   A N    1 
ATOM   123  C  CA   A SER   A 1 7   ? 11.767 -7.609  18.703  0.56 23.89 ?  7   SER   A CA   1 
ATOM   124  C  CA   B SER   A 1 7   ? 11.504 -7.670  18.608  0.44 23.64 ?  7   SER   A CA   1 
ATOM   125  C  C    A SER   A 1 7   ? 10.784 -7.399  17.560  0.56 22.07 ?  7   SER   A C    1 
ATOM   126  C  C    B SER   A 1 7   ? 10.506 -7.339  17.509  0.44 21.26 ?  7   SER   A C    1 
ATOM   127  O  O    A SER   A 1 7   ? 11.029 -6.598  16.652  0.56 21.89 ?  7   SER   A O    1 
ATOM   128  O  O    B SER   A 1 7   ? 10.649 -6.336  16.805  0.44 21.31 ?  7   SER   A O    1 
ATOM   129  C  CB   A SER   A 1 7   ? 11.489 -6.568  19.799  0.56 24.79 ?  7   SER   A CB   1 
ATOM   130  C  CB   B SER   A 1 7   ? 11.186 -6.845  19.860  0.44 25.42 ?  7   SER   A CB   1 
ATOM   131  O  OG   A SER   A 1 7   ? 10.115 -6.550  20.151  0.56 25.76 ?  7   SER   A OG   1 
ATOM   132  O  OG   B SER   A 1 7   ? 10.535 -7.635  20.838  0.44 26.73 ?  7   SER   A OG   1 
ATOM   133  H  H    A SER   A 1 7   ? 13.295 -6.778  17.786  0.56 29.67 ?  7   SER   A H    1 
ATOM   134  H  H    B SER   A 1 7   ? 12.959 -6.712  17.676  0.44 29.32 ?  7   SER   A H    1 
ATOM   135  H  HA   A SER   A 1 7   ? 11.622 -8.493  19.076  0.56 28.70 ?  7   SER   A HA   1 
ATOM   136  H  HA   B SER   A 1 7   ? 11.411 -8.609  18.829  0.44 28.40 ?  7   SER   A HA   1 
ATOM   137  H  HB2  A SER   A 1 7   ? 12.006 -6.797  20.588  0.56 29.77 ?  7   SER   A HB2  1 
ATOM   138  H  HB2  B SER   A 1 7   ? 12.014 -6.501  20.229  0.44 30.53 ?  7   SER   A HB2  1 
ATOM   139  H  HB3  A SER   A 1 7   ? 11.754 -5.693  19.475  0.56 29.77 ?  7   SER   A HB3  1 
ATOM   140  H  HB3  B SER   A 1 7   ? 10.602 -6.114  19.612  0.44 30.53 ?  7   SER   A HB3  1 
ATOM   141  H  HG   A SER   A 1 7   ? 9.980  -5.966  20.740  0.56 30.94 ?  7   SER   A HG   1 
ATOM   142  H  HG   B SER   A 1 7   ? 9.823  -7.950  20.527  0.44 32.09 ?  7   SER   A HG   1 
ATOM   143  N  N    A GLY   A 1 8   ? 9.669  -8.128  17.611  0.56 20.91 ?  8   GLY   A N    1 
ATOM   144  N  N    B GLY   A 1 8   ? 9.488  -8.188  17.371  0.44 19.25 ?  8   GLY   A N    1 
ATOM   145  C  CA   A GLY   A 1 8   ? 8.575  -7.897  16.690  0.56 19.52 ?  8   GLY   A CA   1 
ATOM   146  C  CA   B GLY   A 1 8   ? 8.429  -7.950  16.412  0.44 17.75 ?  8   GLY   A CA   1 
ATOM   147  C  C    A GLY   A 1 8   ? 8.794  -8.379  15.275  0.56 17.77 ?  8   GLY   A C    1 
ATOM   148  C  C    B GLY   A 1 8   ? 8.658  -8.524  15.033  0.44 16.04 ?  8   GLY   A C    1 
ATOM   149  O  O    A GLY   A 1 8   ? 8.075  -7.947  14.371  0.56 18.57 ?  8   GLY   A O    1 
ATOM   150  O  O    B GLY   A 1 8   ? 7.919  -8.172  14.105  0.44 16.23 ?  8   GLY   A O    1 
ATOM   151  H  H    A GLY   A 1 8   ? 9.528  -8.764  18.174  0.56 25.12 ?  8   GLY   A H    1 
ATOM   152  H  H    B GLY   A 1 8   ? 9.395  -8.918  17.827  0.44 23.12 ?  8   GLY   A H    1 
ATOM   153  H  HA2  A GLY   A 1 8   ? 7.781  -8.332  17.036  0.56 23.45 ?  8   GLY   A HA2  1 
ATOM   154  H  HA2  B GLY   A 1 8   ? 7.605  -8.322  16.754  0.44 21.32 ?  8   GLY   A HA2  1 
ATOM   155  H  HA3  A GLY   A 1 8   ? 8.400  -6.945  16.648  0.56 23.45 ?  8   GLY   A HA3  1 
ATOM   156  H  HA3  B GLY   A 1 8   ? 8.310  -6.990  16.317  0.44 21.32 ?  8   GLY   A HA3  1 
ATOM   157  N  N    A TYR   A 1 9   ? 9.766  -9.259  15.046  0.56 16.06 ?  9   TYR   A N    1 
ATOM   158  N  N    B TYR   A 1 9   ? 9.640  -9.407  14.868  0.44 14.91 ?  9   TYR   A N    1 
ATOM   159  C  CA   A TYR   A 1 9   ? 10.013 -9.784  13.712  0.56 14.71 ?  9   TYR   A CA   1 
ATOM   160  C  CA   B TYR   A 1 9   ? 10.001 -9.923  13.555  0.44 13.96 ?  9   TYR   A CA   1 
ATOM   161  C  C    A TYR   A 1 9   ? 9.121  -10.984 13.434  0.56 13.81 ?  9   TYR   A C    1 
ATOM   162  C  C    B TYR   A 1 9   ? 9.237  -11.202 13.224  0.44 13.16 ?  9   TYR   A C    1 
ATOM   163  O  O    A TYR   A 1 9   ? 8.825  -11.786 14.326  0.56 14.78 ?  9   TYR   A O    1 
ATOM   164  O  O    B TYR   A 1 9   ? 9.056  -12.078 14.077  0.44 13.60 ?  9   TYR   A O    1 
ATOM   165  C  CB   A TYR   A 1 9   ? 11.472 -10.211 13.536  0.56 15.04 ?  9   TYR   A CB   1 
ATOM   166  C  CB   B TYR   A 1 9   ? 11.511 -10.175 13.477  0.44 14.49 ?  9   TYR   A CB   1 
ATOM   167  C  CG   A TYR   A 1 9   ? 12.424 -9.054  13.386  0.56 15.14 ?  9   TYR   A CG   1 
ATOM   168  C  CG   B TYR   A 1 9   ? 12.338 -8.910  13.280  0.44 14.87 ?  9   TYR   A CG   1 
ATOM   169  C  CD1  A TYR   A 1 9   ? 12.789 -8.300  14.484  0.56 15.59 ?  9   TYR   A CD1  1 
ATOM   170  C  CD1  B TYR   A 1 9   ? 12.567 -8.030  14.333  0.44 15.22 ?  9   TYR   A CD1  1 
ATOM   171  C  CD2  A TYR   A 1 9   ? 12.937 -8.705  12.146  0.56 14.85 ?  9   TYR   A CD2  1 
ATOM   172  C  CD2  B TYR   A 1 9   ? 12.878 -8.595  12.041  0.44 14.48 ?  9   TYR   A CD2  1 
ATOM   173  C  CE1  A TYR   A 1 9   ? 13.637 -7.228  14.359  0.56 15.99 ?  9   TYR   A CE1  1 
ATOM   174  C  CE1  B TYR   A 1 9   ? 13.315 -6.868  14.153  0.44 15.01 ?  9   TYR   A CE1  1 
ATOM   175  C  CE2  A TYR   A 1 9   ? 13.788 -7.636  12.007  0.56 15.48 ?  9   TYR   A CE2  1 
ATOM   176  C  CE2  B TYR   A 1 9   ? 13.621 -7.440  11.851  0.44 14.41 ?  9   TYR   A CE2  1 
ATOM   177  C  CZ   A TYR   A 1 9   ? 14.137 -6.899  13.115  0.56 16.18 ?  9   TYR   A CZ   1 
ATOM   178  C  CZ   B TYR   A 1 9   ? 13.839 -6.581  12.909  0.44 14.26 ?  9   TYR   A CZ   1 
ATOM   179  O  OH   A TYR   A 1 9   ? 14.987 -5.834  12.971  0.56 17.08 ?  9   TYR   A OH   1 
ATOM   180  O  OH   B TYR   A 1 9   ? 14.584 -5.434  12.715  0.44 14.20 ?  9   TYR   A OH   1 
ATOM   181  H  H    A TYR   A 1 9   ? 10.298 -9.565  15.647  0.56 19.29 ?  9   TYR   A H    1 
ATOM   182  H  H    B TYR   A 1 9   ? 10.110 -9.729  15.513  0.44 17.91 ?  9   TYR   A H    1 
ATOM   183  H  HA   A TYR   A 1 9   ? 9.815  -9.094  13.055  0.56 17.67 ?  9   TYR   A HA   1 
ATOM   184  H  HA   B TYR   A 1 9   ? 9.771  -9.269  12.887  0.44 16.78 ?  9   TYR   A HA   1 
ATOM   185  H  HB2  A TYR   A 1 9   ? 11.745 -10.736 14.302  0.56 18.07 ?  9   TYR   A HB2  1 
ATOM   186  H  HB2  B TYR   A 1 9   ? 11.797 -10.602 14.302  0.44 17.40 ?  9   TYR   A HB2  1 
ATOM   187  H  HB3  A TYR   A 1 9   ? 11.523 -10.747 12.728  0.56 18.07 ?  9   TYR   A HB3  1 
ATOM   188  H  HB3  B TYR   A 1 9   ? 11.682 -10.768 12.728  0.44 17.40 ?  9   TYR   A HB3  1 
ATOM   189  H  HD1  A TYR   A 1 9   ? 12.438 -8.519  15.322  0.56 18.73 ?  9   TYR   A HD1  1 
ATOM   190  H  HD1  B TYR   A 1 9   ? 12.210 -8.223  15.175  0.44 18.29 ?  9   TYR   A HD1  1 
ATOM   191  H  HD2  A TYR   A 1 9   ? 12.699 -9.200  11.393  0.56 17.84 ?  9   TYR   A HD2  1 
ATOM   192  H  HD2  B TYR   A 1 9   ? 12.729 -9.168  11.324  0.44 17.40 ?  9   TYR   A HD2  1 
ATOM   193  H  HE1  A TYR   A 1 9   ? 13.869 -6.731  15.108  0.56 19.21 ?  9   TYR   A HE1  1 
ATOM   194  H  HE1  B TYR   A 1 9   ? 13.462 -6.291  14.869  0.44 18.03 ?  9   TYR   A HE1  1 
ATOM   195  H  HE2  A TYR   A 1 9   ? 14.131 -7.412  11.172  0.56 18.60 ?  9   TYR   A HE2  1 
ATOM   196  H  HE2  B TYR   A 1 9   ? 13.977 -7.246  11.013  0.44 17.31 ?  9   TYR   A HE2  1 
ATOM   197  H  HH   A TYR   A 1 9   ? 15.117 -5.478  13.718  0.56 20.52 ?  9   TYR   A HH   1 
ATOM   198  H  HH   B TYR   A 1 9   ? 14.650 -5.001  13.435  0.44 17.06 ?  9   TYR   A HH   1 
ATOM   199  N  N    A LEU   A 1 10  ? 8.692  -11.085 12.184  0.56 13.20 ?  10  LEU   A N    1 
ATOM   200  N  N    B LEU   A 1 10  ? 8.803  -11.300 11.968  0.44 12.81 ?  10  LEU   A N    1 
ATOM   201  C  CA   A LEU   A 1 10  ? 8.095  -12.303 11.669  0.56 13.64 ?  10  LEU   A CA   1 
ATOM   202  C  CA   B LEU   A 1 10  ? 8.198  -12.512 11.431  0.44 12.74 ?  10  LEU   A CA   1 
ATOM   203  C  C    A LEU   A 1 10  ? 9.221  -13.240 11.246  0.56 12.99 ?  10  LEU   A C    1 
ATOM   204  C  C    B LEU   A 1 10  ? 9.312  -13.455 11.005  0.44 12.16 ?  10  LEU   A C    1 
ATOM   205  O  O    A LEU   A 1 10  ? 10.209 -12.811 10.646  0.56 12.36 ?  10  LEU   A O    1 
ATOM   206  O  O    B LEU   A 1 10  ? 10.238 -13.049 10.297  0.44 11.83 ?  10  LEU   A O    1 
ATOM   207  C  CB   A LEU   A 1 10  ? 7.218  -11.963 10.465  0.56 15.24 ?  10  LEU   A CB   1 
ATOM   208  C  CB   B LEU   A 1 10  ? 7.344  -12.164 10.210  0.44 14.14 ?  10  LEU   A CB   1 
ATOM   209  C  CG   A LEU   A 1 10  ? 6.528  -13.156 9.797   0.56 17.59 ?  10  LEU   A CG   1 
ATOM   210  C  CG   B LEU   A 1 10  ? 6.778  -13.323 9.372   0.44 15.14 ?  10  LEU   A CG   1 
ATOM   211  C  CD1  A LEU   A 1 10  ? 5.464  -13.738 10.709  0.56 18.99 ?  10  LEU   A CD1  1 
ATOM   212  C  CD1  B LEU   A 1 10  ? 5.672  -14.032 10.127  0.44 15.56 ?  10  LEU   A CD1  1 
ATOM   213  C  CD2  A LEU   A 1 10  ? 5.946  -12.768 8.447   0.56 18.81 ?  10  LEU   A CD2  1 
ATOM   214  C  CD2  B LEU   A 1 10  ? 6.281  -12.835 8.020   0.44 15.86 ?  10  LEU   A CD2  1 
ATOM   215  H  H    A LEU   A 1 10  ? 8.739  -10.442 11.606  0.56 15.86 ?  10  LEU   A H    1 
ATOM   216  H  H    B LEU   A 1 10  ? 8.865  -10.670 11.388  0.44 15.39 ?  10  LEU   A H    1 
ATOM   217  H  HA   A LEU   A 1 10  ? 7.557  -12.725 12.357  0.56 16.38 ?  10  LEU   A HA   1 
ATOM   218  H  HA   B LEU   A 1 10  ? 7.646  -12.949 12.098  0.44 15.31 ?  10  LEU   A HA   1 
ATOM   219  H  HB2  A LEU   A 1 10  ? 6.522  -11.349 10.753  0.56 18.31 ?  10  LEU   A HB2  1 
ATOM   220  H  HB2  B LEU   A 1 10  ? 6.587  -11.643 10.516  0.44 16.99 ?  10  LEU   A HB2  1 
ATOM   221  H  HB3  A LEU   A 1 10  ? 7.771  -11.531 9.796   0.56 18.31 ?  10  LEU   A HB3  1 
ATOM   222  H  HB3  B LEU   A 1 10  ? 7.883  -11.623 9.613   0.44 16.99 ?  10  LEU   A HB3  1 
ATOM   223  H  HG   A LEU   A 1 10  ? 7.193  -13.845 9.640   0.56 21.13 ?  10  LEU   A HG   1 
ATOM   224  H  HG   B LEU   A 1 10  ? 7.481  -13.971 9.206   0.44 18.19 ?  10  LEU   A HG   1 
ATOM   225  H  HD11 A LEU   A 1 10  ? 5.016  -14.460 10.243  0.56 22.81 ?  10  LEU   A HD11 1 
ATOM   226  H  HD11 B LEU   A 1 10  ? 5.321  -14.749 9.576   0.44 18.69 ?  10  LEU   A HD11 1 
ATOM   227  H  HD12 A LEU   A 1 10  ? 5.888  -14.076 11.514  0.56 22.81 ?  10  LEU   A HD12 1 
ATOM   228  H  HD12 B LEU   A 1 10  ? 6.032  -14.395 10.952  0.44 18.69 ?  10  LEU   A HD12 1 
ATOM   229  H  HD13 A LEU   A 1 10  ? 4.828  -13.043 10.936  0.56 22.81 ?  10  LEU   A HD13 1 
ATOM   230  H  HD13 B LEU   A 1 10  ? 4.968  -13.394 10.327  0.44 18.69 ?  10  LEU   A HD13 1 
ATOM   231  H  HD21 A LEU   A 1 10  ? 5.523  -13.548 8.057   0.56 22.59 ?  10  LEU   A HD21 1 
ATOM   232  H  HD21 B LEU   A 1 10  ? 5.930  -13.591 7.523   0.44 19.05 ?  10  LEU   A HD21 1 
ATOM   233  H  HD22 A LEU   A 1 10  ? 5.296  -12.064 8.577   0.56 22.59 ?  10  LEU   A HD22 1 
ATOM   234  H  HD22 B LEU   A 1 10  ? 5.582  -12.178 8.161   0.44 19.05 ?  10  LEU   A HD22 1 
ATOM   235  H  HD23 A LEU   A 1 10  ? 6.664  -12.457 7.873   0.56 22.59 ?  10  LEU   A HD23 1 
ATOM   236  H  HD23 B LEU   A 1 10  ? 7.021  -12.436 7.538   0.44 19.05 ?  10  LEU   A HD23 1 
ATOM   237  N  N    A LYS   A 1 11  ? 9.084  -14.519 11.580  0.56 13.21 ?  11  LYS   A N    1 
ATOM   238  N  N    B LYS   A 1 11  ? 9.229  -14.708 11.442  0.44 12.14 ?  11  LYS   A N    1 
ATOM   239  C  CA   A LYS   A 1 11  ? 10.108 -15.516 11.278  0.56 13.08 ?  11  LYS   A CA   1 
ATOM   240  C  CA   B LYS   A 1 11  ? 10.193 -15.719 11.036  0.44 12.23 ?  11  LYS   A CA   1 
ATOM   241  C  C    A LYS   A 1 11  ? 9.786  -16.147 9.928   0.56 13.38 ?  11  LYS   A C    1 
ATOM   242  C  C    B LYS   A 1 11  ? 9.805  -16.230 9.654   0.44 12.80 ?  11  LYS   A C    1 
ATOM   243  O  O    A LYS   A 1 11  ? 8.772  -16.840 9.788   0.56 14.38 ?  11  LYS   A O    1 
ATOM   244  O  O    B LYS   A 1 11  ? 8.645  -16.589 9.423   0.44 13.68 ?  11  LYS   A O    1 
ATOM   245  C  CB   A LYS   A 1 11  ? 10.147 -16.570 12.381  0.56 13.04 ?  11  LYS   A CB   1 
ATOM   246  C  CB   B LYS   A 1 11  ? 10.195 -16.852 12.065  0.44 12.36 ?  11  LYS   A CB   1 
ATOM   247  C  CG   A LYS   A 1 11  ? 11.150 -17.693 12.169  0.56 13.44 ?  11  LYS   A CG   1 
ATOM   248  C  CG   B LYS   A 1 11  ? 11.278 -17.911 11.902  0.44 12.66 ?  11  LYS   A CG   1 
ATOM   249  C  CD   A LYS   A 1 11  ? 11.223 -18.576 13.412  0.56 13.52 ?  11  LYS   A CD   1 
ATOM   250  C  CD   B LYS   A 1 11  ? 11.351 -18.767 13.168  0.44 13.48 ?  11  LYS   A CD   1 
ATOM   251  C  CE   A LYS   A 1 11  ? 12.210 -19.727 13.250  0.56 13.64 ?  11  LYS   A CE   1 
ATOM   252  C  CE   B LYS   A 1 11  ? 12.362 -19.898 13.057  0.44 13.94 ?  11  LYS   A CE   1 
ATOM   253  N  NZ   A LYS   A 1 11  ? 13.613 -19.264 13.040  0.56 13.83 ?  11  LYS   A NZ   1 
ATOM   254  N  NZ   B LYS   A 1 11  ? 13.739 -19.395 12.819  0.44 14.15 ?  11  LYS   A NZ   1 
ATOM   255  H  H    A LYS   A 1 11  ? 8.397  -14.833 11.986  0.56 15.87 ?  11  LYS   A H    1 
ATOM   256  H  H    B LYS   A 1 11  ? 8.620  -15.003 11.973  0.44 14.59 ?  11  LYS   A H    1 
ATOM   257  H  HA   A LYS   A 1 11  ? 10.975 -15.079 11.222  0.56 15.72 ?  11  LYS   A HA   1 
ATOM   258  H  HA   B LYS   A 1 11  ? 11.083 -15.338 10.993  0.44 14.69 ?  11  LYS   A HA   1 
ATOM   259  H  HB2  A LYS   A 1 11  ? 10.371 -16.129 13.215  0.56 15.67 ?  11  LYS   A HB2  1 
ATOM   260  H  HB2  B LYS   A 1 11  ? 10.309 -16.465 12.949  0.44 14.86 ?  11  LYS   A HB2  1 
ATOM   261  H  HB3  A LYS   A 1 11  ? 9.268  -16.969 12.449  0.56 15.67 ?  11  LYS   A HB3  1 
ATOM   262  H  HB3  B LYS   A 1 11  ? 9.342  -17.310 12.023  0.44 14.86 ?  11  LYS   A HB3  1 
ATOM   263  H  HG2  A LYS   A 1 11  ? 10.869 -18.239 11.419  0.56 16.14 ?  11  LYS   A HG2  1 
ATOM   264  H  HG2  B LYS   A 1 11  ? 11.065 -18.490 11.153  0.44 15.22 ?  11  LYS   A HG2  1 
ATOM   265  H  HG3  A LYS   A 1 11  ? 12.028 -17.316 12.007  0.56 16.14 ?  11  LYS   A HG3  1 
ATOM   266  H  HG3  B LYS   A 1 11  ? 12.140 -17.485 11.771  0.44 15.22 ?  11  LYS   A HG3  1 
ATOM   267  H  HD2  A LYS   A 1 11  ? 11.505 -18.038 14.168  0.56 16.25 ?  11  LYS   A HD2  1 
ATOM   268  H  HD2  B LYS   A 1 11  ? 11.610 -18.207 13.917  0.44 16.20 ?  11  LYS   A HD2  1 
ATOM   269  H  HD3  A LYS   A 1 11  ? 10.343 -18.953 13.584  0.56 16.25 ?  11  LYS   A HD3  1 
ATOM   270  H  HD3  B LYS   A 1 11  ? 10.479 -19.161 13.336  0.44 16.20 ?  11  LYS   A HD3  1 
ATOM   271  H  HE2  A LYS   A 1 11  ? 12.193 -20.275 14.050  0.56 16.39 ?  11  LYS   A HE2  1 
ATOM   272  H  HE2  B LYS   A 1 11  ? 12.363 -20.407 13.884  0.44 16.75 ?  11  LYS   A HE2  1 
ATOM   273  H  HE3  A LYS   A 1 11  ? 11.953 -20.259 12.479  0.56 16.39 ?  11  LYS   A HE3  1 
ATOM   274  H  HE3  B LYS   A 1 11  ? 12.115 -20.469 12.314  0.44 16.75 ?  11  LYS   A HE3  1 
ATOM   275  H  HZ1  A LYS   A 1 11  ? 14.157 -19.965 12.951  0.56 16.61 ?  11  LYS   A HZ1  1 
ATOM   276  H  HZ1  B LYS   A 1 11  ? 14.303 -20.081 12.744  0.44 17.00 ?  11  LYS   A HZ1  1 
ATOM   277  H  HZ2  A LYS   A 1 11  ? 13.664 -18.766 12.303  0.56 16.61 ?  11  LYS   A HZ2  1 
ATOM   278  H  HZ2  B LYS   A 1 11  ? 13.763 -18.917 12.070  0.44 17.00 ?  11  LYS   A HZ2  1 
ATOM   279  H  HZ3  A LYS   A 1 11  ? 13.882 -18.778 13.735  0.56 16.61 ?  11  LYS   A HZ3  1 
ATOM   280  H  HZ3  B LYS   A 1 11  ? 13.998 -18.883 13.500  0.44 17.00 ?  11  LYS   A HZ3  1 
ATOM   281  N  N    A LEU   A 1 12  ? 10.647 -15.916 8.933   0.56 12.80 ?  12  LEU   A N    1 
ATOM   282  N  N    B LEU   A 1 12  ? 10.761 -16.229 8.724   0.44 12.06 ?  12  LEU   A N    1 
ATOM   283  C  CA   A LEU   A 1 12  ? 10.424 -16.501 7.615   0.56 12.87 ?  12  LEU   A CA   1 
ATOM   284  C  CA   B LEU   A 1 12  ? 10.533 -16.786 7.392   0.44 12.22 ?  12  LEU   A CA   1 
ATOM   285  C  C    A LEU   A 1 12  ? 11.006 -17.905 7.500   0.56 12.82 ?  12  LEU   A C    1 
ATOM   286  C  C    B LEU   A 1 12  ? 11.126 -18.176 7.220   0.44 11.99 ?  12  LEU   A C    1 
ATOM   287  O  O    A LEU   A 1 12  ? 10.384 -18.785 6.897   0.56 13.50 ?  12  LEU   A O    1 
ATOM   288  O  O    B LEU   A 1 12  ? 10.493 -19.041 6.609   0.44 12.19 ?  12  LEU   A O    1 
ATOM   289  C  CB   A LEU   A 1 12  ? 11.023 -15.614 6.520   0.56 13.88 ?  12  LEU   A CB   1 
ATOM   290  C  CB   B LEU   A 1 12  ? 11.122 -15.872 6.312   0.44 12.41 ?  12  LEU   A CB   1 
ATOM   291  C  CG   A LEU   A 1 12  ? 10.360 -14.253 6.315   0.56 14.86 ?  12  LEU   A CG   1 
ATOM   292  C  CG   B LEU   A 1 12  ? 10.443 -14.522 6.079   0.44 13.14 ?  12  LEU   A CG   1 
ATOM   293  C  CD1  A LEU   A 1 12  ? 11.139 -13.439 5.293   0.56 15.09 ?  12  LEU   A CD1  1 
ATOM   294  C  CD1  B LEU   A 1 12  ? 11.078 -13.825 4.889   0.44 13.55 ?  12  LEU   A CD1  1 
ATOM   295  C  CD2  A LEU   A 1 12  ? 8.913  -14.433 5.880   0.56 15.44 ?  12  LEU   A CD2  1 
ATOM   296  C  CD2  B LEU   A 1 12  ? 8.943  -14.688 5.870   0.44 13.74 ?  12  LEU   A CD2  1 
ATOM   297  H  H    A LEU   A 1 12  ? 11.359 -15.426 8.991   0.56 15.38 ?  12  LEU   A H    1 
ATOM   298  H  H    B LEU   A 1 12  ? 11.554 -15.916 8.842   0.44 14.49 ?  12  LEU   A H    1 
ATOM   299  H  HA   A LEU   A 1 12  ? 9.468  -16.559 7.458   0.56 15.47 ?  12  LEU   A HA   1 
ATOM   300  H  HA   B LEU   A 1 12  ? 9.579  -16.858 7.242   0.44 14.69 ?  12  LEU   A HA   1 
ATOM   301  H  HB2  A LEU   A 1 12  ? 11.955 -15.452 6.733   0.56 16.68 ?  12  LEU   A HB2  1 
ATOM   302  H  HB2  B LEU   A 1 12  ? 12.045 -15.691 6.547   0.44 14.91 ?  12  LEU   A HB2  1 
ATOM   303  H  HB3  A LEU   A 1 12  ? 10.965 -16.090 5.675   0.56 16.68 ?  12  LEU   A HB3  1 
ATOM   304  H  HB3  B LEU   A 1 12  ? 11.098 -16.353 5.470   0.44 14.91 ?  12  LEU   A HB3  1 
ATOM   305  H  HG   A LEU   A 1 12  ? 10.369 -13.768 7.154   0.56 17.86 ?  12  LEU   A HG   1 
ATOM   306  H  HG   B LEU   A 1 12  ? 10.578 -13.965 6.859   0.44 15.79 ?  12  LEU   A HG   1 
ATOM   307  H  HD11 A LEU   A 1 12  ? 10.706 -12.580 5.178   0.56 18.13 ?  12  LEU   A HD11 1 
ATOM   308  H  HD11 B LEU   A 1 12  ? 10.644 -12.970 4.754   0.44 16.29 ?  12  LEU   A HD11 1 
ATOM   309  H  HD12 A LEU   A 1 12  ? 12.046 -13.313 5.614   0.56 18.13 ?  12  LEU   A HD12 1 
ATOM   310  H  HD12 B LEU   A 1 12  ? 12.025 -13.692 5.069   0.44 16.29 ?  12  LEU   A HD12 1 
ATOM   311  H  HD13 A LEU   A 1 12  ? 11.151 -13.920 4.450   0.56 18.13 ?  12  LEU   A HD13 1 
ATOM   312  H  HD13 B LEU   A 1 12  ? 10.970 -14.381 4.101   0.44 16.29 ?  12  LEU   A HD13 1 
ATOM   313  H  HD21 A LEU   A 1 12  ? 8.562  -13.580 5.585   0.56 18.55 ?  12  LEU   A HD21 1 
ATOM   314  H  HD21 B LEU   A 1 12  ? 8.576  -13.853 5.540   0.44 16.51 ?  12  LEU   A HD21 1 
ATOM   315  H  HD22 A LEU   A 1 12  ? 8.879  -15.075 5.152   0.56 18.55 ?  12  LEU   A HD22 1 
ATOM   316  H  HD22 B LEU   A 1 12  ? 8.790  -15.395 5.221   0.44 16.51 ?  12  LEU   A HD22 1 
ATOM   317  H  HD23 A LEU   A 1 12  ? 8.395  -14.763 6.632   0.56 18.55 ?  12  LEU   A HD23 1 
ATOM   318  H  HD23 B LEU   A 1 12  ? 8.528  -14.922 6.715   0.44 16.51 ?  12  LEU   A HD23 1 
ATOM   319  N  N    A THR   A 1 13  ? 12.204 -18.114 8.038   0.56 12.55 ?  13  THR   A N    1 
ATOM   320  N  N    B THR   A 1 13  ? 12.340 -18.392 7.716   0.44 12.59 ?  13  THR   A N    1 
ATOM   321  C  CA   A THR   A 1 13  ? 12.898 -19.394 7.971   0.56 12.52 ?  13  THR   A CA   1 
ATOM   322  C  CA   B THR   A 1 13  ? 13.023 -19.676 7.625   0.44 12.80 ?  13  THR   A CA   1 
ATOM   323  C  C    A THR   A 1 13  ? 13.641 -19.611 9.284   0.56 12.27 ?  13  THR   A C    1 
ATOM   324  C  C    B THR   A 1 13  ? 13.798 -19.877 8.919   0.44 12.41 ?  13  THR   A C    1 
ATOM   325  O  O    A THR   A 1 13  ? 13.511 -18.842 10.241  0.56 12.38 ?  13  THR   A O    1 
ATOM   326  O  O    B THR   A 1 13  ? 13.709 -19.074 9.853   0.44 12.41 ?  13  THR   A O    1 
ATOM   327  C  CB   A THR   A 1 13  ? 13.895 -19.447 6.805   0.56 13.32 ?  13  THR   A CB   1 
ATOM   328  C  CB   B THR   A 1 13  ? 13.981 -19.726 6.426   0.44 13.48 ?  13  THR   A CB   1 
ATOM   329  O  OG1  A THR   A 1 13  ? 14.930 -18.488 7.033   0.56 12.72 ?  13  THR   A OG1  1 
ATOM   330  O  OG1  B THR   A 1 13  ? 15.082 -18.842 6.669   0.44 13.93 ?  13  THR   A OG1  1 
ATOM   331  C  CG2  A THR   A 1 13  ? 13.224 -19.170 5.460   0.56 15.07 ?  13  THR   A CG2  1 
ATOM   332  C  CG2  B THR   A 1 13  ? 13.293 -19.307 5.137   0.44 14.42 ?  13  THR   A CG2  1 
ATOM   333  H  H    A THR   A 1 13  ? 12.650 -17.501 8.439   0.56 15.08 ?  13  THR   A H    1 
ATOM   334  H  H    B THR   A 1 13  ? 12.801 -17.790 8.121   0.44 15.13 ?  13  THR   A H    1 
ATOM   335  H  HA   A THR   A 1 13  ? 12.254 -20.105 7.852   0.56 15.05 ?  13  THR   A HA   1 
ATOM   336  H  HA   B THR   A 1 13  ? 12.368 -20.390 7.529   0.44 15.38 ?  13  THR   A HA   1 
ATOM   337  H  HB   A THR   A 1 13  ? 14.299 -20.325 6.762   0.56 16.00 ?  13  THR   A HB   1 
ATOM   338  H  HB   B THR   A 1 13  ? 14.309 -20.635 6.319   0.44 16.20 ?  13  THR   A HB   1 
ATOM   339  H  HG1  A THR   A 1 13  ? 15.479 -18.492 6.392   0.56 15.29 ?  13  THR   A HG1  1 
ATOM   340  H  HG1  B THR   A 1 13  ? 15.627 -18.877 6.029   0.44 16.73 ?  13  THR   A HG1  1 
ATOM   341  H  HG21 A THR   A 1 13  ? 13.871 -19.274 4.739   0.56 18.11 ?  13  THR   A HG21 1 
ATOM   342  H  HG21 B THR   A 1 13  ? 13.842 -19.560 4.377   0.44 17.33 ?  13  THR   A HG21 1 
ATOM   343  H  HG22 A THR   A 1 13  ? 12.502 -19.804 5.320   0.56 18.11 ?  13  THR   A HG22 1 
ATOM   344  H  HG22 B THR   A 1 13  ? 12.434 -19.745 5.065   0.44 17.33 ?  13  THR   A HG22 1 
ATOM   345  H  HG23 A THR   A 1 13  ? 12.870 -18.273 5.439   0.56 18.11 ?  13  THR   A HG23 1 
ATOM   346  H  HG23 B THR   A 1 13  ? 13.164 -18.347 5.129   0.44 17.33 ?  13  THR   A HG23 1 
ATOM   347  N  N    A ASP   A 1 14  ? 14.445 -20.670 9.308   0.56 13.28 ?  14  ASP   A N    1 
ATOM   348  N  N    B ASP   A 1 14  ? 14.594 -20.948 8.961   0.44 13.22 ?  14  ASP   A N    1 
ATOM   349  C  CA   A ASP   A 1 14  ? 15.283 -20.959 10.460  0.56 14.09 ?  14  ASP   A CA   1 
ATOM   350  C  CA   B ASP   A 1 14  ? 15.423 -21.196 10.132  0.44 13.83 ?  14  ASP   A CA   1 
ATOM   351  C  C    A ASP   A 1 14  ? 16.098 -19.743 10.890  0.56 13.58 ?  14  ASP   A C    1 
ATOM   352  C  C    B ASP   A 1 14  ? 16.276 -19.987 10.498  0.44 12.51 ?  14  ASP   A C    1 
ATOM   353  O  O    A ASP   A 1 14  ? 16.272 -19.496 12.089  0.56 14.05 ?  14  ASP   A O    1 
ATOM   354  O  O    B ASP   A 1 14  ? 16.556 -19.764 11.682  0.44 12.70 ?  14  ASP   A O    1 
ATOM   355  C  CB   A ASP   A 1 14  ? 16.218 -22.108 10.107  0.56 16.79 ?  14  ASP   A CB   1 
ATOM   356  C  CB   B ASP   A 1 14  ? 16.331 -22.402 9.886   0.44 16.89 ?  14  ASP   A CB   1 
ATOM   357  C  CG   A ASP   A 1 14  ? 17.133 -22.459 11.247  0.56 20.32 ?  14  ASP   A CG   1 
ATOM   358  C  CG   B ASP   A 1 14  ? 17.342 -22.596 10.991  0.44 20.02 ?  14  ASP   A CG   1 
ATOM   359  O  OD1  A ASP   A 1 14  ? 16.639 -23.033 12.244  0.56 21.33 ?  14  ASP   A OD1  1 
ATOM   360  O  OD1  B ASP   A 1 14  ? 16.922 -22.674 12.165  0.44 20.72 ?  14  ASP   A OD1  1 
ATOM   361  O  OD2  A ASP   A 1 14  ? 18.330 -22.121 11.156  0.56 22.13 -1 14  ASP   A OD2  1 
ATOM   362  O  OD2  B ASP   A 1 14  ? 18.549 -22.671 10.689  0.44 21.76 -1 14  ASP   A OD2  1 
ATOM   363  H  H    A ASP   A 1 14  ? 14.522 -21.225 8.668   0.56 15.96 ?  14  ASP   A H    1 
ATOM   364  H  H    B ASP   A 1 14  ? 14.672 -21.535 8.331   0.44 15.88 ?  14  ASP   A H    1 
ATOM   365  H  HA   A ASP   A 1 14  ? 14.725 -21.230 11.207  0.56 16.93 ?  14  ASP   A HA   1 
ATOM   366  H  HA   B ASP   A 1 14  ? 14.851 -21.407 10.888  0.44 16.62 ?  14  ASP   A HA   1 
ATOM   367  H  HB2  A ASP   A 1 14  ? 15.676 -22.884 9.864   0.56 20.17 ?  14  ASP   A HB2  1 
ATOM   368  H  HB2  B ASP   A 1 14  ? 15.791 -23.211 9.845   0.44 20.29 ?  14  ASP   A HB2  1 
ATOM   369  H  HB3  A ASP   A 1 14  ? 16.763 -21.848 9.343   0.56 20.17 ?  14  ASP   A HB3  1 
ATOM   370  H  HB3  B ASP   A 1 14  ? 16.807 -22.280 9.050   0.44 20.29 ?  14  ASP   A HB3  1 
ATOM   371  N  N    A ASN   A 1 15  ? 16.612 -18.969 9.928   0.56 13.08 ?  15  ASN   A N    1 
ATOM   372  N  N    B ASN   A 1 15  ? 16.697 -19.189 9.504   0.44 11.62 ?  15  ASN   A N    1 
ATOM   373  C  CA   A ASN   A 1 15  ? 17.581 -17.921 10.227  0.56 12.68 ?  15  ASN   A CA   1 
ATOM   374  C  CA   B ASN   A 1 15  ? 17.686 -18.142 9.743   0.44 11.90 ?  15  ASN   A CA   1 
ATOM   375  C  C    A ASN   A 1 15  ? 17.217 -16.531 9.718   0.56 12.54 ?  15  ASN   A C    1 
ATOM   376  C  C    B ASN   A 1 15  ? 17.319 -16.756 9.217   0.44 11.95 ?  15  ASN   A C    1 
ATOM   377  O  O    A ASN   A 1 15  ? 17.970 -15.591 9.991   0.56 13.07 ?  15  ASN   A O    1 
ATOM   378  O  O    B ASN   A 1 15  ? 18.116 -15.827 9.392   0.44 12.32 ?  15  ASN   A O    1 
ATOM   379  C  CB   A ASN   A 1 15  ? 18.968 -18.290 9.674   0.56 12.70 ?  15  ASN   A CB   1 
ATOM   380  C  CB   B ASN   A 1 15  ? 19.051 -18.547 9.157   0.44 11.74 ?  15  ASN   A CB   1 
ATOM   381  C  CG   A ASN   A 1 15  ? 18.975 -18.444 8.167   0.56 12.99 ?  15  ASN   A CG   1 
ATOM   382  C  CG   B ASN   A 1 15  ? 19.031 -18.625 7.642   0.44 12.30 ?  15  ASN   A CG   1 
ATOM   383  O  OD1  A ASN   A 1 15  ? 18.232 -19.254 7.610   0.56 13.14 ?  15  ASN   A OD1  1 
ATOM   384  O  OD1  B ASN   A 1 15  ? 18.368 -19.484 7.067   0.44 12.20 ?  15  ASN   A OD1  1 
ATOM   385  N  ND2  A ASN   A 1 15  ? 19.801 -17.647 7.493   0.56 13.54 ?  15  ASN   A ND2  1 
ATOM   386  N  ND2  B ASN   A 1 15  ? 19.761 -17.730 6.989   0.44 12.58 ?  15  ASN   A ND2  1 
ATOM   387  H  H    A ASN   A 1 15  ? 16.413 -19.033 9.100   0.56 15.72 ?  15  ASN   A H    1 
ATOM   388  H  H    B ASN   A 1 15  ? 16.421 -19.244 8.690   0.44 13.97 ?  15  ASN   A H    1 
ATOM   389  H  HA   A ASN   A 1 15  ? 17.670 -17.847 11.191  0.56 15.24 ?  15  ASN   A HA   1 
ATOM   390  H  HA   B ASN   A 1 15  ? 17.806 -18.064 10.700  0.44 14.31 ?  15  ASN   A HA   1 
ATOM   391  H  HB2  A ASN   A 1 15  ? 19.600 -17.588 9.910   0.56 15.26 ?  15  ASN   A HB2  1 
ATOM   392  H  HB2  B ASN   A 1 15  ? 19.714 -17.887 9.419   0.44 14.11 ?  15  ASN   A HB2  1 
ATOM   393  H  HB3  A ASN   A 1 15  ? 19.248 -19.130 10.067  0.56 15.26 ?  15  ASN   A HB3  1 
ATOM   394  H  HB3  B ASN   A 1 15  ? 19.306 -19.421 9.506   0.44 14.11 ?  15  ASN   A HB3  1 
ATOM   395  H  HD21 A ASN   A 1 15  ? 19.841 -17.695 6.634   0.56 16.27 ?  15  ASN   A HD21 1 
ATOM   396  H  HD21 B ASN   A 1 15  ? 19.776 -17.740 6.129   0.44 15.12 ?  15  ASN   A HD21 1 
ATOM   397  H  HD22 A ASN   A 1 15  ? 20.302 -17.088 7.914   0.56 16.27 ?  15  ASN   A HD22 1 
ATOM   398  H  HD22 B ASN   A 1 15  ? 20.213 -17.142 7.421   0.44 15.12 ?  15  ASN   A HD22 1 
ATOM   399  N  N    A VAL   A 1 16  ? 16.105 -16.362 9.000   0.56 12.61 ?  16  VAL   A N    1 
ATOM   400  N  N    B VAL   A 1 16  ? 16.164 -16.583 8.575   0.44 11.80 ?  16  VAL   A N    1 
ATOM   401  C  CA   A VAL   A 1 16  ? 15.729 -15.080 8.411   0.56 12.33 ?  16  VAL   A CA   1 
ATOM   402  C  CA   B VAL   A 1 16  ? 15.763 -15.301 8.004   0.44 12.04 ?  16  VAL   A CA   1 
ATOM   403  C  C    A VAL   A 1 16  ? 14.448 -14.578 9.063   0.56 12.45 ?  16  VAL   A C    1 
ATOM   404  C  C    B VAL   A 1 16  ? 14.499 -14.800 8.695   0.44 11.48 ?  16  VAL   A C    1 
ATOM   405  O  O    A VAL   A 1 16  ? 13.455 -15.313 9.164   0.56 12.92 ?  16  VAL   A O    1 
ATOM   406  O  O    B VAL   A 1 16  ? 13.496 -15.520 8.777   0.44 11.05 ?  16  VAL   A O    1 
ATOM   407  C  CB   A VAL   A 1 16  ? 15.593 -15.166 6.880   0.56 13.02 ?  16  VAL   A CB   1 
ATOM   408  C  CB   B VAL   A 1 16  ? 15.554 -15.385 6.481   0.44 12.90 ?  16  VAL   A CB   1 
ATOM   409  C  CG1  A VAL   A 1 16  ? 15.188 -13.802 6.298   0.56 13.44 ?  16  VAL   A CG1  1 
ATOM   410  C  CG1  B VAL   A 1 16  ? 15.129 -14.027 5.936   0.44 13.59 ?  16  VAL   A CG1  1 
ATOM   411  C  CG2  A VAL   A 1 16  ? 16.893 -15.663 6.254   0.56 13.93 ?  16  VAL   A CG2  1 
ATOM   412  C  CG2  B VAL   A 1 16  ? 16.817 -15.875 5.784   0.44 13.04 ?  16  VAL   A CG2  1 
ATOM   413  H  H    A VAL   A 1 16  ? 15.538 -16.989 8.844   0.56 15.16 ?  16  VAL   A H    1 
ATOM   414  H  H    B VAL   A 1 16  ? 15.595 -17.218 8.451   0.44 14.18 ?  16  VAL   A H    1 
ATOM   415  H  HA   A VAL   A 1 16  ? 16.421 -14.432 8.602   0.56 14.82 ?  16  VAL   A HA   1 
ATOM   416  H  HA   B VAL   A 1 16  ? 16.474 -14.660 8.171   0.44 14.46 ?  16  VAL   A HA   1 
ATOM   417  H  HB   A VAL   A 1 16  ? 14.896 -15.804 6.661   0.56 15.64 ?  16  VAL   A HB   1 
ATOM   418  H  HB   B VAL   A 1 16  ? 14.847 -16.023 6.298   0.44 15.50 ?  16  VAL   A HB   1 
ATOM   419  H  HG11 A VAL   A 1 16  ? 15.278 -13.833 5.331   0.56 16.15 ?  16  VAL   A HG11 1 
ATOM   420  H  HG11 B VAL   A 1 16  ? 15.179 -14.047 4.970   0.44 16.32 ?  16  VAL   A HG11 1 
ATOM   421  H  HG12 A VAL   A 1 16  ? 14.265 -13.616 6.534   0.56 16.15 ?  16  VAL   A HG12 1 
ATOM   422  H  HG12 B VAL   A 1 16  ? 14.221 -13.843 6.219   0.44 16.32 ?  16  VAL   A HG12 1 
ATOM   423  H  HG13 A VAL   A 1 16  ? 15.769 -13.117 6.660   0.56 16.15 ?  16  VAL   A HG13 1 
ATOM   424  H  HG13 B VAL   A 1 16  ? 15.730 -13.348 6.285   0.44 16.32 ?  16  VAL   A HG13 1 
ATOM   425  H  HG21 A VAL   A 1 16  ? 16.910 -15.422 5.316   0.56 16.74 ?  16  VAL   A HG21 1 
ATOM   426  H  HG21 B VAL   A 1 16  ? 16.751 -15.674 4.838   0.44 15.66 ?  16  VAL   A HG21 1 
ATOM   427  H  HG22 A VAL   A 1 16  ? 17.641 -15.258 6.716   0.56 16.74 ?  16  VAL   A HG22 1 
ATOM   428  H  HG22 B VAL   A 1 16  ? 17.586 -15.423 6.164   0.44 15.66 ?  16  VAL   A HG22 1 
ATOM   429  H  HG23 A VAL   A 1 16  ? 16.938 -16.629 6.349   0.56 16.74 ?  16  VAL   A HG23 1 
ATOM   430  H  HG23 B VAL   A 1 16  ? 16.902 -16.834 5.914   0.44 15.66 ?  16  VAL   A HG23 1 
ATOM   431  N  N    A TYR   A 1 17  ? 14.476 -13.312 9.478   0.56 12.35 ?  17  TYR   A N    1 
ATOM   432  N  N    B TYR   A 1 17  ? 14.544 -13.547 9.143   0.44 11.74 ?  17  TYR   A N    1 
ATOM   433  C  CA   A TYR   A 1 17  ? 13.389 -12.636 10.167  0.56 12.15 ?  17  TYR   A CA   1 
ATOM   434  C  CA   B TYR   A 1 17  ? 13.455 -12.859 9.821   0.44 11.73 ?  17  TYR   A CA   1 
ATOM   435  C  C    A TYR   A 1 17  ? 13.130 -11.313 9.462   0.56 12.62 ?  17  TYR   A C    1 
ATOM   436  C  C    B TYR   A 1 17  ? 13.182 -11.545 9.097   0.44 12.00 ?  17  TYR   A C    1 
ATOM   437  O  O    A TYR   A 1 17  ? 14.052 -10.729 8.890   0.56 11.99 ?  17  TYR   A O    1 
ATOM   438  O  O    B TYR   A 1 17  ? 14.054 -11.014 8.407   0.44 11.31 ?  17  TYR   A O    1 
ATOM   439  C  CB   A TYR   A 1 17  ? 13.795 -12.389 11.624  0.56 12.74 ?  17  TYR   A CB   1 
ATOM   440  C  CB   B TYR   A 1 17  ? 13.854 -12.552 11.266  0.44 12.10 ?  17  TYR   A CB   1 
ATOM   441  C  CG   A TYR   A 1 17  ? 14.033 -13.677 12.384  0.56 14.12 ?  17  TYR   A CG   1 
ATOM   442  C  CG   B TYR   A 1 17  ? 13.973 -13.776 12.142  0.44 13.73 ?  17  TYR   A CG   1 
ATOM   443  C  CD1  A TYR   A 1 17  ? 15.233 -14.377 12.266  0.56 15.07 ?  17  TYR   A CD1  1 
ATOM   444  C  CD1  B TYR   A 1 17  ? 15.119 -14.565 12.128  0.44 14.60 ?  17  TYR   A CD1  1 
ATOM   445  C  CD2  A TYR   A 1 17  ? 13.045 -14.209 13.201  0.56 14.55 ?  17  TYR   A CD2  1 
ATOM   446  C  CD2  B TYR   A 1 17  ? 12.933 -14.146 12.984  0.44 14.13 ?  17  TYR   A CD2  1 
ATOM   447  C  CE1  A TYR   A 1 17  ? 15.441 -15.573 12.949  0.56 15.84 ?  17  TYR   A CE1  1 
ATOM   448  C  CE1  B TYR   A 1 17  ? 15.220 -15.697 12.929  0.44 14.97 ?  17  TYR   A CE1  1 
ATOM   449  C  CE2  A TYR   A 1 17  ? 13.242 -15.404 13.888  0.56 15.05 ?  17  TYR   A CE2  1 
ATOM   450  C  CE2  B TYR   A 1 17  ? 13.023 -15.272 13.787  0.44 14.48 ?  17  TYR   A CE2  1 
ATOM   451  C  CZ   A TYR   A 1 17  ? 14.442 -16.079 13.760  0.56 15.55 ?  17  TYR   A CZ   1 
ATOM   452  C  CZ   B TYR   A 1 17  ? 14.167 -16.043 13.759  0.44 14.80 ?  17  TYR   A CZ   1 
ATOM   453  O  OH   A TYR   A 1 17  ? 14.637 -17.258 14.446  0.56 16.47 ?  17  TYR   A OH   1 
ATOM   454  O  OH   B TYR   A 1 17  ? 14.247 -17.158 14.561  0.44 15.28 ?  17  TYR   A OH   1 
ATOM   455  H  H    A TYR   A 1 17  ? 15.153 -12.788 9.349   0.56 14.84 ?  17  TYR   A H    1 
ATOM   456  H  H    B TYR   A 1 17  ? 15.240 -13.057 9.052   0.44 14.12 ?  17  TYR   A H    1 
ATOM   457  H  HA   A TYR   A 1 17  ? 12.583 -13.168 10.136  0.56 14.60 ?  17  TYR   A HA   1 
ATOM   458  H  HA   B TYR   A 1 17  ? 12.656 -13.417 9.814   0.44 14.10 ?  17  TYR   A HA   1 
ATOM   459  H  HB2  A TYR   A 1 17  ? 14.612 -11.871 11.639  0.56 15.31 ?  17  TYR   A HB2  1 
ATOM   460  H  HB2  B TYR   A 1 17  ? 14.715 -12.110 11.262  0.44 14.54 ?  17  TYR   A HB2  1 
ATOM   461  H  HB3  A TYR   A 1 17  ? 13.087 -11.903 12.071  0.56 15.31 ?  17  TYR   A HB3  1 
ATOM   462  H  HB3  B TYR   A 1 17  ? 13.184 -11.978 11.654  0.44 14.54 ?  17  TYR   A HB3  1 
ATOM   463  H  HD1  A TYR   A 1 17  ? 15.906 -14.044 11.718  0.56 18.10 ?  17  TYR   A HD1  1 
ATOM   464  H  HD1  B TYR   A 1 17  ? 15.829 -14.335 11.569  0.44 17.55 ?  17  TYR   A HD1  1 
ATOM   465  H  HD2  A TYR   A 1 17  ? 12.233 -13.759 13.285  0.56 17.48 ?  17  TYR   A HD2  1 
ATOM   466  H  HD2  B TYR   A 1 17  ? 12.158 -13.635 13.006  0.44 16.98 ?  17  TYR   A HD2  1 
ATOM   467  H  HE1  A TYR   A 1 17  ? 16.249 -16.032 12.865  0.56 19.03 ?  17  TYR   A HE1  1 
ATOM   468  H  HE1  B TYR   A 1 17  ? 15.996 -16.214 12.913  0.44 17.99 ?  17  TYR   A HE1  1 
ATOM   469  H  HE2  A TYR   A 1 17  ? 12.568 -15.742 14.432  0.56 18.08 ?  17  TYR   A HE2  1 
ATOM   470  H  HE2  B TYR   A 1 17  ? 12.316 -15.503 14.347  0.44 17.39 ?  17  TYR   A HE2  1 
ATOM   471  H  HH   A TYR   A 1 17  ? 15.401 -17.564 14.287  0.56 19.79 ?  17  TYR   A HH   1 
ATOM   472  H  HH   B TYR   A 1 17  ? 13.476 -17.445 14.721  0.44 18.36 ?  17  TYR   A HH   1 
ATOM   473  N  N    A ILE   A 1 18  ? 11.881 -10.831 9.489   0.56 12.59 ?  18  ILE   A N    1 
ATOM   474  N  N    B ILE   A 1 18  ? 11.977 -10.993 9.272   0.44 12.81 ?  18  ILE   A N    1 
ATOM   475  C  CA   A ILE   A 1 18  ? 11.511 -9.638  8.725   0.56 12.34 ?  18  ILE   A CA   1 
ATOM   476  C  CA   B ILE   A 1 18  ? 11.570 -9.812  8.507   0.44 12.94 ?  18  ILE   A CA   1 
ATOM   477  C  C    A ILE   A 1 18  ? 10.552 -8.772  9.533   0.56 12.77 ?  18  ILE   A C    1 
ATOM   478  C  C    B ILE   A 1 18  ? 10.565 -8.976  9.299   0.44 13.57 ?  18  ILE   A C    1 
ATOM   479  O  O    A ILE   A 1 18  ? 9.704  -9.283  10.272  0.56 13.38 ?  18  ILE   A O    1 
ATOM   480  O  O    B ILE   A 1 18  ? 9.785  -9.502  10.097  0.44 13.88 ?  18  ILE   A O    1 
ATOM   481  C  CB   A ILE   A 1 18  ? 10.944 -10.017 7.340   0.56 12.49 ?  18  ILE   A CB   1 
ATOM   482  C  CB   B ILE   A 1 18  ? 11.038 -10.241 7.119   0.44 12.71 ?  18  ILE   A CB   1 
ATOM   483  C  CG1  A ILE   A 1 18  ? 10.895 -8.803  6.413   0.56 13.78 ?  18  ILE   A CG1  1 
ATOM   484  C  CG1  B ILE   A 1 18  ? 10.961 -9.049  6.173   0.44 12.95 ?  18  ILE   A CG1  1 
ATOM   485  C  CG2  A ILE   A 1 18  ? 9.577  -10.691 7.458   0.56 13.41 ?  18  ILE   A CG2  1 
ATOM   486  C  CG2  B ILE   A 1 18  ? 9.692  -10.962 7.239   0.44 12.35 ?  18  ILE   A CG2  1 
ATOM   487  C  CD1  A ILE   A 1 18  ? 10.665 -9.169  4.968   0.56 15.60 ?  18  ILE   A CD1  1 
ATOM   488  C  CD1  B ILE   A 1 18  ? 10.765 -9.457  4.740   0.44 14.25 ?  18  ILE   A CD1  1 
ATOM   489  H  H    A ILE   A 1 18  ? 11.226 -11.183 9.933   0.56 15.13 ?  18  ILE   A H    1 
ATOM   490  H  H    B ILE   A 1 18  ? 11.390 -11.294 9.822   0.44 15.40 ?  18  ILE   A H    1 
ATOM   491  H  HA   A ILE   A 1 18  ? 12.304 -9.113  8.575   0.56 14.83 ?  18  ILE   A HA   1 
ATOM   492  H  HA   B ILE   A 1 18  ? 12.358 -9.272  8.358   0.44 15.54 ?  18  ILE   A HA   1 
ATOM   493  H  HB   A ILE   A 1 18  ? 11.549 -10.656 6.945   0.56 15.01 ?  18  ILE   A HB   1 
ATOM   494  H  HB   B ILE   A 1 18  ? 11.668 -10.875 6.738   0.44 15.27 ?  18  ILE   A HB   1 
ATOM   495  H  HG12 A ILE   A 1 18  ? 10.175 -8.215  6.686   0.56 16.56 ?  18  ILE   A HG12 1 
ATOM   496  H  HG12 B ILE   A 1 18  ? 10.217 -8.486  6.431   0.44 15.56 ?  18  ILE   A HG12 1 
ATOM   497  H  HG13 A ILE   A 1 18  ? 11.744 -8.330  6.462   0.56 16.56 ?  18  ILE   A HG13 1 
ATOM   498  H  HG13 B ILE   A 1 18  ? 11.792 -8.549  6.229   0.44 15.56 ?  18  ILE   A HG13 1 
ATOM   499  H  HG21 A ILE   A 1 18  ? 9.334  -11.059 6.591   0.56 16.11 ?  18  ILE   A HG21 1 
ATOM   500  H  HG21 B ILE   A 1 18  ? 9.467  -11.361 6.381   0.44 14.84 ?  18  ILE   A HG21 1 
ATOM   501  H  HG22 A ILE   A 1 18  ? 9.633  -11.398 8.114   0.56 16.11 ?  18  ILE   A HG22 1 
ATOM   502  H  HG22 B ILE   A 1 18  ? 9.762  -11.654 7.914   0.44 14.84 ?  18  ILE   A HG22 1 
ATOM   503  H  HG23 A ILE   A 1 18  ? 8.919  -10.032 7.730   0.56 16.11 ?  18  ILE   A HG23 1 
ATOM   504  H  HG23 B ILE   A 1 18  ? 9.009  -10.321 7.492   0.44 14.84 ?  18  ILE   A HG23 1 
ATOM   505  H  HD11 A ILE   A 1 18  ? 10.710 -8.365  4.423   0.56 18.74 ?  18  ILE   A HD11 1 
ATOM   506  H  HD11 B ILE   A 1 18  ? 10.795 -8.662  4.183   0.44 17.13 ?  18  ILE   A HD11 1 
ATOM   507  H  HD12 A ILE   A 1 18  ? 11.351 -9.795  4.685   0.56 18.74 ?  18  ILE   A HD12 1 
ATOM   508  H  HD12 B ILE   A 1 18  ? 11.471 -10.068 4.487   0.44 17.13 ?  18  ILE   A HD12 1 
ATOM   509  H  HD13 A ILE   A 1 18  ? 9.789  -9.576  4.878   0.56 18.74 ?  18  ILE   A HD13 1 
ATOM   510  H  HD13 B ILE   A 1 18  ? 9.901  -9.888  4.653   0.44 17.13 ?  18  ILE   A HD13 1 
ATOM   511  N  N    A LYS   A 1 19  ? 10.688 -7.452  9.382   0.56 12.58 ?  19  LYS   A N    1 
ATOM   512  N  N    B LYS   A 1 19  ? 10.581 -7.660  9.055   0.44 13.60 ?  19  LYS   A N    1 
ATOM   513  C  CA   A LYS   A 1 19  ? 9.894  -6.498  10.140  0.56 12.87 ?  19  LYS   A CA   1 
ATOM   514  C  CA   B LYS   A 1 19  ? 9.734  -6.695  9.757   0.44 13.70 ?  19  LYS   A CA   1 
ATOM   515  C  C    A LYS   A 1 19  ? 9.696  -5.252  9.292   0.56 13.12 ?  19  LYS   A C    1 
ATOM   516  C  C    B LYS   A 1 19  ? 9.567  -5.444  8.895   0.44 13.34 ?  19  LYS   A C    1 
ATOM   517  O  O    A LYS   A 1 19  ? 10.611 -4.829  8.582   0.56 13.29 ?  19  LYS   A O    1 
ATOM   518  O  O    B LYS   A 1 19  ? 10.469 -5.072  8.139   0.44 12.66 ?  19  LYS   A O    1 
ATOM   519  C  CB   A LYS   A 1 19  ? 10.639 -6.132  11.429  0.56 13.77 ?  19  LYS   A CB   1 
ATOM   520  C  CB   B LYS   A 1 19  ? 10.364 -6.300  11.103  0.44 14.36 ?  19  LYS   A CB   1 
ATOM   521  C  CG   A LYS   A 1 19  ? 9.912  -5.219  12.389  0.56 15.07 ?  19  LYS   A CG   1 
ATOM   522  C  CG   B LYS   A 1 19  ? 9.561  -5.309  11.963  0.44 14.91 ?  19  LYS   A CG   1 
ATOM   523  C  CD   A LYS   A 1 19  ? 10.818 -4.959  13.579  0.56 16.36 ?  19  LYS   A CD   1 
ATOM   524  C  CD   B LYS   A 1 19  ? 10.337 -4.938  13.233  0.44 15.77 ?  19  LYS   A CD   1 
ATOM   525  C  CE   A LYS   A 1 19  ? 10.181 -4.061  14.609  0.56 17.09 ?  19  LYS   A CE   1 
ATOM   526  C  CE   B LYS   A 1 19  ? 9.530  -4.061  14.189  0.44 16.08 ?  19  LYS   A CE   1 
ATOM   527  N  NZ   A LYS   A 1 19  ? 11.090 -3.888  15.772  0.56 17.43 ?  19  LYS   A NZ   1 
ATOM   528  N  NZ   B LYS   A 1 19  ? 10.375 -3.580  15.327  0.44 16.14 ?  19  LYS   A NZ   1 
ATOM   529  H  H    A LYS   A 1 19  ? 11.251 -7.072  8.844   0.56 15.12 ?  19  LYS   A H    1 
ATOM   530  H  H    B LYS   A 1 19  ? 11.091 -7.308  8.469   0.44 16.34 ?  19  LYS   A H    1 
ATOM   531  H  HA   A LYS   A 1 19  ? 9.029  -6.874  10.368  0.56 15.47 ?  19  LYS   A HA   1 
ATOM   532  H  HA   B LYS   A 1 19  ? 8.862  -7.095  9.922   0.44 16.46 ?  19  LYS   A HA   1 
ATOM   533  H  HB2  A LYS   A 1 19  ? 10.831 -6.951  11.914  0.56 16.54 ?  19  LYS   A HB2  1 
ATOM   534  H  HB2  B LYS   A 1 19  ? 10.485 -7.104  11.631  0.44 17.25 ?  19  LYS   A HB2  1 
ATOM   535  H  HB3  A LYS   A 1 19  ? 11.470 -5.695  11.193  0.56 16.54 ?  19  LYS   A HB3  1 
ATOM   536  H  HB3  B LYS   A 1 19  ? 11.225 -5.897  10.925  0.44 17.25 ?  19  LYS   A HB3  1 
ATOM   537  H  HG2  A LYS   A 1 19  ? 9.714  -4.373  11.955  0.56 18.10 ?  19  LYS   A HG2  1 
ATOM   538  H  HG2  B LYS   A 1 19  ? 9.400  -4.496  11.459  0.44 17.91 ?  19  LYS   A HG2  1 
ATOM   539  H  HG3  A LYS   A 1 19  ? 9.098  -5.645  12.701  0.56 18.10 ?  19  LYS   A HG3  1 
ATOM   540  H  HG3  B LYS   A 1 19  ? 8.720  -5.713  12.228  0.44 17.91 ?  19  LYS   A HG3  1 
ATOM   541  H  HD2  A LYS   A 1 19  ? 11.029 -5.805  14.006  0.56 19.65 ?  19  LYS   A HD2  1 
ATOM   542  H  HD2  B LYS   A 1 19  ? 10.579 -5.749  13.706  0.44 18.94 ?  19  LYS   A HD2  1 
ATOM   543  H  HD3  A LYS   A 1 19  ? 11.633 -4.533  13.268  0.56 19.65 ?  19  LYS   A HD3  1 
ATOM   544  H  HD3  B LYS   A 1 19  ? 11.137 -4.447  12.985  0.44 18.94 ?  19  LYS   A HD3  1 
ATOM   545  H  HE2  A LYS   A 1 19  ? 10.012 -3.189  14.216  0.56 20.53 ?  19  LYS   A HE2  1 
ATOM   546  H  HE2  B LYS   A 1 19  ? 9.193  -3.286  13.712  0.44 19.32 ?  19  LYS   A HE2  1 
ATOM   547  H  HE3  A LYS   A 1 19  ? 9.354  -4.459  14.919  0.56 20.53 ?  19  LYS   A HE3  1 
ATOM   548  H  HE3  B LYS   A 1 19  ? 8.793  -4.576  14.555  0.44 19.32 ?  19  LYS   A HE3  1 
ATOM   549  H  HZ1  A LYS   A 1 19  ? 10.696 -3.391  16.394  0.56 20.94 ?  19  LYS   A HZ1  1 
ATOM   550  H  HZ1  B LYS   A 1 19  ? 9.890  -3.071  15.874  0.44 19.39 ?  19  LYS   A HZ1  1 
ATOM   551  H  HZ2  A LYS   A 1 19  ? 11.293 -4.682  16.118  0.56 20.94 ?  19  LYS   A HZ2  1 
ATOM   552  H  HZ2  B LYS   A 1 19  ? 10.693 -4.273  15.785  0.44 19.39 ?  19  LYS   A HZ2  1 
ATOM   553  H  HZ3  A LYS   A 1 19  ? 11.841 -3.487  15.513  0.56 20.94 ?  19  LYS   A HZ3  1 
ATOM   554  H  HZ3  B LYS   A 1 19  ? 11.058 -3.100  15.017  0.44 19.39 ?  19  LYS   A HZ3  1 
ATOM   555  N  N    A ASN   A 1 20  ? 8.500  -4.671  9.355   0.56 13.97 ?  20  ASN   A N    1 
ATOM   556  N  N    B ASN   A 1 20  ? 8.403  -4.798  9.020   0.44 14.11 ?  20  ASN   A N    1 
ATOM   557  C  CA   A ASN   A 1 20  ? 8.287  -3.341  8.796   0.56 14.35 ?  20  ASN   A CA   1 
ATOM   558  C  CA   B ASN   A 1 20  ? 8.138  -3.509  8.372   0.44 14.54 ?  20  ASN   A CA   1 
ATOM   559  C  C    A ASN   A 1 20  ? 8.907  -2.347  9.762   0.56 14.75 ?  20  ASN   A C    1 
ATOM   560  C  C    B ASN   A 1 20  ? 8.662  -2.407  9.289   0.44 14.98 ?  20  ASN   A C    1 
ATOM   561  O  O    A ASN   A 1 20  ? 8.385  -2.127  10.860  0.56 15.22 ?  20  ASN   A O    1 
ATOM   562  O  O    B ASN   A 1 20  ? 7.972  -1.977  10.219  0.44 15.95 ?  20  ASN   A O    1 
ATOM   563  C  CB   A ASN   A 1 20  ? 6.798  -3.077  8.599   0.56 14.88 ?  20  ASN   A CB   1 
ATOM   564  C  CB   B ASN   A 1 20  ? 6.640  -3.352  8.104   0.44 14.11 ?  20  ASN   A CB   1 
ATOM   565  C  CG   A ASN   A 1 20  ? 6.494  -1.636  8.224   0.56 15.85 ?  20  ASN   A CG   1 
ATOM   566  C  CG   B ASN   A 1 20  ? 6.261  -1.972  7.556   0.44 13.82 ?  20  ASN   A CG   1 
ATOM   567  O  OD1  A ASN   A 1 20  ? 5.503  -1.076  8.679   0.56 18.45 ?  20  ASN   A OD1  1 
ATOM   568  O  OD1  B ASN   A 1 20  ? 5.171  -1.453  7.846   0.44 14.02 ?  20  ASN   A OD1  1 
ATOM   569  N  ND2  A ASN   A 1 20  ? 7.345  -1.029  7.401   0.56 15.52 ?  20  ASN   A ND2  1 
ATOM   570  N  ND2  B ASN   A 1 20  ? 7.143  -1.388  6.742   0.44 14.14 ?  20  ASN   A ND2  1 
ATOM   571  H  H    A ASN   A 1 20  ? 7.798  -5.028  9.707   0.56 16.79 ?  20  ASN   A H    1 
ATOM   572  H  H    B ASN   A 1 20  ? 7.737  -5.104  9.474   0.44 16.95 ?  20  ASN   A H    1 
ATOM   573  H  HA   A ASN   A 1 20  ? 8.735  -3.272  7.943   0.56 17.25 ?  20  ASN   A HA   1 
ATOM   574  H  HA   B ASN   A 1 20  ? 8.609  -3.470  7.527   0.44 17.47 ?  20  ASN   A HA   1 
ATOM   575  H  HB2  A ASN   A 1 20  ? 6.470  -3.644  7.887   0.56 17.88 ?  20  ASN   A HB2  1 
ATOM   576  H  HB2  B ASN   A 1 20  ? 6.359  -4.011  7.452   0.44 16.96 ?  20  ASN   A HB2  1 
ATOM   577  H  HB3  A ASN   A 1 20  ? 6.330  -3.277  9.423   0.56 17.88 ?  20  ASN   A HB3  1 
ATOM   578  H  HB3  B ASN   A 1 20  ? 6.155  -3.484  8.935   0.44 16.96 ?  20  ASN   A HB3  1 
ATOM   579  H  HD21 A ASN   A 1 20  ? 7.209  -0.213  7.167   0.56 18.65 ?  20  ASN   A HD21 1 
ATOM   580  H  HD21 B ASN   A 1 20  ? 6.979  -0.614  6.410   0.44 16.99 ?  20  ASN   A HD21 1 
ATOM   581  H  HD22 A ASN   A 1 20  ? 8.036  -1.449  7.106   0.56 18.65 ?  20  ASN   A HD22 1 
ATOM   582  H  HD22 B ASN   A 1 20  ? 7.885  -1.786  6.549   0.44 16.99 ?  20  ASN   A HD22 1 
ATOM   583  N  N    A ALA   A 1 21  ? 10.043 -1.774  9.375   0.56 15.16 ?  21  ALA   A N    1 
ATOM   584  N  N    B ALA   A 1 21  ? 9.883  -1.935  9.023   0.44 15.39 ?  21  ALA   A N    1 
ATOM   585  C  CA   A ALA   A 1 21  ? 10.747 -0.875  10.271  0.56 15.17 ?  21  ALA   A CA   1 
ATOM   586  C  CA   B ALA   A 1 21  ? 10.517 -0.952  9.896   0.44 15.60 ?  21  ALA   A CA   1 
ATOM   587  C  C    A ALA   A 1 21  ? 11.704 -0.014  9.472   0.56 15.41 ?  21  ALA   A C    1 
ATOM   588  C  C    B ALA   A 1 21  ? 11.630 -0.226  9.151   0.44 14.56 ?  21  ALA   A C    1 
ATOM   589  O  O    A ALA   A 1 21  ? 12.169 -0.406  8.399   0.56 16.17 ?  21  ALA   A O    1 
ATOM   590  O  O    B ALA   A 1 21  ? 12.136 -0.707  8.135   0.44 14.17 ?  21  ALA   A O    1 
ATOM   591  C  CB   A ALA   A 1 21  ? 11.526 -1.656  11.330  0.56 15.92 ?  21  ALA   A CB   1 
ATOM   592  C  CB   B ALA   A 1 21  ? 11.062 -1.609  11.171  0.44 17.19 ?  21  ALA   A CB   1 
ATOM   593  H  H    A ALA   A 1 21  ? 10.425 -1.890  8.610   0.56 18.22 ?  21  ALA   A H    1 
ATOM   594  H  H    B ALA   A 1 21  ? 10.357 -2.170  8.345   0.44 18.49 ?  21  ALA   A H    1 
ATOM   595  H  HA   A ALA   A 1 21  ? 10.105 -0.297  10.717  0.56 18.23 ?  21  ALA   A HA   1 
ATOM   596  H  HA   B ALA   A 1 21  ? 9.853  -0.302  10.161  0.44 18.74 ?  21  ALA   A HA   1 
ATOM   597  H  HB1  A ALA   A 1 21  ? 11.885 -1.030  11.971  0.56 19.12 ?  21  ALA   A HB1  1 
ATOM   598  H  HB1  B ALA   A 1 21  ? 11.473 -0.929  11.726  0.44 20.65 ?  21  ALA   A HB1  1 
ATOM   599  H  HB2  A ALA   A 1 21  ? 10.914 -2.270  11.774  0.56 19.12 ?  21  ALA   A HB2  1 
ATOM   600  H  HB2  B ALA   A 1 21  ? 10.329 -2.029  11.654  0.44 20.65 ?  21  ALA   A HB2  1 
ATOM   601  H  HB3  A ALA   A 1 21  ? 12.234 -2.152  10.898  0.56 19.12 ?  21  ALA   A HB3  1 
ATOM   602  H  HB3  B ALA   A 1 21  ? 11.721 -2.281  10.929  0.44 20.65 ?  21  ALA   A HB3  1 
ATOM   603  N  N    A ASP   A 1 22  ? 11.974 1.167   10.017  0.56 15.39 ?  22  ASP   A N    1 
ATOM   604  N  N    B ASP   A 1 22  ? 11.990 0.949   9.681   0.44 14.30 ?  22  ASP   A N    1 
ATOM   605  C  CA   A ASP   A 1 22  ? 13.022 2.050   9.529   0.56 15.10 ?  22  ASP   A CA   1 
ATOM   606  C  CA   B ASP   A 1 22  ? 13.119 1.744   9.200   0.44 14.25 ?  22  ASP   A CA   1 
ATOM   607  C  C    A ASP   A 1 22  ? 14.346 1.546   10.087  0.56 14.39 ?  22  ASP   A C    1 
ATOM   608  C  C    B ASP   A 1 22  ? 14.399 1.221   9.848   0.44 12.98 ?  22  ASP   A C    1 
ATOM   609  O  O    A ASP   A 1 22  ? 14.563 1.577   11.302  0.56 15.13 ?  22  ASP   A O    1 
ATOM   610  O  O    B ASP   A 1 22  ? 14.513 1.200   11.079  0.44 13.63 ?  22  ASP   A O    1 
ATOM   611  C  CB   A ASP   A 1 22  ? 12.729 3.453   10.043  0.56 15.93 ?  22  ASP   A CB   1 
ATOM   612  C  CB   B ASP   A 1 22  ? 12.884 3.209   9.579   0.44 15.61 ?  22  ASP   A CB   1 
ATOM   613  C  CG   A ASP   A 1 22  ? 13.720 4.483   9.548   0.56 16.49 ?  22  ASP   A CG   1 
ATOM   614  C  CG   B ASP   A 1 22  ? 13.988 4.147   9.096   0.44 16.77 ?  22  ASP   A CG   1 
ATOM   615  O  OD1  A ASP   A 1 22  ? 14.816 4.113   9.083   0.56 16.24 ?  22  ASP   A OD1  1 
ATOM   616  O  OD1  B ASP   A 1 22  ? 15.044 3.672   8.625   0.44 16.08 ?  22  ASP   A OD1  1 
ATOM   617  O  OD2  A ASP   A 1 22  ? 13.386 5.683   9.636   0.56 17.57 -1 22  ASP   A OD2  1 
ATOM   618  O  OD2  B ASP   A 1 22  ? 13.794 5.378   9.194   0.44 19.02 -1 22  ASP   A OD2  1 
ATOM   619  H  H    A ASP   A 1 22  ? 11.535 1.488   10.688  0.56 18.50 ?  22  ASP   A H    1 
ATOM   620  H  H    B ASP   A 1 22  ? 11.566 1.316   10.337  0.44 17.18 ?  22  ASP   A H    1 
ATOM   621  H  HA   A ASP   A 1 22  ? 13.045 2.043   8.558   0.56 18.14 ?  22  ASP   A HA   1 
ATOM   622  H  HA   B ASP   A 1 22  ? 13.187 1.666   8.236   0.44 17.12 ?  22  ASP   A HA   1 
ATOM   623  H  HB2  A ASP   A 1 22  ? 11.843 3.713   9.750   0.56 19.13 ?  22  ASP   A HB2  1 
ATOM   624  H  HB2  B ASP   A 1 22  ? 12.044 3.501   9.193   0.44 18.75 ?  22  ASP   A HB2  1 
ATOM   625  H  HB3  A ASP   A 1 22  ? 12.760 3.434   11.016  0.56 19.13 ?  22  ASP   A HB3  1 
ATOM   626  H  HB3  B ASP   A 1 22  ? 12.847 3.279   10.545  0.44 18.75 ?  22  ASP   A HB3  1 
ATOM   627  N  N    A ILE   A 1 23  ? 15.229 1.079   9.201   0.56 14.36 ?  23  ILE   A N    1 
ATOM   628  N  N    B ILE   A 1 23  ? 15.356 0.781   9.022   0.44 12.53 ?  23  ILE   A N    1 
ATOM   629  C  CA   A ILE   A 1 23  ? 16.489 0.482   9.638   0.56 13.82 ?  23  ILE   A CA   1 
ATOM   630  C  CA   B ILE   A 1 23  ? 16.603 0.211   9.531   0.44 12.44 ?  23  ILE   A CA   1 
ATOM   631  C  C    A ILE   A 1 23  ? 17.285 1.445   10.510  0.56 14.23 ?  23  ILE   A C    1 
ATOM   632  C  C    B ILE   A 1 23  ? 17.324 1.194   10.440  0.44 13.05 ?  23  ILE   A C    1 
ATOM   633  O  O    A ILE   A 1 23  ? 18.023 1.016   11.406  0.56 15.27 ?  23  ILE   A O    1 
ATOM   634  O  O    B ILE   A 1 23  ? 18.006 0.787   11.390  0.44 13.54 ?  23  ILE   A O    1 
ATOM   635  C  CB   A ILE   A 1 23  ? 17.294 -0.025  8.423   0.56 13.51 ?  23  ILE   A CB   1 
ATOM   636  C  CB   B ILE   A 1 23  ? 17.505 -0.295  8.381   0.44 12.42 ?  23  ILE   A CB   1 
ATOM   637  C  CG1  A ILE   A 1 23  ? 18.462 -0.905  8.881   0.56 13.60 ?  23  ILE   A CG1  1 
ATOM   638  C  CG1  B ILE   A 1 23  ? 18.566 -1.258  8.925   0.44 12.31 ?  23  ILE   A CG1  1 
ATOM   639  C  CG2  A ILE   A 1 23  ? 17.762 1.145   7.560   0.56 13.65 ?  23  ILE   A CG2  1 
ATOM   640  C  CG2  B ILE   A 1 23  ? 18.165 0.865   7.646   0.44 12.60 ?  23  ILE   A CG2  1 
ATOM   641  C  CD1  A ILE   A 1 23  ? 19.152 -1.647  7.752   0.56 14.59 ?  23  ILE   A CD1  1 
ATOM   642  C  CD1  B ILE   A 1 23  ? 19.466 -1.857  7.859   0.44 12.66 ?  23  ILE   A CD1  1 
ATOM   643  H  H    A ILE   A 1 23  ? 15.118 1.096   8.351   0.56 17.25 ?  23  ILE   A H    1 
ATOM   644  H  H    B ILE   A 1 23  ? 15.303 0.797   8.176   0.44 15.06 ?  23  ILE   A H    1 
ATOM   645  H  HA   A ILE   A 1 23  ? 16.281 -0.293  10.184  0.56 16.60 ?  23  ILE   A HA   1 
ATOM   646  H  HA   B ILE   A 1 23  ? 16.380 -0.563  10.068  0.44 14.95 ?  23  ILE   A HA   1 
ATOM   647  H  HB   A ILE   A 1 23  ? 16.704 -0.573  7.883   0.56 16.24 ?  23  ILE   A HB   1 
ATOM   648  H  HB   B ILE   A 1 23  ? 16.955 -0.784  7.747   0.44 14.92 ?  23  ILE   A HB   1 
ATOM   649  H  HG12 A ILE   A 1 23  ? 19.122 -0.345  9.318   0.56 16.34 ?  23  ILE   A HG12 1 
ATOM   650  H  HG12 B ILE   A 1 23  ? 19.132 -0.784  9.553   0.44 14.80 ?  23  ILE   A HG12 1 
ATOM   651  H  HG13 A ILE   A 1 23  ? 18.125 -1.565  9.508   0.56 16.34 ?  23  ILE   A HG13 1 
ATOM   652  H  HG13 B ILE   A 1 23  ? 18.122 -1.996  9.377   0.44 14.80 ?  23  ILE   A HG13 1 
ATOM   653  H  HG21 A ILE   A 1 23  ? 18.134 0.801   6.733   0.56 16.40 ?  23  ILE   A HG21 1 
ATOM   654  H  HG21 B ILE   A 1 23  ? 18.523 0.543   6.800   0.44 15.14 ?  23  ILE   A HG21 1 
ATOM   655  H  HG22 A ILE   A 1 23  ? 17.002 1.718   7.364   0.56 16.40 ?  23  ILE   A HG22 1 
ATOM   656  H  HG22 B ILE   A 1 23  ? 17.503 1.550   7.483   0.44 15.14 ?  23  ILE   A HG22 1 
ATOM   657  H  HG23 A ILE   A 1 23  ? 18.436 1.648   8.042   0.56 16.40 ?  23  ILE   A HG23 1 
ATOM   658  H  HG23 B ILE   A 1 23  ? 18.885 1.219   8.192   0.44 15.14 ?  23  ILE   A HG23 1 
ATOM   659  H  HD11 A ILE   A 1 23  ? 19.844 -2.213  8.127   0.56 17.53 ?  23  ILE   A HD11 1 
ATOM   660  H  HD11 B ILE   A 1 23  ? 20.027 -2.536  8.265   0.44 15.22 ?  23  ILE   A HD11 1 
ATOM   661  H  HD12 A ILE   A 1 23  ? 18.497 -2.188  7.286   0.56 17.53 ?  23  ILE   A HD12 1 
ATOM   662  H  HD12 B ILE   A 1 23  ? 18.914 -2.252  7.168   0.44 15.22 ?  23  ILE   A HD12 1 
ATOM   663  H  HD13 A ILE   A 1 23  ? 19.543 -1.001  7.145   0.56 17.53 ?  23  ILE   A HD13 1 
ATOM   664  H  HD13 B ILE   A 1 23  ? 20.018 -1.153  7.483   0.44 15.22 ?  23  ILE   A HD13 1 
ATOM   665  N  N    A VAL   A 1 24  ? 17.151 2.753   10.274  0.56 14.67 ?  24  VAL   A N    1 
ATOM   666  N  N    B VAL   A 1 24  ? 17.185 2.495   10.176  0.44 13.93 ?  24  VAL   A N    1 
ATOM   667  C  CA   A VAL   A 1 24  ? 17.827 3.734   11.121  0.56 15.38 ?  24  VAL   A CA   1 
ATOM   668  C  CA   B VAL   A 1 24  ? 17.834 3.500   11.012  0.44 15.33 ?  24  VAL   A CA   1 
ATOM   669  C  C    A VAL   A 1 24  ? 17.306 3.650   12.549  0.56 16.02 ?  24  VAL   A C    1 
ATOM   670  C  C    B VAL   A 1 24  ? 17.261 3.467   12.422  0.44 15.98 ?  24  VAL   A C    1 
ATOM   671  O  O    A VAL   A 1 24  ? 18.081 3.583   13.512  0.56 16.54 ?  24  VAL   A O    1 
ATOM   672  O  O    B VAL   A 1 24  ? 18.002 3.518   13.411  0.44 16.82 ?  24  VAL   A O    1 
ATOM   673  C  CB   A VAL   A 1 24  ? 17.653 5.152   10.547  0.56 15.66 ?  24  VAL   A CB   1 
ATOM   674  C  CB   B VAL   A 1 24  ? 17.706 4.894   10.368  0.44 16.59 ?  24  VAL   A CB   1 
ATOM   675  C  CG1  A VAL   A 1 24  ? 18.138 6.198   11.548  0.56 16.35 ?  24  VAL   A CG1  1 
ATOM   676  C  CG1  B VAL   A 1 24  ? 18.404 5.944   11.213  0.44 17.89 ?  24  VAL   A CG1  1 
ATOM   677  C  CG2  A VAL   A 1 24  ? 18.382 5.282   9.223   0.56 15.76 ?  24  VAL   A CG2  1 
ATOM   678  C  CG2  B VAL   A 1 24  ? 18.259 4.874   8.951   0.44 16.77 ?  24  VAL   A CG2  1 
ATOM   679  H  H    A VAL   A 1 24  ? 16.678 3.091   9.640   0.56 17.63 ?  24  VAL   A H    1 
ATOM   680  H  H    B VAL   A 1 24  ? 16.714 2.816   9.534   0.44 16.73 ?  24  VAL   A H    1 
ATOM   681  H  HA   A VAL   A 1 24  ? 18.774 3.534   11.136  0.56 18.47 ?  24  VAL   A HA   1 
ATOM   682  H  HA   B VAL   A 1 24  ? 18.778 3.292   11.076  0.44 18.42 ?  24  VAL   A HA   1 
ATOM   683  H  HB   A VAL   A 1 24  ? 16.711 5.311   10.382  0.56 18.82 ?  24  VAL   A HB   1 
ATOM   684  H  HB   B VAL   A 1 24  ? 16.766 5.129   10.316  0.44 19.93 ?  24  VAL   A HB   1 
ATOM   685  H  HG11 A VAL   A 1 24  ? 18.293 7.032   11.078  0.56 19.64 ?  24  VAL   A HG11 1 
ATOM   686  H  HG11 B VAL   A 1 24  ? 18.514 6.751   10.687  0.44 21.49 ?  24  VAL   A HG11 1 
ATOM   687  H  HG12 A VAL   A 1 24  ? 17.459 6.324   12.228  0.56 19.64 ?  24  VAL   A HG12 1 
ATOM   688  H  HG12 B VAL   A 1 24  ? 17.853 6.129   11.989  0.44 21.49 ?  24  VAL   A HG12 1 
ATOM   689  H  HG13 A VAL   A 1 24  ? 18.964 5.888   11.952  0.56 19.64 ?  24  VAL   A HG13 1 
ATOM   690  H  HG13 B VAL   A 1 24  ? 19.268 5.606   11.490  0.44 21.49 ?  24  VAL   A HG13 1 
ATOM   691  H  HG21 A VAL   A 1 24  ? 18.146 6.129   8.814   0.56 18.93 ?  24  VAL   A HG21 1 
ATOM   692  H  HG21 B VAL   A 1 24  ? 18.278 5.780   8.607   0.44 20.15 ?  24  VAL   A HG21 1 
ATOM   693  H  HG22 A VAL   A 1 24  ? 19.338 5.249   9.383   0.56 18.93 ?  24  VAL   A HG22 1 
ATOM   694  H  HG22 B VAL   A 1 24  ? 19.157 4.507   8.969   0.44 20.15 ?  24  VAL   A HG22 1 
ATOM   695  H  HG23 A VAL   A 1 24  ? 18.119 4.551   8.640   0.56 18.93 ?  24  VAL   A HG23 1 
ATOM   696  H  HG23 B VAL   A 1 24  ? 17.688 4.321   8.395   0.44 20.15 ?  24  VAL   A HG23 1 
ATOM   697  N  N    A GLU   A 1 25  ? 15.982 3.691   12.707  0.56 16.54 ?  25  GLU   A N    1 
ATOM   698  N  N    B GLU   A 1 25  ? 15.934 3.376   12.537  0.44 16.32 ?  25  GLU   A N    1 
ATOM   699  C  CA   A GLU   A 1 25  ? 15.399 3.635   14.043  0.56 18.06 ?  25  GLU   A CA   1 
ATOM   700  C  CA   B GLU   A 1 25  ? 15.313 3.299   13.855  0.44 16.96 ?  25  GLU   A CA   1 
ATOM   701  C  C    A GLU   A 1 25  ? 15.620 2.271   14.685  0.56 16.61 ?  25  GLU   A C    1 
ATOM   702  C  C    B GLU   A 1 25  ? 15.603 1.964   14.526  0.44 16.43 ?  25  GLU   A C    1 
ATOM   703  O  O    A GLU   A 1 25  ? 15.832 2.183   15.900  0.56 17.13 ?  25  GLU   A O    1 
ATOM   704  O  O    B GLU   A 1 25  ? 15.841 1.913   15.739  0.44 17.35 ?  25  GLU   A O    1 
ATOM   705  C  CB   A GLU   A 1 25  ? 13.915 4.002   13.987  0.56 20.80 ?  25  GLU   A CB   1 
ATOM   706  C  CB   B GLU   A 1 25  ? 13.809 3.564   13.752  0.44 18.55 ?  25  GLU   A CB   1 
ATOM   707  C  CG   A GLU   A 1 25  ? 13.667 5.458   13.595  0.56 24.20 ?  25  GLU   A CG   1 
ATOM   708  C  CG   B GLU   A 1 25  ? 13.479 4.986   13.322  0.44 21.60 ?  25  GLU   A CG   1 
ATOM   709  C  CD   A GLU   A 1 25  ? 14.463 6.452   14.433  0.56 27.03 ?  25  GLU   A CD   1 
ATOM   710  C  CD   B GLU   A 1 25  ? 14.167 6.024   14.177  0.44 24.32 ?  25  GLU   A CD   1 
ATOM   711  O  OE1  A GLU   A 1 25  ? 14.528 6.291   15.671  0.56 28.04 ?  25  GLU   A OE1  1 
ATOM   712  O  OE1  B GLU   A 1 25  ? 14.202 5.842   15.414  0.44 25.67 ?  25  GLU   A OE1  1 
ATOM   713  O  OE2  A GLU   A 1 25  ? 15.046 7.385   13.843  0.56 28.43 -1 25  GLU   A OE2  1 
ATOM   714  O  OE2  B GLU   A 1 25  ? 14.679 7.014   13.616  0.44 25.34 -1 25  GLU   A OE2  1 
ATOM   715  H  H    A GLU   A 1 25  ? 15.410 3.763   12.065  0.56 19.87 ?  25  GLU   A H    1 
ATOM   716  H  H    B GLU   A 1 25  ? 15.383 3.354   11.878  0.44 19.60 ?  25  GLU   A H    1 
ATOM   717  H  HA   A GLU   A 1 25  ? 15.843 4.289   14.601  0.56 21.69 ?  25  GLU   A HA   1 
ATOM   718  H  HA   B GLU   A 1 25  ? 15.701 3.979   14.419  0.44 20.38 ?  25  GLU   A HA   1 
ATOM   719  H  HB2  A GLU   A 1 25  ? 13.470 3.441   13.327  0.56 24.99 ?  25  GLU   A HB2  1 
ATOM   720  H  HB2  B GLU   A 1 25  ? 13.422 2.965   13.096  0.44 22.28 ?  25  GLU   A HB2  1 
ATOM   721  H  HB3  A GLU   A 1 25  ? 13.516 3.860   14.859  0.56 24.99 ?  25  GLU   A HB3  1 
ATOM   722  H  HB3  B GLU   A 1 25  ? 13.400 3.415   14.619  0.44 22.28 ?  25  GLU   A HB3  1 
ATOM   723  H  HG2  A GLU   A 1 25  ? 13.946 5.585   12.679  0.56 29.06 ?  25  GLU   A HG2  1 
ATOM   724  H  HG2  B GLU   A 1 25  ? 13.762 5.118   12.405  0.44 25.95 ?  25  GLU   A HG2  1 
ATOM   725  H  HG3  A GLU   A 1 25  ? 12.717 5.647   13.687  0.56 29.06 ?  25  GLU   A HG3  1 
ATOM   726  H  HG3  B GLU   A 1 25  ? 12.529 5.138   13.408  0.44 25.95 ?  25  GLU   A HG3  1 
ATOM   727  N  N    A GLU   A 1 26  ? 15.580 1.199   13.888  0.56 16.17 ?  26  GLU   A N    1 
ATOM   728  N  N    B GLU   A 1 26  ? 15.599 0.872   13.758  0.44 16.16 ?  26  GLU   A N    1 
ATOM   729  C  CA   A GLU   A 1 26  ? 15.889 -0.126  14.423  0.56 16.09 ?  26  GLU   A CA   1 
ATOM   730  C  CA   B GLU   A 1 26  ? 15.949 -0.423  14.332  0.44 16.35 ?  26  GLU   A CA   1 
ATOM   731  C  C    A GLU   A 1 26  ? 17.307 -0.166  14.976  0.56 15.30 ?  26  GLU   A C    1 
ATOM   732  C  C    B GLU   A 1 26  ? 17.375 -0.413  14.863  0.44 15.73 ?  26  GLU   A C    1 
ATOM   733  O  O    A GLU   A 1 26  ? 17.536 -0.613  16.106  0.56 15.26 ?  26  GLU   A O    1 
ATOM   734  O  O    B GLU   A 1 26  ? 17.666 -1.022  15.898  0.44 15.87 ?  26  GLU   A O    1 
ATOM   735  C  CB   A GLU   A 1 26  ? 15.732 -1.190  13.334  0.56 17.41 ?  26  GLU   A CB   1 
ATOM   736  C  CB   B GLU   A 1 26  ? 15.768 -1.528  13.291  0.44 17.18 ?  26  GLU   A CB   1 
ATOM   737  C  CG   A GLU   A 1 26  ? 14.345 -1.767  13.164  0.56 20.16 ?  26  GLU   A CG   1 
ATOM   738  C  CG   B GLU   A 1 26  ? 14.318 -1.829  12.969  0.44 18.67 ?  26  GLU   A CG   1 
ATOM   739  C  CD   A GLU   A 1 26  ? 13.898 -2.605  14.349  0.56 21.47 ?  26  GLU   A CD   1 
ATOM   740  C  CD   B GLU   A 1 26  ? 13.563 -2.383  14.157  0.44 19.23 ?  26  GLU   A CD   1 
ATOM   741  O  OE1  A GLU   A 1 26  ? 14.336 -3.770  14.498  0.56 21.51 ?  26  GLU   A OE1  1 
ATOM   742  O  OE1  B GLU   A 1 26  ? 14.087 -3.298  14.826  0.44 19.81 ?  26  GLU   A OE1  1 
ATOM   743  O  OE2  A GLU   A 1 26  ? 13.096 -2.087  15.141  0.56 21.87 -1 26  GLU   A OE2  1 
ATOM   744  O  OE2  B GLU   A 1 26  ? 12.453 -1.887  14.427  0.44 18.41 -1 26  GLU   A OE2  1 
ATOM   745  H  H    A GLU   A 1 26  ? 15.378 1.219   13.050  0.56 19.43 ?  26  GLU   A H    1 
ATOM   746  H  H    B GLU   A 1 26  ? 15.403 0.852   12.921  0.44 19.41 ?  26  GLU   A H    1 
ATOM   747  H  HA   A GLU   A 1 26  ? 15.272 -0.324  15.141  0.56 19.33 ?  26  GLU   A HA   1 
ATOM   748  H  HA   B GLU   A 1 26  ? 15.361 -0.613  15.075  0.44 19.65 ?  26  GLU   A HA   1 
ATOM   749  H  HB2  A GLU   A 1 26  ? 15.990 -0.797  12.485  0.56 20.92 ?  26  GLU   A HB2  1 
ATOM   750  H  HB2  B GLU   A 1 26  ? 16.204 -1.258  12.464  0.44 20.64 ?  26  GLU   A HB2  1 
ATOM   751  H  HB3  A GLU   A 1 26  ? 16.329 -1.922  13.547  0.56 20.92 ?  26  GLU   A HB3  1 
ATOM   752  H  HB3  B GLU   A 1 26  ? 16.176 -2.346  13.621  0.44 20.64 ?  26  GLU   A HB3  1 
ATOM   753  H  HG2  A GLU   A 1 26  ? 13.723 -1.032  13.054  0.56 24.22 ?  26  GLU   A HG2  1 
ATOM   754  H  HG2  B GLU   A 1 26  ? 13.876 -1.009  12.701  0.44 22.42 ?  26  GLU   A HG2  1 
ATOM   755  H  HG3  A GLU   A 1 26  ? 14.334 -2.332  12.377  0.56 24.22 ?  26  GLU   A HG3  1 
ATOM   756  H  HG3  B GLU   A 1 26  ? 14.276 -2.483  12.257  0.44 22.42 ?  26  GLU   A HG3  1 
ATOM   757  N  N    . ALA   A 1 27  ? 18.278 0.290   14.179  1.00 14.95 ?  27  ALA   A N    1 
ATOM   758  C  CA   . ALA   A 1 27  ? 19.664 0.305   14.626  1.00 15.24 ?  27  ALA   A CA   1 
ATOM   759  C  C    . ALA   A 1 27  ? 19.824 1.121   15.902  1.00 17.13 ?  27  ALA   A C    1 
ATOM   760  O  O    . ALA   A 1 27  ? 20.492 0.686   16.845  1.00 17.20 ?  27  ALA   A O    1 
ATOM   761  C  CB   . ALA   A 1 27  ? 20.572 0.835   13.515  1.00 15.14 ?  27  ALA   A CB   1 
ATOM   762  H  H    A ALA   A 1 27  ? 18.157 0.589   13.378  0.56 17.97 ?  27  ALA   A H    1 
ATOM   763  H  H    B ALA   A 1 27  ? 18.114 0.758   13.472  0.44 17.97 ?  27  ALA   A H    1 
ATOM   764  H  HA   . ALA   A 1 27  ? 19.937 -0.602  14.815  1.00 18.31 ?  27  ALA   A HA   1 
ATOM   765  H  HB1  . ALA   A 1 27  ? 21.491 0.836   13.829  1.00 18.18 ?  27  ALA   A HB1  1 
ATOM   766  H  HB2  . ALA   A 1 27  ? 20.493 0.262   12.734  1.00 18.18 ?  27  ALA   A HB2  1 
ATOM   767  H  HB3  . ALA   A 1 27  ? 20.304 1.740   13.284  1.00 18.18 ?  27  ALA   A HB3  1 
ATOM   768  N  N    A LYS   A 1 28  ? 19.212 2.305   15.963  0.56 18.92 ?  28  LYS   A N    1 
ATOM   769  N  N    B LYS   A 1 28  ? 19.203 2.306   15.948  0.44 18.44 ?  28  LYS   A N    1 
ATOM   770  C  CA   A LYS   A 1 28  ? 19.378 3.129   17.157  0.56 21.53 ?  28  LYS   A CA   1 
ATOM   771  C  CA   B LYS   A 1 28  ? 19.285 3.146   17.138  0.44 20.47 ?  28  LYS   A CA   1 
ATOM   772  C  C    A LYS   A 1 28  ? 18.809 2.456   18.402  0.56 22.79 ?  28  LYS   A C    1 
ATOM   773  C  C    B LYS   A 1 28  ? 18.730 2.425   18.358  0.44 21.78 ?  28  LYS   A C    1 
ATOM   774  O  O    A LYS   A 1 28  ? 19.264 2.736   19.516  0.56 23.82 ?  28  LYS   A O    1 
ATOM   775  O  O    B LYS   A 1 28  ? 19.290 2.524   19.455  0.44 22.60 ?  28  LYS   A O    1 
ATOM   776  C  CB   A LYS   A 1 28  ? 18.763 4.513   16.952  0.56 23.53 ?  28  LYS   A CB   1 
ATOM   777  C  CB   B LYS   A 1 28  ? 18.527 4.459   16.917  0.44 21.76 ?  28  LYS   A CB   1 
ATOM   778  C  CG   A LYS   A 1 28  ? 19.637 5.432   16.118  0.56 24.87 ?  28  LYS   A CG   1 
ATOM   779  C  CG   B LYS   A 1 28  ? 19.066 5.338   15.803  0.44 22.72 ?  28  LYS   A CG   1 
ATOM   780  C  CD   A LYS   A 1 28  ? 19.125 6.859   16.120  0.56 26.37 ?  28  LYS   A CD   1 
ATOM   781  C  CD   B LYS   A 1 28  ? 18.428 6.721   15.845  0.44 24.35 ?  28  LYS   A CD   1 
ATOM   782  C  CE   A LYS   A 1 28  ? 17.781 6.960   15.428  0.56 27.31 ?  28  LYS   A CE   1 
ATOM   783  C  CE   B LYS   A 1 28  ? 18.581 7.452   14.519  0.44 25.65 ?  28  LYS   A CE   1 
ATOM   784  N  NZ   A LYS   A 1 28  ? 17.321 8.370   15.334  0.56 27.86 ?  28  LYS   A NZ   1 
ATOM   785  N  NZ   B LYS   A 1 28  ? 18.293 8.912   14.631  0.44 26.49 ?  28  LYS   A NZ   1 
ATOM   786  H  H    A LYS   A 1 28  ? 18.720 2.648   15.347  0.56 22.72 ?  28  LYS   A H    1 
ATOM   787  H  H    B LYS   A 1 28  ? 18.731 2.637   15.312  0.44 22.15 ?  28  LYS   A H    1 
ATOM   788  H  HA   A LYS   A 1 28  ? 20.326 3.257   17.308  0.56 25.86 ?  28  LYS   A HA   1 
ATOM   789  H  HA   B LYS   A 1 28  ? 20.209 3.361   17.323  0.44 24.58 ?  28  LYS   A HA   1 
ATOM   790  H  HB2  A LYS   A 1 28  ? 17.912 4.414   16.501  0.56 28.26 ?  28  LYS   A HB2  1 
ATOM   791  H  HB2  B LYS   A 1 28  ? 17.606 4.256   16.700  0.44 26.14 ?  28  LYS   A HB2  1 
ATOM   792  H  HB3  A LYS   A 1 28  ? 18.632 4.931   17.819  0.56 28.26 ?  28  LYS   A HB3  1 
ATOM   793  H  HB3  B LYS   A 1 28  ? 18.563 4.982   17.732  0.44 26.14 ?  28  LYS   A HB3  1 
ATOM   794  H  HG2  A LYS   A 1 28  ? 20.538 5.433   16.480  0.56 29.86 ?  28  LYS   A HG2  1 
ATOM   795  H  HG2  B LYS   A 1 28  ? 20.023 5.442   15.909  0.44 27.29 ?  28  LYS   A HG2  1 
ATOM   796  H  HG3  A LYS   A 1 28  ? 19.647 5.116   15.201  0.56 29.86 ?  28  LYS   A HG3  1 
ATOM   797  H  HG3  B LYS   A 1 28  ? 18.865 4.939   14.944  0.44 27.29 ?  28  LYS   A HG3  1 
ATOM   798  H  HD2  A LYS   A 1 28  ? 19.020 7.161   17.037  0.56 31.66 ?  28  LYS   A HD2  1 
ATOM   799  H  HD2  B LYS   A 1 28  ? 17.481 6.632   16.035  0.44 29.24 ?  28  LYS   A HD2  1 
ATOM   800  H  HD3  A LYS   A 1 28  ? 19.755 7.427   15.649  0.56 31.66 ?  28  LYS   A HD3  1 
ATOM   801  H  HD3  B LYS   A 1 28  ? 18.860 7.251   16.534  0.44 29.24 ?  28  LYS   A HD3  1 
ATOM   802  H  HE2  A LYS   A 1 28  ? 17.858 6.601   14.530  0.56 32.79 ?  28  LYS   A HE2  1 
ATOM   803  H  HE2  B LYS   A 1 28  ? 19.489 7.344   14.195  0.44 30.80 ?  28  LYS   A HE2  1 
ATOM   804  H  HE3  A LYS   A 1 28  ? 17.122 6.460   15.934  0.56 32.79 ?  28  LYS   A HE3  1 
ATOM   805  H  HE3  B LYS   A 1 28  ? 17.953 7.076   13.883  0.44 30.80 ?  28  LYS   A HE3  1 
ATOM   806  H  HZ1  A LYS   A 1 28  ? 16.533 8.406   14.925  0.56 33.46 ?  28  LYS   A HZ1  1 
ATOM   807  H  HZ1  B LYS   A 1 28  ? 18.392 9.304   13.838  0.44 31.81 ?  28  LYS   A HZ1  1 
ATOM   808  H  HZ2  A LYS   A 1 28  ? 17.243 8.719   16.149  0.56 33.46 ?  28  LYS   A HZ2  1 
ATOM   809  H  HZ2  B LYS   A 1 28  ? 17.458 9.036   14.913  0.44 31.81 ?  28  LYS   A HZ2  1 
ATOM   810  H  HZ3  A LYS   A 1 28  ? 17.911 8.851   14.870  0.56 33.46 ?  28  LYS   A HZ3  1 
ATOM   811  H  HZ3  B LYS   A 1 28  ? 18.853 9.288   15.212  0.44 31.81 ?  28  LYS   A HZ3  1 
ATOM   812  N  N    A LYS   A 1 29  ? 17.821 1.574   18.239  0.56 23.07 ?  29  LYS   A N    1 
ATOM   813  N  N    B LYS   A 1 29  ? 17.635 1.684   18.185  0.44 22.23 ?  29  LYS   A N    1 
ATOM   814  C  CA   A LYS   A 1 29  ? 17.250 0.858   19.379  0.56 24.34 ?  29  LYS   A CA   1 
ATOM   815  C  CA   B LYS   A 1 29  ? 16.970 1.068   19.328  0.44 23.24 ?  29  LYS   A CA   1 
ATOM   816  C  C    A LYS   A 1 29  ? 18.100 -0.345  19.773  0.56 23.88 ?  29  LYS   A C    1 
ATOM   817  C  C    B LYS   A 1 29  ? 17.670 -0.216  19.754  0.44 22.33 ?  29  LYS   A C    1 
ATOM   818  O  O    A LYS   A 1 29  ? 18.479 -0.492  20.941  0.56 24.86 ?  29  LYS   A O    1 
ATOM   819  O  O    B LYS   A 1 29  ? 17.774 -0.502  20.953  0.44 22.37 ?  29  LYS   A O    1 
ATOM   820  C  CB   A LYS   A 1 29  ? 15.829 0.400   19.043  0.56 26.72 ?  29  LYS   A CB   1 
ATOM   821  C  CB   B LYS   A 1 29  ? 15.505 0.790   18.990  0.44 25.55 ?  29  LYS   A CB   1 
ATOM   822  C  CG   A LYS   A 1 29  ? 15.113 -0.311  20.185  0.56 29.28 ?  29  LYS   A CG   1 
ATOM   823  C  CG   B LYS   A 1 29  ? 14.703 0.182   20.129  0.44 27.81 ?  29  LYS   A CG   1 
ATOM   824  C  CD   A LYS   A 1 29  ? 14.741 0.658   21.295  0.56 31.62 ?  29  LYS   A CD   1 
ATOM   825  C  CD   B LYS   A 1 29  ? 14.607 1.131   21.311  0.44 29.78 ?  29  LYS   A CD   1 
ATOM   826  C  CE   A LYS   A 1 29  ? 13.859 -0.006  22.341  0.56 33.12 ?  29  LYS   A CE   1 
ATOM   827  C  CE   B LYS   A 1 29  ? 13.697 0.577   22.394  0.44 31.13 ?  29  LYS   A CE   1 
ATOM   828  N  NZ   A LYS   A 1 29  ? 13.377 0.969   23.357  0.56 33.91 ?  29  LYS   A NZ   1 
ATOM   829  N  NZ   B LYS   A 1 29  ? 13.604 1.500   23.556  0.44 31.89 ?  29  LYS   A NZ   1 
ATOM   830  H  H    A LYS   A 1 29  ? 17.455 1.388   17.486  0.56 27.71 ?  29  LYS   A H    1 
ATOM   831  H  H    B LYS   A 1 29  ? 17.272 1.510   17.423  0.44 26.70 ?  29  LYS   A H    1 
ATOM   832  H  HA   A LYS   A 1 29  ? 17.204 1.456   20.139  0.56 29.23 ?  29  LYS   A HA   1 
ATOM   833  H  HA   B LYS   A 1 29  ? 16.994 1.685   20.073  0.44 27.92 ?  29  LYS   A HA   1 
ATOM   834  H  HB2  A LYS   A 1 29  ? 15.301 1.176   18.805  0.56 32.08 ?  29  LYS   A HB2  1 
ATOM   835  H  HB2  B LYS   A 1 29  ? 15.078 1.626   18.748  0.44 30.69 ?  29  LYS   A HB2  1 
ATOM   836  H  HB3  A LYS   A 1 29  ? 15.868 -0.214  18.294  0.56 32.08 ?  29  LYS   A HB3  1 
ATOM   837  H  HB3  B LYS   A 1 29  ? 15.467 0.174   18.245  0.44 30.69 ?  29  LYS   A HB3  1 
ATOM   838  H  HG2  A LYS   A 1 29  ? 14.297 -0.711  19.847  0.56 35.15 ?  29  LYS   A HG2  1 
ATOM   839  H  HG2  B LYS   A 1 29  ? 13.804 -0.006  19.819  0.44 33.39 ?  29  LYS   A HG2  1 
ATOM   840  H  HG3  A LYS   A 1 29  ? 15.689 -0.997  20.559  0.56 35.15 ?  29  LYS   A HG3  1 
ATOM   841  H  HG3  B LYS   A 1 29  ? 15.132 -0.635  20.428  0.44 33.39 ?  29  LYS   A HG3  1 
ATOM   842  H  HD2  A LYS   A 1 29  ? 15.550 0.971   21.732  0.56 37.96 ?  29  LYS   A HD2  1 
ATOM   843  H  HD2  B LYS   A 1 29  ? 15.489 1.259   21.693  0.44 35.76 ?  29  LYS   A HD2  1 
ATOM   844  H  HD3  A LYS   A 1 29  ? 14.254 1.407   20.915  0.56 37.96 ?  29  LYS   A HD3  1 
ATOM   845  H  HD3  B LYS   A 1 29  ? 14.243 1.979   21.011  0.44 35.76 ?  29  LYS   A HD3  1 
ATOM   846  H  HE2  A LYS   A 1 29  ? 13.086 -0.397  21.904  0.56 39.76 ?  29  LYS   A HE2  1 
ATOM   847  H  HE2  B LYS   A 1 29  ? 12.806 0.453   22.031  0.44 37.38 ?  29  LYS   A HE2  1 
ATOM   848  H  HE3  A LYS   A 1 29  ? 14.368 -0.695  22.797  0.56 39.76 ?  29  LYS   A HE3  1 
ATOM   849  H  HE3  B LYS   A 1 29  ? 14.052 -0.272  22.706  0.44 37.38 ?  29  LYS   A HE3  1 
ATOM   850  H  HZ1  A LYS   A 1 29  ? 12.864 0.556   23.956  0.56 40.72 ?  29  LYS   A HZ1  1 
ATOM   851  H  HZ1  B LYS   A 1 29  ? 12.906 1.282   24.062  0.44 38.29 ?  29  LYS   A HZ1  1 
ATOM   852  H  HZ2  A LYS   A 1 29  ? 14.070 1.339   23.776  0.56 40.72 ?  29  LYS   A HZ2  1 
ATOM   853  H  HZ2  B LYS   A 1 29  ? 14.344 1.445   24.047  0.44 38.29 ?  29  LYS   A HZ2  1 
ATOM   854  H  HZ3  A LYS   A 1 29  ? 12.902 1.610   22.962  0.56 40.72 ?  29  LYS   A HZ3  1 
ATOM   855  H  HZ3  B LYS   A 1 29  ? 13.505 2.338   23.272  0.44 38.29 ?  29  LYS   A HZ3  1 
ATOM   856  N  N    A VAL   A 1 30  ? 18.388 -1.226  18.814  0.56 22.95 ?  30  VAL   A N    1 
ATOM   857  N  N    B VAL   A 1 30  ? 18.152 -0.997  18.791  0.44 21.80 ?  30  VAL   A N    1 
ATOM   858  C  CA   A VAL   A 1 30  ? 19.042 -2.496  19.119  0.56 22.46 ?  30  VAL   A CA   1 
ATOM   859  C  CA   B VAL   A 1 30  ? 18.798 -2.266  19.100  0.44 21.52 ?  30  VAL   A CA   1 
ATOM   860  C  C    A VAL   A 1 30  ? 20.542 -2.324  19.342  0.56 20.91 ?  30  VAL   A C    1 
ATOM   861  C  C    B VAL   A 1 30  ? 20.300 -2.107  19.313  0.44 20.89 ?  30  VAL   A C    1 
ATOM   862  O  O    A VAL   A 1 30  ? 21.136 -3.038  20.158  0.56 21.90 ?  30  VAL   A O    1 
ATOM   863  O  O    B VAL   A 1 30  ? 20.887 -2.826  20.127  0.44 21.21 ?  30  VAL   A O    1 
ATOM   864  C  CB   A VAL   A 1 30  ? 18.756 -3.508  17.995  0.56 23.51 ?  30  VAL   A CB   1 
ATOM   865  C  CB   B VAL   A 1 30  ? 18.502 -3.287  17.986  0.44 22.05 ?  30  VAL   A CB   1 
ATOM   866  C  CG1  A VAL   A 1 30  ? 19.560 -4.786  18.200  0.56 24.36 ?  30  VAL   A CG1  1 
ATOM   867  C  CG1  B VAL   A 1 30  ? 19.262 -4.582  18.227  0.44 22.63 ?  30  VAL   A CG1  1 
ATOM   868  C  CG2  A VAL   A 1 30  ? 17.268 -3.814  17.920  0.56 24.03 ?  30  VAL   A CG2  1 
ATOM   869  C  CG2  B VAL   A 1 30  ? 17.006 -3.550  17.894  0.44 22.33 ?  30  VAL   A CG2  1 
ATOM   870  H  H    A VAL   A 1 30  ? 18.210 -1.114  17.982  0.56 27.56 ?  30  VAL   A H    1 
ATOM   871  H  H    B VAL   A 1 30  ? 18.117 -0.815  17.952  0.44 26.18 ?  30  VAL   A H    1 
ATOM   872  H  HA   A VAL   A 1 30  ? 18.656 -2.852  19.933  0.56 26.97 ?  30  VAL   A HA   1 
ATOM   873  H  HA   B VAL   A 1 30  ? 18.418 -2.616  19.920  0.44 25.85 ?  30  VAL   A HA   1 
ATOM   874  H  HB   A VAL   A 1 30  ? 19.027 -3.123  17.146  0.56 28.24 ?  30  VAL   A HB   1 
ATOM   875  H  HB   B VAL   A 1 30  ? 18.799 -2.926  17.135  0.44 26.48 ?  30  VAL   A HB   1 
ATOM   876  H  HG11 A VAL   A 1 30  ? 19.193 -5.482  17.630  0.56 29.26 ?  30  VAL   A HG11 1 
ATOM   877  H  HG11 B VAL   A 1 30  ? 18.854 -5.290  17.702  0.44 27.18 ?  30  VAL   A HG11 1 
ATOM   878  H  HG12 A VAL   A 1 30  ? 20.486 -4.624  17.964  0.56 29.26 ?  30  VAL   A HG12 1 
ATOM   879  H  HG12 B VAL   A 1 30  ? 20.187 -4.465  17.957  0.44 27.18 ?  30  VAL   A HG12 1 
ATOM   880  H  HG13 A VAL   A 1 30  ? 19.493 -5.055  19.129  0.56 29.26 ?  30  VAL   A HG13 1 
ATOM   881  H  HG13 B VAL   A 1 30  ? 19.215 -4.802  19.169  0.44 27.18 ?  30  VAL   A HG13 1 
ATOM   882  H  HG21 A VAL   A 1 30  ? 17.116 -4.473  17.225  0.56 28.86 ?  30  VAL   A HG21 1 
ATOM   883  H  HG21 B VAL   A 1 30  ? 16.844 -4.222  17.213  0.44 26.82 ?  30  VAL   A HG21 1 
ATOM   884  H  HG22 A VAL   A 1 30  ? 16.975 -4.161  18.777  0.56 28.86 ?  30  VAL   A HG22 1 
ATOM   885  H  HG22 B VAL   A 1 30  ? 16.689 -3.868  18.754  0.44 26.82 ?  30  VAL   A HG22 1 
ATOM   886  H  HG23 A VAL   A 1 30  ? 16.790 -2.997  17.712  0.56 28.86 ?  30  VAL   A HG23 1 
ATOM   887  H  HG23 B VAL   A 1 30  ? 16.556 -2.725  17.658  0.44 26.82 ?  30  VAL   A HG23 1 
ATOM   888  N  N    A LYS   A 1 31  ? 21.175 -1.397  18.633  0.56 19.88 ?  31  LYS   A N    1 
ATOM   889  N  N    B LYS   A 1 31  ? 20.929 -1.173  18.608  0.44 20.94 ?  31  LYS   A N    1 
ATOM   890  C  CA   A LYS   A 1 31  ? 22.629 -1.289  18.582  0.56 20.02 ?  31  LYS   A CA   1 
ATOM   891  C  CA   B LYS   A 1 31  ? 22.382 -1.055  18.559  0.44 21.29 ?  31  LYS   A CA   1 
ATOM   892  C  C    A LYS   A 1 31  ? 23.246 -2.650  18.246  0.56 17.57 ?  31  LYS   A C    1 
ATOM   893  C  C    B LYS   A 1 31  ? 23.010 -2.424  18.293  0.44 19.45 ?  31  LYS   A C    1 
ATOM   894  O  O    A LYS   A 1 31  ? 24.014 -3.206  19.038  0.56 18.36 ?  31  LYS   A O    1 
ATOM   895  O  O    B LYS   A 1 31  ? 23.754 -2.948  19.130  0.44 20.32 ?  31  LYS   A O    1 
ATOM   896  C  CB   A LYS   A 1 31  ? 23.210 -0.729  19.873  0.56 24.33 ?  31  LYS   A CB   1 
ATOM   897  C  CB   B LYS   A 1 31  ? 22.948 -0.428  19.825  0.44 24.42 ?  31  LYS   A CB   1 
ATOM   898  C  CG   A LYS   A 1 31  ? 22.522 0.533   20.368  0.56 28.84 ?  31  LYS   A CG   1 
ATOM   899  C  CG   B LYS   A 1 31  ? 22.264 0.866   20.224  0.44 27.95 ?  31  LYS   A CG   1 
ATOM   900  C  CD   A LYS   A 1 31  ? 23.529 1.590   20.798  0.56 32.31 ?  31  LYS   A CD   1 
ATOM   901  C  CD   B LYS   A 1 31  ? 23.233 1.816   20.902  0.44 30.70 ?  31  LYS   A CD   1 
ATOM   902  C  CE   A LYS   A 1 31  ? 22.890 2.634   21.704  0.56 34.62 ?  31  LYS   A CE   1 
ATOM   903  C  CE   B LYS   A 1 31  ? 22.497 2.861   21.723  0.44 32.78 ?  31  LYS   A CE   1 
ATOM   904  N  NZ   A LYS   A 1 31  ? 21.692 3.273   21.093  0.56 35.78 ?  31  LYS   A NZ   1 
ATOM   905  N  NZ   B LYS   A 1 31  ? 21.395 3.509   20.961  0.44 33.94 ?  31  LYS   A NZ   1 
ATOM   906  H  H    A LYS   A 1 31  ? 20.771 -0.809  18.158  0.56 23.88 ?  31  LYS   A H    1 
ATOM   907  H  H    B LYS   A 1 31  ? 20.520 -0.584  18.137  0.44 25.15 ?  31  LYS   A H    1 
ATOM   908  H  HA   A LYS   A 1 31  ? 22.858 -0.676  17.871  0.56 24.05 ?  31  LYS   A HA   1 
ATOM   909  H  HA   B LYS   A 1 31  ? 22.610 -0.474  17.822  0.44 25.57 ?  31  LYS   A HA   1 
ATOM   910  H  HB2  A LYS   A 1 31  ? 23.134 -1.402  20.563  0.56 29.22 ?  31  LYS   A HB2  1 
ATOM   911  H  HB2  B LYS   A 1 31  ? 22.850 -1.053  20.557  0.44 29.33 ?  31  LYS   A HB2  1 
ATOM   912  H  HB3  A LYS   A 1 31  ? 24.146 -0.516  19.722  0.56 29.22 ?  31  LYS   A HB3  1 
ATOM   913  H  HB3  B LYS   A 1 31  ? 23.890 -0.234  19.681  0.44 29.33 ?  31  LYS   A HB3  1 
ATOM   914  H  HG2  A LYS   A 1 31  ? 21.980 0.904   19.654  0.56 34.63 ?  31  LYS   A HG2  1 
ATOM   915  H  HG2  B LYS   A 1 31  ? 21.913 1.302   19.432  0.44 33.57 ?  31  LYS   A HG2  1 
ATOM   916  H  HG3  A LYS   A 1 31  ? 21.967 0.316   21.133  0.56 34.63 ?  31  LYS   A HG3  1 
ATOM   917  H  HG3  B LYS   A 1 31  ? 21.545 0.669   20.846  0.44 33.57 ?  31  LYS   A HG3  1 
ATOM   918  H  HD2  A LYS   A 1 31  ? 24.252 1.166   21.286  0.56 38.79 ?  31  LYS   A HD2  1 
ATOM   919  H  HD2  B LYS   A 1 31  ? 23.813 1.312   21.495  0.44 36.87 ?  31  LYS   A HD2  1 
ATOM   920  H  HD3  A LYS   A 1 31  ? 23.876 2.042   20.011  0.56 38.79 ?  31  LYS   A HD3  1 
ATOM   921  H  HD3  B LYS   A 1 31  ? 23.760 2.272   20.226  0.44 36.87 ?  31  LYS   A HD3  1 
ATOM   922  H  HE2  A LYS   A 1 31  ? 22.614 2.209   22.531  0.56 41.57 ?  31  LYS   A HE2  1 
ATOM   923  H  HE2  B LYS   A 1 31  ? 22.114 2.435   22.505  0.44 39.36 ?  31  LYS   A HE2  1 
ATOM   924  H  HE3  A LYS   A 1 31  ? 23.538 3.332   21.890  0.56 41.57 ?  31  LYS   A HE3  1 
ATOM   925  H  HE3  B LYS   A 1 31  ? 23.124 3.550   21.991  0.44 39.36 ?  31  LYS   A HE3  1 
ATOM   926  H  HZ1  A LYS   A 1 31  ? 21.360 3.888   21.644  0.56 42.95 ?  31  LYS   A HZ1  1 
ATOM   927  H  HZ1  B LYS   A 1 31  ? 21.032 4.159   21.448  0.44 40.75 ?  31  LYS   A HZ1  1 
ATOM   928  H  HZ2  A LYS   A 1 31  ? 21.913 3.663   20.324  0.56 42.95 ?  31  LYS   A HZ2  1 
ATOM   929  H  HZ2  B LYS   A 1 31  ? 21.711 3.855   20.205  0.44 40.75 ?  31  LYS   A HZ2  1 
ATOM   930  H  HZ3  A LYS   A 1 31  ? 21.066 2.659   20.936  0.56 42.95 ?  31  LYS   A HZ3  1 
ATOM   931  H  HZ3  B LYS   A 1 31  ? 20.767 2.909   20.764  0.44 40.75 ?  31  LYS   A HZ3  1 
ATOM   932  N  N    A PRO   A 1 32  ? 22.928 -3.206  17.081  0.56 16.11 ?  32  PRO   A N    1 
ATOM   933  N  N    B PRO   A 1 32  ? 22.729 -3.024  17.140  0.44 17.26 ?  32  PRO   A N    1 
ATOM   934  C  CA   A PRO   A 1 32  ? 23.411 -4.547  16.746  0.56 16.67 ?  32  PRO   A CA   1 
ATOM   935  C  CA   B PRO   A 1 32  ? 23.217 -4.377  16.869  0.44 16.74 ?  32  PRO   A CA   1 
ATOM   936  C  C    A PRO   A 1 32  ? 24.914 -4.564  16.535  0.56 16.61 ?  32  PRO   A C    1 
ATOM   937  C  C    B PRO   A 1 32  ? 24.724 -4.383  16.670  0.44 16.17 ?  32  PRO   A C    1 
ATOM   938  O  O    A PRO   A 1 32  ? 25.553 -3.540  16.280  0.56 16.20 ?  32  PRO   A O    1 
ATOM   939  O  O    B PRO   A 1 32  ? 25.378 -3.344  16.560  0.44 16.37 ?  32  PRO   A O    1 
ATOM   940  C  CB   A PRO   A 1 32  ? 22.688 -4.854  15.432  0.56 16.80 ?  32  PRO   A CB   1 
ATOM   941  C  CB   B PRO   A 1 32  ? 22.494 -4.742  15.572  0.44 16.69 ?  32  PRO   A CB   1 
ATOM   942  C  CG   A PRO   A 1 32  ? 22.509 -3.507  14.805  0.56 15.92 ?  32  PRO   A CG   1 
ATOM   943  C  CG   B PRO   A 1 32  ? 22.345 -3.432  14.871  0.44 16.45 ?  32  PRO   A CG   1 
ATOM   944  C  CD   A PRO   A 1 32  ? 22.209 -2.588  15.956  0.56 15.48 ?  32  PRO   A CD   1 
ATOM   945  C  CD   B PRO   A 1 32  ? 22.054 -2.441  15.968  0.44 16.47 ?  32  PRO   A CD   1 
ATOM   946  H  HA   A PRO   A 1 32  ? 23.154 -5.191  17.427  0.56 20.02 ?  32  PRO   A HA   1 
ATOM   947  H  HA   B PRO   A 1 32  ? 22.962 -4.992  17.576  0.44 20.11 ?  32  PRO   A HA   1 
ATOM   948  H  HB2  A PRO   A 1 32  ? 23.243 -5.429  14.876  0.56 20.18 ?  32  PRO   A HB2  1 
ATOM   949  H  HB2  B PRO   A 1 32  ? 23.034 -5.356  15.049  0.44 20.05 ?  32  PRO   A HB2  1 
ATOM   950  H  HB3  A PRO   A 1 32  ? 21.832 -5.274  15.613  0.56 20.18 ?  32  PRO   A HB3  1 
ATOM   951  H  HB3  B PRO   A 1 32  ? 21.624 -5.129  15.769  0.44 20.05 ?  32  PRO   A HB3  1 
ATOM   952  H  HG2  A PRO   A 1 32  ? 23.327 -3.248  14.355  0.56 19.12 ?  32  PRO   A HG2  1 
ATOM   953  H  HG2  B PRO   A 1 32  ? 23.173 -3.211  14.416  0.44 19.76 ?  32  PRO   A HG2  1 
ATOM   954  H  HG3  A PRO   A 1 32  ? 21.767 -3.538  14.180  0.56 19.12 ?  32  PRO   A HG3  1 
ATOM   955  H  HG3  B PRO   A 1 32  ? 21.608 -3.479  14.241  0.44 19.76 ?  32  PRO   A HG3  1 
ATOM   956  H  HD2  A PRO   A 1 32  ? 22.556 -1.702  15.769  0.56 18.60 ?  32  PRO   A HD2  1 
ATOM   957  H  HD2  B PRO   A 1 32  ? 22.437 -1.578  15.745  0.44 19.79 ?  32  PRO   A HD2  1 
ATOM   958  H  HD3  A PRO   A 1 32  ? 21.256 -2.571  16.127  0.56 18.60 ?  32  PRO   A HD3  1 
ATOM   959  H  HD3  B PRO   A 1 32  ? 21.097 -2.379  16.116  0.44 19.79 ?  32  PRO   A HD3  1 
ATOM   960  N  N    A THR   A 1 33  ? 25.471 -5.773  16.615  0.56 16.76 ?  33  THR   A N    1 
ATOM   961  N  N    B THR   A 1 33  ? 25.272 -5.596  16.613  0.44 15.98 ?  33  THR   A N    1 
ATOM   962  C  CA   A THR   A 1 33  ? 26.880 -5.950  16.290  0.56 17.11 ?  33  THR   A CA   1 
ATOM   963  C  CA   B THR   A 1 33  ? 26.695 -5.745  16.332  0.44 15.63 ?  33  THR   A CA   1 
ATOM   964  C  C    A THR   A 1 33  ? 27.168 -5.501  14.862  0.56 15.66 ?  33  THR   A C    1 
ATOM   965  C  C    B THR   A 1 33  ? 27.023 -5.295  14.914  0.44 14.52 ?  33  THR   A C    1 
ATOM   966  O  O    A THR   A 1 33  ? 28.231 -4.927  14.589  0.56 15.62 ?  33  THR   A O    1 
ATOM   967  O  O    B THR   A 1 33  ? 27.996 -4.563  14.693  0.44 14.53 ?  33  THR   A O    1 
ATOM   968  C  CB   A THR   A 1 33  ? 27.283 -7.412  16.502  0.56 19.08 ?  33  THR   A CB   1 
ATOM   969  C  CB   B THR   A 1 33  ? 27.110 -7.199  16.548  0.44 17.04 ?  33  THR   A CB   1 
ATOM   970  O  OG1  A THR   A 1 33  ? 27.039 -7.789  17.863  0.56 20.92 ?  33  THR   A OG1  1 
ATOM   971  O  OG1  B THR   A 1 33  ? 26.794 -7.586  17.891  0.44 18.48 ?  33  THR   A OG1  1 
ATOM   972  C  CG2  A THR   A 1 33  ? 28.756 -7.618  16.198  0.56 19.74 ?  33  THR   A CG2  1 
ATOM   973  C  CG2  B THR   A 1 33  ? 28.606 -7.374  16.303  0.44 17.90 ?  33  THR   A CG2  1 
ATOM   974  H  H    A THR   A 1 33  ? 25.060 -6.495  16.841  0.56 20.13 ?  33  THR   A H    1 
ATOM   975  H  H    B THR   A 1 33  ? 24.847 -6.335  16.740  0.44 19.20 ?  33  THR   A H    1 
ATOM   976  H  HA   A THR   A 1 33  ? 27.413 -5.403  16.887  0.56 20.56 ?  33  THR   A HA   1 
ATOM   977  H  HA   B THR   A 1 33  ? 27.197 -5.195  16.954  0.44 18.78 ?  33  THR   A HA   1 
ATOM   978  H  HB   A THR   A 1 33  ? 26.760 -7.980  15.912  0.56 22.92 ?  33  THR   A HB   1 
ATOM   979  H  HB   B THR   A 1 33  ? 26.629 -7.771  15.927  0.44 20.47 ?  33  THR   A HB   1 
ATOM   980  H  HG1  A THR   A 1 33  ? 27.476 -7.292  18.381  0.56 25.12 ?  33  THR   A HG1  1 
ATOM   981  H  HG1  B THR   A 1 33  ? 27.224 -7.109  18.434  0.44 22.19 ?  33  THR   A HG1  1 
ATOM   982  H  HG21 A THR   A 1 33  ? 29.033 -8.498  16.499  0.56 23.71 ?  33  THR   A HG21 1 
ATOM   983  H  HG21 B THR   A 1 33  ? 28.892 -8.249  16.606  0.44 21.51 ?  33  THR   A HG21 1 
ATOM   984  H  HG22 A THR   A 1 33  ? 28.914 -7.546  15.246  0.56 23.71 ?  33  THR   A HG22 1 
ATOM   985  H  HG22 B THR   A 1 33  ? 28.800 -7.293  15.354  0.44 21.51 ?  33  THR   A HG22 1 
ATOM   986  H  HG23 A THR   A 1 33  ? 29.284 -6.949  16.661  0.56 23.71 ?  33  THR   A HG23 1 
ATOM   987  H  HG23 B THR   A 1 33  ? 29.102 -6.695  16.785  0.44 21.51 ?  33  THR   A HG23 1 
ATOM   988  N  N    . VAL   A 1 34  ? 26.227 -5.735  13.942  1.00 14.01 ?  34  VAL   A N    1 
ATOM   989  C  CA   . VAL   A 1 34  ? 26.420 -5.411  12.531  1.00 13.21 ?  34  VAL   A CA   1 
ATOM   990  C  C    . VAL   A 1 34  ? 25.122 -4.861  11.958  1.00 12.80 ?  34  VAL   A C    1 
ATOM   991  O  O    . VAL   A 1 34  ? 24.089 -5.540  11.990  1.00 13.44 ?  34  VAL   A O    1 
ATOM   992  C  CB   . VAL   A 1 34  ? 26.871 -6.623  11.697  1.00 13.54 ?  34  VAL   A CB   1 
ATOM   993  C  CG1  . VAL   A 1 34  ? 27.041 -6.223  10.234  1.00 14.16 ?  34  VAL   A CG1  1 
ATOM   994  C  CG2  . VAL   A 1 34  ? 28.148 -7.237  12.254  1.00 14.92 ?  34  VAL   A CG2  1 
ATOM   995  H  H    A VAL   A 1 34  ? 25.459 -6.087  14.117  0.56 16.84 ?  34  VAL   A H    1 
ATOM   996  H  H    B VAL   A 1 34  ? 25.547 -6.248  14.082  0.44 16.84 ?  34  VAL   A H    1 
ATOM   997  H  HA   . VAL   A 1 34  ? 27.097 -4.720  12.452  1.00 15.87 ?  34  VAL   A HA   1 
ATOM   998  H  HB   . VAL   A 1 34  ? 26.174 -7.298  11.745  1.00 16.27 ?  34  VAL   A HB   1 
ATOM   999  H  HG11 . VAL   A 1 34  ? 27.542 -6.916  9.778   1.00 17.01 ?  34  VAL   A HG11 1 
ATOM   1000 H  HG12 . VAL   A 1 34  ? 26.165 -6.127  9.825   1.00 17.01 ?  34  VAL   A HG12 1 
ATOM   1001 H  HG13 . VAL   A 1 34  ? 27.522 -5.383  10.189  1.00 17.01 ?  34  VAL   A HG13 1 
ATOM   1002 H  HG21 . VAL   A 1 34  ? 28.431 -7.954  11.666  1.00 17.92 ?  34  VAL   A HG21 1 
ATOM   1003 H  HG22 . VAL   A 1 34  ? 28.833 -6.553  12.297  1.00 17.92 ?  34  VAL   A HG22 1 
ATOM   1004 H  HG23 . VAL   A 1 34  ? 27.972 -7.587  13.142  1.00 17.92 ?  34  VAL   A HG23 1 
ATOM   1005 N  N    . VAL   A 1 35  ? 25.189 -3.655  11.392  1.00 11.96 ?  35  VAL   A N    1 
ATOM   1006 C  CA   . VAL   A 1 35  ? 24.161 -3.144  10.493  1.00 11.78 ?  35  VAL   A CA   1 
ATOM   1007 C  C    . VAL   A 1 35  ? 24.716 -3.149  9.074   1.00 11.01 ?  35  VAL   A C    1 
ATOM   1008 O  O    . VAL   A 1 35  ? 25.863 -2.745  8.850   1.00 11.68 ?  35  VAL   A O    1 
ATOM   1009 C  CB   . VAL   A 1 35  ? 23.641 -1.749  10.904  1.00 12.46 ?  35  VAL   A CB   1 
ATOM   1010 C  CG1  . VAL   A 1 35  ? 24.703 -0.662  10.756  1.00 13.11 ?  35  VAL   A CG1  1 
ATOM   1011 C  CG2  . VAL   A 1 35  ? 22.396 -1.394  10.091  1.00 13.02 ?  35  VAL   A CG2  1 
ATOM   1012 H  H    . VAL   A 1 35  ? 25.835 -3.101  11.510  1.00 14.38 ?  35  VAL   A H    1 
ATOM   1013 H  HA   . VAL   A 1 35  ? 23.402 -3.750  10.511  1.00 14.15 ?  35  VAL   A HA   1 
ATOM   1014 H  HB   . VAL   A 1 35  ? 23.374 -1.777  11.834  1.00 14.97 ?  35  VAL   A HB   1 
ATOM   1015 H  HG11 . VAL   A 1 35  ? 24.364 0.164   11.136  1.00 15.76 ?  35  VAL   A HG11 1 
ATOM   1016 H  HG12 . VAL   A 1 35  ? 25.502 -0.941  11.222  1.00 15.76 ?  35  VAL   A HG12 1 
ATOM   1017 H  HG13 . VAL   A 1 35  ? 24.895 -0.533  9.812   1.00 15.76 ?  35  VAL   A HG13 1 
ATOM   1018 H  HG21 . VAL   A 1 35  ? 22.048 -0.545  10.401  1.00 15.65 ?  35  VAL   A HG21 1 
ATOM   1019 H  HG22 . VAL   A 1 35  ? 22.638 -1.332  9.154   1.00 15.65 ?  35  VAL   A HG22 1 
ATOM   1020 H  HG23 . VAL   A 1 35  ? 21.730 -2.091  10.216  1.00 15.65 ?  35  VAL   A HG23 1 
ATOM   1021 N  N    . VAL   A 1 36  ? 23.913 -3.622  8.121   1.00 10.35 ?  36  VAL   A N    1 
ATOM   1022 C  CA   . VAL   A 1 36  ? 24.293 -3.624  6.714   1.00 10.26 ?  36  VAL   A CA   1 
ATOM   1023 C  C    . VAL   A 1 36  ? 23.840 -2.331  6.056   1.00 10.50 ?  36  VAL   A C    1 
ATOM   1024 O  O    . VAL   A 1 36  ? 22.679 -1.925  6.196   1.00 11.07 ?  36  VAL   A O    1 
ATOM   1025 C  CB   . VAL   A 1 36  ? 23.692 -4.839  5.988   1.00 10.36 ?  36  VAL   A CB   1 
ATOM   1026 C  CG1  . VAL   A 1 36  ? 23.943 -4.763  4.497   1.00 11.05 ?  36  VAL   A CG1  1 
ATOM   1027 C  CG2  . VAL   A 1 36  ? 24.245 -6.133  6.562   1.00 11.32 ?  36  VAL   A CG2  1 
ATOM   1028 H  H    . VAL   A 1 36  ? 23.124 -3.952  8.267   1.00 12.44 ?  36  VAL   A H    1 
ATOM   1029 H  HA   . VAL   A 1 36  ? 25.259 -3.685  6.647   1.00 12.34 ?  36  VAL   A HA   1 
ATOM   1030 H  HB   . VAL   A 1 36  ? 22.730 -4.841  6.124   1.00 12.45 ?  36  VAL   A HB   1 
ATOM   1031 H  HG11 . VAL   A 1 36  ? 23.794 -5.636  4.105   1.00 13.29 ?  36  VAL   A HG11 1 
ATOM   1032 H  HG12 . VAL   A 1 36  ? 23.336 -4.116  4.102   1.00 13.29 ?  36  VAL   A HG12 1 
ATOM   1033 H  HG13 . VAL   A 1 36  ? 24.863 -4.487  4.347   1.00 13.29 ?  36  VAL   A HG13 1 
ATOM   1034 H  HG21 . VAL   A 1 36  ? 23.860 -6.887  6.080   1.00 13.60 ?  36  VAL   A HG21 1 
ATOM   1035 H  HG22 . VAL   A 1 36  ? 25.210 -6.140  6.461   1.00 13.60 ?  36  VAL   A HG22 1 
ATOM   1036 H  HG23 . VAL   A 1 36  ? 24.011 -6.193  7.502   1.00 13.60 ?  36  VAL   A HG23 1 
ATOM   1037 N  N    . ASN   A 1 37  ? 24.759 -1.699  5.323   1.00 9.76  ?  37  ASN   A N    1 
ATOM   1038 C  CA   . ASN   A 1 37  ? 24.433 -0.588  4.446   1.00 9.74  ?  37  ASN   A CA   1 
ATOM   1039 C  C    . ASN   A 1 37  ? 24.309 -1.072  3.011   1.00 9.61  ?  37  ASN   A C    1 
ATOM   1040 O  O    . ASN   A 1 37  ? 25.104 -1.895  2.545   1.00 10.24 ?  37  ASN   A O    1 
ATOM   1041 C  CB   . ASN   A 1 37  ? 25.512 0.490   4.523   1.00 10.39 ?  37  ASN   A CB   1 
ATOM   1042 C  CG   . ASN   A 1 37  ? 25.191 1.681   3.666   1.00 10.21 ?  37  ASN   A CG   1 
ATOM   1043 O  OD1  . ASN   A 1 37  ? 24.015 2.014   3.475   1.00 10.97 ?  37  ASN   A OD1  1 
ATOM   1044 N  ND2  . ASN   A 1 37  ? 26.224 2.337   3.144   1.00 10.65 ?  37  ASN   A ND2  1 
ATOM   1045 H  H    . ASN   A 1 37  ? 25.599 -1.897  5.332   1.00 11.74 ?  37  ASN   A H    1 
ATOM   1046 H  HA   . ASN   A 1 37  ? 23.593 -0.194  4.719   1.00 11.71 ?  37  ASN   A HA   1 
ATOM   1047 H  HB2  . ASN   A 1 37  ? 25.594 0.797   5.442   1.00 12.49 ?  37  ASN   A HB2  1 
ATOM   1048 H  HB3  . ASN   A 1 37  ? 26.359 0.121   4.222   1.00 12.49 ?  37  ASN   A HB3  1 
ATOM   1049 H  HD21 . ASN   A 1 37  ? 26.084 3.020   2.643   1.00 12.80 ?  37  ASN   A HD21 1 
ATOM   1050 H  HD22 . ASN   A 1 37  ? 27.020 2.073   3.296   1.00 12.80 ?  37  ASN   A HD22 1 
ATOM   1051 N  N    . ALA   A 1 38  ? 23.302 -0.547  2.315   1.00 10.20 ?  38  ALA   A N    1 
ATOM   1052 C  CA   . ALA   A 1 38  ? 23.127 -0.738  0.879   1.00 10.58 ?  38  ALA   A CA   1 
ATOM   1053 C  C    . ALA   A 1 38  ? 24.014 0.272   0.148   1.00 10.57 ?  38  ALA   A C    1 
ATOM   1054 O  O    . ALA   A 1 38  ? 23.580 1.352   -0.270  1.00 10.96 ?  38  ALA   A O    1 
ATOM   1055 C  CB   . ALA   A 1 38  ? 21.658 -0.572  0.509   1.00 12.30 ?  38  ALA   A CB   1 
ATOM   1056 H  H    . ALA   A 1 38  ? 22.696 -0.052  2.676   1.00 12.27 ?  38  ALA   A H    1 
ATOM   1057 H  HA   . ALA   A 1 38  ? 23.409 -1.632  0.639   1.00 12.72 ?  38  ALA   A HA   1 
ATOM   1058 H  HB1  . ALA   A 1 38  ? 21.559 -0.697  -0.446  1.00 14.79 ?  38  ALA   A HB1  1 
ATOM   1059 H  HB2  . ALA   A 1 38  ? 21.131 -1.233  0.987   1.00 14.79 ?  38  ALA   A HB2  1 
ATOM   1060 H  HB3  . ALA   A 1 38  ? 21.369 0.321   0.754   1.00 14.79 ?  38  ALA   A HB3  1 
ATOM   1061 N  N    . ALA   A 1 39  ? 25.290 -0.080  0.017   1.00 10.73 ?  39  ALA   A N    1 
ATOM   1062 C  CA   . ALA   A 1 39  ? 26.314 0.823   -0.475  1.00 10.44 ?  39  ALA   A CA   1 
ATOM   1063 C  C    . ALA   A 1 39  ? 26.445 0.765   -1.993  1.00 10.51 ?  39  ALA   A C    1 
ATOM   1064 O  O    . ALA   A 1 39  ? 25.975 -0.166  -2.655  1.00 10.75 ?  39  ALA   A O    1 
ATOM   1065 C  CB   . ALA   A 1 39  ? 27.652 0.485   0.190   1.00 11.35 ?  39  ALA   A CB   1 
ATOM   1066 H  H    . ALA   A 1 39  ? 25.592 -0.864  0.229   1.00 12.90 ?  39  ALA   A H    1 
ATOM   1067 H  HA   . ALA   A 1 39  ? 26.072 1.730   -0.221  1.00 12.54 ?  39  ALA   A HA   1 
ATOM   1068 H  HB1  . ALA   A 1 39  ? 28.326 1.100   -0.141  1.00 13.65 ?  39  ALA   A HB1  1 
ATOM   1069 H  HB2  . ALA   A 1 39  ? 27.561 0.592   1.156   1.00 13.65 ?  39  ALA   A HB2  1 
ATOM   1070 H  HB3  . ALA   A 1 39  ? 27.891 -0.423  -0.021  1.00 13.65 ?  39  ALA   A HB3  1 
ATOM   1071 N  N    . ASN   A 1 40  ? 27.116 1.780   -2.542  1.00 11.09 ?  40  ASN   A N    1 
ATOM   1072 C  CA   . ASN   A 1 40  ? 27.659 1.731   -3.894  1.00 11.01 ?  40  ASN   A CA   1 
ATOM   1073 C  C    . ASN   A 1 40  ? 29.183 1.610   -3.817  1.00 10.49 ?  40  ASN   A C    1 
ATOM   1074 O  O    . ASN   A 1 40  ? 29.773 1.699   -2.740  1.00 10.79 ?  40  ASN   A O    1 
ATOM   1075 C  CB   . ASN   A 1 40  ? 27.206 2.930   -4.749  1.00 11.97 ?  40  ASN   A CB   1 
ATOM   1076 C  CG   . ASN   A 1 40  ? 27.574 4.267   -4.143  1.00 12.59 ?  40  ASN   A CG   1 
ATOM   1077 O  OD1  . ASN   A 1 40  ? 28.744 4.530   -3.855  1.00 12.99 ?  40  ASN   A OD1  1 
ATOM   1078 N  ND2  . ASN   A 1 40  ? 26.577 5.127   -3.968  1.00 13.60 ?  40  ASN   A ND2  1 
ATOM   1079 H  H    . ASN   A 1 40  ? 27.283 2.516   -2.134  1.00 13.33 ?  40  ASN   A H    1 
ATOM   1080 H  HA   . ASN   A 1 40  ? 27.325 0.927   -4.327  1.00 13.24 ?  40  ASN   A HA   1 
ATOM   1081 H  HB2  . ASN   A 1 40  ? 27.625 2.868   -5.621  1.00 14.39 ?  40  ASN   A HB2  1 
ATOM   1082 H  HB3  . ASN   A 1 40  ? 26.241 2.897   -4.843  1.00 14.39 ?  40  ASN   A HB3  1 
ATOM   1083 H  HD21 . ASN   A 1 40  ? 26.735 5.906   -3.635  1.00 16.34 ?  40  ASN   A HD21 1 
ATOM   1084 H  HD22 . ASN   A 1 40  ? 25.774 4.910   -4.185  1.00 16.34 ?  40  ASN   A HD22 1 
ATOM   1085 N  N    . VAL   A 1 41  ? 29.807 1.361   -4.972  1.00 11.11 ?  41  VAL   A N    1 
ATOM   1086 C  CA   . VAL   A 1 41  ? 31.233 1.044   -4.992  1.00 11.88 ?  41  VAL   A CA   1 
ATOM   1087 C  C    . VAL   A 1 41  ? 32.098 2.190   -4.500  1.00 11.77 ?  41  VAL   A C    1 
ATOM   1088 O  O    . VAL   A 1 41  ? 33.243 1.964   -4.090  1.00 12.05 ?  41  VAL   A O    1 
ATOM   1089 C  CB   . VAL   A 1 41  ? 31.725 0.566   -6.380  1.00 12.94 ?  41  VAL   A CB   1 
ATOM   1090 C  CG1  . VAL   A 1 41  ? 31.033 -0.727  -6.790  1.00 13.66 ?  41  VAL   A CG1  1 
ATOM   1091 C  CG2  . VAL   A 1 41  ? 31.574 1.647   -7.437  1.00 13.65 ?  41  VAL   A CG2  1 
ATOM   1092 H  H    . VAL   A 1 41  ? 29.431 1.352   -5.744  1.00 13.36 ?  41  VAL   A H    1 
ATOM   1093 H  HA   . VAL   A 1 41  ? 31.386 0.300   -4.385  1.00 14.28 ?  41  VAL   A HA   1 
ATOM   1094 H  HB   . VAL   A 1 41  ? 32.673 0.363   -6.316  1.00 15.56 ?  41  VAL   A HB   1 
ATOM   1095 H  HG11 . VAL   A 1 41  ? 31.370 -1.013  -7.654  1.00 16.41 ?  41  VAL   A HG11 1 
ATOM   1096 H  HG12 . VAL   A 1 41  ? 31.212 -1.410  -6.124  1.00 16.41 ?  41  VAL   A HG12 1 
ATOM   1097 H  HG13 . VAL   A 1 41  ? 30.075 -0.569  -6.848  1.00 16.41 ?  41  VAL   A HG13 1 
ATOM   1098 H  HG21 . VAL   A 1 41  ? 31.801 1.273   -8.306  1.00 16.41 ?  41  VAL   A HG21 1 
ATOM   1099 H  HG22 . VAL   A 1 41  ? 30.658 1.958   -7.442  1.00 16.41 ?  41  VAL   A HG22 1 
ATOM   1100 H  HG23 . VAL   A 1 41  ? 32.175 2.378   -7.228  1.00 16.41 ?  41  VAL   A HG23 1 
ATOM   1101 N  N    . TYR   A 1 42  ? 31.592 3.421   -4.559  1.00 11.57 ?  42  TYR   A N    1 
ATOM   1102 C  CA   . TYR   A 1 42  ? 32.328 4.606   -4.143  1.00 11.53 ?  42  TYR   A CA   1 
ATOM   1103 C  C    . TYR   A 1 42  ? 32.061 4.986   -2.698  1.00 10.98 ?  42  TYR   A C    1 
ATOM   1104 O  O    . TYR   A 1 42  ? 32.624 5.976   -2.213  1.00 11.79 ?  42  TYR   A O    1 
ATOM   1105 C  CB   . TYR   A 1 42  ? 31.978 5.795   -5.057  1.00 12.10 ?  42  TYR   A CB   1 
ATOM   1106 C  CG   . TYR   A 1 42  ? 32.148 5.482   -6.528  1.00 12.83 ?  42  TYR   A CG   1 
ATOM   1107 C  CD1  . TYR   A 1 42  ? 33.408 5.301   -7.081  1.00 13.42 ?  42  TYR   A CD1  1 
ATOM   1108 C  CD2  . TYR   A 1 42  ? 31.048 5.356   -7.365  1.00 14.28 ?  42  TYR   A CD2  1 
ATOM   1109 C  CE1  . TYR   A 1 42  ? 33.564 4.995   -8.423  1.00 14.02 ?  42  TYR   A CE1  1 
ATOM   1110 C  CE2  . TYR   A 1 42  ? 31.200 5.067   -8.711  1.00 15.48 ?  42  TYR   A CE2  1 
ATOM   1111 C  CZ   . TYR   A 1 42  ? 32.461 4.882   -9.234  1.00 15.37 ?  42  TYR   A CZ   1 
ATOM   1112 O  OH   . TYR   A 1 42  ? 32.611 4.581   -10.564 1.00 16.94 ?  42  TYR   A OH   1 
ATOM   1113 H  H    . TYR   A 1 42  ? 30.800 3.592   -4.843  1.00 13.91 ?  42  TYR   A H    1 
ATOM   1114 H  HA   . TYR   A 1 42  ? 33.279 4.436   -4.238  1.00 13.85 ?  42  TYR   A HA   1 
ATOM   1115 H  HB2  . TYR   A 1 42  ? 31.048 6.037   -4.909  1.00 14.54 ?  42  TYR   A HB2  1 
ATOM   1116 H  HB3  . TYR   A 1 42  ? 32.554 6.540   -4.841  1.00 14.54 ?  42  TYR   A HB3  1 
ATOM   1117 H  HD1  . TYR   A 1 42  ? 34.159 5.368   -6.536  1.00 16.13 ?  42  TYR   A HD1  1 
ATOM   1118 H  HD2  . TYR   A 1 42  ? 30.194 5.478   -7.016  1.00 17.15 ?  42  TYR   A HD2  1 
ATOM   1119 H  HE1  . TYR   A 1 42  ? 34.418 4.874   -8.778  1.00 16.84 ?  42  TYR   A HE1  1 
ATOM   1120 H  HE2  . TYR   A 1 42  ? 30.449 4.985   -9.258  1.00 18.59 ?  42  TYR   A HE2  1 
ATOM   1121 H  HH   . TYR   A 1 42  ? 33.431 4.492   -10.748 1.00 20.35 ?  42  TYR   A HH   1 
ATOM   1122 N  N    . LEU   A 1 43  ? 31.207 4.232   -2.010  1.00 10.90 ?  43  LEU   A N    1 
ATOM   1123 C  CA   . LEU   A 1 43  ? 30.759 4.576   -0.664  1.00 10.53 ?  43  LEU   A CA   1 
ATOM   1124 C  C    . LEU   A 1 43  ? 30.278 6.021   -0.580  1.00 10.81 ?  43  LEU   A C    1 
ATOM   1125 O  O    . LEU   A 1 43  ? 30.529 6.727   0.398   1.00 11.84 ?  43  LEU   A O    1 
ATOM   1126 C  CB   . LEU   A 1 43  ? 31.801 4.267   0.408   1.00 11.29 ?  43  LEU   A CB   1 
ATOM   1127 C  CG   . LEU   A 1 43  ? 32.298 2.821   0.484   1.00 11.78 ?  43  LEU   A CG   1 
ATOM   1128 C  CD1  . LEU   A 1 43  ? 33.323 2.699   1.595   1.00 12.44 ?  43  LEU   A CD1  1 
ATOM   1129 C  CD2  . LEU   A 1 43  ? 31.152 1.837   0.703   1.00 11.94 ?  43  LEU   A CD2  1 
ATOM   1130 H  H    . LEU   A 1 43  ? 30.869 3.487   -2.303  1.00 13.11 ?  43  LEU   A H    1 
ATOM   1131 H  HA   . LEU   A 1 43  ? 29.987 4.020   -0.462  1.00 12.65 ?  43  LEU   A HA   1 
ATOM   1132 H  HB2  . LEU   A 1 43  ? 32.571 4.828   0.260   1.00 13.57 ?  43  LEU   A HB2  1 
ATOM   1133 H  HB3  . LEU   A 1 43  ? 31.410 4.472   1.276   1.00 13.57 ?  43  LEU   A HB3  1 
ATOM   1134 H  HG   . LEU   A 1 43  ? 32.736 2.588   -0.353  1.00 14.16 ?  43  LEU   A HG   1 
ATOM   1135 H  HD11 . LEU   A 1 43  ? 33.640 1.782   1.637   1.00 14.95 ?  43  LEU   A HD11 1 
ATOM   1136 H  HD12 . LEU   A 1 43  ? 34.063 3.296   1.407   1.00 14.95 ?  43  LEU   A HD12 1 
ATOM   1137 H  HD13 . LEU   A 1 43  ? 32.904 2.943   2.435   1.00 14.95 ?  43  LEU   A HD13 1 
ATOM   1138 H  HD21 . LEU   A 1 43  ? 31.522 0.951   0.848   1.00 14.35 ?  43  LEU   A HD21 1 
ATOM   1139 H  HD22 . LEU   A 1 43  ? 30.648 2.118   1.480   1.00 14.35 ?  43  LEU   A HD22 1 
ATOM   1140 H  HD23 . LEU   A 1 43  ? 30.586 1.836   -0.082  1.00 14.35 ?  43  LEU   A HD23 1 
ATOM   1141 N  N    A LYS   A 1 44  ? 29.563 6.457   -1.618  0.56 10.90 ?  44  LYS   A N    1 
ATOM   1142 N  N    B LYS   A 1 44  ? 29.570 6.460   -1.621  0.44 11.18 ?  44  LYS   A N    1 
ATOM   1143 C  CA   A LYS   A 1 44  ? 28.920 7.771   -1.630  0.56 11.33 ?  44  LYS   A CA   1 
ATOM   1144 C  CA   B LYS   A 1 44  ? 28.921 7.770   -1.629  0.44 11.87 ?  44  LYS   A CA   1 
ATOM   1145 C  C    A LYS   A 1 44  ? 27.490 7.587   -1.140  0.56 11.02 ?  44  LYS   A C    1 
ATOM   1146 C  C    B LYS   A 1 44  ? 27.495 7.574   -1.136  0.44 11.26 ?  44  LYS   A C    1 
ATOM   1147 O  O    A LYS   A 1 44  ? 26.628 7.077   -1.862  0.56 11.75 ?  44  LYS   A O    1 
ATOM   1148 O  O    B LYS   A 1 44  ? 26.638 7.049   -1.853  0.44 11.69 ?  44  LYS   A O    1 
ATOM   1149 C  CB   A LYS   A 1 44  ? 28.969 8.378   -3.025  0.56 13.46 ?  44  LYS   A CB   1 
ATOM   1150 C  CB   B LYS   A 1 44  ? 28.964 8.384   -3.022  0.44 14.14 ?  44  LYS   A CB   1 
ATOM   1151 C  CG   A LYS   A 1 44  ? 30.353 8.839   -3.451  0.56 16.36 ?  44  LYS   A CG   1 
ATOM   1152 C  CG   B LYS   A 1 44  ? 30.335 8.893   -3.433  0.44 16.69 ?  44  LYS   A CG   1 
ATOM   1153 C  CD   A LYS   A 1 44  ? 30.986 9.775   -2.426  0.56 21.07 ?  44  LYS   A CD   1 
ATOM   1154 C  CD   B LYS   A 1 44  ? 30.949 9.792   -2.366  0.44 20.14 ?  44  LYS   A CD   1 
ATOM   1155 C  CE   A LYS   A 1 44  ? 32.309 10.332  -2.918  0.56 23.92 ?  44  LYS   A CE   1 
ATOM   1156 C  CE   B LYS   A 1 44  ? 32.257 10.396  -2.833  0.44 21.74 ?  44  LYS   A CE   1 
ATOM   1157 N  NZ   A LYS   A 1 44  ? 33.048 11.029  -1.832  0.56 25.37 ?  44  LYS   A NZ   1 
ATOM   1158 N  NZ   B LYS   A 1 44  ? 33.180 10.646  -1.692  0.44 22.22 ?  44  LYS   A NZ   1 
ATOM   1159 H  H    A LYS   A 1 44  ? 29.439 6.002   -2.337  0.56 13.11 ?  44  LYS   A H    1 
ATOM   1160 H  H    B LYS   A 1 44  ? 29.452 6.010   -2.344  0.44 13.44 ?  44  LYS   A H    1 
ATOM   1161 H  HA   A LYS   A 1 44  ? 29.370 8.356   -1.001  0.56 13.61 ?  44  LYS   A HA   1 
ATOM   1162 H  HA   B LYS   A 1 44  ? 29.364 8.355   -0.995  0.44 14.27 ?  44  LYS   A HA   1 
ATOM   1163 H  HB2  A LYS   A 1 44  ? 28.669 7.716   -3.665  0.56 16.18 ?  44  LYS   A HB2  1 
ATOM   1164 H  HB2  B LYS   A 1 44  ? 28.694 7.713   -3.668  0.44 16.99 ?  44  LYS   A HB2  1 
ATOM   1165 H  HB3  A LYS   A 1 44  ? 28.382 9.150   -3.048  0.56 16.18 ?  44  LYS   A HB3  1 
ATOM   1166 H  HB3  B LYS   A 1 44  ? 28.352 9.135   -3.052  0.44 16.99 ?  44  LYS   A HB3  1 
ATOM   1167 H  HG2  A LYS   A 1 44  ? 30.933 8.067   -3.555  0.56 19.66 ?  44  LYS   A HG2  1 
ATOM   1168 H  HG2  B LYS   A 1 44  ? 30.929 8.138   -3.574  0.44 20.05 ?  44  LYS   A HG2  1 
ATOM   1169 H  HG3  A LYS   A 1 44  ? 30.287 9.320   -4.294  0.56 19.66 ?  44  LYS   A HG3  1 
ATOM   1170 H  HG3  B LYS   A 1 44  ? 30.254 9.410   -4.253  0.44 20.05 ?  44  LYS   A HG3  1 
ATOM   1171 H  HD2  A LYS   A 1 44  ? 30.379 10.510  -2.251  0.56 25.30 ?  44  LYS   A HD2  1 
ATOM   1172 H  HD2  B LYS   A 1 44  ? 30.326 10.505  -2.154  0.44 24.19 ?  44  LYS   A HD2  1 
ATOM   1173 H  HD3  A LYS   A 1 44  ? 31.160 9.279   -1.609  0.56 25.30 ?  44  LYS   A HD3  1 
ATOM   1174 H  HD3  B LYS   A 1 44  ? 31.140 9.263   -1.574  0.44 24.19 ?  44  LYS   A HD3  1 
ATOM   1175 H  HE2  A LYS   A 1 44  ? 32.860 9.601   -3.241  0.56 28.72 ?  44  LYS   A HE2  1 
ATOM   1176 H  HE2  B LYS   A 1 44  ? 32.692 9.781   -3.445  0.44 26.11 ?  44  LYS   A HE2  1 
ATOM   1177 H  HE3  A LYS   A 1 44  ? 32.140 10.966  -3.629  0.56 28.72 ?  44  LYS   A HE3  1 
ATOM   1178 H  HE3  B LYS   A 1 44  ? 32.078 11.240  -3.273  0.44 26.11 ?  44  LYS   A HE3  1 
ATOM   1179 H  HZ1  A LYS   A 1 44  ? 33.818 11.345  -2.145  0.56 30.47 ?  44  LYS   A HZ1  1 
ATOM   1180 H  HZ1  B LYS   A 1 44  ? 33.939 11.003  -1.990  0.44 26.69 ?  44  LYS   A HZ1  1 
ATOM   1181 H  HZ2  A LYS   A 1 44  ? 32.562 11.705  -1.520  0.56 30.47 ?  44  LYS   A HZ2  1 
ATOM   1182 H  HZ2  B LYS   A 1 44  ? 32.802 11.212  -1.116  0.44 26.69 ?  44  LYS   A HZ2  1 
ATOM   1183 H  HZ3  A LYS   A 1 44  ? 33.217 10.462  -1.166  0.56 30.47 ?  44  LYS   A HZ3  1 
ATOM   1184 H  HZ3  B LYS   A 1 44  ? 33.361 9.885   -1.272  0.44 26.69 ?  44  LYS   A HZ3  1 
ATOM   1185 N  N    . HIS   A 1 45  ? 27.248 7.975   0.108   1.00 10.81 ?  45  HIS   A N    1 
ATOM   1186 C  CA   . HIS   A 1 45  ? 26.002 7.645   0.797   1.00 10.64 ?  45  HIS   A CA   1 
ATOM   1187 C  C    . HIS   A 1 45  ? 24.984 8.775   0.627   1.00 11.45 ?  45  HIS   A C    1 
ATOM   1188 O  O    . HIS   A 1 45  ? 24.694 9.544   1.545   1.00 13.23 ?  45  HIS   A O    1 
ATOM   1189 C  CB   . HIS   A 1 45  ? 26.295 7.396   2.263   1.00 10.78 ?  45  HIS   A CB   1 
ATOM   1190 C  CG   . HIS   A 1 45  ? 27.406 6.425   2.501   1.00 10.11 ?  45  HIS   A CG   1 
ATOM   1191 N  ND1  . HIS   A 1 45  ? 27.407 5.137   1.996   1.00 10.66 ?  45  HIS   A ND1  1 
ATOM   1192 C  CD2  . HIS   A 1 45  ? 28.565 6.570   3.187   1.00 10.85 ?  45  HIS   A CD2  1 
ATOM   1193 C  CE1  . HIS   A 1 45  ? 28.521 4.536   2.377   1.00 10.49 ?  45  HIS   A CE1  1 
ATOM   1194 N  NE2  . HIS   A 1 45  ? 29.240 5.381   3.096   1.00 10.79 ?  45  HIS   A NE2  1 
ATOM   1195 H  H    A HIS   A 1 45  ? 27.791 8.445   0.583   0.56 12.99 ?  45  HIS   A H    1 
ATOM   1196 H  H    B HIS   A 1 45  ? 27.789 8.448   0.582   0.44 12.99 ?  45  HIS   A H    1 
ATOM   1197 H  HA   . HIS   A 1 45  ? 25.625 6.836   0.415   1.00 12.79 ?  45  HIS   A HA   1 
ATOM   1198 H  HB2  . HIS   A 1 45  ? 26.527 8.236   2.684   1.00 12.96 ?  45  HIS   A HB2  1 
ATOM   1199 H  HB3  . HIS   A 1 45  ? 25.487 7.036   2.683   1.00 12.96 ?  45  HIS   A HB3  1 
ATOM   1200 H  HD2  . HIS   A 1 45  ? 28.847 7.340   3.636   1.00 13.04 ?  45  HIS   A HD2  1 
ATOM   1201 H  HE1  . HIS   A 1 45  ? 28.759 3.662   2.180   1.00 12.61 ?  45  HIS   A HE1  1 
ATOM   1202 H  HE2  . HIS   A 1 45  ? 30.006 5.217   3.452   1.00 12.97 ?  45  HIS   A HE2  1 
ATOM   1203 N  N    A GLY   A 1 46  ? 24.486 8.907   -0.598  0.56 12.52 ?  46  GLY   A N    1 
ATOM   1204 N  N    B GLY   A 1 46  ? 24.347 8.791   -0.541  0.44 12.54 ?  46  GLY   A N    1 
ATOM   1205 C  CA   A GLY   A 1 46  ? 23.710 10.085  -0.946  0.56 12.84 ?  46  GLY   A CA   1 
ATOM   1206 C  CA   B GLY   A 1 46  ? 23.461 9.884   -0.900  0.44 12.82 ?  46  GLY   A CA   1 
ATOM   1207 C  C    A GLY   A 1 46  ? 22.219 9.958   -0.710  0.56 12.81 ?  46  GLY   A C    1 
ATOM   1208 C  C    B GLY   A 1 46  ? 21.999 9.726   -0.520  0.44 12.43 ?  46  GLY   A C    1 
ATOM   1209 O  O    A GLY   A 1 46  ? 21.543 10.949  -0.414  0.56 13.47 ?  46  GLY   A O    1 
ATOM   1210 O  O    B GLY   A 1 46  ? 21.381 10.684  -0.043  0.44 12.96 ?  46  GLY   A O    1 
ATOM   1211 H  H    A GLY   A 1 46  ? 24.573 8.334   -1.231  0.56 15.05 ?  46  GLY   A H    1 
ATOM   1212 H  H    B GLY   A 1 46  ? 24.403 8.176   -1.137  0.44 15.07 ?  46  GLY   A H    1 
ATOM   1213 H  HA2  A GLY   A 1 46  ? 24.034 10.841  -0.425  0.56 15.43 ?  46  GLY   A HA2  1 
ATOM   1214 H  HA2  B GLY   A 1 46  ? 23.778 10.692  -0.471  0.44 15.40 ?  46  GLY   A HA2  1 
ATOM   1215 H  HA3  A GLY   A 1 46  ? 23.843 10.285  -1.881  0.56 15.43 ?  46  GLY   A HA3  1 
ATOM   1216 H  HA3  B GLY   A 1 46  ? 23.505 10.016  -1.857  0.44 15.40 ?  46  GLY   A HA3  1 
ATOM   1217 N  N    A GLY   A 1 47  ? 21.692 8.747   -0.857  0.56 12.39 ?  47  GLY   A N    1 
ATOM   1218 N  N    B GLY   A 1 47  ? 21.429 8.538   -0.725  0.44 11.97 ?  47  GLY   A N    1 
ATOM   1219 C  CA   A GLY   A 1 47  ? 20.260 8.541   -0.783  0.56 12.43 ?  47  GLY   A CA   1 
ATOM   1220 C  CA   B GLY   A 1 47  ? 20.001 8.348   -0.573  0.44 12.05 ?  47  GLY   A CA   1 
ATOM   1221 C  C    A GLY   A 1 47  ? 19.956 7.099   -0.436  0.56 11.67 ?  47  GLY   A C    1 
ATOM   1222 C  C    B GLY   A 1 47  ? 19.666 6.930   -0.164  0.44 11.13 ?  47  GLY   A C    1 
ATOM   1223 O  O    A GLY   A 1 47  ? 20.854 6.291   -0.188  0.56 12.03 ?  47  GLY   A O    1 
ATOM   1224 O  O    B GLY   A 1 47  ? 20.548 6.082   -0.009  0.44 10.98 ?  47  GLY   A O    1 
ATOM   1225 H  H    A GLY   A 1 47  ? 22.144 8.037   -1.004  0.56 14.90 ?  47  GLY   A H    1 
ATOM   1226 H  H    B GLY   A 1 47  ? 21.857 7.826   -0.946  0.44 14.39 ?  47  GLY   A H    1 
ATOM   1227 H  HA2  A GLY   A 1 47  ? 19.875 9.127   -0.110  0.56 14.94 ?  47  GLY   A HA2  1 
ATOM   1228 H  HA2  B GLY   A 1 47  ? 19.657 8.944   0.105   0.44 14.48 ?  47  GLY   A HA2  1 
ATOM   1229 H  HA3  A GLY   A 1 47  ? 19.859 8.747   -1.643  0.56 14.94 ?  47  GLY   A HA3  1 
ATOM   1230 H  HA3  B GLY   A 1 47  ? 19.553 8.538   -1.413  0.44 14.48 ?  47  GLY   A HA3  1 
ATOM   1231 N  N    A GLY   A 1 48  ? 18.668 6.778   -0.435  0.56 11.21 ?  48  GLY   A N    1 
ATOM   1232 N  N    B GLY   A 1 48  ? 18.369 6.677   0.009   0.44 10.97 ?  48  GLY   A N    1 
ATOM   1233 C  CA   A GLY   A 1 48  ? 18.269 5.441   -0.060  0.56 10.94 ?  48  GLY   A CA   1 
ATOM   1234 C  CA   B GLY   A 1 48  ? 17.939 5.356   0.431   0.44 10.20 ?  48  GLY   A CA   1 
ATOM   1235 C  C    A GLY   A 1 48  ? 18.663 5.130   1.375   0.56 10.69 ?  48  GLY   A C    1 
ATOM   1236 C  C    B GLY   A 1 48  ? 18.536 4.985   1.772   0.44 10.70 ?  48  GLY   A C    1 
ATOM   1237 O  O    A GLY   A 1 48  ? 18.833 6.019   2.216   0.56 11.41 ?  48  GLY   A O    1 
ATOM   1238 O  O    B GLY   A 1 48  ? 18.693 5.823   2.670   0.44 10.71 ?  48  GLY   A O    1 
ATOM   1239 H  H    A GLY   A 1 48  ? 18.028 7.308   -0.640  0.56 13.48 ?  48  GLY   A H    1 
ATOM   1240 H  H    B GLY   A 1 48  ? 17.721 7.241   -0.105  0.44 13.19 ?  48  GLY   A H    1 
ATOM   1241 H  HA2  A GLY   A 1 48  ? 17.313 5.348   -0.144  0.56 13.15 ?  48  GLY   A HA2  1 
ATOM   1242 H  HA2  B GLY   A 1 48  ? 16.969 5.322   0.499   0.44 12.26 ?  48  GLY   A HA2  1 
ATOM   1243 H  HA3  A GLY   A 1 48  ? 18.704 4.795   -0.639  0.56 13.15 ?  48  GLY   A HA3  1 
ATOM   1244 H  HA3  B GLY   A 1 48  ? 18.221 4.693   -0.222  0.44 12.26 ?  48  GLY   A HA3  1 
ATOM   1245 N  N    A VAL   A 1 49  ? 18.817 3.830   1.644   0.56 11.12 ?  49  VAL   A N    1 
ATOM   1246 N  N    B VAL   A 1 49  ? 18.868 3.701   1.914   0.44 10.73 ?  49  VAL   A N    1 
ATOM   1247 C  CA   A VAL   A 1 49  ? 19.282 3.389   2.958   0.56 11.45 ?  49  VAL   A CA   1 
ATOM   1248 C  CA   B VAL   A 1 49  ? 19.483 3.207   3.145   0.44 10.55 ?  49  VAL   A CA   1 
ATOM   1249 C  C    A VAL   A 1 49  ? 20.591 4.072   3.328   0.56 10.81 ?  49  VAL   A C    1 
ATOM   1250 C  C    B VAL   A 1 49  ? 20.737 4.002   3.485   0.44 9.39  ?  49  VAL   A C    1 
ATOM   1251 O  O    A VAL   A 1 49  ? 20.780 4.496   4.471   0.56 11.15 ?  49  VAL   A O    1 
ATOM   1252 O  O    B VAL   A 1 49  ? 20.929 4.428   4.629   0.44 9.63  ?  49  VAL   A O    1 
ATOM   1253 C  CB   A VAL   A 1 49  ? 19.418 1.855   2.991   0.56 12.09 ?  49  VAL   A CB   1 
ATOM   1254 C  CB   B VAL   A 1 49  ? 19.800 1.708   3.014   0.44 10.88 ?  49  VAL   A CB   1 
ATOM   1255 C  CG1  A VAL   A 1 49  ? 20.152 1.404   4.253   0.56 12.30 ?  49  VAL   A CG1  1 
ATOM   1256 C  CG1  B VAL   A 1 49  ? 20.620 1.252   4.202   0.44 10.49 ?  49  VAL   A CG1  1 
ATOM   1257 C  CG2  A VAL   A 1 49  ? 18.049 1.192   2.898   0.56 14.02 ?  49  VAL   A CG2  1 
ATOM   1258 C  CG2  B VAL   A 1 49  ? 18.522 0.888   2.884   0.44 11.71 ?  49  VAL   A CG2  1 
ATOM   1259 H  H    A VAL   A 1 49  ? 18.668 3.187   1.092   0.56 13.37 ?  49  VAL   A H    1 
ATOM   1260 H  H    B VAL   A 1 49  ? 18.745 3.097   1.314   0.44 12.89 ?  49  VAL   A H    1 
ATOM   1261 H  HA   A VAL   A 1 49  ? 18.624 3.630   3.627   0.56 13.76 ?  49  VAL   A HA   1 
ATOM   1262 H  HA   B VAL   A 1 49  ? 18.857 3.312   3.876   0.44 12.68 ?  49  VAL   A HA   1 
ATOM   1263 H  HB   A VAL   A 1 49  ? 19.944 1.561   2.230   0.56 14.53 ?  49  VAL   A HB   1 
ATOM   1264 H  HB   B VAL   A 1 49  ? 20.327 1.564   2.212   0.44 13.08 ?  49  VAL   A HB   1 
ATOM   1265 H  HG11 A VAL   A 1 49  ? 19.976 0.459   4.400   0.56 14.78 ?  49  VAL   A HG11 1 
ATOM   1266 H  HG11 B VAL   A 1 49  ? 20.549 0.289   4.283   0.44 12.61 ?  49  VAL   A HG11 1 
ATOM   1267 H  HG12 A VAL   A 1 49  ? 21.103 1.545   4.137   0.56 14.78 ?  49  VAL   A HG12 1 
ATOM   1268 H  HG12 B VAL   A 1 49  ? 21.547 1.503   4.063   0.44 12.61 ?  49  VAL   A HG12 1 
ATOM   1269 H  HG13 A VAL   A 1 49  ? 19.825 1.918   5.007   0.56 14.78 ?  49  VAL   A HG13 1 
ATOM   1270 H  HG13 B VAL   A 1 49  ? 20.275 1.677   5.002   0.44 12.61 ?  49  VAL   A HG13 1 
ATOM   1271 H  HG21 A VAL   A 1 49  ? 18.160 0.226   2.919   0.56 16.85 ?  49  VAL   A HG21 1 
ATOM   1272 H  HG21 B VAL   A 1 49  ? 18.750 -0.046  2.760   0.44 14.08 ?  49  VAL   A HG21 1 
ATOM   1273 H  HG22 A VAL   A 1 49  ? 17.508 1.478   3.649   0.56 16.85 ?  49  VAL   A HG22 1 
ATOM   1274 H  HG22 B VAL   A 1 49  ? 17.996 0.994   3.694   0.44 14.08 ?  49  VAL   A HG22 1 
ATOM   1275 H  HG23 A VAL   A 1 49  ? 17.630 1.457   2.065   0.56 16.85 ?  49  VAL   A HG23 1 
ATOM   1276 H  HG23 B VAL   A 1 49  ? 18.014 1.208   2.120   0.44 14.08 ?  49  VAL   A HG23 1 
ATOM   1277 N  N    A ALA   A 1 50  ? 21.526 4.145   2.378   0.56 10.23 ?  50  ALA   A N    1 
ATOM   1278 N  N    B ALA   A 1 50  ? 21.630 4.167   2.503   0.44 9.46  ?  50  ALA   A N    1 
ATOM   1279 C  CA   A ALA   A 1 50  ? 22.847 4.694   2.667   0.56 9.90  ?  50  ALA   A CA   1 
ATOM   1280 C  CA   B ALA   A 1 50  ? 22.933 4.760   2.784   0.44 9.68  ?  50  ALA   A CA   1 
ATOM   1281 C  C    A ALA   A 1 50  ? 22.760 6.151   3.099   0.56 10.04 ?  50  ALA   A C    1 
ATOM   1282 C  C    B ALA   A 1 50  ? 22.795 6.217   3.201   0.44 9.20  ?  50  ALA   A C    1 
ATOM   1283 O  O    A ALA   A 1 50  ? 23.419 6.567   4.057   0.56 10.86 ?  50  ALA   A O    1 
ATOM   1284 O  O    B ALA   A 1 50  ? 23.376 6.645   4.206   0.44 9.26  ?  50  ALA   A O    1 
ATOM   1285 C  CB   A ALA   A 1 50  ? 23.730 4.561   1.430   0.56 10.03 ?  50  ALA   A CB   1 
ATOM   1286 C  CB   B ALA   A 1 50  ? 23.834 4.638   1.557   0.44 10.26 ?  50  ALA   A CB   1 
ATOM   1287 H  H    A ALA   A 1 50  ? 21.421 3.878   1.571   0.56 12.30 ?  50  ALA   A H    1 
ATOM   1288 H  H    B ALA   A 1 50  ? 21.503 3.951   1.676   0.44 11.37 ?  50  ALA   A H    1 
ATOM   1289 H  HA   A ALA   A 1 50  ? 23.256 4.193   3.392   0.56 11.91 ?  50  ALA   A HA   1 
ATOM   1290 H  HA   B ALA   A 1 50  ? 23.349 4.280   3.514   0.44 11.64 ?  50  ALA   A HA   1 
ATOM   1291 H  HB1  A ALA   A 1 50  ? 24.603 4.934   1.627   0.56 12.06 ?  50  ALA   A HB1  1 
ATOM   1292 H  HB1  B ALA   A 1 50  ? 24.697 5.034   1.759   0.44 12.33 ?  50  ALA   A HB1  1 
ATOM   1293 H  HB2  A ALA   A 1 50  ? 23.809 3.626   1.197   0.56 12.06 ?  50  ALA   A HB2  1 
ATOM   1294 H  HB2  B ALA   A 1 50  ? 23.942 3.702   1.335   0.44 12.33 ?  50  ALA   A HB2  1 
ATOM   1295 H  HB3  A ALA   A 1 50  ? 23.318 5.053   0.701   0.56 12.06 ?  50  ALA   A HB3  1 
ATOM   1296 H  HB3  B ALA   A 1 50  ? 23.422 5.109   0.814   0.44 12.33 ?  50  ALA   A HB3  1 
ATOM   1297 N  N    A GLY   A 1 51  ? 21.968 6.947   2.386   0.56 10.09 ?  51  GLY   A N    1 
ATOM   1298 N  N    B GLY   A 1 51  ? 22.034 6.994   2.432   0.44 10.18 ?  51  GLY   A N    1 
ATOM   1299 C  CA   A GLY   A 1 51  ? 21.821 8.341   2.769   0.56 10.52 ?  51  GLY   A CA   1 
ATOM   1300 C  CA   B GLY   A 1 51  ? 21.830 8.384   2.796   0.44 10.60 ?  51  GLY   A CA   1 
ATOM   1301 C  C    A GLY   A 1 51  ? 21.214 8.496   4.150   0.56 10.40 ?  51  GLY   A C    1 
ATOM   1302 C  C    B GLY   A 1 51  ? 21.192 8.524   4.162   0.44 10.42 ?  51  GLY   A C    1 
ATOM   1303 O  O    A GLY   A 1 51  ? 21.608 9.378   4.919   0.56 11.25 ?  51  GLY   A O    1 
ATOM   1304 O  O    B GLY   A 1 51  ? 21.548 9.417   4.937   0.44 10.97 ?  51  GLY   A O    1 
ATOM   1305 H  H    A GLY   A 1 51  ? 21.529 6.713   1.685   0.56 12.13 ?  51  GLY   A H    1 
ATOM   1306 H  H    B GLY   A 1 51  ? 21.633 6.744   1.712   0.44 12.23 ?  51  GLY   A H    1 
ATOM   1307 H  HA2  A GLY   A 1 51  ? 22.692 8.773   2.764   0.56 12.65 ?  51  GLY   A HA2  1 
ATOM   1308 H  HA2  B GLY   A 1 51  ? 22.684 8.846   2.803   0.44 12.74 ?  51  GLY   A HA2  1 
ATOM   1309 H  HA3  A GLY   A 1 51  ? 21.252 8.795   2.127   0.56 12.65 ?  51  GLY   A HA3  1 
ATOM   1310 H  HA3  B GLY   A 1 51  ? 21.255 8.811   2.141   0.44 12.74 ?  51  GLY   A HA3  1 
ATOM   1311 N  N    . ALA   A 1 52  ? 20.240 7.642   4.478   1.00 10.39 ?  52  ALA   A N    1 
ATOM   1312 C  CA   . ALA   A 1 52  ? 19.586 7.705   5.779   1.00 11.30 ?  52  ALA   A CA   1 
ATOM   1313 C  C    . ALA   A 1 52  ? 20.522 7.284   6.912   1.00 10.69 ?  52  ALA   A C    1 
ATOM   1314 O  O    . ALA   A 1 52  ? 20.576 7.945   7.954   1.00 11.83 ?  52  ALA   A O    1 
ATOM   1315 C  CB   . ALA   A 1 52  ? 18.317 6.855   5.763   1.00 12.27 ?  52  ALA   A CB   1 
ATOM   1316 H  H    A ALA   A 1 52  ? 19.953 7.015   3.962   0.56 12.49 ?  52  ALA   A H    1 
ATOM   1317 H  H    B ALA   A 1 52  ? 19.971 7.006   3.963   0.44 12.49 ?  52  ALA   A H    1 
ATOM   1318 H  HA   . ALA   A 1 52  ? 19.318 8.616   5.943   1.00 13.58 ?  52  ALA   A HA   1 
ATOM   1319 H  HB1  . ALA   A 1 52  ? 17.877 6.925   6.627   1.00 14.75 ?  52  ALA   A HB1  1 
ATOM   1320 H  HB2  . ALA   A 1 52  ? 17.727 7.181   5.066   1.00 14.75 ?  52  ALA   A HB2  1 
ATOM   1321 H  HB3  . ALA   A 1 52  ? 18.552 5.928   5.588   1.00 14.75 ?  52  ALA   A HB3  1 
ATOM   1322 N  N    A LEU   A 1 53  ? 21.268 6.190   6.736   0.56 10.77 ?  53  LEU   A N    1 
ATOM   1323 N  N    B LEU   A 1 53  ? 21.245 6.174   6.741   0.44 10.51 ?  53  LEU   A N    1 
ATOM   1324 C  CA   A LEU   A 1 53  ? 22.218 5.790   7.773   0.56 11.21 ?  53  LEU   A CA   1 
ATOM   1325 C  CA   B LEU   A 1 53  ? 22.222 5.780   7.755   0.44 10.75 ?  53  LEU   A CA   1 
ATOM   1326 C  C    A LEU   A 1 53  ? 23.295 6.848   7.967   0.56 10.35 ?  53  LEU   A C    1 
ATOM   1327 C  C    B LEU   A 1 53  ? 23.245 6.887   7.964   0.44 9.95  ?  53  LEU   A C    1 
ATOM   1328 O  O    A LEU   A 1 53  ? 23.666 7.166   9.100   0.56 11.37 ?  53  LEU   A O    1 
ATOM   1329 O  O    B LEU   A 1 53  ? 23.506 7.303   9.097   0.44 10.28 ?  53  LEU   A O    1 
ATOM   1330 C  CB   A LEU   A 1 53  ? 22.865 4.445   7.432   0.56 11.51 ?  53  LEU   A CB   1 
ATOM   1331 C  CB   B LEU   A 1 53  ? 22.926 4.475   7.361   0.44 10.93 ?  53  LEU   A CB   1 
ATOM   1332 C  CG   A LEU   A 1 53  ? 21.933 3.230   7.412   0.56 11.86 ?  53  LEU   A CG   1 
ATOM   1333 C  CG   B LEU   A 1 53  ? 22.202 3.129   7.510   0.44 11.12 ?  53  LEU   A CG   1 
ATOM   1334 C  CD1  A LEU   A 1 53  ? 22.664 2.030   6.832   0.56 11.88 ?  53  LEU   A CD1  1 
ATOM   1335 C  CD1  B LEU   A 1 53  ? 23.055 2.022   6.902   0.44 11.30 ?  53  LEU   A CD1  1 
ATOM   1336 C  CD2  A LEU   A 1 53  ? 21.410 2.907   8.802   0.56 12.54 ?  53  LEU   A CD2  1 
ATOM   1337 C  CD2  B LEU   A 1 53  ? 21.880 2.802   8.960   0.44 11.02 ?  53  LEU   A CD2  1 
ATOM   1338 H  H    A LEU   A 1 53  ? 21.242 5.673   6.046   0.56 12.95 ?  53  LEU   A H    1 
ATOM   1339 H  H    B LEU   A 1 53  ? 21.196 5.645   6.064   0.44 12.63 ?  53  LEU   A H    1 
ATOM   1340 H  HA   A LEU   A 1 53  ? 21.744 5.688   8.610   0.56 13.47 ?  53  LEU   A HA   1 
ATOM   1341 H  HA   B LEU   A 1 53  ? 21.765 5.631   8.595   0.44 12.92 ?  53  LEU   A HA   1 
ATOM   1342 H  HB2  A LEU   A 1 53  ? 23.268 4.512   6.551   0.56 13.83 ?  53  LEU   A HB2  1 
ATOM   1343 H  HB2  B LEU   A 1 53  ? 23.173 4.546   6.427   0.44 13.14 ?  53  LEU   A HB2  1 
ATOM   1344 H  HB3  A LEU   A 1 53  ? 23.558 4.263   8.087   0.56 13.83 ?  53  LEU   A HB3  1 
ATOM   1345 H  HB3  B LEU   A 1 53  ? 23.733 4.405   7.892   0.44 13.14 ?  53  LEU   A HB3  1 
ATOM   1346 H  HG   A LEU   A 1 53  ? 21.173 3.421   6.839   0.56 14.26 ?  53  LEU   A HG   1 
ATOM   1347 H  HG   B LEU   A 1 53  ? 21.368 3.157   7.015   0.44 13.36 ?  53  LEU   A HG   1 
ATOM   1348 H  HD11 A LEU   A 1 53  ? 22.065 1.269   6.828   0.56 14.27 ?  53  LEU   A HD11 1 
ATOM   1349 H  HD11 B LEU   A 1 53  ? 22.595 1.174   7.001   0.44 13.58 ?  53  LEU   A HD11 1 
ATOM   1350 H  HD12 A LEU   A 1 53  ? 22.943 2.240   5.927   0.56 14.27 ?  53  LEU   A HD12 1 
ATOM   1351 H  HD12 B LEU   A 1 53  ? 23.196 2.214   5.961   0.44 13.58 ?  53  LEU   A HD12 1 
ATOM   1352 H  HD13 A LEU   A 1 53  ? 23.440 1.841   7.383   0.56 14.27 ?  53  LEU   A HD13 1 
ATOM   1353 H  HD13 B LEU   A 1 53  ? 23.908 1.992   7.364   0.44 13.58 ?  53  LEU   A HD13 1 
ATOM   1354 H  HD21 A LEU   A 1 53  ? 20.849 2.117   8.753   0.56 15.06 ?  53  LEU   A HD21 1 
ATOM   1355 H  HD21 B LEU   A 1 53  ? 21.453 1.930   9.003   0.44 13.24 ?  53  LEU   A HD21 1 
ATOM   1356 H  HD22 A LEU   A 1 53  ? 22.162 2.743   9.392   0.56 15.06 ?  53  LEU   A HD22 1 
ATOM   1357 H  HD22 B LEU   A 1 53  ? 22.703 2.791   9.472   0.44 13.24 ?  53  LEU   A HD22 1 
ATOM   1358 H  HD23 A LEU   A 1 53  ? 20.892 3.659   9.127   0.56 15.06 ?  53  LEU   A HD23 1 
ATOM   1359 H  HD23 B LEU   A 1 53  ? 21.280 3.479   9.308   0.44 13.24 ?  53  LEU   A HD23 1 
ATOM   1360 N  N    . ASN   A 1 54  ? 23.812 7.402   6.874   1.00 10.18 ?  54  ASN   A N    1 
ATOM   1361 C  CA   . ASN   A 1 54  ? 24.865 8.393   7.011   1.00 10.29 ?  54  ASN   A CA   1 
ATOM   1362 C  C    . ASN   A 1 54  ? 24.354 9.644   7.725   1.00 10.63 ?  54  ASN   A C    1 
ATOM   1363 O  O    . ASN   A 1 54  ? 25.041 10.203  8.591   1.00 11.12 ?  54  ASN   A O    1 
ATOM   1364 C  CB   . ASN   A 1 54  ? 25.442 8.739   5.654   1.00 10.63 ?  54  ASN   A CB   1 
ATOM   1365 C  CG   . ASN   A 1 54  ? 26.454 9.848   5.765   1.00 10.94 ?  54  ASN   A CG   1 
ATOM   1366 O  OD1  . ASN   A 1 54  ? 27.463 9.703   6.473   1.00 10.73 ?  54  ASN   A OD1  1 
ATOM   1367 N  ND2  . ASN   A 1 54  ? 26.192 10.966  5.111   1.00 11.48 ?  54  ASN   A ND2  1 
ATOM   1368 H  H    A ASN   A 1 54  ? 23.574 7.222   6.068   0.56 12.24 ?  54  ASN   A H    1 
ATOM   1369 H  H    B ASN   A 1 54  ? 23.599 7.200   6.067   0.44 12.24 ?  54  ASN   A H    1 
ATOM   1370 H  HA   . ASN   A 1 54  ? 25.573 8.020   7.549   1.00 12.37 ?  54  ASN   A HA   1 
ATOM   1371 H  HB2  . ASN   A 1 54  ? 25.884 7.954   5.285   1.00 12.77 ?  54  ASN   A HB2  1 
ATOM   1372 H  HB3  . ASN   A 1 54  ? 24.733 9.032   5.062   1.00 12.77 ?  54  ASN   A HB3  1 
ATOM   1373 H  HD21 . ASN   A 1 54  ? 26.742 11.626  5.156   1.00 13.80 ?  54  ASN   A HD21 1 
ATOM   1374 H  HD22 . ASN   A 1 54  ? 25.475 11.032  4.644   1.00 13.80 ?  54  ASN   A HD22 1 
ATOM   1375 N  N    A LYS   A 1 55  ? 23.146 10.094  7.369   0.56 10.55 ?  55  LYS   A N    1 
ATOM   1376 N  N    B LYS   A 1 55  ? 23.142 10.095  7.386   0.44 10.71 ?  55  LYS   A N    1 
ATOM   1377 C  CA   A LYS   A 1 55  ? 22.543 11.242  8.033   0.56 11.47 ?  55  LYS   A CA   1 
ATOM   1378 C  CA   B LYS   A 1 55  ? 22.588 11.268  8.053   0.44 11.81 ?  55  LYS   A CA   1 
ATOM   1379 C  C    A LYS   A 1 55  ? 22.471 11.024  9.538   0.56 11.54 ?  55  LYS   A C    1 
ATOM   1380 C  C    B LYS   A 1 55  ? 22.462 11.036  9.555   0.44 11.71 ?  55  LYS   A C    1 
ATOM   1381 O  O    A LYS   A 1 55  ? 22.774 11.932  10.323  0.56 12.57 ?  55  LYS   A O    1 
ATOM   1382 O  O    B LYS   A 1 55  ? 22.719 11.944  10.356  0.44 12.29 ?  55  LYS   A O    1 
ATOM   1383 C  CB   A LYS   A 1 55  ? 21.150 11.478  7.445   0.56 12.05 ?  55  LYS   A CB   1 
ATOM   1384 C  CB   B LYS   A 1 55  ? 21.240 11.644  7.431   0.44 12.93 ?  55  LYS   A CB   1 
ATOM   1385 C  CG   A LYS   A 1 55  ? 20.361 12.604  8.089   0.56 12.82 ?  55  LYS   A CG   1 
ATOM   1386 C  CG   B LYS   A 1 55  ? 20.641 12.929  7.994   0.44 14.36 ?  55  LYS   A CG   1 
ATOM   1387 C  CD   A LYS   A 1 55  ? 19.046 12.821  7.355   0.56 13.70 ?  55  LYS   A CD   1 
ATOM   1388 C  CD   B LYS   A 1 55  ? 19.367 13.350  7.270   0.44 15.95 ?  55  LYS   A CD   1 
ATOM   1389 C  CE   A LYS   A 1 55  ? 18.237 13.947  7.978   0.56 14.85 ?  55  LYS   A CE   1 
ATOM   1390 C  CE   B LYS   A 1 55  ? 18.216 12.392  7.518   0.44 16.93 ?  55  LYS   A CE   1 
ATOM   1391 N  NZ   A LYS   A 1 55  ? 16.918 14.117  7.307   0.56 15.68 ?  55  LYS   A NZ   1 
ATOM   1392 N  NZ   B LYS   A 1 55  ? 16.913 13.024  7.144   0.44 17.39 ?  55  LYS   A NZ   1 
ATOM   1393 H  H    A LYS   A 1 55  ? 22.653 9.742   6.757   0.56 12.69 ?  55  LYS   A H    1 
ATOM   1394 H  H    B LYS   A 1 55  ? 22.628 9.743   6.790   0.44 12.88 ?  55  LYS   A H    1 
ATOM   1395 H  HA   A LYS   A 1 55  ? 23.079 12.029  7.864   0.56 13.79 ?  55  LYS   A HA   1 
ATOM   1396 H  HA   B LYS   A 1 55  ? 23.190 12.014  7.920   0.44 14.20 ?  55  LYS   A HA   1 
ATOM   1397 H  HB2  A LYS   A 1 55  ? 21.242 11.689  6.503   0.56 14.49 ?  55  LYS   A HB2  1 
ATOM   1398 H  HB2  B LYS   A 1 55  ? 21.360 11.769  6.476   0.44 15.53 ?  55  LYS   A HB2  1 
ATOM   1399 H  HB3  A LYS   A 1 55  ? 20.628 10.663  7.544   0.56 14.49 ?  55  LYS   A HB3  1 
ATOM   1400 H  HB3  B LYS   A 1 55  ? 20.607 10.928  7.592   0.44 15.53 ?  55  LYS   A HB3  1 
ATOM   1401 H  HG2  A LYS   A 1 55  ? 20.159 12.374  9.011   0.56 15.40 ?  55  LYS   A HG2  1 
ATOM   1402 H  HG2  B LYS   A 1 55  ? 20.421 12.794  8.930   0.44 17.26 ?  55  LYS   A HG2  1 
ATOM   1403 H  HG3  A LYS   A 1 55  ? 20.875 13.424  8.048   0.56 15.40 ?  55  LYS   A HG3  1 
ATOM   1404 H  HG3  B LYS   A 1 55  ? 21.288 13.647  7.906   0.44 17.26 ?  55  LYS   A HG3  1 
ATOM   1405 H  HD2  A LYS   A 1 55  ? 19.233 13.051  6.430   0.56 16.46 ?  55  LYS   A HD2  1 
ATOM   1406 H  HD2  B LYS   A 1 55  ? 19.101 14.230  7.585   0.44 19.16 ?  55  LYS   A HD2  1 
ATOM   1407 H  HD3  A LYS   A 1 55  ? 18.520 12.005  7.395   0.56 16.46 ?  55  LYS   A HD3  1 
ATOM   1408 H  HD3  B LYS   A 1 55  ? 19.540 13.377  6.317   0.44 19.16 ?  55  LYS   A HD3  1 
ATOM   1409 H  HE2  A LYS   A 1 55  ? 18.079 13.745  8.912   0.56 17.84 ?  55  LYS   A HE2  1 
ATOM   1410 H  HE2  B LYS   A 1 55  ? 18.336 11.596  6.976   0.44 20.34 ?  55  LYS   A HE2  1 
ATOM   1411 H  HE3  A LYS   A 1 55  ? 18.732 14.777  7.893   0.56 17.84 ?  55  LYS   A HE3  1 
ATOM   1412 H  HE3  B LYS   A 1 55  ? 18.184 12.158  8.459   0.44 20.34 ?  55  LYS   A HE3  1 
ATOM   1413 H  HZ1  A LYS   A 1 55  ? 16.466 14.779  7.690   0.56 18.83 ?  55  LYS   A HZ1  1 
ATOM   1414 H  HZ1  B LYS   A 1 55  ? 16.310 12.883  7.783   0.44 20.89 ?  55  LYS   A HZ1  1 
ATOM   1415 H  HZ2  A LYS   A 1 55  ? 17.039 14.310  6.445   0.56 18.83 ?  55  LYS   A HZ2  1 
ATOM   1416 H  HZ2  B LYS   A 1 55  ? 17.020 13.903  7.040   0.44 20.89 ?  55  LYS   A HZ2  1 
ATOM   1417 H  HZ3  A LYS   A 1 55  ? 16.445 13.366  7.370   0.56 18.83 ?  55  LYS   A HZ3  1 
ATOM   1418 H  HZ3  B LYS   A 1 55  ? 16.612 12.679  6.381   0.44 20.89 ?  55  LYS   A HZ3  1 
ATOM   1419 N  N    . ALA   A 1 56  ? 22.065 9.825   9.958   1.00 11.96 ?  56  ALA   A N    1 
ATOM   1420 C  CA   . ALA   A 1 56  ? 21.935 9.519   11.374  1.00 12.44 ?  56  ALA   A CA   1 
ATOM   1421 C  C    . ALA   A 1 56  ? 23.274 9.532   12.098  1.00 12.26 ?  56  ALA   A C    1 
ATOM   1422 O  O    . ALA   A 1 56  ? 23.296 9.714   13.315  1.00 13.67 ?  56  ALA   A O    1 
ATOM   1423 C  CB   . ALA   A 1 56  ? 21.230 8.176   11.570  1.00 13.51 ?  56  ALA   A CB   1 
ATOM   1424 H  H    A ALA   A 1 56  ? 21.859 9.176   9.437   0.56 14.37 ?  56  ALA   A H    1 
ATOM   1425 H  H    B ALA   A 1 56  ? 21.862 9.179   9.433   0.44 14.37 ?  56  ALA   A H    1 
ATOM   1426 H  HA   . ALA   A 1 56  ? 21.392 10.195  11.794  1.00 14.95 ?  56  ALA   A HA   1 
ATOM   1427 H  HB1  . ALA   A 1 56  ? 21.162 7.990   12.524  1.00 16.24 ?  56  ALA   A HB1  1 
ATOM   1428 H  HB2  . ALA   A 1 56  ? 20.341 8.233   11.185  1.00 16.24 ?  56  ALA   A HB2  1 
ATOM   1429 H  HB3  . ALA   A 1 56  ? 21.738 7.478   11.134  1.00 16.24 ?  56  ALA   A HB3  1 
ATOM   1430 N  N    . THR   A 1 57  ? 24.390 9.343   11.382  1.00 11.56 ?  57  THR   A N    1 
ATOM   1431 C  CA   . THR   A 1 57  ? 25.731 9.469   11.963  1.00 11.68 ?  57  THR   A CA   1 
ATOM   1432 C  C    . THR   A 1 57  ? 26.287 10.886  11.883  1.00 12.16 ?  57  THR   A C    1 
ATOM   1433 O  O    . THR   A 1 57  ? 27.467 11.095  12.180  1.00 12.69 ?  57  THR   A O    1 
ATOM   1434 C  CB   . THR   A 1 57  ? 26.744 8.514   11.300  1.00 11.56 ?  57  THR   A CB   1 
ATOM   1435 O  OG1  . THR   A 1 57  ? 27.130 9.005   10.004  1.00 11.26 ?  57  THR   A OG1  1 
ATOM   1436 C  CG2  . THR   A 1 57  ? 26.214 7.086   11.201  1.00 11.99 ?  57  THR   A CG2  1 
ATOM   1437 H  H    . THR   A 1 57  ? 24.402 9.115   10.550  1.00 13.90 ?  57  THR   A H    1 
ATOM   1438 H  HA   . THR   A 1 57  ? 25.685 9.216   12.904  1.00 14.03 ?  57  THR   A HA   1 
ATOM   1439 H  HB   . THR   A 1 57  ? 27.542 8.480   11.857  1.00 13.89 ?  57  THR   A HB   1 
ATOM   1440 H  HG1  . THR   A 1 57  ? 26.453 9.072   9.510   1.00 13.54 ?  57  THR   A HG1  1 
ATOM   1441 H  HG21 . THR   A 1 57  ? 26.890 6.503   10.815  1.00 14.41 ?  57  THR   A HG21 1 
ATOM   1442 H  HG22 . THR   A 1 57  ? 25.983 6.753   12.083  1.00 14.41 ?  57  THR   A HG22 1 
ATOM   1443 H  HG23 . THR   A 1 57  ? 25.425 7.060   10.640  1.00 14.41 ?  57  THR   A HG23 1 
ATOM   1444 N  N    . ASN   A 1 58  ? 25.480 11.856  11.464  1.00 12.63 ?  58  ASN   A N    1 
ATOM   1445 C  CA   . ASN   A 1 58  ? 25.947 13.236  11.380  1.00 13.61 ?  58  ASN   A CA   1 
ATOM   1446 C  C    . ASN   A 1 58  ? 27.087 13.365  10.367  1.00 12.28 ?  58  ASN   A C    1 
ATOM   1447 O  O    . ASN   A 1 58  ? 27.985 14.198  10.523  1.00 12.99 ?  58  ASN   A O    1 
ATOM   1448 C  CB   . ASN   A 1 58  ? 26.345 13.748  12.782  1.00 15.96 ?  58  ASN   A CB   1 
ATOM   1449 C  CG   . ASN   A 1 58  ? 26.766 15.205  12.803  1.00 19.38 ?  58  ASN   A CG   1 
ATOM   1450 O  OD1  . ASN   A 1 58  ? 26.135 16.050  12.175  1.00 20.91 ?  58  ASN   A OD1  1 
ATOM   1451 N  ND2  . ASN   A 1 58  ? 27.823 15.514  13.571  1.00 20.05 ?  58  ASN   A ND2  1 
ATOM   1452 H  H    . ASN   A 1 58  ? 24.662 11.738  11.217  1.00 15.18 ?  58  ASN   A H    1 
ATOM   1453 H  HA   . ASN   A 1 58  ? 25.215 13.782  11.069  1.00 16.36 ?  58  ASN   A HA   1 
ATOM   1454 H  HB2  . ASN   A 1 58  ? 25.580 13.652  13.381  1.00 19.18 ?  58  ASN   A HB2  1 
ATOM   1455 H  HB3  . ASN   A 1 58  ? 27.086 13.227  13.122  1.00 19.18 ?  58  ASN   A HB3  1 
ATOM   1456 H  HD21 . ASN   A 1 58  ? 28.098 16.330  13.622  1.00 24.08 ?  58  ASN   A HD21 1 
ATOM   1457 H  HD22 . ASN   A 1 58  ? 28.232 14.897  14.006  1.00 24.08 ?  58  ASN   A HD22 1 
ATOM   1458 N  N    . ASN   A 1 59  ? 27.064 12.543  9.313   1.00 11.56 ?  59  ASN   A N    1 
ATOM   1459 C  CA   . ASN   A 1 59  ? 28.054 12.503  8.229   1.00 11.27 ?  59  ASN   A CA   1 
ATOM   1460 C  C    . ASN   A 1 59  ? 29.372 11.827  8.628   1.00 11.22 ?  59  ASN   A C    1 
ATOM   1461 O  O    . ASN   A 1 59  ? 30.292 11.785  7.804   1.00 11.24 ?  59  ASN   A O    1 
ATOM   1462 C  CB   . ASN   A 1 59  ? 28.356 13.884  7.617   1.00 11.45 ?  59  ASN   A CB   1 
ATOM   1463 C  CG   . ASN   A 1 59  ? 28.715 13.811  6.151   1.00 11.69 ?  59  ASN   A CG   1 
ATOM   1464 O  OD1  . ASN   A 1 59  ? 28.008 13.190  5.355   1.00 11.95 ?  59  ASN   A OD1  1 
ATOM   1465 N  ND2  . ASN   A 1 59  ? 29.807 14.471  5.772   1.00 12.35 ?  59  ASN   A ND2  1 
ATOM   1466 H  H    . ASN   A 1 59  ? 26.441 11.958  9.196   1.00 13.89 ?  59  ASN   A H    1 
ATOM   1467 H  HA   . ASN   A 1 59  ? 27.678 11.969  7.519   1.00 13.55 ?  59  ASN   A HA   1 
ATOM   1468 H  HB2  . ASN   A 1 59  ? 27.572 14.450  7.698   1.00 13.76 ?  59  ASN   A HB2  1 
ATOM   1469 H  HB3  . ASN   A 1 59  ? 29.104 14.287  8.084   1.00 13.76 ?  59  ASN   A HB3  1 
ATOM   1470 H  HD21 . ASN   A 1 59  ? 30.056 14.467  4.948   1.00 14.84 ?  59  ASN   A HD21 1 
ATOM   1471 H  HD22 . ASN   A 1 59  ? 30.276 14.904  6.355   1.00 14.84 ?  59  ASN   A HD22 1 
ATOM   1472 N  N    . ALA   A 1 60  ? 29.490 11.286  9.839   1.00 11.26 ?  60  ALA   A N    1 
ATOM   1473 C  CA   . ALA   A 1 60  ? 30.727 10.608  10.206  1.00 11.45 ?  60  ALA   A CA   1 
ATOM   1474 C  C    . ALA   A 1 60  ? 30.959 9.365   9.353   1.00 11.57 ?  60  ALA   A C    1 
ATOM   1475 O  O    . ALA   A 1 60  ? 32.108 9.037   9.035   1.00 11.79 ?  60  ALA   A O    1 
ATOM   1476 C  CB   . ALA   A 1 60  ? 30.715 10.256  11.688  1.00 11.85 ?  60  ALA   A CB   1 
ATOM   1477 H  H    . ALA   A 1 60  ? 28.891 11.301  10.457  1.00 13.54 ?  60  ALA   A H    1 
ATOM   1478 H  HA   . ALA   A 1 60  ? 31.473 11.214  10.055  1.00 13.76 ?  60  ALA   A HA   1 
ATOM   1479 H  HB1  . ALA   A 1 60  ? 31.545 9.808   11.917  1.00 14.24 ?  60  ALA   A HB1  1 
ATOM   1480 H  HB2  . ALA   A 1 60  ? 30.632 11.074  12.209  1.00 14.24 ?  60  ALA   A HB2  1 
ATOM   1481 H  HB3  . ALA   A 1 60  ? 29.963 9.674   11.870  1.00 14.24 ?  60  ALA   A HB3  1 
ATOM   1482 N  N    . MET   A 1 61  ? 29.888 8.668   8.964   1.00 10.95 ?  61  MET   A N    1 
ATOM   1483 C  CA   . MET   A 1 61  ? 30.032 7.527   8.065   1.00 10.89 ?  61  MET   A CA   1 
ATOM   1484 C  C    . MET   A 1 61  ? 30.664 7.951   6.742   1.00 10.72 ?  61  MET   A C    1 
ATOM   1485 O  O    . MET   A 1 61  ? 31.560 7.273   6.227   1.00 10.96 ?  61  MET   A O    1 
ATOM   1486 C  CB   . MET   A 1 61  ? 28.668 6.863   7.851   1.00 10.85 ?  61  MET   A CB   1 
ATOM   1487 C  CG   . MET   A 1 61  ? 28.687 5.688   6.886   1.00 11.33 ?  61  MET   A CG   1 
ATOM   1488 S  SD   . MET   A 1 61  ? 27.061 4.952   6.666   1.00 12.18 ?  61  MET   A SD   1 
ATOM   1489 C  CE   . MET   A 1 61  ? 26.919 4.083   8.235   1.00 13.49 ?  61  MET   A CE   1 
ATOM   1490 H  H    . MET   A 1 61  ? 29.080 8.833   9.204   1.00 13.16 ?  61  MET   A H    1 
ATOM   1491 H  HA   . MET   A 1 61  ? 30.610 6.872   8.486   1.00 13.08 ?  61  MET   A HA   1 
ATOM   1492 H  HB2  . MET   A 1 61  ? 28.345 6.540   8.704   1.00 13.04 ?  61  MET   A HB2  1 
ATOM   1493 H  HB3  . MET   A 1 61  ? 28.054 7.525   7.496   1.00 13.04 ?  61  MET   A HB3  1 
ATOM   1494 H  HG2  . MET   A 1 61  ? 28.987 5.984   6.013   1.00 13.62 ?  61  MET   A HG2  1 
ATOM   1495 H  HG3  . MET   A 1 61  ? 29.276 4.998   7.226   1.00 13.62 ?  61  MET   A HG3  1 
ATOM   1496 H  HE1  . MET   A 1 61  ? 26.082 3.597   8.253   1.00 16.21 ?  61  MET   A HE1  1 
ATOM   1497 H  HE2  . MET   A 1 61  ? 27.664 3.478   8.329   1.00 16.21 ?  61  MET   A HE2  1 
ATOM   1498 H  HE3  . MET   A 1 61  ? 26.931 4.739   8.959   1.00 16.21 ?  61  MET   A HE3  1 
ATOM   1499 N  N    . GLN   A 1 62  ? 30.228 9.081   6.183   1.00 10.68 ?  62  GLN   A N    1 
ATOM   1500 C  CA   . GLN   A 1 62  ? 30.800 9.549   4.923   1.00 10.76 ?  62  GLN   A CA   1 
ATOM   1501 C  C    . GLN   A 1 62  ? 32.269 9.920   5.077   1.00 11.12 ?  62  GLN   A C    1 
ATOM   1502 O  O    . GLN   A 1 62  ? 33.081 9.595   4.206   1.00 11.34 ?  62  GLN   A O    1 
ATOM   1503 C  CB   . GLN   A 1 62  ? 30.006 10.733  4.375   1.00 11.14 ?  62  GLN   A CB   1 
ATOM   1504 C  CG   . GLN   A 1 62  ? 30.386 11.085  2.947   1.00 11.13 ?  62  GLN   A CG   1 
ATOM   1505 C  CD   . GLN   A 1 62  ? 30.058 9.959   1.997   1.00 11.09 ?  62  GLN   A CD   1 
ATOM   1506 O  OE1  . GLN   A 1 62  ? 28.878 9.648   1.783   1.00 11.65 ?  62  GLN   A OE1  1 
ATOM   1507 N  NE2  . GLN   A 1 62  ? 31.085 9.286   1.474   1.00 11.55 ?  62  GLN   A NE2  1 
ATOM   1508 H  H    . GLN   A 1 62  ? 29.609 9.582   6.509   1.00 12.84 ?  62  GLN   A H    1 
ATOM   1509 H  HA   . GLN   A 1 62  ? 30.747 8.826   4.280   1.00 12.94 ?  62  GLN   A HA   1 
ATOM   1510 H  HB2  . GLN   A 1 62  ? 29.061 10.518  4.394   1.00 13.39 ?  62  GLN   A HB2  1 
ATOM   1511 H  HB3  . GLN   A 1 62  ? 30.181 11.513  4.927   1.00 13.39 ?  62  GLN   A HB3  1 
ATOM   1512 H  HG2  . GLN   A 1 62  ? 29.884 11.858  2.662   1.00 13.37 ?  62  GLN   A HG2  1 
ATOM   1513 H  HG3  . GLN   A 1 62  ? 31.336 11.253  2.896   1.00 13.37 ?  62  GLN   A HG3  1 
ATOM   1514 H  HE21 . GLN   A 1 62  ? 31.894 9.516   1.664   1.00 13.88 ?  62  GLN   A HE21 1 
ATOM   1515 H  HE22 . GLN   A 1 62  ? 30.947 8.627   0.935   1.00 13.88 ?  62  GLN   A HE22 1 
ATOM   1516 N  N    . VAL   A 1 63  ? 32.625 10.609  6.162   1.00 11.71 ?  63  VAL   A N    1 
ATOM   1517 C  CA   . VAL   A 1 63  ? 34.015 11.003  6.380   1.00 12.30 ?  63  VAL   A CA   1 
ATOM   1518 C  C    . VAL   A 1 63  ? 34.910 9.766   6.452   1.00 11.41 ?  63  VAL   A C    1 
ATOM   1519 O  O    . VAL   A 1 63  ? 35.965 9.689   5.802   1.00 12.16 ?  63  VAL   A O    1 
ATOM   1520 C  CB   . VAL   A 1 63  ? 34.122 11.882  7.639   1.00 13.95 ?  63  VAL   A CB   1 
ATOM   1521 C  CG1  . VAL   A 1 63  ? 35.565 12.122  8.011   1.00 16.11 ?  63  VAL   A CG1  1 
ATOM   1522 C  CG2  . VAL   A 1 63  ? 33.402 13.219  7.411   1.00 14.25 ?  63  VAL   A CG2  1 
ATOM   1523 H  H    . VAL   A 1 63  ? 32.081 10.858  6.782   1.00 14.08 ?  63  VAL   A H    1 
ATOM   1524 H  HA   . VAL   A 1 63  ? 34.308 11.535  5.626   1.00 14.78 ?  63  VAL   A HA   1 
ATOM   1525 H  HB   . VAL   A 1 63  ? 33.691 11.434  8.383   1.00 16.76 ?  63  VAL   A HB   1 
ATOM   1526 H  HG11 . VAL   A 1 63  ? 35.606 12.860  8.640   1.00 19.36 ?  63  VAL   A HG11 1 
ATOM   1527 H  HG12 . VAL   A 1 63  ? 35.925 11.321  8.414   1.00 19.36 ?  63  VAL   A HG12 1 
ATOM   1528 H  HG13 . VAL   A 1 63  ? 36.060 12.347  7.207   1.00 19.36 ?  63  VAL   A HG13 1 
ATOM   1529 H  HG21 . VAL   A 1 63  ? 33.485 13.765  8.210   1.00 17.12 ?  63  VAL   A HG21 1 
ATOM   1530 H  HG22 . VAL   A 1 63  ? 33.813 13.676  6.658   1.00 17.12 ?  63  VAL   A HG22 1 
ATOM   1531 H  HG23 . VAL   A 1 63  ? 32.467 13.049  7.223   1.00 17.12 ?  63  VAL   A HG23 1 
ATOM   1532 N  N    . GLU   A 1 64  ? 34.485 8.764   7.228   1.00 11.60 ?  64  GLU   A N    1 
ATOM   1533 C  CA   . GLU   A 1 64  ? 35.248 7.525   7.332   1.00 11.49 ?  64  GLU   A CA   1 
ATOM   1534 C  C    . GLU   A 1 64  ? 35.347 6.833   5.979   1.00 11.42 ?  64  GLU   A C    1 
ATOM   1535 O  O    . GLU   A 1 64  ? 36.400 6.290   5.608   1.00 11.69 ?  64  GLU   A O    1 
ATOM   1536 C  CB   . GLU   A 1 64  ? 34.556 6.617   8.349   1.00 12.33 ?  64  GLU   A CB   1 
ATOM   1537 C  CG   . GLU   A 1 64  ? 35.204 5.266   8.498   1.00 12.59 ?  64  GLU   A CG   1 
ATOM   1538 C  CD   . GLU   A 1 64  ? 34.330 4.266   9.228   1.00 13.16 ?  64  GLU   A CD   1 
ATOM   1539 O  OE1  . GLU   A 1 64  ? 33.093 4.358   9.095   1.00 13.98 ?  64  GLU   A OE1  1 
ATOM   1540 O  OE2  . GLU   A 1 64  ? 34.877 3.368   9.907   1.00 13.18 -1 64  GLU   A OE2  1 
ATOM   1541 H  H    . GLU   A 1 64  ? 33.760 8.778   7.690   1.00 13.94 ?  64  GLU   A H    1 
ATOM   1542 H  HA   . GLU   A 1 64  ? 36.143 7.722   7.657   1.00 13.81 ?  64  GLU   A HA   1 
ATOM   1543 H  HB2  . GLU   A 1 64  ? 34.572 7.051   9.223   1.00 14.82 ?  64  GLU   A HB2  1 
ATOM   1544 H  HB3  . GLU   A 1 64  ? 33.635 6.486   8.072   1.00 14.82 ?  64  GLU   A HB3  1 
ATOM   1545 H  HG2  . GLU   A 1 64  ? 35.398 4.905   7.616   1.00 15.13 ?  64  GLU   A HG2  1 
ATOM   1546 H  HG3  . GLU   A 1 64  ? 36.022 5.370   8.998   1.00 15.13 ?  64  GLU   A HG3  1 
ATOM   1547 N  N    . SER   A 1 65  ? 34.232 6.822   5.243   1.00 11.24 ?  65  SER   A N    1 
ATOM   1548 C  CA   . SER   A 1 65  ? 34.178 6.161   3.944   1.00 11.20 ?  65  SER   A CA   1 
ATOM   1549 C  C    . SER   A 1 65  ? 35.104 6.819   2.928   1.00 11.18 ?  65  SER   A C    1 
ATOM   1550 O  O    . SER   A 1 65  ? 35.745 6.131   2.126   1.00 11.77 ?  65  SER   A O    1 
ATOM   1551 C  CB   . SER   A 1 65  ? 32.741 6.162   3.412   1.00 11.23 ?  65  SER   A CB   1 
ATOM   1552 O  OG   . SER   A 1 65  ? 31.887 5.354   4.212   1.00 11.39 ?  65  SER   A OG   1 
ATOM   1553 H  H    . SER   A 1 65  ? 33.495 7.199   5.479   1.00 13.51 ?  65  SER   A H    1 
ATOM   1554 H  HA   . SER   A 1 65  ? 34.459 5.240   4.050   1.00 13.46 ?  65  SER   A HA   1 
ATOM   1555 H  HB2  . SER   A 1 65  ? 32.406 7.070   3.414   1.00 13.50 ?  65  SER   A HB2  1 
ATOM   1556 H  HB3  . SER   A 1 65  ? 32.746 5.810   2.509   1.00 13.50 ?  65  SER   A HB3  1 
ATOM   1557 H  HG   . SER   A 1 65  ? 31.878 5.646   5.006   1.00 13.69 ?  65  SER   A HG   1 
ATOM   1558 N  N    . ASP   A 1 66  ? 35.179 8.152   2.931   1.00 11.36 ?  66  ASP   A N    1 
ATOM   1559 C  CA   . ASP   A 1 66  ? 36.046 8.843   1.979   1.00 12.23 ?  66  ASP   A CA   1 
ATOM   1560 C  C    . ASP   A 1 66  ? 37.508 8.501   2.235   1.00 12.32 ?  66  ASP   A C    1 
ATOM   1561 O  O    . ASP   A 1 66  ? 38.288 8.329   1.290   1.00 13.04 ?  66  ASP   A O    1 
ATOM   1562 C  CB   . ASP   A 1 66  ? 35.822 10.352  2.052   1.00 13.63 ?  66  ASP   A CB   1 
ATOM   1563 C  CG   . ASP   A 1 66  ? 34.490 10.797  1.437   1.00 15.17 ?  66  ASP   A CG   1 
ATOM   1564 O  OD1  . ASP   A 1 66  ? 33.794 9.993   0.780   1.00 15.09 ?  66  ASP   A OD1  1 
ATOM   1565 O  OD2  . ASP   A 1 66  ? 34.172 11.992  1.580   1.00 17.62 -1 66  ASP   A OD2  1 
ATOM   1566 H  H    . ASP   A 1 66  ? 34.737 8.671   3.460   1.00 13.65 ?  66  ASP   A H    1 
ATOM   1567 H  HA   . ASP   A 1 66  ? 35.819 8.549   1.083   1.00 14.70 ?  66  ASP   A HA   1 
ATOM   1568 H  HB2  . ASP   A 1 66  ? 35.832 10.627  2.982   1.00 16.38 ?  66  ASP   A HB2  1 
ATOM   1569 H  HB3  . ASP   A 1 66  ? 36.536 10.796  1.568   1.00 16.38 ?  66  ASP   A HB3  1 
ATOM   1570 N  N    . ASP   A 1 67  ? 37.894 8.384   3.505   1.00 12.36 ?  67  ASP   A N    1 
ATOM   1571 C  CA   . ASP   A 1 67  ? 39.248 7.938   3.819   1.00 13.32 ?  67  ASP   A CA   1 
ATOM   1572 C  C    . ASP   A 1 67  ? 39.477 6.502   3.356   1.00 13.28 ?  67  ASP   A C    1 
ATOM   1573 O  O    . ASP   A 1 67  ? 40.545 6.178   2.821   1.00 14.01 ?  67  ASP   A O    1 
ATOM   1574 C  CB   . ASP   A 1 67  ? 39.521 8.093   5.317   1.00 14.21 ?  67  ASP   A CB   1 
ATOM   1575 C  CG   . ASP   A 1 67  ? 40.804 7.418   5.749   1.00 15.75 ?  67  ASP   A CG   1 
ATOM   1576 O  OD1  . ASP   A 1 67  ? 41.880 8.047   5.630   1.00 18.69 ?  67  ASP   A OD1  1 
ATOM   1577 O  OD2  . ASP   A 1 67  ? 40.744 6.254   6.198   1.00 15.60 -1 67  ASP   A OD2  1 
ATOM   1578 H  H    . ASP   A 1 67  ? 37.406 8.562   4.187   1.00 14.85 ?  67  ASP   A H    1 
ATOM   1579 H  HA   . ASP   A 1 67  ? 39.881 8.501   3.346   1.00 16.01 ?  67  ASP   A HA   1 
ATOM   1580 H  HB2  . ASP   A 1 67  ? 39.596 9.034   5.525   1.00 17.08 ?  67  ASP   A HB2  1 
ATOM   1581 H  HB3  . ASP   A 1 67  ? 38.791 7.694   5.812   1.00 17.08 ?  67  ASP   A HB3  1 
ATOM   1582 N  N    . TYR   A 1 68  ? 38.481 5.623   3.541   1.00 13.18 ?  68  TYR   A N    1 
ATOM   1583 C  CA   . TYR   A 1 68  ? 38.614 4.241   3.077   1.00 12.88 ?  68  TYR   A CA   1 
ATOM   1584 C  C    . TYR   A 1 68  ? 38.859 4.187   1.570   1.00 12.73 ?  68  TYR   A C    1 
ATOM   1585 O  O    . TYR   A 1 68  ? 39.742 3.456   1.097   1.00 13.40 ?  68  TYR   A O    1 
ATOM   1586 C  CB   . TYR   A 1 68  ? 37.364 3.421   3.451   1.00 13.55 ?  68  TYR   A CB   1 
ATOM   1587 C  CG   . TYR   A 1 68  ? 37.397 2.029   2.831   1.00 15.33 ?  68  TYR   A CG   1 
ATOM   1588 C  CD1  . TYR   A 1 68  ? 36.936 1.824   1.534   1.00 16.77 ?  68  TYR   A CD1  1 
ATOM   1589 C  CD2  . TYR   A 1 68  ? 37.936 0.951   3.507   1.00 16.85 ?  68  TYR   A CD2  1 
ATOM   1590 C  CE1  . TYR   A 1 68  ? 37.006 0.605   0.925   1.00 18.20 ?  68  TYR   A CE1  1 
ATOM   1591 C  CE2  . TYR   A 1 68  ? 38.000 -0.312  2.899   1.00 17.85 ?  68  TYR   A CE2  1 
ATOM   1592 C  CZ   . TYR   A 1 68  ? 37.541 -0.457  1.607   1.00 18.50 ?  68  TYR   A CZ   1 
ATOM   1593 O  OH   . TYR   A 1 68  ? 37.619 -1.676  0.987   1.00 19.70 ?  68  TYR   A OH   1 
ATOM   1594 H  H    . TYR   A 1 68  ? 37.728 5.802   3.927   1.00 15.83 ?  68  TYR   A H    1 
ATOM   1595 H  HA   . TYR   A 1 68  ? 39.373 3.835   3.517   1.00 15.48 ?  68  TYR   A HA   1 
ATOM   1596 H  HB2  . TYR   A 1 68  ? 37.319 3.318   4.414   1.00 16.28 ?  68  TYR   A HB2  1 
ATOM   1597 H  HB3  . TYR   A 1 68  ? 36.568 3.876   3.126   1.00 16.28 ?  68  TYR   A HB3  1 
ATOM   1598 H  HD1  . TYR   A 1 68  ? 36.586 2.546   1.060   1.00 20.15 ?  68  TYR   A HD1  1 
ATOM   1599 H  HD2  . TYR   A 1 68  ? 38.265 1.061   4.367   1.00 20.24 ?  68  TYR   A HD2  1 
ATOM   1600 H  HE1  . TYR   A 1 68  ? 36.686 0.498   0.057   1.00 21.86 ?  68  TYR   A HE1  1 
ATOM   1601 H  HE2  . TYR   A 1 68  ? 38.369 -1.038  3.344   1.00 21.45 ?  68  TYR   A HE2  1 
ATOM   1602 H  HH   . TYR   A 1 68  ? 37.956 -2.240  1.512   1.00 23.66 ?  68  TYR   A HH   1 
ATOM   1603 N  N    . ILE   A 1 69  ? 38.072 4.940   0.796   1.00 12.47 ?  69  ILE   A N    1 
ATOM   1604 C  CA   . ILE   A 1 69  ? 38.207 4.922   -0.660  1.00 12.36 ?  69  ILE   A CA   1 
ATOM   1605 C  C    . ILE   A 1 69  ? 39.534 5.538   -1.091  1.00 12.35 ?  69  ILE   A C    1 
ATOM   1606 O  O    . ILE   A 1 69  ? 40.180 5.062   -2.032  1.00 12.70 ?  69  ILE   A O    1 
ATOM   1607 C  CB   . ILE   A 1 69  ? 37.010 5.631   -1.324  1.00 13.18 ?  69  ILE   A CB   1 
ATOM   1608 C  CG1  . ILE   A 1 69  ? 35.698 4.892   -1.041  1.00 13.83 ?  69  ILE   A CG1  1 
ATOM   1609 C  CG2  . ILE   A 1 69  ? 37.250 5.814   -2.834  1.00 14.65 ?  69  ILE   A CG2  1 
ATOM   1610 C  CD1  . ILE   A 1 69  ? 35.540 3.610   -1.807  1.00 14.84 ?  69  ILE   A CD1  1 
ATOM   1611 H  H    . ILE   A 1 69  ? 37.458 5.473   1.086   1.00 14.98 ?  69  ILE   A H    1 
ATOM   1612 H  HA   . ILE   A 1 69  ? 38.205 4.003   -0.958  1.00 14.86 ?  69  ILE   A HA   1 
ATOM   1613 H  HB   . ILE   A 1 69  ? 36.937 6.514   -0.936  1.00 15.84 ?  69  ILE   A HB   1 
ATOM   1614 H  HG12 . ILE   A 1 69  ? 35.665 4.680   -0.093  1.00 16.62 ?  69  ILE   A HG12 1 
ATOM   1615 H  HG13 . ILE   A 1 69  ? 34.959 5.475   -1.271  1.00 16.62 ?  69  ILE   A HG13 1 
ATOM   1616 H  HG21 . ILE   A 1 69  ? 36.402 6.016   -3.266  1.00 17.61 ?  69  ILE   A HG21 1 
ATOM   1617 H  HG22 . ILE   A 1 69  ? 37.865 6.557   -2.970  1.00 17.61 ?  69  ILE   A HG22 1 
ATOM   1618 H  HG23 . ILE   A 1 69  ? 37.622 5.002   -3.201  1.00 17.61 ?  69  ILE   A HG23 1 
ATOM   1619 H  HD11 . ILE   A 1 69  ? 34.750 3.153   -1.485  1.00 17.83 ?  69  ILE   A HD11 1 
ATOM   1620 H  HD12 . ILE   A 1 69  ? 35.439 3.819   -2.750  1.00 17.83 ?  69  ILE   A HD12 1 
ATOM   1621 H  HD13 . ILE   A 1 69  ? 36.323 3.059   -1.669  1.00 17.83 ?  69  ILE   A HD13 1 
ATOM   1622 N  N    . ALA   A 1 70  ? 39.943 6.625   -0.442  1.00 12.92 ?  70  ALA   A N    1 
ATOM   1623 C  CA   . ALA   A 1 70  ? 41.222 7.240   -0.790  1.00 13.74 ?  70  ALA   A CA   1 
ATOM   1624 C  C    . ALA   A 1 70  ? 42.381 6.268   -0.611  1.00 14.25 ?  70  ALA   A C    1 
ATOM   1625 O  O    . ALA   A 1 70  ? 43.369 6.336   -1.346  1.00 16.45 ?  70  ALA   A O    1 
ATOM   1626 C  CB   . ALA   A 1 70  ? 41.444 8.496   0.055   1.00 14.59 ?  70  ALA   A CB   1 
ATOM   1627 H  H    . ALA   A 1 70  ? 39.508 7.023   0.182   1.00 15.53 ?  70  ALA   A H    1 
ATOM   1628 H  HA   . ALA   A 1 70  ? 41.198 7.516   -1.724  1.00 16.51 ?  70  ALA   A HA   1 
ATOM   1629 H  HB1  . ALA   A 1 70  ? 42.301 8.890   -0.186  1.00 17.53 ?  70  ALA   A HB1  1 
ATOM   1630 H  HB2  . ALA   A 1 70  ? 40.731 9.127   -0.116  1.00 17.53 ?  70  ALA   A HB2  1 
ATOM   1631 H  HB3  . ALA   A 1 70  ? 41.452 8.245   0.992   1.00 17.53 ?  70  ALA   A HB3  1 
ATOM   1632 N  N    . THR   A 1 71  ? 42.272 5.349   0.341   1.00 13.78 ?  71  THR   A N    1 
ATOM   1633 C  CA   . THR   A 1 71  ? 43.324 4.375   0.604   1.00 15.84 ?  71  THR   A CA   1 
ATOM   1634 C  C    . THR   A 1 71  ? 43.216 3.139   -0.277  1.00 16.15 ?  71  THR   A C    1 
ATOM   1635 O  O    . THR   A 1 71  ? 44.236 2.618   -0.750  1.00 18.04 ?  71  THR   A O    1 
ATOM   1636 C  CB   . THR   A 1 71  ? 43.245 3.936   2.065   1.00 18.34 ?  71  THR   A CB   1 
ATOM   1637 O  OG1  . THR   A 1 71  ? 43.480 5.065   2.913   1.00 19.87 ?  71  THR   A OG1  1 
ATOM   1638 C  CG2  . THR   A 1 71  ? 44.256 2.828   2.372   1.00 19.76 ?  71  THR   A CG2  1 
ATOM   1639 H  H    . THR   A 1 71  ? 41.577 5.259   0.844   1.00 16.56 ?  71  THR   A H    1 
ATOM   1640 H  HA   . THR   A 1 71  ? 44.185 4.786   0.446   1.00 19.03 ?  71  THR   A HA   1 
ATOM   1641 H  HB   . THR   A 1 71  ? 42.354 3.584   2.237   1.00 22.02 ?  71  THR   A HB   1 
ATOM   1642 H  HG1  . THR   A 1 71  ? 42.897 5.650   2.769   1.00 23.86 ?  71  THR   A HG1  1 
ATOM   1643 H  HG21 . THR   A 1 71  ? 44.381 2.755   3.330   1.00 23.73 ?  71  THR   A HG21 1 
ATOM   1644 H  HG22 . THR   A 1 71  ? 43.938 1.976   2.032   1.00 23.73 ?  71  THR   A HG22 1 
ATOM   1645 H  HG23 . THR   A 1 71  ? 45.109 3.034   1.958   1.00 23.73 ?  71  THR   A HG23 1 
ATOM   1646 N  N    . ASN   A 1 72  ? 41.996 2.639   -0.485  1.00 14.67 ?  72  ASN   A N    1 
ATOM   1647 C  CA   . ASN   A 1 72  ? 41.779 1.312   -1.046  1.00 15.22 ?  72  ASN   A CA   1 
ATOM   1648 C  C    . ASN   A 1 72  ? 41.164 1.301   -2.433  1.00 15.16 ?  72  ASN   A C    1 
ATOM   1649 O  O    . ASN   A 1 72  ? 41.165 0.245   -3.078  1.00 15.77 ?  72  ASN   A O    1 
ATOM   1650 C  CB   . ASN   A 1 72  ? 40.889 0.487   -0.108  1.00 16.15 ?  72  ASN   A CB   1 
ATOM   1651 C  CG   . ASN   A 1 72  ? 41.502 0.333   1.255   1.00 17.01 ?  72  ASN   A CG   1 
ATOM   1652 O  OD1  . ASN   A 1 72  ? 41.040 0.922   2.227   1.00 18.68 ?  72  ASN   A OD1  1 
ATOM   1653 N  ND2  . ASN   A 1 72  ? 42.565 -0.446  1.334   1.00 17.67 ?  72  ASN   A ND2  1 
ATOM   1654 H  H    . ASN   A 1 72  ? 41.260 3.058   -0.302  1.00 17.63 ?  72  ASN   A H    1 
ATOM   1655 H  HA   . ASN   A 1 72  ? 42.634 0.865   -1.110  1.00 18.29 ?  72  ASN   A HA   1 
ATOM   1656 H  HB2  . ASN   A 1 72  ? 40.033 0.925   -0.010  1.00 19.40 ?  72  ASN   A HB2  1 
ATOM   1657 H  HB3  . ASN   A 1 72  ? 40.772 -0.401  -0.487  1.00 19.40 ?  72  ASN   A HB3  1 
ATOM   1658 H  HD21 . ASN   A 1 72  ? 42.961 -0.560  2.092   1.00 21.23 ?  72  ASN   A HD21 1 
ATOM   1659 H  HD22 . ASN   A 1 72  ? 42.871 -0.835  0.630   1.00 21.23 ?  72  ASN   A HD22 1 
ATOM   1660 N  N    . GLY   A 1 73  ? 40.616 2.415   -2.898  1.00 14.40 ?  73  GLY   A N    1 
ATOM   1661 C  CA   . GLY   A 1 73  ? 39.885 2.424   -4.138  1.00 14.28 ?  73  GLY   A CA   1 
ATOM   1662 C  C    . GLY   A 1 73  ? 38.495 1.850   -3.962  1.00 13.45 ?  73  GLY   A C    1 
ATOM   1663 O  O    . GLY   A 1 73  ? 38.110 1.411   -2.874  1.00 13.83 ?  73  GLY   A O    1 
ATOM   1664 H  H    . GLY   A 1 73  ? 40.667 3.194   -2.517  1.00 17.30 ?  73  GLY   A H    1 
ATOM   1665 H  HA2  . GLY   A 1 73  ? 39.807 3.337   -4.464  1.00 17.16 ?  73  GLY   A HA2  1 
ATOM   1666 H  HA3  . GLY   A 1 73  ? 40.355 1.898   -4.800  1.00 17.16 ?  73  GLY   A HA3  1 
ATOM   1667 N  N    . PRO   A 1 74  ? 37.720 1.851   -5.042  1.00 13.53 ?  74  PRO   A N    1 
ATOM   1668 C  CA   . PRO   A 1 74  ? 36.319 1.424   -4.956  1.00 13.79 ?  74  PRO   A CA   1 
ATOM   1669 C  C    . PRO   A 1 74  ? 36.173 -0.058  -4.636  1.00 13.00 ?  74  PRO   A C    1 
ATOM   1670 O  O    . PRO   A 1 74  ? 37.042 -0.888  -4.920  1.00 14.11 ?  74  PRO   A O    1 
ATOM   1671 C  CB   . PRO   A 1 74  ? 35.774 1.717   -6.359  1.00 15.53 ?  74  PRO   A CB   1 
ATOM   1672 C  CG   . PRO   A 1 74  ? 36.727 2.674   -6.974  1.00 18.39 ?  74  PRO   A CG   1 
ATOM   1673 C  CD   . PRO   A 1 74  ? 38.063 2.352   -6.382  1.00 15.86 ?  74  PRO   A CD   1 
ATOM   1674 H  HA   . PRO   A 1 74  ? 35.836 1.950   -4.294  1.00 16.57 ?  74  PRO   A HA   1 
ATOM   1675 H  HB2  . PRO   A 1 74  ? 35.732 0.892   -6.865  1.00 18.66 ?  74  PRO   A HB2  1 
ATOM   1676 H  HB3  . PRO   A 1 74  ? 34.889 2.114   -6.281  1.00 18.66 ?  74  PRO   A HB3  1 
ATOM   1677 H  HG2  . PRO   A 1 74  ? 36.747 2.547   -7.933  1.00 22.09 ?  74  PRO   A HG2  1 
ATOM   1678 H  HG3  . PRO   A 1 74  ? 36.473 3.582   -6.751  1.00 22.09 ?  74  PRO   A HG3  1 
ATOM   1679 H  HD2  . PRO   A 1 74  ? 38.508 1.656   -6.894  1.00 19.06 ?  74  PRO   A HD2  1 
ATOM   1680 H  HD3  . PRO   A 1 74  ? 38.608 3.151   -6.323  1.00 19.06 ?  74  PRO   A HD3  1 
ATOM   1681 N  N    . LEU   A 1 75  ? 35.025 -0.382  -4.051  1.00 12.49 ?  75  LEU   A N    1 
ATOM   1682 C  CA   . LEU   A 1 75  ? 34.631 -1.772  -3.903  1.00 11.86 ?  75  LEU   A CA   1 
ATOM   1683 C  C    . LEU   A 1 75  ? 34.255 -2.354  -5.264  1.00 12.31 ?  75  LEU   A C    1 
ATOM   1684 O  O    . LEU   A 1 75  ? 34.113 -1.641  -6.261  1.00 13.86 ?  75  LEU   A O    1 
ATOM   1685 C  CB   . LEU   A 1 75  ? 33.440 -1.892  -2.954  1.00 12.35 ?  75  LEU   A CB   1 
ATOM   1686 C  CG   . LEU   A 1 75  ? 33.651 -1.486  -1.497  1.00 13.76 ?  75  LEU   A CG   1 
ATOM   1687 C  CD1  . LEU   A 1 75  ? 32.361 -1.688  -0.711  1.00 15.40 ?  75  LEU   A CD1  1 
ATOM   1688 C  CD2  . LEU   A 1 75  ? 34.792 -2.213  -0.848  1.00 17.45 ?  75  LEU   A CD2  1 
ATOM   1689 H  H    . LEU   A 1 75  ? 34.456 0.186   -3.737  1.00 15.01 ?  75  LEU   A H    1 
ATOM   1690 H  HA   . LEU   A 1 75  ? 35.368 -2.282  -3.546  1.00 14.25 ?  75  LEU   A HA   1 
ATOM   1691 H  HB2  . LEU   A 1 75  ? 32.719 -1.346  -3.301  1.00 14.84 ?  75  LEU   A HB2  1 
ATOM   1692 H  HB3  . LEU   A 1 75  ? 33.156 -2.824  -2.949  1.00 14.84 ?  75  LEU   A HB3  1 
ATOM   1693 H  HG   . LEU   A 1 75  ? 33.867 -0.538  -1.477  1.00 16.54 ?  75  LEU   A HG   1 
ATOM   1694 H  HD11 . LEU   A 1 75  ? 32.513 -1.421  0.209   1.00 18.50 ?  75  LEU   A HD11 1 
ATOM   1695 H  HD12 . LEU   A 1 75  ? 31.667 -1.139  -1.106  1.00 18.50 ?  75  LEU   A HD12 1 
ATOM   1696 H  HD13 . LEU   A 1 75  ? 32.114 -2.622  -0.751  1.00 18.50 ?  75  LEU   A HD13 1 
ATOM   1697 H  HD21 . LEU   A 1 75  ? 34.841 -1.957  0.086   1.00 20.96 ?  75  LEU   A HD21 1 
ATOM   1698 H  HD22 . LEU   A 1 75  ? 34.644 -3.168  -0.923  1.00 20.96 ?  75  LEU   A HD22 1 
ATOM   1699 H  HD23 . LEU   A 1 75  ? 35.623 -1.973  -1.296  1.00 20.96 ?  75  LEU   A HD23 1 
ATOM   1700 N  N    . LYS   A 1 76  ? 34.097 -3.678  -5.290  1.00 12.32 ?  76  LYS   A N    1 
ATOM   1701 C  CA   . LYS   A 1 76  ? 33.507 -4.399  -6.410  1.00 12.94 ?  76  LYS   A CA   1 
ATOM   1702 C  C    . LYS   A 1 76  ? 31.993 -4.465  -6.232  1.00 11.88 ?  76  LYS   A C    1 
ATOM   1703 O  O    . LYS   A 1 76  ? 31.500 -4.577  -5.110  1.00 11.83 ?  76  LYS   A O    1 
ATOM   1704 C  CB   . LYS   A 1 76  ? 34.039 -5.841  -6.442  1.00 14.29 ?  76  LYS   A CB   1 
ATOM   1705 C  CG   . LYS   A 1 76  ? 35.540 -5.949  -6.667  1.00 15.58 ?  76  LYS   A CG   1 
ATOM   1706 C  CD   . LYS   A 1 76  ? 36.059 -7.350  -6.417  1.00 16.99 ?  76  LYS   A CD   1 
ATOM   1707 C  CE   . LYS   A 1 76  ? 37.560 -7.416  -6.620  1.00 19.46 ?  76  LYS   A CE   1 
ATOM   1708 N  NZ   . LYS   A 1 76  ? 38.106 -8.765  -6.377  1.00 20.45 ?  76  LYS   A NZ   1 
ATOM   1709 H  H    . LYS   A 1 76  ? 34.331 -4.200  -4.642  1.00 14.81 ?  76  LYS   A H    1 
ATOM   1710 H  HA   . LYS   A 1 76  ? 33.719 -3.958  -7.247  1.00 15.55 ?  76  LYS   A HA   1 
ATOM   1711 H  HB2  . LYS   A 1 76  ? 33.839 -6.265  -5.592  1.00 17.17 ?  76  LYS   A HB2  1 
ATOM   1712 H  HB3  . LYS   A 1 76  ? 33.599 -6.320  -7.159  1.00 17.17 ?  76  LYS   A HB3  1 
ATOM   1713 H  HG2  . LYS   A 1 76  ? 35.744 -5.716  -7.586  1.00 18.71 ?  76  LYS   A HG2  1 
ATOM   1714 H  HG3  . LYS   A 1 76  ? 36.002 -5.350  -6.060  1.00 18.71 ?  76  LYS   A HG3  1 
ATOM   1715 H  HD2  . LYS   A 1 76  ? 35.861 -7.612  -5.503  1.00 20.42 ?  76  LYS   A HD2  1 
ATOM   1716 H  HD3  . LYS   A 1 76  ? 35.637 -7.968  -7.039  1.00 20.42 ?  76  LYS   A HD3  1 
ATOM   1717 H  HE2  . LYS   A 1 76  ? 37.766 -7.171  -7.534  1.00 23.37 ?  76  LYS   A HE2  1 
ATOM   1718 H  HE3  . LYS   A 1 76  ? 37.989 -6.807  -6.003  1.00 23.37 ?  76  LYS   A HE3  1 
ATOM   1719 H  HZ1  . LYS   A 1 76  ? 38.989 -8.772  -6.507  1.00 24.56 ?  76  LYS   A HZ1  1 
ATOM   1720 H  HZ2  . LYS   A 1 76  ? 37.938 -9.026  -5.541  1.00 24.56 ?  76  LYS   A HZ2  1 
ATOM   1721 H  HZ3  . LYS   A 1 76  ? 37.735 -9.358  -6.937  1.00 24.56 ?  76  LYS   A HZ3  1 
ATOM   1722 N  N    . VAL   A 1 77  ? 31.255 -4.441  -7.347  1.00 12.55 ?  77  VAL   A N    1 
ATOM   1723 C  CA   . VAL   A 1 77  ? 29.844 -4.822  -7.271  1.00 12.37 ?  77  VAL   A CA   1 
ATOM   1724 C  C    . VAL   A 1 77  ? 29.774 -6.276  -6.828  1.00 12.36 ?  77  VAL   A C    1 
ATOM   1725 O  O    . VAL   A 1 77  ? 30.433 -7.149  -7.407  1.00 12.76 ?  77  VAL   A O    1 
ATOM   1726 C  CB   . VAL   A 1 77  ? 29.133 -4.614  -8.615  1.00 13.55 ?  77  VAL   A CB   1 
ATOM   1727 C  CG1  . VAL   A 1 77  ? 27.669 -5.031  -8.510  1.00 14.55 ?  77  VAL   A CG1  1 
ATOM   1728 C  CG2  . VAL   A 1 77  ? 29.243 -3.166  -9.054  1.00 15.11 ?  77  VAL   A CG2  1 
ATOM   1729 H  H    . VAL   A 1 77  ? 31.535 -4.210  -8.127  1.00 15.08 ?  77  VAL   A H    1 
ATOM   1730 H  HA   . VAL   A 1 77  ? 29.400 -4.277  -6.603  1.00 14.87 ?  77  VAL   A HA   1 
ATOM   1731 H  HB   . VAL   A 1 77  ? 29.559 -5.163  -9.290  1.00 16.28 ?  77  VAL   A HB   1 
ATOM   1732 H  HG11 . VAL   A 1 77  ? 27.202 -4.735  -9.306  1.00 17.49 ?  77  VAL   A HG11 1 
ATOM   1733 H  HG12 . VAL   A 1 77  ? 27.622 -5.996  -8.437  1.00 17.49 ?  77  VAL   A HG12 1 
ATOM   1734 H  HG13 . VAL   A 1 77  ? 27.281 -4.617  -7.724  1.00 17.49 ?  77  VAL   A HG13 1 
ATOM   1735 H  HG21 . VAL   A 1 77  ? 28.730 -3.042  -9.866  1.00 18.16 ?  77  VAL   A HG21 1 
ATOM   1736 H  HG22 . VAL   A 1 77  ? 28.893 -2.596  -8.350  1.00 18.16 ?  77  VAL   A HG22 1 
ATOM   1737 H  HG23 . VAL   A 1 77  ? 30.176 -2.953  -9.216  1.00 18.16 ?  77  VAL   A HG23 1 
ATOM   1738 N  N    . GLY   A 1 78  ? 28.988 -6.540  -5.782  1.00 11.29 ?  78  GLY   A N    1 
ATOM   1739 C  CA   . GLY   A 1 78  ? 28.955 -7.829  -5.123  1.00 12.22 ?  78  GLY   A CA   1 
ATOM   1740 C  C    . GLY   A 1 78  ? 29.858 -7.921  -3.912  1.00 11.82 ?  78  GLY   A C    1 
ATOM   1741 O  O    . GLY   A 1 78  ? 29.791 -8.923  -3.184  1.00 12.38 ?  78  GLY   A O    1 
ATOM   1742 H  H    . GLY   A 1 78  ? 28.446 -5.964  -5.438  1.00 13.57 ?  78  GLY   A H    1 
ATOM   1743 H  HA2  . GLY   A 1 78  ? 28.046 -8.015  -4.842  1.00 14.69 ?  78  GLY   A HA2  1 
ATOM   1744 H  HA3  . GLY   A 1 78  ? 29.223 -8.513  -5.757  1.00 14.69 ?  78  GLY   A HA3  1 
ATOM   1745 N  N    . GLY   A 1 79  ? 30.708 -6.914  -3.683  1.00 11.35 ?  79  GLY   A N    1 
ATOM   1746 C  CA   . GLY   A 1 79  ? 31.663 -6.930  -2.599  1.00 11.75 ?  79  GLY   A CA   1 
ATOM   1747 C  C    . GLY   A 1 79  ? 31.203 -6.137  -1.389  1.00 10.87 ?  79  GLY   A C    1 
ATOM   1748 O  O    . GLY   A 1 79  ? 30.087 -5.615  -1.328  1.00 11.54 ?  79  GLY   A O    1 
ATOM   1749 H  H    . GLY   A 1 79  ? 30.748 -6.197  -4.162  1.00 13.64 ?  79  GLY   A H    1 
ATOM   1750 H  HA2  . GLY   A 1 79  ? 31.819 -7.855  -2.327  1.00 14.13 ?  79  GLY   A HA2  1 
ATOM   1751 H  HA3  . GLY   A 1 79  ? 32.507 -6.565  -2.907  1.00 14.13 ?  79  GLY   A HA3  1 
ATOM   1752 N  N    . SER   A 1 80  ? 32.100 -6.040  -0.407  1.00 11.82 ?  80  SER   A N    1 
ATOM   1753 C  CA   . SER   A 1 80  ? 31.770 -5.401  0.860   1.00 11.36 ?  80  SER   A CA   1 
ATOM   1754 C  C    . SER   A 1 80  ? 33.038 -4.946  1.566   1.00 11.33 ?  80  SER   A C    1 
ATOM   1755 O  O    . SER   A 1 80  ? 34.153 -5.388  1.252   1.00 12.66 ?  80  SER   A O    1 
ATOM   1756 C  CB   . SER   A 1 80  ? 31.009 -6.357  1.785   1.00 12.20 ?  80  SER   A CB   1 
ATOM   1757 O  OG   . SER   A 1 80  ? 31.830 -7.410  2.265   1.00 13.65 ?  80  SER   A OG   1 
ATOM   1758 H  H    . SER   A 1 80  ? 32.911 -6.328  -0.455  1.00 14.20 ?  80  SER   A H    1 
ATOM   1759 H  HA   . SER   A 1 80  ? 31.217 -4.626  0.678   1.00 13.66 ?  80  SER   A HA   1 
ATOM   1760 H  HB2  . SER   A 1 80  ? 30.675 -5.852  2.544   1.00 14.66 ?  80  SER   A HB2  1 
ATOM   1761 H  HB3  . SER   A 1 80  ? 30.268 -6.741  1.294   1.00 14.66 ?  80  SER   A HB3  1 
ATOM   1762 H  HG   . SER   A 1 80  ? 32.134 -7.853  1.618   1.00 16.41 ?  80  SER   A HG   1 
ATOM   1763 N  N    . CYS   A 1 81  ? 32.842 -4.091  2.570   1.00 11.18 ?  81  CYS   A N    1 
ATOM   1764 C  CA   . CYS   A 1 81  ? 33.886 -3.809  3.542   1.00 11.35 ?  81  CYS   A CA   1 
ATOM   1765 C  C    . CYS   A 1 81  ? 33.240 -3.575  4.901   1.00 11.07 ?  81  CYS   A C    1 
ATOM   1766 O  O    . CYS   A 1 81  ? 32.073 -3.174  4.985   1.00 12.22 ?  81  CYS   A O    1 
ATOM   1767 C  CB   . CYS   A 1 81  ? 34.751 -2.613  3.126   1.00 12.28 ?  81  CYS   A CB   1 
ATOM   1768 S  SG   . CYS   A 1 81  ? 33.863 -1.042  3.120   1.00 12.27 ?  81  CYS   A SG   1 
ATOM   1769 H  H    . CYS   A 1 81  ? 32.107 -3.666  2.715   1.00 13.43 ?  81  CYS   A H    1 
ATOM   1770 H  HA   . CYS   A 1 81  ? 34.470 -4.580  3.612   1.00 13.65 ?  81  CYS   A HA   1 
ATOM   1771 H  HB2  . CYS   A 1 81  ? 35.501 -2.534  3.742   1.00 14.75 ?  81  CYS   A HB2  1 
ATOM   1772 H  HB3  . CYS   A 1 81  ? 35.091 -2.763  2.226   1.00 14.75 ?  81  CYS   A HB3  1 
ATOM   1773 H  HG   . CYS   A 1 81  ? 34.614 -0.168  2.794   1.00 14.74 ?  81  CYS   A HG   1 
ATOM   1774 N  N    . VAL   A 1 82  ? 34.005 -3.842  5.958   1.00 11.36 ?  82  VAL   A N    1 
ATOM   1775 C  CA   . VAL   A 1 82  ? 33.579 -3.595  7.329   1.00 11.75 ?  82  VAL   A CA   1 
ATOM   1776 C  C    . VAL   A 1 82  ? 34.174 -2.280  7.800   1.00 12.08 ?  82  VAL   A C    1 
ATOM   1777 O  O    . VAL   A 1 82  ? 35.396 -2.106  7.793   1.00 12.81 ?  82  VAL   A O    1 
ATOM   1778 C  CB   . VAL   A 1 82  ? 33.995 -4.737  8.267   1.00 13.04 ?  82  VAL   A CB   1 
ATOM   1779 C  CG1  . VAL   A 1 82  ? 33.535 -4.451  9.685   1.00 14.65 ?  82  VAL   A CG1  1 
ATOM   1780 C  CG2  . VAL   A 1 82  ? 33.448 -6.065  7.770   1.00 14.53 ?  82  VAL   A CG2  1 
ATOM   1781 H  H    . VAL   A 1 82  ? 34.801 -4.186  5.899   1.00 13.66 ?  82  VAL   A H    1 
ATOM   1782 H  HA   . VAL   A 1 82  ? 32.614 -3.512  7.345   1.00 14.12 ?  82  VAL   A HA   1 
ATOM   1783 H  HB   . VAL   A 1 82  ? 34.962 -4.790  8.274   1.00 15.67 ?  82  VAL   A HB   1 
ATOM   1784 H  HG11 . VAL   A 1 82  ? 33.640 -5.255  10.216  1.00 17.60 ?  82  VAL   A HG11 1 
ATOM   1785 H  HG12 . VAL   A 1 82  ? 34.070 -3.734  10.062  1.00 17.60 ?  82  VAL   A HG12 1 
ATOM   1786 H  HG13 . VAL   A 1 82  ? 32.598 -4.189  9.670   1.00 17.60 ?  82  VAL   A HG13 1 
ATOM   1787 H  HG21 . VAL   A 1 82  ? 33.677 -6.755  8.411   1.00 17.46 ?  82  VAL   A HG21 1 
ATOM   1788 H  HG22 . VAL   A 1 82  ? 32.484 -5.998  7.685   1.00 17.46 ?  82  VAL   A HG22 1 
ATOM   1789 H  HG23 . VAL   A 1 82  ? 33.843 -6.268  6.908   1.00 17.46 ?  82  VAL   A HG23 1 
ATOM   1790 N  N    . LEU   A 1 83  ? 33.315 -1.359  8.207   1.00 11.61 ?  83  LEU   A N    1 
ATOM   1791 C  CA   . LEU   A 1 83  ? 33.730 -0.090  8.780   1.00 11.47 ?  83  LEU   A CA   1 
ATOM   1792 C  C    . LEU   A 1 83  ? 33.007 0.095   10.110  1.00 11.60 ?  83  LEU   A C    1 
ATOM   1793 O  O    . LEU   A 1 83  ? 32.279 -0.790  10.578  1.00 12.23 ?  83  LEU   A O    1 
ATOM   1794 C  CB   . LEU   A 1 83  ? 33.487 1.069   7.800   1.00 12.14 ?  83  LEU   A CB   1 
ATOM   1795 C  CG   . LEU   A 1 83  ? 34.382 1.061   6.555   1.00 12.86 ?  83  LEU   A CG   1 
ATOM   1796 C  CD1  . LEU   A 1 83  ? 33.945 2.119   5.563   1.00 13.58 ?  83  LEU   A CD1  1 
ATOM   1797 C  CD2  . LEU   A 1 83  ? 35.850 1.279   6.931   1.00 13.70 ?  83  LEU   A CD2  1 
ATOM   1798 H  H    . LEU   A 1 83  ? 32.463 -1.442  8.151   1.00 13.96 ?  83  LEU   A H    1 
ATOM   1799 H  HA   . LEU   A 1 83  ? 34.684 -0.114  8.960   1.00 13.79 ?  83  LEU   A HA   1 
ATOM   1800 H  HB2  . LEU   A 1 83  ? 32.566 1.033   7.492   1.00 14.59 ?  83  LEU   A HB2  1 
ATOM   1801 H  HB3  . LEU   A 1 83  ? 33.638 1.912   8.258   1.00 14.59 ?  83  LEU   A HB3  1 
ATOM   1802 H  HG   . LEU   A 1 83  ? 34.312 0.200   6.120   1.00 15.45 ?  83  LEU   A HG   1 
ATOM   1803 H  HD11 . LEU   A 1 83  ? 34.526 2.085   4.786   1.00 16.32 ?  83  LEU   A HD11 1 
ATOM   1804 H  HD12 . LEU   A 1 83  ? 33.029 1.942   5.297   1.00 16.32 ?  83  LEU   A HD12 1 
ATOM   1805 H  HD13 . LEU   A 1 83  ? 34.005 2.992   5.983   1.00 16.32 ?  83  LEU   A HD13 1 
ATOM   1806 H  HD21 . LEU   A 1 83  ? 36.371 1.425   6.122   1.00 16.46 ?  83  LEU   A HD21 1 
ATOM   1807 H  HD22 . LEU   A 1 83  ? 35.920 2.062   7.506   1.00 16.46 ?  83  LEU   A HD22 1 
ATOM   1808 H  HD23 . LEU   A 1 83  ? 36.182 0.499   7.398   1.00 16.46 ?  83  LEU   A HD23 1 
ATOM   1809 N  N    . SER   A 1 84  ? 33.214 1.248   10.736  1.00 12.40 ?  84  SER   A N    1 
ATOM   1810 C  CA   . SER   A 1 84  ? 32.564 1.512   12.009  1.00 12.49 ?  84  SER   A CA   1 
ATOM   1811 C  C    . SER   A 1 84  ? 31.045 1.603   11.852  1.00 12.46 ?  84  SER   A C    1 
ATOM   1812 O  O    . SER   A 1 84  ? 30.528 2.060   10.833  1.00 12.60 ?  84  SER   A O    1 
ATOM   1813 C  CB   . SER   A 1 84  ? 33.065 2.834   12.581  1.00 13.70 ?  84  SER   A CB   1 
ATOM   1814 O  OG   . SER   A 1 84  ? 32.430 3.124   13.810  1.00 14.57 ?  84  SER   A OG   1 
ATOM   1815 H  H    . SER   A 1 84  ? 33.718 1.889   10.444  1.00 14.91 ?  84  SER   A H    1 
ATOM   1816 H  HA   . SER   A 1 84  ? 32.779 0.798   12.629  1.00 15.01 ?  84  SER   A HA   1 
ATOM   1817 H  HB2  . SER   A 1 84  ? 34.029 2.772   12.713  1.00 16.47 ?  84  SER   A HB2  1 
ATOM   1818 H  HB3  . SER   A 1 84  ? 32.866 3.543   11.954  1.00 16.47 ?  84  SER   A HB3  1 
ATOM   1819 H  HG   . SER   A 1 84  ? 32.734 3.842   14.121  1.00 17.51 ?  84  SER   A HG   1 
ATOM   1820 N  N    . GLY   A 1 85  ? 30.328 1.197   12.900  1.00 12.97 ?  85  GLY   A N    1 
ATOM   1821 C  CA   . GLY   A 1 85  ? 28.905 1.440   12.981  1.00 14.00 ?  85  GLY   A CA   1 
ATOM   1822 C  C    . GLY   A 1 85  ? 28.538 2.759   13.628  1.00 13.37 ?  85  GLY   A C    1 
ATOM   1823 O  O    . GLY   A 1 85  ? 27.347 3.068   13.745  1.00 14.28 ?  85  GLY   A O    1 
ATOM   1824 H  H    . GLY   A 1 85  ? 30.649 0.768   13.576  1.00 15.59 ?  85  GLY   A H    1 
ATOM   1825 H  HA2  . GLY   A 1 85  ? 28.531 1.433   12.085  1.00 16.82 ?  85  GLY   A HA2  1 
ATOM   1826 H  HA3  . GLY   A 1 85  ? 28.486 0.732   13.488  1.00 16.82 ?  85  GLY   A HA3  1 
ATOM   1827 N  N    . HIS   A 1 86  ? 29.522 3.537   14.072  1.00 13.14 ?  86  HIS   A N    1 
ATOM   1828 C  CA   . HIS   A 1 86  ? 29.290 4.879   14.625  1.00 13.44 ?  86  HIS   A CA   1 
ATOM   1829 C  C    . HIS   A 1 86  ? 28.294 4.759   15.771  1.00 14.31 ?  86  HIS   A C    1 
ATOM   1830 O  O    . HIS   A 1 86  ? 28.476 3.887   16.636  1.00 15.85 ?  86  HIS   A O    1 
ATOM   1831 C  CB   . HIS   A 1 86  ? 28.919 5.839   13.504  1.00 13.64 ?  86  HIS   A CB   1 
ATOM   1832 C  CG   . HIS   A 1 86  ? 29.987 5.938   12.474  1.00 13.63 ?  86  HIS   A CG   1 
ATOM   1833 N  ND1  . HIS   A 1 86  ? 31.073 6.778   12.612  1.00 14.42 ?  86  HIS   A ND1  1 
ATOM   1834 C  CD2  . HIS   A 1 86  ? 30.185 5.240   11.332  1.00 13.33 ?  86  HIS   A CD2  1 
ATOM   1835 C  CE1  . HIS   A 1 86  ? 31.880 6.606   11.580  1.00 14.28 ?  86  HIS   A CE1  1 
ATOM   1836 N  NE2  . HIS   A 1 86  ? 31.370 5.674   10.796  1.00 13.80 ?  86  HIS   A NE2  1 
ATOM   1837 H  H    . HIS   A 1 86  ? 30.348 3.318   14.067  1.00 15.78 ?  86  HIS   A H    1 
ATOM   1838 H  HA   . HIS   A 1 86  ? 30.123 5.206   14.998  1.00 16.15 ?  86  HIS   A HA   1 
ATOM   1839 H  HB2  . HIS   A 1 86  ? 28.105 5.534   13.066  1.00 16.39 ?  86  HIS   A HB2  1 
ATOM   1840 H  HB3  . HIS   A 1 86  ? 28.776 6.733   13.867  1.00 16.39 ?  86  HIS   A HB3  1 
ATOM   1841 H  HD2  . HIS   A 1 86  ? 29.628 4.578   10.978  1.00 16.01 ?  86  HIS   A HD2  1 
ATOM   1842 H  HE1  . HIS   A 1 86  ? 32.671 7.064   11.419  1.00 17.15 ?  86  HIS   A HE1  1 
ATOM   1843 H  HE2  . HIS   A 1 86  ? 31.714 5.396   10.048  1.00 16.58 ?  86  HIS   A HE2  1 
ATOM   1844 N  N    . ASN   A 1 87  ? 27.268 5.600   15.825  1.00 15.49 ?  87  ASN   A N    1 
ATOM   1845 C  CA   . ASN   A 1 87  ? 26.281 5.592   16.888  1.00 16.22 ?  87  ASN   A CA   1 
ATOM   1846 C  C    . ASN   A 1 87  ? 25.149 4.603   16.647  1.00 17.19 ?  87  ASN   A C    1 
ATOM   1847 O  O    . ASN   A 1 87  ? 24.212 4.555   17.447  1.00 20.01 ?  87  ASN   A O    1 
ATOM   1848 C  CB   . ASN   A 1 87  ? 25.693 7.001   17.043  1.00 16.83 ?  87  ASN   A CB   1 
ATOM   1849 C  CG   . ASN   A 1 87  ? 25.178 7.568   15.725  1.00 17.83 ?  87  ASN   A CG   1 
ATOM   1850 O  OD1  . ASN   A 1 87  ? 25.821 7.446   14.686  1.00 18.24 ?  87  ASN   A OD1  1 
ATOM   1851 N  ND2  . ASN   A 1 87  ? 24.014 8.193   15.766  1.00 19.13 ?  87  ASN   A ND2  1 
ATOM   1852 H  H    . ASN   A 1 87  ? 27.116 6.205   15.234  1.00 18.61 ?  87  ASN   A H    1 
ATOM   1853 H  HA   . ASN   A 1 87  ? 26.707 5.349   17.729  1.00 19.48 ?  87  ASN   A HA   1 
ATOM   1854 H  HB2  . ASN   A 1 87  ? 24.950 6.969   17.671  1.00 20.21 ?  87  ASN   A HB2  1 
ATOM   1855 H  HB3  . ASN   A 1 87  ? 26.382 7.594   17.381  1.00 20.21 ?  87  ASN   A HB3  1 
ATOM   1856 H  HD21 . ASN   A 1 87  ? 23.685 8.525   15.047  1.00 22.97 ?  87  ASN   A HD21 1 
ATOM   1857 H  HD22 . ASN   A 1 87  ? 23.593 8.271   16.511  1.00 22.97 ?  87  ASN   A HD22 1 
ATOM   1858 N  N    A LEU   A 1 88  ? 25.213 3.820   15.572  0.56 16.05 ?  88  LEU   A N    1 
ATOM   1859 N  N    B LEU   A 1 88  ? 25.220 3.802   15.587  0.44 16.40 ?  88  LEU   A N    1 
ATOM   1860 C  CA   A LEU   A 1 88  ? 24.116 2.946   15.172  0.56 15.57 ?  88  LEU   A CA   1 
ATOM   1861 C  CA   B LEU   A 1 88  ? 24.109 2.948   15.191  0.44 16.04 ?  88  LEU   A CA   1 
ATOM   1862 C  C    A LEU   A 1 88  ? 24.344 1.479   15.509  0.56 15.29 ?  88  LEU   A C    1 
ATOM   1863 C  C    B LEU   A 1 88  ? 24.343 1.464   15.432  0.44 15.46 ?  88  LEU   A C    1 
ATOM   1864 O  O    A LEU   A 1 88  ? 23.374 0.755   15.758  0.56 16.46 ?  88  LEU   A O    1 
ATOM   1865 O  O    B LEU   A 1 88  ? 23.368 0.711   15.520  0.44 16.05 ?  88  LEU   A O    1 
ATOM   1866 C  CB   A LEU   A 1 88  ? 23.886 3.066   13.663  0.56 15.99 ?  88  LEU   A CB   1 
ATOM   1867 C  CB   B LEU   A 1 88  ? 23.806 3.148   13.701  0.44 16.65 ?  88  LEU   A CB   1 
ATOM   1868 C  CG   A LEU   A 1 88  ? 23.624 4.474   13.129  0.56 17.27 ?  88  LEU   A CG   1 
ATOM   1869 C  CG   B LEU   A 1 88  ? 23.505 4.590   13.282  0.44 17.46 ?  88  LEU   A CG   1 
ATOM   1870 C  CD1  A LEU   A 1 88  ? 23.503 4.442   11.617  0.56 17.70 ?  88  LEU   A CD1  1 
ATOM   1871 C  CD1  B LEU   A 1 88  ? 23.329 4.695   11.772  0.44 17.70 ?  88  LEU   A CD1  1 
ATOM   1872 C  CD2  A LEU   A 1 88  ? 22.370 5.067   13.764  0.56 18.96 ?  88  LEU   A CD2  1 
ATOM   1873 C  CD2  B LEU   A 1 88  ? 22.273 5.119   14.009  0.44 18.00 ?  88  LEU   A CD2  1 
ATOM   1874 H  H    A LEU   A 1 88  ? 25.897 3.781   15.055  0.56 19.29 ?  88  LEU   A H    1 
ATOM   1875 H  H    B LEU   A 1 88  ? 25.912 3.733   15.088  0.44 19.71 ?  88  LEU   A H    1 
ATOM   1876 H  HA   A LEU   A 1 88  ? 23.308 3.228   15.623  0.56 18.70 ?  88  LEU   A HA   1 
ATOM   1877 H  HA   B LEU   A 1 88  ? 23.320 3.209   15.692  0.44 19.27 ?  88  LEU   A HA   1 
ATOM   1878 H  HB2  A LEU   A 1 88  ? 24.666 2.729   13.201  0.56 19.21 ?  88  LEU   A HB2  1 
ATOM   1879 H  HB2  B LEU   A 1 88  ? 24.573 2.847   13.193  0.44 20.01 ?  88  LEU   A HB2  1 
ATOM   1880 H  HB3  A LEU   A 1 88  ? 23.112 2.527   13.429  0.56 19.21 ?  88  LEU   A HB3  1 
ATOM   1881 H  HB3  B LEU   A 1 88  ? 23.033 2.609   13.475  0.44 20.01 ?  88  LEU   A HB3  1 
ATOM   1882 H  HG   A LEU   A 1 88  ? 24.372 5.046   13.355  0.56 20.74 ?  88  LEU   A HG   1 
ATOM   1883 H  HG   B LEU   A 1 88  ? 24.257 5.148   13.528  0.44 20.97 ?  88  LEU   A HG   1 
ATOM   1884 H  HD11 A LEU   A 1 88  ? 23.340 5.342   11.292  0.56 21.27 ?  88  LEU   A HD11 1 
ATOM   1885 H  HD11 B LEU   A 1 88  ? 23.147 5.619   11.538  0.44 21.26 ?  88  LEU   A HD11 1 
ATOM   1886 H  HD12 A LEU   A 1 88  ? 24.327 4.098   11.242  0.56 21.27 ?  88  LEU   A HD12 1 
ATOM   1887 H  HD12 B LEU   A 1 88  ? 24.144 4.399   11.336  0.44 21.26 ?  88  LEU   A HD12 1 
ATOM   1888 H  HD13 A LEU   A 1 88  ? 22.761 3.865   11.372  0.56 21.27 ?  88  LEU   A HD13 1 
ATOM   1889 H  HD13 B LEU   A 1 88  ? 22.587 4.133   11.498  0.44 21.26 ?  88  LEU   A HD13 1 
ATOM   1890 H  HD21 A LEU   A 1 88  ? 22.173 5.917   13.340  0.56 22.78 ?  88  LEU   A HD21 1 
ATOM   1891 H  HD21 B LEU   A 1 88  ? 22.038 5.983   13.638  0.44 21.62 ?  88  LEU   A HD21 1 
ATOM   1892 H  HD22 A LEU   A 1 88  ? 21.631 4.453   13.635  0.56 22.78 ?  88  LEU   A HD22 1 
ATOM   1893 H  HD22 B LEU   A 1 88  ? 21.543 4.494   13.885  0.44 21.62 ?  88  LEU   A HD22 1 
ATOM   1894 H  HD23 A LEU   A 1 88  ? 22.531 5.199   14.712  0.56 22.78 ?  88  LEU   A HD23 1 
ATOM   1895 H  HD23 B LEU   A 1 88  ? 22.479 5.207   14.952  0.44 21.62 ?  88  LEU   A HD23 1 
ATOM   1896 N  N    . ALA   A 1 89  ? 25.594 1.028   15.521  1.00 14.83 ?  89  ALA   A N    1 
ATOM   1897 C  CA   . ALA   A 1 89  ? 25.932 -0.380  15.651  1.00 14.82 ?  89  ALA   A CA   1 
ATOM   1898 C  C    . ALA   A 1 89  ? 27.414 -0.434  15.968  1.00 15.25 ?  89  ALA   A C    1 
ATOM   1899 O  O    . ALA   A 1 89  ? 28.121 0.565   15.848  1.00 15.69 ?  89  ALA   A O    1 
ATOM   1900 C  CB   . ALA   A 1 89  ? 25.683 -1.104  14.330  1.00 14.38 ?  89  ALA   A CB   1 
ATOM   1901 H  H    A ALA   A 1 89  ? 26.282 1.539   15.460  0.56 17.82 ?  89  ALA   A H    1 
ATOM   1902 H  H    B ALA   A 1 89  ? 26.280 1.544   15.485  0.44 17.82 ?  89  ALA   A H    1 
ATOM   1903 H  HA   . ALA   A 1 89  ? 25.416 -0.795  16.362  1.00 17.81 ?  89  ALA   A HA   1 
ATOM   1904 H  HB1  . ALA   A 1 89  ? 25.932 -2.036  14.427  1.00 17.28 ?  89  ALA   A HB1  1 
ATOM   1905 H  HB2  . ALA   A 1 89  ? 24.743 -1.035  14.097  1.00 17.28 ?  89  ALA   A HB2  1 
ATOM   1906 H  HB3  . ALA   A 1 89  ? 26.224 -0.690  13.637  1.00 17.28 ?  89  ALA   A HB3  1 
ATOM   1907 N  N    A LYS   A 1 90  ? 27.890 -1.611  16.365  0.56 15.43 ?  90  LYS   A N    1 
ATOM   1908 N  N    B LYS   A 1 90  ? 27.892 -1.612  16.360  0.44 15.84 ?  90  LYS   A N    1 
ATOM   1909 C  CA   A LYS   A 1 90  ? 29.332 -1.765  16.520  0.56 15.94 ?  90  LYS   A CA   1 
ATOM   1910 C  CA   B LYS   A 1 90  ? 29.334 -1.766  16.520  0.44 16.66 ?  90  LYS   A CA   1 
ATOM   1911 C  C    A LYS   A 1 90  ? 30.038 -1.591  15.179  0.56 15.10 ?  90  LYS   A C    1 
ATOM   1912 C  C    B LYS   A 1 90  ? 30.043 -1.598  15.181  0.44 15.41 ?  90  LYS   A C    1 
ATOM   1913 O  O    A LYS   A 1 90  ? 30.975 -0.788  15.051  0.56 16.29 ?  90  LYS   A O    1 
ATOM   1914 O  O    B LYS   A 1 90  ? 30.993 -0.810  15.057  0.44 16.38 ?  90  LYS   A O    1 
ATOM   1915 C  CB   A LYS   A 1 90  ? 29.666 -3.119  17.149  0.56 18.39 ?  90  LYS   A CB   1 
ATOM   1916 C  CB   B LYS   A 1 90  ? 29.665 -3.120  17.148  0.44 19.44 ?  90  LYS   A CB   1 
ATOM   1917 C  CG   A LYS   A 1 90  ? 31.149 -3.291  17.454  0.56 22.41 ?  90  LYS   A CG   1 
ATOM   1918 C  CG   B LYS   A 1 90  ? 31.141 -3.286  17.481  0.44 23.07 ?  90  LYS   A CG   1 
ATOM   1919 C  CD   A LYS   A 1 90  ? 31.402 -4.523  18.307  0.56 26.13 ?  90  LYS   A CD   1 
ATOM   1920 C  CD   B LYS   A 1 90  ? 31.383 -4.517  18.338  0.44 26.38 ?  90  LYS   A CD   1 
ATOM   1921 C  CE   A LYS   A 1 90  ? 32.818 -4.546  18.865  0.56 28.92 ?  90  LYS   A CE   1 
ATOM   1922 C  CE   B LYS   A 1 90  ? 32.789 -4.527  18.921  0.44 28.85 ?  90  LYS   A CE   1 
ATOM   1923 N  NZ   A LYS   A 1 90  ? 33.837 -4.907  17.843  0.56 30.98 ?  90  LYS   A NZ   1 
ATOM   1924 N  NZ   B LYS   A 1 90  ? 33.832 -4.784  17.891  0.44 30.58 ?  90  LYS   A NZ   1 
ATOM   1925 H  H    A LYS   A 1 90  ? 27.417 -2.306  16.546  0.56 18.53 ?  90  LYS   A H    1 
ATOM   1926 H  H    B LYS   A 1 90  ? 27.419 -2.307  16.538  0.44 19.03 ?  90  LYS   A H    1 
ATOM   1927 H  HA   A LYS   A 1 90  ? 29.656 -1.075  17.115  0.56 19.15 ?  90  LYS   A HA   1 
ATOM   1928 H  HA   B LYS   A 1 90  ? 29.657 -1.074  17.114  0.44 20.02 ?  90  LYS   A HA   1 
ATOM   1929 H  HB2  A LYS   A 1 90  ? 29.178 -3.206  17.987  0.56 22.09 ?  90  LYS   A HB2  1 
ATOM   1930 H  HB2  B LYS   A 1 90  ? 29.160 -3.214  17.972  0.44 23.36 ?  90  LYS   A HB2  1 
ATOM   1931 H  HB3  A LYS   A 1 90  ? 29.400 -3.826  16.542  0.56 22.09 ?  90  LYS   A HB3  1 
ATOM   1932 H  HB3  B LYS   A 1 90  ? 29.417 -3.823  16.529  0.44 23.36 ?  90  LYS   A HB3  1 
ATOM   1933 H  HG2  A LYS   A 1 90  ? 31.637 -3.392  16.622  0.56 26.92 ?  90  LYS   A HG2  1 
ATOM   1934 H  HG2  B LYS   A 1 90  ? 31.647 -3.385  16.659  0.44 27.70 ?  90  LYS   A HG2  1 
ATOM   1935 H  HG3  A LYS   A 1 90  ? 31.469 -2.514  17.939  0.56 26.92 ?  90  LYS   A HG3  1 
ATOM   1936 H  HG3  B LYS   A 1 90  ? 31.449 -2.508  17.973  0.44 27.70 ?  90  LYS   A HG3  1 
ATOM   1937 H  HD2  A LYS   A 1 90  ? 30.781 -4.528  19.053  0.56 31.38 ?  90  LYS   A HD2  1 
ATOM   1938 H  HD2  B LYS   A 1 90  ? 30.749 -4.526  19.073  0.44 31.68 ?  90  LYS   A HD2  1 
ATOM   1939 H  HD3  A LYS   A 1 90  ? 31.277 -5.318  17.764  0.56 31.38 ?  90  LYS   A HD3  1 
ATOM   1940 H  HD3  B LYS   A 1 90  ? 31.274 -5.313  17.793  0.44 31.68 ?  90  LYS   A HD3  1 
ATOM   1941 H  HE2  A LYS   A 1 90  ? 33.038 -3.665  19.208  0.56 34.73 ?  90  LYS   A HE2  1 
ATOM   1942 H  HE2  B LYS   A 1 90  ? 32.971 -3.662  19.323  0.44 34.64 ?  90  LYS   A HE2  1 
ATOM   1943 H  HE3  A LYS   A 1 90  ? 32.866 -5.200  19.580  0.56 34.73 ?  90  LYS   A HE3  1 
ATOM   1944 H  HE3  B LYS   A 1 90  ? 32.849 -5.224  19.592  0.44 34.64 ?  90  LYS   A HE3  1 
ATOM   1945 H  HZ1  A LYS   A 1 90  ? 34.644 -4.947  18.218  0.56 37.19 ?  90  LYS   A HZ1  1 
ATOM   1946 H  HZ1  B LYS   A 1 90  ? 34.639 -4.786  18.269  0.44 36.72 ?  90  LYS   A HZ1  1 
ATOM   1947 H  HZ2  A LYS   A 1 90  ? 33.645 -5.701  17.489  0.56 37.19 ?  90  LYS   A HZ2  1 
ATOM   1948 H  HZ2  B LYS   A 1 90  ? 33.692 -5.576  17.508  0.44 36.72 ?  90  LYS   A HZ2  1 
ATOM   1949 H  HZ3  A LYS   A 1 90  ? 33.849 -4.297  17.196  0.56 37.19 ?  90  LYS   A HZ3  1 
ATOM   1950 H  HZ3  B LYS   A 1 90  ? 33.807 -4.152  17.266  0.44 36.72 ?  90  LYS   A HZ3  1 
ATOM   1951 N  N    . HIS   A 1 91  ? 29.576 -2.318  14.161  1.00 13.38 ?  91  HIS   A N    1 
ATOM   1952 C  CA   . HIS   A 1 91  ? 30.164 -2.304  12.835  1.00 12.72 ?  91  HIS   A CA   1 
ATOM   1953 C  C    . HIS   A 1 91  ? 29.086 -2.041  11.802  1.00 11.69 ?  91  HIS   A C    1 
ATOM   1954 O  O    . HIS   A 1 91  ? 27.915 -2.397  11.991  1.00 12.65 ?  91  HIS   A O    1 
ATOM   1955 C  CB   . HIS   A 1 91  ? 30.764 -3.672  12.476  1.00 15.50 ?  91  HIS   A CB   1 
ATOM   1956 C  CG   . HIS   A 1 91  ? 31.756 -4.181  13.470  1.00 19.39 ?  91  HIS   A CG   1 
ATOM   1957 N  ND1  . HIS   A 1 91  ? 33.025 -3.660  13.586  1.00 21.37 ?  91  HIS   A ND1  1 
ATOM   1958 C  CD2  . HIS   A 1 91  ? 31.670 -5.173  14.387  1.00 21.63 ?  91  HIS   A CD2  1 
ATOM   1959 C  CE1  . HIS   A 1 91  ? 33.680 -4.306  14.536  1.00 22.60 ?  91  HIS   A CE1  1 
ATOM   1960 N  NE2  . HIS   A 1 91  ? 32.879 -5.231  15.038  1.00 23.06 ?  91  HIS   A NE2  1 
ATOM   1961 H  H    A HIS   A 1 91  ? 28.891 -2.846  14.223  0.56 16.07 ?  91  HIS   A H    1 
ATOM   1962 H  H    B HIS   A 1 91  ? 28.892 -2.847  14.223  0.44 16.07 ?  91  HIS   A H    1 
ATOM   1963 H  HA   . HIS   A 1 91  ? 30.848 -1.628  12.767  1.00 15.29 ?  91  HIS   A HA   1 
ATOM   1964 H  HB2  . HIS   A 1 91  ? 30.048 -4.325  12.415  1.00 18.62 ?  91  HIS   A HB2  1 
ATOM   1965 H  HB3  . HIS   A 1 91  ? 31.214 -3.601  11.618  1.00 18.62 ?  91  HIS   A HB3  1 
ATOM   1966 H  HD1  . HIS   A 1 91  ? 33.345 -3.013  13.112  1.00 25.67 ?  91  HIS   A HD1  1 
ATOM   1967 H  HD2  . HIS   A 1 91  ? 30.935 -5.714  14.548  1.00 25.97 ?  91  HIS   A HD2  1 
ATOM   1968 H  HE1  . HIS   A 1 91  ? 34.557 -4.136  14.803  1.00 27.15 ?  91  HIS   A HE1  1 
ATOM   1969 N  N    . CYS   A 1 92  ? 29.497 -1.445  10.689  1.00 11.43 ?  92  CYS   A N    1 
ATOM   1970 C  CA   . CYS   A 1 92  ? 28.666 -1.368  9.495   1.00 11.53 ?  92  CYS   A CA   1 
ATOM   1971 C  C    . CYS   A 1 92  ? 29.320 -2.190  8.396   1.00 11.06 ?  92  CYS   A C    1 
ATOM   1972 O  O    . CYS   A 1 92  ? 30.478 -1.940  8.034   1.00 11.92 ?  92  CYS   A O    1 
ATOM   1973 C  CB   . CYS   A 1 92  ? 28.457 0.071   9.026   1.00 11.92 ?  92  CYS   A CB   1 
ATOM   1974 S  SG   . CYS   A 1 92  ? 27.454 0.172   7.503   1.00 11.44 ?  92  CYS   A SG   1 
ATOM   1975 H  H    . CYS   A 1 92  ? 30.264 -1.067  10.600  1.00 13.74 ?  92  CYS   A H    1 
ATOM   1976 H  HA   . CYS   A 1 92  ? 27.798 -1.750  9.681   1.00 13.85 ?  92  CYS   A HA   1 
ATOM   1977 H  HB2  . CYS   A 1 92  ? 27.997 0.572   9.719   1.00 14.32 ?  92  CYS   A HB2  1 
ATOM   1978 H  HB3  . CYS   A 1 92  ? 29.318 0.479   8.839   1.00 14.32 ?  92  CYS   A HB3  1 
ATOM   1979 H  HG   . CYS   A 1 92  ? 27.317 1.323   7.207   1.00 13.76 ?  92  CYS   A HG   1 
ATOM   1980 N  N    . LEU   A 1 93  ? 28.588 -3.176  7.888   1.00 10.95 ?  93  LEU   A N    1 
ATOM   1981 C  CA   . LEU   A 1 93  ? 29.007 -3.931  6.714   1.00 10.84 ?  93  LEU   A CA   1 
ATOM   1982 C  C    . LEU   A 1 93  ? 28.415 -3.249  5.482   1.00 10.05 ?  93  LEU   A C    1 
ATOM   1983 O  O    . LEU   A 1 93  ? 27.200 -3.313  5.252   1.00 10.21 ?  93  LEU   A O    1 
ATOM   1984 C  CB   . LEU   A 1 93  ? 28.527 -5.378  6.823   1.00 11.34 ?  93  LEU   A CB   1 
ATOM   1985 C  CG   . LEU   A 1 93  ? 28.912 -6.273  5.647   1.00 11.42 ?  93  LEU   A CG   1 
ATOM   1986 C  CD1  . LEU   A 1 93  ? 30.418 -6.534  5.632   1.00 12.20 ?  93  LEU   A CD1  1 
ATOM   1987 C  CD2  . LEU   A 1 93  ? 28.131 -7.586  5.708   1.00 12.49 ?  93  LEU   A CD2  1 
ATOM   1988 H  H    . LEU   A 1 93  ? 27.833 -3.427  8.218   1.00 13.16 ?  93  LEU   A H    1 
ATOM   1989 H  HA   . LEU   A 1 93  ? 29.968 -3.920  6.648   1.00 13.03 ?  93  LEU   A HA   1 
ATOM   1990 H  HB2  . LEU   A 1 93  ? 28.911 -5.767  7.628   1.00 13.63 ?  93  LEU   A HB2  1 
ATOM   1991 H  HB3  . LEU   A 1 93  ? 27.561 -5.383  6.892   1.00 13.63 ?  93  LEU   A HB3  1 
ATOM   1992 H  HG   . LEU   A 1 93  ? 28.682 -5.829  4.823   1.00 13.72 ?  93  LEU   A HG   1 
ATOM   1993 H  HD11 . LEU   A 1 93  ? 30.627 -7.141  4.908   1.00 14.66 ?  93  LEU   A HD11 1 
ATOM   1994 H  HD12 . LEU   A 1 93  ? 30.884 -5.691  5.505   1.00 14.66 ?  93  LEU   A HD12 1 
ATOM   1995 H  HD13 . LEU   A 1 93  ? 30.682 -6.928  6.481   1.00 14.66 ?  93  LEU   A HD13 1 
ATOM   1996 H  HD21 . LEU   A 1 93  ? 28.396 -8.141  4.958   1.00 15.01 ?  93  LEU   A HD21 1 
ATOM   1997 H  HD22 . LEU   A 1 93  ? 28.338 -8.037  6.543   1.00 15.01 ?  93  LEU   A HD22 1 
ATOM   1998 H  HD23 . LEU   A 1 93  ? 27.185 -7.389  5.661   1.00 15.01 ?  93  LEU   A HD23 1 
ATOM   1999 N  N    . HIS   A 1 94  ? 29.263 -2.559  4.719   1.00 10.18 ?  94  HIS   A N    1 
ATOM   2000 C  CA   . HIS   A 1 94  ? 28.845 -1.890  3.489   1.00 10.20 ?  94  HIS   A CA   1 
ATOM   2001 C  C    . HIS   A 1 94  ? 28.866 -2.925  2.377   1.00 10.07 ?  94  HIS   A C    1 
ATOM   2002 O  O    . HIS   A 1 94  ? 29.933 -3.445  2.038   1.00 11.63 ?  94  HIS   A O    1 
ATOM   2003 C  CB   . HIS   A 1 94  ? 29.801 -0.738  3.161   1.00 10.16 ?  94  HIS   A CB   1 
ATOM   2004 C  CG   . HIS   A 1 94  ? 29.786 0.354   4.176   1.00 10.35 ?  94  HIS   A CG   1 
ATOM   2005 N  ND1  . HIS   A 1 94  ? 28.914 1.423   4.115   1.00 10.31 ?  94  HIS   A ND1  1 
ATOM   2006 C  CD2  . HIS   A 1 94  ? 30.520 0.520   5.297   1.00 10.93 ?  94  HIS   A CD2  1 
ATOM   2007 C  CE1  . HIS   A 1 94  ? 29.125 2.200   5.161   1.00 10.44 ?  94  HIS   A CE1  1 
ATOM   2008 N  NE2  . HIS   A 1 94  ? 30.094 1.676   5.891   1.00 10.81 ?  94  HIS   A NE2  1 
ATOM   2009 H  H    . HIS   A 1 94  ? 30.099 -2.456  4.897   1.00 12.24 ?  94  HIS   A H    1 
ATOM   2010 H  HA   . HIS   A 1 94  ? 27.942 -1.541  3.586   1.00 12.27 ?  94  HIS   A HA   1 
ATOM   2011 H  HB2  . HIS   A 1 94  ? 30.698 -1.080  3.105   1.00 12.21 ?  94  HIS   A HB2  1 
ATOM   2012 H  HB3  . HIS   A 1 94  ? 29.535 -0.348  2.309   1.00 12.21 ?  94  HIS   A HB3  1 
ATOM   2013 H  HD2  . HIS   A 1 94  ? 31.193 -0.036  5.606   1.00 13.13 ?  94  HIS   A HD2  1 
ATOM   2014 H  HE1  . HIS   A 1 94  ? 28.666 2.990   5.347   1.00 12.55 ?  94  HIS   A HE1  1 
ATOM   2015 H  HE2  . HIS   A 1 94  ? 30.409 2.021   6.615   1.00 13.00 ?  94  HIS   A HE2  1 
ATOM   2016 N  N    . VAL   A 1 95  ? 27.693 -3.252  1.834   1.00 9.74  ?  95  VAL   A N    1 
ATOM   2017 C  CA   . VAL   A 1 95  ? 27.556 -4.289  0.817   1.00 9.92  ?  95  VAL   A CA   1 
ATOM   2018 C  C    . VAL   A 1 95  ? 27.022 -3.659  -0.459  1.00 9.78  ?  95  VAL   A C    1 
ATOM   2019 O  O    . VAL   A 1 95  ? 26.014 -2.939  -0.419  1.00 10.53 ?  95  VAL   A O    1 
ATOM   2020 C  CB   . VAL   A 1 95  ? 26.621 -5.422  1.271   1.00 10.51 ?  95  VAL   A CB   1 
ATOM   2021 C  CG1  . VAL   A 1 95  ? 26.520 -6.468  0.167   1.00 11.55 ?  95  VAL   A CG1  1 
ATOM   2022 C  CG2  . VAL   A 1 95  ? 27.109 -6.033  2.569   1.00 10.84 ?  95  VAL   A CG2  1 
ATOM   2023 H  H    . VAL   A 1 95  ? 26.943 -2.888  2.055   1.00 11.71 ?  95  VAL   A H    1 
ATOM   2024 H  HA   . VAL   A 1 95  ? 28.424 -4.672  0.628   1.00 11.93 ?  95  VAL   A HA   1 
ATOM   2025 H  HB   . VAL   A 1 95  ? 25.735 -5.066  1.425   1.00 12.63 ?  95  VAL   A HB   1 
ATOM   2026 H  HG11 . VAL   A 1 95  ? 26.141 -7.284  0.532   1.00 13.89 ?  95  VAL   A HG11 1 
ATOM   2027 H  HG12 . VAL   A 1 95  ? 25.948 -6.132  -0.543  1.00 13.89 ?  95  VAL   A HG12 1 
ATOM   2028 H  HG13 . VAL   A 1 95  ? 27.408 -6.650  -0.184  1.00 13.89 ?  95  VAL   A HG13 1 
ATOM   2029 H  HG21 . VAL   A 1 95  ? 26.547 -6.796  2.791   1.00 13.03 ?  95  VAL   A HG21 1 
ATOM   2030 H  HG22 . VAL   A 1 95  ? 28.027 -6.322  2.460   1.00 13.03 ?  95  VAL   A HG22 1 
ATOM   2031 H  HG23 . VAL   A 1 95  ? 27.050 -5.368  3.271   1.00 13.03 ?  95  VAL   A HG23 1 
ATOM   2032 N  N    . VAL   A 1 96  ? 27.663 -3.954  -1.592  1.00 9.63  ?  96  VAL   A N    1 
ATOM   2033 C  CA   . VAL   A 1 96  ? 27.261 -3.404  -2.880  1.00 10.22 ?  96  VAL   A CA   1 
ATOM   2034 C  C    . VAL   A 1 96  ? 26.472 -4.462  -3.642  1.00 10.87 ?  96  VAL   A C    1 
ATOM   2035 O  O    . VAL   A 1 96  ? 27.041 -5.405  -4.201  1.00 11.83 ?  96  VAL   A O    1 
ATOM   2036 C  CB   . VAL   A 1 96  ? 28.458 -2.919  -3.698  1.00 10.90 ?  96  VAL   A CB   1 
ATOM   2037 C  CG1  . VAL   A 1 96  ? 27.966 -2.288  -4.975  1.00 11.11 ?  96  VAL   A CG1  1 
ATOM   2038 C  CG2  . VAL   A 1 96  ? 29.304 -1.942  -2.901  1.00 11.48 ?  96  VAL   A CG2  1 
ATOM   2039 H  H    . VAL   A 1 96  ? 28.355 -4.473  -1.629  1.00 11.58 ?  96  VAL   A H    1 
ATOM   2040 H  HA   . VAL   A 1 96  ? 26.681 -2.646  -2.726  1.00 12.29 ?  96  VAL   A HA   1 
ATOM   2041 H  HB   . VAL   A 1 96  ? 29.015 -3.673  -3.929  1.00 13.10 ?  96  VAL   A HB   1 
ATOM   2042 H  HG11 . VAL   A 1 96  ? 28.701 -1.809  -5.391  1.00 13.36 ?  96  VAL   A HG11 1 
ATOM   2043 H  HG12 . VAL   A 1 96  ? 27.646 -2.982  -5.569  1.00 13.36 ?  96  VAL   A HG12 1 
ATOM   2044 H  HG13 . VAL   A 1 96  ? 27.248 -1.668  -4.766  1.00 13.36 ?  96  VAL   A HG13 1 
ATOM   2045 H  HG21 . VAL   A 1 96  ? 30.012 -1.596  -3.468  1.00 13.80 ?  96  VAL   A HG21 1 
ATOM   2046 H  HG22 . VAL   A 1 96  ? 28.741 -1.207  -2.596  1.00 13.80 ?  96  VAL   A HG22 1 
ATOM   2047 H  HG23 . VAL   A 1 96  ? 29.687 -2.398  -2.136  1.00 13.80 ?  96  VAL   A HG23 1 
ATOM   2048 N  N    . GLY   A 1 97  ? 25.154 -4.304  -3.681  1.00 10.78 ?  97  GLY   A N    1 
ATOM   2049 C  CA   . GLY   A 1 97  ? 24.344 -5.064  -4.597  1.00 11.49 ?  97  GLY   A CA   1 
ATOM   2050 C  C    . GLY   A 1 97  ? 24.370 -4.422  -5.971  1.00 11.59 ?  97  GLY   A C    1 
ATOM   2051 O  O    . GLY   A 1 97  ? 24.656 -3.227  -6.115  1.00 12.61 ?  97  GLY   A O    1 
ATOM   2052 H  H    . GLY   A 1 97  ? 24.711 -3.762  -3.176  1.00 12.96 ?  97  GLY   A H    1 
ATOM   2053 H  HA2  . GLY   A 1 97  ? 24.695 -5.966  -4.642  1.00 13.80 ?  97  GLY   A HA2  1 
ATOM   2054 H  HA3  . GLY   A 1 97  ? 23.429 -5.100  -4.274  1.00 13.80 ?  97  GLY   A HA3  1 
ATOM   2055 N  N    A PRO   A 1 98  ? 23.991 -5.148  -7.015  0.56 11.55 ?  98  PRO   A N    1 
ATOM   2056 N  N    B PRO   A 1 98  ? 24.141 -5.245  -6.996  0.44 12.10 ?  98  PRO   A N    1 
ATOM   2057 C  CA   A PRO   A 1 98  ? 23.876 -4.499  -8.328  0.56 12.47 ?  98  PRO   A CA   1 
ATOM   2058 C  CA   B PRO   A 1 98  ? 24.134 -4.748  -8.372  0.44 12.73 ?  98  PRO   A CA   1 
ATOM   2059 C  C    A PRO   A 1 98  ? 22.769 -3.449  -8.349  0.56 12.38 ?  98  PRO   A C    1 
ATOM   2060 C  C    B PRO   A 1 98  ? 23.007 -3.756  -8.590  0.44 12.57 ?  98  PRO   A C    1 
ATOM   2061 O  O    A PRO   A 1 98  ? 21.689 -3.648  -7.786  0.56 11.90 ?  98  PRO   A O    1 
ATOM   2062 O  O    B PRO   A 1 98  ? 21.910 -3.891  -8.041  0.44 13.45 ?  98  PRO   A O    1 
ATOM   2063 C  CB   A PRO   A 1 98  ? 23.564 -5.662  -9.276  0.56 12.21 ?  98  PRO   A CB   1 
ATOM   2064 C  CB   B PRO   A 1 98  ? 23.925 -6.019  -9.206  0.44 12.96 ?  98  PRO   A CB   1 
ATOM   2065 C  CG   A PRO   A 1 98  ? 22.949 -6.710  -8.401  0.56 12.09 ?  98  PRO   A CG   1 
ATOM   2066 C  CG   B PRO   A 1 98  ? 23.293 -7.005  -8.257  0.44 13.36 ?  98  PRO   A CG   1 
ATOM   2067 C  CD   A PRO   A 1 98  ? 23.657 -6.581  -7.071  0.56 11.84 ?  98  PRO   A CD   1 
ATOM   2068 C  CD   B PRO   A 1 98  ? 23.912 -6.700  -6.927  0.44 12.26 ?  98  PRO   A CD   1 
ATOM   2069 H  HA   A PRO   A 1 98  ? 24.719 -4.092  -8.572  0.56 14.99 ?  98  PRO   A HA   1 
ATOM   2070 H  HA   B PRO   A 1 98  ? 24.986 -4.343  -8.596  0.44 15.30 ?  98  PRO   A HA   1 
ATOM   2071 H  HB2  A PRO   A 1 98  ? 22.935 -5.368  -9.952  0.56 14.67 ?  98  PRO   A HB2  1 
ATOM   2072 H  HB2  B PRO   A 1 98  ? 23.333 -5.830  -9.949  0.44 15.57 ?  98  PRO   A HB2  1 
ATOM   2073 H  HB3  A PRO   A 1 98  ? 24.383 -5.983  -9.677  0.56 14.67 ?  98  PRO   A HB3  1 
ATOM   2074 H  HB3  B PRO   A 1 98  ? 24.781 -6.352  -9.523  0.44 15.57 ?  98  PRO   A HB3  1 
ATOM   2075 H  HG2  A PRO   A 1 98  ? 22.001 -6.540  -8.302  0.56 14.53 ?  98  PRO   A HG2  1 
ATOM   2076 H  HG2  B PRO   A 1 98  ? 22.332 -6.865  -8.228  0.44 16.05 ?  98  PRO   A HG2  1 
ATOM   2077 H  HG3  A PRO   A 1 98  ? 23.104 -7.586  -8.787  0.56 14.53 ?  98  PRO   A HG3  1 
ATOM   2078 H  HG3  B PRO   A 1 98  ? 23.499 -7.913  -8.533  0.44 16.05 ?  98  PRO   A HG3  1 
ATOM   2079 H  HD2  A PRO   A 1 98  ? 23.059 -6.829  -6.344  0.56 14.22 ?  98  PRO   A HD2  1 
ATOM   2080 H  HD2  B PRO   A 1 98  ? 23.295 -6.919  -6.207  0.44 14.73 ?  98  PRO   A HD2  1 
ATOM   2081 H  HD3  A PRO   A 1 98  ? 24.466 -7.117  -7.062  0.56 14.22 ?  98  PRO   A HD3  1 
ATOM   2082 H  HD3  B PRO   A 1 98  ? 24.754 -7.175  -6.823  0.44 14.73 ?  98  PRO   A HD3  1 
ATOM   2083 N  N    A ASN   A 1 99  ? 23.056 -2.318  -9.001  0.56 12.79 ?  99  ASN   A N    1 
ATOM   2084 N  N    B ASN   A 1 99  ? 23.288 -2.749  -9.401  0.44 12.73 ?  99  ASN   A N    1 
ATOM   2085 C  CA   A ASN   A 1 99  ? 22.079 -1.246  -9.211  0.56 13.12 ?  99  ASN   A CA   1 
ATOM   2086 C  CA   B ASN   A 1 99  ? 22.305 -1.740  -9.760  0.44 13.60 ?  99  ASN   A CA   1 
ATOM   2087 C  C    A ASN   A 1 99  ? 21.521 -1.387  -10.626 0.56 13.87 ?  99  ASN   A C    1 
ATOM   2088 C  C    B ASN   A 1 99  ? 21.829 -2.046  -11.177 0.44 14.01 ?  99  ASN   A C    1 
ATOM   2089 O  O    A ASN   A 1 99  ? 22.180 -1.030  -11.608 0.56 15.21 ?  99  ASN   A O    1 
ATOM   2090 O  O    B ASN   A 1 99  ? 22.563 -1.839  -12.150 0.44 13.83 ?  99  ASN   A O    1 
ATOM   2091 C  CB   A ASN   A 1 99  ? 22.715 0.125   -8.988  0.56 13.29 ?  99  ASN   A CB   1 
ATOM   2092 C  CB   B ASN   A 1 99  ? 22.903 -0.342  -9.653  0.44 14.66 ?  99  ASN   A CB   1 
ATOM   2093 C  CG   A ASN   A 1 99  ? 21.697 1.267   -9.029  0.56 13.65 ?  99  ASN   A CG   1 
ATOM   2094 C  CG   B ASN   A 1 99  ? 21.868 0.735   -9.846  0.44 15.79 ?  99  ASN   A CG   1 
ATOM   2095 O  OD1  A ASN   A 1 99  ? 20.741 1.242   -9.804  0.56 13.44 ?  99  ASN   A OD1  1 
ATOM   2096 O  OD1  B ASN   A 1 99  ? 21.057 0.646   -10.756 0.44 15.46 ?  99  ASN   A OD1  1 
ATOM   2097 N  ND2  A ASN   A 1 99  ? 21.917 2.284   -8.198  0.56 13.42 ?  99  ASN   A ND2  1 
ATOM   2098 N  ND2  B ASN   A 1 99  ? 21.866 1.740   -8.970  0.44 16.57 ?  99  ASN   A ND2  1 
ATOM   2099 H  H    A ASN   A 1 99  ? 23.833 -2.143  -9.322  0.56 15.37 ?  99  ASN   A H    1 
ATOM   2100 H  H    B ASN   A 1 99  ? 24.060 -2.625  -9.755  0.44 15.30 ?  99  ASN   A H    1 
ATOM   2101 H  HA   A ASN   A 1 99  ? 21.349 -1.354  -8.577  0.56 15.77 ?  99  ASN   A HA   1 
ATOM   2102 H  HA   B ASN   A 1 99  ? 21.546 -1.795  -9.157  0.44 16.35 ?  99  ASN   A HA   1 
ATOM   2103 H  HB2  A ASN   A 1 99  ? 23.151 0.134   -8.122  0.56 15.97 ?  99  ASN   A HB2  1 
ATOM   2104 H  HB2  B ASN   A 1 99  ? 23.297 -0.224  -8.775  0.44 17.61 ?  99  ASN   A HB2  1 
ATOM   2105 H  HB3  A ASN   A 1 99  ? 23.368 0.280   -9.689  0.56 15.97 ?  99  ASN   A HB3  1 
ATOM   2106 H  HB3  B ASN   A 1 99  ? 23.573 -0.240  -10.341 0.44 17.61 ?  99  ASN   A HB3  1 
ATOM   2107 H  HD21 A ASN   A 1 99  ? 21.375 2.948   -8.180  0.56 16.13 ?  99  ASN   A HD21 1 
ATOM   2108 H  HD21 B ASN   A 1 99  ? 21.285 2.374   -9.032  0.44 19.90 ?  99  ASN   A HD21 1 
ATOM   2109 H  HD22 A ASN   A 1 99  ? 22.602 2.271   -7.676  0.56 16.13 ?  99  ASN   A HD22 1 
ATOM   2110 H  HD22 B ASN   A 1 99  ? 22.447 1.755   -8.336  0.44 19.90 ?  99  ASN   A HD22 1 
ATOM   2111 N  N    A VAL   A 1 100 ? 20.295 -1.918  -10.715 0.56 15.35 ?  100 VAL   A N    1 
ATOM   2112 N  N    B VAL   A 1 100 ? 20.602 -2.560  -11.280 0.44 16.26 ?  100 VAL   A N    1 
ATOM   2113 C  CA   A VAL   A 1 100 ? 19.656 -2.173  -12.005 0.56 17.16 ?  100 VAL   A CA   1 
ATOM   2114 C  CA   B VAL   A 1 100 ? 20.060 -2.966  -12.573 0.44 18.96 ?  100 VAL   A CA   1 
ATOM   2115 C  C    A VAL   A 1 100 ? 19.535 -0.891  -12.816 0.56 17.81 ?  100 VAL   A C    1 
ATOM   2116 C  C    B VAL   A 1 100 ? 19.871 -1.767  -13.493 0.44 19.91 ?  100 VAL   A C    1 
ATOM   2117 O  O    A VAL   A 1 100 ? 19.625 -0.914  -14.050 0.56 19.33 ?  100 VAL   A O    1 
ATOM   2118 O  O    B VAL   A 1 100 ? 19.906 -1.909  -14.721 0.44 20.18 ?  100 VAL   A O    1 
ATOM   2119 C  CB   A VAL   A 1 100 ? 18.293 -2.873  -11.796 0.56 18.61 ?  100 VAL   A CB   1 
ATOM   2120 C  CB   B VAL   A 1 100 ? 18.757 -3.761  -12.364 0.44 21.22 ?  100 VAL   A CB   1 
ATOM   2121 C  CG1  A VAL   A 1 100 ? 17.556 -3.040  -13.113 0.56 19.53 ?  100 VAL   A CG1  1 
ATOM   2122 C  CG1  B VAL   A 1 100 ? 17.859 -3.689  -13.596 0.44 22.00 ?  100 VAL   A CG1  1 
ATOM   2123 C  CG2  A VAL   A 1 100 ? 18.498 -4.231  -11.128 0.56 18.81 ?  100 VAL   A CG2  1 
ATOM   2124 C  CG2  B VAL   A 1 100 ? 19.080 -5.202  -12.016 0.44 22.11 ?  100 VAL   A CG2  1 
ATOM   2125 H  H    A VAL   A 1 100 ? 19.809 -2.141  -10.033 0.56 18.45 ?  100 VAL   A H    1 
ATOM   2126 H  H    B VAL   A 1 100 ? 20.071 -2.689  -10.615 0.44 19.54 ?  100 VAL   A H    1 
ATOM   2127 H  HA   A VAL   A 1 100 ? 20.213 -2.785  -12.505 0.56 20.61 ?  100 VAL   A HA   1 
ATOM   2128 H  HA   B VAL   A 1 100 ? 20.698 -3.560  -12.994 0.44 22.78 ?  100 VAL   A HA   1 
ATOM   2129 H  HB   A VAL   A 1 100 ? 17.742 -2.334  -11.207 0.56 22.35 ?  100 VAL   A HB   1 
ATOM   2130 H  HB   B VAL   A 1 100 ? 18.270 -3.373  -11.621 0.44 25.49 ?  100 VAL   A HB   1 
ATOM   2131 H  HG11 A VAL   A 1 100 ? 16.815 -3.654  -12.985 0.56 23.46 ?  100 VAL   A HG11 1 
ATOM   2132 H  HG11 B VAL   A 1 100 ? 17.169 -4.367  -13.517 0.44 26.42 ?  100 VAL   A HG11 1 
ATOM   2133 H  HG12 A VAL   A 1 100 ? 17.222 -2.177  -13.401 0.56 23.46 ?  100 VAL   A HG12 1 
ATOM   2134 H  HG12 B VAL   A 1 100 ? 17.447 -2.810  -13.644 0.44 26.42 ?  100 VAL   A HG12 1 
ATOM   2135 H  HG13 A VAL   A 1 100 ? 18.170 -3.398  -13.774 0.56 23.46 ?  100 VAL   A HG13 1 
ATOM   2136 H  HG13 B VAL   A 1 100 ? 18.390 -3.852  -14.390 0.44 26.42 ?  100 VAL   A HG13 1 
ATOM   2137 H  HG21 A VAL   A 1 100 ? 17.638 -4.676  -11.042 0.56 22.59 ?  100 VAL   A HG21 1 
ATOM   2138 H  HG21 B VAL   A 1 100 ? 18.263 -5.651  -11.754 0.44 26.55 ?  100 VAL   A HG21 1 
ATOM   2139 H  HG22 A VAL   A 1 100 ? 19.092 -4.767  -11.676 0.56 22.59 ?  100 VAL   A HG22 1 
ATOM   2140 H  HG22 B VAL   A 1 100 ? 19.465 -5.635  -12.794 0.44 26.55 ?  100 VAL   A HG22 1 
ATOM   2141 H  HG23 A VAL   A 1 100 ? 18.888 -4.099  -10.249 0.56 22.59 ?  100 VAL   A HG23 1 
ATOM   2142 H  HG23 B VAL   A 1 100 ? 19.714 -5.211  -11.283 0.44 26.55 ?  100 VAL   A HG23 1 
ATOM   2143 N  N    A ASN   A 1 101 ? 19.320 0.241   -12.150 0.56 18.72 ?  101 ASN   A N    1 
ATOM   2144 N  N    B ASN   A 1 101 ? 19.659 -0.581  -12.934 0.44 21.12 ?  101 ASN   A N    1 
ATOM   2145 C  CA   A ASN   A 1 101 ? 19.239 1.518   -12.849 0.56 19.76 ?  101 ASN   A CA   1 
ATOM   2146 C  CA   B ASN   A 1 101 ? 19.563 0.630   -13.738 0.44 23.15 ?  101 ASN   A CA   1 
ATOM   2147 C  C    A ASN   A 1 101 ? 20.589 1.998   -13.373 0.56 21.44 ?  101 ASN   A C    1 
ATOM   2148 C  C    B ASN   A 1 101 ? 20.923 1.153   -14.187 0.44 24.00 ?  101 ASN   A C    1 
ATOM   2149 O  O    A ASN   A 1 101 ? 20.644 3.072   -13.985 0.56 22.89 ?  101 ASN   A O    1 
ATOM   2150 O  O    B ASN   A 1 101 ? 20.989 2.235   -14.782 0.44 24.82 ?  101 ASN   A O    1 
ATOM   2151 C  CB   A ASN   A 1 101 ? 18.593 2.559   -11.939 0.56 19.30 ?  101 ASN   A CB   1 
ATOM   2152 C  CB   B ASN   A 1 101 ? 18.750 1.691   -12.990 0.44 24.53 ?  101 ASN   A CB   1 
ATOM   2153 C  CG   A ASN   A 1 101 ? 17.226 2.116   -11.442 0.56 19.09 ?  101 ASN   A CG   1 
ATOM   2154 C  CG   B ASN   A 1 101 ? 17.345 1.214   -12.667 0.44 25.93 ?  101 ASN   A CG   1 
ATOM   2155 O  OD1  A ASN   A 1 101 ? 16.442 1.514   -12.188 0.56 19.55 ?  101 ASN   A OD1  1 
ATOM   2156 O  OD1  B ASN   A 1 101 ? 16.838 0.286   -13.296 0.44 26.20 ?  101 ASN   A OD1  1 
ATOM   2157 N  ND2  A ASN   A 1 101 ? 16.939 2.388   -10.173 0.56 19.49 ?  101 ASN   A ND2  1 
ATOM   2158 N  ND2  B ASN   A 1 101 ? 16.713 1.840   -11.688 0.44 26.64 ?  101 ASN   A ND2  1 
ATOM   2159 H  H    A ASN   A 1 101 ? 19.205 0.292   -11.300 0.56 22.49 ?  101 ASN   A H    1 
ATOM   2160 H  H    B ASN   A 1 101 ? 19.547 -0.457  -12.090 0.44 25.36 ?  101 ASN   A H    1 
ATOM   2161 H  HA   A ASN   A 1 101 ? 18.655 1.405   -13.613 0.56 23.73 ?  101 ASN   A HA   1 
ATOM   2162 H  HA   B ASN   A 1 101 ? 19.084 0.421   -14.547 0.44 27.80 ?  101 ASN   A HA   1 
ATOM   2163 H  HB2  A ASN   A 1 101 ? 19.165 2.709   -11.169 0.56 23.18 ?  101 ASN   A HB2  1 
ATOM   2164 H  HB2  B ASN   A 1 101 ? 19.194 1.906   -12.156 0.44 29.45 ?  101 ASN   A HB2  1 
ATOM   2165 H  HB3  A ASN   A 1 101 ? 18.483 3.387   -12.435 0.56 23.18 ?  101 ASN   A HB3  1 
ATOM   2166 H  HB3  B ASN   A 1 101 ? 18.673 2.480   -13.544 0.44 29.45 ?  101 ASN   A HB3  1 
ATOM   2167 H  HD21 A ASN   A 1 101 ? 16.177 2.161   -9.847  0.56 23.41 ?  101 ASN   A HD21 1 
ATOM   2168 H  HD21 B ASN   A 1 101 ? 15.915 1.598   -11.469 0.44 31.99 ?  101 ASN   A HD21 1 
ATOM   2169 H  HD22 A ASN   A 1 101 ? 17.510 2.805   -9.680  0.56 23.41 ?  101 ASN   A HD22 1 
ATOM   2170 H  HD22 B ASN   A 1 101 ? 17.097 2.483   -11.274 0.44 31.99 ?  101 ASN   A HD22 1 
ATOM   2171 N  N    A LYS   A 1 102 ? 21.664 1.236   -13.144 0.56 23.25 ?  102 LYS   A N    1 
ATOM   2172 N  N    B LYS   A 1 102 ? 21.993 0.394   -13.939 0.44 24.82 ?  102 LYS   A N    1 
ATOM   2173 C  CA   A LYS   A 1 102 ? 22.949 1.443   -13.800 0.56 25.07 ?  102 LYS   A CA   1 
ATOM   2174 C  CA   B LYS   A 1 102 ? 23.320 0.683   -14.468 0.44 25.37 ?  102 LYS   A CA   1 
ATOM   2175 C  C    A LYS   A 1 102 ? 23.271 0.356   -14.817 0.56 25.62 ?  102 LYS   A C    1 
ATOM   2176 C  C    B LYS   A 1 102 ? 23.833 -0.450  -15.349 0.44 24.33 ?  102 LYS   A C    1 
ATOM   2177 O  O    A LYS   A 1 102 ? 24.341 0.405   -15.433 0.56 26.26 ?  102 LYS   A O    1 
ATOM   2178 O  O    B LYS   A 1 102 ? 25.028 -0.490  -15.663 0.44 24.87 ?  102 LYS   A O    1 
ATOM   2179 C  CB   A LYS   A 1 102 ? 24.081 1.496   -12.766 0.56 26.50 ?  102 LYS   A CB   1 
ATOM   2180 C  CB   B LYS   A 1 102 ? 24.313 0.947   -13.330 0.44 27.06 ?  102 LYS   A CB   1 
ATOM   2181 C  CG   A LYS   A 1 102 ? 23.983 2.629   -11.766 0.56 27.58 ?  102 LYS   A CG   1 
ATOM   2182 C  CG   B LYS   A 1 102 ? 24.152 2.307   -12.672 0.44 28.76 ?  102 LYS   A CG   1 
ATOM   2183 C  CD   A LYS   A 1 102 ? 25.163 2.586   -10.803 0.56 28.98 ?  102 LYS   A CD   1 
ATOM   2184 C  CD   B LYS   A 1 102 ? 24.720 2.322   -11.262 0.44 30.40 ?  102 LYS   A CD   1 
ATOM   2185 C  CE   A LYS   A 1 102 ? 25.085 3.687   -9.760  0.56 30.00 ?  102 LYS   A CE   1 
ATOM   2186 C  CE   B LYS   A 1 102 ? 24.663 3.713   -10.659 0.44 31.66 ?  102 LYS   A CE   1 
ATOM   2187 N  NZ   A LYS   A 1 102 ? 26.157 3.548   -8.734  0.56 30.64 ?  102 LYS   A NZ   1 
ATOM   2188 N  NZ   B LYS   A 1 102 ? 25.589 4.646   -11.355 0.44 32.41 ?  102 LYS   A NZ   1 
ATOM   2189 H  H    A LYS   A 1 102 ? 21.673 0.573   -12.594 0.56 27.92 ?  102 LYS   A H    1 
ATOM   2190 H  H    B LYS   A 1 102 ? 21.972 -0.323  -13.464 0.44 29.80 ?  102 LYS   A H    1 
ATOM   2191 H  HA   A LYS   A 1 102 ? 22.935 2.286   -14.270 0.56 30.11 ?  102 LYS   A HA   1 
ATOM   2192 H  HA   B LYS   A 1 102 ? 23.271 1.492   -15.002 0.44 30.46 ?  102 LYS   A HA   1 
ATOM   2193 H  HB2  A LYS   A 1 102 ? 24.084 0.664   -12.267 0.56 31.82 ?  102 LYS   A HB2  1 
ATOM   2194 H  HB2  B LYS   A 1 102 ? 24.195 0.273   -12.644 0.44 32.49 ?  102 LYS   A HB2  1 
ATOM   2195 H  HB3  A LYS   A 1 102 ? 24.925 1.593   -13.236 0.56 31.82 ?  102 LYS   A HB3  1 
ATOM   2196 H  HB3  B LYS   A 1 102 ? 25.217 0.899   -13.684 0.44 32.49 ?  102 LYS   A HB3  1 
ATOM   2197 H  HG2  A LYS   A 1 102 ? 23.999 3.477   -12.236 0.56 33.12 ?  102 LYS   A HG2  1 
ATOM   2198 H  HG2  B LYS   A 1 102 ? 24.626 2.974   -13.195 0.44 34.53 ?  102 LYS   A HG2  1 
ATOM   2199 H  HG3  A LYS   A 1 102 ? 23.164 2.538   -11.255 0.56 33.12 ?  102 LYS   A HG3  1 
ATOM   2200 H  HG3  B LYS   A 1 102 ? 23.210 2.528   -12.623 0.44 34.53 ?  102 LYS   A HG3  1 
ATOM   2201 H  HD2  A LYS   A 1 102 ? 25.167 1.732   -10.343 0.56 34.79 ?  102 LYS   A HD2  1 
ATOM   2202 H  HD2  B LYS   A 1 102 ? 24.198 1.733   -10.698 0.44 36.50 ?  102 LYS   A HD2  1 
ATOM   2203 H  HD3  A LYS   A 1 102 ? 25.987 2.699   -11.304 0.56 34.79 ?  102 LYS   A HD3  1 
ATOM   2204 H  HD3  B LYS   A 1 102 ? 25.645 2.033   -11.283 0.44 36.50 ?  102 LYS   A HD3  1 
ATOM   2205 H  HE2  A LYS   A 1 102 ? 25.190 4.547   -10.197 0.56 36.02 ?  102 LYS   A HE2  1 
ATOM   2206 H  HE2  B LYS   A 1 102 ? 23.760 4.060   -10.742 0.44 38.02 ?  102 LYS   A HE2  1 
ATOM   2207 H  HE3  A LYS   A 1 102 ? 24.226 3.642   -9.313  0.56 36.02 ?  102 LYS   A HE3  1 
ATOM   2208 H  HE3  B LYS   A 1 102 ? 24.918 3.668   -9.724  0.44 38.02 ?  102 LYS   A HE3  1 
ATOM   2209 H  HZ1  A LYS   A 1 102 ? 26.092 4.202   -8.136  0.56 36.79 ?  102 LYS   A HZ1  1 
ATOM   2210 H  HZ1  B LYS   A 1 102 ? 25.564 5.446   -10.968 0.44 38.92 ?  102 LYS   A HZ1  1 
ATOM   2211 H  HZ2  A LYS   A 1 102 ? 26.078 2.765   -8.318  0.56 36.79 ?  102 LYS   A HZ2  1 
ATOM   2212 H  HZ2  B LYS   A 1 102 ? 26.422 4.332   -11.315 0.44 38.92 ?  102 LYS   A HZ2  1 
ATOM   2213 H  HZ3  A LYS   A 1 102 ? 26.957 3.589   -9.123  0.56 36.79 ?  102 LYS   A HZ3  1 
ATOM   2214 H  HZ3  B LYS   A 1 102 ? 25.353 4.729   -12.209 0.44 38.92 ?  102 LYS   A HZ3  1 
ATOM   2215 N  N    A GLY   A 1 103 ? 22.387 -0.623  -15.002 0.56 26.34 ?  103 GLY   A N    1 
ATOM   2216 N  N    B GLY   A 1 103 ? 22.963 -1.375  -15.748 0.44 22.92 ?  103 GLY   A N    1 
ATOM   2217 C  CA   A GLY   A 1 103 ? 22.632 -1.716  -15.924 0.56 26.73 ?  103 GLY   A CA   1 
ATOM   2218 C  CA   B GLY   A 1 103 ? 23.369 -2.510  -16.553 0.44 22.04 ?  103 GLY   A CA   1 
ATOM   2219 C  C    A GLY   A 1 103 ? 23.473 -2.843  -15.371 0.56 27.07 ?  103 GLY   A C    1 
ATOM   2220 C  C    B GLY   A 1 103 ? 24.083 -3.606  -15.792 0.44 21.17 ?  103 GLY   A C    1 
ATOM   2221 O  O    A GLY   A 1 103 ? 23.976 -3.662  -16.146 0.56 28.23 ?  103 GLY   A O    1 
ATOM   2222 O  O    B GLY   A 1 103 ? 24.658 -4.502  -16.420 0.44 21.32 ?  103 GLY   A O    1 
ATOM   2223 H  H    A GLY   A 1 103 ? 21.632 -0.676  -14.604 0.56 31.63 ?  103 GLY   A H    1 
ATOM   2224 H  H    B GLY   A 1 103 ? 22.126 -1.358  -15.560 0.44 27.53 ?  103 GLY   A H    1 
ATOM   2225 H  HA2  A GLY   A 1 103 ? 21.778 -2.079  -16.222 0.56 32.10 ?  103 GLY   A HA2  1 
ATOM   2226 H  HA2  B GLY   A 1 103 ? 22.579 -2.895  -16.961 0.44 26.47 ?  103 GLY   A HA2  1 
ATOM   2227 H  HA3  A GLY   A 1 103 ? 23.096 -1.375  -16.702 0.56 32.10 ?  103 GLY   A HA3  1 
ATOM   2228 H  HA3  B GLY   A 1 103 ? 23.948 -2.189  -17.268 0.44 26.47 ?  103 GLY   A HA3  1 
ATOM   2229 N  N    A GLU   A 1 104 ? 23.644 -2.915  -14.055 0.56 25.99 ?  104 GLU   A N    1 
ATOM   2230 N  N    B GLU   A 1 104 ? 24.046 -3.577  -14.463 0.44 19.73 ?  104 GLU   A N    1 
ATOM   2231 C  CA   A GLU   A 1 104 ? 24.507 -3.920  -13.452 0.56 25.18 ?  104 GLU   A CA   1 
ATOM   2232 C  CA   B GLU   A 1 104 ? 24.847 -4.489  -13.659 0.44 18.39 ?  104 GLU   A CA   1 
ATOM   2233 C  C    A GLU   A 1 104 ? 23.809 -5.275  -13.368 0.56 25.74 ?  104 GLU   A C    1 
ATOM   2234 C  C    B GLU   A 1 104 ? 24.156 -5.839  -13.500 0.44 17.73 ?  104 GLU   A C    1 
ATOM   2235 O  O    A GLU   A 1 104 ? 22.588 -5.367  -13.205 0.56 26.17 ?  104 GLU   A O    1 
ATOM   2236 O  O    B GLU   A 1 104 ? 22.927 -5.928  -13.414 0.44 18.48 ?  104 GLU   A O    1 
ATOM   2237 C  CB   A GLU   A 1 104 ? 24.991 -3.442  -12.079 0.56 23.96 ?  104 GLU   A CB   1 
ATOM   2238 C  CB   B GLU   A 1 104 ? 25.175 -3.852  -12.306 0.44 18.30 ?  104 GLU   A CB   1 
ATOM   2239 C  CG   A GLU   A 1 104 ? 25.951 -2.254  -12.219 0.56 23.46 ?  104 GLU   A CG   1 
ATOM   2240 C  CG   B GLU   A 1 104 ? 26.033 -2.595  -12.465 0.44 19.03 ?  104 GLU   A CG   1 
ATOM   2241 C  CD   A GLU   A 1 104 ? 26.294 -1.529  -10.924 0.56 22.38 ?  104 GLU   A CD   1 
ATOM   2242 C  CD   B GLU   A 1 104 ? 26.339 -1.871  -11.164 0.44 19.16 ?  104 GLU   A CD   1 
ATOM   2243 O  OE1  A GLU   A 1 104 ? 25.659 -1.783  -9.883  0.56 20.34 ?  104 GLU   A OE1  1 
ATOM   2244 O  OE1  B GLU   A 1 104 ? 25.878 -2.304  -10.091 0.44 19.07 ?  104 GLU   A OE1  1 
ATOM   2245 O  OE2  A GLU   A 1 104 ? 27.212 -0.676  -10.966 0.56 23.54 -1 104 GLU   A OE2  1 
ATOM   2246 O  OE2  B GLU   A 1 104 ? 27.048 -0.844  -11.227 0.44 19.95 -1 104 GLU   A OE2  1 
ATOM   2247 H  H    A GLU   A 1 104 ? 23.278 -2.385  -13.491 0.56 31.21 ?  104 GLU   A H    1 
ATOM   2248 H  H    B GLU   A 1 104 ? 23.559 -3.036  -14.011 0.44 23.70 ?  104 GLU   A H    1 
ATOM   2249 H  HA   A GLU   A 1 104 ? 25.285 -4.033  -14.016 0.56 30.24 ?  104 GLU   A HA   1 
ATOM   2250 H  HA   B GLU   A 1 104 ? 25.685 -4.643  -14.116 0.44 22.09 ?  104 GLU   A HA   1 
ATOM   2251 H  HB2  A GLU   A 1 104 ? 24.224 -3.168  -11.552 0.56 28.78 ?  104 GLU   A HB2  1 
ATOM   2252 H  HB2  B GLU   A 1 104 ? 24.352 -3.601  -11.860 0.44 21.98 ?  104 GLU   A HB2  1 
ATOM   2253 H  HB3  A GLU   A 1 104 ? 25.457 -4.171  -11.638 0.56 28.78 ?  104 GLU   A HB3  1 
ATOM   2254 H  HB3  B GLU   A 1 104 ? 25.671 -4.487  -11.768 0.44 21.98 ?  104 GLU   A HB3  1 
ATOM   2255 H  HG2  A GLU   A 1 104 ? 26.776 -2.578  -12.603 0.56 28.17 ?  104 GLU   A HG2  1 
ATOM   2256 H  HG2  B GLU   A 1 104 ? 26.876 -2.843  -12.873 0.44 22.85 ?  104 GLU   A HG2  1 
ATOM   2257 H  HG3  A GLU   A 1 104 ? 25.542 -1.606  -12.811 0.56 28.17 ?  104 GLU   A HG3  1 
ATOM   2258 H  HG3  B GLU   A 1 104 ? 25.563 -1.969  -13.043 0.44 22.85 ?  104 GLU   A HG3  1 
ATOM   2259 N  N    A ASP   A 1 105 ? 24.611 -6.333  -13.482 0.56 25.94 ?  105 ASP   A N    1 
ATOM   2260 N  N    B ASP   A 1 105 ? 24.972 -6.890  -13.476 0.44 18.04 ?  105 ASP   A N    1 
ATOM   2261 C  CA   A ASP   A 1 105 ? 24.099 -7.690  -13.628 0.56 26.40 ?  105 ASP   A CA   1 
ATOM   2262 C  CA   B ASP   A 1 105 ? 24.497 -8.268  -13.531 0.44 19.17 ?  105 ASP   A CA   1 
ATOM   2263 C  C    A ASP   A 1 105 ? 23.426 -8.140  -12.335 0.56 24.72 ?  105 ASP   A C    1 
ATOM   2264 C  C    B ASP   A 1 105 ? 23.742 -8.631  -12.256 0.44 18.09 ?  105 ASP   A C    1 
ATOM   2265 O  O    A ASP   A 1 105 ? 24.068 -8.203  -11.283 0.56 23.31 ?  105 ASP   A O    1 
ATOM   2266 O  O    B ASP   A 1 105 ? 24.319 -8.644  -11.166 0.44 16.29 ?  105 ASP   A O    1 
ATOM   2267 C  CB   A ASP   A 1 105 ? 25.258 -8.621  -13.983 0.56 28.50 ?  105 ASP   A CB   1 
ATOM   2268 C  CB   B ASP   A 1 105 ? 25.712 -9.174  -13.700 0.44 21.10 ?  105 ASP   A CB   1 
ATOM   2269 C  CG   A ASP   A 1 105 ? 24.811 -10.046 -14.211 0.56 30.54 ?  105 ASP   A CG   1 
ATOM   2270 C  CG   B ASP   A 1 105 ? 25.340 -10.622 -13.931 0.44 22.67 ?  105 ASP   A CG   1 
ATOM   2271 O  OD1  A ASP   A 1 105 ? 23.587 -10.274 -14.318 0.56 31.08 ?  105 ASP   A OD1  1 
ATOM   2272 O  OD1  B ASP   A 1 105 ? 24.133 -10.940 -13.990 0.44 22.87 ?  105 ASP   A OD1  1 
ATOM   2273 O  OD2  A ASP   A 1 105 ? 25.683 -10.937 -14.286 0.56 31.73 -1 105 ASP   A OD2  1 
ATOM   2274 O  OD2  B ASP   A 1 105 ? 26.269 -11.449 -14.048 0.44 23.52 -1 105 ASP   A OD2  1 
ATOM   2275 H  H    A ASP   A 1 105 ? 25.470 -6.295  -13.468 0.56 31.15 ?  105 ASP   A H    1 
ATOM   2276 H  H    B ASP   A 1 105 ? 25.826 -6.824  -13.440 0.44 21.67 ?  105 ASP   A H    1 
ATOM   2277 H  HA   A ASP   A 1 105 ? 23.448 -7.733  -14.346 0.56 31.71 ?  105 ASP   A HA   1 
ATOM   2278 H  HA   B ASP   A 1 105 ? 23.903 -8.385  -14.288 0.44 23.02 ?  105 ASP   A HA   1 
ATOM   2279 H  HB2  A ASP   A 1 105 ? 25.678 -8.313  -14.806 0.56 34.22 ?  105 ASP   A HB2  1 
ATOM   2280 H  HB2  B ASP   A 1 105 ? 26.242 -8.846  -14.450 0.44 25.34 ?  105 ASP   A HB2  1 
ATOM   2281 H  HB3  A ASP   A 1 105 ? 25.912 -8.613  -13.263 0.56 34.22 ?  105 ASP   A HB3  1 
ATOM   2282 H  HB3  B ASP   A 1 105 ? 26.245 -9.140  -12.889 0.44 25.34 ?  105 ASP   A HB3  1 
ATOM   2283 N  N    A ILE   A 1 106 ? 22.130 -8.458  -12.415 0.56 24.30 ?  106 ILE   A N    1 
ATOM   2284 N  N    B ILE   A 1 106 ? 22.453 -8.949  -12.393 0.44 19.08 ?  106 ILE   A N    1 
ATOM   2285 C  CA   A ILE   A 1 106 ? 21.378 -8.895  -11.242 0.56 23.33 ?  106 ILE   A CA   1 
ATOM   2286 C  CA   B ILE   A 1 106 ? 21.662 -9.313  -11.224 0.44 20.32 ?  106 ILE   A CA   1 
ATOM   2287 C  C    A ILE   A 1 106 ? 21.929 -10.190 -10.662 0.56 22.29 ?  106 ILE   A C    1 
ATOM   2288 C  C    B ILE   A 1 106 ? 22.132 -10.622 -10.605 0.44 20.22 ?  106 ILE   A C    1 
ATOM   2289 O  O    A ILE   A 1 106 ? 21.723 -10.470 -9.477  0.56 21.13 ?  106 ILE   A O    1 
ATOM   2290 O  O    B ILE   A 1 106 ? 21.845 -10.881 -9.431  0.44 20.03 ?  106 ILE   A O    1 
ATOM   2291 C  CB   A ILE   A 1 106 ? 19.871 -9.011  -11.573 0.56 24.22 ?  106 ILE   A CB   1 
ATOM   2292 C  CB   B ILE   A 1 106 ? 20.154 -9.316  -11.547 0.44 22.56 ?  106 ILE   A CB   1 
ATOM   2293 C  CG1  A ILE   A 1 106 ? 19.036 -9.111  -10.294 0.56 24.27 ?  106 ILE   A CG1  1 
ATOM   2294 C  CG1  B ILE   A 1 106 ? 19.331 -9.136  -10.268 0.44 23.94 ?  106 ILE   A CG1  1 
ATOM   2295 C  CG2  A ILE   A 1 106 ? 19.602 -10.233 -12.419 0.56 24.81 ?  106 ILE   A CG2  1 
ATOM   2296 C  CG2  B ILE   A 1 106 ? 19.753 -10.603 -12.241 0.44 23.20 ?  106 ILE   A CG2  1 
ATOM   2297 C  CD1  A ILE   A 1 106 ? 19.160 -7.915  -9.384  0.56 24.37 ?  106 ILE   A CD1  1 
ATOM   2298 C  CD1  B ILE   A 1 106 ? 19.683 -7.882  -9.487  0.44 24.57 ?  106 ILE   A CD1  1 
ATOM   2299 H  H    A ILE   A 1 106 ? 21.667 -8.415  -13.135 0.56 29.18 ?  106 ILE   A H    1 
ATOM   2300 H  H    B ILE   A 1 106 ? 22.026 -8.955  -13.134 0.44 22.92 ?  106 ILE   A H    1 
ATOM   2301 H  HA   A ILE   A 1 106 ? 21.477 -8.218  -10.561 0.56 28.02 ?  106 ILE   A HA   1 
ATOM   2302 H  HA   B ILE   A 1 106 ? 21.820 -8.637  -10.556 0.44 24.41 ?  106 ILE   A HA   1 
ATOM   2303 H  HB   A ILE   A 1 106 ? 19.595 -8.221  -12.065 0.56 29.08 ?  106 ILE   A HB   1 
ATOM   2304 H  HB   B ILE   A 1 106 ? 19.965 -8.572  -12.141 0.44 27.09 ?  106 ILE   A HB   1 
ATOM   2305 H  HG12 A ILE   A 1 106 ? 18.100 -9.197  -10.539 0.56 29.14 ?  106 ILE   A HG12 1 
ATOM   2306 H  HG12 B ILE   A 1 106 ? 18.392 -9.081  -10.503 0.44 28.75 ?  106 ILE   A HG12 1 
ATOM   2307 H  HG13 A ILE   A 1 106 ? 19.317 -9.893  -9.795  0.56 29.14 ?  106 ILE   A HG13 1 
ATOM   2308 H  HG13 B ILE   A 1 106 ? 19.482 -9.897  -9.687  0.44 28.75 ?  106 ILE   A HG13 1 
ATOM   2309 H  HG21 A ILE   A 1 106 ? 18.729 -10.142 -12.828 0.56 29.80 ?  106 ILE   A HG21 1 
ATOM   2310 H  HG21 B ILE   A 1 106 ? 18.889 -10.474 -12.662 0.44 27.86 ?  106 ILE   A HG21 1 
ATOM   2311 H  HG22 A ILE   A 1 106 ? 20.288 -10.296 -13.097 0.56 29.80 ?  106 ILE   A HG22 1 
ATOM   2312 H  HG22 B ILE   A 1 106 ? 20.421 -10.817 -12.908 0.44 27.86 ?  106 ILE   A HG22 1 
ATOM   2313 H  HG23 A ILE   A 1 106 ? 19.622 -11.017 -11.848 0.56 29.80 ?  106 ILE   A HG23 1 
ATOM   2314 H  HG23 B ILE   A 1 106 ? 19.699 -11.312 -11.582 0.44 27.86 ?  106 ILE   A HG23 1 
ATOM   2315 H  HD11 A ILE   A 1 106 ? 18.424 -7.922  -8.754  0.56 29.27 ?  106 ILE   A HD11 1 
ATOM   2316 H  HD11 B ILE   A 1 106 ? 18.917 -7.611  -8.962  0.44 29.50 ?  106 ILE   A HD11 1 
ATOM   2317 H  HD12 A ILE   A 1 106 ? 20.004 -7.966  -8.908  0.56 29.27 ?  106 ILE   A HD12 1 
ATOM   2318 H  HD12 B ILE   A 1 106 ? 20.435 -8.074  -8.902  0.44 29.50 ?  106 ILE   A HD12 1 
ATOM   2319 H  HD13 A ILE   A 1 106 ? 19.129 -7.107  -9.920  0.56 29.27 ?  106 ILE   A HD13 1 
ATOM   2320 H  HD13 B ILE   A 1 106 ? 19.922 -7.178  -10.112 0.44 29.50 ?  106 ILE   A HD13 1 
ATOM   2321 N  N    A GLN   A 1 107 ? 22.640 -10.986 -11.466 0.56 22.96 ?  107 GLN   A N    1 
ATOM   2322 N  N    B GLN   A 1 107 ? 22.856 -11.454 -11.362 0.44 20.72 ?  107 GLN   A N    1 
ATOM   2323 C  CA   A GLN   A 1 107 ? 23.236 -12.218 -10.961 0.56 24.32 ?  107 GLN   A CA   1 
ATOM   2324 C  CA   B GLN   A 1 107 ? 23.503 -12.621 -10.771 0.44 22.61 ?  107 GLN   A CA   1 
ATOM   2325 C  C    A GLN   A 1 107 ? 24.233 -11.954 -9.839  0.56 21.95 ?  107 GLN   A C    1 
ATOM   2326 C  C    B GLN   A 1 107 ? 24.432 -12.223 -9.631  0.44 20.58 ?  107 GLN   A C    1 
ATOM   2327 O  O    A GLN   A 1 107 ? 24.486 -12.846 -9.023  0.56 23.51 ?  107 GLN   A O    1 
ATOM   2328 O  O    B GLN   A 1 107 ? 24.676 -13.020 -8.717  0.44 21.38 ?  107 GLN   A O    1 
ATOM   2329 C  CB   A GLN   A 1 107 ? 23.913 -12.982 -12.104 0.56 28.08 ?  107 GLN   A CB   1 
ATOM   2330 C  CB   B GLN   A 1 107 ? 24.273 -13.387 -11.850 0.44 26.22 ?  107 GLN   A CB   1 
ATOM   2331 C  CG   A GLN   A 1 107 ? 23.001 -13.263 -13.291 0.56 32.18 ?  107 GLN   A CG   1 
ATOM   2332 C  CG   B GLN   A 1 107 ? 23.394 -13.931 -12.965 0.44 29.83 ?  107 GLN   A CG   1 
ATOM   2333 C  CD   A GLN   A 1 107 ? 21.752 -14.028 -12.902 0.56 35.41 ?  107 GLN   A CD   1 
ATOM   2334 C  CD   B GLN   A 1 107 ? 22.411 -14.971 -12.469 0.44 32.67 ?  107 GLN   A CD   1 
ATOM   2335 O  OE1  A GLN   A 1 107 ? 21.823 -15.047 -12.213 0.56 36.87 ?  107 GLN   A OE1  1 
ATOM   2336 O  OE1  B GLN   A 1 107 ? 22.749 -15.818 -11.641 0.44 33.94 ?  107 GLN   A OE1  1 
ATOM   2337 N  NE2  A GLN   A 1 107 ? 20.598 -13.537 -13.336 0.56 36.75 ?  107 GLN   A NE2  1 
ATOM   2338 N  NE2  B GLN   A 1 107 ? 21.182 -14.908 -12.968 0.44 33.78 ?  107 GLN   A NE2  1 
ATOM   2339 H  H    A GLN   A 1 107 ? 22.795 -10.829 -12.294 0.56 27.57 ?  107 GLN   A H    1 
ATOM   2340 H  H    B GLN   A 1 107 ? 22.979 -11.367 -12.210 0.44 24.88 ?  107 GLN   A H    1 
ATOM   2341 H  HA   A GLN   A 1 107 ? 22.537 -12.783 -10.604 0.56 29.20 ?  107 GLN   A HA   1 
ATOM   2342 H  HA   B GLN   A 1 107 ? 22.826 -13.214 -10.412 0.44 27.16 ?  107 GLN   A HA   1 
ATOM   2343 H  HB2  A GLN   A 1 107 ? 24.665 -12.463 -12.429 0.56 33.72 ?  107 GLN   A HB2  1 
ATOM   2344 H  HB2  B GLN   A 1 107 ? 24.927 -12.795 -12.254 0.44 31.49 ?  107 GLN   A HB2  1 
ATOM   2345 H  HB3  A GLN   A 1 107 ? 24.227 -13.837 -11.769 0.56 33.72 ?  107 GLN   A HB3  1 
ATOM   2346 H  HB3  B GLN   A 1 107 ? 24.723 -14.143 -11.440 0.44 31.49 ?  107 GLN   A HB3  1 
ATOM   2347 H  HG2  A GLN   A 1 107 ? 22.723 -12.422 -13.686 0.56 38.64 ?  107 GLN   A HG2  1 
ATOM   2348 H  HG2  B GLN   A 1 107 ? 22.890 -13.200 -13.357 0.44 35.81 ?  107 GLN   A HG2  1 
ATOM   2349 H  HG3  A GLN   A 1 107 ? 23.486 -13.791 -13.946 0.56 38.64 ?  107 GLN   A HG3  1 
ATOM   2350 H  HG3  B GLN   A 1 107 ? 23.956 -14.344 -13.641 0.44 35.81 ?  107 GLN   A HG3  1 
ATOM   2351 H  HE21 A GLN   A 1 107 ? 20.587 -12.822 -13.813 0.56 44.12 ?  107 GLN   A HE21 1 
ATOM   2352 H  HE21 B GLN   A 1 107 ? 20.982 -14.301 -13.543 0.44 40.56 ?  107 GLN   A HE21 1 
ATOM   2353 H  HE22 A GLN   A 1 107 ? 19.861 -13.935 -13.142 0.56 44.12 ?  107 GLN   A HE22 1 
ATOM   2354 H  HE22 B GLN   A 1 107 ? 20.588 -15.475 -12.715 0.44 40.56 ?  107 GLN   A HE22 1 
ATOM   2355 N  N    A LEU   A 1 108 ? 24.789 -10.744 -9.764  0.56 18.26 ?  108 LEU   A N    1 
ATOM   2356 N  N    B LEU   A 1 108 ? 24.952 -10.995 -9.658  0.44 18.25 ?  108 LEU   A N    1 
ATOM   2357 C  CA   A LEU   A 1 108 ? 25.728 -10.400 -8.701  0.56 15.76 ?  108 LEU   A CA   1 
ATOM   2358 C  CA   B LEU   A 1 108 ? 25.812 -10.518 -8.584  0.44 16.40 ?  108 LEU   A CA   1 
ATOM   2359 C  C    A LEU   A 1 108 ? 25.046 -10.248 -7.346  0.56 13.54 ?  108 LEU   A C    1 
ATOM   2360 C  C    B LEU   A 1 108 ? 25.052 -10.274 -7.288  0.44 14.20 ?  108 LEU   A C    1 
ATOM   2361 O  O    A LEU   A 1 108 ? 25.738 -10.101 -6.335  0.56 14.01 ?  108 LEU   A O    1 
ATOM   2362 O  O    B LEU   A 1 108 ? 25.692 -10.066 -6.252  0.44 14.52 ?  108 LEU   A O    1 
ATOM   2363 C  CB   A LEU   A 1 108 ? 26.483 -9.119  -9.069  0.56 15.97 ?  108 LEU   A CB   1 
ATOM   2364 C  CB   B LEU   A 1 108 ? 26.556 -9.248  -9.010  0.44 16.87 ?  108 LEU   A CB   1 
ATOM   2365 C  CG   A LEU   A 1 108 ? 27.467 -9.289  -10.228 0.56 17.26 ?  108 LEU   A CG   1 
ATOM   2366 C  CG   B LEU   A 1 108 ? 27.571 -9.445  -10.138 0.44 17.96 ?  108 LEU   A CG   1 
ATOM   2367 C  CD1  A LEU   A 1 108 ? 27.922 -7.943  -10.774 0.56 17.77 ?  108 LEU   A CD1  1 
ATOM   2368 C  CD1  B LEU   A 1 108 ? 28.144 -8.115  -10.611 0.44 18.35 ?  108 LEU   A CD1  1 
ATOM   2369 C  CD2  A LEU   A 1 108 ? 28.667 -10.110 -9.787  0.56 18.64 ?  108 LEU   A CD2  1 
ATOM   2370 C  CD2  B LEU   A 1 108 ? 28.689 -10.375 -9.695  0.44 18.98 ?  108 LEU   A CD2  1 
ATOM   2371 H  H    A LEU   A 1 108 ? 24.636 -10.109 -10.316 0.56 21.93 ?  108 LEU   A H    1 
ATOM   2372 H  H    B LEU   A 1 108 ? 24.821 -10.426 -10.283 0.44 21.92 ?  108 LEU   A H    1 
ATOM   2373 H  HA   A LEU   A 1 108 ? 26.379 -11.114 -8.621  0.56 18.93 ?  108 LEU   A HA   1 
ATOM   2374 H  HA   B LEU   A 1 108 ? 26.479 -11.198 -8.398  0.44 19.70 ?  108 LEU   A HA   1 
ATOM   2375 H  HB2  A LEU   A 1 108 ? 25.840 -8.441  -9.327  0.56 19.19 ?  108 LEU   A HB2  1 
ATOM   2376 H  HB2  B LEU   A 1 108 ? 25.908 -8.593  -9.310  0.44 20.27 ?  108 LEU   A HB2  1 
ATOM   2377 H  HB3  A LEU   A 1 108 ? 26.986 -8.820  -8.297  0.56 19.19 ?  108 LEU   A HB3  1 
ATOM   2378 H  HB3  B LEU   A 1 108 ? 27.039 -8.901  -8.243  0.44 20.27 ?  108 LEU   A HB3  1 
ATOM   2379 H  HG   A LEU   A 1 108 ? 27.030 -9.768  -10.949 0.56 20.73 ?  108 LEU   A HG   1 
ATOM   2380 H  HG   B LEU   A 1 108 ? 27.124 -9.857  -10.892 0.44 21.57 ?  108 LEU   A HG   1 
ATOM   2381 H  HD11 A LEU   A 1 108 ? 28.520 -8.092  -11.526 0.56 21.34 ?  108 LEU   A HD11 1 
ATOM   2382 H  HD11 B LEU   A 1 108 ? 28.775 -8.279  -11.331 0.44 22.04 ?  108 LEU   A HD11 1 
ATOM   2383 H  HD12 A LEU   A 1 108 ? 27.147 -7.440  -11.063 0.56 21.34 ?  108 LEU   A HD12 1 
ATOM   2384 H  HD12 B LEU   A 1 108 ? 27.419 -7.554  -10.932 0.44 22.04 ?  108 LEU   A HD12 1 
ATOM   2385 H  HD13 A LEU   A 1 108 ? 28.390 -7.460  -10.074 0.56 21.34 ?  108 LEU   A HD13 1 
ATOM   2386 H  HD13 B LEU   A 1 108 ? 28.594 -7.681  -9.870  0.44 22.04 ?  108 LEU   A HD13 1 
ATOM   2387 H  HD21 A LEU   A 1 108 ? 29.337 -10.095 -10.487 0.56 22.39 ?  108 LEU   A HD21 1 
ATOM   2388 H  HD21 B LEU   A 1 108 ? 29.409 -10.332 -10.342 0.44 22.80 ?  108 LEU   A HD21 1 
ATOM   2389 H  HD22 A LEU   A 1 108 ? 29.029 -9.726  -8.973  0.56 22.39 ?  108 LEU   A HD22 1 
ATOM   2390 H  HD22 B LEU   A 1 108 ? 29.008 -10.090 -8.824  0.44 22.80 ?  108 LEU   A HD22 1 
ATOM   2391 H  HD23 A LEU   A 1 108 ? 28.382 -11.023 -9.622  0.56 22.39 ?  108 LEU   A HD23 1 
ATOM   2392 H  HD23 B LEU   A 1 108 ? 28.343 -11.279 -9.642  0.44 22.80 ?  108 LEU   A HD23 1 
ATOM   2393 N  N    . LEU   A 1 109 ? 23.715 -10.321 -7.299  1.00 13.53 ?  109 LEU   A N    1 
ATOM   2394 C  CA   . LEU   A 1 109 ? 22.997 -10.180 -6.039  1.00 12.84 ?  109 LEU   A CA   1 
ATOM   2395 C  C    . LEU   A 1 109 ? 23.321 -11.332 -5.091  1.00 12.33 ?  109 LEU   A C    1 
ATOM   2396 O  O    . LEU   A 1 109 ? 23.455 -11.129 -3.880  1.00 12.81 ?  109 LEU   A O    1 
ATOM   2397 C  CB   . LEU   A 1 109 ? 21.497 -10.086 -6.310  1.00 13.37 ?  109 LEU   A CB   1 
ATOM   2398 C  CG   . LEU   A 1 109 ? 20.598 -9.820  -5.104  1.00 13.83 ?  109 LEU   A CG   1 
ATOM   2399 C  CD1  . LEU   A 1 109 ? 21.039 -8.562  -4.370  1.00 14.01 ?  109 LEU   A CD1  1 
ATOM   2400 C  CD2  . LEU   A 1 109 ? 19.133 -9.713  -5.540  1.00 15.03 ?  109 LEU   A CD2  1 
ATOM   2401 H  H    A LEU   A 1 109 ? 23.209 -10.452 -7.980  0.56 16.25 ?  109 LEU   A H    1 
ATOM   2402 H  H    B LEU   A 1 109 ? 23.223 -10.435 -7.993  0.44 16.25 ?  109 LEU   A H    1 
ATOM   2403 H  HA   . LEU   A 1 109 ? 23.278 -9.354  -5.613  1.00 15.43 ?  109 LEU   A HA   1 
ATOM   2404 H  HB2  . LEU   A 1 109 ? 21.348 -9.364  -6.940  1.00 16.07 ?  109 LEU   A HB2  1 
ATOM   2405 H  HB3  . LEU   A 1 109 ? 21.206 -10.922 -6.701  1.00 16.07 ?  109 LEU   A HB3  1 
ATOM   2406 H  HG   . LEU   A 1 109 ? 20.668 -10.561 -4.485  1.00 16.62 ?  109 LEU   A HG   1 
ATOM   2407 H  HD11 . LEU   A 1 109 ? 20.352 -8.298  -3.740  1.00 16.83 ?  109 LEU   A HD11 1 
ATOM   2408 H  HD12 . LEU   A 1 109 ? 21.868 -8.741  -3.900  1.00 16.83 ?  109 LEU   A HD12 1 
ATOM   2409 H  HD13 . LEU   A 1 109 ? 21.178 -7.850  -5.020  1.00 16.83 ?  109 LEU   A HD13 1 
ATOM   2410 H  HD21 . LEU   A 1 109 ? 18.603 -9.367  -4.802  1.00 18.06 ?  109 LEU   A HD21 1 
ATOM   2411 H  HD22 . LEU   A 1 109 ? 19.066 -9.114  -6.300  1.00 18.06 ?  109 LEU   A HD22 1 
ATOM   2412 H  HD23 . LEU   A 1 109 ? 18.809 -10.596 -5.789  1.00 18.06 ?  109 LEU   A HD23 1 
ATOM   2413 N  N    . LYS   A 1 110 ? 23.456 -12.550 -5.619  1.00 12.45 ?  110 LYS   A N    1 
ATOM   2414 C  CA   . LYS   A 1 110 ? 23.825 -13.666 -4.753  1.00 12.69 ?  110 LYS   A CA   1 
ATOM   2415 C  C    . LYS   A 1 110 ? 25.202 -13.443 -4.139  1.00 12.06 ?  110 LYS   A C    1 
ATOM   2416 O  O    . LYS   A 1 110 ? 25.389 -13.647 -2.938  1.00 12.29 ?  110 LYS   A O    1 
ATOM   2417 C  CB   . LYS   A 1 110 ? 23.761 -14.994 -5.510  1.00 13.58 ?  110 LYS   A CB   1 
ATOM   2418 C  CG   . LYS   A 1 110 ? 23.934 -16.205 -4.599  1.00 13.73 ?  110 LYS   A CG   1 
ATOM   2419 C  CD   . LYS   A 1 110 ? 23.698 -17.526 -5.318  1.00 14.56 ?  110 LYS   A CD   1 
ATOM   2420 C  CE   . LYS   A 1 110 ? 23.819 -18.708 -4.370  1.00 15.27 ?  110 LYS   A CE   1 
ATOM   2421 N  NZ   . LYS   A 1 110 ? 22.649 -18.831 -3.469  1.00 15.20 ?  110 LYS   A NZ   1 
ATOM   2422 H  H    . LYS   A 1 110 ? 23.335 -12.750 -6.441  1.00 14.96 ?  110 LYS   A H    1 
ATOM   2423 H  HA   . LYS   A 1 110 ? 23.180 -13.718 -4.023  1.00 15.25 ?  110 LYS   A HA   1 
ATOM   2424 H  HB2  . LYS   A 1 110 ? 22.898 -15.071 -5.945  1.00 16.32 ?  110 LYS   A HB2  1 
ATOM   2425 H  HB3  . LYS   A 1 110 ? 24.470 -15.016 -6.167  1.00 16.32 ?  110 LYS   A HB3  1 
ATOM   2426 H  HG2  . LYS   A 1 110 ? 24.836 -16.209 -4.244  1.00 16.49 ?  110 LYS   A HG2  1 
ATOM   2427 H  HG3  . LYS   A 1 110 ? 23.294 -16.143 -3.868  1.00 16.49 ?  110 LYS   A HG3  1 
ATOM   2428 H  HD2  . LYS   A 1 110 ? 22.807 -17.531 -5.694  1.00 17.50 ?  110 LYS   A HD2  1 
ATOM   2429 H  HD3  . LYS   A 1 110 ? 24.362 -17.627 -6.018  1.00 17.50 ?  110 LYS   A HD3  1 
ATOM   2430 H  HE2  . LYS   A 1 110 ? 23.895 -19.526 -4.886  1.00 18.34 ?  110 LYS   A HE2  1 
ATOM   2431 H  HE3  . LYS   A 1 110 ? 24.613 -18.594 -3.816  1.00 18.34 ?  110 LYS   A HE3  1 
ATOM   2432 H  HZ1  . LYS   A 1 110 ? 22.745 -19.529 -2.929  1.00 18.26 ?  110 LYS   A HZ1  1 
ATOM   2433 H  HZ2  . LYS   A 1 110 ? 22.559 -18.093 -2.978  1.00 18.26 ?  110 LYS   A HZ2  1 
ATOM   2434 H  HZ3  . LYS   A 1 110 ? 21.905 -18.942 -3.953  1.00 18.26 ?  110 LYS   A HZ3  1 
ATOM   2435 N  N    . SER   A 1 111 ? 26.170 -12.993 -4.943  1.00 12.15 ?  111 SER   A N    1 
ATOM   2436 C  CA   . SER   A 1 111 ? 27.498 -12.681 -4.415  1.00 12.31 ?  111 SER   A CA   1 
ATOM   2437 C  C    . SER   A 1 111 ? 27.426 -11.633 -3.310  1.00 11.66 ?  111 SER   A C    1 
ATOM   2438 O  O    . SER   A 1 111 ? 28.115 -11.741 -2.288  1.00 12.42 ?  111 SER   A O    1 
ATOM   2439 C  CB   . SER   A 1 111 ? 28.398 -12.195 -5.551  1.00 13.41 ?  111 SER   A CB   1 
ATOM   2440 O  OG   . SER   A 1 111 ? 28.469 -13.176 -6.573  1.00 15.08 ?  111 SER   A OG   1 
ATOM   2441 H  H    . SER   A 1 111 ? 26.076 -12.863 -5.784  1.00 14.60 ?  111 SER   A H    1 
ATOM   2442 H  HA   . SER   A 1 111 ? 27.890 -13.492 -4.047  1.00 14.79 ?  111 SER   A HA   1 
ATOM   2443 H  HB2  . SER   A 1 111 ? 28.020 -11.386 -5.931  1.00 16.12 ?  111 SER   A HB2  1 
ATOM   2444 H  HB3  . SER   A 1 111 ? 29.284 -12.023 -5.208  1.00 16.12 ?  111 SER   A HB3  1 
ATOM   2445 H  HG   . SER   A 1 111 ? 28.978 -12.906 -7.199  1.00 18.12 ?  111 SER   A HG   1 
ATOM   2446 N  N    . ALA   A 1 112 ? 26.590 -10.610 -3.499  1.00 11.78 ?  112 ALA   A N    1 
ATOM   2447 C  CA   . ALA   A 1 112 ? 26.434 -9.575  -2.484  1.00 11.60 ?  112 ALA   A CA   1 
ATOM   2448 C  C    . ALA   A 1 112 ? 25.941 -10.171 -1.166  1.00 11.40 ?  112 ALA   A C    1 
ATOM   2449 O  O    . ALA   A 1 112 ? 26.482 -9.876  -0.094  1.00 11.80 ?  112 ALA   A O    1 
ATOM   2450 C  CB   . ALA   A 1 112 ? 25.474 -8.496  -2.988  1.00 12.09 ?  112 ALA   A CB   1 
ATOM   2451 H  H    . ALA   A 1 112 ? 26.112 -10.496 -4.201  1.00 14.16 ?  112 ALA   A H    1 
ATOM   2452 H  HA   . ALA   A 1 112 ? 27.293 -9.159  -2.320  1.00 13.94 ?  112 ALA   A HA   1 
ATOM   2453 H  HB1  . ALA   A 1 112 ? 25.394 -7.803  -2.309  1.00 14.53 ?  112 ALA   A HB1  1 
ATOM   2454 H  HB2  . ALA   A 1 112 ? 25.826 -8.114  -3.806  1.00 14.53 ?  112 ALA   A HB2  1 
ATOM   2455 H  HB3  . ALA   A 1 112 ? 24.605 -8.894  -3.154  1.00 14.53 ?  112 ALA   A HB3  1 
ATOM   2456 N  N    . TYR   A 1 113 ? 24.907 -11.017 -1.223  1.00 11.44 ?  113 TYR   A N    1 
ATOM   2457 C  CA   . TYR   A 1 113 ? 24.389 -11.626 -0.000  1.00 11.35 ?  113 TYR   A CA   1 
ATOM   2458 C  C    . TYR   A 1 113 ? 25.391 -12.571 0.655   1.00 10.83 ?  113 TYR   A C    1 
ATOM   2459 O  O    . TYR   A 1 113 ? 25.345 -12.755 1.874   1.00 11.80 ?  113 TYR   A O    1 
ATOM   2460 C  CB   . TYR   A 1 113 ? 23.071 -12.356 -0.278  1.00 11.65 ?  113 TYR   A CB   1 
ATOM   2461 C  CG   . TYR   A 1 113 ? 21.853 -11.452 -0.238  1.00 11.67 ?  113 TYR   A CG   1 
ATOM   2462 C  CD1  . TYR   A 1 113 ? 21.469 -10.820 0.939   1.00 12.14 ?  113 TYR   A CD1  1 
ATOM   2463 C  CD2  . TYR   A 1 113 ? 21.065 -11.268 -1.362  1.00 11.56 ?  113 TYR   A CD2  1 
ATOM   2464 C  CE1  . TYR   A 1 113 ? 20.344 -10.020 0.990   1.00 12.77 ?  113 TYR   A CE1  1 
ATOM   2465 C  CE2  . TYR   A 1 113 ? 19.916 -10.461 -1.318  1.00 12.21 ?  113 TYR   A CE2  1 
ATOM   2466 C  CZ   . TYR   A 1 113 ? 19.571 -9.846  -0.136  1.00 12.37 ?  113 TYR   A CZ   1 
ATOM   2467 O  OH   . TYR   A 1 113 ? 18.447 -9.044  -0.049  1.00 13.18 ?  113 TYR   A OH   1 
ATOM   2468 H  H    . TYR   A 1 113 ? 24.506 -11.257 -1.947  1.00 13.75 ?  113 TYR   A H    1 
ATOM   2469 H  HA   . TYR   A 1 113 ? 24.206 -10.923 0.633   1.00 13.64 ?  113 TYR   A HA   1 
ATOM   2470 H  HB2  . TYR   A 1 113 ? 23.111 -12.754 -1.160  1.00 14.00 ?  113 TYR   A HB2  1 
ATOM   2471 H  HB3  . TYR   A 1 113 ? 22.951 -13.050 0.390   1.00 14.00 ?  113 TYR   A HB3  1 
ATOM   2472 H  HD1  . TYR   A 1 113 ? 21.981 -10.945 1.709   1.00 14.59 ?  113 TYR   A HD1  1 
ATOM   2473 H  HD2  . TYR   A 1 113 ? 21.294 -11.691 -2.156  1.00 13.89 ?  113 TYR   A HD2  1 
ATOM   2474 H  HE1  . TYR   A 1 113 ? 20.111 -9.611  1.790   1.00 15.35 ?  113 TYR   A HE1  1 
ATOM   2475 H  HE2  . TYR   A 1 113 ? 19.393 -10.337 -2.076  1.00 14.67 ?  113 TYR   A HE2  1 
ATOM   2476 H  HH   . TYR   A 1 113 ? 18.064 -9.020  -0.800  1.00 15.83 ?  113 TYR   A HH   1 
ATOM   2477 N  N    . GLU   A 1 114 ? 26.292 -13.184 -0.123  1.00 11.20 ?  114 GLU   A N    1 
ATOM   2478 C  CA   . GLU   A 1 114 ? 27.280 -14.078 0.478   1.00 11.90 ?  114 GLU   A CA   1 
ATOM   2479 C  C    . GLU   A 1 114 ? 28.125 -13.365 1.528   1.00 11.87 ?  114 GLU   A C    1 
ATOM   2480 O  O    . GLU   A 1 114 ? 28.606 -14.002 2.474   1.00 12.21 ?  114 GLU   A O    1 
ATOM   2481 C  CB   . GLU   A 1 114 ? 28.154 -14.728 -0.603  1.00 11.91 ?  114 GLU   A CB   1 
ATOM   2482 C  CG   . GLU   A 1 114 ? 27.413 -15.779 -1.390  1.00 12.54 ?  114 GLU   A CG   1 
ATOM   2483 C  CD   . GLU   A 1 114 ? 28.131 -16.302 -2.628  1.00 12.85 ?  114 GLU   A CD   1 
ATOM   2484 O  OE1  . GLU   A 1 114 ? 29.094 -15.673 -3.115  1.00 13.12 ?  114 GLU   A OE1  1 
ATOM   2485 O  OE2  . GLU   A 1 114 ? 27.693 -17.356 -3.137  1.00 14.27 -1 114 GLU   A OE2  1 
ATOM   2486 H  H    . GLU   A 1 114 ? 26.354 -13.092 -0.978  1.00 13.46 ?  114 GLU   A H    1 
ATOM   2487 H  HA   . GLU   A 1 114 ? 26.808 -14.791 0.928   1.00 14.30 ?  114 GLU   A HA   1 
ATOM   2488 H  HB2  . GLU   A 1 114 ? 28.453 -14.039 -1.225  1.00 14.31 ?  114 GLU   A HB2  1 
ATOM   2489 H  HB3  . GLU   A 1 114 ? 28.921 -15.145 -0.184  1.00 14.31 ?  114 GLU   A HB3  1 
ATOM   2490 H  HG2  . GLU   A 1 114 ? 27.253 -16.539 -0.810  1.00 15.07 ?  114 GLU   A HG2  1 
ATOM   2491 H  HG3  . GLU   A 1 114 ? 26.562 -15.407 -1.677  1.00 15.07 ?  114 GLU   A HG3  1 
ATOM   2492 N  N    . ASN   A 1 115 ? 28.311 -12.049 1.391   1.00 11.45 ?  115 ASN   A N    1 
ATOM   2493 C  CA   . ASN   A 1 115 ? 29.071 -11.311 2.395   1.00 11.65 ?  115 ASN   A CA   1 
ATOM   2494 C  C    . ASN   A 1 115 ? 28.446 -11.437 3.782   1.00 11.50 ?  115 ASN   A C    1 
ATOM   2495 O  O    . ASN   A 1 115 ? 29.150 -11.361 4.792   1.00 12.02 ?  115 ASN   A O    1 
ATOM   2496 C  CB   . ASN   A 1 115 ? 29.185 -9.834  2.008   1.00 12.02 ?  115 ASN   A CB   1 
ATOM   2497 C  CG   . ASN   A 1 115 ? 29.984 -9.625  0.744   1.00 12.71 ?  115 ASN   A CG   1 
ATOM   2498 O  OD1  . ASN   A 1 115 ? 31.202 -9.739  0.764   1.00 15.77 ?  115 ASN   A OD1  1 
ATOM   2499 N  ND2  . ASN   A 1 115 ? 29.314 -9.324  -0.354  1.00 12.15 ?  115 ASN   A ND2  1 
ATOM   2500 H  H    . ASN   A 1 115 ? 28.005 -11.568 0.747   1.00 13.76 ?  115 ASN   A H    1 
ATOM   2501 H  HA   . ASN   A 1 115 ? 29.964 -11.679 2.444   1.00 14.00 ?  115 ASN   A HA   1 
ATOM   2502 H  HB2  . ASN   A 1 115 ? 28.292 -9.476  1.875   1.00 14.45 ?  115 ASN   A HB2  1 
ATOM   2503 H  HB3  . ASN   A 1 115 ? 29.627 -9.357  2.729   1.00 14.45 ?  115 ASN   A HB3  1 
ATOM   2504 H  HD21 . ASN   A 1 115 ? 29.733 -9.204  -1.096  1.00 14.60 ?  115 ASN   A HD21 1 
ATOM   2505 H  HD22 . ASN   A 1 115 ? 28.454 -9.271  -0.335  1.00 14.60 ?  115 ASN   A HD22 1 
ATOM   2506 N  N    . PHE   A 1 116 ? 27.118 -11.603 3.855   1.00 11.51 ?  116 PHE   A N    1 
ATOM   2507 C  CA   . PHE   A 1 116 ? 26.459 -11.701 5.157   1.00 11.55 ?  116 PHE   A CA   1 
ATOM   2508 C  C    . PHE   A 1 116 ? 26.930 -12.930 5.933   1.00 11.93 ?  116 PHE   A C    1 
ATOM   2509 O  O    . PHE   A 1 116 ? 26.854 -12.953 7.165   1.00 12.34 ?  116 PHE   A O    1 
ATOM   2510 C  CB   . PHE   A 1 116 ? 24.930 -11.830 5.014   1.00 12.07 ?  116 PHE   A CB   1 
ATOM   2511 C  CG   . PHE   A 1 116 ? 24.175 -10.584 4.538   1.00 11.39 ?  116 PHE   A CG   1 
ATOM   2512 C  CD1  . PHE   A 1 116 ? 24.746 -9.570  3.782   1.00 11.74 ?  116 PHE   A CD1  1 
ATOM   2513 C  CD2  . PHE   A 1 116 ? 22.817 -10.479 4.849   1.00 12.22 ?  116 PHE   A CD2  1 
ATOM   2514 C  CE1  . PHE   A 1 116 ? 23.977 -8.496  3.352   1.00 12.07 ?  116 PHE   A CE1  1 
ATOM   2515 C  CE2  . PHE   A 1 116 ? 22.054 -9.405  4.431   1.00 12.29 ?  116 PHE   A CE2  1 
ATOM   2516 C  CZ   . PHE   A 1 116 ? 22.626 -8.421  3.676   1.00 11.58 ?  116 PHE   A CZ   1 
ATOM   2517 H  H    . PHE   A 1 116 ? 26.586 -11.655 3.178   1.00 13.84 ?  116 PHE   A H    1 
ATOM   2518 H  HA   . PHE   A 1 116 ? 26.650 -10.908 5.681   1.00 13.88 ?  116 PHE   A HA   1 
ATOM   2519 H  HB2  . PHE   A 1 116 ? 24.741 -12.540 4.381   1.00 14.51 ?  116 PHE   A HB2  1 
ATOM   2520 H  HB3  . PHE   A 1 116 ? 24.564 -12.075 5.883   1.00 14.51 ?  116 PHE   A HB3  1 
ATOM   2521 H  HD1  . PHE   A 1 116 ? 25.641 -9.632  3.549   1.00 14.11 ?  116 PHE   A HD1  1 
ATOM   2522 H  HD2  . PHE   A 1 116 ? 22.412 -11.156 5.356   1.00 14.69 ?  116 PHE   A HD2  1 
ATOM   2523 H  HE1  . PHE   A 1 116 ? 24.375 -7.826  2.847   1.00 14.50 ?  116 PHE   A HE1  1 
ATOM   2524 H  HE2  . PHE   A 1 116 ? 21.150 -9.360  4.660   1.00 14.76 ?  116 PHE   A HE2  1 
ATOM   2525 H  HZ   . PHE   A 1 116 ? 22.121 -7.689  3.405   1.00 13.92 ?  116 PHE   A HZ   1 
ATOM   2526 N  N    . ASN   A 1 117 ? 27.376 -13.976 5.233   1.00 11.98 ?  117 ASN   A N    1 
ATOM   2527 C  CA   . ASN   A 1 117 ? 27.739 -15.219 5.906   1.00 12.72 ?  117 ASN   A CA   1 
ATOM   2528 C  C    . ASN   A 1 117 ? 28.996 -15.106 6.748   1.00 13.06 ?  117 ASN   A C    1 
ATOM   2529 O  O    . ASN   A 1 117 ? 29.284 -16.027 7.518   1.00 13.81 ?  117 ASN   A O    1 
ATOM   2530 C  CB   . ASN   A 1 117 ? 27.864 -16.353 4.895   1.00 12.56 ?  117 ASN   A CB   1 
ATOM   2531 C  CG   . ASN   A 1 117 ? 26.524 -16.735 4.340   1.00 12.80 ?  117 ASN   A CG   1 
ATOM   2532 O  OD1  . ASN   A 1 117 ? 25.534 -16.756 5.072   1.00 13.41 ?  117 ASN   A OD1  1 
ATOM   2533 N  ND2  . ASN   A 1 117 ? 26.462 -17.003 3.055   1.00 12.24 ?  117 ASN   A ND2  1 
ATOM   2534 H  H    . ASN   A 1 117 ? 27.455 -13.993 4.376   1.00 14.40 ?  117 ASN   A H    1 
ATOM   2535 H  HA   . ASN   A 1 117 ? 27.014 -15.451 6.510   1.00 15.28 ?  117 ASN   A HA   1 
ATOM   2536 H  HB2  . ASN   A 1 117 ? 28.427 -16.064 4.161   1.00 15.09 ?  117 ASN   A HB2  1 
ATOM   2537 H  HB3  . ASN   A 1 117 ? 28.248 -17.126 5.334   1.00 15.09 ?  117 ASN   A HB3  1 
ATOM   2538 H  HD21 . ASN   A 1 117 ? 25.716 -17.219 2.703   1.00 14.71 ?  117 ASN   A HD21 1 
ATOM   2539 H  HD22 . ASN   A 1 117 ? 27.179 -16.965 2.581   1.00 14.71 ?  117 ASN   A HD22 1 
ATOM   2540 N  N    . GLN   A 1 118 ? 29.732 -14.001 6.639   1.00 12.92 ?  118 GLN   A N    1 
ATOM   2541 C  CA   . GLN   A 1 118 ? 30.904 -13.769 7.472   1.00 13.54 ?  118 GLN   A CA   1 
ATOM   2542 C  C    . GLN   A 1 118 ? 30.553 -13.200 8.839   1.00 13.57 ?  118 GLN   A C    1 
ATOM   2543 O  O    . GLN   A 1 118 ? 31.464 -12.925 9.626   1.00 14.86 ?  118 GLN   A O    1 
ATOM   2544 C  CB   . GLN   A 1 118 ? 31.899 -12.857 6.743   1.00 13.67 ?  118 GLN   A CB   1 
ATOM   2545 C  CG   . GLN   A 1 118 ? 32.377 -13.437 5.419   1.00 13.62 ?  118 GLN   A CG   1 
ATOM   2546 C  CD   . GLN   A 1 118 ? 33.225 -14.685 5.595   1.00 14.25 ?  118 GLN   A CD   1 
ATOM   2547 O  OE1  . GLN   A 1 118 ? 34.081 -14.747 6.486   1.00 14.87 ?  118 GLN   A OE1  1 
ATOM   2548 N  NE2  . GLN   A 1 118 ? 32.987 -15.688 4.747   1.00 14.22 ?  118 GLN   A NE2  1 
ATOM   2549 H  H    . GLN   A 1 118 ? 29.565 -13.351 6.089   1.00 15.53 ?  118 GLN   A H    1 
ATOM   2550 H  HA   . GLN   A 1 118 ? 31.338 -14.622 7.620   1.00 16.27 ?  118 GLN   A HA   1 
ATOM   2551 H  HB2  . GLN   A 1 118 ? 31.473 -12.006 6.567   1.00 16.43 ?  118 GLN   A HB2  1 
ATOM   2552 H  HB3  . GLN   A 1 118 ? 32.675 -12.728 7.313   1.00 16.43 ?  118 GLN   A HB3  1 
ATOM   2553 H  HG2  . GLN   A 1 118 ? 31.605 -13.674 4.876   1.00 16.37 ?  118 GLN   A HG2  1 
ATOM   2554 H  HG3  . GLN   A 1 118 ? 32.912 -12.775 4.957   1.00 16.37 ?  118 GLN   A HG3  1 
ATOM   2555 H  HE21 . GLN   A 1 118 ? 32.375 -15.609 4.142   1.00 17.08 ?  118 GLN   A HE21 1 
ATOM   2556 H  HE22 . GLN   A 1 118 ? 33.437 -16.419 4.802   1.00 17.08 ?  118 GLN   A HE22 1 
ATOM   2557 N  N    . HIS   A 1 119 ? 29.262 -13.035 9.142   1.00 13.12 ?  119 HIS   A N    1 
ATOM   2558 C  CA   . HIS   A 1 119 ? 28.798 -12.423 10.381  1.00 13.41 ?  119 HIS   A CA   1 
ATOM   2559 C  C    . HIS   A 1 119 ? 27.654 -13.240 10.954  1.00 14.02 ?  119 HIS   A C    1 
ATOM   2560 O  O    . HIS   A 1 119 ? 26.710 -13.583 10.236  1.00 14.22 ?  119 HIS   A O    1 
ATOM   2561 C  CB   . HIS   A 1 119 ? 28.341 -10.993 10.101  1.00 13.85 ?  119 HIS   A CB   1 
ATOM   2562 C  CG   . HIS   A 1 119 ? 29.419 -10.186 9.481   1.00 14.86 ?  119 HIS   A CG   1 
ATOM   2563 N  ND1  . HIS   A 1 119 ? 30.390 -9.564  10.232  1.00 17.03 ?  119 HIS   A ND1  1 
ATOM   2564 C  CD2  . HIS   A 1 119 ? 29.757 -9.999  8.186   1.00 15.83 ?  119 HIS   A CD2  1 
ATOM   2565 C  CE1  . HIS   A 1 119 ? 31.258 -8.987  9.421   1.00 17.44 ?  119 HIS   A CE1  1 
ATOM   2566 N  NE2  . HIS   A 1 119 ? 30.908 -9.251  8.175   1.00 17.21 ?  119 HIS   A NE2  1 
ATOM   2567 H  H    . HIS   A 1 119 ? 28.612 -13.288 8.628   1.00 15.77 ?  119 HIS   A H    1 
ATOM   2568 H  HA   . HIS   A 1 119 ? 29.521 -12.403 11.024  1.00 16.12 ?  119 HIS   A HA   1 
ATOM   2569 H  HB2  . HIS   A 1 119 ? 27.586 -11.015 9.492   1.00 16.64 ?  119 HIS   A HB2  1 
ATOM   2570 H  HB3  . HIS   A 1 119 ? 28.088 -10.573 10.936  1.00 16.64 ?  119 HIS   A HB3  1 
ATOM   2571 H  HD2  . HIS   A 1 119 ? 29.306 -10.326 7.440   1.00 19.02 ?  119 HIS   A HD2  1 
ATOM   2572 H  HE1  . HIS   A 1 119 ? 31.993 -8.478  9.681   1.00 20.95 ?  119 HIS   A HE1  1 
ATOM   2573 H  HE2  . HIS   A 1 119 ? 31.313 -8.961  7.469   1.00 20.67 ?  119 HIS   A HE2  1 
ATOM   2574 N  N    A GLU   A 1 120 ? 27.746 -13.566 12.245  0.56 14.59 ?  120 GLU   A N    1 
ATOM   2575 N  N    B GLU   A 1 120 ? 27.727 -13.510 12.261  0.44 15.53 ?  120 GLU   A N    1 
ATOM   2576 C  CA   A GLU   A 1 120 ? 26.788 -14.501 12.834  0.56 16.01 ?  120 GLU   A CA   1 
ATOM   2577 C  CA   B GLU   A 1 120 ? 26.771 -14.416 12.893  0.44 17.45 ?  120 GLU   A CA   1 
ATOM   2578 C  C    A GLU   A 1 120 ? 25.373 -13.935 12.895  0.56 14.68 ?  120 GLU   A C    1 
ATOM   2579 C  C    B GLU   A 1 120 ? 25.360 -13.838 12.924  0.44 16.72 ?  120 GLU   A C    1 
ATOM   2580 O  O    A GLU   A 1 120 ? 24.403 -14.701 12.793  0.56 14.55 ?  120 GLU   A O    1 
ATOM   2581 O  O    B GLU   A 1 120 ? 24.384 -14.577 12.743  0.44 17.27 ?  120 GLU   A O    1 
ATOM   2582 C  CB   A GLU   A 1 120 ? 27.244 -14.920 14.231  0.56 19.88 ?  120 GLU   A CB   1 
ATOM   2583 C  CB   B GLU   A 1 120 ? 27.235 -14.773 14.307  0.44 20.87 ?  120 GLU   A CB   1 
ATOM   2584 C  CG   A GLU   A 1 120 ? 28.452 -15.842 14.235  0.56 24.89 ?  120 GLU   A CG   1 
ATOM   2585 C  CG   B GLU   A 1 120 ? 28.407 -15.739 14.349  0.44 25.09 ?  120 GLU   A CG   1 
ATOM   2586 C  CD   A GLU   A 1 120 ? 28.661 -16.534 15.567  0.56 28.95 ?  120 GLU   A CD   1 
ATOM   2587 C  CD   B GLU   A 1 120 ? 28.447 -16.538 15.637  0.44 28.56 ?  120 GLU   A CD   1 
ATOM   2588 O  OE1  A GLU   A 1 120 ? 28.238 -15.972 16.601  0.56 30.73 ?  120 GLU   A OE1  1 
ATOM   2589 O  OE1  B GLU   A 1 120 ? 28.067 -15.983 16.692  0.44 29.81 ?  120 GLU   A OE1  1 
ATOM   2590 O  OE2  A GLU   A 1 120 ? 29.247 -17.638 15.578  0.56 31.10 -1 120 GLU   A OE2  1 
ATOM   2591 O  OE2  B GLU   A 1 120 ? 28.841 -17.723 15.593  0.44 30.55 -1 120 GLU   A OE2  1 
ATOM   2592 H  H    A GLU   A 1 120 ? 28.346 -13.272 12.790  0.56 17.53 ?  120 GLU   A H    1 
ATOM   2593 H  H    B GLU   A 1 120 ? 28.321 -13.186 12.796  0.44 18.66 ?  120 GLU   A H    1 
ATOM   2594 H  HA   A GLU   A 1 120 ? 26.765 -15.301 12.288  0.56 19.23 ?  120 GLU   A HA   1 
ATOM   2595 H  HA   B GLU   A 1 120 ? 26.739 -15.236 12.383  0.44 20.97 ?  120 GLU   A HA   1 
ATOM   2596 H  HB2  A GLU   A 1 120 ? 27.475 -14.129 14.740  0.56 23.88 ?  120 GLU   A HB2  1 
ATOM   2597 H  HB2  B GLU   A 1 120 ? 27.507 -13.964 14.767  0.44 25.07 ?  120 GLU   A HB2  1 
ATOM   2598 H  HB3  A GLU   A 1 120 ? 26.513 -15.389 14.671  0.56 23.88 ?  120 GLU   A HB3  1 
ATOM   2599 H  HB3  B GLU   A 1 120 ? 26.498 -15.189 14.784  0.44 25.07 ?  120 GLU   A HB3  1 
ATOM   2600 H  HG2  A GLU   A 1 120 ? 28.339 -16.514 13.544  0.56 29.89 ?  120 GLU   A HG2  1 
ATOM   2601 H  HG2  B GLU   A 1 120 ? 28.335 -16.360 13.608  0.44 30.14 ?  120 GLU   A HG2  1 
ATOM   2602 H  HG3  A GLU   A 1 120 ? 29.248 -15.320 14.067  0.56 29.89 ?  120 GLU   A HG3  1 
ATOM   2603 H  HG3  B GLU   A 1 120 ? 29.235 -15.237 14.283  0.44 30.14 ?  120 GLU   A HG3  1 
ATOM   2604 N  N    A VAL   A 1 121 ? 25.236 -12.622 13.093  0.56 13.74 ?  121 VAL   A N    1 
ATOM   2605 N  N    B VAL   A 1 121 ? 25.224 -12.534 13.170  0.44 15.68 ?  121 VAL   A N    1 
ATOM   2606 C  CA   A VAL   A 1 121 ? 23.943 -11.948 13.188  0.56 14.24 ?  121 VAL   A CA   1 
ATOM   2607 C  CA   B VAL   A 1 121 ? 23.917 -11.887 13.273  0.44 15.49 ?  121 VAL   A CA   1 
ATOM   2608 C  C    A VAL   A 1 121 ? 24.068 -10.582 12.520  0.56 13.34 ?  121 VAL   A C    1 
ATOM   2609 C  C    B VAL   A 1 121 ? 24.006 -10.509 12.634  0.44 13.76 ?  121 VAL   A C    1 
ATOM   2610 O  O    A VAL   A 1 121 ? 25.074 -9.888  12.699  0.56 14.14 ?  121 VAL   A O    1 
ATOM   2611 O  O    B VAL   A 1 121 ? 24.927 -9.743  12.937  0.44 13.30 ?  121 VAL   A O    1 
ATOM   2612 C  CB   A VAL   A 1 121 ? 23.501 -11.767 14.659  0.56 17.23 ?  121 VAL   A CB   1 
ATOM   2613 C  CB   B VAL   A 1 121 ? 23.434 -11.758 14.734  0.44 18.08 ?  121 VAL   A CB   1 
ATOM   2614 C  CG1  A VAL   A 1 121 ? 22.101 -11.170 14.731  0.56 17.61 ?  121 VAL   A CG1  1 
ATOM   2615 C  CG1  B VAL   A 1 121 ? 22.061 -11.100 14.780  0.44 18.60 ?  121 VAL   A CG1  1 
ATOM   2616 C  CG2  A VAL   A 1 121 ? 23.554 -13.074 15.427  0.56 18.93 ?  121 VAL   A CG2  1 
ATOM   2617 C  CG2  B VAL   A 1 121 ? 23.388 -13.109 15.421  0.44 19.42 ?  121 VAL   A CG2  1 
ATOM   2618 H  H    A VAL   A 1 121 ? 25.903 -12.090 13.190  0.56 16.51 ?  121 VAL   A H    1 
ATOM   2619 H  H    B VAL   A 1 121 ? 25.887 -11.991 13.275  0.44 18.83 ?  121 VAL   A H    1 
ATOM   2620 H  HA   A VAL   A 1 121 ? 23.270 -12.474 12.726  0.56 17.11 ?  121 VAL   A HA   1 
ATOM   2621 H  HA   B VAL   A 1 121 ? 23.266 -12.404 12.783  0.44 18.61 ?  121 VAL   A HA   1 
ATOM   2622 H  HB   A VAL   A 1 121 ? 24.108 -11.148 15.092  0.56 20.70 ?  121 VAL   A HB   1 
ATOM   2623 H  HB   B VAL   A 1 121 ? 24.051 -11.192 15.224  0.44 21.72 ?  121 VAL   A HB   1 
ATOM   2624 H  HG11 A VAL   A 1 121 ? 21.805 -11.167 15.657  0.56 21.16 ?  121 VAL   A HG11 1 
ATOM   2625 H  HG11 B VAL   A 1 121 ? 21.690 -11.206 15.671  0.44 22.34 ?  121 VAL   A HG11 1 
ATOM   2626 H  HG12 A VAL   A 1 121 ? 22.123 -10.262 14.392  0.56 21.16 ?  121 VAL   A HG12 1 
ATOM   2627 H  HG12 B VAL   A 1 121 ? 22.149 -10.158 14.570  0.44 22.34 ?  121 VAL   A HG12 1 
ATOM   2628 H  HG13 A VAL   A 1 121 ? 21.498 -11.711 14.197  0.56 21.16 ?  121 VAL   A HG13 1 
ATOM   2629 H  HG13 B VAL   A 1 121 ? 21.482 -11.533 14.131  0.44 22.34 ?  121 VAL   A HG13 1 
ATOM   2630 H  HG21 A VAL   A 1 121 ? 23.195 -12.930 16.322  0.56 22.74 ?  121 VAL   A HG21 1 
ATOM   2631 H  HG21 B VAL   A 1 121 ? 23.027 -12.995 16.317  0.44 23.32 ?  121 VAL   A HG21 1 
ATOM   2632 H  HG22 A VAL   A 1 121 ? 23.017 -13.737 14.964  0.56 22.74 ?  121 VAL   A HG22 1 
ATOM   2633 H  HG22 B VAL   A 1 121 ? 22.817 -13.704 14.911  0.44 23.32 ?  121 VAL   A HG22 1 
ATOM   2634 H  HG23 A VAL   A 1 121 ? 24.472 -13.373 15.488  0.56 22.74 ?  121 VAL   A HG23 1 
ATOM   2635 H  HG23 B VAL   A 1 121 ? 24.285 -13.470 15.471  0.44 23.32 ?  121 VAL   A HG23 1 
ATOM   2636 N  N    . LEU   A 1 122 ? 23.038 -10.179 11.776  1.00 12.99 ?  122 LEU   A N    1 
ATOM   2637 C  CA   . LEU   A 1 122 ? 23.031 -8.885  11.100  1.00 12.67 ?  122 LEU   A CA   1 
ATOM   2638 C  C    . LEU   A 1 122 ? 21.636 -8.289  11.063  1.00 12.50 ?  122 LEU   A C    1 
ATOM   2639 O  O    . LEU   A 1 122 ? 20.645 -9.007  10.915  1.00 13.68 ?  122 LEU   A O    1 
ATOM   2640 C  CB   . LEU   A 1 122 ? 23.456 -8.993  9.629   1.00 13.82 ?  122 LEU   A CB   1 
ATOM   2641 C  CG   . LEU   A 1 122 ? 24.679 -9.828  9.283   1.00 14.01 ?  122 LEU   A CG   1 
ATOM   2642 C  CD1  . LEU   A 1 122 ? 24.292 -11.277 9.053   1.00 14.85 ?  122 LEU   A CD1  1 
ATOM   2643 C  CD2  . LEU   A 1 122 ? 25.397 -9.262  8.066   1.00 13.13 ?  122 LEU   A CD2  1 
ATOM   2644 H  H    A LEU   A 1 122 ? 22.320 -10.639 11.654  0.56 15.62 ?  122 LEU   A H    1 
ATOM   2645 H  H    B LEU   A 1 122 ? 22.377 -10.692 11.570  0.44 15.62 ?  122 LEU   A H    1 
ATOM   2646 H  HA   . LEU   A 1 122 ? 23.629 -8.269  11.550  1.00 15.23 ?  122 LEU   A HA   1 
ATOM   2647 H  HB2  . LEU   A 1 122 ? 22.723 -9.377  9.130   1.00 16.61 ?  122 LEU   A HB2  1 
ATOM   2648 H  HB3  . LEU   A 1 122 ? 23.640 -8.105  9.301   1.00 16.61 ?  122 LEU   A HB3  1 
ATOM   2649 H  HG   . LEU   A 1 122 ? 25.312 -9.810  10.020  1.00 16.83 ?  122 LEU   A HG   1 
ATOM   2650 H  HD11 . LEU   A 1 122 ? 25.079 -11.791 8.809   1.00 17.85 ?  122 LEU   A HD11 1 
ATOM   2651 H  HD12 . LEU   A 1 122 ? 23.910 -11.635 9.871   1.00 17.85 ?  122 LEU   A HD12 1 
ATOM   2652 H  HD13 . LEU   A 1 122 ? 23.637 -11.322 8.338   1.00 17.85 ?  122 LEU   A HD13 1 
ATOM   2653 H  HD21 . LEU   A 1 122 ? 26.159 -9.828  7.842   1.00 15.78 ?  122 LEU   A HD21 1 
ATOM   2654 H  HD22 . LEU   A 1 122 ? 24.783 -9.235  7.316   1.00 15.78 ?  122 LEU   A HD22 1 
ATOM   2655 H  HD23 . LEU   A 1 122 ? 25.710 -8.366  8.269   1.00 15.78 ?  122 LEU   A HD23 1 
ATOM   2656 N  N    A LEU   A 1 123 ? 21.576 -6.963  11.167  0.56 12.27 ?  123 LEU   A N    1 
ATOM   2657 N  N    B LEU   A 1 123 ? 21.580 -6.964  11.204  0.44 12.35 ?  123 LEU   A N    1 
ATOM   2658 C  CA   A LEU   A 1 123 ? 20.415 -6.177  10.758  0.56 11.59 ?  123 LEU   A CA   1 
ATOM   2659 C  CA   B LEU   A 1 123 ? 20.408 -6.160  10.881  0.44 11.83 ?  123 LEU   A CA   1 
ATOM   2660 C  C    A LEU   A 1 123 ? 20.677 -5.676  9.346   0.56 11.40 ?  123 LEU   A C    1 
ATOM   2661 C  C    B LEU   A 1 123 ? 20.632 -5.592  9.488   0.44 10.88 ?  123 LEU   A C    1 
ATOM   2662 O  O    A LEU   A 1 123 ? 21.774 -5.185  9.065   0.56 11.38 ?  123 LEU   A O    1 
ATOM   2663 O  O    B LEU   A 1 123 ? 21.602 -4.857  9.276   0.44 10.73 ?  123 LEU   A O    1 
ATOM   2664 C  CB   A LEU   A 1 123 ? 20.243 -4.983  11.696  0.56 12.24 ?  123 LEU   A CB   1 
ATOM   2665 C  CB   B LEU   A 1 123 ? 20.273 -5.016  11.886  0.44 12.69 ?  123 LEU   A CB   1 
ATOM   2666 C  CG   A LEU   A 1 123 ? 19.199 -3.922  11.341  0.56 13.16 ?  123 LEU   A CG   1 
ATOM   2667 C  CG   B LEU   A 1 123 ? 19.242 -3.940  11.539  0.44 13.21 ?  123 LEU   A CG   1 
ATOM   2668 C  CD1  A LEU   A 1 123 ? 17.793 -4.508  11.348  0.56 13.91 ?  123 LEU   A CD1  1 
ATOM   2669 C  CD1  B LEU   A 1 123 ? 17.827 -4.518  11.502  0.44 14.13 ?  123 LEU   A CD1  1 
ATOM   2670 C  CD2  A LEU   A 1 123 ? 19.301 -2.745  12.306  0.56 13.54 ?  123 LEU   A CD2  1 
ATOM   2671 C  CD2  B LEU   A 1 123 ? 19.336 -2.789  12.525  0.44 13.88 ?  123 LEU   A CD2  1 
ATOM   2672 H  H    A LEU   A 1 123 ? 22.217 -6.485  11.493  0.56 14.75 ?  123 LEU   A H    1 
ATOM   2673 H  H    B LEU   A 1 123 ? 22.239 -6.491  11.496  0.44 14.84 ?  123 LEU   A H    1 
ATOM   2674 H  HA   A LEU   A 1 123 ? 19.619 -6.730  10.765  0.56 13.93 ?  123 LEU   A HA   1 
ATOM   2675 H  HA   B LEU   A 1 123 ? 19.605 -6.697  10.888  0.44 14.21 ?  123 LEU   A HA   1 
ATOM   2676 H  HB2  A LEU   A 1 123 ? 20.003 -5.328  12.567  0.56 14.71 ?  123 LEU   A HB2  1 
ATOM   2677 H  HB2  B LEU   A 1 123 ? 20.020 -5.389  12.745  0.44 15.25 ?  123 LEU   A HB2  1 
ATOM   2678 H  HB3  A LEU   A 1 123 ? 21.094 -4.530  11.754  0.56 14.71 ?  123 LEU   A HB3  1 
ATOM   2679 H  HB3  B LEU   A 1 123 ? 21.133 -4.572  11.970  0.44 15.25 ?  123 LEU   A HB3  1 
ATOM   2680 H  HG   A LEU   A 1 123 ? 19.377 -3.582  10.448  0.56 15.82 ?  123 LEU   A HG   1 
ATOM   2681 H  HG   B LEU   A 1 123 ? 19.436 -3.580  10.658  0.44 15.88 ?  123 LEU   A HG   1 
ATOM   2682 H  HD11 A LEU   A 1 123 ? 17.156 -3.810  11.132  0.56 16.72 ?  123 LEU   A HD11 1 
ATOM   2683 H  HD11 B LEU   A 1 123 ? 17.196 -3.806  11.312  0.44 16.98 ?  123 LEU   A HD11 1 
ATOM   2684 H  HD12 A LEU   A 1 123 ? 17.745 -5.217  10.687  0.56 16.72 ?  123 LEU   A HD12 1 
ATOM   2685 H  HD12 B LEU   A 1 123 ? 17.778 -5.195  10.806  0.44 16.98 ?  123 LEU   A HD12 1 
ATOM   2686 H  HD13 A LEU   A 1 123 ? 17.606 -4.866  12.230  0.56 16.72 ?  123 LEU   A HD13 1 
ATOM   2687 H  HD13 B LEU   A 1 123 ? 17.625 -4.917  12.363  0.44 16.98 ?  123 LEU   A HD13 1 
ATOM   2688 H  HD21 A LEU   A 1 123 ? 18.633 -2.083  12.070  0.56 16.27 ?  123 LEU   A HD21 1 
ATOM   2689 H  HD21 B LEU   A 1 123 ? 18.676 -2.119  12.291  0.44 16.68 ?  123 LEU   A HD21 1 
ATOM   2690 H  HD22 A LEU   A 1 123 ? 19.141 -3.067  13.209  0.56 16.27 ?  123 LEU   A HD22 1 
ATOM   2691 H  HD22 B LEU   A 1 123 ? 19.164 -3.128  13.417  0.44 16.68 ?  123 LEU   A HD22 1 
ATOM   2692 H  HD23 A LEU   A 1 123 ? 20.188 -2.361  12.245  0.56 16.27 ?  123 LEU   A HD23 1 
ATOM   2693 H  HD23 B LEU   A 1 123 ? 20.227 -2.410  12.480  0.44 16.68 ?  123 LEU   A HD23 1 
ATOM   2694 N  N    A ALA   A 1 124 ? 19.684 -5.780  8.459   0.56 10.92 ?  124 ALA   A N    1 
ATOM   2695 N  N    B ALA   A 1 124 ? 19.761 -5.923  8.540   0.44 10.78 ?  124 ALA   A N    1 
ATOM   2696 C  CA   A ALA   A 1 124 ? 19.985 -5.549  7.053   0.56 10.55 ?  124 ALA   A CA   1 
ATOM   2697 C  CA   B ALA   A 1 124 ? 20.022 -5.587  7.150   0.44 10.70 ?  124 ALA   A CA   1 
ATOM   2698 C  C    A ALA   A 1 124 ? 18.750 -5.121  6.275   0.56 10.32 ?  124 ALA   A C    1 
ATOM   2699 C  C    B ALA   A 1 124 ? 18.783 -5.068  6.441   0.44 11.40 ?  124 ALA   A C    1 
ATOM   2700 O  O    A ALA   A 1 124 ? 17.626 -5.517  6.612   0.56 10.49 ?  124 ALA   A O    1 
ATOM   2701 O  O    B ALA   A 1 124 ? 17.651 -5.333  6.864   0.44 12.01 ?  124 ALA   A O    1 
ATOM   2702 C  CB   A ALA   A 1 124 ? 20.582 -6.806  6.413   0.56 11.40 ?  124 ALA   A CB   1 
ATOM   2703 C  CB   B ALA   A 1 124 ? 20.551 -6.798  6.371   0.44 10.93 ?  124 ALA   A CB   1 
ATOM   2704 H  H    A ALA   A 1 124 ? 18.868 -5.958  8.646   0.56 13.13 ?  124 ALA   A H    1 
ATOM   2705 H  H    B ALA   A 1 124 ? 19.018 -6.339  8.672   0.44 12.96 ?  124 ALA   A H    1 
ATOM   2706 H  HA   A ALA   A 1 124 ? 20.651 -4.848  7.000   0.56 12.68 ?  124 ALA   A HA   1 
ATOM   2707 H  HA   B ALA   A 1 124 ? 20.700 -4.897  7.117   0.44 12.87 ?  124 ALA   A HA   1 
ATOM   2708 H  HB1  A ALA   A 1 124 ? 20.777 -6.626  5.481   0.56 13.70 ?  124 ALA   A HB1  1 
ATOM   2709 H  HB1  B ALA   A 1 124 ? 20.718 -6.541  5.449   0.44 13.14 ?  124 ALA   A HB1  1 
ATOM   2710 H  HB2  A ALA   A 1 124 ? 21.407 -7.040  6.879   0.56 13.70 ?  124 ALA   A HB2  1 
ATOM   2711 H  HB2  B ALA   A 1 124 ? 21.383 -7.097  6.781   0.44 13.14 ?  124 ALA   A HB2  1 
ATOM   2712 H  HB3  A ALA   A 1 124 ? 19.949 -7.534  6.488   0.56 13.70 ?  124 ALA   A HB3  1 
ATOM   2713 H  HB3  B ALA   A 1 124 ? 19.896 -7.510  6.403   0.44 13.14 ?  124 ALA   A HB3  1 
ATOM   2714 N  N    A PRO   A 1 125 ? 18.938 -4.365  5.200   0.56 10.62 ?  125 PRO   A N    1 
ATOM   2715 N  N    B PRO   A 1 125 ? 18.971 -4.338  5.346   0.44 11.33 ?  125 PRO   A N    1 
ATOM   2716 C  CA   A PRO   A 1 125 ? 17.874 -4.119  4.230   0.56 10.77 ?  125 PRO   A CA   1 
ATOM   2717 C  CA   B PRO   A 1 125 ? 17.886 -4.075  4.404   0.44 11.62 ?  125 PRO   A CA   1 
ATOM   2718 C  C    A PRO   A 1 125 ? 17.921 -5.199  3.156   0.56 10.82 ?  125 PRO   A C    1 
ATOM   2719 C  C    B PRO   A 1 125 ? 17.922 -5.134  3.307   0.44 11.58 ?  125 PRO   A C    1 
ATOM   2720 O  O    A PRO   A 1 125 ? 18.874 -5.973  3.063   0.56 11.58 ?  125 PRO   A O    1 
ATOM   2721 O  O    B PRO   A 1 125 ? 18.879 -5.901  3.183   0.44 11.96 ?  125 PRO   A O    1 
ATOM   2722 C  CB   A PRO   A 1 125 ? 18.321 -2.784  3.626   0.56 10.90 ?  125 PRO   A CB   1 
ATOM   2723 C  CB   B PRO   A 1 125 ? 18.298 -2.714  3.828   0.44 12.09 ?  125 PRO   A CB   1 
ATOM   2724 C  CG   A PRO   A 1 125 ? 19.825 -2.955  3.540   0.56 11.13 ?  125 PRO   A CG   1 
ATOM   2725 C  CG   B PRO   A 1 125 ? 19.799 -2.835  3.723   0.44 12.39 ?  125 PRO   A CG   1 
ATOM   2726 C  CD   A PRO   A 1 125 ? 20.205 -3.732  4.786   0.56 11.14 ?  125 PRO   A CD   1 
ATOM   2727 C  CD   B PRO   A 1 125 ? 20.230 -3.704  4.899   0.44 12.39 ?  125 PRO   A CD   1 
ATOM   2728 H  HA   A PRO   A 1 125 ? 16.994 -4.059  4.647   0.56 12.94 ?  125 PRO   A HA   1 
ATOM   2729 H  HA   B PRO   A 1 125 ? 17.019 -4.025  4.834   0.44 13.97 ?  125 PRO   A HA   1 
ATOM   2730 H  HB2  A PRO   A 1 125 ? 17.923 -2.670  2.750   0.56 13.10 ?  125 PRO   A HB2  1 
ATOM   2731 H  HB2  B PRO   A 1 125 ? 17.896 -2.577  2.953   0.44 14.53 ?  125 PRO   A HB2  1 
ATOM   2732 H  HB3  A PRO   A 1 125 ? 18.078 -2.056  4.221   0.56 13.10 ?  125 PRO   A HB3  1 
ATOM   2733 H  HB3  B PRO   A 1 125 ? 18.048 -1.997  4.438   0.44 14.53 ?  125 PRO   A HB3  1 
ATOM   2734 H  HG2  A PRO   A 1 125 ? 20.057 -3.459  2.742   0.56 13.37 ?  125 PRO   A HG2  1 
ATOM   2735 H  HG2  B PRO   A 1 125 ? 20.033 -3.258  2.880   0.44 14.89 ?  125 PRO   A HG2  1 
ATOM   2736 H  HG3  A PRO   A 1 125 ? 20.257 -2.086  3.534   0.56 13.37 ?  125 PRO   A HG3  1 
ATOM   2737 H  HG3  B PRO   A 1 125 ? 20.205 -1.953  3.780   0.44 14.89 ?  125 PRO   A HG3  1 
ATOM   2738 H  HD2  A PRO   A 1 125 ? 20.871 -4.406  4.586   0.56 13.39 ?  125 PRO   A HD2  1 
ATOM   2739 H  HD2  B PRO   A 1 125 ? 20.869 -4.371  4.602   0.44 14.88 ?  125 PRO   A HD2  1 
ATOM   2740 H  HD3  A PRO   A 1 125 ? 20.513 -3.127  5.484   0.56 13.39 ?  125 PRO   A HD3  1 
ATOM   2741 H  HD3  B PRO   A 1 125 ? 20.600 -3.148  5.603   0.44 14.88 ?  125 PRO   A HD3  1 
ATOM   2742 N  N    A LEU   A 1 126 ? 16.892 -5.212  2.315   0.56 11.38 ?  126 LEU   A N    1 
ATOM   2743 N  N    B LEU   A 1 126 ? 16.868 -5.154  2.495   0.44 12.12 ?  126 LEU   A N    1 
ATOM   2744 C  CA   A LEU   A 1 126 ? 16.934 -6.043  1.119   0.56 11.62 ?  126 LEU   A CA   1 
ATOM   2745 C  CA   B LEU   A 1 126 ? 16.937 -5.896  1.244   0.44 12.20 ?  126 LEU   A CA   1 
ATOM   2746 C  C    A LEU   A 1 126 ? 17.871 -5.427  0.089   0.56 11.63 ?  126 LEU   A C    1 
ATOM   2747 C  C    B LEU   A 1 126 ? 17.917 -5.201  0.307   0.44 11.64 ?  126 LEU   A C    1 
ATOM   2748 O  O    A LEU   A 1 126 ? 17.634 -4.319  -0.407  0.56 11.53 ?  126 LEU   A O    1 
ATOM   2749 O  O    B LEU   A 1 126 ? 17.993 -3.972  0.277   0.44 12.27 ?  126 LEU   A O    1 
ATOM   2750 C  CB   A LEU   A 1 126 ? 15.539 -6.223  0.538   0.56 12.54 ?  126 LEU   A CB   1 
ATOM   2751 C  CB   B LEU   A 1 126 ? 15.564 -5.963  0.579   0.44 13.57 ?  126 LEU   A CB   1 
ATOM   2752 C  CG   A LEU   A 1 126 ? 14.667 -7.170  1.357   0.56 13.47 ?  126 LEU   A CG   1 
ATOM   2753 C  CG   B LEU   A 1 126 ? 14.548 -6.991  1.081   0.44 14.57 ?  126 LEU   A CG   1 
ATOM   2754 C  CD1  A LEU   A 1 126 ? 13.227 -7.042  0.918   0.56 14.32 ?  126 LEU   A CD1  1 
ATOM   2755 C  CD1  B LEU   A 1 126 ? 13.254 -6.853  0.292   0.44 15.09 ?  126 LEU   A CD1  1 
ATOM   2756 C  CD2  A LEU   A 1 126 ? 15.148 -8.616  1.224   0.56 13.48 ?  126 LEU   A CD2  1 
ATOM   2757 C  CD2  B LEU   A 1 126 ? 15.074 -8.416  0.977   0.44 15.16 ?  126 LEU   A CD2  1 
ATOM   2758 H  H    A LEU   A 1 126 ? 16.171 -4.750  2.408   0.56 13.67 ?  126 LEU   A H    1 
ATOM   2759 H  H    B LEU   A 1 126 ? 16.121 -4.742  2.635   0.44 14.57 ?  126 LEU   A H    1 
ATOM   2760 H  HA   A LEU   A 1 126 ? 17.280 -6.913  1.349   0.56 13.97 ?  126 LEU   A HA   1 
ATOM   2761 H  HA   B LEU   A 1 126 ? 17.250 -6.793  1.416   0.44 14.66 ?  126 LEU   A HA   1 
ATOM   2762 H  HB2  A LEU   A 1 126 ? 15.092 -5.362  0.507   0.56 15.07 ?  126 LEU   A HB2  1 
ATOM   2763 H  HB2  B LEU   A 1 126 ? 15.144 -5.093  0.675   0.44 16.31 ?  126 LEU   A HB2  1 
ATOM   2764 H  HB3  A LEU   A 1 126 ? 15.612 -6.588  -0.359  0.56 15.07 ?  126 LEU   A HB3  1 
ATOM   2765 H  HB3  B LEU   A 1 126 ? 15.699 -6.145  -0.362  0.44 16.31 ?  126 LEU   A HB3  1 
ATOM   2766 H  HG   A LEU   A 1 126 ? 14.719 -6.923  2.293   0.56 16.19 ?  126 LEU   A HG   1 
ATOM   2767 H  HG   B LEU   A 1 126 ? 14.348 -6.813  2.012   0.44 17.50 ?  126 LEU   A HG   1 
ATOM   2768 H  HD11 A LEU   A 1 126 ? 12.682 -7.654  1.438   0.56 17.20 ?  126 LEU   A HD11 1 
ATOM   2769 H  HD11 B LEU   A 1 126 ? 12.614 -7.509  0.614   0.44 18.12 ?  126 LEU   A HD11 1 
ATOM   2770 H  HD12 A LEU   A 1 126 ? 12.933 -6.130  1.066   0.56 17.20 ?  126 LEU   A HD12 1 
ATOM   2771 H  HD12 B LEU   A 1 126 ? 12.901 -5.959  0.414   0.44 18.12 ?  126 LEU   A HD12 1 
ATOM   2772 H  HD13 A LEU   A 1 126 ? 13.164 -7.263  -0.025  0.56 17.20 ?  126 LEU   A HD13 1 
ATOM   2773 H  HD13 B LEU   A 1 126 ? 13.439 -7.011  -0.649  0.44 18.12 ?  126 LEU   A HD13 1 
ATOM   2774 H  HD21 A LEU   A 1 126 ? 14.489 -9.206  1.621   0.56 16.20 ?  126 LEU   A HD21 1 
ATOM   2775 H  HD21 B LEU   A 1 126 ? 14.359 -9.035  1.191   0.44 18.21 ?  126 LEU   A HD21 1 
ATOM   2776 H  HD22 A LEU   A 1 126 ? 15.256 -8.827  0.283   0.56 16.20 ?  126 LEU   A HD22 1 
ATOM   2777 H  HD22 B LEU   A 1 126 ? 15.387 -8.573  0.072   0.44 18.21 ?  126 LEU   A HD22 1 
ATOM   2778 H  HD23 A LEU   A 1 126 ? 15.997 -8.711  1.684   0.56 16.20 ?  126 LEU   A HD23 1 
ATOM   2779 H  HD23 B LEU   A 1 126 ? 15.807 -8.529  1.603   0.44 18.21 ?  126 LEU   A HD23 1 
ATOM   2780 N  N    A LEU   A 1 127 ? 18.933 -6.158  -0.239  0.56 11.47 ?  127 LEU   A N    1 
ATOM   2781 N  N    B LEU   A 1 127 ? 18.676 -5.986  -0.458  0.44 11.62 ?  127 LEU   A N    1 
ATOM   2782 C  CA   A LEU   A 1 127 ? 19.916 -5.668  -1.189  0.56 11.31 ?  127 LEU   A CA   1 
ATOM   2783 C  CA   B LEU   A 1 127 ? 19.682 -5.436  -1.357  0.44 11.62 ?  127 LEU   A CA   1 
ATOM   2784 C  C    A LEU   A 1 127 ? 19.278 -5.444  -2.550  0.56 10.92 ?  127 LEU   A C    1 
ATOM   2785 C  C    B LEU   A 1 127 ? 19.179 -5.383  -2.800  0.44 11.82 ?  127 LEU   A C    1 
ATOM   2786 O  O    A LEU   A 1 127 ? 18.429 -6.219  -3.000  0.56 11.47 ?  127 LEU   A O    1 
ATOM   2787 O  O    B LEU   A 1 127 ? 18.384 -6.217  -3.243  0.44 11.36 ?  127 LEU   A O    1 
ATOM   2788 C  CB   A LEU   A 1 127 ? 21.069 -6.665  -1.310  0.56 12.16 ?  127 LEU   A CB   1 
ATOM   2789 C  CB   B LEU   A 1 127 ? 20.994 -6.234  -1.292  0.44 12.49 ?  127 LEU   A CB   1 
ATOM   2790 C  CG   A LEU   A 1 127 ? 21.866 -6.895  -0.027  0.56 12.10 ?  127 LEU   A CG   1 
ATOM   2791 C  CG   B LEU   A 1 127 ? 21.780 -6.224  0.030   0.44 13.64 ?  127 LEU   A CG   1 
ATOM   2792 C  CD1  A LEU   A 1 127 ? 22.960 -7.900  -0.295  0.56 12.67 ?  127 LEU   A CD1  1 
ATOM   2793 C  CD1  B LEU   A 1 127 ? 23.000 -7.148  -0.031  0.44 14.44 ?  127 LEU   A CD1  1 
ATOM   2794 C  CD2  A LEU   A 1 127 ? 22.473 -5.601  0.480   0.56 13.24 ?  127 LEU   A CD2  1 
ATOM   2795 C  CD2  B LEU   A 1 127 ? 22.205 -4.805  0.414   0.44 14.31 ?  127 LEU   A CD2  1 
ATOM   2796 H  H    A LEU   A 1 127 ? 19.097 -6.941  0.069   0.56 13.79 ?  127 LEU   A H    1 
ATOM   2797 H  H    B LEU   A 1 127 ? 18.628 -6.847  -0.460  0.44 13.97 ?  127 LEU   A H    1 
ATOM   2798 H  HA   A LEU   A 1 127 ? 20.270 -4.826  -0.884  0.56 13.60 ?  127 LEU   A HA   1 
ATOM   2799 H  HA   B LEU   A 1 127 ? 19.880 -4.530  -1.074  0.44 13.96 ?  127 LEU   A HA   1 
ATOM   2800 H  HB2  A LEU   A 1 127 ? 20.709 -7.523  -1.587  0.56 14.62 ?  127 LEU   A HB2  1 
ATOM   2801 H  HB2  B LEU   A 1 127 ? 20.793 -7.160  -1.491  0.44 15.01 ?  127 LEU   A HB2  1 
ATOM   2802 H  HB3  A LEU   A 1 127 ? 21.688 -6.341  -1.981  0.56 14.62 ?  127 LEU   A HB3  1 
ATOM   2803 H  HB3  B LEU   A 1 127 ? 21.588 -5.883  -1.973  0.44 15.01 ?  127 LEU   A HB3  1 
ATOM   2804 H  HG   A LEU   A 1 127 ? 21.282 -7.256  0.661   0.56 14.54 ?  127 LEU   A HG   1 
ATOM   2805 H  HG   B LEU   A 1 127 ? 21.205 -6.555  0.735   0.44 16.38 ?  127 LEU   A HG   1 
ATOM   2806 H  HD11 A LEU   A 1 127 ? 23.428 -8.087  0.534   0.56 15.23 ?  127 LEU   A HD11 1 
ATOM   2807 H  HD11 B LEU   A 1 127 ? 23.468 -7.113  0.821   0.44 17.36 ?  127 LEU   A HD11 1 
ATOM   2808 H  HD12 A LEU   A 1 127 ? 22.565 -8.714  -0.644  0.56 15.23 ?  127 LEU   A HD12 1 
ATOM   2809 H  HD12 B LEU   A 1 127 ? 22.702 -8.055  -0.204  0.44 17.36 ?  127 LEU   A HD12 1 
ATOM   2810 H  HD13 A LEU   A 1 127 ? 23.576 -7.526  -0.945  0.56 15.23 ?  127 LEU   A HD13 1 
ATOM   2811 H  HD13 B LEU   A 1 127 ? 23.589 -6.851  -0.741  0.44 17.36 ?  127 LEU   A HD13 1 
ATOM   2812 H  HD21 A LEU   A 1 127 ? 23.099 -5.804  1.192   0.56 15.91 ?  127 LEU   A HD21 1 
ATOM   2813 H  HD21 B LEU   A 1 127 ? 22.772 -4.846  1.201   0.44 17.20 ?  127 LEU   A HD21 1 
ATOM   2814 H  HD22 A LEU   A 1 127 ? 22.938 -5.166  -0.254  0.56 15.91 ?  127 LEU   A HD22 1 
ATOM   2815 H  HD22 B LEU   A 1 127 ? 22.695 -4.411  -0.326  0.44 17.20 ?  127 LEU   A HD22 1 
ATOM   2816 H  HD23 A LEU   A 1 127 ? 21.766 -5.028  0.810   0.56 15.91 ?  127 LEU   A HD23 1 
ATOM   2817 H  HD23 B LEU   A 1 127 ? 21.413 -4.280  0.604   0.44 17.20 ?  127 LEU   A HD23 1 
ATOM   2818 N  N    A SER   A 1 128 ? 19.715 -4.376  -3.209  0.56 10.99 ?  128 SER   A N    1 
ATOM   2819 N  N    B SER   A 1 128 ? 19.666 -4.377  -3.528  0.44 11.87 ?  128 SER   A N    1 
ATOM   2820 C  CA   A SER   A 1 128 ? 19.309 -3.980  -4.552  0.56 10.73 ?  128 SER   A CA   1 
ATOM   2821 C  CA   B SER   A 1 128 ? 19.449 -4.191  -4.962  0.44 12.11 ?  128 SER   A CA   1 
ATOM   2822 C  C    A SER   A 1 128 ? 17.850 -3.550  -4.643  0.56 11.02 ?  128 SER   A C    1 
ATOM   2823 C  C    B SER   A 1 128 ? 18.049 -3.726  -5.349  0.44 12.26 ?  128 SER   A C    1 
ATOM   2824 O  O    A SER   A 1 128 ? 17.367 -3.286  -5.748  0.56 11.60 ?  128 SER   A O    1 
ATOM   2825 O  O    B SER   A 1 128 ? 17.820 -3.375  -6.511  0.44 13.25 ?  128 SER   A O    1 
ATOM   2826 C  CB   A SER   A 1 128 ? 19.658 -5.027  -5.616  0.56 10.83 ?  128 SER   A CB   1 
ATOM   2827 C  CB   B SER   A 1 128 ? 19.853 -5.429  -5.768  0.44 12.50 ?  128 SER   A CB   1 
ATOM   2828 O  OG   A SER   A 1 128 ? 21.065 -5.203  -5.696  0.56 11.59 ?  128 SER   A OG   1 
ATOM   2829 O  OG   B SER   A 1 128 ? 21.259 -5.591  -5.775  0.44 12.09 ?  128 SER   A OG   1 
ATOM   2830 H  H    A SER   A 1 128 ? 20.289 -3.830  -2.872  0.56 13.21 ?  128 SER   A H    1 
ATOM   2831 H  H    B SER   A 1 128 ? 20.168 -3.769  -3.189  0.44 14.27 ?  128 SER   A H    1 
ATOM   2832 H  HA   A SER   A 1 128 ? 19.830 -3.202  -4.777  0.56 12.90 ?  128 SER   A HA   1 
ATOM   2833 H  HA   B SER   A 1 128 ? 20.039 -3.484  -5.239  0.44 14.55 ?  128 SER   A HA   1 
ATOM   2834 H  HB2  A SER   A 1 128 ? 19.247 -5.873  -5.384  0.56 13.02 ?  128 SER   A HB2  1 
ATOM   2835 H  HB2  B SER   A 1 128 ? 19.443 -6.215  -5.380  0.44 15.02 ?  128 SER   A HB2  1 
ATOM   2836 H  HB3  A SER   A 1 128 ? 19.337 -4.724  -6.480  0.56 13.02 ?  128 SER   A HB3  1 
ATOM   2837 H  HB3  B SER   A 1 128 ? 19.554 -5.313  -6.684  0.44 15.02 ?  128 SER   A HB3  1 
ATOM   2838 H  HG   A SER   A 1 128 ? 21.440 -4.469  -5.878  0.56 13.93 ?  128 SER   A HG   1 
ATOM   2839 H  HG   B SER   A 1 128 ? 21.620 -4.898  -6.090  0.44 14.53 ?  128 SER   A HG   1 
ATOM   2840 N  N    A ALA   A 1 129 ? 17.141 -3.464  -3.519  0.56 10.90 ?  129 ALA   A N    1 
ATOM   2841 N  N    B ALA   A 1 129 ? 17.114 -3.698  -4.406  0.44 12.63 ?  129 ALA   A N    1 
ATOM   2842 C  CA   A ALA   A 1 129 ? 15.778 -2.960  -3.520  0.56 11.20 ?  129 ALA   A CA   1 
ATOM   2843 C  CA   B ALA   A 1 129 ? 15.776 -3.197  -4.696  0.44 13.43 ?  129 ALA   A CA   1 
ATOM   2844 C  C    A ALA   A 1 129 ? 15.792 -1.430  -3.526  0.56 11.17 ?  129 ALA   A C    1 
ATOM   2845 C  C    B ALA   A 1 129 ? 15.726 -1.694  -4.399  0.44 13.37 ?  129 ALA   A C    1 
ATOM   2846 O  O    A ALA   A 1 129 ? 16.841 -0.784  -3.609  0.56 11.65 ?  129 ALA   A O    1 
ATOM   2847 O  O    B ALA   A 1 129 ? 16.761 -1.019  -4.391  0.44 13.20 ?  129 ALA   A O    1 
ATOM   2848 C  CB   A ALA   A 1 129 ? 15.002 -3.529  -2.330  0.56 12.14 ?  129 ALA   A CB   1 
ATOM   2849 C  CB   B ALA   A 1 129 ? 14.723 -4.069  -3.995  0.44 15.09 ?  129 ALA   A CB   1 
ATOM   2850 H  H    A ALA   A 1 129 ? 17.429 -3.702  -2.743  0.56 13.10 ?  129 ALA   A H    1 
ATOM   2851 H  H    B ALA   A 1 129 ? 17.221 -3.974  -3.593  0.44 15.18 ?  129 ALA   A H    1 
ATOM   2852 H  HA   A ALA   A 1 129 ? 15.334 -3.253  -4.325  0.56 13.46 ?  129 ALA   A HA   1 
ATOM   2853 H  HA   B ALA   A 1 129 ? 15.616 -3.293  -5.643  0.44 16.14 ?  129 ALA   A HA   1 
ATOM   2854 H  HB1  A ALA   A 1 129 ? 14.094 -3.186  -2.349  0.56 14.59 ?  129 ALA   A HB1  1 
ATOM   2855 H  HB1  B ALA   A 1 129 ? 13.838 -3.726  -4.197  0.44 18.13 ?  129 ALA   A HB1  1 
ATOM   2856 H  HB2  A ALA   A 1 129 ? 14.988 -4.498  -2.393  0.56 14.59 ?  129 ALA   A HB2  1 
ATOM   2857 H  HB2  B ALA   A 1 129 ? 14.801 -4.984  -4.321  0.44 18.13 ?  129 ALA   A HB2  1 
ATOM   2858 H  HB3  A ALA   A 1 129 ? 15.437 -3.260  -1.504  0.56 14.59 ?  129 ALA   A HB3  1 
ATOM   2859 H  HB3  B ALA   A 1 129 ? 14.875 -4.051  -3.038  0.44 18.13 ?  129 ALA   A HB3  1 
ATOM   2860 N  N    A GLY   A 1 130 ? 14.606 -0.842  -3.455  0.56 12.22 ?  130 GLY   A N    1 
ATOM   2861 N  N    B GLY   A 1 130 ? 14.533 -1.150  -4.171  0.44 13.46 ?  130 GLY   A N    1 
ATOM   2862 C  CA   A GLY   A 1 130 ? 14.524 0.609   -3.429  0.56 13.08 ?  130 GLY   A CA   1 
ATOM   2863 C  CA   B GLY   A 1 130 ? 14.421 0.285   -3.970  0.44 14.21 ?  130 GLY   A CA   1 
ATOM   2864 C  C    A GLY   A 1 130 ? 15.129 1.210   -4.681  0.56 12.88 ?  130 GLY   A C    1 
ATOM   2865 C  C    B GLY   A 1 130 ? 15.036 1.045   -5.125  0.44 14.37 ?  130 GLY   A C    1 
ATOM   2866 O  O    A GLY   A 1 130 ? 14.853 0.768   -5.801  0.56 12.59 ?  130 GLY   A O    1 
ATOM   2867 O  O    B GLY   A 1 130 ? 14.871 0.679   -6.296  0.44 14.69 ?  130 GLY   A O    1 
ATOM   2868 H  H    A GLY   A 1 130 ? 13.847 -1.254  -3.429  0.56 14.69 ?  130 GLY   A H    1 
ATOM   2869 H  H    B GLY   A 1 130 ? 13.786 -1.579  -4.133  0.44 16.17 ?  130 GLY   A H    1 
ATOM   2870 H  HA2  A GLY   A 1 130 ? 13.593 0.880   -3.361  0.56 15.72 ?  130 GLY   A HA2  1 
ATOM   2871 H  HA2  B GLY   A 1 130 ? 13.483 0.534   -3.891  0.44 17.07 ?  130 GLY   A HA2  1 
ATOM   2872 H  HA3  A GLY   A 1 130 ? 15.004 0.948   -2.662  0.56 15.72 ?  130 GLY   A HA3  1 
ATOM   2873 H  HA3  B GLY   A 1 130 ? 14.875 0.540   -3.152  0.44 17.07 ?  130 GLY   A HA3  1 
ATOM   2874 N  N    A ILE   A 1 131 ? 15.976 2.230   -4.492  0.56 13.11 ?  131 ILE   A N    1 
ATOM   2875 N  N    B ILE   A 1 131 ? 15.766 2.116   -4.802  0.44 14.57 ?  131 ILE   A N    1 
ATOM   2876 C  CA   A ILE   A 1 131 ? 16.531 2.982   -5.614  0.56 13.29 ?  131 ILE   A CA   1 
ATOM   2877 C  CA   B ILE   A 1 131 ? 16.369 2.965   -5.827  0.44 14.41 ?  131 ILE   A CA   1 
ATOM   2878 C  C    A ILE   A 1 131 ? 17.527 2.187   -6.442  0.56 13.38 ?  131 ILE   A C    1 
ATOM   2879 C  C    B ILE   A 1 131 ? 17.479 2.260   -6.608  0.44 13.99 ?  131 ILE   A C    1 
ATOM   2880 O  O    A ILE   A 1 131 ? 17.913 2.655   -7.518  0.56 14.36 ?  131 ILE   A O    1 
ATOM   2881 O  O    B ILE   A 1 131 ? 18.014 2.830   -7.566  0.44 13.92 ?  131 ILE   A O    1 
ATOM   2882 C  CB   A ILE   A 1 131 ? 17.151 4.329   -5.180  0.56 14.32 ?  131 ILE   A CB   1 
ATOM   2883 C  CB   B ILE   A 1 131 ? 16.839 4.323   -5.266  0.44 14.75 ?  131 ILE   A CB   1 
ATOM   2884 C  CG1  A ILE   A 1 131 ? 18.450 4.116   -4.392  0.56 15.48 ?  131 ILE   A CG1  1 
ATOM   2885 C  CG1  B ILE   A 1 131 ? 17.944 4.144   -4.221  0.44 16.26 ?  131 ILE   A CG1  1 
ATOM   2886 C  CG2  A ILE   A 1 131 ? 16.150 5.133   -4.365  0.56 14.58 ?  131 ILE   A CG2  1 
ATOM   2887 C  CG2  B ILE   A 1 131 ? 15.655 5.096   -4.690  0.44 13.60 ?  131 ILE   A CG2  1 
ATOM   2888 C  CD1  A ILE   A 1 131 ? 19.112 5.420   -3.944  0.56 16.48 ?  131 ILE   A CD1  1 
ATOM   2889 C  CD1  B ILE   A 1 131 ? 18.539 5.460   -3.747  0.44 17.40 ?  131 ILE   A CD1  1 
ATOM   2890 H  H    A ILE   A 1 131 ? 16.234 2.500   -3.724  0.56 15.76 ?  131 ILE   A H    1 
ATOM   2891 H  H    B ILE   A 1 131 ? 15.896 2.392   -3.993  0.44 17.51 ?  131 ILE   A H    1 
ATOM   2892 H  HA   A ILE   A 1 131 ? 15.804 3.195   -6.217  0.56 15.97 ?  131 ILE   A HA   1 
ATOM   2893 H  HA   B ILE   A 1 131 ? 15.679 3.164   -6.469  0.44 17.32 ?  131 ILE   A HA   1 
ATOM   2894 H  HB   A ILE   A 1 131 ? 17.360 4.835   -5.980  0.56 17.20 ?  131 ILE   A HB   1 
ATOM   2895 H  HB   B ILE   A 1 131 ? 17.205 4.835   -6.003  0.44 17.73 ?  131 ILE   A HB   1 
ATOM   2896 H  HG12 A ILE   A 1 131 ? 18.254 3.590   -3.602  0.56 18.60 ?  131 ILE   A HG12 1 
ATOM   2897 H  HG12 B ILE   A 1 131 ? 17.575 3.687   -3.448  0.44 19.53 ?  131 ILE   A HG12 1 
ATOM   2898 H  HG13 A ILE   A 1 131 ? 19.088 3.645   -4.952  0.56 18.60 ?  131 ILE   A HG13 1 
ATOM   2899 H  HG13 B ILE   A 1 131 ? 18.662 3.614   -4.604  0.44 19.53 ?  131 ILE   A HG13 1 
ATOM   2900 H  HG21 A ILE   A 1 131 ? 16.475 6.040   -4.274  0.56 17.51 ?  131 ILE   A HG21 1 
ATOM   2901 H  HG21 B ILE   A 1 131 ? 15.937 5.998   -4.482  0.44 16.34 ?  131 ILE   A HG21 1 
ATOM   2902 H  HG22 A ILE   A 1 131 ? 15.297 5.127   -4.823  0.56 17.51 ?  131 ILE   A HG22 1 
ATOM   2903 H  HG22 B ILE   A 1 131 ? 14.942 5.114   -5.348  0.44 16.34 ?  131 ILE   A HG22 1 
ATOM   2904 H  HG23 A ILE   A 1 131 ? 16.058 4.721   -3.490  0.56 17.51 ?  131 ILE   A HG23 1 
ATOM   2905 H  HG23 B ILE   A 1 131 ? 15.348 4.648   -3.885  0.44 16.34 ?  131 ILE   A HG23 1 
ATOM   2906 H  HD11 A ILE   A 1 131 ? 19.990 5.221   -3.585  0.56 19.80 ?  131 ILE   A HD11 1 
ATOM   2907 H  HD11 B ILE   A 1 131 ? 19.307 5.275   -3.186  0.44 20.90 ?  131 ILE   A HD11 1 
ATOM   2908 H  HD12 A ILE   A 1 131 ? 19.193 6.013   -4.708  0.56 19.80 ?  131 ILE   A HD12 1 
ATOM   2909 H  HD12 B ILE   A 1 131 ? 18.811 5.978   -4.521  0.44 20.90 ?  131 ILE   A HD12 1 
ATOM   2910 H  HD13 A ILE   A 1 131 ? 18.561 5.837   -3.261  0.56 19.80 ?  131 ILE   A HD13 1 
ATOM   2911 H  HD13 B ILE   A 1 131 ? 17.868 5.947   -3.243  0.44 20.90 ?  131 ILE   A HD13 1 
ATOM   2912 N  N    A PHE   A 1 132 ? 17.960 1.005   -5.978  0.56 12.93 ?  132 PHE   A N    1 
ATOM   2913 N  N    B PHE   A 1 132 ? 17.832 1.021   -6.225  0.44 14.27 ?  132 PHE   A N    1 
ATOM   2914 C  CA   A PHE   A 1 132 ? 18.809 0.141   -6.795  0.56 13.16 ?  132 PHE   A CA   1 
ATOM   2915 C  CA   B PHE   A 1 132 ? 18.799 0.247   -7.004  0.44 14.91 ?  132 PHE   A CA   1 
ATOM   2916 C  C    A PHE   A 1 132 ? 18.021 -0.619  -7.867  0.56 13.18 ?  132 PHE   A C    1 
ATOM   2917 C  C    B PHE   A 1 132 ? 18.164 -0.480  -8.190  0.44 15.44 ?  132 PHE   A C    1 
ATOM   2918 O  O    A PHE   A 1 132 ? 18.633 -1.282  -8.713  0.56 13.49 ?  132 PHE   A O    1 
ATOM   2919 O  O    B PHE   A 1 132 ? 18.892 -0.923  -9.086  0.44 16.02 ?  132 PHE   A O    1 
ATOM   2920 C  CB   A PHE   A 1 132 ? 19.614 -0.842  -5.924  0.56 12.83 ?  132 PHE   A CB   1 
ATOM   2921 C  CB   B PHE   A 1 132 ? 19.555 -0.751  -6.113  0.44 14.19 ?  132 PHE   A CB   1 
ATOM   2922 C  CG   A PHE   A 1 132 ? 20.837 -0.243  -5.244  0.56 12.47 ?  132 PHE   A CG   1 
ATOM   2923 C  CG   B PHE   A 1 132 ? 20.725 -0.156  -5.355  0.44 13.97 ?  132 PHE   A CG   1 
ATOM   2924 C  CD1  A PHE   A 1 132 ? 20.719 0.796   -4.334  0.56 13.09 ?  132 PHE   A CD1  1 
ATOM   2925 C  CD1  B PHE   A 1 132 ? 20.543 0.862   -4.430  0.44 14.23 ?  132 PHE   A CD1  1 
ATOM   2926 C  CD2  A PHE   A 1 132 ? 22.099 -0.773  -5.483  0.56 13.21 ?  132 PHE   A CD2  1 
ATOM   2927 C  CD2  B PHE   A 1 132 ? 22.005 -0.656  -5.545  0.44 14.45 ?  132 PHE   A CD2  1 
ATOM   2928 C  CE1  A PHE   A 1 132 ? 21.838 1.318   -3.704  0.56 13.65 ?  132 PHE   A CE1  1 
ATOM   2929 C  CE1  B PHE   A 1 132 ? 21.623 1.388   -3.731  0.44 14.60 ?  132 PHE   A CE1  1 
ATOM   2930 C  CE2  A PHE   A 1 132 ? 23.222 -0.257  -4.852  0.56 13.94 ?  132 PHE   A CE2  1 
ATOM   2931 C  CE2  B PHE   A 1 132 ? 23.085 -0.139  -4.849  0.44 14.96 ?  132 PHE   A CE2  1 
ATOM   2932 C  CZ   A PHE   A 1 132 ? 23.089 0.792   -3.960  0.56 13.85 ?  132 PHE   A CZ   1 
ATOM   2933 C  CZ   B PHE   A 1 132 ? 22.893 0.884   -3.940  0.44 14.85 ?  132 PHE   A CZ   1 
ATOM   2934 H  H    A PHE   A 1 132 ? 17.777 0.690   -5.197  0.56 15.54 ?  132 PHE   A H    1 
ATOM   2935 H  H    B PHE   A 1 132 ? 17.546 0.609   -5.523  0.44 17.14 ?  132 PHE   A H    1 
ATOM   2936 H  HA   A PHE   A 1 132 ? 19.456 0.702   -7.250  0.56 15.82 ?  132 PHE   A HA   1 
ATOM   2937 H  HA   B PHE   A 1 132 ? 19.457 0.856   -7.366  0.44 17.91 ?  132 PHE   A HA   1 
ATOM   2938 H  HB2  A PHE   A 1 132 ? 19.037 -1.184  -5.227  0.56 15.42 ?  132 PHE   A HB2  1 
ATOM   2939 H  HB2  B PHE   A 1 132 ? 18.945 -1.115  -5.459  0.44 17.06 ?  132 PHE   A HB2  1 
ATOM   2940 H  HB3  A PHE   A 1 132 ? 19.919 -1.579  -6.484  0.56 15.42 ?  132 PHE   A HB3  1 
ATOM   2941 H  HB3  B PHE   A 1 132 ? 19.906 -1.468  -6.669  0.44 17.06 ?  132 PHE   A HB3  1 
ATOM   2942 H  HD1  A PHE   A 1 132 ? 19.884 1.151   -4.155  0.56 15.73 ?  132 PHE   A HD1  1 
ATOM   2943 H  HD1  B PHE   A 1 132 ? 19.694 1.207   -4.284  0.44 17.10 ?  132 PHE   A HD1  1 
ATOM   2944 H  HD2  A PHE   A 1 132 ? 22.204 -1.481  -6.083  0.56 15.88 ?  132 PHE   A HD2  1 
ATOM   2945 H  HD2  B PHE   A 1 132 ? 22.146 -1.344  -6.157  0.44 17.37 ?  132 PHE   A HD2  1 
ATOM   2946 H  HE1  A PHE   A 1 132 ? 21.746 2.021   -3.102  0.56 16.40 ?  132 PHE   A HE1  1 
ATOM   2947 H  HE1  B PHE   A 1 132 ? 21.496 2.076   -3.116  0.44 17.54 ?  132 PHE   A HE1  1 
ATOM   2948 H  HE2  A PHE   A 1 132 ? 24.069 -0.611  -5.030  0.56 16.75 ?  132 PHE   A HE2  1 
ATOM   2949 H  HE2  B PHE   A 1 132 ? 23.941 -0.480  -4.995  0.44 17.98 ?  132 PHE   A HE2  1 
ATOM   2950 H  HZ   A PHE   A 1 132 ? 23.840 1.146   -3.536  0.56 16.64 ?  132 PHE   A HZ   1 
ATOM   2951 H  HZ   B PHE   A 1 132 ? 23.619 1.233   -3.472  0.44 17.84 ?  132 PHE   A HZ   1 
ATOM   2952 N  N    A GLY   A 1 133 ? 16.687 -0.552  -7.846  0.56 13.30 ?  133 GLY   A N    1 
ATOM   2953 N  N    B GLY   A 1 133 ? 16.837 -0.633  -8.216  0.44 15.05 ?  133 GLY   A N    1 
ATOM   2954 C  CA   A GLY   A 1 133 ? 15.879 -0.930  -8.993  0.56 13.90 ?  133 GLY   A CA   1 
ATOM   2955 C  CA   B GLY   A 1 133 ? 16.115 -0.981  -9.423  0.44 14.97 ?  133 GLY   A CA   1 
ATOM   2956 C  C    A GLY   A 1 133 ? 15.609 -2.404  -9.209  0.56 14.57 ?  133 GLY   A C    1 
ATOM   2957 C  C    B GLY   A 1 133 ? 15.574 -2.396  -9.504  0.44 15.14 ?  133 GLY   A C    1 
ATOM   2958 O  O    A GLY   A 1 133 ? 15.050 -2.752  -10.255 0.56 15.70 ?  133 GLY   A O    1 
ATOM   2959 O  O    B GLY   A 1 133 ? 14.669 -2.639  -10.313 0.44 15.81 ?  133 GLY   A O    1 
ATOM   2960 H  H    A GLY   A 1 133 ? 16.223 -0.282  -7.172  0.56 15.99 ?  133 GLY   A H    1 
ATOM   2961 H  H    B GLY   A 1 133 ? 16.333 -0.538  -7.527  0.44 18.08 ?  133 GLY   A H    1 
ATOM   2962 H  HA2  A GLY   A 1 133 ? 15.018 -0.486  -8.921  0.56 16.70 ?  133 GLY   A HA2  1 
ATOM   2963 H  HA2  B GLY   A 1 133 ? 15.360 -0.384  -9.510  0.44 17.98 ?  133 GLY   A HA2  1 
ATOM   2964 H  HA3  A GLY   A 1 133 ? 16.310 -0.600  -9.795  0.56 16.70 ?  133 GLY   A HA3  1 
ATOM   2965 H  HA3  B GLY   A 1 133 ? 16.696 -0.840  -10.187 0.44 17.98 ?  133 GLY   A HA3  1 
ATOM   2966 N  N    A ALA   A 1 134 ? 15.980 -3.282  -8.280  0.56 14.03 ?  134 ALA   A N    1 
ATOM   2967 N  N    B ALA   A 1 134 ? 16.081 -3.335  -8.706  0.44 14.86 ?  134 ALA   A N    1 
ATOM   2968 C  CA   A ALA   A 1 134 ? 15.632 -4.691  -8.413  0.56 13.74 ?  134 ALA   A CA   1 
ATOM   2969 C  CA   B ALA   A 1 134 ? 15.726 -4.734  -8.917  0.44 14.29 ?  134 ALA   A CA   1 
ATOM   2970 C  C    A ALA   A 1 134 ? 14.270 -4.967  -7.780  0.56 13.77 ?  134 ALA   A C    1 
ATOM   2971 C  C    B ALA   A 1 134 ? 14.383 -5.078  -8.267  0.44 14.17 ?  134 ALA   A C    1 
ATOM   2972 O  O    A ALA   A 1 134 ? 13.758 -4.183  -6.978  0.56 14.45 ?  134 ALA   A O    1 
ATOM   2973 O  O    B ALA   A 1 134 ? 13.776 -4.279  -7.550  0.44 14.19 ?  134 ALA   A O    1 
ATOM   2974 C  CB   A ALA   A 1 134 ? 16.694 -5.578  -7.762  0.56 13.90 ?  134 ALA   A CB   1 
ATOM   2975 C  CB   B ALA   A 1 134 ? 16.832 -5.657  -8.407  0.44 14.90 ?  134 ALA   A CB   1 
ATOM   2976 H  H    A ALA   A 1 134 ? 16.441 -3.088  -7.576  0.56 16.86 ?  134 ALA   A H    1 
ATOM   2977 H  H    B ALA   A 1 134 ? 16.624 -3.188  -8.049  0.44 17.86 ?  134 ALA   A H    1 
ATOM   2978 H  HA   A ALA   A 1 134 ? 15.587 -4.917  -9.354  0.56 16.51 ?  134 ALA   A HA   1 
ATOM   2979 H  HA   B ALA   A 1 134 ? 15.637 -4.886  -9.868  0.44 17.17 ?  134 ALA   A HA   1 
ATOM   2980 H  HB1  A ALA   A 1 134 ? 16.450 -6.507  -7.898  0.56 16.70 ?  134 ALA   A HB1  1 
ATOM   2981 H  HB1  B ALA   A 1 134 ? 16.572 -6.579  -8.569  0.44 17.90 ?  134 ALA   A HB1  1 
ATOM   2982 H  HB2  A ALA   A 1 134 ? 17.553 -5.398  -8.178  0.56 16.70 ?  134 ALA   A HB2  1 
ATOM   2983 H  HB2  B ALA   A 1 134 ? 17.655 -5.460  -8.884  0.44 17.90 ?  134 ALA   A HB2  1 
ATOM   2984 H  HB3  A ALA   A 1 134 ? 16.736 -5.380  -6.816  0.56 16.70 ?  134 ALA   A HB3  1 
ATOM   2985 H  HB3  B ALA   A 1 134 ? 16.957 -5.511  -7.457  0.44 17.90 ?  134 ALA   A HB3  1 
ATOM   2986 N  N    A ASP   A 1 135 ? 13.689 -6.102  -8.156  0.56 13.83 ?  135 ASP   A N    1 
ATOM   2987 N  N    B ASP   A 1 135 ? 13.930 -6.303  -8.536  0.44 14.31 ?  135 ASP   A N    1 
ATOM   2988 C  CA   A ASP   A 1 135 ? 12.434 -6.558  -7.569  0.56 14.55 ?  135 ASP   A CA   1 
ATOM   2989 C  CA   B ASP   A 1 135 ? 12.665 -6.801  -8.006  0.44 14.52 ?  135 ASP   A CA   1 
ATOM   2990 C  C    A ASP   A 1 135 ? 12.686 -7.000  -6.132  0.56 13.69 ?  135 ASP   A C    1 
ATOM   2991 C  C    B ASP   A 1 135 ? 12.854 -7.236  -6.557  0.44 13.69 ?  135 ASP   A C    1 
ATOM   2992 O  O    A ASP   A 1 135 ? 13.454 -7.948  -5.914  0.56 13.40 ?  135 ASP   A O    1 
ATOM   2993 O  O    B ASP   A 1 135 ? 13.663 -8.133  -6.293  0.44 13.86 ?  135 ASP   A O    1 
ATOM   2994 C  CB   A ASP   A 1 135 ? 11.918 -7.735  -8.389  0.56 16.84 ?  135 ASP   A CB   1 
ATOM   2995 C  CB   B ASP   A 1 135 ? 12.197 -7.991  -8.838  0.44 16.25 ?  135 ASP   A CB   1 
ATOM   2996 C  CG   A ASP   A 1 135 ? 10.718 -8.411  -7.759  0.56 19.81 ?  135 ASP   A CG   1 
ATOM   2997 C  CG   B ASP   A 1 135 ? 10.810 -8.492  -8.434  0.44 18.32 ?  135 ASP   A CG   1 
ATOM   2998 O  OD1  A ASP   A 1 135 ? 10.058 -7.786  -6.897  0.56 20.02 ?  135 ASP   A OD1  1 
ATOM   2999 O  OD1  B ASP   A 1 135 ? 10.384 -8.263  -7.283  0.44 18.93 ?  135 ASP   A OD1  1 
ATOM   3000 O  OD2  A ASP   A 1 135 ? 10.453 -9.578  -8.125  0.56 22.28 -1 135 ASP   A OD2  1 
ATOM   3001 O  OD2  B ASP   A 1 135 ? 10.139 -9.128  -9.273  0.44 19.68 -1 135 ASP   A OD2  1 
ATOM   3002 H  H    A ASP   A 1 135 ? 14.003 -6.631  -8.755  0.56 16.62 ?  135 ASP   A H    1 
ATOM   3003 H  H    B ASP   A 1 135 ? 14.350 -6.872  -9.023  0.44 17.19 ?  135 ASP   A H    1 
ATOM   3004 H  HA   A ASP   A 1 135 ? 11.772 -5.842  -7.594  0.56 17.48 ?  135 ASP   A HA   1 
ATOM   3005 H  HA   B ASP   A 1 135 ? 11.998 -6.105  -8.056  0.44 17.45 ?  135 ASP   A HA   1 
ATOM   3006 H  HB2  A ASP   A 1 135 ? 11.678 -7.422  -9.279  0.56 20.23 ?  135 ASP   A HB2  1 
ATOM   3007 H  HB2  B ASP   A 1 135 ? 12.171 -7.724  -9.773  0.44 19.52 ?  135 ASP   A HB2  1 
ATOM   3008 H  HB3  A ASP   A 1 135 ? 12.612 -8.406  -8.452  0.56 20.23 ?  135 ASP   A HB3  1 
ATOM   3009 H  HB3  B ASP   A 1 135 ? 12.826 -8.722  -8.724  0.44 19.52 ?  135 ASP   A HB3  1 
ATOM   3010 N  N    A PRO   A 1 136 ? 12.082 -6.357  -5.128  0.56 13.46 ?  136 PRO   A N    1 
ATOM   3011 N  N    B PRO   A 1 136 ? 12.133 -6.648  -5.599  0.44 13.37 ?  136 PRO   A N    1 
ATOM   3012 C  CA   A PRO   A 1 136 ? 12.342 -6.773  -3.738  0.56 13.51 ?  136 PRO   A CA   1 
ATOM   3013 C  CA   B PRO   A 1 136 ? 12.345 -7.027  -4.192  0.44 13.24 ?  136 PRO   A CA   1 
ATOM   3014 C  C    A PRO   A 1 136 ? 11.893 -8.190  -3.419  0.56 12.81 ?  136 PRO   A C    1 
ATOM   3015 C  C    B PRO   A 1 136 ? 11.910 -8.444  -3.860  0.44 12.65 ?  136 PRO   A C    1 
ATOM   3016 O  O    A PRO   A 1 136 ? 12.466 -8.815  -2.517  0.56 12.06 ?  136 PRO   A O    1 
ATOM   3017 O  O    B PRO   A 1 136 ? 12.507 -9.062  -2.971  0.44 12.54 ?  136 PRO   A O    1 
ATOM   3018 C  CB   A PRO   A 1 136 ? 11.588 -5.725  -2.906  0.56 14.20 ?  136 PRO   A CB   1 
ATOM   3019 C  CB   B PRO   A 1 136 ? 11.531 -5.982  -3.418  0.44 13.75 ?  136 PRO   A CB   1 
ATOM   3020 C  CG   A PRO   A 1 136 ? 10.552 -5.179  -3.833  0.56 15.38 ?  136 PRO   A CG   1 
ATOM   3021 C  CG   B PRO   A 1 136 ? 10.492 -5.523  -4.398  0.44 13.88 ?  136 PRO   A CG   1 
ATOM   3022 C  CD   A PRO   A 1 136 ? 11.185 -5.190  -5.193  0.56 14.26 ?  136 PRO   A CD   1 
ATOM   3023 C  CD   B PRO   A 1 136 ? 11.131 -5.580  -5.745  0.44 13.80 ?  136 PRO   A CD   1 
ATOM   3024 H  HA   A PRO   A 1 136 ? 13.291 -6.696  -3.545  0.56 16.23 ?  136 PRO   A HA   1 
ATOM   3025 H  HA   B PRO   A 1 136 ? 13.282 -6.938  -3.952  0.44 15.91 ?  136 PRO   A HA   1 
ATOM   3026 H  HB2  A PRO   A 1 136 ? 11.175 -6.152  -2.140  0.56 17.06 ?  136 PRO   A HB2  1 
ATOM   3027 H  HB2  B PRO   A 1 136 ? 11.119 -6.394  -2.640  0.44 16.52 ?  136 PRO   A HB2  1 
ATOM   3028 H  HB3  A PRO   A 1 136 ? 12.200 -5.027  -2.624  0.56 17.06 ?  136 PRO   A HB3  1 
ATOM   3029 H  HB3  B PRO   A 1 136 ? 12.112 -5.251  -3.152  0.44 16.52 ?  136 PRO   A HB3  1 
ATOM   3030 H  HG2  A PRO   A 1 136 ? 9.769  -5.751  -3.818  0.56 18.48 ?  136 PRO   A HG2  1 
ATOM   3031 H  HG2  B PRO   A 1 136 ? 9.729  -6.117  -4.361  0.44 16.68 ?  136 PRO   A HG2  1 
ATOM   3032 H  HG3  A PRO   A 1 136 ? 10.323 -4.275  -3.570  0.56 18.48 ?  136 PRO   A HG3  1 
ATOM   3033 H  HG3  B PRO   A 1 136 ? 10.233 -4.614  -4.189  0.44 16.68 ?  136 PRO   A HG3  1 
ATOM   3034 H  HD2  A PRO   A 1 136 ? 10.508 -5.322  -5.878  0.56 17.13 ?  136 PRO   A HD2  1 
ATOM   3035 H  HD2  B PRO   A 1 136 ? 10.483 -5.829  -6.422  0.44 16.58 ?  136 PRO   A HD2  1 
ATOM   3036 H  HD3  A PRO   A 1 136 ? 11.689 -4.374  -5.344  0.56 17.13 ?  136 PRO   A HD3  1 
ATOM   3037 H  HD3  B PRO   A 1 136 ? 11.568 -4.741  -5.958  0.44 16.58 ?  136 PRO   A HD3  1 
ATOM   3038 N  N    A ILE   A 1 137 ? 10.873 -8.708  -4.109  0.56 13.70 ?  137 ILE   A N    1 
ATOM   3039 N  N    B ILE   A 1 137 ? 10.880 -8.974  -4.525  0.44 12.92 ?  137 ILE   A N    1 
ATOM   3040 C  CA   A ILE   A 1 137 ? 10.485 -10.104 -3.911  0.56 14.12 ?  137 ILE   A CA   1 
ATOM   3041 C  CA   B ILE   A 1 137 ? 10.509 -10.371 -4.311  0.44 13.41 ?  137 ILE   A CA   1 
ATOM   3042 C  C    A ILE   A 1 137 ? 11.630 -11.025 -4.310  0.56 13.80 ?  137 ILE   A C    1 
ATOM   3043 C  C    B ILE   A 1 137 ? 11.682 -11.280 -4.650  0.44 13.12 ?  137 ILE   A C    1 
ATOM   3044 O  O    A ILE   A 1 137 ? 11.938 -12.004 -3.615  0.56 14.08 ?  137 ILE   A O    1 
ATOM   3045 O  O    B ILE   A 1 137 ? 11.997 -12.222 -3.912  0.44 13.56 ?  137 ILE   A O    1 
ATOM   3046 C  CB   A ILE   A 1 137 ? 9.192  -10.419 -4.687  0.56 15.55 ?  137 ILE   A CB   1 
ATOM   3047 C  CB   B ILE   A 1 137 ? 9.246  -10.719 -5.123  0.44 14.85 ?  137 ILE   A CB   1 
ATOM   3048 C  CG1  A ILE   A 1 137 ? 8.028  -9.565  -4.170  0.56 16.97 ?  137 ILE   A CG1  1 
ATOM   3049 C  CG1  B ILE   A 1 137 ? 8.053  -9.901  -4.621  0.44 16.41 ?  137 ILE   A CG1  1 
ATOM   3050 C  CG2  A ILE   A 1 137 ? 8.855  -11.905 -4.590  0.56 15.94 ?  137 ILE   A CG2  1 
ATOM   3051 C  CG2  B ILE   A 1 137 ? 8.943  -12.209 -5.036  0.44 15.19 ?  137 ILE   A CG2  1 
ATOM   3052 C  CD1  A ILE   A 1 137 ? 6.731  -9.804  -4.909  0.56 18.24 ?  137 ILE   A CD1  1 
ATOM   3053 C  CD1  B ILE   A 1 137 ? 6.779  -10.099 -5.421  0.44 17.73 ?  137 ILE   A CD1  1 
ATOM   3054 H  H    A ILE   A 1 137 ? 10.397 -8.275  -4.683  0.56 16.46 ?  137 ILE   A H    1 
ATOM   3055 H  H    B ILE   A 1 137 ? 10.389 -8.556  -5.091  0.44 15.52 ?  137 ILE   A H    1 
ATOM   3056 H  HA   A ILE   A 1 137 ? 10.306 -10.243 -2.971  0.56 16.97 ?  137 ILE   A HA   1 
ATOM   3057 H  HA   B ILE   A 1 137 ? 10.300 -10.507 -3.376  0.44 16.11 ?  137 ILE   A HA   1 
ATOM   3058 H  HB   A ILE   A 1 137 ? 9.332  -10.199 -5.619  0.56 18.68 ?  137 ILE   A HB   1 
ATOM   3059 H  HB   B ILE   A 1 137 ? 9.400  -10.491 -6.051  0.44 17.84 ?  137 ILE   A HB   1 
ATOM   3060 H  HG12 A ILE   A 1 137 ? 7.880  -9.764  -3.233  0.56 20.39 ?  137 ILE   A HG12 1 
ATOM   3061 H  HG12 B ILE   A 1 137 ? 7.867  -10.147 -3.701  0.44 19.72 ?  137 ILE   A HG12 1 
ATOM   3062 H  HG13 A ILE   A 1 137 ? 8.256  -8.625  -4.274  0.56 20.39 ?  137 ILE   A HG13 1 
ATOM   3063 H  HG13 B ILE   A 1 137 ? 8.282  -8.956  -4.664  0.44 19.72 ?  137 ILE   A HG13 1 
ATOM   3064 H  HG21 A ILE   A 1 137 ? 8.005  -12.081 -5.024  0.56 19.15 ?  137 ILE   A HG21 1 
ATOM   3065 H  HG21 B ILE   A 1 137 ? 8.176  -12.414 -5.593  0.44 18.24 ?  137 ILE   A HG21 1 
ATOM   3066 H  HG22 A ILE   A 1 137 ? 9.549  -12.413 -5.033  0.56 19.15 ?  137 ILE   A HG22 1 
ATOM   3067 H  HG22 B ILE   A 1 137 ? 9.703  -12.713 -5.352  0.44 18.24 ?  137 ILE   A HG22 1 
ATOM   3068 H  HG23 A ILE   A 1 137 ? 8.803  -12.151 -3.656  0.56 19.15 ?  137 ILE   A HG23 1 
ATOM   3069 H  HG23 B ILE   A 1 137 ? 8.749  -12.435 -4.114  0.44 18.24 ?  137 ILE   A HG23 1 
ATOM   3070 H  HD11 A ILE   A 1 137 ? 6.081  -10.190 -4.299  0.56 21.91 ?  137 ILE   A HD11 1 
ATOM   3071 H  HD11 B ILE   A 1 137 ? 6.042  -9.728  -4.917  0.44 21.30 ?  137 ILE   A HD11 1 
ATOM   3072 H  HD12 A ILE   A 1 137 ? 6.419  -8.958  -5.246  0.56 21.91 ?  137 ILE   A HD12 1 
ATOM   3073 H  HD12 B ILE   A 1 137 ? 6.868  -9.642  -6.271  0.44 21.30 ?  137 ILE   A HD12 1 
ATOM   3074 H  HD13 A ILE   A 1 137 ? 6.888  -10.408 -5.654  0.56 21.91 ?  137 ILE   A HD13 1 
ATOM   3075 H  HD13 B ILE   A 1 137 ? 6.623  -11.042 -5.564  0.44 21.30 ?  137 ILE   A HD13 1 
ATOM   3076 N  N    A HIS   A 1 138 ? 12.279 -10.723 -5.436  0.56 14.39 ?  138 HIS   A N    1 
ATOM   3077 N  N    B HIS   A 1 138 ? 12.349 -11.006 -5.771  0.44 13.04 ?  138 HIS   A N    1 
ATOM   3078 C  CA   A HIS   A 1 138 ? 13.447 -11.491 -5.853  0.56 14.39 ?  138 HIS   A CA   1 
ATOM   3079 C  CA   B HIS   A 1 138 ? 13.531 -11.776 -6.136  0.44 13.56 ?  138 HIS   A CA   1 
ATOM   3080 C  C    A HIS   A 1 138 ? 14.597 -11.340 -4.859  0.56 13.66 ?  138 HIS   A C    1 
ATOM   3081 C  C    B HIS   A 1 138 ? 14.633 -11.629 -5.093  0.44 13.06 ?  138 HIS   A C    1 
ATOM   3082 O  O    A HIS   A 1 138 ? 15.240 -12.331 -4.489  0.56 14.08 ?  138 HIS   A O    1 
ATOM   3083 O  O    B HIS   A 1 138 ? 15.313 -12.606 -4.756  0.44 13.12 ?  138 HIS   A O    1 
ATOM   3084 C  CB   A HIS   A 1 138 ? 13.863 -11.067 -7.263  0.56 15.39 ?  138 HIS   A CB   1 
ATOM   3085 C  CB   B HIS   A 1 138 ? 14.031 -11.334 -7.509  0.44 14.93 ?  138 HIS   A CB   1 
ATOM   3086 C  CG   A HIS   A 1 138 ? 15.137 -11.700 -7.728  0.56 16.21 ?  138 HIS   A CG   1 
ATOM   3087 C  CG   B HIS   A 1 138 ? 15.313 -11.987 -7.913  0.44 15.79 ?  138 HIS   A CG   1 
ATOM   3088 N  ND1  A HIS   A 1 138 ? 15.253 -13.052 -7.974  0.56 17.01 ?  138 HIS   A ND1  1 
ATOM   3089 N  ND1  B HIS   A 1 138 ? 15.425 -13.348 -8.101  0.44 16.62 ?  138 HIS   A ND1  1 
ATOM   3090 C  CD2  A HIS   A 1 138 ? 16.356 -11.167 -7.979  0.56 16.59 ?  138 HIS   A CD2  1 
ATOM   3091 C  CD2  B HIS   A 1 138 ? 16.542 -11.471 -8.148  0.44 16.00 ?  138 HIS   A CD2  1 
ATOM   3092 C  CE1  A HIS   A 1 138 ? 16.487 -13.322 -8.363  0.56 17.37 ?  138 HIS   A CE1  1 
ATOM   3093 C  CE1  B HIS   A 1 138 ? 16.667 -13.640 -8.443  0.44 16.83 ?  138 HIS   A CE1  1 
ATOM   3094 N  NE2  A HIS   A 1 138 ? 17.176 -12.195 -8.373  0.56 16.99 ?  138 HIS   A NE2  1 
ATOM   3095 N  NE2  B HIS   A 1 138 ? 17.365 -12.520 -8.478  0.44 16.54 ?  138 HIS   A NE2  1 
ATOM   3096 H  H    A HIS   A 1 138 ? 12.059 -10.080 -5.976  0.56 17.29 ?  138 HIS   A H    1 
ATOM   3097 H  H    B HIS   A 1 138 ? 12.143 -10.379 -6.327  0.44 15.67 ?  138 HIS   A H    1 
ATOM   3098 H  HA   A HIS   A 1 138 ? 13.200 -12.423 -5.889  0.56 17.29 ?  138 HIS   A HA   1 
ATOM   3099 H  HA   B HIS   A 1 138 ? 13.291 -12.712 -6.195  0.44 16.30 ?  138 HIS   A HA   1 
ATOM   3100 H  HB2  A HIS   A 1 138 ? 13.161 -11.319 -7.890  0.56 18.49 ?  138 HIS   A HB2  1 
ATOM   3101 H  HB2  B HIS   A 1 138 ? 13.358 -11.553 -8.176  0.44 17.93 ?  138 HIS   A HB2  1 
ATOM   3102 H  HB3  A HIS   A 1 138 ? 13.985 -10.104 -7.286  0.56 18.49 ?  138 HIS   A HB3  1 
ATOM   3103 H  HB3  B HIS   A 1 138 ? 14.175 -10.372 -7.497  0.44 17.93 ?  138 HIS   A HB3  1 
ATOM   3104 H  HD1  A HIS   A 1 138 ? 14.620 -13.630 -7.891  0.56 20.43 ?  138 HIS   A HD1  1 
ATOM   3105 H  HD2  A HIS   A 1 138 ? 16.591 -10.271 -7.905  0.56 19.93 ?  138 HIS   A HD2  1 
ATOM   3106 H  HD2  B HIS   A 1 138 ? 16.781 -10.573 -8.099  0.44 19.22 ?  138 HIS   A HD2  1 
ATOM   3107 H  HE1  A HIS   A 1 138 ? 16.814 -14.164 -8.587  0.56 20.86 ?  138 HIS   A HE1  1 
ATOM   3108 H  HE1  B HIS   A 1 138 ? 16.988 -14.489 -8.626  0.44 20.22 ?  138 HIS   A HE1  1 
ATOM   3109 H  HE2  B HIS   A 1 138 ? 18.197 -12.458 -8.675  0.44 19.87 ?  138 HIS   A HE2  1 
ATOM   3110 N  N    A SER   A 1 139 ? 14.867 -10.109 -4.410  0.56 12.97 ?  139 SER   A N    1 
ATOM   3111 N  N    B SER   A 1 139 ? 14.828 -10.415 -4.572  0.44 12.57 ?  139 SER   A N    1 
ATOM   3112 C  CA   A SER   A 1 139 ? 15.922 -9.896  -3.426  0.56 12.83 ?  139 SER   A CA   1 
ATOM   3113 C  CA   B SER   A 1 139 ? 15.905 -10.198 -3.612  0.44 12.10 ?  139 SER   A CA   1 
ATOM   3114 C  C    A SER   A 1 139 ? 15.700 -10.757 -2.190  0.56 12.66 ?  139 SER   A C    1 
ATOM   3115 C  C    B SER   A 1 139 ? 15.665 -10.972 -2.321  0.44 12.59 ?  139 SER   A C    1 
ATOM   3116 O  O    A SER   A 1 139 ? 16.654 -11.310 -1.629  0.56 12.36 ?  139 SER   A O    1 
ATOM   3117 O  O    B SER   A 1 139 ? 16.582 -11.623 -1.807  0.44 12.43 ?  139 SER   A O    1 
ATOM   3118 C  CB   A SER   A 1 139 ? 16.012 -8.410  -3.058  0.56 12.86 ?  139 SER   A CB   1 
ATOM   3119 C  CB   B SER   A 1 139 ? 16.092 -8.706  -3.329  0.44 11.62 ?  139 SER   A CB   1 
ATOM   3120 O  OG   A SER   A 1 139 ? 17.024 -8.177  -2.088  0.56 13.32 ?  139 SER   A OG   1 
ATOM   3121 O  OG   B SER   A 1 139 ? 17.179 -8.519  -2.436  0.44 10.54 ?  139 SER   A OG   1 
ATOM   3122 H  H    A SER   A 1 139 ? 14.452 -9.394  -4.644  0.56 15.59 ?  139 SER   A H    1 
ATOM   3123 H  H    B SER   A 1 139 ? 14.362 -9.719  -4.755  0.44 15.11 ?  139 SER   A H    1 
ATOM   3124 H  HA   A SER   A 1 139 ? 16.771 -10.158 -3.809  0.56 15.42 ?  139 SER   A HA   1 
ATOM   3125 H  HA   B SER   A 1 139 ? 16.733 -10.524 -3.999  0.44 14.54 ?  139 SER   A HA   1 
ATOM   3126 H  HB2  A SER   A 1 139 ? 16.228 -7.901  -3.857  0.56 15.46 ?  139 SER   A HB2  1 
ATOM   3127 H  HB2  B SER   A 1 139 ? 16.294 -8.245  -4.158  0.44 13.97 ?  139 SER   A HB2  1 
ATOM   3128 H  HB3  A SER   A 1 139 ? 15.162 -8.117  -2.700  0.56 15.46 ?  139 SER   A HB3  1 
ATOM   3129 H  HB3  B SER   A 1 139 ? 15.287 -8.351  -2.930  0.44 13.97 ?  139 SER   A HB3  1 
ATOM   3130 H  HG   A SER   A 1 139 ? 17.059 -7.345  -1.899  0.56 16.01 ?  139 SER   A HG   1 
ATOM   3131 H  HG   B SER   A 1 139 ? 17.287 -7.705  -2.266  0.44 12.67 ?  139 SER   A HG   1 
ATOM   3132 N  N    . LEU   A 1 140 ? 14.447 -10.907 -1.769  1.00 12.82 ?  140 LEU   A N    1 
ATOM   3133 C  CA   . LEU   A 1 140 ? 14.156 -11.706 -0.581  1.00 12.78 ?  140 LEU   A CA   1 
ATOM   3134 C  C    . LEU   A 1 140 ? 14.424 -13.187 -0.837  1.00 12.76 ?  140 LEU   A C    1 
ATOM   3135 O  O    . LEU   A 1 140 ? 14.981 -13.889 0.022   1.00 13.70 ?  140 LEU   A O    1 
ATOM   3136 C  CB   . LEU   A 1 140 ? 12.711 -11.483 -0.142  1.00 13.15 ?  140 LEU   A CB   1 
ATOM   3137 C  CG   . LEU   A 1 140 ? 12.244 -12.319 1.051   1.00 13.80 ?  140 LEU   A CG   1 
ATOM   3138 C  CD1  . LEU   A 1 140 ? 13.145 -12.140 2.263   1.00 14.49 ?  140 LEU   A CD1  1 
ATOM   3139 C  CD2  . LEU   A 1 140 ? 10.785 -11.976 1.387   1.00 15.03 ?  140 LEU   A CD2  1 
ATOM   3140 H  H    A LEU   A 1 140 ? 13.757 -10.562 -2.149  0.56 15.41 ?  140 LEU   A H    1 
ATOM   3141 H  H    B LEU   A 1 140 ? 13.796 -10.418 -2.050  0.44 15.41 ?  140 LEU   A H    1 
ATOM   3142 H  HA   . LEU   A 1 140 ? 14.729 -11.420 0.143   1.00 15.36 ?  140 LEU   A HA   1 
ATOM   3143 H  HB2  . LEU   A 1 140 ? 12.599 -10.555 0.099   1.00 15.80 ?  140 LEU   A HB2  1 
ATOM   3144 H  HB3  . LEU   A 1 140 ? 12.126 -11.697 -0.890  1.00 15.80 ?  140 LEU   A HB3  1 
ATOM   3145 H  HG   . LEU   A 1 140 ? 12.258 -13.259 0.798   1.00 16.58 ?  140 LEU   A HG   1 
ATOM   3146 H  HD11 . LEU   A 1 140 ? 12.750 -12.607 3.017   1.00 17.42 ?  140 LEU   A HD11 1 
ATOM   3147 H  HD12 . LEU   A 1 140 ? 14.014 -12.522 2.060   1.00 17.42 ?  140 LEU   A HD12 1 
ATOM   3148 H  HD13 . LEU   A 1 140 ? 13.227 -11.200 2.457   1.00 17.42 ?  140 LEU   A HD13 1 
ATOM   3149 H  HD21 . LEU   A 1 140 ? 10.497 -12.515 2.142   1.00 18.06 ?  140 LEU   A HD21 1 
ATOM   3150 H  HD22 . LEU   A 1 140 ? 10.725 -11.035 1.610   1.00 18.06 ?  140 LEU   A HD22 1 
ATOM   3151 H  HD23 . LEU   A 1 140 ? 10.224 -12.168 0.616   1.00 18.06 ?  140 LEU   A HD23 1 
ATOM   3152 N  N    . ARG   A 1 141 ? 14.046 -13.675 -2.021  1.00 13.25 ?  141 ARG   A N    1 
ATOM   3153 C  CA   . ARG   A 1 141 ? 14.290 -15.070 -2.371  1.00 14.49 ?  141 ARG   A CA   1 
ATOM   3154 C  C    . ARG   A 1 141 ? 15.785 -15.377 -2.374  1.00 13.74 ?  141 ARG   A C    1 
ATOM   3155 O  O    . ARG   A 1 141 ? 16.227 -16.383 -1.807  1.00 14.12 ?  141 ARG   A O    1 
ATOM   3156 C  CB   . ARG   A 1 141 ? 13.677 -15.356 -3.743  1.00 15.95 ?  141 ARG   A CB   1 
ATOM   3157 C  CG   . ARG   A 1 141 ? 13.717 -16.808 -4.172  1.00 18.99 ?  141 ARG   A CG   1 
ATOM   3158 C  CD   . ARG   A 1 141 ? 12.678 -17.585 -3.429  1.00 21.97 ?  141 ARG   A CD   1 
ATOM   3159 N  NE   . ARG   A 1 141 ? 13.258 -18.331 -2.325  1.00 22.77 ?  141 ARG   A NE   1 
ATOM   3160 C  CZ   . ARG   A 1 141 ? 12.544 -18.869 -1.344  1.00 23.48 ?  141 ARG   A CZ   1 
ATOM   3161 N  NH1  . ARG   A 1 141 ? 11.254 -18.613 -1.208  1.00 22.67 ?  141 ARG   A NH1  1 
ATOM   3162 N  NH2  . ARG   A 1 141 ? 13.145 -19.665 -0.464  1.00 24.76 ?  141 ARG   A NH2  1 
ATOM   3163 H  H    . ARG   A 1 141 ? 13.648 -13.217 -2.632  1.00 15.92 ?  141 ARG   A H    1 
ATOM   3164 H  HA   . ARG   A 1 141 ? 13.863 -15.644 -1.722  1.00 17.42 ?  141 ARG   A HA   1 
ATOM   3165 H  HB2  . ARG   A 1 141 ? 12.749 -15.071 -3.739  1.00 19.16 ?  141 ARG   A HB2  1 
ATOM   3166 H  HB3  . ARG   A 1 141 ? 14.163 -14.845 -4.411  1.00 19.16 ?  141 ARG   A HB3  1 
ATOM   3167 H  HG2  . ARG   A 1 141 ? 13.533 -16.872 -5.124  1.00 22.81 ?  141 ARG   A HG2  1 
ATOM   3168 H  HG3  . ARG   A 1 141 ? 14.591 -17.186 -3.974  1.00 22.81 ?  141 ARG   A HG3  1 
ATOM   3169 H  HD2  . ARG   A 1 141 ? 12.021 -16.974 -3.057  1.00 26.38 ?  141 ARG   A HD2  1 
ATOM   3170 H  HD3  . ARG   A 1 141 ? 12.246 -18.205 -4.037  1.00 26.38 ?  141 ARG   A HD3  1 
ATOM   3171 H  HE   . ARG   A 1 141 ? 14.085 -18.555 -2.383  1.00 27.34 ?  141 ARG   A HE   1 
ATOM   3172 H  HH11 . ARG   A 1 141 ? 10.847 -18.113 -1.777  1.00 27.22 ?  141 ARG   A HH11 1 
ATOM   3173 H  HH12 . ARG   A 1 141 ? 10.810 -18.967 -0.559  1.00 27.22 ?  141 ARG   A HH12 1 
ATOM   3174 H  HH21 . ARG   A 1 141 ? 13.984 -19.832 -0.538  1.00 29.74 ?  141 ARG   A HH21 1 
ATOM   3175 H  HH22 . ARG   A 1 141 ? 12.696 -20.003 0.189   1.00 29.74 ?  141 ARG   A HH22 1 
ATOM   3176 N  N    . VAL   A 1 142 ? 16.583 -14.521 -3.015  1.00 13.45 ?  142 VAL   A N    1 
ATOM   3177 C  CA   . VAL   A 1 142 ? 18.029 -14.731 -3.024  1.00 13.28 ?  142 VAL   A CA   1 
ATOM   3178 C  C    . VAL   A 1 142 ? 18.578 -14.698 -1.606  1.00 12.69 ?  142 VAL   A C    1 
ATOM   3179 O  O    . VAL   A 1 142 ? 19.443 -15.503 -1.241  1.00 13.15 ?  142 VAL   A O    1 
ATOM   3180 C  CB   . VAL   A 1 142 ? 18.737 -13.713 -3.938  1.00 13.60 ?  142 VAL   A CB   1 
ATOM   3181 C  CG1  . VAL   A 1 142 ? 20.255 -13.917 -3.880  1.00 13.46 ?  142 VAL   A CG1  1 
ATOM   3182 C  CG2  . VAL   A 1 142 ? 18.254 -13.843 -5.368  1.00 14.90 ?  142 VAL   A CG2  1 
ATOM   3183 H  H    . VAL   A 1 142 ? 16.321 -13.814 -3.440  1.00 16.16 ?  142 VAL   A H    1 
ATOM   3184 H  HA   . VAL   A 1 142 ? 18.210 -15.606 -3.383  1.00 15.95 ?  142 VAL   A HA   1 
ATOM   3185 H  HB   . VAL   A 1 142 ? 18.550 -12.808 -3.633  1.00 16.34 ?  142 VAL   A HB   1 
ATOM   3186 H  HG11 . VAL   A 1 142 ? 20.673 -13.425 -4.607  1.00 16.17 ?  142 VAL   A HG11 1 
ATOM   3187 H  HG12 . VAL   A 1 142 ? 20.593 -13.586 -3.030  1.00 16.17 ?  142 VAL   A HG12 1 
ATOM   3188 H  HG13 . VAL   A 1 142 ? 20.453 -14.862 -3.968  1.00 16.17 ?  142 VAL   A HG13 1 
ATOM   3189 H  HG21 . VAL   A 1 142 ? 18.671 -13.149 -5.904  1.00 17.90 ?  142 VAL   A HG21 1 
ATOM   3190 H  HG22 . VAL   A 1 142 ? 18.507 -14.716 -5.701  1.00 17.90 ?  142 VAL   A HG22 1 
ATOM   3191 H  HG23 . VAL   A 1 142 ? 17.294 -13.742 -5.382  1.00 17.90 ?  142 VAL   A HG23 1 
ATOM   3192 N  N    . CYS   A 1 143 ? 18.108 -13.755 -0.790  1.00 12.48 ?  143 CYS   A N    1 
ATOM   3193 C  CA   . CYS   A 1 143 ? 18.557 -13.691 0.596   1.00 13.16 ?  143 CYS   A CA   1 
ATOM   3194 C  C    . CYS   A 1 143 ? 18.334 -15.027 1.298   1.00 12.74 ?  143 CYS   A C    1 
ATOM   3195 O  O    . CYS   A 1 143 ? 19.249 -15.597 1.898   1.00 12.77 ?  143 CYS   A O    1 
ATOM   3196 C  CB   . CYS   A 1 143 ? 17.807 -12.576 1.325   1.00 13.31 ?  143 CYS   A CB   1 
ATOM   3197 S  SG   . CYS   A 1 143 ? 18.302 -12.365 3.044   1.00 13.74 ?  143 CYS   A SG   1 
ATOM   3198 H  H    . CYS   A 1 143 ? 17.532 -13.156 -1.006  1.00 14.99 ?  143 CYS   A H    1 
ATOM   3199 H  HA   . CYS   A 1 143 ? 19.502 -13.494 0.624   1.00 15.81 ?  143 CYS   A HA   1 
ATOM   3200 H  HB2  . CYS   A 1 143 ? 17.961 -11.741 0.862   1.00 15.99 ?  143 CYS   A HB2  1 
ATOM   3201 H  HB3  . CYS   A 1 143 ? 16.857 -12.783 1.317   1.00 15.99 ?  143 CYS   A HB3  1 
ATOM   3202 H  HG   . CYS   A 1 143 ? 17.714 -11.423 3.498   1.00 16.51 ?  143 CYS   A HG   1 
ATOM   3203 N  N    . VAL   A 1 144 ? 17.100 -15.529 1.249   1.00 13.48 ?  144 VAL   A N    1 
ATOM   3204 C  CA   . VAL   A 1 144 ? 16.749 -16.753 1.960   1.00 14.73 ?  144 VAL   A CA   1 
ATOM   3205 C  C    . VAL   A 1 144 ? 17.572 -17.928 1.460   1.00 14.49 ?  144 VAL   A C    1 
ATOM   3206 O  O    . VAL   A 1 144 ? 17.926 -18.831 2.232   1.00 15.08 ?  144 VAL   A O    1 
ATOM   3207 C  CB   . VAL   A 1 144 ? 15.234 -16.996 1.811   1.00 17.49 ?  144 VAL   A CB   1 
ATOM   3208 C  CG1  . VAL   A 1 144 ? 14.868 -18.437 2.116   1.00 19.56 ?  144 VAL   A CG1  1 
ATOM   3209 C  CG2  . VAL   A 1 144 ? 14.465 -15.993 2.686   1.00 17.52 ?  144 VAL   A CG2  1 
ATOM   3210 H  H    . VAL   A 1 144 ? 16.440 -15.171 0.817   1.00 16.20 ?  144 VAL   A H    1 
ATOM   3211 H  HA   . VAL   A 1 144 ? 16.931 -16.638 2.900   1.00 17.70 ?  144 VAL   A HA   1 
ATOM   3212 H  HB   . VAL   A 1 144 ? 14.979 -16.819 0.887   1.00 21.01 ?  144 VAL   A HB   1 
ATOM   3213 H  HG11 . VAL   A 1 144 ? 13.912 -18.489 2.286   1.00 23.50 ?  144 VAL   A HG11 1 
ATOM   3214 H  HG12 . VAL   A 1 144 ? 15.094 -18.989 1.351   1.00 23.50 ?  144 VAL   A HG12 1 
ATOM   3215 H  HG13 . VAL   A 1 144 ? 15.358 -18.725 2.897   1.00 23.50 ?  144 VAL   A HG13 1 
ATOM   3216 H  HG21 . VAL   A 1 144 ? 13.508 -16.153 2.595   1.00 21.05 ?  144 VAL   A HG21 1 
ATOM   3217 H  HG22 . VAL   A 1 144 ? 14.728 -16.107 3.611   1.00 21.05 ?  144 VAL   A HG22 1 
ATOM   3218 H  HG23 . VAL   A 1 144 ? 14.669 -15.087 2.395   1.00 21.05 ?  144 VAL   A HG23 1 
ATOM   3219 N  N    . ASP   A 1 145 ? 17.848 -17.963 0.160   1.00 14.75 ?  145 ASP   A N    1 
ATOM   3220 C  CA   . ASP   A 1 145 ? 18.565 -19.076 -0.454  1.00 15.35 ?  145 ASP   A CA   1 
ATOM   3221 C  C    . ASP   A 1 145 ? 20.085 -18.928 -0.393  1.00 15.33 ?  145 ASP   A C    1 
ATOM   3222 O  O    . ASP   A 1 145 ? 20.797 -19.829 -0.853  1.00 17.36 ?  145 ASP   A O    1 
ATOM   3223 C  CB   . ASP   A 1 145 ? 18.138 -19.228 -1.919  1.00 16.73 ?  145 ASP   A CB   1 
ATOM   3224 C  CG   . ASP   A 1 145 ? 16.703 -19.700 -2.071  1.00 18.98 ?  145 ASP   A CG   1 
ATOM   3225 O  OD1  . ASP   A 1 145 ? 16.121 -20.237 -1.102  1.00 20.02 ?  145 ASP   A OD1  1 
ATOM   3226 O  OD2  . ASP   A 1 145 ? 16.156 -19.531 -3.179  1.00 20.68 -1 145 ASP   A OD2  1 
ATOM   3227 H  H    . ASP   A 1 145 ? 17.613 -17.350 -0.400  1.00 17.72 ?  145 ASP   A H    1 
ATOM   3228 H  HA   . ASP   A 1 145 ? 18.327 -19.892 0.005   1.00 18.44 ?  145 ASP   A HA   1 
ATOM   3229 H  HB2  . ASP   A 1 145 ? 18.221 -18.365 -2.362  1.00 20.09 ?  145 ASP   A HB2  1 
ATOM   3230 H  HB3  . ASP   A 1 145 ? 18.718 -19.874 -2.350  1.00 20.09 ?  145 ASP   A HB3  1 
ATOM   3231 N  N    . THR   A 1 146 ? 20.603 -17.824 0.150   1.00 13.66 ?  146 THR   A N    1 
ATOM   3232 C  CA   . THR   A 1 146 ? 22.042 -17.568 0.174   1.00 13.12 ?  146 THR   A CA   1 
ATOM   3233 C  C    . THR   A 1 146 ? 22.586 -17.383 1.580   1.00 13.01 ?  146 THR   A C    1 
ATOM   3234 O  O    . THR   A 1 146 ? 23.659 -17.920 1.903   1.00 14.26 ?  146 THR   A O    1 
ATOM   3235 C  CB   . THR   A 1 146 ? 22.365 -16.320 -0.668  1.00 12.93 ?  146 THR   A CB   1 
ATOM   3236 O  OG1  . THR   A 1 146 ? 21.867 -16.507 -1.992  1.00 13.56 ?  146 THR   A OG1  1 
ATOM   3237 C  CG2  . THR   A 1 146 ? 23.860 -16.088 -0.734  1.00 13.63 ?  146 THR   A CG2  1 
ATOM   3238 H  H    . THR   A 1 146 ? 20.131 -17.196 0.506   1.00 16.41 ?  146 THR   A H    1 
ATOM   3239 H  HA   . THR   A 1 146 ? 22.504 -18.317 -0.221  1.00 15.77 ?  146 THR   A HA   1 
ATOM   3240 H  HB   . THR   A 1 146 ? 21.948 -15.538 -0.267  1.00 15.53 ?  146 THR   A HB   1 
ATOM   3241 H  HG1  . THR   A 1 146 ? 21.034 -16.600 -1.972  1.00 16.30 ?  146 THR   A HG1  1 
ATOM   3242 H  HG21 . THR   A 1 146 ? 24.059 -15.433 -1.420  1.00 16.37 ?  146 THR   A HG21 1 
ATOM   3243 H  HG22 . THR   A 1 146 ? 24.185 -15.758 0.119   1.00 16.37 ?  146 THR   A HG22 1 
ATOM   3244 H  HG23 . THR   A 1 146 ? 24.312 -16.917 -0.948  1.00 16.37 ?  146 THR   A HG23 1 
ATOM   3245 N  N    . VAL   A 1 147 ? 21.909 -16.588 2.405   1.00 12.75 ?  147 VAL   A N    1 
ATOM   3246 C  CA   . VAL   A 1 147 ? 22.393 -16.290 3.745   1.00 13.19 ?  147 VAL   A CA   1 
ATOM   3247 C  C    . VAL   A 1 147 ? 22.071 -17.460 4.663   1.00 13.39 ?  147 VAL   A C    1 
ATOM   3248 O  O    . VAL   A 1 147 ? 20.932 -17.944 4.703   1.00 13.81 ?  147 VAL   A O    1 
ATOM   3249 C  CB   . VAL   A 1 147 ? 21.771 -14.984 4.261   1.00 13.18 ?  147 VAL   A CB   1 
ATOM   3250 C  CG1  . VAL   A 1 147 ? 22.318 -14.649 5.631   1.00 14.31 ?  147 VAL   A CG1  1 
ATOM   3251 C  CG2  . VAL   A 1 147 ? 22.030 -13.839 3.276   1.00 13.44 ?  147 VAL   A CG2  1 
ATOM   3252 H  H    . VAL   A 1 147 ? 21.158 -16.212 2.213   1.00 15.32 ?  147 VAL   A H    1 
ATOM   3253 H  HA   . VAL   A 1 147 ? 23.353 -16.179 3.717   1.00 15.85 ?  147 VAL   A HA   1 
ATOM   3254 H  HB   . VAL   A 1 147 ? 20.814 -15.099 4.344   1.00 15.84 ?  147 VAL   A HB   1 
ATOM   3255 H  HG11 . VAL   A 1 147 ? 22.050 -13.750 5.866   1.00 17.19 ?  147 VAL   A HG11 1 
ATOM   3256 H  HG12 . VAL   A 1 147 ? 21.962 -15.281 6.277   1.00 17.19 ?  147 VAL   A HG12 1 
ATOM   3257 H  HG13 . VAL   A 1 147 ? 23.287 -14.712 5.608   1.00 17.19 ?  147 VAL   A HG13 1 
ATOM   3258 H  HG21 . VAL   A 1 147 ? 21.709 -13.012 3.669   1.00 16.15 ?  147 VAL   A HG21 1 
ATOM   3259 H  HG22 . VAL   A 1 147 ? 22.978 -13.781 3.102   1.00 16.15 ?  147 VAL   A HG22 1 
ATOM   3260 H  HG23 . VAL   A 1 147 ? 21.548 -14.022 2.454   1.00 16.15 ?  147 VAL   A HG23 1 
ATOM   3261 N  N    . ARG   A 1 148 ? 23.083 -17.913 5.404   1.00 13.42 ?  148 ARG   A N    1 
ATOM   3262 C  CA   . ARG   A 1 148 ? 22.960 -18.988 6.374   1.00 13.64 ?  148 ARG   A CA   1 
ATOM   3263 C  C    . ARG   A 1 148 ? 23.075 -18.511 7.810   1.00 14.16 ?  148 ARG   A C    1 
ATOM   3264 O  O    . ARG   A 1 148 ? 22.661 -19.237 8.725   1.00 15.37 ?  148 ARG   A O    1 
ATOM   3265 C  CB   . ARG   A 1 148 ? 24.014 -20.075 6.111   1.00 14.52 ?  148 ARG   A CB   1 
ATOM   3266 C  CG   . ARG   A 1 148 ? 23.879 -20.725 4.749   1.00 15.70 ?  148 ARG   A CG   1 
ATOM   3267 C  CD   . ARG   A 1 148 ? 24.983 -21.751 4.490   1.00 16.70 ?  148 ARG   A CD   1 
ATOM   3268 N  NE   . ARG   A 1 148 ? 26.324 -21.168 4.525   1.00 16.69 ?  148 ARG   A NE   1 
ATOM   3269 C  CZ   . ARG   A 1 148 ? 26.846 -20.441 3.546   1.00 15.85 ?  148 ARG   A CZ   1 
ATOM   3270 N  NH1  . ARG   A 1 148 ? 26.184 -20.221 2.421   1.00 16.29 ?  148 ARG   A NH1  1 
ATOM   3271 N  NH2  . ARG   A 1 148 ? 28.057 -19.903 3.707   1.00 16.19 ?  148 ARG   A NH2  1 
ATOM   3272 H  H    . ARG   A 1 148 ? 23.882 -17.588 5.352   1.00 16.12 ?  148 ARG   A H    1 
ATOM   3273 H  HA   . ARG   A 1 148 ? 22.090 -19.391 6.277   1.00 16.39 ?  148 ARG   A HA   1 
ATOM   3274 H  HB2  . ARG   A 1 148 ? 24.899 -19.685 6.168   1.00 17.44 ?  148 ARG   A HB2  1 
ATOM   3275 H  HB3  . ARG   A 1 148 ? 23.918 -20.774 6.779   1.00 17.44 ?  148 ARG   A HB3  1 
ATOM   3276 H  HG2  . ARG   A 1 148 ? 23.021 -21.172 4.696   1.00 18.86 ?  148 ARG   A HG2  1 
ATOM   3277 H  HG3  . ARG   A 1 148 ? 23.936 -20.033 4.067   1.00 18.86 ?  148 ARG   A HG3  1 
ATOM   3278 H  HD2  . ARG   A 1 148 ? 24.937 -22.436 5.171   1.00 20.06 ?  148 ARG   A HD2  1 
ATOM   3279 H  HD3  . ARG   A 1 148 ? 24.846 -22.141 3.613   1.00 20.06 ?  148 ARG   A HD3  1 
ATOM   3280 H  HE   . ARG   A 1 148 ? 26.799 -21.297 5.225   1.00 20.05 ?  148 ARG   A HE   1 
ATOM   3281 H  HH11 . ARG   A 1 148 ? 25.399 -20.547 2.307   1.00 19.57 ?  148 ARG   A HH11 1 
ATOM   3282 H  HH12 . ARG   A 1 148 ? 26.542 -19.738 1.801   1.00 19.57 ?  148 ARG   A HH12 1 
ATOM   3283 H  HH21 . ARG   A 1 148 ? 28.492 -20.037 4.435   1.00 19.44 ?  148 ARG   A HH21 1 
ATOM   3284 H  HH22 . ARG   A 1 148 ? 28.406 -19.428 3.079   1.00 19.44 ?  148 ARG   A HH22 1 
ATOM   3285 N  N    . THR   A 1 149 ? 23.617 -17.315 8.021   1.00 14.02 ?  149 THR   A N    1 
ATOM   3286 C  CA   . THR   A 1 149 ? 23.686 -16.713 9.337   1.00 14.24 ?  149 THR   A CA   1 
ATOM   3287 C  C    . THR   A 1 149 ? 22.357 -16.018 9.634   1.00 13.84 ?  149 THR   A C    1 
ATOM   3288 O  O    . THR   A 1 149 ? 21.431 -16.010 8.811   1.00 14.31 ?  149 THR   A O    1 
ATOM   3289 C  CB   . THR   A 1 149 ? 24.883 -15.772 9.391   1.00 14.64 ?  149 THR   A CB   1 
ATOM   3290 O  OG1  . THR   A 1 149 ? 24.762 -14.850 8.306   1.00 14.58 ?  149 THR   A OG1  1 
ATOM   3291 C  CG2  . THR   A 1 149 ? 26.204 -16.566 9.284   1.00 15.24 ?  149 THR   A CG2  1 
ATOM   3292 H  H    . THR   A 1 149 ? 23.965 -16.820 7.401   1.00 16.85 ?  149 THR   A H    1 
ATOM   3293 H  HA   . THR   A 1 149 ? 23.815 -17.413 9.996   1.00 17.11 ?  149 THR   A HA   1 
ATOM   3294 H  HB   . THR   A 1 149 ? 24.874 -15.291 10.232  1.00 17.58 ?  149 THR   A HB   1 
ATOM   3295 H  HG1  . THR   A 1 149 ? 25.410 -14.319 8.304   1.00 17.51 ?  149 THR   A HG1  1 
ATOM   3296 H  HG21 . THR   A 1 149 ? 26.961 -15.963 9.335   1.00 18.32 ?  149 THR   A HG21 1 
ATOM   3297 H  HG22 . THR   A 1 149 ? 26.268 -17.211 10.009  1.00 18.32 ?  149 THR   A HG22 1 
ATOM   3298 H  HG23 . THR   A 1 149 ? 26.240 -17.045 8.439   1.00 18.32 ?  149 THR   A HG23 1 
ATOM   3299 N  N    . ASN   A 1 150 ? 22.222 -15.483 10.840  1.00 14.10 ?  150 ASN   A N    1 
ATOM   3300 C  CA   . ASN   A 1 150 ? 20.933 -14.968 11.295  1.00 14.44 ?  150 ASN   A CA   1 
ATOM   3301 C  C    . ASN   A 1 150 ? 20.757 -13.529 10.831  1.00 13.97 ?  150 ASN   A C    1 
ATOM   3302 O  O    . ASN   A 1 150 ? 21.507 -12.637 11.249  1.00 14.85 ?  150 ASN   A O    1 
ATOM   3303 C  CB   . ASN   A 1 150 ? 20.832 -15.072 12.811  1.00 16.98 ?  150 ASN   A CB   1 
ATOM   3304 C  CG   . ASN   A 1 150 ? 20.752 -16.503 13.274  1.00 21.05 ?  150 ASN   A CG   1 
ATOM   3305 O  OD1  . ASN   A 1 150 ? 20.169 -17.343 12.594  1.00 22.31 ?  150 ASN   A OD1  1 
ATOM   3306 N  ND2  . ASN   A 1 150 ? 21.352 -16.798 14.424  1.00 23.34 ?  150 ASN   A ND2  1 
ATOM   3307 H  H    . ASN   A 1 150 ? 22.856 -15.418 11.419  1.00 16.94 ?  150 ASN   A H    1 
ATOM   3308 H  HA   . ASN   A 1 150 ? 20.219 -15.506 10.912  1.00 17.35 ?  150 ASN   A HA   1 
ATOM   3309 H  HB2  . ASN   A 1 150 ? 21.614 -14.676 13.216  1.00 20.40 ?  150 ASN   A HB2  1 
ATOM   3310 H  HB3  . ASN   A 1 150 ? 20.028 -14.622 13.114  1.00 20.40 ?  150 ASN   A HB3  1 
ATOM   3311 H  HD21 . ASN   A 1 150 ? 21.337 -17.606 14.735  1.00 28.03 ?  150 ASN   A HD21 1 
ATOM   3312 H  HD22 . ASN   A 1 150 ? 21.754 -16.182 14.872  1.00 28.03 ?  150 ASN   A HD22 1 
ATOM   3313 N  N    . VAL   A 1 151 ? 19.778 -13.303 9.963   1.00 13.36 ?  151 VAL   A N    1 
ATOM   3314 C  CA   . VAL   A 1 151 ? 19.574 -11.997 9.359   1.00 13.43 ?  151 VAL   A CA   1 
ATOM   3315 C  C    . VAL   A 1 151 ? 18.189 -11.480 9.715   1.00 13.08 ?  151 VAL   A C    1 
ATOM   3316 O  O    . VAL   A 1 151 ? 17.180 -12.189 9.562   1.00 14.68 ?  151 VAL   A O    1 
ATOM   3317 C  CB   . VAL   A 1 151 ? 19.866 -11.990 7.844   1.00 14.82 ?  151 VAL   A CB   1 
ATOM   3318 C  CG1  . VAL   A 1 151 ? 19.026 -12.998 7.101   1.00 15.95 ?  151 VAL   A CG1  1 
ATOM   3319 C  CG2  . VAL   A 1 151 ? 19.701 -10.577 7.275   1.00 15.21 ?  151 VAL   A CG2  1 
ATOM   3320 H  H    . VAL   A 1 151 ? 19.209 -13.899 9.710   1.00 16.05 ?  151 VAL   A H    1 
ATOM   3321 H  HA   . VAL   A 1 151 ? 20.214 -11.386 9.760   1.00 16.14 ?  151 VAL   A HA   1 
ATOM   3322 H  HB   . VAL   A 1 151 ? 20.797 -12.244 7.715   1.00 17.80 ?  151 VAL   A HB   1 
ATOM   3323 H  HG11 . VAL   A 1 151 ? 19.205 -12.925 6.151   1.00 19.16 ?  151 VAL   A HG11 1 
ATOM   3324 H  HG12 . VAL   A 1 151 ? 19.260 -13.892 7.410   1.00 19.16 ?  151 VAL   A HG12 1 
ATOM   3325 H  HG13 . VAL   A 1 151 ? 18.089 -12.825 7.277   1.00 19.16 ?  151 VAL   A HG13 1 
ATOM   3326 H  HG21 . VAL   A 1 151 ? 20.022 -10.571 6.356   1.00 18.28 ?  151 VAL   A HG21 1 
ATOM   3327 H  HG22 . VAL   A 1 151 ? 18.766 -10.333 7.298   1.00 18.28 ?  151 VAL   A HG22 1 
ATOM   3328 H  HG23 . VAL   A 1 151 ? 20.225 -9.958  7.806   1.00 18.28 ?  151 VAL   A HG23 1 
ATOM   3329 N  N    A TYR   A 1 152 ? 18.170 -10.256 10.232  0.56 13.09 ?  152 TYR   A N    1 
ATOM   3330 N  N    B TYR   A 1 152 ? 18.152 -10.226 10.164  0.44 13.63 ?  152 TYR   A N    1 
ATOM   3331 C  CA   A TYR   A 1 152 ? 16.973 -9.524  10.609  0.56 13.02 ?  152 TYR   A CA   1 
ATOM   3332 C  CA   B TYR   A 1 152 ? 16.934 -9.508  10.517  0.44 13.65 ?  152 TYR   A CA   1 
ATOM   3333 C  C    A TYR   A 1 152 ? 16.791 -8.416  9.584   0.56 12.32 ?  152 TYR   A C    1 
ATOM   3334 C  C    B TYR   A 1 152 ? 16.723 -8.409  9.481   0.44 13.04 ?  152 TYR   A C    1 
ATOM   3335 O  O    A TYR   A 1 152 ? 17.583 -7.466  9.534   0.56 12.26 ?  152 TYR   A O    1 
ATOM   3336 O  O    B TYR   A 1 152 ? 17.443 -7.404  9.476   0.44 13.43 ?  152 TYR   A O    1 
ATOM   3337 C  CB   A TYR   A 1 152 ? 17.142 -8.985  12.024  0.56 13.93 ?  152 TYR   A CB   1 
ATOM   3338 C  CB   B TYR   A 1 152 ? 17.060 -8.955  11.934  0.44 14.43 ?  152 TYR   A CB   1 
ATOM   3339 C  CG   A TYR   A 1 152 ? 17.114 -10.111 13.025  0.56 14.59 ?  152 TYR   A CG   1 
ATOM   3340 C  CG   B TYR   A 1 152 ? 16.965 -10.047 12.975  0.44 15.14 ?  152 TYR   A CG   1 
ATOM   3341 C  CD1  A TYR   A 1 152 ? 18.259 -10.837 13.324  0.56 15.84 ?  152 TYR   A CD1  1 
ATOM   3342 C  CD1  B TYR   A 1 152 ? 18.054 -10.863 13.267  0.44 16.14 ?  152 TYR   A CD1  1 
ATOM   3343 C  CD2  A TYR   A 1 152 ? 15.927 -10.489 13.632  0.56 14.84 ?  152 TYR   A CD2  1 
ATOM   3344 C  CD2  B TYR   A 1 152 ? 15.774 -10.286 13.645  0.44 15.63 ?  152 TYR   A CD2  1 
ATOM   3345 C  CE1  A TYR   A 1 152 ? 18.231 -11.889 14.217  0.56 16.91 ?  152 TYR   A CE1  1 
ATOM   3346 C  CE1  B TYR   A 1 152 ? 17.959 -11.879 14.208  0.44 17.11 ?  152 TYR   A CE1  1 
ATOM   3347 C  CE2  A TYR   A 1 152 ? 15.885 -11.545 14.530  0.56 16.00 ?  152 TYR   A CE2  1 
ATOM   3348 C  CE2  B TYR   A 1 152 ? 15.669 -11.297 14.587  0.44 16.65 ?  152 TYR   A CE2  1 
ATOM   3349 C  CZ   A TYR   A 1 152 ? 17.045 -12.240 14.820  0.56 16.73 ?  152 TYR   A CZ   1 
ATOM   3350 C  CZ   B TYR   A 1 152 ? 16.763 -12.089 14.864  0.44 17.37 ?  152 TYR   A CZ   1 
ATOM   3351 O  OH   A TYR   A 1 152 ? 17.022 -13.298 15.707  0.56 18.68 ?  152 TYR   A OH   1 
ATOM   3352 O  OH   B TYR   A 1 152 ? 16.658 -13.095 15.798  0.44 19.22 ?  152 TYR   A OH   1 
ATOM   3353 H  H    A TYR   A 1 152 ? 18.893 -9.797  10.367  0.56 15.73 ?  152 TYR   A H    1 
ATOM   3354 H  H    B TYR   A 1 152 ? 18.863 -9.741  10.268  0.44 16.38 ?  152 TYR   A H    1 
ATOM   3355 H  HA   A TYR   A 1 152 ? 16.208 -10.116 10.578  0.56 15.65 ?  152 TYR   A HA   1 
ATOM   3356 H  HA   B TYR   A 1 152 ? 16.181 -10.115 10.486  0.44 16.40 ?  152 TYR   A HA   1 
ATOM   3357 H  HB2  A TYR   A 1 152 ? 17.996 -8.536  12.097  0.56 16.74 ?  152 TYR   A HB2  1 
ATOM   3358 H  HB2  B TYR   A 1 152 ? 17.920 -8.521  12.033  0.44 17.34 ?  152 TYR   A HB2  1 
ATOM   3359 H  HB3  A TYR   A 1 152 ? 16.418 -8.378  12.224  0.56 16.74 ?  152 TYR   A HB3  1 
ATOM   3360 H  HB3  B TYR   A 1 152 ? 16.343 -8.324  12.095  0.44 17.34 ?  152 TYR   A HB3  1 
ATOM   3361 H  HD1  A TYR   A 1 152 ? 19.064 -10.607 12.919  0.56 19.03 ?  152 TYR   A HD1  1 
ATOM   3362 H  HD1  B TYR   A 1 152 ? 18.861 -10.724 12.824  0.44 19.39 ?  152 TYR   A HD1  1 
ATOM   3363 H  HD2  A TYR   A 1 152 ? 15.142 -10.025 13.435  0.56 17.83 ?  152 TYR   A HD2  1 
ATOM   3364 H  HD2  B TYR   A 1 152 ? 15.031 -9.758  13.462  0.44 18.78 ?  152 TYR   A HD2  1 
ATOM   3365 H  HE1  A TYR   A 1 152 ? 19.006 -12.359 14.417  0.56 20.31 ?  152 TYR   A HE1  1 
ATOM   3366 H  HE1  B TYR   A 1 152 ? 18.701 -12.412 14.397  0.44 20.55 ?  152 TYR   A HE1  1 
ATOM   3367 H  HE2  A TYR   A 1 152 ? 15.079 -11.778 14.936  0.56 19.22 ?  152 TYR   A HE2  1 
ATOM   3368 H  HE2  B TYR   A 1 152 ? 14.866 -11.444 15.035  0.44 20.00 ?  152 TYR   A HE2  1 
ATOM   3369 H  HH   A TYR   A 1 152 ? 16.240 -13.393 16.010  0.56 22.44 ?  152 TYR   A HH   1 
ATOM   3370 H  HH   B TYR   A 1 152 ? 15.889 -13.112 16.127  0.44 23.09 ?  152 TYR   A HH   1 
ATOM   3371 N  N    A LEU   A 1 153 ? 15.776 -8.571  8.741   0.56 12.58 ?  153 LEU   A N    1 
ATOM   3372 N  N    B LEU   A 1 153 ? 15.751 -8.620  8.595   0.44 12.70 ?  153 LEU   A N    1 
ATOM   3373 C  CA   A LEU   A 1 153 ? 15.525 -7.656  7.640   0.56 12.45 ?  153 LEU   A CA   1 
ATOM   3374 C  CA   B LEU   A 1 153 ? 15.502 -7.735  7.463   0.44 12.13 ?  153 LEU   A CA   1 
ATOM   3375 C  C    A LEU   A 1 153 ? 14.550 -6.578  8.076   0.56 12.78 ?  153 LEU   A C    1 
ATOM   3376 C  C    B LEU   A 1 153 ? 14.479 -6.678  7.854   0.44 12.06 ?  153 LEU   A C    1 
ATOM   3377 O  O    A LEU   A 1 153 ? 13.479 -6.875  8.617   0.56 13.28 ?  153 LEU   A O    1 
ATOM   3378 O  O    B LEU   A 1 153 ? 13.349 -7.011  8.230   0.44 12.43 ?  153 LEU   A O    1 
ATOM   3379 C  CB   A LEU   A 1 153 ? 14.928 -8.405  6.451   0.56 12.76 ?  153 LEU   A CB   1 
ATOM   3380 C  CB   B LEU   A 1 153 ? 14.982 -8.546  6.277   0.44 12.11 ?  153 LEU   A CB   1 
ATOM   3381 C  CG   A LEU   A 1 153 ? 15.850 -9.382  5.722   0.56 12.87 ?  153 LEU   A CG   1 
ATOM   3382 C  CG   B LEU   A 1 153 ? 15.952 -9.586  5.713   0.44 12.33 ?  153 LEU   A CG   1 
ATOM   3383 C  CD1  A LEU   A 1 153 ? 15.019 -10.283 4.824   0.56 12.75 ?  153 LEU   A CD1  1 
ATOM   3384 C  CD1  B LEU   A 1 153 ? 15.267 -10.399 4.620   0.44 12.47 ?  153 LEU   A CD1  1 
ATOM   3385 C  CD2  A LEU   A 1 153 ? 16.905 -8.640  4.913   0.56 12.56 ?  153 LEU   A CD2  1 
ATOM   3386 C  CD2  B LEU   A 1 153 ? 17.218 -8.914  5.190   0.44 11.75 ?  153 LEU   A CD2  1 
ATOM   3387 H  H    A LEU   A 1 153 ? 15.202 -9.213  8.796   0.56 15.12 ?  153 LEU   A H    1 
ATOM   3388 H  H    B LEU   A 1 153 ? 15.204 -9.286  8.637   0.44 15.26 ?  153 LEU   A H    1 
ATOM   3389 H  HA   A LEU   A 1 153 ? 16.354 -7.243  7.375   0.56 14.97 ?  153 LEU   A HA   1 
ATOM   3390 H  HA   B LEU   A 1 153 ? 16.321 -7.295  7.207   0.44 14.57 ?  153 LEU   A HA   1 
ATOM   3391 H  HB2  A LEU   A 1 153 ? 14.161 -8.906  6.767   0.56 15.34 ?  153 LEU   A HB2  1 
ATOM   3392 H  HB2  B LEU   A 1 153 ? 14.180 -9.019  6.553   0.44 14.56 ?  153 LEU   A HB2  1 
ATOM   3393 H  HB3  A LEU   A 1 153 ? 14.636 -7.744  5.804   0.56 15.34 ?  153 LEU   A HB3  1 
ATOM   3394 H  HB3  B LEU   A 1 153 ? 14.765 -7.934  5.557   0.44 14.56 ?  153 LEU   A HB3  1 
ATOM   3395 H  HG   A LEU   A 1 153 ? 16.304 -9.938  6.378   0.56 15.47 ?  153 LEU   A HG   1 
ATOM   3396 H  HG   B LEU   A 1 153 ? 16.209 -10.197 6.424   0.44 14.82 ?  153 LEU   A HG   1 
ATOM   3397 H  HD11 A LEU   A 1 153 ? 15.610 -10.894 4.361   0.56 15.33 ?  153 LEU   A HD11 1 
ATOM   3398 H  HD11 B LEU   A 1 153 ? 15.747 -11.230 4.492   0.44 14.99 ?  153 LEU   A HD11 1 
ATOM   3399 H  HD12 A LEU   A 1 153 ? 14.387 -10.776 5.367   0.56 15.33 ?  153 LEU   A HD12 1 
ATOM   3400 H  HD12 B LEU   A 1 153 ? 14.354 -10.584 4.891   0.44 14.99 ?  153 LEU   A HD12 1 
ATOM   3401 H  HD13 A LEU   A 1 153 ? 14.544 -9.730  4.182   0.56 15.33 ?  153 LEU   A HD13 1 
ATOM   3402 H  HD13 B LEU   A 1 153 ? 15.266 -9.883  3.797   0.44 14.99 ?  153 LEU   A HD13 1 
ATOM   3403 H  HD21 A LEU   A 1 153 ? 17.453 -9.287  4.451   0.56 15.10 ?  153 LEU   A HD21 1 
ATOM   3404 H  HD21 B LEU   A 1 153 ? 17.769 -9.578  4.750   0.44 14.13 ?  153 LEU   A HD21 1 
ATOM   3405 H  HD22 A LEU   A 1 153 ? 16.453 -8.065  4.273   0.56 15.10 ?  153 LEU   A HD22 1 
ATOM   3406 H  HD22 B LEU   A 1 153 ? 16.969 -8.219  4.565   0.44 14.13 ?  153 LEU   A HD22 1 
ATOM   3407 H  HD23 A LEU   A 1 153 ? 17.444 -8.107  5.515   0.56 15.10 ?  153 LEU   A HD23 1 
ATOM   3408 H  HD23 B LEU   A 1 153 ? 17.703 -8.530  5.939   0.44 14.13 ?  153 LEU   A HD23 1 
ATOM   3409 N  N    A ALA   A 1 154 ? 14.928 -5.330  7.826   0.56 13.30 ?  154 ALA   A N    1 
ATOM   3410 N  N    B ALA   A 1 154 ? 14.870 -5.409  7.751   0.44 12.60 ?  154 ALA   A N    1 
ATOM   3411 C  CA   A ALA   A 1 154 ? 14.061 -4.179  8.014   0.56 13.58 ?  154 ALA   A CA   1 
ATOM   3412 C  CA   B ALA   A 1 154 ? 13.990 -4.281  8.027   0.44 13.07 ?  154 ALA   A CA   1 
ATOM   3413 C  C    A ALA   A 1 154 ? 13.582 -3.722  6.646   0.56 13.66 ?  154 ALA   A C    1 
ATOM   3414 C  C    B ALA   A 1 154 ? 13.538 -3.684  6.698   0.44 13.21 ?  154 ALA   A C    1 
ATOM   3415 O  O    A ALA   A 1 154 ? 14.395 -3.446  5.755   0.56 14.17 ?  154 ALA   A O    1 
ATOM   3416 O  O    B ALA   A 1 154 ? 14.357 -3.156  5.937   0.44 13.54 ?  154 ALA   A O    1 
ATOM   3417 C  CB   A ALA   A 1 154 ? 14.817 -3.046  8.703   0.56 13.98 ?  154 ALA   A CB   1 
ATOM   3418 C  CB   B ALA   A 1 154 ? 14.714 -3.238  8.882   0.44 13.39 ?  154 ALA   A CB   1 
ATOM   3419 H  H    A ALA   A 1 154 ? 15.707 -5.124  7.533   0.56 15.98 ?  154 ALA   A H    1 
ATOM   3420 H  H    B ALA   A 1 154 ? 15.663 -5.171  7.516   0.44 15.14 ?  154 ALA   A H    1 
ATOM   3421 H  HA   A ALA   A 1 154 ? 13.292 -4.425  8.552   0.56 16.32 ?  154 ALA   A HA   1 
ATOM   3422 H  HA   B ALA   A 1 154 ? 13.208 -4.583  8.515   0.44 15.70 ?  154 ALA   A HA   1 
ATOM   3423 H  HB1  A ALA   A 1 154 ? 14.216 -2.292  8.809   0.56 16.80 ?  154 ALA   A HB1  1 
ATOM   3424 H  HB1  B ALA   A 1 154 ? 14.113 -2.496  9.060   0.44 16.09 ?  154 ALA   A HB1  1 
ATOM   3425 H  HB2  A ALA   A 1 154 ? 15.122 -3.355  9.567   0.56 16.80 ?  154 ALA   A HB2  1 
ATOM   3426 H  HB2  B ALA   A 1 154 ? 14.986 -3.647  9.722   0.44 16.09 ?  154 ALA   A HB2  1 
ATOM   3427 H  HB3  A ALA   A 1 154 ? 15.572 -2.794  8.151   0.56 16.80 ?  154 ALA   A HB3  1 
ATOM   3428 H  HB3  B ALA   A 1 154 ? 15.497 -2.921  8.404   0.44 16.09 ?  154 ALA   A HB3  1 
ATOM   3429 N  N    A VAL   A 1 155 ? 12.266 -3.654  6.487   0.56 14.18 ?  155 VAL   A N    1 
ATOM   3430 N  N    B VAL   A 1 155 ? 12.237 -3.772  6.430   0.44 13.71 ?  155 VAL   A N    1 
ATOM   3431 C  CA   A VAL   A 1 155 ? 11.624 -3.161  5.277   0.56 14.98 ?  155 VAL   A CA   1 
ATOM   3432 C  CA   B VAL   A 1 155 ? 11.631 -3.347  5.171   0.44 13.93 ?  155 VAL   A CA   1 
ATOM   3433 C  C    A VAL   A 1 155 ? 10.909 -1.873  5.659   0.56 15.53 ?  155 VAL   A C    1 
ATOM   3434 C  C    B VAL   A 1 155 ? 10.909 -2.029  5.430   0.44 14.24 ?  155 VAL   A C    1 
ATOM   3435 O  O    A VAL   A 1 155 ? 9.968  -1.893  6.461   0.56 15.84 ?  155 VAL   A O    1 
ATOM   3436 O  O    B VAL   A 1 155 ? 9.913  -1.989  6.160   0.44 14.40 ?  155 VAL   A O    1 
ATOM   3437 C  CB   A VAL   A 1 155 ? 10.664 -4.204  4.688   0.56 15.24 ?  155 VAL   A CB   1 
ATOM   3438 C  CB   B VAL   A 1 155 ? 10.678 -4.419  4.619   0.44 13.92 ?  155 VAL   A CB   1 
ATOM   3439 C  CG1  A VAL   A 1 155 ? 9.941  -3.649  3.473   0.56 15.45 ?  155 VAL   A CG1  1 
ATOM   3440 C  CG1  B VAL   A 1 155 ? 9.986  -3.934  3.352   0.44 14.44 ?  155 VAL   A CG1  1 
ATOM   3441 C  CG2  A VAL   A 1 155 ? 11.440 -5.467  4.320   0.56 16.01 ?  155 VAL   A CG2  1 
ATOM   3442 C  CG2  B VAL   A 1 155 ? 11.435 -5.717  4.347   0.44 14.64 ?  155 VAL   A CG2  1 
ATOM   3443 H  H    A VAL   A 1 155 ? 11.701 -3.900  7.091   0.56 17.04 ?  155 VAL   A H    1 
ATOM   3444 H  H    B VAL   A 1 155 ? 11.664 -4.086  6.986   0.44 16.47 ?  155 VAL   A H    1 
ATOM   3445 H  HA   A VAL   A 1 155 ? 12.297 -2.956  4.613   0.56 17.99 ?  155 VAL   A HA   1 
ATOM   3446 H  HA   B VAL   A 1 155 ? 12.324 -3.192  4.512   0.44 16.74 ?  155 VAL   A HA   1 
ATOM   3447 H  HB   A VAL   A 1 155 ? 9.996  -4.439  5.357   0.56 18.31 ?  155 VAL   A HB   1 
ATOM   3448 H  HB   B VAL   A 1 155 ? 9.995  -4.609  5.282   0.44 16.72 ?  155 VAL   A HB   1 
ATOM   3449 H  HG11 A VAL   A 1 155 ? 9.451  -4.370  3.043   0.56 18.56 ?  155 VAL   A HG11 1 
ATOM   3450 H  HG11 B VAL   A 1 155 ? 9.549  -4.688  2.921   0.44 17.35 ?  155 VAL   A HG11 1 
ATOM   3451 H  HG12 A VAL   A 1 155 ? 9.321  -2.958  3.758   0.56 18.56 ?  155 VAL   A HG12 1 
ATOM   3452 H  HG12 B VAL   A 1 155 ? 9.322  -3.265  3.587   0.44 17.35 ?  155 VAL   A HG12 1 
ATOM   3453 H  HG13 A VAL   A 1 155 ? 10.592 -3.280  2.860   0.56 18.56 ?  155 VAL   A HG13 1 
ATOM   3454 H  HG13 B VAL   A 1 155 ? 10.646 -3.553  2.755   0.44 17.35 ?  155 VAL   A HG13 1 
ATOM   3455 H  HG21 A VAL   A 1 155 ? 10.838 -6.094  3.889   0.56 19.24 ?  155 VAL   A HG21 1 
ATOM   3456 H  HG21 B VAL   A 1 155 ? 10.825 -6.363  3.957   0.44 17.59 ?  155 VAL   A HG21 1 
ATOM   3457 H  HG22 A VAL   A 1 155 ? 12.158 -5.228  3.713   0.56 19.24 ?  155 VAL   A HG22 1 
ATOM   3458 H  HG22 B VAL   A 1 155 ? 12.162 -5.535  3.731   0.44 17.59 ?  155 VAL   A HG22 1 
ATOM   3459 H  HG23 A VAL   A 1 155 ? 11.806 -5.861  5.127   0.56 19.24 ?  155 VAL   A HG23 1 
ATOM   3460 H  HG23 B VAL   A 1 155 ? 11.788 -6.059  5.183   0.44 17.59 ?  155 VAL   A HG23 1 
ATOM   3461 N  N    A PHE   A 1 156 ? 11.373 -0.749  5.107   0.56 16.06 ?  156 PHE   A N    1 
ATOM   3462 N  N    B PHE   A 1 156 ? 11.405 -0.954  4.815   0.44 15.33 ?  156 PHE   A N    1 
ATOM   3463 C  CA   A PHE   A 1 156 ? 10.839 0.557   5.492   0.56 17.18 ?  156 PHE   A CA   1 
ATOM   3464 C  CA   B PHE   A 1 156 ? 10.913 0.397   5.087   0.44 16.13 ?  156 PHE   A CA   1 
ATOM   3465 C  C    A PHE   A 1 156 ? 9.386  0.721   5.059   0.56 17.52 ?  156 PHE   A C    1 
ATOM   3466 C  C    B PHE   A 1 156 ? 9.465  0.565   4.643   0.44 16.76 ?  156 PHE   A C    1 
ATOM   3467 O  O    A PHE   A 1 156 ? 8.557  1.241   5.818   0.56 18.02 ?  156 PHE   A O    1 
ATOM   3468 O  O    B PHE   A 1 156 ? 8.641  1.125   5.378   0.44 17.67 ?  156 PHE   A O    1 
ATOM   3469 C  CB   A PHE   A 1 156 ? 11.708 1.656   4.874   0.56 18.20 ?  156 PHE   A CB   1 
ATOM   3470 C  CB   B PHE   A 1 156 ? 11.840 1.385   4.362   0.44 15.60 ?  156 PHE   A CB   1 
ATOM   3471 C  CG   A PHE   A 1 156 ? 11.211 3.049   5.146   0.56 19.96 ?  156 PHE   A CG   1 
ATOM   3472 C  CG   B PHE   A 1 156 ? 11.559 2.857   4.623   0.44 15.58 ?  156 PHE   A CG   1 
ATOM   3473 C  CD1  A PHE   A 1 156 ? 11.131 3.516   6.444   0.56 20.53 ?  156 PHE   A CD1  1 
ATOM   3474 C  CD1  B PHE   A 1 156 ? 11.788 3.424   5.871   0.44 16.07 ?  156 PHE   A CD1  1 
ATOM   3475 C  CD2  A PHE   A 1 156 ? 10.828 3.889   4.108   0.56 21.00 ?  156 PHE   A CD2  1 
ATOM   3476 C  CD2  B PHE   A 1 156 ? 11.138 3.681   3.592   0.44 16.24 ?  156 PHE   A CD2  1 
ATOM   3477 C  CE1  A PHE   A 1 156 ? 10.676 4.791   6.709   0.56 21.16 ?  156 PHE   A CE1  1 
ATOM   3478 C  CE1  B PHE   A 1 156 ? 11.556 4.780   6.093   0.44 16.51 ?  156 PHE   A CE1  1 
ATOM   3479 C  CE2  A PHE   A 1 156 ? 10.372 5.172   4.366   0.56 21.55 ?  156 PHE   A CE2  1 
ATOM   3480 C  CE2  B PHE   A 1 156 ? 10.908 5.033   3.806   0.44 16.39 ?  156 PHE   A CE2  1 
ATOM   3481 C  CZ   A PHE   A 1 156 ? 10.300 5.624   5.668   0.56 21.50 ?  156 PHE   A CZ   1 
ATOM   3482 C  CZ   B PHE   A 1 156 ? 11.115 5.582   5.061   0.44 16.39 ?  156 PHE   A CZ   1 
ATOM   3483 H  H    A PHE   A 1 156 ? 12.002 -0.718  4.514   0.56 19.30 ?  156 PHE   A H    1 
ATOM   3484 H  H    B PHE   A 1 156 ? 12.034 -0.986  4.229   0.44 18.41 ?  156 PHE   A H    1 
ATOM   3485 H  HA   A PHE   A 1 156 ? 10.888 0.653   6.454   0.56 20.64 ?  156 PHE   A HA   1 
ATOM   3486 H  HA   B PHE   A 1 156 ? 10.964 0.569   6.037   0.44 19.38 ?  156 PHE   A HA   1 
ATOM   3487 H  HB2  A PHE   A 1 156 ? 12.611 1.592   5.232   0.56 21.86 ?  156 PHE   A HB2  1 
ATOM   3488 H  HB2  B PHE   A 1 156 ? 12.752 1.209   4.645   0.44 18.74 ?  156 PHE   A HB2  1 
ATOM   3489 H  HB3  A PHE   A 1 156 ? 11.735 1.536   3.910   0.56 21.86 ?  156 PHE   A HB3  1 
ATOM   3490 H  HB3  B PHE   A 1 156 ? 11.764 1.239   3.407   0.44 18.74 ?  156 PHE   A HB3  1 
ATOM   3491 H  HD1  A PHE   A 1 156 ? 11.385 2.961   7.146   0.56 24.65 ?  156 PHE   A HD1  1 
ATOM   3492 H  HD1  B PHE   A 1 156 ? 12.083 2.886   6.575   0.44 19.31 ?  156 PHE   A HD1  1 
ATOM   3493 H  HD2  A PHE   A 1 156 ? 10.883 3.586   3.229   0.56 25.22 ?  156 PHE   A HD2  1 
ATOM   3494 H  HD2  B PHE   A 1 156 ? 10.993 3.318   2.750   0.44 19.51 ?  156 PHE   A HD2  1 
ATOM   3495 H  HE1  A PHE   A 1 156 ? 10.628 5.092   7.588   0.56 25.42 ?  156 PHE   A HE1  1 
ATOM   3496 H  HE1  B PHE   A 1 156 ? 11.700 5.141   6.940   0.44 19.83 ?  156 PHE   A HE1  1 
ATOM   3497 H  HE2  A PHE   A 1 156 ? 10.122 5.725   3.663   0.56 25.88 ?  156 PHE   A HE2  1 
ATOM   3498 H  HE2  B PHE   A 1 156 ? 10.609 5.571   3.111   0.44 19.70 ?  156 PHE   A HE2  1 
ATOM   3499 H  HZ   A PHE   A 1 156 ? 9.993  6.481   5.848   0.56 25.83 ?  156 PHE   A HZ   1 
ATOM   3500 H  HZ   B PHE   A 1 156 ? 10.959 6.488   5.208   0.44 19.69 ?  156 PHE   A HZ   1 
ATOM   3501 N  N    A ASP   A 1 157 ? 9.068  0.304   3.840   0.56 17.09 ?  157 ASP   A N    1 
ATOM   3502 N  N    B ASP   A 1 157 ? 9.134  0.080   3.453   0.44 17.35 ?  157 ASP   A N    1 
ATOM   3503 C  CA   A ASP   A 1 157 ? 7.760  0.550   3.252   0.56 18.77 ?  157 ASP   A CA   1 
ATOM   3504 C  CA   B ASP   A 1 157 ? 7.861  0.383   2.818   0.44 17.45 ?  157 ASP   A CA   1 
ATOM   3505 C  C    A ASP   A 1 157 ? 6.774  -0.502  3.754   0.56 19.55 ?  157 ASP   A C    1 
ATOM   3506 C  C    B ASP   A 1 157 ? 6.785  -0.577  3.316   0.44 17.39 ?  157 ASP   A C    1 
ATOM   3507 O  O    A ASP   A 1 157 ? 6.965  -1.703  3.523   0.56 19.46 ?  157 ASP   A O    1 
ATOM   3508 O  O    B ASP   A 1 157 ? 6.886  -1.796  3.119   0.44 16.92 ?  157 ASP   A O    1 
ATOM   3509 C  CB   A ASP   A 1 157 ? 7.891  0.490   1.732   0.56 19.67 ?  157 ASP   A CB   1 
ATOM   3510 C  CB   B ASP   A 1 157 ? 8.019  0.294   1.304   0.44 17.89 ?  157 ASP   A CB   1 
ATOM   3511 C  CG   A ASP   A 1 157 ? 6.662  0.989   1.024   0.56 21.49 ?  157 ASP   A CG   1 
ATOM   3512 C  CG   B ASP   A 1 157 ? 6.853  0.893   0.569   0.44 18.40 ?  157 ASP   A CG   1 
ATOM   3513 O  OD1  A ASP   A 1 157 ? 6.484  2.218   0.946   0.56 22.13 ?  157 ASP   A OD1  1 
ATOM   3514 O  OD1  B ASP   A 1 157 ? 5.802  0.227   0.485   0.44 19.44 ?  157 ASP   A OD1  1 
ATOM   3515 O  OD2  A ASP   A 1 157 ? 5.868  0.151   0.553   0.56 22.53 -1 157 ASP   A OD2  1 
ATOM   3516 O  OD2  B ASP   A 1 157 ? 6.976  2.040   0.103   0.44 17.79 -1 157 ASP   A OD2  1 
ATOM   3517 H  H    A ASP   A 1 157 ? 9.607  -0.131  3.327   0.56 20.53 ?  157 ASP   A H    1 
ATOM   3518 H  H    B ASP   A 1 157 ? 9.642  -0.436  2.987   0.44 20.84 ?  157 ASP   A H    1 
ATOM   3519 H  HA   A ASP   A 1 157 ? 7.448  1.438   3.504   0.56 22.54 ?  157 ASP   A HA   1 
ATOM   3520 H  HA   B ASP   A 1 157 ? 7.595  1.288   3.050   0.44 20.96 ?  157 ASP   A HA   1 
ATOM   3521 H  HB2  A ASP   A 1 157 ? 8.656  1.025   1.454   0.56 23.62 ?  157 ASP   A HB2  1 
ATOM   3522 H  HB2  B ASP   A 1 157 ? 8.824  0.769   1.046   0.44 21.49 ?  157 ASP   A HB2  1 
ATOM   3523 H  HB3  A ASP   A 1 157 ? 8.022  -0.427  1.460   0.56 23.62 ?  157 ASP   A HB3  1 
ATOM   3524 H  HB3  B ASP   A 1 157 ? 8.089  -0.641  1.054   0.44 21.49 ?  157 ASP   A HB3  1 
ATOM   3525 N  N    A LYS   A 1 158 ? 5.727  -0.053  4.452   0.56 20.68 ?  158 LYS   A N    1 
ATOM   3526 N  N    B LYS   A 1 158 ? 5.755  -0.021  3.959   0.44 18.20 ?  158 LYS   A N    1 
ATOM   3527 C  CA   A LYS   A 1 158 ? 4.752  -0.995  4.995   0.56 21.59 ?  158 LYS   A CA   1 
ATOM   3528 C  CA   B LYS   A 1 158 ? 4.694  -0.845  4.525   0.44 18.76 ?  158 LYS   A CA   1 
ATOM   3529 C  C    A LYS   A 1 158 ? 4.014  -1.726  3.884   0.56 21.23 ?  158 LYS   A C    1 
ATOM   3530 C  C    B LYS   A 1 158 ? 4.048  -1.715  3.453   0.44 18.55 ?  158 LYS   A C    1 
ATOM   3531 O  O    A LYS   A 1 158 ? 3.802  -2.942  3.966   0.56 21.98 ?  158 LYS   A O    1 
ATOM   3532 O  O    B LYS   A 1 158 ? 3.814  -2.911  3.661   0.44 18.78 ?  158 LYS   A O    1 
ATOM   3533 C  CB   A LYS   A 1 158 ? 3.768  -0.273  5.917   0.56 22.95 ?  158 LYS   A CB   1 
ATOM   3534 C  CB   B LYS   A 1 158 ? 3.646  0.047   5.198   0.44 19.84 ?  158 LYS   A CB   1 
ATOM   3535 C  CG   A LYS   A 1 158 ? 2.529  -1.092  6.298   0.56 24.67 ?  158 LYS   A CG   1 
ATOM   3536 C  CG   B LYS   A 1 158 ? 2.452  -0.723  5.741   0.44 20.89 ?  158 LYS   A CG   1 
ATOM   3537 C  CD   A LYS   A 1 158 ? 2.866  -2.382  7.051   0.56 25.68 ?  158 LYS   A CD   1 
ATOM   3538 C  CD   B LYS   A 1 158 ? 1.254  0.170   5.989   0.44 22.12 ?  158 LYS   A CD   1 
ATOM   3539 C  CE   A LYS   A 1 158 ? 1.592  -3.045  7.590   0.56 25.94 ?  158 LYS   A CE   1 
ATOM   3540 C  CE   B LYS   A 1 158 ? 0.117  -0.608  6.635   0.44 22.70 ?  158 LYS   A CE   1 
ATOM   3541 N  NZ   A LYS   A 1 158 ? 1.805  -4.422  8.130   0.56 25.90 ?  158 LYS   A NZ   1 
ATOM   3542 N  NZ   B LYS   A 1 158 ? -0.278 -1.807  5.843   0.44 22.91 ?  158 LYS   A NZ   1 
ATOM   3543 H  H    A LYS   A 1 158 ? 5.572  0.777   4.623   0.56 24.83 ?  158 LYS   A H    1 
ATOM   3544 H  H    B LYS   A 1 158 ? 5.651  0.826   4.078   0.44 21.86 ?  158 LYS   A H    1 
ATOM   3545 H  HA   A LYS   A 1 158 ? 5.224  -1.654  5.522   0.56 25.93 ?  158 LYS   A HA   1 
ATOM   3546 H  HA   B LYS   A 1 158 ? 5.066  -1.427  5.205   0.44 22.54 ?  158 LYS   A HA   1 
ATOM   3547 H  HB2  A LYS   A 1 158 ? 4.229  -0.040  6.738   0.56 27.56 ?  158 LYS   A HB2  1 
ATOM   3548 H  HB2  B LYS   A 1 158 ? 4.061  0.516   5.946   0.44 23.83 ?  158 LYS   A HB2  1 
ATOM   3549 H  HB3  A LYS   A 1 158 ? 3.463  0.534   5.475   0.56 27.56 ?  158 LYS   A HB3  1 
ATOM   3550 H  HB3  B LYS   A 1 158 ? 3.318  0.694   4.553   0.44 23.83 ?  158 LYS   A HB3  1 
ATOM   3551 H  HG2  A LYS   A 1 158 ? 1.968  -0.553  6.877   0.56 29.62 ?  158 LYS   A HG2  1 
ATOM   3552 H  HG2  B LYS   A 1 158 ? 2.182  -1.404  5.107   0.44 25.09 ?  158 LYS   A HG2  1 
ATOM   3553 H  HG3  A LYS   A 1 158 ? 2.033  -1.329  5.498   0.56 29.62 ?  158 LYS   A HG3  1 
ATOM   3554 H  HG3  B LYS   A 1 158 ? 2.702  -1.134  6.581   0.44 25.09 ?  158 LYS   A HG3  1 
ATOM   3555 H  HD2  A LYS   A 1 158 ? 3.301  -3.006  6.451   0.56 30.84 ?  158 LYS   A HD2  1 
ATOM   3556 H  HD2  B LYS   A 1 158 ? 1.509  0.891   6.584   0.44 26.56 ?  158 LYS   A HD2  1 
ATOM   3557 H  HD3  A LYS   A 1 158 ? 3.443  -2.177  7.803   0.56 30.84 ?  158 LYS   A HD3  1 
ATOM   3558 H  HD3  B LYS   A 1 158 ? 0.939  0.527   5.142   0.44 26.56 ?  158 LYS   A HD3  1 
ATOM   3559 H  HE2  A LYS   A 1 158 ? 1.233  -2.499  8.308   0.56 31.15 ?  158 LYS   A HE2  1 
ATOM   3560 H  HE2  B LYS   A 1 158 ? 0.398  -0.908  7.513   0.44 27.26 ?  158 LYS   A HE2  1 
ATOM   3561 H  HE3  A LYS   A 1 158 ? 0.945  -3.108  6.873   0.56 31.15 ?  158 LYS   A HE3  1 
ATOM   3562 H  HE3  B LYS   A 1 158 ? -0.658 -0.031  6.711   0.44 27.26 ?  158 LYS   A HE3  1 
ATOM   3563 H  HZ1  A LYS   A 1 158 ? 1.034  -4.756  8.429   0.56 31.10 ?  158 LYS   A HZ1  1 
ATOM   3564 H  HZ1  B LYS   A 1 158 ? -0.976 -2.209  6.224   0.44 27.52 ?  158 LYS   A HZ1  1 
ATOM   3565 H  HZ2  A LYS   A 1 158 ? 2.119  -4.955  7.490   0.56 31.10 ?  158 LYS   A HZ2  1 
ATOM   3566 H  HZ2  B LYS   A 1 158 ? -0.500 -1.567  5.015   0.44 27.52 ?  158 LYS   A HZ2  1 
ATOM   3567 H  HZ3  A LYS   A 1 158 ? 2.388  -4.402  8.802   0.56 31.10 ?  158 LYS   A HZ3  1 
ATOM   3568 H  HZ3  B LYS   A 1 158 ? 0.400  -2.385  5.803   0.44 27.52 ?  158 LYS   A HZ3  1 
ATOM   3569 N  N    A ASN   A 1 159 ? 3.596  -1.005  2.843   0.56 20.69 ?  159 ASN   A N    1 
ATOM   3570 N  N    B ASN   A 1 159 ? 3.742  -1.128  2.297   0.44 19.22 ?  159 ASN   A N    1 
ATOM   3571 C  CA   A ASN   A 1 159 ? 2.949  -1.682  1.727   0.56 20.41 ?  159 ASN   A CA   1 
ATOM   3572 C  CA   B ASN   A 1 159 ? 3.017  -1.876  1.276   0.44 19.56 ?  159 ASN   A CA   1 
ATOM   3573 C  C    A ASN   A 1 159 ? 3.870  -2.734  1.122   0.56 19.26 ?  159 ASN   A C    1 
ATOM   3574 C  C    B ASN   A 1 159 ? 3.860  -3.016  0.701   0.44 18.69 ?  159 ASN   A C    1 
ATOM   3575 O  O    A ASN   A 1 159 ? 3.431  -3.845  0.803   0.56 18.23 ?  159 ASN   A O    1 
ATOM   3576 O  O    B ASN   A 1 159 ? 3.342  -4.108  0.437   0.44 18.92 ?  159 ASN   A O    1 
ATOM   3577 C  CB   A ASN   A 1 159 ? 2.466  -0.668  0.686   0.56 22.02 ?  159 ASN   A CB   1 
ATOM   3578 C  CB   B ASN   A 1 159 ? 2.501  -0.914  0.199   0.44 21.16 ?  159 ASN   A CB   1 
ATOM   3579 C  CG   A ASN   A 1 159 ? 1.162  0.016   1.094   0.56 24.27 ?  159 ASN   A CG   1 
ATOM   3580 C  CG   B ASN   A 1 159 ? 1.430  0.042   0.726   0.44 23.06 ?  159 ASN   A CG   1 
ATOM   3581 O  OD1  A ASN   A 1 159 ? 0.319  -0.579  1.763   0.56 25.74 ?  159 ASN   A OD1  1 
ATOM   3582 O  OD1  B ASN   A 1 159 ? 1.357  1.203   0.310   0.44 24.28 ?  159 ASN   A OD1  1 
ATOM   3583 N  ND2  A ASN   A 1 159 ? 0.995  1.267   0.690   0.56 24.97 ?  159 ASN   A ND2  1 
ATOM   3584 N  ND2  B ASN   A 1 159 ? 0.593  -0.446  1.645   0.44 23.90 ?  159 ASN   A ND2  1 
ATOM   3585 H  H    A ASN   A 1 159 ? 3.679  -0.153  2.757   0.56 24.85 ?  159 ASN   A H    1 
ATOM   3586 H  H    B ASN   A 1 159 ? 3.944  -0.315  2.089   0.44 23.09 ?  159 ASN   A H    1 
ATOM   3587 H  HA   A ASN   A 1 159 ? 2.172  -2.148  2.059   0.56 24.52 ?  159 ASN   A HA   1 
ATOM   3588 H  HA   B ASN   A 1 159 ? 2.252  -2.289  1.690   0.44 23.50 ?  159 ASN   A HA   1 
ATOM   3589 H  HB2  A ASN   A 1 159 ? 3.139  0.021   0.574   0.56 26.45 ?  159 ASN   A HB2  1 
ATOM   3590 H  HB2  B ASN   A 1 159 ? 3.229  -0.363  -0.128  0.44 25.42 ?  159 ASN   A HB2  1 
ATOM   3591 H  HB3  A ASN   A 1 159 ? 2.314  -1.125  -0.157  0.56 26.45 ?  159 ASN   A HB3  1 
ATOM   3592 H  HB3  B ASN   A 1 159 ? 2.108  -1.417  -0.526  0.44 25.42 ?  159 ASN   A HB3  1 
ATOM   3593 H  HD21 A ASN   A 1 159 ? 0.278  1.687   0.898   0.56 29.98 ?  159 ASN   A HD21 1 
ATOM   3594 H  HD21 B ASN   A 1 159 ? -0.030 0.047   1.971   0.44 28.71 ?  159 ASN   A HD21 1 
ATOM   3595 H  HD22 A ASN   A 1 159 ? 1.607  1.651   0.228   0.56 29.98 ?  159 ASN   A HD22 1 
ATOM   3596 H  HD22 B ASN   A 1 159 ? 0.668  -1.262  1.917   0.44 28.71 ?  159 ASN   A HD22 1 
ATOM   3597 N  N    A LEU   A 1 160 ? 5.160  -2.424  0.989   0.56 18.54 ?  160 LEU   A N    1 
ATOM   3598 N  N    B LEU   A 1 160 ? 5.165  -2.803  0.537   0.44 16.90 ?  160 LEU   A N    1 
ATOM   3599 C  CA   A LEU   A 1 160 ? 6.085  -3.439  0.494   0.56 17.58 ?  160 LEU   A CA   1 
ATOM   3600 C  CA   B LEU   A 1 160 ? 6.023  -3.855  -0.003  0.44 15.54 ?  160 LEU   A CA   1 
ATOM   3601 C  C    A LEU   A 1 160 ? 6.223  -4.586  1.487   0.56 16.28 ?  160 LEU   A C    1 
ATOM   3602 C  C    B LEU   A 1 160 ? 6.151  -5.016  0.974   0.44 14.42 ?  160 LEU   A C    1 
ATOM   3603 O  O    A LEU   A 1 160 ? 6.234  -5.758  1.092   0.56 16.57 ?  160 LEU   A O    1 
ATOM   3604 O  O    B LEU   A 1 160 ? 6.147  -6.186  0.570   0.44 14.84 ?  160 LEU   A O    1 
ATOM   3605 C  CB   A LEU   A 1 160 ? 7.447  -2.824  0.178   0.56 17.90 ?  160 LEU   A CB   1 
ATOM   3606 C  CB   B LEU   A 1 160 ? 7.405  -3.279  -0.302  0.44 15.40 ?  160 LEU   A CB   1 
ATOM   3607 C  CG   A LEU   A 1 160 ? 8.471  -3.857  -0.297  0.56 18.45 ?  160 LEU   A CG   1 
ATOM   3608 C  CG   B LEU   A 1 160 ? 8.484  -4.309  -0.649  0.44 15.99 ?  160 LEU   A CG   1 
ATOM   3609 C  CD1  A LEU   A 1 160 ? 7.952  -4.612  -1.507  0.56 19.02 ?  160 LEU   A CD1  1 
ATOM   3610 C  CD1  B LEU   A 1 160 ? 8.089  -5.056  -1.908  0.44 16.62 ?  160 LEU   A CD1  1 
ATOM   3611 C  CD2  A LEU   A 1 160 ? 9.791  -3.191  -0.613  0.56 18.54 ?  160 LEU   A CD2  1 
ATOM   3612 C  CD2  B LEU   A 1 160 ? 9.856  -3.658  -0.799  0.44 16.45 ?  160 LEU   A CD2  1 
ATOM   3613 H  H    A LEU   A 1 160 ? 5.517  -1.657  1.174   0.56 22.28 ?  160 LEU   A H    1 
ATOM   3614 H  H    B LEU   A 1 160 ? 5.576  -2.079  0.753   0.44 20.31 ?  160 LEU   A H    1 
ATOM   3615 H  HA   A LEU   A 1 160 ? 5.727  -3.793  -0.331  0.56 21.12 ?  160 LEU   A HA   1 
ATOM   3616 H  HA   B LEU   A 1 160 ? 5.642  -4.183  -0.833  0.44 18.67 ?  160 LEU   A HA   1 
ATOM   3617 H  HB2  A LEU   A 1 160 ? 7.350  -2.148  -0.521  0.56 21.51 ?  160 LEU   A HB2  1 
ATOM   3618 H  HB2  B LEU   A 1 160 ? 7.330  -2.668  -1.054  0.44 18.50 ?  160 LEU   A HB2  1 
ATOM   3619 H  HB3  A LEU   A 1 160 ? 7.801  -2.419  0.981   0.56 21.51 ?  160 LEU   A HB3  1 
ATOM   3620 H  HB3  B LEU   A 1 160 ? 7.709  -2.790  0.480   0.44 18.50 ?  160 LEU   A HB3  1 
ATOM   3621 H  HG   A LEU   A 1 160 ? 8.628  -4.497  0.414   0.56 22.16 ?  160 LEU   A HG   1 
ATOM   3622 H  HG   B LEU   A 1 160 ? 8.552  -4.952  0.070   0.44 19.21 ?  160 LEU   A HG   1 
ATOM   3623 H  HD11 A LEU   A 1 160 ? 8.674  -5.138  -1.880  0.56 22.85 ?  160 LEU   A HD11 1 
ATOM   3624 H  HD11 B LEU   A 1 160 ? 8.813  -5.642  -2.164  0.44 19.97 ?  160 LEU   A HD11 1 
ATOM   3625 H  HD12 A LEU   A 1 160 ? 7.228  -5.197  -1.232  0.56 22.85 ?  160 LEU   A HD12 1 
ATOM   3626 H  HD12 B LEU   A 1 160 ? 7.288  -5.575  -1.727  0.44 19.97 ?  160 LEU   A HD12 1 
ATOM   3627 H  HD13 A LEU   A 1 160 ? 7.632  -3.975  -2.165  0.56 22.85 ?  160 LEU   A HD13 1 
ATOM   3628 H  HD13 B LEU   A 1 160 ? 7.913  -4.413  -2.613  0.44 19.97 ?  160 LEU   A HD13 1 
ATOM   3629 H  HD21 A LEU   A 1 160 ? 10.423 -3.869  -0.903  0.56 22.27 ?  160 LEU   A HD21 1 
ATOM   3630 H  HD21 B LEU   A 1 160 ? 10.508 -4.344  -1.017  0.44 19.76 ?  160 LEU   A HD21 1 
ATOM   3631 H  HD22 A LEU   A 1 160 ? 9.655  -2.542  -1.321  0.56 22.27 ?  160 LEU   A HD22 1 
ATOM   3632 H  HD22 B LEU   A 1 160 ? 9.821  -2.999  -1.510  0.44 19.76 ?  160 LEU   A HD22 1 
ATOM   3633 H  HD23 A LEU   A 1 160 ? 10.122 -2.750  0.184   0.56 22.27 ?  160 LEU   A HD23 1 
ATOM   3634 H  HD23 B LEU   A 1 160 ? 10.099 -3.228  0.037   0.44 19.76 ?  160 LEU   A HD23 1 
ATOM   3635 N  N    A TYR   A 1 161 ? 6.332  -4.271  2.778   0.56 15.44 ?  161 TYR   A N    1 
ATOM   3636 N  N    B TYR   A 1 161 ? 6.300  -4.704  2.260   0.44 13.83 ?  161 TYR   A N    1 
ATOM   3637 C  CA   A TYR   A 1 161 ? 6.424  -5.317  3.789   0.56 15.25 ?  161 TYR   A CA   1 
ATOM   3638 C  CA   B TYR   A 1 161 ? 6.393  -5.739  3.280   0.44 13.98 ?  161 TYR   A CA   1 
ATOM   3639 C  C    A TYR   A 1 161 ? 5.270  -6.302  3.671   0.56 16.56 ?  161 TYR   A C    1 
ATOM   3640 C  C    B TYR   A 1 161 ? 5.198  -6.675  3.217   0.44 14.72 ?  161 TYR   A C    1 
ATOM   3641 O  O    A TYR   A 1 161 ? 5.470  -7.523  3.725   0.56 15.47 ?  161 TYR   A O    1 
ATOM   3642 O  O    B TYR   A 1 161 ? 5.357  -7.901  3.178   0.44 14.14 ?  161 TYR   A O    1 
ATOM   3643 C  CB   A TYR   A 1 161 ? 6.465  -4.699  5.187   0.56 15.34 ?  161 TYR   A CB   1 
ATOM   3644 C  CB   B TYR   A 1 161 ? 6.469  -5.089  4.656   0.44 13.66 ?  161 TYR   A CB   1 
ATOM   3645 C  CG   A TYR   A 1 161 ? 6.367  -5.731  6.285   0.56 15.11 ?  161 TYR   A CG   1 
ATOM   3646 C  CG   B TYR   A 1 161 ? 6.356  -6.085  5.773   0.44 13.36 ?  161 TYR   A CG   1 
ATOM   3647 C  CD1  A TYR   A 1 161 ? 7.489  -6.418  6.723   0.56 14.45 ?  161 TYR   A CD1  1 
ATOM   3648 C  CD1  B TYR   A 1 161 ? 7.458  -6.815  6.180   0.44 13.42 ?  161 TYR   A CD1  1 
ATOM   3649 C  CD2  A TYR   A 1 161 ? 5.147  -6.023  6.879   0.56 15.40 ?  161 TYR   A CD2  1 
ATOM   3650 C  CD2  B TYR   A 1 161 ? 5.142  -6.309  6.415   0.44 14.02 ?  161 TYR   A CD2  1 
ATOM   3651 C  CE1  A TYR   A 1 161 ? 7.400  -7.369  7.720   0.56 14.99 ?  161 TYR   A CE1  1 
ATOM   3652 C  CE1  B TYR   A 1 161 ? 7.366  -7.736  7.193   0.44 13.14 ?  161 TYR   A CE1  1 
ATOM   3653 C  CE2  A TYR   A 1 161 ? 5.046  -6.973  7.879   0.56 15.76 ?  161 TYR   A CE2  1 
ATOM   3654 C  CE2  B TYR   A 1 161 ? 5.038  -7.234  7.435   0.44 13.78 ?  161 TYR   A CE2  1 
ATOM   3655 C  CZ   A TYR   A 1 161 ? 6.177  -7.642  8.299   0.56 15.52 ?  161 TYR   A CZ   1 
ATOM   3656 C  CZ   B TYR   A 1 161 ? 6.158  -7.946  7.820   0.44 13.43 ?  161 TYR   A CZ   1 
ATOM   3657 O  OH   A TYR   A 1 161 ? 6.084  -8.586  9.296   0.56 16.35 ?  161 TYR   A OH   1 
ATOM   3658 O  OH   B TYR   A 1 161 ? 6.080  -8.869  8.834   0.44 13.77 ?  161 TYR   A OH   1 
ATOM   3659 H  H    A TYR   A 1 161 ? 6.354  -3.467  3.086   0.56 18.55 ?  161 TYR   A H    1 
ATOM   3660 H  H    B TYR   A 1 161 ? 6.348  -3.909  2.562   0.44 16.62 ?  161 TYR   A H    1 
ATOM   3661 H  HA   A TYR   A 1 161 ? 7.242  -5.810  3.656   0.56 18.33 ?  161 TYR   A HA   1 
ATOM   3662 H  HA   B TYR   A 1 161 ? 7.197  -6.267  3.141   0.44 16.79 ?  161 TYR   A HA   1 
ATOM   3663 H  HB2  A TYR   A 1 161 ? 7.303  -4.219  5.294   0.56 18.43 ?  161 TYR   A HB2  1 
ATOM   3664 H  HB2  B TYR   A 1 161 ? 7.322  -4.636  4.742   0.44 16.41 ?  161 TYR   A HB2  1 
ATOM   3665 H  HB3  A TYR   A 1 161 ? 5.720  -4.079  5.281   0.56 18.43 ?  161 TYR   A HB3  1 
ATOM   3666 H  HB3  B TYR   A 1 161 ? 5.744  -4.451  4.743   0.44 16.41 ?  161 TYR   A HB3  1 
ATOM   3667 H  HD1  A TYR   A 1 161 ? 8.316  -6.232  6.339   0.56 17.36 ?  161 TYR   A HD1  1 
ATOM   3668 H  HD1  B TYR   A 1 161 ? 8.273  -6.684  5.757   0.44 16.12 ?  161 TYR   A HD1  1 
ATOM   3669 H  HD2  A TYR   A 1 161 ? 4.377  -5.576  6.597   0.56 18.51 ?  161 TYR   A HD2  1 
ATOM   3670 H  HD2  B TYR   A 1 161 ? 4.386  -5.829  6.157   0.44 16.85 ?  161 TYR   A HD2  1 
ATOM   3671 H  HE1  A TYR   A 1 161 ? 8.162  -7.818  8.008   0.56 18.02 ?  161 TYR   A HE1  1 
ATOM   3672 H  HE1  B TYR   A 1 161 ? 8.112  -8.224  7.454   0.44 15.80 ?  161 TYR   A HE1  1 
ATOM   3673 H  HE2  A TYR   A 1 161 ? 4.217  -7.159  8.265   0.56 18.94 ?  161 TYR   A HE2  1 
ATOM   3674 H  HE2  B TYR   A 1 161 ? 4.218  -7.373  7.861   0.44 16.56 ?  161 TYR   A HE2  1 
ATOM   3675 H  HH   A TYR   A 1 161 ? 5.278  -8.653  9.550   0.56 19.64 ?  161 TYR   A HH   1 
ATOM   3676 H  HH   B TYR   A 1 161 ? 5.285  -8.904  9.131   0.44 16.54 ?  161 TYR   A HH   1 
ATOM   3677 N  N    A ASP   A 1 162 ? 4.047  -5.788  3.508   0.56 18.27 ?  162 ASP   A N    1 
ATOM   3678 N  N    B ASP   A 1 162 ? 3.987  -6.107  3.249   0.44 16.52 ?  162 ASP   A N    1 
ATOM   3679 C  CA   A ASP   A 1 162 ? 2.891  -6.681  3.462   0.56 19.21 ?  162 ASP   A CA   1 
ATOM   3680 C  CA   B ASP   A 1 162 ? 2.776  -6.907  3.089   0.44 18.06 ?  162 ASP   A CA   1 
ATOM   3681 C  C    A ASP   A 1 162 ? 2.932  -7.584  2.237   0.56 19.26 ?  162 ASP   A C    1 
ATOM   3682 C  C    B ASP   A 1 162 ? 2.862  -7.741  1.821   0.44 18.36 ?  162 ASP   A C    1 
ATOM   3683 O  O    A ASP   A 1 162 ? 2.567  -8.765  2.317   0.56 20.11 ?  162 ASP   A O    1 
ATOM   3684 O  O    B ASP   A 1 162 ? 2.498  -8.924  1.810   0.44 18.62 ?  162 ASP   A O    1 
ATOM   3685 C  CB   A ASP   A 1 162 ? 1.586  -5.884  3.510   0.56 20.16 ?  162 ASP   A CB   1 
ATOM   3686 C  CB   B ASP   A 1 162 ? 1.552  -5.983  3.030   0.44 19.79 ?  162 ASP   A CB   1 
ATOM   3687 C  CG   A ASP   A 1 162 ? 1.257  -5.386  4.896   0.56 20.96 ?  162 ASP   A CG   1 
ATOM   3688 C  CG   B ASP   A 1 162 ? 1.318  -5.229  4.325   0.44 20.95 ?  162 ASP   A CG   1 
ATOM   3689 O  OD1  A ASP   A 1 162 ? 1.924  -5.809  5.863   0.56 21.82 ?  162 ASP   A OD1  1 
ATOM   3690 O  OD1  B ASP   A 1 162 ? 1.855  -5.654  5.367   0.44 21.69 ?  162 ASP   A OD1  1 
ATOM   3691 O  OD2  A ASP   A 1 162 ? 0.322  -4.569  5.011   0.56 21.34 -1 162 ASP   A OD2  1 
ATOM   3692 O  OD2  B ASP   A 1 162 ? 0.571  -4.225  4.306   0.44 21.23 -1 162 ASP   A OD2  1 
ATOM   3693 H  H    A ASP   A 1 162 ? 3.859  -4.937  3.430   0.56 21.95 ?  162 ASP   A H    1 
ATOM   3694 H  H    B ASP   A 1 162 ? 3.846  -5.267  3.364   0.44 19.85 ?  162 ASP   A H    1 
ATOM   3695 H  HA   A ASP   A 1 162 ? 2.913  -7.246  4.242   0.56 23.07 ?  162 ASP   A HA   1 
ATOM   3696 H  HA   B ASP   A 1 162 ? 2.665  -7.498  3.850   0.44 21.70 ?  162 ASP   A HA   1 
ATOM   3697 H  HB2  A ASP   A 1 162 ? 1.654  -5.107  2.938   0.56 24.21 ?  162 ASP   A HB2  1 
ATOM   3698 H  HB2  B ASP   A 1 162 ? 1.668  -5.335  2.312   0.44 23.77 ?  162 ASP   A HB2  1 
ATOM   3699 H  HB3  A ASP   A 1 162 ? 0.855  -6.452  3.217   0.56 24.21 ?  162 ASP   A HB3  1 
ATOM   3700 H  HB3  B ASP   A 1 162 ? 0.752  -6.504  2.874   0.44 23.77 ?  162 ASP   A HB3  1 
ATOM   3701 N  N    A LYS   A 1 163 ? 3.378  -7.055  1.094   0.56 20.07 ?  163 LYS   A N    1 
ATOM   3702 N  N    B LYS   A 1 163 ? 3.349  -7.132  0.740   0.44 19.46 ?  163 LYS   A N    1 
ATOM   3703 C  CA   A LYS   A 1 163 ? 3.419  -7.875  -0.112  0.56 20.62 ?  163 LYS   A CA   1 
ATOM   3704 C  CA   B LYS   A 1 163 ? 3.508  -7.851  -0.517  0.44 20.27 ?  163 LYS   A CA   1 
ATOM   3705 C  C    A LYS   A 1 163 ? 4.501  -8.949  -0.015  0.56 20.26 ?  163 LYS   A C    1 
ATOM   3706 C  C    B LYS   A 1 163 ? 4.544  -8.965  -0.393  0.44 19.20 ?  163 LYS   A C    1 
ATOM   3707 O  O    A LYS   A 1 163 ? 4.314  -10.077 -0.487  0.56 20.53 ?  163 LYS   A O    1 
ATOM   3708 O  O    B LYS   A 1 163 ? 4.354  -10.064 -0.928  0.44 19.44 ?  163 LYS   A O    1 
ATOM   3709 C  CB   A LYS   A 1 163 ? 3.626  -6.990  -1.344  0.56 23.15 ?  163 LYS   A CB   1 
ATOM   3710 C  CB   B LYS   A 1 163 ? 3.905  -6.860  -1.610  0.44 22.58 ?  163 LYS   A CB   1 
ATOM   3711 C  CG   A LYS   A 1 163 ? 3.723  -7.763  -2.653  0.56 26.19 ?  163 LYS   A CG   1 
ATOM   3712 C  CG   B LYS   A 1 163 ? 4.087  -7.479  -2.976  0.44 25.19 ?  163 LYS   A CG   1 
ATOM   3713 C  CD   A LYS   A 1 163 ? 4.063  -6.840  -3.810  0.56 29.28 ?  163 LYS   A CD   1 
ATOM   3714 C  CD   B LYS   A 1 163 ? 4.538  -6.434  -3.979  0.44 27.64 ?  163 LYS   A CD   1 
ATOM   3715 C  CE   A LYS   A 1 163 ? 3.999  -7.565  -5.143  0.56 31.39 ?  163 LYS   A CE   1 
ATOM   3716 C  CE   B LYS   A 1 163 ? 4.699  -7.028  -5.365  0.44 29.45 ?  163 LYS   A CE   1 
ATOM   3717 N  NZ   A LYS   A 1 163 ? 4.645  -6.777  -6.231  0.56 32.81 ?  163 LYS   A NZ   1 
ATOM   3718 N  NZ   B LYS   A 1 163 ? 5.315  -6.059  -6.310  0.44 30.56 ?  163 LYS   A NZ   1 
ATOM   3719 H  H    A LYS   A 1 163 ? 3.664  -6.237  0.996   0.56 24.10 ?  163 LYS   A H    1 
ATOM   3720 H  H    B LYS   A 1 163 ? 3.585  -6.300  0.714   0.44 23.37 ?  163 LYS   A H    1 
ATOM   3721 H  HA   A LYS   A 1 163 ? 2.560  -8.311  -0.208  0.56 24.77 ?  163 LYS   A HA   1 
ATOM   3722 H  HA   B LYS   A 1 163 ? 2.656  -8.243  -0.761  0.44 24.34 ?  163 LYS   A HA   1 
ATOM   3723 H  HB2  A LYS   A 1 163 ? 2.872  -6.374  -1.423  0.56 27.81 ?  163 LYS   A HB2  1 
ATOM   3724 H  HB2  B LYS   A 1 163 ? 3.211  -6.181  -1.684  0.44 27.12 ?  163 LYS   A HB2  1 
ATOM   3725 H  HB3  A LYS   A 1 163 ? 4.444  -6.483  -1.237  0.56 27.81 ?  163 LYS   A HB3  1 
ATOM   3726 H  HB3  B LYS   A 1 163 ? 4.742  -6.439  -1.363  0.44 27.12 ?  163 LYS   A HB3  1 
ATOM   3727 H  HG2  A LYS   A 1 163 ? 4.423  -8.430  -2.587  0.56 31.45 ?  163 LYS   A HG2  1 
ATOM   3728 H  HG2  B LYS   A 1 163 ? 4.765  -8.170  -2.929  0.44 30.25 ?  163 LYS   A HG2  1 
ATOM   3729 H  HG3  A LYS   A 1 163 ? 2.870  -8.187  -2.842  0.56 31.45 ?  163 LYS   A HG3  1 
ATOM   3730 H  HG3  B LYS   A 1 163 ? 3.242  -7.851  -3.275  0.44 30.25 ?  163 LYS   A HG3  1 
ATOM   3731 H  HD2  A LYS   A 1 163 ? 3.428  -6.108  -3.835  0.56 35.16 ?  163 LYS   A HD2  1 
ATOM   3732 H  HD2  B LYS   A 1 163 ? 3.874  -5.728  -4.024  0.44 33.19 ?  163 LYS   A HD2  1 
ATOM   3733 H  HD3  A LYS   A 1 163 ? 4.964  -6.498  -3.692  0.56 35.16 ?  163 LYS   A HD3  1 
ATOM   3734 H  HD3  B LYS   A 1 163 ? 5.394  -6.073  -3.700  0.44 33.19 ?  163 LYS   A HD3  1 
ATOM   3735 H  HE2  A LYS   A 1 163 ? 4.441  -8.424  -5.069  0.56 37.69 ?  163 LYS   A HE2  1 
ATOM   3736 H  HE2  B LYS   A 1 163 ? 5.273  -7.805  -5.312  0.44 35.37 ?  163 LYS   A HE2  1 
ATOM   3737 H  HE3  A LYS   A 1 163 ? 3.072  -7.694  -5.385  0.56 37.69 ?  163 LYS   A HE3  1 
ATOM   3738 H  HE3  B LYS   A 1 163 ? 3.826  -7.279  -5.708  0.44 35.37 ?  163 LYS   A HE3  1 
ATOM   3739 H  HZ1  A LYS   A 1 163 ? 4.597  -7.221  -7.000  0.56 39.40 ?  163 LYS   A HZ1  1 
ATOM   3740 H  HZ1  B LYS   A 1 163 ? 4.798  -5.339  -6.385  0.44 36.70 ?  163 LYS   A HZ1  1 
ATOM   3741 H  HZ2  A LYS   A 1 163 ? 4.232  -5.993  -6.323  0.56 39.40 ?  163 LYS   A HZ2  1 
ATOM   3742 H  HZ2  B LYS   A 1 163 ? 6.115  -5.810  -6.008  0.44 36.70 ?  163 LYS   A HZ2  1 
ATOM   3743 H  HZ3  A LYS   A 1 163 ? 5.502  -6.630  -6.035  0.56 39.40 ?  163 LYS   A HZ3  1 
ATOM   3744 H  HZ3  B LYS   A 1 163 ? 5.410  -6.434  -7.110  0.44 36.70 ?  163 LYS   A HZ3  1 
ATOM   3745 N  N    A LEU   A 1 164 ? 5.638  -8.618  0.595   0.56 18.71 ?  164 LEU   A N    1 
ATOM   3746 N  N    B LEU   A 1 164 ? 5.650  -8.701  0.306   0.44 17.73 ?  164 LEU   A N    1 
ATOM   3747 C  CA   A LEU   A 1 164 ? 6.718  -9.594  0.727   0.56 17.70 ?  164 LEU   A CA   1 
ATOM   3748 C  CA   B LEU   A 1 164 ? 6.692  -9.716  0.456   0.44 17.30 ?  164 LEU   A CA   1 
ATOM   3749 C  C    A LEU   A 1 164 ? 6.282  -10.787 1.564   0.56 17.85 ?  164 LEU   A C    1 
ATOM   3750 C  C    B LEU   A 1 164 ? 6.203  -10.878 1.307   0.44 17.57 ?  164 LEU   A C    1 
ATOM   3751 O  O    A LEU   A 1 164 ? 6.611  -11.937 1.247   0.56 17.70 ?  164 LEU   A O    1 
ATOM   3752 O  O    B LEU   A 1 164 ? 6.412  -12.047 0.962   0.44 17.76 ?  164 LEU   A O    1 
ATOM   3753 C  CB   A LEU   A 1 164 ? 7.924  -8.926  1.376   0.56 16.67 ?  164 LEU   A CB   1 
ATOM   3754 C  CB   B LEU   A 1 164 ? 7.936  -9.098  1.089   0.44 16.74 ?  164 LEU   A CB   1 
ATOM   3755 C  CG   A LEU   A 1 164 ? 8.705  -7.947  0.503   0.56 17.02 ?  164 LEU   A CG   1 
ATOM   3756 C  CG   B LEU   A 1 164 ? 8.729  -8.108  0.238   0.44 16.48 ?  164 LEU   A CG   1 
ATOM   3757 C  CD1  A LEU   A 1 164 ? 9.622  -7.097  1.368   0.56 16.87 ?  164 LEU   A CD1  1 
ATOM   3758 C  CD1  B LEU   A 1 164 ? 9.716  -7.347  1.110   0.44 16.29 ?  164 LEU   A CD1  1 
ATOM   3759 C  CD2  A LEU   A 1 164 ? 9.503  -8.697  -0.552  0.56 17.46 ?  164 LEU   A CD2  1 
ATOM   3760 C  CD2  B LEU   A 1 164 ? 9.456  -8.827  -0.885  0.44 16.81 ?  164 LEU   A CD2  1 
ATOM   3761 H  H    A LEU   A 1 164 ? 5.805  -7.841  0.935   0.56 22.47 ?  164 LEU   A H    1 
ATOM   3762 H  H    B LEU   A 1 164 ? 5.822  -7.951  0.698   0.44 21.30 ?  164 LEU   A H    1 
ATOM   3763 H  HA   A LEU   A 1 164 ? 6.972  -9.904  -0.157  0.56 21.27 ?  164 LEU   A HA   1 
ATOM   3764 H  HA   B LEU   A 1 164 ? 6.928  -10.058 -0.416  0.44 20.78 ?  164 LEU   A HA   1 
ATOM   3765 H  HB2  A LEU   A 1 164 ? 7.617  -8.435  2.155   0.56 20.03 ?  164 LEU   A HB2  1 
ATOM   3766 H  HB2  B LEU   A 1 164 ? 7.667  -8.630  1.893   0.44 20.11 ?  164 LEU   A HB2  1 
ATOM   3767 H  HB3  A LEU   A 1 164 ? 8.539  -9.619  1.651   0.56 20.03 ?  164 LEU   A HB3  1 
ATOM   3768 H  HB3  B LEU   A 1 164 ? 8.542  -9.817  1.324   0.44 20.11 ?  164 LEU   A HB3  1 
ATOM   3769 H  HG   A LEU   A 1 164 ? 8.083  -7.352  0.051   0.56 20.45 ?  164 LEU   A HG   1 
ATOM   3770 H  HG   B LEU   A 1 164 ? 8.120  -7.466  -0.156  0.44 19.80 ?  164 LEU   A HG   1 
ATOM   3771 H  HD11 A LEU   A 1 164 ? 10.118 -6.486  0.801   0.56 20.26 ?  164 LEU   A HD11 1 
ATOM   3772 H  HD11 B LEU   A 1 164 ? 10.217 -6.729  0.555   0.44 19.57 ?  164 LEU   A HD11 1 
ATOM   3773 H  HD12 A LEU   A 1 164 ? 9.085  -6.595  2.003   0.56 20.26 ?  164 LEU   A HD12 1 
ATOM   3774 H  HD12 B LEU   A 1 164 ? 9.227  -6.858  1.791   0.44 19.57 ?  164 LEU   A HD12 1 
ATOM   3775 H  HD13 A LEU   A 1 164 ? 10.235 -7.679  1.844   0.56 20.26 ?  164 LEU   A HD13 1 
ATOM   3776 H  HD13 B LEU   A 1 164 ? 10.321 -7.980  1.529   0.44 19.57 ?  164 LEU   A HD13 1 
ATOM   3777 H  HD21 A LEU   A 1 164 ? 10.033 -8.060  -1.058  0.56 20.97 ?  164 LEU   A HD21 1 
ATOM   3778 H  HD21 B LEU   A 1 164 ? 9.984  -8.182  -1.381  0.44 20.19 ?  164 LEU   A HD21 1 
ATOM   3779 H  HD22 A LEU   A 1 164 ? 10.083 -9.335  -0.112  0.56 20.97 ?  164 LEU   A HD22 1 
ATOM   3780 H  HD22 B LEU   A 1 164 ? 10.035 -9.504  -0.502  0.44 20.19 ?  164 LEU   A HD22 1 
ATOM   3781 H  HD23 A LEU   A 1 164 ? 8.888  -9.157  -1.143  0.56 20.97 ?  164 LEU   A HD23 1 
ATOM   3782 H  HD23 B LEU   A 1 164 ? 8.802  -9.240  -1.469  0.44 20.19 ?  164 LEU   A HD23 1 
ATOM   3783 N  N    A VAL   A 1 165 ? 5.567  -10.527 2.656   0.56 17.92 ?  165 VAL   A N    1 
ATOM   3784 N  N    B VAL   A 1 165 ? 5.569  -10.572 2.439   0.44 17.49 ?  165 VAL   A N    1 
ATOM   3785 C  CA   A VAL   A 1 165 ? 5.114  -11.605 3.528   0.56 18.19 ?  165 VAL   A CA   1 
ATOM   3786 C  CA   B VAL   A 1 165 ? 5.061  -11.621 3.318   0.44 17.83 ?  165 VAL   A CA   1 
ATOM   3787 C  C    A VAL   A 1 165 ? 4.080  -12.470 2.819   0.56 18.56 ?  165 VAL   A C    1 
ATOM   3788 C  C    B VAL   A 1 165 ? 4.004  -12.444 2.597   0.44 18.88 ?  165 VAL   A C    1 
ATOM   3789 O  O    A VAL   A 1 165 ? 4.162  -13.705 2.833   0.56 18.26 ?  165 VAL   A O    1 
ATOM   3790 O  O    B VAL   A 1 165 ? 4.091  -13.675 2.517   0.44 18.72 ?  165 VAL   A O    1 
ATOM   3791 C  CB   A VAL   A 1 165 ? 4.568  -11.020 4.843   0.56 19.16 ?  165 VAL   A CB   1 
ATOM   3792 C  CB   B VAL   A 1 165 ? 4.512  -11.002 4.617   0.44 18.22 ?  165 VAL   A CB   1 
ATOM   3793 C  CG1  A VAL   A 1 165 ? 3.820  -12.083 5.638   0.56 20.06 ?  165 VAL   A CG1  1 
ATOM   3794 C  CG1  B VAL   A 1 165 ? 3.781  -12.048 5.442   0.44 18.85 ?  165 VAL   A CG1  1 
ATOM   3795 C  CG2  A VAL   A 1 165 ? 5.700  -10.411 5.661   0.56 19.49 ?  165 VAL   A CG2  1 
ATOM   3796 C  CG2  B VAL   A 1 165 ? 5.638  -10.367 5.417   0.44 18.38 ?  165 VAL   A CG2  1 
ATOM   3797 H  H    A VAL   A 1 165 ? 5.343  -9.737  2.916   0.56 21.53 ?  165 VAL   A H    1 
ATOM   3798 H  H    B VAL   A 1 165 ? 5.411  -9.771  2.713   0.44 21.01 ?  165 VAL   A H    1 
ATOM   3799 H  HA   A VAL   A 1 165 ? 5.870  -12.167 3.745   0.56 21.85 ?  165 VAL   A HA   1 
ATOM   3800 H  HA   B VAL   A 1 165 ? 5.790  -12.211 3.560   0.44 21.42 ?  165 VAL   A HA   1 
ATOM   3801 H  HB   A VAL   A 1 165 ? 3.941  -10.310 4.635   0.56 23.02 ?  165 VAL   A HB   1 
ATOM   3802 H  HB   B VAL   A 1 165 ? 3.880  -10.301 4.395   0.44 21.88 ?  165 VAL   A HB   1 
ATOM   3803 H  HG11 A VAL   A 1 165 ? 3.735  -11.783 6.556   0.56 24.10 ?  165 VAL   A HG11 1 
ATOM   3804 H  HG11 B VAL   A 1 165 ? 3.693  -11.718 6.348   0.44 22.65 ?  165 VAL   A HG11 1 
ATOM   3805 H  HG12 A VAL   A 1 165 ? 2.941  -12.208 5.249   0.56 24.10 ?  165 VAL   A HG12 1 
ATOM   3806 H  HG12 B VAL   A 1 165 ? 2.903  -12.199 5.059   0.44 22.65 ?  165 VAL   A HG12 1 
ATOM   3807 H  HG13 A VAL   A 1 165 ? 4.323  -12.910 5.606   0.56 24.10 ?  165 VAL   A HG13 1 
ATOM   3808 H  HG13 B VAL   A 1 165 ? 4.295  -12.870 5.438   0.44 22.65 ?  165 VAL   A HG13 1 
ATOM   3809 H  HG21 A VAL   A 1 165 ? 5.337  -10.050 6.485   0.56 23.41 ?  165 VAL   A HG21 1 
ATOM   3810 H  HG21 B VAL   A 1 165 ? 5.286  -10.051 6.264   0.44 22.08 ?  165 VAL   A HG21 1 
ATOM   3811 H  HG22 A VAL   A 1 165 ? 6.353  -11.100 5.860   0.56 23.41 ?  165 VAL   A HG22 1 
ATOM   3812 H  HG22 B VAL   A 1 165 ? 6.328  -11.029 5.573   0.44 22.08 ?  165 VAL   A HG22 1 
ATOM   3813 H  HG23 A VAL   A 1 165 ? 6.116  -9.701  5.145   0.56 23.41 ?  165 VAL   A HG23 1 
ATOM   3814 H  HG23 B VAL   A 1 165 ? 6.004  -9.621  4.913   0.44 22.08 ?  165 VAL   A HG23 1 
ATOM   3815 N  N    A SER   A 1 166 ? 3.083  -11.836 2.200   0.56 19.25 ?  166 SER   A N    1 
ATOM   3816 N  N    B SER   A 1 166 ? 2.993  -11.770 2.049   0.44 20.45 ?  166 SER   A N    1 
ATOM   3817 C  CA   A SER   A 1 166 ? 1.970  -12.595 1.636   0.56 20.92 ?  166 SER   A CA   1 
ATOM   3818 C  CA   B SER   A 1 166 ? 1.865  -12.475 1.453   0.44 21.98 ?  166 SER   A CA   1 
ATOM   3819 C  C    A SER   A 1 166 ? 2.405  -13.456 0.461   0.56 21.29 ?  166 SER   A C    1 
ATOM   3820 C  C    B SER   A 1 166 ? 2.271  -13.296 0.242   0.44 21.89 ?  166 SER   A C    1 
ATOM   3821 O  O    A SER   A 1 166 ? 1.822  -14.526 0.234   0.56 22.39 ?  166 SER   A O    1 
ATOM   3822 O  O    B SER   A 1 166 ? 1.514  -14.181 -0.172  0.44 21.72 ?  166 SER   A O    1 
ATOM   3823 C  CB   A SER   A 1 166 ? 0.843  -11.648 1.216   0.56 23.11 ?  166 SER   A CB   1 
ATOM   3824 C  CB   B SER   A 1 166 ? 0.782  -11.480 1.037   0.44 23.73 ?  166 SER   A CB   1 
ATOM   3825 O  OG   A SER   A 1 166 ? 0.300  -10.967 2.336   0.56 25.60 ?  166 SER   A OG   1 
ATOM   3826 O  OG   B SER   A 1 166 ? 0.308  -10.741 2.149   0.44 25.51 ?  166 SER   A OG   1 
ATOM   3827 H  H    A SER   A 1 166 ? 3.016  -10.984 2.108   0.56 23.12 ?  166 SER   A H    1 
ATOM   3828 H  H    B SER   A 1 166 ? 2.938  -10.913 2.012   0.44 24.56 ?  166 SER   A H    1 
ATOM   3829 H  HA   A SER   A 1 166 ? 1.610  -13.188 2.311   0.56 25.13 ?  166 SER   A HA   1 
ATOM   3830 H  HA   B SER   A 1 166 ? 1.484  -13.074 2.112   0.44 26.40 ?  166 SER   A HA   1 
ATOM   3831 H  HB2  A SER   A 1 166 ? 1.185  -11.005 0.574   0.56 27.75 ?  166 SER   A HB2  1 
ATOM   3832 H  HB2  B SER   A 1 166 ? 1.151  -10.867 0.384   0.44 28.50 ?  166 SER   A HB2  1 
ATOM   3833 H  HB3  A SER   A 1 166 ? 0.122  -12.160 0.814   0.56 27.75 ?  166 SER   A HB3  1 
ATOM   3834 H  HB3  B SER   A 1 166 ? 0.040  -11.971 0.647   0.44 28.50 ?  166 SER   A HB3  1 
ATOM   3835 H  HG   A SER   A 1 166 ? -0.293 -10.422 2.087   0.56 30.74 ?  166 SER   A HG   1 
ATOM   3836 H  HG   B SER   A 1 166 ? 0.941  -10.311 2.497   0.44 30.63 ?  166 SER   A HG   1 
ATOM   3837 N  N    A SER   A 1 167 ? 3.418  -13.018 -0.288  0.56 21.41 ?  167 SER   A N    1 
ATOM   3838 N  N    B SER   A 1 167 ? 3.432  -13.014 -0.348  0.44 21.92 ?  167 SER   A N    1 
ATOM   3839 C  CA   A SER   A 1 167 ? 3.878  -13.737 -1.468  0.56 22.49 ?  167 SER   A CA   1 
ATOM   3840 C  CA   B SER   A 1 167 ? 3.908  -13.747 -1.509  0.44 22.50 ?  167 SER   A CA   1 
ATOM   3841 C  C    A SER   A 1 167 ? 5.029  -14.692 -1.174  0.56 22.67 ?  167 SER   A C    1 
ATOM   3842 C  C    B SER   A 1 167 ? 5.060  -14.687 -1.185  0.44 22.58 ?  167 SER   A C    1 
ATOM   3843 O  O    A SER   A 1 167 ? 5.492  -15.380 -2.090  0.56 23.35 ?  167 SER   A O    1 
ATOM   3844 O  O    B SER   A 1 167 ? 5.561  -15.362 -2.092  0.44 23.03 ?  167 SER   A O    1 
ATOM   3845 C  CB   A SER   A 1 167 ? 4.286  -12.745 -2.569  0.56 23.20 ?  167 SER   A CB   1 
ATOM   3846 C  CB   B SER   A 1 167 ? 4.323  -12.773 -2.622  0.44 22.93 ?  167 SER   A CB   1 
ATOM   3847 O  OG   A SER   A 1 167 ? 5.347  -11.907 -2.137  0.56 23.71 ?  167 SER   A OG   1 
ATOM   3848 O  OG   B SER   A 1 167 ? 5.352  -11.901 -2.183  0.44 23.24 ?  167 SER   A OG   1 
ATOM   3849 H  H    A SER   A 1 167 ? 3.853  -12.286 -0.132  0.56 25.72 ?  167 SER   A H    1 
ATOM   3850 H  H    B SER   A 1 167 ? 3.962  -12.382 -0.094  0.44 26.32 ?  167 SER   A H    1 
ATOM   3851 H  HA   A SER   A 1 167 ? 3.143  -14.261 -1.813  0.56 27.01 ?  167 SER   A HA   1 
ATOM   3852 H  HA   B SER   A 1 167 ? 3.182  -14.285 -1.853  0.44 27.03 ?  167 SER   A HA   1 
ATOM   3853 H  HB2  A SER   A 1 167 ? 4.576  -13.243 -3.350  0.56 27.87 ?  167 SER   A HB2  1 
ATOM   3854 H  HB2  B SER   A 1 167 ? 4.643  -13.284 -3.382  0.44 27.54 ?  167 SER   A HB2  1 
ATOM   3855 H  HB3  A SER   A 1 167 ? 3.515  -12.195 -2.803  0.56 27.87 ?  167 SER   A HB3  1 
ATOM   3856 H  HB3  B SER   A 1 167 ? 3.546  -12.249 -2.885  0.44 27.54 ?  167 SER   A HB3  1 
ATOM   3857 H  HG   A SER   A 1 167 ? 5.094  -11.451 -1.476  0.56 28.47 ?  167 SER   A HG   1 
ATOM   3858 H  HG   B SER   A 1 167 ? 5.088  -11.465 -1.514  0.44 27.91 ?  167 SER   A HG   1 
ATOM   3859 N  N    . PHE   A 1 168 ? 5.492  -14.758 0.072   1.00 22.14 ?  168 PHE   A N    1 
ATOM   3860 C  CA   . PHE   A 1 168 ? 6.657  -15.574 0.402   1.00 22.95 ?  168 PHE   A CA   1 
ATOM   3861 C  C    . PHE   A 1 168 ? 6.343  -17.055 0.256   1.00 27.41 ?  168 PHE   A C    1 
ATOM   3862 O  O    . PHE   A 1 168 ? 5.317  -17.539 0.746   1.00 27.92 ?  168 PHE   A O    1 
ATOM   3863 C  CB   . PHE   A 1 168 ? 7.138  -15.311 1.827   1.00 20.68 ?  168 PHE   A CB   1 
ATOM   3864 C  CG   . PHE   A 1 168 ? 8.413  -16.045 2.159   1.00 19.04 ?  168 PHE   A CG   1 
ATOM   3865 C  CD1  . PHE   A 1 168 ? 9.601  -15.661 1.570   1.00 18.75 ?  168 PHE   A CD1  1 
ATOM   3866 C  CD2  . PHE   A 1 168 ? 8.424  -17.129 3.027   1.00 18.01 ?  168 PHE   A CD2  1 
ATOM   3867 C  CE1  . PHE   A 1 168 ? 10.775 -16.326 1.846   1.00 18.36 ?  168 PHE   A CE1  1 
ATOM   3868 C  CE2  . PHE   A 1 168 ? 9.605  -17.798 3.306   1.00 18.19 ?  168 PHE   A CE2  1 
ATOM   3869 C  CZ   . PHE   A 1 168 ? 10.777 -17.393 2.713   1.00 18.39 ?  168 PHE   A CZ   1 
ATOM   3870 H  H    A PHE   A 1 168 ? 5.152  -14.339 0.741   0.56 26.60 ?  168 PHE   A H    1 
ATOM   3871 H  H    B PHE   A 1 168 ? 5.141  -14.342 0.738   0.44 26.60 ?  168 PHE   A H    1 
ATOM   3872 H  HA   . PHE   A 1 168 ? 7.381  -15.354 -0.207  1.00 27.56 ?  168 PHE   A HA   1 
ATOM   3873 H  HB2  . PHE   A 1 168 ? 7.299  -14.361 1.936   1.00 24.84 ?  168 PHE   A HB2  1 
ATOM   3874 H  HB3  . PHE   A 1 168 ? 6.450  -15.603 2.448   1.00 24.84 ?  168 PHE   A HB3  1 
ATOM   3875 H  HD1  . PHE   A 1 168 ? 9.609  -14.940 0.983   1.00 22.52 ?  168 PHE   A HD1  1 
ATOM   3876 H  HD2  . PHE   A 1 168 ? 7.629  -17.407 3.430   1.00 21.63 ?  168 PHE   A HD2  1 
ATOM   3877 H  HE1  . PHE   A 1 168 ? 11.571 -16.055 1.448   1.00 22.05 ?  168 PHE   A HE1  1 
ATOM   3878 H  HE2  . PHE   A 1 168 ? 9.602  -18.521 3.893   1.00 21.85 ?  168 PHE   A HE2  1 
ATOM   3879 H  HZ   . PHE   A 1 168 ? 11.571 -17.841 2.900   1.00 22.09 ?  168 PHE   A HZ   1 
ATOM   3880 N  N    . LEU   A 1 169 ? 7.251  -17.783 -0.382  1.00 33.26 ?  169 LEU   A N    1 
ATOM   3881 C  CA   . LEU   A 1 169 ? 7.073  -19.213 -0.556  1.00 39.88 ?  169 LEU   A CA   1 
ATOM   3882 C  C    . LEU   A 1 169 ? 7.926  -19.966 0.458   1.00 42.40 ?  169 LEU   A C    1 
ATOM   3883 O  O    . LEU   A 1 169 ? 7.406  -20.477 1.453   1.00 43.38 ?  169 LEU   A O    1 
ATOM   3884 C  CB   . LEU   A 1 169 ? 7.429  -19.631 -1.985  1.00 43.12 ?  169 LEU   A CB   1 
ATOM   3885 C  CG   . LEU   A 1 169 ? 7.037  -21.056 -2.386  1.00 45.34 ?  169 LEU   A CG   1 
ATOM   3886 C  CD1  . LEU   A 1 169 ? 5.610  -21.368 -1.958  1.00 46.27 ?  169 LEU   A CD1  1 
ATOM   3887 C  CD2  . LEU   A 1 169 ? 7.193  -21.245 -3.888  1.00 46.15 ?  169 LEU   A CD2  1 
ATOM   3888 O  OXT  . LEU   A 1 169 ? 9.147  -20.065 0.320   1.00 43.08 -1 169 LEU   A OXT  1 
ATOM   3889 H  H    . LEU   A 1 169 ? 7.982  -17.471 -0.716  1.00 39.93 ?  169 LEU   A H    1 
ATOM   3890 H  HA   . LEU   A 1 169 ? 6.144  -19.428 -0.392  1.00 47.88 ?  169 LEU   A HA   1 
ATOM   3891 H  HB2  . LEU   A 1 169 ? 6.985  -19.026 -2.599  1.00 51.77 ?  169 LEU   A HB2  1 
ATOM   3892 H  HB3  . LEU   A 1 169 ? 8.390  -19.555 -2.095  1.00 51.77 ?  169 LEU   A HB3  1 
ATOM   3893 H  HG   . LEU   A 1 169 ? 7.628  -21.685 -1.943  1.00 54.42 ?  169 LEU   A HG   1 
ATOM   3894 H  HD11 . LEU   A 1 169 ? 5.304  -22.155 -2.432  1.00 55.55 ?  169 LEU   A HD11 1 
ATOM   3895 H  HD12 . LEU   A 1 169 ? 5.596  -21.532 -1.001  1.00 55.55 ?  169 LEU   A HD12 1 
ATOM   3896 H  HD13 . LEU   A 1 169 ? 5.044  -20.610 -2.174  1.00 55.55 ?  169 LEU   A HD13 1 
ATOM   3897 H  HD21 . LEU   A 1 169 ? 6.950  -22.156 -4.118  1.00 55.40 ?  169 LEU   A HD21 1 
ATOM   3898 H  HD22 . LEU   A 1 169 ? 6.607  -20.621 -4.346  1.00 55.40 ?  169 LEU   A HD22 1 
ATOM   3899 H  HD23 . LEU   A 1 169 ? 8.115  -21.075 -4.133  1.00 55.40 ?  169 LEU   A HD23 1 
ATOM   3900 N  N    A SER   B 1 1   ? 50.820 -9.248  -23.700 0.56 26.61 ?  1   SER   B N    1 
ATOM   3901 N  N    B SER   B 1 1   ? 50.728 -9.292  -23.710 0.44 24.69 ?  1   SER   B N    1 
ATOM   3902 C  CA   A SER   B 1 1   ? 51.313 -10.300 -22.788 0.56 26.75 ?  1   SER   B CA   1 
ATOM   3903 C  CA   B SER   B 1 1   ? 51.226 -10.277 -22.728 0.44 24.49 ?  1   SER   B CA   1 
ATOM   3904 C  C    A SER   B 1 1   ? 50.233 -11.343 -22.531 0.56 26.24 ?  1   SER   B C    1 
ATOM   3905 C  C    B SER   B 1 1   ? 50.183 -11.356 -22.480 0.44 24.28 ?  1   SER   B C    1 
ATOM   3906 O  O    A SER   B 1 1   ? 49.044 -11.139 -22.817 0.56 25.96 ?  1   SER   B O    1 
ATOM   3907 O  O    B SER   B 1 1   ? 48.980 -11.167 -22.717 0.44 24.11 ?  1   SER   B O    1 
ATOM   3908 C  CB   A SER   B 1 1   ? 51.779 -9.694  -21.466 0.56 27.60 ?  1   SER   B CB   1 
ATOM   3909 C  CB   B SER   B 1 1   ? 51.583 -9.597  -21.411 0.44 24.72 ?  1   SER   B CB   1 
ATOM   3910 O  OG   A SER   B 1 1   ? 50.674 -9.340  -20.657 0.56 29.37 ?  1   SER   B OG   1 
ATOM   3911 O  OG   B SER   B 1 1   ? 50.463 -9.557  -20.546 0.44 25.82 ?  1   SER   B OG   1 
ATOM   3912 H  H1   A SER   B 1 1   ? 50.746 -9.586  -24.517 0.56 31.95 ?  1   SER   B H1   1 
ATOM   3913 H  H1   B SER   B 1 1   ? 51.422 -8.929  -24.129 0.44 29.65 ?  1   SER   B H1   1 
ATOM   3914 H  H2   A SER   B 1 1   ? 50.030 -8.967  -23.414 0.56 31.95 ?  1   SER   B H2   1 
ATOM   3915 H  H2   B SER   B 1 1   ? 50.204 -9.705  -24.295 0.44 29.65 ?  1   SER   B H2   1 
ATOM   3916 H  H3   A SER   B 1 1   ? 51.400 -8.576  -23.702 0.56 31.95 ?  1   SER   B H3   1 
ATOM   3917 H  H3   B SER   B 1 1   ? 50.271 -8.665  -23.282 0.44 29.65 ?  1   SER   B H3   1 
ATOM   3918 H  HA   A SER   B 1 1   ? 52.069 -10.733 -23.210 0.56 32.12 ?  1   SER   B HA   1 
ATOM   3919 H  HA   B SER   B 1 1   ? 52.022 -10.690 -23.089 0.44 29.41 ?  1   SER   B HA   1 
ATOM   3920 H  HB2  A SER   B 1 1   ? 52.319 -10.350 -21.002 0.56 33.14 ?  1   SER   B HB2  1 
ATOM   3921 H  HB2  B SER   B 1 1   ? 52.290 -10.102 -20.985 0.44 29.69 ?  1   SER   B HB2  1 
ATOM   3922 H  HB3  A SER   B 1 1   ? 52.303 -8.899  -21.649 0.56 33.14 ?  1   SER   B HB3  1 
ATOM   3923 H  HB3  B SER   B 1 1   ? 51.883 -8.691  -21.593 0.44 29.69 ?  1   SER   B HB3  1 
ATOM   3924 H  HG   A SER   B 1 1   ? 50.945 -8.957  -19.960 0.56 35.26 ?  1   SER   B HG   1 
ATOM   3925 H  HG   B SER   B 1 1   ? 50.656 -9.117  -19.855 0.44 31.01 ?  1   SER   B HG   1 
ATOM   3926 N  N    A MET   B 1 2   ? 50.668 -12.465 -21.974 0.56 26.16 ?  2   MET   B N    1 
ATOM   3927 N  N    B MET   B 1 2   ? 50.659 -12.493 -21.994 0.44 24.27 ?  2   MET   B N    1 
ATOM   3928 C  CA   A MET   B 1 2   ? 49.843 -13.654 -21.810 0.56 26.46 ?  2   MET   B CA   1 
ATOM   3929 C  CA   B MET   B 1 2   ? 49.839 -13.680 -21.798 0.44 24.56 ?  2   MET   B CA   1 
ATOM   3930 C  C    A MET   B 1 2   ? 49.594 -13.866 -20.323 0.56 24.40 ?  2   MET   B C    1 
ATOM   3931 C  C    B MET   B 1 2   ? 49.595 -13.850 -20.309 0.44 23.42 ?  2   MET   B C    1 
ATOM   3932 O  O    A MET   B 1 2   ? 50.521 -14.179 -19.571 0.56 24.72 ?  2   MET   B O    1 
ATOM   3933 O  O    B MET   B 1 2   ? 50.530 -14.111 -19.546 0.44 23.69 ?  2   MET   B O    1 
ATOM   3934 C  CB   A MET   B 1 2   ? 50.572 -14.847 -22.416 0.56 30.10 ?  2   MET   B CB   1 
ATOM   3935 C  CB   B MET   B 1 2   ? 50.564 -14.884 -22.369 0.44 27.14 ?  2   MET   B CB   1 
ATOM   3936 C  CG   A MET   B 1 2   ? 49.746 -16.115 -22.534 0.56 33.63 ?  2   MET   B CG   1 
ATOM   3937 C  CG   B MET   B 1 2   ? 49.671 -16.053 -22.763 0.44 29.19 ?  2   MET   B CG   1 
ATOM   3938 S  SD   A MET   B 1 2   ? 50.613 -17.353 -23.518 0.56 36.95 ?  2   MET   B SD   1 
ATOM   3939 S  SD   B MET   B 1 2   ? 50.532 -17.200 -23.848 0.44 30.99 ?  2   MET   B SD   1 
ATOM   3940 C  CE   A MET   B 1 2   ? 51.120 -16.337 -24.902 0.56 37.08 ?  2   MET   B CE   1 
ATOM   3941 C  CE   B MET   B 1 2   ? 51.741 -16.104 -24.569 0.44 31.28 ?  2   MET   B CE   1 
ATOM   3942 H  H    A MET   B 1 2   ? 51.470 -12.569 -21.677 0.56 31.42 ?  2   MET   B H    1 
ATOM   3943 H  H    B MET   B 1 2   ? 51.484 -12.613 -21.767 0.44 29.15 ?  2   MET   B H    1 
ATOM   3944 H  HA   A MET   B 1 2   ? 49.002 -13.543 -22.278 0.56 31.77 ?  2   MET   B HA   1 
ATOM   3945 H  HA   B MET   B 1 2   ? 49.000 -13.591 -22.275 0.44 29.49 ?  2   MET   B HA   1 
ATOM   3946 H  HB2  A MET   B 1 2   ? 50.859 -14.573 -23.297 0.56 36.14 ?  2   MET   B HB2  1 
ATOM   3947 H  HB2  B MET   B 1 2   ? 50.983 -14.512 -23.148 0.44 32.60 ?  2   MET   B HB2  1 
ATOM   3948 H  HB3  A MET   B 1 2   ? 51.345 -15.064 -21.876 0.56 36.14 ?  2   MET   B HB3  1 
ATOM   3949 H  HB3  B MET   B 1 2   ? 51.235 -15.226 -21.755 0.44 32.60 ?  2   MET   B HB3  1 
ATOM   3950 H  HG2  A MET   B 1 2   ? 49.589 -16.483 -21.647 0.56 40.38 ?  2   MET   B HG2  1 
ATOM   3951 H  HG2  B MET   B 1 2   ? 49.393 -16.537 -21.964 0.44 35.06 ?  2   MET   B HG2  1 
ATOM   3952 H  HG3  A MET   B 1 2   ? 48.903 -15.918 -22.971 0.56 40.38 ?  2   MET   B HG3  1 
ATOM   3953 H  HG3  B MET   B 1 2   ? 48.898 -15.729 -23.242 0.44 35.06 ?  2   MET   B HG3  1 
ATOM   3954 H  HE1  A MET   B 1 2   ? 51.289 -16.905 -25.658 0.56 44.51 ?  2   MET   B HE1  1 
ATOM   3955 H  HE1  B MET   B 1 2   ? 52.201 -16.599 -25.226 0.44 37.55 ?  2   MET   B HE1  1 
ATOM   3956 H  HE2  A MET   B 1 2   ? 50.406 -15.708 -25.107 0.56 44.51 ?  2   MET   B HE2  1 
ATOM   3957 H  HE2  B MET   B 1 2   ? 51.281 -15.342 -24.976 0.44 37.55 ?  2   MET   B HE2  1 
ATOM   3958 H  HE3  A MET   B 1 2   ? 51.927 -15.847 -24.662 0.56 44.51 ?  2   MET   B HE3  1 
ATOM   3959 H  HE3  B MET   B 1 2   ? 52.379 -15.799 -23.892 0.44 37.55 ?  2   MET   B HE3  1 
ATOM   3960 N  N    . VAL   B 1 3   ? 48.343 -13.689 -19.901 1.00 22.21 ?  3   VAL   B N    1 
ATOM   3961 C  CA   . VAL   B 1 3   ? 47.933 -13.930 -18.526 1.00 20.96 ?  3   VAL   B CA   1 
ATOM   3962 C  C    . VAL   B 1 3   ? 46.699 -14.819 -18.547 1.00 19.56 ?  3   VAL   B C    1 
ATOM   3963 O  O    . VAL   B 1 3   ? 45.973 -14.893 -19.542 1.00 20.39 ?  3   VAL   B O    1 
ATOM   3964 C  CB   . VAL   B 1 3   ? 47.654 -12.619 -17.758 1.00 22.94 ?  3   VAL   B CB   1 
ATOM   3965 C  CG1  . VAL   B 1 3   ? 48.927 -11.763 -17.656 1.00 23.40 ?  3   VAL   B CG1  1 
ATOM   3966 C  CG2  . VAL   B 1 3   ? 46.531 -11.850 -18.426 1.00 23.45 ?  3   VAL   B CG2  1 
ATOM   3967 H  H    A VAL   B 1 3   ? 47.701 -13.430 -20.413 0.56 26.68 ?  3   VAL   B H    1 
ATOM   3968 H  H    B VAL   B 1 3   ? 47.702 -13.431 -20.415 0.44 26.68 ?  3   VAL   B H    1 
ATOM   3969 H  HA   . VAL   B 1 3   ? 48.639 -14.405 -18.060 1.00 25.17 ?  3   VAL   B HA   1 
ATOM   3970 H  HB   . VAL   B 1 3   ? 47.374 -12.843 -16.856 1.00 27.55 ?  3   VAL   B HB   1 
ATOM   3971 H  HG11 . VAL   B 1 3   ? 48.718 -10.956 -17.161 1.00 28.10 ?  3   VAL   B HG11 1 
ATOM   3972 H  HG12 . VAL   B 1 3   ? 49.610 -12.271 -17.194 1.00 28.10 ?  3   VAL   B HG12 1 
ATOM   3973 H  HG13 . VAL   B 1 3   ? 49.223 -11.539 -18.550 1.00 28.10 ?  3   VAL   B HG13 1 
ATOM   3974 H  HG21 . VAL   B 1 3   ? 46.470 -10.972 -18.026 1.00 28.17 ?  3   VAL   B HG21 1 
ATOM   3975 H  HG22 . VAL   B 1 3   ? 46.718 -11.774 -19.374 1.00 28.17 ?  3   VAL   B HG22 1 
ATOM   3976 H  HG23 . VAL   B 1 3   ? 45.695 -12.332 -18.294 1.00 28.17 ?  3   VAL   B HG23 1 
ATOM   3977 N  N    . ASN   B 1 4   ? 46.469 -15.506 -17.429 1.00 17.56 ?  4   ASN   B N    1 
ATOM   3978 C  CA   . ASN   B 1 4   ? 45.326 -16.411 -17.307 1.00 16.73 ?  4   ASN   B CA   1 
ATOM   3979 C  C    . ASN   B 1 4   ? 45.262 -17.377 -18.487 1.00 16.90 ?  4   ASN   B C    1 
ATOM   3980 O  O    . ASN   B 1 4   ? 44.202 -17.620 -19.056 1.00 17.43 ?  4   ASN   B O    1 
ATOM   3981 C  CB   . ASN   B 1 4   ? 44.012 -15.636 -17.156 1.00 16.19 ?  4   ASN   B CB   1 
ATOM   3982 C  CG   . ASN   B 1 4   ? 43.962 -14.828 -15.873 1.00 14.96 ?  4   ASN   B CG   1 
ATOM   3983 O  OD1  . ASN   B 1 4   ? 44.252 -15.339 -14.796 1.00 15.08 ?  4   ASN   B OD1  1 
ATOM   3984 N  ND2  . ASN   B 1 4   ? 43.615 -13.548 -15.988 1.00 15.86 ?  4   ASN   B ND2  1 
ATOM   3985 H  H    . ASN   B 1 4   ? 46.966 -15.471 -16.730 1.00 21.10 ?  4   ASN   B H    1 
ATOM   3986 H  HA   . ASN   B 1 4   ? 45.446 -16.941 -16.504 1.00 20.10 ?  4   ASN   B HA   1 
ATOM   3987 H  HB2  . ASN   B 1 4   ? 43.914 -15.024 -17.901 1.00 19.46 ?  4   ASN   B HB2  1 
ATOM   3988 H  HB3  . ASN   B 1 4   ? 43.272 -16.266 -17.144 1.00 19.46 ?  4   ASN   B HB3  1 
ATOM   3989 H  HD21 . ASN   B 1 4   ? 43.577 -13.047 -15.285 1.00 19.05 ?  4   ASN   B HD21 1 
ATOM   3990 H  HD22 . ASN   B 1 4   ? 43.426 -13.218 -16.757 1.00 19.05 ?  4   ASN   B HD22 1 
ATOM   3991 N  N    . SER   B 1 5   ? 46.415 -17.931 -18.859 1.00 17.67 ?  5   SER   B N    1 
ATOM   3992 C  CA   . SER   B 1 5   ? 46.506 -18.836 -20.004 1.00 19.71 ?  5   SER   B CA   1 
ATOM   3993 C  C    . SER   B 1 5   ? 46.476 -20.274 -19.500 1.00 21.60 ?  5   SER   B C    1 
ATOM   3994 O  O    . SER   B 1 5   ? 47.474 -20.987 -19.482 1.00 24.16 ?  5   SER   B O    1 
ATOM   3995 C  CB   . SER   B 1 5   ? 47.769 -18.547 -20.815 1.00 21.12 ?  5   SER   B CB   1 
ATOM   3996 O  OG   . SER   B 1 5   ? 48.939 -18.704 -20.027 1.00 24.47 ?  5   SER   B OG   1 
ATOM   3997 H  H    . SER   B 1 5   ? 47.167 -17.804 -18.459 1.00 21.22 ?  5   SER   B H    1 
ATOM   3998 H  HA   . SER   B 1 5   ? 45.738 -18.703 -20.581 1.00 23.67 ?  5   SER   B HA   1 
ATOM   3999 H  HB2  . SER   B 1 5   ? 47.803 -19.162 -21.568 1.00 25.37 ?  5   SER   B HB2  1 
ATOM   4000 H  HB3  . SER   B 1 5   ? 47.717 -17.636 -21.140 1.00 25.37 ?  5   SER   B HB3  1 
ATOM   4001 H  HG   . SER   B 1 5   ? 48.993 -19.495 -19.759 1.00 29.39 ?  5   SER   B HG   1 
ATOM   4002 N  N    . PHE   B 1 6   ? 45.290 -20.672 -19.054 1.00 22.10 ?  6   PHE   B N    1 
ATOM   4003 C  CA   . PHE   B 1 6   ? 45.063 -22.020 -18.557 1.00 21.45 ?  6   PHE   B CA   1 
ATOM   4004 C  C    . PHE   B 1 6   ? 44.940 -22.971 -19.737 1.00 25.13 ?  6   PHE   B C    1 
ATOM   4005 O  O    . PHE   B 1 6   ? 44.240 -22.674 -20.710 1.00 27.33 ?  6   PHE   B O    1 
ATOM   4006 C  CB   . PHE   B 1 6   ? 43.779 -22.050 -17.729 1.00 19.56 ?  6   PHE   B CB   1 
ATOM   4007 C  CG   . PHE   B 1 6   ? 43.834 -21.199 -16.493 1.00 18.16 ?  6   PHE   B CG   1 
ATOM   4008 C  CD1  . PHE   B 1 6   ? 44.348 -21.702 -15.313 1.00 17.29 ?  6   PHE   B CD1  1 
ATOM   4009 C  CD2  . PHE   B 1 6   ? 43.374 -19.893 -16.516 1.00 17.34 ?  6   PHE   B CD2  1 
ATOM   4010 C  CE1  . PHE   B 1 6   ? 44.389 -20.920 -14.171 1.00 16.58 ?  6   PHE   B CE1  1 
ATOM   4011 C  CE2  . PHE   B 1 6   ? 43.422 -19.100 -15.387 1.00 17.66 ?  6   PHE   B CE2  1 
ATOM   4012 C  CZ   . PHE   B 1 6   ? 43.935 -19.605 -14.216 1.00 16.75 ?  6   PHE   B CZ   1 
ATOM   4013 H  H    . PHE   B 1 6   ? 44.593 -20.174 -19.033 1.00 26.54 ?  6   PHE   B H    1 
ATOM   4014 H  HA   . PHE   B 1 6   ? 45.803 -22.303 -18.003 1.00 25.76 ?  6   PHE   B HA   1 
ATOM   4015 H  HB2  . PHE   B 1 6   ? 43.044 -21.729 -18.280 1.00 23.49 ?  6   PHE   B HB2  1 
ATOM   4016 H  HB3  . PHE   B 1 6   ? 43.601 -22.965 -17.456 1.00 23.49 ?  6   PHE   B HB3  1 
ATOM   4017 H  HD1  . PHE   B 1 6   ? 44.662 -22.579 -15.283 1.00 20.77 ?  6   PHE   B HD1  1 
ATOM   4018 H  HD2  . PHE   B 1 6   ? 43.026 -19.549 -17.305 1.00 20.83 ?  6   PHE   B HD2  1 
ATOM   4019 H  HE1  . PHE   B 1 6   ? 44.745 -21.259 -13.381 1.00 19.92 ?  6   PHE   B HE1  1 
ATOM   4020 H  HE2  . PHE   B 1 6   ? 43.106 -18.227 -15.416 1.00 21.22 ?  6   PHE   B HE2  1 
ATOM   4021 H  HZ   . PHE   B 1 6   ? 43.965 -19.080 -13.449 1.00 20.12 ?  6   PHE   B HZ   1 
ATOM   4022 N  N    A SER   B 1 7   ? 45.627 -24.112 -19.640 0.56 26.21 ?  7   SER   B N    1 
ATOM   4023 N  N    B SER   B 1 7   ? 45.622 -24.112 -19.665 0.44 25.25 ?  7   SER   B N    1 
ATOM   4024 C  CA   A SER   B 1 7   ? 45.712 -25.093 -20.711 0.56 28.52 ?  7   SER   B CA   1 
ATOM   4025 C  CA   B SER   B 1 7   ? 45.614 -25.051 -20.778 0.44 26.45 ?  7   SER   B CA   1 
ATOM   4026 C  C    A SER   B 1 7   ? 45.697 -26.491 -20.114 0.56 28.43 ?  7   SER   B C    1 
ATOM   4027 C  C    B SER   B 1 7   ? 45.551 -26.480 -20.264 0.44 26.23 ?  7   SER   B C    1 
ATOM   4028 O  O    A SER   B 1 7   ? 46.320 -26.741 -19.078 0.56 29.02 ?  7   SER   B O    1 
ATOM   4029 O  O    B SER   B 1 7   ? 46.208 -26.829 -19.280 0.44 26.62 ?  7   SER   B O    1 
ATOM   4030 C  CB   A SER   B 1 7   ? 47.004 -24.902 -21.520 0.56 30.49 ?  7   SER   B CB   1 
ATOM   4031 C  CB   B SER   B 1 7   ? 46.847 -24.864 -21.675 0.44 27.41 ?  7   SER   B CB   1 
ATOM   4032 O  OG   A SER   B 1 7   ? 47.159 -25.919 -22.496 0.56 31.99 ?  7   SER   B OG   1 
ATOM   4033 O  OG   B SER   B 1 7   ? 46.590 -25.341 -22.985 0.44 27.98 ?  7   SER   B OG   1 
ATOM   4034 H  H    A SER   B 1 7   ? 46.071 -24.342 -18.939 0.56 31.48 ?  7   SER   B H    1 
ATOM   4035 H  H    B SER   B 1 7   ? 46.099 -24.361 -18.991 0.44 30.32 ?  7   SER   B H    1 
ATOM   4036 H  HA   A SER   B 1 7   ? 44.957 -25.004 -21.307 0.56 34.25 ?  7   SER   B HA   1 
ATOM   4037 H  HA   B SER   B 1 7   ? 44.830 -24.898 -21.320 0.44 31.76 ?  7   SER   B HA   1 
ATOM   4038 H  HB2  A SER   B 1 7   ? 46.970 -24.042 -21.968 0.56 36.61 ?  7   SER   B HB2  1 
ATOM   4039 H  HB2  B SER   B 1 7   ? 47.067 -23.919 -21.720 0.44 32.91 ?  7   SER   B HB2  1 
ATOM   4040 H  HB3  A SER   B 1 7   ? 47.764 -24.928 -20.916 0.56 36.61 ?  7   SER   B HB3  1 
ATOM   4041 H  HB3  B SER   B 1 7   ? 47.593 -25.359 -21.302 0.44 32.91 ?  7   SER   B HB3  1 
ATOM   4042 H  HG   A SER   B 1 7   ? 47.870 -25.798 -22.928 0.56 38.42 ?  7   SER   B HG   1 
ATOM   4043 H  HG   B SER   B 1 7   ? 47.268 -25.231 -23.471 0.44 33.60 ?  7   SER   B HG   1 
ATOM   4044 N  N    A GLY   B 1 8   ? 44.980 -27.399 -20.772 0.56 27.91 ?  8   GLY   B N    1 
ATOM   4045 N  N    B GLY   B 1 8   ? 44.751 -27.301 -20.942 0.44 25.66 ?  8   GLY   B N    1 
ATOM   4046 C  CA   A GLY   B 1 8   ? 44.974 -28.787 -20.365 0.56 26.79 ?  8   GLY   B CA   1 
ATOM   4047 C  CA   B GLY   B 1 8   ? 44.671 -28.709 -20.621 0.44 24.77 ?  8   GLY   B CA   1 
ATOM   4048 C  C    A GLY   B 1 8   ? 44.045 -29.116 -19.225 0.56 25.57 ?  8   GLY   B C    1 
ATOM   4049 C  C    B GLY   B 1 8   ? 43.803 -29.053 -19.438 0.44 23.77 ?  8   GLY   B C    1 
ATOM   4050 O  O    A GLY   B 1 8   ? 44.244 -30.140 -18.562 0.56 26.74 ?  8   GLY   B O    1 
ATOM   4051 O  O    B GLY   B 1 8   ? 43.959 -30.141 -18.873 0.44 24.58 ?  8   GLY   B O    1 
ATOM   4052 H  H    A GLY   B 1 8   ? 44.490 -27.231 -21.455 0.56 33.51 ?  8   GLY   B H    1 
ATOM   4053 H  H    B GLY   B 1 8   ? 44.254 -27.060 -21.598 0.44 30.81 ?  8   GLY   B H    1 
ATOM   4054 H  HA2  A GLY   B 1 8   ? 44.729 -29.339 -21.124 0.56 32.17 ?  8   GLY   B HA2  1 
ATOM   4055 H  HA2  B GLY   B 1 8   ? 44.313 -29.185 -21.383 0.44 29.74 ?  8   GLY   B HA2  1 
ATOM   4056 H  HA3  A GLY   B 1 8   ? 45.864 -29.042 -20.083 0.56 32.17 ?  8   GLY   B HA3  1 
ATOM   4057 H  HA3  B GLY   B 1 8   ? 45.562 -29.045 -20.444 0.44 29.74 ?  8   GLY   B HA3  1 
ATOM   4058 N  N    A TYR   B 1 9   ? 43.031 -28.290 -18.974 0.56 23.63 ?  9   TYR   B N    1 
ATOM   4059 N  N    B TYR   B 1 9   ? 42.873 -28.181 -19.057 0.44 22.30 ?  9   TYR   B N    1 
ATOM   4060 C  CA   A TYR   B 1 9   ? 42.083 -28.559 -17.905 0.56 21.67 ?  9   TYR   B CA   1 
ATOM   4061 C  CA   B TYR   B 1 9   ? 41.988 -28.461 -17.939 0.44 21.00 ?  9   TYR   B CA   1 
ATOM   4062 C  C    A TYR   B 1 9   ? 40.887 -29.344 -18.419 0.56 21.08 ?  9   TYR   B C    1 
ATOM   4063 C  C    B TYR   B 1 9   ? 40.785 -29.264 -18.401 0.44 20.72 ?  9   TYR   B C    1 
ATOM   4064 O  O    A TYR   B 1 9   ? 40.497 -29.241 -19.586 0.56 22.20 ?  9   TYR   B O    1 
ATOM   4065 O  O    B TYR   B 1 9   ? 40.284 -29.088 -19.515 0.44 21.94 ?  9   TYR   B O    1 
ATOM   4066 C  CB   A TYR   B 1 9   ? 41.608 -27.263 -17.247 0.56 21.00 ?  9   TYR   B CB   1 
ATOM   4067 C  CB   B TYR   B 1 9   ? 41.496 -27.172 -17.285 0.44 20.45 ?  9   TYR   B CB   1 
ATOM   4068 C  CG   A TYR   B 1 9   ? 42.652 -26.656 -16.335 0.56 20.38 ?  9   TYR   B CG   1 
ATOM   4069 C  CG   B TYR   B 1 9   ? 42.524 -26.541 -16.385 0.44 19.91 ?  9   TYR   B CG   1 
ATOM   4070 C  CD1  A TYR   B 1 9   ? 43.774 -26.027 -16.856 0.56 20.34 ?  9   TYR   B CD1  1 
ATOM   4071 C  CD1  B TYR   B 1 9   ? 43.571 -25.806 -16.914 0.44 19.74 ?  9   TYR   B CD1  1 
ATOM   4072 C  CD2  A TYR   B 1 9   ? 42.525 -26.727 -14.955 0.56 19.86 ?  9   TYR   B CD2  1 
ATOM   4073 C  CD2  B TYR   B 1 9   ? 42.457 -26.691 -15.008 0.44 19.35 ?  9   TYR   B CD2  1 
ATOM   4074 C  CE1  A TYR   B 1 9   ? 44.740 -25.480 -16.028 0.56 20.32 ?  9   TYR   B CE1  1 
ATOM   4075 C  CE1  B TYR   B 1 9   ? 44.523 -25.230 -16.099 0.44 19.62 ?  9   TYR   B CE1  1 
ATOM   4076 C  CE2  A TYR   B 1 9   ? 43.486 -26.184 -14.118 0.56 19.93 ?  9   TYR   B CE2  1 
ATOM   4077 C  CE2  B TYR   B 1 9   ? 43.407 -26.121 -14.182 0.44 19.45 ?  9   TYR   B CE2  1 
ATOM   4078 C  CZ   A TYR   B 1 9   ? 44.592 -25.558 -14.662 0.56 20.44 ?  9   TYR   B CZ   1 
ATOM   4079 C  CZ   B TYR   B 1 9   ? 44.439 -25.387 -14.734 0.44 19.72 ?  9   TYR   B CZ   1 
ATOM   4080 O  OH   A TYR   B 1 9   ? 45.551 -25.020 -13.836 0.56 20.94 ?  9   TYR   B OH   1 
ATOM   4081 O  OH   B TYR   B 1 9   ? 45.389 -24.815 -13.922 0.44 20.43 ?  9   TYR   B OH   1 
ATOM   4082 H  H    A TYR   B 1 9   ? 42.864 -27.568 -19.415 0.56 28.37 ?  9   TYR   B H    1 
ATOM   4083 H  H    B TYR   B 1 9   ? 42.720 -27.425 -19.442 0.44 26.79 ?  9   TYR   B H    1 
ATOM   4084 H  HA   A TYR   B 1 9   ? 42.512 -29.093 -17.225 0.56 26.02 ?  9   TYR   B HA   1 
ATOM   4085 H  HA   B TYR   B 1 9   ? 42.458 -28.976 -17.269 0.44 25.23 ?  9   TYR   B HA   1 
ATOM   4086 H  HB2  A TYR   B 1 9   ? 41.390 -26.610 -17.931 0.56 25.22 ?  9   TYR   B HB2  1 
ATOM   4087 H  HB2  B TYR   B 1 9   ? 41.254 -26.527 -17.970 0.44 24.56 ?  9   TYR   B HB2  1 
ATOM   4088 H  HB3  A TYR   B 1 9   ? 40.825 -27.457 -16.710 0.56 25.22 ?  9   TYR   B HB3  1 
ATOM   4089 H  HB3  B TYR   B 1 9   ? 40.726 -27.388 -16.744 0.44 24.56 ?  9   TYR   B HB3  1 
ATOM   4090 H  HD1  A TYR   B 1 9   ? 43.876 -25.973 -17.778 0.56 24.43 ?  9   TYR   B HD1  1 
ATOM   4091 H  HD1  B TYR   B 1 9   ? 43.632 -25.698 -17.835 0.44 23.71 ?  9   TYR   B HD1  1 
ATOM   4092 H  HD2  A TYR   B 1 9   ? 41.777 -27.150 -14.586 0.56 23.86 ?  9   TYR   B HD2  1 
ATOM   4093 H  HD2  B TYR   B 1 9   ? 41.757 -27.185 -14.634 0.44 23.24 ?  9   TYR   B HD2  1 
ATOM   4094 H  HE1  A TYR   B 1 9   ? 45.481 -25.063 -16.395 0.56 24.41 ?  9   TYR   B HE1  1 
ATOM   4095 H  HE1  B TYR   B 1 9   ? 45.218 -24.742 -16.469 0.44 23.57 ?  9   TYR   B HE1  1 
ATOM   4096 H  HE2  A TYR   B 1 9   ? 43.379 -26.241 -13.194 0.56 23.93 ?  9   TYR   B HE2  1 
ATOM   4097 H  HE2  B TYR   B 1 9   ? 43.342 -26.231 -13.260 0.44 23.36 ?  9   TYR   B HE2  1 
ATOM   4098 H  HH   A TYR   B 1 9   ? 46.160 -24.678 -14.295 0.56 25.15 ?  9   TYR   B HH   1 
ATOM   4099 H  HH   B TYR   B 1 9   ? 45.949 -24.409 -14.392 0.44 24.54 ?  9   TYR   B HH   1 
ATOM   4100 N  N    . LEU   B 1 10  ? 40.324 -30.152 -17.525 1.00 19.93 ?  10  LEU   B N    1 
ATOM   4101 C  CA   . LEU   B 1 10  ? 39.127 -30.928 -17.780 1.00 20.12 ?  10  LEU   B CA   1 
ATOM   4102 C  C    . LEU   B 1 10  ? 37.946 -30.148 -17.225 1.00 19.90 ?  10  LEU   B C    1 
ATOM   4103 O  O    . LEU   B 1 10  ? 37.972 -29.708 -16.071 1.00 19.21 ?  10  LEU   B O    1 
ATOM   4104 C  CB   . LEU   B 1 10  ? 39.231 -32.283 -17.081 1.00 21.08 ?  10  LEU   B CB   1 
ATOM   4105 C  CG   . LEU   B 1 10  ? 38.100 -33.259 -17.392 1.00 22.58 ?  10  LEU   B CG   1 
ATOM   4106 C  CD1  . LEU   B 1 10  ? 38.262 -33.800 -18.803 1.00 23.63 ?  10  LEU   B CD1  1 
ATOM   4107 C  CD2  . LEU   B 1 10  ? 38.053 -34.384 -16.373 1.00 23.30 ?  10  LEU   B CD2  1 
ATOM   4108 H  H    A LEU   B 1 10  ? 40.630 -30.268 -16.727 0.56 23.93 ?  10  LEU   B H    1 
ATOM   4109 H  H    B LEU   B 1 10  ? 40.686 -30.321 -16.761 0.44 23.93 ?  10  LEU   B H    1 
ATOM   4110 H  HA   . LEU   B 1 10  ? 39.001 -31.063 -18.730 1.00 24.16 ?  10  LEU   B HA   1 
ATOM   4111 H  HB2  . LEU   B 1 10  ? 40.063 -32.702 -17.351 1.00 25.32 ?  10  LEU   B HB2  1 
ATOM   4112 H  HB3  . LEU   B 1 10  ? 39.237 -32.136 -16.122 1.00 25.32 ?  10  LEU   B HB3  1 
ATOM   4113 H  HG   . LEU   B 1 10  ? 37.254 -32.785 -17.351 1.00 27.11 ?  10  LEU   B HG   1 
ATOM   4114 H  HD11 . LEU   B 1 10  ? 37.569 -34.459 -18.967 1.00 28.37 ?  10  LEU   B HD11 1 
ATOM   4115 H  HD12 . LEU   B 1 10  ? 38.177 -33.068 -19.433 1.00 28.37 ?  10  LEU   B HD12 1 
ATOM   4116 H  HD13 . LEU   B 1 10  ? 39.136 -34.210 -18.884 1.00 28.37 ?  10  LEU   B HD13 1 
ATOM   4117 H  HD21 . LEU   B 1 10  ? 37.327 -34.983 -16.603 1.00 27.98 ?  10  LEU   B HD21 1 
ATOM   4118 H  HD22 . LEU   B 1 10  ? 38.897 -34.857 -16.390 1.00 27.98 ?  10  LEU   B HD22 1 
ATOM   4119 H  HD23 . LEU   B 1 10  ? 37.902 -34.001 -15.494 1.00 27.98 ?  10  LEU   B HD23 1 
ATOM   4120 N  N    A LYS   B 1 11  ? 36.925 -29.969 -18.053 0.56 20.95 ?  11  LYS   B N    1 
ATOM   4121 N  N    B LYS   B 1 11  ? 36.912 -29.986 -18.044 0.44 21.04 ?  11  LYS   B N    1 
ATOM   4122 C  CA   A LYS   B 1 11  ? 35.723 -29.262 -17.646 0.56 22.79 ?  11  LYS   B CA   1 
ATOM   4123 C  CA   B LYS   B 1 11  ? 35.723 -29.245 -17.646 0.44 22.75 ?  11  LYS   B CA   1 
ATOM   4124 C  C    A LYS   B 1 11  ? 34.876 -30.185 -16.777 0.56 21.58 ?  11  LYS   B C    1 
ATOM   4125 C  C    B LYS   B 1 11  ? 34.824 -30.146 -16.806 0.44 21.64 ?  11  LYS   B C    1 
ATOM   4126 O  O    A LYS   B 1 11  ? 34.559 -31.310 -17.179 0.56 22.60 ?  11  LYS   B O    1 
ATOM   4127 O  O    B LYS   B 1 11  ? 34.396 -31.209 -17.269 0.44 22.51 ?  11  LYS   B O    1 
ATOM   4128 C  CB   A LYS   B 1 11  ? 34.952 -28.841 -18.899 0.56 26.34 ?  11  LYS   B CB   1 
ATOM   4129 C  CB   B LYS   B 1 11  ? 34.986 -28.776 -18.900 0.44 25.93 ?  11  LYS   B CB   1 
ATOM   4130 C  CG   A LYS   B 1 11  ? 33.870 -27.800 -18.680 0.56 29.49 ?  11  LYS   B CG   1 
ATOM   4131 C  CG   B LYS   B 1 11  ? 33.861 -27.790 -18.653 0.44 28.76 ?  11  LYS   B CG   1 
ATOM   4132 C  CD   A LYS   B 1 11  ? 33.165 -27.473 -19.992 0.56 31.89 ?  11  LYS   B CD   1 
ATOM   4133 C  CD   B LYS   B 1 11  ? 33.126 -27.478 -19.950 0.44 30.97 ?  11  LYS   B CD   1 
ATOM   4134 C  CE   A LYS   B 1 11  ? 32.162 -26.345 -19.823 0.56 33.63 ?  11  LYS   B CE   1 
ATOM   4135 C  CE   B LYS   B 1 11  ? 32.096 -26.376 -19.764 0.44 32.55 ?  11  LYS   B CE   1 
ATOM   4136 N  NZ   A LYS   B 1 11  ? 32.833 -25.051 -19.524 0.56 34.62 ?  11  LYS   B NZ   1 
ATOM   4137 N  NZ   B LYS   B 1 11  ? 32.732 -25.054 -19.502 0.44 33.44 ?  11  LYS   B NZ   1 
ATOM   4138 H  H    A LYS   B 1 11  ? 36.896 -30.258 -18.862 0.56 25.17 ?  11  LYS   B H    1 
ATOM   4139 H  H    B LYS   B 1 11  ? 36.871 -30.299 -18.845 0.44 25.27 ?  11  LYS   B H    1 
ATOM   4140 H  HA   A LYS   B 1 11  ? 35.951 -28.468 -17.140 0.56 27.37 ?  11  LYS   B HA   1 
ATOM   4141 H  HA   B LYS   B 1 11  ? 35.972 -28.470 -17.121 0.44 27.32 ?  11  LYS   B HA   1 
ATOM   4142 H  HB2  A LYS   B 1 11  ? 35.584 -28.468 -19.539 0.56 31.63 ?  11  LYS   B HB2  1 
ATOM   4143 H  HB2  B LYS   B 1 11  ? 35.625 -28.347 -19.491 0.44 31.14 ?  11  LYS   B HB2  1 
ATOM   4144 H  HB3  A LYS   B 1 11  ? 34.528 -29.622 -19.285 0.56 31.63 ?  11  LYS   B HB3  1 
ATOM   4145 H  HB3  B LYS   B 1 11  ? 34.603 -29.549 -19.343 0.44 31.14 ?  11  LYS   B HB3  1 
ATOM   4146 H  HG2  A LYS   B 1 11  ? 33.211 -28.145 -18.059 0.56 35.41 ?  11  LYS   B HG2  1 
ATOM   4147 H  HG2  B LYS   B 1 11  ? 33.227 -28.173 -18.027 0.44 34.54 ?  11  LYS   B HG2  1 
ATOM   4148 H  HG3  A LYS   B 1 11  ? 34.268 -26.985 -18.337 0.56 35.41 ?  11  LYS   B HG3  1 
ATOM   4149 H  HG3  B LYS   B 1 11  ? 34.228 -26.963 -18.303 0.44 34.54 ?  11  LYS   B HG3  1 
ATOM   4150 H  HD2  A LYS   B 1 11  ? 33.823 -27.196 -20.651 0.56 38.30 ?  11  LYS   B HD2  1 
ATOM   4151 H  HD2  B LYS   B 1 11  ? 33.767 -27.186 -20.618 0.44 37.18 ?  11  LYS   B HD2  1 
ATOM   4152 H  HD3  A LYS   B 1 11  ? 32.690 -28.259 -20.307 0.56 38.30 ?  11  LYS   B HD3  1 
ATOM   4153 H  HD3  B LYS   B 1 11  ? 32.666 -28.276 -20.256 0.44 37.18 ?  11  LYS   B HD3  1 
ATOM   4154 H  HE2  A LYS   B 1 11  ? 31.654 -26.242 -20.643 0.56 40.38 ?  11  LYS   B HE2  1 
ATOM   4155 H  HE2  B LYS   B 1 11  ? 31.562 -26.300 -20.570 0.44 39.09 ?  11  LYS   B HE2  1 
ATOM   4156 H  HE3  A LYS   B 1 11  ? 31.567 -26.558 -19.086 0.56 40.38 ?  11  LYS   B HE3  1 
ATOM   4157 H  HE3  B LYS   B 1 11  ? 31.530 -26.597 -19.008 0.44 39.09 ?  11  LYS   B HE3  1 
ATOM   4158 H  HZ1  A LYS   B 1 11  ? 32.226 -24.405 -19.449 0.56 41.56 ?  11  LYS   B HZ1  1 
ATOM   4159 H  HZ1  B LYS   B 1 11  ? 32.107 -24.425 -19.427 0.44 40.15 ?  11  LYS   B HZ1  1 
ATOM   4160 H  HZ2  A LYS   B 1 11  ? 33.286 -25.114 -18.761 0.56 41.56 ?  11  LYS   B HZ2  1 
ATOM   4161 H  HZ2  B LYS   B 1 11  ? 33.202 -25.087 -18.747 0.44 40.15 ?  11  LYS   B HZ2  1 
ATOM   4162 H  HZ3  A LYS   B 1 11  ? 33.398 -24.844 -20.180 0.56 41.56 ?  11  LYS   B HZ3  1 
ATOM   4163 H  HZ3  B LYS   B 1 11  ? 33.277 -24.841 -20.173 0.44 40.15 ?  11  LYS   B HZ3  1 
ATOM   4164 N  N    . LEU   B 1 12  ? 34.532 -29.723 -15.575 1.00 20.01 ?  12  LEU   B N    1 
ATOM   4165 C  CA   . LEU   B 1 12  ? 33.592 -30.433 -14.710 1.00 18.68 ?  12  LEU   B CA   1 
ATOM   4166 C  C    . LEU   B 1 12  ? 32.201 -29.826 -14.778 1.00 18.60 ?  12  LEU   B C    1 
ATOM   4167 O  O    . LEU   B 1 12  ? 31.211 -30.542 -14.935 1.00 19.50 ?  12  LEU   B O    1 
ATOM   4168 C  CB   . LEU   B 1 12  ? 34.072 -30.450 -13.253 1.00 17.80 ?  12  LEU   B CB   1 
ATOM   4169 C  CG   . LEU   B 1 12  ? 35.402 -31.148 -12.984 1.00 17.84 ?  12  LEU   B CG   1 
ATOM   4170 C  CD1  . LEU   B 1 12  ? 35.756 -31.091 -11.509 1.00 17.75 ?  12  LEU   B CD1  1 
ATOM   4171 C  CD2  . LEU   B 1 12  ? 35.381 -32.587 -13.476 1.00 18.59 ?  12  LEU   B CD2  1 
ATOM   4172 H  H    A LEU   B 1 12  ? 34.832 -28.989 -15.235 0.56 24.03 ?  12  LEU   B H    1 
ATOM   4173 H  H    B LEU   B 1 12  ? 34.864 -29.012 -15.218 0.44 24.03 ?  12  LEU   B H    1 
ATOM   4174 H  HA   . LEU   B 1 12  ? 33.519 -31.348 -15.010 1.00 22.44 ?  12  LEU   B HA   1 
ATOM   4175 H  HB2  . LEU   B 1 12  ? 34.156 -29.534 -12.950 1.00 21.38 ?  12  LEU   B HB2  1 
ATOM   4176 H  HB3  . LEU   B 1 12  ? 33.395 -30.902 -12.721 1.00 21.38 ?  12  LEU   B HB3  1 
ATOM   4177 H  HG   . LEU   B 1 12  ? 36.096 -30.679 -13.469 1.00 21.43 ?  12  LEU   B HG   1 
ATOM   4178 H  HD11 . LEU   B 1 12  ? 36.608 -31.538 -11.372 1.00 21.33 ?  12  LEU   B HD11 1 
ATOM   4179 H  HD12 . LEU   B 1 12  ? 35.823 -30.164 -11.232 1.00 21.33 ?  12  LEU   B HD12 1 
ATOM   4180 H  HD13 . LEU   B 1 12  ? 35.064 -31.540 -10.998 1.00 21.33 ?  12  LEU   B HD13 1 
ATOM   4181 H  HD21 . LEU   B 1 12  ? 36.184 -33.037 -13.171 1.00 22.33 ?  12  LEU   B HD21 1 
ATOM   4182 H  HD22 . LEU   B 1 12  ? 34.596 -33.033 -13.120 1.00 22.33 ?  12  LEU   B HD22 1 
ATOM   4183 H  HD23 . LEU   B 1 12  ? 35.349 -32.590 -14.446 1.00 22.33 ?  12  LEU   B HD23 1 
ATOM   4184 N  N    . THR   B 1 13  ? 32.117 -28.507 -14.663 1.00 18.43 ?  13  THR   B N    1 
ATOM   4185 C  CA   . THR   B 1 13  ? 30.894 -27.753 -14.866 1.00 18.68 ?  13  THR   B CA   1 
ATOM   4186 C  C    . THR   B 1 13  ? 31.239 -26.566 -15.758 1.00 20.96 ?  13  THR   B C    1 
ATOM   4187 O  O    . THR   B 1 13  ? 32.389 -26.388 -16.176 1.00 22.30 ?  13  THR   B O    1 
ATOM   4188 C  CB   . THR   B 1 13  ? 30.308 -27.264 -13.538 1.00 18.13 ?  13  THR   B CB   1 
ATOM   4189 O  OG1  . THR   B 1 13  ? 31.155 -26.238 -13.003 1.00 17.57 ?  13  THR   B OG1  1 
ATOM   4190 C  CG2  . THR   B 1 13  ? 30.200 -28.403 -12.542 1.00 18.58 ?  13  THR   B CG2  1 
ATOM   4191 H  H    . THR   B 1 13  ? 32.789 -28.004 -14.464 1.00 22.14 ?  13  THR   B H    1 
ATOM   4192 H  HA   . THR   B 1 13  ? 30.233 -28.311 -15.310 1.00 22.43 ?  13  THR   B HA   1 
ATOM   4193 H  HB   . THR   B 1 13  ? 29.417 -26.898 -13.692 1.00 21.78 ?  13  THR   B HB   1 
ATOM   4194 H  HG1  . THR   B 1 13  ? 30.839 -25.473 -13.196 1.00 21.10 ?  13  THR   B HG1  1 
ATOM   4195 H  HG21 . THR   B 1 13  ? 29.706 -28.112 -11.759 1.00 22.32 ?  13  THR   B HG21 1 
ATOM   4196 H  HG22 . THR   B 1 13  ? 29.736 -29.151 -12.947 1.00 22.32 ?  13  THR   B HG22 1 
ATOM   4197 H  HG23 . THR   B 1 13  ? 31.085 -28.688 -12.270 1.00 22.32 ?  13  THR   B HG23 1 
ATOM   4198 N  N    A ASP   B 1 14  ? 30.238 -25.732 -16.037 0.56 22.06 ?  14  ASP   B N    1 
ATOM   4199 N  N    B ASP   B 1 14  ? 30.238 -25.730 -16.040 0.44 21.87 ?  14  ASP   B N    1 
ATOM   4200 C  CA   A ASP   B 1 14  ? 30.478 -24.586 -16.904 0.56 23.57 ?  14  ASP   B CA   1 
ATOM   4201 C  CA   B ASP   B 1 14  ? 30.469 -24.581 -16.908 0.44 23.05 ?  14  ASP   B CA   1 
ATOM   4202 C  C    A ASP   B 1 14  ? 31.589 -23.694 -16.366 0.56 21.69 ?  14  ASP   B C    1 
ATOM   4203 C  C    B ASP   B 1 14  ? 31.515 -23.624 -16.353 0.44 21.37 ?  14  ASP   B C    1 
ATOM   4204 O  O    A ASP   B 1 14  ? 32.295 -23.052 -17.152 0.56 22.77 ?  14  ASP   B O    1 
ATOM   4205 O  O    B ASP   B 1 14  ? 32.073 -22.835 -17.122 0.44 22.19 ?  14  ASP   B O    1 
ATOM   4206 C  CB   A ASP   B 1 14  ? 29.189 -23.789 -17.106 0.56 26.92 ?  14  ASP   B CB   1 
ATOM   4207 C  CB   B ASP   B 1 14  ? 29.168 -23.817 -17.154 0.44 25.88 ?  14  ASP   B CB   1 
ATOM   4208 C  CG   A ASP   B 1 14  ? 28.196 -24.498 -18.005 0.56 30.03 ?  14  ASP   B CG   1 
ATOM   4209 C  CG   B ASP   B 1 14  ? 28.276 -24.498 -18.173 0.44 28.39 ?  14  ASP   B CG   1 
ATOM   4210 O  OD1  A ASP   B 1 14  ? 28.556 -25.527 -18.621 0.56 30.84 ?  14  ASP   B OD1  1 
ATOM   4211 O  OD1  B ASP   B 1 14  ? 28.808 -25.209 -19.052 0.44 29.11 ?  14  ASP   B OD1  1 
ATOM   4212 O  OD2  A ASP   B 1 14  ? 27.042 -24.029 -18.086 0.56 31.56 -1 14  ASP   B OD2  1 
ATOM   4213 O  OD2  B ASP   B 1 14  ? 27.042 -24.328 -18.095 0.44 29.58 -1 14  ASP   B OD2  1 
ATOM   4214 H  H    A ASP   B 1 14  ? 29.436 -25.794 -15.737 0.56 26.50 ?  14  ASP   B H    1 
ATOM   4215 H  H    B ASP   B 1 14  ? 29.435 -25.801 -15.746 0.44 26.27 ?  14  ASP   B H    1 
ATOM   4216 H  HA   A ASP   B 1 14  ? 30.770 -24.899 -17.771 0.56 28.31 ?  14  ASP   B HA   1 
ATOM   4217 H  HA   B ASP   B 1 14  ? 30.794 -24.896 -17.764 0.44 27.68 ?  14  ASP   B HA   1 
ATOM   4218 H  HB2  A ASP   B 1 14  ? 28.748 -23.667 -16.255 0.56 32.33 ?  14  ASP   B HB2  1 
ATOM   4219 H  HB2  B ASP   B 1 14  ? 28.676 -23.755 -16.323 0.44 31.08 ?  14  ASP   B HB2  1 
ATOM   4220 H  HB3  A ASP   B 1 14  ? 29.399 -22.928 -17.502 0.56 32.33 ?  14  ASP   B HB3  1 
ATOM   4221 H  HB3  B ASP   B 1 14  ? 29.383 -22.926 -17.481 0.44 31.08 ?  14  ASP   B HB3  1 
ATOM   4222 N  N    . ASN   B 1 15  ? 31.783 -23.659 -15.043 1.00 19.00 ?  15  ASN   B N    1 
ATOM   4223 C  CA   . ASN   B 1 15  ? 32.752 -22.748 -14.436 1.00 16.72 ?  15  ASN   B CA   1 
ATOM   4224 C  C    . ASN   B 1 15  ? 33.845 -23.410 -13.604 1.00 15.31 ?  15  ASN   B C    1 
ATOM   4225 O  O    . ASN   B 1 15  ? 34.719 -22.692 -13.101 1.00 15.63 ?  15  ASN   B O    1 
ATOM   4226 C  CB   . ASN   B 1 15  ? 32.052 -21.691 -13.566 1.00 16.82 ?  15  ASN   B CB   1 
ATOM   4227 C  CG   . ASN   B 1 15  ? 31.423 -22.295 -12.328 1.00 16.51 ?  15  ASN   B CG   1 
ATOM   4228 O  OD1  . ASN   B 1 15  ? 30.474 -23.076 -12.418 1.00 18.10 ?  15  ASN   B OD1  1 
ATOM   4229 N  ND2  . ASN   B 1 15  ? 31.957 -21.960 -11.168 1.00 15.17 ?  15  ASN   B ND2  1 
ATOM   4230 H  H    A ASN   B 1 15  ? 31.361 -24.152 -14.478 0.56 22.82 ?  15  ASN   B H    1 
ATOM   4231 H  H    B ASN   B 1 15  ? 31.395 -24.184 -14.483 0.44 22.82 ?  15  ASN   B H    1 
ATOM   4232 H  HA   . ASN   B 1 15  ? 33.199 -22.263 -15.140 1.00 20.08 ?  15  ASN   B HA   1 
ATOM   4233 H  HB2  . ASN   B 1 15  ? 32.705 -21.022 -13.284 1.00 20.21 ?  15  ASN   B HB2  1 
ATOM   4234 H  HB3  . ASN   B 1 15  ? 31.350 -21.254 -14.083 1.00 20.21 ?  15  ASN   B HB3  1 
ATOM   4235 H  HD21 . ASN   B 1 15  ? 31.630 -22.273 -10.437 1.00 18.22 ?  15  ASN   B HD21 1 
ATOM   4236 H  HD22 . ASN   B 1 15  ? 32.630 -21.417 -11.134 1.00 18.22 ?  15  ASN   B HD22 1 
ATOM   4237 N  N    . VAL   B 1 16  ? 33.834 -24.730 -13.436 1.00 15.16 ?  16  VAL   B N    1 
ATOM   4238 C  CA   . VAL   B 1 16  ? 34.836 -25.420 -12.629 1.00 14.76 ?  16  VAL   B CA   1 
ATOM   4239 C  C    . VAL   B 1 16  ? 35.621 -26.360 -13.527 1.00 14.93 ?  16  VAL   B C    1 
ATOM   4240 O  O    . VAL   B 1 16  ? 35.043 -27.243 -14.180 1.00 15.81 ?  16  VAL   B O    1 
ATOM   4241 C  CB   . VAL   B 1 16  ? 34.215 -26.184 -11.451 1.00 14.93 ?  16  VAL   B CB   1 
ATOM   4242 C  CG1  . VAL   B 1 16  ? 35.294 -26.937 -10.671 1.00 14.68 ?  16  VAL   B CG1  1 
ATOM   4243 C  CG2  . VAL   B 1 16  ? 33.433 -25.233 -10.549 1.00 15.62 ?  16  VAL   B CG2  1 
ATOM   4244 H  H    . VAL   B 1 16  ? 33.240 -25.257 -13.783 1.00 18.22 ?  16  VAL   B H    1 
ATOM   4245 H  HA   . VAL   B 1 16  ? 35.448 -24.765 -12.267 1.00 17.73 ?  16  VAL   B HA   1 
ATOM   4246 H  HB   . VAL   B 1 16  ? 33.585 -26.839 -11.797 1.00 17.94 ?  16  VAL   B HB   1 
ATOM   4247 H  HG11 . VAL   B 1 16  ? 34.921 -27.229 -9.823  1.00 17.64 ?  16  VAL   B HG11 1 
ATOM   4248 H  HG12 . VAL   B 1 16  ? 35.579 -27.705 -11.187 1.00 17.64 ?  16  VAL   B HG12 1 
ATOM   4249 H  HG13 . VAL   B 1 16  ? 36.040 -26.340 -10.515 1.00 17.64 ?  16  VAL   B HG13 1 
ATOM   4250 H  HG21 . VAL   B 1 16  ? 33.093 -25.726 -9.785  1.00 18.77 ?  16  VAL   B HG21 1 
ATOM   4251 H  HG22 . VAL   B 1 16  ? 34.020 -24.524 -10.251 1.00 18.77 ?  16  VAL   B HG22 1 
ATOM   4252 H  HG23 . VAL   B 1 16  ? 32.690 -24.856 -11.052 1.00 18.77 ?  16  VAL   B HG23 1 
ATOM   4253 N  N    . TYR   B 1 17  ? 36.939 -26.187 -13.519 1.00 14.89 ?  17  TYR   B N    1 
ATOM   4254 C  CA   . TYR   B 1 17  ? 37.877 -26.939 -14.334 1.00 15.65 ?  17  TYR   B CA   1 
ATOM   4255 C  C    . TYR   B 1 17  ? 38.933 -27.556 -13.427 1.00 14.63 ?  17  TYR   B C    1 
ATOM   4256 O  O    . TYR   B 1 17  ? 39.233 -27.023 -12.356 1.00 14.62 ?  17  TYR   B O    1 
ATOM   4257 C  CB   . TYR   B 1 17  ? 38.584 -26.015 -15.332 1.00 19.30 ?  17  TYR   B CB   1 
ATOM   4258 C  CG   . TYR   B 1 17  ? 37.660 -25.242 -16.242 1.00 23.24 ?  17  TYR   B CG   1 
ATOM   4259 C  CD1  . TYR   B 1 17  ? 37.118 -24.024 -15.851 1.00 25.39 ?  17  TYR   B CD1  1 
ATOM   4260 C  CD2  . TYR   B 1 17  ? 37.331 -25.732 -17.499 1.00 25.75 ?  17  TYR   B CD2  1 
ATOM   4261 C  CE1  . TYR   B 1 17  ? 36.269 -23.315 -16.688 1.00 27.33 ?  17  TYR   B CE1  1 
ATOM   4262 C  CE2  . TYR   B 1 17  ? 36.490 -25.033 -18.342 1.00 27.54 ?  17  TYR   B CE2  1 
ATOM   4263 C  CZ   . TYR   B 1 17  ? 35.959 -23.827 -17.932 1.00 28.25 ?  17  TYR   B CZ   1 
ATOM   4264 O  OH   . TYR   B 1 17  ? 35.123 -23.131 -18.772 1.00 29.52 ?  17  TYR   B OH   1 
ATOM   4265 H  H    . TYR   B 1 17  ? 37.334 -25.599 -13.018 1.00 17.89 ?  17  TYR   B H    1 
ATOM   4266 H  HA   . TYR   B 1 17  ? 37.408 -27.639 -14.819 1.00 18.80 ?  17  TYR   B HA   1 
ATOM   4267 H  HB2  . TYR   B 1 17  ? 39.134 -25.383 -14.849 1.00 23.18 ?  17  TYR   B HB2  1 
ATOM   4268 H  HB3  . TYR   B 1 17  ? 39.131 -26.565 -15.901 1.00 23.18 ?  17  TYR   B HB3  1 
ATOM   4269 H  HD1  . TYR   B 1 17  ? 37.325 -23.678 -15.015 1.00 30.48 ?  17  TYR   B HD1  1 
ATOM   4270 H  HD2  . TYR   B 1 17  ? 37.682 -26.544 -17.782 1.00 30.93 ?  17  TYR   B HD2  1 
ATOM   4271 H  HE1  . TYR   B 1 17  ? 35.913 -22.500 -16.415 1.00 32.82 ?  17  TYR   B HE1  1 
ATOM   4272 H  HE2  . TYR   B 1 17  ? 36.276 -25.375 -19.182 1.00 33.07 ?  17  TYR   B HE2  1 
ATOM   4273 H  HH   . TYR   B 1 17  ? 35.018 -23.552 -19.491 1.00 35.45 ?  17  TYR   B HH   1 
ATOM   4274 N  N    . ILE   B 1 18  ? 39.532 -28.661 -13.864 1.00 15.00 ?  18  ILE   B N    1 
ATOM   4275 C  CA   . ILE   B 1 18  ? 40.460 -29.391 -13.009 1.00 15.04 ?  18  ILE   B CA   1 
ATOM   4276 C  C    . ILE   B 1 18  ? 41.612 -29.946 -13.836 1.00 15.52 ?  18  ILE   B C    1 
ATOM   4277 O  O    . ILE   B 1 18  ? 41.443 -30.330 -14.997 1.00 16.97 ?  18  ILE   B O    1 
ATOM   4278 C  CB   . ILE   B 1 18  ? 39.715 -30.491 -12.211 1.00 15.44 ?  18  ILE   B CB   1 
ATOM   4279 C  CG1  . ILE   B 1 18  ? 40.575 -31.044 -11.071 1.00 15.94 ?  18  ILE   B CG1  1 
ATOM   4280 C  CG2  . ILE   B 1 18  ? 39.210 -31.610 -13.138 1.00 15.87 ?  18  ILE   B CG2  1 
ATOM   4281 C  CD1  . ILE   B 1 18  ? 39.772 -31.846 -10.065 1.00 17.48 ?  18  ILE   B CD1  1 
ATOM   4282 H  H    . ILE   B 1 18  ? 39.417 -29.000 -14.643 1.00 18.02 ?  18  ILE   B H    1 
ATOM   4283 H  HA   . ILE   B 1 18  ? 40.827 -28.772 -12.356 1.00 18.07 ?  18  ILE   B HA   1 
ATOM   4284 H  HB   . ILE   B 1 18  ? 38.931 -30.088 -11.805 1.00 18.55 ?  18  ILE   B HB   1 
ATOM   4285 H  HG12 . ILE   B 1 18  ? 41.258 -31.621 -11.440 1.00 19.15 ?  18  ILE   B HG12 1 
ATOM   4286 H  HG13 . ILE   B 1 18  ? 40.984 -30.299 -10.601 1.00 19.15 ?  18  ILE   B HG13 1 
ATOM   4287 H  HG21 . ILE   B 1 18  ? 38.621 -32.199 -12.635 1.00 19.06 ?  18  ILE   B HG21 1 
ATOM   4288 H  HG22 . ILE   B 1 18  ? 38.720 -31.210 -13.874 1.00 19.06 ?  18  ILE   B HG22 1 
ATOM   4289 H  HG23 . ILE   B 1 18  ? 39.967 -32.110 -13.475 1.00 19.06 ?  18  ILE   B HG23 1 
ATOM   4290 H  HD11 . ILE   B 1 18  ? 40.359 -32.120 -9.342  1.00 21.00 ?  18  ILE   B HD11 1 
ATOM   4291 H  HD12 . ILE   B 1 18  ? 39.056 -31.292 -9.717  1.00 21.00 ?  18  ILE   B HD12 1 
ATOM   4292 H  HD13 . ILE   B 1 18  ? 39.404 -32.627 -10.505 1.00 21.00 ?  18  ILE   B HD13 1 
ATOM   4293 N  N    . LYS   B 1 19  ? 42.797 -29.979 -13.225 1.00 16.04 ?  19  LYS   B N    1 
ATOM   4294 C  CA   . LYS   B 1 19  ? 44.000 -30.453 -13.894 1.00 16.74 ?  19  LYS   B CA   1 
ATOM   4295 C  C    . LYS   B 1 19  ? 44.909 -31.136 -12.882 1.00 16.69 ?  19  LYS   B C    1 
ATOM   4296 O  O    . LYS   B 1 19  ? 45.001 -30.715 -11.727 1.00 16.14 ?  19  LYS   B O    1 
ATOM   4297 C  CB   . LYS   B 1 19  ? 44.759 -29.292 -14.545 1.00 18.57 ?  19  LYS   B CB   1 
ATOM   4298 C  CG   . LYS   B 1 19  ? 45.941 -29.710 -15.400 1.00 20.98 ?  19  LYS   B CG   1 
ATOM   4299 C  CD   . LYS   B 1 19  ? 46.665 -28.488 -15.947 1.00 23.01 ?  19  LYS   B CD   1 
ATOM   4300 C  CE   . LYS   B 1 19  ? 47.820 -28.873 -16.849 1.00 25.14 ?  19  LYS   B CE   1 
ATOM   4301 N  NZ   . LYS   B 1 19  ? 48.590 -27.683 -17.301 1.00 26.73 ?  19  LYS   B NZ   1 
ATOM   4302 H  H    . LYS   B 1 19  ? 42.912 -29.734 -12.406 1.00 19.27 ?  19  LYS   B H    1 
ATOM   4303 H  HA   . LYS   B 1 19  ? 43.745 -31.094 -14.578 1.00 20.11 ?  19  LYS   B HA   1 
ATOM   4304 H  HB2  . LYS   B 1 19  ? 44.142 -28.816 -15.117 1.00 22.31 ?  19  LYS   B HB2  1 
ATOM   4305 H  HB3  . LYS   B 1 19  ? 45.079 -28.705 -13.842 1.00 22.31 ?  19  LYS   B HB3  1 
ATOM   4306 H  HG2  . LYS   B 1 19  ? 46.558 -30.226 -14.861 1.00 25.20 ?  19  LYS   B HG2  1 
ATOM   4307 H  HG3  . LYS   B 1 19  ? 45.617 -30.242 -16.147 1.00 25.20 ?  19  LYS   B HG3  1 
ATOM   4308 H  HD2  . LYS   B 1 19  ? 46.038 -27.953 -16.460 1.00 27.64 ?  19  LYS   B HD2  1 
ATOM   4309 H  HD3  . LYS   B 1 19  ? 47.013 -27.970 -15.203 1.00 27.64 ?  19  LYS   B HD3  1 
ATOM   4310 H  HE2  . LYS   B 1 19  ? 48.421 -29.460 -16.362 1.00 30.19 ?  19  LYS   B HE2  1 
ATOM   4311 H  HE3  . LYS   B 1 19  ? 47.472 -29.328 -17.633 1.00 30.19 ?  19  LYS   B HE3  1 
ATOM   4312 H  HZ1  . LYS   B 1 19  ? 49.233 -27.932 -17.865 1.00 32.10 ?  19  LYS   B HZ1  1 
ATOM   4313 H  HZ2  . LYS   B 1 19  ? 48.050 -27.109 -17.716 1.00 32.10 ?  19  LYS   B HZ2  1 
ATOM   4314 H  HZ3  . LYS   B 1 19  ? 48.962 -27.276 -16.603 1.00 32.10 ?  19  LYS   B HZ3  1 
ATOM   4315 N  N    . ASN   B 1 20  ? 45.587 -32.190 -13.325 1.00 17.98 ?  20  ASN   B N    1 
ATOM   4316 C  CA   . ASN   B 1 20  ? 46.613 -32.835 -12.510 1.00 19.19 ?  20  ASN   B CA   1 
ATOM   4317 C  C    . ASN   B 1 20  ? 47.895 -32.025 -12.680 1.00 19.70 ?  20  ASN   B C    1 
ATOM   4318 O  O    . ASN   B 1 20  ? 48.549 -32.093 -13.726 1.00 21.78 ?  20  ASN   B O    1 
ATOM   4319 C  CB   . ASN   B 1 20  ? 46.777 -34.286 -12.957 1.00 21.34 ?  20  ASN   B CB   1 
ATOM   4320 C  CG   . ASN   B 1 20  ? 47.937 -35.000 -12.273 1.00 22.92 ?  20  ASN   B CG   1 
ATOM   4321 O  OD1  . ASN   B 1 20  ? 48.597 -35.850 -12.881 1.00 25.20 ?  20  ASN   B OD1  1 
ATOM   4322 N  ND2  . ASN   B 1 20  ? 48.181 -34.679 -11.012 1.00 22.36 ?  20  ASN   B ND2  1 
ATOM   4323 H  H    . ASN   B 1 20  ? 45.462 -32.552 -14.094 1.00 21.60 ?  20  ASN   B H    1 
ATOM   4324 H  HA   . ASN   B 1 20  ? 46.334 -32.820 -11.577 1.00 23.05 ?  20  ASN   B HA   1 
ATOM   4325 H  HB2  . ASN   B 1 20  ? 45.954 -34.774 -12.756 1.00 25.63 ?  20  ASN   B HB2  1 
ATOM   4326 H  HB3  . ASN   B 1 20  ? 46.933 -34.302 -13.913 1.00 25.63 ?  20  ASN   B HB3  1 
ATOM   4327 H  HD21 . ASN   B 1 20  ? 48.822 -35.057 -10.591 1.00 26.85 ?  20  ASN   B HD21 1 
ATOM   4328 H  HD22 . ASN   B 1 20  ? 47.701 -34.078 -10.613 1.00 26.85 ?  20  ASN   B HD22 1 
ATOM   4329 N  N    . ALA   B 1 21  ? 48.255 -31.235 -11.664 1.00 19.30 ?  21  ALA   B N    1 
ATOM   4330 C  CA   . ALA   B 1 21  ? 49.392 -30.340 -11.815 1.00 20.15 ?  21  ALA   B CA   1 
ATOM   4331 C  C    . ALA   B 1 21  ? 49.855 -29.813 -10.462 1.00 18.70 ?  21  ALA   B C    1 
ATOM   4332 O  O    . ALA   B 1 21  ? 49.113 -29.820 -9.475  1.00 18.11 ?  21  ALA   B O    1 
ATOM   4333 C  CB   . ALA   B 1 21  ? 49.041 -29.187 -12.753 1.00 22.10 ?  21  ALA   B CB   1 
ATOM   4334 H  H    . ALA   B 1 21  ? 47.864 -31.212 -10.894 1.00 23.19 ?  21  ALA   B H    1 
ATOM   4335 H  HA   . ALA   B 1 21  ? 50.124 -30.842 -12.210 1.00 24.20 ?  21  ALA   B HA   1 
ATOM   4336 H  HB1  . ALA   B 1 21  ? 49.839 -28.666 -12.902 1.00 26.54 ?  21  ALA   B HB1  1 
ATOM   4337 H  HB2  . ALA   B 1 21  ? 48.722 -29.558 -13.592 1.00 26.54 ?  21  ALA   B HB2  1 
ATOM   4338 H  HB3  . ALA   B 1 21  ? 48.350 -28.651 -12.342 1.00 26.54 ?  21  ALA   B HB3  1 
ATOM   4339 N  N    . ASP   B 1 22  ? 51.114 -29.370 -10.450 1.00 17.46 ?  22  ASP   B N    1 
ATOM   4340 C  CA   . ASP   B 1 22  ? 51.739 -28.674 -9.329  1.00 16.57 ?  22  ASP   B CA   1 
ATOM   4341 C  C    . ASP   B 1 22  ? 51.328 -27.204 -9.398  1.00 14.99 ?  22  ASP   B C    1 
ATOM   4342 O  O    . ASP   B 1 22  ? 51.628 -26.524 -10.383 1.00 15.80 ?  22  ASP   B O    1 
ATOM   4343 C  CB   . ASP   B 1 22  ? 53.258 -28.841 -9.492  1.00 18.23 ?  22  ASP   B CB   1 
ATOM   4344 C  CG   . ASP   B 1 22  ? 54.084 -28.092 -8.453  1.00 19.69 ?  22  ASP   B CG   1 
ATOM   4345 O  OD1  . ASP   B 1 22  ? 53.714 -26.981 -8.045  1.00 19.33 ?  22  ASP   B OD1  1 
ATOM   4346 O  OD2  . ASP   B 1 22  ? 55.157 -28.610 -8.071  1.00 22.18 -1 22  ASP   B OD2  1 
ATOM   4347 H  H    . ASP   B 1 22  ? 51.650 -29.468 -11.119 1.00 20.97 ?  22  ASP   B H    1 
ATOM   4348 H  HA   . ASP   B 1 22  ? 51.454 -29.060 -8.484  1.00 19.91 ?  22  ASP   B HA   1 
ATOM   4349 H  HB2  . ASP   B 1 22  ? 53.481 -29.778 -9.426  1.00 21.90 ?  22  ASP   B HB2  1 
ATOM   4350 H  HB3  . ASP   B 1 22  ? 53.515 -28.496 -10.361 1.00 21.90 ?  22  ASP   B HB3  1 
ATOM   4351 N  N    . ILE   B 1 23  ? 50.616 -26.723 -8.371  1.00 14.29 ?  23  ILE   B N    1 
ATOM   4352 C  CA   . ILE   B 1 23  ? 50.035 -25.375 -8.423  1.00 13.48 ?  23  ILE   B CA   1 
ATOM   4353 C  C    . ILE   B 1 23  ? 51.099 -24.290 -8.559  1.00 13.19 ?  23  ILE   B C    1 
ATOM   4354 O  O    . ILE   B 1 23  ? 50.838 -23.240 -9.157  1.00 12.71 ?  23  ILE   B O    1 
ATOM   4355 C  CB   . ILE   B 1 23  ? 49.112 -25.126 -7.215  1.00 13.89 ?  23  ILE   B CB   1 
ATOM   4356 C  CG1  . ILE   B 1 23  ? 48.296 -23.842 -7.407  1.00 14.56 ?  23  ILE   B CG1  1 
ATOM   4357 C  CG2  . ILE   B 1 23  ? 49.896 -25.111 -5.910  1.00 14.84 ?  23  ILE   B CG2  1 
ATOM   4358 C  CD1  . ILE   B 1 23  ? 47.172 -23.675 -6.392  1.00 15.31 ?  23  ILE   B CD1  1 
ATOM   4359 H  H    . ILE   B 1 23  ? 50.453 -27.151 -7.648  1.00 17.17 ?  23  ILE   B H    1 
ATOM   4360 H  HA   . ILE   B 1 23  ? 49.481 -25.319 -9.214  1.00 16.19 ?  23  ILE   B HA   1 
ATOM   4361 H  HB   . ILE   B 1 23  ? 48.485 -25.864 -7.172  1.00 16.69 ?  23  ILE   B HB   1 
ATOM   4362 H  HG12 . ILE   B 1 23  ? 48.896 -23.078 -7.320  1.00 17.49 ?  23  ILE   B HG12 1 
ATOM   4363 H  HG13 . ILE   B 1 23  ? 47.906 -23.848 -8.295  1.00 17.49 ?  23  ILE   B HG13 1 
ATOM   4364 H  HG21 . ILE   B 1 23  ? 49.274 -25.096 -5.168  1.00 17.83 ?  23  ILE   B HG21 1 
ATOM   4365 H  HG22 . ILE   B 1 23  ? 50.446 -25.910 -5.864  1.00 17.83 ?  23  ILE   B HG22 1 
ATOM   4366 H  HG23 . ILE   B 1 23  ? 50.460 -24.322 -5.888  1.00 17.83 ?  23  ILE   B HG23 1 
ATOM   4367 H  HD11 . ILE   B 1 23  ? 46.668 -22.877 -6.612  1.00 18.40 ?  23  ILE   B HD11 1 
ATOM   4368 H  HD12 . ILE   B 1 23  ? 46.597 -24.454 -6.434  1.00 18.40 ?  23  ILE   B HD12 1 
ATOM   4369 H  HD13 . ILE   B 1 23  ? 47.557 -23.592 -5.507  1.00 18.40 ?  23  ILE   B HD13 1 
ATOM   4370 N  N    . VAL   B 1 24  ? 52.295 -24.503 -8.004  1.00 13.27 ?  24  VAL   B N    1 
ATOM   4371 C  CA   . VAL   B 1 24  ? 53.370 -23.521 -8.159  1.00 14.54 ?  24  VAL   B CA   1 
ATOM   4372 C  C    . VAL   B 1 24  ? 53.831 -23.468 -9.607  1.00 14.41 ?  24  VAL   B C    1 
ATOM   4373 O  O    . VAL   B 1 24  ? 53.968 -22.388 -10.197 1.00 14.82 ?  24  VAL   B O    1 
ATOM   4374 C  CB   . VAL   B 1 24  ? 54.540 -23.841 -7.207  1.00 15.05 ?  24  VAL   B CB   1 
ATOM   4375 C  CG1  . VAL   B 1 24  ? 55.762 -22.966 -7.525  1.00 15.79 ?  24  VAL   B CG1  1 
ATOM   4376 C  CG2  . VAL   B 1 24  ? 54.112 -23.659 -5.767  1.00 15.63 ?  24  VAL   B CG2  1 
ATOM   4377 H  H    . VAL   B 1 24  ? 52.508 -25.191 -7.539  1.00 15.94 ?  24  VAL   B H    1 
ATOM   4378 H  HA   . VAL   B 1 24  ? 53.034 -22.645 -7.923  1.00 17.47 ?  24  VAL   B HA   1 
ATOM   4379 H  HB   . VAL   B 1 24  ? 54.800 -24.769 -7.320  1.00 18.09 ?  24  VAL   B HB   1 
ATOM   4380 H  HG11 . VAL   B 1 24  ? 56.360 -22.973 -6.761  1.00 18.97 ?  24  VAL   B HG11 1 
ATOM   4381 H  HG12 . VAL   B 1 24  ? 56.214 -23.330 -8.301  1.00 18.97 ?  24  VAL   B HG12 1 
ATOM   4382 H  HG13 . VAL   B 1 24  ? 55.463 -22.063 -7.703  1.00 18.97 ?  24  VAL   B HG13 1 
ATOM   4383 H  HG21 . VAL   B 1 24  ? 54.830 -23.940 -5.180  1.00 18.78 ?  24  VAL   B HG21 1 
ATOM   4384 H  HG22 . VAL   B 1 24  ? 53.909 -22.721 -5.613  1.00 18.78 ?  24  VAL   B HG22 1 
ATOM   4385 H  HG23 . VAL   B 1 24  ? 53.320 -24.197 -5.600  1.00 18.78 ?  24  VAL   B HG23 1 
ATOM   4386 N  N    . GLU   B 1 25  ? 54.098 -24.638 -10.198 1.00 15.45 ?  25  GLU   B N    1 
ATOM   4387 C  CA   . GLU   B 1 25  ? 54.485 -24.673 -11.602 1.00 17.12 ?  25  GLU   B CA   1 
ATOM   4388 C  C    . GLU   B 1 25  ? 53.372 -24.136 -12.487 1.00 15.59 ?  25  GLU   B C    1 
ATOM   4389 O  O    . GLU   B 1 25  ? 53.635 -23.415 -13.458 1.00 16.82 ?  25  GLU   B O    1 
ATOM   4390 C  CB   . GLU   B 1 25  ? 54.890 -26.089 -12.005 1.00 21.14 ?  25  GLU   B CB   1 
ATOM   4391 C  CG   . GLU   B 1 25  ? 56.203 -26.529 -11.373 1.00 26.65 ?  25  GLU   B CG   1 
ATOM   4392 C  CD   . GLU   B 1 25  ? 57.309 -25.488 -11.478 1.00 31.51 ?  25  GLU   B CD   1 
ATOM   4393 O  OE1  . GLU   B 1 25  ? 57.687 -25.122 -12.612 1.00 33.18 ?  25  GLU   B OE1  1 
ATOM   4394 O  OE2  . GLU   B 1 25  ? 57.796 -25.022 -10.420 1.00 33.04 -1 25  GLU   B OE2  1 
ATOM   4395 H  H    . GLU   B 1 25  ? 54.065 -25.405 -9.812  1.00 18.56 ?  25  GLU   B H    1 
ATOM   4396 H  HA   . GLU   B 1 25  ? 55.239 -24.082 -11.731 1.00 20.57 ?  25  GLU   B HA   1 
ATOM   4397 H  HB2  . GLU   B 1 25  ? 54.199 -26.710 -11.719 1.00 25.39 ?  25  GLU   B HB2  1 
ATOM   4398 H  HB3  . GLU   B 1 25  ? 54.988 -26.129 -12.970 1.00 25.39 ?  25  GLU   B HB3  1 
ATOM   4399 H  HG2  . GLU   B 1 25  ? 56.062 -26.696 -10.435 1.00 32.00 ?  25  GLU   B HG2  1 
ATOM   4400 H  HG3  . GLU   B 1 25  ? 56.515 -27.329 -11.821 1.00 32.00 ?  25  GLU   B HG3  1 
ATOM   4401 N  N    A GLU   B 1 26  ? 52.120 -24.466 -12.162 0.56 15.08 ?  26  GLU   B N    1 
ATOM   4402 N  N    B GLU   B 1 26  ? 52.118 -24.464 -12.160 0.44 15.25 ?  26  GLU   B N    1 
ATOM   4403 C  CA   A GLU   B 1 26  ? 50.992 -23.936 -12.922 0.56 15.72 ?  26  GLU   B CA   1 
ATOM   4404 C  CA   B GLU   B 1 26  ? 50.989 -23.940 -12.923 0.44 15.86 ?  26  GLU   B CA   1 
ATOM   4405 C  C    A GLU   B 1 26  ? 50.947 -22.419 -12.844 0.56 14.41 ?  26  GLU   B C    1 
ATOM   4406 C  C    B GLU   B 1 26  ? 50.932 -22.421 -12.842 0.44 14.48 ?  26  GLU   B C    1 
ATOM   4407 O  O    A GLU   B 1 26  ? 50.757 -21.740 -13.859 0.56 15.48 ?  26  GLU   B O    1 
ATOM   4408 O  O    B GLU   B 1 26  ? 50.720 -21.743 -13.853 0.44 15.34 ?  26  GLU   B O    1 
ATOM   4409 C  CB   A GLU   B 1 26  ? 49.680 -24.518 -12.399 0.56 17.33 ?  26  GLU   B CB   1 
ATOM   4410 C  CB   B GLU   B 1 26  ? 49.677 -24.538 -12.411 0.44 17.58 ?  26  GLU   B CB   1 
ATOM   4411 C  CG   A GLU   B 1 26  ? 49.322 -25.864 -12.985 0.56 19.71 ?  26  GLU   B CG   1 
ATOM   4412 C  CG   B GLU   B 1 26  ? 49.196 -25.755 -13.176 0.44 20.03 ?  26  GLU   B CG   1 
ATOM   4413 C  CD   A GLU   B 1 26  ? 49.150 -25.836 -14.500 0.56 20.30 ?  26  GLU   B CD   1 
ATOM   4414 C  CD   B GLU   B 1 26  ? 48.842 -25.428 -14.622 0.44 20.78 ?  26  GLU   B CD   1 
ATOM   4415 O  OE1  A GLU   B 1 26  ? 48.332 -25.039 -15.010 0.56 19.84 ?  26  GLU   B OE1  1 
ATOM   4416 O  OE1  B GLU   B 1 26  ? 47.760 -24.848 -14.875 0.44 21.70 ?  26  GLU   B OE1  1 
ATOM   4417 O  OE2  A GLU   B 1 26  ? 49.840 -26.617 -15.179 0.56 21.05 -1 26  GLU   B OE2  1 
ATOM   4418 O  OE2  B GLU   B 1 26  ? 49.655 -25.745 -15.506 0.44 20.25 -1 26  GLU   B OE2  1 
ATOM   4419 H  H    A GLU   B 1 26  ? 51.898 -24.990 -11.513 0.56 18.12 ?  26  GLU   B H    1 
ATOM   4420 H  H    B GLU   B 1 26  ? 51.898 -24.985 -11.510 0.44 18.33 ?  26  GLU   B H    1 
ATOM   4421 H  HA   A GLU   B 1 26  ? 51.090 -24.186 -13.851 0.56 18.89 ?  26  GLU   B HA   1 
ATOM   4422 H  HA   B GLU   B 1 26  ? 51.096 -24.186 -13.853 0.44 19.06 ?  26  GLU   B HA   1 
ATOM   4423 H  HB2  A GLU   B 1 26  ? 49.749 -24.623 -11.434 0.56 20.82 ?  26  GLU   B HB2  1 
ATOM   4424 H  HB2  B GLU   B 1 26  ? 49.793 -24.796 -11.485 0.44 21.12 ?  26  GLU   B HB2  1 
ATOM   4425 H  HB3  A GLU   B 1 26  ? 48.960 -23.900 -12.605 0.56 20.82 ?  26  GLU   B HB3  1 
ATOM   4426 H  HB3  B GLU   B 1 26  ? 48.984 -23.860 -12.476 0.44 21.12 ?  26  GLU   B HB3  1 
ATOM   4427 H  HG2  A GLU   B 1 26  ? 50.037 -26.478 -12.785 0.56 23.67 ?  26  GLU   B HG2  1 
ATOM   4428 H  HG2  B GLU   B 1 26  ? 49.892 -26.435 -13.143 0.44 24.06 ?  26  GLU   B HG2  1 
ATOM   4429 H  HG3  A GLU   B 1 26  ? 48.492 -26.161 -12.584 0.56 23.67 ?  26  GLU   B HG3  1 
ATOM   4430 H  HG3  B GLU   B 1 26  ? 48.388 -26.090 -12.762 0.44 24.06 ?  26  GLU   B HG3  1 
ATOM   4431 N  N    . ALA   B 1 27  ? 51.097 -21.867 -11.639 1.00 13.48 ?  27  ALA   B N    1 
ATOM   4432 C  CA   . ALA   B 1 27  ? 51.059 -20.417 -11.492 1.00 13.85 ?  27  ALA   B CA   1 
ATOM   4433 C  C    . ALA   B 1 27  ? 52.128 -19.755 -12.354 1.00 14.91 ?  27  ALA   B C    1 
ATOM   4434 O  O    . ALA   B 1 27  ? 51.864 -18.754 -13.038 1.00 15.60 ?  27  ALA   B O    1 
ATOM   4435 C  CB   . ALA   B 1 27  ? 51.221 -20.032 -10.020 1.00 13.88 ?  27  ALA   B CB   1 
ATOM   4436 H  H    A ALA   B 1 27  ? 51.221 -22.303 -10.907 0.56 16.20 ?  27  ALA   B H    1 
ATOM   4437 H  H    B ALA   B 1 27  ? 51.228 -22.303 -10.908 0.44 16.20 ?  27  ALA   B H    1 
ATOM   4438 H  HA   . ALA   B 1 27  ? 50.202 -20.091 -11.788 1.00 16.64 ?  27  ALA   B HA   1 
ATOM   4439 H  HB1  . ALA   B 1 27  ? 51.187 -19.066 -9.937  1.00 16.68 ?  27  ALA   B HB1  1 
ATOM   4440 H  HB2  . ALA   B 1 27  ? 50.494 -20.430 -9.509  1.00 16.68 ?  27  ALA   B HB2  1 
ATOM   4441 H  HB3  . ALA   B 1 27  ? 52.071 -20.363 -9.691  1.00 16.68 ?  27  ALA   B HB3  1 
ATOM   4442 N  N    . LYS   B 1 28  ? 53.343 -20.308 -12.351 1.00 16.48 ?  28  LYS   B N    1 
ATOM   4443 C  CA   . LYS   B 1 28  ? 54.417 -19.687 -13.118 1.00 18.64 ?  28  LYS   B CA   1 
ATOM   4444 C  C    . LYS   B 1 28  ? 54.168 -19.776 -14.618 1.00 18.98 ?  28  LYS   B C    1 
ATOM   4445 O  O    . LYS   B 1 28  ? 54.589 -18.883 -15.365 1.00 19.97 ?  28  LYS   B O    1 
ATOM   4446 C  CB   . LYS   B 1 28  ? 55.775 -20.274 -12.717 1.00 21.59 ?  28  LYS   B CB   1 
ATOM   4447 C  CG   . LYS   B 1 28  ? 56.165 -19.926 -11.281 1.00 24.85 ?  28  LYS   B CG   1 
ATOM   4448 C  CD   . LYS   B 1 28  ? 57.584 -20.349 -10.927 1.00 28.55 ?  28  LYS   B CD   1 
ATOM   4449 C  CE   . LYS   B 1 28  ? 57.681 -21.837 -10.704 1.00 31.46 ?  28  LYS   B CE   1 
ATOM   4450 N  NZ   . LYS   B 1 28  ? 59.033 -22.226 -10.210 1.00 34.34 ?  28  LYS   B NZ   1 
ATOM   4451 H  H    . LYS   B 1 28  ? 53.567 -21.027 -11.926 1.00 19.80 ?  28  LYS   B H    1 
ATOM   4452 H  HA   . LYS   B 1 28  ? 54.444 -18.749 -12.897 1.00 22.39 ?  28  LYS   B HA   1 
ATOM   4453 H  HB2  . LYS   B 1 28  ? 55.748 -21.239 -12.791 1.00 25.93 ?  28  LYS   B HB2  1 
ATOM   4454 H  HB3  . LYS   B 1 28  ? 56.465 -19.917 -13.304 1.00 25.93 ?  28  LYS   B HB3  1 
ATOM   4455 H  HG2  . LYS   B 1 28  ? 56.097 -18.964 -11.163 1.00 29.84 ?  28  LYS   B HG2  1 
ATOM   4456 H  HG3  . LYS   B 1 28  ? 55.556 -20.376 -10.675 1.00 29.84 ?  28  LYS   B HG3  1 
ATOM   4457 H  HD2  . LYS   B 1 28  ? 58.177 -20.106 -11.656 1.00 34.29 ?  28  LYS   B HD2  1 
ATOM   4458 H  HD3  . LYS   B 1 28  ? 57.854 -19.896 -10.112 1.00 34.29 ?  28  LYS   B HD3  1 
ATOM   4459 H  HE2  . LYS   B 1 28  ? 57.025 -22.105 -10.041 1.00 37.78 ?  28  LYS   B HE2  1 
ATOM   4460 H  HE3  . LYS   B 1 28  ? 57.518 -22.298 -11.542 1.00 37.78 ?  28  LYS   B HE3  1 
ATOM   4461 H  HZ1  . LYS   B 1 28  ? 59.069 -23.105 -10.085 1.00 41.23 ?  28  LYS   B HZ1  1 
ATOM   4462 H  HZ2  . LYS   B 1 28  ? 59.652 -21.991 -10.805 1.00 41.23 ?  28  LYS   B HZ2  1 
ATOM   4463 H  HZ3  . LYS   B 1 28  ? 59.203 -21.816 -9.438  1.00 41.23 ?  28  LYS   B HZ3  1 
ATOM   4464 N  N    . LYS   B 1 29  ? 53.467 -20.814 -15.077 1.00 20.01 ?  29  LYS   B N    1 
ATOM   4465 C  CA   . LYS   B 1 29  ? 53.170 -20.960 -16.499 1.00 22.92 ?  29  LYS   B CA   1 
ATOM   4466 C  C    . LYS   B 1 29  ? 51.921 -20.193 -16.925 1.00 21.84 ?  29  LYS   B C    1 
ATOM   4467 O  O    . LYS   B 1 29  ? 51.919 -19.558 -17.986 1.00 23.43 ?  29  LYS   B O    1 
ATOM   4468 C  CB   . LYS   B 1 29  ? 53.012 -22.442 -16.854 1.00 27.52 ?  29  LYS   B CB   1 
ATOM   4469 C  CG   . LYS   B 1 29  ? 52.806 -22.707 -18.341 1.00 31.57 ?  29  LYS   B CG   1 
ATOM   4470 C  CD   . LYS   B 1 29  ? 52.989 -24.182 -18.685 1.00 34.79 ?  29  LYS   B CD   1 
ATOM   4471 C  CE   . LYS   B 1 29  ? 51.862 -25.040 -18.133 1.00 36.84 ?  29  LYS   B CE   1 
ATOM   4472 N  NZ   . LYS   B 1 29  ? 52.086 -26.490 -18.409 1.00 37.97 ?  29  LYS   B NZ   1 
ATOM   4473 H  H    . LYS   B 1 29  ? 53.148 -21.449 -14.582 1.00 24.04 ?  29  LYS   B H    1 
ATOM   4474 H  HA   . LYS   B 1 29  ? 53.916 -20.615 -17.007 1.00 27.53 ?  29  LYS   B HA   1 
ATOM   4475 H  HB2  . LYS   B 1 29  ? 53.815 -22.914 -16.580 1.00 33.04 ?  29  LYS   B HB2  1 
ATOM   4476 H  HB3  . LYS   B 1 29  ? 52.245 -22.797 -16.383 1.00 33.04 ?  29  LYS   B HB3  1 
ATOM   4477 H  HG2  . LYS   B 1 29  ? 51.905 -22.448 -18.590 1.00 37.91 ?  29  LYS   B HG2  1 
ATOM   4478 H  HG3  . LYS   B 1 29  ? 53.454 -22.195 -18.851 1.00 37.91 ?  29  LYS   B HG3  1 
ATOM   4479 H  HD2  . LYS   B 1 29  ? 53.002 -24.287 -19.650 1.00 41.77 ?  29  LYS   B HD2  1 
ATOM   4480 H  HD3  . LYS   B 1 29  ? 53.823 -24.499 -18.305 1.00 41.77 ?  29  LYS   B HD3  1 
ATOM   4481 H  HE2  . LYS   B 1 29  ? 51.808 -24.921 -17.172 1.00 44.23 ?  29  LYS   B HE2  1 
ATOM   4482 H  HE3  . LYS   B 1 29  ? 51.026 -24.778 -18.551 1.00 44.23 ?  29  LYS   B HE3  1 
ATOM   4483 H  HZ1  . LYS   B 1 29  ? 51.415 -26.971 -18.077 1.00 45.58 ?  29  LYS   B HZ1  1 
ATOM   4484 H  HZ2  . LYS   B 1 29  ? 52.134 -26.628 -19.287 1.00 45.58 ?  29  LYS   B HZ2  1 
ATOM   4485 H  HZ3  . LYS   B 1 29  ? 52.847 -26.757 -18.032 1.00 45.58 ?  29  LYS   B HZ3  1 
ATOM   4486 N  N    . VAL   B 1 30  ? 50.858 -20.245 -16.117 1.00 20.23 ?  30  VAL   B N    1 
ATOM   4487 C  CA   . VAL   B 1 30  ? 49.569 -19.657 -16.486 1.00 20.48 ?  30  VAL   B CA   1 
ATOM   4488 C  C    . VAL   B 1 30  ? 49.579 -18.144 -16.348 1.00 18.76 ?  30  VAL   B C    1 
ATOM   4489 O  O    . VAL   B 1 30  ? 48.842 -17.443 -17.058 1.00 19.88 ?  30  VAL   B O    1 
ATOM   4490 C  CB   . VAL   B 1 30  ? 48.463 -20.263 -15.601 1.00 22.04 ?  30  VAL   B CB   1 
ATOM   4491 C  CG1  . VAL   B 1 30  ? 47.182 -19.447 -15.684 1.00 22.60 ?  30  VAL   B CG1  1 
ATOM   4492 C  CG2  . VAL   B 1 30  ? 48.215 -21.715 -15.979 1.00 23.14 ?  30  VAL   B CG2  1 
ATOM   4493 H  H    . VAL   B 1 30  ? 50.853 -20.634 -15.342 1.00 24.30 ?  30  VAL   B H    1 
ATOM   4494 H  HA   . VAL   B 1 30  ? 49.371 -19.893 -17.407 1.00 24.60 ?  30  VAL   B HA   1 
ATOM   4495 H  HB   . VAL   B 1 30  ? 48.757 -20.258 -14.676 1.00 26.47 ?  30  VAL   B HB   1 
ATOM   4496 H  HG11 . VAL   B 1 30  ? 46.434 -20.025 -15.463 1.00 27.15 ?  30  VAL   B HG11 1 
ATOM   4497 H  HG12 . VAL   B 1 30  ? 47.228 -18.717 -15.052 1.00 27.15 ?  30  VAL   B HG12 1 
ATOM   4498 H  HG13 . VAL   B 1 30  ? 47.074 -19.116 -16.584 1.00 27.15 ?  30  VAL   B HG13 1 
ATOM   4499 H  HG21 . VAL   B 1 30  ? 47.525 -22.085 -15.400 1.00 27.79 ?  30  VAL   B HG21 1 
ATOM   4500 H  HG22 . VAL   B 1 30  ? 47.918 -21.755 -16.904 1.00 27.79 ?  30  VAL   B HG22 1 
ATOM   4501 H  HG23 . VAL   B 1 30  ? 49.036 -22.217 -15.874 1.00 27.79 ?  30  VAL   B HG23 1 
ATOM   4502 N  N    . LYS   B 1 31  ? 50.359 -17.633 -15.410 1.00 18.33 ?  31  LYS   B N    1 
ATOM   4503 C  CA   . LYS   B 1 31  ? 50.396 -16.221 -15.060 1.00 18.89 ?  31  LYS   B CA   1 
ATOM   4504 C  C    . LYS   B 1 31  ? 48.999 -15.738 -14.673 1.00 16.48 ?  31  LYS   B C    1 
ATOM   4505 O  O    . LYS   B 1 31  ? 48.464 -14.813 -15.298 1.00 17.15 ?  31  LYS   B O    1 
ATOM   4506 C  CB   . LYS   B 1 31  ? 51.029 -15.416 -16.200 1.00 22.07 ?  31  LYS   B CB   1 
ATOM   4507 C  CG   . LYS   B 1 31  ? 52.462 -15.863 -16.513 1.00 25.81 ?  31  LYS   B CG   1 
ATOM   4508 C  CD   . LYS   B 1 31  ? 53.068 -15.064 -17.648 1.00 29.31 ?  31  LYS   B CD   1 
ATOM   4509 C  CE   . LYS   B 1 31  ? 54.563 -15.269 -17.733 1.00 32.10 ?  31  LYS   B CE   1 
ATOM   4510 N  NZ   . LYS   B 1 31  ? 55.233 -14.854 -16.470 1.00 33.72 ?  31  LYS   B NZ   1 
ATOM   4511 H  H    . LYS   B 1 31  ? 50.910 -18.115 -14.951 1.00 22.02 ?  31  LYS   B H    1 
ATOM   4512 H  HA   . LYS   B 1 31  ? 50.965 -16.134 -14.292 1.00 22.69 ?  31  LYS   B HA   1 
ATOM   4513 H  HB2  . LYS   B 1 31  ? 50.503 -15.525 -17.006 1.00 26.50 ?  31  LYS   B HB2  1 
ATOM   4514 H  HB3  . LYS   B 1 31  ? 51.059 -14.486 -15.939 1.00 26.50 ?  31  LYS   B HB3  1 
ATOM   4515 H  HG2  . LYS   B 1 31  ? 53.009 -15.742 -15.721 1.00 30.99 ?  31  LYS   B HG2  1 
ATOM   4516 H  HG3  . LYS   B 1 31  ? 52.457 -16.801 -16.771 1.00 30.99 ?  31  LYS   B HG3  1 
ATOM   4517 H  HD2  . LYS   B 1 31  ? 52.671 -15.355 -18.482 1.00 35.20 ?  31  LYS   B HD2  1 
ATOM   4518 H  HD3  . LYS   B 1 31  ? 52.894 -14.126 -17.497 1.00 35.20 ?  31  LYS   B HD3  1 
ATOM   4519 H  HE2  . LYS   B 1 31  ? 54.755 -16.208 -17.887 1.00 38.54 ?  31  LYS   B HE2  1 
ATOM   4520 H  HE3  . LYS   B 1 31  ? 54.918 -14.730 -18.458 1.00 38.54 ?  31  LYS   B HE3  1 
ATOM   4521 H  HZ1  . LYS   B 1 31  ? 56.113 -14.818 -16.590 1.00 40.48 ?  31  LYS   B HZ1  1 
ATOM   4522 H  HZ2  . LYS   B 1 31  ? 54.941 -14.050 -16.222 1.00 40.48 ?  31  LYS   B HZ2  1 
ATOM   4523 H  HZ3  . LYS   B 1 31  ? 55.052 -15.438 -15.823 1.00 40.48 ?  31  LYS   B HZ3  1 
ATOM   4524 N  N    . PRO   B 1 32  ? 48.389 -16.325 -13.641 1.00 14.65 ?  32  PRO   B N    1 
ATOM   4525 C  CA   . PRO   B 1 32  ? 47.018 -15.955 -13.276 1.00 13.82 ?  32  PRO   B CA   1 
ATOM   4526 C  C    . PRO   B 1 32  ? 46.956 -14.608 -12.574 1.00 13.99 ?  32  PRO   B C    1 
ATOM   4527 O  O    . PRO   B 1 32  ? 47.893 -14.187 -11.889 1.00 15.48 ?  32  PRO   B O    1 
ATOM   4528 C  CB   . PRO   B 1 32  ? 46.619 -17.062 -12.297 1.00 14.19 ?  32  PRO   B CB   1 
ATOM   4529 C  CG   . PRO   B 1 32  ? 47.929 -17.416 -11.626 1.00 14.67 ?  32  PRO   B CG   1 
ATOM   4530 C  CD   . PRO   B 1 32  ? 48.974 -17.298 -12.698 1.00 14.99 ?  32  PRO   B CD   1 
ATOM   4531 H  HA   . PRO   B 1 32  ? 46.434 -15.981 -14.055 1.00 16.61 ?  32  PRO   B HA   1 
ATOM   4532 H  HB2  . PRO   B 1 32  ? 45.983 -16.716 -11.654 1.00 17.05 ?  32  PRO   B HB2  1 
ATOM   4533 H  HB3  . PRO   B 1 32  ? 46.257 -17.824 -12.774 1.00 17.05 ?  32  PRO   B HB3  1 
ATOM   4534 H  HG2  . PRO   B 1 32  ? 48.109 -16.795 -10.902 1.00 17.63 ?  32  PRO   B HG2  1 
ATOM   4535 H  HG3  . PRO   B 1 32  ? 47.891 -18.328 -11.288 1.00 17.63 ?  32  PRO   B HG3  1 
ATOM   4536 H  HD2  . PRO   B 1 32  ? 49.797 -16.948 -12.332 1.00 18.01 ?  32  PRO   B HD2  1 
ATOM   4537 H  HD3  . PRO   B 1 32  ? 49.108 -18.153 -13.133 1.00 18.01 ?  32  PRO   B HD3  1 
ATOM   4538 N  N    . THR   B 1 33  ? 45.805 -13.946 -12.729 1.00 13.54 ?  33  THR   B N    1 
ATOM   4539 C  CA   . THR   B 1 33  ? 45.529 -12.769 -11.915 1.00 13.93 ?  33  THR   B CA   1 
ATOM   4540 C  C    . THR   B 1 33  ? 45.489 -13.122 -10.432 1.00 13.37 ?  33  THR   B C    1 
ATOM   4541 O  O    . THR   B 1 33  ? 45.972 -12.350 -9.589  1.00 14.25 ?  33  THR   B O    1 
ATOM   4542 C  CB   . THR   B 1 33  ? 44.207 -12.137 -12.350 1.00 14.69 ?  33  THR   B CB   1 
ATOM   4543 O  OG1  . THR   B 1 33  ? 44.225 -11.894 -13.758 1.00 14.56 ?  33  THR   B OG1  1 
ATOM   4544 C  CG2  . THR   B 1 33  ? 43.976 -10.840 -11.613 1.00 16.07 ?  33  THR   B CG2  1 
ATOM   4545 H  H    . THR   B 1 33  ? 45.177 -14.167 -13.282 1.00 16.27 ?  33  THR   B H    1 
ATOM   4546 H  HA   . THR   B 1 33  ? 46.234 -12.125 -12.058 1.00 16.74 ?  33  THR   B HA   1 
ATOM   4547 H  HB   . THR   B 1 33  ? 43.477 -12.749 -12.148 1.00 17.65 ?  33  THR   B HB   1 
ATOM   4548 H  HG1  . THR   B 1 33  ? 43.509 -11.520 -13.999 1.00 17.49 ?  33  THR   B HG1  1 
ATOM   4549 H  HG21 . THR   B 1 33  ? 43.227 -10.368 -12.000 1.00 19.30 ?  33  THR   B HG21 1 
ATOM   4550 H  HG22 . THR   B 1 33  ? 43.790 -11.019 -10.677 1.00 19.30 ?  33  THR   B HG22 1 
ATOM   4551 H  HG23 . THR   B 1 33  ? 44.769 -10.282 -11.675 1.00 19.30 ?  33  THR   B HG23 1 
ATOM   4552 N  N    . VAL   B 1 34  ? 44.927 -14.286 -10.090 1.00 12.61 ?  34  VAL   B N    1 
ATOM   4553 C  CA   . VAL   B 1 34  ? 44.718 -14.677 -8.700  1.00 12.36 ?  34  VAL   B CA   1 
ATOM   4554 C  C    . VAL   B 1 34  ? 45.134 -16.130 -8.527  1.00 11.51 ?  34  VAL   B C    1 
ATOM   4555 O  O    . VAL   B 1 34  ? 44.605 -17.016 -9.211  1.00 11.96 ?  34  VAL   B O    1 
ATOM   4556 C  CB   . VAL   B 1 34  ? 43.249 -14.513 -8.262  1.00 13.14 ?  34  VAL   B CB   1 
ATOM   4557 C  CG1  . VAL   B 1 34  ? 43.076 -14.962 -6.815  1.00 13.67 ?  34  VAL   B CG1  1 
ATOM   4558 C  CG2  . VAL   B 1 34  ? 42.770 -13.080 -8.466  1.00 14.12 ?  34  VAL   B CG2  1 
ATOM   4559 H  H    . VAL   B 1 34  ? 44.663 -14.880 -10.656 1.00 15.15 ?  34  VAL   B H    1 
ATOM   4560 H  HA   . VAL   B 1 34  ? 45.273 -14.126 -8.123  1.00 14.86 ?  34  VAL   B HA   1 
ATOM   4561 H  HB   . VAL   B 1 34  ? 42.696 -15.083 -8.818  1.00 15.79 ?  34  VAL   B HB   1 
ATOM   4562 H  HG11 . VAL   B 1 34  ? 42.222 -14.632 -6.485  1.00 16.42 ?  34  VAL   B HG11 1 
ATOM   4563 H  HG12 . VAL   B 1 34  ? 43.089 -15.929 -6.780  1.00 16.42 ?  34  VAL   B HG12 1 
ATOM   4564 H  HG13 . VAL   B 1 34  ? 43.796 -14.595 -6.283  1.00 16.42 ?  34  VAL   B HG13 1 
ATOM   4565 H  HG21 . VAL   B 1 34  ? 41.850 -13.006 -8.159  1.00 16.97 ?  34  VAL   B HG21 1 
ATOM   4566 H  HG22 . VAL   B 1 34  ? 43.336 -12.478 -7.963  1.00 16.97 ?  34  VAL   B HG22 1 
ATOM   4567 H  HG23 . VAL   B 1 34  ? 42.814 -12.861 -9.414  1.00 16.97 ?  34  VAL   B HG23 1 
ATOM   4568 N  N    . VAL   B 1 35  ? 46.042 -16.382 -7.590  1.00 10.59 ?  35  VAL   B N    1 
ATOM   4569 C  CA   . VAL   B 1 35  ? 46.264 -17.724 -7.070  1.00 10.53 ?  35  VAL   B CA   1 
ATOM   4570 C  C    . VAL   B 1 35  ? 45.720 -17.773 -5.651  1.00 10.32 ?  35  VAL   B C    1 
ATOM   4571 O  O    . VAL   B 1 35  ? 45.946 -16.853 -4.856  1.00 10.54 ?  35  VAL   B O    1 
ATOM   4572 C  CB   . VAL   B 1 35  ? 47.744 -18.162 -7.149  1.00 11.41 ?  35  VAL   B CB   1 
ATOM   4573 C  CG1  . VAL   B 1 35  ? 48.650 -17.326 -6.240  1.00 12.21 ?  35  VAL   B CG1  1 
ATOM   4574 C  CG2  . VAL   B 1 35  ? 47.873 -19.656 -6.832  1.00 12.30 ?  35  VAL   B CG2  1 
ATOM   4575 H  H    . VAL   B 1 35  ? 46.545 -15.780 -7.226  1.00 12.73 ?  35  VAL   B H    1 
ATOM   4576 H  HA   . VAL   B 1 35  ? 45.748 -18.350 -7.596  1.00 12.66 ?  35  VAL   B HA   1 
ATOM   4577 H  HB   . VAL   B 1 35  ? 48.048 -18.035 -8.062  1.00 13.71 ?  35  VAL   B HB   1 
ATOM   4578 H  HG11 . VAL   B 1 35  ? 49.572 -17.568 -6.418  1.00 14.68 ?  35  VAL   B HG11 1 
ATOM   4579 H  HG12 . VAL   B 1 35  ? 48.505 -16.391 -6.431  1.00 14.68 ?  35  VAL   B HG12 1 
ATOM   4580 H  HG13 . VAL   B 1 35  ? 48.428 -17.521 -5.316  1.00 14.68 ?  35  VAL   B HG13 1 
ATOM   4581 H  HG21 . VAL   B 1 35  ? 48.795 -19.930 -6.938  1.00 14.78 ?  35  VAL   B HG21 1 
ATOM   4582 H  HG22 . VAL   B 1 35  ? 47.584 -19.817 -5.917  1.00 14.78 ?  35  VAL   B HG22 1 
ATOM   4583 H  HG23 . VAL   B 1 35  ? 47.308 -20.165 -7.443  1.00 14.78 ?  35  VAL   B HG23 1 
ATOM   4584 N  N    . VAL   B 1 36  ? 45.001 -18.854 -5.332  1.00 10.50 ?  36  VAL   B N    1 
ATOM   4585 C  CA   . VAL   B 1 36  ? 44.456 -19.051 -3.998  1.00 10.12 ?  36  VAL   B CA   1 
ATOM   4586 C  C    . VAL   B 1 36  ? 45.462 -19.814 -3.142  1.00 9.70  ?  36  VAL   B C    1 
ATOM   4587 O  O    . VAL   B 1 36  ? 45.997 -20.850 -3.561  1.00 10.60 ?  36  VAL   B O    1 
ATOM   4588 C  CB   . VAL   B 1 36  ? 43.115 -19.807 -4.068  1.00 10.39 ?  36  VAL   B CB   1 
ATOM   4589 C  CG1  . VAL   B 1 36  ? 42.613 -20.171 -2.676  1.00 11.17 ?  36  VAL   B CG1  1 
ATOM   4590 C  CG2  . VAL   B 1 36  ? 42.089 -18.982 -4.829  1.00 11.10 ?  36  VAL   B CG2  1 
ATOM   4591 H  H    . VAL   B 1 36  ? 44.828 -19.498 -5.877  1.00 12.62 ?  36  VAL   B H    1 
ATOM   4592 H  HA   . VAL   B 1 36  ? 44.293 -18.188 -3.586  1.00 12.17 ?  36  VAL   B HA   1 
ATOM   4593 H  HB   . VAL   B 1 36  ? 43.247 -20.631 -4.558  1.00 12.49 ?  36  VAL   B HB   1 
ATOM   4594 H  HG11 . VAL   B 1 36  ? 41.674 -20.400 -2.728  1.00 13.43 ?  36  VAL   B HG11 1 
ATOM   4595 H  HG12 . VAL   B 1 36  ? 43.121 -20.925 -2.343  1.00 13.43 ?  36  VAL   B HG12 1 
ATOM   4596 H  HG13 . VAL   B 1 36  ? 42.733 -19.404 -2.089  1.00 13.43 ?  36  VAL   B HG13 1 
ATOM   4597 H  HG21 . VAL   B 1 36  ? 41.243 -19.461 -4.846  1.00 13.35 ?  36  VAL   B HG21 1 
ATOM   4598 H  HG22 . VAL   B 1 36  ? 41.976 -18.126 -4.391  1.00 13.35 ?  36  VAL   B HG22 1 
ATOM   4599 H  HG23 . VAL   B 1 36  ? 42.403 -18.847 -5.741  1.00 13.35 ?  36  VAL   B HG23 1 
ATOM   4600 N  N    . ASN   B 1 37  ? 45.679 -19.327 -1.927  1.00 9.92  ?  37  ASN   B N    1 
ATOM   4601 C  CA   . ASN   B 1 37  ? 46.430 -20.047 -0.914  1.00 10.23 ?  37  ASN   B CA   1 
ATOM   4602 C  C    . ASN   B 1 37  ? 45.479 -20.714 0.072   1.00 10.72 ?  37  ASN   B C    1 
ATOM   4603 O  O    . ASN   B 1 37  ? 44.469 -20.133 0.480   1.00 10.95 ?  37  ASN   B O    1 
ATOM   4604 C  CB   . ASN   B 1 37  ? 47.360 -19.102 -0.157  1.00 10.18 ?  37  ASN   B CB   1 
ATOM   4605 C  CG   . ASN   B 1 37  ? 48.211 -19.813 0.858   1.00 10.80 ?  37  ASN   B CG   1 
ATOM   4606 O  OD1  . ASN   B 1 37  ? 48.542 -20.990 0.686   1.00 11.46 ?  37  ASN   B OD1  1 
ATOM   4607 N  ND2  . ASN   B 1 37  ? 48.568 -19.115 1.927   1.00 10.74 ?  37  ASN   B ND2  1 
ATOM   4608 H  H    . ASN   B 1 37  ? 45.390 -18.558 -1.656  1.00 11.93 ?  37  ASN   B H    1 
ATOM   4609 H  HA   . ASN   B 1 37  ? 46.963 -20.736 -1.328  1.00 12.30 ?  37  ASN   B HA   1 
ATOM   4610 H  HB2  . ASN   B 1 37  ? 47.955 -18.672 -0.794  1.00 12.24 ?  37  ASN   B HB2  1 
ATOM   4611 H  HB3  . ASN   B 1 37  ? 46.836 -18.436 0.310   1.00 12.24 ?  37  ASN   B HB3  1 
ATOM   4612 H  HD21 . ASN   B 1 37  ? 49.064 -19.475 2.531   1.00 12.90 ?  37  ASN   B HD21 1 
ATOM   4613 H  HD22 . ASN   B 1 37  ? 48.328 -18.298 2.008   1.00 12.90 ?  37  ASN   B HD22 1 
ATOM   4614 N  N    . ALA   B 1 38  ? 45.824 -21.946 0.449   1.00 10.73 ?  38  ALA   B N    1 
ATOM   4615 C  CA   . ALA   B 1 38  ? 45.174 -22.680 1.535   1.00 11.20 ?  38  ALA   B CA   1 
ATOM   4616 C  C    . ALA   B 1 38  ? 45.761 -22.189 2.858   1.00 11.06 ?  38  ALA   B C    1 
ATOM   4617 O  O    . ALA   B 1 38  ? 46.659 -22.801 3.449   1.00 11.90 ?  38  ALA   B O    1 
ATOM   4618 C  CB   . ALA   B 1 38  ? 45.389 -24.177 1.355   1.00 12.35 ?  38  ALA   B CB   1 
ATOM   4619 H  H    . ALA   B 1 38  ? 46.459 -22.390 0.082   1.00 12.90 ?  38  ALA   B H    1 
ATOM   4620 H  HA   . ALA   B 1 38  ? 44.220 -22.498 1.533   1.00 13.46 ?  38  ALA   B HA   1 
ATOM   4621 H  HB1  . ALA   B 1 38  ? 44.946 -24.649 2.087   1.00 14.84 ?  38  ALA   B HB1  1 
ATOM   4622 H  HB2  . ALA   B 1 38  ? 44.997 -24.451 0.511   1.00 14.84 ?  38  ALA   B HB2  1 
ATOM   4623 H  HB3  . ALA   B 1 38  ? 46.334 -24.367 1.367   1.00 14.84 ?  38  ALA   B HB3  1 
ATOM   4624 N  N    . ALA   B 1 39  ? 45.242 -21.050 3.317   1.00 10.78 ?  39  ALA   B N    1 
ATOM   4625 C  CA   . ALA   B 1 39  ? 45.801 -20.317 4.441   1.00 11.22 ?  39  ALA   B CA   1 
ATOM   4626 C  C    . ALA   B 1 39  ? 45.185 -20.762 5.765   1.00 11.41 ?  39  ALA   B C    1 
ATOM   4627 O  O    . ALA   B 1 39  ? 44.143 -21.421 5.813   1.00 12.18 ?  39  ALA   B O    1 
ATOM   4628 C  CB   . ALA   B 1 39  ? 45.558 -18.817 4.252   1.00 11.89 ?  39  ALA   B CB   1 
ATOM   4629 H  H    . ALA   B 1 39  ? 44.545 -20.674 2.976   1.00 12.96 ?  39  ALA   B H    1 
ATOM   4630 H  HA   . ALA   B 1 39  ? 46.754 -20.465 4.482   1.00 13.48 ?  39  ALA   B HA   1 
ATOM   4631 H  HB1  . ALA   B 1 39  ? 45.933 -18.335 5.007   1.00 14.29 ?  39  ALA   B HB1  1 
ATOM   4632 H  HB2  . ALA   B 1 39  ? 45.987 -18.525 3.430   1.00 14.29 ?  39  ALA   B HB2  1 
ATOM   4633 H  HB3  . ALA   B 1 39  ? 44.602 -18.650 4.199   1.00 14.29 ?  39  ALA   B HB3  1 
ATOM   4634 N  N    . ASN   B 1 40  ? 45.829 -20.350 6.853   1.00 12.01 ?  40  ASN   B N    1 
ATOM   4635 C  CA   . ASN   B 1 40  ? 45.264 -20.386 8.191   1.00 12.72 ?  40  ASN   B CA   1 
ATOM   4636 C  C    . ASN   B 1 40  ? 45.078 -18.954 8.702   1.00 12.48 ?  40  ASN   B C    1 
ATOM   4637 O  O    . ASN   B 1 40  ? 45.491 -17.981 8.062   1.00 12.19 ?  40  ASN   B O    1 
ATOM   4638 C  CB   . ASN   B 1 40  ? 46.113 -21.260 9.130   1.00 13.13 ?  40  ASN   B CB   1 
ATOM   4639 C  CG   . ASN   B 1 40  ? 47.567 -20.847 9.165   1.00 14.74 ?  40  ASN   B CG   1 
ATOM   4640 O  OD1  . ASN   B 1 40  ? 47.876 -19.664 9.270   1.00 17.08 ?  40  ASN   B OD1  1 
ATOM   4641 N  ND2  . ASN   B 1 40  ? 48.470 -21.814 9.088   1.00 14.84 ?  40  ASN   B ND2  1 
ATOM   4642 H  H    . ASN   B 1 40  ? 46.632 -20.037 6.832   1.00 14.43 ?  40  ASN   B H    1 
ATOM   4643 H  HA   . ASN   B 1 40  ? 44.384 -20.784 8.142   1.00 15.28 ?  40  ASN   B HA   1 
ATOM   4644 H  HB2  . ASN   B 1 40  ? 45.755 -21.192 10.031  1.00 15.77 ?  40  ASN   B HB2  1 
ATOM   4645 H  HB3  . ASN   B 1 40  ? 46.068 -22.181 8.827   1.00 15.77 ?  40  ASN   B HB3  1 
ATOM   4646 H  HD21 . ASN   B 1 40  ? 49.310 -21.624 9.108   1.00 17.83 ?  40  ASN   B HD21 1 
ATOM   4647 H  HD22 . ASN   B 1 40  ? 48.219 -22.634 9.016   1.00 17.83 ?  40  ASN   B HD22 1 
ATOM   4648 N  N    . VAL   B 1 41  ? 44.425 -18.819 9.860   1.00 13.04 ?  41  VAL   B N    1 
ATOM   4649 C  CA   . VAL   B 1 41  ? 43.969 -17.498 10.305  1.00 13.67 ?  41  VAL   B CA   1 
ATOM   4650 C  C    . VAL   B 1 41  ? 45.123 -16.546 10.591  1.00 13.29 ?  41  VAL   B C    1 
ATOM   4651 O  O    . VAL   B 1 41  ? 44.944 -15.325 10.512  1.00 13.64 ?  41  VAL   B O    1 
ATOM   4652 C  CB   . VAL   B 1 41  ? 43.012 -17.582 11.511  1.00 15.12 ?  41  VAL   B CB   1 
ATOM   4653 C  CG1  . VAL   B 1 41  ? 41.684 -18.233 11.117  1.00 15.30 ?  41  VAL   B CG1  1 
ATOM   4654 C  CG2  . VAL   B 1 41  ? 43.679 -18.292 12.679  1.00 16.12 ?  41  VAL   B CG2  1 
ATOM   4655 H  H    . VAL   B 1 41  ? 44.237 -19.463 10.390  1.00 15.67 ?  41  VAL   B H    1 
ATOM   4656 H  HA   . VAL   B 1 41  ? 43.462 -17.105 9.576   1.00 16.42 ?  41  VAL   B HA   1 
ATOM   4657 H  HB   . VAL   B 1 41  ? 42.808 -16.680 11.800  1.00 18.17 ?  41  VAL   B HB   1 
ATOM   4658 H  HG11 . VAL   B 1 41  ? 41.093 -18.241 11.887  1.00 18.39 ?  41  VAL   B HG11 1 
ATOM   4659 H  HG12 . VAL   B 1 41  ? 41.280 -17.722 10.397  1.00 18.39 ?  41  VAL   B HG12 1 
ATOM   4660 H  HG13 . VAL   B 1 41  ? 41.852 -19.142 10.821  1.00 18.39 ?  41  VAL   B HG13 1 
ATOM   4661 H  HG21 . VAL   B 1 41  ? 43.072 -18.300 13.432  1.00 19.36 ?  41  VAL   B HG21 1 
ATOM   4662 H  HG22 . VAL   B 1 41  ? 43.893 -19.203 12.417  1.00 19.36 ?  41  VAL   B HG22 1 
ATOM   4663 H  HG23 . VAL   B 1 41  ? 44.493 -17.818 12.913  1.00 19.36 ?  41  VAL   B HG23 1 
ATOM   4664 N  N    . TYR   B 1 42  ? 46.295 -17.065 10.963  1.00 13.63 ?  42  TYR   B N    1 
ATOM   4665 C  CA   . TYR   B 1 42  ? 47.451 -16.218 11.228  1.00 13.53 ?  42  TYR   B CA   1 
ATOM   4666 C  C    . TYR   B 1 42  ? 48.411 -16.150 10.047  1.00 12.98 ?  42  TYR   B C    1 
ATOM   4667 O  O    . TYR   B 1 42  ? 49.503 -15.583 10.179  1.00 14.69 ?  42  TYR   B O    1 
ATOM   4668 C  CB   . TYR   B 1 42  ? 48.150 -16.628 12.530  1.00 15.39 ?  42  TYR   B CB   1 
ATOM   4669 C  CG   . TYR   B 1 42  ? 47.550 -15.938 13.756  1.00 15.81 ?  42  TYR   B CG   1 
ATOM   4670 C  CD1  . TYR   B 1 42  ? 47.753 -14.577 13.974  1.00 14.89 ?  42  TYR   B CD1  1 
ATOM   4671 C  CD2  . TYR   B 1 42  ? 46.781 -16.634 14.676  1.00 17.98 ?  42  TYR   B CD2  1 
ATOM   4672 C  CE1  . TYR   B 1 42  ? 47.210 -13.932 15.063  1.00 15.93 ?  42  TYR   B CE1  1 
ATOM   4673 C  CE2  . TYR   B 1 42  ? 46.235 -15.994 15.784  1.00 18.32 ?  42  TYR   B CE2  1 
ATOM   4674 C  CZ   . TYR   B 1 42  ? 46.458 -14.638 15.974  1.00 18.21 ?  42  TYR   B CZ   1 
ATOM   4675 O  OH   . TYR   B 1 42  ? 45.932 -13.977 17.068  1.00 21.25 ?  42  TYR   B OH   1 
ATOM   4676 H  H    . TYR   B 1 42  ? 46.441 -17.910 11.060  1.00 16.37 ?  42  TYR   B H    1 
ATOM   4677 H  HA   . TYR   B 1 42  ? 47.126 -15.319 11.361  1.00 16.26 ?  42  TYR   B HA   1 
ATOM   4678 H  HB2  . TYR   B 1 42  ? 48.062 -17.587 12.648  1.00 18.49 ?  42  TYR   B HB2  1 
ATOM   4679 H  HB3  . TYR   B 1 42  ? 49.088 -16.386 12.472  1.00 18.49 ?  42  TYR   B HB3  1 
ATOM   4680 H  HD1  . TYR   B 1 42  ? 48.266 -14.095 13.357  1.00 17.89 ?  42  TYR   B HD1  1 
ATOM   4681 H  HD2  . TYR   B 1 42  ? 46.631 -17.547 14.547  1.00 21.60 ?  42  TYR   B HD2  1 
ATOM   4682 H  HE1  . TYR   B 1 42  ? 47.368 -13.026 15.188  1.00 19.14 ?  42  TYR   B HE1  1 
ATOM   4683 H  HE2  . TYR   B 1 42  ? 45.725 -16.475 16.392  1.00 22.00 ?  42  TYR   B HE2  1 
ATOM   4684 H  HH   . TYR   B 1 42  ? 46.150 -13.172 17.039  1.00 25.52 ?  42  TYR   B HH   1 
ATOM   4685 N  N    . LEU   B 1 43  ? 48.008 -16.666 8.888   1.00 11.88 ?  43  LEU   B N    1 
ATOM   4686 C  CA   . LEU   B 1 43  ? 48.824 -16.599 7.679   1.00 11.89 ?  43  LEU   B CA   1 
ATOM   4687 C  C    . LEU   B 1 43  ? 50.237 -17.107 7.944   1.00 11.91 ?  43  LEU   B C    1 
ATOM   4688 O  O    . LEU   B 1 43  ? 51.219 -16.518 7.490   1.00 12.89 ?  43  LEU   B O    1 
ATOM   4689 C  CB   . LEU   B 1 43  ? 48.845 -15.192 7.066   1.00 12.04 ?  43  LEU   B CB   1 
ATOM   4690 C  CG   . LEU   B 1 43  ? 47.489 -14.575 6.703   1.00 12.53 ?  43  LEU   B CG   1 
ATOM   4691 C  CD1  . LEU   B 1 43  ? 47.689 -13.174 6.125   1.00 13.57 ?  43  LEU   B CD1  1 
ATOM   4692 C  CD2  . LEU   B 1 43  ? 46.702 -15.464 5.746   1.00 12.54 ?  43  LEU   B CD2  1 
ATOM   4693 H  H    . LEU   B 1 43  ? 47.259 -17.075 8.773   1.00 14.28 ?  43  LEU   B H    1 
ATOM   4694 H  HA   . LEU   B 1 43  ? 48.425 -17.190 7.011   1.00 14.29 ?  43  LEU   B HA   1 
ATOM   4695 H  HB2  . LEU   B 1 43  ? 49.275 -14.597 7.694   1.00 14.47 ?  43  LEU   B HB2  1 
ATOM   4696 H  HB3  . LEU   B 1 43  ? 49.368 -15.229 6.246   1.00 14.47 ?  43  LEU   B HB3  1 
ATOM   4697 H  HG   . LEU   B 1 43  ? 46.967 -14.487 7.513   1.00 15.06 ?  43  LEU   B HG   1 
ATOM   4698 H  HD11 . LEU   B 1 43  ? 46.819 -12.800 5.907   1.00 16.30 ?  43  LEU   B HD11 1 
ATOM   4699 H  HD12 . LEU   B 1 43  ? 48.127 -12.620 6.790   1.00 16.30 ?  43  LEU   B HD12 1 
ATOM   4700 H  HD13 . LEU   B 1 43  ? 48.234 -13.234 5.329   1.00 16.30 ?  43  LEU   B HD13 1 
ATOM   4701 H  HD21 . LEU   B 1 43  ? 45.898 -14.996 5.470   1.00 15.07 ?  43  LEU   B HD21 1 
ATOM   4702 H  HD22 . LEU   B 1 43  ? 47.251 -15.663 4.972   1.00 15.07 ?  43  LEU   B HD22 1 
ATOM   4703 H  HD23 . LEU   B 1 43  ? 46.464 -16.287 6.202   1.00 15.07 ?  43  LEU   B HD23 1 
ATOM   4704 N  N    . LYS   B 1 44  ? 50.334 -18.228 8.664   1.00 12.23 ?  44  LYS   B N    1 
ATOM   4705 C  CA   . LYS   B 1 44  ? 51.603 -18.907 8.915   1.00 12.92 ?  44  LYS   B CA   1 
ATOM   4706 C  C    . LYS   B 1 44  ? 51.722 -20.027 7.889   1.00 12.58 ?  44  LYS   B C    1 
ATOM   4707 O  O    . LYS   B 1 44  ? 51.030 -21.044 7.978   1.00 13.72 ?  44  LYS   B O    1 
ATOM   4708 C  CB   . LYS   B 1 44  ? 51.650 -19.416 10.351  1.00 14.82 ?  44  LYS   B CB   1 
ATOM   4709 C  CG   . LYS   B 1 44  ? 51.865 -18.309 11.373  1.00 17.92 ?  44  LYS   B CG   1 
ATOM   4710 C  CD   . LYS   B 1 44  ? 53.043 -17.430 10.947  1.00 21.10 ?  44  LYS   B CD   1 
ATOM   4711 C  CE   . LYS   B 1 44  ? 53.603 -16.589 12.064  1.00 23.86 ?  44  LYS   B CE   1 
ATOM   4712 N  NZ   . LYS   B 1 44  ? 54.747 -15.749 11.631  1.00 25.09 ?  44  LYS   B NZ   1 
ATOM   4713 H  H    . LYS   B 1 44  ? 49.661 -18.609 9.034   1.00 14.70 ?  44  LYS   B H    1 
ATOM   4714 H  HA   . LYS   B 1 44  ? 52.332 -18.292 8.749   1.00 15.52 ?  44  LYS   B HA   1 
ATOM   4715 H  HB2  . LYS   B 1 44  ? 50.798 -19.851 10.555  1.00 17.80 ?  44  LYS   B HB2  1 
ATOM   4716 H  HB3  . LYS   B 1 44  ? 52.369 -20.056 10.434  1.00 17.80 ?  44  LYS   B HB3  1 
ATOM   4717 H  HG2  . LYS   B 1 44  ? 51.069 -17.764 11.435  1.00 21.53 ?  44  LYS   B HG2  1 
ATOM   4718 H  HG3  . LYS   B 1 44  ? 52.075 -18.709 12.236  1.00 21.53 ?  44  LYS   B HG3  1 
ATOM   4719 H  HD2  . LYS   B 1 44  ? 53.748 -18.005 10.595  1.00 25.34 ?  44  LYS   B HD2  1 
ATOM   4720 H  HD3  . LYS   B 1 44  ? 52.736 -16.828 10.247  1.00 25.34 ?  44  LYS   B HD3  1 
ATOM   4721 H  HE2  . LYS   B 1 44  ? 52.907 -15.995 12.362  1.00 28.65 ?  44  LYS   B HE2  1 
ATOM   4722 H  HE3  . LYS   B 1 44  ? 53.897 -17.172 12.782  1.00 28.65 ?  44  LYS   B HE3  1 
ATOM   4723 H  HZ1  . LYS   B 1 44  ? 55.038 -15.259 12.316  1.00 30.13 ?  44  LYS   B HZ1  1 
ATOM   4724 H  HZ2  . LYS   B 1 44  ? 55.413 -16.258 11.335  1.00 30.13 ?  44  LYS   B HZ2  1 
ATOM   4725 H  HZ3  . LYS   B 1 44  ? 54.491 -15.200 10.976  1.00 30.13 ?  44  LYS   B HZ3  1 
ATOM   4726 N  N    . HIS   B 1 45  ? 52.570 -19.809 6.887   1.00 12.32 ?  45  HIS   B N    1 
ATOM   4727 C  CA   . HIS   B 1 45  ? 52.590 -20.641 5.684   1.00 12.39 ?  45  HIS   B CA   1 
ATOM   4728 C  C    . HIS   B 1 45  ? 53.610 -21.766 5.837   1.00 14.62 ?  45  HIS   B C    1 
ATOM   4729 O  O    . HIS   B 1 45  ? 54.673 -21.777 5.223   1.00 17.13 ?  45  HIS   B O    1 
ATOM   4730 C  CB   . HIS   B 1 45  ? 52.900 -19.791 4.466   1.00 12.14 ?  45  HIS   B CB   1 
ATOM   4731 C  CG   . HIS   B 1 45  ? 52.029 -18.587 4.356   1.00 12.01 ?  45  HIS   B CG   1 
ATOM   4732 N  ND1  . HIS   B 1 45  ? 50.652 -18.669 4.310   1.00 12.22 ?  45  HIS   B ND1  1 
ATOM   4733 C  CD2  . HIS   B 1 45  ? 52.342 -17.273 4.281   1.00 13.24 ?  45  HIS   B CD2  1 
ATOM   4734 C  CE1  . HIS   B 1 45  ? 50.163 -17.447 4.205   1.00 12.15 ?  45  HIS   B CE1  1 
ATOM   4735 N  NE2  . HIS   B 1 45  ? 51.163 -16.584 4.180   1.00 13.00 ?  45  HIS   B NE2  1 
ATOM   4736 H  H    . HIS   B 1 45  ? 53.140 -19.167 6.871   1.00 14.80 ?  45  HIS   B H    1 
ATOM   4737 H  HA   . HIS   B 1 45  ? 51.708 -21.038 5.554   1.00 14.89 ?  45  HIS   B HA   1 
ATOM   4738 H  HB2  . HIS   B 1 45  ? 53.820 -19.495 4.512   1.00 14.59 ?  45  HIS   B HB2  1 
ATOM   4739 H  HB3  . HIS   B 1 45  ? 52.771 -20.332 3.662   1.00 14.59 ?  45  HIS   B HB3  1 
ATOM   4740 H  HD2  . HIS   B 1 45  ? 53.198 -16.906 4.289   1.00 15.91 ?  45  HIS   B HD2  1 
ATOM   4741 H  HE1  . HIS   B 1 45  ? 49.260 -17.233 4.145   1.00 14.61 ?  45  HIS   B HE1  1 
ATOM   4742 H  HE2  . HIS   B 1 45  ? 51.084 -15.729 4.126   1.00 15.62 ?  45  HIS   B HE2  1 
ATOM   4743 N  N    A GLY   B 1 46  ? 53.239 -22.744 6.657   0.56 15.52 ?  46  GLY   B N    1 
ATOM   4744 N  N    B GLY   B 1 46  ? 53.250 -22.730 6.674   0.44 15.56 ?  46  GLY   B N    1 
ATOM   4745 C  CA   A GLY   B 1 46  ? 54.170 -23.786 7.048   0.56 17.38 ?  46  GLY   B CA   1 
ATOM   4746 C  CA   B GLY   B 1 46  ? 54.178 -23.785 7.021   0.44 17.04 ?  46  GLY   B CA   1 
ATOM   4747 C  C    A GLY   B 1 46  ? 54.210 -25.025 6.174   0.56 18.93 ?  46  GLY   B C    1 
ATOM   4748 C  C    B GLY   B 1 46  ? 54.196 -24.952 6.055   0.44 18.28 ?  46  GLY   B C    1 
ATOM   4749 O  O    A GLY   B 1 46  ? 55.289 -25.482 5.785   0.56 21.35 ?  46  GLY   B O    1 
ATOM   4750 O  O    B GLY   B 1 46  ? 55.231 -25.262 5.455   0.44 19.50 ?  46  GLY   B O    1 
ATOM   4751 H  H    A GLY   B 1 46  ? 52.455 -22.810 7.013   0.56 18.65 ?  46  GLY   B H    1 
ATOM   4752 H  H    B GLY   B 1 46  ? 52.478 -22.784 7.059   0.44 18.69 ?  46  GLY   B H    1 
ATOM   4753 H  HA2  A GLY   B 1 46  ? 55.062 -23.406 7.072   0.56 20.87 ?  46  GLY   B HA2  1 
ATOM   4754 H  HA2  B GLY   B 1 46  ? 55.072 -23.411 7.063   0.44 20.47 ?  46  GLY   B HA2  1 
ATOM   4755 H  HA3  A GLY   B 1 46  ? 53.946 -24.076 7.945   0.56 20.87 ?  46  GLY   B HA3  1 
ATOM   4756 H  HA3  B GLY   B 1 46  ? 53.952 -24.120 7.903   0.44 20.47 ?  46  GLY   B HA3  1 
ATOM   4757 N  N    . GLY   B 1 47  ? 53.048 -25.601 5.876   1.00 18.87 ?  47  GLY   B N    1 
ATOM   4758 C  CA   . GLY   B 1 47  ? 52.981 -26.871 5.184   1.00 16.99 ?  47  GLY   B CA   1 
ATOM   4759 C  C    . GLY   B 1 47  ? 52.063 -26.846 3.978   1.00 14.60 ?  47  GLY   B C    1 
ATOM   4760 O  O    . GLY   B 1 47  ? 51.412 -25.845 3.687   1.00 14.31 ?  47  GLY   B O    1 
ATOM   4761 H  H    A GLY   B 1 47  ? 52.277 -25.277 6.086   0.56 22.67 ?  47  GLY   B H    1 
ATOM   4762 H  H    B GLY   B 1 47  ? 52.283 -25.315 6.154   0.44 22.67 ?  47  GLY   B H    1 
ATOM   4763 H  HA2  . GLY   B 1 47  ? 53.864 -27.127 4.880   1.00 20.41 ?  47  GLY   B HA2  1 
ATOM   4764 H  HA3  . GLY   B 1 47  ? 52.660 -27.550 5.796   1.00 20.41 ?  47  GLY   B HA3  1 
ATOM   4765 N  N    . GLY   B 1 48  ? 52.012 -27.985 3.289   1.00 13.85 ?  48  GLY   B N    1 
ATOM   4766 C  CA   . GLY   B 1 48  ? 51.091 -28.130 2.178   1.00 13.59 ?  48  GLY   B CA   1 
ATOM   4767 C  C    . GLY   B 1 48  ? 51.233 -27.019 1.161   1.00 12.73 ?  48  GLY   B C    1 
ATOM   4768 O  O    . GLY   B 1 48  ? 52.338 -26.561 0.850   1.00 13.39 ?  48  GLY   B O    1 
ATOM   4769 H  H    . GLY   B 1 48  ? 52.496 -28.671 3.446   1.00 16.64 ?  48  GLY   B H    1 
ATOM   4770 H  HA2  . GLY   B 1 48  ? 51.257 -28.981 1.731   1.00 16.33 ?  48  GLY   B HA2  1 
ATOM   4771 H  HA3  . GLY   B 1 48  ? 50.179 -28.131 2.502   1.00 16.33 ?  48  GLY   B HA3  1 
ATOM   4772 N  N    . VAL   B 1 49  ? 50.092 -26.591 0.621   1.00 12.64 ?  49  VAL   B N    1 
ATOM   4773 C  CA   . VAL   B 1 49  ? 50.085 -25.570 -0.422  1.00 12.16 ?  49  VAL   B CA   1 
ATOM   4774 C  C    . VAL   B 1 49  ? 50.746 -24.287 0.070   1.00 11.37 ?  49  VAL   B C    1 
ATOM   4775 O  O    . VAL   B 1 49  ? 51.538 -23.669 -0.646  1.00 12.23 ?  49  VAL   B O    1 
ATOM   4776 C  CB   . VAL   B 1 49  ? 48.642 -25.318 -0.905  1.00 13.74 ?  49  VAL   B CB   1 
ATOM   4777 C  CG1  . VAL   B 1 49  ? 48.567 -24.066 -1.777  1.00 14.09 ?  49  VAL   B CG1  1 
ATOM   4778 C  CG2  . VAL   B 1 49  ? 48.112 -26.532 -1.661  1.00 15.51 ?  49  VAL   B CG2  1 
ATOM   4779 H  H    . VAL   B 1 49  ? 49.309 -26.870 0.843   1.00 15.19 ?  49  VAL   B H    1 
ATOM   4780 H  HA   . VAL   B 1 49  ? 50.591 -25.894 -1.184  1.00 14.61 ?  49  VAL   B HA   1 
ATOM   4781 H  HB   . VAL   B 1 49  ? 48.070 -25.178 -0.135  1.00 16.51 ?  49  VAL   B HB   1 
ATOM   4782 H  HG11 . VAL   B 1 49  ? 47.733 -24.078 -2.277  1.00 16.93 ?  49  VAL   B HG11 1 
ATOM   4783 H  HG12 . VAL   B 1 49  ? 48.593 -23.279 -1.209  1.00 16.93 ?  49  VAL   B HG12 1 
ATOM   4784 H  HG13 . VAL   B 1 49  ? 49.316 -24.060 -2.391  1.00 16.93 ?  49  VAL   B HG13 1 
ATOM   4785 H  HG21 . VAL   B 1 49  ? 47.204 -26.353 -1.954  1.00 18.64 ?  49  VAL   B HG21 1 
ATOM   4786 H  HG22 . VAL   B 1 49  ? 48.680 -26.697 -2.431  1.00 18.64 ?  49  VAL   B HG22 1 
ATOM   4787 H  HG23 . VAL   B 1 49  ? 48.124 -27.300 -1.070  1.00 18.64 ?  49  VAL   B HG23 1 
ATOM   4788 N  N    . ALA   B 1 50  ? 50.399 -23.846 1.277   1.00 11.36 ?  50  ALA   B N    1 
ATOM   4789 C  CA   . ALA   B 1 50  ? 50.922 -22.572 1.760   1.00 11.53 ?  50  ALA   B CA   1 
ATOM   4790 C  C    . ALA   B 1 50  ? 52.443 -22.604 1.859   1.00 11.59 ?  50  ALA   B C    1 
ATOM   4791 O  O    . ALA   B 1 50  ? 53.122 -21.636 1.486   1.00 11.70 ?  50  ALA   B O    1 
ATOM   4792 C  CB   . ALA   B 1 50  ? 50.297 -22.220 3.107   1.00 11.84 ?  50  ALA   B CB   1 
ATOM   4793 H  H    . ALA   B 1 50  ? 49.866 -24.249 1.817   1.00 13.66 ?  50  ALA   B H    1 
ATOM   4794 H  HA   . ALA   B 1 50  ? 50.688 -21.875 1.134   1.00 13.85 ?  50  ALA   B HA   1 
ATOM   4795 H  HB1  . ALA   B 1 50  ? 50.659 -21.373 3.413   1.00 14.23 ?  50  ALA   B HB1  1 
ATOM   4796 H  HB2  . ALA   B 1 50  ? 49.335 -22.146 2.999   1.00 14.23 ?  50  ALA   B HB2  1 
ATOM   4797 H  HB3  . ALA   B 1 50  ? 50.505 -22.918 3.748   1.00 14.23 ?  50  ALA   B HB3  1 
ATOM   4798 N  N    . GLY   B 1 51  ? 52.995 -23.699 2.377   1.00 12.22 ?  51  GLY   B N    1 
ATOM   4799 C  CA   . GLY   B 1 51  ? 54.439 -23.801 2.451   1.00 12.85 ?  51  GLY   B CA   1 
ATOM   4800 C  C    . GLY   B 1 51  ? 55.091 -23.758 1.084   1.00 12.79 ?  51  GLY   B C    1 
ATOM   4801 O  O    . GLY   B 1 51  ? 56.138 -23.129 0.906   1.00 13.05 ?  51  GLY   B O    1 
ATOM   4802 H  H    . GLY   B 1 51  ? 52.567 -24.383 2.677   1.00 14.68 ?  51  GLY   B H    1 
ATOM   4803 H  HA2  . GLY   B 1 51  ? 54.789 -23.067 2.976   1.00 15.44 ?  51  GLY   B HA2  1 
ATOM   4804 H  HA3  . GLY   B 1 51  ? 54.687 -24.635 2.875   1.00 15.44 ?  51  GLY   B HA3  1 
ATOM   4805 N  N    . ALA   B 1 52  ? 54.485 -24.423 0.100   1.00 12.21 ?  52  ALA   B N    1 
ATOM   4806 C  CA   . ALA   B 1 52  ? 55.042 -24.434 -1.247  1.00 12.61 ?  52  ALA   B CA   1 
ATOM   4807 C  C    . ALA   B 1 52  ? 54.963 -23.056 -1.895  1.00 12.16 ?  52  ALA   B C    1 
ATOM   4808 O  O    . ALA   B 1 52  ? 55.936 -22.601 -2.517  1.00 12.89 ?  52  ALA   B O    1 
ATOM   4809 C  CB   . ALA   B 1 52  ? 54.315 -25.464 -2.104  1.00 13.38 ?  52  ALA   B CB   1 
ATOM   4810 H  H    . ALA   B 1 52  ? 53.752 -24.865 0.181   1.00 14.67 ?  52  ALA   B H    1 
ATOM   4811 H  HA   . ALA   B 1 52  ? 55.976 -24.685 -1.201  1.00 15.15 ?  52  ALA   B HA   1 
ATOM   4812 H  HB1  . ALA   B 1 52  ? 54.701 -25.460 -2.997  1.00 16.07 ?  52  ALA   B HB1  1 
ATOM   4813 H  HB2  . ALA   B 1 52  ? 54.427 -26.339 -1.703  1.00 16.07 ?  52  ALA   B HB2  1 
ATOM   4814 H  HB3  . ALA   B 1 52  ? 53.377 -25.234 -2.149  1.00 16.07 ?  52  ALA   B HB3  1 
ATOM   4815 N  N    . LEU   B 1 53  ? 53.818 -22.375 -1.773  1.00 11.75 ?  53  LEU   B N    1 
ATOM   4816 C  CA   . LEU   B 1 53  ? 53.713 -21.031 -2.339  1.00 11.76 ?  53  LEU   B CA   1 
ATOM   4817 C  C    . LEU   B 1 53  ? 54.723 -20.090 -1.689  1.00 11.69 ?  53  LEU   B C    1 
ATOM   4818 O  O    . LEU   B 1 53  ? 55.431 -19.344 -2.375  1.00 12.16 ?  53  LEU   B O    1 
ATOM   4819 C  CB   . LEU   B 1 53  ? 52.290 -20.483 -2.170  1.00 12.17 ?  53  LEU   B CB   1 
ATOM   4820 C  CG   . LEU   B 1 53  ? 51.150 -21.216 -2.888  1.00 12.33 ?  53  LEU   B CG   1 
ATOM   4821 C  CD1  . LEU   B 1 53  ? 49.815 -20.585 -2.547  1.00 14.21 ?  53  LEU   B CD1  1 
ATOM   4822 C  CD2  . LEU   B 1 53  ? 51.360 -21.236 -4.395  1.00 14.33 ?  53  LEU   B CD2  1 
ATOM   4823 H  H    . LEU   B 1 53  ? 53.113 -22.654 -1.373  1.00 14.13 ?  53  LEU   B H    1 
ATOM   4824 H  HA   . LEU   B 1 53  ? 53.913 -21.074 -3.292  1.00 14.13 ?  53  LEU   B HA   1 
ATOM   4825 H  HB2  . LEU   B 1 53  ? 52.083 -20.492 -1.226  1.00 14.62 ?  53  LEU   B HB2  1 
ATOM   4826 H  HB3  . LEU   B 1 53  ? 52.285 -19.569 -2.491  1.00 14.62 ?  53  LEU   B HB3  1 
ATOM   4827 H  HG   . LEU   B 1 53  ? 51.125 -22.134 -2.581  1.00 14.82 ?  53  LEU   B HG   1 
ATOM   4828 H  HD11 . LEU   B 1 53  ? 49.107 -21.066 -3.010  1.00 17.07 ?  53  LEU   B HD11 1 
ATOM   4829 H  HD12 . LEU   B 1 53  ? 49.672 -20.640 -1.587  1.00 17.07 ?  53  LEU   B HD12 1 
ATOM   4830 H  HD13 . LEU   B 1 53  ? 49.817 -19.657 -2.827  1.00 17.07 ?  53  LEU   B HD13 1 
ATOM   4831 H  HD21 . LEU   B 1 53  ? 50.648 -21.750 -4.808  1.00 17.22 ?  53  LEU   B HD21 1 
ATOM   4832 H  HD22 . LEU   B 1 53  ? 51.343 -20.326 -4.731  1.00 17.22 ?  53  LEU   B HD22 1 
ATOM   4833 H  HD23 . LEU   B 1 53  ? 52.217 -21.647 -4.593  1.00 17.22 ?  53  LEU   B HD23 1 
ATOM   4834 N  N    . ASN   B 1 54  ? 54.815 -20.118 -0.364  1.00 11.31 ?  54  ASN   B N    1 
ATOM   4835 C  CA   . ASN   B 1 54  ? 55.733 -19.207 0.307   1.00 12.04 ?  54  ASN   B CA   1 
ATOM   4836 C  C    . ASN   B 1 54  ? 57.179 -19.492 -0.083  1.00 12.75 ?  54  ASN   B C    1 
ATOM   4837 O  O    . ASN   B 1 54  ? 57.959 -18.558 -0.325  1.00 12.88 ?  54  ASN   B O    1 
ATOM   4838 C  CB   . ASN   B 1 54  ? 55.574 -19.279 1.814   1.00 13.24 ?  54  ASN   B CB   1 
ATOM   4839 C  CG   . ASN   B 1 54  ? 56.551 -18.363 2.515   1.00 13.22 ?  54  ASN   B CG   1 
ATOM   4840 O  OD1  . ASN   B 1 54  ? 56.566 -17.152 2.266   1.00 13.17 ?  54  ASN   B OD1  1 
ATOM   4841 N  ND2  . ASN   B 1 54  ? 57.397 -18.929 3.371   1.00 14.68 ?  54  ASN   B ND2  1 
ATOM   4842 H  H    . ASN   B 1 54  ? 54.373 -20.643 0.150   1.00 13.60 ?  54  ASN   B H    1 
ATOM   4843 H  HA   . ASN   B 1 54  ? 55.526 -18.304 0.025   1.00 14.47 ?  54  ASN   B HA   1 
ATOM   4844 H  HB2  . ASN   B 1 54  ? 54.677 -19.001 2.054   1.00 15.91 ?  54  ASN   B HB2  1 
ATOM   4845 H  HB3  . ASN   B 1 54  ? 55.739 -20.185 2.112   1.00 15.91 ?  54  ASN   B HB3  1 
ATOM   4846 H  HD21 . ASN   B 1 54  ? 57.980 -18.448 3.788   1.00 17.64 ?  54  ASN   B HD21 1 
ATOM   4847 H  HD22 . ASN   B 1 54  ? 57.369 -19.778 3.509   1.00 17.64 ?  54  ASN   B HD22 1 
ATOM   4848 N  N    . LYS   B 1 55  ? 57.558 -20.774 -0.150  1.00 13.26 ?  55  LYS   B N    1 
ATOM   4849 C  CA   . LYS   B 1 55  ? 58.912 -21.123 -0.573  1.00 14.24 ?  55  LYS   B CA   1 
ATOM   4850 C  C    . LYS   B 1 55  ? 59.205 -20.580 -1.965  1.00 14.18 ?  55  LYS   B C    1 
ATOM   4851 O  O    . LYS   B 1 55  ? 60.305 -20.075 -2.222  1.00 14.79 ?  55  LYS   B O    1 
ATOM   4852 C  CB   . LYS   B 1 55  ? 59.091 -22.640 -0.529  1.00 16.11 ?  55  LYS   B CB   1 
ATOM   4853 C  CG   . LYS   B 1 55  ? 60.454 -23.118 -0.999  1.00 20.36 ?  55  LYS   B CG   1 
ATOM   4854 C  CD   . LYS   B 1 55  ? 60.620 -24.615 -0.786  1.00 23.89 ?  55  LYS   B CD   1 
ATOM   4855 C  CE   . LYS   B 1 55  ? 60.698 -24.972 0.698   1.00 26.72 ?  55  LYS   B CE   1 
ATOM   4856 N  NZ   . LYS   B 1 55  ? 61.035 -26.400 0.920   1.00 28.30 ?  55  LYS   B NZ   1 
ATOM   4857 H  H    . LYS   B 1 55  ? 57.053 -21.445 0.035   1.00 15.94 ?  55  LYS   B H    1 
ATOM   4858 H  HA   . LYS   B 1 55  ? 59.545 -20.726 0.039   1.00 17.11 ?  55  LYS   B HA   1 
ATOM   4859 H  HB2  . LYS   B 1 55  ? 58.967 -22.932 0.388   1.00 19.35 ?  55  LYS   B HB2  1 
ATOM   4860 H  HB3  . LYS   B 1 55  ? 58.420 -23.052 -1.096  1.00 19.35 ?  55  LYS   B HB3  1 
ATOM   4861 H  HG2  . LYS   B 1 55  ? 60.550 -22.933 -1.948  1.00 24.45 ?  55  LYS   B HG2  1 
ATOM   4862 H  HG3  . LYS   B 1 55  ? 61.146 -22.658 -0.497  1.00 24.45 ?  55  LYS   B HG3  1 
ATOM   4863 H  HD2  . LYS   B 1 55  ? 59.859 -25.082 -1.170  1.00 28.69 ?  55  LYS   B HD2  1 
ATOM   4864 H  HD3  . LYS   B 1 55  ? 61.441 -24.913 -1.210  1.00 28.69 ?  55  LYS   B HD3  1 
ATOM   4865 H  HE2  . LYS   B 1 55  ? 61.381 -24.421 1.115   1.00 32.09 ?  55  LYS   B HE2  1 
ATOM   4866 H  HE3  . LYS   B 1 55  ? 59.835 -24.793 1.110   1.00 32.09 ?  55  LYS   B HE3  1 
ATOM   4867 H  HZ1  . LYS   B 1 55  ? 61.040 -26.572 1.793   1.00 33.98 ?  55  LYS   B HZ1  1 
ATOM   4868 H  HZ2  . LYS   B 1 55  ? 60.427 -26.914 0.525   1.00 33.98 ?  55  LYS   B HZ2  1 
ATOM   4869 H  HZ3  . LYS   B 1 55  ? 61.835 -26.575 0.582   1.00 33.98 ?  55  LYS   B HZ3  1 
ATOM   4870 N  N    . ALA   B 1 56  ? 58.232 -20.665 -2.877  1.00 13.64 ?  56  ALA   B N    1 
ATOM   4871 C  CA   . ALA   B 1 56  ? 58.449 -20.167 -4.230  1.00 14.30 ?  56  ALA   B CA   1 
ATOM   4872 C  C    . ALA   B 1 56  ? 58.735 -18.671 -4.233  1.00 13.85 ?  56  ALA   B C    1 
ATOM   4873 O  O    . ALA   B 1 56  ? 59.471 -18.179 -5.102  1.00 15.10 ?  56  ALA   B O    1 
ATOM   4874 C  CB   . ALA   B 1 56  ? 57.242 -20.495 -5.110  1.00 15.50 ?  56  ALA   B CB   1 
ATOM   4875 H  H    . ALA   B 1 56  ? 57.442 -20.987 -2.736  1.00 16.39 ?  56  ALA   B H    1 
ATOM   4876 H  HA   . ALA   B 1 56  ? 59.219 -20.612 -4.606  1.00 17.19 ?  56  ALA   B HA   1 
ATOM   4877 H  HB1  . ALA   B 1 56  ? 57.403 -20.163 -6.009  1.00 18.62 ?  56  ALA   B HB1  1 
ATOM   4878 H  HB2  . ALA   B 1 56  ? 57.121 -21.459 -5.135  1.00 18.62 ?  56  ALA   B HB2  1 
ATOM   4879 H  HB3  . ALA   B 1 56  ? 56.450 -20.075 -4.741  1.00 18.62 ?  56  ALA   B HB3  1 
ATOM   4880 N  N    . THR   B 1 57  ? 58.166 -17.931 -3.276  1.00 13.54 ?  57  THR   B N    1 
ATOM   4881 C  CA   . THR   B 1 57  ? 58.408 -16.498 -3.159  1.00 13.74 ?  57  THR   B CA   1 
ATOM   4882 C  C    . THR   B 1 57  ? 59.663 -16.173 -2.359  1.00 14.47 ?  57  THR   B C    1 
ATOM   4883 O  O    . THR   B 1 57  ? 59.909 -14.999 -2.067  1.00 15.17 ?  57  THR   B O    1 
ATOM   4884 C  CB   . THR   B 1 57  ? 57.210 -15.763 -2.523  1.00 12.77 ?  57  THR   B CB   1 
ATOM   4885 O  OG1  . THR   B 1 57  ? 57.190 -15.976 -1.102  1.00 13.27 ?  57  THR   B OG1  1 
ATOM   4886 C  CG2  . THR   B 1 57  ? 55.886 -16.189 -3.158  1.00 13.25 ?  57  THR   B CG2  1 
ATOM   4887 H  H    . THR   B 1 57  ? 57.619 -18.242 -2.681  1.00 16.27 ?  57  THR   B H    1 
ATOM   4888 H  HA   . THR   B 1 57  ? 58.523 -16.137 -4.052  1.00 16.51 ?  57  THR   B HA   1 
ATOM   4889 H  HB   . THR   B 1 57  ? 57.312 -14.813 -2.692  1.00 15.34 ?  57  THR   B HB   1 
ATOM   4890 H  HG1  . THR   B 1 57  ? 57.118 -16.794 -0.938  1.00 15.95 ?  57  THR   B HG1  1 
ATOM   4891 H  HG21 . THR   B 1 57  ? 55.164 -15.635 -2.828  1.00 15.92 ?  57  THR   B HG21 1 
ATOM   4892 H  HG22 . THR   B 1 57  ? 55.936 -16.104 -4.123  1.00 15.92 ?  57  THR   B HG22 1 
ATOM   4893 H  HG23 . THR   B 1 57  ? 55.696 -17.116 -2.937  1.00 15.92 ?  57  THR   B HG23 1 
ATOM   4894 N  N    . ASN   B 1 58  ? 60.458 -17.177 -1.997  1.00 15.15 ?  58  ASN   B N    1 
ATOM   4895 C  CA   . ASN   B 1 58  ? 61.659 -16.963 -1.191  1.00 18.39 ?  58  ASN   B CA   1 
ATOM   4896 C  C    . ASN   B 1 58  ? 61.329 -16.248 0.123   1.00 15.90 ?  58  ASN   B C    1 
ATOM   4897 O  O    . ASN   B 1 58  ? 62.071 -15.375 0.586   1.00 16.29 ?  58  ASN   B O    1 
ATOM   4898 C  CB   . ASN   B 1 58  ? 62.747 -16.223 -1.976  1.00 25.51 ?  58  ASN   B CB   1 
ATOM   4899 C  CG   . ASN   B 1 58  ? 64.124 -16.396 -1.364  1.00 35.08 ?  58  ASN   B CG   1 
ATOM   4900 O  OD1  . ASN   B 1 58  ? 64.445 -17.454 -0.823  1.00 37.55 ?  58  ASN   B OD1  1 
ATOM   4901 N  ND2  . ASN   B 1 58  ? 64.943 -15.355 -1.443  1.00 41.88 ?  58  ASN   B ND2  1 
ATOM   4902 H  H    . ASN   B 1 58  ? 60.321 -18.004 -2.206  1.00 18.20 ?  58  ASN   B H    1 
ATOM   4903 H  HA   . ASN   B 1 58  ? 62.021 -17.836 -0.970  1.00 22.09 ?  58  ASN   B HA   1 
ATOM   4904 H  HB2  . ASN   B 1 58  ? 62.779 -16.567 -2.886  1.00 30.63 ?  58  ASN   B HB2  1 
ATOM   4905 H  HB3  . ASN   B 1 58  ? 62.545 -15.276 -1.989  1.00 30.63 ?  58  ASN   B HB3  1 
ATOM   4906 H  HD21 . ASN   B 1 58  ? 65.735 -15.405 -1.110  1.00 50.28 ?  58  ASN   B HD21 1 
ATOM   4907 H  HD22 . ASN   B 1 58  ? 64.682 -14.632 -1.826  1.00 50.28 ?  58  ASN   B HD22 1 
ATOM   4908 N  N    . ASN   B 1 59  ? 60.206 -16.630 0.731   1.00 14.95 ?  59  ASN   B N    1 
ATOM   4909 C  CA   . ASN   B 1 59  ? 59.730 -16.155 2.032   1.00 14.89 ?  59  ASN   B CA   1 
ATOM   4910 C  C    . ASN   B 1 59  ? 59.130 -14.750 1.973   1.00 14.39 ?  59  ASN   B C    1 
ATOM   4911 O  O    . ASN   B 1 59  ? 58.706 -14.237 3.017   1.00 14.32 ?  59  ASN   B O    1 
ATOM   4912 C  CB   . ASN   B 1 59  ? 60.805 -16.210 3.135   1.00 15.94 ?  59  ASN   B CB   1 
ATOM   4913 C  CG   . ASN   B 1 59  ? 60.219 -16.368 4.520   1.00 16.92 ?  59  ASN   B CG   1 
ATOM   4914 O  OD1  . ASN   B 1 59  ? 59.387 -17.247 4.761   1.00 16.91 ?  59  ASN   B OD1  1 
ATOM   4915 N  ND2  . ASN   B 1 59  ? 60.646 -15.518 5.443   1.00 17.36 ?  59  ASN   B ND2  1 
ATOM   4916 H  H    . ASN   B 1 59  ? 59.666 -17.207 0.385   1.00 17.96 ?  59  ASN   B H    1 
ATOM   4917 H  HA   . ASN   B 1 59  ? 59.025 -16.754 2.317   1.00 17.89 ?  59  ASN   B HA   1 
ATOM   4918 H  HB2  . ASN   B 1 59  ? 61.392 -16.970 2.982   1.00 19.15 ?  59  ASN   B HB2  1 
ATOM   4919 H  HB3  . ASN   B 1 59  ? 61.319 -15.389 3.126   1.00 19.15 ?  59  ASN   B HB3  1 
ATOM   4920 H  HD21 . ASN   B 1 59  ? 60.343 -15.565 6.250   1.00 20.85 ?  59  ASN   B HD21 1 
ATOM   4921 H  HD22 . ASN   B 1 59  ? 61.230 -14.919 5.243   1.00 20.85 ?  59  ASN   B HD22 1 
ATOM   4922 N  N    . ALA   B 1 60  ? 59.068 -14.110 0.802   1.00 13.91 ?  60  ALA   B N    1 
ATOM   4923 C  CA   . ALA   B 1 60  ? 58.476 -12.777 0.728   1.00 13.99 ?  60  ALA   B CA   1 
ATOM   4924 C  C    . ALA   B 1 60  ? 57.007 -12.799 1.131   1.00 13.01 ?  60  ALA   B C    1 
ATOM   4925 O  O    . ALA   B 1 60  ? 56.507 -11.849 1.744   1.00 13.49 ?  60  ALA   B O    1 
ATOM   4926 C  CB   . ALA   B 1 60  ? 58.639 -12.199 -0.676  1.00 14.83 ?  60  ALA   B CB   1 
ATOM   4927 H  H    . ALA   B 1 60  ? 59.365 -14.425 0.058   1.00 16.71 ?  60  ALA   B H    1 
ATOM   4928 H  HA   . ALA   B 1 60  ? 58.945 -12.197 1.348   1.00 16.80 ?  60  ALA   B HA   1 
ATOM   4929 H  HB1  . ALA   B 1 60  ? 58.240 -11.320 -0.699  1.00 17.82 ?  60  ALA   B HB1  1 
ATOM   4930 H  HB2  . ALA   B 1 60  ? 59.586 -12.144 -0.886  1.00 17.82 ?  60  ALA   B HB2  1 
ATOM   4931 H  HB3  . ALA   B 1 60  ? 58.196 -12.786 -1.309  1.00 17.82 ?  60  ALA   B HB3  1 
ATOM   4932 N  N    . MET   B 1 61  ? 56.296 -13.874 0.783   1.00 12.30 ?  61  MET   B N    1 
ATOM   4933 C  CA   . MET   B 1 61  ? 54.897 -13.996 1.174   1.00 11.93 ?  61  MET   B CA   1 
ATOM   4934 C  C    . MET   B 1 61  ? 54.754 -13.995 2.695   1.00 11.95 ?  61  MET   B C    1 
ATOM   4935 O  O    . MET   B 1 61  ? 53.856 -13.337 3.241   1.00 11.98 ?  61  MET   B O    1 
ATOM   4936 C  CB   . MET   B 1 61  ? 54.315 -15.269 0.553   1.00 12.17 ?  61  MET   B CB   1 
ATOM   4937 C  CG   . MET   B 1 61  ? 52.867 -15.547 0.945   1.00 12.11 ?  61  MET   B CG   1 
ATOM   4938 S  SD   . MET   B 1 61  ? 52.223 -17.051 0.188   1.00 12.58 ?  61  MET   B SD   1 
ATOM   4939 C  CE   . MET   B 1 61  ? 51.951 -16.464 -1.481  1.00 13.57 ?  61  MET   B CE   1 
ATOM   4940 H  H    . MET   B 1 61  ? 56.601 -14.545 0.326   1.00 14.78 ?  61  MET   B H    1 
ATOM   4941 H  HA   . MET   B 1 61  ? 54.407 -13.247 0.806   1.00 14.34 ?  61  MET   B HA   1 
ATOM   4942 H  HB2  . MET   B 1 61  ? 54.349 -15.193 -0.416  1.00 14.62 ?  61  MET   B HB2  1 
ATOM   4943 H  HB3  . MET   B 1 61  ? 54.850 -16.031 0.835   1.00 14.62 ?  61  MET   B HB3  1 
ATOM   4944 H  HG2  . MET   B 1 61  ? 52.812 -15.657 1.908   1.00 14.55 ?  61  MET   B HG2  1 
ATOM   4945 H  HG3  . MET   B 1 61  ? 52.313 -14.806 0.662   1.00 14.55 ?  61  MET   B HG3  1 
ATOM   4946 H  HE1  . MET   B 1 61  ? 51.574 -17.183 -2.011  1.00 16.30 ?  61  MET   B HE1  1 
ATOM   4947 H  HE2  . MET   B 1 61  ? 51.330 -15.714 -1.457  1.00 16.30 ?  61  MET   B HE2  1 
ATOM   4948 H  HE3  . MET   B 1 61  ? 52.795 -16.177 -1.860  1.00 16.30 ?  61  MET   B HE3  1 
ATOM   4949 N  N    . GLN   B 1 62  ? 55.629 -14.714 3.401   1.00 11.94 ?  62  GLN   B N    1 
ATOM   4950 C  CA   . GLN   B 1 62  ? 55.525 -14.757 4.856   1.00 12.46 ?  62  GLN   B CA   1 
ATOM   4951 C  C    . GLN   B 1 62  ? 55.807 -13.398 5.479   1.00 12.62 ?  62  GLN   B C    1 
ATOM   4952 O  O    . GLN   B 1 62  ? 55.124 -12.992 6.426   1.00 13.32 ?  62  GLN   B O    1 
ATOM   4953 C  CB   . GLN   B 1 62  ? 56.478 -15.802 5.433   1.00 13.05 ?  62  GLN   B CB   1 
ATOM   4954 C  CG   . GLN   B 1 62  ? 56.240 -16.066 6.909   1.00 13.34 ?  62  GLN   B CG   1 
ATOM   4955 C  CD   . GLN   B 1 62  ? 54.868 -16.664 7.143   1.00 12.74 ?  62  GLN   B CD   1 
ATOM   4956 O  OE1  . GLN   B 1 62  ? 54.611 -17.807 6.764   1.00 13.44 ?  62  GLN   B OE1  1 
ATOM   4957 N  NE2  . GLN   B 1 62  ? 53.960 -15.882 7.717   1.00 13.12 ?  62  GLN   B NE2  1 
ATOM   4958 H  H    . GLN   B 1 62  ? 56.268 -15.180 3.066   1.00 14.34 ?  62  GLN   B H    1 
ATOM   4959 H  HA   . GLN   B 1 62  ? 54.619 -15.013 5.095   1.00 14.98 ?  62  GLN   B HA   1 
ATOM   4960 H  HB2  . GLN   B 1 62  ? 56.361 -16.640 4.955   1.00 15.68 ?  62  GLN   B HB2  1 
ATOM   4961 H  HB3  . GLN   B 1 62  ? 57.392 -15.488 5.324   1.00 15.68 ?  62  GLN   B HB3  1 
ATOM   4962 H  HG2  . GLN   B 1 62  ? 56.908 -16.693 7.229   1.00 16.03 ?  62  GLN   B HG2  1 
ATOM   4963 H  HG3  . GLN   B 1 62  ? 56.304 -15.231 7.397   1.00 16.03 ?  62  GLN   B HG3  1 
ATOM   4964 H  HE21 . GLN   B 1 62  ? 54.169 -15.083 7.959   1.00 15.76 ?  62  GLN   B HE21 1 
ATOM   4965 H  HE22 . GLN   B 1 62  ? 53.167 -16.182 7.863   1.00 15.76 ?  62  GLN   B HE22 1 
ATOM   4966 N  N    . VAL   B 1 63  ? 56.822 -12.689 4.984   1.00 13.44 ?  63  VAL   B N    1 
ATOM   4967 C  CA   . VAL   B 1 63  ? 57.130 -11.370 5.534   1.00 14.65 ?  63  VAL   B CA   1 
ATOM   4968 C  C    . VAL   B 1 63  ? 55.939 -10.432 5.349   1.00 13.19 ?  63  VAL   B C    1 
ATOM   4969 O  O    . VAL   B 1 63  ? 55.524 -9.724  6.277   1.00 13.88 ?  63  VAL   B O    1 
ATOM   4970 C  CB   . VAL   B 1 63  ? 58.420 -10.818 4.903   1.00 15.45 ?  63  VAL   B CB   1 
ATOM   4971 C  CG1  . VAL   B 1 63  ? 58.643 -9.370  5.332   1.00 16.38 ?  63  VAL   B CG1  1 
ATOM   4972 C  CG2  . VAL   B 1 63  ? 59.611 -11.685 5.305   1.00 15.95 ?  63  VAL   B CG2  1 
ATOM   4973 H  H    . VAL   B 1 63  ? 57.336 -12.949 4.340   1.00 16.16 ?  63  VAL   B H    1 
ATOM   4974 H  HA   . VAL   B 1 63  ? 57.291 -11.467 6.482   1.00 17.61 ?  63  VAL   B HA   1 
ATOM   4975 H  HB   . VAL   B 1 63  ? 58.349 -10.846 3.934   1.00 18.56 ?  63  VAL   B HB   1 
ATOM   4976 H  HG11 . VAL   B 1 63  ? 59.561 -9.125  5.148   1.00 19.68 ?  63  VAL   B HG11 1 
ATOM   4977 H  HG12 . VAL   B 1 63  ? 58.040 -8.799  4.833   1.00 19.68 ?  63  VAL   B HG12 1 
ATOM   4978 H  HG13 . VAL   B 1 63  ? 58.465 -9.297  6.283   1.00 19.68 ?  63  VAL   B HG13 1 
ATOM   4979 H  HG21 . VAL   B 1 63  ? 60.421 -11.316 4.918   1.00 19.16 ?  63  VAL   B HG21 1 
ATOM   4980 H  HG22 . VAL   B 1 63  ? 59.685 -11.689 6.275   1.00 19.16 ?  63  VAL   B HG22 1 
ATOM   4981 H  HG23 . VAL   B 1 63  ? 59.474 -12.589 4.984   1.00 19.16 ?  63  VAL   B HG23 1 
ATOM   4982 N  N    . GLU   B 1 64  ? 55.375 -10.418 4.144   1.00 12.84 ?  64  GLU   B N    1 
ATOM   4983 C  CA   . GLU   B 1 64  ? 54.208 -9.586  3.865   1.00 12.74 ?  64  GLU   B CA   1 
ATOM   4984 C  C    . GLU   B 1 64  ? 53.025 -9.986  4.740   1.00 12.47 ?  64  GLU   B C    1 
ATOM   4985 O  O    . GLU   B 1 64  ? 52.277 -9.126  5.234   1.00 12.85 ?  64  GLU   B O    1 
ATOM   4986 C  CB   . GLU   B 1 64  ? 53.850 -9.748  2.388   1.00 13.12 ?  64  GLU   B CB   1 
ATOM   4987 C  CG   . GLU   B 1 64  ? 52.587 -9.006  1.943   1.00 13.12 ?  64  GLU   B CG   1 
ATOM   4988 C  CD   . GLU   B 1 64  ? 52.058 -9.506  0.609   1.00 13.83 ?  64  GLU   B CD   1 
ATOM   4989 O  OE1  . GLU   B 1 64  ? 52.237 -10.716 0.304   1.00 14.22 ?  64  GLU   B OE1  1 
ATOM   4990 O  OE2  . GLU   B 1 64  ? 51.440 -8.694  -0.128  1.00 14.53 -1 64  GLU   B OE2  1 
ATOM   4991 H  H    . GLU   B 1 64  ? 55.651 -10.884 3.468   1.00 15.43 ?  64  GLU   B H    1 
ATOM   4992 H  HA   . GLU   B 1 64  ? 54.422 -8.660  4.033   1.00 15.31 ?  64  GLU   B HA   1 
ATOM   4993 H  HB2  . GLU   B 1 64  ? 54.582 -9.409  1.850   1.00 15.77 ?  64  GLU   B HB2  1 
ATOM   4994 H  HB3  . GLU   B 1 64  ? 53.715 -10.688 2.200   1.00 15.77 ?  64  GLU   B HB3  1 
ATOM   4995 H  HG2  . GLU   B 1 64  ? 51.882 -9.132  2.603   1.00 15.76 ?  64  GLU   B HG2  1 
ATOM   4996 H  HG3  . GLU   B 1 64  ? 52.787 -8.063  1.853   1.00 15.76 ?  64  GLU   B HG3  1 
ATOM   4997 N  N    . SER   B 1 65  ? 52.841 -11.293 4.932   1.00 12.23 ?  65  SER   B N    1 
ATOM   4998 C  CA   . SER   B 1 65  ? 51.734 -11.802 5.729   1.00 12.23 ?  65  SER   B CA   1 
ATOM   4999 C  C    . SER   B 1 65  ? 51.862 -11.402 7.192   1.00 12.57 ?  65  SER   B C    1 
ATOM   5000 O  O    . SER   B 1 65  ? 50.863 -11.025 7.821   1.00 12.81 ?  65  SER   B O    1 
ATOM   5001 C  CB   . SER   B 1 65  ? 51.657 -13.325 5.593   1.00 12.64 ?  65  SER   B CB   1 
ATOM   5002 O  OG   . SER   B 1 65  ? 51.299 -13.722 4.276   1.00 12.44 ?  65  SER   B OG   1 
ATOM   5003 H  H    . SER   B 1 65  ? 53.349 -11.915 4.613   1.00 14.70 ?  65  SER   B H    1 
ATOM   5004 H  HA   . SER   B 1 65  ? 50.901 -11.432 5.391   1.00 14.70 ?  65  SER   B HA   1 
ATOM   5005 H  HB2  . SER   B 1 65  ? 52.520 -13.703 5.812   1.00 15.19 ?  65  SER   B HB2  1 
ATOM   5006 H  HB3  . SER   B 1 65  ? 50.985 -13.661 6.213   1.00 15.19 ?  65  SER   B HB3  1 
ATOM   5007 H  HG   . SER   B 1 65  ? 51.869 -13.432 3.724   1.00 14.96 ?  65  SER   B HG   1 
ATOM   5008 N  N    . ASP   B 1 66  ? 53.069 -11.500 7.764   1.00 12.88 ?  66  ASP   B N    1 
ATOM   5009 C  CA   . ASP   B 1 66  ? 53.245 -11.104 9.159   1.00 13.28 ?  66  ASP   B CA   1 
ATOM   5010 C  C    . ASP   B 1 66  ? 52.931 -9.624  9.347   1.00 13.22 ?  66  ASP   B C    1 
ATOM   5011 O  O    . ASP   B 1 66  ? 52.349 -9.229  10.363  1.00 13.96 ?  66  ASP   B O    1 
ATOM   5012 C  CB   . ASP   B 1 66  ? 54.668 -11.417 9.630   1.00 14.41 ?  66  ASP   B CB   1 
ATOM   5013 C  CG   . ASP   B 1 66  ? 54.938 -12.914 9.770   1.00 15.97 ?  66  ASP   B CG   1 
ATOM   5014 O  OD1  . ASP   B 1 66  ? 53.989 -13.725 9.687   1.00 16.88 ?  66  ASP   B OD1  1 
ATOM   5015 O  OD2  . ASP   B 1 66  ? 56.118 -13.277 9.983   1.00 19.10 -1 66  ASP   B OD2  1 
ATOM   5016 H  H    . ASP   B 1 66  ? 53.770 -11.806 7.382   1.00 15.47 ?  66  ASP   B H    1 
ATOM   5017 H  HA   . ASP   B 1 66  ? 52.634 -11.603 9.721   1.00 15.96 ?  66  ASP   B HA   1 
ATOM   5018 H  HB2  . ASP   B 1 66  ? 55.302 -11.057 8.993   1.00 17.31 ?  66  ASP   B HB2  1 
ATOM   5019 H  HB3  . ASP   B 1 66  ? 54.812 -11.008 10.504  1.00 17.31 ?  66  ASP   B HB3  1 
ATOM   5020 N  N    . ASP   B 1 67  ? 53.318 -8.785  8.383   1.00 12.88 ?  67  ASP   B N    1 
ATOM   5021 C  CA   . ASP   B 1 67  ? 52.971 -7.372  8.456   1.00 13.55 ?  67  ASP   B CA   1 
ATOM   5022 C  C    . ASP   B 1 67  ? 51.459 -7.167  8.373   1.00 13.68 ?  67  ASP   B C    1 
ATOM   5023 O  O    . ASP   B 1 67  ? 50.898 -6.356  9.119   1.00 14.10 ?  67  ASP   B O    1 
ATOM   5024 C  CB   . ASP   B 1 67  ? 53.684 -6.609  7.346   1.00 14.81 ?  67  ASP   B CB   1 
ATOM   5025 C  CG   . ASP   B 1 67  ? 53.265 -5.161  7.296   1.00 16.28 ?  67  ASP   B CG   1 
ATOM   5026 O  OD1  . ASP   B 1 67  ? 53.771 -4.343  8.103   1.00 17.54 ?  67  ASP   B OD1  1 
ATOM   5027 O  OD2  . ASP   B 1 67  ? 52.394 -4.864  6.462   1.00 17.39 -1 67  ASP   B OD2  1 
ATOM   5028 H  H    . ASP   B 1 67  ? 53.779 -9.008  7.690   1.00 15.48 ?  67  ASP   B H    1 
ATOM   5029 H  HA   . ASP   B 1 67  ? 53.272 -7.013  9.302   1.00 16.28 ?  67  ASP   B HA   1 
ATOM   5030 H  HB2  . ASP   B 1 67  ? 54.641 -6.642  7.498   1.00 17.79 ?  67  ASP   B HB2  1 
ATOM   5031 H  HB3  . ASP   B 1 67  ? 53.471 -7.018  6.489   1.00 17.79 ?  67  ASP   B HB3  1 
ATOM   5032 N  N    . TYR   B 1 68  ? 50.779 -7.900  7.479   1.00 13.41 ?  68  TYR   B N    1 
ATOM   5033 C  CA   . TYR   B 1 68  ? 49.321 -7.821  7.401   1.00 14.17 ?  68  TYR   B CA   1 
ATOM   5034 C  C    . TYR   B 1 68  ? 48.683 -8.161  8.743   1.00 14.07 ?  68  TYR   B C    1 
ATOM   5035 O  O    . TYR   B 1 68  ? 47.738 -7.488  9.182   1.00 14.45 ?  68  TYR   B O    1 
ATOM   5036 C  CB   . TYR   B 1 68  ? 48.788 -8.751  6.302   1.00 14.78 ?  68  TYR   B CB   1 
ATOM   5037 C  CG   . TYR   B 1 68  ? 47.281 -8.899  6.361   1.00 16.34 ?  68  TYR   B CG   1 
ATOM   5038 C  CD1  . TYR   B 1 68  ? 46.692 -9.850  7.188   1.00 17.16 ?  68  TYR   B CD1  1 
ATOM   5039 C  CD2  . TYR   B 1 68  ? 46.447 -8.068  5.627   1.00 17.15 ?  68  TYR   B CD2  1 
ATOM   5040 C  CE1  . TYR   B 1 68  ? 45.327 -9.971  7.282   1.00 17.96 ?  68  TYR   B CE1  1 
ATOM   5041 C  CE2  . TYR   B 1 68  ? 45.059 -8.198  5.705   1.00 17.57 ?  68  TYR   B CE2  1 
ATOM   5042 C  CZ   . TYR   B 1 68  ? 44.522 -9.148  6.540   1.00 17.73 ?  68  TYR   B CZ   1 
ATOM   5043 O  OH   . TYR   B 1 68  ? 43.151 -9.270  6.646   1.00 18.90 ?  68  TYR   B OH   1 
ATOM   5044 H  H    . TYR   B 1 68  ? 51.137 -8.455  6.918   1.00 16.12 ?  68  TYR   B H    1 
ATOM   5045 H  HA   . TYR   B 1 68  ? 49.072 -6.916  7.175   1.00 17.02 ?  68  TYR   B HA   1 
ATOM   5046 H  HB2  . TYR   B 1 68  ? 49.014 -8.383  5.435   1.00 17.76 ?  68  TYR   B HB2  1 
ATOM   5047 H  HB3  . TYR   B 1 68  ? 49.177 -9.631  6.407   1.00 17.76 ?  68  TYR   B HB3  1 
ATOM   5048 H  HD1  . TYR   B 1 68  ? 47.230 -10.417 7.692   1.00 20.62 ?  68  TYR   B HD1  1 
ATOM   5049 H  HD2  . TYR   B 1 68  ? 46.816 -7.417  5.081   1.00 20.60 ?  68  TYR   B HD2  1 
ATOM   5050 H  HE1  . TYR   B 1 68  ? 44.946 -10.627 7.829   1.00 21.57 ?  68  TYR   B HE1  1 
ATOM   5051 H  HE2  . TYR   B 1 68  ? 44.500 -7.632  5.221   1.00 21.11 ?  68  TYR   B HE2  1 
ATOM   5052 H  HH   . TYR   B 1 68  ? 42.762 -8.721  6.137   1.00 22.70 ?  68  TYR   B HH   1 
ATOM   5053 N  N    . ILE   B 1 69  ? 49.165 -9.227  9.393   1.00 13.49 ?  69  ILE   B N    1 
ATOM   5054 C  CA   . ILE   B 1 69  ? 48.607 -9.653  10.674  1.00 13.85 ?  69  ILE   B CA   1 
ATOM   5055 C  C    . ILE   B 1 69  ? 48.855 -8.603  11.750  1.00 13.83 ?  69  ILE   B C    1 
ATOM   5056 O  O    . ILE   B 1 69  ? 47.982 -8.326  12.581  1.00 14.06 ?  69  ILE   B O    1 
ATOM   5057 C  CB   . ILE   B 1 69  ? 49.183 -11.027 11.071  1.00 14.55 ?  69  ILE   B CB   1 
ATOM   5058 C  CG1  . ILE   B 1 69  ? 48.651 -12.133 10.151  1.00 15.09 ?  69  ILE   B CG1  1 
ATOM   5059 C  CG2  . ILE   B 1 69  ? 48.897 -11.341 12.536  1.00 15.69 ?  69  ILE   B CG2  1 
ATOM   5060 C  CD1  . ILE   B 1 69  ? 47.170 -12.435 10.312  1.00 15.84 ?  69  ILE   B CD1  1 
ATOM   5061 H  H    . ILE   B 1 69  ? 49.814 -9.720  9.110   1.00 16.21 ?  69  ILE   B H    1 
ATOM   5062 H  HA   . ILE   B 1 69  ? 47.651 -9.752  10.576  1.00 16.64 ?  69  ILE   B HA   1 
ATOM   5063 H  HB   . ILE   B 1 69  ? 50.148 -10.992 10.959  1.00 17.48 ?  69  ILE   B HB   1 
ATOM   5064 H  HG12 . ILE   B 1 69  ? 48.800 -11.869 9.229   1.00 18.14 ?  69  ILE   B HG12 1 
ATOM   5065 H  HG13 . ILE   B 1 69  ? 49.140 -12.953 10.334  1.00 18.14 ?  69  ILE   B HG13 1 
ATOM   5066 H  HG21 . ILE   B 1 69  ? 49.043 -12.291 12.687  1.00 18.85 ?  69  ILE   B HG21 1 
ATOM   5067 H  HG22 . ILE   B 1 69  ? 49.496 -10.826 13.097  1.00 18.85 ?  69  ILE   B HG22 1 
ATOM   5068 H  HG23 . ILE   B 1 69  ? 47.975 -11.116 12.733  1.00 18.85 ?  69  ILE   B HG23 1 
ATOM   5069 H  HD11 . ILE   B 1 69  ? 46.932 -13.156 9.709   1.00 19.03 ?  69  ILE   B HD11 1 
ATOM   5070 H  HD12 . ILE   B 1 69  ? 46.998 -12.701 11.228  1.00 19.03 ?  69  ILE   B HD12 1 
ATOM   5071 H  HD13 . ILE   B 1 69  ? 46.659 -11.642 10.094  1.00 19.03 ?  69  ILE   B HD13 1 
ATOM   5072 N  N    . ALA   B 1 70  ? 50.044 -8.006  11.764  1.00 13.65 ?  70  ALA   B N    1 
ATOM   5073 C  CA   . ALA   B 1 70  ? 50.323 -6.965  12.749  1.00 13.82 ?  70  ALA   B CA   1 
ATOM   5074 C  C    . ALA   B 1 70  ? 49.316 -5.831  12.639  1.00 14.12 ?  70  ALA   B C    1 
ATOM   5075 O  O    . ALA   B 1 70  ? 48.862 -5.294  13.653  1.00 14.57 ?  70  ALA   B O    1 
ATOM   5076 C  CB   . ALA   B 1 70  ? 51.748 -6.439  12.574  1.00 14.28 ?  70  ALA   B CB   1 
ATOM   5077 H  H    . ALA   B 1 70  ? 50.687 -8.178  11.224  1.00 16.41 ?  70  ALA   B H    1 
ATOM   5078 H  HA   . ALA   B 1 70  ? 50.254 -7.341  13.637  1.00 16.60 ?  70  ALA   B HA   1 
ATOM   5079 H  HB1  . ALA   B 1 70  ? 51.935 -5.783  13.266  1.00 17.16 ?  70  ALA   B HB1  1 
ATOM   5080 H  HB2  . ALA   B 1 70  ? 52.374 -7.179  12.649  1.00 17.16 ?  70  ALA   B HB2  1 
ATOM   5081 H  HB3  . ALA   B 1 70  ? 51.835 -6.027  11.698  1.00 17.16 ?  70  ALA   B HB3  1 
ATOM   5082 N  N    . THR   B 1 71  ? 48.944 -5.467  11.416  1.00 14.50 ?  71  THR   B N    1 
ATOM   5083 C  CA   . THR   B 1 71  ? 48.049 -4.336  11.207  1.00 15.40 ?  71  THR   B CA   1 
ATOM   5084 C  C    . THR   B 1 71  ? 46.585 -4.706  11.420  1.00 15.86 ?  71  THR   B C    1 
ATOM   5085 O  O    . THR   B 1 71  ? 45.809 -3.896  11.944  1.00 17.38 ?  71  THR   B O    1 
ATOM   5086 C  CB   . THR   B 1 71  ? 48.266 -3.773  9.802   1.00 17.05 ?  71  THR   B CB   1 
ATOM   5087 O  OG1  . THR   B 1 71  ? 49.587 -3.229  9.704   1.00 18.94 ?  71  THR   B OG1  1 
ATOM   5088 C  CG2  . THR   B 1 71  ? 47.240 -2.700  9.470   1.00 18.29 ?  71  THR   B CG2  1 
ATOM   5089 H  H    . THR   B 1 71  ? 49.193 -5.862  10.692  1.00 17.42 ?  71  THR   B H    1 
ATOM   5090 H  HA   . THR   B 1 71  ? 48.272 -3.640  11.840  1.00 18.51 ?  71  THR   B HA   1 
ATOM   5091 H  HB   . THR   B 1 71  ? 48.183 -4.482  9.149   1.00 20.48 ?  71  THR   B HB   1 
ATOM   5092 H  HG1  . THR   B 1 71  ? 49.711 -2.892  8.938   1.00 22.75 ?  71  THR   B HG1  1 
ATOM   5093 H  HG21 . THR   B 1 71  ? 47.543 -2.171  8.712   1.00 21.97 ?  71  THR   B HG21 1 
ATOM   5094 H  HG22 . THR   B 1 71  ? 46.390 -3.107  9.245   1.00 21.97 ?  71  THR   B HG22 1 
ATOM   5095 H  HG23 . THR   B 1 71  ? 47.118 -2.109  10.231  1.00 21.97 ?  71  THR   B HG23 1 
ATOM   5096 N  N    . ASN   B 1 72  ? 46.189 -5.916  11.018  1.00 15.48 ?  72  ASN   B N    1 
ATOM   5097 C  CA   . ASN   B 1 72  ? 44.786 -6.278  10.898  1.00 16.23 ?  72  ASN   B CA   1 
ATOM   5098 C  C    . ASN   B 1 72  ? 44.324 -7.369  11.852  1.00 16.73 ?  72  ASN   B C    1 
ATOM   5099 O  O    . ASN   B 1 72  ? 43.109 -7.532  12.023  1.00 17.94 ?  72  ASN   B O    1 
ATOM   5100 C  CB   . ASN   B 1 72  ? 44.473 -6.719  9.458   1.00 16.94 ?  72  ASN   B CB   1 
ATOM   5101 C  CG   . ASN   B 1 72  ? 44.762 -5.630  8.449   1.00 17.81 ?  72  ASN   B CG   1 
ATOM   5102 O  OD1  . ASN   B 1 72  ? 45.781 -5.651  7.757   1.00 19.00 ?  72  ASN   B OD1  1 
ATOM   5103 N  ND2  . ASN   B 1 72  ? 43.885 -4.647  8.384   1.00 19.59 ?  72  ASN   B ND2  1 
ATOM   5104 H  H    . ASN   B 1 72  ? 46.733 -6.561  10.814  1.00 18.59 ?  72  ASN   B H    1 
ATOM   5105 H  HA   . ASN   B 1 72  ? 44.255 -5.494  11.083  1.00 19.49 ?  72  ASN   B HA   1 
ATOM   5106 H  HB2  . ASN   B 1 72  ? 45.022 -7.488  9.235   1.00 20.35 ?  72  ASN   B HB2  1 
ATOM   5107 H  HB3  . ASN   B 1 72  ? 43.536 -6.946  9.394   1.00 20.35 ?  72  ASN   B HB3  1 
ATOM   5108 H  HD21 . ASN   B 1 72  ? 44.002 -4.000  7.827   1.00 23.53 ?  72  ASN   B HD21 1 
ATOM   5109 H  HD22 . ASN   B 1 72  ? 43.186 -4.660  8.884   1.00 23.53 ?  72  ASN   B HD22 1 
ATOM   5110 N  N    . GLY   B 1 73  ? 45.234 -8.114  12.474  1.00 16.21 ?  73  GLY   B N    1 
ATOM   5111 C  CA   . GLY   B 1 73  ? 44.842 -9.251  13.268  1.00 15.66 ?  73  GLY   B CA   1 
ATOM   5112 C  C    . GLY   B 1 73  ? 44.485 -10.441 12.405  1.00 14.33 ?  73  GLY   B C    1 
ATOM   5113 O  O    . GLY   B 1 73  ? 44.467 -10.362 11.174  1.00 14.14 ?  73  GLY   B O    1 
ATOM   5114 H  H    . GLY   B 1 73  ? 46.085 -7.976  12.450  1.00 19.48 ?  73  GLY   B H    1 
ATOM   5115 H  HA2  . GLY   B 1 73  ? 45.571 -9.503  13.860  1.00 18.81 ?  73  GLY   B HA2  1 
ATOM   5116 H  HA3  . GLY   B 1 73  ? 44.072 -9.020  13.812  1.00 18.81 ?  73  GLY   B HA3  1 
ATOM   5117 N  N    . PRO   B 1 74  ? 44.177 -11.563 13.051  1.00 14.62 ?  74  PRO   B N    1 
ATOM   5118 C  CA   . PRO   B 1 74  ? 43.924 -12.805 12.316  1.00 14.10 ?  74  PRO   B CA   1 
ATOM   5119 C  C    . PRO   B 1 74  ? 42.627 -12.752 11.527  1.00 13.51 ?  74  PRO   B C    1 
ATOM   5120 O  O    . PRO   B 1 74  ? 41.694 -12.010 11.854  1.00 14.80 ?  74  PRO   B O    1 
ATOM   5121 C  CB   . PRO   B 1 74  ? 43.837 -13.857 13.429  1.00 15.14 ?  74  PRO   B CB   1 
ATOM   5122 C  CG   . PRO   B 1 74  ? 43.401 -13.088 14.636  1.00 16.90 ?  74  PRO   B CG   1 
ATOM   5123 C  CD   . PRO   B 1 74  ? 44.064 -11.749 14.508  1.00 16.20 ?  74  PRO   B CD   1 
ATOM   5124 H  HA   . PRO   B 1 74  ? 44.667 -13.010 11.723  1.00 16.94 ?  74  PRO   B HA   1 
ATOM   5125 H  HB2  . PRO   B 1 74  ? 43.178 -14.529 13.189  1.00 18.19 ?  74  PRO   B HB2  1 
ATOM   5126 H  HB3  . PRO   B 1 74  ? 44.707 -14.260 13.568  1.00 18.19 ?  74  PRO   B HB3  1 
ATOM   5127 H  HG2  . PRO   B 1 74  ? 42.435 -12.992 14.632  1.00 20.31 ?  74  PRO   B HG2  1 
ATOM   5128 H  HG3  . PRO   B 1 74  ? 43.697 -13.542 15.438  1.00 20.31 ?  74  PRO   B HG3  1 
ATOM   5129 H  HD2  . PRO   B 1 74  ? 43.504 -11.056 14.900  1.00 19.46 ?  74  PRO   B HD2  1 
ATOM   5130 H  HD3  . PRO   B 1 74  ? 44.943 -11.766 14.918  1.00 19.46 ?  74  PRO   B HD3  1 
ATOM   5131 N  N    . LEU   B 1 75  ? 42.590 -13.554 10.468  1.00 13.10 ?  75  LEU   B N    1 
ATOM   5132 C  CA   . LEU   B 1 75  ? 41.376 -13.757 9.700   1.00 12.75 ?  75  LEU   B CA   1 
ATOM   5133 C  C    . LEU   B 1 75  ? 40.393 -14.607 10.499  1.00 13.49 ?  75  LEU   B C    1 
ATOM   5134 O  O    . LEU   B 1 75  ? 40.731 -15.197 11.526  1.00 14.46 ?  75  LEU   B O    1 
ATOM   5135 C  CB   . LEU   B 1 75  ? 41.695 -14.476 8.389   1.00 12.82 ?  75  LEU   B CB   1 
ATOM   5136 C  CG   . LEU   B 1 75  ? 42.531 -13.711 7.360   1.00 14.50 ?  75  LEU   B CG   1 
ATOM   5137 C  CD1  . LEU   B 1 75  ? 42.728 -14.532 6.094   1.00 15.94 ?  75  LEU   B CD1  1 
ATOM   5138 C  CD2  . LEU   B 1 75  ? 41.916 -12.378 7.034   1.00 18.49 ?  75  LEU   B CD2  1 
ATOM   5139 H  H    . LEU   B 1 75  ? 43.266 -14.004 10.172  1.00 15.74 ?  75  LEU   B H    1 
ATOM   5140 H  HA   . LEU   B 1 75  ? 40.966 -12.903 9.499   1.00 15.32 ?  75  LEU   B HA   1 
ATOM   5141 H  HB2  . LEU   B 1 75  ? 42.182 -15.294 8.601   1.00 15.41 ?  75  LEU   B HB2  1 
ATOM   5142 H  HB3  . LEU   B 1 75  ? 40.858 -14.713 7.958   1.00 15.41 ?  75  LEU   B HB3  1 
ATOM   5143 H  HG   . LEU   B 1 75  ? 43.409 -13.549 7.737   1.00 17.42 ?  75  LEU   B HG   1 
ATOM   5144 H  HD11 . LEU   B 1 75  ? 43.269 -14.021 5.466   1.00 19.15 ?  75  LEU   B HD11 1 
ATOM   5145 H  HD12 . LEU   B 1 75  ? 43.183 -15.361 6.316   1.00 19.15 ?  75  LEU   B HD12 1 
ATOM   5146 H  HD13 . LEU   B 1 75  ? 41.864 -14.725 5.699   1.00 19.15 ?  75  LEU   B HD13 1 
ATOM   5147 H  HD21 . LEU   B 1 75  ? 42.387 -11.988 6.284   1.00 22.21 ?  75  LEU   B HD21 1 
ATOM   5148 H  HD22 . LEU   B 1 75  ? 40.982 -12.511 6.811   1.00 22.21 ?  75  LEU   B HD22 1 
ATOM   5149 H  HD23 . LEU   B 1 75  ? 41.992 -11.800 7.810   1.00 22.21 ?  75  LEU   B HD23 1 
ATOM   5150 N  N    . LYS   B 1 76  ? 39.156 -14.662 10.005  1.00 14.51 ?  76  LYS   B N    1 
ATOM   5151 C  CA   . LYS   B 1 76  ? 38.164 -15.620 10.475  1.00 15.70 ?  76  LYS   B CA   1 
ATOM   5152 C  C    . LYS   B 1 76  ? 38.273 -16.903 9.657   1.00 14.62 ?  76  LYS   B C    1 
ATOM   5153 O  O    . LYS   B 1 76  ? 38.563 -16.862 8.463   1.00 14.38 ?  76  LYS   B O    1 
ATOM   5154 C  CB   . LYS   B 1 76  ? 36.750 -15.061 10.264  1.00 17.38 ?  76  LYS   B CB   1 
ATOM   5155 C  CG   . LYS   B 1 76  ? 36.453 -13.686 10.886  1.00 19.02 ?  76  LYS   B CG   1 
ATOM   5156 C  CD   . LYS   B 1 76  ? 35.054 -13.170 10.508  1.00 20.08 ?  76  LYS   B CD   1 
ATOM   5157 C  CE   . LYS   B 1 76  ? 34.774 -11.799 11.107  1.00 21.58 ?  76  LYS   B CE   1 
ATOM   5158 N  NZ   . LYS   B 1 76  ? 33.493 -11.204 10.637  1.00 22.31 ?  76  LYS   B NZ   1 
ATOM   5159 H  H    . LYS   B 1 76  ? 38.869 -14.150 9.374   1.00 17.43 ?  76  LYS   B H    1 
ATOM   5160 H  HA   . LYS   B 1 76  ? 38.306 -15.825 11.411  1.00 18.86 ?  76  LYS   B HA   1 
ATOM   5161 H  HB2  . LYS   B 1 76  ? 36.596 -14.985 9.310   1.00 20.88 ?  76  LYS   B HB2  1 
ATOM   5162 H  HB3  . LYS   B 1 76  ? 36.121 -15.691 10.643  1.00 20.88 ?  76  LYS   B HB3  1 
ATOM   5163 H  HG2  . LYS   B 1 76  ? 36.501 -13.757 11.852  1.00 22.85 ?  76  LYS   B HG2  1 
ATOM   5164 H  HG3  . LYS   B 1 76  ? 37.110 -13.044 10.568  1.00 22.85 ?  76  LYS   B HG3  1 
ATOM   5165 H  HD2  . LYS   B 1 76  ? 34.991 -13.099 9.542   1.00 24.12 ?  76  LYS   B HD2  1 
ATOM   5166 H  HD3  . LYS   B 1 76  ? 34.386 -13.789 10.841  1.00 24.12 ?  76  LYS   B HD3  1 
ATOM   5167 H  HE2  . LYS   B 1 76  ? 34.730 -11.882 12.071  1.00 25.92 ?  76  LYS   B HE2  1 
ATOM   5168 H  HE3  . LYS   B 1 76  ? 35.493 -11.197 10.859  1.00 25.92 ?  76  LYS   B HE3  1 
ATOM   5169 H  HZ1  . LYS   B 1 76  ? 33.373 -10.404 11.012  1.00 26.80 ?  76  LYS   B HZ1  1 
ATOM   5170 H  HZ2  . LYS   B 1 76  ? 33.508 -11.106 9.751   1.00 26.80 ?  76  LYS   B HZ2  1 
ATOM   5171 H  HZ3  . LYS   B 1 76  ? 32.811 -11.731 10.857  1.00 26.80 ?  76  LYS   B HZ3  1 
ATOM   5172 N  N    . VAL   B 1 77  ? 38.029 -18.049 10.302  1.00 15.09 ?  77  VAL   B N    1 
ATOM   5173 C  CA   . VAL   B 1 77  ? 37.817 -19.272 9.534   1.00 15.20 ?  77  VAL   B CA   1 
ATOM   5174 C  C    . VAL   B 1 77  ? 36.628 -19.047 8.612   1.00 13.99 ?  77  VAL   B C    1 
ATOM   5175 O  O    . VAL   B 1 77  ? 35.562 -18.594 9.049   1.00 14.44 ?  77  VAL   B O    1 
ATOM   5176 C  CB   . VAL   B 1 77  ? 37.606 -20.479 10.461  1.00 17.32 ?  77  VAL   B CB   1 
ATOM   5177 C  CG1  . VAL   B 1 77  ? 37.354 -21.733 9.630   1.00 17.70 ?  77  VAL   B CG1  1 
ATOM   5178 C  CG2  . VAL   B 1 77  ? 38.808 -20.667 11.386  1.00 18.48 ?  77  VAL   B CG2  1 
ATOM   5179 H  H    . VAL   B 1 77  ? 37.980 -18.139 11.150  1.00 18.13 ?  77  VAL   B H    1 
ATOM   5180 H  HA   . VAL   B 1 77  ? 38.593 -19.442 8.980   1.00 18.26 ?  77  VAL   B HA   1 
ATOM   5181 H  HB   . VAL   B 1 77  ? 36.819 -20.319 11.008  1.00 20.80 ?  77  VAL   B HB   1 
ATOM   5182 H  HG11 . VAL   B 1 77  ? 37.380 -22.504 10.216  1.00 21.26 ?  77  VAL   B HG11 1 
ATOM   5183 H  HG12 . VAL   B 1 77  ? 36.480 -21.669 9.209   1.00 21.26 ?  77  VAL   B HG12 1 
ATOM   5184 H  HG13 . VAL   B 1 77  ? 38.043 -21.805 8.953   1.00 21.26 ?  77  VAL   B HG13 1 
ATOM   5185 H  HG21 . VAL   B 1 77  ? 38.673 -21.471 11.909  1.00 22.20 ?  77  VAL   B HG21 1 
ATOM   5186 H  HG22 . VAL   B 1 77  ? 39.606 -20.750 10.844  1.00 22.20 ?  77  VAL   B HG22 1 
ATOM   5187 H  HG23 . VAL   B 1 77  ? 38.878 -19.896 11.969  1.00 22.20 ?  77  VAL   B HG23 1 
ATOM   5188 N  N    . GLY   B 1 78  ? 36.813 -19.336 7.322   1.00 13.54 ?  78  GLY   B N    1 
ATOM   5189 C  CA   . GLY   B 1 78  ? 35.841 -19.021 6.300   1.00 13.34 ?  78  GLY   B CA   1 
ATOM   5190 C  C    . GLY   B 1 78  ? 36.081 -17.708 5.590   1.00 12.77 ?  78  GLY   B C    1 
ATOM   5191 O  O    . GLY   B 1 78  ? 35.388 -17.424 4.604   1.00 13.27 ?  78  GLY   B O    1 
ATOM   5192 H  H    . GLY   B 1 78  ? 37.517 -19.724 7.013   1.00 16.27 ?  78  GLY   B H    1 
ATOM   5193 H  HA2  . GLY   B 1 78  ? 35.843 -19.721 5.633   1.00 16.03 ?  78  GLY   B HA2  1 
ATOM   5194 H  HA3  . GLY   B 1 78  ? 34.961 -18.984 6.701   1.00 16.03 ?  78  GLY   B HA3  1 
ATOM   5195 N  N    . GLY   B 1 79  ? 37.030 -16.899 6.069   1.00 12.97 ?  79  GLY   B N    1 
ATOM   5196 C  CA   . GLY   B 1 79  ? 37.329 -15.608 5.483   1.00 12.50 ?  79  GLY   B CA   1 
ATOM   5197 C  C    . GLY   B 1 79  ? 38.569 -15.638 4.599   1.00 12.10 ?  79  GLY   B C    1 
ATOM   5198 O  O    . GLY   B 1 79  ? 39.182 -16.678 4.367   1.00 12.50 ?  79  GLY   B O    1 
ATOM   5199 H  H    . GLY   B 1 79  ? 37.529 -17.082 6.746   1.00 15.59 ?  79  GLY   B H    1 
ATOM   5200 H  HA2  . GLY   B 1 79  ? 36.576 -15.312 4.943   1.00 15.02 ?  79  GLY   B HA2  1 
ATOM   5201 H  HA3  . GLY   B 1 79  ? 37.476 -14.955 6.184   1.00 15.02 ?  79  GLY   B HA3  1 
ATOM   5202 N  N    . SER   B 1 80  ? 38.934 -14.450 4.109   1.00 11.74 ?  80  SER   B N    1 
ATOM   5203 C  CA   . SER   B 1 80  ? 40.052 -14.324 3.183   1.00 11.71 ?  80  SER   B CA   1 
ATOM   5204 C  C    . SER   B 1 80  ? 40.635 -12.918 3.234   1.00 11.62 ?  80  SER   B C    1 
ATOM   5205 O  O    . SER   B 1 80  ? 40.022 -11.981 3.747   1.00 12.52 ?  80  SER   B O    1 
ATOM   5206 C  CB   . SER   B 1 80  ? 39.626 -14.624 1.743   1.00 12.21 ?  80  SER   B CB   1 
ATOM   5207 O  OG   . SER   B 1 80  ? 38.790 -13.602 1.228   1.00 12.95 ?  80  SER   B OG   1 
ATOM   5208 H  H    . SER   B 1 80  ? 38.550 -13.705 4.295   1.00 14.11 ?  80  SER   B H    1 
ATOM   5209 H  HA   . SER   B 1 80  ? 40.739 -14.956 3.437   1.00 14.08 ?  80  SER   B HA   1 
ATOM   5210 H  HB2  . SER   B 1 80  ? 40.417 -14.681 1.180   1.00 14.68 ?  80  SER   B HB2  1 
ATOM   5211 H  HB3  . SER   B 1 80  ? 39.143 -15.462 1.718   1.00 14.68 ?  80  SER   B HB3  1 
ATOM   5212 H  HG   . SER   B 1 80  ? 38.091 -13.533 1.700   1.00 15.56 ?  80  SER   B HG   1 
ATOM   5213 N  N    . CYS   B 1 81  ? 41.823 -12.778 2.650   1.00 11.43 ?  81  CYS   B N    1 
ATOM   5214 C  CA   . CYS   B 1 81  ? 42.377 -11.468 2.338   1.00 11.56 ?  81  CYS   B CA   1 
ATOM   5215 C  C    . CYS   B 1 81  ? 43.146 -11.554 1.028   1.00 10.95 ?  81  CYS   B C    1 
ATOM   5216 O  O    . CYS   B 1 81  ? 43.635 -12.621 0.645   1.00 11.80 ?  81  CYS   B O    1 
ATOM   5217 C  CB   . CYS   B 1 81  ? 43.269 -10.921 3.462   1.00 12.34 ?  81  CYS   B CB   1 
ATOM   5218 S  SG   . CYS   B 1 81  ? 44.791 -11.872 3.705   1.00 12.88 ?  81  CYS   B SG   1 
ATOM   5219 H  H    . CYS   B 1 81  ? 42.335 -13.435 2.417   1.00 13.74 ?  81  CYS   B H    1 
ATOM   5220 H  HA   . CYS   B 1 81  ? 41.648 -10.842 2.211   1.00 13.89 ?  81  CYS   B HA   1 
ATOM   5221 H  HB2  . CYS   B 1 81  ? 43.517 -10.006 3.255   1.00 14.83 ?  81  CYS   B HB2  1 
ATOM   5222 H  HB3  . CYS   B 1 81  ? 42.764 -10.938 4.297   1.00 14.83 ?  81  CYS   B HB3  1 
ATOM   5223 H  HG   . CYS   B 1 81  ? 45.414 -11.377 4.607   1.00 15.48 ?  81  CYS   B HG   1 
ATOM   5224 N  N    . VAL   B 1 82  ? 43.257 -10.410 0.354   1.00 11.24 ?  82  VAL   B N    1 
ATOM   5225 C  CA   . VAL   B 1 82  ? 44.014 -10.286 -0.888  1.00 11.32 ?  82  VAL   B CA   1 
ATOM   5226 C  C    . VAL   B 1 82  ? 45.359 -9.647  -0.579  1.00 11.66 ?  82  VAL   B C    1 
ATOM   5227 O  O    . VAL   B 1 82  ? 45.420 -8.530  -0.047  1.00 13.09 ?  82  VAL   B O    1 
ATOM   5228 C  CB   . VAL   B 1 82  ? 43.263 -9.451  -1.939  1.00 12.43 ?  82  VAL   B CB   1 
ATOM   5229 C  CG1  . VAL   B 1 82  ? 44.100 -9.334  -3.208  1.00 13.91 ?  82  VAL   B CG1  1 
ATOM   5230 C  CG2  . VAL   B 1 82  ? 41.895 -10.043 -2.237  1.00 13.84 ?  82  VAL   B CG2  1 
ATOM   5231 H  H    . VAL   B 1 82  ? 42.886 -9.667  0.602   1.00 13.51 ?  82  VAL   B H    1 
ATOM   5232 H  HA   . VAL   B 1 82  ? 44.169 -11.166 -1.255  1.00 13.61 ?  82  VAL   B HA   1 
ATOM   5233 H  HB   . VAL   B 1 82  ? 43.128 -8.557  -1.595  1.00 14.94 ?  82  VAL   B HB   1 
ATOM   5234 H  HG11 . VAL   B 1 82  ? 43.538 -9.011  -3.930  1.00 16.71 ?  82  VAL   B HG11 1 
ATOM   5235 H  HG12 . VAL   B 1 82  ? 44.827 -8.708  -3.054  1.00 16.71 ?  82  VAL   B HG12 1 
ATOM   5236 H  HG13 . VAL   B 1 82  ? 44.458 -10.207 -3.435  1.00 16.71 ?  82  VAL   B HG13 1 
ATOM   5237 H  HG21 . VAL   B 1 82  ? 41.464 -9.516  -2.931  1.00 16.63 ?  82  VAL   B HG21 1 
ATOM   5238 H  HG22 . VAL   B 1 82  ? 42.002 -10.959 -2.541  1.00 16.63 ?  82  VAL   B HG22 1 
ATOM   5239 H  HG23 . VAL   B 1 82  ? 41.358 -10.024 -1.430  1.00 16.63 ?  82  VAL   B HG23 1 
ATOM   5240 N  N    . LEU   B 1 83  ? 46.432 -10.341 -0.942  1.00 11.38 ?  83  LEU   B N    1 
ATOM   5241 C  CA   . LEU   B 1 83  ? 47.792 -9.829  -0.826  1.00 11.38 ?  83  LEU   B CA   1 
ATOM   5242 C  C    . LEU   B 1 83  ? 48.490 -9.985  -2.175  1.00 11.23 ?  83  LEU   B C    1 
ATOM   5243 O  O    . LEU   B 1 83  ? 47.883 -10.407 -3.162  1.00 11.21 ?  83  LEU   B O    1 
ATOM   5244 C  CB   . LEU   B 1 83  ? 48.544 -10.509 0.325   1.00 12.04 ?  83  LEU   B CB   1 
ATOM   5245 C  CG   . LEU   B 1 83  ? 48.047 -10.157 1.728   1.00 13.04 ?  83  LEU   B CG   1 
ATOM   5246 C  CD1  . LEU   B 1 83  ? 48.693 -11.021 2.795   1.00 13.49 ?  83  LEU   B CD1  1 
ATOM   5247 C  CD2  . LEU   B 1 83  ? 48.258 -8.671  2.031   1.00 14.00 ?  83  LEU   B CD2  1 
ATOM   5248 H  H    . LEU   B 1 83  ? 46.389 -11.140 -1.269  1.00 13.68 ?  83  LEU   B H    1 
ATOM   5249 H  HA   . LEU   B 1 83  ? 47.742 -8.883  -0.638  1.00 13.68 ?  83  LEU   B HA   1 
ATOM   5250 H  HB2  . LEU   B 1 83  ? 48.470 -11.467 0.217   1.00 14.46 ?  83  LEU   B HB2  1 
ATOM   5251 H  HB3  . LEU   B 1 83  ? 49.477 -10.246 0.267   1.00 14.46 ?  83  LEU   B HB3  1 
ATOM   5252 H  HG   . LEU   B 1 83  ? 47.096 -10.322 1.758   1.00 15.66 ?  83  LEU   B HG   1 
ATOM   5253 H  HD11 . LEU   B 1 83  ? 48.341 -10.767 3.663   1.00 16.21 ?  83  LEU   B HD11 1 
ATOM   5254 H  HD12 . LEU   B 1 83  ? 48.478 -11.954 2.616   1.00 16.21 ?  83  LEU   B HD12 1 
ATOM   5255 H  HD13 . LEU   B 1 83  ? 49.652 -10.895 2.775   1.00 16.21 ?  83  LEU   B HD13 1 
ATOM   5256 H  HD21 . LEU   B 1 83  ? 48.078 -8.515  2.971   1.00 16.83 ?  83  LEU   B HD21 1 
ATOM   5257 H  HD22 . LEU   B 1 83  ? 49.174 -8.431  1.825   1.00 16.83 ?  83  LEU   B HD22 1 
ATOM   5258 H  HD23 . LEU   B 1 83  ? 47.648 -8.148  1.487   1.00 16.83 ?  83  LEU   B HD23 1 
ATOM   5259 N  N    . SER   B 1 84  ? 49.770 -9.620  -2.230  1.00 12.01 ?  84  SER   B N    1 
ATOM   5260 C  CA   . SER   B 1 84  ? 50.505 -9.748  -3.481  1.00 12.54 ?  84  SER   B CA   1 
ATOM   5261 C  C    . SER   B 1 84  ? 50.667 -11.215 -3.873  1.00 11.43 ?  84  SER   B C    1 
ATOM   5262 O  O    . SER   B 1 84  ? 50.774 -12.101 -3.026  1.00 11.57 ?  84  SER   B O    1 
ATOM   5263 C  CB   . SER   B 1 84  ? 51.896 -9.131  -3.347  1.00 14.30 ?  84  SER   B CB   1 
ATOM   5264 O  OG   . SER   B 1 84  ? 52.633 -9.360  -4.536  1.00 15.36 ?  84  SER   B OG   1 
ATOM   5265 H  H    . SER   B 1 84  ? 50.213 -9.290  -1.576  1.00 14.43 ?  84  SER   B H    1 
ATOM   5266 H  HA   . SER   B 1 84  ? 50.031 -9.287  -4.190  1.00 15.07 ?  84  SER   B HA   1 
ATOM   5267 H  HB2  . SER   B 1 84  ? 51.807 -8.171  -3.197  1.00 17.18 ?  84  SER   B HB2  1 
ATOM   5268 H  HB3  . SER   B 1 84  ? 52.358 -9.538  -2.596  1.00 17.18 ?  84  SER   B HB3  1 
ATOM   5269 H  HG   . SER   B 1 84  ? 53.402 -9.011  -4.463  1.00 18.45 ?  84  SER   B HG   1 
ATOM   5270 N  N    . GLY   B 1 85  ? 50.725 -11.456 -5.179  1.00 12.17 ?  85  GLY   B N    1 
ATOM   5271 C  CA   . GLY   B 1 85  ? 51.078 -12.760 -5.687  1.00 13.14 ?  85  GLY   B CA   1 
ATOM   5272 C  C    . GLY   B 1 85  ? 52.550 -12.945 -5.998  1.00 12.77 ?  85  GLY   B C    1 
ATOM   5273 O  O    . GLY   B 1 85  ? 52.927 -14.026 -6.456  1.00 13.02 ?  85  GLY   B O    1 
ATOM   5274 H  H    . GLY   B 1 85  ? 50.574 -10.875 -5.792  1.00 14.63 ?  85  GLY   B H    1 
ATOM   5275 H  HA2  . GLY   B 1 85  ? 50.823 -13.434 -5.035  1.00 15.79 ?  85  GLY   B HA2  1 
ATOM   5276 H  HA3  . GLY   B 1 85  ? 50.583 -12.929 -6.500  1.00 15.79 ?  85  GLY   B HA3  1 
ATOM   5277 N  N    . HIS   B 1 86  ? 53.399 -11.938 -5.785  1.00 12.88 ?  86  HIS   B N    1 
ATOM   5278 C  CA   . HIS   B 1 86  ? 54.864 -12.102 -5.875  1.00 12.51 ?  86  HIS   B CA   1 
ATOM   5279 C  C    . HIS   B 1 86  ? 55.233 -12.626 -7.262  1.00 12.57 ?  86  HIS   B C    1 
ATOM   5280 O  O    . HIS   B 1 86  ? 54.836 -12.021 -8.270  1.00 13.58 ?  86  HIS   B O    1 
ATOM   5281 C  CB   . HIS   B 1 86  ? 55.362 -12.930 -4.690  1.00 13.04 ?  86  HIS   B CB   1 
ATOM   5282 C  CG   . HIS   B 1 86  ? 55.040 -12.315 -3.369  1.00 13.23 ?  86  HIS   B CG   1 
ATOM   5283 N  ND1  . HIS   B 1 86  ? 55.878 -11.418 -2.745  1.00 14.85 ?  86  HIS   B ND1  1 
ATOM   5284 C  CD2  . HIS   B 1 86  ? 53.953 -12.437 -2.570  1.00 13.30 ?  86  HIS   B CD2  1 
ATOM   5285 C  CE1  . HIS   B 1 86  ? 55.318 -11.012 -1.619  1.00 14.34 ?  86  HIS   B CE1  1 
ATOM   5286 N  NE2  . HIS   B 1 86  ? 54.145 -11.608 -1.494  1.00 13.76 ?  86  HIS   B NE2  1 
ATOM   5287 H  H    . HIS   B 1 86  ? 53.156 -11.136 -5.584  1.00 15.48 ?  86  HIS   B H    1 
ATOM   5288 H  HA   . HIS   B 1 86  ? 55.271 -11.229 -5.786  1.00 15.03 ?  86  HIS   B HA   1 
ATOM   5289 H  HB2  . HIS   B 1 86  ? 54.954 -13.809 -4.717  1.00 15.67 ?  86  HIS   B HB2  1 
ATOM   5290 H  HB3  . HIS   B 1 86  ? 56.331 -13.018 -4.748  1.00 15.67 ?  86  HIS   B HB3  1 
ATOM   5291 H  HD2  . HIS   B 1 86  ? 53.205 -12.960 -2.736  1.00 15.98 ?  86  HIS   B HD2  1 
ATOM   5292 H  HE1  . HIS   B 1 86  ? 55.698 -10.419 -1.007  1.00 17.23 ?  86  HIS   B HE1  1 
ATOM   5293 H  HE2  . HIS   B 1 86  ? 53.607 -11.514 -0.831  1.00 16.53 ?  86  HIS   B HE2  1 
ATOM   5294 N  N    . ASN   B 1 87  ? 56.001 -13.710 -7.368  1.00 12.89 ?  87  ASN   B N    1 
ATOM   5295 C  CA   . ASN   B 1 87  ? 56.397 -14.289 -8.644  1.00 14.31 ?  87  ASN   B CA   1 
ATOM   5296 C  C    . ASN   B 1 87  ? 55.414 -15.330 -9.148  1.00 13.75 ?  87  ASN   B C    1 
ATOM   5297 O  O    . ASN   B 1 87  ? 55.722 -16.031 -10.119 1.00 15.75 ?  87  ASN   B O    1 
ATOM   5298 C  CB   . ASN   B 1 87  ? 57.786 -14.927 -8.523  1.00 16.21 ?  87  ASN   B CB   1 
ATOM   5299 C  CG   . ASN   B 1 87  ? 57.834 -16.039 -7.478  1.00 16.73 ?  87  ASN   B CG   1 
ATOM   5300 O  OD1  . ASN   B 1 87  ? 57.206 -15.944 -6.418  1.00 16.09 ?  87  ASN   B OD1  1 
ATOM   5301 N  ND2  . ASN   B 1 87  ? 58.574 -17.113 -7.784  1.00 19.09 ?  87  ASN   B ND2  1 
ATOM   5302 H  H    . ASN   B 1 87  ? 56.305 -14.148 -6.690  1.00 15.48 ?  87  ASN   B H    1 
ATOM   5303 H  HA   . ASN   B 1 87  ? 56.447 -13.588 -9.302  1.00 17.20 ?  87  ASN   B HA   1 
ATOM   5304 H  HB2  . ASN   B 1 87  ? 58.037 -15.309 -9.382  1.00 19.47 ?  87  ASN   B HB2  1 
ATOM   5305 H  HB3  . ASN   B 1 87  ? 58.426 -14.246 -8.266  1.00 19.47 ?  87  ASN   B HB3  1 
ATOM   5306 H  HD21 . ASN   B 1 87  ? 58.640 -17.765 -7.229  1.00 22.93 ?  87  ASN   B HD21 1 
ATOM   5307 H  HD22 . ASN   B 1 87  ? 59.002 -17.147 -8.535  1.00 22.93 ?  87  ASN   B HD22 1 
ATOM   5308 N  N    . LEU   B 1 88  ? 54.240 -15.431 -8.524  1.00 12.64 ?  88  LEU   B N    1 
ATOM   5309 C  CA   . LEU   B 1 88  ? 53.253 -16.454 -8.845  1.00 13.33 ?  88  LEU   B CA   1 
ATOM   5310 C  C    . LEU   B 1 88  ? 52.024 -15.933 -9.568  1.00 13.02 ?  88  LEU   B C    1 
ATOM   5311 O  O    . LEU   B 1 88  ? 51.420 -16.678 -10.350 1.00 14.70 ?  88  LEU   B O    1 
ATOM   5312 C  CB   . LEU   B 1 88  ? 52.770 -17.123 -7.555  1.00 14.62 ?  88  LEU   B CB   1 
ATOM   5313 C  CG   . LEU   B 1 88  ? 53.893 -17.788 -6.771  1.00 16.41 ?  88  LEU   B CG   1 
ATOM   5314 C  CD1  . LEU   B 1 88  ? 53.407 -18.193 -5.395  1.00 17.72 ?  88  LEU   B CD1  1 
ATOM   5315 C  CD2  . LEU   B 1 88  ? 54.396 -18.986 -7.545  1.00 20.12 ?  88  LEU   B CD2  1 
ATOM   5316 H  H    . LEU   B 1 88  ? 53.987 -14.906 -7.882  1.00 15.19 ?  88  LEU   B H    1 
ATOM   5317 H  HA   . LEU   B 1 88  ? 53.659 -17.128 -9.399  1.00 16.02 ?  88  LEU   B HA   1 
ATOM   5318 H  HB2  . LEU   B 1 88  ? 52.359 -16.453 -6.981  1.00 17.56 ?  88  LEU   B HB2  1 
ATOM   5319 H  HB3  . LEU   B 1 88  ? 52.112 -17.805 -7.778  1.00 17.56 ?  88  LEU   B HB3  1 
ATOM   5320 H  HG   . LEU   B 1 88  ? 54.624 -17.160 -6.668  1.00 19.72 ?  88  LEU   B HG   1 
ATOM   5321 H  HD11 . LEU   B 1 88  ? 54.086 -18.740 -4.972  1.00 21.28 ?  88  LEU   B HD11 1 
ATOM   5322 H  HD12 . LEU   B 1 88  ? 53.247 -17.395 -4.870  1.00 21.28 ?  88  LEU   B HD12 1 
ATOM   5323 H  HD13 . LEU   B 1 88  ? 52.585 -18.698 -5.492  1.00 21.28 ?  88  LEU   B HD13 1 
ATOM   5324 H  HD21 . LEU   B 1 88  ? 54.992 -19.496 -6.978  1.00 24.17 ?  88  LEU   B HD21 1 
ATOM   5325 H  HD22 . LEU   B 1 88  ? 53.639 -19.533 -7.808  1.00 24.17 ?  88  LEU   B HD22 1 
ATOM   5326 H  HD23 . LEU   B 1 88  ? 54.870 -18.679 -8.334  1.00 24.17 ?  88  LEU   B HD23 1 
ATOM   5327 N  N    . ALA   B 1 89  ? 51.621 -14.696 -9.301  1.00 12.27 ?  89  ALA   B N    1 
ATOM   5328 C  CA   . ALA   B 1 89  ? 50.333 -14.193 -9.752  1.00 11.74 ?  89  ALA   B CA   1 
ATOM   5329 C  C    . ALA   B 1 89  ? 50.315 -12.703 -9.460  1.00 11.99 ?  89  ALA   B C    1 
ATOM   5330 O  O    . ALA   B 1 89  ? 51.150 -12.196 -8.711  1.00 12.62 ?  89  ALA   B O    1 
ATOM   5331 C  CB   . ALA   B 1 89  ? 49.201 -14.877 -8.996  1.00 11.98 ?  89  ALA   B CB   1 
ATOM   5332 H  H    . ALA   B 1 89  ? 52.082 -14.116 -8.862  1.00 14.75 ?  89  ALA   B H    1 
ATOM   5333 H  HA   . ALA   B 1 89  ? 50.223 -14.337 -10.712 1.00 14.11 ?  89  ALA   B HA   1 
ATOM   5334 H  HB1  . ALA   B 1 89  ? 48.353 -14.540 -9.327  1.00 14.40 ?  89  ALA   B HB1  1 
ATOM   5335 H  HB2  . ALA   B 1 89  ? 49.257 -15.835 -9.152  1.00 14.40 ?  89  ALA   B HB2  1 
ATOM   5336 H  HB3  . ALA   B 1 89  ? 49.295 -14.686 -8.056  1.00 14.40 ?  89  ALA   B HB3  1 
ATOM   5337 N  N    . LYS   B 1 90  ? 49.341 -11.998 -10.031 1.00 12.73 ?  90  LYS   B N    1 
ATOM   5338 C  CA   . LYS   B 1 90  ? 49.169 -10.607 -9.626  1.00 13.00 ?  90  LYS   B CA   1 
ATOM   5339 C  C    . LYS   B 1 90  ? 48.837 -10.527 -8.139  1.00 12.18 ?  90  LYS   B C    1 
ATOM   5340 O  O    . LYS   B 1 90  ? 49.483 -9.785  -7.384  1.00 12.85 ?  90  LYS   B O    1 
ATOM   5341 C  CB   . LYS   B 1 90  ? 48.104 -9.935  -10.490 1.00 14.52 ?  90  LYS   B CB   1 
ATOM   5342 C  CG   . LYS   B 1 90  ? 47.778 -8.508  -10.079 1.00 14.68 ?  90  LYS   B CG   1 
ATOM   5343 C  CD   . LYS   B 1 90  ? 48.966 -7.587  -10.149 1.00 16.72 ?  90  LYS   B CD   1 
ATOM   5344 C  CE   . LYS   B 1 90  ? 48.498 -6.189  -9.822  1.00 19.00 ?  90  LYS   B CE   1 
ATOM   5345 N  NZ   . LYS   B 1 90  ? 49.624 -5.233  -9.756  1.00 18.14 ?  90  LYS   B NZ   1 
ATOM   5346 H  H    . LYS   B 1 90  ? 48.793 -12.287 -10.627 1.00 15.30 ?  90  LYS   B H    1 
ATOM   5347 H  HA   . LYS   B 1 90  ? 50.002 -10.137 -9.770  1.00 15.62 ?  90  LYS   B HA   1 
ATOM   5348 H  HB2  . LYS   B 1 90  ? 48.415 -9.910  -11.411 1.00 17.44 ?  90  LYS   B HB2  1 
ATOM   5349 H  HB3  . LYS   B 1 90  ? 47.285 -10.452 -10.440 1.00 17.44 ?  90  LYS   B HB3  1 
ATOM   5350 H  HG2  . LYS   B 1 90  ? 47.095 -8.158  -10.675 1.00 17.64 ?  90  LYS   B HG2  1 
ATOM   5351 H  HG3  . LYS   B 1 90  ? 47.444 -8.505  -9.166  1.00 17.64 ?  90  LYS   B HG3  1 
ATOM   5352 H  HD2  . LYS   B 1 90  ? 49.633 -7.852  -9.495  1.00 20.09 ?  90  LYS   B HD2  1 
ATOM   5353 H  HD3  . LYS   B 1 90  ? 49.340 -7.591  -11.044 1.00 20.09 ?  90  LYS   B HD3  1 
ATOM   5354 H  HE2  . LYS   B 1 90  ? 47.887 -5.880  -10.512 1.00 22.82 ?  90  LYS   B HE2  1 
ATOM   5355 H  HE3  . LYS   B 1 90  ? 48.056 -6.185  -8.959  1.00 22.82 ?  90  LYS   B HE3  1 
ATOM   5356 H  HZ1  . LYS   B 1 90  ? 49.328 -4.414  -9.566  1.00 21.79 ?  90  LYS   B HZ1  1 
ATOM   5357 H  HZ2  . LYS   B 1 90  ? 50.203 -5.482  -9.128  1.00 21.79 ?  90  LYS   B HZ2  1 
ATOM   5358 H  HZ3  . LYS   B 1 90  ? 50.050 -5.204  -10.541 1.00 21.79 ?  90  LYS   B HZ3  1 
ATOM   5359 N  N    . HIS   B 1 91  ? 47.860 -11.327 -7.696  1.00 10.89 ?  91  HIS   B N    1 
ATOM   5360 C  CA   . HIS   B 1 91  ? 47.398 -11.358 -6.323  1.00 11.45 ?  91  HIS   B CA   1 
ATOM   5361 C  C    . HIS   B 1 91  ? 47.383 -12.786 -5.805  1.00 10.52 ?  91  HIS   B C    1 
ATOM   5362 O  O    . HIS   B 1 91  ? 47.149 -13.734 -6.564  1.00 11.30 ?  91  HIS   B O    1 
ATOM   5363 C  CB   . HIS   B 1 91  ? 45.946 -10.868 -6.215  1.00 13.00 ?  91  HIS   B CB   1 
ATOM   5364 C  CG   . HIS   B 1 91  ? 45.753 -9.447  -6.617  1.00 16.13 ?  91  HIS   B CG   1 
ATOM   5365 N  ND1  . HIS   B 1 91  ? 46.386 -8.395  -5.988  1.00 18.36 ?  91  HIS   B ND1  1 
ATOM   5366 C  CD2  . HIS   B 1 91  ? 44.963 -8.898  -7.565  1.00 18.50 ?  91  HIS   B CD2  1 
ATOM   5367 C  CE1  . HIS   B 1 91  ? 46.008 -7.258  -6.545  1.00 19.55 ?  91  HIS   B CE1  1 
ATOM   5368 N  NE2  . HIS   B 1 91  ? 45.146 -7.536  -7.507  1.00 19.90 ?  91  HIS   B NE2  1 
ATOM   5369 H  H    . HIS   B 1 91  ? 47.429 -11.872 -8.205  1.00 13.09 ?  91  HIS   B H    1 
ATOM   5370 H  HA   . HIS   B 1 91  ? 47.971 -10.805 -5.758  1.00 13.77 ?  91  HIS   B HA   1 
ATOM   5371 H  HB2  . HIS   B 1 91  ? 45.387 -11.414 -6.790  1.00 15.62 ?  91  HIS   B HB2  1 
ATOM   5372 H  HB3  . HIS   B 1 91  ? 45.650 -10.958 -5.293  1.00 15.62 ?  91  HIS   B HB3  1 
ATOM   5373 H  HD2  . HIS   B 1 91  ? 44.411 -9.346  -8.160  1.00 22.22 ?  91  HIS   B HD2  1 
ATOM   5374 H  HE1  . HIS   B 1 91  ? 46.299 -6.406  -6.297  1.00 23.49 ?  91  HIS   B HE1  1 
ATOM   5375 H  HE2  . HIS   B 1 91  ? 44.765 -6.950  -8.012  1.00 23.90 ?  91  HIS   B HE2  1 
ATOM   5376 N  N    . CYS   B 1 92  ? 47.566 -12.922 -4.499  1.00 10.38 ?  92  CYS   B N    1 
ATOM   5377 C  CA   . CYS   B 1 92  ? 47.254 -14.156 -3.789  1.00 10.50 ?  92  CYS   B CA   1 
ATOM   5378 C  C    . CYS   B 1 92  ? 46.034 -13.910 -2.912  1.00 9.94  ?  92  CYS   B C    1 
ATOM   5379 O  O    . CYS   B 1 92  ? 46.046 -13.005 -2.064  1.00 11.06 ?  92  CYS   B O    1 
ATOM   5380 C  CB   . CYS   B 1 92  ? 48.422 -14.607 -2.920  1.00 10.85 ?  92  CYS   B CB   1 
ATOM   5381 S  SG   . CYS   B 1 92  ? 48.066 -16.151 -2.026  1.00 10.97 ?  92  CYS   B SG   1 
ATOM   5382 H  H    . CYS   B 1 92  ? 47.888 -12.303 -3.987  1.00 12.47 ?  92  CYS   B H    1 
ATOM   5383 H  HA   . CYS   B 1 92  ? 47.053 -14.856 -4.431  1.00 12.62 ?  92  CYS   B HA   1 
ATOM   5384 H  HB2  . CYS   B 1 92  ? 49.195 -14.751 -3.477  1.00 13.04 ?  92  CYS   B HB2  1 
ATOM   5385 H  HB3  . CYS   B 1 92  ? 48.603 -13.916 -2.262  1.00 13.04 ?  92  CYS   B HB3  1 
ATOM   5386 H  HG   . CYS   B 1 92  ? 49.042 -16.455 -1.395  1.00 13.19 ?  92  CYS   B HG   1 
ATOM   5387 N  N    . LEU   B 1 93  ? 44.993 -14.715 -3.123  1.00 10.03 ?  93  LEU   B N    1 
ATOM   5388 C  CA   . LEU   B 1 93  ? 43.820 -14.725 -2.264  1.00 10.51 ?  93  LEU   B CA   1 
ATOM   5389 C  C    . LEU   B 1 93  ? 44.044 -15.785 -1.191  1.00 9.95  ?  93  LEU   B C    1 
ATOM   5390 O  O    . LEU   B 1 93  ? 43.999 -16.988 -1.477  1.00 10.68 ?  93  LEU   B O    1 
ATOM   5391 C  CB   . LEU   B 1 93  ? 42.556 -15.002 -3.070  1.00 10.98 ?  93  LEU   B CB   1 
ATOM   5392 C  CG   . LEU   B 1 93  ? 41.263 -15.015 -2.256  1.00 11.57 ?  93  LEU   B CG   1 
ATOM   5393 C  CD1  . LEU   B 1 93  ? 40.905 -13.621 -1.781  1.00 12.05 ?  93  LEU   B CD1  1 
ATOM   5394 C  CD2  . LEU   B 1 93  ? 40.132 -15.623 -3.078  1.00 11.59 ?  93  LEU   B CD2  1 
ATOM   5395 H  H    . LEU   B 1 93  ? 44.948 -15.282 -3.774  1.00 12.06 ?  93  LEU   B H    1 
ATOM   5396 H  HA   . LEU   B 1 93  ? 43.728 -13.862 -1.834  1.00 12.63 ?  93  LEU   B HA   1 
ATOM   5397 H  HB2  . LEU   B 1 93  ? 42.462 -14.307 -3.747  1.00 13.20 ?  93  LEU   B HB2  1 
ATOM   5398 H  HB3  . LEU   B 1 93  ? 42.639 -15.863 -3.499  1.00 13.20 ?  93  LEU   B HB3  1 
ATOM   5399 H  HG   . LEU   B 1 93  ? 41.389 -15.569 -1.472  1.00 13.91 ?  93  LEU   B HG   1 
ATOM   5400 H  HD11 . LEU   B 1 93  ? 40.054 -13.656 -1.319  1.00 14.48 ?  93  LEU   B HD11 1 
ATOM   5401 H  HD12 . LEU   B 1 93  ? 41.596 -13.301 -1.188  1.00 14.48 ?  93  LEU   B HD12 1 
ATOM   5402 H  HD13 . LEU   B 1 93  ? 40.833 -13.036 -2.557  1.00 14.48 ?  93  LEU   B HD13 1 
ATOM   5403 H  HD21 . LEU   B 1 93  ? 39.318 -15.615 -2.552  1.00 13.93 ?  93  LEU   B HD21 1 
ATOM   5404 H  HD22 . LEU   B 1 93  ? 40.010 -15.101 -3.886  1.00 13.93 ?  93  LEU   B HD22 1 
ATOM   5405 H  HD23 . LEU   B 1 93  ? 40.367 -16.538 -3.309  1.00 13.93 ?  93  LEU   B HD23 1 
ATOM   5406 N  N    . HIS   B 1 94  ? 44.318 -15.345 0.029   1.00 9.99  ?  94  HIS   B N    1 
ATOM   5407 C  CA   . HIS   B 1 94  ? 44.536 -16.249 1.152   1.00 10.21 ?  94  HIS   B CA   1 
ATOM   5408 C  C    . HIS   B 1 94  ? 43.175 -16.601 1.732   1.00 10.68 ?  94  HIS   B C    1 
ATOM   5409 O  O    . HIS   B 1 94  ? 42.507 -15.732 2.292   1.00 11.87 ?  94  HIS   B O    1 
ATOM   5410 C  CB   . HIS   B 1 94  ? 45.411 -15.580 2.209   1.00 10.66 ?  94  HIS   B CB   1 
ATOM   5411 C  CG   . HIS   B 1 94  ? 46.793 -15.280 1.735   1.00 10.74 ?  94  HIS   B CG   1 
ATOM   5412 N  ND1  . HIS   B 1 94  ? 47.821 -16.196 1.814   1.00 10.66 ?  94  HIS   B ND1  1 
ATOM   5413 C  CD2  . HIS   B 1 94  ? 47.300 -14.172 1.138   1.00 10.83 ?  94  HIS   B CD2  1 
ATOM   5414 C  CE1  . HIS   B 1 94  ? 48.910 -15.642 1.307   1.00 10.96 ?  94  HIS   B CE1  1 
ATOM   5415 N  NE2  . HIS   B 1 94  ? 48.622 -14.419 0.886   1.00 11.03 ?  94  HIS   B NE2  1 
ATOM   5416 H  H    . HIS   B 1 94  ? 44.393 -14.508 0.233   1.00 12.01 ?  94  HIS   B H    1 
ATOM   5417 H  HA   . HIS   B 1 94  ? 44.966 -17.057 0.841   1.00 12.28 ?  94  HIS   B HA   1 
ATOM   5418 H  HB2  . HIS   B 1 94  ? 45.001 -14.744 2.470   1.00 12.81 ?  94  HIS   B HB2  1 
ATOM   5419 H  HB3  . HIS   B 1 94  ? 45.482 -16.173 2.969   1.00 12.81 ?  94  HIS   B HB3  1 
ATOM   5420 H  HD2  . HIS   B 1 94  ? 46.843 -13.389 0.948   1.00 13.02 ?  94  HIS   B HD2  1 
ATOM   5421 H  HE1  . HIS   B 1 94  ? 49.740 -16.062 1.241   1.00 13.17 ?  94  HIS   B HE1  1 
ATOM   5422 H  HE2  . HIS   B 1 94  ? 49.178 -13.879 0.520   1.00 13.25 ?  94  HIS   B HE2  1 
ATOM   5423 N  N    . VAL   B 1 95  ? 42.739 -17.853 1.580   1.00 10.40 ?  95  VAL   B N    1 
ATOM   5424 C  CA   . VAL   B 1 95  ? 41.408 -18.287 2.014   1.00 10.60 ?  95  VAL   B CA   1 
ATOM   5425 C  C    . VAL   B 1 95  ? 41.568 -19.321 3.115   1.00 11.03 ?  95  VAL   B C    1 
ATOM   5426 O  O    . VAL   B 1 95  ? 42.343 -20.271 2.962   1.00 11.40 ?  95  VAL   B O    1 
ATOM   5427 C  CB   . VAL   B 1 95  ? 40.592 -18.896 0.860   1.00 11.05 ?  95  VAL   B CB   1 
ATOM   5428 C  CG1  . VAL   B 1 95  ? 39.212 -19.338 1.349   1.00 12.79 ?  95  VAL   B CG1  1 
ATOM   5429 C  CG2  . VAL   B 1 95  ? 40.473 -17.907 -0.280  1.00 11.02 ?  95  VAL   B CG2  1 
ATOM   5430 H  H    . VAL   B 1 95  ? 43.205 -18.481 1.219   1.00 12.50 ?  95  VAL   B H    1 
ATOM   5431 H  HA   . VAL   B 1 95  ? 40.921 -17.531 2.372   1.00 12.74 ?  95  VAL   B HA   1 
ATOM   5432 H  HB   . VAL   B 1 95  ? 41.053 -19.673 0.523   1.00 13.29 ?  95  VAL   B HB   1 
ATOM   5433 H  HG11 . VAL   B 1 95  ? 38.646 -19.519 0.579   1.00 15.37 ?  95  VAL   B HG11 1 
ATOM   5434 H  HG12 . VAL   B 1 95  ? 39.304 -20.141 1.882   1.00 15.37 ?  95  VAL   B HG12 1 
ATOM   5435 H  HG13 . VAL   B 1 95  ? 38.817 -18.627 1.881   1.00 15.37 ?  95  VAL   B HG13 1 
ATOM   5436 H  HG21 . VAL   B 1 95  ? 39.897 -18.286 -0.960  1.00 13.24 ?  95  VAL   B HG21 1 
ATOM   5437 H  HG22 . VAL   B 1 95  ? 40.089 -17.083 0.060   1.00 13.24 ?  95  VAL   B HG22 1 
ATOM   5438 H  HG23 . VAL   B 1 95  ? 41.355 -17.741 -0.641  1.00 13.24 ?  95  VAL   B HG23 1 
ATOM   5439 N  N    . VAL   B 1 96  ? 40.837 -19.144 4.209   1.00 11.46 ?  96  VAL   B N    1 
ATOM   5440 C  CA   . VAL   B 1 96  ? 40.921 -20.048 5.355   1.00 11.95 ?  96  VAL   B CA   1 
ATOM   5441 C  C    . VAL   B 1 96  ? 39.733 -21.005 5.313   1.00 12.66 ?  96  VAL   B C    1 
ATOM   5442 O  O    . VAL   B 1 96  ? 38.615 -20.651 5.699   1.00 13.36 ?  96  VAL   B O    1 
ATOM   5443 C  CB   . VAL   B 1 96  ? 40.976 -19.295 6.685   1.00 12.95 ?  96  VAL   B CB   1 
ATOM   5444 C  CG1  . VAL   B 1 96  ? 41.119 -20.283 7.835   1.00 13.34 ?  96  VAL   B CG1  1 
ATOM   5445 C  CG2  . VAL   B 1 96  ? 42.114 -18.280 6.697   1.00 12.99 ?  96  VAL   B CG2  1 
ATOM   5446 H  H    . VAL   B 1 96  ? 40.276 -18.502 4.315   1.00 13.77 ?  96  VAL   B H    1 
ATOM   5447 H  HA   . VAL   B 1 96  ? 41.734 -20.575 5.281   1.00 14.37 ?  96  VAL   B HA   1 
ATOM   5448 H  HB   . VAL   B 1 96  ? 40.145 -18.812 6.808   1.00 15.56 ?  96  VAL   B HB   1 
ATOM   5449 H  HG11 . VAL   B 1 96  ? 41.329 -19.797 8.649   1.00 16.03 ?  96  VAL   B HG11 1 
ATOM   5450 H  HG12 . VAL   B 1 96  ? 40.282 -20.765 7.950   1.00 16.03 ?  96  VAL   B HG12 1 
ATOM   5451 H  HG13 . VAL   B 1 96  ? 41.833 -20.909 7.633   1.00 16.03 ?  96  VAL   B HG13 1 
ATOM   5452 H  HG21 . VAL   B 1 96  ? 42.155 -17.859 7.570   1.00 15.61 ?  96  VAL   B HG21 1 
ATOM   5453 H  HG22 . VAL   B 1 96  ? 42.948 -18.735 6.509   1.00 15.61 ?  96  VAL   B HG22 1 
ATOM   5454 H  HG23 . VAL   B 1 96  ? 41.944 -17.607 6.016   1.00 15.61 ?  96  VAL   B HG23 1 
ATOM   5455 N  N    . GLY   B 1 97  ? 39.967 -22.232 4.864   1.00 12.47 ?  97  GLY   B N    1 
ATOM   5456 C  CA   . GLY   B 1 97  ? 38.999 -23.292 5.033   1.00 13.31 ?  97  GLY   B CA   1 
ATOM   5457 C  C    . GLY   B 1 97  ? 39.135 -23.894 6.414   1.00 14.83 ?  97  GLY   B C    1 
ATOM   5458 O  O    . GLY   B 1 97  ? 40.181 -23.770 7.062   1.00 15.06 ?  97  GLY   B O    1 
ATOM   5459 H  H    . GLY   B 1 97  ? 40.689 -22.469 4.450   1.00 14.98 ?  97  GLY   B H    1 
ATOM   5460 H  HA2  . GLY   B 1 97  ? 38.104 -22.930 4.918   1.00 15.99 ?  97  GLY   B HA2  1 
ATOM   5461 H  HA3  . GLY   B 1 97  ? 39.145 -23.981 4.367   1.00 15.99 ?  97  GLY   B HA3  1 
ATOM   5462 N  N    . PRO   B 1 98  ? 38.088 -24.565 6.892   1.00 16.06 ?  98  PRO   B N    1 
ATOM   5463 C  CA   . PRO   B 1 98  ? 38.192 -25.256 8.181   1.00 17.41 ?  98  PRO   B CA   1 
ATOM   5464 C  C    . PRO   B 1 98  ? 39.214 -26.385 8.134   1.00 17.16 ?  98  PRO   B C    1 
ATOM   5465 O  O    . PRO   B 1 98  ? 39.314 -27.123 7.154   1.00 17.07 ?  98  PRO   B O    1 
ATOM   5466 C  CB   . PRO   B 1 98  ? 36.772 -25.788 8.412   1.00 18.01 ?  98  PRO   B CB   1 
ATOM   5467 C  CG   . PRO   B 1 98  ? 36.187 -25.914 7.055   1.00 17.55 ?  98  PRO   B CG   1 
ATOM   5468 C  CD   . PRO   B 1 98  ? 36.767 -24.766 6.267   1.00 16.48 ?  98  PRO   B CD   1 
ATOM   5469 H  HA   . PRO   B 1 98  ? 38.426 -24.631 8.882   1.00 20.92 ?  98  PRO   B HA   1 
ATOM   5470 H  HB2  . PRO   B 1 98  ? 36.817 -26.656 8.848   1.00 21.64 ?  98  PRO   B HB2  1 
ATOM   5471 H  HB3  . PRO   B 1 98  ? 36.269 -25.159 8.947   1.00 21.64 ?  98  PRO   B HB3  1 
ATOM   5472 H  HG2  . PRO   B 1 98  ? 36.450 -26.764 6.665   1.00 21.08 ?  98  PRO   B HG2  1 
ATOM   5473 H  HG3  . PRO   B 1 98  ? 35.224 -25.844 7.108   1.00 21.08 ?  98  PRO   B HG3  1 
ATOM   5474 H  HD2  . PRO   B 1 98  ? 36.860 -25.013 5.329   1.00 19.80 ?  98  PRO   B HD2  1 
ATOM   5475 H  HD3  . PRO   B 1 98  ? 36.218 -23.973 6.369   1.00 19.80 ?  98  PRO   B HD3  1 
ATOM   5476 N  N    . ASN   B 1 99  ? 39.968 -26.522 9.220   1.00 18.25 ?  99  ASN   B N    1 
ATOM   5477 C  CA   . ASN   B 1 99  ? 40.955 -27.591 9.376   1.00 19.20 ?  99  ASN   B CA   1 
ATOM   5478 C  C    . ASN   B 1 99  ? 40.344 -28.663 10.272  1.00 21.38 ?  99  ASN   B C    1 
ATOM   5479 O  O    . ASN   B 1 99  ? 40.314 -28.515 11.496  1.00 22.84 ?  99  ASN   B O    1 
ATOM   5480 C  CB   . ASN   B 1 99  ? 42.234 -27.026 9.980   1.00 19.53 ?  99  ASN   B CB   1 
ATOM   5481 C  CG   . ASN   B 1 99  ? 43.373 -28.027 9.978   1.00 19.87 ?  99  ASN   B CG   1 
ATOM   5482 O  OD1  . ASN   B 1 99  ? 43.167 -29.213 10.197  1.00 20.69 ?  99  ASN   B OD1  1 
ATOM   5483 N  ND2  . ASN   B 1 99  ? 44.577 -27.551 9.727   1.00 20.29 ?  99  ASN   B ND2  1 
ATOM   5484 H  H    . ASN   B 1 99  ? 39.917 -25.998 9.899   1.00 21.92 ?  99  ASN   B H    1 
ATOM   5485 H  HA   . ASN   B 1 99  ? 41.147 -27.988 8.516   1.00 23.06 ?  99  ASN   B HA   1 
ATOM   5486 H  HB2  . ASN   B 1 99  ? 42.498 -26.257 9.469   1.00 23.46 ?  99  ASN   B HB2  1 
ATOM   5487 H  HB3  . ASN   B 1 99  ? 42.053 -26.778 10.902  1.00 23.46 ?  99  ASN   B HB3  1 
ATOM   5488 H  HD21 . ASN   B 1 99  ? 45.251 -28.077 9.709   1.00 24.37 ?  99  ASN   B HD21 1 
ATOM   5489 H  HD22 . ASN   B 1 99  ? 44.675 -26.709 9.581   1.00 24.37 ?  99  ASN   B HD22 1 
ATOM   5490 N  N    . VAL   B 1 100 ? 39.831 -29.731 9.651   1.00 23.84 ?  100 VAL   B N    1 
ATOM   5491 C  CA   . VAL   B 1 100 ? 39.224 -30.824 10.411  1.00 27.04 ?  100 VAL   B CA   1 
ATOM   5492 C  C    . VAL   B 1 100 ? 40.249 -31.492 11.320  1.00 28.17 ?  100 VAL   B C    1 
ATOM   5493 O  O    . VAL   B 1 100 ? 39.904 -31.984 12.401  1.00 29.17 ?  100 VAL   B O    1 
ATOM   5494 C  CB   . VAL   B 1 100 ? 38.540 -31.825 9.455   1.00 29.55 ?  100 VAL   B CB   1 
ATOM   5495 C  CG1  . VAL   B 1 100 ? 38.059 -33.055 10.216  1.00 30.47 ?  100 VAL   B CG1  1 
ATOM   5496 C  CG2  . VAL   B 1 100 ? 37.372 -31.154 8.746   1.00 30.00 ?  100 VAL   B CG2  1 
ATOM   5497 H  H    . VAL   B 1 100 ? 39.811 -29.844 8.792   1.00 28.63 ?  100 VAL   B H    1 
ATOM   5498 H  HA   . VAL   B 1 100 ? 38.524 -30.458 10.973  1.00 32.48 ?  100 VAL   B HA   1 
ATOM   5499 H  HB   . VAL   B 1 100 ? 39.173 -32.120 8.781   1.00 35.48 ?  100 VAL   B HB   1 
ATOM   5500 H  HG11 . VAL   B 1 100 ? 37.442 -33.555 9.654   1.00 36.59 ?  100 VAL   B HG11 1 
ATOM   5501 H  HG12 . VAL   B 1 100 ? 38.821 -33.611 10.439  1.00 36.59 ?  100 VAL   B HG12 1 
ATOM   5502 H  HG13 . VAL   B 1 100 ? 37.605 -32.769 11.024  1.00 36.59 ?  100 VAL   B HG13 1 
ATOM   5503 H  HG21 . VAL   B 1 100 ? 36.934 -31.801 8.170   1.00 36.02 ?  100 VAL   B HG21 1 
ATOM   5504 H  HG22 . VAL   B 1 100 ? 36.745 -30.830 9.413   1.00 36.02 ?  100 VAL   B HG22 1 
ATOM   5505 H  HG23 . VAL   B 1 100 ? 37.708 -30.414 8.219   1.00 36.02 ?  100 VAL   B HG23 1 
ATOM   5506 N  N    . ASN   B 1 101 ? 41.517 -31.537 10.902  1.00 28.79 ?  101 ASN   B N    1 
ATOM   5507 C  CA   . ASN   B 1 101 ? 42.559 -32.078 11.773  1.00 30.86 ?  101 ASN   B CA   1 
ATOM   5508 C  C    . ASN   B 1 101 ? 42.747 -31.239 13.031  1.00 34.21 ?  101 ASN   B C    1 
ATOM   5509 O  O    . ASN   B 1 101 ? 43.355 -31.717 13.997  1.00 34.95 ?  101 ASN   B O    1 
ATOM   5510 C  CB   . ASN   B 1 101 ? 43.879 -32.222 11.012  1.00 30.14 ?  101 ASN   B CB   1 
ATOM   5511 C  CG   . ASN   B 1 101 ? 43.864 -33.387 10.039  1.00 29.16 ?  101 ASN   B CG   1 
ATOM   5512 O  OD1  . ASN   B 1 101 ? 43.186 -34.384 10.267  1.00 30.00 ?  101 ASN   B OD1  1 
ATOM   5513 N  ND2  . ASN   B 1 101 ? 44.604 -33.261 8.944   1.00 28.45 ?  101 ASN   B ND2  1 
ATOM   5514 H  H    . ASN   B 1 101 ? 41.787 -31.285 10.128  1.00 34.57 ?  101 ASN   B H    1 
ATOM   5515 H  HA   . ASN   B 1 101 ? 42.290 -32.964 12.056  1.00 37.06 ?  101 ASN   B HA   1 
ATOM   5516 H  HB2  . ASN   B 1 101 ? 44.049 -31.415 10.506  1.00 36.19 ?  101 ASN   B HB2  1 
ATOM   5517 H  HB3  . ASN   B 1 101 ? 44.595 -32.374 11.648  1.00 36.19 ?  101 ASN   B HB3  1 
ATOM   5518 H  HD21 . ASN   B 1 101 ? 44.625 -33.896 8.364   1.00 34.16 ?  101 ASN   B HD21 1 
ATOM   5519 H  HD22 . ASN   B 1 101 ? 45.062 -32.546 8.816   1.00 34.16 ?  101 ASN   B HD22 1 
ATOM   5520 N  N    A LYS   B 1 102 ? 42.249 -30.002 13.035  0.56 36.18 ?  102 LYS   B N    1 
ATOM   5521 N  N    B LYS   B 1 102 ? 42.249 -30.003 13.038  0.44 36.14 ?  102 LYS   B N    1 
ATOM   5522 C  CA   A LYS   B 1 102 ? 42.208 -29.162 14.224  0.56 38.40 ?  102 LYS   B CA   1 
ATOM   5523 C  CA   B LYS   B 1 102 ? 42.210 -29.173 14.233  0.44 38.26 ?  102 LYS   B CA   1 
ATOM   5524 C  C    A LYS   B 1 102 ? 40.829 -29.139 14.871  0.56 37.97 ?  102 LYS   B C    1 
ATOM   5525 C  C    B LYS   B 1 102 ? 40.823 -29.127 14.861  0.44 37.91 ?  102 LYS   B C    1 
ATOM   5526 O  O    A LYS   B 1 102 ? 40.596 -28.336 15.780  0.56 38.17 ?  102 LYS   B O    1 
ATOM   5527 O  O    B LYS   B 1 102 ? 40.581 -28.301 15.746  0.44 38.08 ?  102 LYS   B O    1 
ATOM   5528 C  CB   A LYS   B 1 102 ? 42.620 -27.729 13.882  0.56 40.91 ?  102 LYS   B CB   1 
ATOM   5529 C  CB   B LYS   B 1 102 ? 42.673 -27.751 13.913  0.44 40.55 ?  102 LYS   B CB   1 
ATOM   5530 C  CG   A LYS   B 1 102 ? 44.078 -27.539 13.512  0.56 43.33 ?  102 LYS   B CG   1 
ATOM   5531 C  CG   B LYS   B 1 102 ? 44.142 -27.626 13.551  0.44 42.76 ?  102 LYS   B CG   1 
ATOM   5532 C  CD   A LYS   B 1 102 ? 44.326 -26.086 13.138  0.56 45.29 ?  102 LYS   B CD   1 
ATOM   5533 C  CD   B LYS   B 1 102 ? 44.467 -26.199 13.139  0.44 44.55 ?  102 LYS   B CD   1 
ATOM   5534 C  CE   A LYS   B 1 102 ? 45.788 -25.806 12.849  0.56 46.79 ?  102 LYS   B CE   1 
ATOM   5535 C  CE   B LYS   B 1 102 ? 45.955 -25.993 12.919  0.44 45.97 ?  102 LYS   B CE   1 
ATOM   5536 N  NZ   A LYS   B 1 102 ? 45.997 -24.379 12.466  0.56 47.58 ?  102 LYS   B NZ   1 
ATOM   5537 N  NZ   B LYS   B 1 102 ? 46.252 -24.592 12.503  0.44 46.72 ?  102 LYS   B NZ   1 
ATOM   5538 H  H    A LYS   B 1 102 ? 41.922 -29.618 12.337  0.56 43.44 ?  102 LYS   B H    1 
ATOM   5539 H  H    B LYS   B 1 102 ? 41.920 -29.616 12.344  0.44 43.38 ?  102 LYS   B H    1 
ATOM   5540 H  HA   A LYS   B 1 102 ? 42.841 -29.506 14.872  0.56 46.10 ?  102 LYS   B HA   1 
ATOM   5541 H  HA   B LYS   B 1 102 ? 42.823 -29.540 14.887  0.44 45.93 ?  102 LYS   B HA   1 
ATOM   5542 H  HB2  A LYS   B 1 102 ? 42.088 -27.426 13.131  0.56 49.11 ?  102 LYS   B HB2  1 
ATOM   5543 H  HB2  B LYS   B 1 102 ? 42.157 -27.418 13.163  0.44 48.69 ?  102 LYS   B HB2  1 
ATOM   5544 H  HB3  A LYS   B 1 102 ? 42.443 -27.167 14.653  0.56 49.11 ?  102 LYS   B HB3  1 
ATOM   5545 H  HB3  B LYS   B 1 102 ? 42.515 -27.192 14.691  0.44 48.69 ?  102 LYS   B HB3  1 
ATOM   5546 H  HG2  A LYS   B 1 102 ? 44.640 -27.763 14.271  0.56 52.02 ?  102 LYS   B HG2  1 
ATOM   5547 H  HG2  B LYS   B 1 102 ? 44.686 -27.855 14.322  0.44 51.34 ?  102 LYS   B HG2  1 
ATOM   5548 H  HG3  A LYS   B 1 102 ? 44.297 -28.097 12.749  0.56 52.02 ?  102 LYS   B HG3  1 
ATOM   5549 H  HG3  B LYS   B 1 102 ? 44.343 -28.216 12.808  0.44 51.34 ?  102 LYS   B HG3  1 
ATOM   5550 H  HD2  A LYS   B 1 102 ? 43.814 -25.872 12.342  0.56 54.37 ?  102 LYS   B HD2  1 
ATOM   5551 H  HD2  B LYS   B 1 102 ? 44.007 -25.996 12.309  0.44 53.49 ?  102 LYS   B HD2  1 
ATOM   5552 H  HD3  A LYS   B 1 102 ? 44.049 -25.518 13.874  0.56 54.37 ?  102 LYS   B HD3  1 
ATOM   5553 H  HD3  B LYS   B 1 102 ? 44.177 -25.592 13.838  0.44 53.49 ?  102 LYS   B HD3  1 
ATOM   5554 H  HE2  A LYS   B 1 102 ? 46.313 -25.989 13.644  0.56 56.17 ?  102 LYS   B HE2  1 
ATOM   5555 H  HE2  B LYS   B 1 102 ? 46.430 -26.172 13.746  0.44 55.18 ?  102 LYS   B HE2  1 
ATOM   5556 H  HE3  A LYS   B 1 102 ? 46.083 -26.366 12.114  0.56 56.17 ?  102 LYS   B HE3  1 
ATOM   5557 H  HE3  B LYS   B 1 102 ? 46.263 -26.590 12.219  0.44 55.18 ?  102 LYS   B HE3  1 
ATOM   5558 H  HZ1  A LYS   B 1 102 ? 46.858 -24.231 12.300  0.56 57.12 ?  102 LYS   B HZ1  1 
ATOM   5559 H  HZ1  B LYS   B 1 102 ? 47.127 -24.490 12.379  0.44 56.09 ?  102 LYS   B HZ1  1 
ATOM   5560 H  HZ2  A LYS   B 1 102 ? 45.524 -24.188 11.736  0.56 57.12 ?  102 LYS   B HZ2  1 
ATOM   5561 H  HZ2  B LYS   B 1 102 ? 45.828 -24.405 11.743  0.44 56.09 ?  102 LYS   B HZ2  1 
ATOM   5562 H  HZ3  A LYS   B 1 102 ? 45.733 -23.845 13.128  0.56 57.12 ?  102 LYS   B HZ3  1 
ATOM   5563 H  HZ3  B LYS   B 1 102 ? 45.981 -24.024 13.133  0.44 56.09 ?  102 LYS   B HZ3  1 
ATOM   5564 N  N    . GLY   B 1 103 ? 39.905 -29.981 14.413  1.00 37.50 ?  103 GLY   B N    1 
ATOM   5565 C  CA   . GLY   B 1 103 ? 38.576 -30.037 14.988  1.00 37.38 ?  103 GLY   B CA   1 
ATOM   5566 C  C    . GLY   B 1 103 ? 37.621 -28.961 14.523  1.00 36.81 ?  103 GLY   B C    1 
ATOM   5567 O  O    . GLY   B 1 103 ? 36.520 -28.858 15.076  1.00 37.15 ?  103 GLY   B O    1 
ATOM   5568 H  H    A GLY   B 1 103 ? 40.027 -30.530 13.763  0.56 45.02 ?  103 GLY   B H    1 
ATOM   5569 H  H    B GLY   B 1 103 ? 40.030 -30.536 13.770  0.44 45.02 ?  103 GLY   B H    1 
ATOM   5570 H  HA2  . GLY   B 1 103 ? 38.183 -30.902 14.786  1.00 44.87 ?  103 GLY   B HA2  1 
ATOM   5571 H  HA3  . GLY   B 1 103 ? 38.646 -29.960 15.952  1.00 44.87 ?  103 GLY   B HA3  1 
ATOM   5572 N  N    . GLU   B 1 104 ? 37.998 -28.158 13.532  1.00 35.25 ?  104 GLU   B N    1 
ATOM   5573 C  CA   . GLU   B 1 104 ? 37.134 -27.081 13.072  1.00 33.93 ?  104 GLU   B CA   1 
ATOM   5574 C  C    . GLU   B 1 104 ? 35.941 -27.635 12.293  1.00 34.52 ?  104 GLU   B C    1 
ATOM   5575 O  O    . GLU   B 1 104 ? 35.968 -28.749 11.763  1.00 35.18 ?  104 GLU   B O    1 
ATOM   5576 C  CB   . GLU   B 1 104 ? 37.937 -26.074 12.249  1.00 32.62 ?  104 GLU   B CB   1 
ATOM   5577 C  CG   . GLU   B 1 104 ? 39.016 -25.395 13.086  1.00 31.48 ?  104 GLU   B CG   1 
ATOM   5578 C  CD   . GLU   B 1 104 ? 39.964 -24.516 12.291  1.00 30.51 ?  104 GLU   B CD   1 
ATOM   5579 O  OE1  . GLU   B 1 104 ? 39.984 -24.598 11.046  1.00 28.91 ?  104 GLU   B OE1  1 
ATOM   5580 O  OE2  . GLU   B 1 104 ? 40.702 -23.735 12.928  1.00 30.66 -1 104 GLU   B OE2  1 
ATOM   5581 H  H    . GLU   B 1 104 ? 38.752 -28.207 13.121  1.00 42.32 ?  104 GLU   B H    1 
ATOM   5582 H  HA   . GLU   B 1 104 ? 36.787 -26.616 13.847  1.00 40.74 ?  104 GLU   B HA   1 
ATOM   5583 H  HB2  . GLU   B 1 104 ? 38.366 -26.535 11.512  1.00 39.17 ?  104 GLU   B HB2  1 
ATOM   5584 H  HB3  . GLU   B 1 104 ? 37.335 -25.390 11.912  1.00 39.17 ?  104 GLU   B HB3  1 
ATOM   5585 H  HG2  . GLU   B 1 104 ? 38.586 -24.839 13.755  1.00 37.80 ?  104 GLU   B HG2  1 
ATOM   5586 H  HG3  . GLU   B 1 104 ? 39.550 -26.077 13.519  1.00 37.80 ?  104 GLU   B HG3  1 
ATOM   5587 N  N    A ASP   B 1 105 ? 34.884 -26.826 12.223  0.56 34.50 ?  105 ASP   B N    1 
ATOM   5588 N  N    B ASP   B 1 105 ? 34.878 -26.834 12.234  0.44 34.70 ?  105 ASP   B N    1 
ATOM   5589 C  CA   A ASP   B 1 105 ? 33.609 -27.263 11.668  0.56 34.82 ?  105 ASP   B CA   1 
ATOM   5590 C  CA   B ASP   B 1 105 ? 33.608 -27.284 11.677  0.44 34.94 ?  105 ASP   B CA   1 
ATOM   5591 C  C    A ASP   B 1 105 ? 33.687 -27.300 10.148  0.56 32.84 ?  105 ASP   B C    1 
ATOM   5592 C  C    B ASP   B 1 105 ? 33.688 -27.305 10.156  0.44 33.10 ?  105 ASP   B C    1 
ATOM   5593 O  O    A ASP   B 1 105 ? 33.867 -26.260 9.505   0.56 32.06 ?  105 ASP   B O    1 
ATOM   5594 O  O    B ASP   B 1 105 ? 33.878 -26.261 9.523   0.44 32.57 ?  105 ASP   B O    1 
ATOM   5595 C  CB   A ASP   B 1 105 ? 32.501 -26.312 12.114  0.56 37.37 ?  105 ASP   B CB   1 
ATOM   5596 C  CB   B ASP   B 1 105 ? 32.476 -26.368 12.136  0.44 37.05 ?  105 ASP   B CB   1 
ATOM   5597 C  CG   A ASP   B 1 105 ? 31.127 -26.771 11.671  0.56 39.47 ?  105 ASP   B CG   1 
ATOM   5598 C  CG   B ASP   B 1 105 ? 31.107 -26.905 11.766  0.44 38.72 ?  105 ASP   B CG   1 
ATOM   5599 O  OD1  A ASP   B 1 105 ? 31.014 -27.901 11.152  0.56 39.80 ?  105 ASP   B OD1  1 
ATOM   5600 O  OD1  B ASP   B 1 105 ? 31.039 -27.993 11.156  0.44 39.11 ?  105 ASP   B OD1  1 
ATOM   5601 O  OD2  A ASP   B 1 105 ? 30.160 -25.997 11.836  0.56 40.64 -1 105 ASP   B OD2  1 
ATOM   5602 O  OD2  B ASP   B 1 105 ? 30.098 -26.242 12.089  0.44 39.40 -1 105 ASP   B OD2  1 
ATOM   5603 H  H    A ASP   B 1 105 ? 34.883 -26.009 12.489  0.56 41.42 ?  105 ASP   B H    1 
ATOM   5604 H  H    B ASP   B 1 105 ? 34.868 -26.019 12.508  0.44 41.66 ?  105 ASP   B H    1 
ATOM   5605 H  HA   A ASP   B 1 105 ? 33.399 -28.153 11.988  0.56 41.81 ?  105 ASP   B HA   1 
ATOM   5606 H  HA   B ASP   B 1 105 ? 33.418 -28.183 11.986  0.44 41.95 ?  105 ASP   B HA   1 
ATOM   5607 H  HB2  A ASP   B 1 105 ? 32.511 -26.246 13.082  0.56 44.87 ?  105 ASP   B HB2  1 
ATOM   5608 H  HB2  B ASP   B 1 105 ? 32.511 -26.277 13.100  0.44 44.49 ?  105 ASP   B HB2  1 
ATOM   5609 H  HB3  A ASP   B 1 105 ? 32.651 -25.440 11.719  0.56 44.87 ?  105 ASP   B HB3  1 
ATOM   5610 H  HB3  B ASP   B 1 105 ? 32.577 -25.500 11.715  0.44 44.49 ?  105 ASP   B HB3  1 
ATOM   5611 N  N    . ILE   B 1 106 ? 33.522 -28.496 9.574   1.00 32.13 ?  106 ILE   B N    1 
ATOM   5612 C  CA   . ILE   B 1 106 ? 33.527 -28.651 8.125   1.00 30.13 ?  106 ILE   B CA   1 
ATOM   5613 C  C    . ILE   B 1 106 ? 32.427 -27.824 7.463   1.00 28.32 ?  106 ILE   B C    1 
ATOM   5614 O  O    . ILE   B 1 106 ? 32.515 -27.518 6.271   1.00 27.60 ?  106 ILE   B O    1 
ATOM   5615 C  CB   . ILE   B 1 106 ? 33.431 -30.157 7.775   1.00 30.55 ?  106 ILE   B CB   1 
ATOM   5616 C  CG1  . ILE   B 1 106 ? 33.703 -30.404 6.291   1.00 30.77 ?  106 ILE   B CG1  1 
ATOM   5617 C  CG2  . ILE   B 1 106 ? 32.066 -30.713 8.153   1.00 31.50 ?  106 ILE   B CG2  1 
ATOM   5618 C  CD1  . ILE   B 1 106 ? 35.058 -29.930 5.845   1.00 30.67 ?  106 ILE   B CD1  1 
ATOM   5619 H  H    A ILE   B 1 106 ? 33.401 -29.230 10.006  0.56 38.57 ?  106 ILE   B H    1 
ATOM   5620 H  H    B ILE   B 1 106 ? 33.401 -29.231 10.003  0.44 38.57 ?  106 ILE   B H    1 
ATOM   5621 H  HA   . ILE   B 1 106 ? 34.372 -28.323 7.790   1.00 36.17 ?  106 ILE   B HA   1 
ATOM   5622 H  HB   . ILE   B 1 106 ? 34.103 -30.632 8.289   1.00 36.68 ?  106 ILE   B HB   1 
ATOM   5623 H  HG12 . ILE   B 1 106 ? 33.654 -31.359 6.116   1.00 36.95 ?  106 ILE   B HG12 1 
ATOM   5624 H  HG13 . ILE   B 1 106 ? 33.037 -29.940 5.764   1.00 36.95 ?  106 ILE   B HG13 1 
ATOM   5625 H  HG21 . ILE   B 1 106 ? 32.084 -31.680 8.068   1.00 37.82 ?  106 ILE   B HG21 1 
ATOM   5626 H  HG22 . ILE   B 1 106 ? 31.868 -30.467 9.070   1.00 37.82 ?  106 ILE   B HG22 1 
ATOM   5627 H  HG23 . ILE   B 1 106 ? 31.396 -30.343 7.558   1.00 37.82 ?  106 ILE   B HG23 1 
ATOM   5628 H  HD11 . ILE   B 1 106 ? 35.270 -30.337 4.991   1.00 36.83 ?  106 ILE   B HD11 1 
ATOM   5629 H  HD12 . ILE   B 1 106 ? 35.042 -28.964 5.754   1.00 36.83 ?  106 ILE   B HD12 1 
ATOM   5630 H  HD13 . ILE   B 1 106 ? 35.719 -30.190 6.506   1.00 36.83 ?  106 ILE   B HD13 1 
ATOM   5631 N  N    A GLN   B 1 107 ? 31.385 -27.454 8.211   0.56 28.32 ?  107 GLN   B N    1 
ATOM   5632 N  N    B GLN   B 1 107 ? 31.397 -27.440 8.219   0.44 28.33 ?  107 GLN   B N    1 
ATOM   5633 C  CA   A GLN   B 1 107 ? 30.309 -26.650 7.641   0.56 28.08 ?  107 GLN   B CA   1 
ATOM   5634 C  CA   B GLN   B 1 107 ? 30.309 -26.646 7.661   0.44 28.08 ?  107 GLN   B CA   1 
ATOM   5635 C  C    A GLN   B 1 107 ? 30.795 -25.293 7.146   0.56 25.58 ?  107 GLN   B C    1 
ATOM   5636 C  C    B GLN   B 1 107 ? 30.778 -25.280 7.176   0.44 25.64 ?  107 GLN   B C    1 
ATOM   5637 O  O    A GLN   B 1 107 ? 30.156 -24.707 6.267   0.56 25.77 ?  107 GLN   B O    1 
ATOM   5638 O  O    B GLN   B 1 107 ? 30.108 -24.674 6.335   0.44 25.92 ?  107 GLN   B O    1 
ATOM   5639 C  CB   A GLN   B 1 107 ? 29.190 -26.466 8.670   0.56 31.45 ?  107 GLN   B CB   1 
ATOM   5640 C  CB   B GLN   B 1 107 ? 29.201 -26.485 8.706   0.44 31.07 ?  107 GLN   B CB   1 
ATOM   5641 C  CG   A GLN   B 1 107 ? 27.862 -25.991 8.082   0.56 34.49 ?  107 GLN   B CG   1 
ATOM   5642 C  CG   B GLN   B 1 107 ? 27.857 -26.033 8.148   0.44 33.76 ?  107 GLN   B CG   1 
ATOM   5643 C  CD   A GLN   B 1 107 ? 27.767 -24.480 7.963   0.56 36.70 ?  107 GLN   B CD   1 
ATOM   5644 C  CD   B GLN   B 1 107 ? 27.717 -24.523 8.089   0.44 35.75 ?  107 GLN   B CD   1 
ATOM   5645 O  OE1  A GLN   B 1 107 ? 28.585 -23.748 8.523   0.56 37.52 ?  107 GLN   B OE1  1 
ATOM   5646 O  OE1  B GLN   B 1 107 ? 28.517 -23.788 8.670   0.44 36.40 ?  107 GLN   B OE1  1 
ATOM   5647 N  NE2  A GLN   B 1 107 ? 26.761 -24.004 7.234   0.56 37.55 ?  107 GLN   B NE2  1 
ATOM   5648 N  NE2  B GLN   B 1 107 ? 26.691 -24.051 7.386   0.44 36.55 ?  107 GLN   B NE2  1 
ATOM   5649 H  H    A GLN   B 1 107 ? 31.277 -27.657 9.034   0.56 34.01 ?  107 GLN   B H    1 
ATOM   5650 H  H    B GLN   B 1 107 ? 31.309 -27.622 9.048   0.44 34.01 ?  107 GLN   B H    1 
ATOM   5651 H  HA   A GLN   B 1 107 ? 29.935 -27.124 6.881   0.56 33.72 ?  107 GLN   B HA   1 
ATOM   5652 H  HA   B GLN   B 1 107 ? 29.933 -27.117 6.900   0.44 33.72 ?  107 GLN   B HA   1 
ATOM   5653 H  HB2  A GLN   B 1 107 ? 29.031 -27.315 9.105   0.56 37.76 ?  107 GLN   B HB2  1 
ATOM   5654 H  HB2  B GLN   B 1 107 ? 29.064 -27.340 9.138   0.44 37.30 ?  107 GLN   B HB2  1 
ATOM   5655 H  HB3  A GLN   B 1 107 ? 29.477 -25.811 9.325   0.56 37.76 ?  107 GLN   B HB3  1 
ATOM   5656 H  HB3  B GLN   B 1 107 ? 29.487 -25.830 9.362   0.44 37.30 ?  107 GLN   B HB3  1 
ATOM   5657 H  HG2  A GLN   B 1 107 ? 27.757 -26.366 7.193   0.56 41.41 ?  107 GLN   B HG2  1 
ATOM   5658 H  HG2  B GLN   B 1 107 ? 27.754 -26.378 7.248   0.44 40.54 ?  107 GLN   B HG2  1 
ATOM   5659 H  HG3  A GLN   B 1 107 ? 27.139 -26.294 8.655   0.56 41.41 ?  107 GLN   B HG3  1 
ATOM   5660 H  HG3  B GLN   B 1 107 ? 27.149 -26.381 8.716   0.44 40.54 ?  107 GLN   B HG3  1 
ATOM   5661 H  HE21 A GLN   B 1 107 ? 26.208 -24.546 6.856   0.56 45.08 ?  107 GLN   B HE21 1 
ATOM   5662 H  HE21 B GLN   B 1 107 ? 26.152 -24.594 6.992   0.44 43.88 ?  107 GLN   B HE21 1 
ATOM   5663 H  HE22 A GLN   B 1 107 ? 26.659 -23.155 7.139   0.56 45.08 ?  107 GLN   B HE22 1 
ATOM   5664 H  HE22 B GLN   B 1 107 ? 26.566 -23.202 7.325   0.44 43.88 ?  107 GLN   B HE22 1 
ATOM   5665 N  N    . LEU   B 1 108 ? 31.916 -24.787 7.674   1.00 23.33 ?  108 LEU   B N    1 
ATOM   5666 C  CA   . LEU   B 1 108 ? 32.453 -23.490 7.257   1.00 20.28 ?  108 LEU   B CA   1 
ATOM   5667 C  C    . LEU   B 1 108 ? 33.099 -23.521 5.880   1.00 17.49 ?  108 LEU   B C    1 
ATOM   5668 O  O    . LEU   B 1 108 ? 33.528 -22.468 5.388   1.00 16.25 ?  108 LEU   B O    1 
ATOM   5669 C  CB   . LEU   B 1 108 ? 33.451 -22.971 8.294   1.00 20.68 ?  108 LEU   B CB   1 
ATOM   5670 C  CG   . LEU   B 1 108 ? 32.828 -22.421 9.577   1.00 22.33 ?  108 LEU   B CG   1 
ATOM   5671 C  CD1  . LEU   B 1 108 ? 33.825 -22.443 10.719  1.00 22.83 ?  108 LEU   B CD1  1 
ATOM   5672 C  CD2  . LEU   B 1 108 ? 32.331 -21.003 9.344   1.00 22.88 ?  108 LEU   B CD2  1 
ATOM   5673 H  H    A LEU   B 1 108 ? 32.375 -25.175 8.285   0.56 28.02 ?  108 LEU   B H    1 
ATOM   5674 H  H    B LEU   B 1 108 ? 32.392 -25.187 8.265   0.44 28.02 ?  108 LEU   B H    1 
ATOM   5675 H  HA   . LEU   B 1 108 ? 31.718 -22.859 7.220   1.00 24.36 ?  108 LEU   B HA   1 
ATOM   5676 H  HB2  . LEU   B 1 108 ? 34.039 -23.696 8.548   1.00 24.84 ?  108 LEU   B HB2  1 
ATOM   5677 H  HB3  . LEU   B 1 108 ? 33.966 -22.255 7.894   1.00 24.84 ?  108 LEU   B HB3  1 
ATOM   5678 H  HG   . LEU   B 1 108 ? 32.067 -22.968 9.829   1.00 26.82 ?  108 LEU   B HG   1 
ATOM   5679 H  HD11 . LEU   B 1 108 ? 33.393 -22.109 11.524  1.00 27.42 ?  108 LEU   B HD11 1 
ATOM   5680 H  HD12 . LEU   B 1 108 ? 34.123 -23.354 10.860  1.00 27.42 ?  108 LEU   B HD12 1 
ATOM   5681 H  HD13 . LEU   B 1 108 ? 34.579 -21.878 10.492  1.00 27.42 ?  108 LEU   B HD13 1 
ATOM   5682 H  HD21 . LEU   B 1 108 ? 31.936 -20.667 10.163  1.00 27.48 ?  108 LEU   B HD21 1 
ATOM   5683 H  HD22 . LEU   B 1 108 ? 33.081 -20.445 9.085   1.00 27.48 ?  108 LEU   B HD22 1 
ATOM   5684 H  HD23 . LEU   B 1 108 ? 31.667 -21.014 8.637   1.00 27.48 ?  108 LEU   B HD23 1 
ATOM   5685 N  N    . LEU   B 1 109 ? 33.160 -24.690 5.250   1.00 15.87 ?  109 LEU   B N    1 
ATOM   5686 C  CA   . LEU   B 1 109 ? 33.782 -24.809 3.938   1.00 15.15 ?  109 LEU   B CA   1 
ATOM   5687 C  C    . LEU   B 1 109 ? 33.008 -24.039 2.872   1.00 14.63 ?  109 LEU   B C    1 
ATOM   5688 O  O    . LEU   B 1 109 ? 33.617 -23.463 1.962   1.00 14.08 ?  109 LEU   B O    1 
ATOM   5689 C  CB   . LEU   B 1 109 ? 33.908 -26.289 3.578   1.00 15.50 ?  109 LEU   B CB   1 
ATOM   5690 C  CG   . LEU   B 1 109 ? 34.681 -26.646 2.314   1.00 14.74 ?  109 LEU   B CG   1 
ATOM   5691 C  CD1  . LEU   B 1 109 ? 36.055 -26.003 2.312   1.00 14.30 ?  109 LEU   B CD1  1 
ATOM   5692 C  CD2  . LEU   B 1 109 ? 34.813 -28.162 2.184   1.00 15.59 ?  109 LEU   B CD2  1 
ATOM   5693 H  H    . LEU   B 1 109 ? 32.864 -25.429 5.561   1.00 19.07 ?  109 LEU   B H    1 
ATOM   5694 H  HA   . LEU   B 1 109 ? 34.676 -24.434 3.976   1.00 18.20 ?  109 LEU   B HA   1 
ATOM   5695 H  HB2  . LEU   B 1 109 ? 34.353 -26.740 4.311   1.00 18.62 ?  109 LEU   B HB2  1 
ATOM   5696 H  HB3  . LEU   B 1 109 ? 33.017 -26.653 3.474   1.00 18.62 ?  109 LEU   B HB3  1 
ATOM   5697 H  HG   . LEU   B 1 109 ? 34.193 -26.334 1.536   1.00 17.71 ?  109 LEU   B HG   1 
ATOM   5698 H  HD11 . LEU   B 1 109 ? 36.579 -26.376 1.584   1.00 17.18 ?  109 LEU   B HD11 1 
ATOM   5699 H  HD12 . LEU   B 1 109 ? 35.951 -25.050 2.191   1.00 17.18 ?  109 LEU   B HD12 1 
ATOM   5700 H  HD13 . LEU   B 1 109 ? 36.489 -26.191 3.158   1.00 17.18 ?  109 LEU   B HD13 1 
ATOM   5701 H  HD21 . LEU   B 1 109 ? 35.373 -28.371 1.415   1.00 18.73 ?  109 LEU   B HD21 1 
ATOM   5702 H  HD22 . LEU   B 1 109 ? 35.220 -28.518 2.989   1.00 18.73 ?  109 LEU   B HD22 1 
ATOM   5703 H  HD23 . LEU   B 1 109 ? 33.932 -28.554 2.060   1.00 18.73 ?  109 LEU   B HD23 1 
ATOM   5704 N  N    . LYS   B 1 110 ? 31.674 -23.997 2.965   1.00 14.16 ?  110 LYS   B N    1 
ATOM   5705 C  CA   . LYS   B 1 110 ? 30.917 -23.242 1.970   1.00 13.87 ?  110 LYS   B CA   1 
ATOM   5706 C  C    . LYS   B 1 110 ? 31.252 -21.755 2.051   1.00 13.48 ?  110 LYS   B C    1 
ATOM   5707 O  O    . LYS   B 1 110 ? 31.520 -21.113 1.029   1.00 13.48 ?  110 LYS   B O    1 
ATOM   5708 C  CB   . LYS   B 1 110 ? 29.411 -23.492 2.118   1.00 14.47 ?  110 LYS   B CB   1 
ATOM   5709 C  CG   . LYS   B 1 110 ? 28.607 -22.906 0.955   1.00 14.89 ?  110 LYS   B CG   1 
ATOM   5710 C  CD   . LYS   B 1 110 ? 27.130 -23.300 1.009   1.00 15.16 ?  110 LYS   B CD   1 
ATOM   5711 C  CE   . LYS   B 1 110 ? 26.365 -22.782 -0.215  1.00 16.44 ?  110 LYS   B CE   1 
ATOM   5712 N  NZ   . LYS   B 1 110 ? 26.723 -23.499 -1.471  1.00 16.67 ?  110 LYS   B NZ   1 
ATOM   5713 H  H    . LYS   B 1 110 ? 31.202 -24.384 3.570   1.00 17.01 ?  110 LYS   B H    1 
ATOM   5714 H  HA   . LYS   B 1 110 ? 31.176 -23.547 1.087   1.00 16.67 ?  110 LYS   B HA   1 
ATOM   5715 H  HB2  . LYS   B 1 110 ? 29.249 -24.448 2.142   1.00 17.39 ?  110 LYS   B HB2  1 
ATOM   5716 H  HB3  . LYS   B 1 110 ? 29.096 -23.079 2.935   1.00 17.39 ?  110 LYS   B HB3  1 
ATOM   5717 H  HG2  . LYS   B 1 110 ? 28.659 -21.941 0.982   1.00 17.89 ?  110 LYS   B HG2  1 
ATOM   5718 H  HG3  . LYS   B 1 110 ? 28.969 -23.238 0.118   1.00 17.89 ?  110 LYS   B HG3  1 
ATOM   5719 H  HD2  . LYS   B 1 110 ? 27.053 -24.267 1.028   1.00 18.21 ?  110 LYS   B HD2  1 
ATOM   5720 H  HD3  . LYS   B 1 110 ? 26.725 -22.917 1.806   1.00 18.21 ?  110 LYS   B HD3  1 
ATOM   5721 H  HE2  . LYS   B 1 110 ? 25.414 -22.893 -0.067  1.00 19.74 ?  110 LYS   B HE2  1 
ATOM   5722 H  HE3  . LYS   B 1 110 ? 26.572 -21.839 -0.339  1.00 19.74 ?  110 LYS   B HE3  1 
ATOM   5723 H  HZ1  . LYS   B 1 110 ? 26.264 -23.169 -2.154  1.00 20.02 ?  110 LYS   B HZ1  1 
ATOM   5724 H  HZ2  . LYS   B 1 110 ? 27.596 -23.405 -1.636  1.00 20.02 ?  110 LYS   B HZ2  1 
ATOM   5725 H  HZ3  . LYS   B 1 110 ? 26.541 -24.366 -1.387  1.00 20.02 ?  110 LYS   B HZ3  1 
ATOM   5726 N  N    . SER   B 1 111 ? 31.278 -21.203 3.269   1.00 14.05 ?  111 SER   B N    1 
ATOM   5727 C  CA   . SER   B 1 111 ? 31.677 -19.809 3.448   1.00 13.61 ?  111 SER   B CA   1 
ATOM   5728 C  C    . SER   B 1 111 ? 33.055 -19.556 2.847   1.00 13.43 ?  111 SER   B C    1 
ATOM   5729 O  O    . SER   B 1 111 ? 33.279 -18.532 2.183   1.00 13.70 ?  111 SER   B O    1 
ATOM   5730 C  CB   . SER   B 1 111 ? 31.693 -19.466 4.935   1.00 14.85 ?  111 SER   B CB   1 
ATOM   5731 O  OG   . SER   B 1 111 ? 30.394 -19.453 5.484   1.00 16.00 ?  111 SER   B OG   1 
ATOM   5732 H  H    . SER   B 1 111 ? 31.085 -21.620 3.999   1.00 16.88 ?  111 SER   B H    1 
ATOM   5733 H  HA   . SER   B 1 111 ? 31.040 -19.235 3.007   1.00 16.35 ?  111 SER   B HA   1 
ATOM   5734 H  HB2  . SER   B 1 111 ? 32.215 -20.136 5.409   1.00 17.84 ?  111 SER   B HB2  1 
ATOM   5735 H  HB3  . SER   B 1 111 ? 32.091 -18.595 5.055   1.00 17.84 ?  111 SER   B HB3  1 
ATOM   5736 H  HG   . SER   B 1 111 ? 30.426 -19.257 6.310   1.00 19.22 ?  111 SER   B HG   1 
ATOM   5737 N  N    . ALA   B 1 112 ? 33.996 -20.475 3.074   1.00 13.36 ?  112 ALA   B N    1 
ATOM   5738 C  CA   . ALA   B 1 112 ? 35.339 -20.303 2.532   1.00 12.80 ?  112 ALA   B CA   1 
ATOM   5739 C  C    . ALA   B 1 112 ? 35.309 -20.212 1.008   1.00 12.43 ?  112 ALA   B C    1 
ATOM   5740 O  O    . ALA   B 1 112 ? 35.936 -19.328 0.411   1.00 12.88 ?  112 ALA   B O    1 
ATOM   5741 C  CB   . ALA   B 1 112 ? 36.242 -21.436 3.020   1.00 13.10 ?  112 ALA   B CB   1 
ATOM   5742 H  H    . ALA   B 1 112 ? 33.881 -21.198 3.537   1.00 16.05 ?  112 ALA   B H    1 
ATOM   5743 H  HA   . ALA   B 1 112 ? 35.698 -19.471 2.868   1.00 15.38 ?  112 ALA   B HA   1 
ATOM   5744 H  HB1  . ALA   B 1 112 ? 37.133 -21.304 2.655   1.00 15.74 ?  112 ALA   B HB1  1 
ATOM   5745 H  HB2  . ALA   B 1 112 ? 36.282 -21.412 3.992   1.00 15.74 ?  112 ALA   B HB2  1 
ATOM   5746 H  HB3  . ALA   B 1 112 ? 35.883 -22.283 2.725   1.00 15.74 ?  112 ALA   B HB3  1 
ATOM   5747 N  N    . TYR   B 1 113 ? 34.567 -21.114 0.357   1.00 12.57 ?  113 TYR   B N    1 
ATOM   5748 C  CA   . TYR   B 1 113 ? 34.492 -21.078 -1.098  1.00 12.58 ?  113 TYR   B CA   1 
ATOM   5749 C  C    . TYR   B 1 113 ? 33.782 -19.831 -1.621  1.00 12.13 ?  113 TYR   B C    1 
ATOM   5750 O  O    . TYR   B 1 113 ? 34.057 -19.402 -2.747  1.00 12.05 ?  113 TYR   B O    1 
ATOM   5751 C  CB   . TYR   B 1 113 ? 33.825 -22.342 -1.638  1.00 12.39 ?  113 TYR   B CB   1 
ATOM   5752 C  CG   . TYR   B 1 113 ? 34.784 -23.486 -1.891  1.00 12.86 ?  113 TYR   B CG   1 
ATOM   5753 C  CD1  . TYR   B 1 113 ? 35.771 -23.385 -2.862  1.00 13.52 ?  113 TYR   B CD1  1 
ATOM   5754 C  CD2  . TYR   B 1 113 ? 34.686 -24.667 -1.179  1.00 13.29 ?  113 TYR   B CD2  1 
ATOM   5755 C  CE1  . TYR   B 1 113 ? 36.653 -24.420 -3.108  1.00 13.57 ?  113 TYR   B CE1  1 
ATOM   5756 C  CE2  . TYR   B 1 113 ? 35.563 -25.719 -1.418  1.00 13.74 ?  113 TYR   B CE2  1 
ATOM   5757 C  CZ   . TYR   B 1 113 ? 36.538 -25.591 -2.390  1.00 13.71 ?  113 TYR   B CZ   1 
ATOM   5758 O  OH   . TYR   B 1 113 ? 37.424 -26.609 -2.667  1.00 14.52 ?  113 TYR   B OH   1 
ATOM   5759 H  H    . TYR   B 1 113 ? 34.095 -21.738 0.731   1.00 15.10 ?  113 TYR   B H    1 
ATOM   5760 H  HA   . TYR   B 1 113 ? 35.396 -21.059 -1.438  1.00 15.11 ?  113 TYR   B HA   1 
ATOM   5761 H  HB2  . TYR   B 1 113 ? 33.164 -22.649 -0.996  1.00 14.89 ?  113 TYR   B HB2  1 
ATOM   5762 H  HB3  . TYR   B 1 113 ? 33.387 -22.129 -2.478  1.00 14.89 ?  113 TYR   B HB3  1 
ATOM   5763 H  HD1  . TYR   B 1 113 ? 35.849 -22.596 -3.351  1.00 16.25 ?  113 TYR   B HD1  1 
ATOM   5764 H  HD2  . TYR   B 1 113 ? 34.024 -24.753 -0.531  1.00 15.97 ?  113 TYR   B HD2  1 
ATOM   5765 H  HE1  . TYR   B 1 113 ? 37.307 -24.333 -3.764  1.00 16.30 ?  113 TYR   B HE1  1 
ATOM   5766 H  HE2  . TYR   B 1 113 ? 35.483 -26.511 -0.934  1.00 16.51 ?  113 TYR   B HE2  1 
ATOM   5767 H  HH   . TYR   B 1 113 ? 37.259 -27.273 -2.177  1.00 17.45 ?  113 TYR   B HH   1 
ATOM   5768 N  N    . GLU   B 1 114 ? 32.866 -19.248 -0.842  1.00 12.19 ?  114 GLU   B N    1 
ATOM   5769 C  CA   . GLU   B 1 114 ? 32.182 -18.040 -1.298  1.00 12.18 ?  114 GLU   B CA   1 
ATOM   5770 C  C    . GLU   B 1 114 ? 33.166 -16.919 -1.603  1.00 12.11 ?  114 GLU   B C    1 
ATOM   5771 O  O    . GLU   B 1 114 ? 32.886 -16.057 -2.443  1.00 12.35 ?  114 GLU   B O    1 
ATOM   5772 C  CB   . GLU   B 1 114 ? 31.127 -17.609 -0.276  1.00 12.63 ?  114 GLU   B CB   1 
ATOM   5773 C  CG   . GLU   B 1 114 ? 29.906 -18.530 -0.342  1.00 12.89 ?  114 GLU   B CG   1 
ATOM   5774 C  CD   . GLU   B 1 114 ? 28.879 -18.347 0.766   1.00 13.27 ?  114 GLU   B CD   1 
ATOM   5775 O  OE1  . GLU   B 1 114 ? 29.168 -17.728 1.813   1.00 13.13 ?  114 GLU   B OE1  1 
ATOM   5776 O  OE2  . GLU   B 1 114 ? 27.757 -18.888 0.595   1.00 14.03 -1 114 GLU   B OE2  1 
ATOM   5777 H  H    . GLU   B 1 114 ? 32.619 -19.537 -0.066  1.00 14.65 ?  114 GLU   B H    1 
ATOM   5778 H  HA   . GLU   B 1 114 ? 31.715 -18.245 -2.120  1.00 14.63 ?  114 GLU   B HA   1 
ATOM   5779 H  HB2  . GLU   B 1 114 ? 31.501 -17.660 0.620   1.00 15.18 ?  114 GLU   B HB2  1 
ATOM   5780 H  HB3  . GLU   B 1 114 ? 30.838 -16.705 -0.470  1.00 15.18 ?  114 GLU   B HB3  1 
ATOM   5781 H  HG2  . GLU   B 1 114 ? 29.455 -18.376 -1.181  1.00 15.49 ?  114 GLU   B HG2  1 
ATOM   5782 H  HG3  . GLU   B 1 114 ? 30.216 -19.448 -0.299  1.00 15.49 ?  114 GLU   B HG3  1 
ATOM   5783 N  N    . ASN   B 1 115 ? 34.334 -16.916 -0.954  1.00 11.77 ?  115 ASN   B N    1 
ATOM   5784 C  CA   . ASN   B 1 115 ? 35.327 -15.886 -1.258  1.00 11.69 ?  115 ASN   B CA   1 
ATOM   5785 C  C    . ASN   B 1 115 ? 35.736 -15.917 -2.724  1.00 11.69 ?  115 ASN   B C    1 
ATOM   5786 O  O    . ASN   B 1 115 ? 36.124 -14.878 -3.283  1.00 12.03 ?  115 ASN   B O    1 
ATOM   5787 C  CB   . ASN   B 1 115 ? 36.566 -16.055 -0.370  1.00 12.52 ?  115 ASN   B CB   1 
ATOM   5788 C  CG   . ASN   B 1 115 ? 36.293 -15.784 1.093   1.00 12.69 ?  115 ASN   B CG   1 
ATOM   5789 O  OD1  . ASN   B 1 115 ? 36.287 -14.635 1.534   1.00 14.27 ?  115 ASN   B OD1  1 
ATOM   5790 N  ND2  . ASN   B 1 115 ? 36.122 -16.848 1.873   1.00 13.11 ?  115 ASN   B ND2  1 
ATOM   5791 H  H    . ASN   B 1 115 ? 34.567 -17.474 -0.337  1.00 14.15 ?  115 ASN   B H    1 
ATOM   5792 H  HA   . ASN   B 1 115 ? 34.948 -15.014 -1.072  1.00 14.05 ?  115 ASN   B HA   1 
ATOM   5793 H  HB2  . ASN   B 1 115 ? 36.895 -16.963 -0.453  1.00 15.05 ?  115 ASN   B HB2  1 
ATOM   5794 H  HB3  . ASN   B 1 115 ? 37.250 -15.429 -0.659  1.00 15.05 ?  115 ASN   B HB3  1 
ATOM   5795 H  HD21 . ASN   B 1 115 ? 35.977 -16.747 2.715   1.00 15.75 ?  115 ASN   B HD21 1 
ATOM   5796 H  HD22 . ASN   B 1 115 ? 36.153 -17.641 1.537   1.00 15.75 ?  115 ASN   B HD22 1 
ATOM   5797 N  N    . PHE   B 1 116 ? 35.707 -17.099 -3.353  1.00 11.42 ?  116 PHE   B N    1 
ATOM   5798 C  CA   . PHE   B 1 116 ? 36.139 -17.197 -4.742  1.00 11.89 ?  116 PHE   B CA   1 
ATOM   5799 C  C    . PHE   B 1 116 ? 35.241 -16.371 -5.657  1.00 11.47 ?  116 PHE   B C    1 
ATOM   5800 O  O    . PHE   B 1 116 ? 35.680 -15.929 -6.728  1.00 12.20 ?  116 PHE   B O    1 
ATOM   5801 C  CB   . PHE   B 1 116 ? 36.103 -18.645 -5.254  1.00 11.20 ?  116 PHE   B CB   1 
ATOM   5802 C  CG   . PHE   B 1 116 ? 37.178 -19.593 -4.707  1.00 11.26 ?  116 PHE   B CG   1 
ATOM   5803 C  CD1  . PHE   B 1 116 ? 37.820 -19.409 -3.496  1.00 12.13 ?  116 PHE   B CD1  1 
ATOM   5804 C  CD2  . PHE   B 1 116 ? 37.481 -20.734 -5.444  1.00 11.64 ?  116 PHE   B CD2  1 
ATOM   5805 C  CE1  . PHE   B 1 116 ? 38.752 -20.345 -3.042  1.00 12.54 ?  116 PHE   B CE1  1 
ATOM   5806 C  CE2  . PHE   B 1 116 ? 38.408 -21.663 -5.000  1.00 11.78 ?  116 PHE   B CE2  1 
ATOM   5807 C  CZ   . PHE   B 1 116 ? 39.037 -21.472 -3.799  1.00 11.88 ?  116 PHE   B CZ   1 
ATOM   5808 H  H    . PHE   B 1 116 ? 35.440 -17.841 -3.004  1.00 13.72 ?  116 PHE   B H    1 
ATOM   5809 H  HA   . PHE   B 1 116 ? 37.045 -16.870 -4.826  1.00 14.29 ?  116 PHE   B HA   1 
ATOM   5810 H  HB2  . PHE   B 1 116 ? 35.232 -19.025 -5.030  1.00 13.47 ?  116 PHE   B HB2  1 
ATOM   5811 H  HB3  . PHE   B 1 116 ? 36.195 -18.629 -6.222  1.00 13.47 ?  116 PHE   B HB3  1 
ATOM   5812 H  HD1  . PHE   B 1 116 ? 37.616 -18.666 -2.975  1.00 14.57 ?  116 PHE   B HD1  1 
ATOM   5813 H  HD2  . PHE   B 1 116 ? 37.046 -20.881 -6.256  1.00 13.98 ?  116 PHE   B HD2  1 
ATOM   5814 H  HE1  . PHE   B 1 116 ? 39.183 -20.210 -2.231  1.00 15.07 ?  116 PHE   B HE1  1 
ATOM   5815 H  HE2  . PHE   B 1 116 ? 38.601 -22.411 -5.516  1.00 14.16 ?  116 PHE   B HE2  1 
ATOM   5816 H  HZ   . PHE   B 1 116 ? 39.672 -22.081 -3.505  1.00 14.28 ?  116 PHE   B HZ   1 
ATOM   5817 N  N    . ASN   B 1 117 ? 33.973 -16.169 -5.273  1.00 11.87 ?  117 ASN   B N    1 
ATOM   5818 C  CA   . ASN   B 1 117 ? 33.024 -15.461 -6.135  1.00 12.26 ?  117 ASN   B CA   1 
ATOM   5819 C  C    . ASN   B 1 117 ? 33.336 -13.981 -6.283  1.00 12.84 ?  117 ASN   B C    1 
ATOM   5820 O  O    . ASN   B 1 117 ? 32.731 -13.326 -7.135  1.00 13.97 ?  117 ASN   B O    1 
ATOM   5821 C  CB   . ASN   B 1 117 ? 31.602 -15.679 -5.638  1.00 12.50 ?  117 ASN   B CB   1 
ATOM   5822 C  CG   . ASN   B 1 117 ? 31.145 -17.082 -5.889  1.00 12.70 ?  117 ASN   B CG   1 
ATOM   5823 O  OD1  . ASN   B 1 117 ? 31.502 -17.676 -6.912  1.00 13.48 ?  117 ASN   B OD1  1 
ATOM   5824 N  ND2  . ASN   B 1 117 ? 30.413 -17.655 -4.943  1.00 12.68 ?  117 ASN   B ND2  1 
ATOM   5825 H  H    . ASN   B 1 117 ? 33.647 -16.424 -4.516  1.00 14.27 ?  117 ASN   B H    1 
ATOM   5826 H  HA   . ASN   B 1 117 ? 33.080 -15.854 -7.015  1.00 14.73 ?  117 ASN   B HA   1 
ATOM   5827 H  HB2  . ASN   B 1 117 ? 31.564 -15.511 -4.679  1.00 15.02 ?  117 ASN   B HB2  1 
ATOM   5828 H  HB3  . ASN   B 1 117 ? 31.003 -15.070 -6.102  1.00 15.02 ?  117 ASN   B HB3  1 
ATOM   5829 H  HD21 . ASN   B 1 117 ? 30.127 -18.462 -5.046  1.00 15.24 ?  117 ASN   B HD21 1 
ATOM   5830 H  HD22 . ASN   B 1 117 ? 30.192 -17.214 -4.236  1.00 15.24 ?  117 ASN   B HD22 1 
ATOM   5831 N  N    . GLN   B 1 118 ? 34.279 -13.455 -5.509  1.00 12.34 ?  118 GLN   B N    1 
ATOM   5832 C  CA   . GLN   B 1 118 ? 34.710 -12.068 -5.644  1.00 12.91 ?  118 GLN   B CA   1 
ATOM   5833 C  C    . GLN   B 1 118 ? 35.779 -11.876 -6.714  1.00 13.44 ?  118 GLN   B C    1 
ATOM   5834 O  O    . GLN   B 1 118 ? 36.255 -10.751 -6.895  1.00 14.86 ?  118 GLN   B O    1 
ATOM   5835 C  CB   . GLN   B 1 118 ? 35.191 -11.542 -4.287  1.00 13.46 ?  118 GLN   B CB   1 
ATOM   5836 C  CG   . GLN   B 1 118 ? 34.097 -11.574 -3.219  1.00 13.72 ?  118 GLN   B CG   1 
ATOM   5837 C  CD   . GLN   B 1 118 ? 32.921 -10.671 -3.559  1.00 13.52 ?  118 GLN   B CD   1 
ATOM   5838 O  OE1  . GLN   B 1 118 ? 33.111 -9.535  -4.006  1.00 14.24 ?  118 GLN   B OE1  1 
ATOM   5839 N  NE2  . GLN   B 1 118 ? 31.709 -11.165 -3.350  1.00 13.98 ?  118 GLN   B NE2  1 
ATOM   5840 H  H    . GLN   B 1 118 ? 34.703 -13.885 -4.897  1.00 14.83 ?  118 GLN   B H    1 
ATOM   5841 H  HA   . GLN   B 1 118 ? 33.951 -11.533 -5.912  1.00 15.51 ?  118 GLN   B HA   1 
ATOM   5842 H  HB2  . GLN   B 1 118 ? 35.934 -12.082 -3.979  1.00 16.17 ?  118 GLN   B HB2  1 
ATOM   5843 H  HB3  . GLN   B 1 118 ? 35.479 -10.616 -4.388  1.00 16.17 ?  118 GLN   B HB3  1 
ATOM   5844 H  HG2  . GLN   B 1 118 ? 33.770 -12.485 -3.136  1.00 16.48 ?  118 GLN   B HG2  1 
ATOM   5845 H  HG3  . GLN   B 1 118 ? 34.474 -11.280 -2.374  1.00 16.48 ?  118 GLN   B HG3  1 
ATOM   5846 H  HE21 . GLN   B 1 118 ? 31.621 -11.959 -3.030  1.00 16.80 ?  118 GLN   B HE21 1 
ATOM   5847 H  HE22 . GLN   B 1 118 ? 31.022 -10.689 -3.527  1.00 16.80 ?  118 GLN   B HE22 1 
ATOM   5848 N  N    . HIS   B 1 119 ? 36.123 -12.929 -7.455  1.00 12.29 ?  119 HIS   B N    1 
ATOM   5849 C  CA   . HIS   B 1 119 ? 37.177 -12.888 -8.462  1.00 12.37 ?  119 HIS   B CA   1 
ATOM   5850 C  C    . HIS   B 1 119 ? 36.693 -13.609 -9.707  1.00 12.62 ?  119 HIS   B C    1 
ATOM   5851 O  O    . HIS   B 1 119 ? 36.182 -14.725 -9.611  1.00 13.26 ?  119 HIS   B O    1 
ATOM   5852 C  CB   . HIS   B 1 119 ? 38.443 -13.538 -7.905  1.00 12.87 ?  119 HIS   B CB   1 
ATOM   5853 C  CG   . HIS   B 1 119 ? 38.917 -12.859 -6.668  1.00 14.00 ?  119 HIS   B CG   1 
ATOM   5854 N  ND1  . HIS   B 1 119 ? 39.732 -11.749 -6.703  1.00 15.85 ?  119 HIS   B ND1  1 
ATOM   5855 C  CD2  . HIS   B 1 119 ? 38.609 -13.062 -5.366  1.00 15.09 ?  119 HIS   B CD2  1 
ATOM   5856 C  CE1  . HIS   B 1 119 ? 39.937 -11.324 -5.470  1.00 16.77 ?  119 HIS   B CE1  1 
ATOM   5857 N  NE2  . HIS   B 1 119 ? 39.256 -12.093 -4.641  1.00 16.78 ?  119 HIS   B NE2  1 
ATOM   5858 H  H    . HIS   B 1 119 ? 35.741 -13.707 -7.393  1.00 14.77 ?  119 HIS   B H    1 
ATOM   5859 H  HA   . HIS   B 1 119 ? 37.367 -11.964 -8.691  1.00 14.87 ?  119 HIS   B HA   1 
ATOM   5860 H  HB2  . HIS   B 1 119 ? 38.256 -14.465 -7.695  1.00 15.47 ?  119 HIS   B HB2  1 
ATOM   5861 H  HB3  . HIS   B 1 119 ? 39.144 -13.481 -8.574  1.00 15.47 ?  119 HIS   B HB3  1 
ATOM   5862 H  HD2  . HIS   B 1 119 ? 38.059 -13.733 -5.028  1.00 18.13 ?  119 HIS   B HD2  1 
ATOM   5863 H  HE1  . HIS   B 1 119 ? 40.479 -10.611 -5.221  1.00 20.14 ?  119 HIS   B HE1  1 
ATOM   5864 H  HE2  . HIS   B 1 119 ? 39.253 -12.030 -3.781  1.00 20.15 ?  119 HIS   B HE2  1 
ATOM   5865 N  N    A GLU   B 1 120 ? 36.857 -12.984 -10.875 0.56 13.31 ?  120 GLU   B N    1 
ATOM   5866 N  N    B GLU   B 1 120 ? 36.858 -12.977 -10.871 0.44 13.63 ?  120 GLU   B N    1 
ATOM   5867 C  CA   A GLU   B 1 120 ? 36.272 -13.556 -12.084 0.56 14.91 ?  120 GLU   B CA   1 
ATOM   5868 C  CA   B GLU   B 1 120 ? 36.288 -13.539 -12.093 0.44 15.16 ?  120 GLU   B CA   1 
ATOM   5869 C  C    A GLU   B 1 120 ? 36.950 -14.856 -12.502 0.56 13.93 ?  120 GLU   B C    1 
ATOM   5870 C  C    B GLU   B 1 120 ? 36.947 -14.855 -12.486 0.44 14.12 ?  120 GLU   B C    1 
ATOM   5871 O  O    A GLU   B 1 120 ? 36.296 -15.724 -13.093 0.56 14.01 ?  120 GLU   B O    1 
ATOM   5872 O  O    B GLU   B 1 120 ? 36.278 -15.736 -13.039 0.44 14.19 ?  120 GLU   B O    1 
ATOM   5873 C  CB   A GLU   B 1 120 ? 36.289 -12.541 -13.228 0.56 18.99 ?  120 GLU   B CB   1 
ATOM   5874 C  CB   B GLU   B 1 120 ? 36.373 -12.528 -13.237 0.44 18.86 ?  120 GLU   B CB   1 
ATOM   5875 C  CG   A GLU   B 1 120 ? 35.255 -11.438 -13.075 0.56 24.27 ?  120 GLU   B CG   1 
ATOM   5876 C  CG   B GLU   B 1 120 ? 35.463 -11.323 -13.058 0.44 23.43 ?  120 GLU   B CG   1 
ATOM   5877 C  CD   A GLU   B 1 120 ? 35.141 -10.561 -14.304 0.56 28.30 ?  120 GLU   B CD   1 
ATOM   5878 C  CD   B GLU   B 1 120 ? 35.412 -10.444 -14.294 0.44 27.18 ?  120 GLU   B CD   1 
ATOM   5879 O  OE1  A GLU   B 1 120 ? 36.180 -10.281 -14.941 0.56 30.31 ?  120 GLU   B OE1  1 
ATOM   5880 O  OE1  B GLU   B 1 120 ? 36.376 -10.485 -15.090 0.44 29.08 ?  120 GLU   B OE1  1 
ATOM   5881 O  OE2  A GLU   B 1 120 ? 34.006 -10.158 -14.636 0.56 30.68 -1 120 GLU   B OE2  1 
ATOM   5882 O  OE2  B GLU   B 1 120 ? 34.417 -9.711  -14.467 0.44 29.03 -1 120 GLU   B OE2  1 
ATOM   5883 H  H    A GLU   B 1 120 ? 37.291 -12.245 -10.991 0.56 16.00 ?  120 GLU   B H    1 
ATOM   5884 H  H    B GLU   B 1 120 ? 37.286 -12.235 -10.979 0.44 16.38 ?  120 GLU   B H    1 
ATOM   5885 H  HA   A GLU   B 1 120 ? 35.347 -13.764 -11.900 0.56 17.92 ?  120 GLU   B HA   1 
ATOM   5886 H  HA   B GLU   B 1 120 ? 35.353 -13.721 -11.936 0.44 18.22 ?  120 GLU   B HA   1 
ATOM   5887 H  HB2  A GLU   B 1 120 ? 37.162 -12.125 -13.270 0.56 22.81 ?  120 GLU   B HB2  1 
ATOM   5888 H  HB2  B GLU   B 1 120 ? 37.282 -12.200 -13.306 0.44 22.65 ?  120 GLU   B HB2  1 
ATOM   5889 H  HB3  A GLU   B 1 120 ? 36.104 -13.006 -14.061 0.56 22.81 ?  120 GLU   B HB3  1 
ATOM   5890 H  HB3  B GLU   B 1 120 ? 36.119 -12.968 -14.065 0.44 22.65 ?  120 GLU   B HB3  1 
ATOM   5891 H  HG2  A GLU   B 1 120 ? 34.383 -11.837 -12.927 0.56 29.15 ?  120 GLU   B HG2  1 
ATOM   5892 H  HG2  B GLU   B 1 120 ? 34.564 -11.634 -12.849 0.44 28.14 ?  120 GLU   B HG2  1 
ATOM   5893 H  HG3  A GLU   B 1 120 ? 35.497 -10.880 -12.320 0.56 29.15 ?  120 GLU   B HG3  1 
ATOM   5894 H  HG3  B GLU   B 1 120 ? 35.798 -10.776 -12.333 0.44 28.14 ?  120 GLU   B HG3  1 
ATOM   5895 N  N    . VAL   B 1 121 ? 38.242 -15.006 -12.221 1.00 13.33 ?  121 VAL   B N    1 
ATOM   5896 C  CA   . VAL   B 1 121 ? 38.983 -16.217 -12.571 1.00 13.02 ?  121 VAL   B CA   1 
ATOM   5897 C  C    . VAL   B 1 121 ? 40.096 -16.432 -11.552 1.00 12.82 ?  121 VAL   B C    1 
ATOM   5898 O  O    . VAL   B 1 121 ? 40.779 -15.482 -11.152 1.00 13.09 ?  121 VAL   B O    1 
ATOM   5899 C  CB   . VAL   B 1 121 ? 39.503 -16.158 -14.027 1.00 15.22 ?  121 VAL   B CB   1 
ATOM   5900 C  CG1  . VAL   B 1 121 ? 40.354 -14.913 -14.262 1.00 16.51 ?  121 VAL   B CG1  1 
ATOM   5901 C  CG2  . VAL   B 1 121 ? 40.272 -17.427 -14.385 1.00 16.63 ?  121 VAL   B CG2  1 
ATOM   5902 H  H    A VAL   B 1 121 ? 38.727 -14.408 -11.835 0.56 16.02 ?  121 VAL   B H    1 
ATOM   5903 H  H    B VAL   B 1 121 ? 38.731 -14.407 -11.841 0.44 16.02 ?  121 VAL   B H    1 
ATOM   5904 H  HA   . VAL   B 1 121 ? 38.374 -16.969 -12.513 1.00 15.65 ?  121 VAL   B HA   1 
ATOM   5905 H  HB   . VAL   B 1 121 ? 38.739 -16.107 -14.626 1.00 18.29 ?  121 VAL   B HB   1 
ATOM   5906 H  HG11 . VAL   B 1 121 ? 40.683 -14.923 -15.174 1.00 19.84 ?  121 VAL   B HG11 1 
ATOM   5907 H  HG12 . VAL   B 1 121 ? 39.806 -14.124 -14.118 1.00 19.84 ?  121 VAL   B HG12 1 
ATOM   5908 H  HG13 . VAL   B 1 121 ? 41.098 -14.916 -13.641 1.00 19.84 ?  121 VAL   B HG13 1 
ATOM   5909 H  HG21 . VAL   B 1 121 ? 40.472 -17.419 -15.336 1.00 19.98 ?  121 VAL   B HG21 1 
ATOM   5910 H  HG22 . VAL   B 1 121 ? 41.101 -17.450 -13.878 1.00 19.98 ?  121 VAL   B HG22 1 
ATOM   5911 H  HG23 . VAL   B 1 121 ? 39.730 -18.201 -14.169 1.00 19.98 ?  121 VAL   B HG23 1 
ATOM   5912 N  N    . LEU   B 1 122 ? 40.274 -17.686 -11.128 1.00 12.16 ?  122 LEU   B N    1 
ATOM   5913 C  CA   . LEU   B 1 122 ? 41.249 -18.049 -10.104 1.00 11.75 ?  122 LEU   B CA   1 
ATOM   5914 C  C    . LEU   B 1 122 ? 41.901 -19.382 -10.426 1.00 11.29 ?  122 LEU   B C    1 
ATOM   5915 O  O    . LEU   B 1 122 ? 41.243 -20.304 -10.924 1.00 12.73 ?  122 LEU   B O    1 
ATOM   5916 C  CB   . LEU   B 1 122 ? 40.600 -18.269 -8.725  1.00 13.63 ?  122 LEU   B CB   1 
ATOM   5917 C  CG   . LEU   B 1 122 ? 39.561 -17.257 -8.230  1.00 13.69 ?  122 LEU   B CG   1 
ATOM   5918 C  CD1  . LEU   B 1 122 ? 38.161 -17.617 -8.710  1.00 14.25 ?  122 LEU   B CD1  1 
ATOM   5919 C  CD2  . LEU   B 1 122 ? 39.596 -17.158 -6.722  1.00 12.95 ?  122 LEU   B CD2  1 
ATOM   5920 H  H    . LEU   B 1 122 ? 39.836 -18.363 -11.431 1.00 14.61 ?  122 LEU   B H    1 
ATOM   5921 H  HA   . LEU   B 1 122 ? 41.931 -17.364 -10.025 1.00 14.12 ?  122 LEU   B HA   1 
ATOM   5922 H  HB2  . LEU   B 1 122 ? 40.160 -19.133 -8.738  1.00 16.38 ?  122 LEU   B HB2  1 
ATOM   5923 H  HB3  . LEU   B 1 122 ? 41.304 -18.283 -8.061  1.00 16.38 ?  122 LEU   B HB3  1 
ATOM   5924 H  HG   . LEU   B 1 122 ? 39.776 -16.384 -8.590  1.00 16.45 ?  122 LEU   B HG   1 
ATOM   5925 H  HD11 . LEU   B 1 122 ? 37.527 -16.974 -8.351  1.00 17.12 ?  122 LEU   B HD11 1 
ATOM   5926 H  HD12 . LEU   B 1 122 ? 38.140 -17.584 -9.683  1.00 17.12 ?  122 LEU   B HD12 1 
ATOM   5927 H  HD13 . LEU   B 1 122 ? 37.936 -18.508 -8.406  1.00 17.12 ?  122 LEU   B HD13 1 
ATOM   5928 H  HD21 . LEU   B 1 122 ? 38.908 -16.540 -6.425  1.00 15.56 ?  122 LEU   B HD21 1 
ATOM   5929 H  HD22 . LEU   B 1 122 ? 39.435 -18.037 -6.341  1.00 15.56 ?  122 LEU   B HD22 1 
ATOM   5930 H  HD23 . LEU   B 1 122 ? 40.469 -16.835 -6.447  1.00 15.56 ?  122 LEU   B HD23 1 
ATOM   5931 N  N    . LEU   B 1 123 ? 43.185 -19.491 -10.076 1.00 10.83 ?  123 LEU   B N    1 
ATOM   5932 C  CA   . LEU   B 1 123 ? 43.891 -20.761 -9.952  1.00 11.28 ?  123 LEU   B CA   1 
ATOM   5933 C  C    . LEU   B 1 123 ? 43.859 -21.153 -8.478  1.00 10.86 ?  123 LEU   B C    1 
ATOM   5934 O  O    . LEU   B 1 123 ? 44.219 -20.331 -7.626  1.00 11.41 ?  123 LEU   B O    1 
ATOM   5935 C  CB   . LEU   B 1 123 ? 45.343 -20.586 -10.405 1.00 11.91 ?  123 LEU   B CB   1 
ATOM   5936 C  CG   . LEU   B 1 123 ? 46.280 -21.780 -10.168 1.00 12.24 ?  123 LEU   B CG   1 
ATOM   5937 C  CD1  . LEU   B 1 123 ? 45.846 -23.028 -10.931 1.00 13.27 ?  123 LEU   B CD1  1 
ATOM   5938 C  CD2  . LEU   B 1 123 ? 47.693 -21.387 -10.559 1.00 13.28 ?  123 LEU   B CD2  1 
ATOM   5939 H  H    . LEU   B 1 123 ? 43.680 -18.814 -9.879  1.00 13.01 ?  123 LEU   B H    1 
ATOM   5940 H  HA   . LEU   B 1 123 ? 43.455 -21.448 -10.481 1.00 13.56 ?  123 LEU   B HA   1 
ATOM   5941 H  HB2  . LEU   B 1 123 ? 45.336 -20.405 -11.358 1.00 14.31 ?  123 LEU   B HB2  1 
ATOM   5942 H  HB3  . LEU   B 1 123 ? 45.714 -19.824 -9.935  1.00 14.31 ?  123 LEU   B HB3  1 
ATOM   5943 H  HG   . LEU   B 1 123 ? 46.282 -21.992 -9.223  1.00 14.71 ?  123 LEU   B HG   1 
ATOM   5944 H  HD11 . LEU   B 1 123 ? 46.481 -23.737 -10.753 1.00 15.95 ?  123 LEU   B HD11 1 
ATOM   5945 H  HD12 . LEU   B 1 123 ? 44.962 -23.290 -10.628 1.00 15.95 ?  123 LEU   B HD12 1 
ATOM   5946 H  HD13 . LEU   B 1 123 ? 45.826 -22.826 -11.878 1.00 15.95 ?  123 LEU   B HD13 1 
ATOM   5947 H  HD21 . LEU   B 1 123 ? 48.278 -22.142 -10.410 1.00 15.95 ?  123 LEU   B HD21 1 
ATOM   5948 H  HD22 . LEU   B 1 123 ? 47.699 -21.139 -11.498 1.00 15.95 ?  123 LEU   B HD22 1 
ATOM   5949 H  HD23 . LEU   B 1 123 ? 47.971 -20.634 -10.017 1.00 15.95 ?  123 LEU   B HD23 1 
ATOM   5950 N  N    . ALA   B 1 124 ? 43.425 -22.385 -8.165  1.00 10.85 ?  124 ALA   B N    1 
ATOM   5951 C  CA   . ALA   B 1 124 ? 43.173 -22.705 -6.766  1.00 11.19 ?  124 ALA   B CA   1 
ATOM   5952 C  C    . ALA   B 1 124 ? 43.444 -24.164 -6.435  1.00 10.70 ?  124 ALA   B C    1 
ATOM   5953 O  O    . ALA   B 1 124 ? 43.305 -25.039 -7.300  1.00 11.41 ?  124 ALA   B O    1 
ATOM   5954 C  CB   . ALA   B 1 124 ? 41.716 -22.401 -6.381  1.00 11.61 ?  124 ALA   B CB   1 
ATOM   5955 H  H    . ALA   B 1 124 ? 43.259 -23.024 -8.725  1.00 13.04 ?  124 ALA   B H    1 
ATOM   5956 H  HA   . ALA   B 1 124 ? 43.745 -22.154 -6.220  1.00 13.45 ?  124 ALA   B HA   1 
ATOM   5957 H  HB1  . ALA   B 1 124 ? 41.576 -22.620 -5.446  1.00 13.96 ?  124 ALA   B HB1  1 
ATOM   5958 H  HB2  . ALA   B 1 124 ? 41.543 -21.452 -6.522  1.00 13.96 ?  124 ALA   B HB2  1 
ATOM   5959 H  HB3  . ALA   B 1 124 ? 41.118 -22.926 -6.936  1.00 13.96 ?  124 ALA   B HB3  1 
ATOM   5960 N  N    . PRO   B 1 125 ? 43.746 -24.455 -5.174  1.00 11.12 ?  125 PRO   B N    1 
ATOM   5961 C  CA   . PRO   B 1 125 ? 43.686 -25.822 -4.657  1.00 11.85 ?  125 PRO   B CA   1 
ATOM   5962 C  C    . PRO   B 1 125 ? 42.285 -26.093 -4.107  1.00 12.02 ?  125 PRO   B C    1 
ATOM   5963 O  O    . PRO   B 1 125 ? 41.483 -25.177 -3.918  1.00 12.42 ?  125 PRO   B O    1 
ATOM   5964 C  CB   . PRO   B 1 125 ? 44.679 -25.756 -3.495  1.00 12.82 ?  125 PRO   B CB   1 
ATOM   5965 C  CG   . PRO   B 1 125 ? 44.438 -24.372 -2.919  1.00 12.85 ?  125 PRO   B CG   1 
ATOM   5966 C  CD   . PRO   B 1 125 ? 44.080 -23.490 -4.113  1.00 12.01 ?  125 PRO   B CD   1 
ATOM   5967 H  HA   . PRO   B 1 125 ? 43.956 -26.490 -5.314  1.00 14.25 ?  125 PRO   B HA   1 
ATOM   5968 H  HB2  . PRO   B 1 125 ? 44.476 -26.445 -2.839  1.00 15.41 ?  125 PRO   B HB2  1 
ATOM   5969 H  HB3  . PRO   B 1 125 ? 45.589 -25.844 -3.820  1.00 15.41 ?  125 PRO   B HB3  1 
ATOM   5970 H  HG2  . PRO   B 1 125 ? 43.704 -24.399 -2.285  1.00 15.45 ?  125 PRO   B HG2  1 
ATOM   5971 H  HG3  . PRO   B 1 125 ? 45.248 -24.049 -2.483  1.00 15.45 ?  125 PRO   B HG3  1 
ATOM   5972 H  HD2  . PRO   B 1 125 ? 43.316 -22.936 -3.913  1.00 14.43 ?  125 PRO   B HD2  1 
ATOM   5973 H  HD3  . PRO   B 1 125 ? 44.851 -22.952 -4.376  1.00 14.43 ?  125 PRO   B HD3  1 
ATOM   5974 N  N    . LEU   B 1 126 ? 42.023 -27.363 -3.792  1.00 12.53 ?  126 LEU   B N    1 
ATOM   5975 C  CA   . LEU   B 1 126 ? 40.800 -27.721 -3.081  1.00 12.92 ?  126 LEU   B CA   1 
ATOM   5976 C  C    . LEU   B 1 126 ? 40.914 -27.322 -1.616  1.00 13.24 ?  126 LEU   B C    1 
ATOM   5977 O  O    . LEU   B 1 126 ? 41.803 -27.790 -0.900  1.00 15.29 ?  126 LEU   B O    1 
ATOM   5978 C  CB   . LEU   B 1 126 ? 40.545 -29.216 -3.193  1.00 14.57 ?  126 LEU   B CB   1 
ATOM   5979 C  CG   . LEU   B 1 126 ? 40.017 -29.710 -4.543  1.00 15.44 ?  126 LEU   B CG   1 
ATOM   5980 C  CD1  . LEU   B 1 126 ? 40.062 -31.215 -4.622  1.00 17.44 ?  126 LEU   B CD1  1 
ATOM   5981 C  CD2  . LEU   B 1 126 ? 38.601 -29.207 -4.800  1.00 15.90 ?  126 LEU   B CD2  1 
ATOM   5982 H  H    . LEU   B 1 126 ? 42.545 -28.026 -3.965  1.00 15.06 ?  126 LEU   B H    1 
ATOM   5983 H  HA   . LEU   B 1 126 ? 40.056 -27.241 -3.473  1.00 15.53 ?  126 LEU   B HA   1 
ATOM   5984 H  HB2  . LEU   B 1 126 ? 41.377 -29.679 -3.022  1.00 17.51 ?  126 LEU   B HB2  1 
ATOM   5985 H  HB3  . LEU   B 1 126 ? 39.892 -29.460 -2.521  1.00 17.51 ?  126 LEU   B HB3  1 
ATOM   5986 H  HG   . LEU   B 1 126 ? 40.587 -29.351 -5.246  1.00 18.55 ?  126 LEU   B HG   1 
ATOM   5987 H  HD11 . LEU   B 1 126 ? 39.723 -31.493 -5.487  1.00 20.95 ?  126 LEU   B HD11 1 
ATOM   5988 H  HD12 . LEU   B 1 126 ? 40.978 -31.508 -4.513  1.00 20.95 ?  126 LEU   B HD12 1 
ATOM   5989 H  HD13 . LEU   B 1 126 ? 39.508 -31.582 -3.915  1.00 20.95 ?  126 LEU   B HD13 1 
ATOM   5990 H  HD21 . LEU   B 1 126 ? 38.264 -29.616 -5.612  1.00 19.10 ?  126 LEU   B HD21 1 
ATOM   5991 H  HD22 . LEU   B 1 126 ? 38.039 -29.449 -4.049  1.00 19.10 ?  126 LEU   B HD22 1 
ATOM   5992 H  HD23 . LEU   B 1 126 ? 38.616 -28.240 -4.902  1.00 19.10 ?  126 LEU   B HD23 1 
ATOM   5993 N  N    . LEU   B 1 127 ? 39.987 -26.492 -1.156  1.00 12.97 ?  127 LEU   B N    1 
ATOM   5994 C  CA   . LEU   B 1 127 ? 40.040 -25.998 0.211   1.00 13.52 ?  127 LEU   B CA   1 
ATOM   5995 C  C    . LEU   B 1 127 ? 39.754 -27.112 1.209   1.00 13.54 ?  127 LEU   B C    1 
ATOM   5996 O  O    . LEU   B 1 127 ? 38.926 -28.000 0.975   1.00 13.86 ?  127 LEU   B O    1 
ATOM   5997 C  CB   . LEU   B 1 127 ? 39.026 -24.877 0.417   1.00 14.25 ?  127 LEU   B CB   1 
ATOM   5998 C  CG   . LEU   B 1 127 ? 39.217 -23.619 -0.428  1.00 14.67 ?  127 LEU   B CG   1 
ATOM   5999 C  CD1  . LEU   B 1 127 ? 38.104 -22.639 -0.115  1.00 15.14 ?  127 LEU   B CD1  1 
ATOM   6000 C  CD2  . LEU   B 1 127 ? 40.587 -22.997 -0.189  1.00 15.23 ?  127 LEU   B CD2  1 
ATOM   6001 H  H    . LEU   B 1 127 ? 39.322 -26.185 -1.618  1.00 15.58 ?  127 LEU   B H    1 
ATOM   6002 H  HA   . LEU   B 1 127 ? 40.927 -25.638 0.386   1.00 16.24 ?  127 LEU   B HA   1 
ATOM   6003 H  HB2  . LEU   B 1 127 ? 38.141 -25.228 0.216   1.00 17.12 ?  127 LEU   B HB2  1 
ATOM   6004 H  HB3  . LEU   B 1 127 ? 39.055 -24.607 1.348   1.00 17.12 ?  127 LEU   B HB3  1 
ATOM   6005 H  HG   . LEU   B 1 127 ? 39.147 -23.854 -1.365  1.00 17.63 ?  127 LEU   B HG   1 
ATOM   6006 H  HD11 . LEU   B 1 127 ? 38.234 -21.832 -0.645  1.00 18.19 ?  127 LEU   B HD11 1 
ATOM   6007 H  HD12 . LEU   B 1 127 ? 37.249 -23.039 -0.332  1.00 18.19 ?  127 LEU   B HD12 1 
ATOM   6008 H  HD13 . LEU   B 1 127 ? 38.134 -22.413 0.830   1.00 18.19 ?  127 LEU   B HD13 1 
ATOM   6009 H  HD21 . LEU   B 1 127 ? 40.627 -22.136 -0.628  1.00 18.30 ?  127 LEU   B HD21 1 
ATOM   6010 H  HD22 . LEU   B 1 127 ? 40.724 -22.890 0.767   1.00 18.30 ?  127 LEU   B HD22 1 
ATOM   6011 H  HD23 . LEU   B 1 127 ? 41.268 -23.587 -0.552  1.00 18.30 ?  127 LEU   B HD23 1 
ATOM   6012 N  N    . SER   B 1 128 ? 40.436 -27.031 2.343   1.00 13.61 ?  128 SER   B N    1 
ATOM   6013 C  CA   . SER   B 1 128 ? 40.310 -27.933 3.477   1.00 14.35 ?  128 SER   B CA   1 
ATOM   6014 C  C    . SER   B 1 128 ? 40.792 -29.347 3.176   1.00 16.02 ?  128 SER   B C    1 
ATOM   6015 O  O    . SER   B 1 128 ? 40.687 -30.213 4.043   1.00 17.45 ?  128 SER   B O    1 
ATOM   6016 C  CB   . SER   B 1 128 ? 38.902 -27.925 4.095   1.00 14.65 ?  128 SER   B CB   1 
ATOM   6017 O  OG   . SER   B 1 128 ? 38.612 -26.640 4.645   1.00 15.20 ?  128 SER   B OG   1 
ATOM   6018 H  H    . SER   B 1 128 ? 41.018 -26.410 2.483   1.00 16.35 ?  128 SER   B H    1 
ATOM   6019 H  HA   . SER   B 1 128 ? 40.898 -27.594 4.161   1.00 17.24 ?  128 SER   B HA   1 
ATOM   6020 H  HB2  . SER   B 1 128 ? 38.245 -28.140 3.415   1.00 17.60 ?  128 SER   B HB2  1 
ATOM   6021 H  HB3  . SER   B 1 128 ? 38.866 -28.592 4.808   1.00 17.60 ?  128 SER   B HB3  1 
ATOM   6022 H  HG   . SER   B 1 128 ? 39.179 -26.449 5.237   1.00 18.26 ?  128 SER   B HG   1 
ATOM   6023 N  N    . ALA   B 1 129 ? 41.367 -29.590 1.993   1.00 16.82 ?  129 ALA   B N    1 
ATOM   6024 C  CA   . ALA   B 1 129 ? 41.907 -30.891 1.634   1.00 17.85 ?  129 ALA   B CA   1 
ATOM   6025 C  C    . ALA   B 1 129 ? 43.312 -31.060 2.202   1.00 16.50 ?  129 ALA   B C    1 
ATOM   6026 O  O    . ALA   B 1 129 ? 43.871 -30.169 2.854   1.00 16.28 ?  129 ALA   B O    1 
ATOM   6027 C  CB   . ALA   B 1 129 ? 41.936 -31.047 0.114   1.00 20.15 ?  129 ALA   B CB   1 
ATOM   6028 H  H    . ALA   B 1 129 ? 41.452 -29.001 1.364   1.00 20.20 ?  129 ALA   B H    1 
ATOM   6029 H  HA   . ALA   B 1 129 ? 41.340 -31.584 1.997   1.00 21.45 ?  129 ALA   B HA   1 
ATOM   6030 H  HB1  . ALA   B 1 129 ? 42.286 -31.926 -0.108  1.00 24.20 ?  129 ALA   B HB1  1 
ATOM   6031 H  HB2  . ALA   B 1 129 ? 41.036 -30.954 -0.234  1.00 24.20 ?  129 ALA   B HB2  1 
ATOM   6032 H  HB3  . ALA   B 1 129 ? 42.509 -30.361 -0.266  1.00 24.20 ?  129 ALA   B HB3  1 
ATOM   6033 N  N    . GLY   B 1 130 ? 43.890 -32.229 1.939   1.00 16.53 ?  130 GLY   B N    1 
ATOM   6034 C  CA   . GLY   B 1 130 ? 45.279 -32.456 2.288   1.00 17.21 ?  130 GLY   B CA   1 
ATOM   6035 C  C    . GLY   B 1 130 ? 45.491 -32.366 3.779   1.00 16.93 ?  130 GLY   B C    1 
ATOM   6036 O  O    . GLY   B 1 130 ? 44.786 -33.006 4.573   1.00 17.70 ?  130 GLY   B O    1 
ATOM   6037 H  H    . GLY   B 1 130 ? 43.508 -32.895 1.549   1.00 19.86 ?  130 GLY   B H    1 
ATOM   6038 H  HA2  . GLY   B 1 130 ? 45.552 -33.341 1.989   1.00 20.67 ?  130 GLY   B HA2  1 
ATOM   6039 H  HA3  . GLY   B 1 130 ? 45.843 -31.799 1.851   1.00 20.67 ?  130 GLY   B HA3  1 
ATOM   6040 N  N    . ILE   B 1 131 ? 46.477 -31.549 4.170   1.00 17.31 ?  131 ILE   B N    1 
ATOM   6041 C  CA   . ILE   B 1 131 ? 46.846 -31.426 5.570   1.00 18.43 ?  131 ILE   B CA   1 
ATOM   6042 C  C    . ILE   B 1 131 ? 45.733 -30.832 6.418   1.00 17.66 ?  131 ILE   B C    1 
ATOM   6043 O  O    . ILE   B 1 131 ? 45.806 -30.901 7.647   1.00 19.28 ?  131 ILE   B O    1 
ATOM   6044 C  CB   . ILE   B 1 131 ? 48.172 -30.648 5.767   1.00 20.26 ?  131 ILE   B CB   1 
ATOM   6045 C  CG1  . ILE   B 1 131 ? 48.005 -29.165 5.409   1.00 21.04 ?  131 ILE   B CG1  1 
ATOM   6046 C  CG2  . ILE   B 1 131 ? 49.289 -31.276 4.944   1.00 21.31 ?  131 ILE   B CG2  1 
ATOM   6047 C  CD1  . ILE   B 1 131 ? 49.221 -28.314 5.729   1.00 22.45 ?  131 ILE   B CD1  1 
ATOM   6048 H  H    . ILE   B 1 131 ? 46.935 -31.047 3.633   1.00 20.80 ?  131 ILE   B H    1 
ATOM   6049 H  HA   . ILE   B 1 131 ? 46.997 -32.321 5.903   1.00 22.13 ?  131 ILE   B HA   1 
ATOM   6050 H  HB   . ILE   B 1 131 ? 48.410 -30.708 6.706   1.00 24.34 ?  131 ILE   B HB   1 
ATOM   6051 H  HG12 . ILE   B 1 131 ? 47.828 -29.096 4.459   1.00 25.27 ?  131 ILE   B HG12 1 
ATOM   6052 H  HG13 . ILE   B 1 131 ? 47.253 -28.799 5.907   1.00 25.27 ?  131 ILE   B HG13 1 
ATOM   6053 H  HG21 . ILE   B 1 131 ? 50.130 -30.873 5.204   1.00 25.59 ?  131 ILE   B HG21 1 
ATOM   6054 H  HG22 . ILE   B 1 131 ? 49.306 -32.228 5.115   1.00 25.59 ?  131 ILE   B HG22 1 
ATOM   6055 H  HG23 . ILE   B 1 131 ? 49.114 -31.109 4.004   1.00 25.59 ?  131 ILE   B HG23 1 
ATOM   6056 H  HD11 . ILE   B 1 131 ? 48.999 -27.383 5.579   1.00 26.96 ?  131 ILE   B HD11 1 
ATOM   6057 H  HD12 . ILE   B 1 131 ? 49.464 -28.452 6.659   1.00 26.96 ?  131 ILE   B HD12 1 
ATOM   6058 H  HD13 . ILE   B 1 131 ? 49.951 -28.581 5.152   1.00 26.96 ?  131 ILE   B HD13 1 
ATOM   6059 N  N    . PHE   B 1 132 ? 44.704 -30.247 5.796   1.00 16.59 ?  132 PHE   B N    1 
ATOM   6060 C  CA   . PHE   B 1 132 ? 43.557 -29.736 6.536   1.00 16.95 ?  132 PHE   B CA   1 
ATOM   6061 C  C    . PHE   B 1 132 ? 42.536 -30.819 6.877   1.00 18.28 ?  132 PHE   B C    1 
ATOM   6062 O  O    . PHE   B 1 132 ? 41.644 -30.564 7.692   1.00 20.17 ?  132 PHE   B O    1 
ATOM   6063 C  CB   . PHE   B 1 132 ? 42.870 -28.609 5.756   1.00 16.03 ?  132 PHE   B CB   1 
ATOM   6064 C  CG   . PHE   B 1 132 ? 43.566 -27.268 5.851   1.00 15.70 ?  132 PHE   B CG   1 
ATOM   6065 C  CD1  . PHE   B 1 132 ? 44.860 -27.092 5.389   1.00 17.11 ?  132 PHE   B CD1  1 
ATOM   6066 C  CD2  . PHE   B 1 132 ? 42.889 -26.165 6.359   1.00 15.28 ?  132 PHE   B CD2  1 
ATOM   6067 C  CE1  . PHE   B 1 132 ? 45.481 -25.852 5.468   1.00 17.14 ?  132 PHE   B CE1  1 
ATOM   6068 C  CE2  . PHE   B 1 132 ? 43.498 -24.920 6.432   1.00 15.88 ?  132 PHE   B CE2  1 
ATOM   6069 C  CZ   . PHE   B 1 132 ? 44.793 -24.768 5.990   1.00 16.62 ?  132 PHE   B CZ   1 
ATOM   6070 H  H    . PHE   B 1 132 ? 44.649 -30.142 4.945   1.00 19.92 ?  132 PHE   B H    1 
ATOM   6071 H  HA   . PHE   B 1 132 ? 43.874 -29.366 7.372   1.00 20.36 ?  132 PHE   B HA   1 
ATOM   6072 H  HB2  . PHE   B 1 132 ? 42.842 -28.858 4.822   1.00 19.26 ?  132 PHE   B HB2  1 
ATOM   6073 H  HB3  . PHE   B 1 132 ? 41.968 -28.503 6.098   1.00 19.26 ?  132 PHE   B HB3  1 
ATOM   6074 H  HD1  . PHE   B 1 132 ? 45.328 -27.822 5.046   1.00 20.55 ?  132 PHE   B HD1  1 
ATOM   6075 H  HD2  . PHE   B 1 132 ? 42.014 -26.263 6.665   1.00 18.36 ?  132 PHE   B HD2  1 
ATOM   6076 H  HE1  . PHE   B 1 132 ? 46.358 -25.749 5.169   1.00 20.59 ?  132 PHE   B HE1  1 
ATOM   6077 H  HE2  . PHE   B 1 132 ? 43.037 -24.192 6.790   1.00 19.07 ?  132 PHE   B HE2  1 
ATOM   6078 H  HZ   . PHE   B 1 132 ? 45.210 -23.931 6.044   1.00 19.97 ?  132 PHE   B HZ   1 
ATOM   6079 N  N    . GLY   B 1 133 ? 42.626 -32.010 6.273   1.00 18.05 ?  133 GLY   B N    1 
ATOM   6080 C  CA   . GLY   B 1 133 ? 41.920 -33.176 6.773   1.00 18.96 ?  133 GLY   B CA   1 
ATOM   6081 C  C    . GLY   B 1 133 ? 40.520 -33.438 6.250   1.00 19.91 ?  133 GLY   B C    1 
ATOM   6082 O  O    . GLY   B 1 133 ? 39.933 -34.454 6.633   1.00 21.59 ?  133 GLY   B O    1 
ATOM   6083 H  H    . GLY   B 1 133 ? 43.096 -32.160 5.565   1.00 21.68 ?  133 GLY   B H    1 
ATOM   6084 H  HA2  . GLY   B 1 133 ? 42.458 -33.961 6.583   1.00 22.77 ?  133 GLY   B HA2  1 
ATOM   6085 H  HA3  . GLY   B 1 133 ? 41.844 -33.096 7.733   1.00 22.77 ?  133 GLY   B HA3  1 
ATOM   6086 N  N    . ALA   B 1 134 ? 39.957 -32.576 5.410   1.00 18.79 ?  134 ALA   B N    1 
ATOM   6087 C  CA   . ALA   B 1 134 ? 38.633 -32.865 4.878   1.00 18.66 ?  134 ALA   B CA   1 
ATOM   6088 C  C    . ALA   B 1 134 ? 38.729 -33.837 3.705   1.00 18.68 ?  134 ALA   B C    1 
ATOM   6089 O  O    . ALA   B 1 134 ? 39.787 -34.011 3.092   1.00 19.48 ?  134 ALA   B O    1 
ATOM   6090 C  CB   . ALA   B 1 134 ? 37.929 -31.582 4.438   1.00 18.91 ?  134 ALA   B CB   1 
ATOM   6091 H  H    . ALA   B 1 134 ? 40.301 -31.831 5.152   1.00 22.56 ?  134 ALA   B H    1 
ATOM   6092 H  HA   . ALA   B 1 134 ? 38.095 -33.280 5.572   1.00 22.42 ?  134 ALA   B HA   1 
ATOM   6093 H  HB1  . ALA   B 1 134 ? 37.041 -31.804 4.116   1.00 22.72 ?  134 ALA   B HB1  1 
ATOM   6094 H  HB2  . ALA   B 1 134 ? 37.863 -30.982 5.198   1.00 22.72 ?  134 ALA   B HB2  1 
ATOM   6095 H  HB3  . ALA   B 1 134 ? 38.443 -31.165 3.731   1.00 22.72 ?  134 ALA   B HB3  1 
ATOM   6096 N  N    . ASP   B 1 135 ? 37.603 -34.475 3.406   1.00 19.34 ?  135 ASP   B N    1 
ATOM   6097 C  CA   . ASP   B 1 135 ? 37.521 -35.359 2.253   1.00 20.17 ?  135 ASP   B CA   1 
ATOM   6098 C  C    . ASP   B 1 135 ? 37.606 -34.517 0.986   1.00 18.53 ?  135 ASP   B C    1 
ATOM   6099 O  O    . ASP   B 1 135 ? 36.739 -33.655 0.764   1.00 18.38 ?  135 ASP   B O    1 
ATOM   6100 C  CB   . ASP   B 1 135 ? 36.197 -36.119 2.299   1.00 21.88 ?  135 ASP   B CB   1 
ATOM   6101 C  CG   . ASP   B 1 135 ? 36.050 -37.126 1.168   1.00 23.59 ?  135 ASP   B CG   1 
ATOM   6102 O  OD1  . ASP   B 1 135 ? 36.916 -37.159 0.270   1.00 23.59 ?  135 ASP   B OD1  1 
ATOM   6103 O  OD2  . ASP   B 1 135 ? 35.064 -37.898 1.188   1.00 26.63 -1 135 ASP   B OD2  1 
ATOM   6104 H  H    . ASP   B 1 135 ? 36.871 -34.406 3.851   1.00 23.23 ?  135 ASP   B H    1 
ATOM   6105 H  HA   . ASP   B 1 135 ? 38.249 -35.998 2.282   1.00 24.22 ?  135 ASP   B HA   1 
ATOM   6106 H  HB2  . ASP   B 1 135 ? 36.144 -36.600 3.140   1.00 26.28 ?  135 ASP   B HB2  1 
ATOM   6107 H  HB3  . ASP   B 1 135 ? 35.470 -35.487 2.229   1.00 26.28 ?  135 ASP   B HB3  1 
ATOM   6108 N  N    . PRO   B 1 136 ? 38.614 -34.718 0.134   1.00 18.56 ?  136 PRO   B N    1 
ATOM   6109 C  CA   . PRO   B 1 136 ? 38.698 -33.904 -1.088  1.00 17.55 ?  136 PRO   B CA   1 
ATOM   6110 C  C    . PRO   B 1 136 ? 37.497 -34.063 -2.003  1.00 16.96 ?  136 PRO   B C    1 
ATOM   6111 O  O    . PRO   B 1 136 ? 37.164 -33.120 -2.728  1.00 15.96 ?  136 PRO   B O    1 
ATOM   6112 C  CB   . PRO   B 1 136 ? 40.008 -34.373 -1.740  1.00 18.45 ?  136 PRO   B CB   1 
ATOM   6113 C  CG   . PRO   B 1 136 ? 40.231 -35.761 -1.174  1.00 20.03 ?  136 PRO   B CG   1 
ATOM   6114 C  CD   . PRO   B 1 136 ? 39.724 -35.680 0.235   1.00 19.59 ?  136 PRO   B CD   1 
ATOM   6115 H  HA   . PRO   B 1 136 ? 38.784 -32.966 -0.863  1.00 21.08 ?  136 PRO   B HA   1 
ATOM   6116 H  HB2  . PRO   B 1 136 ? 39.910 -34.406 -2.706  1.00 22.17 ?  136 PRO   B HB2  1 
ATOM   6117 H  HB3  . PRO   B 1 136 ? 40.733 -33.778 -1.489  1.00 22.17 ?  136 PRO   B HB3  1 
ATOM   6118 H  HG2  . PRO   B 1 136 ? 39.720 -36.414 -1.681  1.00 24.05 ?  136 PRO   B HG2  1 
ATOM   6119 H  HG3  . PRO   B 1 136 ? 41.176 -35.980 -1.185  1.00 24.05 ?  136 PRO   B HG3  1 
ATOM   6120 H  HD2  . PRO   B 1 136 ? 39.400 -36.545 0.528   1.00 23.53 ?  136 PRO   B HD2  1 
ATOM   6121 H  HD3  . PRO   B 1 136 ? 40.415 -35.337 0.828   1.00 23.53 ?  136 PRO   B HD3  1 
ATOM   6122 N  N    . ILE   B 1 137 ? 36.840 -35.228 -1.992  1.00 17.47 ?  137 ILE   B N    1 
ATOM   6123 C  CA   . ILE   B 1 137 ? 35.617 -35.402 -2.773  1.00 18.05 ?  137 ILE   B CA   1 
ATOM   6124 C  C    . ILE   B 1 137 ? 34.542 -34.437 -2.293  1.00 17.18 ?  137 ILE   B C    1 
ATOM   6125 O  O    . ILE   B 1 137 ? 33.822 -33.824 -3.095  1.00 16.81 ?  137 ILE   B O    1 
ATOM   6126 C  CB   . ILE   B 1 137 ? 35.145 -36.870 -2.703  1.00 19.95 ?  137 ILE   B CB   1 
ATOM   6127 C  CG1  . ILE   B 1 137 ? 36.153 -37.776 -3.413  1.00 21.84 ?  137 ILE   B CG1  1 
ATOM   6128 C  CG2  . ILE   B 1 137 ? 33.740 -37.021 -3.295  1.00 20.29 ?  137 ILE   B CG2  1 
ATOM   6129 C  CD1  . ILE   B 1 137 ? 35.839 -39.259 -3.301  1.00 24.09 ?  137 ILE   B CD1  1 
ATOM   6130 H  H    . ILE   B 1 137 ? 37.084 -35.928 -1.554  1.00 20.98 ?  137 ILE   B H    1 
ATOM   6131 H  HA   . ILE   B 1 137 ? 35.804 -35.200 -3.704  1.00 21.68 ?  137 ILE   B HA   1 
ATOM   6132 H  HB   . ILE   B 1 137 ? 35.107 -37.133 -1.774  1.00 23.96 ?  137 ILE   B HB   1 
ATOM   6133 H  HG12 . ILE   B 1 137 ? 36.173 -37.557 -4.356  1.00 26.23 ?  137 ILE   B HG12 1 
ATOM   6134 H  HG13 . ILE   B 1 137 ? 37.030 -37.639 -3.023  1.00 26.23 ?  137 ILE   B HG13 1 
ATOM   6135 H  HG21 . ILE   B 1 137 ? 33.481 -37.957 -3.288  1.00 24.37 ?  137 ILE   B HG21 1 
ATOM   6136 H  HG22 . ILE   B 1 137 ? 33.109 -36.519 -2.759  1.00 24.37 ?  137 ILE   B HG22 1 
ATOM   6137 H  HG23 . ILE   B 1 137 ? 33.741 -36.689 -4.205  1.00 24.37 ?  137 ILE   B HG23 1 
ATOM   6138 H  HD11 . ILE   B 1 137 ? 36.445 -39.744 -3.880  1.00 28.93 ?  137 ILE   B HD11 1 
ATOM   6139 H  HD12 . ILE   B 1 137 ? 35.960 -39.545 -2.380  1.00 28.93 ?  137 ILE   B HD12 1 
ATOM   6140 H  HD13 . ILE   B 1 137 ? 34.927 -39.430 -3.583  1.00 28.93 ?  137 ILE   B HD13 1 
ATOM   6141 N  N    . HIS   B 1 138 ? 34.421 -34.281 -0.977  1.00 17.62 ?  138 HIS   B N    1 
ATOM   6142 C  CA   . HIS   B 1 138 ? 33.471 -33.315 -0.441  1.00 17.84 ?  138 HIS   B CA   1 
ATOM   6143 C  C    . HIS   B 1 138 ? 33.880 -31.887 -0.771  1.00 16.63 ?  138 HIS   B C    1 
ATOM   6144 O  O    . HIS   B 1 138 ? 33.028 -31.043 -1.068  1.00 17.49 ?  138 HIS   B O    1 
ATOM   6145 C  CB   . HIS   B 1 138 ? 33.364 -33.487 1.066   1.00 19.38 ?  138 HIS   B CB   1 
ATOM   6146 C  CG   . HIS   B 1 138 ? 32.440 -32.504 1.703   1.00 20.59 ?  138 HIS   B CG   1 
ATOM   6147 N  ND1  . HIS   B 1 138 ? 31.101 -32.432 1.385   1.00 22.53 ?  138 HIS   B ND1  1 
ATOM   6148 C  CD2  . HIS   B 1 138 ? 32.665 -31.530 2.615   1.00 21.16 ?  138 HIS   B CD2  1 
ATOM   6149 C  CE1  . HIS   B 1 138 ? 30.537 -31.467 2.088   1.00 22.65 ?  138 HIS   B CE1  1 
ATOM   6150 N  NE2  . HIS   B 1 138 ? 31.464 -30.903 2.842   1.00 21.71 ?  138 HIS   B NE2  1 
ATOM   6151 H  H    . HIS   B 1 138 ? 34.876 -34.710 -0.385  1.00 21.17 ?  138 HIS   B H    1 
ATOM   6152 H  HA   . HIS   B 1 138 ? 32.599 -33.484 -0.830  1.00 21.43 ?  138 HIS   B HA   1 
ATOM   6153 H  HB2  . HIS   B 1 138 ? 33.029 -34.377 1.258   1.00 23.28 ?  138 HIS   B HB2  1 
ATOM   6154 H  HB3  . HIS   B 1 138 ? 34.240 -33.370 1.459   1.00 23.28 ?  138 HIS   B HB3  1 
ATOM   6155 H  HD1  . HIS   B 1 138 ? 30.695 -32.942 0.821   1.00 27.05 ?  138 HIS   B HD1  1 
ATOM   6156 H  HD2  . HIS   B 1 138 ? 33.471 -31.332 3.026   1.00 25.42 ?  138 HIS   B HD2  1 
ATOM   6157 H  HE1  . HIS   B 1 138 ? 29.634 -31.230 2.057   1.00 27.20 ?  138 HIS   B HE1  1 
ATOM   6158 N  N    . SER   B 1 139 ? 35.174 -31.587 -0.707  1.00 16.08 ?  139 SER   B N    1 
ATOM   6159 C  CA   . SER   B 1 139 ? 35.610 -30.237 -1.028  1.00 15.36 ?  139 SER   B CA   1 
ATOM   6160 C  C    . SER   B 1 139 ? 35.277 -29.888 -2.469  1.00 14.62 ?  139 SER   B C    1 
ATOM   6161 O  O    . SER   B 1 139 ? 34.827 -28.773 -2.750  1.00 14.61 ?  139 SER   B O    1 
ATOM   6162 C  CB   . SER   B 1 139 ? 37.103 -30.093 -0.754  1.00 15.63 ?  139 SER   B CB   1 
ATOM   6163 O  OG   . SER   B 1 139 ? 37.521 -28.759 -0.996  1.00 15.80 ?  139 SER   B OG   1 
ATOM   6164 H  H    . SER   B 1 139 ? 35.802 -32.133 -0.495  1.00 19.31 ?  139 SER   B H    1 
ATOM   6165 H  HA   . SER   B 1 139 ? 35.135 -29.612 -0.463  1.00 18.45 ?  139 SER   B HA   1 
ATOM   6166 H  HB2  . SER   B 1 139 ? 37.272 -30.322 0.176   1.00 18.78 ?  139 SER   B HB2  1 
ATOM   6167 H  HB3  . SER   B 1 139 ? 37.596 -30.684 -1.338  1.00 18.78 ?  139 SER   B HB3  1 
ATOM   6168 H  HG   . SER   B 1 139 ? 38.343 -28.680 -0.821  1.00 18.98 ?  139 SER   B HG   1 
ATOM   6169 N  N    . LEU   B 1 140 ? 35.462 -30.832 -3.394  1.00 14.14 ?  140 LEU   B N    1 
ATOM   6170 C  CA   . LEU   B 1 140 ? 35.088 -30.586 -4.781  1.00 14.10 ?  140 LEU   B CA   1 
ATOM   6171 C  C    . LEU   B 1 140 ? 33.586 -30.356 -4.899  1.00 14.45 ?  140 LEU   B C    1 
ATOM   6172 O  O    . LEU   B 1 140 ? 33.144 -29.472 -5.639  1.00 14.50 ?  140 LEU   B O    1 
ATOM   6173 C  CB   . LEU   B 1 140 ? 35.557 -31.750 -5.663  1.00 14.58 ?  140 LEU   B CB   1 
ATOM   6174 C  CG   . LEU   B 1 140 ? 35.191 -31.655 -7.139  1.00 14.89 ?  140 LEU   B CG   1 
ATOM   6175 C  CD1  . LEU   B 1 140 ? 35.767 -30.386 -7.747  1.00 15.88 ?  140 LEU   B CD1  1 
ATOM   6176 C  CD2  . LEU   B 1 140 ? 35.674 -32.892 -7.883  1.00 16.05 ?  140 LEU   B CD2  1 
ATOM   6177 H  H    . LEU   B 1 140 ? 35.798 -31.610 -3.250  1.00 16.99 ?  140 LEU   B H    1 
ATOM   6178 H  HA   . LEU   B 1 140 ? 35.540 -29.788 -5.095  1.00 16.95 ?  140 LEU   B HA   1 
ATOM   6179 H  HB2  . LEU   B 1 140 ? 36.526 -31.813 -5.614  1.00 17.51 ?  140 LEU   B HB2  1 
ATOM   6180 H  HB3  . LEU   B 1 140 ? 35.166 -32.574 -5.330  1.00 17.51 ?  140 LEU   B HB3  1 
ATOM   6181 H  HG   . LEU   B 1 140 ? 34.228 -31.609 -7.225  1.00 17.89 ?  140 LEU   B HG   1 
ATOM   6182 H  HD11 . LEU   B 1 140 ? 35.644 -30.414 -8.708  1.00 19.08 ?  140 LEU   B HD11 1 
ATOM   6183 H  HD12 . LEU   B 1 140 ? 35.308 -29.619 -7.375  1.00 19.08 ?  140 LEU   B HD12 1 
ATOM   6184 H  HD13 . LEU   B 1 140 ? 36.715 -30.340 -7.537  1.00 19.08 ?  140 LEU   B HD13 1 
ATOM   6185 H  HD21 . LEU   B 1 140 ? 35.429 -32.813 -8.820  1.00 19.28 ?  140 LEU   B HD21 1 
ATOM   6186 H  HD22 . LEU   B 1 140 ? 36.633 -32.965 -7.794  1.00 19.28 ?  140 LEU   B HD22 1 
ATOM   6187 H  HD23 . LEU   B 1 140 ? 35.243 -33.675 -7.498  1.00 19.28 ?  140 LEU   B HD23 1 
ATOM   6188 N  N    A ARG   B 1 141 ? 32.790 -31.148 -4.172  0.56 14.81 ?  141 ARG   B N    1 
ATOM   6189 N  N    B ARG   B 1 141 ? 32.793 -31.151 -4.174  0.44 14.70 ?  141 ARG   B N    1 
ATOM   6190 C  CA   A ARG   B 1 141 ? 31.342 -30.977 -4.147  0.56 15.59 ?  141 ARG   B CA   1 
ATOM   6191 C  CA   B ARG   B 1 141 ? 31.344 -30.982 -4.141  0.44 15.27 ?  141 ARG   B CA   1 
ATOM   6192 C  C    A ARG   B 1 141 ? 30.960 -29.564 -3.730  0.56 15.03 ?  141 ARG   B C    1 
ATOM   6193 C  C    B ARG   B 1 141 ? 30.965 -29.566 -3.732  0.44 14.92 ?  141 ARG   B C    1 
ATOM   6194 O  O    A ARG   B 1 141 ? 30.157 -28.895 -4.396  0.56 15.36 ?  141 ARG   B O    1 
ATOM   6195 O  O    B ARG   B 1 141 ? 30.178 -28.893 -4.411  0.44 15.16 ?  141 ARG   B O    1 
ATOM   6196 C  CB   A ARG   B 1 141 ? 30.757 -31.990 -3.159  0.56 17.20 ?  141 ARG   B CB   1 
ATOM   6197 C  CB   B ARG   B 1 141 ? 30.769 -31.998 -3.147  0.44 16.34 ?  141 ARG   B CB   1 
ATOM   6198 C  CG   A ARG   B 1 141 ? 29.267 -31.903 -2.933  0.56 18.90 ?  141 ARG   B CG   1 
ATOM   6199 C  CG   B ARG   B 1 141 ? 29.302 -31.842 -2.805  0.44 17.23 ?  141 ARG   B CG   1 
ATOM   6200 C  CD   A ARG   B 1 141 ? 28.548 -32.564 -4.058  0.56 20.76 ?  141 ARG   B CD   1 
ATOM   6201 C  CD   B ARG   B 1 141 ? 28.456 -32.486 -3.851  0.44 17.85 ?  141 ARG   B CD   1 
ATOM   6202 N  NE   A ARG   B 1 141 ? 28.226 -31.634 -5.130  0.56 21.02 ?  141 ARG   B NE   1 
ATOM   6203 N  NE   B ARG   B 1 141 ? 28.191 -31.589 -4.965  0.44 17.79 ?  141 ARG   B NE   1 
ATOM   6204 C  CZ   A ARG   B 1 141 ? 28.187 -31.957 -6.415  0.56 21.23 ?  141 ARG   B CZ   1 
ATOM   6205 C  CZ   B ARG   B 1 141 ? 28.226 -31.943 -6.242  0.44 17.55 ?  141 ARG   B CZ   1 
ATOM   6206 N  NH1  A ARG   B 1 141 ? 28.595 -33.141 -6.844  0.56 21.17 ?  141 ARG   B NH1  1 
ATOM   6207 N  NH1  B ARG   B 1 141 ? 28.663 -33.134 -6.620  0.44 17.08 ?  141 ARG   B NH1  1 
ATOM   6208 N  NH2  A ARG   B 1 141 ? 27.723 -31.072 -7.292  0.56 21.89 ?  141 ARG   B NH2  1 
ATOM   6209 N  NH2  B ARG   B 1 141 ? 27.817 -31.079 -7.166  0.44 18.47 ?  141 ARG   B NH2  1 
ATOM   6210 H  H    A ARG   B 1 141 ? 33.076 -31.789 -3.679  0.56 17.79 ?  141 ARG   B H    1 
ATOM   6211 H  H    B ARG   B 1 141 ? 33.081 -31.796 -3.686  0.44 17.66 ?  141 ARG   B H    1 
ATOM   6212 H  HA   A ARG   B 1 141 ? 30.976 -31.147 -5.026  0.56 18.73 ?  141 ARG   B HA   1 
ATOM   6213 H  HA   B ARG   B 1 141 ? 30.974 -31.159 -5.016  0.44 18.35 ?  141 ARG   B HA   1 
ATOM   6214 H  HB2  A ARG   B 1 141 ? 30.963 -32.882 -3.478  0.56 20.67 ?  141 ARG   B HB2  1 
ATOM   6215 H  HB2  B ARG   B 1 141 ? 30.897 -32.887 -3.514  0.44 19.63 ?  141 ARG   B HB2  1 
ATOM   6216 H  HB3  A ARG   B 1 141 ? 31.184 -31.855 -2.299  0.56 20.67 ?  141 ARG   B HB3  1 
ATOM   6217 H  HB3  B ARG   B 1 141 ? 31.263 -31.926 -2.317  0.44 19.63 ?  141 ARG   B HB3  1 
ATOM   6218 H  HG2  A ARG   B 1 141 ? 29.044 -32.360 -2.108  0.56 22.71 ?  141 ARG   B HG2  1 
ATOM   6219 H  HG2  B ARG   B 1 141 ? 29.128 -32.277 -1.959  0.44 20.70 ?  141 ARG   B HG2  1 
ATOM   6220 H  HG3  A ARG   B 1 141 ? 28.987 -30.973 -2.885  0.56 22.71 ?  141 ARG   B HG3  1 
ATOM   6221 H  HG3  B ARG   B 1 141 ? 29.062 -30.902 -2.751  0.44 20.70 ?  141 ARG   B HG3  1 
ATOM   6222 H  HD2  A ARG   B 1 141 ? 29.108 -33.269 -4.418  0.56 24.93 ?  141 ARG   B HD2  1 
ATOM   6223 H  HD2  B ARG   B 1 141 ? 28.912 -33.279 -4.182  0.44 21.44 ?  141 ARG   B HD2  1 
ATOM   6224 H  HD3  A ARG   B 1 141 ? 27.724 -32.941 -3.722  0.56 24.93 ?  141 ARG   B HD3  1 
ATOM   6225 H  HD3  B ARG   B 1 141 ? 27.609 -32.741 -3.460  0.44 21.44 ?  141 ARG   B HD3  1 
ATOM   6226 H  HE   A ARG   B 1 141 ? 28.039 -30.821 -4.912  0.56 25.24 ?  141 ARG   B HE   1 
ATOM   6227 H  HE   B ARG   B 1 141 ? 28.007 -30.769 -4.782  0.44 21.37 ?  141 ARG   B HE   1 
ATOM   6228 H  HH11 A ARG   B 1 141 ? 28.887 -33.729 -6.288  0.56 25.43 ?  141 ARG   B HH11 1 
ATOM   6229 H  HH11 B ARG   B 1 141 ? 28.920 -33.713 -6.038  0.44 20.52 ?  141 ARG   B HH11 1 
ATOM   6230 H  HH12 A ARG   B 1 141 ? 28.566 -33.324 -7.681  0.56 25.43 ?  141 ARG   B HH12 1 
ATOM   6231 H  HH12 B ARG   B 1 141 ? 28.682 -33.337 -7.454  0.44 20.52 ?  141 ARG   B HH12 1 
ATOM   6232 H  HH21 A ARG   B 1 141 ? 27.463 -30.296 -7.025  0.56 26.29 ?  141 ARG   B HH21 1 
ATOM   6233 H  HH21 B ARG   B 1 141 ? 27.540 -30.298 -6.935  0.44 22.18 ?  141 ARG   B HH21 1 
ATOM   6234 H  HH22 A ARG   B 1 141 ? 27.711 -31.263 -8.131  0.56 26.29 ?  141 ARG   B HH22 1 
ATOM   6235 H  HH22 B ARG   B 1 141 ? 27.854 -31.290 -8.000  0.44 22.18 ?  141 ARG   B HH22 1 
ATOM   6236 N  N    . VAL   B 1 142 ? 31.505 -29.105 -2.604  1.00 15.02 ?  142 VAL   B N    1 
ATOM   6237 C  CA   . VAL   B 1 142 ? 31.177 -27.768 -2.130  1.00 14.66 ?  142 VAL   B CA   1 
ATOM   6238 C  C    . VAL   B 1 142 ? 31.648 -26.718 -3.129  1.00 14.42 ?  142 VAL   B C    1 
ATOM   6239 O  O    . VAL   B 1 142 ? 30.946 -25.734 -3.391  1.00 14.80 ?  142 VAL   B O    1 
ATOM   6240 C  CB   . VAL   B 1 142 ? 31.733 -27.536 -0.713  1.00 15.13 ?  142 VAL   B CB   1 
ATOM   6241 C  CG1  . VAL   B 1 142 ? 31.413 -26.117 -0.245  1.00 15.19 ?  142 VAL   B CG1  1 
ATOM   6242 C  CG2  . VAL   B 1 142 ? 31.167 -28.562 0.257   1.00 16.08 ?  142 VAL   B CG2  1 
ATOM   6243 H  H    A VAL   B 1 142 ? 32.058 -29.538 -2.106  0.56 18.04 ?  142 VAL   B H    1 
ATOM   6244 H  H    B VAL   B 1 142 ? 32.060 -29.536 -2.106  0.44 18.04 ?  142 VAL   B H    1 
ATOM   6245 H  HA   . VAL   B 1 142 ? 30.217 -27.691 -2.070  1.00 17.61 ?  142 VAL   B HA   1 
ATOM   6246 H  HB   . VAL   B 1 142 ? 32.701 -27.633 -0.727  1.00 18.18 ?  142 VAL   B HB   1 
ATOM   6247 H  HG11 . VAL   B 1 142 ? 31.602 -26.046 0.703   1.00 18.26 ?  142 VAL   B HG11 1 
ATOM   6248 H  HG12 . VAL   B 1 142 ? 31.969 -25.487 -0.737  1.00 18.26 ?  142 VAL   B HG12 1 
ATOM   6249 H  HG13 . VAL   B 1 142 ? 30.478 -25.933 -0.413  1.00 18.26 ?  142 VAL   B HG13 1 
ATOM   6250 H  HG21 . VAL   B 1 142 ? 31.486 -28.357 1.150   1.00 19.32 ?  142 VAL   B HG21 1 
ATOM   6251 H  HG22 . VAL   B 1 142 ? 30.202 -28.517 0.228   1.00 19.32 ?  142 VAL   B HG22 1 
ATOM   6252 H  HG23 . VAL   B 1 142 ? 31.472 -29.442 -0.009  1.00 19.32 ?  142 VAL   B HG23 1 
ATOM   6253 N  N    . CYS   B 1 143 ? 32.832 -26.917 -3.716  1.00 14.00 ?  143 CYS   B N    1 
ATOM   6254 C  CA   . CYS   B 1 143 ? 33.327 -25.986 -4.727  1.00 13.97 ?  143 CYS   B CA   1 
ATOM   6255 C  C    . CYS   B 1 143 ? 32.321 -25.844 -5.864  1.00 13.96 ?  143 CYS   B C    1 
ATOM   6256 O  O    . CYS   B 1 143 ? 31.918 -24.733 -6.228  1.00 14.32 ?  143 CYS   B O    1 
ATOM   6257 C  CB   . CYS   B 1 143 ? 34.682 -26.472 -5.254  1.00 13.90 ?  143 CYS   B CB   1 
ATOM   6258 S  SG   . CYS   B 1 143 ? 35.431 -25.380 -6.487  1.00 14.26 ?  143 CYS   B SG   1 
ATOM   6259 H  H    . CYS   B 1 143 ? 33.363 -27.570 -3.547  1.00 16.82 ?  143 CYS   B H    1 
ATOM   6260 H  HA   . CYS   B 1 143 ? 33.460 -25.110 -4.328  1.00 16.79 ?  143 CYS   B HA   1 
ATOM   6261 H  HB2  . CYS   B 1 143 ? 35.307 -26.543 -4.511  1.00 16.70 ?  143 CYS   B HB2  1 
ATOM   6262 H  HB3  . CYS   B 1 143 ? 34.568 -27.341 -5.660  1.00 16.70 ?  143 CYS   B HB3  1 
ATOM   6263 H  HG   . CYS   B 1 143 ? 36.509 -25.816 -6.804  1.00 17.14 ?  143 CYS   B HG   1 
ATOM   6264 N  N    . VAL   B 1 144 ? 31.910 -26.968 -6.449  1.00 14.85 ?  144 VAL   B N    1 
ATOM   6265 C  CA   . VAL   B 1 144 ? 31.004 -26.905 -7.589  1.00 15.83 ?  144 VAL   B CA   1 
ATOM   6266 C  C    . VAL   B 1 144 ? 29.662 -26.291 -7.206  1.00 15.63 ?  144 VAL   B C    1 
ATOM   6267 O  O    . VAL   B 1 144 ? 29.041 -25.582 -8.009  1.00 16.81 ?  144 VAL   B O    1 
ATOM   6268 C  CB   . VAL   B 1 144 ? 30.842 -28.322 -8.158  1.00 18.23 ?  144 VAL   B CB   1 
ATOM   6269 C  CG1  . VAL   B 1 144 ? 29.557 -28.455 -8.974  1.00 21.05 ?  144 VAL   B CG1  1 
ATOM   6270 C  CG2  . VAL   B 1 144 ? 32.075 -28.724 -8.962  1.00 18.49 ?  144 VAL   B CG2  1 
ATOM   6271 H  H    . VAL   B 1 144 ? 32.147 -27.763 -6.217  1.00 17.85 ?  144 VAL   B H    1 
ATOM   6272 H  HA   . VAL   B 1 144 ? 31.394 -26.351 -8.283  1.00 19.01 ?  144 VAL   B HA   1 
ATOM   6273 H  HB   . VAL   B 1 144 ? 30.773 -28.944 -7.418  1.00 21.90 ?  144 VAL   B HB   1 
ATOM   6274 H  HG11 . VAL   B 1 144 ? 29.626 -29.247 -9.538  1.00 25.28 ?  144 VAL   B HG11 1 
ATOM   6275 H  HG12 . VAL   B 1 144 ? 28.806 -28.553 -8.369  1.00 25.28 ?  144 VAL   B HG12 1 
ATOM   6276 H  HG13 . VAL   B 1 144 ? 29.448 -27.671 -9.528  1.00 25.28 ?  144 VAL   B HG13 1 
ATOM   6277 H  HG21 . VAL   B 1 144 ? 31.952 -29.624 -9.308  1.00 22.21 ?  144 VAL   B HG21 1 
ATOM   6278 H  HG22 . VAL   B 1 144 ? 32.189 -28.102 -9.700  1.00 22.21 ?  144 VAL   B HG22 1 
ATOM   6279 H  HG23 . VAL   B 1 144 ? 32.852 -28.696 -8.384  1.00 22.21 ?  144 VAL   B HG23 1 
ATOM   6280 N  N    . ASP   B 1 145 ? 29.196 -26.545 -5.986  1.00 15.84 ?  145 ASP   B N    1 
ATOM   6281 C  CA   . ASP   B 1 145 ? 27.891 -26.068 -5.553  1.00 16.47 ?  145 ASP   B CA   1 
ATOM   6282 C  C    . ASP   B 1 145 ? 27.931 -24.644 -5.019  1.00 16.13 ?  145 ASP   B C    1 
ATOM   6283 O  O    . ASP   B 1 145 ? 26.875 -24.105 -4.668  1.00 17.85 ?  145 ASP   B O    1 
ATOM   6284 C  CB   . ASP   B 1 145 ? 27.303 -26.980 -4.470  1.00 18.27 ?  145 ASP   B CB   1 
ATOM   6285 C  CG   . ASP   B 1 145 ? 26.934 -28.353 -4.982  1.00 20.29 ?  145 ASP   B CG   1 
ATOM   6286 O  OD1  . ASP   B 1 145 ? 26.825 -28.542 -6.211  1.00 20.16 ?  145 ASP   B OD1  1 
ATOM   6287 O  OD2  . ASP   B 1 145 ? 26.745 -29.243 -4.132  1.00 22.30 -1 145 ASP   B OD2  1 
ATOM   6288 H  H    . ASP   B 1 145 ? 29.632 -26.979 -5.386  1.00 19.03 ?  145 ASP   B H    1 
ATOM   6289 H  HA   . ASP   B 1 145 ? 27.295 -26.062 -6.312  1.00 19.78 ?  145 ASP   B HA   1 
ATOM   6290 H  HB2  . ASP   B 1 145 ? 27.956 -27.097 -3.769  1.00 21.95 ?  145 ASP   B HB2  1 
ATOM   6291 H  HB3  . ASP   B 1 145 ? 26.500 -26.565 -4.119  1.00 21.95 ?  145 ASP   B HB3  1 
ATOM   6292 N  N    . THR   B 1 146 ? 29.111 -24.030 -4.932  1.00 14.43 ?  146 THR   B N    1 
ATOM   6293 C  CA   . THR   B 1 146 ? 29.245 -22.703 -4.334  1.00 14.19 ?  146 THR   B CA   1 
ATOM   6294 C  C    . THR   B 1 146 ? 29.872 -21.679 -5.263  1.00 13.87 ?  146 THR   B C    1 
ATOM   6295 O  O    . THR   B 1 146 ? 29.411 -20.522 -5.323  1.00 14.07 ?  146 THR   B O    1 
ATOM   6296 C  CB   . THR   B 1 146 ? 30.073 -22.806 -3.049  1.00 14.44 ?  146 THR   B CB   1 
ATOM   6297 O  OG1  . THR   B 1 146 ? 29.497 -23.792 -2.182  1.00 14.98 ?  146 THR   B OG1  1 
ATOM   6298 C  CG2  . THR   B 1 146 ? 30.146 -21.460 -2.338  1.00 14.70 ?  146 THR   B CG2  1 
ATOM   6299 H  H    . THR   B 1 146 ? 29.863 -24.355 -5.215  1.00 17.33 ?  146 THR   B H    1 
ATOM   6300 H  HA   . THR   B 1 146 ? 28.373 -22.374 -4.090  1.00 17.04 ?  146 THR   B HA   1 
ATOM   6301 H  HB   . THR   B 1 146 ? 30.985 -23.064 -3.274  1.00 17.35 ?  146 THR   B HB   1 
ATOM   6302 H  HG1  . THR   B 1 146 ? 29.537 -24.549 -2.551  1.00 18.00 ?  146 THR   B HG1  1 
ATOM   6303 H  HG21 . THR   B 1 146 ? 30.496 -21.572 -1.442  1.00 17.66 ?  146 THR   B HG21 1 
ATOM   6304 H  HG22 . THR   B 1 146 ? 30.733 -20.853 -2.826  1.00 17.66 ?  146 THR   B HG22 1 
ATOM   6305 H  HG23 . THR   B 1 146 ? 29.263 -21.064 -2.286  1.00 17.66 ?  146 THR   B HG23 1 
ATOM   6306 N  N    . VAL   B 1 147 ? 30.932 -22.059 -5.966  1.00 13.27 ?  147 VAL   B N    1 
ATOM   6307 C  CA   . VAL   B 1 147 ? 31.656 -21.117 -6.807  1.00 13.17 ?  147 VAL   B CA   1 
ATOM   6308 C  C    . VAL   B 1 147 ? 30.925 -20.978 -8.130  1.00 13.50 ?  147 VAL   B C    1 
ATOM   6309 O  O    . VAL   B 1 147 ? 30.549 -21.978 -8.757  1.00 14.41 ?  147 VAL   B O    1 
ATOM   6310 C  CB   . VAL   B 1 147 ? 33.111 -21.570 -7.007  1.00 12.88 ?  147 VAL   B CB   1 
ATOM   6311 C  CG1  . VAL   B 1 147 ? 33.868 -20.538 -7.829  1.00 12.73 ?  147 VAL   B CG1  1 
ATOM   6312 C  CG2  . VAL   B 1 147 ? 33.791 -21.773 -5.665  1.00 13.44 ?  147 VAL   B CG2  1 
ATOM   6313 H  H    . VAL   B 1 147 ? 31.251 -22.862 -5.979  1.00 15.94 ?  147 VAL   B H    1 
ATOM   6314 H  HA   . VAL   B 1 147 ? 31.673 -20.253 -6.376  1.00 15.83 ?  147 VAL   B HA   1 
ATOM   6315 H  HB   . VAL   B 1 147 ? 33.129 -22.414 -7.492  1.00 15.48 ?  147 VAL   B HB   1 
ATOM   6316 H  HG11 . VAL   B 1 147 ? 34.814 -20.747 -7.815  1.00 15.29 ?  147 VAL   B HG11 1 
ATOM   6317 H  HG12 . VAL   B 1 147 ? 33.541 -20.549 -8.743  1.00 15.29 ?  147 VAL   B HG12 1 
ATOM   6318 H  HG13 . VAL   B 1 147 ? 33.722 -19.657 -7.440  1.00 15.29 ?  147 VAL   B HG13 1 
ATOM   6319 H  HG21 . VAL   B 1 147 ? 34.730 -21.962 -5.810  1.00 16.15 ?  147 VAL   B HG21 1 
ATOM   6320 H  HG22 . VAL   B 1 147 ? 33.693 -20.962 -5.140  1.00 16.15 ?  147 VAL   B HG22 1 
ATOM   6321 H  HG23 . VAL   B 1 147 ? 33.369 -22.516 -5.206  1.00 16.15 ?  147 VAL   B HG23 1 
ATOM   6322 N  N    . ARG   B 1 148 ? 30.728 -19.728 -8.552  1.00 13.40 ?  148 ARG   B N    1 
ATOM   6323 C  CA   . ARG   B 1 148 ? 30.098 -19.410 -9.822  1.00 13.58 ?  148 ARG   B CA   1 
ATOM   6324 C  C    . ARG   B 1 148 ? 31.049 -18.728 -10.793 1.00 13.81 ?  148 ARG   B C    1 
ATOM   6325 O  O    . ARG   B 1 148 ? 30.753 -18.688 -11.991 1.00 15.40 ?  148 ARG   B O    1 
ATOM   6326 C  CB   . ARG   B 1 148 ? 28.854 -18.531 -9.606  1.00 14.01 ?  148 ARG   B CB   1 
ATOM   6327 C  CG   . ARG   B 1 148 ? 27.784 -19.244 -8.797  1.00 14.59 ?  148 ARG   B CG   1 
ATOM   6328 C  CD   . ARG   B 1 148 ? 26.571 -18.361 -8.495  1.00 15.58 ?  148 ARG   B CD   1 
ATOM   6329 N  NE   . ARG   B 1 148 ? 26.948 -17.157 -7.763  1.00 15.95 ?  148 ARG   B NE   1 
ATOM   6330 C  CZ   . ARG   B 1 148 ? 27.252 -17.122 -6.471  1.00 14.69 ?  148 ARG   B CZ   1 
ATOM   6331 N  NH1  . ARG   B 1 148 ? 27.196 -18.209 -5.714  1.00 14.56 ?  148 ARG   B NH1  1 
ATOM   6332 N  NH2  . ARG   B 1 148 ? 27.641 -15.970 -5.928  1.00 14.52 ?  148 ARG   B NH2  1 
ATOM   6333 H  H    . ARG   B 1 148 ? 30.959 -19.026 -8.099  1.00 16.10 ?  148 ARG   B H    1 
ATOM   6334 H  HA   . ARG   B 1 148 ? 29.807 -20.233 -10.235 1.00 16.32 ?  148 ARG   B HA   1 
ATOM   6335 H  HB2  . ARG   B 1 148 ? 29.114 -17.727 -9.125  1.00 16.83 ?  148 ARG   B HB2  1 
ATOM   6336 H  HB3  . ARG   B 1 148 ? 28.480 -18.295 -10.469 1.00 16.83 ?  148 ARG   B HB3  1 
ATOM   6337 H  HG2  . ARG   B 1 148 ? 27.478 -20.017 -9.299  1.00 17.53 ?  148 ARG   B HG2  1 
ATOM   6338 H  HG3  . ARG   B 1 148 ? 28.166 -19.529 -7.953  1.00 17.53 ?  148 ARG   B HG3  1 
ATOM   6339 H  HD2  . ARG   B 1 148 ? 26.159 -18.093 -9.332  1.00 18.72 ?  148 ARG   B HD2  1 
ATOM   6340 H  HD3  . ARG   B 1 148 ? 25.940 -18.865 -7.957  1.00 18.72 ?  148 ARG   B HD3  1 
ATOM   6341 H  HE   . ARG   B 1 148 ? 26.985 -16.422 -8.200  1.00 19.16 ?  148 ARG   B HE   1 
ATOM   6342 H  HH11 . ARG   B 1 148 ? 26.941 -18.962 -6.049  1.00 17.50 ?  148 ARG   B HH11 1 
ATOM   6343 H  HH12 . ARG   B 1 148 ? 27.390 -18.163 -4.876  1.00 17.50 ?  148 ARG   B HH12 1 
ATOM   6344 H  HH21 . ARG   B 1 148 ? 27.691 -15.265 -6.412  1.00 17.45 ?  148 ARG   B HH21 1 
ATOM   6345 H  HH22 . ARG   B 1 148 ? 27.842 -15.936 -5.093  1.00 17.45 ?  148 ARG   B HH22 1 
ATOM   6346 N  N    . THR   B 1 149 ? 32.164 -18.185 -10.305 1.00 13.33 ?  149 THR   B N    1 
ATOM   6347 C  CA   . THR   B 1 149 ? 33.200 -17.619 -11.154 1.00 13.23 ?  149 THR   B CA   1 
ATOM   6348 C  C    . THR   B 1 149 ? 34.087 -18.753 -11.672 1.00 13.29 ?  149 THR   B C    1 
ATOM   6349 O  O    . THR   B 1 149 ? 33.891 -19.924 -11.343 1.00 13.76 ?  149 THR   B O    1 
ATOM   6350 C  CB   . THR   B 1 149 ? 33.977 -16.576 -10.364 1.00 13.77 ?  149 THR   B CB   1 
ATOM   6351 O  OG1  . THR   B 1 149 ? 34.436 -17.181 -9.152  1.00 13.62 ?  149 THR   B OG1  1 
ATOM   6352 C  CG2  . THR   B 1 149 ? 33.096 -15.368 -10.044 1.00 14.48 ?  149 THR   B CG2  1 
ATOM   6353 H  H    . THR   B 1 149 ? 32.339 -18.126 -9.462  1.00 16.02 ?  149 THR   B H    1 
ATOM   6354 H  HA   . THR   B 1 149 ? 32.787 -17.180 -11.913 1.00 15.89 ?  149 THR   B HA   1 
ATOM   6355 H  HB   . THR   B 1 149 ? 34.738 -16.282 -10.883 1.00 16.54 ?  149 THR   B HB   1 
ATOM   6356 H  HG1  . THR   B 1 149 ? 34.865 -16.619 -8.692  1.00 16.37 ?  149 THR   B HG1  1 
ATOM   6357 H  HG21 . THR   B 1 149 ? 33.608 -14.706 -9.551  1.00 17.39 ?  149 THR   B HG21 1 
ATOM   6358 H  HG22 . THR   B 1 149 ? 32.773 -14.966 -10.865 1.00 17.39 ?  149 THR   B HG22 1 
ATOM   6359 H  HG23 . THR   B 1 149 ? 32.336 -15.639 -9.506  1.00 17.39 ?  149 THR   B HG23 1 
ATOM   6360 N  N    . ASN   B 1 150 ? 35.051 -18.426 -12.521 1.00 13.38 ?  150 ASN   B N    1 
ATOM   6361 C  CA   . ASN   B 1 150 ? 35.817 -19.448 -13.224 1.00 13.53 ?  150 ASN   B CA   1 
ATOM   6362 C  C    . ASN   B 1 150 ? 36.981 -19.901 -12.350 1.00 13.01 ?  150 ASN   B C    1 
ATOM   6363 O  O    . ASN   B 1 150 ? 37.922 -19.139 -12.108 1.00 13.85 ?  150 ASN   B O    1 
ATOM   6364 C  CB   . ASN   B 1 150 ? 36.292 -18.913 -14.567 1.00 15.54 ?  150 ASN   B CB   1 
ATOM   6365 C  CG   . ASN   B 1 150 ? 35.153 -18.707 -15.523 1.00 18.67 ?  150 ASN   B CG   1 
ATOM   6366 O  OD1  . ASN   B 1 150 ? 34.245 -19.528 -15.593 1.00 19.66 ?  150 ASN   B OD1  1 
ATOM   6367 N  ND2  . ASN   B 1 150 ? 35.171 -17.599 -16.243 1.00 20.83 ?  150 ASN   B ND2  1 
ATOM   6368 H  H    . ASN   B 1 150 ? 35.293 -17.617 -12.694 1.00 16.08 ?  150 ASN   B H    1 
ATOM   6369 H  HA   . ASN   B 1 150 ? 35.238 -20.211 -13.387 1.00 16.25 ?  150 ASN   B HA   1 
ATOM   6370 H  HB2  . ASN   B 1 150 ? 36.730 -18.056 -14.428 1.00 18.67 ?  150 ASN   B HB2  1 
ATOM   6371 H  HB3  . ASN   B 1 150 ? 36.909 -19.545 -14.958 1.00 18.67 ?  150 ASN   B HB3  1 
ATOM   6372 H  HD21 . ASN   B 1 150 ? 34.539 -17.435 -16.806 1.00 25.02 ?  150 ASN   B HD21 1 
ATOM   6373 H  HD22 . ASN   B 1 150 ? 35.822 -17.040 -16.162 1.00 25.02 ?  150 ASN   B HD22 1 
ATOM   6374 N  N    . VAL   B 1 151 ? 36.922 -21.144 -11.876 1.00 12.81 ?  151 VAL   B N    1 
ATOM   6375 C  CA   . VAL   B 1 151 ? 37.938 -21.681 -10.984 1.00 13.09 ?  151 VAL   B CA   1 
ATOM   6376 C  C    . VAL   B 1 151 ? 38.638 -22.853 -11.660 1.00 12.77 ?  151 VAL   B C    1 
ATOM   6377 O  O    . VAL   B 1 151 ? 37.992 -23.788 -12.155 1.00 13.99 ?  151 VAL   B O    1 
ATOM   6378 C  CB   . VAL   B 1 151 ? 37.380 -22.031 -9.587  1.00 14.23 ?  151 VAL   B CB   1 
ATOM   6379 C  CG1  . VAL   B 1 151 ? 36.202 -23.013 -9.662  1.00 15.62 ?  151 VAL   B CG1  1 
ATOM   6380 C  CG2  . VAL   B 1 151 ? 38.491 -22.540 -8.683  1.00 14.60 ?  151 VAL   B CG2  1 
ATOM   6381 H  H    . VAL   B 1 151 ? 36.286 -21.701 -12.062 1.00 15.40 ?  151 VAL   B H    1 
ATOM   6382 H  HA   . VAL   B 1 151 ? 38.605 -20.989 -10.850 1.00 15.72 ?  151 VAL   B HA   1 
ATOM   6383 H  HB   . VAL   B 1 151 ? 37.043 -21.214 -9.188  1.00 17.09 ?  151 VAL   B HB   1 
ATOM   6384 H  HG11 . VAL   B 1 151 ? 35.895 -23.205 -8.761  1.00 18.76 ?  151 VAL   B HG11 1 
ATOM   6385 H  HG12 . VAL   B 1 151 ? 35.483 -22.607 -10.174 1.00 18.76 ?  151 VAL   B HG12 1 
ATOM   6386 H  HG13 . VAL   B 1 151 ? 36.495 -23.829 -10.092 1.00 18.76 ?  151 VAL   B HG13 1 
ATOM   6387 H  HG21 . VAL   B 1 151 ? 38.147 -22.616 -7.777  1.00 17.55 ?  151 VAL   B HG21 1 
ATOM   6388 H  HG22 . VAL   B 1 151 ? 38.786 -23.408 -8.996  1.00 17.55 ?  151 VAL   B HG22 1 
ATOM   6389 H  HG23 . VAL   B 1 151 ? 39.229 -21.911 -8.701  1.00 17.55 ?  151 VAL   B HG23 1 
ATOM   6390 N  N    . TYR   B 1 152 ? 39.968 -22.774 -11.678 1.00 12.17 ?  152 TYR   B N    1 
ATOM   6391 C  CA   . TYR   B 1 152 ? 40.863 -23.763 -12.263 1.00 12.61 ?  152 TYR   B CA   1 
ATOM   6392 C  C    . TYR   B 1 152 ? 41.588 -24.447 -11.109 1.00 12.04 ?  152 TYR   B C    1 
ATOM   6393 O  O    . TYR   B 1 152 ? 42.445 -23.836 -10.462 1.00 12.32 ?  152 TYR   B O    1 
ATOM   6394 C  CB   . TYR   B 1 152 ? 41.834 -23.064 -13.218 1.00 13.55 ?  152 TYR   B CB   1 
ATOM   6395 C  CG   . TYR   B 1 152 ? 41.154 -22.587 -14.482 1.00 14.28 ?  152 TYR   B CG   1 
ATOM   6396 C  CD1  . TYR   B 1 152 ? 40.514 -21.351 -14.540 1.00 14.65 ?  152 TYR   B CD1  1 
ATOM   6397 C  CD2  . TYR   B 1 152 ? 41.117 -23.392 -15.605 1.00 15.69 ?  152 TYR   B CD2  1 
ATOM   6398 C  CE1  . TYR   B 1 152 ? 39.877 -20.932 -15.692 1.00 16.36 ?  152 TYR   B CE1  1 
ATOM   6399 C  CE2  . TYR   B 1 152 ? 40.486 -22.986 -16.757 1.00 16.55 ?  152 TYR   B CE2  1 
ATOM   6400 C  CZ   . TYR   B 1 152 ? 39.870 -21.754 -16.799 1.00 16.76 ?  152 TYR   B CZ   1 
ATOM   6401 O  OH   . TYR   B 1 152 ? 39.240 -21.366 -17.956 1.00 19.44 ?  152 TYR   B OH   1 
ATOM   6402 H  H    . TYR   B 1 152 ? 40.405 -22.108 -11.331 1.00 14.62 ?  152 TYR   B H    1 
ATOM   6403 H  HA   . TYR   B 1 152 ? 40.352 -24.422 -12.753 1.00 15.15 ?  152 TYR   B HA   1 
ATOM   6404 H  HB2  . TYR   B 1 152 ? 42.215 -22.290 -12.769 1.00 16.28 ?  152 TYR   B HB2  1 
ATOM   6405 H  HB3  . TYR   B 1 152 ? 42.540 -23.679 -13.465 1.00 16.28 ?  152 TYR   B HB3  1 
ATOM   6406 H  HD1  . TYR   B 1 152 ? 40.522 -20.794 -13.792 1.00 17.60 ?  152 TYR   B HD1  1 
ATOM   6407 H  HD2  . TYR   B 1 152 ? 41.529 -24.225 -15.579 1.00 18.85 ?  152 TYR   B HD2  1 
ATOM   6408 H  HE1  . TYR   B 1 152 ? 39.461 -20.097 -15.728 1.00 19.65 ?  152 TYR   B HE1  1 
ATOM   6409 H  HE2  . TYR   B 1 152 ? 40.479 -23.541 -17.504 1.00 19.88 ?  152 TYR   B HE2  1 
ATOM   6410 H  HH   . TYR   B 1 152 ? 39.322 -21.961 -18.546 1.00 23.35 ?  152 TYR   B HH   1 
ATOM   6411 N  N    . LEU   B 1 153 ? 41.222 -25.704 -10.841 1.00 12.12 ?  153 LEU   B N    1 
ATOM   6412 C  CA   . LEU   B 1 153 ? 41.734 -26.450 -9.703  1.00 12.21 ?  153 LEU   B CA   1 
ATOM   6413 C  C    . LEU   B 1 153 ? 42.963 -27.251 -10.106 1.00 12.46 ?  153 LEU   B C    1 
ATOM   6414 O  O    . LEU   B 1 153 ? 42.940 -27.983 -11.099 1.00 13.73 ?  153 LEU   B O    1 
ATOM   6415 C  CB   . LEU   B 1 153 ? 40.657 -27.407 -9.186  1.00 12.22 ?  153 LEU   B CB   1 
ATOM   6416 C  CG   . LEU   B 1 153 ? 39.409 -26.752 -8.597  1.00 13.30 ?  153 LEU   B CG   1 
ATOM   6417 C  CD1  . LEU   B 1 153 ? 38.304 -27.794 -8.436  1.00 14.53 ?  153 LEU   B CD1  1 
ATOM   6418 C  CD2  . LEU   B 1 153 ? 39.725 -26.096 -7.261  1.00 13.65 ?  153 LEU   B CD2  1 
ATOM   6419 H  H    . LEU   B 1 153 ? 40.645 -26.142 -11.310 1.00 14.57 ?  153 LEU   B H    1 
ATOM   6420 H  HA   . LEU   B 1 153 ? 41.962 -25.837 -8.991  1.00 14.67 ?  153 LEU   B HA   1 
ATOM   6421 H  HB2  . LEU   B 1 153 ? 40.363 -27.973 -9.917  1.00 14.68 ?  153 LEU   B HB2  1 
ATOM   6422 H  HB3  . LEU   B 1 153 ? 41.044 -27.960 -8.487  1.00 14.68 ?  153 LEU   B HB3  1 
ATOM   6423 H  HG   . LEU   B 1 153 ? 39.086 -26.061 -9.200  1.00 15.98 ?  153 LEU   B HG   1 
ATOM   6424 H  HD11 . LEU   B 1 153 ? 37.500 -27.354 -8.106  1.00 17.45 ?  153 LEU   B HD11 1 
ATOM   6425 H  HD12 . LEU   B 1 153 ? 38.127 -28.197 -9.296  1.00 17.45 ?  153 LEU   B HD12 1 
ATOM   6426 H  HD13 . LEU   B 1 153 ? 38.595 -28.464 -7.802  1.00 17.45 ?  153 LEU   B HD13 1 
ATOM   6427 H  HD21 . LEU   B 1 153 ? 38.912 -25.732 -6.880  1.00 16.40 ?  153 LEU   B HD21 1 
ATOM   6428 H  HD22 . LEU   B 1 153 ? 40.099 -26.766 -6.663  1.00 16.40 ?  153 LEU   B HD22 1 
ATOM   6429 H  HD23 . LEU   B 1 153 ? 40.372 -25.387 -7.403  1.00 16.40 ?  153 LEU   B HD23 1 
ATOM   6430 N  N    . ALA   B 1 154 ? 44.018 -27.140 -9.306  1.00 12.69 ?  154 ALA   B N    1 
ATOM   6431 C  CA   . ALA   B 1 154 ? 45.246 -27.900 -9.492  1.00 13.96 ?  154 ALA   B CA   1 
ATOM   6432 C  C    . ALA   B 1 154 ? 45.316 -28.976 -8.417  1.00 14.37 ?  154 ALA   B C    1 
ATOM   6433 O  O    . ALA   B 1 154 ? 45.280 -28.670 -7.216  1.00 16.33 ?  154 ALA   B O    1 
ATOM   6434 C  CB   . ALA   B 1 154 ? 46.471 -26.992 -9.430  1.00 15.20 ?  154 ALA   B CB   1 
ATOM   6435 H  H    . ALA   B 1 154 ? 44.039 -26.605 -8.629  1.00 15.24 ?  154 ALA   B H    1 
ATOM   6436 H  HA   . ALA   B 1 154 ? 45.224 -28.328 -10.362 1.00 16.77 ?  154 ALA   B HA   1 
ATOM   6437 H  HB1  . ALA   B 1 154 ? 47.267 -27.532 -9.560  1.00 18.26 ?  154 ALA   B HB1  1 
ATOM   6438 H  HB2  . ALA   B 1 154 ? 46.409 -26.324 -10.133 1.00 18.26 ?  154 ALA   B HB2  1 
ATOM   6439 H  HB3  . ALA   B 1 154 ? 46.502 -26.558 -8.564  1.00 18.26 ?  154 ALA   B HB3  1 
ATOM   6440 N  N    . VAL   B 1 155 ? 45.402 -30.228 -8.849  1.00 14.10 ?  155 VAL   B N    1 
ATOM   6441 C  CA   . VAL   B 1 155 ? 45.505 -31.373 -7.956  1.00 14.83 ?  155 VAL   B CA   1 
ATOM   6442 C  C    . VAL   B 1 155 ? 46.837 -32.053 -8.246  1.00 14.46 ?  155 VAL   B C    1 
ATOM   6443 O  O    . VAL   B 1 155 ? 47.060 -32.548 -9.358  1.00 16.18 ?  155 VAL   B O    1 
ATOM   6444 C  CB   . VAL   B 1 155 ? 44.337 -32.358 -8.138  1.00 15.98 ?  155 VAL   B CB   1 
ATOM   6445 C  CG1  . VAL   B 1 155 ? 44.529 -33.559 -7.225  1.00 15.93 ?  155 VAL   B CG1  1 
ATOM   6446 C  CG2  . VAL   B 1 155 ? 42.997 -31.663 -7.866  1.00 16.77 ?  155 VAL   B CG2  1 
ATOM   6447 H  H    . VAL   B 1 155 ? 45.410 -30.447 -9.686  1.00 16.94 ?  155 VAL   B H    1 
ATOM   6448 H  HA   . VAL   B 1 155 ? 45.509 -31.069 -7.038  1.00 17.82 ?  155 VAL   B HA   1 
ATOM   6449 H  HB   . VAL   B 1 155 ? 44.327 -32.676 -9.054  1.00 19.20 ?  155 VAL   B HB   1 
ATOM   6450 H  HG11 . VAL   B 1 155 ? 43.699 -34.059 -7.175  1.00 19.14 ?  155 VAL   B HG11 1 
ATOM   6451 H  HG12 . VAL   B 1 155 ? 45.230 -34.129 -7.586  1.00 19.14 ?  155 VAL   B HG12 1 
ATOM   6452 H  HG13 . VAL   B 1 155 ? 44.780 -33.251 -6.339  1.00 19.14 ?  155 VAL   B HG13 1 
ATOM   6453 H  HG21 . VAL   B 1 155 ? 42.278 -32.314 -7.955  1.00 20.15 ?  155 VAL   B HG21 1 
ATOM   6454 H  HG22 . VAL   B 1 155 ? 43.001 -31.304 -6.964  1.00 20.15 ?  155 VAL   B HG22 1 
ATOM   6455 H  HG23 . VAL   B 1 155 ? 42.872 -30.947 -8.507  1.00 20.15 ?  155 VAL   B HG23 1 
ATOM   6456 N  N    . PHE   B 1 156 ? 47.713 -32.088 -7.241  1.00 14.87 ?  156 PHE   B N    1 
ATOM   6457 C  CA   . PHE   B 1 156 ? 49.089 -32.549 -7.451  1.00 16.21 ?  156 PHE   B CA   1 
ATOM   6458 C  C    . PHE   B 1 156 ? 49.175 -34.049 -7.738  1.00 17.49 ?  156 PHE   B C    1 
ATOM   6459 O  O    . PHE   B 1 156 ? 49.880 -34.480 -8.662  1.00 19.36 ?  156 PHE   B O    1 
ATOM   6460 C  CB   . PHE   B 1 156 ? 49.927 -32.189 -6.224  1.00 15.96 ?  156 PHE   B CB   1 
ATOM   6461 C  CG   . PHE   B 1 156 ? 51.353 -32.649 -6.299  1.00 16.38 ?  156 PHE   B CG   1 
ATOM   6462 C  CD1  . PHE   B 1 156 ? 52.219 -32.119 -7.237  1.00 18.22 ?  156 PHE   B CD1  1 
ATOM   6463 C  CD2  . PHE   B 1 156 ? 51.834 -33.592 -5.410  1.00 16.51 ?  156 PHE   B CD2  1 
ATOM   6464 C  CE1  . PHE   B 1 156 ? 53.542 -32.536 -7.297  1.00 18.71 ?  156 PHE   B CE1  1 
ATOM   6465 C  CE2  . PHE   B 1 156 ? 53.154 -34.009 -5.467  1.00 17.79 ?  156 PHE   B CE2  1 
ATOM   6466 C  CZ   . PHE   B 1 156 ? 53.999 -33.482 -6.416  1.00 18.48 ?  156 PHE   B CZ   1 
ATOM   6467 H  H    . PHE   B 1 156 ? 47.535 -31.863 -6.431  1.00 17.86 ?  156 PHE   B H    1 
ATOM   6468 H  HA   . PHE   B 1 156 ? 49.459 -32.079 -8.209  1.00 19.48 ?  156 PHE   B HA   1 
ATOM   6469 H  HB2  . PHE   B 1 156 ? 49.933 -31.224 -6.125  1.00 19.17 ?  156 PHE   B HB2  1 
ATOM   6470 H  HB3  . PHE   B 1 156 ? 49.528 -32.596 -5.439  1.00 19.17 ?  156 PHE   B HB3  1 
ATOM   6471 H  HD1  . PHE   B 1 156 ? 51.914 -31.475 -7.840  1.00 21.89 ?  156 PHE   B HD1  1 
ATOM   6472 H  HD2  . PHE   B 1 156 ? 51.263 -33.957 -4.773  1.00 19.83 ?  156 PHE   B HD2  1 
ATOM   6473 H  HE1  . PHE   B 1 156 ? 54.118 -32.174 -7.937  1.00 22.47 ?  156 PHE   B HE1  1 
ATOM   6474 H  HE2  . PHE   B 1 156 ? 53.467 -34.654 -4.872  1.00 21.37 ?  156 PHE   B HE2  1 
ATOM   6475 H  HZ   . PHE   B 1 156 ? 54.887 -33.762 -6.454  1.00 22.20 ?  156 PHE   B HZ   1 
ATOM   6476 N  N    . ASP   B 1 157 ? 48.515 -34.866 -6.929  1.00 17.91 ?  157 ASP   B N    1 
ATOM   6477 C  CA   . ASP   B 1 157 ? 48.659 -36.315 -7.026  1.00 19.13 ?  157 ASP   B CA   1 
ATOM   6478 C  C    . ASP   B 1 157 ? 47.738 -36.865 -8.112  1.00 19.01 ?  157 ASP   B C    1 
ATOM   6479 O  O    . ASP   B 1 157 ? 46.512 -36.735 -8.013  1.00 18.25 ?  157 ASP   B O    1 
ATOM   6480 C  CB   . ASP   B 1 157 ? 48.306 -36.926 -5.676  1.00 20.51 ?  157 ASP   B CB   1 
ATOM   6481 C  CG   . ASP   B 1 157 ? 48.442 -38.434 -5.658  1.00 22.69 ?  157 ASP   B CG   1 
ATOM   6482 O  OD1  . ASP   B 1 157 ? 48.766 -39.038 -6.707  1.00 23.25 ?  157 ASP   B OD1  1 
ATOM   6483 O  OD2  . ASP   B 1 157 ? 48.233 -39.013 -4.575  1.00 24.95 -1 157 ASP   B OD2  1 
ATOM   6484 H  H    . ASP   B 1 157 ? 47.983 -34.609 -6.314  1.00 21.52 ?  157 ASP   B H    1 
ATOM   6485 H  HA   . ASP   B 1 157 ? 49.579 -36.546 -7.246  1.00 22.98 ?  157 ASP   B HA   1 
ATOM   6486 H  HB2  . ASP   B 1 157 ? 48.885 -36.546 -4.999  1.00 24.63 ?  157 ASP   B HB2  1 
ATOM   6487 H  HB3  . ASP   B 1 157 ? 47.382 -36.704 -5.474  1.00 24.63 ?  157 ASP   B HB3  1 
ATOM   6488 N  N    A LYS   B 1 158 ? 48.331 -37.513 -9.122  0.56 19.63 ?  158 LYS   B N    1 
ATOM   6489 N  N    B LYS   B 1 158 ? 48.333 -37.465 -9.151  0.44 19.73 ?  158 LYS   B N    1 
ATOM   6490 C  CA   A LYS   B 1 158 ? 47.553 -38.133 -10.194 0.56 20.52 ?  158 LYS   B CA   1 
ATOM   6491 C  CA   B LYS   B 1 158 ? 47.555 -38.026 -10.255 0.44 20.79 ?  158 LYS   B CA   1 
ATOM   6492 C  C    A LYS   B 1 158 ? 46.487 -39.081 -9.649  0.56 20.40 ?  158 LYS   B C    1 
ATOM   6493 C  C    B LYS   B 1 158 ? 46.490 -38.996 -9.756  0.44 20.73 ?  158 LYS   B C    1 
ATOM   6494 O  O    A LYS   B 1 158 ? 45.366 -39.136 -10.170 0.56 20.58 ?  158 LYS   B O    1 
ATOM   6495 O  O    B LYS   B 1 158 ? 45.393 -39.075 -10.324 0.44 20.82 ?  158 LYS   B O    1 
ATOM   6496 C  CB   A LYS   B 1 158 ? 48.499 -38.872 -11.151 0.56 22.39 ?  158 LYS   B CB   1 
ATOM   6497 C  CB   B LYS   B 1 158 ? 48.499 -38.719 -11.247 0.44 22.42 ?  158 LYS   B CB   1 
ATOM   6498 C  CG   A LYS   B 1 158 ? 47.814 -39.784 -12.163 0.56 24.38 ?  158 LYS   B CG   1 
ATOM   6499 C  CG   B LYS   B 1 158 ? 47.821 -39.645 -12.255 0.44 24.07 ?  158 LYS   B CG   1 
ATOM   6500 C  CD   A LYS   B 1 158 ? 46.951 -39.010 -13.139 0.56 26.18 ?  158 LYS   B CD   1 
ATOM   6501 C  CD   B LYS   B 1 158 ? 46.921 -38.887 -13.215 0.44 25.73 ?  158 LYS   B CD   1 
ATOM   6502 C  CE   A LYS   B 1 158 ? 46.367 -39.933 -14.194 0.56 27.42 ?  158 LYS   B CE   1 
ATOM   6503 C  CE   B LYS   B 1 158 ? 46.346 -39.815 -14.274 0.44 26.87 ?  158 LYS   B CE   1 
ATOM   6504 N  NZ   A LYS   B 1 158 ? 45.320 -39.257 -15.009 0.56 27.65 ?  158 LYS   B NZ   1 
ATOM   6505 N  NZ   B LYS   B 1 158 ? 45.297 -39.150 -15.097 0.44 27.21 ?  158 LYS   B NZ   1 
ATOM   6506 H  H    A LYS   B 1 158 ? 49.185 -37.611 -9.206  0.56 23.58 ?  158 LYS   B H    1 
ATOM   6507 H  H    B LYS   B 1 158 ? 49.185 -37.561 -9.238  0.44 23.70 ?  158 LYS   B H    1 
ATOM   6508 H  HA   A LYS   B 1 158 ? 47.107 -37.439 -10.703 0.56 24.65 ?  158 LYS   B HA   1 
ATOM   6509 H  HA   B LYS   B 1 158 ? 47.110 -37.306 -10.730 0.44 24.97 ?  158 LYS   B HA   1 
ATOM   6510 H  HB2  A LYS   B 1 158 ? 49.009 -38.214 -11.656 0.56 26.89 ?  158 LYS   B HB2  1 
ATOM   6511 H  HB2  B LYS   B 1 158 ? 48.973 -38.039 -11.756 0.44 26.93 ?  158 LYS   B HB2  1 
ATOM   6512 H  HB3  A LYS   B 1 158 ? 49.107 -39.419 -10.630 0.56 26.89 ?  158 LYS   B HB3  1 
ATOM   6513 H  HB3  B LYS   B 1 158 ? 49.138 -39.251 -10.749 0.44 26.93 ?  158 LYS   B HB3  1 
ATOM   6514 H  HG2  A LYS   B 1 158 ? 48.494 -40.249 -12.675 0.56 29.28 ?  158 LYS   B HG2  1 
ATOM   6515 H  HG2  B LYS   B 1 158 ? 48.506 -40.087 -12.779 0.44 28.91 ?  158 LYS   B HG2  1 
ATOM   6516 H  HG3  A LYS   B 1 158 ? 47.255 -40.431 -11.704 0.56 29.28 ?  158 LYS   B HG3  1 
ATOM   6517 H  HG3  B LYS   B 1 158 ? 47.288 -40.311 -11.792 0.44 28.91 ?  158 LYS   B HG3  1 
ATOM   6518 H  HD2  A LYS   B 1 158 ? 46.219 -38.589 -12.662 0.56 31.43 ?  158 LYS   B HD2  1 
ATOM   6519 H  HD2  B LYS   B 1 158 ? 46.186 -38.491 -12.723 0.44 30.89 ?  158 LYS   B HD2  1 
ATOM   6520 H  HD3  A LYS   B 1 158 ? 47.492 -38.339 -13.587 0.56 31.43 ?  158 LYS   B HD3  1 
ATOM   6521 H  HD3  B LYS   B 1 158 ? 47.438 -38.198 -13.662 0.44 30.89 ?  158 LYS   B HD3  1 
ATOM   6522 H  HE2  A LYS   B 1 158 ? 47.074 -40.222 -14.792 0.56 32.92 ?  158 LYS   B HE2  1 
ATOM   6523 H  HE2  B LYS   B 1 158 ? 47.058 -40.102 -14.867 0.44 32.26 ?  158 LYS   B HE2  1 
ATOM   6524 H  HE3  A LYS   B 1 158 ? 45.964 -40.701 -13.759 0.56 32.92 ?  158 LYS   B HE3  1 
ATOM   6525 H  HE3  B LYS   B 1 158 ? 45.945 -40.585 -13.839 0.44 32.26 ?  158 LYS   B HE3  1 
ATOM   6526 H  HZ1  A LYS   B 1 158 ? 44.995 -39.819 -15.616 0.56 33.20 ?  158 LYS   B HZ1  1 
ATOM   6527 H  HZ1  B LYS   B 1 158 ? 44.981 -39.717 -15.705 0.44 32.67 ?  158 LYS   B HZ1  1 
ATOM   6528 H  HZ2  A LYS   B 1 158 ? 44.656 -38.983 -14.483 0.56 33.20 ?  158 LYS   B HZ2  1 
ATOM   6529 H  HZ2  B LYS   B 1 158 ? 44.627 -38.881 -14.576 0.44 32.67 ?  158 LYS   B HZ2  1 
ATOM   6530 H  HZ3  A LYS   B 1 158 ? 45.668 -38.551 -15.424 0.56 33.20 ?  158 LYS   B HZ3  1 
ATOM   6531 H  HZ3  B LYS   B 1 158 ? 45.641 -38.442 -15.513 0.44 32.67 ?  158 LYS   B HZ3  1 
ATOM   6532 N  N    A ASN   B 1 159 ? 46.816 -39.849 -8.608  0.56 20.70 ?  159 ASN   B N    1 
ATOM   6533 N  N    B ASN   B 1 159 ? 46.795 -39.752 -8.700  0.44 20.96 ?  159 ASN   B N    1 
ATOM   6534 C  CA   A ASN   B 1 159 ? 45.854 -40.817 -8.087  0.56 20.96 ?  159 ASN   B CA   1 
ATOM   6535 C  CA   B ASN   B 1 159 ? 45.839 -40.739 -8.205  0.44 21.00 ?  159 ASN   B CA   1 
ATOM   6536 C  C    A ASN   B 1 159 ? 44.669 -40.132 -7.409  0.56 20.28 ?  159 ASN   B C    1 
ATOM   6537 C  C    B ASN   B 1 159 ? 44.654 -40.071 -7.509  0.44 20.48 ?  159 ASN   B C    1 
ATOM   6538 O  O    A ASN   B 1 159 ? 43.542 -40.641 -7.465  0.56 20.32 ?  159 ASN   B O    1 
ATOM   6539 O  O    B ASN   B 1 159 ? 43.511 -40.529 -7.643  0.44 20.55 ?  159 ASN   B O    1 
ATOM   6540 C  CB   A ASN   B 1 159 ? 46.549 -41.785 -7.133  0.56 22.43 ?  159 ASN   B CB   1 
ATOM   6541 C  CB   B ASN   B 1 159 ? 46.547 -41.738 -7.290  0.44 21.66 ?  159 ASN   B CB   1 
ATOM   6542 C  CG   A ASN   B 1 159 ? 47.580 -42.650 -7.831  0.56 24.22 ?  159 ASN   B CG   1 
ATOM   6543 C  CG   B ASN   B 1 159 ? 47.557 -42.588 -8.035  0.44 22.68 ?  159 ASN   B CG   1 
ATOM   6544 O  OD1  A ASN   B 1 159 ? 47.342 -43.155 -8.932  0.56 25.46 ?  159 ASN   B OD1  1 
ATOM   6545 O  OD1  B ASN   B 1 159 ? 47.300 -43.033 -9.157  0.44 23.41 ?  159 ASN   B OD1  1 
ATOM   6546 N  ND2  A ASN   B 1 159 ? 48.733 -42.830 -7.191  0.56 24.89 ?  159 ASN   B ND2  1 
ATOM   6547 N  ND2  B ASN   B 1 159 ? 48.715 -42.819 -7.415  0.44 23.36 ?  159 ASN   B ND2  1 
ATOM   6548 H  H    A ASN   B 1 159 ? 47.572 -39.825 -8.201  0.56 24.86 ?  159 ASN   B H    1 
ATOM   6549 H  H    B ASN   B 1 159 ? 47.537 -39.713 -8.271  0.44 25.17 ?  159 ASN   B H    1 
ATOM   6550 H  HA   A ASN   B 1 159 ? 45.513 -41.336 -8.834  0.56 25.18 ?  159 ASN   B HA   1 
ATOM   6551 H  HA   B ASN   B 1 159 ? 45.499 -41.238 -8.965  0.44 25.23 ?  159 ASN   B HA   1 
ATOM   6552 H  HB2  A ASN   B 1 159 ? 46.999 -41.279 -6.440  0.56 26.94 ?  159 ASN   B HB2  1 
ATOM   6553 H  HB2  B ASN   B 1 159 ? 47.019 -41.259 -6.594  0.44 26.02 ?  159 ASN   B HB2  1 
ATOM   6554 H  HB3  A ASN   B 1 159 ? 45.884 -42.371 -6.743  0.56 26.94 ?  159 ASN   B HB3  1 
ATOM   6555 H  HB3  B ASN   B 1 159 ? 45.889 -42.334 -6.901  0.44 26.02 ?  159 ASN   B HB3  1 
ATOM   6556 H  HD21 A ASN   B 1 159 ? 49.351 -43.315 -7.545  0.56 29.89 ?  159 ASN   B HD21 1 
ATOM   6557 H  HD21 B ASN   B 1 159 ? 49.324 -43.300 -7.793  0.44 28.05 ?  159 ASN   B HD21 1 
ATOM   6558 H  HD22 A ASN   B 1 159 ? 48.859 -42.473 -6.419  0.56 29.89 ?  159 ASN   B HD22 1 
ATOM   6559 H  HD22 B ASN   B 1 159 ? 48.856 -42.497 -6.629  0.44 28.05 ?  159 ASN   B HD22 1 
ATOM   6560 N  N    . LEU   B 1 160 ? 44.892 -38.980 -6.773  1.00 19.93 ?  160 LEU   B N    1 
ATOM   6561 C  CA   . LEU   B 1 160 ? 43.770 -38.235 -6.209  1.00 19.03 ?  160 LEU   B CA   1 
ATOM   6562 C  C    . LEU   B 1 160 ? 42.972 -37.566 -7.316  1.00 18.00 ?  160 LEU   B C    1 
ATOM   6563 O  O    . LEU   B 1 160 ? 41.735 -37.560 -7.278  1.00 17.83 ?  160 LEU   B O    1 
ATOM   6564 C  CB   . LEU   B 1 160 ? 44.243 -37.203 -5.187  1.00 18.65 ?  160 LEU   B CB   1 
ATOM   6565 C  CG   . LEU   B 1 160 ? 43.114 -36.301 -4.658  1.00 18.08 ?  160 LEU   B CG   1 
ATOM   6566 C  CD1  . LEU   B 1 160 ? 41.998 -37.135 -4.042  1.00 19.25 ?  160 LEU   B CD1  1 
ATOM   6567 C  CD2  . LEU   B 1 160 ? 43.650 -35.291 -3.652  1.00 18.07 ?  160 LEU   B CD2  1 
ATOM   6568 H  H    A LEU   B 1 160 ? 45.666 -38.622 -6.661  0.56 23.94 ?  160 LEU   B H    1 
ATOM   6569 H  H    B LEU   B 1 160 ? 45.671 -38.660 -6.602  0.44 23.94 ?  160 LEU   B H    1 
ATOM   6570 H  HA   . LEU   B 1 160 ? 43.185 -38.862 -5.759  1.00 22.86 ?  160 LEU   B HA   1 
ATOM   6571 H  HB2  . LEU   B 1 160 ? 44.637 -37.674 -4.434  1.00 22.40 ?  160 LEU   B HB2  1 
ATOM   6572 H  HB3  . LEU   B 1 160 ? 44.914 -36.638 -5.606  1.00 22.40 ?  160 LEU   B HB3  1 
ATOM   6573 H  HG   . LEU   B 1 160 ? 42.739 -35.806 -5.400  1.00 21.72 ?  160 LEU   B HG   1 
ATOM   6574 H  HD11 . LEU   B 1 160 ? 41.381 -36.543 -3.591  1.00 23.12 ?  160 LEU   B HD11 1 
ATOM   6575 H  HD12 . LEU   B 1 160 ? 41.537 -37.623 -4.745  1.00 23.12 ?  160 LEU   B HD12 1 
ATOM   6576 H  HD13 . LEU   B 1 160 ? 42.383 -37.761 -3.406  1.00 23.12 ?  160 LEU   B HD13 1 
ATOM   6577 H  HD21 . LEU   B 1 160 ? 42.922 -34.720 -3.368  1.00 21.70 ?  160 LEU   B HD21 1 
ATOM   6578 H  HD22 . LEU   B 1 160 ? 44.018 -35.767 -2.892  1.00 21.70 ?  160 LEU   B HD22 1 
ATOM   6579 H  HD23 . LEU   B 1 160 ? 44.342 -34.760 -4.078  1.00 21.70 ?  160 LEU   B HD23 1 
ATOM   6580 N  N    A TYR   B 1 161 ? 43.664 -37.005 -8.310  0.56 17.94 ?  161 TYR   B N    1 
ATOM   6581 N  N    B TYR   B 1 161 ? 43.659 -37.007 -8.319  0.44 17.96 ?  161 TYR   B N    1 
ATOM   6582 C  CA   A TYR   B 1 161 ? 42.992 -36.445 -9.477  0.56 17.80 ?  161 TYR   B CA   1 
ATOM   6583 C  CA   B TYR   B 1 161 ? 42.969 -36.441 -9.476  0.44 17.90 ?  161 TYR   B CA   1 
ATOM   6584 C  C    A TYR   B 1 161 ? 42.031 -37.462 -10.082 0.56 17.91 ?  161 TYR   B C    1 
ATOM   6585 C  C    B TYR   B 1 161 ? 42.023 -37.464 -10.090 0.44 17.97 ?  161 TYR   B C    1 
ATOM   6586 O  O    A TYR   B 1 161 ? 40.856 -37.163 -10.322 0.56 17.81 ?  161 TYR   B O    1 
ATOM   6587 O  O    B TYR   B 1 161 ? 40.851 -37.170 -10.352 0.44 17.84 ?  161 TYR   B O    1 
ATOM   6588 C  CB   A TYR   B 1 161 ? 44.046 -36.004 -10.501 0.56 18.22 ?  161 TYR   B CB   1 
ATOM   6589 C  CB   B TYR   B 1 161 ? 43.989 -35.953 -10.516 0.44 18.28 ?  161 TYR   B CB   1 
ATOM   6590 C  CG   A TYR   B 1 161 ? 43.476 -35.526 -11.812 0.56 18.51 ?  161 TYR   B CG   1 
ATOM   6591 C  CG   B TYR   B 1 161 ? 43.376 -35.478 -11.822 0.44 18.78 ?  161 TYR   B CG   1 
ATOM   6592 C  CD1  A TYR   B 1 161 ? 43.097 -34.202 -11.979 0.56 18.48 ?  161 TYR   B CD1  1 
ATOM   6593 C  CD1  B TYR   B 1 161 ? 42.992 -34.153 -11.988 0.44 18.85 ?  161 TYR   B CD1  1 
ATOM   6594 C  CD2  A TYR   B 1 161 ? 43.305 -36.399 -12.881 0.56 19.00 ?  161 TYR   B CD2  1 
ATOM   6595 C  CD2  B TYR   B 1 161 ? 43.176 -36.354 -12.885 0.44 19.13 ?  161 TYR   B CD2  1 
ATOM   6596 C  CE1  A TYR   B 1 161 ? 42.574 -33.758 -13.171 0.56 19.58 ?  161 TYR   B CE1  1 
ATOM   6597 C  CE1  B TYR   B 1 161 ? 42.429 -33.712 -13.170 0.44 19.68 ?  161 TYR   B CE1  1 
ATOM   6598 C  CE2  A TYR   B 1 161 ? 42.779 -35.965 -14.076 0.56 20.05 ?  161 TYR   B CE2  1 
ATOM   6599 C  CE2  B TYR   B 1 161 ? 42.611 -35.922 -14.072 0.44 19.92 ?  161 TYR   B CE2  1 
ATOM   6600 C  CZ   A TYR   B 1 161 ? 42.417 -34.644 -14.218 0.56 20.22 ?  161 TYR   B CZ   1 
ATOM   6601 C  CZ   B TYR   B 1 161 ? 42.243 -34.600 -14.210 0.44 20.08 ?  161 TYR   B CZ   1 
ATOM   6602 O  OH   A TYR   B 1 161 ? 41.892 -34.207 -15.408 0.56 22.17 ?  161 TYR   B OH   1 
ATOM   6603 O  OH   B TYR   B 1 161 ? 41.678 -34.166 -15.388 0.44 21.42 ?  161 TYR   B OH   1 
ATOM   6604 H  H    A TYR   B 1 161 ? 44.520 -36.947 -8.336  0.56 21.55 ?  161 TYR   B H    1 
ATOM   6605 H  H    B TYR   B 1 161 ? 44.514 -36.953 -8.356  0.44 21.57 ?  161 TYR   B H    1 
ATOM   6606 H  HA   A TYR   B 1 161 ? 42.482 -35.666 -9.212  0.56 21.38 ?  161 TYR   B HA   1 
ATOM   6607 H  HA   B TYR   B 1 161 ? 42.444 -35.678 -9.193  0.44 21.51 ?  161 TYR   B HA   1 
ATOM   6608 H  HB2  A TYR   B 1 161 ? 44.562 -35.276 -10.122 0.56 21.88 ?  161 TYR   B HB2  1 
ATOM   6609 H  HB2  B TYR   B 1 161 ? 44.486 -35.210 -10.139 0.44 21.96 ?  161 TYR   B HB2  1 
ATOM   6610 H  HB3  A TYR   B 1 161 ? 44.630 -36.755 -10.692 0.56 21.88 ?  161 TYR   B HB3  1 
ATOM   6611 H  HB3  B TYR   B 1 161 ? 44.595 -36.680 -10.725 0.44 21.96 ?  161 TYR   B HB3  1 
ATOM   6612 H  HD1  A TYR   B 1 161 ? 43.205 -33.601 -11.275 0.56 22.19 ?  161 TYR   B HD1  1 
ATOM   6613 H  HD1  B TYR   B 1 161 ? 43.116 -33.549 -11.292 0.44 22.64 ?  161 TYR   B HD1  1 
ATOM   6614 H  HD2  A TYR   B 1 161 ? 43.547 -37.291 -12.789 0.56 22.82 ?  161 TYR   B HD2  1 
ATOM   6615 H  HD2  B TYR   B 1 161 ? 43.422 -37.245 -12.800 0.44 22.98 ?  161 TYR   B HD2  1 
ATOM   6616 H  HE1  A TYR   B 1 161 ? 42.327 -32.864 -13.268 0.56 23.52 ?  161 TYR   B HE1  1 
ATOM   6617 H  HE1  B TYR   B 1 161 ? 42.180 -32.818 -13.266 0.44 23.64 ?  161 TYR   B HE1  1 
ATOM   6618 H  HE2  A TYR   B 1 161 ? 42.668 -36.556 -14.785 0.56 24.08 ?  161 TYR   B HE2  1 
ATOM   6619 H  HE2  B TYR   B 1 161 ? 42.485 -36.516 -14.777 0.44 23.93 ?  161 TYR   B HE2  1 
ATOM   6620 H  HH   A TYR   B 1 161 ? 41.850 -34.840 -15.956 0.56 26.62 ?  161 TYR   B HH   1 
ATOM   6621 H  HH   B TYR   B 1 161 ? 41.624 -34.802 -15.934 0.44 25.73 ?  161 TYR   B HH   1 
ATOM   6622 N  N    . ASP   B 1 162 ? 42.515 -38.685 -10.311 1.00 18.27 ?  162 ASP   B N    1 
ATOM   6623 C  CA   . ASP   B 1 162 ? 41.676 -39.718 -10.909 1.00 18.95 ?  162 ASP   B CA   1 
ATOM   6624 C  C    . ASP   B 1 162 ? 40.480 -40.048 -10.024 1.00 18.49 ?  162 ASP   B C    1 
ATOM   6625 O  O    . ASP   B 1 162 ? 39.371 -40.260 -10.525 1.00 18.78 ?  162 ASP   B O    1 
ATOM   6626 C  CB   . ASP   B 1 162 ? 42.496 -40.987 -11.162 1.00 20.31 ?  162 ASP   B CB   1 
ATOM   6627 C  CG   . ASP   B 1 162 ? 43.525 -40.826 -12.268 1.00 21.83 ?  162 ASP   B CG   1 
ATOM   6628 O  OD1  . ASP   B 1 162 ? 43.415 -39.888 -13.078 1.00 21.99 ?  162 ASP   B OD1  1 
ATOM   6629 O  OD2  . ASP   B 1 162 ? 44.433 -41.681 -12.347 1.00 23.30 -1 162 ASP   B OD2  1 
ATOM   6630 H  H    A ASP   B 1 162 ? 43.317 -38.937 -10.132 0.56 21.94 ?  162 ASP   B H    1 
ATOM   6631 H  H    B ASP   B 1 162 ? 43.317 -38.934 -10.129 0.44 21.94 ?  162 ASP   B H    1 
ATOM   6632 H  HA   . ASP   B 1 162 ? 41.339 -39.403 -11.759 1.00 22.76 ?  162 ASP   B HA   1 
ATOM   6633 H  HB2  . ASP   B 1 162 ? 42.977 -41.221 -10.357 1.00 24.39 ?  162 ASP   B HB2  1 
ATOM   6634 H  HB3  . ASP   B 1 162 ? 41.897 -41.704 -11.418 1.00 24.39 ?  162 ASP   B HB3  1 
ATOM   6635 N  N    . LYS   B 1 163 ? 40.686 -40.120 -8.708  1.00 17.61 ?  163 LYS   B N    1 
ATOM   6636 C  CA   . LYS   B 1 163 ? 39.571 -40.399 -7.810  1.00 18.41 ?  163 LYS   B CA   1 
ATOM   6637 C  C    . LYS   B 1 163 ? 38.532 -39.284 -7.861  1.00 17.42 ?  163 LYS   B C    1 
ATOM   6638 O  O    . LYS   B 1 163 ? 37.320 -39.545 -7.836  1.00 18.35 ?  163 LYS   B O    1 
ATOM   6639 C  CB   . LYS   B 1 163 ? 40.083 -40.580 -6.383  1.00 21.36 ?  163 LYS   B CB   1 
ATOM   6640 C  CG   . LYS   B 1 163 ? 39.005 -41.026 -5.422  1.00 26.53 ?  163 LYS   B CG   1 
ATOM   6641 C  CD   . LYS   B 1 163 ? 39.536 -41.249 -4.020  1.00 31.25 ?  163 LYS   B CD   1 
ATOM   6642 C  CE   . LYS   B 1 163 ? 38.449 -41.829 -3.126  1.00 34.05 ?  163 LYS   B CE   1 
ATOM   6643 N  NZ   . LYS   B 1 163 ? 38.749 -41.679 -1.675  1.00 37.13 ?  163 LYS   B NZ   1 
ATOM   6644 H  H    . LYS   B 1 163 ? 41.448 -40.016 -8.320  1.00 21.16 ?  163 LYS   B H    1 
ATOM   6645 H  HA   . LYS   B 1 163 ? 39.143 -41.224 -8.082  1.00 22.11 ?  163 LYS   B HA   1 
ATOM   6646 H  HB2  . LYS   B 1 163 ? 40.782 -41.257 -6.382  1.00 25.66 ?  163 LYS   B HB2  1 
ATOM   6647 H  HB3  . LYS   B 1 163 ? 40.439 -39.739 -6.064  1.00 25.66 ?  163 LYS   B HB3  1 
ATOM   6648 H  HG2  . LYS   B 1 163 ? 38.317 -40.346 -5.377  1.00 31.86 ?  163 LYS   B HG2  1 
ATOM   6649 H  HG3  . LYS   B 1 163 ? 38.626 -41.864 -5.737  1.00 31.86 ?  163 LYS   B HG3  1 
ATOM   6650 H  HD2  . LYS   B 1 163 ? 40.276 -41.877 -4.052  1.00 37.52 ?  163 LYS   B HD2  1 
ATOM   6651 H  HD3  . LYS   B 1 163 ? 39.825 -40.403 -3.647  1.00 37.52 ?  163 LYS   B HD3  1 
ATOM   6652 H  HE2  . LYS   B 1 163 ? 37.611 -41.381 -3.311  1.00 40.89 ?  163 LYS   B HE2  1 
ATOM   6653 H  HE3  . LYS   B 1 163 ? 38.362 -42.776 -3.317  1.00 40.89 ?  163 LYS   B HE3  1 
ATOM   6654 H  HZ1  . LYS   B 1 163 ? 38.088 -42.029 -1.192  1.00 44.57 ?  163 LYS   B HZ1  1 
ATOM   6655 H  HZ2  . LYS   B 1 163 ? 39.507 -42.099 -1.477  1.00 44.57 ?  163 LYS   B HZ2  1 
ATOM   6656 H  HZ3  . LYS   B 1 163 ? 38.832 -40.817 -1.470  1.00 44.57 ?  163 LYS   B HZ3  1 
ATOM   6657 N  N    . LEU   B 1 164 ? 38.990 -38.032 -7.927  1.00 16.17 ?  164 LEU   B N    1 
ATOM   6658 C  CA   . LEU   B 1 164 ? 38.085 -36.887 -7.978  1.00 15.81 ?  164 LEU   B CA   1 
ATOM   6659 C  C    . LEU   B 1 164 ? 37.297 -36.866 -9.281  1.00 16.42 ?  164 LEU   B C    1 
ATOM   6660 O  O    . LEU   B 1 164 ? 36.075 -36.660 -9.275  1.00 17.37 ?  164 LEU   B O    1 
ATOM   6661 C  CB   . LEU   B 1 164 ? 38.889 -35.596 -7.824  1.00 15.26 ?  164 LEU   B CB   1 
ATOM   6662 C  CG   . LEU   B 1 164 ? 39.427 -35.312 -6.425  1.00 15.93 ?  164 LEU   B CG   1 
ATOM   6663 C  CD1  . LEU   B 1 164 ? 40.516 -34.248 -6.495  1.00 15.86 ?  164 LEU   B CD1  1 
ATOM   6664 C  CD2  . LEU   B 1 164 ? 38.320 -34.874 -5.486  1.00 17.79 ?  164 LEU   B CD2  1 
ATOM   6665 H  H    . LEU   B 1 164 ? 39.828 -37.819 -7.948  1.00 19.43 ?  164 LEU   B H    1 
ATOM   6666 H  HA   . LEU   B 1 164 ? 37.460 -36.945 -7.248  1.00 18.99 ?  164 LEU   B HA   1 
ATOM   6667 H  HB2  . LEU   B 1 164 ? 39.652 -35.633 -8.426  1.00 18.33 ?  164 LEU   B HB2  1 
ATOM   6668 H  HB3  . LEU   B 1 164 ? 38.323 -34.851 -8.070  1.00 18.33 ?  164 LEU   B HB3  1 
ATOM   6669 H  HG   . LEU   B 1 164 ? 39.831 -36.118 -6.069  1.00 19.13 ?  164 LEU   B HG   1 
ATOM   6670 H  HD11 . LEU   B 1 164 ? 40.849 -34.069 -5.598  1.00 19.06 ?  164 LEU   B HD11 1 
ATOM   6671 H  HD12 . LEU   B 1 164 ? 41.248 -34.570 -7.052  1.00 19.06 ?  164 LEU   B HD12 1 
ATOM   6672 H  HD13 . LEU   B 1 164 ? 40.150 -33.435 -6.877  1.00 19.06 ?  164 LEU   B HD13 1 
ATOM   6673 H  HD21 . LEU   B 1 164 ? 38.703 -34.655 -4.623  1.00 21.37 ?  164 LEU   B HD21 1 
ATOM   6674 H  HD22 . LEU   B 1 164 ? 37.878 -34.095 -5.860  1.00 21.37 ?  164 LEU   B HD22 1 
ATOM   6675 H  HD23 . LEU   B 1 164 ? 37.685 -35.601 -5.393  1.00 21.37 ?  164 LEU   B HD23 1 
ATOM   6676 N  N    . VAL   B 1 165 ? 37.981 -37.046 -10.411 1.00 18.37 ?  165 VAL   B N    1 
ATOM   6677 C  CA   . VAL   B 1 165 ? 37.315 -36.980 -11.708 1.00 20.33 ?  165 VAL   B CA   1 
ATOM   6678 C  C    . VAL   B 1 165 ? 36.373 -38.164 -11.878 1.00 22.45 ?  165 VAL   B C    1 
ATOM   6679 O  O    . VAL   B 1 165 ? 35.204 -38.007 -12.258 1.00 23.45 ?  165 VAL   B O    1 
ATOM   6680 C  CB   . VAL   B 1 165 ? 38.350 -36.918 -12.847 1.00 21.23 ?  165 VAL   B CB   1 
ATOM   6681 C  CG1  . VAL   B 1 165 ? 37.664 -37.049 -14.187 1.00 22.82 ?  165 VAL   B CG1  1 
ATOM   6682 C  CG2  . VAL   B 1 165 ? 39.144 -35.624 -12.782 1.00 20.60 ?  165 VAL   B CG2  1 
ATOM   6683 H  H    . VAL   B 1 165 ? 38.830 -37.203 -10.455 1.00 22.06 ?  165 VAL   B H    1 
ATOM   6684 H  HA   . VAL   B 1 165 ? 36.787 -36.171 -11.750 1.00 24.42 ?  165 VAL   B HA   1 
ATOM   6685 H  HB   . VAL   B 1 165 ? 38.980 -37.650 -12.752 1.00 25.50 ?  165 VAL   B HB   1 
ATOM   6686 H  HG11 . VAL   B 1 165 ? 38.254 -36.723 -14.882 1.00 27.41 ?  165 VAL   B HG11 1 
ATOM   6687 H  HG12 . VAL   B 1 165 ? 37.466 -37.987 -14.343 1.00 27.41 ?  165 VAL   B HG12 1 
ATOM   6688 H  HG13 . VAL   B 1 165 ? 36.844 -36.536 -14.175 1.00 27.41 ?  165 VAL   B HG13 1 
ATOM   6689 H  HG21 . VAL   B 1 165 ? 39.749 -35.581 -13.542 1.00 24.74 ?  165 VAL   B HG21 1 
ATOM   6690 H  HG22 . VAL   B 1 165 ? 38.528 -34.872 -12.814 1.00 24.74 ?  165 VAL   B HG22 1 
ATOM   6691 H  HG23 . VAL   B 1 165 ? 39.652 -35.598 -11.957 1.00 24.74 ?  165 VAL   B HG23 1 
ATOM   6692 N  N    . SER   B 1 166 ? 36.875 -39.371 -11.589 1.00 23.66 ?  166 SER   B N    1 
ATOM   6693 C  CA   . SER   B 1 166 ? 36.118 -40.578 -11.883 1.00 24.71 ?  166 SER   B CA   1 
ATOM   6694 C  C    . SER   B 1 166 ? 34.863 -40.670 -11.031 1.00 25.05 ?  166 SER   B C    1 
ATOM   6695 O  O    . SER   B 1 166 ? 33.894 -41.304 -11.447 1.00 26.50 ?  166 SER   B O    1 
ATOM   6696 C  CB   . SER   B 1 166 ? 36.983 -41.836 -11.716 1.00 25.23 ?  166 SER   B CB   1 
ATOM   6697 O  OG   . SER   B 1 166 ? 37.360 -42.045 -10.365 1.00 25.31 ?  166 SER   B OG   1 
ATOM   6698 H  H    . SER   B 1 166 ? 37.649 -39.512 -11.229 1.00 28.41 ?  166 SER   B H    1 
ATOM   6699 H  HA   . SER   B 1 166 ? 35.841 -40.548 -12.812 1.00 29.67 ?  166 SER   B HA   1 
ATOM   6700 H  HB2  . SER   B 1 166 ? 36.478 -42.607 -12.020 1.00 30.30 ?  166 SER   B HB2  1 
ATOM   6701 H  HB3  . SER   B 1 166 ? 37.786 -41.739 -12.256 1.00 30.30 ?  166 SER   B HB3  1 
ATOM   6702 H  HG   . SER   B 1 166 ? 37.809 -41.387 -10.091 1.00 30.39 ?  166 SER   B HG   1 
ATOM   6703 N  N    . SER   B 1 167 ? 34.850 -40.055 -9.852  1.00 23.00 ?  167 SER   B N    1 
ATOM   6704 C  CA   . SER   B 1 167 ? 33.697 -40.106 -8.961  1.00 22.27 ?  167 SER   B CA   1 
ATOM   6705 C  C    . SER   B 1 167 ? 32.790 -38.876 -9.046  1.00 21.61 ?  167 SER   B C    1 
ATOM   6706 O  O    . SER   B 1 167 ? 31.709 -38.880 -8.447  1.00 21.82 ?  167 SER   B O    1 
ATOM   6707 C  CB   . SER   B 1 167 ? 34.156 -40.307 -7.509  1.00 22.33 ?  167 SER   B CB   1 
ATOM   6708 O  OG   . SER   B 1 167 ? 34.819 -39.144 -7.018  1.00 22.33 ?  167 SER   B OG   1 
ATOM   6709 H  H    . SER   B 1 167 ? 35.505 -39.601 -9.547  1.00 27.62 ?  167 SER   B H    1 
ATOM   6710 H  HA   . SER   B 1 167 ? 33.159 -40.878 -9.205  1.00 26.75 ?  167 SER   B HA   1 
ATOM   6711 H  HB2  . SER   B 1 167 ? 33.376 -40.495 -6.962  1.00 26.81 ?  167 SER   B HB2  1 
ATOM   6712 H  HB3  . SER   B 1 167 ? 34.763 -41.071 -7.479  1.00 26.81 ?  167 SER   B HB3  1 
ATOM   6713 H  HG   . SER   B 1 167 ? 35.496 -38.997 -7.481  1.00 26.82 ?  167 SER   B HG   1 
ATOM   6714 N  N    . PHE   B 1 168 ? 33.182 -37.827 -9.771  1.00 21.56 ?  168 PHE   B N    1 
ATOM   6715 C  CA   . PHE   B 1 168 ? 32.338 -36.631 -9.845  1.00 19.87 ?  168 PHE   B CA   1 
ATOM   6716 C  C    . PHE   B 1 168 ? 31.044 -36.903 -10.609 1.00 16.76 ?  168 PHE   B C    1 
ATOM   6717 O  O    . PHE   B 1 168 ? 29.979 -36.338 -10.282 1.00 17.16 ?  168 PHE   B O    1 
ATOM   6718 C  CB   . PHE   B 1 168 ? 33.109 -35.489 -10.501 1.00 20.66 ?  168 PHE   B CB   1 
ATOM   6719 C  CG   . PHE   B 1 168 ? 32.297 -34.249 -10.682 1.00 20.69 ?  168 PHE   B CG   1 
ATOM   6720 C  CD1  . PHE   B 1 168 ? 31.921 -33.494 -9.582  1.00 21.97 ?  168 PHE   B CD1  1 
ATOM   6721 C  CD2  . PHE   B 1 168 ? 31.884 -33.848 -11.938 1.00 19.96 ?  168 PHE   B CD2  1 
ATOM   6722 C  CE1  . PHE   B 1 168 ? 31.156 -32.352 -9.730  1.00 21.78 ?  168 PHE   B CE1  1 
ATOM   6723 C  CE2  . PHE   B 1 168 ? 31.127 -32.695 -12.098 1.00 21.01 ?  168 PHE   B CE2  1 
ATOM   6724 C  CZ   . PHE   B 1 168 ? 30.757 -31.949 -10.989 1.00 21.32 ?  168 PHE   B CZ   1 
ATOM   6725 H  H    . PHE   B 1 168 ? 33.913 -37.782 -10.221 1.00 25.90 ?  168 PHE   B H    1 
ATOM   6726 H  HA   . PHE   B 1 168 ? 32.099 -36.359 -8.949  1.00 23.86 ?  168 PHE   B HA   1 
ATOM   6727 H  HB2  . PHE   B 1 168 ? 33.870 -35.265 -9.944  1.00 24.82 ?  168 PHE   B HB2  1 
ATOM   6728 H  HB3  . PHE   B 1 168 ? 33.412 -35.773 -11.377 1.00 24.82 ?  168 PHE   B HB3  1 
ATOM   6729 H  HD1  . PHE   B 1 168 ? 32.183 -33.762 -8.733  1.00 26.38 ?  168 PHE   B HD1  1 
ATOM   6730 H  HD2  . PHE   B 1 168 ? 32.129 -34.341 -12.683 1.00 23.98 ?  168 PHE   B HD2  1 
ATOM   6731 H  HE1  . PHE   B 1 168 ? 30.912 -31.856 -8.985  1.00 26.16 ?  168 PHE   B HE1  1 
ATOM   6732 H  HE2  . PHE   B 1 168 ? 30.855 -32.430 -12.950 1.00 25.23 ?  168 PHE   B HE2  1 
ATOM   6733 H  HZ   . PHE   B 1 168 ? 30.242 -31.181 -11.096 1.00 25.61 ?  168 PHE   B HZ   1 
ATOM   6734 N  N    . LEU   B 1 169 ? 31.119 -37.765 -11.620 1.00 16.73 ?  169 LEU   B N    1 
ATOM   6735 C  CA   . LEU   B 1 169 ? 29.963 -38.097 -12.443 1.00 19.32 ?  169 LEU   B CA   1 
ATOM   6736 C  C    . LEU   B 1 169 ? 29.947 -39.545 -12.919 1.00 22.53 ?  169 LEU   B C    1 
ATOM   6737 O  O    . LEU   B 1 169 ? 29.033 -39.969 -13.634 1.00 24.81 ?  169 LEU   B O    1 
ATOM   6738 C  CB   . LEU   B 1 169 ? 29.910 -37.189 -13.668 1.00 21.32 ?  169 LEU   B CB   1 
ATOM   6739 C  CG   . LEU   B 1 169 ? 28.686 -36.283 -13.767 1.00 24.59 ?  169 LEU   B CG   1 
ATOM   6740 C  CD1  . LEU   B 1 169 ? 28.618 -35.670 -15.146 1.00 25.72 ?  169 LEU   B CD1  1 
ATOM   6741 C  CD2  . LEU   B 1 169 ? 27.406 -37.042 -13.453 1.00 24.38 ?  169 LEU   B CD2  1 
ATOM   6742 O  OXT  . LEU   B 1 169 ? 30.841 -40.320 -12.609 1.00 23.35 -1 169 LEU   B OXT  1 
ATOM   6743 H  H    . LEU   B 1 169 ? 31.840 -38.171 -11.860 1.00 20.10 ?  169 LEU   B H    1 
ATOM   6744 H  HA   . LEU   B 1 169 ? 29.171 -37.945 -11.910 1.00 23.20 ?  169 LEU   B HA   1 
ATOM   6745 H  HB2  . LEU   B 1 169 ? 30.693 -36.616 -13.667 1.00 25.61 ?  169 LEU   B HB2  1 
ATOM   6746 H  HB3  . LEU   B 1 169 ? 29.918 -37.743 -14.465 1.00 25.61 ?  169 LEU   B HB3  1 
ATOM   6747 H  HG   . LEU   B 1 169 ? 28.771 -35.559 -13.123 1.00 29.53 ?  169 LEU   B HG   1 
ATOM   6748 H  HD11 . LEU   B 1 169 ? 27.856 -35.071 -15.188 1.00 30.89 ?  169 LEU   B HD11 1 
ATOM   6749 H  HD12 . LEU   B 1 169 ? 29.437 -35.177 -15.310 1.00 30.89 ?  169 LEU   B HD12 1 
ATOM   6750 H  HD13 . LEU   B 1 169 ? 28.520 -36.379 -15.799 1.00 30.89 ?  169 LEU   B HD13 1 
ATOM   6751 H  HD21 . LEU   B 1 169 ? 26.665 -36.621 -13.910 1.00 29.28 ?  169 LEU   B HD21 1 
ATOM   6752 H  HD22 . LEU   B 1 169 ? 27.505 -37.960 -13.759 1.00 29.28 ?  169 LEU   B HD22 1 
ATOM   6753 H  HD23 . LEU   B 1 169 ? 27.258 -37.030 -12.495 1.00 29.28 ?  169 LEU   B HD23 1 
HETATM 6754 S  S    B DMS   C 2 .   ? 6.369  4.241   4.235   0.44 18.82 ?  401 DMS   A S    1 
HETATM 6755 O  O    B DMS   C 2 .   ? 5.578  3.000   4.569   0.44 17.67 ?  401 DMS   A O    1 
HETATM 6756 C  C1   B DMS   C 2 .   ? 7.759  4.353   5.411   0.44 18.87 ?  401 DMS   A C1   1 
HETATM 6757 C  C2   B DMS   C 2 .   ? 5.364  5.649   4.812   0.44 19.17 ?  401 DMS   A C2   1 
HETATM 6758 H  H11  B DMS   C 2 .   ? 8.271  5.224   5.174   0.44 22.67 ?  401 DMS   A H11  1 
HETATM 6759 H  H12  B DMS   C 2 .   ? 8.344  3.502   5.284   0.44 22.67 ?  401 DMS   A H12  1 
HETATM 6760 H  H13  B DMS   C 2 .   ? 7.309  4.391   6.346   0.44 22.67 ?  401 DMS   A H13  1 
HETATM 6761 H  H21  B DMS   C 2 .   ? 5.452  5.628   5.842   0.44 23.03 ?  401 DMS   A H21  1 
HETATM 6762 H  H22  B DMS   C 2 .   ? 5.783  6.506   4.389   0.44 23.03 ?  401 DMS   A H22  1 
HETATM 6763 H  H23  B DMS   C 2 .   ? 4.391  5.484   4.489   0.44 23.03 ?  401 DMS   A H23  1 
HETATM 6764 N  N2   B A1A56 D 3 .   ? 15.240 0.982   1.913   0.22 7.95  ?  402 A1A56 A N2   1 
HETATM 6765 C  C3   B A1A56 D 3 .   ? 15.275 0.189   -0.392  0.22 9.18  ?  402 A1A56 A C3   1 
HETATM 6766 C  C6   B A1A56 D 3 .   ? 15.047 -0.112  5.384   0.22 8.21  ?  402 A1A56 A C6   1 
HETATM 6767 C  C9   B A1A56 D 3 .   ? 15.536 3.729   3.885   0.22 8.60  ?  402 A1A56 A C9   1 
HETATM 6768 C  C1   B A1A56 D 3 .   ? 13.294 1.792   -0.560  0.22 11.62 ?  402 A1A56 A C1   1 
HETATM 6769 C  C10  B A1A56 D 3 .   ? 15.584 4.328   5.141   0.22 7.84  ?  402 A1A56 A C10  1 
HETATM 6770 C  C11  B A1A56 D 3 .   ? 15.229 2.151   1.004   0.22 8.54  ?  402 A1A56 A C11  1 
HETATM 6771 C  C2   B A1A56 D 3 .   ? 14.811 1.664   -0.416  0.22 9.74  ?  402 A1A56 A C2   1 
HETATM 6772 C  C4   B A1A56 D 3 .   ? 15.160 -0.254  1.102   0.22 8.55  ?  402 A1A56 A C4   1 
HETATM 6773 C  C5   B A1A56 D 3 .   ? 15.216 1.051   3.319   0.22 8.23  ?  402 A1A56 A C5   1 
HETATM 6774 C  C7   B A1A56 D 3 .   ? 15.313 2.120   5.479   0.22 8.08  ?  402 A1A56 A C7   1 
HETATM 6775 C  C8   B A1A56 D 3 .   ? 15.352 2.289   4.058   0.22 8.42  ?  402 A1A56 A C8   1 
HETATM 6776 N  N1   B A1A56 D 3 .   ? 12.729 2.676   -1.485  0.22 11.95 ?  402 A1A56 A N1   1 
HETATM 6777 N  N3   B A1A56 D 3 .   ? 15.086 -0.118  4.011   0.22 8.44  ?  402 A1A56 A N3   1 
HETATM 6778 N  N4   B A1A56 D 3 .   ? 15.159 0.957   6.152   0.22 7.66  ?  402 A1A56 A N4   1 
HETATM 6779 N  N5   B A1A56 D 3 .   ? 15.442 3.331   6.080   0.22 7.91  ?  402 A1A56 A N5   1 
HETATM 6780 O  O1   B A1A56 D 3 .   ? 12.604 1.097   0.171   0.22 11.81 ?  402 A1A56 A O1   1 
HETATM 6781 O  O2   B A1A56 D 3 .   ? 15.481 2.447   -1.381  0.22 9.80  ?  402 A1A56 A O2   1 
HETATM 6782 H  H4   B A1A56 D 3 .   ? 16.291 0.069   -0.808  0.22 11.03 ?  402 A1A56 A H4   1 
HETATM 6783 H  H5   B A1A56 D 3 .   ? 14.650 -0.446  -1.084  0.22 11.03 ?  402 A1A56 A H5   1 
HETATM 6784 H  H8   B A1A56 D 3 .   ? 14.918 -1.064  5.967   0.22 9.87  ?  402 A1A56 A H8   1 
HETATM 6785 H  H9   B A1A56 D 3 .   ? 15.615 4.296   2.997   0.22 10.34 ?  402 A1A56 A H9   1 
HETATM 6786 H  H10  B A1A56 D 3 .   ? 15.691 5.318   5.538   0.22 9.43  ?  402 A1A56 A H10  1 
HETATM 6787 H  H13  B A1A56 D 3 .   ? 14.553 2.970   1.313   0.22 10.27 ?  402 A1A56 A H13  1 
HETATM 6788 H  H12  B A1A56 D 3 .   ? 16.249 2.610   0.928   0.22 10.27 ?  402 A1A56 A H12  1 
HETATM 6789 H  H7   B A1A56 D 3 .   ? 15.972 -0.959  1.353   0.22 10.28 ?  402 A1A56 A H7   1 
HETATM 6790 H  H6   B A1A56 D 3 .   ? 14.236 -0.849  1.252   0.22 10.28 ?  402 A1A56 A H6   1 
HETATM 6791 H  H2   B A1A56 D 3 .   ? 13.258 3.261   -2.090  0.22 14.36 ?  402 A1A56 A H2   1 
HETATM 6792 H  H1   B A1A56 D 3 .   ? 11.758 2.792   -1.607  0.22 14.36 ?  402 A1A56 A H1   1 
HETATM 6793 H  H11  B A1A56 D 3 .   ? 15.446 3.500   7.096   0.22 9.52  ?  402 A1A56 A H11  1 
HETATM 6794 H  H3   B A1A56 D 3 .   ? 15.930 1.885   -2.029  0.22 11.79 ?  402 A1A56 A H3   1 
HETATM 6795 O  O1   C A1A57 E 4 .   ? 15.718 10.190  7.050   0.22 20.97 ?  403 A1A57 A O1   1 
HETATM 6796 C  C1   C A1A57 E 4 .   ? 14.498 10.170  7.152   0.22 20.57 ?  403 A1A57 A C1   1 
HETATM 6797 C  C2   C A1A57 E 4 .   ? 13.704 8.905   6.618   0.22 20.33 ?  403 A1A57 A C2   1 
HETATM 6798 C  C3   C A1A57 E 4 .   ? 13.475 9.079   5.128   0.22 19.96 ?  403 A1A57 A C3   1 
HETATM 6799 C  C4   C A1A57 E 4 .   ? 14.778 8.537   4.511   0.22 19.65 ?  403 A1A57 A C4   1 
HETATM 6800 C  C5   C A1A57 E 4 .   ? 15.245 6.047   4.402   0.22 17.32 ?  403 A1A57 A C5   1 
HETATM 6801 C  C6   C A1A57 E 4 .   ? 15.521 5.268   2.131   0.22 16.89 ?  403 A1A57 A C6   1 
HETATM 6802 C  C7   C A1A57 E 4 .   ? 15.416 3.696   3.704   0.22 16.27 ?  403 A1A57 A C7   1 
HETATM 6803 C  C8   C A1A57 E 4 .   ? 15.261 4.646   4.806   0.22 16.40 ?  403 A1A57 A C8   1 
HETATM 6804 C  C10  C A1A57 E 4 .   ? 15.266 2.449   5.565   0.22 16.03 ?  403 A1A57 A C10  1 
HETATM 6805 C  C11  C A1A57 E 4 .   ? 14.538 7.499   6.630   0.22 20.15 ?  403 A1A57 A C11  1 
HETATM 6806 C  C9   C A1A57 E 4 .   ? 15.167 3.772   5.978   0.22 16.07 ?  403 A1A57 A C9   1 
HETATM 6807 N  N1   C A1A57 E 4 .   ? 13.818 11.288  7.708   0.22 20.76 ?  403 A1A57 A N1   1 
HETATM 6808 N  N2   C A1A57 E 4 .   ? 15.102 7.276   5.220   0.22 19.14 ?  403 A1A57 A N2   1 
HETATM 6809 N  N3   C A1A57 E 4 .   ? 15.383 6.272   3.061   0.22 16.99 ?  403 A1A57 A N3   1 
HETATM 6810 N  N4   C A1A57 E 4 .   ? 15.546 3.963   2.370   0.22 16.99 ?  403 A1A57 A N4   1 
HETATM 6811 N  N5   C A1A57 E 4 .   ? 15.411 2.436   4.207   0.22 16.01 ?  403 A1A57 A N5   1 
HETATM 6812 O  O2   C A1A57 E 4 .   ? 12.511 8.775   7.325   0.22 20.44 ?  403 A1A57 A O2   1 
HETATM 6813 H  H4   C A1A57 E 4 .   ? 12.560 8.552   4.755   0.22 23.97 ?  403 A1A57 A H4   1 
HETATM 6814 H  H5   C A1A57 E 4 .   ? 13.283 10.147  4.860   0.22 23.97 ?  403 A1A57 A H5   1 
HETATM 6815 H  H6   C A1A57 E 4 .   ? 15.579 9.300   4.566   0.22 23.60 ?  403 A1A57 A H6   1 
HETATM 6816 H  H7   C A1A57 E 4 .   ? 14.622 8.408   3.409   0.22 23.60 ?  403 A1A57 A H7   1 
HETATM 6817 H  H8   C A1A57 E 4 .   ? 15.625 5.535   1.065   0.22 20.29 ?  403 A1A57 A H8   1 
HETATM 6818 H  H10  C A1A57 E 4 .   ? 15.255 1.472   6.044   0.22 19.25 ?  403 A1A57 A H10  1 
HETATM 6819 H  H12  C A1A57 E 4 .   ? 15.351 7.576   7.399   0.22 24.20 ?  403 A1A57 A H12  1 
HETATM 6820 H  H13  C A1A57 E 4 .   ? 13.865 6.690   6.986   0.22 24.20 ?  403 A1A57 A H13  1 
HETATM 6821 H  H9   C A1A57 E 4 .   ? 15.046 4.016   7.027   0.22 19.31 ?  403 A1A57 A H9   1 
HETATM 6822 H  H2   C A1A57 E 4 .   ? 12.818 11.337  7.809   0.22 24.94 ?  403 A1A57 A H2   1 
HETATM 6823 H  H1   C A1A57 E 4 .   ? 14.292 12.105  8.040   0.22 24.94 ?  403 A1A57 A H1   1 
HETATM 6824 H  H11  C A1A57 E 4 .   ? 15.507 1.575   3.661   0.22 19.24 ?  403 A1A57 A H11  1 
HETATM 6825 H  H3   C A1A57 E 4 .   ? 12.649 8.319   8.173   0.22 24.56 ?  403 A1A57 A H3   1 
HETATM 6826 CL CL   B CL    F 5 .   ? 18.481 2.005   -0.954  0.44 16.37 ?  404 CL    A CL   1 
HETATM 6827 O  O    . HOH   G 6 .   ? 17.688 -1.752  0.259   1.00 29.45 ?  501 HOH   A O    1 
HETATM 6828 O  O    B HOH   G 6 .   ? 10.507 2.404   -1.627  0.44 40.54 ?  502 HOH   A O    1 
HETATM 6829 O  O    . HOH   G 6 .   ? 11.883 0.371   14.656  1.00 33.64 ?  503 HOH   A O    1 
HETATM 6830 O  O    A HOH   G 6 .   ? 14.734 -4.574  20.384  0.56 37.30 ?  504 HOH   A O    1 
HETATM 6831 O  O    . HOH   G 6 .   ? 7.644  -6.345  -6.710  1.00 40.86 ?  505 HOH   A O    1 
HETATM 6832 O  O    . HOH   G 6 .   ? 15.714 2.207   24.414  1.00 48.02 ?  506 HOH   A O    1 
HETATM 6833 O  O    A HOH   G 6 .   ? 15.190 -12.257 18.560  0.56 31.58 ?  507 HOH   A O    1 
HETATM 6834 O  O    . HOH   G 6 .   ? -0.661 -8.492  2.122   1.00 45.91 ?  508 HOH   A O    1 
HETATM 6835 O  O    . HOH   G 6 .   ? 28.972 0.482   -9.708  1.00 23.20 ?  509 HOH   A O    1 
HETATM 6836 O  O    . HOH   G 6 .   ? 19.536 -11.156 24.127  1.00 78.84 ?  510 HOH   A O    1 
HETATM 6837 O  O    . HOH   G 6 .   ? 34.354 -1.865  12.513  1.00 38.42 ?  511 HOH   A O    1 
HETATM 6838 O  O    . HOH   G 6 .   ? 16.964 -17.856 15.116  1.00 28.47 ?  512 HOH   A O    1 
HETATM 6839 O  O    A HOH   G 6 .   ? 4.676  3.926   0.553   0.56 22.21 ?  513 HOH   A O    1 
HETATM 6840 O  O    . HOH   G 6 .   ? 0.876  -4.245  -0.082  1.00 32.57 ?  514 HOH   A O    1 
HETATM 6841 O  O    . HOH   G 6 .   ? 18.902 -21.952 7.012   1.00 36.53 ?  515 HOH   A O    1 
HETATM 6842 O  O    B HOH   G 6 .   ? 18.418 -0.867  -2.486  0.44 20.48 ?  516 HOH   A O    1 
HETATM 6843 O  O    . HOH   G 6 .   ? 20.025 -12.583 -8.894  1.00 26.56 ?  517 HOH   A O    1 
HETATM 6844 O  O    . HOH   G 6 .   ? 7.905  -12.530 -1.062  1.00 22.98 ?  518 HOH   A O    1 
HETATM 6845 O  O    B HOH   G 6 .   ? 16.713 -2.825  -1.628  0.44 20.96 ?  519 HOH   A O    1 
HETATM 6846 O  O    . HOH   G 6 .   ? 30.228 -13.299 -8.437  1.00 21.45 ?  520 HOH   A O    1 
HETATM 6847 O  O    . HOH   G 6 .   ? 28.101 -6.214  19.640  1.00 42.71 ?  521 HOH   A O    1 
HETATM 6848 O  O    . HOH   G 6 .   ? 14.204 -4.543  -11.991 1.00 35.15 ?  522 HOH   A O    1 
HETATM 6849 O  O    A HOH   G 6 .   ? 14.710 -13.968 16.647  0.56 23.16 ?  523 HOH   A O    1 
HETATM 6850 O  O    B HOH   G 6 .   ? 8.784  3.835   0.585   0.44 23.47 ?  524 HOH   A O    1 
HETATM 6851 O  O    . HOH   G 6 .   ? 16.988 -19.250 4.879   1.00 16.04 ?  525 HOH   A O    1 
HETATM 6852 O  O    A HOH   G 6 .   ? -0.499 -3.082  3.032   0.56 30.87 ?  526 HOH   A O    1 
HETATM 6853 O  O    . HOH   G 6 .   ? 22.227 5.321   18.959  1.00 45.64 ?  527 HOH   A O    1 
HETATM 6854 O  O    . HOH   G 6 .   ? 42.329 10.561  5.081   1.00 20.64 ?  528 HOH   A O    1 
HETATM 6855 O  O    . HOH   G 6 .   ? 9.861  -21.364 5.591   1.00 20.99 ?  529 HOH   A O    1 
HETATM 6856 O  O    . HOH   G 6 .   ? 24.177 -7.719  14.428  1.00 17.16 ?  530 HOH   A O    1 
HETATM 6857 O  O    . HOH   G 6 .   ? 11.785 -10.971 -10.176 1.00 50.03 ?  531 HOH   A O    1 
HETATM 6858 O  O    . HOH   G 6 .   ? 14.883 3.956   17.598  1.00 41.29 ?  532 HOH   A O    1 
HETATM 6859 O  O    . HOH   G 6 .   ? 28.385 -0.188  -13.402 1.00 39.35 ?  533 HOH   A O    1 
HETATM 6860 O  O    . HOH   G 6 .   ? 9.099  -10.163 19.193  1.00 42.42 ?  534 HOH   A O    1 
HETATM 6861 O  O    . HOH   G 6 .   ? 38.191 10.275  7.097   1.00 46.16 ?  535 HOH   A O    1 
HETATM 6862 O  O    . HOH   G 6 .   ? 36.132 -5.099  -0.482  1.00 31.37 ?  536 HOH   A O    1 
HETATM 6863 O  O    . HOH   G 6 .   ? 14.542 -0.618  -12.336 1.00 24.88 ?  537 HOH   A O    1 
HETATM 6864 O  O    . HOH   G 6 .   ? 37.447 2.843   10.285  1.00 23.93 ?  538 HOH   A O    1 
HETATM 6865 O  O    . HOH   G 6 .   ? 15.257 -8.081  -9.990  1.00 25.59 ?  539 HOH   A O    1 
HETATM 6866 O  O    A HOH   G 6 .   ? 6.911  -8.144  11.799  0.56 18.09 ?  540 HOH   A O    1 
HETATM 6867 O  O    . HOH   G 6 .   ? 43.295 7.723   2.687   1.00 36.46 ?  541 HOH   A O    1 
HETATM 6868 O  O    . HOH   G 6 .   ? 22.496 -11.927 21.831  1.00 54.32 ?  542 HOH   A O    1 
HETATM 6869 O  O    . HOH   G 6 .   ? 14.049 -23.019 7.357   1.00 18.99 ?  543 HOH   A O    1 
HETATM 6870 O  O    . HOH   G 6 .   ? 44.291 7.200   6.433   1.00 28.13 ?  544 HOH   A O    1 
HETATM 6871 O  O    A HOH   G 6 .   ? 14.246 0.588   6.758   0.78 28.78 ?  545 HOH   A O    1 
HETATM 6872 O  O    B HOH   G 6 .   ? 14.955 -2.888  3.332   0.44 13.03 ?  546 HOH   A O    1 
HETATM 6873 O  O    A HOH   G 6 .   ? 3.566  -9.448  9.676   0.56 31.99 ?  547 HOH   A O    1 
HETATM 6874 O  O    . HOH   G 6 .   ? 23.884 -15.734 -9.205  1.00 35.00 ?  548 HOH   A O    1 
HETATM 6875 O  O    . HOH   G 6 .   ? 13.626 -15.300 -7.633  1.00 26.67 ?  549 HOH   A O    1 
HETATM 6876 O  O    . HOH   G 6 .   ? 38.509 5.003   7.038   1.00 15.56 ?  550 HOH   A O    1 
HETATM 6877 O  O    A HOH   G 6 .   ? 15.501 11.931  8.005   0.78 45.13 ?  551 HOH   A O    1 
HETATM 6878 O  O    . HOH   G 6 .   ? 27.312 13.788  2.815   1.00 31.44 ?  552 HOH   A O    1 
HETATM 6879 O  O    . HOH   G 6 .   ? 31.015 -18.079 7.821   1.00 18.66 ?  553 HOH   A O    1 
HETATM 6880 O  O    . HOH   G 6 .   ? 20.676 -19.794 -5.045  1.00 28.25 ?  554 HOH   A O    1 
HETATM 6881 O  O    . HOH   G 6 .   ? 18.605 -19.339 13.536  1.00 32.22 ?  555 HOH   A O    1 
HETATM 6882 O  O    . HOH   G 6 .   ? 34.027 -1.171  -8.925  1.00 26.74 ?  556 HOH   A O    1 
HETATM 6883 O  O    . HOH   G 6 .   ? 25.727 -0.787  -7.367  1.00 17.81 ?  557 HOH   A O    1 
HETATM 6884 O  O    A HOH   G 6 .   ? 14.614 -3.642  3.060   0.56 17.49 ?  558 HOH   A O    1 
HETATM 6885 O  O    . HOH   G 6 .   ? 31.615 8.227   14.842  1.00 25.19 ?  559 HOH   A O    1 
HETATM 6886 O  O    . HOH   G 6 .   ? 10.877 1.715   12.441  1.00 23.28 ?  560 HOH   A O    1 
HETATM 6887 O  O    . HOH   G 6 .   ? 6.549  -3.186  12.568  1.00 33.40 ?  561 HOH   A O    1 
HETATM 6888 O  O    . HOH   G 6 .   ? 39.753 -1.028  -5.123  1.00 21.73 ?  562 HOH   A O    1 
HETATM 6889 O  O    . HOH   G 6 .   ? 26.810 11.421  1.645   1.00 17.30 ?  563 HOH   A O    1 
HETATM 6890 O  O    . HOH   G 6 .   ? 42.567 4.330   5.550   1.00 36.12 ?  564 HOH   A O    1 
HETATM 6891 O  O    . HOH   G 6 .   ? 27.569 -6.204  -13.956 1.00 39.67 ?  565 HOH   A O    1 
HETATM 6892 O  O    . HOH   G 6 .   ? 14.370 -21.299 -4.250  1.00 29.40 ?  566 HOH   A O    1 
HETATM 6893 O  O    . HOH   G 6 .   ? 35.756 -12.620 6.881   1.00 15.87 ?  567 HOH   A O    1 
HETATM 6894 O  O    . HOH   G 6 .   ? 13.291 -1.477  -6.882  1.00 20.17 ?  568 HOH   A O    1 
HETATM 6895 O  O    B HOH   G 6 .   ? 21.159 -2.210  -2.777  0.44 13.30 ?  569 HOH   A O    1 
HETATM 6896 O  O    . HOH   G 6 .   ? 24.024 -2.117  -2.110  1.00 11.18 ?  570 HOH   A O    1 
HETATM 6897 O  O    . HOH   G 6 .   ? 37.120 -2.831  9.795   1.00 48.23 ?  571 HOH   A O    1 
HETATM 6898 O  O    . HOH   G 6 .   ? 22.700 12.479  1.558   1.00 15.52 ?  572 HOH   A O    1 
HETATM 6899 O  O    B HOH   G 6 .   ? 11.471 -0.922  1.648   0.44 15.91 ?  573 HOH   A O    1 
HETATM 6900 O  O    A HOH   G 6 .   ? 21.235 -2.387  -2.077  0.56 11.64 ?  574 HOH   A O    1 
HETATM 6901 O  O    . HOH   G 6 .   ? 31.113 -13.935 -2.423  1.00 14.63 ?  575 HOH   A O    1 
HETATM 6902 O  O    . HOH   G 6 .   ? 20.120 4.606   -7.627  1.00 21.36 ?  576 HOH   A O    1 
HETATM 6903 O  O    . HOH   G 6 .   ? 16.533 -22.072 0.913   1.00 27.27 ?  577 HOH   A O    1 
HETATM 6904 O  O    . HOH   G 6 .   ? 31.895 -9.361  -6.646  1.00 25.68 ?  578 HOH   A O    1 
HETATM 6905 O  O    . HOH   G 6 .   ? 17.188 -17.868 -5.126  1.00 27.41 ?  579 HOH   A O    1 
HETATM 6906 O  O    . HOH   G 6 .   ? 18.474 9.488   8.870   1.00 25.64 ?  580 HOH   A O    1 
HETATM 6907 O  O    . HOH   G 6 .   ? 22.023 -19.298 11.416  1.00 37.96 ?  581 HOH   A O    1 
HETATM 6908 O  O    . HOH   G 6 .   ? 30.744 3.106   8.280   1.00 12.34 ?  582 HOH   A O    1 
HETATM 6909 O  O    . HOH   G 6 .   ? 43.986 8.512   -2.945  1.00 29.64 ?  583 HOH   A O    1 
HETATM 6910 O  O    . HOH   G 6 .   ? 24.614 -17.466 12.779  1.00 26.05 ?  584 HOH   A O    1 
HETATM 6911 O  O    . HOH   G 6 .   ? 27.367 -10.545 14.123  1.00 18.48 ?  585 HOH   A O    1 
HETATM 6912 O  O    . HOH   G 6 .   ? 21.859 -21.890 8.487   1.00 28.98 ?  586 HOH   A O    1 
HETATM 6913 O  O    . HOH   G 6 .   ? 37.237 12.016  4.959   1.00 28.94 ?  587 HOH   A O    1 
HETATM 6914 O  O    . HOH   G 6 .   ? 33.631 -7.148  4.372   1.00 16.45 ?  588 HOH   A O    1 
HETATM 6915 O  O    . HOH   G 6 .   ? 14.436 -24.599 11.547  1.00 38.80 ?  589 HOH   A O    1 
HETATM 6916 O  O    B HOH   G 6 .   ? 21.230 2.845   -0.048  0.44 15.65 ?  590 HOH   A O    1 
HETATM 6917 O  O    . HOH   G 6 .   ? 16.217 16.548  8.497   1.00 45.79 ?  591 HOH   A O    1 
HETATM 6918 O  O    . HOH   G 6 .   ? 21.096 10.268  14.959  1.00 35.83 ?  592 HOH   A O    1 
HETATM 6919 O  O    B HOH   G 6 .   ? 3.757  2.314   2.533   0.44 16.67 ?  593 HOH   A O    1 
HETATM 6920 O  O    . HOH   G 6 .   ? 37.514 -2.110  5.933   1.00 27.57 ?  594 HOH   A O    1 
HETATM 6921 O  O    . HOH   G 6 .   ? 31.927 -7.276  -9.794  1.00 22.51 ?  595 HOH   A O    1 
HETATM 6922 O  O    . HOH   G 6 .   ? 24.351 3.560   -1.844  1.00 15.79 ?  596 HOH   A O    1 
HETATM 6923 O  O    B HOH   G 6 .   ? 4.576  3.470   0.500   0.44 21.43 ?  597 HOH   A O    1 
HETATM 6924 O  O    . HOH   G 6 .   ? 30.535 1.939   16.700  1.00 20.92 ?  598 HOH   A O    1 
HETATM 6925 O  O    . HOH   G 6 .   ? 32.712 -9.266  5.984   1.00 20.58 ?  599 HOH   A O    1 
HETATM 6926 O  O    A HOH   G 6 .   ? 8.960  -12.100 17.146  0.56 33.73 ?  600 HOH   A O    1 
HETATM 6927 O  O    A HOH   G 6 .   ? 5.276  2.649   5.211   0.56 30.00 ?  601 HOH   A O    1 
HETATM 6928 O  O    . HOH   G 6 .   ? 24.540 1.988   -6.990  1.00 21.59 ?  602 HOH   A O    1 
HETATM 6929 O  O    . HOH   G 6 .   ? 20.514 -20.008 2.789   1.00 19.92 ?  603 HOH   A O    1 
HETATM 6930 O  O    . HOH   G 6 .   ? 23.435 11.390  4.045   1.00 12.61 ?  604 HOH   A O    1 
HETATM 6931 O  O    . HOH   G 6 .   ? 15.148 -21.461 14.198  1.00 18.46 ?  605 HOH   A O    1 
HETATM 6932 O  O    . HOH   G 6 .   ? 8.028  -21.576 4.015   1.00 48.64 ?  606 HOH   A O    1 
HETATM 6933 O  O    A HOH   G 6 .   ? 11.047 -0.370  1.887   0.56 20.69 ?  607 HOH   A O    1 
HETATM 6934 O  O    A HOH   G 6 .   ? 18.946 -0.660  -1.657  0.56 12.73 ?  608 HOH   A O    1 
HETATM 6935 O  O    A HOH   G 6 .   ? 6.430  -5.588  11.126  0.56 17.23 ?  609 HOH   A O    1 
HETATM 6936 O  O    . HOH   G 6 .   ? 27.200 2.378   18.734  1.00 35.54 ?  610 HOH   A O    1 
HETATM 6937 O  O    . HOH   G 6 .   ? 23.942 -20.262 -1.324  1.00 17.94 ?  611 HOH   A O    1 
HETATM 6938 O  O    . HOH   G 6 .   ? 13.736 -4.772  17.281  1.00 29.79 ?  612 HOH   A O    1 
HETATM 6939 O  O    . HOH   G 6 .   ? 10.313 -22.162 -1.289  1.00 51.54 ?  613 HOH   A O    1 
HETATM 6940 O  O    A HOH   G 6 .   ? 21.332 3.166   -0.378  0.56 10.92 ?  614 HOH   A O    1 
HETATM 6941 O  O    . HOH   G 6 .   ? 30.850 6.185   -12.202 1.00 28.03 ?  615 HOH   A O    1 
HETATM 6942 O  O    . HOH   G 6 .   ? 40.926 -8.253  -6.766  1.00 35.71 ?  616 HOH   A O    1 
HETATM 6943 O  O    . HOH   G 6 .   ? 26.903 4.170   -0.686  1.00 12.97 ?  617 HOH   A O    1 
HETATM 6944 O  O    . HOH   G 6 .   ? 30.215 -12.850 13.597  1.00 20.18 ?  618 HOH   A O    1 
HETATM 6945 O  O    . HOH   G 6 .   ? 38.080 -1.335  -1.864  1.00 20.27 ?  619 HOH   A O    1 
HETATM 6946 O  O    A HOH   G 6 .   ? 15.774 -0.931  5.233   0.78 36.31 ?  620 HOH   A O    1 
HETATM 6947 O  O    A HOH   G 6 .   ? 28.565 -10.645 -13.924 0.56 33.25 ?  621 HOH   A O    1 
HETATM 6948 O  O    . HOH   G 6 .   ? 35.123 -5.241  -3.047  1.00 17.90 ?  622 HOH   A O    1 
HETATM 6949 O  O    . HOH   G 6 .   ? 27.947 0.797   -7.152  1.00 14.64 ?  623 HOH   A O    1 
HETATM 6950 O  O    . HOH   G 6 .   ? 10.387 -13.769 -1.878  1.00 18.11 ?  624 HOH   A O    1 
HETATM 6951 O  O    . HOH   G 6 .   ? 21.856 -13.838 -8.202  1.00 44.60 ?  625 HOH   A O    1 
HETATM 6952 O  O    . HOH   G 6 .   ? 29.972 -10.039 13.093  1.00 24.97 ?  626 HOH   A O    1 
HETATM 6953 O  O    . HOH   G 6 .   ? 32.722 -4.348  -9.883  1.00 29.15 ?  627 HOH   A O    1 
HETATM 6954 O  O    . HOH   G 6 .   ? 16.216 -14.123 20.125  1.00 59.57 ?  628 HOH   A O    1 
HETATM 6955 O  O    . HOH   G 6 .   ? 18.369 -15.873 16.144  1.00 41.76 ?  629 HOH   A O    1 
HETATM 6956 O  O    . HOH   G 6 .   ? 18.592 4.893   -15.040 1.00 61.98 ?  630 HOH   A O    1 
HETATM 6957 O  O    . HOH   G 6 .   ? 41.597 1.515   5.052   1.00 37.98 ?  631 HOH   A O    1 
HETATM 6958 O  O    . HOH   G 6 .   ? 24.041 3.921   -4.840  1.00 20.79 ?  632 HOH   A O    1 
HETATM 6959 O  O    B HOH   G 6 .   ? 11.831 -2.058  -3.415  0.44 16.33 ?  633 HOH   A O    1 
HETATM 6960 O  O    . HOH   G 6 .   ? 26.920 -3.156  19.558  1.00 39.02 ?  634 HOH   A O    1 
HETATM 6961 O  O    . HOH   G 6 .   ? 36.694 -4.951  5.431   1.00 24.14 ?  635 HOH   A O    1 
HETATM 6962 O  O    B HOH   G 6 .   ? 10.588 -0.250  -1.524  0.44 24.04 ?  636 HOH   A O    1 
HETATM 6963 O  O    A HOH   G 6 .   ? 18.589 -2.466  -16.369 0.56 32.44 ?  637 HOH   A O    1 
HETATM 6964 O  O    . HOH   G 6 .   ? 44.999 -0.530  3.051   1.00 42.36 ?  638 HOH   A O    1 
HETATM 6965 O  O    . HOH   G 6 .   ? 32.473 -10.624 3.313   1.00 32.73 ?  639 HOH   A O    1 
HETATM 6966 O  O    . HOH   G 6 .   ? 21.375 -14.716 17.843  1.00 57.32 ?  640 HOH   A O    1 
HETATM 6967 O  O    . HOH   G 6 .   ? 22.518 8.194   18.363  1.00 45.70 ?  641 HOH   A O    1 
HETATM 6968 O  O    A HOH   G 6 .   ? 18.848 2.043   -0.785  0.56 13.40 ?  642 HOH   A O    1 
HETATM 6969 O  O    . HOH   G 6 .   ? 37.742 -8.785  -3.383  1.00 22.69 ?  643 HOH   A O    1 
HETATM 6970 O  O    . HOH   G 6 .   ? 23.431 -20.876 1.324   1.00 20.15 ?  644 HOH   A O    1 
HETATM 6971 O  O    . HOH   G 6 .   ? 23.467 -7.987  17.078  1.00 23.59 ?  645 HOH   A O    1 
HETATM 6972 O  O    . HOH   G 6 .   ? 34.411 -8.053  -0.501  1.00 29.56 ?  646 HOH   A O    1 
HETATM 6973 O  O    A HOH   G 6 .   ? 11.676 -10.745 16.929  0.56 20.56 ?  647 HOH   A O    1 
HETATM 6974 O  O    . HOH   G 6 .   ? -1.424 -4.916  7.519   1.00 51.60 ?  648 HOH   A O    1 
HETATM 6975 O  O    A HOH   G 6 .   ? 15.994 6.967   2.947   0.78 15.83 ?  649 HOH   A O    1 
HETATM 6976 O  O    . HOH   G 6 .   ? 23.190 7.566   -3.301  1.00 32.90 ?  650 HOH   A O    1 
HETATM 6977 O  O    . HOH   G 6 .   ? 9.466  -16.241 -2.114  1.00 35.61 ?  651 HOH   A O    1 
HETATM 6978 O  O    A HOH   G 6 .   ? 16.245 2.956   -1.480  0.78 19.53 ?  652 HOH   A O    1 
HETATM 6979 O  O    . HOH   G 6 .   ? 20.511 -17.687 24.838  1.00 57.94 ?  653 HOH   A O    1 
HETATM 6980 O  O    . HOH   G 6 .   ? 31.329 -12.781 0.074   1.00 20.66 ?  654 HOH   A O    1 
HETATM 6981 O  O    A HOH   G 6 .   ? 14.005 -0.326  3.420   0.78 33.86 ?  655 HOH   A O    1 
HETATM 6982 O  O    . HOH   G 6 .   ? 30.538 14.727  2.709   1.00 18.73 ?  656 HOH   A O    1 
HETATM 6983 O  O    . HOH   G 6 .   ? 21.371 -9.097  21.343  1.00 56.58 ?  657 HOH   A O    1 
HETATM 6984 O  O    . HOH   G 6 .   ? 32.384 -15.878 10.962  1.00 29.77 ?  658 HOH   A O    1 
HETATM 6985 O  O    . HOH   G 6 .   ? 29.863 -1.954  -12.774 1.00 48.61 ?  659 HOH   A O    1 
HETATM 6986 O  O    . HOH   G 6 .   ? 25.380 8.196   -4.849  1.00 30.76 ?  660 HOH   A O    1 
HETATM 6987 O  O    . HOH   G 6 .   ? 29.787 -16.129 10.902  1.00 35.77 ?  661 HOH   A O    1 
HETATM 6988 O  O    . HOH   G 6 .   ? 24.745 5.572   20.687  1.00 54.50 ?  662 HOH   A O    1 
HETATM 6989 O  O    . HOH   G 6 .   ? 19.909 -17.406 -5.076  1.00 25.37 ?  663 HOH   A O    1 
HETATM 6990 O  O    B HOH   G 6 .   ? 13.686 14.391  7.466   0.44 29.69 ?  664 HOH   A O    1 
HETATM 6991 O  O    . HOH   G 6 .   ? 27.791 7.087   -6.634  1.00 40.82 ?  665 HOH   A O    1 
HETATM 6992 O  O    . HOH   G 6 .   ? 21.894 5.125   -5.934  1.00 34.28 ?  666 HOH   A O    1 
HETATM 6993 O  O    B HOH   G 6 .   ? 13.798 -2.961  -1.083  0.44 21.01 ?  667 HOH   A O    1 
HETATM 6994 O  O    . HOH   G 6 .   ? 24.555 14.737  7.790   1.00 38.03 ?  668 HOH   A O    1 
HETATM 6995 O  O    . HOH   G 6 .   ? 23.223 -22.442 -3.211  1.00 37.67 ?  669 HOH   A O    1 
HETATM 6996 O  O    . HOH   G 6 .   ? 18.799 11.041  11.170  1.00 33.16 ?  670 HOH   A O    1 
HETATM 6997 O  O    . HOH   G 6 .   ? 27.439 -11.289 16.651  1.00 38.76 ?  671 HOH   A O    1 
HETATM 6998 O  O    . HOH   G 6 .   ? 15.735 -21.506 3.651   1.00 23.95 ?  672 HOH   A O    1 
HETATM 6999 O  O    . HOH   G 6 .   ? 39.667 -7.033  -3.435  1.00 45.21 ?  673 HOH   A O    1 
HETATM 7000 O  O    . HOH   G 6 .   ? 26.927 11.667  -1.376  1.00 35.33 ?  674 HOH   A O    1 
HETATM 7001 O  O    . HOH   G 6 .   ? 11.071 -15.064 -6.209  1.00 36.95 ?  675 HOH   A O    1 
HETATM 7002 O  O    . HOH   G 6 .   ? 18.158 -16.291 -9.002  1.00 42.99 ?  676 HOH   A O    1 
HETATM 7003 O  O    . HOH   G 6 .   ? 25.848 10.787  -3.740  1.00 27.08 ?  677 HOH   A O    1 
HETATM 7004 O  O    . HOH   G 6 .   ? 23.390 13.701  5.516   1.00 18.77 ?  678 HOH   A O    1 
HETATM 7005 O  O    . HOH   G 6 .   ? 12.155 1.677   17.236  1.00 39.31 ?  679 HOH   A O    1 
HETATM 7006 O  O    . HOH   G 6 .   ? 8.109  -3.277  -5.894  1.00 59.41 ?  680 HOH   A O    1 
HETATM 7007 O  O    A HOH   G 6 .   ? 11.910 -13.348 16.268  0.56 36.13 ?  681 HOH   A O    1 
HETATM 7008 O  O    B HOH   G 6 .   ? 8.537  1.614   -3.603  0.44 27.83 ?  682 HOH   A O    1 
HETATM 7009 O  O    . HOH   G 6 .   ? 28.749 8.995   17.538  1.00 35.39 ?  683 HOH   A O    1 
HETATM 7010 O  O    . HOH   G 6 .   ? 35.082 7.506   12.224  1.00 48.19 ?  684 HOH   A O    1 
HETATM 7011 O  O    . HOH   G 6 .   ? 23.140 11.816  -4.110  1.00 20.76 ?  685 HOH   A O    1 
HETATM 7012 O  O    . HOH   G 6 .   ? 15.712 -17.349 -7.049  1.00 31.63 ?  686 HOH   A O    1 
HETATM 7013 O  O    . HOH   G 6 .   ? 16.851 -20.449 16.095  1.00 29.29 ?  687 HOH   A O    1 
HETATM 7014 O  O    . HOH   G 6 .   ? 17.394 -18.719 19.733  1.00 59.12 ?  688 HOH   A O    1 
HETATM 7015 O  O    . HOH   G 6 .   ? 41.002 -3.959  -0.397  1.00 42.30 ?  689 HOH   A O    1 
HETATM 7016 O  O    . HOH   G 6 .   ? 16.141 -6.739  -12.118 1.00 45.30 ?  690 HOH   A O    1 
HETATM 7017 O  O    . HOH   G 6 .   ? 44.462 10.420  -1.573  1.00 33.80 ?  691 HOH   A O    1 
HETATM 7018 O  O    . HOH   G 6 .   ? 28.577 -4.704  -12.316 1.00 44.04 ?  692 HOH   A O    1 
HETATM 7019 O  O    . HOH   G 6 .   ? 13.902 -25.141 8.893   1.00 32.89 ?  693 HOH   A O    1 
HETATM 7020 O  O    . HOH   G 6 .   ? 14.060 -10.345 -11.028 1.00 35.03 ?  694 HOH   A O    1 
HETATM 7021 O  O    . HOH   G 6 .   ? 25.802 -18.807 -11.819 1.00 43.03 ?  695 HOH   A O    1 
HETATM 7022 O  O    . HOH   G 6 .   ? 39.159 2.403   7.377   1.00 32.74 ?  696 HOH   A O    1 
HETATM 7023 O  O    . HOH   G 6 .   ? 41.697 9.397   -3.909  1.00 31.25 ?  697 HOH   A O    1 
HETATM 7024 O  O    . HOH   G 6 .   ? 31.521 -0.583  -10.540 1.00 31.53 ?  698 HOH   A O    1 
HETATM 7025 O  O    . HOH   G 6 .   ? 23.177 -12.893 19.242  1.00 54.23 ?  699 HOH   A O    1 
HETATM 7026 O  O    . HOH   G 6 .   ? 16.154 -23.362 5.712   1.00 31.02 ?  700 HOH   A O    1 
HETATM 7027 O  O    . HOH   G 6 .   ? 20.096 -22.315 4.255   1.00 31.88 ?  701 HOH   A O    1 
HETATM 7028 O  O    B HOH   G 6 .   ? 12.809 -3.294  1.418   0.44 16.18 ?  702 HOH   A O    1 
HETATM 7029 O  O    . HOH   G 6 .   ? 28.839 -7.981  -15.170 1.00 55.94 ?  703 HOH   A O    1 
HETATM 7030 O  O    . HOH   G 6 .   ? 30.907 0.763   19.203  1.00 41.91 ?  704 HOH   A O    1 
HETATM 7031 O  O    . HOH   G 6 .   ? 18.418 -23.180 1.849   1.00 52.08 ?  705 HOH   A O    1 
HETATM 7032 O  O    B HOH   G 6 .   ? 5.399  6.010   1.224   0.44 18.75 ?  706 HOH   A O    1 
HETATM 7033 O  O    . HOH   G 6 .   ? 40.627 -0.275  -7.694  1.00 33.43 ?  707 HOH   A O    1 
HETATM 7034 O  O    . HOH   G 6 .   ? 37.377 -6.611  7.650   1.00 25.65 ?  708 HOH   A O    1 
HETATM 7035 O  O    . HOH   G 6 .   ? 30.767 -5.854  -11.896 1.00 49.37 ?  709 HOH   A O    1 
HETATM 7036 O  O    . HOH   G 6 .   ? 30.728 5.760   -14.714 1.00 34.03 ?  710 HOH   A O    1 
HETATM 7037 O  O    . HOH   G 6 .   ? 39.502 -0.071  6.702   1.00 32.10 ?  711 HOH   A O    1 
HETATM 7038 O  O    . HOH   G 6 .   ? 20.609 -16.115 -7.434  1.00 28.93 ?  712 HOH   A O    1 
HETATM 7039 O  O    . HOH   G 6 .   ? 28.938 14.406  0.858   1.00 53.21 ?  713 HOH   A O    1 
HETATM 7040 O  O    . HOH   G 6 .   ? 37.941 13.993  6.680   1.00 38.43 ?  714 HOH   A O    1 
HETATM 7041 O  O    B HOH   G 6 .   ? 7.977  6.659   2.045   0.44 19.80 ?  715 HOH   A O    1 
HETATM 7042 O  O    . HOH   G 6 .   ? 22.047 -23.992 4.527   1.00 27.85 ?  716 HOH   A O    1 
HETATM 7043 O  O    . HOH   G 6 .   ? 36.403 -6.468  10.306  1.00 50.02 ?  717 HOH   A O    1 
HETATM 7044 O  O    . HOH   G 6 .   ? 17.220 -6.849  -14.182 1.00 50.47 ?  718 HOH   A O    1 
HETATM 7045 O  O    A HOH   G 6 .   ? 14.823 8.664   4.842   0.78 34.76 ?  719 HOH   A O    1 
HETATM 7046 O  O    . HOH   G 6 .   ? 24.103 9.031   -7.205  1.00 39.79 ?  720 HOH   A O    1 
HETATM 7047 O  O    . HOH   G 6 .   ? 15.779 -12.427 27.397  1.00 45.33 ?  721 HOH   A O    1 
HETATM 7048 O  O    . HOH   G 6 .   ? 16.300 -21.184 18.763  1.00 40.59 ?  722 HOH   A O    1 
HETATM 7049 O  O    B HOH   G 6 .   ? 10.448 10.875  7.324   0.44 29.27 ?  723 HOH   A O    1 
HETATM 7050 O  O    . HOH   G 6 .   ? 14.711 -22.727 19.832  1.00 35.94 ?  724 HOH   A O    1 
HETATM 7051 O  O    . HOH   H 6 .   ? 29.872 -22.402 5.553   1.00 20.40 ?  201 HOH   B O    1 
HETATM 7052 O  O    . HOH   H 6 .   ? 27.675 -29.134 -1.807  1.00 35.44 ?  202 HOH   B O    1 
HETATM 7053 O  O    . HOH   H 6 .   ? 38.067 -39.389 -0.148  1.00 39.88 ?  203 HOH   B O    1 
HETATM 7054 O  O    . HOH   H 6 .   ? 41.616 -36.069 -17.127 1.00 34.49 ?  204 HOH   B O    1 
HETATM 7055 O  O    . HOH   H 6 .   ? 31.056 -28.717 4.556   1.00 30.58 ?  205 HOH   B O    1 
HETATM 7056 O  O    . HOH   H 6 .   ? 27.930 -41.736 -15.114 1.00 39.25 ?  206 HOH   B O    1 
HETATM 7057 O  O    . HOH   H 6 .   ? 59.125 -18.651 6.905   1.00 36.26 ?  207 HOH   B O    1 
HETATM 7058 O  O    . HOH   H 6 .   ? 30.032 -26.275 4.193   1.00 27.80 ?  208 HOH   B O    1 
HETATM 7059 O  O    . HOH   H 6 .   ? 30.194 -40.959 -8.015  1.00 18.60 ?  209 HOH   B O    1 
HETATM 7060 O  O    . HOH   H 6 .   ? 54.507 -9.452  -8.598  1.00 19.61 ?  210 HOH   B O    1 
HETATM 7061 O  O    . HOH   H 6 .   ? 50.200 -3.348  7.167   1.00 32.99 ?  211 HOH   B O    1 
HETATM 7062 O  O    . HOH   H 6 .   ? 52.980 -13.474 -20.212 1.00 31.86 ?  212 HOH   B O    1 
HETATM 7063 O  O    . HOH   H 6 .   ? 48.055 -6.917  15.549  1.00 26.64 ?  213 HOH   B O    1 
HETATM 7064 O  O    . HOH   H 6 .   ? 56.361 -19.721 7.193   1.00 31.82 ?  214 HOH   B O    1 
HETATM 7065 O  O    . HOH   H 6 .   ? 41.348 -7.756  5.455   1.00 41.61 ?  215 HOH   B O    1 
HETATM 7066 O  O    . HOH   H 6 .   ? 58.205 -12.974 8.384   1.00 29.71 ?  216 HOH   B O    1 
HETATM 7067 O  O    . HOH   H 6 .   ? 49.417 -22.780 -19.762 1.00 47.12 ?  217 HOH   B O    1 
HETATM 7068 O  O    . HOH   H 6 .   ? 57.734 -24.404 5.092   1.00 40.99 ?  218 HOH   B O    1 
HETATM 7069 O  O    . HOH   H 6 .   ? 56.695 -30.777 -7.737  1.00 26.72 ?  219 HOH   B O    1 
HETATM 7070 O  O    . HOH   H 6 .   ? 26.506 -19.323 -1.740  1.00 14.97 ?  220 HOH   B O    1 
HETATM 7071 O  O    . HOH   H 6 .   ? 57.156 -26.886 -7.581  1.00 38.23 ?  221 HOH   B O    1 
HETATM 7072 O  O    . HOH   H 6 .   ? 41.515 -39.183 -14.847 1.00 22.70 ?  222 HOH   B O    1 
HETATM 7073 O  O    . HOH   H 6 .   ? 55.383 -16.544 -14.295 1.00 34.54 ?  223 HOH   B O    1 
HETATM 7074 O  O    . HOH   H 6 .   ? 34.529 -36.375 -7.083  1.00 20.80 ?  224 HOH   B O    1 
HETATM 7075 O  O    . HOH   H 6 .   ? 37.115 -19.713 -18.127 1.00 43.27 ?  225 HOH   B O    1 
HETATM 7076 O  O    . HOH   H 6 .   ? 57.401 -16.309 -12.216 1.00 18.32 ?  226 HOH   B O    1 
HETATM 7077 O  O    . HOH   H 6 .   ? 44.441 -7.040  1.982   1.00 35.91 ?  227 HOH   B O    1 
HETATM 7078 O  O    . HOH   H 6 .   ? 32.704 -43.725 -11.267 1.00 24.23 ?  228 HOH   B O    1 
HETATM 7079 O  O    . HOH   H 6 .   ? 38.512 -11.054 -2.241  1.00 20.22 ?  229 HOH   B O    1 
HETATM 7080 O  O    . HOH   H 6 .   ? 47.380 -7.252  -3.729  1.00 41.98 ?  230 HOH   B O    1 
HETATM 7081 O  O    . HOH   H 6 .   ? 40.575 -16.087 14.092  1.00 25.44 ?  231 HOH   B O    1 
HETATM 7082 O  O    . HOH   H 6 .   ? 45.182 -34.906 6.853   1.00 44.85 ?  232 HOH   B O    1 
HETATM 7083 O  O    . HOH   H 6 .   ? 35.108 -8.023  -2.938  1.00 18.48 ?  233 HOH   B O    1 
HETATM 7084 O  O    . HOH   H 6 .   ? 50.765 -6.075  0.192   1.00 27.80 ?  234 HOH   B O    1 
HETATM 7085 O  O    . HOH   H 6 .   ? 25.328 -25.825 -1.203  1.00 34.66 ?  235 HOH   B O    1 
HETATM 7086 O  O    . HOH   H 6 .   ? 27.108 -31.802 -9.845  1.00 20.99 ?  236 HOH   B O    1 
HETATM 7087 O  O    . HOH   H 6 .   ? 50.947 -39.872 -8.113  1.00 36.41 ?  237 HOH   B O    1 
HETATM 7088 O  O    . HOH   H 6 .   ? 42.994 -43.225 -8.138  1.00 29.87 ?  238 HOH   B O    1 
HETATM 7089 O  O    . HOH   H 6 .   ? 50.775 -12.973 -0.438  1.00 11.91 ?  239 HOH   B O    1 
HETATM 7090 O  O    . HOH   H 6 .   ? 48.507 -36.507 -15.535 1.00 47.31 ?  240 HOH   B O    1 
HETATM 7091 O  O    . HOH   H 6 .   ? 51.672 -6.464  4.361   1.00 19.18 ?  241 HOH   B O    1 
HETATM 7092 O  O    . HOH   H 6 .   ? 44.891 -43.562 -10.409 1.00 27.92 ?  242 HOH   B O    1 
HETATM 7093 O  O    . HOH   H 6 .   ? 57.670 -24.341 -3.730  1.00 20.76 ?  243 HOH   B O    1 
HETATM 7094 O  O    . HOH   H 6 .   ? 46.404 -1.540  13.210  1.00 27.25 ?  244 HOH   B O    1 
HETATM 7095 O  O    . HOH   H 6 .   ? 28.264 -34.315 -9.298  1.00 17.77 ?  245 HOH   B O    1 
HETATM 7096 O  O    . HOH   H 6 .   ? 41.410 -9.595  13.119  1.00 23.29 ?  246 HOH   B O    1 
HETATM 7097 O  O    . HOH   H 6 .   ? 39.325 -10.854 6.148   1.00 24.54 ?  247 HOH   B O    1 
HETATM 7098 O  O    . HOH   H 6 .   ? 28.427 -19.681 -13.065 1.00 25.47 ?  248 HOH   B O    1 
HETATM 7099 O  O    . HOH   H 6 .   ? 34.914 -24.618 13.864  1.00 37.21 ?  249 HOH   B O    1 
HETATM 7100 O  O    . HOH   H 6 .   ? 30.461 -42.196 -10.631 1.00 30.93 ?  250 HOH   B O    1 
HETATM 7101 O  O    . HOH   H 6 .   ? 44.544 -27.723 -0.599  1.00 22.46 ?  251 HOH   B O    1 
HETATM 7102 O  O    . HOH   H 6 .   ? 42.647 -22.838 3.926   1.00 12.12 ?  252 HOH   B O    1 
HETATM 7103 O  O    . HOH   H 6 .   ? 29.840 -34.161 -0.358  1.00 35.82 ?  253 HOH   B O    1 
HETATM 7104 O  O    . HOH   H 6 .   ? 42.585 -25.333 2.721   1.00 15.77 ?  254 HOH   B O    1 
HETATM 7105 O  O    . HOH   H 6 .   ? 39.564 -11.098 0.332   1.00 16.74 ?  255 HOH   B O    1 
HETATM 7106 O  O    . HOH   H 6 .   ? 34.342 -18.279 11.523  1.00 26.86 ?  256 HOH   B O    1 
HETATM 7107 O  O    . HOH   H 6 .   ? 41.914 -23.517 9.368   1.00 20.15 ?  257 HOH   B O    1 
HETATM 7108 O  O    . HOH   H 6 .   ? 40.375 -12.750 -11.457 1.00 15.76 ?  258 HOH   B O    1 
HETATM 7109 O  O    . HOH   H 6 .   ? 29.733 -25.181 -10.672 1.00 17.54 ?  259 HOH   B O    1 
HETATM 7110 O  O    . HOH   H 6 .   ? 58.236 -10.671 -4.021  1.00 20.43 ?  260 HOH   B O    1 
HETATM 7111 O  O    . HOH   H 6 .   ? 42.884 -20.241 -20.623 1.00 40.39 ?  261 HOH   B O    1 
HETATM 7112 O  O    . HOH   H 6 .   ? 30.866 -15.706 2.718   1.00 14.55 ?  262 HOH   B O    1 
HETATM 7113 O  O    . HOH   H 6 .   ? 42.389 -9.910  9.363   1.00 21.18 ?  263 HOH   B O    1 
HETATM 7114 O  O    . HOH   H 6 .   ? 51.551 -13.793 11.049  1.00 26.07 ?  264 HOH   B O    1 
HETATM 7115 O  O    . HOH   H 6 .   ? 33.506 -16.948 8.114   1.00 19.61 ?  265 HOH   B O    1 
HETATM 7116 O  O    . HOH   H 6 .   ? 43.149 -32.372 -17.102 1.00 25.92 ?  266 HOH   B O    1 
HETATM 7117 O  O    . HOH   H 6 .   ? 28.431 -30.889 -14.733 1.00 32.64 ?  267 HOH   B O    1 
HETATM 7118 O  O    . HOH   H 6 .   ? 48.075 -22.778 5.876   1.00 18.72 ?  268 HOH   B O    1 
HETATM 7119 O  O    . HOH   H 6 .   ? 34.966 -33.267 -19.156 1.00 32.68 ?  269 HOH   B O    1 
HETATM 7120 O  O    . HOH   H 6 .   ? 31.796 -17.869 -14.470 1.00 30.42 ?  270 HOH   B O    1 
HETATM 7121 O  O    . HOH   H 6 .   ? 46.883 -29.542 9.866   1.00 30.61 ?  271 HOH   B O    1 
HETATM 7122 O  O    . HOH   H 6 .   ? 38.936 -11.868 12.430  1.00 37.45 ?  272 HOH   B O    1 
HETATM 7123 O  O    . HOH   H 6 .   ? 43.412 -15.807 -12.142 1.00 14.79 ?  273 HOH   B O    1 
HETATM 7124 O  O    . HOH   H 6 .   ? 42.425 -34.680 3.852   1.00 27.36 ?  274 HOH   B O    1 
HETATM 7125 O  O    . HOH   H 6 .   ? 49.315 -28.731 -6.866  1.00 16.03 ?  275 HOH   B O    1 
HETATM 7126 O  O    . HOH   H 6 .   ? 47.915 -24.509 -17.755 1.00 34.52 ?  276 HOH   B O    1 
HETATM 7127 O  O    . HOH   H 6 .   ? 57.192 -12.077 12.309  1.00 38.48 ?  277 HOH   B O    1 
HETATM 7128 O  O    . HOH   H 6 .   ? 51.684 -5.989  -7.963  1.00 42.31 ?  278 HOH   B O    1 
HETATM 7129 O  O    . HOH   H 6 .   ? 56.192 -23.578 -14.671 1.00 27.53 ?  279 HOH   B O    1 
HETATM 7130 O  O    . HOH   H 6 .   ? 49.695 -0.441  10.210  1.00 28.93 ?  280 HOH   B O    1 
HETATM 7131 O  O    . HOH   H 6 .   ? 41.176 -5.508  11.560  1.00 48.50 ?  281 HOH   B O    1 
HETATM 7132 O  O    . HOH   H 6 .   ? 36.044 -43.480 -8.301  1.00 42.10 ?  282 HOH   B O    1 
HETATM 7133 O  O    . HOH   H 6 .   ? 56.962 -8.618  8.459   1.00 18.71 ?  283 HOH   B O    1 
HETATM 7134 O  O    . HOH   H 6 .   ? 57.516 -9.217  1.400   1.00 20.02 ?  284 HOH   B O    1 
HETATM 7135 O  O    . HOH   H 6 .   ? 46.601 -31.213 -4.772  1.00 22.18 ?  285 HOH   B O    1 
HETATM 7136 O  O    . HOH   H 6 .   ? 48.402 -25.034 3.169   1.00 14.09 ?  286 HOH   B O    1 
HETATM 7137 O  O    . HOH   H 6 .   ? 48.623 -12.143 -14.309 1.00 27.17 ?  287 HOH   B O    1 
HETATM 7138 O  O    . HOH   H 6 .   ? 34.488 -12.747 2.693   1.00 23.11 ?  288 HOH   B O    1 
HETATM 7139 O  O    . HOH   H 6 .   ? 27.959 -22.869 -7.928  1.00 18.44 ?  289 HOH   B O    1 
HETATM 7140 O  O    . HOH   H 6 .   ? 38.375 -12.214 -16.190 1.00 51.42 ?  290 HOH   B O    1 
HETATM 7141 O  O    . HOH   H 6 .   ? 27.562 -26.629 -15.552 1.00 34.52 ?  291 HOH   B O    1 
HETATM 7142 O  O    . HOH   H 6 .   ? 49.913 -24.677 5.848   1.00 35.99 ?  292 HOH   B O    1 
HETATM 7143 O  O    . HOH   H 6 .   ? 52.522 -10.399 12.991  1.00 23.67 ?  293 HOH   B O    1 
HETATM 7144 O  O    . HOH   H 6 .   ? 33.559 -15.292 -13.895 1.00 22.72 ?  294 HOH   B O    1 
HETATM 7145 O  O    . HOH   H 6 .   ? 48.724 -20.002 5.998   1.00 14.59 ?  295 HOH   B O    1 
HETATM 7146 O  O    . HOH   H 6 .   ? 47.072 -33.974 -4.579  1.00 19.72 ?  296 HOH   B O    1 
HETATM 7147 O  O    . HOH   H 6 .   ? 42.697 -12.268 -18.423 1.00 28.27 ?  297 HOH   B O    1 
HETATM 7148 O  O    . HOH   H 6 .   ? 51.200 -37.570 -9.646  1.00 27.37 ?  298 HOH   B O    1 
HETATM 7149 O  O    . HOH   H 6 .   ? 36.814 -12.732 -1.437  1.00 28.12 ?  299 HOH   B O    1 
HETATM 7150 O  O    . HOH   H 6 .   ? 45.282 -33.352 -15.981 1.00 26.18 ?  300 HOH   B O    1 
HETATM 7151 O  O    . HOH   H 6 .   ? 59.805 -15.245 8.222   1.00 31.31 ?  301 HOH   B O    1 
HETATM 7152 O  O    . HOH   H 6 .   ? 44.629 -27.453 2.107   1.00 16.55 ?  302 HOH   B O    1 
HETATM 7153 O  O    . HOH   H 6 .   ? 38.389 -9.369  -13.256 1.00 32.94 ?  303 HOH   B O    1 
HETATM 7154 O  O    . HOH   H 6 .   ? 35.088 -33.643 4.663   1.00 33.39 ?  304 HOH   B O    1 
HETATM 7155 O  O    . HOH   H 6 .   ? 25.958 -21.464 -3.441  1.00 16.95 ?  305 HOH   B O    1 
HETATM 7156 O  O    . HOH   H 6 .   ? 52.475 -29.232 -13.046 1.00 25.83 ?  306 HOH   B O    1 
HETATM 7157 O  O    . HOH   H 6 .   ? 44.012 -29.354 -4.658  1.00 24.17 ?  307 HOH   B O    1 
HETATM 7158 O  O    . HOH   H 6 .   ? 52.584 -35.620 -8.768  1.00 30.98 ?  308 HOH   B O    1 
HETATM 7159 O  O    . HOH   H 6 .   ? 53.463 -30.188 4.581   1.00 18.70 ?  309 HOH   B O    1 
HETATM 7160 O  O    . HOH   H 6 .   ? 62.741 -13.568 4.748   1.00 27.14 ?  310 HOH   B O    1 
HETATM 7161 O  O    . HOH   H 6 .   ? 37.304 -35.625 7.288   1.00 33.73 ?  311 HOH   B O    1 
HETATM 7162 O  O    . HOH   H 6 .   ? 38.319 -12.657 8.006   1.00 17.81 ?  312 HOH   B O    1 
HETATM 7163 O  O    . HOH   H 6 .   ? 40.283 -10.845 -9.470  1.00 17.82 ?  313 HOH   B O    1 
HETATM 7164 O  O    . HOH   H 6 .   ? 43.234 -21.394 10.715  1.00 16.68 ?  314 HOH   B O    1 
HETATM 7165 O  O    . HOH   H 6 .   ? 36.943 -30.577 -20.954 1.00 32.48 ?  315 HOH   B O    1 
HETATM 7166 O  O    . HOH   H 6 .   ? 37.395 -17.890 13.194  1.00 33.19 ?  316 HOH   B O    1 
HETATM 7167 O  O    . HOH   H 6 .   ? 37.904 -10.210 -10.667 1.00 18.65 ?  317 HOH   B O    1 
HETATM 7168 O  O    . HOH   H 6 .   ? 53.031 -16.031 -12.757 1.00 26.30 ?  318 HOH   B O    1 
HETATM 7169 O  O    . HOH   H 6 .   ? 48.123 -32.677 -16.612 1.00 44.32 ?  319 HOH   B O    1 
HETATM 7170 O  O    . HOH   H 6 .   ? 43.183 -34.462 0.104   1.00 23.13 ?  320 HOH   B O    1 
HETATM 7171 O  O    . HOH   H 6 .   ? 32.849 -34.591 -5.801  1.00 18.36 ?  321 HOH   B O    1 
HETATM 7172 O  O    . HOH   H 6 .   ? 41.790 -8.046  1.413   1.00 24.21 ?  322 HOH   B O    1 
HETATM 7173 O  O    . HOH   H 6 .   ? 53.639 -12.626 -22.150 1.00 30.33 ?  323 HOH   B O    1 
HETATM 7174 O  O    . HOH   H 6 .   ? 45.818 -40.366 -3.457  1.00 32.56 ?  324 HOH   B O    1 
HETATM 7175 O  O    . HOH   H 6 .   ? 26.354 -21.040 -6.171  1.00 17.11 ?  325 HOH   B O    1 
HETATM 7176 O  O    . HOH   H 6 .   ? 43.501 -15.372 18.114  1.00 30.28 ?  326 HOH   B O    1 
HETATM 7177 O  O    . HOH   H 6 .   ? 42.480 -9.672  -14.776 1.00 41.97 ?  327 HOH   B O    1 
HETATM 7178 O  O    . HOH   H 6 .   ? 45.715 -36.334 -16.054 1.00 37.51 ?  328 HOH   B O    1 
HETATM 7179 O  O    . HOH   H 6 .   ? 44.690 -24.546 9.632   1.00 21.88 ?  329 HOH   B O    1 
HETATM 7180 O  O    . HOH   H 6 .   ? 47.262 -24.439 8.240   1.00 24.07 ?  330 HOH   B O    1 
HETATM 7181 O  O    . HOH   H 6 .   ? 62.883 -20.223 -0.670  1.00 37.45 ?  331 HOH   B O    1 
HETATM 7182 O  O    . HOH   H 6 .   ? 44.139 -1.728  7.670   1.00 48.57 ?  332 HOH   B O    1 
HETATM 7183 O  O    . HOH   H 6 .   ? 36.747 -12.373 4.337   1.00 17.50 ?  333 HOH   B O    1 
HETATM 7184 O  O    . HOH   H 6 .   ? 51.400 -33.140 -10.939 1.00 46.78 ?  334 HOH   B O    1 
HETATM 7185 O  O    . HOH   H 6 .   ? 33.612 -31.152 11.068  1.00 37.34 ?  335 HOH   B O    1 
HETATM 7186 O  O    . HOH   H 6 .   ? 57.604 -22.015 3.340   1.00 31.80 ?  336 HOH   B O    1 
HETATM 7187 O  O    . HOH   H 6 .   ? 34.436 -10.345 7.861   1.00 21.93 ?  337 HOH   B O    1 
HETATM 7188 O  O    . HOH   H 6 .   ? 27.759 -14.748 -9.479  1.00 38.34 ?  338 HOH   B O    1 
HETATM 7189 O  O    . HOH   H 6 .   ? 59.951 -17.255 -10.522 1.00 35.76 ?  339 HOH   B O    1 
HETATM 7190 O  O    . HOH   H 6 .   ? 47.475 -27.402 2.083   1.00 15.56 ?  340 HOH   B O    1 
HETATM 7191 O  O    . HOH   H 6 .   ? 37.138 -15.203 -16.582 1.00 43.08 ?  341 HOH   B O    1 
HETATM 7192 O  O    . HOH   H 6 .   ? 42.794 -43.546 -14.293 1.00 41.58 ?  342 HOH   B O    1 
HETATM 7193 O  O    . HOH   H 6 .   ? 46.841 -19.892 12.321  1.00 32.18 ?  343 HOH   B O    1 
HETATM 7194 O  O    . HOH   H 6 .   ? 41.289 -24.471 15.985  1.00 45.32 ?  344 HOH   B O    1 
HETATM 7195 O  O    . HOH   H 6 .   ? 37.032 -45.147 -9.645  1.00 36.59 ?  345 HOH   B O    1 
HETATM 7196 O  O    . HOH   H 6 .   ? 28.881 -42.858 -12.252 1.00 44.24 ?  346 HOH   B O    1 
HETATM 7197 O  O    . HOH   H 6 .   ? 33.023 -14.660 1.120   1.00 20.85 ?  347 HOH   B O    1 
HETATM 7198 O  O    . HOH   H 6 .   ? 38.589 -22.350 15.062  1.00 46.60 ?  348 HOH   B O    1 
HETATM 7199 O  O    . HOH   H 6 .   ? 39.621 -23.630 -20.341 1.00 40.49 ?  349 HOH   B O    1 
HETATM 7200 O  O    . HOH   H 6 .   ? 33.688 -9.721  -8.820  1.00 31.67 ?  350 HOH   B O    1 
HETATM 7201 O  O    . HOH   H 6 .   ? 44.165 -37.339 -17.720 1.00 35.96 ?  351 HOH   B O    1 
HETATM 7202 O  O    . HOH   H 6 .   ? 39.855 -44.174 -11.198 1.00 46.20 ?  352 HOH   B O    1 
HETATM 7203 O  O    . HOH   H 6 .   ? 40.376 -43.466 -9.115  1.00 27.24 ?  353 HOH   B O    1 
HETATM 7204 O  O    . HOH   H 6 .   ? 27.794 -26.610 -0.423  1.00 32.54 ?  354 HOH   B O    1 
HETATM 7205 O  O    . HOH   H 6 .   ? 33.926 -7.891  11.549  1.00 41.31 ?  355 HOH   B O    1 
HETATM 7206 O  O    . HOH   H 6 .   ? 23.278 -23.653 6.847   1.00 34.56 ?  356 HOH   B O    1 
HETATM 7207 O  O    . HOH   H 6 .   ? 62.587 -20.073 -4.858  1.00 47.34 ?  357 HOH   B O    1 
HETATM 7208 O  O    . HOH   H 6 .   ? 55.764 -8.266  10.815  1.00 24.22 ?  358 HOH   B O    1 
HETATM 7209 O  O    . HOH   H 6 .   ? 56.613 -7.243  3.029   1.00 25.44 ?  359 HOH   B O    1 
HETATM 7210 O  O    . HOH   H 6 .   ? 56.812 -21.598 -16.388 1.00 41.86 ?  360 HOH   B O    1 
HETATM 7211 O  O    . HOH   H 6 .   ? 36.169 -8.473  -9.754  1.00 35.28 ?  361 HOH   B O    1 
HETATM 7212 O  O    . HOH   H 6 .   ? 61.520 -19.892 1.803   1.00 37.01 ?  362 HOH   B O    1 
HETATM 7213 O  O    . HOH   H 6 .   ? 40.261 -8.846  9.907   1.00 37.51 ?  363 HOH   B O    1 
HETATM 7214 O  O    . HOH   H 6 .   ? 27.168 -25.937 -11.298 1.00 34.96 ?  364 HOH   B O    1 
HETATM 7215 O  O    . HOH   H 6 .   ? 40.457 -11.293 -13.865 1.00 32.84 ?  365 HOH   B O    1 
HETATM 7216 O  O    . HOH   H 6 .   ? 43.201 -12.711 -21.083 1.00 43.03 ?  366 HOH   B O    1 
HETATM 7217 O  O    . HOH   H 6 .   ? 48.276 -26.413 8.838   1.00 43.49 ?  367 HOH   B O    1 
HETATM 7218 O  O    . HOH   H 6 .   ? 36.158 -8.609  9.034   1.00 32.25 ?  368 HOH   B O    1 
HETATM 7219 O  O    . HOH   H 6 .   ? 32.588 -23.615 14.077  1.00 42.88 ?  369 HOH   B O    1 
HETATM 7220 O  O    . HOH   H 6 .   ? 54.293 -5.762  2.969   1.00 36.37 ?  370 HOH   B O    1 
HETATM 7221 O  O    . HOH   H 6 .   ? 39.872 -7.044  7.861   1.00 39.75 ?  371 HOH   B O    1 
HETATM 7222 O  O    . HOH   H 6 .   ? 59.029 -10.416 9.185   1.00 37.50 ?  372 HOH   B O    1 
HETATM 7223 O  O    . HOH   H 6 .   ? 40.171 -7.857  3.131   1.00 44.06 ?  373 HOH   B O    1 
HETATM 7224 O  O    . HOH   H 6 .   ? 52.074 -12.912 13.324  1.00 28.93 ?  374 HOH   B O    1 
HETATM 7225 O  O    . HOH   H 6 .   ? 41.815 -10.051 -17.462 1.00 55.79 ?  375 HOH   B O    1 
HETATM 7226 O  O    . HOH   H 6 .   ? 56.106 -7.778  -0.607  1.00 36.30 ?  376 HOH   B O    1 
HETATM 7227 O  O    . HOH   H 6 .   ? 63.083 -12.400 7.111   1.00 35.95 ?  377 HOH   B O    1 
HETATM 7228 O  O    . HOH   H 6 .   ? 36.522 -22.818 13.318  1.00 29.96 ?  378 HOH   B O    1 
HETATM 7229 O  O    . HOH   H 6 .   ? 38.028 -10.486 10.064  1.00 28.90 ?  379 HOH   B O    1 
HETATM 7230 O  O    . HOH   H 6 .   ? 42.645 -17.156 -23.075 1.00 46.96 ?  380 HOH   B O    1 
HETATM 7231 O  O    . HOH   H 6 .   ? 41.812 -6.653  -4.844  1.00 46.98 ?  381 HOH   B O    1 
HETATM 7232 O  O    . HOH   H 6 .   ? 39.611 -14.016 15.617  1.00 53.63 ?  382 HOH   B O    1 
HETATM 7233 O  O    . HOH   H 6 .   ? 44.060 -5.581  -3.451  1.00 42.66 ?  383 HOH   B O    1 
HETATM 7234 O  O    . HOH   H 6 .   ? 60.458 -22.266 2.921   1.00 48.38 ?  384 HOH   B O    1 
HETATM 7235 O  O    . HOH   H 6 .   ? 46.788 -5.427  2.944   1.00 39.28 ?  385 HOH   B O    1 
HETATM 7236 O  O    . HOH   H 6 .   ? 52.895 -29.924 7.281   1.00 23.01 ?  386 HOH   B O    1 
HETATM 7237 O  O    . HOH   H 6 .   ? 41.035 -9.719  15.824  1.00 49.72 ?  387 HOH   B O    1 
HETATM 7238 O  O    . HOH   H 6 .   ? 23.916 -20.841 -7.614  1.00 29.69 ?  388 HOH   B O    1 
HETATM 7239 O  O    . HOH   H 6 .   ? 35.288 -20.370 13.360  1.00 35.03 ?  389 HOH   B O    1 
HETATM 7240 O  O    . HOH   H 6 .   ? 35.393 -33.738 7.464   1.00 45.07 ?  390 HOH   B O    1 
HETATM 7241 O  O    . HOH   H 6 .   ? 44.182 -31.673 -3.807  1.00 44.26 ?  391 HOH   B O    1 
HETATM 7242 O  O    . HOH   H 6 .   ? 23.157 -23.742 1.585   1.00 37.72 ?  392 HOH   B O    1 
HETATM 7243 O  O    . HOH   H 6 .   ? 40.754 -6.585  -0.775  1.00 27.07 ?  393 HOH   B O    1 
HETATM 7244 O  O    . HOH   H 6 .   ? 28.032 -27.070 2.397   1.00 28.27 ?  394 HOH   B O    1 
HETATM 7245 O  O    . HOH   H 6 .   ? 26.629 -27.903 -13.381 1.00 38.33 ?  395 HOH   B O    1 
HETATM 7246 O  O    . HOH   H 6 .   ? 24.643 -20.610 -10.533 1.00 40.05 ?  396 HOH   B O    1 
HETATM 7247 O  O    . HOH   H 6 .   ? 26.822 -30.603 -12.558 1.00 28.92 ?  397 HOH   B O    1 
HETATM 7248 O  O    . HOH   H 6 .   ? 50.650 -30.927 8.867   1.00 31.01 ?  398 HOH   B O    1 
HETATM 7249 O  O    . HOH   H 6 .   ? 34.327 -33.461 9.660   1.00 37.71 ?  399 HOH   B O    1 
HETATM 7250 O  O    . HOH   H 6 .   ? 45.741 -20.022 15.286  1.00 44.73 ?  400 HOH   B O    1 
HETATM 7251 O  O    . HOH   H 6 .   ? 57.515 -6.407  -2.257  1.00 32.78 ?  401 HOH   B O    1 
HETATM 7252 O  O    . HOH   H 6 .   ? 40.930 -11.804 -22.201 1.00 41.32 ?  402 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   A VAL   A 3   ? 0.7208 0.7200 0.8385 -0.0014 -0.0225 0.0654  3   VAL   A N   
2    N  N   B VAL   A 3   ? 0.7065 0.6975 0.8171 -0.0119 -0.0175 0.0459  3   VAL   A N   
3    C  CA  A VAL   A 3   ? 0.7171 0.7166 0.8271 -0.0027 -0.0226 0.0648  3   VAL   A CA  
4    C  CA  B VAL   A 3   ? 0.7025 0.6936 0.8053 -0.0130 -0.0178 0.0456  3   VAL   A CA  
5    C  C   A VAL   A 3   ? 0.6986 0.7015 0.7859 -0.0107 -0.0231 0.0682  3   VAL   A C   
6    C  C   B VAL   A 3   ? 0.6833 0.6763 0.7611 -0.0203 -0.0182 0.0472  3   VAL   A C   
7    O  O   A VAL   A 3   ? 0.7031 0.7048 0.8006 -0.0096 -0.0245 0.0695  3   VAL   A O   
8    O  O   B VAL   A 3   ? 0.6878 0.6799 0.7750 -0.0195 -0.0191 0.0479  3   VAL   A O   
9    C  CB  A VAL   A 3   ? 0.7284 0.7258 0.8456 0.0023  -0.0206 0.0625  3   VAL   A CB  
10   C  CB  B VAL   A 3   ? 0.7142 0.7042 0.8260 -0.0084 -0.0163 0.0447  3   VAL   A CB  
11   C  CG1 A VAL   A 3   ? 0.7327 0.7292 0.8526 0.0039  -0.0197 0.0623  3   VAL   A CG1 
12   C  CG1 B VAL   A 3   ? 0.7188 0.7080 0.8335 -0.0069 -0.0156 0.0449  3   VAL   A CG1 
13   C  CG2 A VAL   A 3   ? 0.7315 0.7283 0.8528 0.0043  -0.0194 0.0624  3   VAL   A CG2 
14   C  CG2 B VAL   A 3   ? 0.7173 0.7074 0.8336 -0.0067 -0.0153 0.0452  3   VAL   A CG2 
31   N  N   A ASN   A 4   ? 0.6725 0.6805 0.7174 -0.0209 -0.0202 0.0705  4   ASN   A N   
32   N  N   B ASN   A 4   ? 0.6564 0.6522 0.6921 -0.0293 -0.0159 0.0488  4   ASN   A N   
33   C  CA  A ASN   A 4   ? 0.6442 0.6568 0.6424 -0.0325 -0.0166 0.0704  4   ASN   A CA  
34   C  CA  B ASN   A 4   ? 0.6274 0.6257 0.6172 -0.0393 -0.0138 0.0485  4   ASN   A CA  
35   C  C   A ASN   A 4   ? 0.6019 0.6244 0.5973 -0.0495 -0.0013 0.0574  4   ASN   A C   
36   C  C   B ASN   A 4   ? 0.5857 0.5913 0.5679 -0.0541 0.0022  0.0416  4   ASN   A C   
37   O  O   A ASN   A 4   ? 0.6056 0.6266 0.5945 -0.0488 -0.0039 0.0597  4   ASN   A O   
38   O  O   B ASN   A 4   ? 0.5887 0.5934 0.5640 -0.0533 0.0004  0.0438  4   ASN   A O   
39   C  CB  A ASN   A 4   ? 0.6559 0.6630 0.6086 -0.0291 -0.0265 0.0827  4   ASN   A CB  
40   C  CB  B ASN   A 4   ? 0.6379 0.6312 0.5877 -0.0362 -0.0261 0.0553  4   ASN   A CB  
41   C  CG  A ASN   A 4   ? 0.6656 0.6670 0.5785 -0.0272 -0.0333 0.0933  4   ASN   A CG  
42   C  CG  B ASN   A 4   ? 0.6465 0.6347 0.5621 -0.0342 -0.0355 0.0612  4   ASN   A CG  
43   O  OD1 A ASN   A 4   ? 0.6693 0.6674 0.5672 -0.0269 -0.0362 0.0971  4   ASN   A OD1 
44   O  OD1 B ASN   A 4   ? 0.6501 0.6350 0.5524 -0.0334 -0.0393 0.0637  4   ASN   A OD1 
45   N  ND2 A ASN   A 4   ? 0.6688 0.6693 0.5670 -0.0262 -0.0351 0.0983  4   ASN   A ND2 
46   N  ND2 B ASN   A 4   ? 0.6488 0.6363 0.5531 -0.0335 -0.0380 0.0641  4   ASN   A ND2 
59   N  N   A SER   A 5   ? 0.5535 0.5868 0.5512 -0.0682 0.0160  0.0435  5   SER   A N   
60   N  N   B SER   A 5   ? 0.5387 0.5525 0.5212 -0.0705 0.0192  0.0339  5   SER   A N   
61   C  CA  A SER   A 5   ? 0.5031 0.5466 0.5065 -0.0852 0.0346  0.0311  5   SER   A CA  
62   C  CA  B SER   A 5   ? 0.4896 0.5119 0.4769 -0.0853 0.0369  0.0267  5   SER   A CA  
63   C  C   A SER   A 5   ? 0.4493 0.4971 0.4393 -0.1009 0.0537  0.0275  5   SER   A C   
64   C  C   B SER   A 5   ? 0.4367 0.4639 0.4116 -0.0997 0.0573  0.0263  5   SER   A C   
65   O  O   A SER   A 5   ? 0.4512 0.5002 0.4388 -0.1006 0.0581  0.0217  5   SER   A O   
66   O  O   B SER   A 5   ? 0.4383 0.4659 0.4049 -0.0995 0.0601  0.0198  5   SER   A O   
67   C  CB  A SER   A 5   ? 0.5075 0.5542 0.5238 -0.0852 0.0357  0.0241  5   SER   A CB  
68   C  CB  B SER   A 5   ? 0.4935 0.5178 0.4936 -0.0839 0.0357  0.0212  5   SER   A CB  
69   O  OG  A SER   A 5   ? 0.5103 0.5585 0.5369 -0.0849 0.0387  0.0191  5   SER   A OG  
70   O  OG  B SER   A 5   ? 0.4960 0.5203 0.5062 -0.0829 0.0365  0.0166  5   SER   A OG  
81   N  N   A PHE   A 6   ? 0.3932 0.4429 0.3705 -0.1151 0.0664  0.0312  6   PHE   A N   
82   N  N   B PHE   A 6   ? 0.3815 0.4137 0.3511 -0.1131 0.0727  0.0312  6   PHE   A N   
83   C  CA  A PHE   A 6   ? 0.3405 0.3901 0.3107 -0.1233 0.0696  0.0387  6   PHE   A CA  
84   C  CA  B PHE   A 6   ? 0.3285 0.3657 0.3046 -0.1199 0.0775  0.0359  6   PHE   A CA  
85   C  C   A PHE   A 6   ? 0.3256 0.3793 0.2982 -0.1258 0.0797  0.0337  6   PHE   A C   
86   C  C   B PHE   A 6   ? 0.3121 0.3561 0.3079 -0.1147 0.0858  0.0286  6   PHE   A C   
87   O  O   A PHE   A 6   ? 0.3273 0.3874 0.3305 -0.1258 0.0809  0.0372  6   PHE   A O   
88   O  O   B PHE   A 6   ? 0.3158 0.3617 0.3300 -0.1105 0.0870  0.0338  6   PHE   A O   
89   C  CB  A PHE   A 6   ? 0.3115 0.3553 0.2692 -0.1184 0.0496  0.0409  6   PHE   A CB  
90   C  CB  B PHE   A 6   ? 0.2996 0.3342 0.2656 -0.1238 0.0636  0.0434  6   PHE   A CB  
91   C  CG  A PHE   A 6   ? 0.2879 0.3299 0.2453 -0.1057 0.0325  0.0387  6   PHE   A CG  
92   C  CG  B PHE   A 6   ? 0.2783 0.3139 0.2438 -0.1169 0.0498  0.0461  6   PHE   A CG  
93   C  CD1 A PHE   A 6   ? 0.2762 0.3157 0.2356 -0.0962 0.0269  0.0380  6   PHE   A CD1 
94   C  CD1 B PHE   A 6   ? 0.2682 0.3042 0.2344 -0.1114 0.0510  0.0480  6   PHE   A CD1 
95   C  CD2 A PHE   A 6   ? 0.2842 0.3260 0.2518 -0.0908 0.0264  0.0364  6   PHE   A CD2 
96   C  CD2 B PHE   A 6   ? 0.2757 0.3120 0.2514 -0.1060 0.0394  0.0426  6   PHE   A CD2 
97   C  CE1 A PHE   A 6   ? 0.2711 0.3104 0.2356 -0.0891 0.0224  0.0375  6   PHE   A CE1 
98   C  CE1 B PHE   A 6   ? 0.2640 0.3011 0.2335 -0.1069 0.0456  0.0451  6   PHE   A CE1 
99   C  CE2 A PHE   A 6   ? 0.2780 0.3202 0.2613 -0.0837 0.0240  0.0298  6   PHE   A CE2 
100  C  CE2 B PHE   A 6   ? 0.2703 0.3099 0.2588 -0.1005 0.0359  0.0331  6   PHE   A CE2 
101  C  CZ  A PHE   A 6   ? 0.2729 0.3122 0.2487 -0.0851 0.0180  0.0297  6   PHE   A CZ  
102  C  CZ  B PHE   A 6   ? 0.2664 0.3032 0.2492 -0.1033 0.0346  0.0349  6   PHE   A CZ  
121  N  N   A SER   A 7   ? 0.3099 0.3591 0.2698 -0.1235 0.0804  0.0268  7   SER   A N   
122  N  N   B SER   A 7   ? 0.2924 0.3389 0.2965 -0.1116 0.0881  0.0199  7   SER   A N   
123  C  CA  A SER   A 7   ? 0.2994 0.3458 0.2627 -0.1099 0.0779  0.0050  7   SER   A CA  
124  C  CA  B SER   A 7   ? 0.2727 0.3274 0.2983 -0.0979 0.0844  -0.0003 7   SER   A CA  
125  C  C   A SER   A 7   ? 0.2780 0.3186 0.2421 -0.0975 0.0893  0.0109  7   SER   A C   
126  C  C   B SER   A 7   ? 0.2489 0.2988 0.2603 -0.0900 0.0868  -0.0026 7   SER   A C   
127  O  O   A SER   A 7   ? 0.2851 0.3162 0.2305 -0.0967 0.1002  0.0097  7   SER   A O   
128  O  O   B SER   A 7   ? 0.2486 0.2980 0.2631 -0.0924 0.0961  -0.0033 7   SER   A O   
129  C  CB  A SER   A 7   ? 0.3094 0.3561 0.2763 -0.1084 0.0749  -0.0012 7   SER   A CB  
130  C  CB  B SER   A 7   ? 0.2821 0.3446 0.3392 -0.0855 0.0802  -0.0042 7   SER   A CB  
131  O  OG  A SER   A 7   ? 0.3214 0.3630 0.2945 -0.1040 0.0701  -0.0087 7   SER   A OG  
132  O  OG  B SER   A 7   ? 0.2941 0.3540 0.3673 -0.0746 0.0757  0.0003  7   SER   A OG  
143  N  N   A GLY   A 8   ? 0.2544 0.2938 0.2464 -0.0822 0.0783  0.0059  8   GLY   A N   
144  N  N   B GLY   A 8   ? 0.2242 0.2704 0.2367 -0.0788 0.0687  -0.0096 8   GLY   A N   
145  C  CA  A GLY   A 8   ? 0.2352 0.2667 0.2398 -0.0573 0.0678  0.0093  8   GLY   A CA  
146  C  CA  B GLY   A 8   ? 0.2095 0.2449 0.2198 -0.0540 0.0550  -0.0047 8   GLY   A CA  
147  C  C   A GLY   A 8   ? 0.2046 0.2429 0.2277 -0.0391 0.0577  0.0164  8   GLY   A C   
148  C  C   B GLY   A 8   ? 0.1859 0.2233 0.2003 -0.0358 0.0467  0.0007  8   GLY   A C   
149  O  O   A GLY   A 8   ? 0.2107 0.2451 0.2496 -0.0206 0.0493  -0.0015 8   GLY   A O   
150  O  O   B GLY   A 8   ? 0.1872 0.2233 0.2063 -0.0182 0.0501  -0.0070 8   GLY   A O   
157  N  N   A TYR   A 9   ? 0.1759 0.2161 0.2182 -0.0341 0.0429  0.0360  9   TYR   A N   
158  N  N   B TYR   A 9   ? 0.1693 0.2049 0.1923 -0.0293 0.0278  0.0031  9   TYR   A N   
159  C  CA  A TYR   A 9   ? 0.1563 0.2007 0.2019 -0.0232 0.0364  0.0471  9   TYR   A CA  
160  C  CA  B TYR   A 9   ? 0.1571 0.1928 0.1807 -0.0182 0.0240  0.0116  9   TYR   A CA  
161  C  C   A TYR   A 9   ? 0.1472 0.1792 0.1982 -0.0026 0.0403  0.0560  9   TYR   A C   
162  C  C   B TYR   A 9   ? 0.1522 0.1722 0.1758 -0.0070 0.0295  0.0148  9   TYR   A C   
163  O  O   A TYR   A 9   ? 0.1579 0.1946 0.2089 0.0015  0.0417  0.0470  9   TYR   A O   
164  O  O   B TYR   A 9   ? 0.1600 0.1763 0.1804 -0.0080 0.0329  0.0011  9   TYR   A O   
165  C  CB  A TYR   A 9   ? 0.1539 0.2139 0.2035 -0.0181 0.0278  0.0309  9   TYR   A CB  
166  C  CB  B TYR   A 9   ? 0.1550 0.2045 0.1909 -0.0115 0.0207  0.0190  9   TYR   A CB  
167  C  CG  A TYR   A 9   ? 0.1551 0.2213 0.1988 -0.0131 0.0329  0.0179  9   TYR   A CG  
168  C  CG  B TYR   A 9   ? 0.1550 0.2119 0.1979 -0.0076 0.0251  0.0197  9   TYR   A CG  
169  C  CD1 A TYR   A 9   ? 0.1564 0.2249 0.2110 -0.0205 0.0391  0.0073  9   TYR   A CD1 
170  C  CD1 B TYR   A 9   ? 0.1581 0.2157 0.2044 -0.0186 0.0167  0.0246  9   TYR   A CD1 
171  C  CD2 A TYR   A 9   ? 0.1556 0.2146 0.1939 -0.0165 0.0191  0.0296  9   TYR   A CD2 
172  C  CD2 B TYR   A 9   ? 0.1495 0.2061 0.1945 -0.0053 0.0225  0.0281  9   TYR   A CD2 
173  C  CE1 A TYR   A 9   ? 0.1597 0.2267 0.2211 -0.0172 0.0364  -0.0015 9   TYR   A CE1 
174  C  CE1 B TYR   A 9   ? 0.1528 0.2155 0.2019 -0.0161 0.0231  0.0216  9   TYR   A CE1 
175  C  CE2 A TYR   A 9   ? 0.1608 0.2164 0.2111 -0.0208 0.0240  0.0214  9   TYR   A CE2 
176  C  CE2 B TYR   A 9   ? 0.1444 0.2049 0.1982 -0.0068 0.0234  0.0246  9   TYR   A CE2 
177  C  CZ  A TYR   A 9   ? 0.1610 0.2225 0.2313 -0.0246 0.0358  0.0063  9   TYR   A CZ  
178  C  CZ  B TYR   A 9   ? 0.1413 0.2044 0.1963 -0.0140 0.0274  0.0241  9   TYR   A CZ  
179  O  OH  A TYR   A 9   ? 0.1613 0.2233 0.2645 -0.0300 0.0308  -0.0001 9   TYR   A OH  
180  O  OH  B TYR   A 9   ? 0.1275 0.2068 0.2052 -0.0248 0.0295  0.0239  9   TYR   A OH  
199  N  N   A LEU   A 10  ? 0.1444 0.1688 0.1881 -0.0056 0.0361  0.0439  10  LEU   A N   
200  N  N   B LEU   A 10  ? 0.1475 0.1585 0.1807 -0.0083 0.0205  0.0273  10  LEU   A N   
201  C  CA  A LEU   A 10  ? 0.1423 0.1715 0.2044 -0.0093 0.0111  0.0505  10  LEU   A CA  
202  C  CA  B LEU   A 10  ? 0.1460 0.1572 0.1810 -0.0175 0.0206  0.0446  10  LEU   A CA  
203  C  C   A LEU   A 10  ? 0.1430 0.1612 0.1895 -0.0132 0.0009  0.0426  10  LEU   A C   
204  C  C   B LEU   A 10  ? 0.1431 0.1467 0.1721 -0.0193 0.0312  0.0236  10  LEU   A C   
205  O  O   A LEU   A 10  ? 0.1499 0.1482 0.1715 -0.0159 0.0153  0.0286  10  LEU   A O   
206  O  O   B LEU   A 10  ? 0.1522 0.1330 0.1643 -0.0220 0.0577  0.0033  10  LEU   A O   
207  C  CB  A LEU   A 10  ? 0.1480 0.1858 0.2453 -0.0189 -0.0051 0.0653  10  LEU   A CB  
208  C  CB  B LEU   A 10  ? 0.1506 0.1751 0.2117 -0.0182 0.0118  0.0658  10  LEU   A CB  
209  C  CG  A LEU   A 10  ? 0.1660 0.2077 0.2946 -0.0145 -0.0232 0.0716  10  LEU   A CG  
210  C  CG  B LEU   A 10  ? 0.1668 0.1831 0.2253 -0.0073 0.0056  0.0820  10  LEU   A CG  
211  C  CD1 A LEU   A 10  ? 0.1832 0.2170 0.3214 -0.0184 -0.0129 0.0537  10  LEU   A CD1 
212  C  CD1 B LEU   A 10  ? 0.1760 0.1898 0.2254 -0.0046 0.0104  0.0726  10  LEU   A CD1 
213  C  CD2 A LEU   A 10  ? 0.1797 0.2230 0.3120 -0.0030 -0.0127 0.0622  10  LEU   A CD2 
214  C  CD2 B LEU   A 10  ? 0.1777 0.1928 0.2321 -0.0086 0.0155  0.0763  10  LEU   A CD2 
237  N  N   A LYS   A 11  ? 0.1477 0.1628 0.1913 -0.0198 -0.0063 0.0499  11  LYS   A N   
238  N  N   B LYS   A 11  ? 0.1383 0.1475 0.1754 -0.0198 0.0230  0.0346  11  LYS   A N   
239  C  CA  A LYS   A 11  ? 0.1549 0.1550 0.1871 -0.0302 -0.0057 0.0408  11  LYS   A CA  
240  C  CA  B LYS   A 11  ? 0.1388 0.1399 0.1859 -0.0289 0.0213  0.0332  11  LYS   A CA  
241  C  C   A LYS   A 11  ? 0.1549 0.1681 0.1853 -0.0384 -0.0161 0.0368  11  LYS   A C   
242  C  C   B LYS   A 11  ? 0.1407 0.1508 0.1948 -0.0305 0.0187  0.0416  11  LYS   A C   
243  O  O   A LYS   A 11  ? 0.1639 0.1954 0.1869 -0.0590 -0.0191 0.0419  11  LYS   A O   
244  O  O   B LYS   A 11  ? 0.1450 0.1706 0.2041 -0.0315 0.0103  0.0588  11  LYS   A O   
245  C  CB  A LYS   A 11  ? 0.1717 0.1438 0.1799 -0.0214 -0.0027 0.0215  11  LYS   A CB  
246  C  CB  B LYS   A 11  ? 0.1484 0.1355 0.1858 -0.0290 0.0189  0.0269  11  LYS   A CB  
247  C  CG  A LYS   A 11  ? 0.1833 0.1498 0.1774 -0.0194 -0.0041 0.0207  11  LYS   A CG  
248  C  CG  B LYS   A 11  ? 0.1545 0.1386 0.1880 -0.0289 0.0234  0.0281  11  LYS   A CG  
249  C  CD  A LYS   A 11  ? 0.1949 0.1508 0.1681 -0.0109 -0.0062 0.0170  11  LYS   A CD  
250  C  CD  B LYS   A 11  ? 0.1664 0.1496 0.1963 -0.0226 0.0185  0.0308  11  LYS   A CD  
251  C  CE  A LYS   A 11  ? 0.2021 0.1544 0.1617 -0.0104 -0.0003 0.0237  11  LYS   A CE  
252  C  CE  B LYS   A 11  ? 0.1716 0.1520 0.2061 -0.0184 0.0224  0.0328  11  LYS   A CE  
253  N  NZ  A LYS   A 11  ? 0.2010 0.1555 0.1688 0.0011  -0.0067 0.0357  11  LYS   A NZ  
254  N  NZ  B LYS   A 11  ? 0.1705 0.1496 0.2176 -0.0101 0.0246  0.0274  11  LYS   A NZ  
281  N  N   A LEU   A 12  ? 0.1497 0.1524 0.1842 -0.0246 -0.0132 0.0332  12  LEU   A N   
282  N  N   B LEU   A 12  ? 0.1384 0.1405 0.1793 -0.0312 0.0239  0.0274  12  LEU   A N   
283  C  CA  A LEU   A 12  ? 0.1525 0.1697 0.1669 -0.0138 -0.0082 0.0393  12  LEU   A CA  
284  C  CA  B LEU   A 12  ? 0.1537 0.1472 0.1635 -0.0233 0.0161  0.0274  12  LEU   A CA  
285  C  C   A LEU   A 12  ? 0.1489 0.1653 0.1729 -0.0248 0.0040  0.0341  12  LEU   A C   
286  C  C   B LEU   A 12  ? 0.1573 0.1376 0.1605 -0.0317 0.0137  0.0210  12  LEU   A C   
287  O  O   A LEU   A 12  ? 0.1593 0.1730 0.1805 -0.0222 0.0079  0.0326  12  LEU   A O   
288  O  O   B LEU   A 12  ? 0.1597 0.1432 0.1604 -0.0279 0.0145  0.0033  12  LEU   A O   
289  C  CB  A LEU   A 12  ? 0.1660 0.1771 0.1845 -0.0110 -0.0070 0.0442  12  LEU   A CB  
290  C  CB  B LEU   A 12  ? 0.1648 0.1471 0.1596 -0.0186 0.0100  0.0238  12  LEU   A CB  
291  C  CG  A LEU   A 12  ? 0.1744 0.1746 0.2156 -0.0084 0.0119  0.0473  12  LEU   A CG  
292  C  CG  B LEU   A 12  ? 0.1747 0.1509 0.1735 -0.0117 0.0259  0.0226  12  LEU   A CG  
293  C  CD1 A LEU   A 12  ? 0.1867 0.1773 0.2094 0.0012  0.0169  0.0416  12  LEU   A CD1 
294  C  CD1 B LEU   A 12  ? 0.1865 0.1484 0.1800 -0.0058 0.0343  0.0310  12  LEU   A CD1 
295  C  CD2 A LEU   A 12  ? 0.1704 0.1788 0.2376 -0.0119 0.0173  0.0431  12  LEU   A CD2 
296  C  CD2 B LEU   A 12  ? 0.1761 0.1540 0.1921 -0.0061 0.0171  0.0241  12  LEU   A CD2 
319  N  N   A THR   A 13  ? 0.1451 0.1544 0.1772 -0.0195 0.0087  0.0148  13  THR   A N   
320  N  N   B THR   A 13  ? 0.1604 0.1410 0.1769 -0.0261 0.0198  0.0052  13  THR   A N   
321  C  CA  A THR   A 13  ? 0.1493 0.1496 0.1769 -0.0284 0.0103  0.0075  13  THR   A CA  
322  C  CA  B THR   A 13  ? 0.1576 0.1463 0.1825 -0.0206 0.0341  0.0015  13  THR   A CA  
323  C  C   A THR   A 13  ? 0.1484 0.1395 0.1782 -0.0255 0.0158  0.0149  13  THR   A C   
324  C  C   B THR   A 13  ? 0.1476 0.1379 0.1858 -0.0123 0.0325  0.0099  13  THR   A C   
325  O  O   A THR   A 13  ? 0.1579 0.1382 0.1743 -0.0213 0.0170  0.0113  13  THR   A O   
326  O  O   B THR   A 13  ? 0.1463 0.1401 0.1851 -0.0046 0.0340  0.0092  13  THR   A O   
327  C  CB  A THR   A 13  ? 0.1541 0.1682 0.1836 -0.0254 0.0141  0.0146  13  THR   A CB  
328  C  CB  B THR   A 13  ? 0.1656 0.1552 0.1913 -0.0196 0.0345  0.0047  13  THR   A CB  
329  O  OG1 A THR   A 13  ? 0.1482 0.1634 0.1717 -0.0237 0.0246  0.0195  13  THR   A OG1 
330  O  OG1 B THR   A 13  ? 0.1733 0.1458 0.2100 -0.0157 0.0273  -0.0021 13  THR   A OG1 
331  C  CG2 A THR   A 13  ? 0.1618 0.1873 0.2236 -0.0173 0.0135  0.0071  13  THR   A CG2 
332  C  CG2 B THR   A 13  ? 0.1733 0.1742 0.2004 -0.0209 0.0409  0.0039  13  THR   A CG2 
347  N  N   A ASP   A 14  ? 0.1578 0.1414 0.2055 -0.0207 0.0166  0.0283  14  ASP   A N   
348  N  N   B ASP   A 14  ? 0.1533 0.1437 0.2053 -0.0094 0.0254  0.0097  14  ASP   A N   
349  C  CA  A ASP   A 14  ? 0.1617 0.1415 0.2321 -0.0129 0.0135  0.0467  14  ASP   A CA  
350  C  CA  B ASP   A 14  ? 0.1573 0.1559 0.2125 -0.0106 0.0212  0.0167  14  ASP   A CA  
351  C  C   A ASP   A 14  ? 0.1586 0.1467 0.2106 -0.0092 0.0104  0.0468  14  ASP   A C   
352  C  C   B ASP   A 14  ? 0.1507 0.1503 0.1741 -0.0120 0.0204  0.0196  14  ASP   A C   
353  O  O   A ASP   A 14  ? 0.1633 0.1544 0.2162 -0.0160 0.0285  0.0377  14  ASP   A O   
354  O  O   B ASP   A 14  ? 0.1538 0.1609 0.1679 -0.0070 0.0301  0.0243  14  ASP   A O   
355  C  CB  A ASP   A 14  ? 0.1801 0.1594 0.2984 -0.0195 0.0183  0.0587  14  ASP   A CB  
356  C  CB  B ASP   A 14  ? 0.1807 0.1892 0.2720 -0.0060 0.0177  0.0193  14  ASP   A CB  
357  C  CG  A ASP   A 14  ? 0.1979 0.2081 0.3662 -0.0227 0.0312  0.0509  14  ASP   A CG  
358  C  CG  B ASP   A 14  ? 0.2035 0.2243 0.3328 -0.0025 0.0088  0.0165  14  ASP   A CG  
359  O  OD1 A ASP   A 14  ? 0.2010 0.2241 0.3852 -0.0313 0.0230  0.0630  14  ASP   A OD1 
360  O  OD1 B ASP   A 14  ? 0.2094 0.2292 0.3487 0.0013  -0.0175 0.0339  14  ASP   A OD1 
361  O  OD2 A ASP   A 14  ? 0.2146 0.2294 0.3970 -0.0156 0.0269  0.0219  14  ASP   A OD2 
362  O  OD2 B ASP   A 14  ? 0.2192 0.2457 0.3620 0.0045  0.0128  -0.0046 14  ASP   A OD2 
371  N  N   A ASN   A 15  ? 0.1514 0.1417 0.2040 -0.0083 0.0041  0.0394  15  ASN   A N   
372  N  N   B ASN   A 15  ? 0.1410 0.1322 0.1684 -0.0257 0.0223  0.0167  15  ASN   A N   
373  C  CA  A ASN   A 15  ? 0.1457 0.1465 0.1895 0.0004  -0.0044 0.0210  15  ASN   A CA  
374  C  CA  B ASN   A 15  ? 0.1436 0.1325 0.1762 -0.0163 0.0246  0.0021  15  ASN   A CA  
375  C  C   A ASN   A 15  ? 0.1395 0.1430 0.1941 -0.0094 0.0083  0.0215  15  ASN   A C   
376  C  C   B ASN   A 15  ? 0.1444 0.1322 0.1776 -0.0163 0.0204  -0.0026 15  ASN   A C   
377  O  O   A ASN   A 15  ? 0.1451 0.1477 0.2039 -0.0147 0.0025  0.0150  15  ASN   A O   
378  O  O   B ASN   A 15  ? 0.1371 0.1319 0.1990 -0.0085 0.0042  0.0015  15  ASN   A O   
379  C  CB  A ASN   A 15  ? 0.1557 0.1481 0.1785 0.0024  0.0007  0.0191  15  ASN   A CB  
380  C  CB  B ASN   A 15  ? 0.1427 0.1365 0.1669 -0.0211 0.0205  -0.0019 15  ASN   A CB  
381  C  CG  A ASN   A 15  ? 0.1627 0.1542 0.1765 -0.0010 0.0109  0.0079  15  ASN   A CG  
382  C  CG  B ASN   A 15  ? 0.1416 0.1525 0.1730 -0.0219 0.0350  -0.0002 15  ASN   A CG  
383  O  OD1 A ASN   A 15  ? 0.1730 0.1498 0.1764 -0.0109 0.0183  0.0097  15  ASN   A OD1 
384  O  OD1 B ASN   A 15  ? 0.1491 0.1535 0.1610 -0.0276 0.0410  -0.0099 15  ASN   A OD1 
385  N  ND2 A ASN   A 15  ? 0.1696 0.1678 0.1769 -0.0030 0.0053  0.0159  15  ASN   A ND2 
386  N  ND2 B ASN   A 15  ? 0.1445 0.1623 0.1711 -0.0243 0.0287  0.0163  15  ASN   A ND2 
399  N  N   A VAL   A 16  ? 0.1433 0.1402 0.1958 -0.0163 0.0067  0.0400  16  VAL   A N   
400  N  N   B VAL   A 16  ? 0.1506 0.1407 0.1569 -0.0179 0.0156  0.0048  16  VAL   A N   
401  C  CA  A VAL   A 16  ? 0.1469 0.1441 0.1777 -0.0105 0.0044  0.0360  16  VAL   A CA  
402  C  CA  B VAL   A 16  ? 0.1510 0.1428 0.1635 -0.0234 0.0126  0.0130  16  VAL   A CA  
403  C  C   A VAL   A 16  ? 0.1382 0.1489 0.1857 -0.0130 0.0040  0.0291  16  VAL   A C   
404  C  C   B VAL   A 16  ? 0.1450 0.1350 0.1564 -0.0237 0.0156  0.0116  16  VAL   A C   
405  O  O   A VAL   A 16  ? 0.1417 0.1486 0.2004 -0.0165 0.0126  0.0167  16  VAL   A O   
406  O  O   B VAL   A 16  ? 0.1369 0.1335 0.1496 -0.0351 0.0203  0.0094  16  VAL   A O   
407  C  CB  A VAL   A 16  ? 0.1653 0.1590 0.1702 0.0070  0.0072  0.0344  16  VAL   A CB  
408  C  CB  B VAL   A 16  ? 0.1632 0.1586 0.1684 -0.0099 0.0256  0.0188  16  VAL   A CB  
409  C  CG1 A VAL   A 16  ? 0.1775 0.1660 0.1673 0.0121  0.0125  0.0339  16  VAL   A CG1 
410  C  CG1 B VAL   A 16  ? 0.1713 0.1720 0.1730 -0.0065 0.0219  0.0274  16  VAL   A CG1 
411  C  CG2 A VAL   A 16  ? 0.1681 0.1715 0.1896 0.0139  0.0213  0.0224  16  VAL   A CG2 
412  C  CG2 B VAL   A 16  ? 0.1641 0.1633 0.1679 -0.0121 0.0381  0.0171  16  VAL   A CG2 
431  N  N   A TYR   A 17  ? 0.1353 0.1428 0.1912 -0.0168 0.0144  0.0314  17  TYR   A N   
432  N  N   B TYR   A 17  ? 0.1420 0.1291 0.1751 -0.0198 0.0255  0.0138  17  TYR   A N   
433  C  CA  A TYR   A 17  ? 0.1423 0.1453 0.1741 -0.0205 0.0114  0.0314  17  TYR   A CA  
434  C  CA  B TYR   A 17  ? 0.1483 0.1325 0.1650 -0.0201 0.0274  0.0108  17  TYR   A CA  
435  C  C   A TYR   A 17  ? 0.1421 0.1484 0.1891 -0.0097 0.0127  0.0335  17  TYR   A C   
436  C  C   B TYR   A 17  ? 0.1520 0.1291 0.1750 -0.0226 0.0244  0.0047  17  TYR   A C   
437  O  O   A TYR   A 17  ? 0.1365 0.1504 0.1686 -0.0094 0.0149  0.0349  17  TYR   A O   
438  O  O   B TYR   A 17  ? 0.1471 0.1254 0.1572 -0.0247 0.0306  0.0055  17  TYR   A O   
439  C  CB  A TYR   A 17  ? 0.1561 0.1471 0.1811 -0.0263 -0.0064 0.0316  17  TYR   A CB  
440  C  CB  B TYR   A 17  ? 0.1552 0.1401 0.1645 -0.0223 0.0194  0.0284  17  TYR   A CB  
441  C  CG  A TYR   A 17  ? 0.1820 0.1557 0.1986 -0.0295 -0.0178 0.0305  17  TYR   A CG  
442  C  CG  B TYR   A 17  ? 0.1826 0.1483 0.1907 -0.0263 -0.0037 0.0393  17  TYR   A CG  
443  C  CD1 A TYR   A 17  ? 0.1968 0.1598 0.2158 -0.0207 -0.0209 0.0363  17  TYR   A CD1 
444  C  CD1 B TYR   A 17  ? 0.1924 0.1545 0.2080 -0.0239 -0.0154 0.0368  17  TYR   A CD1 
445  C  CD2 A TYR   A 17  ? 0.1927 0.1658 0.1944 -0.0368 -0.0181 0.0344  17  TYR   A CD2 
446  C  CD2 B TYR   A 17  ? 0.1960 0.1505 0.1902 -0.0368 -0.0087 0.0437  17  TYR   A CD2 
447  C  CE1 A TYR   A 17  ? 0.2057 0.1681 0.2281 -0.0234 -0.0151 0.0446  17  TYR   A CE1 
448  C  CE1 B TYR   A 17  ? 0.1996 0.1554 0.2138 -0.0277 -0.0260 0.0379  17  TYR   A CE1 
449  C  CE2 A TYR   A 17  ? 0.2025 0.1718 0.1974 -0.0379 -0.0225 0.0349  17  TYR   A CE2 
450  C  CE2 B TYR   A 17  ? 0.2054 0.1540 0.1907 -0.0410 -0.0268 0.0374  17  TYR   A CE2 
451  C  CZ  A TYR   A 17  ? 0.2076 0.1743 0.2090 -0.0320 -0.0253 0.0524  17  TYR   A CZ  
452  C  CZ  B TYR   A 17  ? 0.2098 0.1547 0.1978 -0.0363 -0.0326 0.0456  17  TYR   A CZ  
453  O  OH  A TYR   A 17  ? 0.2158 0.1832 0.2269 -0.0263 -0.0142 0.0466  17  TYR   A OH  
454  O  OH  B TYR   A 17  ? 0.2225 0.1554 0.2025 -0.0314 -0.0369 0.0387  17  TYR   A OH  
473  N  N   A ILE   A 18  ? 0.1319 0.1475 0.1991 -0.0093 0.0186  0.0518  18  ILE   A N   
474  N  N   B ILE   A 18  ? 0.1523 0.1392 0.1954 -0.0235 0.0269  0.0267  18  ILE   A N   
475  C  CA  A ILE   A 18  ? 0.1353 0.1450 0.1885 -0.0095 0.0199  0.0498  18  ILE   A CA  
476  C  CA  B ILE   A 18  ? 0.1506 0.1443 0.1966 -0.0154 0.0289  0.0228  18  ILE   A CA  
477  C  C   A ILE   A 18  ? 0.1385 0.1552 0.1916 -0.0169 0.0159  0.0505  18  ILE   A C   
478  C  C   B ILE   A 18  ? 0.1549 0.1491 0.2113 -0.0194 0.0313  0.0227  18  ILE   A C   
479  O  O   A ILE   A 18  ? 0.1404 0.1681 0.1999 -0.0200 0.0271  0.0572  18  ILE   A O   
480  O  O   B ILE   A 18  ? 0.1567 0.1581 0.2127 -0.0242 0.0346  0.0271  18  ILE   A O   
481  C  CB  A ILE   A 18  ? 0.1504 0.1413 0.1828 -0.0030 0.0221  0.0467  18  ILE   A CB  
482  C  CB  B ILE   A 18  ? 0.1526 0.1453 0.1848 -0.0081 0.0203  0.0331  18  ILE   A CB  
483  C  CG1 A ILE   A 18  ? 0.1682 0.1570 0.1984 -0.0120 0.0210  0.0477  18  ILE   A CG1 
484  C  CG1 B ILE   A 18  ? 0.1571 0.1528 0.1820 -0.0016 0.0148  0.0313  18  ILE   A CG1 
485  C  CG2 A ILE   A 18  ? 0.1621 0.1496 0.1977 -0.0087 0.0138  0.0524  18  ILE   A CG2 
486  C  CG2 B ILE   A 18  ? 0.1459 0.1387 0.1844 -0.0007 0.0256  0.0280  18  ILE   A CG2 
487  C  CD1 A ILE   A 18  ? 0.1975 0.1803 0.2149 -0.0081 0.0181  0.0454  18  ILE   A CD1 
488  C  CD1 B ILE   A 18  ? 0.1795 0.1668 0.1953 0.0070  0.0095  0.0508  18  ILE   A CD1 
511  N  N   A LYS   A 19  ? 0.1422 0.1616 0.1742 -0.0105 0.0365  0.0409  19  LYS   A N   
512  N  N   B LYS   A 19  ? 0.1542 0.1533 0.2090 -0.0134 0.0361  0.0248  19  LYS   A N   
513  C  CA  A LYS   A 19  ? 0.1547 0.1768 0.1575 -0.0076 0.0401  0.0375  19  LYS   A CA  
514  C  CA  B LYS   A 19  ? 0.1558 0.1650 0.1997 -0.0085 0.0258  0.0208  19  LYS   A CA  
515  C  C   A LYS   A 19  ? 0.1588 0.1671 0.1726 -0.0116 0.0372  0.0355  19  LYS   A C   
516  C  C   B LYS   A 19  ? 0.1471 0.1619 0.1977 -0.0081 0.0301  0.0218  19  LYS   A C   
517  O  O   A LYS   A 19  ? 0.1556 0.1635 0.1858 -0.0129 0.0295  0.0372  19  LYS   A O   
518  O  O   B LYS   A 19  ? 0.1429 0.1587 0.1796 -0.0012 0.0325  0.0358  19  LYS   A O   
519  C  CB  A LYS   A 19  ? 0.1587 0.1945 0.1698 -0.0130 0.0331  0.0292  19  LYS   A CB  
520  C  CB  B LYS   A 19  ? 0.1659 0.1824 0.1972 -0.0109 0.0187  0.0185  19  LYS   A CB  
521  C  CG  A LYS   A 19  ? 0.1864 0.2121 0.1739 -0.0143 0.0239  0.0314  19  LYS   A CG  
522  C  CG  B LYS   A 19  ? 0.1703 0.1974 0.1987 -0.0145 0.0117  0.0174  19  LYS   A CG  
523  C  CD  A LYS   A 19  ? 0.2073 0.2267 0.1874 -0.0134 0.0230  0.0384  19  LYS   A CD  
524  C  CD  B LYS   A 19  ? 0.1786 0.2173 0.2033 -0.0093 0.0061  0.0162  19  LYS   A CD  
525  C  CE  A LYS   A 19  ? 0.2175 0.2302 0.2015 -0.0160 0.0208  0.0366  19  LYS   A CE  
526  C  CE  B LYS   A 19  ? 0.1889 0.2239 0.1981 -0.0088 0.0092  0.0232  19  LYS   A CE  
527  N  NZ  A LYS   A 19  ? 0.2198 0.2368 0.2056 -0.0198 0.0293  0.0306  19  LYS   A NZ  
528  N  NZ  B LYS   A 19  ? 0.1921 0.2334 0.1878 0.0038  0.0153  0.0164  19  LYS   A NZ  
555  N  N   A ASN   A 20  ? 0.1652 0.1674 0.1982 -0.0130 0.0475  0.0426  20  ASN   A N   
556  N  N   B ASN   A 20  ? 0.1454 0.1707 0.2198 -0.0065 0.0316  0.0339  20  ASN   A N   
557  C  CA  A ASN   A 20  ? 0.1685 0.1766 0.2003 -0.0020 0.0425  0.0368  20  ASN   A CA  
558  C  CA  B ASN   A 20  ? 0.1440 0.1850 0.2235 0.0108  0.0302  0.0287  20  ASN   A CA  
559  C  C   A ASN   A 20  ? 0.1770 0.1845 0.1991 -0.0099 0.0558  0.0337  20  ASN   A C   
560  C  C   B ASN   A 20  ? 0.1549 0.1960 0.2182 0.0106  0.0385  0.0310  20  ASN   A C   
561  O  O   A ASN   A 20  ? 0.1843 0.1982 0.1956 -0.0209 0.0522  0.0369  20  ASN   A O   
562  O  O   B ASN   A 20  ? 0.1750 0.2115 0.2194 0.0079  0.0331  0.0305  20  ASN   A O   
563  C  CB  A ASN   A 20  ? 0.1755 0.1760 0.2137 0.0082  0.0426  0.0325  20  ASN   A CB  
564  C  CB  B ASN   A 20  ? 0.1332 0.1844 0.2186 0.0097  0.0299  0.0250  20  ASN   A CB  
565  C  CG  A ASN   A 20  ? 0.1941 0.1772 0.2311 0.0178  0.0439  0.0201  20  ASN   A CG  
566  C  CG  B ASN   A 20  ? 0.1312 0.1830 0.2112 0.0216  0.0262  0.0300  20  ASN   A CG  
567  O  OD1 A ASN   A 20  ? 0.2223 0.1986 0.2800 0.0294  0.0565  0.0050  20  ASN   A OD1 
568  O  OD1 B ASN   A 20  ? 0.1377 0.1754 0.2197 0.0296  0.0287  0.0194  20  ASN   A OD1 
569  N  ND2 A ASN   A 20  ? 0.1952 0.1686 0.2260 0.0145  0.0285  0.0300  20  ASN   A ND2 
570  N  ND2 B ASN   A 20  ? 0.1450 0.1826 0.2097 0.0180  0.0106  0.0502  20  ASN   A ND2 
583  N  N   A ALA   A 21  ? 0.1831 0.1804 0.2126 -0.0105 0.0458  0.0262  21  ALA   A N   
584  N  N   B ALA   A 21  ? 0.1613 0.1921 0.2312 0.0046  0.0477  0.0251  21  ALA   A N   
585  C  CA  A ALA   A 21  ? 0.1932 0.1764 0.2069 -0.0142 0.0415  0.0422  21  ALA   A CA  
586  C  CA  B ALA   A 21  ? 0.1732 0.1866 0.2328 -0.0014 0.0394  0.0318  21  ALA   A CA  
587  C  C   A ALA   A 21  ? 0.1964 0.1755 0.2138 -0.0059 0.0379  0.0232  21  ALA   A C   
588  C  C   B ALA   A 21  ? 0.1627 0.1715 0.2191 -0.0166 0.0555  0.0226  21  ALA   A C   
589  O  O   A ALA   A 21  ? 0.2000 0.1891 0.2254 -0.0068 0.0374  0.0137  21  ALA   A O   
590  O  O   B ALA   A 21  ? 0.1508 0.1658 0.2217 -0.0291 0.0632  0.0044  21  ALA   A O   
591  C  CB  A ALA   A 21  ? 0.1993 0.1804 0.2251 -0.0254 0.0361  0.0570  21  ALA   A CB  
592  C  CB  B ALA   A 21  ? 0.1924 0.2013 0.2595 0.0067  0.0145  0.0315  21  ALA   A CB  
603  N  N   A ASP   A 22  ? 0.1958 0.1675 0.2217 0.0001  0.0417  0.0147  22  ASP   A N   
604  N  N   B ASP   A 22  ? 0.1642 0.1671 0.2122 -0.0135 0.0638  0.0104  22  ASP   A N   
605  C  CA  A ASP   A 22  ? 0.1947 0.1569 0.2222 0.0107  0.0396  0.0274  22  ASP   A CA  
606  C  CA  B ASP   A 22  ? 0.1708 0.1621 0.2084 -0.0128 0.0600  -0.0038 22  ASP   A CA  
607  C  C   A ASP   A 22  ? 0.1858 0.1602 0.2009 0.0051  0.0368  0.0371  22  ASP   A C   
608  C  C   B ASP   A 22  ? 0.1631 0.1623 0.1677 -0.0236 0.0692  -0.0005 22  ASP   A C   
609  O  O   A ASP   A 22  ? 0.1963 0.1660 0.2125 0.0016  0.0388  0.0391  22  ASP   A O   
610  O  O   B ASP   A 22  ? 0.1710 0.1714 0.1754 -0.0341 0.0718  -0.0043 22  ASP   A O   
611  C  CB  A ASP   A 22  ? 0.2138 0.1569 0.2344 0.0192  0.0373  0.0131  22  ASP   A CB  
612  C  CB  B ASP   A 22  ? 0.1962 0.1627 0.2341 -0.0010 0.0614  -0.0190 22  ASP   A CB  
613  C  CG  A ASP   A 22  ? 0.2202 0.1524 0.2541 0.0149  0.0269  0.0173  22  ASP   A CG  
614  C  CG  B ASP   A 22  ? 0.2125 0.1590 0.2658 0.0093  0.0643  -0.0116 22  ASP   A CG  
615  O  OD1 A ASP   A 22  ? 0.2193 0.1422 0.2556 -0.0080 0.0129  0.0290  22  ASP   A OD1 
616  O  OD1 B ASP   A 22  ? 0.2118 0.1503 0.2486 -0.0065 0.0615  -0.0061 22  ASP   A OD1 
617  O  OD2 A ASP   A 22  ? 0.2281 0.1622 0.2773 0.0317  0.0391  0.0038  22  ASP   A OD2 
618  O  OD2 B ASP   A 22  ? 0.2355 0.1756 0.3117 0.0181  0.0618  -0.0033 22  ASP   A OD2 
627  N  N   A ILE   A 23  ? 0.1854 0.1654 0.1947 0.0035  0.0350  0.0359  23  ILE   A N   
628  N  N   B ILE   A 23  ? 0.1606 0.1567 0.1587 -0.0189 0.0548  0.0040  23  ILE   A N   
629  C  CA  A ILE   A 23  ? 0.1814 0.1629 0.1808 -0.0000 0.0364  0.0279  23  ILE   A CA  
630  C  CA  B ILE   A 23  ? 0.1542 0.1621 0.1563 -0.0239 0.0372  0.0149  23  ILE   A CA  
631  C  C   A ILE   A 23  ? 0.1801 0.1812 0.1796 0.0013  0.0520  0.0200  23  ILE   A C   
632  C  C   B ILE   A 23  ? 0.1595 0.1730 0.1635 -0.0314 0.0412  0.0112  23  ILE   A C   
633  O  O   A ILE   A 23  ? 0.1877 0.1986 0.1938 -0.0020 0.0403  0.0184  23  ILE   A O   
634  O  O   B ILE   A 23  ? 0.1652 0.1745 0.1745 -0.0264 0.0289  0.0164  23  ILE   A O   
635  C  CB  A ILE   A 23  ? 0.1872 0.1612 0.1651 -0.0005 0.0287  0.0171  23  ILE   A CB  
636  C  CB  B ILE   A 23  ? 0.1567 0.1592 0.1560 -0.0053 0.0241  0.0297  23  ILE   A CB  
637  C  CG1 A ILE   A 23  ? 0.1914 0.1622 0.1631 0.0007  0.0331  0.0097  23  ILE   A CG1 
638  C  CG1 B ILE   A 23  ? 0.1590 0.1580 0.1509 -0.0011 0.0151  0.0226  23  ILE   A CG1 
639  C  CG2 A ILE   A 23  ? 0.1848 0.1645 0.1694 0.0001  0.0375  0.0230  23  ILE   A CG2 
640  C  CG2 B ILE   A 23  ? 0.1575 0.1622 0.1589 0.0120  0.0208  0.0324  23  ILE   A CG2 
641  C  CD1 A ILE   A 23  ? 0.1961 0.1729 0.1853 0.0016  0.0206  -0.0013 23  ILE   A CD1 
642  C  CD1 B ILE   A 23  ? 0.1590 0.1588 0.1633 0.0013  0.0013  0.0142  23  ILE   A CD1 
665  N  N   A VAL   A 24  ? 0.1862 0.1853 0.1859 -0.0093 0.0415  0.0094  24  VAL   A N   
666  N  N   B VAL   A 24  ? 0.1720 0.1849 0.1722 -0.0414 0.0369  -0.0043 24  VAL   A N   
667  C  CA  A VAL   A 24  ? 0.1938 0.1932 0.1973 -0.0156 0.0316  0.0022  24  VAL   A CA  
668  C  CA  B VAL   A 24  ? 0.1859 0.1959 0.2007 -0.0443 0.0337  -0.0017 24  VAL   A CA  
669  C  C   A VAL   A 24  ? 0.2038 0.2075 0.1973 -0.0155 0.0304  0.0007  24  VAL   A C   
670  C  C   B VAL   A 24  ? 0.1958 0.2124 0.1987 -0.0382 0.0447  -0.0071 24  VAL   A C   
671  O  O   A VAL   A 24  ? 0.2154 0.2131 0.1998 -0.0164 0.0344  -0.0021 24  VAL   A O   
672  O  O   B VAL   A 24  ? 0.2087 0.2209 0.2096 -0.0309 0.0475  -0.0047 24  VAL   A O   
673  C  CB  A VAL   A 24  ? 0.1964 0.1876 0.2110 -0.0230 0.0322  0.0054  24  VAL   A CB  
674  C  CB  B VAL   A 24  ? 0.1915 0.1977 0.2411 -0.0542 0.0253  0.0147  24  VAL   A CB  
675  C  CG1 A VAL   A 24  ? 0.2044 0.1960 0.2207 -0.0096 0.0290  -0.0094 24  VAL   A CG1 
676  C  CG1 B VAL   A 24  ? 0.2064 0.2051 0.2684 -0.0426 0.0108  0.0103  24  VAL   A CG1 
677  C  CG2 A VAL   A 24  ? 0.2035 0.1880 0.2072 -0.0264 0.0388  0.0187  24  VAL   A CG2 
678  C  CG2 B VAL   A 24  ? 0.1948 0.1968 0.2456 -0.0620 0.0255  0.0173  24  VAL   A CG2 
697  N  N   A GLU   A 25  ? 0.2078 0.2236 0.1971 -0.0178 0.0452  -0.0078 25  GLU   A N   
698  N  N   B GLU   A 25  ? 0.1962 0.2290 0.1947 -0.0387 0.0731  -0.0122 25  GLU   A N   
699  C  CA  A GLU   A 25  ? 0.2221 0.2469 0.2170 -0.0066 0.0467  -0.0023 25  GLU   A CA  
700  C  CA  B GLU   A 25  ? 0.2001 0.2491 0.1953 -0.0426 0.0820  -0.0150 25  GLU   A CA  
701  C  C   A GLU   A 25  ? 0.2117 0.2464 0.1728 -0.0196 0.0485  0.0059  25  GLU   A C   
702  C  C   B GLU   A 25  ? 0.1968 0.2574 0.1699 -0.0442 0.0719  -0.0097 25  GLU   A C   
703  O  O   A GLU   A 25  ? 0.2174 0.2592 0.1742 -0.0206 0.0483  -0.0043 25  GLU   A O   
704  O  O   B GLU   A 25  ? 0.2091 0.2670 0.1832 -0.0459 0.0678  -0.0164 25  GLU   A O   
705  C  CB  A GLU   A 25  ? 0.2472 0.2708 0.2724 0.0029  0.0468  0.0054  25  GLU   A CB  
706  C  CB  B GLU   A 25  ? 0.2140 0.2632 0.2275 -0.0431 0.0954  -0.0129 25  GLU   A CB  
707  C  CG  A GLU   A 25  ? 0.2815 0.2943 0.3436 0.0029  0.0403  0.0031  25  GLU   A CG  
708  C  CG  B GLU   A 25  ? 0.2487 0.2783 0.2938 -0.0465 0.0803  -0.0124 25  GLU   A CG  
709  C  CD  A GLU   A 25  ? 0.3106 0.3142 0.4021 0.0004  0.0322  -0.0037 25  GLU   A CD  
710  C  CD  B GLU   A 25  ? 0.2773 0.2913 0.3555 -0.0516 0.0622  -0.0162 25  GLU   A CD  
711  O  OE1 A GLU   A 25  ? 0.3231 0.3194 0.4229 0.0038  0.0241  -0.0207 25  GLU   A OE1 
712  O  OE1 B GLU   A 25  ? 0.2908 0.2974 0.3869 -0.0498 0.0564  -0.0210 25  GLU   A OE1 
713  O  OE2 A GLU   A 25  ? 0.3206 0.3266 0.4332 -0.0045 0.0207  -0.0119 25  GLU   A OE2 
714  O  OE2 B GLU   A 25  ? 0.2879 0.2930 0.3819 -0.0566 0.0556  -0.0206 25  GLU   A OE2 
727  N  N   A GLU   A 26  ? 0.2012 0.2346 0.1788 -0.0346 0.0505  0.0035  26  GLU   A N   
728  N  N   B GLU   A 26  ? 0.1874 0.2535 0.1729 -0.0475 0.0641  -0.0056 26  GLU   A N   
729  C  CA  A GLU   A 26  ? 0.2122 0.2285 0.1707 -0.0469 0.0535  0.0051  26  GLU   A CA  
730  C  CA  B GLU   A 26  ? 0.1975 0.2531 0.1708 -0.0497 0.0529  0.0027  26  GLU   A CA  
731  C  C   A GLU   A 26  ? 0.2038 0.2226 0.1550 -0.0410 0.0411  0.0046  26  GLU   A C   
732  C  C   B GLU   A 26  ? 0.1978 0.2377 0.1620 -0.0465 0.0435  -0.0028 26  GLU   A C   
733  O  O   A GLU   A 26  ? 0.2094 0.2130 0.1574 -0.0435 0.0352  0.0081  26  GLU   A O   
734  O  O   B GLU   A 26  ? 0.2037 0.2343 0.1648 -0.0481 0.0506  -0.0072 26  GLU   A O   
735  C  CB  A GLU   A 26  ? 0.2333 0.2290 0.1994 -0.0628 0.0528  0.0113  26  GLU   A CB  
736  C  CB  B GLU   A 26  ? 0.2036 0.2645 0.1847 -0.0550 0.0296  0.0106  26  GLU   A CB  
737  C  CG  A GLU   A 26  ? 0.2542 0.2426 0.2694 -0.0661 0.0583  -0.0092 26  GLU   A CG  
738  C  CG  B GLU   A 26  ? 0.2131 0.2802 0.2159 -0.0504 0.0183  0.0082  26  GLU   A CG  
739  C  CD  A GLU   A 26  ? 0.2623 0.2526 0.3008 -0.0717 0.0868  -0.0198 26  GLU   A CD  
740  C  CD  B GLU   A 26  ? 0.2110 0.2922 0.2275 -0.0472 0.0252  0.0169  26  GLU   A CD  
741  O  OE1 A GLU   A 26  ? 0.2537 0.2697 0.2938 -0.0623 0.1221  -0.0628 26  GLU   A OE1 
742  O  OE1 B GLU   A 26  ? 0.2236 0.3060 0.2230 -0.0383 0.0457  0.0246  26  GLU   A OE1 
743  O  OE2 A GLU   A 26  ? 0.2754 0.2525 0.3032 -0.0748 0.0871  -0.0023 26  GLU   A OE2 
744  O  OE2 B GLU   A 26  ? 0.1997 0.2930 0.2066 -0.0499 0.0309  0.0161  26  GLU   A OE2 
757  N  N   . ALA   A 27  ? 0.1855 0.2232 0.1595 -0.0412 0.0381  0.0040  27  ALA   A N   
758  C  CA  . ALA   A 27  ? 0.1869 0.2317 0.1606 -0.0351 0.0321  0.0097  27  ALA   A CA  
759  C  C   . ALA   A 27  ? 0.2158 0.2572 0.1779 -0.0462 0.0374  -0.0092 27  ALA   A C   
760  O  O   . ALA   A 27  ? 0.2181 0.2558 0.1795 -0.0514 0.0273  0.0001  27  ALA   A O   
761  C  CB  . ALA   A 27  ? 0.1748 0.2230 0.1772 -0.0313 0.0304  0.0116  27  ALA   A CB  
768  N  N   A LYS   A 28  ? 0.2447 0.2798 0.1942 -0.0445 0.0313  -0.0334 28  LYS   A N   
769  N  N   B LYS   A 28  ? 0.2379 0.2719 0.1908 -0.0432 0.0287  -0.0325 28  LYS   A N   
770  C  CA  A LYS   A 28  ? 0.2788 0.3142 0.2250 -0.0332 0.0330  -0.0522 28  LYS   A CA  
771  C  CA  B LYS   A 28  ? 0.2640 0.2971 0.2165 -0.0309 0.0247  -0.0509 28  LYS   A CA  
772  C  C   A LYS   A 28  ? 0.3019 0.3447 0.2193 -0.0378 0.0464  -0.0443 28  LYS   A C   
773  C  C   B LYS   A 28  ? 0.2862 0.3199 0.2212 -0.0264 0.0262  -0.0457 28  LYS   A C   
774  O  O   A LYS   A 28  ? 0.3125 0.3514 0.2413 -0.0340 0.0258  -0.0522 28  LYS   A O   
775  O  O   B LYS   A 28  ? 0.2956 0.3255 0.2376 -0.0246 0.0098  -0.0530 28  LYS   A O   
776  C  CB  A LYS   A 28  ? 0.2953 0.3248 0.2741 -0.0155 0.0273  -0.0580 28  LYS   A CB  
777  C  CB  B LYS   A 28  ? 0.2738 0.3059 0.2473 -0.0220 0.0249  -0.0559 28  LYS   A CB  
778  C  CG  A LYS   A 28  ? 0.3062 0.3324 0.3062 -0.0057 0.0268  -0.0584 28  LYS   A CG  
779  C  CG  B LYS   A 28  ? 0.2802 0.3137 0.2694 -0.0191 0.0272  -0.0608 28  LYS   A CG  
780  C  CD  A LYS   A 28  ? 0.3124 0.3443 0.3451 -0.0015 0.0263  -0.0577 28  LYS   A CD  
781  C  CD  B LYS   A 28  ? 0.2908 0.3259 0.3084 -0.0186 0.0302  -0.0640 28  LYS   A CD  
782  C  CE  A LYS   A 28  ? 0.3164 0.3502 0.3708 -0.0026 0.0303  -0.0566 28  LYS   A CE  
783  C  CE  B LYS   A 28  ? 0.3006 0.3345 0.3393 -0.0212 0.0307  -0.0618 28  LYS   A CE  
784  N  NZ  A LYS   A 28  ? 0.3222 0.3521 0.3844 -0.0018 0.0351  -0.0531 28  LYS   A NZ  
785  N  NZ  B LYS   A 28  ? 0.3068 0.3394 0.3602 -0.0218 0.0294  -0.0572 28  LYS   A NZ  
812  N  N   A LYS   A 29  ? 0.3093 0.3677 0.1995 -0.0504 0.0838  -0.0208 29  LYS   A N   
813  N  N   B LYS   A 29  ? 0.2939 0.3370 0.2138 -0.0261 0.0473  -0.0257 29  LYS   A N   
814  C  CA  A LYS   A 29  ? 0.3240 0.3897 0.2112 -0.0583 0.1034  -0.0045 29  LYS   A CA  
815  C  CA  B LYS   A 29  ? 0.3030 0.3541 0.2261 -0.0247 0.0565  -0.0073 29  LYS   A CA  
816  C  C   A LYS   A 29  ? 0.3253 0.3844 0.1977 -0.0724 0.0888  0.0107  29  LYS   A C   
817  C  C   B LYS   A 29  ? 0.3000 0.3487 0.1999 -0.0298 0.0477  0.0126  29  LYS   A C   
818  O  O   A LYS   A 29  ? 0.3320 0.3959 0.2165 -0.0676 0.0868  0.0063  29  LYS   A O   
819  O  O   B LYS   A 29  ? 0.2955 0.3543 0.2000 -0.0273 0.0528  0.0158  29  LYS   A O   
820  C  CB  A LYS   A 29  ? 0.3368 0.4153 0.2630 -0.0481 0.1181  -0.0013 29  LYS   A CB  
821  C  CB  B LYS   A 29  ? 0.3176 0.3752 0.2781 -0.0164 0.0647  -0.0087 29  LYS   A CB  
822  C  CG  A LYS   A 29  ? 0.3523 0.4359 0.3242 -0.0380 0.1231  0.0014  29  LYS   A CG  
823  C  CG  B LYS   A 29  ? 0.3338 0.3924 0.3303 -0.0070 0.0704  -0.0132 29  LYS   A CG  
824  C  CD  A LYS   A 29  ? 0.3638 0.4518 0.3856 -0.0304 0.1213  -0.0023 29  LYS   A CD  
825  C  CD  B LYS   A 29  ? 0.3454 0.4061 0.3801 -0.0015 0.0704  -0.0150 29  LYS   A CD  
826  C  CE  A LYS   A 29  ? 0.3709 0.4614 0.4259 -0.0259 0.1203  -0.0020 29  LYS   A CE  
827  C  CE  B LYS   A 29  ? 0.3532 0.4171 0.4127 0.0006  0.0707  -0.0146 29  LYS   A CE  
828  N  NZ  A LYS   A 29  ? 0.3724 0.4669 0.4492 -0.0214 0.1173  -0.0036 29  LYS   A NZ  
829  N  NZ  B LYS   A 29  ? 0.3566 0.4233 0.4319 0.0015  0.0700  -0.0125 29  LYS   A NZ  
856  N  N   A VAL   A 30  ? 0.3190 0.3667 0.1863 -0.0891 0.0768  0.0213  30  VAL   A N   
857  N  N   B VAL   A 30  ? 0.3001 0.3363 0.1918 -0.0381 0.0394  0.0271  30  VAL   A N   
858  C  CA  A VAL   A 30  ? 0.3184 0.3495 0.1854 -0.1004 0.0515  0.0343  30  VAL   A CA  
859  C  CA  B VAL   A 30  ? 0.2997 0.3236 0.1944 -0.0446 0.0181  0.0408  30  VAL   A CA  
860  C  C   A VAL   A 30  ? 0.3196 0.3303 0.1447 -0.0982 0.0382  0.0412  30  VAL   A C   
861  C  C   B VAL   A 30  ? 0.3005 0.3154 0.1779 -0.0431 0.0061  0.0407  30  VAL   A C   
862  O  O   A VAL   A 30  ? 0.3281 0.3331 0.1710 -0.0965 0.0295  0.0424  30  VAL   A O   
863  O  O   B VAL   A 30  ? 0.3024 0.3149 0.1887 -0.0442 -0.0022 0.0465  30  VAL   A O   
864  C  CB  A VAL   A 30  ? 0.3190 0.3489 0.2255 -0.1106 0.0395  0.0369  30  VAL   A CB  
865  C  CB  B VAL   A 30  ? 0.3007 0.3180 0.2191 -0.0505 0.0100  0.0459  30  VAL   A CB  
866  C  CG1 A VAL   A 30  ? 0.3258 0.3526 0.2473 -0.1089 0.0260  0.0338  30  VAL   A CG1 
867  C  CG1 B VAL   A 30  ? 0.3057 0.3187 0.2354 -0.0498 0.0031  0.0436  30  VAL   A CG1 
868  C  CG2 A VAL   A 30  ? 0.3165 0.3473 0.2492 -0.1170 0.0437  0.0380  30  VAL   A CG2 
869  C  CG2 B VAL   A 30  ? 0.2986 0.3146 0.2352 -0.0537 0.0119  0.0510  30  VAL   A CG2 
888  N  N   A LYS   A 31  ? 0.3104 0.3084 0.1366 -0.0951 0.0252  0.0350  31  LYS   A N   
889  N  N   B LYS   A 31  ? 0.2998 0.3075 0.1883 -0.0386 -0.0039 0.0357  31  LYS   A N   
890  C  CA  A LYS   A 31  ? 0.3162 0.3024 0.1421 -0.0815 0.0023  0.0315  31  LYS   A CA  
891  C  CA  B LYS   A 31  ? 0.3013 0.3042 0.2035 -0.0300 -0.0143 0.0296  31  LYS   A CA  
892  C  C   A LYS   A 31  ? 0.2896 0.2712 0.1068 -0.0638 -0.0051 0.0567  31  LYS   A C   
893  C  C   B LYS   A 31  ? 0.2756 0.2861 0.1773 -0.0192 -0.0084 0.0461  31  LYS   A C   
894  O  O   A LYS   A 31  ? 0.2979 0.2795 0.1200 -0.0598 -0.0226 0.0728  31  LYS   A O   
895  O  O   B LYS   A 31  ? 0.2823 0.2925 0.1973 -0.0149 -0.0178 0.0494  31  LYS   A O   
896  C  CB  A LYS   A 31  ? 0.3439 0.3272 0.2532 -0.0708 -0.0172 0.0102  31  LYS   A CB  
897  C  CB  B LYS   A 31  ? 0.3274 0.3234 0.2770 -0.0298 -0.0301 0.0122  31  LYS   A CB  
898  C  CG  A LYS   A 31  ? 0.3735 0.3506 0.3716 -0.0581 -0.0328 -0.0032 31  LYS   A CG  
899  C  CG  B LYS   A 31  ? 0.3534 0.3439 0.3649 -0.0278 -0.0410 -0.0019 31  LYS   A CG  
900  C  CD  A LYS   A 31  ? 0.3988 0.3697 0.4592 -0.0479 -0.0469 -0.0156 31  LYS   A CD  
901  C  CD  B LYS   A 31  ? 0.3731 0.3601 0.4335 -0.0255 -0.0547 -0.0171 31  LYS   A CD  
902  C  CE  A LYS   A 31  ? 0.4150 0.3812 0.5192 -0.0401 -0.0596 -0.0254 31  LYS   A CE  
903  C  CE  B LYS   A 31  ? 0.3876 0.3734 0.4845 -0.0259 -0.0644 -0.0280 31  LYS   A CE  
904  N  NZ  A LYS   A 31  ? 0.4237 0.3885 0.5472 -0.0349 -0.0668 -0.0295 31  LYS   A NZ  
905  N  NZ  B LYS   A 31  ? 0.3983 0.3806 0.5106 -0.0263 -0.0680 -0.0355 31  LYS   A NZ  
932  N  N   A PRO   A 32  ? 0.2653 0.2477 0.0992 -0.0737 -0.0000 0.0372  32  PRO   A N   
933  N  N   B PRO   A 32  ? 0.2426 0.2626 0.1507 -0.0162 0.0117  0.0393  32  PRO   A N   
934  C  CA  A PRO   A 32  ? 0.2547 0.2327 0.1459 -0.0726 -0.0121 0.0415  32  PRO   A CA  
935  C  CA  B PRO   A 32  ? 0.2313 0.2488 0.1559 -0.0122 0.0074  0.0465  32  PRO   A CA  
936  C  C   A PRO   A 32  ? 0.2487 0.2275 0.1550 -0.0622 -0.0095 0.0398  32  PRO   A C   
937  C  C   B PRO   A 32  ? 0.2226 0.2398 0.1521 -0.0051 -0.0014 0.0525  32  PRO   A C   
938  O  O   A PRO   A 32  ? 0.2445 0.2200 0.1508 -0.0680 -0.0146 0.0289  32  PRO   A O   
939  O  O   B PRO   A 32  ? 0.2149 0.2361 0.1711 -0.0000 -0.0113 0.0464  32  PRO   A O   
940  C  CB  A PRO   A 32  ? 0.2511 0.2355 0.1518 -0.0745 -0.0190 0.0275  32  PRO   A CB  
941  C  CB  B PRO   A 32  ? 0.2259 0.2510 0.1574 -0.0122 0.0105  0.0277  32  PRO   A CB  
942  C  CG  A PRO   A 32  ? 0.2511 0.2400 0.1136 -0.0687 -0.0289 0.0168  32  PRO   A CG  
943  C  CG  B PRO   A 32  ? 0.2276 0.2566 0.1407 -0.0103 0.0097  0.0181  32  PRO   A CG  
944  C  CD  A PRO   A 32  ? 0.2525 0.2406 0.0950 -0.0703 -0.0104 0.0290  32  PRO   A CD  
945  C  CD  B PRO   A 32  ? 0.2304 0.2595 0.1360 -0.0114 0.0176  0.0253  32  PRO   A CD  
960  N  N   A THR   A 33  ? 0.2497 0.2283 0.1586 -0.0510 -0.0079 0.0467  33  THR   A N   
961  N  N   B THR   A 33  ? 0.2235 0.2343 0.1494 -0.0040 -0.0092 0.0626  33  THR   A N   
962  C  CA  A THR   A 33  ? 0.2476 0.2326 0.1699 -0.0366 -0.0258 0.0492  33  THR   A CA  
963  C  CA  B THR   A 33  ? 0.2241 0.2267 0.1432 -0.0018 -0.0332 0.0693  33  THR   A CA  
964  C  C   A THR   A 33  ? 0.2179 0.2202 0.1570 -0.0313 -0.0325 0.0489  33  THR   A C   
965  C  C   B THR   A 33  ? 0.2048 0.2085 0.1382 -0.0155 -0.0328 0.0528  33  THR   A C   
966  O  O   A THR   A 33  ? 0.2120 0.2123 0.1694 -0.0287 -0.0404 0.0531  33  THR   A O   
967  O  O   B THR   A 33  ? 0.1998 0.1925 0.1597 -0.0162 -0.0319 0.0387  33  THR   A O   
968  C  CB  A THR   A 33  ? 0.2750 0.2534 0.1964 -0.0268 -0.0292 0.0560  33  THR   A CB  
969  C  CB  B THR   A 33  ? 0.2476 0.2411 0.1587 0.0080  -0.0346 0.0900  33  THR   A CB  
970  O  OG1 A THR   A 33  ? 0.2966 0.2683 0.2299 -0.0159 -0.0195 0.0586  33  THR   A OG1 
971  O  OG1 B THR   A 33  ? 0.2660 0.2581 0.1778 0.0133  -0.0341 0.0979  33  THR   A OG1 
972  C  CG2 A THR   A 33  ? 0.2798 0.2599 0.2104 -0.0201 -0.0345 0.0574  33  THR   A CG2 
973  C  CG2 B THR   A 33  ? 0.2498 0.2451 0.1854 0.0113  -0.0324 0.0843  33  THR   A CG2 
988  N  N   . VAL   A 34  ? 0.1932 0.2088 0.1304 -0.0286 -0.0235 0.0452  34  VAL   A N   
989  C  CA  . VAL   A 34  ? 0.1786 0.1904 0.1327 -0.0230 -0.0151 0.0399  34  VAL   A CA  
990  C  C   . VAL   A 34  ? 0.1726 0.1790 0.1349 -0.0305 -0.0102 0.0423  34  VAL   A C   
991  O  O   . VAL   A 34  ? 0.1728 0.1800 0.1578 -0.0402 -0.0073 0.0376  34  VAL   A O   
992  C  CB  . VAL   A 34  ? 0.1772 0.1886 0.1486 -0.0241 -0.0013 0.0294  34  VAL   A CB  
993  C  CG1 . VAL   A 34  ? 0.1874 0.1915 0.1592 -0.0215 0.0044  0.0152  34  VAL   A CG1 
994  C  CG2 . VAL   A 34  ? 0.1829 0.2069 0.1770 -0.0236 -0.0038 0.0213  34  VAL   A CG2 
1005 N  N   . VAL   A 35  ? 0.1595 0.1717 0.1234 -0.0300 -0.0087 0.0279  35  VAL   A N   
1006 C  CA  . VAL   A 35  ? 0.1526 0.1672 0.1277 -0.0239 -0.0037 0.0238  35  VAL   A CA  
1007 C  C   . VAL   A 35  ? 0.1459 0.1525 0.1199 -0.0155 0.0005  0.0196  35  VAL   A C   
1008 O  O   . VAL   A 35  ? 0.1374 0.1615 0.1449 -0.0235 0.0098  0.0141  35  VAL   A O   
1009 C  CB  . VAL   A 35  ? 0.1578 0.1685 0.1470 -0.0101 0.0093  0.0146  35  VAL   A CB  
1010 C  CG1 . VAL   A 35  ? 0.1639 0.1641 0.1702 -0.0078 0.0068  0.0080  35  VAL   A CG1 
1011 C  CG2 . VAL   A 35  ? 0.1558 0.1741 0.1649 0.0007  0.0202  0.0000  35  VAL   A CG2 
1021 N  N   . VAL   A 36  ? 0.1354 0.1462 0.1116 -0.0129 0.0018  0.0277  36  VAL   A N   
1022 C  CA  . VAL   A 36  ? 0.1304 0.1351 0.1244 -0.0059 0.0031  0.0140  36  VAL   A CA  
1023 C  C   . VAL   A 36  ? 0.1294 0.1392 0.1305 -0.0120 0.0122  0.0186  36  VAL   A C   
1024 O  O   . VAL   A 36  ? 0.1347 0.1395 0.1465 -0.0103 0.0169  0.0150  36  VAL   A O   
1025 C  CB  . VAL   A 36  ? 0.1316 0.1306 0.1312 -0.0101 0.0052  0.0173  36  VAL   A CB  
1026 C  CG1 . VAL   A 36  ? 0.1345 0.1413 0.1442 -0.0131 0.0099  0.0044  36  VAL   A CG1 
1027 C  CG2 . VAL   A 36  ? 0.1440 0.1436 0.1424 -0.0063 -0.0025 0.0339  36  VAL   A CG2 
1037 N  N   . ASN   A 37  ? 0.1294 0.1307 0.1109 -0.0040 0.0020  0.0170  37  ASN   A N   
1038 C  CA  . ASN   A 37  ? 0.1235 0.1280 0.1187 0.0005  0.0040  0.0243  37  ASN   A CA  
1039 C  C   . ASN   A 37  ? 0.1177 0.1267 0.1208 -0.0020 0.0136  0.0318  37  ASN   A C   
1040 O  O   . ASN   A 37  ? 0.1356 0.1353 0.1181 -0.0015 0.0133  0.0125  37  ASN   A O   
1041 C  CB  . ASN   A 37  ? 0.1323 0.1313 0.1313 0.0007  0.0069  0.0174  37  ASN   A CB  
1042 C  CG  . ASN   A 37  ? 0.1286 0.1254 0.1341 0.0024  0.0089  0.0073  37  ASN   A CG  
1043 O  OD1 . ASN   A 37  ? 0.1302 0.1285 0.1581 0.0002  0.0080  0.0170  37  ASN   A OD1 
1044 N  ND2 . ASN   A 37  ? 0.1286 0.1334 0.1428 0.0010  0.0077  0.0202  37  ASN   A ND2 
1051 N  N   . ALA   A 38  ? 0.1217 0.1348 0.1312 -0.0042 0.0114  0.0125  38  ALA   A N   
1052 C  CA  . ALA   A 38  ? 0.1283 0.1444 0.1293 -0.0015 0.0026  0.0096  38  ALA   A CA  
1053 C  C   . ALA   A 38  ? 0.1252 0.1459 0.1307 0.0093  -0.0031 0.0092  38  ALA   A C   
1054 O  O   . ALA   A 38  ? 0.1312 0.1479 0.1374 0.0121  0.0000  0.0099  38  ALA   A O   
1055 C  CB  . ALA   A 38  ? 0.1339 0.1901 0.1436 -0.0218 -0.0079 0.0009  38  ALA   A CB  
1061 N  N   . ALA   A 39  ? 0.1253 0.1402 0.1423 0.0025  0.0094  0.0242  39  ALA   A N   
1062 C  CA  . ALA   A 39  ? 0.1291 0.1350 0.1323 0.0110  0.0114  0.0111  39  ALA   A CA  
1063 C  C   . ALA   A 39  ? 0.1367 0.1362 0.1264 0.0032  0.0084  0.0164  39  ALA   A C   
1064 O  O   . ALA   A 39  ? 0.1460 0.1347 0.1278 -0.0026 0.0068  0.0055  39  ALA   A O   
1065 C  CB  . ALA   A 39  ? 0.1352 0.1530 0.1432 0.0007  0.0073  0.0054  39  ALA   A CB  
1071 N  N   . ASN   A 40  ? 0.1434 0.1365 0.1415 -0.0082 0.0229  0.0134  40  ASN   A N   
1072 C  CA  . ASN   A 40  ? 0.1487 0.1308 0.1390 -0.0046 0.0184  0.0144  40  ASN   A CA  
1073 C  C   . ASN   A 40  ? 0.1497 0.1254 0.1237 -0.0041 0.0285  0.0281  40  ASN   A C   
1074 O  O   . ASN   A 40  ? 0.1454 0.1324 0.1321 -0.0007 0.0206  0.0227  40  ASN   A O   
1075 C  CB  . ASN   A 40  ? 0.1541 0.1421 0.1586 0.0012  0.0153  0.0075  40  ASN   A CB  
1076 C  CG  . ASN   A 40  ? 0.1601 0.1418 0.1765 0.0032  0.0149  0.0218  40  ASN   A CG  
1077 O  OD1 . ASN   A 40  ? 0.1662 0.1362 0.1912 -0.0046 0.0181  0.0119  40  ASN   A OD1 
1078 N  ND2 . ASN   A 40  ? 0.1668 0.1580 0.1920 0.0083  -0.0022 -0.0078 40  ASN   A ND2 
1085 N  N   . VAL   A 41  ? 0.1561 0.1300 0.1362 -0.0022 0.0222  0.0198  41  VAL   A N   
1086 C  CA  . VAL   A 41  ? 0.1606 0.1325 0.1582 0.0033  0.0374  0.0156  41  VAL   A CA  
1087 C  C   . VAL   A 41  ? 0.1590 0.1347 0.1535 0.0079  0.0340  0.0209  41  VAL   A C   
1088 O  O   . VAL   A 41  ? 0.1604 0.1282 0.1693 0.0048  0.0284  0.0141  41  VAL   A O   
1089 C  CB  . VAL   A 41  ? 0.1772 0.1452 0.1694 -0.0077 0.0504  -0.0006 41  VAL   A CB  
1090 C  CG1 . VAL   A 41  ? 0.1895 0.1488 0.1807 -0.0020 0.0530  -0.0153 41  VAL   A CG1 
1091 C  CG2 . VAL   A 41  ? 0.2009 0.1606 0.1572 -0.0093 0.0497  0.0028  41  VAL   A CG2 
1101 N  N   . TYR   A 42  ? 0.1393 0.1282 0.1722 0.0016  0.0350  0.0250  42  TYR   A N   
1102 C  CA  . TYR   A 42  ? 0.1410 0.1266 0.1704 -0.0045 0.0317  0.0274  42  TYR   A CA  
1103 C  C   . TYR   A 42  ? 0.1360 0.1282 0.1532 -0.0011 0.0307  0.0325  42  TYR   A C   
1104 O  O   . TYR   A 42  ? 0.1400 0.1320 0.1759 -0.0198 0.0239  0.0052  42  TYR   A O   
1105 C  CB  . TYR   A 42  ? 0.1623 0.1415 0.1558 0.0008  0.0401  0.0384  42  TYR   A CB  
1106 C  CG  . TYR   A 42  ? 0.1815 0.1451 0.1611 -0.0004 0.0320  0.0355  42  TYR   A CG  
1107 C  CD1 . TYR   A 42  ? 0.1901 0.1572 0.1629 -0.0086 0.0415  0.0425  42  TYR   A CD1 
1108 C  CD2 . TYR   A 42  ? 0.2049 0.1660 0.1716 -0.0007 0.0286  0.0332  42  TYR   A CD2 
1109 C  CE1 . TYR   A 42  ? 0.1993 0.1679 0.1655 -0.0060 0.0462  0.0418  42  TYR   A CE1 
1110 C  CE2 . TYR   A 42  ? 0.2183 0.1845 0.1852 -0.0129 0.0335  0.0405  42  TYR   A CE2 
1111 C  CZ  . TYR   A 42  ? 0.2271 0.1863 0.1706 -0.0148 0.0545  0.0447  42  TYR   A CZ  
1112 O  OH  . TYR   A 42  ? 0.2483 0.1986 0.1966 -0.0271 0.0520  0.0248  42  TYR   A OH  
1122 N  N   . LEU   A 43  ? 0.1363 0.1341 0.1440 -0.0045 0.0144  0.0131  43  LEU   A N   
1123 C  CA  . LEU   A 43  ? 0.1326 0.1287 0.1386 -0.0053 0.0106  0.0122  43  LEU   A CA  
1124 C  C   . LEU   A 43  ? 0.1325 0.1326 0.1456 -0.0013 0.0145  0.0120  43  LEU   A C   
1125 O  O   . LEU   A 43  ? 0.1501 0.1352 0.1644 0.0021  0.0030  0.0041  43  LEU   A O   
1126 C  CB  . LEU   A 43  ? 0.1392 0.1251 0.1645 -0.0040 0.0113  0.0073  43  LEU   A CB  
1127 C  CG  . LEU   A 43  ? 0.1453 0.1307 0.1715 -0.0024 0.0051  0.0126  43  LEU   A CG  
1128 C  CD1 . LEU   A 43  ? 0.1480 0.1333 0.1915 -0.0033 -0.0028 0.0156  43  LEU   A CD1 
1129 C  CD2 . LEU   A 43  ? 0.1536 0.1342 0.1660 -0.0074 0.0101  0.0245  43  LEU   A CD2 
1141 N  N   A LYS   A 44  ? 0.1421 0.1285 0.1437 -0.0031 0.0092  0.0124  44  LYS   A N   
1142 N  N   B LYS   A 44  ? 0.1406 0.1369 0.1474 0.0006  0.0096  0.0071  44  LYS   A N   
1143 C  CA  A LYS   A 44  ? 0.1545 0.1297 0.1461 -0.0036 0.0188  0.0273  44  LYS   A CA  
1144 C  CA  B LYS   A 44  ? 0.1504 0.1446 0.1561 0.0022  0.0148  0.0119  44  LYS   A CA  
1145 C  C   A LYS   A 44  ? 0.1398 0.1331 0.1460 0.0044  0.0059  0.0109  44  LYS   A C   
1146 C  C   B LYS   A 44  ? 0.1379 0.1395 0.1505 0.0056  0.0063  0.0073  44  LYS   A C   
1147 O  O   A LYS   A 44  ? 0.1484 0.1473 0.1508 -0.0026 0.0056  -0.0000 44  LYS   A O   
1148 O  O   B LYS   A 44  ? 0.1428 0.1490 0.1523 -0.0015 0.0086  0.0019  44  LYS   A O   
1149 C  CB  A LYS   A 44  ? 0.1897 0.1401 0.1817 -0.0080 0.0308  0.0490  44  LYS   A CB  
1150 C  CB  B LYS   A 44  ? 0.1794 0.1636 0.1941 0.0034  0.0201  0.0157  44  LYS   A CB  
1151 C  CG  A LYS   A 44  ? 0.2209 0.1652 0.2357 -0.0220 0.0570  0.0643  44  LYS   A CG  
1152 C  CG  B LYS   A 44  ? 0.2045 0.1884 0.2413 0.0020  0.0355  0.0182  44  LYS   A CG  
1153 C  CD  A LYS   A 44  ? 0.2571 0.2168 0.3266 -0.0271 0.0414  0.0512  44  LYS   A CD  
1154 C  CD  B LYS   A 44  ? 0.2326 0.2269 0.3058 -0.0052 0.0278  0.0193  44  LYS   A CD  
1155 C  CE  A LYS   A 44  ? 0.2758 0.2520 0.3809 -0.0312 0.0343  0.0455  44  LYS   A CE  
1156 C  CE  B LYS   A 44  ? 0.2431 0.2438 0.3391 -0.0072 0.0245  0.0178  44  LYS   A CE  
1157 N  NZ  A LYS   A 44  ? 0.2837 0.2714 0.4089 -0.0339 0.0343  0.0502  44  LYS   A NZ  
1158 N  NZ  B LYS   A 44  ? 0.2424 0.2499 0.3521 -0.0020 0.0257  0.0211  44  LYS   A NZ  
1185 N  N   . HIS   A 45  ? 0.1320 0.1296 0.1491 0.0055  0.0035  0.0145  45  HIS   A N   
1186 C  CA  . HIS   A 45  ? 0.1257 0.1299 0.1486 0.0009  0.0023  0.0156  45  HIS   A CA  
1187 C  C   . HIS   A 45  ? 0.1390 0.1469 0.1492 0.0070  0.0079  0.0224  45  HIS   A C   
1188 O  O   . HIS   A 45  ? 0.1636 0.1614 0.1778 0.0262  0.0067  0.0034  45  HIS   A O   
1189 C  CB  . HIS   A 45  ? 0.1292 0.1279 0.1526 -0.0044 0.0017  0.0116  45  HIS   A CB  
1190 C  CG  . HIS   A 45  ? 0.1268 0.1249 0.1326 -0.0073 0.0069  0.0186  45  HIS   A CG  
1191 N  ND1 . HIS   A 45  ? 0.1208 0.1337 0.1505 -0.0046 0.0025  0.0213  45  HIS   A ND1 
1192 C  CD2 . HIS   A 45  ? 0.1268 0.1306 0.1549 -0.0076 -0.0019 0.0215  45  HIS   A CD2 
1193 C  CE1 . HIS   A 45  ? 0.1211 0.1368 0.1408 -0.0050 -0.0055 0.0247  45  HIS   A CE1 
1194 N  NE2 . HIS   A 45  ? 0.1230 0.1398 0.1471 0.0012  0.0012  0.0260  45  HIS   A NE2 
1203 N  N   A GLY   A 46  ? 0.1476 0.1544 0.1738 0.0245  0.0011  0.0423  46  GLY   A N   
1204 N  N   B GLY   A 46  ? 0.1505 0.1519 0.1740 0.0077  -0.0049 0.0263  46  GLY   A N   
1205 C  CA  A GLY   A 46  ? 0.1469 0.1557 0.1854 0.0146  -0.0023 0.0516  46  GLY   A CA  
1206 C  CA  B GLY   A 46  ? 0.1471 0.1583 0.1815 -0.0011 -0.0114 0.0208  46  GLY   A CA  
1207 C  C   A GLY   A 46  ? 0.1528 0.1482 0.1859 0.0227  -0.0017 0.0552  46  GLY   A C   
1208 C  C   B GLY   A 46  ? 0.1440 0.1543 0.1738 -0.0020 -0.0003 0.0245  46  GLY   A C   
1209 O  O   A GLY   A 46  ? 0.1568 0.1391 0.2160 0.0172  -0.0087 0.0659  46  GLY   A O   
1210 O  O   B GLY   A 46  ? 0.1457 0.1658 0.1810 -0.0076 -0.0120 0.0178  46  GLY   A O   
1217 N  N   A GLY   A 47  ? 0.1453 0.1523 0.1734 0.0225  -0.0120 0.0336  47  GLY   A N   
1218 N  N   B GLY   A 47  ? 0.1463 0.1482 0.1604 0.0022  0.0021  0.0177  47  GLY   A N   
1219 C  CA  A GLY   A 47  ? 0.1445 0.1551 0.1727 0.0210  -0.0218 0.0251  47  GLY   A CA  
1220 C  CA  B GLY   A 47  ? 0.1406 0.1523 0.1649 0.0017  -0.0034 0.0143  47  GLY   A CA  
1221 C  C   A GLY   A 47  ? 0.1359 0.1463 0.1613 0.0167  -0.0203 0.0208  47  GLY   A C   
1222 C  C   B GLY   A 47  ? 0.1312 0.1439 0.1476 0.0048  -0.0034 0.0069  47  GLY   A C   
1223 O  O   A GLY   A 47  ? 0.1373 0.1335 0.1864 0.0171  -0.0192 0.0134  47  GLY   A O   
1224 O  O   B GLY   A 47  ? 0.1298 0.1386 0.1487 0.0101  -0.0160 0.0177  47  GLY   A O   
1231 N  N   A GLY   A 48  ? 0.1355 0.1502 0.1404 0.0181  -0.0141 0.0141  48  GLY   A N   
1232 N  N   B GLY   A 48  ? 0.1330 0.1447 0.1392 0.0052  0.0079  0.0052  48  GLY   A N   
1233 C  CA  A GLY   A 48  ? 0.1288 0.1476 0.1392 0.0118  -0.0103 0.0058  48  GLY   A CA  
1234 C  CA  B GLY   A 48  ? 0.1289 0.1290 0.1296 -0.0036 0.0029  -0.0039 48  GLY   A CA  
1235 C  C   A GLY   A 48  ? 0.1318 0.1485 0.1259 0.0043  0.0017  0.0019  48  GLY   A C   
1236 C  C   B GLY   A 48  ? 0.1327 0.1290 0.1450 -0.0069 0.0027  0.0084  48  GLY   A C   
1237 O  O   A GLY   A 48  ? 0.1455 0.1470 0.1410 0.0071  -0.0037 0.0081  48  GLY   A O   
1238 O  O   B GLY   A 48  ? 0.1425 0.1314 0.1331 -0.0033 0.0104  0.0021  48  GLY   A O   
1245 N  N   A VAL   A 49  ? 0.1296 0.1441 0.1488 0.0036  -0.0166 0.0032  49  VAL   A N   
1246 N  N   B VAL   A 49  ? 0.1279 0.1276 0.1520 -0.0044 -0.0072 0.0050  49  VAL   A N   
1247 C  CA  A VAL   A 49  ? 0.1405 0.1367 0.1579 -0.0012 -0.0064 0.0113  49  VAL   A CA  
1248 C  CA  B VAL   A 49  ? 0.1199 0.1332 0.1477 -0.0009 0.0005  0.0128  49  VAL   A CA  
1249 C  C   A VAL   A 49  ? 0.1351 0.1313 0.1445 -0.0081 -0.0062 0.0134  49  VAL   A C   
1250 C  C   B VAL   A 49  ? 0.1262 0.1294 0.1013 0.0044  0.0145  -0.0122 49  VAL   A C   
1251 O  O   A VAL   A 49  ? 0.1425 0.1307 0.1504 -0.0110 -0.0019 0.0114  49  VAL   A O   
1252 O  O   B VAL   A 49  ? 0.1352 0.1370 0.0938 0.0062  0.0268  -0.0135 49  VAL   A O   
1253 C  CB  A VAL   A 49  ? 0.1537 0.1352 0.1705 -0.0052 -0.0096 0.0058  49  VAL   A CB  
1254 C  CB  B VAL   A 49  ? 0.1129 0.1340 0.1665 0.0041  -0.0075 0.0126  49  VAL   A CB  
1255 C  CG1 A VAL   A 49  ? 0.1502 0.1291 0.1881 0.0011  0.0076  0.0056  49  VAL   A CG1 
1256 C  CG1 B VAL   A 49  ? 0.1011 0.1334 0.1642 0.0159  -0.0085 0.0215  49  VAL   A CG1 
1257 C  CG2 A VAL   A 49  ? 0.1700 0.1498 0.2130 -0.0290 -0.0127 0.0078  49  VAL   A CG2 
1258 C  CG2 B VAL   A 49  ? 0.1175 0.1407 0.1867 0.0079  -0.0001 0.0083  49  VAL   A CG2 
1277 N  N   A ALA   A 50  ? 0.1285 0.1272 0.1331 -0.0077 -0.0180 0.0207  50  ALA   A N   
1278 N  N   B ALA   A 50  ? 0.1289 0.1253 0.1052 0.0136  0.0148  -0.0096 50  ALA   A N   
1279 C  CA  A ALA   A 50  ? 0.1250 0.1259 0.1255 -0.0185 -0.0130 0.0265  50  ALA   A CA  
1280 C  CA  B ALA   A 50  ? 0.1300 0.1280 0.1098 0.0024  0.0114  -0.0072 50  ALA   A CA  
1281 C  C   A ALA   A 50  ? 0.1171 0.1274 0.1369 -0.0127 -0.0155 0.0225  50  ALA   A C   
1282 C  C   B ALA   A 50  ? 0.1265 0.1273 0.0957 0.0013  0.0131  -0.0038 50  ALA   A C   
1283 O  O   A ALA   A 50  ? 0.1201 0.1306 0.1620 -0.0048 -0.0166 0.0097  50  ALA   A O   
1284 O  O   B ALA   A 50  ? 0.1297 0.1305 0.0918 0.0002  0.0190  -0.0061 50  ALA   A O   
1285 C  CB  A ALA   A 50  ? 0.1228 0.1295 0.1289 -0.0116 -0.0161 0.0195  50  ALA   A CB  
1286 C  CB  B ALA   A 50  ? 0.1355 0.1295 0.1247 0.0102  0.0169  -0.0163 50  ALA   A CB  
1297 N  N   A GLY   A 51  ? 0.1239 0.1233 0.1363 -0.0050 -0.0154 0.0169  51  GLY   A N   
1298 N  N   B GLY   A 51  ? 0.1329 0.1299 0.1238 0.0080  0.0027  -0.0041 51  GLY   A N   
1299 C  CA  A GLY   A 51  ? 0.1311 0.1182 0.1504 0.0065  -0.0183 0.0151  51  GLY   A CA  
1300 C  CA  B GLY   A 51  ? 0.1373 0.1280 0.1373 0.0098  -0.0066 -0.0062 51  GLY   A CA  
1301 C  C   A GLY   A 51  ? 0.1192 0.1292 0.1468 0.0041  -0.0018 -0.0042 51  GLY   A C   
1302 C  C   B GLY   A 51  ? 0.1254 0.1348 0.1358 0.0046  0.0011  -0.0128 51  GLY   A C   
1303 O  O   A GLY   A 51  ? 0.1240 0.1379 0.1655 0.0004  -0.0072 -0.0062 51  GLY   A O   
1304 O  O   B GLY   A 51  ? 0.1315 0.1411 0.1440 0.0016  -0.0069 -0.0157 51  GLY   A O   
1311 N  N   . ALA   A 52  ? 0.1196 0.1406 0.1345 -0.0017 -0.0040 -0.0100 52  ALA   A N   
1312 C  CA  . ALA   A 52  ? 0.1260 0.1462 0.1571 -0.0056 -0.0024 -0.0077 52  ALA   A CA  
1313 C  C   . ALA   A 52  ? 0.1254 0.1419 0.1389 -0.0086 0.0056  -0.0055 52  ALA   A C   
1314 O  O   . ALA   A 52  ? 0.1406 0.1582 0.1508 -0.0096 0.0082  -0.0129 52  ALA   A O   
1315 C  CB  . ALA   A 52  ? 0.1317 0.1693 0.1652 -0.0112 -0.0036 -0.0035 52  ALA   A CB  
1322 N  N   A LEU   A 53  ? 0.1281 0.1347 0.1465 -0.0058 0.0038  0.0023  53  LEU   A N   
1323 N  N   B LEU   A 53  ? 0.1239 0.1377 0.1378 -0.0046 0.0027  -0.0031 53  LEU   A N   
1324 C  CA  A LEU   A 53  ? 0.1381 0.1468 0.1409 -0.0069 0.0008  0.0087  53  LEU   A CA  
1325 C  CA  B LEU   A 53  ? 0.1317 0.1479 0.1287 -0.0027 -0.0007 0.0003  53  LEU   A CA  
1326 C  C   A LEU   A 53  ? 0.1340 0.1469 0.1125 -0.0003 0.0048  0.0017  53  LEU   A C   
1327 C  C   B LEU   A 53  ? 0.1296 0.1475 0.1010 0.0102  -0.0044 0.0005  53  LEU   A C   
1328 O  O   A LEU   A 53  ? 0.1428 0.1528 0.1365 -0.0202 0.0083  0.0081  53  LEU   A O   
1329 O  O   B LEU   A 53  ? 0.1428 0.1509 0.0969 0.0130  -0.0077 0.0038  53  LEU   A O   
1330 C  CB  A LEU   A 53  ? 0.1447 0.1476 0.1451 -0.0063 0.0022  0.0198  53  LEU   A CB  
1331 C  CB  B LEU   A 53  ? 0.1375 0.1483 0.1295 -0.0059 0.0069  -0.0026 53  LEU   A CB  
1332 C  CG  A LEU   A 53  ? 0.1450 0.1506 0.1551 -0.0112 -0.0019 0.0228  53  LEU   A CG  
1333 C  CG  B LEU   A 53  ? 0.1405 0.1501 0.1318 -0.0112 0.0010  -0.0050 53  LEU   A CG  
1334 C  CD1 A LEU   A 53  ? 0.1401 0.1589 0.1522 0.0011  -0.0055 0.0179  53  LEU   A CD1 
1335 C  CD1 B LEU   A 53  ? 0.1417 0.1594 0.1282 -0.0105 0.0020  -0.0234 53  LEU   A CD1 
1336 C  CD2 A LEU   A 53  ? 0.1509 0.1624 0.1629 -0.0128 -0.0067 0.0264  53  LEU   A CD2 
1337 C  CD2 B LEU   A 53  ? 0.1374 0.1507 0.1305 -0.0121 0.0125  0.0069  53  LEU   A CD2 
1360 N  N   . ASN   A 54  ? 0.1278 0.1445 0.1145 0.0004  -0.0045 0.0023  54  ASN   A N   
1361 C  CA  . ASN   A 54  ? 0.1153 0.1394 0.1363 -0.0043 -0.0062 -0.0002 54  ASN   A CA  
1362 C  C   . ASN   A 54  ? 0.1253 0.1415 0.1373 -0.0061 -0.0057 -0.0002 54  ASN   A C   
1363 O  O   . ASN   A 54  ? 0.1291 0.1479 0.1456 -0.0061 -0.0057 -0.0105 54  ASN   A O   
1364 C  CB  . ASN   A 54  ? 0.1171 0.1401 0.1466 -0.0070 -0.0059 0.0024  54  ASN   A CB  
1365 C  CG  . ASN   A 54  ? 0.1217 0.1399 0.1539 0.0013  -0.0057 -0.0034 54  ASN   A CG  
1366 O  OD1 . ASN   A 54  ? 0.1237 0.1403 0.1436 -0.0030 -0.0086 -0.0012 54  ASN   A OD1 
1367 N  ND2 . ASN   A 54  ? 0.1311 0.1456 0.1595 -0.0091 -0.0103 0.0114  54  ASN   A ND2 
1375 N  N   A LYS   A 55  ? 0.1274 0.1369 0.1367 -0.0025 -0.0061 -0.0044 55  LYS   A N   
1376 N  N   B LYS   A 55  ? 0.1307 0.1425 0.1339 -0.0001 -0.0028 -0.0015 55  LYS   A N   
1377 C  CA  A LYS   A 55  ? 0.1350 0.1442 0.1566 0.0028  -0.0145 -0.0159 55  LYS   A CA  
1378 C  CA  B LYS   A 55  ? 0.1404 0.1538 0.1546 0.0075  -0.0080 -0.0066 55  LYS   A CA  
1379 C  C   A LYS   A 55  ? 0.1289 0.1551 0.1545 -0.0060 -0.0018 -0.0178 55  LYS   A C   
1380 C  C   B LYS   A 55  ? 0.1343 0.1591 0.1515 -0.0031 -0.0018 -0.0153 55  LYS   A C   
1381 O  O   A LYS   A 55  ? 0.1436 0.1671 0.1667 0.0001  -0.0083 -0.0227 55  LYS   A O   
1382 O  O   B LYS   A 55  ? 0.1457 0.1674 0.1539 0.0018  -0.0057 -0.0246 55  LYS   A O   
1383 C  CB  A LYS   A 55  ? 0.1430 0.1486 0.1664 0.0112  -0.0198 -0.0344 55  LYS   A CB  
1384 C  CB  B LYS   A 55  ? 0.1498 0.1653 0.1760 0.0110  -0.0042 -0.0099 55  LYS   A CB  
1385 C  CG  A LYS   A 55  ? 0.1490 0.1666 0.1714 0.0184  -0.0257 -0.0349 55  LYS   A CG  
1386 C  CG  B LYS   A 55  ? 0.1545 0.1867 0.2045 0.0141  -0.0078 -0.0250 55  LYS   A CG  
1387 C  CD  A LYS   A 55  ? 0.1528 0.1886 0.1792 0.0308  -0.0212 -0.0265 55  LYS   A CD  
1388 C  CD  B LYS   A 55  ? 0.1691 0.2089 0.2280 0.0144  -0.0135 -0.0302 55  LYS   A CD  
1389 C  CE  A LYS   A 55  ? 0.1651 0.2174 0.1816 0.0610  -0.0227 -0.0286 55  LYS   A CE  
1390 C  CE  B LYS   A 55  ? 0.1784 0.2294 0.2356 0.0075  -0.0243 -0.0230 55  LYS   A CE  
1391 N  NZ  A LYS   A 55  ? 0.1738 0.2328 0.1891 0.0738  -0.0279 -0.0276 55  LYS   A NZ  
1392 N  NZ  B LYS   A 55  ? 0.1809 0.2393 0.2407 0.0036  -0.0337 -0.0244 55  LYS   A NZ  
1419 N  N   . ALA   A 56  ? 0.1386 0.1624 0.1533 -0.0119 -0.0001 -0.0155 56  ALA   A N   
1420 C  CA  . ALA   A 56  ? 0.1490 0.1755 0.1479 -0.0133 0.0167  -0.0157 56  ALA   A CA  
1421 C  C   . ALA   A 56  ? 0.1570 0.1874 0.1215 -0.0126 0.0139  -0.0238 56  ALA   A C   
1422 O  O   . ALA   A 56  ? 0.1639 0.2170 0.1384 0.0017  0.0144  -0.0137 56  ALA   A O   
1423 C  CB  . ALA   A 56  ? 0.1544 0.1973 0.1618 -0.0202 0.0209  -0.0074 56  ALA   A CB  
1430 N  N   . THR   A 57  ? 0.1449 0.1710 0.1234 -0.0126 0.0050  -0.0146 57  THR   A N   
1431 C  CA  . THR   A 57  ? 0.1495 0.1665 0.1276 -0.0146 0.0038  -0.0091 57  THR   A CA  
1432 C  C   . THR   A 57  ? 0.1493 0.1748 0.1379 -0.0104 0.0026  -0.0163 57  THR   A C   
1433 O  O   . THR   A 57  ? 0.1454 0.1811 0.1558 -0.0149 -0.0054 -0.0235 57  THR   A O   
1434 C  CB  . THR   A 57  ? 0.1472 0.1668 0.1252 -0.0086 0.0040  -0.0104 57  THR   A CB  
1435 O  OG1 . THR   A 57  ? 0.1341 0.1649 0.1289 -0.0057 -0.0027 -0.0120 57  THR   A OG1 
1436 C  CG2 . THR   A 57  ? 0.1508 0.1660 0.1387 -0.0093 0.0044  -0.0006 57  THR   A CG2 
1444 N  N   . ASN   A 58  ? 0.1470 0.1661 0.1667 -0.0086 0.0053  -0.0287 58  ASN   A N   
1445 C  CA  . ASN   A 58  ? 0.1662 0.1639 0.1870 -0.0140 0.0158  -0.0351 58  ASN   A CA  
1446 C  C   . ASN   A 58  ? 0.1447 0.1534 0.1682 0.0003  0.0026  -0.0210 58  ASN   A C   
1447 O  O   . ASN   A 58  ? 0.1495 0.1607 0.1834 -0.0135 -0.0038 -0.0260 58  ASN   A O   
1448 C  CB  . ASN   A 58  ? 0.2111 0.1772 0.2183 -0.0189 0.0332  -0.0509 58  ASN   A CB  
1449 C  CG  . ASN   A 58  ? 0.2512 0.2048 0.2803 -0.0142 0.0241  -0.0212 58  ASN   A CG  
1450 O  OD1 . ASN   A 58  ? 0.2782 0.2017 0.3145 0.0217  0.0489  -0.0146 58  ASN   A OD1 
1451 N  ND2 . ASN   A 58  ? 0.2583 0.2136 0.2898 -0.0139 0.0133  -0.0205 58  ASN   A ND2 
1458 N  N   . ASN   A 59  ? 0.1342 0.1438 0.1610 -0.0026 -0.0104 -0.0151 59  ASN   A N   
1459 C  CA  . ASN   A 59  ? 0.1359 0.1385 0.1539 -0.0035 -0.0071 -0.0109 59  ASN   A CA  
1460 C  C   . ASN   A 59  ? 0.1354 0.1397 0.1514 -0.0136 -0.0102 0.0068  59  ASN   A C   
1461 O  O   . ASN   A 59  ? 0.1382 0.1423 0.1464 -0.0127 -0.0045 0.0084  59  ASN   A O   
1462 C  CB  . ASN   A 59  ? 0.1398 0.1330 0.1622 0.0002  -0.0154 -0.0105 59  ASN   A CB  
1463 C  CG  . ASN   A 59  ? 0.1416 0.1364 0.1660 -0.0007 -0.0286 0.0015  59  ASN   A CG  
1464 O  OD1 . ASN   A 59  ? 0.1532 0.1503 0.1504 -0.0128 -0.0173 0.0025  59  ASN   A OD1 
1465 N  ND2 . ASN   A 59  ? 0.1563 0.1412 0.1717 -0.0212 -0.0121 0.0018  59  ASN   A ND2 
1472 N  N   . ALA   A 60  ? 0.1291 0.1453 0.1535 -0.0062 0.0005  -0.0010 60  ALA   A N   
1473 C  CA  . ALA   A 60  ? 0.1301 0.1448 0.1601 -0.0036 -0.0168 0.0025  60  ALA   A CA  
1474 C  C   . ALA   A 60  ? 0.1350 0.1420 0.1626 -0.0020 -0.0124 0.0024  60  ALA   A C   
1475 O  O   . ALA   A 60  ? 0.1232 0.1404 0.1842 -0.0052 -0.0065 -0.0017 60  ALA   A O   
1476 C  CB  . ALA   A 60  ? 0.1403 0.1546 0.1553 -0.0048 -0.0216 -0.0158 60  ALA   A CB  
1482 N  N   . MET   A 61  ? 0.1323 0.1340 0.1495 -0.0072 -0.0015 -0.0092 61  MET   A N   
1483 C  CA  . MET   A 61  ? 0.1273 0.1339 0.1525 -0.0106 -0.0031 -0.0008 61  MET   A CA  
1484 C  C   . MET   A 61  ? 0.1249 0.1307 0.1518 -0.0074 -0.0025 0.0013  61  MET   A C   
1485 O  O   . MET   A 61  ? 0.1270 0.1288 0.1606 -0.0051 0.0096  0.0066  61  MET   A O   
1486 C  CB  . MET   A 61  ? 0.1359 0.1377 0.1387 -0.0057 0.0057  -0.0002 61  MET   A CB  
1487 C  CG  . MET   A 61  ? 0.1320 0.1439 0.1545 -0.0033 -0.0023 0.0013  61  MET   A CG  
1488 S  SD  . MET   A 61  ? 0.1382 0.1419 0.1829 -0.0102 0.0016  -0.0141 61  MET   A SD  
1489 C  CE  . MET   A 61  ? 0.1561 0.1537 0.2027 -0.0170 0.0155  -0.0225 61  MET   A CE  
1499 N  N   . GLN   A 62  ? 0.1254 0.1281 0.1523 -0.0032 -0.0016 0.0036  62  GLN   A N   
1500 C  CA  . GLN   A 62  ? 0.1291 0.1259 0.1540 -0.0061 0.0016  0.0096  62  GLN   A CA  
1501 C  C   . GLN   A 62  ? 0.1298 0.1165 0.1760 -0.0023 0.0072  0.0048  62  GLN   A C   
1502 O  O   . GLN   A 62  ? 0.1331 0.1344 0.1636 -0.0025 0.0034  0.0062  62  GLN   A O   
1503 C  CB  . GLN   A 62  ? 0.1373 0.1193 0.1668 -0.0035 0.0036  0.0019  62  GLN   A CB  
1504 C  CG  . GLN   A 62  ? 0.1346 0.1247 0.1635 -0.0036 0.0008  0.0144  62  GLN   A CG  
1505 C  CD  . GLN   A 62  ? 0.1384 0.1251 0.1581 -0.0012 0.0088  0.0102  62  GLN   A CD  
1506 O  OE1 . GLN   A 62  ? 0.1426 0.1409 0.1592 -0.0056 0.0016  0.0075  62  GLN   A OE1 
1507 N  NE2 . GLN   A 62  ? 0.1464 0.1288 0.1636 0.0085  0.0030  -0.0026 62  GLN   A NE2 
1516 N  N   . VAL   A 63  ? 0.1282 0.1311 0.1858 -0.0089 0.0041  -0.0171 63  VAL   A N   
1517 C  CA  . VAL   A 63  ? 0.1318 0.1374 0.1981 -0.0112 -0.0012 -0.0154 63  VAL   A CA  
1518 C  C   . VAL   A 63  ? 0.1224 0.1355 0.1757 -0.0117 -0.0065 -0.0168 63  VAL   A C   
1519 O  O   . VAL   A 63  ? 0.1221 0.1366 0.2035 -0.0116 -0.0023 -0.0027 63  VAL   A O   
1520 C  CB  . VAL   A 63  ? 0.1446 0.1555 0.2298 -0.0123 -0.0129 -0.0305 63  VAL   A CB  
1521 C  CG1 . VAL   A 63  ? 0.1572 0.1738 0.2812 -0.0099 -0.0177 -0.0499 63  VAL   A CG1 
1522 C  CG2 . VAL   A 63  ? 0.1477 0.1508 0.2429 -0.0124 0.0055  -0.0295 63  VAL   A CG2 
1532 N  N   . GLU   A 64  ? 0.1281 0.1406 0.1722 -0.0099 -0.0052 -0.0077 64  GLU   A N   
1533 C  CA  . GLU   A 64  ? 0.1252 0.1381 0.1731 -0.0088 -0.0037 -0.0000 64  GLU   A CA  
1534 C  C   . GLU   A 64  ? 0.1230 0.1344 0.1763 -0.0084 0.0059  0.0067  64  GLU   A C   
1535 O  O   . GLU   A 64  ? 0.1305 0.1417 0.1722 -0.0014 0.0111  -0.0006 64  GLU   A O   
1536 C  CB  . GLU   A 64  ? 0.1392 0.1520 0.1774 -0.0068 -0.0003 0.0020  64  GLU   A CB  
1537 C  CG  . GLU   A 64  ? 0.1443 0.1526 0.1815 -0.0147 -0.0006 0.0031  64  GLU   A CG  
1538 C  CD  . GLU   A 64  ? 0.1529 0.1620 0.1850 -0.0172 0.0019  0.0019  64  GLU   A CD  
1539 O  OE1 . GLU   A 64  ? 0.1473 0.1691 0.2147 -0.0219 0.0062  0.0096  64  GLU   A OE1 
1540 O  OE2 . GLU   A 64  ? 0.1679 0.1598 0.1732 -0.0177 -0.0060 0.0116  64  GLU   A OE2 
1547 N  N   . SER   A 65  ? 0.1189 0.1308 0.1775 -0.0008 0.0012  0.0063  65  SER   A N   
1548 C  CA  . SER   A 65  ? 0.1266 0.1309 0.1680 -0.0008 0.0035  0.0020  65  SER   A CA  
1549 C  C   . SER   A 65  ? 0.1257 0.1387 0.1604 -0.0106 0.0062  0.0052  65  SER   A C   
1550 O  O   . SER   A 65  ? 0.1341 0.1455 0.1674 0.0008  0.0166  0.0021  65  SER   A O   
1551 C  CB  . SER   A 65  ? 0.1304 0.1316 0.1647 -0.0051 0.0077  0.0134  65  SER   A CB  
1552 O  OG  . SER   A 65  ? 0.1334 0.1447 0.1547 -0.0090 0.0008  0.0173  65  SER   A OG  
1558 N  N   . ASP   A 66  ? 0.1343 0.1326 0.1647 -0.0051 0.0141  0.0100  66  ASP   A N   
1559 C  CA  . ASP   A 66  ? 0.1369 0.1396 0.1882 -0.0046 0.0110  0.0122  66  ASP   A CA  
1560 C  C   . ASP   A 66  ? 0.1385 0.1420 0.1876 -0.0021 0.0180  0.0242  66  ASP   A C   
1561 O  O   . ASP   A 66  ? 0.1428 0.1531 0.1997 -0.0043 0.0303  0.0251  66  ASP   A O   
1562 C  CB  . ASP   A 66  ? 0.1500 0.1494 0.2186 0.0093  0.0159  0.0325  66  ASP   A CB  
1563 C  CG  . ASP   A 66  ? 0.1766 0.1616 0.2383 0.0057  0.0059  0.0491  66  ASP   A CG  
1564 O  OD1 . ASP   A 66  ? 0.1705 0.1907 0.2121 -0.0064 -0.0025 0.0506  66  ASP   A OD1 
1565 O  OD2 . ASP   A 66  ? 0.1872 0.1805 0.3017 0.0253  -0.0123 0.0290  66  ASP   A OD2 
1570 N  N   . ASP   A 67  ? 0.1286 0.1441 0.1969 -0.0022 0.0153  0.0259  67  ASP   A N   
1571 C  CA  . ASP   A 67  ? 0.1295 0.1577 0.2189 -0.0044 0.0076  0.0241  67  ASP   A CA  
1572 C  C   . ASP   A 67  ? 0.1330 0.1595 0.2120 0.0018  0.0193  0.0267  67  ASP   A C   
1573 O  O   . ASP   A 67  ? 0.1284 0.1739 0.2300 0.0041  0.0306  0.0422  67  ASP   A O   
1574 C  CB  . ASP   A 67  ? 0.1367 0.1651 0.2381 -0.0092 -0.0129 0.0390  67  ASP   A CB  
1575 C  CG  . ASP   A 67  ? 0.1381 0.1857 0.2747 -0.0138 -0.0240 0.0541  67  ASP   A CG  
1576 O  OD1 . ASP   A 67  ? 0.1451 0.2050 0.3598 -0.0181 -0.0298 0.0642  67  ASP   A OD1 
1577 O  OD2 . ASP   A 67  ? 0.1419 0.1931 0.2579 0.0008  -0.0154 0.0455  67  ASP   A OD2 
1582 N  N   . TYR   A 68  ? 0.1453 0.1473 0.2080 0.0073  0.0228  0.0297  68  TYR   A N   
1583 C  CA  . TYR   A 68  ? 0.1507 0.1426 0.1961 0.0058  0.0292  0.0241  68  TYR   A CA  
1584 C  C   . TYR   A 68  ? 0.1407 0.1439 0.1992 0.0024  0.0296  0.0164  68  TYR   A C   
1585 O  O   . TYR   A 68  ? 0.1453 0.1488 0.2150 0.0089  0.0377  0.0237  68  TYR   A O   
1586 C  CB  . TYR   A 68  ? 0.1523 0.1429 0.2196 0.0054  0.0447  0.0287  68  TYR   A CB  
1587 C  CG  . TYR   A 68  ? 0.1565 0.1620 0.2638 0.0071  0.0597  0.0310  68  TYR   A CG  
1588 C  CD1 . TYR   A 68  ? 0.1683 0.1670 0.3019 -0.0188 0.0563  -0.0127 68  TYR   A CD1 
1589 C  CD2 . TYR   A 68  ? 0.1793 0.1716 0.2893 0.0155  0.0686  0.0408  68  TYR   A CD2 
1590 C  CE1 . TYR   A 68  ? 0.1780 0.1792 0.3344 -0.0122 0.0583  -0.0175 68  TYR   A CE1 
1591 C  CE2 . TYR   A 68  ? 0.1841 0.1752 0.3191 0.0040  0.0816  0.0079  68  TYR   A CE2 
1592 C  CZ  . TYR   A 68  ? 0.1793 0.1767 0.3471 -0.0125 0.0634  -0.0173 68  TYR   A CZ  
1593 O  OH  . TYR   A 68  ? 0.2018 0.1800 0.3665 -0.0080 0.0384  -0.0435 68  TYR   A OH  
1603 N  N   . ILE   A 69  ? 0.1361 0.1383 0.1993 0.0021  0.0203  0.0146  69  ILE   A N   
1604 C  CA  . ILE   A 69  ? 0.1387 0.1453 0.1858 0.0082  0.0176  0.0062  69  ILE   A CA  
1605 C  C   . ILE   A 69  ? 0.1413 0.1471 0.1810 0.0062  0.0243  0.0204  69  ILE   A C   
1606 O  O   . ILE   A 69  ? 0.1491 0.1553 0.1783 0.0028  0.0241  0.0234  69  ILE   A O   
1607 C  CB  . ILE   A 69  ? 0.1433 0.1685 0.1891 0.0015  0.0161  -0.0034 69  ILE   A CB  
1608 C  CG1 . ILE   A 69  ? 0.1468 0.1762 0.2024 0.0045  0.0235  -0.0215 69  ILE   A CG1 
1609 C  CG2 . ILE   A 69  ? 0.1669 0.1843 0.2055 0.0157  0.0094  -0.0187 69  ILE   A CG2 
1610 C  CD1 . ILE   A 69  ? 0.1526 0.1861 0.2251 -0.0095 0.0206  -0.0298 69  ILE   A CD1 
1622 N  N   . ALA   A 70  ? 0.1472 0.1470 0.1968 -0.0077 0.0207  0.0231  70  ALA   A N   
1623 C  CA  . ALA   A 70  ? 0.1523 0.1610 0.2087 -0.0118 0.0300  0.0300  70  ALA   A CA  
1624 C  C   . ALA   A 70  ? 0.1533 0.1763 0.2117 -0.0084 0.0318  0.0275  70  ALA   A C   
1625 O  O   . ALA   A 70  ? 0.1675 0.2147 0.2427 0.0127  0.0522  0.0514  70  ALA   A O   
1626 C  CB  . ALA   A 70  ? 0.1558 0.1606 0.2380 -0.0152 0.0282  0.0259  70  ALA   A CB  
1632 N  N   . THR   A 71  ? 0.1432 0.1781 0.2023 0.0026  0.0268  0.0404  71  THR   A N   
1633 C  CA  . THR   A 71  ? 0.1601 0.1926 0.2493 0.0116  0.0209  0.0444  71  THR   A CA  
1634 C  C   . THR   A 71  ? 0.1498 0.1831 0.2806 0.0204  0.0302  0.0354  71  THR   A C   
1635 O  O   . THR   A 71  ? 0.1562 0.2014 0.3280 0.0183  0.0496  0.0014  71  THR   A O   
1636 C  CB  . THR   A 71  ? 0.1916 0.2223 0.2828 0.0199  -0.0159 0.0466  71  THR   A CB  
1637 O  OG1 . THR   A 71  ? 0.2221 0.2394 0.2933 0.0074  -0.0400 0.0407  71  THR   A OG1 
1638 C  CG2 . THR   A 71  ? 0.1979 0.2422 0.3107 0.0264  -0.0228 0.0635  71  THR   A CG2 
1646 N  N   . ASN   A 72  ? 0.1475 0.1701 0.2398 0.0204  0.0396  0.0365  72  ASN   A N   
1647 C  CA  . ASN   A 72  ? 0.1563 0.1715 0.2507 0.0184  0.0495  0.0395  72  ASN   A CA  
1648 C  C   . ASN   A 72  ? 0.1643 0.1688 0.2428 0.0138  0.0564  0.0250  72  ASN   A C   
1649 O  O   . ASN   A 72  ? 0.1838 0.1639 0.2516 0.0183  0.0475  0.0080  72  ASN   A O   
1650 C  CB  . ASN   A 72  ? 0.1785 0.1871 0.2480 0.0222  0.0558  0.0430  72  ASN   A CB  
1651 C  CG  . ASN   A 72  ? 0.2048 0.1999 0.2414 0.0237  0.0515  0.0485  72  ASN   A CG  
1652 O  OD1 . ASN   A 72  ? 0.2207 0.2282 0.2607 0.0239  0.0497  0.0466  72  ASN   A OD1 
1653 N  ND2 . ASN   A 72  ? 0.2179 0.2010 0.2527 0.0503  0.0365  0.0394  72  ASN   A ND2 
1660 N  N   . GLY   A 73  ? 0.1627 0.1633 0.2212 0.0082  0.0523  0.0100  73  GLY   A N   
1661 C  CA  . GLY   A 73  ? 0.1764 0.1660 0.2001 -0.0046 0.0549  0.0142  73  GLY   A CA  
1662 C  C   . GLY   A 73  ? 0.1746 0.1522 0.1841 0.0025  0.0601  0.0214  73  GLY   A C   
1663 O  O   . GLY   A 73  ? 0.1771 0.1565 0.1919 0.0139  0.0436  0.0285  73  GLY   A O   
1667 N  N   . PRO   A 74  ? 0.1830 0.1504 0.1808 -0.0107 0.0593  0.0077  74  PRO   A N   
1668 C  CA  . PRO   A 74  ? 0.1786 0.1468 0.1985 -0.0013 0.0513  0.0162  74  PRO   A CA  
1669 C  C   . PRO   A 74  ? 0.1684 0.1319 0.1937 0.0002  0.0372  0.0078  74  PRO   A C   
1670 O  O   . PRO   A 74  ? 0.1717 0.1429 0.2213 0.0052  0.0390  -0.0000 74  PRO   A O   
1671 C  CB  . PRO   A 74  ? 0.1936 0.1771 0.2193 0.0005  0.0566  0.0317  74  PRO   A CB  
1672 C  CG  . PRO   A 74  ? 0.2185 0.2167 0.2635 -0.0200 0.0430  0.0082  74  PRO   A CG  
1673 C  CD  . PRO   A 74  ? 0.1963 0.1888 0.2177 -0.0201 0.0468  -0.0030 74  PRO   A CD  
1681 N  N   . LEU   A 75  ? 0.1692 0.1294 0.1758 -0.0010 0.0309  0.0050  75  LEU   A N   
1682 C  CA  . LEU   A 75  ? 0.1644 0.1267 0.1594 -0.0013 0.0155  0.0117  75  LEU   A CA  
1683 C  C   . LEU   A 75  ? 0.1756 0.1377 0.1544 0.0044  0.0142  0.0141  75  LEU   A C   
1684 O  O   . LEU   A 75  ? 0.2178 0.1557 0.1532 0.0156  0.0136  0.0139  75  LEU   A O   
1685 C  CB  . LEU   A 75  ? 0.1664 0.1323 0.1705 -0.0038 0.0122  0.0170  75  LEU   A CB  
1686 C  CG  . LEU   A 75  ? 0.1864 0.1642 0.1724 -0.0332 0.0076  0.0136  75  LEU   A CG  
1687 C  CD1 . LEU   A 75  ? 0.1965 0.2149 0.1737 -0.0373 0.0113  -0.0041 75  LEU   A CD1 
1688 C  CD2 . LEU   A 75  ? 0.2251 0.2074 0.2304 -0.0118 0.0012  0.0269  75  LEU   A CD2 
1700 N  N   . LYS   A 76  ? 0.1641 0.1336 0.1704 -0.0011 0.0040  0.0073  76  LYS   A N   
1701 C  CA  . LYS   A 76  ? 0.1639 0.1545 0.1732 -0.0063 0.0075  0.0021  76  LYS   A CA  
1702 C  C   . LYS   A 76  ? 0.1565 0.1498 0.1450 0.0035  0.0080  0.0132  76  LYS   A C   
1703 O  O   . LYS   A 76  ? 0.1668 0.1363 0.1463 -0.0029 0.0175  0.0162  76  LYS   A O   
1704 C  CB  . LYS   A 76  ? 0.1670 0.1755 0.2005 0.0034  0.0129  -0.0234 76  LYS   A CB  
1705 C  CG  . LYS   A 76  ? 0.1726 0.1718 0.2475 0.0050  0.0061  -0.0196 76  LYS   A CG  
1706 C  CD  . LYS   A 76  ? 0.1782 0.1740 0.2935 0.0176  -0.0133 -0.0132 76  LYS   A CD  
1707 C  CE  . LYS   A 76  ? 0.1927 0.1903 0.3563 0.0093  -0.0015 -0.0165 76  LYS   A CE  
1708 N  NZ  . LYS   A 76  ? 0.1939 0.1858 0.3973 0.0026  -0.0084 -0.0321 76  LYS   A NZ  
1722 N  N   . VAL   A 77  ? 0.1716 0.1562 0.1491 -0.0042 0.0167  0.0209  77  VAL   A N   
1723 C  CA  . VAL   A 77  ? 0.1698 0.1557 0.1444 0.0019  0.0133  0.0144  77  VAL   A CA  
1724 C  C   . VAL   A 77  ? 0.1663 0.1529 0.1504 0.0044  0.0164  0.0039  77  VAL   A C   
1725 O  O   . VAL   A 77  ? 0.1725 0.1563 0.1562 0.0079  0.0300  -0.0064 77  VAL   A O   
1726 C  CB  . VAL   A 77  ? 0.1815 0.1721 0.1612 -0.0003 0.0142  0.0217  77  VAL   A CB  
1727 C  CG1 . VAL   A 77  ? 0.1781 0.1835 0.1913 0.0061  0.0143  0.0134  77  VAL   A CG1 
1728 C  CG2 . VAL   A 77  ? 0.2026 0.1834 0.1883 0.0008  0.0004  0.0269  77  VAL   A CG2 
1738 N  N   . GLY   A 78  ? 0.1546 0.1424 0.1319 0.0053  0.0170  0.0042  78  GLY   A N   
1739 C  CA  . GLY   A 78  ? 0.1554 0.1472 0.1617 0.0026  0.0305  0.0073  78  GLY   A CA  
1740 C  C   . GLY   A 78  ? 0.1464 0.1355 0.1671 0.0019  0.0244  0.0144  78  GLY   A C   
1741 O  O   . GLY   A 78  ? 0.1499 0.1377 0.1826 0.0018  0.0211  0.0277  78  GLY   A O   
1745 N  N   . GLY   A 79  ? 0.1505 0.1319 0.1488 -0.0028 0.0205  0.0124  79  GLY   A N   
1746 C  CA  . GLY   A 79  ? 0.1481 0.1409 0.1575 0.0012  0.0140  0.0132  79  GLY   A CA  
1747 C  C   . GLY   A 79  ? 0.1337 0.1309 0.1484 -0.0017 0.0130  0.0049  79  GLY   A C   
1748 O  O   . GLY   A 79  ? 0.1399 0.1406 0.1581 0.0122  0.0149  0.0031  79  GLY   A O   
1752 N  N   . SER   A 80  ? 0.1284 0.1406 0.1800 -0.0033 0.0138  0.0020  80  SER   A N   
1753 C  CA  . SER   A 80  ? 0.1322 0.1384 0.1611 -0.0024 0.0106  0.0053  80  SER   A CA  
1754 C  C   . SER   A 80  ? 0.1324 0.1386 0.1595 -0.0014 0.0102  0.0204  80  SER   A C   
1755 O  O   . SER   A 80  ? 0.1288 0.1583 0.1940 0.0081  0.0140  0.0051  80  SER   A O   
1756 C  CB  . SER   A 80  ? 0.1473 0.1400 0.1762 -0.0046 0.0133  0.0064  80  SER   A CB  
1757 O  OG  . SER   A 80  ? 0.1666 0.1374 0.2148 0.0047  -0.0028 0.0211  80  SER   A OG  
1763 N  N   . CYS   A 81  ? 0.1293 0.1370 0.1583 0.0060  -0.0028 0.0207  81  CYS   A N   
1764 C  CA  . CYS   A 81  ? 0.1269 0.1465 0.1580 -0.0047 -0.0097 0.0249  81  CYS   A CA  
1765 C  C   . CYS   A 81  ? 0.1236 0.1458 0.1513 -0.0126 0.0011  0.0252  81  CYS   A C   
1766 O  O   . CYS   A 81  ? 0.1251 0.1718 0.1673 0.0002  0.0014  0.0309  81  CYS   A O   
1767 C  CB  . CYS   A 81  ? 0.1359 0.1498 0.1806 -0.0098 -0.0018 0.0310  81  CYS   A CB  
1768 S  SG  . CYS   A 81  ? 0.1472 0.1385 0.1804 -0.0124 0.0014  0.0158  81  CYS   A SG  
1774 N  N   . VAL   A 82  ? 0.1300 0.1515 0.1503 -0.0044 -0.0108 0.0256  82  VAL   A N   
1775 C  CA  . VAL   A 82  ? 0.1402 0.1559 0.1503 0.0021  -0.0084 0.0365  82  VAL   A CA  
1776 C  C   . VAL   A 82  ? 0.1405 0.1552 0.1632 -0.0045 -0.0081 0.0274  82  VAL   A C   
1777 O  O   . VAL   A 82  ? 0.1374 0.1602 0.1890 -0.0077 -0.0005 0.0077  82  VAL   A O   
1778 C  CB  . VAL   A 82  ? 0.1674 0.1666 0.1615 -0.0007 -0.0056 0.0366  82  VAL   A CB  
1779 C  CG1 . VAL   A 82  ? 0.1913 0.1776 0.1877 -0.0005 -0.0047 0.0281  82  VAL   A CG1 
1780 C  CG2 . VAL   A 82  ? 0.1708 0.1714 0.2098 0.0008  -0.0041 0.0285  82  VAL   A CG2 
1790 N  N   . LEU   A 83  ? 0.1377 0.1549 0.1487 -0.0107 -0.0151 0.0138  83  LEU   A N   
1791 C  CA  . LEU   A 83  ? 0.1370 0.1583 0.1406 -0.0162 -0.0092 0.0096  83  LEU   A CA  
1792 C  C   . LEU   A 83  ? 0.1412 0.1568 0.1428 -0.0119 -0.0157 0.0195  83  LEU   A C   
1793 O  O   . LEU   A 83  ? 0.1496 0.1559 0.1591 -0.0169 -0.0066 0.0227  83  LEU   A O   
1794 C  CB  . LEU   A 83  ? 0.1429 0.1678 0.1507 -0.0195 -0.0091 0.0252  83  LEU   A CB  
1795 C  CG  . LEU   A 83  ? 0.1565 0.1692 0.1629 -0.0164 -0.0003 0.0113  83  LEU   A CG  
1796 C  CD1 . LEU   A 83  ? 0.1692 0.1718 0.1749 -0.0294 -0.0129 0.0214  83  LEU   A CD1 
1797 C  CD2 . LEU   A 83  ? 0.1566 0.1849 0.1791 -0.0117 0.0135  0.0165  83  LEU   A CD2 
1809 N  N   . SER   A 84  ? 0.1528 0.1617 0.1568 -0.0158 -0.0089 0.0206  84  SER   A N   
1810 C  CA  . SER   A 84  ? 0.1684 0.1656 0.1406 -0.0105 -0.0022 0.0150  84  SER   A CA  
1811 C  C   . SER   A 84  ? 0.1704 0.1643 0.1388 -0.0195 0.0036  0.0174  84  SER   A C   
1812 O  O   . SER   A 84  ? 0.1642 0.1742 0.1403 -0.0117 -0.0034 0.0187  84  SER   A O   
1813 C  CB  . SER   A 84  ? 0.1752 0.1848 0.1606 -0.0059 -0.0133 -0.0025 84  SER   A CB  
1814 O  OG  . SER   A 84  ? 0.1796 0.2093 0.1649 -0.0151 -0.0254 -0.0058 84  SER   A OG  
1820 N  N   . GLY   A 85  ? 0.1779 0.1752 0.1397 -0.0180 0.0087  0.0189  85  GLY   A N   
1821 C  CA  . GLY   A 85  ? 0.1789 0.1848 0.1681 -0.0223 0.0143  0.0006  85  GLY   A CA  
1822 C  C   . GLY   A 85  ? 0.1760 0.1961 0.1360 -0.0223 -0.0007 0.0061  85  GLY   A C   
1823 O  O   . GLY   A 85  ? 0.1815 0.2129 0.1481 -0.0354 0.0069  -0.0119 85  GLY   A O   
1827 N  N   . HIS   A 86  ? 0.1777 0.1889 0.1325 -0.0160 -0.0061 0.0111  86  HIS   A N   
1828 C  CA  . HIS   A 86  ? 0.1970 0.1902 0.1236 -0.0152 -0.0025 0.0121  86  HIS   A CA  
1829 C  C   . HIS   A 86  ? 0.2248 0.2044 0.1147 -0.0262 -0.0087 0.0067  86  HIS   A C   
1830 O  O   . HIS   A 86  ? 0.2350 0.2294 0.1380 -0.0205 0.0040  0.0118  86  HIS   A O   
1831 C  CB  . HIS   A 86  ? 0.1969 0.1839 0.1376 -0.0098 0.0006  0.0171  86  HIS   A CB  
1832 C  CG  . HIS   A 86  ? 0.1827 0.1838 0.1513 -0.0090 -0.0009 0.0143  86  HIS   A CG  
1833 N  ND1 . HIS   A 86  ? 0.1875 0.1826 0.1778 -0.0199 -0.0084 0.0184  86  HIS   A ND1 
1834 C  CD2 . HIS   A 86  ? 0.1783 0.1805 0.1476 0.0026  -0.0015 0.0171  86  HIS   A CD2 
1835 C  CE1 . HIS   A 86  ? 0.1828 0.1862 0.1734 -0.0131 0.0133  0.0212  86  HIS   A CE1 
1836 N  NE2 . HIS   A 86  ? 0.1812 0.1835 0.1597 0.0038  0.0100  0.0301  86  HIS   A NE2 
1844 N  N   . ASN   A 87  ? 0.2332 0.2146 0.1408 -0.0169 0.0098  -0.0017 87  ASN   A N   
1845 C  CA  . ASN   A 87  ? 0.2522 0.2269 0.1370 -0.0119 0.0326  -0.0147 87  ASN   A CA  
1846 C  C   . ASN   A 87  ? 0.2485 0.2434 0.1615 -0.0196 0.0526  -0.0012 87  ASN   A C   
1847 O  O   . ASN   A 87  ? 0.2873 0.2684 0.2048 -0.0371 0.0955  -0.0144 87  ASN   A O   
1848 C  CB  . ASN   A 87  ? 0.2683 0.2318 0.1393 -0.0024 0.0392  -0.0121 87  ASN   A CB  
1849 C  CG  . ASN   A 87  ? 0.2793 0.2458 0.1523 0.0030  0.0461  0.0054  87  ASN   A CG  
1850 O  OD1 . ASN   A 87  ? 0.2958 0.2442 0.1529 0.0153  0.0342  0.0109  87  ASN   A OD1 
1851 N  ND2 . ASN   A 87  ? 0.2785 0.2726 0.1756 0.0048  0.0389  0.0001  87  ASN   A ND2 
1858 N  N   A LEU   A 88  ? 0.2223 0.2287 0.1590 -0.0197 0.0294  0.0057  88  LEU   A N   
1859 N  N   B LEU   A 88  ? 0.2255 0.2341 0.1637 -0.0207 0.0392  -0.0005 88  LEU   A N   
1860 C  CA  A LEU   A 88  ? 0.2044 0.2223 0.1648 -0.0262 0.0310  0.0303  88  LEU   A CA  
1861 C  CA  B LEU   A 88  ? 0.2085 0.2299 0.1711 -0.0258 0.0438  0.0145  88  LEU   A CA  
1862 C  C   A LEU   A 88  ? 0.1958 0.2245 0.1607 -0.0279 0.0302  0.0356  88  LEU   A C   
1863 C  C   B LEU   A 88  ? 0.1965 0.2272 0.1638 -0.0265 0.0362  0.0329  88  LEU   A C   
1864 O  O   A LEU   A 88  ? 0.1954 0.2269 0.2032 -0.0251 0.0317  0.0415  88  LEU   A O   
1865 O  O   B LEU   A 88  ? 0.1927 0.2284 0.1885 -0.0221 0.0427  0.0532  88  LEU   A O   
1866 C  CB  A LEU   A 88  ? 0.1993 0.2258 0.1825 -0.0319 -0.0005 0.0437  88  LEU   A CB  
1867 C  CB  B LEU   A 88  ? 0.2066 0.2370 0.1892 -0.0313 0.0334  0.0097  88  LEU   A CB  
1868 C  CG  A LEU   A 88  ? 0.2157 0.2328 0.2077 -0.0330 -0.0159 0.0576  88  LEU   A CG  
1869 C  CG  B LEU   A 88  ? 0.2145 0.2454 0.2034 -0.0313 0.0289  0.0070  88  LEU   A CG  
1870 C  CD1 A LEU   A 88  ? 0.2243 0.2391 0.2091 -0.0331 -0.0210 0.0470  88  LEU   A CD1 
1871 C  CD1 B LEU   A 88  ? 0.2180 0.2510 0.2035 -0.0305 0.0322  -0.0079 88  LEU   A CD1 
1872 C  CD2 A LEU   A 88  ? 0.2281 0.2406 0.2517 -0.0306 -0.0092 0.0468  88  LEU   A CD2 
1873 C  CD2 B LEU   A 88  ? 0.2187 0.2503 0.2150 -0.0274 0.0346  0.0012  88  LEU   A CD2 
1896 N  N   . ALA   A 89  ? 0.1944 0.2226 0.1466 -0.0254 0.0178  0.0149  89  ALA   A N   
1897 C  CA  . ALA   A 89  ? 0.1981 0.2284 0.1366 -0.0125 0.0173  0.0230  89  ALA   A CA  
1898 C  C   . ALA   A 89  ? 0.2013 0.2295 0.1488 -0.0093 0.0104  0.0231  89  ALA   A C   
1899 O  O   . ALA   A 89  ? 0.1899 0.2193 0.1872 -0.0229 0.0033  -0.0053 89  ALA   A O   
1900 C  CB  . ALA   A 89  ? 0.1881 0.2281 0.1301 -0.0130 0.0172  0.0343  89  ALA   A CB  
1907 N  N   A LYS   A 90  ? 0.2027 0.2391 0.1443 -0.0162 -0.0063 0.0311  90  LYS   A N   
1908 N  N   B LYS   A 90  ? 0.2067 0.2399 0.1553 -0.0159 -0.0047 0.0262  90  LYS   A N   
1909 C  CA  A LYS   A 90  ? 0.2106 0.2517 0.1433 -0.0121 -0.0215 0.0304  90  LYS   A CA  
1910 C  CA  B LYS   A 90  ? 0.2163 0.2526 0.1643 -0.0147 -0.0175 0.0233  90  LYS   A CA  
1911 C  C   A LYS   A 90  ? 0.1921 0.2372 0.1443 -0.0194 -0.0195 0.0143  90  LYS   A C   
1912 C  C   B LYS   A 90  ? 0.1962 0.2376 0.1519 -0.0208 -0.0205 0.0132  90  LYS   A C   
1913 O  O   A LYS   A 90  ? 0.1950 0.2481 0.1760 -0.0197 -0.0177 0.0071  90  LYS   A O   
1914 O  O   B LYS   A 90  ? 0.1978 0.2485 0.1761 -0.0219 -0.0214 0.0057  90  LYS   A O   
1915 C  CB  A LYS   A 90  ? 0.2372 0.2806 0.1810 -0.0102 -0.0308 0.0479  90  LYS   A CB  
1916 C  CB  B LYS   A 90  ? 0.2447 0.2810 0.2130 -0.0143 -0.0218 0.0333  90  LYS   A CB  
1917 C  CG  A LYS   A 90  ? 0.2679 0.3035 0.2802 -0.0086 -0.0280 0.0542  90  LYS   A CG  
1918 C  CG  B LYS   A 90  ? 0.2745 0.3032 0.2987 -0.0134 -0.0201 0.0364  90  LYS   A CG  
1919 C  CD  A LYS   A 90  ? 0.2999 0.3264 0.3665 -0.0105 -0.0132 0.0595  90  LYS   A CD  
1920 C  CD  B LYS   A 90  ? 0.3045 0.3240 0.3738 -0.0141 -0.0109 0.0393  90  LYS   A CD  
1921 C  CE  A LYS   A 90  ? 0.3178 0.3468 0.4342 -0.0124 -0.0021 0.0567  90  LYS   A CE  
1922 C  CE  B LYS   A 90  ? 0.3210 0.3425 0.4325 -0.0144 -0.0037 0.0366  90  LYS   A CE  
1923 N  NZ  A LYS   A 90  ? 0.3341 0.3650 0.4778 -0.0141 0.0062  0.0482  90  LYS   A NZ  
1924 N  NZ  B LYS   A 90  ? 0.3351 0.3576 0.4693 -0.0149 0.0025  0.0301  90  LYS   A NZ  
1951 N  N   . HIS   A 91  ? 0.1853 0.2128 0.1102 -0.0224 -0.0282 0.0225  91  HIS   A N   
1952 C  CA  . HIS   A 91  ? 0.1776 0.1841 0.1217 -0.0106 -0.0265 0.0224  91  HIS   A CA  
1953 C  C   . HIS   A 91  ? 0.1615 0.1687 0.1142 -0.0105 -0.0189 0.0237  91  HIS   A C   
1954 O  O   . HIS   A 91  ? 0.1577 0.1839 0.1391 -0.0228 -0.0020 0.0210  91  HIS   A O   
1955 C  CB  . HIS   A 91  ? 0.1951 0.2101 0.1838 0.0075  -0.0460 0.0277  91  HIS   A CB  
1956 C  CG  . HIS   A 91  ? 0.2343 0.2590 0.2435 0.0175  -0.0697 0.0026  91  HIS   A CG  
1957 N  ND1 . HIS   A 91  ? 0.2447 0.2890 0.2783 0.0197  -0.0840 -0.0207 91  HIS   A ND1 
1958 C  CD2 . HIS   A 91  ? 0.2662 0.2882 0.2673 0.0196  -0.0796 0.0128  91  HIS   A CD2 
1959 C  CE1 . HIS   A 91  ? 0.2607 0.3022 0.2959 0.0236  -0.0851 -0.0111 91  HIS   A CE1 
1960 N  NE2 . HIS   A 91  ? 0.2765 0.3026 0.2971 0.0269  -0.0860 0.0039  91  HIS   A NE2 
1969 N  N   . CYS   A 92  ? 0.1549 0.1631 0.1163 -0.0147 -0.0125 0.0223  92  CYS   A N   
1970 C  CA  . CYS   A 92  ? 0.1497 0.1582 0.1301 -0.0110 0.0041  0.0202  92  CYS   A CA  
1971 C  C   . CYS   A 92  ? 0.1412 0.1511 0.1279 -0.0160 0.0060  0.0177  92  CYS   A C   
1972 O  O   . CYS   A 92  ? 0.1460 0.1521 0.1548 -0.0187 0.0005  0.0149  92  CYS   A O   
1973 C  CB  . CYS   A 92  ? 0.1474 0.1578 0.1476 -0.0087 0.0000  0.0138  92  CYS   A CB  
1974 S  SG  . CYS   A 92  ? 0.1465 0.1442 0.1442 -0.0113 -0.0026 0.0153  92  CYS   A SG  
1980 N  N   . LEU   A 93  ? 0.1387 0.1342 0.1431 -0.0117 0.0130  0.0148  93  LEU   A N   
1981 C  CA  . LEU   A 93  ? 0.1262 0.1377 0.1479 -0.0105 0.0043  0.0200  93  LEU   A CA  
1982 C  C   . LEU   A 93  ? 0.1242 0.1240 0.1336 -0.0030 0.0023  0.0138  93  LEU   A C   
1983 O  O   . LEU   A 93  ? 0.1255 0.1379 0.1245 -0.0040 0.0017  0.0112  93  LEU   A O   
1984 C  CB  . LEU   A 93  ? 0.1340 0.1384 0.1584 0.0001  -0.0032 0.0214  93  LEU   A CB  
1985 C  CG  . LEU   A 93  ? 0.1412 0.1408 0.1519 -0.0006 0.0108  0.0242  93  LEU   A CG  
1986 C  CD1 . LEU   A 93  ? 0.1464 0.1464 0.1707 0.0000  0.0071  0.0147  93  LEU   A CD1 
1987 C  CD2 . LEU   A 93  ? 0.1562 0.1349 0.1837 -0.0127 0.0025  0.0189  93  LEU   A CD2 
1999 N  N   . HIS   A 94  ? 0.1250 0.1255 0.1363 -0.0044 0.0064  0.0202  94  HIS   A N   
2000 C  CA  . HIS   A 94  ? 0.1225 0.1280 0.1373 -0.0033 0.0026  0.0154  94  HIS   A CA  
2001 C  C   . HIS   A 94  ? 0.1227 0.1223 0.1377 -0.0062 0.0005  0.0153  94  HIS   A C   
2002 O  O   . HIS   A 94  ? 0.1268 0.1434 0.1717 0.0013  0.0041  -0.0086 94  HIS   A O   
2003 C  CB  . HIS   A 94  ? 0.1226 0.1252 0.1381 -0.0065 -0.0035 0.0119  94  HIS   A CB  
2004 C  CG  . HIS   A 94  ? 0.1340 0.1237 0.1356 -0.0072 -0.0023 0.0184  94  HIS   A CG  
2005 N  ND1 . HIS   A 94  ? 0.1258 0.1254 0.1406 -0.0020 0.0002  0.0171  94  HIS   A ND1 
2006 C  CD2 . HIS   A 94  ? 0.1360 0.1334 0.1458 -0.0090 -0.0026 0.0101  94  HIS   A CD2 
2007 C  CE1 . HIS   A 94  ? 0.1312 0.1299 0.1356 -0.0078 -0.0034 0.0134  94  HIS   A CE1 
2008 N  NE2 . HIS   A 94  ? 0.1333 0.1331 0.1445 -0.0169 -0.0050 0.0044  94  HIS   A NE2 
2016 N  N   . VAL   A 95  ? 0.1223 0.1240 0.1238 -0.0059 0.0057  0.0123  95  VAL   A N   
2017 C  CA  . VAL   A 95  ? 0.1278 0.1282 0.1211 -0.0027 0.0085  0.0154  95  VAL   A CA  
2018 C  C   . VAL   A 95  ? 0.1264 0.1253 0.1200 -0.0090 0.0026  0.0103  95  VAL   A C   
2019 O  O   . VAL   A 95  ? 0.1328 0.1339 0.1334 0.0142  0.0009  0.0101  95  VAL   A O   
2020 C  CB  . VAL   A 95  ? 0.1303 0.1272 0.1417 -0.0125 0.0110  0.0115  95  VAL   A CB  
2021 C  CG1 . VAL   A 95  ? 0.1471 0.1313 0.1606 -0.0197 0.0051  0.0027  95  VAL   A CG1 
2022 C  CG2 . VAL   A 95  ? 0.1327 0.1342 0.1448 -0.0149 0.0168  0.0218  95  VAL   A CG2 
2032 N  N   . VAL   A 96  ? 0.1312 0.1256 0.1092 -0.0057 0.0057  0.0107  96  VAL   A N   
2033 C  CA  . VAL   A 96  ? 0.1331 0.1293 0.1259 -0.0042 0.0064  0.0172  96  VAL   A CA  
2034 C  C   . VAL   A 96  ? 0.1366 0.1354 0.1409 -0.0036 0.0046  0.0179  96  VAL   A C   
2035 O  O   . VAL   A 96  ? 0.1472 0.1417 0.1607 -0.0055 0.0157  -0.0027 96  VAL   A O   
2036 C  CB  . VAL   A 96  ? 0.1422 0.1344 0.1374 -0.0057 0.0158  0.0095  96  VAL   A CB  
2037 C  CG1 . VAL   A 96  ? 0.1526 0.1406 0.1290 -0.0026 0.0147  0.0101  96  VAL   A CG1 
2038 C  CG2 . VAL   A 96  ? 0.1445 0.1410 0.1507 -0.0087 0.0212  0.0079  96  VAL   A CG2 
2048 N  N   . GLY   A 97  ? 0.1352 0.1384 0.1361 -0.0064 0.0046  0.0135  97  GLY   A N   
2049 C  CA  . GLY   A 97  ? 0.1459 0.1560 0.1345 -0.0088 -0.0042 0.0179  97  GLY   A CA  
2050 C  C   . GLY   A 97  ? 0.1463 0.1680 0.1258 -0.0125 -0.0089 0.0113  97  GLY   A C   
2051 O  O   . GLY   A 97  ? 0.1606 0.1637 0.1550 -0.0189 -0.0073 0.0218  97  GLY   A O   
2055 N  N   A PRO   A 98  ? 0.1498 0.1745 0.1144 -0.0027 -0.0065 0.0142  98  PRO   A N   
2056 N  N   B PRO   A 98  ? 0.1523 0.1721 0.1355 -0.0016 0.0004  0.0267  98  PRO   A N   
2057 C  CA  A PRO   A 98  ? 0.1539 0.1849 0.1352 -0.0047 -0.0044 0.0104  98  PRO   A CA  
2058 C  CA  B PRO   A 98  ? 0.1557 0.1788 0.1491 0.0028  -0.0052 0.0262  98  PRO   A CA  
2059 C  C   A PRO   A 98  ? 0.1588 0.1875 0.1239 -0.0164 -0.0076 0.0129  98  PRO   A C   
2060 C  C   B PRO   A 98  ? 0.1682 0.1712 0.1381 0.0006  0.0009  0.0261  98  PRO   A C   
2061 O  O   A PRO   A 98  ? 0.1554 0.1660 0.1309 -0.0069 0.0066  0.0096  98  PRO   A O   
2062 O  O   B PRO   A 98  ? 0.1653 0.1668 0.1789 0.0003  0.0214  0.0268  98  PRO   A O   
2063 C  CB  A PRO   A 98  ? 0.1543 0.1894 0.1202 0.0152  -0.0087 0.0055  98  PRO   A CB  
2064 C  CB  B PRO   A 98  ? 0.1576 0.1832 0.1515 0.0113  -0.0076 0.0298  98  PRO   A CB  
2065 C  CG  A PRO   A 98  ? 0.1525 0.1827 0.1242 0.0191  -0.0154 -0.0001 98  PRO   A CG  
2066 C  CG  B PRO   A 98  ? 0.1661 0.1800 0.1614 0.0097  -0.0108 0.0268  98  PRO   A CG  
2067 C  CD  A PRO   A 98  ? 0.1520 0.1718 0.1259 0.0083  -0.0087 0.0011  98  PRO   A CD  
2068 C  CD  B PRO   A 98  ? 0.1522 0.1686 0.1450 0.0050  -0.0137 0.0307  98  PRO   A CD  
2083 N  N   A ASN   A 99  ? 0.1662 0.2051 0.1148 -0.0227 0.0057  0.0137  99  ASN   A N   
2084 N  N   B ASN   A 99  ? 0.1917 0.1623 0.1296 0.0076  -0.0055 0.0368  99  ASN   A N   
2085 C  CA  A ASN   A 99  ? 0.1860 0.2132 0.0995 -0.0241 0.0097  0.0235  99  ASN   A CA  
2086 C  CA  B ASN   A 99  ? 0.2221 0.1618 0.1330 0.0107  -0.0097 0.0422  99  ASN   A CA  
2087 C  C   A ASN   A 99  ? 0.2060 0.2366 0.0843 -0.0278 0.0140  0.0331  99  ASN   A C   
2088 C  C   B ASN   A 99  ? 0.2343 0.1643 0.1337 0.0025  -0.0183 0.0440  99  ASN   A C   
2089 O  O   A ASN   A 99  ? 0.2154 0.2453 0.1172 -0.0176 0.0040  0.0093  99  ASN   A O   
2090 O  O   B ASN   A 99  ? 0.2351 0.1557 0.1347 -0.0028 -0.0312 0.0338  99  ASN   A O   
2091 C  CB  A ASN   A 99  ? 0.1836 0.2043 0.1171 -0.0220 -0.0085 0.0221  99  ASN   A CB  
2092 C  CB  B ASN   A 99  ? 0.2368 0.1629 0.1572 0.0188  -0.0143 0.0264  99  ASN   A CB  
2093 C  CG  A ASN   A 99  ? 0.1862 0.1871 0.1454 -0.0146 -0.0143 0.0147  99  ASN   A CG  
2094 C  CG  B ASN   A 99  ? 0.2467 0.1729 0.1805 0.0190  -0.0251 0.0211  99  ASN   A CG  
2095 O  OD1 A ASN   A 99  ? 0.1880 0.1933 0.1293 0.0000  -0.0116 0.0075  99  ASN   A OD1 
2096 O  OD1 B ASN   A 99  ? 0.2424 0.1795 0.1654 0.0191  -0.0318 0.0392  99  ASN   A OD1 
2097 N  ND2 A ASN   A 99  ? 0.1845 0.1698 0.1558 -0.0112 -0.0277 0.0287  99  ASN   A ND2 
2098 N  ND2 B ASN   A 99  ? 0.2537 0.1791 0.1967 0.0331  -0.0447 0.0051  99  ASN   A ND2 
2111 N  N   A VAL   A 100 ? 0.2217 0.2503 0.1115 -0.0389 -0.0157 0.0257  100 VAL   A N   
2112 N  N   B VAL   A 100 ? 0.2558 0.1911 0.1710 0.0047  -0.0172 0.0454  100 VAL   A N   
2113 C  CA  A VAL   A 100 ? 0.2402 0.2688 0.1429 -0.0413 -0.0309 0.0299  100 VAL   A CA  
2114 C  CA  B VAL   A 100 ? 0.2924 0.2116 0.2164 0.0085  -0.0172 0.0484  100 VAL   A CA  
2115 C  C   A VAL   A 100 ? 0.2482 0.2914 0.1370 -0.0474 -0.0427 0.0531  100 VAL   A C   
2116 C  C   B VAL   A 100 ? 0.3116 0.2186 0.2264 0.0187  -0.0191 0.0463  100 VAL   A C   
2117 O  O   A VAL   A 100 ? 0.2603 0.3029 0.1713 -0.0447 -0.0174 0.0504  100 VAL   A O   
2118 O  O   B VAL   A 100 ? 0.3140 0.2207 0.2319 0.0155  -0.0309 0.0362  100 VAL   A O   
2119 C  CB  A VAL   A 100 ? 0.2563 0.2697 0.1811 -0.0405 -0.0166 0.0122  100 VAL   A CB  
2120 C  CB  B VAL   A 100 ? 0.3110 0.2289 0.2665 -0.0039 -0.0108 0.0441  100 VAL   A CB  
2121 C  CG1 A VAL   A 100 ? 0.2593 0.2770 0.2058 -0.0426 -0.0044 -0.0028 100 VAL   A CG1 
2122 C  CG1 B VAL   A 100 ? 0.3142 0.2333 0.2883 -0.0057 -0.0137 0.0327  100 VAL   A CG1 
2123 C  CG2 A VAL   A 100 ? 0.2663 0.2689 0.1794 -0.0382 -0.0140 0.0227  100 VAL   A CG2 
2124 C  CG2 B VAL   A 100 ? 0.3185 0.2355 0.2861 -0.0066 -0.0056 0.0481  100 VAL   A CG2 
2143 N  N   A ASN   A 101 ? 0.2495 0.2982 0.1637 -0.0550 -0.0588 0.0796  101 ASN   A N   
2144 N  N   B ASN   A 101 ? 0.3320 0.2350 0.2354 0.0272  -0.0094 0.0481  101 ASN   A N   
2145 C  CA  A ASN   A 101 ? 0.2625 0.3069 0.1813 -0.0614 -0.0608 0.0950  101 ASN   A CA  
2146 C  CA  B ASN   A 101 ? 0.3531 0.2614 0.2651 0.0385  0.0005  0.0546  101 ASN   A CA  
2147 C  C   A ASN   A 101 ? 0.2880 0.3327 0.1938 -0.0577 -0.0282 0.1109  101 ASN   A C   
2148 C  C   B ASN   A 101 ? 0.3645 0.2745 0.2729 0.0387  0.0081  0.0638  101 ASN   A C   
2149 O  O   A ASN   A 101 ? 0.3024 0.3333 0.2341 -0.0512 -0.0114 0.0917  101 ASN   A O   
2150 O  O   B ASN   A 101 ? 0.3715 0.2787 0.2928 0.0366  0.0133  0.0741  101 ASN   A O   
2151 C  CB  A ASN   A 101 ? 0.2629 0.2895 0.1809 -0.0683 -0.0809 0.0930  101 ASN   A CB  
2152 C  CB  B ASN   A 101 ? 0.3622 0.2758 0.2939 0.0475  0.0069  0.0526  101 ASN   A CB  
2153 C  CG  A ASN   A 101 ? 0.2680 0.2712 0.1860 -0.0809 -0.0848 0.0751  101 ASN   A CG  
2154 C  CG  B ASN   A 101 ? 0.3688 0.2914 0.3249 0.0516  0.0114  0.0476  101 ASN   A CG  
2155 O  OD1 A ASN   A 101 ? 0.2692 0.2824 0.1912 -0.0734 -0.0787 0.0464  101 ASN   A OD1 
2156 O  OD1 B ASN   A 101 ? 0.3681 0.2981 0.3295 0.0528  0.0041  0.0393  101 ASN   A OD1 
2157 N  ND2 A ASN   A 101 ? 0.2739 0.2590 0.2076 -0.0847 -0.0860 0.0749  101 ASN   A ND2 
2158 N  ND2 B ASN   A 101 ? 0.3745 0.3000 0.3376 0.0509  0.0167  0.0472  101 ASN   A ND2 
2171 N  N   A LYS   A 102 ? 0.2955 0.3634 0.2246 -0.0610 -0.0240 0.1136  102 LYS   A N   
2172 N  N   B LYS   A 102 ? 0.3688 0.2872 0.2870 0.0395  0.0130  0.0539  102 LYS   A N   
2173 C  CA  A LYS   A 102 ? 0.3109 0.3903 0.2514 -0.0578 -0.0232 0.1100  102 LYS   A CA  
2174 C  CA  B LYS   A 102 ? 0.3737 0.3019 0.2882 0.0350  0.0260  0.0525  102 LYS   A CA  
2175 C  C   A LYS   A 102 ? 0.3206 0.4105 0.2422 -0.0427 -0.0143 0.0994  102 LYS   A C   
2176 C  C   B LYS   A 102 ? 0.3580 0.3028 0.2637 0.0453  0.0209  0.0620  102 LYS   A C   
2177 O  O   A LYS   A 102 ? 0.3270 0.4186 0.2522 -0.0376 -0.0125 0.0983  102 LYS   A O   
2178 O  O   B LYS   A 102 ? 0.3597 0.3022 0.2829 0.0504  0.0259  0.0703  102 LYS   A O   
2179 C  CB  A LYS   A 102 ? 0.3182 0.3953 0.2932 -0.0654 -0.0366 0.1041  102 LYS   A CB  
2180 C  CB  B LYS   A 102 ? 0.3910 0.3127 0.3243 0.0233  0.0305  0.0416  102 LYS   A CB  
2181 C  CG  A LYS   A 102 ? 0.3246 0.3982 0.3250 -0.0696 -0.0492 0.0933  102 LYS   A CG  
2182 C  CG  B LYS   A 102 ? 0.4055 0.3204 0.3669 0.0132  0.0358  0.0327  102 LYS   A CG  
2183 C  CD  A LYS   A 102 ? 0.3344 0.4020 0.3645 -0.0727 -0.0593 0.0772  102 LYS   A CD  
2184 C  CD  B LYS   A 102 ? 0.4169 0.3300 0.4082 0.0049  0.0441  0.0276  102 LYS   A CD  
2185 C  CE  A LYS   A 102 ? 0.3439 0.4048 0.3912 -0.0752 -0.0626 0.0714  102 LYS   A CE  
2186 C  CE  B LYS   A 102 ? 0.4241 0.3380 0.4409 -0.0004 0.0477  0.0216  102 LYS   A CE  
2187 N  NZ  A LYS   A 102 ? 0.3493 0.4060 0.4087 -0.0789 -0.0586 0.0649  102 LYS   A NZ  
2188 N  NZ  B LYS   A 102 ? 0.4285 0.3440 0.4591 -0.0026 0.0507  0.0194  102 LYS   A NZ  
2215 N  N   A GLY   A 103 ? 0.3205 0.4239 0.2563 -0.0304 -0.0092 0.0782  103 GLY   A N   
2216 N  N   B GLY   A 103 ? 0.3387 0.3068 0.2255 0.0537  0.0098  0.0493  103 GLY   A N   
2217 C  CA  A GLY   A 103 ? 0.3216 0.4329 0.2612 -0.0201 0.0017  0.0618  103 GLY   A CA  
2218 C  CA  B GLY   A 103 ? 0.3201 0.3071 0.2103 0.0619  -0.0001 0.0458  103 GLY   A CA  
2219 C  C   A GLY   A 103 ? 0.3210 0.4421 0.2653 -0.0136 0.0130  0.0460  103 GLY   A C   
2220 C  C   B GLY   A 103 ? 0.3016 0.3081 0.1948 0.0677  -0.0193 0.0419  103 GLY   A C   
2221 O  O   A GLY   A 103 ? 0.3286 0.4490 0.2951 -0.0048 0.0069  0.0304  103 GLY   A O   
2222 O  O   B GLY   A 103 ? 0.3100 0.3107 0.1896 0.0741  -0.0191 0.0435  103 GLY   A O   
2229 N  N   A GLU   A 104 ? 0.3087 0.4411 0.2377 -0.0218 0.0331  0.0416  104 GLU   A N   
2230 N  N   B GLU   A 104 ? 0.2724 0.3013 0.1761 0.0615  -0.0297 0.0451  104 GLU   A N   
2231 C  CA  A GLU   A 104 ? 0.2948 0.4360 0.2261 -0.0323 0.0459  0.0358  104 GLU   A CA  
2232 C  CA  B GLU   A 104 ? 0.2493 0.2956 0.1538 0.0450  -0.0305 0.0413  104 GLU   A CA  
2233 C  C   A GLU   A 104 ? 0.2991 0.4419 0.2368 -0.0274 0.0414  0.0127  104 GLU   A C   
2234 C  C   B GLU   A 104 ? 0.2345 0.2852 0.1538 0.0541  -0.0233 0.0222  104 GLU   A C   
2235 O  O   A GLU   A 104 ? 0.2976 0.4423 0.2543 -0.0290 0.0374  0.0055  104 GLU   A O   
2236 O  O   B GLU   A 104 ? 0.2283 0.2766 0.1971 0.0511  -0.0203 0.0174  104 GLU   A O   
2237 C  CB  A GLU   A 104 ? 0.2743 0.4229 0.2133 -0.0489 0.0552  0.0587  104 GLU   A CB  
2238 C  CB  B GLU   A 104 ? 0.2451 0.2995 0.1507 0.0236  -0.0265 0.0594  104 GLU   A CB  
2239 C  CG  A GLU   A 104 ? 0.2559 0.4091 0.2263 -0.0618 0.0456  0.0741  104 GLU   A CG  
2240 C  CG  B GLU   A 104 ? 0.2432 0.3083 0.1714 0.0085  -0.0388 0.0689  104 GLU   A CG  
2241 C  CD  A GLU   A 104 ? 0.2315 0.3960 0.2227 -0.0775 0.0407  0.0912  104 GLU   A CD  
2242 C  CD  B GLU   A 104 ? 0.2398 0.3156 0.1725 0.0019  -0.0620 0.0740  104 GLU   A CD  
2243 O  OE1 A GLU   A 104 ? 0.2164 0.3739 0.1826 -0.0748 0.0277  0.1007  104 GLU   A OE1 
2244 O  OE1 B GLU   A 104 ? 0.2347 0.3203 0.1696 0.0033  -0.0701 0.0662  104 GLU   A OE1 
2245 O  OE2 A GLU   A 104 ? 0.2374 0.3954 0.2619 -0.0844 0.0398  0.0972  104 GLU   A OE2 
2246 O  OE2 B GLU   A 104 ? 0.2488 0.3223 0.1869 -0.0089 -0.0633 0.0747  104 GLU   A OE2 
2259 N  N   A ASP   A 105 ? 0.3021 0.4460 0.2375 -0.0185 0.0441  -0.0084 105 ASP   A N   
2260 N  N   B ASP   A 105 ? 0.2373 0.2852 0.1630 0.0585  -0.0153 0.0091  105 ASP   A N   
2261 C  CA  A ASP   A 105 ? 0.3008 0.4494 0.2531 -0.0094 0.0439  -0.0359 105 ASP   A CA  
2262 C  CA  B ASP   A 105 ? 0.2456 0.2855 0.1971 0.0634  -0.0028 -0.0189 105 ASP   A CA  
2263 C  C   A ASP   A 105 ? 0.2741 0.4382 0.2267 -0.0230 0.0358  -0.0561 105 ASP   A C   
2264 C  C   B ASP   A 105 ? 0.2465 0.2705 0.1703 0.0583  -0.0021 -0.0208 105 ASP   A C   
2265 O  O   A ASP   A 105 ? 0.2630 0.4391 0.1836 -0.0232 0.0399  -0.0756 105 ASP   A O   
2266 O  O   B ASP   A 105 ? 0.2411 0.2573 0.1206 0.0664  -0.0045 -0.0089 105 ASP   A O   
2267 C  CB  A ASP   A 105 ? 0.3216 0.4602 0.3010 0.0099  0.0501  -0.0433 105 ASP   A CB  
2268 C  CB  B ASP   A 105 ? 0.2492 0.2964 0.2561 0.0741  0.0073  -0.0407 105 ASP   A CB  
2269 C  CG  A ASP   A 105 ? 0.3410 0.4690 0.3504 0.0234  0.0518  -0.0528 105 ASP   A CG  
2270 C  CG  B ASP   A 105 ? 0.2547 0.3030 0.3036 0.0815  0.0089  -0.0572 105 ASP   A CG  
2271 O  OD1 A ASP   A 105 ? 0.3471 0.4738 0.3600 0.0255  0.0512  -0.0620 105 ASP   A OD1 
2272 O  OD1 B ASP   A 105 ? 0.2622 0.3032 0.3034 0.0773  0.0091  -0.0711 105 ASP   A OD1 
2273 O  OD2 A ASP   A 105 ? 0.3528 0.4717 0.3812 0.0316  0.0526  -0.0506 105 ASP   A OD2 
2274 O  OD2 B ASP   A 105 ? 0.2513 0.3059 0.3363 0.0892  0.0112  -0.0542 105 ASP   A OD2 
2283 N  N   A ILE   A 106 ? 0.2567 0.4216 0.2449 -0.0367 0.0066  -0.0671 106 ILE   A N   
2284 N  N   B ILE   A 106 ? 0.2545 0.2708 0.1997 0.0467  -0.0155 -0.0195 106 ILE   A N   
2285 C  CA  A ILE   A 106 ? 0.2343 0.4010 0.2513 -0.0534 -0.0159 -0.0803 106 ILE   A CA  
2286 C  CA  B ILE   A 106 ? 0.2643 0.2756 0.2322 0.0260  -0.0147 -0.0213 106 ILE   A CA  
2287 C  C   A ILE   A 106 ? 0.2201 0.3698 0.2571 -0.0734 -0.0137 -0.1092 106 ILE   A C   
2288 C  C   B ILE   A 106 ? 0.2679 0.2711 0.2294 0.0112  -0.0087 -0.0109 106 ILE   A C   
2289 O  O   A ILE   A 106 ? 0.1980 0.3549 0.2499 -0.0859 -0.0011 -0.1181 106 ILE   A O   
2290 O  O   B ILE   A 106 ? 0.2613 0.2707 0.2290 0.0071  0.0027  -0.0069 106 ILE   A O   
2291 C  CB  A ILE   A 106 ? 0.2326 0.4098 0.2778 -0.0440 -0.0358 -0.0509 106 ILE   A CB  
2292 C  CB  B ILE   A 106 ? 0.2797 0.2948 0.2826 0.0145  -0.0139 -0.0140 106 ILE   A CB  
2293 C  CG1 A ILE   A 106 ? 0.2107 0.4129 0.2986 -0.0337 -0.0399 -0.0257 106 ILE   A CG1 
2294 C  CG1 B ILE   A 106 ? 0.2875 0.3076 0.3146 0.0093  -0.0020 -0.0033 106 ILE   A CG1 
2295 C  CG2 A ILE   A 106 ? 0.2457 0.4115 0.2855 -0.0428 -0.0388 -0.0464 106 ILE   A CG2 
2296 C  CG2 B ILE   A 106 ? 0.2860 0.2992 0.2963 0.0097  -0.0142 -0.0152 106 ILE   A CG2 
2297 C  CD1 A ILE   A 106 ? 0.2035 0.4123 0.3101 -0.0223 -0.0392 -0.0198 106 ILE   A CD1 
2298 C  CD1 B ILE   A 106 ? 0.2941 0.3101 0.3292 0.0100  0.0064  -0.0087 106 ILE   A CD1 
2321 N  N   A GLN   A 107 ? 0.2369 0.3499 0.2854 -0.0726 -0.0070 -0.1286 107 GLN   A N   
2322 N  N   B GLN   A 107 ? 0.2784 0.2632 0.2456 0.0052  -0.0055 -0.0066 107 GLN   A N   
2323 C  CA  A GLN   A 107 ? 0.2546 0.3267 0.3426 -0.0603 0.0157  -0.1281 107 GLN   A CA  
2324 C  CA  B GLN   A 107 ? 0.2918 0.2652 0.3022 0.0005  0.0033  -0.0018 107 GLN   A CA  
2325 C  C   A GLN   A 107 ? 0.2258 0.2814 0.3269 -0.0506 0.0472  -0.1039 107 GLN   A C   
2326 C  C   B GLN   A 107 ? 0.2670 0.2347 0.2802 0.0026  0.0195  0.0052  107 GLN   A C   
2327 O  O   A GLN   A 107 ? 0.2305 0.2764 0.3863 -0.0470 0.0619  -0.0966 107 GLN   A O   
2328 O  O   B GLN   A 107 ? 0.2712 0.2371 0.3040 -0.0016 0.0142  0.0037  107 GLN   A O   
2329 C  CB  A GLN   A 107 ? 0.2963 0.3486 0.4222 -0.0620 0.0006  -0.1282 107 GLN   A CB  
2330 C  CB  B GLN   A 107 ? 0.3247 0.3009 0.3708 -0.0088 -0.0124 -0.0044 107 GLN   A CB  
2331 C  CG  A GLN   A 107 ? 0.3379 0.3729 0.5121 -0.0590 -0.0105 -0.1148 107 GLN   A CG  
2332 C  CG  B GLN   A 107 ? 0.3541 0.3378 0.4414 -0.0130 -0.0263 0.0010  107 GLN   A CG  
2333 C  CD  A GLN   A 107 ? 0.3649 0.3921 0.5884 -0.0574 -0.0183 -0.1001 107 GLN   A CD  
2334 C  CD  B GLN   A 107 ? 0.3772 0.3637 0.5003 -0.0149 -0.0356 0.0074  107 GLN   A CD  
2335 O  OE1 A GLN   A 107 ? 0.3776 0.4027 0.6205 -0.0530 -0.0210 -0.0926 107 GLN   A OE1 
2336 O  OE1 B GLN   A 107 ? 0.3850 0.3798 0.5246 -0.0143 -0.0386 0.0112  107 GLN   A OE1 
2337 N  NE2 A GLN   A 107 ? 0.3828 0.3984 0.6150 -0.0602 -0.0230 -0.0992 107 GLN   A NE2 
2338 N  NE2 B GLN   A 107 ? 0.3862 0.3748 0.5226 -0.0149 -0.0425 0.0076  107 GLN   A NE2 
2355 N  N   A LEU   A 108 ? 0.1935 0.2373 0.2628 -0.0483 0.0463  -0.0912 108 LEU   A N   
2356 N  N   B LEU   A 108 ? 0.2398 0.2098 0.2438 0.0011  0.0261  0.0060  108 LEU   A N   
2357 C  CA  A LEU   A 108 ? 0.1796 0.2001 0.2190 -0.0321 0.0337  -0.0453 108 LEU   A CA  
2358 C  CA  B LEU   A 108 ? 0.2156 0.1903 0.2173 0.0071  0.0275  0.0051  108 LEU   A CA  
2359 C  C   A LEU   A 108 ? 0.1616 0.1580 0.1950 -0.0156 0.0298  -0.0101 108 LEU   A C   
2360 C  C   B LEU   A 108 ? 0.1814 0.1602 0.1978 0.0053  0.0297  0.0105  108 LEU   A C   
2361 O  O   A LEU   A 108 ? 0.1605 0.1555 0.2164 -0.0068 0.0308  -0.0033 108 LEU   A O   
2362 O  O   B LEU   A 108 ? 0.1787 0.1592 0.2139 0.0129  0.0378  0.0091  108 LEU   A O   
2363 C  CB  A LEU   A 108 ? 0.1836 0.2133 0.2100 -0.0367 0.0388  -0.0383 108 LEU   A CB  
2364 C  CB  B LEU   A 108 ? 0.2242 0.2065 0.2104 0.0085  0.0305  0.0015  108 LEU   A CB  
2365 C  CG  A LEU   A 108 ? 0.1910 0.2353 0.2293 -0.0299 0.0573  -0.0296 108 LEU   A CG  
2366 C  CG  B LEU   A 108 ? 0.2319 0.2230 0.2273 0.0163  0.0377  0.0005  108 LEU   A CG  
2367 C  CD1 A LEU   A 108 ? 0.1988 0.2429 0.2333 -0.0392 0.0634  -0.0218 108 LEU   A CD1 
2368 C  CD1 B LEU   A 108 ? 0.2397 0.2292 0.2284 0.0129  0.0389  0.0031  108 LEU   A CD1 
2369 C  CD2 A LEU   A 108 ? 0.1946 0.2498 0.2640 -0.0226 0.0674  -0.0157 108 LEU   A CD2 
2370 C  CD2 B LEU   A 108 ? 0.2342 0.2363 0.2508 0.0224  0.0429  0.0042  108 LEU   A CD2 
2393 N  N   . LEU   A 109 ? 0.1593 0.1551 0.1996 0.0016  0.0264  0.0074  109 LEU   A N   
2394 C  CA  . LEU   A 109 ? 0.1541 0.1465 0.1874 0.0025  0.0124  0.0116  109 LEU   A CA  
2395 C  C   . LEU   A 109 ? 0.1391 0.1395 0.1897 0.0001  0.0194  -0.0055 109 LEU   A C   
2396 O  O   . LEU   A 109 ? 0.1468 0.1357 0.2042 -0.0043 0.0121  -0.0051 109 LEU   A O   
2397 C  CB  . LEU   A 109 ? 0.1547 0.1484 0.2049 0.0118  0.0092  0.0244  109 LEU   A CB  
2398 C  CG  . LEU   A 109 ? 0.1535 0.1554 0.2166 0.0073  0.0121  0.0267  109 LEU   A CG  
2399 C  CD1 . LEU   A 109 ? 0.1539 0.1475 0.2309 -0.0003 0.0215  0.0007  109 LEU   A CD1 
2400 C  CD2 . LEU   A 109 ? 0.1501 0.1806 0.2406 0.0037  0.0100  0.0368  109 LEU   A CD2 
2413 N  N   . LYS   A 110 ? 0.1471 0.1412 0.1847 -0.0006 0.0069  -0.0023 110 LYS   A N   
2414 C  CA  . LYS   A 110 ? 0.1475 0.1387 0.1959 -0.0050 -0.0008 0.0063  110 LYS   A CA  
2415 C  C   . LYS   A 110 ? 0.1439 0.1283 0.1862 -0.0049 0.0086  -0.0058 110 LYS   A C   
2416 O  O   . LYS   A 110 ? 0.1391 0.1318 0.1959 -0.0057 0.0132  -0.0070 110 LYS   A O   
2417 C  CB  . LYS   A 110 ? 0.1553 0.1477 0.2129 -0.0054 -0.0012 -0.0028 110 LYS   A CB  
2418 C  CG  . LYS   A 110 ? 0.1530 0.1418 0.2267 -0.0007 -0.0037 -0.0066 110 LYS   A CG  
2419 C  CD  . LYS   A 110 ? 0.1564 0.1493 0.2477 -0.0047 0.0015  -0.0155 110 LYS   A CD  
2420 C  CE  . LYS   A 110 ? 0.1652 0.1496 0.2653 -0.0102 0.0101  -0.0205 110 LYS   A CE  
2421 N  NZ  . LYS   A 110 ? 0.1604 0.1499 0.2673 -0.0187 0.0170  -0.0104 110 LYS   A NZ  
2435 N  N   . SER   A 111 ? 0.1445 0.1288 0.1884 -0.0005 0.0009  -0.0060 111 SER   A N   
2436 C  CA  . SER   A 111 ? 0.1409 0.1402 0.1865 -0.0033 0.0088  -0.0022 111 SER   A CA  
2437 C  C   . SER   A 111 ? 0.1329 0.1324 0.1777 -0.0083 0.0100  0.0049  111 SER   A C   
2438 O  O   . SER   A 111 ? 0.1475 0.1270 0.1975 -0.0024 0.0081  0.0015  111 SER   A O   
2439 C  CB  . SER   A 111 ? 0.1549 0.1661 0.1885 -0.0041 0.0115  -0.0165 111 SER   A CB  
2440 O  OG  . SER   A 111 ? 0.2023 0.1843 0.1863 0.0063  0.0144  -0.0240 111 SER   A OG  
2446 N  N   . ALA   A 112 ? 0.1384 0.1286 0.1806 0.0009  0.0172  0.0139  112 ALA   A N   
2447 C  CA  . ALA   A 112 ? 0.1505 0.1224 0.1677 -0.0042 0.0238  0.0103  112 ALA   A CA  
2448 C  C   . ALA   A 112 ? 0.1343 0.1190 0.1797 0.0040  0.0074  0.0054  112 ALA   A C   
2449 O  O   . ALA   A 112 ? 0.1378 0.1293 0.1812 -0.0099 0.0137  0.0071  112 ALA   A O   
2450 C  CB  . ALA   A 112 ? 0.1550 0.1285 0.1760 0.0008  0.0121  0.0183  112 ALA   A CB  
2456 N  N   . TYR   A 113 ? 0.1250 0.1228 0.1871 -0.0051 0.0051  0.0101  113 TYR   A N   
2457 C  CA  . TYR   A 113 ? 0.1279 0.1245 0.1787 -0.0042 0.0119  0.0175  113 TYR   A CA  
2458 C  C   . TYR   A 113 ? 0.1247 0.1260 0.1609 -0.0098 0.0168  0.0167  113 TYR   A C   
2459 O  O   . TYR   A 113 ? 0.1360 0.1271 0.1854 0.0001  0.0271  0.0094  113 TYR   A O   
2460 C  CB  . TYR   A 113 ? 0.1266 0.1330 0.1831 -0.0041 0.0020  0.0222  113 TYR   A CB  
2461 C  CG  . TYR   A 113 ? 0.1299 0.1367 0.1767 -0.0111 0.0182  0.0206  113 TYR   A CG  
2462 C  CD1 . TYR   A 113 ? 0.1348 0.1487 0.1777 -0.0017 0.0171  0.0240  113 TYR   A CD1 
2463 C  CD2 . TYR   A 113 ? 0.1348 0.1426 0.1618 -0.0146 0.0118  0.0141  113 TYR   A CD2 
2464 C  CE1 . TYR   A 113 ? 0.1376 0.1614 0.1863 0.0051  0.0151  0.0156  113 TYR   A CE1 
2465 C  CE2 . TYR   A 113 ? 0.1339 0.1520 0.1781 -0.0091 0.0045  0.0223  113 TYR   A CE2 
2466 C  CZ  . TYR   A 113 ? 0.1315 0.1532 0.1854 0.0034  0.0116  0.0272  113 TYR   A CZ  
2467 O  OH  . TYR   A 113 ? 0.1323 0.1547 0.2137 0.0073  0.0091  0.0155  113 TYR   A OH  
2477 N  N   . GLU   A 114 ? 0.1274 0.1242 0.1739 -0.0002 0.0178  0.0137  114 GLU   A N   
2478 C  CA  . GLU   A 114 ? 0.1303 0.1159 0.2058 0.0015  0.0101  0.0143  114 GLU   A CA  
2479 C  C   . GLU   A 114 ? 0.1266 0.1170 0.2073 -0.0042 0.0170  0.0138  114 GLU   A C   
2480 O  O   . GLU   A 114 ? 0.1431 0.1194 0.2012 -0.0005 0.0148  0.0163  114 GLU   A O   
2481 C  CB  . GLU   A 114 ? 0.1288 0.1187 0.2049 -0.0056 0.0143  0.0082  114 GLU   A CB  
2482 C  CG  . GLU   A 114 ? 0.1358 0.1251 0.2154 -0.0044 0.0202  0.0041  114 GLU   A CG  
2483 C  CD  . GLU   A 114 ? 0.1428 0.1287 0.2167 0.0003  0.0126  -0.0040 114 GLU   A CD  
2484 O  OE1 . GLU   A 114 ? 0.1457 0.1302 0.2227 -0.0078 0.0160  -0.0095 114 GLU   A OE1 
2485 O  OE2 . GLU   A 114 ? 0.1710 0.1381 0.2330 -0.0080 0.0105  -0.0216 114 GLU   A OE2 
2492 N  N   . ASN   A 115 ? 0.1269 0.1258 0.1822 -0.0056 0.0120  0.0100  115 ASN   A N   
2493 C  CA  . ASN   A 115 ? 0.1331 0.1281 0.1815 -0.0105 0.0158  0.0114  115 ASN   A CA  
2494 C  C   . ASN   A 115 ? 0.1368 0.1284 0.1718 -0.0135 0.0048  0.0095  115 ASN   A C   
2495 O  O   . ASN   A 115 ? 0.1393 0.1397 0.1777 -0.0093 0.0148  0.0173  115 ASN   A O   
2496 C  CB  . ASN   A 115 ? 0.1434 0.1366 0.1768 -0.0107 0.0149  0.0141  115 ASN   A CB  
2497 C  CG  . ASN   A 115 ? 0.1393 0.1496 0.1942 -0.0126 0.0195  0.0075  115 ASN   A CG  
2498 O  OD1 . ASN   A 115 ? 0.1432 0.2380 0.2182 -0.0075 0.0237  0.0231  115 ASN   A OD1 
2499 N  ND2 . ASN   A 115 ? 0.1407 0.1346 0.1862 -0.0108 0.0297  0.0101  115 ASN   A ND2 
2506 N  N   . PHE   A 116 ? 0.1261 0.1295 0.1819 -0.0022 0.0119  0.0196  116 PHE   A N   
2507 C  CA  . PHE   A 116 ? 0.1280 0.1358 0.1750 -0.0003 0.0145  0.0235  116 PHE   A CA  
2508 C  C   . PHE   A 116 ? 0.1301 0.1414 0.1816 -0.0102 0.0156  0.0278  116 PHE   A C   
2509 O  O   . PHE   A 116 ? 0.1322 0.1472 0.1895 0.0047  0.0168  0.0318  116 PHE   A O   
2510 C  CB  . PHE   A 116 ? 0.1333 0.1309 0.1944 -0.0051 0.0170  0.0230  116 PHE   A CB  
2511 C  CG  . PHE   A 116 ? 0.1321 0.1297 0.1709 -0.0012 0.0172  0.0214  116 PHE   A CG  
2512 C  CD1 . PHE   A 116 ? 0.1363 0.1270 0.1828 0.0010  0.0046  0.0107  116 PHE   A CD1 
2513 C  CD2 . PHE   A 116 ? 0.1360 0.1374 0.1909 -0.0043 0.0275  0.0204  116 PHE   A CD2 
2514 C  CE1 . PHE   A 116 ? 0.1400 0.1277 0.1908 -0.0108 0.0041  0.0078  116 PHE   A CE1 
2515 C  CE2 . PHE   A 116 ? 0.1381 0.1326 0.1961 0.0014  0.0238  0.0145  116 PHE   A CE2 
2516 C  CZ  . PHE   A 116 ? 0.1390 0.1222 0.1788 0.0062  0.0067  0.0125  116 PHE   A CZ  
2526 N  N   . ASN   A 117 ? 0.1310 0.1338 0.1905 -0.0072 0.0163  0.0242  117 ASN   A N   
2527 C  CA  . ASN   A 117 ? 0.1355 0.1341 0.2136 -0.0001 0.0250  0.0270  117 ASN   A CA  
2528 C  C   . ASN   A 117 ? 0.1373 0.1406 0.2185 0.0018  0.0260  0.0247  117 ASN   A C   
2529 O  O   . ASN   A 117 ? 0.1460 0.1442 0.2345 -0.0055 0.0044  0.0388  117 ASN   A O   
2530 C  CB  . ASN   A 117 ? 0.1304 0.1336 0.2132 -0.0017 0.0133  0.0360  117 ASN   A CB  
2531 C  CG  . ASN   A 117 ? 0.1355 0.1365 0.2144 0.0016  0.0131  0.0390  117 ASN   A CG  
2532 O  OD1 . ASN   A 117 ? 0.1357 0.1548 0.2189 -0.0097 0.0099  0.0239  117 ASN   A OD1 
2533 N  ND2 . ASN   A 117 ? 0.1286 0.1310 0.2056 -0.0061 0.0121  0.0290  117 ASN   A ND2 
2540 N  N   . GLN   A 118 ? 0.1291 0.1380 0.2239 -0.0044 0.0131  0.0325  118 GLN   A N   
2541 C  CA  . GLN   A 118 ? 0.1357 0.1511 0.2275 -0.0093 0.0068  0.0311  118 GLN   A CA  
2542 C  C   . GLN   A 118 ? 0.1403 0.1591 0.2163 -0.0147 0.0060  0.0409  118 GLN   A C   
2543 O  O   . GLN   A 118 ? 0.1375 0.1820 0.2451 -0.0038 -0.0074 0.0150  118 GLN   A O   
2544 C  CB  . GLN   A 118 ? 0.1324 0.1465 0.2407 -0.0013 0.0202  0.0158  118 GLN   A CB  
2545 C  CG  . GLN   A 118 ? 0.1362 0.1487 0.2325 0.0003  0.0167  0.0214  118 GLN   A CG  
2546 C  CD  . GLN   A 118 ? 0.1366 0.1576 0.2471 0.0010  0.0110  0.0271  118 GLN   A CD  
2547 O  OE1 . GLN   A 118 ? 0.1397 0.1701 0.2551 0.0088  0.0086  0.0211  118 GLN   A OE1 
2548 N  NE2 . GLN   A 118 ? 0.1372 0.1557 0.2473 0.0045  0.0049  0.0299  118 GLN   A NE2 
2557 N  N   . HIS   A 119 ? 0.1444 0.1519 0.2023 -0.0050 0.0014  0.0376  119 HIS   A N   
2558 C  CA  . HIS   A 119 ? 0.1479 0.1619 0.1998 -0.0029 0.0053  0.0405  119 HIS   A CA  
2559 C  C   . HIS   A 119 ? 0.1618 0.1713 0.1995 -0.0110 0.0118  0.0567  119 HIS   A C   
2560 O  O   . HIS   A 119 ? 0.1613 0.1761 0.2027 -0.0207 -0.0040 0.0419  119 HIS   A O   
2561 C  CB  . HIS   A 119 ? 0.1527 0.1587 0.2147 -0.0052 0.0216  0.0335  119 HIS   A CB  
2562 C  CG  . HIS   A 119 ? 0.1541 0.1631 0.2476 0.0010  0.0207  0.0392  119 HIS   A CG  
2563 N  ND1 . HIS   A 119 ? 0.1679 0.1795 0.2997 -0.0080 0.0217  0.0271  119 HIS   A ND1 
2564 C  CD2 . HIS   A 119 ? 0.1627 0.1784 0.2605 0.0166  0.0466  0.0576  119 HIS   A CD2 
2565 C  CE1 . HIS   A 119 ? 0.1691 0.1780 0.3157 -0.0066 0.0329  0.0531  119 HIS   A CE1 
2566 N  NE2 . HIS   A 119 ? 0.1735 0.1819 0.2985 0.0055  0.0555  0.0744  119 HIS   A NE2 
2574 N  N   A GLU   A 120 ? 0.1685 0.1859 0.1999 -0.0026 -0.0001 0.0750  120 GLU   A N   
2575 N  N   B GLU   A 120 ? 0.1812 0.1959 0.2130 -0.0065 0.0032  0.0675  120 GLU   A N   
2576 C  CA  A GLU   A 120 ? 0.1806 0.2054 0.2222 -0.0003 0.0012  0.1066  120 GLU   A CA  
2577 C  CA  B GLU   A 120 ? 0.2026 0.2226 0.2380 -0.0030 0.0045  0.0837  120 GLU   A CA  
2578 C  C   A GLU   A 120 ? 0.1586 0.1938 0.2053 -0.0116 0.0018  0.1017  120 GLU   A C   
2579 C  C   B GLU   A 120 ? 0.1918 0.2234 0.2203 -0.0065 0.0059  0.0712  120 GLU   A C   
2580 O  O   A GLU   A 120 ? 0.1588 0.1890 0.2051 -0.0128 -0.0053 0.1116  120 GLU   A O   
2581 O  O   B GLU   A 120 ? 0.1959 0.2305 0.2297 -0.0094 -0.0015 0.0624  120 GLU   A O   
2582 C  CB  A GLU   A 120 ? 0.2269 0.2472 0.2814 0.0070  0.0054  0.1368  120 GLU   A CB  
2583 C  CB  B GLU   A 120 ? 0.2410 0.2557 0.2963 0.0003  0.0086  0.1059  120 GLU   A CB  
2584 C  CG  A GLU   A 120 ? 0.2809 0.2890 0.3757 0.0239  0.0009  0.1273  120 GLU   A CG  
2585 C  CG  B GLU   A 120 ? 0.2852 0.2904 0.3778 0.0105  0.0059  0.0991  120 GLU   A CG  
2586 C  CD  A GLU   A 120 ? 0.3234 0.3201 0.4564 0.0379  0.0092  0.1146  120 GLU   A CD  
2587 C  CD  B GLU   A 120 ? 0.3178 0.3189 0.4484 0.0195  0.0096  0.0894  120 GLU   A CD  
2588 O  OE1 A GLU   A 120 ? 0.3403 0.3466 0.4809 0.0386  0.0100  0.1081  120 GLU   A OE1 
2589 O  OE1 B GLU   A 120 ? 0.3306 0.3366 0.4656 0.0205  0.0129  0.0872  120 GLU   A OE1 
2590 O  OE2 A GLU   A 120 ? 0.3468 0.3372 0.4975 0.0404  0.0108  0.1074  120 GLU   A OE2 
2591 O  OE2 B GLU   A 120 ? 0.3419 0.3342 0.4845 0.0200  0.0088  0.0853  120 GLU   A OE2 
2604 N  N   A VAL   A 121 ? 0.1523 0.1964 0.1733 -0.0152 0.0100  0.0884  121 VAL   A N   
2605 N  N   B VAL   A 121 ? 0.1847 0.2204 0.1905 -0.0046 0.0095  0.0644  121 VAL   A N   
2606 C  CA  A VAL   A 121 ? 0.1658 0.2112 0.1641 -0.0147 0.0321  0.0809  121 VAL   A CA  
2607 C  CA  B VAL   A 121 ? 0.1857 0.2251 0.1776 -0.0015 0.0195  0.0588  121 VAL   A CA  
2608 C  C   A VAL   A 121 ? 0.1603 0.1954 0.1512 -0.0192 0.0189  0.0493  121 VAL   A C   
2609 C  C   B VAL   A 121 ? 0.1677 0.2003 0.1548 -0.0078 0.0139  0.0446  121 VAL   A C   
2610 O  O   A VAL   A 121 ? 0.1597 0.1928 0.1847 -0.0316 0.0049  0.0348  121 VAL   A O   
2611 O  O   B VAL   A 121 ? 0.1616 0.1920 0.1518 -0.0123 0.0103  0.0330  121 VAL   A O   
2612 C  CB  A VAL   A 121 ? 0.2029 0.2457 0.2062 -0.0066 0.0384  0.0870  121 VAL   A CB  
2613 C  CB  B VAL   A 121 ? 0.2149 0.2559 0.2162 0.0068  0.0216  0.0596  121 VAL   A CB  
2614 C  CG1 A VAL   A 121 ? 0.2073 0.2599 0.2020 -0.0041 0.0468  0.0925  121 VAL   A CG1 
2615 C  CG1 B VAL   A 121 ? 0.2184 0.2684 0.2197 0.0086  0.0260  0.0621  121 VAL   A CG1 
2616 C  CG2 A VAL   A 121 ? 0.2177 0.2580 0.2435 -0.0161 0.0349  0.0795  121 VAL   A CG2 
2617 C  CG2 B VAL   A 121 ? 0.2290 0.2670 0.2418 0.0069  0.0173  0.0515  121 VAL   A CG2 
2636 N  N   . LEU   A 122 ? 0.1547 0.1774 0.1617 -0.0176 0.0089  0.0470  122 LEU   A N   
2637 C  CA  . LEU   A 122 ? 0.1634 0.1581 0.1600 -0.0173 0.0256  0.0486  122 LEU   A CA  
2638 C  C   . LEU   A 122 ? 0.1521 0.1593 0.1636 -0.0233 0.0140  0.0364  122 LEU   A C   
2639 O  O   . LEU   A 122 ? 0.1498 0.1637 0.2064 -0.0247 0.0089  0.0378  122 LEU   A O   
2640 C  CB  . LEU   A 122 ? 0.1742 0.1579 0.1931 -0.0101 0.0097  0.0509  122 LEU   A CB  
2641 C  CG  . LEU   A 122 ? 0.1720 0.1618 0.1985 -0.0111 0.0221  0.0324  122 LEU   A CG  
2642 C  CD1 . LEU   A 122 ? 0.1893 0.1623 0.2127 -0.0107 0.0275  0.0352  122 LEU   A CD1 
2643 C  CD2 . LEU   A 122 ? 0.1677 0.1566 0.1746 -0.0069 0.0331  0.0274  122 LEU   A CD2 
2656 N  N   A LEU   A 123 ? 0.1510 0.1557 0.1596 -0.0263 0.0070  0.0404  123 LEU   A N   
2657 N  N   B LEU   A 123 ? 0.1522 0.1571 0.1600 -0.0174 0.0063  0.0287  123 LEU   A N   
2658 C  CA  A LEU   A 123 ? 0.1486 0.1530 0.1389 -0.0246 0.0081  0.0419  123 LEU   A CA  
2659 C  CA  B LEU   A 123 ? 0.1510 0.1542 0.1441 -0.0085 0.0051  0.0203  123 LEU   A CA  
2660 C  C   A LEU   A 123 ? 0.1425 0.1440 0.1466 -0.0179 0.0020  0.0383  123 LEU   A C   
2661 C  C   B LEU   A 123 ? 0.1492 0.1457 0.1185 -0.0073 0.0109  0.0189  123 LEU   A C   
2662 O  O   A LEU   A 123 ? 0.1309 0.1400 0.1614 -0.0202 0.0119  0.0233  123 LEU   A O   
2663 O  O   B LEU   A 123 ? 0.1467 0.1387 0.1223 -0.0126 0.0174  0.0082  123 LEU   A O   
2664 C  CB  A LEU   A 123 ? 0.1614 0.1633 0.1404 -0.0303 0.0294  0.0426  123 LEU   A CB  
2665 C  CB  B LEU   A 123 ? 0.1590 0.1644 0.1586 -0.0063 0.0037  0.0175  123 LEU   A CB  
2666 C  CG  A LEU   A 123 ? 0.1646 0.1778 0.1577 -0.0251 0.0341  0.0235  123 LEU   A CG  
2667 C  CG  B LEU   A 123 ? 0.1622 0.1750 0.1649 -0.0043 0.0003  0.0130  123 LEU   A CG  
2668 C  CD1 A LEU   A 123 ? 0.1687 0.1910 0.1688 -0.0169 0.0295  0.0112  123 LEU   A CD1 
2669 C  CD1 B LEU   A 123 ? 0.1643 0.1838 0.1888 0.0012  0.0054  0.0004  123 LEU   A CD1 
2670 C  CD2 A LEU   A 123 ? 0.1749 0.1799 0.1598 -0.0264 0.0272  0.0195  123 LEU   A CD2 
2671 C  CD2 B LEU   A 123 ? 0.1737 0.1797 0.1741 -0.0020 -0.0139 0.0111  123 LEU   A CD2 
2694 N  N   A ALA   A 124 ? 0.1416 0.1416 0.1318 -0.0198 0.0054  0.0392  124 ALA   A N   
2695 N  N   B ALA   A 124 ? 0.1485 0.1441 0.1170 -0.0026 0.0082  0.0142  124 ALA   A N   
2696 C  CA  A ALA   A 124 ? 0.1291 0.1348 0.1369 -0.0178 0.0114  0.0300  124 ALA   A CA  
2697 C  CA  B ALA   A 124 ? 0.1424 0.1446 0.1196 0.0024  -0.0042 0.0146  124 ALA   A CA  
2698 C  C   A ALA   A 124 ? 0.1286 0.1348 0.1287 -0.0113 0.0201  0.0252  124 ALA   A C   
2699 C  C   B ALA   A 124 ? 0.1489 0.1506 0.1335 0.0022  -0.0032 0.0169  124 ALA   A C   
2700 O  O   A ALA   A 124 ? 0.1228 0.1312 0.1447 -0.0145 0.0239  0.0173  124 ALA   A O   
2701 O  O   B ALA   A 124 ? 0.1504 0.1582 0.1476 -0.0035 0.0048  0.0231  124 ALA   A O   
2702 C  CB  A ALA   A 124 ? 0.1350 0.1349 0.1632 -0.0174 0.0160  0.0294  124 ALA   A CB  
2703 C  CB  B ALA   A 124 ? 0.1397 0.1414 0.1342 0.0121  -0.0063 0.0179  124 ALA   A CB  
2714 N  N   A PRO   A 125 ? 0.1236 0.1352 0.1447 -0.0164 0.0221  0.0281  125 PRO   A N   
2715 N  N   B PRO   A 125 ? 0.1468 0.1503 0.1332 0.0051  -0.0085 0.0271  125 PRO   A N   
2716 C  CA  A PRO   A 125 ? 0.1288 0.1339 0.1463 -0.0128 0.0175  0.0187  125 PRO   A CA  
2717 C  CA  B PRO   A 125 ? 0.1496 0.1489 0.1432 0.0047  -0.0111 0.0196  125 PRO   A CA  
2718 C  C   A PRO   A 125 ? 0.1266 0.1385 0.1460 -0.0083 0.0195  0.0205  125 PRO   A C   
2719 C  C   B PRO   A 125 ? 0.1429 0.1493 0.1477 0.0019  -0.0112 0.0175  125 PRO   A C   
2720 O  O   A PRO   A 125 ? 0.1366 0.1354 0.1679 -0.0033 0.0220  0.0155  125 PRO   A O   
2721 O  O   B PRO   A 125 ? 0.1422 0.1425 0.1696 0.0003  -0.0199 0.0127  125 PRO   A O   
2722 C  CB  A PRO   A 125 ? 0.1438 0.1307 0.1397 -0.0194 0.0230  0.0213  125 PRO   A CB  
2723 C  CB  B PRO   A 125 ? 0.1597 0.1490 0.1509 0.0053  -0.0043 0.0182  125 PRO   A CB  
2724 C  CG  A PRO   A 125 ? 0.1432 0.1346 0.1449 -0.0226 0.0163  0.0242  125 PRO   A CG  
2725 C  CG  B PRO   A 125 ? 0.1627 0.1532 0.1550 0.0020  -0.0019 0.0142  125 PRO   A CG  
2726 C  CD  A PRO   A 125 ? 0.1342 0.1419 0.1470 -0.0302 0.0253  0.0277  125 PRO   A CD  
2727 C  CD  B PRO   A 125 ? 0.1572 0.1578 0.1555 -0.0026 -0.0000 0.0228  125 PRO   A CD  
2742 N  N   A LEU   A 126 ? 0.1262 0.1549 0.1511 -0.0006 0.0221  0.0167  126 LEU   A N   
2743 N  N   B LEU   A 126 ? 0.1472 0.1621 0.1512 0.0013  -0.0061 0.0216  126 LEU   A N   
2744 C  CA  A LEU   A 126 ? 0.1320 0.1523 0.1573 -0.0085 0.0063  0.0245  126 LEU   A CA  
2745 C  CA  B LEU   A 126 ? 0.1469 0.1576 0.1591 -0.0032 -0.0101 0.0180  126 LEU   A CA  
2746 C  C   A LEU   A 126 ? 0.1382 0.1458 0.1578 -0.0049 -0.0012 0.0214  126 LEU   A C   
2747 C  C   B LEU   A 126 ? 0.1444 0.1452 0.1527 0.0049  -0.0044 0.0139  126 LEU   A C   
2748 O  O   A LEU   A 126 ? 0.1433 0.1341 0.1605 -0.0064 0.0079  0.0123  126 LEU   A O   
2749 O  O   B LEU   A 126 ? 0.1430 0.1372 0.1861 -0.0060 0.0113  0.0155  126 LEU   A O   
2750 C  CB  A LEU   A 126 ? 0.1418 0.1611 0.1735 -0.0124 0.0012  0.0277  126 LEU   A CB  
2751 C  CB  B LEU   A 126 ? 0.1581 0.1727 0.1847 -0.0125 -0.0078 0.0214  126 LEU   A CB  
2752 C  CG  A LEU   A 126 ? 0.1386 0.1840 0.1895 -0.0151 0.0025  0.0259  126 LEU   A CG  
2753 C  CG  B LEU   A 126 ? 0.1587 0.1821 0.2126 -0.0101 -0.0067 0.0256  126 LEU   A CG  
2754 C  CD1 A LEU   A 126 ? 0.1417 0.2032 0.1990 -0.0193 0.0095  0.0258  126 LEU   A CD1 
2755 C  CD1 B LEU   A 126 ? 0.1576 0.1908 0.2248 -0.0086 -0.0173 0.0308  126 LEU   A CD1 
2756 C  CD2 A LEU   A 126 ? 0.1541 0.1777 0.1804 -0.0308 0.0078  0.0419  126 LEU   A CD2 
2757 C  CD2 B LEU   A 126 ? 0.1672 0.1827 0.2262 -0.0209 0.0021  0.0242  126 LEU   A CD2 
2780 N  N   A LEU   A 127 ? 0.1309 0.1514 0.1535 -0.0034 0.0062  0.0250  127 LEU   A N   
2781 N  N   B LEU   A 127 ? 0.1478 0.1465 0.1472 0.0081  0.0046  0.0146  127 LEU   A N   
2782 C  CA  A LEU   A 127 ? 0.1341 0.1504 0.1454 -0.0033 0.0041  0.0145  127 LEU   A CA  
2783 C  CA  B LEU   A 127 ? 0.1442 0.1509 0.1463 0.0011  0.0032  0.0136  127 LEU   A CA  
2784 C  C   A LEU   A 127 ? 0.1421 0.1497 0.1230 0.0001  0.0055  0.0094  127 LEU   A C   
2785 C  C   B LEU   A 127 ? 0.1383 0.1492 0.1617 -0.0114 -0.0033 0.0071  127 LEU   A C   
2786 O  O   A LEU   A 127 ? 0.1476 0.1525 0.1356 -0.0025 -0.0050 0.0169  127 LEU   A O   
2787 O  O   B LEU   A 127 ? 0.1394 0.1481 0.1443 -0.0320 0.0022  0.0079  127 LEU   A O   
2788 C  CB  A LEU   A 127 ? 0.1362 0.1559 0.1700 0.0110  0.0125  0.0096  127 LEU   A CB  
2789 C  CB  B LEU   A 127 ? 0.1488 0.1732 0.1527 0.0020  0.0154  0.0170  127 LEU   A CB  
2790 C  CG  A LEU   A 127 ? 0.1378 0.1549 0.1670 0.0122  0.0052  0.0210  127 LEU   A CG  
2791 C  CG  B LEU   A 127 ? 0.1499 0.1957 0.1725 0.0050  0.0124  0.0252  127 LEU   A CG  
2792 C  CD1 A LEU   A 127 ? 0.1425 0.1465 0.1925 -0.0006 0.0037  0.0213  127 LEU   A CD1 
2793 C  CD1 B LEU   A 127 ? 0.1476 0.2065 0.1947 0.0082  0.0152  0.0232  127 LEU   A CD1 
2794 C  CD2 A LEU   A 127 ? 0.1473 0.1600 0.1957 0.0194  -0.0088 0.0235  127 LEU   A CD2 
2795 C  CD2 B LEU   A 127 ? 0.1607 0.2013 0.1819 0.0106  -0.0100 0.0252  127 LEU   A CD2 
2818 N  N   A SER   A 128 ? 0.1535 0.1456 0.1184 -0.0038 0.0018  0.0051  128 SER   A N   
2819 N  N   B SER   A 128 ? 0.1389 0.1447 0.1675 -0.0153 -0.0029 0.0077  128 SER   A N   
2820 C  CA  A SER   A 128 ? 0.1531 0.1428 0.1119 -0.0010 -0.0013 0.0085  128 SER   A CA  
2821 C  CA  B SER   A 128 ? 0.1425 0.1475 0.1700 -0.0109 0.0041  0.0075  128 SER   A CA  
2822 C  C   A SER   A 128 ? 0.1534 0.1520 0.1133 0.0021  0.0004  0.0146  128 SER   A C   
2823 C  C   B SER   A 128 ? 0.1560 0.1502 0.1596 -0.0033 -0.0009 0.0243  128 SER   A C   
2824 O  O   A SER   A 128 ? 0.1543 0.1636 0.1230 0.0048  0.0167  0.0071  128 SER   A O   
2825 O  O   B SER   A 128 ? 0.1696 0.1599 0.1739 0.0011  0.0004  0.0304  128 SER   A O   
2826 C  CB  A SER   A 128 ? 0.1557 0.1312 0.1246 0.0005  -0.0048 0.0187  128 SER   A CB  
2827 C  CB  B SER   A 128 ? 0.1400 0.1491 0.1859 -0.0085 0.0056  0.0115  128 SER   A CB  
2828 O  OG  A SER   A 128 ? 0.1577 0.1420 0.1405 0.0025  -0.0058 0.0121  128 SER   A OG  
2829 O  OG  B SER   A 128 ? 0.1309 0.1458 0.1827 -0.0010 0.0177  0.0150  128 SER   A OG  
2840 N  N   A ALA   A 129 ? 0.1484 0.1506 0.1150 -0.0002 0.0030  0.0182  129 ALA   A N   
2841 N  N   B ALA   A 129 ? 0.1590 0.1505 0.1703 0.0013  -0.0033 0.0228  129 ALA   A N   
2842 C  CA  A ALA   A 129 ? 0.1432 0.1511 0.1312 0.0042  0.0092  0.0217  129 ALA   A CA  
2843 C  CA  B ALA   A 129 ? 0.1666 0.1507 0.1932 0.0003  -0.0021 0.0068  129 ALA   A CA  
2844 C  C   A ALA   A 129 ? 0.1516 0.1472 0.1255 0.0042  0.0098  0.0024  129 ALA   A C   
2845 C  C   B ALA   A 129 ? 0.1799 0.1546 0.1733 0.0043  -0.0027 0.0129  129 ALA   A C   
2846 O  O   A ALA   A 129 ? 0.1606 0.1462 0.1359 0.0015  -0.0006 0.0216  129 ALA   A O   
2847 O  O   B ALA   A 129 ? 0.1803 0.1571 0.1640 -0.0030 0.0000  0.0179  129 ALA   A O   
2848 C  CB  A ALA   A 129 ? 0.1358 0.1595 0.1659 0.0079  0.0136  0.0256  129 ALA   A CB  
2849 C  CB  B ALA   A 129 ? 0.1743 0.1566 0.2425 -0.0007 0.0141  0.0072  129 ALA   A CB  
2860 N  N   A GLY   A 130 ? 0.1633 0.1471 0.1540 0.0070  0.0051  -0.0049 130 GLY   A N   
2861 N  N   B GLY   A 130 ? 0.1956 0.1564 0.1594 0.0084  -0.0038 0.0108  130 GLY   A N   
2862 C  CA  A GLY   A 130 ? 0.1711 0.1493 0.1768 0.0069  -0.0024 -0.0009 130 GLY   A CA  
2863 C  CA  B GLY   A 130 ? 0.2123 0.1611 0.1665 0.0073  -0.0169 0.0091  130 GLY   A CA  
2864 C  C   A GLY   A 130 ? 0.1622 0.1437 0.1835 0.0084  -0.0106 0.0026  130 GLY   A C   
2865 C  C   B GLY   A 130 ? 0.2171 0.1627 0.1661 0.0017  -0.0328 0.0162  130 GLY   A C   
2866 O  O   A GLY   A 130 ? 0.1581 0.1444 0.1760 0.0118  -0.0055 0.0087  130 GLY   A O   
2867 O  O   B GLY   A 130 ? 0.2135 0.1650 0.1797 -0.0005 -0.0386 0.0138  130 GLY   A O   
2874 N  N   A ILE   A 131 ? 0.1658 0.1442 0.1883 -0.0077 -0.0246 0.0133  131 ILE   A N   
2875 N  N   B ILE   A 131 ? 0.2237 0.1620 0.1679 -0.0088 -0.0331 0.0328  131 ILE   A N   
2876 C  CA  A ILE   A 131 ? 0.1811 0.1500 0.1739 -0.0126 -0.0438 0.0138  131 ILE   A CA  
2877 C  CA  B ILE   A 131 ? 0.2184 0.1604 0.1687 -0.0154 -0.0378 0.0260  131 ILE   A CA  
2878 C  C   A ILE   A 131 ? 0.1725 0.1546 0.1812 -0.0114 -0.0246 0.0181  131 ILE   A C   
2879 C  C   B ILE   A 131 ? 0.2118 0.1538 0.1658 -0.0136 -0.0273 0.0317  131 ILE   A C   
2880 O  O   A ILE   A 131 ? 0.1840 0.1680 0.1936 -0.0126 -0.0138 0.0268  131 ILE   A O   
2881 O  O   B ILE   A 131 ? 0.2197 0.1429 0.1665 -0.0151 -0.0167 0.0255  131 ILE   A O   
2882 C  CB  A ILE   A 131 ? 0.1964 0.1671 0.1805 -0.0162 -0.0564 0.0018  131 ILE   A CB  
2883 C  CB  B ILE   A 131 ? 0.2168 0.1693 0.1745 -0.0185 -0.0355 0.0011  131 ILE   A CB  
2884 C  CG1 A ILE   A 131 ? 0.1944 0.2004 0.1934 -0.0175 -0.0515 -0.0061 131 ILE   A CG1 
2885 C  CG1 B ILE   A 131 ? 0.2212 0.1983 0.1982 -0.0257 -0.0306 -0.0086 131 ILE   A CG1 
2886 C  CG2 A ILE   A 131 ? 0.2072 0.1562 0.1904 -0.0118 -0.0456 0.0033  131 ILE   A CG2 
2887 C  CG2 B ILE   A 131 ? 0.2130 0.1505 0.1531 -0.0151 -0.0269 0.0024  131 ILE   A CG2 
2888 C  CD1 A ILE   A 131 ? 0.1951 0.2118 0.2193 -0.0168 -0.0542 -0.0163 131 ILE   A CD1 
2889 C  CD1 B ILE   A 131 ? 0.2251 0.2153 0.2208 -0.0209 -0.0272 -0.0121 131 ILE   A CD1 
2912 N  N   A PHE   A 132 ? 0.1628 0.1483 0.1804 -0.0078 -0.0250 0.0110  132 PHE   A N   
2913 N  N   B PHE   A 132 ? 0.2050 0.1618 0.1752 -0.0106 -0.0257 0.0339  132 PHE   A N   
2914 C  CA  A PHE   A 132 ? 0.1660 0.1542 0.1800 -0.0176 -0.0117 0.0033  132 PHE   A CA  
2915 C  CA  B PHE   A 132 ? 0.2030 0.1764 0.1871 -0.0084 -0.0240 0.0273  132 PHE   A CA  
2916 C  C   A PHE   A 132 ? 0.1689 0.1606 0.1714 -0.0215 -0.0095 0.0160  132 PHE   A C   
2917 C  C   B PHE   A 132 ? 0.2004 0.1887 0.1977 -0.0060 -0.0221 0.0282  132 PHE   A C   
2918 O  O   A PHE   A 132 ? 0.1783 0.1599 0.1745 -0.0315 -0.0023 0.0270  132 PHE   A O   
2919 O  O   B PHE   A 132 ? 0.2111 0.2012 0.1963 -0.0155 -0.0111 0.0388  132 PHE   A O   
2920 C  CB  A PHE   A 132 ? 0.1620 0.1448 0.1806 -0.0137 -0.0236 0.0097  132 PHE   A CB  
2921 C  CB  B PHE   A 132 ? 0.2006 0.1720 0.1667 -0.0075 -0.0177 0.0383  132 PHE   A CB  
2922 C  CG  A PHE   A 132 ? 0.1617 0.1378 0.1742 -0.0036 -0.0293 0.0078  132 PHE   A CG  
2923 C  CG  B PHE   A 132 ? 0.2022 0.1715 0.1571 0.0029  -0.0187 0.0320  132 PHE   A CG  
2924 C  CD1 A PHE   A 132 ? 0.1595 0.1432 0.1948 0.0079  -0.0326 0.0035  132 PHE   A CD1 
2925 C  CD1 B PHE   A 132 ? 0.2027 0.1764 0.1617 0.0082  -0.0218 0.0319  132 PHE   A CD1 
2926 C  CD2 A PHE   A 132 ? 0.1624 0.1524 0.1872 0.0072  -0.0374 0.0130  132 PHE   A CD2 
2927 C  CD2 B PHE   A 132 ? 0.2015 0.1781 0.1695 0.0110  -0.0194 0.0195  132 PHE   A CD2 
2928 C  CE1 A PHE   A 132 ? 0.1580 0.1553 0.2051 0.0082  -0.0397 -0.0026 132 PHE   A CE1 
2929 C  CE1 B PHE   A 132 ? 0.2020 0.1838 0.1688 0.0094  -0.0140 0.0185  132 PHE   A CE1 
2930 C  CE2 A PHE   A 132 ? 0.1602 0.1617 0.2079 0.0097  -0.0363 0.0060  132 PHE   A CE2 
2931 C  CE2 B PHE   A 132 ? 0.1997 0.1845 0.1843 0.0179  -0.0123 0.0075  132 PHE   A CE2 
2932 C  CZ  A PHE   A 132 ? 0.1568 0.1571 0.2122 0.0084  -0.0395 0.0052  132 PHE   A CZ  
2933 C  CZ  B PHE   A 132 ? 0.2001 0.1851 0.1790 0.0152  -0.0094 0.0070  132 PHE   A CZ  
2952 N  N   A GLY   A 133 ? 0.1698 0.1703 0.1653 -0.0167 -0.0191 0.0212  133 GLY   A N   
2953 N  N   B GLY   A 133 ? 0.1918 0.1876 0.1924 0.0019  -0.0277 0.0222  133 GLY   A N   
2954 C  CA  A GLY   A 133 ? 0.1783 0.1850 0.1648 -0.0222 -0.0169 0.0187  133 GLY   A CA  
2955 C  CA  B GLY   A 133 ? 0.1910 0.1867 0.1910 0.0018  -0.0281 -0.0005 133 GLY   A CA  
2956 C  C   A GLY   A 133 ? 0.1820 0.1977 0.1739 -0.0240 -0.0308 0.0088  133 GLY   A C   
2957 C  C   B GLY   A 133 ? 0.1875 0.1919 0.1959 -0.0044 -0.0293 -0.0148 133 GLY   A C   
2958 O  O   A GLY   A 133 ? 0.1849 0.2134 0.1982 -0.0277 -0.0480 0.0058  133 GLY   A O   
2959 O  O   B GLY   A 133 ? 0.1906 0.2015 0.2085 0.0003  -0.0418 -0.0157 133 GLY   A O   
2966 N  N   A ALA   A 134 ? 0.1863 0.1877 0.1593 -0.0174 -0.0065 0.0079  134 ALA   A N   
2967 N  N   B ALA   A 134 ? 0.1815 0.1842 0.1990 -0.0086 -0.0076 -0.0167 134 ALA   A N   
2968 C  CA  A ALA   A 134 ? 0.1801 0.1812 0.1606 -0.0120 -0.0077 0.0108  134 ALA   A CA  
2969 C  CA  B ALA   A 134 ? 0.1749 0.1818 0.1861 -0.0157 -0.0117 -0.0182 134 ALA   A CA  
2970 C  C   A ALA   A 134 ? 0.1810 0.1809 0.1611 -0.0048 -0.0038 0.0011  134 ALA   A C   
2971 C  C   B ALA   A 134 ? 0.1735 0.1852 0.1796 -0.0176 -0.0114 -0.0040 134 ALA   A C   
2972 O  O   A ALA   A 134 ? 0.1935 0.1859 0.1699 -0.0019 0.0069  -0.0042 134 ALA   A O   
2973 O  O   B ALA   A 134 ? 0.1808 0.1878 0.1704 -0.0226 -0.0135 -0.0007 134 ALA   A O   
2974 C  CB  A ALA   A 134 ? 0.1832 0.1783 0.1666 -0.0084 -0.0067 0.0090  134 ALA   A CB  
2975 C  CB  B ALA   A 134 ? 0.1779 0.1809 0.2074 -0.0113 -0.0050 -0.0277 134 ALA   A CB  
2986 N  N   A ASP   A 135 ? 0.1858 0.1771 0.1626 -0.0033 -0.0038 0.0078  135 ASP   A N   
2987 N  N   B ASP   A 135 ? 0.1721 0.1846 0.1870 -0.0107 -0.0116 0.0041  135 ASP   A N   
2988 C  CA  A ASP   A 135 ? 0.1858 0.1883 0.1786 -0.0082 -0.0170 0.0133  135 ASP   A CA  
2989 C  CA  B ASP   A 135 ? 0.1782 0.1904 0.1832 -0.0190 -0.0166 0.0072  135 ASP   A CA  
2990 C  C   A ASP   A 135 ? 0.1709 0.1780 0.1712 -0.0049 -0.0154 0.0154  135 ASP   A C   
2991 C  C   B ASP   A 135 ? 0.1696 0.1754 0.1751 -0.0111 -0.0123 0.0097  135 ASP   A C   
2992 O  O   A ASP   A 135 ? 0.1634 0.1739 0.1718 -0.0078 -0.0055 0.0208  135 ASP   A O   
2993 O  O   B ASP   A 135 ? 0.1592 0.1709 0.1964 -0.0109 -0.0091 0.0116  135 ASP   A O   
2994 C  CB  A ASP   A 135 ? 0.2073 0.2177 0.2149 -0.0208 -0.0313 0.0092  135 ASP   A CB  
2995 C  CB  B ASP   A 135 ? 0.1945 0.2134 0.2095 -0.0421 -0.0300 -0.0002 135 ASP   A CB  
2996 C  CG  A ASP   A 135 ? 0.2317 0.2459 0.2749 -0.0292 -0.0310 0.0071  135 ASP   A CG  
2997 C  CG  B ASP   A 135 ? 0.2104 0.2400 0.2458 -0.0631 -0.0404 -0.0101 135 ASP   A CG  
2998 O  OD1 A ASP   A 135 ? 0.2245 0.2495 0.2867 -0.0247 -0.0418 0.0104  135 ASP   A OD1 
2999 O  OD1 B ASP   A 135 ? 0.2044 0.2529 0.2620 -0.0692 -0.0407 -0.0161 135 ASP   A OD1 
3000 O  OD2 A ASP   A 135 ? 0.2566 0.2649 0.3252 -0.0324 -0.0177 0.0239  135 ASP   A OD2 
3001 O  OD2 B ASP   A 135 ? 0.2278 0.2551 0.2647 -0.0668 -0.0467 -0.0062 135 ASP   A OD2 
3010 N  N   A PRO   A 136 ? 0.1643 0.1730 0.1739 0.0022  -0.0140 0.0142  136 PRO   A N   
3011 N  N   B PRO   A 136 ? 0.1722 0.1683 0.1674 -0.0008 -0.0100 0.0138  136 PRO   A N   
3012 C  CA  A PRO   A 136 ? 0.1607 0.1752 0.1773 -0.0003 -0.0060 0.0055  136 PRO   A CA  
3013 C  CA  B PRO   A 136 ? 0.1725 0.1607 0.1700 -0.0047 -0.0083 0.0092  136 PRO   A CA  
3014 C  C   A PRO   A 136 ? 0.1434 0.1724 0.1709 0.0051  0.0013  0.0086  136 PRO   A C   
3015 C  C   B PRO   A 136 ? 0.1570 0.1587 0.1650 -0.0078 -0.0010 0.0034  136 PRO   A C   
3016 O  O   A PRO   A 136 ? 0.1321 0.1638 0.1624 0.0082  0.0125  0.0089  136 PRO   A O   
3017 O  O   B PRO   A 136 ? 0.1510 0.1647 0.1608 -0.0124 0.0106  0.0061  136 PRO   A O   
3018 C  CB  A PRO   A 136 ? 0.1777 0.1781 0.1837 0.0016  -0.0144 0.0058  136 PRO   A CB  
3019 C  CB  B PRO   A 136 ? 0.1896 0.1550 0.1779 0.0044  -0.0076 0.0200  136 PRO   A CB  
3020 C  CG  A PRO   A 136 ? 0.1919 0.1834 0.2090 0.0062  -0.0147 0.0039  136 PRO   A CG  
3021 C  CG  B PRO   A 136 ? 0.1925 0.1632 0.1717 0.0048  -0.0025 -0.0004 136 PRO   A CG  
3022 C  CD  A PRO   A 136 ? 0.1793 0.1762 0.1863 0.0051  -0.0068 0.0134  136 PRO   A CD  
3023 C  CD  B PRO   A 136 ? 0.1871 0.1682 0.1690 0.0070  -0.0025 0.0059  136 PRO   A CD  
3038 N  N   A ILE   A 137 ? 0.1475 0.1807 0.1923 -0.0007 -0.0075 0.0072  137 ILE   A N   
3039 N  N   B ILE   A 137 ? 0.1508 0.1637 0.1763 -0.0108 -0.0073 -0.0020 137 ILE   A N   
3040 C  CA  A ILE   A 137 ? 0.1533 0.1935 0.1898 -0.0095 -0.0088 0.0058  137 ILE   A CA  
3041 C  CA  B ILE   A 137 ? 0.1507 0.1718 0.1870 -0.0187 -0.0092 0.0101  137 ILE   A CA  
3042 C  C   A ILE   A 137 ? 0.1520 0.1873 0.1849 -0.0145 -0.0025 0.0023  137 ILE   A C   
3043 C  C   B ILE   A 137 ? 0.1496 0.1667 0.1821 -0.0161 -0.0071 0.0169  137 ILE   A C   
3044 O  O   A ILE   A 137 ? 0.1607 0.1848 0.1895 -0.0183 -0.0006 -0.0022 137 ILE   A O   
3045 O  O   B ILE   A 137 ? 0.1578 0.1606 0.1966 -0.0177 0.0012  0.0228  137 ILE   A O   
3046 C  CB  A ILE   A 137 ? 0.1651 0.2070 0.2186 -0.0145 -0.0303 -0.0032 137 ILE   A CB  
3047 C  CB  B ILE   A 137 ? 0.1601 0.1929 0.2111 -0.0122 -0.0129 -0.0002 137 ILE   A CB  
3048 C  CG1 A ILE   A 137 ? 0.1770 0.2310 0.2368 -0.0063 -0.0436 0.0005  137 ILE   A CG1 
3049 C  CG1 B ILE   A 137 ? 0.1755 0.2154 0.2327 -0.0035 -0.0193 -0.0051 137 ILE   A CG1 
3050 C  CG2 A ILE   A 137 ? 0.1737 0.2037 0.2283 -0.0210 -0.0378 -0.0133 137 ILE   A CG2 
3051 C  CG2 B ILE   A 137 ? 0.1666 0.1965 0.2139 -0.0158 -0.0150 -0.0142 137 ILE   A CG2 
3052 C  CD1 A ILE   A 137 ? 0.1934 0.2479 0.2518 -0.0017 -0.0381 -0.0045 137 ILE   A CD1 
3053 C  CD1 B ILE   A 137 ? 0.1929 0.2302 0.2504 0.0029  -0.0194 -0.0182 137 ILE   A CD1 
3076 N  N   A HIS   A 138 ? 0.1525 0.1952 0.1990 -0.0104 0.0102  -0.0023 138 HIS   A N   
3077 N  N   B HIS   A 138 ? 0.1444 0.1755 0.1755 -0.0138 -0.0067 0.0127  138 HIS   A N   
3078 C  CA  A HIS   A 138 ? 0.1560 0.1905 0.2004 -0.0111 0.0076  -0.0034 138 HIS   A CA  
3079 C  CA  B HIS   A 138 ? 0.1495 0.1893 0.1766 -0.0140 0.0002  0.0072  138 HIS   A CA  
3080 C  C   A HIS   A 138 ? 0.1497 0.1648 0.2044 -0.0075 -0.0014 0.0113  138 HIS   A C   
3081 C  C   B HIS   A 138 ? 0.1470 0.1821 0.1673 -0.0123 -0.0016 0.0134  138 HIS   A C   
3082 O  O   A HIS   A 138 ? 0.1627 0.1662 0.2061 -0.0038 -0.0037 0.0082  138 HIS   A O   
3083 O  O   B HIS   A 138 ? 0.1520 0.1827 0.1638 -0.0154 0.0105  0.0126  138 HIS   A O   
3084 C  CB  A HIS   A 138 ? 0.1713 0.2106 0.2030 -0.0073 0.0009  -0.0137 138 HIS   A CB  
3085 C  CB  B HIS   A 138 ? 0.1740 0.2123 0.1808 -0.0137 -0.0073 0.0061  138 HIS   A CB  
3086 C  CG  A HIS   A 138 ? 0.1847 0.2225 0.2089 -0.0113 0.0031  -0.0293 138 HIS   A CG  
3087 C  CG  B HIS   A 138 ? 0.1880 0.2216 0.1903 -0.0187 0.0056  0.0080  138 HIS   A CG  
3088 N  ND1 A HIS   A 138 ? 0.1936 0.2310 0.2217 -0.0073 0.0087  -0.0425 138 HIS   A ND1 
3089 N  ND1 B HIS   A 138 ? 0.1939 0.2313 0.2062 -0.0212 0.0121  0.0008  138 HIS   A ND1 
3090 C  CD2 A HIS   A 138 ? 0.1858 0.2323 0.2122 -0.0083 0.0058  -0.0261 138 HIS   A CD2 
3091 C  CD2 B HIS   A 138 ? 0.1926 0.2250 0.1901 -0.0167 0.0001  0.0100  138 HIS   A CD2 
3092 C  CE1 A HIS   A 138 ? 0.1975 0.2370 0.2252 -0.0010 0.0082  -0.0414 138 HIS   A CE1 
3093 C  CE1 B HIS   A 138 ? 0.1991 0.2368 0.2036 -0.0165 0.0106  0.0017  138 HIS   A CE1 
3094 N  NE2 A HIS   A 138 ? 0.1912 0.2405 0.2138 -0.0026 0.0115  -0.0340 138 HIS   A NE2 
3095 N  NE2 B HIS   A 138 ? 0.1975 0.2342 0.1966 -0.0130 0.0059  0.0057  138 HIS   A NE2 
3110 N  N   A SER   A 139 ? 0.1411 0.1493 0.2024 -0.0135 0.0012  0.0223  139 SER   A N   
3111 N  N   B SER   A 139 ? 0.1422 0.1739 0.1617 -0.0100 -0.0074 0.0213  139 SER   A N   
3112 C  CA  A SER   A 139 ? 0.1393 0.1489 0.1995 -0.0111 0.0014  0.0189  139 SER   A CA  
3113 C  CA  B SER   A 139 ? 0.1375 0.1636 0.1587 -0.0194 0.0079  0.0277  139 SER   A CA  
3114 C  C   A SER   A 139 ? 0.1360 0.1444 0.2008 -0.0115 0.0062  0.0145  139 SER   A C   
3115 C  C   B SER   A 139 ? 0.1332 0.1603 0.1848 -0.0206 0.0133  0.0305  139 SER   A C   
3116 O  O   A SER   A 139 ? 0.1340 0.1287 0.2068 -0.0155 -0.0106 0.0097  139 SER   A O   
3117 O  O   B SER   A 139 ? 0.1266 0.1566 0.1891 -0.0236 0.0164  0.0158  139 SER   A O   
3118 C  CB  A SER   A 139 ? 0.1409 0.1471 0.2007 -0.0074 0.0069  0.0165  139 SER   A CB  
3119 C  CB  B SER   A 139 ? 0.1373 0.1528 0.1514 -0.0142 0.0200  0.0118  139 SER   A CB  
3120 O  OG  A SER   A 139 ? 0.1456 0.1464 0.2141 -0.0126 -0.0020 0.0159  139 SER   A OG  
3121 O  OG  B SER   A 139 ? 0.1280 0.1335 0.1390 -0.0030 0.0174  0.0031  139 SER   A OG  
3132 N  N   . LEU   A 140 ? 0.1344 0.1676 0.1852 -0.0096 0.0062  0.0358  140 LEU   A N   
3133 C  CA  . LEU   A 140 ? 0.1294 0.1621 0.1940 -0.0072 0.0032  0.0329  140 LEU   A CA  
3134 C  C   . LEU   A 140 ? 0.1263 0.1730 0.1857 -0.0088 0.0092  0.0358  140 LEU   A C   
3135 O  O   . LEU   A 140 ? 0.1301 0.1751 0.2153 -0.0049 0.0033  0.0396  140 LEU   A O   
3136 C  CB  . LEU   A 140 ? 0.1296 0.1699 0.2000 -0.0064 -0.0008 0.0321  140 LEU   A CB  
3137 C  CG  . LEU   A 140 ? 0.1294 0.1881 0.2067 -0.0262 0.0070  0.0521  140 LEU   A CG  
3138 C  CD1 . LEU   A 140 ? 0.1381 0.1909 0.2217 -0.0094 0.0036  0.0549  140 LEU   A CD1 
3139 C  CD2 . LEU   A 140 ? 0.1388 0.2100 0.2224 -0.0208 0.0096  0.0562  140 LEU   A CD2 
3152 N  N   . ARG   A 141 ? 0.1354 0.1750 0.1931 -0.0110 0.0000  0.0254  141 ARG   A N   
3153 C  CA  . ARG   A 141 ? 0.1467 0.1849 0.2191 -0.0200 0.0016  0.0116  141 ARG   A CA  
3154 C  C   . ARG   A 141 ? 0.1471 0.1669 0.2081 -0.0169 0.0057  0.0150  141 ARG   A C   
3155 O  O   . ARG   A 141 ? 0.1424 0.1665 0.2275 -0.0117 0.0070  0.0171  141 ARG   A O   
3156 C  CB  . ARG   A 141 ? 0.1639 0.2086 0.2335 -0.0249 -0.0022 -0.0171 141 ARG   A CB  
3157 C  CG  . ARG   A 141 ? 0.1987 0.2437 0.2792 -0.0381 0.0088  -0.0263 141 ARG   A CG  
3158 C  CD  . ARG   A 141 ? 0.2381 0.2726 0.3240 -0.0508 0.0052  -0.0304 141 ARG   A CD  
3159 N  NE  . ARG   A 141 ? 0.2302 0.2911 0.3437 -0.0503 0.0059  -0.0183 141 ARG   A NE  
3160 C  CZ  . ARG   A 141 ? 0.2397 0.3096 0.3428 -0.0609 0.0082  -0.0102 141 ARG   A CZ  
3161 N  NH1 . ARG   A 141 ? 0.2127 0.3156 0.3329 -0.0758 0.0257  -0.0314 141 ARG   A NH1 
3162 N  NH2 . ARG   A 141 ? 0.2508 0.3255 0.3645 -0.0464 -0.0075 -0.0005 141 ARG   A NH2 
3176 N  N   . VAL   A 142 ? 0.1379 0.1631 0.2101 -0.0071 -0.0012 0.0101  142 VAL   A N   
3177 C  CA  . VAL   A 142 ? 0.1373 0.1602 0.2070 -0.0054 0.0202  0.0075  142 VAL   A CA  
3178 C  C   . VAL   A 142 ? 0.1303 0.1518 0.2002 -0.0113 0.0074  0.0168  142 VAL   A C   
3179 O  O   . VAL   A 142 ? 0.1368 0.1570 0.2058 -0.0037 0.0105  0.0179  142 VAL   A O   
3180 C  CB  . VAL   A 142 ? 0.1518 0.1721 0.1929 -0.0072 0.0173  0.0128  142 VAL   A CB  
3181 C  CG1 . VAL   A 142 ? 0.1470 0.1607 0.2036 -0.0176 0.0152  0.0019  142 VAL   A CG1 
3182 C  CG2 . VAL   A 142 ? 0.1633 0.1883 0.2144 -0.0004 0.0252  0.0112  142 VAL   A CG2 
3192 N  N   . CYS   A 143 ? 0.1320 0.1470 0.1950 -0.0126 0.0091  0.0231  143 CYS   A N   
3193 C  CA  . CYS   A 143 ? 0.1330 0.1575 0.2094 -0.0124 0.0090  0.0239  143 CYS   A CA  
3194 C  C   . CYS   A 143 ? 0.1340 0.1480 0.2020 -0.0106 0.0017  0.0295  143 CYS   A C   
3195 O  O   . CYS   A 143 ? 0.1309 0.1508 0.2034 -0.0059 0.0085  0.0245  143 CYS   A O   
3196 C  CB  . CYS   A 143 ? 0.1392 0.1576 0.2089 0.0000  0.0233  0.0386  143 CYS   A CB  
3197 S  SG  . CYS   A 143 ? 0.1597 0.1625 0.1998 0.0052  0.0123  0.0163  143 CYS   A SG  
3203 N  N   . VAL   A 144 ? 0.1320 0.1562 0.2241 -0.0135 0.0094  0.0391  144 VAL   A N   
3204 C  CA  . VAL   A 144 ? 0.1373 0.1636 0.2589 -0.0115 0.0227  0.0461  144 VAL   A CA  
3205 C  C   . VAL   A 144 ? 0.1437 0.1570 0.2497 -0.0216 -0.0079 0.0326  144 VAL   A C   
3206 O  O   . VAL   A 144 ? 0.1597 0.1573 0.2559 -0.0038 -0.0026 0.0400  144 VAL   A O   
3207 C  CB  . VAL   A 144 ? 0.1690 0.1874 0.3081 -0.0008 0.0437  0.0509  144 VAL   A CB  
3208 C  CG1 . VAL   A 144 ? 0.1952 0.2046 0.3434 -0.0146 0.0177  0.0457  144 VAL   A CG1 
3209 C  CG2 . VAL   A 144 ? 0.1513 0.1963 0.3181 0.0026  0.0513  0.0672  144 VAL   A CG2 
3219 N  N   . ASP   A 145 ? 0.1523 0.1523 0.2558 -0.0159 0.0035  0.0198  145 ASP   A N   
3220 C  CA  . ASP   A 145 ? 0.1638 0.1557 0.2636 -0.0172 0.0006  0.0096  145 ASP   A CA  
3221 C  C   . ASP   A 145 ? 0.1574 0.1539 0.2711 -0.0120 0.0054  -0.0041 145 ASP   A C   
3222 O  O   . ASP   A 145 ? 0.1738 0.1610 0.3248 -0.0153 -0.0009 -0.0329 145 ASP   A O   
3223 C  CB  . ASP   A 145 ? 0.1716 0.1816 0.2823 -0.0275 -0.0121 0.0141  145 ASP   A CB  
3224 C  CG  . ASP   A 145 ? 0.1890 0.2214 0.3107 -0.0451 -0.0217 0.0254  145 ASP   A CG  
3225 O  OD1 . ASP   A 145 ? 0.1871 0.2378 0.3358 -0.0587 -0.0107 0.0243  145 ASP   A OD1 
3226 O  OD2 . ASP   A 145 ? 0.2147 0.2493 0.3218 -0.0559 -0.0411 0.0225  145 ASP   A OD2 
3231 N  N   . THR   A 146 ? 0.1419 0.1438 0.2332 -0.0109 0.0130  0.0104  146 THR   A N   
3232 C  CA  . THR   A 146 ? 0.1393 0.1416 0.2177 -0.0077 0.0090  0.0097  146 THR   A CA  
3233 C  C   . THR   A 146 ? 0.1331 0.1382 0.2229 -0.0024 0.0153  0.0104  146 THR   A C   
3234 O  O   . THR   A 146 ? 0.1439 0.1481 0.2499 0.0027  0.0059  0.0134  146 THR   A O   
3235 C  CB  . THR   A 146 ? 0.1346 0.1427 0.2138 -0.0084 0.0069  0.0066  146 THR   A CB  
3236 O  OG1 . THR   A 146 ? 0.1413 0.1578 0.2163 -0.0030 0.0060  0.0017  146 THR   A OG1 
3237 C  CG2 . THR   A 146 ? 0.1422 0.1403 0.2352 -0.0048 0.0107  0.0082  146 THR   A CG2 
3245 N  N   . VAL   A 147 ? 0.1294 0.1398 0.2152 -0.0006 0.0145  0.0097  147 VAL   A N   
3246 C  CA  . VAL   A 147 ? 0.1360 0.1422 0.2230 -0.0110 0.0301  0.0157  147 VAL   A CA  
3247 C  C   . VAL   A 147 ? 0.1403 0.1412 0.2272 -0.0088 0.0220  0.0323  147 VAL   A C   
3248 O  O   . VAL   A 147 ? 0.1402 0.1485 0.2360 -0.0116 0.0140  0.0329  147 VAL   A O   
3249 C  CB  . VAL   A 147 ? 0.1445 0.1410 0.2154 -0.0130 0.0244  0.0174  147 VAL   A CB  
3250 C  CG1 . VAL   A 147 ? 0.1805 0.1465 0.2165 -0.0072 0.0190  0.0301  147 VAL   A CG1 
3251 C  CG2 . VAL   A 147 ? 0.1464 0.1445 0.2198 -0.0105 0.0179  0.0232  147 VAL   A CG2 
3261 N  N   . ARG   A 148 ? 0.1361 0.1450 0.2288 -0.0092 0.0233  0.0459  148 ARG   A N   
3262 C  CA  . ARG   A 148 ? 0.1455 0.1506 0.2222 -0.0126 0.0110  0.0537  148 ARG   A CA  
3263 C  C   . ARG   A 148 ? 0.1574 0.1510 0.2296 -0.0143 0.0114  0.0574  148 ARG   A C   
3264 O  O   . ARG   A 148 ? 0.1842 0.1636 0.2362 -0.0163 0.0236  0.0541  148 ARG   A O   
3265 C  CB  . ARG   A 148 ? 0.1542 0.1462 0.2512 -0.0065 0.0249  0.0410  148 ARG   A CB  
3266 C  CG  . ARG   A 148 ? 0.1680 0.1509 0.2777 -0.0066 0.0501  0.0352  148 ARG   A CG  
3267 C  CD  . ARG   A 148 ? 0.1872 0.1492 0.2982 -0.0043 0.0513  0.0605  148 ARG   A CD  
3268 N  NE  . ARG   A 148 ? 0.1808 0.1568 0.2966 0.0112  0.0543  0.0654  148 ARG   A NE  
3269 C  CZ  . ARG   A 148 ? 0.1729 0.1412 0.2882 0.0116  0.0502  0.0573  148 ARG   A CZ  
3270 N  NH1 . ARG   A 148 ? 0.1826 0.1432 0.2932 -0.0041 0.0560  0.0264  148 ARG   A NH1 
3271 N  NH2 . ARG   A 148 ? 0.1605 0.1587 0.2958 0.0183  0.0534  0.0584  148 ARG   A NH2 
3285 N  N   . THR   A 149 ? 0.1507 0.1555 0.2268 -0.0127 0.0024  0.0503  149 THR   A N   
3286 C  CA  . THR   A 149 ? 0.1534 0.1606 0.2272 -0.0082 0.0007  0.0452  149 THR   A CA  
3287 C  C   . THR   A 149 ? 0.1467 0.1624 0.2168 -0.0177 0.0137  0.0503  149 THR   A C   
3288 O  O   . THR   A 149 ? 0.1457 0.1709 0.2271 -0.0227 0.0113  0.0559  149 THR   A O   
3289 C  CB  . THR   A 149 ? 0.1537 0.1674 0.2349 -0.0103 0.0110  0.0361  149 THR   A CB  
3290 O  OG1 . THR   A 149 ? 0.1560 0.1533 0.2445 -0.0141 0.0081  0.0418  149 THR   A OG1 
3291 C  CG2 . THR   A 149 ? 0.1506 0.1830 0.2456 -0.0032 0.0084  0.0299  149 THR   A CG2 
3299 N  N   . ASN   A 150 ? 0.1510 0.1651 0.2195 -0.0121 0.0050  0.0630  150 ASN   A N   
3300 C  CA  . ASN   A 150 ? 0.1613 0.1707 0.2167 -0.0160 0.0072  0.0588  150 ASN   A CA  
3301 C  C   . ASN   A 150 ? 0.1466 0.1659 0.2186 -0.0205 0.0031  0.0484  150 ASN   A C   
3302 O  O   . ASN   A 150 ? 0.1541 0.1748 0.2352 -0.0166 -0.0081 0.0502  150 ASN   A O   
3303 C  CB  . ASN   A 150 ? 0.2039 0.1954 0.2458 -0.0166 0.0211  0.0814  150 ASN   A CB  
3304 C  CG  . ASN   A 150 ? 0.2565 0.2284 0.3149 -0.0187 0.0035  0.0850  150 ASN   A CG  
3305 O  OD1 . ASN   A 150 ? 0.2816 0.2322 0.3340 -0.0283 0.0005  0.0969  150 ASN   A OD1 
3306 N  ND2 . ASN   A 150 ? 0.2866 0.2497 0.3504 -0.0116 -0.0116 0.0817  150 ASN   A ND2 
3313 N  N   . VAL   A 151 ? 0.1442 0.1518 0.2115 -0.0138 0.0040  0.0447  151 VAL   A N   
3314 C  CA  . VAL   A 151 ? 0.1562 0.1580 0.1962 -0.0186 0.0081  0.0510  151 VAL   A CA  
3315 C  C   . VAL   A 151 ? 0.1450 0.1518 0.2003 -0.0258 0.0089  0.0508  151 VAL   A C   
3316 O  O   . VAL   A 151 ? 0.1547 0.1579 0.2451 -0.0172 0.0079  0.0485  151 VAL   A O   
3317 C  CB  . VAL   A 151 ? 0.1801 0.1838 0.1991 -0.0072 0.0174  0.0400  151 VAL   A CB  
3318 C  CG1 . VAL   A 151 ? 0.1798 0.2026 0.2237 -0.0176 0.0142  0.0331  151 VAL   A CG1 
3319 C  CG2 . VAL   A 151 ? 0.1939 0.1794 0.2047 -0.0054 0.0257  0.0429  151 VAL   A CG2 
3329 N  N   A TYR   A 152 ? 0.1393 0.1521 0.2060 -0.0310 -0.0007 0.0534  152 TYR   A N   
3330 N  N   B TYR   A 152 ? 0.1464 0.1569 0.2146 -0.0220 0.0066  0.0406  152 TYR   A N   
3331 C  CA  A TYR   A 152 ? 0.1420 0.1650 0.1878 -0.0247 -0.0042 0.0523  152 TYR   A CA  
3332 C  CA  B TYR   A 152 ? 0.1515 0.1661 0.2010 -0.0138 0.0111  0.0409  152 TYR   A CA  
3333 C  C   A TYR   A 152 ? 0.1381 0.1610 0.1692 -0.0225 0.0046  0.0523  152 TYR   A C   
3334 C  C   B TYR   A 152 ? 0.1435 0.1589 0.1928 -0.0122 0.0224  0.0418  152 TYR   A C   
3335 O  O   A TYR   A 152 ? 0.1443 0.1507 0.1709 -0.0312 0.0112  0.0467  152 TYR   A O   
3336 O  O   B TYR   A 152 ? 0.1460 0.1547 0.2096 -0.0139 0.0201  0.0327  152 TYR   A O   
3337 C  CB  A TYR   A 152 ? 0.1537 0.1761 0.1997 -0.0183 0.0070  0.0616  152 TYR   A CB  
3338 C  CB  B TYR   A 152 ? 0.1694 0.1788 0.2001 -0.0075 0.0237  0.0512  152 TYR   A CB  
3339 C  CG  A TYR   A 152 ? 0.1627 0.1942 0.1974 -0.0188 0.0241  0.0574  152 TYR   A CG  
3340 C  CG  B TYR   A 152 ? 0.1863 0.1972 0.1918 -0.0029 0.0295  0.0469  152 TYR   A CG  
3341 C  CD1 A TYR   A 152 ? 0.1768 0.2135 0.2114 -0.0091 0.0294  0.0646  152 TYR   A CD1 
3342 C  CD1 B TYR   A 152 ? 0.1946 0.2119 0.2069 0.0021  0.0330  0.0510  152 TYR   A CD1 
3343 C  CD2 A TYR   A 152 ? 0.1669 0.1973 0.1997 -0.0259 0.0250  0.0481  152 TYR   A CD2 
3344 C  CD2 B TYR   A 152 ? 0.1951 0.2062 0.1926 -0.0045 0.0269  0.0387  152 TYR   A CD2 
3345 C  CE1 A TYR   A 152 ? 0.2058 0.2242 0.2126 -0.0025 0.0228  0.0762  152 TYR   A CE1 
3346 C  CE1 B TYR   A 152 ? 0.2130 0.2256 0.2114 0.0086  0.0188  0.0556  152 TYR   A CE1 
3347 C  CE2 A TYR   A 152 ? 0.1924 0.2052 0.2104 -0.0284 0.0320  0.0603  152 TYR   A CE2 
3348 C  CE2 B TYR   A 152 ? 0.2115 0.2180 0.2030 -0.0032 0.0223  0.0444  152 TYR   A CE2 
3349 C  CZ  A TYR   A 152 ? 0.2182 0.2121 0.2054 -0.0151 0.0313  0.0850  152 TYR   A CZ  
3350 C  CZ  B TYR   A 152 ? 0.2258 0.2269 0.2072 0.0012  0.0197  0.0623  152 TYR   A CZ  
3351 O  OH  A TYR   A 152 ? 0.2439 0.2254 0.2404 -0.0042 0.0395  0.1029  152 TYR   A OH  
3352 O  OH  B TYR   A 152 ? 0.2496 0.2484 0.2324 0.0017  0.0176  0.0761  152 TYR   A OH  
3371 N  N   A LEU   A 153 ? 0.1358 0.1609 0.1812 -0.0198 0.0060  0.0499  153 LEU   A N   
3372 N  N   B LEU   A 153 ? 0.1405 0.1525 0.1895 -0.0156 0.0291  0.0404  153 LEU   A N   
3373 C  CA  A LEU   A 153 ? 0.1278 0.1574 0.1880 -0.0096 0.0064  0.0470  153 LEU   A CA  
3374 C  CA  B LEU   A 153 ? 0.1328 0.1422 0.1857 -0.0134 0.0316  0.0304  153 LEU   A CA  
3375 C  C   A LEU   A 153 ? 0.1335 0.1616 0.1906 -0.0099 0.0127  0.0469  153 LEU   A C   
3376 C  C   B LEU   A 153 ? 0.1360 0.1326 0.1894 -0.0183 0.0301  0.0205  153 LEU   A C   
3377 O  O   A LEU   A 153 ? 0.1386 0.1716 0.1944 -0.0121 0.0202  0.0399  153 LEU   A O   
3378 O  O   B LEU   A 153 ? 0.1419 0.1325 0.1978 -0.0218 0.0289  0.0152  153 LEU   A O   
3379 C  CB  A LEU   A 153 ? 0.1230 0.1547 0.2073 -0.0045 0.0084  0.0442  153 LEU   A CB  
3380 C  CB  B LEU   A 153 ? 0.1296 0.1404 0.1902 -0.0134 0.0314  0.0169  153 LEU   A CB  
3381 C  CG  A LEU   A 153 ? 0.1285 0.1546 0.2061 -0.0075 0.0131  0.0405  153 LEU   A CG  
3382 C  CG  B LEU   A 153 ? 0.1332 0.1384 0.1968 -0.0151 0.0276  0.0178  153 LEU   A CG  
3383 C  CD1 A LEU   A 153 ? 0.1295 0.1602 0.1950 -0.0084 0.0242  0.0320  153 LEU   A CD1 
3384 C  CD1 B LEU   A 153 ? 0.1417 0.1381 0.1941 -0.0126 0.0228  0.0090  153 LEU   A CD1 
3385 C  CD2 A LEU   A 153 ? 0.1268 0.1492 0.2013 -0.0061 0.0047  0.0351  153 LEU   A CD2 
3386 C  CD2 B LEU   A 153 ? 0.1264 0.1344 0.1857 -0.0091 0.0185  0.0143  153 LEU   A CD2 
3409 N  N   A ALA   A 154 ? 0.1369 0.1583 0.2102 -0.0043 0.0263  0.0559  154 ALA   A N   
3410 N  N   B ALA   A 154 ? 0.1339 0.1357 0.2091 -0.0192 0.0305  0.0246  154 ALA   A N   
3411 C  CA  A ALA   A 154 ? 0.1525 0.1543 0.2093 0.0054  0.0377  0.0569  154 ALA   A CA  
3412 C  CA  B ALA   A 154 ? 0.1440 0.1396 0.2129 -0.0149 0.0241  0.0235  154 ALA   A CA  
3413 C  C   A ALA   A 154 ? 0.1511 0.1560 0.2120 0.0166  0.0502  0.0589  154 ALA   A C   
3414 C  C   B ALA   A 154 ? 0.1463 0.1478 0.2078 -0.0081 0.0342  0.0356  154 ALA   A C   
3415 O  O   A ALA   A 154 ? 0.1528 0.1565 0.2291 0.0170  0.0448  0.0541  154 ALA   A O   
3416 O  O   B ALA   A 154 ? 0.1519 0.1552 0.2074 -0.0086 0.0258  0.0400  154 ALA   A O   
3417 C  CB  A ALA   A 154 ? 0.1617 0.1557 0.2139 0.0135  0.0410  0.0477  154 ALA   A CB  
3418 C  CB  B ALA   A 154 ? 0.1474 0.1398 0.2215 -0.0027 0.0215  0.0195  154 ALA   A CB  
3429 N  N   A VAL   A 155 ? 0.1617 0.1601 0.2170 0.0208  0.0498  0.0706  155 VAL   A N   
3430 N  N   B VAL   A 155 ? 0.1503 0.1490 0.2217 -0.0064 0.0420  0.0466  155 VAL   A N   
3431 C  CA  A VAL   A 155 ? 0.1744 0.1723 0.2223 0.0273  0.0345  0.0618  155 VAL   A CA  
3432 C  CA  B VAL   A 155 ? 0.1491 0.1538 0.2265 -0.0120 0.0457  0.0513  155 VAL   A CA  
3433 C  C   A VAL   A 155 ? 0.1804 0.1839 0.2257 0.0383  0.0305  0.0589  155 VAL   A C   
3434 C  C   B VAL   A 155 ? 0.1577 0.1591 0.2241 -0.0130 0.0560  0.0612  155 VAL   A C   
3435 O  O   A VAL   A 155 ? 0.1784 0.1889 0.2346 0.0457  0.0237  0.0546  155 VAL   A O   
3436 O  O   B VAL   A 155 ? 0.1542 0.1580 0.2349 -0.0059 0.0673  0.0606  155 VAL   A O   
3437 C  CB  A VAL   A 155 ? 0.1813 0.1758 0.2220 0.0304  0.0138  0.0502  155 VAL   A CB  
3438 C  CB  B VAL   A 155 ? 0.1444 0.1534 0.2310 -0.0078 0.0288  0.0362  155 VAL   A CB  
3439 C  CG1 A VAL   A 155 ? 0.1944 0.1799 0.2126 0.0329  0.0027  0.0491  155 VAL   A CG1 
3440 C  CG1 B VAL   A 155 ? 0.1585 0.1573 0.2327 -0.0001 0.0209  0.0328  155 VAL   A CG1 
3441 C  CG2 A VAL   A 155 ? 0.1896 0.1818 0.2370 0.0357  -0.0016 0.0454  155 VAL   A CG2 
3442 C  CG2 B VAL   A 155 ? 0.1518 0.1575 0.2469 0.0044  0.0048  0.0348  155 VAL   A CG2 
3461 N  N   A PHE   A 156 ? 0.1873 0.1866 0.2363 0.0438  0.0421  0.0738  156 PHE   A N   
3462 N  N   B PHE   A 156 ? 0.1717 0.1633 0.2474 -0.0152 0.0557  0.0700  156 PHE   A N   
3463 C  CA  A PHE   A 156 ? 0.2054 0.1886 0.2589 0.0522  0.0429  0.0763  156 PHE   A CA  
3464 C  CA  B PHE   A 156 ? 0.1861 0.1704 0.2565 -0.0104 0.0465  0.0693  156 PHE   A CA  
3465 C  C   A PHE   A 156 ? 0.2041 0.1909 0.2705 0.0560  0.0576  0.0784  156 PHE   A C   
3466 C  C   B PHE   A 156 ? 0.1925 0.1822 0.2619 -0.0047 0.0632  0.0808  156 PHE   A C   
3467 O  O   A PHE   A 156 ? 0.2096 0.1926 0.2826 0.0508  0.0678  0.0596  156 PHE   A O   
3468 O  O   B PHE   A 156 ? 0.2035 0.1898 0.2779 -0.0013 0.0658  0.0713  156 PHE   A O   
3469 C  CB  A PHE   A 156 ? 0.2303 0.1994 0.2618 0.0489  0.0366  0.0892  156 PHE   A CB  
3470 C  CB  B PHE   A 156 ? 0.1920 0.1610 0.2398 -0.0031 0.0355  0.0728  156 PHE   A CB  
3471 C  CG  A PHE   A 156 ? 0.2589 0.2111 0.2883 0.0564  0.0219  0.0751  156 PHE   A CG  
3472 C  CG  B PHE   A 156 ? 0.2015 0.1678 0.2225 0.0090  0.0322  0.0758  156 PHE   A CG  
3473 C  CD1 A PHE   A 156 ? 0.2724 0.2162 0.2913 0.0611  0.0228  0.0674  156 PHE   A CD1 
3474 C  CD1 B PHE   A 156 ? 0.2054 0.1747 0.2306 0.0237  0.0245  0.0606  156 PHE   A CD1 
3475 C  CD2 A PHE   A 156 ? 0.2751 0.2243 0.2985 0.0590  0.0210  0.0758  156 PHE   A CD2 
3476 C  CD2 B PHE   A 156 ? 0.2180 0.1769 0.2222 0.0086  0.0361  0.0772  156 PHE   A CD2 
3477 C  CE1 A PHE   A 156 ? 0.2822 0.2179 0.3041 0.0637  0.0271  0.0674  156 PHE   A CE1 
3478 C  CE1 B PHE   A 156 ? 0.2098 0.1801 0.2373 0.0153  0.0269  0.0458  156 PHE   A CE1 
3479 C  CE2 A PHE   A 156 ? 0.2857 0.2275 0.3054 0.0627  0.0201  0.0751  156 PHE   A CE2 
3480 C  CE2 B PHE   A 156 ? 0.2159 0.1809 0.2262 0.0075  0.0361  0.0722  156 PHE   A CE2 
3481 C  CZ  A PHE   A 156 ? 0.2860 0.2215 0.3096 0.0693  0.0297  0.0680  156 PHE   A CZ  
3482 C  CZ  B PHE   A 156 ? 0.2099 0.1775 0.2353 -0.0027 0.0303  0.0518  156 PHE   A CZ  
3501 N  N   A ASP   A 157 ? 0.1985 0.1913 0.2596 0.0696  0.0510  0.0926  157 ASP   A N   
3502 N  N   B ASP   A 157 ? 0.1883 0.1983 0.2726 -0.0007 0.0510  0.1003  157 ASP   A N   
3503 C  CA  A ASP   A 157 ? 0.2137 0.2161 0.2832 0.0587  0.0456  0.1057  157 ASP   A CA  
3504 C  CA  B ASP   A 157 ? 0.1870 0.2134 0.2626 0.0094  0.0449  0.1120  157 ASP   A CA  
3505 C  C   A ASP   A 157 ? 0.2056 0.2380 0.2994 0.0557  0.0533  0.1197  157 ASP   A C   
3506 C  C   B ASP   A 157 ? 0.1784 0.2293 0.2530 0.0242  0.0433  0.1248  157 ASP   A C   
3507 O  O   A ASP   A 157 ? 0.2039 0.2439 0.2917 0.0501  0.0521  0.1237  157 ASP   A O   
3508 O  O   B ASP   A 157 ? 0.1733 0.2278 0.2419 0.0249  0.0444  0.1303  157 ASP   A O   
3509 C  CB  A ASP   A 157 ? 0.2297 0.2208 0.2967 0.0624  0.0369  0.0994  157 ASP   A CB  
3510 C  CB  B ASP   A 157 ? 0.1949 0.2124 0.2723 0.0173  0.0388  0.1100  157 ASP   A CB  
3511 C  CG  A ASP   A 157 ? 0.2516 0.2328 0.3321 0.0590  0.0268  0.0894  157 ASP   A CG  
3512 C  CG  B ASP   A 157 ? 0.2027 0.2132 0.2833 0.0215  0.0350  0.1076  157 ASP   A CG  
3513 O  OD1 A ASP   A 157 ? 0.2606 0.2389 0.3414 0.0589  0.0167  0.0785  157 ASP   A OD1 
3514 O  OD1 B ASP   A 157 ? 0.2108 0.2034 0.3243 0.0135  0.0247  0.1108  157 ASP   A OD1 
3515 O  OD2 A ASP   A 157 ? 0.2576 0.2289 0.3696 0.0520  0.0168  0.1002  157 ASP   A OD2 
3516 O  OD2 B ASP   A 157 ? 0.1997 0.2165 0.2596 0.0275  0.0276  0.1056  157 ASP   A OD2 
3525 N  N   A LYS   A 158 ? 0.2081 0.2590 0.3185 0.0517  0.0714  0.1138  158 LYS   A N   
3526 N  N   B LYS   A 158 ? 0.1840 0.2537 0.2538 0.0325  0.0446  0.1198  158 LYS   A N   
3527 C  CA  A LYS   A 158 ? 0.2072 0.2764 0.3367 0.0546  0.0724  0.1109  158 LYS   A CA  
3528 C  CA  B LYS   A 158 ? 0.1869 0.2749 0.2511 0.0384  0.0364  0.1180  158 LYS   A CA  
3529 C  C   A LYS   A 158 ? 0.1946 0.2754 0.3366 0.0499  0.0625  0.1130  158 LYS   A C   
3530 C  C   B LYS   A 158 ? 0.1777 0.2807 0.2463 0.0518  0.0281  0.1298  158 LYS   A C   
3531 O  O   A LYS   A 158 ? 0.1988 0.2855 0.3509 0.0410  0.0635  0.1122  158 LYS   A O   
3532 O  O   B LYS   A 158 ? 0.1754 0.2879 0.2501 0.0492  0.0367  0.1277  158 LYS   A O   
3533 C  CB  A LYS   A 158 ? 0.2198 0.2883 0.3639 0.0573  0.0894  0.1057  158 LYS   A CB  
3534 C  CB  B LYS   A 158 ? 0.1992 0.2836 0.2710 0.0245  0.0346  0.1042  158 LYS   A CB  
3535 C  CG  A LYS   A 158 ? 0.2390 0.3043 0.3940 0.0542  0.1027  0.1020  158 LYS   A CG  
3536 C  CG  B LYS   A 158 ? 0.2107 0.2951 0.2878 0.0143  0.0217  0.0855  158 LYS   A CG  
3537 C  CD  A LYS   A 158 ? 0.2475 0.3168 0.4115 0.0571  0.1144  0.1010  158 LYS   A CD  
3538 C  CD  B LYS   A 158 ? 0.2205 0.3080 0.3119 0.0110  0.0079  0.0701  158 LYS   A CD  
3539 C  CE  A LYS   A 158 ? 0.2489 0.3221 0.4147 0.0504  0.1253  0.1138  158 LYS   A CE  
3540 C  CE  B LYS   A 158 ? 0.2234 0.3127 0.3262 0.0095  -0.0027 0.0627  158 LYS   A CE  
3541 N  NZ  A LYS   A 158 ? 0.2429 0.3214 0.4196 0.0419  0.1402  0.1281  158 LYS   A NZ  
3542 N  NZ  B LYS   A 158 ? 0.2237 0.3117 0.3352 0.0070  -0.0050 0.0614  158 LYS   A NZ  
3569 N  N   A ASN   A 159 ? 0.1879 0.2672 0.3312 0.0437  0.0504  0.1032  159 ASN   A N   
3570 N  N   B ASN   A 159 ? 0.1852 0.2854 0.2598 0.0537  0.0180  0.1221  159 ASN   A N   
3571 C  CA  A ASN   A 159 ? 0.1887 0.2582 0.3287 0.0344  0.0154  0.0912  159 ASN   A CA  
3572 C  CA  B ASN   A 159 ? 0.1886 0.2810 0.2737 0.0506  0.0048  0.1213  159 ASN   A CA  
3573 C  C   A ASN   A 159 ? 0.1822 0.2439 0.3055 0.0236  0.0131  0.0650  159 ASN   A C   
3574 C  C   B ASN   A 159 ? 0.1762 0.2733 0.2606 0.0310  0.0093  0.1143  159 ASN   A C   
3575 O  O   A ASN   A 159 ? 0.1630 0.2349 0.2947 0.0166  -0.0094 0.0414  159 ASN   A O   
3576 O  O   B ASN   A 159 ? 0.1697 0.2860 0.2631 0.0236  0.0014  0.1054  159 ASN   A O   
3577 C  CB  A ASN   A 159 ? 0.2033 0.2674 0.3659 0.0319  -0.0124 0.0993  159 ASN   A CB  
3578 C  CB  B ASN   A 159 ? 0.2082 0.2806 0.3152 0.0583  -0.0053 0.1201  159 ASN   A CB  
3579 C  CG  A ASN   A 159 ? 0.2238 0.2812 0.4173 0.0364  -0.0134 0.0952  159 ASN   A CG  
3580 C  CG  B ASN   A 159 ? 0.2293 0.2849 0.3620 0.0540  0.0028  0.1043  159 ASN   A CG  
3581 O  OD1 A ASN   A 159 ? 0.2357 0.2976 0.4447 0.0381  -0.0036 0.0882  159 ASN   A OD1 
3582 O  OD1 B ASN   A 159 ? 0.2417 0.2902 0.3906 0.0495  0.0052  0.0895  159 ASN   A OD1 
3583 N  ND2 A ASN   A 159 ? 0.2268 0.2849 0.4370 0.0382  -0.0144 0.0877  159 ASN   A ND2 
3584 N  ND2 B ASN   A 159 ? 0.2308 0.2937 0.3837 0.0498  0.0149  0.0935  159 ASN   A ND2 
3597 N  N   A LEU   A 160 ? 0.1815 0.2318 0.2913 0.0290  0.0162  0.0595  160 LEU   A N   
3598 N  N   B LEU   A 160 ? 0.1578 0.2463 0.2382 0.0211  0.0080  0.1185  160 LEU   A N   
3599 C  CA  A LEU   A 160 ? 0.1854 0.2226 0.2601 0.0178  0.0188  0.0586  160 LEU   A CA  
3600 C  CA  B LEU   A 160 ? 0.1527 0.2257 0.2122 0.0022  0.0229  0.1071  160 LEU   A CA  
3601 C  C   A LEU   A 160 ? 0.1675 0.2155 0.2355 0.0089  0.0247  0.0567  160 LEU   A C   
3602 C  C   B LEU   A 160 ? 0.1368 0.2184 0.1929 0.0032  0.0060  0.0867  160 LEU   A C   
3603 O  O   A LEU   A 160 ? 0.1639 0.2284 0.2373 0.0001  0.0139  0.0463  160 LEU   A O   
3604 O  O   B LEU   A 160 ? 0.1364 0.2253 0.2021 -0.0065 0.0015  0.0800  160 LEU   A O   
3605 C  CB  A LEU   A 160 ? 0.2001 0.2257 0.2545 0.0134  0.0251  0.0491  160 LEU   A CB  
3606 C  CB  B LEU   A 160 ? 0.1655 0.2201 0.1994 -0.0112 0.0293  0.0970  160 LEU   A CB  
3607 C  CG  A LEU   A 160 ? 0.2084 0.2283 0.2643 0.0116  0.0268  0.0291  160 LEU   A CG  
3608 C  CG  B LEU   A 160 ? 0.1675 0.2227 0.2173 -0.0227 0.0251  0.0781  160 LEU   A CG  
3609 C  CD1 A LEU   A 160 ? 0.2211 0.2324 0.2691 0.0157  0.0275  0.0138  160 LEU   A CD1 
3610 C  CD1 B LEU   A 160 ? 0.1775 0.2308 0.2233 -0.0177 0.0287  0.0664  160 LEU   A CD1 
3611 C  CD2 A LEU   A 160 ? 0.2087 0.2289 0.2668 0.0088  0.0355  0.0279  160 LEU   A CD2 
3612 C  CD2 B LEU   A 160 ? 0.1725 0.2189 0.2336 -0.0345 0.0229  0.0757  160 LEU   A CD2 
3635 N  N   A TYR   A 161 ? 0.1656 0.2032 0.2181 0.0083  0.0334  0.0659  161 TYR   A N   
3636 N  N   B TYR   A 161 ? 0.1395 0.2104 0.1756 0.0055  0.0201  0.0755  161 TYR   A N   
3637 C  CA  A TYR   A 161 ? 0.1593 0.2031 0.2172 0.0103  0.0398  0.0533  161 TYR   A CA  
3638 C  CA  B TYR   A 161 ? 0.1473 0.2076 0.1761 -0.0013 0.0207  0.0734  161 TYR   A CA  
3639 C  C   A TYR   A 161 ? 0.1569 0.2252 0.2471 -0.0048 0.0254  0.0688  161 TYR   A C   
3640 C  C   B TYR   A 161 ? 0.1435 0.2211 0.1945 0.0073  0.0007  0.0780  161 TYR   A C   
3641 O  O   A TYR   A 161 ? 0.1439 0.2222 0.2216 -0.0141 0.0170  0.0640  161 TYR   A O   
3642 O  O   B TYR   A 161 ? 0.1411 0.2182 0.1781 -0.0002 -0.0064 0.0648  161 TYR   A O   
3643 C  CB  A TYR   A 161 ? 0.1667 0.1965 0.2196 0.0147  0.0500  0.0333  161 TYR   A CB  
3644 C  CB  B TYR   A 161 ? 0.1553 0.1903 0.1733 -0.0023 0.0298  0.0619  161 TYR   A CB  
3645 C  CG  A TYR   A 161 ? 0.1619 0.1845 0.2278 0.0195  0.0322  0.0280  161 TYR   A CG  
3646 C  CG  B TYR   A 161 ? 0.1553 0.1814 0.1708 -0.0007 0.0275  0.0450  161 TYR   A CG  
3647 C  CD1 A TYR   A 161 ? 0.1562 0.1698 0.2230 0.0118  0.0229  0.0219  161 TYR   A CD1 
3648 C  CD1 B TYR   A 161 ? 0.1484 0.1776 0.1839 -0.0035 0.0171  0.0239  161 TYR   A CD1 
3649 C  CD2 A TYR   A 161 ? 0.1605 0.1880 0.2368 0.0272  0.0260  0.0358  161 TYR   A CD2 
3650 C  CD2 B TYR   A 161 ? 0.1588 0.1836 0.1903 0.0074  0.0239  0.0383  161 TYR   A CD2 
3651 C  CE1 A TYR   A 161 ? 0.1637 0.1772 0.2289 0.0103  0.0119  0.0221  161 TYR   A CE1 
3652 C  CE1 B TYR   A 161 ? 0.1532 0.1679 0.1784 -0.0028 0.0044  0.0212  161 TYR   A CE1 
3653 C  CE2 A TYR   A 161 ? 0.1677 0.1884 0.2428 0.0121  0.0221  0.0427  161 TYR   A CE2 
3654 C  CE2 B TYR   A 161 ? 0.1591 0.1785 0.1860 -0.0036 0.0212  0.0365  161 TYR   A CE2 
3655 C  CZ  A TYR   A 161 ? 0.1745 0.1828 0.2324 0.0089  0.0080  0.0392  161 TYR   A CZ  
3656 C  CZ  B TYR   A 161 ? 0.1666 0.1697 0.1740 -0.0074 0.0049  0.0378  161 TYR   A CZ  
3657 O  OH  A TYR   A 161 ? 0.1864 0.1834 0.2515 0.0085  -0.0117 0.0399  161 TYR   A OH  
3658 O  OH  B TYR   A 161 ? 0.1840 0.1680 0.1711 -0.0148 0.0040  0.0386  161 TYR   A OH  
3677 N  N   A ASP   A 162 ? 0.1549 0.2559 0.2835 -0.0012 0.0384  0.0887  162 ASP   A N   
3678 N  N   B ASP   A 162 ? 0.1402 0.2433 0.2443 0.0174  0.0023  0.0919  162 ASP   A N   
3679 C  CA  A ASP   A 162 ? 0.1508 0.2965 0.2825 0.0057  0.0424  0.0963  162 ASP   A CA  
3680 C  CA  B ASP   A 162 ? 0.1426 0.2830 0.2607 0.0088  -0.0030 0.0979  162 ASP   A CA  
3681 C  C   A ASP   A 162 ? 0.1462 0.3107 0.2748 0.0007  0.0288  0.1091  162 ASP   A C   
3682 C  C   B ASP   A 162 ? 0.1414 0.3033 0.2527 0.0030  -0.0069 0.1019  162 ASP   A C   
3683 O  O   A ASP   A 162 ? 0.1572 0.3155 0.2913 0.0029  0.0293  0.0978  162 ASP   A O   
3684 O  O   B ASP   A 162 ? 0.1395 0.3107 0.2574 -0.0024 0.0002  0.0882  162 ASP   A O   
3685 C  CB  A ASP   A 162 ? 0.1598 0.3191 0.2870 0.0156  0.0536  0.0931  162 ASP   A CB  
3686 C  CB  B ASP   A 162 ? 0.1565 0.3078 0.2875 0.0124  -0.0037 0.0941  162 ASP   A CB  
3687 C  CG  A ASP   A 162 ? 0.1659 0.3373 0.2933 0.0236  0.0597  0.0947  162 ASP   A CG  
3688 C  CG  B ASP   A 162 ? 0.1666 0.3273 0.3019 0.0138  0.0075  0.0998  162 ASP   A CG  
3689 O  OD1 A ASP   A 162 ? 0.1809 0.3500 0.2980 0.0265  0.0552  0.0893  162 ASP   A OD1 
3690 O  OD1 B ASP   A 162 ? 0.1750 0.3337 0.3155 0.0157  0.0045  0.1009  162 ASP   A OD1 
3691 O  OD2 A ASP   A 162 ? 0.1641 0.3403 0.3066 0.0282  0.0776  0.0899  162 ASP   A OD2 
3692 O  OD2 B ASP   A 162 ? 0.1726 0.3359 0.2984 0.0141  0.0260  0.1081  162 ASP   A OD2 
3701 N  N   A LYS   A 163 ? 0.1579 0.3260 0.2787 0.0013  0.0110  0.1108  163 LYS   A N   
3702 N  N   B LYS   A 163 ? 0.1574 0.3177 0.2640 0.0010  -0.0123 0.0979  163 LYS   A N   
3703 C  CA  A LYS   A 163 ? 0.1696 0.3369 0.2771 0.0002  -0.0104 0.1083  163 LYS   A CA  
3704 C  CA  B LYS   A 163 ? 0.1770 0.3250 0.2680 -0.0018 -0.0041 0.0892  163 LYS   A CA  
3705 C  C   A LYS   A 163 ? 0.1638 0.3311 0.2750 -0.0049 -0.0043 0.0993  163 LYS   A C   
3706 C  C   B LYS   A 163 ? 0.1732 0.3186 0.2377 -0.0154 0.0053  0.0848  163 LYS   A C   
3707 O  O   A LYS   A 163 ? 0.1606 0.3427 0.2767 -0.0097 -0.0123 0.0935  163 LYS   A O   
3708 O  O   B LYS   A 163 ? 0.1708 0.3335 0.2343 -0.0187 0.0114  0.0822  163 LYS   A O   
3709 C  CB  A LYS   A 163 ? 0.2103 0.3582 0.3113 0.0125  -0.0202 0.1031  163 LYS   A CB  
3710 C  CB  B LYS   A 163 ? 0.2133 0.3372 0.3074 0.0099  0.0032  0.0893  163 LYS   A CB  
3711 C  CG  A LYS   A 163 ? 0.2520 0.3763 0.3666 0.0181  -0.0155 0.0952  163 LYS   A CG  
3712 C  CG  B LYS   A 163 ? 0.2520 0.3466 0.3586 0.0126  0.0134  0.0845  163 LYS   A CG  
3713 C  CD  A LYS   A 163 ? 0.2954 0.3936 0.4236 0.0195  -0.0134 0.0872  163 LYS   A CD  
3714 C  CD  B LYS   A 163 ? 0.2838 0.3568 0.4097 0.0121  0.0241  0.0779  163 LYS   A CD  
3715 C  CE  A LYS   A 163 ? 0.3145 0.4052 0.4731 0.0187  -0.0119 0.0802  163 LYS   A CE  
3716 C  CE  B LYS   A 163 ? 0.3060 0.3641 0.4490 0.0100  0.0310  0.0750  163 LYS   A CE  
3717 N  NZ  A LYS   A 163 ? 0.3349 0.4128 0.4990 0.0150  -0.0114 0.0769  163 LYS   A NZ  
3718 N  NZ  B LYS   A 163 ? 0.3154 0.3682 0.4776 0.0080  0.0320  0.0715  163 LYS   A NZ  
3745 N  N   A LEU   A 164 ? 0.1488 0.3058 0.2564 -0.0056 -0.0002 0.0991  164 LEU   A N   
3746 N  N   B LEU   A 164 ? 0.1628 0.2931 0.2179 -0.0283 0.0013  0.0798  164 LEU   A N   
3747 C  CA  A LEU   A 164 ? 0.1475 0.2885 0.2367 -0.0105 0.0015  0.0881  164 LEU   A CA  
3748 C  CA  B LEU   A 164 ? 0.1632 0.2753 0.2189 -0.0378 0.0095  0.0644  164 LEU   A CA  
3749 C  C   A LEU   A 164 ? 0.1532 0.2863 0.2386 -0.0220 0.0061  0.0880  164 LEU   A C   
3750 C  C   B LEU   A 164 ? 0.1691 0.2722 0.2265 -0.0371 0.0118  0.0641  164 LEU   A C   
3751 O  O   A LEU   A 164 ? 0.1518 0.2886 0.2319 -0.0340 0.0246  0.0776  164 LEU   A O   
3752 O  O   B LEU   A 164 ? 0.1690 0.2750 0.2307 -0.0339 0.0235  0.0497  164 LEU   A O   
3753 C  CB  A LEU   A 164 ? 0.1447 0.2733 0.2155 -0.0015 0.0097  0.0888  164 LEU   A CB  
3754 C  CB  B LEU   A 164 ? 0.1605 0.2626 0.2130 -0.0425 0.0198  0.0596  164 LEU   A CB  
3755 C  CG  A LEU   A 164 ? 0.1559 0.2627 0.2281 0.0052  0.0087  0.0776  164 LEU   A CG  
3756 C  CG  B LEU   A 164 ? 0.1633 0.2528 0.2103 -0.0404 0.0218  0.0480  164 LEU   A CG  
3757 C  CD1 A LEU   A 164 ? 0.1509 0.2566 0.2333 0.0123  0.0079  0.0688  164 LEU   A CD1 
3758 C  CD1 B LEU   A 164 ? 0.1592 0.2481 0.2115 -0.0410 0.0231  0.0500  164 LEU   A CD1 
3759 C  CD2 A LEU   A 164 ? 0.1682 0.2622 0.2328 -0.0024 0.0134  0.0739  164 LEU   A CD2 
3760 C  CD2 B LEU   A 164 ? 0.1721 0.2520 0.2147 -0.0401 0.0167  0.0325  164 LEU   A CD2 
3783 N  N   A VAL   A 165 ? 0.1509 0.2844 0.2458 -0.0196 0.0166  0.0986  165 VAL   A N   
3784 N  N   B VAL   A 165 ? 0.1725 0.2712 0.2207 -0.0304 0.0242  0.0772  165 VAL   A N   
3785 C  CA  A VAL   A 165 ? 0.1606 0.2869 0.2435 -0.0190 0.0328  0.1076  165 VAL   A CA  
3786 C  CA  B VAL   A 165 ? 0.1883 0.2736 0.2156 -0.0229 0.0317  0.0883  165 VAL   A CA  
3787 C  C   A VAL   A 165 ? 0.1458 0.2992 0.2601 -0.0102 0.0171  0.1110  165 VAL   A C   
3788 C  C   B VAL   A 165 ? 0.1894 0.2887 0.2393 -0.0185 0.0178  0.0883  165 VAL   A C   
3789 O  O   A VAL   A 165 ? 0.1372 0.2980 0.2585 -0.0087 0.0247  0.1064  165 VAL   A O   
3790 O  O   B VAL   A 165 ? 0.1828 0.2891 0.2395 -0.0146 0.0277  0.0802  165 VAL   A O   
3791 C  CB  A VAL   A 165 ? 0.1909 0.2790 0.2583 -0.0205 0.0460  0.0922  165 VAL   A CB  
3792 C  CB  B VAL   A 165 ? 0.2096 0.2633 0.2192 -0.0182 0.0427  0.0812  165 VAL   A CB  
3793 C  CG1 A VAL   A 165 ? 0.2052 0.2848 0.2723 -0.0286 0.0475  0.0719  165 VAL   A CG1 
3794 C  CG1 B VAL   A 165 ? 0.2201 0.2672 0.2291 -0.0214 0.0428  0.0676  165 VAL   A CG1 
3795 C  CG2 A VAL   A 165 ? 0.2028 0.2733 0.2646 -0.0165 0.0434  0.0990  165 VAL   A CG2 
3796 C  CG2 B VAL   A 165 ? 0.2186 0.2589 0.2209 -0.0093 0.0329  0.0852  165 VAL   A CG2 
3815 N  N   A SER   A 166 ? 0.1290 0.3131 0.2894 -0.0060 0.0226  0.1111  166 SER   A N   
3816 N  N   B SER   A 166 ? 0.1929 0.3066 0.2776 -0.0148 -0.0004 0.0803  166 SER   A N   
3817 C  CA  A SER   A 166 ? 0.1466 0.3349 0.3135 -0.0142 0.0102  0.1050  166 SER   A CA  
3818 C  CA  B SER   A 166 ? 0.2030 0.3281 0.3043 -0.0158 -0.0234 0.0701  166 SER   A CA  
3819 C  C   A SER   A 166 ? 0.1559 0.3520 0.3011 -0.0231 -0.0137 0.0868  166 SER   A C   
3820 C  C   B SER   A 166 ? 0.1897 0.3374 0.3045 -0.0140 -0.0468 0.0645  166 SER   A C   
3821 O  O   A SER   A 166 ? 0.1750 0.3615 0.3143 -0.0263 -0.0143 0.0705  166 SER   A O   
3822 O  O   B SER   A 166 ? 0.1769 0.3376 0.3109 -0.0145 -0.0687 0.0616  166 SER   A O   
3823 C  CB  A SER   A 166 ? 0.1737 0.3453 0.3591 -0.0046 0.0183  0.0936  166 SER   A CB  
3824 C  CB  B SER   A 166 ? 0.2246 0.3408 0.3363 -0.0079 -0.0263 0.0559  166 SER   A CB  
3825 O  OG  A SER   A 166 ? 0.2154 0.3565 0.4006 -0.0067 0.0295  0.0890  166 SER   A OG  
3826 O  OG  B SER   A 166 ? 0.2502 0.3528 0.3661 -0.0089 -0.0208 0.0509  166 SER   A OG  
3837 N  N   A SER   A 167 ? 0.1672 0.3601 0.2863 -0.0096 -0.0171 0.0763  167 SER   A N   
3838 N  N   B SER   A 167 ? 0.1971 0.3475 0.2882 -0.0040 -0.0432 0.0606  167 SER   A N   
3839 C  CA  A SER   A 167 ? 0.2048 0.3663 0.2836 -0.0003 -0.0273 0.0516  167 SER   A CA  
3840 C  CA  B SER   A 167 ? 0.2187 0.3558 0.2806 0.0021  -0.0402 0.0442  167 SER   A CA  
3841 C  C   A SER   A 167 ? 0.2142 0.3682 0.2788 0.0092  -0.0134 0.0340  167 SER   A C   
3842 C  C   B SER   A 167 ? 0.2189 0.3620 0.2772 0.0104  -0.0226 0.0312  167 SER   A C   
3843 O  O   A SER   A 167 ? 0.2300 0.3740 0.2832 0.0101  -0.0212 0.0317  167 SER   A O   
3844 O  O   B SER   A 167 ? 0.2292 0.3662 0.2796 0.0113  -0.0322 0.0302  167 SER   A O   
3845 C  CB  A SER   A 167 ? 0.2234 0.3704 0.2879 0.0062  -0.0245 0.0560  167 SER   A CB  
3846 C  CB  B SER   A 167 ? 0.2332 0.3584 0.2797 0.0066  -0.0370 0.0485  167 SER   A CB  
3847 O  OG  A SER   A 167 ? 0.2351 0.3719 0.2938 0.0104  -0.0153 0.0584  167 SER   A OG  
3848 O  OG  B SER   A 167 ? 0.2426 0.3591 0.2813 0.0104  -0.0300 0.0508  167 SER   A OG  
3859 N  N   . PHE   A 168 ? 0.2068 0.3646 0.2700 0.0194  -0.0060 0.0250  168 PHE   A N   
3860 C  CA  . PHE   A 168 ? 0.2096 0.3658 0.2966 0.0167  0.0068  0.0168  168 PHE   A CA  
3861 C  C   . PHE   A 168 ? 0.2639 0.4043 0.3732 -0.0086 0.0158  0.0050  168 PHE   A C   
3862 O  O   . PHE   A 168 ? 0.2541 0.4079 0.3989 -0.0288 0.0384  0.0211  168 PHE   A O   
3863 C  CB  . PHE   A 168 ? 0.1886 0.3308 0.2665 0.0186  0.0070  0.0210  168 PHE   A CB  
3864 C  CG  . PHE   A 168 ? 0.1782 0.2997 0.2455 0.0162  0.0013  0.0251  168 PHE   A CG  
3865 C  CD1 . PHE   A 168 ? 0.1798 0.2952 0.2374 0.0053  -0.0007 0.0401  168 PHE   A CD1 
3866 C  CD2 . PHE   A 168 ? 0.1669 0.2770 0.2404 0.0096  0.0128  0.0192  168 PHE   A CD2 
3867 C  CE1 . PHE   A 168 ? 0.1719 0.2845 0.2412 -0.0016 -0.0054 0.0468  168 PHE   A CE1 
3868 C  CE2 . PHE   A 168 ? 0.1773 0.2644 0.2493 0.0082  0.0160  0.0351  168 PHE   A CE2 
3869 C  CZ  . PHE   A 168 ? 0.1763 0.2737 0.2487 0.0007  0.0065  0.0458  168 PHE   A CZ  
3880 N  N   . LEU   A 169 ? 0.3510 0.4451 0.4675 -0.0230 -0.0094 -0.0267 169 LEU   A N   
3881 C  CA  . LEU   A 169 ? 0.4448 0.4966 0.5738 -0.0267 -0.0336 -0.0416 169 LEU   A CA  
3882 C  C   . LEU   A 169 ? 0.4739 0.5118 0.6254 -0.0280 -0.0474 -0.0403 169 LEU   A C   
3883 O  O   . LEU   A 169 ? 0.4907 0.5158 0.6416 -0.0304 -0.0518 -0.0398 169 LEU   A O   
3884 C  CB  . LEU   A 169 ? 0.4944 0.5278 0.6164 -0.0306 -0.0417 -0.0589 169 LEU   A CB  
3885 C  CG  . LEU   A 169 ? 0.5273 0.5510 0.6442 -0.0336 -0.0440 -0.0754 169 LEU   A CG  
3886 C  CD1 . LEU   A 169 ? 0.5384 0.5594 0.6602 -0.0336 -0.0441 -0.0808 169 LEU   A CD1 
3887 C  CD2 . LEU   A 169 ? 0.5411 0.5573 0.6551 -0.0347 -0.0419 -0.0802 169 LEU   A CD2 
3888 O  OXT . LEU   A 169 ? 0.4830 0.5177 0.6362 -0.0290 -0.0477 -0.0395 169 LEU   A OXT 
3900 N  N   A SER   B 1   ? 0.3563 0.3437 0.3109 -0.1016 -0.0802 0.0544  1   SER   B N   
3901 N  N   B SER   B 1   ? 0.3294 0.2998 0.3089 -0.1058 -0.0567 0.0170  1   SER   B N   
3902 C  CA  A SER   B 1   ? 0.3469 0.3492 0.3202 -0.1076 -0.0887 0.0437  1   SER   B CA  
3903 C  CA  B SER   B 1   ? 0.3178 0.3063 0.3065 -0.1129 -0.0627 0.0091  1   SER   B CA  
3904 C  C   A SER   B 1   ? 0.3254 0.3521 0.3196 -0.1078 -0.0995 0.0549  1   SER   B C   
3905 C  C   B SER   B 1   ? 0.2981 0.3177 0.3068 -0.1095 -0.0797 0.0298  1   SER   B C   
3906 O  O   A SER   B 1   ? 0.3349 0.3540 0.2974 -0.0991 -0.0992 0.0555  1   SER   B O   
3907 O  O   B SER   B 1   ? 0.3038 0.3215 0.2906 -0.1038 -0.0755 0.0266  1   SER   B O   
3908 C  CB  A SER   B 1   ? 0.3554 0.3503 0.3430 -0.1109 -0.0768 0.0268  1   SER   B CB  
3909 C  CB  B SER   B 1   ? 0.3230 0.2983 0.3181 -0.1205 -0.0475 -0.0187 1   SER   B CB  
3910 O  OG  A SER   B 1   ? 0.3674 0.3610 0.3875 -0.1096 -0.0580 0.0200  1   SER   B OG  
3911 O  OG  B SER   B 1   ? 0.3299 0.3025 0.3488 -0.1242 -0.0354 -0.0312 1   SER   B OG  
3926 N  N   A MET   B 2   ? 0.3034 0.3497 0.3410 -0.1112 -0.0924 0.0865  2   MET   B N   
3927 N  N   B MET   B 2   ? 0.2820 0.3212 0.3189 -0.1066 -0.0859 0.0726  2   MET   B N   
3928 C  CA  A MET   B 2   ? 0.2875 0.3510 0.3667 -0.0979 -0.0830 0.1092  2   MET   B CA  
3929 C  CA  B MET   B 2   ? 0.2718 0.3289 0.3325 -0.0886 -0.0882 0.1101  2   MET   B CA  
3930 C  C   A MET   B 2   ? 0.2526 0.3347 0.3399 -0.0852 -0.0922 0.1357  2   MET   B C   
3931 C  C   B MET   B 2   ? 0.2460 0.3216 0.3223 -0.0818 -0.0918 0.1364  2   MET   B C   
3932 O  O   A MET   B 2   ? 0.2468 0.3464 0.3460 -0.0766 -0.1051 0.1332  2   MET   B O   
3933 O  O   B MET   B 2   ? 0.2421 0.3308 0.3272 -0.0748 -0.1013 0.1346  2   MET   B O   
3934 C  CB  A MET   B 2   ? 0.3146 0.3789 0.4503 -0.0800 -0.0531 0.0873  2   MET   B CB  
3935 C  CB  B MET   B 2   ? 0.2947 0.3535 0.3832 -0.0632 -0.0747 0.1055  2   MET   B CB  
3936 C  CG  A MET   B 2   ? 0.3407 0.4034 0.5339 -0.0614 -0.0274 0.0737  2   MET   B CG  
3937 C  CG  B MET   B 2   ? 0.3148 0.3732 0.4213 -0.0382 -0.0669 0.1131  2   MET   B CG  
3938 S  SD  A MET   B 2   ? 0.3661 0.4270 0.6107 -0.0453 -0.0078 0.0604  2   MET   B SD  
3939 S  SD  B MET   B 2   ? 0.3331 0.3924 0.4518 -0.0144 -0.0698 0.1191  2   MET   B SD  
3940 C  CE  A MET   B 2   ? 0.3637 0.4289 0.6161 -0.0476 0.0016  0.0579  2   MET   B CE  
3941 C  CE  B MET   B 2   ? 0.3329 0.3928 0.4627 -0.0163 -0.0576 0.1127  2   MET   B CE  
3960 N  N   . VAL   B 3   ? 0.2256 0.3046 0.3138 -0.0854 -0.0861 0.1578  3   VAL   B N   
3961 C  CA  . VAL   B 3   ? 0.2174 0.2722 0.3066 -0.0790 -0.0845 0.1408  3   VAL   B CA  
3962 C  C   . VAL   B 3   ? 0.2000 0.2666 0.2767 -0.0707 -0.0733 0.1217  3   VAL   B C   
3963 O  O   . VAL   B 3   ? 0.1992 0.2928 0.2828 -0.0725 -0.0737 0.1323  3   VAL   B O   
3964 C  CB  . VAL   B 3   ? 0.2399 0.2629 0.3689 -0.0777 -0.0740 0.1209  3   VAL   B CB  
3965 C  CG1 . VAL   B 3   ? 0.2489 0.2497 0.3906 -0.0864 -0.0761 0.1138  3   VAL   B CG1 
3966 C  CG2 . VAL   B 3   ? 0.2397 0.2675 0.3839 -0.0777 -0.0499 0.1339  3   VAL   B CG2 
3977 N  N   . ASN   B 4   ? 0.1915 0.2314 0.2444 -0.0628 -0.0655 0.0961  4   ASN   B N   
3978 C  CA  . ASN   B 4   ? 0.1998 0.2358 0.2001 -0.0631 -0.0581 0.0558  4   ASN   B CA  
3979 C  C   . ASN   B 4   ? 0.2011 0.2551 0.1860 -0.0675 -0.0537 0.0426  4   ASN   B C   
3980 O  O   . ASN   B 4   ? 0.2012 0.2604 0.2005 -0.0607 -0.0505 0.0250  4   ASN   B O   
3981 C  CB  . ASN   B 4   ? 0.2011 0.2251 0.1892 -0.0589 -0.0650 0.0482  4   ASN   B CB  
3982 C  CG  . ASN   B 4   ? 0.1976 0.2048 0.1662 -0.0593 -0.0601 0.0419  4   ASN   B CG  
3983 O  OD1 . ASN   B 4   ? 0.2027 0.1939 0.1763 -0.0584 -0.0537 0.0383  4   ASN   B OD1 
3984 N  ND2 . ASN   B 4   ? 0.2195 0.2119 0.1711 -0.0395 -0.0405 0.0360  4   ASN   B ND2 
3991 N  N   . SER   B 5   ? 0.2063 0.2722 0.1928 -0.0738 -0.0401 0.0335  5   SER   B N   
3992 C  CA  . SER   B 5   ? 0.2350 0.3067 0.2072 -0.0612 -0.0159 0.0312  5   SER   B CA  
3993 C  C   . SER   B 5   ? 0.2581 0.3107 0.2521 -0.0790 0.0104  0.0309  5   SER   B C   
3994 O  O   . SER   B 5   ? 0.2769 0.3033 0.3377 -0.0689 0.0485  0.0306  5   SER   B O   
3995 C  CB  . SER   B 5   ? 0.2503 0.3275 0.2247 -0.0505 -0.0002 0.0427  5   SER   B CB  
3996 O  OG  . SER   B 5   ? 0.2847 0.3570 0.2882 -0.0368 0.0053  0.0541  5   SER   B OG  
4002 N  N   . PHE   B 6   ? 0.2794 0.3267 0.2336 -0.0905 0.0307  0.0349  6   PHE   B N   
4003 C  CA  . PHE   B 6   ? 0.2946 0.3307 0.1898 -0.1079 0.0363  0.0137  6   PHE   B CA  
4004 C  C   . PHE   B 6   ? 0.3422 0.3540 0.2587 -0.1113 0.0635  -0.0260 6   PHE   B C   
4005 O  O   . PHE   B 6   ? 0.3543 0.3838 0.3001 -0.0983 0.0504  -0.0298 6   PHE   B O   
4006 C  CB  . PHE   B 6   ? 0.2661 0.3137 0.1634 -0.1043 0.0126  0.0128  6   PHE   B CB  
4007 C  CG  . PHE   B 6   ? 0.2300 0.2874 0.1726 -0.1002 -0.0143 0.0135  6   PHE   B CG  
4008 C  CD1 . PHE   B 6   ? 0.2303 0.2601 0.1666 -0.0914 -0.0262 0.0131  6   PHE   B CD1 
4009 C  CD2 . PHE   B 6   ? 0.2023 0.2856 0.1709 -0.0747 -0.0096 0.0464  6   PHE   B CD2 
4010 C  CE1 . PHE   B 6   ? 0.2272 0.2318 0.1709 -0.0736 -0.0270 0.0255  6   PHE   B CE1 
4011 C  CE2 . PHE   B 6   ? 0.2054 0.2660 0.1996 -0.0627 0.0024  0.0487  6   PHE   B CE2 
4012 C  CZ  . PHE   B 6   ? 0.2119 0.2391 0.1853 -0.0617 -0.0153 0.0340  6   PHE   B CZ  
4022 N  N   A SER   B 7   ? 0.3685 0.3477 0.2799 -0.1220 0.0894  -0.0439 7   SER   B N   
4023 N  N   B SER   B 7   ? 0.3535 0.3373 0.2686 -0.1211 0.0770  -0.0454 7   SER   B N   
4024 C  CA  A SER   B 7   ? 0.3977 0.3577 0.3283 -0.1148 0.1010  -0.0492 7   SER   B CA  
4025 C  CA  B SER   B 7   ? 0.3672 0.3351 0.3027 -0.1162 0.0790  -0.0532 7   SER   B CA  
4026 C  C   A SER   B 7   ? 0.4011 0.3523 0.3268 -0.1131 0.1159  -0.0623 7   SER   B C   
4027 C  C   B SER   B 7   ? 0.3618 0.3271 0.3076 -0.1150 0.0909  -0.0651 7   SER   B C   
4028 O  O   A SER   B 7   ? 0.4116 0.3556 0.3353 -0.1149 0.1222  -0.0661 7   SER   B O   
4029 O  O   B SER   B 7   ? 0.3704 0.3237 0.3174 -0.1237 0.0848  -0.0734 7   SER   B O   
4030 C  CB  A SER   B 7   ? 0.4150 0.3681 0.3754 -0.1102 0.1066  -0.0440 7   SER   B CB  
4031 C  CB  B SER   B 7   ? 0.3794 0.3359 0.3260 -0.1131 0.0795  -0.0500 7   SER   B CB  
4032 O  OG  A SER   B 7   ? 0.4272 0.3770 0.4113 -0.1056 0.1085  -0.0427 7   SER   B OG  
4033 O  OG  B SER   B 7   ? 0.3869 0.3358 0.3406 -0.1098 0.0809  -0.0495 7   SER   B OG  
4044 N  N   A GLY   B 8   ? 0.3957 0.3414 0.3232 -0.1029 0.1191  -0.0719 8   GLY   B N   
4045 N  N   B GLY   B 8   ? 0.3514 0.3209 0.3027 -0.0983 0.1007  -0.0727 8   GLY   B N   
4046 C  CA  A GLY   B 8   ? 0.3837 0.3231 0.3113 -0.0988 0.1205  -0.0736 8   GLY   B CA  
4047 C  CA  B GLY   B 8   ? 0.3388 0.3080 0.2942 -0.0880 0.1089  -0.0726 8   GLY   B CA  
4048 C  C   A GLY   B 8   ? 0.3720 0.2979 0.3017 -0.0971 0.1209  -0.0679 8   GLY   B C   
4049 C  C   B GLY   B 8   ? 0.3277 0.2892 0.2861 -0.0820 0.1167  -0.0707 8   GLY   B C   
4050 O  O   A GLY   B 8   ? 0.3831 0.3106 0.3223 -0.0865 0.1216  -0.0754 8   GLY   B O   
4051 O  O   B GLY   B 8   ? 0.3351 0.2905 0.3083 -0.0777 0.1129  -0.0854 8   GLY   B O   
4058 N  N   A TYR   B 9   ? 0.3591 0.2666 0.2720 -0.0922 0.1018  -0.0768 9   TYR   B N   
4059 N  N   B TYR   B 9   ? 0.3156 0.2719 0.2599 -0.0775 0.1037  -0.0755 9   TYR   B N   
4060 C  CA  A TYR   B 9   ? 0.3413 0.2316 0.2504 -0.0848 0.0818  -0.0716 9   TYR   B CA  
4061 C  CA  B TYR   B 9   ? 0.3032 0.2529 0.2420 -0.0743 0.0844  -0.0715 9   TYR   B CA  
4062 C  C   A TYR   B 9   ? 0.3282 0.2324 0.2405 -0.0795 0.0592  -0.0651 9   TYR   B C   
4063 C  C   B TYR   B 9   ? 0.3077 0.2416 0.2381 -0.0722 0.0628  -0.0675 9   TYR   B C   
4064 O  O   A TYR   B 9   ? 0.3342 0.2416 0.2679 -0.0802 0.0576  -0.0527 9   TYR   B O   
4065 O  O   B TYR   B 9   ? 0.3120 0.2510 0.2708 -0.0688 0.0611  -0.0588 9   TYR   B O   
4066 C  CB  A TYR   B 9   ? 0.3399 0.2008 0.2572 -0.0870 0.0753  -0.0593 9   TYR   B CB  
4067 C  CB  B TYR   B 9   ? 0.2899 0.2453 0.2418 -0.0782 0.0768  -0.0654 9   TYR   B CB  
4068 C  CG  A TYR   B 9   ? 0.3359 0.1807 0.2577 -0.0917 0.0698  -0.0608 9   TYR   B CG  
4069 C  CG  B TYR   B 9   ? 0.2766 0.2400 0.2398 -0.0869 0.0656  -0.0646 9   TYR   B CG  
4070 C  CD1 A TYR   B 9   ? 0.3351 0.1761 0.2616 -0.0998 0.0775  -0.0596 9   TYR   B CD1 
4071 C  CD1 B TYR   B 9   ? 0.2697 0.2377 0.2428 -0.0952 0.0685  -0.0649 9   TYR   B CD1 
4072 C  CD2 A TYR   B 9   ? 0.3298 0.1792 0.2458 -0.0858 0.0633  -0.0621 9   TYR   B CD2 
4073 C  CD2 B TYR   B 9   ? 0.2684 0.2413 0.2254 -0.0893 0.0555  -0.0682 9   TYR   B CD2 
4074 C  CE1 A TYR   B 9   ? 0.3328 0.1828 0.2566 -0.0974 0.0807  -0.0704 9   TYR   B CE1 
4075 C  CE1 B TYR   B 9   ? 0.2642 0.2390 0.2424 -0.0993 0.0660  -0.0718 9   TYR   B CE1 
4076 C  CE2 A TYR   B 9   ? 0.3321 0.1767 0.2483 -0.0837 0.0667  -0.0577 9   TYR   B CE2 
4077 C  CE2 B TYR   B 9   ? 0.2673 0.2424 0.2292 -0.0900 0.0529  -0.0664 9   TYR   B CE2 
4078 C  CZ  A TYR   B 9   ? 0.3326 0.1842 0.2597 -0.0886 0.0736  -0.0735 9   TYR   B CZ  
4079 C  CZ  B TYR   B 9   ? 0.2644 0.2452 0.2397 -0.0963 0.0541  -0.0724 9   TYR   B CZ  
4080 O  OH  A TYR   B 9   ? 0.3317 0.1890 0.2751 -0.0892 0.0736  -0.0826 9   TYR   B OH  
4081 O  OH  B TYR   B 9   ? 0.2615 0.2544 0.2605 -0.1004 0.0454  -0.0721 9   TYR   B OH  
4100 N  N   . LEU   B 10  ? 0.3090 0.2183 0.2298 -0.0801 0.0486  -0.0618 10  LEU   B N   
4101 C  CA  . LEU   B 10  ? 0.3116 0.2164 0.2364 -0.1022 0.0003  -0.0397 10  LEU   B CA  
4102 C  C   . LEU   B 10  ? 0.2994 0.2247 0.2319 -0.0950 -0.0218 -0.0290 10  LEU   B C   
4103 O  O   . LEU   B 10  ? 0.2753 0.2281 0.2264 -0.0821 -0.0132 -0.0169 10  LEU   B O   
4104 C  CB  . LEU   B 10  ? 0.3365 0.2148 0.2497 -0.1038 -0.0176 -0.0111 10  LEU   B CB  
4105 C  CG  . LEU   B 10  ? 0.3585 0.2227 0.2766 -0.0971 -0.0501 -0.0008 10  LEU   B CG  
4106 C  CD1 . LEU   B 10  ? 0.3726 0.2283 0.2968 -0.0897 -0.0504 -0.0066 10  LEU   B CD1 
4107 C  CD2 . LEU   B 10  ? 0.3651 0.2315 0.2887 -0.0962 -0.0409 0.0207  10  LEU   B CD2 
4120 N  N   A LYS   B 11  ? 0.3142 0.2441 0.2379 -0.0867 -0.0333 -0.0235 11  LYS   B N   
4121 N  N   B LYS   B 11  ? 0.3109 0.2447 0.2438 -0.0847 -0.0305 -0.0235 11  LYS   B N   
4122 C  CA  A LYS   B 11  ? 0.3272 0.2627 0.2762 -0.0755 -0.0361 -0.0301 11  LYS   B CA  
4123 C  CA  B LYS   B 11  ? 0.3207 0.2638 0.2797 -0.0719 -0.0340 -0.0286 11  LYS   B CA  
4124 C  C   A LYS   B 11  ? 0.3065 0.2391 0.2743 -0.0885 -0.0334 -0.0466 11  LYS   B C   
4125 C  C   B LYS   B 11  ? 0.3015 0.2458 0.2750 -0.0808 -0.0320 -0.0414 11  LYS   B C   
4126 O  O   A LYS   B 11  ? 0.3205 0.2466 0.2917 -0.1021 -0.0370 -0.0728 11  LYS   B O   
4127 O  O   B LYS   B 11  ? 0.3110 0.2592 0.2852 -0.0863 -0.0354 -0.0561 11  LYS   B O   
4128 C  CB  A LYS   B 11  ? 0.3567 0.3033 0.3409 -0.0520 -0.0409 -0.0290 11  LYS   B CB  
4129 C  CB  B LYS   B 11  ? 0.3462 0.2992 0.3399 -0.0502 -0.0386 -0.0268 11  LYS   B CB  
4130 C  CG  A LYS   B 11  ? 0.3804 0.3308 0.4092 -0.0371 -0.0481 -0.0320 11  LYS   B CG  
4131 C  CG  B LYS   B 11  ? 0.3667 0.3235 0.4027 -0.0364 -0.0440 -0.0297 11  LYS   B CG  
4132 C  CD  A LYS   B 11  ? 0.3985 0.3493 0.4640 -0.0266 -0.0533 -0.0330 11  LYS   B CD  
4133 C  CD  B LYS   B 11  ? 0.3824 0.3401 0.4540 -0.0262 -0.0481 -0.0303 11  LYS   B CD  
4134 C  CE  A LYS   B 11  ? 0.4097 0.3617 0.5065 -0.0210 -0.0544 -0.0347 11  LYS   B CE  
4135 C  CE  B LYS   B 11  ? 0.3918 0.3514 0.4936 -0.0206 -0.0491 -0.0309 11  LYS   B CE  
4136 N  NZ  A LYS   B 11  ? 0.4163 0.3691 0.5299 -0.0176 -0.0548 -0.0323 11  LYS   B NZ  
4137 N  NZ  B LYS   B 11  ? 0.3971 0.3579 0.5154 -0.0175 -0.0494 -0.0284 11  LYS   B NZ  
4164 N  N   . LEU   B 12  ? 0.2705 0.2220 0.2676 -0.0770 -0.0342 -0.0479 12  LEU   B N   
4165 C  CA  . LEU   B 12  ? 0.2359 0.1969 0.2769 -0.0639 -0.0223 -0.0373 12  LEU   B CA  
4166 C  C   . LEU   B 12  ? 0.2227 0.2000 0.2842 -0.0626 -0.0418 -0.0319 12  LEU   B C   
4167 O  O   . LEU   B 12  ? 0.2232 0.1981 0.3195 -0.0641 -0.0667 -0.0253 12  LEU   B O   
4168 C  CB  . LEU   B 12  ? 0.2348 0.1733 0.2683 -0.0455 -0.0185 -0.0326 12  LEU   B CB  
4169 C  CG  . LEU   B 12  ? 0.2385 0.1695 0.2698 -0.0441 -0.0073 -0.0214 12  LEU   B CG  
4170 C  CD1 . LEU   B 12  ? 0.2423 0.1656 0.2667 -0.0305 -0.0150 0.0003  12  LEU   B CD1 
4171 C  CD2 . LEU   B 12  ? 0.2522 0.1758 0.2783 -0.0481 -0.0075 -0.0350 12  LEU   B CD2 
4184 N  N   . THR   B 13  ? 0.2177 0.2053 0.2773 -0.0623 -0.0330 -0.0509 13  THR   B N   
4185 C  CA  . THR   B 13  ? 0.2236 0.2073 0.2787 -0.0697 -0.0545 -0.0265 13  THR   B CA  
4186 C  C   . THR   B 13  ? 0.2746 0.2245 0.2971 -0.0846 -0.0828 -0.0197 13  THR   B C   
4187 O  O   . THR   B 13  ? 0.3026 0.2264 0.3183 -0.0854 -0.0472 -0.0284 13  THR   B O   
4188 C  CB  . THR   B 13  ? 0.2066 0.2018 0.2806 -0.0629 -0.0552 -0.0151 13  THR   B CB  
4189 O  OG1 . THR   B 13  ? 0.1945 0.1917 0.2812 -0.0514 -0.0472 -0.0188 13  THR   B OG1 
4190 C  CG2 . THR   B 13  ? 0.2199 0.2071 0.2792 -0.0553 -0.0423 -0.0018 13  THR   B CG2 
4198 N  N   A ASP   B 14  ? 0.2876 0.2387 0.3120 -0.0895 -0.1084 -0.0000 14  ASP   B N   
4199 N  N   B ASP   B 14  ? 0.2860 0.2377 0.3074 -0.0866 -0.1008 0.0016  14  ASP   B N   
4200 C  CA  A ASP   B 14  ? 0.3009 0.2545 0.3402 -0.0854 -0.1102 0.0142  14  ASP   B CA  
4201 C  CA  B ASP   B 14  ? 0.2966 0.2520 0.3273 -0.0810 -0.1014 0.0183  14  ASP   B CA  
4202 C  C   A ASP   B 14  ? 0.2887 0.2357 0.2998 -0.0885 -0.0991 0.0151  14  ASP   B C   
4203 C  C   B ASP   B 14  ? 0.2837 0.2344 0.2938 -0.0829 -0.0981 0.0193  14  ASP   B C   
4204 O  O   A ASP   B 14  ? 0.3140 0.2489 0.3023 -0.0901 -0.0942 0.0221  14  ASP   B O   
4205 O  O   B ASP   B 14  ? 0.3043 0.2431 0.2956 -0.0818 -0.0980 0.0285  14  ASP   B O   
4206 C  CB  A ASP   B 14  ? 0.3192 0.2930 0.4108 -0.0766 -0.1197 0.0232  14  ASP   B CB  
4207 C  CB  B ASP   B 14  ? 0.3138 0.2865 0.3832 -0.0712 -0.1022 0.0302  14  ASP   B CB  
4208 C  CG  A ASP   B 14  ? 0.3397 0.3235 0.4777 -0.0676 -0.1212 0.0153  14  ASP   B CG  
4209 C  CG  B ASP   B 14  ? 0.3311 0.3140 0.4337 -0.0619 -0.0991 0.0258  14  ASP   B CG  
4210 O  OD1 A ASP   B 14  ? 0.3476 0.3302 0.4939 -0.0713 -0.1244 0.0053  14  ASP   B OD1 
4211 O  OD1 B ASP   B 14  ? 0.3372 0.3227 0.4463 -0.0614 -0.0961 0.0214  14  ASP   B OD1 
4212 O  OD2 A ASP   B 14  ? 0.3469 0.3403 0.5120 -0.0626 -0.1191 0.0145  14  ASP   B OD2 
4213 O  OD2 B ASP   B 14  ? 0.3373 0.3271 0.4596 -0.0594 -0.0993 0.0237  14  ASP   B OD2 
4222 N  N   . ASN   B 15  ? 0.2501 0.2068 0.2648 -0.0748 -0.0997 0.0217  15  ASN   B N   
4223 C  CA  . ASN   B 15  ? 0.2074 0.1765 0.2514 -0.0496 -0.0649 0.0074  15  ASN   B CA  
4224 C  C   . ASN   B 15  ? 0.1813 0.1603 0.2401 -0.0321 -0.0516 0.0005  15  ASN   B C   
4225 O  O   . ASN   B 15  ? 0.1784 0.1562 0.2594 -0.0305 -0.0544 -0.0062 15  ASN   B O   
4226 C  CB  . ASN   B 15  ? 0.1954 0.1727 0.2710 -0.0218 -0.0631 0.0045  15  ASN   B CB  
4227 C  CG  . ASN   B 15  ? 0.1787 0.1697 0.2790 -0.0257 -0.0358 0.0092  15  ASN   B CG  
4228 O  OD1 . ASN   B 15  ? 0.1806 0.2020 0.3051 -0.0488 -0.0421 0.0136  15  ASN   B OD1 
4229 N  ND2 . ASN   B 15  ? 0.1785 0.1548 0.2429 -0.0134 -0.0052 -0.0087 15  ASN   B ND2 
4237 N  N   . VAL   B 16  ? 0.1808 0.1524 0.2430 -0.0380 -0.0597 0.0034  16  VAL   B N   
4238 C  CA  . VAL   B 16  ? 0.1819 0.1579 0.2208 -0.0375 -0.0395 -0.0207 16  VAL   B CA  
4239 C  C   . VAL   B 16  ? 0.1825 0.1732 0.2114 -0.0397 -0.0466 -0.0066 16  VAL   B C   
4240 O  O   . VAL   B 16  ? 0.1841 0.1808 0.2357 -0.0311 -0.0439 -0.0280 16  VAL   B O   
4241 C  CB  . VAL   B 16  ? 0.1798 0.1552 0.2323 -0.0224 -0.0325 -0.0222 16  VAL   B CB  
4242 C  CG1 . VAL   B 16  ? 0.1861 0.1587 0.2131 -0.0028 -0.0257 -0.0090 16  VAL   B CG1 
4243 C  CG2 . VAL   B 16  ? 0.1800 0.1587 0.2549 -0.0057 -0.0264 -0.0223 16  VAL   B CG2 
4253 N  N   . TYR   B 17  ? 0.1842 0.1798 0.2016 -0.0379 -0.0318 -0.0181 17  TYR   B N   
4254 C  CA  . TYR   B 17  ? 0.1915 0.1953 0.2077 -0.0483 -0.0435 -0.0020 17  TYR   B CA  
4255 C  C   . TYR   B 17  ? 0.1865 0.1648 0.2044 -0.0439 -0.0225 -0.0138 17  TYR   B C   
4256 O  O   . TYR   B 17  ? 0.1826 0.1716 0.2014 -0.0401 -0.0266 -0.0313 17  TYR   B O   
4257 C  CB  . TYR   B 17  ? 0.2344 0.2529 0.2458 -0.0391 -0.0475 0.0333  17  TYR   B CB  
4258 C  CG  . TYR   B 17  ? 0.2672 0.3152 0.3007 -0.0341 -0.0679 0.0448  17  TYR   B CG  
4259 C  CD1 . TYR   B 17  ? 0.2892 0.3406 0.3348 -0.0348 -0.0718 0.0563  17  TYR   B CD1 
4260 C  CD2 . TYR   B 17  ? 0.2920 0.3497 0.3368 -0.0269 -0.0714 0.0490  17  TYR   B CD2 
4261 C  CE1 . TYR   B 17  ? 0.3108 0.3686 0.3592 -0.0268 -0.0830 0.0591  17  TYR   B CE1 
4262 C  CE2 . TYR   B 17  ? 0.3129 0.3718 0.3618 -0.0146 -0.0881 0.0637  17  TYR   B CE2 
4263 C  CZ  . TYR   B 17  ? 0.3255 0.3767 0.3712 -0.0148 -0.0951 0.0643  17  TYR   B CZ  
4264 O  OH  . TYR   B 17  ? 0.3420 0.3929 0.3869 -0.0073 -0.1029 0.0639  17  TYR   B OH  
4274 N  N   . ILE   B 18  ? 0.1985 0.1686 0.2029 -0.0378 -0.0140 -0.0214 18  ILE   B N   
4275 C  CA  . ILE   B 18  ? 0.2012 0.1611 0.2090 -0.0431 0.0016  -0.0352 18  ILE   B CA  
4276 C  C   . ILE   B 18  ? 0.2102 0.1676 0.2119 -0.0510 -0.0031 -0.0424 18  ILE   B C   
4277 O  O   . ILE   B 18  ? 0.2326 0.1872 0.2251 -0.0466 0.0027  -0.0510 18  ILE   B O   
4278 C  CB  . ILE   B 18  ? 0.2067 0.1618 0.2182 -0.0499 -0.0040 -0.0290 18  ILE   B CB  
4279 C  CG1 . ILE   B 18  ? 0.2049 0.1662 0.2345 -0.0514 0.0008  -0.0227 18  ILE   B CG1 
4280 C  CG2 . ILE   B 18  ? 0.2131 0.1719 0.2179 -0.0510 -0.0116 -0.0257 18  ILE   B CG2 
4281 C  CD1 . ILE   B 18  ? 0.2119 0.1914 0.2609 -0.0476 -0.0175 0.0125  18  ILE   B CD1 
4293 N  N   . LYS   B 19  ? 0.2133 0.1730 0.2233 -0.0317 0.0372  -0.0471 19  LYS   B N   
4294 C  CA  . LYS   B 19  ? 0.2178 0.1753 0.2429 -0.0361 0.0340  -0.0581 19  LYS   B CA  
4295 C  C   . LYS   B 19  ? 0.2037 0.1707 0.2597 -0.0286 0.0384  -0.0794 19  LYS   B C   
4296 O  O   . LYS   B 19  ? 0.1988 0.1749 0.2397 -0.0262 0.0345  -0.0709 19  LYS   B O   
4297 C  CB  . LYS   B 19  ? 0.2485 0.2026 0.2544 -0.0463 0.0501  -0.0462 19  LYS   B CB  
4298 C  CG  . LYS   B 19  ? 0.2823 0.2273 0.2877 -0.0526 0.0583  -0.0511 19  LYS   B CG  
4299 C  CD  . LYS   B 19  ? 0.3165 0.2559 0.3020 -0.0596 0.0769  -0.0465 19  LYS   B CD  
4300 C  CE  . LYS   B 19  ? 0.3458 0.2823 0.3270 -0.0627 0.0683  -0.0524 19  LYS   B CE  
4301 N  NZ  . LYS   B 19  ? 0.3697 0.3004 0.3455 -0.0674 0.0689  -0.0472 19  LYS   B NZ  
4315 N  N   . ASN   B 20  ? 0.1994 0.1850 0.2988 -0.0267 0.0501  -0.0858 20  ASN   B N   
4316 C  CA  . ASN   B 20  ? 0.2018 0.2037 0.3238 -0.0230 0.0446  -0.1069 20  ASN   B CA  
4317 C  C   . ASN   B 20  ? 0.2068 0.2319 0.3099 -0.0242 0.0575  -0.1150 20  ASN   B C   
4318 O  O   . ASN   B 20  ? 0.2286 0.2731 0.3259 -0.0321 0.0585  -0.1127 20  ASN   B O   
4319 C  CB  . ASN   B 20  ? 0.2380 0.2134 0.3595 0.0081  0.0319  -0.1101 20  ASN   B CB  
4320 C  CG  . ASN   B 20  ? 0.2700 0.2210 0.3797 0.0378  0.0290  -0.1161 20  ASN   B CG  
4321 O  OD1 . ASN   B 20  ? 0.3080 0.2477 0.4016 0.0513  0.0222  -0.1193 20  ASN   B OD1 
4322 N  ND2 . ASN   B 20  ? 0.2609 0.2145 0.3740 0.0369  0.0128  -0.1134 20  ASN   B ND2 
4329 N  N   . ALA   B 21  ? 0.2085 0.2146 0.3103 -0.0317 0.0631  -0.0965 21  ALA   B N   
4330 C  CA  . ALA   B 21  ? 0.2217 0.2190 0.3249 -0.0346 0.0499  -0.0770 21  ALA   B CA  
4331 C  C   . ALA   B 21  ? 0.2163 0.1931 0.3012 -0.0300 0.0567  -0.0532 21  ALA   B C   
4332 O  O   . ALA   B 21  ? 0.2229 0.1775 0.2875 -0.0408 0.0497  -0.0440 21  ALA   B O   
4333 C  CB  . ALA   B 21  ? 0.2389 0.2480 0.3527 -0.0500 0.0500  -0.0521 21  ALA   B CB  
4339 N  N   . ASP   B 22  ? 0.2074 0.1752 0.2807 -0.0294 0.0480  -0.0494 22  ASP   B N   
4340 C  CA  . ASP   B 22  ? 0.2002 0.1699 0.2596 -0.0163 0.0433  -0.0438 22  ASP   B CA  
4341 C  C   . ASP   B 22  ? 0.1906 0.1642 0.2148 -0.0254 0.0347  -0.0267 22  ASP   B C   
4342 O  O   . ASP   B 22  ? 0.1961 0.1742 0.2300 -0.0149 0.0208  -0.0213 22  ASP   B O   
4343 C  CB  . ASP   B 22  ? 0.2033 0.1804 0.3090 -0.0041 0.0363  -0.0319 22  ASP   B CB  
4344 C  CG  . ASP   B 22  ? 0.2001 0.2032 0.3449 0.0074  0.0141  -0.0309 22  ASP   B CG  
4345 O  OD1 . ASP   B 22  ? 0.2093 0.1883 0.3368 0.0050  -0.0086 -0.0216 22  ASP   B OD1 
4346 O  OD2 . ASP   B 22  ? 0.2082 0.2302 0.4045 0.0181  -0.0120 -0.0370 22  ASP   B OD2 
4351 N  N   . ILE   B 23  ? 0.1916 0.1574 0.1941 -0.0147 0.0029  0.0125  23  ILE   B N   
4352 C  CA  . ILE   B 23  ? 0.1803 0.1506 0.1811 -0.0147 -0.0027 0.0059  23  ILE   B CA  
4353 C  C   . ILE   B 23  ? 0.1759 0.1547 0.1706 -0.0053 -0.0107 0.0007  23  ILE   B C   
4354 O  O   . ILE   B 23  ? 0.1593 0.1499 0.1738 -0.0079 -0.0053 0.0013  23  ILE   B O   
4355 C  CB  . ILE   B 23  ? 0.1706 0.1544 0.2027 -0.0213 0.0012  0.0150  23  ILE   B CB  
4356 C  CG1 . ILE   B 23  ? 0.1708 0.1650 0.2174 -0.0106 0.0077  0.0229  23  ILE   B CG1 
4357 C  CG2 . ILE   B 23  ? 0.1798 0.1745 0.2094 -0.0171 -0.0008 0.0043  23  ILE   B CG2 
4358 C  CD1 . ILE   B 23  ? 0.1875 0.1718 0.2226 -0.0051 0.0061  0.0147  23  ILE   B CD1 
4370 N  N   . VAL   B 24  ? 0.1718 0.1552 0.1771 -0.0119 -0.0094 -0.0004 24  VAL   B N   
4371 C  CA  . VAL   B 24  ? 0.1645 0.1634 0.2245 -0.0064 -0.0173 0.0019  24  VAL   B CA  
4372 C  C   . VAL   B 24  ? 0.1628 0.1616 0.2232 -0.0079 -0.0088 0.0012  24  VAL   B C   
4373 O  O   . VAL   B 24  ? 0.1625 0.1701 0.2304 -0.0185 -0.0071 0.0074  24  VAL   B O   
4374 C  CB  . VAL   B 24  ? 0.1701 0.1706 0.2313 0.0014  -0.0222 0.0021  24  VAL   B CB  
4375 C  CG1 . VAL   B 24  ? 0.1663 0.1742 0.2592 -0.0121 -0.0192 -0.0003 24  VAL   B CG1 
4376 C  CG2 . VAL   B 24  ? 0.1814 0.1973 0.2152 0.0043  -0.0237 -0.0156 24  VAL   B CG2 
4386 N  N   . GLU   B 25  ? 0.1838 0.1727 0.2305 -0.0080 0.0063  0.0000  25  GLU   B N   
4387 C  CA  . GLU   B 25  ? 0.1998 0.2034 0.2474 0.0024  0.0239  -0.0123 25  GLU   B CA  
4388 C  C   . GLU   B 25  ? 0.1976 0.1947 0.2001 -0.0131 0.0256  -0.0104 25  GLU   B C   
4389 O  O   . GLU   B 25  ? 0.2023 0.2169 0.2198 -0.0128 0.0256  0.0011  25  GLU   B O   
4390 C  CB  . GLU   B 25  ? 0.2264 0.2511 0.3257 0.0290  0.0389  -0.0145 25  GLU   B CB  
4391 C  CG  . GLU   B 25  ? 0.2686 0.3128 0.4312 0.0323  0.0331  -0.0127 25  GLU   B CG  
4392 C  CD  . GLU   B 25  ? 0.3254 0.3627 0.5090 0.0207  0.0350  -0.0139 25  GLU   B CD  
4393 O  OE1 . GLU   B 25  ? 0.3338 0.3904 0.5363 0.0237  0.0487  -0.0169 25  GLU   B OE1 
4394 O  OE2 . GLU   B 25  ? 0.3253 0.3909 0.5392 0.0164  0.0242  -0.0168 25  GLU   B OE2 
4401 N  N   A GLU   B 26  ? 0.1985 0.1832 0.1911 -0.0262 0.0237  -0.0148 26  GLU   B N   
4402 N  N   B GLU   B 26  ? 0.1908 0.1852 0.2036 -0.0241 0.0191  -0.0006 26  GLU   B N   
4403 C  CA  A GLU   B 26  ? 0.2052 0.1944 0.1977 -0.0370 0.0067  -0.0118 26  GLU   B CA  
4404 C  CA  B GLU   B 26  ? 0.1895 0.1932 0.2201 -0.0309 0.0039  0.0119  26  GLU   B CA  
4405 C  C   A GLU   B 26  ? 0.1834 0.1883 0.1756 -0.0326 0.0056  0.0035  26  GLU   B C   
4406 C  C   B GLU   B 26  ? 0.1758 0.1878 0.1866 -0.0296 0.0066  0.0154  26  GLU   B C   
4407 O  O   A GLU   B 26  ? 0.2017 0.2065 0.1798 -0.0275 0.0024  0.0069  26  GLU   B O   
4408 O  O   B GLU   B 26  ? 0.1913 0.2037 0.1877 -0.0255 0.0061  0.0170  26  GLU   B O   
4409 C  CB  A GLU   B 26  ? 0.2361 0.2107 0.2116 -0.0448 0.0147  -0.0007 26  GLU   B CB  
4410 C  CB  B GLU   B 26  ? 0.2052 0.2057 0.2570 -0.0331 0.0042  0.0336  26  GLU   B CB  
4411 C  CG  A GLU   B 26  ? 0.2720 0.2328 0.2440 -0.0433 0.0273  -0.0116 26  GLU   B CG  
4412 C  CG  B GLU   B 26  ? 0.2272 0.2260 0.3080 -0.0288 0.0109  0.0302  26  GLU   B CG  
4413 C  CD  A GLU   B 26  ? 0.2916 0.2391 0.2404 -0.0537 0.0464  -0.0332 26  GLU   B CD  
4414 C  CD  B GLU   B 26  ? 0.2311 0.2269 0.3317 -0.0370 0.0209  0.0232  26  GLU   B CD  
4415 O  OE1 A GLU   B 26  ? 0.3016 0.2303 0.2219 -0.0537 0.0845  -0.0382 26  GLU   B OE1 
4416 O  OE1 B GLU   B 26  ? 0.2355 0.2296 0.3593 -0.0518 0.0472  0.0074  26  GLU   B OE1 
4417 O  OE2 A GLU   B 26  ? 0.2934 0.2529 0.2535 -0.0581 0.0513  -0.0073 26  GLU   B OE2 
4418 O  OE2 B GLU   B 26  ? 0.2232 0.2208 0.3255 -0.0305 0.0242  0.0226  26  GLU   B OE2 
4431 N  N   . ALA   B 27  ? 0.1636 0.1765 0.1722 -0.0253 0.0092  0.0170  27  ALA   B N   
4432 C  CA  . ALA   B 27  ? 0.1617 0.1767 0.1879 -0.0160 0.0011  0.0266  27  ALA   B CA  
4433 C  C   . ALA   B 27  ? 0.1663 0.1945 0.2058 -0.0134 0.0141  0.0392  27  ALA   B C   
4434 O  O   . ALA   B 27  ? 0.1703 0.2028 0.2196 -0.0068 0.0107  0.0520  27  ALA   B O   
4435 C  CB  . ALA   B 27  ? 0.1700 0.1592 0.1982 -0.0191 0.0033  0.0184  27  ALA   B CB  
4442 N  N   . LYS   B 28  ? 0.1587 0.2109 0.2566 -0.0200 0.0226  0.0578  28  LYS   B N   
4443 C  CA  . LYS   B 28  ? 0.1778 0.2496 0.2808 -0.0066 0.0549  0.0808  28  LYS   B CA  
4444 C  C   . LYS   B 28  ? 0.1996 0.2594 0.2623 -0.0018 0.0672  0.0670  28  LYS   B C   
4445 O  O   . LYS   B 28  ? 0.2291 0.2657 0.2639 -0.0060 0.0733  0.0577  28  LYS   B O   
4446 C  CB  . LYS   B 28  ? 0.1987 0.2915 0.3302 0.0059  0.0708  0.0997  28  LYS   B CB  
4447 C  CG  . LYS   B 28  ? 0.2207 0.3462 0.3773 0.0163  0.0750  0.1119  28  LYS   B CG  
4448 C  CD  . LYS   B 28  ? 0.2526 0.3972 0.4352 0.0229  0.0861  0.1192  28  LYS   B CD  
4449 C  CE  . LYS   B 28  ? 0.2837 0.4322 0.4797 0.0321  0.0868  0.1243  28  LYS   B CE  
4450 N  NZ  . LYS   B 28  ? 0.3333 0.4620 0.5093 0.0433  0.0842  0.1269  28  LYS   B NZ  
4464 N  N   . LYS   B 29  ? 0.2166 0.2812 0.2626 0.0107  0.0580  0.0548  29  LYS   B N   
4465 C  CA  . LYS   B 29  ? 0.2606 0.3188 0.2915 0.0099  0.0533  0.0537  29  LYS   B CA  
4466 C  C   . LYS   B 29  ? 0.2531 0.3237 0.2532 0.0102  0.0355  0.0713  29  LYS   B C   
4467 O  O   . LYS   B 29  ? 0.2776 0.3512 0.2612 0.0154  0.0411  0.0752  29  LYS   B O   
4468 C  CB  . LYS   B 29  ? 0.3157 0.3531 0.3766 0.0080  0.0540  0.0423  29  LYS   B CB  
4469 C  CG  . LYS   B 29  ? 0.3599 0.3809 0.4588 0.0073  0.0631  0.0360  29  LYS   B CG  
4470 C  CD  . LYS   B 29  ? 0.3961 0.3995 0.5262 0.0051  0.0740  0.0286  29  LYS   B CD  
4471 C  CE  . LYS   B 29  ? 0.4149 0.4106 0.5743 0.0023  0.0852  0.0256  29  LYS   B CE  
4472 N  NZ  . LYS   B 29  ? 0.4266 0.4188 0.5972 0.0006  0.0919  0.0235  29  LYS   B NZ  
4486 N  N   . VAL   B 30  ? 0.2223 0.3032 0.2432 -0.0038 0.0235  0.0697  30  VAL   B N   
4487 C  CA  . VAL   B 30  ? 0.2155 0.2876 0.2751 -0.0188 -0.0102 0.0712  30  VAL   B CA  
4488 C  C   . VAL   B 30  ? 0.1905 0.2791 0.2432 -0.0254 -0.0103 0.0879  30  VAL   B C   
4489 O  O   . VAL   B 30  ? 0.2040 0.3001 0.2511 -0.0239 -0.0085 0.0951  30  VAL   B O   
4490 C  CB  . VAL   B 30  ? 0.2283 0.2796 0.3294 -0.0358 -0.0350 0.0752  30  VAL   B CB  
4491 C  CG1 . VAL   B 30  ? 0.2389 0.2878 0.3322 -0.0319 -0.0328 0.0721  30  VAL   B CG1 
4492 C  CG2 . VAL   B 30  ? 0.2465 0.2806 0.3523 -0.0456 -0.0370 0.0600  30  VAL   B CG2 
4502 N  N   . LYS   B 31  ? 0.1814 0.2425 0.2726 -0.0351 -0.0124 0.0894  31  LYS   B N   
4503 C  CA  . LYS   B 31  ? 0.1682 0.2405 0.3090 -0.0381 -0.0185 0.0901  31  LYS   B CA  
4504 C  C   . LYS   B 31  ? 0.1589 0.2042 0.2630 -0.0400 -0.0296 0.0810  31  LYS   B C   
4505 O  O   . LYS   B 31  ? 0.1559 0.2189 0.2767 -0.0316 -0.0237 0.1008  31  LYS   B O   
4506 C  CB  . LYS   B 31  ? 0.1788 0.2928 0.3670 -0.0288 0.0133  0.1082  31  LYS   B CB  
4507 C  CG  . LYS   B 31  ? 0.2224 0.3423 0.4160 -0.0303 0.0329  0.1192  31  LYS   B CG  
4508 C  CD  . LYS   B 31  ? 0.2529 0.3912 0.4697 -0.0290 0.0322  0.1127  31  LYS   B CD  
4509 C  CE  . LYS   B 31  ? 0.2851 0.4172 0.5172 -0.0254 0.0223  0.1046  31  LYS   B CE  
4510 N  NZ  . LYS   B 31  ? 0.3092 0.4384 0.5336 -0.0146 0.0138  0.0941  31  LYS   B NZ  
4524 N  N   . PRO   B 32  ? 0.1796 0.1717 0.2052 -0.0411 -0.0428 0.0554  32  PRO   B N   
4525 C  CA  . PRO   B 32  ? 0.1935 0.1677 0.1639 -0.0434 -0.0417 0.0326  32  PRO   B CA  
4526 C  C   . PRO   B 32  ? 0.1981 0.1561 0.1775 -0.0489 -0.0588 0.0431  32  PRO   B C   
4527 O  O   . PRO   B 32  ? 0.2074 0.1526 0.2280 -0.0443 -0.0798 0.0389  32  PRO   B O   
4528 C  CB  . PRO   B 32  ? 0.2045 0.1661 0.1685 -0.0436 -0.0342 0.0163  32  PRO   B CB  
4529 C  CG  . PRO   B 32  ? 0.2220 0.1568 0.1787 -0.0401 -0.0567 0.0257  32  PRO   B CG  
4530 C  CD  . PRO   B 32  ? 0.2045 0.1558 0.2093 -0.0349 -0.0577 0.0324  32  PRO   B CD  
4538 N  N   . THR   B 33  ? 0.2018 0.1513 0.1615 -0.0395 -0.0486 0.0299  33  THR   B N   
4539 C  CA  . THR   B 33  ? 0.2092 0.1546 0.1655 -0.0433 -0.0535 0.0319  33  THR   B CA  
4540 C  C   . THR   B 33  ? 0.2072 0.1408 0.1599 -0.0360 -0.0500 0.0241  33  THR   B C   
4541 O  O   . THR   B 33  ? 0.2272 0.1514 0.1629 -0.0500 -0.0585 0.0271  33  THR   B O   
4542 C  CB  . THR   B 33  ? 0.2236 0.1649 0.1696 -0.0280 -0.0661 0.0273  33  THR   B CB  
4543 O  OG1 . THR   B 33  ? 0.2111 0.1708 0.1712 -0.0349 -0.0581 0.0344  33  THR   B OG1 
4544 C  CG2 . THR   B 33  ? 0.2506 0.1677 0.1922 -0.0153 -0.0563 0.0218  33  THR   B CG2 
4552 N  N   . VAL   B 34  ? 0.1897 0.1398 0.1495 -0.0340 -0.0416 0.0203  34  VAL   B N   
4553 C  CA  . VAL   B 34  ? 0.1736 0.1410 0.1551 -0.0289 -0.0447 0.0107  34  VAL   B CA  
4554 C  C   . VAL   B 34  ? 0.1592 0.1376 0.1406 -0.0326 -0.0257 0.0083  34  VAL   B C   
4555 O  O   . VAL   B 34  ? 0.1764 0.1400 0.1380 -0.0314 -0.0338 0.0050  34  VAL   B O   
4556 C  CB  . VAL   B 34  ? 0.1831 0.1471 0.1689 -0.0063 -0.0365 0.0059  34  VAL   B CB  
4557 C  CG1 . VAL   B 34  ? 0.1761 0.1615 0.1817 -0.0064 -0.0210 -0.0030 34  VAL   B CG1 
4558 C  CG2 . VAL   B 34  ? 0.1879 0.1503 0.1983 -0.0096 -0.0276 0.0081  34  VAL   B CG2 
4568 N  N   . VAL   B 35  ? 0.1511 0.1344 0.1168 -0.0320 -0.0111 0.0065  35  VAL   B N   
4569 C  CA  . VAL   B 35  ? 0.1450 0.1306 0.1244 -0.0199 -0.0095 0.0059  35  VAL   B CA  
4570 C  C   . VAL   B 35  ? 0.1374 0.1262 0.1286 -0.0204 -0.0110 0.0024  35  VAL   B C   
4571 O  O   . VAL   B 35  ? 0.1433 0.1321 0.1249 -0.0244 0.0028  -0.0086 35  VAL   B O   
4572 C  CB  . VAL   B 35  ? 0.1482 0.1458 0.1393 -0.0187 -0.0004 0.0041  35  VAL   B CB  
4573 C  CG1 . VAL   B 35  ? 0.1431 0.1578 0.1631 -0.0267 0.0002  -0.0027 35  VAL   B CG1 
4574 C  CG2 . VAL   B 35  ? 0.1519 0.1540 0.1615 -0.0128 -0.0027 -0.0003 35  VAL   B CG2 
4584 N  N   . VAL   B 36  ? 0.1384 0.1288 0.1318 -0.0186 -0.0141 0.0062  36  VAL   B N   
4585 C  CA  . VAL   B 36  ? 0.1352 0.1251 0.1242 -0.0157 -0.0092 0.0041  36  VAL   B CA  
4586 C  C   . VAL   B 36  ? 0.1356 0.1300 0.1028 -0.0085 -0.0036 0.0081  36  VAL   B C   
4587 O  O   . VAL   B 36  ? 0.1402 0.1359 0.1266 -0.0094 -0.0056 -0.0080 36  VAL   B O   
4588 C  CB  . VAL   B 36  ? 0.1364 0.1303 0.1282 -0.0162 -0.0048 0.0028  36  VAL   B CB  
4589 C  CG1 . VAL   B 36  ? 0.1349 0.1418 0.1478 -0.0215 -0.0039 0.0050  36  VAL   B CG1 
4590 C  CG2 . VAL   B 36  ? 0.1391 0.1401 0.1428 -0.0149 -0.0179 0.0104  36  VAL   B CG2 
4600 N  N   . ASN   B 37  ? 0.1366 0.1331 0.1074 -0.0021 -0.0061 0.0080  37  ASN   B N   
4601 C  CA  . ASN   B 37  ? 0.1352 0.1318 0.1218 -0.0023 -0.0139 0.0041  37  ASN   B CA  
4602 C  C   . ASN   B 37  ? 0.1344 0.1341 0.1388 0.0045  -0.0100 0.0057  37  ASN   B C   
4603 O  O   . ASN   B 37  ? 0.1412 0.1380 0.1369 0.0037  0.0051  0.0088  37  ASN   B O   
4604 C  CB  . ASN   B 37  ? 0.1359 0.1314 0.1195 -0.0051 -0.0172 0.0033  37  ASN   B CB  
4605 C  CG  . ASN   B 37  ? 0.1431 0.1324 0.1348 -0.0021 -0.0103 0.0025  37  ASN   B CG  
4606 O  OD1 . ASN   B 37  ? 0.1493 0.1385 0.1478 0.0105  -0.0153 0.0012  37  ASN   B OD1 
4607 N  ND2 . ASN   B 37  ? 0.1468 0.1281 0.1329 0.0015  -0.0152 0.0046  37  ASN   B ND2 
4614 N  N   . ALA   B 38  ? 0.1474 0.1294 0.1309 0.0087  0.0038  0.0102  38  ALA   B N   
4615 C  CA  . ALA   B 38  ? 0.1516 0.1340 0.1399 0.0049  0.0040  0.0075  38  ALA   B CA  
4616 C  C   . ALA   B 38  ? 0.1461 0.1294 0.1448 0.0045  0.0068  0.0141  38  ALA   B C   
4617 O  O   . ALA   B 38  ? 0.1649 0.1400 0.1474 0.0077  0.0032  0.0120  38  ALA   B O   
4618 C  CB  . ALA   B 38  ? 0.1783 0.1458 0.1452 -0.0069 0.0097  0.0100  38  ALA   B CB  
4624 N  N   . ALA   B 39  ? 0.1472 0.1305 0.1320 0.0099  0.0003  0.0065  39  ALA   B N   
4625 C  CA  . ALA   B 39  ? 0.1521 0.1365 0.1376 0.0125  -0.0077 0.0050  39  ALA   B CA  
4626 C  C   . ALA   B 39  ? 0.1635 0.1503 0.1196 0.0114  -0.0048 0.0002  39  ALA   B C   
4627 O  O   . ALA   B 39  ? 0.1729 0.1511 0.1387 0.0051  0.0005  0.0017  39  ALA   B O   
4628 C  CB  . ALA   B 39  ? 0.1484 0.1416 0.1618 -0.0007 -0.0031 0.0065  39  ALA   B CB  
4634 N  N   . ASN   B 40  ? 0.1668 0.1696 0.1198 -0.0041 0.0051  -0.0109 40  ASN   B N   
4635 C  CA  . ASN   B 40  ? 0.1730 0.1714 0.1388 -0.0004 -0.0018 -0.0029 40  ASN   B CA  
4636 C  C   . ASN   B 40  ? 0.1755 0.1685 0.1301 0.0067  -0.0059 -0.0039 40  ASN   B C   
4637 O  O   . ASN   B 40  ? 0.1772 0.1605 0.1254 0.0128  -0.0089 0.0008  40  ASN   B O   
4638 C  CB  . ASN   B 40  ? 0.1856 0.1613 0.1518 0.0120  -0.0163 0.0124  40  ASN   B CB  
4639 C  CG  . ASN   B 40  ? 0.1937 0.1711 0.1954 0.0059  -0.0263 0.0215  40  ASN   B CG  
4640 O  OD1 . ASN   B 40  ? 0.1921 0.1659 0.2911 0.0034  -0.0416 0.0268  40  ASN   B OD1 
4641 N  ND2 . ASN   B 40  ? 0.1923 0.1684 0.2032 0.0074  -0.0290 0.0171  40  ASN   B ND2 
4648 N  N   . VAL   B 41  ? 0.1842 0.1757 0.1357 0.0137  0.0057  -0.0019 41  VAL   B N   
4649 C  CA  . VAL   B 41  ? 0.1859 0.1871 0.1462 0.0100  0.0020  -0.0075 41  VAL   B CA  
4650 C  C   . VAL   B 41  ? 0.1855 0.1857 0.1336 0.0146  -0.0046 -0.0041 41  VAL   B C   
4651 O  O   . VAL   B 41  ? 0.1888 0.1903 0.1393 0.0161  -0.0122 -0.0126 41  VAL   B O   
4652 C  CB  . VAL   B 41  ? 0.2052 0.2015 0.1678 -0.0032 0.0228  -0.0195 41  VAL   B CB  
4653 C  CG1 . VAL   B 41  ? 0.2050 0.2050 0.1715 0.0019  0.0415  -0.0279 41  VAL   B CG1 
4654 C  CG2 . VAL   B 41  ? 0.2222 0.2197 0.1705 -0.0148 0.0239  -0.0176 41  VAL   B CG2 
4664 N  N   . TYR   B 42  ? 0.2002 0.1828 0.1347 0.0202  -0.0181 -0.0013 42  TYR   B N   
4665 C  CA  . TYR   B 42  ? 0.2047 0.1850 0.1245 0.0254  -0.0297 -0.0142 42  TYR   B CA  
4666 C  C   . TYR   B 42  ? 0.1851 0.1726 0.1354 0.0229  -0.0185 -0.0129 42  TYR   B C   
4667 O  O   . TYR   B 42  ? 0.1879 0.1843 0.1859 0.0199  -0.0284 -0.0180 42  TYR   B O   
4668 C  CB  . TYR   B 42  ? 0.2314 0.2070 0.1463 0.0217  -0.0315 0.0011  42  TYR   B CB  
4669 C  CG  . TYR   B 42  ? 0.2351 0.2206 0.1449 0.0057  -0.0326 0.0194  42  TYR   B CG  
4670 C  CD1 . TYR   B 42  ? 0.2222 0.2161 0.1275 0.0031  -0.0161 0.0106  42  TYR   B CD1 
4671 C  CD2 . TYR   B 42  ? 0.2520 0.2369 0.1945 0.0066  -0.0217 0.0204  42  TYR   B CD2 
4672 C  CE1 . TYR   B 42  ? 0.2341 0.2358 0.1355 0.0028  -0.0186 0.0018  42  TYR   B CE1 
4673 C  CE2 . TYR   B 42  ? 0.2533 0.2544 0.1883 0.0133  0.0023  0.0292  42  TYR   B CE2 
4674 C  CZ  . TYR   B 42  ? 0.2579 0.2639 0.1702 0.0240  0.0084  0.0063  42  TYR   B CZ  
4675 O  OH  . TYR   B 42  ? 0.2928 0.2965 0.2180 0.0436  0.0163  0.0120  42  TYR   B OH  
4685 N  N   . LEU   B 43  ? 0.1755 0.1585 0.1175 0.0064  -0.0142 -0.0154 43  LEU   B N   
4686 C  CA  . LEU   B 43  ? 0.1736 0.1614 0.1168 0.0062  -0.0188 -0.0092 43  LEU   B CA  
4687 C  C   . LEU   B 43  ? 0.1742 0.1622 0.1159 0.0052  -0.0151 -0.0005 43  LEU   B C   
4688 O  O   . LEU   B 43  ? 0.1727 0.1626 0.1545 0.0032  -0.0229 0.0021  43  LEU   B O   
4689 C  CB  . LEU   B 43  ? 0.1664 0.1491 0.1418 0.0041  -0.0213 -0.0018 43  LEU   B CB  
4690 C  CG  . LEU   B 43  ? 0.1728 0.1466 0.1568 -0.0015 -0.0248 -0.0034 43  LEU   B CG  
4691 C  CD1 . LEU   B 43  ? 0.1796 0.1488 0.1871 -0.0025 -0.0421 -0.0045 43  LEU   B CD1 
4692 C  CD2 . LEU   B 43  ? 0.1689 0.1498 0.1579 -0.0060 -0.0261 -0.0057 43  LEU   B CD2 
4704 N  N   . LYS   B 44  ? 0.1734 0.1566 0.1347 0.0095  -0.0075 -0.0059 44  LYS   B N   
4705 C  CA  . LYS   B 44  ? 0.1860 0.1670 0.1379 0.0154  -0.0119 0.0002  44  LYS   B CA  
4706 C  C   . LYS   B 44  ? 0.1785 0.1552 0.1443 0.0174  -0.0150 -0.0033 44  LYS   B C   
4707 O  O   . LYS   B 44  ? 0.1924 0.1562 0.1728 0.0031  -0.0101 -0.0025 44  LYS   B O   
4708 C  CB  . LYS   B 44  ? 0.2191 0.1876 0.1562 0.0206  -0.0216 -0.0080 44  LYS   B CB  
4709 C  CG  . LYS   B 44  ? 0.2590 0.2146 0.2075 0.0174  -0.0501 0.0062  44  LYS   B CG  
4710 C  CD  . LYS   B 44  ? 0.2955 0.2347 0.2714 -0.0006 -0.0655 -0.0039 44  LYS   B CD  
4711 C  CE  . LYS   B 44  ? 0.3242 0.2604 0.3219 -0.0098 -0.0697 0.0086  44  LYS   B CE  
4712 N  NZ  . LYS   B 44  ? 0.3388 0.2687 0.3456 -0.0086 -0.0800 0.0201  44  LYS   B NZ  
4726 N  N   . HIS   B 45  ? 0.1721 0.1638 0.1321 0.0052  -0.0107 0.0105  45  HIS   B N   
4727 C  CA  . HIS   B 45  ? 0.1699 0.1621 0.1388 0.0018  -0.0146 -0.0013 45  HIS   B CA  
4728 C  C   . HIS   B 45  ? 0.1900 0.1784 0.1869 0.0160  -0.0184 0.0026  45  HIS   B C   
4729 O  O   . HIS   B 45  ? 0.2081 0.2076 0.2353 0.0389  0.0029  0.0065  45  HIS   B O   
4730 C  CB  . HIS   B 45  ? 0.1610 0.1607 0.1396 0.0005  -0.0079 -0.0013 45  HIS   B CB  
4731 C  CG  . HIS   B 45  ? 0.1648 0.1554 0.1360 -0.0038 -0.0143 0.0043  45  HIS   B CG  
4732 N  ND1 . HIS   B 45  ? 0.1634 0.1496 0.1513 0.0000  -0.0141 -0.0034 45  HIS   B ND1 
4733 C  CD2 . HIS   B 45  ? 0.1811 0.1571 0.1649 -0.0096 -0.0260 0.0056  45  HIS   B CD2 
4734 C  CE1 . HIS   B 45  ? 0.1779 0.1363 0.1476 -0.0028 -0.0305 -0.0045 45  HIS   B CE1 
4735 N  NE2 . HIS   B 45  ? 0.1850 0.1489 0.1598 0.0021  -0.0250 -0.0038 45  HIS   B NE2 
4743 N  N   A GLY   B 46  ? 0.1964 0.1727 0.2207 0.0219  -0.0345 0.0090  46  GLY   B N   
4744 N  N   B GLY   B 46  ? 0.2004 0.1806 0.2101 0.0214  -0.0332 0.0165  46  GLY   B N   
4745 C  CA  A GLY   B 46  ? 0.2142 0.1815 0.2646 0.0191  -0.0402 0.0050  46  GLY   B CA  
4746 C  CA  B GLY   B 46  ? 0.2167 0.1912 0.2397 0.0190  -0.0410 0.0200  46  GLY   B CA  
4747 C  C   A GLY   B 46  ? 0.2231 0.1962 0.2999 0.0228  -0.0333 0.0061  46  GLY   B C   
4748 C  C   B GLY   B 46  ? 0.2254 0.2041 0.2649 0.0205  -0.0374 0.0271  46  GLY   B C   
4749 O  O   A GLY   B 46  ? 0.2324 0.2022 0.3767 0.0280  -0.0059 -0.0200 46  GLY   B O   
4750 O  O   B GLY   B 46  ? 0.2339 0.2137 0.2936 0.0238  -0.0218 0.0369  46  GLY   B O   
4757 N  N   . GLY   B 47  ? 0.2311 0.2130 0.2729 0.0036  -0.0287 0.0078  47  GLY   B N   
4758 C  CA  . GLY   B 47  ? 0.2224 0.1866 0.2364 0.0039  -0.0271 0.0098  47  GLY   B CA  
4759 C  C   . GLY   B 47  ? 0.1944 0.1657 0.1946 -0.0025 -0.0039 0.0137  47  GLY   B C   
4760 O  O   . GLY   B 47  ? 0.2026 0.1541 0.1870 0.0040  -0.0099 0.0139  47  GLY   B O   
4765 N  N   . GLY   B 48  ? 0.1679 0.1549 0.2034 0.0071  -0.0142 0.0207  48  GLY   B N   
4766 C  CA  . GLY   B 48  ? 0.1634 0.1499 0.2029 -0.0064 -0.0088 0.0103  48  GLY   B CA  
4767 C  C   . GLY   B 48  ? 0.1562 0.1477 0.1799 -0.0030 -0.0036 -0.0014 48  GLY   B C   
4768 O  O   . GLY   B 48  ? 0.1451 0.1454 0.2183 0.0003  -0.0121 0.0051  48  GLY   B O   
4772 N  N   . VAL   B 49  ? 0.1578 0.1489 0.1737 0.0128  -0.0029 0.0028  49  VAL   B N   
4773 C  CA  . VAL   B 49  ? 0.1514 0.1571 0.1535 0.0138  -0.0109 -0.0137 49  VAL   B CA  
4774 C  C   . VAL   B 49  ? 0.1476 0.1483 0.1361 0.0080  -0.0083 -0.0042 49  VAL   B C   
4775 O  O   . VAL   B 49  ? 0.1567 0.1505 0.1574 0.0065  -0.0029 0.0006  49  VAL   B O   
4776 C  CB  . VAL   B 49  ? 0.1568 0.1741 0.1910 0.0033  -0.0273 -0.0112 49  VAL   B CB  
4777 C  CG1 . VAL   B 49  ? 0.1525 0.1866 0.1962 0.0086  -0.0386 0.0019  49  VAL   B CG1 
4778 C  CG2 . VAL   B 49  ? 0.1805 0.1940 0.2149 -0.0119 -0.0480 -0.0167 49  VAL   B CG2 
4788 N  N   . ALA   B 50  ? 0.1459 0.1412 0.1446 -0.0008 -0.0032 0.0057  50  ALA   B N   
4789 C  CA  . ALA   B 50  ? 0.1514 0.1352 0.1513 0.0065  -0.0036 -0.0027 50  ALA   B CA  
4790 C  C   . ALA   B 50  ? 0.1499 0.1367 0.1538 0.0038  0.0021  0.0036  50  ALA   B C   
4791 O  O   . ALA   B 50  ? 0.1534 0.1396 0.1515 0.0066  0.0008  0.0005  50  ALA   B O   
4792 C  CB  . ALA   B 50  ? 0.1603 0.1350 0.1545 -0.0053 -0.0111 0.0013  50  ALA   B CB  
4798 N  N   . GLY   B 51  ? 0.1486 0.1496 0.1660 0.0114  -0.0094 0.0086  51  GLY   B N   
4799 C  CA  . GLY   B 51  ? 0.1488 0.1529 0.1863 0.0186  -0.0149 0.0095  51  GLY   B CA  
4800 C  C   . GLY   B 51  ? 0.1494 0.1522 0.1842 0.0182  -0.0068 0.0106  51  GLY   B C   
4801 O  O   . GLY   B 51  ? 0.1477 0.1628 0.1855 0.0082  -0.0097 0.0002  51  GLY   B O   
4805 N  N   . ALA   B 52  ? 0.1448 0.1426 0.1764 0.0137  -0.0084 0.0027  52  ALA   B N   
4806 C  CA  . ALA   B 52  ? 0.1539 0.1505 0.1746 0.0138  -0.0010 -0.0077 52  ALA   B CA  
4807 C  C   . ALA   B 52  ? 0.1417 0.1516 0.1687 0.0106  -0.0060 -0.0052 52  ALA   B C   
4808 O  O   . ALA   B 52  ? 0.1440 0.1545 0.1914 0.0041  -0.0037 0.0010  52  ALA   B O   
4809 C  CB  . ALA   B 52  ? 0.1702 0.1468 0.1912 0.0094  -0.0005 -0.0101 52  ALA   B CB  
4815 N  N   . LEU   B 53  ? 0.1420 0.1500 0.1547 0.0092  -0.0080 0.0026  53  LEU   B N   
4816 C  CA  . LEU   B 53  ? 0.1419 0.1571 0.1478 0.0110  -0.0101 -0.0004 53  LEU   B CA  
4817 C  C   . LEU   B 53  ? 0.1459 0.1521 0.1460 0.0112  0.0006  0.0045  53  LEU   B C   
4818 O  O   . LEU   B 53  ? 0.1494 0.1592 0.1534 0.0028  0.0046  0.0113  53  LEU   B O   
4819 C  CB  . LEU   B 53  ? 0.1441 0.1596 0.1585 0.0085  -0.0034 0.0148  53  LEU   B CB  
4820 C  CG  . LEU   B 53  ? 0.1410 0.1658 0.1617 0.0009  -0.0020 0.0256  53  LEU   B CG  
4821 C  CD1 . LEU   B 53  ? 0.1544 0.1847 0.2006 0.0160  -0.0006 -0.0030 53  LEU   B CD1 
4822 C  CD2 . LEU   B 53  ? 0.1590 0.1983 0.1874 -0.0070 -0.0109 -0.0106 53  LEU   B CD2 
4834 N  N   . ASN   B 54  ? 0.1486 0.1390 0.1421 0.0018  -0.0084 0.0001  54  ASN   B N   
4835 C  CA  . ASN   B 54  ? 0.1532 0.1558 0.1485 0.0046  -0.0067 -0.0024 54  ASN   B CA  
4836 C  C   . ASN   B 54  ? 0.1462 0.1579 0.1803 0.0040  -0.0039 -0.0038 54  ASN   B C   
4837 O  O   . ASN   B 54  ? 0.1448 0.1587 0.1858 -0.0022 0.0027  -0.0020 54  ASN   B O   
4838 C  CB  . ASN   B 54  ? 0.1565 0.1676 0.1790 0.0057  -0.0082 -0.0006 54  ASN   B CB  
4839 C  CG  . ASN   B 54  ? 0.1538 0.1731 0.1754 0.0016  -0.0083 -0.0040 54  ASN   B CG  
4840 O  OD1 . ASN   B 54  ? 0.1512 0.1671 0.1821 0.0020  -0.0131 -0.0182 54  ASN   B OD1 
4841 N  ND2 . ASN   B 54  ? 0.1627 0.1877 0.2075 -0.0001 -0.0273 0.0133  54  ASN   B ND2 
4848 N  N   . LYS   B 55  ? 0.1440 0.1569 0.2030 0.0121  -0.0023 0.0011  55  LYS   B N   
4849 C  CA  . LYS   B 55  ? 0.1469 0.1710 0.2233 0.0154  -0.0008 -0.0032 55  LYS   B CA  
4850 C  C   . LYS   B 55  ? 0.1491 0.1725 0.2173 0.0114  0.0035  -0.0060 55  LYS   B C   
4851 O  O   . LYS   B 55  ? 0.1506 0.1870 0.2244 0.0107  0.0043  -0.0127 55  LYS   B O   
4852 C  CB  . LYS   B 55  ? 0.1640 0.1817 0.2664 0.0293  0.0139  -0.0024 55  LYS   B CB  
4853 C  CG  . LYS   B 55  ? 0.2089 0.2177 0.3468 0.0280  0.0159  0.0125  55  LYS   B CG  
4854 C  CD  . LYS   B 55  ? 0.2508 0.2488 0.4083 0.0412  0.0332  0.0098  55  LYS   B CD  
4855 C  CE  . LYS   B 55  ? 0.2748 0.2715 0.4690 0.0450  0.0509  0.0124  55  LYS   B CE  
4856 N  NZ  . LYS   B 55  ? 0.2820 0.2914 0.5019 0.0466  0.0403  0.0254  55  LYS   B NZ  
4870 N  N   . ALA   B 56  ? 0.1515 0.1756 0.1912 0.0120  -0.0053 -0.0104 56  ALA   B N   
4871 C  CA  . ALA   B 56  ? 0.1645 0.1913 0.1876 0.0012  0.0002  -0.0085 56  ALA   B CA  
4872 C  C   . ALA   B 56  ? 0.1637 0.1879 0.1745 -0.0017 0.0169  -0.0056 56  ALA   B C   
4873 O  O   . ALA   B 56  ? 0.1718 0.2020 0.2000 0.0031  0.0254  -0.0033 56  ALA   B O   
4874 C  CB  . ALA   B 56  ? 0.1826 0.2090 0.1973 -0.0085 -0.0024 -0.0111 56  ALA   B CB  
4880 N  N   . THR   B 57  ? 0.1489 0.1746 0.1910 -0.0053 0.0259  -0.0006 57  THR   B N   
4881 C  CA  . THR   B 57  ? 0.1636 0.1720 0.1864 -0.0016 0.0183  -0.0020 57  THR   B CA  
4882 C  C   . THR   B 57  ? 0.1604 0.1796 0.2097 -0.0043 0.0238  -0.0040 57  THR   B C   
4883 O  O   . THR   B 57  ? 0.1669 0.1815 0.2280 -0.0214 0.0181  -0.0108 57  THR   B O   
4884 C  CB  . THR   B 57  ? 0.1710 0.1590 0.1551 -0.0065 0.0073  0.0076  57  THR   B CB  
4885 O  OG1 . THR   B 57  ? 0.1639 0.1556 0.1847 -0.0089 0.0114  0.0014  57  THR   B OG1 
4886 C  CG2 . THR   B 57  ? 0.1708 0.1714 0.1613 -0.0117 0.0064  0.0016  57  THR   B CG2 
4894 N  N   . ASN   B 58  ? 0.1537 0.1984 0.2235 -0.0143 0.0079  -0.0280 58  ASN   B N   
4895 C  CA  . ASN   B 58  ? 0.1787 0.2461 0.2738 -0.0273 0.0266  -0.0230 58  ASN   B CA  
4896 C  C   . ASN   B 58  ? 0.1535 0.2217 0.2291 -0.0162 -0.0016 -0.0123 58  ASN   B C   
4897 O  O   . ASN   B 58  ? 0.1547 0.2254 0.2387 -0.0155 -0.0029 -0.0211 58  ASN   B O   
4898 C  CB  . ASN   B 58  ? 0.2606 0.3222 0.3865 -0.0467 0.0763  -0.0187 58  ASN   B CB  
4899 C  CG  . ASN   B 58  ? 0.3833 0.4128 0.5367 -0.0517 0.0999  0.0078  58  ASN   B CG  
4900 O  OD1 . ASN   B 58  ? 0.4001 0.4323 0.5942 -0.0518 0.1017  0.0172  58  ASN   B OD1 
4901 N  ND2 . ASN   B 58  ? 0.5034 0.5034 0.5845 -0.0562 0.1110  0.0171  58  ASN   B ND2 
4908 N  N   . ASN   B 59  ? 0.1532 0.2042 0.2106 -0.0087 -0.0108 -0.0079 59  ASN   B N   
4909 C  CA  . ASN   B 59  ? 0.1576 0.2052 0.2030 -0.0104 -0.0201 -0.0063 59  ASN   B CA  
4910 C  C   . ASN   B 59  ? 0.1535 0.1943 0.1992 -0.0141 -0.0203 -0.0100 59  ASN   B C   
4911 O  O   . ASN   B 59  ? 0.1530 0.1945 0.1968 -0.0114 -0.0160 -0.0015 59  ASN   B O   
4912 C  CB  . ASN   B 59  ? 0.1641 0.2227 0.2190 -0.0035 -0.0331 -0.0020 59  ASN   B CB  
4913 C  CG  . ASN   B 59  ? 0.1746 0.2367 0.2315 0.0032  -0.0387 0.0043  59  ASN   B CG  
4914 O  OD1 . ASN   B 59  ? 0.1770 0.2365 0.2289 -0.0002 -0.0333 0.0182  59  ASN   B OD1 
4915 N  ND2 . ASN   B 59  ? 0.1843 0.2443 0.2311 -0.0072 -0.0451 0.0030  59  ASN   B ND2 
4922 N  N   . ALA   B 60  ? 0.1510 0.1805 0.1970 -0.0138 -0.0030 -0.0110 60  ALA   B N   
4923 C  CA  . ALA   B 60  ? 0.1666 0.1697 0.1951 -0.0174 -0.0031 0.0011  60  ALA   B CA  
4924 C  C   . ALA   B 60  ? 0.1645 0.1619 0.1681 -0.0150 -0.0036 0.0036  60  ALA   B C   
4925 O  O   . ALA   B 60  ? 0.1661 0.1657 0.1806 -0.0164 -0.0050 -0.0096 60  ALA   B O   
4926 C  CB  . ALA   B 60  ? 0.1839 0.1673 0.2125 -0.0137 0.0041  0.0017  60  ALA   B CB  
4932 N  N   . MET   B 61  ? 0.1523 0.1522 0.1629 -0.0130 -0.0003 0.0001  61  MET   B N   
4933 C  CA  . MET   B 61  ? 0.1526 0.1494 0.1514 -0.0098 -0.0112 -0.0060 61  MET   B CA  
4934 C  C   . MET   B 61  ? 0.1518 0.1462 0.1560 -0.0134 -0.0198 -0.0001 61  MET   B C   
4935 O  O   . MET   B 61  ? 0.1599 0.1453 0.1501 -0.0051 -0.0115 -0.0157 61  MET   B O   
4936 C  CB  . MET   B 61  ? 0.1483 0.1516 0.1623 0.0008  -0.0075 -0.0069 61  MET   B CB  
4937 C  CG  . MET   B 61  ? 0.1461 0.1532 0.1607 -0.0030 -0.0033 -0.0038 61  MET   B CG  
4938 S  SD  . MET   B 61  ? 0.1454 0.1495 0.1829 -0.0031 -0.0064 -0.0086 61  MET   B SD  
4939 C  CE  . MET   B 61  ? 0.1479 0.1703 0.1973 -0.0039 -0.0064 -0.0197 61  MET   B CE  
4949 N  N   . GLN   B 62  ? 0.1515 0.1545 0.1476 -0.0080 -0.0192 -0.0042 62  GLN   B N   
4950 C  CA  . GLN   B 62  ? 0.1601 0.1581 0.1553 -0.0059 -0.0165 0.0020  62  GLN   B CA  
4951 C  C   . GLN   B 62  ? 0.1581 0.1597 0.1616 -0.0092 -0.0254 -0.0067 62  GLN   B C   
4952 O  O   . GLN   B 62  ? 0.1663 0.1630 0.1767 -0.0041 -0.0256 -0.0070 62  GLN   B O   
4953 C  CB  . GLN   B 62  ? 0.1639 0.1585 0.1735 0.0038  -0.0124 0.0038  62  GLN   B CB  
4954 C  CG  . GLN   B 62  ? 0.1666 0.1646 0.1756 -0.0004 -0.0310 -0.0012 62  GLN   B CG  
4955 C  CD  . GLN   B 62  ? 0.1685 0.1650 0.1508 0.0015  -0.0288 0.0027  62  GLN   B CD  
4956 O  OE1 . GLN   B 62  ? 0.1756 0.1633 0.1716 -0.0011 -0.0313 -0.0076 62  GLN   B OE1 
4957 N  NE2 . GLN   B 62  ? 0.1694 0.1689 0.1600 0.0077  -0.0236 -0.0053 62  GLN   B NE2 
4966 N  N   . VAL   B 63  ? 0.1594 0.1632 0.1882 -0.0113 -0.0279 -0.0110 63  VAL   B N   
4967 C  CA  . VAL   B 63  ? 0.1731 0.1679 0.2158 -0.0109 -0.0347 -0.0063 63  VAL   B CA  
4968 C  C   . VAL   B 63  ? 0.1712 0.1561 0.1738 -0.0183 -0.0370 -0.0214 63  VAL   B C   
4969 O  O   . VAL   B 63  ? 0.1847 0.1608 0.1817 -0.0127 -0.0434 -0.0212 63  VAL   B O   
4970 C  CB  . VAL   B 63  ? 0.1707 0.1782 0.2382 -0.0217 -0.0337 -0.0164 63  VAL   B CB  
4971 C  CG1 . VAL   B 63  ? 0.1775 0.1888 0.2561 -0.0251 -0.0262 -0.0143 63  VAL   B CG1 
4972 C  CG2 . VAL   B 63  ? 0.1653 0.1971 0.2435 -0.0121 -0.0423 -0.0115 63  VAL   B CG2 
4982 N  N   . GLU   B 64  ? 0.1689 0.1529 0.1660 -0.0117 -0.0306 -0.0144 64  GLU   B N   
4983 C  CA  . GLU   B 64  ? 0.1685 0.1469 0.1688 -0.0154 -0.0342 -0.0059 64  GLU   B CA  
4984 C  C   . GLU   B 64  ? 0.1650 0.1485 0.1604 -0.0075 -0.0354 -0.0156 64  GLU   B C   
4985 O  O   . GLU   B 64  ? 0.1711 0.1513 0.1658 -0.0079 -0.0221 -0.0184 64  GLU   B O   
4986 C  CB  . GLU   B 64  ? 0.1680 0.1552 0.1754 -0.0175 -0.0238 -0.0058 64  GLU   B CB  
4987 C  CG  . GLU   B 64  ? 0.1755 0.1524 0.1704 -0.0239 -0.0289 -0.0206 64  GLU   B CG  
4988 C  CD  . GLU   B 64  ? 0.1794 0.1724 0.1736 -0.0290 -0.0356 -0.0048 64  GLU   B CD  
4989 O  OE1 . GLU   B 64  ? 0.1771 0.1869 0.1762 -0.0326 -0.0190 -0.0275 64  GLU   B OE1 
4990 O  OE2 . GLU   B 64  ? 0.1896 0.1782 0.1841 -0.0312 -0.0365 -0.0105 64  GLU   B OE2 
4997 N  N   . SER   B 65  ? 0.1659 0.1475 0.1515 -0.0113 -0.0236 -0.0150 65  SER   B N   
4998 C  CA  . SER   B 65  ? 0.1597 0.1432 0.1618 -0.0025 -0.0261 -0.0088 65  SER   B CA  
4999 C  C   . SER   B 65  ? 0.1653 0.1451 0.1673 0.0087  -0.0348 -0.0166 65  SER   B C   
5000 O  O   . SER   B 65  ? 0.1674 0.1536 0.1658 0.0052  -0.0270 -0.0179 65  SER   B O   
5001 C  CB  . SER   B 65  ? 0.1604 0.1513 0.1686 -0.0046 -0.0157 -0.0123 65  SER   B CB  
5002 O  OG  . SER   B 65  ? 0.1635 0.1532 0.1562 -0.0044 -0.0153 -0.0217 65  SER   B OG  
5008 N  N   . ASP   B 66  ? 0.1791 0.1534 0.1568 -0.0005 -0.0372 -0.0225 66  ASP   B N   
5009 C  CA  . ASP   B 66  ? 0.1840 0.1654 0.1553 0.0098  -0.0400 -0.0175 66  ASP   B CA  
5010 C  C   . ASP   B 66  ? 0.1898 0.1666 0.1457 -0.0054 -0.0354 -0.0252 66  ASP   B C   
5011 O  O   . ASP   B 66  ? 0.1952 0.1763 0.1589 0.0025  -0.0283 -0.0262 66  ASP   B O   
5012 C  CB  . ASP   B 66  ? 0.1948 0.1734 0.1792 0.0142  -0.0458 -0.0243 66  ASP   B CB  
5013 C  CG  . ASP   B 66  ? 0.2241 0.1843 0.1985 0.0198  -0.0567 -0.0034 66  ASP   B CG  
5014 O  OD1 . ASP   B 66  ? 0.2513 0.1828 0.2072 0.0155  -0.0490 0.0089  66  ASP   B OD1 
5015 O  OD2 . ASP   B 66  ? 0.2397 0.2105 0.2756 0.0424  -0.0583 -0.0086 66  ASP   B OD2 
5020 N  N   . ASP   B 67  ? 0.1803 0.1601 0.1491 -0.0086 -0.0264 -0.0198 67  ASP   B N   
5021 C  CA  . ASP   B 67  ? 0.1946 0.1579 0.1624 -0.0054 -0.0312 -0.0109 67  ASP   B CA  
5022 C  C   . ASP   B 67  ? 0.1880 0.1572 0.1746 0.0009  -0.0258 -0.0187 67  ASP   B C   
5023 O  O   . ASP   B 67  ? 0.1930 0.1629 0.1798 0.0038  -0.0216 -0.0311 67  ASP   B O   
5024 C  CB  . ASP   B 67  ? 0.2111 0.1680 0.1835 -0.0099 -0.0453 -0.0152 67  ASP   B CB  
5025 C  CG  . ASP   B 67  ? 0.2495 0.1698 0.1993 -0.0046 -0.0687 -0.0180 67  ASP   B CG  
5026 O  OD1 . ASP   B 67  ? 0.2762 0.1711 0.2190 -0.0060 -0.0675 -0.0165 67  ASP   B OD1 
5027 O  OD2 . ASP   B 67  ? 0.2616 0.1838 0.2155 0.0119  -0.0725 -0.0146 67  ASP   B OD2 
5032 N  N   . TYR   B 68  ? 0.1823 0.1562 0.1711 0.0016  -0.0407 -0.0270 68  TYR   B N   
5033 C  CA  . TYR   B 68  ? 0.1787 0.1748 0.1847 0.0088  -0.0436 -0.0320 68  TYR   B CA  
5034 C  C   . TYR   B 68  ? 0.1747 0.1716 0.1884 0.0082  -0.0308 -0.0369 68  TYR   B C   
5035 O  O   . TYR   B 68  ? 0.1803 0.1802 0.1884 0.0074  -0.0335 -0.0503 68  TYR   B O   
5036 C  CB  . TYR   B 68  ? 0.1836 0.1954 0.1826 0.0094  -0.0579 -0.0380 68  TYR   B CB  
5037 C  CG  . TYR   B 68  ? 0.1997 0.2119 0.2091 0.0128  -0.0490 -0.0657 68  TYR   B CG  
5038 C  CD1 . TYR   B 68  ? 0.2009 0.2205 0.2306 -0.0071 -0.0426 -0.0823 68  TYR   B CD1 
5039 C  CD2 . TYR   B 68  ? 0.2022 0.2254 0.2241 0.0171  -0.0656 -0.0564 68  TYR   B CD2 
5040 C  CE1 . TYR   B 68  ? 0.2008 0.2342 0.2474 -0.0014 -0.0269 -0.0839 68  TYR   B CE1 
5041 C  CE2 . TYR   B 68  ? 0.1991 0.2292 0.2394 0.0156  -0.0431 -0.0838 68  TYR   B CE2 
5042 C  CZ  . TYR   B 68  ? 0.1930 0.2326 0.2483 0.0059  -0.0326 -0.0858 68  TYR   B CZ  
5043 O  OH  . TYR   B 68  ? 0.1897 0.2486 0.2796 -0.0023 -0.0251 -0.0459 68  TYR   B OH  
5053 N  N   . ILE   B 69  ? 0.1725 0.1625 0.1775 0.0055  -0.0342 -0.0316 69  ILE   B N   
5054 C  CA  . ILE   B 69  ? 0.1813 0.1702 0.1747 0.0007  -0.0244 -0.0350 69  ILE   B CA  
5055 C  C   . ILE   B 69  ? 0.1798 0.1721 0.1736 0.0064  -0.0275 -0.0247 69  ILE   B C   
5056 O  O   . ILE   B 69  ? 0.1841 0.1809 0.1691 0.0103  -0.0191 -0.0366 69  ILE   B O   
5057 C  CB  . ILE   B 69  ? 0.1843 0.1737 0.1948 0.0019  -0.0031 -0.0367 69  ILE   B CB  
5058 C  CG1 . ILE   B 69  ? 0.1897 0.1753 0.2085 -0.0073 0.0053  -0.0281 69  ILE   B CG1 
5059 C  CG2 . ILE   B 69  ? 0.1926 0.1836 0.2199 -0.0045 0.0018  -0.0283 69  ILE   B CG2 
5060 C  CD1 . ILE   B 69  ? 0.1960 0.1850 0.2207 -0.0228 0.0060  -0.0349 69  ILE   B CD1 
5072 N  N   . ALA   B 70  ? 0.1781 0.1681 0.1726 0.0098  -0.0282 -0.0271 70  ALA   B N   
5073 C  CA  . ALA   B 70  ? 0.1838 0.1716 0.1696 0.0033  -0.0423 -0.0286 70  ALA   B CA  
5074 C  C   . ALA   B 70  ? 0.1931 0.1696 0.1738 -0.0053 -0.0448 -0.0391 70  ALA   B C   
5075 O  O   . ALA   B 70  ? 0.1975 0.1693 0.1870 0.0013  -0.0381 -0.0428 70  ALA   B O   
5076 C  CB  . ALA   B 70  ? 0.1866 0.1831 0.1729 0.0018  -0.0377 -0.0347 70  ALA   B CB  
5082 N  N   . THR   B 71  ? 0.1993 0.1711 0.1804 0.0059  -0.0575 -0.0385 71  THR   B N   
5083 C  CA  . THR   B 71  ? 0.2123 0.1721 0.2009 0.0092  -0.0645 -0.0350 71  THR   B CA  
5084 C  C   . THR   B 71  ? 0.2050 0.1749 0.2225 0.0255  -0.0588 -0.0551 71  THR   B C   
5085 O  O   . THR   B 71  ? 0.2121 0.1828 0.2654 0.0287  -0.0581 -0.0644 71  THR   B O   
5086 C  CB  . THR   B 71  ? 0.2375 0.1881 0.2221 0.0003  -0.0694 -0.0144 71  THR   B CB  
5087 O  OG1 . THR   B 71  ? 0.2534 0.2123 0.2540 -0.0175 -0.0699 0.0028  71  THR   B OG1 
5088 C  CG2 . THR   B 71  ? 0.2549 0.1865 0.2536 0.0057  -0.0432 0.0041  71  THR   B CG2 
5096 N  N   . ASN   B 72  ? 0.1882 0.1825 0.2173 0.0196  -0.0567 -0.0704 72  ASN   B N   
5097 C  CA  . ASN   B 72  ? 0.1849 0.1931 0.2386 0.0182  -0.0429 -0.0798 72  ASN   B CA  
5098 C  C   . ASN   B 72  ? 0.1834 0.2038 0.2486 0.0041  -0.0188 -0.0776 72  ASN   B C   
5099 O  O   . ASN   B 72  ? 0.1848 0.2186 0.2782 0.0058  -0.0080 -0.0736 72  ASN   B O   
5100 C  CB  . ASN   B 72  ? 0.1947 0.2030 0.2459 0.0136  -0.0613 -0.0728 72  ASN   B CB  
5101 C  CG  . ASN   B 72  ? 0.2118 0.2162 0.2487 0.0269  -0.0662 -0.0395 72  ASN   B CG  
5102 O  OD1 . ASN   B 72  ? 0.2382 0.2375 0.2461 0.0111  -0.0400 -0.0391 72  ASN   B OD1 
5103 N  ND2 . ASN   B 72  ? 0.2199 0.2252 0.2992 0.0449  -0.0465 -0.0112 72  ASN   B ND2 
5110 N  N   . GLY   B 73  ? 0.1884 0.2034 0.2241 0.0004  -0.0241 -0.0737 73  GLY   B N   
5111 C  CA  . GLY   B 73  ? 0.1872 0.2160 0.1916 -0.0039 -0.0157 -0.0650 73  GLY   B CA  
5112 C  C   . GLY   B 73  ? 0.1879 0.2139 0.1427 0.0055  -0.0168 -0.0558 73  GLY   B C   
5113 O  O   . GLY   B 73  ? 0.1799 0.2015 0.1559 0.0123  -0.0188 -0.0493 73  GLY   B O   
5117 N  N   . PRO   B 74  ? 0.1850 0.2240 0.1465 0.0023  -0.0297 -0.0367 74  PRO   B N   
5118 C  CA  . PRO   B 74  ? 0.1765 0.2198 0.1395 0.0080  -0.0175 -0.0247 74  PRO   B CA  
5119 C  C   . PRO   B 74  ? 0.1684 0.1983 0.1464 0.0086  -0.0120 -0.0170 74  PRO   B C   
5120 O  O   . PRO   B 74  ? 0.1736 0.2063 0.1826 0.0105  -0.0086 -0.0271 74  PRO   B O   
5121 C  CB  . PRO   B 74  ? 0.1919 0.2408 0.1426 -0.0023 -0.0140 -0.0159 74  PRO   B CB  
5122 C  CG  . PRO   B 74  ? 0.2153 0.2551 0.1719 -0.0015 -0.0146 -0.0127 74  PRO   B CG  
5123 C  CD  . PRO   B 74  ? 0.2106 0.2413 0.1635 0.0087  -0.0137 -0.0224 74  PRO   B CD  
5131 N  N   . LEU   B 75  ? 0.1690 0.1900 0.1388 0.0053  -0.0184 -0.0164 75  LEU   B N   
5132 C  CA  . LEU   B 75  ? 0.1712 0.1844 0.1288 0.0036  -0.0139 -0.0064 75  LEU   B CA  
5133 C  C   . LEU   B 75  ? 0.1775 0.1940 0.1410 0.0093  -0.0021 -0.0003 75  LEU   B C   
5134 O  O   . LEU   B 75  ? 0.1885 0.2134 0.1475 -0.0006 -0.0023 0.0020  75  LEU   B O   
5135 C  CB  . LEU   B 75  ? 0.1712 0.1921 0.1240 -0.0063 -0.0209 0.0089  75  LEU   B CB  
5136 C  CG  . LEU   B 75  ? 0.2000 0.2075 0.1434 -0.0299 -0.0145 0.0075  75  LEU   B CG  
5137 C  CD1 . LEU   B 75  ? 0.2328 0.2171 0.1558 -0.0474 0.0137  0.0018  75  LEU   B CD1 
5138 C  CD2 . LEU   B 75  ? 0.2409 0.2353 0.2264 -0.0193 -0.0018 0.0244  75  LEU   B CD2 
5150 N  N   . LYS   B 76  ? 0.1741 0.2102 0.1668 0.0035  0.0028  0.0106  76  LYS   B N   
5151 C  CA  . LYS   B 76  ? 0.1816 0.2193 0.1957 -0.0063 0.0219  0.0085  76  LYS   B CA  
5152 C  C   . LYS   B 76  ? 0.1801 0.2056 0.1697 -0.0006 0.0140  0.0291  76  LYS   B C   
5153 O  O   . LYS   B 76  ? 0.1833 0.1839 0.1793 -0.0009 0.0037  0.0214  76  LYS   B O   
5154 C  CB  . LYS   B 76  ? 0.2008 0.2260 0.2336 -0.0085 0.0364  -0.0189 76  LYS   B CB  
5155 C  CG  . LYS   B 76  ? 0.2127 0.2415 0.2684 -0.0007 0.0242  -0.0231 76  LYS   B CG  
5156 C  CD  . LYS   B 76  ? 0.2191 0.2440 0.2998 0.0091  0.0090  -0.0414 76  LYS   B CD  
5157 C  CE  . LYS   B 76  ? 0.2267 0.2527 0.3406 0.0162  -0.0049 -0.0467 76  LYS   B CE  
5158 N  NZ  . LYS   B 76  ? 0.2252 0.2591 0.3635 0.0128  -0.0200 -0.0639 76  LYS   B NZ  
5172 N  N   . VAL   B 77  ? 0.1891 0.2157 0.1685 0.0015  0.0164  0.0298  77  VAL   B N   
5173 C  CA  . VAL   B 77  ? 0.1960 0.2087 0.1727 0.0103  0.0196  0.0593  77  VAL   B CA  
5174 C  C   . VAL   B 77  ? 0.1790 0.1823 0.1701 0.0086  0.0283  0.0446  77  VAL   B C   
5175 O  O   . VAL   B 77  ? 0.1812 0.1816 0.1859 0.0154  0.0394  0.0286  77  VAL   B O   
5176 C  CB  . VAL   B 77  ? 0.2139 0.2203 0.2238 0.0082  0.0255  0.0713  77  VAL   B CB  
5177 C  CG1 . VAL   B 77  ? 0.2099 0.2080 0.2546 0.0001  0.0265  0.0811  77  VAL   B CG1 
5178 C  CG2 . VAL   B 77  ? 0.2376 0.2361 0.2285 0.0030  0.0088  0.0789  77  VAL   B CG2 
5188 N  N   . GLY   B 78  ? 0.1740 0.1672 0.1733 0.0078  0.0230  0.0253  78  GLY   B N   
5189 C  CA  . GLY   B 78  ? 0.1709 0.1639 0.1720 0.0028  0.0329  0.0143  78  GLY   B CA  
5190 C  C   . GLY   B 78  ? 0.1618 0.1598 0.1637 0.0069  0.0233  0.0270  78  GLY   B C   
5191 O  O   . GLY   B 78  ? 0.1582 0.1590 0.1870 0.0158  0.0170  0.0273  78  GLY   B O   
5195 N  N   . GLY   B 79  ? 0.1564 0.1672 0.1693 0.0089  0.0177  0.0212  79  GLY   B N   
5196 C  CA  . GLY   B 79  ? 0.1589 0.1555 0.1605 0.0142  0.0151  0.0191  79  GLY   B CA  
5197 C  C   . GLY   B 79  ? 0.1489 0.1504 0.1604 0.0109  0.0142  0.0055  79  GLY   B C   
5198 O  O   . GLY   B 79  ? 0.1529 0.1521 0.1701 0.0128  0.0193  0.0150  79  GLY   B O   
5202 N  N   . SER   B 80  ? 0.1459 0.1447 0.1556 0.0031  0.0202  0.0108  80  SER   B N   
5203 C  CA  . SER   B 80  ? 0.1416 0.1445 0.1589 0.0040  0.0018  0.0067  80  SER   B CA  
5204 C  C   . SER   B 80  ? 0.1485 0.1385 0.1545 0.0055  -0.0032 0.0035  80  SER   B C   
5205 O  O   . SER   B 80  ? 0.1556 0.1455 0.1746 0.0123  0.0020  -0.0019 80  SER   B O   
5206 C  CB  . SER   B 80  ? 0.1490 0.1471 0.1678 -0.0018 0.0058  0.0132  80  SER   B CB  
5207 O  OG  . SER   B 80  ? 0.1520 0.1652 0.1749 -0.0071 -0.0061 0.0169  80  SER   B OG  
5213 N  N   . CYS   B 81  ? 0.1450 0.1297 0.1597 0.0014  -0.0040 -0.0050 81  CYS   B N   
5214 C  CA  . CYS   B 81  ? 0.1482 0.1323 0.1587 0.0007  -0.0078 -0.0020 81  CYS   B CA  
5215 C  C   . CYS   B 81  ? 0.1414 0.1352 0.1395 0.0030  -0.0097 -0.0046 81  CYS   B C   
5216 O  O   . CYS   B 81  ? 0.1595 0.1285 0.1604 0.0088  0.0002  -0.0053 81  CYS   B O   
5217 C  CB  . CYS   B 81  ? 0.1562 0.1456 0.1671 -0.0068 -0.0116 0.0014  81  CYS   B CB  
5218 S  SG  . CYS   B 81  ? 0.1624 0.1598 0.1673 -0.0041 -0.0230 -0.0093 81  CYS   B SG  
5224 N  N   . VAL   B 82  ? 0.1478 0.1328 0.1464 0.0029  -0.0098 -0.0047 82  VAL   B N   
5225 C  CA  . VAL   B 82  ? 0.1570 0.1368 0.1363 -0.0037 -0.0108 0.0042  82  VAL   B CA  
5226 C  C   . VAL   B 82  ? 0.1591 0.1273 0.1564 -0.0060 -0.0098 0.0006  82  VAL   B C   
5227 O  O   . VAL   B 82  ? 0.1678 0.1304 0.1992 -0.0054 -0.0084 -0.0194 82  VAL   B O   
5228 C  CB  . VAL   B 82  ? 0.1601 0.1560 0.1564 -0.0039 -0.0205 0.0111  82  VAL   B CB  
5229 C  CG1 . VAL   B 82  ? 0.1751 0.1805 0.1727 0.0046  -0.0183 0.0318  82  VAL   B CG1 
5230 C  CG2 . VAL   B 82  ? 0.1696 0.1645 0.1918 -0.0038 -0.0361 0.0171  82  VAL   B CG2 
5240 N  N   . LEU   B 83  ? 0.1492 0.1243 0.1588 -0.0169 -0.0165 -0.0114 83  LEU   B N   
5241 C  CA  . LEU   B 83  ? 0.1576 0.1350 0.1400 -0.0131 -0.0196 -0.0111 83  LEU   B CA  
5242 C  C   . LEU   B 83  ? 0.1525 0.1334 0.1408 -0.0164 -0.0221 -0.0053 83  LEU   B C   
5243 O  O   . LEU   B 83  ? 0.1537 0.1400 0.1323 -0.0189 -0.0139 -0.0001 83  LEU   B O   
5244 C  CB  . LEU   B 83  ? 0.1630 0.1391 0.1552 -0.0145 -0.0184 -0.0122 83  LEU   B CB  
5245 C  CG  . LEU   B 83  ? 0.1758 0.1606 0.1588 -0.0176 -0.0157 -0.0182 83  LEU   B CG  
5246 C  CD1 . LEU   B 83  ? 0.1849 0.1702 0.1575 -0.0116 -0.0255 -0.0085 83  LEU   B CD1 
5247 C  CD2 . LEU   B 83  ? 0.1927 0.1664 0.1729 -0.0075 -0.0188 -0.0124 83  LEU   B CD2 
5259 N  N   . SER   B 84  ? 0.1558 0.1414 0.1591 -0.0225 -0.0163 -0.0033 84  SER   B N   
5260 C  CA  . SER   B 84  ? 0.1562 0.1635 0.1568 -0.0326 -0.0157 0.0160  84  SER   B CA  
5261 C  C   . SER   B 84  ? 0.1494 0.1813 0.1034 -0.0208 -0.0223 0.0172  84  SER   B C   
5262 O  O   . SER   B 84  ? 0.1562 0.1734 0.1102 -0.0122 -0.0111 0.0037  84  SER   B O   
5263 C  CB  . SER   B 84  ? 0.1720 0.1652 0.2060 -0.0257 0.0005  0.0212  84  SER   B CB  
5264 O  OG  . SER   B 84  ? 0.1724 0.1800 0.2312 -0.0394 -0.0032 0.0213  84  SER   B OG  
5270 N  N   . GLY   B 85  ? 0.1545 0.1911 0.1168 -0.0193 -0.0211 0.0247  85  GLY   B N   
5271 C  CA  . GLY   B 85  ? 0.1570 0.1967 0.1456 -0.0334 -0.0088 -0.0079 85  GLY   B CA  
5272 C  C   . GLY   B 85  ? 0.1566 0.1799 0.1486 -0.0390 -0.0063 0.0058  85  GLY   B C   
5273 O  O   . GLY   B 85  ? 0.1643 0.1799 0.1504 -0.0509 0.0103  -0.0091 85  GLY   B O   
5277 N  N   . HIS   B 86  ? 0.1545 0.1664 0.1686 -0.0338 -0.0112 0.0099  86  HIS   B N   
5278 C  CA  . HIS   B 86  ? 0.1511 0.1692 0.1550 -0.0298 -0.0179 0.0196  86  HIS   B CA  
5279 C  C   . HIS   B 86  ? 0.1543 0.1821 0.1411 -0.0443 -0.0045 0.0317  86  HIS   B C   
5280 O  O   . HIS   B 86  ? 0.1701 0.2002 0.1455 -0.0348 0.0045  0.0299  86  HIS   B O   
5281 C  CB  . HIS   B 86  ? 0.1613 0.1737 0.1604 -0.0165 -0.0220 0.0106  86  HIS   B CB  
5282 C  CG  . HIS   B 86  ? 0.1616 0.1818 0.1591 -0.0114 -0.0245 0.0135  86  HIS   B CG  
5283 N  ND1 . HIS   B 86  ? 0.1700 0.2046 0.1896 -0.0267 -0.0250 -0.0008 86  HIS   B ND1 
5284 C  CD2 . HIS   B 86  ? 0.1658 0.1811 0.1583 -0.0068 -0.0234 0.0088  86  HIS   B CD2 
5285 C  CE1 . HIS   B 86  ? 0.1733 0.1957 0.1758 -0.0184 -0.0061 -0.0230 86  HIS   B CE1 
5286 N  NE2 . HIS   B 86  ? 0.1734 0.1869 0.1625 0.0020  -0.0124 -0.0039 86  HIS   B NE2 
5294 N  N   . ASN   B 87  ? 0.1505 0.1823 0.1568 -0.0278 0.0055  0.0217  87  ASN   B N   
5295 C  CA  . ASN   B 87  ? 0.1653 0.2050 0.1735 -0.0294 0.0218  0.0148  87  ASN   B CA  
5296 C  C   . ASN   B 87  ? 0.1826 0.1883 0.1516 -0.0281 0.0373  0.0122  87  ASN   B C   
5297 O  O   . ASN   B 87  ? 0.2078 0.1955 0.1950 -0.0249 0.0571  0.0037  87  ASN   B O   
5298 C  CB  . ASN   B 87  ? 0.1694 0.2443 0.2020 -0.0268 0.0205  0.0145  87  ASN   B CB  
5299 C  CG  . ASN   B 87  ? 0.1706 0.2629 0.2021 0.0018  0.0323  0.0317  87  ASN   B CG  
5300 O  OD1 . ASN   B 87  ? 0.1657 0.2490 0.1967 0.0125  0.0471  0.0457  87  ASN   B OD1 
5301 N  ND2 . ASN   B 87  ? 0.2019 0.2769 0.2466 0.0123  0.0515  0.0250  87  ASN   B ND2 
5308 N  N   . LEU   B 88  ? 0.1656 0.1770 0.1376 -0.0293 0.0142  0.0058  88  LEU   B N   
5309 C  CA  . LEU   B 88  ? 0.1846 0.1709 0.1510 -0.0370 0.0033  -0.0023 88  LEU   B CA  
5310 C  C   . LEU   B 88  ? 0.1828 0.1616 0.1503 -0.0422 -0.0009 -0.0064 88  LEU   B C   
5311 O  O   . LEU   B 88  ? 0.2041 0.1683 0.1861 -0.0207 -0.0257 -0.0087 88  LEU   B O   
5312 C  CB  . LEU   B 88  ? 0.1961 0.1865 0.1728 -0.0503 -0.0074 0.0085  88  LEU   B CB  
5313 C  CG  . LEU   B 88  ? 0.2341 0.2164 0.1731 -0.0447 -0.0185 0.0249  88  LEU   B CG  
5314 C  CD1 . LEU   B 88  ? 0.2460 0.2429 0.1843 -0.0589 -0.0127 0.0433  88  LEU   B CD1 
5315 C  CD2 . LEU   B 88  ? 0.2731 0.2422 0.2493 -0.0037 -0.0387 -0.0001 88  LEU   B CD2 
5327 N  N   . ALA   B 89  ? 0.1640 0.1660 0.1363 -0.0404 0.0254  -0.0119 89  ALA   B N   
5328 C  CA  . ALA   B 89  ? 0.1574 0.1633 0.1253 -0.0376 0.0062  0.0046  89  ALA   B CA  
5329 C  C   . ALA   B 89  ? 0.1700 0.1628 0.1227 -0.0425 0.0094  0.0105  89  ALA   B C   
5330 O  O   . ALA   B 89  ? 0.1494 0.1703 0.1595 -0.0371 0.0074  -0.0199 89  ALA   B O   
5331 C  CB  . ALA   B 89  ? 0.1492 0.1642 0.1417 -0.0398 0.0110  0.0106  89  ALA   B CB  
5337 N  N   . LYS   B 90  ? 0.2047 0.1513 0.1276 -0.0536 -0.0107 0.0070  90  LYS   B N   
5338 C  CA  . LYS   B 90  ? 0.2137 0.1468 0.1335 -0.0485 -0.0160 0.0089  90  LYS   B CA  
5339 C  C   . LYS   B 90  ? 0.1895 0.1447 0.1285 -0.0363 -0.0168 -0.0001 90  LYS   B C   
5340 O  O   . LYS   B 90  ? 0.1936 0.1579 0.1370 -0.0530 -0.0067 0.0013  90  LYS   B O   
5341 C  CB  . LYS   B 90  ? 0.2245 0.1554 0.1717 -0.0373 -0.0124 0.0241  90  LYS   B CB  
5342 C  CG  . LYS   B 90  ? 0.2162 0.1667 0.1750 -0.0189 0.0090  0.0166  90  LYS   B CG  
5343 C  CD  . LYS   B 90  ? 0.2341 0.1864 0.2148 -0.0036 0.0254  0.0063  90  LYS   B CD  
5344 C  CE  . LYS   B 90  ? 0.2627 0.2041 0.2551 -0.0106 0.0385  -0.0057 90  LYS   B CE  
5345 N  NZ  . LYS   B 90  ? 0.2633 0.1891 0.2368 -0.0314 0.0636  -0.0112 90  LYS   B NZ  
5359 N  N   . HIS   B 91  ? 0.1658 0.1334 0.1144 -0.0314 -0.0133 0.0083  91  HIS   B N   
5360 C  CA  . HIS   B 91  ? 0.1586 0.1308 0.1459 -0.0236 -0.0179 0.0048  91  HIS   B CA  
5361 C  C   . HIS   B 91  ? 0.1497 0.1354 0.1146 -0.0273 -0.0075 0.0090  91  HIS   B C   
5362 O  O   . HIS   B 91  ? 0.1652 0.1426 0.1214 -0.0297 -0.0158 -0.0020 91  HIS   B O   
5363 C  CB  . HIS   B 91  ? 0.1729 0.1324 0.1887 -0.0147 -0.0161 0.0176  91  HIS   B CB  
5364 C  CG  . HIS   B 91  ? 0.2108 0.1545 0.2476 -0.0004 0.0137  0.0225  91  HIS   B CG  
5365 N  ND1 . HIS   B 91  ? 0.2369 0.1596 0.3011 0.0008  0.0237  0.0025  91  HIS   B ND1 
5366 C  CD2 . HIS   B 91  ? 0.2269 0.1850 0.2909 0.0136  0.0013  0.0572  91  HIS   B CD2 
5367 C  CE1 . HIS   B 91  ? 0.2397 0.1761 0.3272 0.0191  0.0268  0.0153  91  HIS   B CE1 
5368 N  NE2 . HIS   B 91  ? 0.2423 0.1892 0.3244 0.0247  0.0204  0.0590  91  HIS   B NE2 
5376 N  N   . CYS   B 92  ? 0.1472 0.1361 0.1110 -0.0265 -0.0103 -0.0005 92  CYS   B N   
5377 C  CA  . CYS   B 92  ? 0.1480 0.1335 0.1175 -0.0220 -0.0089 -0.0053 92  CYS   B CA  
5378 C  C   . CYS   B 92  ? 0.1368 0.1265 0.1142 -0.0112 -0.0063 0.0031  92  CYS   B C   
5379 O  O   . CYS   B 92  ? 0.1496 0.1348 0.1358 -0.0101 -0.0024 -0.0021 92  CYS   B O   
5380 C  CB  . CYS   B 92  ? 0.1468 0.1340 0.1313 -0.0148 -0.0131 -0.0033 92  CYS   B CB  
5381 S  SG  . CYS   B 92  ? 0.1476 0.1381 0.1312 -0.0127 -0.0110 0.0041  92  CYS   B SG  
5387 N  N   . LEU   B 93  ? 0.1364 0.1325 0.1122 -0.0121 -0.0012 -0.0052 93  LEU   B N   
5388 C  CA  . LEU   B 93  ? 0.1434 0.1339 0.1220 -0.0056 -0.0094 -0.0023 93  LEU   B CA  
5389 C  C   . LEU   B 93  ? 0.1336 0.1336 0.1110 -0.0047 -0.0112 0.0099  93  LEU   B C   
5390 O  O   . LEU   B 93  ? 0.1406 0.1273 0.1379 -0.0100 -0.0061 0.0009  93  LEU   B O   
5391 C  CB  . LEU   B 93  ? 0.1425 0.1297 0.1451 0.0013  -0.0084 0.0076  93  LEU   B CB  
5392 C  CG  . LEU   B 93  ? 0.1398 0.1396 0.1603 -0.0061 -0.0040 0.0161  93  LEU   B CG  
5393 C  CD1 . LEU   B 93  ? 0.1374 0.1468 0.1735 0.0020  -0.0094 -0.0035 93  LEU   B CD1 
5394 C  CD2 . LEU   B 93  ? 0.1426 0.1420 0.1559 -0.0073 -0.0168 0.0059  93  LEU   B CD2 
5406 N  N   . HIS   B 94  ? 0.1413 0.1251 0.1131 -0.0040 -0.0099 0.0080  94  HIS   B N   
5407 C  CA  . HIS   B 94  ? 0.1445 0.1251 0.1185 0.0005  -0.0047 0.0035  94  HIS   B CA  
5408 C  C   . HIS   B 94  ? 0.1351 0.1305 0.1400 -0.0016 -0.0054 0.0067  94  HIS   B C   
5409 O  O   . HIS   B 94  ? 0.1351 0.1368 0.1793 -0.0055 0.0094  -0.0092 94  HIS   B O   
5410 C  CB  . HIS   B 94  ? 0.1378 0.1327 0.1344 0.0022  -0.0118 0.0028  94  HIS   B CB  
5411 C  CG  . HIS   B 94  ? 0.1399 0.1299 0.1385 -0.0069 -0.0289 0.0002  94  HIS   B CG  
5412 N  ND1 . HIS   B 94  ? 0.1435 0.1367 0.1249 -0.0028 -0.0187 0.0003  94  HIS   B ND1 
5413 C  CD2 . HIS   B 94  ? 0.1440 0.1312 0.1364 0.0038  -0.0181 0.0046  94  HIS   B CD2 
5414 C  CE1 . HIS   B 94  ? 0.1508 0.1335 0.1320 -0.0084 -0.0139 -0.0024 94  HIS   B CE1 
5415 N  NE2 . HIS   B 94  ? 0.1391 0.1376 0.1422 -0.0100 -0.0162 0.0012  94  HIS   B NE2 
5423 N  N   . VAL   B 95  ? 0.1314 0.1238 0.1399 -0.0034 -0.0017 0.0076  95  VAL   B N   
5424 C  CA  . VAL   B 95  ? 0.1282 0.1363 0.1380 0.0021  0.0021  0.0138  95  VAL   B CA  
5425 C  C   . VAL   B 95  ? 0.1436 0.1331 0.1424 0.0038  0.0159  0.0141  95  VAL   B C   
5426 O  O   . VAL   B 95  ? 0.1524 0.1327 0.1479 0.0083  0.0033  0.0188  95  VAL   B O   
5427 C  CB  . VAL   B 95  ? 0.1365 0.1317 0.1518 0.0001  -0.0092 0.0094  95  VAL   B CB  
5428 C  CG1 . VAL   B 95  ? 0.1461 0.1519 0.1881 -0.0087 0.0062  0.0122  95  VAL   B CG1 
5429 C  CG2 . VAL   B 95  ? 0.1510 0.1293 0.1384 0.0024  -0.0094 0.0066  95  VAL   B CG2 
5439 N  N   . VAL   B 96  ? 0.1498 0.1372 0.1484 0.0086  0.0060  0.0167  96  VAL   B N   
5440 C  CA  . VAL   B 96  ? 0.1627 0.1505 0.1410 0.0066  0.0027  0.0214  96  VAL   B CA  
5441 C  C   . VAL   B 96  ? 0.1681 0.1500 0.1629 0.0066  0.0207  0.0181  96  VAL   B C   
5442 O  O   . VAL   B 96  ? 0.1690 0.1535 0.1851 -0.0012 0.0240  0.0031  96  VAL   B O   
5443 C  CB  . VAL   B 96  ? 0.1740 0.1713 0.1468 0.0054  0.0087  0.0207  96  VAL   B CB  
5444 C  CG1 . VAL   B 96  ? 0.1679 0.1815 0.1574 0.0150  0.0134  0.0110  96  VAL   B CG1 
5445 C  CG2 . VAL   B 96  ? 0.1783 0.1736 0.1418 0.0102  0.0173  0.0033  96  VAL   B CG2 
5455 N  N   . GLY   B 97  ? 0.1753 0.1548 0.1435 0.0011  0.0113  0.0206  97  GLY   B N   
5456 C  CA  . GLY   B 97  ? 0.1907 0.1508 0.1640 0.0157  0.0099  0.0255  97  GLY   B CA  
5457 C  C   . GLY   B 97  ? 0.2213 0.1645 0.1776 0.0158  0.0115  0.0304  97  GLY   B C   
5458 O  O   . GLY   B 97  ? 0.2404 0.1700 0.1620 0.0084  0.0006  0.0125  97  GLY   B O   
5462 N  N   . PRO   B 98  ? 0.2357 0.1733 0.2012 0.0183  0.0452  0.0464  98  PRO   B N   
5463 C  CA  . PRO   B 98  ? 0.2513 0.1942 0.2161 0.0386  0.0659  0.0400  98  PRO   B CA  
5464 C  C   . PRO   B 98  ? 0.2696 0.1908 0.1916 0.0569  0.0722  0.0557  98  PRO   B C   
5465 O  O   . PRO   B 98  ? 0.2596 0.1827 0.2064 0.0464  0.0738  0.0541  98  PRO   B O   
5466 C  CB  . PRO   B 98  ? 0.2384 0.2037 0.2424 0.0400  0.0722  0.0491  98  PRO   B CB  
5467 C  CG  . PRO   B 98  ? 0.2268 0.1916 0.2482 0.0295  0.0648  0.0699  98  PRO   B CG  
5468 C  CD  . PRO   B 98  ? 0.2137 0.1804 0.2322 0.0273  0.0661  0.0607  98  PRO   B CD  
5476 N  N   . ASN   B 99  ? 0.2888 0.2123 0.1924 0.0698  0.0721  0.0407  99  ASN   B N   
5477 C  CA  . ASN   B 99  ? 0.3086 0.2257 0.1951 0.0893  0.0633  0.0598  99  ASN   B CA  
5478 C  C   . ASN   B 99  ? 0.3287 0.2607 0.2228 0.0983  0.0892  0.0873  99  ASN   B C   
5479 O  O   . ASN   B 99  ? 0.3462 0.2828 0.2387 0.0969  0.0851  0.0861  99  ASN   B O   
5480 C  CB  . ASN   B 99  ? 0.3206 0.2235 0.1979 0.0831  0.0454  0.0610  99  ASN   B CB  
5481 C  CG  . ASN   B 99  ? 0.3241 0.2282 0.2027 0.0729  0.0414  0.0510  99  ASN   B CG  
5482 O  OD1 . ASN   B 99  ? 0.3197 0.2287 0.2377 0.0761  0.0509  0.0594  99  ASN   B OD1 
5483 N  ND2 . ASN   B 99  ? 0.3248 0.2287 0.2176 0.0718  0.0111  0.0329  99  ASN   B ND2 
5490 N  N   . VAL   B 100 ? 0.3479 0.2731 0.2848 0.0840  0.1081  0.1112  100 VAL   B N   
5491 C  CA  . VAL   B 100 ? 0.3773 0.3004 0.3499 0.0661  0.0931  0.1401  100 VAL   B CA  
5492 C  C   . VAL   B 100 ? 0.4072 0.3163 0.3467 0.0720  0.0860  0.1660  100 VAL   B C   
5493 O  O   . VAL   B 100 ? 0.4118 0.3339 0.3627 0.0737  0.1060  0.1451  100 VAL   B O   
5494 C  CB  . VAL   B 100 ? 0.3812 0.3144 0.4271 0.0318  0.0820  0.1475  100 VAL   B CB  
5495 C  CG1 . VAL   B 100 ? 0.3847 0.3207 0.4524 0.0219  0.0743  0.1421  100 VAL   B CG1 
5496 C  CG2 . VAL   B 100 ? 0.3798 0.3211 0.4388 0.0201  0.0866  0.1606  100 VAL   B CG2 
5506 N  N   . ASN   B 101 ? 0.4334 0.3250 0.3357 0.0775  0.0556  0.1775  101 ASN   B N   
5507 C  CA  . ASN   B 101 ? 0.4681 0.3473 0.3572 0.0677  0.0280  0.1718  101 ASN   B CA  
5508 C  C   . ASN   B 101 ? 0.5195 0.4037 0.3764 0.0505  0.0146  0.1546  101 ASN   B C   
5509 O  O   . ASN   B 101 ? 0.5207 0.4122 0.3951 0.0543  0.0180  0.1296  101 ASN   B O   
5510 C  CB  . ASN   B 101 ? 0.4552 0.3279 0.3622 0.0619  0.0280  0.1403  101 ASN   B CB  
5511 C  CG  . ASN   B 101 ? 0.4399 0.3077 0.3603 0.0579  0.0226  0.1324  101 ASN   B CG  
5512 O  OD1 . ASN   B 101 ? 0.4377 0.3073 0.3948 0.0498  0.0362  0.1220  101 ASN   B OD1 
5513 N  ND2 . ASN   B 101 ? 0.4291 0.2963 0.3556 0.0571  0.0184  0.1255  101 ASN   B ND2 
5520 N  N   A LYS   B 102 ? 0.5448 0.4324 0.3975 0.0376  0.0148  0.1412  102 LYS   B N   
5521 N  N   B LYS   B 102 ? 0.5437 0.4324 0.3970 0.0391  0.0126  0.1407  102 LYS   B N   
5522 C  CA  A LYS   B 102 ? 0.5677 0.4631 0.4283 0.0243  0.0186  0.1205  102 LYS   B CA  
5523 C  CA  B LYS   B 102 ? 0.5653 0.4622 0.4262 0.0275  0.0140  0.1212  102 LYS   B CA  
5524 C  C   A LYS   B 102 ? 0.5703 0.4669 0.4053 0.0272  0.0235  0.1323  102 LYS   B C   
5525 C  C   B LYS   B 102 ? 0.5688 0.4669 0.4048 0.0286  0.0216  0.1325  102 LYS   B C   
5526 O  O   A LYS   B 102 ? 0.5765 0.4691 0.4046 0.0257  0.0170  0.1361  102 LYS   B O   
5527 O  O   B LYS   B 102 ? 0.5741 0.4698 0.4028 0.0266  0.0163  0.1370  102 LYS   B O   
5528 C  CB  A LYS   B 102 ? 0.5847 0.4868 0.4829 0.0106  0.0247  0.0829  102 LYS   B CB  
5529 C  CB  B LYS   B 102 ? 0.5803 0.4845 0.4761 0.0170  0.0141  0.0856  102 LYS   B CB  
5530 C  CG  A LYS   B 102 ? 0.5984 0.5060 0.5419 -0.0001 0.0300  0.0445  102 LYS   B CG  
5531 C  CG  B LYS   B 102 ? 0.5922 0.5026 0.5300 0.0090  0.0136  0.0505  102 LYS   B CG  
5532 C  CD  A LYS   B 102 ? 0.6090 0.5210 0.5909 -0.0084 0.0348  0.0132  102 LYS   B CD  
5533 C  CD  B LYS   B 102 ? 0.6015 0.5165 0.5749 0.0026  0.0140  0.0212  102 LYS   B CD  
5534 C  CE  A LYS   B 102 ? 0.6153 0.5310 0.6316 -0.0149 0.0397  -0.0082 102 LYS   B CE  
5535 C  CE  B LYS   B 102 ? 0.6072 0.5259 0.6133 -0.0021 0.0154  0.0007  102 LYS   B CE  
5536 N  NZ  A LYS   B 102 ? 0.6185 0.5365 0.6527 -0.0179 0.0422  -0.0202 102 LYS   B NZ  
5537 N  NZ  B LYS   B 102 ? 0.6106 0.5312 0.6335 -0.0045 0.0160  -0.0100 102 LYS   B NZ  
5564 N  N   . GLY   B 103 ? 0.5649 0.4662 0.3936 0.0318  0.0371  0.1320  103 GLY   B N   
5565 C  CA  . GLY   B 103 ? 0.5539 0.4641 0.4022 0.0400  0.0657  0.1181  103 GLY   B CA  
5566 C  C   . GLY   B 103 ? 0.5387 0.4584 0.4014 0.0455  0.0938  0.1051  103 GLY   B C   
5567 O  O   . GLY   B 103 ? 0.5432 0.4629 0.4054 0.0409  0.0981  0.1069  103 GLY   B O   
5572 N  N   . GLU   B 104 ? 0.5158 0.4451 0.3786 0.0555  0.1182  0.0832  104 GLU   B N   
5573 C  CA  . GLU   B 104 ? 0.4915 0.4309 0.3669 0.0694  0.1327  0.0597  104 GLU   B CA  
5574 C  C   . GLU   B 104 ? 0.4857 0.4328 0.3929 0.0431  0.1765  0.0631  104 GLU   B C   
5575 O  O   . GLU   B 104 ? 0.4819 0.4283 0.4265 0.0398  0.1773  0.0623  104 GLU   B O   
5576 C  CB  . GLU   B 104 ? 0.4793 0.4146 0.3455 0.1068  0.0897  0.0270  104 GLU   B CB  
5577 C  CG  . GLU   B 104 ? 0.4684 0.4006 0.3270 0.1359  0.0376  -0.0027 104 GLU   B CG  
5578 C  CD  . GLU   B 104 ? 0.4600 0.3905 0.3089 0.1509  -0.0020 -0.0265 104 GLU   B CD  
5579 O  OE1 . GLU   B 104 ? 0.4500 0.3804 0.2680 0.1617  0.0035  -0.0374 104 GLU   B OE1 
5580 O  OE2 . GLU   B 104 ? 0.4596 0.3931 0.3124 0.1491  -0.0349 -0.0390 104 GLU   B OE2 
5587 N  N   A ASP   B 105 ? 0.4812 0.4359 0.3936 0.0328  0.2017  0.0660  105 ASP   B N   
5588 N  N   B ASP   B 105 ? 0.4834 0.4356 0.3995 0.0318  0.1915  0.0652  105 ASP   B N   
5589 C  CA  A ASP   B 105 ? 0.4794 0.4378 0.4058 0.0231  0.2191  0.0548  105 ASP   B CA  
5590 C  CA  B ASP   B 105 ? 0.4822 0.4364 0.4089 0.0213  0.2022  0.0565  105 ASP   B CA  
5591 C  C   A ASP   B 105 ? 0.4598 0.4146 0.3734 0.0115  0.2298  0.0550  105 ASP   B C   
5592 C  C   B ASP   B 105 ? 0.4627 0.4151 0.3799 0.0105  0.2188  0.0559  105 ASP   B C   
5593 O  O   A ASP   B 105 ? 0.4476 0.4087 0.3617 0.0108  0.2321  0.0592  105 ASP   B O   
5594 O  O   B ASP   B 105 ? 0.4575 0.4122 0.3678 0.0101  0.2313  0.0615  105 ASP   B O   
5595 C  CB  A ASP   B 105 ? 0.4923 0.4570 0.4707 0.0281  0.2201  0.0380  105 ASP   B CB  
5596 C  CB  B ASP   B 105 ? 0.4941 0.4528 0.4611 0.0237  0.1930  0.0445  105 ASP   B CB  
5597 C  CG  A ASP   B 105 ? 0.4997 0.4699 0.5302 0.0297  0.2208  0.0273  105 ASP   B CG  
5598 C  CG  B ASP   B 105 ? 0.5009 0.4633 0.5069 0.0236  0.1856  0.0376  105 ASP   B CG  
5599 O  OD1 A ASP   B 105 ? 0.4988 0.4736 0.5397 0.0256  0.2326  0.0324  105 ASP   B OD1 
5600 O  OD1 B ASP   B 105 ? 0.5018 0.4664 0.5178 0.0205  0.1891  0.0406  105 ASP   B OD1 
5601 O  OD2 A ASP   B 105 ? 0.5032 0.4748 0.5662 0.0351  0.2099  0.0171  105 ASP   B OD2 
5602 O  OD2 B ASP   B 105 ? 0.5020 0.4675 0.5274 0.0260  0.1807  0.0329  105 ASP   B OD2 
5611 N  N   . ILE   B 106 ? 0.4464 0.3927 0.3815 0.0024  0.2146  0.0534  106 ILE   B N   
5612 C  CA  . ILE   B 106 ? 0.4120 0.3499 0.3827 -0.0171 0.2081  0.0426  106 ILE   B CA  
5613 C  C   . ILE   B 106 ? 0.3670 0.3300 0.3792 -0.0196 0.1964  0.0219  106 ILE   B C   
5614 O  O   . ILE   B 106 ? 0.3582 0.3050 0.3855 -0.0323 0.2066  0.0287  106 ILE   B O   
5615 C  CB  . ILE   B 106 ? 0.4296 0.3378 0.3932 -0.0287 0.2066  0.0433  106 ILE   B CB  
5616 C  CG1 . ILE   B 106 ? 0.4408 0.3339 0.3945 -0.0212 0.1953  0.0343  106 ILE   B CG1 
5617 C  CG2 . ILE   B 106 ? 0.4335 0.3445 0.4189 -0.0366 0.2075  0.0388  106 ILE   B CG2 
5618 C  CD1 . ILE   B 106 ? 0.4474 0.3342 0.3838 -0.0145 0.1889  0.0305  106 ILE   B CD1 
5631 N  N   A GLN   B 107 ? 0.3520 0.3369 0.3872 -0.0213 0.1771  0.0163  107 GLN   B N   
5632 N  N   B GLN   B 107 ? 0.3542 0.3366 0.3854 -0.0201 0.1727  0.0156  107 GLN   B N   
5633 C  CA  A GLN   B 107 ? 0.3336 0.3406 0.3928 -0.0225 0.1534  0.0143  107 GLN   B CA  
5634 C  CA  B GLN   B 107 ? 0.3380 0.3398 0.3892 -0.0196 0.1464  0.0130  107 GLN   B CA  
5635 C  C   A GLN   B 107 ? 0.3004 0.3146 0.3571 -0.0104 0.1362  -0.0001 107 GLN   B C   
5636 C  C   B GLN   B 107 ? 0.3049 0.3161 0.3532 -0.0093 0.1340  0.0018  107 GLN   B C   
5637 O  O   A GLN   B 107 ? 0.2877 0.3145 0.3769 -0.0026 0.1136  -0.0246 107 GLN   B O   
5638 O  O   B GLN   B 107 ? 0.2978 0.3183 0.3687 -0.0048 0.1148  -0.0162 107 GLN   B O   
5639 C  CB  A GLN   B 107 ? 0.3608 0.3760 0.4581 -0.0268 0.1227  0.0171  107 GLN   B CB  
5640 C  CB  B GLN   B 107 ? 0.3636 0.3703 0.4465 -0.0227 0.1160  0.0148  107 GLN   B CB  
5641 C  CG  A GLN   B 107 ? 0.3872 0.4039 0.5192 -0.0263 0.0886  0.0188  107 GLN   B CG  
5642 C  CG  B GLN   B 107 ? 0.3878 0.3944 0.5007 -0.0216 0.0843  0.0154  107 GLN   B CG  
5643 C  CD  A GLN   B 107 ? 0.4063 0.4232 0.5651 -0.0275 0.0631  0.0212  107 GLN   B CD  
5644 C  CD  B GLN   B 107 ? 0.4057 0.4111 0.5415 -0.0217 0.0595  0.0164  107 GLN   B CD  
5645 O  OE1 A GLN   B 107 ? 0.4127 0.4304 0.5824 -0.0244 0.0593  0.0202  107 GLN   B OE1 
5646 O  OE1 B GLN   B 107 ? 0.4112 0.4169 0.5550 -0.0197 0.0557  0.0164  107 GLN   B OE1 
5647 N  NE2 A GLN   B 107 ? 0.4150 0.4294 0.5823 -0.0282 0.0511  0.0248  107 GLN   B NE2 
5648 N  NE2 B GLN   B 107 ? 0.4142 0.4169 0.5577 -0.0217 0.0484  0.0184  107 GLN   B NE2 
5665 N  N   . LEU   B 108 ? 0.2765 0.2933 0.3166 0.0066  0.1283  0.0044  108 LEU   B N   
5666 C  CA  . LEU   B 108 ? 0.2458 0.2610 0.2639 0.0227  0.0917  0.0252  108 LEU   B CA  
5667 C  C   . LEU   B 108 ? 0.2017 0.2105 0.2523 0.0179  0.0541  0.0258  108 LEU   B C   
5668 O  O   . LEU   B 108 ? 0.1855 0.1899 0.2421 0.0200  0.0364  0.0244  108 LEU   B O   
5669 C  CB  . LEU   B 108 ? 0.2604 0.2850 0.2405 0.0286  0.0959  0.0399  108 LEU   B CB  
5670 C  CG  . LEU   B 108 ? 0.2765 0.3106 0.2613 0.0308  0.0782  0.0265  108 LEU   B CG  
5671 C  CD1 . LEU   B 108 ? 0.2869 0.3297 0.2507 0.0254  0.0723  0.0264  108 LEU   B CD1 
5672 C  CD2 . LEU   B 108 ? 0.2897 0.3151 0.2647 0.0363  0.0591  0.0115  108 LEU   B CD2 
5685 N  N   . LEU   B 109 ? 0.1824 0.1828 0.2380 0.0058  0.0443  0.0236  109 LEU   B N   
5686 C  CA  . LEU   B 109 ? 0.1638 0.1565 0.2553 0.0021  0.0390  0.0295  109 LEU   B CA  
5687 C  C   . LEU   B 109 ? 0.1584 0.1408 0.2567 0.0041  0.0411  0.0208  109 LEU   B C   
5688 O  O   . LEU   B 109 ? 0.1524 0.1333 0.2492 0.0048  0.0417  0.0287  109 LEU   B O   
5689 C  CB  . LEU   B 109 ? 0.1757 0.1454 0.2677 0.0050  0.0291  0.0334  109 LEU   B CB  
5690 C  CG  . LEU   B 109 ? 0.1681 0.1362 0.2557 0.0040  0.0336  0.0201  109 LEU   B CG  
5691 C  CD1 . LEU   B 109 ? 0.1603 0.1475 0.2356 0.0142  0.0299  0.0269  109 LEU   B CD1 
5692 C  CD2 . LEU   B 109 ? 0.1774 0.1479 0.2671 0.0014  0.0290  0.0195  109 LEU   B CD2 
5704 N  N   . LYS   B 110 ? 0.1528 0.1430 0.2420 -0.0012 0.0349  0.0179  110 LYS   B N   
5705 C  CA  . LYS   B 110 ? 0.1467 0.1379 0.2425 -0.0028 0.0313  0.0167  110 LYS   B CA  
5706 C  C   . LYS   B 110 ? 0.1431 0.1397 0.2294 0.0012  0.0389  0.0106  110 LYS   B C   
5707 O  O   . LYS   B 110 ? 0.1405 0.1416 0.2302 -0.0072 0.0295  0.0049  110 LYS   B O   
5708 C  CB  . LYS   B 110 ? 0.1515 0.1367 0.2616 -0.0051 0.0327  0.0126  110 LYS   B CB  
5709 C  CG  . LYS   B 110 ? 0.1502 0.1411 0.2743 -0.0094 0.0194  0.0208  110 LYS   B CG  
5710 C  CD  . LYS   B 110 ? 0.1572 0.1349 0.2839 -0.0030 0.0197  0.0183  110 LYS   B CD  
5711 C  CE  . LYS   B 110 ? 0.1574 0.1557 0.3113 -0.0030 0.0281  0.0171  110 LYS   B CE  
5712 N  NZ  . LYS   B 110 ? 0.1604 0.1686 0.3043 0.0086  0.0220  0.0075  110 LYS   B NZ  
5726 N  N   . SER   B 111 ? 0.1535 0.1438 0.2364 0.0014  0.0341  0.0177  111 SER   B N   
5727 C  CA  . SER   B 111 ? 0.1585 0.1417 0.2168 0.0016  0.0279  0.0205  111 SER   B CA  
5728 C  C   . SER   B 111 ? 0.1556 0.1364 0.2182 0.0014  0.0195  0.0068  111 SER   B C   
5729 O  O   . SER   B 111 ? 0.1490 0.1404 0.2313 -0.0034 0.0160  0.0018  111 SER   B O   
5730 C  CB  . SER   B 111 ? 0.1689 0.1650 0.2302 0.0126  0.0446  0.0274  111 SER   B CB  
5731 O  OG  . SER   B 111 ? 0.1901 0.1943 0.2235 0.0143  0.0479  0.0395  111 SER   B OG  
5737 N  N   . ALA   B 112 ? 0.1429 0.1400 0.2246 0.0000  0.0318  0.0140  112 ALA   B N   
5738 C  CA  . ALA   B 112 ? 0.1403 0.1460 0.2000 -0.0001 0.0192  0.0009  112 ALA   B CA  
5739 C  C   . ALA   B 112 ? 0.1314 0.1404 0.2006 0.0045  0.0135  -0.0020 112 ALA   B C   
5740 O  O   . ALA   B 112 ? 0.1346 0.1392 0.2156 -0.0064 0.0112  0.0057  112 ALA   B O   
5741 C  CB  . ALA   B 112 ? 0.1449 0.1480 0.2047 0.0044  0.0250  0.0114  112 ALA   B CB  
5747 N  N   . TYR   B 113 ? 0.1301 0.1329 0.2145 0.0013  0.0143  0.0064  113 TYR   B N   
5748 C  CA  . TYR   B 113 ? 0.1255 0.1330 0.2194 -0.0028 0.0151  -0.0052 113 TYR   B CA  
5749 C  C   . TYR   B 113 ? 0.1266 0.1247 0.2095 -0.0084 0.0145  0.0011  113 TYR   B C   
5750 O  O   . TYR   B 113 ? 0.1288 0.1282 0.2008 -0.0045 0.0075  -0.0036 113 TYR   B O   
5751 C  CB  . TYR   B 113 ? 0.1302 0.1236 0.2168 -0.0055 0.0183  0.0063  113 TYR   B CB  
5752 C  CG  . TYR   B 113 ? 0.1351 0.1266 0.2269 -0.0024 0.0108  0.0112  113 TYR   B CG  
5753 C  CD1 . TYR   B 113 ? 0.1414 0.1298 0.2426 -0.0045 0.0125  0.0200  113 TYR   B CD1 
5754 C  CD2 . TYR   B 113 ? 0.1482 0.1298 0.2271 -0.0037 0.0090  0.0169  113 TYR   B CD2 
5755 C  CE1 . TYR   B 113 ? 0.1499 0.1367 0.2288 -0.0030 0.0171  0.0049  113 TYR   B CE1 
5756 C  CE2 . TYR   B 113 ? 0.1530 0.1280 0.2412 0.0051  0.0102  0.0221  113 TYR   B CE2 
5757 C  CZ  . TYR   B 113 ? 0.1422 0.1330 0.2459 0.0036  0.0155  0.0116  113 TYR   B CZ  
5758 O  OH  . TYR   B 113 ? 0.1541 0.1223 0.2753 0.0075  0.0207  0.0015  113 TYR   B OH  
5768 N  N   . GLU   B 114 ? 0.1257 0.1183 0.2190 -0.0076 0.0176  0.0080  114 GLU   B N   
5769 C  CA  . GLU   B 114 ? 0.1295 0.1165 0.2166 0.0059  0.0118  0.0096  114 GLU   B CA  
5770 C  C   . GLU   B 114 ? 0.1311 0.1195 0.2095 0.0043  0.0102  0.0007  114 GLU   B C   
5771 O  O   . GLU   B 114 ? 0.1277 0.1297 0.2118 0.0015  0.0009  0.0064  114 GLU   B O   
5772 C  CB  . GLU   B 114 ? 0.1292 0.1305 0.2201 0.0016  0.0164  0.0039  114 GLU   B CB  
5773 C  CG  . GLU   B 114 ? 0.1377 0.1236 0.2285 -0.0028 0.0185  -0.0018 114 GLU   B CG  
5774 C  CD  . GLU   B 114 ? 0.1378 0.1260 0.2404 -0.0088 0.0153  0.0092  114 GLU   B CD  
5775 O  OE1 . GLU   B 114 ? 0.1333 0.1416 0.2238 -0.0057 0.0209  0.0060  114 GLU   B OE1 
5776 O  OE2 . GLU   B 114 ? 0.1350 0.1500 0.2482 -0.0185 0.0135  0.0061  114 GLU   B OE2 
5783 N  N   . ASN   B 115 ? 0.1314 0.1214 0.1944 -0.0038 0.0034  0.0053  115 ASN   B N   
5784 C  CA  . ASN   B 115 ? 0.1318 0.1271 0.1854 -0.0119 0.0070  0.0079  115 ASN   B CA  
5785 C  C   . ASN   B 115 ? 0.1285 0.1223 0.1935 -0.0099 -0.0004 -0.0006 115 ASN   B C   
5786 O  O   . ASN   B 115 ? 0.1373 0.1278 0.1921 -0.0087 0.0047  -0.0004 115 ASN   B O   
5787 C  CB  . ASN   B 115 ? 0.1446 0.1372 0.1940 -0.0101 0.0078  0.0030  115 ASN   B CB  
5788 C  CG  . ASN   B 115 ? 0.1512 0.1405 0.1905 -0.0023 0.0124  -0.0001 115 ASN   B CG  
5789 O  OD1 . ASN   B 115 ? 0.1951 0.1550 0.1920 -0.0025 0.0191  -0.0071 115 ASN   B OD1 
5790 N  ND2 . ASN   B 115 ? 0.1470 0.1545 0.1965 -0.0028 0.0119  0.0082  115 ASN   B ND2 
5797 N  N   . PHE   B 116 ? 0.1309 0.1273 0.1755 0.0005  0.0044  0.0037  116 PHE   B N   
5798 C  CA  . PHE   B 116 ? 0.1316 0.1314 0.1886 -0.0076 0.0021  -0.0002 116 PHE   B CA  
5799 C  C   . PHE   B 116 ? 0.1314 0.1127 0.1918 -0.0091 -0.0043 0.0015  116 PHE   B C   
5800 O  O   . PHE   B 116 ? 0.1403 0.1279 0.1954 -0.0096 -0.0085 0.0095  116 PHE   B O   
5801 C  CB  . PHE   B 116 ? 0.1273 0.1269 0.1715 -0.0059 -0.0144 0.0070  116 PHE   B CB  
5802 C  CG  . PHE   B 116 ? 0.1200 0.1257 0.1820 -0.0061 -0.0057 0.0046  116 PHE   B CG  
5803 C  CD1 . PHE   B 116 ? 0.1292 0.1331 0.1985 -0.0014 0.0046  0.0050  116 PHE   B CD1 
5804 C  CD2 . PHE   B 116 ? 0.1280 0.1405 0.1735 -0.0021 -0.0001 -0.0021 116 PHE   B CD2 
5805 C  CE1 . PHE   B 116 ? 0.1368 0.1370 0.2027 -0.0007 -0.0093 0.0033  116 PHE   B CE1 
5806 C  CE2 . PHE   B 116 ? 0.1319 0.1399 0.1758 0.0021  0.0035  0.0046  116 PHE   B CE2 
5807 C  CZ  . PHE   B 116 ? 0.1255 0.1443 0.1816 0.0030  -0.0054 0.0026  116 PHE   B CZ  
5817 N  N   . ASN   B 117 ? 0.1343 0.1255 0.1913 -0.0019 -0.0108 0.0068  117 ASN   B N   
5818 C  CA  . ASN   B 117 ? 0.1434 0.1284 0.1939 -0.0021 -0.0157 0.0015  117 ASN   B CA  
5819 C  C   . ASN   B 117 ? 0.1467 0.1303 0.2108 -0.0007 -0.0171 0.0070  117 ASN   B C   
5820 O  O   . ASN   B 117 ? 0.1479 0.1386 0.2444 -0.0084 -0.0327 0.0168  117 ASN   B O   
5821 C  CB  . ASN   B 117 ? 0.1424 0.1327 0.1999 0.0038  -0.0149 -0.0050 117 ASN   B CB  
5822 C  CG  . ASN   B 117 ? 0.1386 0.1285 0.2155 0.0004  -0.0028 -0.0036 117 ASN   B CG  
5823 O  OD1 . ASN   B 117 ? 0.1516 0.1330 0.2278 -0.0115 0.0008  -0.0038 117 ASN   B OD1 
5824 N  ND2 . ASN   B 117 ? 0.1411 0.1332 0.2074 -0.0009 0.0079  0.0026  117 ASN   B ND2 
5831 N  N   . GLN   B 118 ? 0.1456 0.1189 0.2045 -0.0060 -0.0133 0.0002  118 GLN   B N   
5832 C  CA  . GLN   B 118 ? 0.1488 0.1252 0.2164 0.0033  -0.0117 0.0022  118 GLN   B CA  
5833 C  C   . GLN   B 118 ? 0.1497 0.1245 0.2364 -0.0042 -0.0106 -0.0023 118 GLN   B C   
5834 O  O   . GLN   B 118 ? 0.1655 0.1199 0.2791 -0.0076 -0.0045 0.0040  118 GLN   B O   
5835 C  CB  . GLN   B 118 ? 0.1547 0.1315 0.2252 0.0051  -0.0211 -0.0006 118 GLN   B CB  
5836 C  CG  . GLN   B 118 ? 0.1599 0.1408 0.2204 0.0060  -0.0066 -0.0079 118 GLN   B CG  
5837 C  CD  . GLN   B 118 ? 0.1604 0.1309 0.2224 0.0068  -0.0127 -0.0148 118 GLN   B CD  
5838 O  OE1 . GLN   B 118 ? 0.1688 0.1276 0.2447 0.0034  -0.0011 0.0045  118 GLN   B OE1 
5839 N  NE2 . GLN   B 118 ? 0.1711 0.1344 0.2256 -0.0043 -0.0094 -0.0038 118 GLN   B NE2 
5848 N  N   . HIS   B 119 ? 0.1531 0.1262 0.1877 -0.0085 -0.0153 0.0052  119 HIS   B N   
5849 C  CA  . HIS   B 119 ? 0.1630 0.1415 0.1656 -0.0066 -0.0191 0.0113  119 HIS   B CA  
5850 C  C   . HIS   B 119 ? 0.1670 0.1457 0.1670 -0.0056 -0.0359 0.0130  119 HIS   B C   
5851 O  O   . HIS   B 119 ? 0.1703 0.1421 0.1915 -0.0253 -0.0236 0.0096  119 HIS   B O   
5852 C  CB  . HIS   B 119 ? 0.1673 0.1446 0.1773 -0.0017 -0.0258 0.0036  119 HIS   B CB  
5853 C  CG  . HIS   B 119 ? 0.1708 0.1647 0.1966 0.0108  -0.0384 -0.0101 119 HIS   B CG  
5854 N  ND1 . HIS   B 119 ? 0.1873 0.1796 0.2354 0.0017  -0.0469 -0.0307 119 HIS   B ND1 
5855 C  CD2 . HIS   B 119 ? 0.1834 0.1862 0.2038 0.0396  -0.0494 -0.0197 119 HIS   B CD2 
5856 C  CE1 . HIS   B 119 ? 0.2074 0.1962 0.2335 0.0139  -0.0664 -0.0430 119 HIS   B CE1 
5857 N  NE2 . HIS   B 119 ? 0.2047 0.2100 0.2228 0.0332  -0.0526 -0.0357 119 HIS   B NE2 
5865 N  N   A GLU   B 120 ? 0.1849 0.1450 0.1759 -0.0125 -0.0528 0.0185  120 GLU   B N   
5866 N  N   B GLU   B 120 ? 0.1848 0.1516 0.1815 -0.0081 -0.0448 0.0192  120 GLU   B N   
5867 C  CA  A GLU   B 120 ? 0.2103 0.1650 0.1913 -0.0130 -0.0550 0.0394  120 GLU   B CA  
5868 C  CA  B GLU   B 120 ? 0.2085 0.1705 0.1971 -0.0066 -0.0462 0.0369  120 GLU   B CA  
5869 C  C   A GLU   B 120 ? 0.1916 0.1592 0.1784 -0.0221 -0.0501 0.0309  120 GLU   B C   
5870 C  C   B GLU   B 120 ? 0.1915 0.1613 0.1836 -0.0166 -0.0424 0.0287  120 GLU   B C   
5871 O  O   A GLU   B 120 ? 0.1853 0.1698 0.1773 -0.0246 -0.0539 0.0214  120 GLU   B O   
5872 O  O   B GLU   B 120 ? 0.1863 0.1691 0.1836 -0.0162 -0.0399 0.0181  120 GLU   B O   
5873 C  CB  A GLU   B 120 ? 0.2641 0.1959 0.2614 0.0010  -0.0645 0.0622  120 GLU   B CB  
5874 C  CB  B GLU   B 120 ? 0.2559 0.2019 0.2585 0.0080  -0.0558 0.0577  120 GLU   B CB  
5875 C  CG  A GLU   B 120 ? 0.3053 0.2482 0.3688 0.0049  -0.0715 0.0651  120 GLU   B CG  
5876 C  CG  B GLU   B 120 ? 0.2931 0.2494 0.3478 0.0141  -0.0618 0.0640  120 GLU   B CG  
5877 C  CD  A GLU   B 120 ? 0.3317 0.2874 0.4561 0.0031  -0.0786 0.0794  120 GLU   B CD  
5878 C  CD  B GLU   B 120 ? 0.3233 0.2842 0.4251 0.0147  -0.0599 0.0733  120 GLU   B CD  
5879 O  OE1 A GLU   B 120 ? 0.3532 0.3081 0.4902 -0.0032 -0.0693 0.0928  120 GLU   B OE1 
5880 O  OE1 B GLU   B 120 ? 0.3424 0.3076 0.4550 0.0150  -0.0558 0.0818  120 GLU   B OE1 
5881 O  OE2 A GLU   B 120 ? 0.3478 0.3151 0.5029 0.0008  -0.0785 0.0716  120 GLU   B OE2 
5882 O  OE2 B GLU   B 120 ? 0.3378 0.3039 0.4614 0.0106  -0.0598 0.0730  120 GLU   B OE2 
5895 N  N   . VAL   B 121 ? 0.1807 0.1484 0.1775 -0.0242 -0.0372 0.0264  121 VAL   B N   
5896 C  CA  . VAL   B 121 ? 0.1682 0.1574 0.1691 -0.0204 -0.0311 0.0176  121 VAL   B CA  
5897 C  C   . VAL   B 121 ? 0.1658 0.1516 0.1697 -0.0259 -0.0200 0.0251  121 VAL   B C   
5898 O  O   . VAL   B 121 ? 0.1771 0.1446 0.1755 -0.0385 -0.0355 0.0189  121 VAL   B O   
5899 C  CB  . VAL   B 121 ? 0.1977 0.2008 0.1800 -0.0122 -0.0298 0.0239  121 VAL   B CB  
5900 C  CG1 . VAL   B 121 ? 0.2009 0.2106 0.2159 -0.0329 -0.0099 0.0207  121 VAL   B CG1 
5901 C  CG2 . VAL   B 121 ? 0.2250 0.2282 0.1786 -0.0022 -0.0244 0.0028  121 VAL   B CG2 
5912 N  N   . LEU   B 122 ? 0.1576 0.1444 0.1598 -0.0193 -0.0204 0.0119  122 LEU   B N   
5913 C  CA  . LEU   B 122 ? 0.1475 0.1569 0.1421 -0.0192 -0.0240 0.0166  122 LEU   B CA  
5914 C  C   . LEU   B 122 ? 0.1473 0.1407 0.1409 -0.0279 -0.0180 0.0146  122 LEU   B C   
5915 O  O   . LEU   B 122 ? 0.1604 0.1453 0.1781 -0.0362 -0.0236 0.0016  122 LEU   B O   
5916 C  CB  . LEU   B 122 ? 0.1670 0.1675 0.1834 -0.0001 -0.0284 0.0192  122 LEU   B CB  
5917 C  CG  . LEU   B 122 ? 0.1528 0.1735 0.1938 -0.0180 -0.0077 0.0144  122 LEU   B CG  
5918 C  CD1 . LEU   B 122 ? 0.1551 0.1928 0.1934 -0.0232 -0.0197 0.0111  122 LEU   B CD1 
5919 C  CD2 . LEU   B 122 ? 0.1590 0.1726 0.1606 -0.0082 -0.0086 -0.0016 122 LEU   B CD2 
5931 N  N   . LEU   B 123 ? 0.1498 0.1284 0.1332 -0.0198 -0.0162 0.0099  123 LEU   B N   
5932 C  CA  . LEU   B 123 ? 0.1521 0.1336 0.1430 -0.0263 -0.0144 0.0025  123 LEU   B CA  
5933 C  C   . LEU   B 123 ? 0.1448 0.1322 0.1356 -0.0262 -0.0165 0.0025  123 LEU   B C   
5934 O  O   . LEU   B 123 ? 0.1559 0.1303 0.1475 -0.0316 -0.0145 -0.0035 123 LEU   B O   
5935 C  CB  . LEU   B 123 ? 0.1579 0.1351 0.1595 -0.0246 -0.0185 -0.0064 123 LEU   B CB  
5936 C  CG  . LEU   B 123 ? 0.1493 0.1429 0.1729 -0.0205 -0.0102 0.0035  123 LEU   B CG  
5937 C  CD1 . LEU   B 123 ? 0.1604 0.1539 0.1900 -0.0181 0.0001  -0.0134 123 LEU   B CD1 
5938 C  CD2 . LEU   B 123 ? 0.1643 0.1459 0.1942 -0.0185 0.0015  0.0171  123 LEU   B CD2 
5950 N  N   . ALA   B 124 ? 0.1424 0.1285 0.1413 -0.0151 -0.0102 -0.0003 124 ALA   B N   
5951 C  CA  . ALA   B 124 ? 0.1363 0.1245 0.1642 -0.0137 -0.0064 -0.0081 124 ALA   B CA  
5952 C  C   . ALA   B 124 ? 0.1325 0.1235 0.1504 -0.0184 -0.0063 0.0001  124 ALA   B C   
5953 O  O   . ALA   B 124 ? 0.1444 0.1297 0.1594 -0.0139 -0.0137 0.0012  124 ALA   B O   
5954 C  CB  . ALA   B 124 ? 0.1447 0.1310 0.1654 -0.0100 0.0028  -0.0046 124 ALA   B CB  
5960 N  N   . PRO   B 125 ? 0.1448 0.1303 0.1472 -0.0163 -0.0149 0.0111  125 PRO   B N   
5961 C  CA  . PRO   B 125 ? 0.1545 0.1331 0.1628 -0.0152 -0.0173 0.0249  125 PRO   B CA  
5962 C  C   . PRO   B 125 ? 0.1461 0.1276 0.1831 -0.0148 -0.0133 0.0160  125 PRO   B C   
5963 O  O   . PRO   B 125 ? 0.1442 0.1283 0.1995 -0.0135 -0.0056 0.0188  125 PRO   B O   
5964 C  CB  . PRO   B 125 ? 0.1578 0.1580 0.1713 -0.0195 -0.0223 0.0318  125 PRO   B CB  
5965 C  CG  . PRO   B 125 ? 0.1620 0.1624 0.1639 -0.0234 -0.0276 0.0200  125 PRO   B CG  
5966 C  CD  . PRO   B 125 ? 0.1601 0.1451 0.1511 -0.0277 -0.0116 0.0027  125 PRO   B CD  
5974 N  N   . LEU   B 126 ? 0.1494 0.1242 0.2024 -0.0168 0.0074  0.0171  126 LEU   B N   
5975 C  CA  . LEU   B 126 ? 0.1594 0.1329 0.1987 -0.0111 0.0162  0.0209  126 LEU   B CA  
5976 C  C   . LEU   B 126 ? 0.1588 0.1421 0.2021 -0.0010 0.0136  0.0160  126 LEU   B C   
5977 O  O   . LEU   B 126 ? 0.1797 0.1721 0.2291 0.0253  -0.0072 -0.0046 126 LEU   B O   
5978 C  CB  . LEU   B 126 ? 0.1771 0.1378 0.2387 -0.0167 0.0284  0.0188  126 LEU   B CB  
5979 C  CG  . LEU   B 126 ? 0.1916 0.1417 0.2533 -0.0195 0.0355  -0.0030 126 LEU   B CG  
5980 C  CD1 . LEU   B 126 ? 0.2024 0.1461 0.3143 -0.0167 0.0249  -0.0105 126 LEU   B CD1 
5981 C  CD2 . LEU   B 126 ? 0.1952 0.1550 0.2539 -0.0352 0.0236  -0.0130 126 LEU   B CD2 
5993 N  N   . LEU   B 127 ? 0.1552 0.1313 0.2062 0.0040  0.0271  0.0121  127 LEU   B N   
5994 C  CA  . LEU   B 127 ? 0.1536 0.1398 0.2202 -0.0073 0.0259  0.0201  127 LEU   B CA  
5995 C  C   . LEU   B 127 ? 0.1505 0.1345 0.2294 -0.0028 0.0232  0.0247  127 LEU   B C   
5996 O  O   . LEU   B 127 ? 0.1537 0.1416 0.2314 -0.0173 0.0141  0.0185  127 LEU   B O   
5997 C  CB  . LEU   B 127 ? 0.1667 0.1406 0.2340 -0.0066 0.0263  0.0163  127 LEU   B CB  
5998 C  CG  . LEU   B 127 ? 0.1760 0.1417 0.2397 0.0012  0.0262  0.0158  127 LEU   B CG  
5999 C  CD1 . LEU   B 127 ? 0.1834 0.1456 0.2463 0.0044  0.0224  0.0039  127 LEU   B CD1 
6000 C  CD2 . LEU   B 127 ? 0.1831 0.1458 0.2498 -0.0115 0.0217  0.0176  127 LEU   B CD2 
6012 N  N   . SER   B 128 ? 0.1548 0.1379 0.2244 0.0008  0.0043  0.0161  128 SER   B N   
6013 C  CA  . SER   B 128 ? 0.1698 0.1440 0.2316 0.0058  -0.0107 0.0277  128 SER   B CA  
6014 C  C   . SER   B 128 ? 0.1855 0.1501 0.2732 0.0065  -0.0302 0.0239  128 SER   B C   
6015 O  O   . SER   B 128 ? 0.1960 0.1538 0.3132 0.0032  -0.0225 0.0395  128 SER   B O   
6016 C  CB  . SER   B 128 ? 0.1752 0.1451 0.2363 0.0035  0.0036  0.0397  128 SER   B CB  
6017 O  OG  . SER   B 128 ? 0.1774 0.1605 0.2395 0.0060  0.0055  0.0383  128 SER   B OG  
6023 N  N   . ALA   B 129 ? 0.1941 0.1531 0.2918 0.0232  -0.0146 0.0081  129 ALA   B N   
6024 C  CA  . ALA   B 129 ? 0.2063 0.1616 0.3104 0.0258  -0.0160 -0.0091 129 ALA   B CA  
6025 C  C   . ALA   B 129 ? 0.1936 0.1491 0.2844 0.0202  0.0046  0.0022  129 ALA   B C   
6026 O  O   . ALA   B 129 ? 0.1819 0.1549 0.2816 0.0153  0.0001  0.0009  129 ALA   B O   
6027 C  CB  . ALA   B 129 ? 0.2316 0.1886 0.3453 0.0273  0.0007  -0.0120 129 ALA   B CB  
6033 N  N   . GLY   B 130 ? 0.1940 0.1516 0.2825 0.0320  0.0115  -0.0120 130 GLY   B N   
6034 C  CA  . GLY   B 130 ? 0.1961 0.1584 0.2994 0.0292  0.0249  -0.0059 130 GLY   B CA  
6035 C  C   . GLY   B 130 ? 0.1990 0.1591 0.2854 0.0167  0.0213  0.0030  130 GLY   B C   
6036 O  O   . GLY   B 130 ? 0.2045 0.1743 0.2936 0.0196  0.0093  0.0078  130 GLY   B O   
6040 N  N   . ILE   B 131 ? 0.1966 0.1724 0.2888 0.0292  0.0121  0.0097  131 ILE   B N   
6041 C  CA  . ILE   B 131 ? 0.2190 0.1926 0.2886 0.0281  0.0030  0.0265  131 ILE   B CA  
6042 C  C   . ILE   B 131 ? 0.2305 0.1888 0.2519 0.0160  0.0057  0.0255  131 ILE   B C   
6043 O  O   . ILE   B 131 ? 0.2546 0.2086 0.2695 0.0154  -0.0121 0.0215  131 ILE   B O   
6044 C  CB  . ILE   B 131 ? 0.2138 0.2280 0.3280 0.0248  -0.0061 0.0399  131 ILE   B CB  
6045 C  CG1 . ILE   B 131 ? 0.2179 0.2439 0.3376 -0.0016 -0.0000 0.0442  131 ILE   B CG1 
6046 C  CG2 . ILE   B 131 ? 0.2100 0.2442 0.3555 0.0326  -0.0060 0.0295  131 ILE   B CG2 
6047 C  CD1 . ILE   B 131 ? 0.2327 0.2616 0.3586 -0.0165 -0.0093 0.0435  131 ILE   B CD1 
6059 N  N   . PHE   B 132 ? 0.2207 0.1714 0.2380 0.0113  0.0289  0.0212  132 PHE   B N   
6060 C  CA  . PHE   B 132 ? 0.2297 0.1714 0.2428 0.0067  0.0497  0.0181  132 PHE   B CA  
6061 C  C   . PHE   B 132 ? 0.2431 0.1846 0.2670 0.0129  0.0668  0.0158  132 PHE   B C   
6062 O  O   . PHE   B 132 ? 0.2594 0.2080 0.2988 0.0078  0.0768  0.0171  132 PHE   B O   
6063 C  CB  . PHE   B 132 ? 0.2133 0.1672 0.2286 0.0041  0.0467  0.0211  132 PHE   B CB  
6064 C  CG  . PHE   B 132 ? 0.2033 0.1746 0.2187 0.0126  0.0280  0.0181  132 PHE   B CG  
6065 C  CD1 . PHE   B 132 ? 0.2183 0.1770 0.2548 0.0067  0.0181  0.0130  132 PHE   B CD1 
6066 C  CD2 . PHE   B 132 ? 0.2037 0.1783 0.1987 0.0263  0.0137  0.0325  132 PHE   B CD2 
6067 C  CE1 . PHE   B 132 ? 0.2209 0.1769 0.2536 0.0026  0.0144  0.0061  132 PHE   B CE1 
6068 C  CE2 . PHE   B 132 ? 0.2144 0.1832 0.2057 0.0220  0.0136  0.0193  132 PHE   B CE2 
6069 C  CZ  . PHE   B 132 ? 0.2233 0.1815 0.2269 0.0093  0.0020  0.0206  132 PHE   B CZ  
6079 N  N   . GLY   B 133 ? 0.2393 0.1786 0.2678 0.0091  0.0477  0.0452  133 GLY   B N   
6080 C  CA  . GLY   B 133 ? 0.2467 0.1901 0.2835 -0.0186 0.0408  0.0555  133 GLY   B CA  
6081 C  C   . GLY   B 133 ? 0.2531 0.2020 0.3014 -0.0345 0.0411  0.0523  133 GLY   B C   
6082 O  O   . GLY   B 133 ? 0.2692 0.2127 0.3386 -0.0521 0.0394  0.0647  133 GLY   B O   
6086 N  N   . ALA   B 134 ? 0.2364 0.1975 0.2798 -0.0343 0.0417  0.0341  134 ALA   B N   
6087 C  CA  . ALA   B 134 ? 0.2332 0.1896 0.2863 -0.0287 0.0492  0.0202  134 ALA   B CA  
6088 C  C   . ALA   B 134 ? 0.2441 0.1759 0.2896 -0.0212 0.0405  0.0395  134 ALA   B C   
6089 O  O   . ALA   B 134 ? 0.2433 0.1981 0.2990 -0.0123 0.0202  0.0360  134 ALA   B O   
6090 C  CB  . ALA   B 134 ? 0.2253 0.1934 0.2999 -0.0248 0.0408  0.0112  134 ALA   B CB  
6096 N  N   . ASP   B 135 ? 0.2646 0.1734 0.2969 -0.0188 0.0277  0.0432  135 ASP   B N   
6097 C  CA  . ASP   B 135 ? 0.2801 0.1673 0.3189 -0.0154 0.0178  0.0488  135 ASP   B CA  
6098 C  C   . ASP   B 135 ? 0.2575 0.1570 0.2897 -0.0067 0.0051  0.0468  135 ASP   B C   
6099 O  O   . ASP   B 135 ? 0.2454 0.1482 0.3047 -0.0094 0.0004  0.0410  135 ASP   B O   
6100 C  CB  . ASP   B 135 ? 0.3100 0.1738 0.3476 -0.0299 0.0155  0.0479  135 ASP   B CB  
6101 C  CG  . ASP   B 135 ? 0.3329 0.1781 0.3853 -0.0491 0.0085  0.0389  135 ASP   B CG  
6102 O  OD1 . ASP   B 135 ? 0.3445 0.1649 0.3870 -0.0311 -0.0065 0.0344  135 ASP   B OD1 
6103 O  OD2 . ASP   B 135 ? 0.3506 0.2219 0.4395 -0.0644 0.0127  0.0358  135 ASP   B OD2 
6108 N  N   . PRO   B 136 ? 0.2404 0.1696 0.2953 0.0172  -0.0186 0.0283  136 PRO   B N   
6109 C  CA  . PRO   B 136 ? 0.2102 0.1561 0.3006 0.0163  -0.0179 0.0108  136 PRO   B CA  
6110 C  C   . PRO   B 136 ? 0.1900 0.1396 0.3149 0.0138  -0.0105 0.0082  136 PRO   B C   
6111 O  O   . PRO   B 136 ? 0.1715 0.1358 0.2991 0.0094  -0.0089 0.0075  136 PRO   B O   
6112 C  CB  . PRO   B 136 ? 0.2145 0.1794 0.3073 0.0312  -0.0224 -0.0027 136 PRO   B CB  
6113 C  CG  . PRO   B 136 ? 0.2411 0.1944 0.3254 0.0320  -0.0096 0.0039  136 PRO   B CG  
6114 C  CD  . PRO   B 136 ? 0.2454 0.1841 0.3147 0.0402  -0.0103 0.0212  136 PRO   B CD  
6122 N  N   . ILE   B 137 ? 0.1998 0.1335 0.3304 0.0105  -0.0047 -0.0001 137 ILE   B N   
6123 C  CA  . ILE   B 137 ? 0.2109 0.1313 0.3437 -0.0033 0.0040  -0.0023 137 ILE   B CA  
6124 C  C   . ILE   B 137 ? 0.1986 0.1288 0.3254 -0.0087 0.0181  0.0060  137 ILE   B C   
6125 O  O   . ILE   B 137 ? 0.1882 0.1384 0.3122 -0.0109 0.0094  0.0153  137 ILE   B O   
6126 C  CB  . ILE   B 137 ? 0.2430 0.1407 0.3742 0.0017  -0.0004 0.0006  137 ILE   B CB  
6127 C  CG1 . ILE   B 137 ? 0.2607 0.1582 0.4109 0.0065  -0.0058 -0.0048 137 ILE   B CG1 
6128 C  CG2 . ILE   B 137 ? 0.2499 0.1424 0.3785 -0.0264 -0.0012 0.0103  137 ILE   B CG2 
6129 C  CD1 . ILE   B 137 ? 0.2808 0.1942 0.4403 0.0163  -0.0194 0.0002  137 ILE   B CD1 
6141 N  N   . HIS   B 138 ? 0.2089 0.1365 0.3240 -0.0035 0.0228  0.0165  138 HIS   B N   
6142 C  CA  . HIS   B 138 ? 0.2162 0.1476 0.3140 -0.0021 0.0425  0.0251  138 HIS   B CA  
6143 C  C   . HIS   B 138 ? 0.1980 0.1431 0.2908 -0.0045 0.0437  0.0224  138 HIS   B C   
6144 O  O   . HIS   B 138 ? 0.1884 0.1499 0.3263 -0.0008 0.0437  0.0264  138 HIS   B O   
6145 C  CB  . HIS   B 138 ? 0.2463 0.1610 0.3291 -0.0122 0.0629  0.0277  138 HIS   B CB  
6146 C  CG  . HIS   B 138 ? 0.2700 0.1740 0.3384 -0.0173 0.0924  0.0425  138 HIS   B CG  
6147 N  ND1 . HIS   B 138 ? 0.2821 0.2002 0.3736 -0.0112 0.0999  0.0300  138 HIS   B ND1 
6148 C  CD2 . HIS   B 138 ? 0.2867 0.1830 0.3345 -0.0181 0.0982  0.0243  138 HIS   B CD2 
6149 C  CE1 . HIS   B 138 ? 0.2878 0.2048 0.3679 -0.0096 0.1010  0.0291  138 HIS   B CE1 
6150 N  NE2 . HIS   B 138 ? 0.2945 0.1862 0.3442 -0.0083 0.1057  0.0264  138 HIS   B NE2 
6158 N  N   . SER   B 139 ? 0.1926 0.1341 0.2841 -0.0019 0.0294  0.0130  139 SER   B N   
6159 C  CA  . SER   B 139 ? 0.1910 0.1309 0.2616 -0.0039 0.0290  0.0049  139 SER   B CA  
6160 C  C   . SER   B 139 ? 0.1642 0.1251 0.2662 -0.0008 0.0182  0.0051  139 SER   B C   
6161 O  O   . SER   B 139 ? 0.1604 0.1280 0.2668 0.0005  0.0077  0.0088  139 SER   B O   
6162 C  CB  . SER   B 139 ? 0.1960 0.1290 0.2690 -0.0016 0.0152  0.0030  139 SER   B CB  
6163 O  OG  . SER   B 139 ? 0.1901 0.1278 0.2823 -0.0018 -0.0099 0.0184  139 SER   B OG  
6169 N  N   . LEU   B 140 ? 0.1607 0.1228 0.2536 -0.0057 0.0268  -0.0045 140 LEU   B N   
6170 C  CA  . LEU   B 140 ? 0.1524 0.1235 0.2600 -0.0071 0.0158  0.0002  140 LEU   B CA  
6171 C  C   . LEU   B 140 ? 0.1486 0.1259 0.2747 -0.0077 0.0026  -0.0097 140 LEU   B C   
6172 O  O   . LEU   B 140 ? 0.1488 0.1345 0.2677 -0.0042 0.0017  -0.0001 140 LEU   B O   
6173 C  CB  . LEU   B 140 ? 0.1511 0.1275 0.2752 -0.0080 0.0164  -0.0043 140 LEU   B CB  
6174 C  CG  . LEU   B 140 ? 0.1578 0.1286 0.2794 -0.0126 0.0021  -0.0031 140 LEU   B CG  
6175 C  CD1 . LEU   B 140 ? 0.1720 0.1388 0.2926 -0.0138 0.0180  -0.0009 140 LEU   B CD1 
6176 C  CD2 . LEU   B 140 ? 0.1809 0.1435 0.2853 -0.0069 -0.0078 -0.0132 140 LEU   B CD2 
6188 N  N   A ARG   B 141 ? 0.1430 0.1300 0.2897 -0.0078 0.0126  -0.0036 141 ARG   B N   
6189 N  N   B ARG   B 141 ? 0.1472 0.1290 0.2824 -0.0084 0.0097  -0.0054 141 ARG   B N   
6190 C  CA  A ARG   B 141 ? 0.1492 0.1273 0.3159 -0.0162 0.0262  -0.0021 141 ARG   B CA  
6191 C  CA  B ARG   B 141 ? 0.1541 0.1267 0.2994 -0.0144 0.0191  -0.0058 141 ARG   B CA  
6192 C  C   A ARG   B 141 ? 0.1436 0.1231 0.3042 -0.0123 0.0135  -0.0019 141 ARG   B C   
6193 C  C   B ARG   B 141 ? 0.1480 0.1236 0.2954 -0.0136 0.0125  -0.0045 141 ARG   B C   
6194 O  O   A ARG   B 141 ? 0.1484 0.1309 0.3045 -0.0096 0.0013  -0.0153 141 ARG   B O   
6195 O  O   B ARG   B 141 ? 0.1521 0.1299 0.2941 -0.0142 0.0051  -0.0150 141 ARG   B O   
6196 C  CB  A ARG   B 141 ? 0.1715 0.1462 0.3360 -0.0250 0.0395  -0.0054 141 ARG   B CB  
6197 C  CB  B ARG   B 141 ? 0.1745 0.1409 0.3053 -0.0181 0.0242  -0.0128 141 ARG   B CB  
6198 C  CG  A ARG   B 141 ? 0.1985 0.1745 0.3452 -0.0180 0.0439  -0.0014 141 ARG   B CG  
6199 C  CG  B ARG   B 141 ? 0.1967 0.1614 0.2965 -0.0099 0.0196  -0.0152 141 ARG   B CG  
6200 C  CD  A ARG   B 141 ? 0.2341 0.2020 0.3527 -0.0164 0.0355  -0.0026 141 ARG   B CD  
6201 C  CD  B ARG   B 141 ? 0.2224 0.1722 0.2836 -0.0088 0.0072  -0.0319 141 ARG   B CD  
6202 N  NE  A ARG   B 141 ? 0.2499 0.2041 0.3445 -0.0229 0.0417  -0.0063 141 ARG   B NE  
6203 N  NE  B ARG   B 141 ? 0.2339 0.1697 0.2724 -0.0137 -0.0006 -0.0465 141 ARG   B NE  
6204 C  CZ  A ARG   B 141 ? 0.2685 0.2022 0.3360 -0.0220 0.0417  -0.0153 141 ARG   B CZ  
6205 C  CZ  B ARG   B 141 ? 0.2491 0.1618 0.2559 -0.0091 0.0001  -0.0583 141 ARG   B CZ  
6206 N  NH1 A ARG   B 141 ? 0.2821 0.1924 0.3300 -0.0221 0.0438  -0.0096 141 ARG   B NH1 
6207 N  NH1 B ARG   B 141 ? 0.2628 0.1480 0.2384 -0.0095 0.0048  -0.0552 141 ARG   B NH1 
6208 N  NH2 A ARG   B 141 ? 0.2747 0.2146 0.3425 -0.0100 0.0311  -0.0147 141 ARG   B NH2 
6209 N  NH2 B ARG   B 141 ? 0.2550 0.1782 0.2685 0.0039  -0.0118 -0.0458 141 ARG   B NH2 
6236 N  N   . VAL   B 142 ? 0.1503 0.1228 0.2976 -0.0112 0.0167  -0.0114 142 VAL   B N   
6237 C  CA  . VAL   B 142 ? 0.1450 0.1229 0.2890 -0.0070 0.0221  -0.0072 142 VAL   B CA  
6238 C  C   . VAL   B 142 ? 0.1375 0.1200 0.2905 -0.0068 0.0055  -0.0037 142 VAL   B C   
6239 O  O   . VAL   B 142 ? 0.1461 0.1237 0.2926 0.0023  0.0080  -0.0044 142 VAL   B O   
6240 C  CB  . VAL   B 142 ? 0.1550 0.1364 0.2835 -0.0068 0.0237  0.0047  142 VAL   B CB  
6241 C  CG1 . VAL   B 142 ? 0.1543 0.1410 0.2820 0.0043  0.0340  0.0009  142 VAL   B CG1 
6242 C  CG2 . VAL   B 142 ? 0.1806 0.1386 0.2920 -0.0004 0.0237  0.0075  142 VAL   B CG2 
6253 N  N   . CYS   B 143 ? 0.1361 0.1282 0.2677 -0.0021 0.0080  -0.0002 143 CYS   B N   
6254 C  CA  . CYS   B 143 ? 0.1345 0.1243 0.2722 -0.0041 0.0104  -0.0011 143 CYS   B CA  
6255 C  C   . CYS   B 143 ? 0.1298 0.1269 0.2735 -0.0066 0.0128  -0.0078 143 CYS   B C   
6256 O  O   . CYS   B 143 ? 0.1376 0.1352 0.2712 0.0007  0.0018  -0.0021 143 CYS   B O   
6257 C  CB  . CYS   B 143 ? 0.1406 0.1372 0.2503 -0.0054 0.0015  0.0002  143 CYS   B CB  
6258 S  SG  . CYS   B 143 ? 0.1473 0.1499 0.2447 -0.0063 0.0041  0.0027  143 CYS   B SG  
6264 N  N   . VAL   B 144 ? 0.1387 0.1320 0.2937 -0.0075 0.0020  -0.0126 144 VAL   B N   
6265 C  CA  . VAL   B 144 ? 0.1490 0.1385 0.3138 -0.0162 0.0012  -0.0241 144 VAL   B CA  
6266 C  C   . VAL   B 144 ? 0.1399 0.1333 0.3207 -0.0105 -0.0045 -0.0053 144 VAL   B C   
6267 O  O   . VAL   B 144 ? 0.1531 0.1573 0.3281 -0.0041 -0.0108 0.0186  144 VAL   B O   
6268 C  CB  . VAL   B 144 ? 0.1673 0.1586 0.3670 -0.0178 -0.0041 -0.0421 144 VAL   B CB  
6269 C  CG1 . VAL   B 144 ? 0.1926 0.2081 0.3989 -0.0063 -0.0044 -0.0398 144 VAL   B CG1 
6270 C  CG2 . VAL   B 144 ? 0.1852 0.1643 0.3530 -0.0036 -0.0235 -0.0607 144 VAL   B CG2 
6280 N  N   . ASP   B 145 ? 0.1379 0.1343 0.3297 -0.0057 0.0010  -0.0159 145 ASP   B N   
6281 C  CA  . ASP   B 145 ? 0.1382 0.1361 0.3513 -0.0077 0.0111  -0.0083 145 ASP   B CA  
6282 C  C   . ASP   B 145 ? 0.1370 0.1430 0.3329 -0.0112 0.0034  -0.0001 145 ASP   B C   
6283 O  O   . ASP   B 145 ? 0.1355 0.1524 0.3902 -0.0121 0.0109  -0.0177 145 ASP   B O   
6284 C  CB  . ASP   B 145 ? 0.1523 0.1474 0.3946 -0.0139 0.0271  -0.0016 145 ASP   B CB  
6285 C  CG  . ASP   B 145 ? 0.1712 0.1524 0.4472 -0.0187 0.0408  -0.0043 145 ASP   B CG  
6286 O  OD1 . ASP   B 145 ? 0.1725 0.1455 0.4481 -0.0246 0.0008  -0.0103 145 ASP   B OD1 
6287 O  OD2 . ASP   B 145 ? 0.2010 0.1600 0.4861 -0.0325 0.0634  -0.0058 145 ASP   B OD2 
6292 N  N   . THR   B 146 ? 0.1323 0.1291 0.2867 -0.0129 -0.0020 0.0025  146 THR   B N   
6293 C  CA  . THR   B 146 ? 0.1369 0.1305 0.2715 -0.0071 0.0117  -0.0005 146 THR   B CA  
6294 C  C   . THR   B 146 ? 0.1385 0.1293 0.2594 -0.0069 0.0005  -0.0056 146 THR   B C   
6295 O  O   . THR   B 146 ? 0.1449 0.1283 0.2612 -0.0021 -0.0013 0.0029  146 THR   B O   
6296 C  CB  . THR   B 146 ? 0.1390 0.1324 0.2773 -0.0043 0.0219  0.0027  146 THR   B CB  
6297 O  OG1 . THR   B 146 ? 0.1429 0.1324 0.2938 -0.0053 0.0303  0.0158  146 THR   B OG1 
6298 C  CG2 . THR   B 146 ? 0.1507 0.1432 0.2645 -0.0046 0.0217  -0.0039 146 THR   B CG2 
6306 N  N   . VAL   B 147 ? 0.1467 0.1345 0.2228 -0.0035 0.0121  0.0074  147 VAL   B N   
6307 C  CA  . VAL   B 147 ? 0.1422 0.1325 0.2258 -0.0101 -0.0010 0.0027  147 VAL   B CA  
6308 C  C   . VAL   B 147 ? 0.1403 0.1306 0.2421 -0.0210 -0.0078 -0.0035 147 VAL   B C   
6309 O  O   . VAL   B 147 ? 0.1562 0.1402 0.2509 -0.0170 -0.0287 -0.0043 147 VAL   B O   
6310 C  CB  . VAL   B 147 ? 0.1444 0.1448 0.2003 -0.0113 -0.0075 0.0016  147 VAL   B CB  
6311 C  CG1 . VAL   B 147 ? 0.1450 0.1555 0.1831 -0.0133 -0.0075 0.0029  147 VAL   B CG1 
6312 C  CG2 . VAL   B 147 ? 0.1442 0.1429 0.2234 -0.0108 0.0029  0.0034  147 VAL   B CG2 
6322 N  N   . ARG   B 148 ? 0.1408 0.1314 0.2371 -0.0104 -0.0160 -0.0083 148 ARG   B N   
6323 C  CA  . ARG   B 148 ? 0.1434 0.1391 0.2335 -0.0091 -0.0264 -0.0128 148 ARG   B CA  
6324 C  C   . ARG   B 148 ? 0.1487 0.1515 0.2246 -0.0103 -0.0380 -0.0047 148 ARG   B C   
6325 O  O   . ARG   B 148 ? 0.1648 0.1755 0.2446 -0.0307 -0.0494 0.0059  148 ARG   B O   
6326 C  CB  . ARG   B 148 ? 0.1513 0.1487 0.2322 -0.0042 -0.0263 -0.0210 148 ARG   B CB  
6327 C  CG  . ARG   B 148 ? 0.1515 0.1618 0.2411 -0.0100 -0.0261 -0.0356 148 ARG   B CG  
6328 C  CD  . ARG   B 148 ? 0.1590 0.1832 0.2498 0.0069  -0.0249 -0.0438 148 ARG   B CD  
6329 N  NE  . ARG   B 148 ? 0.1677 0.1857 0.2526 0.0213  -0.0408 -0.0446 148 ARG   B NE  
6330 C  CZ  . ARG   B 148 ? 0.1540 0.1765 0.2276 0.0145  -0.0343 -0.0332 148 ARG   B CZ  
6331 N  NH1 . ARG   B 148 ? 0.1469 0.1823 0.2241 0.0060  -0.0139 -0.0274 148 ARG   B NH1 
6332 N  NH2 . ARG   B 148 ? 0.1772 0.1577 0.2169 0.0165  -0.0209 -0.0195 148 ARG   B NH2 
6346 N  N   . THR   B 149 ? 0.1581 0.1412 0.2071 -0.0133 -0.0317 0.0073  149 THR   B N   
6347 C  CA  . THR   B 149 ? 0.1648 0.1442 0.1936 -0.0226 -0.0308 0.0069  149 THR   B CA  
6348 C  C   . THR   B 149 ? 0.1627 0.1458 0.1963 -0.0225 -0.0385 0.0032  149 THR   B C   
6349 O  O   . THR   B 149 ? 0.1683 0.1428 0.2118 -0.0216 -0.0168 0.0060  149 THR   B O   
6350 C  CB  . THR   B 149 ? 0.1688 0.1458 0.2085 -0.0132 -0.0365 -0.0013 149 THR   B CB  
6351 O  OG1 . THR   B 149 ? 0.1646 0.1498 0.2032 -0.0195 -0.0382 -0.0029 149 THR   B OG1 
6352 C  CG2 . THR   B 149 ? 0.1800 0.1557 0.2143 -0.0125 -0.0338 0.0065  149 THR   B CG2 
6360 N  N   . ASN   B 150 ? 0.1745 0.1441 0.1900 -0.0252 -0.0413 0.0007  150 ASN   B N   
6361 C  CA  . ASN   B 150 ? 0.1849 0.1655 0.1635 -0.0279 -0.0361 -0.0014 150 ASN   B CA  
6362 C  C   . ASN   B 150 ? 0.1635 0.1560 0.1749 -0.0195 -0.0292 -0.0002 150 ASN   B C   
6363 O  O   . ASN   B 150 ? 0.1669 0.1540 0.2053 -0.0290 -0.0392 0.0006  150 ASN   B O   
6364 C  CB  . ASN   B 150 ? 0.2072 0.2023 0.1810 -0.0359 -0.0519 0.0104  150 ASN   B CB  
6365 C  CG  . ASN   B 150 ? 0.2361 0.2427 0.2307 -0.0339 -0.0542 0.0262  150 ASN   B CG  
6366 O  OD1 . ASN   B 150 ? 0.2425 0.2655 0.2389 -0.0409 -0.0702 0.0234  150 ASN   B OD1 
6367 N  ND2 . ASN   B 150 ? 0.2556 0.2613 0.2746 -0.0255 -0.0574 0.0673  150 ASN   B ND2 
6374 N  N   . VAL   B 151 ? 0.1530 0.1550 0.1789 -0.0212 -0.0359 0.0037  151 VAL   B N   
6375 C  CA  . VAL   B 151 ? 0.1598 0.1568 0.1806 -0.0242 -0.0311 0.0013  151 VAL   B CA  
6376 C  C   . VAL   B 151 ? 0.1601 0.1492 0.1758 -0.0338 -0.0317 -0.0053 151 VAL   B C   
6377 O  O   . VAL   B 151 ? 0.1667 0.1621 0.2029 -0.0293 -0.0228 -0.0210 151 VAL   B O   
6378 C  CB  . VAL   B 151 ? 0.1870 0.1614 0.1922 -0.0106 -0.0323 0.0011  151 VAL   B CB  
6379 C  CG1 . VAL   B 151 ? 0.1994 0.1588 0.2352 -0.0246 -0.0191 -0.0058 151 VAL   B CG1 
6380 C  CG2 . VAL   B 151 ? 0.1970 0.1775 0.1804 -0.0040 -0.0249 0.0033  151 VAL   B CG2 
6390 N  N   . TYR   B 152 ? 0.1575 0.1351 0.1697 -0.0276 -0.0227 -0.0107 152 TYR   B N   
6391 C  CA  . TYR   B 152 ? 0.1598 0.1523 0.1671 -0.0299 -0.0191 -0.0095 152 TYR   B CA  
6392 C  C   . TYR   B 152 ? 0.1596 0.1400 0.1577 -0.0269 -0.0207 -0.0101 152 TYR   B C   
6393 O  O   . TYR   B 152 ? 0.1689 0.1415 0.1576 -0.0268 -0.0112 0.0040  152 TYR   B O   
6394 C  CB  . TYR   B 152 ? 0.1744 0.1725 0.1680 -0.0335 -0.0133 0.0063  152 TYR   B CB  
6395 C  CG  . TYR   B 152 ? 0.1911 0.1881 0.1633 -0.0477 -0.0187 -0.0003 152 TYR   B CG  
6396 C  CD1 . TYR   B 152 ? 0.2018 0.1996 0.1551 -0.0443 -0.0326 0.0103  152 TYR   B CD1 
6397 C  CD2 . TYR   B 152 ? 0.2166 0.2126 0.1671 -0.0461 -0.0106 -0.0145 152 TYR   B CD2 
6398 C  CE1 . TYR   B 152 ? 0.2220 0.2252 0.1743 -0.0401 -0.0394 0.0286  152 TYR   B CE1 
6399 C  CE2 . TYR   B 152 ? 0.2241 0.2364 0.1683 -0.0454 -0.0152 -0.0129 152 TYR   B CE2 
6400 C  CZ  . TYR   B 152 ? 0.2289 0.2462 0.1617 -0.0469 -0.0439 0.0202  152 TYR   B CZ  
6401 O  OH  . TYR   B 152 ? 0.2547 0.2823 0.2016 -0.0314 -0.0470 0.0215  152 TYR   B OH  
6411 N  N   . LEU   B 153 ? 0.1664 0.1348 0.1593 -0.0341 -0.0167 -0.0071 153 LEU   B N   
6412 C  CA  . LEU   B 153 ? 0.1651 0.1375 0.1612 -0.0253 -0.0056 -0.0084 153 LEU   B CA  
6413 C  C   . LEU   B 153 ? 0.1645 0.1322 0.1767 -0.0259 -0.0048 -0.0223 153 LEU   B C   
6414 O  O   . LEU   B 153 ? 0.1664 0.1607 0.1945 -0.0178 -0.0090 -0.0398 153 LEU   B O   
6415 C  CB  . LEU   B 153 ? 0.1630 0.1305 0.1708 -0.0323 -0.0057 0.0074  153 LEU   B CB  
6416 C  CG  . LEU   B 153 ? 0.1580 0.1446 0.2027 -0.0210 0.0038  0.0011  153 LEU   B CG  
6417 C  CD1 . LEU   B 153 ? 0.1671 0.1617 0.2232 -0.0293 0.0064  0.0101  153 LEU   B CD1 
6418 C  CD2 . LEU   B 153 ? 0.1635 0.1559 0.1991 -0.0227 0.0121  0.0029  153 LEU   B CD2 
6430 N  N   . ALA   B 154 ? 0.1608 0.1372 0.1839 -0.0102 -0.0096 -0.0191 154 ALA   B N   
6431 C  CA  . ALA   B 154 ? 0.1670 0.1470 0.2162 -0.0015 -0.0077 -0.0316 154 ALA   B CA  
6432 C  C   . ALA   B 154 ? 0.1850 0.1493 0.2117 0.0046  -0.0237 -0.0421 154 ALA   B C   
6433 O  O   . ALA   B 154 ? 0.2326 0.1460 0.2417 0.0096  -0.0188 -0.0152 154 ALA   B O   
6434 C  CB  . ALA   B 154 ? 0.1718 0.1695 0.2362 -0.0056 -0.0012 -0.0439 154 ALA   B CB  
6440 N  N   . VAL   B 155 ? 0.1531 0.1470 0.2354 -0.0069 -0.0018 -0.0224 155 VAL   B N   
6441 C  CA  . VAL   B 155 ? 0.1491 0.1409 0.2734 -0.0070 -0.0144 -0.0177 155 VAL   B CA  
6442 C  C   . VAL   B 155 ? 0.1449 0.1401 0.2644 -0.0010 -0.0104 -0.0361 155 VAL   B C   
6443 O  O   . VAL   B 155 ? 0.1609 0.1618 0.2920 0.0046  -0.0100 -0.0596 155 VAL   B O   
6444 C  CB  . VAL   B 155 ? 0.1576 0.1580 0.2916 -0.0062 -0.0224 -0.0002 155 VAL   B CB  
6445 C  CG1 . VAL   B 155 ? 0.1610 0.1522 0.2922 -0.0072 -0.0258 -0.0060 155 VAL   B CG1 
6446 C  CG2 . VAL   B 155 ? 0.1534 0.1685 0.3153 -0.0012 -0.0261 0.0398  155 VAL   B CG2 
6456 N  N   . PHE   B 156 ? 0.1346 0.1472 0.2831 0.0018  -0.0094 -0.0273 156 PHE   B N   
6457 C  CA  . PHE   B 156 ? 0.1433 0.1551 0.3177 0.0088  -0.0096 -0.0364 156 PHE   B CA  
6458 C  C   . PHE   B 156 ? 0.1460 0.1650 0.3536 0.0196  -0.0155 -0.0474 156 PHE   B C   
6459 O  O   . PHE   B 156 ? 0.1719 0.1911 0.3727 0.0304  -0.0094 -0.0602 156 PHE   B O   
6460 C  CB  . PHE   B 156 ? 0.1488 0.1513 0.3062 0.0063  -0.0044 -0.0393 156 PHE   B CB  
6461 C  CG  . PHE   B 156 ? 0.1493 0.1659 0.3071 0.0000  -0.0055 -0.0131 156 PHE   B CG  
6462 C  CD1 . PHE   B 156 ? 0.1541 0.1950 0.3433 0.0049  0.0036  0.0280  156 PHE   B CD1 
6463 C  CD2 . PHE   B 156 ? 0.1586 0.1761 0.2924 0.0143  -0.0189 -0.0150 156 PHE   B CD2 
6464 C  CE1 . PHE   B 156 ? 0.1538 0.2057 0.3511 0.0068  0.0026  0.0295  156 PHE   B CE1 
6465 C  CE2 . PHE   B 156 ? 0.1603 0.1895 0.3261 0.0148  -0.0216 -0.0041 156 PHE   B CE2 
6466 C  CZ  . PHE   B 156 ? 0.1513 0.2000 0.3511 0.0139  -0.0188 0.0046  156 PHE   B CZ  
6476 N  N   . ASP   B 157 ? 0.1498 0.1555 0.3752 0.0167  -0.0343 -0.0353 157 ASP   B N   
6477 C  CA  . ASP   B 157 ? 0.1708 0.1591 0.3970 0.0098  -0.0332 -0.0400 157 ASP   B CA  
6478 C  C   . ASP   B 157 ? 0.1685 0.1626 0.3914 0.0054  -0.0189 -0.0683 157 ASP   B C   
6479 O  O   . ASP   B 157 ? 0.1496 0.1622 0.3817 0.0087  -0.0159 -0.0447 157 ASP   B O   
6480 C  CB  . ASP   B 157 ? 0.1935 0.1710 0.4148 0.0060  -0.0582 -0.0270 157 ASP   B CB  
6481 C  CG  . ASP   B 157 ? 0.2356 0.1876 0.4387 0.0031  -0.0528 -0.0246 157 ASP   B CG  
6482 O  OD1 . ASP   B 157 ? 0.2412 0.1906 0.4515 0.0105  -0.0453 -0.0249 157 ASP   B OD1 
6483 O  OD2 . ASP   B 157 ? 0.2749 0.2133 0.4598 0.0006  -0.0372 -0.0226 157 ASP   B OD2 
6488 N  N   A LYS   B 158 ? 0.1648 0.1883 0.3927 0.0003  -0.0101 -0.0904 158 LYS   B N   
6489 N  N   B LYS   B 158 ? 0.1774 0.1945 0.3778 0.0060  -0.0107 -0.0833 158 LYS   B N   
6490 C  CA  A LYS   B 158 ? 0.1801 0.2042 0.3954 0.0008  -0.0034 -0.1146 158 LYS   B CA  
6491 C  CA  B LYS   B 158 ? 0.1998 0.2186 0.3715 0.0107  -0.0044 -0.0965 158 LYS   B CA  
6492 C  C   A LYS   B 158 ? 0.1775 0.1872 0.4104 0.0036  -0.0186 -0.1090 158 LYS   B C   
6493 C  C   B LYS   B 158 ? 0.2011 0.2110 0.3755 0.0162  -0.0145 -0.0880 158 LYS   B C   
6494 O  O   A LYS   B 158 ? 0.1736 0.1882 0.4202 0.0003  -0.0165 -0.1186 158 LYS   B O   
6495 O  O   B LYS   B 158 ? 0.2016 0.2149 0.3747 0.0147  -0.0149 -0.0858 158 LYS   B O   
6496 C  CB  A LYS   B 158 ? 0.2061 0.2501 0.3944 0.0022  0.0072  -0.1251 158 LYS   B CB  
6497 C  CB  B LYS   B 158 ? 0.2253 0.2547 0.3720 0.0134  0.0051  -0.1075 158 LYS   B CB  
6498 C  CG  A LYS   B 158 ? 0.2394 0.2936 0.3933 0.0019  0.0080  -0.1331 158 LYS   B CG  
6499 C  CG  B LYS   B 158 ? 0.2534 0.2871 0.3742 0.0135  0.0097  -0.1169 158 LYS   B CG  
6500 C  CD  A LYS   B 158 ? 0.2595 0.3325 0.4025 -0.0005 0.0126  -0.1227 158 LYS   B CD  
6501 C  CD  B LYS   B 158 ? 0.2731 0.3191 0.3853 0.0110  0.0143  -0.1116 158 LYS   B CD  
6502 C  CE  A LYS   B 158 ? 0.2773 0.3572 0.4073 0.0009  0.0107  -0.1167 158 LYS   B CE  
6503 C  CE  B LYS   B 158 ? 0.2894 0.3389 0.3925 0.0125  0.0149  -0.1091 158 LYS   B CE  
6504 N  NZ  A LYS   B 158 ? 0.2781 0.3673 0.4050 -0.0024 0.0073  -0.1188 158 LYS   B NZ  
6505 N  NZ  B LYS   B 158 ? 0.2931 0.3474 0.3934 0.0106  0.0140  -0.1105 158 LYS   B NZ  
6532 N  N   A ASN   B 159 ? 0.1779 0.1734 0.4353 0.0087  -0.0382 -0.0827 159 ASN   B N   
6533 N  N   B ASN   B 159 ? 0.1998 0.2020 0.3946 0.0216  -0.0263 -0.0756 159 ASN   B N   
6534 C  CA  A ASN   B 159 ? 0.1919 0.1617 0.4430 0.0181  -0.0594 -0.0653 159 ASN   B CA  
6535 C  CA  B ASN   B 159 ? 0.2035 0.1889 0.4057 0.0291  -0.0408 -0.0684 159 ASN   B CA  
6536 C  C   A ASN   B 159 ? 0.1794 0.1516 0.4395 0.0123  -0.0737 -0.0513 159 ASN   B C   
6537 C  C   B ASN   B 159 ? 0.1887 0.1688 0.4206 0.0223  -0.0516 -0.0620 159 ASN   B C   
6538 O  O   A ASN   B 159 ? 0.1789 0.1436 0.4498 -0.0051 -0.0935 -0.0281 159 ASN   B O   
6539 O  O   B ASN   B 159 ? 0.1893 0.1626 0.4291 0.0197  -0.0520 -0.0555 159 ASN   B O   
6540 C  CB  A ASN   B 159 ? 0.2138 0.1783 0.4601 0.0294  -0.0622 -0.0626 159 ASN   B CB  
6541 C  CB  B ASN   B 159 ? 0.2161 0.2009 0.4060 0.0415  -0.0451 -0.0666 159 ASN   B CB  
6542 C  CG  A ASN   B 159 ? 0.2479 0.2034 0.4689 0.0310  -0.0651 -0.0631 159 ASN   B CG  
6543 C  CG  B ASN   B 159 ? 0.2364 0.2200 0.4052 0.0475  -0.0484 -0.0628 159 ASN   B CG  
6544 O  OD1 A ASN   B 159 ? 0.2730 0.2143 0.4803 0.0375  -0.0557 -0.0699 159 ASN   B OD1 
6545 O  OD1 B ASN   B 159 ? 0.2480 0.2300 0.4115 0.0547  -0.0430 -0.0641 159 ASN   B OD1 
6546 N  ND2 A ASN   B 159 ? 0.2496 0.2154 0.4807 0.0268  -0.0700 -0.0544 159 ASN   B ND2 
6547 N  ND2 B ASN   B 159 ? 0.2396 0.2306 0.4175 0.0464  -0.0490 -0.0544 159 ASN   B ND2 
6560 N  N   . LEU   B 160 ? 0.1754 0.1599 0.4219 0.0134  -0.0570 -0.0493 160 LEU   B N   
6561 C  CA  . LEU   B 160 ? 0.1711 0.1609 0.3911 0.0128  -0.0501 -0.0327 160 LEU   B CA  
6562 C  C   . LEU   B 160 ? 0.1622 0.1472 0.3745 0.0003  -0.0318 -0.0449 160 LEU   B C   
6563 O  O   . LEU   B 160 ? 0.1492 0.1509 0.3775 0.0022  -0.0431 -0.0246 160 LEU   B O   
6564 C  CB  . LEU   B 160 ? 0.1704 0.1701 0.3681 0.0071  -0.0551 -0.0139 160 LEU   B CB  
6565 C  CG  . LEU   B 160 ? 0.1670 0.1805 0.3393 0.0101  -0.0411 0.0025  160 LEU   B CG  
6566 C  CD1 . LEU   B 160 ? 0.1899 0.2009 0.3405 -0.0057 -0.0221 0.0008  160 LEU   B CD1 
6567 C  CD2 . LEU   B 160 ? 0.1749 0.1795 0.3321 0.0204  -0.0286 -0.0080 160 LEU   B CD2 
6580 N  N   A TYR   B 161 ? 0.1592 0.1520 0.3706 -0.0068 -0.0106 -0.0615 161 TYR   B N   
6581 N  N   B TYR   B 161 ? 0.1649 0.1540 0.3635 -0.0052 -0.0127 -0.0587 161 TYR   B N   
6582 C  CA  A TYR   B 161 ? 0.1677 0.1546 0.3540 -0.0169 0.0147  -0.0642 161 TYR   B CA  
6583 C  CA  B TYR   B 161 ? 0.1762 0.1598 0.3443 -0.0114 0.0093  -0.0606 161 TYR   B CA  
6584 C  C   A TYR   B 161 ? 0.1733 0.1533 0.3539 -0.0090 0.0247  -0.0503 161 TYR   B C   
6585 C  C   B TYR   B 161 ? 0.1776 0.1564 0.3488 -0.0077 0.0193  -0.0520 161 TYR   B C   
6586 O  O   A TYR   B 161 ? 0.1760 0.1530 0.3477 -0.0172 0.0289  -0.0373 161 TYR   B O   
6587 O  O   B TYR   B 161 ? 0.1802 0.1564 0.3412 -0.0137 0.0234  -0.0442 161 TYR   B O   
6588 C  CB  A TYR   B 161 ? 0.1808 0.1653 0.3461 -0.0328 0.0350  -0.0665 161 TYR   B CB  
6589 C  CB  B TYR   B 161 ? 0.1943 0.1739 0.3264 -0.0196 0.0251  -0.0620 161 TYR   B CB  
6590 C  CG  A TYR   B 161 ? 0.2044 0.1656 0.3333 -0.0360 0.0505  -0.0759 161 TYR   B CG  
6591 C  CG  B TYR   B 161 ? 0.2205 0.1828 0.3104 -0.0231 0.0366  -0.0626 161 TYR   B CG  
6592 C  CD1 A TYR   B 161 ? 0.2110 0.1659 0.3251 -0.0450 0.0481  -0.0821 161 TYR   B CD1 
6593 C  CD1 B TYR   B 161 ? 0.2269 0.1869 0.3023 -0.0298 0.0411  -0.0649 161 TYR   B CD1 
6594 C  CD2 A TYR   B 161 ? 0.2276 0.1679 0.3262 -0.0388 0.0466  -0.0745 161 TYR   B CD2 
6595 C  CD2 B TYR   B 161 ? 0.2387 0.1880 0.3001 -0.0234 0.0360  -0.0572 161 TYR   B CD2 
6596 C  CE1 A TYR   B 161 ? 0.2292 0.1836 0.3313 -0.0461 0.0449  -0.0736 161 TYR   B CE1 
6597 C  CE1 B TYR   B 161 ? 0.2410 0.2015 0.3052 -0.0324 0.0404  -0.0573 161 TYR   B CE1 
6598 C  CE2 A TYR   B 161 ? 0.2441 0.1859 0.3318 -0.0418 0.0444  -0.0671 161 TYR   B CE2 
6599 C  CE2 B TYR   B 161 ? 0.2518 0.2021 0.3031 -0.0278 0.0397  -0.0502 161 TYR   B CE2 
6600 C  CZ  A TYR   B 161 ? 0.2457 0.1922 0.3303 -0.0536 0.0372  -0.0629 161 TYR   B CZ  
6601 C  CZ  B TYR   B 161 ? 0.2535 0.2078 0.3018 -0.0375 0.0338  -0.0473 161 TYR   B CZ  
6602 O  OH  A TYR   B 161 ? 0.2716 0.2160 0.3546 -0.0576 0.0339  -0.0616 161 TYR   B OH  
6603 O  OH  B TYR   B 161 ? 0.2699 0.2254 0.3187 -0.0419 0.0333  -0.0469 161 TYR   B OH  
6622 N  N   . ASP   B 162 ? 0.1781 0.1552 0.3607 -0.0132 0.0055  -0.0640 162 ASP   B N   
6623 C  CA  . ASP   B 162 ? 0.1850 0.1647 0.3703 -0.0083 -0.0100 -0.0629 162 ASP   B CA  
6624 C  C   . ASP   B 162 ? 0.1805 0.1567 0.3653 -0.0118 -0.0208 -0.0450 162 ASP   B C   
6625 O  O   . ASP   B 162 ? 0.1814 0.1569 0.3752 -0.0121 -0.0401 -0.0348 162 ASP   B O   
6626 C  CB  . ASP   B 162 ? 0.2025 0.1765 0.3927 -0.0002 -0.0178 -0.0837 162 ASP   B CB  
6627 C  CG  . ASP   B 162 ? 0.2045 0.2007 0.4243 0.0083  -0.0134 -0.0945 162 ASP   B CG  
6628 O  OD1 . ASP   B 162 ? 0.2045 0.2177 0.4133 -0.0008 -0.0074 -0.0957 162 ASP   B OD1 
6629 O  OD2 . ASP   B 162 ? 0.2171 0.2175 0.4508 0.0258  -0.0064 -0.0922 162 ASP   B OD2 
6635 N  N   . LYS   B 163 ? 0.1743 0.1392 0.3557 -0.0118 -0.0330 -0.0297 163 LYS   B N   
6636 C  CA  . LYS   B 163 ? 0.1863 0.1539 0.3592 -0.0147 -0.0242 -0.0184 163 LYS   B CA  
6637 C  C   . LYS   B 163 ? 0.1642 0.1484 0.3494 -0.0216 -0.0203 -0.0062 163 LYS   B C   
6638 O  O   . LYS   B 163 ? 0.1584 0.1606 0.3782 -0.0274 -0.0226 0.0015  163 LYS   B O   
6639 C  CB  . LYS   B 163 ? 0.2332 0.1892 0.3893 -0.0070 -0.0406 -0.0028 163 LYS   B CB  
6640 C  CG  . LYS   B 163 ? 0.3039 0.2583 0.4458 -0.0033 -0.0252 0.0001  163 LYS   B CG  
6641 C  CD  . LYS   B 163 ? 0.3637 0.3231 0.5005 -0.0131 -0.0226 -0.0052 163 LYS   B CD  
6642 C  CE  . LYS   B 163 ? 0.4030 0.3537 0.5372 -0.0221 -0.0187 -0.0053 163 LYS   B CE  
6643 N  NZ  . LYS   B 163 ? 0.4526 0.4007 0.5573 -0.0289 -0.0161 -0.0097 163 LYS   B NZ  
6657 N  N   . LEU   B 164 ? 0.1486 0.1398 0.3261 -0.0154 -0.0235 -0.0047 164 LEU   B N   
6658 C  CA  . LEU   B 164 ? 0.1495 0.1402 0.3110 -0.0085 -0.0291 -0.0009 164 LEU   B CA  
6659 C  C   . LEU   B 164 ? 0.1613 0.1412 0.3213 -0.0141 -0.0414 0.0091  164 LEU   B C   
6660 O  O   . LEU   B 164 ? 0.1629 0.1631 0.3340 -0.0154 -0.0369 0.0075  164 LEU   B O   
6661 C  CB  . LEU   B 164 ? 0.1459 0.1360 0.2979 -0.0046 -0.0206 -0.0045 164 LEU   B CB  
6662 C  CG  . LEU   B 164 ? 0.1603 0.1500 0.2948 -0.0085 -0.0095 0.0049  164 LEU   B CG  
6663 C  CD1 . LEU   B 164 ? 0.1703 0.1488 0.2835 -0.0178 -0.0209 -0.0159 164 LEU   B CD1 
6664 C  CD2 . LEU   B 164 ? 0.1764 0.1874 0.3122 -0.0106 0.0180  -0.0113 164 LEU   B CD2 
6676 N  N   . VAL   B 165 ? 0.2001 0.1534 0.3444 -0.0283 -0.0556 0.0003  165 VAL   B N   
6677 C  CA  . VAL   B 165 ? 0.2434 0.1684 0.3607 -0.0423 -0.0742 -0.0032 165 VAL   B CA  
6678 C  C   . VAL   B 165 ? 0.2774 0.1818 0.3939 -0.0498 -0.1105 -0.0056 165 VAL   B C   
6679 O  O   . VAL   B 165 ? 0.2969 0.1958 0.3983 -0.0563 -0.1174 0.0035  165 VAL   B O   
6680 C  CB  . VAL   B 165 ? 0.2737 0.1783 0.3546 -0.0243 -0.0371 -0.0173 165 VAL   B CB  
6681 C  CG1 . VAL   B 165 ? 0.2957 0.1895 0.3818 -0.0266 -0.0243 -0.0187 165 VAL   B CG1 
6682 C  CG2 . VAL   B 165 ? 0.2682 0.1776 0.3369 -0.0183 -0.0182 -0.0228 165 VAL   B CG2 
6692 N  N   . SER   B 166 ? 0.2887 0.1664 0.4437 -0.0520 -0.1200 -0.0198 166 SER   B N   
6693 C  CA  . SER   B 166 ? 0.2843 0.1638 0.4906 -0.0435 -0.1047 -0.0259 166 SER   B CA  
6694 C  C   . SER   B 166 ? 0.2661 0.1773 0.5085 -0.0405 -0.0922 0.0049  166 SER   B C   
6695 O  O   . SER   B 166 ? 0.2710 0.1984 0.5377 -0.0608 -0.1069 -0.0222 166 SER   B O   
6696 C  CB  . SER   B 166 ? 0.2764 0.1682 0.5142 -0.0327 -0.1013 -0.0359 166 SER   B CB  
6697 O  OG  . SER   B 166 ? 0.2574 0.1744 0.5297 -0.0238 -0.1033 -0.0149 166 SER   B OG  
6703 N  N   . SER   B 167 ? 0.2348 0.1697 0.4694 -0.0415 -0.0953 0.0407  167 SER   B N   
6704 C  CA  . SER   B 167 ? 0.2219 0.1799 0.4444 -0.0308 -0.0662 0.0513  167 SER   B CA  
6705 C  C   . SER   B 167 ? 0.2106 0.1948 0.4159 -0.0499 -0.0610 0.0739  167 SER   B C   
6706 O  O   . SER   B 167 ? 0.2013 0.2064 0.4212 -0.0595 -0.0595 0.0715  167 SER   B O   
6707 C  CB  . SER   B 167 ? 0.2114 0.1796 0.4573 -0.0263 -0.0334 0.0488  167 SER   B CB  
6708 O  OG  . SER   B 167 ? 0.2018 0.1954 0.4513 -0.0167 -0.0067 0.0435  167 SER   B OG  
6714 N  N   . PHE   B 168 ? 0.2173 0.1976 0.4043 -0.0468 -0.0451 0.0772  168 PHE   B N   
6715 C  CA  . PHE   B 168 ? 0.2125 0.1859 0.3566 -0.0528 -0.0320 0.0480  168 PHE   B CA  
6716 C  C   . PHE   B 168 ? 0.1823 0.1674 0.2870 -0.0282 -0.0122 0.0175  168 PHE   B C   
6717 O  O   . PHE   B 168 ? 0.2121 0.1626 0.2773 0.0011  -0.0074 -0.0071 168 PHE   B O   
6718 C  CB  . PHE   B 168 ? 0.2277 0.1945 0.3630 -0.0607 -0.0426 0.0542  168 PHE   B CB  
6719 C  CG  . PHE   B 168 ? 0.2524 0.1839 0.3498 -0.0594 -0.0369 0.0304  168 PHE   B CG  
6720 C  CD1 . PHE   B 168 ? 0.2781 0.1910 0.3656 -0.0571 -0.0444 0.0127  168 PHE   B CD1 
6721 C  CD2 . PHE   B 168 ? 0.2414 0.1732 0.3439 -0.0555 -0.0469 0.0241  168 PHE   B CD2 
6722 C  CE1 . PHE   B 168 ? 0.2869 0.1923 0.3482 -0.0474 -0.0343 0.0321  168 PHE   B CE1 
6723 C  CE2 . PHE   B 168 ? 0.2667 0.1820 0.3495 -0.0421 -0.0504 0.0222  168 PHE   B CE2 
6724 C  CZ  . PHE   B 168 ? 0.2787 0.1806 0.3508 -0.0291 -0.0441 0.0457  168 PHE   B CZ  
6734 N  N   . LEU   B 169 ? 0.1918 0.1737 0.2701 0.0027  0.0090  0.0154  169 LEU   B N   
6735 C  CA  . LEU   B 169 ? 0.2207 0.2104 0.3029 0.0007  0.0150  -0.0226 169 LEU   B CA  
6736 C  C   . LEU   B 169 ? 0.2601 0.2407 0.3550 0.0146  0.0040  -0.0445 169 LEU   B C   
6737 O  O   . LEU   B 169 ? 0.2850 0.2605 0.3972 0.0116  0.0057  -0.0676 169 LEU   B O   
6738 C  CB  . LEU   B 169 ? 0.2434 0.2534 0.3133 -0.0074 0.0072  -0.0009 169 LEU   B CB  
6739 C  CG  . LEU   B 169 ? 0.2875 0.2929 0.3539 -0.0001 0.0114  0.0041  169 LEU   B CG  
6740 C  CD1 . LEU   B 169 ? 0.3096 0.3102 0.3575 -0.0091 0.0044  0.0181  169 LEU   B CD1 
6741 C  CD2 . LEU   B 169 ? 0.2812 0.2985 0.3468 0.0213  0.0336  -0.0044 169 LEU   B CD2 
6742 O  OXT . LEU   B 169 ? 0.2842 0.2548 0.3483 0.0493  0.0161  -0.0454 169 LEU   B OXT 
6754 S  S   B DMS   C .   ? 0.2151 0.2026 0.2972 -0.0299 0.0043  0.0062  401 DMS   A S   
6755 O  O   B DMS   C .   ? 0.2077 0.1962 0.2673 -0.0436 0.0144  0.0086  401 DMS   A O   
6756 C  C1  B DMS   C .   ? 0.2196 0.2042 0.2932 -0.0271 0.0012  0.0079  401 DMS   A C1  
6757 C  C2  B DMS   C .   ? 0.2163 0.2088 0.3034 -0.0195 -0.0017 0.0074  401 DMS   A C2  
6764 N  N2  B A1A56 D .   ? 0.0987 0.0973 0.1062 -0.0075 -0.0046 0.0251  402 A1A56 A N2  
6765 C  C3  B A1A56 D .   ? 0.1189 0.1114 0.1183 0.0037  -0.0098 0.0136  402 A1A56 A C3  
6766 C  C6  B A1A56 D .   ? 0.0962 0.1219 0.0937 -0.0062 0.0146  0.0214  402 A1A56 A C6  
6767 C  C9  B A1A56 D .   ? 0.0863 0.1283 0.1122 -0.0092 0.0321  0.0143  402 A1A56 A C9  
6768 C  C1  B A1A56 D .   ? 0.1542 0.1386 0.1486 -0.0013 -0.0153 0.0085  402 A1A56 A C1  
6769 C  C10 B A1A56 D .   ? 0.0780 0.1155 0.1045 -0.0152 0.0259  0.0102  402 A1A56 A C10 
6770 C  C11 B A1A56 D .   ? 0.1150 0.0990 0.1106 -0.0081 -0.0114 0.0166  402 A1A56 A C11 
6771 C  C2  B A1A56 D .   ? 0.1387 0.1169 0.1145 -0.0043 -0.0167 0.0183  402 A1A56 A C2  
6772 C  C4  B A1A56 D .   ? 0.0964 0.1045 0.1238 0.0094  0.0034  0.0155  402 A1A56 A C4  
6773 C  C5  B A1A56 D .   ? 0.0994 0.1067 0.1066 -0.0095 0.0062  0.0108  402 A1A56 A C5  
6774 C  C7  B A1A56 D .   ? 0.0940 0.1157 0.0975 -0.0076 0.0255  0.0091  402 A1A56 A C7  
6775 C  C8  B A1A56 D .   ? 0.0925 0.1186 0.1090 -0.0077 0.0214  0.0067  402 A1A56 A C8  
6776 N  N1  B A1A56 D .   ? 0.1653 0.1462 0.1426 -0.0014 -0.0172 -0.0075 402 A1A56 A N1  
6777 N  N3  B A1A56 D .   ? 0.0934 0.1158 0.1116 -0.0172 -0.0008 0.0181  402 A1A56 A N3  
6778 N  N4  B A1A56 D .   ? 0.0960 0.1136 0.0816 -0.0172 0.0374  0.0329  402 A1A56 A N4  
6779 N  N5  B A1A56 D .   ? 0.0906 0.1098 0.1002 -0.0010 0.0172  0.0108  402 A1A56 A N5  
6780 O  O1  B A1A56 D .   ? 0.1483 0.1481 0.1525 0.0123  -0.0267 0.0221  402 A1A56 A O1  
6781 O  O2  B A1A56 D .   ? 0.1540 0.1098 0.1088 -0.0017 -0.0070 0.0097  402 A1A56 A O2  
6795 O  O1  C A1A57 E .   ? 0.2297 0.2854 0.2818 0.0093  -0.0237 -0.0209 403 A1A57 A O1  
6796 C  C1  C A1A57 E .   ? 0.2248 0.2758 0.2810 0.0056  -0.0196 -0.0219 403 A1A57 A C1  
6797 C  C2  C A1A57 E .   ? 0.2186 0.2723 0.2817 -0.0003 -0.0227 -0.0249 403 A1A57 A C2  
6798 C  C3  C A1A57 E .   ? 0.2097 0.2710 0.2776 -0.0041 -0.0271 -0.0239 403 A1A57 A C3  
6799 C  C4  C A1A57 E .   ? 0.2006 0.2709 0.2750 -0.0077 -0.0274 -0.0266 403 A1A57 A C4  
6800 C  C5  C A1A57 E .   ? 0.1761 0.2684 0.2134 -0.0155 -0.0357 -0.0060 403 A1A57 A C5  
6801 C  C6  C A1A57 E .   ? 0.1656 0.2733 0.2027 -0.0092 -0.0342 0.0074  403 A1A57 A C6  
6802 C  C7  C A1A57 E .   ? 0.1670 0.2651 0.1859 -0.0070 -0.0220 0.0014  403 A1A57 A C7  
6803 C  C8  C A1A57 E .   ? 0.1714 0.2622 0.1894 -0.0088 -0.0230 0.0005  403 A1A57 A C8  
6804 C  C10 C A1A57 E .   ? 0.1678 0.2612 0.1799 -0.0031 -0.0199 0.0029  403 A1A57 A C10 
6805 C  C11 C A1A57 E .   ? 0.2096 0.2769 0.2791 -0.0090 -0.0219 -0.0237 403 A1A57 A C11 
6806 C  C9  C A1A57 E .   ? 0.1721 0.2621 0.1765 -0.0058 -0.0194 0.0033  403 A1A57 A C9  
6807 N  N1  C A1A57 E .   ? 0.2291 0.2715 0.2883 0.0021  -0.0111 -0.0221 403 A1A57 A N1  
6808 N  N2  C A1A57 E .   ? 0.1942 0.2752 0.2580 -0.0087 -0.0302 -0.0207 403 A1A57 A N2  
6809 N  N3  C A1A57 E .   ? 0.1682 0.2690 0.2085 -0.0140 -0.0460 0.0079  403 A1A57 A N3  
6810 N  N4  C A1A57 E .   ? 0.1683 0.2723 0.2050 -0.0080 -0.0236 0.0042  403 A1A57 A N4  
6811 N  N5  C A1A57 E .   ? 0.1644 0.2593 0.1848 -0.0033 -0.0187 -0.0026 403 A1A57 A N5  
6812 O  O2  C A1A57 E .   ? 0.2195 0.2677 0.2896 0.0037  -0.0252 -0.0273 403 A1A57 A O2  
6826 CL CL  B CL    F .   ? 0.1970 0.1744 0.2506 -0.0216 0.0075  -0.0084 404 CL    A CL  
6827 O  O   . HOH   G .   ? 0.5803 0.2493 0.2893 -0.0505 0.0508  -0.0180 501 HOH   A O   
6828 O  O   B HOH   G .   ? 0.4704 0.6105 0.4593 -0.0960 0.1524  0.0624  502 HOH   A O   
6829 O  O   . HOH   G .   ? 0.4719 0.3616 0.4447 -0.0129 0.1309  0.0035  503 HOH   A O   
6830 O  O   A HOH   G .   ? 0.3577 0.6094 0.4501 -0.0709 -0.0076 0.1276  504 HOH   A O   
6831 O  O   . HOH   G .   ? 0.3064 0.6899 0.5562 -0.0658 -0.1035 0.1860  505 HOH   A O   
6832 O  O   . HOH   G .   ? 0.6004 0.7049 0.5193 -0.0214 0.0746  0.1254  506 HOH   A O   
6833 O  O   A HOH   G .   ? 0.4384 0.3543 0.4072 -0.0890 0.0373  0.1308  507 HOH   A O   
6834 O  O   . HOH   G .   ? 0.6970 0.5151 0.5322 -0.0514 0.0478  0.0309  508 HOH   A O   
6835 O  O   . HOH   G .   ? 0.3444 0.3584 0.1786 -0.0741 0.0659  0.0203  509 HOH   A O   
6836 O  O   . HOH   G .   ? 1.0911 1.0331 0.8713 -0.0224 -0.0959 -0.0681 510 HOH   A O   
6837 O  O   . HOH   G .   ? 0.6311 0.4917 0.3370 0.2127  -0.1170 0.0382  511 HOH   A O   
6838 O  O   . HOH   G .   ? 0.3154 0.2926 0.4736 -0.0622 -0.1510 0.1539  512 HOH   A O   
6839 O  O   A HOH   G .   ? 0.2166 0.1842 0.4431 -0.0221 -0.0690 0.0214  513 HOH   A O   
6840 O  O   . HOH   G .   ? 0.2623 0.5598 0.4154 0.0389  -0.0629 0.0718  514 HOH   A O   
6841 O  O   . HOH   G .   ? 0.5217 0.2313 0.6350 0.0600  0.0338  -0.0306 515 HOH   A O   
6842 O  O   B HOH   G .   ? 0.2614 0.2047 0.3122 -0.0144 0.0565  0.0374  516 HOH   A O   
6843 O  O   . HOH   G .   ? 0.2001 0.3892 0.4198 -0.0176 0.0503  -0.1107 517 HOH   A O   
6844 O  O   . HOH   G .   ? 0.1768 0.3918 0.3045 -0.0013 0.0276  0.1101  518 HOH   A O   
6845 O  O   B HOH   G .   ? 0.2527 0.1538 0.3898 -0.0280 -0.0924 -0.0010 519 HOH   A O   
6846 O  O   . HOH   G .   ? 0.1899 0.3013 0.3239 0.0368  -0.0137 -0.0327 520 HOH   A O   
6847 O  O   . HOH   G .   ? 0.6650 0.6038 0.3541 -0.0419 -0.0814 0.1207  521 HOH   A O   
6848 O  O   . HOH   G .   ? 0.5416 0.3986 0.3954 -0.1441 -0.1468 0.0304  522 HOH   A O   
6849 O  O   A HOH   G .   ? 0.3121 0.2906 0.2773 -0.0697 -0.0238 0.0958  523 HOH   A O   
6850 O  O   B HOH   G .   ? 0.3252 0.2083 0.3584 0.0568  -0.1185 0.0662  524 HOH   A O   
6851 O  O   . HOH   G .   ? 0.1776 0.1741 0.2577 -0.0288 0.0122  0.0399  525 HOH   A O   
6852 O  O   A HOH   G .   ? 0.2485 0.4302 0.4944 0.0345  0.0064  0.0697  526 HOH   A O   
6853 O  O   . HOH   G .   ? 0.5775 0.6203 0.5361 0.0337  0.3056  -0.0781 527 HOH   A O   
6854 O  O   . HOH   G .   ? 0.2188 0.1881 0.3773 -0.0485 0.0251  -0.0312 528 HOH   A O   
6855 O  O   . HOH   G .   ? 0.2984 0.2233 0.2758 -0.0492 0.0342  -0.0147 529 HOH   A O   
6856 O  O   . HOH   G .   ? 0.2447 0.2110 0.1964 -0.0622 0.0113  0.0446  530 HOH   A O   
6857 O  O   . HOH   G .   ? 0.6200 0.6515 0.6295 -0.1308 -0.1256 -0.1139 531 HOH   A O   
6858 O  O   . HOH   G .   ? 0.4583 0.5655 0.5449 0.1845  0.0799  -0.1287 532 HOH   A O   
6859 O  O   . HOH   G .   ? 0.4820 0.6240 0.3889 -0.1587 0.1386  0.1139  533 HOH   A O   
6860 O  O   . HOH   G .   ? 0.4802 0.4914 0.6400 -0.0195 0.1253  0.2977  534 HOH   A O   
6861 O  O   . HOH   G .   ? 0.6774 0.5899 0.4866 0.1518  -0.1010 -0.0115 535 HOH   A O   
6862 O  O   . HOH   G .   ? 0.3478 0.3482 0.4959 -0.0605 0.1821  0.0209  536 HOH   A O   
6863 O  O   . HOH   G .   ? 0.3331 0.3022 0.3098 -0.0361 -0.0951 0.0242  537 HOH   A O   
6864 O  O   . HOH   G .   ? 0.2292 0.3011 0.3790 -0.0470 -0.0791 0.1193  538 HOH   A O   
6865 O  O   . HOH   G .   ? 0.2706 0.3101 0.3918 -0.0061 -0.0090 -0.0651 539 HOH   A O   
6866 O  O   A HOH   G .   ? 0.2042 0.2036 0.2795 0.0141  0.1024  0.0338  540 HOH   A O   
6867 O  O   . HOH   G .   ? 0.4141 0.5905 0.3808 -0.0238 -0.0440 0.1409  541 HOH   A O   
6868 O  O   . HOH   G .   ? 0.6576 0.5675 0.8387 -0.0990 0.0029  0.1442  542 HOH   A O   
6869 O  O   . HOH   G .   ? 0.2552 0.1874 0.2789 0.0055  0.0021  0.0252  543 HOH   A O   
6870 O  O   . HOH   G .   ? 0.2634 0.4658 0.3398 0.1257  -0.0646 -0.0245 544 HOH   A O   
6871 O  O   A HOH   G .   ? 0.2098 0.6271 0.2565 0.0577  0.0112  0.0417  545 HOH   A O   
6872 O  O   B HOH   G .   ? 0.1442 0.1512 0.1998 0.0057  0.0097  0.0204  546 HOH   A O   
6873 O  O   A HOH   G .   ? 0.3602 0.3703 0.4850 -0.0648 0.1349  0.1705  547 HOH   A O   
6874 O  O   . HOH   G .   ? 0.4730 0.3287 0.5281 0.0838  -0.0392 -0.0178 548 HOH   A O   
6875 O  O   . HOH   G .   ? 0.3400 0.3159 0.3574 -0.0593 0.0047  -0.0310 549 HOH   A O   
6876 O  O   . HOH   G .   ? 0.1430 0.2143 0.2339 -0.0044 -0.0088 0.0485  550 HOH   A O   
6877 O  O   A HOH   G .   ? 0.3717 0.5730 0.7698 -0.0480 -0.0936 0.2415  551 HOH   A O   
6878 O  O   . HOH   G .   ? 0.5687 0.1925 0.4332 0.0492  -0.1443 0.0363  552 HOH   A O   
6879 O  O   . HOH   G .   ? 0.2259 0.2065 0.2768 0.0361  0.0297  0.0425  553 HOH   A O   
6880 O  O   . HOH   G .   ? 0.2660 0.3947 0.4125 -0.0869 -0.0836 -0.0457 554 HOH   A O   
6881 O  O   . HOH   G .   ? 0.4066 0.3729 0.4448 -0.1700 -0.0990 0.1948  555 HOH   A O   
6882 O  O   . HOH   G .   ? 0.3353 0.4407 0.2402 -0.0419 0.0424  0.0149  556 HOH   A O   
6883 O  O   . HOH   G .   ? 0.1909 0.2547 0.2313 -0.0395 -0.0207 0.1050  557 HOH   A O   
6884 O  O   A HOH   G .   ? 0.1670 0.2576 0.2398 0.0649  0.0548  0.0541  558 HOH   A O   
6885 O  O   . HOH   G .   ? 0.3308 0.3991 0.2273 -0.1307 -0.0089 -0.0659 559 HOH   A O   
6886 O  O   . HOH   G .   ? 0.2565 0.3137 0.3145 -0.0331 0.1052  -0.0236 560 HOH   A O   
6887 O  O   . HOH   G .   ? 0.3296 0.4384 0.5009 -0.0827 0.1783  0.0445  561 HOH   A O   
6888 O  O   . HOH   G .   ? 0.2074 0.2052 0.4132 0.0279  0.1016  0.0008  562 HOH   A O   
6889 O  O   . HOH   G .   ? 0.2261 0.1780 0.2533 0.0352  -0.0269 0.0043  563 HOH   A O   
6890 O  O   . HOH   G .   ? 0.4058 0.4767 0.4899 0.2204  0.1048  0.0464  564 HOH   A O   
6891 O  O   . HOH   G .   ? 0.4185 0.7131 0.3758 -0.1014 -0.0107 0.1397  565 HOH   A O   
6892 O  O   . HOH   G .   ? 0.3115 0.3350 0.4707 -0.0714 -0.0956 -0.0909 566 HOH   A O   
6893 O  O   . HOH   G .   ? 0.1504 0.1933 0.2593 0.0054  0.0021  0.0110  567 HOH   A O   
6894 O  O   . HOH   G .   ? 0.2174 0.1881 0.3609 -0.0108 -0.0274 -0.0064 568 HOH   A O   
6895 O  O   B HOH   G .   ? 0.2152 0.1937 0.0965 -0.0072 -0.0459 0.0264  569 HOH   A O   
6896 O  O   . HOH   G .   ? 0.1395 0.1374 0.1480 -0.0021 0.0144  0.0129  570 HOH   A O   
6897 O  O   . HOH   G .   ? 0.4133 0.8276 0.5918 -0.1049 -0.1762 0.1177  571 HOH   A O   
6898 O  O   . HOH   G .   ? 0.1710 0.1867 0.2318 0.0137  -0.0268 0.0367  572 HOH   A O   
6899 O  O   B HOH   G .   ? 0.2346 0.1620 0.2080 -0.0011 0.0365  0.0559  573 HOH   A O   
6900 O  O   A HOH   G .   ? 0.1429 0.1491 0.1504 0.0208  -0.0282 -0.0044 574 HOH   A O   
6901 O  O   . HOH   G .   ? 0.1668 0.1373 0.2520 -0.0114 0.0287  -0.0055 575 HOH   A O   
6902 O  O   . HOH   G .   ? 0.2410 0.2526 0.3181 -0.0026 -0.0201 0.0801  576 HOH   A O   
6903 O  O   . HOH   G .   ? 0.3474 0.2568 0.4318 -0.0611 -0.0034 -0.0290 577 HOH   A O   
6904 O  O   . HOH   G .   ? 0.4268 0.2345 0.3143 0.1183  0.0724  0.0292  578 HOH   A O   
6905 O  O   . HOH   G .   ? 0.2555 0.4384 0.3475 -0.0276 0.0405  0.0242  579 HOH   A O   
6906 O  O   . HOH   G .   ? 0.2148 0.2622 0.4973 0.0095  0.1087  -0.1007 580 HOH   A O   
6907 O  O   . HOH   G .   ? 0.6775 0.4229 0.3420 0.0955  0.0145  0.1470  581 HOH   A O   
6908 O  O   . HOH   G .   ? 0.1495 0.1646 0.1546 -0.0122 -0.0120 0.0025  582 HOH   A O   
6909 O  O   . HOH   G .   ? 0.2613 0.4759 0.3889 0.0629  0.0927  0.2380  583 HOH   A O   
6910 O  O   . HOH   G .   ? 0.3323 0.2931 0.3643 -0.0250 -0.0356 0.1077  584 HOH   A O   
6911 O  O   . HOH   G .   ? 0.2106 0.2385 0.2532 -0.0358 -0.0519 0.0616  585 HOH   A O   
6912 O  O   . HOH   G .   ? 0.4117 0.2229 0.4663 -0.0930 0.1045  0.0302  586 HOH   A O   
6913 O  O   . HOH   G .   ? 0.4876 0.2707 0.3412 -0.1667 0.1639  -0.0477 587 HOH   A O   
6914 O  O   . HOH   G .   ? 0.1872 0.1930 0.2447 -0.0247 0.0122  0.0189  588 HOH   A O   
6915 O  O   . HOH   G .   ? 0.4197 0.4587 0.5957 0.1549  0.0831  -0.1443 589 HOH   A O   
6916 O  O   B HOH   G .   ? 0.1687 0.1587 0.2674 0.0101  -0.0707 0.0015  590 HOH   A O   
6917 O  O   . HOH   G .   ? 0.5196 0.6904 0.5297 0.1337  -0.1410 -0.1338 591 HOH   A O   
6918 O  O   . HOH   G .   ? 0.3426 0.7400 0.2787 0.1705  0.0633  -0.0349 592 HOH   A O   
6919 O  O   B HOH   G .   ? 0.1814 0.1950 0.2568 -0.0066 -0.0450 0.0069  593 HOH   A O   
6920 O  O   . HOH   G .   ? 0.2611 0.3798 0.4068 -0.0311 0.1315  -0.0902 594 HOH   A O   
6921 O  O   . HOH   G .   ? 0.3263 0.2977 0.2314 0.0036  0.0625  0.0042  595 HOH   A O   
6922 O  O   . HOH   G .   ? 0.2159 0.2011 0.1831 0.0034  0.0202  0.0267  596 HOH   A O   
6923 O  O   B HOH   G .   ? 0.3115 0.1355 0.3674 -0.0633 -0.0635 0.0018  597 HOH   A O   
6924 O  O   . HOH   G .   ? 0.2979 0.2524 0.2444 -0.0563 -0.0830 0.0349  598 HOH   A O   
6925 O  O   . HOH   G .   ? 0.1877 0.1904 0.4037 0.0424  0.1071  0.0925  599 HOH   A O   
6926 O  O   A HOH   G .   ? 0.5248 0.4057 0.3512 -0.1307 0.0313  0.1555  600 HOH   A O   
6927 O  O   A HOH   G .   ? 0.3622 0.2808 0.4967 0.0418  0.1388  0.0879  601 HOH   A O   
6928 O  O   . HOH   G .   ? 0.2111 0.2269 0.3825 -0.0032 -0.0560 0.0683  602 HOH   A O   
6929 O  O   . HOH   G .   ? 0.2352 0.1831 0.3383 0.0055  -0.0381 0.0133  603 HOH   A O   
6930 O  O   . HOH   G .   ? 0.1274 0.1447 0.2071 -0.0024 -0.0231 0.0068  604 HOH   A O   
6931 O  O   . HOH   G .   ? 0.1985 0.2209 0.2818 -0.0079 -0.0254 0.0838  605 HOH   A O   
6932 O  O   . HOH   G .   ? 0.7730 0.4875 0.5876 0.0427  -0.1292 0.0468  606 HOH   A O   
6933 O  O   A HOH   G .   ? 0.3238 0.2062 0.2563 0.0467  0.0578  0.0680  607 HOH   A O   
6934 O  O   A HOH   G .   ? 0.1410 0.1490 0.1935 -0.0001 -0.0058 0.0285  608 HOH   A O   
6935 O  O   A HOH   G .   ? 0.1232 0.2482 0.2834 -0.0017 0.0749  0.0700  609 HOH   A O   
6936 O  O   . HOH   G .   ? 0.5935 0.5673 0.1894 -0.0094 0.0587  0.0634  610 HOH   A O   
6937 O  O   . HOH   G .   ? 0.1567 0.1727 0.3523 -0.0028 0.0042  0.0218  611 HOH   A O   
6938 O  O   . HOH   G .   ? 0.3589 0.3763 0.3967 -0.1562 0.1276  -0.0215 612 HOH   A O   
6939 O  O   . HOH   G .   ? 0.6282 0.6752 0.6550 -0.1287 0.0450  -0.0500 613 HOH   A O   
6940 O  O   A HOH   G .   ? 0.1422 0.1501 0.1225 0.0056  0.0014  -0.0116 614 HOH   A O   
6941 O  O   . HOH   G .   ? 0.4902 0.2700 0.3049 -0.1371 0.0453  0.0260  615 HOH   A O   
6942 O  O   . HOH   G .   ? 0.2450 0.3574 0.7543 -0.0285 0.0342  -0.0440 616 HOH   A O   
6943 O  O   . HOH   G .   ? 0.1756 0.1526 0.1645 -0.0271 0.0247  0.0018  617 HOH   A O   
6944 O  O   . HOH   G .   ? 0.1988 0.2952 0.2727 -0.0114 -0.0506 0.0728  618 HOH   A O   
6945 O  O   . HOH   G .   ? 0.2632 0.2287 0.2784 -0.0531 0.0104  0.0533  619 HOH   A O   
6946 O  O   A HOH   G .   ? 0.3936 0.5157 0.4705 -0.1564 0.0663  0.0744  620 HOH   A O   
6947 O  O   A HOH   G .   ? 0.3736 0.5667 0.3230 0.1379  -0.0330 -0.0224 621 HOH   A O   
6948 O  O   . HOH   G .   ? 0.3261 0.1379 0.2162 -0.0019 -0.0553 0.0160  622 HOH   A O   
6949 O  O   . HOH   G .   ? 0.2116 0.1745 0.1700 -0.0085 0.0251  0.0188  623 HOH   A O   
6950 O  O   . HOH   G .   ? 0.1720 0.2232 0.2928 -0.0225 0.0067  0.0452  624 HOH   A O   
6951 O  O   . HOH   G .   ? 0.4261 0.6512 0.6173 0.2531  0.1788  0.0754  625 HOH   A O   
6952 O  O   . HOH   G .   ? 0.1936 0.2658 0.4892 -0.0217 -0.0229 0.0291  626 HOH   A O   
6953 O  O   . HOH   G .   ? 0.2803 0.6333 0.1939 0.0003  0.0614  0.0406  627 HOH   A O   
6954 O  O   . HOH   G .   ? 0.6096 0.8354 0.8185 -0.0319 -0.0903 -0.0526 628 HOH   A O   
6955 O  O   . HOH   G .   ? 0.4883 0.5222 0.5762 -0.1257 -0.0790 -0.1539 629 HOH   A O   
6956 O  O   . HOH   G .   ? 0.7843 0.9552 0.6154 0.2821  -0.1436 0.2275  630 HOH   A O   
6957 O  O   . HOH   G .   ? 0.4076 0.6973 0.3382 -0.0566 0.0044  0.1753  631 HOH   A O   
6958 O  O   . HOH   G .   ? 0.2092 0.2568 0.3239 -0.0090 -0.0218 0.0155  632 HOH   A O   
6959 O  O   B HOH   G .   ? 0.1510 0.1758 0.2936 0.0248  0.0691  0.1172  633 HOH   A O   
6960 O  O   . HOH   G .   ? 0.5623 0.4761 0.4443 -0.0365 -0.1610 -0.0301 634 HOH   A O   
6961 O  O   . HOH   G .   ? 0.2394 0.3793 0.2984 0.1371  0.0008  0.0287  635 HOH   A O   
6962 O  O   B HOH   G .   ? 0.3094 0.3063 0.2977 -0.0321 0.0729  -0.1141 636 HOH   A O   
6963 O  O   A HOH   G .   ? 0.5204 0.4452 0.2669 -0.1240 0.0234  0.1454  637 HOH   A O   
6964 O  O   . HOH   G .   ? 0.6153 0.4450 0.5493 0.1835  -0.0693 0.1563  638 HOH   A O   
6965 O  O   . HOH   G .   ? 0.4314 0.2362 0.5760 -0.0907 -0.2429 0.1116  639 HOH   A O   
6966 O  O   . HOH   G .   ? 0.7378 0.6394 0.8009 -0.0113 -0.0814 0.2537  640 HOH   A O   
6967 O  O   . HOH   G .   ? 0.5711 0.7104 0.4549 0.0469  0.2887  -0.0608 641 HOH   A O   
6968 O  O   A HOH   G .   ? 0.1875 0.1643 0.1575 -0.0008 0.0237  -0.0193 642 HOH   A O   
6969 O  O   . HOH   G .   ? 0.1966 0.2126 0.4528 -0.0163 -0.0781 0.0629  643 HOH   A O   
6970 O  O   . HOH   G .   ? 0.2789 0.1783 0.3083 0.0187  0.0200  0.0218  644 HOH   A O   
6971 O  O   . HOH   G .   ? 0.3916 0.3053 0.1994 -0.1115 0.0212  0.0778  645 HOH   A O   
6972 O  O   . HOH   G .   ? 0.3971 0.3627 0.3636 0.2208  -0.0628 -0.0545 646 HOH   A O   
6973 O  O   A HOH   G .   ? 0.3041 0.2413 0.2360 -0.0939 -0.0071 0.0211  647 HOH   A O   
6974 O  O   . HOH   G .   ? 0.8605 0.5733 0.5267 -0.1170 0.1489  0.1075  648 HOH   A O   
6975 O  O   A HOH   G .   ? 0.1835 0.1539 0.2641 0.0125  -0.0669 0.0201  649 HOH   A O   
6976 O  O   . HOH   G .   ? 0.2774 0.3684 0.6041 -0.0158 0.1197  -0.1561 650 HOH   A O   
6977 O  O   . HOH   G .   ? 0.4785 0.2408 0.6338 -0.0373 0.1191  -0.0557 651 HOH   A O   
6978 O  O   A HOH   G .   ? 0.2504 0.2027 0.2889 0.0151  -0.0708 0.0117  652 HOH   A O   
6979 O  O   . HOH   G .   ? 0.7540 0.7059 0.7415 0.0279  -0.0727 -0.0483 653 HOH   A O   
6980 O  O   . HOH   G .   ? 0.2394 0.2843 0.2611 0.0159  -0.0089 -0.0472 654 HOH   A O   
6981 O  O   A HOH   G .   ? 0.5978 0.2912 0.3975 0.1459  0.1880  0.1364  655 HOH   A O   
6982 O  O   . HOH   G .   ? 0.2184 0.2102 0.2830 0.0063  0.0200  0.0455  656 HOH   A O   
6983 O  O   . HOH   G .   ? 0.7175 0.6505 0.7817 -0.1386 0.0066  -0.1291 657 HOH   A O   
6984 O  O   . HOH   G .   ? 0.4688 0.3231 0.3393 0.0616  0.0675  0.0023  658 HOH   A O   
6985 O  O   . HOH   G .   ? 0.6495 0.6950 0.5025 -0.0866 0.1205  0.1199  659 HOH   A O   
6986 O  O   . HOH   G .   ? 0.3978 0.3947 0.3761 0.1950  -0.0260 0.0248  660 HOH   A O   
6987 O  O   . HOH   G .   ? 0.4488 0.4987 0.4116 0.0261  0.1620  -0.0529 661 HOH   A O   
6988 O  O   . HOH   G .   ? 0.8083 0.7695 0.4929 0.0154  -0.0995 -0.0115 662 HOH   A O   
6989 O  O   . HOH   G .   ? 0.2554 0.2654 0.4431 -0.0423 0.0332  -0.0989 663 HOH   A O   
6990 O  O   B HOH   G .   ? 0.3733 0.3896 0.3653 0.0726  -0.0301 0.0653  664 HOH   A O   
6991 O  O   . HOH   G .   ? 0.5623 0.5354 0.4531 -0.0058 -0.0025 0.0499  665 HOH   A O   
6992 O  O   . HOH   G .   ? 0.3143 0.3767 0.6115 0.0244  -0.1202 -0.0774 666 HOH   A O   
6993 O  O   B HOH   G .   ? 0.2092 0.2896 0.2994 -0.0063 0.0310  -0.0057 667 HOH   A O   
6994 O  O   . HOH   G .   ? 0.4317 0.4951 0.5181 0.0878  -0.0144 0.1567  668 HOH   A O   
6995 O  O   . HOH   G .   ? 0.3589 0.5092 0.5632 -0.1645 0.1698  -0.1913 669 HOH   A O   
6996 O  O   . HOH   G .   ? 0.2626 0.4652 0.5319 0.0495  0.0096  -0.1628 670 HOH   A O   
6997 O  O   . HOH   G .   ? 0.4023 0.6586 0.4120 -0.1255 -0.1419 0.2442  671 HOH   A O   
6998 O  O   . HOH   G .   ? 0.2862 0.2632 0.3607 -0.0897 0.0284  -0.0247 672 HOH   A O   
6999 O  O   . HOH   G .   ? 0.6355 0.3471 0.7352 0.0957  0.0244  0.2417  673 HOH   A O   
7000 O  O   . HOH   G .   ? 0.3399 0.4993 0.5031 -0.1253 0.0296  0.0058  674 HOH   A O   
7001 O  O   . HOH   G .   ? 0.4168 0.5853 0.4019 0.0676  -0.0988 -0.0764 675 HOH   A O   
7002 O  O   . HOH   G .   ? 0.6248 0.5602 0.4485 0.1671  -0.0159 -0.0686 676 HOH   A O   
7003 O  O   . HOH   G .   ? 0.3311 0.2680 0.4299 0.0126  0.1051  -0.0101 677 HOH   A O   
7004 O  O   . HOH   G .   ? 0.2638 0.1771 0.2724 0.0211  -0.0866 -0.0221 678 HOH   A O   
7005 O  O   . HOH   G .   ? 0.5533 0.4476 0.4925 0.0108  0.0999  0.0135  679 HOH   A O   
7006 O  O   . HOH   G .   ? 0.8339 0.7786 0.6448 0.1962  -0.1504 -0.0852 680 HOH   A O   
7007 O  O   A HOH   G .   ? 0.5415 0.4364 0.3949 0.0334  0.0445  0.1032  681 HOH   A O   
7008 O  O   B HOH   G .   ? 0.4671 0.2367 0.3535 -0.0838 0.0052  0.0586  682 HOH   A O   
7009 O  O   . HOH   G .   ? 0.4187 0.4595 0.4666 -0.2201 0.0110  -0.0351 683 HOH   A O   
7010 O  O   . HOH   G .   ? 0.5640 0.6661 0.6010 -0.1718 -0.1350 -0.0140 684 HOH   A O   
7011 O  O   . HOH   G .   ? 0.2564 0.2706 0.2618 0.0366  0.0032  -0.0048 685 HOH   A O   
7012 O  O   . HOH   G .   ? 0.3789 0.5264 0.2965 0.0446  0.0234  0.0259  686 HOH   A O   
7013 O  O   . HOH   G .   ? 0.4517 0.2808 0.3805 -0.0693 -0.1463 0.0604  687 HOH   A O   
7014 O  O   . HOH   G .   ? 0.7789 0.6872 0.7802 -0.0497 0.0406  -0.1098 688 HOH   A O   
7015 O  O   . HOH   G .   ? 0.6139 0.5091 0.4841 -0.0776 -0.0395 -0.1064 689 HOH   A O   
7016 O  O   . HOH   G .   ? 0.6730 0.5136 0.5347 -0.1230 -0.0207 -0.0575 690 HOH   A O   
7017 O  O   . HOH   G .   ? 0.3375 0.4593 0.4873 0.0110  0.1536  0.1328  691 HOH   A O   
7018 O  O   . HOH   G .   ? 0.8439 0.4049 0.4244 -0.0307 0.1637  0.0044  692 HOH   A O   
7019 O  O   . HOH   G .   ? 0.4365 0.3171 0.4961 -0.0936 -0.0269 0.1279  693 HOH   A O   
7020 O  O   . HOH   G .   ? 0.4526 0.5468 0.3318 -0.0209 -0.0365 -0.0122 694 HOH   A O   
7021 O  O   . HOH   G .   ? 0.5816 0.5932 0.4602 0.1268  -0.0369 -0.0432 695 HOH   A O   
7022 O  O   . HOH   G .   ? 0.2641 0.2383 0.7418 0.0043  -0.1203 0.0482  696 HOH   A O   
7023 O  O   . HOH   G .   ? 0.2626 0.5407 0.3843 0.0901  0.0974  0.2462  697 HOH   A O   
7024 O  O   . HOH   G .   ? 0.5160 0.3972 0.2848 -0.1388 0.1610  -0.0759 698 HOH   A O   
7025 O  O   . HOH   G .   ? 0.8150 0.7433 0.5022 -0.1065 0.1308  0.2106  699 HOH   A O   
7026 O  O   . HOH   G .   ? 0.3012 0.2946 0.5827 -0.0006 0.1354  -0.0809 700 HOH   A O   
7027 O  O   . HOH   G .   ? 0.3201 0.2413 0.6499 0.0269  0.0767  0.0763  701 HOH   A O   
7028 O  O   B HOH   G .   ? 0.1682 0.2027 0.2438 -0.0341 0.0018  0.0191  702 HOH   A O   
7029 O  O   . HOH   G .   ? 0.6310 0.7267 0.7677 0.0900  0.2605  -0.1244 703 HOH   A O   
7030 O  O   . HOH   G .   ? 0.8437 0.4109 0.3378 -0.0139 -0.1435 0.0169  704 HOH   A O   
7031 O  O   . HOH   G .   ? 0.5949 0.7017 0.6824 0.1280  -0.1223 0.0406  705 HOH   A O   
7032 O  O   B HOH   G .   ? 0.2267 0.1585 0.3272 -0.0057 -0.0879 0.0032  706 HOH   A O   
7033 O  O   . HOH   G .   ? 0.4992 0.3085 0.4624 0.0246  0.2442  0.0493  707 HOH   A O   
7034 O  O   . HOH   G .   ? 0.2353 0.3698 0.3694 0.0618  -0.0505 0.0633  708 HOH   A O   
7035 O  O   . HOH   G .   ? 0.4007 0.9484 0.5267 -0.0684 -0.0098 0.2597  709 HOH   A O   
7036 O  O   . HOH   G .   ? 0.6558 0.2584 0.3788 -0.0616 0.0396  0.0207  710 HOH   A O   
7037 O  O   . HOH   G .   ? 0.3223 0.4221 0.4753 0.0816  -0.0629 -0.0458 711 HOH   A O   
7038 O  O   . HOH   G .   ? 0.3113 0.4469 0.3411 0.0140  -0.0541 -0.0814 712 HOH   A O   
7039 O  O   . HOH   G .   ? 0.6054 0.8523 0.5641 0.1194  -0.0516 0.1975  713 HOH   A O   
7040 O  O   . HOH   G .   ? 0.5978 0.2970 0.5656 0.0103  -0.1311 0.1640  714 HOH   A O   
7041 O  O   B HOH   G .   ? 0.2544 0.2046 0.2933 -0.0050 -0.0901 -0.0195 715 HOH   A O   
7042 O  O   . HOH   G .   ? 0.3328 0.2552 0.4702 0.0043  0.0247  0.0484  716 HOH   A O   
7043 O  O   . HOH   G .   ? 0.5607 0.7391 0.6005 0.3258  -0.0251 0.1656  717 HOH   A O   
7044 O  O   . HOH   G .   ? 0.6966 0.6960 0.5249 -0.1020 -0.1351 -0.1341 718 HOH   A O   
7045 O  O   A HOH   G .   ? 0.2793 0.7365 0.3048 0.1728  0.0259  -0.0668 719 HOH   A O   
7046 O  O   . HOH   G .   ? 0.2931 0.7377 0.4812 0.0695  0.0673  -0.1095 720 HOH   A O   
7047 O  O   . HOH   G .   ? 0.5817 0.6646 0.4762 -0.0511 -0.0555 0.0972  721 HOH   A O   
7048 O  O   . HOH   G .   ? 0.5032 0.5219 0.5171 0.1020  0.0597  0.1620  722 HOH   A O   
7049 O  O   B HOH   G .   ? 0.4922 0.4010 0.2189 -0.0209 -0.0885 -0.0582 723 HOH   A O   
7050 O  O   . HOH   G .   ? 0.2538 0.5172 0.5944 0.0012  -0.0424 0.3096  724 HOH   A O   
7051 O  O   . HOH   H .   ? 0.2353 0.2086 0.3312 0.0160  0.0734  0.0099  201 HOH   B O   
7052 O  O   . HOH   H .   ? 0.3425 0.3191 0.6849 0.0037  -0.0097 -0.0451 202 HOH   B O   
7053 O  O   . HOH   H .   ? 0.7628 0.3470 0.4056 0.0767  0.0325  -0.0238 203 HOH   B O   
7054 O  O   . HOH   H .   ? 0.5390 0.3601 0.4113 -0.0259 0.0145  -0.1779 204 HOH   B O   
7055 O  O   . HOH   H .   ? 0.3231 0.2493 0.5894 -0.0158 0.2024  0.0434  205 HOH   B O   
7056 O  O   . HOH   H .   ? 0.3151 0.6337 0.5428 -0.0091 0.1918  -0.1487 206 HOH   B O   
7057 O  O   . HOH   H .   ? 0.2590 0.7137 0.4051 0.0100  0.0056  0.2648  207 HOH   B O   
7058 O  O   . HOH   H .   ? 0.3234 0.1915 0.5413 0.0091  0.1823  0.0651  208 HOH   B O   
7059 O  O   . HOH   H .   ? 0.1628 0.2159 0.3281 -0.0182 -0.0098 0.0118  209 HOH   B O   
7060 O  O   . HOH   H .   ? 0.1953 0.2253 0.3245 -0.0054 0.0303  -0.0421 210 HOH   B O   
7061 O  O   . HOH   H .   ? 0.4171 0.4785 0.3577 0.2014  -0.0171 0.0356  211 HOH   B O   
7062 O  O   . HOH   H .   ? 0.3245 0.3837 0.5022 -0.0751 0.0302  -0.1596 212 HOH   B O   
7063 O  O   . HOH   H .   ? 0.3093 0.3840 0.3188 -0.0738 -0.0012 -0.1190 213 HOH   B O   
7064 O  O   . HOH   H .   ? 0.2731 0.2766 0.6594 0.0572  -0.1079 0.0386  214 HOH   B O   
7065 O  O   . HOH   H .   ? 0.5085 0.6061 0.4665 0.3055  -0.0975 0.0169  215 HOH   B O   
7066 O  O   . HOH   H .   ? 0.4004 0.3701 0.3583 -0.0212 -0.1374 0.0505  216 HOH   B O   
7067 O  O   . HOH   H .   ? 0.5813 0.6415 0.5676 0.2038  0.0696  0.0169  217 HOH   B O   
7068 O  O   . HOH   H .   ? 0.4064 0.5033 0.6479 0.2468  0.0609  -0.0763 218 HOH   B O   
7069 O  O   . HOH   H .   ? 0.3245 0.2823 0.4086 0.0564  -0.0926 -0.0565 219 HOH   B O   
7070 O  O   . HOH   H .   ? 0.1605 0.1572 0.2510 -0.0226 0.0091  0.0049  220 HOH   B O   
7071 O  O   . HOH   H .   ? 0.4128 0.3817 0.6582 -0.0048 -0.1650 -0.1046 221 HOH   B O   
7072 O  O   . HOH   H .   ? 0.2325 0.2250 0.4051 -0.0285 0.0041  -0.0502 222 HOH   B O   
7073 O  O   . HOH   H .   ? 0.5760 0.2855 0.4509 -0.1638 -0.0087 0.0343  223 HOH   B O   
7074 O  O   . HOH   H .   ? 0.1864 0.2262 0.3779 -0.0202 0.0232  -0.0287 224 HOH   B O   
7075 O  O   . HOH   H .   ? 0.5396 0.7084 0.3962 0.2726  0.0899  0.0911  225 HOH   B O   
7076 O  O   . HOH   H .   ? 0.2418 0.1813 0.2729 -0.0255 0.1013  -0.0041 226 HOH   B O   
7077 O  O   . HOH   H .   ? 0.4944 0.4403 0.4298 0.0304  0.1101  -0.1830 227 HOH   B O   
7078 O  O   . HOH   H .   ? 0.2522 0.3152 0.3533 -0.0971 0.0276  -0.0160 228 HOH   B O   
7079 O  O   . HOH   H .   ? 0.2586 0.2284 0.2812 0.0897  -0.0977 -0.0765 229 HOH   B O   
7080 O  O   . HOH   H .   ? 0.5351 0.4102 0.6496 0.0639  -0.0574 0.2753  230 HOH   B O   
7081 O  O   . HOH   H .   ? 0.3903 0.3230 0.2533 0.0376  0.0637  0.0518  231 HOH   B O   
7082 O  O   . HOH   H .   ? 0.6803 0.6560 0.3679 -0.0008 -0.0224 0.1283  232 HOH   B O   
7083 O  O   . HOH   H .   ? 0.2084 0.1346 0.3592 0.0162  -0.0600 -0.0105 233 HOH   B O   
7084 O  O   . HOH   H .   ? 0.5373 0.2213 0.2978 0.0082  -0.1067 -0.0045 234 HOH   B O   
7085 O  O   . HOH   H .   ? 0.6100 0.3265 0.3804 -0.2409 0.0090  0.0163  235 HOH   B O   
7086 O  O   . HOH   H .   ? 0.2138 0.2061 0.3774 0.0093  -0.0565 -0.0523 236 HOH   B O   
7087 O  O   . HOH   H .   ? 0.2565 0.5457 0.5813 0.1605  -0.0336 -0.0668 237 HOH   B O   
7088 O  O   . HOH   H .   ? 0.3088 0.1806 0.6454 -0.0192 -0.1180 -0.0231 238 HOH   B O   
7089 O  O   . HOH   H .   ? 0.1596 0.1475 0.1454 -0.0080 -0.0057 -0.0040 239 HOH   B O   
7090 O  O   . HOH   H .   ? 0.7327 0.5809 0.4841 0.2473  -0.0481 -0.1383 240 HOH   B O   
7091 O  O   . HOH   H .   ? 0.3460 0.1891 0.1938 0.0287  -0.0760 -0.0116 241 HOH   B O   
7092 O  O   . HOH   H .   ? 0.3513 0.2891 0.4206 0.0790  -0.0628 -0.0710 242 HOH   B O   
7093 O  O   . HOH   H .   ? 0.2651 0.2265 0.2974 0.0648  0.0593  -0.0079 243 HOH   B O   
7094 O  O   . HOH   H .   ? 0.3524 0.2655 0.4174 0.0405  -0.0835 -0.1366 244 HOH   B O   
7095 O  O   . HOH   H .   ? 0.1871 0.1523 0.3357 -0.0079 -0.0180 -0.0140 245 HOH   B O   
7096 O  O   . HOH   H .   ? 0.2627 0.2745 0.3476 0.0304  0.0368  -0.0925 246 HOH   B O   
7097 O  O   . HOH   H .   ? 0.2948 0.3519 0.2856 -0.0771 0.0231  -0.0496 247 HOH   B O   
7098 O  O   . HOH   H .   ? 0.2377 0.3901 0.3401 -0.0538 -0.0783 -0.0504 248 HOH   B O   
7099 O  O   . HOH   H .   ? 0.6463 0.4508 0.3169 -0.1055 -0.0088 0.0239  249 HOH   B O   
7100 O  O   . HOH   H .   ? 0.4634 0.3941 0.3177 0.0610  0.0118  -0.0499 250 HOH   B O   
7101 O  O   . HOH   H .   ? 0.2490 0.3433 0.2611 -0.0286 -0.0193 0.0421  251 HOH   B O   
7102 O  O   . HOH   H .   ? 0.1644 0.1358 0.1604 0.0019  -0.0074 0.0047  252 HOH   B O   
7103 O  O   . HOH   H .   ? 0.4049 0.3978 0.5582 -0.1608 0.0251  0.0564  253 HOH   B O   
7104 O  O   . HOH   H .   ? 0.1560 0.1587 0.2846 -0.0030 -0.0021 -0.0101 254 HOH   B O   
7105 O  O   . HOH   H .   ? 0.2258 0.1965 0.2138 -0.0306 -0.0431 0.0275  255 HOH   B O   
7106 O  O   . HOH   H .   ? 0.3548 0.4095 0.2561 -0.0048 0.0915  0.0185  256 HOH   B O   
7107 O  O   . HOH   H .   ? 0.3290 0.2143 0.2222 0.0205  -0.0383 -0.0176 257 HOH   B O   
7108 O  O   . HOH   H .   ? 0.2101 0.1648 0.2240 -0.0292 -0.0472 0.0288  258 HOH   B O   
7109 O  O   . HOH   H .   ? 0.1645 0.1761 0.3258 -0.0268 -0.0095 0.0157  259 HOH   B O   
7110 O  O   . HOH   H .   ? 0.2390 0.3136 0.2238 -0.0646 0.0298  0.0483  260 HOH   B O   
7111 O  O   . HOH   H .   ? 0.5361 0.7026 0.2959 -0.0817 -0.0880 -0.0112 261 HOH   B O   
7112 O  O   . HOH   H .   ? 0.1427 0.1703 0.2399 -0.0091 0.0011  0.0124  262 HOH   B O   
7113 O  O   . HOH   H .   ? 0.2574 0.2795 0.2679 -0.0375 -0.0825 0.0301  263 HOH   B O   
7114 O  O   . HOH   H .   ? 0.2881 0.4227 0.2799 -0.1055 -0.0420 -0.0252 264 HOH   B O   
7115 O  O   . HOH   H .   ? 0.1879 0.2739 0.2832 0.0338  0.0457  0.0891  265 HOH   B O   
7116 O  O   . HOH   H .   ? 0.3546 0.3153 0.3149 -0.0478 0.0313  -0.0671 266 HOH   B O   
7117 O  O   . HOH   H .   ? 0.2258 0.5097 0.5048 -0.0178 -0.0134 -0.1395 267 HOH   B O   
7118 O  O   . HOH   H .   ? 0.2407 0.2558 0.2146 0.0066  -0.0030 0.0052  268 HOH   B O   
7119 O  O   . HOH   H .   ? 0.4913 0.3284 0.4218 -0.0736 0.0689  -0.0208 269 HOH   B O   
7120 O  O   . HOH   H .   ? 0.3297 0.4770 0.3491 -0.0219 -0.0846 0.0895  270 HOH   B O   
7121 O  O   . HOH   H .   ? 0.3538 0.3644 0.4448 0.1208  -0.0374 -0.0875 271 HOH   B O   
7122 O  O   . HOH   H .   ? 0.3151 0.4625 0.6454 -0.0718 0.0222  -0.1371 272 HOH   B O   
7123 O  O   . HOH   H .   ? 0.1967 0.1874 0.1777 -0.0479 -0.0525 0.0206  273 HOH   B O   
7124 O  O   . HOH   H .   ? 0.3027 0.1995 0.5372 0.0157  0.0649  0.0567  274 HOH   B O   
7125 O  O   . HOH   H .   ? 0.1999 0.1692 0.2399 -0.0249 -0.0163 0.0116  275 HOH   B O   
7126 O  O   . HOH   H .   ? 0.4840 0.3843 0.4435 -0.1498 0.0881  -0.1473 276 HOH   B O   
7127 O  O   . HOH   H .   ? 0.4785 0.5251 0.4585 0.0279  -0.1462 0.0582  277 HOH   B O   
7128 O  O   . HOH   H .   ? 0.5099 0.5827 0.5149 0.2442  -0.0438 0.0795  278 HOH   B O   
7129 O  O   . HOH   H .   ? 0.2630 0.3910 0.3921 0.0208  0.1046  0.0077  279 HOH   B O   
7130 O  O   . HOH   H .   ? 0.4011 0.2781 0.4201 -0.0528 -0.0671 -0.0232 280 HOH   B O   
7131 O  O   . HOH   H .   ? 0.3045 0.7660 0.7724 0.1894  -0.0632 -0.1235 281 HOH   B O   
7132 O  O   . HOH   H .   ? 0.4314 0.5249 0.6432 0.0557  0.1079  -0.0230 282 HOH   B O   
7133 O  O   . HOH   H .   ? 0.2329 0.2553 0.2226 -0.0390 -0.0654 -0.0367 283 HOH   B O   
7134 O  O   . HOH   H .   ? 0.2659 0.1977 0.2970 -0.0611 0.0231  -0.0191 284 HOH   B O   
7135 O  O   . HOH   H .   ? 0.2527 0.3190 0.2710 0.0993  -0.0441 -0.0358 285 HOH   B O   
7136 O  O   . HOH   H .   ? 0.1839 0.1611 0.1904 0.0059  0.0136  -0.0005 286 HOH   B O   
7137 O  O   . HOH   H .   ? 0.2220 0.2423 0.5681 -0.0401 0.0100  0.1514  287 HOH   B O   
7138 O  O   . HOH   H .   ? 0.2370 0.3257 0.3154 -0.0214 0.0239  -0.1000 288 HOH   B O   
7139 O  O   . HOH   H .   ? 0.1710 0.1629 0.3668 -0.0132 0.0084  -0.0171 289 HOH   B O   
7140 O  O   . HOH   H .   ? 0.8332 0.7298 0.3909 0.0106  -0.0440 0.1144  290 HOH   B O   
7141 O  O   . HOH   H .   ? 0.3157 0.4831 0.5127 -0.1204 -0.1239 0.0575  291 HOH   B O   
7142 O  O   . HOH   H .   ? 0.5882 0.3974 0.3817 0.2632  0.1533  0.1138  292 HOH   B O   
7143 O  O   . HOH   H .   ? 0.4113 0.2708 0.2173 0.0532  -0.0769 -0.0184 293 HOH   B O   
7144 O  O   . HOH   H .   ? 0.2541 0.2666 0.3425 -0.0080 -0.0839 0.0470  294 HOH   B O   
7145 O  O   . HOH   H .   ? 0.1679 0.2201 0.1665 -0.0122 -0.0140 0.0093  295 HOH   B O   
7146 O  O   . HOH   H .   ? 0.1935 0.2175 0.3383 0.0250  0.0133  0.0181  296 HOH   B O   
7147 O  O   . HOH   H .   ? 0.4151 0.4003 0.2589 0.1076  -0.0822 0.0412  297 HOH   B O   
7148 O  O   . HOH   H .   ? 0.1856 0.3778 0.4765 0.0372  -0.0001 -0.1569 298 HOH   B O   
7149 O  O   . HOH   H .   ? 0.3940 0.2297 0.4447 -0.1045 -0.2026 0.0758  299 HOH   B O   
7150 O  O   . HOH   H .   ? 0.3525 0.3336 0.3085 -0.0428 0.0424  -0.1620 300 HOH   B O   
7151 O  O   . HOH   H .   ? 0.2776 0.6723 0.2397 0.0921  -0.0348 -0.0915 301 HOH   B O   
7152 O  O   . HOH   H .   ? 0.2010 0.1671 0.2605 0.0139  0.0029  0.0160  302 HOH   B O   
7153 O  O   . HOH   H .   ? 0.6112 0.2784 0.3619 0.0619  -0.0116 0.0970  303 HOH   B O   
7154 O  O   . HOH   H .   ? 0.3499 0.4911 0.4279 -0.1744 0.1250  -0.0693 304 HOH   B O   
7155 O  O   . HOH   H .   ? 0.1620 0.1562 0.3258 0.0113  0.0019  -0.0013 305 HOH   B O   
7156 O  O   . HOH   H .   ? 0.2883 0.3160 0.3771 -0.0448 0.1223  -0.0998 306 HOH   B O   
7157 O  O   . HOH   H .   ? 0.3436 0.2001 0.3744 0.0705  0.1291  0.0700  307 HOH   B O   
7158 O  O   . HOH   H .   ? 0.2125 0.3464 0.6184 0.0733  -0.0702 -0.1725 308 HOH   B O   
7159 O  O   . HOH   H .   ? 0.2144 0.1692 0.3270 0.0325  -0.0865 0.0065  309 HOH   B O   
7160 O  O   . HOH   H .   ? 0.2048 0.2908 0.5358 -0.0028 -0.0714 -0.0187 310 HOH   B O   
7161 O  O   . HOH   H .   ? 0.5269 0.3356 0.4191 -0.0758 0.0454  0.0933  311 HOH   B O   
7162 O  O   . HOH   H .   ? 0.1772 0.2676 0.2321 -0.0130 -0.0157 0.0564  312 HOH   B O   
7163 O  O   . HOH   H .   ? 0.2238 0.1745 0.2788 -0.0309 -0.0218 -0.0081 313 HOH   B O   
7164 O  O   . HOH   H .   ? 0.2298 0.2022 0.2018 -0.0039 0.0203  0.0250  314 HOH   B O   
7165 O  O   . HOH   H .   ? 0.4976 0.4639 0.2727 0.0017  -0.0323 -0.0594 315 HOH   B O   
7166 O  O   . HOH   H .   ? 0.4455 0.5582 0.2573 0.0094  0.1008  0.1388  316 HOH   B O   
7167 O  O   . HOH   H .   ? 0.2631 0.1621 0.2833 -0.0238 -0.0282 0.0317  317 HOH   B O   
7168 O  O   . HOH   H .   ? 0.4797 0.2998 0.2198 -0.1796 0.0481  -0.0147 318 HOH   B O   
7169 O  O   . HOH   H .   ? 0.6559 0.4764 0.5518 0.1337  0.2007  0.0334  319 HOH   B O   
7170 O  O   . HOH   H .   ? 0.2160 0.3164 0.3465 0.0778  -0.0355 -0.0904 320 HOH   B O   
7171 O  O   . HOH   H .   ? 0.1719 0.1932 0.3325 -0.0376 -0.0194 0.0003  321 HOH   B O   
7172 O  O   . HOH   H .   ? 0.4124 0.2186 0.2889 0.1318  0.0870  0.0262  322 HOH   B O   
7173 O  O   . HOH   H .   ? 0.2362 0.5082 0.4079 -0.0941 -0.0021 -0.0745 323 HOH   B O   
7174 O  O   . HOH   H .   ? 0.3655 0.3033 0.5682 -0.0253 -0.0965 0.1496  324 HOH   B O   
7175 O  O   . HOH   H .   ? 0.1665 0.1687 0.3149 -0.0170 -0.0113 -0.0131 325 HOH   B O   
7176 O  O   . HOH   H .   ? 0.4419 0.4764 0.2322 0.1153  -0.0602 -0.0227 326 HOH   B O   
7177 O  O   . HOH   H .   ? 0.4761 0.6563 0.4621 0.0530  -0.1232 0.1102  327 HOH   B O   
7178 O  O   . HOH   H .   ? 0.5572 0.3995 0.4686 -0.0083 0.0941  -0.1609 328 HOH   B O   
7179 O  O   . HOH   H .   ? 0.3480 0.2295 0.2537 0.0435  -0.0370 0.0115  329 HOH   B O   
7180 O  O   . HOH   H .   ? 0.2949 0.2103 0.4094 0.0005  0.0007  0.0507  330 HOH   B O   
7181 O  O   . HOH   H .   ? 0.4952 0.4041 0.5235 0.0685  0.0068  0.0579  331 HOH   B O   
7182 O  O   . HOH   H .   ? 0.6391 0.5102 0.6960 0.2024  -0.0486 0.1774  332 HOH   B O   
7183 O  O   . HOH   H .   ? 0.1909 0.1885 0.2855 0.0242  0.0363  0.0163  333 HOH   B O   
7184 O  O   . HOH   H .   ? 0.3739 0.4702 0.9334 -0.0282 -0.0980 0.2454  334 HOH   B O   
7185 O  O   . HOH   H .   ? 0.5722 0.4103 0.4365 0.1070  0.1532  0.2000  335 HOH   B O   
7186 O  O   . HOH   H .   ? 0.2829 0.3379 0.5876 -0.0569 -0.1777 0.1850  336 HOH   B O   
7187 O  O   . HOH   H .   ? 0.2400 0.1906 0.4024 0.0172  -0.0732 -0.0334 337 HOH   B O   
7188 O  O   . HOH   H .   ? 0.8659 0.2294 0.3613 0.0629  -0.1030 -0.0147 338 HOH   B O   
7189 O  O   . HOH   H .   ? 0.4593 0.3124 0.5869 0.1348  0.2318  0.1869  339 HOH   B O   
7190 O  O   . HOH   H .   ? 0.1846 0.1512 0.2553 0.0060  -0.0164 0.0116  340 HOH   B O   
7191 O  O   . HOH   H .   ? 0.4464 0.7339 0.4565 -0.1103 -0.1037 0.2257  341 HOH   B O   
7192 O  O   . HOH   H .   ? 0.5750 0.4679 0.5369 -0.1034 -0.1182 -0.1262 342 HOH   B O   
7193 O  O   . HOH   H .   ? 0.4691 0.3841 0.3698 0.0643  -0.1161 -0.0966 343 HOH   B O   
7194 O  O   . HOH   H .   ? 0.5947 0.5689 0.5583 -0.1166 -0.0914 0.1167  344 HOH   B O   
7195 O  O   . HOH   H .   ? 0.3907 0.5480 0.4514 -0.1386 -0.0570 -0.0643 345 HOH   B O   
7196 O  O   . HOH   H .   ? 0.4473 0.4733 0.7603 -0.0981 -0.0438 0.0375  346 HOH   B O   
7197 O  O   . HOH   H .   ? 0.2283 0.2015 0.3622 -0.0024 0.0835  -0.0135 347 HOH   B O   
7198 O  O   . HOH   H .   ? 0.5056 0.6044 0.6606 -0.1242 0.0388  0.1669  348 HOH   B O   
7199 O  O   . HOH   H .   ? 0.5867 0.5864 0.3654 -0.0635 -0.1316 0.0329  349 HOH   B O   
7200 O  O   . HOH   H .   ? 0.2395 0.6309 0.3328 0.1529  -0.0611 -0.1435 350 HOH   B O   
7201 O  O   . HOH   H .   ? 0.3715 0.4411 0.5536 -0.1713 0.0467  -0.0452 351 HOH   B O   
7202 O  O   . HOH   H .   ? 0.4487 0.6988 0.6077 -0.0014 -0.1119 0.0789  352 HOH   B O   
7203 O  O   . HOH   H .   ? 0.3206 0.2447 0.4699 -0.0294 -0.0958 -0.0627 353 HOH   B O   
7204 O  O   . HOH   H .   ? 0.2487 0.4943 0.4934 0.0521  0.0214  0.0193  354 HOH   B O   
7205 O  O   . HOH   H .   ? 0.5031 0.5752 0.4914 0.1875  -0.1029 0.1610  355 HOH   B O   
7206 O  O   . HOH   H .   ? 0.4816 0.2758 0.5557 -0.0789 0.1223  0.0384  356 HOH   B O   
7207 O  O   . HOH   H .   ? 0.5069 0.6039 0.6879 0.0563  0.0279  -0.0808 357 HOH   B O   
7208 O  O   . HOH   H .   ? 0.3776 0.2218 0.3209 -0.0731 0.0353  -0.0664 358 HOH   B O   
7209 O  O   . HOH   H .   ? 0.3564 0.2509 0.3591 -0.0582 -0.0169 -0.0597 359 HOH   B O   
7210 O  O   . HOH   H .   ? 0.4739 0.4786 0.6381 0.0061  0.0595  0.1705  360 HOH   B O   
7211 O  O   . HOH   H .   ? 0.5213 0.3379 0.4814 0.0148  0.1493  -0.0487 361 HOH   B O   
7212 O  O   . HOH   H .   ? 0.5419 0.3432 0.5213 -0.0002 -0.1828 -0.0634 362 HOH   B O   
7213 O  O   . HOH   H .   ? 0.4042 0.6607 0.3605 0.2167  0.0017  0.0289  363 HOH   B O   
7214 O  O   . HOH   H .   ? 0.2290 0.4105 0.6889 -0.0785 -0.0745 -0.0860 364 HOH   B O   
7215 O  O   . HOH   H .   ? 0.6487 0.2567 0.3422 -0.0320 0.0104  0.0661  365 HOH   B O   
7216 O  O   . HOH   H .   ? 0.5766 0.4864 0.5719 0.0292  0.0808  0.0404  366 HOH   B O   
7217 O  O   . HOH   H .   ? 0.5385 0.5717 0.5421 -0.0569 -0.0129 -0.1145 367 HOH   B O   
7218 O  O   . HOH   H .   ? 0.3619 0.3731 0.4905 0.0699  -0.1588 -0.0241 368 HOH   B O   
7219 O  O   . HOH   H .   ? 0.6703 0.5105 0.4484 0.1733  0.0751  0.0854  369 HOH   B O   
7220 O  O   . HOH   H .   ? 0.5053 0.3179 0.5588 -0.1386 -0.0344 0.0076  370 HOH   B O   
7221 O  O   . HOH   H .   ? 0.3902 0.5920 0.5280 0.2376  0.0936  0.1736  371 HOH   B O   
7222 O  O   . HOH   H .   ? 0.4900 0.6010 0.3340 0.1432  -0.1346 0.0395  372 HOH   B O   
7223 O  O   . HOH   H .   ? 0.3988 0.6882 0.5869 0.0543  0.0049  -0.0335 373 HOH   B O   
7224 O  O   . HOH   H .   ? 0.3678 0.3714 0.3599 0.0982  -0.1050 -0.0440 374 HOH   B O   
7225 O  O   . HOH   H .   ? 0.7778 0.7345 0.6076 0.2265  -0.1062 0.0313  375 HOH   B O   
7226 O  O   . HOH   H .   ? 0.6588 0.4048 0.3155 -0.0485 -0.1161 -0.0629 376 HOH   B O   
7227 O  O   . HOH   H .   ? 0.4052 0.4577 0.5030 -0.0426 -0.0650 -0.0251 377 HOH   B O   
7228 O  O   . HOH   H .   ? 0.3673 0.5249 0.2463 0.0405  0.0138  -0.0036 378 HOH   B O   
7229 O  O   . HOH   H .   ? 0.2449 0.4601 0.3929 -0.0115 -0.0178 -0.0871 379 HOH   B O   
7230 O  O   . HOH   H .   ? 0.5732 0.7837 0.4273 -0.1470 0.0453  -0.1591 380 HOH   B O   
7231 O  O   . HOH   H .   ? 0.4634 0.6976 0.6241 0.1040  0.0134  0.2670  381 HOH   B O   
7232 O  O   . HOH   H .   ? 0.6175 0.7225 0.6977 -0.0381 0.2914  0.1246  382 HOH   B O   
7233 O  O   . HOH   H .   ? 0.6877 0.3542 0.5789 -0.1191 -0.0713 -0.0176 383 HOH   B O   
7234 O  O   . HOH   H .   ? 0.3870 0.8822 0.5691 0.1359  0.1269  0.0624  384 HOH   B O   
7235 O  O   . HOH   H .   ? 0.6937 0.3710 0.4276 0.0267  0.0813  -0.0950 385 HOH   B O   
7236 O  O   . HOH   H .   ? 0.2823 0.2765 0.3155 0.0076  0.0029  0.0133  386 HOH   B O   
7237 O  O   . HOH   H .   ? 0.8116 0.5927 0.4849 0.2383  0.1021  0.0003  387 HOH   B O   
7238 O  O   . HOH   H .   ? 0.2456 0.4446 0.4380 -0.0690 -0.1115 -0.0163 388 HOH   B O   
7239 O  O   . HOH   H .   ? 0.4993 0.4532 0.3783 0.0000  0.1049  -0.0254 389 HOH   B O   
7240 O  O   . HOH   H .   ? 0.6090 0.4949 0.6084 -0.0844 0.0589  -0.0221 390 HOH   B O   
7241 O  O   . HOH   H .   ? 0.5903 0.5313 0.5602 0.0823  0.1420  0.0480  391 HOH   B O   
7242 O  O   . HOH   H .   ? 0.4882 0.3950 0.5499 -0.2048 -0.0009 0.1145  392 HOH   B O   
7243 O  O   . HOH   H .   ? 0.4371 0.2445 0.3468 0.0705  -0.0551 0.0196  393 HOH   B O   
7244 O  O   . HOH   H .   ? 0.3723 0.2192 0.4827 -0.0410 0.0072  0.0592  394 HOH   B O   
7245 O  O   . HOH   H .   ? 0.2484 0.4840 0.7238 -0.1169 -0.0816 -0.0410 395 HOH   B O   
7246 O  O   . HOH   H .   ? 0.4548 0.6255 0.4414 0.0970  -0.0078 -0.1321 396 HOH   B O   
7247 O  O   . HOH   H .   ? 0.2118 0.3000 0.5869 -0.0674 -0.0680 0.0301  397 HOH   B O   
7248 O  O   . HOH   H .   ? 0.3275 0.4496 0.4011 0.0259  0.0267  -0.0946 398 HOH   B O   
7249 O  O   . HOH   H .   ? 0.4737 0.4807 0.4786 0.1103  0.1002  0.0674  399 HOH   B O   
7250 O  O   . HOH   H .   ? 0.5099 0.5542 0.6356 0.0560  -0.1505 0.2305  400 HOH   B O   
7251 O  O   . HOH   H .   ? 0.5192 0.3978 0.3284 -0.2083 -0.0530 0.0970  401 HOH   B O   
7252 O  O   . HOH   H .   ? 0.6352 0.5344 0.4005 0.1847  -0.0350 -0.0323 402 HOH   B O   
# 
