data_7HEJ
# 
_entry.id   7HEJ 
# 
_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   7HEJ         pdb_00007hej 10.2210/pdb7hej/pdb 
WWPDB D_1001407373 ?            ?                   
# 
_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                        7HEJ 
_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 'trifluoroacetic acid'                                                           114.023   1   ? ? ? ? 
3 non-polymer syn '(2S)-2-[(3R)-oxolan-3-yl]-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]ethan-1-ol' 248.281   1   ? ? ? ? 
4 non-polymer syn 'CHLORIDE ION'                                                                   35.453    1   ? ? ? ? 
5 water       nat water                                                                            18.015    425 ? ? ? ? 
# 
_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 'trifluoroacetic acid'                                                           TFA   
3 '(2S)-2-[(3R)-oxolan-3-yl]-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]ethan-1-ol' A1A9W 
4 'CHLORIDE ION'                                                                   CL    
5 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 
A1A9W non-polymer         . '(2S)-2-[(3R)-oxolan-3-yl]-2-[(7H-pyrrolo[2,3-d]pyrimidin-4-yl)amino]ethan-1-ol' ? 'C12 H16 N4 O2'  
248.281 
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 
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 
TFA   non-polymer         . 'trifluoroacetic acid'                                                           ? 'C2 H F3 O2'     
114.023 
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 TFA   1   201 201  TFA   TFA A . 
D 3 A1A9W 1   202 201  A1A9W LA1 A . 
E 4 CL    1   203 1    CL    CL  A . 
F 5 HOH   1   301 292  HOH   HOH A . 
F 5 HOH   2   302 196  HOH   HOH A . 
F 5 HOH   3   303 153  HOH   HOH A . 
F 5 HOH   4   304 1289 HOH   HOH A . 
F 5 HOH   5   305 1313 HOH   HOH A . 
F 5 HOH   6   306 1286 HOH   HOH A . 
F 5 HOH   7   307 229  HOH   HOH A . 
F 5 HOH   8   308 1301 HOH   HOH A . 
F 5 HOH   9   309 493  HOH   HOH A . 
F 5 HOH   10  310 625  HOH   HOH A . 
F 5 HOH   11  311 6    HOH   HOH A . 
F 5 HOH   12  312 281  HOH   HOH A . 
F 5 HOH   13  313 18   HOH   HOH A . 
F 5 HOH   14  314 86   HOH   HOH A . 
F 5 HOH   15  315 247  HOH   HOH A . 
F 5 HOH   16  316 9    HOH   HOH A . 
F 5 HOH   17  317 209  HOH   HOH A . 
F 5 HOH   18  318 136  HOH   HOH A . 
F 5 HOH   19  319 109  HOH   HOH A . 
F 5 HOH   20  320 76   HOH   HOH A . 
F 5 HOH   21  321 1275 HOH   HOH A . 
F 5 HOH   22  322 14   HOH   HOH A . 
F 5 HOH   23  323 405  HOH   HOH A . 
F 5 HOH   24  324 1290 HOH   HOH A . 
F 5 HOH   25  325 661  HOH   HOH A . 
F 5 HOH   26  326 124  HOH   HOH A . 
F 5 HOH   27  327 278  HOH   HOH A . 
F 5 HOH   28  328 192  HOH   HOH A . 
F 5 HOH   29  329 1    HOH   HOH A . 
F 5 HOH   30  330 1283 HOH   HOH A . 
F 5 HOH   31  331 236  HOH   HOH A . 
F 5 HOH   32  332 1295 HOH   HOH A . 
F 5 HOH   33  333 15   HOH   HOH A . 
F 5 HOH   34  334 105  HOH   HOH A . 
F 5 HOH   35  335 469  HOH   HOH A . 
F 5 HOH   36  336 15   HOH   HOH A . 
F 5 HOH   37  337 630  HOH   HOH A . 
F 5 HOH   38  338 296  HOH   HOH A . 
F 5 HOH   39  339 57   HOH   HOH A . 
F 5 HOH   40  340 1300 HOH   HOH A . 
F 5 HOH   41  341 225  HOH   HOH A . 
F 5 HOH   42  342 140  HOH   HOH A . 
F 5 HOH   43  343 164  HOH   HOH A . 
F 5 HOH   44  344 320  HOH   HOH A . 
F 5 HOH   45  345 337  HOH   HOH A . 
F 5 HOH   46  346 165  HOH   HOH A . 
F 5 HOH   47  347 8    HOH   HOH A . 
F 5 HOH   48  348 21   HOH   HOH A . 
F 5 HOH   49  349 151  HOH   HOH A . 
F 5 HOH   50  350 155  HOH   HOH A . 
F 5 HOH   51  351 241  HOH   HOH A . 
F 5 HOH   52  352 964  HOH   HOH A . 
F 5 HOH   53  353 39   HOH   HOH A . 
F 5 HOH   54  354 169  HOH   HOH A . 
F 5 HOH   55  355 33   HOH   HOH A . 
F 5 HOH   56  356 42   HOH   HOH A . 
F 5 HOH   57  357 92   HOH   HOH A . 
F 5 HOH   58  358 36   HOH   HOH A . 
F 5 HOH   59  359 354  HOH   HOH A . 
F 5 HOH   60  360 93   HOH   HOH A . 
F 5 HOH   61  361 393  HOH   HOH A . 
F 5 HOH   62  362 939  HOH   HOH A . 
F 5 HOH   63  363 662  HOH   HOH A . 
F 5 HOH   64  364 66   HOH   HOH A . 
F 5 HOH   65  365 2    HOH   HOH A . 
F 5 HOH   66  366 102  HOH   HOH A . 
F 5 HOH   67  367 396  HOH   HOH A . 
F 5 HOH   68  368 409  HOH   HOH A . 
F 5 HOH   69  369 26   HOH   HOH A . 
F 5 HOH   70  370 5    HOH   HOH A . 
F 5 HOH   71  371 49   HOH   HOH A . 
F 5 HOH   72  372 1094 HOH   HOH A . 
F 5 HOH   73  373 24   HOH   HOH A . 
F 5 HOH   74  374 138  HOH   HOH A . 
F 5 HOH   75  375 19   HOH   HOH A . 
F 5 HOH   76  376 162  HOH   HOH A . 
F 5 HOH   77  377 218  HOH   HOH A . 
F 5 HOH   78  378 81   HOH   HOH A . 
F 5 HOH   79  379 139  HOH   HOH A . 
F 5 HOH   80  380 16   HOH   HOH A . 
F 5 HOH   81  381 45   HOH   HOH A . 
F 5 HOH   82  382 159  HOH   HOH A . 
F 5 HOH   83  383 56   HOH   HOH A . 
F 5 HOH   84  384 1308 HOH   HOH A . 
F 5 HOH   85  385 4    HOH   HOH A . 
F 5 HOH   86  386 62   HOH   HOH A . 
F 5 HOH   87  387 148  HOH   HOH A . 
F 5 HOH   88  388 140  HOH   HOH A . 
F 5 HOH   89  389 46   HOH   HOH A . 
F 5 HOH   90  390 186  HOH   HOH A . 
F 5 HOH   91  391 134  HOH   HOH A . 
F 5 HOH   92  392 27   HOH   HOH A . 
F 5 HOH   93  393 1310 HOH   HOH A . 
F 5 HOH   94  394 366  HOH   HOH A . 
F 5 HOH   95  395 199  HOH   HOH A . 
F 5 HOH   96  396 17   HOH   HOH A . 
F 5 HOH   97  397 154  HOH   HOH A . 
F 5 HOH   98  398 74   HOH   HOH A . 
F 5 HOH   99  399 35   HOH   HOH A . 
F 5 HOH   100 400 96   HOH   HOH A . 
F 5 HOH   101 401 461  HOH   HOH A . 
F 5 HOH   102 402 116  HOH   HOH A . 
F 5 HOH   103 403 5    HOH   HOH A . 
F 5 HOH   104 404 351  HOH   HOH A . 
F 5 HOH   105 405 34   HOH   HOH A . 
F 5 HOH   106 406 115  HOH   HOH A . 
F 5 HOH   107 407 12   HOH   HOH A . 
F 5 HOH   108 408 11   HOH   HOH A . 
F 5 HOH   109 409 85   HOH   HOH A . 
F 5 HOH   110 410 78   HOH   HOH A . 
F 5 HOH   111 411 12   HOH   HOH A . 
F 5 HOH   112 412 58   HOH   HOH A . 
F 5 HOH   113 413 83   HOH   HOH A . 
F 5 HOH   114 414 1315 HOH   HOH A . 
F 5 HOH   115 415 333  HOH   HOH A . 
F 5 HOH   116 416 195  HOH   HOH A . 
F 5 HOH   117 417 67   HOH   HOH A . 
F 5 HOH   118 418 25   HOH   HOH A . 
F 5 HOH   119 419 303  HOH   HOH A . 
F 5 HOH   120 420 68   HOH   HOH A . 
F 5 HOH   121 421 121  HOH   HOH A . 
F 5 HOH   122 422 381  HOH   HOH A . 
F 5 HOH   123 423 3    HOH   HOH A . 
F 5 HOH   124 424 123  HOH   HOH A . 
F 5 HOH   125 425 125  HOH   HOH A . 
F 5 HOH   126 426 1068 HOH   HOH A . 
F 5 HOH   127 427 6    HOH   HOH A . 
F 5 HOH   128 428 53   HOH   HOH A . 
F 5 HOH   129 429 1296 HOH   HOH A . 
F 5 HOH   130 430 122  HOH   HOH A . 
F 5 HOH   131 431 95   HOH   HOH A . 
F 5 HOH   132 432 156  HOH   HOH A . 
F 5 HOH   133 433 70   HOH   HOH A . 
F 5 HOH   134 434 51   HOH   HOH A . 
F 5 HOH   135 435 582  HOH   HOH A . 
F 5 HOH   136 436 397  HOH   HOH A . 
F 5 HOH   137 437 132  HOH   HOH A . 
F 5 HOH   138 438 7    HOH   HOH A . 
F 5 HOH   139 439 1222 HOH   HOH A . 
F 5 HOH   140 440 1279 HOH   HOH A . 
F 5 HOH   141 441 13   HOH   HOH A . 
F 5 HOH   142 442 1309 HOH   HOH A . 
F 5 HOH   143 443 1238 HOH   HOH A . 
F 5 HOH   144 444 71   HOH   HOH A . 
F 5 HOH   145 445 212  HOH   HOH A . 
F 5 HOH   146 446 80   HOH   HOH A . 
F 5 HOH   147 447 16   HOH   HOH A . 
F 5 HOH   148 448 952  HOH   HOH A . 
F 5 HOH   149 449 94   HOH   HOH A . 
F 5 HOH   150 450 79   HOH   HOH A . 
F 5 HOH   151 451 73   HOH   HOH A . 
F 5 HOH   152 452 944  HOH   HOH A . 
F 5 HOH   153 453 188  HOH   HOH A . 
F 5 HOH   154 454 97   HOH   HOH A . 
F 5 HOH   155 455 40   HOH   HOH A . 
F 5 HOH   156 456 576  HOH   HOH A . 
F 5 HOH   157 457 104  HOH   HOH A . 
F 5 HOH   158 458 1189 HOH   HOH A . 
F 5 HOH   159 459 1119 HOH   HOH A . 
F 5 HOH   160 460 330  HOH   HOH A . 
F 5 HOH   161 461 1134 HOH   HOH A . 
F 5 HOH   162 462 509  HOH   HOH A . 
F 5 HOH   163 463 107  HOH   HOH A . 
F 5 HOH   164 464 726  HOH   HOH A . 
F 5 HOH   165 465 163  HOH   HOH A . 
F 5 HOH   166 466 408  HOH   HOH A . 
F 5 HOH   167 467 319  HOH   HOH A . 
F 5 HOH   168 468 756  HOH   HOH A . 
F 5 HOH   169 469 63   HOH   HOH A . 
F 5 HOH   170 470 556  HOH   HOH A . 
F 5 HOH   171 471 126  HOH   HOH A . 
F 5 HOH   172 472 361  HOH   HOH A . 
F 5 HOH   173 473 280  HOH   HOH A . 
F 5 HOH   174 474 801  HOH   HOH A . 
F 5 HOH   175 475 370  HOH   HOH A . 
F 5 HOH   176 476 1276 HOH   HOH A . 
F 5 HOH   177 477 1307 HOH   HOH A . 
F 5 HOH   178 478 250  HOH   HOH A . 
F 5 HOH   179 479 3    HOH   HOH A . 
F 5 HOH   180 480 4    HOH   HOH A . 
F 5 HOH   181 481 342  HOH   HOH A . 
F 5 HOH   182 482 267  HOH   HOH A . 
F 5 HOH   183 483 224  HOH   HOH A . 
F 5 HOH   184 484 695  HOH   HOH A . 
F 5 HOH   185 485 1306 HOH   HOH A . 
F 5 HOH   186 486 202  HOH   HOH A . 
F 5 HOH   187 487 1287 HOH   HOH A . 
F 5 HOH   188 488 521  HOH   HOH A . 
F 5 HOH   189 489 674  HOH   HOH A . 
F 5 HOH   190 490 135  HOH   HOH A . 
F 5 HOH   191 491 7    HOH   HOH A . 
F 5 HOH   192 492 919  HOH   HOH A . 
F 5 HOH   193 493 318  HOH   HOH A . 
F 5 HOH   194 494 1299 HOH   HOH A . 
F 5 HOH   195 495 10   HOH   HOH A . 
F 5 HOH   196 496 711  HOH   HOH A . 
F 5 HOH   197 497 309  HOH   HOH A . 
F 5 HOH   198 498 331  HOH   HOH A . 
F 5 HOH   199 499 1314 HOH   HOH A . 
F 5 HOH   200 500 315  HOH   HOH A . 
F 5 HOH   201 501 941  HOH   HOH A . 
F 5 HOH   202 502 326  HOH   HOH A . 
F 5 HOH   203 503 805  HOH   HOH A . 
F 5 HOH   204 504 17   HOH   HOH A . 
F 5 HOH   205 505 263  HOH   HOH A . 
F 5 HOH   206 506 356  HOH   HOH A . 
F 5 HOH   207 507 208  HOH   HOH A . 
F 5 HOH   208 508 152  HOH   HOH A . 
F 5 HOH   209 509 1284 HOH   HOH A . 
F 5 HOH   210 510 180  HOH   HOH A . 
F 5 HOH   211 511 1071 HOH   HOH A . 
F 5 HOH   212 512 350  HOH   HOH A . 
F 5 HOH   213 513 376  HOH   HOH A . 
F 5 HOH   214 514 363  HOH   HOH A . 
F 5 HOH   215 515 371  HOH   HOH A . 
F 5 HOH   216 516 313  HOH   HOH A . 
F 5 HOH   217 517 8    HOH   HOH A . 
F 5 HOH   218 518 429  HOH   HOH A . 
F 5 HOH   219 519 185  HOH   HOH A . 
F 5 HOH   220 520 70   HOH   HOH A . 
F 5 HOH   221 521 772  HOH   HOH A . 
F 5 HOH   222 522 1074 HOH   HOH A . 
F 5 HOH   223 523 1292 HOH   HOH A . 
F 5 HOH   224 524 346  HOH   HOH A . 
F 5 HOH   225 525 1078 HOH   HOH A . 
G 5 HOH   1   201 64   HOH   HOH B . 
G 5 HOH   2   202 549  HOH   HOH B . 
G 5 HOH   3   203 240  HOH   HOH B . 
G 5 HOH   4   204 364  HOH   HOH B . 
G 5 HOH   5   205 1249 HOH   HOH B . 
G 5 HOH   6   206 398  HOH   HOH B . 
G 5 HOH   7   207 654  HOH   HOH B . 
G 5 HOH   8   208 358  HOH   HOH B . 
G 5 HOH   9   209 232  HOH   HOH B . 
G 5 HOH   10  210 758  HOH   HOH B . 
G 5 HOH   11  211 900  HOH   HOH B . 
G 5 HOH   12  212 50   HOH   HOH B . 
G 5 HOH   13  213 120  HOH   HOH B . 
G 5 HOH   14  214 743  HOH   HOH B . 
G 5 HOH   15  215 531  HOH   HOH B . 
G 5 HOH   16  216 353  HOH   HOH B . 
G 5 HOH   17  217 332  HOH   HOH B . 
G 5 HOH   18  218 444  HOH   HOH B . 
G 5 HOH   19  219 1140 HOH   HOH B . 
G 5 HOH   20  220 264  HOH   HOH B . 
G 5 HOH   21  221 452  HOH   HOH B . 
G 5 HOH   22  222 82   HOH   HOH B . 
G 5 HOH   23  223 205  HOH   HOH B . 
G 5 HOH   24  224 343  HOH   HOH B . 
G 5 HOH   25  225 131  HOH   HOH B . 
G 5 HOH   26  226 75   HOH   HOH B . 
G 5 HOH   27  227 172  HOH   HOH B . 
G 5 HOH   28  228 282  HOH   HOH B . 
G 5 HOH   29  229 1278 HOH   HOH B . 
G 5 HOH   30  230 60   HOH   HOH B . 
G 5 HOH   31  231 54   HOH   HOH B . 
G 5 HOH   32  232 1312 HOH   HOH B . 
G 5 HOH   33  233 325  HOH   HOH B . 
G 5 HOH   34  234 272  HOH   HOH B . 
G 5 HOH   35  235 276  HOH   HOH B . 
G 5 HOH   36  236 69   HOH   HOH B . 
G 5 HOH   37  237 127  HOH   HOH B . 
G 5 HOH   38  238 723  HOH   HOH B . 
G 5 HOH   39  239 110  HOH   HOH B . 
G 5 HOH   40  240 128  HOH   HOH B . 
G 5 HOH   41  241 133  HOH   HOH B . 
G 5 HOH   42  242 1    HOH   HOH B . 
G 5 HOH   43  243 300  HOH   HOH B . 
G 5 HOH   44  244 181  HOH   HOH B . 
G 5 HOH   45  245 14   HOH   HOH B . 
G 5 HOH   46  246 129  HOH   HOH B . 
G 5 HOH   47  247 144  HOH   HOH B . 
G 5 HOH   48  248 166  HOH   HOH B . 
G 5 HOH   49  249 41   HOH   HOH B . 
G 5 HOH   50  250 9    HOH   HOH B . 
G 5 HOH   51  251 30   HOH   HOH B . 
G 5 HOH   52  252 52   HOH   HOH B . 
G 5 HOH   53  253 252  HOH   HOH B . 
G 5 HOH   54  254 143  HOH   HOH B . 
G 5 HOH   55  255 150  HOH   HOH B . 
G 5 HOH   56  256 231  HOH   HOH B . 
G 5 HOH   57  257 103  HOH   HOH B . 
G 5 HOH   58  258 72   HOH   HOH B . 
G 5 HOH   59  259 47   HOH   HOH B . 
G 5 HOH   60  260 271  HOH   HOH B . 
G 5 HOH   61  261 347  HOH   HOH B . 
G 5 HOH   62  262 31   HOH   HOH B . 
G 5 HOH   63  263 391  HOH   HOH B . 
G 5 HOH   64  264 302  HOH   HOH B . 
G 5 HOH   65  265 59   HOH   HOH B . 
G 5 HOH   66  266 10   HOH   HOH B . 
G 5 HOH   67  267 242  HOH   HOH B . 
G 5 HOH   68  268 61   HOH   HOH B . 
G 5 HOH   69  269 221  HOH   HOH B . 
G 5 HOH   70  270 11   HOH   HOH B . 
G 5 HOH   71  271 243  HOH   HOH B . 
G 5 HOH   72  272 84   HOH   HOH B . 
G 5 HOH   73  273 117  HOH   HOH B . 
G 5 HOH   74  274 1277 HOH   HOH B . 
G 5 HOH   75  275 20   HOH   HOH B . 
G 5 HOH   76  276 175  HOH   HOH B . 
G 5 HOH   77  277 77   HOH   HOH B . 
G 5 HOH   78  278 147  HOH   HOH B . 
G 5 HOH   79  279 114  HOH   HOH B . 
G 5 HOH   80  280 287  HOH   HOH B . 
G 5 HOH   81  281 43   HOH   HOH B . 
G 5 HOH   82  282 235  HOH   HOH B . 
G 5 HOH   83  283 1305 HOH   HOH B . 
G 5 HOH   84  284 22   HOH   HOH B . 
G 5 HOH   85  285 216  HOH   HOH B . 
G 5 HOH   86  286 99   HOH   HOH B . 
G 5 HOH   87  287 220  HOH   HOH B . 
G 5 HOH   88  288 299  HOH   HOH B . 
G 5 HOH   89  289 1066 HOH   HOH B . 
G 5 HOH   90  290 88   HOH   HOH B . 
G 5 HOH   91  291 13   HOH   HOH B . 
G 5 HOH   92  292 106  HOH   HOH B . 
G 5 HOH   93  293 1106 HOH   HOH B . 
G 5 HOH   94  294 137  HOH   HOH B . 
G 5 HOH   95  295 89   HOH   HOH B . 
G 5 HOH   96  296 416  HOH   HOH B . 
G 5 HOH   97  297 160  HOH   HOH B . 
G 5 HOH   98  298 112  HOH   HOH B . 
G 5 HOH   99  299 387  HOH   HOH B . 
G 5 HOH   100 300 311  HOH   HOH B . 
G 5 HOH   101 301 316  HOH   HOH B . 
G 5 HOH   102 302 142  HOH   HOH B . 
G 5 HOH   103 303 32   HOH   HOH B . 
G 5 HOH   104 304 215  HOH   HOH B . 
G 5 HOH   105 305 297  HOH   HOH B . 
G 5 HOH   106 306 101  HOH   HOH B . 
G 5 HOH   107 307 38   HOH   HOH B . 
G 5 HOH   108 308 48   HOH   HOH B . 
G 5 HOH   109 309 37   HOH   HOH B . 
G 5 HOH   110 310 118  HOH   HOH B . 
G 5 HOH   111 311 170  HOH   HOH B . 
G 5 HOH   112 312 141  HOH   HOH B . 
G 5 HOH   113 313 635  HOH   HOH B . 
G 5 HOH   114 314 44   HOH   HOH B . 
G 5 HOH   115 315 1285 HOH   HOH B . 
G 5 HOH   116 316 91   HOH   HOH B . 
G 5 HOH   117 317 177  HOH   HOH B . 
G 5 HOH   118 318 23   HOH   HOH B . 
G 5 HOH   119 319 28   HOH   HOH B . 
G 5 HOH   120 320 197  HOH   HOH B . 
G 5 HOH   121 321 704  HOH   HOH B . 
G 5 HOH   122 322 1274 HOH   HOH B . 
G 5 HOH   123 323 55   HOH   HOH B . 
G 5 HOH   124 324 100  HOH   HOH B . 
G 5 HOH   125 325 161  HOH   HOH B . 
G 5 HOH   126 326 29   HOH   HOH B . 
G 5 HOH   127 327 207  HOH   HOH B . 
G 5 HOH   128 328 1294 HOH   HOH B . 
G 5 HOH   129 329 341  HOH   HOH B . 
G 5 HOH   130 330 98   HOH   HOH B . 
G 5 HOH   131 331 182  HOH   HOH B . 
G 5 HOH   132 332 717  HOH   HOH B . 
G 5 HOH   133 333 334  HOH   HOH B . 
G 5 HOH   134 334 1291 HOH   HOH B . 
G 5 HOH   135 335 65   HOH   HOH B . 
G 5 HOH   136 336 1126 HOH   HOH B . 
G 5 HOH   137 337 445  HOH   HOH B . 
G 5 HOH   138 338 1293 HOH   HOH B . 
G 5 HOH   139 339 234  HOH   HOH B . 
G 5 HOH   140 340 619  HOH   HOH B . 
G 5 HOH   141 341 362  HOH   HOH B . 
G 5 HOH   142 342 339  HOH   HOH B . 
G 5 HOH   143 343 178  HOH   HOH B . 
G 5 HOH   144 344 960  HOH   HOH B . 
G 5 HOH   145 345 90   HOH   HOH B . 
G 5 HOH   146 346 463  HOH   HOH B . 
G 5 HOH   147 347 87   HOH   HOH B . 
G 5 HOH   148 348 623  HOH   HOH B . 
G 5 HOH   149 349 1304 HOH   HOH B . 
G 5 HOH   150 350 191  HOH   HOH B . 
G 5 HOH   151 351 335  HOH   HOH B . 
G 5 HOH   152 352 304  HOH   HOH B . 
G 5 HOH   153 353 1046 HOH   HOH B . 
G 5 HOH   154 354 1280 HOH   HOH B . 
G 5 HOH   155 355 541  HOH   HOH B . 
G 5 HOH   156 356 290  HOH   HOH B . 
G 5 HOH   157 357 203  HOH   HOH B . 
G 5 HOH   158 358 1077 HOH   HOH B . 
G 5 HOH   159 359 389  HOH   HOH B . 
G 5 HOH   160 360 718  HOH   HOH B . 
G 5 HOH   161 361 283  HOH   HOH B . 
G 5 HOH   162 362 1072 HOH   HOH B . 
G 5 HOH   163 363 479  HOH   HOH B . 
G 5 HOH   164 364 1316 HOH   HOH B . 
G 5 HOH   165 365 291  HOH   HOH B . 
G 5 HOH   166 366 898  HOH   HOH B . 
G 5 HOH   167 367 340  HOH   HOH B . 
G 5 HOH   168 368 615  HOH   HOH B . 
G 5 HOH   169 369 373  HOH   HOH B . 
G 5 HOH   170 370 667  HOH   HOH B . 
G 5 HOH   171 371 1303 HOH   HOH B . 
G 5 HOH   172 372 190  HOH   HOH B . 
G 5 HOH   173 373 431  HOH   HOH B . 
G 5 HOH   174 374 310  HOH   HOH B . 
G 5 HOH   175 375 1173 HOH   HOH B . 
G 5 HOH   176 376 149  HOH   HOH B . 
G 5 HOH   177 377 1000 HOH   HOH B . 
G 5 HOH   178 378 183  HOH   HOH B . 
G 5 HOH   179 379 1163 HOH   HOH B . 
G 5 HOH   180 380 418  HOH   HOH B . 
G 5 HOH   181 381 1311 HOH   HOH B . 
G 5 HOH   182 382 176  HOH   HOH B . 
G 5 HOH   183 383 424  HOH   HOH B . 
G 5 HOH   184 384 981  HOH   HOH B . 
G 5 HOH   185 385 491  HOH   HOH B . 
G 5 HOH   186 386 1298 HOH   HOH B . 
G 5 HOH   187 387 248  HOH   HOH B . 
G 5 HOH   188 388 470  HOH   HOH B . 
G 5 HOH   189 389 265  HOH   HOH B . 
G 5 HOH   190 390 184  HOH   HOH B . 
G 5 HOH   191 391 360  HOH   HOH B . 
G 5 HOH   192 392 410  HOH   HOH B . 
G 5 HOH   193 393 355  HOH   HOH B . 
G 5 HOH   194 394 274  HOH   HOH B . 
G 5 HOH   195 395 314  HOH   HOH B . 
G 5 HOH   196 396 157  HOH   HOH B . 
G 5 HOH   197 397 566  HOH   HOH B . 
G 5 HOH   198 398 321  HOH   HOH B . 
G 5 HOH   199 399 792  HOH   HOH B . 
G 5 HOH   200 400 558  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           7HEJ 
_cell.length_a           88.694 
_cell.length_b           88.694 
_cell.length_c           39.436 
_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                         7HEJ 
_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          7HEJ 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.14 
_exptl_crystal.density_percent_sol   42.44 
_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   2023-05-24 
_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                     7HEJ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.350 
_reflns.d_resolution_high            1.000 
_reflns.number_obs                   164844 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.600 
_reflns.pdbx_Rmerge_I_obs            0.041 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        17.200 
_reflns.B_iso_Wilson_estimate        12.030 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.044 
_reflns.pdbx_Rpim_I_all              0.017 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     1053836 
_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                      ? 
# 
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 
1 1 1.000 1.020  ? 33638 7570 ? 0.943 ? ? ? 4.400 ? 1.100  ? ? ? ? ? ? 92.900 1.068 0.491 0.722 
1 2 5.480 44.350 ? 7521  1091 ? 0.031 ? ? ? 6.900 ? 57.000 ? ? ? ? ? ? 99.800 0.034 0.013 0.998 
# 
_refine.entry_id                                 7HEJ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0000 
_refine.ls_d_res_low                             44.3500 
_refine.pdbx_ls_sigma_F                          1.350 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.5500 
_refine.ls_number_reflns_obs                     164770 
_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                          0.1428 
_refine.ls_R_factor_R_work                       0.1421 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1552 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8200 
_refine.ls_number_reflns_R_free                  7946 
_refine.ls_number_reflns_R_work                  156824 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               18.6302 
_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                            0.0900 
_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                                64.840 
_refine.B_iso_min                                8.210 
_refine.pdbx_overall_phase_error                 16.4400 
_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                        44.3500 
_refine_hist.pdbx_number_atoms_ligand         42 
_refine_hist.number_atoms_solvent             425 
_refine_hist.number_atoms_total               3009 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           14.90 
_refine_hist.pdbx_B_iso_mean_solvent          29.69 
_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 
1.0000 1.0100  30 91.0000  4817 . 0.3509 0.3354 . 258 0.0000 5075 . 'X-RAY DIFFRACTION' 
1.0100 1.0200  30 96.0000  5003 . 0.2869 0.3140 . 212 0.0000 5215 . 'X-RAY DIFFRACTION' 
1.0200 1.0400  30 100.0000 5264 . 0.2381 0.2337 . 268 0.0000 5532 . 'X-RAY DIFFRACTION' 
1.0400 1.0500  30 100.0000 5155 . 0.2110 0.2298 . 267 0.0000 5422 . 'X-RAY DIFFRACTION' 
1.0500 1.0600  30 100.0000 5194 . 0.1936 0.2146 . 323 0.0000 5517 . 'X-RAY DIFFRACTION' 
1.0600 1.0800  30 100.0000 5227 . 0.1797 0.1972 . 249 0.0000 5476 . 'X-RAY DIFFRACTION' 
1.0800 1.0900  30 100.0000 5236 . 0.1749 0.2018 . 258 0.0000 5494 . 'X-RAY DIFFRACTION' 
1.0900 1.1100  30 100.0000 5213 . 0.1583 0.1837 . 248 0.0000 5461 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 5244 . 0.1527 0.1652 . 278 0.0000 5522 . 'X-RAY DIFFRACTION' 
1.1300 1.1400  30 100.0000 5184 . 0.1422 0.1673 . 242 0.0000 5426 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 5271 . 0.1322 0.1491 . 276 0.0000 5547 . 'X-RAY DIFFRACTION' 
1.1600 1.1900  30 100.0000 5242 . 0.1265 0.1495 . 257 0.0000 5499 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 5148 . 0.1205 0.1509 . 286 0.0000 5434 . 'X-RAY DIFFRACTION' 
1.2100 1.2300  30 100.0000 5335 . 0.1184 0.1387 . 225 0.0000 5560 . 'X-RAY DIFFRACTION' 
1.2300 1.2600  30 100.0000 5185 . 0.1221 0.1363 . 261 0.0000 5446 . 'X-RAY DIFFRACTION' 
1.2600 1.2900  30 100.0000 5241 . 0.1218 0.1391 . 276 0.0000 5517 . 'X-RAY DIFFRACTION' 
1.2900 1.3200  30 100.0000 5222 . 0.1242 0.1464 . 285 0.0000 5507 . 'X-RAY DIFFRACTION' 
1.3200 1.3600  30 100.0000 5242 . 0.1315 0.1396 . 278 0.0000 5520 . 'X-RAY DIFFRACTION' 
1.3600 1.4000  30 100.0000 5250 . 0.1338 0.1571 . 251 0.0000 5501 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 5225 . 0.1321 0.1594 . 267 0.0000 5492 . 'X-RAY DIFFRACTION' 
1.4400 1.4900  30 100.0000 5281 . 0.1248 0.1309 . 245 0.0000 5526 . 'X-RAY DIFFRACTION' 
1.4900 1.5500  30 100.0000 5211 . 0.1186 0.1265 . 283 0.0000 5494 . 'X-RAY DIFFRACTION' 
1.5500 1.6200  30 100.0000 5280 . 0.1187 0.1328 . 264 0.0000 5544 . 'X-RAY DIFFRACTION' 
1.6200 1.7100  30 100.0000 5279 . 0.1262 0.1438 . 255 0.0000 5534 . 'X-RAY DIFFRACTION' 
1.7100 1.8200  30 100.0000 5266 . 0.1345 0.1368 . 253 0.0000 5519 . 'X-RAY DIFFRACTION' 
1.8200 1.9600  30 100.0000 5259 . 0.1331 0.1368 . 283 0.0000 5542 . 'X-RAY DIFFRACTION' 
1.9600 2.1500  30 100.0000 5287 . 0.1389 0.1417 . 285 0.0000 5572 . 'X-RAY DIFFRACTION' 
2.1500 2.4700  30 100.0000 5278 . 0.1368 0.1427 . 289 0.0000 5567 . 'X-RAY DIFFRACTION' 
2.4700 3.1100  30 100.0000 5311 . 0.1487 0.1633 . 256 0.0000 5567 . 'X-RAY DIFFRACTION' 
3.1100 44.3500 30 100.0000 5474 . 0.1499 0.1701 . 268 0.0000 5742 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HEJ 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003679' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HEJ 
_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 5 ? 
# 
_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 7HEJ A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HEJ 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 7HEJ SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HEJ MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HEJ SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HEJ 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 
2 1 B,G       
# 
_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 LYS A 19  ? N LYS A 19  O VAL A 155 ? O VAL A 155 
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 HIS B 94  ? O HIS B 94  N CYS B 81  ? N CYS B 81  
# 
_pdbx_entry_details.entry_id                   7HEJ 
_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 
# 
_pdbx_validate_close_contact.id               1 
_pdbx_validate_close_contact.PDB_model_num    1 
_pdbx_validate_close_contact.auth_atom_id_1   HZ2 
_pdbx_validate_close_contact.auth_asym_id_1   A 
_pdbx_validate_close_contact.auth_comp_id_1   LYS 
_pdbx_validate_close_contact.auth_seq_id_1    29 
_pdbx_validate_close_contact.PDB_ins_code_1   ? 
_pdbx_validate_close_contact.label_alt_id_1   B 
_pdbx_validate_close_contact.auth_atom_id_2   O 
_pdbx_validate_close_contact.auth_asym_id_2   A 
_pdbx_validate_close_contact.auth_comp_id_2   HOH 
_pdbx_validate_close_contact.auth_seq_id_2    305 
_pdbx_validate_close_contact.PDB_ins_code_2   ? 
_pdbx_validate_close_contact.label_alt_id_2   ? 
_pdbx_validate_close_contact.dist             1.58 
# 
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 ASN A 15  ? B -141.69 16.32   
2 1 HIS A 86  ? ? 55.19   -133.33 
3 1 SER A 128 ? B 70.05   -9.15   
4 1 HIS B 86  ? ? 56.94   -127.88 
# 
_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 524 ? 5.92 . 
2 1 O ? A HOH 525 ? 7.56 . 
3 1 O ? B HOH 400 ? 6.54 . 
# 
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 
A1A9W N2   N  Y N 1   
A1A9W C3   C  Y N 2   
A1A9W C6   C  Y N 3   
A1A9W C9   C  N R 4   
A1A9W C12  C  N N 5   
A1A9W C1   C  N N 6   
A1A9W C10  C  N N 7   
A1A9W C11  C  N N 8   
A1A9W C2   C  N S 9   
A1A9W C4   C  Y N 10  
A1A9W C5   C  Y N 11  
A1A9W C7   C  Y N 12  
A1A9W C8   C  Y N 13  
A1A9W N1   N  N N 14  
A1A9W N3   N  Y N 15  
A1A9W N4   N  Y N 16  
A1A9W O1   O  N N 17  
A1A9W O2   O  N N 18  
A1A9W H2   H  N N 19  
A1A9W H16  H  N N 20  
A1A9W H15  H  N N 21  
A1A9W H5   H  N N 22  
A1A9W H4   H  N N 23  
A1A9W H11  H  N N 24  
A1A9W H12  H  N N 25  
A1A9W H14  H  N N 26  
A1A9W H13  H  N N 27  
A1A9W H1   H  N N 28  
A1A9W H7   H  N N 29  
A1A9W H8   H  N N 30  
A1A9W H9   H  N N 31  
A1A9W H6   H  N N 32  
A1A9W H10  H  N N 33  
A1A9W H3   H  N N 34  
ALA   N    N  N N 35  
ALA   CA   C  N S 36  
ALA   C    C  N N 37  
ALA   O    O  N N 38  
ALA   CB   C  N N 39  
ALA   OXT  O  N N 40  
ALA   H    H  N N 41  
ALA   H2   H  N N 42  
ALA   HA   H  N N 43  
ALA   HB1  H  N N 44  
ALA   HB2  H  N N 45  
ALA   HB3  H  N N 46  
ALA   HXT  H  N N 47  
ARG   N    N  N N 48  
ARG   CA   C  N S 49  
ARG   C    C  N N 50  
ARG   O    O  N N 51  
ARG   CB   C  N N 52  
ARG   CG   C  N N 53  
ARG   CD   C  N N 54  
ARG   NE   N  N N 55  
ARG   CZ   C  N N 56  
ARG   NH1  N  N N 57  
ARG   NH2  N  N N 58  
ARG   OXT  O  N N 59  
ARG   H    H  N N 60  
ARG   H2   H  N N 61  
ARG   HA   H  N N 62  
ARG   HB2  H  N N 63  
ARG   HB3  H  N N 64  
ARG   HG2  H  N N 65  
ARG   HG3  H  N N 66  
ARG   HD2  H  N N 67  
ARG   HD3  H  N N 68  
ARG   HE   H  N N 69  
ARG   HH11 H  N N 70  
ARG   HH12 H  N N 71  
ARG   HH21 H  N N 72  
ARG   HH22 H  N N 73  
ARG   HXT  H  N N 74  
ASN   N    N  N N 75  
ASN   CA   C  N S 76  
ASN   C    C  N N 77  
ASN   O    O  N N 78  
ASN   CB   C  N N 79  
ASN   CG   C  N N 80  
ASN   OD1  O  N N 81  
ASN   ND2  N  N N 82  
ASN   OXT  O  N N 83  
ASN   H    H  N N 84  
ASN   H2   H  N N 85  
ASN   HA   H  N N 86  
ASN   HB2  H  N N 87  
ASN   HB3  H  N N 88  
ASN   HD21 H  N N 89  
ASN   HD22 H  N N 90  
ASN   HXT  H  N N 91  
ASP   N    N  N N 92  
ASP   CA   C  N S 93  
ASP   C    C  N N 94  
ASP   O    O  N N 95  
ASP   CB   C  N N 96  
ASP   CG   C  N N 97  
ASP   OD1  O  N N 98  
ASP   OD2  O  N N 99  
ASP   OXT  O  N N 100 
ASP   H    H  N N 101 
ASP   H2   H  N N 102 
ASP   HA   H  N N 103 
ASP   HB2  H  N N 104 
ASP   HB3  H  N N 105 
ASP   HD2  H  N N 106 
ASP   HXT  H  N N 107 
CL    CL   CL N N 108 
CYS   N    N  N N 109 
CYS   CA   C  N R 110 
CYS   C    C  N N 111 
CYS   O    O  N N 112 
CYS   CB   C  N N 113 
CYS   SG   S  N N 114 
CYS   OXT  O  N N 115 
CYS   H    H  N N 116 
CYS   H2   H  N N 117 
CYS   HA   H  N N 118 
CYS   HB2  H  N N 119 
CYS   HB3  H  N N 120 
CYS   HG   H  N N 121 
CYS   HXT  H  N N 122 
GLN   N    N  N N 123 
GLN   CA   C  N S 124 
GLN   C    C  N N 125 
GLN   O    O  N N 126 
GLN   CB   C  N N 127 
GLN   CG   C  N N 128 
GLN   CD   C  N N 129 
GLN   OE1  O  N N 130 
GLN   NE2  N  N N 131 
GLN   OXT  O  N N 132 
GLN   H    H  N N 133 
GLN   H2   H  N N 134 
GLN   HA   H  N N 135 
GLN   HB2  H  N N 136 
GLN   HB3  H  N N 137 
GLN   HG2  H  N N 138 
GLN   HG3  H  N N 139 
GLN   HE21 H  N N 140 
GLN   HE22 H  N N 141 
GLN   HXT  H  N N 142 
GLU   N    N  N N 143 
GLU   CA   C  N S 144 
GLU   C    C  N N 145 
GLU   O    O  N N 146 
GLU   CB   C  N N 147 
GLU   CG   C  N N 148 
GLU   CD   C  N N 149 
GLU   OE1  O  N N 150 
GLU   OE2  O  N N 151 
GLU   OXT  O  N N 152 
GLU   H    H  N N 153 
GLU   H2   H  N N 154 
GLU   HA   H  N N 155 
GLU   HB2  H  N N 156 
GLU   HB3  H  N N 157 
GLU   HG2  H  N N 158 
GLU   HG3  H  N N 159 
GLU   HE2  H  N N 160 
GLU   HXT  H  N N 161 
GLY   N    N  N N 162 
GLY   CA   C  N N 163 
GLY   C    C  N N 164 
GLY   O    O  N N 165 
GLY   OXT  O  N N 166 
GLY   H    H  N N 167 
GLY   H2   H  N N 168 
GLY   HA2  H  N N 169 
GLY   HA3  H  N N 170 
GLY   HXT  H  N N 171 
HIS   N    N  N N 172 
HIS   CA   C  N S 173 
HIS   C    C  N N 174 
HIS   O    O  N N 175 
HIS   CB   C  N N 176 
HIS   CG   C  Y N 177 
HIS   ND1  N  Y N 178 
HIS   CD2  C  Y N 179 
HIS   CE1  C  Y N 180 
HIS   NE2  N  Y N 181 
HIS   OXT  O  N N 182 
HIS   H    H  N N 183 
HIS   H2   H  N N 184 
HIS   HA   H  N N 185 
HIS   HB2  H  N N 186 
HIS   HB3  H  N N 187 
HIS   HD1  H  N N 188 
HIS   HD2  H  N N 189 
HIS   HE1  H  N N 190 
HIS   HE2  H  N N 191 
HIS   HXT  H  N N 192 
HOH   O    O  N N 193 
HOH   H1   H  N N 194 
HOH   H2   H  N N 195 
ILE   N    N  N N 196 
ILE   CA   C  N S 197 
ILE   C    C  N N 198 
ILE   O    O  N N 199 
ILE   CB   C  N S 200 
ILE   CG1  C  N N 201 
ILE   CG2  C  N N 202 
ILE   CD1  C  N N 203 
ILE   OXT  O  N N 204 
ILE   H    H  N N 205 
ILE   H2   H  N N 206 
ILE   HA   H  N N 207 
ILE   HB   H  N N 208 
ILE   HG12 H  N N 209 
ILE   HG13 H  N N 210 
ILE   HG21 H  N N 211 
ILE   HG22 H  N N 212 
ILE   HG23 H  N N 213 
ILE   HD11 H  N N 214 
ILE   HD12 H  N N 215 
ILE   HD13 H  N N 216 
ILE   HXT  H  N N 217 
LEU   N    N  N N 218 
LEU   CA   C  N S 219 
LEU   C    C  N N 220 
LEU   O    O  N N 221 
LEU   CB   C  N N 222 
LEU   CG   C  N N 223 
LEU   CD1  C  N N 224 
LEU   CD2  C  N N 225 
LEU   OXT  O  N N 226 
LEU   H    H  N N 227 
LEU   H2   H  N N 228 
LEU   HA   H  N N 229 
LEU   HB2  H  N N 230 
LEU   HB3  H  N N 231 
LEU   HG   H  N N 232 
LEU   HD11 H  N N 233 
LEU   HD12 H  N N 234 
LEU   HD13 H  N N 235 
LEU   HD21 H  N N 236 
LEU   HD22 H  N N 237 
LEU   HD23 H  N N 238 
LEU   HXT  H  N N 239 
LYS   N    N  N N 240 
LYS   CA   C  N S 241 
LYS   C    C  N N 242 
LYS   O    O  N N 243 
LYS   CB   C  N N 244 
LYS   CG   C  N N 245 
LYS   CD   C  N N 246 
LYS   CE   C  N N 247 
LYS   NZ   N  N N 248 
LYS   OXT  O  N N 249 
LYS   H    H  N N 250 
LYS   H2   H  N N 251 
LYS   HA   H  N N 252 
LYS   HB2  H  N N 253 
LYS   HB3  H  N N 254 
LYS   HG2  H  N N 255 
LYS   HG3  H  N N 256 
LYS   HD2  H  N N 257 
LYS   HD3  H  N N 258 
LYS   HE2  H  N N 259 
LYS   HE3  H  N N 260 
LYS   HZ1  H  N N 261 
LYS   HZ2  H  N N 262 
LYS   HZ3  H  N N 263 
LYS   HXT  H  N N 264 
MET   N    N  N N 265 
MET   CA   C  N S 266 
MET   C    C  N N 267 
MET   O    O  N N 268 
MET   CB   C  N N 269 
MET   CG   C  N N 270 
MET   SD   S  N N 271 
MET   CE   C  N N 272 
MET   OXT  O  N N 273 
MET   H    H  N N 274 
MET   H2   H  N N 275 
MET   HA   H  N N 276 
MET   HB2  H  N N 277 
MET   HB3  H  N N 278 
MET   HG2  H  N N 279 
MET   HG3  H  N N 280 
MET   HE1  H  N N 281 
MET   HE2  H  N N 282 
MET   HE3  H  N N 283 
MET   HXT  H  N N 284 
PHE   N    N  N N 285 
PHE   CA   C  N S 286 
PHE   C    C  N N 287 
PHE   O    O  N N 288 
PHE   CB   C  N N 289 
PHE   CG   C  Y N 290 
PHE   CD1  C  Y N 291 
PHE   CD2  C  Y N 292 
PHE   CE1  C  Y N 293 
PHE   CE2  C  Y N 294 
PHE   CZ   C  Y N 295 
PHE   OXT  O  N N 296 
PHE   H    H  N N 297 
PHE   H2   H  N N 298 
PHE   HA   H  N N 299 
PHE   HB2  H  N N 300 
PHE   HB3  H  N N 301 
PHE   HD1  H  N N 302 
PHE   HD2  H  N N 303 
PHE   HE1  H  N N 304 
PHE   HE2  H  N N 305 
PHE   HZ   H  N N 306 
PHE   HXT  H  N N 307 
PRO   N    N  N N 308 
PRO   CA   C  N S 309 
PRO   C    C  N N 310 
PRO   O    O  N N 311 
PRO   CB   C  N N 312 
PRO   CG   C  N N 313 
PRO   CD   C  N N 314 
PRO   OXT  O  N N 315 
PRO   H    H  N N 316 
PRO   HA   H  N N 317 
PRO   HB2  H  N N 318 
PRO   HB3  H  N N 319 
PRO   HG2  H  N N 320 
PRO   HG3  H  N N 321 
PRO   HD2  H  N N 322 
PRO   HD3  H  N N 323 
PRO   HXT  H  N N 324 
SER   N    N  N N 325 
SER   CA   C  N S 326 
SER   C    C  N N 327 
SER   O    O  N N 328 
SER   CB   C  N N 329 
SER   OG   O  N N 330 
SER   OXT  O  N N 331 
SER   H    H  N N 332 
SER   H2   H  N N 333 
SER   HA   H  N N 334 
SER   HB2  H  N N 335 
SER   HB3  H  N N 336 
SER   HG   H  N N 337 
SER   HXT  H  N N 338 
TFA   C1   C  N N 339 
TFA   C2   C  N N 340 
TFA   O    O  N N 341 
TFA   F1   F  N N 342 
TFA   F2   F  N N 343 
TFA   F3   F  N N 344 
TFA   OXT  O  N N 345 
TFA   HXT  H  N N 346 
THR   N    N  N N 347 
THR   CA   C  N S 348 
THR   C    C  N N 349 
THR   O    O  N N 350 
THR   CB   C  N R 351 
THR   OG1  O  N N 352 
THR   CG2  C  N N 353 
THR   OXT  O  N N 354 
THR   H    H  N N 355 
THR   H2   H  N N 356 
THR   HA   H  N N 357 
THR   HB   H  N N 358 
THR   HG1  H  N N 359 
THR   HG21 H  N N 360 
THR   HG22 H  N N 361 
THR   HG23 H  N N 362 
THR   HXT  H  N N 363 
TYR   N    N  N N 364 
TYR   CA   C  N S 365 
TYR   C    C  N N 366 
TYR   O    O  N N 367 
TYR   CB   C  N N 368 
TYR   CG   C  Y N 369 
TYR   CD1  C  Y N 370 
TYR   CD2  C  Y N 371 
TYR   CE1  C  Y N 372 
TYR   CE2  C  Y N 373 
TYR   CZ   C  Y N 374 
TYR   OH   O  N N 375 
TYR   OXT  O  N N 376 
TYR   H    H  N N 377 
TYR   H2   H  N N 378 
TYR   HA   H  N N 379 
TYR   HB2  H  N N 380 
TYR   HB3  H  N N 381 
TYR   HD1  H  N N 382 
TYR   HD2  H  N N 383 
TYR   HE1  H  N N 384 
TYR   HE2  H  N N 385 
TYR   HH   H  N N 386 
TYR   HXT  H  N N 387 
VAL   N    N  N N 388 
VAL   CA   C  N S 389 
VAL   C    C  N N 390 
VAL   O    O  N N 391 
VAL   CB   C  N N 392 
VAL   CG1  C  N N 393 
VAL   CG2  C  N N 394 
VAL   OXT  O  N N 395 
VAL   H    H  N N 396 
VAL   H2   H  N N 397 
VAL   HA   H  N N 398 
VAL   HB   H  N N 399 
VAL   HG11 H  N N 400 
VAL   HG12 H  N N 401 
VAL   HG13 H  N N 402 
VAL   HG21 H  N N 403 
VAL   HG22 H  N N 404 
VAL   HG23 H  N N 405 
VAL   HXT  H  N N 406 
# 
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 
A1A9W C1  O1   sing N N 1   
A1A9W C1  C2   sing N N 2   
A1A9W C10 C9   sing N N 3   
A1A9W C10 C11  sing N N 4   
A1A9W C9  C2   sing N N 5   
A1A9W C9  C12  sing N N 6   
A1A9W C2  N1   sing N N 7   
A1A9W C11 O2   sing N N 8   
A1A9W C12 O2   sing N N 9   
A1A9W N1  C3   sing N N 10  
A1A9W C3  C6   doub Y N 11  
A1A9W C3  N2   sing Y N 12  
A1A9W C7  C6   sing Y N 13  
A1A9W C7  C8   doub Y N 14  
A1A9W C6  C5   sing Y N 15  
A1A9W N2  C4   doub Y N 16  
A1A9W C8  N4   sing Y N 17  
A1A9W C5  N4   sing Y N 18  
A1A9W C5  N3   doub Y N 19  
A1A9W C4  N3   sing Y N 20  
A1A9W C9  H2   sing N N 21  
A1A9W C12 H16  sing N N 22  
A1A9W C12 H15  sing N N 23  
A1A9W C1  H5   sing N N 24  
A1A9W C1  H4   sing N N 25  
A1A9W C10 H11  sing N N 26  
A1A9W C10 H12  sing N N 27  
A1A9W C11 H14  sing N N 28  
A1A9W C11 H13  sing N N 29  
A1A9W C2  H1   sing N N 30  
A1A9W C4  H7   sing N N 31  
A1A9W C7  H8   sing N N 32  
A1A9W C8  H9   sing N N 33  
A1A9W N1  H6   sing N N 34  
A1A9W N4  H10  sing N N 35  
A1A9W O1  H3   sing N N 36  
ALA   N   CA   sing N N 37  
ALA   N   H    sing N N 38  
ALA   N   H2   sing N N 39  
ALA   CA  C    sing N N 40  
ALA   CA  CB   sing N N 41  
ALA   CA  HA   sing N N 42  
ALA   C   O    doub N N 43  
ALA   C   OXT  sing N N 44  
ALA   CB  HB1  sing N N 45  
ALA   CB  HB2  sing N N 46  
ALA   CB  HB3  sing N N 47  
ALA   OXT HXT  sing N N 48  
ARG   N   CA   sing N N 49  
ARG   N   H    sing N N 50  
ARG   N   H2   sing N N 51  
ARG   CA  C    sing N N 52  
ARG   CA  CB   sing N N 53  
ARG   CA  HA   sing N N 54  
ARG   C   O    doub N N 55  
ARG   C   OXT  sing N N 56  
ARG   CB  CG   sing N N 57  
ARG   CB  HB2  sing N N 58  
ARG   CB  HB3  sing N N 59  
ARG   CG  CD   sing N N 60  
ARG   CG  HG2  sing N N 61  
ARG   CG  HG3  sing N N 62  
ARG   CD  NE   sing N N 63  
ARG   CD  HD2  sing N N 64  
ARG   CD  HD3  sing N N 65  
ARG   NE  CZ   sing N N 66  
ARG   NE  HE   sing N N 67  
ARG   CZ  NH1  sing N N 68  
ARG   CZ  NH2  doub N N 69  
ARG   NH1 HH11 sing N N 70  
ARG   NH1 HH12 sing N N 71  
ARG   NH2 HH21 sing N N 72  
ARG   NH2 HH22 sing N N 73  
ARG   OXT HXT  sing N N 74  
ASN   N   CA   sing N N 75  
ASN   N   H    sing N N 76  
ASN   N   H2   sing N N 77  
ASN   CA  C    sing N N 78  
ASN   CA  CB   sing N N 79  
ASN   CA  HA   sing N N 80  
ASN   C   O    doub N N 81  
ASN   C   OXT  sing N N 82  
ASN   CB  CG   sing N N 83  
ASN   CB  HB2  sing N N 84  
ASN   CB  HB3  sing N N 85  
ASN   CG  OD1  doub N N 86  
ASN   CG  ND2  sing N N 87  
ASN   ND2 HD21 sing N N 88  
ASN   ND2 HD22 sing N N 89  
ASN   OXT HXT  sing N N 90  
ASP   N   CA   sing N N 91  
ASP   N   H    sing N N 92  
ASP   N   H2   sing N N 93  
ASP   CA  C    sing N N 94  
ASP   CA  CB   sing N N 95  
ASP   CA  HA   sing N N 96  
ASP   C   O    doub N N 97  
ASP   C   OXT  sing N N 98  
ASP   CB  CG   sing N N 99  
ASP   CB  HB2  sing N N 100 
ASP   CB  HB3  sing N N 101 
ASP   CG  OD1  doub N N 102 
ASP   CG  OD2  sing N N 103 
ASP   OD2 HD2  sing N N 104 
ASP   OXT HXT  sing N N 105 
CYS   N   CA   sing N N 106 
CYS   N   H    sing N N 107 
CYS   N   H2   sing N N 108 
CYS   CA  C    sing N N 109 
CYS   CA  CB   sing N N 110 
CYS   CA  HA   sing N N 111 
CYS   C   O    doub N N 112 
CYS   C   OXT  sing N N 113 
CYS   CB  SG   sing N N 114 
CYS   CB  HB2  sing N N 115 
CYS   CB  HB3  sing N N 116 
CYS   SG  HG   sing N N 117 
CYS   OXT HXT  sing N N 118 
GLN   N   CA   sing N N 119 
GLN   N   H    sing N N 120 
GLN   N   H2   sing N N 121 
GLN   CA  C    sing N N 122 
GLN   CA  CB   sing N N 123 
GLN   CA  HA   sing N N 124 
GLN   C   O    doub N N 125 
GLN   C   OXT  sing N N 126 
GLN   CB  CG   sing N N 127 
GLN   CB  HB2  sing N N 128 
GLN   CB  HB3  sing N N 129 
GLN   CG  CD   sing N N 130 
GLN   CG  HG2  sing N N 131 
GLN   CG  HG3  sing N N 132 
GLN   CD  OE1  doub N N 133 
GLN   CD  NE2  sing N N 134 
GLN   NE2 HE21 sing N N 135 
GLN   NE2 HE22 sing N N 136 
GLN   OXT HXT  sing N N 137 
GLU   N   CA   sing N N 138 
GLU   N   H    sing N N 139 
GLU   N   H2   sing N N 140 
GLU   CA  C    sing N N 141 
GLU   CA  CB   sing N N 142 
GLU   CA  HA   sing N N 143 
GLU   C   O    doub N N 144 
GLU   C   OXT  sing N N 145 
GLU   CB  CG   sing N N 146 
GLU   CB  HB2  sing N N 147 
GLU   CB  HB3  sing N N 148 
GLU   CG  CD   sing N N 149 
GLU   CG  HG2  sing N N 150 
GLU   CG  HG3  sing N N 151 
GLU   CD  OE1  doub N N 152 
GLU   CD  OE2  sing N N 153 
GLU   OE2 HE2  sing N N 154 
GLU   OXT HXT  sing N N 155 
GLY   N   CA   sing N N 156 
GLY   N   H    sing N N 157 
GLY   N   H2   sing N N 158 
GLY   CA  C    sing N N 159 
GLY   CA  HA2  sing N N 160 
GLY   CA  HA3  sing N N 161 
GLY   C   O    doub N N 162 
GLY   C   OXT  sing N N 163 
GLY   OXT HXT  sing N N 164 
HIS   N   CA   sing N N 165 
HIS   N   H    sing N N 166 
HIS   N   H2   sing N N 167 
HIS   CA  C    sing N N 168 
HIS   CA  CB   sing N N 169 
HIS   CA  HA   sing N N 170 
HIS   C   O    doub N N 171 
HIS   C   OXT  sing N N 172 
HIS   CB  CG   sing N N 173 
HIS   CB  HB2  sing N N 174 
HIS   CB  HB3  sing N N 175 
HIS   CG  ND1  sing Y N 176 
HIS   CG  CD2  doub Y N 177 
HIS   ND1 CE1  doub Y N 178 
HIS   ND1 HD1  sing N N 179 
HIS   CD2 NE2  sing Y N 180 
HIS   CD2 HD2  sing N N 181 
HIS   CE1 NE2  sing Y N 182 
HIS   CE1 HE1  sing N N 183 
HIS   NE2 HE2  sing N N 184 
HIS   OXT HXT  sing N N 185 
HOH   O   H1   sing N N 186 
HOH   O   H2   sing N N 187 
ILE   N   CA   sing N N 188 
ILE   N   H    sing N N 189 
ILE   N   H2   sing N N 190 
ILE   CA  C    sing N N 191 
ILE   CA  CB   sing N N 192 
ILE   CA  HA   sing N N 193 
ILE   C   O    doub N N 194 
ILE   C   OXT  sing N N 195 
ILE   CB  CG1  sing N N 196 
ILE   CB  CG2  sing N N 197 
ILE   CB  HB   sing N N 198 
ILE   CG1 CD1  sing N N 199 
ILE   CG1 HG12 sing N N 200 
ILE   CG1 HG13 sing N N 201 
ILE   CG2 HG21 sing N N 202 
ILE   CG2 HG22 sing N N 203 
ILE   CG2 HG23 sing N N 204 
ILE   CD1 HD11 sing N N 205 
ILE   CD1 HD12 sing N N 206 
ILE   CD1 HD13 sing N N 207 
ILE   OXT HXT  sing N N 208 
LEU   N   CA   sing N N 209 
LEU   N   H    sing N N 210 
LEU   N   H2   sing N N 211 
LEU   CA  C    sing N N 212 
LEU   CA  CB   sing N N 213 
LEU   CA  HA   sing N N 214 
LEU   C   O    doub N N 215 
LEU   C   OXT  sing N N 216 
LEU   CB  CG   sing N N 217 
LEU   CB  HB2  sing N N 218 
LEU   CB  HB3  sing N N 219 
LEU   CG  CD1  sing N N 220 
LEU   CG  CD2  sing N N 221 
LEU   CG  HG   sing N N 222 
LEU   CD1 HD11 sing N N 223 
LEU   CD1 HD12 sing N N 224 
LEU   CD1 HD13 sing N N 225 
LEU   CD2 HD21 sing N N 226 
LEU   CD2 HD22 sing N N 227 
LEU   CD2 HD23 sing N N 228 
LEU   OXT HXT  sing N N 229 
LYS   N   CA   sing N N 230 
LYS   N   H    sing N N 231 
LYS   N   H2   sing N N 232 
LYS   CA  C    sing N N 233 
LYS   CA  CB   sing N N 234 
LYS   CA  HA   sing N N 235 
LYS   C   O    doub N N 236 
LYS   C   OXT  sing N N 237 
LYS   CB  CG   sing N N 238 
LYS   CB  HB2  sing N N 239 
LYS   CB  HB3  sing N N 240 
LYS   CG  CD   sing N N 241 
LYS   CG  HG2  sing N N 242 
LYS   CG  HG3  sing N N 243 
LYS   CD  CE   sing N N 244 
LYS   CD  HD2  sing N N 245 
LYS   CD  HD3  sing N N 246 
LYS   CE  NZ   sing N N 247 
LYS   CE  HE2  sing N N 248 
LYS   CE  HE3  sing N N 249 
LYS   NZ  HZ1  sing N N 250 
LYS   NZ  HZ2  sing N N 251 
LYS   NZ  HZ3  sing N N 252 
LYS   OXT HXT  sing N N 253 
MET   N   CA   sing N N 254 
MET   N   H    sing N N 255 
MET   N   H2   sing N N 256 
MET   CA  C    sing N N 257 
MET   CA  CB   sing N N 258 
MET   CA  HA   sing N N 259 
MET   C   O    doub N N 260 
MET   C   OXT  sing N N 261 
MET   CB  CG   sing N N 262 
MET   CB  HB2  sing N N 263 
MET   CB  HB3  sing N N 264 
MET   CG  SD   sing N N 265 
MET   CG  HG2  sing N N 266 
MET   CG  HG3  sing N N 267 
MET   SD  CE   sing N N 268 
MET   CE  HE1  sing N N 269 
MET   CE  HE2  sing N N 270 
MET   CE  HE3  sing N N 271 
MET   OXT HXT  sing N N 272 
PHE   N   CA   sing N N 273 
PHE   N   H    sing N N 274 
PHE   N   H2   sing N N 275 
PHE   CA  C    sing N N 276 
PHE   CA  CB   sing N N 277 
PHE   CA  HA   sing N N 278 
PHE   C   O    doub N N 279 
PHE   C   OXT  sing N N 280 
PHE   CB  CG   sing N N 281 
PHE   CB  HB2  sing N N 282 
PHE   CB  HB3  sing N N 283 
PHE   CG  CD1  doub Y N 284 
PHE   CG  CD2  sing Y N 285 
PHE   CD1 CE1  sing Y N 286 
PHE   CD1 HD1  sing N N 287 
PHE   CD2 CE2  doub Y N 288 
PHE   CD2 HD2  sing N N 289 
PHE   CE1 CZ   doub Y N 290 
PHE   CE1 HE1  sing N N 291 
PHE   CE2 CZ   sing Y N 292 
PHE   CE2 HE2  sing N N 293 
PHE   CZ  HZ   sing N N 294 
PHE   OXT HXT  sing N N 295 
PRO   N   CA   sing N N 296 
PRO   N   CD   sing N N 297 
PRO   N   H    sing N N 298 
PRO   CA  C    sing N N 299 
PRO   CA  CB   sing N N 300 
PRO   CA  HA   sing N N 301 
PRO   C   O    doub N N 302 
PRO   C   OXT  sing N N 303 
PRO   CB  CG   sing N N 304 
PRO   CB  HB2  sing N N 305 
PRO   CB  HB3  sing N N 306 
PRO   CG  CD   sing N N 307 
PRO   CG  HG2  sing N N 308 
PRO   CG  HG3  sing N N 309 
PRO   CD  HD2  sing N N 310 
PRO   CD  HD3  sing N N 311 
PRO   OXT HXT  sing N N 312 
SER   N   CA   sing N N 313 
SER   N   H    sing N N 314 
SER   N   H2   sing N N 315 
SER   CA  C    sing N N 316 
SER   CA  CB   sing N N 317 
SER   CA  HA   sing N N 318 
SER   C   O    doub N N 319 
SER   C   OXT  sing N N 320 
SER   CB  OG   sing N N 321 
SER   CB  HB2  sing N N 322 
SER   CB  HB3  sing N N 323 
SER   OG  HG   sing N N 324 
SER   OXT HXT  sing N N 325 
TFA   C1  C2   sing N N 326 
TFA   C1  O    doub N N 327 
TFA   C1  OXT  sing N N 328 
TFA   C2  F1   sing N N 329 
TFA   C2  F2   sing N N 330 
TFA   C2  F3   sing N N 331 
TFA   OXT HXT  sing N N 332 
THR   N   CA   sing N N 333 
THR   N   H    sing N N 334 
THR   N   H2   sing N N 335 
THR   CA  C    sing N N 336 
THR   CA  CB   sing N N 337 
THR   CA  HA   sing N N 338 
THR   C   O    doub N N 339 
THR   C   OXT  sing N N 340 
THR   CB  OG1  sing N N 341 
THR   CB  CG2  sing N N 342 
THR   CB  HB   sing N N 343 
THR   OG1 HG1  sing N N 344 
THR   CG2 HG21 sing N N 345 
THR   CG2 HG22 sing N N 346 
THR   CG2 HG23 sing N N 347 
THR   OXT HXT  sing N N 348 
TYR   N   CA   sing N N 349 
TYR   N   H    sing N N 350 
TYR   N   H2   sing N N 351 
TYR   CA  C    sing N N 352 
TYR   CA  CB   sing N N 353 
TYR   CA  HA   sing N N 354 
TYR   C   O    doub N N 355 
TYR   C   OXT  sing N N 356 
TYR   CB  CG   sing N N 357 
TYR   CB  HB2  sing N N 358 
TYR   CB  HB3  sing N N 359 
TYR   CG  CD1  doub Y N 360 
TYR   CG  CD2  sing Y N 361 
TYR   CD1 CE1  sing Y N 362 
TYR   CD1 HD1  sing N N 363 
TYR   CD2 CE2  doub Y N 364 
TYR   CD2 HD2  sing N N 365 
TYR   CE1 CZ   doub Y N 366 
TYR   CE1 HE1  sing N N 367 
TYR   CE2 CZ   sing Y N 368 
TYR   CE2 HE2  sing N N 369 
TYR   CZ  OH   sing N N 370 
TYR   OH  HH   sing N N 371 
TYR   OXT HXT  sing N N 372 
VAL   N   CA   sing N N 373 
VAL   N   H    sing N N 374 
VAL   N   H2   sing N N 375 
VAL   CA  C    sing N N 376 
VAL   CA  CB   sing N N 377 
VAL   CA  HA   sing N N 378 
VAL   C   O    doub N N 379 
VAL   C   OXT  sing N N 380 
VAL   CB  CG1  sing N N 381 
VAL   CB  CG2  sing N N 382 
VAL   CB  HB   sing N N 383 
VAL   CG1 HG11 sing N N 384 
VAL   CG1 HG12 sing N N 385 
VAL   CG1 HG13 sing N N 386 
VAL   CG2 HG21 sing N N 387 
VAL   CG2 HG22 sing N N 388 
VAL   CG2 HG23 sing N N 389 
VAL   OXT HXT  sing N N 390 
# 
_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                    7HEJ 
_atom_sites.fract_transf_matrix[1][1]   0.011275 
_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]   0.011275 
_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]   0.025358 
_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 
F  
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    . VAL   A 1 3   ? 19.498 -16.178 22.239  1.00 48.24 ?  3   VAL   A N    1 
ATOM   2    C  CA   . VAL   A 1 3   ? 18.580 -15.062 22.435  1.00 47.61 ?  3   VAL   A CA   1 
ATOM   3    C  C    . VAL   A 1 3   ? 19.280 -13.746 22.114  1.00 44.96 ?  3   VAL   A C    1 
ATOM   4    O  O    . VAL   A 1 3   ? 20.398 -13.503 22.568  1.00 45.66 ?  3   VAL   A O    1 
ATOM   5    C  CB   . VAL   A 1 3   ? 17.996 -15.062 23.863  1.00 49.12 ?  3   VAL   A CB   1 
ATOM   6    C  CG1  . VAL   A 1 3   ? 16.975 -13.941 24.028  1.00 49.62 ?  3   VAL   A CG1  1 
ATOM   7    C  CG2  . VAL   A 1 3   ? 17.364 -16.411 24.174  1.00 49.58 ?  3   VAL   A CG2  1 
ATOM   8    H  HA   . VAL   A 1 3   ? 17.840 -15.153 21.821  1.00 57.14 ?  3   VAL   A HA   1 
ATOM   9    H  HB   . VAL   A 1 3   ? 18.710 -14.911 24.502  1.00 58.94 ?  3   VAL   A HB   1 
ATOM   10   H  HG11 . VAL   A 1 3   ? 16.520 -14.051 24.879  1.00 59.55 ?  3   VAL   A HG11 1 
ATOM   11   H  HG12 . VAL   A 1 3   ? 17.433 -13.087 24.008  1.00 59.55 ?  3   VAL   A HG12 1 
ATOM   12   H  HG13 . VAL   A 1 3   ? 16.332 -13.991 23.304  1.00 59.55 ?  3   VAL   A HG13 1 
ATOM   13   H  HG21 . VAL   A 1 3   ? 16.916 -16.361 25.033  1.00 59.50 ?  3   VAL   A HG21 1 
ATOM   14   H  HG22 . VAL   A 1 3   ? 16.723 -16.626 23.479  1.00 59.50 ?  3   VAL   A HG22 1 
ATOM   15   H  HG23 . VAL   A 1 3   ? 18.060 -17.086 24.202  1.00 59.50 ?  3   VAL   A HG23 1 
ATOM   16   N  N    A ASN   A 1 4   ? 18.601 -12.908 21.329  0.68 42.51 ?  4   ASN   A N    1 
ATOM   17   N  N    B ASN   A 1 4   ? 18.635 -12.902 21.317  0.32 43.54 ?  4   ASN   A N    1 
ATOM   18   C  CA   A ASN   A 1 4   ? 19.030 -11.546 21.037  0.68 39.68 ?  4   ASN   A CA   1 
ATOM   19   C  CA   B ASN   A 1 4   ? 19.232 -11.647 20.878  0.32 41.75 ?  4   ASN   A CA   1 
ATOM   20   C  C    A ASN   A 1 4   ? 17.853 -10.598 21.264  0.68 37.03 ?  4   ASN   A C    1 
ATOM   21   C  C    B ASN   A 1 4   ? 18.347 -10.472 21.294  0.32 39.64 ?  4   ASN   A C    1 
ATOM   22   O  O    A ASN   A 1 4   ? 16.742 -11.023 21.597  0.68 36.98 ?  4   ASN   A O    1 
ATOM   23   O  O    B ASN   A 1 4   ? 17.382 -10.625 22.050  0.32 39.72 ?  4   ASN   A O    1 
ATOM   24   C  CB   A ASN   A 1 4   ? 19.607 -11.424 19.619  0.68 39.19 ?  4   ASN   A CB   1 
ATOM   25   C  CB   B ASN   A 1 4   ? 19.497 -11.673 19.371  0.32 41.86 ?  4   ASN   A CB   1 
ATOM   26   C  CG   A ASN   A 1 4   ? 18.624 -11.844 18.546  0.68 38.58 ?  4   ASN   A CG   1 
ATOM   27   C  CG   B ASN   A 1 4   ? 18.257 -12.000 18.569  0.32 41.88 ?  4   ASN   A CG   1 
ATOM   28   O  OD1  A ASN   A 1 4   ? 17.479 -11.393 18.525  0.68 38.28 ?  4   ASN   A OD1  1 
ATOM   29   O  OD1  B ASN   A 1 4   ? 17.427 -11.131 18.303  0.32 41.87 ?  4   ASN   A OD1  1 
ATOM   30   N  ND2  A ASN   A 1 4   ? 19.069 -12.715 17.646  0.68 38.39 ?  4   ASN   A ND2  1 
ATOM   31   N  ND2  B ASN   A 1 4   ? 18.124 -13.262 18.177  0.32 41.92 ?  4   ASN   A ND2  1 
ATOM   32   H  H    A ASN   A 1 4   ? 17.861 -13.118 20.944  0.68 51.02 ?  4   ASN   A H    1 
ATOM   33   H  H    B ASN   A 1 4   ? 17.840 -13.037 21.015  0.32 52.26 ?  4   ASN   A H    1 
ATOM   34   H  HA   A ASN   A 1 4   ? 19.733 -11.305 21.655  0.68 47.62 ?  4   ASN   A HA   1 
ATOM   35   H  HA   B ASN   A 1 4   ? 20.089 -11.544 21.319  0.32 50.11 ?  4   ASN   A HA   1 
ATOM   36   H  HB2  A ASN   A 1 4   ? 19.852 -10.498 19.457  0.68 47.03 ?  4   ASN   A HB2  1 
ATOM   37   H  HB2  B ASN   A 1 4   ? 19.824 -10.804 19.087  0.32 50.24 ?  4   ASN   A HB2  1 
ATOM   38   H  HB3  A ASN   A 1 4   ? 20.390 -11.990 19.549  0.68 47.03 ?  4   ASN   A HB3  1 
ATOM   39   H  HB3  B ASN   A 1 4   ? 20.163 -12.351 19.185  0.32 50.24 ?  4   ASN   A HB3  1 
ATOM   40   H  HD21 A ASN   A 1 4   ? 18.553 -12.985 17.014  0.68 46.07 ?  4   ASN   A HD21 1 
ATOM   41   H  HD21 B ASN   A 1 4   ? 17.437 -13.498 17.720  0.32 50.31 ?  4   ASN   A HD21 1 
ATOM   42   H  HD22 A ASN   A 1 4   ? 19.878 -13.008 17.694  0.68 46.07 ?  4   ASN   A HD22 1 
ATOM   43   H  HD22 B ASN   A 1 4   ? 18.726 -13.842 18.382  0.32 50.31 ?  4   ASN   A HD22 1 
ATOM   44   N  N    A SER   A 1 5   ? 18.100 -9.301  21.076  0.68 34.27 ?  5   SER   A N    1 
ATOM   45   N  N    B SER   A 1 5   ? 18.683 -9.289  20.782  0.32 37.35 ?  5   SER   A N    1 
ATOM   46   C  CA   A SER   A 1 5   ? 17.155 -8.256  21.451  0.68 31.56 ?  5   SER   A CA   1 
ATOM   47   C  CA   B SER   A 1 5   ? 18.046 -8.043  21.184  0.32 34.95 ?  5   SER   A CA   1 
ATOM   48   C  C    A SER   A 1 5   ? 16.285 -7.777  20.290  0.68 28.63 ?  5   SER   A C    1 
ATOM   49   C  C    B SER   A 1 5   ? 16.971 -7.572  20.213  0.32 32.20 ?  5   SER   A C    1 
ATOM   50   O  O    A SER   A 1 5   ? 15.577 -6.775  20.436  0.68 28.79 ?  5   SER   A O    1 
ATOM   51   O  O    B SER   A 1 5   ? 16.320 -6.556  20.480  0.32 32.33 ?  5   SER   A O    1 
ATOM   52   C  CB   A SER   A 1 5   ? 17.896 -7.070  22.076  0.68 32.02 ?  5   SER   A CB   1 
ATOM   53   C  CB   B SER   A 1 5   ? 19.103 -6.946  21.365  0.32 35.24 ?  5   SER   A CB   1 
ATOM   54   O  OG   A SER   A 1 5   ? 18.814 -6.499  21.160  0.68 32.39 ?  5   SER   A OG   1 
ATOM   55   O  OG   B SER   A 1 5   ? 20.252 -7.207  20.577  0.32 35.40 ?  5   SER   A OG   1 
ATOM   56   H  H    A SER   A 1 5   ? 18.823 -8.999  20.721  0.68 41.13 ?  5   SER   A H    1 
ATOM   57   H  H    B SER   A 1 5   ? 19.287 -9.187  20.180  0.32 44.82 ?  5   SER   A H    1 
ATOM   58   H  HA   A SER   A 1 5   ? 16.563 -8.609  22.131  0.68 37.88 ?  5   SER   A HA   1 
ATOM   59   H  HA   B SER   A 1 5   ? 17.626 -8.181  22.045  0.32 41.95 ?  5   SER   A HA   1 
ATOM   60   H  HB2  A SER   A 1 5   ? 17.251 -6.391  22.331  0.68 38.42 ?  5   SER   A HB2  1 
ATOM   61   H  HB2  B SER   A 1 5   ? 18.728 -6.097  21.084  0.32 42.30 ?  5   SER   A HB2  1 
ATOM   62   H  HB3  A SER   A 1 5   ? 18.379 -7.375  22.864  0.68 38.42 ?  5   SER   A HB3  1 
ATOM   63   H  HB3  B SER   A 1 5   ? 19.354 -6.901  22.302  0.32 42.30 ?  5   SER   A HB3  1 
ATOM   64   H  HG   A SER   A 1 5   ? 19.220 -5.856  21.522  0.68 38.87 ?  5   SER   A HG   1 
ATOM   65   H  HG   B SER   A 1 5   ? 20.829 -6.608  20.702  0.32 42.48 ?  5   SER   A HG   1 
ATOM   66   N  N    A PHE   A 1 6   ? 16.310 -8.462  19.151  0.68 25.33 ?  6   PHE   A N    1 
ATOM   67   N  N    B PHE   A 1 6   ? 16.768 -8.272  19.100  0.32 29.19 ?  6   PHE   A N    1 
ATOM   68   C  CA   A PHE   A 1 6   ? 15.442 -8.085  18.041  0.68 22.24 ?  6   PHE   A CA   1 
ATOM   69   C  CA   B PHE   A 1 6   ? 15.712 -7.898  18.170  0.32 26.18 ?  6   PHE   A CA   1 
ATOM   70   C  C    A PHE   A 1 6   ? 13.996 -8.438  18.372  0.68 21.64 ?  6   PHE   A C    1 
ATOM   71   C  C    B PHE   A 1 6   ? 14.350 -8.291  18.730  0.32 25.30 ?  6   PHE   A C    1 
ATOM   72   O  O    A PHE   A 1 6   ? 13.713 -9.547  18.830  0.68 22.41 ?  6   PHE   A O    1 
ATOM   73   O  O    B PHE   A 1 6   ? 14.221 -9.243  19.505  0.32 25.54 ?  6   PHE   A O    1 
ATOM   74   C  CB   A PHE   A 1 6   ? 15.880 -8.804  16.770  0.68 20.57 ?  6   PHE   A CB   1 
ATOM   75   C  CB   B PHE   A 1 6   ? 15.936 -8.572  16.817  0.32 24.19 ?  6   PHE   A CB   1 
ATOM   76   C  CG   A PHE   A 1 6   ? 17.164 -8.273  16.190  0.68 19.26 ?  6   PHE   A CG   1 
ATOM   77   C  CG   B PHE   A 1 6   ? 17.217 -8.164  16.144  0.32 22.40 ?  6   PHE   A CG   1 
ATOM   78   C  CD1  A PHE   A 1 6   ? 17.169 -7.104  15.449  0.68 18.57 ?  6   PHE   A CD1  1 
ATOM   79   C  CD1  B PHE   A 1 6   ? 17.306 -6.955  15.475  0.32 21.58 ?  6   PHE   A CD1  1 
ATOM   80   C  CD2  A PHE   A 1 6   ? 18.357 -8.945  16.385  0.68 19.91 ?  6   PHE   A CD2  1 
ATOM   81   C  CD2  B PHE   A 1 6   ? 18.330 -8.987  16.181  0.32 21.87 ?  6   PHE   A CD2  1 
ATOM   82   C  CE1  A PHE   A 1 6   ? 18.342 -6.611  14.913  0.68 18.69 ?  6   PHE   A CE1  1 
ATOM   83   C  CE1  B PHE   A 1 6   ? 18.481 -6.573  14.855  0.32 21.24 ?  6   PHE   A CE1  1 
ATOM   84   C  CE2  A PHE   A 1 6   ? 19.531 -8.461  15.850  0.68 19.97 ?  6   PHE   A CE2  1 
ATOM   85   C  CE2  B PHE   A 1 6   ? 19.508 -8.613  15.562  0.32 21.45 ?  6   PHE   A CE2  1 
ATOM   86   C  CZ   A PHE   A 1 6   ? 19.523 -7.289  15.113  0.68 19.17 ?  6   PHE   A CZ   1 
ATOM   87   C  CZ   B PHE   A 1 6   ? 19.584 -7.402  14.899  0.32 21.19 ?  6   PHE   A CZ   1 
ATOM   88   H  H    A PHE   A 1 6   ? 16.805 -9.150  19.003  0.68 30.40 ?  6   PHE   A H    1 
ATOM   89   H  H    B PHE   A 1 6   ? 17.226 -8.959  18.860  0.32 35.03 ?  6   PHE   A H    1 
ATOM   90   H  HA   A PHE   A 1 6   ? 15.495 -7.135  17.901  0.68 26.70 ?  6   PHE   A HA   1 
ATOM   91   H  HA   B PHE   A 1 6   ? 15.724 -6.938  18.039  0.32 31.42 ?  6   PHE   A HA   1 
ATOM   92   H  HB2  A PHE   A 1 6   ? 16.006 -9.748  16.974  0.68 24.69 ?  6   PHE   A HB2  1 
ATOM   93   H  HB2  B PHE   A 1 6   ? 15.962 -9.533  16.946  0.32 29.03 ?  6   PHE   A HB2  1 
ATOM   94   H  HB3  A PHE   A 1 6   ? 15.182 -8.708  16.104  0.68 24.69 ?  6   PHE   A HB3  1 
ATOM   95   H  HB3  B PHE   A 1 6   ? 15.203 -8.339  16.226  0.32 29.03 ?  6   PHE   A HB3  1 
ATOM   96   H  HD1  A PHE   A 1 6   ? 16.367 -6.649  15.315  0.68 22.28 ?  6   PHE   A HD1  1 
ATOM   97   H  HD1  B PHE   A 1 6   ? 16.565 -6.394  15.444  0.32 25.90 ?  6   PHE   A HD1  1 
ATOM   98   H  HD2  A PHE   A 1 6   ? 18.366 -9.735  16.884  0.68 23.89 ?  6   PHE   A HD2  1 
ATOM   99   H  HD2  B PHE   A 1 6   ? 18.285 -9.802  16.627  0.32 26.25 ?  6   PHE   A HD2  1 
ATOM   100  H  HE1  A PHE   A 1 6   ? 18.328 -5.827  14.418  0.68 22.43 ?  6   PHE   A HE1  1 
ATOM   101  H  HE1  B PHE   A 1 6   ? 18.529 -5.759  14.409  0.32 25.50 ?  6   PHE   A HE1  1 
ATOM   102  H  HE2  A PHE   A 1 6   ? 20.330 -8.916  15.989  0.68 23.97 ?  6   PHE   A HE2  1 
ATOM   103  H  HE2  B PHE   A 1 6   ? 20.251 -9.173  15.595  0.32 25.74 ?  6   PHE   A HE2  1 
ATOM   104  H  HZ   A PHE   A 1 6   ? 20.312 -6.959  14.754  0.68 23.00 ?  6   PHE   A HZ   1 
ATOM   105  H  HZ   B PHE   A 1 6   ? 20.376 -7.147  14.483  0.32 25.43 ?  6   PHE   A HZ   1 
ATOM   106  N  N    A SER   A 1 7   ? 13.075 -7.499  18.131  0.68 20.67 ?  7   SER   A N    1 
ATOM   107  N  N    B SER   A 1 7   ? 13.322 -7.544  18.330  0.32 24.13 ?  7   SER   A N    1 
ATOM   108  C  CA   A SER   A 1 7   ? 11.695 -7.610  18.596  0.68 20.72 ?  7   SER   A CA   1 
ATOM   109  C  CA   B SER   A 1 7   ? 11.988 -7.740  18.876  0.32 23.25 ?  7   SER   A CA   1 
ATOM   110  C  C    A SER   A 1 7   ? 10.705 -7.396  17.457  0.68 18.91 ?  7   SER   A C    1 
ATOM   111  C  C    B SER   A 1 7   ? 10.953 -7.313  17.846  0.32 21.60 ?  7   SER   A C    1 
ATOM   112  O  O    A SER   A 1 7   ? 10.899 -6.524  16.606  0.68 19.09 ?  7   SER   A O    1 
ATOM   113  O  O    B SER   A 1 7   ? 11.172 -6.359  17.095  0.32 21.59 ?  7   SER   A O    1 
ATOM   114  C  CB   A SER   A 1 7   ? 11.426 -6.573  19.699  0.68 22.73 ?  7   SER   A CB   1 
ATOM   115  C  CB   B SER   A 1 7   ? 11.811 -6.929  20.165  0.32 23.93 ?  7   SER   A CB   1 
ATOM   116  O  OG   A SER   A 1 7   ? 10.081 -6.618  20.135  0.68 24.15 ?  7   SER   A OG   1 
ATOM   117  O  OG   B SER   A 1 7   ? 10.620 -7.289  20.842  0.32 24.44 ?  7   SER   A OG   1 
ATOM   118  H  H    A SER   A 1 7   ? 13.232 -6.785  17.682  0.68 24.81 ?  7   SER   A H    1 
ATOM   119  H  H    B SER   A 1 7   ? 13.373 -6.917  17.740  0.32 28.96 ?  7   SER   A H    1 
ATOM   120  H  HA   A SER   A 1 7   ? 11.546 -8.493  18.965  0.68 24.87 ?  7   SER   A HA   1 
ATOM   121  H  HA   B SER   A 1 7   ? 11.853 -8.678  19.079  0.32 27.91 ?  7   SER   A HA   1 
ATOM   122  H  HB2  A SER   A 1 7   ? 12.012 -6.758  20.451  0.68 27.28 ?  7   SER   A HB2  1 
ATOM   123  H  HB2  B SER   A 1 7   ? 12.572 -7.093  20.746  0.32 28.73 ?  7   SER   A HB2  1 
ATOM   124  H  HB3  A SER   A 1 7   ? 11.609 -5.688  19.349  0.68 27.28 ?  7   SER   A HB3  1 
ATOM   125  H  HB3  B SER   A 1 7   ? 11.768 -5.986  19.940  0.32 28.73 ?  7   SER   A HB3  1 
ATOM   126  H  HG   A SER   A 1 7   ? 9.956  -6.052  20.744  0.68 28.99 ?  7   SER   A HG   1 
ATOM   127  H  HG   B SER   A 1 7   ? 10.547 -6.840  21.549  0.32 29.34 ?  7   SER   A HG   1 
ATOM   128  N  N    A GLY   A 1 8   ? 9.630  -8.186  17.455  0.68 17.27 ?  8   GLY   A N    1 
ATOM   129  N  N    B GLY   A 1 8   ? 9.831  -8.032  17.813  0.32 19.97 ?  8   GLY   A N    1 
ATOM   130  C  CA   A GLY   A 1 8   ? 8.544  -7.978  16.516  0.68 16.22 ?  8   GLY   A CA   1 
ATOM   131  C  CA   B GLY   A 1 8   ? 8.742  -7.698  16.920  0.32 18.38 ?  8   GLY   A CA   1 
ATOM   132  C  C    A GLY   A 1 8   ? 8.774  -8.489  15.113  0.68 14.96 ?  8   GLY   A C    1 
ATOM   133  C  C    B GLY   A 1 8   ? 8.864  -8.241  15.517  0.32 16.53 ?  8   GLY   A C    1 
ATOM   134  O  O    A GLY   A 1 8   ? 8.039  -8.097  14.199  0.68 15.75 ?  8   GLY   A O    1 
ATOM   135  O  O    B GLY   A 1 8   ? 8.048  -7.881  14.661  0.32 16.79 ?  8   GLY   A O    1 
ATOM   136  H  H    A GLY   A 1 8   ? 9.511  -8.845  17.992  0.68 20.73 ?  8   GLY   A H    1 
ATOM   137  H  H    B GLY   A 1 8   ? 9.682  -8.725  18.299  0.32 23.96 ?  8   GLY   A H    1 
ATOM   138  H  HA2  A GLY   A 1 8   ? 7.747  -8.409  16.864  0.68 19.47 ?  8   GLY   A HA2  1 
ATOM   139  H  HA2  B GLY   A 1 8   ? 7.914  -8.039  17.289  0.32 22.07 ?  8   GLY   A HA2  1 
ATOM   140  H  HA3  A GLY   A 1 8   ? 8.364  -7.029  16.451  0.68 19.47 ?  8   GLY   A HA3  1 
ATOM   141  H  HA3  B GLY   A 1 8   ? 8.669  -6.733  16.857  0.32 22.07 ?  8   GLY   A HA3  1 
ATOM   142  N  N    A TYR   A 1 9   ? 9.762  -9.360  14.905  0.68 14.18 ?  9   TYR   A N    1 
ATOM   143  N  N    B TYR   A 1 9   ? 9.847  -9.094  15.249  0.32 14.89 ?  9   TYR   A N    1 
ATOM   144  C  CA   A TYR   A 1 9   ? 10.044 -9.907  13.586  0.68 13.52 ?  9   TYR   A CA   1 
ATOM   145  C  CA   B TYR   A 1 9   ? 10.055 -9.620  13.909  0.32 13.69 ?  9   TYR   A CA   1 
ATOM   146  C  C    A TYR   A 1 9   ? 9.191  -11.137 13.307  0.68 12.79 ?  9   TYR   A C    1 
ATOM   147  C  C    B TYR   A 1 9   ? 9.185  -10.844 13.659  0.32 12.79 ?  9   TYR   A C    1 
ATOM   148  O  O    A TYR   A 1 9   ? 8.939  -11.960 14.194  0.68 13.84 ?  9   TYR   A O    1 
ATOM   149  O  O    B TYR   A 1 9   ? 8.898  -11.632 14.566  0.32 13.68 ?  9   TYR   A O    1 
ATOM   150  C  CB   A TYR   A 1 9   ? 11.523 -10.291 13.450  0.68 14.16 ?  9   TYR   A CB   1 
ATOM   151  C  CB   B TYR   A 1 9   ? 11.526 -9.992  13.700  0.32 14.10 ?  9   TYR   A CB   1 
ATOM   152  C  CG   A TYR   A 1 9   ? 12.444 -9.103  13.314  0.68 14.48 ?  9   TYR   A CG   1 
ATOM   153  C  CG   B TYR   A 1 9   ? 12.410 -8.796  13.441  0.32 14.17 ?  9   TYR   A CG   1 
ATOM   154  C  CD1  A TYR   A 1 9   ? 12.801 -8.354  14.425  0.68 14.80 ?  9   TYR   A CD1  1 
ATOM   155  C  CD1  B TYR   A 1 9   ? 12.658 -7.870  14.442  0.32 14.33 ?  9   TYR   A CD1  1 
ATOM   156  C  CD2  A TYR   A 1 9   ? 12.938 -8.721  12.073  0.68 14.95 ?  9   TYR   A CD2  1 
ATOM   157  C  CD2  B TYR   A 1 9   ? 12.982 -8.587  12.193  0.32 14.13 ?  9   TYR   A CD2  1 
ATOM   158  C  CE1  A TYR   A 1 9   ? 13.625 -7.258  14.308  0.68 15.67 ?  9   TYR   A CE1  1 
ATOM   159  C  CE1  B TYR   A 1 9   ? 13.453 -6.768  14.212  0.32 14.49 ?  9   TYR   A CE1  1 
ATOM   160  C  CE2  A TYR   A 1 9   ? 13.765 -7.628  11.946  0.68 15.38 ?  9   TYR   A CE2  1 
ATOM   161  C  CE2  B TYR   A 1 9   ? 13.782 -7.486  11.953  0.32 14.14 ?  9   TYR   A CE2  1 
ATOM   162  C  CZ   A TYR   A 1 9   ? 14.100 -6.901  13.065  0.68 16.09 ?  9   TYR   A CZ   1 
ATOM   163  C  CZ   B TYR   A 1 9   ? 14.011 -6.580  12.967  0.32 14.36 ?  9   TYR   A CZ   1 
ATOM   164  O  OH   A TYR   A 1 9   ? 14.917 -5.813  12.930  0.68 17.16 ?  9   TYR   A OH   1 
ATOM   165  O  OH   B TYR   A 1 9   ? 14.799 -5.479  12.737  0.32 14.55 ?  9   TYR   A OH   1 
ATOM   166  H  H    A TYR   A 1 9   ? 10.272 -9.668  15.521  0.68 17.02 ?  9   TYR   A H    1 
ATOM   167  H  H    B TYR   A 1 9   ? 10.414 -9.387  15.831  0.32 17.87 ?  9   TYR   A H    1 
ATOM   168  H  HA   A TYR   A 1 9   ? 9.842  -9.246  12.909  0.68 16.23 ?  9   TYR   A HA   1 
ATOM   169  H  HA   B TYR   A 1 9   ? 9.823  -8.934  13.260  0.32 16.43 ?  9   TYR   A HA   1 
ATOM   170  H  HB2  A TYR   A 1 9   ? 11.796 -10.796 14.233  0.68 17.00 ?  9   TYR   A HB2  1 
ATOM   171  H  HB2  B TYR   A 1 9   ? 11.853 -10.446 14.492  0.32 16.93 ?  9   TYR   A HB2  1 
ATOM   172  H  HB3  A TYR   A 1 9   ? 11.625 -10.839 12.655  0.68 17.00 ?  9   TYR   A HB3  1 
ATOM   173  H  HB3  B TYR   A 1 9   ? 11.588 -10.582 12.932  0.32 16.93 ?  9   TYR   A HB3  1 
ATOM   174  H  HD1  A TYR   A 1 9   ? 12.472 -8.594  15.263  0.68 17.77 ?  9   TYR   A HD1  1 
ATOM   175  H  HD1  B TYR   A 1 9   ? 12.281 -7.996  15.282  0.32 17.20 ?  9   TYR   A HD1  1 
ATOM   176  H  HD2  A TYR   A 1 9   ? 12.707 -9.212  11.316  0.68 17.94 ?  9   TYR   A HD2  1 
ATOM   177  H  HD2  B TYR   A 1 9   ? 12.824 -9.198  11.508  0.32 16.97 ?  9   TYR   A HD2  1 
ATOM   178  H  HE1  A TYR   A 1 9   ? 13.860 -6.765  15.060  0.68 18.81 ?  9   TYR   A HE1  1 
ATOM   179  H  HE1  B TYR   A 1 9   ? 13.616 -6.157  14.894  0.32 17.39 ?  9   TYR   A HE1  1 
ATOM   180  H  HE2  A TYR   A 1 9   ? 14.096 -7.383  11.109  0.68 18.47 ?  9   TYR   A HE2  1 
ATOM   181  H  HE2  B TYR   A 1 9   ? 14.163 -7.357  11.113  0.32 16.97 ?  9   TYR   A HE2  1 
ATOM   182  H  HH   A TYR   A 1 9   ? 15.070 -5.465  13.679  0.68 20.60 ?  9   TYR   A HH   1 
ATOM   183  H  HH   B TYR   A 1 9   ? 14.862 -5.019  13.438  0.32 17.46 ?  9   TYR   A HH   1 
ATOM   184  N  N    A LEU   A 1 10  ? 8.779  -11.269 12.052  0.68 12.40 ?  10  LEU   A N    1 
ATOM   185  N  N    B LEU   A 1 10  ? 8.754  -10.984 12.408  0.32 11.99 ?  10  LEU   A N    1 
ATOM   186  C  CA   A LEU   A 1 10  ? 8.194  -12.503 11.557  0.68 11.93 ?  10  LEU   A CA   1 
ATOM   187  C  CA   B LEU   A 1 10  ? 8.095  -12.192 11.936  0.32 11.88 ?  10  LEU   A CA   1 
ATOM   188  C  C    A LEU   A 1 10  ? 9.319  -13.439 11.133  0.68 12.03 ?  10  LEU   A C    1 
ATOM   189  C  C    B LEU   A 1 10  ? 9.170  -13.157 11.450  0.32 11.61 ?  10  LEU   A C    1 
ATOM   190  O  O    A LEU   A 1 10  ? 10.275 -13.019 10.477  0.68 12.67 ?  10  LEU   A O    1 
ATOM   191  O  O    B LEU   A 1 10  ? 10.044 -12.776 10.665  0.32 11.64 ?  10  LEU   A O    1 
ATOM   192  C  CB   A LEU   A 1 10  ? 7.316  -12.192 10.347  0.68 12.78 ?  10  LEU   A CB   1 
ATOM   193  C  CB   B LEU   A 1 10  ? 7.139  -11.846 10.794  0.32 12.09 ?  10  LEU   A CB   1 
ATOM   194  C  CG   A LEU   A 1 10  ? 6.623  -13.376 9.673   0.68 14.93 ?  10  LEU   A CG   1 
ATOM   195  C  CG   B LEU   A 1 10  ? 6.406  -13.027 10.164  0.32 13.01 ?  10  LEU   A CG   1 
ATOM   196  C  CD1  A LEU   A 1 10  ? 5.564  -13.954 10.590  0.68 15.97 ?  10  LEU   A CD1  1 
ATOM   197  C  CD1  B LEU   A 1 10  ? 5.370  -13.583 11.131  0.32 14.17 ?  10  LEU   A CD1  1 
ATOM   198  C  CD2  A LEU   A 1 10  ? 6.022  -12.975 8.332   0.68 16.24 ?  10  LEU   A CD2  1 
ATOM   199  C  CD2  B LEU   A 1 10  ? 5.760  -12.603 8.860   0.32 14.04 ?  10  LEU   A CD2  1 
ATOM   200  H  H    A LEU   A 1 10  ? 8.843  -10.657 11.446  0.68 14.88 ?  10  LEU   A H    1 
ATOM   201  H  H    B LEU   A 1 10  ? 8.834  -10.375 11.800  0.32 14.40 ?  10  LEU   A H    1 
ATOM   202  H  HA   A LEU   A 1 10  ? 7.662  -12.930 12.249  0.68 14.33 ?  10  LEU   A HA   1 
ATOM   203  H  HA   B LEU   A 1 10  ? 7.588  -12.603 12.655  0.32 14.26 ?  10  LEU   A HA   1 
ATOM   204  H  HB2  A LEU   A 1 10  ? 6.621  -11.585 10.627  0.68 15.34 ?  10  LEU   A HB2  1 
ATOM   205  H  HB2  B LEU   A 1 10  ? 6.457  -11.233 11.128  0.32 14.51 ?  10  LEU   A HB2  1 
ATOM   206  H  HB3  A LEU   A 1 10  ? 7.869  -11.773 9.674   0.68 15.34 ?  10  LEU   A HB3  1 
ATOM   207  H  HB3  B LEU   A 1 10  ? 7.641  -11.408 10.090  0.32 14.51 ?  10  LEU   A HB3  1 
ATOM   208  H  HG   A LEU   A 1 10  ? 7.276  -14.079 9.503   0.68 17.92 ?  10  LEU   A HG   1 
ATOM   209  H  HG   B LEU   A 1 10  ? 7.043  -13.732 9.970   0.32 15.62 ?  10  LEU   A HG   1 
ATOM   210  H  HD11 A LEU   A 1 10  ? 5.168  -14.735 10.172  0.68 19.18 ?  10  LEU   A HD11 1 
ATOM   211  H  HD11 B LEU   A 1 10  ? 4.916  -14.331 10.712  0.32 17.01 ?  10  LEU   A HD11 1 
ATOM   212  H  HD12 A LEU   A 1 10  ? 5.973  -14.203 11.433  0.68 19.18 ?  10  LEU   A HD12 1 
ATOM   213  H  HD12 B LEU   A 1 10  ? 5.815  -13.879 11.941  0.32 17.01 ?  10  LEU   A HD12 1 
ATOM   214  H  HD13 A LEU   A 1 10  ? 4.881  -13.280 10.744  0.68 19.18 ?  10  LEU   A HD13 1 
ATOM   215  H  HD13 B LEU   A 1 10  ? 4.730  -12.885 11.343  0.32 17.01 ?  10  LEU   A HD13 1 
ATOM   216  H  HD21 A LEU   A 1 10  ? 5.590  -13.749 7.935   0.68 19.49 ?  10  LEU   A HD21 1 
ATOM   217  H  HD21 B LEU   A 1 10  ? 5.507  -13.397 8.366   0.32 16.85 ?  10  LEU   A HD21 1 
ATOM   218  H  HD22 A LEU   A 1 10  ? 5.371  -12.273 8.480   0.68 19.49 ?  10  LEU   A HD22 1 
ATOM   219  H  HD22 B LEU   A 1 10  ? 4.975  -12.072 9.058   0.32 16.85 ?  10  LEU   A HD22 1 
ATOM   220  H  HD23 A LEU   A 1 10  ? 6.731  -12.658 7.753   0.68 19.49 ?  10  LEU   A HD23 1 
ATOM   221  H  HD23 B LEU   A 1 10  ? 6.396  -12.082 8.346   0.32 16.85 ?  10  LEU   A HD23 1 
ATOM   222  N  N    A LYS   A 1 11  ? 9.211  -14.708 11.517  0.68 12.09 ?  11  LYS   A N    1 
ATOM   223  N  N    B LYS   A 1 11  ? 9.122  -14.393 11.934  0.32 11.71 ?  11  LYS   A N    1 
ATOM   224  C  CA   A LYS   A 1 11  ? 10.214 -15.710 11.188  0.68 12.16 ?  11  LYS   A CA   1 
ATOM   225  C  CA   B LYS   A 1 11  ? 10.087 -15.407 11.531  0.32 11.59 ?  11  LYS   A CA   1 
ATOM   226  C  C    A LYS   A 1 11  ? 9.865  -16.311 9.837   0.68 12.09 ?  11  LYS   A C    1 
ATOM   227  C  C    B LYS   A 1 11  ? 9.700  -15.947 10.160  0.32 10.92 ?  11  LYS   A C    1 
ATOM   228  O  O    A LYS   A 1 11  ? 8.796  -16.906 9.684   0.68 13.69 ?  11  LYS   A O    1 
ATOM   229  O  O    B LYS   A 1 11  ? 8.574  -16.419 9.969   0.32 11.14 ?  11  LYS   A O    1 
ATOM   230  C  CB   A LYS   A 1 11  ? 10.246 -16.783 12.275  0.68 12.66 ?  11  LYS   A CB   1 
ATOM   231  C  CB   B LYS   A 1 11  ? 10.123 -16.530 12.567  0.32 11.96 ?  11  LYS   A CB   1 
ATOM   232  C  CG   A LYS   A 1 11  ? 11.254 -17.896 12.071  0.68 13.13 ?  11  LYS   A CG   1 
ATOM   233  C  CG   B LYS   A 1 11  ? 11.184 -17.604 12.317  0.32 12.16 ?  11  LYS   A CG   1 
ATOM   234  C  CD   A LYS   A 1 11  ? 11.326 -18.737 13.346  0.68 13.99 ?  11  LYS   A CD   1 
ATOM   235  C  CD   B LYS   A 1 11  ? 11.263 -18.593 13.483  0.32 12.71 ?  11  LYS   A CD   1 
ATOM   236  C  CE   A LYS   A 1 11  ? 12.315 -19.884 13.251  0.68 14.05 ?  11  LYS   A CE   1 
ATOM   237  C  CE   B LYS   A 1 11  ? 12.317 -19.681 13.261  0.32 12.96 ?  11  LYS   A CE   1 
ATOM   238  N  NZ   A LYS   A 1 11  ? 13.684 -19.407 12.931  0.68 14.10 ?  11  LYS   A NZ   1 
ATOM   239  N  NZ   B LYS   A 1 11  ? 13.709 -19.147 13.242  0.32 12.92 ?  11  LYS   A NZ   1 
ATOM   240  H  H    A LYS   A 1 11  ? 8.544  -15.028 11.962  0.68 14.52 ?  11  LYS   A H    1 
ATOM   241  H  H    B LYS   A 1 11  ? 8.538  -14.664 12.501  0.32 14.05 ?  11  LYS   A H    1 
ATOM   242  H  HA   A LYS   A 1 11  ? 11.088 -15.298 11.130  0.68 14.60 ?  11  LYS   A HA   1 
ATOM   243  H  HA   B LYS   A 1 11  ? 10.966 -15.006 11.467  0.32 13.91 ?  11  LYS   A HA   1 
ATOM   244  H  HB2  A LYS   A 1 11  ? 10.460 -16.355 13.119  0.68 15.20 ?  11  LYS   A HB2  1 
ATOM   245  H  HB2  B LYS   A 1 11  ? 10.300 -16.134 13.434  0.32 14.36 ?  11  LYS   A HB2  1 
ATOM   246  H  HB3  A LYS   A 1 11  ? 9.371  -17.192 12.333  0.68 15.20 ?  11  LYS   A HB3  1 
ATOM   247  H  HB3  B LYS   A 1 11  ? 9.257  -16.963 12.576  0.32 14.36 ?  11  LYS   A HB3  1 
ATOM   248  H  HG2  A LYS   A 1 11  ? 10.970 -18.470 11.338  0.68 15.76 ?  11  LYS   A HG2  1 
ATOM   249  H  HG2  B LYS   A 1 11  ? 10.953 -18.099 11.516  0.32 14.60 ?  11  LYS   A HG2  1 
ATOM   250  H  HG3  A LYS   A 1 11  ? 12.131 -17.525 11.895  0.68 15.76 ?  11  LYS   A HG3  1 
ATOM   251  H  HG3  B LYS   A 1 11  ? 12.050 -17.183 12.216  0.32 14.60 ?  11  LYS   A HG3  1 
ATOM   252  H  HD2  A LYS   A 1 11  ? 11.594 -18.170 14.083  0.68 16.79 ?  11  LYS   A HD2  1 
ATOM   253  H  HD2  B LYS   A 1 11  ? 11.494 -18.113 14.293  0.32 15.25 ?  11  LYS   A HD2  1 
ATOM   254  H  HD3  A LYS   A 1 11  ? 10.447 -19.116 13.523  0.68 16.79 ?  11  LYS   A HD3  1 
ATOM   255  H  HD3  B LYS   A 1 11  ? 10.402 -19.029 13.589  0.32 15.25 ?  11  LYS   A HD3  1 
ATOM   256  H  HE2  A LYS   A 1 11  ? 12.347 -20.348 14.103  0.68 16.86 ?  11  LYS   A HE2  1 
ATOM   257  H  HE2  B LYS   A 1 11  ? 12.260 -20.333 13.979  0.32 15.56 ?  11  LYS   A HE2  1 
ATOM   258  H  HE3  A LYS   A 1 11  ? 12.033 -20.491 12.550  0.68 16.86 ?  11  LYS   A HE3  1 
ATOM   259  H  HE3  B LYS   A 1 11  ? 12.154 -20.116 12.409  0.32 15.56 ?  11  LYS   A HE3  1 
ATOM   260  H  HZ1  A LYS   A 1 11  ? 14.245 -20.096 12.890  0.68 16.93 ?  11  LYS   A HZ1  1 
ATOM   261  H  HZ1  B LYS   A 1 11  ? 14.290 -19.809 13.106  0.32 15.50 ?  11  LYS   A HZ1  1 
ATOM   262  H  HZ2  A LYS   A 1 11  ? 13.685 -18.987 12.146  0.68 16.93 ?  11  LYS   A HZ2  1 
ATOM   263  H  HZ2  B LYS   A 1 11  ? 13.796 -18.550 12.587  0.32 15.50 ?  11  LYS   A HZ2  1 
ATOM   264  H  HZ3  A LYS   A 1 11  ? 13.966 -18.843 13.560  0.68 16.93 ?  11  LYS   A HZ3  1 
ATOM   265  H  HZ3  B LYS   A 1 11  ? 13.895 -18.754 14.018  0.32 15.50 ?  11  LYS   A HZ3  1 
ATOM   266  N  N    A LEU   A 1 12  ? 10.759 -16.168 8.860   0.68 11.27 ?  12  LEU   A N    1 
ATOM   267  N  N    B LEU   A 1 12  ? 10.617 -15.854 9.198   0.32 10.83 ?  12  LEU   A N    1 
ATOM   268  C  CA   A LEU   A 1 12  ? 10.506 -16.756 7.548   0.68 11.61 ?  12  LEU   A CA   1 
ATOM   269  C  CA   B LEU   A 1 12  ? 10.369 -16.363 7.854   0.32 10.81 ?  12  LEU   A CA   1 
ATOM   270  C  C    A LEU   A 1 12  ? 11.104 -18.150 7.410   0.68 11.59 ?  12  LEU   A C    1 
ATOM   271  C  C    B LEU   A 1 12  ? 10.924 -17.766 7.655   0.32 10.84 ?  12  LEU   A C    1 
ATOM   272  O  O    A LEU   A 1 12  ? 10.485 -19.028 6.800   0.68 11.80 ?  12  LEU   A O    1 
ATOM   273  O  O    B LEU   A 1 12  ? 10.254 -18.631 7.083   0.32 11.01 ?  12  LEU   A O    1 
ATOM   274  C  CB   A LEU   A 1 12  ? 11.049 -15.857 6.432   0.68 11.73 ?  12  LEU   A CB   1 
ATOM   275  C  CB   B LEU   A 1 12  ? 10.965 -15.417 6.803   0.32 11.64 ?  12  LEU   A CB   1 
ATOM   276  C  CG   A LEU   A 1 12  ? 10.391 -14.487 6.257   0.68 12.49 ?  12  LEU   A CG   1 
ATOM   277  C  CG   B LEU   A 1 12  ? 10.268 -14.065 6.658   0.32 12.46 ?  12  LEU   A CG   1 
ATOM   278  C  CD1  A LEU   A 1 12  ? 11.128 -13.705 5.190   0.68 13.05 ?  12  LEU   A CD1  1 
ATOM   279  C  CD1  B LEU   A 1 12  ? 10.787 -13.319 5.437   0.32 13.04 ?  12  LEU   A CD1  1 
ATOM   280  C  CD2  A LEU   A 1 12  ? 8.913  -14.625 5.905   0.68 13.29 ?  12  LEU   A CD2  1 
ATOM   281  C  CD2  B LEU   A 1 12  ? 8.766  -14.259 6.572   0.32 12.84 ?  12  LEU   A CD2  1 
ATOM   282  H  H    A LEU   A 1 12  ? 11.511 -15.745 8.927   0.68 13.53 ?  12  LEU   A H    1 
ATOM   283  H  H    B LEU   A 1 12  ? 11.397 -15.489 9.299   0.32 13.00 ?  12  LEU   A H    1 
ATOM   284  H  HA   A LEU   A 1 12  ? 9.552  -16.840 7.427   0.68 13.94 ?  12  LEU   A HA   1 
ATOM   285  H  HA   B LEU   A 1 12  ? 9.411  -16.406 7.714   0.32 12.97 ?  12  LEU   A HA   1 
ATOM   286  H  HB2  A LEU   A 1 12  ? 11.989 -15.703 6.599   0.68 14.08 ?  12  LEU   A HB2  1 
ATOM   287  H  HB2  B LEU   A 1 12  ? 11.891 -15.240 7.035   0.32 13.97 ?  12  LEU   A HB2  1 
ATOM   288  H  HB3  A LEU   A 1 12  ? 10.946 -16.334 5.591   0.68 14.08 ?  12  LEU   A HB3  1 
ATOM   289  H  HB3  B LEU   A 1 12  ? 10.927 -15.855 5.938   0.32 13.97 ?  12  LEU   A HB3  1 
ATOM   290  H  HG   A LEU   A 1 12  ? 10.453 -13.997 7.089   0.68 14.99 ?  12  LEU   A HG   1 
ATOM   291  H  HG   B LEU   A 1 12  ? 10.455 -13.522 7.442   0.32 14.95 ?  12  LEU   A HG   1 
ATOM   292  H  HD11 A LEU   A 1 12  ? 10.704 -12.839 5.084   0.68 15.67 ?  12  LEU   A HD11 1 
ATOM   293  H  HD11 B LEU   A 1 12  ? 10.336 -12.461 5.372   0.32 15.65 ?  12  LEU   A HD11 1 
ATOM   294  H  HD12 A LEU   A 1 12  ? 12.051 -13.590 5.467   0.68 15.67 ?  12  LEU   A HD12 1 
ATOM   295  H  HD12 B LEU   A 1 12  ? 11.742 -13.183 5.531   0.32 15.65 ?  12  LEU   A HD12 1 
ATOM   296  H  HD13 A LEU   A 1 12  ? 11.092 -14.196 4.354   0.68 15.67 ?  12  LEU   A HD13 1 
ATOM   297  H  HD13 B LEU   A 1 12  ? 10.604 -13.847 4.643   0.32 15.65 ?  12  LEU   A HD13 1 
ATOM   298  H  HD21 A LEU   A 1 12  ? 8.549  -13.749 5.708   0.68 15.95 ?  12  LEU   A HD21 1 
ATOM   299  H  HD21 B LEU   A 1 12  ? 8.365  -13.466 6.190   0.32 15.41 ?  12  LEU   A HD21 1 
ATOM   300  H  HD22 A LEU   A 1 12  ? 8.824  -15.202 5.127   0.68 15.95 ?  12  LEU   A HD22 1 
ATOM   301  H  HD22 B LEU   A 1 12  ? 8.582  -15.029 6.012   0.32 15.41 ?  12  LEU   A HD22 1 
ATOM   302  H  HD23 A LEU   A 1 12  ? 8.441  -15.018 6.658   0.68 15.95 ?  12  LEU   A HD23 1 
ATOM   303  H  HD23 B LEU   A 1 12  ? 8.417  -14.411 7.466   0.32 15.41 ?  12  LEU   A HD23 1 
ATOM   304  N  N    A THR   A 1 13  ? 12.311 -18.353 7.931   0.68 11.96 ?  13  THR   A N    1 
ATOM   305  N  N    B THR   A 1 13  ? 12.154 -17.996 8.100   0.32 11.10 ?  13  THR   A N    1 
ATOM   306  C  CA   A THR   A 1 13  ? 13.016 -19.628 7.849   0.68 12.49 ?  13  THR   A CA   1 
ATOM   307  C  CA   B THR   A 1 13  ? 12.800 -19.292 7.992   0.32 11.61 ?  13  THR   A CA   1 
ATOM   308  C  C    A THR   A 1 13  ? 13.789 -19.827 9.148   0.68 12.84 ?  13  THR   A C    1 
ATOM   309  C  C    B THR   A 1 13  ? 13.560 -19.553 9.284   0.32 12.29 ?  13  THR   A C    1 
ATOM   310  O  O    A THR   A 1 13  ? 13.684 -19.035 10.088  0.68 12.91 ?  13  THR   A O    1 
ATOM   311  O  O    B THR   A 1 13  ? 13.449 -18.810 10.265  0.32 12.82 ?  13  THR   A O    1 
ATOM   312  C  CB   A THR   A 1 13  ? 13.994 -19.680 6.666   0.68 13.26 ?  13  THR   A CB   1 
ATOM   313  C  CB   B THR   A 1 13  ? 13.755 -19.339 6.792   0.32 11.81 ?  13  THR   A CB   1 
ATOM   314  O  OG1  A THR   A 1 13  ? 15.069 -18.769 6.908   0.68 13.47 ?  13  THR   A OG1  1 
ATOM   315  O  OG1  B THR   A 1 13  ? 14.820 -18.409 7.006   0.32 11.82 ?  13  THR   A OG1  1 
ATOM   316  C  CG2  A THR   A 1 13  ? 13.319 -19.331 5.347   0.68 14.37 ?  13  THR   A CG2  1 
ATOM   317  C  CG2  B THR   A 1 13  ? 13.032 -19.016 5.481   0.32 11.99 ?  13  THR   A CG2  1 
ATOM   318  H  H    A THR   A 1 13  ? 12.764 -17.749 8.341   0.68 14.36 ?  13  THR   A H    1 
ATOM   319  H  H    B THR   A 1 13  ? 12.643 -17.390 8.464   0.32 13.32 ?  13  THR   A H    1 
ATOM   320  H  HA   A THR   A 1 13  ? 12.376 -20.355 7.750   0.68 14.99 ?  13  THR   A HA   1 
ATOM   321  H  HA   B THR   A 1 13  ? 12.127 -19.979 7.881   0.32 13.94 ?  13  THR   A HA   1 
ATOM   322  H  HB   A THR   A 1 13  ? 14.355 -20.581 6.585   0.68 15.92 ?  13  THR   A HB   1 
ATOM   323  H  HB   B THR   A 1 13  ? 14.130 -20.227 6.716   0.32 14.18 ?  13  THR   A HB   1 
ATOM   324  H  HG1  A THR   A 1 13  ? 15.610 -18.787 6.259   0.68 16.17 ?  13  THR   A HG1  1 
ATOM   325  H  HG1  B THR   A 1 13  ? 15.343 -18.413 6.344   0.32 14.19 ?  13  THR   A HG1  1 
ATOM   326  H  HG21 A THR   A 1 13  ? 13.936 -19.479 4.610   0.68 17.24 ?  13  THR   A HG21 1 
ATOM   327  H  HG21 B THR   A 1 13  ? 13.646 -19.107 4.732   0.32 14.39 ?  13  THR   A HG21 1 
ATOM   328  H  HG22 A THR   A 1 13  ? 12.538 -19.892 5.215   0.68 17.24 ?  13  THR   A HG22 1 
ATOM   329  H  HG22 B THR   A 1 13  ? 12.292 -19.633 5.351   0.32 14.39 ?  13  THR   A HG22 1 
ATOM   330  H  HG23 A THR   A 1 13  ? 13.047 -18.404 5.349   0.68 17.24 ?  13  THR   A HG23 1 
ATOM   331  H  HG23 B THR   A 1 13  ? 12.689 -18.112 5.499   0.32 14.39 ?  13  THR   A HG23 1 
ATOM   332  N  N    A ASP   A 1 14  ? 14.602 -20.886 9.187   0.68 13.57 ?  14  ASP   A N    1 
ATOM   333  N  N    B ASP   A 1 14  ? 14.351 -20.622 9.265   0.32 12.85 ?  14  ASP   A N    1 
ATOM   334  C  CA   A ASP   A 1 14  ? 15.437 -21.124 10.358  0.68 14.63 ?  14  ASP   A CA   1 
ATOM   335  C  CA   B ASP   A 1 14  ? 15.218 -20.952 10.383  0.32 13.73 ?  14  ASP   A CA   1 
ATOM   336  C  C    A ASP   A 1 14  ? 16.206 -19.868 10.766  0.68 14.55 ?  14  ASP   A C    1 
ATOM   337  C  C    B ASP   A 1 14  ? 16.183 -19.826 10.727  0.32 12.96 ?  14  ASP   A C    1 
ATOM   338  O  O    A ASP   A 1 14  ? 16.307 -19.551 11.957  0.68 15.10 ?  14  ASP   A O    1 
ATOM   339  O  O    B ASP   A 1 14  ? 16.650 -19.755 11.869  0.32 12.95 ?  14  ASP   A O    1 
ATOM   340  C  CB   A ASP   A 1 14  ? 16.403 -22.277 10.085  0.68 16.80 ?  14  ASP   A CB   1 
ATOM   341  C  CB   B ASP   A 1 14  ? 16.040 -22.181 10.020  0.32 15.32 ?  14  ASP   A CB   1 
ATOM   342  C  CG   A ASP   A 1 14  ? 17.322 -22.540 11.258  0.68 20.70 ?  14  ASP   A CG   1 
ATOM   343  C  CG   B ASP   A 1 14  ? 16.984 -22.580 11.117  0.32 17.17 ?  14  ASP   A CG   1 
ATOM   344  O  OD1  A ASP   A 1 14  ? 16.808 -22.839 12.356  0.68 22.15 ?  14  ASP   A OD1  1 
ATOM   345  O  OD1  B ASP   A 1 14  ? 16.510 -23.153 12.124  0.32 17.73 ?  14  ASP   A OD1  1 
ATOM   346  O  OD2  A ASP   A 1 14  ? 18.553 -22.431 11.088  0.68 23.14 -1 14  ASP   A OD2  1 
ATOM   347  O  OD2  B ASP   A 1 14  ? 18.191 -22.305 10.975  0.32 18.41 -1 14  ASP   A OD2  1 
ATOM   348  H  H    A ASP   A 1 14  ? 14.704 -21.466 8.553   0.68 16.29 ?  14  ASP   A H    1 
ATOM   349  H  H    B ASP   A 1 14  ? 14.400 -21.164 8.608   0.32 15.43 ?  14  ASP   A H    1 
ATOM   350  H  HA   A ASP   A 1 14  ? 14.874 -21.386 11.101  0.68 17.56 ?  14  ASP   A HA   1 
ATOM   351  H  HA   B ASP   A 1 14  ? 14.679 -21.157 11.164  0.32 16.48 ?  14  ASP   A HA   1 
ATOM   352  H  HB2  A ASP   A 1 14  ? 15.886 -23.090 9.893   0.68 20.17 ?  14  ASP   A HB2  1 
ATOM   353  H  HB2  B ASP   A 1 14  ? 15.445 -22.925 9.859   0.32 18.39 ?  14  ASP   A HB2  1 
ATOM   354  H  HB3  A ASP   A 1 14  ? 16.961 -22.066 9.323   0.68 20.17 ?  14  ASP   A HB3  1 
ATOM   355  H  HB3  B ASP   A 1 14  ? 16.557 -21.988 9.217   0.32 18.39 ?  14  ASP   A HB3  1 
ATOM   356  N  N    A ASN   A 1 15  ? 16.732 -19.120 9.790   0.68 13.60 ?  15  ASN   A N    1 
ATOM   357  N  N    B ASN   A 1 15  ? 16.505 -18.950 9.766   0.32 12.08 ?  15  ASN   A N    1 
ATOM   358  C  CA   A ASN   A 1 15  ? 17.689 -18.054 10.073  0.68 13.76 ?  15  ASN   A CA   1 
ATOM   359  C  CA   B ASN   A 1 15  ? 17.561 -17.968 9.988   0.32 12.23 ?  15  ASN   A CA   1 
ATOM   360  C  C    A ASN   A 1 15  ? 17.283 -16.667 9.587   0.68 13.35 ?  15  ASN   A C    1 
ATOM   361  C  C    B ASN   A 1 15  ? 17.261 -16.596 9.384   0.32 12.45 ?  15  ASN   A C    1 
ATOM   362  O  O    A ASN   A 1 15  ? 17.982 -15.700 9.921   0.68 12.80 ?  15  ASN   A O    1 
ATOM   363  O  O    B ASN   A 1 15  ? 18.181 -15.779 9.257   0.32 12.78 ?  15  ASN   A O    1 
ATOM   364  C  CB   A ASN   A 1 15  ? 19.067 -18.390 9.471   0.68 13.78 ?  15  ASN   A CB   1 
ATOM   365  C  CB   B ASN   A 1 15  ? 18.901 -18.487 9.440   0.32 12.13 ?  15  ASN   A CB   1 
ATOM   366  C  CG   A ASN   A 1 15  ? 19.019 -18.544 7.964   0.68 14.35 ?  15  ASN   A CG   1 
ATOM   367  C  CG   B ASN   A 1 15  ? 18.961 -18.476 7.925   0.32 12.51 ?  15  ASN   A CG   1 
ATOM   368  O  OD1  A ASN   A 1 15  ? 18.224 -19.327 7.433   0.68 15.35 ?  15  ASN   A OD1  1 
ATOM   369  O  OD1  B ASN   A 1 15  ? 18.374 -19.330 7.258   0.32 13.07 ?  15  ASN   A OD1  1 
ATOM   370  N  ND2  A ASN   A 1 15  ? 19.853 -17.774 7.261   0.68 13.93 ?  15  ASN   A ND2  1 
ATOM   371  N  ND2  B ASN   A 1 15  ? 19.685 -17.506 7.372   0.32 12.17 ?  15  ASN   A ND2  1 
ATOM   372  H  H    A ASN   A 1 15  ? 16.554 -19.217 8.959   0.68 16.33 ?  15  ASN   A H    1 
ATOM   373  H  H    B ASN   A 1 15  ? 16.132 -18.909 8.996   0.32 14.50 ?  15  ASN   A H    1 
ATOM   374  H  HA   A ASN   A 1 15  ? 17.818 -18.006 11.035  0.68 16.52 ?  15  ASN   A HA   1 
ATOM   375  H  HA   B ASN   A 1 15  ? 17.669 -17.842 10.943  0.32 14.69 ?  15  ASN   A HA   1 
ATOM   376  H  HB2  A ASN   A 1 15  ? 19.695 -17.673 9.688   0.68 16.55 ?  15  ASN   A HB2  1 
ATOM   377  H  HB2  B ASN   A 1 15  ? 19.616 -17.925 9.774   0.32 14.56 ?  15  ASN   A HB2  1 
ATOM   378  H  HB3  A ASN   A 1 15  ? 19.394 -19.226 9.849   0.68 16.55 ?  15  ASN   A HB3  1 
ATOM   379  H  HB3  B ASN   A 1 15  ? 19.029 -19.401 9.735   0.32 14.56 ?  15  ASN   A HB3  1 
ATOM   380  H  HD21 A ASN   A 1 15  ? 19.865 -17.824 6.402   0.68 16.72 ?  15  ASN   A HD21 1 
ATOM   381  H  HD21 B ASN   A 1 15  ? 19.753 -17.450 6.516   0.32 14.61 ?  15  ASN   A HD21 1 
ATOM   382  H  HD22 A ASN   A 1 15  ? 20.395 -17.231 7.661   0.68 16.72 ?  15  ASN   A HD22 1 
ATOM   383  H  HD22 B ASN   A 1 15  ? 20.085 -16.926 7.871   0.32 14.61 ?  15  ASN   A HD22 1 
ATOM   384  N  N    A VAL   A 1 16  ? 16.212 -16.535 8.798   0.68 12.91 ?  16  VAL   A N    1 
ATOM   385  N  N    B VAL   A 1 16  ? 16.009 -16.308 9.029   0.32 11.85 ?  16  VAL   A N    1 
ATOM   386  C  CA   A VAL   A 1 16  ? 15.796 -15.253 8.234   0.68 12.70 ?  16  VAL   A CA   1 
ATOM   387  C  CA   B VAL   A 1 16  ? 15.636 -15.048 8.394   0.32 11.90 ?  16  VAL   A CA   1 
ATOM   388  C  C    A VAL   A 1 16  ? 14.514 -14.773 8.904   0.68 12.17 ?  16  VAL   A C    1 
ATOM   389  C  C    B VAL   A 1 16  ? 14.373 -14.521 9.064   0.32 11.75 ?  16  VAL   A C    1 
ATOM   390  O  O    A VAL   A 1 16  ? 13.519 -15.506 8.985   0.68 12.16 ?  16  VAL   A O    1 
ATOM   391  O  O    B VAL   A 1 16  ? 13.373 -15.240 9.173   0.32 11.73 ?  16  VAL   A O    1 
ATOM   392  C  CB   A VAL   A 1 16  ? 15.628 -15.310 6.707   0.68 13.49 ?  16  VAL   A CB   1 
ATOM   393  C  CB   B VAL   A 1 16  ? 15.432 -15.212 6.874   0.32 12.68 ?  16  VAL   A CB   1 
ATOM   394  C  CG1  A VAL   A 1 16  ? 15.212 -13.936 6.174   0.68 14.38 ?  16  VAL   A CG1  1 
ATOM   395  C  CG1  B VAL   A 1 16  ? 14.995 -13.895 6.227   0.32 13.43 ?  16  VAL   A CG1  1 
ATOM   396  C  CG2  A VAL   A 1 16  ? 16.907 -15.768 6.035   0.68 14.17 ?  16  VAL   A CG2  1 
ATOM   397  C  CG2  B VAL   A 1 16  ? 16.701 -15.741 6.207   0.32 13.26 ?  16  VAL   A CG2  1 
ATOM   398  H  H    A VAL   A 1 16  ? 15.731 -17.203 8.556   0.68 15.50 ?  16  VAL   A H    1 
ATOM   399  H  H    B VAL   A 1 16  ? 15.343 -16.831 9.160   0.32 14.22 ?  16  VAL   A H    1 
ATOM   400  H  HA   A VAL   A 1 16  ? 16.492 -14.604 8.420   0.68 15.25 ?  16  VAL   A HA   1 
ATOM   401  H  HA   B VAL   A 1 16  ? 16.339 -14.393 8.536   0.32 14.28 ?  16  VAL   A HA   1 
ATOM   402  H  HB   A VAL   A 1 16  ? 14.929 -15.948 6.489   0.68 16.19 ?  16  VAL   A HB   1 
ATOM   403  H  HB   B VAL   A 1 16  ? 14.730 -15.860 6.727   0.32 15.22 ?  16  VAL   A HB   1 
ATOM   404  H  HG11 A VAL   A 1 16  ? 15.297 -13.936 5.209   0.68 17.26 ?  16  VAL   A HG11 1 
ATOM   405  H  HG11 B VAL   A 1 16  ? 15.051 -13.989 5.261   0.32 16.12 ?  16  VAL   A HG11 1 
ATOM   406  H  HG12 A VAL   A 1 16  ? 14.288 -13.768 6.423   0.68 17.26 ?  16  VAL   A HG12 1 
ATOM   407  H  HG12 B VAL   A 1 16  ? 14.081 -13.702 6.484   0.32 16.12 ?  16  VAL   A HG12 1 
ATOM   408  H  HG13 A VAL   A 1 16  ? 15.789 -13.261 6.560   0.68 17.26 ?  16  VAL   A HG13 1 
ATOM   409  H  HG13 B VAL   A 1 16  ? 15.583 -13.185 6.523   0.32 16.12 ?  16  VAL   A HG13 1 
ATOM   410  H  HG21 A VAL   A 1 16  ? 16.795 -15.703 5.074   0.68 17.00 ?  16  VAL   A HG21 1 
ATOM   411  H  HG21 B VAL   A 1 16  ? 16.552 -15.803 5.250   0.32 15.92 ?  16  VAL   A HG21 1 
ATOM   412  H  HG22 A VAL   A 1 16  ? 17.635 -15.199 6.324   0.68 17.00 ?  16  VAL   A HG22 1 
ATOM   413  H  HG22 B VAL   A 1 16  ? 17.434 -15.133 6.388   0.32 15.92 ?  16  VAL   A HG22 1 
ATOM   414  H  HG23 A VAL   A 1 16  ? 17.084 -16.688 6.287   0.68 17.00 ?  16  VAL   A HG23 1 
ATOM   415  H  HG23 B VAL   A 1 16  ? 16.904 -16.620 6.565   0.32 15.92 ?  16  VAL   A HG23 1 
ATOM   416  N  N    A TYR   A 1 17  ? 14.536 -13.509 9.319   0.68 12.02 ?  17  TYR   A N    1 
ATOM   417  N  N    B TYR   A 1 17  ? 14.424 -13.259 9.494   0.32 11.67 ?  17  TYR   A N    1 
ATOM   418  C  CA   A TYR   A 1 17  ? 13.445 -12.817 9.984   0.68 11.88 ?  17  TYR   A CA   1 
ATOM   419  C  CA   B TYR   A 1 17  ? 13.368 -12.601 10.247  0.32 11.31 ?  17  TYR   A CA   1 
ATOM   420  C  C    A TYR   A 1 17  ? 13.179 -11.505 9.256   0.68 11.88 ?  17  TYR   A C    1 
ATOM   421  C  C    B TYR   A 1 17  ? 13.109 -11.243 9.610   0.32 10.93 ?  17  TYR   A C    1 
ATOM   422  O  O    A TYR   A 1 17  ? 14.077 -10.951 8.619   0.68 11.25 ?  17  TYR   A O    1 
ATOM   423  O  O    B TYR   A 1 17  ? 14.035 -10.610 9.099   0.32 10.86 ?  17  TYR   A O    1 
ATOM   424  C  CB   A TYR   A 1 17  ? 13.855 -12.512 11.423  0.68 12.75 ?  17  TYR   A CB   1 
ATOM   425  C  CB   B TYR   A 1 17  ? 13.814 -12.417 11.707  0.32 12.11 ?  17  TYR   A CB   1 
ATOM   426  C  CG   A TYR   A 1 17  ? 14.009 -13.749 12.270  0.68 14.11 ?  17  TYR   A CG   1 
ATOM   427  C  CG   B TYR   A 1 17  ? 14.123 -13.722 12.426  0.32 12.98 ?  17  TYR   A CG   1 
ATOM   428  C  CD1  A TYR   A 1 17  ? 15.168 -14.519 12.225  0.68 15.00 ?  17  TYR   A CD1  1 
ATOM   429  C  CD1  B TYR   A 1 17  ? 15.339 -14.383 12.249  0.32 13.68 ?  17  TYR   A CD1  1 
ATOM   430  C  CD2  A TYR   A 1 17  ? 12.982 -14.164 13.103  0.68 14.11 ?  17  TYR   A CD2  1 
ATOM   431  C  CD2  B TYR   A 1 17  ? 13.194 -14.294 13.284  0.32 13.23 ?  17  TYR   A CD2  1 
ATOM   432  C  CE1  A TYR   A 1 17  ? 15.298 -15.667 12.994  0.68 15.15 ?  17  TYR   A CE1  1 
ATOM   433  C  CE1  B TYR   A 1 17  ? 15.610 -15.581 12.908  0.32 14.08 ?  17  TYR   A CE1  1 
ATOM   434  C  CE2  A TYR   A 1 17  ? 13.101 -15.311 13.877  0.68 14.90 ?  17  TYR   A CE2  1 
ATOM   435  C  CE2  B TYR   A 1 17  ? 13.457 -15.485 13.946  0.32 13.59 ?  17  TYR   A CE2  1 
ATOM   436  C  CZ   A TYR   A 1 17  ? 14.260 -16.059 13.820  0.68 14.92 ?  17  TYR   A CZ   1 
ATOM   437  C  CZ   B TYR   A 1 17  ? 14.662 -16.124 13.755  0.32 13.96 ?  17  TYR   A CZ   1 
ATOM   438  O  OH   A TYR   A 1 17  ? 14.382 -17.199 14.586  0.68 15.24 ?  17  TYR   A OH   1 
ATOM   439  O  OH   B TYR   A 1 17  ? 14.906 -17.306 14.422  0.32 14.14 ?  17  TYR   A OH   1 
ATOM   440  H  H    A TYR   A 1 17  ? 15.226 -13.011 9.207   0.68 14.43 ?  17  TYR   A H    1 
ATOM   441  H  H    B TYR   A 1 17  ? 15.091 -12.731 9.343   0.32 14.00 ?  17  TYR   A H    1 
ATOM   442  H  HA   A TYR   A 1 17  ? 12.648 -13.382 9.977   0.68 14.26 ?  17  TYR   A HA   1 
ATOM   443  H  HA   B TYR   A 1 17  ? 12.549 -13.116 10.218  0.32 13.57 ?  17  TYR   A HA   1 
ATOM   444  H  HB2  A TYR   A 1 17  ? 14.704 -12.052 11.415  0.68 15.31 ?  17  TYR   A HB2  1 
ATOM   445  H  HB2  B TYR   A 1 17  ? 14.617 -11.875 11.716  0.32 14.54 ?  17  TYR   A HB2  1 
ATOM   446  H  HB3  A TYR   A 1 17  ? 13.175 -11.962 11.826  0.68 15.31 ?  17  TYR   A HB3  1 
ATOM   447  H  HB3  B TYR   A 1 17  ? 13.108 -11.967 12.197  0.32 14.54 ?  17  TYR   A HB3  1 
ATOM   448  H  HD1  A TYR   A 1 17  ? 15.871 -14.266 11.666  0.68 18.01 ?  17  TYR   A HD1  1 
ATOM   449  H  HD1  B TYR   A 1 17  ? 15.978 -14.025 11.677  0.32 16.42 ?  17  TYR   A HD1  1 
ATOM   450  H  HD2  A TYR   A 1 17  ? 12.197 -13.672 13.145  0.68 16.94 ?  17  TYR   A HD2  1 
ATOM   451  H  HD2  B TYR   A 1 17  ? 12.378 -13.871 13.416  0.32 15.88 ?  17  TYR   A HD2  1 
ATOM   452  H  HE1  A TYR   A 1 17  ? 16.083 -16.173 12.955  0.68 18.19 ?  17  TYR   A HE1  1 
ATOM   453  H  HE1  B TYR   A 1 17  ? 16.427 -16.017 12.785  0.32 16.90 ?  17  TYR   A HE1  1 
ATOM   454  H  HE2  A TYR   A 1 17  ? 12.402 -15.574 14.433  0.68 17.89 ?  17  TYR   A HE2  1 
ATOM   455  H  HE2  B TYR   A 1 17  ? 12.821 -15.851 14.518  0.32 16.32 ?  17  TYR   A HE2  1 
ATOM   456  H  HH   A TYR   A 1 17  ? 13.624 -17.444 14.853  0.68 18.29 ?  17  TYR   A HH   1 
ATOM   457  H  HH   B TYR   A 1 17  ? 15.652 -17.625 14.203  0.32 16.97 ?  17  TYR   A HH   1 
ATOM   458  N  N    A ILE   A 1 18  ? 11.952 -10.986 9.360   0.68 12.27 ?  18  ILE   A N    1 
ATOM   459  N  N    B ILE   A 1 18  ? 11.853 -10.788 9.626   0.32 10.61 ?  18  ILE   A N    1 
ATOM   460  C  CA   A ILE   A 1 18  ? 11.567 -9.805  8.589   0.68 11.95 ?  18  ILE   A CA   1 
ATOM   461  C  CA   B ILE   A 1 18  ? 11.475 -9.586  8.885   0.32 10.37 ?  18  ILE   A CA   1 
ATOM   462  C  C    A ILE   A 1 18  ? 10.587 -8.945  9.383   0.68 12.70 ?  18  ILE   A C    1 
ATOM   463  C  C    B ILE   A 1 18  ? 10.567 -8.705  9.730   0.32 10.49 ?  18  ILE   A C    1 
ATOM   464  O  O    A ILE   A 1 18  ? 9.772  -9.454  10.157  0.68 13.19 ?  18  ILE   A O    1 
ATOM   465  O  O    B ILE   A 1 18  ? 9.731  -9.199  10.495  0.32 10.90 ?  18  ILE   A O    1 
ATOM   466  C  CB   A ILE   A 1 18  ? 11.018 -10.224 7.206   0.68 11.65 ?  18  ILE   A CB   1 
ATOM   467  C  CB   B ILE   A 1 18  ? 10.833 -9.936  7.526   0.32 10.41 ?  18  ILE   A CB   1 
ATOM   468  C  CG1  A ILE   A 1 18  ? 10.962 -9.031  6.260   0.68 11.85 ?  18  ILE   A CG1  1 
ATOM   469  C  CG1  B ILE   A 1 18  ? 10.796 -8.715  6.602   0.32 11.51 ?  18  ILE   A CG1  1 
ATOM   470  C  CG2  A ILE   A 1 18  ? 9.663  -10.921 7.346   0.68 11.38 ?  18  ILE   A CG2  1 
ATOM   471  C  CG2  B ILE   A 1 18  ? 9.439  -10.514 7.718   0.32 10.68 ?  18  ILE   A CG2  1 
ATOM   472  C  CD1  A ILE   A 1 18  ? 10.740 -9.426  4.835   0.68 12.89 ?  18  ILE   A CD1  1 
ATOM   473  C  CD1  B ILE   A 1 18  ? 10.398 -9.058  5.179   0.32 12.45 ?  18  ILE   A CD1  1 
ATOM   474  H  H    A ILE   A 1 18  ? 11.337 -11.316 9.861   0.68 14.73 ?  18  ILE   A H    1 
ATOM   475  H  H    B ILE   A 1 18  ? 11.197 -11.155 10.056  0.32 12.73 ?  18  ILE   A H    1 
ATOM   476  H  HA   A ILE   A 1 18  ? 12.369 -9.284  8.430   0.68 14.34 ?  18  ILE   A HA   1 
ATOM   477  H  HA   B ILE   A 1 18  ? 12.273 -9.072  8.708   0.32 12.45 ?  18  ILE   A HA   1 
ATOM   478  H  HB   A ILE   A 1 18  ? 11.635 -10.873 6.820   0.68 13.99 ?  18  ILE   A HB   1 
ATOM   479  H  HB   B ILE   A 1 18  ? 11.383 -10.607 7.108   0.32 12.50 ?  18  ILE   A HB   1 
ATOM   480  H  HG12 A ILE   A 1 18  ? 10.236 -8.452  6.531   0.68 14.23 ?  18  ILE   A HG12 1 
ATOM   481  H  HG12 B ILE   A 1 18  ? 10.155 -8.071  6.941   0.32 13.82 ?  18  ILE   A HG12 1 
ATOM   482  H  HG13 A ILE   A 1 18  ? 11.806 -8.554  6.310   0.68 14.23 ?  18  ILE   A HG13 1 
ATOM   483  H  HG13 B ILE   A 1 18  ? 11.681 -8.311  6.571   0.32 13.82 ?  18  ILE   A HG13 1 
ATOM   484  H  HG21 A ILE   A 1 18  ? 9.423  -11.329 6.493   0.68 13.66 ?  18  ILE   A HG21 1 
ATOM   485  H  HG21 B ILE   A 1 18  ? 9.158  -10.935 6.889   0.32 12.83 ?  18  ILE   A HG21 1 
ATOM   486  H  HG22 A ILE   A 1 18  ? 9.727  -11.613 8.025   0.68 13.66 ?  18  ILE   A HG22 1 
ATOM   487  H  HG22 B ILE   A 1 18  ? 9.466  -11.168 8.430   0.32 12.83 ?  18  ILE   A HG22 1 
ATOM   488  H  HG23 A ILE   A 1 18  ? 8.992  -10.272 7.598   0.68 13.66 ?  18  ILE   A HG23 1 
ATOM   489  H  HG23 B ILE   A 1 18  ? 8.824  -9.798  7.948   0.32 12.83 ?  18  ILE   A HG23 1 
ATOM   490  H  HD11 A ILE   A 1 18  ? 10.765 -8.626  4.282   0.68 15.48 ?  18  ILE   A HD11 1 
ATOM   491  H  HD11 B ILE   A 1 18  ? 10.404 -8.251  4.641   0.32 14.94 ?  18  ILE   A HD11 1 
ATOM   492  H  HD12 A ILE   A 1 18  ? 11.436 -10.039 4.562   0.68 15.48 ?  18  ILE   A HD12 1 
ATOM   493  H  HD12 B ILE   A 1 18  ? 11.035 -9.697  4.818   0.32 14.94 ?  18  ILE   A HD12 1 
ATOM   494  H  HD13 A ILE   A 1 18  ? 9.871  -9.850  4.758   0.68 15.48 ?  18  ILE   A HD13 1 
ATOM   495  H  HD13 B ILE   A 1 18  ? 9.509  -9.444  5.183   0.32 14.94 ?  18  ILE   A HD13 1 
ATOM   496  N  N    A LYS   A 1 19  ? 10.661 -7.626  9.168   0.68 12.49 ?  19  LYS   A N    1 
ATOM   497  N  N    B LYS   A 1 19  ? 10.733 -7.391  9.580   0.32 10.57 ?  19  LYS   A N    1 
ATOM   498  C  CA   A LYS   A 1 19  ? 9.839  -6.661  9.894   0.68 13.27 ?  19  LYS   A CA   1 
ATOM   499  C  CA   B LYS   A 1 19  ? 9.952  -6.426  10.336  0.32 11.98 ?  19  LYS   A CA   1 
ATOM   500  C  C    A LYS   A 1 19  ? 9.668  -5.396  9.058   0.68 13.31 ?  19  LYS   A C    1 
ATOM   501  C  C    B LYS   A 1 19  ? 9.750  -5.193  9.473   0.32 12.42 ?  19  LYS   A C    1 
ATOM   502  O  O    A LYS   A 1 19  ? 10.563 -5.016  8.299   0.68 12.86 ?  19  LYS   A O    1 
ATOM   503  O  O    B LYS   A 1 19  ? 10.663 -4.779  8.755   0.32 12.19 ?  19  LYS   A O    1 
ATOM   504  C  CB   A LYS   A 1 19  ? 10.526 -6.304  11.219  0.68 14.63 ?  19  LYS   A CB   1 
ATOM   505  C  CB   B LYS   A 1 19  ? 10.680 -6.036  11.626  0.32 13.09 ?  19  LYS   A CB   1 
ATOM   506  C  CG   A LYS   A 1 19  ? 9.808  -5.304  12.122  0.68 16.24 ?  19  LYS   A CG   1 
ATOM   507  C  CG   B LYS   A 1 19  ? 9.861  -5.198  12.574  0.32 14.37 ?  19  LYS   A CG   1 
ATOM   508  C  CD   A LYS   A 1 19  ? 10.670 -5.049  13.358  0.68 17.72 ?  19  LYS   A CD   1 
ATOM   509  C  CD   B LYS   A 1 19  ? 10.697 -4.763  13.756  0.32 15.58 ?  19  LYS   A CD   1 
ATOM   510  C  CE   A LYS   A 1 19  ? 10.041 -4.091  14.356  0.68 18.88 ?  19  LYS   A CE   1 
ATOM   511  C  CE   B LYS   A 1 19  ? 9.893  -3.904  14.705  0.32 16.43 ?  19  LYS   A CE   1 
ATOM   512  N  NZ   A LYS   A 1 19  ? 10.934 -3.899  15.542  0.68 19.12 ?  19  LYS   A NZ   1 
ATOM   513  N  NZ   B LYS   A 1 19  ? 10.741 -3.392  15.807  0.32 16.82 ?  19  LYS   A NZ   1 
ATOM   514  H  H    A LYS   A 1 19  ? 11.195 -7.275  8.597   0.68 14.99 ?  19  LYS   A H    1 
ATOM   515  H  H    B LYS   A 1 19  ? 11.304 -7.022  9.037   0.32 12.69 ?  19  LYS   A H    1 
ATOM   516  H  HA   A LYS   A 1 19  ? 8.968  -7.059  10.079  0.68 15.93 ?  19  LYS   A HA   1 
ATOM   517  H  HA   B LYS   A 1 19  ? 9.089  -6.800  10.564  0.32 14.38 ?  19  LYS   A HA   1 
ATOM   518  H  HB2  A LYS   A 1 19  ? 10.638 -7.122  11.732  0.68 17.56 ?  19  LYS   A HB2  1 
ATOM   519  H  HB2  B LYS   A 1 19  ? 10.928 -6.846  12.099  0.32 15.71 ?  19  LYS   A HB2  1 
ATOM   520  H  HB3  A LYS   A 1 19  ? 11.394 -5.934  11.012  0.68 17.56 ?  19  LYS   A HB3  1 
ATOM   521  H  HB3  B LYS   A 1 19  ? 11.478 -5.532  11.400  0.32 15.71 ?  19  LYS   A HB3  1 
ATOM   522  H  HG2  A LYS   A 1 19  ? 9.680  -4.465  11.652  0.68 19.50 ?  19  LYS   A HG2  1 
ATOM   523  H  HG2  B LYS   A 1 19  ? 9.545  -4.406  12.116  0.32 17.25 ?  19  LYS   A HG2  1 
ATOM   524  H  HG3  A LYS   A 1 19  ? 8.953  -5.669  12.407  0.68 19.50 ?  19  LYS   A HG3  1 
ATOM   525  H  HG3  B LYS   A 1 19  ? 9.114  -5.723  12.904  0.32 17.25 ?  19  LYS   A HG3  1 
ATOM   526  H  HD2  A LYS   A 1 19  ? 10.822 -5.891  13.817  0.68 21.27 ?  19  LYS   A HD2  1 
ATOM   527  H  HD2  B LYS   A 1 19  ? 10.999 -5.551  14.238  0.32 18.70 ?  19  LYS   A HD2  1 
ATOM   528  H  HD3  A LYS   A 1 19  ? 11.517 -4.669  13.079  0.68 21.27 ?  19  LYS   A HD3  1 
ATOM   529  H  HD3  B LYS   A 1 19  ? 11.458 -4.251  13.440  0.32 18.70 ?  19  LYS   A HD3  1 
ATOM   530  H  HE2  A LYS   A 1 19  ? 9.906  -3.227  13.937  0.68 22.66 ?  19  LYS   A HE2  1 
ATOM   531  H  HE2  B LYS   A 1 19  ? 9.530  -3.149  14.218  0.32 19.72 ?  19  LYS   A HE2  1 
ATOM   532  H  HE3  A LYS   A 1 19  ? 9.197  -4.452  14.668  0.68 22.66 ?  19  LYS   A HE3  1 
ATOM   533  H  HE3  B LYS   A 1 19  ? 9.178  -4.436  15.087  0.32 19.72 ?  19  LYS   A HE3  1 
ATOM   534  H  HZ1  A LYS   A 1 19  ? 10.565 -3.325  16.114  0.68 22.95 ?  19  LYS   A HZ1  1 
ATOM   535  H  HZ1  B LYS   A 1 19  ? 10.253 -2.890  16.354  0.32 20.19 ?  19  LYS   A HZ1  1 
ATOM   536  H  HZ2  A LYS   A 1 19  ? 11.059 -4.678  15.956  0.68 22.95 ?  19  LYS   A HZ2  1 
ATOM   537  H  HZ2  B LYS   A 1 19  ? 11.085 -4.072  16.266  0.32 20.19 ?  19  LYS   A HZ2  1 
ATOM   538  H  HZ3  A LYS   A 1 19  ? 11.722 -3.581  15.282  0.68 22.95 ?  19  LYS   A HZ3  1 
ATOM   539  H  HZ3  B LYS   A 1 19  ? 11.405 -2.901  15.476  0.32 20.19 ?  19  LYS   A HZ3  1 
ATOM   540  N  N    A ASN   A 1 20  ? 8.509  -4.745  9.202   0.68 14.04 ?  20  ASN   A N    1 
ATOM   541  N  N    B ASN   A 1 20  ? 8.551  -4.619  9.530   0.32 13.79 ?  20  ASN   A N    1 
ATOM   542  C  CA   A ASN   A 1 20  ? 8.300  -3.407  8.649   0.68 15.24 ?  20  ASN   A CA   1 
ATOM   543  C  CA   B ASN   A 1 20  ? 8.276  -3.367  8.830   0.32 15.36 ?  20  ASN   A CA   1 
ATOM   544  C  C    A ASN   A 1 20  ? 8.933  -2.414  9.619   0.68 16.11 ?  20  ASN   A C    1 
ATOM   545  C  C    B ASN   A 1 20  ? 8.834  -2.218  9.656   0.32 15.55 ?  20  ASN   A C    1 
ATOM   546  O  O    A ASN   A 1 20  ? 8.435  -2.217  10.731  0.68 16.73 ?  20  ASN   A O    1 
ATOM   547  O  O    B ASN   A 1 20  ? 8.176  -1.719  10.574  0.32 15.70 ?  20  ASN   A O    1 
ATOM   548  C  CB   A ASN   A 1 20  ? 6.802  -3.156  8.450   0.68 16.12 ?  20  ASN   A CB   1 
ATOM   549  C  CB   B ASN   A 1 20  ? 6.781  -3.188  8.613   0.32 16.72 ?  20  ASN   A CB   1 
ATOM   550  C  CG   A ASN   A 1 20  ? 6.472  -1.736  7.984   0.68 16.94 ?  20  ASN   A CG   1 
ATOM   551  C  CG   B ASN   A 1 20  ? 6.426  -1.773  8.214   0.32 17.99 ?  20  ASN   A CG   1 
ATOM   552  O  OD1  A ASN   A 1 20  ? 5.387  -1.226  8.276   0.68 18.74 ?  20  ASN   A OD1  1 
ATOM   553  O  OD1  B ASN   A 1 20  ? 5.739  -1.064  8.948   0.32 18.93 ?  20  ASN   A OD1  1 
ATOM   554  N  ND2  A ASN   A 1 20  ? 7.383  -1.106  7.247   0.68 16.84 ?  20  ASN   A ND2  1 
ATOM   555  N  ND2  B ASN   A 1 20  ? 6.922  -1.342  7.060   0.32 18.39 ?  20  ASN   A ND2  1 
ATOM   556  H  H    A ASN   A 1 20  ? 7.825  -5.070  9.618   0.68 16.86 ?  20  ASN   A H    1 
ATOM   557  H  H    B ASN   A 1 20  ? 7.876  -4.948  9.952   0.32 16.55 ?  20  ASN   A H    1 
ATOM   558  H  HA   A ASN   A 1 20  ? 8.744  -3.346  7.792   0.68 18.29 ?  20  ASN   A HA   1 
ATOM   559  H  HA   B ASN   A 1 20  ? 8.723  -3.373  7.970   0.32 18.43 ?  20  ASN   A HA   1 
ATOM   560  H  HB2  A ASN   A 1 20  ? 6.465  -3.767  7.780   0.68 19.35 ?  20  ASN   A HB2  1 
ATOM   561  H  HB2  B ASN   A 1 20  ? 6.491  -3.786  7.907   0.32 20.07 ?  20  ASN   A HB2  1 
ATOM   562  H  HB3  A ASN   A 1 20  ? 6.347  -3.313  9.293   0.68 19.35 ?  20  ASN   A HB3  1 
ATOM   563  H  HB3  B ASN   A 1 20  ? 6.315  -3.397  9.439   0.32 20.07 ?  20  ASN   A HB3  1 
ATOM   564  H  HD21 A ASN   A 1 20  ? 7.233  -0.304  6.978   0.68 20.22 ?  20  ASN   A HD21 1 
ATOM   565  H  HD21 B ASN   A 1 20  ? 6.750  -0.545  6.791   0.32 22.07 ?  20  ASN   A HD21 1 
ATOM   566  H  HD22 A ASN   A 1 20  ? 8.125  -1.493  7.048   0.68 20.22 ?  20  ASN   A HD22 1 
ATOM   567  H  HD22 B ASN   A 1 20  ? 7.410  -1.863  6.580   0.32 22.07 ?  20  ASN   A HD22 1 
ATOM   568  N  N    A ALA   A 1 21  ? 10.059 -1.821  9.228   0.68 16.35 ?  21  ALA   A N    1 
ATOM   569  N  N    B ALA   A 1 21  ? 10.043 -1.780  9.316   0.32 15.65 ?  21  ALA   A N    1 
ATOM   570  C  CA   A ALA   A 1 21  ? 10.762 -0.940  10.147  0.68 16.30 ?  21  ALA   A CA   1 
ATOM   571  C  CA   B ALA   A 1 21  ? 10.676 -0.693  10.043  0.32 15.52 ?  21  ALA   A CA   1 
ATOM   572  C  C    A ALA   A 1 21  ? 11.714 -0.038  9.384   0.68 15.74 ?  21  ALA   A C    1 
ATOM   573  C  C    B ALA   A 1 21  ? 11.785 -0.101  9.190   0.32 14.74 ?  21  ALA   A C    1 
ATOM   574  O  O    A ALA   A 1 21  ? 12.163 -0.371  8.283   0.68 15.73 ?  21  ALA   A O    1 
ATOM   575  O  O    B ALA   A 1 21  ? 12.337 -0.769  8.313   0.32 14.67 ?  21  ALA   A O    1 
ATOM   576  C  CB   A ALA   A 1 21  ? 11.534 -1.733  11.205  0.68 16.73 ?  21  ALA   A CB   1 
ATOM   577  C  CB   B ALA   A 1 21  ? 11.245 -1.172  11.383  0.32 16.01 ?  21  ALA   A CB   1 
ATOM   578  H  H    A ALA   A 1 21  ? 10.424 -1.911  8.456   0.68 19.63 ?  21  ALA   A H    1 
ATOM   579  H  H    B ALA   A 1 21  ? 10.513 -2.093  8.665   0.32 18.78 ?  21  ALA   A H    1 
ATOM   580  H  HA   A ALA   A 1 21  ? 10.116 -0.379  10.604  0.68 19.56 ?  21  ALA   A HA   1 
ATOM   581  H  HA   B ALA   A 1 21  ? 10.018 -0.004  10.219  0.32 18.63 ?  21  ALA   A HA   1 
ATOM   582  H  HB1  A ALA   A 1 21  ? 11.964 -1.110  11.810  0.68 20.08 ?  21  ALA   A HB1  1 
ATOM   583  H  HB1  B ALA   A 1 21  ? 11.655 -0.418  11.838  0.32 19.22 ?  21  ALA   A HB1  1 
ATOM   584  H  HB2  A ALA   A 1 21  ? 10.907 -2.291  11.697  0.68 20.08 ?  21  ALA   A HB2  1 
ATOM   585  H  HB2  B ALA   A 1 21  ? 10.524 -1.530  11.925  0.32 19.22 ?  21  ALA   A HB2  1 
ATOM   586  H  HB3  A ALA   A 1 21  ? 12.195 -2.287  10.766  0.68 20.08 ?  21  ALA   A HB3  1 
ATOM   587  H  HB3  B ALA   A 1 21  ? 11.909 -1.859  11.219  0.32 19.22 ?  21  ALA   A HB3  1 
ATOM   588  N  N    A ASP   A 1 22  ? 11.998 1.112   9.994   0.68 15.86 ?  22  ASP   A N    1 
ATOM   589  N  N    B ASP   A 1 22  ? 12.078 1.171   9.444   0.32 14.51 ?  22  ASP   A N    1 
ATOM   590  C  CA   A ASP   A 1 22  ? 13.037 2.030   9.542   0.68 16.10 ?  22  ASP   A CA   1 
ATOM   591  C  CA   B ASP   A 1 22  ? 13.269 1.811   8.900   0.32 14.40 ?  22  ASP   A CA   1 
ATOM   592  C  C    A ASP   A 1 22  ? 14.362 1.544   10.117  0.68 14.66 ?  22  ASP   A C    1 
ATOM   593  C  C    B ASP   A 1 22  ? 14.502 1.200   9.560   0.32 13.46 ?  22  ASP   A C    1 
ATOM   594  O  O    A ASP   A 1 22  ? 14.549 1.538   11.338  0.68 15.10 ?  22  ASP   A O    1 
ATOM   595  O  O    B ASP   A 1 22  ? 14.588 1.135   10.789  0.32 13.37 ?  22  ASP   A O    1 
ATOM   596  C  CB   A ASP   A 1 22  ? 12.698 3.435   10.037  0.68 18.11 ?  22  ASP   A CB   1 
ATOM   597  C  CB   B ASP   A 1 22  ? 13.193 3.310   9.208   0.32 15.45 ?  22  ASP   A CB   1 
ATOM   598  C  CG   A ASP   A 1 22  ? 13.709 4.483   9.603   0.68 20.44 ?  22  ASP   A CG   1 
ATOM   599  C  CG   B ASP   A 1 22  ? 14.295 4.125   8.552   0.32 16.15 ?  22  ASP   A CG   1 
ATOM   600  O  OD1  A ASP   A 1 22  ? 14.806 4.127   9.128   0.68 21.26 ?  22  ASP   A OD1  1 
ATOM   601  O  OD1  B ASP   A 1 22  ? 15.262 3.543   8.025   0.32 15.93 ?  22  ASP   A OD1  1 
ATOM   602  O  OD2  A ASP   A 1 22  ? 13.397 5.683   9.746   0.68 22.01 -1 22  ASP   A OD2  1 
ATOM   603  O  OD2  B ASP   A 1 22  ? 14.190 5.372   8.577   0.32 16.79 -1 22  ASP   A OD2  1 
ATOM   604  H  H    A ASP   A 1 22  ? 11.578 1.394   10.693  0.68 19.03 ?  22  ASP   A H    1 
ATOM   605  H  H    B ASP   A 1 22  ? 11.585 1.690   9.923   0.32 17.42 ?  22  ASP   A H    1 
ATOM   606  H  HA   A ASP   A 1 22  ? 13.089 2.035   8.575   0.68 19.32 ?  22  ASP   A HA   1 
ATOM   607  H  HA   B ASP   A 1 22  ? 13.311 1.676   7.938   0.32 17.29 ?  22  ASP   A HA   1 
ATOM   608  H  HB2  A ASP   A 1 22  ? 11.829 3.694   9.689   0.68 21.74 ?  22  ASP   A HB2  1 
ATOM   609  H  HB2  B ASP   A 1 22  ? 12.348 3.653   8.892   0.32 18.55 ?  22  ASP   A HB2  1 
ATOM   610  H  HB3  A ASP   A 1 22  ? 12.675 3.434   11.008  0.68 21.74 ?  22  ASP   A HB3  1 
ATOM   611  H  HB3  B ASP   A 1 22  ? 13.273 3.433   10.164  0.32 18.55 ?  22  ASP   A HB3  1 
ATOM   612  N  N    A ILE   A 1 23  ? 15.276 1.120   9.238   0.68 14.04 ?  23  ILE   A N    1 
ATOM   613  N  N    B ILE   A 1 23  ? 15.452 0.731   8.743   0.32 13.01 ?  23  ILE   A N    1 
ATOM   614  C  CA   A ILE   A 1 23  ? 16.528 0.507   9.678   0.68 13.62 ?  23  ILE   A CA   1 
ATOM   615  C  CA   B ILE   A 1 23  ? 16.661 0.115   9.289   0.32 12.46 ?  23  ILE   A CA   1 
ATOM   616  C  C    A ILE   A 1 23  ? 17.327 1.458   10.556  0.68 13.88 ?  23  ILE   A C    1 
ATOM   617  C  C    B ILE   A 1 23  ? 17.391 1.081   10.210  0.32 13.09 ?  23  ILE   A C    1 
ATOM   618  O  O    A ILE   A 1 23  ? 18.058 1.020   11.453  0.68 14.35 ?  23  ILE   A O    1 
ATOM   619  O  O    B ILE   A 1 23  ? 18.009 0.664   11.197  0.32 13.27 ?  23  ILE   A O    1 
ATOM   620  C  CB   A ILE   A 1 23  ? 17.335 0.006   8.461   0.68 13.54 ?  23  ILE   A CB   1 
ATOM   621  C  CB   B ILE   A 1 23  ? 17.580 -0.433  8.173   0.32 11.97 ?  23  ILE   A CB   1 
ATOM   622  C  CG1  A ILE   A 1 23  ? 18.479 -0.903  8.911   0.68 13.53 ?  23  ILE   A CG1  1 
ATOM   623  C  CG1  B ILE   A 1 23  ? 18.659 -1.342  8.775   0.32 11.70 ?  23  ILE   A CG1  1 
ATOM   624  C  CG2  A ILE   A 1 23  ? 17.839 1.179   7.617   0.68 13.77 ?  23  ILE   A CG2  1 
ATOM   625  C  CG2  B ILE   A 1 23  ? 18.225 0.701   7.383   0.32 11.84 ?  23  ILE   A CG2  1 
ATOM   626  C  CD1  A ILE   A 1 23  ? 19.146 -1.641  7.771   0.68 13.53 ?  23  ILE   A CD1  1 
ATOM   627  C  CD1  B ILE   A 1 23  ? 19.552 -2.021  7.747   0.32 11.74 ?  23  ILE   A CD1  1 
ATOM   628  H  H    A ILE   A 1 23  ? 15.186 1.176   8.387   0.68 16.86 ?  23  ILE   A H    1 
ATOM   629  H  H    B ILE   A 1 23  ? 15.417 0.753   7.892   0.32 15.62 ?  23  ILE   A H    1 
ATOM   630  H  HA   A ILE   A 1 23  ? 16.314 -0.268  10.217  0.68 16.35 ?  23  ILE   A HA   1 
ATOM   631  H  HA   B ILE   A 1 23  ? 16.392 -0.645  9.826   0.32 14.96 ?  23  ILE   A HA   1 
ATOM   632  H  HB   A ILE   A 1 23  ? 16.738 -0.519  7.906   0.68 16.26 ?  23  ILE   A HB   1 
ATOM   633  H  HB   B ILE   A 1 23  ? 17.044 -0.965  7.564   0.32 14.37 ?  23  ILE   A HB   1 
ATOM   634  H  HG12 A ILE   A 1 23  ? 19.156 -0.364  9.350   0.68 16.24 ?  23  ILE   A HG12 1 
ATOM   635  H  HG12 B ILE   A 1 23  ? 19.231 -0.813  9.353   0.32 14.05 ?  23  ILE   A HG12 1 
ATOM   636  H  HG13 A ILE   A 1 23  ? 18.131 -1.563  9.529   0.68 16.24 ?  23  ILE   A HG13 1 
ATOM   637  H  HG13 B ILE   A 1 23  ? 18.228 -2.040  9.294   0.32 14.05 ?  23  ILE   A HG13 1 
ATOM   638  H  HG21 A ILE   A 1 23  ? 18.196 0.840   6.781   0.68 16.53 ?  23  ILE   A HG21 1 
ATOM   639  H  HG21 B ILE   A 1 23  ? 18.628 0.334   6.576   0.32 14.22 ?  23  ILE   A HG21 1 
ATOM   640  H  HG22 A ILE   A 1 23  ? 17.095 1.780   7.434   0.68 16.53 ?  23  ILE   A HG22 1 
ATOM   641  H  HG22 B ILE   A 1 23  ? 17.545 1.346   7.146   0.32 14.22 ?  23  ILE   A HG22 1 
ATOM   642  H  HG23 A ILE   A 1 23  ? 18.529 1.652   8.105   0.68 16.53 ?  23  ILE   A HG23 1 
ATOM   643  H  HG23 B ILE   A 1 23  ? 18.909 1.120   7.928   0.32 14.22 ?  23  ILE   A HG23 1 
ATOM   644  H  HD11 A ILE   A 1 23  ? 19.819 -2.237  8.132   0.68 16.24 ?  23  ILE   A HD11 1 
ATOM   645  H  HD11 B ILE   A 1 23  ? 20.139 -2.648  8.203   0.32 14.09 ?  23  ILE   A HD11 1 
ATOM   646  H  HD12 A ILE   A 1 23  ? 18.473 -2.152  7.293   0.68 16.24 ?  23  ILE   A HD12 1 
ATOM   647  H  HD12 B ILE   A 1 23  ? 18.995 -2.496  7.111   0.32 14.09 ?  23  ILE   A HD12 1 
ATOM   648  H  HD13 A ILE   A 1 23  ? 19.557 -0.997  7.175   0.68 16.24 ?  23  ILE   A HD13 1 
ATOM   649  H  HD13 B ILE   A 1 23  ? 20.079 -1.349  7.290   0.32 14.09 ?  23  ILE   A HD13 1 
ATOM   650  N  N    A VAL   A 1 24  ? 17.200 2.765   10.324  0.68 14.64 ?  24  VAL   A N    1 
ATOM   651  N  N    B VAL   A 1 24  ? 17.327 2.380   9.913   0.32 14.06 ?  24  VAL   A N    1 
ATOM   652  C  CA   A VAL   A 1 24  ? 17.883 3.736   11.174  0.68 15.93 ?  24  VAL   A CA   1 
ATOM   653  C  CA   B VAL   A 1 24  ? 17.969 3.371   10.771  0.32 15.28 ?  24  VAL   A CA   1 
ATOM   654  C  C    A VAL   A 1 24  ? 17.351 3.660   12.598  0.68 16.57 ?  24  VAL   A C    1 
ATOM   655  C  C    B VAL   A 1 24  ? 17.322 3.377   12.148  0.32 16.04 ?  24  VAL   A C    1 
ATOM   656  O  O    A VAL   A 1 24  ? 18.117 3.584   13.568  0.68 17.00 ?  24  VAL   A O    1 
ATOM   657  O  O    B VAL   A 1 24  ? 18.011 3.426   13.174  0.32 16.71 ?  24  VAL   A O    1 
ATOM   658  C  CB   A VAL   A 1 24  ? 17.737 5.152   10.589  0.68 16.79 ?  24  VAL   A CB   1 
ATOM   659  C  CB   B VAL   A 1 24  ? 17.926 4.756   10.100  0.32 15.97 ?  24  VAL   A CB   1 
ATOM   660  C  CG1  A VAL   A 1 24  ? 18.224 6.196   11.586  0.68 17.31 ?  24  VAL   A CG1  1 
ATOM   661  C  CG1  B VAL   A 1 24  ? 18.598 5.791   10.978  0.32 16.54 ?  24  VAL   A CG1  1 
ATOM   662  C  CG2  A VAL   A 1 24  ? 18.493 5.257   9.275   0.68 17.42 ?  24  VAL   A CG2  1 
ATOM   663  C  CG2  B VAL   A 1 24  ? 18.588 4.690   8.736   0.32 16.02 ?  24  VAL   A CG2  1 
ATOM   664  H  H    A VAL   A 1 24  ? 16.729 3.110   9.690   0.68 17.58 ?  24  VAL   A H    1 
ATOM   665  H  H    B VAL   A 1 24  ? 16.920 2.708   9.233   0.32 16.88 ?  24  VAL   A H    1 
ATOM   666  H  HA   A VAL   A 1 24  ? 18.827 3.524   11.195  0.68 19.12 ?  24  VAL   A HA   1 
ATOM   667  H  HA   B VAL   A 1 24  ? 18.900 3.128   10.885  0.32 18.34 ?  24  VAL   A HA   1 
ATOM   668  H  HB   A VAL   A 1 24  ? 16.801 5.327   10.404  0.68 20.15 ?  24  VAL   A HB   1 
ATOM   669  H  HB   B VAL   A 1 24  ? 17.001 5.020   9.973   0.32 19.16 ?  24  VAL   A HB   1 
ATOM   670  H  HG11 A VAL   A 1 24  ? 18.383 7.029   11.115  0.68 20.77 ?  24  VAL   A HG11 1 
ATOM   671  H  HG11 B VAL   A 1 24  ? 18.769 6.589   10.455  0.32 19.86 ?  24  VAL   A HG11 1 
ATOM   672  H  HG12 A VAL   A 1 24  ? 17.547 6.324   12.266  0.68 20.77 ?  24  VAL   A HG12 1 
ATOM   673  H  HG12 B VAL   A 1 24  ? 18.002 5.999   11.714  0.32 19.86 ?  24  VAL   A HG12 1 
ATOM   674  H  HG13 A VAL   A 1 24  ? 19.050 5.883   11.988  0.68 20.77 ?  24  VAL   A HG13 1 
ATOM   675  H  HG13 B VAL   A 1 24  ? 19.433 5.429   11.315  0.32 19.86 ?  24  VAL   A HG13 1 
ATOM   676  H  HG21 A VAL   A 1 24  ? 18.206 6.057   8.805   0.68 20.91 ?  24  VAL   A HG21 1 
ATOM   677  H  HG21 B VAL   A 1 24  ? 18.689 5.589   8.390   0.32 19.23 ?  24  VAL   A HG21 1 
ATOM   678  H  HG22 A VAL   A 1 24  ? 19.445 5.314   9.460   0.68 20.91 ?  24  VAL   A HG22 1 
ATOM   679  H  HG22 B VAL   A 1 24  ? 19.459 4.272   8.829   0.32 19.23 ?  24  VAL   A HG22 1 
ATOM   680  H  HG23 A VAL   A 1 24  ? 18.308 4.475   8.731   0.68 20.91 ?  24  VAL   A HG23 1 
ATOM   681  H  HG23 B VAL   A 1 24  ? 18.034 4.164   8.139   0.32 19.23 ?  24  VAL   A HG23 1 
ATOM   682  N  N    A GLU   A 1 25  ? 16.026 3.691   12.743  0.68 17.03 ?  25  GLU   A N    1 
ATOM   683  N  N    B GLU   A 1 25  ? 15.989 3.310   12.197  0.32 16.51 ?  25  GLU   A N    1 
ATOM   684  C  CA   A GLU   A 1 25  ? 15.429 3.625   14.071  0.68 18.36 ?  25  GLU   A CA   1 
ATOM   685  C  CA   B GLU   A 1 25  ? 15.302 3.258   13.483  0.32 17.54 ?  25  GLU   A CA   1 
ATOM   686  C  C    A GLU   A 1 25  ? 15.672 2.268   14.717  0.68 17.39 ?  25  GLU   A C    1 
ATOM   687  C  C    B GLU   A 1 25  ? 15.572 1.942   14.203  0.32 17.56 ?  25  GLU   A C    1 
ATOM   688  O  O    A GLU   A 1 25  ? 15.907 2.186   15.928  0.68 17.68 ?  25  GLU   A O    1 
ATOM   689  O  O    B GLU   A 1 25  ? 15.756 1.924   15.425  0.32 17.81 ?  25  GLU   A O    1 
ATOM   690  C  CB   A GLU   A 1 25  ? 13.937 3.960   13.991  0.68 20.70 ?  25  GLU   A CB   1 
ATOM   691  C  CB   B GLU   A 1 25  ? 13.803 3.490   13.289  0.32 18.91 ?  25  GLU   A CB   1 
ATOM   692  C  CG   A GLU   A 1 25  ? 13.674 5.422   13.648  0.68 23.61 ?  25  GLU   A CG   1 
ATOM   693  C  CG   B GLU   A 1 25  ? 13.476 4.883   12.768  0.32 20.66 ?  25  GLU   A CG   1 
ATOM   694  C  CD   A GLU   A 1 25  ? 14.457 6.380   14.529  0.68 25.92 ?  25  GLU   A CD   1 
ATOM   695  C  CD   B GLU   A 1 25  ? 13.945 5.982   13.703  0.32 22.15 ?  25  GLU   A CD   1 
ATOM   696  O  OE1  A GLU   A 1 25  ? 14.538 6.139   15.753  0.68 26.60 ?  25  GLU   A OE1  1 
ATOM   697  O  OE1  B GLU   A 1 25  ? 13.843 5.798   14.935  0.32 22.94 ?  25  GLU   A OE1  1 
ATOM   698  O  OE2  A GLU   A 1 25  ? 15.012 7.360   13.992  0.68 27.16 -1 25  GLU   A OE2  1 
ATOM   699  O  OE2  B GLU   A 1 25  ? 14.425 7.022   13.206  0.32 22.79 -1 25  GLU   A OE2  1 
ATOM   700  H  H    A GLU   A 1 25  ? 15.460 3.760   12.097  0.68 20.44 ?  25  GLU   A H    1 
ATOM   701  H  H    B GLU   A 1 25  ? 15.472 3.295   11.509  0.32 19.81 ?  25  GLU   A H    1 
ATOM   702  H  HA   A GLU   A 1 25  ? 15.855 4.285   14.637  0.68 22.04 ?  25  GLU   A HA   1 
ATOM   703  H  HA   B GLU   A 1 25  ? 15.643 3.970   14.042  0.32 21.05 ?  25  GLU   A HA   1 
ATOM   704  H  HB2  A GLU   A 1 25  ? 13.522 3.418   13.299  0.68 24.84 ?  25  GLU   A HB2  1 
ATOM   705  H  HB2  B GLU   A 1 25  ? 13.464 2.845   12.646  0.32 22.70 ?  25  GLU   A HB2  1 
ATOM   706  H  HB3  A GLU   A 1 25  ? 13.518 3.778   14.847  0.68 24.84 ?  25  GLU   A HB3  1 
ATOM   707  H  HB3  B GLU   A 1 25  ? 13.354 3.376   14.140  0.32 22.70 ?  25  GLU   A HB3  1 
ATOM   708  H  HG2  A GLU   A 1 25  ? 13.943 5.587   12.733  0.68 28.33 ?  25  GLU   A HG2  1 
ATOM   709  H  HG2  B GLU   A 1 25  ? 13.920 5.014   11.915  0.32 24.80 ?  25  GLU   A HG2  1 
ATOM   710  H  HG3  A GLU   A 1 25  ? 12.728 5.610   13.759  0.68 28.33 ?  25  GLU   A HG3  1 
ATOM   711  H  HG3  B GLU   A 1 25  ? 12.516 4.963   12.661  0.32 24.80 ?  25  GLU   A HG3  1 
ATOM   712  N  N    A GLU   A 1 26  ? 15.636 1.194   13.925  0.68 16.84 ?  26  GLU   A N    1 
ATOM   713  N  N    B GLU   A 1 26  ? 15.604 0.829   13.466  0.32 17.27 ?  26  GLU   A N    1 
ATOM   714  C  CA   A GLU   A 1 26  ? 15.929 -0.130  14.465  0.68 16.55 ?  26  GLU   A CA   1 
ATOM   715  C  CA   B GLU   A 1 26  ? 15.955 -0.447  14.081  0.32 17.41 ?  26  GLU   A CA   1 
ATOM   716  C  C    A GLU   A 1 26  ? 17.352 -0.194  15.003  0.68 15.65 ?  26  GLU   A C    1 
ATOM   717  C  C    B GLU   A 1 26  ? 17.370 -0.413  14.640  0.32 16.95 ?  26  GLU   A C    1 
ATOM   718  O  O    A GLU   A 1 26  ? 17.591 -0.691  16.109  0.68 15.86 ?  26  GLU   A O    1 
ATOM   719  O  O    B GLU   A 1 26  ? 17.640 -0.979  15.706  0.32 16.92 ?  26  GLU   A O    1 
ATOM   720  C  CB   A GLU   A 1 26  ? 15.731 -1.192  13.384  0.68 17.89 ?  26  GLU   A CB   1 
ATOM   721  C  CB   B GLU   A 1 26  ? 15.814 -1.583  13.067  0.32 17.89 ?  26  GLU   A CB   1 
ATOM   722  C  CG   A GLU   A 1 26  ? 14.325 -1.727  13.259  0.68 21.02 ?  26  GLU   A CG   1 
ATOM   723  C  CG   B GLU   A 1 26  ? 14.381 -1.992  12.796  0.32 18.27 ?  26  GLU   A CG   1 
ATOM   724  C  CD   A GLU   A 1 26  ? 13.910 -2.564  14.458  0.68 22.96 ?  26  GLU   A CD   1 
ATOM   725  C  CD   B GLU   A 1 26  ? 13.675 -2.511  14.030  0.32 18.45 ?  26  GLU   A CD   1 
ATOM   726  O  OE1  A GLU   A 1 26  ? 14.404 -3.706  14.624  0.68 23.69 ?  26  GLU   A OE1  1 
ATOM   727  O  OE1  B GLU   A 1 26  ? 14.171 -3.481  14.643  0.32 19.39 ?  26  GLU   A OE1  1 
ATOM   728  O  OE2  A GLU   A 1 26  ? 13.088 -2.064  15.242  0.68 24.29 -1 26  GLU   A OE2  1 
ATOM   729  O  OE2  B GLU   A 1 26  ? 12.627 -1.938  14.392  0.32 17.14 -1 26  GLU   A OE2  1 
ATOM   730  H  H    A GLU   A 1 26  ? 15.453 1.213   13.086  0.68 20.21 ?  26  GLU   A H    1 
ATOM   731  H  H    B GLU   A 1 26  ? 15.429 0.785   12.626  0.32 20.73 ?  26  GLU   A H    1 
ATOM   732  H  HA   A GLU   A 1 26  ? 15.319 -0.315  15.194  0.68 19.86 ?  26  GLU   A HA   1 
ATOM   733  H  HA   B GLU   A 1 26  ? 15.354 -0.622  14.819  0.32 20.90 ?  26  GLU   A HA   1 
ATOM   734  H  HB2  A GLU   A 1 26  ? 15.976 -0.808  12.527  0.68 21.47 ?  26  GLU   A HB2  1 
ATOM   735  H  HB2  B GLU   A 1 26  ? 16.202 -1.300  12.222  0.32 21.48 ?  26  GLU   A HB2  1 
ATOM   736  H  HB3  A GLU   A 1 26  ? 16.314 -1.939  13.584  0.68 21.47 ?  26  GLU   A HB3  1 
ATOM   737  H  HB3  B GLU   A 1 26  ? 16.288 -2.363  13.398  0.32 21.48 ?  26  GLU   A HB3  1 
ATOM   738  H  HG2  A GLU   A 1 26  ? 13.710 -0.978  13.178  0.68 25.23 ?  26  GLU   A HG2  1 
ATOM   739  H  HG2  B GLU   A 1 26  ? 13.886 -1.222  12.485  0.32 21.93 ?  26  GLU   A HG2  1 
ATOM   740  H  HG3  A GLU   A 1 26  ? 14.266 -2.286  12.469  0.68 25.23 ?  26  GLU   A HG3  1 
ATOM   741  H  HG3  B GLU   A 1 26  ? 14.373 -2.693  12.127  0.32 21.93 ?  26  GLU   A HG3  1 
ATOM   742  N  N    A ALA   A 1 27  ? 18.317 0.302   14.226  0.68 14.88 ?  27  ALA   A N    1 
ATOM   743  N  N    B ALA   A 1 27  ? 18.292 0.242   13.933  0.32 16.27 ?  27  ALA   A N    1 
ATOM   744  C  CA   A ALA   A 1 27  ? 19.709 0.252   14.664  0.68 15.42 ?  27  ALA   A CA   1 
ATOM   745  C  CA   B ALA   A 1 27  ? 19.665 0.317   14.420  0.32 16.26 ?  27  ALA   A CA   1 
ATOM   746  C  C    A ALA   A 1 27  ? 19.912 1.038   15.953  0.68 16.89 ?  27  ALA   A C    1 
ATOM   747  C  C    B ALA   A 1 27  ? 19.761 1.196   15.664  0.32 16.89 ?  27  ALA   A C    1 
ATOM   748  O  O    A ALA   A 1 27  ? 20.601 0.577   16.870  0.68 17.14 ?  27  ALA   A O    1 
ATOM   749  O  O    B ALA   A 1 27  ? 20.409 0.826   16.650  0.32 16.77 ?  27  ALA   A O    1 
ATOM   750  C  CB   A ALA   A 1 27  ? 20.632 0.776   13.560  0.68 14.90 ?  27  ALA   A CB   1 
ATOM   751  C  CB   B ALA   A 1 27  ? 20.590 0.825   13.314  0.32 15.95 ?  27  ALA   A CB   1 
ATOM   752  H  H    A ALA   A 1 27  ? 18.196 0.670   13.458  0.68 17.86 ?  27  ALA   A H    1 
ATOM   753  H  H    B ALA   A 1 27  ? 18.150 0.638   13.179  0.32 19.53 ?  27  ALA   A H    1 
ATOM   754  H  HA   A ALA   A 1 27  ? 19.949 -0.670  14.837  0.68 18.51 ?  27  ALA   A HA   1 
ATOM   755  H  HA   B ALA   A 1 27  ? 19.956 -0.575  14.661  0.32 19.52 ?  27  ALA   A HA   1 
ATOM   756  H  HB1  A ALA   A 1 27  ? 21.553 0.732   13.869  0.68 17.88 ?  27  ALA   A HB1  1 
ATOM   757  H  HB1  B ALA   A 1 27  ? 21.496 0.868   13.658  0.32 19.14 ?  27  ALA   A HB1  1 
ATOM   758  H  HB2  A ALA   A 1 27  ? 20.525 0.224   12.769  0.68 17.88 ?  27  ALA   A HB2  1 
ATOM   759  H  HB2  B ALA   A 1 27  ? 20.551 0.211   12.562  0.32 19.14 ?  27  ALA   A HB2  1 
ATOM   760  H  HB3  A ALA   A 1 27  ? 20.397 1.694   13.357  0.68 17.88 ?  27  ALA   A HB3  1 
ATOM   761  H  HB3  B ALA   A 1 27  ? 20.298 1.706   13.036  0.32 19.14 ?  27  ALA   A HB3  1 
ATOM   762  N  N    A LYS   A 1 28  ? 19.315 2.227   16.046  0.68 18.60 ?  28  LYS   A N    1 
ATOM   763  N  N    B LYS   A 1 28  ? 19.108 2.361   15.640  0.32 18.07 ?  28  LYS   A N    1 
ATOM   764  C  CA   A LYS   A 1 28  ? 19.462 3.026   17.259  0.68 21.03 ?  28  LYS   A CA   1 
ATOM   765  C  CA   B LYS   A 1 28  ? 19.187 3.283   16.770  0.32 19.76 ?  28  LYS   A CA   1 
ATOM   766  C  C    A LYS   A 1 28  ? 18.904 2.297   18.476  0.68 22.15 ?  28  LYS   A C    1 
ATOM   767  C  C    B LYS   A 1 28  ? 18.737 2.634   18.071  0.32 20.83 ?  28  LYS   A C    1 
ATOM   768  O  O    A LYS   A 1 28  ? 19.463 2.393   19.574  0.68 23.28 ?  28  LYS   A O    1 
ATOM   769  O  O    B LYS   A 1 28  ? 19.266 2.961   19.140  0.32 20.85 ?  28  LYS   A O    1 
ATOM   770  C  CB   A LYS   A 1 28  ? 18.811 4.399   17.077  0.68 22.92 ?  28  LYS   A CB   1 
ATOM   771  C  CB   B LYS   A 1 28  ? 18.340 4.526   16.494  0.32 20.71 ?  28  LYS   A CB   1 
ATOM   772  C  CG   A LYS   A 1 28  ? 19.614 5.329   16.175  0.68 24.64 ?  28  LYS   A CG   1 
ATOM   773  C  CG   B LYS   A 1 28  ? 18.916 5.457   15.445  0.32 21.64 ?  28  LYS   A CG   1 
ATOM   774  C  CD   A LYS   A 1 28  ? 19.139 6.772   16.253  0.68 26.70 ?  28  LYS   A CD   1 
ATOM   775  C  CD   B LYS   A 1 28  ? 18.046 6.693   15.285  0.32 22.55 ?  28  LYS   A CD   1 
ATOM   776  C  CE   A LYS   A 1 28  ? 17.839 6.969   15.502  0.68 28.29 ?  28  LYS   A CE   1 
ATOM   777  C  CE   B LYS   A 1 28  ? 18.589 7.636   14.223  0.32 23.21 ?  28  LYS   A CE   1 
ATOM   778  N  NZ   A LYS   A 1 28  ? 17.457 8.405   15.440  0.68 29.23 ?  28  LYS   A NZ   1 
ATOM   779  N  NZ   B LYS   A 1 28  ? 17.814 8.907   14.160  0.32 23.46 ?  28  LYS   A NZ   1 
ATOM   780  H  H    A LYS   A 1 28  ? 18.837 2.587   15.435  0.68 22.32 ?  28  LYS   A H    1 
ATOM   781  H  H    B LYS   A 1 28  ? 18.622 2.639   14.990  0.32 21.69 ?  28  LYS   A H    1 
ATOM   782  H  HA   A LYS   A 1 28  ? 20.404 3.171   17.430  0.68 25.25 ?  28  LYS   A HA   1 
ATOM   783  H  HA   B LYS   A 1 28  ? 20.105 3.567   16.884  0.32 23.72 ?  28  LYS   A HA   1 
ATOM   784  H  HB2  A LYS   A 1 28  ? 17.936 4.287   16.677  0.68 27.51 ?  28  LYS   A HB2  1 
ATOM   785  H  HB2  B LYS   A 1 28  ? 17.464 4.244   16.188  0.32 24.85 ?  28  LYS   A HB2  1 
ATOM   786  H  HB3  A LYS   A 1 28  ? 18.727 4.831   17.942  0.68 27.51 ?  28  LYS   A HB3  1 
ATOM   787  H  HB3  B LYS   A 1 28  ? 18.251 5.031   17.317  0.32 24.85 ?  28  LYS   A HB3  1 
ATOM   788  H  HG2  A LYS   A 1 28  ? 20.545 5.306   16.443  0.68 29.57 ?  28  LYS   A HG2  1 
ATOM   789  H  HG2  B LYS   A 1 28  ? 19.801 5.741   15.720  0.32 25.98 ?  28  LYS   A HG2  1 
ATOM   790  H  HG3  A LYS   A 1 28  ? 19.524 5.034   15.256  0.68 29.57 ?  28  LYS   A HG3  1 
ATOM   791  H  HG3  B LYS   A 1 28  ? 18.962 5.000   14.591  0.32 25.98 ?  28  LYS   A HG3  1 
ATOM   792  H  HD2  A LYS   A 1 28  ? 18.993 7.013   17.181  0.68 32.05 ?  28  LYS   A HD2  1 
ATOM   793  H  HD2  B LYS   A 1 28  ? 17.152 6.423   15.023  0.32 27.06 ?  28  LYS   A HD2  1 
ATOM   794  H  HD3  A LYS   A 1 28  ? 19.809 7.352   15.858  0.68 32.05 ?  28  LYS   A HD3  1 
ATOM   795  H  HD3  B LYS   A 1 28  ? 18.017 7.173   16.127  0.32 27.06 ?  28  LYS   A HD3  1 
ATOM   796  H  HE2  A LYS   A 1 28  ? 17.942 6.642   14.594  0.68 33.96 ?  28  LYS   A HE2  1 
ATOM   797  H  HE2  B LYS   A 1 28  ? 19.511 7.852   14.430  0.32 27.85 ?  28  LYS   A HE2  1 
ATOM   798  H  HE3  A LYS   A 1 28  ? 17.132 6.485   15.955  0.68 33.96 ?  28  LYS   A HE3  1 
ATOM   799  H  HE3  B LYS   A 1 28  ? 18.537 7.206   13.356  0.32 27.85 ?  28  LYS   A HE3  1 
ATOM   800  H  HZ1  A LYS   A 1 28  ? 16.693 8.498   14.995  0.68 35.08 ?  28  LYS   A HZ1  1 
ATOM   801  H  HZ1  B LYS   A 1 28  ? 18.151 9.438   13.531  0.32 28.15 ?  28  LYS   A HZ1  1 
ATOM   802  H  HZ2  A LYS   A 1 28  ? 17.355 8.729   16.263  0.68 35.08 ?  28  LYS   A HZ2  1 
ATOM   803  H  HZ2  B LYS   A 1 28  ? 16.962 8.734   13.967  0.32 28.15 ?  28  LYS   A HZ2  1 
ATOM   804  H  HZ3  A LYS   A 1 28  ? 18.092 8.871   15.024  0.68 35.08 ?  28  LYS   A HZ3  1 
ATOM   805  H  HZ3  B LYS   A 1 28  ? 17.854 9.324   14.945  0.32 28.15 ?  28  LYS   A HZ3  1 
ATOM   806  N  N    A LYS   A 1 29  ? 17.817 1.544   18.297  0.68 22.95 ?  29  LYS   A N    1 
ATOM   807  N  N    B LYS   A 1 29  ? 17.766 1.724   18.008  0.32 22.04 ?  29  LYS   A N    1 
ATOM   808  C  CA   A LYS   A 1 29  ? 17.208 0.833   19.419  0.68 24.72 ?  29  LYS   A CA   1 
ATOM   809  C  CA   B LYS   A 1 29  ? 17.209 1.107   19.205  0.32 23.64 ?  29  LYS   A CA   1 
ATOM   810  C  C    A LYS   A 1 29  ? 18.014 -0.403  19.803  0.68 24.52 ?  29  LYS   A C    1 
ATOM   811  C  C    B LYS   A 1 29  ? 17.986 -0.135  19.631  0.32 23.72 ?  29  LYS   A C    1 
ATOM   812  O  O    A LYS   A 1 29  ? 18.292 -0.632  20.986  0.68 25.22 ?  29  LYS   A O    1 
ATOM   813  O  O    B LYS   A 1 29  ? 18.303 -0.295  20.813  0.32 24.26 ?  29  LYS   A O    1 
ATOM   814  C  CB   A LYS   A 1 29  ? 15.776 0.428   19.062  0.68 27.14 ?  29  LYS   A CB   1 
ATOM   815  C  CB   B LYS   A 1 29  ? 15.740 0.748   18.963  0.32 25.12 ?  29  LYS   A CB   1 
ATOM   816  C  CG   A LYS   A 1 29  ? 15.022 -0.269  20.188  0.68 29.52 ?  29  LYS   A CG   1 
ATOM   817  C  CG   B LYS   A 1 29  ? 15.010 0.204   20.181  0.32 26.48 ?  29  LYS   A CG   1 
ATOM   818  C  CD   A LYS   A 1 29  ? 14.691 0.696   21.316  0.68 31.56 ?  29  LYS   A CD   1 
ATOM   819  C  CD   B LYS   A 1 29  ? 14.909 1.245   21.282  0.32 27.70 ?  29  LYS   A CD   1 
ATOM   820  C  CE   A LYS   A 1 29  ? 13.812 0.041   22.371  0.68 32.97 ?  29  LYS   A CE   1 
ATOM   821  C  CE   B LYS   A 1 29  ? 13.896 0.830   22.337  0.32 28.60 ?  29  LYS   A CE   1 
ATOM   822  N  NZ   A LYS   A 1 29  ? 13.378 1.015   23.412  0.68 33.85 ?  29  LYS   A NZ   1 
ATOM   823  N  NZ   B LYS   A 1 29  ? 13.809 1.819   23.446  0.32 29.09 ?  29  LYS   A NZ   1 
ATOM   824  H  H    A LYS   A 1 29  ? 17.416 1.427   17.546  0.68 27.55 ?  29  LYS   A H    1 
ATOM   825  H  H    B LYS   A 1 29  ? 17.407 1.448   17.276  0.32 26.45 ?  29  LYS   A H    1 
ATOM   826  H  HA   A LYS   A 1 29  ? 17.169 1.422   20.190  0.68 29.67 ?  29  LYS   A HA   1 
ATOM   827  H  HA   B LYS   A 1 29  ? 17.247 1.743   19.934  0.32 28.37 ?  29  LYS   A HA   1 
ATOM   828  H  HB2  A LYS   A 1 29  ? 15.275 1.222   18.824  0.68 32.57 ?  29  LYS   A HB2  1 
ATOM   829  H  HB2  B LYS   A 1 29  ? 15.272 1.545   18.674  0.32 30.14 ?  29  LYS   A HB2  1 
ATOM   830  H  HB3  A LYS   A 1 29  ? 15.803 -0.182  18.309  0.68 32.57 ?  29  LYS   A HB3  1 
ATOM   831  H  HB3  B LYS   A 1 29  ? 15.697 0.072   18.270  0.32 30.14 ?  29  LYS   A HB3  1 
ATOM   832  H  HG2  A LYS   A 1 29  ? 14.189 -0.625  19.842  0.68 35.43 ?  29  LYS   A HG2  1 
ATOM   833  H  HG2  B LYS   A 1 29  ? 14.111 -0.053  19.924  0.32 31.78 ?  29  LYS   A HG2  1 
ATOM   834  H  HG3  A LYS   A 1 29  ? 15.564 -0.988  20.552  0.68 35.43 ?  29  LYS   A HG3  1 
ATOM   835  H  HG3  B LYS   A 1 29  ? 15.490 -0.564  20.531  0.32 31.78 ?  29  LYS   A HG3  1 
ATOM   836  H  HD2  A LYS   A 1 29  ? 15.513 0.987   21.741  0.68 37.88 ?  29  LYS   A HD2  1 
ATOM   837  H  HD2  B LYS   A 1 29  ? 15.774 1.343   21.712  0.32 33.24 ?  29  LYS   A HD2  1 
ATOM   838  H  HD3  A LYS   A 1 29  ? 14.213 1.459   20.953  0.68 37.88 ?  29  LYS   A HD3  1 
ATOM   839  H  HD3  B LYS   A 1 29  ? 14.625 2.090   20.900  0.32 33.24 ?  29  LYS   A HD3  1 
ATOM   840  H  HE2  A LYS   A 1 29  ? 13.020 -0.322  21.945  0.68 39.57 ?  29  LYS   A HE2  1 
ATOM   841  H  HE2  B LYS   A 1 29  ? 13.020 0.759   21.925  0.32 34.33 ?  29  LYS   A HE2  1 
ATOM   842  H  HE3  A LYS   A 1 29  ? 14.313 -0.667  22.806  0.68 39.57 ?  29  LYS   A HE3  1 
ATOM   843  H  HE3  B LYS   A 1 29  ? 14.159 -0.025  22.712  0.32 34.33 ?  29  LYS   A HE3  1 
ATOM   844  H  HZ1  A LYS   A 1 29  ? 12.867 0.607   24.015  0.68 40.62 ?  29  LYS   A HZ1  1 
ATOM   845  H  HZ1  B LYS   A 1 29  ? 13.402 1.455   24.148  0.32 34.92 ?  29  LYS   A HZ1  1 
ATOM   846  H  HZ2  A LYS   A 1 29  ? 14.089 1.360   23.821  0.68 40.62 ?  29  LYS   A HZ2  1 
ATOM   847  H  HZ2  B LYS   A 1 29  ? 14.626 2.076   23.686  0.32 34.92 ?  29  LYS   A HZ2  1 
ATOM   848  H  HZ3  A LYS   A 1 29  ? 12.912 1.674   23.037  0.68 40.62 ?  29  LYS   A HZ3  1 
ATOM   849  H  HZ3  B LYS   A 1 29  ? 13.351 2.534   23.181  0.32 34.92 ?  29  LYS   A HZ3  1 
ATOM   850  N  N    A VAL   A 1 30  ? 18.370 -1.226  18.817  0.68 23.35 ?  30  VAL   A N    1 
ATOM   851  N  N    B VAL   A 1 30  ? 18.297 -1.019  18.682  0.32 23.43 ?  30  VAL   A N    1 
ATOM   852  C  CA   A VAL   A 1 30  ? 19.031 -2.495  19.102  0.68 22.51 ?  30  VAL   A CA   1 
ATOM   853  C  CA   B VAL   A 1 30  ? 18.893 -2.305  19.029  0.32 23.18 ?  30  VAL   A CA   1 
ATOM   854  C  C    A VAL   A 1 30  ? 20.527 -2.312  19.318  0.68 21.32 ?  30  VAL   A C    1 
ATOM   855  C  C    B VAL   A 1 30  ? 20.388 -2.170  19.297  0.32 22.86 ?  30  VAL   A C    1 
ATOM   856  O  O    A VAL   A 1 30  ? 21.136 -3.044  20.107  0.68 21.77 ?  30  VAL   A O    1 
ATOM   857  O  O    B VAL   A 1 30  ? 20.936 -2.855  20.168  0.32 22.91 ?  30  VAL   A O    1 
ATOM   858  C  CB   A VAL   A 1 30  ? 18.748 -3.491  17.963  0.68 23.10 ?  30  VAL   A CB   1 
ATOM   859  C  CB   B VAL   A 1 30  ? 18.600 -3.336  17.922  0.32 23.33 ?  30  VAL   A CB   1 
ATOM   860  C  CG1  A VAL   A 1 30  ? 19.532 -4.783  18.163  0.68 23.60 ?  30  VAL   A CG1  1 
ATOM   861  C  CG1  B VAL   A 1 30  ? 19.321 -4.645  18.206  0.32 23.56 ?  30  VAL   A CG1  1 
ATOM   862  C  CG2  A VAL   A 1 30  ? 17.258 -3.777  17.861  0.68 23.50 ?  30  VAL   A CG2  1 
ATOM   863  C  CG2  B VAL   A 1 30  ? 17.101 -3.566  17.794  0.32 23.39 ?  30  VAL   A CG2  1 
ATOM   864  H  H    A VAL   A 1 30  ? 18.223 -1.082  17.985  0.68 28.02 ?  30  VAL   A H    1 
ATOM   865  H  H    B VAL   A 1 30  ? 18.170 -0.901  17.839  0.32 28.12 ?  30  VAL   A H    1 
ATOM   866  H  HA   A VAL   A 1 30  ? 18.650 -2.869  19.913  0.68 27.02 ?  30  VAL   A HA   1 
ATOM   867  H  HA   B VAL   A 1 30  ? 18.473 -2.629  19.841  0.32 27.83 ?  30  VAL   A HA   1 
ATOM   868  H  HB   A VAL   A 1 30  ? 19.035 -3.101  17.122  0.68 27.73 ?  30  VAL   A HB   1 
ATOM   869  H  HB   B VAL   A 1 30  ? 18.926 -2.995  17.074  0.32 28.00 ?  30  VAL   A HB   1 
ATOM   870  H  HG11 A VAL   A 1 30  ? 19.175 -5.463  17.569  0.68 28.32 ?  30  VAL   A HG11 1 
ATOM   871  H  HG11 B VAL   A 1 30  ? 18.944 -5.340  17.644  0.32 28.28 ?  30  VAL   A HG11 1 
ATOM   872  H  HG12 A VAL   A 1 30  ? 20.466 -4.625  17.958  0.68 28.32 ?  30  VAL   A HG12 1 
ATOM   873  H  HG12 B VAL   A 1 30  ? 20.265 -4.538  18.009  0.32 28.28 ?  30  VAL   A HG12 1 
ATOM   874  H  HG13 A VAL   A 1 30  ? 19.436 -5.070  19.085  0.68 28.32 ?  30  VAL   A HG13 1 
ATOM   875  H  HG13 B VAL   A 1 30  ? 19.199 -4.875  19.140  0.32 28.28 ?  30  VAL   A HG13 1 
ATOM   876  H  HG21 A VAL   A 1 30  ? 17.109 -4.440  17.167  0.68 28.20 ?  30  VAL   A HG21 1 
ATOM   877  H  HG21 B VAL   A 1 30  ? 16.941 -4.244  17.118  0.32 28.08 ?  30  VAL   A HG21 1 
ATOM   878  H  HG22 A VAL   A 1 30  ? 16.944 -4.118  18.714  0.68 28.20 ?  30  VAL   A HG22 1 
ATOM   879  H  HG22 B VAL   A 1 30  ? 16.754 -3.865  18.649  0.32 28.08 ?  30  VAL   A HG22 1 
ATOM   880  H  HG23 A VAL   A 1 30  ? 16.793 -2.957  17.640  0.68 28.20 ?  30  VAL   A HG23 1 
ATOM   881  H  HG23 B VAL   A 1 30  ? 16.675 -2.735  17.536  0.32 28.08 ?  30  VAL   A HG23 1 
ATOM   882  N  N    A LYS   A 1 31  ? 21.139 -1.352  18.633  0.68 20.11 ?  31  LYS   A N    1 
ATOM   883  N  N    B LYS   A 1 31  ? 21.064 -1.290  18.568  0.32 22.57 ?  31  LYS   A N    1 
ATOM   884  C  CA   A LYS   A 1 31  ? 22.589 -1.222  18.574  0.68 20.80 ?  31  LYS   A CA   1 
ATOM   885  C  CA   B LYS   A 1 31  ? 22.520 -1.219  18.554  0.32 22.73 ?  31  LYS   A CA   1 
ATOM   886  C  C    A LYS   A 1 31  ? 23.212 -2.577  18.232  0.68 19.09 ?  31  LYS   A C    1 
ATOM   887  C  C    B LYS   A 1 31  ? 23.121 -2.597  18.264  0.32 20.34 ?  31  LYS   A C    1 
ATOM   888  O  O    A LYS   A 1 31  ? 24.006 -3.119  19.011  0.68 19.85 ?  31  LYS   A O    1 
ATOM   889  O  O    B LYS   A 1 31  ? 23.819 -3.170  19.111  0.32 20.74 ?  31  LYS   A O    1 
ATOM   890  C  CB   A LYS   A 1 31  ? 23.166 -0.665  19.867  0.68 24.68 ?  31  LYS   A CB   1 
ATOM   891  C  CB   B LYS   A 1 31  ? 23.075 -0.638  19.846  0.32 25.56 ?  31  LYS   A CB   1 
ATOM   892  C  CG   A LYS   A 1 31  ? 22.491 0.603   20.354  0.68 29.30 ?  31  LYS   A CG   1 
ATOM   893  C  CG   B LYS   A 1 31  ? 22.401 0.650   20.286  0.32 28.48 ?  31  LYS   A CG   1 
ATOM   894  C  CD   A LYS   A 1 31  ? 23.511 1.627   20.821  0.68 32.77 ?  31  LYS   A CD   1 
ATOM   895  C  CD   B LYS   A 1 31  ? 23.418 1.658   20.794  0.32 30.81 ?  31  LYS   A CD   1 
ATOM   896  C  CE   A LYS   A 1 31  ? 22.875 2.664   21.731  0.68 35.06 ?  31  LYS   A CE   1 
ATOM   897  C  CE   B LYS   A 1 31  ? 22.767 2.725   21.657  0.32 32.40 ?  31  LYS   A CE   1 
ATOM   898  N  NZ   A LYS   A 1 31  ? 21.676 3.301   21.122  0.68 36.30 ?  31  LYS   A NZ   1 
ATOM   899  N  NZ   B LYS   A 1 31  ? 21.594 3.362   20.997  0.32 33.31 ?  31  LYS   A NZ   1 
ATOM   900  H  H    A LYS   A 1 31  ? 20.718 -0.755  18.181  0.68 24.13 ?  31  LYS   A H    1 
ATOM   901  H  H    B LYS   A 1 31  ? 20.688 -0.707  18.064  0.32 27.10 ?  31  LYS   A H    1 
ATOM   902  H  HA   A LYS   A 1 31  ? 22.806 -0.603  17.863  0.68 24.97 ?  31  LYS   A HA   1 
ATOM   903  H  HA   B LYS   A 1 31  ? 22.782 -0.621  17.840  0.32 27.28 ?  31  LYS   A HA   1 
ATOM   904  H  HB2  A LYS   A 1 31  ? 23.077 -1.334  20.560  0.68 29.62 ?  31  LYS   A HB2  1 
ATOM   905  H  HB2  B LYS   A 1 31  ? 22.957 -1.287  20.550  0.32 30.68 ?  31  LYS   A HB2  1 
ATOM   906  H  HB3  A LYS   A 1 31  ? 24.104 -0.462  19.722  0.68 29.62 ?  31  LYS   A HB3  1 
ATOM   907  H  HB3  B LYS   A 1 31  ? 24.021 -0.451  19.724  0.32 30.68 ?  31  LYS   A HB3  1 
ATOM   908  H  HG2  A LYS   A 1 31  ? 21.978 0.993   19.629  0.68 35.16 ?  31  LYS   A HG2  1 
ATOM   909  H  HG2  B LYS   A 1 31  ? 21.933 1.042   19.532  0.32 34.18 ?  31  LYS   A HG2  1 
ATOM   910  H  HG3  A LYS   A 1 31  ? 21.910 0.390   21.101  0.68 35.16 ?  31  LYS   A HG3  1 
ATOM   911  H  HG3  B LYS   A 1 31  ? 21.778 0.456   21.005  0.32 34.18 ?  31  LYS   A HG3  1 
ATOM   912  H  HD2  A LYS   A 1 31  ? 24.215 1.178   21.316  0.68 39.33 ?  31  LYS   A HD2  1 
ATOM   913  H  HD2  B LYS   A 1 31  ? 24.083 1.198   21.329  0.32 36.97 ?  31  LYS   A HD2  1 
ATOM   914  H  HD3  A LYS   A 1 31  ? 23.883 2.085   20.049  0.68 39.33 ?  31  LYS   A HD3  1 
ATOM   915  H  HD3  B LYS   A 1 31  ? 23.840 2.094   20.037  0.32 36.97 ?  31  LYS   A HD3  1 
ATOM   916  H  HE2  A LYS   A 1 31  ? 22.601 2.234   22.556  0.68 42.08 ?  31  LYS   A HE2  1 
ATOM   917  H  HE2  B LYS   A 1 31  ? 22.465 2.319   22.484  0.32 38.89 ?  31  LYS   A HE2  1 
ATOM   918  H  HE3  A LYS   A 1 31  ? 23.523 3.361   21.918  0.68 42.08 ?  31  LYS   A HE3  1 
ATOM   919  H  HE3  B LYS   A 1 31  ? 23.418 3.418   21.846  0.32 38.89 ?  31  LYS   A HE3  1 
ATOM   920  H  HZ1  A LYS   A 1 31  ? 21.353 3.926   21.668  0.68 43.56 ?  31  LYS   A HZ1  1 
ATOM   921  H  HZ1  B LYS   A 1 31  ? 21.266 4.005   21.518  0.32 39.98 ?  31  LYS   A HZ1  1 
ATOM   922  H  HZ2  A LYS   A 1 31  ? 21.892 3.679   20.346  0.68 43.56 ?  31  LYS   A HZ2  1 
ATOM   923  H  HZ2  B LYS   A 1 31  ? 21.839 3.717   20.219  0.32 39.98 ?  31  LYS   A HZ2  1 
ATOM   924  H  HZ3  A LYS   A 1 31  ? 21.045 2.689   20.979  0.68 43.56 ?  31  LYS   A HZ3  1 
ATOM   925  H  HZ3  B LYS   A 1 31  ? 20.959 2.755   20.852  0.32 39.98 ?  31  LYS   A HZ3  1 
ATOM   926  N  N    . PRO   A 1 32  ? 22.870 -3.149  17.082  1.00 17.73 ?  32  PRO   A N    1 
ATOM   927  C  CA   . PRO   A 1 32  ? 23.347 -4.494  16.764  1.00 17.37 ?  32  PRO   A CA   1 
ATOM   928  C  C    . PRO   A 1 32  ? 24.848 -4.513  16.560  1.00 17.23 ?  32  PRO   A C    1 
ATOM   929  O  O    . PRO   A 1 32  ? 25.495 -3.485  16.356  1.00 17.16 ?  32  PRO   A O    1 
ATOM   930  C  CB   . PRO   A 1 32  ? 22.626 -4.809  15.450  1.00 17.45 ?  32  PRO   A CB   1 
ATOM   931  C  CG   . PRO   A 1 32  ? 22.472 -3.464  14.802  1.00 16.28 ?  32  PRO   A CG   1 
ATOM   932  C  CD   . PRO   A 1 32  ? 22.164 -2.536  15.945  1.00 16.56 ?  32  PRO   A CD   1 
ATOM   933  H  HA   . PRO   A 1 32  ? 23.088 -5.126  17.451  1.00 20.85 ?  32  PRO   A HA   1 
ATOM   934  H  HB2  . PRO   A 1 32  ? 23.172 -5.400  14.906  1.00 20.95 ?  32  PRO   A HB2  1 
ATOM   935  H  HB3  . PRO   A 1 32  ? 21.760 -5.211  15.633  1.00 20.95 ?  32  PRO   A HB3  1 
ATOM   936  H  HG2  . PRO   A 1 32  ? 23.299 -3.222  14.361  1.00 19.54 ?  32  PRO   A HG2  1 
ATOM   937  H  HG3  . PRO   A 1 32  ? 21.737 -3.495  14.166  1.00 19.54 ?  32  PRO   A HG3  1 
ATOM   938  H  HD2  . PRO   A 1 32  ? 22.520 -1.653  15.746  1.00 19.87 ?  32  PRO   A HD2  1 
ATOM   939  H  HD3  . PRO   A 1 32  ? 21.211 -2.510  16.101  1.00 19.87 ?  32  PRO   A HD3  1 
ATOM   940  N  N    . THR   A 1 33  ? 25.398 -5.723  16.592  1.00 17.05 ?  33  THR   A N    1 
ATOM   941  C  CA   . THR   A 1 33  ? 26.811 -5.887  16.284  1.00 17.20 ?  33  THR   A CA   1 
ATOM   942  C  C    . THR   A 1 33  ? 27.117 -5.432  14.863  1.00 15.75 ?  33  THR   A C    1 
ATOM   943  O  O    . THR   A 1 33  ? 28.146 -4.788  14.619  1.00 15.92 ?  33  THR   A O    1 
ATOM   944  C  CB   . THR   A 1 33  ? 27.216 -7.345  16.490  1.00 18.82 ?  33  THR   A CB   1 
ATOM   945  O  OG1  . THR   A 1 33  ? 26.896 -7.736  17.828  1.00 20.62 ?  33  THR   A OG1  1 
ATOM   946  C  CG2  . THR   A 1 33  ? 28.704 -7.527  16.254  1.00 19.72 ?  33  THR   A CG2  1 
ATOM   947  H  H    . THR   A 1 33  ? 24.977 -6.448  16.782  1.00 20.47 ?  33  THR   A H    1 
ATOM   948  H  HA   . THR   A 1 33  ? 27.329 -5.343  16.896  1.00 20.65 ?  33  THR   A HA   1 
ATOM   949  H  HB   . THR   A 1 33  ? 26.730 -7.909  15.865  1.00 22.59 ?  33  THR   A HB   1 
ATOM   950  H  HG1  . THR   A 1 33  ? 27.316 -7.259  18.380  1.00 24.75 ?  33  THR   A HG1  1 
ATOM   951  H  HG21 . THR   A 1 33  ? 28.978 -8.411  16.544  1.00 23.67 ?  33  THR   A HG21 1 
ATOM   952  H  HG22 . THR   A 1 33  ? 28.905 -7.429  15.311  1.00 23.67 ?  33  THR   A HG22 1 
ATOM   953  H  HG23 . THR   A 1 33  ? 29.200 -6.863  16.756  1.00 23.67 ?  33  THR   A HG23 1 
ATOM   954  N  N    . VAL   A 1 34  ? 26.234 -5.752  13.916  1.00 14.36 ?  34  VAL   A N    1 
ATOM   955  C  CA   . VAL   A 1 34  ? 26.438 -5.430  12.508  1.00 12.88 ?  34  VAL   A CA   1 
ATOM   956  C  C    . VAL   A 1 34  ? 25.142 -4.874  11.933  1.00 12.16 ?  34  VAL   A C    1 
ATOM   957  O  O    . VAL   A 1 34  ? 24.103 -5.545  11.971  1.00 12.97 ?  34  VAL   A O    1 
ATOM   958  C  CB   . VAL   A 1 34  ? 26.884 -6.647  11.678  1.00 13.64 ?  34  VAL   A CB   1 
ATOM   959  C  CG1  . VAL   A 1 34  ? 27.063 -6.258  10.217  1.00 13.78 ?  34  VAL   A CG1  1 
ATOM   960  C  CG2  . VAL   A 1 34  ? 28.166 -7.254  12.244  1.00 14.90 ?  34  VAL   A CG2  1 
ATOM   961  H  H    . VAL   A 1 34  ? 25.498 -6.170  14.070  1.00 17.24 ?  34  VAL   A H    1 
ATOM   962  H  HA   . VAL   A 1 34  ? 27.120 -4.741  12.431  1.00 15.46 ?  34  VAL   A HA   1 
ATOM   963  H  HB   . VAL   A 1 34  ? 26.192 -7.322  11.730  1.00 16.37 ?  34  VAL   A HB   1 
ATOM   964  H  HG11 . VAL   A 1 34  ? 27.556 -6.962  9.767   1.00 16.54 ?  34  VAL   A HG11 1 
ATOM   965  H  HG12 . VAL   A 1 34  ? 26.192 -6.152  9.808   1.00 16.54 ?  34  VAL   A HG12 1 
ATOM   966  H  HG13 . VAL   A 1 34  ? 27.560 -5.427  10.170  1.00 16.54 ?  34  VAL   A HG13 1 
ATOM   967  H  HG21 . VAL   A 1 34  ? 28.437 -7.997  11.683  1.00 17.89 ?  34  VAL   A HG21 1 
ATOM   968  H  HG22 . VAL   A 1 34  ? 28.862 -6.576  12.254  1.00 17.89 ?  34  VAL   A HG22 1 
ATOM   969  H  HG23 . VAL   A 1 34  ? 28.001 -7.567  13.149  1.00 17.89 ?  34  VAL   A HG23 1 
ATOM   970  N  N    . VAL   A 1 35  ? 25.207 -3.663  11.382  1.00 11.66 ?  35  VAL   A N    1 
ATOM   971  C  CA   . VAL   A 1 35  ? 24.178 -3.152  10.488  1.00 11.14 ?  35  VAL   A CA   1 
ATOM   972  C  C    . VAL   A 1 35  ? 24.738 -3.159  9.074   1.00 10.50 ?  35  VAL   A C    1 
ATOM   973  O  O    . VAL   A 1 35  ? 25.886 -2.757  8.846   1.00 11.24 ?  35  VAL   A O    1 
ATOM   974  C  CB   . VAL   A 1 35  ? 23.652 -1.756  10.892  1.00 11.79 ?  35  VAL   A CB   1 
ATOM   975  C  CG1  . VAL   A 1 35  ? 24.729 -0.670  10.768  1.00 12.55 ?  35  VAL   A CG1  1 
ATOM   976  C  CG2  . VAL   A 1 35  ? 22.422 -1.399  10.054  1.00 12.33 ?  35  VAL   A CG2  1 
ATOM   977  H  H    . VAL   A 1 35  ? 25.851 -3.106  11.508  1.00 14.00 ?  35  VAL   A H    1 
ATOM   978  H  HA   . VAL   A 1 35  ? 23.420 -3.761  10.506  1.00 13.38 ?  35  VAL   A HA   1 
ATOM   979  H  HB   . VAL   A 1 35  ? 23.365 -1.788  11.815  1.00 14.15 ?  35  VAL   A HB   1 
ATOM   980  H  HG11 . VAL   A 1 35  ? 24.383 0.159   11.133  1.00 15.07 ?  35  VAL   A HG11 1 
ATOM   981  H  HG12 . VAL   A 1 35  ? 25.511 -0.951  11.266  1.00 15.07 ?  35  VAL   A HG12 1 
ATOM   982  H  HG13 . VAL   A 1 35  ? 24.956 -0.551  9.833   1.00 15.07 ?  35  VAL   A HG13 1 
ATOM   983  H  HG21 . VAL   A 1 35  ? 22.063 -0.555  10.359  1.00 14.80 ?  35  VAL   A HG21 1 
ATOM   984  H  HG22 . VAL   A 1 35  ? 22.686 -1.326  9.119   1.00 14.80 ?  35  VAL   A HG22 1 
ATOM   985  H  HG23 . VAL   A 1 35  ? 21.757 -2.100  10.150  1.00 14.80 ?  35  VAL   A HG23 1 
ATOM   986  N  N    . VAL   A 1 36  ? 23.928 -3.624  8.125   1.00 10.08 ?  36  VAL   A N    1 
ATOM   987  C  CA   . VAL   A 1 36  ? 24.305 -3.635  6.720   1.00 9.63  ?  36  VAL   A CA   1 
ATOM   988  C  C    . VAL   A 1 36  ? 23.849 -2.344  6.055   1.00 9.98  ?  36  VAL   A C    1 
ATOM   989  O  O    . VAL   A 1 36  ? 22.684 -1.945  6.179   1.00 10.65 ?  36  VAL   A O    1 
ATOM   990  C  CB   . VAL   A 1 36  ? 23.704 -4.853  5.999   1.00 9.82  ?  36  VAL   A CB   1 
ATOM   991  C  CG1  . VAL   A 1 36  ? 23.976 -4.784  4.514   1.00 10.37 ?  36  VAL   A CG1  1 
ATOM   992  C  CG2  . VAL   A 1 36  ? 24.249 -6.140  6.588   1.00 10.56 ?  36  VAL   A CG2  1 
ATOM   993  H  H    . VAL   A 1 36  ? 23.135 -3.936  8.271   1.00 12.10 ?  36  VAL   A H    1 
ATOM   994  H  HA   . VAL   A 1 36  ? 25.273 -3.694  6.650   1.00 11.56 ?  36  VAL   A HA   1 
ATOM   995  H  HB   . VAL   A 1 36  ? 22.744 -4.847  6.128   1.00 11.79 ?  36  VAL   A HB   1 
ATOM   996  H  HG11 . VAL   A 1 36  ? 23.835 -5.659  4.126   1.00 12.45 ?  36  VAL   A HG11 1 
ATOM   997  H  HG12 . VAL   A 1 36  ? 23.365 -4.143  4.108   1.00 12.45 ?  36  VAL   A HG12 1 
ATOM   998  H  HG13 . VAL   A 1 36  ? 24.892 -4.500  4.372   1.00 12.45 ?  36  VAL   A HG13 1 
ATOM   999  H  HG21 . VAL   A 1 36  ? 23.868 -6.895  6.109   1.00 12.67 ?  36  VAL   A HG21 1 
ATOM   1000 H  HG22 . VAL   A 1 36  ? 25.216 -6.148  6.497   1.00 12.67 ?  36  VAL   A HG22 1 
ATOM   1001 H  HG23 . VAL   A 1 36  ? 24.006 -6.191  7.527   1.00 12.67 ?  36  VAL   A HG23 1 
ATOM   1002 N  N    . ASN   A 1 37  ? 24.773 -1.708  5.332   1.00 9.42  ?  37  ASN   A N    1 
ATOM   1003 C  CA   . ASN   A 1 37  ? 24.451 -0.593  4.460   1.00 9.26  ?  37  ASN   A CA   1 
ATOM   1004 C  C    . ASN   A 1 37  ? 24.314 -1.070  3.024   1.00 9.24  ?  37  ASN   A C    1 
ATOM   1005 O  O    . ASN   A 1 37  ? 25.097 -1.904  2.551   1.00 10.02 ?  37  ASN   A O    1 
ATOM   1006 C  CB   . ASN   A 1 37  ? 25.527 0.485   4.540   1.00 9.67  ?  37  ASN   A CB   1 
ATOM   1007 C  CG   . ASN   A 1 37  ? 25.205 1.684   3.687   1.00 9.82  ?  37  ASN   A CG   1 
ATOM   1008 O  OD1  . ASN   A 1 37  ? 24.036 2.021   3.495   1.00 10.27 ?  37  ASN   A OD1  1 
ATOM   1009 N  ND2  . ASN   A 1 37  ? 26.238 2.333   3.166   1.00 10.31 ?  37  ASN   A ND2  1 
ATOM   1010 H  H    . ASN   A 1 37  ? 25.610 -1.911  5.338   1.00 11.31 ?  37  ASN   A H    1 
ATOM   1011 H  HA   . ASN   A 1 37  ? 23.613 -0.198  4.737   1.00 11.11 ?  37  ASN   A HA   1 
ATOM   1012 H  HB2  . ASN   A 1 37  ? 25.612 0.787   5.460   1.00 11.60 ?  37  ASN   A HB2  1 
ATOM   1013 H  HB3  . ASN   A 1 37  ? 26.377 0.117   4.237   1.00 11.60 ?  37  ASN   A HB3  1 
ATOM   1014 H  HD21 . ASN   A 1 37  ? 26.104 3.023   2.668   1.00 12.38 ?  37  ASN   A HD21 1 
ATOM   1015 H  HD22 . ASN   A 1 37  ? 27.036 2.073   3.322   1.00 12.38 ?  37  ASN   A HD22 1 
ATOM   1016 N  N    A ALA   A 1 38  ? 23.298 -0.533  2.342   0.68 9.70  ?  38  ALA   A N    1 
ATOM   1017 N  N    B ALA   A 1 38  ? 23.304 -0.540  2.329   0.32 9.67  ?  38  ALA   A N    1 
ATOM   1018 C  CA   A ALA   A 1 38  ? 23.110 -0.682  0.900   0.68 9.81  ?  38  ALA   A CA   1 
ATOM   1019 C  CA   B ALA   A 1 38  ? 23.136 -0.775  0.894   0.32 10.12 ?  38  ALA   A CA   1 
ATOM   1020 C  C    A ALA   A 1 38  ? 24.025 0.318   0.196   0.68 9.69  ?  38  ALA   A C    1 
ATOM   1021 C  C    B ALA   A 1 38  ? 23.985 0.243   0.135   0.32 10.24 ?  38  ALA   A C    1 
ATOM   1022 O  O    A ALA   A 1 38  ? 23.626 1.424   -0.183  0.68 9.33  ?  38  ALA   A O    1 
ATOM   1023 O  O    B ALA   A 1 38  ? 23.498 1.226   -0.430  0.32 10.31 ?  38  ALA   A O    1 
ATOM   1024 C  CB   A ALA   A 1 38  ? 21.649 -0.441  0.542   0.68 10.81 ?  38  ALA   A CB   1 
ATOM   1025 C  CB   B ALA   A 1 38  ? 21.665 -0.699  0.508   0.32 10.85 ?  38  ALA   A CB   1 
ATOM   1026 H  H    A ALA   A 1 38  ? 22.690 -0.049  2.713   0.68 11.64 ?  38  ALA   A H    1 
ATOM   1027 H  H    B ALA   A 1 38  ? 22.693 -0.039  2.676   0.32 11.61 ?  38  ALA   A H    1 
ATOM   1028 H  HA   A ALA   A 1 38  ? 23.357 -1.577  0.629   0.68 11.78 ?  38  ALA   A HA   1 
ATOM   1029 H  HA   B ALA   A 1 38  ? 23.463 -1.663  0.678   0.32 12.15 ?  38  ALA   A HA   1 
ATOM   1030 H  HB1  A ALA   A 1 38  ? 21.539 -0.534  -0.416  0.68 12.98 ?  38  ALA   A HB1  1 
ATOM   1031 H  HB1  B ALA   A 1 38  ? 21.586 -0.847  -0.446  0.32 13.02 ?  38  ALA   A HB1  1 
ATOM   1032 H  HB2  A ALA   A 1 38  ? 21.098 -1.095  1.003   0.68 12.98 ?  38  ALA   A HB2  1 
ATOM   1033 H  HB2  B ALA   A 1 38  ? 21.170 -1.379  0.992   0.32 13.02 ?  38  ALA   A HB2  1 
ATOM   1034 H  HB3  A ALA   A 1 38  ? 21.397 0.455   0.819   0.68 12.98 ?  38  ALA   A HB3  1 
ATOM   1035 H  HB3  B ALA   A 1 38  ? 21.326 0.181   0.732   0.32 13.02 ?  38  ALA   A HB3  1 
ATOM   1036 N  N    A ALA   A 1 39  ? 25.280 -0.085  0.026   0.68 9.87  ?  39  ALA   A N    1 
ATOM   1037 N  N    B ALA   A 1 39  ? 25.287 -0.016  0.121   0.32 10.30 ?  39  ALA   A N    1 
ATOM   1038 C  CA   A ALA   A 1 39  ? 26.338 0.790   -0.443  0.68 9.51  ?  39  ALA   A CA   1 
ATOM   1039 C  CA   B ALA   A 1 39  ? 26.259 0.924   -0.405  0.32 10.49 ?  39  ALA   A CA   1 
ATOM   1040 C  C    A ALA   A 1 39  ? 26.461 0.767   -1.965  0.68 9.81  ?  39  ALA   A C    1 
ATOM   1041 C  C    B ALA   A 1 39  ? 26.405 0.780   -1.916  0.32 9.93  ?  39  ALA   A C    1 
ATOM   1042 O  O    A ALA   A 1 39  ? 25.946 -0.125  -2.649  0.68 10.12 ?  39  ALA   A O    1 
ATOM   1043 O  O    B ALA   A 1 39  ? 26.027 -0.231  -2.516  0.32 9.94  ?  39  ALA   A O    1 
ATOM   1044 C  CB   A ALA   A 1 39  ? 27.664 0.372   0.201   0.68 9.75  ?  39  ALA   A CB   1 
ATOM   1045 C  CB   B ALA   A 1 39  ? 27.616 0.686   0.258   0.32 11.10 ?  39  ALA   A CB   1 
ATOM   1046 H  H    A ALA   A 1 39  ? 25.543 -0.891  0.185   0.68 11.85 ?  39  ALA   A H    1 
ATOM   1047 H  H    B ALA   A 1 39  ? 25.629 -0.746  0.414   0.32 12.36 ?  39  ALA   A H    1 
ATOM   1048 H  HA   A ALA   A 1 39  ? 26.142 1.700   -0.167  0.68 11.42 ?  39  ALA   A HA   1 
ATOM   1049 H  HA   B ALA   A 1 39  ? 25.976 1.830   -0.203  0.32 12.60 ?  39  ALA   A HA   1 
ATOM   1050 H  HB1  A ALA   A 1 39  ? 28.365 0.965   -0.109  0.68 11.71 ?  39  ALA   A HB1  1 
ATOM   1051 H  HB1  B ALA   A 1 39  ? 28.257 1.316   -0.102  0.32 13.33 ?  39  ALA   A HB1  1 
ATOM   1052 H  HB2  A ALA   A 1 39  ? 27.581 0.445   1.171   0.68 11.71 ?  39  ALA   A HB2  1 
ATOM   1053 H  HB2  B ALA   A 1 39  ? 27.526 0.813   1.216   0.32 13.33 ?  39  ALA   A HB2  1 
ATOM   1054 H  HB3  A ALA   A 1 39  ? 27.862 -0.541  -0.043  0.68 11.71 ?  39  ALA   A HB3  1 
ATOM   1055 H  HB3  B ALA   A 1 39  ? 27.902 -0.223  0.072   0.32 13.33 ?  39  ALA   A HB3  1 
ATOM   1056 N  N    A ASN   A 1 40  ? 27.178 1.764   -2.489  0.68 9.93  ?  40  ASN   A N    1 
ATOM   1057 N  N    B ASN   A 1 40  ? 26.973 1.817   -2.528  0.32 9.87  ?  40  ASN   A N    1 
ATOM   1058 C  CA   A ASN   A 1 40  ? 27.728 1.718   -3.836  0.68 9.92  ?  40  ASN   A CA   1 
ATOM   1059 C  CA   B ASN   A 1 40  ? 27.451 1.760   -3.901  0.32 10.12 ?  40  ASN   A CA   1 
ATOM   1060 C  C    A ASN   A 1 40  ? 29.250 1.610   -3.758  0.68 9.28  ?  40  ASN   A C    1 
ATOM   1061 C  C    B ASN   A 1 40  ? 28.975 1.637   -3.898  0.32 9.83  ?  40  ASN   A C    1 
ATOM   1062 O  O    A ASN   A 1 40  ? 29.847 1.720   -2.684  0.68 9.65  ?  40  ASN   A O    1 
ATOM   1063 O  O    B ASN   A 1 40  ? 29.626 1.717   -2.854  0.32 9.91  ?  40  ASN   A O    1 
ATOM   1064 C  CB   A ASN   A 1 40  ? 27.251 2.892   -4.709  0.68 10.47 ?  40  ASN   A CB   1 
ATOM   1065 C  CB   B ASN   A 1 40  ? 26.983 2.989   -4.690  0.32 11.06 ?  40  ASN   A CB   1 
ATOM   1066 C  CG   A ASN   A 1 40  ? 27.605 4.248   -4.136  0.68 11.47 ?  40  ASN   A CG   1 
ATOM   1067 C  CG   B ASN   A 1 40  ? 27.414 4.290   -4.052  0.32 12.00 ?  40  ASN   A CG   1 
ATOM   1068 O  OD1  A ASN   A 1 40  ? 28.760 4.508   -3.783  0.68 12.43 ?  40  ASN   A OD1  1 
ATOM   1069 O  OD1  B ASN   A 1 40  ? 28.605 4.599   -3.990  0.32 12.54 ?  40  ASN   A OD1  1 
ATOM   1070 N  ND2  A ASN   A 1 40  ? 26.601 5.132   -4.048  0.68 12.12 ?  40  ASN   A ND2  1 
ATOM   1071 N  ND2  B ASN   A 1 40  ? 26.441 5.067   -3.580  0.32 12.30 ?  40  ASN   A ND2  1 
ATOM   1072 H  H    A ASN   A 1 40  ? 27.368 2.481   -2.066  0.68 11.92 ?  40  ASN   A H    1 
ATOM   1073 H  H    B ASN   A 1 40  ? 27.097 2.580   -2.152  0.32 11.85 ?  40  ASN   A H    1 
ATOM   1074 H  HA   A ASN   A 1 40  ? 27.421 0.905   -4.261  0.68 11.91 ?  40  ASN   A HA   1 
ATOM   1075 H  HA   B ASN   A 1 40  ? 27.082 0.969   -4.331  0.32 12.15 ?  40  ASN   A HA   1 
ATOM   1076 H  HB2  A ASN   A 1 40  ? 27.663 2.815   -5.584  0.68 12.57 ?  40  ASN   A HB2  1 
ATOM   1077 H  HB2  B ASN   A 1 40  ? 27.359 2.953   -5.580  0.32 13.28 ?  40  ASN   A HB2  1 
ATOM   1078 H  HB3  A ASN   A 1 40  ? 26.288 2.840   -4.791  0.68 12.57 ?  40  ASN   A HB3  1 
ATOM   1079 H  HB3  B ASN   A 1 40  ? 26.010 2.981   -4.739  0.32 13.28 ?  40  ASN   A HB3  1 
ATOM   1080 H  HD21 A ASN   A 1 40  ? 26.745 5.921   -3.733  0.68 14.55 ?  40  ASN   A HD21 1 
ATOM   1081 H  HD21 B ASN   A 1 40  ? 26.633 5.816   -3.204  0.32 14.77 ?  40  ASN   A HD21 1 
ATOM   1082 H  HD22 A ASN   A 1 40  ? 25.809 4.911   -4.299  0.68 14.55 ?  40  ASN   A HD22 1 
ATOM   1083 H  HD22 B ASN   A 1 40  ? 25.618 4.821   -3.648  0.32 14.77 ?  40  ASN   A HD22 1 
ATOM   1084 N  N    A VAL   A 1 41  ? 29.875 1.347   -4.910  0.68 9.70  ?  41  VAL   A N    1 
ATOM   1085 N  N    B VAL   A 1 41  ? 29.549 1.432   -5.087  0.32 10.02 ?  41  VAL   A N    1 
ATOM   1086 C  CA   A VAL   A 1 41  ? 31.303 1.038   -4.931  0.68 10.22 ?  41  VAL   A CA   1 
ATOM   1087 C  CA   B VAL   A 1 41  ? 30.974 1.115   -5.168  0.32 10.53 ?  41  VAL   A CA   1 
ATOM   1088 C  C    A VAL   A 1 41  ? 32.157 2.198   -4.459  0.68 10.17 ?  41  VAL   A C    1 
ATOM   1089 C  C    B VAL   A 1 41  ? 31.861 2.245   -4.662  0.32 10.57 ?  41  VAL   A C    1 
ATOM   1090 O  O    A VAL   A 1 41  ? 33.293 1.985   -4.021  0.68 10.77 ?  41  VAL   A O    1 
ATOM   1091 O  O    B VAL   A 1 41  ? 33.015 2.001   -4.290  0.32 10.81 ?  41  VAL   A O    1 
ATOM   1092 C  CB   A VAL   A 1 41  ? 31.788 0.547   -6.316  0.68 10.40 ?  41  VAL   A CB   1 
ATOM   1093 C  CB   B VAL   A 1 41  ? 31.388 0.693   -6.595  0.32 11.24 ?  41  VAL   A CB   1 
ATOM   1094 C  CG1  A VAL   A 1 41  ? 31.094 -0.751  -6.714  0.68 11.36 ?  41  VAL   A CG1  1 
ATOM   1095 C  CG1  B VAL   A 1 41  ? 30.741 -0.632  -6.968  0.32 12.00 ?  41  VAL   A CG1  1 
ATOM   1096 C  CG2  A VAL   A 1 41  ? 31.635 1.616   -7.393  0.68 10.60 ?  41  VAL   A CG2  1 
ATOM   1097 C  CG2  B VAL   A 1 41  ? 31.038 1.778   -7.606  0.32 11.66 ?  41  VAL   A CG2  1 
ATOM   1098 H  H    A VAL   A 1 41  ? 29.501 1.333   -5.678  0.68 11.64 ?  41  VAL   A H    1 
ATOM   1099 H  H    B VAL   A 1 41  ? 29.138 1.467   -5.843  0.32 12.03 ?  41  VAL   A H    1 
ATOM   1100 H  HA   A VAL   A 1 41  ? 31.467 0.313   -4.310  0.68 12.26 ?  41  VAL   A HA   1 
ATOM   1101 H  HA   B VAL   A 1 41  ? 31.132 0.347   -4.596  0.32 12.65 ?  41  VAL   A HA   1 
ATOM   1102 H  HB   A VAL   A 1 41  ? 32.734 0.348   -6.253  0.68 12.49 ?  41  VAL   A HB   1 
ATOM   1103 H  HB   B VAL   A 1 41  ? 32.348 0.565   -6.614  0.32 13.50 ?  41  VAL   A HB   1 
ATOM   1104 H  HG11 A VAL   A 1 41  ? 31.429 -1.046  -7.576  0.68 13.64 ?  41  VAL   A HG11 1 
ATOM   1105 H  HG11 B VAL   A 1 41  ? 30.989 -0.860  -7.877  0.32 14.41 ?  41  VAL   A HG11 1 
ATOM   1106 H  HG12 A VAL   A 1 41  ? 31.274 -1.429  -6.042  0.68 13.64 ?  41  VAL   A HG12 1 
ATOM   1107 H  HG12 B VAL   A 1 41  ? 31.054 -1.321  -6.358  0.32 14.41 ?  41  VAL   A HG12 1 
ATOM   1108 H  HG13 A VAL   A 1 41  ? 30.135 -0.596  -6.772  0.68 13.64 ?  41  VAL   A HG13 1 
ATOM   1109 H  HG13 B VAL   A 1 41  ? 29.778 -0.548  -6.900  0.32 14.41 ?  41  VAL   A HG13 1 
ATOM   1110 H  HG21 A VAL   A 1 41  ? 31.863 1.228   -8.257  0.68 12.73 ?  41  VAL   A HG21 1 
ATOM   1111 H  HG21 B VAL   A 1 41  ? 31.377 1.516   -8.476  0.32 14.00 ?  41  VAL   A HG21 1 
ATOM   1112 H  HG22 A VAL   A 1 41  ? 30.720 1.928   -7.404  0.68 12.73 ?  41  VAL   A HG22 1 
ATOM   1113 H  HG22 B VAL   A 1 41  ? 30.074 1.878   -7.646  0.32 14.00 ?  41  VAL   A HG22 1 
ATOM   1114 H  HG23 A VAL   A 1 41  ? 32.238 2.350   -7.197  0.68 12.73 ?  41  VAL   A HG23 1 
ATOM   1115 H  HG23 B VAL   A 1 41  ? 31.447 2.611   -7.329  0.32 14.00 ?  41  VAL   A HG23 1 
ATOM   1116 N  N    A TYR   A 1 42  ? 31.650 3.428   -4.560  0.68 10.48 ?  42  TYR   A N    1 
ATOM   1117 N  N    B TYR   A 1 42  ? 31.364 3.483   -4.654  0.32 10.63 ?  42  TYR   A N    1 
ATOM   1118 C  CA   A TYR   A 1 42  ? 32.376 4.621   -4.144  0.68 10.67 ?  42  TYR   A CA   1 
ATOM   1119 C  CA   B TYR   A 1 42  ? 32.143 4.639   -4.225  0.32 10.78 ?  42  TYR   A CA   1 
ATOM   1120 C  C    A TYR   A 1 42  ? 32.102 4.993   -2.697  0.68 10.42 ?  42  TYR   A C    1 
ATOM   1121 C  C    B TYR   A 1 42  ? 31.911 5.018   -2.769  0.32 10.83 ?  42  TYR   A C    1 
ATOM   1122 O  O    A TYR   A 1 42  ? 32.663 5.981   -2.205  0.68 11.32 ?  42  TYR   A O    1 
ATOM   1123 O  O    B TYR   A 1 42  ? 32.486 6.009   -2.304  0.32 11.24 ?  42  TYR   A O    1 
ATOM   1124 C  CB   A TYR   A 1 42  ? 32.026 5.803   -5.066  0.68 11.52 ?  42  TYR   A CB   1 
ATOM   1125 C  CB   B TYR   A 1 42  ? 31.828 5.848   -5.113  0.32 11.27 ?  42  TYR   A CB   1 
ATOM   1126 C  CG   A TYR   A 1 42  ? 32.235 5.477   -6.530  0.68 11.86 ?  42  TYR   A CG   1 
ATOM   1127 C  CG   B TYR   A 1 42  ? 31.956 5.563   -6.589  0.32 11.47 ?  42  TYR   A CG   1 
ATOM   1128 C  CD1  A TYR   A 1 42  ? 33.511 5.280   -7.038  0.68 12.66 ?  42  TYR   A CD1  1 
ATOM   1129 C  CD1  B TYR   A 1 42  ? 33.199 5.347   -7.168  0.32 11.50 ?  42  TYR   A CD1  1 
ATOM   1130 C  CD2  A TYR   A 1 42  ? 31.161 5.328   -7.397  0.68 13.04 ?  42  TYR   A CD2  1 
ATOM   1131 C  CD2  B TYR   A 1 42  ? 30.835 5.508   -7.405  0.32 12.42 ?  42  TYR   A CD2  1 
ATOM   1132 C  CE1  A TYR   A 1 42  ? 33.712 4.958   -8.370  0.68 12.90 ?  42  TYR   A CE1  1 
ATOM   1133 C  CE1  B TYR   A 1 42  ? 33.323 5.078   -8.516  0.32 11.64 ?  42  TYR   A CE1  1 
ATOM   1134 C  CE2  A TYR   A 1 42  ? 31.355 5.013   -8.734  0.68 13.83 ?  42  TYR   A CE2  1 
ATOM   1135 C  CE2  B TYR   A 1 42  ? 30.947 5.247   -8.756  0.32 12.54 ?  42  TYR   A CE2  1 
ATOM   1136 C  CZ   A TYR   A 1 42  ? 32.634 4.830   -9.213  0.68 13.51 ?  42  TYR   A CZ   1 
ATOM   1137 C  CZ   B TYR   A 1 42  ? 32.194 5.032   -9.307  0.32 12.02 ?  42  TYR   A CZ   1 
ATOM   1138 O  OH   A TYR   A 1 42  ? 32.836 4.508   -10.534 0.68 14.61 ?  42  TYR   A OH   1 
ATOM   1139 O  OH   B TYR   A 1 42  ? 32.319 4.770   -10.650 0.32 12.41 ?  42  TYR   A OH   1 
ATOM   1140 H  H    A TYR   A 1 42  ? 30.868 3.599   -4.872  0.68 12.58 ?  42  TYR   A H    1 
ATOM   1141 H  H    B TYR   A 1 42  ? 30.563 3.679   -4.911  0.32 12.76 ?  42  TYR   A H    1 
ATOM   1142 H  HA   A TYR   A 1 42  ? 33.327 4.461   -4.228  0.68 12.81 ?  42  TYR   A HA   1 
ATOM   1143 H  HA   B TYR   A 1 42  ? 33.083 4.434   -4.333  0.32 12.94 ?  42  TYR   A HA   1 
ATOM   1144 H  HB2  A TYR   A 1 42  ? 31.092 6.043   -4.940  0.68 13.83 ?  42  TYR   A HB2  1 
ATOM   1145 H  HB2  B TYR   A 1 42  ? 30.916 6.134   -4.942  0.32 13.52 ?  42  TYR   A HB2  1 
ATOM   1146 H  HB3  A TYR   A 1 42  ? 32.591 6.563   -4.843  0.68 13.83 ?  42  TYR   A HB3  1 
ATOM   1147 H  HB3  B TYR   A 1 42  ? 32.443 6.567   -4.893  0.32 13.52 ?  42  TYR   A HB3  1 
ATOM   1148 H  HD1  A TYR   A 1 42  ? 34.248 5.367   -6.472  0.68 15.20 ?  42  TYR   A HD1  1 
ATOM   1149 H  HD1  B TYR   A 1 42  ? 33.962 5.377   -6.635  0.32 13.80 ?  42  TYR   A HD1  1 
ATOM   1150 H  HD2  A TYR   A 1 42  ? 30.295 5.455   -7.077  0.68 15.65 ?  42  TYR   A HD2  1 
ATOM   1151 H  HD2  B TYR   A 1 42  ? 29.994 5.654   -7.034  0.32 14.91 ?  42  TYR   A HD2  1 
ATOM   1152 H  HE1  A TYR   A 1 42  ? 34.576 4.840   -8.695  0.68 15.49 ?  42  TYR   A HE1  1 
ATOM   1153 H  HE1  B TYR   A 1 42  ? 34.164 4.934   -8.888  0.32 13.98 ?  42  TYR   A HE1  1 
ATOM   1154 H  HE2  A TYR   A 1 42  ? 30.622 4.927   -9.305  0.68 16.61 ?  42  TYR   A HE2  1 
ATOM   1155 H  HE2  B TYR   A 1 42  ? 30.188 5.212   -9.291  0.32 15.05 ?  42  TYR   A HE2  1 
ATOM   1156 H  HH   A TYR   A 1 42  ? 33.656 4.382   -10.673 0.68 17.53 ?  42  TYR   A HH   1 
ATOM   1157 H  HH   B TYR   A 1 42  ? 31.568 4.767   -11.016 0.32 14.90 ?  42  TYR   A HH   1 
ATOM   1158 N  N    A LEU   A 1 43  ? 31.243 4.233   -2.018  0.68 10.34 ?  43  LEU   A N    1 
ATOM   1159 N  N    B LEU   A 1 43  ? 31.082 4.265   -2.045  0.32 10.50 ?  43  LEU   A N    1 
ATOM   1160 C  CA   A LEU   A 1 43  ? 30.794 4.566   -0.668  0.68 10.01 ?  43  LEU   A CA   1 
ATOM   1161 C  CA   B LEU   A 1 43  ? 30.657 4.623   -0.689  0.32 10.34 ?  43  LEU   A CA   1 
ATOM   1162 C  C    A LEU   A 1 43  ? 30.320 6.017   -0.575  0.68 10.23 ?  43  LEU   A C    1 
ATOM   1163 C  C    B LEU   A 1 43  ? 30.164 6.066   -0.611  0.32 10.42 ?  43  LEU   A C    1 
ATOM   1164 O  O    A LEU   A 1 43  ? 30.615 6.730   0.387   0.68 11.35 ?  43  LEU   A O    1 
ATOM   1165 O  O    B LEU   A 1 43  ? 30.364 6.765   0.386   0.32 10.36 ?  43  LEU   A O    1 
ATOM   1166 C  CB   A LEU   A 1 43  ? 31.844 4.252   0.394   0.68 10.58 ?  43  LEU   A CB   1 
ATOM   1167 C  CB   B LEU   A 1 43  ? 31.730 4.341   0.363   0.32 9.96  ?  43  LEU   A CB   1 
ATOM   1168 C  CG   A LEU   A 1 43  ? 32.343 2.803   0.460   0.68 11.11 ?  43  LEU   A CG   1 
ATOM   1169 C  CG   B LEU   A 1 43  ? 32.190 2.889   0.518   0.32 10.07 ?  43  LEU   A CG   1 
ATOM   1170 C  CD1  A LEU   A 1 43  ? 33.440 2.686   1.509   0.68 11.49 ?  43  LEU   A CD1  1 
ATOM   1171 C  CD1  B LEU   A 1 43  ? 33.132 2.777   1.711   0.32 10.59 ?  43  LEU   A CD1  1 
ATOM   1172 C  CD2  A LEU   A 1 43  ? 31.219 1.822   0.749   0.68 11.60 ?  43  LEU   A CD2  1 
ATOM   1173 C  CD2  B LEU   A 1 43  ? 31.011 1.927   0.653   0.32 10.40 ?  43  LEU   A CD2  1 
ATOM   1174 H  H    A LEU   A 1 43  ? 30.902 3.499   -2.320  0.68 12.42 ?  43  LEU   A H    1 
ATOM   1175 H  H    B LEU   A 1 43  ? 30.746 3.524   -2.320  0.32 12.60 ?  43  LEU   A H    1 
ATOM   1176 H  HA   A LEU   A 1 43  ? 30.024 4.006   -0.468  0.68 12.01 ?  43  LEU   A HA   1 
ATOM   1177 H  HA   B LEU   A 1 43  ? 29.896 4.069   -0.467  0.32 12.41 ?  43  LEU   A HA   1 
ATOM   1178 H  HB2  A LEU   A 1 43  ? 32.617 4.814   0.239   0.68 12.70 ?  43  LEU   A HB2  1 
ATOM   1179 H  HB2  B LEU   A 1 43  ? 32.513 4.869   0.151   0.32 11.95 ?  43  LEU   A HB2  1 
ATOM   1180 H  HB3  A LEU   A 1 43  ? 31.466 4.456   1.265   0.68 12.70 ?  43  LEU   A HB3  1 
ATOM   1181 H  HB3  B LEU   A 1 43  ? 31.380 4.618   1.226   0.32 11.95 ?  43  LEU   A HB3  1 
ATOM   1182 H  HG   A LEU   A 1 43  ? 32.733 2.562   -0.397  0.68 13.34 ?  43  LEU   A HG   1 
ATOM   1183 H  HG   B LEU   A 1 43  ? 32.688 2.635   -0.274  0.32 12.09 ?  43  LEU   A HG   1 
ATOM   1184 H  HD11 A LEU   A 1 43  ? 33.751 1.766   1.543   0.68 13.79 ?  43  LEU   A HD11 1 
ATOM   1185 H  HD11 B LEU   A 1 43  ? 33.421 1.855   1.800   0.32 12.72 ?  43  LEU   A HD11 1 
ATOM   1186 H  HD12 A LEU   A 1 43  ? 34.172 3.273   1.268   0.68 13.79 ?  43  LEU   A HD12 1 
ATOM   1187 H  HD12 B LEU   A 1 43  ? 33.899 3.351   1.561   0.32 12.72 ?  43  LEU   A HD12 1 
ATOM   1188 H  HD13 A LEU   A 1 43  ? 33.078 2.942   2.372   0.68 13.79 ?  43  LEU   A HD13 1 
ATOM   1189 H  HD13 B LEU   A 1 43  ? 32.661 3.055   2.512   0.32 12.72 ?  43  LEU   A HD13 1 
ATOM   1190 H  HD21 A LEU   A 1 43  ? 31.595 0.933   0.859   0.68 13.92 ?  43  LEU   A HD21 1 
ATOM   1191 H  HD21 B LEU   A 1 43  ? 31.346 1.048   0.890   0.32 12.49 ?  43  LEU   A HD21 1 
ATOM   1192 H  HD22 A LEU   A 1 43  ? 30.769 2.093   1.563   0.68 13.92 ?  43  LEU   A HD22 1 
ATOM   1193 H  HD22 B LEU   A 1 43  ? 30.415 2.253   1.345   0.32 12.49 ?  43  LEU   A HD22 1 
ATOM   1194 H  HD23 A LEU   A 1 43  ? 30.598 1.829   0.006   0.68 13.92 ?  43  LEU   A HD23 1 
ATOM   1195 H  HD23 B LEU   A 1 43  ? 30.541 1.884   -0.195  0.32 12.49 ?  43  LEU   A HD23 1 
ATOM   1196 N  N    A LYS   A 1 44  ? 29.572 6.453   -1.590  0.68 10.08 ?  44  LYS   A N    1 
ATOM   1197 N  N    B LYS   A 1 44  ? 29.488 6.507   -1.668  0.32 10.74 ?  44  LYS   A N    1 
ATOM   1198 C  CA   A LYS   A 1 44  ? 28.933 7.767   -1.590  0.68 10.64 ?  44  LYS   A CA   1 
ATOM   1199 C  CA   B LYS   A 1 44  ? 28.833 7.813   -1.689  0.32 11.33 ?  44  LYS   A CA   1 
ATOM   1200 C  C    A LYS   A 1 44  ? 27.498 7.577   -1.113  0.68 10.19 ?  44  LYS   A C    1 
ATOM   1201 C  C    B LYS   A 1 44  ? 27.426 7.632   -1.144  0.32 10.34 ?  44  LYS   A C    1 
ATOM   1202 O  O    A LYS   A 1 44  ? 26.656 7.039   -1.839  0.68 11.29 ?  44  LYS   A O    1 
ATOM   1203 O  O    B LYS   A 1 44  ? 26.521 7.181   -1.851  0.32 10.47 ?  44  LYS   A O    1 
ATOM   1204 C  CB   A LYS   A 1 44  ? 28.994 8.412   -2.970  0.68 12.83 ?  44  LYS   A CB   1 
ATOM   1205 C  CB   B LYS   A 1 44  ? 28.823 8.387   -3.102  0.32 13.76 ?  44  LYS   A CB   1 
ATOM   1206 C  CG   A LYS   A 1 44  ? 30.386 8.852   -3.386  0.68 15.58 ?  44  LYS   A CG   1 
ATOM   1207 C  CG   B LYS   A 1 44  ? 30.168 8.929   -3.570  0.32 16.29 ?  44  LYS   A CG   1 
ATOM   1208 C  CD   A LYS   A 1 44  ? 31.014 9.832   -2.397  0.68 20.20 ?  44  LYS   A CD   1 
ATOM   1209 C  CD   B LYS   A 1 44  ? 30.976 9.492   -2.405  0.32 19.13 ?  44  LYS   A CD   1 
ATOM   1210 C  CE   A LYS   A 1 44  ? 32.372 10.302  -2.884  0.68 23.16 ?  44  LYS   A CE   1 
ATOM   1211 C  CE   B LYS   A 1 44  ? 31.918 10.583  -2.844  0.32 20.79 ?  44  LYS   A CE   1 
ATOM   1212 N  NZ   A LYS   A 1 44  ? 33.176 10.909  -1.791  0.68 24.57 ?  44  LYS   A NZ   1 
ATOM   1213 N  NZ   B LYS   A 1 44  ? 32.816 10.995  -1.735  0.32 22.01 ?  44  LYS   A NZ   1 
ATOM   1214 H  H    A LYS   A 1 44  ? 29.421 5.995   -2.303  0.68 12.10 ?  44  LYS   A H    1 
ATOM   1215 H  H    B LYS   A 1 44  ? 29.395 6.065   -2.399  0.32 12.89 ?  44  LYS   A H    1 
ATOM   1216 H  HA   A LYS   A 1 44  ? 29.380 8.338   -0.950  0.68 12.77 ?  44  LYS   A HA   1 
ATOM   1217 H  HA   B LYS   A 1 44  ? 29.279 8.407   -1.067  0.32 13.61 ?  44  LYS   A HA   1 
ATOM   1218 H  HB2  A LYS   A 1 44  ? 28.676 7.777   -3.627  0.68 15.40 ?  44  LYS   A HB2  1 
ATOM   1219 H  HB2  B LYS   A 1 44  ? 28.559 7.685   -3.722  0.32 16.52 ?  44  LYS   A HB2  1 
ATOM   1220 H  HB3  A LYS   A 1 44  ? 28.425 9.198   -2.968  0.68 15.40 ?  44  LYS   A HB3  1 
ATOM   1221 H  HB3  B LYS   A 1 44  ? 28.183 9.114   -3.145  0.32 16.52 ?  44  LYS   A HB3  1 
ATOM   1222 H  HG2  A LYS   A 1 44  ? 30.966 8.074   -3.443  0.68 18.70 ?  44  LYS   A HG2  1 
ATOM   1223 H  HG2  B LYS   A 1 44  ? 30.678 8.213   -3.984  0.32 19.55 ?  44  LYS   A HG2  1 
ATOM   1224 H  HG3  A LYS   A 1 44  ? 30.340 9.293   -4.249  0.68 18.70 ?  44  LYS   A HG3  1 
ATOM   1225 H  HG3  B LYS   A 1 44  ? 30.022 9.646   -4.210  0.32 19.55 ?  44  LYS   A HG3  1 
ATOM   1226 H  HD2  A LYS   A 1 44  ? 30.433 10.598  -2.294  0.68 24.25 ?  44  LYS   A HD2  1 
ATOM   1227 H  HD2  B LYS   A 1 44  ? 30.372 9.900   -1.765  0.32 22.96 ?  44  LYS   A HD2  1 
ATOM   1228 H  HD3  A LYS   A 1 44  ? 31.143 9.386   -1.542  0.68 24.25 ?  44  LYS   A HD3  1 
ATOM   1229 H  HD3  B LYS   A 1 44  ? 31.480 8.769   -1.984  0.32 22.96 ?  44  LYS   A HD3  1 
ATOM   1230 H  HE2  A LYS   A 1 44  ? 32.864 9.546   -3.237  0.68 27.79 ?  44  LYS   A HE2  1 
ATOM   1231 H  HE2  B LYS   A 1 44  ? 32.459 10.260  -3.577  0.32 24.96 ?  44  LYS   A HE2  1 
ATOM   1232 H  HE3  A LYS   A 1 44  ? 32.243 10.971  -3.575  0.68 27.79 ?  44  LYS   A HE3  1 
ATOM   1233 H  HE3  B LYS   A 1 44  ? 31.397 11.355  -3.119  0.32 24.96 ?  44  LYS   A HE3  1 
ATOM   1234 H  HZ1  A LYS   A 1 44  ? 33.962 11.178  -2.106  0.68 29.49 ?  44  LYS   A HZ1  1 
ATOM   1235 H  HZ1  B LYS   A 1 44  ? 33.362 11.640  -2.012  0.32 26.42 ?  44  LYS   A HZ1  1 
ATOM   1236 H  HZ2  A LYS   A 1 44  ? 32.743 11.614  -1.453  0.68 29.49 ?  44  LYS   A HZ2  1 
ATOM   1237 H  HZ2  B LYS   A 1 44  ? 32.337 11.296  -1.048  0.32 26.42 ?  44  LYS   A HZ2  1 
ATOM   1238 H  HZ3  A LYS   A 1 44  ? 33.307 10.315  -1.144  0.68 29.49 ?  44  LYS   A HZ3  1 
ATOM   1239 H  HZ3  B LYS   A 1 44  ? 33.303 10.300  -1.464  0.32 26.42 ?  44  LYS   A HZ3  1 
ATOM   1240 N  N    . HIS   A 1 45  ? 27.241 7.982   0.126   1.00 10.10 ?  45  HIS   A N    1 
ATOM   1241 C  CA   . HIS   A 1 45  ? 26.007 7.639   0.826   1.00 10.15 ?  45  HIS   A CA   1 
ATOM   1242 C  C    . HIS   A 1 45  ? 24.983 8.761   0.663   1.00 10.89 ?  45  HIS   A C    1 
ATOM   1243 O  O    . HIS   A 1 45  ? 24.705 9.531   1.580   1.00 12.54 ?  45  HIS   A O    1 
ATOM   1244 C  CB   . HIS   A 1 45  ? 26.307 7.389   2.292   1.00 10.11 ?  45  HIS   A CB   1 
ATOM   1245 C  CG   . HIS   A 1 45  ? 27.415 6.420   2.523   1.00 9.57  ?  45  HIS   A CG   1 
ATOM   1246 N  ND1  . HIS   A 1 45  ? 27.406 5.133   2.025   1.00 10.13 ?  45  HIS   A ND1  1 
ATOM   1247 C  CD2  . HIS   A 1 45  ? 28.580 6.573   3.196   1.00 10.03 ?  45  HIS   A CD2  1 
ATOM   1248 C  CE1  . HIS   A 1 45  ? 28.524 4.537   2.401   1.00 10.18 ?  45  HIS   A CE1  1 
ATOM   1249 N  NE2  . HIS   A 1 45  ? 29.253 5.385   3.109   1.00 10.26 ?  45  HIS   A NE2  1 
ATOM   1250 H  H    A HIS   A 1 45  ? 27.777 8.468   0.591   0.68 12.13 ?  45  HIS   A H    1 
ATOM   1251 H  H    B HIS   A 1 45  ? 27.811 8.413   0.604   0.32 12.13 ?  45  HIS   A H    1 
ATOM   1252 H  HA   . HIS   A 1 45  ? 25.631 6.828   0.445   1.00 12.19 ?  45  HIS   A HA   1 
ATOM   1253 H  HB2  . HIS   A 1 45  ? 26.544 8.230   2.711   1.00 12.13 ?  45  HIS   A HB2  1 
ATOM   1254 H  HB3  . HIS   A 1 45  ? 25.502 7.032   2.717   1.00 12.13 ?  45  HIS   A HB3  1 
ATOM   1255 H  HD2  . HIS   A 1 45  ? 28.869 7.342   3.638   1.00 12.04 ?  45  HIS   A HD2  1 
ATOM   1256 H  HE1  . HIS   A 1 45  ? 28.757 3.659   2.209   1.00 12.22 ?  45  HIS   A HE1  1 
ATOM   1257 H  HE2  . HIS   A 1 45  ? 30.022 5.218   3.458   1.00 12.32 ?  45  HIS   A HE2  1 
ATOM   1258 N  N    A GLY   A 1 46  ? 24.396 8.822   -0.526  0.68 11.88 ?  46  GLY   A N    1 
ATOM   1259 N  N    B GLY   A 1 46  ? 24.411 8.848   -0.532  0.32 11.29 ?  46  GLY   A N    1 
ATOM   1260 C  CA   A GLY   A 1 46  ? 23.569 9.958   -0.880  0.68 12.75 ?  46  GLY   A CA   1 
ATOM   1261 C  CA   B GLY   A 1 46  ? 23.589 10.001  -0.851  0.32 11.57 ?  46  GLY   A CA   1 
ATOM   1262 C  C    A GLY   A 1 46  ? 22.082 9.803   -0.641  0.68 12.75 ?  46  GLY   A C    1 
ATOM   1263 C  C    B GLY   A 1 46  ? 22.131 9.900   -0.443  0.32 11.23 ?  46  GLY   A C    1 
ATOM   1264 O  O    A GLY   A 1 46  ? 21.401 10.787  -0.330  0.68 13.72 ?  46  GLY   A O    1 
ATOM   1265 O  O    B GLY   A 1 46  ? 21.524 10.896  -0.035  0.32 11.84 ?  46  GLY   A O    1 
ATOM   1266 H  H    A GLY   A 1 46  ? 24.455 8.222   -1.138  0.68 14.26 ?  46  GLY   A H    1 
ATOM   1267 H  H    B GLY   A 1 46  ? 24.472 8.264   -1.159  0.32 13.56 ?  46  GLY   A H    1 
ATOM   1268 H  HA2  A GLY   A 1 46  ? 23.867 10.733  -0.375  0.68 15.30 ?  46  GLY   A HA2  1 
ATOM   1269 H  HA2  B GLY   A 1 46  ? 23.961 10.784  -0.406  0.32 13.89 ?  46  GLY   A HA2  1 
ATOM   1270 H  HA3  A GLY   A 1 46  ? 23.688 10.153  -1.820  0.68 15.30 ?  46  GLY   A HA3  1 
ATOM   1271 H  HA3  B GLY   A 1 46  ? 23.623 10.160  -1.804  0.32 13.89 ?  46  GLY   A HA3  1 
ATOM   1272 N  N    A GLY   A 1 47  ? 21.558 8.592   -0.810  0.68 12.37 ?  47  GLY   A N    1 
ATOM   1273 N  N    B GLY   A 1 47  ? 21.555 8.711   -0.558  0.32 11.10 ?  47  GLY   A N    1 
ATOM   1274 C  CA   A GLY   A 1 47  ? 20.127 8.377   -0.774  0.68 11.95 ?  47  GLY   A CA   1 
ATOM   1275 C  CA   B GLY   A 1 47  ? 20.143 8.528   -0.313  0.32 11.20 ?  47  GLY   A CA   1 
ATOM   1276 C  C    A GLY   A 1 47  ? 19.805 6.952   -0.382  0.68 11.67 ?  47  GLY   A C    1 
ATOM   1277 C  C    B GLY   A 1 47  ? 19.832 7.076   -0.015  0.32 10.63 ?  47  GLY   A C    1 
ATOM   1278 O  O    A GLY   A 1 47  ? 20.697 6.127   -0.170  0.68 11.60 ?  47  GLY   A O    1 
ATOM   1279 O  O    B GLY   A 1 47  ? 20.732 6.248   0.143   0.32 10.45 ?  47  GLY   A O    1 
ATOM   1280 H  H    A GLY   A 1 47  ? 22.018 7.872   -0.936  0.68 14.85 ?  47  GLY   A H    1 
ATOM   1281 H  H    B GLY   A 1 47  ? 21.974 7.995   -0.767  0.32 13.32 ?  47  GLY   A H    1 
ATOM   1282 H  HA2  A GLY   A 1 47  ? 19.716 8.979   -0.136  0.68 14.35 ?  47  GLY   A HA2  1 
ATOM   1283 H  HA2  B GLY   A 1 47  ? 19.864 9.065   0.446   0.32 13.44 ?  47  GLY   A HA2  1 
ATOM   1284 H  HA3  A GLY   A 1 47  ? 19.752 8.541   -1.651  0.68 14.35 ?  47  GLY   A HA3  1 
ATOM   1285 H  HA3  B GLY   A 1 47  ? 19.638 8.810   -1.093  0.32 13.44 ?  47  GLY   A HA3  1 
ATOM   1286 N  N    A GLY   A 1 48  ? 18.511 6.658   -0.305  0.68 11.65 ?  48  GLY   A N    1 
ATOM   1287 N  N    B GLY   A 1 48  ? 18.538 6.777   0.065   0.32 11.23 ?  48  GLY   A N    1 
ATOM   1288 C  CA   A GLY   A 1 48  ? 18.105 5.341   0.126   0.68 12.06 ?  48  GLY   A CA   1 
ATOM   1289 C  CA   B GLY   A 1 48  ? 18.123 5.422   0.378   0.32 11.26 ?  48  GLY   A CA   1 
ATOM   1290 C  C    A GLY   A 1 48  ? 18.592 5.058   1.532   0.68 11.39 ?  48  GLY   A C    1 
ATOM   1291 C  C    B GLY   A 1 48  ? 18.630 4.993   1.737   0.32 11.01 ?  48  GLY   A C    1 
ATOM   1292 O  O    A GLY   A 1 48  ? 18.781 5.967   2.353   0.68 11.47 ?  48  GLY   A O    1 
ATOM   1293 O  O    B GLY   A 1 48  ? 18.711 5.789   2.681   0.32 11.56 ?  48  GLY   A O    1 
ATOM   1294 H  H    A GLY   A 1 48  ? 17.861 7.195   -0.482  0.68 13.98 ?  48  GLY   A H    1 
ATOM   1295 H  H    B GLY   A 1 48  ? 17.892 7.331   -0.054  0.32 13.49 ?  48  GLY   A H    1 
ATOM   1296 H  HA2  A GLY   A 1 48  ? 17.139 5.263   0.110   0.68 14.48 ?  48  GLY   A HA2  1 
ATOM   1297 H  HA2  B GLY   A 1 48  ? 17.156 5.367   0.374   0.32 13.52 ?  48  GLY   A HA2  1 
ATOM   1298 H  HA3  A GLY   A 1 48  ? 18.485 4.671   -0.460  0.68 14.48 ?  48  GLY   A HA3  1 
ATOM   1299 H  HA3  B GLY   A 1 48  ? 18.473 4.809   -0.288  0.32 13.52 ?  48  GLY   A HA3  1 
ATOM   1300 N  N    A VAL   A 1 49  ? 18.805 3.771   1.812   0.68 11.20 ?  49  VAL   A N    1 
ATOM   1301 N  N    B VAL   A 1 49  ? 18.979 3.709   1.842   0.32 10.60 ?  49  VAL   A N    1 
ATOM   1302 C  CA   A VAL   A 1 49  ? 19.312 3.356   3.116   0.68 11.24 ?  49  VAL   A CA   1 
ATOM   1303 C  CA   B VAL   A 1 49  ? 19.549 3.188   3.081   0.32 10.06 ?  49  VAL   A CA   1 
ATOM   1304 C  C    A VAL   A 1 49  ? 20.623 4.062   3.439   0.68 10.46 ?  49  VAL   A C    1 
ATOM   1305 C  C    B VAL   A 1 49  ? 20.803 3.966   3.456   0.32 9.14  ?  49  VAL   A C    1 
ATOM   1306 O  O    A VAL   A 1 49  ? 20.834 4.503   4.572   0.68 10.83 ?  49  VAL   A O    1 
ATOM   1307 O  O    B VAL   A 1 49  ? 20.980 4.372   4.610   0.32 9.02  ?  49  VAL   A O    1 
ATOM   1308 C  CB   A VAL   A 1 49  ? 19.468 1.822   3.152   0.68 11.77 ?  49  VAL   A CB   1 
ATOM   1309 C  CB   B VAL   A 1 49  ? 19.853 1.685   2.943   0.32 9.87  ?  49  VAL   A CB   1 
ATOM   1310 C  CG1  A VAL   A 1 49  ? 20.273 1.378   4.372   0.68 11.54 ?  49  VAL   A CG1  1 
ATOM   1311 C  CG1  B VAL   A 1 49  ? 20.708 1.214   4.117   0.32 9.43  ?  49  VAL   A CG1  1 
ATOM   1312 C  CG2  A VAL   A 1 49  ? 18.099 1.149   3.137   0.68 13.64 ?  49  VAL   A CG2  1 
ATOM   1313 C  CG2  B VAL   A 1 49  ? 18.573 0.872   2.843   0.32 10.14 ?  49  VAL   A CG2  1 
ATOM   1314 H  H    A VAL   A 1 49  ? 18.663 3.121   1.269   0.68 13.44 ?  49  VAL   A H    1 
ATOM   1315 H  H    B VAL   A 1 49  ? 18.903 3.130   1.215   0.32 12.72 ?  49  VAL   A H    1 
ATOM   1316 H  HA   A VAL   A 1 49  ? 18.672 3.596   3.802   0.68 13.49 ?  49  VAL   A HA   1 
ATOM   1317 H  HA   B VAL   A 1 49  ? 18.907 3.294   3.798   0.32 12.08 ?  49  VAL   A HA   1 
ATOM   1318 H  HB   A VAL   A 1 49  ? 19.954 1.533   2.363   0.68 14.13 ?  49  VAL   A HB   1 
ATOM   1319 H  HB   B VAL   A 1 49  ? 20.359 1.539   2.129   0.32 11.85 ?  49  VAL   A HB   1 
ATOM   1320 H  HG11 A VAL   A 1 49  ? 20.124 0.431   4.518   0.68 13.85 ?  49  VAL   A HG11 1 
ATOM   1321 H  HG11 B VAL   A 1 49  ? 20.635 0.250   4.197   0.32 11.32 ?  49  VAL   A HG11 1 
ATOM   1322 H  HG12 A VAL   A 1 49  ? 21.213 1.545   4.212   0.68 13.85 ?  49  VAL   A HG12 1 
ATOM   1323 H  HG12 B VAL   A 1 49  ? 21.636 1.458   3.956   0.32 11.32 ?  49  VAL   A HG12 1 
ATOM   1324 H  HG13 A VAL   A 1 49  ? 19.970 1.881   5.145   0.68 13.85 ?  49  VAL   A HG13 1 
ATOM   1325 H  HG13 B VAL   A 1 49  ? 20.391 1.636   4.931   0.32 11.32 ?  49  VAL   A HG13 1 
ATOM   1326 H  HG21 A VAL   A 1 49  ? 18.219 0.186   3.157   0.68 16.38 ?  49  VAL   A HG21 1 
ATOM   1327 H  HG21 B VAL   A 1 49  ? 18.799 -0.058  2.687   0.32 12.17 ?  49  VAL   A HG21 1 
ATOM   1328 H  HG22 A VAL   A 1 49  ? 17.599 1.437   3.915   0.68 16.38 ?  49  VAL   A HG22 1 
ATOM   1329 H  HG22 B VAL   A 1 49  ? 18.082 0.958   3.676   0.32 12.17 ?  49  VAL   A HG22 1 
ATOM   1330 H  HG23 A VAL   A 1 49  ? 17.634 1.408   2.327   0.68 16.38 ?  49  VAL   A HG23 1 
ATOM   1331 H  HG23 B VAL   A 1 49  ? 18.041 1.212   2.107   0.32 12.17 ?  49  VAL   A HG23 1 
ATOM   1332 N  N    A ALA   A 1 50  ? 21.534 4.141   2.466   0.68 9.94  ?  50  ALA   A N    1 
ATOM   1333 N  N    B ALA   A 1 50  ? 21.705 4.154   2.492   0.32 8.89  ?  50  ALA   A N    1 
ATOM   1334 C  CA   A ALA   A 1 50  ? 22.857 4.701   2.727   0.68 9.58  ?  50  ALA   A CA   1 
ATOM   1335 C  CA   B ALA   A 1 50  ? 23.000 4.750   2.797   0.32 9.19  ?  50  ALA   A CA   1 
ATOM   1336 C  C    A ALA   A 1 50  ? 22.765 6.156   3.153   0.68 9.59  ?  50  ALA   A C    1 
ATOM   1337 C  C    B ALA   A 1 50  ? 22.851 6.207   3.209   0.32 9.37  ?  50  ALA   A C    1 
ATOM   1338 O  O    A ALA   A 1 50  ? 23.405 6.574   4.124   0.68 10.12 ?  50  ALA   A O    1 
ATOM   1339 O  O    B ALA   A 1 50  ? 23.451 6.648   4.196   0.32 9.59  ?  50  ALA   A O    1 
ATOM   1340 C  CB   A ALA   A 1 50  ? 23.725 4.573   1.481   0.68 9.43  ?  50  ALA   A CB   1 
ATOM   1341 C  CB   B ALA   A 1 50  ? 23.933 4.616   1.594   0.32 9.25  ?  50  ALA   A CB   1 
ATOM   1342 H  H    A ALA   A 1 50  ? 21.412 3.874   1.656   0.68 11.94 ?  50  ALA   A H    1 
ATOM   1343 H  H    B ALA   A 1 50  ? 21.589 3.943   1.665   0.32 10.68 ?  50  ALA   A H    1 
ATOM   1344 H  HA   A ALA   A 1 50  ? 23.281 4.207   3.447   0.68 11.50 ?  50  ALA   A HA   1 
ATOM   1345 H  HA   B ALA   A 1 50  ? 23.398 4.275   3.539   0.32 11.03 ?  50  ALA   A HA   1 
ATOM   1346 H  HB1  A ALA   A 1 50  ? 24.600 4.952   1.667   0.68 11.32 ?  50  ALA   A HB1  1 
ATOM   1347 H  HB1  B ALA   A 1 50  ? 24.787 5.019   1.811   0.32 11.10 ?  50  ALA   A HB1  1 
ATOM   1348 H  HB2  A ALA   A 1 50  ? 23.810 3.638   1.247   0.68 11.32 ?  50  ALA   A HB2  1 
ATOM   1349 H  HB2  B ALA   A 1 50  ? 24.053 3.674   1.391   0.32 11.10 ?  50  ALA   A HB2  1 
ATOM   1350 H  HB3  A ALA   A 1 50  ? 23.303 5.061   0.755   0.68 11.32 ?  50  ALA   A HB3  1 
ATOM   1351 H  HB3  B ALA   A 1 50  ? 23.537 5.069   0.833   0.32 11.10 ?  50  ALA   A HB3  1 
ATOM   1352 N  N    A GLY   A 1 51  ? 21.985 6.952   2.423   0.68 9.67  ?  51  GLY   A N    1 
ATOM   1353 N  N    B GLY   A 1 51  ? 22.055 6.972   2.463   0.32 9.77  ?  51  GLY   A N    1 
ATOM   1354 C  CA   A GLY   A 1 51  ? 21.826 8.341   2.805   0.68 10.47 ?  51  GLY   A CA   1 
ATOM   1355 C  CA   B GLY   A 1 51  ? 21.845 8.360   2.829   0.32 10.27 ?  51  GLY   A CA   1 
ATOM   1356 C  C    A GLY   A 1 51  ? 21.227 8.483   4.189   0.68 10.34 ?  51  GLY   A C    1 
ATOM   1357 C  C    B GLY   A 1 51  ? 21.211 8.502   4.198   0.32 10.32 ?  51  GLY   A C    1 
ATOM   1358 O  O    A GLY   A 1 51  ? 21.619 9.363   4.959   0.68 11.06 ?  51  GLY   A O    1 
ATOM   1359 O  O    B GLY   A 1 51  ? 21.565 9.399   4.967   0.32 10.62 ?  51  GLY   A O    1 
ATOM   1360 H  H    A GLY   A 1 51  ? 21.553 6.711   1.716   0.68 11.61 ?  51  GLY   A H    1 
ATOM   1361 H  H    B GLY   A 1 51  ? 21.640 6.714   1.754   0.32 11.73 ?  51  GLY   A H    1 
ATOM   1362 H  HA2  A GLY   A 1 51  ? 22.689 8.780   2.794   0.68 12.57 ?  51  GLY   A HA2  1 
ATOM   1363 H  HA2  B GLY   A 1 51  ? 22.696 8.824   2.835   0.32 12.33 ?  51  GLY   A HA2  1 
ATOM   1364 H  HA3  A GLY   A 1 51  ? 21.243 8.786   2.168   0.68 12.57 ?  51  GLY   A HA3  1 
ATOM   1365 H  HA3  B GLY   A 1 51  ? 21.267 8.784   2.178   0.32 12.33 ?  51  GLY   A HA3  1 
ATOM   1366 N  N    . ALA   A 1 52  ? 20.264 7.617   4.522   1.00 10.52 ?  52  ALA   A N    1 
ATOM   1367 C  CA   . ALA   A 1 52  ? 19.610 7.679   5.824   1.00 11.17 ?  52  ALA   A CA   1 
ATOM   1368 C  C    . ALA   A 1 52  ? 20.559 7.268   6.949   1.00 10.47 ?  52  ALA   A C    1 
ATOM   1369 O  O    . ALA   A 1 52  ? 20.628 7.934   7.987   1.00 11.30 ?  52  ALA   A O    1 
ATOM   1370 C  CB   . ALA   A 1 52  ? 18.352 6.807   5.807   1.00 12.77 ?  52  ALA   A CB   1 
ATOM   1371 H  H    A ALA   A 1 52  ? 19.983 6.978   4.013   0.68 12.63 ?  52  ALA   A H    1 
ATOM   1372 H  H    B ALA   A 1 52  ? 19.995 6.972   4.013   0.32 12.63 ?  52  ALA   A H    1 
ATOM   1373 H  HA   . ALA   A 1 52  ? 19.334 8.588   5.988   1.00 13.41 ?  52  ALA   A HA   1 
ATOM   1374 H  HB1  . ALA   A 1 52  ? 17.903 6.885   6.666   1.00 15.33 ?  52  ALA   A HB1  1 
ATOM   1375 H  HB2  . ALA   A 1 52  ? 17.762 7.120   5.101   1.00 15.33 ?  52  ALA   A HB2  1 
ATOM   1376 H  HB3  . ALA   A 1 52  ? 18.601 5.886   5.645   1.00 15.33 ?  52  ALA   A HB3  1 
ATOM   1377 N  N    A LEU   A 1 53  ? 21.296 6.171   6.772   0.68 10.31 ?  53  LEU   A N    1 
ATOM   1378 N  N    B LEU   A 1 53  ? 21.294 6.166   6.762   0.32 10.29 ?  53  LEU   A N    1 
ATOM   1379 C  CA   A LEU   A 1 53  ? 22.263 5.781   7.796   0.68 10.48 ?  53  LEU   A CA   1 
ATOM   1380 C  CA   B LEU   A 1 53  ? 22.265 5.746   7.771   0.32 10.40 ?  53  LEU   A CA   1 
ATOM   1381 C  C    A LEU   A 1 53  ? 23.313 6.864   7.975   0.68 9.66  ?  53  LEU   A C    1 
ATOM   1382 C  C    B LEU   A 1 53  ? 23.294 6.839   8.010   0.32 10.43 ?  53  LEU   A C    1 
ATOM   1383 O  O    A LEU   A 1 53  ? 23.643 7.246   9.100   0.68 10.64 ?  53  LEU   A O    1 
ATOM   1384 O  O    B LEU   A 1 53  ? 23.609 7.173   9.156   0.32 11.21 ?  53  LEU   A O    1 
ATOM   1385 C  CB   A LEU   A 1 53  ? 22.926 4.446   7.443   0.68 11.19 ?  53  LEU   A CB   1 
ATOM   1386 C  CB   B LEU   A 1 53  ? 22.969 4.451   7.343   0.32 10.28 ?  53  LEU   A CB   1 
ATOM   1387 C  CG   A LEU   A 1 53  ? 22.003 3.220   7.455   0.68 11.74 ?  53  LEU   A CG   1 
ATOM   1388 C  CG   B LEU   A 1 53  ? 22.284 3.084   7.487   0.32 9.60  ?  53  LEU   A CG   1 
ATOM   1389 C  CD1  A LEU   A 1 53  ? 22.730 2.006   6.906   0.68 11.81 ?  53  LEU   A CD1  1 
ATOM   1390 C  CD1  B LEU   A 1 53  ? 23.173 2.008   6.872   0.32 9.77  ?  53  LEU   A CD1  1 
ATOM   1391 C  CD2  A LEU   A 1 53  ? 21.469 2.941   8.853   0.68 12.55 ?  53  LEU   A CD2  1 
ATOM   1392 C  CD2  B LEU   A 1 53  ? 21.974 2.737   8.935   0.32 9.07  ?  53  LEU   A CD2  1 
ATOM   1393 H  H    A LEU   A 1 53  ? 21.253 5.643   6.092   0.68 12.38 ?  53  LEU   A H    1 
ATOM   1394 H  H    B LEU   A 1 53  ? 21.254 5.655   6.072   0.32 12.35 ?  53  LEU   A H    1 
ATOM   1395 H  HA   A LEU   A 1 53  ? 21.802 5.666   8.640   0.68 12.58 ?  53  LEU   A HA   1 
ATOM   1396 H  HA   B LEU   A 1 53  ? 21.807 5.579   8.608   0.32 12.48 ?  53  LEU   A HA   1 
ATOM   1397 H  HB2  A LEU   A 1 53  ? 23.304 4.516   6.550   0.68 13.44 ?  53  LEU   A HB2  1 
ATOM   1398 H  HB2  B LEU   A 1 53  ? 23.187 4.539   6.403   0.32 12.34 ?  53  LEU   A HB2  1 
ATOM   1399 H  HB3  A LEU   A 1 53  ? 23.639 4.277   8.079   0.68 13.44 ?  53  LEU   A HB3  1 
ATOM   1400 H  HB3  B LEU   A 1 53  ? 23.793 4.388   7.847   0.32 12.34 ?  53  LEU   A HB3  1 
ATOM   1401 H  HG   A LEU   A 1 53  ? 21.244 3.395   6.874   0.68 14.10 ?  53  LEU   A HG   1 
ATOM   1402 H  HG   B LEU   A 1 53  ? 21.449 3.088   6.994   0.32 11.53 ?  53  LEU   A HG   1 
ATOM   1403 H  HD11 A LEU   A 1 53  ? 22.129 1.246   6.922   0.68 14.17 ?  53  LEU   A HD11 1 
ATOM   1404 H  HD11 B LEU   A 1 53  ? 22.739 1.145   6.969   0.32 11.73 ?  53  LEU   A HD11 1 
ATOM   1405 H  HD12 A LEU   A 1 53  ? 23.009 2.191   5.996   0.68 14.17 ?  53  LEU   A HD12 1 
ATOM   1406 H  HD12 B LEU   A 1 53  ? 23.307 2.208   5.933   0.32 11.73 ?  53  LEU   A HD12 1 
ATOM   1407 H  HD13 A LEU   A 1 53  ? 23.505 1.830   7.462   0.68 14.17 ?  53  LEU   A HD13 1 
ATOM   1408 H  HD13 B LEU   A 1 53  ? 24.026 2.002   7.335   0.32 11.73 ?  53  LEU   A HD13 1 
ATOM   1409 H  HD21 A LEU   A 1 53  ? 20.965 2.113   8.840   0.68 15.06 ?  53  LEU   A HD21 1 
ATOM   1410 H  HD21 B LEU   A 1 53  ? 21.445 1.922   8.961   0.32 10.89 ?  53  LEU   A HD21 1 
ATOM   1411 H  HD22 A LEU   A 1 53  ? 22.214 2.868   9.467   0.68 15.06 ?  53  LEU   A HD22 1 
ATOM   1412 H  HD22 B LEU   A 1 53  ? 22.807 2.602   9.414   0.32 10.89 ?  53  LEU   A HD22 1 
ATOM   1413 H  HD23 A LEU   A 1 53  ? 20.890 3.673   9.122   0.68 15.06 ?  53  LEU   A HD23 1 
ATOM   1414 H  HD23 B LEU   A 1 53  ? 21.477 3.465   9.335   0.32 10.89 ?  53  LEU   A HD23 1 
ATOM   1415 N  N    A ASN   A 1 54  ? 23.846 7.377   6.872   0.68 9.76  ?  54  ASN   A N    1 
ATOM   1416 N  N    B ASN   A 1 54  ? 23.830 7.413   6.934   0.32 10.31 ?  54  ASN   A N    1 
ATOM   1417 C  CA   A ASN   A 1 54  ? 24.891 8.380   6.995   0.68 9.95  ?  54  ASN   A CA   1 
ATOM   1418 C  CA   B ASN   A 1 54  ? 24.881 8.408   7.095   0.32 10.08 ?  54  ASN   A CA   1 
ATOM   1419 C  C    A ASN   A 1 54  ? 24.377 9.633   7.702   0.68 10.31 ?  54  ASN   A C    1 
ATOM   1420 C  C    B ASN   A 1 54  ? 24.360 9.640   7.827   0.32 10.07 ?  54  ASN   A C    1 
ATOM   1421 O  O    A ASN   A 1 54  ? 25.083 10.216  8.534   0.68 10.73 ?  54  ASN   A O    1 
ATOM   1422 O  O    B ASN   A 1 54  ? 25.011 10.150  8.746   0.32 10.12 ?  54  ASN   A O    1 
ATOM   1423 C  CB   A ASN   A 1 54  ? 25.455 8.723   5.627   0.68 10.22 ?  54  ASN   A CB   1 
ATOM   1424 C  CB   B ASN   A 1 54  ? 25.467 8.791   5.741   0.32 9.85  ?  54  ASN   A CB   1 
ATOM   1425 C  CG   A ASN   A 1 54  ? 26.497 9.796   5.718   0.68 10.38 ?  54  ASN   A CG   1 
ATOM   1426 C  CG   B ASN   A 1 54  ? 26.429 9.946   5.855   0.32 8.89  ?  54  ASN   A CG   1 
ATOM   1427 O  OD1  A ASN   A 1 54  ? 27.493 9.640   6.433   0.68 10.90 ?  54  ASN   A OD1  1 
ATOM   1428 O  OD1  B ASN   A 1 54  ? 27.464 9.835   6.517   0.32 8.65  ?  54  ASN   A OD1  1 
ATOM   1429 N  ND2  A ASN   A 1 54  ? 26.282 10.902  5.027   0.68 11.07 ?  54  ASN   A ND2  1 
ATOM   1430 N  ND2  B ASN   A 1 54  ? 26.090 11.072  5.237   0.32 9.09  ?  54  ASN   A ND2  1 
ATOM   1431 H  H    A ASN   A 1 54  ? 23.626 7.161   6.069   0.68 11.72 ?  54  ASN   A H    1 
ATOM   1432 H  H    B ASN   A 1 54  ? 23.600 7.252   6.119   0.32 12.38 ?  54  ASN   A H    1 
ATOM   1433 H  HA   A ASN   A 1 54  ? 25.605 8.014   7.533   0.68 11.95 ?  54  ASN   A HA   1 
ATOM   1434 H  HA   B ASN   A 1 54  ? 25.592 8.027   7.628   0.32 12.10 ?  54  ASN   A HA   1 
ATOM   1435 H  HB2  A ASN   A 1 54  ? 25.873 7.929   5.253   0.68 12.27 ?  54  ASN   A HB2  1 
ATOM   1436 H  HB2  B ASN   A 1 54  ? 25.953 8.030   5.379   0.32 11.83 ?  54  ASN   A HB2  1 
ATOM   1437 H  HB3  A ASN   A 1 54  ? 24.745 9.034   5.054   0.68 12.27 ?  54  ASN   A HB3  1 
ATOM   1438 H  HB3  B ASN   A 1 54  ? 24.753 9.048   5.142   0.32 11.83 ?  54  ASN   A HB3  1 
ATOM   1439 H  HD21 A ASN   A 1 54  ? 26.850 11.545  5.062   0.68 13.29 ?  54  ASN   A HD21 1 
ATOM   1440 H  HD21 B ASN   A 1 54  ? 26.606 11.759  5.281   0.32 10.92 ?  54  ASN   A HD21 1 
ATOM   1441 H  HD22 A ASN   A 1 54  ? 25.577 10.971  4.544   0.68 13.29 ?  54  ASN   A HD22 1 
ATOM   1442 H  HD22 B ASN   A 1 54  ? 25.360 11.110  4.786   0.32 10.92 ?  54  ASN   A HD22 1 
ATOM   1443 N  N    A LYS   A 1 55  ? 23.153 10.067  7.377   0.68 10.45 ?  55  LYS   A N    1 
ATOM   1444 N  N    B LYS   A 1 55  ? 23.181 10.132  7.431   0.32 10.29 ?  55  LYS   A N    1 
ATOM   1445 C  CA   A LYS   A 1 55  ? 22.565 11.222  8.046   0.68 11.22 ?  55  LYS   A CA   1 
ATOM   1446 C  CA   B LYS   A 1 55  ? 22.606 11.292  8.101   0.32 11.20 ?  55  LYS   A CA   1 
ATOM   1447 C  C    A LYS   A 1 55  ? 22.501 11.004  9.552   0.68 11.27 ?  55  LYS   A C    1 
ATOM   1448 C  C    B LYS   A 1 55  ? 22.451 11.036  9.594   0.32 11.48 ?  55  LYS   A C    1 
ATOM   1449 O  O    A LYS   A 1 55  ? 22.813 11.909  10.336  0.68 11.98 ?  55  LYS   A O    1 
ATOM   1450 O  O    B LYS   A 1 55  ? 22.654 11.942  10.412  0.32 11.60 ?  55  LYS   A O    1 
ATOM   1451 C  CB   A LYS   A 1 55  ? 21.177 11.480  7.459   0.68 11.69 ?  55  LYS   A CB   1 
ATOM   1452 C  CB   B LYS   A 1 55  ? 21.266 11.653  7.457   0.32 12.02 ?  55  LYS   A CB   1 
ATOM   1453 C  CG   A LYS   A 1 55  ? 20.424 12.642  8.070   0.68 13.35 ?  55  LYS   A CG   1 
ATOM   1454 C  CG   B LYS   A 1 55  ? 20.562 12.845  8.094   0.32 13.32 ?  55  LYS   A CG   1 
ATOM   1455 C  CD   A LYS   A 1 55  ? 19.075 12.806  7.382   0.68 14.53 ?  55  LYS   A CD   1 
ATOM   1456 C  CD   B LYS   A 1 55  ? 19.240 13.155  7.398   0.32 14.27 ?  55  LYS   A CD   1 
ATOM   1457 C  CE   A LYS   A 1 55  ? 18.252 13.937  7.977   0.68 15.92 ?  55  LYS   A CE   1 
ATOM   1458 C  CE   B LYS   A 1 55  ? 18.410 14.159  8.190   0.32 15.60 ?  55  LYS   A CE   1 
ATOM   1459 N  NZ   A LYS   A 1 55  ? 16.903 14.018  7.348   0.68 16.43 ?  55  LYS   A NZ   1 
ATOM   1460 N  NZ   B LYS   A 1 55  ? 17.074 14.397  7.572   0.32 16.05 ?  55  LYS   A NZ   1 
ATOM   1461 H  H    A LYS   A 1 55  ? 22.641 9.702   6.785   0.68 12.55 ?  55  LYS   A H    1 
ATOM   1462 H  H    B LYS   A 1 55  ? 22.699 9.811   6.793   0.32 12.35 ?  55  LYS   A H    1 
ATOM   1463 H  HA   A LYS   A 1 55  ? 23.112 12.001  7.876   0.68 13.46 ?  55  LYS   A HA   1 
ATOM   1464 H  HA   B LYS   A 1 55  ? 23.203 12.047  7.988   0.32 13.44 ?  55  LYS   A HA   1 
ATOM   1465 H  HB2  A LYS   A 1 55  ? 21.268 11.664  6.510   0.68 14.03 ?  55  LYS   A HB2  1 
ATOM   1466 H  HB2  B LYS   A 1 55  ? 21.418 11.870  6.523   0.32 14.43 ?  55  LYS   A HB2  1 
ATOM   1467 H  HB3  A LYS   A 1 55  ? 20.631 10.686  7.582   0.68 14.03 ?  55  LYS   A HB3  1 
ATOM   1468 H  HB3  B LYS   A 1 55  ? 20.671 10.892  7.524   0.32 14.43 ?  55  LYS   A HB3  1 
ATOM   1469 H  HG2  A LYS   A 1 55  ? 20.266 12.475  9.012   0.68 16.02 ?  55  LYS   A HG2  1 
ATOM   1470 H  HG2  B LYS   A 1 55  ? 20.370 12.648  9.024   0.32 15.99 ?  55  LYS   A HG2  1 
ATOM   1471 H  HG3  A LYS   A 1 55  ? 20.928 13.461  7.948   0.68 16.02 ?  55  LYS   A HG3  1 
ATOM   1472 H  HG3  B LYS   A 1 55  ? 21.129 13.629  8.027   0.32 15.99 ?  55  LYS   A HG3  1 
ATOM   1473 H  HD2  A LYS   A 1 55  ? 19.217 12.995  6.442   0.68 17.44 ?  55  LYS   A HD2  1 
ATOM   1474 H  HD2  B LYS   A 1 55  ? 19.419 13.534  6.523   0.32 17.13 ?  55  LYS   A HD2  1 
ATOM   1475 H  HD3  A LYS   A 1 55  ? 18.567 11.982  7.481   0.68 17.44 ?  55  LYS   A HD3  1 
ATOM   1476 H  HD3  B LYS   A 1 55  ? 18.725 12.337  7.309   0.32 17.13 ?  55  LYS   A HD3  1 
ATOM   1477 H  HE2  A LYS   A 1 55  ? 18.140 13.785  8.928   0.68 19.11 ?  55  LYS   A HE2  1 
ATOM   1478 H  HE2  B LYS   A 1 55  ? 18.270 13.816  9.088   0.32 18.72 ?  55  LYS   A HE2  1 
ATOM   1479 H  HE3  A LYS   A 1 55  ? 18.714 14.778  7.824   0.68 19.11 ?  55  LYS   A HE3  1 
ATOM   1480 H  HE3  B LYS   A 1 55  ? 18.881 15.005  8.226   0.32 18.72 ?  55  LYS   A HE3  1 
ATOM   1481 H  HZ1  A LYS   A 1 55  ? 16.339 14.430  7.899   0.68 19.72 ?  55  LYS   A HZ1  1 
ATOM   1482 H  HZ1  B LYS   A 1 55  ? 16.611 14.982  8.060   0.32 19.27 ?  55  LYS   A HZ1  1 
ATOM   1483 H  HZ2  A LYS   A 1 55  ? 16.949 14.478  6.587   0.68 19.72 ?  55  LYS   A HZ2  1 
ATOM   1484 H  HZ2  B LYS   A 1 55  ? 17.172 14.721  6.749   0.32 19.27 ?  55  LYS   A HZ2  1 
ATOM   1485 H  HZ3  A LYS   A 1 55  ? 16.597 13.201  7.178   0.68 19.72 ?  55  LYS   A HZ3  1 
ATOM   1486 H  HZ3  B LYS   A 1 55  ? 16.616 13.634  7.529   0.32 19.27 ?  55  LYS   A HZ3  1 
ATOM   1487 N  N    . ALA   A 1 56  ? 22.097 9.805   9.973   1.00 11.69 ?  56  ALA   A N    1 
ATOM   1488 C  CA   . ALA   A 1 56  ? 21.969 9.488   11.388  1.00 12.47 ?  56  ALA   A CA   1 
ATOM   1489 C  C    . ALA   A 1 56  ? 23.308 9.509   12.113  1.00 12.19 ?  56  ALA   A C    1 
ATOM   1490 O  O    . ALA   A 1 56  ? 23.329 9.691   13.331  1.00 13.57 ?  56  ALA   A O    1 
ATOM   1491 C  CB   . ALA   A 1 56  ? 21.273 8.136   11.570  1.00 13.33 ?  56  ALA   A CB   1 
ATOM   1492 H  H    A ALA   A 1 56  ? 21.898 9.155   9.450   0.68 14.03 ?  56  ALA   A H    1 
ATOM   1493 H  H    B ALA   A 1 56  ? 21.925 9.156   9.439   0.32 14.03 ?  56  ALA   A H    1 
ATOM   1494 H  HA   . ALA   A 1 56  ? 21.416 10.154  11.807  1.00 14.97 ?  56  ALA   A HA   1 
ATOM   1495 H  HB1  . ALA   A 1 56  ? 21.200 7.942   12.521  1.00 16.00 ?  56  ALA   A HB1  1 
ATOM   1496 H  HB2  . ALA   A 1 56  ? 20.388 8.184   11.177  1.00 16.00 ?  56  ALA   A HB2  1 
ATOM   1497 H  HB3  . ALA   A 1 56  ? 21.793 7.444   11.134  1.00 16.00 ?  56  ALA   A HB3  1 
ATOM   1498 N  N    . THR   A 1 57  ? 24.424 9.322   11.398  1.00 11.42 ?  57  THR   A N    1 
ATOM   1499 C  CA   . THR   A 1 57  ? 25.765 9.452   11.974  1.00 11.39 ?  57  THR   A CA   1 
ATOM   1500 C  C    . THR   A 1 57  ? 26.314 10.870  11.894  1.00 11.72 ?  57  THR   A C    1 
ATOM   1501 O  O    . THR   A 1 57  ? 27.499 11.080  12.182  1.00 12.48 ?  57  THR   A O    1 
ATOM   1502 C  CB   . THR   A 1 57  ? 26.781 8.507   11.303  1.00 11.42 ?  57  THR   A CB   1 
ATOM   1503 O  OG1  . THR   A 1 57  ? 27.159 8.999   10.003  1.00 10.99 ?  57  THR   A OG1  1 
ATOM   1504 C  CG2  . THR   A 1 57  ? 26.251 7.080   11.201  1.00 11.69 ?  57  THR   A CG2  1 
ATOM   1505 H  H    . THR   A 1 57  ? 24.433 9.096   10.567  1.00 13.71 ?  57  THR   A H    1 
ATOM   1506 H  HA   . THR   A 1 57  ? 25.722 9.197   12.915  1.00 13.68 ?  57  THR   A HA   1 
ATOM   1507 H  HB   . THR   A 1 57  ? 27.581 8.473   11.858  1.00 13.71 ?  57  THR   A HB   1 
ATOM   1508 H  HG1  . THR   A 1 57  ? 26.473 9.063   9.517   1.00 13.20 ?  57  THR   A HG1  1 
ATOM   1509 H  HG21 . THR   A 1 57  ? 26.933 6.493   10.832  1.00 14.04 ?  57  THR   A HG21 1 
ATOM   1510 H  HG22 . THR   A 1 57  ? 25.999 6.750   12.079  1.00 14.04 ?  57  THR   A HG22 1 
ATOM   1511 H  HG23 . THR   A 1 57  ? 25.474 7.051   10.623  1.00 14.04 ?  57  THR   A HG23 1 
ATOM   1512 N  N    . ASN   A 1 58  ? 25.501 11.842  11.487  1.00 12.24 ?  58  ASN   A N    1 
ATOM   1513 C  CA   . ASN   A 1 58  ? 25.968 13.221  11.388  1.00 13.03 ?  58  ASN   A CA   1 
ATOM   1514 C  C    . ASN   A 1 58  ? 27.118 13.342  10.383  1.00 12.08 ?  58  ASN   A C    1 
ATOM   1515 O  O    . ASN   A 1 58  ? 28.013 14.174  10.541  1.00 12.62 ?  58  ASN   A O    1 
ATOM   1516 C  CB   . ASN   A 1 58  ? 26.346 13.754  12.784  1.00 15.89 ?  58  ASN   A CB   1 
ATOM   1517 C  CG   . ASN   A 1 58  ? 26.767 15.206  12.782  1.00 19.60 ?  58  ASN   A CG   1 
ATOM   1518 O  OD1  . ASN   A 1 58  ? 26.146 16.034  12.131  1.00 21.38 ?  58  ASN   A OD1  1 
ATOM   1519 N  ND2  . ASN   A 1 58  ? 27.823 15.525  13.535  1.00 20.95 ?  58  ASN   A ND2  1 
ATOM   1520 H  H    . ASN   A 1 58  ? 24.679 11.722  11.253  1.00 14.69 ?  58  ASN   A H    1 
ATOM   1521 H  HA   . ASN   A 1 58  ? 25.236 13.760  11.059  1.00 15.64 ?  58  ASN   A HA   1 
ATOM   1522 H  HB2  . ASN   A 1 58  ? 25.570 13.668  13.373  1.00 19.07 ?  58  ASN   A HB2  1 
ATOM   1523 H  HB3  . ASN   A 1 58  ? 27.080 13.240  13.140  1.00 19.07 ?  58  ASN   A HB3  1 
ATOM   1524 H  HD21 . ASN   A 1 58  ? 28.093 16.342  13.571  1.00 25.15 ?  58  ASN   A HD21 1 
ATOM   1525 H  HD22 . ASN   A 1 58  ? 28.225 14.916  13.981  1.00 25.15 ?  58  ASN   A HD22 1 
ATOM   1526 N  N    . ASN   A 1 59  ? 27.097 12.520  9.331   1.00 11.25 ?  59  ASN   A N    1 
ATOM   1527 C  CA   . ASN   A 1 59  ? 28.082 12.496  8.242   1.00 10.98 ?  59  ASN   A CA   1 
ATOM   1528 C  C    . ASN   A 1 59  ? 29.398 11.815  8.635   1.00 10.75 ?  59  ASN   A C    1 
ATOM   1529 O  O    . ASN   A 1 59  ? 30.315 11.765  7.806   1.00 11.06 ?  59  ASN   A O    1 
ATOM   1530 C  CB   . ASN   A 1 59  ? 28.373 13.882  7.635   1.00 11.11 ?  59  ASN   A CB   1 
ATOM   1531 C  CG   . ASN   A 1 59  ? 28.737 13.810  6.167   1.00 11.36 ?  59  ASN   A CG   1 
ATOM   1532 O  OD1  . ASN   A 1 59  ? 28.028 13.190  5.371   1.00 11.67 ?  59  ASN   A OD1  1 
ATOM   1533 N  ND2  . ASN   A 1 59  ? 29.827 14.467  5.791   1.00 12.02 ?  59  ASN   A ND2  1 
ATOM   1534 H  H    . ASN   A 1 59  ? 26.479 11.930  9.217   1.00 13.51 ?  59  ASN   A H    1 
ATOM   1535 H  HA   . ASN   A 1 59  ? 27.703 11.967  7.529   1.00 13.18 ?  59  ASN   A HA   1 
ATOM   1536 H  HB2  . ASN   A 1 59  ? 27.583 14.441  7.717   1.00 13.34 ?  59  ASN   A HB2  1 
ATOM   1537 H  HB3  . ASN   A 1 59  ? 29.117 14.290  8.103   1.00 13.34 ?  59  ASN   A HB3  1 
ATOM   1538 H  HD21 . ASN   A 1 59  ? 30.077 14.455  4.966   1.00 14.43 ?  59  ASN   A HD21 1 
ATOM   1539 H  HD22 . ASN   A 1 59  ? 30.302 14.889  6.373   1.00 14.43 ?  59  ASN   A HD22 1 
ATOM   1540 N  N    . ALA   A 1 60  ? 29.521 11.270  9.847   1.00 10.75 ?  60  ALA   A N    1 
ATOM   1541 C  CA   . ALA   A 1 60  ? 30.753 10.578  10.209  1.00 10.96 ?  60  ALA   A CA   1 
ATOM   1542 C  C    . ALA   A 1 60  ? 30.974 9.343   9.347   1.00 10.96 ?  60  ALA   A C    1 
ATOM   1543 O  O    . ALA   A 1 60  ? 32.120 9.021   9.014   1.00 11.38 ?  60  ALA   A O    1 
ATOM   1544 C  CB   . ALA   A 1 60  ? 30.741 10.223  11.692  1.00 11.63 ?  60  ALA   A CB   1 
ATOM   1545 H  H    . ALA   A 1 60  ? 28.918 11.279  10.459  1.00 12.91 ?  60  ALA   A H    1 
ATOM   1546 H  HA   . ALA   A 1 60  ? 31.500 11.180  10.057  1.00 13.16 ?  60  ALA   A HA   1 
ATOM   1547 H  HB1  . ALA   A 1 60  ? 31.565 9.768   11.916  1.00 13.97 ?  60  ALA   A HB1  1 
ATOM   1548 H  HB2  . ALA   A 1 60  ? 30.661 11.041  12.210  1.00 13.97 ?  60  ALA   A HB2  1 
ATOM   1549 H  HB3  . ALA   A 1 60  ? 29.982 9.646   11.870  1.00 13.97 ?  60  ALA   A HB3  1 
ATOM   1550 N  N    . MET   A 1 61  ? 29.901 8.653   8.959   1.00 10.42 ?  61  MET   A N    1 
ATOM   1551 C  CA   . MET   A 1 61  ? 30.044 7.517   8.057   1.00 10.20 ?  61  MET   A CA   1 
ATOM   1552 C  C    . MET   A 1 61  ? 30.680 7.940   6.737   1.00 10.29 ?  61  MET   A C    1 
ATOM   1553 O  O    . MET   A 1 61  ? 31.573 7.259   6.223   1.00 10.68 ?  61  MET   A O    1 
ATOM   1554 C  CB   . MET   A 1 61  ? 28.684 6.857   7.839   1.00 10.15 ?  61  MET   A CB   1 
ATOM   1555 C  CG   . MET   A 1 61  ? 28.702 5.691   6.871   1.00 11.00 ?  61  MET   A CG   1 
ATOM   1556 S  SD   . MET   A 1 61  ? 27.076 4.941   6.660   1.00 11.84 ?  61  MET   A SD   1 
ATOM   1557 C  CE   . MET   A 1 61  ? 26.941 4.055   8.219   1.00 13.20 ?  61  MET   A CE   1 
ATOM   1558 H  H    . MET   A 1 61  ? 29.095 8.825   9.195   1.00 12.51 ?  61  MET   A H    1 
ATOM   1559 H  HA   . MET   A 1 61  ? 30.621 6.861   8.478   1.00 12.25 ?  61  MET   A HA   1 
ATOM   1560 H  HB2  . MET   A 1 61  ? 28.360 6.525   8.691   1.00 12.18 ?  61  MET   A HB2  1 
ATOM   1561 H  HB3  . MET   A 1 61  ? 28.067 7.517   7.490   1.00 12.18 ?  61  MET   A HB3  1 
ATOM   1562 H  HG2  . MET   A 1 61  ? 28.988 5.992   5.998   1.00 13.21 ?  61  MET   A HG2  1 
ATOM   1563 H  HG3  . MET   A 1 61  ? 29.298 5.002   7.202   1.00 13.21 ?  61  MET   A HG3  1 
ATOM   1564 H  HE1  . MET   A 1 61  ? 26.100 3.569   8.238   1.00 15.84 ?  61  MET   A HE1  1 
ATOM   1565 H  HE2  . MET   A 1 61  ? 27.682 3.435   8.296   1.00 15.84 ?  61  MET   A HE2  1 
ATOM   1566 H  HE3  . MET   A 1 61  ? 26.967 4.692   8.954   1.00 15.84 ?  61  MET   A HE3  1 
ATOM   1567 N  N    . GLN   A 1 62  ? 30.242 9.070   6.180   1.00 10.23 ?  62  GLN   A N    1 
ATOM   1568 C  CA   . GLN   A 1 62  ? 30.806 9.536   4.917   1.00 10.44 ?  62  GLN   A CA   1 
ATOM   1569 C  C    . GLN   A 1 62  ? 32.277 9.913   5.064   1.00 10.32 ?  62  GLN   A C    1 
ATOM   1570 O  O    . GLN   A 1 62  ? 33.089 9.599   4.189   1.00 10.74 ?  62  GLN   A O    1 
ATOM   1571 C  CB   . GLN   A 1 62  ? 30.008 10.723  4.386   1.00 10.43 ?  62  GLN   A CB   1 
ATOM   1572 C  CG   . GLN   A 1 62  ? 30.386 11.087  2.964   1.00 10.47 ?  62  GLN   A CG   1 
ATOM   1573 C  CD   . GLN   A 1 62  ? 30.061 9.956   2.014   1.00 10.71 ?  62  GLN   A CD   1 
ATOM   1574 O  OE1  . GLN   A 1 62  ? 28.883 9.646   1.798   1.00 11.35 ?  62  GLN   A OE1  1 
ATOM   1575 N  NE2  . GLN   A 1 62  ? 31.085 9.289   1.490   1.00 11.22 ?  62  GLN   A NE2  1 
ATOM   1576 H  H    . GLN   A 1 62  ? 29.623 9.567   6.506   1.00 12.28 ?  62  GLN   A H    1 
ATOM   1577 H  HA   . GLN   A 1 62  ? 30.748 8.816   4.269   1.00 12.53 ?  62  GLN   A HA   1 
ATOM   1578 H  HB2  . GLN   A 1 62  ? 29.064 10.507  4.405   1.00 12.52 ?  62  GLN   A HB2  1 
ATOM   1579 H  HB3  . GLN   A 1 62  ? 30.182 11.497  4.950   1.00 12.52 ?  62  GLN   A HB3  1 
ATOM   1580 H  HG2  . GLN   A 1 62  ? 29.876 11.866  2.687   1.00 12.57 ?  62  GLN   A HG2  1 
ATOM   1581 H  HG3  . GLN   A 1 62  ? 31.334 11.269  2.912   1.00 12.57 ?  62  GLN   A HG3  1 
ATOM   1582 H  HE21 . GLN   A 1 62  ? 31.892 9.522   1.683   1.00 13.47 ?  62  GLN   A HE21 1 
ATOM   1583 H  HE22 . GLN   A 1 62  ? 30.943 8.631   0.957   1.00 13.47 ?  62  GLN   A HE22 1 
ATOM   1584 N  N    . VAL   A 1 63  ? 32.635 10.597  6.152   1.00 10.93 ?  63  VAL   A N    1 
ATOM   1585 C  CA   . VAL   A 1 63  ? 34.026 10.991  6.366   1.00 11.72 ?  63  VAL   A CA   1 
ATOM   1586 C  C    . VAL   A 1 63  ? 34.921 9.755   6.436   1.00 11.10 ?  63  VAL   A C    1 
ATOM   1587 O  O    . VAL   A 1 63  ? 35.975 9.684   5.787   1.00 11.82 ?  63  VAL   A O    1 
ATOM   1588 C  CB   . VAL   A 1 63  ? 34.133 11.872  7.625   1.00 13.28 ?  63  VAL   A CB   1 
ATOM   1589 C  CG1  . VAL   A 1 63  ? 35.574 12.113  7.988   1.00 14.98 ?  63  VAL   A CG1  1 
ATOM   1590 C  CG2  . VAL   A 1 63  ? 33.412 13.203  7.404   1.00 13.73 ?  63  VAL   A CG2  1 
ATOM   1591 H  H    . VAL   A 1 63  ? 32.092 10.844  6.777   1.00 13.13 ?  63  VAL   A H    1 
ATOM   1592 H  HA   . VAL   A 1 63  ? 34.313 11.523  5.610   1.00 14.06 ?  63  VAL   A HA   1 
ATOM   1593 H  HB   . VAL   A 1 63  ? 33.711 11.422  8.371   1.00 15.95 ?  63  VAL   A HB   1 
ATOM   1594 H  HG11 . VAL   A 1 63  ? 35.623 12.850  8.614   1.00 17.99 ?  63  VAL   A HG11 1 
ATOM   1595 H  HG12 . VAL   A 1 63  ? 35.938 11.310  8.390   1.00 17.99 ?  63  VAL   A HG12 1 
ATOM   1596 H  HG13 . VAL   A 1 63  ? 36.068 12.334  7.180   1.00 17.99 ?  63  VAL   A HG13 1 
ATOM   1597 H  HG21 . VAL   A 1 63  ? 33.499 13.750  8.204   1.00 16.49 ?  63  VAL   A HG21 1 
ATOM   1598 H  HG22 . VAL   A 1 63  ? 33.814 13.663  6.649   1.00 16.49 ?  63  VAL   A HG22 1 
ATOM   1599 H  HG23 . VAL   A 1 63  ? 32.475 13.031  7.225   1.00 16.49 ?  63  VAL   A HG23 1 
ATOM   1600 N  N    . GLU   A 1 64  ? 34.495 8.750   7.207   1.00 10.96 ?  64  GLU   A N    1 
ATOM   1601 C  CA   . GLU   A 1 64  ? 35.252 7.509   7.309   1.00 11.37 ?  64  GLU   A CA   1 
ATOM   1602 C  C    . GLU   A 1 64  ? 35.349 6.823   5.953   1.00 11.04 ?  64  GLU   A C    1 
ATOM   1603 O  O    . GLU   A 1 64  ? 36.402 6.281   5.580   1.00 11.42 ?  64  GLU   A O    1 
ATOM   1604 C  CB   . GLU   A 1 64  ? 34.560 6.598   8.321   1.00 11.50 ?  64  GLU   A CB   1 
ATOM   1605 C  CG   . GLU   A 1 64  ? 35.214 5.249   8.470   1.00 12.41 ?  64  GLU   A CG   1 
ATOM   1606 C  CD   . GLU   A 1 64  ? 34.336 4.256   9.203   1.00 12.81 ?  64  GLU   A CD   1 
ATOM   1607 O  OE1  . GLU   A 1 64  ? 33.097 4.351   9.065   1.00 13.55 ?  64  GLU   A OE1  1 
ATOM   1608 O  OE2  . GLU   A 1 64  ? 34.881 3.372   9.897   1.00 13.07 -1 64  GLU   A OE2  1 
ATOM   1609 H  H    . GLU   A 1 64  ? 33.767 8.761   7.669   1.00 13.16 ?  64  GLU   A H    1 
ATOM   1610 H  HA   . GLU   A 1 64  ? 36.149 7.707   7.627   1.00 13.65 ?  64  GLU   A HA   1 
ATOM   1611 H  HB2  . GLU   A 1 64  ? 34.575 7.035   9.192   1.00 13.80 ?  64  GLU   A HB2  1 
ATOM   1612 H  HB3  . GLU   A 1 64  ? 33.644 6.465   8.039   1.00 13.80 ?  64  GLU   A HB3  1 
ATOM   1613 H  HG2  . GLU   A 1 64  ? 35.409 4.880   7.593   1.00 14.90 ?  64  GLU   A HG2  1 
ATOM   1614 H  HG3  . GLU   A 1 64  ? 36.035 5.350   8.974   1.00 14.90 ?  64  GLU   A HG3  1 
ATOM   1615 N  N    . SER   A 1 65  ? 34.236 6.816   5.213   1.00 10.48 ?  65  SER   A N    1 
ATOM   1616 C  CA   . SER   A 1 65  ? 34.191 6.154   3.915   1.00 10.46 ?  65  SER   A CA   1 
ATOM   1617 C  C    . SER   A 1 65  ? 35.113 6.824   2.906   1.00 10.64 ?  65  SER   A C    1 
ATOM   1618 O  O    . SER   A 1 65  ? 35.745 6.143   2.093   1.00 11.45 ?  65  SER   A O    1 
ATOM   1619 C  CB   . SER   A 1 65  ? 32.758 6.156   3.379   1.00 10.71 ?  65  SER   A CB   1 
ATOM   1620 O  OG   . SER   A 1 65  ? 31.904 5.347   4.177   1.00 11.03 ?  65  SER   A OG   1 
ATOM   1621 H  H    . SER   A 1 65  ? 33.498 7.198   5.440   1.00 12.59 ?  65  SER   A H    1 
ATOM   1622 H  HA   . SER   A 1 65  ? 34.475 5.235   4.018   1.00 12.55 ?  65  SER   A HA   1 
ATOM   1623 H  HB2  . SER   A 1 65  ? 32.417 7.062   3.380   1.00 12.85 ?  65  SER   A HB2  1 
ATOM   1624 H  HB3  . SER   A 1 65  ? 32.764 5.806   2.474   1.00 12.85 ?  65  SER   A HB3  1 
ATOM   1625 H  HG   . SER   A 1 65  ? 31.900 5.640   4.968   1.00 13.24 ?  65  SER   A HG   1 
ATOM   1626 N  N    . ASP   A 1 66  ? 35.184 8.159   2.922   1.00 10.77 ?  66  ASP   A N    1 
ATOM   1627 C  CA   . ASP   A 1 66  ? 36.051 8.854   1.976   1.00 11.91 ?  66  ASP   A CA   1 
ATOM   1628 C  C    . ASP   A 1 66  ? 37.512 8.497   2.223   1.00 11.73 ?  66  ASP   A C    1 
ATOM   1629 O  O    . ASP   A 1 66  ? 38.285 8.317   1.275   1.00 12.60 ?  66  ASP   A O    1 
ATOM   1630 C  CB   . ASP   A 1 66  ? 35.832 10.361  2.075   1.00 13.04 ?  66  ASP   A CB   1 
ATOM   1631 C  CG   . ASP   A 1 66  ? 34.495 10.818  1.470   1.00 14.90 ?  66  ASP   A CG   1 
ATOM   1632 O  OD1  . ASP   A 1 66  ? 33.780 10.012  0.835   1.00 14.97 ?  66  ASP   A OD1  1 
ATOM   1633 O  OD2  . ASP   A 1 66  ? 34.194 12.020  1.609   1.00 17.43 -1 66  ASP   A OD2  1 
ATOM   1634 H  H    . ASP   A 1 66  ? 34.739 8.671   3.453   1.00 12.94 ?  66  ASP   A H    1 
ATOM   1635 H  HA   . ASP   A 1 66  ? 35.820 8.576   1.075   1.00 14.30 ?  66  ASP   A HA   1 
ATOM   1636 H  HB2  . ASP   A 1 66  ? 35.842 10.622  3.009   1.00 15.66 ?  66  ASP   A HB2  1 
ATOM   1637 H  HB3  . ASP   A 1 66  ? 36.550 10.813  1.599   1.00 15.66 ?  66  ASP   A HB3  1 
ATOM   1638 N  N    . ASP   A 1 67  ? 37.903 8.365   3.491   1.00 11.89 ?  67  ASP   A N    1 
ATOM   1639 C  CA   . ASP   A 1 67  ? 39.256 7.916   3.795   1.00 12.80 ?  67  ASP   A CA   1 
ATOM   1640 C  C    . ASP   A 1 67  ? 39.477 6.481   3.327   1.00 12.49 ?  67  ASP   A C    1 
ATOM   1641 O  O    . ASP   A 1 67  ? 40.537 6.158   2.774   1.00 13.13 ?  67  ASP   A O    1 
ATOM   1642 C  CB   . ASP   A 1 67  ? 39.525 8.055   5.291   1.00 14.15 ?  67  ASP   A CB   1 
ATOM   1643 C  CG   . ASP   A 1 67  ? 40.819 7.393   5.713   1.00 15.33 ?  67  ASP   A CG   1 
ATOM   1644 O  OD1  . ASP   A 1 67  ? 41.891 8.028   5.580   1.00 17.88 ?  67  ASP   A OD1  1 
ATOM   1645 O  OD2  . ASP   A 1 67  ? 40.765 6.229   6.173   1.00 15.14 -1 67  ASP   A OD2  1 
ATOM   1646 H  H    . ASP   A 1 67  ? 37.413 8.525   4.175   1.00 14.27 ?  67  ASP   A H    1 
ATOM   1647 H  HA   . ASP   A 1 67  ? 39.889 8.477   3.322   1.00 15.37 ?  67  ASP   A HA   1 
ATOM   1648 H  HB2  . ASP   A 1 67  ? 39.580 8.994   5.511   1.00 16.98 ?  67  ASP   A HB2  1 
ATOM   1649 H  HB3  . ASP   A 1 67  ? 38.799 7.636   5.781   1.00 16.98 ?  67  ASP   A HB3  1 
ATOM   1650 N  N    . TYR   A 1 68  ? 38.484 5.604   3.526   1.00 12.13 ?  68  TYR   A N    1 
ATOM   1651 C  CA   . TYR   A 1 68  ? 38.602 4.227   3.048   1.00 12.36 ?  68  TYR   A CA   1 
ATOM   1652 C  C    . TYR   A 1 68  ? 38.848 4.182   1.540   1.00 12.27 ?  68  TYR   A C    1 
ATOM   1653 O  O    . TYR   A 1 68  ? 39.721 3.445   1.066   1.00 12.55 ?  68  TYR   A O    1 
ATOM   1654 C  CB   . TYR   A 1 68  ? 37.349 3.411   3.423   1.00 12.55 ?  68  TYR   A CB   1 
ATOM   1655 C  CG   . TYR   A 1 68  ? 37.376 2.025   2.794   1.00 14.07 ?  68  TYR   A CG   1 
ATOM   1656 C  CD1  . TYR   A 1 68  ? 36.918 1.833   1.494   1.00 15.10 ?  68  TYR   A CD1  1 
ATOM   1657 C  CD2  . TYR   A 1 68  ? 37.907 0.935   3.465   1.00 15.50 ?  68  TYR   A CD2  1 
ATOM   1658 C  CE1  . TYR   A 1 68  ? 36.988 0.617   0.876   1.00 16.33 ?  68  TYR   A CE1  1 
ATOM   1659 C  CE2  . TYR   A 1 68  ? 37.972 -0.324  2.846   1.00 16.24 ?  68  TYR   A CE2  1 
ATOM   1660 C  CZ   . TYR   A 1 68  ? 37.514 -0.458  1.553   1.00 16.60 ?  68  TYR   A CZ   1 
ATOM   1661 O  OH   . TYR   A 1 68  ? 37.597 -1.671  0.925   1.00 17.48 ?  68  TYR   A OH   1 
ATOM   1662 H  H    . TYR   A 1 68  ? 37.741 5.779   3.929   1.00 14.56 ?  68  TYR   A H    1 
ATOM   1663 H  HA   . TYR   A 1 68  ? 39.361 3.812   3.484   1.00 14.84 ?  68  TYR   A HA   1 
ATOM   1664 H  HB2  . TYR   A 1 68  ? 37.311 3.302   4.386   1.00 15.07 ?  68  TYR   A HB2  1 
ATOM   1665 H  HB3  . TYR   A 1 68  ? 36.556 3.871   3.106   1.00 15.07 ?  68  TYR   A HB3  1 
ATOM   1666 H  HD1  . TYR   A 1 68  ? 36.578 2.563   1.024   1.00 18.12 ?  68  TYR   A HD1  1 
ATOM   1667 H  HD2  . TYR   A 1 68  ? 38.234 1.043   4.327   1.00 18.61 ?  68  TYR   A HD2  1 
ATOM   1668 H  HE1  . TYR   A 1 68  ? 36.673 0.517   0.006   1.00 19.60 ?  68  TYR   A HE1  1 
ATOM   1669 H  HE2  . TYR   A 1 68  ? 38.333 -1.052  3.290   1.00 19.49 ?  68  TYR   A HE2  1 
ATOM   1670 H  HH   . TYR   A 1 68  ? 37.923 -2.241  1.452   1.00 20.98 ?  68  TYR   A HH   1 
ATOM   1671 N  N    . ILE   A 1 69  ? 38.063 4.942   0.767   1.00 11.55 ?  69  ILE   A N    1 
ATOM   1672 C  CA   . ILE   A 1 69  ? 38.199 4.930   -0.689  1.00 11.73 ?  69  ILE   A CA   1 
ATOM   1673 C  C    . ILE   A 1 69  ? 39.532 5.534   -1.116  1.00 11.78 ?  69  ILE   A C    1 
ATOM   1674 O  O    . ILE   A 1 69  ? 40.181 5.048   -2.051  1.00 12.23 ?  69  ILE   A O    1 
ATOM   1675 C  CB   . ILE   A 1 69  ? 37.009 5.651   -1.353  1.00 12.54 ?  69  ILE   A CB   1 
ATOM   1676 C  CG1  . ILE   A 1 69  ? 35.694 4.921   -1.074  1.00 12.90 ?  69  ILE   A CG1  1 
ATOM   1677 C  CG2  . ILE   A 1 69  ? 37.251 5.826   -2.859  1.00 13.91 ?  69  ILE   A CG2  1 
ATOM   1678 C  CD1  . ILE   A 1 69  ? 35.532 3.633   -1.840  1.00 13.84 ?  69  ILE   A CD1  1 
ATOM   1679 H  H    . ILE   A 1 69  ? 37.457 5.475   1.063   1.00 13.87 ?  69  ILE   A H    1 
ATOM   1680 H  HA   . ILE   A 1 69  ? 38.190 4.011   -0.987  1.00 14.08 ?  69  ILE   A HA   1 
ATOM   1681 H  HB   . ILE   A 1 69  ? 36.944 6.536   -0.963  1.00 15.06 ?  69  ILE   A HB   1 
ATOM   1682 H  HG12 . ILE   A 1 69  ? 35.652 4.712   -0.126  1.00 15.48 ?  69  ILE   A HG12 1 
ATOM   1683 H  HG13 . ILE   A 1 69  ? 34.959 5.507   -1.310  1.00 15.48 ?  69  ILE   A HG13 1 
ATOM   1684 H  HG21 . ILE   A 1 69  ? 36.408 6.034   -3.292  1.00 16.69 ?  69  ILE   A HG21 1 
ATOM   1685 H  HG22 . ILE   A 1 69  ? 37.877 6.559   -2.997  1.00 16.69 ?  69  ILE   A HG22 1 
ATOM   1686 H  HG23 . ILE   A 1 69  ? 37.616 5.007   -3.221  1.00 16.69 ?  69  ILE   A HG23 1 
ATOM   1687 H  HD11 . ILE   A 1 69  ? 34.739 3.181   -1.520  1.00 16.61 ?  69  ILE   A HD11 1 
ATOM   1688 H  HD12 . ILE   A 1 69  ? 35.438 3.841   -2.784  1.00 16.61 ?  69  ILE   A HD12 1 
ATOM   1689 H  HD13 . ILE   A 1 69  ? 36.313 3.080   -1.697  1.00 16.61 ?  69  ILE   A HD13 1 
ATOM   1690 N  N    . ALA   A 1 70  ? 39.954 6.613   -0.460  1.00 12.31 ?  70  ALA   A N    1 
ATOM   1691 C  CA   . ALA   A 1 70  ? 41.233 7.220   -0.816  1.00 13.17 ?  70  ALA   A CA   1 
ATOM   1692 C  C    . ALA   A 1 70  ? 42.380 6.234   -0.639  1.00 13.43 ?  70  ALA   A C    1 
ATOM   1693 O  O    . ALA   A 1 70  ? 43.352 6.265   -1.398  1.00 15.40 ?  70  ALA   A O    1 
ATOM   1694 C  CB   . ALA   A 1 70  ? 41.472 8.477   0.022   1.00 13.91 ?  70  ALA   A CB   1 
ATOM   1695 H  H    . ALA   A 1 70  ? 39.528 7.005   0.174   1.00 14.78 ?  70  ALA   A H    1 
ATOM   1696 H  HA   . ALA   A 1 70  ? 41.204 7.490   -1.749  1.00 15.81 ?  70  ALA   A HA   1 
ATOM   1697 H  HB1  . ALA   A 1 70  ? 42.331 8.864   -0.230  1.00 16.70 ?  70  ALA   A HB1  1 
ATOM   1698 H  HB2  . ALA   A 1 70  ? 40.765 9.115   -0.147  1.00 16.70 ?  70  ALA   A HB2  1 
ATOM   1699 H  HB3  . ALA   A 1 70  ? 41.487 8.234   0.961   1.00 16.70 ?  70  ALA   A HB3  1 
ATOM   1700 N  N    . THR   A 1 71  ? 42.269 5.335   0.336   1.00 12.98 ?  71  THR   A N    1 
ATOM   1701 C  CA   . THR   A 1 71  ? 43.324 4.360   0.589   1.00 14.48 ?  71  THR   A CA   1 
ATOM   1702 C  C    . THR   A 1 71  ? 43.203 3.133   -0.304  1.00 14.60 ?  71  THR   A C    1 
ATOM   1703 O  O    . THR   A 1 71  ? 44.216 2.614   -0.793  1.00 16.60 ?  71  THR   A O    1 
ATOM   1704 C  CB   . THR   A 1 71  ? 43.252 3.915   2.045   1.00 16.74 ?  71  THR   A CB   1 
ATOM   1705 O  OG1  . THR   A 1 71  ? 43.483 5.041   2.893   1.00 18.11 ?  71  THR   A OG1  1 
ATOM   1706 C  CG2  . THR   A 1 71  ? 44.265 2.815   2.340   1.00 18.32 ?  71  THR   A CG2  1 
ATOM   1707 H  H    . THR   A 1 71  ? 41.591 5.265   0.855   1.00 15.58 ?  71  THR   A H    1 
ATOM   1708 H  HA   . THR   A 1 71  ? 44.187 4.766   0.425   1.00 17.38 ?  71  THR   A HA   1 
ATOM   1709 H  HB   . THR   A 1 71  ? 42.364 3.558   2.216   1.00 20.09 ?  71  THR   A HB   1 
ATOM   1710 H  HG1  . THR   A 1 71  ? 42.897 5.626   2.751   1.00 21.74 ?  71  THR   A HG1  1 
ATOM   1711 H  HG21 . THR   A 1 71  ? 44.391 2.737   3.298   1.00 21.99 ?  71  THR   A HG21 1 
ATOM   1712 H  HG22 . THR   A 1 71  ? 43.954 1.964   1.993   1.00 21.99 ?  71  THR   A HG22 1 
ATOM   1713 H  HG23 . THR   A 1 71  ? 45.118 3.031   1.929   1.00 21.99 ?  71  THR   A HG23 1 
ATOM   1714 N  N    . ASN   A 1 72  ? 41.978 2.630   -0.495  1.00 13.58 ?  72  ASN   A N    1 
ATOM   1715 C  CA   . ASN   A 1 72  ? 41.759 1.307   -1.060  1.00 13.87 ?  72  ASN   A CA   1 
ATOM   1716 C  C    . ASN   A 1 72  ? 41.141 1.298   -2.445  1.00 13.74 ?  72  ASN   A C    1 
ATOM   1717 O  O    . ASN   A 1 72  ? 41.142 0.242   -3.092  1.00 14.87 ?  72  ASN   A O    1 
ATOM   1718 C  CB   . ASN   A 1 72  ? 40.862 0.491   -0.122  1.00 14.57 ?  72  ASN   A CB   1 
ATOM   1719 C  CG   . ASN   A 1 72  ? 41.478 0.328   1.241   1.00 15.75 ?  72  ASN   A CG   1 
ATOM   1720 O  OD1  . ASN   A 1 72  ? 41.027 0.920   2.215   1.00 17.30 ?  72  ASN   A OD1  1 
ATOM   1721 N  ND2  . ASN   A 1 72  ? 42.539 -0.448  1.310   1.00 16.23 ?  72  ASN   A ND2  1 
ATOM   1722 H  H    . ASN   A 1 72  ? 41.247 3.046   -0.299  1.00 16.30 ?  72  ASN   A H    1 
ATOM   1723 H  HA   . ASN   A 1 72  ? 42.612 0.853   -1.121  1.00 16.65 ?  72  ASN   A HA   1 
ATOM   1724 H  HB2  . ASN   A 1 72  ? 40.012 0.938   -0.022  1.00 17.49 ?  72  ASN   A HB2  1 
ATOM   1725 H  HB3  . ASN   A 1 72  ? 40.733 -0.396  -0.503  1.00 17.49 ?  72  ASN   A HB3  1 
ATOM   1726 H  HD21 . ASN   A 1 72  ? 42.934 -0.567  2.065   1.00 19.48 ?  72  ASN   A HD21 1 
ATOM   1727 H  HD22 . ASN   A 1 72  ? 42.840 -0.834  0.603   1.00 19.48 ?  72  ASN   A HD22 1 
ATOM   1728 N  N    . GLY   A 1 73  ? 40.589 2.410   -2.907  1.00 13.46 ?  73  GLY   A N    1 
ATOM   1729 C  CA   . GLY   A 1 73  ? 39.860 2.417   -4.148  1.00 13.13 ?  73  GLY   A CA   1 
ATOM   1730 C  C    . GLY   A 1 73  ? 38.467 1.843   -3.976  1.00 12.56 ?  73  GLY   A C    1 
ATOM   1731 O  O    . GLY   A 1 73  ? 38.079 1.395   -2.892  1.00 13.05 ?  73  GLY   A O    1 
ATOM   1732 H  H    . GLY   A 1 73  ? 40.632 3.183   -2.521  1.00 16.16 ?  73  GLY   A H    1 
ATOM   1733 H  HA2  . GLY   A 1 73  ? 39.787 3.333   -4.475  1.00 15.76 ?  73  GLY   A HA2  1 
ATOM   1734 H  HA3  . GLY   A 1 73  ? 40.339 1.895   -4.813  1.00 15.76 ?  73  GLY   A HA3  1 
ATOM   1735 N  N    . PRO   A 1 74  ? 37.691 1.858   -5.056  1.00 13.03 ?  74  PRO   A N    1 
ATOM   1736 C  CA   . PRO   A 1 74  ? 36.293 1.432   -4.975  1.00 12.98 ?  74  PRO   A CA   1 
ATOM   1737 C  C    . PRO   A 1 74  ? 36.143 -0.049  -4.660  1.00 12.49 ?  74  PRO   A C    1 
ATOM   1738 O  O    . PRO   A 1 74  ? 37.013 -0.880  -4.939  1.00 13.55 ?  74  PRO   A O    1 
ATOM   1739 C  CB   . PRO   A 1 74  ? 35.750 1.738   -6.376  1.00 14.62 ?  74  PRO   A CB   1 
ATOM   1740 C  CG   . PRO   A 1 74  ? 36.701 2.709   -6.977  1.00 17.16 ?  74  PRO   A CG   1 
ATOM   1741 C  CD   . PRO   A 1 74  ? 38.035 2.366   -6.394  1.00 14.84 ?  74  PRO   A CD   1 
ATOM   1742 H  HA   . PRO   A 1 74  ? 35.814 1.960   -4.314  1.00 15.58 ?  74  PRO   A HA   1 
ATOM   1743 H  HB2  . PRO   A 1 74  ? 35.716 0.920   -6.894  1.00 17.55 ?  74  PRO   A HB2  1 
ATOM   1744 H  HB3  . PRO   A 1 74  ? 34.864 2.131   -6.300  1.00 17.55 ?  74  PRO   A HB3  1 
ATOM   1745 H  HG2  . PRO   A 1 74  ? 36.714 2.601   -7.941  1.00 20.59 ?  74  PRO   A HG2  1 
ATOM   1746 H  HG3  . PRO   A 1 74  ? 36.449 3.611   -6.735  1.00 20.59 ?  74  PRO   A HG3  1 
ATOM   1747 H  HD2  . PRO   A 1 74  ? 38.472 1.672   -6.921  1.00 17.82 ?  74  PRO   A HD2  1 
ATOM   1748 H  HD3  . PRO   A 1 74  ? 38.591 3.163   -6.339  1.00 17.82 ?  74  PRO   A HD3  1 
ATOM   1749 N  N    . LEU   A 1 75  ? 34.997 -0.371  -4.074  1.00 11.68 ?  75  LEU   A N    1 
ATOM   1750 C  CA   . LEU   A 1 75  ? 34.599 -1.759  -3.925  1.00 11.42 ?  75  LEU   A CA   1 
ATOM   1751 C  C    . LEU   A 1 75  ? 34.212 -2.333  -5.285  1.00 11.98 ?  75  LEU   A C    1 
ATOM   1752 O  O    . LEU   A 1 75  ? 34.087 -1.618  -6.283  1.00 13.58 ?  75  LEU   A O    1 
ATOM   1753 C  CB   . LEU   A 1 75  ? 33.408 -1.877  -2.977  1.00 11.70 ?  75  LEU   A CB   1 
ATOM   1754 C  CG   . LEU   A 1 75  ? 33.619 -1.461  -1.524  1.00 13.12 ?  75  LEU   A CG   1 
ATOM   1755 C  CD1  . LEU   A 1 75  ? 32.330 -1.662  -0.736  1.00 15.17 ?  75  LEU   A CD1  1 
ATOM   1756 C  CD2  . LEU   A 1 75  ? 34.766 -2.174  -0.856  1.00 16.25 ?  75  LEU   A CD2  1 
ATOM   1757 H  H    . LEU   A 1 75  ? 34.436 0.198   -3.753  1.00 14.02 ?  75  LEU   A H    1 
ATOM   1758 H  HA   . LEU   A 1 75  ? 35.337 -2.274  -3.571  1.00 13.71 ?  75  LEU   A HA   1 
ATOM   1759 H  HB2  . LEU   A 1 75  ? 32.688 -1.333  -3.326  1.00 14.04 ?  75  LEU   A HB2  1 
ATOM   1760 H  HB3  . LEU   A 1 75  ? 33.127 -2.808  -2.968  1.00 14.04 ?  75  LEU   A HB3  1 
ATOM   1761 H  HG   . LEU   A 1 75  ? 33.831 -0.515  -1.508  1.00 15.75 ?  75  LEU   A HG   1 
ATOM   1762 H  HD11 . LEU   A 1 75  ? 32.480 -1.391  0.183   1.00 18.20 ?  75  LEU   A HD11 1 
ATOM   1763 H  HD12 . LEU   A 1 75  ? 31.638 -1.113  -1.135  1.00 18.20 ?  75  LEU   A HD12 1 
ATOM   1764 H  HD13 . LEU   A 1 75  ? 32.082 -2.595  -0.774  1.00 18.20 ?  75  LEU   A HD13 1 
ATOM   1765 H  HD21 . LEU   A 1 75  ? 34.818 -1.893  0.072   1.00 19.50 ?  75  LEU   A HD21 1 
ATOM   1766 H  HD22 . LEU   A 1 75  ? 34.622 -3.130  -0.905  1.00 19.50 ?  75  LEU   A HD22 1 
ATOM   1767 H  HD23 . LEU   A 1 75  ? 35.597 -1.943  -1.311  1.00 19.50 ?  75  LEU   A HD23 1 
ATOM   1768 N  N    . LYS   A 1 76  ? 34.031 -3.652  -5.309  1.00 12.21 ?  76  LYS   A N    1 
ATOM   1769 C  CA   . LYS   A 1 76  ? 33.435 -4.367  -6.433  1.00 12.83 ?  76  LYS   A CA   1 
ATOM   1770 C  C    . LYS   A 1 76  ? 31.923 -4.450  -6.240  1.00 11.56 ?  76  LYS   A C    1 
ATOM   1771 O  O    . LYS   A 1 76  ? 31.442 -4.572  -5.117  1.00 11.62 ?  76  LYS   A O    1 
ATOM   1772 C  CB   . LYS   A 1 76  ? 33.975 -5.806  -6.489  1.00 14.45 ?  76  LYS   A CB   1 
ATOM   1773 C  CG   . LYS   A 1 76  ? 35.485 -5.919  -6.682  1.00 15.87 ?  76  LYS   A CG   1 
ATOM   1774 C  CD   . LYS   A 1 76  ? 36.003 -7.322  -6.456  1.00 17.22 ?  76  LYS   A CD   1 
ATOM   1775 C  CE   . LYS   A 1 76  ? 37.503 -7.379  -6.660  1.00 19.79 ?  76  LYS   A CE   1 
ATOM   1776 N  NZ   . LYS   A 1 76  ? 38.037 -8.741  -6.469  1.00 20.52 ?  76  LYS   A NZ   1 
ATOM   1777 H  H    . LYS   A 1 76  ? 34.260 -4.174  -4.662  1.00 14.66 ?  76  LYS   A H    1 
ATOM   1778 H  HA   . LYS   A 1 76  ? 33.633 -3.914  -7.268  1.00 15.40 ?  76  LYS   A HA   1 
ATOM   1779 H  HB2  . LYS   A 1 76  ? 33.750 -6.250  -5.657  1.00 17.35 ?  76  LYS   A HB2  1 
ATOM   1780 H  HB3  . LYS   A 1 76  ? 33.548 -6.264  -7.229  1.00 17.35 ?  76  LYS   A HB3  1 
ATOM   1781 H  HG2  . LYS   A 1 76  ? 35.707 -5.659  -7.590  1.00 19.05 ?  76  LYS   A HG2  1 
ATOM   1782 H  HG3  . LYS   A 1 76  ? 35.929 -5.331  -6.051  1.00 19.05 ?  76  LYS   A HG3  1 
ATOM   1783 H  HD2  . LYS   A 1 76  ? 35.802 -7.599  -5.548  1.00 20.67 ?  76  LYS   A HD2  1 
ATOM   1784 H  HD3  . LYS   A 1 76  ? 35.582 -7.927  -7.092  1.00 20.67 ?  76  LYS   A HD3  1 
ATOM   1785 H  HE2  . LYS   A 1 76  ? 37.712 -7.095  -7.562  1.00 23.75 ?  76  LYS   A HE2  1 
ATOM   1786 H  HE3  . LYS   A 1 76  ? 37.931 -6.795  -6.015  1.00 23.75 ?  76  LYS   A HE3  1 
ATOM   1787 H  HZ1  . LYS   A 1 76  ? 38.918 -8.749  -6.595  1.00 24.63 ?  76  LYS   A HZ1  1 
ATOM   1788 H  HZ2  . LYS   A 1 76  ? 37.861 -9.032  -5.645  1.00 24.63 ?  76  LYS   A HZ2  1 
ATOM   1789 H  HZ3  . LYS   A 1 76  ? 37.661 -9.305  -7.054  1.00 24.63 ?  76  LYS   A HZ3  1 
ATOM   1790 N  N    . VAL   A 1 77  ? 31.171 -4.420  -7.345  1.00 12.06 ?  77  VAL   A N    1 
ATOM   1791 C  CA   . VAL   A 1 77  ? 29.763 -4.805  -7.260  1.00 11.85 ?  77  VAL   A CA   1 
ATOM   1792 C  C    . VAL   A 1 77  ? 29.698 -6.259  -6.816  1.00 11.58 ?  77  VAL   A C    1 
ATOM   1793 O  O    . VAL   A 1 77  ? 30.358 -7.130  -7.395  1.00 12.05 ?  77  VAL   A O    1 
ATOM   1794 C  CB   . VAL   A 1 77  ? 29.039 -4.591  -8.597  1.00 12.89 ?  77  VAL   A CB   1 
ATOM   1795 C  CG1  . VAL   A 1 77  ? 27.582 -5.029  -8.480  1.00 13.76 ?  77  VAL   A CG1  1 
ATOM   1796 C  CG2  . VAL   A 1 77  ? 29.121 -3.136  -9.027  1.00 14.44 ?  77  VAL   A CG2  1 
ATOM   1797 H  H    . VAL   A 1 77  ? 31.448 -4.176  -8.123  1.00 14.48 ?  77  VAL   A H    1 
ATOM   1798 H  HA   . VAL   A 1 77  ? 29.327 -4.261  -6.588  1.00 14.22 ?  77  VAL   A HA   1 
ATOM   1799 H  HB   . VAL   A 1 77  ? 29.467 -5.128  -9.281  1.00 15.47 ?  77  VAL   A HB   1 
ATOM   1800 H  HG11 . VAL   A 1 77  ? 27.099 -4.716  -9.258  1.00 16.52 ?  77  VAL   A HG11 1 
ATOM   1801 H  HG12 . VAL   A 1 77  ? 27.547 -5.996  -8.433  1.00 16.52 ?  77  VAL   A HG12 1 
ATOM   1802 H  HG13 . VAL   A 1 77  ? 27.203 -4.641  -7.676  1.00 16.52 ?  77  VAL   A HG13 1 
ATOM   1803 H  HG21 . VAL   A 1 77  ? 28.615 -3.023  -9.846  1.00 17.33 ?  77  VAL   A HG21 1 
ATOM   1804 H  HG22 . VAL   A 1 77  ? 28.744 -2.581  -8.326  1.00 17.33 ?  77  VAL   A HG22 1 
ATOM   1805 H  HG23 . VAL   A 1 77  ? 30.049 -2.900  -9.174  1.00 17.33 ?  77  VAL   A HG23 1 
ATOM   1806 N  N    . GLY   A 1 78  ? 28.914 -6.526  -5.770  1.00 11.32 ?  78  GLY   A N    1 
ATOM   1807 C  CA   . GLY   A 1 78  ? 28.895 -7.815  -5.115  1.00 11.34 ?  78  GLY   A CA   1 
ATOM   1808 C  C    . GLY   A 1 78  ? 29.806 -7.903  -3.911  1.00 11.16 ?  78  GLY   A C    1 
ATOM   1809 O  O    . GLY   A 1 78  ? 29.750 -8.909  -3.183  1.00 11.68 ?  78  GLY   A O    1 
ATOM   1810 H  H    . GLY   A 1 78  ? 28.372 -5.951  -5.424  1.00 13.59 ?  78  GLY   A H    1 
ATOM   1811 H  HA2  . GLY   A 1 78  ? 27.991 -8.005  -4.829  1.00 13.61 ?  78  GLY   A HA2  1 
ATOM   1812 H  HA3  . GLY   A 1 78  ? 29.162 -8.494  -5.754  1.00 13.61 ?  78  GLY   A HA3  1 
ATOM   1813 N  N    . GLY   A 1 79  ? 30.663 -6.902  -3.695  1.00 11.00 ?  79  GLY   A N    1 
ATOM   1814 C  CA   . GLY   A 1 79  ? 31.624 -6.918  -2.617  1.00 11.47 ?  79  GLY   A CA   1 
ATOM   1815 C  C    . GLY   A 1 79  ? 31.178 -6.117  -1.404  1.00 10.73 ?  79  GLY   A C    1 
ATOM   1816 O  O    . GLY   A 1 79  ? 30.064 -5.604  -1.326  1.00 11.41 ?  79  GLY   A O    1 
ATOM   1817 H  H    . GLY   A 1 79  ? 30.706 -6.192  -4.180  1.00 13.20 ?  79  GLY   A H    1 
ATOM   1818 H  HA2  . GLY   A 1 79  ? 31.776 -7.844  -2.342  1.00 13.77 ?  79  GLY   A HA2  1 
ATOM   1819 H  HA3  . GLY   A 1 79  ? 32.467 -6.561  -2.933  1.00 13.77 ?  79  GLY   A HA3  1 
ATOM   1820 N  N    . SER   A 1 80  ? 32.083 -6.028  -0.434  1.00 11.63 ?  80  SER   A N    1 
ATOM   1821 C  CA   . SER   A 1 80  ? 31.762 -5.399  0.834   1.00 11.08 ?  80  SER   A CA   1 
ATOM   1822 C  C    . SER   A 1 80  ? 33.033 -4.951  1.536   1.00 11.10 ?  80  SER   A C    1 
ATOM   1823 O  O    . SER   A 1 80  ? 34.145 -5.385  1.208   1.00 12.48 ?  80  SER   A O    1 
ATOM   1824 C  CB   . SER   A 1 80  ? 30.996 -6.360  1.755   1.00 12.13 ?  80  SER   A CB   1 
ATOM   1825 O  OG   . SER   A 1 80  ? 31.827 -7.406  2.235   1.00 13.64 ?  80  SER   A OG   1 
ATOM   1826 H  H    . SER   A 1 80  ? 32.891 -6.314  -0.494  1.00 13.96 ?  80  SER   A H    1 
ATOM   1827 H  HA   . SER   A 1 80  ? 31.210 -4.615  0.654   1.00 13.30 ?  80  SER   A HA   1 
ATOM   1828 H  HB2  . SER   A 1 80  ? 30.653 -5.855  2.508   1.00 14.56 ?  80  SER   A HB2  1 
ATOM   1829 H  HB3  . SER   A 1 80  ? 30.258 -6.743  1.253   1.00 14.56 ?  80  SER   A HB3  1 
ATOM   1830 H  HG   . SER   A 1 80  ? 32.128 -7.844  1.582   1.00 16.37 ?  80  SER   A HG   1 
ATOM   1831 N  N    . CYS   A 1 81  ? 32.840 -4.098  2.537   1.00 10.85 ?  81  CYS   A N    1 
ATOM   1832 C  CA   . CYS   A 1 81  ? 33.889 -3.815  3.502   1.00 11.10 ?  81  CYS   A CA   1 
ATOM   1833 C  C    . CYS   A 1 81  ? 33.244 -3.582  4.860   1.00 10.82 ?  81  CYS   A C    1 
ATOM   1834 O  O    . CYS   A 1 81  ? 32.077 -3.187  4.950   1.00 11.96 ?  81  CYS   A O    1 
ATOM   1835 C  CB   . CYS   A 1 81  ? 34.765 -2.624  3.089   1.00 11.65 ?  81  CYS   A CB   1 
ATOM   1836 S  SG   . CYS   A 1 81  ? 33.867 -1.051  3.103   1.00 11.62 ?  81  CYS   A SG   1 
ATOM   1837 H  H    . CYS   A 1 81  ? 32.103 -3.674  2.682   1.00 13.03 ?  81  CYS   A H    1 
ATOM   1838 H  HA   . CYS   A 1 81  ? 34.464 -4.592  3.572   1.00 13.32 ?  81  CYS   A HA   1 
ATOM   1839 H  HB2  . CYS   A 1 81  ? 35.514 -2.554  3.706   1.00 13.99 ?  81  CYS   A HB2  1 
ATOM   1840 H  HB3  . CYS   A 1 81  ? 35.102 -2.776  2.187   1.00 13.99 ?  81  CYS   A HB3  1 
ATOM   1841 H  HG   . CYS   A 1 81  ? 34.614 -0.172  2.772   1.00 13.95 ?  81  CYS   A HG   1 
ATOM   1842 N  N    . VAL   A 1 82  ? 34.012 -3.841  5.916   1.00 11.18 ?  82  VAL   A N    1 
ATOM   1843 C  CA   . VAL   A 1 82  ? 33.582 -3.597  7.286   1.00 11.57 ?  82  VAL   A CA   1 
ATOM   1844 C  C    . VAL   A 1 82  ? 34.179 -2.282  7.754   1.00 11.80 ?  82  VAL   A C    1 
ATOM   1845 O  O    . VAL   A 1 82  ? 35.404 -2.111  7.740   1.00 12.47 ?  82  VAL   A O    1 
ATOM   1846 C  CB   . VAL   A 1 82  ? 34.007 -4.732  8.228   1.00 13.34 ?  82  VAL   A CB   1 
ATOM   1847 C  CG1  . VAL   A 1 82  ? 33.559 -4.425  9.649   1.00 14.51 ?  82  VAL   A CG1  1 
ATOM   1848 C  CG2  . VAL   A 1 82  ? 33.453 -6.064  7.759   1.00 14.53 ?  82  VAL   A CG2  1 
ATOM   1849 H  H    . VAL   A 1 82  ? 34.810 -4.173  5.858   1.00 13.42 ?  82  VAL   A H    1 
ATOM   1850 H  HA   . VAL   A 1 82  ? 32.616 -3.516  7.306   1.00 13.89 ?  82  VAL   A HA   1 
ATOM   1851 H  HB   . VAL   A 1 82  ? 34.974 -4.787  8.226   1.00 16.01 ?  82  VAL   A HB   1 
ATOM   1852 H  HG11 . VAL   A 1 82  ? 33.643 -5.230  10.182  1.00 17.41 ?  82  VAL   A HG11 1 
ATOM   1853 H  HG12 . VAL   A 1 82  ? 34.121 -3.725  10.020  1.00 17.41 ?  82  VAL   A HG12 1 
ATOM   1854 H  HG13 . VAL   A 1 82  ? 32.633 -4.134  9.635   1.00 17.41 ?  82  VAL   A HG13 1 
ATOM   1855 H  HG21 . VAL   A 1 82  ? 33.707 -6.749  8.397   1.00 17.44 ?  82  VAL   A HG21 1 
ATOM   1856 H  HG22 . VAL   A 1 82  ? 32.487 -6.003  7.704   1.00 17.44 ?  82  VAL   A HG22 1 
ATOM   1857 H  HG23 . VAL   A 1 82  ? 33.823 -6.270  6.886   1.00 17.44 ?  82  VAL   A HG23 1 
ATOM   1858 N  N    . LEU   A 1 83  ? 33.325 -1.361  8.178   1.00 11.27 ?  83  LEU   A N    1 
ATOM   1859 C  CA   . LEU   A 1 83  ? 33.741 -0.094  8.754   1.00 11.15 ?  83  LEU   A CA   1 
ATOM   1860 C  C    . LEU   A 1 83  ? 33.016 0.088   10.081  1.00 11.42 ?  83  LEU   A C    1 
ATOM   1861 O  O    . LEU   A 1 83  ? 32.291 -0.802  10.544  1.00 12.02 ?  83  LEU   A O    1 
ATOM   1862 C  CB   . LEU   A 1 83  ? 33.491 1.059   7.774   1.00 11.70 ?  83  LEU   A CB   1 
ATOM   1863 C  CG   . LEU   A 1 83  ? 34.399 1.054   6.541   1.00 12.23 ?  83  LEU   A CG   1 
ATOM   1864 C  CD1  . LEU   A 1 83  ? 33.971 2.097   5.530   1.00 12.98 ?  83  LEU   A CD1  1 
ATOM   1865 C  CD2  . LEU   A 1 83  ? 35.867 1.274   6.944   1.00 13.10 ?  83  LEU   A CD2  1 
ATOM   1866 H  H    . LEU   A 1 83  ? 32.470 -1.450  8.134   1.00 13.53 ?  83  LEU   A H    1 
ATOM   1867 H  HA   . LEU   A 1 83  ? 34.690 -0.121  8.934   1.00 13.38 ?  83  LEU   A HA   1 
ATOM   1868 H  HB2  . LEU   A 1 83  ? 32.575 1.014   7.452   1.00 14.04 ?  83  LEU   A HB2  1 
ATOM   1869 H  HB3  . LEU   A 1 83  ? 33.630 1.905   8.230   1.00 14.04 ?  83  LEU   A HB3  1 
ATOM   1870 H  HG   . LEU   A 1 83  ? 34.344 0.186   6.115   1.00 14.68 ?  83  LEU   A HG   1 
ATOM   1871 H  HD11 . LEU   A 1 83  ? 34.571 2.057   4.765   1.00 15.58 ?  83  LEU   A HD11 1 
ATOM   1872 H  HD12 . LEU   A 1 83  ? 33.066 1.906   5.249   1.00 15.58 ?  83  LEU   A HD12 1 
ATOM   1873 H  HD13 . LEU   A 1 83  ? 34.019 2.972   5.940   1.00 15.58 ?  83  LEU   A HD13 1 
ATOM   1874 H  HD21 . LEU   A 1 83  ? 36.397 1.446   6.147   1.00 15.73 ?  83  LEU   A HD21 1 
ATOM   1875 H  HD22 . LEU   A 1 83  ? 35.924 2.038   7.543   1.00 15.73 ?  83  LEU   A HD22 1 
ATOM   1876 H  HD23 . LEU   A 1 83  ? 36.202 0.481   7.393   1.00 15.73 ?  83  LEU   A HD23 1 
ATOM   1877 N  N    . SER   A 1 84  ? 33.231 1.239   10.710  1.00 11.91 ?  84  SER   A N    1 
ATOM   1878 C  CA   . SER   A 1 84  ? 32.586 1.498   11.986  1.00 12.01 ?  84  SER   A CA   1 
ATOM   1879 C  C    . SER   A 1 84  ? 31.069 1.581   11.835  1.00 12.00 ?  84  SER   A C    1 
ATOM   1880 O  O    . SER   A 1 84  ? 30.545 2.044   10.822  1.00 12.11 ?  84  SER   A O    1 
ATOM   1881 C  CB   . SER   A 1 84  ? 33.079 2.824   12.550  1.00 13.22 ?  84  SER   A CB   1 
ATOM   1882 O  OG   . SER   A 1 84  ? 32.452 3.101   13.785  1.00 14.13 ?  84  SER   A OG   1 
ATOM   1883 H  H    . SER   A 1 84  ? 33.741 1.878   10.420  1.00 14.30 ?  84  SER   A H    1 
ATOM   1884 H  HA   . SER   A 1 84  ? 32.810 0.792   12.609  1.00 14.41 ?  84  SER   A HA   1 
ATOM   1885 H  HB2  . SER   A 1 84  ? 34.040 2.779   12.683  1.00 15.87 ?  84  SER   A HB2  1 
ATOM   1886 H  HB3  . SER   A 1 84  ? 32.869 3.536   11.919  1.00 15.87 ?  84  SER   A HB3  1 
ATOM   1887 H  HG   . SER   A 1 84  ? 32.729 3.836   14.087  1.00 16.96 ?  84  SER   A HG   1 
ATOM   1888 N  N    . GLY   A 1 85  ? 30.359 1.167   12.880  1.00 12.99 ?  85  GLY   A N    1 
ATOM   1889 C  CA   . GLY   A 1 85  ? 28.936 1.406   12.967  1.00 13.29 ?  85  GLY   A CA   1 
ATOM   1890 C  C    . GLY   A 1 85  ? 28.570 2.727   13.605  1.00 12.86 ?  85  GLY   A C    1 
ATOM   1891 O  O    . GLY   A 1 85  ? 27.379 3.045   13.711  1.00 13.62 ?  85  GLY   A O    1 
ATOM   1892 H  H    . GLY   A 1 85  ? 30.689 0.741   13.555  1.00 15.59 ?  85  GLY   A H    1 
ATOM   1893 H  HA2  . GLY   A 1 85  ? 28.562 1.383   12.071  1.00 15.95 ?  85  GLY   A HA2  1 
ATOM   1894 H  HA3  . GLY   A 1 85  ? 28.528 0.697   13.482  1.00 15.95 ?  85  GLY   A HA3  1 
ATOM   1895 N  N    . HIS   A 1 86  ? 29.558 3.503   14.042  1.00 12.72 ?  86  HIS   A N    1 
ATOM   1896 C  CA   . HIS   A 1 86  ? 29.332 4.836   14.609  1.00 13.10 ?  86  HIS   A CA   1 
ATOM   1897 C  C    . HIS   A 1 86  ? 28.343 4.719   15.762  1.00 13.93 ?  86  HIS   A C    1 
ATOM   1898 O  O    . HIS   A 1 86  ? 28.519 3.841   16.623  1.00 15.33 ?  86  HIS   A O    1 
ATOM   1899 C  CB   . HIS   A 1 86  ? 28.960 5.811   13.503  1.00 13.14 ?  86  HIS   A CB   1 
ATOM   1900 C  CG   . HIS   A 1 86  ? 30.019 5.910   12.467  1.00 13.12 ?  86  HIS   A CG   1 
ATOM   1901 N  ND1  . HIS   A 1 86  ? 31.109 6.744   12.598  1.00 14.13 ?  86  HIS   A ND1  1 
ATOM   1902 C  CD2  . HIS   A 1 86  ? 30.202 5.218   11.320  1.00 12.72 ?  86  HIS   A CD2  1 
ATOM   1903 C  CE1  . HIS   A 1 86  ? 31.903 6.577   11.556  1.00 13.95 ?  86  HIS   A CE1  1 
ATOM   1904 N  NE2  . HIS   A 1 86  ? 31.384 5.648   10.775  1.00 13.30 ?  86  HIS   A NE2  1 
ATOM   1905 H  H    . HIS   A 1 86  ? 30.380 3.278   14.031  1.00 15.27 ?  86  HIS   A H    1 
ATOM   1906 H  HA   . HIS   A 1 86  ? 30.168 5.149   14.984  1.00 15.73 ?  86  HIS   A HA   1 
ATOM   1907 H  HB2  . HIS   A 1 86  ? 28.140 5.520   13.072  1.00 15.77 ?  86  HIS   A HB2  1 
ATOM   1908 H  HB3  . HIS   A 1 86  ? 28.833 6.701   13.881  1.00 15.77 ?  86  HIS   A HB3  1 
ATOM   1909 H  HD2  . HIS   A 1 86  ? 29.639 4.556   10.971  1.00 15.27 ?  86  HIS   A HD2  1 
ATOM   1910 H  HE1  . HIS   A 1 86  ? 32.695 7.033   11.388  1.00 16.74 ?  86  HIS   A HE1  1 
ATOM   1911 H  HE2  . HIS   A 1 86  ? 31.717 5.370   10.023  1.00 15.96 ?  86  HIS   A HE2  1 
ATOM   1912 N  N    . ASN   A 1 87  ? 27.334 5.575   15.830  1.00 15.18 ?  87  ASN   A N    1 
ATOM   1913 C  CA   . ASN   A 1 87  ? 26.352 5.567   16.897  1.00 16.03 ?  87  ASN   A CA   1 
ATOM   1914 C  C    . ASN   A 1 87  ? 25.231 4.571   16.661  1.00 17.20 ?  87  ASN   A C    1 
ATOM   1915 O  O    . ASN   A 1 87  ? 24.311 4.507   17.478  1.00 19.29 ?  87  ASN   A O    1 
ATOM   1916 C  CB   . ASN   A 1 87  ? 25.752 6.971   17.052  1.00 16.60 ?  87  ASN   A CB   1 
ATOM   1917 C  CG   . ASN   A 1 87  ? 25.251 7.549   15.732  1.00 17.55 ?  87  ASN   A CG   1 
ATOM   1918 O  OD1  . ASN   A 1 87  ? 25.895 7.418   14.695  1.00 18.06 ?  87  ASN   A OD1  1 
ATOM   1919 N  ND2  . ASN   A 1 87  ? 24.100 8.195   15.773  1.00 18.70 ?  87  ASN   A ND2  1 
ATOM   1920 H  H    . ASN   A 1 87  ? 27.189 6.189   15.250  1.00 18.22 ?  87  ASN   A H    1 
ATOM   1921 H  HA   . ASN   A 1 87  ? 26.780 5.329   17.737  1.00 19.24 ?  87  ASN   A HA   1 
ATOM   1922 H  HB2  . ASN   A 1 87  ? 24.999 6.928   17.671  1.00 19.93 ?  87  ASN   A HB2  1 
ATOM   1923 H  HB3  . ASN   A 1 87  ? 26.431 7.564   17.403  1.00 19.93 ?  87  ASN   A HB3  1 
ATOM   1924 H  HD21 . ASN   A 1 87  ? 23.777 8.532   15.052  1.00 22.45 ?  87  ASN   A HD21 1 
ATOM   1925 H  HD22 . ASN   A 1 87  ? 23.678 8.277   16.517  1.00 22.45 ?  87  ASN   A HD22 1 
ATOM   1926 N  N    . LEU   A 1 88  ? 25.285 3.793   15.584  1.00 15.90 ?  88  LEU   A N    1 
ATOM   1927 C  CA   . LEU   A 1 88  ? 24.174 2.937   15.188  1.00 15.63 ?  88  LEU   A CA   1 
ATOM   1928 C  C    . LEU   A 1 88  ? 24.381 1.459   15.478  1.00 15.42 ?  88  LEU   A C    1 
ATOM   1929 O  O    . LEU   A 1 88  ? 23.397 0.734   15.642  1.00 16.56 ?  88  LEU   A O    1 
ATOM   1930 C  CB   . LEU   A 1 88  ? 23.914 3.099   13.689  1.00 15.79 ?  88  LEU   A CB   1 
ATOM   1931 C  CG   . LEU   A 1 88  ? 23.607 4.520   13.214  1.00 17.42 ?  88  LEU   A CG   1 
ATOM   1932 C  CD1  . LEU   A 1 88  ? 23.456 4.533   11.703  1.00 18.07 ?  88  LEU   A CD1  1 
ATOM   1933 C  CD2  . LEU   A 1 88  ? 22.354 5.075   13.887  1.00 19.19 ?  88  LEU   A CD2  1 
ATOM   1934 H  H    . LEU   A 1 88  ? 25.970 3.741   15.067  1.00 19.08 ?  88  LEU   A H    1 
ATOM   1935 H  HA   . LEU   A 1 88  ? 23.379 3.222   15.660  1.00 18.76 ?  88  LEU   A HA   1 
ATOM   1936 H  HB2  . LEU   A 1 88  ? 24.697 2.801   13.205  1.00 18.95 ?  88  LEU   A HB2  1 
ATOM   1937 H  HB3  . LEU   A 1 88  ? 23.153 2.548   13.450  1.00 18.95 ?  88  LEU   A HB3  1 
ATOM   1938 H  HG   . LEU   A 1 88  ? 24.348 5.101   13.443  1.00 20.91 ?  88  LEU   A HG   1 
ATOM   1939 H  HD11 . LEU   A 1 88  ? 23.275 5.441   11.409  1.00 21.68 ?  88  LEU   A HD11 1 
ATOM   1940 H  HD12 . LEU   A 1 88  ? 24.279 4.214   11.301  1.00 21.68 ?  88  LEU   A HD12 1 
ATOM   1941 H  HD13 . LEU   A 1 88  ? 22.719 3.953   11.454  1.00 21.68 ?  88  LEU   A HD13 1 
ATOM   1942 H  HD21 . LEU   A 1 88  ? 22.134 5.932   13.488  1.00 23.04 ?  88  LEU   A HD21 1 
ATOM   1943 H  HD22 . LEU   A 1 88  ? 21.624 4.451   13.755  1.00 23.04 ?  88  LEU   A HD22 1 
ATOM   1944 H  HD23 . LEU   A 1 88  ? 22.529 5.186   14.834  1.00 23.04 ?  88  LEU   A HD23 1 
ATOM   1945 N  N    . ALA   A 1 89  ? 25.627 1.001   15.528  1.00 14.57 ?  89  ALA   A N    1 
ATOM   1946 C  CA   . ALA   A 1 89  ? 25.961 -0.411  15.631  1.00 14.32 ?  89  ALA   A CA   1 
ATOM   1947 C  C    . ALA   A 1 89  ? 27.442 -0.481  15.961  1.00 14.91 ?  89  ALA   A C    1 
ATOM   1948 O  O    . ALA   A 1 89  ? 28.160 0.514   15.850  1.00 15.50 ?  89  ALA   A O    1 
ATOM   1949 C  CB   . ALA   A 1 89  ? 25.685 -1.125  14.308  1.00 13.87 ?  89  ALA   A CB   1 
ATOM   1950 H  H    . ALA   A 1 89  ? 26.319 1.512   15.495  1.00 17.49 ?  89  ALA   A H    1 
ATOM   1951 H  HA   . ALA   A 1 89  ? 25.448 -0.826  16.344  1.00 17.19 ?  89  ALA   A HA   1 
ATOM   1952 H  HB1  . ALA   A 1 89  ? 25.924 -2.061  14.399  1.00 16.65 ?  89  ALA   A HB1  1 
ATOM   1953 H  HB2  . ALA   A 1 89  ? 24.737 -1.049  14.097  1.00 16.65 ?  89  ALA   A HB2  1 
ATOM   1954 H  HB3  . ALA   A 1 89  ? 26.212 -0.714  13.609  1.00 16.65 ?  89  ALA   A HB3  1 
ATOM   1955 N  N    . LYS   A 1 90  ? 27.912 -1.661  16.353  1.00 15.54 ?  90  LYS   A N    1 
ATOM   1956 C  CA   . LYS   A 1 90  ? 29.356 -1.813  16.509  1.00 16.41 ?  90  LYS   A CA   1 
ATOM   1957 C  C    . LYS   A 1 90  ? 30.065 -1.630  15.168  1.00 15.06 ?  90  LYS   A C    1 
ATOM   1958 O  O    . LYS   A 1 90  ? 31.007 -0.826  15.046  1.00 16.19 ?  90  LYS   A O    1 
ATOM   1959 C  CB   . LYS   A 1 90  ? 29.687 -3.168  17.137  1.00 19.31 ?  90  LYS   A CB   1 
ATOM   1960 C  CG   . LYS   A 1 90  ? 31.167 -3.328  17.460  1.00 24.60 ?  90  LYS   A CG   1 
ATOM   1961 C  CD   . LYS   A 1 90  ? 31.408 -4.524  18.368  1.00 30.32 ?  90  LYS   A CD   1 
ATOM   1962 C  CE   . LYS   A 1 90  ? 32.824 -4.538  18.925  1.00 34.66 ?  90  LYS   A CE   1 
ATOM   1963 N  NZ   . LYS   A 1 90  ? 33.835 -4.956  17.916  1.00 37.13 ?  90  LYS   A NZ   1 
ATOM   1964 H  H    . LYS   A 1 90  ? 27.435 -2.352  16.537  1.00 18.66 ?  90  LYS   A H    1 
ATOM   1965 H  HA   . LYS   A 1 90  ? 29.675 -1.124  17.107  1.00 19.69 ?  90  LYS   A HA   1 
ATOM   1966 H  HB2  . LYS   A 1 90  ? 29.187 -3.262  17.967  1.00 23.18 ?  90  LYS   A HB2  1 
ATOM   1967 H  HB3  . LYS   A 1 90  ? 29.435 -3.874  16.522  1.00 23.18 ?  90  LYS   A HB3  1 
ATOM   1968 H  HG2  . LYS   A 1 90  ? 31.663 -3.463  16.637  1.00 29.53 ?  90  LYS   A HG2  1 
ATOM   1969 H  HG3  . LYS   A 1 90  ? 31.484 -2.531  17.915  1.00 29.53 ?  90  LYS   A HG3  1 
ATOM   1970 H  HD2  . LYS   A 1 90  ? 30.789 -4.488  19.116  1.00 36.39 ?  90  LYS   A HD2  1 
ATOM   1971 H  HD3  . LYS   A 1 90  ? 31.272 -5.342  17.863  1.00 36.39 ?  90  LYS   A HD3  1 
ATOM   1972 H  HE2  . LYS   A 1 90  ? 33.055 -3.645  19.227  1.00 41.59 ?  90  LYS   A HE2  1 
ATOM   1973 H  HE3  . LYS   A 1 90  ? 32.867 -5.160  19.668  1.00 41.59 ?  90  LYS   A HE3  1 
ATOM   1974 H  HZ1  . LYS   A 1 90  ? 34.646 -4.967  18.283  1.00 44.56 ?  90  LYS   A HZ1  1 
ATOM   1975 H  HZ2  . LYS   A 1 90  ? 33.644 -5.772  17.615  1.00 44.56 ?  90  LYS   A HZ2  1 
ATOM   1976 H  HZ3  . LYS   A 1 90  ? 33.835 -4.388  17.232  1.00 44.56 ?  90  LYS   A HZ3  1 
ATOM   1977 N  N    . HIS   A 1 91  ? 29.595 -2.344  14.143  1.00 13.34 ?  91  HIS   A N    1 
ATOM   1978 C  CA   . HIS   A 1 91  ? 30.180 -2.331  12.817  1.00 12.82 ?  91  HIS   A CA   1 
ATOM   1979 C  C    . HIS   A 1 91  ? 29.103 -2.055  11.784  1.00 11.77 ?  91  HIS   A C    1 
ATOM   1980 O  O    . HIS   A 1 91  ? 27.936 -2.406  11.974  1.00 12.48 ?  91  HIS   A O    1 
ATOM   1981 C  CB   . HIS   A 1 91  ? 30.778 -3.696  12.461  1.00 15.07 ?  91  HIS   A CB   1 
ATOM   1982 C  CG   . HIS   A 1 91  ? 31.753 -4.214  13.467  1.00 19.24 ?  91  HIS   A CG   1 
ATOM   1983 N  ND1  . HIS   A 1 91  ? 33.043 -3.740  13.566  1.00 21.31 ?  91  HIS   A ND1  1 
ATOM   1984 C  CD2  . HIS   A 1 91  ? 31.633 -5.175  14.412  1.00 20.92 ?  91  HIS   A CD2  1 
ATOM   1985 C  CE1  . HIS   A 1 91  ? 33.676 -4.384  14.531  1.00 22.15 ?  91  HIS   A CE1  1 
ATOM   1986 N  NE2  . HIS   A 1 91  ? 32.842 -5.263  15.059  1.00 22.24 ?  91  HIS   A NE2  1 
ATOM   1987 H  H    . HIS   A 1 91  ? 28.906 -2.874  14.205  1.00 16.01 ?  91  HIS   A H    1 
ATOM   1988 H  HA   . HIS   A 1 91  ? 30.868 -1.656  12.761  1.00 15.39 ?  91  HIS   A HA   1 
ATOM   1989 H  HB2  . HIS   A 1 91  ? 30.062 -4.347  12.390  1.00 18.09 ?  91  HIS   A HB2  1 
ATOM   1990 H  HB3  . HIS   A 1 91  ? 31.241 -3.624  11.613  1.00 18.09 ?  91  HIS   A HB3  1 
ATOM   1991 H  HD1  . HIS   A 1 91  ? 33.387 -3.121  13.072  1.00 25.58 ?  91  HIS   A HD1  1 
ATOM   1992 H  HD2  . HIS   A 1 91  ? 30.882 -5.683  14.594  1.00 25.11 ?  91  HIS   A HD2  1 
ATOM   1993 H  HE1  . HIS   A 1 91  ? 34.562 -4.239  14.792  1.00 26.58 ?  91  HIS   A HE1  1 
ATOM   1994 N  N    . CYS   A 1 92  ? 29.513 -1.460  10.671  1.00 11.40 ?  92  CYS   A N    1 
ATOM   1995 C  CA   . CYS   A 1 92  ? 28.681 -1.381  9.480   1.00 11.20 ?  92  CYS   A CA   1 
ATOM   1996 C  C    . CYS   A 1 92  ? 29.334 -2.203  8.377   1.00 10.79 ?  92  CYS   A C    1 
ATOM   1997 O  O    . CYS   A 1 92  ? 30.496 -1.958  8.015   1.00 11.50 ?  92  CYS   A O    1 
ATOM   1998 C  CB   . CYS   A 1 92  ? 28.480 0.063   9.019   1.00 11.56 ?  92  CYS   A CB   1 
ATOM   1999 S  SG   . CYS   A 1 92  ? 27.474 0.165   7.506   1.00 10.96 ?  92  CYS   A SG   1 
ATOM   2000 H  H    . CYS   A 1 92  ? 30.288 -1.089  10.584  1.00 13.69 ?  92  CYS   A H    1 
ATOM   2001 H  HA   . CYS   A 1 92  ? 27.813 -1.760  9.674   1.00 13.44 ?  92  CYS   A HA   1 
ATOM   2002 H  HB2  . CYS   A 1 92  ? 28.025 0.564   9.716   1.00 13.88 ?  92  CYS   A HB2  1 
ATOM   2003 H  HB3  . CYS   A 1 92  ? 29.342 0.465   8.830   1.00 13.88 ?  92  CYS   A HB3  1 
ATOM   2004 H  HG   . CYS   A 1 92  ? 27.340 1.314   7.211   1.00 13.16 ?  92  CYS   A HG   1 
ATOM   2005 N  N    . LEU   A 1 93  ? 28.599 -3.188  7.871   1.00 10.59 ?  93  LEU   A N    1 
ATOM   2006 C  CA   . LEU   A 1 93  ? 29.009 -3.949  6.698   1.00 10.23 ?  93  LEU   A CA   1 
ATOM   2007 C  C    . LEU   A 1 93  ? 28.418 -3.256  5.474   1.00 9.87  ?  93  LEU   A C    1 
ATOM   2008 O  O    . LEU   A 1 93  ? 27.204 -3.310  5.245   1.00 10.03 ?  93  LEU   A O    1 
ATOM   2009 C  CB   . LEU   A 1 93  ? 28.524 -5.392  6.808   1.00 10.96 ?  93  LEU   A CB   1 
ATOM   2010 C  CG   . LEU   A 1 93  ? 28.921 -6.294  5.639   1.00 11.05 ?  93  LEU   A CG   1 
ATOM   2011 C  CD1  . LEU   A 1 93  ? 30.425 -6.557  5.629   1.00 12.04 ?  93  LEU   A CD1  1 
ATOM   2012 C  CD2  . LEU   A 1 93  ? 28.145 -7.615  5.679   1.00 11.70 ?  93  LEU   A CD2  1 
ATOM   2013 H  H    . LEU   A 1 93  ? 27.843 -3.435  8.204   1.00 12.71 ?  93  LEU   A H    1 
ATOM   2014 H  HA   . LEU   A 1 93  ? 29.973 -3.940  6.630   1.00 12.28 ?  93  LEU   A HA   1 
ATOM   2015 H  HB2  . LEU   A 1 93  ? 28.896 -5.777  7.620   1.00 13.15 ?  93  LEU   A HB2  1 
ATOM   2016 H  HB3  . LEU   A 1 93  ? 27.558 -5.390  6.863   1.00 13.15 ?  93  LEU   A HB3  1 
ATOM   2017 H  HG   . LEU   A 1 93  ? 28.701 -5.854  4.812   1.00 13.27 ?  93  LEU   A HG   1 
ATOM   2018 H  HD11 . LEU   A 1 93  ? 30.638 -7.176  4.913   1.00 14.45 ?  93  LEU   A HD11 1 
ATOM   2019 H  HD12 . LEU   A 1 93  ? 30.895 -5.722  5.500   1.00 14.45 ?  93  LEU   A HD12 1 
ATOM   2020 H  HD13 . LEU   A 1 93  ? 30.686 -6.952  6.485   1.00 14.45 ?  93  LEU   A HD13 1 
ATOM   2021 H  HD21 . LEU   A 1 93  ? 28.423 -8.167  4.929   1.00 14.04 ?  93  LEU   A HD21 1 
ATOM   2022 H  HD22 . LEU   A 1 93  ? 28.338 -8.075  6.513   1.00 14.04 ?  93  LEU   A HD22 1 
ATOM   2023 H  HD23 . LEU   A 1 93  ? 27.197 -7.426  5.617   1.00 14.04 ?  93  LEU   A HD23 1 
ATOM   2024 N  N    . HIS   A 1 94  ? 29.270 -2.567  4.714   1.00 9.69  ?  94  HIS   A N    1 
ATOM   2025 C  CA   . HIS   A 1 94  ? 28.849 -1.893  3.490   1.00 9.76  ?  94  HIS   A CA   1 
ATOM   2026 C  C    . HIS   A 1 94  ? 28.863 -2.926  2.381   1.00 9.81  ?  94  HIS   A C    1 
ATOM   2027 O  O    . HIS   A 1 94  ? 29.930 -3.445  2.042   1.00 11.22 ?  94  HIS   A O    1 
ATOM   2028 C  CB   . HIS   A 1 94  ? 29.813 -0.753  3.163   1.00 9.82  ?  94  HIS   A CB   1 
ATOM   2029 C  CG   . HIS   A 1 94  ? 29.797 0.340   4.175   1.00 9.75  ?  94  HIS   A CG   1 
ATOM   2030 N  ND1  . HIS   A 1 94  ? 28.926 1.408   4.110   1.00 10.02 ?  94  HIS   A ND1  1 
ATOM   2031 C  CD2  . HIS   A 1 94  ? 30.533 0.509   5.297   1.00 10.44 ?  94  HIS   A CD2  1 
ATOM   2032 C  CE1  . HIS   A 1 94  ? 29.137 2.187   5.154   1.00 10.14 ?  94  HIS   A CE1  1 
ATOM   2033 N  NE2  . HIS   A 1 94  ? 30.106 1.665   5.889   1.00 10.49 ?  94  HIS   A NE2  1 
ATOM   2034 H  H    . HIS   A 1 94  ? 30.107 -2.470  4.892   1.00 11.63 ?  94  HIS   A H    1 
ATOM   2035 H  HA   . HIS   A 1 94  ? 27.946 -1.540  3.593   1.00 11.72 ?  94  HIS   A HA   1 
ATOM   2036 H  HB2  . HIS   A 1 94  ? 30.706 -1.103  3.115   1.00 11.79 ?  94  HIS   A HB2  1 
ATOM   2037 H  HB3  . HIS   A 1 94  ? 29.554 -0.365  2.309   1.00 11.79 ?  94  HIS   A HB3  1 
ATOM   2038 H  HD2  . HIS   A 1 94  ? 31.203 -0.047  5.611   1.00 12.53 ?  94  HIS   A HD2  1 
ATOM   2039 H  HE1  . HIS   A 1 94  ? 28.673 2.977   5.336   1.00 12.17 ?  94  HIS   A HE1  1 
ATOM   2040 H  HE2  . HIS   A 1 94  ? 30.415 2.014   6.612   1.00 12.60 ?  94  HIS   A HE2  1 
ATOM   2041 N  N    . VAL   A 1 95  ? 27.693 -3.248  1.831   1.00 9.22  ?  95  VAL   A N    1 
ATOM   2042 C  CA   . VAL   A 1 95  ? 27.555 -4.282  0.812   1.00 9.57  ?  95  VAL   A CA   1 
ATOM   2043 C  C    . VAL   A 1 95  ? 27.009 -3.644  -0.451  1.00 9.38  ?  95  VAL   A C    1 
ATOM   2044 O  O    . VAL   A 1 95  ? 25.998 -2.930  -0.401  1.00 9.97  ?  95  VAL   A O    1 
ATOM   2045 C  CB   . VAL   A 1 95  ? 26.626 -5.423  1.267   1.00 10.20 ?  95  VAL   A CB   1 
ATOM   2046 C  CG1  . VAL   A 1 95  ? 26.519 -6.469  0.168   1.00 11.12 ?  95  VAL   A CG1  1 
ATOM   2047 C  CG2  . VAL   A 1 95  ? 27.121 -6.036  2.557   1.00 10.25 ?  95  VAL   A CG2  1 
ATOM   2048 H  H    . VAL   A 1 95  ? 26.946 -2.879  2.045   1.00 11.07 ?  95  VAL   A H    1 
ATOM   2049 H  HA   . VAL   A 1 95  ? 28.422 -4.658  0.611   1.00 11.49 ?  95  VAL   A HA   1 
ATOM   2050 H  HB   . VAL   A 1 95  ? 25.740 -5.070  1.423   1.00 12.25 ?  95  VAL   A HB   1 
ATOM   2051 H  HG11 . VAL   A 1 95  ? 26.125 -7.281  0.537   1.00 13.35 ?  95  VAL   A HG11 1 
ATOM   2052 H  HG12 . VAL   A 1 95  ? 25.955 -6.133  -0.547  1.00 13.35 ?  95  VAL   A HG12 1 
ATOM   2053 H  HG13 . VAL   A 1 95  ? 27.405 -6.670  -0.176  1.00 13.35 ?  95  VAL   A HG13 1 
ATOM   2054 H  HG21 . VAL   A 1 95  ? 26.557 -6.795  2.780   1.00 12.30 ?  95  VAL   A HG21 1 
ATOM   2055 H  HG22 . VAL   A 1 95  ? 28.036 -6.324  2.441   1.00 12.30 ?  95  VAL   A HG22 1 
ATOM   2056 H  HG23 . VAL   A 1 95  ? 27.065 -5.368  3.258   1.00 12.30 ?  95  VAL   A HG23 1 
ATOM   2057 N  N    . VAL   A 1 96  ? 27.643 -3.932  -1.584  1.00 9.44  ?  96  VAL   A N    1 
ATOM   2058 C  CA   . VAL   A 1 96  ? 27.232 -3.384  -2.870  1.00 10.02 ?  96  VAL   A CA   1 
ATOM   2059 C  C    . VAL   A 1 96  ? 26.427 -4.433  -3.630  1.00 10.37 ?  96  VAL   A C    1 
ATOM   2060 O  O    . VAL   A 1 96  ? 26.985 -5.380  -4.192  1.00 11.28 ?  96  VAL   A O    1 
ATOM   2061 C  CB   . VAL   A 1 96  ? 28.423 -2.910  -3.698  1.00 10.33 ?  96  VAL   A CB   1 
ATOM   2062 C  CG1  . VAL   A 1 96  ? 27.922 -2.271  -4.975  1.00 10.51 ?  96  VAL   A CG1  1 
ATOM   2063 C  CG2  . VAL   A 1 96  ? 29.281 -1.940  -2.904  1.00 11.04 ?  96  VAL   A CG2  1 
ATOM   2064 H  H    . VAL   A 1 96  ? 28.338 -4.445  -1.630  1.00 11.33 ?  96  VAL   A H    1 
ATOM   2065 H  HA   . VAL   A 1 96  ? 26.656 -2.622  -2.714  1.00 12.02 ?  96  VAL   A HA   1 
ATOM   2066 H  HB   . VAL   A 1 96  ? 28.971 -3.666  -3.938  1.00 12.40 ?  96  VAL   A HB   1 
ATOM   2067 H  HG11 . VAL   A 1 96  ? 28.660 -1.795  -5.393  1.00 12.62 ?  96  VAL   A HG11 1 
ATOM   2068 H  HG12 . VAL   A 1 96  ? 27.596 -2.960  -5.568  1.00 12.62 ?  96  VAL   A HG12 1 
ATOM   2069 H  HG13 . VAL   A 1 96  ? 27.212 -1.646  -4.759  1.00 12.62 ?  96  VAL   A HG13 1 
ATOM   2070 H  HG21 . VAL   A 1 96  ? 29.980 -1.585  -3.475  1.00 13.25 ?  96  VAL   A HG21 1 
ATOM   2071 H  HG22 . VAL   A 1 96  ? 28.723 -1.208  -2.580  1.00 13.25 ?  96  VAL   A HG22 1 
ATOM   2072 H  HG23 . VAL   A 1 96  ? 29.674 -2.405  -2.149  1.00 13.25 ?  96  VAL   A HG23 1 
ATOM   2073 N  N    A GLY   A 1 97  ? 25.108 -4.280  -3.653  0.68 10.43 ?  97  GLY   A N    1 
ATOM   2074 N  N    B GLY   A 1 97  ? 25.111 -4.255  -3.679  0.32 10.40 ?  97  GLY   A N    1 
ATOM   2075 C  CA   A GLY   A 1 97  ? 24.298 -5.036  -4.572  0.68 11.01 ?  97  GLY   A CA   1 
ATOM   2076 C  CA   B GLY   A 1 97  ? 24.287 -5.038  -4.565  0.32 10.67 ?  97  GLY   A CA   1 
ATOM   2077 C  C    A GLY   A 1 97  ? 24.312 -4.364  -5.929  0.68 10.96 ?  97  GLY   A C    1 
ATOM   2078 C  C    B GLY   A 1 97  ? 24.279 -4.440  -5.958  0.32 10.80 ?  97  GLY   A C    1 
ATOM   2079 O  O    A GLY   A 1 97  ? 24.632 -3.176  -6.048  0.68 11.74 ?  97  GLY   A O    1 
ATOM   2080 O  O    B GLY   A 1 97  ? 24.475 -3.233  -6.136  0.32 10.89 ?  97  GLY   A O    1 
ATOM   2081 H  H    A GLY   A 1 97  ? 24.668 -3.742  -3.143  0.68 12.52 ?  97  GLY   A H    1 
ATOM   2082 H  H    B GLY   A 1 97  ? 24.677 -3.685  -3.202  0.32 12.49 ?  97  GLY   A H    1 
ATOM   2083 H  HA2  A GLY   A 1 97  ? 24.653 -5.936  -4.651  0.68 13.21 ?  97  GLY   A HA2  1 
ATOM   2084 H  HA2  B GLY   A 1 97  ? 24.634 -5.942  -4.608  0.32 12.81 ?  97  GLY   A HA2  1 
ATOM   2085 H  HA3  A GLY   A 1 97  ? 23.386 -5.085  -4.244  0.68 13.21 ?  97  GLY   A HA3  1 
ATOM   2086 H  HA3  B GLY   A 1 97  ? 23.378 -5.068  -4.228  0.32 12.81 ?  97  GLY   A HA3  1 
ATOM   2087 N  N    A PRO   A 1 98  ? 23.966 -5.100  -6.981  0.68 10.93 ?  98  PRO   A N    1 
ATOM   2088 N  N    B PRO   A 1 98  ? 24.049 -5.268  -6.974  0.32 11.16 ?  98  PRO   A N    1 
ATOM   2089 C  CA   A PRO   A 1 98  ? 23.842 -4.469  -8.300  0.68 11.74 ?  98  PRO   A CA   1 
ATOM   2090 C  CA   B PRO   A 1 98  ? 24.001 -4.750  -8.347  0.32 11.66 ?  98  PRO   A CA   1 
ATOM   2091 C  C    A PRO   A 1 98  ? 22.721 -3.435  -8.318  0.68 11.54 ?  98  PRO   A C    1 
ATOM   2092 C  C    B PRO   A 1 98  ? 22.872 -3.743  -8.523  0.32 11.84 ?  98  PRO   A C    1 
ATOM   2093 O  O    A PRO   A 1 98  ? 21.650 -3.630  -7.738  0.68 11.53 ?  98  PRO   A O    1 
ATOM   2094 O  O    B PRO   A 1 98  ? 21.775 -3.903  -7.982  0.32 12.34 ?  98  PRO   A O    1 
ATOM   2095 C  CB   A PRO   A 1 98  ? 23.534 -5.650  -9.228  0.68 11.86 ?  98  PRO   A CB   1 
ATOM   2096 C  CB   B PRO   A 1 98  ? 23.769 -6.010  -9.191  0.32 11.74 ?  98  PRO   A CB   1 
ATOM   2097 C  CG   A PRO   A 1 98  ? 22.923 -6.688  -8.339  0.68 11.87 ?  98  PRO   A CG   1 
ATOM   2098 C  CG   B PRO   A 1 98  ? 23.132 -6.986  -8.248  0.32 11.98 ?  98  PRO   A CG   1 
ATOM   2099 C  CD   A PRO   A 1 98  ? 23.641 -6.538  -7.018  0.68 11.36 ?  98  PRO   A CD   1 
ATOM   2100 C  CD   B PRO   A 1 98  ? 23.780 -6.715  -6.920  0.32 11.26 ?  98  PRO   A CD   1 
ATOM   2101 H  HA   A PRO   A 1 98  ? 24.679 -4.060  -8.557  0.68 14.09 ?  98  PRO   A HA   1 
ATOM   2102 H  HA   B PRO   A 1 98  ? 24.847 -4.342  -8.593  0.32 13.99 ?  98  PRO   A HA   1 
ATOM   2103 H  HB2  A PRO   A 1 98  ? 22.902 -5.376  -9.910  0.68 14.23 ?  98  PRO   A HB2  1 
ATOM   2104 H  HB2  B PRO   A 1 98  ? 23.174 -5.806  -9.930  0.32 14.10 ?  98  PRO   A HB2  1 
ATOM   2105 H  HB3  A PRO   A 1 98  ? 24.353 -5.981  -9.627  0.68 14.23 ?  98  PRO   A HB3  1 
ATOM   2106 H  HB3  B PRO   A 1 98  ? 24.618 -6.351  -9.516  0.32 14.10 ?  98  PRO   A HB3  1 
ATOM   2107 H  HG2  A PRO   A 1 98  ? 21.977 -6.519  -8.237  0.68 14.25 ?  98  PRO   A HG2  1 
ATOM   2108 H  HG2  B PRO   A 1 98  ? 22.177 -6.820  -8.205  0.32 14.38 ?  98  PRO   A HG2  1 
ATOM   2109 H  HG3  A PRO   A 1 98  ? 23.078 -7.572  -8.713  0.68 14.25 ?  98  PRO   A HG3  1 
ATOM   2110 H  HG3  B PRO   A 1 98  ? 23.312 -7.891  -8.543  0.32 14.38 ?  98  PRO   A HG3  1 
ATOM   2111 H  HD2  A PRO   A 1 98  ? 23.048 -6.782  -6.284  0.68 13.64 ?  98  PRO   A HD2  1 
ATOM   2112 H  HD2  B PRO   A 1 98  ? 23.168 -6.922  -6.196  0.32 13.52 ?  98  PRO   A HD2  1 
ATOM   2113 H  HD3  A PRO   A 1 98  ? 24.452 -7.073  -7.006  0.68 13.64 ?  98  PRO   A HD3  1 
ATOM   2114 H  HD3  B PRO   A 1 98  ? 24.610 -7.214  -6.839  0.32 13.52 ?  98  PRO   A HD3  1 
ATOM   2115 N  N    A ASN   A 1 99  ? 22.988 -2.315  -8.984  0.68 12.42 ?  99  ASN   A N    1 
ATOM   2116 N  N    B ASN   A 1 99  ? 23.155 -2.688  -9.284  0.32 11.89 ?  99  ASN   A N    1 
ATOM   2117 C  CA   A ASN   A 1 99  ? 22.003 -1.260  -9.200  0.68 13.35 ?  99  ASN   A CA   1 
ATOM   2118 C  CA   B ASN   A 1 99  ? 22.178 -1.647  -9.587  0.32 12.22 ?  99  ASN   A CA   1 
ATOM   2119 C  C    A ASN   A 1 99  ? 21.462 -1.414  -10.617 0.68 14.71 ?  99  ASN   A C    1 
ATOM   2120 C  C    B ASN   A 1 99  ? 21.568 -1.944  -10.952 0.32 12.93 ?  99  ASN   A C    1 
ATOM   2121 O  O    A ASN   A 1 99  ? 22.151 -1.092  -11.594 0.68 15.62 ?  99  ASN   A O    1 
ATOM   2122 O  O    B ASN   A 1 99  ? 22.246 -1.844  -11.981 0.32 12.69 ?  99  ASN   A O    1 
ATOM   2123 C  CB   A ASN   A 1 99  ? 22.639 0.113   -8.995  0.68 13.52 ?  99  ASN   A CB   1 
ATOM   2124 C  CB   B ASN   A 1 99  ? 22.840 -0.274  -9.582  0.32 12.97 ?  99  ASN   A CB   1 
ATOM   2125 C  CG   A ASN   A 1 99  ? 21.615 1.241   -8.980  0.68 13.74 ?  99  ASN   A CG   1 
ATOM   2126 C  CG   B ASN   A 1 99  ? 21.853 0.854   -9.816  0.32 13.74 ?  99  ASN   A CG   1 
ATOM   2127 O  OD1  A ASN   A 1 99  ? 20.617 1.195   -9.701  0.68 14.37 ?  99  ASN   A OD1  1 
ATOM   2128 O  OD1  B ASN   A 1 99  ? 20.917 0.722   -10.600 0.32 13.82 ?  99  ASN   A OD1  1 
ATOM   2129 N  ND2  A ASN   A 1 99  ? 21.869 2.267   -8.170  0.68 14.14 ?  99  ASN   A ND2  1 
ATOM   2130 N  ND2  B ASN   A 1 99  ? 22.058 1.971   -9.129  0.32 14.64 ?  99  ASN   A ND2  1 
ATOM   2131 H  H    A ASN   A 1 99  ? 23.760 -2.136  -9.311  0.68 14.91 ?  99  ASN   A H    1 
ATOM   2132 H  H    B ASN   A 1 99  ? 23.932 -2.543  -9.625  0.32 14.28 ?  99  ASN   A H    1 
ATOM   2133 H  HA   A ASN   A 1 99  ? 21.270 -1.367  -8.563  0.68 16.03 ?  99  ASN   A HA   1 
ATOM   2134 H  HA   B ASN   A 1 99  ? 21.471 -1.668  -8.917  0.32 14.67 ?  99  ASN   A HA   1 
ATOM   2135 H  HB2  A ASN   A 1 99  ? 23.113 0.122   -8.152  0.68 16.23 ?  99  ASN   A HB2  1 
ATOM   2136 H  HB2  B ASN   A 1 99  ? 23.266 -0.133  -8.724  0.32 15.57 ?  99  ASN   A HB2  1 
ATOM   2137 H  HB3  A ASN   A 1 99  ? 23.258 0.275   -9.726  0.68 16.23 ?  99  ASN   A HB3  1 
ATOM   2138 H  HB3  B ASN   A 1 99  ? 23.493 -0.252  -10.293 0.32 15.57 ?  99  ASN   A HB3  1 
ATOM   2139 H  HD21 A ASN   A 1 99  ? 21.322 2.927   -8.126  0.68 16.97 ?  99  ASN   A HD21 1 
ATOM   2140 H  HD21 B ASN   A 1 99  ? 21.524 2.637   -9.223  0.32 17.57 ?  99  ASN   A HD21 1 
ATOM   2141 H  HD22 A ASN   A 1 99  ? 22.579 2.262   -7.684  0.68 16.97 ?  99  ASN   A HD22 1 
ATOM   2142 H  HD22 B ASN   A 1 99  ? 22.722 2.023   -8.589  0.32 17.57 ?  99  ASN   A HD22 1 
ATOM   2143 N  N    A VAL   A 1 100 ? 20.226 -1.910  -10.719 0.68 16.27 ?  100 VAL   A N    1 
ATOM   2144 N  N    B VAL   A 1 100 ? 20.278 -2.285  -10.950 0.32 14.58 ?  100 VAL   A N    1 
ATOM   2145 C  CA   A VAL   A 1 100 ? 19.614 -2.145  -12.023 0.68 17.85 ?  100 VAL   A CA   1 
ATOM   2146 C  CA   B VAL   A 1 100 ? 19.587 -2.665  -12.178 0.32 16.39 ?  100 VAL   A CA   1 
ATOM   2147 C  C    A VAL   A 1 100 ? 19.477 -0.842  -12.797 0.68 18.11 ?  100 VAL   A C    1 
ATOM   2148 C  C    B VAL   A 1 100 ? 19.612 -1.524  -13.180 0.32 16.67 ?  100 VAL   A C    1 
ATOM   2149 O  O    A VAL   A 1 100 ? 19.563 -0.830  -14.030 0.68 18.63 ?  100 VAL   A O    1 
ATOM   2150 O  O    B VAL   A 1 100 ? 19.701 -1.745  -14.395 0.32 16.64 ?  100 VAL   A O    1 
ATOM   2151 C  CB   A VAL   A 1 100 ? 18.271 -2.887  -11.855 0.68 19.64 ?  100 VAL   A CB   1 
ATOM   2152 C  CB   B VAL   A 1 100 ? 18.143 -3.088  -11.857 0.32 18.07 ?  100 VAL   A CB   1 
ATOM   2153 C  CG1  A VAL   A 1 100 ? 17.530 -2.998  -13.183 0.68 19.85 ?  100 VAL   A CG1  1 
ATOM   2154 C  CG1  B VAL   A 1 100 ? 17.504 -3.745  -13.068 0.32 18.38 ?  100 VAL   A CG1  1 
ATOM   2155 C  CG2  A VAL   A 1 100 ? 18.513 -4.272  -11.268 0.68 20.02 ?  100 VAL   A CG2  1 
ATOM   2156 C  CG2  B VAL   A 1 100 ? 18.127 -4.005  -10.657 0.32 18.77 ?  100 VAL   A CG2  1 
ATOM   2157 H  H    A VAL   A 1 100 ? 19.718 -2.120  -10.048 0.68 19.53 ?  100 VAL   A H    1 
ATOM   2158 H  H    B VAL   A 1 100 ? 19.783 -2.293  -10.248 0.32 17.50 ?  100 VAL   A H    1 
ATOM   2159 H  HA   A VAL   A 1 100 ? 20.195 -2.728  -12.534 0.68 21.43 ?  100 VAL   A HA   1 
ATOM   2160 H  HA   B VAL   A 1 100 ? 20.041 -3.415  -12.584 0.32 19.67 ?  100 VAL   A HA   1 
ATOM   2161 H  HB   A VAL   A 1 100 ? 17.705 -2.398  -11.240 0.68 23.57 ?  100 VAL   A HB   1 
ATOM   2162 H  HB   B VAL   A 1 100 ? 17.625 -2.294  -11.642 0.32 21.69 ?  100 VAL   A HB   1 
ATOM   2163 H  HG11 A VAL   A 1 100 ? 16.801 -3.637  -13.088 0.68 23.83 ?  100 VAL   A HG11 1 
ATOM   2164 H  HG11 B VAL   A 1 100 ? 16.616 -4.046  -12.827 0.32 22.06 ?  100 VAL   A HG11 1 
ATOM   2165 H  HG12 A VAL   A 1 100 ? 17.173 -2.130  -13.425 0.68 23.83 ?  100 VAL   A HG12 1 
ATOM   2166 H  HG12 B VAL   A 1 100 ? 17.450 -3.098  -13.790 0.32 22.06 ?  100 VAL   A HG12 1 
ATOM   2167 H  HG13 A VAL   A 1 100 ? 18.145 -3.308  -13.866 0.68 23.83 ?  100 VAL   A HG13 1 
ATOM   2168 H  HG13 B VAL   A 1 100 ? 18.049 -4.498  -13.339 0.32 22.06 ?  100 VAL   A HG13 1 
ATOM   2169 H  HG21 A VAL   A 1 100 ? 17.666 -4.743  -11.199 0.68 24.03 ?  100 VAL   A HG21 1 
ATOM   2170 H  HG21 B VAL   A 1 100 ? 17.314 -4.525  -10.673 0.32 22.53 ?  100 VAL   A HG21 1 
ATOM   2171 H  HG22 A VAL   A 1 100 ? 19.115 -4.762  -11.851 0.68 24.03 ?  100 VAL   A HG22 1 
ATOM   2172 H  HG22 B VAL   A 1 100 ? 18.901 -4.588  -10.702 0.32 22.53 ?  100 VAL   A HG22 1 
ATOM   2173 H  HG23 A VAL   A 1 100 ? 18.910 -4.177  -10.388 0.68 24.03 ?  100 VAL   A HG23 1 
ATOM   2174 H  HG23 B VAL   A 1 100 ? 18.166 -3.467  -9.850  0.32 22.53 ?  100 VAL   A HG23 1 
ATOM   2175 N  N    A ASN   A 1 101 ? 19.275 0.273   -12.101 0.68 19.15 ?  101 ASN   A N    1 
ATOM   2176 N  N    B ASN   A 1 101 ? 19.496 -0.287  -12.690 0.32 17.18 ?  101 ASN   A N    1 
ATOM   2177 C  CA   A ASN   A 1 101 ? 19.206 1.557   -12.786 0.68 20.21 ?  101 ASN   A CA   1 
ATOM   2178 C  CA   B ASN   A 1 101 ? 19.447 0.869   -13.579 0.32 17.85 ?  101 ASN   A CA   1 
ATOM   2179 C  C    A ASN   A 1 101 ? 20.556 2.009   -13.341 0.68 22.47 ?  101 ASN   A C    1 
ATOM   2180 C  C    B ASN   A 1 101 ? 20.789 1.122   -14.249 0.32 18.73 ?  101 ASN   A C    1 
ATOM   2181 O  O    A ASN   A 1 101 ? 20.613 3.062   -13.988 0.68 24.05 ?  101 ASN   A O    1 
ATOM   2182 O  O    B ASN   A 1 101 ? 20.834 1.719   -15.330 0.32 18.87 ?  101 ASN   A O    1 
ATOM   2183 C  CB   A ASN   A 1 101 ? 18.585 2.598   -11.856 0.68 19.40 ?  101 ASN   A CB   1 
ATOM   2184 C  CB   B ASN   A 1 101 ? 18.988 2.104   -12.799 0.32 17.83 ?  101 ASN   A CB   1 
ATOM   2185 C  CG   A ASN   A 1 101 ? 17.213 2.170   -11.347 0.68 18.72 ?  101 ASN   A CG   1 
ATOM   2186 C  CG   B ASN   A 1 101 ? 17.767 1.828   -11.941 0.32 18.26 ?  101 ASN   A CG   1 
ATOM   2187 O  OD1  A ASN   A 1 101 ? 16.384 1.665   -12.108 0.68 18.70 ?  101 ASN   A OD1  1 
ATOM   2188 O  OD1  B ASN   A 1 101 ? 16.825 1.161   -12.372 0.32 19.08 ?  101 ASN   A OD1  1 
ATOM   2189 N  ND2  A ASN   A 1 101 ? 16.978 2.348   -10.055 0.68 18.77 ?  101 ASN   A ND2  1 
ATOM   2190 N  ND2  B ASN   A 1 101 ? 17.784 2.329   -10.713 0.32 18.37 ?  101 ASN   A ND2  1 
ATOM   2191 H  H    A ASN   A 1 101 ? 19.166 0.310   -11.253 0.68 22.98 ?  101 ASN   A H    1 
ATOM   2192 H  H    B ASN   A 1 101 ? 19.438 -0.087  -11.852 0.32 20.62 ?  101 ASN   A H    1 
ATOM   2193 H  HA   A ASN   A 1 101 ? 18.612 1.461   -13.545 0.68 24.26 ?  101 ASN   A HA   1 
ATOM   2194 H  HA   B ASN   A 1 101 ? 18.802 0.711   -14.279 0.32 21.43 ?  101 ASN   A HA   1 
ATOM   2195 H  HB2  A ASN   A 1 101 ? 19.168 2.730   -11.093 0.68 23.29 ?  101 ASN   A HB2  1 
ATOM   2196 H  HB2  B ASN   A 1 101 ? 19.703 2.403   -12.215 0.32 21.40 ?  101 ASN   A HB2  1 
ATOM   2197 H  HB3  A ASN   A 1 101 ? 18.484 3.434   -12.344 0.68 23.29 ?  101 ASN   A HB3  1 
ATOM   2198 H  HB3  B ASN   A 1 101 ? 18.759 2.814   -13.426 0.32 21.40 ?  101 ASN   A HB3  1 
ATOM   2199 H  HD21 A ASN   A 1 101 ? 16.219 2.120   -9.725  0.68 22.53 ?  101 ASN   A HD21 1 
ATOM   2200 H  HD21 B ASN   A 1 101 ? 17.114 2.203   -10.189 0.32 22.04 ?  101 ASN   A HD21 1 
ATOM   2201 H  HD22 A ASN   A 1 101 ? 17.580 2.700   -9.553  0.68 22.53 ?  101 ASN   A HD22 1 
ATOM   2202 H  HD22 B ASN   A 1 101 ? 18.459 2.790   -10.446 0.32 22.04 ?  101 ASN   A HD22 1 
ATOM   2203 N  N    A LYS   A 1 102 ? 21.626 1.234   -13.122 0.68 24.12 ?  102 LYS   A N    1 
ATOM   2204 N  N    B LYS   A 1 102 ? 21.884 0.686   -13.628 0.32 19.93 ?  102 LYS   A N    1 
ATOM   2205 C  CA   A LYS   A 1 102 ? 22.912 1.438   -13.777 0.68 25.47 ?  102 LYS   A CA   1 
ATOM   2206 C  CA   B LYS   A 1 102 ? 23.207 0.791   -14.229 0.32 20.60 ?  102 LYS   A CA   1 
ATOM   2207 C  C    A LYS   A 1 102 ? 23.242 0.347   -14.786 0.68 25.90 ?  102 LYS   A C    1 
ATOM   2208 C  C    B LYS   A 1 102 ? 23.518 -0.375  -15.160 0.32 20.37 ?  102 LYS   A C    1 
ATOM   2209 O  O    A LYS   A 1 102 ? 24.316 0.394   -15.394 0.68 26.31 ?  102 LYS   A O    1 
ATOM   2210 O  O    B LYS   A 1 102 ? 24.648 -0.472  -15.648 0.32 20.25 ?  102 LYS   A O    1 
ATOM   2211 C  CB   A LYS   A 1 102 ? 24.045 1.508   -12.744 0.68 26.95 ?  102 LYS   A CB   1 
ATOM   2212 C  CB   B LYS   A 1 102 ? 24.285 0.840   -13.139 0.32 21.46 ?  102 LYS   A CB   1 
ATOM   2213 C  CG   A LYS   A 1 102 ? 23.932 2.641   -11.746 0.68 28.12 ?  102 LYS   A CG   1 
ATOM   2214 C  CG   B LYS   A 1 102 ? 24.188 2.020   -12.182 0.32 22.16 ?  102 LYS   A CG   1 
ATOM   2215 C  CD   A LYS   A 1 102 ? 25.110 2.621   -10.783 0.68 29.44 ?  102 LYS   A CD   1 
ATOM   2216 C  CD   B LYS   A 1 102 ? 25.242 1.908   -11.081 0.32 23.01 ?  102 LYS   A CD   1 
ATOM   2217 C  CE   A LYS   A 1 102 ? 25.015 3.729   -9.750  0.68 30.48 ?  102 LYS   A CE   1 
ATOM   2218 C  CE   B LYS   A 1 102 ? 25.055 2.970   -10.006 0.32 23.60 ?  102 LYS   A CE   1 
ATOM   2219 N  NZ   A LYS   A 1 102 ? 26.121 3.642   -8.754  0.68 31.06 ?  102 LYS   A NZ   1 
ATOM   2220 N  NZ   B LYS   A 1 102 ? 25.088 2.394   -8.628  0.32 23.96 ?  102 LYS   A NZ   1 
ATOM   2221 H  H    A LYS   A 1 102 ? 21.629 0.558   -12.587 0.68 28.95 ?  102 LYS   A H    1 
ATOM   2222 H  H    B LYS   A 1 102 ? 21.886 0.319   -12.850 0.32 23.92 ?  102 LYS   A H    1 
ATOM   2223 H  HA   A LYS   A 1 102 ? 22.899 2.274   -14.259 0.68 30.57 ?  102 LYS   A HA   1 
ATOM   2224 H  HA   B LYS   A 1 102 ? 23.261 1.620   -14.733 0.32 24.73 ?  102 LYS   A HA   1 
ATOM   2225 H  HB2  A LYS   A 1 102 ? 24.059 0.677   -12.243 0.68 32.34 ?  102 LYS   A HB2  1 
ATOM   2226 H  HB2  B LYS   A 1 102 ? 24.220 0.032   -12.608 0.32 25.76 ?  102 LYS   A HB2  1 
ATOM   2227 H  HB3  A LYS   A 1 102 ? 24.888 1.615   -13.214 0.68 32.34 ?  102 LYS   A HB3  1 
ATOM   2228 H  HB3  B LYS   A 1 102 ? 25.157 0.879   -13.566 0.32 25.76 ?  102 LYS   A HB3  1 
ATOM   2229 H  HG2  A LYS   A 1 102 ? 23.935 3.488   -12.220 0.68 33.75 ?  102 LYS   A HG2  1 
ATOM   2230 H  HG2  B LYS   A 1 102 ? 24.344 2.845   -12.668 0.32 26.60 ?  102 LYS   A HG2  1 
ATOM   2231 H  HG3  A LYS   A 1 102 ? 23.114 2.540   -11.236 0.68 33.75 ?  102 LYS   A HG3  1 
ATOM   2232 H  HG3  B LYS   A 1 102 ? 23.311 2.032   -11.769 0.32 26.60 ?  102 LYS   A HG3  1 
ATOM   2233 H  HD2  A LYS   A 1 102 ? 25.125 1.771   -10.316 0.68 35.33 ?  102 LYS   A HD2  1 
ATOM   2234 H  HD2  B LYS   A 1 102 ? 25.181 1.035   -10.662 0.32 27.61 ?  102 LYS   A HD2  1 
ATOM   2235 H  HD3  A LYS   A 1 102 ? 25.933 2.741   -11.283 0.68 35.33 ?  102 LYS   A HD3  1 
ATOM   2236 H  HD3  B LYS   A 1 102 ? 26.122 2.026   -11.472 0.32 27.61 ?  102 LYS   A HD3  1 
ATOM   2237 H  HE2  A LYS   A 1 102 ? 25.073 4.588   -10.197 0.68 36.58 ?  102 LYS   A HE2  1 
ATOM   2238 H  HE2  B LYS   A 1 102 ? 25.772 3.620   -10.077 0.32 28.33 ?  102 LYS   A HE2  1 
ATOM   2239 H  HE3  A LYS   A 1 102 ? 24.171 3.653   -9.277  0.68 36.58 ?  102 LYS   A HE3  1 
ATOM   2240 H  HE3  B LYS   A 1 102 ? 24.198 3.403   -10.132 0.32 28.33 ?  102 LYS   A HE3  1 
ATOM   2241 H  HZ1  A LYS   A 1 102 ? 26.047 4.299   -8.160  0.68 37.28 ?  102 LYS   A HZ1  1 
ATOM   2242 H  HZ1  B LYS   A 1 102 ? 24.774 2.986   -8.042  0.32 28.76 ?  102 LYS   A HZ1  1 
ATOM   2243 H  HZ2  A LYS   A 1 102 ? 26.086 2.861   -8.329  0.68 37.28 ?  102 LYS   A HZ2  1 
ATOM   2244 H  HZ2  B LYS   A 1 102 ? 24.585 1.659   -8.593  0.32 28.76 ?  102 LYS   A HZ2  1 
ATOM   2245 H  HZ3  A LYS   A 1 102 ? 26.907 3.712   -9.167  0.68 37.28 ?  102 LYS   A HZ3  1 
ATOM   2246 H  HZ3  B LYS   A 1 102 ? 25.922 2.180   -8.406  0.32 28.76 ?  102 LYS   A HZ3  1 
ATOM   2247 N  N    A GLY   A 1 103 ? 22.365 -0.639  -14.970 0.68 26.60 ?  103 GLY   A N    1 
ATOM   2248 N  N    B GLY   A 1 103 ? 22.563 -1.271  -15.399 0.32 20.42 ?  103 GLY   A N    1 
ATOM   2249 C  CA   A GLY   A 1 103 ? 22.618 -1.719  -15.904 0.68 26.70 ?  103 GLY   A CA   1 
ATOM   2250 C  CA   B GLY   A 1 103 ? 22.827 -2.430  -16.226 0.32 20.33 ?  103 GLY   A CA   1 
ATOM   2251 C  C    A GLY   A 1 103 ? 23.470 -2.847  -15.369 0.68 26.64 ?  103 GLY   A C    1 
ATOM   2252 C  C    B GLY   A 1 103 ? 23.625 -3.522  -15.551 0.32 19.74 ?  103 GLY   A C    1 
ATOM   2253 O  O    A GLY   A 1 103 ? 24.058 -3.587  -16.162 0.68 27.50 ?  103 GLY   A O    1 
ATOM   2254 O  O    B GLY   A 1 103 ? 24.078 -4.451  -16.232 0.32 19.77 ?  103 GLY   A O    1 
ATOM   2255 H  H    A GLY   A 1 103 ? 21.616 -0.708  -14.561 0.68 31.92 ?  103 GLY   A H    1 
ATOM   2256 H  H    B GLY   A 1 103 ? 21.760 -1.225  -15.086 0.32 24.50 ?  103 GLY   A H    1 
ATOM   2257 H  HA2  A GLY   A 1 103 ? 21.768 -2.085  -16.207 0.68 32.05 ?  103 GLY   A HA2  1 
ATOM   2258 H  HA2  B GLY   A 1 103 ? 21.988 -2.819  -16.504 0.32 24.41 ?  103 GLY   A HA2  1 
ATOM   2259 H  HA3  A GLY   A 1 103 ? 23.082 -1.369  -16.679 0.68 32.05 ?  103 GLY   A HA3  1 
ATOM   2260 H  HA3  B GLY   A 1 103 ? 23.303 -2.133  -17.021 0.32 24.41 ?  103 GLY   A HA3  1 
ATOM   2261 N  N    A GLU   A 1 104 ? 23.562 -3.004  -14.051 0.68 25.10 ?  104 GLU   A N    1 
ATOM   2262 N  N    B GLU   A 1 104 ? 23.798 -3.454  -14.235 0.32 18.93 ?  104 GLU   A N    1 
ATOM   2263 C  CA   A GLU   A 1 104 ? 24.430 -4.010  -13.455 0.68 23.55 ?  104 GLU   A CA   1 
ATOM   2264 C  CA   B GLU   A 1 104 ? 24.664 -4.391  -13.536 0.32 18.07 ?  104 GLU   A CA   1 
ATOM   2265 C  C    A GLU   A 1 104 ? 23.735 -5.368  -13.360 0.68 23.87 ?  104 GLU   A C    1 
ATOM   2266 C  C    B GLU   A 1 104 ? 23.970 -5.738  -13.356 0.32 18.39 ?  104 GLU   A C    1 
ATOM   2267 O  O    A GLU   A 1 104 ? 22.508 -5.459  -13.264 0.68 24.11 ?  104 GLU   A O    1 
ATOM   2268 O  O    B GLU   A 1 104 ? 22.775 -5.810  -13.051 0.32 18.28 ?  104 GLU   A O    1 
ATOM   2269 C  CB   A GLU   A 1 104 ? 24.929 -3.528  -12.088 0.68 21.73 ?  104 GLU   A CB   1 
ATOM   2270 C  CB   B GLU   A 1 104 ? 25.099 -3.799  -12.193 0.32 17.45 ?  104 GLU   A CB   1 
ATOM   2271 C  CG   A GLU   A 1 104 ? 25.878 -2.331  -12.237 0.68 21.11 ?  104 GLU   A CG   1 
ATOM   2272 C  CG   B GLU   A 1 104 ? 25.868 -2.488  -12.357 0.32 17.76 ?  104 GLU   A CG   1 
ATOM   2273 C  CD   A GLU   A 1 104 ? 26.181 -1.556  -10.960 0.68 19.94 ?  104 GLU   A CD   1 
ATOM   2274 C  CD   B GLU   A 1 104 ? 26.242 -1.816  -11.046 0.32 17.76 ?  104 GLU   A CD   1 
ATOM   2275 O  OE1  A GLU   A 1 104 ? 25.620 -1.866  -9.888  0.68 18.39 ?  104 GLU   A OE1  1 
ATOM   2276 O  OE1  B GLU   A 1 104 ? 25.683 -2.177  -9.990  0.32 17.57 ?  104 GLU   A OE1  1 
ATOM   2277 O  OE2  A GLU   A 1 104 ? 26.990 -0.603  -11.055 0.68 20.72 -1 104 GLU   A OE2  1 
ATOM   2278 O  OE2  B GLU   A 1 104 ? 27.101 -0.908  -11.081 0.32 18.44 -1 104 GLU   A OE2  1 
ATOM   2279 H  H    A GLU   A 1 104 ? 23.136 -2.525  -13.477 0.68 30.12 ?  104 GLU   A H    1 
ATOM   2280 H  H    B GLU   A 1 104 ? 23.414 -2.872  -13.729 0.32 22.72 ?  104 GLU   A H    1 
ATOM   2281 H  HA   A GLU   A 1 104 ? 25.203 -4.119  -14.027 0.68 28.27 ?  104 GLU   A HA   1 
ATOM   2282 H  HA   B GLU   A 1 104 ? 25.465 -4.530  -14.068 0.32 21.69 ?  104 GLU   A HA   1 
ATOM   2283 H  HB2  A GLU   A 1 104 ? 24.168 -3.259  -11.551 0.68 26.08 ?  104 GLU   A HB2  1 
ATOM   2284 H  HB2  B GLU   A 1 104 ? 24.315 -3.621  -11.654 0.32 20.94 ?  104 GLU   A HB2  1 
ATOM   2285 H  HB3  A GLU   A 1 104 ? 25.408 -4.252  -11.655 0.68 26.08 ?  104 GLU   A HB3  1 
ATOM   2286 H  HB3  B GLU   A 1 104 ? 25.682 -4.430  -11.744 0.32 20.94 ?  104 GLU   A HB3  1 
ATOM   2287 H  HG2  A GLU   A 1 104 ? 26.718 -2.655  -12.587 0.68 25.33 ?  104 GLU   A HG2  1 
ATOM   2288 H  HG2  B GLU   A 1 104 ? 26.690 -2.664  -12.839 0.32 21.31 ?  104 GLU   A HG2  1 
ATOM   2289 H  HG3  A GLU   A 1 104 ? 25.478 -1.706  -12.860 0.68 25.33 ?  104 GLU   A HG3  1 
ATOM   2290 H  HG3  B GLU   A 1 104 ? 25.322 -1.864  -12.862 0.32 21.31 ?  104 GLU   A HG3  1 
ATOM   2291 N  N    A ASP   A 1 105 ? 24.546 -6.427  -13.389 0.68 24.38 ?  105 ASP   A N    1 
ATOM   2292 N  N    B ASP   A 1 105 ? 24.740 -6.805  -13.560 0.32 19.56 ?  105 ASP   A N    1 
ATOM   2293 C  CA   A ASP   A 1 105 ? 24.052 -7.792  -13.544 0.68 25.34 ?  105 ASP   A CA   1 
ATOM   2294 C  CA   B ASP   A 1 105 ? 24.221 -8.169  -13.586 0.32 20.91 ?  105 ASP   A CA   1 
ATOM   2295 C  C    A ASP   A 1 105 ? 23.378 -8.271  -12.260 0.68 23.19 ?  105 ASP   A C    1 
ATOM   2296 C  C    B ASP   A 1 105 ? 23.500 -8.512  -12.288 0.32 20.81 ?  105 ASP   A C    1 
ATOM   2297 O  O    A ASP   A 1 105 ? 24.017 -8.353  -11.207 0.68 21.36 ?  105 ASP   A O    1 
ATOM   2298 O  O    B ASP   A 1 105 ? 24.107 -8.528  -11.214 0.32 19.95 ?  105 ASP   A O    1 
ATOM   2299 C  CB   A ASP   A 1 105 ? 25.227 -8.702  -13.900 0.68 28.45 ?  105 ASP   A CB   1 
ATOM   2300 C  CB   B ASP   A 1 105 ? 25.402 -9.116  -13.802 0.32 22.50 ?  105 ASP   A CB   1 
ATOM   2301 C  CG   A ASP   A 1 105 ? 24.804 -10.130 -14.156 0.68 31.13 ?  105 ASP   A CG   1 
ATOM   2302 C  CG   B ASP   A 1 105 ? 24.995 -10.579 -13.847 0.32 23.79 ?  105 ASP   A CG   1 
ATOM   2303 O  OD1  A ASP   A 1 105 ? 23.586 -10.376 -14.272 0.68 31.88 ?  105 ASP   A OD1  1 
ATOM   2304 O  OD1  B ASP   A 1 105 ? 23.783 -10.872 -13.908 0.32 23.91 ?  105 ASP   A OD1  1 
ATOM   2305 O  OD2  A ASP   A 1 105 ? 25.693 -11.004 -14.246 0.68 32.51 -1 105 ASP   A OD2  1 
ATOM   2306 O  OD2  B ASP   A 1 105 ? 25.904 -11.440 -13.814 0.32 24.72 -1 105 ASP   A OD2  1 
ATOM   2307 H  H    A ASP   A 1 105 ? 25.404 -6.378  -13.323 0.68 29.26 ?  105 ASP   A H    1 
ATOM   2308 H  H    B ASP   A 1 105 ? 25.583 -6.755  -13.702 0.32 23.47 ?  105 ASP   A H    1 
ATOM   2309 H  HA   A ASP   A 1 105 ? 23.407 -7.830  -14.267 0.68 30.42 ?  105 ASP   A HA   1 
ATOM   2310 H  HA   B ASP   A 1 105 ? 23.595 -8.264  -14.322 0.32 25.10 ?  105 ASP   A HA   1 
ATOM   2311 H  HB2  A ASP   A 1 105 ? 25.655 -8.373  -14.708 0.68 34.14 ?  105 ASP   A HB2  1 
ATOM   2312 H  HB2  B ASP   A 1 105 ? 25.837 -8.881  -14.638 0.32 27.00 ?  105 ASP   A HB2  1 
ATOM   2313 H  HB3  A ASP   A 1 105 ? 25.864 -8.704  -13.168 0.68 34.14 ?  105 ASP   A HB3  1 
ATOM   2314 H  HB3  B ASP   A 1 105 ? 26.021 -9.012  -13.065 0.32 27.00 ?  105 ASP   A HB3  1 
ATOM   2315 N  N    A ILE   A 1 106 ? 22.092 -8.619  -12.354 0.68 22.84 ?  106 ILE   A N    1 
ATOM   2316 N  N    B ILE   A 1 106 ? 22.202 -8.812  -12.394 0.32 21.49 ?  106 ILE   A N    1 
ATOM   2317 C  CA   A ILE   A 1 106 ? 21.338 -9.030  -11.174 0.68 22.16 ?  106 ILE   A CA   1 
ATOM   2318 C  CA   B ILE   A 1 106 ? 21.421 -9.162  -11.214 0.32 22.22 ?  106 ILE   A CA   1 
ATOM   2319 C  C    A ILE   A 1 106 ? 21.881 -10.317 -10.570 0.68 21.23 ?  106 ILE   A C    1 
ATOM   2320 C  C    B ILE   A 1 106 ? 21.930 -10.442 -10.570 0.32 22.28 ?  106 ILE   A C    1 
ATOM   2321 O  O    A ILE   A 1 106 ? 21.670 -10.572 -9.382  0.68 20.52 ?  106 ILE   A O    1 
ATOM   2322 O  O    B ILE   A 1 106 ? 21.716 -10.657 -9.372  0.32 22.17 ?  106 ILE   A O    1 
ATOM   2323 C  CB   A ILE   A 1 106 ? 19.830 -9.125  -11.504 0.68 23.50 ?  106 ILE   A CB   1 
ATOM   2324 C  CB   B ILE   A 1 106 ? 19.913 -9.240  -11.549 0.32 23.21 ?  106 ILE   A CB   1 
ATOM   2325 C  CG1  A ILE   A 1 106 ? 18.995 -9.201  -10.223 0.68 23.92 ?  106 ILE   A CG1  1 
ATOM   2326 C  CG1  B ILE   A 1 106 ? 19.074 -9.250  -10.268 0.32 23.71 ?  106 ILE   A CG1  1 
ATOM   2327 C  CG2  A ILE   A 1 106 ? 19.545 -10.331 -12.380 0.68 24.11 ?  106 ILE   A CG2  1 
ATOM   2328 C  CG2  B ILE   A 1 106 ? 19.608 -10.481 -12.362 0.32 23.50 ?  106 ILE   A CG2  1 
ATOM   2329 C  CD1  A ILE   A 1 106 ? 19.103 -7.973  -9.347  0.68 24.20 ?  106 ILE   A CD1  1 
ATOM   2330 C  CD1  B ILE   A 1 106 ? 19.264 -8.027  -9.398  0.32 23.96 ?  106 ILE   A CD1  1 
ATOM   2331 H  H    A ILE   A 1 106 ? 21.643 -8.618  -13.084 0.68 27.41 ?  106 ILE   A H    1 
ATOM   2332 H  H    B ILE   A 1 106 ? 21.762 -8.813  -13.130 0.32 25.80 ?  106 ILE   A H    1 
ATOM   2333 H  HA   A ILE   A 1 106 ? 21.447 -8.346  -10.504 0.68 26.59 ?  106 ILE   A HA   1 
ATOM   2334 H  HA   B ILE   A 1 106 ? 21.542 -8.458  -10.565 0.32 26.67 ?  106 ILE   A HA   1 
ATOM   2335 H  HB   A ILE   A 1 106 ? 19.574 -8.326  -11.990 0.68 28.20 ?  106 ILE   A HB   1 
ATOM   2336 H  HB   B ILE   A 1 106 ? 19.670 -8.459  -12.071 0.32 27.86 ?  106 ILE   A HB   1 
ATOM   2337 H  HG12 A ILE   A 1 106 ? 18.062 -9.307  -10.466 0.68 28.71 ?  106 ILE   A HG12 1 
ATOM   2338 H  HG12 B ILE   A 1 106 ? 18.136 -9.293  -10.510 0.32 28.46 ?  106 ILE   A HG12 1 
ATOM   2339 H  HG13 A ILE   A 1 106 ? 19.287 -9.964  -9.701  0.68 28.71 ?  106 ILE   A HG13 1 
ATOM   2340 H  HG13 B ILE   A 1 106 ? 19.314 -10.027 -9.742  0.32 28.46 ?  106 ILE   A HG13 1 
ATOM   2341 H  HG21 A ILE   A 1 106 ? 18.646 -10.253 -12.736 0.68 28.93 ?  106 ILE   A HG21 1 
ATOM   2342 H  HG21 B ILE   A 1 106 ? 18.722 -10.392 -12.748 0.32 28.20 ?  106 ILE   A HG21 1 
ATOM   2343 H  HG22 A ILE   A 1 106 ? 20.188 -10.350 -13.104 0.68 28.93 ?  106 ILE   A HG22 1 
ATOM   2344 H  HG22 B ILE   A 1 106 ? 20.270 -10.565 -13.063 0.32 28.20 ?  106 ILE   A HG22 1 
ATOM   2345 H  HG23 A ILE   A 1 106 ? 19.622 -11.135 -11.845 0.68 28.93 ?  106 ILE   A HG23 1 
ATOM   2346 H  HG23 B ILE   A 1 106 ? 19.639 -11.255 -11.779 0.32 28.20 ?  106 ILE   A HG23 1 
ATOM   2347 H  HD11 A ILE   A 1 106 ? 18.380 -7.981  -8.704  0.68 29.04 ?  106 ILE   A HD11 1 
ATOM   2348 H  HD11 B ILE   A 1 106 ? 18.520 -7.964  -8.781  0.32 28.76 ?  106 ILE   A HD11 1 
ATOM   2349 H  HD12 A ILE   A 1 106 ? 19.957 -7.987  -8.885  0.68 29.04 ?  106 ILE   A HD12 1 
ATOM   2350 H  HD12 B ILE   A 1 106 ? 20.096 -8.115  -8.906  0.32 28.76 ?  106 ILE   A HD12 1 
ATOM   2351 H  HD13 A ILE   A 1 106 ? 19.042 -7.181  -9.905  0.68 29.04 ?  106 ILE   A HD13 1 
ATOM   2352 H  HD13 B ILE   A 1 106 ? 19.294 -7.240  -9.964  0.32 28.76 ?  106 ILE   A HD13 1 
ATOM   2353 N  N    A GLN   A 1 107 ? 22.596 -11.129 -11.359 0.68 21.78 ?  107 GLN   A N    1 
ATOM   2354 N  N    B GLN   A 1 107 ? 22.612 -11.300 -11.335 0.32 22.57 ?  107 GLN   A N    1 
ATOM   2355 C  CA   A GLN   A 1 107 ? 23.200 -12.349 -10.828 0.68 23.91 ?  107 GLN   A CA   1 
ATOM   2356 C  CA   B GLN   A 1 107 ? 23.246 -12.470 -10.742 0.32 23.33 ?  107 GLN   A CA   1 
ATOM   2357 C  C    A GLN   A 1 107 ? 24.166 -12.044 -9.689  0.68 21.60 ?  107 GLN   A C    1 
ATOM   2358 C  C    B GLN   A 1 107 ? 24.248 -12.082 -9.665  0.32 21.06 ?  107 GLN   A C    1 
ATOM   2359 O  O    A GLN   A 1 107 ? 24.376 -12.882 -8.805  0.68 23.00 ?  107 GLN   A O    1 
ATOM   2360 O  O    B GLN   A 1 107 ? 24.574 -12.911 -8.808  0.32 21.77 ?  107 GLN   A O    1 
ATOM   2361 C  CB   A GLN   A 1 107 ? 23.904 -13.108 -11.958 0.68 28.05 ?  107 GLN   A CB   1 
ATOM   2362 C  CB   B GLN   A 1 107 ? 23.932 -13.305 -11.826 0.32 26.16 ?  107 GLN   A CB   1 
ATOM   2363 C  CG   A GLN   A 1 107 ? 23.036 -13.318 -13.196 0.68 32.40 ?  107 GLN   A CG   1 
ATOM   2364 C  CG   B GLN   A 1 107 ? 22.982 -13.838 -12.886 0.32 28.92 ?  107 GLN   A CG   1 
ATOM   2365 C  CD   A GLN   A 1 107 ? 21.752 -14.064 -12.887 0.68 35.89 ?  107 GLN   A CD   1 
ATOM   2366 C  CD   B GLN   A 1 107 ? 21.917 -14.748 -12.307 0.32 31.28 ?  107 GLN   A CD   1 
ATOM   2367 O  OE1  A GLN   A 1 107 ? 21.772 -15.127 -12.266 0.68 37.29 ?  107 GLN   A OE1  1 
ATOM   2368 O  OE1  B GLN   A 1 107 ? 22.185 -15.539 -11.402 0.32 32.12 ?  107 GLN   A OE1  1 
ATOM   2369 N  NE2  A GLN   A 1 107 ? 20.625 -13.507 -13.316 0.68 37.00 ?  107 GLN   A NE2  1 
ATOM   2370 N  NE2  B GLN   A 1 107 ? 20.697 -14.633 -12.821 0.32 31.97 ?  107 GLN   A NE2  1 
ATOM   2371 H  H    A GLN   A 1 107 ? 22.746 -10.994 -12.193 0.68 26.14 ?  107 GLN   A H    1 
ATOM   2372 H  H    B GLN   A 1 107 ? 22.721 -11.227 -12.185 0.32 27.09 ?  107 GLN   A H    1 
ATOM   2373 H  HA   A GLN   A 1 107 ? 22.510 -12.924 -10.475 0.68 28.69 ?  107 GLN   A HA   1 
ATOM   2374 H  HA   B GLN   A 1 107 ? 22.566 -13.022 -10.330 0.32 28.00 ?  107 GLN   A HA   1 
ATOM   2375 H  HB2  A GLN   A 1 107 ? 24.692 -12.611 -12.235 0.68 33.67 ?  107 GLN   A HB2  1 
ATOM   2376 H  HB2  B GLN   A 1 107 ? 24.596 -12.758 -12.273 0.32 31.40 ?  107 GLN   A HB2  1 
ATOM   2377 H  HB3  A GLN   A 1 107 ? 24.169 -13.985 -11.638 0.68 33.67 ?  107 GLN   A HB3  1 
ATOM   2378 H  HB3  B GLN   A 1 107 ? 24.363 -14.068 -11.409 0.32 31.40 ?  107 GLN   A HB3  1 
ATOM   2379 H  HG2  A GLN   A 1 107 ? 22.797 -12.456 -13.574 0.68 38.88 ?  107 GLN   A HG2  1 
ATOM   2380 H  HG2  B GLN   A 1 107 ? 22.539 -13.092 -13.319 0.32 34.70 ?  107 GLN   A HG2  1 
ATOM   2381 H  HG3  A GLN   A 1 107 ? 23.534 -13.834 -13.849 0.68 38.88 ?  107 GLN   A HG3  1 
ATOM   2382 H  HG3  B GLN   A 1 107 ? 23.488 -14.348 -13.539 0.32 34.70 ?  107 GLN   A HG3  1 
ATOM   2383 H  HE21 A GLN   A 1 107 ? 20.648 -12.763 -13.746 0.68 44.40 ?  107 GLN   A HE21 1 
ATOM   2384 H  HE21 B GLN   A 1 107 ? 20.548 -14.066 -13.451 0.32 38.37 ?  107 GLN   A HE21 1 
ATOM   2385 H  HE22 A GLN   A 1 107 ? 19.872 -13.893 -13.163 0.68 44.40 ?  107 GLN   A HE22 1 
ATOM   2386 H  HE22 B GLN   A 1 107 ? 20.057 -15.125 -12.525 0.32 38.37 ?  107 GLN   A HE22 1 
ATOM   2387 N  N    . LEU   A 1 108 ? 24.735 -10.838 -9.674  1.00 18.33 ?  108 LEU   A N    1 
ATOM   2388 C  CA   . LEU   A 1 108 ? 25.651 -10.412 -8.628  1.00 15.57 ?  108 LEU   A CA   1 
ATOM   2389 C  C    . LEU   A 1 108 ? 24.951 -10.231 -7.290  1.00 13.73 ?  108 LEU   A C    1 
ATOM   2390 O  O    . LEU   A 1 108 ? 25.630 -10.069 -6.275  1.00 14.13 ?  108 LEU   A O    1 
ATOM   2391 C  CB   . LEU   A 1 108 ? 26.374 -9.122  -9.043  1.00 15.57 ?  108 LEU   A CB   1 
ATOM   2392 C  CG   . LEU   A 1 108 ? 27.377 -9.325  -10.179 1.00 17.28 ?  108 LEU   A CG   1 
ATOM   2393 C  CD1  . LEU   A 1 108 ? 27.854 -7.994  -10.742 1.00 17.86 ?  108 LEU   A CD1  1 
ATOM   2394 C  CD2  . LEU   A 1 108 ? 28.567 -10.150 -9.709  1.00 19.06 ?  108 LEU   A CD2  1 
ATOM   2395 H  H    A LEU   A 1 108 ? 24.591 -10.235 -10.264 0.68 22.01 ?  108 LEU   A H    1 
ATOM   2396 H  H    B LEU   A 1 108 ? 24.560 -10.244 -10.264 0.32 22.01 ?  108 LEU   A H    1 
ATOM   2397 H  HA   . LEU   A 1 108 ? 26.324 -11.097 -8.504  1.00 18.69 ?  108 LEU   A HA   1 
ATOM   2398 H  HB2  . LEU   A 1 108 ? 25.714 -8.476  -9.343  1.00 18.69 ?  108 LEU   A HB2  1 
ATOM   2399 H  HB3  . LEU   A 1 108 ? 26.855 -8.771  -8.280  1.00 18.69 ?  108 LEU   A HB3  1 
ATOM   2400 H  HG   . LEU   A 1 108 ? 26.946 -9.814  -10.898 1.00 20.74 ?  108 LEU   A HG   1 
ATOM   2401 H  HD11 . LEU   A 1 108 ? 28.466 -8.163  -11.480 1.00 21.44 ?  108 LEU   A HD11 1 
ATOM   2402 H  HD12 . LEU   A 1 108 ? 27.089 -7.491  -11.058 1.00 21.44 ?  108 LEU   A HD12 1 
ATOM   2403 H  HD13 . LEU   A 1 108 ? 28.312 -7.500  -10.044 1.00 21.44 ?  108 LEU   A HD13 1 
ATOM   2404 H  HD21 . LEU   A 1 108 ? 29.263 -10.111 -10.380 1.00 22.88 ?  108 LEU   A HD21 1 
ATOM   2405 H  HD22 . LEU   A 1 108 ? 28.891 -9.783  -8.872  1.00 22.88 ?  108 LEU   A HD22 1 
ATOM   2406 H  HD23 . LEU   A 1 108 ? 28.282 -11.068 -9.578  1.00 22.88 ?  108 LEU   A HD23 1 
ATOM   2407 N  N    . LEU   A 1 109 ? 23.620 -10.285 -7.256  1.00 13.17 ?  109 LEU   A N    1 
ATOM   2408 C  CA   . LEU   A 1 109 ? 22.923 -10.157 -5.984  1.00 12.43 ?  109 LEU   A CA   1 
ATOM   2409 C  C    . LEU   A 1 109 ? 23.264 -11.312 -5.049  1.00 11.76 ?  109 LEU   A C    1 
ATOM   2410 O  O    . LEU   A 1 109 ? 23.399 -11.120 -3.835  1.00 12.12 ?  109 LEU   A O    1 
ATOM   2411 C  CB   . LEU   A 1 109 ? 21.420 -10.074 -6.237  1.00 13.26 ?  109 LEU   A CB   1 
ATOM   2412 C  CG   . LEU   A 1 109 ? 20.532 -9.790  -5.031  1.00 13.05 ?  109 LEU   A CG   1 
ATOM   2413 C  CD1  . LEU   A 1 109 ? 20.988 -8.534  -4.311  1.00 13.67 ?  109 LEU   A CD1  1 
ATOM   2414 C  CD2  . LEU   A 1 109 ? 19.080 -9.651  -5.471  1.00 14.22 ?  109 LEU   A CD2  1 
ATOM   2415 H  H    . LEU   A 1 109 ? 23.108 -10.385 -7.938  1.00 15.81 ?  109 LEU   A H    1 
ATOM   2416 H  HA   . LEU   A 1 109 ? 23.203 -9.330  -5.555  1.00 14.92 ?  109 LEU   A HA   1 
ATOM   2417 H  HB2  . LEU   A 1 109 ? 21.260 -9.363  -6.880  1.00 15.92 ?  109 LEU   A HB2  1 
ATOM   2418 H  HB3  . LEU   A 1 109 ? 21.128 -10.916 -6.611  1.00 15.92 ?  109 LEU   A HB3  1 
ATOM   2419 H  HG   . LEU   A 1 109 ? 20.587 -10.528 -4.409  1.00 15.67 ?  109 LEU   A HG   1 
ATOM   2420 H  HD11 . LEU   A 1 109 ? 20.298 -8.245  -3.695  1.00 16.41 ?  109 LEU   A HD11 1 
ATOM   2421 H  HD12 . LEU   A 1 109 ? 21.807 -8.721  -3.828  1.00 16.41 ?  109 LEU   A HD12 1 
ATOM   2422 H  HD13 . LEU   A 1 109 ? 21.150 -7.832  -4.970  1.00 16.41 ?  109 LEU   A HD13 1 
ATOM   2423 H  HD21 . LEU   A 1 109 ? 18.543 -9.370  -4.712  1.00 17.07 ?  109 LEU   A HD21 1 
ATOM   2424 H  HD22 . LEU   A 1 109 ? 19.022 -8.989  -6.178  1.00 17.07 ?  109 LEU   A HD22 1 
ATOM   2425 H  HD23 . LEU   A 1 109 ? 18.765 -10.509 -5.798  1.00 17.07 ?  109 LEU   A HD23 1 
ATOM   2426 N  N    . LYS   A 1 110 ? 23.401 -12.525 -5.587  1.00 11.73 ?  110 LYS   A N    1 
ATOM   2427 C  CA   . LYS   A 1 110 ? 23.781 -13.646 -4.736  1.00 11.84 ?  110 LYS   A CA   1 
ATOM   2428 C  C    . LYS   A 1 110 ? 25.160 -13.423 -4.127  1.00 11.17 ?  110 LYS   A C    1 
ATOM   2429 O  O    . LYS   A 1 110 ? 25.353 -13.619 -2.926  1.00 11.51 ?  110 LYS   A O    1 
ATOM   2430 C  CB   . LYS   A 1 110 ? 23.709 -14.969 -5.502  1.00 12.47 ?  110 LYS   A CB   1 
ATOM   2431 C  CG   . LYS   A 1 110 ? 23.906 -16.180 -4.593  1.00 12.76 ?  110 LYS   A CG   1 
ATOM   2432 C  CD   . LYS   A 1 110 ? 23.672 -17.506 -5.302  1.00 13.33 ?  110 LYS   A CD   1 
ATOM   2433 C  CE   . LYS   A 1 110 ? 23.781 -18.680 -4.340  1.00 14.06 ?  110 LYS   A CE   1 
ATOM   2434 N  NZ   . LYS   A 1 110 ? 22.593 -18.808 -3.463  1.00 14.58 ?  110 LYS   A NZ   1 
ATOM   2435 H  H    . LYS   A 1 110 ? 23.285 -12.717 -6.413  1.00 14.08 ?  110 LYS   A H    1 
ATOM   2436 H  HA   . LYS   A 1 110 ? 23.142 -13.703 -4.003  1.00 14.21 ?  110 LYS   A HA   1 
ATOM   2437 H  HB2  . LYS   A 1 110 ? 22.836 -15.048 -5.921  1.00 14.97 ?  110 LYS   A HB2  1 
ATOM   2438 H  HB3  . LYS   A 1 110 ? 24.404 -14.983 -6.175  1.00 14.97 ?  110 LYS   A HB3  1 
ATOM   2439 H  HG2  . LYS   A 1 110 ? 24.814 -16.176 -4.252  1.00 15.32 ?  110 LYS   A HG2  1 
ATOM   2440 H  HG3  . LYS   A 1 110 ? 23.279 -16.125 -3.853  1.00 15.32 ?  110 LYS   A HG3  1 
ATOM   2441 H  HD2  . LYS   A 1 110 ? 22.788 -17.513 -5.687  1.00 16.00 ?  110 LYS   A HD2  1 
ATOM   2442 H  HD3  . LYS   A 1 110 ? 24.347 -17.619 -5.991  1.00 16.00 ?  110 LYS   A HD3  1 
ATOM   2443 H  HE2  . LYS   A 1 110 ? 23.873 -19.502 -4.845  1.00 16.87 ?  110 LYS   A HE2  1 
ATOM   2444 H  HE3  . LYS   A 1 110 ? 24.561 -18.556 -3.768  1.00 16.87 ?  110 LYS   A HE3  1 
ATOM   2445 H  HZ1  . LYS   A 1 110 ? 22.684 -19.497 -2.916  1.00 17.50 ?  110 LYS   A HZ1  1 
ATOM   2446 H  HZ2  . LYS   A 1 110 ? 22.490 -18.063 -2.981  1.00 17.50 ?  110 LYS   A HZ2  1 
ATOM   2447 H  HZ3  . LYS   A 1 110 ? 21.862 -18.924 -3.963  1.00 17.50 ?  110 LYS   A HZ3  1 
ATOM   2448 N  N    . SER   A 1 111 ? 26.124 -12.984 -4.942  1.00 11.45 ?  111 SER   A N    1 
ATOM   2449 C  CA   . SER   A 1 111 ? 27.455 -12.673 -4.426  1.00 11.56 ?  111 SER   A CA   1 
ATOM   2450 C  C    . SER   A 1 111 ? 27.383 -11.624 -3.321  1.00 11.35 ?  111 SER   A C    1 
ATOM   2451 O  O    . SER   A 1 111 ? 28.079 -11.724 -2.304  1.00 11.93 ?  111 SER   A O    1 
ATOM   2452 C  CB   . SER   A 1 111 ? 28.343 -12.178 -5.568  1.00 12.85 ?  111 SER   A CB   1 
ATOM   2453 O  OG   . SER   A 1 111 ? 28.430 -13.165 -6.587  1.00 14.82 ?  111 SER   A OG   1 
ATOM   2454 H  H    . SER   A 1 111 ? 26.024 -12.861 -5.786  1.00 13.75 ?  111 SER   A H    1 
ATOM   2455 H  HA   . SER   A 1 111 ? 27.848 -13.481 -4.058  1.00 13.88 ?  111 SER   A HA   1 
ATOM   2456 H  HB2  . SER   A 1 111 ? 27.950 -11.375 -5.945  1.00 15.43 ?  111 SER   A HB2  1 
ATOM   2457 H  HB3  . SER   A 1 111 ? 29.225 -11.990 -5.222  1.00 15.43 ?  111 SER   A HB3  1 
ATOM   2458 H  HG   . SER   A 1 111 ? 28.931 -12.883 -7.210  1.00 17.78 ?  111 SER   A HG   1 
ATOM   2459 N  N    . ALA   A 1 112 ? 26.536 -10.609 -3.501  1.00 11.19 ?  112 ALA   A N    1 
ATOM   2460 C  CA   . ALA   A 1 112 ? 26.390 -9.573  -2.482  1.00 11.40 ?  112 ALA   A CA   1 
ATOM   2461 C  C    . ALA   A 1 112 ? 25.908 -10.172 -1.162  1.00 11.10 ?  112 ALA   A C    1 
ATOM   2462 O  O    . ALA   A 1 112 ? 26.456 -9.879  -0.093  1.00 11.30 ?  112 ALA   A O    1 
ATOM   2463 C  CB   . ALA   A 1 112 ? 25.434 -8.486  -2.977  1.00 12.06 ?  112 ALA   A CB   1 
ATOM   2464 H  H    . ALA   A 1 112 ? 26.045 -10.497 -4.195  1.00 13.43 ?  112 ALA   A H    1 
ATOM   2465 H  HA   . ALA   A 1 112 ? 27.255 -9.157  -2.325  1.00 13.68 ?  112 ALA   A HA   1 
ATOM   2466 H  HB1  . ALA   A 1 112 ? 25.364 -7.792  -2.295  1.00 14.48 ?  112 ALA   A HB1  1 
ATOM   2467 H  HB2  . ALA   A 1 112 ? 25.782 -8.102  -3.796  1.00 14.48 ?  112 ALA   A HB2  1 
ATOM   2468 H  HB3  . ALA   A 1 112 ? 24.562 -8.877  -3.136  1.00 14.48 ?  112 ALA   A HB3  1 
ATOM   2469 N  N    . TYR   A 1 113 ? 24.871 -11.009 -1.215  1.00 11.14 ?  113 TYR   A N    1 
ATOM   2470 C  CA   . TYR   A 1 113 ? 24.362 -11.619 0.010   1.00 10.91 ?  113 TYR   A CA   1 
ATOM   2471 C  C    . TYR   A 1 113 ? 25.366 -12.570 0.656   1.00 10.65 ?  113 TYR   A C    1 
ATOM   2472 O  O    . TYR   A 1 113 ? 25.324 -12.755 1.875   1.00 11.30 ?  113 TYR   A O    1 
ATOM   2473 C  CB   . TYR   A 1 113 ? 23.041 -12.340 -0.263  1.00 11.13 ?  113 TYR   A CB   1 
ATOM   2474 C  CG   . TYR   A 1 113 ? 21.828 -11.443 -0.180  1.00 11.16 ?  113 TYR   A CG   1 
ATOM   2475 C  CD1  . TYR   A 1 113 ? 21.468 -10.842 1.022   1.00 11.39 ?  113 TYR   A CD1  1 
ATOM   2476 C  CD2  . TYR   A 1 113 ? 21.023 -11.218 -1.291  1.00 11.19 ?  113 TYR   A CD2  1 
ATOM   2477 C  CE1  . TYR   A 1 113 ? 20.346 -10.044 1.116   1.00 11.57 ?  113 TYR   A CE1  1 
ATOM   2478 C  CE2  . TYR   A 1 113 ? 19.876 -10.413 -1.204  1.00 11.49 ?  113 TYR   A CE2  1 
ATOM   2479 C  CZ   . TYR   A 1 113 ? 19.550 -9.835  0.007   1.00 11.50 ?  113 TYR   A CZ   1 
ATOM   2480 O  OH   . TYR   A 1 113 ? 18.427 -9.044  0.135   1.00 11.83 ?  113 TYR   A OH   1 
ATOM   2481 H  H    . TYR   A 1 113 ? 24.457 -11.231 -1.934  1.00 13.37 ?  113 TYR   A H    1 
ATOM   2482 H  HA   . TYR   A 1 113 ? 24.184 -10.915 0.650   1.00 13.10 ?  113 TYR   A HA   1 
ATOM   2483 H  HB2  . TYR   A 1 113 ? 23.066 -12.715 -1.156  1.00 13.36 ?  113 TYR   A HB2  1 
ATOM   2484 H  HB3  . TYR   A 1 113 ? 22.930 -13.048 0.389   1.00 13.36 ?  113 TYR   A HB3  1 
ATOM   2485 H  HD1  . TYR   A 1 113 ? 21.991 -10.988 1.776   1.00 13.67 ?  113 TYR   A HD1  1 
ATOM   2486 H  HD2  . TYR   A 1 113 ? 21.236 -11.619 -2.101  1.00 13.44 ?  113 TYR   A HD2  1 
ATOM   2487 H  HE1  . TYR   A 1 113 ? 20.122 -9.657  1.930   1.00 13.89 ?  113 TYR   A HE1  1 
ATOM   2488 H  HE2  . TYR   A 1 113 ? 19.335 -10.267 -1.948  1.00 13.80 ?  113 TYR   A HE2  1 
ATOM   2489 H  HH   . TYR   A 1 113 ? 18.036 -8.996  -0.611  1.00 14.20 ?  113 TYR   A HH   1 
ATOM   2490 N  N    . GLU   A 1 114 ? 26.269 -13.182 -0.125  1.00 11.05 ?  114 GLU   A N    1 
ATOM   2491 C  CA   . GLU   A 1 114 ? 27.257 -14.080 0.471   1.00 11.16 ?  114 GLU   A CA   1 
ATOM   2492 C  C    . GLU   A 1 114 ? 28.103 -13.371 1.522   1.00 11.19 ?  114 GLU   A C    1 
ATOM   2493 O  O    . GLU   A 1 114 ? 28.576 -14.009 2.470   1.00 11.54 ?  114 GLU   A O    1 
ATOM   2494 C  CB   . GLU   A 1 114 ? 28.130 -14.724 -0.614  1.00 11.32 ?  114 GLU   A CB   1 
ATOM   2495 C  CG   . GLU   A 1 114 ? 27.363 -15.769 -1.401  1.00 11.84 ?  114 GLU   A CG   1 
ATOM   2496 C  CD   . GLU   A 1 114 ? 28.073 -16.305 -2.634  1.00 12.13 ?  114 GLU   A CD   1 
ATOM   2497 O  OE1  . GLU   A 1 114 ? 29.024 -15.678 -3.139  1.00 12.30 ?  114 GLU   A OE1  1 
ATOM   2498 O  OE2  . GLU   A 1 114 ? 27.634 -17.367 -3.118  1.00 13.33 -1 114 GLU   A OE2  1 
ATOM   2499 H  H    . GLU   A 1 114 ? 26.329 -13.084 -0.984  1.00 13.26 ?  114 GLU   A H    1 
ATOM   2500 H  HA   . GLU   A 1 114 ? 26.780 -14.792 0.917   1.00 13.40 ?  114 GLU   A HA   1 
ATOM   2501 H  HB2  . GLU   A 1 114 ? 28.427 -14.042 -1.237  1.00 13.59 ?  114 GLU   A HB2  1 
ATOM   2502 H  HB3  . GLU   A 1 114 ? 28.886 -15.160 -0.201  1.00 13.59 ?  114 GLU   A HB3  1 
ATOM   2503 H  HG2  . GLU   A 1 114 ? 27.181 -16.524 -0.823  1.00 14.21 ?  114 GLU   A HG2  1 
ATOM   2504 H  HG3  . GLU   A 1 114 ? 26.519 -15.381 -1.697  1.00 14.21 ?  114 GLU   A HG3  1 
ATOM   2505 N  N    . ASN   A 1 115 ? 28.288 -12.053 1.391   1.00 10.95 ?  115 ASN   A N    1 
ATOM   2506 C  CA   . ASN   A 1 115 ? 29.057 -11.324 2.395   1.00 11.25 ?  115 ASN   A CA   1 
ATOM   2507 C  C    . ASN   A 1 115 ? 28.439 -11.456 3.780   1.00 11.12 ?  115 ASN   A C    1 
ATOM   2508 O  O    . ASN   A 1 115 ? 29.150 -11.384 4.789   1.00 11.58 ?  115 ASN   A O    1 
ATOM   2509 C  CB   . ASN   A 1 115 ? 29.168 -9.849  2.015   1.00 11.59 ?  115 ASN   A CB   1 
ATOM   2510 C  CG   . ASN   A 1 115 ? 29.960 -9.636  0.753   1.00 12.31 ?  115 ASN   A CG   1 
ATOM   2511 O  OD1  . ASN   A 1 115 ? 31.179 -9.736  0.766   1.00 15.42 ?  115 ASN   A OD1  1 
ATOM   2512 N  ND2  . ASN   A 1 115 ? 29.282 -9.333  -0.338  1.00 11.93 ?  115 ASN   A ND2  1 
ATOM   2513 H  H    . ASN   A 1 115 ? 27.975 -11.567 0.748   1.00 13.14 ?  115 ASN   A H    1 
ATOM   2514 H  HA   . ASN   A 1 115 ? 29.948 -11.694 2.433   1.00 13.50 ?  115 ASN   A HA   1 
ATOM   2515 H  HB2  . ASN   A 1 115 ? 28.277 -9.487  1.887   1.00 13.92 ?  115 ASN   A HB2  1 
ATOM   2516 H  HB3  . ASN   A 1 115 ? 29.614 -9.375  2.739   1.00 13.92 ?  115 ASN   A HB3  1 
ATOM   2517 H  HD21 . ASN   A 1 115 ? 29.692 -9.201  -1.080  1.00 14.32 ?  115 ASN   A HD21 1 
ATOM   2518 H  HD22 . ASN   A 1 115 ? 28.421 -9.288  -0.309  1.00 14.32 ?  115 ASN   A HD22 1 
ATOM   2519 N  N    . PHE   A 1 116 ? 27.112 -11.630 3.856   1.00 11.15 ?  116 PHE   A N    1 
ATOM   2520 C  CA   . PHE   A 1 116 ? 26.457 -11.719 5.158   1.00 11.16 ?  116 PHE   A CA   1 
ATOM   2521 C  C    . PHE   A 1 116 ? 26.929 -12.949 5.933   1.00 11.42 ?  116 PHE   A C    1 
ATOM   2522 O  O    . PHE   A 1 116 ? 26.856 -12.968 7.164   1.00 12.04 ?  116 PHE   A O    1 
ATOM   2523 C  CB   . PHE   A 1 116 ? 24.928 -11.846 5.021   1.00 11.26 ?  116 PHE   A CB   1 
ATOM   2524 C  CG   . PHE   A 1 116 ? 24.177 -10.601 4.553   1.00 10.84 ?  116 PHE   A CG   1 
ATOM   2525 C  CD1  . PHE   A 1 116 ? 24.755 -9.578  3.806   1.00 10.93 ?  116 PHE   A CD1  1 
ATOM   2526 C  CD2  . PHE   A 1 116 ? 22.826 -10.498 4.868   1.00 11.49 ?  116 PHE   A CD2  1 
ATOM   2527 C  CE1  . PHE   A 1 116 ? 23.990 -8.502  3.383   1.00 11.32 ?  116 PHE   A CE1  1 
ATOM   2528 C  CE2  . PHE   A 1 116 ? 22.067 -9.426  4.457   1.00 11.53 ?  116 PHE   A CE2  1 
ATOM   2529 C  CZ   . PHE   A 1 116 ? 22.640 -8.427  3.714   1.00 11.19 ?  116 PHE   A CZ   1 
ATOM   2530 H  H    . PHE   A 1 116 ? 26.579 -11.682 3.180   1.00 13.38 ?  116 PHE   A H    1 
ATOM   2531 H  HA   . PHE   A 1 116 ? 26.651 -10.926 5.682   1.00 13.40 ?  116 PHE   A HA   1 
ATOM   2532 H  HB2  . PHE   A 1 116 ? 24.741 -12.557 4.383   1.00 13.52 ?  116 PHE   A HB2  1 
ATOM   2533 H  HB3  . PHE   A 1 116 ? 24.567 -12.096 5.887   1.00 13.52 ?  116 PHE   A HB3  1 
ATOM   2534 H  HD1  . PHE   A 1 116 ? 25.649 -9.642  3.573   1.00 13.12 ?  116 PHE   A HD1  1 
ATOM   2535 H  HD2  . PHE   A 1 116 ? 22.417 -11.182 5.363   1.00 13.79 ?  116 PHE   A HD2  1 
ATOM   2536 H  HE1  . PHE   A 1 116 ? 24.386 -7.827  2.887   1.00 13.59 ?  116 PHE   A HE1  1 
ATOM   2537 H  HE2  . PHE   A 1 116 ? 21.163 -9.385  4.685   1.00 13.85 ?  116 PHE   A HE2  1 
ATOM   2538 H  HZ   . PHE   A 1 116 ? 22.130 -7.696  3.445   1.00 13.43 ?  116 PHE   A HZ   1 
ATOM   2539 N  N    . ASN   A 1 117 ? 27.374 -13.999 5.231   1.00 11.74 ?  117 ASN   A N    1 
ATOM   2540 C  CA   . ASN   A 1 117 ? 27.743 -15.244 5.898   1.00 11.86 ?  117 ASN   A CA   1 
ATOM   2541 C  C    . ASN   A 1 117 ? 29.001 -15.124 6.735   1.00 12.25 ?  117 ASN   A C    1 
ATOM   2542 O  O    . ASN   A 1 117 ? 29.298 -16.046 7.505   1.00 13.14 ?  117 ASN   A O    1 
ATOM   2543 C  CB   . ASN   A 1 117 ? 27.865 -16.367 4.877   1.00 12.03 ?  117 ASN   A CB   1 
ATOM   2544 C  CG   . ASN   A 1 117 ? 26.512 -16.753 4.334   1.00 12.00 ?  117 ASN   A CG   1 
ATOM   2545 O  OD1  . ASN   A 1 117 ? 25.535 -16.781 5.081   1.00 12.91 ?  117 ASN   A OD1  1 
ATOM   2546 N  ND2  . ASN   A 1 117 ? 26.430 -17.016 3.045   1.00 12.02 ?  117 ASN   A ND2  1 
ATOM   2547 H  H    . ASN   A 1 117 ? 27.450 -14.014 4.370   1.00 14.09 ?  117 ASN   A H    1 
ATOM   2548 H  HA   . ASN   A 1 117 ? 27.018 -15.481 6.498   1.00 14.23 ?  117 ASN   A HA   1 
ATOM   2549 H  HB2  . ASN   A 1 117 ? 28.416 -16.070 4.136   1.00 14.44 ?  117 ASN   A HB2  1 
ATOM   2550 H  HB3  . ASN   A 1 117 ? 28.253 -17.142 5.302   1.00 14.44 ?  117 ASN   A HB3  1 
ATOM   2551 H  HD21 . ASN   A 1 117 ? 25.676 -17.232 2.702   1.00 14.43 ?  117 ASN   A HD21 1 
ATOM   2552 H  HD22 . ASN   A 1 117 ? 27.136 -16.973 2.557   1.00 14.43 ?  117 ASN   A HD22 1 
ATOM   2553 N  N    . GLN   A 1 118 ? 29.732 -14.016 6.614   1.00 12.13 ?  118 GLN   A N    1 
ATOM   2554 C  CA   . GLN   A 1 118 ? 30.906 -13.780 7.439   1.00 12.86 ?  118 GLN   A CA   1 
ATOM   2555 C  C    . GLN   A 1 118 ? 30.559 -13.206 8.806   1.00 13.00 ?  118 GLN   A C    1 
ATOM   2556 O  O    . GLN   A 1 118 ? 31.474 -12.916 9.588   1.00 14.43 ?  118 GLN   A O    1 
ATOM   2557 C  CB   . GLN   A 1 118 ? 31.900 -12.872 6.706   1.00 13.11 ?  118 GLN   A CB   1 
ATOM   2558 C  CG   . GLN   A 1 118 ? 32.371 -13.451 5.382   1.00 13.02 ?  118 GLN   A CG   1 
ATOM   2559 C  CD   . GLN   A 1 118 ? 33.204 -14.715 5.558   1.00 13.32 ?  118 GLN   A CD   1 
ATOM   2560 O  OE1  . GLN   A 1 118 ? 34.070 -14.788 6.443   1.00 14.05 ?  118 GLN   A OE1  1 
ATOM   2561 N  NE2  . GLN   A 1 118 ? 32.959 -15.713 4.707   1.00 13.64 ?  118 GLN   A NE2  1 
ATOM   2562 H  H    . GLN   A 1 118 ? 29.558 -13.376 6.056   1.00 14.56 ?  118 GLN   A H    1 
ATOM   2563 H  HA   . GLN   A 1 118 ? 31.340 -14.633 7.585   1.00 15.43 ?  118 GLN   A HA   1 
ATOM   2564 H  HB2  . GLN   A 1 118 ? 31.479 -12.018 6.532   1.00 15.74 ?  118 GLN   A HB2  1 
ATOM   2565 H  HB3  . GLN   A 1 118 ? 32.681 -12.749 7.272   1.00 15.74 ?  118 GLN   A HB3  1 
ATOM   2566 H  HG2  . GLN   A 1 118 ? 31.598 -13.668 4.835   1.00 15.63 ?  118 GLN   A HG2  1 
ATOM   2567 H  HG3  . GLN   A 1 118 ? 32.920 -12.791 4.925   1.00 15.63 ?  118 GLN   A HG3  1 
ATOM   2568 H  HE21 . GLN   A 1 118 ? 32.346 -15.625 4.099   1.00 16.37 ?  118 GLN   A HE21 1 
ATOM   2569 H  HE22 . GLN   A 1 118 ? 33.398 -16.447 4.760   1.00 16.37 ?  118 GLN   A HE22 1 
ATOM   2570 N  N    . HIS   A 1 119 ? 29.268 -13.046 9.111   1.00 12.53 ?  119 HIS   A N    1 
ATOM   2571 C  CA   . HIS   A 1 119 ? 28.814 -12.439 10.356  1.00 13.09 ?  119 HIS   A CA   1 
ATOM   2572 C  C    . HIS   A 1 119 ? 27.674 -13.260 10.932  1.00 13.32 ?  119 HIS   A C    1 
ATOM   2573 O  O    . HIS   A 1 119 ? 26.730 -13.601 10.215  1.00 13.63 ?  119 HIS   A O    1 
ATOM   2574 C  CB   . HIS   A 1 119 ? 28.357 -11.007 10.081  1.00 13.51 ?  119 HIS   A CB   1 
ATOM   2575 C  CG   . HIS   A 1 119 ? 29.438 -10.193 9.474   1.00 14.86 ?  119 HIS   A CG   1 
ATOM   2576 N  ND1  . HIS   A 1 119 ? 30.406 -9.579  10.235  1.00 17.08 ?  119 HIS   A ND1  1 
ATOM   2577 C  CD2  . HIS   A 1 119 ? 29.786 -10.002 8.182   1.00 16.01 ?  119 HIS   A CD2  1 
ATOM   2578 C  CE1  . HIS   A 1 119 ? 31.276 -8.993  9.433   1.00 17.37 ?  119 HIS   A CE1  1 
ATOM   2579 N  NE2  . HIS   A 1 119 ? 30.932 -9.244  8.183   1.00 17.18 ?  119 HIS   A NE2  1 
ATOM   2580 H  H    . HIS   A 1 119 ? 28.619 -13.302 8.600   1.00 15.04 ?  119 HIS   A H    1 
ATOM   2581 H  HA   . HIS   A 1 119 ? 29.541 -12.425 10.994  1.00 15.71 ?  119 HIS   A HA   1 
ATOM   2582 H  HB2  . HIS   A 1 119 ? 27.604 -11.029 9.466   1.00 16.22 ?  119 HIS   A HB2  1 
ATOM   2583 H  HB3  . HIS   A 1 119 ? 28.094 -10.596 10.917  1.00 16.22 ?  119 HIS   A HB3  1 
ATOM   2584 H  HD2  . HIS   A 1 119 ? 29.335 -10.318 7.430   1.00 19.21 ?  119 HIS   A HD2  1 
ATOM   2585 H  HE1  . HIS   A 1 119 ? 32.011 -8.492  9.704   1.00 20.85 ?  119 HIS   A HE1  1 
ATOM   2586 H  HE2  . HIS   A 1 119 ? 31.343 -8.954  7.483   1.00 20.62 ?  119 HIS   A HE2  1 
ATOM   2587 N  N    . GLU   A 1 120 ? 27.753 -13.559 12.230  1.00 14.07 ?  120 GLU   A N    1 
ATOM   2588 C  CA   . GLU   A 1 120 ? 26.795 -14.486 12.829  1.00 16.39 ?  120 GLU   A CA   1 
ATOM   2589 C  C    . GLU   A 1 120 ? 25.379 -13.922 12.879  1.00 14.83 ?  120 GLU   A C    1 
ATOM   2590 O  O    . GLU   A 1 120 ? 24.409 -14.687 12.768  1.00 14.92 ?  120 GLU   A O    1 
ATOM   2591 C  CB   . GLU   A 1 120 ? 27.257 -14.881 14.231  1.00 21.76 ?  120 GLU   A CB   1 
ATOM   2592 C  CG   . GLU   A 1 120 ? 28.477 -15.790 14.248  1.00 29.48 ?  120 GLU   A CG   1 
ATOM   2593 C  CD   . GLU   A 1 120 ? 28.631 -16.534 15.558  1.00 36.27 ?  120 GLU   A CD   1 
ATOM   2594 O  OE1  . GLU   A 1 120 ? 28.239 -15.981 16.608  1.00 38.04 ?  120 GLU   A OE1  1 
ATOM   2595 O  OE2  . GLU   A 1 120 ? 29.142 -17.674 15.537  1.00 40.50 -1 120 GLU   A OE2  1 
ATOM   2596 H  H    . GLU   A 1 120 ? 28.347 -13.246 12.773  1.00 16.89 ?  120 GLU   A H    1 
ATOM   2597 H  HA   . GLU   A 1 120 ? 26.775 -15.294 12.298  1.00 19.67 ?  120 GLU   A HA   1 
ATOM   2598 H  HB2  . GLU   A 1 120 ? 27.488 -14.084 14.733  1.00 26.12 ?  120 GLU   A HB2  1 
ATOM   2599 H  HB3  . GLU   A 1 120 ? 26.539 -15.355 14.683  1.00 26.12 ?  120 GLU   A HB3  1 
ATOM   2600 H  HG2  . GLU   A 1 120 ? 28.402 -16.440 13.531  1.00 35.38 ?  120 GLU   A HG2  1 
ATOM   2601 H  HG3  . GLU   A 1 120 ? 29.278 -15.259 14.135  1.00 35.38 ?  120 GLU   A HG3  1 
ATOM   2602 N  N    . VAL   A 1 121 ? 25.243 -12.613 13.092  1.00 14.06 ?  121 VAL   A N    1 
ATOM   2603 C  CA   . VAL   A 1 121 ? 23.949 -11.947 13.207  1.00 14.02 ?  121 VAL   A CA   1 
ATOM   2604 C  C    . VAL   A 1 121 ? 24.061 -10.568 12.567  1.00 12.76 ?  121 VAL   A C    1 
ATOM   2605 O  O    . VAL   A 1 121 ? 25.029 -9.840  12.814  1.00 13.53 ?  121 VAL   A O    1 
ATOM   2606 C  CB   . VAL   A 1 121 ? 23.508 -11.796 14.682  1.00 16.97 ?  121 VAL   A CB   1 
ATOM   2607 C  CG1  . VAL   A 1 121 ? 22.111 -11.188 14.765  1.00 17.47 ?  121 VAL   A CG1  1 
ATOM   2608 C  CG2  . VAL   A 1 121 ? 23.545 -13.120 15.423  1.00 19.08 ?  121 VAL   A CG2  1 
ATOM   2609 H  H    . VAL   A 1 121 ? 25.909 -12.071 13.177  1.00 16.88 ?  121 VAL   A H    1 
ATOM   2610 H  HA   . VAL   A 1 121 ? 23.276 -12.464 12.735  1.00 16.83 ?  121 VAL   A HA   1 
ATOM   2611 H  HB   . VAL   A 1 121 ? 24.117 -11.192 15.129  1.00 20.36 ?  121 VAL   A HB   1 
ATOM   2612 H  HG11 . VAL   A 1 121 ? 21.800 -11.237 15.685  1.00 20.97 ?  121 VAL   A HG11 1 
ATOM   2613 H  HG12 . VAL   A 1 121 ? 22.147 -10.263 14.480  1.00 20.97 ?  121 VAL   A HG12 1 
ATOM   2614 H  HG13 . VAL   A 1 121 ? 21.511 -11.691 14.191  1.00 20.97 ?  121 VAL   A HG13 1 
ATOM   2615 H  HG21 . VAL   A 1 121 ? 23.192 -12.992 16.323  1.00 22.90 ?  121 VAL   A HG21 1 
ATOM   2616 H  HG22 . VAL   A 1 121 ? 22.995 -13.767 14.950  1.00 22.90 ?  121 VAL   A HG22 1 
ATOM   2617 H  HG23 . VAL   A 1 121 ? 24.458 -13.435 15.472  1.00 22.90 ?  121 VAL   A HG23 1 
ATOM   2618 N  N    . LEU   A 1 122 ? 23.051 -10.186 11.780  1.00 12.15 ?  122 LEU   A N    1 
ATOM   2619 C  CA   . LEU   A 1 122 ? 23.056 -8.891  11.105  1.00 11.94 ?  122 LEU   A CA   1 
ATOM   2620 C  C    . LEU   A 1 122 ? 21.658 -8.302  11.068  1.00 11.92 ?  122 LEU   A C    1 
ATOM   2621 O  O    . LEU   A 1 122 ? 20.671 -9.024  10.932  1.00 12.94 ?  122 LEU   A O    1 
ATOM   2622 C  CB   . LEU   A 1 122 ? 23.490 -8.988  9.639   1.00 13.22 ?  122 LEU   A CB   1 
ATOM   2623 C  CG   . LEU   A 1 122 ? 24.702 -9.841  9.294   1.00 13.36 ?  122 LEU   A CG   1 
ATOM   2624 C  CD1  . LEU   A 1 122 ? 24.300 -11.287 9.065   1.00 14.30 ?  122 LEU   A CD1  1 
ATOM   2625 C  CD2  . LEU   A 1 122 ? 25.395 -9.282  8.070   1.00 13.01 ?  122 LEU   A CD2  1 
ATOM   2626 H  H    . LEU   A 1 122 ? 22.346 -10.659 11.622  1.00 14.59 ?  122 LEU   A H    1 
ATOM   2627 H  HA   . LEU   A 1 122 ? 23.647 -8.277  11.569  1.00 14.34 ?  122 LEU   A HA   1 
ATOM   2628 H  HB2  . LEU   A 1 122 ? 22.754 -9.351  9.133   1.00 15.87 ?  122 LEU   A HB2  1 
ATOM   2629 H  HB3  . LEU   A 1 122 ? 23.691 -8.097  9.327   1.00 15.87 ?  122 LEU   A HB3  1 
ATOM   2630 H  HG   . LEU   A 1 122 ? 25.343 -9.824  10.027  1.00 16.04 ?  122 LEU   A HG   1 
ATOM   2631 H  HD11 . LEU   A 1 122 ? 25.080 -11.805 8.806   1.00 17.17 ?  122 LEU   A HD11 1 
ATOM   2632 H  HD12 . LEU   A 1 122 ? 23.928 -11.647 9.887   1.00 17.17 ?  122 LEU   A HD12 1 
ATOM   2633 H  HD13 . LEU   A 1 122 ? 23.634 -11.323 8.360   1.00 17.17 ?  122 LEU   A HD13 1 
ATOM   2634 H  HD21 . LEU   A 1 122 ? 26.145 -9.858  7.828   1.00 15.62 ?  122 LEU   A HD21 1 
ATOM   2635 H  HD22 . LEU   A 1 122 ? 24.765 -9.245  7.335   1.00 15.62 ?  122 LEU   A HD22 1 
ATOM   2636 H  HD23 . LEU   A 1 122 ? 25.726 -8.390  8.269   1.00 15.62 ?  122 LEU   A HD23 1 
ATOM   2637 N  N    . LEU   A 1 123 ? 21.594 -6.974  11.160  1.00 11.63 ?  123 LEU   A N    1 
ATOM   2638 C  CA   . LEU   A 1 123 ? 20.424 -6.177  10.790  1.00 11.52 ?  123 LEU   A CA   1 
ATOM   2639 C  C    . LEU   A 1 123 ? 20.677 -5.659  9.381   1.00 10.82 ?  123 LEU   A C    1 
ATOM   2640 O  O    . LEU   A 1 123 ? 21.727 -5.060  9.136   1.00 11.56 ?  123 LEU   A O    1 
ATOM   2641 C  CB   . LEU   A 1 123 ? 20.293 -5.002  11.760  1.00 11.82 ?  123 LEU   A CB   1 
ATOM   2642 C  CG   . LEU   A 1 123 ? 19.250 -3.943  11.409  1.00 12.79 ?  123 LEU   A CG   1 
ATOM   2643 C  CD1  . LEU   A 1 123 ? 17.849 -4.535  11.406  1.00 13.25 ?  123 LEU   A CD1  1 
ATOM   2644 C  CD2  . LEU   A 1 123 ? 19.335 -2.756  12.373  1.00 13.42 ?  123 LEU   A CD2  1 
ATOM   2645 H  H    . LEU   A 1 123 ? 22.250 -6.492  11.445  1.00 13.97 ?  123 LEU   A H    1 
ATOM   2646 H  HA   . LEU   A 1 123 ? 19.618 -6.718  10.812  1.00 13.83 ?  123 LEU   A HA   1 
ATOM   2647 H  HB2  . LEU   A 1 123 ? 20.055 -5.350  12.638  1.00 14.19 ?  123 LEU   A HB2  1 
ATOM   2648 H  HB3  . LEU   A 1 123 ? 21.146 -4.550  11.817  1.00 14.19 ?  123 LEU   A HB3  1 
ATOM   2649 H  HG   . LEU   A 1 123 ? 19.420 -3.600  10.516  1.00 15.36 ?  123 LEU   A HG   1 
ATOM   2650 H  HD11 . LEU   A 1 123 ? 17.202 -3.837  11.224  1.00 15.91 ?  123 LEU   A HD11 1 
ATOM   2651 H  HD12 . LEU   A 1 123 ? 17.797 -5.221  10.720  1.00 15.91 ?  123 LEU   A HD12 1 
ATOM   2652 H  HD13 . LEU   A 1 123 ? 17.672 -4.930  12.277  1.00 15.91 ?  123 LEU   A HD13 1 
ATOM   2653 H  HD21 . LEU   A 1 123 ? 18.663 -2.097  12.132  1.00 16.11 ?  123 LEU   A HD21 1 
ATOM   2654 H  HD22 . LEU   A 1 123 ? 19.171 -3.075  13.277  1.00 16.11 ?  123 LEU   A HD22 1 
ATOM   2655 H  HD23 . LEU   A 1 123 ? 20.218 -2.366  12.314  1.00 16.11 ?  123 LEU   A HD23 1 
ATOM   2656 N  N    A ALA   A 1 124 ? 19.710 -5.821  8.477   0.68 10.40 ?  124 ALA   A N    1 
ATOM   2657 N  N    B ALA   A 1 124 ? 19.765 -5.934  8.451   0.32 10.75 ?  124 ALA   A N    1 
ATOM   2658 C  CA   A ALA   A 1 124 ? 19.989 -5.527  7.079   0.68 9.95  ?  124 ALA   A CA   1 
ATOM   2659 C  CA   B ALA   A 1 124 ? 20.091 -5.726  7.049   0.32 10.95 ?  124 ALA   A CA   1 
ATOM   2660 C  C    A ALA   A 1 124 ? 18.738 -5.060  6.348   0.68 9.75  ?  124 ALA   A C    1 
ATOM   2661 C  C    B ALA   A 1 124 ? 18.871 -5.277  6.259   0.32 10.47 ?  124 ALA   A C    1 
ATOM   2662 O  O    A ALA   A 1 124 ? 17.610 -5.397  6.738   0.68 10.73 ?  124 ALA   A O    1 
ATOM   2663 O  O    B ALA   A 1 124 ? 17.736 -5.624  6.611   0.32 10.78 ?  124 ALA   A O    1 
ATOM   2664 C  CB   A ALA   A 1 124 ? 20.561 -6.752  6.359   0.68 10.32 ?  124 ALA   A CB   1 
ATOM   2665 C  CB   B ALA   A 1 124 ? 20.678 -7.004  6.428   0.32 11.59 ?  124 ALA   A CB   1 
ATOM   2666 H  H    A ALA   A 1 124 ? 18.905 -6.090  8.645   0.68 12.48 ?  124 ALA   A H    1 
ATOM   2667 H  H    B ALA   A 1 124 ? 18.975 -6.241  8.598   0.32 12.90 ?  124 ALA   A H    1 
ATOM   2668 H  HA   A ALA   A 1 124 ? 20.652 -4.820  7.048   0.68 11.95 ?  124 ALA   A HA   1 
ATOM   2669 H  HA   B ALA   A 1 124 ? 20.760 -5.036  6.990   0.32 13.14 ?  124 ALA   A HA   1 
ATOM   2670 H  HB1  A ALA   A 1 124 ? 20.740 -6.516  5.435   0.68 12.38 ?  124 ALA   A HB1  1 
ATOM   2671 H  HB1  B ALA   A 1 124 ? 20.890 -6.841  5.495   0.32 13.91 ?  124 ALA   A HB1  1 
ATOM   2672 H  HB2  A ALA   A 1 124 ? 21.388 -7.015  6.797   0.68 12.38 ?  124 ALA   A HB2  1 
ATOM   2673 H  HB2  B ALA   A 1 124 ? 21.491 -7.246  6.909   0.32 13.91 ?  124 ALA   A HB2  1 
ATOM   2674 H  HB3  A ALA   A 1 124 ? 19.918 -7.472  6.402   0.68 12.38 ?  124 ALA   A HB3  1 
ATOM   2675 H  HB3  B ALA   A 1 124 ? 20.032 -7.724  6.500   0.32 13.91 ?  124 ALA   A HB3  1 
ATOM   2676 N  N    A PRO   A 1 125 ? 18.915 -4.315  5.257   0.68 10.11 ?  125 PRO   A N    1 
ATOM   2677 N  N    B PRO   A 1 125 ? 19.077 -4.526  5.181   0.32 9.38  ?  125 PRO   A N    1 
ATOM   2678 C  CA   A PRO   A 1 125 ? 17.857 -4.099  4.271   0.68 10.93 ?  125 PRO   A CA   1 
ATOM   2679 C  CA   B PRO   A 1 125 ? 17.984 -4.161  4.283   0.32 9.86  ?  125 PRO   A CA   1 
ATOM   2680 C  C    A PRO   A 1 125 ? 17.929 -5.179  3.193   0.68 10.56 ?  125 PRO   A C    1 
ATOM   2681 C  C    B PRO   A 1 125 ? 17.924 -5.152  3.127   0.32 10.51 ?  125 PRO   A C    1 
ATOM   2682 O  O    A PRO   A 1 125 ? 18.903 -5.930  3.093   0.68 10.90 ?  125 PRO   A O    1 
ATOM   2683 O  O    B PRO   A 1 125 ? 18.793 -6.010  2.962   0.32 10.79 ?  125 PRO   A O    1 
ATOM   2684 C  CB   A PRO   A 1 125 ? 18.269 -2.748  3.669   0.68 11.24 ?  125 PRO   A CB   1 
ATOM   2685 C  CB   B PRO   A 1 125 ? 18.453 -2.800  3.762   0.32 9.33  ?  125 PRO   A CB   1 
ATOM   2686 C  CG   A PRO   A 1 125 ? 19.783 -2.874  3.601   0.68 11.69 ?  125 PRO   A CG   1 
ATOM   2687 C  CG   B PRO   A 1 125 ? 19.946 -3.001  3.610   0.32 8.92  ?  125 PRO   A CG   1 
ATOM   2688 C  CD   A PRO   A 1 125 ? 20.157 -3.603  4.884   0.68 10.97 ?  125 PRO   A CD   1 
ATOM   2689 C  CD   B PRO   A 1 125 ? 20.357 -3.956  4.721   0.32 8.21  ?  125 PRO   A CD   1 
ATOM   2690 H  HA   A PRO   A 1 125 ? 16.975 -4.056  4.675   0.68 13.12 ?  125 PRO   A HA   1 
ATOM   2691 H  HA   B PRO   A 1 125 ? 17.134 -4.096  4.751   0.32 11.84 ?  125 PRO   A HA   1 
ATOM   2692 H  HB2  A PRO   A 1 125 ? 17.881 -2.640  2.786   0.68 13.49 ?  125 PRO   A HB2  1 
ATOM   2693 H  HB2  B PRO   A 1 125 ? 18.031 -2.612  2.908   0.32 11.20 ?  125 PRO   A HB2  1 
ATOM   2694 H  HB3  A PRO   A 1 125 ? 18.001 -2.024  4.260   0.68 13.49 ?  125 PRO   A HB3  1 
ATOM   2695 H  HB3  B PRO   A 1 125 ? 18.252 -2.109  4.413   0.32 11.20 ?  125 PRO   A HB3  1 
ATOM   2696 H  HG2  A PRO   A 1 125 ? 20.036 -3.400  2.823   0.68 14.03 ?  125 PRO   A HG2  1 
ATOM   2697 H  HG2  B PRO   A 1 125 ? 20.133 -3.392  2.742   0.32 10.70 ?  125 PRO   A HG2  1 
ATOM   2698 H  HG3  A PRO   A 1 125 ? 20.188 -1.995  3.569   0.68 14.03 ?  125 PRO   A HG3  1 
ATOM   2699 H  HG3  B PRO   A 1 125 ? 20.398 -2.152  3.709   0.32 10.70 ?  125 PRO   A HG3  1 
ATOM   2700 H  HD2  A PRO   A 1 125 ? 20.880 -4.224  4.723   0.68 13.17 ?  125 PRO   A HD2  1 
ATOM   2701 H  HD2  B PRO   A 1 125 ? 20.937 -4.652  4.370   0.32 9.86  ?  125 PRO   A HD2  1 
ATOM   2702 H  HD3  A PRO   A 1 125 ? 20.391 -2.957  5.576   0.68 13.17 ?  125 PRO   A HD3  1 
ATOM   2703 H  HD3  B PRO   A 1 125 ? 20.785 -3.466  5.439   0.32 9.86  ?  125 PRO   A HD3  1 
ATOM   2704 N  N    A LEU   A 1 126 ? 16.886 -5.223  2.363   0.68 10.34 ?  126 LEU   A N    1 
ATOM   2705 N  N    B LEU   A 1 126 ? 16.891 -4.996  2.307   0.32 11.18 ?  126 LEU   A N    1 
ATOM   2706 C  CA   A LEU   A 1 126 ? 16.916 -6.049  1.163   0.68 10.55 ?  126 LEU   A CA   1 
ATOM   2707 C  CA   B LEU   A 1 126 ? 16.764 -5.788  1.087   0.32 10.93 ?  126 LEU   A CA   1 
ATOM   2708 C  C    A LEU   A 1 126 ? 17.854 -5.430  0.130   0.68 10.57 ?  126 LEU   A C    1 
ATOM   2709 C  C    B LEU   A 1 126 ? 17.707 -5.218  0.034   0.32 10.25 ?  126 LEU   A C    1 
ATOM   2710 O  O    A LEU   A 1 126 ? 17.653 -4.295  -0.318  0.68 11.30 ?  126 LEU   A O    1 
ATOM   2711 O  O    B LEU   A 1 126 ? 17.428 -4.184  -0.577  0.32 10.47 ?  126 LEU   A O    1 
ATOM   2712 C  CB   A LEU   A 1 126 ? 15.510 -6.201  0.595   0.68 10.98 ?  126 LEU   A CB   1 
ATOM   2713 C  CB   B LEU   A 1 126 ? 15.323 -5.772  0.597   0.32 11.79 ?  126 LEU   A CB   1 
ATOM   2714 C  CG   A LEU   A 1 126 ? 14.604 -7.155  1.372   0.68 11.62 ?  126 LEU   A CG   1 
ATOM   2715 C  CG   B LEU   A 1 126 ? 14.348 -6.628  1.400   0.32 12.09 ?  126 LEU   A CG   1 
ATOM   2716 C  CD1  A LEU   A 1 126 ? 13.182 -7.023  0.862   0.68 13.16 ?  126 LEU   A CD1  1 
ATOM   2717 C  CD1  B LEU   A 1 126 ? 12.944 -6.462  0.849   0.32 12.32 ?  126 LEU   A CD1  1 
ATOM   2718 C  CD2  A LEU   A 1 126 ? 15.084 -8.604  1.254   0.68 11.65 ?  126 LEU   A CD2  1 
ATOM   2719 C  CD2  B LEU   A 1 126 ? 14.752 -8.096  1.383   0.32 12.02 ?  126 LEU   A CD2  1 
ATOM   2720 H  H    A LEU   A 1 126 ? 16.155 -4.774  2.462   0.68 12.42 ?  126 LEU   A H    1 
ATOM   2721 H  H    B LEU   A 1 126 ? 16.246 -4.435  2.441   0.32 13.42 ?  126 LEU   A H    1 
ATOM   2722 H  HA   A LEU   A 1 126 ? 17.252 -6.925  1.384   0.68 12.66 ?  126 LEU   A HA   1 
ATOM   2723 H  HA   B LEU   A 1 126 ? 17.027 -6.700  1.279   0.32 13.12 ?  126 LEU   A HA   1 
ATOM   2724 H  HB2  A LEU   A 1 126 ? 15.076 -5.333  0.593   0.68 13.18 ?  126 LEU   A HB2  1 
ATOM   2725 H  HB2  B LEU   A 1 126 ? 14.998 -4.856  0.627   0.32 14.15 ?  126 LEU   A HB2  1 
ATOM   2726 H  HB3  A LEU   A 1 126 ? 15.569 -6.536  -0.313  0.68 13.18 ?  126 LEU   A HB3  1 
ATOM   2727 H  HB3  B LEU   A 1 126 ? 15.311 -6.092  -0.314  0.32 14.15 ?  126 LEU   A HB3  1 
ATOM   2728 H  HG   A LEU   A 1 126 ? 14.606 -6.914  2.310   0.68 13.95 ?  126 LEU   A HG   1 
ATOM   2729 H  HG   B LEU   A 1 126 ? 14.343 -6.326  2.322   0.32 14.51 ?  126 LEU   A HG   1 
ATOM   2730 H  HD11 A LEU   A 1 126 ? 12.610 -7.637  1.350   0.68 15.80 ?  126 LEU   A HD11 1 
ATOM   2731 H  HD11 B LEU   A 1 126 ? 12.334 -7.010  1.367   0.32 14.79 ?  126 LEU   A HD11 1 
ATOM   2732 H  HD12 A LEU   A 1 126 ? 12.882 -6.112  0.998   0.68 15.80 ?  126 LEU   A HD12 1 
ATOM   2733 H  HD12 B LEU   A 1 126 ? 12.686 -5.528  0.913   0.32 14.79 ?  126 LEU   A HD12 1 
ATOM   2734 H  HD13 A LEU   A 1 126 ? 13.165 -7.239  -0.085  0.68 15.80 ?  126 LEU   A HD13 1 
ATOM   2735 H  HD13 B LEU   A 1 126 ? 12.934 -6.743  -0.080  0.32 14.79 ?  126 LEU   A HD13 1 
ATOM   2736 H  HD21 A LEU   A 1 126 ? 14.416 -9.197  1.633   0.68 13.98 ?  126 LEU   A HD21 1 
ATOM   2737 H  HD21 B LEU   A 1 126 ? 14.012 -8.630  1.712   0.32 14.43 ?  126 LEU   A HD21 1 
ATOM   2738 H  HD22 A LEU   A 1 126 ? 15.220 -8.818  0.316   0.68 13.98 ?  126 LEU   A HD22 1 
ATOM   2739 H  HD22 B LEU   A 1 126 ? 14.965 -8.352  0.473   0.32 14.43 ?  126 LEU   A HD22 1 
ATOM   2740 H  HD23 A LEU   A 1 126 ? 15.922 -8.701  1.736   0.68 13.98 ?  126 LEU   A HD23 1 
ATOM   2741 H  HD23 B LEU   A 1 126 ? 15.526 -8.217  1.952   0.32 14.43 ?  126 LEU   A HD23 1 
ATOM   2742 N  N    A LEU   A 1 127 ? 18.887 -6.178  -0.240  0.68 10.77 ?  127 LEU   A N    1 
ATOM   2743 N  N    B LEU   A 1 127 ? 18.826 -5.899  -0.194  0.32 9.81  ?  127 LEU   A N    1 
ATOM   2744 C  CA   A LEU   A 1 127 ? 19.877 -5.681  -1.179  0.68 10.61 ?  127 LEU   A CA   1 
ATOM   2745 C  CA   B LEU   A 1 127 ? 19.824 -5.394  -1.124  0.32 10.10 ?  127 LEU   A CA   1 
ATOM   2746 C  C    A LEU   A 1 127 ? 19.261 -5.491  -2.554  0.68 10.19 ?  127 LEU   A C    1 
ATOM   2747 C  C    B LEU   A 1 127 ? 19.280 -5.353  -2.550  0.32 10.39 ?  127 LEU   A C    1 
ATOM   2748 O  O    A LEU   A 1 127 ? 18.435 -6.290  -3.011  0.68 10.68 ?  127 LEU   A O    1 
ATOM   2749 O  O    B LEU   A 1 127 ? 18.458 -6.179  -2.959  0.32 10.58 ?  127 LEU   A O    1 
ATOM   2750 C  CB   A LEU   A 1 127 ? 21.052 -6.652  -1.273  0.68 11.15 ?  127 LEU   A CB   1 
ATOM   2751 C  CB   B LEU   A 1 127 ? 21.083 -6.261  -1.078  0.32 10.72 ?  127 LEU   A CB   1 
ATOM   2752 C  CG   A LEU   A 1 127 ? 21.853 -6.868  0.011   0.68 11.62 ?  127 LEU   A CG   1 
ATOM   2753 C  CG   B LEU   A 1 127 ? 21.874 -6.229  0.232   0.32 11.21 ?  127 LEU   A CG   1 
ATOM   2754 C  CD1  A LEU   A 1 127 ? 22.948 -7.867  -0.256  0.68 11.94 ?  127 LEU   A CD1  1 
ATOM   2755 C  CD1  B LEU   A 1 127 ? 23.041 -7.205  0.165   0.32 11.70 ?  127 LEU   A CD1  1 
ATOM   2756 C  CD2  A LEU   A 1 127 ? 22.451 -5.571  0.515   0.68 12.48 ?  127 LEU   A CD2  1 
ATOM   2757 C  CD2  B LEU   A 1 127 ? 22.370 -4.818  0.545   0.32 11.71 ?  127 LEU   A CD2  1 
ATOM   2758 H  H    A LEU   A 1 127 ? 19.032 -6.979  0.038   0.68 12.93 ?  127 LEU   A H    1 
ATOM   2759 H  H    B LEU   A 1 127 ? 19.033 -6.647  0.181   0.32 11.77 ?  127 LEU   A H    1 
ATOM   2760 H  HA   A LEU   A 1 127 ? 20.211 -4.827  -0.875  0.68 12.74 ?  127 LEU   A HA   1 
ATOM   2761 H  HA   B LEU   A 1 127 ? 20.067 -4.489  -0.864  0.32 12.13 ?  127 LEU   A HA   1 
ATOM   2762 H  HB2  A LEU   A 1 127 ? 20.710 -7.518  -1.549  0.68 13.39 ?  127 LEU   A HB2  1 
ATOM   2763 H  HB2  B LEU   A 1 127 ? 20.820 -7.181  -1.240  0.32 12.87 ?  127 LEU   A HB2  1 
ATOM   2764 H  HB3  A LEU   A 1 127 ? 21.668 -6.322  -1.944  0.68 13.39 ?  127 LEU   A HB3  1 
ATOM   2765 H  HB3  B LEU   A 1 127 ? 21.677 -5.966  -1.786  0.32 12.87 ?  127 LEU   A HB3  1 
ATOM   2766 H  HG   A LEU   A 1 127 ? 21.268 -7.228  0.701   0.68 13.95 ?  127 LEU   A HG   1 
ATOM   2767 H  HG   B LEU   A 1 127 ? 21.293 -6.509  0.958   0.32 13.45 ?  127 LEU   A HG   1 
ATOM   2768 H  HD11 A LEU   A 1 127 ? 23.436 -8.029  0.568   0.68 14.33 ?  127 LEU   A HD11 1 
ATOM   2769 H  HD11 B LEU   A 1 127 ? 23.570 -7.117  0.972   0.32 14.04 ?  127 LEU   A HD11 1 
ATOM   2770 H  HD12 A LEU   A 1 127 ? 22.552 -8.696  -0.572  0.68 14.33 ?  127 LEU   A HD12 1 
ATOM   2771 H  HD12 B LEU   A 1 127 ? 22.692 -8.107  0.092   0.32 14.04 ?  127 LEU   A HD12 1 
ATOM   2772 H  HD13 A LEU   A 1 127 ? 23.545 -7.507  -0.929  0.68 14.33 ?  127 LEU   A HD13 1 
ATOM   2773 H  HD13 B LEU   A 1 127 ? 23.581 -6.993  -0.611  0.32 14.04 ?  127 LEU   A HD13 1 
ATOM   2774 H  HD21 A LEU   A 1 127 ? 23.049 -5.766  1.253   0.68 14.98 ?  127 LEU   A HD21 1 
ATOM   2775 H  HD21 B LEU   A 1 127 ? 22.985 -4.858  1.294   0.32 14.06 ?  127 LEU   A HD21 1 
ATOM   2776 H  HD22 A LEU   A 1 127 ? 22.948 -5.155  -0.210  0.68 14.98 ?  127 LEU   A HD22 1 
ATOM   2777 H  HD22 B LEU   A 1 127 ? 22.823 -4.464  -0.236  0.32 14.06 ?  127 LEU   A HD22 1 
ATOM   2778 H  HD23 A LEU   A 1 127 ? 21.740 -4.985  0.808   0.68 14.98 ?  127 LEU   A HD23 1 
ATOM   2779 H  HD23 B LEU   A 1 127 ? 21.611 -4.258  0.770   0.32 14.06 ?  127 LEU   A HD23 1 
ATOM   2780 N  N    A SER   A 1 128 ? 19.691 -4.426  -3.222  0.68 10.07 ?  128 SER   A N    1 
ATOM   2781 N  N    B SER   A 1 128 ? 19.763 -4.365  -3.303  0.32 10.56 ?  128 SER   A N    1 
ATOM   2782 C  CA   A SER   A 1 128 ? 19.289 -4.032  -4.564  0.68 10.43 ?  128 SER   A CA   1 
ATOM   2783 C  CA   B SER   A 1 128 ? 19.425 -4.135  -4.705  0.32 10.28 ?  128 SER   A CA   1 
ATOM   2784 C  C    A SER   A 1 128 ? 17.830 -3.589  -4.658  0.68 10.83 ?  128 SER   A C    1 
ATOM   2785 C  C    B SER   A 1 128 ? 17.994 -3.648  -4.930  0.32 9.91  ?  128 SER   A C    1 
ATOM   2786 O  O    A SER   A 1 128 ? 17.369 -3.293  -5.761  0.68 12.06 ?  128 SER   A O    1 
ATOM   2787 O  O    B SER   A 1 128 ? 17.651 -3.247  -6.046  0.32 10.06 ?  128 SER   A O    1 
ATOM   2788 C  CB   A SER   A 1 128 ? 19.630 -5.078  -5.637  0.68 10.61 ?  128 SER   A CB   1 
ATOM   2789 C  CB   B SER   A 1 128 ? 19.746 -5.360  -5.568  0.32 10.52 ?  128 SER   A CB   1 
ATOM   2790 O  OG   A SER   A 1 128 ? 21.036 -5.279  -5.710  0.68 11.30 ?  128 SER   A OG   1 
ATOM   2791 O  OG   B SER   A 1 128 ? 21.150 -5.536  -5.687  0.32 10.84 ?  128 SER   A OG   1 
ATOM   2792 H  H    A SER   A 1 128 ? 20.274 -3.875  -2.893  0.68 12.09 ?  128 SER   A H    1 
ATOM   2793 H  H    B SER   A 1 128 ? 20.335 -3.796  -3.009  0.32 12.68 ?  128 SER   A H    1 
ATOM   2794 H  HA   A SER   A 1 128 ? 19.811 -3.251  -4.791  0.68 12.52 ?  128 SER   A HA   1 
ATOM   2795 H  HA   B SER   A 1 128 ? 19.997 -3.425  -5.022  0.32 12.35 ?  128 SER   A HA   1 
ATOM   2796 H  HB2  A SER   A 1 128 ? 19.194 -5.915  -5.412  0.68 12.74 ?  128 SER   A HB2  1 
ATOM   2797 H  HB2  B SER   A 1 128 ? 19.362 -6.150  -5.163  0.32 12.62 ?  128 SER   A HB2  1 
ATOM   2798 H  HB3  A SER   A 1 128 ? 19.312 -4.759  -6.499  0.68 12.74 ?  128 SER   A HB3  1 
ATOM   2799 H  HB3  B SER   A 1 128 ? 19.370 -5.225  -6.454  0.32 12.62 ?  128 SER   A HB3  1 
ATOM   2800 H  HG   A SER   A 1 128 ? 21.417 -4.552  -5.889  0.68 13.56 ?  128 SER   A HG   1 
ATOM   2801 H  HG   B SER   A 1 128 ? 21.494 -4.856  -6.044  0.32 13.01 ?  128 SER   A HG   1 
ATOM   2802 N  N    A ALA   A 1 129 ? 17.102 -3.515  -3.542  0.68 11.30 ?  129 ALA   A N    1 
ATOM   2803 N  N    B ALA   A 1 129 ? 17.161 -3.662  -3.890  0.32 10.05 ?  129 ALA   A N    1 
ATOM   2804 C  CA   A ALA   A 1 129 ? 15.727 -3.037  -3.534  0.68 11.72 ?  129 ALA   A CA   1 
ATOM   2805 C  CA   B ALA   A 1 129 ? 15.797 -3.164  -3.988  0.32 10.16 ?  129 ALA   A CA   1 
ATOM   2806 C  C    A ALA   A 1 129 ? 15.711 -1.508  -3.509  0.68 11.20 ?  129 ALA   A C    1 
ATOM   2807 C  C    B ALA   A 1 129 ? 15.794 -1.653  -3.746  0.32 10.89 ?  129 ALA   A C    1 
ATOM   2808 O  O    A ALA   A 1 129 ? 16.754 -0.847  -3.546  0.68 11.38 ?  129 ALA   A O    1 
ATOM   2809 O  O    B ALA   A 1 129 ? 16.840 -0.999  -3.769  0.32 10.89 ?  129 ALA   A O    1 
ATOM   2810 C  CB   A ALA   A 1 129 ? 14.960 -3.647  -2.358  0.68 12.89 ?  129 ALA   A CB   1 
ATOM   2811 C  CB   B ALA   A 1 129 ? 14.882 -3.943  -3.040  0.32 9.35  ?  129 ALA   A CB   1 
ATOM   2812 H  H    A ALA   A 1 129 ? 17.390 -3.744  -2.763  0.68 13.57 ?  129 ALA   A H    1 
ATOM   2813 H  H    B ALA   A 1 129 ? 17.363 -3.960  -3.109  0.32 12.06 ?  129 ALA   A H    1 
ATOM   2814 H  HA   A ALA   A 1 129 ? 15.291 -3.323  -4.347  0.68 14.07 ?  129 ALA   A HA   1 
ATOM   2815 H  HA   B ALA   A 1 129 ? 15.477 -3.313  -4.888  0.32 12.19 ?  129 ALA   A HA   1 
ATOM   2816 H  HB1  A ALA   A 1 129 ? 14.046 -3.320  -2.369  0.68 15.48 ?  129 ALA   A HB1  1 
ATOM   2817 H  HB1  B ALA   A 1 129 ? 13.978 -3.604  -3.125  0.32 11.22 ?  129 ALA   A HB1  1 
ATOM   2818 H  HB2  A ALA   A 1 129 ? 14.966 -4.613  -2.439  0.68 15.48 ?  129 ALA   A HB2  1 
ATOM   2819 H  HB2  B ALA   A 1 129 ? 14.906 -4.883  -3.281  0.32 11.22 ?  129 ALA   A HB2  1 
ATOM   2820 H  HB3  A ALA   A 1 129 ? 15.390 -3.385  -1.525  0.68 15.48 ?  129 ALA   A HB3  1 
ATOM   2821 H  HB3  B ALA   A 1 129 ? 15.196 -3.829  -2.130  0.32 11.22 ?  129 ALA   A HB3  1 
ATOM   2822 N  N    A GLY   A 1 130 ? 14.509 -0.941  -3.455  0.68 12.00 ?  130 GLY   A N    1 
ATOM   2823 N  N    B GLY   A 1 130 ? 14.612 -1.081  -3.522  0.32 11.74 ?  130 GLY   A N    1 
ATOM   2824 C  CA   A GLY   A 1 130 ? 14.386 0.506   -3.458  0.68 12.09 ?  130 GLY   A CA   1 
ATOM   2825 C  CA   B GLY   A 1 130 ? 14.533 0.351   -3.287  0.32 12.03 ?  130 GLY   A CA   1 
ATOM   2826 C  C    A GLY   A 1 130 ? 15.051 1.109   -4.676  0.68 12.03 ?  130 GLY   A C    1 
ATOM   2827 C  C    B GLY   A 1 130 ? 15.050 1.119   -4.484  0.32 12.10 ?  130 GLY   A C    1 
ATOM   2828 O  O    A GLY   A 1 130 ? 14.872 0.641   -5.805  0.68 12.33 ?  130 GLY   A O    1 
ATOM   2829 O  O    B GLY   A 1 130 ? 14.746 0.794   -5.637  0.32 12.16 ?  130 GLY   A O    1 
ATOM   2830 H  H    A GLY   A 1 130 ? 13.761 -1.371  -3.413  0.68 14.40 ?  130 GLY   A H    1 
ATOM   2831 H  H    B GLY   A 1 130 ? 13.856 -1.494  -3.512  0.32 14.09 ?  130 GLY   A H    1 
ATOM   2832 H  HA2  A GLY   A 1 130 ? 13.445 0.748   -3.459  0.68 14.51 ?  130 GLY   A HA2  1 
ATOM   2833 H  HA2  B GLY   A 1 130 ? 13.609 0.603   -3.113  0.32 14.44 ?  130 GLY   A HA2  1 
ATOM   2834 H  HA3  A GLY   A 1 130 ? 14.801 0.869   -2.665  0.68 14.51 ?  130 GLY   A HA3  1 
ATOM   2835 H  HA3  B GLY   A 1 130 ? 15.067 0.589   -2.517  0.32 14.44 ?  130 GLY   A HA3  1 
ATOM   2836 N  N    A ILE   A 1 131 ? 15.837 2.168   -4.444  0.68 12.13 ?  131 ILE   A N    1 
ATOM   2837 N  N    B ILE   A 1 131 ? 15.854 2.152   -4.213  0.32 12.40 ?  131 ILE   A N    1 
ATOM   2838 C  CA   A ILE   A 1 131 ? 16.422 2.942   -5.537  0.68 12.14 ?  131 ILE   A CA   1 
ATOM   2839 C  CA   B ILE   A 1 131 ? 16.411 2.980   -5.280  0.32 12.50 ?  131 ILE   A CA   1 
ATOM   2840 C  C    A ILE   A 1 131 ? 17.476 2.182   -6.331  0.68 11.71 ?  131 ILE   A C    1 
ATOM   2841 C  C    B ILE   A 1 131 ? 17.377 2.226   -6.183  0.32 12.48 ?  131 ILE   A C    1 
ATOM   2842 O  O    A ILE   A 1 131 ? 17.923 2.691   -7.369  0.68 12.52 ?  131 ILE   A O    1 
ATOM   2843 O  O    B ILE   A 1 131 ? 17.728 2.738   -7.253  0.32 12.76 ?  131 ILE   A O    1 
ATOM   2844 C  CB   A ILE   A 1 131 ? 16.947 4.318   -5.067  0.68 13.20 ?  131 ILE   A CB   1 
ATOM   2845 C  CB   B ILE   A 1 131 ? 17.090 4.255   -4.732  0.32 13.06 ?  131 ILE   A CB   1 
ATOM   2846 C  CG1  A ILE   A 1 131 ? 18.178 4.175   -4.165  0.68 14.41 ?  131 ILE   A CG1  1 
ATOM   2847 C  CG1  B ILE   A 1 131 ? 18.294 3.906   -3.851  0.32 13.66 ?  131 ILE   A CG1  1 
ATOM   2848 C  CG2  A ILE   A 1 131 ? 15.832 5.109   -4.378  0.68 13.39 ?  131 ILE   A CG2  1 
ATOM   2849 C  CG2  B ILE   A 1 131 ? 16.090 5.109   -3.964  0.32 13.51 ?  131 ILE   A CG2  1 
ATOM   2850 C  CD1  A ILE   A 1 131 ? 18.801 5.517   -3.770  0.68 15.39 ?  131 ILE   A CD1  1 
ATOM   2851 C  CD1  B ILE   A 1 131 ? 19.018 5.129   -3.296  0.32 14.07 ?  131 ILE   A CD1  1 
ATOM   2852 H  H    A ILE   A 1 131 ? 16.025 2.462   -3.659  0.68 14.56 ?  131 ILE   A H    1 
ATOM   2853 H  H    B ILE   A 1 131 ? 16.079 2.395   -3.420  0.32 14.89 ?  131 ILE   A H    1 
ATOM   2854 H  HA   A ILE   A 1 131 ? 15.712 3.125   -6.163  0.68 14.57 ?  131 ILE   A HA   1 
ATOM   2855 H  HA   B ILE   A 1 131 ? 15.677 3.276   -5.837  0.32 15.00 ?  131 ILE   A HA   1 
ATOM   2856 H  HB   A ILE   A 1 131 ? 17.214 4.808   -5.857  0.68 15.85 ?  131 ILE   A HB   1 
ATOM   2857 H  HB   B ILE   A 1 131 ? 17.407 4.774   -5.486  0.32 15.67 ?  131 ILE   A HB   1 
ATOM   2858 H  HG12 A ILE   A 1 131 ? 17.922 3.712   -3.353  0.68 17.30 ?  131 ILE   A HG12 1 
ATOM   2859 H  HG12 B ILE   A 1 131 ? 17.989 3.376   -3.101  0.32 16.40 ?  131 ILE   A HG12 1 
ATOM   2860 H  HG13 A ILE   A 1 131 ? 18.859 3.663   -4.634  0.68 17.30 ?  131 ILE   A HG13 1 
ATOM   2861 H  HG13 B ILE   A 1 131 ? 18.932 3.403   -4.378  0.32 16.40 ?  131 ILE   A HG13 1 
ATOM   2862 H  HG21 A ILE   A 1 131 ? 16.133 6.019   -4.238  0.68 16.07 ?  131 ILE   A HG21 1 
ATOM   2863 H  HG21 B ILE   A 1 131 ? 16.478 5.983   -3.800  0.32 16.22 ?  131 ILE   A HG21 1 
ATOM   2864 H  HG22 A ILE   A 1 131 ? 15.046 5.102   -4.946  0.68 16.07 ?  131 ILE   A HG22 1 
ATOM   2865 H  HG22 B ILE   A 1 131 ? 15.284 5.203   -4.497  0.32 16.22 ?  131 ILE   A HG22 1 
ATOM   2866 H  HG23 A ILE   A 1 131 ? 15.628 4.690   -3.527  0.68 16.07 ?  131 ILE   A HG23 1 
ATOM   2867 H  HG23 B ILE   A 1 131 ? 15.882 4.674   -3.124  0.32 16.22 ?  131 ILE   A HG23 1 
ATOM   2868 H  HD11 A ILE   A 1 131 ? 19.634 5.354   -3.300  0.68 18.47 ?  131 ILE   A HD11 1 
ATOM   2869 H  HD11 B ILE   A 1 131 ? 19.844 4.844   -2.877  0.32 16.89 ?  131 ILE   A HD11 1 
ATOM   2870 H  HD12 A ILE   A 1 131 ? 18.970 6.036   -4.573  0.68 18.47 ?  131 ILE   A HD12 1 
ATOM   2871 H  HD12 B ILE   A 1 131 ? 19.211 5.742   -4.025  0.32 16.89 ?  131 ILE   A HD12 1 
ATOM   2872 H  HD13 A ILE   A 1 131 ? 18.184 5.994   -3.193  0.68 18.47 ?  131 ILE   A HD13 1 
ATOM   2873 H  HD13 B ILE   A 1 131 ? 18.450 5.568   -2.642  0.32 16.89 ?  131 ILE   A HD13 1 
ATOM   2874 N  N    A PHE   A 1 132 ? 17.880 0.979   -5.893  0.68 11.42 ?  132 PHE   A N    1 
ATOM   2875 N  N    B PHE   A 1 132 ? 17.809 1.023   -5.793  0.32 12.50 ?  132 PHE   A N    1 
ATOM   2876 C  CA   A PHE   A 1 132 ? 18.735 0.138   -6.727  0.68 11.70 ?  132 PHE   A CA   1 
ATOM   2877 C  CA   B PHE   A 1 132 ? 18.775 0.272   -6.590  0.32 12.77 ?  132 PHE   A CA   1 
ATOM   2878 C  C    A PHE   A 1 132 ? 17.949 -0.620  -7.797  0.68 12.33 ?  132 PHE   A C    1 
ATOM   2879 C  C    B PHE   A 1 132 ? 18.151 -0.468  -7.774  0.32 13.35 ?  132 PHE   A C    1 
ATOM   2880 O  O    A PHE   A 1 132 ? 18.563 -1.271  -8.649  0.68 12.67 ?  132 PHE   A O    1 
ATOM   2881 O  O    B PHE   A 1 132 ? 18.894 -0.954  -8.633  0.32 13.89 ?  132 PHE   A O    1 
ATOM   2882 C  CB   A PHE   A 1 132 ? 19.558 -0.845  -5.881  0.68 11.27 ?  132 PHE   A CB   1 
ATOM   2883 C  CB   B PHE   A 1 132 ? 19.569 -0.705  -5.713  0.32 12.22 ?  132 PHE   A CB   1 
ATOM   2884 C  CG   A PHE   A 1 132 ? 20.772 -0.237  -5.202  0.68 11.05 ?  132 PHE   A CG   1 
ATOM   2885 C  CG   B PHE   A 1 132 ? 20.800 -0.104  -5.068  0.32 11.77 ?  132 PHE   A CG   1 
ATOM   2886 C  CD1  A PHE   A 1 132 ? 20.647 0.820   -4.314  0.68 12.01 ?  132 PHE   A CD1  1 
ATOM   2887 C  CD1  B PHE   A 1 132 ? 20.688 0.819   -4.039  0.32 12.05 ?  132 PHE   A CD1  1 
ATOM   2888 C  CD2  A PHE   A 1 132 ? 22.033 -0.775  -5.412  0.68 12.03 ?  132 PHE   A CD2  1 
ATOM   2889 C  CD2  B PHE   A 1 132 ? 22.071 -0.491  -5.471  0.32 11.89 ?  132 PHE   A CD2  1 
ATOM   2890 C  CE1  A PHE   A 1 132 ? 21.766 1.348   -3.679  0.68 12.46 ?  132 PHE   A CE1  1 
ATOM   2891 C  CE1  B PHE   A 1 132 ? 21.818 1.357   -3.440  0.32 12.25 ?  132 PHE   A CE1  1 
ATOM   2892 C  CE2  A PHE   A 1 132 ? 23.149 -0.257  -4.778  0.68 12.18 ?  132 PHE   A CE2  1 
ATOM   2893 C  CE2  B PHE   A 1 132 ? 23.204 0.044   -4.874  0.32 12.33 ?  132 PHE   A CE2  1 
ATOM   2894 C  CZ   A PHE   A 1 132 ? 23.013 0.807   -3.910  0.68 12.34 ?  132 PHE   A CZ   1 
ATOM   2895 C  CZ   B PHE   A 1 132 ? 23.073 0.969   -3.857  0.32 12.37 ?  132 PHE   A CZ   1 
ATOM   2896 H  H    A PHE   A 1 132 ? 17.675 0.630   -5.125  0.68 13.71 ?  132 PHE   A H    1 
ATOM   2897 H  H    B PHE   A 1 132 ? 17.559 0.630   -5.069  0.32 15.01 ?  132 PHE   A H    1 
ATOM   2898 H  HA   A PHE   A 1 132 ? 19.368 0.713   -7.179  0.68 14.05 ?  132 PHE   A HA   1 
ATOM   2899 H  HA   B PHE   A 1 132 ? 19.409 0.910   -6.950  0.32 15.33 ?  132 PHE   A HA   1 
ATOM   2900 H  HB2  A PHE   A 1 132 ? 18.989 -1.207  -5.184  0.68 13.52 ?  132 PHE   A HB2  1 
ATOM   2901 H  HB2  B PHE   A 1 132 ? 18.993 -1.025  -5.003  0.32 14.67 ?  132 PHE   A HB2  1 
ATOM   2902 H  HB3  A PHE   A 1 132 ? 19.872 -1.566  -6.452  0.68 13.52 ?  132 PHE   A HB3  1 
ATOM   2903 H  HB3  B PHE   A 1 132 ? 19.858 -1.446  -6.264  0.32 14.67 ?  132 PHE   A HB3  1 
ATOM   2904 H  HD1  A PHE   A 1 132 ? 19.812 1.189   -4.147  0.68 14.42 ?  132 PHE   A HD1  1 
ATOM   2905 H  HD1  B PHE   A 1 132 ? 19.846 1.089   -3.752  0.32 14.46 ?  132 PHE   A HD1  1 
ATOM   2906 H  HD2  A PHE   A 1 132 ? 22.134 -1.495  -5.995  0.68 14.45 ?  132 PHE   A HD2  1 
ATOM   2907 H  HD2  B PHE   A 1 132 ? 22.168 -1.113  -6.155  0.32 14.27 ?  132 PHE   A HD2  1 
ATOM   2908 H  HE1  A PHE   A 1 132 ? 21.675 2.065   -3.091  0.68 14.95 ?  132 PHE   A HE1  1 
ATOM   2909 H  HE1  B PHE   A 1 132 ? 21.730 1.981   -2.755  0.32 14.70 ?  132 PHE   A HE1  1 
ATOM   2910 H  HE2  A PHE   A 1 132 ? 23.989 -0.621  -4.941  0.68 14.62 ?  132 PHE   A HE2  1 
ATOM   2911 H  HE2  B PHE   A 1 132 ? 24.051 -0.220  -5.158  0.32 14.80 ?  132 PHE   A HE2  1 
ATOM   2912 H  HZ   A PHE   A 1 132 ? 23.760 1.165   -3.487  0.68 14.82 ?  132 PHE   A HZ   1 
ATOM   2913 H  HZ   B PHE   A 1 132 ? 23.832 1.330   -3.455  0.32 14.85 ?  132 PHE   A HZ   1 
ATOM   2914 N  N    A GLY   A 1 133 ? 16.617 -0.569  -7.766  0.68 12.51 ?  133 GLY   A N    1 
ATOM   2915 N  N    B GLY   A 1 133 ? 16.822 -0.587  -7.847  0.32 13.28 ?  133 GLY   A N    1 
ATOM   2916 C  CA   A GLY   A 1 133 ? 15.805 -0.922  -8.917  0.68 13.14 ?  133 GLY   A CA   1 
ATOM   2917 C  CA   B GLY   A 1 133 ? 16.144 -0.982  -9.068  0.32 13.22 ?  133 GLY   A CA   1 
ATOM   2918 C  C    A GLY   A 1 133 ? 15.538 -2.393  -9.162  0.68 13.66 ?  133 GLY   A C    1 
ATOM   2919 C  C    B GLY   A 1 133 ? 15.481 -2.347  -9.053  0.32 13.10 ?  133 GLY   A C    1 
ATOM   2920 O  O    A GLY   A 1 133 ? 14.950 -2.719  -10.199 0.68 14.22 ?  133 GLY   A O    1 
ATOM   2921 O  O    B GLY   A 1 133 ? 14.572 -2.576  -9.862  0.32 13.16 ?  133 GLY   A O    1 
ATOM   2922 H  H    A GLY   A 1 133 ? 16.159 -0.328  -7.081  0.68 15.01 ?  133 GLY   A H    1 
ATOM   2923 H  H    B GLY   A 1 133 ? 16.290 -0.444  -7.186  0.32 15.94 ?  133 GLY   A H    1 
ATOM   2924 H  HA2  A GLY   A 1 133 ? 14.941 -0.490  -8.825  0.68 15.77 ?  133 GLY   A HA2  1 
ATOM   2925 H  HA2  B GLY   A 1 133 ? 15.455 -0.336  -9.271  0.32 15.87 ?  133 GLY   A HA2  1 
ATOM   2926 H  HA3  A GLY   A 1 133 ? 16.227 -0.568  -9.714  0.68 15.77 ?  133 GLY   A HA3  1 
ATOM   2927 H  HA3  B GLY   A 1 133 ? 16.783 -0.970  -9.799  0.32 15.87 ?  133 GLY   A HA3  1 
ATOM   2928 N  N    A ALA   A 1 134 ? 15.943 -3.293  -8.269  0.68 13.37 ?  134 ALA   A N    1 
ATOM   2929 N  N    B ALA   A 1 134 ? 15.897 -3.258  -8.180  0.32 12.78 ?  134 ALA   A N    1 
ATOM   2930 C  CA   A ALA   A 1 134 ? 15.629 -4.702  -8.452  0.68 13.84 ?  134 ALA   A CA   1 
ATOM   2931 C  CA   B ALA   A 1 134 ? 15.431 -4.635  -8.269  0.32 12.83 ?  134 ALA   A CA   1 
ATOM   2932 C  C    A ALA   A 1 134 ? 14.266 -5.027  -7.842  0.68 13.52 ?  134 ALA   A C    1 
ATOM   2933 C  C    B ALA   A 1 134 ? 14.132 -4.843  -7.499  0.32 12.67 ?  134 ALA   A C    1 
ATOM   2934 O  O    A ALA   A 1 134 ? 13.684 -4.241  -7.090  0.68 14.30 ?  134 ALA   A O    1 
ATOM   2935 O  O    B ALA   A 1 134 ? 13.770 -4.070  -6.607  0.32 13.02 ?  134 ALA   A O    1 
ATOM   2936 C  CB   A ALA   A 1 134 ? 16.720 -5.583  -7.845  0.68 15.07 ?  134 ALA   A CB   1 
ATOM   2937 C  CB   B ALA   A 1 134 ? 16.486 -5.605  -7.748  0.32 13.21 ?  134 ALA   A CB   1 
ATOM   2938 H  H    A ALA   A 1 134 ? 16.406 -3.111  -7.561  0.68 16.04 ?  134 ALA   A H    1 
ATOM   2939 H  H    B ALA   A 1 134 ? 16.441 -3.100  -7.533  0.32 15.34 ?  134 ALA   A H    1 
ATOM   2940 H  HA   A ALA   A 1 134 ? 15.592 -4.891  -9.404  0.68 16.62 ?  134 ALA   A HA   1 
ATOM   2941 H  HA   B ALA   A 1 134 ? 15.259 -4.840  -9.200  0.32 15.40 ?  134 ALA   A HA   1 
ATOM   2942 H  HB1  A ALA   A 1 134 ? 16.493 -6.512  -8.000  0.68 18.09 ?  134 ALA   A HB1  1 
ATOM   2943 H  HB1  B ALA   A 1 134 ? 16.145 -6.508  -7.837  0.32 15.85 ?  134 ALA   A HB1  1 
ATOM   2944 H  HB2  A ALA   A 1 134 ? 17.570 -5.375  -8.270  0.68 18.09 ?  134 ALA   A HB2  1 
ATOM   2945 H  HB2  B ALA   A 1 134 ? 17.290 -5.497  -8.275  0.32 15.85 ?  134 ALA   A HB2  1 
ATOM   2946 H  HB3  A ALA   A 1 134 ? 16.776 -5.407  -6.895  0.68 18.09 ?  134 ALA   A HB3  1 
ATOM   2947 H  HB3  B ALA   A 1 134 ? 16.663 -5.405  -6.818  0.32 15.85 ?  134 ALA   A HB3  1 
ATOM   2948 N  N    A ASP   A 1 135 ? 13.753 -6.204  -8.187  0.68 13.76 ?  135 ASP   A N    1 
ATOM   2949 N  N    B ASP   A 1 135 ? 13.436 -5.917  -7.859  0.32 12.83 ?  135 ASP   A N    1 
ATOM   2950 C  CA   A ASP   A 1 135 ? 12.488 -6.683  -7.638  0.68 14.29 ?  135 ASP   A CA   1 
ATOM   2951 C  CA   B ASP   A 1 135 ? 12.193 -6.300  -7.204  0.32 13.29 ?  135 ASP   A CA   1 
ATOM   2952 C  C    A ASP   A 1 135 ? 12.704 -7.117  -6.195  0.68 13.92 ?  135 ASP   A C    1 
ATOM   2953 C  C    B ASP   A 1 135 ? 12.499 -6.799  -5.797  0.32 12.50 ?  135 ASP   A C    1 
ATOM   2954 O  O    A ASP   A 1 135 ? 13.500 -8.032  -5.950  0.68 13.92 ?  135 ASP   A O    1 
ATOM   2955 O  O    B ASP   A 1 135 ? 13.246 -7.776  -5.646  0.32 12.32 ?  135 ASP   A O    1 
ATOM   2956 C  CB   A ASP   A 1 135 ? 12.013 -7.869  -8.471  0.68 16.42 ?  135 ASP   A CB   1 
ATOM   2957 C  CB   B ASP   A 1 135 ? 11.542 -7.414  -8.016  0.32 14.44 ?  135 ASP   A CB   1 
ATOM   2958 C  CG   A ASP   A 1 135 ? 10.726 -8.499  -7.947  0.68 18.57 ?  135 ASP   A CG   1 
ATOM   2959 C  CG   B ASP   A 1 135 ? 10.136 -7.739  -7.553  0.32 15.59 ?  135 ASP   A CG   1 
ATOM   2960 O  OD1  A ASP   A 1 135 ? 10.177 -8.046  -6.924  0.68 18.77 ?  135 ASP   A OD1  1 
ATOM   2961 O  OD1  B ASP   A 1 135 ? 9.795  -7.416  -6.394  0.32 15.58 ?  135 ASP   A OD1  1 
ATOM   2962 O  OD2  A ASP   A 1 135 ? 10.255 -9.466  -8.580  0.68 20.86 -1 135 ASP   A OD2  1 
ATOM   2963 O  OD2  B ASP   A 1 135 ? 9.379  -8.341  -8.344  0.32 16.70 -1 135 ASP   A OD2  1 
ATOM   2964 H  H    A ASP   A 1 135 ? 14.120 -6.748  -8.744  0.68 16.52 ?  135 ASP   A H    1 
ATOM   2965 H  H    B ASP   A 1 135 ? 13.665 -6.447  -8.493  0.32 15.40 ?  135 ASP   A H    1 
ATOM   2966 H  HA   A ASP   A 1 135 ? 11.825 -5.977  -7.683  0.68 17.15 ?  135 ASP   A HA   1 
ATOM   2967 H  HA   B ASP   A 1 135 ? 11.585 -5.538  -7.176  0.32 15.95 ?  135 ASP   A HA   1 
ATOM   2968 H  HB2  A ASP   A 1 135 ? 11.844 -7.572  -9.376  0.68 19.71 ?  135 ASP   A HB2  1 
ATOM   2969 H  HB2  B ASP   A 1 135 ? 11.530 -7.153  -8.953  0.32 17.33 ?  135 ASP   A HB2  1 
ATOM   2970 H  HB3  A ASP   A 1 135 ? 12.700 -8.553  -8.466  0.68 19.71 ?  135 ASP   A HB3  1 
ATOM   2971 H  HB3  B ASP   A 1 135 ? 12.054 -8.224  -7.903  0.32 17.33 ?  135 ASP   A HB3  1 
ATOM   2972 N  N    A PRO   A 1 136 ? 12.030 -6.507  -5.218  0.68 13.70 ?  136 PRO   A N    1 
ATOM   2973 N  N    B PRO   A 1 136 ? 11.959 -6.172  -4.749  0.32 12.06 ?  136 PRO   A N    1 
ATOM   2974 C  CA   A PRO   A 1 136 ? 12.258 -6.905  -3.818  0.68 14.02 ?  136 PRO   A CA   1 
ATOM   2975 C  CA   B PRO   A 1 136 ? 12.242 -6.649  -3.385  0.32 12.43 ?  136 PRO   A CA   1 
ATOM   2976 C  C    A PRO   A 1 136 ? 11.840 -8.330  -3.498  0.68 13.25 ?  136 PRO   A C    1 
ATOM   2977 C  C    B PRO   A 1 136 ? 11.817 -8.085  -3.135  0.32 12.06 ?  136 PRO   A C    1 
ATOM   2978 O  O    A PRO   A 1 136 ? 12.442 -8.950  -2.615  0.68 13.29 ?  136 PRO   A O    1 
ATOM   2979 O  O    B PRO   A 1 136 ? 12.397 -8.748  -2.266  0.32 11.59 ?  136 PRO   A O    1 
ATOM   2980 C  CB   A PRO   A 1 136 ? 11.450 -5.871  -3.022  0.68 14.69 ?  136 PRO   A CB   1 
ATOM   2981 C  CB   B PRO   A 1 136 ? 11.475 -5.654  -2.499  0.32 12.92 ?  136 PRO   A CB   1 
ATOM   2982 C  CG   A PRO   A 1 136 ? 10.409 -5.380  -3.984  0.68 15.07 ?  136 PRO   A CG   1 
ATOM   2983 C  CG   B PRO   A 1 136 ? 10.421 -5.081  -3.396  0.32 12.99 ?  136 PRO   A CG   1 
ATOM   2984 C  CD   A PRO   A 1 136 ? 11.056 -5.406  -5.333  0.68 14.51 ?  136 PRO   A CD   1 
ATOM   2985 C  CD   B PRO   A 1 136 ? 11.066 -5.002  -4.745  0.32 12.27 ?  136 PRO   A CD   1 
ATOM   2986 H  HA   A PRO   A 1 136 ? 13.197 -6.804  -3.595  0.68 16.82 ?  136 PRO   A HA   1 
ATOM   2987 H  HA   B PRO   A 1 136 ? 13.189 -6.565  -3.197  0.32 14.92 ?  136 PRO   A HA   1 
ATOM   2988 H  HB2  A PRO   A 1 136 ? 11.038 -6.298  -2.252  0.68 17.63 ?  136 PRO   A HB2  1 
ATOM   2989 H  HB2  B PRO   A 1 136 ? 11.074 -6.119  -1.751  0.32 15.51 ?  136 PRO   A HB2  1 
ATOM   2990 H  HB3  A PRO   A 1 136 ? 12.033 -5.148  -2.739  0.68 17.63 ?  136 PRO   A HB3  1 
ATOM   2991 H  HB3  B PRO   A 1 136 ? 12.076 -4.956  -2.190  0.32 15.51 ?  136 PRO   A HB3  1 
ATOM   2992 H  HG2  A PRO   A 1 136 ? 9.642  -5.969  -3.960  0.68 18.08 ?  136 PRO   A HG2  1 
ATOM   2993 H  HG2  B PRO   A 1 136 ? 9.650  -5.671  -3.419  0.32 15.59 ?  136 PRO   A HG2  1 
ATOM   2994 H  HG3  A PRO   A 1 136 ? 10.154 -4.474  -3.748  0.68 18.08 ?  136 PRO   A HG3  1 
ATOM   2995 H  HG3  B PRO   A 1 136 ? 10.168 -4.198  -3.089  0.32 15.59 ?  136 PRO   A HG3  1 
ATOM   2996 H  HD2  A PRO   A 1 136 ? 10.397 -5.611  -6.017  0.68 17.42 ?  136 PRO   A HD2  1 
ATOM   2997 H  HD2  B PRO   A 1 136 ? 10.394 -5.080  -5.444  0.32 14.73 ?  136 PRO   A HD2  1 
ATOM   2998 H  HD3  A PRO   A 1 136 ? 11.508 -4.569  -5.515  0.68 17.42 ?  136 PRO   A HD3  1 
ATOM   2999 H  HD3  B PRO   A 1 136 ? 11.576 -4.180  -4.836  0.32 14.73 ?  136 PRO   A HD3  1 
ATOM   3000 N  N    A ILE   A 1 137 ? 10.813 -8.861  -4.165  0.68 13.51 ?  137 ILE   A N    1 
ATOM   3001 N  N    B ILE   A 1 137 ? 10.810 -8.581  -3.858  0.32 12.41 ?  137 ILE   A N    1 
ATOM   3002 C  CA   A ILE   A 1 137 ? 10.450 -10.261 -3.956  0.68 13.79 ?  137 ILE   A CA   1 
ATOM   3003 C  CA   B ILE   A 1 137 ? 10.404 -9.979  -3.715  0.32 12.84 ?  137 ILE   A CA   1 
ATOM   3004 C  C    A ILE   A 1 137 ? 11.615 -11.159 -4.339  0.68 13.25 ?  137 ILE   A C    1 
ATOM   3005 C  C    B ILE   A 1 137 ? 11.550 -10.902 -4.113  0.32 12.44 ?  137 ILE   A C    1 
ATOM   3006 O  O    A ILE   A 1 137 ? 11.930 -12.133 -3.644  0.68 13.46 ?  137 ILE   A O    1 
ATOM   3007 O  O    B ILE   A 1 137 ? 11.868 -11.872 -3.414  0.32 12.33 ?  137 ILE   A O    1 
ATOM   3008 C  CB   A ILE   A 1 137 ? 9.166  -10.609 -4.734  0.68 15.17 ?  137 ILE   A CB   1 
ATOM   3009 C  CB   B ILE   A 1 137 ? 9.136  -10.258 -4.546  0.32 13.64 ?  137 ILE   A CB   1 
ATOM   3010 C  CG1  A ILE   A 1 137 ? 7.970  -9.811  -4.195  0.68 16.55 ?  137 ILE   A CG1  1 
ATOM   3011 C  CG1  B ILE   A 1 137 ? 8.028  -9.251  -4.216  0.32 14.71 ?  137 ILE   A CG1  1 
ATOM   3012 C  CG2  A ILE   A 1 137 ? 8.893  -12.113 -4.666  0.68 15.19 ?  137 ILE   A CG2  1 
ATOM   3013 C  CG2  B ILE   A 1 137 ? 8.651  -11.690 -4.316  0.32 13.91 ?  137 ILE   A CG2  1 
ATOM   3014 C  CD1  A ILE   A 1 137 ? 6.690  -10.008 -4.984  0.68 17.83 ?  137 ILE   A CD1  1 
ATOM   3015 C  CD1  B ILE   A 1 137 ? 6.789  -9.423  -5.066  0.32 15.34 ?  137 ILE   A CD1  1 
ATOM   3016 H  H    A ILE   A 1 137 ? 10.320 -8.444  -4.731  0.68 16.21 ?  137 ILE   A H    1 
ATOM   3017 H  H    B ILE   A 1 137 ? 10.347 -8.126  -4.428  0.32 14.90 ?  137 ILE   A H    1 
ATOM   3018 H  HA   A ILE   A 1 137 ? 10.272 -10.405 -3.017  0.68 16.56 ?  137 ILE   A HA   1 
ATOM   3019 H  HA   B ILE   A 1 137 ? 10.187 -10.149 -2.785  0.32 15.41 ?  137 ILE   A HA   1 
ATOM   3020 H  HB   A ILE   A 1 137 ? 9.295  -10.372 -5.664  0.68 18.21 ?  137 ILE   A HB   1 
ATOM   3021 H  HB   B ILE   A 1 137 ? 9.358  -10.159 -5.482  0.32 16.37 ?  137 ILE   A HB   1 
ATOM   3022 H  HG12 A ILE   A 1 137 ? 7.803  -10.080 -3.278  0.68 19.87 ?  137 ILE   A HG12 1 
ATOM   3023 H  HG12 B ILE   A 1 137 ? 7.771  -9.355  -3.288  0.32 17.65 ?  137 ILE   A HG12 1 
ATOM   3024 H  HG13 A ILE   A 1 137 ? 8.195  -8.865  -4.222  0.68 19.87 ?  137 ILE   A HG13 1 
ATOM   3025 H  HG13 B ILE   A 1 137 ? 8.355  -8.348  -4.367  0.32 17.65 ?  137 ILE   A HG13 1 
ATOM   3026 H  HG21 A ILE   A 1 137 ? 7.988  -12.304 -4.964  0.68 18.24 ?  137 ILE   A HG21 1 
ATOM   3027 H  HG21 B ILE   A 1 137 ? 7.881  -11.866 -4.879  0.32 16.69 ?  137 ILE   A HG21 1 
ATOM   3028 H  HG22 A ILE   A 1 137 ? 9.523  -12.576 -5.240  0.68 18.24 ?  137 ILE   A HG22 1 
ATOM   3029 H  HG22 B ILE   A 1 137 ? 9.364  -12.304 -4.543  0.32 16.69 ?  137 ILE   A HG22 1 
ATOM   3030 H  HG23 A ILE   A 1 137 ? 8.999  -12.411 -3.750  0.68 18.24 ?  137 ILE   A HG23 1 
ATOM   3031 H  HG23 B ILE   A 1 137 ? 8.408  -11.793 -3.384  0.32 16.69 ?  137 ILE   A HG23 1 
ATOM   3032 H  HD11 A ILE   A 1 137 ? 5.987  -10.282 -4.378  0.68 21.40 ?  137 ILE   A HD11 1 
ATOM   3033 H  HD11 B ILE   A 1 137 ? 6.047  -9.677  -4.494  0.32 18.41 ?  137 ILE   A HD11 1 
ATOM   3034 H  HD12 A ILE   A 1 137 ? 6.464  -9.168  -5.406  0.68 21.40 ?  137 ILE   A HD12 1 
ATOM   3035 H  HD12 B ILE   A 1 137 ? 6.597  -8.587  -5.513  0.32 18.41 ?  137 ILE   A HD12 1 
ATOM   3036 H  HD13 A ILE   A 1 137 ? 6.830  -10.683 -5.664  0.68 21.40 ?  137 ILE   A HD13 1 
ATOM   3037 H  HD13 B ILE   A 1 137 ? 6.949  -10.114 -5.728  0.32 18.41 ?  137 ILE   A HD13 1 
ATOM   3038 N  N    A HIS   A 1 138 ? 12.281 -10.833 -5.447  0.68 13.59 ?  138 HIS   A N    1 
ATOM   3039 N  N    B HIS   A 1 138 ? 12.182 -10.612 -5.253  0.32 12.72 ?  138 HIS   A N    1 
ATOM   3040 C  CA   A HIS   A 1 138 ? 13.485 -11.556 -5.828  0.68 13.71 ?  138 HIS   A CA   1 
ATOM   3041 C  CA   B HIS   A 1 138 ? 13.299 -11.426 -5.724  0.32 12.75 ?  138 HIS   A CA   1 
ATOM   3042 C  C    A HIS   A 1 138 ? 14.599 -11.372 -4.800  0.68 13.22 ?  138 HIS   A C    1 
ATOM   3043 C  C    B HIS   A 1 138 ? 14.476 -11.353 -4.759  0.32 12.81 ?  138 HIS   A C    1 
ATOM   3044 O  O    A HIS   A 1 138 ? 15.290 -12.338 -4.450  0.68 13.54 ?  138 HIS   A O    1 
ATOM   3045 O  O    B HIS   A 1 138 ? 15.088 -12.375 -4.423  0.32 13.35 ?  138 HIS   A O    1 
ATOM   3046 C  CB   A HIS   A 1 138 ? 13.937 -11.128 -7.222  0.68 15.02 ?  138 HIS   A CB   1 
ATOM   3047 C  CB   B HIS   A 1 138 ? 13.711 -10.953 -7.121  0.32 12.88 ?  138 HIS   A CB   1 
ATOM   3048 C  CG   A HIS   A 1 138 ? 15.180 -11.821 -7.681  0.68 15.75 ?  138 HIS   A CG   1 
ATOM   3049 C  CG   B HIS   A 1 138 ? 15.008 -11.528 -7.598  0.32 13.18 ?  138 HIS   A CG   1 
ATOM   3050 N  ND1  A HIS   A 1 138 ? 15.243 -13.184 -7.881  0.68 16.94 ?  138 HIS   A ND1  1 
ATOM   3051 N  ND1  B HIS   A 1 138 ? 15.145 -12.847 -7.973  0.32 14.13 ?  138 HIS   A ND1  1 
ATOM   3052 C  CD2  A HIS   A 1 138 ? 16.416 -11.342 -7.952  0.68 15.82 ?  138 HIS   A CD2  1 
ATOM   3053 C  CD2  B HIS   A 1 138 ? 16.228 -10.962 -7.761  0.32 12.75 ?  138 HIS   A CD2  1 
ATOM   3054 C  CE1  A HIS   A 1 138 ? 16.460 -13.512 -8.273  0.68 17.46 ?  138 HIS   A CE1  1 
ATOM   3055 C  CE1  B HIS   A 1 138 ? 16.392 -13.068 -8.349  0.32 13.93 ?  138 HIS   A CE1  1 
ATOM   3056 N  NE2  A HIS   A 1 138 ? 17.193 -12.413 -8.322  0.68 16.49 ?  138 HIS   A NE2  1 
ATOM   3057 N  NE2  B HIS   A 1 138 ? 17.071 -11.942 -8.227  0.32 13.21 ?  138 HIS   A NE2  1 
ATOM   3058 H  H    A HIS   A 1 138 ? 12.050 -10.204 -5.993  0.68 16.31 ?  138 HIS   A H    1 
ATOM   3059 H  H    B HIS   A 1 138 ? 11.984 -9.946  -5.763  0.32 15.26 ?  138 HIS   A H    1 
ATOM   3060 H  HA   A HIS   A 1 138 ? 13.274 -12.500 -5.871  0.68 16.46 ?  138 HIS   A HA   1 
ATOM   3061 H  HA   B HIS   A 1 138 ? 13.012 -12.348 -5.788  0.32 15.30 ?  138 HIS   A HA   1 
ATOM   3062 H  HB2  A HIS   A 1 138 ? 13.229 -11.334 -7.859  0.68 18.03 ?  138 HIS   A HB2  1 
ATOM   3063 H  HB2  B HIS   A 1 138 ? 13.020 -11.213 -7.755  0.32 15.46 ?  138 HIS   A HB2  1 
ATOM   3064 H  HB3  A HIS   A 1 138 ? 14.107 -10.175 -7.222  0.68 18.03 ?  138 HIS   A HB3  1 
ATOM   3065 H  HB3  B HIS   A 1 138 ? 13.798 -9.987  -7.113  0.32 15.46 ?  138 HIS   A HB3  1 
ATOM   3066 H  HD1  A HIS   A 1 138 ? 14.585 -13.731 -7.778  0.68 20.33 ?  138 HIS   A HD1  1 
ATOM   3067 H  HD2  A HIS   A 1 138 ? 16.681 -10.453 -7.901  0.68 18.99 ?  138 HIS   A HD2  1 
ATOM   3068 H  HD2  B HIS   A 1 138 ? 16.451 -10.076 -7.589  0.32 15.30 ?  138 HIS   A HD2  1 
ATOM   3069 H  HE1  A HIS   A 1 138 ? 16.751 -14.369 -8.473  0.68 20.95 ?  138 HIS   A HE1  1 
ATOM   3070 H  HE1  B HIS   A 1 138 ? 16.734 -13.881 -8.643  0.32 16.72 ?  138 HIS   A HE1  1 
ATOM   3071 H  HE2  B HIS   A 1 138 ? 17.903 -11.838 -8.411  0.32 15.86 ?  138 HIS   A HE2  1 
ATOM   3072 N  N    . SER   A 1 139 ? 14.802 -10.146 -4.306  1.00 12.64 ?  139 SER   A N    1 
ATOM   3073 C  CA   . SER   A 1 139 ? 15.868 -9.953  -3.334  1.00 12.32 ?  139 SER   A CA   1 
ATOM   3074 C  C    . SER   A 1 139 ? 15.645 -10.791 -2.080  1.00 11.86 ?  139 SER   A C    1 
ATOM   3075 O  O    . SER   A 1 139 ? 16.591 -11.383 -1.548  1.00 12.15 ?  139 SER   A O    1 
ATOM   3076 C  CB   . SER   A 1 139 ? 15.990 -8.476  -2.978  1.00 12.37 ?  139 SER   A CB   1 
ATOM   3077 O  OG   . SER   A 1 139 ? 17.060 -8.298  -2.069  1.00 12.74 ?  139 SER   A OG   1 
ATOM   3078 H  H    A SER   A 1 139 ? 14.355 -9.439  -4.512  0.68 15.17 ?  139 SER   A H    1 
ATOM   3079 H  H    B SER   A 1 139 ? 14.409 -9.417  -4.545  0.32 15.17 ?  139 SER   A H    1 
ATOM   3080 H  HA   . SER   A 1 139 ? 16.709 -10.229 -3.732  1.00 14.79 ?  139 SER   A HA   1 
ATOM   3081 H  HB2  . SER   A 1 139 ? 16.163 -7.959  -3.783  1.00 14.85 ?  139 SER   A HB2  1 
ATOM   3082 H  HB3  . SER   A 1 139 ? 15.163 -8.174  -2.562  1.00 14.85 ?  139 SER   A HB3  1 
ATOM   3083 H  HG   . SER   A 1 139 ? 17.136 -7.483  -1.864  1.00 15.30 ?  139 SER   A HG   1 
ATOM   3084 N  N    A LEU   A 1 140 ? 14.396 -10.901 -1.627  0.68 11.89 ?  140 LEU   A N    1 
ATOM   3085 N  N    B LEU   A 1 140 ? 14.420 -10.775 -1.544  0.32 11.09 ?  140 LEU   A N    1 
ATOM   3086 C  CA   A LEU   A 1 140 ? 14.121 -11.749 -0.472  0.68 11.97 ?  140 LEU   A CA   1 
ATOM   3087 C  CA   B LEU   A 1 140 ? 14.141 -11.537 -0.330  0.32 10.68 ?  140 LEU   A CA   1 
ATOM   3088 C  C    A LEU   A 1 140 ? 14.404 -13.216 -0.783  0.68 11.95 ?  140 LEU   A C    1 
ATOM   3089 C  C    B LEU   A 1 140 ? 14.391 -13.023 -0.552  0.32 10.77 ?  140 LEU   A C    1 
ATOM   3090 O  O    A LEU   A 1 140 ? 14.976 -13.934 0.048   0.68 12.38 ?  140 LEU   A O    1 
ATOM   3091 O  O    B LEU   A 1 140 ? 14.904 -13.716 0.336   0.32 11.05 ?  140 LEU   A O    1 
ATOM   3092 C  CB   A LEU   A 1 140 ? 12.679 -11.552 -0.012  0.68 12.57 ?  140 LEU   A CB   1 
ATOM   3093 C  CB   B LEU   A 1 140 ? 12.701 -11.293 0.130   0.32 10.52 ?  140 LEU   A CB   1 
ATOM   3094 C  CG   A LEU   A 1 140 ? 12.224 -12.405 1.173   0.68 13.21 ?  140 LEU   A CG   1 
ATOM   3095 C  CG   B LEU   A 1 140 ? 12.224 -12.184 1.282   0.32 10.83 ?  140 LEU   A CG   1 
ATOM   3096 C  CD1  A LEU   A 1 140 ? 13.176 -12.273 2.350   0.68 13.26 ?  140 LEU   A CD1  1 
ATOM   3097 C  CD1  B LEU   A 1 140 ? 12.988 -11.876 2.564   0.32 10.36 ?  140 LEU   A CD1  1 
ATOM   3098 C  CD2  A LEU   A 1 140 ? 10.801 -12.014 1.582   0.68 14.38 ?  140 LEU   A CD2  1 
ATOM   3099 C  CD2  B LEU   A 1 140 ? 10.720 -12.056 1.492   0.32 11.76 ?  140 LEU   A CD2  1 
ATOM   3100 H  H    A LEU   A 1 140 ? 13.709 -10.507 -1.964  0.68 14.28 ?  140 LEU   A H    1 
ATOM   3101 H  H    B LEU   A 1 140 ? 13.750 -10.331 -1.857  0.32 13.31 ?  140 LEU   A H    1 
ATOM   3102 H  HA   A LEU   A 1 140 ? 14.705 -11.485 0.249   0.68 14.37 ?  140 LEU   A HA   1 
ATOM   3103 H  HA   B LEU   A 1 140 ? 14.731 -11.229 0.377   0.32 12.83 ?  140 LEU   A HA   1 
ATOM   3104 H  HB2  A LEU   A 1 140 ? 12.567 -10.627 0.240   0.68 15.09 ?  140 LEU   A HB2  1 
ATOM   3105 H  HB2  B LEU   A 1 140 ? 12.619 -10.369 0.425   0.32 12.63 ?  140 LEU   A HB2  1 
ATOM   3106 H  HB3  A LEU   A 1 140 ? 12.093 -11.761 -0.757  0.68 15.09 ?  140 LEU   A HB3  1 
ATOM   3107 H  HB3  B LEU   A 1 140 ? 12.105 -11.444 -0.620  0.32 12.63 ?  140 LEU   A HB3  1 
ATOM   3108 H  HG   A LEU   A 1 140 ? 12.208 -13.339 0.903   0.68 15.86 ?  140 LEU   A HG   1 
ATOM   3109 H  HG   B LEU   A 1 140 ? 12.395 -13.108 1.059   0.32 13.00 ?  140 LEU   A HG   1 
ATOM   3110 H  HD11 A LEU   A 1 140 ? 12.792 -12.726 3.118   0.68 15.91 ?  140 LEU   A HD11 1 
ATOM   3111 H  HD11 B LEU   A 1 140 ? 12.639 -12.433 3.277   0.32 12.44 ?  140 LEU   A HD11 1 
ATOM   3112 H  HD12 A LEU   A 1 140 ? 14.025 -12.686 2.119   0.68 15.91 ?  140 LEU   A HD12 1 
ATOM   3113 H  HD12 B LEU   A 1 140 ? 13.927 -12.068 2.423   0.32 12.44 ?  140 LEU   A HD12 1 
ATOM   3114 H  HD13 A LEU   A 1 140 ? 13.306 -11.335 2.548   0.68 15.91 ?  140 LEU   A HD13 1 
ATOM   3115 H  HD13 B LEU   A 1 140 ? 12.869 -10.940 2.786   0.32 12.44 ?  140 LEU   A HD13 1 
ATOM   3116 H  HD21 A LEU   A 1 140 ? 10.526 -12.564 2.335   0.68 17.26 ?  140 LEU   A HD21 1 
ATOM   3117 H  HD21 B LEU   A 1 140 ? 10.444 -12.693 2.174   0.32 14.11 ?  140 LEU   A HD21 1 
ATOM   3118 H  HD22 A LEU   A 1 140 ? 10.791 -11.079 1.838   0.68 17.26 ?  140 LEU   A HD22 1 
ATOM   3119 H  HD22 B LEU   A 1 140 ? 10.516 -11.156 1.780   0.32 14.11 ?  140 LEU   A HD22 1 
ATOM   3120 H  HD23 A LEU   A 1 140 ? 10.202 -12.160 0.833   0.68 17.26 ?  140 LEU   A HD23 1 
ATOM   3121 H  HD23 B LEU   A 1 140 ? 10.267 -12.253 0.657   0.32 14.11 ?  140 LEU   A HD23 1 
ATOM   3122 N  N    A ARG   A 1 141 ? 14.007 -13.677 -1.972  0.68 12.38 ?  141 ARG   A N    1 
ATOM   3123 N  N    B ARG   A 1 141 ? 14.026 -13.531 -1.731  0.32 11.25 ?  141 ARG   A N    1 
ATOM   3124 C  CA   A ARG   A 1 141 ? 14.262 -15.060 -2.362  0.68 13.45 ?  141 ARG   A CA   1 
ATOM   3125 C  CA   B ARG   A 1 141 ? 14.247 -14.943 -2.021  0.32 11.46 ?  141 ARG   A CA   1 
ATOM   3126 C  C    A ARG   A 1 141 ? 15.756 -15.362 -2.341  0.68 13.30 ?  141 ARG   A C    1 
ATOM   3127 C  C    B ARG   A 1 141 ? 15.736 -15.249 -2.126  0.32 11.34 ?  141 ARG   A C    1 
ATOM   3128 O  O    A ARG   A 1 141 ? 16.188 -16.391 -1.807  0.68 13.51 ?  141 ARG   A O    1 
ATOM   3129 O  O    B ARG   A 1 141 ? 16.220 -16.235 -1.556  0.32 11.57 ?  141 ARG   A O    1 
ATOM   3130 C  CB   A ARG   A 1 141 ? 13.680 -15.300 -3.756  0.68 14.92 ?  141 ARG   A CB   1 
ATOM   3131 C  CB   B ARG   A 1 141 ? 13.510 -15.345 -3.301  0.32 11.77 ?  141 ARG   A CB   1 
ATOM   3132 C  CG   A ARG   A 1 141 ? 13.620 -16.757 -4.176  0.68 17.31 ?  141 ARG   A CG   1 
ATOM   3133 C  CG   B ARG   A 1 141 ? 13.689 -16.818 -3.683  0.32 12.47 ?  141 ARG   A CG   1 
ATOM   3134 C  CD   A ARG   A 1 141 ? 12.592 -17.500 -3.358  0.68 18.71 ?  141 ARG   A CD   1 
ATOM   3135 C  CD   B ARG   A 1 141 ? 13.082 -17.748 -2.643  0.32 13.25 ?  141 ARG   A CD   1 
ATOM   3136 N  NE   A ARG   A 1 141 ? 13.211 -18.290 -2.304  0.68 19.71 ?  141 ARG   A NE   1 
ATOM   3137 N  NE   B ARG   A 1 141 ? 11.649 -17.522 -2.503  0.32 13.80 ?  141 ARG   A NE   1 
ATOM   3138 C  CZ   A ARG   A 1 141 ? 12.538 -18.857 -1.311  0.68 20.35 ?  141 ARG   A CZ   1 
ATOM   3139 C  CZ   B ARG   A 1 141 ? 10.888 -18.068 -1.564  0.32 14.00 ?  141 ARG   A CZ   1 
ATOM   3140 N  NH1  A ARG   A 1 141 ? 11.243 -18.646 -1.146  0.68 20.85 ?  141 ARG   A NH1  1 
ATOM   3141 N  NH1  B ARG   A 1 141 ? 11.390 -18.889 -0.655  0.32 14.05 ?  141 ARG   A NH1  1 
ATOM   3142 N  NH2  A ARG   A 1 141 ? 13.180 -19.653 -0.463  0.68 20.66 ?  141 ARG   A NH2  1 
ATOM   3143 N  NH2  B ARG   A 1 141 ? 9.589  -17.782 -1.537  0.32 14.70 ?  141 ARG   A NH2  1 
ATOM   3144 H  H    A ARG   A 1 141 ? 13.584 -13.218 -2.565  0.68 14.86 ?  141 ARG   A H    1 
ATOM   3145 H  H    B ARG   A 1 141 ? 13.650 -13.082 -2.364  0.32 13.51 ?  141 ARG   A H    1 
ATOM   3146 H  HA   A ARG   A 1 141 ? 13.824 -15.659 -1.738  0.68 16.14 ?  141 ARG   A HA   1 
ATOM   3147 H  HA   B ARG   A 1 141 ? 13.885 -15.466 -1.293  0.32 13.76 ?  141 ARG   A HA   1 
ATOM   3148 H  HB2  A ARG   A 1 141 ? 12.775 -14.952 -3.778  0.68 17.90 ?  141 ARG   A HB2  1 
ATOM   3149 H  HB2  B ARG   A 1 141 ? 12.556 -15.183 -3.178  0.32 14.13 ?  141 ARG   A HB2  1 
ATOM   3150 H  HB3  A ARG   A 1 141 ? 14.226 -14.834 -4.404  0.68 17.90 ?  141 ARG   A HB3  1 
ATOM   3151 H  HB3  B ARG   A 1 141 ? 13.836 -14.803 -4.036  0.32 14.13 ?  141 ARG   A HB3  1 
ATOM   3152 H  HG2  A ARG   A 1 141 ? 13.369 -16.817 -5.112  0.68 20.77 ?  141 ARG   A HG2  1 
ATOM   3153 H  HG2  B ARG   A 1 141 ? 13.245 -16.982 -4.530  0.32 14.97 ?  141 ARG   A HG2  1 
ATOM   3154 H  HG3  A ARG   A 1 141 ? 14.486 -17.176 -4.033  0.68 20.77 ?  141 ARG   A HG3  1 
ATOM   3155 H  HG3  B ARG   A 1 141 ? 14.635 -17.021 -3.760  0.32 14.97 ?  141 ARG   A HG3  1 
ATOM   3156 H  HD2  A ARG   A 1 141 ? 11.993 -16.862 -2.941  0.68 22.45 ?  141 ARG   A HD2  1 
ATOM   3157 H  HD2  B ARG   A 1 141 ? 13.216 -18.665 -2.918  0.32 15.91 ?  141 ARG   A HD2  1 
ATOM   3158 H  HD3  A ARG   A 1 141 ? 12.092 -18.097 -3.939  0.68 22.45 ?  141 ARG   A HD3  1 
ATOM   3159 H  HD3  B ARG   A 1 141 ? 13.501 -17.590 -1.782  0.32 15.91 ?  141 ARG   A HD3  1 
ATOM   3160 H  HE   A ARG   A 1 141 ? 14.046 -18.482 -2.386  0.68 23.65 ?  141 ARG   A HE   1 
ATOM   3161 H  HE   B ARG   A 1 141 ? 11.268 -16.998 -3.070  0.32 16.57 ?  141 ARG   A HE   1 
ATOM   3162 H  HH11 A ARG   A 1 141 ? 10.812 -18.145 -1.694  0.68 25.03 ?  141 ARG   A HH11 1 
ATOM   3163 H  HH11 B ARG   A 1 141 ? 12.226 -19.084 -0.665  0.32 16.87 ?  141 ARG   A HH11 1 
ATOM   3164 H  HH12 A ARG   A 1 141 ? 10.828 -19.025 -0.493  0.68 25.03 ?  141 ARG   A HH12 1 
ATOM   3165 H  HH12 B ARG   A 1 141 ? 10.874 -19.234 -0.060  0.32 16.87 ?  141 ARG   A HH12 1 
ATOM   3166 H  HH21 A ARG   A 1 141 ? 14.026 -19.792 -0.560  0.68 24.79 ?  141 ARG   A HH21 1 
ATOM   3167 H  HH21 B ARG   A 1 141 ? 9.252  -17.248 -2.122  0.32 17.65 ?  141 ARG   A HH21 1 
ATOM   3168 H  HH22 A ARG   A 1 141 ? 12.759 -20.017 0.191   0.68 24.79 ?  141 ARG   A HH22 1 
ATOM   3169 H  HH22 B ARG   A 1 141 ? 9.084  -18.131 -0.934  0.32 17.65 ?  141 ARG   A HH22 1 
ATOM   3170 N  N    A VAL   A 1 142 ? 16.565 -14.475 -2.924  0.68 12.75 ?  142 VAL   A N    1 
ATOM   3171 N  N    B VAL   A 1 142 ? 16.484 -14.409 -2.848  0.32 11.46 ?  142 VAL   A N    1 
ATOM   3172 C  CA   A VAL   A 1 142 ? 18.010 -14.688 -2.923  0.68 12.49 ?  142 VAL   A CA   1 
ATOM   3173 C  CA   B VAL   A 1 142 ? 17.930 -14.602 -2.937  0.32 11.73 ?  142 VAL   A CA   1 
ATOM   3174 C  C    A VAL   A 1 142 ? 18.557 -14.652 -1.502  0.68 12.13 ?  142 VAL   A C    1 
ATOM   3175 C  C    B VAL   A 1 142 ? 18.543 -14.617 -1.543  0.32 11.72 ?  142 VAL   A C    1 
ATOM   3176 O  O    A VAL   A 1 142 ? 19.411 -15.468 -1.135  0.68 12.50 ?  142 VAL   A O    1 
ATOM   3177 O  O    B VAL   A 1 142 ? 19.424 -15.431 -1.240  0.32 11.87 ?  142 VAL   A O    1 
ATOM   3178 C  CB   A VAL   A 1 142 ? 18.726 -13.688 -3.851  0.68 12.52 ?  142 VAL   A CB   1 
ATOM   3179 C  CB   B VAL   A 1 142 ? 18.567 -13.524 -3.836  0.32 12.14 ?  142 VAL   A CB   1 
ATOM   3180 C  CG1  A VAL   A 1 142 ? 20.235 -13.923 -3.811  0.68 11.79 ?  142 VAL   A CG1  1 
ATOM   3181 C  CG1  B VAL   A 1 142 ? 20.083 -13.626 -3.790  0.32 12.46 ?  142 VAL   A CG1  1 
ATOM   3182 C  CG2  A VAL   A 1 142 ? 18.223 -13.825 -5.278  0.68 13.68 ?  142 VAL   A CG2  1 
ATOM   3183 C  CG2  B VAL   A 1 142 ? 18.083 -13.664 -5.269  0.32 12.50 ?  142 VAL   A CG2  1 
ATOM   3184 H  H    A VAL   A 1 142 ? 16.308 -13.754 -3.323  0.68 15.31 ?  142 VAL   A H    1 
ATOM   3185 H  H    B VAL   A 1 142 ? 16.185 -13.720 -3.281  0.32 13.76 ?  142 VAL   A H    1 
ATOM   3186 H  HA   A VAL   A 1 142 ? 18.187 -15.569 -3.277  0.68 14.99 ?  142 VAL   A HA   1 
ATOM   3187 H  HA   B VAL   A 1 142 ? 18.101 -15.459 -3.349  0.32 14.08 ?  142 VAL   A HA   1 
ATOM   3188 H  HB   A VAL   A 1 142 ? 18.555 -12.778 -3.552  0.68 15.03 ?  142 VAL   A HB   1 
ATOM   3189 H  HB   B VAL   A 1 142 ? 18.314 -12.640 -3.517  0.32 14.57 ?  142 VAL   A HB   1 
ATOM   3190 H  HG11 A VAL   A 1 142 ? 20.651 -13.440 -4.542  0.68 14.15 ?  142 VAL   A HG11 1 
ATOM   3191 H  HG11 B VAL   A 1 142 ? 20.457 -13.052 -4.476  0.32 14.96 ?  142 VAL   A HG11 1 
ATOM   3192 H  HG12 A VAL   A 1 142 ? 20.586 -13.604 -2.965  0.68 14.15 ?  142 VAL   A HG12 1 
ATOM   3193 H  HG12 B VAL   A 1 142 ? 20.396 -13.341 -2.918  0.32 14.96 ?  142 VAL   A HG12 1 
ATOM   3194 H  HG13 A VAL   A 1 142 ? 20.407 -14.873 -3.905  0.68 14.15 ?  142 VAL   A HG13 1 
ATOM   3195 H  HG13 B VAL   A 1 142 ? 20.338 -14.545 -3.951  0.32 14.96 ?  142 VAL   A HG13 1 
ATOM   3196 H  HG21 A VAL   A 1 142 ? 18.717 -13.209 -5.847  0.68 16.42 ?  142 VAL   A HG21 1 
ATOM   3197 H  HG21 B VAL   A 1 142 ? 18.494 -12.969 -5.811  0.32 15.00 ?  142 VAL   A HG21 1 
ATOM   3198 H  HG22 A VAL   A 1 142 ? 18.370 -14.735 -5.575  0.68 16.42 ?  142 VAL   A HG22 1 
ATOM   3199 H  HG22 B VAL   A 1 142 ? 18.343 -14.537 -5.602  0.32 15.00 ?  142 VAL   A HG22 1 
ATOM   3200 H  HG23 A VAL   A 1 142 ? 17.281 -13.612 -5.301  0.68 16.42 ?  142 VAL   A HG23 1 
ATOM   3201 H  HG23 B VAL   A 1 142 ? 17.121 -13.573 -5.288  0.32 15.00 ?  142 VAL   A HG23 1 
ATOM   3202 N  N    . CYS   A 1 143 ? 18.081 -13.717 -0.677  1.00 11.85 ?  143 CYS   A N    1 
ATOM   3203 C  CA   . CYS   A 1 143 ? 18.547 -13.674 0.704   1.00 12.19 ?  143 CYS   A CA   1 
ATOM   3204 C  C    . CYS   A 1 143 ? 18.314 -15.013 1.398   1.00 12.06 ?  143 CYS   A C    1 
ATOM   3205 O  O    . CYS   A 1 143 ? 19.231 -15.599 1.980   1.00 12.07 ?  143 CYS   A O    1 
ATOM   3206 C  CB   . CYS   A 1 143 ? 17.817 -12.559 1.446   1.00 12.57 ?  143 CYS   A CB   1 
ATOM   3207 S  SG   . CYS   A 1 143 ? 18.314 -12.382 3.168   1.00 12.89 ?  143 CYS   A SG   1 
ATOM   3208 H  H    A CYS   A 1 143 ? 17.504 -13.117 -0.887  0.68 14.23 ?  143 CYS   A H    1 
ATOM   3209 H  H    B CYS   A 1 143 ? 17.496 -13.119 -0.867  0.32 14.23 ?  143 CYS   A H    1 
ATOM   3210 H  HA   . CYS   A 1 143 ? 19.497 -13.488 0.720   1.00 14.63 ?  143 CYS   A HA   1 
ATOM   3211 H  HB2  . CYS   A 1 143 ? 17.988 -11.717 0.995   1.00 15.09 ?  143 CYS   A HB2  1 
ATOM   3212 H  HB3  . CYS   A 1 143 ? 16.867 -12.744 1.433   1.00 15.09 ?  143 CYS   A HB3  1 
ATOM   3213 H  HG   . CYS   A 1 143 ? 17.731 -11.444 3.642   1.00 15.47 ?  143 CYS   A HG   1 
ATOM   3214 N  N    . VAL   A 1 144 ? 17.083 -15.512 1.341   1.00 12.80 ?  144 VAL   A N    1 
ATOM   3215 C  CA   . VAL   A 1 144 ? 16.740 -16.750 2.031   1.00 13.82 ?  144 VAL   A CA   1 
ATOM   3216 C  C    . VAL   A 1 144 ? 17.564 -17.917 1.509   1.00 13.63 ?  144 VAL   A C    1 
ATOM   3217 O  O    . VAL   A 1 144 ? 17.925 -18.826 2.268   1.00 14.31 ?  144 VAL   A O    1 
ATOM   3218 C  CB   . VAL   A 1 144 ? 15.228 -16.996 1.885   1.00 16.37 ?  144 VAL   A CB   1 
ATOM   3219 C  CG1  . VAL   A 1 144 ? 14.870 -18.435 2.205   1.00 17.95 ?  144 VAL   A CG1  1 
ATOM   3220 C  CG2  . VAL   A 1 144 ? 14.463 -16.001 2.760   1.00 16.67 ?  144 VAL   A CG2  1 
ATOM   3221 H  H    . VAL   A 1 144 ? 16.425 -15.149 0.910   1.00 15.37 ?  144 VAL   A H    1 
ATOM   3222 H  HA   . VAL   A 1 144 ? 16.926 -16.646 2.973   1.00 16.59 ?  144 VAL   A HA   1 
ATOM   3223 H  HB   . VAL   A 1 144 ? 14.966 -16.827 0.960   1.00 19.65 ?  144 VAL   A HB   1 
ATOM   3224 H  HG11 . VAL   A 1 144 ? 13.913 -18.492 2.384   1.00 21.54 ?  144 VAL   A HG11 1 
ATOM   3225 H  HG12 . VAL   A 1 144 ? 15.091 -18.998 1.447   1.00 21.54 ?  144 VAL   A HG12 1 
ATOM   3226 H  HG13 . VAL   A 1 144 ? 15.364 -18.716 2.988   1.00 21.54 ?  144 VAL   A HG13 1 
ATOM   3227 H  HG21 . VAL   A 1 144 ? 13.508 -16.176 2.690   1.00 20.01 ?  144 VAL   A HG21 1 
ATOM   3228 H  HG22 . VAL   A 1 144 ? 14.747 -16.104 3.681   1.00 20.01 ?  144 VAL   A HG22 1 
ATOM   3229 H  HG23 . VAL   A 1 144 ? 14.649 -15.096 2.456   1.00 20.01 ?  144 VAL   A HG23 1 
ATOM   3230 N  N    . ASP   A 1 145 ? 17.829 -17.940 0.206   1.00 13.72 ?  145 ASP   A N    1 
ATOM   3231 C  CA   . ASP   A 1 145 ? 18.543 -19.044 -0.426  1.00 14.28 ?  145 ASP   A CA   1 
ATOM   3232 C  C    . ASP   A 1 145 ? 20.062 -18.895 -0.379  1.00 14.21 ?  145 ASP   A C    1 
ATOM   3233 O  O    . ASP   A 1 145 ? 20.771 -19.783 -0.867  1.00 16.08 ?  145 ASP   A O    1 
ATOM   3234 C  CB   . ASP   A 1 145 ? 18.096 -19.182 -1.883  1.00 15.70 ?  145 ASP   A CB   1 
ATOM   3235 C  CG   . ASP   A 1 145 ? 16.652 -19.636 -2.015  1.00 18.02 ?  145 ASP   A CG   1 
ATOM   3236 O  OD1  . ASP   A 1 145 ? 16.091 -20.187 -1.042  1.00 18.48 ?  145 ASP   A OD1  1 
ATOM   3237 O  OD2  . ASP   A 1 145 ? 16.078 -19.434 -3.101  1.00 19.50 -1 145 ASP   A OD2  1 
ATOM   3238 H  H    . ASP   A 1 145 ? 17.585 -17.322 -0.345  1.00 16.47 ?  145 ASP   A H    1 
ATOM   3239 H  HA   . ASP   A 1 145 ? 18.305 -19.866 0.030   1.00 17.14 ?  145 ASP   A HA   1 
ATOM   3240 H  HB2  . ASP   A 1 145 ? 18.193 -18.321 -2.325  1.00 18.84 ?  145 ASP   A HB2  1 
ATOM   3241 H  HB3  . ASP   A 1 145 ? 18.653 -19.842 -2.321  1.00 18.84 ?  145 ASP   A HB3  1 
ATOM   3242 N  N    . THR   A 1 146 ? 20.581 -17.801 0.169   1.00 12.68 ?  146 THR   A N    1 
ATOM   3243 C  CA   . THR   A 1 146 ? 22.022 -17.552 0.190   1.00 12.22 ?  146 THR   A CA   1 
ATOM   3244 C  C    . THR   A 1 146 ? 22.575 -17.363 1.589   1.00 12.20 ?  146 THR   A C    1 
ATOM   3245 O  O    . THR   A 1 146 ? 23.653 -17.890 1.903   1.00 13.33 ?  146 THR   A O    1 
ATOM   3246 C  CB   . THR   A 1 146 ? 22.346 -16.302 -0.646  1.00 12.19 ?  146 THR   A CB   1 
ATOM   3247 O  OG1  . THR   A 1 146 ? 21.825 -16.465 -1.965  1.00 12.74 ?  146 THR   A OG1  1 
ATOM   3248 C  CG2  . THR   A 1 146 ? 23.844 -16.072 -0.735  1.00 12.87 ?  146 THR   A CG2  1 
ATOM   3249 H  H    . THR   A 1 146 ? 20.113 -17.173 0.532   1.00 15.22 ?  146 THR   A H    1 
ATOM   3250 H  HA   . THR   A 1 146 ? 22.480 -18.302 -0.210  1.00 14.67 ?  146 THR   A HA   1 
ATOM   3251 H  HB   . THR   A 1 146 ? 21.945 -15.521 -0.232  1.00 14.64 ?  146 THR   A HB   1 
ATOM   3252 H  HG1  . THR   A 1 146 ? 20.990 -16.538 -1.934  1.00 15.30 ?  146 THR   A HG1  1 
ATOM   3253 H  HG21 . THR   A 1 146 ? 24.034 -15.407 -1.415  1.00 15.45 ?  146 THR   A HG21 1 
ATOM   3254 H  HG22 . THR   A 1 146 ? 24.185 -15.760 0.116   1.00 15.45 ?  146 THR   A HG22 1 
ATOM   3255 H  HG23 . THR   A 1 146 ? 24.289 -16.901 -0.973  1.00 15.45 ?  146 THR   A HG23 1 
ATOM   3256 N  N    . VAL   A 1 147 ? 21.892 -16.586 2.421   1.00 12.13 ?  147 VAL   A N    1 
ATOM   3257 C  CA   . VAL   A 1 147 ? 22.381 -16.289 3.758   1.00 12.41 ?  147 VAL   A CA   1 
ATOM   3258 C  C    . VAL   A 1 147 ? 22.063 -17.459 4.675   1.00 12.90 ?  147 VAL   A C    1 
ATOM   3259 O  O    . VAL   A 1 147 ? 20.920 -17.934 4.726   1.00 13.37 ?  147 VAL   A O    1 
ATOM   3260 C  CB   . VAL   A 1 147 ? 21.764 -14.982 4.279   1.00 12.38 ?  147 VAL   A CB   1 
ATOM   3261 C  CG1  . VAL   A 1 147 ? 22.299 -14.670 5.659   1.00 13.30 ?  147 VAL   A CG1  1 
ATOM   3262 C  CG2  . VAL   A 1 147 ? 22.017 -13.834 3.303   1.00 12.30 ?  147 VAL   A CG2  1 
ATOM   3263 H  H    . VAL   A 1 147 ? 21.133 -16.220 2.237   1.00 14.56 ?  147 VAL   A H    1 
ATOM   3264 H  HA   . VAL   A 1 147 ? 23.343 -16.178 3.725   1.00 14.90 ?  147 VAL   A HA   1 
ATOM   3265 H  HB   . VAL   A 1 147 ? 20.807 -15.097 4.355   1.00 14.86 ?  147 VAL   A HB   1 
ATOM   3266 H  HG11 . VAL   A 1 147 ? 22.055 -13.763 5.894   1.00 15.96 ?  147 VAL   A HG11 1 
ATOM   3267 H  HG12 . VAL   A 1 147 ? 21.908 -15.292 6.295   1.00 15.96 ?  147 VAL   A HG12 1 
ATOM   3268 H  HG13 . VAL   A 1 147 ? 23.264 -14.764 5.653   1.00 15.96 ?  147 VAL   A HG13 1 
ATOM   3269 H  HG21 . VAL   A 1 147 ? 21.693 -13.009 3.698   1.00 14.77 ?  147 VAL   A HG21 1 
ATOM   3270 H  HG22 . VAL   A 1 147 ? 22.966 -13.770 3.128   1.00 14.77 ?  147 VAL   A HG22 1 
ATOM   3271 H  HG23 . VAL   A 1 147 ? 21.537 -14.014 2.478   1.00 14.77 ?  147 VAL   A HG23 1 
ATOM   3272 N  N    . ARG   A 1 148 ? 23.084 -17.923 5.395   1.00 13.02 ?  148 ARG   A N    1 
ATOM   3273 C  CA   . ARG   A 1 148 ? 22.954 -18.999 6.362   1.00 13.18 ?  148 ARG   A CA   1 
ATOM   3274 C  C    . ARG   A 1 148 ? 23.074 -18.526 7.797   1.00 13.45 ?  148 ARG   A C    1 
ATOM   3275 O  O    . ARG   A 1 148 ? 22.666 -19.252 8.710   1.00 15.01 ?  148 ARG   A O    1 
ATOM   3276 C  CB   . ARG   A 1 148 ? 24.003 -20.087 6.094   1.00 14.03 ?  148 ARG   A CB   1 
ATOM   3277 C  CG   . ARG   A 1 148 ? 23.844 -20.732 4.732   1.00 15.25 ?  148 ARG   A CG   1 
ATOM   3278 C  CD   . ARG   A 1 148 ? 24.930 -21.762 4.450   1.00 16.08 ?  148 ARG   A CD   1 
ATOM   3279 N  NE   . ARG   A 1 148 ? 26.267 -21.180 4.469   1.00 15.93 ?  148 ARG   A NE   1 
ATOM   3280 C  CZ   . ARG   A 1 148 ? 26.776 -20.446 3.488   1.00 15.36 ?  148 ARG   A CZ   1 
ATOM   3281 N  NH1  . ARG   A 1 148 ? 26.099 -20.214 2.374   1.00 15.81 ?  148 ARG   A NH1  1 
ATOM   3282 N  NH2  . ARG   A 1 148 ? 27.994 -19.923 3.631   1.00 15.57 ?  148 ARG   A NH2  1 
ATOM   3283 H  H    . ARG   A 1 148 ? 23.886 -17.613 5.328   1.00 15.62 ?  148 ARG   A H    1 
ATOM   3284 H  HA   . ARG   A 1 148 ? 22.081 -19.400 6.259   1.00 15.82 ?  148 ARG   A HA   1 
ATOM   3285 H  HB2  . ARG   A 1 148 ? 24.887 -19.698 6.138   1.00 16.84 ?  148 ARG   A HB2  1 
ATOM   3286 H  HB3  . ARG   A 1 148 ? 23.910 -20.785 6.761   1.00 16.84 ?  148 ARG   A HB3  1 
ATOM   3287 H  HG2  . ARG   A 1 148 ? 22.981 -21.173 4.692   1.00 18.31 ?  148 ARG   A HG2  1 
ATOM   3288 H  HG3  . ARG   A 1 148 ? 23.893 -20.038 4.052   1.00 18.31 ?  148 ARG   A HG3  1 
ATOM   3289 H  HD2  . ARG   A 1 148 ? 24.891 -22.450 5.129   1.00 19.30 ?  148 ARG   A HD2  1 
ATOM   3290 H  HD3  . ARG   A 1 148 ? 24.777 -22.144 3.573   1.00 19.30 ?  148 ARG   A HD3  1 
ATOM   3291 H  HE   . ARG   A 1 148 ? 26.752 -21.312 5.163   1.00 19.12 ?  148 ARG   A HE   1 
ATOM   3292 H  HH11 . ARG   A 1 148 ? 25.308 -20.532 2.271   1.00 18.97 ?  148 ARG   A HH11 1 
ATOM   3293 H  HH12 . ARG   A 1 148 ? 26.447 -19.727 1.752   1.00 18.97 ?  148 ARG   A HH12 1 
ATOM   3294 H  HH21 . ARG   A 1 148 ? 28.440 -20.060 4.351   1.00 18.69 ?  148 ARG   A HH21 1 
ATOM   3295 H  HH22 . ARG   A 1 148 ? 28.334 -19.440 3.001   1.00 18.69 ?  148 ARG   A HH22 1 
ATOM   3296 N  N    . THR   A 1 149 ? 23.623 -17.337 8.013   1.00 13.47 ?  149 THR   A N    1 
ATOM   3297 C  CA   . THR   A 1 149 ? 23.699 -16.735 9.329   1.00 13.68 ?  149 THR   A CA   1 
ATOM   3298 C  C    . THR   A 1 149 ? 22.374 -16.034 9.629   1.00 13.23 ?  149 THR   A C    1 
ATOM   3299 O  O    . THR   A 1 149 ? 21.442 -16.032 8.814   1.00 13.93 ?  149 THR   A O    1 
ATOM   3300 C  CB   . THR   A 1 149 ? 24.898 -15.797 9.387   1.00 14.02 ?  149 THR   A CB   1 
ATOM   3301 O  OG1  . THR   A 1 149 ? 24.770 -14.872 8.308   1.00 13.96 ?  149 THR   A OG1  1 
ATOM   3302 C  CG2  . THR   A 1 149 ? 26.209 -16.589 9.264   1.00 14.86 ?  149 THR   A CG2  1 
ATOM   3303 H  H    . THR   A 1 149 ? 23.973 -16.846 7.393   1.00 16.17 ?  149 THR   A H    1 
ATOM   3304 H  HA   . THR   A 1 149 ? 23.824 -17.434 9.987   1.00 16.42 ?  149 THR   A HA   1 
ATOM   3305 H  HB   . THR   A 1 149 ? 24.887 -15.321 10.232  1.00 16.83 ?  149 THR   A HB   1 
ATOM   3306 H  HG1  . THR   A 1 149 ? 25.414 -14.334 8.312   1.00 16.76 ?  149 THR   A HG1  1 
ATOM   3307 H  HG21 . THR   A 1 149 ? 26.966 -15.989 9.321   1.00 17.83 ?  149 THR   A HG21 1 
ATOM   3308 H  HG22 . THR   A 1 149 ? 26.271 -17.245 9.978   1.00 17.83 ?  149 THR   A HG22 1 
ATOM   3309 H  HG23 . THR   A 1 149 ? 26.239 -17.055 8.411   1.00 17.83 ?  149 THR   A HG23 1 
ATOM   3310 N  N    . ASN   A 1 150 ? 22.249 -15.489 10.832  1.00 13.51 ?  150 ASN   A N    1 
ATOM   3311 C  CA   . ASN   A 1 150 ? 20.965 -14.981 11.309  1.00 13.95 ?  150 ASN   A CA   1 
ATOM   3312 C  C    . ASN   A 1 150 ? 20.785 -13.544 10.844  1.00 12.86 ?  150 ASN   A C    1 
ATOM   3313 O  O    . ASN   A 1 150 ? 21.531 -12.648 11.258  1.00 14.47 ?  150 ASN   A O    1 
ATOM   3314 C  CB   . ASN   A 1 150 ? 20.894 -15.094 12.827  1.00 16.39 ?  150 ASN   A CB   1 
ATOM   3315 C  CG   . ASN   A 1 150 ? 20.791 -16.524 13.286  1.00 20.35 ?  150 ASN   A CG   1 
ATOM   3316 O  OD1  . ASN   A 1 150 ? 20.195 -17.357 12.605  1.00 21.56 ?  150 ASN   A OD1  1 
ATOM   3317 N  ND2  . ASN   A 1 150 ? 21.385 -16.827 14.437  1.00 22.40 ?  150 ASN   A ND2  1 
ATOM   3318 H  H    . ASN   A 1 150 ? 22.890 -15.414 11.400  1.00 16.22 ?  150 ASN   A H    1 
ATOM   3319 H  HA   . ASN   A 1 150 ? 20.245 -15.520 10.934  1.00 16.75 ?  150 ASN   A HA   1 
ATOM   3320 H  HB2  . ASN   A 1 150 ? 21.695 -14.712 13.213  1.00 19.68 ?  150 ASN   A HB2  1 
ATOM   3321 H  HB3  . ASN   A 1 150 ? 20.109 -14.625 13.147  1.00 19.68 ?  150 ASN   A HB3  1 
ATOM   3322 H  HD21 . ASN   A 1 150 ? 21.359 -17.634 14.744  1.00 26.89 ?  150 ASN   A HD21 1 
ATOM   3323 H  HD22 . ASN   A 1 150 ? 21.794 -16.217 14.886  1.00 26.89 ?  150 ASN   A HD22 1 
ATOM   3324 N  N    . VAL   A 1 151 ? 19.797 -13.317 9.986   1.00 12.64 ?  151 VAL   A N    1 
ATOM   3325 C  CA   . VAL   A 1 151 ? 19.586 -12.013 9.377   1.00 12.60 ?  151 VAL   A CA   1 
ATOM   3326 C  C    . VAL   A 1 151 ? 18.195 -11.500 9.733   1.00 12.49 ?  151 VAL   A C    1 
ATOM   3327 O  O    . VAL   A 1 151 ? 17.188 -12.212 9.585   1.00 13.85 ?  151 VAL   A O    1 
ATOM   3328 C  CB   . VAL   A 1 151 ? 19.887 -12.020 7.864   1.00 13.85 ?  151 VAL   A CB   1 
ATOM   3329 C  CG1  . VAL   A 1 151 ? 19.068 -13.054 7.116   1.00 14.60 ?  151 VAL   A CG1  1 
ATOM   3330 C  CG2  . VAL   A 1 151 ? 19.707 -10.619 7.271   1.00 14.11 ?  151 VAL   A CG2  1 
ATOM   3331 H  H    . VAL   A 1 151 ? 19.228 -13.914 9.738   1.00 15.17 ?  151 VAL   A H    1 
ATOM   3332 H  HA   . VAL   A 1 151 ? 20.223 -11.398 9.772   1.00 15.13 ?  151 VAL   A HA   1 
ATOM   3333 H  HB   . VAL   A 1 151 ? 20.822 -12.257 7.739   1.00 16.63 ?  151 VAL   A HB   1 
ATOM   3334 H  HG11 . VAL   A 1 151 ? 19.276 -13.009 6.167   1.00 17.52 ?  151 VAL   A HG11 1 
ATOM   3335 H  HG12 . VAL   A 1 151 ? 19.287 -13.941 7.454   1.00 17.52 ?  151 VAL   A HG12 1 
ATOM   3336 H  HG13 . VAL   A 1 151 ? 18.124 -12.877 7.253   1.00 17.52 ?  151 VAL   A HG13 1 
ATOM   3337 H  HG21 . VAL   A 1 151 ? 20.022 -10.621 6.349   1.00 16.93 ?  151 VAL   A HG21 1 
ATOM   3338 H  HG22 . VAL   A 1 151 ? 18.767 -10.382 7.293   1.00 16.93 ?  151 VAL   A HG22 1 
ATOM   3339 H  HG23 . VAL   A 1 151 ? 20.223 -9.985  7.791   1.00 16.93 ?  151 VAL   A HG23 1 
ATOM   3340 N  N    . TYR   A 1 152 ? 18.174 -10.255 10.216  1.00 12.62 ?  152 TYR   A N    1 
ATOM   3341 C  CA   . TYR   A 1 152 ? 16.977 -9.525  10.601  1.00 12.20 ?  152 TYR   A CA   1 
ATOM   3342 C  C    . TYR   A 1 152 ? 16.788 -8.425  9.570   1.00 11.75 ?  152 TYR   A C    1 
ATOM   3343 O  O    . TYR   A 1 152 ? 17.569 -7.466  9.521   1.00 12.28 ?  152 TYR   A O    1 
ATOM   3344 C  CB   . TYR   A 1 152 ? 17.155 -8.973  12.011  1.00 12.98 ?  152 TYR   A CB   1 
ATOM   3345 C  CG   . TYR   A 1 152 ? 17.111 -10.092 13.011  1.00 13.79 ?  152 TYR   A CG   1 
ATOM   3346 C  CD1  . TYR   A 1 152 ? 18.237 -10.861 13.286  1.00 15.33 ?  152 TYR   A CD1  1 
ATOM   3347 C  CD2  . TYR   A 1 152 ? 15.925 -10.429 13.643  1.00 14.18 ?  152 TYR   A CD2  1 
ATOM   3348 C  CE1  . TYR   A 1 152 ? 18.188 -11.915 14.177  1.00 16.89 ?  152 TYR   A CE1  1 
ATOM   3349 C  CE2  . TYR   A 1 152 ? 15.862 -11.492 14.537  1.00 15.69 ?  152 TYR   A CE2  1 
ATOM   3350 C  CZ   . TYR   A 1 152 ? 17.001 -12.226 14.802  1.00 16.74 ?  152 TYR   A CZ   1 
ATOM   3351 O  OH   . TYR   A 1 152 ? 16.948 -13.284 15.685  1.00 19.10 ?  152 TYR   A OH   1 
ATOM   3352 H  H    . TYR   A 1 152 ? 18.894 -9.783  10.317  1.00 15.15 ?  152 TYR   A H    1 
ATOM   3353 H  HA   . TYR   A 1 152 ? 16.212 -10.117 10.582  1.00 14.64 ?  152 TYR   A HA   1 
ATOM   3354 H  HB2  . TYR   A 1 152 ? 18.021 -8.540  12.080  1.00 15.58 ?  152 TYR   A HB2  1 
ATOM   3355 H  HB3  . TYR   A 1 152 ? 16.444 -8.354  12.210  1.00 15.58 ?  152 TYR   A HB3  1 
ATOM   3356 H  HD1  . TYR   A 1 152 ? 19.039 -10.659 12.861  1.00 18.40 ?  152 TYR   A HD1  1 
ATOM   3357 H  HD2  . TYR   A 1 152 ? 15.153 -9.936  13.460  1.00 17.03 ?  152 TYR   A HD2  1 
ATOM   3358 H  HE1  . TYR   A 1 152 ? 18.952 -12.412 14.353  1.00 20.27 ?  152 TYR   A HE1  1 
ATOM   3359 H  HE2  . TYR   A 1 152 ? 15.059 -11.695 14.958  1.00 18.83 ?  152 TYR   A HE2  1 
ATOM   3360 H  HH   . TYR   A 1 152 ? 16.170 -13.351 15.996  1.00 22.92 ?  152 TYR   A HH   1 
ATOM   3361 N  N    . LEU   A 1 153 ? 15.780 -8.591  8.723   1.00 11.84 ?  153 LEU   A N    1 
ATOM   3362 C  CA   . LEU   A 1 153 ? 15.525 -7.695  7.607   1.00 11.91 ?  153 LEU   A CA   1 
ATOM   3363 C  C    . LEU   A 1 153 ? 14.533 -6.618  8.012   1.00 12.23 ?  153 LEU   A C    1 
ATOM   3364 O  O    . LEU   A 1 153 ? 13.423 -6.922  8.467   1.00 13.21 ?  153 LEU   A O    1 
ATOM   3365 C  CB   . LEU   A 1 153 ? 14.961 -8.475  6.422   1.00 12.14 ?  153 LEU   A CB   1 
ATOM   3366 C  CG   . LEU   A 1 153 ? 15.905 -9.482  5.763   1.00 12.29 ?  153 LEU   A CG   1 
ATOM   3367 C  CD1  . LEU   A 1 153 ? 15.135 -10.372 4.807   1.00 12.77 ?  153 LEU   A CD1  1 
ATOM   3368 C  CD2  . LEU   A 1 153 ? 17.029 -8.767  5.025   1.00 12.63 ?  153 LEU   A CD2  1 
ATOM   3369 H  H    . LEU   A 1 153 ? 15.204 -9.235  8.784   1.00 14.21 ?  153 LEU   A H    1 
ATOM   3370 H  HA   . LEU   A 1 153 ? 16.351 -7.279  7.347   1.00 14.30 ?  153 LEU   A HA   1 
ATOM   3371 H  HB2  . LEU   A 1 153 ? 14.179 -8.963  6.727   1.00 14.57 ?  153 LEU   A HB2  1 
ATOM   3372 H  HB3  . LEU   A 1 153 ? 14.694 -7.835  5.744   1.00 14.57 ?  153 LEU   A HB3  1 
ATOM   3373 H  HG   . LEU   A 1 153 ? 16.305 -10.037 6.452   1.00 14.75 ?  153 LEU   A HG   1 
ATOM   3374 H  HD11 . LEU   A 1 153 ? 15.720 -11.080 4.502   1.00 15.33 ?  153 LEU   A HD11 1 
ATOM   3375 H  HD12 . LEU   A 1 153 ? 14.374 -10.744 5.273   1.00 15.33 ?  153 LEU   A HD12 1 
ATOM   3376 H  HD13 . LEU   A 1 153 ? 14.837 -9.836  4.056   1.00 15.33 ?  153 LEU   A HD13 1 
ATOM   3377 H  HD21 . LEU   A 1 153 ? 17.601 -9.430  4.618   1.00 15.16 ?  153 LEU   A HD21 1 
ATOM   3378 H  HD22 . LEU   A 1 153 ? 16.636 -8.198  4.345   1.00 15.16 ?  153 LEU   A HD22 1 
ATOM   3379 H  HD23 . LEU   A 1 153 ? 17.530 -8.232  5.658   1.00 15.16 ?  153 LEU   A HD23 1 
ATOM   3380 N  N    A ALA   A 1 154 ? 14.920 -5.367  7.803   0.68 12.54 ?  154 ALA   A N    1 
ATOM   3381 N  N    B ALA   A 1 154 ? 14.936 -5.360  7.862   0.32 12.10 ?  154 ALA   A N    1 
ATOM   3382 C  CA   A ALA   A 1 154 ? 14.041 -4.222  7.987   0.68 13.00 ?  154 ALA   A CA   1 
ATOM   3383 C  CA   B ALA   A 1 154 ? 14.091 -4.210  8.159   0.32 12.20 ?  154 ALA   A CA   1 
ATOM   3384 C  C    A ALA   A 1 154 ? 13.563 -3.753  6.621   0.68 12.70 ?  154 ALA   A C    1 
ATOM   3385 C  C    B ALA   A 1 154 ? 13.603 -3.641  6.831   0.32 11.89 ?  154 ALA   A C    1 
ATOM   3386 O  O    A ALA   A 1 154 ? 14.378 -3.410  5.758   0.68 13.48 ?  154 ALA   A O    1 
ATOM   3387 O  O    B ALA   A 1 154 ? 14.412 -3.205  6.007   0.32 11.84 ?  154 ALA   A O    1 
ATOM   3388 C  CB   A ALA   A 1 154 ? 14.782 -3.089  8.693   0.68 13.54 ?  154 ALA   A CB   1 
ATOM   3389 C  CB   B ALA   A 1 154 ? 14.883 -3.163  8.946   0.32 12.53 ?  154 ALA   A CB   1 
ATOM   3390 H  H    A ALA   A 1 154 ? 15.712 -5.149  7.542   0.68 15.05 ?  154 ALA   A H    1 
ATOM   3391 H  H    B ALA   A 1 154 ? 15.715 -5.137  7.572   0.32 14.53 ?  154 ALA   A H    1 
ATOM   3392 H  HA   A ALA   A 1 154 ? 13.272 -4.476  8.519   0.68 15.61 ?  154 ALA   A HA   1 
ATOM   3393 H  HA   B ALA   A 1 154 ? 13.326 -4.479  8.691   0.32 14.65 ?  154 ALA   A HA   1 
ATOM   3394 H  HB1  A ALA   A 1 154 ? 14.178 -2.338  8.801   0.68 16.25 ?  154 ALA   A HB1  1 
ATOM   3395 H  HB1  B ALA   A 1 154 ? 14.311 -2.403  9.142   0.32 15.04 ?  154 ALA   A HB1  1 
ATOM   3396 H  HB2  A ALA   A 1 154 ? 15.084 -3.401  9.558   0.68 16.25 ?  154 ALA   A HB2  1 
ATOM   3397 H  HB2  B ALA   A 1 154 ? 15.196 -3.558  9.780   0.32 15.04 ?  154 ALA   A HB2  1 
ATOM   3398 H  HB3  A ALA   A 1 154 ? 15.543 -2.825  8.151   0.68 16.25 ?  154 ALA   A HB3  1 
ATOM   3399 H  HB3  B ALA   A 1 154 ? 15.645 -2.874  8.418   0.32 15.04 ?  154 ALA   A HB3  1 
ATOM   3400 N  N    A VAL   A 1 155 ? 12.247 -3.747  6.430   0.38 11.12 ?  155 VAL   A N    1 
ATOM   3401 N  N    B VAL   A 1 155 ? 12.287 -3.661  6.620   0.32 11.44 ?  155 VAL   A N    1 
ATOM   3402 C  CA   A VAL   A 1 155 ? 11.604 -3.236  5.225   0.38 12.94 ?  155 VAL   A CA   1 
ATOM   3403 C  CA   B VAL   A 1 155 ? 11.671 -3.308  5.343   0.32 13.03 ?  155 VAL   A CA   1 
ATOM   3404 C  CA   T VAL   A 1 155 ? 11.603 -3.318  5.245   0.30 13.83 ?  155 VAL   A CA   1 
ATOM   3405 C  C    A VAL   A 1 155 ? 10.920 -1.928  5.598   0.38 14.00 ?  155 VAL   A C    1 
ATOM   3406 C  C    B VAL   A 1 155 ? 10.881 -2.020  5.539   0.32 14.31 ?  155 VAL   A C    1 
ATOM   3407 C  C    T VAL   A 1 155 ? 11.011 -1.946  5.570   0.30 13.53 ?  155 VAL   A C    1 
ATOM   3408 O  O    A VAL   A 1 155 ? 9.987  -1.920  6.410   0.38 14.36 ?  155 VAL   A O    1 
ATOM   3409 O  O    B VAL   A 1 155 ? 9.855  -2.009  6.229   0.32 14.46 ?  155 VAL   A O    1 
ATOM   3410 O  O    T VAL   A 1 155 ? 10.187 -1.812  6.472   0.30 13.30 ?  155 VAL   A O    1 
ATOM   3411 C  CB   A VAL   A 1 155 ? 10.592 -4.246  4.664   0.38 13.37 ?  155 VAL   A CB   1 
ATOM   3412 C  CB   B VAL   A 1 155 ? 10.769 -4.435  4.823   0.32 13.16 ?  155 VAL   A CB   1 
ATOM   3413 C  CB   T VAL   A 1 155 ? 10.547 -4.305  4.713   0.30 13.93 ?  155 VAL   A CB   1 
ATOM   3414 C  CG1  A VAL   A 1 155 ? 9.942  -3.701  3.401   0.38 14.10 ?  155 VAL   A CG1  1 
ATOM   3415 C  CG1  B VAL   A 1 155 ? 9.975  -3.977  3.603   0.32 13.45 ?  155 VAL   A CG1  1 
ATOM   3416 C  CG1  T VAL   A 1 155 ? 9.865  -3.740  3.477   0.30 14.45 ?  155 VAL   A CG1  1 
ATOM   3417 C  CG2  A VAL   A 1 155 ? 11.266 -5.584  4.393   0.38 13.95 ?  155 VAL   A CG2  1 
ATOM   3418 C  CG2  B VAL   A 1 155 ? 11.600 -5.668  4.500   0.32 13.90 ?  155 VAL   A CG2  1 
ATOM   3419 C  CG2  T VAL   A 1 155 ? 11.187 -5.656  4.405   0.30 14.18 ?  155 VAL   A CG2  1 
ATOM   3420 H  H    A VAL   A 1 155 ? 11.686 -4.062  7.003   0.38 13.35 ?  155 VAL   A H    1 
ATOM   3421 H  H    B VAL   A 1 155 ? 11.714 -3.885  7.223   0.32 13.73 ?  155 VAL   A H    1 
ATOM   3422 H  HA   A VAL   A 1 155 ? 12.273 -3.057  4.549   0.38 15.53 ?  155 VAL   A HA   1 
ATOM   3423 H  HA   B VAL   A 1 155 ? 12.366 -3.141  4.687   0.32 15.64 ?  155 VAL   A HA   1 
ATOM   3424 H  HB   A VAL   A 1 155 ? 9.891  -4.388  5.322   0.38 16.04 ?  155 VAL   A HB   1 
ATOM   3425 H  HB   B VAL   A 1 155 ? 10.137 -4.674  5.519   0.32 15.79 ?  155 VAL   A HB   1 
ATOM   3426 H  HB   T VAL   A 1 155 ? 9.871  -4.441  5.395   0.30 16.72 ?  155 VAL   A HB   1 
ATOM   3427 H  HG11 A VAL   A 1 155 ? 9.410  -4.403  2.995   0.38 16.93 ?  155 VAL   A HG11 1 
ATOM   3428 H  HG11 B VAL   A 1 155 ? 9.807  -4.738  3.024   0.32 16.15 ?  155 VAL   A HG11 1 
ATOM   3429 H  HG11 T VAL   A 1 155 ? 9.323  -4.435  3.073   0.30 17.35 ?  155 VAL   A HG11 1 
ATOM   3430 H  HG12 A VAL   A 1 155 ? 9.374  -2.949  3.633   0.38 16.93 ?  155 VAL   A HG12 1 
ATOM   3431 H  HG12 B VAL   A 1 155 ? 9.134  -3.595  3.898   0.32 16.15 ?  155 VAL   A HG12 1 
ATOM   3432 H  HG12 T VAL   A 1 155 ? 9.305  -2.992  3.737   0.30 17.35 ?  155 VAL   A HG12 1 
ATOM   3433 H  HG13 A VAL   A 1 155 ? 10.637 -3.416  2.788   0.38 16.93 ?  155 VAL   A HG13 1 
ATOM   3434 H  HG13 B VAL   A 1 155 ? 10.487 -3.307  3.128   0.32 16.15 ?  155 VAL   A HG13 1 
ATOM   3435 H  HG13 T VAL   A 1 155 ? 10.544 -3.445  2.850   0.30 17.35 ?  155 VAL   A HG13 1 
ATOM   3436 H  HG21 A VAL   A 1 155 ? 10.630 -6.177  3.965   0.38 16.75 ?  155 VAL   A HG21 1 
ATOM   3437 H  HG21 B VAL   A 1 155 ? 11.062 -6.281  3.978   0.32 16.69 ?  155 VAL   A HG21 1 
ATOM   3438 H  HG21 T VAL   A 1 155 ? 10.506 -6.261  4.074   0.30 17.03 ?  155 VAL   A HG21 1 
ATOM   3439 H  HG22 A VAL   A 1 155 ? 12.029 -5.439  3.810   0.38 16.75 ?  155 VAL   A HG22 1 
ATOM   3440 H  HG22 B VAL   A 1 155 ? 12.379 -5.395  3.991   0.32 16.69 ?  155 VAL   A HG22 1 
ATOM   3441 H  HG22 T VAL   A 1 155 ? 11.876 -5.532  3.730   0.30 17.03 ?  155 VAL   A HG22 1 
ATOM   3442 H  HG23 A VAL   A 1 155 ? 11.562 -5.965  5.234   0.38 16.75 ?  155 VAL   A HG23 1 
ATOM   3443 H  HG23 B VAL   A 1 155 ? 11.877 -6.087  5.329   0.32 16.69 ?  155 VAL   A HG23 1 
ATOM   3444 H  HG23 T VAL   A 1 155 ? 11.582 -6.012  5.216   0.30 17.03 ?  155 VAL   A HG23 1 
ATOM   3445 N  N    A PHE   A 1 156 ? 11.381 -0.820  5.010   0.38 14.96 ?  156 PHE   A N    1 
ATOM   3446 N  N    B PHE   A 1 156 ? 11.345 -0.936  4.913   0.32 15.74 ?  156 PHE   A N    1 
ATOM   3447 N  N    T PHE   A 1 156 ? 11.443 -0.929  4.822   0.30 13.68 ?  156 PHE   A N    1 
ATOM   3448 C  CA   A PHE   A 1 156 ? 10.861 0.490   5.403   0.38 16.06 ?  156 PHE   A CA   1 
ATOM   3449 C  CA   B PHE   A 1 156 ? 10.720 0.369   5.117   0.32 17.32 ?  156 PHE   A CA   1 
ATOM   3450 C  CA   T PHE   A 1 156 ? 11.042 0.445   5.121   0.30 13.79 ?  156 PHE   A CA   1 
ATOM   3451 C  C    A PHE   A 1 156 ? 9.392  0.652   5.026   0.38 15.72 ?  156 PHE   A C    1 
ATOM   3452 C  C    B PHE   A 1 156 ? 9.328  0.433   4.489   0.32 17.91 ?  156 PHE   A C    1 
ATOM   3453 C  C    T PHE   A 1 156 ? 9.577  0.686   4.780   0.30 13.98 ?  156 PHE   A C    1 
ATOM   3454 O  O    A PHE   A 1 156 ? 8.598  1.183   5.813   0.38 15.53 ?  156 PHE   A O    1 
ATOM   3455 O  O    B PHE   A 1 156 ? 8.374  0.910   5.115   0.32 17.96 ?  156 PHE   A O    1 
ATOM   3456 O  O    T PHE   A 1 156 ? 8.854  1.345   5.536   0.30 14.19 ?  156 PHE   A O    1 
ATOM   3457 C  CB   A PHE   A 1 156 ? 11.702 1.607   4.780   0.38 17.34 ?  156 PHE   A CB   1 
ATOM   3458 C  CB   B PHE   A 1 156 ? 11.622 1.465   4.540   0.32 18.41 ?  156 PHE   A CB   1 
ATOM   3459 C  CB   T PHE   A 1 156 ? 11.934 1.415   4.341   0.30 13.39 ?  156 PHE   A CB   1 
ATOM   3460 C  CG   A PHE   A 1 156 ? 11.179 2.990   5.073   0.38 18.27 ?  156 PHE   A CG   1 
ATOM   3461 C  CG   B PHE   A 1 156 ? 11.341 2.847   5.082   0.32 19.50 ?  156 PHE   A CG   1 
ATOM   3462 C  CG   T PHE   A 1 156 ? 11.571 2.866   4.527   0.30 12.99 ?  156 PHE   A CG   1 
ATOM   3463 C  CD1  A PHE   A 1 156 ? 11.138 3.459   6.376   0.38 18.48 ?  156 PHE   A CD1  1 
ATOM   3464 C  CD1  B PHE   A 1 156 ? 10.574 3.028   6.224   0.32 19.87 ?  156 PHE   A CD1  1 
ATOM   3465 C  CD1  T PHE   A 1 156 ? 11.934 3.538   5.686   0.30 13.79 ?  156 PHE   A CD1  1 
ATOM   3466 C  CD2  A PHE   A 1 156 ? 10.728 3.816   4.054   0.38 18.71 ?  156 PHE   A CD2  1 
ATOM   3467 C  CD2  B PHE   A 1 156 ? 11.850 3.967   4.445   0.32 19.90 ?  156 PHE   A CD2  1 
ATOM   3468 C  CD2  T PHE   A 1 156 ? 10.880 3.561   3.544   0.30 13.37 ?  156 PHE   A CD2  1 
ATOM   3469 C  CE1  A PHE   A 1 156 ? 10.659 4.723   6.660   0.38 18.89 ?  156 PHE   A CE1  1 
ATOM   3470 C  CE1  B PHE   A 1 156 ? 10.321 4.292   6.717   0.32 20.18 ?  156 PHE   A CE1  1 
ATOM   3471 C  CE1  T PHE   A 1 156 ? 11.607 4.868   5.869   0.30 14.25 ?  156 PHE   A CE1  1 
ATOM   3472 C  CE2  A PHE   A 1 156 ? 10.243 5.086   4.332   0.38 19.10 ?  156 PHE   A CE2  1 
ATOM   3473 C  CE2  B PHE   A 1 156 ? 11.598 5.238   4.935   0.32 20.01 ?  156 PHE   A CE2  1 
ATOM   3474 C  CE2  T PHE   A 1 156 ? 10.553 4.896   3.719   0.30 14.01 ?  156 PHE   A CE2  1 
ATOM   3475 C  CZ   A PHE   A 1 156 ? 10.212 5.539   5.636   0.38 19.30 ?  156 PHE   A CZ   1 
ATOM   3476 C  CZ   B PHE   A 1 156 ? 10.833 5.399   6.072   0.32 20.30 ?  156 PHE   A CZ   1 
ATOM   3477 C  CZ   T PHE   A 1 156 ? 10.917 5.552   4.885   0.30 14.15 ?  156 PHE   A CZ   1 
ATOM   3478 H  H    A PHE   A 1 156 ? 11.981 -0.802  4.392   0.38 17.95 ?  156 PHE   A H    1 
ATOM   3479 H  H    B PHE   A 1 156 ? 12.025 -0.923  4.387   0.32 18.90 ?  156 PHE   A H    1 
ATOM   3480 H  H    T PHE   A 1 156 ? 11.960 -1.009  4.140   0.30 16.43 ?  156 PHE   A H    1 
ATOM   3481 H  HA   A PHE   A 1 156 ? 10.933 0.579   6.365   0.38 19.28 ?  156 PHE   A HA   1 
ATOM   3482 H  HA   B PHE   A 1 156 ? 10.633 0.497   6.073   0.32 20.79 ?  156 PHE   A HA   1 
ATOM   3483 H  HA   T PHE   A 1 156 ? 11.167 0.615   6.067   0.30 16.55 ?  156 PHE   A HA   1 
ATOM   3484 H  HB2  A PHE   A 1 156 ? 12.610 1.554   5.128   0.38 20.82 ?  156 PHE   A HB2  1 
ATOM   3485 H  HB2  B PHE   A 1 156 ? 12.548 1.254   4.745   0.32 22.09 ?  156 PHE   A HB2  1 
ATOM   3486 H  HB2  T PHE   A 1 156 ? 12.851 1.300   4.637   0.30 16.07 ?  156 PHE   A HB2  1 
ATOM   3487 H  HB3  A PHE   A 1 156 ? 11.717 1.494   3.817   0.38 20.82 ?  156 PHE   A HB3  1 
ATOM   3488 H  HB3  B PHE   A 1 156 ? 11.501 1.498   3.577   0.32 22.09 ?  156 PHE   A HB3  1 
ATOM   3489 H  HB3  T PHE   A 1 156 ? 11.865 1.211   3.397   0.30 16.07 ?  156 PHE   A HB3  1 
ATOM   3490 H  HD1  A PHE   A 1 156 ? 11.440 2.914   7.069   0.38 22.18 ?  156 PHE   A HD1  1 
ATOM   3491 H  HD1  B PHE   A 1 156 ? 10.226 2.286   6.667   0.32 23.85 ?  156 PHE   A HD1  1 
ATOM   3492 H  HD1  T PHE   A 1 156 ? 12.394 3.080   6.356   0.30 16.55 ?  156 PHE   A HD1  1 
ATOM   3493 H  HD2  A PHE   A 1 156 ? 10.752 3.514   3.175   0.38 22.45 ?  156 PHE   A HD2  1 
ATOM   3494 H  HD2  B PHE   A 1 156 ? 12.366 3.867   3.677   0.32 23.88 ?  156 PHE   A HD2  1 
ATOM   3495 H  HD2  T PHE   A 1 156 ? 10.632 3.124   2.764   0.30 16.05 ?  156 PHE   A HD2  1 
ATOM   3496 H  HE1  A PHE   A 1 156 ? 10.638 5.025   7.541   0.38 22.67 ?  156 PHE   A HE1  1 
ATOM   3497 H  HE1  B PHE   A 1 156 ? 9.804  4.393   7.485   0.32 24.22 ?  156 PHE   A HE1  1 
ATOM   3498 H  HE1  T PHE   A 1 156 ? 11.850 5.301   6.657   0.30 17.10 ?  156 PHE   A HE1  1 
ATOM   3499 H  HE2  A PHE   A 1 156 ? 9.948  5.631   3.642   0.38 22.92 ?  156 PHE   A HE2  1 
ATOM   3500 H  HE2  B PHE   A 1 156 ? 11.943 5.983   4.498   0.32 24.02 ?  156 PHE   A HE2  1 
ATOM   3501 H  HE2  T PHE   A 1 156 ? 10.085 5.350   3.059   0.30 16.82 ?  156 PHE   A HE2  1 
ATOM   3502 H  HZ   A PHE   A 1 156 ? 9.890  6.390   5.828   0.38 23.17 ?  156 PHE   A HZ   1 
ATOM   3503 H  HZ   B PHE   A 1 156 ? 10.661 6.250   6.404   0.32 24.37 ?  156 PHE   A HZ   1 
ATOM   3504 H  HZ   T PHE   A 1 156 ? 10.693 6.444   5.008   0.30 16.98 ?  156 PHE   A HZ   1 
ATOM   3505 N  N    A ASP   A 1 157 ? 9.011  0.198   3.836   0.38 16.16 ?  157 ASP   A N    1 
ATOM   3506 N  N    B ASP   A 1 157 ? 9.197  -0.031  3.247   0.32 18.83 ?  157 ASP   A N    1 
ATOM   3507 N  N    T ASP   A 1 157 ? 9.127  0.156   3.650   0.30 14.31 ?  157 ASP   A N    1 
ATOM   3508 C  CA   A ASP   A 1 157 ? 7.689  0.462   3.279   0.38 17.40 ?  157 ASP   A CA   1 
ATOM   3509 C  CA   B ASP   A 1 157 ? 7.948  0.097   2.500   0.32 19.67 ?  157 ASP   A CA   1 
ATOM   3510 C  CA   T ASP   A 1 157 ? 7.820  0.467   3.091   0.30 14.92 ?  157 ASP   A CA   1 
ATOM   3511 C  C    A ASP   A 1 157 ? 6.698  -0.585  3.778   0.38 17.87 ?  157 ASP   A C    1 
ATOM   3512 C  C    B ASP   A 1 157 ? 6.882  -0.830  3.077   0.32 19.48 ?  157 ASP   A C    1 
ATOM   3513 C  C    T ASP   A 1 157 ? 6.790  -0.518  3.633   0.30 15.72 ?  157 ASP   A C    1 
ATOM   3514 O  O    A ASP   A 1 157 ? 6.864  -1.780  3.510   0.38 17.61 ?  157 ASP   A O    1 
ATOM   3515 O  O    B ASP   A 1 157 ? 7.048  -2.054  3.080   0.32 19.48 ?  157 ASP   A O    1 
ATOM   3516 O  O    T ASP   A 1 157 ? 6.909  -1.729  3.415   0.30 15.53 ?  157 ASP   A O    1 
ATOM   3517 C  CB   A ASP   A 1 157 ? 7.775  0.431   1.754   0.38 18.31 ?  157 ASP   A CB   1 
ATOM   3518 C  CB   B ASP   A 1 157 ? 8.206  -0.256  1.039   0.32 20.85 ?  157 ASP   A CB   1 
ATOM   3519 C  CB   T ASP   A 1 157 ? 7.915  0.349   1.574   0.30 15.02 ?  157 ASP   A CB   1 
ATOM   3520 C  CG   A ASP   A 1 157 ? 6.511  0.919   1.085   0.38 19.30 ?  157 ASP   A CG   1 
ATOM   3521 C  CG   B ASP   A 1 157 ? 7.056  0.137   0.126   0.32 21.78 ?  157 ASP   A CG   1 
ATOM   3522 C  CG   T ASP   A 1 157 ? 6.754  0.989   0.869   0.30 14.98 ?  157 ASP   A CG   1 
ATOM   3523 O  OD1  A ASP   A 1 157 ? 6.241  2.135   1.131   0.38 20.16 ?  157 ASP   A OD1  1 
ATOM   3524 O  OD1  B ASP   A 1 157 ? 5.888  0.049   0.560   0.32 21.97 ?  157 ASP   A OD1  1 
ATOM   3525 O  OD1  T ASP   A 1 157 ? 5.634  0.454   0.990   0.30 15.71 ?  157 ASP   A OD1  1 
ATOM   3526 O  OD2  A ASP   A 1 157 ? 5.787  0.081   0.507   0.38 19.26 -1 157 ASP   A OD2  1 
ATOM   3527 O  OD2  B ASP   A 1 157 ? 7.319  0.533   -1.029  0.32 22.35 -1 157 ASP   A OD2  1 
ATOM   3528 O  OD2  T ASP   A 1 157 ? 6.959  2.031   0.209   0.30 14.32 -1 157 ASP   A OD2  1 
ATOM   3529 H  H    A ASP   A 1 157 ? 9.514  -0.281  3.325   0.38 19.40 ?  157 ASP   A H    1 
ATOM   3530 H  H    B ASP   A 1 157 ? 9.828  -0.415  2.810   0.32 22.60 ?  157 ASP   A H    1 
ATOM   3531 H  H    T ASP   A 1 157 ? 9.574  -0.404  3.177   0.30 17.18 ?  157 ASP   A H    1 
ATOM   3532 H  HA   A ASP   A 1 157 ? 7.389  1.339   3.561   0.38 20.89 ?  157 ASP   A HA   1 
ATOM   3533 H  HA   B ASP   A 1 157 ? 7.628  1.013   2.550   0.32 23.61 ?  157 ASP   A HA   1 
ATOM   3534 H  HA   T ASP   A 1 157 ? 7.557  1.372   3.326   0.30 17.91 ?  157 ASP   A HA   1 
ATOM   3535 H  HB2  A ASP   A 1 157 ? 8.526  0.975   1.472   0.38 21.98 ?  157 ASP   A HB2  1 
ATOM   3536 H  HB2  B ASP   A 1 157 ? 9.013  0.194   0.747   0.32 25.02 ?  157 ASP   A HB2  1 
ATOM   3537 H  HB2  T ASP   A 1 157 ? 8.729  0.767   1.273   0.30 18.03 ?  157 ASP   A HB2  1 
ATOM   3538 H  HB3  A ASP   A 1 157 ? 7.903  -0.482  1.465   0.38 21.98 ?  157 ASP   A HB3  1 
ATOM   3539 H  HB3  B ASP   A 1 157 ? 8.326  -1.215  0.968   0.32 25.02 ?  157 ASP   A HB3  1 
ATOM   3540 H  HB3  T ASP   A 1 157 ? 7.928  -0.594  1.348   0.30 18.03 ?  157 ASP   A HB3  1 
ATOM   3541 N  N    A LYS   A 1 158 ? 5.660  -0.134  4.492   0.38 18.92 ?  158 LYS   A N    1 
ATOM   3542 N  N    B LYS   A 1 158 ? 5.768  -0.250  3.530   0.32 19.90 ?  158 LYS   A N    1 
ATOM   3543 N  N    T LYS   A 1 158 ? 5.772  0.000   4.328   0.30 17.07 ?  158 LYS   A N    1 
ATOM   3544 C  CA   A LYS   A 1 158 ? 4.680  -1.066  5.048   0.38 19.72 ?  158 LYS   A CA   1 
ATOM   3545 C  CA   B LYS   A 1 158 ? 4.739  -1.047  4.192   0.32 20.56 ?  158 LYS   A CA   1 
ATOM   3546 C  CA   T LYS   A 1 158 ? 4.783  -0.882  4.944   0.30 18.73 ?  158 LYS   A CA   1 
ATOM   3547 C  C    A LYS   A 1 158 ? 3.947  -1.813  3.943   0.38 18.91 ?  158 LYS   A C    1 
ATOM   3548 C  C    B LYS   A 1 158 ? 4.004  -1.950  3.207   0.32 19.70 ?  158 LYS   A C    1 
ATOM   3549 C  C    T LYS   A 1 158 ? 4.021  -1.679  3.894   0.30 18.75 ?  158 LYS   A C    1 
ATOM   3550 O  O    A LYS   A 1 158 ? 3.764  -3.034  4.017   0.38 18.93 ?  158 LYS   A O    1 
ATOM   3551 O  O    B LYS   A 1 158 ? 3.809  -3.143  3.469   0.32 19.52 ?  158 LYS   A O    1 
ATOM   3552 O  O    T LYS   A 1 158 ? 3.777  -2.878  4.071   0.30 18.84 ?  158 LYS   A O    1 
ATOM   3553 C  CB   A LYS   A 1 158 ? 3.685  -0.323  5.942   0.38 21.12 ?  158 LYS   A CB   1 
ATOM   3554 C  CB   B LYS   A 1 158 ? 3.758  -0.130  4.924   0.32 22.15 ?  158 LYS   A CB   1 
ATOM   3555 C  CB   T LYS   A 1 158 ? 3.814  -0.082  5.816   0.30 20.40 ?  158 LYS   A CB   1 
ATOM   3556 C  CG   A LYS   A 1 158 ? 2.451  -1.140  6.356   0.38 22.36 ?  158 LYS   A CG   1 
ATOM   3557 C  CG   B LYS   A 1 158 ? 2.507  -0.833  5.410   0.32 23.63 ?  158 LYS   A CG   1 
ATOM   3558 C  CG   T LYS   A 1 158 ? 2.583  -0.869  6.272   0.30 22.02 ?  158 LYS   A CG   1 
ATOM   3559 C  CD   A LYS   A 1 158 ? 2.803  -2.423  7.115   0.38 23.36 ?  158 LYS   A CD   1 
ATOM   3560 C  CD   B LYS   A 1 158 ? 2.842  -2.057  6.256   0.32 25.09 ?  158 LYS   A CD   1 
ATOM   3561 C  CD   T LYS   A 1 158 ? 2.951  -2.080  7.126   0.30 23.53 ?  158 LYS   A CD   1 
ATOM   3562 C  CE   A LYS   A 1 158 ? 1.555  -3.074  7.705   0.38 24.01 ?  158 LYS   A CE   1 
ATOM   3563 C  CE   B LYS   A 1 158 ? 2.262  -1.953  7.653   0.32 26.09 ?  158 LYS   A CE   1 
ATOM   3564 C  CE   T LYS   A 1 158 ? 1.712  -2.883  7.509   0.30 24.57 ?  158 LYS   A CE   1 
ATOM   3565 N  NZ   A LYS   A 1 158 ? 1.817  -4.424  8.284   0.38 24.20 ?  158 LYS   A NZ   1 
ATOM   3566 N  NZ   B LYS   A 1 158 ? 1.287  -3.040  7.919   0.32 26.67 ?  158 LYS   A NZ   1 
ATOM   3567 N  NZ   T LYS   A 1 158 ? 2.036  -4.100  8.308   0.30 25.08 ?  158 LYS   A NZ   1 
ATOM   3568 H  H    A LYS   A 1 158 ? 5.505  0.693   4.663   0.38 22.70 ?  158 LYS   A H    1 
ATOM   3569 H  H    B LYS   A 1 158 ? 5.591  0.590   3.469   0.32 23.89 ?  158 LYS   A H    1 
ATOM   3570 H  H    T LYS   A 1 158 ? 5.632  0.840   4.453   0.30 20.49 ?  158 LYS   A H    1 
ATOM   3571 H  HA   A LYS   A 1 158 ? 5.139  -1.720  5.595   0.38 23.67 ?  158 LYS   A HA   1 
ATOM   3572 H  HA   B LYS   A 1 158 ? 5.175  -1.613  4.848   0.32 24.68 ?  158 LYS   A HA   1 
ATOM   3573 H  HA   T LYS   A 1 158 ? 5.242  -1.513  5.519   0.30 22.48 ?  158 LYS   A HA   1 
ATOM   3574 H  HB2  A LYS   A 1 158 ? 4.136  -0.040  6.751   0.38 25.35 ?  158 LYS   A HB2  1 
ATOM   3575 H  HB2  B LYS   A 1 158 ? 4.203  0.250   5.698   0.32 26.58 ?  158 LYS   A HB2  1 
ATOM   3576 H  HB2  T LYS   A 1 158 ? 4.283  0.212   6.614   0.30 24.49 ?  158 LYS   A HB2  1 
ATOM   3577 H  HB3  A LYS   A 1 158 ? 3.365  0.457   5.463   0.38 25.35 ?  158 LYS   A HB3  1 
ATOM   3578 H  HB3  B LYS   A 1 158 ? 3.483  0.577   4.322   0.32 26.58 ?  158 LYS   A HB3  1 
ATOM   3579 H  HB3  T LYS   A 1 158 ? 3.503  0.687   5.317   0.30 24.49 ?  158 LYS   A HB3  1 
ATOM   3580 H  HG2  A LYS   A 1 158 ? 1.900  -0.595  6.939   0.38 26.83 ?  158 LYS   A HG2  1 
ATOM   3581 H  HG2  B LYS   A 1 158 ? 1.989  -0.212  5.942   0.32 28.36 ?  158 LYS   A HG2  1 
ATOM   3582 H  HG2  T LYS   A 1 158 ? 2.023  -0.290  6.810   0.30 26.43 ?  158 LYS   A HG2  1 
ATOM   3583 H  HG3  A LYS   A 1 158 ? 1.942  -1.385  5.566   0.38 26.83 ?  158 LYS   A HG3  1 
ATOM   3584 H  HG3  B LYS   A 1 158 ? 1.984  -1.127  4.650   0.32 28.36 ?  158 LYS   A HG3  1 
ATOM   3585 H  HG3  T LYS   A 1 158 ? 2.081  -1.180  5.500   0.30 26.43 ?  158 LYS   A HG3  1 
ATOM   3586 H  HD2  A LYS   A 1 158 ? 3.220  -3.053  6.510   0.38 28.03 ?  158 LYS   A HD2  1 
ATOM   3587 H  HD2  B LYS   A 1 158 ? 2.475  -2.850  5.830   0.32 30.11 ?  158 LYS   A HD2  1 
ATOM   3588 H  HD2  T LYS   A 1 158 ? 3.545  -2.661  6.627   0.30 28.25 ?  158 LYS   A HD2  1 
ATOM   3589 H  HD3  A LYS   A 1 158 ? 3.399  -2.210  7.847   0.38 28.03 ?  158 LYS   A HD3  1 
ATOM   3590 H  HD3  B LYS   A 1 158 ? 3.804  -2.147  6.348   0.32 30.11 ?  158 LYS   A HD3  1 
ATOM   3591 H  HD3  T LYS   A 1 158 ? 3.382  -1.779  7.942   0.30 28.25 ?  158 LYS   A HD3  1 
ATOM   3592 H  HE2  A LYS   A 1 158 ? 1.208  -2.507  8.413   0.38 28.81 ?  158 LYS   A HE2  1 
ATOM   3593 H  HE2  B LYS   A 1 158 ? 2.986  -2.029  8.292   0.32 31.32 ?  158 LYS   A HE2  1 
ATOM   3594 H  HE2  T LYS   A 1 158 ? 1.123  -2.324  8.041   0.30 29.49 ?  158 LYS   A HE2  1 
ATOM   3595 H  HE3  A LYS   A 1 158 ? 0.892  -3.171  7.007   0.38 28.81 ?  158 LYS   A HE3  1 
ATOM   3596 H  HE3  B LYS   A 1 158 ? 1.810  -1.103  7.765   0.32 31.32 ?  158 LYS   A HE3  1 
ATOM   3597 H  HE3  T LYS   A 1 158 ? 1.257  -3.168  6.701   0.30 29.49 ?  158 LYS   A HE3  1 
ATOM   3598 H  HZ1  A LYS   A 1 158 ? 1.064  -4.764  8.616   0.38 29.04 ?  158 LYS   A HZ1  1 
ATOM   3599 H  HZ1  B LYS   A 1 158 ? 1.130  -3.092  8.792   0.32 32.01 ?  158 LYS   A HZ1  1 
ATOM   3600 H  HZ1  T LYS   A 1 158 ? 1.289  -4.540  8.511   0.30 30.10 ?  158 LYS   A HZ1  1 
ATOM   3601 H  HZ2  A LYS   A 1 158 ? 2.127  -4.970  7.652   0.38 29.04 ?  158 LYS   A HZ2  1 
ATOM   3602 H  HZ2  B LYS   A 1 158 ? 0.523  -2.875  7.494   0.32 32.01 ?  158 LYS   A HZ2  1 
ATOM   3603 H  HZ2  T LYS   A 1 158 ? 2.569  -4.638  7.840   0.30 30.10 ?  158 LYS   A HZ2  1 
ATOM   3604 H  HZ3  A LYS   A 1 158 ? 2.420  -4.366  8.936   0.38 29.04 ?  158 LYS   A HZ3  1 
ATOM   3605 H  HZ3  B LYS   A 1 158 ? 1.615  -3.818  7.638   0.32 32.01 ?  158 LYS   A HZ3  1 
ATOM   3606 H  HZ3  T LYS   A 1 158 ? 2.449  -3.869  9.062   0.30 30.10 ?  158 LYS   A HZ3  1 
ATOM   3607 N  N    A ASN   A 1 159 ? 3.506  -1.094  2.912   0.38 18.53 ?  159 ASN   A N    1 
ATOM   3608 N  N    B ASN   A 1 159 ? 3.564  -1.396  2.075   0.32 19.16 ?  159 ASN   A N    1 
ATOM   3609 N  N    T ASN   A 1 159 ? 3.619  -1.034  2.806   0.30 19.00 ?  159 ASN   A N    1 
ATOM   3610 C  CA   A ASN   A 1 159 ? 2.840  -1.764  1.803   0.38 18.07 ?  159 ASN   A CA   1 
ATOM   3611 C  CA   B ASN   A 1 159 ? 2.845  -2.208  1.099   0.32 18.93 ?  159 ASN   A CA   1 
ATOM   3612 C  CA   T ASN   A 1 159 ? 2.886  -1.728  1.757   0.30 19.43 ?  159 ASN   A CA   1 
ATOM   3613 C  C    A ASN   A 1 159 ? 3.750  -2.812  1.183   0.38 16.56 ?  159 ASN   A C    1 
ATOM   3614 C  C    B ASN   A 1 159 ? 3.716  -3.354  0.590   0.32 17.36 ?  159 ASN   A C    1 
ATOM   3615 C  C    T ASN   A 1 159 ? 3.730  -2.823  1.117   0.30 19.34 ?  159 ASN   A C    1 
ATOM   3616 O  O    A ASN   A 1 159 ? 3.310  -3.928  0.889   0.38 16.21 ?  159 ASN   A O    1 
ATOM   3617 O  O    B ASN   A 1 159 ? 3.241  -4.484  0.419   0.32 17.29 ?  159 ASN   A O    1 
ATOM   3618 O  O    T ASN   A 1 159 ? 3.217  -3.885  0.781   0.30 19.27 ?  159 ASN   A O    1 
ATOM   3619 C  CB   A ASN   A 1 159 ? 2.363  -0.744  0.768   0.38 19.61 ?  159 ASN   A CB   1 
ATOM   3620 C  CB   B ASN   A 1 159 ? 2.349  -1.321  -0.046  0.32 20.27 ?  159 ASN   A CB   1 
ATOM   3621 C  CB   T ASN   A 1 159 ? 2.382  -0.744  0.697   0.30 20.40 ?  159 ASN   A CB   1 
ATOM   3622 C  CG   A ASN   A 1 159 ? 1.121  -0.004  1.216   0.38 21.39 ?  159 ASN   A CG   1 
ATOM   3623 C  CG   B ASN   A 1 159 ? 1.278  -0.339  0.400   0.32 21.70 ?  159 ASN   A CG   1 
ATOM   3624 C  CG   T ASN   A 1 159 ? 1.156  0.023   1.154   0.30 21.54 ?  159 ASN   A CG   1 
ATOM   3625 O  OD1  A ASN   A 1 159 ? 0.285  -0.558  1.923   0.38 22.27 ?  159 ASN   A OD1  1 
ATOM   3626 O  OD1  B ASN   A 1 159 ? 1.410  0.317   1.433   0.32 22.38 ?  159 ASN   A OD1  1 
ATOM   3627 O  OD1  T ASN   A 1 159 ? 0.351  -0.487  1.927   0.30 22.07 ?  159 ASN   A OD1  1 
ATOM   3628 N  ND2  A ASN   A 1 159 ? 0.996  1.253   0.812   0.38 21.67 ?  159 ASN   A ND2  1 
ATOM   3629 N  ND2  B ASN   A 1 159 ? 0.203  -0.245  -0.376  0.32 22.06 ?  159 ASN   A ND2  1 
ATOM   3630 N  ND2  T ASN   A 1 159 ? 1.012  1.253   0.678   0.30 21.73 ?  159 ASN   A ND2  1 
ATOM   3631 H  H    A ASN   A 1 159 ? 3.579  -0.245  2.831   0.38 22.24 ?  159 ASN   A H    1 
ATOM   3632 H  H    B ASN   A 1 159 ? 3.673  -0.570  1.854   0.32 23.00 ?  159 ASN   A H    1 
ATOM   3633 H  H    T ASN   A 1 159 ? 3.749  -0.200  2.658   0.30 22.81 ?  159 ASN   A H    1 
ATOM   3634 H  HA   A ASN   A 1 159 ? 2.058  -2.230  2.141   0.38 21.69 ?  159 ASN   A HA   1 
ATOM   3635 H  HA   B ASN   A 1 159 ? 2.066  -2.589  1.526   0.32 22.73 ?  159 ASN   A HA   1 
ATOM   3636 H  HA   T ASN   A 1 159 ? 2.114  -2.161  2.150   0.30 23.32 ?  159 ASN   A HA   1 
ATOM   3637 H  HB2  A ASN   A 1 159 ? 3.059  -0.091  0.621   0.38 23.54 ?  159 ASN   A HB2  1 
ATOM   3638 H  HB2  B ASN   A 1 159 ? 3.093  -0.803  -0.397  0.32 24.33 ?  159 ASN   A HB2  1 
ATOM   3639 H  HB2  T ASN   A 1 159 ? 3.079  -0.103  0.502   0.30 24.48 ?  159 ASN   A HB2  1 
ATOM   3640 H  HB3  A ASN   A 1 159 ? 2.154  -1.206  -0.060  0.38 23.54 ?  159 ASN   A HB3  1 
ATOM   3641 H  HB3  B ASN   A 1 159 ? 1.968  -1.870  -0.743  0.32 24.33 ?  159 ASN   A HB3  1 
ATOM   3642 H  HB3  T ASN   A 1 159 ? 2.147  -1.239  -0.106  0.30 24.48 ?  159 ASN   A HB3  1 
ATOM   3643 H  HD21 A ASN   A 1 159 ? 0.305  1.711   1.040   0.38 26.01 ?  159 ASN   A HD21 1 
ATOM   3644 H  HD21 B ASN   A 1 159 ? -0.436 0.294   -0.167  0.32 26.48 ?  159 ASN   A HD21 1 
ATOM   3645 H  HD21 T ASN   A 1 159 ? 0.329  1.724   0.907   0.30 26.09 ?  159 ASN   A HD21 1 
ATOM   3646 H  HD22 A ASN   A 1 159 ? 1.605  1.605   0.322   0.38 26.01 ?  159 ASN   A HD22 1 
ATOM   3647 H  HD22 B ASN   A 1 159 ? 0.144  -0.723  -1.087  0.32 26.48 ?  159 ASN   A HD22 1 
ATOM   3648 H  HD22 T ASN   A 1 159 ? 1.598  1.574   0.142   0.30 26.09 ?  159 ASN   A HD22 1 
ATOM   3649 N  N    A LEU   A 1 160 ? 5.033  -2.495  1.011   0.38 15.07 ?  160 LEU   A N    1 
ATOM   3650 N  N    B LEU   A 1 160 ? 5.004  -3.087  0.370   0.32 15.80 ?  160 LEU   A N    1 
ATOM   3651 N  N    T LEU   A 1 160 ? 5.026  -2.575  0.966   0.30 19.21 ?  160 LEU   A N    1 
ATOM   3652 C  CA   A LEU   A 1 160 ? 5.944  -3.510  0.497   0.38 13.94 ?  160 LEU   A CA   1 
ATOM   3653 C  CA   B LEU   A 1 160 ? 5.907  -4.136  -0.091  0.32 15.01 ?  160 LEU   A CA   1 
ATOM   3654 C  CA   T LEU   A 1 160 ? 5.902  -3.549  0.323   0.30 19.31 ?  160 LEU   A CA   1 
ATOM   3655 C  C    A LEU   A 1 160 ? 6.124  -4.646  1.496   0.38 12.69 ?  160 LEU   A C    1 
ATOM   3656 C  C    B LEU   A 1 160 ? 6.099  -5.212  0.974   0.32 13.86 ?  160 LEU   A C    1 
ATOM   3657 O  O    A LEU   A 1 160 ? 6.135  -5.820  1.110   0.38 11.97 ?  160 LEU   A O    1 
ATOM   3658 O  O    B LEU   A 1 160 ? 6.141  -6.405  0.655   0.32 13.85 ?  160 LEU   A O    1 
ATOM   3659 C  CB   A LEU   A 1 160 ? 7.286  -2.893  0.115   0.38 14.20 ?  160 LEU   A CB   1 
ATOM   3660 C  CB   B LEU   A 1 160 ? 7.251  -3.528  -0.492  0.32 15.83 ?  160 LEU   A CB   1 
ATOM   3661 C  CB   T LEU   A 1 160 ? 7.340  -3.041  0.304   0.30 19.50 ?  160 LEU   A CB   1 
ATOM   3662 C  CG   A LEU   A 1 160 ? 8.309  -3.939  -0.332  0.38 14.71 ?  160 LEU   A CG   1 
ATOM   3663 C  CG   B LEU   A 1 160 ? 7.293  -2.739  -1.806  0.32 17.73 ?  160 LEU   A CG   1 
ATOM   3664 C  CG   T LEU   A 1 160 ? 8.224  -3.534  -0.843  0.30 19.92 ?  160 LEU   A CG   1 
ATOM   3665 C  CD1  A LEU   A 1 160 ? 7.816  -4.708  -1.545  0.38 15.44 ?  160 LEU   A CD1  1 
ATOM   3666 C  CD1  B LEU   A 1 160 ? 8.679  -2.156  -2.075  0.32 18.39 ?  160 LEU   A CD1  1 
ATOM   3667 C  CD1  T LEU   A 1 160 ? 9.683  -3.428  -0.457  0.30 19.82 ?  160 LEU   A CD1  1 
ATOM   3668 C  CD2  A LEU   A 1 160 ? 9.624  -3.267  -0.636  0.38 15.03 ?  160 LEU   A CD2  1 
ATOM   3669 C  CD2  B LEU   A 1 160 ? 6.845  -3.617  -2.964  0.32 18.37 ?  160 LEU   A CD2  1 
ATOM   3670 C  CD2  T LEU   A 1 160 ? 7.875  -4.953  -1.245  0.30 19.98 ?  160 LEU   A CD2  1 
ATOM   3671 H  H    A LEU   A 1 160 ? 5.388  -1.727  1.184   0.38 18.09 ?  160 LEU   A H    1 
ATOM   3672 H  H    B LEU   A 1 160 ? 5.368  -2.318  0.484   0.32 18.97 ?  160 LEU   A H    1 
ATOM   3673 H  H    T LEU   A 1 160 ? 5.423  -1.856  1.231   0.30 23.06 ?  160 LEU   A H    1 
ATOM   3674 H  HA   A LEU   A 1 160 ? 5.562  -3.879  -0.311  0.38 16.74 ?  160 LEU   A HA   1 
ATOM   3675 H  HA   B LEU   A 1 160 ? 5.518  -4.559  -0.871  0.32 18.02 ?  160 LEU   A HA   1 
ATOM   3676 H  HB2  A LEU   A 1 160 ? 7.162  -2.251  -0.614  0.38 17.05 ?  160 LEU   A HB2  1 
ATOM   3677 H  HB2  B LEU   A 1 160 ? 7.527  -2.930  0.216   0.32 19.01 ?  160 LEU   A HB2  1 
ATOM   3678 H  HB2  T LEU   A 1 160 ? 7.306  -2.079  0.219   0.30 23.41 ?  160 LEU   A HB2  1 
ATOM   3679 H  HB3  A LEU   A 1 160 ? 7.656  -2.439  0.888   0.38 17.05 ?  160 LEU   A HB3  1 
ATOM   3680 H  HB3  B LEU   A 1 160 ? 7.893  -4.247  -0.570  0.32 19.01 ?  160 LEU   A HB3  1 
ATOM   3681 H  HB3  T LEU   A 1 160 ? 7.768  -3.283  1.145   0.30 23.41 ?  160 LEU   A HB3  1 
ATOM   3682 H  HG   A LEU   A 1 160 ? 8.463  -4.565  0.387   0.38 17.66 ?  160 LEU   A HG   1 
ATOM   3683 H  HG   B LEU   A 1 160 ? 6.680  -1.996  -1.739  0.32 21.29 ?  160 LEU   A HG   1 
ATOM   3684 H  HG   T LEU   A 1 160 ? 8.081  -2.959  -1.613  0.30 23.92 ?  160 LEU   A HG   1 
ATOM   3685 H  HD11 A LEU   A 1 160 ? 8.543  -5.242  -1.894  0.38 18.54 ?  160 LEU   A HD11 1 
ATOM   3686 H  HD11 B LEU   A 1 160 ? 8.829  -2.117  -3.035  0.32 22.07 ?  160 LEU   A HD11 1 
ATOM   3687 H  HD11 T LEU   A 1 160 ? 10.228 -3.698  -1.212  0.30 23.79 ?  160 LEU   A HD11 1 
ATOM   3688 H  HD12 A LEU   A 1 160 ? 7.081  -5.282  -1.276  0.38 18.54 ?  160 LEU   A HD12 1 
ATOM   3689 H  HD12 B LEU   A 1 160 ? 8.726  -1.263  -1.700  0.32 22.07 ?  160 LEU   A HD12 1 
ATOM   3690 H  HD12 T LEU   A 1 160 ? 9.880  -2.509  -0.217  0.30 23.79 ?  160 LEU   A HD12 1 
ATOM   3691 H  HD13 A LEU   A 1 160 ? 7.514  -4.077  -2.218  0.38 18.54 ?  160 LEU   A HD13 1 
ATOM   3692 H  HD13 B LEU   A 1 160 ? 9.348  -2.723  -1.662  0.32 22.07 ?  160 LEU   A HD13 1 
ATOM   3693 H  HD13 T LEU   A 1 160 ? 9.850  -4.012  0.299   0.30 23.79 ?  160 LEU   A HD13 1 
ATOM   3694 H  HD21 A LEU   A 1 160 ? 10.266 -3.942  -0.911  0.38 18.04 ?  160 LEU   A HD21 1 
ATOM   3695 H  HD21 B LEU   A 1 160 ? 7.005  -3.147  -3.794  0.32 22.05 ?  160 LEU   A HD21 1 
ATOM   3696 H  HD21 T LEU   A 1 160 ? 8.576  -5.296  -1.820  0.30 23.98 ?  160 LEU   A HD21 1 
ATOM   3697 H  HD22 A LEU   A 1 160 ? 9.497  -2.623  -1.350  0.38 18.04 ?  160 LEU   A HD22 1 
ATOM   3698 H  HD22 B LEU   A 1 160 ? 7.352  -4.445  -2.946  0.32 22.05 ?  160 LEU   A HD22 1 
ATOM   3699 H  HD22 T LEU   A 1 160 ? 7.803  -5.496  -0.446  0.30 23.98 ?  160 LEU   A HD22 1 
ATOM   3700 H  HD23 A LEU   A 1 160 ? 9.944  -2.815  0.162   0.38 18.04 ?  160 LEU   A HD23 1 
ATOM   3701 H  HD23 B LEU   A 1 160 ? 5.899  -3.805  -2.870  0.32 22.05 ?  160 LEU   A HD23 1 
ATOM   3702 H  HD23 T LEU   A 1 160 ? 7.029  -4.946  -1.720  0.30 23.98 ?  160 LEU   A HD23 1 
ATOM   3703 N  N    A TYR   A 1 161 ? 6.277  -4.322  2.782   0.68 13.93 ?  161 TYR   A N    1 
ATOM   3704 N  N    B TYR   A 1 161 ? 6.221  -4.808  2.241   0.32 13.31 ?  161 TYR   A N    1 
ATOM   3705 C  CA   A TYR   A 1 161 ? 6.392  -5.371  3.790   0.68 14.60 ?  161 TYR   A CA   1 
ATOM   3706 C  CA   B TYR   A 1 161 ? 6.350  -5.777  3.328   0.32 13.73 ?  161 TYR   A CA   1 
ATOM   3707 C  C    A TYR   A 1 161 ? 5.228  -6.346  3.700   0.68 16.02 ?  161 TYR   A C    1 
ATOM   3708 C  C    B TYR   A 1 161 ? 5.174  -6.744  3.337   0.32 14.24 ?  161 TYR   A C    1 
ATOM   3709 O  O    A TYR   A 1 161 ? 5.423  -7.566  3.682   0.68 15.87 ?  161 TYR   A O    1 
ATOM   3710 O  O    B TYR   A 1 161 ? 5.357  -7.958  3.487   0.32 14.22 ?  161 TYR   A O    1 
ATOM   3711 C  CB   A TYR   A 1 161 ? 6.465  -4.781  5.197   0.68 14.72 ?  161 TYR   A CB   1 
ATOM   3712 C  CB   B TYR   A 1 161 ? 6.463  -5.030  4.660   0.32 14.09 ?  161 TYR   A CB   1 
ATOM   3713 C  CG   A TYR   A 1 161 ? 6.371  -5.863  6.245   0.68 14.76 ?  161 TYR   A CG   1 
ATOM   3714 C  CG   B TYR   A 1 161 ? 6.357  -5.889  5.903   0.32 14.85 ?  161 TYR   A CG   1 
ATOM   3715 C  CD1  A TYR   A 1 161 ? 7.482  -6.624  6.573   0.68 14.69 ?  161 TYR   A CD1  1 
ATOM   3716 C  CD1  B TYR   A 1 161 ? 7.486  -6.462  6.474   0.32 15.15 ?  161 TYR   A CD1  1 
ATOM   3717 C  CD2  A TYR   A 1 161 ? 5.170  -6.140  6.888   0.68 14.82 ?  161 TYR   A CD2  1 
ATOM   3718 C  CD2  B TYR   A 1 161 ? 5.131  -6.101  6.521   0.32 15.44 ?  161 TYR   A CD2  1 
ATOM   3719 C  CE1  A TYR   A 1 161 ? 7.406  -7.624  7.511   0.68 14.20 ?  161 TYR   A CE1  1 
ATOM   3720 C  CE1  B TYR   A 1 161 ? 7.394  -7.244  7.615   0.32 15.40 ?  161 TYR   A CE1  1 
ATOM   3721 C  CE2  A TYR   A 1 161 ? 5.085  -7.144  7.832   0.68 14.77 ?  161 TYR   A CE2  1 
ATOM   3722 C  CE2  B TYR   A 1 161 ? 5.029  -6.880  7.662   0.32 15.68 ?  161 TYR   A CE2  1 
ATOM   3723 C  CZ   A TYR   A 1 161 ? 6.208  -7.879  8.136   0.68 14.20 ?  161 TYR   A CZ   1 
ATOM   3724 C  CZ   B TYR   A 1 161 ? 6.162  -7.448  8.205   0.32 15.82 ?  161 TYR   A CZ   1 
ATOM   3725 O  OH   A TYR   A 1 161 ? 6.145  -8.873  9.076   0.68 14.27 ?  161 TYR   A OH   1 
ATOM   3726 O  OH   B TYR   A 1 161 ? 6.063  -8.225  9.339   0.32 16.79 ?  161 TYR   A OH   1 
ATOM   3727 H  H    A TYR   A 1 161 ? 6.318  -3.514  3.086   0.68 16.72 ?  161 TYR   A H    1 
ATOM   3728 H  H    B TYR   A 1 161 ? 6.228  -3.990  2.494   0.32 15.98 ?  161 TYR   A H    1 
ATOM   3729 H  HA   A TYR   A 1 161 ? 7.204  -5.865  3.633   0.68 17.53 ?  161 TYR   A HA   1 
ATOM   3730 H  HA   B TYR   A 1 161 ? 7.158  -6.295  3.202   0.32 16.48 ?  161 TYR   A HA   1 
ATOM   3731 H  HB2  A TYR   A 1 161 ? 7.313  -4.318  5.309   0.68 17.67 ?  161 TYR   A HB2  1 
ATOM   3732 H  HB2  B TYR   A 1 161 ? 7.325  -4.585  4.687   0.32 16.92 ?  161 TYR   A HB2  1 
ATOM   3733 H  HB3  A TYR   A 1 161 ? 5.728  -4.160  5.329   0.68 17.67 ?  161 TYR   A HB3  1 
ATOM   3734 H  HB3  B TYR   A 1 161 ? 5.757  -4.367  4.700   0.32 16.92 ?  161 TYR   A HB3  1 
ATOM   3735 H  HD1  A TYR   A 1 161 ? 8.292  -6.457  6.149   0.68 17.64 ?  161 TYR   A HD1  1 
ATOM   3736 H  HD1  B TYR   A 1 161 ? 8.317  -6.326  6.077   0.32 18.19 ?  161 TYR   A HD1  1 
ATOM   3737 H  HD2  A TYR   A 1 161 ? 4.408  -5.645  6.680   0.68 17.79 ?  161 TYR   A HD2  1 
ATOM   3738 H  HD2  B TYR   A 1 161 ? 4.363  -5.721  6.158   0.32 18.54 ?  161 TYR   A HD2  1 
ATOM   3739 H  HE1  A TYR   A 1 161 ? 8.159  -8.130  7.720   0.68 17.04 ?  161 TYR   A HE1  1 
ATOM   3740 H  HE1  B TYR   A 1 161 ? 8.160  -7.622  7.986   0.32 18.48 ?  161 TYR   A HE1  1 
ATOM   3741 H  HE2  A TYR   A 1 161 ? 4.272  -7.323  8.257   0.68 17.73 ?  161 TYR   A HE2  1 
ATOM   3742 H  HE2  B TYR   A 1 161 ? 4.200  -7.014  8.063   0.32 18.82 ?  161 TYR   A HE2  1 
ATOM   3743 H  HH   A TYR   A 1 161 ? 6.890  -9.247  9.162   0.68 17.13 ?  161 TYR   A HH   1 
ATOM   3744 H  HH   B TYR   A 1 161 ? 6.819  -8.503  9.566   0.32 20.15 ?  161 TYR   A HH   1 
ATOM   3745 N  N    A ASP   A 1 162 ? 4.000  -5.826  3.655   0.68 16.68 ?  162 ASP   A N    1 
ATOM   3746 N  N    B ASP   A 1 162 ? 3.957  -6.221  3.163   0.32 14.72 ?  162 ASP   A N    1 
ATOM   3747 C  CA   A ASP   A 1 162 ? 2.847  -6.720  3.586   0.68 17.72 ?  162 ASP   A CA   1 
ATOM   3748 C  CA   B ASP   A 1 162 ? 2.772  -7.070  3.107   0.32 15.92 ?  162 ASP   A CA   1 
ATOM   3749 C  C    A ASP   A 1 162 ? 2.878  -7.564  2.322   0.68 17.66 ?  162 ASP   A C    1 
ATOM   3750 C  C    B ASP   A 1 162 ? 2.866  -8.064  1.954   0.32 15.74 ?  162 ASP   A C    1 
ATOM   3751 O  O    A ASP   A 1 162 ? 2.540  -8.754  2.355   0.68 17.86 ?  162 ASP   A O    1 
ATOM   3752 O  O    B ASP   A 1 162 ? 2.504  -9.238  2.103   0.32 15.94 ?  162 ASP   A O    1 
ATOM   3753 C  CB   A ASP   A 1 162 ? 1.540  -5.937  3.667   0.68 18.83 ?  162 ASP   A CB   1 
ATOM   3754 C  CB   B ASP   A 1 162 ? 1.522  -6.193  2.964   0.32 17.68 ?  162 ASP   A CB   1 
ATOM   3755 C  CG   A ASP   A 1 162 ? 1.236  -5.465  5.056   0.68 19.98 ?  162 ASP   A CG   1 
ATOM   3756 C  CG   B ASP   A 1 162 ? 1.335  -5.236  4.133   0.32 19.23 ?  162 ASP   A CG   1 
ATOM   3757 O  OD1  A ASP   A 1 162 ? 1.882  -5.939  6.013   0.68 20.47 ?  162 ASP   A OD1  1 
ATOM   3758 O  OD1  B ASP   A 1 162 ? 1.864  -5.521  5.227   0.32 19.52 ?  162 ASP   A OD1  1 
ATOM   3759 O  OD2  A ASP   A 1 162 ? 0.340  -4.611  5.182   0.68 21.19 -1 162 ASP   A OD2  1 
ATOM   3760 O  OD2  B ASP   A 1 162 ? 0.632  -4.215  3.965   0.32 20.24 -1 162 ASP   A OD2  1 
ATOM   3761 H  H    A ASP   A 1 162 ? 3.806  -4.976  3.664   0.68 20.02 ?  162 ASP   A H    1 
ATOM   3762 H  H    B ASP   A 1 162 ? 3.797  -5.385  3.068   0.32 17.67 ?  162 ASP   A H    1 
ATOM   3763 H  HA   A ASP   A 1 162 ? 2.877  -7.319  4.339   0.68 21.26 ?  162 ASP   A HA   1 
ATOM   3764 H  HA   B ASP   A 1 162 ? 2.687  -7.567  3.934   0.32 19.12 ?  162 ASP   A HA   1 
ATOM   3765 H  HB2  A ASP   A 1 162 ? 1.590  -5.150  3.107   0.68 22.60 ?  162 ASP   A HB2  1 
ATOM   3766 H  HB2  B ASP   A 1 162 ? 1.579  -5.683  2.135   0.32 21.22 ?  162 ASP   A HB2  1 
ATOM   3767 H  HB3  A ASP   A 1 162 ? 0.806  -6.506  3.382   0.68 22.60 ?  162 ASP   A HB3  1 
ATOM   3768 H  HB3  B ASP   A 1 162 ? 0.731  -6.746  2.957   0.32 21.22 ?  162 ASP   A HB3  1 
ATOM   3769 N  N    A LYS   A 1 163 ? 3.264  -6.967  1.191   0.68 17.86 ?  163 LYS   A N    1 
ATOM   3770 N  N    B LYS   A 1 163 ? 3.356  -7.611  0.797   0.32 15.58 ?  163 LYS   A N    1 
ATOM   3771 C  CA   A LYS   A 1 163 ? 3.354  -7.747  -0.037  0.68 18.44 ?  163 LYS   A CA   1 
ATOM   3772 C  CA   B LYS   A 1 163 ? 3.469  -8.491  -0.362  0.32 15.89 ?  163 LYS   A CA   1 
ATOM   3773 C  C    A LYS   A 1 163 ? 4.433  -8.812  0.075   0.68 17.66 ?  163 LYS   A C    1 
ATOM   3774 C  C    B LYS   A 1 163 ? 4.582  -9.519  -0.175  0.32 14.81 ?  163 LYS   A C    1 
ATOM   3775 O  O    A LYS   A 1 163 ? 4.265  -9.930  -0.423  0.68 17.71 ?  163 LYS   A O    1 
ATOM   3776 O  O    B LYS   A 1 163 ? 4.446  -10.674 -0.598  0.32 15.17 ?  163 LYS   A O    1 
ATOM   3777 C  CB   A LYS   A 1 163 ? 3.620  -6.841  -1.239  0.68 20.79 ?  163 LYS   A CB   1 
ATOM   3778 C  CB   B LYS   A 1 163 ? 3.707  -7.656  -1.622  0.32 18.09 ?  163 LYS   A CB   1 
ATOM   3779 C  CG   A LYS   A 1 163 ? 3.729  -7.604  -2.554  0.68 23.76 ?  163 LYS   A CG   1 
ATOM   3780 C  CG   B LYS   A 1 163 ? 3.483  -8.411  -2.925  0.32 20.55 ?  163 LYS   A CG   1 
ATOM   3781 C  CD   A LYS   A 1 163 ? 4.113  -6.699  -3.706  0.68 26.58 ?  163 LYS   A CD   1 
ATOM   3782 C  CD   B LYS   A 1 163 ? 3.293  -7.463  -4.107  0.32 22.76 ?  163 LYS   A CD   1 
ATOM   3783 C  CE   A LYS   A 1 163 ? 4.091  -7.454  -5.027  0.68 28.77 ?  163 LYS   A CE   1 
ATOM   3784 C  CE   B LYS   A 1 163 ? 4.570  -6.713  -4.452  0.32 24.48 ?  163 LYS   A CE   1 
ATOM   3785 N  NZ   A LYS   A 1 163 ? 4.694  -6.665  -6.136  0.68 30.11 ?  163 LYS   A NZ   1 
ATOM   3786 N  NZ   B LYS   A 1 163 ? 4.562  -6.214  -5.859  0.32 25.43 ?  163 LYS   A NZ   1 
ATOM   3787 H  H    A LYS   A 1 163 ? 3.468  -6.128  1.110   0.68 21.43 ?  163 LYS   A H    1 
ATOM   3788 H  H    B LYS   A 1 163 ? 3.616  -6.802  0.662   0.32 18.70 ?  163 LYS   A H    1 
ATOM   3789 H  HA   A LYS   A 1 163 ? 2.506  -8.196  -0.185  0.68 22.13 ?  163 LYS   A HA   1 
ATOM   3790 H  HA   B LYS   A 1 163 ? 2.631  -8.966  -0.475  0.32 19.07 ?  163 LYS   A HA   1 
ATOM   3791 H  HB2  A LYS   A 1 163 ? 2.885  -6.206  -1.327  0.68 24.95 ?  163 LYS   A HB2  1 
ATOM   3792 H  HB2  B LYS   A 1 163 ? 3.105  -6.897  -1.613  0.32 21.71 ?  163 LYS   A HB2  1 
ATOM   3793 H  HB3  A LYS   A 1 163 ? 4.449  -6.364  -1.100  0.68 24.95 ?  163 LYS   A HB3  1 
ATOM   3794 H  HB3  B LYS   A 1 163 ? 4.626  -7.345  -1.617  0.32 21.71 ?  163 LYS   A HB3  1 
ATOM   3795 H  HG2  A LYS   A 1 163 ? 4.409  -8.290  -2.475  0.68 28.51 ?  163 LYS   A HG2  1 
ATOM   3796 H  HG2  B LYS   A 1 163 ? 4.254  -8.970  -3.108  0.32 24.67 ?  163 LYS   A HG2  1 
ATOM   3797 H  HG3  A LYS   A 1 163 ? 2.870  -8.010  -2.759  0.68 28.51 ?  163 LYS   A HG3  1 
ATOM   3798 H  HG3  B LYS   A 1 163 ? 2.685  -8.956  -2.845  0.32 24.67 ?  163 LYS   A HG3  1 
ATOM   3799 H  HD2  A LYS   A 1 163 ? 3.481  -5.966  -3.763  0.68 31.90 ?  163 LYS   A HD2  1 
ATOM   3800 H  HD2  B LYS   A 1 163 ? 3.023  -7.973  -4.886  0.32 27.32 ?  163 LYS   A HD2  1 
ATOM   3801 H  HD3  A LYS   A 1 163 ? 5.011  -6.361  -3.561  0.68 31.90 ?  163 LYS   A HD3  1 
ATOM   3802 H  HD3  B LYS   A 1 163 ? 2.612  -6.807  -3.886  0.32 27.32 ?  163 LYS   A HD3  1 
ATOM   3803 H  HE2  A LYS   A 1 163 ? 4.588  -8.280  -4.930  0.68 34.52 ?  163 LYS   A HE2  1 
ATOM   3804 H  HE2  B LYS   A 1 163 ? 4.657  -5.947  -3.866  0.32 29.38 ?  163 LYS   A HE2  1 
ATOM   3805 H  HE3  A LYS   A 1 163 ? 3.172  -7.649  -5.264  0.68 34.52 ?  163 LYS   A HE3  1 
ATOM   3806 H  HE3  B LYS   A 1 163 ? 5.330  -7.303  -4.339  0.32 29.38 ?  163 LYS   A HE3  1 
ATOM   3807 H  HZ1  A LYS   A 1 163 ? 4.667  -7.132  -6.893  0.68 36.14 ?  163 LYS   A HZ1  1 
ATOM   3808 H  HZ1  B LYS   A 1 163 ? 5.320  -5.782  -6.034  0.32 30.52 ?  163 LYS   A HZ1  1 
ATOM   3809 H  HZ2  A LYS   A 1 163 ? 4.242  -5.905  -6.248  0.68 36.14 ?  163 LYS   A HZ2  1 
ATOM   3810 H  HZ2  B LYS   A 1 163 ? 4.482  -6.897  -6.425  0.32 30.52 ?  163 LYS   A HZ2  1 
ATOM   3811 H  HZ3  A LYS   A 1 163 ? 5.542  -6.471  -5.946  0.68 36.14 ?  163 LYS   A HZ3  1 
ATOM   3812 H  HZ3  B LYS   A 1 163 ? 3.878  -5.658  -5.980  0.32 30.52 ?  163 LYS   A HZ3  1 
ATOM   3813 N  N    A LEU   A 1 164 ? 5.553  -8.479  0.721   0.68 16.36 ?  164 LEU   A N    1 
ATOM   3814 N  N    B LEU   A 1 164 ? 5.691  -9.116  0.454   0.32 13.74 ?  164 LEU   A N    1 
ATOM   3815 C  CA   A LEU   A 1 164 ? 6.638  -9.443  0.864   0.68 16.33 ?  164 LEU   A CA   1 
ATOM   3816 C  CA   B LEU   A 1 164 ? 6.785  -10.049 0.714   0.32 13.42 ?  164 LEU   A CA   1 
ATOM   3817 C  C    A LEU   A 1 164 ? 6.201  -10.653 1.682   0.68 16.77 ?  164 LEU   A C    1 
ATOM   3818 C  C    B LEU   A 1 164 ? 6.332  -11.161 1.649   0.32 13.78 ?  164 LEU   A C    1 
ATOM   3819 O  O    A LEU   A 1 164 ? 6.507  -11.797 1.324   0.68 16.83 ?  164 LEU   A O    1 
ATOM   3820 O  O    B LEU   A 1 164 ? 6.603  -12.343 1.411   0.32 13.66 ?  164 LEU   A O    1 
ATOM   3821 C  CB   A LEU   A 1 164 ? 7.842  -8.757  1.501   0.68 16.09 ?  164 LEU   A CB   1 
ATOM   3822 C  CB   B LEU   A 1 164 ? 7.969  -9.306  1.339   0.32 13.07 ?  164 LEU   A CB   1 
ATOM   3823 C  CG   A LEU   A 1 164 ? 8.637  -7.883  0.534   0.68 16.50 ?  164 LEU   A CG   1 
ATOM   3824 C  CG   B LEU   A 1 164 ? 8.723  -8.257  0.523   0.32 13.41 ?  164 LEU   A CG   1 
ATOM   3825 C  CD1  A LEU   A 1 164 ? 9.640  -7.064  1.311   0.68 16.25 ?  164 LEU   A CD1  1 
ATOM   3826 C  CD1  B LEU   A 1 164 ? 9.348  -7.193  1.426   0.32 13.23 ?  164 LEU   A CD1  1 
ATOM   3827 C  CD2  A LEU   A 1 164 ? 9.348  -8.726  -0.522  0.68 16.57 ?  164 LEU   A CD2  1 
ATOM   3828 C  CD2  B LEU   A 1 164 ? 9.797  -8.935  -0.291  0.32 13.62 ?  164 LEU   A CD2  1 
ATOM   3829 H  H    A LEU   A 1 164 ? 5.706  -7.701  1.077   0.68 19.64 ?  164 LEU   A H    1 
ATOM   3830 H  H    B LEU   A 1 164 ? 5.829  -8.326  0.747   0.32 16.50 ?  164 LEU   A H    1 
ATOM   3831 H  HA   A LEU   A 1 164 ? 6.899  -9.745  -0.017  0.68 19.60 ?  164 LEU   A HA   1 
ATOM   3832 H  HA   B LEU   A 1 164 ? 7.071  -10.457 -0.117  0.32 16.11 ?  164 LEU   A HA   1 
ATOM   3833 H  HB2  A LEU   A 1 164 ? 7.536  -8.180  2.224   0.68 19.31 ?  164 LEU   A HB2  1 
ATOM   3834 H  HB2  B LEU   A 1 164 ? 7.644  -8.861  2.131   0.32 15.69 ?  164 LEU   A HB2  1 
ATOM   3835 H  HB3  A LEU   A 1 164 ? 8.442  -9.428  1.849   0.68 19.31 ?  164 LEU   A HB3  1 
ATOM   3836 H  HB3  B LEU   A 1 164 ? 8.624  -9.974  1.600   0.32 15.69 ?  164 LEU   A HB3  1 
ATOM   3837 H  HG   A LEU   A 1 164 ? 8.038  -7.269  0.079   0.68 19.81 ?  164 LEU   A HG   1 
ATOM   3838 H  HG   B LEU   A 1 164 ? 8.111  -7.819  -0.084  0.32 16.10 ?  164 LEU   A HG   1 
ATOM   3839 H  HD11 A LEU   A 1 164 ? 10.146 -6.514  0.696   0.68 19.51 ?  164 LEU   A HD11 1 
ATOM   3840 H  HD11 B LEU   A 1 164 ? 10.085 -6.773  0.958   0.32 15.88 ?  164 LEU   A HD11 1 
ATOM   3841 H  HD12 A LEU   A 1 164 ? 9.162  -6.504  1.944   0.68 19.51 ?  164 LEU   A HD12 1 
ATOM   3842 H  HD12 B LEU   A 1 164 ? 8.676  -6.528  1.644   0.32 15.88 ?  164 LEU   A HD12 1 
ATOM   3843 H  HD13 A LEU   A 1 164 ? 10.234 -7.666  1.786   0.68 19.51 ?  164 LEU   A HD13 1 
ATOM   3844 H  HD13 B LEU   A 1 164 ? 9.672  -7.615  2.239   0.32 15.88 ?  164 LEU   A HD13 1 
ATOM   3845 H  HD21 A LEU   A 1 164 ? 9.994  -8.172  -0.990  0.68 19.89 ?  164 LEU   A HD21 1 
ATOM   3846 H  HD21 B LEU   A 1 164 ? 10.161 -8.297  -0.923  0.32 16.35 ?  164 LEU   A HD21 1 
ATOM   3847 H  HD22 A LEU   A 1 164 ? 9.802  -9.462  -0.083  0.68 19.89 ?  164 LEU   A HD22 1 
ATOM   3848 H  HD22 B LEU   A 1 164 ? 10.498 -9.245  0.307   0.32 16.35 ?  164 LEU   A HD22 1 
ATOM   3849 H  HD23 A LEU   A 1 164 ? 8.692  -9.068  -1.149  0.68 19.89 ?  164 LEU   A HD23 1 
ATOM   3850 H  HD23 B LEU   A 1 164 ? 9.405  -9.685  -0.760  0.32 16.35 ?  164 LEU   A HD23 1 
ATOM   3851 N  N    A VAL   A 1 165 ? 5.492  -10.419 2.786   0.68 16.63 ?  165 VAL   A N    1 
ATOM   3852 N  N    B VAL   A 1 165 ? 5.661  -10.787 2.740   0.32 14.11 ?  165 VAL   A N    1 
ATOM   3853 C  CA   A VAL   A 1 165 ? 5.035  -11.524 3.623   0.68 16.89 ?  165 VAL   A CA   1 
ATOM   3854 C  CA   B VAL   A 1 165 ? 5.145  -11.769 3.688   0.32 14.44 ?  165 VAL   A CA   1 
ATOM   3855 C  C    A VAL   A 1 165 ? 4.016  -12.373 2.876   0.68 16.89 ?  165 VAL   A C    1 
ATOM   3856 C  C    B VAL   A 1 165 ? 4.092  -12.640 3.018   0.32 14.59 ?  165 VAL   A C    1 
ATOM   3857 O  O    A VAL   A 1 165 ? 4.127  -13.604 2.818   0.68 16.76 ?  165 VAL   A O    1 
ATOM   3858 O  O    B VAL   A 1 165 ? 4.148  -13.873 3.084   0.32 14.40 ?  165 VAL   A O    1 
ATOM   3859 C  CB   A VAL   A 1 165 ? 4.464  -10.987 4.947   0.68 17.77 ?  165 VAL   A CB   1 
ATOM   3860 C  CB   B VAL   A 1 165 ? 4.593  -11.053 4.937   0.32 15.12 ?  165 VAL   A CB   1 
ATOM   3861 C  CG1  A VAL   A 1 165 ? 3.730  -12.093 5.704   0.68 17.92 ?  165 VAL   A CG1  1 
ATOM   3862 C  CG1  B VAL   A 1 165 ? 3.814  -12.014 5.825   0.32 15.38 ?  165 VAL   A CG1  1 
ATOM   3863 C  CG2  A VAL   A 1 165 ? 5.574  -10.382 5.791   0.68 17.94 ?  165 VAL   A CG2  1 
ATOM   3864 C  CG2  B VAL   A 1 165 ? 5.726  -10.396 5.720   0.32 15.32 ?  165 VAL   A CG2  1 
ATOM   3865 H  H    A VAL   A 1 165 ? 5.270  -9.634  3.069   0.68 19.96 ?  165 VAL   A H    1 
ATOM   3866 H  H    B VAL   A 1 165 ? 5.492  -9.979  2.955   0.32 16.94 ?  165 VAL   A H    1 
ATOM   3867 H  HA   A VAL   A 1 165 ? 5.796  -12.085 3.836   0.68 20.28 ?  165 VAL   A HA   1 
ATOM   3868 H  HA   B VAL   A 1 165 ? 5.865  -12.351 3.981   0.32 17.33 ?  165 VAL   A HA   1 
ATOM   3869 H  HB   A VAL   A 1 165 ? 3.827  -10.283 4.752   0.68 21.33 ?  165 VAL   A HB   1 
ATOM   3870 H  HB   B VAL   A 1 165 ? 3.985  -10.352 4.657   0.32 18.15 ?  165 VAL   A HB   1 
ATOM   3871 H  HG11 A VAL   A 1 165 ? 3.634  -11.828 6.631   0.68 21.51 ?  165 VAL   A HG11 1 
ATOM   3872 H  HG11 B VAL   A 1 165 ? 3.708  -11.611 6.704   0.32 18.47 ?  165 VAL   A HG11 1 
ATOM   3873 H  HG12 A VAL   A 1 165 ? 2.855  -12.221 5.306   0.68 21.51 ?  165 VAL   A HG12 1 
ATOM   3874 H  HG12 B VAL   A 1 165 ? 2.943  -12.172 5.431   0.32 18.47 ?  165 VAL   A HG12 1 
ATOM   3875 H  HG13 A VAL   A 1 165 ? 4.247  -12.911 5.646   0.68 21.51 ?  165 VAL   A HG13 1 
ATOM   3876 H  HG13 B VAL   A 1 165 ? 4.307  -12.842 5.900   0.32 18.47 ?  165 VAL   A HG13 1 
ATOM   3877 H  HG21 A VAL   A 1 165 ? 5.201  -10.073 6.631   0.68 21.54 ?  165 VAL   A HG21 1 
ATOM   3878 H  HG21 B VAL   A 1 165 ? 5.357  -9.947  6.499   0.32 18.39 ?  165 VAL   A HG21 1 
ATOM   3879 H  HG22 A VAL   A 1 165 ? 6.251  -11.057 5.957   0.68 21.54 ?  165 VAL   A HG22 1 
ATOM   3880 H  HG22 B VAL   A 1 165 ? 6.355  -11.079 6.002   0.32 18.39 ?  165 VAL   A HG22 1 
ATOM   3881 H  HG23 A VAL   A 1 165 ? 5.967  -9.634  5.310   0.68 21.54 ?  165 VAL   A HG23 1 
ATOM   3882 H  HG23 B VAL   A 1 165 ? 6.173  -9.751  5.149   0.32 18.39 ?  165 VAL   A HG23 1 
ATOM   3883 N  N    A SER   A 1 166 ? 3.005  -11.729 2.293   0.68 17.17 ?  166 SER   A N    1 
ATOM   3884 N  N    B SER   A 1 166 ? 3.129  -12.010 2.339   0.32 14.75 ?  166 SER   A N    1 
ATOM   3885 C  CA   A SER   A 1 166 ? 1.901  -12.473 1.701   0.68 17.97 ?  166 SER   A CA   1 
ATOM   3886 C  CA   B SER   A 1 166 ? 1.989  -12.763 1.827   0.32 15.23 ?  166 SER   A CA   1 
ATOM   3887 C  C    A SER   A 1 166 ? 2.330  -13.274 0.487   0.68 17.97 ?  166 SER   A C    1 
ATOM   3888 C  C    B SER   A 1 166 ? 2.409  -13.785 0.774   0.32 15.02 ?  166 SER   A C    1 
ATOM   3889 O  O    A SER   A 1 166 ? 1.653  -14.248 0.137   0.68 19.19 ?  166 SER   A O    1 
ATOM   3890 O  O    B SER   A 1 166 ? 1.824  -14.871 0.697   0.32 15.07 ?  166 SER   A O    1 
ATOM   3891 C  CB   A SER   A 1 166 ? 0.776  -11.525 1.291   0.68 19.01 ?  166 SER   A CB   1 
ATOM   3892 C  CB   B SER   A 1 166 ? 0.883  -11.812 1.329   0.32 16.02 ?  166 SER   A CB   1 
ATOM   3893 O  OG   A SER   A 1 166 ? 0.174  -10.922 2.421   0.68 20.05 ?  166 SER   A OG   1 
ATOM   3894 O  OG   B SER   A 1 166 ? 1.280  -11.024 0.219   0.32 16.70 ?  166 SER   A OG   1 
ATOM   3895 H  H    A SER   A 1 166 ? 2.933  -10.876 2.237   0.68 20.60 ?  166 SER   A H    1 
ATOM   3896 H  H    B SER   A 1 166 ? 3.116  -11.170 2.166   0.32 17.71 ?  166 SER   A H    1 
ATOM   3897 H  HA   A SER   A 1 166 ? 1.543  -13.092 2.364   0.68 21.57 ?  166 SER   A HA   1 
ATOM   3898 H  HA   B SER   A 1 166 ? 1.601  -13.260 2.559   0.32 18.28 ?  166 SER   A HA   1 
ATOM   3899 H  HB2  A SER   A 1 166 ? 1.141  -10.836 0.718   0.68 22.82 ?  166 SER   A HB2  1 
ATOM   3900 H  HB2  B SER   A 1 166 ? 0.112  -12.334 1.059   0.32 19.23 ?  166 SER   A HB2  1 
ATOM   3901 H  HB3  A SER   A 1 166 ? 0.098  -12.031 0.811   0.68 22.82 ?  166 SER   A HB3  1 
ATOM   3902 H  HB3  B SER   A 1 166 ? 0.625  -11.218 2.061   0.32 19.23 ?  166 SER   A HB3  1 
ATOM   3903 H  HG   A SER   A 1 166 ? -0.435 -10.402 2.178   0.68 24.06 ?  166 SER   A HG   1 
ATOM   3904 H  HG   B SER   A 1 166 ? 0.660  -10.501 -0.007  0.32 20.04 ?  166 SER   A HG   1 
ATOM   3905 N  N    A SER   A 1 167 ? 3.418  -12.886 -0.173  0.68 16.80 ?  167 SER   A N    1 
ATOM   3906 N  N    B SER   A 1 167 ? 3.454  -13.494 -0.001  0.32 15.23 ?  167 SER   A N    1 
ATOM   3907 C  CA   A SER   A 1 167 ? 3.895  -13.605 -1.343  0.68 17.14 ?  167 SER   A CA   1 
ATOM   3908 C  CA   B SER   A 1 167 ? 3.824  -14.330 -1.136  0.32 15.24 ?  167 SER   A CA   1 
ATOM   3909 C  C    A SER   A 1 167 ? 5.045  -14.554 -1.036  0.68 17.49 ?  167 SER   A C    1 
ATOM   3910 C  C    B SER   A 1 167 ? 4.988  -15.273 -0.834  0.32 14.85 ?  167 SER   A C    1 
ATOM   3911 O  O    A SER   A 1 167 ? 5.573  -15.177 -1.962  0.68 18.55 ?  167 SER   A O    1 
ATOM   3912 O  O    B SER   A 1 167 ? 5.578  -15.832 -1.765  0.32 15.39 ?  167 SER   A O    1 
ATOM   3913 C  CB   A SER   A 1 167 ? 4.326  -12.620 -2.437  0.68 17.33 ?  167 SER   A CB   1 
ATOM   3914 C  CB   B SER   A 1 167 ? 4.132  -13.459 -2.357  0.32 15.68 ?  167 SER   A CB   1 
ATOM   3915 O  OG   A SER   A 1 167 ? 5.388  -11.793 -1.992  0.68 17.68 ?  167 SER   A OG   1 
ATOM   3916 O  OG   B SER   A 1 167 ? 5.347  -12.740 -2.199  0.32 16.06 ?  167 SER   A OG   1 
ATOM   3917 H  H    A SER   A 1 167 ? 3.887  -12.190 0.037   0.68 20.17 ?  167 SER   A H    1 
ATOM   3918 H  H    B SER   A 1 167 ? 3.973  -12.821 0.130   0.32 18.28 ?  167 SER   A H    1 
ATOM   3919 H  HA   A SER   A 1 167 ? 3.160  -14.125 -1.697  0.68 20.58 ?  167 SER   A HA   1 
ATOM   3920 H  HA   B SER   A 1 167 ? 3.068  -14.889 -1.360  0.32 18.30 ?  167 SER   A HA   1 
ATOM   3921 H  HB2  A SER   A 1 167 ? 4.620  -13.124 -3.211  0.68 20.80 ?  167 SER   A HB2  1 
ATOM   3922 H  HB2  B SER   A 1 167 ? 4.200  -14.033 -3.135  0.32 18.83 ?  167 SER   A HB2  1 
ATOM   3923 H  HB3  A SER   A 1 167 ? 3.564  -12.064 -2.678  0.68 20.80 ?  167 SER   A HB3  1 
ATOM   3924 H  HB3  B SER   A 1 167 ? 3.404  -12.826 -2.477  0.32 18.83 ?  167 SER   A HB3  1 
ATOM   3925 H  HG   A SER   A 1 167 ? 5.130  -11.346 -1.326  0.68 21.22 ?  167 SER   A HG   1 
ATOM   3926 H  HG   B SER   A 1 167 ? 5.296  -12.243 -1.524  0.32 19.28 ?  167 SER   A HG   1 
ATOM   3927 N  N    A PHE   A 1 168 ? 5.453  -14.681 0.225   0.68 16.94 ?  168 PHE   A N    1 
ATOM   3928 N  N    B PHE   A 1 168 ? 5.296  -15.508 0.443   0.32 14.00 ?  168 PHE   A N    1 
ATOM   3929 C  CA   A PHE   A 1 168 ? 6.630  -15.484 0.530   0.68 17.68 ?  168 PHE   A CA   1 
ATOM   3930 C  CA   B PHE   A 1 168 ? 6.563  -16.151 0.781   0.32 13.84 ?  168 PHE   A CA   1 
ATOM   3931 C  C    A PHE   A 1 168 ? 6.322  -16.967 0.402   0.68 19.39 ?  168 PHE   A C    1 
ATOM   3932 C  C    B PHE   A 1 168 ? 6.502  -17.671 0.677   0.32 14.52 ?  168 PHE   A C    1 
ATOM   3933 O  O    A PHE   A 1 168 ? 5.324  -17.457 0.938   0.68 20.80 ?  168 PHE   A O    1 
ATOM   3934 O  O    B PHE   A 1 168 ? 7.367  -18.285 0.041   0.32 14.30 ?  168 PHE   A O    1 
ATOM   3935 C  CB   A PHE   A 1 168 ? 7.148  -15.207 1.937   0.68 17.06 ?  168 PHE   A CB   1 
ATOM   3936 C  CB   B PHE   A 1 168 ? 7.023  -15.741 2.180   0.32 14.30 ?  168 PHE   A CB   1 
ATOM   3937 C  CG   A PHE   A 1 168 ? 8.410  -15.958 2.246   0.68 16.32 ?  168 PHE   A CG   1 
ATOM   3938 C  CG   B PHE   A 1 168 ? 8.339  -16.346 2.572   0.32 14.63 ?  168 PHE   A CG   1 
ATOM   3939 C  CD1  A PHE   A 1 168 ? 9.595  -15.593 1.637   0.68 16.43 ?  168 PHE   A CD1  1 
ATOM   3940 C  CD1  B PHE   A 1 168 ? 9.514  -15.901 1.994   0.32 15.09 ?  168 PHE   A CD1  1 
ATOM   3941 C  CD2  A PHE   A 1 168 ? 8.413  -17.051 3.100   0.68 16.05 ?  168 PHE   A CD2  1 
ATOM   3942 C  CD2  B PHE   A 1 168 ? 8.404  -17.369 3.504   0.32 14.68 ?  168 PHE   A CD2  1 
ATOM   3943 C  CE1  A PHE   A 1 168 ? 10.760 -16.280 1.889   0.68 15.94 ?  168 PHE   A CE1  1 
ATOM   3944 C  CE1  B PHE   A 1 168 ? 10.727 -16.455 2.341   0.32 15.24 ?  168 PHE   A CE1  1 
ATOM   3945 C  CE2  A PHE   A 1 168 ? 9.589  -17.741 3.359   0.68 16.12 ?  168 PHE   A CE2  1 
ATOM   3946 C  CE2  B PHE   A 1 168 ? 9.620  -17.925 3.857   0.32 15.15 ?  168 PHE   A CE2  1 
ATOM   3947 C  CZ   A PHE   A 1 168 ? 10.758 -17.353 2.749   0.68 15.71 ?  168 PHE   A CZ   1 
ATOM   3948 C  CZ   B PHE   A 1 168 ? 10.781 -17.467 3.274   0.32 15.33 ?  168 PHE   A CZ   1 
ATOM   3949 H  H    A PHE   A 1 168 ? 5.076  -14.313 0.908   0.68 20.33 ?  168 PHE   A H    1 
ATOM   3950 H  H    B PHE   A 1 168 ? 4.797  -15.317 1.118   0.32 16.81 ?  168 PHE   A H    1 
ATOM   3951 H  HA   A PHE   A 1 168 ? 7.331  -15.262 -0.101  0.68 21.22 ?  168 PHE   A HA   1 
ATOM   3952 H  HA   B PHE   A 1 168 ? 7.238  -15.849 0.156   0.32 16.61 ?  168 PHE   A HA   1 
ATOM   3953 H  HB2  A PHE   A 1 168 ? 7.328  -14.260 2.027   0.68 20.47 ?  168 PHE   A HB2  1 
ATOM   3954 H  HB2  B PHE   A 1 168 ? 7.123  -14.777 2.207   0.32 17.16 ?  168 PHE   A HB2  1 
ATOM   3955 H  HB3  A PHE   A 1 168 ? 6.470  -15.478 2.580   0.68 20.47 ?  168 PHE   A HB3  1 
ATOM   3956 H  HB3  B PHE   A 1 168 ? 6.363  -16.026 2.828   0.32 17.16 ?  168 PHE   A HB3  1 
ATOM   3957 H  HD1  A PHE   A 1 168 ? 9.606  -14.867 1.054   0.68 19.72 ?  168 PHE   A HD1  1 
ATOM   3958 H  HD1  B PHE   A 1 168 ? 9.485  -15.217 1.364   0.32 18.12 ?  168 PHE   A HD1  1 
ATOM   3959 H  HD2  A PHE   A 1 168 ? 7.624  -17.318 3.515   0.68 19.27 ?  168 PHE   A HD2  1 
ATOM   3960 H  HD2  B PHE   A 1 168 ? 7.623  -17.681 3.901   0.32 17.62 ?  168 PHE   A HD2  1 
ATOM   3961 H  HE1  A PHE   A 1 168 ? 11.554 -16.018 1.480   0.68 19.14 ?  168 PHE   A HE1  1 
ATOM   3962 H  HE1  B PHE   A 1 168 ? 11.511 -16.143 1.948   0.32 18.29 ?  168 PHE   A HE1  1 
ATOM   3963 H  HE2  A PHE   A 1 168 ? 9.583  -18.469 3.939   0.68 19.35 ?  168 PHE   A HE2  1 
ATOM   3964 H  HE2  B PHE   A 1 168 ? 9.653  -18.610 4.486   0.32 18.19 ?  168 PHE   A HE2  1 
ATOM   3965 H  HZ   A PHE   A 1 168 ? 11.549 -17.815 2.920   0.68 18.86 ?  168 PHE   A HZ   1 
ATOM   3966 H  HZ   B PHE   A 1 168 ? 11.599 -17.841 3.510   0.32 18.41 ?  168 PHE   A HZ   1 
ATOM   3967 N  N    A LEU   A 1 169 ? 7.208  -17.691 -0.275  0.68 20.96 ?  169 LEU   A N    1 
ATOM   3968 N  N    B LEU   A 1 169 ? 5.528  -18.301 1.327   0.32 16.00 ?  169 LEU   A N    1 
ATOM   3969 C  CA   A LEU   A 1 169 ? 7.027  -19.126 -0.436  0.68 23.18 ?  169 LEU   A CA   1 
ATOM   3970 C  CA   B LEU   A 1 169 ? 5.514  -19.760 1.415   0.32 17.77 ?  169 LEU   A CA   1 
ATOM   3971 C  C    A LEU   A 1 169 ? 7.860  -19.887 0.591   0.68 23.05 ?  169 LEU   A C    1 
ATOM   3972 C  C    B LEU   A 1 169 ? 4.950  -20.413 0.154   0.32 18.92 ?  169 LEU   A C    1 
ATOM   3973 O  O    A LEU   A 1 169 ? 7.305  -20.384 1.575   0.68 23.55 ?  169 LEU   A O    1 
ATOM   3974 O  O    B LEU   A 1 169 ? 4.033  -19.896 -0.487  0.32 19.16 ?  169 LEU   A O    1 
ATOM   3975 C  CB   A LEU   A 1 169 ? 7.364  -19.563 -1.867  0.68 24.69 ?  169 LEU   A CB   1 
ATOM   3976 C  CB   B LEU   A 1 169 ? 4.721  -20.223 2.641   0.32 18.16 ?  169 LEU   A CB   1 
ATOM   3977 C  CG   A LEU   A 1 169 ? 7.033  -21.018 -2.223  0.68 26.05 ?  169 LEU   A CG   1 
ATOM   3978 C  CG   B LEU   A 1 169 ? 4.951  -21.692 3.012   0.32 18.71 ?  169 LEU   A CG   1 
ATOM   3979 C  CD1  A LEU   A 1 169 ? 5.594  -21.356 -1.863  0.68 26.64 ?  169 LEU   A CD1  1 
ATOM   3980 C  CD1  B LEU   A 1 169 ? 6.397  -21.909 3.436   0.32 19.26 ?  169 LEU   A CD1  1 
ATOM   3981 C  CD2  A LEU   A 1 169 ? 7.285  -21.286 -3.702  0.68 26.38 ?  169 LEU   A CD2  1 
ATOM   3982 C  CD2  B LEU   A 1 169 ? 3.994  -22.139 4.105   0.32 18.94 ?  169 LEU   A CD2  1 
ATOM   3983 O  OXT  A LEU   A 1 169 ? 9.083  -20.015 0.481   0.68 22.35 -1 169 LEU   A OXT  1 
ATOM   3984 O  OXT  B LEU   A 1 169 ? 5.403  -21.487 -0.245  0.32 19.84 -1 169 LEU   A OXT  1 
ATOM   3985 H  H    A LEU   A 1 169 ? 7.923  -17.377 -0.641  0.68 25.15 ?  169 LEU   A H    1 
ATOM   3986 H  H    B LEU   A 1 169 ? 4.874  -17.912 1.729   0.32 19.20 ?  169 LEU   A H    1 
ATOM   3987 H  HA   A LEU   A 1 169 ? 6.104  -19.344 -0.266  0.68 27.82 ?  169 LEU   A HA   1 
ATOM   3988 H  HA   B LEU   A 1 169 ? 6.428  -20.063 1.521   0.32 21.33 ?  169 LEU   A HA   1 
ATOM   3989 H  HB2  A LEU   A 1 169 ? 6.867  -18.999 -2.481  0.68 29.64 ?  169 LEU   A HB2  1 
ATOM   3990 H  HB2  B LEU   A 1 169 ? 4.978  -19.682 3.405   0.32 21.79 ?  169 LEU   A HB2  1 
ATOM   3991 H  HB3  A LEU   A 1 169 ? 8.313  -19.442 -2.014  0.68 29.64 ?  169 LEU   A HB3  1 
ATOM   3992 H  HB3  B LEU   A 1 169 ? 3.776  -20.110 2.462   0.32 21.79 ?  169 LEU   A HB3  1 
ATOM   3993 H  HG   A LEU   A 1 169 ? 7.612  -21.607 -1.715  0.68 31.27 ?  169 LEU   A HG   1 
ATOM   3994 H  HG   B LEU   A 1 169 ? 4.787  -22.241 2.231   0.32 22.46 ?  169 LEU   A HG   1 
ATOM   3995 H  HD11 A LEU   A 1 169 ? 5.352  -22.197 -2.282  0.68 31.97 ?  169 LEU   A HD11 1 
ATOM   3996 H  HD11 B LEU   A 1 169 ? 6.468  -22.762 3.890   0.32 23.11 ?  169 LEU   A HD11 1 
ATOM   3997 H  HD12 A LEU   A 1 169 ? 5.519  -21.435 -0.899  0.68 31.97 ?  169 LEU   A HD12 1 
ATOM   3998 H  HD12 B LEU   A 1 169 ? 6.964  -21.908 2.647   0.32 23.11 ?  169 LEU   A HD12 1 
ATOM   3999 H  HD13 A LEU   A 1 169 ? 5.013  -20.648 -2.185  0.68 31.97 ?  169 LEU   A HD13 1 
ATOM   4000 H  HD13 B LEU   A 1 169 ? 6.664  -21.193 4.035   0.32 23.11 ?  169 LEU   A HD13 1 
ATOM   4001 H  HD21 A LEU   A 1 169 ? 7.075  -22.214 -3.896  0.68 31.66 ?  169 LEU   A HD21 1 
ATOM   4002 H  HD21 B LEU   A 1 169 ? 4.164  -23.072 4.309   0.32 22.73 ?  169 LEU   A HD21 1 
ATOM   4003 H  HD22 A LEU   A 1 169 ? 6.717  -20.703 -4.230  0.68 31.66 ?  169 LEU   A HD22 1 
ATOM   4004 H  HD22 B LEU   A 1 169 ? 4.143  -21.596 4.895   0.32 22.73 ?  169 LEU   A HD22 1 
ATOM   4005 H  HD23 A LEU   A 1 169 ? 8.217  -21.110 -3.901  0.68 31.66 ?  169 LEU   A HD23 1 
ATOM   4006 H  HD23 B LEU   A 1 169 ? 3.085  -22.028 3.791   0.32 22.73 ?  169 LEU   A HD23 1 
ATOM   4007 N  N    A SER   B 1 1   ? 50.755 -9.253  -23.685 0.68 27.44 ?  1   SER   B N    1 
ATOM   4008 N  N    B SER   B 1 1   ? 50.693 -9.270  -23.651 0.32 26.80 ?  1   SER   B N    1 
ATOM   4009 C  CA   A SER   B 1 1   ? 51.255 -10.299 -22.769 0.68 27.43 ?  1   SER   B CA   1 
ATOM   4010 C  CA   B SER   B 1 1   ? 51.208 -10.271 -22.694 0.32 26.70 ?  1   SER   B CA   1 
ATOM   4011 C  C    A SER   B 1 1   ? 50.179 -11.344 -22.504 0.68 26.66 ?  1   SER   B C    1 
ATOM   4012 C  C    B SER   B 1 1   ? 50.172 -11.356 -22.460 0.32 26.14 ?  1   SER   B C    1 
ATOM   4013 O  O    A SER   B 1 1   ? 48.987 -11.140 -22.774 0.68 26.59 ?  1   SER   B O    1 
ATOM   4014 O  O    B SER   B 1 1   ? 48.978 -11.169 -22.713 0.32 26.13 ?  1   SER   B O    1 
ATOM   4015 C  CB   A SER   B 1 1   ? 51.722 -9.686  -21.451 0.68 28.03 ?  1   SER   B CB   1 
ATOM   4016 C  CB   B SER   B 1 1   ? 51.569 -9.612  -21.367 0.32 27.03 ?  1   SER   B CB   1 
ATOM   4017 O  OG   A SER   B 1 1   ? 50.624 -9.408  -20.605 0.68 29.64 ?  1   SER   B OG   1 
ATOM   4018 O  OG   B SER   B 1 1   ? 50.414 -9.417  -20.572 0.32 27.79 ?  1   SER   B OG   1 
ATOM   4019 H  H1   A SER   B 1 1   ? 50.649 -9.605  -24.493 0.68 32.94 ?  1   SER   B H1   1 
ATOM   4020 H  H1   B SER   B 1 1   ? 50.623 -9.647  -24.452 0.32 32.16 ?  1   SER   B H1   1 
ATOM   4021 H  H2   A SER   B 1 1   ? 49.981 -8.950  -23.380 0.68 32.94 ?  1   SER   B H2   1 
ATOM   4022 H  H2   B SER   B 1 1   ? 49.898 -8.991  -23.377 0.32 32.16 ?  1   SER   B H2   1 
ATOM   4023 H  H3   A SER   B 1 1   ? 51.349 -8.594  -23.719 0.68 32.94 ?  1   SER   B H3   1 
ATOM   4024 H  H3   B SER   B 1 1   ? 51.261 -8.590  -23.686 0.32 32.16 ?  1   SER   B H3   1 
ATOM   4025 H  HA   A SER   B 1 1   ? 52.012 -10.731 -23.190 0.68 32.92 ?  1   SER   B HA   1 
ATOM   4026 H  HA   B SER   B 1 1   ? 52.002 -10.674 -23.068 0.32 32.04 ?  1   SER   B HA   1 
ATOM   4027 H  HB2  A SER   B 1 1   ? 52.308 -10.317 -21.008 0.68 33.65 ?  1   SER   B HB2  1 
ATOM   4028 H  HB2  B SER   B 1 1   ? 52.193 -10.187 -20.898 0.32 32.44 ?  1   SER   B HB2  1 
ATOM   4029 H  HB3  A SER   B 1 1   ? 52.201 -8.862  -21.637 0.68 33.65 ?  1   SER   B HB3  1 
ATOM   4030 H  HB3  B SER   B 1 1   ? 51.977 -8.750  -21.542 0.32 32.44 ?  1   SER   B HB3  1 
ATOM   4031 H  HG   A SER   B 1 1   ? 50.884 -8.955  -19.946 0.68 35.57 ?  1   SER   B HG   1 
ATOM   4032 H  HG   B SER   B 1 1   ? 50.595 -8.905  -19.931 0.32 33.35 ?  1   SER   B HG   1 
ATOM   4033 N  N    A MET   B 1 2   ? 50.622 -12.467 -21.956 0.68 25.91 ?  2   MET   B N    1 
ATOM   4034 N  N    B MET   B 1 2   ? 50.642 -12.491 -21.964 0.32 25.42 ?  2   MET   B N    1 
ATOM   4035 C  CA   A MET   B 1 2   ? 49.802 -13.660 -21.799 0.68 26.03 ?  2   MET   B CA   1 
ATOM   4036 C  CA   B MET   B 1 2   ? 49.820 -13.676 -21.774 0.32 24.93 ?  2   MET   B CA   1 
ATOM   4037 C  C    A MET   B 1 2   ? 49.544 -13.871 -20.314 0.68 23.95 ?  2   MET   B C    1 
ATOM   4038 C  C    B MET   B 1 2   ? 49.556 -13.827 -20.286 0.32 23.41 ?  2   MET   B C    1 
ATOM   4039 O  O    A MET   B 1 2   ? 50.466 -14.191 -19.559 0.68 24.16 ?  2   MET   B O    1 
ATOM   4040 O  O    B MET   B 1 2   ? 50.484 -14.059 -19.504 0.32 23.56 ?  2   MET   B O    1 
ATOM   4041 C  CB   A MET   B 1 2   ? 50.538 -14.849 -22.404 0.68 29.43 ?  2   MET   B CB   1 
ATOM   4042 C  CB   B MET   B 1 2   ? 50.556 -14.889 -22.316 0.32 26.43 ?  2   MET   B CB   1 
ATOM   4043 C  CG   A MET   B 1 2   ? 49.698 -16.102 -22.574 0.68 32.59 ?  2   MET   B CG   1 
ATOM   4044 C  CG   B MET   B 1 2   ? 49.659 -16.045 -22.737 0.32 27.58 ?  2   MET   B CG   1 
ATOM   4045 S  SD   A MET   B 1 2   ? 50.540 -17.313 -23.608 0.68 35.66 ?  2   MET   B SD   1 
ATOM   4046 S  SD   B MET   B 1 2   ? 50.511 -17.115 -23.898 0.32 28.56 ?  2   MET   B SD   1 
ATOM   4047 C  CE   A MET   B 1 2   ? 51.063 -16.254 -24.950 0.68 35.89 ?  2   MET   B CE   1 
ATOM   4048 C  CE   B MET   B 1 2   ? 51.410 -15.891 -24.828 0.32 28.93 ?  2   MET   B CE   1 
ATOM   4049 H  H    A MET   B 1 2   ? 51.426 -12.567 -21.659 0.68 31.10 ?  2   MET   B H    1 
ATOM   4050 H  H    B MET   B 1 2   ? 51.462 -12.608 -21.722 0.32 30.51 ?  2   MET   B H    1 
ATOM   4051 H  HA   A MET   B 1 2   ? 48.965 -13.549 -22.271 0.68 31.24 ?  2   MET   B HA   1 
ATOM   4052 H  HA   B MET   B 1 2   ? 48.988 -13.590 -22.263 0.32 29.93 ?  2   MET   B HA   1 
ATOM   4053 H  HB2  A MET   B 1 2   ? 50.861 -14.561 -23.269 0.68 35.32 ?  2   MET   B HB2  1 
ATOM   4054 H  HB2  B MET   B 1 2   ? 51.079 -14.547 -23.050 0.32 31.72 ?  2   MET   B HB2  1 
ATOM   4055 H  HB3  A MET   B 1 2   ? 51.288 -15.087 -21.842 0.68 35.32 ?  2   MET   B HB3  1 
ATOM   4056 H  HB3  B MET   B 1 2   ? 51.150 -15.246 -21.652 0.32 31.72 ?  2   MET   B HB3  1 
ATOM   4057 H  HG2  A MET   B 1 2   ? 49.535 -16.499 -21.700 0.68 39.11 ?  2   MET   B HG2  1 
ATOM   4058 H  HG2  B MET   B 1 2   ? 49.421 -16.572 -21.950 0.32 33.11 ?  2   MET   B HG2  1 
ATOM   4059 H  HG3  A MET   B 1 2   ? 48.858 -15.878 -23.003 0.68 39.11 ?  2   MET   B HG3  1 
ATOM   4060 H  HG3  B MET   B 1 2   ? 48.859 -15.713 -23.170 0.32 33.11 ?  2   MET   B HG3  1 
ATOM   4061 H  HE1  A MET   B 1 2   ? 51.208 -16.795 -25.728 0.68 43.08 ?  2   MET   B HE1  1 
ATOM   4062 H  HE1  B MET   B 1 2   ? 51.597 -16.283 -25.663 0.32 34.72 ?  2   MET   B HE1  1 
ATOM   4063 H  HE2  A MET   B 1 2   ? 50.361 -15.601 -25.118 0.68 43.08 ?  2   MET   B HE2  1 
ATOM   4064 H  HE2  B MET   B 1 2   ? 50.851 -15.102 -24.958 0.32 34.72 ?  2   MET   B HE2  1 
ATOM   4065 H  HE3  A MET   B 1 2   ? 51.886 -15.793 -24.702 0.68 43.08 ?  2   MET   B HE3  1 
ATOM   4066 H  HE3  B MET   B 1 2   ? 52.239 -15.650 -24.362 0.32 34.72 ?  2   MET   B HE3  1 
ATOM   4067 N  N    . VAL   B 1 3   ? 48.296 -13.675 -19.898 1.00 21.76 ?  3   VAL   B N    1 
ATOM   4068 C  CA   . VAL   B 1 3   ? 47.873 -13.909 -18.527 1.00 20.38 ?  3   VAL   B CA   1 
ATOM   4069 C  C    . VAL   B 1 3   ? 46.639 -14.800 -18.556 1.00 18.53 ?  3   VAL   B C    1 
ATOM   4070 O  O    . VAL   B 1 3   ? 45.911 -14.870 -19.551 1.00 19.17 ?  3   VAL   B O    1 
ATOM   4071 C  CB   . VAL   B 1 3   ? 47.586 -12.599 -17.761 1.00 22.07 ?  3   VAL   B CB   1 
ATOM   4072 C  CG1  . VAL   B 1 3   ? 48.860 -11.751 -17.638 1.00 22.80 ?  3   VAL   B CG1  1 
ATOM   4073 C  CG2  . VAL   B 1 3   ? 46.474 -11.818 -18.443 1.00 22.84 ?  3   VAL   B CG2  1 
ATOM   4074 H  H    A VAL   B 1 3   ? 47.662 -13.411 -20.414 0.68 26.12 ?  3   VAL   B H    1 
ATOM   4075 H  H    B VAL   B 1 3   ? 47.662 -13.426 -20.422 0.32 26.12 ?  3   VAL   B H    1 
ATOM   4076 H  HA   . VAL   B 1 3   ? 48.573 -14.386 -18.055 1.00 24.46 ?  3   VAL   B HA   1 
ATOM   4077 H  HB   . VAL   B 1 3   ? 47.289 -12.823 -16.865 1.00 26.49 ?  3   VAL   B HB   1 
ATOM   4078 H  HG11 . VAL   B 1 3   ? 48.650 -10.942 -17.147 1.00 27.36 ?  3   VAL   B HG11 1 
ATOM   4079 H  HG12 . VAL   B 1 3   ? 49.532 -12.263 -17.162 1.00 27.36 ?  3   VAL   B HG12 1 
ATOM   4080 H  HG13 . VAL   B 1 3   ? 49.177 -11.530 -18.526 1.00 27.36 ?  3   VAL   B HG13 1 
ATOM   4081 H  HG21 . VAL   B 1 3   ? 46.399 -10.949 -18.025 1.00 27.41 ?  3   VAL   B HG21 1 
ATOM   4082 H  HG22 . VAL   B 1 3   ? 46.688 -11.718 -19.383 1.00 27.41 ?  3   VAL   B HG22 1 
ATOM   4083 H  HG23 . VAL   B 1 3   ? 45.639 -12.306 -18.345 1.00 27.41 ?  3   VAL   B HG23 1 
ATOM   4084 N  N    . ASN   B 1 4   ? 46.413 -15.494 -17.444 1.00 16.42 ?  4   ASN   B N    1 
ATOM   4085 C  CA   . ASN   B 1 4   ? 45.275 -16.404 -17.324 1.00 15.60 ?  4   ASN   B CA   1 
ATOM   4086 C  C    . ASN   B 1 4   ? 45.216 -17.368 -18.506 1.00 15.77 ?  4   ASN   B C    1 
ATOM   4087 O  O    . ASN   B 1 4   ? 44.159 -17.607 -19.082 1.00 16.46 ?  4   ASN   B O    1 
ATOM   4088 C  CB   . ASN   B 1 4   ? 43.961 -15.633 -17.168 1.00 14.99 ?  4   ASN   B CB   1 
ATOM   4089 C  CG   . ASN   B 1 4   ? 43.916 -14.820 -15.889 1.00 14.38 ?  4   ASN   B CG   1 
ATOM   4090 O  OD1  . ASN   B 1 4   ? 44.201 -15.330 -14.807 1.00 14.08 ?  4   ASN   B OD1  1 
ATOM   4091 N  ND2  . ASN   B 1 4   ? 43.571 -13.544 -16.008 1.00 15.40 ?  4   ASN   B ND2  1 
ATOM   4092 H  H    . ASN   B 1 4   ? 46.911 -15.464 -16.745 1.00 19.71 ?  4   ASN   B H    1 
ATOM   4093 H  HA   . ASN   B 1 4   ? 45.395 -16.937 -16.525 1.00 18.72 ?  4   ASN   B HA   1 
ATOM   4094 H  HB2  . ASN   B 1 4   ? 43.861 -15.022 -17.915 1.00 17.99 ?  4   ASN   B HB2  1 
ATOM   4095 H  HB3  . ASN   B 1 4   ? 43.224 -16.263 -17.154 1.00 17.99 ?  4   ASN   B HB3  1 
ATOM   4096 H  HD21 . ASN   B 1 4   ? 43.535 -13.040 -15.309 1.00 18.49 ?  4   ASN   B HD21 1 
ATOM   4097 H  HD22 . ASN   B 1 4   ? 43.384 -13.216 -16.780 1.00 18.49 ?  4   ASN   B HD22 1 
ATOM   4098 N  N    . SER   B 1 5   ? 46.373 -17.914 -18.882 1.00 16.86 ?  5   SER   B N    1 
ATOM   4099 C  CA   . SER   B 1 5   ? 46.471 -18.830 -20.019 1.00 19.06 ?  5   SER   B CA   1 
ATOM   4100 C  C    . SER   B 1 5   ? 46.454 -20.248 -19.466 1.00 20.73 ?  5   SER   B C    1 
ATOM   4101 O  O    . SER   B 1 5   ? 47.476 -20.920 -19.362 1.00 22.76 ?  5   SER   B O    1 
ATOM   4102 C  CB   . SER   B 1 5   ? 47.732 -18.548 -20.832 1.00 20.58 ?  5   SER   B CB   1 
ATOM   4103 O  OG   . SER   B 1 5   ? 48.897 -18.707 -20.040 1.00 23.28 ?  5   SER   B OG   1 
ATOM   4104 H  H    . SER   B 1 5   ? 47.123 -17.769 -18.492 1.00 20.23 ?  5   SER   B H    1 
ATOM   4105 H  HA   . SER   B 1 5   ? 45.702 -18.717 -20.598 1.00 22.87 ?  5   SER   B HA   1 
ATOM   4106 H  HB2  . SER   B 1 5   ? 47.766 -19.162 -21.586 1.00 24.70 ?  5   SER   B HB2  1 
ATOM   4107 H  HB3  . SER   B 1 5   ? 47.688 -17.635 -21.158 1.00 24.70 ?  5   SER   B HB3  1 
ATOM   4108 H  HG   . SER   B 1 5   ? 48.958 -19.504 -19.780 1.00 27.95 ?  5   SER   B HG   1 
ATOM   4109 N  N    . PHE   B 1 6   ? 45.262 -20.686 -19.076 1.00 21.31 ?  6   PHE   B N    1 
ATOM   4110 C  CA   . PHE   B 1 6   ? 45.073 -22.026 -18.543 1.00 20.80 ?  6   PHE   B CA   1 
ATOM   4111 C  C    . PHE   B 1 6   ? 44.992 -23.013 -19.697 1.00 24.40 ?  6   PHE   B C    1 
ATOM   4112 O  O    . PHE   B 1 6   ? 44.306 -22.757 -20.691 1.00 26.43 ?  6   PHE   B O    1 
ATOM   4113 C  CB   . PHE   B 1 6   ? 43.786 -22.080 -17.720 1.00 18.98 ?  6   PHE   B CB   1 
ATOM   4114 C  CG   . PHE   B 1 6   ? 43.809 -21.211 -16.492 1.00 16.99 ?  6   PHE   B CG   1 
ATOM   4115 C  CD1  . PHE   B 1 6   ? 44.318 -21.690 -15.301 1.00 15.85 ?  6   PHE   B CD1  1 
ATOM   4116 C  CD2  . PHE   B 1 6   ? 43.322 -19.913 -16.533 1.00 16.57 ?  6   PHE   B CD2  1 
ATOM   4117 C  CE1  . PHE   B 1 6   ? 44.328 -20.896 -14.164 1.00 15.53 ?  6   PHE   B CE1  1 
ATOM   4118 C  CE2  . PHE   B 1 6   ? 43.338 -19.110 -15.407 1.00 17.22 ?  6   PHE   B CE2  1 
ATOM   4119 C  CZ   . PHE   B 1 6   ? 43.849 -19.594 -14.223 1.00 16.36 ?  6   PHE   B CZ   1 
ATOM   4120 H  H    . PHE   B 1 6   ? 44.537 -20.226 -19.119 1.00 25.58 ?  6   PHE   B H    1 
ATOM   4121 H  HA   . PHE   B 1 6   ? 45.817 -22.270 -17.974 1.00 24.96 ?  6   PHE   B HA   1 
ATOM   4122 H  HB2  . PHE   B 1 6   ? 43.045 -21.787 -18.274 1.00 22.78 ?  6   PHE   B HB2  1 
ATOM   4123 H  HB3  . PHE   B 1 6   ? 43.633 -22.995 -17.430 1.00 22.78 ?  6   PHE   B HB3  1 
ATOM   4124 H  HD1  . PHE   B 1 6   ? 44.649 -22.559 -15.257 1.00 19.03 ?  6   PHE   B HD1  1 
ATOM   4125 H  HD2  . PHE   B 1 6   ? 42.974 -19.584 -17.327 1.00 19.89 ?  6   PHE   B HD2  1 
ATOM   4126 H  HE1  . PHE   B 1 6   ? 44.683 -21.225 -13.367 1.00 18.64 ?  6   PHE   B HE1  1 
ATOM   4127 H  HE2  . PHE   B 1 6   ? 43.003 -18.244 -15.449 1.00 20.66 ?  6   PHE   B HE2  1 
ATOM   4128 H  HZ   . PHE   B 1 6   ? 43.857 -19.060 -13.462 1.00 19.64 ?  6   PHE   B HZ   1 
ATOM   4129 N  N    . SER   B 1 7   ? 45.709 -24.128 -19.573 1.00 25.76 ?  7   SER   B N    1 
ATOM   4130 C  CA   . SER   B 1 7   ? 45.784 -25.119 -20.636 1.00 28.88 ?  7   SER   B CA   1 
ATOM   4131 C  C    . SER   B 1 7   ? 45.722 -26.520 -20.048 1.00 27.79 ?  7   SER   B C    1 
ATOM   4132 O  O    . SER   B 1 7   ? 46.321 -26.795 -19.004 1.00 28.56 ?  7   SER   B O    1 
ATOM   4133 C  CB   . SER   B 1 7   ? 47.079 -24.953 -21.445 1.00 32.14 ?  7   SER   B CB   1 
ATOM   4134 O  OG   . SER   B 1 7   ? 47.056 -25.753 -22.615 1.00 33.76 ?  7   SER   B OG   1 
ATOM   4135 H  H    . SER   B 1 7   ? 46.176 -24.328 -18.875 1.00 30.92 ?  7   SER   B H    1 
ATOM   4136 H  HA   . SER   B 1 7   ? 45.034 -25.007 -21.235 1.00 34.66 ?  7   SER   B HA   1 
ATOM   4137 H  HB2  . SER   B 1 7   ? 47.174 -24.020 -21.701 1.00 38.57 ?  7   SER   B HB2  1 
ATOM   4138 H  HB3  . SER   B 1 7   ? 47.833 -25.222 -20.897 1.00 38.57 ?  7   SER   B HB3  1 
ATOM   4139 H  HG   . SER   B 1 7   ? 47.768 -25.645 -23.049 1.00 40.52 ?  7   SER   B HG   1 
ATOM   4140 N  N    . GLY   B 1 8   ? 44.994 -27.402 -20.730 1.00 27.08 ?  8   GLY   B N    1 
ATOM   4141 C  CA   . GLY   B 1 8   ? 44.949 -28.794 -20.343 1.00 26.19 ?  8   GLY   B CA   1 
ATOM   4142 C  C    . GLY   B 1 8   ? 44.007 -29.115 -19.212 1.00 24.78 ?  8   GLY   B C    1 
ATOM   4143 O  O    . GLY   B 1 8   ? 44.146 -30.178 -18.592 1.00 25.89 ?  8   GLY   B O    1 
ATOM   4144 H  H    . GLY   B 1 8   ? 44.523 -27.209 -21.420 1.00 32.50 ?  8   GLY   B H    1 
ATOM   4145 H  HA2  . GLY   B 1 8   ? 44.680 -29.321 -21.109 1.00 31.43 ?  8   GLY   B HA2  1 
ATOM   4146 H  HA3  . GLY   B 1 8   ? 45.835 -29.076 -20.076 1.00 31.43 ?  8   GLY   B HA3  1 
ATOM   4147 N  N    . TYR   B 1 9   ? 43.034 -28.252 -18.931 1.00 23.07 ?  9   TYR   B N    1 
ATOM   4148 C  CA   . TYR   B 1 9   ? 42.083 -28.526 -17.868 1.00 21.08 ?  9   TYR   B CA   1 
ATOM   4149 C  C    . TYR   B 1 9   ? 40.904 -29.323 -18.387 1.00 20.56 ?  9   TYR   B C    1 
ATOM   4150 O  O    . TYR   B 1 9   ? 40.495 -29.197 -19.545 1.00 22.22 ?  9   TYR   B O    1 
ATOM   4151 C  CB   . TYR   B 1 9   ? 41.572 -27.241 -17.224 1.00 20.36 ?  9   TYR   B CB   1 
ATOM   4152 C  CG   . TYR   B 1 9   ? 42.600 -26.613 -16.317 1.00 19.49 ?  9   TYR   B CG   1 
ATOM   4153 C  CD1  . TYR   B 1 9   ? 43.698 -25.946 -16.843 1.00 19.80 ?  9   TYR   B CD1  1 
ATOM   4154 C  CD2  . TYR   B 1 9   ? 42.489 -26.705 -14.938 1.00 18.87 ?  9   TYR   B CD2  1 
ATOM   4155 C  CE1  . TYR   B 1 9   ? 44.653 -25.387 -16.022 1.00 19.98 ?  9   TYR   B CE1  1 
ATOM   4156 C  CE2  . TYR   B 1 9   ? 43.440 -26.143 -14.107 1.00 19.01 ?  9   TYR   B CE2  1 
ATOM   4157 C  CZ   . TYR   B 1 9   ? 44.520 -25.480 -14.656 1.00 19.64 ?  9   TYR   B CZ   1 
ATOM   4158 O  OH   . TYR   B 1 9   ? 45.471 -24.927 -13.835 1.00 20.34 ?  9   TYR   B OH   1 
ATOM   4159 H  H    . TYR   B 1 9   ? 42.885 -27.518 -19.356 1.00 27.68 ?  9   TYR   B H    1 
ATOM   4160 H  HA   . TYR   B 1 9   ? 42.512 -29.052 -17.183 1.00 25.30 ?  9   TYR   B HA   1 
ATOM   4161 H  HB2  . TYR   B 1 9   ? 41.337 -26.598 -17.913 1.00 24.44 ?  9   TYR   B HB2  1 
ATOM   4162 H  HB3  . TYR   B 1 9   ? 40.794 -27.458 -16.689 1.00 24.44 ?  9   TYR   B HB3  1 
ATOM   4163 H  HD1  . TYR   B 1 9   ? 43.789 -25.884 -17.767 1.00 23.76 ?  9   TYR   B HD1  1 
ATOM   4164 H  HD2  . TYR   B 1 9   ? 41.755 -27.156 -14.568 1.00 22.65 ?  9   TYR   B HD2  1 
ATOM   4165 H  HE1  . TYR   B 1 9   ? 45.375 -24.946 -16.390 1.00 23.98 ?  9   TYR   B HE1  1 
ATOM   4166 H  HE2  . TYR   B 1 9   ? 43.340 -26.218 -13.184 1.00 22.82 ?  9   TYR   B HE2  1 
ATOM   4167 H  HH   . TYR   B 1 9   ? 46.059 -24.566 -14.300 1.00 24.41 ?  9   TYR   B HH   1 
ATOM   4168 N  N    . LEU   B 1 10  ? 40.366 -30.155 -17.507 1.00 18.87 ?  10  LEU   B N    1 
ATOM   4169 C  CA   . LEU   B 1 10  ? 39.164 -30.920 -17.772 1.00 18.59 ?  10  LEU   B CA   1 
ATOM   4170 C  C    . LEU   B 1 10  ? 37.980 -30.149 -17.212 1.00 18.12 ?  10  LEU   B C    1 
ATOM   4171 O  O    . LEU   B 1 10  ? 38.004 -29.723 -16.052 1.00 17.60 ?  10  LEU   B O    1 
ATOM   4172 C  CB   . LEU   B 1 10  ? 39.272 -32.284 -17.093 1.00 19.39 ?  10  LEU   B CB   1 
ATOM   4173 C  CG   . LEU   B 1 10  ? 38.135 -33.245 -17.418 1.00 20.98 ?  10  LEU   B CG   1 
ATOM   4174 C  CD1  . LEU   B 1 10  ? 38.250 -33.742 -18.854 1.00 22.04 ?  10  LEU   B CD1  1 
ATOM   4175 C  CD2  . LEU   B 1 10  ? 38.108 -34.404 -16.439 1.00 22.15 ?  10  LEU   B CD2  1 
ATOM   4176 H  H    . LEU   B 1 10  ? 40.685 -30.296 -16.714 1.00 22.65 ?  10  LEU   B H    1 
ATOM   4177 H  HA   . LEU   B 1 10  ? 39.042 -31.044 -18.724 1.00 22.31 ?  10  LEU   B HA   1 
ATOM   4178 H  HB2  . LEU   B 1 10  ? 40.102 -32.704 -17.374 1.00 23.27 ?  10  LEU   B HB2  1 
ATOM   4179 H  HB3  . LEU   B 1 10  ? 39.283 -32.156 -16.131 1.00 23.27 ?  10  LEU   B HB3  1 
ATOM   4180 H  HG   . LEU   B 1 10  ? 37.292 -32.774 -17.336 1.00 25.18 ?  10  LEU   B HG   1 
ATOM   4181 H  HD11 . LEU   B 1 10  ? 37.564 -34.407 -19.012 1.00 26.45 ?  10  LEU   B HD11 1 
ATOM   4182 H  HD12 . LEU   B 1 10  ? 38.125 -32.989 -19.456 1.00 26.45 ?  10  LEU   B HD12 1 
ATOM   4183 H  HD13 . LEU   B 1 10  ? 39.128 -34.129 -18.984 1.00 26.45 ?  10  LEU   B HD13 1 
ATOM   4184 H  HD21 . LEU   B 1 10  ? 37.378 -34.996 -16.675 1.00 26.59 ?  10  LEU   B HD21 1 
ATOM   4185 H  HD22 . LEU   B 1 10  ? 38.951 -34.877 -16.489 1.00 26.59 ?  10  LEU   B HD22 1 
ATOM   4186 H  HD23 . LEU   B 1 10  ? 37.975 -34.052 -15.545 1.00 26.59 ?  10  LEU   B HD23 1 
ATOM   4187 N  N    . LYS   B 1 11  ? 36.954 -29.967 -18.036 1.00 19.17 ?  11  LYS   B N    1 
ATOM   4188 C  CA   . LYS   B 1 11  ? 35.757 -29.250 -17.626 1.00 21.28 ?  11  LYS   B CA   1 
ATOM   4189 C  C    . LYS   B 1 11  ? 34.881 -30.174 -16.787 1.00 20.35 ?  11  LYS   B C    1 
ATOM   4190 O  O    . LYS   B 1 11  ? 34.505 -31.262 -17.239 1.00 21.93 ?  11  LYS   B O    1 
ATOM   4191 C  CB   . LYS   B 1 11  ? 35.011 -28.781 -18.876 1.00 25.15 ?  11  LYS   B CB   1 
ATOM   4192 C  CG   . LYS   B 1 11  ? 33.870 -27.810 -18.631 1.00 28.53 ?  11  LYS   B CG   1 
ATOM   4193 C  CD   . LYS   B 1 11  ? 33.153 -27.495 -19.940 1.00 31.27 ?  11  LYS   B CD   1 
ATOM   4194 C  CE   . LYS   B 1 11  ? 32.135 -26.380 -19.776 1.00 33.28 ?  11  LYS   B CE   1 
ATOM   4195 N  NZ   . LYS   B 1 11  ? 32.789 -25.062 -19.559 1.00 34.42 ?  11  LYS   B NZ   1 
ATOM   4196 H  H    . LYS   B 1 11  ? 36.923 -30.257 -18.846 1.00 23.00 ?  11  LYS   B H    1 
ATOM   4197 H  HA   . LYS   B 1 11  ? 35.999 -28.474 -17.097 1.00 25.54 ?  11  LYS   B HA   1 
ATOM   4198 H  HB2  . LYS   B 1 11  ? 35.644 -28.337 -19.465 1.00 30.19 ?  11  LYS   B HB2  1 
ATOM   4199 H  HB3  . LYS   B 1 11  ? 34.641 -29.555 -19.325 1.00 30.19 ?  11  LYS   B HB3  1 
ATOM   4200 H  HG2  . LYS   B 1 11  ? 33.231 -28.209 -18.021 1.00 34.25 ?  11  LYS   B HG2  1 
ATOM   4201 H  HG3  . LYS   B 1 11  ? 34.219 -26.983 -18.267 1.00 34.25 ?  11  LYS   B HG3  1 
ATOM   4202 H  HD2  . LYS   B 1 11  ? 33.806 -27.214 -20.601 1.00 37.53 ?  11  LYS   B HD2  1 
ATOM   4203 H  HD3  . LYS   B 1 11  ? 32.688 -28.289 -20.248 1.00 37.53 ?  11  LYS   B HD3  1 
ATOM   4204 H  HE2  . LYS   B 1 11  ? 31.592 -26.323 -20.578 1.00 39.94 ?  11  LYS   B HE2  1 
ATOM   4205 H  HE3  . LYS   B 1 11  ? 31.575 -26.574 -19.008 1.00 39.94 ?  11  LYS   B HE3  1 
ATOM   4206 H  HZ1  . LYS   B 1 11  ? 32.172 -24.427 -19.474 1.00 41.31 ?  11  LYS   B HZ1  1 
ATOM   4207 H  HZ2  . LYS   B 1 11  ? 33.285 -25.086 -18.821 1.00 41.31 ?  11  LYS   B HZ2  1 
ATOM   4208 H  HZ3  . LYS   B 1 11  ? 33.312 -24.865 -20.253 1.00 41.31 ?  11  LYS   B HZ3  1 
ATOM   4209 N  N    . LEU   B 1 12  ? 34.555 -29.747 -15.567 1.00 18.69 ?  12  LEU   B N    1 
ATOM   4210 C  CA   . LEU   B 1 12  ? 33.600 -30.455 -14.722 1.00 18.07 ?  12  LEU   B CA   1 
ATOM   4211 C  C    . LEU   B 1 12  ? 32.210 -29.847 -14.813 1.00 17.83 ?  12  LEU   B C    1 
ATOM   4212 O  O    . LEU   B 1 12  ? 31.225 -30.564 -14.994 1.00 18.09 ?  12  LEU   B O    1 
ATOM   4213 C  CB   . LEU   B 1 12  ? 34.066 -30.463 -13.262 1.00 17.41 ?  12  LEU   B CB   1 
ATOM   4214 C  CG   . LEU   B 1 12  ? 35.409 -31.140 -12.994 1.00 17.38 ?  12  LEU   B CG   1 
ATOM   4215 C  CD1  . LEU   B 1 12  ? 35.757 -31.086 -11.515 1.00 17.57 ?  12  LEU   B CD1  1 
ATOM   4216 C  CD2  . LEU   B 1 12  ? 35.409 -32.577 -13.501 1.00 17.82 ?  12  LEU   B CD2  1 
ATOM   4217 H  H    . LEU   B 1 12  ? 34.871 -29.033 -15.205 1.00 22.44 ?  12  LEU   B H    1 
ATOM   4218 H  HA   . LEU   B 1 12  ? 33.529 -31.371 -15.024 1.00 21.69 ?  12  LEU   B HA   1 
ATOM   4219 H  HB2  . LEU   B 1 12  ? 34.132 -29.546 -12.958 1.00 20.89 ?  12  LEU   B HB2  1 
ATOM   4220 H  HB3  . LEU   B 1 12  ? 33.394 -30.928 -12.733 1.00 20.89 ?  12  LEU   B HB3  1 
ATOM   4221 H  HG   . LEU   B 1 12  ? 36.096 -30.656 -13.476 1.00 20.86 ?  12  LEU   B HG   1 
ATOM   4222 H  HD11 . LEU   B 1 12  ? 36.618 -31.518 -11.378 1.00 21.09 ?  12  LEU   B HD11 1 
ATOM   4223 H  HD12 . LEU   B 1 12  ? 35.809 -30.159 -11.233 1.00 21.09 ?  12  LEU   B HD12 1 
ATOM   4224 H  HD13 . LEU   B 1 12  ? 35.073 -31.549 -11.008 1.00 21.09 ?  12  LEU   B HD13 1 
ATOM   4225 H  HD21 . LEU   B 1 12  ? 36.211 -33.020 -13.187 1.00 21.39 ?  12  LEU   B HD21 1 
ATOM   4226 H  HD22 . LEU   B 1 12  ? 34.622 -33.030 -13.160 1.00 21.39 ?  12  LEU   B HD22 1 
ATOM   4227 H  HD23 . LEU   B 1 12  ? 35.392 -32.568 -14.471 1.00 21.39 ?  12  LEU   B HD23 1 
ATOM   4228 N  N    . THR   B 1 13  ? 32.121 -28.531 -14.690 1.00 17.74 ?  13  THR   B N    1 
ATOM   4229 C  CA   . THR   B 1 13  ? 30.899 -27.778 -14.894 1.00 17.64 ?  13  THR   B CA   1 
ATOM   4230 C  C    . THR   B 1 13  ? 31.234 -26.590 -15.784 1.00 19.34 ?  13  THR   B C    1 
ATOM   4231 O  O    . THR   B 1 13  ? 32.382 -26.398 -16.203 1.00 20.48 ?  13  THR   B O    1 
ATOM   4232 C  CB   . THR   B 1 13  ? 30.303 -27.296 -13.565 1.00 17.20 ?  13  THR   B CB   1 
ATOM   4233 O  OG1  . THR   B 1 13  ? 31.151 -26.275 -13.022 1.00 16.99 ?  13  THR   B OG1  1 
ATOM   4234 C  CG2  . THR   B 1 13  ? 30.171 -28.450 -12.570 1.00 17.54 ?  13  THR   B CG2  1 
ATOM   4235 H  H    . THR   B 1 13  ? 32.788 -28.030 -14.481 1.00 21.29 ?  13  THR   B H    1 
ATOM   4236 H  HA   . THR   B 1 13  ? 30.240 -28.332 -15.341 1.00 21.17 ?  13  THR   B HA   1 
ATOM   4237 H  HB   . THR   B 1 13  ? 29.413 -26.926 -13.722 1.00 20.65 ?  13  THR   B HB   1 
ATOM   4238 H  HG1  . THR   B 1 13  ? 30.895 -25.514 -13.289 1.00 20.39 ?  13  THR   B HG1  1 
ATOM   4239 H  HG21 . THR   B 1 13  ? 29.670 -28.162 -11.790 1.00 21.05 ?  13  THR   B HG21 1 
ATOM   4240 H  HG22 . THR   B 1 13  ? 29.707 -29.193 -12.985 1.00 21.05 ?  13  THR   B HG22 1 
ATOM   4241 H  HG23 . THR   B 1 13  ? 31.051 -28.744 -12.288 1.00 21.05 ?  13  THR   B HG23 1 
ATOM   4242 N  N    . ASP   B 1 14  ? 30.225 -25.766 -16.057 1.00 20.27 ?  14  ASP   B N    1 
ATOM   4243 C  CA   . ASP   B 1 14  ? 30.446 -24.607 -16.911 1.00 21.82 ?  14  ASP   B CA   1 
ATOM   4244 C  C    . ASP   B 1 14  ? 31.506 -23.664 -16.360 1.00 20.12 ?  14  ASP   B C    1 
ATOM   4245 O  O    . ASP   B 1 14  ? 32.098 -22.906 -17.136 1.00 21.85 ?  14  ASP   B O    1 
ATOM   4246 C  CB   . ASP   B 1 14  ? 29.142 -23.842 -17.123 1.00 25.60 ?  14  ASP   B CB   1 
ATOM   4247 C  CG   . ASP   B 1 14  ? 28.208 -24.543 -18.080 1.00 29.44 ?  14  ASP   B CG   1 
ATOM   4248 O  OD1  . ASP   B 1 14  ? 28.677 -25.377 -18.886 1.00 30.82 ?  14  ASP   B OD1  1 
ATOM   4249 O  OD2  . ASP   B 1 14  ? 26.995 -24.261 -18.023 1.00 30.90 -1 14  ASP   B OD2  1 
ATOM   4250 H  H    . ASP   B 1 14  ? 29.421 -25.845 -15.755 1.00 24.33 ?  14  ASP   B H    1 
ATOM   4251 H  HA   . ASP   B 1 14  ? 30.751 -24.911 -17.774 1.00 26.19 ?  14  ASP   B HA   1 
ATOM   4252 H  HB2  . ASP   B 1 14  ? 28.672 -23.762 -16.281 1.00 30.73 ?  14  ASP   B HB2  1 
ATOM   4253 H  HB3  . ASP   B 1 14  ? 29.343 -22.959 -17.478 1.00 30.73 ?  14  ASP   B HB3  1 
ATOM   4254 N  N    . ASN   B 1 15  ? 31.756 -23.681 -15.047 1.00 17.52 ?  15  ASN   B N    1 
ATOM   4255 C  CA   . ASN   B 1 15  ? 32.715 -22.758 -14.451 1.00 15.65 ?  15  ASN   B CA   1 
ATOM   4256 C  C    . ASN   B 1 15  ? 33.810 -23.414 -13.620 1.00 14.40 ?  15  ASN   B C    1 
ATOM   4257 O  O    . ASN   B 1 15  ? 34.660 -22.688 -13.093 1.00 14.39 ?  15  ASN   B O    1 
ATOM   4258 C  CB   . ASN   B 1 15  ? 32.001 -21.707 -13.584 1.00 15.77 ?  15  ASN   B CB   1 
ATOM   4259 C  CG   . ASN   B 1 15  ? 31.384 -22.310 -12.340 1.00 15.56 ?  15  ASN   B CG   1 
ATOM   4260 O  OD1  . ASN   B 1 15  ? 30.439 -23.101 -12.426 1.00 17.17 ?  15  ASN   B OD1  1 
ATOM   4261 N  ND2  . ASN   B 1 15  ? 31.911 -21.958 -11.181 1.00 14.64 ?  15  ASN   B ND2  1 
ATOM   4262 H  H    . ASN   B 1 15  ? 31.365 -24.201 -14.482 1.00 21.03 ?  15  ASN   B H    1 
ATOM   4263 H  HA   . ASN   B 1 15  ? 33.153 -22.273 -15.160 1.00 18.78 ?  15  ASN   B HA   1 
ATOM   4264 H  HB2  . ASN   B 1 15  ? 32.646 -21.028 -13.305 1.00 18.93 ?  15  ASN   B HB2  1 
ATOM   4265 H  HB3  . ASN   B 1 15  ? 31.293 -21.284 -14.099 1.00 18.93 ?  15  ASN   B HB3  1 
ATOM   4266 H  HD21 . ASN   B 1 15  ? 31.594 -22.270 -10.445 1.00 17.58 ?  15  ASN   B HD21 1 
ATOM   4267 H  HD22 . ASN   B 1 15  ? 32.579 -21.406 -11.153 1.00 17.58 ?  15  ASN   B HD22 1 
ATOM   4268 N  N    . VAL   B 1 16  ? 33.820 -24.738 -13.472 1.00 14.40 ?  16  VAL   B N    1 
ATOM   4269 C  CA   . VAL   B 1 16  ? 34.823 -25.425 -12.664 1.00 14.10 ?  16  VAL   B CA   1 
ATOM   4270 C  C    . VAL   B 1 16  ? 35.617 -26.364 -13.555 1.00 14.29 ?  16  VAL   B C    1 
ATOM   4271 O  O    . VAL   B 1 16  ? 35.042 -27.250 -14.206 1.00 15.24 ?  16  VAL   B O    1 
ATOM   4272 C  CB   . VAL   B 1 16  ? 34.200 -26.190 -11.484 1.00 14.36 ?  16  VAL   B CB   1 
ATOM   4273 C  CG1  . VAL   B 1 16  ? 35.288 -26.915 -10.693 1.00 14.45 ?  16  VAL   B CG1  1 
ATOM   4274 C  CG2  . VAL   B 1 16  ? 33.401 -25.241 -10.591 1.00 15.15 ?  16  VAL   B CG2  1 
ATOM   4275 H  H    . VAL   B 1 16  ? 33.237 -25.268 -13.831 1.00 17.29 ?  16  VAL   B H    1 
ATOM   4276 H  HA   . VAL   B 1 16  ? 35.431 -24.766 -12.297 1.00 16.93 ?  16  VAL   B HA   1 
ATOM   4277 H  HB   . VAL   B 1 16  ? 33.588 -26.859 -11.830 1.00 17.24 ?  16  VAL   B HB   1 
ATOM   4278 H  HG11 . VAL   B 1 16  ? 34.918 -27.207 -9.845  1.00 17.34 ?  16  VAL   B HG11 1 
ATOM   4279 H  HG12 . VAL   B 1 16  ? 35.596 -27.679 -11.200 1.00 17.34 ?  16  VAL   B HG12 1 
ATOM   4280 H  HG13 . VAL   B 1 16  ? 36.023 -26.300 -10.536 1.00 17.34 ?  16  VAL   B HG13 1 
ATOM   4281 H  HG21 . VAL   B 1 16  ? 33.069 -25.734 -9.823  1.00 18.19 ?  16  VAL   B HG21 1 
ATOM   4282 H  HG22 . VAL   B 1 16  ? 33.976 -24.520 -10.299 1.00 18.19 ?  16  VAL   B HG22 1 
ATOM   4283 H  HG23 . VAL   B 1 16  ? 32.653 -24.885 -11.099 1.00 18.19 ?  16  VAL   B HG23 1 
ATOM   4284 N  N    . TYR   B 1 17  ? 36.940 -26.197 -13.530 1.00 14.77 ?  17  TYR   B N    1 
ATOM   4285 C  CA   . TYR   B 1 17  ? 37.885 -26.948 -14.340 1.00 14.91 ?  17  TYR   B CA   1 
ATOM   4286 C  C    . TYR   B 1 17  ? 38.936 -27.557 -13.423 1.00 13.87 ?  17  TYR   B C    1 
ATOM   4287 O  O    . TYR   B 1 17  ? 39.215 -27.023 -12.346 1.00 14.26 ?  17  TYR   B O    1 
ATOM   4288 C  CB   . TYR   B 1 17  ? 38.588 -26.023 -15.340 1.00 17.64 ?  17  TYR   B CB   1 
ATOM   4289 C  CG   . TYR   B 1 17  ? 37.660 -25.255 -16.251 1.00 20.78 ?  17  TYR   B CG   1 
ATOM   4290 C  CD1  . TYR   B 1 17  ? 37.082 -24.059 -15.846 1.00 22.16 ?  17  TYR   B CD1  1 
ATOM   4291 C  CD2  . TYR   B 1 17  ? 37.365 -25.727 -17.522 1.00 22.55 ?  17  TYR   B CD2  1 
ATOM   4292 C  CE1  . TYR   B 1 17  ? 36.233 -23.353 -16.682 1.00 23.72 ?  17  TYR   B CE1  1 
ATOM   4293 C  CE2  . TYR   B 1 17  ? 36.521 -25.029 -18.366 1.00 23.97 ?  17  TYR   B CE2  1 
ATOM   4294 C  CZ   . TYR   B 1 17  ? 35.956 -23.845 -17.939 1.00 24.62 ?  17  TYR   B CZ   1 
ATOM   4295 O  OH   . TYR   B 1 17  ? 35.116 -23.149 -18.776 1.00 25.76 ?  17  TYR   B OH   1 
ATOM   4296 H  H    . TYR   B 1 17  ? 37.329 -25.619 -13.021 1.00 17.72 ?  17  TYR   B H    1 
ATOM   4297 H  HA   . TYR   B 1 17  ? 37.421 -27.655 -14.825 1.00 17.90 ?  17  TYR   B HA   1 
ATOM   4298 H  HB2  . TYR   B 1 17  ? 39.123 -25.381 -14.848 1.00 21.17 ?  17  TYR   B HB2  1 
ATOM   4299 H  HB3  . TYR   B 1 17  ? 39.157 -26.563 -15.903 1.00 21.17 ?  17  TYR   B HB3  1 
ATOM   4300 H  HD1  . TYR   B 1 17  ? 37.267 -23.726 -14.998 1.00 26.60 ?  17  TYR   B HD1  1 
ATOM   4301 H  HD2  . TYR   B 1 17  ? 37.741 -26.526 -17.813 1.00 27.06 ?  17  TYR   B HD2  1 
ATOM   4302 H  HE1  . TYR   B 1 17  ? 35.852 -22.553 -16.398 1.00 28.47 ?  17  TYR   B HE1  1 
ATOM   4303 H  HE2  . TYR   B 1 17  ? 36.329 -25.360 -19.215 1.00 28.77 ?  17  TYR   B HE2  1 
ATOM   4304 H  HH   . TYR   B 1 17  ? 35.031 -23.555 -19.505 1.00 30.92 ?  17  TYR   B HH   1 
ATOM   4305 N  N    . ILE   B 1 18  ? 39.546 -28.662 -13.855 1.00 14.26 ?  18  ILE   B N    1 
ATOM   4306 C  CA   . ILE   B 1 18  ? 40.473 -29.387 -12.994 1.00 14.22 ?  18  ILE   B CA   1 
ATOM   4307 C  C    . ILE   B 1 18  ? 41.630 -29.940 -13.815 1.00 14.62 ?  18  ILE   B C    1 
ATOM   4308 O  O    . ILE   B 1 18  ? 41.468 -30.326 -14.977 1.00 16.06 ?  18  ILE   B O    1 
ATOM   4309 C  CB   . ILE   B 1 18  ? 39.723 -30.487 -12.196 1.00 14.82 ?  18  ILE   B CB   1 
ATOM   4310 C  CG1  . ILE   B 1 18  ? 40.577 -31.031 -11.046 1.00 14.93 ?  18  ILE   B CG1  1 
ATOM   4311 C  CG2  . ILE   B 1 18  ? 39.227 -31.602 -13.127 1.00 15.16 ?  18  ILE   B CG2  1 
ATOM   4312 C  CD1  . ILE   B 1 18  ? 39.770 -31.839 -10.040 1.00 16.33 ?  18  ILE   B CD1  1 
ATOM   4313 H  H    . ILE   B 1 18  ? 39.431 -29.013 -14.630 1.00 17.12 ?  18  ILE   B H    1 
ATOM   4314 H  HA   . ILE   B 1 18  ? 40.834 -28.771 -12.341 1.00 17.07 ?  18  ILE   B HA   1 
ATOM   4315 H  HB   . ILE   B 1 18  ? 38.934 -30.085 -11.798 1.00 17.79 ?  18  ILE   B HB   1 
ATOM   4316 H  HG12 . ILE   B 1 18  ? 41.268 -31.602 -11.405 1.00 17.92 ?  18  ILE   B HG12 1 
ATOM   4317 H  HG13 . ILE   B 1 18  ? 40.973 -30.281 -10.572 1.00 17.92 ?  18  ILE   B HG13 1 
ATOM   4318 H  HG21 . ILE   B 1 18  ? 38.633 -32.189 -12.631 1.00 18.19 ?  18  ILE   B HG21 1 
ATOM   4319 H  HG22 . ILE   B 1 18  ? 38.747 -31.198 -13.866 1.00 18.19 ?  18  ILE   B HG22 1 
ATOM   4320 H  HG23 . ILE   B 1 18  ? 39.987 -32.101 -13.456 1.00 18.19 ?  18  ILE   B HG23 1 
ATOM   4321 H  HD11 . ILE   B 1 18  ? 40.354 -32.118 -9.316  1.00 19.61 ?  18  ILE   B HD11 1 
ATOM   4322 H  HD12 . ILE   B 1 18  ? 39.051 -31.289 -9.690  1.00 19.61 ?  18  ILE   B HD12 1 
ATOM   4323 H  HD13 . ILE   B 1 18  ? 39.401 -32.620 -10.484 1.00 19.61 ?  18  ILE   B HD13 1 
ATOM   4324 N  N    . LYS   B 1 19  ? 42.808 -29.982 -13.192 1.00 15.03 ?  19  LYS   B N    1 
ATOM   4325 C  CA   . LYS   B 1 19  ? 44.019 -30.448 -13.849 1.00 15.95 ?  19  LYS   B CA   1 
ATOM   4326 C  C    . LYS   B 1 19  ? 44.919 -31.130 -12.829 1.00 15.78 ?  19  LYS   B C    1 
ATOM   4327 O  O    . LYS   B 1 19  ? 45.002 -30.700 -11.676 1.00 15.11 ?  19  LYS   B O    1 
ATOM   4328 C  CB   . LYS   B 1 19  ? 44.783 -29.278 -14.481 1.00 17.21 ?  19  LYS   B CB   1 
ATOM   4329 C  CG   . LYS   B 1 19  ? 45.974 -29.686 -15.325 1.00 19.12 ?  19  LYS   B CG   1 
ATOM   4330 C  CD   . LYS   B 1 19  ? 46.707 -28.458 -15.848 1.00 20.75 ?  19  LYS   B CD   1 
ATOM   4331 C  CE   . LYS   B 1 19  ? 47.860 -28.835 -16.757 1.00 22.56 ?  19  LYS   B CE   1 
ATOM   4332 N  NZ   . LYS   B 1 19  ? 48.599 -27.637 -17.236 1.00 23.59 ?  19  LYS   B NZ   1 
ATOM   4333 H  H    . LYS   B 1 19  ? 42.919 -29.736 -12.371 1.00 18.04 ?  19  LYS   B H    1 
ATOM   4334 H  HA   . LYS   B 1 19  ? 43.783 -31.084 -14.539 1.00 19.14 ?  19  LYS   B HA   1 
ATOM   4335 H  HB2  . LYS   B 1 19  ? 44.170 -28.788 -15.051 1.00 20.66 ?  19  LYS   B HB2  1 
ATOM   4336 H  HB3  . LYS   B 1 19  ? 45.100 -28.697 -13.768 1.00 20.66 ?  19  LYS   B HB3  1 
ATOM   4337 H  HG2  . LYS   B 1 19  ? 46.583 -30.207 -14.783 1.00 22.95 ?  19  LYS   B HG2  1 
ATOM   4338 H  HG3  . LYS   B 1 19  ? 45.658 -30.208 -16.080 1.00 22.95 ?  19  LYS   B HG3  1 
ATOM   4339 H  HD2  . LYS   B 1 19  ? 46.085 -27.908 -16.352 1.00 24.91 ?  19  LYS   B HD2  1 
ATOM   4340 H  HD3  . LYS   B 1 19  ? 47.061 -27.957 -15.095 1.00 24.91 ?  19  LYS   B HD3  1 
ATOM   4341 H  HE2  . LYS   B 1 19  ? 48.477 -29.402 -16.268 1.00 27.07 ?  19  LYS   B HE2  1 
ATOM   4342 H  HE3  . LYS   B 1 19  ? 47.511 -29.311 -17.529 1.00 27.07 ?  19  LYS   B HE3  1 
ATOM   4343 H  HZ1  . LYS   B 1 19  ? 49.251 -27.884 -17.790 1.00 28.31 ?  19  LYS   B HZ1  1 
ATOM   4344 H  HZ2  . LYS   B 1 19  ? 48.045 -27.090 -17.668 1.00 28.31 ?  19  LYS   B HZ2  1 
ATOM   4345 H  HZ3  . LYS   B 1 19  ? 48.955 -27.203 -16.547 1.00 28.31 ?  19  LYS   B HZ3  1 
ATOM   4346 N  N    . ASN   B 1 20  ? 45.599 -32.186 -13.263 1.00 16.81 ?  20  ASN   B N    1 
ATOM   4347 C  CA   . ASN   B 1 20  ? 46.628 -32.821 -12.447 1.00 17.91 ?  20  ASN   B CA   1 
ATOM   4348 C  C    . ASN   B 1 20  ? 47.900 -32.000 -12.633 1.00 18.29 ?  20  ASN   B C    1 
ATOM   4349 O  O    . ASN   B 1 20  ? 48.546 -32.067 -13.682 1.00 19.92 ?  20  ASN   B O    1 
ATOM   4350 C  CB   . ASN   B 1 20  ? 46.802 -34.274 -12.885 1.00 19.53 ?  20  ASN   B CB   1 
ATOM   4351 C  CG   . ASN   B 1 20  ? 47.967 -34.974 -12.204 1.00 20.82 ?  20  ASN   B CG   1 
ATOM   4352 O  OD1  . ASN   B 1 20  ? 48.624 -35.823 -12.811 1.00 23.04 ?  20  ASN   B OD1  1 
ATOM   4353 N  ND2  . ASN   B 1 20  ? 48.219 -34.645 -10.946 1.00 20.52 ?  20  ASN   B ND2  1 
ATOM   4354 H  H    . ASN   B 1 20  ? 45.481 -32.555 -14.030 1.00 20.17 ?  20  ASN   B H    1 
ATOM   4355 H  HA   . ASN   B 1 20  ? 46.359 -32.804 -11.514 1.00 21.49 ?  20  ASN   B HA   1 
ATOM   4356 H  HB2  . ASN   B 1 20  ? 45.990 -34.766 -12.673 1.00 23.44 ?  20  ASN   B HB2  1 
ATOM   4357 H  HB3  . ASN   B 1 20  ? 46.957 -34.296 -13.841 1.00 23.44 ?  20  ASN   B HB3  1 
ATOM   4358 H  HD21 . ASN   B 1 20  ? 48.872 -35.015 -10.527 1.00 24.62 ?  20  ASN   B HD21 1 
ATOM   4359 H  HD22 . ASN   B 1 20  ? 47.742 -34.046 -10.547 1.00 24.62 ?  20  ASN   B HD22 1 
ATOM   4360 N  N    . ALA   B 1 21  ? 48.256 -31.198 -11.628 1.00 17.92 ?  21  ALA   B N    1 
ATOM   4361 C  CA   . ALA   B 1 21  ? 49.372 -30.276 -11.781 1.00 18.72 ?  21  ALA   B CA   1 
ATOM   4362 C  C    . ALA   B 1 21  ? 49.834 -29.779 -10.420 1.00 17.55 ?  21  ALA   B C    1 
ATOM   4363 O  O    . ALA   B 1 21  ? 49.092 -29.806 -9.434  1.00 17.15 ?  21  ALA   B O    1 
ATOM   4364 C  CB   . ALA   B 1 21  ? 48.986 -29.094 -12.670 1.00 20.04 ?  21  ALA   B CB   1 
ATOM   4365 H  H    . ALA   B 1 21  ? 47.868 -31.176 -10.854 1.00 21.51 ?  21  ALA   B H    1 
ATOM   4366 H  HA   . ALA   B 1 21  ? 50.110 -30.748 -12.196 1.00 22.46 ?  21  ALA   B HA   1 
ATOM   4367 H  HB1  . ALA   B 1 21  ? 49.774 -28.554 -12.813 1.00 24.06 ?  21  ALA   B HB1  1 
ATOM   4368 H  HB2  . ALA   B 1 21  ? 48.656 -29.437 -13.512 1.00 24.06 ?  21  ALA   B HB2  1 
ATOM   4369 H  HB3  . ALA   B 1 21  ? 48.297 -28.580 -12.224 1.00 24.06 ?  21  ALA   B HB3  1 
ATOM   4370 N  N    . ASP   B 1 22  ? 51.090 -29.333 -10.399 1.00 16.56 ?  22  ASP   B N    1 
ATOM   4371 C  CA   . ASP   B 1 22  ? 51.700 -28.638 -9.270  1.00 15.87 ?  22  ASP   B CA   1 
ATOM   4372 C  C    . ASP   B 1 22  ? 51.295 -27.166 -9.351  1.00 14.33 ?  22  ASP   B C    1 
ATOM   4373 O  O    . ASP   B 1 22  ? 51.604 -26.495 -10.339 1.00 14.38 ?  22  ASP   B O    1 
ATOM   4374 C  CB   . ASP   B 1 22  ? 53.218 -28.810 -9.430  1.00 17.17 ?  22  ASP   B CB   1 
ATOM   4375 C  CG   . ASP   B 1 22  ? 54.048 -28.050 -8.403  1.00 18.76 ?  22  ASP   B CG   1 
ATOM   4376 O  OD1  . ASP   B 1 22  ? 53.684 -26.934 -7.998  1.00 18.69 ?  22  ASP   B OD1  1 
ATOM   4377 O  OD2  . ASP   B 1 22  ? 55.126 -28.566 -8.032  1.00 21.23 -1 22  ASP   B OD2  1 
ATOM   4378 H  H    . ASP   B 1 22  ? 51.634 -29.426 -11.062 1.00 19.88 ?  22  ASP   B H    1 
ATOM   4379 H  HA   . ASP   B 1 22  ? 51.414 -29.021 -8.426  1.00 19.05 ?  22  ASP   B HA   1 
ATOM   4380 H  HB2  . ASP   B 1 22  ? 53.444 -29.747 -9.353  1.00 20.61 ?  22  ASP   B HB2  1 
ATOM   4381 H  HB3  . ASP   B 1 22  ? 53.483 -28.475 -10.301 1.00 20.61 ?  22  ASP   B HB3  1 
ATOM   4382 N  N    . ILE   B 1 23  ? 50.585 -26.670 -8.330  1.00 13.58 ?  23  ILE   B N    1 
ATOM   4383 C  CA   . ILE   B 1 23  ? 49.995 -25.330 -8.405  1.00 12.80 ?  23  ILE   B CA   1 
ATOM   4384 C  C    . ILE   B 1 23  ? 51.053 -24.245 -8.541  1.00 12.61 ?  23  ILE   B C    1 
ATOM   4385 O  O    . ILE   B 1 23  ? 50.793 -23.202 -9.148  1.00 12.14 ?  23  ILE   B O    1 
ATOM   4386 C  CB   . ILE   B 1 23  ? 49.051 -25.084 -7.214  1.00 13.59 ?  23  ILE   B CB   1 
ATOM   4387 C  CG1  . ILE   B 1 23  ? 48.220 -23.818 -7.428  1.00 13.99 ?  23  ILE   B CG1  1 
ATOM   4388 C  CG2  . ILE   B 1 23  ? 49.811 -25.042 -5.902  1.00 14.54 ?  23  ILE   B CG2  1 
ATOM   4389 C  CD1  . ILE   B 1 23  ? 47.102 -23.656 -6.412  1.00 14.73 ?  23  ILE   B CD1  1 
ATOM   4390 H  H    . ILE   B 1 23  ? 50.431 -27.090 -7.596  1.00 16.30 ?  23  ILE   B H    1 
ATOM   4391 H  HA   . ILE   B 1 23  ? 49.452 -25.292 -9.207  1.00 15.36 ?  23  ILE   B HA   1 
ATOM   4392 H  HB   . ILE   B 1 23  ? 48.433 -25.832 -7.174  1.00 16.31 ?  23  ILE   B HB   1 
ATOM   4393 H  HG12 . ILE   B 1 23  ? 48.801 -23.043 -7.358  1.00 16.80 ?  23  ILE   B HG12 1 
ATOM   4394 H  HG13 . ILE   B 1 23  ? 47.819 -23.846 -8.314  1.00 16.80 ?  23  ILE   B HG13 1 
ATOM   4395 H  HG21 . ILE   B 1 23  ? 49.174 -25.045 -5.171  1.00 17.46 ?  23  ILE   B HG21 1 
ATOM   4396 H  HG22 . ILE   B 1 23  ? 50.383 -25.822 -5.848  1.00 17.46 ?  23  ILE   B HG22 1 
ATOM   4397 H  HG23 . ILE   B 1 23  ? 50.346 -24.234 -5.876  1.00 17.46 ?  23  ILE   B HG23 1 
ATOM   4398 H  HD11 . ILE   B 1 23  ? 46.560 -22.892 -6.657  1.00 17.68 ?  23  ILE   B HD11 1 
ATOM   4399 H  HD12 . ILE   B 1 23  ? 46.559 -24.462 -6.417  1.00 17.68 ?  23  ILE   B HD12 1 
ATOM   4400 H  HD13 . ILE   B 1 23  ? 47.490 -23.525 -5.535  1.00 17.68 ?  23  ILE   B HD13 1 
ATOM   4401 N  N    . VAL   B 1 24  ? 52.246 -24.452 -7.981  1.00 12.88 ?  24  VAL   B N    1 
ATOM   4402 C  CA   . VAL   B 1 24  ? 53.320 -23.473 -8.148  1.00 13.67 ?  24  VAL   B CA   1 
ATOM   4403 C  C    . VAL   B 1 24  ? 53.775 -23.425 -9.601  1.00 13.55 ?  24  VAL   B C    1 
ATOM   4404 O  O    . VAL   B 1 24  ? 53.922 -22.346 -10.191 1.00 14.06 ?  24  VAL   B O    1 
ATOM   4405 C  CB   . VAL   B 1 24  ? 54.497 -23.789 -7.205  1.00 14.60 ?  24  VAL   B CB   1 
ATOM   4406 C  CG1  . VAL   B 1 24  ? 55.701 -22.909 -7.531  1.00 15.28 ?  24  VAL   B CG1  1 
ATOM   4407 C  CG2  . VAL   B 1 24  ? 54.084 -23.603 -5.764  1.00 15.65 ?  24  VAL   B CG2  1 
ATOM   4408 H  H    . VAL   B 1 24  ? 52.457 -25.135 -7.506  1.00 15.46 ?  24  VAL   B H    1 
ATOM   4409 H  HA   . VAL   B 1 24  ? 52.990 -22.595 -7.914  1.00 16.41 ?  24  VAL   B HA   1 
ATOM   4410 H  HB   . VAL   B 1 24  ? 54.765 -24.717 -7.319  1.00 17.53 ?  24  VAL   B HB   1 
ATOM   4411 H  HG11 . VAL   B 1 24  ? 56.301 -22.902 -6.768  1.00 18.35 ?  24  VAL   B HG11 1 
ATOM   4412 H  HG12 . VAL   B 1 24  ? 56.155 -23.270 -8.305  1.00 18.35 ?  24  VAL   B HG12 1 
ATOM   4413 H  HG13 . VAL   B 1 24  ? 55.388 -22.009 -7.712  1.00 18.35 ?  24  VAL   B HG13 1 
ATOM   4414 H  HG21 . VAL   B 1 24  ? 54.816 -23.867 -5.186  1.00 18.78 ?  24  VAL   B HG21 1 
ATOM   4415 H  HG22 . VAL   B 1 24  ? 53.867 -22.669 -5.619  1.00 18.78 ?  24  VAL   B HG22 1 
ATOM   4416 H  HG23 . VAL   B 1 24  ? 53.306 -24.155 -5.586  1.00 18.78 ?  24  VAL   B HG23 1 
ATOM   4417 N  N    . GLU   B 1 25  ? 54.037 -24.595 -10.189 1.00 14.36 ?  25  GLU   B N    1 
ATOM   4418 C  CA   . GLU   B 1 25  ? 54.429 -24.634 -11.592 1.00 15.98 ?  25  GLU   B CA   1 
ATOM   4419 C  C    . GLU   B 1 25  ? 53.323 -24.090 -12.481 1.00 15.01 ?  25  GLU   B C    1 
ATOM   4420 O  O    . GLU   B 1 25  ? 53.591 -23.370 -13.452 1.00 15.77 ?  25  GLU   B O    1 
ATOM   4421 C  CB   . GLU   B 1 25  ? 54.811 -26.058 -11.989 1.00 20.00 ?  25  GLU   B CB   1 
ATOM   4422 C  CG   . GLU   B 1 25  ? 56.111 -26.514 -11.344 1.00 25.31 ?  25  GLU   B CG   1 
ATOM   4423 C  CD   . GLU   B 1 25  ? 57.227 -25.481 -11.444 1.00 30.24 ?  25  GLU   B CD   1 
ATOM   4424 O  OE1  . GLU   B 1 25  ? 57.617 -25.128 -12.578 1.00 32.13 ?  25  GLU   B OE1  1 
ATOM   4425 O  OE2  . GLU   B 1 25  ? 57.702 -25.004 -10.387 1.00 31.85 -1 25  GLU   B OE2  1 
ATOM   4426 H  H    . GLU   B 1 25  ? 53.995 -25.367 -9.801  1.00 17.24 ?  25  GLU   B H    1 
ATOM   4427 H  HA   . GLU   B 1 25  ? 55.192 -24.055 -11.715 1.00 19.18 ?  25  GLU   B HA   1 
ATOM   4428 H  HB2  . GLU   B 1 25  ? 54.108 -26.667 -11.706 1.00 24.01 ?  25  GLU   B HB2  1 
ATOM   4429 H  HB3  . GLU   B 1 25  ? 54.917 -26.100 -12.952 1.00 24.01 ?  25  GLU   B HB3  1 
ATOM   4430 H  HG2  . GLU   B 1 25  ? 55.956 -26.680 -10.407 1.00 30.37 ?  25  GLU   B HG2  1 
ATOM   4431 H  HG3  . GLU   B 1 25  ? 56.415 -27.318 -11.789 1.00 30.37 ?  25  GLU   B HG3  1 
ATOM   4432 N  N    . GLU   B 1 26  ? 52.071 -24.413 -12.153 1.00 14.19 ?  26  GLU   B N    1 
ATOM   4433 C  CA   . GLU   B 1 26  ? 50.942 -23.884 -12.909 1.00 14.66 ?  26  GLU   B CA   1 
ATOM   4434 C  C    . GLU   B 1 26  ? 50.903 -22.368 -12.832 1.00 13.74 ?  26  GLU   B C    1 
ATOM   4435 O  O    . GLU   B 1 26  ? 50.707 -21.692 -13.847 1.00 14.94 ?  26  GLU   B O    1 
ATOM   4436 C  CB   . GLU   B 1 26  ? 49.631 -24.459 -12.370 1.00 16.56 ?  26  GLU   B CB   1 
ATOM   4437 C  CG   . GLU   B 1 26  ? 49.153 -25.722 -13.056 1.00 20.38 ?  26  GLU   B CG   1 
ATOM   4438 C  CD   . GLU   B 1 26  ? 48.918 -25.564 -14.560 1.00 21.92 ?  26  GLU   B CD   1 
ATOM   4439 O  OE1  . GLU   B 1 26  ? 47.935 -24.921 -14.993 1.00 22.40 ?  26  GLU   B OE1  1 
ATOM   4440 O  OE2  . GLU   B 1 26  ? 49.725 -26.122 -15.313 1.00 23.76 -1 26  GLU   B OE2  1 
ATOM   4441 H  H    . GLU   B 1 26  ? 51.849 -24.942 -11.506 1.00 17.03 ?  26  GLU   B H    1 
ATOM   4442 H  HA   . GLU   B 1 26  ? 51.032 -24.140 -13.837 1.00 17.60 ?  26  GLU   B HA   1 
ATOM   4443 H  HB2  . GLU   B 1 26  ? 49.745 -24.664 -11.425 1.00 19.88 ?  26  GLU   B HB2  1 
ATOM   4444 H  HB3  . GLU   B 1 26  ? 48.935 -23.788 -12.469 1.00 19.88 ?  26  GLU   B HB3  1 
ATOM   4445 H  HG2  . GLU   B 1 26  ? 49.830 -26.398 -12.941 1.00 24.46 ?  26  GLU   B HG2  1 
ATOM   4446 H  HG3  . GLU   B 1 26  ? 48.320 -25.999 -12.646 1.00 24.46 ?  26  GLU   B HG3  1 
ATOM   4447 N  N    . ALA   B 1 27  ? 51.052 -21.816 -11.627 1.00 12.94 ?  27  ALA   B N    1 
ATOM   4448 C  CA   . ALA   B 1 27  ? 51.005 -20.366 -11.481 1.00 13.28 ?  27  ALA   B CA   1 
ATOM   4449 C  C    . ALA   B 1 27  ? 52.076 -19.700 -12.336 1.00 14.38 ?  27  ALA   B C    1 
ATOM   4450 O  O    . ALA   B 1 27  ? 51.814 -18.697 -13.015 1.00 15.04 ?  27  ALA   B O    1 
ATOM   4451 C  CB   . ALA   B 1 27  ? 51.155 -19.981 -10.009 1.00 13.58 ?  27  ALA   B CB   1 
ATOM   4452 H  H    . ALA   B 1 27  ? 51.170 -22.253 -10.890 1.00 15.53 ?  27  ALA   B H    1 
ATOM   4453 H  HA   . ALA   B 1 27  ? 50.143 -20.047 -11.781 1.00 15.94 ?  27  ALA   B HA   1 
ATOM   4454 H  HB1  . ALA   B 1 27  ? 51.117 -19.016 -9.928  1.00 16.30 ?  27  ALA   B HB1  1 
ATOM   4455 H  HB2  . ALA   B 1 27  ? 50.428 -20.382 -9.501  1.00 16.30 ?  27  ALA   B HB2  1 
ATOM   4456 H  HB3  . ALA   B 1 27  ? 52.005 -20.309 -9.678  1.00 16.30 ?  27  ALA   B HB3  1 
ATOM   4457 N  N    . LYS   B 1 28  ? 53.291 -20.250 -12.325 1.00 15.56 ?  28  LYS   B N    1 
ATOM   4458 C  CA   . LYS   B 1 28  ? 54.365 -19.638 -13.097 1.00 17.52 ?  28  LYS   B CA   1 
ATOM   4459 C  C    . LYS   B 1 28  ? 54.102 -19.720 -14.596 1.00 18.19 ?  28  LYS   B C    1 
ATOM   4460 O  O    . LYS   B 1 28  ? 54.496 -18.814 -15.343 1.00 19.59 ?  28  LYS   B O    1 
ATOM   4461 C  CB   . LYS   B 1 28  ? 55.716 -20.243 -12.702 1.00 20.38 ?  28  LYS   B CB   1 
ATOM   4462 C  CG   . LYS   B 1 28  ? 56.121 -19.882 -11.273 1.00 23.91 ?  28  LYS   B CG   1 
ATOM   4463 C  CD   . LYS   B 1 28  ? 57.549 -20.282 -10.936 1.00 28.67 ?  28  LYS   B CD   1 
ATOM   4464 C  CE   . LYS   B 1 28  ? 57.666 -21.761 -10.661 1.00 32.10 ?  28  LYS   B CE   1 
ATOM   4465 N  NZ   . LYS   B 1 28  ? 59.026 -22.106 -10.161 1.00 34.13 ?  28  LYS   B NZ   1 
ATOM   4466 H  H    . LYS   B 1 28  ? 53.517 -20.960 -11.886 1.00 18.68 ?  28  LYS   B H    1 
ATOM   4467 H  HA   . LYS   B 1 28  ? 54.406 -18.699 -12.870 1.00 21.03 ?  28  LYS   B HA   1 
ATOM   4468 H  HB2  . LYS   B 1 28  ? 55.669 -21.210 -12.759 1.00 24.46 ?  28  LYS   B HB2  1 
ATOM   4469 H  HB3  . LYS   B 1 28  ? 56.407 -19.908 -13.298 1.00 24.46 ?  28  LYS   B HB3  1 
ATOM   4470 H  HG2  . LYS   B 1 28  ? 56.044 -18.920 -11.160 1.00 28.69 ?  28  LYS   B HG2  1 
ATOM   4471 H  HG3  . LYS   B 1 28  ? 55.529 -20.335 -10.655 1.00 28.69 ?  28  LYS   B HG3  1 
ATOM   4472 H  HD2  . LYS   B 1 28  ? 58.126 -20.064 -11.686 1.00 34.41 ?  28  LYS   B HD2  1 
ATOM   4473 H  HD3  . LYS   B 1 28  ? 57.836 -19.799 -10.144 1.00 34.41 ?  28  LYS   B HD3  1 
ATOM   4474 H  HE2  . LYS   B 1 28  ? 57.018 -22.014 -9.985  1.00 38.53 ?  28  LYS   B HE2  1 
ATOM   4475 H  HE3  . LYS   B 1 28  ? 57.507 -22.255 -11.481 1.00 38.53 ?  28  LYS   B HE3  1 
ATOM   4476 H  HZ1  . LYS   B 1 28  ? 59.080 -22.979 -10.003 1.00 40.96 ?  28  LYS   B HZ1  1 
ATOM   4477 H  HZ2  . LYS   B 1 28  ? 59.638 -21.883 -10.768 1.00 40.96 ?  28  LYS   B HZ2  1 
ATOM   4478 H  HZ3  . LYS   B 1 28  ? 59.193 -21.664 -9.406  1.00 40.96 ?  28  LYS   B HZ3  1 
ATOM   4479 N  N    . LYS   B 1 29  ? 53.409 -20.768 -15.050 1.00 19.34 ?  29  LYS   B N    1 
ATOM   4480 C  CA   . LYS   B 1 29  ? 53.124 -20.919 -16.474 1.00 22.30 ?  29  LYS   B CA   1 
ATOM   4481 C  C    . LYS   B 1 29  ? 51.885 -20.139 -16.905 1.00 21.20 ?  29  LYS   B C    1 
ATOM   4482 O  O    . LYS   B 1 29  ? 51.891 -19.499 -17.963 1.00 22.64 ?  29  LYS   B O    1 
ATOM   4483 C  CB   . LYS   B 1 29  ? 52.959 -22.401 -16.820 1.00 27.19 ?  29  LYS   B CB   1 
ATOM   4484 C  CG   . LYS   B 1 29  ? 52.826 -22.675 -18.312 1.00 31.68 ?  29  LYS   B CG   1 
ATOM   4485 C  CD   . LYS   B 1 29  ? 53.080 -24.141 -18.643 1.00 35.41 ?  29  LYS   B CD   1 
ATOM   4486 C  CE   . LYS   B 1 29  ? 51.970 -25.041 -18.125 1.00 37.96 ?  29  LYS   B CE   1 
ATOM   4487 N  NZ   . LYS   B 1 29  ? 52.247 -26.478 -18.411 1.00 39.11 ?  29  LYS   B NZ   1 
ATOM   4488 H  H    . LYS   B 1 29  ? 53.100 -21.402 -14.552 1.00 23.21 ?  29  LYS   B H    1 
ATOM   4489 H  HA   . LYS   B 1 29  ? 53.874 -20.579 -16.976 1.00 26.77 ?  29  LYS   B HA   1 
ATOM   4490 H  HB2  . LYS   B 1 29  ? 53.738 -22.882 -16.499 1.00 32.63 ?  29  LYS   B HB2  1 
ATOM   4491 H  HB3  . LYS   B 1 29  ? 52.162 -22.739 -16.384 1.00 32.63 ?  29  LYS   B HB3  1 
ATOM   4492 H  HG2  . LYS   B 1 29  ? 51.927 -22.450 -18.598 1.00 38.03 ?  29  LYS   B HG2  1 
ATOM   4493 H  HG3  . LYS   B 1 29  ? 53.475 -22.138 -18.795 1.00 38.03 ?  29  LYS   B HG3  1 
ATOM   4494 H  HD2  . LYS   B 1 29  ? 53.131 -24.247 -19.606 1.00 42.50 ?  29  LYS   B HD2  1 
ATOM   4495 H  HD3  . LYS   B 1 29  ? 53.913 -24.423 -18.232 1.00 42.50 ?  29  LYS   B HD3  1 
ATOM   4496 H  HE2  . LYS   B 1 29  ? 51.890 -24.933 -17.165 1.00 45.56 ?  29  LYS   B HE2  1 
ATOM   4497 H  HE3  . LYS   B 1 29  ? 51.136 -24.801 -18.560 1.00 45.56 ?  29  LYS   B HE3  1 
ATOM   4498 H  HZ1  . LYS   B 1 29  ? 51.584 -26.984 -18.099 1.00 46.93 ?  29  LYS   B HZ1  1 
ATOM   4499 H  HZ2  . LYS   B 1 29  ? 52.320 -26.606 -19.289 1.00 46.93 ?  29  LYS   B HZ2  1 
ATOM   4500 H  HZ3  . LYS   B 1 29  ? 53.007 -26.725 -18.019 1.00 46.93 ?  29  LYS   B HZ3  1 
ATOM   4501 N  N    . VAL   B 1 30  ? 50.816 -20.194 -16.104 1.00 19.29 ?  30  VAL   B N    1 
ATOM   4502 C  CA   . VAL   B 1 30  ? 49.523 -19.614 -16.476 1.00 19.29 ?  30  VAL   B CA   1 
ATOM   4503 C  C    . VAL   B 1 30  ? 49.519 -18.099 -16.341 1.00 18.22 ?  30  VAL   B C    1 
ATOM   4504 O  O    . VAL   B 1 30  ? 48.772 -17.404 -17.047 1.00 18.88 ?  30  VAL   B O    1 
ATOM   4505 C  CB   . VAL   B 1 30  ? 48.425 -20.228 -15.583 1.00 20.53 ?  30  VAL   B CB   1 
ATOM   4506 C  CG1  . VAL   B 1 30  ? 47.139 -19.410 -15.644 1.00 21.10 ?  30  VAL   B CG1  1 
ATOM   4507 C  CG2  . VAL   B 1 30  ? 48.169 -21.678 -15.966 1.00 21.34 ?  30  VAL   B CG2  1 
ATOM   4508 H  H    . VAL   B 1 30  ? 50.807 -20.581 -15.327 1.00 23.15 ?  30  VAL   B H    1 
ATOM   4509 H  HA   . VAL   B 1 30  ? 49.321 -19.852 -17.393 1.00 23.15 ?  30  VAL   B HA   1 
ATOM   4510 H  HB   . VAL   B 1 30  ? 48.728 -20.230 -14.662 1.00 24.64 ?  30  VAL   B HB   1 
ATOM   4511 H  HG11 . VAL   B 1 30  ? 46.398 -19.983 -15.388 1.00 25.33 ?  30  VAL   B HG11 1 
ATOM   4512 H  HG12 . VAL   B 1 30  ? 47.203 -18.668 -15.026 1.00 25.33 ?  30  VAL   B HG12 1 
ATOM   4513 H  HG13 . VAL   B 1 30  ? 47.003 -19.096 -16.546 1.00 25.33 ?  30  VAL   B HG13 1 
ATOM   4514 H  HG21 . VAL   B 1 30  ? 47.483 -22.048 -15.381 1.00 25.61 ?  30  VAL   B HG21 1 
ATOM   4515 H  HG22 . VAL   B 1 30  ? 47.862 -21.713 -16.887 1.00 25.61 ?  30  VAL   B HG22 1 
ATOM   4516 H  HG23 . VAL   B 1 30  ? 48.988 -22.183 -15.870 1.00 25.61 ?  30  VAL   B HG23 1 
ATOM   4517 N  N    . LYS   B 1 31  ? 50.303 -17.582 -15.410 1.00 17.95 ?  31  LYS   B N    1 
ATOM   4518 C  CA   . LYS   B 1 31  ? 50.330 -16.171 -15.055 1.00 18.41 ?  31  LYS   B CA   1 
ATOM   4519 C  C    . LYS   B 1 31  ? 48.934 -15.691 -14.657 1.00 16.33 ?  31  LYS   B C    1 
ATOM   4520 O  O    . LYS   B 1 31  ? 48.393 -14.768 -15.278 1.00 17.30 ?  31  LYS   B O    1 
ATOM   4521 C  CB   . LYS   B 1 31  ? 50.960 -15.362 -16.193 1.00 21.28 ?  31  LYS   B CB   1 
ATOM   4522 C  CG   . LYS   B 1 31  ? 52.398 -15.796 -16.496 1.00 24.45 ?  31  LYS   B CG   1 
ATOM   4523 C  CD   . LYS   B 1 31  ? 52.981 -15.053 -17.679 1.00 27.80 ?  31  LYS   B CD   1 
ATOM   4524 C  CE   . LYS   B 1 31  ? 54.468 -15.302 -17.809 1.00 30.08 ?  31  LYS   B CE   1 
ATOM   4525 N  NZ   . LYS   B 1 31  ? 55.188 -14.857 -16.585 1.00 31.11 ?  31  LYS   B NZ   1 
ATOM   4526 H  H    . LYS   B 1 31  ? 50.854 -18.061 -14.959 1.00 21.54 ?  31  LYS   B H    1 
ATOM   4527 H  HA   . LYS   B 1 31  ? 50.894 -16.082 -14.286 1.00 22.10 ?  31  LYS   B HA   1 
ATOM   4528 H  HB2  . LYS   B 1 31  ? 50.436 -15.479 -17.001 1.00 25.54 ?  31  LYS   B HB2  1 
ATOM   4529 H  HB3  . LYS   B 1 31  ? 50.976 -14.431 -15.935 1.00 25.54 ?  31  LYS   B HB3  1 
ATOM   4530 H  HG2  . LYS   B 1 31  ? 52.946 -15.621 -15.715 1.00 29.35 ?  31  LYS   B HG2  1 
ATOM   4531 H  HG3  . LYS   B 1 31  ? 52.407 -16.748 -16.699 1.00 29.35 ?  31  LYS   B HG3  1 
ATOM   4532 H  HD2  . LYS   B 1 31  ? 52.547 -15.360 -18.489 1.00 33.37 ?  31  LYS   B HD2  1 
ATOM   4533 H  HD3  . LYS   B 1 31  ? 52.839 -14.105 -17.555 1.00 33.37 ?  31  LYS   B HD3  1 
ATOM   4534 H  HE2  . LYS   B 1 31  ? 54.630 -16.252 -17.932 1.00 36.10 ?  31  LYS   B HE2  1 
ATOM   4535 H  HE3  . LYS   B 1 31  ? 54.812 -14.802 -18.566 1.00 36.10 ?  31  LYS   B HE3  1 
ATOM   4536 H  HZ1  . LYS   B 1 31  ? 56.065 -14.864 -16.728 1.00 37.33 ?  31  LYS   B HZ1  1 
ATOM   4537 H  HZ2  . LYS   B 1 31  ? 54.936 -14.031 -16.370 1.00 37.33 ?  31  LYS   B HZ2  1 
ATOM   4538 H  HZ3  . LYS   B 1 31  ? 55.000 -15.401 -15.906 1.00 37.33 ?  31  LYS   B HZ3  1 
ATOM   4539 N  N    . PRO   B 1 32  ? 48.328 -16.283 -13.621 1.00 14.34 ?  32  PRO   B N    1 
ATOM   4540 C  CA   . PRO   B 1 32  ? 46.951 -15.924 -13.259 1.00 13.47 ?  32  PRO   B CA   1 
ATOM   4541 C  C    . PRO   B 1 32  ? 46.879 -14.578 -12.557 1.00 13.68 ?  32  PRO   B C    1 
ATOM   4542 O  O    . PRO   B 1 32  ? 47.805 -14.159 -11.856 1.00 14.74 ?  32  PRO   B O    1 
ATOM   4543 C  CB   . PRO   B 1 32  ? 46.556 -17.038 -12.282 1.00 13.59 ?  32  PRO   B CB   1 
ATOM   4544 C  CG   . PRO   B 1 32  ? 47.855 -17.384 -11.607 1.00 13.82 ?  32  PRO   B CG   1 
ATOM   4545 C  CD   . PRO   B 1 32  ? 48.910 -17.255 -12.674 1.00 14.34 ?  32  PRO   B CD   1 
ATOM   4546 H  HA   . PRO   B 1 32  ? 46.368 -15.940 -14.038 1.00 16.17 ?  32  PRO   B HA   1 
ATOM   4547 H  HB2  . PRO   B 1 32  ? 45.908 -16.703 -11.640 1.00 16.31 ?  32  PRO   B HB2  1 
ATOM   4548 H  HB3  . PRO   B 1 32  ? 46.202 -17.801 -12.766 1.00 16.31 ?  32  PRO   B HB3  1 
ATOM   4549 H  HG2  . PRO   B 1 32  ? 48.022 -16.761 -10.879 1.00 16.59 ?  32  PRO   B HG2  1 
ATOM   4550 H  HG3  . PRO   B 1 32  ? 47.818 -18.295 -11.270 1.00 16.59 ?  32  PRO   B HG3  1 
ATOM   4551 H  HD2  . PRO   B 1 32  ? 49.728 -16.902 -12.297 1.00 17.22 ?  32  PRO   B HD2  1 
ATOM   4552 H  HD3  . PRO   B 1 32  ? 49.052 -18.106 -13.110 1.00 17.22 ?  32  PRO   B HD3  1 
ATOM   4553 N  N    . THR   B 1 33  ? 45.731 -13.918 -12.726 1.00 12.93 ?  33  THR   B N    1 
ATOM   4554 C  CA   . THR   B 1 33  ? 45.437 -12.744 -11.912 1.00 13.26 ?  33  THR   B CA   1 
ATOM   4555 C  C    . THR   B 1 33  ? 45.392 -13.099 -10.432 1.00 12.96 ?  33  THR   B C    1 
ATOM   4556 O  O    . THR   B 1 33  ? 45.876 -12.328 -9.590  1.00 14.04 ?  33  THR   B O    1 
ATOM   4557 C  CB   . THR   B 1 33  ? 44.120 -12.109 -12.356 1.00 13.91 ?  33  THR   B CB   1 
ATOM   4558 O  OG1  . THR   B 1 33  ? 44.163 -11.858 -13.762 1.00 13.82 ?  33  THR   B OG1  1 
ATOM   4559 C  CG2  . THR   B 1 33  ? 43.877 -10.814 -11.610 1.00 15.15 ?  33  THR   B CG2  1 
ATOM   4560 H  H    . THR   B 1 33  ? 45.117 -14.129 -13.300 1.00 15.52 ?  33  THR   B H    1 
ATOM   4561 H  HA   . THR   B 1 33  ? 46.138 -12.092 -12.045 1.00 15.91 ?  33  THR   B HA   1 
ATOM   4562 H  HB   . THR   B 1 33  ? 43.384 -12.718 -12.169 1.00 16.70 ?  33  THR   B HB   1 
ATOM   4563 H  HG1  . THR   B 1 33  ? 43.445 -11.486 -14.013 1.00 16.59 ?  33  THR   B HG1  1 
ATOM   4564 H  HG21 . THR   B 1 33  ? 43.127 -10.343 -11.998 1.00 18.19 ?  33  THR   B HG21 1 
ATOM   4565 H  HG22 . THR   B 1 33  ? 43.685 -11.000 -10.677 1.00 18.19 ?  33  THR   B HG22 1 
ATOM   4566 H  HG23 . THR   B 1 33  ? 44.667 -10.252 -11.663 1.00 18.19 ?  33  THR   B HG23 1 
ATOM   4567 N  N    . VAL   B 1 34  ? 44.834 -14.268 -10.094 1.00 12.18 ?  34  VAL   B N    1 
ATOM   4568 C  CA   . VAL   B 1 34  ? 44.637 -14.663 -8.703  1.00 11.81 ?  34  VAL   B CA   1 
ATOM   4569 C  C    . VAL   B 1 34  ? 45.066 -16.112 -8.533  1.00 10.92 ?  34  VAL   B C    1 
ATOM   4570 O  O    . VAL   B 1 34  ? 44.541 -17.002 -9.214  1.00 11.59 ?  34  VAL   B O    1 
ATOM   4571 C  CB   . VAL   B 1 34  ? 43.171 -14.516 -8.256  1.00 12.98 ?  34  VAL   B CB   1 
ATOM   4572 C  CG1  . VAL   B 1 34  ? 43.007 -14.965 -6.813  1.00 13.38 ?  34  VAL   B CG1  1 
ATOM   4573 C  CG2  . VAL   B 1 34  ? 42.684 -13.087 -8.441  1.00 13.88 ?  34  VAL   B CG2  1 
ATOM   4574 H  H    . VAL   B 1 34  ? 44.568 -14.859 -10.663 1.00 14.62 ?  34  VAL   B H    1 
ATOM   4575 H  HA   . VAL   B 1 34  ? 45.194 -14.110 -8.130  1.00 14.18 ?  34  VAL   B HA   1 
ATOM   4576 H  HB   . VAL   B 1 34  ? 42.620 -15.085 -8.809  1.00 15.59 ?  34  VAL   B HB   1 
ATOM   4577 H  HG11 . VAL   B 1 34  ? 42.155 -14.644 -6.476  1.00 16.06 ?  34  VAL   B HG11 1 
ATOM   4578 H  HG12 . VAL   B 1 34  ? 43.028 -15.935 -6.776  1.00 16.06 ?  34  VAL   B HG12 1 
ATOM   4579 H  HG13 . VAL   B 1 34  ? 43.730 -14.598 -6.279  1.00 16.06 ?  34  VAL   B HG13 1 
ATOM   4580 H  HG21 . VAL   B 1 34  ? 41.768 -13.020 -8.128  1.00 16.67 ?  34  VAL   B HG21 1 
ATOM   4581 H  HG22 . VAL   B 1 34  ? 43.252 -12.486 -7.930  1.00 16.67 ?  34  VAL   B HG22 1 
ATOM   4582 H  HG23 . VAL   B 1 34  ? 42.727 -12.854 -9.384  1.00 16.67 ?  34  VAL   B HG23 1 
ATOM   4583 N  N    . VAL   B 1 35  ? 45.975 -16.361 -7.595  1.00 10.41 ?  35  VAL   B N    1 
ATOM   4584 C  CA   . VAL   B 1 35  ? 46.200 -17.705 -7.074  1.00 10.02 ?  35  VAL   B CA   1 
ATOM   4585 C  C    . VAL   B 1 35  ? 45.663 -17.756 -5.653  1.00 10.02 ?  35  VAL   B C    1 
ATOM   4586 O  O    . VAL   B 1 35  ? 45.885 -16.831 -4.863  1.00 10.37 ?  35  VAL   B O    1 
ATOM   4587 C  CB   . VAL   B 1 35  ? 47.682 -18.132 -7.157  1.00 10.75 ?  35  VAL   B CB   1 
ATOM   4588 C  CG1  . VAL   B 1 35  ? 48.582 -17.286 -6.240  1.00 11.64 ?  35  VAL   B CG1  1 
ATOM   4589 C  CG2  . VAL   B 1 35  ? 47.824 -19.626 -6.842  1.00 11.55 ?  35  VAL   B CG2  1 
ATOM   4590 H  H    . VAL   B 1 35  ? 46.482 -15.763 -7.239  1.00 12.50 ?  35  VAL   B H    1 
ATOM   4591 H  HA   . VAL   B 1 35  ? 45.682 -18.334 -7.601  1.00 12.03 ?  35  VAL   B HA   1 
ATOM   4592 H  HB   . VAL   B 1 35  ? 47.986 -18.003 -8.070  1.00 12.91 ?  35  VAL   B HB   1 
ATOM   4593 H  HG11 . VAL   B 1 35  ? 49.504 -17.514 -6.418  1.00 13.98 ?  35  VAL   B HG11 1 
ATOM   4594 H  HG12 . VAL   B 1 35  ? 48.418 -16.354 -6.421  1.00 13.98 ?  35  VAL   B HG12 1 
ATOM   4595 H  HG13 . VAL   B 1 35  ? 48.360 -17.494 -5.316  1.00 13.98 ?  35  VAL   B HG13 1 
ATOM   4596 H  HG21 . VAL   B 1 35  ? 48.745 -19.895 -6.948  1.00 13.86 ?  35  VAL   B HG21 1 
ATOM   4597 H  HG22 . VAL   B 1 35  ? 47.533 -19.791 -5.927  1.00 13.86 ?  35  VAL   B HG22 1 
ATOM   4598 H  HG23 . VAL   B 1 35  ? 47.259 -20.140 -7.453  1.00 13.86 ?  35  VAL   B HG23 1 
ATOM   4599 N  N    . VAL   B 1 36  ? 44.936 -18.828 -5.339  1.00 9.98  ?  36  VAL   B N    1 
ATOM   4600 C  CA   . VAL   B 1 36  ? 44.392 -19.030 -4.006  1.00 9.86  ?  36  VAL   B CA   1 
ATOM   4601 C  C    . VAL   B 1 36  ? 45.401 -19.792 -3.156  1.00 9.50  ?  36  VAL   B C    1 
ATOM   4602 O  O    . VAL   B 1 36  ? 45.940 -20.828 -3.576  1.00 10.59 ?  36  VAL   B O    1 
ATOM   4603 C  CB   . VAL   B 1 36  ? 43.058 -19.793 -4.077  1.00 10.24 ?  36  VAL   B CB   1 
ATOM   4604 C  CG1  . VAL   B 1 36  ? 42.565 -20.162 -2.683  1.00 10.68 ?  36  VAL   B CG1  1 
ATOM   4605 C  CG2  . VAL   B 1 36  ? 42.028 -18.963 -4.817  1.00 10.69 ?  36  VAL   B CG2  1 
ATOM   4606 H  H    . VAL   B 1 36  ? 44.750 -19.465 -5.887  1.00 11.98 ?  36  VAL   B H    1 
ATOM   4607 H  HA   . VAL   B 1 36  ? 44.228 -18.171 -3.590  1.00 11.84 ?  36  VAL   B HA   1 
ATOM   4608 H  HB   . VAL   B 1 36  ? 43.189 -20.615 -4.573  1.00 12.29 ?  36  VAL   B HB   1 
ATOM   4609 H  HG11 . VAL   B 1 36  ? 41.624 -20.392 -2.731  1.00 12.82 ?  36  VAL   B HG11 1 
ATOM   4610 H  HG12 . VAL   B 1 36  ? 43.073 -20.918 -2.353  1.00 12.82 ?  36  VAL   B HG12 1 
ATOM   4611 H  HG13 . VAL   B 1 36  ? 42.684 -19.398 -2.093  1.00 12.82 ?  36  VAL   B HG13 1 
ATOM   4612 H  HG21 . VAL   B 1 36  ? 41.184 -19.440 -4.832  1.00 12.84 ?  36  VAL   B HG21 1 
ATOM   4613 H  HG22 . VAL   B 1 36  ? 41.918 -18.112 -4.359  1.00 12.84 ?  36  VAL   B HG22 1 
ATOM   4614 H  HG23 . VAL   B 1 36  ? 42.337 -18.808 -5.725  1.00 12.84 ?  36  VAL   B HG23 1 
ATOM   4615 N  N    . ASN   B 1 37  ? 45.622 -19.301 -1.941  1.00 9.75  ?  37  ASN   B N    1 
ATOM   4616 C  CA   . ASN   B 1 37  ? 46.374 -20.026 -0.931  1.00 10.06 ?  37  ASN   B CA   1 
ATOM   4617 C  C    . ASN   B 1 37  ? 45.426 -20.697 0.050   1.00 10.28 ?  37  ASN   B C    1 
ATOM   4618 O  O    . ASN   B 1 37  ? 44.413 -20.119 0.459   1.00 10.93 ?  37  ASN   B O    1 
ATOM   4619 C  CB   . ASN   B 1 37  ? 47.295 -19.079 -0.164  1.00 10.21 ?  37  ASN   B CB   1 
ATOM   4620 C  CG   . ASN   B 1 37  ? 48.145 -19.798 0.845   1.00 10.56 ?  37  ASN   B CG   1 
ATOM   4621 O  OD1  . ASN   B 1 37  ? 48.485 -20.973 0.666   1.00 11.22 ?  37  ASN   B OD1  1 
ATOM   4622 N  ND2  . ASN   B 1 37  ? 48.499 -19.099 1.917   1.00 10.71 ?  37  ASN   B ND2  1 
ATOM   4623 H  H    . ASN   B 1 37  ? 45.338 -18.531 -1.669  1.00 11.71 ?  37  ASN   B H    1 
ATOM   4624 H  HA   . ASN   B 1 37  ? 46.911 -20.711 -1.349  1.00 12.07 ?  37  ASN   B HA   1 
ATOM   4625 H  HB2  . ASN   B 1 37  ? 47.885 -18.642 -0.792  1.00 12.26 ?  37  ASN   B HB2  1 
ATOM   4626 H  HB3  . ASN   B 1 37  ? 46.759 -18.426 0.310   1.00 12.26 ?  37  ASN   B HB3  1 
ATOM   4627 H  HD21 . ASN   B 1 37  ? 48.993 -19.460 2.524   1.00 12.86 ?  37  ASN   B HD21 1 
ATOM   4628 H  HD22 . ASN   B 1 37  ? 48.247 -18.286 2.007   1.00 12.86 ?  37  ASN   B HD22 1 
ATOM   4629 N  N    . ALA   B 1 38  ? 45.770 -21.931 0.421   1.00 10.49 ?  38  ALA   B N    1 
ATOM   4630 C  CA   . ALA   B 1 38  ? 45.115 -22.674 1.499   1.00 10.84 ?  38  ALA   B CA   1 
ATOM   4631 C  C    . ALA   B 1 38  ? 45.698 -22.187 2.824   1.00 10.55 ?  38  ALA   B C    1 
ATOM   4632 O  O    . ALA   B 1 38  ? 46.600 -22.792 3.413   1.00 11.45 ?  38  ALA   B O    1 
ATOM   4633 C  CB   . ALA   B 1 38  ? 45.347 -24.165 1.313   1.00 12.05 ?  38  ALA   B CB   1 
ATOM   4634 H  H    . ALA   B 1 38  ? 46.410 -22.375 0.055   1.00 12.59 ?  38  ALA   B H    1 
ATOM   4635 H  HA   . ALA   B 1 38  ? 44.160 -22.502 1.491   1.00 13.01 ?  38  ALA   B HA   1 
ATOM   4636 H  HB1  . ALA   B 1 38  ? 44.903 -24.650 2.036   1.00 14.47 ?  38  ALA   B HB1  1 
ATOM   4637 H  HB2  . ALA   B 1 38  ? 44.972 -24.445 0.462   1.00 14.47 ?  38  ALA   B HB2  1 
ATOM   4638 H  HB3  . ALA   B 1 38  ? 46.296 -24.349 1.335   1.00 14.47 ?  38  ALA   B HB3  1 
ATOM   4639 N  N    . ALA   B 1 39  ? 45.187 -21.045 3.278   1.00 10.58 ?  39  ALA   B N    1 
ATOM   4640 C  CA   . ALA   B 1 39  ? 45.736 -20.313 4.407   1.00 10.65 ?  39  ALA   B CA   1 
ATOM   4641 C  C    . ALA   B 1 39  ? 45.120 -20.759 5.732   1.00 10.58 ?  39  ALA   B C    1 
ATOM   4642 O  O    . ALA   B 1 39  ? 44.091 -21.433 5.784   1.00 11.82 ?  39  ALA   B O    1 
ATOM   4643 C  CB   . ALA   B 1 39  ? 45.497 -18.813 4.210   1.00 11.46 ?  39  ALA   B CB   1 
ATOM   4644 H  H    . ALA   B 1 39  ? 44.496 -20.671 2.926   1.00 12.71 ?  39  ALA   B H    1 
ATOM   4645 H  HA   . ALA   B 1 39  ? 46.688 -20.463 4.447   1.00 12.78 ?  39  ALA   B HA   1 
ATOM   4646 H  HB1  . ALA   B 1 39  ? 45.865 -18.333 4.967   1.00 13.75 ?  39  ALA   B HB1  1 
ATOM   4647 H  HB2  . ALA   B 1 39  ? 45.935 -18.526 3.391   1.00 13.75 ?  39  ALA   B HB2  1 
ATOM   4648 H  HB3  . ALA   B 1 39  ? 44.542 -18.647 4.146   1.00 13.75 ?  39  ALA   B HB3  1 
ATOM   4649 N  N    . ASN   B 1 40  ? 45.758 -20.329 6.815   1.00 11.32 ?  40  ASN   B N    1 
ATOM   4650 C  CA   . ASN   B 1 40  ? 45.199 -20.384 8.154   1.00 12.19 ?  40  ASN   B CA   1 
ATOM   4651 C  C    . ASN   B 1 40  ? 45.018 -18.959 8.679   1.00 11.86 ?  40  ASN   B C    1 
ATOM   4652 O  O    . ASN   B 1 40  ? 45.427 -17.980 8.048   1.00 11.81 ?  40  ASN   B O    1 
ATOM   4653 C  CB   . ASN   B 1 40  ? 46.051 -21.260 9.088   1.00 12.89 ?  40  ASN   B CB   1 
ATOM   4654 C  CG   . ASN   B 1 40  ? 47.501 -20.849 9.121   1.00 14.09 ?  40  ASN   B CG   1 
ATOM   4655 O  OD1  . ASN   B 1 40  ? 47.814 -19.666 9.172   1.00 16.04 ?  40  ASN   B OD1  1 
ATOM   4656 N  ND2  . ASN   B 1 40  ? 48.395 -21.822 9.098   1.00 14.28 ?  40  ASN   B ND2  1 
ATOM   4657 H  H    . ASN   B 1 40  ? 46.549 -19.995 6.791   1.00 13.59 ?  40  ASN   B H    1 
ATOM   4658 H  HA   . ASN   B 1 40  ? 44.316 -20.779 8.105   1.00 14.63 ?  40  ASN   B HA   1 
ATOM   4659 H  HB2  . ASN   B 1 40  ? 45.698 -21.192 9.987   1.00 15.47 ?  40  ASN   B HB2  1 
ATOM   4660 H  HB3  . ASN   B 1 40  ? 46.004 -22.177 8.779   1.00 15.47 ?  40  ASN   B HB3  1 
ATOM   4661 H  HD21 . ASN   B 1 40  ? 49.234 -21.639 9.119   1.00 17.14 ?  40  ASN   B HD21 1 
ATOM   4662 H  HD22 . ASN   B 1 40  ? 48.134 -22.642 9.063   1.00 17.14 ?  40  ASN   B HD22 1 
ATOM   4663 N  N    . VAL   B 1 41  ? 44.369 -18.836 9.837   1.00 12.45 ?  41  VAL   B N    1 
ATOM   4664 C  CA   . VAL   B 1 41  ? 43.905 -17.519 10.281  1.00 13.05 ?  41  VAL   B CA   1 
ATOM   4665 C  C    . VAL   B 1 41  ? 45.052 -16.562 10.573  1.00 12.66 ?  41  VAL   B C    1 
ATOM   4666 O  O    . VAL   B 1 41  ? 44.869 -15.342 10.484  1.00 13.02 ?  41  VAL   B O    1 
ATOM   4667 C  CB   . VAL   B 1 41  ? 42.936 -17.598 11.476  1.00 14.72 ?  41  VAL   B CB   1 
ATOM   4668 C  CG1  . VAL   B 1 41  ? 41.640 -18.283 11.074  1.00 15.00 ?  41  VAL   B CG1  1 
ATOM   4669 C  CG2  . VAL   B 1 41  ? 43.594 -18.280 12.670  1.00 15.70 ?  41  VAL   B CG2  1 
ATOM   4670 H  H    . VAL   B 1 41  ? 44.191 -19.480 10.370  1.00 14.95 ?  41  VAL   B H    1 
ATOM   4671 H  HA   . VAL   B 1 41  ? 43.406 -17.125 9.553   1.00 15.67 ?  41  VAL   B HA   1 
ATOM   4672 H  HB   . VAL   B 1 41  ? 42.710 -16.697 11.751  1.00 17.67 ?  41  VAL   B HB   1 
ATOM   4673 H  HG11 . VAL   B 1 41  ? 41.038 -18.296 11.836  1.00 18.00 ?  41  VAL   B HG11 1 
ATOM   4674 H  HG12 . VAL   B 1 41  ? 41.237 -17.791 10.343  1.00 18.00 ?  41  VAL   B HG12 1 
ATOM   4675 H  HG13 . VAL   B 1 41  ? 41.836 -19.191 10.795  1.00 18.00 ?  41  VAL   B HG13 1 
ATOM   4676 H  HG21 . VAL   B 1 41  ? 42.960 -18.316 13.401  1.00 18.85 ?  41  VAL   B HG21 1 
ATOM   4677 H  HG22 . VAL   B 1 41  ? 43.855 -19.180 12.415  1.00 18.85 ?  41  VAL   B HG22 1 
ATOM   4678 H  HG23 . VAL   B 1 41  ? 44.376 -17.771 12.932  1.00 18.85 ?  41  VAL   B HG23 1 
ATOM   4679 N  N    . TYR   B 1 42  ? 46.221 -17.072 10.961  1.00 13.14 ?  42  TYR   B N    1 
ATOM   4680 C  CA   . TYR   B 1 42  ? 47.375 -16.225 11.232  1.00 13.28 ?  42  TYR   B CA   1 
ATOM   4681 C  C    . TYR   B 1 42  ? 48.339 -16.154 10.050  1.00 12.65 ?  42  TYR   B C    1 
ATOM   4682 O  O    . TYR   B 1 42  ? 49.431 -15.589 10.181  1.00 13.93 ?  42  TYR   B O    1 
ATOM   4683 C  CB   . TYR   B 1 42  ? 48.063 -16.645 12.537  1.00 15.05 ?  42  TYR   B CB   1 
ATOM   4684 C  CG   . TYR   B 1 42  ? 47.471 -15.951 13.765  1.00 15.16 ?  42  TYR   B CG   1 
ATOM   4685 C  CD1  . TYR   B 1 42  ? 47.687 -14.595 13.978  1.00 14.36 ?  42  TYR   B CD1  1 
ATOM   4686 C  CD2  . TYR   B 1 42  ? 46.701 -16.637 14.696  1.00 16.84 ?  42  TYR   B CD2  1 
ATOM   4687 C  CE1  . TYR   B 1 42  ? 47.168 -13.940 15.069  1.00 15.35 ?  42  TYR   B CE1  1 
ATOM   4688 C  CE2  . TYR   B 1 42  ? 46.175 -15.983 15.807  1.00 17.14 ?  42  TYR   B CE2  1 
ATOM   4689 C  CZ   . TYR   B 1 42  ? 46.413 -14.629 15.988  1.00 16.99 ?  42  TYR   B CZ   1 
ATOM   4690 O  OH   . TYR   B 1 42  ? 45.910 -13.947 17.081  1.00 19.67 ?  42  TYR   B OH   1 
ATOM   4691 H  H    . TYR   B 1 42  ? 46.372 -17.919 11.061  1.00 15.77 ?  42  TYR   B H    1 
ATOM   4692 H  HA   . TYR   B 1 42  ? 47.049 -15.327 11.366  1.00 15.94 ?  42  TYR   B HA   1 
ATOM   4693 H  HB2  . TYR   B 1 42  ? 47.962 -17.602 12.654  1.00 18.07 ?  42  TYR   B HB2  1 
ATOM   4694 H  HB3  . TYR   B 1 42  ? 49.004 -16.415 12.484  1.00 18.07 ?  42  TYR   B HB3  1 
ATOM   4695 H  HD1  . TYR   B 1 42  ? 48.204 -14.118 13.355  1.00 17.24 ?  42  TYR   B HD1  1 
ATOM   4696 H  HD2  . TYR   B 1 42  ? 46.540 -17.548 14.572  1.00 20.21 ?  42  TYR   B HD2  1 
ATOM   4697 H  HE1  . TYR   B 1 42  ? 47.334 -13.031 15.186  1.00 18.43 ?  42  TYR   B HE1  1 
ATOM   4698 H  HE2  . TYR   B 1 42  ? 45.660 -16.456 16.420  1.00 20.57 ?  42  TYR   B HE2  1 
ATOM   4699 H  HH   . TYR   B 1 42  ? 46.141 -13.145 17.037  1.00 23.61 ?  42  TYR   B HH   1 
ATOM   4700 N  N    . LEU   B 1 43  ? 47.942 -16.674 8.892   1.00 11.90 ?  43  LEU   B N    1 
ATOM   4701 C  CA   . LEU   B 1 43  ? 48.754 -16.603 7.680   1.00 11.76 ?  43  LEU   B CA   1 
ATOM   4702 C  C    . LEU   B 1 43  ? 50.165 -17.113 7.934   1.00 11.93 ?  43  LEU   B C    1 
ATOM   4703 O  O    . LEU   B 1 43  ? 51.146 -16.526 7.481   1.00 12.73 ?  43  LEU   B O    1 
ATOM   4704 C  CB   . LEU   B 1 43  ? 48.776 -15.197 7.078   1.00 12.11 ?  43  LEU   B CB   1 
ATOM   4705 C  CG   . LEU   B 1 43  ? 47.418 -14.581 6.713   1.00 12.30 ?  43  LEU   B CG   1 
ATOM   4706 C  CD1  . LEU   B 1 43  ? 47.632 -13.186 6.125   1.00 13.33 ?  43  LEU   B CD1  1 
ATOM   4707 C  CD2  . LEU   B 1 43  ? 46.650 -15.468 5.747   1.00 12.52 ?  43  LEU   B CD2  1 
ATOM   4708 H  H    . LEU   B 1 43  ? 47.202 -17.091 8.778   1.00 14.28 ?  43  LEU   B H    1 
ATOM   4709 H  HA   . LEU   B 1 43  ? 48.359 -17.193 7.013   1.00 14.11 ?  43  LEU   B HA   1 
ATOM   4710 H  HB2  . LEU   B 1 43  ? 49.203 -14.604 7.714   1.00 14.54 ?  43  LEU   B HB2  1 
ATOM   4711 H  HB3  . LEU   B 1 43  ? 49.302 -15.226 6.263   1.00 14.54 ?  43  LEU   B HB3  1 
ATOM   4712 H  HG   . LEU   B 1 43  ? 46.891 -14.481 7.521   1.00 14.76 ?  43  LEU   B HG   1 
ATOM   4713 H  HD11 . LEU   B 1 43  ? 46.770 -12.802 5.901   1.00 16.00 ?  43  LEU   B HD11 1 
ATOM   4714 H  HD12 . LEU   B 1 43  ? 48.080 -12.629 6.783   1.00 16.00 ?  43  LEU   B HD12 1 
ATOM   4715 H  HD13 . LEU   B 1 43  ? 48.180 -13.259 5.328   1.00 16.00 ?  43  LEU   B HD13 1 
ATOM   4716 H  HD21 . LEU   B 1 43  ? 45.853 -14.999 5.456   1.00 15.03 ?  43  LEU   B HD21 1 
ATOM   4717 H  HD22 . LEU   B 1 43  ? 47.216 -15.668 4.987   1.00 15.03 ?  43  LEU   B HD22 1 
ATOM   4718 H  HD23 . LEU   B 1 43  ? 46.405 -16.288 6.204   1.00 15.03 ?  43  LEU   B HD23 1 
ATOM   4719 N  N    . LYS   B 1 44  ? 50.263 -18.232 8.656   1.00 12.24 ?  44  LYS   B N    1 
ATOM   4720 C  CA   . LYS   B 1 44  ? 51.529 -18.911 8.901   1.00 12.77 ?  44  LYS   B CA   1 
ATOM   4721 C  C    . LYS   B 1 44  ? 51.648 -20.029 7.876   1.00 12.18 ?  44  LYS   B C    1 
ATOM   4722 O  O    . LYS   B 1 44  ? 50.950 -21.042 7.962   1.00 13.37 ?  44  LYS   B O    1 
ATOM   4723 C  CB   . LYS   B 1 44  ? 51.582 -19.426 10.338  1.00 14.28 ?  44  LYS   B CB   1 
ATOM   4724 C  CG   . LYS   B 1 44  ? 51.787 -18.321 11.364  1.00 17.06 ?  44  LYS   B CG   1 
ATOM   4725 C  CD   . LYS   B 1 44  ? 52.970 -17.444 10.944  1.00 20.46 ?  44  LYS   B CD   1 
ATOM   4726 C  CE   . LYS   B 1 44  ? 53.560 -16.644 12.076  1.00 23.36 ?  44  LYS   B CE   1 
ATOM   4727 N  NZ   . LYS   B 1 44  ? 54.694 -15.794 11.649  1.00 24.65 ?  44  LYS   B NZ   1 
ATOM   4728 H  H    . LYS   B 1 44  ? 49.589 -18.617 9.027   1.00 14.69 ?  44  LYS   B H    1 
ATOM   4729 H  HA   . LYS   B 1 44  ? 52.260 -18.296 8.741   1.00 15.33 ?  44  LYS   B HA   1 
ATOM   4730 H  HB2  . LYS   B 1 44  ? 50.739 -19.868 10.545  1.00 17.14 ?  44  LYS   B HB2  1 
ATOM   4731 H  HB3  . LYS   B 1 44  ? 52.312 -20.055 10.422  1.00 17.14 ?  44  LYS   B HB3  1 
ATOM   4732 H  HG2  . LYS   B 1 44  ? 50.994 -17.773 11.422  1.00 20.47 ?  44  LYS   B HG2  1 
ATOM   4733 H  HG3  . LYS   B 1 44  ? 51.993 -18.719 12.230  1.00 20.47 ?  44  LYS   B HG3  1 
ATOM   4734 H  HD2  . LYS   B 1 44  ? 53.663 -18.016 10.569  1.00 24.56 ?  44  LYS   B HD2  1 
ATOM   4735 H  HD3  . LYS   B 1 44  ? 52.661 -16.819 10.268  1.00 24.56 ?  44  LYS   B HD3  1 
ATOM   4736 H  HE2  . LYS   B 1 44  ? 52.886 -16.038 12.385  1.00 28.04 ?  44  LYS   B HE2  1 
ATOM   4737 H  HE3  . LYS   B 1 44  ? 53.850 -17.243 12.788  1.00 28.04 ?  44  LYS   B HE3  1 
ATOM   4738 H  HZ1  . LYS   B 1 44  ? 55.008 -15.337 12.345  1.00 29.59 ?  44  LYS   B HZ1  1 
ATOM   4739 H  HZ2  . LYS   B 1 44  ? 55.344 -16.295 11.310  1.00 29.59 ?  44  LYS   B HZ2  1 
ATOM   4740 H  HZ3  . LYS   B 1 44  ? 54.419 -15.216 11.027  1.00 29.59 ?  44  LYS   B HZ3  1 
ATOM   4741 N  N    . HIS   B 1 45  ? 52.498 -19.810 6.877   1.00 11.68 ?  45  HIS   B N    1 
ATOM   4742 C  CA   . HIS   B 1 45  ? 52.523 -20.642 5.676   1.00 12.01 ?  45  HIS   B CA   1 
ATOM   4743 C  C    . HIS   B 1 45  ? 53.537 -21.770 5.844   1.00 14.19 ?  45  HIS   B C    1 
ATOM   4744 O  O    . HIS   B 1 45  ? 54.595 -21.794 5.224   1.00 16.55 ?  45  HIS   B O    1 
ATOM   4745 C  CB   . HIS   B 1 45  ? 52.845 -19.788 4.463   1.00 12.06 ?  45  HIS   B CB   1 
ATOM   4746 C  CG   . HIS   B 1 45  ? 51.975 -18.586 4.347   1.00 11.99 ?  45  HIS   B CG   1 
ATOM   4747 N  ND1  . HIS   B 1 45  ? 50.598 -18.664 4.320   1.00 11.93 ?  45  HIS   B ND1  1 
ATOM   4748 C  CD2  . HIS   B 1 45  ? 52.291 -17.274 4.264   1.00 12.76 ?  45  HIS   B CD2  1 
ATOM   4749 C  CE1  . HIS   B 1 45  ? 50.110 -17.441 4.212   1.00 11.78 ?  45  HIS   B CE1  1 
ATOM   4750 N  NE2  . HIS   B 1 45  ? 51.113 -16.582 4.173   1.00 12.23 ?  45  HIS   B NE2  1 
ATOM   4751 H  H    . HIS   B 1 45  ? 53.065 -19.165 6.864   1.00 14.02 ?  45  HIS   B H    1 
ATOM   4752 H  HA   . HIS   B 1 45  ? 51.642 -21.034 5.541   1.00 14.42 ?  45  HIS   B HA   1 
ATOM   4753 H  HB2  . HIS   B 1 45  ? 53.766 -19.491 4.523   1.00 14.48 ?  45  HIS   B HB2  1 
ATOM   4754 H  HB3  . HIS   B 1 45  ? 52.727 -20.327 3.659   1.00 14.48 ?  45  HIS   B HB3  1 
ATOM   4755 H  HD2  . HIS   B 1 45  ? 53.149 -16.910 4.263   1.00 15.32 ?  45  HIS   B HD2  1 
ATOM   4756 H  HE1  . HIS   B 1 45  ? 49.208 -17.226 4.159   1.00 14.14 ?  45  HIS   B HE1  1 
ATOM   4757 H  HE2  . HIS   B 1 45  ? 51.036 -15.728 4.112   1.00 14.68 ?  45  HIS   B HE2  1 
ATOM   4758 N  N    . GLY   B 1 46  ? 53.168 -22.733 6.682   1.00 15.14 ?  46  GLY   B N    1 
ATOM   4759 C  CA   . GLY   B 1 46  ? 54.088 -23.791 7.052   1.00 16.88 ?  46  GLY   B CA   1 
ATOM   4760 C  C    . GLY   B 1 46  ? 54.145 -24.979 6.111   1.00 18.23 ?  46  GLY   B C    1 
ATOM   4761 O  O    . GLY   B 1 46  ? 55.220 -25.381 5.658   1.00 21.62 ?  46  GLY   B O    1 
ATOM   4762 H  H    . GLY   B 1 46  ? 52.393 -22.775 7.068   1.00 18.17 ?  46  GLY   B H    1 
ATOM   4763 H  HA2  . GLY   B 1 46  ? 54.976 -23.413 7.121   1.00 20.26 ?  46  GLY   B HA2  1 
ATOM   4764 H  HA3  . GLY   B 1 46  ? 53.835 -24.122 7.930   1.00 20.26 ?  46  GLY   B HA3  1 
ATOM   4765 N  N    . GLY   B 1 47  ? 52.990 -25.557 5.800   1.00 17.68 ?  47  GLY   B N    1 
ATOM   4766 C  CA   . GLY   B 1 47  ? 52.940 -26.848 5.143   1.00 15.65 ?  47  GLY   B CA   1 
ATOM   4767 C  C    . GLY   B 1 47  ? 52.028 -26.833 3.932   1.00 13.53 ?  47  GLY   B C    1 
ATOM   4768 O  O    . GLY   B 1 47  ? 51.373 -25.833 3.638   1.00 13.80 ?  47  GLY   B O    1 
ATOM   4769 H  H    . GLY   B 1 47  ? 52.213 -25.227 5.979   1.00 21.22 ?  47  GLY   B H    1 
ATOM   4770 H  HA2  . GLY   B 1 47  ? 53.832 -27.100 4.853   1.00 18.79 ?  47  GLY   B HA2  1 
ATOM   4771 H  HA3  . GLY   B 1 47  ? 52.622 -27.518 5.770   1.00 18.79 ?  47  GLY   B HA3  1 
ATOM   4772 N  N    . GLY   B 1 48  ? 51.989 -27.974 3.249   1.00 12.97 ?  48  GLY   B N    1 
ATOM   4773 C  CA   . GLY   B 1 48  ? 51.061 -28.121 2.146   1.00 12.67 ?  48  GLY   B CA   1 
ATOM   4774 C  C    . GLY   B 1 48  ? 51.196 -27.009 1.135   1.00 12.17 ?  48  GLY   B C    1 
ATOM   4775 O  O    . GLY   B 1 48  ? 52.296 -26.540 0.827   1.00 13.05 ?  48  GLY   B O    1 
ATOM   4776 H  H    . GLY   B 1 48  ? 52.486 -28.656 3.399   1.00 15.57 ?  48  GLY   B H    1 
ATOM   4777 H  HA2  . GLY   B 1 48  ? 51.221 -28.967 1.697   1.00 15.21 ?  48  GLY   B HA2  1 
ATOM   4778 H  HA3  . GLY   B 1 48  ? 50.151 -28.119 2.481   1.00 15.21 ?  48  GLY   B HA3  1 
ATOM   4779 N  N    . VAL   B 1 49  ? 50.051 -26.582 0.603   1.00 12.18 ?  49  VAL   B N    1 
ATOM   4780 C  CA   . VAL   B 1 49  ? 50.035 -25.558 -0.437  1.00 12.21 ?  49  VAL   B CA   1 
ATOM   4781 C  C    . VAL   B 1 49  ? 50.699 -24.272 0.051   1.00 11.24 ?  49  VAL   B C    1 
ATOM   4782 O  O    . VAL   B 1 49  ? 51.488 -23.650 -0.669  1.00 11.97 ?  49  VAL   B O    1 
ATOM   4783 C  CB   . VAL   B 1 49  ? 48.592 -25.304 -0.915  1.00 13.17 ?  49  VAL   B CB   1 
ATOM   4784 C  CG1  . VAL   B 1 49  ? 48.519 -24.063 -1.799  1.00 13.11 ?  49  VAL   B CG1  1 
ATOM   4785 C  CG2  . VAL   B 1 49  ? 48.043 -26.524 -1.653  1.00 14.37 ?  49  VAL   B CG2  1 
ATOM   4786 H  H    . VAL   B 1 49  ? 49.264 -26.863 0.826   1.00 14.62 ?  49  VAL   B H    1 
ATOM   4787 H  HA   . VAL   B 1 49  ? 50.537 -25.878 -1.200  1.00 14.65 ?  49  VAL   B HA   1 
ATOM   4788 H  HB   . VAL   B 1 49  ? 48.025 -25.147 -0.146  1.00 15.81 ?  49  VAL   B HB   1 
ATOM   4789 H  HG11 . VAL   B 1 49  ? 47.684 -24.075 -2.297  1.00 15.73 ?  49  VAL   B HG11 1 
ATOM   4790 H  HG12 . VAL   B 1 49  ? 48.552 -23.269 -1.240  1.00 15.73 ?  49  VAL   B HG12 1 
ATOM   4791 H  HG13 . VAL   B 1 49  ? 49.267 -24.066 -2.416  1.00 15.73 ?  49  VAL   B HG13 1 
ATOM   4792 H  HG21 . VAL   B 1 49  ? 47.135 -26.339 -1.945  1.00 17.24 ?  49  VAL   B HG21 1 
ATOM   4793 H  HG22 . VAL   B 1 49  ? 48.605 -26.708 -2.424  1.00 17.24 ?  49  VAL   B HG22 1 
ATOM   4794 H  HG23 . VAL   B 1 49  ? 48.048 -27.283 -1.051  1.00 17.24 ?  49  VAL   B HG23 1 
ATOM   4795 N  N    . ALA   B 1 50  ? 50.347 -23.822 1.258   1.00 11.07 ?  50  ALA   B N    1 
ATOM   4796 C  CA   . ALA   B 1 50  ? 50.868 -22.547 1.738   1.00 11.01 ?  50  ALA   B CA   1 
ATOM   4797 C  C    . ALA   B 1 50  ? 52.386 -22.581 1.847   1.00 11.28 ?  50  ALA   B C    1 
ATOM   4798 O  O    . ALA   B 1 50  ? 53.066 -21.614 1.478   1.00 11.19 ?  50  ALA   B O    1 
ATOM   4799 C  CB   . ALA   B 1 50  ? 50.231 -22.185 3.076   1.00 11.23 ?  50  ALA   B CB   1 
ATOM   4800 H  H    . ALA   B 1 50  ? 49.817 -24.224 1.802   1.00 13.29 ?  50  ALA   B H    1 
ATOM   4801 H  HA   . ALA   B 1 50  ? 50.642 -21.855 1.103   1.00 13.21 ?  50  ALA   B HA   1 
ATOM   4802 H  HB1  . ALA   B 1 50  ? 50.592 -21.335 3.379   1.00 13.48 ?  50  ALA   B HB1  1 
ATOM   4803 H  HB2  . ALA   B 1 50  ? 49.270 -22.110 2.957   1.00 13.48 ?  50  ALA   B HB2  1 
ATOM   4804 H  HB3  . ALA   B 1 50  ? 50.431 -22.878 3.723   1.00 13.48 ?  50  ALA   B HB3  1 
ATOM   4805 N  N    . GLY   B 1 51  ? 52.935 -23.678 2.362   1.00 11.87 ?  51  GLY   B N    1 
ATOM   4806 C  CA   . GLY   B 1 51  ? 54.378 -23.788 2.434   1.00 12.56 ?  51  GLY   B CA   1 
ATOM   4807 C  C    . GLY   B 1 51  ? 55.024 -23.729 1.066   1.00 12.30 ?  51  GLY   B C    1 
ATOM   4808 O  O    . GLY   B 1 51  ? 56.069 -23.096 0.890   1.00 13.16 ?  51  GLY   B O    1 
ATOM   4809 H  H    . GLY   B 1 51  ? 52.504 -24.363 2.658   1.00 14.25 ?  51  GLY   B H    1 
ATOM   4810 H  HA2  . GLY   B 1 51  ? 54.732 -23.061 2.969   1.00 15.08 ?  51  GLY   B HA2  1 
ATOM   4811 H  HA3  . GLY   B 1 51  ? 54.623 -24.628 2.855   1.00 15.08 ?  51  GLY   B HA3  1 
ATOM   4812 N  N    . ALA   B 1 52  ? 54.418 -24.388 0.081   1.00 12.08 ?  52  ALA   B N    1 
ATOM   4813 C  CA   . ALA   B 1 52  ? 54.985 -24.397 -1.260  1.00 12.36 ?  52  ALA   B CA   1 
ATOM   4814 C  C    . ALA   B 1 52  ? 54.904 -23.022 -1.911  1.00 11.84 ?  52  ALA   B C    1 
ATOM   4815 O  O    . ALA   B 1 52  ? 55.874 -22.572 -2.541  1.00 12.61 ?  52  ALA   B O    1 
ATOM   4816 C  CB   . ALA   B 1 52  ? 54.282 -25.442 -2.120  1.00 13.17 ?  52  ALA   B CB   1 
ATOM   4817 H  H    . ALA   B 1 52  ? 53.678 -24.825 0.162   1.00 14.50 ?  52  ALA   B H    1 
ATOM   4818 H  HA   . ALA   B 1 52  ? 55.917 -24.640 -1.199  1.00 14.84 ?  52  ALA   B HA   1 
ATOM   4819 H  HB1  . ALA   B 1 52  ? 54.677 -25.435 -3.008  1.00 15.81 ?  52  ALA   B HB1  1 
ATOM   4820 H  HB2  . ALA   B 1 52  ? 54.407 -26.317 -1.715  1.00 15.81 ?  52  ALA   B HB2  1 
ATOM   4821 H  HB3  . ALA   B 1 52  ? 53.340 -25.234 -2.174  1.00 15.81 ?  52  ALA   B HB3  1 
ATOM   4822 N  N    . LEU   B 1 53  ? 53.758 -22.346 -1.792  1.00 11.44 ?  53  LEU   B N    1 
ATOM   4823 C  CA   . LEU   B 1 53  ? 53.648 -21.006 -2.359  1.00 11.68 ?  53  LEU   B CA   1 
ATOM   4824 C  C    . LEU   B 1 53  ? 54.656 -20.068 -1.710  1.00 11.51 ?  53  LEU   B C    1 
ATOM   4825 O  O    . LEU   B 1 53  ? 55.360 -19.320 -2.397  1.00 12.32 ?  53  LEU   B O    1 
ATOM   4826 C  CB   . LEU   B 1 53  ? 52.228 -20.459 -2.187  1.00 12.00 ?  53  LEU   B CB   1 
ATOM   4827 C  CG   . LEU   B 1 53  ? 51.091 -21.186 -2.912  1.00 12.51 ?  53  LEU   B CG   1 
ATOM   4828 C  CD1  . LEU   B 1 53  ? 49.750 -20.578 -2.556  1.00 14.08 ?  53  LEU   B CD1  1 
ATOM   4829 C  CD2  . LEU   B 1 53  ? 51.292 -21.175 -4.421  1.00 14.25 ?  53  LEU   B CD2  1 
ATOM   4830 H  H    . LEU   B 1 53  ? 53.050 -22.630 -1.400  1.00 13.73 ?  53  LEU   B H    1 
ATOM   4831 H  HA   . LEU   B 1 53  ? 53.847 -21.048 -3.314  1.00 14.02 ?  53  LEU   B HA   1 
ATOM   4832 H  HB2  . LEU   B 1 53  ? 52.018 -20.475 -1.244  1.00 14.40 ?  53  LEU   B HB2  1 
ATOM   4833 H  HB3  . LEU   B 1 53  ? 52.222 -19.542 -2.502  1.00 14.40 ?  53  LEU   B HB3  1 
ATOM   4834 H  HG   . LEU   B 1 53  ? 51.074 -22.110 -2.624  1.00 15.01 ?  53  LEU   B HG   1 
ATOM   4835 H  HD11 . LEU   B 1 53  ? 49.048 -21.061 -3.023  1.00 16.90 ?  53  LEU   B HD11 1 
ATOM   4836 H  HD12 . LEU   B 1 53  ? 49.614 -20.654 -1.595  1.00 16.90 ?  53  LEU   B HD12 1 
ATOM   4837 H  HD13 . LEU   B 1 53  ? 49.742 -19.647 -2.817  1.00 16.90 ?  53  LEU   B HD13 1 
ATOM   4838 H  HD21 . LEU   B 1 53  ? 50.579 -21.687 -4.838  1.00 17.11 ?  53  LEU   B HD21 1 
ATOM   4839 H  HD22 . LEU   B 1 53  ? 51.263 -20.259 -4.737  1.00 17.11 ?  53  LEU   B HD22 1 
ATOM   4840 H  HD23 . LEU   B 1 53  ? 52.148 -21.575 -4.630  1.00 17.11 ?  53  LEU   B HD23 1 
ATOM   4841 N  N    . ASN   B 1 54  ? 54.748 -20.101 -0.383  1.00 11.44 ?  54  ASN   B N    1 
ATOM   4842 C  CA   . ASN   B 1 54  ? 55.662 -19.192 0.292   1.00 11.94 ?  54  ASN   B CA   1 
ATOM   4843 C  C    . ASN   B 1 54  ? 57.105 -19.468 -0.107  1.00 12.23 ?  54  ASN   B C    1 
ATOM   4844 O  O    . ASN   B 1 54  ? 57.880 -18.532 -0.343  1.00 12.62 ?  54  ASN   B O    1 
ATOM   4845 C  CB   . ASN   B 1 54  ? 55.506 -19.271 1.801   1.00 12.60 ?  54  ASN   B CB   1 
ATOM   4846 C  CG   . ASN   B 1 54  ? 56.480 -18.356 2.505   1.00 12.88 ?  54  ASN   B CG   1 
ATOM   4847 O  OD1  . ASN   B 1 54  ? 56.495 -17.145 2.260   1.00 13.07 ?  54  ASN   B OD1  1 
ATOM   4848 N  ND2  . ASN   B 1 54  ? 57.321 -18.926 3.359   1.00 14.33 ?  54  ASN   B ND2  1 
ATOM   4849 H  H    . ASN   B 1 54  ? 54.306 -20.631 0.129   1.00 13.73 ?  54  ASN   B H    1 
ATOM   4850 H  HA   . ASN   B 1 54  ? 55.447 -18.288 0.019   1.00 14.33 ?  54  ASN   B HA   1 
ATOM   4851 H  HB2  . ASN   B 1 54  ? 54.604 -19.002 2.043   1.00 15.13 ?  54  ASN   B HB2  1 
ATOM   4852 H  HB3  . ASN   B 1 54  ? 55.672 -20.181 2.093   1.00 15.13 ?  54  ASN   B HB3  1 
ATOM   4853 H  HD21 . ASN   B 1 54  ? 57.902 -18.449 3.779   1.00 17.20 ?  54  ASN   B HD21 1 
ATOM   4854 H  HD22 . ASN   B 1 54  ? 57.291 -19.777 3.495   1.00 17.20 ?  54  ASN   B HD22 1 
ATOM   4855 N  N    . LYS   B 1 55  ? 57.491 -20.746 -0.173  1.00 13.03 ?  55  LYS   B N    1 
ATOM   4856 C  CA   . LYS   B 1 55  ? 58.844 -21.089 -0.593  1.00 13.97 ?  55  LYS   B CA   1 
ATOM   4857 C  C    . LYS   B 1 55  ? 59.138 -20.545 -1.984  1.00 13.57 ?  55  LYS   B C    1 
ATOM   4858 O  O    . LYS   B 1 55  ? 60.236 -20.041 -2.237  1.00 14.08 ?  55  LYS   B O    1 
ATOM   4859 C  CB   . LYS   B 1 55  ? 59.035 -22.605 -0.545  1.00 15.50 ?  55  LYS   B CB   1 
ATOM   4860 C  CG   . LYS   B 1 55  ? 60.411 -23.071 -0.977  1.00 19.28 ?  55  LYS   B CG   1 
ATOM   4861 C  CD   . LYS   B 1 55  ? 60.575 -24.570 -0.799  1.00 22.62 ?  55  LYS   B CD   1 
ATOM   4862 C  CE   . LYS   B 1 55  ? 60.623 -24.965 0.675   1.00 25.39 ?  55  LYS   B CE   1 
ATOM   4863 N  NZ   . LYS   B 1 55  ? 61.030 -26.379 0.857   1.00 26.62 ?  55  LYS   B NZ   1 
ATOM   4864 H  H    . LYS   B 1 55  ? 56.990 -21.417 0.016   1.00 15.64 ?  55  LYS   B H    1 
ATOM   4865 H  HA   . LYS   B 1 55  ? 59.476 -20.688 0.020   1.00 16.76 ?  55  LYS   B HA   1 
ATOM   4866 H  HB2  . LYS   B 1 55  ? 58.892 -22.902 0.368   1.00 18.60 ?  55  LYS   B HB2  1 
ATOM   4867 H  HB3  . LYS   B 1 55  ? 58.385 -23.022 -1.130  1.00 18.60 ?  55  LYS   B HB3  1 
ATOM   4868 H  HG2  . LYS   B 1 55  ? 60.542 -22.863 -1.915  1.00 23.14 ?  55  LYS   B HG2  1 
ATOM   4869 H  HG3  . LYS   B 1 55  ? 61.085 -22.626 -0.439  1.00 23.14 ?  55  LYS   B HG3  1 
ATOM   4870 H  HD2  . LYS   B 1 55  ? 59.826 -25.030 -1.210  1.00 27.15 ?  55  LYS   B HD2  1 
ATOM   4871 H  HD3  . LYS   B 1 55  ? 61.408 -24.856 -1.212  1.00 27.15 ?  55  LYS   B HD3  1 
ATOM   4872 H  HE2  . LYS   B 1 55  ? 61.264 -24.395 1.133   1.00 30.47 ?  55  LYS   B HE2  1 
ATOM   4873 H  HE3  . LYS   B 1 55  ? 59.739 -24.846 1.062   1.00 30.47 ?  55  LYS   B HE3  1 
ATOM   4874 H  HZ1  . LYS   B 1 55  ? 61.009 -26.589 1.722   1.00 31.95 ?  55  LYS   B HZ1  1 
ATOM   4875 H  HZ2  . LYS   B 1 55  ? 60.471 -26.912 0.416   1.00 31.95 ?  55  LYS   B HZ2  1 
ATOM   4876 H  HZ3  . LYS   B 1 55  ? 61.853 -26.499 0.547   1.00 31.95 ?  55  LYS   B HZ3  1 
ATOM   4877 N  N    . ALA   B 1 56  ? 58.170 -20.636 -2.901  1.00 13.25 ?  56  ALA   B N    1 
ATOM   4878 C  CA   . ALA   B 1 56  ? 58.393 -20.133 -4.252  1.00 13.98 ?  56  ALA   B CA   1 
ATOM   4879 C  C    . ALA   B 1 56  ? 58.674 -18.638 -4.248  1.00 13.87 ?  56  ALA   B C    1 
ATOM   4880 O  O    . ALA   B 1 56  ? 59.406 -18.144 -5.116  1.00 14.88 ?  56  ALA   B O    1 
ATOM   4881 C  CB   . ALA   B 1 56  ? 57.196 -20.463 -5.145  1.00 14.77 ?  56  ALA   B CB   1 
ATOM   4882 H  H    . ALA   B 1 56  ? 57.385 -20.970 -2.766  1.00 15.91 ?  56  ALA   B H    1 
ATOM   4883 H  HA   . ALA   B 1 56  ? 59.170 -20.572 -4.621  1.00 16.78 ?  56  ALA   B HA   1 
ATOM   4884 H  HB1  . ALA   B 1 56  ? 57.369 -20.127 -6.041  1.00 17.73 ?  56  ALA   B HB1  1 
ATOM   4885 H  HB2  . ALA   B 1 56  ? 57.082 -21.427 -5.174  1.00 17.73 ?  56  ALA   B HB2  1 
ATOM   4886 H  HB3  . ALA   B 1 56  ? 56.401 -20.045 -4.784  1.00 17.73 ?  56  ALA   B HB3  1 
ATOM   4887 N  N    . THR   B 1 57  ? 58.104 -17.903 -3.290  1.00 13.62 ?  57  THR   B N    1 
ATOM   4888 C  CA   . THR   B 1 57  ? 58.341 -16.469 -3.164  1.00 13.37 ?  57  THR   B CA   1 
ATOM   4889 C  C    . THR   B 1 57  ? 59.592 -16.143 -2.355  1.00 14.40 ?  57  THR   B C    1 
ATOM   4890 O  O    . THR   B 1 57  ? 59.827 -14.968 -2.052  1.00 14.64 ?  57  THR   B O    1 
ATOM   4891 C  CB   . THR   B 1 57  ? 57.140 -15.742 -2.523  1.00 12.75 ?  57  THR   B CB   1 
ATOM   4892 O  OG1  . THR   B 1 57  ? 57.126 -15.953 -1.104  1.00 12.93 ?  57  THR   B OG1  1 
ATOM   4893 C  CG2  . THR   B 1 57  ? 55.816 -16.157 -3.154  1.00 12.87 ?  57  THR   B CG2  1 
ATOM   4894 H  H    . THR   B 1 57  ? 57.557 -18.215 -2.699  1.00 16.35 ?  57  THR   B H    1 
ATOM   4895 H  HA   . THR   B 1 57  ? 58.459 -16.098 -4.051  1.00 16.05 ?  57  THR   B HA   1 
ATOM   4896 H  HB   . THR   B 1 57  ? 57.242 -14.790 -2.689  1.00 15.30 ?  57  THR   B HB   1 
ATOM   4897 H  HG1  . THR   B 1 57  ? 57.058 -16.773 -0.939  1.00 15.53 ?  57  THR   B HG1  1 
ATOM   4898 H  HG21 . THR   B 1 57  ? 55.091 -15.630 -2.786  1.00 15.45 ?  57  THR   B HG21 1 
ATOM   4899 H  HG22 . THR   B 1 57  ? 55.847 -16.024 -4.115  1.00 15.45 ?  57  THR   B HG22 1 
ATOM   4900 H  HG23 . THR   B 1 57  ? 55.643 -17.095 -2.976  1.00 15.45 ?  57  THR   B HG23 1 
ATOM   4901 N  N    . ASN   B 1 58  ? 60.386 -17.148 -1.991  1.00 15.17 ?  58  ASN   B N    1 
ATOM   4902 C  CA   . ASN   B 1 58  ? 61.582 -16.934 -1.183  1.00 18.29 ?  58  ASN   B CA   1 
ATOM   4903 C  C    . ASN   B 1 58  ? 61.243 -16.222 0.126   1.00 15.77 ?  58  ASN   B C    1 
ATOM   4904 O  O    . ASN   B 1 58  ? 61.981 -15.352 0.595   1.00 16.43 ?  58  ASN   B O    1 
ATOM   4905 C  CB   . ASN   B 1 58  ? 62.666 -16.184 -1.964  1.00 26.51 ?  58  ASN   B CB   1 
ATOM   4906 C  CG   . ASN   B 1 58  ? 64.038 -16.325 -1.336  1.00 35.28 ?  58  ASN   B CG   1 
ATOM   4907 O  OD1  . ASN   B 1 58  ? 64.342 -17.337 -0.704  1.00 37.73 ?  58  ASN   B OD1  1 
ATOM   4908 N  ND2  . ASN   B 1 58  ? 64.874 -15.308 -1.504  1.00 41.35 ?  58  ASN   B ND2  1 
ATOM   4909 H  H    . ASN   B 1 58  ? 60.248 -17.973 -2.199  1.00 18.20 ?  58  ASN   B H    1 
ATOM   4910 H  HA   . ASN   B 1 58  ? 61.948 -17.804 -0.957  1.00 21.95 ?  58  ASN   B HA   1 
ATOM   4911 H  HB2  . ASN   B 1 58  ? 62.710 -16.539 -2.868  1.00 31.82 ?  58  ASN   B HB2  1 
ATOM   4912 H  HB3  . ASN   B 1 58  ? 62.444 -15.241 -1.990  1.00 31.82 ?  58  ASN   B HB3  1 
ATOM   4913 H  HD21 . ASN   B 1 58  ? 65.664 -15.342 -1.167  1.00 49.62 ?  58  ASN   B HD21 1 
ATOM   4914 H  HD22 . ASN   B 1 58  ? 64.625 -14.617 -1.949  1.00 49.62 ?  58  ASN   B HD22 1 
ATOM   4915 N  N    . ASN   B 1 59  ? 60.115 -16.602 0.725   1.00 14.88 ?  59  ASN   B N    1 
ATOM   4916 C  CA   . ASN   B 1 59  ? 59.640 -16.127 2.023   1.00 14.46 ?  59  ASN   B CA   1 
ATOM   4917 C  C    . ASN   B 1 59  ? 59.046 -14.722 1.964   1.00 13.96 ?  59  ASN   B C    1 
ATOM   4918 O  O    . ASN   B 1 59  ? 58.609 -14.218 3.006   1.00 13.95 ?  59  ASN   B O    1 
ATOM   4919 C  CB   . ASN   B 1 59  ? 60.713 -16.177 3.125   1.00 15.53 ?  59  ASN   B CB   1 
ATOM   4920 C  CG   . ASN   B 1 59  ? 60.128 -16.359 4.508   1.00 16.42 ?  59  ASN   B CG   1 
ATOM   4921 O  OD1  . ASN   B 1 59  ? 59.302 -17.247 4.738   1.00 16.73 ?  59  ASN   B OD1  1 
ATOM   4922 N  ND2  . ASN   B 1 59  ? 60.552 -15.516 5.442   1.00 17.11 ?  59  ASN   B ND2  1 
ATOM   4923 H  H    . ASN   B 1 59  ? 59.573 -17.180 0.380   1.00 17.87 ?  59  ASN   B H    1 
ATOM   4924 H  HA   . ASN   B 1 59  ? 58.931 -16.719 2.310   1.00 17.36 ?  59  ASN   B HA   1 
ATOM   4925 H  HB2  . ASN   B 1 59  ? 61.310 -16.923 2.958   1.00 18.64 ?  59  ASN   B HB2  1 
ATOM   4926 H  HB3  . ASN   B 1 59  ? 61.213 -15.346 3.126   1.00 18.64 ?  59  ASN   B HB3  1 
ATOM   4927 H  HD21 . ASN   B 1 59  ? 60.249 -15.578 6.245   1.00 20.53 ?  59  ASN   B HD21 1 
ATOM   4928 H  HD22 . ASN   B 1 59  ? 61.125 -14.908 5.244   1.00 20.53 ?  59  ASN   B HD22 1 
ATOM   4929 N  N    . ALA   B 1 60  ? 58.989 -14.081 0.794   1.00 13.63 ?  60  ALA   B N    1 
ATOM   4930 C  CA   . ALA   B 1 60  ? 58.393 -12.749 0.718   1.00 13.52 ?  60  ALA   B CA   1 
ATOM   4931 C  C    . ALA   B 1 60  ? 56.925 -12.775 1.120   1.00 12.78 ?  60  ALA   B C    1 
ATOM   4932 O  O    . ALA   B 1 60  ? 56.423 -11.824 1.733   1.00 13.23 ?  60  ALA   B O    1 
ATOM   4933 C  CB   . ALA   B 1 60  ? 58.554 -12.174 -0.689  1.00 14.56 ?  60  ALA   B CB   1 
ATOM   4934 H  H    . ALA   B 1 60  ? 59.283 -14.394 0.050   1.00 16.36 ?  60  ALA   B H    1 
ATOM   4935 H  HA   . ALA   B 1 60  ? 58.856 -12.167 1.336   1.00 16.23 ?  60  ALA   B HA   1 
ATOM   4936 H  HB1  . ALA   B 1 60  ? 58.154 -11.294 -0.716  1.00 17.47 ?  60  ALA   B HB1  1 
ATOM   4937 H  HB2  . ALA   B 1 60  ? 59.501 -12.117 -0.898  1.00 17.47 ?  60  ALA   B HB2  1 
ATOM   4938 H  HB3  . ALA   B 1 60  ? 58.113 -12.762 -1.323  1.00 17.47 ?  60  ALA   B HB3  1 
ATOM   4939 N  N    . MET   B 1 61  ? 56.217 -13.851 0.772   1.00 12.05 ?  61  MET   B N    1 
ATOM   4940 C  CA   . MET   B 1 61  ? 54.821 -13.976 1.167   1.00 11.83 ?  61  MET   B CA   1 
ATOM   4941 C  C    . MET   B 1 61  ? 54.682 -13.983 2.688   1.00 11.97 ?  61  MET   B C    1 
ATOM   4942 O  O    . MET   B 1 61  ? 53.782 -13.334 3.239   1.00 11.93 ?  61  MET   B O    1 
ATOM   4943 C  CB   . MET   B 1 61  ? 54.244 -15.246 0.537   1.00 11.62 ?  61  MET   B CB   1 
ATOM   4944 C  CG   . MET   B 1 61  ? 52.805 -15.535 0.952   1.00 11.43 ?  61  MET   B CG   1 
ATOM   4945 S  SD   . MET   B 1 61  ? 52.156 -17.031 0.186   1.00 12.29 ?  61  MET   B SD   1 
ATOM   4946 C  CE   . MET   B 1 61  ? 51.894 -16.439 -1.484  1.00 13.50 ?  61  MET   B CE   1 
ATOM   4947 H  H    . MET   B 1 61  ? 56.523 -14.523 0.316   1.00 14.46 ?  61  MET   B H    1 
ATOM   4948 H  HA   . MET   B 1 61  ? 54.329 -13.225 0.804   1.00 14.20 ?  61  MET   B HA   1 
ATOM   4949 H  HB2  . MET   B 1 61  ? 54.258 -15.154 -0.432  1.00 13.95 ?  61  MET   B HB2  1 
ATOM   4950 H  HB3  . MET   B 1 61  ? 54.787 -16.005 0.799   1.00 13.95 ?  61  MET   B HB3  1 
ATOM   4951 H  HG2  . MET   B 1 61  ? 52.768 -15.657 1.915   1.00 13.72 ?  61  MET   B HG2  1 
ATOM   4952 H  HG3  . MET   B 1 61  ? 52.242 -14.788 0.692   1.00 13.72 ?  61  MET   B HG3  1 
ATOM   4953 H  HE1  . MET   B 1 61  ? 51.507 -17.154 -2.014  1.00 16.21 ?  61  MET   B HE1  1 
ATOM   4954 H  HE2  . MET   B 1 61  ? 51.290 -15.680 -1.461  1.00 16.21 ?  61  MET   B HE2  1 
ATOM   4955 H  HE3  . MET   B 1 61  ? 52.746 -16.172 -1.863  1.00 16.21 ?  61  MET   B HE3  1 
ATOM   4956 N  N    . GLN   B 1 62  ? 55.568 -14.696 3.388   1.00 12.07 ?  62  GLN   B N    1 
ATOM   4957 C  CA   . GLN   B 1 62  ? 55.458 -14.756 4.842   1.00 12.19 ?  62  GLN   B CA   1 
ATOM   4958 C  C    . GLN   B 1 62  ? 55.739 -13.401 5.476   1.00 12.32 ?  62  GLN   B C    1 
ATOM   4959 O  O    . GLN   B 1 62  ? 55.053 -12.999 6.422   1.00 12.97 ?  62  GLN   B O    1 
ATOM   4960 C  CB   . GLN   B 1 62  ? 56.408 -15.811 5.411   1.00 12.83 ?  62  GLN   B CB   1 
ATOM   4961 C  CG   . GLN   B 1 62  ? 56.178 -16.077 6.888   1.00 12.86 ?  62  GLN   B CG   1 
ATOM   4962 C  CD   . GLN   B 1 62  ? 54.803 -16.670 7.130   1.00 12.33 ?  62  GLN   B CD   1 
ATOM   4963 O  OE1  . GLN   B 1 62  ? 54.546 -17.821 6.769   1.00 12.80 ?  62  GLN   B OE1  1 
ATOM   4964 N  NE2  . GLN   B 1 62  ? 53.896 -15.879 7.695   1.00 12.89 ?  62  GLN   B NE2  1 
ATOM   4965 H  H    . GLN   B 1 62  ? 56.218 -15.148 3.045   1.00 14.48 ?  62  GLN   B H    1 
ATOM   4966 H  HA   . GLN   B 1 62  ? 54.553 -15.012 5.071   1.00 14.63 ?  62  GLN   B HA   1 
ATOM   4967 H  HB2  . GLN   B 1 62  ? 56.278 -16.648 4.935   1.00 15.40 ?  62  GLN   B HB2  1 
ATOM   4968 H  HB3  . GLN   B 1 62  ? 57.323 -15.508 5.299   1.00 15.40 ?  62  GLN   B HB3  1 
ATOM   4969 H  HG2  . GLN   B 1 62  ? 56.844 -16.709 7.204   1.00 15.44 ?  62  GLN   B HG2  1 
ATOM   4970 H  HG3  . GLN   B 1 62  ? 56.247 -15.244 7.380   1.00 15.44 ?  62  GLN   B HG3  1 
ATOM   4971 H  HE21 . GLN   B 1 62  ? 54.105 -15.075 7.921   1.00 15.48 ?  62  GLN   B HE21 1 
ATOM   4972 H  HE22 . GLN   B 1 62  ? 53.102 -16.173 7.842   1.00 15.48 ?  62  GLN   B HE22 1 
ATOM   4973 N  N    . VAL   B 1 63  ? 56.755 -12.692 4.986   1.00 12.96 ?  63  VAL   B N    1 
ATOM   4974 C  CA   . VAL   B 1 63  ? 57.061 -11.374 5.539   1.00 13.88 ?  63  VAL   B CA   1 
ATOM   4975 C  C    . VAL   B 1 63  ? 55.867 -10.441 5.359   1.00 13.21 ?  63  VAL   B C    1 
ATOM   4976 O  O    . VAL   B 1 63  ? 55.450 -9.737  6.292   1.00 13.87 ?  63  VAL   B O    1 
ATOM   4977 C  CB   . VAL   B 1 63  ? 58.349 -10.817 4.909   1.00 15.04 ?  63  VAL   B CB   1 
ATOM   4978 C  CG1  . VAL   B 1 63  ? 58.578 -9.381  5.356   1.00 15.82 ?  63  VAL   B CG1  1 
ATOM   4979 C  CG2  . VAL   B 1 63  ? 59.535 -11.694 5.296   1.00 15.77 ?  63  VAL   B CG2  1 
ATOM   4980 H  H    . VAL   B 1 63  ? 57.268 -12.942 4.334   1.00 15.56 ?  63  VAL   B H    1 
ATOM   4981 H  HA   . VAL   B 1 63  ? 57.221 -11.473 6.486   1.00 16.66 ?  63  VAL   B HA   1 
ATOM   4982 H  HB   . VAL   B 1 63  ? 58.275 -10.829 3.942   1.00 18.05 ?  63  VAL   B HB   1 
ATOM   4983 H  HG11 . VAL   B 1 63  ? 59.497 -9.136  5.170   1.00 18.98 ?  63  VAL   B HG11 1 
ATOM   4984 H  HG12 . VAL   B 1 63  ? 57.974 -8.801  4.871   1.00 18.98 ?  63  VAL   B HG12 1 
ATOM   4985 H  HG13 . VAL   B 1 63  ? 58.407 -9.321  6.310   1.00 18.98 ?  63  VAL   B HG13 1 
ATOM   4986 H  HG21 . VAL   B 1 63  ? 60.347 -11.320 4.917   1.00 18.92 ?  63  VAL   B HG21 1 
ATOM   4987 H  HG22 . VAL   B 1 63  ? 59.608 -11.718 6.266   1.00 18.92 ?  63  VAL   B HG22 1 
ATOM   4988 H  HG23 . VAL   B 1 63  ? 59.395 -12.591 4.956   1.00 18.92 ?  63  VAL   B HG23 1 
ATOM   4989 N  N    . GLU   B 1 64  ? 55.298 -10.428 4.153   1.00 12.72 ?  64  GLU   B N    1 
ATOM   4990 C  CA   . GLU   B 1 64  ? 54.136 -9.587  3.882   1.00 12.48 ?  64  GLU   B CA   1 
ATOM   4991 C  C    . GLU   B 1 64  ? 52.955 -9.989  4.756   1.00 12.06 ?  64  GLU   B C    1 
ATOM   4992 O  O    . GLU   B 1 64  ? 52.206 -9.130  5.250   1.00 12.67 ?  64  GLU   B O    1 
ATOM   4993 C  CB   . GLU   B 1 64  ? 53.775 -9.726  2.402   1.00 12.68 ?  64  GLU   B CB   1 
ATOM   4994 C  CG   . GLU   B 1 64  ? 52.505 -9.014  1.975   1.00 12.97 ?  64  GLU   B CG   1 
ATOM   4995 C  CD   . GLU   B 1 64  ? 51.977 -9.513  0.636   1.00 13.58 ?  64  GLU   B CD   1 
ATOM   4996 O  OE1  . GLU   B 1 64  ? 52.163 -10.719 0.320   1.00 14.26 ?  64  GLU   B OE1  1 
ATOM   4997 O  OE2  . GLU   B 1 64  ? 51.354 -8.699  -0.090  1.00 14.18 -1 64  GLU   B OE2  1 
ATOM   4998 H  H    . GLU   B 1 64  ? 55.574 -10.886 3.475   1.00 15.27 ?  64  GLU   B H    1 
ATOM   4999 H  HA   . GLU   B 1 64  ? 54.352 -8.661  4.060   1.00 14.98 ?  64  GLU   B HA   1 
ATOM   5000 H  HB2  . GLU   B 1 64  ? 54.498 -9.355  1.868   1.00 15.23 ?  64  GLU   B HB2  1 
ATOM   5001 H  HB3  . GLU   B 1 64  ? 53.667 -10.663 2.195   1.00 15.23 ?  64  GLU   B HB3  1 
ATOM   5002 H  HG2  . GLU   B 1 64  ? 51.804 -9.159  2.636   1.00 15.57 ?  64  GLU   B HG2  1 
ATOM   5003 H  HG3  . GLU   B 1 64  ? 52.681 -8.063  1.894   1.00 15.57 ?  64  GLU   B HG3  1 
ATOM   5004 N  N    . SER   B 1 65  ? 52.772 -11.296 4.945   1.00 11.95 ?  65  SER   B N    1 
ATOM   5005 C  CA   . SER   B 1 65  ? 51.659 -11.802 5.736   1.00 11.97 ?  65  SER   B CA   1 
ATOM   5006 C  C    . SER   B 1 65  ? 51.792 -11.406 7.200   1.00 12.37 ?  65  SER   B C    1 
ATOM   5007 O  O    . SER   B 1 65  ? 50.793 -11.037 7.836   1.00 12.44 ?  65  SER   B O    1 
ATOM   5008 C  CB   . SER   B 1 65  ? 51.585 -13.322 5.606   1.00 12.00 ?  65  SER   B CB   1 
ATOM   5009 O  OG   . SER   B 1 65  ? 51.233 -13.726 4.290   1.00 12.31 ?  65  SER   B OG   1 
ATOM   5010 H  H    . SER   B 1 65  ? 53.280 -11.916 4.622   1.00 14.35 ?  65  SER   B H    1 
ATOM   5011 H  HA   . SER   B 1 65  ? 50.827 -11.432 5.398   1.00 14.37 ?  65  SER   B HA   1 
ATOM   5012 H  HB2  . SER   B 1 65  ? 52.445 -13.700 5.828   1.00 14.41 ?  65  SER   B HB2  1 
ATOM   5013 H  HB3  . SER   B 1 65  ? 50.909 -13.656 6.225   1.00 14.41 ?  65  SER   B HB3  1 
ATOM   5014 H  HG   . SER   B 1 65  ? 51.802 -13.439 3.740   1.00 14.78 ?  65  SER   B HG   1 
ATOM   5015 N  N    . ASP   B 1 66  ? 53.001 -11.505 7.765   1.00 12.61 ?  66  ASP   B N    1 
ATOM   5016 C  CA   . ASP   B 1 66  ? 53.184 -11.114 9.159   1.00 12.79 ?  66  ASP   B CA   1 
ATOM   5017 C  C    . ASP   B 1 66  ? 52.876 -9.634  9.356   1.00 12.89 ?  66  ASP   B C    1 
ATOM   5018 O  O    . ASP   B 1 66  ? 52.295 -9.244  10.375  1.00 13.44 ?  66  ASP   B O    1 
ATOM   5019 C  CB   . ASP   B 1 66  ? 54.610 -11.425 9.614   1.00 13.89 ?  66  ASP   B CB   1 
ATOM   5020 C  CG   . ASP   B 1 66  ? 54.875 -12.916 9.769   1.00 15.84 ?  66  ASP   B CG   1 
ATOM   5021 O  OD1  . ASP   B 1 66  ? 53.923 -13.726 9.686   1.00 16.40 ?  66  ASP   B OD1  1 
ATOM   5022 O  OD2  . ASP   B 1 66  ? 56.051 -13.281 9.992   1.00 18.34 -1 66  ASP   B OD2  1 
ATOM   5023 H  H    . ASP   B 1 66  ? 53.704 -11.800 7.375   1.00 15.14 ?  66  ASP   B H    1 
ATOM   5024 H  HA   . ASP   B 1 66  ? 52.577 -11.619 9.721   1.00 15.35 ?  66  ASP   B HA   1 
ATOM   5025 H  HB2  . ASP   B 1 66  ? 55.236 -11.081 8.958   1.00 16.68 ?  66  ASP   B HB2  1 
ATOM   5026 H  HB3  . ASP   B 1 66  ? 54.770 -10.998 10.475  1.00 16.68 ?  66  ASP   B HB3  1 
ATOM   5027 N  N    . ASP   B 1 67  ? 53.251 -8.794  8.390   1.00 12.50 ?  67  ASP   B N    1 
ATOM   5028 C  CA   . ASP   B 1 67  ? 52.906 -7.381  8.474   1.00 13.13 ?  67  ASP   B CA   1 
ATOM   5029 C  C    . ASP   B 1 67  ? 51.396 -7.171  8.389   1.00 13.25 ?  67  ASP   B C    1 
ATOM   5030 O  O    . ASP   B 1 67  ? 50.836 -6.355  9.132   1.00 13.99 ?  67  ASP   B O    1 
ATOM   5031 C  CB   . ASP   B 1 67  ? 53.625 -6.614  7.370   1.00 14.34 ?  67  ASP   B CB   1 
ATOM   5032 C  CG   . ASP   B 1 67  ? 53.197 -5.172  7.315   1.00 15.79 ?  67  ASP   B CG   1 
ATOM   5033 O  OD1  . ASP   B 1 67  ? 53.689 -4.355  8.128   1.00 16.90 ?  67  ASP   B OD1  1 
ATOM   5034 O  OD2  . ASP   B 1 67  ? 52.331 -4.879  6.475   1.00 16.97 -1 67  ASP   B OD2  1 
ATOM   5035 H  H    . ASP   B 1 67  ? 53.705 -9.015  7.693   1.00 15.00 ?  67  ASP   B H    1 
ATOM   5036 H  HA   . ASP   B 1 67  ? 53.210 -7.031  9.324   1.00 15.76 ?  67  ASP   B HA   1 
ATOM   5037 H  HB2  . ASP   B 1 67  ? 54.583 -6.637  7.536   1.00 17.21 ?  67  ASP   B HB2  1 
ATOM   5038 H  HB3  . ASP   B 1 67  ? 53.433 -7.033  6.512   1.00 17.21 ?  67  ASP   B HB3  1 
ATOM   5039 N  N    . TYR   B 1 68  ? 50.717 -7.904  7.499   1.00 13.09 ?  68  TYR   B N    1 
ATOM   5040 C  CA   . TYR   B 1 68  ? 49.260 -7.829  7.426   1.00 13.67 ?  68  TYR   B CA   1 
ATOM   5041 C  C    . TYR   B 1 68  ? 48.625 -8.169  8.771   1.00 13.04 ?  68  TYR   B C    1 
ATOM   5042 O  O    . TYR   B 1 68  ? 47.697 -7.485  9.220   1.00 13.95 ?  68  TYR   B O    1 
ATOM   5043 C  CB   . TYR   B 1 68  ? 48.728 -8.763  6.330   1.00 14.47 ?  68  TYR   B CB   1 
ATOM   5044 C  CG   . TYR   B 1 68  ? 47.224 -8.916  6.388   1.00 15.39 ?  68  TYR   B CG   1 
ATOM   5045 C  CD1  . TYR   B 1 68  ? 46.637 -9.871  7.211   1.00 16.36 ?  68  TYR   B CD1  1 
ATOM   5046 C  CD2  . TYR   B 1 68  ? 46.392 -8.074  5.667   1.00 16.51 ?  68  TYR   B CD2  1 
ATOM   5047 C  CE1  . TYR   B 1 68  ? 45.271 -9.995  7.302   1.00 17.31 ?  68  TYR   B CE1  1 
ATOM   5048 C  CE2  . TYR   B 1 68  ? 45.009 -8.198  5.746   1.00 16.78 ?  68  TYR   B CE2  1 
ATOM   5049 C  CZ   . TYR   B 1 68  ? 44.467 -9.156  6.570   1.00 17.04 ?  68  TYR   B CZ   1 
ATOM   5050 O  OH   . TYR   B 1 68  ? 43.100 -9.271  6.664   1.00 18.02 ?  68  TYR   B OH   1 
ATOM   5051 H  H    . TYR   B 1 68  ? 51.078 -8.459  6.938   1.00 15.71 ?  68  TYR   B H    1 
ATOM   5052 H  HA   . TYR   B 1 68  ? 49.012 -6.924  7.197   1.00 16.41 ?  68  TYR   B HA   1 
ATOM   5053 H  HB2  . TYR   B 1 68  ? 48.955 -8.396  5.464   1.00 17.37 ?  68  TYR   B HB2  1 
ATOM   5054 H  HB3  . TYR   B 1 68  ? 49.121 -9.641  6.439   1.00 17.37 ?  68  TYR   B HB3  1 
ATOM   5055 H  HD1  . TYR   B 1 68  ? 47.178 -10.442 7.710   1.00 19.64 ?  68  TYR   B HD1  1 
ATOM   5056 H  HD2  . TYR   B 1 68  ? 46.765 -7.418  5.126   1.00 19.81 ?  68  TYR   B HD2  1 
ATOM   5057 H  HE1  . TYR   B 1 68  ? 44.890 -10.652 7.845   1.00 20.78 ?  68  TYR   B HE1  1 
ATOM   5058 H  HE2  . TYR   B 1 68  ? 44.457 -7.630  5.261   1.00 20.14 ?  68  TYR   B HE2  1 
ATOM   5059 H  HH   . TYR   B 1 68  ? 42.716 -8.713  6.156   1.00 21.63 ?  68  TYR   B HH   1 
ATOM   5060 N  N    . ILE   B 1 69  ? 49.104 -9.235  9.419   1.00 12.80 ?  69  ILE   B N    1 
ATOM   5061 C  CA   . ILE   B 1 69  ? 48.547 -9.658  10.701  1.00 13.36 ?  69  ILE   B CA   1 
ATOM   5062 C  C    . ILE   B 1 69  ? 48.803 -8.610  11.775  1.00 13.14 ?  69  ILE   B C    1 
ATOM   5063 O  O    . ILE   B 1 69  ? 47.935 -8.336  12.610  1.00 13.59 ?  69  ILE   B O    1 
ATOM   5064 C  CB   . ILE   B 1 69  ? 49.123 -11.030 11.099  1.00 14.21 ?  69  ILE   B CB   1 
ATOM   5065 C  CG1  . ILE   B 1 69  ? 48.596 -12.134 10.174  1.00 14.68 ?  69  ILE   B CG1  1 
ATOM   5066 C  CG2  . ILE   B 1 69  ? 48.837 -11.342 12.565  1.00 15.16 ?  69  ILE   B CG2  1 
ATOM   5067 C  CD1  . ILE   B 1 69  ? 47.118 -12.438 10.327  1.00 15.08 ?  69  ILE   B CD1  1 
ATOM   5068 H  H    . ILE   B 1 69  ? 49.754 -9.725  9.142   1.00 15.36 ?  69  ILE   B H    1 
ATOM   5069 H  HA   . ILE   B 1 69  ? 47.589 -9.753  10.607  1.00 16.04 ?  69  ILE   B HA   1 
ATOM   5070 H  HB   . ILE   B 1 69  ? 50.088 -10.988 10.993  1.00 17.05 ?  69  ILE   B HB   1 
ATOM   5071 H  HG12 . ILE   B 1 69  ? 48.751 -11.861 9.254   1.00 17.62 ?  69  ILE   B HG12 1 
ATOM   5072 H  HG13 . ILE   B 1 69  ? 49.090 -12.949 10.356  1.00 17.62 ?  69  ILE   B HG13 1 
ATOM   5073 H  HG21 . ILE   B 1 69  ? 48.976 -12.291 12.714  1.00 18.19 ?  69  ILE   B HG21 1 
ATOM   5074 H  HG22 . ILE   B 1 69  ? 49.442 -10.831 13.126  1.00 18.19 ?  69  ILE   B HG22 1 
ATOM   5075 H  HG23 . ILE   B 1 69  ? 47.918 -11.108 12.764  1.00 18.19 ?  69  ILE   B HG23 1 
ATOM   5076 H  HD11 . ILE   B 1 69  ? 46.888 -13.161 9.725   1.00 18.11 ?  69  ILE   B HD11 1 
ATOM   5077 H  HD12 . ILE   B 1 69  ? 46.944 -12.701 11.243  1.00 18.11 ?  69  ILE   B HD12 1 
ATOM   5078 H  HD13 . ILE   B 1 69  ? 46.607 -11.646 10.104  1.00 18.11 ?  69  ILE   B HD13 1 
ATOM   5079 N  N    . ALA   B 1 70  ? 49.997 -8.021  11.793  1.00 13.43 ?  70  ALA   B N    1 
ATOM   5080 C  CA   . ALA   B 1 70  ? 50.280 -6.986  12.783  1.00 13.13 ?  70  ALA   B CA   1 
ATOM   5081 C  C    . ALA   B 1 70  ? 49.285 -5.840  12.672  1.00 13.47 ?  70  ALA   B C    1 
ATOM   5082 O  O    . ALA   B 1 70  ? 48.844 -5.289  13.685  1.00 13.69 ?  70  ALA   B O    1 
ATOM   5083 C  CB   . ALA   B 1 70  ? 51.709 -6.478  12.611  1.00 13.56 ?  70  ALA   B CB   1 
ATOM   5084 H  H    . ALA   B 1 70  ? 50.638 -8.196  11.257  1.00 16.12 ?  70  ALA   B H    1 
ATOM   5085 H  HA   . ALA   B 1 70  ? 50.203 -7.366  13.672  1.00 15.76 ?  70  ALA   B HA   1 
ATOM   5086 H  HB1  . ALA   B 1 70  ? 51.897 -5.820  13.299  1.00 16.28 ?  70  ALA   B HB1  1 
ATOM   5087 H  HB2  . ALA   B 1 70  ? 52.324 -7.226  12.695  1.00 16.28 ?  70  ALA   B HB2  1 
ATOM   5088 H  HB3  . ALA   B 1 70  ? 51.801 -6.076  11.733  1.00 16.28 ?  70  ALA   B HB3  1 
ATOM   5089 N  N    . THR   B 1 71  ? 48.906 -5.482  11.448  1.00 13.98 ?  71  THR   B N    1 
ATOM   5090 C  CA   . THR   B 1 71  ? 48.015 -4.348  11.236  1.00 14.95 ?  71  THR   B CA   1 
ATOM   5091 C  C    . THR   B 1 71  ? 46.548 -4.713  11.442  1.00 15.71 ?  71  THR   B C    1 
ATOM   5092 O  O    . THR   B 1 71  ? 45.770 -3.892  11.949  1.00 17.02 ?  71  THR   B O    1 
ATOM   5093 C  CB   . THR   B 1 71  ? 48.233 -3.785  9.829   1.00 16.77 ?  71  THR   B CB   1 
ATOM   5094 O  OG1  . THR   B 1 71  ? 49.558 -3.249  9.733   1.00 18.74 ?  71  THR   B OG1  1 
ATOM   5095 C  CG2  . THR   B 1 71  ? 47.212 -2.698  9.503   1.00 17.98 ?  71  THR   B CG2  1 
ATOM   5096 H  H    . THR   B 1 71  ? 49.154 -5.879  10.726  1.00 16.78 ?  71  THR   B H    1 
ATOM   5097 H  HA   . THR   B 1 71  ? 48.239 -3.650  11.868  1.00 17.95 ?  71  THR   B HA   1 
ATOM   5098 H  HB   . THR   B 1 71  ? 48.144 -4.492  9.174   1.00 20.13 ?  71  THR   B HB   1 
ATOM   5099 H  HG1  . THR   B 1 71  ? 49.687 -2.912  8.969   1.00 22.49 ?  71  THR   B HG1  1 
ATOM   5100 H  HG21 . THR   B 1 71  ? 47.515 -2.173  8.742   1.00 21.58 ?  71  THR   B HG21 1 
ATOM   5101 H  HG22 . THR   B 1 71  ? 46.357 -3.097  9.286   1.00 21.58 ?  71  THR   B HG22 1 
ATOM   5102 H  HG23 . THR   B 1 71  ? 47.103 -2.105  10.264  1.00 21.58 ?  71  THR   B HG23 1 
ATOM   5103 N  N    . ASN   B 1 72  ? 46.153 -5.932  11.056  1.00 15.27 ?  72  ASN   B N    1 
ATOM   5104 C  CA   . ASN   B 1 72  ? 44.749 -6.294  10.929  1.00 15.82 ?  72  ASN   B CA   1 
ATOM   5105 C  C    . ASN   B 1 72  ? 44.281 -7.392  11.875  1.00 16.11 ?  72  ASN   B C    1 
ATOM   5106 O  O    . ASN   B 1 72  ? 43.066 -7.550  12.046  1.00 17.29 ?  72  ASN   B O    1 
ATOM   5107 C  CB   . ASN   B 1 72  ? 44.448 -6.726  9.485   1.00 16.65 ?  72  ASN   B CB   1 
ATOM   5108 C  CG   . ASN   B 1 72  ? 44.724 -5.626  8.486   1.00 17.51 ?  72  ASN   B CG   1 
ATOM   5109 O  OD1  . ASN   B 1 72  ? 45.737 -5.638  7.781   1.00 18.77 ?  72  ASN   B OD1  1 
ATOM   5110 N  ND2  . ASN   B 1 72  ? 43.844 -4.643  8.448   1.00 19.19 ?  72  ASN   B ND2  1 
ATOM   5111 H  H    . ASN   B 1 72  ? 46.697 -6.575  10.858  1.00 18.33 ?  72  ASN   B H    1 
ATOM   5112 H  HA   . ASN   B 1 72  ? 44.217 -5.509  11.113  1.00 18.99 ?  72  ASN   B HA   1 
ATOM   5113 H  HB2  . ASN   B 1 72  ? 45.010 -7.485  9.255   1.00 19.99 ?  72  ASN   B HB2  1 
ATOM   5114 H  HB3  . ASN   B 1 72  ? 43.514 -6.969  9.415   1.00 19.99 ?  72  ASN   B HB3  1 
ATOM   5115 H  HD21 . ASN   B 1 72  ? 43.947 -3.988  7.898   1.00 23.04 ?  72  ASN   B HD21 1 
ATOM   5116 H  HD22 . ASN   B 1 72  ? 43.148 -4.665  8.957   1.00 23.04 ?  72  ASN   B HD22 1 
ATOM   5117 N  N    . GLY   B 1 73  ? 45.187 -8.146  12.493  1.00 15.55 ?  73  GLY   B N    1 
ATOM   5118 C  CA   . GLY   B 1 73  ? 44.794 -9.287  13.283  1.00 15.05 ?  73  GLY   B CA   1 
ATOM   5119 C  C    . GLY   B 1 73  ? 44.425 -10.469 12.412  1.00 13.88 ?  73  GLY   B C    1 
ATOM   5120 O  O    . GLY   B 1 73  ? 44.412 -10.384 11.181  1.00 13.77 ?  73  GLY   B O    1 
ATOM   5121 H  H    . GLY   B 1 73  ? 46.038 -8.012  12.465  1.00 18.66 ?  73  GLY   B H    1 
ATOM   5122 H  HA2  . GLY   B 1 73  ? 45.525 -9.545  13.868  1.00 18.07 ?  73  GLY   B HA2  1 
ATOM   5123 H  HA3  . GLY   B 1 73  ? 44.028 -9.055  13.832  1.00 18.07 ?  73  GLY   B HA3  1 
ATOM   5124 N  N    . PRO   B 1 74  ? 44.116 -11.596 13.049  1.00 13.88 ?  74  PRO   B N    1 
ATOM   5125 C  CA   . PRO   B 1 74  ? 43.864 -12.826 12.298  1.00 13.36 ?  74  PRO   B CA   1 
ATOM   5126 C  C    . PRO   B 1 74  ? 42.566 -12.766 11.509  1.00 13.06 ?  74  PRO   B C    1 
ATOM   5127 O  O    . PRO   B 1 74  ? 41.628 -12.024 11.828  1.00 14.26 ?  74  PRO   B O    1 
ATOM   5128 C  CB   . PRO   B 1 74  ? 43.795 -13.897 13.394  1.00 14.42 ?  74  PRO   B CB   1 
ATOM   5129 C  CG   . PRO   B 1 74  ? 43.350 -13.155 14.607  1.00 15.97 ?  74  PRO   B CG   1 
ATOM   5130 C  CD   . PRO   B 1 74  ? 44.012 -11.808 14.502  1.00 15.43 ?  74  PRO   B CD   1 
ATOM   5131 H  HA   . PRO   B 1 74  ? 44.604 -13.015 11.697  1.00 16.03 ?  74  PRO   B HA   1 
ATOM   5132 H  HB2  . PRO   B 1 74  ? 43.150 -14.577 13.145  1.00 17.31 ?  74  PRO   B HB2  1 
ATOM   5133 H  HB3  . PRO   B 1 74  ? 44.674 -14.285 13.527  1.00 17.31 ?  74  PRO   B HB3  1 
ATOM   5134 H  HG2  . PRO   B 1 74  ? 42.383 -13.063 14.597  1.00 19.17 ?  74  PRO   B HG2  1 
ATOM   5135 H  HG3  . PRO   B 1 74  ? 43.644 -13.621 15.403  1.00 19.17 ?  74  PRO   B HG3  1 
ATOM   5136 H  HD2  . PRO   B 1 74  ? 43.454 -11.123 14.911  1.00 18.52 ?  74  PRO   B HD2  1 
ATOM   5137 H  HD3  . PRO   B 1 74  ? 44.894 -11.830 14.905  1.00 18.52 ?  74  PRO   B HD3  1 
ATOM   5138 N  N    . LEU   B 1 75  ? 42.532 -13.579 10.455  1.00 12.38 ?  75  LEU   B N    1 
ATOM   5139 C  CA   . LEU   B 1 75  ? 41.320 -13.787 9.687   1.00 12.73 ?  75  LEU   B CA   1 
ATOM   5140 C  C    . LEU   B 1 75  ? 40.342 -14.643 10.487  1.00 12.96 ?  75  LEU   B C    1 
ATOM   5141 O  O    . LEU   B 1 75  ? 40.682 -15.212 11.524  1.00 13.98 ?  75  LEU   B O    1 
ATOM   5142 C  CB   . LEU   B 1 75  ? 41.644 -14.500 8.375   1.00 12.68 ?  75  LEU   B CB   1 
ATOM   5143 C  CG   . LEU   B 1 75  ? 42.488 -13.750 7.339   1.00 14.47 ?  75  LEU   B CG   1 
ATOM   5144 C  CD1  . LEU   B 1 75  ? 42.687 -14.589 6.079   1.00 15.67 ?  75  LEU   B CD1  1 
ATOM   5145 C  CD2  . LEU   B 1 75  ? 41.879 -12.418 6.990   1.00 17.54 ?  75  LEU   B CD2  1 
ATOM   5146 H  H    . LEU   B 1 75  ? 43.205 -14.027 10.163  1.00 14.86 ?  75  LEU   B H    1 
ATOM   5147 H  HA   . LEU   B 1 75  ? 40.900 -12.935 9.488   1.00 15.28 ?  75  LEU   B HA   1 
ATOM   5148 H  HB2  . LEU   B 1 75  ? 42.121 -15.318 8.588   1.00 15.22 ?  75  LEU   B HB2  1 
ATOM   5149 H  HB3  . LEU   B 1 75  ? 40.806 -14.729 7.940   1.00 15.22 ?  75  LEU   B HB3  1 
ATOM   5150 H  HG   . LEU   B 1 75  ? 43.365 -13.582 7.718   1.00 17.37 ?  75  LEU   B HG   1 
ATOM   5151 H  HD11 . LEU   B 1 75  ? 43.231 -14.087 5.446   1.00 18.82 ?  75  LEU   B HD11 1 
ATOM   5152 H  HD12 . LEU   B 1 75  ? 43.140 -15.414 6.314   1.00 18.82 ?  75  LEU   B HD12 1 
ATOM   5153 H  HD13 . LEU   B 1 75  ? 41.824 -14.785 5.686   1.00 18.82 ?  75  LEU   B HD13 1 
ATOM   5154 H  HD21 . LEU   B 1 75  ? 42.384 -12.021 6.265   1.00 21.05 ?  75  LEU   B HD21 1 
ATOM   5155 H  HD22 . LEU   B 1 75  ? 40.959 -12.554 6.721   1.00 21.05 ?  75  LEU   B HD22 1 
ATOM   5156 H  HD23 . LEU   B 1 75  ? 41.915 -11.842 7.772   1.00 21.05 ?  75  LEU   B HD23 1 
ATOM   5157 N  N    . LYS   B 1 76  ? 39.111 -14.726 9.986   1.00 14.11 ?  76  LYS   B N    1 
ATOM   5158 C  CA   . LYS   B 1 76  ? 38.129 -15.689 10.468  1.00 15.33 ?  76  LYS   B CA   1 
ATOM   5159 C  C    . LYS   B 1 76  ? 38.221 -16.961 9.632   1.00 14.12 ?  76  LYS   B C    1 
ATOM   5160 O  O    . LYS   B 1 76  ? 38.498 -16.904 8.435   1.00 13.90 ?  76  LYS   B O    1 
ATOM   5161 C  CB   . LYS   B 1 76  ? 36.711 -15.126 10.294  1.00 17.56 ?  76  LYS   B CB   1 
ATOM   5162 C  CG   . LYS   B 1 76  ? 36.439 -13.744 10.907  1.00 19.42 ?  76  LYS   B CG   1 
ATOM   5163 C  CD   . LYS   B 1 76  ? 35.033 -13.224 10.550  1.00 20.73 ?  76  LYS   B CD   1 
ATOM   5164 C  CE   . LYS   B 1 76  ? 34.754 -11.863 11.174  1.00 22.43 ?  76  LYS   B CE   1 
ATOM   5165 N  NZ   . LYS   B 1 76  ? 33.463 -11.268 10.722  1.00 23.04 ?  76  LYS   B NZ   1 
ATOM   5166 H  H    . LYS   B 1 76  ? 38.817 -14.230 9.349   1.00 16.94 ?  76  LYS   B H    1 
ATOM   5167 H  HA   . LYS   B 1 76  ? 38.286 -15.909 11.400  1.00 18.41 ?  76  LYS   B HA   1 
ATOM   5168 H  HB2  . LYS   B 1 76  ? 36.525 -15.063 9.345   1.00 21.08 ?  76  LYS   B HB2  1 
ATOM   5169 H  HB3  . LYS   B 1 76  ? 36.087 -15.748 10.702  1.00 21.08 ?  76  LYS   B HB3  1 
ATOM   5170 H  HG2  . LYS   B 1 76  ? 36.507 -13.805 11.873  1.00 23.31 ?  76  LYS   B HG2  1 
ATOM   5171 H  HG3  . LYS   B 1 76  ? 37.095 -13.112 10.567  1.00 23.31 ?  76  LYS   B HG3  1 
ATOM   5172 H  HD2  . LYS   B 1 76  ? 34.964 -13.139 9.586   1.00 24.89 ?  76  LYS   B HD2  1 
ATOM   5173 H  HD3  . LYS   B 1 76  ? 34.372 -13.852 10.878  1.00 24.89 ?  76  LYS   B HD3  1 
ATOM   5174 H  HE2  . LYS   B 1 76  ? 34.720 -11.960 12.137  1.00 26.93 ?  76  LYS   B HE2  1 
ATOM   5175 H  HE3  . LYS   B 1 76  ? 35.467 -11.253 10.927  1.00 26.93 ?  76  LYS   B HE3  1 
ATOM   5176 H  HZ1  . LYS   B 1 76  ? 33.340 -10.475 11.110  1.00 27.66 ?  76  LYS   B HZ1  1 
ATOM   5177 H  HZ2  . LYS   B 1 76  ? 33.467 -11.158 9.839   1.00 27.66 ?  76  LYS   B HZ2  1 
ATOM   5178 H  HZ3  . LYS   B 1 76  ? 32.786 -11.803 10.942  1.00 27.66 ?  76  LYS   B HZ3  1 
ATOM   5179 N  N    . VAL   B 1 77  ? 37.983 -18.118 10.261  1.00 14.98 ?  77  VAL   B N    1 
ATOM   5180 C  CA   . VAL   B 1 77  ? 37.779 -19.332 9.479   1.00 14.95 ?  77  VAL   B CA   1 
ATOM   5181 C  C    . VAL   B 1 77  ? 36.585 -19.103 8.564   1.00 13.84 ?  77  VAL   B C    1 
ATOM   5182 O  O    . VAL   B 1 77  ? 35.521 -18.653 9.010   1.00 14.01 ?  77  VAL   B O    1 
ATOM   5183 C  CB   . VAL   B 1 77  ? 37.579 -20.550 10.392  1.00 16.42 ?  77  VAL   B CB   1 
ATOM   5184 C  CG1  . VAL   B 1 77  ? 37.294 -21.789 9.552   1.00 17.11 ?  77  VAL   B CG1  1 
ATOM   5185 C  CG2  . VAL   B 1 77  ? 38.808 -20.776 11.276  1.00 17.70 ?  77  VAL   B CG2  1 
ATOM   5186 H  H    . VAL   B 1 77  ? 37.934 -18.220 11.107  1.00 17.98 ?  77  VAL   B H    1 
ATOM   5187 H  HA   . VAL   B 1 77  ? 38.554 -19.494 8.921   1.00 17.94 ?  77  VAL   B HA   1 
ATOM   5188 H  HB   . VAL   B 1 77  ? 36.812 -20.393 10.966  1.00 19.71 ?  77  VAL   B HB   1 
ATOM   5189 H  HG11 . VAL   B 1 77  ? 37.344 -22.571 10.124  1.00 20.53 ?  77  VAL   B HG11 1 
ATOM   5190 H  HG12 . VAL   B 1 77  ? 36.402 -21.720 9.171   1.00 20.53 ?  77  VAL   B HG12 1 
ATOM   5191 H  HG13 . VAL   B 1 77  ? 37.953 -21.851 8.846   1.00 20.53 ?  77  VAL   B HG13 1 
ATOM   5192 H  HG21 . VAL   B 1 77  ? 38.664 -21.569 11.812  1.00 21.25 ?  77  VAL   B HG21 1 
ATOM   5193 H  HG22 . VAL   B 1 77  ? 39.583 -20.890 10.708  1.00 21.25 ?  77  VAL   B HG22 1 
ATOM   5194 H  HG23 . VAL   B 1 77  ? 38.925 -20.002 11.849  1.00 21.25 ?  77  VAL   B HG23 1 
ATOM   5195 N  N    . GLY   B 1 78  ? 36.765 -19.382 7.273   1.00 13.31 ?  78  GLY   B N    1 
ATOM   5196 C  CA   . GLY   B 1 78  ? 35.787 -19.054 6.262   1.00 12.97 ?  78  GLY   B CA   1 
ATOM   5197 C  C    . GLY   B 1 78  ? 36.030 -17.736 5.564   1.00 12.39 ?  78  GLY   B C    1 
ATOM   5198 O  O    . GLY   B 1 78  ? 35.345 -17.448 4.576   1.00 13.02 ?  78  GLY   B O    1 
ATOM   5199 H  H    . GLY   B 1 78  ? 37.464 -19.775 6.956   1.00 15.98 ?  78  GLY   B H    1 
ATOM   5200 H  HA2  . GLY   B 1 78  ? 35.778 -19.749 5.589   1.00 15.56 ?  78  GLY   B HA2  1 
ATOM   5201 H  HA3  . GLY   B 1 78  ? 34.909 -19.014 6.671   1.00 15.56 ?  78  GLY   B HA3  1 
ATOM   5202 N  N    . GLY   B 1 79  ? 36.979 -16.930 6.049   1.00 12.28 ?  79  GLY   B N    1 
ATOM   5203 C  CA   . GLY   B 1 79  ? 37.276 -15.634 5.474   1.00 12.04 ?  79  GLY   B CA   1 
ATOM   5204 C  C    . GLY   B 1 79  ? 38.515 -15.653 4.588   1.00 11.60 ?  79  GLY   B C    1 
ATOM   5205 O  O    . GLY   B 1 79  ? 39.131 -16.687 4.343   1.00 12.17 ?  79  GLY   B O    1 
ATOM   5206 H  H    . GLY   B 1 79  ? 37.476 -17.121 6.723   1.00 14.75 ?  79  GLY   B H    1 
ATOM   5207 H  HA2  . GLY   B 1 79  ? 36.523 -15.334 4.938   1.00 14.45 ?  79  GLY   B HA2  1 
ATOM   5208 H  HA3  . GLY   B 1 79  ? 37.424 -14.989 6.182   1.00 14.45 ?  79  GLY   B HA3  1 
ATOM   5209 N  N    . SER   B 1 80  ? 38.882 -14.462 4.112   1.00 11.63 ?  80  SER   B N    1 
ATOM   5210 C  CA   . SER   B 1 80  ? 39.992 -14.333 3.179   1.00 11.50 ?  80  SER   B CA   1 
ATOM   5211 C  C    . SER   B 1 80  ? 40.568 -12.926 3.235   1.00 11.26 ?  80  SER   B C    1 
ATOM   5212 O  O    . SER   B 1 80  ? 39.947 -11.992 3.746   1.00 12.42 ?  80  SER   B O    1 
ATOM   5213 C  CB   . SER   B 1 80  ? 39.552 -14.621 1.740   1.00 11.80 ?  80  SER   B CB   1 
ATOM   5214 O  OG   . SER   B 1 80  ? 38.704 -13.600 1.240   1.00 12.95 ?  80  SER   B OG   1 
ATOM   5215 H  H    . SER   B 1 80  ? 38.512 -13.714 4.319   1.00 13.96 ?  80  SER   B H    1 
ATOM   5216 H  HA   . SER   B 1 80  ? 40.685 -14.963 3.425   1.00 13.80 ?  80  SER   B HA   1 
ATOM   5217 H  HB2  . SER   B 1 80  ? 40.337 -14.675 1.172   1.00 14.17 ?  80  SER   B HB2  1 
ATOM   5218 H  HB3  . SER   B 1 80  ? 39.072 -15.464 1.719   1.00 14.17 ?  80  SER   B HB3  1 
ATOM   5219 H  HG   . SER   B 1 80  ? 38.012 -13.540 1.725   1.00 15.54 ?  80  SER   B HG   1 
ATOM   5220 N  N    . CYS   B 1 81  ? 41.757 -12.784 2.654   1.00 11.12 ?  81  CYS   B N    1 
ATOM   5221 C  CA   . CYS   B 1 81  ? 42.306 -11.473 2.340   1.00 11.31 ?  81  CYS   B CA   1 
ATOM   5222 C  C    . CYS   B 1 81  ? 43.078 -11.559 1.032   1.00 10.55 ?  81  CYS   B C    1 
ATOM   5223 O  O    . CYS   B 1 81  ? 43.589 -12.621 0.659   1.00 11.65 ?  81  CYS   B O    1 
ATOM   5224 C  CB   . CYS   B 1 81  ? 43.197 -10.921 3.461   1.00 12.00 ?  81  CYS   B CB   1 
ATOM   5225 S  SG   . CYS   B 1 81  ? 44.714 -11.861 3.706   1.00 12.36 ?  81  CYS   B SG   1 
ATOM   5226 H  H    . CYS   B 1 81  ? 42.268 -13.441 2.423   1.00 13.35 ?  81  CYS   B H    1 
ATOM   5227 H  HA   . CYS   B 1 81  ? 41.572 -10.849 2.210   1.00 13.57 ?  81  CYS   B HA   1 
ATOM   5228 H  HB2  . CYS   B 1 81  ? 43.446 -10.008 3.247   1.00 14.41 ?  81  CYS   B HB2  1 
ATOM   5229 H  HB3  . CYS   B 1 81  ? 42.696 -10.934 4.296   1.00 14.41 ?  81  CYS   B HB3  1 
ATOM   5230 H  HG   . CYS   B 1 81  ? 45.340 -11.364 4.606   1.00 14.84 ?  81  CYS   B HG   1 
ATOM   5231 N  N    . VAL   B 1 82  ? 43.176 -10.418 0.353   1.00 10.80 ?  82  VAL   B N    1 
ATOM   5232 C  CA   . VAL   B 1 82  ? 43.944 -10.294 -0.882  1.00 10.98 ?  82  VAL   B CA   1 
ATOM   5233 C  C    . VAL   B 1 82  ? 45.286 -9.653  -0.559  1.00 11.31 ?  82  VAL   B C    1 
ATOM   5234 O  O    . VAL   B 1 82  ? 45.339 -8.534  -0.027  1.00 12.58 ?  82  VAL   B O    1 
ATOM   5235 C  CB   . VAL   B 1 82  ? 43.201 -9.455  -1.931  1.00 12.22 ?  82  VAL   B CB   1 
ATOM   5236 C  CG1  . VAL   B 1 82  ? 44.058 -9.310  -3.184  1.00 13.30 ?  82  VAL   B CG1  1 
ATOM   5237 C  CG2  . VAL   B 1 82  ? 41.849 -10.060 -2.255  1.00 13.17 ?  82  VAL   B CG2  1 
ATOM   5238 H  H    . VAL   B 1 82  ? 42.791 -9.680  0.588   1.00 12.97 ?  82  VAL   B H    1 
ATOM   5239 H  HA   . VAL   B 1 82  ? 44.107 -11.174 -1.250  1.00 13.18 ?  82  VAL   B HA   1 
ATOM   5240 H  HB   . VAL   B 1 82  ? 43.049 -8.570  -1.576  1.00 14.67 ?  82  VAL   B HB   1 
ATOM   5241 H  HG11 . VAL   B 1 82  ? 43.503 -9.005  -3.918  1.00 15.96 ?  82  VAL   B HG11 1 
ATOM   5242 H  HG12 . VAL   B 1 82  ? 44.763 -8.658  -3.016  1.00 15.96 ?  82  VAL   B HG12 1 
ATOM   5243 H  HG13 . VAL   B 1 82  ? 44.453 -10.169 -3.405  1.00 15.96 ?  82  VAL   B HG13 1 
ATOM   5244 H  HG21 . VAL   B 1 82  ? 41.420 -9.534  -2.949  1.00 15.81 ?  82  VAL   B HG21 1 
ATOM   5245 H  HG22 . VAL   B 1 82  ? 41.973 -10.974 -2.568  1.00 15.81 ?  82  VAL   B HG22 1 
ATOM   5246 H  HG23 . VAL   B 1 82  ? 41.300 -10.061 -1.455  1.00 15.81 ?  82  VAL   B HG23 1 
ATOM   5247 N  N    . LEU   B 1 83  ? 46.364 -10.344 -0.920  1.00 10.91 ?  83  LEU   B N    1 
ATOM   5248 C  CA   . LEU   B 1 83  ? 47.721 -9.828  -0.799  1.00 10.86 ?  83  LEU   B CA   1 
ATOM   5249 C  C    . LEU   B 1 83  ? 48.419 -9.974  -2.149  1.00 10.77 ?  83  LEU   B C    1 
ATOM   5250 O  O    . LEU   B 1 83  ? 47.816 -10.394 -3.140  1.00 11.00 ?  83  LEU   B O    1 
ATOM   5251 C  CB   . LEU   B 1 83  ? 48.470 -10.506 0.356   1.00 11.51 ?  83  LEU   B CB   1 
ATOM   5252 C  CG   . LEU   B 1 83  ? 47.960 -10.143 1.757   1.00 12.59 ?  83  LEU   B CG   1 
ATOM   5253 C  CD1  . LEU   B 1 83  ? 48.591 -11.011 2.821   1.00 13.22 ?  83  LEU   B CD1  1 
ATOM   5254 C  CD2  . LEU   B 1 83  ? 48.167 -8.661  2.079   1.00 13.52 ?  83  LEU   B CD2  1 
ATOM   5255 H  H    . LEU   B 1 83  ? 46.327 -11.143 -1.243  1.00 13.09 ?  83  LEU   B H    1 
ATOM   5256 H  HA   . LEU   B 1 83  ? 47.668 -8.883  -0.606  1.00 13.04 ?  83  LEU   B HA   1 
ATOM   5257 H  HB2  . LEU   B 1 83  ? 48.396 -11.462 0.253   1.00 13.82 ?  83  LEU   B HB2  1 
ATOM   5258 H  HB3  . LEU   B 1 83  ? 49.403 -10.241 0.303   1.00 13.82 ?  83  LEU   B HB3  1 
ATOM   5259 H  HG   . LEU   B 1 83  ? 47.008 -10.304 1.780   1.00 15.12 ?  83  LEU   B HG   1 
ATOM   5260 H  HD11 . LEU   B 1 83  ? 48.236 -10.755 3.689   1.00 15.87 ?  83  LEU   B HD11 1 
ATOM   5261 H  HD12 . LEU   B 1 83  ? 48.371 -11.939 2.639   1.00 15.87 ?  83  LEU   B HD12 1 
ATOM   5262 H  HD13 . LEU   B 1 83  ? 49.551 -10.888 2.808   1.00 15.87 ?  83  LEU   B HD13 1 
ATOM   5263 H  HD21 . LEU   B 1 83  ? 47.954 -8.507  3.013   1.00 16.23 ?  83  LEU   B HD21 1 
ATOM   5264 H  HD22 . LEU   B 1 83  ? 49.091 -8.422  1.908   1.00 16.23 ?  83  LEU   B HD22 1 
ATOM   5265 H  HD23 . LEU   B 1 83  ? 47.580 -8.128  1.517   1.00 16.23 ?  83  LEU   B HD23 1 
ATOM   5266 N  N    . SER   B 1 84  ? 49.697 -9.601  -2.205  1.00 11.85 ?  84  SER   B N    1 
ATOM   5267 C  CA   . SER   B 1 84  ? 50.427 -9.716  -3.458  1.00 12.35 ?  84  SER   B CA   1 
ATOM   5268 C  C    . SER   B 1 84  ? 50.585 -11.176 -3.867  1.00 11.43 ?  84  SER   B C    1 
ATOM   5269 O  O    . SER   B 1 84  ? 50.699 -12.073 -3.030  1.00 11.35 ?  84  SER   B O    1 
ATOM   5270 C  CB   . SER   B 1 84  ? 51.823 -9.120  -3.312  1.00 13.93 ?  84  SER   B CB   1 
ATOM   5271 O  OG   . SER   B 1 84  ? 52.560 -9.322  -4.505  1.00 15.25 ?  84  SER   B OG   1 
ATOM   5272 H  H    . SER   B 1 84  ? 50.148 -9.269  -1.550  1.00 14.22 ?  84  SER   B H    1 
ATOM   5273 H  HA   . SER   B 1 84  ? 49.957 -9.244  -4.161  1.00 14.83 ?  84  SER   B HA   1 
ATOM   5274 H  HB2  . SER   B 1 84  ? 51.745 -8.167  -3.136  1.00 16.72 ?  84  SER   B HB2  1 
ATOM   5275 H  HB3  . SER   B 1 84  ? 52.283 -9.556  -2.578  1.00 16.72 ?  84  SER   B HB3  1 
ATOM   5276 H  HG   . SER   B 1 84  ? 53.331 -8.984  -4.428  1.00 18.30 ?  84  SER   B HG   1 
ATOM   5277 N  N    . GLY   B 1 85  ? 50.648 -11.403 -5.173  1.00 12.44 ?  85  GLY   B N    1 
ATOM   5278 C  CA   . GLY   B 1 85  ? 50.998 -12.697 -5.705  1.00 13.08 ?  85  GLY   B CA   1 
ATOM   5279 C  C    . GLY   B 1 85  ? 52.467 -12.888 -6.009  1.00 12.48 ?  85  GLY   B C    1 
ATOM   5280 O  O    . GLY   B 1 85  ? 52.847 -13.963 -6.478  1.00 12.86 ?  85  GLY   B O    1 
ATOM   5281 H  H    . GLY   B 1 85  ? 50.498 -10.813 -5.777  1.00 14.93 ?  85  GLY   B H    1 
ATOM   5282 H  HA2  . GLY   B 1 85  ? 50.736 -13.384 -5.069  1.00 15.70 ?  85  GLY   B HA2  1 
ATOM   5283 H  HA3  . GLY   B 1 85  ? 50.509 -12.849 -6.524  1.00 15.70 ?  85  GLY   B HA3  1 
ATOM   5284 N  N    . HIS   B 1 86  ? 53.315 -11.888 -5.778  1.00 12.53 ?  86  HIS   B N    1 
ATOM   5285 C  CA   . HIS   B 1 86  ? 54.777 -12.051 -5.863  1.00 12.35 ?  86  HIS   B CA   1 
ATOM   5286 C  C    . HIS   B 1 86  ? 55.152 -12.564 -7.252  1.00 12.53 ?  86  HIS   B C    1 
ATOM   5287 O  O    . HIS   B 1 86  ? 54.764 -11.947 -8.256  1.00 13.40 ?  86  HIS   B O    1 
ATOM   5288 C  CB   . HIS   B 1 86  ? 55.271 -12.892 -4.690  1.00 12.96 ?  86  HIS   B CB   1 
ATOM   5289 C  CG   . HIS   B 1 86  ? 54.955 -12.289 -3.366  1.00 13.01 ?  86  HIS   B CG   1 
ATOM   5290 N  ND1  . HIS   B 1 86  ? 55.787 -11.382 -2.746  1.00 14.36 ?  86  HIS   B ND1  1 
ATOM   5291 C  CD2  . HIS   B 1 86  ? 53.878 -12.432 -2.559  1.00 13.44 ?  86  HIS   B CD2  1 
ATOM   5292 C  CE1  . HIS   B 1 86  ? 55.232 -10.995 -1.611  1.00 14.22 ?  86  HIS   B CE1  1 
ATOM   5293 N  NE2  . HIS   B 1 86  ? 54.071 -11.612 -1.476  1.00 13.58 ?  86  HIS   B NE2  1 
ATOM   5294 H  H    . HIS   B 1 86  ? 53.072 -11.094 -5.563  1.00 15.04 ?  86  HIS   B H    1 
ATOM   5295 H  HA   . HIS   B 1 86  ? 55.183 -11.177 -5.769  1.00 14.83 ?  86  HIS   B HA   1 
ATOM   5296 H  HB2  . HIS   B 1 86  ? 54.856 -13.766 -4.728  1.00 15.55 ?  86  HIS   B HB2  1 
ATOM   5297 H  HB3  . HIS   B 1 86  ? 56.237 -12.981 -4.749  1.00 15.55 ?  86  HIS   B HB3  1 
ATOM   5298 H  HD2  . HIS   B 1 86  ? 53.132 -12.970 -2.716  1.00 16.13 ?  86  HIS   B HD2  1 
ATOM   5299 H  HE1  . HIS   B 1 86  ? 55.603 -10.400 -1.000  1.00 17.07 ?  86  HIS   B HE1  1 
ATOM   5300 H  HE2  . HIS   B 1 86  ? 53.534 -11.530 -0.807  1.00 16.30 ?  86  HIS   B HE2  1 
ATOM   5301 N  N    . ASN   B 1 87  ? 55.922 -13.646 -7.358  1.00 12.80 ?  87  ASN   B N    1 
ATOM   5302 C  CA   . ASN   B 1 87  ? 56.319 -14.219 -8.634  1.00 13.63 ?  87  ASN   B CA   1 
ATOM   5303 C  C    . ASN   B 1 87  ? 55.337 -15.262 -9.138  1.00 13.51 ?  87  ASN   B C    1 
ATOM   5304 O  O    . ASN   B 1 87  ? 55.657 -15.977 -10.093 1.00 15.23 ?  87  ASN   B O    1 
ATOM   5305 C  CB   . ASN   B 1 87  ? 57.713 -14.847 -8.515  1.00 15.55 ?  87  ASN   B CB   1 
ATOM   5306 C  CG   . ASN   B 1 87  ? 57.767 -15.958 -7.475  1.00 16.39 ?  87  ASN   B CG   1 
ATOM   5307 O  OD1  . ASN   B 1 87  ? 57.123 -15.878 -6.425  1.00 15.34 ?  87  ASN   B OD1  1 
ATOM   5308 N  ND2  . ASN   B 1 87  ? 58.521 -17.016 -7.775  1.00 18.41 ?  87  ASN   B ND2  1 
ATOM   5309 H  H    . ASN   B 1 87  ? 56.224 -14.084 -6.685  1.00 15.37 ?  87  ASN   B H    1 
ATOM   5310 H  HA   . ASN   B 1 87  ? 56.364 -13.512 -9.294  1.00 16.36 ?  87  ASN   B HA   1 
ATOM   5311 H  HB2  . ASN   B 1 87  ? 57.963 -15.225 -9.373  1.00 18.67 ?  87  ASN   B HB2  1 
ATOM   5312 H  HB3  . ASN   B 1 87  ? 58.345 -14.159 -8.257  1.00 18.67 ?  87  ASN   B HB3  1 
ATOM   5313 H  HD21 . ASN   B 1 87  ? 58.587 -17.667 -7.220  1.00 22.09 ?  87  ASN   B HD21 1 
ATOM   5314 H  HD22 . ASN   B 1 87  ? 58.952 -17.041 -8.521  1.00 22.09 ?  87  ASN   B HD22 1 
ATOM   5315 N  N    . LEU   B 1 88  ? 54.154 -15.359 -8.526  1.00 12.48 ?  88  LEU   B N    1 
ATOM   5316 C  CA   . LEU   B 1 88  ? 53.178 -16.390 -8.853  1.00 12.72 ?  88  LEU   B CA   1 
ATOM   5317 C  C    . LEU   B 1 88  ? 51.947 -15.874 -9.574  1.00 12.44 ?  88  LEU   B C    1 
ATOM   5318 O  O    . LEU   B 1 88  ? 51.349 -16.620 -10.361 1.00 14.22 ?  88  LEU   B O    1 
ATOM   5319 C  CB   . LEU   B 1 88  ? 52.709 -17.079 -7.569  1.00 13.62 ?  88  LEU   B CB   1 
ATOM   5320 C  CG   . LEU   B 1 88  ? 53.833 -17.727 -6.774  1.00 15.85 ?  88  LEU   B CG   1 
ATOM   5321 C  CD1  . LEU   B 1 88  ? 53.334 -18.126 -5.397  1.00 17.55 ?  88  LEU   B CD1  1 
ATOM   5322 C  CD2  . LEU   B 1 88  ? 54.372 -18.924 -7.530  1.00 18.92 ?  88  LEU   B CD2  1 
ATOM   5323 H  H    . LEU   B 1 88  ? 53.890 -14.827 -7.900  1.00 14.98 ?  88  LEU   B H    1 
ATOM   5324 H  HA   . LEU   B 1 88  ? 53.592 -17.054 -9.418  1.00 15.27 ?  88  LEU   B HA   1 
ATOM   5325 H  HB2  . LEU   B 1 88  ? 52.280 -16.424 -6.995  1.00 16.35 ?  88  LEU   B HB2  1 
ATOM   5326 H  HB3  . LEU   B 1 88  ? 52.072 -17.776 -7.801  1.00 16.35 ?  88  LEU   B HB3  1 
ATOM   5327 H  HG   . LEU   B 1 88  ? 54.553 -17.088 -6.660  1.00 19.02 ?  88  LEU   B HG   1 
ATOM   5328 H  HD11 . LEU   B 1 88  ? 54.009 -18.670 -4.962  1.00 21.06 ?  88  LEU   B HD11 1 
ATOM   5329 H  HD12 . LEU   B 1 88  ? 53.165 -17.326 -4.876  1.00 21.06 ?  88  LEU   B HD12 1 
ATOM   5330 H  HD13 . LEU   B 1 88  ? 52.514 -18.635 -5.498  1.00 21.06 ?  88  LEU   B HD13 1 
ATOM   5331 H  HD21 . LEU   B 1 88  ? 55.004 -19.393 -6.965  1.00 22.71 ?  88  LEU   B HD21 1 
ATOM   5332 H  HD22 . LEU   B 1 88  ? 53.635 -19.509 -7.760  1.00 22.71 ?  88  LEU   B HD22 1 
ATOM   5333 H  HD23 . LEU   B 1 88  ? 54.815 -18.616 -8.336  1.00 22.71 ?  88  LEU   B HD23 1 
ATOM   5334 N  N    . ALA   B 1 89  ? 51.539 -14.641 -9.301  1.00 11.86 ?  89  ALA   B N    1 
ATOM   5335 C  CA   . ALA   B 1 89  ? 50.249 -14.145 -9.752  1.00 11.46 ?  89  ALA   B CA   1 
ATOM   5336 C  C    . ALA   B 1 89  ? 50.222 -12.656 -9.467  1.00 11.85 ?  89  ALA   B C    1 
ATOM   5337 O  O    . ALA   B 1 89  ? 51.054 -12.140 -8.721  1.00 12.60 ?  89  ALA   B O    1 
ATOM   5338 C  CB   . ALA   B 1 89  ? 49.108 -14.822 -8.999  1.00 11.57 ?  89  ALA   B CB   1 
ATOM   5339 H  H    . ALA   B 1 89  ? 51.986 -14.065 -8.842  1.00 14.24 ?  89  ALA   B H    1 
ATOM   5340 H  HA   . ALA   B 1 89  ? 50.141 -14.288 -10.706 1.00 13.75 ?  89  ALA   B HA   1 
ATOM   5341 H  HB1  . ALA   B 1 89  ? 48.261 -14.485 -9.339  1.00 13.89 ?  89  ALA   B HB1  1 
ATOM   5342 H  HB2  . ALA   B 1 89  ? 49.163 -15.779 -9.148  1.00 13.89 ?  89  ALA   B HB2  1 
ATOM   5343 H  HB3  . ALA   B 1 89  ? 49.191 -14.625 -8.058  1.00 13.89 ?  89  ALA   B HB3  1 
ATOM   5344 N  N    . LYS   B 1 90  ? 49.234 -11.965 -10.032 1.00 12.75 ?  90  LYS   B N    1 
ATOM   5345 C  CA   . LYS   B 1 90  ? 49.049 -10.578 -9.627  1.00 12.83 ?  90  LYS   B CA   1 
ATOM   5346 C  C    . LYS   B 1 90  ? 48.731 -10.504 -8.138  1.00 12.56 ?  90  LYS   B C    1 
ATOM   5347 O  O    . LYS   B 1 90  ? 49.373 -9.755  -7.387  1.00 13.67 ?  90  LYS   B O    1 
ATOM   5348 C  CB   . LYS   B 1 90  ? 47.970 -9.913  -10.479 1.00 14.19 ?  90  LYS   B CB   1 
ATOM   5349 C  CG   . LYS   B 1 90  ? 47.671 -8.471  -10.090 1.00 14.83 ?  90  LYS   B CG   1 
ATOM   5350 C  CD   . LYS   B 1 90  ? 48.881 -7.571  -10.167 1.00 17.41 ?  90  LYS   B CD   1 
ATOM   5351 C  CE   . LYS   B 1 90  ? 48.433 -6.146  -9.935  1.00 19.34 ?  90  LYS   B CE   1 
ATOM   5352 N  NZ   . LYS   B 1 90  ? 49.582 -5.223  -9.794  1.00 19.16 ?  90  LYS   B NZ   1 
ATOM   5353 H  H    . LYS   B 1 90  ? 48.684 -12.264 -10.620 1.00 15.30 ?  90  LYS   B H    1 
ATOM   5354 H  HA   . LYS   B 1 90  ? 49.875 -10.099 -9.774  1.00 15.41 ?  90  LYS   B HA   1 
ATOM   5355 H  HB2  . LYS   B 1 90  ? 48.262 -9.908  -11.407 1.00 17.03 ?  90  LYS   B HB2  1 
ATOM   5356 H  HB3  . LYS   B 1 90  ? 47.146 -10.416 -10.401 1.00 17.03 ?  90  LYS   B HB3  1 
ATOM   5357 H  HG2  . LYS   B 1 90  ? 46.998 -8.114  -10.692 1.00 17.80 ?  90  LYS   B HG2  1 
ATOM   5358 H  HG3  . LYS   B 1 90  ? 47.337 -8.450  -9.178  1.00 17.80 ?  90  LYS   B HG3  1 
ATOM   5359 H  HD2  . LYS   B 1 90  ? 49.519 -7.813  -9.475  1.00 20.90 ?  90  LYS   B HD2  1 
ATOM   5360 H  HD3  . LYS   B 1 90  ? 49.286 -7.635  -11.046 1.00 20.90 ?  90  LYS   B HD3  1 
ATOM   5361 H  HE2  . LYS   B 1 90  ? 47.902 -5.844  -10.692 1.00 23.21 ?  90  LYS   B HE2  1 
ATOM   5362 H  HE3  . LYS   B 1 90  ? 47.910 -6.094  -9.121  1.00 23.21 ?  90  LYS   B HE3  1 
ATOM   5363 H  HZ1  . LYS   B 1 90  ? 49.298 -4.389  -9.662  1.00 22.99 ?  90  LYS   B HZ1  1 
ATOM   5364 H  HZ2  . LYS   B 1 90  ? 50.089 -5.467  -9.104  1.00 22.99 ?  90  LYS   B HZ2  1 
ATOM   5365 H  HZ3  . LYS   B 1 90  ? 50.081 -5.239  -10.535 1.00 22.99 ?  90  LYS   B HZ3  1 
ATOM   5366 N  N    . HIS   B 1 91  ? 47.766 -11.311 -7.695  1.00 11.16 ?  91  HIS   B N    1 
ATOM   5367 C  CA   . HIS   B 1 91  ? 47.297 -11.335 -6.323  1.00 11.19 ?  91  HIS   B CA   1 
ATOM   5368 C  C    . HIS   B 1 91  ? 47.297 -12.761 -5.805  1.00 10.58 ?  91  HIS   B C    1 
ATOM   5369 O  O    . HIS   B 1 91  ? 47.072 -13.714 -6.558  1.00 11.02 ?  91  HIS   B O    1 
ATOM   5370 C  CB   . HIS   B 1 91  ? 45.843 -10.861 -6.217  1.00 12.68 ?  91  HIS   B CB   1 
ATOM   5371 C  CG   . HIS   B 1 91  ? 45.634 -9.451  -6.646  1.00 15.88 ?  91  HIS   B CG   1 
ATOM   5372 N  ND1  . HIS   B 1 91  ? 46.257 -8.383  -6.037  1.00 18.43 ?  91  HIS   B ND1  1 
ATOM   5373 C  CD2  . HIS   B 1 91  ? 44.842 -8.928  -7.607  1.00 18.07 ?  91  HIS   B CD2  1 
ATOM   5374 C  CE1  . HIS   B 1 91  ? 45.875 -7.260  -6.619  1.00 19.54 ?  91  HIS   B CE1  1 
ATOM   5375 N  NE2  . HIS   B 1 91  ? 45.011 -7.565  -7.573  1.00 19.54 ?  91  HIS   B NE2  1 
ATOM   5376 H  H    . HIS   B 1 91  ? 47.350 -11.876 -8.194  1.00 13.39 ?  91  HIS   B H    1 
ATOM   5377 H  HA   . HIS   B 1 91  ? 47.864 -10.776 -5.756  1.00 13.44 ?  91  HIS   B HA   1 
ATOM   5378 H  HB2  . HIS   B 1 91  ? 45.288 -11.425 -6.779  1.00 15.22 ?  91  HIS   B HB2  1 
ATOM   5379 H  HB3  . HIS   B 1 91  ? 45.551 -10.934 -5.293  1.00 15.22 ?  91  HIS   B HB3  1 
ATOM   5380 H  HD1  . HIS   B 1 91  ? 46.815 -8.439  -5.384  1.00 22.12 ?  91  HIS   B HD1  1 
ATOM   5381 H  HD2  . HIS   B 1 91  ? 44.291 -9.390  -8.193  1.00 21.69 ?  91  HIS   B HD2  1 
ATOM   5382 H  HE1  . HIS   B 1 91  ? 46.161 -6.402  -6.388  1.00 23.46 ?  91  HIS   B HE1  1 
ATOM   5383 N  N    . CYS   B 1 92  ? 47.491 -12.896 -4.501  1.00 10.50 ?  92  CYS   B N    1 
ATOM   5384 C  CA   . CYS   B 1 92  ? 47.189 -14.130 -3.790  1.00 10.27 ?  92  CYS   B CA   1 
ATOM   5385 C  C    . CYS   B 1 92  ? 45.967 -13.896 -2.910  1.00 9.91  ?  92  CYS   B C    1 
ATOM   5386 O  O    . CYS   B 1 92  ? 45.965 -12.991 -2.065  1.00 10.73 ?  92  CYS   B O    1 
ATOM   5387 C  CB   . CYS   B 1 92  ? 48.363 -14.585 -2.931  1.00 10.83 ?  92  CYS   B CB   1 
ATOM   5388 S  SG   . CYS   B 1 92  ? 48.005 -16.123 -2.045  1.00 10.87 ?  92  CYS   B SG   1 
ATOM   5389 H  H    . CYS   B 1 92  ? 47.821 -12.278 -3.994  1.00 12.61 ?  92  CYS   B H    1 
ATOM   5390 H  HA   . CYS   B 1 92  ? 46.991 -14.829 -4.431  1.00 12.33 ?  92  CYS   B HA   1 
ATOM   5391 H  HB2  . CYS   B 1 92  ? 49.134 -14.733 -3.493  1.00 13.00 ?  92  CYS   B HB2  1 
ATOM   5392 H  HB3  . CYS   B 1 92  ? 48.555 -13.897 -2.271  1.00 13.00 ?  92  CYS   B HB3  1 
ATOM   5393 H  HG   . CYS   B 1 92  ? 48.972 -16.437 -1.411  1.00 13.05 ?  92  CYS   B HG   1 
ATOM   5394 N  N    . LEU   B 1 93  ? 44.931 -14.702 -3.123  1.00 9.92  ?  93  LEU   B N    1 
ATOM   5395 C  CA   . LEU   B 1 93  ? 43.754 -14.708 -2.268  1.00 10.22 ?  93  LEU   B CA   1 
ATOM   5396 C  C    . LEU   B 1 93  ? 43.980 -15.773 -1.204  1.00 9.63  ?  93  LEU   B C    1 
ATOM   5397 O  O    . LEU   B 1 93  ? 43.935 -16.973 -1.497  1.00 10.28 ?  93  LEU   B O    1 
ATOM   5398 C  CB   . LEU   B 1 93  ? 42.495 -15.001 -3.078  1.00 10.64 ?  93  LEU   B CB   1 
ATOM   5399 C  CG   . LEU   B 1 93  ? 41.199 -15.018 -2.263  1.00 11.24 ?  93  LEU   B CG   1 
ATOM   5400 C  CD1  . LEU   B 1 93  ? 40.845 -13.632 -1.774  1.00 11.54 ?  93  LEU   B CD1  1 
ATOM   5401 C  CD2  . LEU   B 1 93  ? 40.071 -15.605 -3.089  1.00 11.64 ?  93  LEU   B CD2  1 
ATOM   5402 H  H    . LEU   B 1 93  ? 44.892 -15.278 -3.773  1.00 11.91 ?  93  LEU   B H    1 
ATOM   5403 H  HA   . LEU   B 1 93  ? 43.663 -13.847 -1.838  1.00 12.27 ?  93  LEU   B HA   1 
ATOM   5404 H  HB2  . LEU   B 1 93  ? 42.401 -14.311 -3.756  1.00 12.77 ?  93  LEU   B HB2  1 
ATOM   5405 H  HB3  . LEU   B 1 93  ? 42.589 -15.863 -3.500  1.00 12.77 ?  93  LEU   B HB3  1 
ATOM   5406 H  HG   . LEU   B 1 93  ? 41.320 -15.584 -1.487  1.00 13.49 ?  93  LEU   B HG   1 
ATOM   5407 H  HD11 . LEU   B 1 93  ? 39.991 -13.664 -1.322  1.00 13.85 ?  93  LEU   B HD11 1 
ATOM   5408 H  HD12 . LEU   B 1 93  ? 41.535 -13.325 -1.167  1.00 13.85 ?  93  LEU   B HD12 1 
ATOM   5409 H  HD13 . LEU   B 1 93  ? 40.790 -13.033 -2.541  1.00 13.85 ?  93  LEU   B HD13 1 
ATOM   5410 H  HD21 . LEU   B 1 93  ? 39.258 -15.606 -2.558  1.00 13.98 ?  93  LEU   B HD21 1 
ATOM   5411 H  HD22 . LEU   B 1 93  ? 39.946 -15.067 -3.885  1.00 13.98 ?  93  LEU   B HD22 1 
ATOM   5412 H  HD23 . LEU   B 1 93  ? 40.302 -16.515 -3.338  1.00 13.98 ?  93  LEU   B HD23 1 
ATOM   5413 N  N    . HIS   B 1 94  ? 44.249 -15.338 0.019   1.00 9.73  ?  94  HIS   B N    1 
ATOM   5414 C  CA   . HIS   B 1 94  ? 44.472 -16.243 1.137   1.00 10.04 ?  94  HIS   B CA   1 
ATOM   5415 C  C    . HIS   B 1 94  ? 43.110 -16.596 1.714   1.00 10.45 ?  94  HIS   B C    1 
ATOM   5416 O  O    . HIS   B 1 94  ? 42.442 -15.726 2.271   1.00 11.62 ?  94  HIS   B O    1 
ATOM   5417 C  CB   . HIS   B 1 94  ? 45.343 -15.569 2.194   1.00 10.23 ?  94  HIS   B CB   1 
ATOM   5418 C  CG   . HIS   B 1 94  ? 46.726 -15.268 1.729   1.00 10.30 ?  94  HIS   B CG   1 
ATOM   5419 N  ND1  . HIS   B 1 94  ? 47.753 -16.183 1.811   1.00 10.43 ?  94  HIS   B ND1  1 
ATOM   5420 C  CD2  . HIS   B 1 94  ? 47.231 -14.165 1.127   1.00 10.36 ?  94  HIS   B CD2  1 
ATOM   5421 C  CE1  . HIS   B 1 94  ? 48.841 -15.634 1.302   1.00 10.40 ?  94  HIS   B CE1  1 
ATOM   5422 N  NE2  . HIS   B 1 94  ? 48.553 -14.413 0.878   1.00 10.58 ?  94  HIS   B NE2  1 
ATOM   5423 H  H    . HIS   B 1 94  ? 44.314 -14.499 0.225   1.00 11.68 ?  94  HIS   B H    1 
ATOM   5424 H  HA   . HIS   B 1 94  ? 44.907 -17.049 0.824   1.00 12.05 ?  94  HIS   B HA   1 
ATOM   5425 H  HB2  . HIS   B 1 94  ? 44.927 -14.733 2.451   1.00 12.28 ?  94  HIS   B HB2  1 
ATOM   5426 H  HB3  . HIS   B 1 94  ? 45.408 -16.159 2.957   1.00 12.28 ?  94  HIS   B HB3  1 
ATOM   5427 H  HD2  . HIS   B 1 94  ? 46.773 -13.384 0.925   1.00 12.44 ?  94  HIS   B HD2  1 
ATOM   5428 H  HE1  . HIS   B 1 94  ? 49.673 -16.050 1.247   1.00 12.49 ?  94  HIS   B HE1  1 
ATOM   5429 H  HE2  . HIS   B 1 94  ? 49.110 -13.875 0.509   1.00 12.71 ?  94  HIS   B HE2  1 
ATOM   5430 N  N    . VAL   B 1 95  ? 42.679 -17.850 1.564   1.00 10.20 ?  95  VAL   B N    1 
ATOM   5431 C  CA   . VAL   B 1 95  ? 41.351 -18.285 1.998   1.00 10.23 ?  95  VAL   B CA   1 
ATOM   5432 C  C    . VAL   B 1 95  ? 41.517 -19.321 3.093   1.00 10.54 ?  95  VAL   B C    1 
ATOM   5433 O  O    . VAL   B 1 95  ? 42.287 -20.274 2.934   1.00 11.24 ?  95  VAL   B O    1 
ATOM   5434 C  CB   . VAL   B 1 95  ? 40.530 -18.889 0.840   1.00 10.65 ?  95  VAL   B CB   1 
ATOM   5435 C  CG1  . VAL   B 1 95  ? 39.157 -19.337 1.329   1.00 11.70 ?  95  VAL   B CG1  1 
ATOM   5436 C  CG2  . VAL   B 1 95  ? 40.412 -17.913 -0.303  1.00 10.76 ?  95  VAL   B CG2  1 
ATOM   5437 H  H    . VAL   B 1 95  ? 43.141 -18.478 1.201   1.00 12.24 ?  95  VAL   B H    1 
ATOM   5438 H  HA   . VAL   B 1 95  ? 40.860 -17.530 2.360   1.00 12.28 ?  95  VAL   B HA   1 
ATOM   5439 H  HB   . VAL   B 1 95  ? 40.988 -19.670 0.507   1.00 12.79 ?  95  VAL   B HB   1 
ATOM   5440 H  HG11 . VAL   B 1 95  ? 38.588 -19.525 0.559   1.00 14.05 ?  95  VAL   B HG11 1 
ATOM   5441 H  HG12 . VAL   B 1 95  ? 39.250 -20.141 1.864   1.00 14.05 ?  95  VAL   B HG12 1 
ATOM   5442 H  HG13 . VAL   B 1 95  ? 38.754 -18.631 1.860   1.00 14.05 ?  95  VAL   B HG13 1 
ATOM   5443 H  HG21 . VAL   B 1 95  ? 39.834 -18.299 -0.982  1.00 12.92 ?  95  VAL   B HG21 1 
ATOM   5444 H  HG22 . VAL   B 1 95  ? 40.026 -17.088 0.028   1.00 12.92 ?  95  VAL   B HG22 1 
ATOM   5445 H  HG23 . VAL   B 1 95  ? 41.291 -17.752 -0.665  1.00 12.92 ?  95  VAL   B HG23 1 
ATOM   5446 N  N    . VAL   B 1 96  ? 40.786 -19.149 4.187   1.00 10.77 ?  96  VAL   B N    1 
ATOM   5447 C  CA   . VAL   B 1 96  ? 40.866 -20.064 5.324   1.00 11.47 ?  96  VAL   B CA   1 
ATOM   5448 C  C    . VAL   B 1 96  ? 39.678 -21.024 5.273   1.00 11.82 ?  96  VAL   B C    1 
ATOM   5449 O  O    . VAL   B 1 96  ? 38.559 -20.667 5.650   1.00 12.53 ?  96  VAL   B O    1 
ATOM   5450 C  CB   . VAL   B 1 96  ? 40.914 -19.316 6.659   1.00 12.15 ?  96  VAL   B CB   1 
ATOM   5451 C  CG1  . VAL   B 1 96  ? 41.100 -20.313 7.795   1.00 12.87 ?  96  VAL   B CG1  1 
ATOM   5452 C  CG2  . VAL   B 1 96  ? 42.025 -18.279 6.667   1.00 12.96 ?  96  VAL   B CG2  1 
ATOM   5453 H  H    . VAL   B 1 96  ? 40.227 -18.509 4.299   1.00 12.93 ?  96  VAL   B H    1 
ATOM   5454 H  HA   . VAL   B 1 96  ? 41.677 -20.593 5.252   1.00 13.77 ?  96  VAL   B HA   1 
ATOM   5455 H  HB   . VAL   B 1 96  ? 40.069 -18.861 6.801   1.00 14.59 ?  96  VAL   B HB   1 
ATOM   5456 H  HG11 . VAL   B 1 96  ? 41.287 -19.825 8.616   1.00 15.45 ?  96  VAL   B HG11 1 
ATOM   5457 H  HG12 . VAL   B 1 96  ? 40.290 -20.834 7.904   1.00 15.45 ?  96  VAL   B HG12 1 
ATOM   5458 H  HG13 . VAL   B 1 96  ? 41.846 -20.897 7.587   1.00 15.45 ?  96  VAL   B HG13 1 
ATOM   5459 H  HG21 . VAL   B 1 96  ? 42.074 -17.871 7.549   1.00 15.55 ?  96  VAL   B HG21 1 
ATOM   5460 H  HG22 . VAL   B 1 96  ? 42.866 -18.709 6.457   1.00 15.55 ?  96  VAL   B HG22 1 
ATOM   5461 H  HG23 . VAL   B 1 96  ? 41.826 -17.597 6.004   1.00 15.55 ?  96  VAL   B HG23 1 
ATOM   5462 N  N    . GLY   B 1 97  ? 39.915 -22.253 4.828   1.00 11.81 ?  97  GLY   B N    1 
ATOM   5463 C  CA   . GLY   B 1 97  ? 38.941 -23.310 4.983   1.00 12.55 ?  97  GLY   B CA   1 
ATOM   5464 C  C    . GLY   B 1 97  ? 39.066 -23.923 6.360   1.00 13.59 ?  97  GLY   B C    1 
ATOM   5465 O  O    . GLY   B 1 97  ? 40.106 -23.797 7.018   1.00 14.02 ?  97  GLY   B O    1 
ATOM   5466 H  H    . GLY   B 1 97  ? 40.642 -22.496 4.432   1.00 14.17 ?  97  GLY   B H    1 
ATOM   5467 H  HA2  . GLY   B 1 97  ? 38.046 -22.940 4.865   1.00 15.07 ?  97  GLY   B HA2  1 
ATOM   5468 H  HA3  . GLY   B 1 97  ? 39.083 -23.991 4.305   1.00 15.07 ?  97  GLY   B HA3  1 
ATOM   5469 N  N    . PRO   B 1 98  ? 38.018 -24.605 6.823   1.00 14.68 ?  98  PRO   B N    1 
ATOM   5470 C  CA   . PRO   B 1 98  ? 38.112 -25.300 8.110   1.00 15.55 ?  98  PRO   B CA   1 
ATOM   5471 C  C    . PRO   B 1 98  ? 39.139 -26.420 8.067   1.00 15.24 ?  98  PRO   B C    1 
ATOM   5472 O  O    . PRO   B 1 98  ? 39.248 -27.156 7.088   1.00 15.48 ?  98  PRO   B O    1 
ATOM   5473 C  CB   . PRO   B 1 98  ? 36.695 -25.847 8.321   1.00 15.78 ?  98  PRO   B CB   1 
ATOM   5474 C  CG   . PRO   B 1 98  ? 36.129 -25.980 6.952   1.00 15.39 ?  98  PRO   B CG   1 
ATOM   5475 C  CD   . PRO   B 1 98  ? 36.700 -24.800 6.190   1.00 14.54 ?  98  PRO   B CD   1 
ATOM   5476 H  HA   . PRO   B 1 98  ? 38.337 -24.676 8.812   1.00 18.66 ?  98  PRO   B HA   1 
ATOM   5477 H  HB2  . PRO   B 1 98  ? 36.744 -26.712 8.759   1.00 18.94 ?  98  PRO   B HB2  1 
ATOM   5478 H  HB3  . PRO   B 1 98  ? 36.180 -25.221 8.846   1.00 18.94 ?  98  PRO   B HB3  1 
ATOM   5479 H  HG2  . PRO   B 1 98  ? 36.419 -26.822 6.557   1.00 18.48 ?  98  PRO   B HG2  1 
ATOM   5480 H  HG3  . PRO   B 1 98  ? 35.162 -25.937 6.992   1.00 18.48 ?  98  PRO   B HG3  1 
ATOM   5481 H  HD2  . PRO   B 1 98  ? 36.791 -25.021 5.246   1.00 17.45 ?  98  PRO   B HD2  1 
ATOM   5482 H  HD3  . PRO   B 1 98  ? 36.145 -24.015 6.317   1.00 17.45 ?  98  PRO   B HD3  1 
ATOM   5483 N  N    . ASN   B 1 99  ? 39.891 -26.547 9.153   1.00 16.37 ?  99  ASN   B N    1 
ATOM   5484 C  CA   . ASN   B 1 99  ? 40.871 -27.617 9.317   1.00 17.29 ?  99  ASN   B CA   1 
ATOM   5485 C  C    . ASN   B 1 99  ? 40.247 -28.700 10.194  1.00 19.84 ?  99  ASN   B C    1 
ATOM   5486 O  O    . ASN   B 1 99  ? 40.176 -28.559 11.417  1.00 20.29 ?  99  ASN   B O    1 
ATOM   5487 C  CB   . ASN   B 1 99  ? 42.146 -27.061 9.937   1.00 17.53 ?  99  ASN   B CB   1 
ATOM   5488 C  CG   . ASN   B 1 99  ? 43.276 -28.066 9.946   1.00 18.28 ?  99  ASN   B CG   1 
ATOM   5489 O  OD1  . ASN   B 1 99  ? 43.053 -29.255 10.120  1.00 18.86 ?  99  ASN   B OD1  1 
ATOM   5490 N  ND2  . ASN   B 1 99  ? 44.493 -27.593 9.752   1.00 18.36 ?  99  ASN   B ND2  1 
ATOM   5491 H  H    . ASN   B 1 99  ? 39.848 -26.008 9.818   1.00 19.64 ?  99  ASN   B H    1 
ATOM   5492 H  HA   . ASN   B 1 99  ? 41.079 -28.006 8.454   1.00 20.76 ?  99  ASN   B HA   1 
ATOM   5493 H  HB2  . ASN   B 1 99  ? 42.426 -26.290 9.431   1.00 21.04 ?  99  ASN   B HB2  1 
ATOM   5494 H  HB3  . ASN   B 1 99  ? 41.957 -26.812 10.857  1.00 21.04 ?  99  ASN   B HB3  1 
ATOM   5495 H  HD21 . ASN   B 1 99  ? 45.163 -28.128 9.744   1.00 22.04 ?  99  ASN   B HD21 1 
ATOM   5496 H  HD22 . ASN   B 1 99  ? 44.605 -26.751 9.637   1.00 22.04 ?  99  ASN   B HD22 1 
ATOM   5497 N  N    A VAL   B 1 100 ? 39.775 -29.777 9.560   0.68 21.68 ?  100 VAL   B N    1 
ATOM   5498 N  N    B VAL   B 1 100 ? 39.795 -29.784 9.556   0.32 21.86 ?  100 VAL   B N    1 
ATOM   5499 C  CA   A VAL   B 1 100 ? 39.166 -30.873 10.312  0.68 24.21 ?  100 VAL   B CA   1 
ATOM   5500 C  CA   B VAL   B 1 100 ? 39.172 -30.885 10.288  0.32 24.07 ?  100 VAL   B CA   1 
ATOM   5501 C  C    A VAL   B 1 100 ? 40.178 -31.534 11.240  0.68 24.76 ?  100 VAL   B C    1 
ATOM   5502 C  C    B VAL   B 1 100 ? 40.172 -31.555 11.220  0.32 24.76 ?  100 VAL   B C    1 
ATOM   5503 O  O    A VAL   B 1 100 ? 39.811 -32.041 12.307  0.68 25.27 ?  100 VAL   B O    1 
ATOM   5504 O  O    B VAL   B 1 100 ? 39.794 -32.082 12.274  0.32 24.98 ?  100 VAL   B O    1 
ATOM   5505 C  CB   A VAL   B 1 100 ? 38.510 -31.887 9.352   0.68 26.34 ?  100 VAL   B CB   1 
ATOM   5506 C  CB   B VAL   B 1 100 ? 38.537 -31.883 9.298   0.32 25.53 ?  100 VAL   B CB   1 
ATOM   5507 C  CG1  A VAL   B 1 100 ? 38.024 -33.111 10.116  0.68 27.15 ?  100 VAL   B CG1  1 
ATOM   5508 C  CG1  B VAL   B 1 100 ? 38.016 -33.112 10.030  0.32 26.06 ?  100 VAL   B CG1  1 
ATOM   5509 C  CG2  A VAL   B 1 100 ? 37.356 -31.237 8.607   0.68 26.86 ?  100 VAL   B CG2  1 
ATOM   5510 C  CG2  B VAL   B 1 100 ? 37.413 -31.212 8.523   0.32 25.94 ?  100 VAL   B CG2  1 
ATOM   5511 H  H    A VAL   B 1 100 ? 39.783 -29.888 8.705   0.68 26.02 ?  100 VAL   B H    1 
ATOM   5512 H  H    B VAL   B 1 100 ? 39.834 -29.902 8.705   0.32 26.23 ?  100 VAL   B H    1 
ATOM   5513 H  HA   A VAL   B 1 100 ? 38.455 -30.508 10.864  0.68 29.06 ?  100 VAL   B HA   1 
ATOM   5514 H  HA   B VAL   B 1 100 ? 38.455 -30.527 10.833  0.32 28.89 ?  100 VAL   B HA   1 
ATOM   5515 H  HB   A VAL   B 1 100 ? 39.166 -32.183 8.702   0.68 31.62 ?  100 VAL   B HB   1 
ATOM   5516 H  HB   B VAL   B 1 100 ? 39.209 -32.176 8.663   0.32 30.64 ?  100 VAL   B HB   1 
ATOM   5517 H  HG11 A VAL   B 1 100 ? 37.430 -33.624 9.545   0.68 32.59 ?  100 VAL   B HG11 1 
ATOM   5518 H  HG11 B VAL   B 1 100 ? 37.443 -33.616 9.430   0.32 31.28 ?  100 VAL   B HG11 1 
ATOM   5519 H  HG12 A VAL   B 1 100 ? 38.786 -33.656 10.369  0.68 32.59 ?  100 VAL   B HG12 1 
ATOM   5520 H  HG12 B VAL   B 1 100 ? 38.767 -33.661 10.306  0.32 31.28 ?  100 VAL   B HG12 1 
ATOM   5521 H  HG13 A VAL   B 1 100 ? 37.546 -32.821 10.909  0.68 32.59 ?  100 VAL   B HG13 1 
ATOM   5522 H  HG13 B VAL   B 1 100 ? 37.509 -32.827 10.806  0.32 31.28 ?  100 VAL   B HG13 1 
ATOM   5523 H  HG21 A VAL   B 1 100 ? 36.949 -31.894 8.020   0.68 32.24 ?  100 VAL   B HG21 1 
ATOM   5524 H  HG21 B VAL   B 1 100 ? 37.005 -31.862 7.931   0.32 31.14 ?  100 VAL   B HG21 1 
ATOM   5525 H  HG22 A VAL   B 1 100 ? 36.703 -30.921 9.252   0.68 32.24 ?  100 VAL   B HG22 1 
ATOM   5526 H  HG22 B VAL   B 1 100 ? 36.754 -30.877 9.152   0.32 31.14 ?  100 VAL   B HG22 1 
ATOM   5527 H  HG23 A VAL   B 1 100 ? 37.695 -30.493 8.088   0.68 32.24 ?  100 VAL   B HG23 1 
ATOM   5528 H  HG23 B VAL   B 1 100 ? 37.781 -30.478 8.008   0.32 31.14 ?  100 VAL   B HG23 1 
ATOM   5529 N  N    . ASN   B 1 101 ? 41.455 -31.563 10.851  1.00 25.29 ?  101 ASN   B N    1 
ATOM   5530 C  CA   . ASN   B 1 101 ? 42.492 -32.098 11.731  1.00 27.11 ?  101 ASN   B CA   1 
ATOM   5531 C  C    . ASN   B 1 101 ? 42.687 -31.261 12.989  1.00 29.42 ?  101 ASN   B C    1 
ATOM   5532 O  O    . ASN   B 1 101 ? 43.327 -31.737 13.936  1.00 30.57 ?  101 ASN   B O    1 
ATOM   5533 C  CB   . ASN   B 1 101 ? 43.817 -32.235 10.978  1.00 27.13 ?  101 ASN   B CB   1 
ATOM   5534 C  CG   . ASN   B 1 101 ? 43.809 -33.391 9.995   1.00 26.66 ?  101 ASN   B CG   1 
ATOM   5535 O  OD1  . ASN   B 1 101 ? 43.144 -34.394 10.216  1.00 27.41 ?  101 ASN   B OD1  1 
ATOM   5536 N  ND2  . ASN   B 1 101 ? 44.544 -33.249 8.900   1.00 25.99 ?  101 ASN   B ND2  1 
ATOM   5537 H  H    A ASN   B 1 101 ? 41.739 -31.298 10.083  0.68 30.36 ?  101 ASN   B H    1 
ATOM   5538 H  H    B ASN   B 1 101 ? 41.746 -31.277 10.094  0.32 30.36 ?  101 ASN   B H    1 
ATOM   5539 H  HA   . ASN   B 1 101 ? 42.224 -32.981 12.018  1.00 32.54 ?  101 ASN   B HA   1 
ATOM   5540 H  HB2  . ASN   B 1 101 ? 43.993 -31.425 10.479  1.00 32.56 ?  101 ASN   B HB2  1 
ATOM   5541 H  HB3  . ASN   B 1 101 ? 44.531 -32.390 11.621  1.00 32.56 ?  101 ASN   B HB3  1 
ATOM   5542 H  HD21 . ASN   B 1 101 ? 44.572 -33.882 8.318   1.00 31.19 ?  101 ASN   B HD21 1 
ATOM   5543 H  HD22 . ASN   B 1 101 ? 44.990 -32.527 8.774   1.00 31.19 ?  101 ASN   B HD22 1 
ATOM   5544 N  N    . LYS   B 1 102 ? 42.160 -30.035 13.016  1.00 31.74 ?  102 LYS   B N    1 
ATOM   5545 C  CA   . LYS   B 1 102 ? 42.118 -29.205 14.213  1.00 34.54 ?  102 LYS   B CA   1 
ATOM   5546 C  C    . LYS   B 1 102 ? 40.730 -29.164 14.841  1.00 33.84 ?  102 LYS   B C    1 
ATOM   5547 O  O    . LYS   B 1 102 ? 40.493 -28.354 15.742  1.00 34.39 ?  102 LYS   B O    1 
ATOM   5548 C  CB   . LYS   B 1 102 ? 42.562 -27.776 13.892  1.00 38.00 ?  102 LYS   B CB   1 
ATOM   5549 C  CG   . LYS   B 1 102 ? 44.022 -27.618 13.505  1.00 41.19 ?  102 LYS   B CG   1 
ATOM   5550 C  CD   . LYS   B 1 102 ? 44.280 -26.193 13.039  1.00 44.01 ?  102 LYS   B CD   1 
ATOM   5551 C  CE   . LYS   B 1 102 ? 45.751 -25.925 12.781  1.00 46.07 ?  102 LYS   B CE   1 
ATOM   5552 N  NZ   . LYS   B 1 102 ? 45.961 -24.529 12.295  1.00 47.26 ?  102 LYS   B NZ   1 
ATOM   5553 H  H    . LYS   B 1 102 ? 41.805 -29.652 12.331  1.00 38.10 ?  102 LYS   B H    1 
ATOM   5554 H  HA   . LYS   B 1 102 ? 42.735 -29.565 14.868  1.00 41.45 ?  102 LYS   B HA   1 
ATOM   5555 H  HB2  . LYS   B 1 102 ? 42.029 -27.445 13.153  1.00 45.61 ?  102 LYS   B HB2  1 
ATOM   5556 H  HB3  . LYS   B 1 102 ? 42.409 -27.222 14.675  1.00 45.61 ?  102 LYS   B HB3  1 
ATOM   5557 H  HG2  . LYS   B 1 102 ? 44.585 -27.797 14.276  1.00 49.44 ?  102 LYS   B HG2  1 
ATOM   5558 H  HG3  . LYS   B 1 102 ? 44.235 -28.225 12.779  1.00 49.44 ?  102 LYS   B HG3  1 
ATOM   5559 H  HD2  . LYS   B 1 102 ? 43.795 -26.038 12.213  1.00 52.82 ?  102 LYS   B HD2  1 
ATOM   5560 H  HD3  . LYS   B 1 102 ? 43.976 -25.576 13.723  1.00 52.82 ?  102 LYS   B HD3  1 
ATOM   5561 H  HE2  . LYS   B 1 102 ? 46.249 -26.040 13.606  1.00 55.29 ?  102 LYS   B HE2  1 
ATOM   5562 H  HE3  . LYS   B 1 102 ? 46.076 -26.537 12.102  1.00 55.29 ?  102 LYS   B HE3  1 
ATOM   5563 H  HZ1  . LYS   B 1 102 ? 46.826 -24.384 12.148  1.00 56.71 ?  102 LYS   B HZ1  1 
ATOM   5564 H  HZ2  . LYS   B 1 102 ? 45.512 -24.400 11.537  1.00 56.71 ?  102 LYS   B HZ2  1 
ATOM   5565 H  HZ3  . LYS   B 1 102 ? 45.670 -23.948 12.904  1.00 56.71 ?  102 LYS   B HZ3  1 
ATOM   5566 N  N    . GLY   B 1 103 ? 39.805 -29.999 14.373  1.00 33.04 ?  103 GLY   B N    1 
ATOM   5567 C  CA   . GLY   B 1 103 ? 38.472 -30.050 14.939  1.00 32.59 ?  103 GLY   B CA   1 
ATOM   5568 C  C    . GLY   B 1 103 ? 37.530 -28.961 14.481  1.00 31.53 ?  103 GLY   B C    1 
ATOM   5569 O  O    . GLY   B 1 103 ? 36.430 -28.843 15.034  1.00 32.01 ?  103 GLY   B O    1 
ATOM   5570 H  H    . GLY   B 1 103 ? 39.930 -30.546 13.723  1.00 39.65 ?  103 GLY   B H    1 
ATOM   5571 H  HA2  . GLY   B 1 103 ? 38.071 -30.905 14.717  1.00 39.11 ?  103 GLY   B HA2  1 
ATOM   5572 H  HA3  . GLY   B 1 103 ? 38.539 -29.995 15.906  1.00 39.11 ?  103 GLY   B HA3  1 
ATOM   5573 N  N    A GLU   B 1 104 ? 37.926 -28.153 13.500  0.68 30.27 ?  104 GLU   B N    1 
ATOM   5574 N  N    B GLU   B 1 104 ? 37.911 -28.170 13.482  0.32 30.98 ?  104 GLU   B N    1 
ATOM   5575 C  CA   A GLU   B 1 104 ? 37.088 -27.056 13.043  0.68 28.94 ?  104 GLU   B CA   1 
ATOM   5576 C  CA   B GLU   B 1 104 ? 37.053 -27.092 13.016  0.32 30.23 ?  104 GLU   B CA   1 
ATOM   5577 C  C    A GLU   B 1 104 ? 35.903 -27.583 12.234  0.68 29.14 ?  104 GLU   B C    1 
ATOM   5578 C  C    B GLU   B 1 104 ? 35.891 -27.643 12.190  0.32 30.32 ?  104 GLU   B C    1 
ATOM   5579 O  O    A GLU   B 1 104 ? 35.939 -28.674 11.656  0.68 29.59 ?  104 GLU   B O    1 
ATOM   5580 O  O    B GLU   B 1 104 ? 35.964 -28.726 11.602  0.32 30.48 ?  104 GLU   B O    1 
ATOM   5581 C  CB   A GLU   B 1 104 ? 37.922 -26.061 12.235  0.68 27.75 ?  104 GLU   B CB   1 
ATOM   5582 C  CB   B GLU   B 1 104 ? 37.872 -26.078 12.218  0.32 29.42 ?  104 GLU   B CB   1 
ATOM   5583 C  CG   A GLU   B 1 104 ? 39.030 -25.425 13.066  0.68 26.52 ?  104 GLU   B CG   1 
ATOM   5584 C  CG   B GLU   B 1 104 ? 38.970 -25.432 13.053  0.32 28.67 ?  104 GLU   B CG   1 
ATOM   5585 C  CD   A GLU   B 1 104 ? 39.957 -24.535 12.267  0.68 25.13 ?  104 GLU   B CD   1 
ATOM   5586 C  CD   B GLU   B 1 104 ? 39.914 -24.570 12.240  0.32 27.96 ?  104 GLU   B CD   1 
ATOM   5587 O  OE1  A GLU   B 1 104 ? 39.948 -24.597 11.020  0.68 23.33 ?  104 GLU   B OE1  1 
ATOM   5588 O  OE1  B GLU   B 1 104 ? 39.839 -24.600 10.994  0.32 27.39 ?  104 GLU   B OE1  1 
ATOM   5589 O  OE2  A GLU   B 1 104 ? 40.707 -23.768 12.904  0.68 25.12 -1 104 GLU   B OE2  1 
ATOM   5590 O  OE2  B GLU   B 1 104 ? 40.736 -23.859 12.854  0.32 27.86 -1 104 GLU   B OE2  1 
ATOM   5591 H  H    A GLU   B 1 104 ? 38.680 -28.215 13.093  0.68 36.33 ?  104 GLU   B H    1 
ATOM   5592 H  H    B GLU   B 1 104 ? 38.660 -28.234 13.066  0.32 37.18 ?  104 GLU   B H    1 
ATOM   5593 H  HA   A GLU   B 1 104 ? 36.741 -26.585 13.818  0.68 34.74 ?  104 GLU   B HA   1 
ATOM   5594 H  HA   B GLU   B 1 104 ? 36.681 -26.633 13.783  0.32 36.29 ?  104 GLU   B HA   1 
ATOM   5595 H  HB2  A GLU   B 1 104 ? 38.335 -26.523 11.489  0.68 33.31 ?  104 GLU   B HB2  1 
ATOM   5596 H  HB2  B GLU   B 1 104 ? 38.290 -26.526 11.466  0.32 35.31 ?  104 GLU   B HB2  1 
ATOM   5597 H  HB3  A GLU   B 1 104 ? 37.346 -25.351 11.910  0.68 33.31 ?  104 GLU   B HB3  1 
ATOM   5598 H  HB3  B GLU   B 1 104 ? 37.284 -25.374 11.900  0.32 35.31 ?  104 GLU   B HB3  1 
ATOM   5599 H  HG2  A GLU   B 1 104 ? 38.631 -24.881 13.764  0.68 31.83 ?  104 GLU   B HG2  1 
ATOM   5600 H  HG2  B GLU   B 1 104 ? 38.561 -24.871 13.731  0.32 34.41 ?  104 GLU   B HG2  1 
ATOM   5601 H  HG3  A GLU   B 1 104 ? 39.571 -26.123 13.465  0.68 31.83 ?  104 GLU   B HG3  1 
ATOM   5602 H  HG3  B GLU   B 1 104 ? 39.495 -26.130 13.478  0.32 34.41 ?  104 GLU   B HG3  1 
ATOM   5603 N  N    A ASP   B 1 105 ? 34.838 -26.783 12.201  0.68 28.88 ?  105 ASP   B N    1 
ATOM   5604 N  N    B ASP   B 1 105 ? 34.804 -26.874 12.155  0.32 30.17 ?  105 ASP   B N    1 
ATOM   5605 C  CA   A ASP   B 1 105 ? 33.560 -27.231 11.659  0.68 29.28 ?  105 ASP   B CA   1 
ATOM   5606 C  CA   B ASP   B 1 105 ? 33.543 -27.343 11.594  0.32 30.21 ?  105 ASP   B CA   1 
ATOM   5607 C  C    A ASP   B 1 105 ? 33.612 -27.283 10.136  0.68 27.20 ?  105 ASP   B C    1 
ATOM   5608 C  C    B ASP   B 1 105 ? 33.620 -27.359 10.071  0.32 29.13 ?  105 ASP   B C    1 
ATOM   5609 O  O    A ASP   B 1 105 ? 33.776 -26.253 9.475   0.68 26.15 ?  105 ASP   B O    1 
ATOM   5610 O  O    B ASP   B 1 105 ? 33.833 -26.318 9.440   0.32 28.82 ?  105 ASP   B O    1 
ATOM   5611 C  CB   A ASP   B 1 105 ? 32.448 -26.290 12.120  0.68 32.20 ?  105 ASP   B CB   1 
ATOM   5612 C  CB   B ASP   B 1 105 ? 32.400 -26.444 12.063  0.32 31.30 ?  105 ASP   B CB   1 
ATOM   5613 C  CG   A ASP   B 1 105 ? 31.070 -26.764 11.698  0.68 34.46 ?  105 ASP   B CG   1 
ATOM   5614 C  CG   B ASP   B 1 105 ? 31.034 -27.013 11.724  0.32 32.16 ?  105 ASP   B CG   1 
ATOM   5615 O  OD1  A ASP   B 1 105 ? 30.964 -27.873 11.133  0.68 34.80 ?  105 ASP   B OD1  1 
ATOM   5616 O  OD1  B ASP   B 1 105 ? 30.974 -28.039 11.013  0.32 32.36 ?  105 ASP   B OD1  1 
ATOM   5617 O  OD2  A ASP   B 1 105 ? 30.089 -26.024 11.930  0.68 35.63 -1 105 ASP   B OD2  1 
ATOM   5618 O  OD2  B ASP   B 1 105 ? 30.019 -26.441 12.175  0.32 32.47 -1 105 ASP   B OD2  1 
ATOM   5619 H  H    A ASP   B 1 105 ? 34.834 -25.973 12.486  0.68 34.66 ?  105 ASP   B H    1 
ATOM   5620 H  H    B ASP   B 1 105 ? 34.773 -26.068 12.450  0.32 36.21 ?  105 ASP   B H    1 
ATOM   5621 H  HA   A ASP   B 1 105 ? 33.364 -28.120 11.991  0.68 35.14 ?  105 ASP   B HA   1 
ATOM   5622 H  HA   B ASP   B 1 105 ? 33.365 -28.245 11.901  0.32 36.26 ?  105 ASP   B HA   1 
ATOM   5623 H  HB2  A ASP   B 1 105 ? 32.472 -26.220 13.089  0.68 38.64 ?  105 ASP   B HB2  1 
ATOM   5624 H  HB2  B ASP   B 1 105 ? 32.450 -26.343 13.028  0.32 37.56 ?  105 ASP   B HB2  1 
ATOM   5625 H  HB3  A ASP   B 1 105 ? 32.587 -25.416 11.723  0.68 38.64 ?  105 ASP   B HB3  1 
ATOM   5626 H  HB3  B ASP   B 1 105 ? 32.485 -25.574 11.638  0.32 37.56 ?  105 ASP   B HB3  1 
ATOM   5627 N  N    A ILE   B 1 106 ? 33.439 -28.486 9.581   0.68 26.75 ?  106 ILE   B N    1 
ATOM   5628 N  N    B ILE   B 1 106 ? 33.435 -28.545 9.484   0.32 28.40 ?  106 ILE   B N    1 
ATOM   5629 C  CA   A ILE   B 1 106 ? 33.440 -28.672 8.135   0.68 25.80 ?  106 ILE   B CA   1 
ATOM   5630 C  CA   B ILE   B 1 106 ? 33.445 -28.693 8.033   0.32 27.76 ?  106 ILE   B CA   1 
ATOM   5631 C  C    A ILE   B 1 106 ? 32.343 -27.856 7.460   0.68 24.64 ?  106 ILE   B C    1 
ATOM   5632 C  C    B ILE   B 1 106 ? 32.344 -27.873 7.373   0.32 27.04 ?  106 ILE   B C    1 
ATOM   5633 O  O    A ILE   B 1 106 ? 32.449 -27.540 6.271   0.68 23.72 ?  106 ILE   B O    1 
ATOM   5634 O  O    B ILE   B 1 106 ? 32.424 -27.583 6.174   0.32 26.76 ?  106 ILE   B O    1 
ATOM   5635 C  CB   A ILE   B 1 106 ? 33.334 -30.179 7.807   0.68 26.52 ?  106 ILE   B CB   1 
ATOM   5636 C  CB   B ILE   B 1 106 ? 33.349 -30.192 7.666   0.32 27.96 ?  106 ILE   B CB   1 
ATOM   5637 C  CG1  A ILE   B 1 106 ? 33.594 -30.435 6.322   0.68 26.77 ?  106 ILE   B CG1  1 
ATOM   5638 C  CG1  B ILE   B 1 106 ? 33.618 -30.413 6.175   0.32 27.97 ?  106 ILE   B CG1  1 
ATOM   5639 C  CG2  A ILE   B 1 106 ? 31.967 -30.718 8.208   0.68 27.05 ?  106 ILE   B CG2  1 
ATOM   5640 C  CG2  B ILE   B 1 106 ? 31.985 -30.752 8.046   0.32 28.24 ?  106 ILE   B CG2  1 
ATOM   5641 C  CD1  A ILE   B 1 106 ? 34.966 -30.000 5.864   0.68 26.81 ?  106 ILE   B CD1  1 
ATOM   5642 C  CD1  B ILE   B 1 106 ? 34.979 -29.936 5.727   0.32 27.98 ?  106 ILE   B CD1  1 
ATOM   5643 H  H    A ILE   B 1 106 ? 33.319 -29.207 10.028  0.68 32.10 ?  106 ILE   B H    1 
ATOM   5644 H  H    B ILE   B 1 106 ? 33.311 -29.279 9.909   0.32 34.09 ?  106 ILE   B H    1 
ATOM   5645 H  HA   A ILE   B 1 106 ? 34.287 -28.354 7.795   0.68 30.96 ?  106 ILE   B HA   1 
ATOM   5646 H  HA   B ILE   B 1 106 ? 34.290 -28.360 7.704   0.32 33.32 ?  106 ILE   B HA   1 
ATOM   5647 H  HB   A ILE   B 1 106 ? 34.008 -30.651 8.321   0.68 31.83 ?  106 ILE   B HB   1 
ATOM   5648 H  HB   B ILE   B 1 106 ? 34.023 -30.671 8.169   0.32 33.56 ?  106 ILE   B HB   1 
ATOM   5649 H  HG12 A ILE   B 1 106 ? 33.517 -31.388 6.151   0.68 32.13 ?  106 ILE   B HG12 1 
ATOM   5650 H  HG12 B ILE   B 1 106 ? 33.564 -31.365 5.986   0.32 33.57 ?  106 ILE   B HG12 1 
ATOM   5651 H  HG13 A ILE   B 1 106 ? 32.939 -29.953 5.797   0.68 32.13 ?  106 ILE   B HG13 1 
ATOM   5652 H  HG13 B ILE   B 1 106 ? 32.951 -29.939 5.658   0.32 33.57 ?  106 ILE   B HG13 1 
ATOM   5653 H  HG21 A ILE   B 1 106 ? 31.979 -31.685 8.144   0.68 32.47 ?  106 ILE   B HG21 1 
ATOM   5654 H  HG21 B ILE   B 1 106 ? 32.002 -31.717 7.946   0.32 33.90 ?  106 ILE   B HG21 1 
ATOM   5655 H  HG22 A ILE   B 1 106 ? 31.777 -30.449 9.121   0.68 32.47 ?  106 ILE   B HG22 1 
ATOM   5656 H  HG22 B ILE   B 1 106 ? 31.796 -30.520 8.969   0.32 33.90 ?  106 ILE   B HG22 1 
ATOM   5657 H  HG23 A ILE   B 1 106 ? 31.295 -30.355 7.610   0.68 32.47 ?  106 ILE   B HG23 1 
ATOM   5658 H  HG23 B ILE   B 1 106 ? 31.310 -30.371 7.464   0.32 33.90 ?  106 ILE   B HG23 1 
ATOM   5659 H  HD11 A ILE   B 1 106 ? 35.156 -30.408 5.006   0.68 32.18 ?  106 ILE   B HD11 1 
ATOM   5660 H  HD11 B ILE   B 1 106 ? 35.179 -30.325 4.862   0.32 33.58 ?  106 ILE   B HD11 1 
ATOM   5661 H  HD12 A ILE   B 1 106 ? 34.981 -29.033 5.780   0.68 32.18 ?  106 ILE   B HD12 1 
ATOM   5662 H  HD12 B ILE   B 1 106 ? 34.968 -28.969 5.660   0.32 33.58 ?  106 ILE   B HD12 1 
ATOM   5663 H  HD13 A ILE   B 1 106 ? 35.624 -30.286 6.518   0.68 32.18 ?  106 ILE   B HD13 1 
ATOM   5664 H  HD13 B ILE   B 1 106 ? 35.641 -30.217 6.378   0.32 33.58 ?  106 ILE   B HD13 1 
ATOM   5665 N  N    A GLN   B 1 107 ? 31.288 -27.495 8.194   0.68 25.13 ?  107 GLN   B N    1 
ATOM   5666 N  N    B GLN   B 1 107 ? 31.313 -27.486 8.128   0.32 26.90 ?  107 GLN   B N    1 
ATOM   5667 C  CA   A GLN   B 1 107 ? 30.221 -26.682 7.620   0.68 25.56 ?  107 GLN   B CA   1 
ATOM   5668 C  CA   B GLN   B 1 107 ? 30.234 -26.682 7.567   0.32 26.68 ?  107 GLN   B CA   1 
ATOM   5669 C  C    A GLN   B 1 107 ? 30.722 -25.338 7.101   0.68 23.51 ?  107 GLN   B C    1 
ATOM   5670 C  C    B GLN   B 1 107 ? 30.717 -25.317 7.097   0.32 24.19 ?  107 GLN   B C    1 
ATOM   5671 O  O    A GLN   B 1 107 ? 30.088 -24.763 6.211   0.68 23.84 ?  107 GLN   B O    1 
ATOM   5672 O  O    B GLN   B 1 107 ? 30.063 -24.702 6.248   0.32 24.40 ?  107 GLN   B O    1 
ATOM   5673 C  CB   A GLN   B 1 107 ? 29.116 -26.465 8.657   0.68 29.16 ?  107 GLN   B CB   1 
ATOM   5674 C  CB   B GLN   B 1 107 ? 29.117 -26.521 8.604   0.32 29.15 ?  107 GLN   B CB   1 
ATOM   5675 C  CG   A GLN   B 1 107 ? 27.789 -25.968 8.084   0.68 32.61 ?  107 GLN   B CG   1 
ATOM   5676 C  CG   B GLN   B 1 107 ? 27.792 -26.012 8.047   0.32 31.43 ?  107 GLN   B CG   1 
ATOM   5677 C  CD   A GLN   B 1 107 ? 27.725 -24.455 7.948   0.68 35.20 ?  107 GLN   B CD   1 
ATOM   5678 C  CD   B GLN   B 1 107 ? 27.699 -24.496 8.035   0.32 33.22 ?  107 GLN   B CD   1 
ATOM   5679 O  OE1  A GLN   B 1 107 ? 28.552 -23.733 8.507   0.68 36.13 ?  107 GLN   B OE1  1 
ATOM   5680 O  OE1  B GLN   B 1 107 ? 28.529 -23.805 8.626   0.32 33.82 ?  107 GLN   B OE1  1 
ATOM   5681 N  NE2  A GLN   B 1 107 ? 26.734 -23.969 7.204   0.68 36.11 ?  107 GLN   B NE2  1 
ATOM   5682 N  NE2  B GLN   B 1 107 ? 26.679 -23.973 7.362   0.32 33.86 ?  107 GLN   B NE2  1 
ATOM   5683 H  H    A GLN   B 1 107 ? 31.168 -27.710 9.012   0.68 30.16 ?  107 GLN   B H    1 
ATOM   5684 H  H    B GLN   B 1 107 ? 31.217 -27.674 8.959   0.32 32.29 ?  107 GLN   B H    1 
ATOM   5685 H  HA   A GLN   B 1 107 ? 29.832 -27.159 6.870   0.68 30.67 ?  107 GLN   B HA   1 
ATOM   5686 H  HA   B GLN   B 1 107 ? 29.862 -27.144 6.801   0.32 32.02 ?  107 GLN   B HA   1 
ATOM   5687 H  HB2  A GLN   B 1 107 ? 28.944 -27.307 9.101   0.68 35.00 ?  107 GLN   B HB2  1 
ATOM   5688 H  HB2  B GLN   B 1 107 ? 28.949 -27.384 9.006   0.32 34.98 ?  107 GLN   B HB2  1 
ATOM   5689 H  HB3  A GLN   B 1 107 ? 29.423 -25.811 9.304   0.68 35.00 ?  107 GLN   B HB3  1 
ATOM   5690 H  HB3  B GLN   B 1 107 ? 29.412 -25.896 9.284   0.32 34.98 ?  107 GLN   B HB3  1 
ATOM   5691 H  HG2  A GLN   B 1 107 ? 27.661 -26.350 7.202   0.68 39.13 ?  107 GLN   B HG2  1 
ATOM   5692 H  HG2  B GLN   B 1 107 ? 27.689 -26.324 7.135   0.32 37.73 ?  107 GLN   B HG2  1 
ATOM   5693 H  HG3  A GLN   B 1 107 ? 27.068 -26.248 8.672   0.68 39.13 ?  107 GLN   B HG3  1 
ATOM   5694 H  HG3  B GLN   B 1 107 ? 27.067 -26.355 8.597   0.32 37.73 ?  107 GLN   B HG3  1 
ATOM   5695 H  HE21 A GLN   B 1 107 ? 26.174 -24.504 6.827   0.68 43.33 ?  107 GLN   B HE21 1 
ATOM   5696 H  HE21 B GLN   B 1 107 ? 26.118 -24.487 6.961   0.32 40.63 ?  107 GLN   B HE21 1 
ATOM   5697 H  HE22 A GLN   B 1 107 ? 26.649 -23.118 7.098   0.68 43.33 ?  107 GLN   B HE22 1 
ATOM   5698 H  HE22 B GLN   B 1 107 ? 26.580 -23.119 7.328   0.32 40.63 ?  107 GLN   B HE22 1 
ATOM   5699 N  N    . LEU   B 1 108 ? 31.846 -24.832 7.619   1.00 21.61 ?  108 LEU   B N    1 
ATOM   5700 C  CA   . LEU   B 1 108 ? 32.387 -23.535 7.207   1.00 18.97 ?  108 LEU   B CA   1 
ATOM   5701 C  C    . LEU   B 1 108 ? 33.033 -23.560 5.832   1.00 16.49 ?  108 LEU   B C    1 
ATOM   5702 O  O    . LEU   B 1 108 ? 33.463 -22.505 5.343   1.00 15.90 ?  108 LEU   B O    1 
ATOM   5703 C  CB   . LEU   B 1 108 ? 33.393 -23.035 8.244   1.00 19.55 ?  108 LEU   B CB   1 
ATOM   5704 C  CG   . LEU   B 1 108 ? 32.771 -22.541 9.549   1.00 21.03 ?  108 LEU   B CG   1 
ATOM   5705 C  CD1  . LEU   B 1 108 ? 33.796 -22.507 10.667  1.00 21.42 ?  108 LEU   B CD1  1 
ATOM   5706 C  CD2  . LEU   B 1 108 ? 32.173 -21.158 9.341   1.00 21.96 ?  108 LEU   B CD2  1 
ATOM   5707 H  H    A LEU   B 1 108 ? 32.310 -25.224 8.223   0.68 25.94 ?  108 LEU   B H    1 
ATOM   5708 H  H    B LEU   B 1 108 ? 32.308 -25.231 8.220   0.32 25.94 ?  108 LEU   B H    1 
ATOM   5709 H  HA   . LEU   B 1 108 ? 31.658 -22.897 7.173   1.00 22.77 ?  108 LEU   B HA   1 
ATOM   5710 H  HB2  . LEU   B 1 108 ? 33.996 -23.759 8.467   1.00 23.47 ?  108 LEU   B HB2  1 
ATOM   5711 H  HB3  . LEU   B 1 108 ? 33.892 -22.298 7.862   1.00 23.47 ?  108 LEU   B HB3  1 
ATOM   5712 H  HG   . LEU   B 1 108 ? 32.054 -23.141 9.812   1.00 25.25 ?  108 LEU   B HG   1 
ATOM   5713 H  HD11 . LEU   B 1 108 ? 33.358 -22.229 11.488  1.00 25.71 ?  108 LEU   B HD11 1 
ATOM   5714 H  HD12 . LEU   B 1 108 ? 34.174 -23.392 10.775  1.00 25.71 ?  108 LEU   B HD12 1 
ATOM   5715 H  HD13 . LEU   B 1 108 ? 34.493 -21.873 10.435  1.00 25.71 ?  108 LEU   B HD13 1 
ATOM   5716 H  HD21 . LEU   B 1 108 ? 31.817 -20.837 10.185  1.00 26.36 ?  108 LEU   B HD21 1 
ATOM   5717 H  HD22 . LEU   B 1 108 ? 32.867 -20.559 9.025   1.00 26.36 ?  108 LEU   B HD22 1 
ATOM   5718 H  HD23 . LEU   B 1 108 ? 31.461 -21.216 8.684   1.00 26.36 ?  108 LEU   B HD23 1 
ATOM   5719 N  N    . LEU   B 1 109 ? 33.095 -24.730 5.201   1.00 15.30 ?  109 LEU   B N    1 
ATOM   5720 C  CA   . LEU   B 1 109 ? 33.725 -24.839 3.893   1.00 14.43 ?  109 LEU   B CA   1 
ATOM   5721 C  C    . LEU   B 1 109 ? 32.961 -24.054 2.833   1.00 13.77 ?  109 LEU   B C    1 
ATOM   5722 O  O    . LEU   B 1 109 ? 33.577 -23.464 1.938   1.00 13.39 ?  109 LEU   B O    1 
ATOM   5723 C  CB   . LEU   B 1 109 ? 33.833 -26.315 3.516   1.00 14.51 ?  109 LEU   B CB   1 
ATOM   5724 C  CG   . LEU   B 1 109 ? 34.613 -26.661 2.254   1.00 14.27 ?  109 LEU   B CG   1 
ATOM   5725 C  CD1  . LEU   B 1 109 ? 35.990 -25.999 2.261   1.00 14.08 ?  109 LEU   B CD1  1 
ATOM   5726 C  CD2  . LEU   B 1 109 ? 34.748 -28.169 2.128   1.00 15.05 ?  109 LEU   B CD2  1 
ATOM   5727 H  H    . LEU   B 1 109 ? 32.793 -25.472 5.506   1.00 18.37 ?  109 LEU   B H    1 
ATOM   5728 H  HA   . LEU   B 1 109 ? 34.623 -24.479 3.942   1.00 17.32 ?  109 LEU   B HA   1 
ATOM   5729 H  HB2  . LEU   B 1 109 ? 34.264 -26.785 4.247   1.00 17.42 ?  109 LEU   B HB2  1 
ATOM   5730 H  HB3  . LEU   B 1 109 ? 32.936 -26.667 3.398   1.00 17.42 ?  109 LEU   B HB3  1 
ATOM   5731 H  HG   . LEU   B 1 109 ? 34.125 -26.346 1.473   1.00 17.13 ?  109 LEU   B HG   1 
ATOM   5732 H  HD11 . LEU   B 1 109 ? 36.526 -26.372 1.542   1.00 16.90 ?  109 LEU   B HD11 1 
ATOM   5733 H  HD12 . LEU   B 1 109 ? 35.879 -25.046 2.130   1.00 16.90 ?  109 LEU   B HD12 1 
ATOM   5734 H  HD13 . LEU   B 1 109 ? 36.416 -26.174 3.114   1.00 16.90 ?  109 LEU   B HD13 1 
ATOM   5735 H  HD21 . LEU   B 1 109 ? 35.317 -28.378 1.368   1.00 18.07 ?  109 LEU   B HD21 1 
ATOM   5736 H  HD22 . LEU   B 1 109 ? 35.142 -28.522 2.940   1.00 18.07 ?  109 LEU   B HD22 1 
ATOM   5737 H  HD23 . LEU   B 1 109 ? 33.867 -28.560 1.992   1.00 18.07 ?  109 LEU   B HD23 1 
ATOM   5738 N  N    . LYS   B 1 110 ? 31.627 -24.022 2.912   1.00 13.61 ?  110 LYS   B N    1 
ATOM   5739 C  CA   . LYS   B 1 110 ? 30.871 -23.262 1.921   1.00 13.31 ?  110 LYS   B CA   1 
ATOM   5740 C  C    . LYS   B 1 110 ? 31.206 -21.773 2.009   1.00 13.21 ?  110 LYS   B C    1 
ATOM   5741 O  O    . LYS   B 1 110 ? 31.459 -21.123 0.991   1.00 12.76 ?  110 LYS   B O    1 
ATOM   5742 C  CB   . LYS   B 1 110 ? 29.368 -23.508 2.071   1.00 13.77 ?  110 LYS   B CB   1 
ATOM   5743 C  CG   . LYS   B 1 110 ? 28.560 -22.900 0.927   1.00 14.11 ?  110 LYS   B CG   1 
ATOM   5744 C  CD   . LYS   B 1 110 ? 27.090 -23.316 0.964   1.00 14.47 ?  110 LYS   B CD   1 
ATOM   5745 C  CE   . LYS   B 1 110 ? 26.324 -22.790 -0.252  1.00 15.37 ?  110 LYS   B CE   1 
ATOM   5746 N  NZ   . LYS   B 1 110 ? 26.665 -23.506 -1.513  1.00 15.59 ?  110 LYS   B NZ   1 
ATOM   5747 H  H    . LYS   B 1 110 ? 31.155 -24.425 3.502   1.00 16.34 ?  110 LYS   B H    1 
ATOM   5748 H  HA   . LYS   B 1 110 ? 31.129 -23.564 1.033   1.00 15.97 ?  110 LYS   B HA   1 
ATOM   5749 H  HB2  . LYS   B 1 110 ? 29.204 -24.467 2.078   1.00 16.52 ?  110 LYS   B HB2  1 
ATOM   5750 H  HB3  . LYS   B 1 110 ? 29.061 -23.113 2.899   1.00 16.52 ?  110 LYS   B HB3  1 
ATOM   5751 H  HG2  . LYS   B 1 110 ? 28.594 -21.935 0.986   1.00 16.93 ?  110 LYS   B HG2  1 
ATOM   5752 H  HG3  . LYS   B 1 110 ? 28.928 -23.197 0.079   1.00 16.93 ?  110 LYS   B HG3  1 
ATOM   5753 H  HD2  . LYS   B 1 110 ? 27.027 -24.289 0.965   1.00 17.37 ?  110 LYS   B HD2  1 
ATOM   5754 H  HD3  . LYS   B 1 110 ? 26.671 -22.959 1.765   1.00 17.37 ?  110 LYS   B HD3  1 
ATOM   5755 H  HE2  . LYS   B 1 110 ? 25.372 -22.897 -0.100  1.00 18.45 ?  110 LYS   B HE2  1 
ATOM   5756 H  HE3  . LYS   B 1 110 ? 26.538 -21.854 -0.375  1.00 18.45 ?  110 LYS   B HE3  1 
ATOM   5757 H  HZ1  . LYS   B 1 110 ? 26.203 -23.168 -2.192  1.00 18.71 ?  110 LYS   B HZ1  1 
ATOM   5758 H  HZ2  . LYS   B 1 110 ? 27.536 -23.421 -1.685  1.00 18.71 ?  110 LYS   B HZ2  1 
ATOM   5759 H  HZ3  . LYS   B 1 110 ? 26.472 -24.373 -1.434  1.00 18.71 ?  110 LYS   B HZ3  1 
ATOM   5760 N  N    . SER   B 1 111 ? 31.226 -21.222 3.228   1.00 13.59 ?  111 SER   B N    1 
ATOM   5761 C  CA   . SER   B 1 111 ? 31.618 -19.826 3.407   1.00 13.49 ?  111 SER   B CA   1 
ATOM   5762 C  C    . SER   B 1 111 ? 32.998 -19.568 2.817   1.00 12.73 ?  111 SER   B C    1 
ATOM   5763 O  O    . SER   B 1 111 ? 33.224 -18.537 2.167   1.00 12.96 ?  111 SER   B O    1 
ATOM   5764 C  CB   . SER   B 1 111 ? 31.615 -19.469 4.891   1.00 14.36 ?  111 SER   B CB   1 
ATOM   5765 O  OG   . SER   B 1 111 ? 30.309 -19.464 5.416   1.00 15.92 ?  111 SER   B OG   1 
ATOM   5766 H  H    . SER   B 1 111 ? 31.028 -21.639 3.954   1.00 16.31 ?  111 SER   B H    1 
ATOM   5767 H  HA   . SER   B 1 111 ? 30.985 -19.257 2.952   1.00 16.19 ?  111 SER   B HA   1 
ATOM   5768 H  HB2  . SER   B 1 111 ? 32.134 -20.130 5.377   1.00 17.24 ?  111 SER   B HB2  1 
ATOM   5769 H  HB3  . SER   B 1 111 ? 32.000 -18.592 5.006   1.00 17.24 ?  111 SER   B HB3  1 
ATOM   5770 H  HG   . SER   B 1 111 ? 30.320 -19.261 6.237   1.00 19.11 ?  111 SER   B HG   1 
ATOM   5771 N  N    . ALA   B 1 112 ? 33.938 -20.486 3.043   1.00 12.89 ?  112 ALA   B N    1 
ATOM   5772 C  CA   . ALA   B 1 112 ? 35.282 -20.314 2.503   1.00 12.55 ?  112 ALA   B CA   1 
ATOM   5773 C  C    . ALA   B 1 112 ? 35.251 -20.219 0.979   1.00 11.75 ?  112 ALA   B C    1 
ATOM   5774 O  O    . ALA   B 1 112 ? 35.877 -19.331 0.386   1.00 12.28 ?  112 ALA   B O    1 
ATOM   5775 C  CB   . ALA   B 1 112 ? 36.184 -21.455 2.980   1.00 12.98 ?  112 ALA   B CB   1 
ATOM   5776 H  H    . ALA   B 1 112 ? 33.822 -21.211 3.504   1.00 15.47 ?  112 ALA   B H    1 
ATOM   5777 H  HA   . ALA   B 1 112 ? 35.646 -19.485 2.848   1.00 15.07 ?  112 ALA   B HA   1 
ATOM   5778 H  HB1  . ALA   B 1 112 ? 37.075 -21.318 2.618   1.00 15.59 ?  112 ALA   B HB1  1 
ATOM   5779 H  HB2  . ALA   B 1 112 ? 36.220 -21.444 3.951   1.00 15.59 ?  112 ALA   B HB2  1 
ATOM   5780 H  HB3  . ALA   B 1 112 ? 35.823 -22.296 2.670   1.00 15.59 ?  112 ALA   B HB3  1 
ATOM   5781 N  N    . TYR   B 1 113 ? 34.518 -21.123 0.322   1.00 11.83 ?  113 TYR   B N    1 
ATOM   5782 C  CA   . TYR   B 1 113 ? 34.445 -21.076 -1.132  1.00 11.52 ?  113 TYR   B CA   1 
ATOM   5783 C  C    . TYR   B 1 113 ? 33.733 -19.830 -1.648  1.00 11.37 ?  113 TYR   B C    1 
ATOM   5784 O  O    . TYR   B 1 113 ? 34.000 -19.402 -2.775  1.00 11.38 ?  113 TYR   B O    1 
ATOM   5785 C  CB   . TYR   B 1 113 ? 33.770 -22.335 -1.677  1.00 11.78 ?  113 TYR   B CB   1 
ATOM   5786 C  CG   . TYR   B 1 113 ? 34.729 -23.482 -1.934  1.00 12.31 ?  113 TYR   B CG   1 
ATOM   5787 C  CD1  . TYR   B 1 113 ? 35.722 -23.382 -2.901  1.00 12.77 ?  113 TYR   B CD1  1 
ATOM   5788 C  CD2  . TYR   B 1 113 ? 34.628 -24.673 -1.230  1.00 12.33 ?  113 TYR   B CD2  1 
ATOM   5789 C  CE1  . TYR   B 1 113 ? 36.600 -24.412 -3.143  1.00 12.65 ?  113 TYR   B CE1  1 
ATOM   5790 C  CE2  . TYR   B 1 113 ? 35.497 -25.724 -1.473  1.00 12.75 ?  113 TYR   B CE2  1 
ATOM   5791 C  CZ   . TYR   B 1 113 ? 36.477 -25.592 -2.434  1.00 12.54 ?  113 TYR   B CZ   1 
ATOM   5792 O  OH   . TYR   B 1 113 ? 37.359 -26.607 -2.708  1.00 13.60 ?  113 TYR   B OH   1 
ATOM   5793 H  H    . TYR   B 1 113 ? 34.055 -21.753 0.693   1.00 14.20 ?  113 TYR   B H    1 
ATOM   5794 H  HA   . TYR   B 1 113 ? 35.348 -21.060 -1.472  1.00 13.82 ?  113 TYR   B HA   1 
ATOM   5795 H  HB2  . TYR   B 1 113 ? 33.109 -22.647 -1.032  1.00 14.15 ?  113 TYR   B HB2  1 
ATOM   5796 H  HB3  . TYR   B 1 113 ? 33.331 -22.120 -2.513  1.00 14.15 ?  113 TYR   B HB3  1 
ATOM   5797 H  HD1  . TYR   B 1 113 ? 35.807 -22.590 -3.384  1.00 15.32 ?  113 TYR   B HD1  1 
ATOM   5798 H  HD2  . TYR   B 1 113 ? 33.960 -24.770 -0.592  1.00 14.80 ?  113 TYR   B HD2  1 
ATOM   5799 H  HE1  . TYR   B 1 113 ? 37.257 -24.325 -3.800  1.00 15.18 ?  113 TYR   B HE1  1 
ATOM   5800 H  HE2  . TYR   B 1 113 ? 35.410 -26.522 -1.002  1.00 15.31 ?  113 TYR   B HE2  1 
ATOM   5801 H  HH   . TYR   B 1 113 ? 37.182 -27.277 -2.232  1.00 16.33 ?  113 TYR   B HH   1 
ATOM   5802 N  N    . GLU   B 1 114 ? 32.811 -19.253 -0.870  1.00 11.62 ?  114 GLU   B N    1 
ATOM   5803 C  CA   . GLU   B 1 114 ? 32.129 -18.043 -1.324  1.00 11.39 ?  114 GLU   B CA   1 
ATOM   5804 C  C    . GLU   B 1 114 ? 33.114 -16.924 -1.625  1.00 11.30 ?  114 GLU   B C    1 
ATOM   5805 O  O    . GLU   B 1 114 ? 32.835 -16.068 -2.467  1.00 11.77 ?  114 GLU   B O    1 
ATOM   5806 C  CB   . GLU   B 1 114 ? 31.072 -17.615 -0.301  1.00 12.03 ?  114 GLU   B CB   1 
ATOM   5807 C  CG   . GLU   B 1 114 ? 29.853 -18.531 -0.371  1.00 12.37 ?  114 GLU   B CG   1 
ATOM   5808 C  CD   . GLU   B 1 114 ? 28.828 -18.345 0.736   1.00 12.38 ?  114 GLU   B CD   1 
ATOM   5809 O  OE1  . GLU   B 1 114 ? 29.119 -17.728 1.777   1.00 12.55 ?  114 GLU   B OE1  1 
ATOM   5810 O  OE2  . GLU   B 1 114 ? 27.708 -18.886 0.573   1.00 13.32 -1 114 GLU   B OE2  1 
ATOM   5811 H  H    . GLU   B 1 114 ? 32.562 -19.542 -0.095  1.00 13.95 ?  114 GLU   B H    1 
ATOM   5812 H  HA   . GLU   B 1 114 ? 31.670 -18.245 -2.149  1.00 13.67 ?  114 GLU   B HA   1 
ATOM   5813 H  HB2  . GLU   B 1 114 ? 31.446 -17.670 0.594   1.00 14.44 ?  114 GLU   B HB2  1 
ATOM   5814 H  HB3  . GLU   B 1 114 ? 30.786 -16.711 -0.494  1.00 14.44 ?  114 GLU   B HB3  1 
ATOM   5815 H  HG2  . GLU   B 1 114 ? 29.405 -18.377 -1.213  1.00 14.85 ?  114 GLU   B HG2  1 
ATOM   5816 H  HG3  . GLU   B 1 114 ? 30.164 -19.452 -0.330  1.00 14.85 ?  114 GLU   B HG3  1 
ATOM   5817 N  N    . ASN   B 1 115 ? 34.278 -16.917 -0.973  1.00 11.21 ?  115 ASN   B N    1 
ATOM   5818 C  CA   . ASN   B 1 115 ? 35.270 -15.887 -1.271  1.00 11.03 ?  115 ASN   B CA   1 
ATOM   5819 C  C    . ASN   B 1 115 ? 35.678 -15.909 -2.734  1.00 10.93 ?  115 ASN   B C    1 
ATOM   5820 O  O    . ASN   B 1 115 ? 36.068 -14.869 -3.289  1.00 11.58 ?  115 ASN   B O    1 
ATOM   5821 C  CB   . ASN   B 1 115 ? 36.508 -16.062 -0.388  1.00 11.70 ?  115 ASN   B CB   1 
ATOM   5822 C  CG   . ASN   B 1 115 ? 36.236 -15.793 1.070   1.00 12.06 ?  115 ASN   B CG   1 
ATOM   5823 O  OD1  . ASN   B 1 115 ? 36.237 -14.648 1.515   1.00 13.91 ?  115 ASN   B OD1  1 
ATOM   5824 N  ND2  . ASN   B 1 115 ? 36.066 -16.859 1.843   1.00 12.28 ?  115 ASN   B ND2  1 
ATOM   5825 H  H    . ASN   B 1 115 ? 34.515 -17.476 -0.355  1.00 13.45 ?  115 ASN   B H    1 
ATOM   5826 H  HA   . ASN   B 1 115 ? 34.895 -15.016 -1.080  1.00 13.24 ?  115 ASN   B HA   1 
ATOM   5827 H  HB2  . ASN   B 1 115 ? 36.837 -16.970 -0.471  1.00 14.05 ?  115 ASN   B HB2  1 
ATOM   5828 H  HB3  . ASN   B 1 115 ? 37.197 -15.437 -0.677  1.00 14.05 ?  115 ASN   B HB3  1 
ATOM   5829 H  HD21 . ASN   B 1 115 ? 35.916 -16.761 2.686   1.00 14.74 ?  115 ASN   B HD21 1 
ATOM   5830 H  HD22 . ASN   B 1 115 ? 36.088 -17.649 1.503   1.00 14.74 ?  115 ASN   B HD22 1 
ATOM   5831 N  N    . PHE   B 1 116 ? 35.652 -17.088 -3.367  1.00 10.71 ?  116 PHE   B N    1 
ATOM   5832 C  CA   . PHE   B 1 116 ? 36.083 -17.181 -4.756  1.00 11.03 ?  116 PHE   B CA   1 
ATOM   5833 C  C    . PHE   B 1 116 ? 35.184 -16.355 -5.669  1.00 10.91 ?  116 PHE   B C    1 
ATOM   5834 O  O    . PHE   B 1 116 ? 35.622 -15.927 -6.744  1.00 11.49 ?  116 PHE   B O    1 
ATOM   5835 C  CB   . PHE   B 1 116 ? 36.049 -18.627 -5.274  1.00 10.75 ?  116 PHE   B CB   1 
ATOM   5836 C  CG   . PHE   B 1 116 ? 37.117 -19.577 -4.724  1.00 10.75 ?  116 PHE   B CG   1 
ATOM   5837 C  CD1  . PHE   B 1 116 ? 37.770 -19.391 -3.516  1.00 11.56 ?  116 PHE   B CD1  1 
ATOM   5838 C  CD2  . PHE   B 1 116 ? 37.417 -20.714 -5.454  1.00 11.16 ?  116 PHE   B CD2  1 
ATOM   5839 C  CE1  . PHE   B 1 116 ? 38.701 -20.326 -3.059  1.00 11.62 ?  116 PHE   B CE1  1 
ATOM   5840 C  CE2  . PHE   B 1 116 ? 38.343 -21.649 -5.007  1.00 11.20 ?  116 PHE   B CE2  1 
ATOM   5841 C  CZ   . PHE   B 1 116 ? 38.981 -21.461 -3.811  1.00 11.17 ?  116 PHE   B CZ   1 
ATOM   5842 H  H    . PHE   B 1 116 ? 35.392 -17.836 -3.019  1.00 12.86 ?  116 PHE   B H    1 
ATOM   5843 H  HA   . PHE   B 1 116 ? 36.993 -16.854 -4.834  1.00 13.24 ?  116 PHE   B HA   1 
ATOM   5844 H  HB2  . PHE   B 1 116 ? 35.179 -19.006 -5.054  1.00 12.91 ?  116 PHE   B HB2  1 
ATOM   5845 H  HB3  . PHE   B 1 116 ? 36.148 -18.605 -6.239  1.00 12.91 ?  116 PHE   B HB3  1 
ATOM   5846 H  HD1  . PHE   B 1 116 ? 37.572 -18.642 -2.999  1.00 13.88 ?  116 PHE   B HD1  1 
ATOM   5847 H  HD2  . PHE   B 1 116 ? 36.979 -20.865 -6.262  1.00 13.39 ?  116 PHE   B HD2  1 
ATOM   5848 H  HE1  . PHE   B 1 116 ? 39.135 -20.185 -2.249  1.00 13.94 ?  116 PHE   B HE1  1 
ATOM   5849 H  HE2  . PHE   B 1 116 ? 38.529 -22.398 -5.522  1.00 13.45 ?  116 PHE   B HE2  1 
ATOM   5850 H  HZ   . PHE   B 1 116 ? 39.615 -22.069 -3.514  1.00 13.41 ?  116 PHE   B HZ   1 
ATOM   5851 N  N    . ASN   B 1 117 ? 33.916 -16.153 -5.283  1.00 11.33 ?  117 ASN   B N    1 
ATOM   5852 C  CA   . ASN   B 1 117 ? 32.970 -15.455 -6.149  1.00 11.52 ?  117 ASN   B CA   1 
ATOM   5853 C  C    . ASN   B 1 117 ? 33.281 -13.976 -6.300  1.00 11.89 ?  117 ASN   B C    1 
ATOM   5854 O  O    . ASN   B 1 117 ? 32.682 -13.324 -7.158  1.00 13.03 ?  117 ASN   B O    1 
ATOM   5855 C  CB   . ASN   B 1 117 ? 31.549 -15.672 -5.653  1.00 11.85 ?  117 ASN   B CB   1 
ATOM   5856 C  CG   . ASN   B 1 117 ? 31.097 -17.079 -5.901  1.00 12.09 ?  117 ASN   B CG   1 
ATOM   5857 O  OD1  . ASN   B 1 117 ? 31.450 -17.677 -6.918  1.00 12.93 ?  117 ASN   B OD1  1 
ATOM   5858 N  ND2  . ASN   B 1 117 ? 30.360 -17.646 -4.961  1.00 12.22 ?  117 ASN   B ND2  1 
ATOM   5859 H  H    . ASN   B 1 117 ? 33.589 -16.409 -4.524  1.00 13.60 ?  117 ASN   B H    1 
ATOM   5860 H  HA   . ASN   B 1 117 ? 33.028 -15.852 -7.026  1.00 13.82 ?  117 ASN   B HA   1 
ATOM   5861 H  HB2  . ASN   B 1 117 ? 31.512 -15.506 -4.694  1.00 14.23 ?  117 ASN   B HB2  1 
ATOM   5862 H  HB3  . ASN   B 1 117 ? 30.951 -15.065 -6.117  1.00 14.23 ?  117 ASN   B HB3  1 
ATOM   5863 H  HD21 . ASN   B 1 117 ? 30.076 -18.450 -5.064  1.00 14.67 ?  117 ASN   B HD21 1 
ATOM   5864 H  HD22 . ASN   B 1 117 ? 30.140 -17.198 -4.258  1.00 14.67 ?  117 ASN   B HD22 1 
ATOM   5865 N  N    . GLN   B 1 118 ? 34.215 -13.447 -5.518  1.00 11.44 ?  118 GLN   B N    1 
ATOM   5866 C  CA   . GLN   B 1 118 ? 34.643 -12.062 -5.659  1.00 12.31 ?  118 GLN   B CA   1 
ATOM   5867 C  C    . GLN   B 1 118 ? 35.711 -11.873 -6.729  1.00 12.27 ?  118 GLN   B C    1 
ATOM   5868 O  O    . GLN   B 1 118 ? 36.184 -10.748 -6.913  1.00 13.77 ?  118 GLN   B O    1 
ATOM   5869 C  CB   . GLN   B 1 118 ? 35.123 -11.529 -4.307  1.00 12.65 ?  118 GLN   B CB   1 
ATOM   5870 C  CG   . GLN   B 1 118 ? 34.044 -11.569 -3.238  1.00 12.71 ?  118 GLN   B CG   1 
ATOM   5871 C  CD   . GLN   B 1 118 ? 32.873 -10.666 -3.567  1.00 12.72 ?  118 GLN   B CD   1 
ATOM   5872 O  OE1  . GLN   B 1 118 ? 33.062 -9.526  -4.007  1.00 13.49 ?  118 GLN   B OE1  1 
ATOM   5873 N  NE2  . GLN   B 1 118 ? 31.657 -11.164 -3.369  1.00 13.11 ?  118 GLN   B NE2  1 
ATOM   5874 H  H    . GLN   B 1 118 ? 34.630 -13.868 -4.890  1.00 13.73 ?  118 GLN   B H    1 
ATOM   5875 H  HA   . GLN   B 1 118 ? 33.879 -11.531 -5.933  1.00 14.78 ?  118 GLN   B HA   1 
ATOM   5876 H  HB2  . GLN   B 1 118 ? 35.869 -12.060 -4.002  1.00 15.18 ?  118 GLN   B HB2  1 
ATOM   5877 H  HB3  . GLN   B 1 118 ? 35.398 -10.600 -4.414  1.00 15.18 ?  118 GLN   B HB3  1 
ATOM   5878 H  HG2  . GLN   B 1 118 ? 33.713 -12.476 -3.158  1.00 15.26 ?  118 GLN   B HG2  1 
ATOM   5879 H  HG3  . GLN   B 1 118 ? 34.424 -11.276 -2.395  1.00 15.26 ?  118 GLN   B HG3  1 
ATOM   5880 H  HE21 . GLN   B 1 118 ? 31.568 -11.963 -3.061  1.00 15.73 ?  118 GLN   B HE21 1 
ATOM   5881 H  HE22 . GLN   B 1 118 ? 30.968 -10.687 -3.541  1.00 15.73 ?  118 GLN   B HE22 1 
ATOM   5882 N  N    . HIS   B 1 119 ? 36.067 -12.929 -7.460  1.00 11.57 ?  119 HIS   B N    1 
ATOM   5883 C  CA   . HIS   B 1 119 ? 37.109 -12.883 -8.478  1.00 11.92 ?  119 HIS   B CA   1 
ATOM   5884 C  C    . HIS   B 1 119 ? 36.627 -13.611 -9.717  1.00 11.95 ?  119 HIS   B C    1 
ATOM   5885 O  O    . HIS   B 1 119 ? 36.122 -14.729 -9.615  1.00 12.72 ?  119 HIS   B O    1 
ATOM   5886 C  CB   . HIS   B 1 119 ? 38.388 -13.519 -7.931  1.00 12.32 ?  119 HIS   B CB   1 
ATOM   5887 C  CG   . HIS   B 1 119 ? 38.869 -12.823 -6.707  1.00 13.55 ?  119 HIS   B CG   1 
ATOM   5888 N  ND1  . HIS   B 1 119 ? 39.674 -11.705 -6.761  1.00 15.09 ?  119 HIS   B ND1  1 
ATOM   5889 C  CD2  . HIS   B 1 119 ? 38.564 -13.010 -5.403  1.00 14.73 ?  119 HIS   B CD2  1 
ATOM   5890 C  CE1  . HIS   B 1 119 ? 39.880 -11.263 -5.534  1.00 16.12 ?  119 HIS   B CE1  1 
ATOM   5891 N  NE2  . HIS   B 1 119 ? 39.210 -12.029 -4.693  1.00 16.17 ?  119 HIS   B NE2  1 
ATOM   5892 H  H    . HIS   B 1 119 ? 35.698 -13.710 -7.390  1.00 13.89 ?  119 HIS   B H    1 
ATOM   5893 H  HA   . HIS   B 1 119 ? 37.293 -11.960 -8.715  1.00 14.31 ?  119 HIS   B HA   1 
ATOM   5894 H  HB2  . HIS   B 1 119 ? 38.215 -14.446 -7.709  1.00 14.80 ?  119 HIS   B HB2  1 
ATOM   5895 H  HB3  . HIS   B 1 119 ? 39.085 -13.462 -8.606  1.00 14.80 ?  119 HIS   B HB3  1 
ATOM   5896 H  HD2  . HIS   B 1 119 ? 38.020 -13.681 -5.053  1.00 17.68 ?  119 HIS   B HD2  1 
ATOM   5897 H  HE1  . HIS   B 1 119 ? 40.413 -10.541 -5.300  1.00 19.34 ?  119 HIS   B HE1  1 
ATOM   5898 H  HE2  . HIS   B 1 119 ? 39.207 -11.950 -3.836  1.00 19.40 ?  119 HIS   B HE2  1 
ATOM   5899 N  N    . GLU   B 1 120 ? 36.779 -12.992 -10.888 1.00 12.75 ?  120 GLU   B N    1 
ATOM   5900 C  CA   . GLU   B 1 120 ? 36.192 -13.578 -12.089 1.00 14.10 ?  120 GLU   B CA   1 
ATOM   5901 C  C    . GLU   B 1 120 ? 36.870 -14.880 -12.497 1.00 12.90 ?  120 GLU   B C    1 
ATOM   5902 O  O    . GLU   B 1 120 ? 36.209 -15.758 -13.064 1.00 13.03 ?  120 GLU   B O    1 
ATOM   5903 C  CB   . GLU   B 1 120 ? 36.199 -12.573 -13.237 1.00 19.06 ?  120 GLU   B CB   1 
ATOM   5904 C  CG   . GLU   B 1 120 ? 35.234 -11.420 -13.017 1.00 25.41 ?  120 GLU   B CG   1 
ATOM   5905 C  CD   . GLU   B 1 120 ? 35.073 -10.534 -14.235 1.00 31.38 ?  120 GLU   B CD   1 
ATOM   5906 O  OE1  . GLU   B 1 120 ? 36.058 -10.358 -14.982 1.00 33.45 ?  120 GLU   B OE1  1 
ATOM   5907 O  OE2  . GLU   B 1 120 ? 33.955 -10.017 -14.443 1.00 34.14 -1 120 GLU   B OE2  1 
ATOM   5908 H  H    . GLU   B 1 120 ? 37.203 -12.249 -11.012 1.00 15.30 ?  120 GLU   B H    1 
ATOM   5909 H  HA   . GLU   B 1 120 ? 35.268 -13.786 -11.897 1.00 16.93 ?  120 GLU   B HA   1 
ATOM   5910 H  HB2  . GLU   B 1 120 ? 37.087 -12.200 -13.333 1.00 22.88 ?  120 GLU   B HB2  1 
ATOM   5911 H  HB3  . GLU   B 1 120 ? 35.937 -13.025 -14.055 1.00 22.88 ?  120 GLU   B HB3  1 
ATOM   5912 H  HG2  . GLU   B 1 120 ? 34.355 -11.774 -12.805 1.00 30.49 ?  120 GLU   B HG2  1 
ATOM   5913 H  HG3  . GLU   B 1 120 ? 35.554 -10.870 -12.287 1.00 30.49 ?  120 GLU   B HG3  1 
ATOM   5914 N  N    . VAL   B 1 121 ? 38.169 -15.023 -12.234 1.00 12.65 ?  121 VAL   B N    1 
ATOM   5915 C  CA   . VAL   B 1 121 ? 38.917 -16.229 -12.584 1.00 12.30 ?  121 VAL   B CA   1 
ATOM   5916 C  C    . VAL   B 1 121 ? 40.030 -16.432 -11.565 1.00 11.79 ?  121 VAL   B C    1 
ATOM   5917 O  O    . VAL   B 1 121 ? 40.711 -15.478 -11.174 1.00 12.57 ?  121 VAL   B O    1 
ATOM   5918 C  CB   . VAL   B 1 121 ? 39.435 -16.181 -14.041 1.00 14.18 ?  121 VAL   B CB   1 
ATOM   5919 C  CG1  . VAL   B 1 121 ? 40.299 -14.946 -14.293 1.00 15.04 ?  121 VAL   B CG1  1 
ATOM   5920 C  CG2  . VAL   B 1 121 ? 40.181 -17.463 -14.397 1.00 15.62 ?  121 VAL   B CG2  1 
ATOM   5921 H  H    . VAL   B 1 121 ? 38.650 -14.420 -11.851 1.00 15.19 ?  121 VAL   B H    1 
ATOM   5922 H  HA   . VAL   B 1 121 ? 38.313 -16.983 -12.521 1.00 14.77 ?  121 VAL   B HA   1 
ATOM   5923 H  HB   . VAL   B 1 121 ? 38.667 -16.122 -14.637 1.00 17.02 ?  121 VAL   B HB   1 
ATOM   5924 H  HG11 . VAL   B 1 121 ? 40.608 -14.958 -15.213 1.00 18.05 ?  121 VAL   B HG11 1 
ATOM   5925 H  HG12 . VAL   B 1 121 ? 39.767 -14.149 -14.135 1.00 18.05 ?  121 VAL   B HG12 1 
ATOM   5926 H  HG13 . VAL   B 1 121 ? 41.058 -14.963 -13.690 1.00 18.05 ?  121 VAL   B HG13 1 
ATOM   5927 H  HG21 . VAL   B 1 121 ? 40.384 -17.456 -15.348 1.00 18.75 ?  121 VAL   B HG21 1 
ATOM   5928 H  HG22 . VAL   B 1 121 ? 41.005 -17.502 -13.887 1.00 18.75 ?  121 VAL   B HG22 1 
ATOM   5929 H  HG23 . VAL   B 1 121 ? 39.621 -18.225 -14.186 1.00 18.75 ?  121 VAL   B HG23 1 
ATOM   5930 N  N    . LEU   B 1 122 ? 40.211 -17.684 -11.132 1.00 11.23 ?  122 LEU   B N    1 
ATOM   5931 C  CA   . LEU   B 1 122 ? 41.191 -18.035 -10.109 1.00 11.01 ?  122 LEU   B CA   1 
ATOM   5932 C  C    . LEU   B 1 122 ? 41.844 -19.366 -10.438 1.00 10.91 ?  122 LEU   B C    1 
ATOM   5933 O  O    . LEU   B 1 122 ? 41.183 -20.288 -10.936 1.00 12.08 ?  122 LEU   B O    1 
ATOM   5934 C  CB   . LEU   B 1 122 ? 40.538 -18.271 -8.735  1.00 12.67 ?  122 LEU   B CB   1 
ATOM   5935 C  CG   . LEU   B 1 122 ? 39.507 -17.245 -8.250  1.00 12.64 ?  122 LEU   B CG   1 
ATOM   5936 C  CD1  . LEU   B 1 122 ? 38.112 -17.596 -8.733  1.00 13.53 ?  122 LEU   B CD1  1 
ATOM   5937 C  CD2  . LEU   B 1 122 ? 39.540 -17.131 -6.737  1.00 12.33 ?  122 LEU   B CD2  1 
ATOM   5938 H  H    . LEU   B 1 122 ? 39.768 -18.364 -11.424 1.00 13.48 ?  122 LEU   B H    1 
ATOM   5939 H  HA   . LEU   B 1 122 ? 41.867 -17.344 -10.031 1.00 13.22 ?  122 LEU   B HA   1 
ATOM   5940 H  HB2  . LEU   B 1 122 ? 40.088 -19.127 -8.758  1.00 15.21 ?  122 LEU   B HB2  1 
ATOM   5941 H  HB3  . LEU   B 1 122 ? 41.239 -18.294 -8.068  1.00 15.21 ?  122 LEU   B HB3  1 
ATOM   5942 H  HG   . LEU   B 1 122 ? 39.734 -16.374 -8.613  1.00 15.17 ?  122 LEU   B HG   1 
ATOM   5943 H  HD11 . LEU   B 1 122 ? 37.481 -16.954 -8.366  1.00 16.24 ?  122 LEU   B HD11 1 
ATOM   5944 H  HD12 . LEU   B 1 122 ? 38.094 -17.551 -9.704  1.00 16.24 ?  122 LEU   B HD12 1 
ATOM   5945 H  HD13 . LEU   B 1 122 ? 37.888 -18.487 -8.437  1.00 16.24 ?  122 LEU   B HD13 1 
ATOM   5946 H  HD21 . LEU   B 1 122 ? 38.863 -16.498 -6.447  1.00 14.80 ?  122 LEU   B HD21 1 
ATOM   5947 H  HD22 . LEU   B 1 122 ? 39.364 -18.002 -6.347  1.00 14.80 ?  122 LEU   B HD22 1 
ATOM   5948 H  HD23 . LEU   B 1 122 ? 40.419 -16.820 -6.461  1.00 14.80 ?  122 LEU   B HD23 1 
ATOM   5949 N  N    . LEU   B 1 123 ? 43.129 -19.479 -10.079 1.00 10.69 ?  123 LEU   B N    1 
ATOM   5950 C  CA   . LEU   B 1 123 ? 43.843 -20.746 -9.956  1.00 10.74 ?  123 LEU   B CA   1 
ATOM   5951 C  C    . LEU   B 1 123 ? 43.815 -21.140 -8.484  1.00 10.51 ?  123 LEU   B C    1 
ATOM   5952 O  O    . LEU   B 1 123 ? 44.162 -20.315 -7.631  1.00 10.94 ?  123 LEU   B O    1 
ATOM   5953 C  CB   . LEU   B 1 123 ? 45.293 -20.562 -10.411 1.00 11.43 ?  123 LEU   B CB   1 
ATOM   5954 C  CG   . LEU   B 1 123 ? 46.235 -21.750 -10.168 1.00 11.78 ?  123 LEU   B CG   1 
ATOM   5955 C  CD1  . LEU   B 1 123 ? 45.811 -22.990 -10.949 1.00 12.45 ?  123 LEU   B CD1  1 
ATOM   5956 C  CD2  . LEU   B 1 123 ? 47.652 -21.358 -10.535 1.00 12.59 ?  123 LEU   B CD2  1 
ATOM   5957 H  H    . LEU   B 1 123 ? 43.626 -18.798 -9.892  1.00 12.84 ?  123 LEU   B H    1 
ATOM   5958 H  HA   . LEU   B 1 123 ? 43.410 -21.435 -10.487 1.00 12.89 ?  123 LEU   B HA   1 
ATOM   5959 H  HB2  . LEU   B 1 123 ? 45.288 -20.387 -11.367 1.00 13.72 ?  123 LEU   B HB2  1 
ATOM   5960 H  HB3  . LEU   B 1 123 ? 45.662 -19.798 -9.946  1.00 13.72 ?  123 LEU   B HB3  1 
ATOM   5961 H  HG   . LEU   B 1 123 ? 46.225 -21.976 -9.226  1.00 14.14 ?  123 LEU   B HG   1 
ATOM   5962 H  HD11 . LEU   B 1 123 ? 46.444 -23.702 -10.777 1.00 14.94 ?  123 LEU   B HD11 1 
ATOM   5963 H  HD12 . LEU   B 1 123 ? 44.924 -23.258 -10.656 1.00 14.94 ?  123 LEU   B HD12 1 
ATOM   5964 H  HD13 . LEU   B 1 123 ? 45.796 -22.777 -11.894 1.00 14.94 ?  123 LEU   B HD13 1 
ATOM   5965 H  HD21 . LEU   B 1 123 ? 48.238 -22.115 -10.378 1.00 15.11 ?  123 LEU   B HD21 1 
ATOM   5966 H  HD22 . LEU   B 1 123 ? 47.677 -21.108 -11.472 1.00 15.11 ?  123 LEU   B HD22 1 
ATOM   5967 H  HD23 . LEU   B 1 123 ? 47.923 -20.609 -9.983  1.00 15.11 ?  123 LEU   B HD23 1 
ATOM   5968 N  N    . ALA   B 1 124 ? 43.383 -22.368 -8.173  1.00 10.44 ?  124 ALA   B N    1 
ATOM   5969 C  CA   . ALA   B 1 124 ? 43.124 -22.677 -6.774  1.00 10.43 ?  124 ALA   B CA   1 
ATOM   5970 C  C    . ALA   B 1 124 ? 43.400 -24.136 -6.449  1.00 10.29 ?  124 ALA   B C    1 
ATOM   5971 O  O    . ALA   B 1 124 ? 43.263 -25.012 -7.313  1.00 11.19 ?  124 ALA   B O    1 
ATOM   5972 C  CB   . ALA   B 1 124 ? 41.669 -22.368 -6.414  1.00 11.06 ?  124 ALA   B CB   1 
ATOM   5973 H  H    . ALA   B 1 124 ? 43.208 -23.004 -8.736  1.00 12.53 ?  124 ALA   B H    1 
ATOM   5974 H  HA   . ALA   B 1 124 ? 43.699 -22.126 -6.231  1.00 12.52 ?  124 ALA   B HA   1 
ATOM   5975 H  HB1  . ALA   B 1 124 ? 41.516 -22.580 -5.482  1.00 13.28 ?  124 ALA   B HB1  1 
ATOM   5976 H  HB2  . ALA   B 1 124 ? 41.500 -21.423 -6.570  1.00 13.28 ?  124 ALA   B HB2  1 
ATOM   5977 H  HB3  . ALA   B 1 124 ? 41.080 -22.900 -6.975  1.00 13.28 ?  124 ALA   B HB3  1 
ATOM   5978 N  N    . PRO   B 1 125 ? 43.693 -24.432 -5.184  1.00 10.58 ?  125 PRO   B N    1 
ATOM   5979 C  CA   . PRO   B 1 125 ? 43.630 -25.795 -4.659  1.00 11.34 ?  125 PRO   B CA   1 
ATOM   5980 C  C    . PRO   B 1 125 ? 42.229 -26.070 -4.116  1.00 11.40 ?  125 PRO   B C    1 
ATOM   5981 O  O    . PRO   B 1 125 ? 41.432 -25.153 -3.904  1.00 12.09 ?  125 PRO   B O    1 
ATOM   5982 C  CB   . PRO   B 1 125 ? 44.610 -25.716 -3.482  1.00 12.68 ?  125 PRO   B CB   1 
ATOM   5983 C  CG   . PRO   B 1 125 ? 44.361 -24.333 -2.918  1.00 12.54 ?  125 PRO   B CG   1 
ATOM   5984 C  CD   . PRO   B 1 125 ? 44.022 -23.461 -4.122  1.00 11.34 ?  125 PRO   B CD   1 
ATOM   5985 H  HA   . PRO   B 1 125 ? 43.909 -26.463 -5.304  1.00 13.61 ?  125 PRO   B HA   1 
ATOM   5986 H  HB2  . PRO   B 1 125 ? 44.400 -26.399 -2.820  1.00 15.23 ?  125 PRO   B HB2  1 
ATOM   5987 H  HB3  . PRO   B 1 125 ? 45.523 -25.803 -3.791  1.00 15.23 ?  125 PRO   B HB3  1 
ATOM   5988 H  HG2  . PRO   B 1 125 ? 43.615 -24.356 -2.293  1.00 15.05 ?  125 PRO   B HG2  1 
ATOM   5989 H  HG3  . PRO   B 1 125 ? 45.162 -24.006 -2.469  1.00 15.05 ?  125 PRO   B HG3  1 
ATOM   5990 H  HD2  . PRO   B 1 125 ? 43.259 -22.894 -3.932  1.00 13.61 ?  125 PRO   B HD2  1 
ATOM   5991 H  HD3  . PRO   B 1 125 ? 44.798 -22.928 -4.381  1.00 13.61 ?  125 PRO   B HD3  1 
ATOM   5992 N  N    . LEU   B 1 126 ? 41.961 -27.347 -3.837  1.00 11.97 ?  126 LEU   B N    1 
ATOM   5993 C  CA   . LEU   B 1 126 ? 40.739 -27.710 -3.126  1.00 12.47 ?  126 LEU   B CA   1 
ATOM   5994 C  C    . LEU   B 1 126 ? 40.855 -27.311 -1.663  1.00 12.79 ?  126 LEU   B C    1 
ATOM   5995 O  O    . LEU   B 1 126 ? 41.744 -27.779 -0.944  1.00 14.51 ?  126 LEU   B O    1 
ATOM   5996 C  CB   . LEU   B 1 126 ? 40.486 -29.206 -3.238  1.00 13.84 ?  126 LEU   B CB   1 
ATOM   5997 C  CG   . LEU   B 1 126 ? 39.958 -29.696 -4.587  1.00 14.89 ?  126 LEU   B CG   1 
ATOM   5998 C  CD1  . LEU   B 1 126 ? 40.004 -31.204 -4.657  1.00 16.83 ?  126 LEU   B CD1  1 
ATOM   5999 C  CD2  . LEU   B 1 126 ? 38.542 -29.204 -4.834  1.00 15.30 ?  126 LEU   B CD2  1 
ATOM   6000 H  H    . LEU   B 1 126 ? 42.468 -28.009 -4.040  1.00 14.37 ?  126 LEU   B H    1 
ATOM   6001 H  HA   . LEU   B 1 126 ? 39.989 -27.233 -3.516  1.00 14.96 ?  126 LEU   B HA   1 
ATOM   6002 H  HB2  . LEU   B 1 126 ? 41.320 -29.665 -3.068  1.00 16.61 ?  126 LEU   B HB2  1 
ATOM   6003 H  HB3  . LEU   B 1 126 ? 39.835 -29.451 -2.565  1.00 16.61 ?  126 LEU   B HB3  1 
ATOM   6004 H  HG   . LEU   B 1 126 ? 40.525 -29.346 -5.292  1.00 17.87 ?  126 LEU   B HG   1 
ATOM   6005 H  HD11 . LEU   B 1 126 ? 39.662 -31.490 -5.519  1.00 20.20 ?  126 LEU   B HD11 1 
ATOM   6006 H  HD12 . LEU   B 1 126 ? 40.918 -31.500 -4.546  1.00 20.20 ?  126 LEU   B HD12 1 
ATOM   6007 H  HD13 . LEU   B 1 126 ? 39.449 -31.569 -3.947  1.00 20.20 ?  126 LEU   B HD13 1 
ATOM   6008 H  HD21 . LEU   B 1 126 ? 38.201 -29.619 -5.642  1.00 18.36 ?  126 LEU   B HD21 1 
ATOM   6009 H  HD22 . LEU   B 1 126 ? 37.985 -29.444 -4.078  1.00 18.36 ?  126 LEU   B HD22 1 
ATOM   6010 H  HD23 . LEU   B 1 126 ? 38.554 -28.238 -4.941  1.00 18.36 ?  126 LEU   B HD23 1 
ATOM   6011 N  N    . LEU   B 1 127 ? 39.930 -26.475 -1.211  1.00 12.61 ?  127 LEU   B N    1 
ATOM   6012 C  CA   . LEU   B 1 127 ? 39.982 -25.984 0.153   1.00 13.28 ?  127 LEU   B CA   1 
ATOM   6013 C  C    . LEU   B 1 127 ? 39.710 -27.105 1.145   1.00 13.00 ?  127 LEU   B C    1 
ATOM   6014 O  O    . LEU   B 1 127 ? 38.889 -28.001 0.914   1.00 13.41 ?  127 LEU   B O    1 
ATOM   6015 C  CB   . LEU   B 1 127 ? 38.957 -24.870 0.357   1.00 13.62 ?  127 LEU   B CB   1 
ATOM   6016 C  CG   . LEU   B 1 127 ? 39.141 -23.606 -0.481  1.00 14.24 ?  127 LEU   B CG   1 
ATOM   6017 C  CD1  . LEU   B 1 127 ? 38.021 -22.634 -0.157  1.00 14.41 ?  127 LEU   B CD1  1 
ATOM   6018 C  CD2  . LEU   B 1 127 ? 40.503 -22.962 -0.241  1.00 14.92 ?  127 LEU   B CD2  1 
ATOM   6019 H  H    . LEU   B 1 127 ? 39.266 -26.170 -1.675  1.00 15.14 ?  127 LEU   B H    1 
ATOM   6020 H  HA   . LEU   B 1 127 ? 40.865 -25.621 0.329   1.00 15.95 ?  127 LEU   B HA   1 
ATOM   6021 H  HB2  . LEU   B 1 127 ? 38.077 -25.223 0.152   1.00 16.35 ?  127 LEU   B HB2  1 
ATOM   6022 H  HB3  . LEU   B 1 127 ? 38.983 -24.598 1.288   1.00 16.35 ?  127 LEU   B HB3  1 
ATOM   6023 H  HG   . LEU   B 1 127 ? 39.065 -23.829 -1.419  1.00 17.10 ?  127 LEU   B HG   1 
ATOM   6024 H  HD11 . LEU   B 1 127 ? 38.140 -21.822 -0.683  1.00 17.30 ?  127 LEU   B HD11 1 
ATOM   6025 H  HD12 . LEU   B 1 127 ? 37.166 -23.038 -0.371  1.00 17.30 ?  127 LEU   B HD12 1 
ATOM   6026 H  HD13 . LEU   B 1 127 ? 38.052 -22.412 0.789   1.00 17.30 ?  127 LEU   B HD13 1 
ATOM   6027 H  HD21 . LEU   B 1 127 ? 40.535 -22.106 -0.697  1.00 17.91 ?  127 LEU   B HD21 1 
ATOM   6028 H  HD22 . LEU   B 1 127 ? 40.626 -22.831 0.714   1.00 17.91 ?  127 LEU   B HD22 1 
ATOM   6029 H  HD23 . LEU   B 1 127 ? 41.190 -23.550 -0.586  1.00 17.91 ?  127 LEU   B HD23 1 
ATOM   6030 N  N    . SER   B 1 128 ? 40.396 -27.025 2.273   1.00 13.05 ?  128 SER   B N    1 
ATOM   6031 C  CA   . SER   B 1 128 ? 40.276 -27.938 3.395   1.00 13.46 ?  128 SER   B CA   1 
ATOM   6032 C  C    . SER   B 1 128 ? 40.764 -29.346 3.074   1.00 14.54 ?  128 SER   B C    1 
ATOM   6033 O  O    . SER   B 1 128 ? 40.663 -30.225 3.926   1.00 15.82 ?  128 SER   B O    1 
ATOM   6034 C  CB   . SER   B 1 128 ? 38.870 -27.939 4.014   1.00 13.69 ?  128 SER   B CB   1 
ATOM   6035 O  OG   . SER   B 1 128 ? 38.561 -26.663 4.567   1.00 14.26 ?  128 SER   B OG   1 
ATOM   6036 H  H    . SER   B 1 128 ? 40.968 -26.402 2.420   1.00 15.66 ?  128 SER   B H    1 
ATOM   6037 H  HA   . SER   B 1 128 ? 40.863 -27.608 4.080   1.00 16.16 ?  128 SER   B HA   1 
ATOM   6038 H  HB2  . SER   B 1 128 ? 38.214 -28.166 3.334   1.00 16.44 ?  128 SER   B HB2  1 
ATOM   6039 H  HB3  . SER   B 1 128 ? 38.841 -28.611 4.726   1.00 16.44 ?  128 SER   B HB3  1 
ATOM   6040 H  HG   . SER   B 1 128 ? 39.131 -26.469 5.154   1.00 17.12 ?  128 SER   B HG   1 
ATOM   6041 N  N    . ALA   B 1 129 ? 41.339 -29.570 1.890   1.00 15.57 ?  129 ALA   B N    1 
ATOM   6042 C  CA   . ALA   B 1 129 ? 41.885 -30.869 1.536   1.00 16.31 ?  129 ALA   B CA   1 
ATOM   6043 C  C    . ALA   B 1 129 ? 43.278 -31.043 2.129   1.00 15.53 ?  129 ALA   B C    1 
ATOM   6044 O  O    . ALA   B 1 129 ? 43.838 -30.144 2.771   1.00 15.24 ?  129 ALA   B O    1 
ATOM   6045 C  CB   . ALA   B 1 129 ? 41.947 -31.028 0.019   1.00 18.24 ?  129 ALA   B CB   1 
ATOM   6046 H  H    . ALA   B 1 129 ? 41.426 -28.979 1.267   1.00 18.70 ?  129 ALA   B H    1 
ATOM   6047 H  HA   . ALA   B 1 129 ? 41.312 -31.564 1.891   1.00 19.58 ?  129 ALA   B HA   1 
ATOM   6048 H  HB1  . ALA   B 1 129 ? 42.302 -31.909 -0.192  1.00 21.89 ?  129 ALA   B HB1  1 
ATOM   6049 H  HB2  . ALA   B 1 129 ? 41.056 -30.936 -0.346  1.00 21.89 ?  129 ALA   B HB2  1 
ATOM   6050 H  HB3  . ALA   B 1 129 ? 42.530 -30.344 -0.348  1.00 21.89 ?  129 ALA   B HB3  1 
ATOM   6051 N  N    . GLY   B 1 130 ? 43.843 -32.226 1.894   1.00 15.51 ?  130 GLY   B N    1 
ATOM   6052 C  CA   . GLY   B 1 130 ? 45.230 -32.464 2.246   1.00 16.11 ?  130 GLY   B CA   1 
ATOM   6053 C  C    . GLY   B 1 130 ? 45.445 -32.368 3.737   1.00 16.18 ?  130 GLY   B C    1 
ATOM   6054 O  O    . GLY   B 1 130 ? 44.746 -33.012 4.535   1.00 16.81 ?  130 GLY   B O    1 
ATOM   6055 H  H    . GLY   B 1 130 ? 43.447 -32.897 1.528   1.00 18.61 ?  130 GLY   B H    1 
ATOM   6056 H  HA2  . GLY   B 1 130 ? 45.494 -33.353 1.951   1.00 19.34 ?  130 GLY   B HA2  1 
ATOM   6057 H  HA3  . GLY   B 1 130 ? 45.797 -31.813 1.807   1.00 19.34 ?  130 GLY   B HA3  1 
ATOM   6058 N  N    . ILE   B 1 131 ? 46.422 -31.543 4.124   1.00 16.62 ?  131 ILE   B N    1 
ATOM   6059 C  CA   . ILE   B 1 131 ? 46.780 -31.413 5.525   1.00 17.29 ?  131 ILE   B CA   1 
ATOM   6060 C  C    . ILE   B 1 131 ? 45.665 -30.810 6.359   1.00 16.39 ?  131 ILE   B C    1 
ATOM   6061 O  O    . ILE   B 1 131 ? 45.736 -30.870 7.589   1.00 17.97 ?  131 ILE   B O    1 
ATOM   6062 C  CB   . ILE   B 1 131 ? 48.105 -30.637 5.720   1.00 19.23 ?  131 ILE   B CB   1 
ATOM   6063 C  CG1  . ILE   B 1 131 ? 47.942 -29.160 5.343   1.00 20.25 ?  131 ILE   B CG1  1 
ATOM   6064 C  CG2  . ILE   B 1 131 ? 49.222 -31.282 4.909   1.00 20.30 ?  131 ILE   B CG2  1 
ATOM   6065 C  CD1  . ILE   B 1 131 ? 49.155 -28.304 5.660   1.00 21.39 ?  131 ILE   B CD1  1 
ATOM   6066 H  H    . ILE   B 1 131 ? 46.890 -31.054 3.590   1.00 19.95 ?  131 ILE   B H    1 
ATOM   6067 H  HA   . ILE   B 1 131 ? 46.925 -32.301 5.875   1.00 20.75 ?  131 ILE   B HA   1 
ATOM   6068 H  HB   . ILE   B 1 131 ? 48.340 -30.684 6.662   1.00 23.09 ?  131 ILE   B HB   1 
ATOM   6069 H  HG12 . ILE   B 1 131 ? 47.774 -29.103 4.391   1.00 24.31 ?  131 ILE   B HG12 1 
ATOM   6070 H  HG13 . ILE   B 1 131 ? 47.188 -28.786 5.830   1.00 24.31 ?  131 ILE   B HG13 1 
ATOM   6071 H  HG21 . ILE   B 1 131 ? 50.065 -30.886 5.170   1.00 24.36 ?  131 ILE   B HG21 1 
ATOM   6072 H  HG22 . ILE   B 1 131 ? 49.227 -32.233 5.088   1.00 24.36 ?  131 ILE   B HG22 1 
ATOM   6073 H  HG23 . ILE   B 1 131 ? 49.053 -31.122 3.967   1.00 24.36 ?  131 ILE   B HG23 1 
ATOM   6074 H  HD11 . ILE   B 1 131 ? 48.938 -27.376 5.480   1.00 25.67 ?  131 ILE   B HD11 1 
ATOM   6075 H  HD12 . ILE   B 1 131 ? 49.383 -28.416 6.596   1.00 25.67 ?  131 ILE   B HD12 1 
ATOM   6076 H  HD13 . ILE   B 1 131 ? 49.894 -28.587 5.101   1.00 25.67 ?  131 ILE   B HD13 1 
ATOM   6077 N  N    . PHE   B 1 132 ? 44.637 -30.233 5.726   1.00 15.40 ?  132 PHE   B N    1 
ATOM   6078 C  CA   . PHE   B 1 132 ? 43.477 -29.730 6.455   1.00 15.64 ?  132 PHE   B CA   1 
ATOM   6079 C  C    . PHE   B 1 132 ? 42.453 -30.818 6.778   1.00 17.02 ?  132 PHE   B C    1 
ATOM   6080 O  O    . PHE   B 1 132 ? 41.542 -30.565 7.575   1.00 18.41 ?  132 PHE   B O    1 
ATOM   6081 C  CB   . PHE   B 1 132 ? 42.798 -28.595 5.678   1.00 14.90 ?  132 PHE   B CB   1 
ATOM   6082 C  CG   . PHE   B 1 132 ? 43.497 -27.254 5.789   1.00 14.78 ?  132 PHE   B CG   1 
ATOM   6083 C  CD1  . PHE   B 1 132 ? 44.792 -27.074 5.319   1.00 15.77 ?  132 PHE   B CD1  1 
ATOM   6084 C  CD2  . PHE   B 1 132 ? 42.828 -26.155 6.314   1.00 14.45 ?  132 PHE   B CD2  1 
ATOM   6085 C  CE1  . PHE   B 1 132 ? 45.416 -25.833 5.413   1.00 16.06 ?  132 PHE   B CE1  1 
ATOM   6086 C  CE2  . PHE   B 1 132 ? 43.441 -24.914 6.397   1.00 14.87 ?  132 PHE   B CE2  1 
ATOM   6087 C  CZ   . PHE   B 1 132 ? 44.734 -24.757 5.951   1.00 15.78 ?  132 PHE   B CZ   1 
ATOM   6088 H  H    . PHE   B 1 132 ? 44.582 -30.126 4.873   1.00 18.49 ?  132 PHE   B H    1 
ATOM   6089 H  HA   . PHE   B 1 132 ? 43.777 -29.362 7.297   1.00 18.77 ?  132 PHE   B HA   1 
ATOM   6090 H  HB2  . PHE   B 1 132 ? 42.776 -28.834 4.741   1.00 17.89 ?  132 PHE   B HB2  1 
ATOM   6091 H  HB3  . PHE   B 1 132 ? 41.891 -28.485 6.011   1.00 17.89 ?  132 PHE   B HB3  1 
ATOM   6092 H  HD1  . PHE   B 1 132 ? 45.255 -27.801 4.964   1.00 18.93 ?  132 PHE   B HD1  1 
ATOM   6093 H  HD2  . PHE   B 1 132 ? 41.956 -26.254 6.621   1.00 17.35 ?  132 PHE   B HD2  1 
ATOM   6094 H  HE1  . PHE   B 1 132 ? 46.288 -25.733 5.109   1.00 19.28 ?  132 PHE   B HE1  1 
ATOM   6095 H  HE2  . PHE   B 1 132 ? 42.985 -24.189 6.766   1.00 17.84 ?  132 PHE   B HE2  1 
ATOM   6096 H  HZ   . PHE   B 1 132 ? 45.150 -23.924 6.013   1.00 18.94 ?  132 PHE   B HZ   1 
ATOM   6097 N  N    . GLY   B 1 133 ? 42.560 -32.010 6.182   1.00 16.90 ?  133 GLY   B N    1 
ATOM   6098 C  CA   . GLY   B 1 133 ? 41.845 -33.176 6.671   1.00 17.86 ?  133 GLY   B CA   1 
ATOM   6099 C  C    . GLY   B 1 133 ? 40.444 -33.428 6.142   1.00 18.35 ?  133 GLY   B C    1 
ATOM   6100 O  O    . GLY   B 1 133 ? 39.853 -34.447 6.509   1.00 20.18 ?  133 GLY   B O    1 
ATOM   6101 H  H    . GLY   B 1 133 ? 43.049 -32.162 5.490   1.00 20.29 ?  133 GLY   B H    1 
ATOM   6102 H  HA2  . GLY   B 1 133 ? 42.379 -33.961 6.472   1.00 21.44 ?  133 GLY   B HA2  1 
ATOM   6103 H  HA3  . GLY   B 1 133 ? 41.777 -33.105 7.634   1.00 21.44 ?  133 GLY   B HA3  1 
ATOM   6104 N  N    . ALA   B 1 134 ? 39.881 -32.557 5.313   1.00 17.52 ?  134 ALA   B N    1 
ATOM   6105 C  CA   . ALA   B 1 134 ? 38.558 -32.851 4.784   1.00 17.36 ?  134 ALA   B CA   1 
ATOM   6106 C  C    . ALA   B 1 134 ? 38.645 -33.845 3.632   1.00 17.39 ?  134 ALA   B C    1 
ATOM   6107 O  O    . ALA   B 1 134 ? 39.699 -34.038 3.020   1.00 18.31 ?  134 ALA   B O    1 
ATOM   6108 C  CB   . ALA   B 1 134 ? 37.870 -31.577 4.303   1.00 17.64 ?  134 ALA   B CB   1 
ATOM   6109 H  H    . ALA   B 1 134 ? 40.228 -31.810 5.056   1.00 21.02 ?  134 ALA   B H    1 
ATOM   6110 H  HA   . ALA   B 1 134 ? 38.014 -33.239 5.489   1.00 20.83 ?  134 ALA   B HA   1 
ATOM   6111 H  HB1  . ALA   B 1 134 ? 36.985 -31.803 3.974   1.00 21.18 ?  134 ALA   B HB1  1 
ATOM   6112 H  HB2  . ALA   B 1 134 ? 37.798 -30.956 5.045   1.00 21.18 ?  134 ALA   B HB2  1 
ATOM   6113 H  HB3  . ALA   B 1 134 ? 38.397 -31.183 3.591   1.00 21.18 ?  134 ALA   B HB3  1 
ATOM   6114 N  N    . ASP   B 1 135 ? 37.509 -34.467 3.339   1.00 17.84 ?  135 ASP   B N    1 
ATOM   6115 C  CA   . ASP   B 1 135 ? 37.409 -35.357 2.196   1.00 18.42 ?  135 ASP   B CA   1 
ATOM   6116 C  C    . ASP   B 1 135 ? 37.513 -34.521 0.927   1.00 17.19 ?  135 ASP   B C    1 
ATOM   6117 O  O    . ASP   B 1 135 ? 36.660 -33.650 0.700   1.00 17.04 ?  135 ASP   B O    1 
ATOM   6118 C  CB   . ASP   B 1 135 ? 36.067 -36.086 2.248   1.00 19.92 ?  135 ASP   B CB   1 
ATOM   6119 C  CG   . ASP   B 1 135 ? 35.892 -37.085 1.123   1.00 21.65 ?  135 ASP   B CG   1 
ATOM   6120 O  OD1  . ASP   B 1 135 ? 36.761 -37.138 0.225   1.00 21.37 ?  135 ASP   B OD1  1 
ATOM   6121 O  OD2  . ASP   B 1 135 ? 34.891 -37.841 1.149   1.00 24.18 -1 135 ASP   B OD2  1 
ATOM   6122 H  H    . ASP   B 1 135 ? 36.780 -34.387 3.788   1.00 21.42 ?  135 ASP   B H    1 
ATOM   6123 H  HA   . ASP   B 1 135 ? 38.126 -36.013 2.229   1.00 22.11 ?  135 ASP   B HA   1 
ATOM   6124 H  HB2  . ASP   B 1 135 ? 36.005 -36.562 3.089   1.00 23.91 ?  135 ASP   B HB2  1 
ATOM   6125 H  HB3  . ASP   B 1 135 ? 35.358 -35.432 2.179   1.00 23.91 ?  135 ASP   B HB3  1 
ATOM   6126 N  N    . PRO   B 1 136 ? 38.530 -34.726 0.089   1.00 17.24 ?  136 PRO   B N    1 
ATOM   6127 C  CA   . PRO   B 1 136 ? 38.627 -33.911 -1.131  1.00 16.40 ?  136 PRO   B CA   1 
ATOM   6128 C  C    . PRO   B 1 136 ? 37.433 -34.066 -2.051  1.00 15.94 ?  136 PRO   B C    1 
ATOM   6129 O  O    . PRO   B 1 136 ? 37.110 -33.121 -2.777  1.00 15.28 ?  136 PRO   B O    1 
ATOM   6130 C  CB   . PRO   B 1 136 ? 39.934 -34.391 -1.779  1.00 17.36 ?  136 PRO   B CB   1 
ATOM   6131 C  CG   . PRO   B 1 136 ? 40.145 -35.766 -1.223  1.00 18.54 ?  136 PRO   B CG   1 
ATOM   6132 C  CD   . PRO   B 1 136 ? 39.624 -35.707 0.181   1.00 18.31 ?  136 PRO   B CD   1 
ATOM   6133 H  HA   . PRO   B 1 136 ? 38.717 -32.975 -0.902  1.00 19.69 ?  136 PRO   B HA   1 
ATOM   6134 H  HB2  . PRO   B 1 136 ? 39.837 -34.421 -2.745  1.00 20.84 ?  136 PRO   B HB2  1 
ATOM   6135 H  HB3  . PRO   B 1 136 ? 40.661 -33.801 -1.526  1.00 20.84 ?  136 PRO   B HB3  1 
ATOM   6136 H  HG2  . PRO   B 1 136 ? 39.644 -36.414 -1.744  1.00 22.25 ?  136 PRO   B HG2  1 
ATOM   6137 H  HG3  . PRO   B 1 136 ? 41.091 -35.983 -1.226  1.00 22.25 ?  136 PRO   B HG3  1 
ATOM   6138 H  HD2  . PRO   B 1 136 ? 39.283 -36.572 0.454   1.00 21.97 ?  136 PRO   B HD2  1 
ATOM   6139 H  HD3  . PRO   B 1 136 ? 40.312 -35.387 0.789   1.00 21.97 ?  136 PRO   B HD3  1 
ATOM   6140 N  N    . ILE   B 1 137 ? 36.771 -35.229 -2.051  1.00 16.44 ?  137 ILE   B N    1 
ATOM   6141 C  CA   . ILE   B 1 137 ? 35.555 -35.396 -2.843  1.00 16.62 ?  137 ILE   B CA   1 
ATOM   6142 C  C    . ILE   B 1 137 ? 34.481 -34.425 -2.371  1.00 16.03 ?  137 ILE   B C    1 
ATOM   6143 O  O    . ILE   B 1 137 ? 33.769 -33.813 -3.177  1.00 15.80 ?  137 ILE   B O    1 
ATOM   6144 C  CB   . ILE   B 1 137 ? 35.079 -36.863 -2.779  1.00 18.52 ?  137 ILE   B CB   1 
ATOM   6145 C  CG1  . ILE   B 1 137 ? 36.091 -37.773 -3.478  1.00 20.74 ?  137 ILE   B CG1  1 
ATOM   6146 C  CG2  . ILE   B 1 137 ? 33.687 -37.006 -3.397  1.00 19.06 ?  137 ILE   B CG2  1 
ATOM   6147 C  CD1  . ILE   B 1 137 ? 35.780 -39.255 -3.352  1.00 22.91 ?  137 ILE   B CD1  1 
ATOM   6148 H  H    . ILE   B 1 137 ? 37.006 -35.931 -1.612  1.00 19.73 ?  137 ILE   B H    1 
ATOM   6149 H  HA   . ILE   B 1 137 ? 35.751 -35.196 -3.774  1.00 19.94 ?  137 ILE   B HA   1 
ATOM   6150 H  HB   . ILE   B 1 137 ? 35.020 -37.127 -1.852  1.00 22.23 ?  137 ILE   B HB   1 
ATOM   6151 H  HG12 . ILE   B 1 137 ? 36.111 -37.562 -4.423  1.00 24.90 ?  137 ILE   B HG12 1 
ATOM   6152 H  HG13 . ILE   B 1 137 ? 36.965 -37.629 -3.087  1.00 24.90 ?  137 ILE   B HG13 1 
ATOM   6153 H  HG21 . ILE   B 1 137 ? 33.459 -37.947 -3.479  1.00 22.88 ?  137 ILE   B HG21 1 
ATOM   6154 H  HG22 . ILE   B 1 137 ? 33.033 -36.572 -2.825  1.00 22.88 ?  137 ILE   B HG22 1 
ATOM   6155 H  HG23 . ILE   B 1 137 ? 33.681 -36.593 -4.276  1.00 22.88 ?  137 ILE   B HG23 1 
ATOM   6156 H  HD11 . ILE   B 1 137 ? 36.519 -39.758 -3.726  1.00 27.50 ?  137 ILE   B HD11 1 
ATOM   6157 H  HD12 . ILE   B 1 137 ? 35.667 -39.480 -2.414  1.00 27.50 ?  137 ILE   B HD12 1 
ATOM   6158 H  HD13 . ILE   B 1 137 ? 34.967 -39.459 -3.842  1.00 27.50 ?  137 ILE   B HD13 1 
ATOM   6159 N  N    . HIS   B 1 138 ? 34.349 -34.273 -1.058  1.00 16.23 ?  138 HIS   B N    1 
ATOM   6160 C  CA   . HIS   B 1 138 ? 33.401 -33.306 -0.521  1.00 16.66 ?  138 HIS   B CA   1 
ATOM   6161 C  C    . HIS   B 1 138 ? 33.823 -31.878 -0.842  1.00 15.74 ?  138 HIS   B C    1 
ATOM   6162 O  O    . HIS   B 1 138 ? 32.979 -31.032 -1.158  1.00 16.11 ?  138 HIS   B O    1 
ATOM   6163 C  CB   . HIS   B 1 138 ? 33.284 -33.491 0.984   1.00 17.91 ?  138 HIS   B CB   1 
ATOM   6164 C  CG   . HIS   B 1 138 ? 32.361 -32.508 1.627   1.00 19.18 ?  138 HIS   B CG   1 
ATOM   6165 N  ND1  . HIS   B 1 138 ? 31.023 -32.430 1.308   1.00 20.62 ?  138 HIS   B ND1  1 
ATOM   6166 C  CD2  . HIS   B 1 138 ? 32.589 -31.535 2.540   1.00 19.78 ?  138 HIS   B CD2  1 
ATOM   6167 C  CE1  . HIS   B 1 138 ? 30.461 -31.464 2.011   1.00 20.75 ?  138 HIS   B CE1  1 
ATOM   6168 N  NE2  . HIS   B 1 138 ? 31.388 -30.908 2.770   1.00 20.17 ?  138 HIS   B NE2  1 
ATOM   6169 H  H    . HIS   B 1 138 ? 34.793 -34.714 -0.468  1.00 19.48 ?  138 HIS   B H    1 
ATOM   6170 H  HA   . HIS   B 1 138 ? 32.529 -33.468 -0.917  1.00 19.99 ?  138 HIS   B HA   1 
ATOM   6171 H  HB2  . HIS   B 1 138 ? 32.942 -34.380 1.167   1.00 21.50 ?  138 HIS   B HB2  1 
ATOM   6172 H  HB3  . HIS   B 1 138 ? 34.159 -33.382 1.383   1.00 21.50 ?  138 HIS   B HB3  1 
ATOM   6173 H  HD1  . HIS   B 1 138 ? 30.615 -32.938 0.743   1.00 24.75 ?  138 HIS   B HD1  1 
ATOM   6174 H  HD2  . HIS   B 1 138 ? 33.396 -31.337 2.950   1.00 23.74 ?  138 HIS   B HD2  1 
ATOM   6175 H  HE1  . HIS   B 1 138 ? 29.559 -31.227 1.983   1.00 24.90 ?  138 HIS   B HE1  1 
ATOM   6176 N  N    . SER   B 1 139 ? 35.116 -31.581 -0.761  1.00 15.52 ?  139 SER   B N    1 
ATOM   6177 C  CA   . SER   B 1 139 ? 35.558 -30.232 -1.081  1.00 14.78 ?  139 SER   B CA   1 
ATOM   6178 C  C    . SER   B 1 139 ? 35.220 -29.880 -2.521  1.00 13.88 ?  139 SER   B C    1 
ATOM   6179 O  O    . SER   B 1 139 ? 34.770 -28.766 -2.805  1.00 13.89 ?  139 SER   B O    1 
ATOM   6180 C  CB   . SER   B 1 139 ? 37.052 -30.094 -0.815  1.00 14.98 ?  139 SER   B CB   1 
ATOM   6181 O  OG   . SER   B 1 139 ? 37.459 -28.762 -1.070  1.00 14.99 ?  139 SER   B OG   1 
ATOM   6182 H  H    . SER   B 1 139 ? 35.736 -32.125 -0.537  1.00 18.62 ?  139 SER   B H    1 
ATOM   6183 H  HA   . SER   B 1 139 ? 35.086 -29.604 -0.515  1.00 17.74 ?  139 SER   B HA   1 
ATOM   6184 H  HB2  . SER   B 1 139 ? 37.226 -30.309 0.115   1.00 17.99 ?  139 SER   B HB2  1 
ATOM   6185 H  HB3  . SER   B 1 139 ? 37.538 -30.694 -1.397  1.00 17.99 ?  139 SER   B HB3  1 
ATOM   6186 H  HG   . SER   B 1 139 ? 38.286 -28.680 -0.918  1.00 18.00 ?  139 SER   B HG   1 
ATOM   6187 N  N    . LEU   B 1 140 ? 35.411 -30.825 -3.443  1.00 13.56 ?  140 LEU   B N    1 
ATOM   6188 C  CA   . LEU   B 1 140 ? 35.046 -30.584 -4.831  1.00 13.52 ?  140 LEU   B CA   1 
ATOM   6189 C  C    . LEU   B 1 140 ? 33.545 -30.355 -4.966  1.00 13.83 ?  140 LEU   B C    1 
ATOM   6190 O  O    . LEU   B 1 140 ? 33.110 -29.469 -5.706  1.00 13.94 ?  140 LEU   B O    1 
ATOM   6191 C  CB   . LEU   B 1 140 ? 35.518 -31.745 -5.704  1.00 13.75 ?  140 LEU   B CB   1 
ATOM   6192 C  CG   . LEU   B 1 140 ? 35.156 -31.638 -7.177  1.00 13.85 ?  140 LEU   B CG   1 
ATOM   6193 C  CD1  . LEU   B 1 140 ? 35.723 -30.366 -7.766  1.00 14.80 ?  140 LEU   B CD1  1 
ATOM   6194 C  CD2  . LEU   B 1 140 ? 35.634 -32.866 -7.928  1.00 15.36 ?  140 LEU   B CD2  1 
ATOM   6195 H  H    . LEU   B 1 140 ? 35.742 -31.604 -3.294  1.00 16.28 ?  140 LEU   B H    1 
ATOM   6196 H  HA   . LEU   B 1 140 ? 35.500 -29.782 -5.139  1.00 16.23 ?  140 LEU   B HA   1 
ATOM   6197 H  HB2  . LEU   B 1 140 ? 36.485 -31.806 -5.648  1.00 16.50 ?  140 LEU   B HB2  1 
ATOM   6198 H  HB3  . LEU   B 1 140 ? 35.121 -32.566 -5.372  1.00 16.50 ?  140 LEU   B HB3  1 
ATOM   6199 H  HG   . LEU   B 1 140 ? 34.193 -31.591 -7.262  1.00 16.62 ?  140 LEU   B HG   1 
ATOM   6200 H  HD11 . LEU   B 1 140 ? 35.628 -30.396 -8.729  1.00 17.77 ?  140 LEU   B HD11 1 
ATOM   6201 H  HD12 . LEU   B 1 140 ? 35.233 -29.605 -7.410  1.00 17.77 ?  140 LEU   B HD12 1 
ATOM   6202 H  HD13 . LEU   B 1 140 ? 36.660 -30.296 -7.526  1.00 17.77 ?  140 LEU   B HD13 1 
ATOM   6203 H  HD21 . LEU   B 1 140 ? 35.388 -32.771 -8.863  1.00 18.44 ?  140 LEU   B HD21 1 
ATOM   6204 H  HD22 . LEU   B 1 140 ? 36.592 -32.935 -7.839  1.00 18.44 ?  140 LEU   B HD22 1 
ATOM   6205 H  HD23 . LEU   B 1 140 ? 35.200 -33.645 -7.550  1.00 18.44 ?  140 LEU   B HD23 1 
ATOM   6206 N  N    . ARG   B 1 141 ? 32.740 -31.147 -4.254  1.00 14.01 ?  141 ARG   B N    1 
ATOM   6207 C  CA   . ARG   B 1 141 ? 31.291 -30.967 -4.233  1.00 15.13 ?  141 ARG   B CA   1 
ATOM   6208 C  C    . ARG   B 1 141 ? 30.917 -29.555 -3.810  1.00 14.49 ?  141 ARG   B C    1 
ATOM   6209 O  O    . ARG   B 1 141 ? 30.114 -28.879 -4.470  1.00 14.57 ?  141 ARG   B O    1 
ATOM   6210 C  CB   . ARG   B 1 141 ? 30.706 -31.988 -3.248  1.00 16.27 ?  141 ARG   B CB   1 
ATOM   6211 C  CG   . ARG   B 1 141 ? 29.240 -31.874 -2.927  1.00 18.13 ?  141 ARG   B CG   1 
ATOM   6212 C  CD   . ARG   B 1 141 ? 28.449 -32.521 -3.992  1.00 19.63 ?  141 ARG   B CD   1 
ATOM   6213 N  NE   . ARG   B 1 141 ? 28.191 -31.613 -5.098  1.00 19.93 ?  141 ARG   B NE   1 
ATOM   6214 C  CZ   . ARG   B 1 141 ? 28.189 -31.962 -6.377  1.00 19.62 ?  141 ARG   B CZ   1 
ATOM   6215 N  NH1  . ARG   B 1 141 ? 28.603 -33.157 -6.771  1.00 19.40 ?  141 ARG   B NH1  1 
ATOM   6216 N  NH2  . ARG   B 1 141 ? 27.759 -31.090 -7.283  1.00 20.45 ?  141 ARG   B NH2  1 
ATOM   6217 H  H    . ARG   B 1 141 ? 33.018 -31.799 -3.772  1.00 16.82 ?  141 ARG   B H    1 
ATOM   6218 H  HA   . ARG   B 1 141 ? 30.923 -31.136 -5.112  1.00 18.17 ?  141 ARG   B HA   1 
ATOM   6219 H  HB2  . ARG   B 1 141 ? 30.863 -32.878 -3.605  1.00 19.52 ?  141 ARG   B HB2  1 
ATOM   6220 H  HB3  . ARG   B 1 141 ? 31.186 -31.904 -2.409  1.00 19.52 ?  141 ARG   B HB3  1 
ATOM   6221 H  HG2  . ARG   B 1 141 ? 29.064 -32.315 -2.085  1.00 21.76 ?  141 ARG   B HG2  1 
ATOM   6222 H  HG3  . ARG   B 1 141 ? 28.985 -30.934 -2.872  1.00 21.76 ?  141 ARG   B HG3  1 
ATOM   6223 H  HD2  . ARG   B 1 141 ? 28.935 -33.296 -4.325  1.00 23.57 ?  141 ARG   B HD2  1 
ATOM   6224 H  HD3  . ARG   B 1 141 ? 27.602 -32.803 -3.624  1.00 23.57 ?  141 ARG   B HD3  1 
ATOM   6225 H  HE   . ARG   B 1 141 ? 28.008 -30.794 -4.907  1.00 23.92 ?  141 ARG   B HE   1 
ATOM   6226 H  HH11 . ARG   B 1 141 ? 28.875 -33.739 -6.199  1.00 23.28 ?  141 ARG   B HH11 1 
ATOM   6227 H  HH12 . ARG   B 1 141 ? 28.601 -33.356 -7.607  1.00 23.28 ?  141 ARG   B HH12 1 
ATOM   6228 H  HH21 . ARG   B 1 141 ? 27.497 -30.308 -7.039  1.00 24.55 ?  141 ARG   B HH21 1 
ATOM   6229 H  HH22 . ARG   B 1 141 ? 27.773 -31.296 -8.119  1.00 24.55 ?  141 ARG   B HH22 1 
ATOM   6230 N  N    . VAL   B 1 142 ? 31.462 -29.108 -2.681  1.00 14.23 ?  142 VAL   B N    1 
ATOM   6231 C  CA   . VAL   B 1 142 ? 31.128 -27.775 -2.196  1.00 14.09 ?  142 VAL   B CA   1 
ATOM   6232 C  C    . VAL   B 1 142 ? 31.605 -26.719 -3.183  1.00 13.92 ?  142 VAL   B C    1 
ATOM   6233 O  O    . VAL   B 1 142 ? 30.906 -25.732 -3.440  1.00 14.21 ?  142 VAL   B O    1 
ATOM   6234 C  CB   . VAL   B 1 142 ? 31.680 -27.550 -0.776  1.00 14.89 ?  142 VAL   B CB   1 
ATOM   6235 C  CG1  . VAL   B 1 142 ? 31.377 -26.128 -0.304  1.00 14.63 ?  142 VAL   B CG1  1 
ATOM   6236 C  CG2  . VAL   B 1 142 ? 31.093 -28.572 0.181   1.00 15.67 ?  142 VAL   B CG2  1 
ATOM   6237 H  H    . VAL   B 1 142 ? 32.019 -29.545 -2.190  1.00 17.09 ?  142 VAL   B H    1 
ATOM   6238 H  HA   . VAL   B 1 142 ? 30.169 -27.701 -2.142  1.00 16.91 ?  142 VAL   B HA   1 
ATOM   6239 H  HB   . VAL   B 1 142 ? 32.646 -27.665 -0.786  1.00 17.87 ?  142 VAL   B HB   1 
ATOM   6240 H  HG11 . VAL   B 1 142 ? 31.573 -26.063 0.642   1.00 17.56 ?  142 VAL   B HG11 1 
ATOM   6241 H  HG12 . VAL   B 1 142 ? 31.935 -25.504 -0.798  1.00 17.56 ?  142 VAL   B HG12 1 
ATOM   6242 H  HG13 . VAL   B 1 142 ? 30.443 -25.937 -0.465  1.00 17.56 ?  142 VAL   B HG13 1 
ATOM   6243 H  HG21 . VAL   B 1 142 ? 31.411 -28.384 1.077   1.00 18.81 ?  142 VAL   B HG21 1 
ATOM   6244 H  HG22 . VAL   B 1 142 ? 30.126 -28.509 0.151   1.00 18.81 ?  142 VAL   B HG22 1 
ATOM   6245 H  HG23 . VAL   B 1 142 ? 31.376 -29.459 -0.092  1.00 18.81 ?  142 VAL   B HG23 1 
ATOM   6246 N  N    . CYS   B 1 143 ? 32.789 -26.913 -3.765  1.00 13.41 ?  143 CYS   B N    1 
ATOM   6247 C  CA   . CYS   B 1 143 ? 33.282 -25.977 -4.769  1.00 13.53 ?  143 CYS   B CA   1 
ATOM   6248 C  C    . CYS   B 1 143 ? 32.278 -25.832 -5.908  1.00 13.46 ?  143 CYS   B C    1 
ATOM   6249 O  O    . CYS   B 1 143 ? 31.865 -24.722 -6.261  1.00 13.61 ?  143 CYS   B O    1 
ATOM   6250 C  CB   . CYS   B 1 143 ? 34.637 -26.464 -5.296  1.00 13.76 ?  143 CYS   B CB   1 
ATOM   6251 S  SG   . CYS   B 1 143 ? 35.385 -25.367 -6.516  1.00 13.87 ?  143 CYS   B SG   1 
ATOM   6252 H  H    . CYS   B 1 143 ? 33.326 -27.564 -3.596  1.00 16.09 ?  143 CYS   B H    1 
ATOM   6253 H  HA   . CYS   B 1 143 ? 33.417 -25.103 -4.368  1.00 16.25 ?  143 CYS   B HA   1 
ATOM   6254 H  HB2  . CYS   B 1 143 ? 35.262 -26.544 -4.557  1.00 16.52 ?  143 CYS   B HB2  1 
ATOM   6255 H  HB3  . CYS   B 1 143 ? 34.522 -27.328 -5.715  1.00 16.52 ?  143 CYS   B HB3  1 
ATOM   6256 H  HG   . CYS   B 1 143 ? 36.462 -25.801 -6.834  1.00 16.64 ?  143 CYS   B HG   1 
ATOM   6257 N  N    . VAL   B 1 144 ? 31.881 -26.953 -6.502  1.00 13.86 ?  144 VAL   B N    1 
ATOM   6258 C  CA   . VAL   B 1 144 ? 30.971 -26.902 -7.641  1.00 14.96 ?  144 VAL   B CA   1 
ATOM   6259 C  C    . VAL   B 1 144 ? 29.632 -26.282 -7.258  1.00 15.17 ?  144 VAL   B C    1 
ATOM   6260 O  O    . VAL   B 1 144 ? 29.015 -25.570 -8.058  1.00 16.29 ?  144 VAL   B O    1 
ATOM   6261 C  CB   . VAL   B 1 144 ? 30.805 -28.314 -8.213  1.00 17.25 ?  144 VAL   B CB   1 
ATOM   6262 C  CG1  . VAL   B 1 144 ? 29.522 -28.435 -9.033  1.00 19.42 ?  144 VAL   B CG1  1 
ATOM   6263 C  CG2  . VAL   B 1 144 ? 32.039 -28.707 -9.011  1.00 17.38 ?  144 VAL   B CG2  1 
ATOM   6264 H  H    . VAL   B 1 144 ? 32.133 -27.745 -6.280  1.00 16.64 ?  144 VAL   B H    1 
ATOM   6265 H  HA   . VAL   B 1 144 ? 31.356 -26.346 -8.337  1.00 17.96 ?  144 VAL   B HA   1 
ATOM   6266 H  HB   . VAL   B 1 144 ? 30.729 -28.937 -7.471  1.00 20.71 ?  144 VAL   B HB   1 
ATOM   6267 H  HG11 . VAL   B 1 144 ? 29.591 -29.222 -9.601  1.00 23.31 ?  144 VAL   B HG11 1 
ATOM   6268 H  HG12 . VAL   B 1 144 ? 28.768 -28.534 -8.432  1.00 23.31 ?  144 VAL   B HG12 1 
ATOM   6269 H  HG13 . VAL   B 1 144 ? 29.418 -27.645 -9.580  1.00 23.31 ?  144 VAL   B HG13 1 
ATOM   6270 H  HG21 . VAL   B 1 144 ? 31.918 -29.607 -9.358  1.00 20.87 ?  144 VAL   B HG21 1 
ATOM   6271 H  HG22 . VAL   B 1 144 ? 32.150 -28.085 -9.747  1.00 20.87 ?  144 VAL   B HG22 1 
ATOM   6272 H  HG23 . VAL   B 1 144 ? 32.813 -28.679 -8.431  1.00 20.87 ?  144 VAL   B HG23 1 
ATOM   6273 N  N    . ASP   B 1 145 ? 29.164 -26.530 -6.039  1.00 15.26 ?  145 ASP   B N    1 
ATOM   6274 C  CA   . ASP   B 1 145 ? 27.852 -26.061 -5.613  1.00 15.72 ?  145 ASP   B CA   1 
ATOM   6275 C  C    . ASP   B 1 145 ? 27.881 -24.636 -5.071  1.00 15.20 ?  145 ASP   B C    1 
ATOM   6276 O  O    . ASP   B 1 145 ? 26.820 -24.094 -4.735  1.00 17.03 ?  145 ASP   B O    1 
ATOM   6277 C  CB   . ASP   B 1 145 ? 27.264 -26.982 -4.535  1.00 17.02 ?  145 ASP   B CB   1 
ATOM   6278 C  CG   . ASP   B 1 145 ? 26.903 -28.356 -5.049  1.00 18.47 ?  145 ASP   B CG   1 
ATOM   6279 O  OD1  . ASP   B 1 145 ? 26.811 -28.547 -6.278  1.00 18.82 ?  145 ASP   B OD1  1 
ATOM   6280 O  OD2  . ASP   B 1 145 ? 26.707 -29.241 -4.196  1.00 20.56 -1 145 ASP   B OD2  1 
ATOM   6281 H  H    . ASP   B 1 145 ? 29.600 -26.948 -5.429  1.00 18.32 ?  145 ASP   B H    1 
ATOM   6282 H  HA   . ASP   B 1 145 ? 27.260 -26.057 -6.379  1.00 18.87 ?  145 ASP   B HA   1 
ATOM   6283 H  HB2  . ASP   B 1 145 ? 27.910 -27.097 -3.834  1.00 20.43 ?  145 ASP   B HB2  1 
ATOM   6284 H  HB3  . ASP   B 1 145 ? 26.453 -26.576 -4.191  1.00 20.43 ?  145 ASP   B HB3  1 
ATOM   6285 N  N    . THR   B 1 146 ? 29.060 -24.022 -4.966  1.00 13.61 ?  146 THR   B N    1 
ATOM   6286 C  CA   . THR   B 1 146 ? 29.187 -22.699 -4.362  1.00 13.32 ?  146 THR   B CA   1 
ATOM   6287 C  C    . THR   B 1 146 ? 29.824 -21.671 -5.279  1.00 12.97 ?  146 THR   B C    1 
ATOM   6288 O  O    . THR   B 1 146 ? 29.375 -20.512 -5.324  1.00 13.31 ?  146 THR   B O    1 
ATOM   6289 C  CB   . THR   B 1 146 ? 30.020 -22.805 -3.082  1.00 13.61 ?  146 THR   B CB   1 
ATOM   6290 O  OG1  . THR   B 1 146 ? 29.451 -23.795 -2.218  1.00 13.83 ?  146 THR   B OG1  1 
ATOM   6291 C  CG2  . THR   B 1 146 ? 30.101 -21.463 -2.366  1.00 14.00 ?  146 THR   B CG2  1 
ATOM   6292 H  H    . THR   B 1 146 ? 29.812 -24.344 -5.242  1.00 16.34 ?  146 THR   B H    1 
ATOM   6293 H  HA   . THR   B 1 146 ? 28.313 -22.369 -4.119  1.00 15.99 ?  146 THR   B HA   1 
ATOM   6294 H  HB   . THR   B 1 146 ? 30.928 -23.065 -3.315  1.00 16.33 ?  146 THR   B HB   1 
ATOM   6295 H  HG1  . THR   B 1 146 ? 29.486 -24.554 -2.595  1.00 16.60 ?  146 THR   B HG1  1 
ATOM   6296 H  HG21 . THR   B 1 146 ? 30.444 -21.585 -1.469  1.00 16.81 ?  146 THR   B HG21 1 
ATOM   6297 H  HG22 . THR   B 1 146 ? 30.697 -20.862 -2.849  1.00 16.81 ?  146 THR   B HG22 1 
ATOM   6298 H  HG23 . THR   B 1 146 ? 29.222 -21.060 -2.318  1.00 16.81 ?  146 THR   B HG23 1 
ATOM   6299 N  N    . VAL   B 1 147 ? 30.889 -22.046 -5.977  1.00 12.77 ?  147 VAL   B N    1 
ATOM   6300 C  CA   . VAL   B 1 147 ? 31.613 -21.104 -6.816  1.00 12.51 ?  147 VAL   B CA   1 
ATOM   6301 C  C    . VAL   B 1 147 ? 30.878 -20.973 -8.137  1.00 12.73 ?  147 VAL   B C    1 
ATOM   6302 O  O    . VAL   B 1 147 ? 30.503 -21.977 -8.757  1.00 13.65 ?  147 VAL   B O    1 
ATOM   6303 C  CB   . VAL   B 1 147 ? 33.066 -21.563 -7.026  1.00 12.94 ?  147 VAL   B CB   1 
ATOM   6304 C  CG1  . VAL   B 1 147 ? 33.822 -20.533 -7.834  1.00 13.05 ?  147 VAL   B CG1  1 
ATOM   6305 C  CG2  . VAL   B 1 147 ? 33.746 -21.786 -5.692  1.00 12.89 ?  147 VAL   B CG2  1 
ATOM   6306 H  H    . VAL   B 1 147 ? 31.212 -22.846 -5.993  1.00 15.33 ?  147 VAL   B H    1 
ATOM   6307 H  HA   . VAL   B 1 147 ? 31.631 -20.238 -6.388  1.00 15.01 ?  147 VAL   B HA   1 
ATOM   6308 H  HB   . VAL   B 1 147 ? 33.074 -22.404 -7.520  1.00 15.53 ?  147 VAL   B HB   1 
ATOM   6309 H  HG11 . VAL   B 1 147 ? 34.765 -20.754 -7.824  1.00 15.66 ?  147 VAL   B HG11 1 
ATOM   6310 H  HG12 . VAL   B 1 147 ? 33.491 -20.534 -8.745  1.00 15.66 ?  147 VAL   B HG12 1 
ATOM   6311 H  HG13 . VAL   B 1 147 ? 33.684 -19.660 -7.432  1.00 15.66 ?  147 VAL   B HG13 1 
ATOM   6312 H  HG21 . VAL   B 1 147 ? 34.686 -21.985 -5.845  1.00 15.48 ?  147 VAL   B HG21 1 
ATOM   6313 H  HG22 . VAL   B 1 147 ? 33.664 -20.980 -5.159  1.00 15.48 ?  147 VAL   B HG22 1 
ATOM   6314 H  HG23 . VAL   B 1 147 ? 33.323 -22.529 -5.237  1.00 15.48 ?  147 VAL   B HG23 1 
ATOM   6315 N  N    . ARG   B 1 148 ? 30.670 -19.726 -8.561  1.00 12.66 ?  148 ARG   B N    1 
ATOM   6316 C  CA   . ARG   B 1 148 ? 30.049 -19.414 -9.836  1.00 12.98 ?  148 ARG   B CA   1 
ATOM   6317 C  C    . ARG   B 1 148 ? 31.003 -18.737 -10.808 1.00 12.97 ?  148 ARG   B C    1 
ATOM   6318 O  O    . ARG   B 1 148 ? 30.718 -18.711 -12.008 1.00 14.53 ?  148 ARG   B O    1 
ATOM   6319 C  CB   . ARG   B 1 148 ? 28.808 -18.532 -9.622  1.00 13.47 ?  148 ARG   B CB   1 
ATOM   6320 C  CG   . ARG   B 1 148 ? 27.730 -19.243 -8.813  1.00 14.58 ?  148 ARG   B CG   1 
ATOM   6321 C  CD   . ARG   B 1 148 ? 26.521 -18.355 -8.488  1.00 15.08 ?  148 ARG   B CD   1 
ATOM   6322 N  NE   . ARG   B 1 148 ? 26.911 -17.154 -7.763  1.00 14.92 ?  148 ARG   B NE   1 
ATOM   6323 C  CZ   . ARG   B 1 148 ? 27.214 -17.113 -6.473  1.00 13.92 ?  148 ARG   B CZ   1 
ATOM   6324 N  NH1  . ARG   B 1 148 ? 27.147 -18.192 -5.709  1.00 14.00 ?  148 ARG   B NH1  1 
ATOM   6325 N  NH2  . ARG   B 1 148 ? 27.617 -15.964 -5.938  1.00 13.75 ?  148 ARG   B NH2  1 
ATOM   6326 H  H    . ARG   B 1 148 ? 30.890 -19.021 -8.108  1.00 15.19 ?  148 ARG   B H    1 
ATOM   6327 H  HA   . ARG   B 1 148 ? 29.755 -20.239 -10.244 1.00 15.58 ?  148 ARG   B HA   1 
ATOM   6328 H  HB2  . ARG   B 1 148 ? 29.065 -17.730 -9.139  1.00 16.17 ?  148 ARG   B HB2  1 
ATOM   6329 H  HB3  . ARG   B 1 148 ? 28.433 -18.297 -10.484 1.00 16.17 ?  148 ARG   B HB3  1 
ATOM   6330 H  HG2  . ARG   B 1 148 ? 27.409 -20.007 -9.324  1.00 17.50 ?  148 ARG   B HG2  1 
ATOM   6331 H  HG3  . ARG   B 1 148 ? 28.110 -19.546 -7.976  1.00 17.50 ?  148 ARG   B HG3  1 
ATOM   6332 H  HD2  . ARG   B 1 148 ? 26.090 -18.085 -9.314  1.00 18.10 ?  148 ARG   B HD2  1 
ATOM   6333 H  HD3  . ARG   B 1 148 ? 25.896 -18.855 -7.936  1.00 18.10 ?  148 ARG   B HD3  1 
ATOM   6334 H  HE   . ARG   B 1 148 ? 26.967 -16.424 -8.208  1.00 17.91 ?  148 ARG   B HE   1 
ATOM   6335 H  HH11 . ARG   B 1 148 ? 26.884 -18.944 -6.039  1.00 16.80 ?  148 ARG   B HH11 1 
ATOM   6336 H  HH12 . ARG   B 1 148 ? 27.341 -18.141 -4.871  1.00 16.80 ?  148 ARG   B HH12 1 
ATOM   6337 H  HH21 . ARG   B 1 148 ? 27.678 -15.260 -6.427  1.00 16.50 ?  148 ARG   B HH21 1 
ATOM   6338 H  HH22 . ARG   B 1 148 ? 27.819 -15.925 -5.103  1.00 16.50 ?  148 ARG   B HH22 1 
ATOM   6339 N  N    . THR   B 1 149 ? 32.110 -18.182 -10.319 1.00 12.93 ?  149 THR   B N    1 
ATOM   6340 C  CA   . THR   B 1 149 ? 33.152 -17.620 -11.163 1.00 12.97 ?  149 THR   B CA   1 
ATOM   6341 C  C    . THR   B 1 149 ? 34.039 -18.758 -11.672 1.00 12.45 ?  149 THR   B C    1 
ATOM   6342 O  O    . THR   B 1 149 ? 33.841 -19.926 -11.330 1.00 12.94 ?  149 THR   B O    1 
ATOM   6343 C  CB   . THR   B 1 149 ? 33.921 -16.567 -10.378 1.00 13.06 ?  149 THR   B CB   1 
ATOM   6344 O  OG1  . THR   B 1 149 ? 34.381 -17.162 -9.161  1.00 13.15 ?  149 THR   B OG1  1 
ATOM   6345 C  CG2  . THR   B 1 149 ? 33.028 -15.359 -10.085 1.00 13.91 ?  149 THR   B CG2  1 
ATOM   6346 H  H    . THR   B 1 149 ? 32.276 -18.118 -9.479  1.00 15.52 ?  149 THR   B H    1 
ATOM   6347 H  HA   . THR   B 1 149 ? 32.745 -17.186 -11.928 1.00 15.57 ?  149 THR   B HA   1 
ATOM   6348 H  HB   . THR   B 1 149 ? 34.684 -16.275 -10.890 1.00 15.68 ?  149 THR   B HB   1 
ATOM   6349 H  HG1  . THR   B 1 149 ? 34.793 -16.590 -8.694  1.00 15.79 ?  149 THR   B HG1  1 
ATOM   6350 H  HG21 . THR   B 1 149 ? 33.530 -14.687 -9.595  1.00 16.69 ?  149 THR   B HG21 1 
ATOM   6351 H  HG22 . THR   B 1 149 ? 32.716 -14.970 -10.918 1.00 16.69 ?  149 THR   B HG22 1 
ATOM   6352 H  HG23 . THR   B 1 149 ? 32.261 -15.627 -9.556  1.00 16.69 ?  149 THR   B HG23 1 
ATOM   6353 N  N    . ASN   B 1 150 ? 35.005 -18.436 -12.521 1.00 12.66 ?  150 ASN   B N    1 
ATOM   6354 C  CA   . ASN   B 1 150 ? 35.764 -19.464 -13.222 1.00 13.04 ?  150 ASN   B CA   1 
ATOM   6355 C  C    . ASN   B 1 150 ? 36.928 -19.915 -12.349 1.00 12.56 ?  150 ASN   B C    1 
ATOM   6356 O  O    . ASN   B 1 150 ? 37.861 -19.146 -12.097 1.00 13.16 ?  150 ASN   B O    1 
ATOM   6357 C  CB   . ASN   B 1 150 ? 36.237 -18.932 -14.566 1.00 14.72 ?  150 ASN   B CB   1 
ATOM   6358 C  CG   . ASN   B 1 150 ? 35.096 -18.713 -15.511 1.00 17.42 ?  150 ASN   B CG   1 
ATOM   6359 O  OD1  . ASN   B 1 150 ? 34.193 -19.536 -15.585 1.00 18.35 ?  150 ASN   B OD1  1 
ATOM   6360 N  ND2  . ASN   B 1 150 ? 35.100 -17.591 -16.209 1.00 19.38 ?  150 ASN   B ND2  1 
ATOM   6361 H  H    . ASN   B 1 150 ? 35.252 -17.630 -12.702 1.00 15.20 ?  150 ASN   B H    1 
ATOM   6362 H  HA   . ASN   B 1 150 ? 35.185 -20.230 -13.382 1.00 15.65 ?  150 ASN   B HA   1 
ATOM   6363 H  HB2  . ASN   B 1 150 ? 36.682 -18.081 -14.430 1.00 17.67 ?  150 ASN   B HB2  1 
ATOM   6364 H  HB3  . ASN   B 1 150 ? 36.841 -19.570 -14.967 1.00 17.67 ?  150 ASN   B HB3  1 
ATOM   6365 H  HD21 . ASN   B 1 150 ? 34.463 -17.420 -16.763 1.00 23.26 ?  150 ASN   B HD21 1 
ATOM   6366 H  HD22 . ASN   B 1 150 ? 35.751 -17.033 -16.124 1.00 23.26 ?  150 ASN   B HD22 1 
ATOM   6367 N  N    . VAL   B 1 151 ? 36.883 -21.161 -11.890 1.00 12.45 ?  151 VAL   B N    1 
ATOM   6368 C  CA   . VAL   B 1 151 ? 37.899 -21.690 -10.995 1.00 12.59 ?  151 VAL   B CA   1 
ATOM   6369 C  C    . VAL   B 1 151 ? 38.604 -22.859 -11.671 1.00 12.56 ?  151 VAL   B C    1 
ATOM   6370 O  O    . VAL   B 1 151 ? 37.961 -23.791 -12.177 1.00 13.36 ?  151 VAL   B O    1 
ATOM   6371 C  CB   . VAL   B 1 151 ? 37.334 -22.034 -9.602  1.00 13.68 ?  151 VAL   B CB   1 
ATOM   6372 C  CG1  . VAL   B 1 151 ? 36.174 -23.034 -9.690  1.00 14.61 ?  151 VAL   B CG1  1 
ATOM   6373 C  CG2  . VAL   B 1 151 ? 38.443 -22.523 -8.678  1.00 14.08 ?  151 VAL   B CG2  1 
ATOM   6374 H  H    . VAL   B 1 151 ? 36.259 -21.724 -12.087 1.00 14.95 ?  151 VAL   B H    1 
ATOM   6375 H  HA   . VAL   B 1 151 ? 38.563 -20.994 -10.857 1.00 15.11 ?  151 VAL   B HA   1 
ATOM   6376 H  HB   . VAL   B 1 151 ? 36.976 -21.223 -9.210  1.00 16.42 ?  151 VAL   B HB   1 
ATOM   6377 H  HG11 . VAL   B 1 151 ? 35.849 -23.227 -8.796  1.00 17.54 ?  151 VAL   B HG11 1 
ATOM   6378 H  HG12 . VAL   B 1 151 ? 35.459 -22.650 -10.224 1.00 17.54 ?  151 VAL   B HG12 1 
ATOM   6379 H  HG13 . VAL   B 1 151 ? 36.489 -23.854 -10.107 1.00 17.54 ?  151 VAL   B HG13 1 
ATOM   6380 H  HG21 . VAL   B 1 151 ? 38.085 -22.612 -7.778  1.00 16.90 ?  151 VAL   B HG21 1 
ATOM   6381 H  HG22 . VAL   B 1 151 ? 38.762 -23.384 -8.990  1.00 16.90 ?  151 VAL   B HG22 1 
ATOM   6382 H  HG23 . VAL   B 1 151 ? 39.165 -21.878 -8.682  1.00 16.90 ?  151 VAL   B HG23 1 
ATOM   6383 N  N    . TYR   B 1 152 ? 39.933 -22.774 -11.689 1.00 11.90 ?  152 TYR   B N    1 
ATOM   6384 C  CA   . TYR   B 1 152 ? 40.834 -23.755 -12.272 1.00 11.94 ?  152 TYR   B CA   1 
ATOM   6385 C  C    . TYR   B 1 152 ? 41.556 -24.432 -11.114 1.00 11.41 ?  152 TYR   B C    1 
ATOM   6386 O  O    . TYR   B 1 152 ? 42.404 -23.815 -10.462 1.00 11.90 ?  152 TYR   B O    1 
ATOM   6387 C  CB   . TYR   B 1 152 ? 41.804 -23.046 -13.217 1.00 12.70 ?  152 TYR   B CB   1 
ATOM   6388 C  CG   . TYR   B 1 152 ? 41.124 -22.584 -14.482 1.00 13.15 ?  152 TYR   B CG   1 
ATOM   6389 C  CD1  . TYR   B 1 152 ? 40.458 -21.361 -14.549 1.00 13.58 ?  152 TYR   B CD1  1 
ATOM   6390 C  CD2  . TYR   B 1 152 ? 41.115 -23.394 -15.603 1.00 14.38 ?  152 TYR   B CD2  1 
ATOM   6391 C  CE1  . TYR   B 1 152 ? 39.814 -20.962 -15.708 1.00 15.04 ?  152 TYR   B CE1  1 
ATOM   6392 C  CE2  . TYR   B 1 152 ? 40.475 -23.011 -16.758 1.00 15.28 ?  152 TYR   B CE2  1 
ATOM   6393 C  CZ   . TYR   B 1 152 ? 39.830 -21.790 -16.811 1.00 15.63 ?  152 TYR   B CZ   1 
ATOM   6394 O  OH   . TYR   B 1 152 ? 39.197 -21.420 -17.972 1.00 18.11 ?  152 TYR   B OH   1 
ATOM   6395 H  H    . TYR   B 1 152 ? 40.365 -22.107 -11.338 1.00 14.28 ?  152 TYR   B H    1 
ATOM   6396 H  HA   . TYR   B 1 152 ? 40.327 -24.419 -12.769 1.00 14.33 ?  152 TYR   B HA   1 
ATOM   6397 H  HB2  . TYR   B 1 152 ? 42.170 -22.267 -12.767 1.00 15.25 ?  152 TYR   B HB2  1 
ATOM   6398 H  HB3  . TYR   B 1 152 ? 42.518 -23.655 -13.459 1.00 15.25 ?  152 TYR   B HB3  1 
ATOM   6399 H  HD1  . TYR   B 1 152 ? 40.444 -20.802 -13.803 1.00 16.30 ?  152 TYR   B HD1  1 
ATOM   6400 H  HD2  . TYR   B 1 152 ? 41.545 -24.220 -15.572 1.00 17.26 ?  152 TYR   B HD2  1 
ATOM   6401 H  HE1  . TYR   B 1 152 ? 39.377 -20.143 -15.744 1.00 18.06 ?  152 TYR   B HE1  1 
ATOM   6402 H  HE2  . TYR   B 1 152 ? 40.486 -23.568 -17.504 1.00 18.35 ?  152 TYR   B HE2  1 
ATOM   6403 H  HH   . TYR   B 1 152 ? 39.293 -22.017 -18.555 1.00 21.74 ?  152 TYR   B HH   1 
ATOM   6404 N  N    . LEU   B 1 153 ? 41.190 -25.684 -10.839 1.00 11.69 ?  153 LEU   B N    1 
ATOM   6405 C  CA   . LEU   B 1 153 ? 41.698 -26.430 -9.697  1.00 11.19 ?  153 LEU   B CA   1 
ATOM   6406 C  C    . LEU   B 1 153 ? 42.931 -27.231 -10.092 1.00 11.98 ?  153 LEU   B C    1 
ATOM   6407 O  O    . LEU   B 1 153 ? 42.915 -27.961 -11.086 1.00 13.10 ?  153 LEU   B O    1 
ATOM   6408 C  CB   . LEU   B 1 153 ? 40.619 -27.390 -9.184  1.00 12.01 ?  153 LEU   B CB   1 
ATOM   6409 C  CG   . LEU   B 1 153 ? 39.357 -26.731 -8.624  1.00 12.91 ?  153 LEU   B CG   1 
ATOM   6410 C  CD1  . LEU   B 1 153 ? 38.251 -27.762 -8.473  1.00 13.72 ?  153 LEU   B CD1  1 
ATOM   6411 C  CD2  . LEU   B 1 153 ? 39.651 -26.062 -7.290  1.00 13.64 ?  153 LEU   B CD2  1 
ATOM   6412 H  H    . LEU   B 1 153 ? 40.618 -26.131 -11.310 1.00 14.03 ?  153 LEU   B H    1 
ATOM   6413 H  HA   . LEU   B 1 153 ? 41.928 -25.813 -8.988  1.00 13.44 ?  153 LEU   B HA   1 
ATOM   6414 H  HB2  . LEU   B 1 153 ? 40.346 -27.965 -9.912  1.00 14.41 ?  153 LEU   B HB2  1 
ATOM   6415 H  HB3  . LEU   B 1 153 ? 41.002 -27.926 -8.471  1.00 14.41 ?  153 LEU   B HB3  1 
ATOM   6416 H  HG   . LEU   B 1 153 ? 39.047 -26.042 -9.240  1.00 15.49 ?  153 LEU   B HG   1 
ATOM   6417 H  HD11 . LEU   B 1 153 ? 37.441 -27.309 -8.178  1.00 16.47 ?  153 LEU   B HD11 1 
ATOM   6418 H  HD12 . LEU   B 1 153 ? 38.100 -28.180 -9.331  1.00 16.47 ?  153 LEU   B HD12 1 
ATOM   6419 H  HD13 . LEU   B 1 153 ? 38.524 -28.414 -7.818  1.00 16.47 ?  153 LEU   B HD13 1 
ATOM   6420 H  HD21 . LEU   B 1 153 ? 38.831 -25.686 -6.932  1.00 16.38 ?  153 LEU   B HD21 1 
ATOM   6421 H  HD22 . LEU   B 1 153 ? 40.005 -26.726 -6.678  1.00 16.38 ?  153 LEU   B HD22 1 
ATOM   6422 H  HD23 . LEU   B 1 153 ? 40.304 -25.357 -7.426  1.00 16.38 ?  153 LEU   B HD23 1 
ATOM   6423 N  N    . ALA   B 1 154 ? 43.982 -27.121 -9.287  1.00 11.94 ?  154 ALA   B N    1 
ATOM   6424 C  CA   . ALA   B 1 154 ? 45.210 -27.880 -9.475  1.00 13.32 ?  154 ALA   B CA   1 
ATOM   6425 C  C    . ALA   B 1 154 ? 45.272 -28.956 -8.401  1.00 13.65 ?  154 ALA   B C    1 
ATOM   6426 O  O    . ALA   B 1 154 ? 45.188 -28.656 -7.202  1.00 14.88 ?  154 ALA   B O    1 
ATOM   6427 C  CB   . ALA   B 1 154 ? 46.433 -26.968 -9.409  1.00 14.07 ?  154 ALA   B CB   1 
ATOM   6428 H  H    . ALA   B 1 154 ? 44.005 -26.591 -8.605  1.00 14.33 ?  154 ALA   B H    1 
ATOM   6429 H  HA   . ALA   B 1 154 ? 45.197 -28.306 -10.341 1.00 15.99 ?  154 ALA   B HA   1 
ATOM   6430 H  HB1  . ALA   B 1 154 ? 47.236 -27.497 -9.536  1.00 16.88 ?  154 ALA   B HB1  1 
ATOM   6431 H  HB2  . ALA   B 1 154 ? 46.370 -26.295 -10.110 1.00 16.88 ?  154 ALA   B HB2  1 
ATOM   6432 H  HB3  . ALA   B 1 154 ? 46.463 -26.529 -8.542  1.00 16.88 ?  154 ALA   B HB3  1 
ATOM   6433 N  N    . VAL   B 1 155 ? 45.390 -30.204 -8.833  1.00 13.15 ?  155 VAL   B N    1 
ATOM   6434 C  CA   . VAL   B 1 155 ? 45.498 -31.350 -7.941  1.00 13.24 ?  155 VAL   B CA   1 
ATOM   6435 C  C    . VAL   B 1 155 ? 46.835 -32.024 -8.220  1.00 13.10 ?  155 VAL   B C    1 
ATOM   6436 O  O    . VAL   B 1 155 ? 47.072 -32.514 -9.332  1.00 15.06 ?  155 VAL   B O    1 
ATOM   6437 C  CB   . VAL   B 1 155 ? 44.340 -32.339 -8.138  1.00 14.67 ?  155 VAL   B CB   1 
ATOM   6438 C  CG1  . VAL   B 1 155 ? 44.523 -33.541 -7.227  1.00 14.66 ?  155 VAL   B CG1  1 
ATOM   6439 C  CG2  . VAL   B 1 155 ? 43.002 -31.645 -7.880  1.00 15.57 ?  155 VAL   B CG2  1 
ATOM   6440 H  H    . VAL   B 1 155 ? 45.420 -30.419 -9.668  1.00 15.78 ?  155 VAL   B H    1 
ATOM   6441 H  HA   . VAL   B 1 155 ? 45.489 -31.050 -7.020  1.00 15.90 ?  155 VAL   B HA   1 
ATOM   6442 H  HB   . VAL   B 1 155 ? 44.340 -32.650 -9.058  1.00 17.62 ?  155 VAL   B HB   1 
ATOM   6443 H  HG11 . VAL   B 1 155 ? 43.691 -34.040 -7.187  1.00 17.60 ?  155 VAL   B HG11 1 
ATOM   6444 H  HG12 . VAL   B 1 155 ? 45.227 -34.108 -7.584  1.00 17.60 ?  155 VAL   B HG12 1 
ATOM   6445 H  HG13 . VAL   B 1 155 ? 44.765 -33.234 -6.339  1.00 17.60 ?  155 VAL   B HG13 1 
ATOM   6446 H  HG21 . VAL   B 1 155 ? 42.286 -32.299 -7.969  1.00 18.68 ?  155 VAL   B HG21 1 
ATOM   6447 H  HG22 . VAL   B 1 155 ? 43.003 -31.279 -6.983  1.00 18.68 ?  155 VAL   B HG22 1 
ATOM   6448 H  HG23 . VAL   B 1 155 ? 42.879 -30.936 -8.530  1.00 18.68 ?  155 VAL   B HG23 1 
ATOM   6449 N  N    . PHE   B 1 156 ? 47.699 -32.066 -7.207  1.00 13.46 ?  156 PHE   B N    1 
ATOM   6450 C  CA   . PHE   B 1 156 ? 49.077 -32.517 -7.412  1.00 14.75 ?  156 PHE   B CA   1 
ATOM   6451 C  C    . PHE   B 1 156 ? 49.176 -34.016 -7.695  1.00 16.06 ?  156 PHE   B C    1 
ATOM   6452 O  O    . PHE   B 1 156 ? 49.903 -34.441 -8.603  1.00 17.81 ?  156 PHE   B O    1 
ATOM   6453 C  CB   . PHE   B 1 156 ? 49.906 -32.149 -6.185  1.00 14.95 ?  156 PHE   B CB   1 
ATOM   6454 C  CG   . PHE   B 1 156 ? 51.329 -32.613 -6.244  1.00 15.48 ?  156 PHE   B CG   1 
ATOM   6455 C  CD1  . PHE   B 1 156 ? 52.211 -32.070 -7.157  1.00 17.14 ?  156 PHE   B CD1  1 
ATOM   6456 C  CD2  . PHE   B 1 156 ? 51.787 -33.574 -5.367  1.00 15.70 ?  156 PHE   B CD2  1 
ATOM   6457 C  CE1  . PHE   B 1 156 ? 53.529 -32.481 -7.203  1.00 17.96 ?  156 PHE   B CE1  1 
ATOM   6458 C  CE2  . PHE   B 1 156 ? 53.105 -33.988 -5.406  1.00 17.27 ?  156 PHE   B CE2  1 
ATOM   6459 C  CZ   . PHE   B 1 156 ? 53.969 -33.447 -6.331  1.00 17.81 ?  156 PHE   B CZ   1 
ATOM   6460 H  H    . PHE   B 1 156 ? 47.513 -31.850 -6.397  1.00 16.16 ?  156 PHE   B H    1 
ATOM   6461 H  HA   . PHE   B 1 156 ? 49.445 -32.048 -8.173  1.00 17.71 ?  156 PHE   B HA   1 
ATOM   6462 H  HB2  . PHE   B 1 156 ? 49.916 -31.183 -6.100  1.00 17.95 ?  156 PHE   B HB2  1 
ATOM   6463 H  HB3  . PHE   B 1 156 ? 49.499 -32.545 -5.401  1.00 17.95 ?  156 PHE   B HB3  1 
ATOM   6464 H  HD1  . PHE   B 1 156 ? 51.917 -31.413 -7.748  1.00 20.58 ?  156 PHE   B HD1  1 
ATOM   6465 H  HD2  . PHE   B 1 156 ? 51.198 -33.947 -4.748  1.00 18.85 ?  156 PHE   B HD2  1 
ATOM   6466 H  HE1  . PHE   B 1 156 ? 54.117 -32.109 -7.825  1.00 21.56 ?  156 PHE   B HE1  1 
ATOM   6467 H  HE2  . PHE   B 1 156 ? 53.400 -34.649 -4.818  1.00 20.72 ?  156 PHE   B HE2  1 
ATOM   6468 H  HZ   . PHE   B 1 156 ? 54.857 -33.730 -6.358  1.00 21.37 ?  156 PHE   B HZ   1 
ATOM   6469 N  N    . ASP   B 1 157 ? 48.509 -34.836 -6.896  1.00 16.59 ?  157 ASP   B N    1 
ATOM   6470 C  CA   . ASP   B 1 157 ? 48.656 -36.283 -6.992  1.00 17.71 ?  157 ASP   B CA   1 
ATOM   6471 C  C    . ASP   B 1 157 ? 47.739 -36.827 -8.082  1.00 17.99 ?  157 ASP   B C    1 
ATOM   6472 O  O    . ASP   B 1 157 ? 46.513 -36.703 -7.983  1.00 17.13 ?  157 ASP   B O    1 
ATOM   6473 C  CB   . ASP   B 1 157 ? 48.295 -36.896 -5.646  1.00 19.12 ?  157 ASP   B CB   1 
ATOM   6474 C  CG   . ASP   B 1 157 ? 48.423 -38.409 -5.631  1.00 20.75 ?  157 ASP   B CG   1 
ATOM   6475 O  OD1  . ASP   B 1 157 ? 48.768 -39.016 -6.672  1.00 21.14 ?  157 ASP   B OD1  1 
ATOM   6476 O  OD2  . ASP   B 1 157 ? 48.188 -38.989 -4.554  1.00 22.42 -1 157 ASP   B OD2  1 
ATOM   6477 H  H    . ASP   B 1 157 ? 47.970 -34.581 -6.285  1.00 19.92 ?  157 ASP   B H    1 
ATOM   6478 H  HA   . ASP   B 1 157 ? 49.578 -36.515 -7.208  1.00 21.25 ?  157 ASP   B HA   1 
ATOM   6479 H  HB2  . ASP   B 1 157 ? 48.874 -36.521 -4.966  1.00 22.95 ?  157 ASP   B HB2  1 
ATOM   6480 H  HB3  . ASP   B 1 157 ? 47.370 -36.676 -5.445  1.00 22.95 ?  157 ASP   B HB3  1 
ATOM   6481 N  N    . LYS   B 1 158 ? 48.333 -37.446 -9.111  1.00 19.07 ?  158 LYS   B N    1 
ATOM   6482 C  CA   . LYS   B 1 158 ? 47.556 -38.057 -10.192 1.00 20.05 ?  158 LYS   B CA   1 
ATOM   6483 C  C    . LYS   B 1 158 ? 46.496 -39.020 -9.660  1.00 19.94 ?  158 LYS   B C    1 
ATOM   6484 O  O    . LYS   B 1 158 ? 45.390 -39.106 -10.209 1.00 20.11 ?  158 LYS   B O    1 
ATOM   6485 C  CB   . LYS   B 1 158 ? 48.504 -38.776 -11.162 1.00 21.67 ?  158 LYS   B CB   1 
ATOM   6486 C  CG   . LYS   B 1 158 ? 47.829 -39.682 -12.184 1.00 23.72 ?  158 LYS   B CG   1 
ATOM   6487 C  CD   . LYS   B 1 158 ? 46.959 -38.906 -13.154 1.00 25.57 ?  158 LYS   B CD   1 
ATOM   6488 C  CE   . LYS   B 1 158 ? 46.363 -39.826 -14.209 1.00 27.20 ?  158 LYS   B CE   1 
ATOM   6489 N  NZ   . LYS   B 1 158 ? 45.291 -39.154 -14.997 1.00 27.61 ?  158 LYS   B NZ   1 
ATOM   6490 H  H    . LYS   B 1 158 ? 49.189 -37.525 -9.207  1.00 22.89 ?  158 LYS   B H    1 
ATOM   6491 H  HA   . LYS   B 1 158 ? 47.108 -37.356 -10.694 1.00 24.06 ?  158 LYS   B HA   1 
ATOM   6492 H  HB2  . LYS   B 1 158 ? 49.009 -38.110 -11.661 1.00 26.01 ?  158 LYS   B HB2  1 
ATOM   6493 H  HB3  . LYS   B 1 158 ? 49.118 -39.324 -10.649 1.00 26.01 ?  158 LYS   B HB3  1 
ATOM   6494 H  HG2  . LYS   B 1 158 ? 48.514 -40.137 -12.701 1.00 28.46 ?  158 LYS   B HG2  1 
ATOM   6495 H  HG3  . LYS   B 1 158 ? 47.276 -40.341 -11.733 1.00 28.46 ?  158 LYS   B HG3  1 
ATOM   6496 H  HD2  . LYS   B 1 158 ? 46.232 -38.485 -12.669 1.00 30.69 ?  158 LYS   B HD2  1 
ATOM   6497 H  HD3  . LYS   B 1 158 ? 47.497 -38.236 -13.605 1.00 30.69 ?  158 LYS   B HD3  1 
ATOM   6498 H  HE2  . LYS   B 1 158 ? 47.059 -40.102 -14.822 1.00 32.64 ?  158 LYS   B HE2  1 
ATOM   6499 H  HE3  . LYS   B 1 158 ? 45.974 -40.601 -13.773 1.00 32.64 ?  158 LYS   B HE3  1 
ATOM   6500 H  HZ1  . LYS   B 1 158 ? 44.960 -39.714 -15.603 1.00 33.14 ?  158 LYS   B HZ1  1 
ATOM   6501 H  HZ2  . LYS   B 1 158 ? 44.633 -38.891 -14.457 1.00 33.14 ?  158 LYS   B HZ2  1 
ATOM   6502 H  HZ3  . LYS   B 1 158 ? 45.623 -38.439 -15.413 1.00 33.14 ?  158 LYS   B HZ3  1 
ATOM   6503 N  N    . ASN   B 1 159 ? 46.816 -39.773 -8.606  1.00 19.91 ?  159 ASN   B N    1 
ATOM   6504 C  CA   . ASN   B 1 159 ? 45.864 -40.757 -8.100  1.00 20.34 ?  159 ASN   B CA   1 
ATOM   6505 C  C    . ASN   B 1 159 ? 44.668 -40.089 -7.418  1.00 19.49 ?  159 ASN   B C    1 
ATOM   6506 O  O    . ASN   B 1 159 ? 43.535 -40.580 -7.519  1.00 19.75 ?  159 ASN   B O    1 
ATOM   6507 C  CB   . ASN   B 1 159 ? 46.572 -41.739 -7.171  1.00 21.79 ?  159 ASN   B CB   1 
ATOM   6508 C  CG   . ASN   B 1 159 ? 47.598 -42.583 -7.896  1.00 23.75 ?  159 ASN   B CG   1 
ATOM   6509 O  OD1  . ASN   B 1 159 ? 47.348 -43.080 -9.005  1.00 24.40 ?  159 ASN   B OD1  1 
ATOM   6510 N  ND2  . ASN   B 1 159 ? 48.763 -42.758 -7.275  1.00 24.53 ?  159 ASN   B ND2  1 
ATOM   6511 H  H    . ASN   B 1 159 ? 47.563 -39.726 -8.185  1.00 23.89 ?  159 ASN   B H    1 
ATOM   6512 H  HA   . ASN   B 1 159 ? 45.530 -41.262 -8.860  1.00 24.42 ?  159 ASN   B HA   1 
ATOM   6513 H  HB2  . ASN   B 1 159 ? 47.027 -41.244 -6.474  1.00 26.15 ?  159 ASN   B HB2  1 
ATOM   6514 H  HB3  . ASN   B 1 159 ? 45.917 -42.337 -6.793  1.00 26.15 ?  159 ASN   B HB3  1 
ATOM   6515 H  HD21 . ASN   B 1 159 ? 49.389 -43.230 -7.644  1.00 29.44 ?  159 ASN   B HD21 1 
ATOM   6516 H  HD22 . ASN   B 1 159 ? 48.898 -42.418 -6.496  1.00 29.44 ?  159 ASN   B HD22 1 
ATOM   6517 N  N    . LEU   B 1 160 ? 44.886 -38.961 -6.733  1.00 18.30 ?  160 LEU   B N    1 
ATOM   6518 C  CA   . LEU   B 1 160 ? 43.754 -38.224 -6.186  1.00 17.27 ?  160 LEU   B CA   1 
ATOM   6519 C  C    . LEU   B 1 160 ? 42.965 -37.556 -7.298  1.00 16.61 ?  160 LEU   B C    1 
ATOM   6520 O  O    . LEU   B 1 160 ? 41.730 -37.557 -7.276  1.00 16.54 ?  160 LEU   B O    1 
ATOM   6521 C  CB   . LEU   B 1 160 ? 44.222 -37.189 -5.165  1.00 17.00 ?  160 LEU   B CB   1 
ATOM   6522 C  CG   . LEU   B 1 160 ? 43.090 -36.296 -4.639  1.00 16.77 ?  160 LEU   B CG   1 
ATOM   6523 C  CD1  . LEU   B 1 160 ? 41.979 -37.144 -4.035  1.00 17.70 ?  160 LEU   B CD1  1 
ATOM   6524 C  CD2  . LEU   B 1 160 ? 43.617 -35.301 -3.623  1.00 17.04 ?  160 LEU   B CD2  1 
ATOM   6525 H  H    . LEU   B 1 160 ? 45.662 -38.617 -6.581  1.00 21.96 ?  160 LEU   B H    1 
ATOM   6526 H  HA   . LEU   B 1 160 ? 43.169 -38.854 -5.740  1.00 20.73 ?  160 LEU   B HA   1 
ATOM   6527 H  HB2  . LEU   B 1 160 ? 44.619 -37.658 -4.412  1.00 20.41 ?  160 LEU   B HB2  1 
ATOM   6528 H  HB3  . LEU   B 1 160 ? 44.890 -36.621 -5.584  1.00 20.41 ?  160 LEU   B HB3  1 
ATOM   6529 H  HG   . LEU   B 1 160 ? 42.717 -35.798 -5.379  1.00 20.13 ?  160 LEU   B HG   1 
ATOM   6530 H  HD11 . LEU   B 1 160 ? 41.362 -36.564 -3.569  1.00 21.24 ?  160 LEU   B HD11 1 
ATOM   6531 H  HD12 . LEU   B 1 160 ? 41.516 -37.621 -4.744  1.00 21.24 ?  160 LEU   B HD12 1 
ATOM   6532 H  HD13 . LEU   B 1 160 ? 42.368 -37.783 -3.412  1.00 21.24 ?  160 LEU   B HD13 1 
ATOM   6533 H  HD21 . LEU   B 1 160 ? 42.883 -34.739 -3.334  1.00 20.45 ?  160 LEU   B HD21 1 
ATOM   6534 H  HD22 . LEU   B 1 160 ? 43.983 -35.785 -2.868  1.00 20.45 ?  160 LEU   B HD22 1 
ATOM   6535 H  HD23 . LEU   B 1 160 ? 44.306 -34.762 -4.040  1.00 20.45 ?  160 LEU   B HD23 1 
ATOM   6536 N  N    . TYR   B 1 161 ? 43.662 -36.978 -8.279  1.00 17.04 ?  161 TYR   B N    1 
ATOM   6537 C  CA   . TYR   B 1 161 ? 42.994 -36.418 -9.448  1.00 16.95 ?  161 TYR   B CA   1 
ATOM   6538 C  C    . TYR   B 1 161 ? 42.049 -37.440 -10.067 1.00 16.97 ?  161 TYR   B C    1 
ATOM   6539 O  O    . TYR   B 1 161 ? 40.877 -37.146 -10.327 1.00 16.67 ?  161 TYR   B O    1 
ATOM   6540 C  CB   . TYR   B 1 161 ? 44.038 -35.950 -10.470 1.00 17.62 ?  161 TYR   B CB   1 
ATOM   6541 C  CG   . TYR   B 1 161 ? 43.456 -35.477 -11.785 1.00 18.07 ?  161 TYR   B CG   1 
ATOM   6542 C  CD1  . TYR   B 1 161 ? 43.068 -34.153 -11.955 1.00 18.14 ?  161 TYR   B CD1  1 
ATOM   6543 C  CD2  . TYR   B 1 161 ? 43.280 -36.355 -12.852 1.00 18.42 ?  161 TYR   B CD2  1 
ATOM   6544 C  CE1  . TYR   B 1 161 ? 42.535 -33.717 -13.141 1.00 19.17 ?  161 TYR   B CE1  1 
ATOM   6545 C  CE2  . TYR   B 1 161 ? 42.738 -35.925 -14.044 1.00 19.81 ?  161 TYR   B CE2  1 
ATOM   6546 C  CZ   . TYR   B 1 161 ? 42.369 -34.604 -14.184 1.00 19.89 ?  161 TYR   B CZ   1 
ATOM   6547 O  OH   . TYR   B 1 161 ? 41.828 -34.163 -15.368 1.00 21.73 ?  161 TYR   B OH   1 
ATOM   6548 H  H    . TYR   B 1 161 ? 44.518 -36.909 -8.296  1.00 20.45 ?  161 TYR   B H    1 
ATOM   6549 H  HA   . TYR   B 1 161 ? 42.472 -35.647 -9.179  1.00 20.35 ?  161 TYR   B HA   1 
ATOM   6550 H  HB2  . TYR   B 1 161 ? 44.540 -35.210 -10.092 1.00 21.15 ?  161 TYR   B HB2  1 
ATOM   6551 H  HB3  . TYR   B 1 161 ? 44.641 -36.685 -10.665 1.00 21.15 ?  161 TYR   B HB3  1 
ATOM   6552 H  HD1  . TYR   B 1 161 ? 43.181 -33.548 -11.258 1.00 21.78 ?  161 TYR   B HD1  1 
ATOM   6553 H  HD2  . TYR   B 1 161 ? 43.524 -37.249 -12.762 1.00 22.11 ?  161 TYR   B HD2  1 
ATOM   6554 H  HE1  . TYR   B 1 161 ? 42.286 -32.824 -13.238 1.00 23.01 ?  161 TYR   B HE1  1 
ATOM   6555 H  HE2  . TYR   B 1 161 ? 42.624 -36.520 -14.752 1.00 23.77 ?  161 TYR   B HE2  1 
ATOM   6556 H  HH   . TYR   B 1 161 ? 41.782 -34.798 -15.917 1.00 26.09 ?  161 TYR   B HH   1 
ATOM   6557 N  N    . ASP   B 1 162 ? 42.540 -38.660 -10.289 1.00 17.22 ?  162 ASP   B N    1 
ATOM   6558 C  CA   . ASP   B 1 162 ? 41.706 -39.690 -10.900 1.00 17.79 ?  162 ASP   B CA   1 
ATOM   6559 C  C    . ASP   B 1 162 ? 40.505 -40.027 -10.024 1.00 17.20 ?  162 ASP   B C    1 
ATOM   6560 O  O    . ASP   B 1 162 ? 39.398 -40.238 -10.533 1.00 17.51 ?  162 ASP   B O    1 
ATOM   6561 C  CB   . ASP   B 1 162 ? 42.533 -40.950 -11.160 1.00 19.22 ?  162 ASP   B CB   1 
ATOM   6562 C  CG   . ASP   B 1 162 ? 43.533 -40.785 -12.290 1.00 20.58 ?  162 ASP   B CG   1 
ATOM   6563 O  OD1  . ASP   B 1 162 ? 43.399 -39.838 -13.089 1.00 20.97 ?  162 ASP   B OD1  1 
ATOM   6564 O  OD2  . ASP   B 1 162 ? 44.442 -41.635 -12.395 1.00 22.06 -1 162 ASP   B OD2  1 
ATOM   6565 H  H    . ASP   B 1 162 ? 43.339 -38.909 -10.099 1.00 20.66 ?  162 ASP   B H    1 
ATOM   6566 H  HA   . ASP   B 1 162 ? 41.375 -39.369 -11.750 1.00 21.36 ?  162 ASP   B HA   1 
ATOM   6567 H  HB2  . ASP   B 1 162 ? 43.034 -41.176 -10.363 1.00 23.07 ?  162 ASP   B HB2  1 
ATOM   6568 H  HB3  . ASP   B 1 162 ? 41.938 -41.678 -11.398 1.00 23.07 ?  162 ASP   B HB3  1 
ATOM   6569 N  N    . LYS   B 1 163 ? 40.703 -40.109 -8.707  1.00 16.62 ?  163 LYS   B N    1 
ATOM   6570 C  CA   . LYS   B 1 163 ? 39.578 -40.379 -7.818  1.00 17.31 ?  163 LYS   B CA   1 
ATOM   6571 C  C    . LYS   B 1 163 ? 38.538 -39.268 -7.888  1.00 16.10 ?  163 LYS   B C    1 
ATOM   6572 O  O    . LYS   B 1 163 ? 37.328 -39.537 -7.888  1.00 16.94 ?  163 LYS   B O    1 
ATOM   6573 C  CB   . LYS   B 1 163 ? 40.062 -40.561 -6.382  1.00 20.26 ?  163 LYS   B CB   1 
ATOM   6574 C  CG   . LYS   B 1 163 ? 38.978 -41.077 -5.463  1.00 25.76 ?  163 LYS   B CG   1 
ATOM   6575 C  CD   . LYS   B 1 163 ? 39.441 -41.216 -4.027  1.00 30.54 ?  163 LYS   B CD   1 
ATOM   6576 C  CE   . LYS   B 1 163 ? 38.363 -41.895 -3.194  1.00 34.06 ?  163 LYS   B CE   1 
ATOM   6577 N  NZ   . LYS   B 1 163 ? 38.455 -41.559 -1.747  1.00 36.48 ?  163 LYS   B NZ   1 
ATOM   6578 H  H    . LYS   B 1 163 ? 41.464 -40.011 -8.314  1.00 19.95 ?  163 LYS   B H    1 
ATOM   6579 H  HA   . LYS   B 1 163 ? 39.153 -41.203 -8.096  1.00 20.78 ?  163 LYS   B HA   1 
ATOM   6580 H  HB2  . LYS   B 1 163 ? 40.793 -41.200 -6.376  1.00 24.31 ?  163 LYS   B HB2  1 
ATOM   6581 H  HB3  . LYS   B 1 163 ? 40.365 -39.707 -6.040  1.00 24.31 ?  163 LYS   B HB3  1 
ATOM   6582 H  HG2  . LYS   B 1 163 ? 38.229 -40.464 -5.477  1.00 30.91 ?  163 LYS   B HG2  1 
ATOM   6583 H  HG3  . LYS   B 1 163 ? 38.694 -41.955 -5.772  1.00 30.91 ?  163 LYS   B HG3  1 
ATOM   6584 H  HD2  . LYS   B 1 163 ? 40.244 -41.762 -3.996  1.00 36.66 ?  163 LYS   B HD2  1 
ATOM   6585 H  HD3  . LYS   B 1 163 ? 39.613 -40.338 -3.656  1.00 36.66 ?  163 LYS   B HD3  1 
ATOM   6586 H  HE2  . LYS   B 1 163 ? 37.490 -41.625 -3.518  1.00 40.87 ?  163 LYS   B HE2  1 
ATOM   6587 H  HE3  . LYS   B 1 163 ? 38.460 -42.855 -3.283  1.00 40.87 ?  163 LYS   B HE3  1 
ATOM   6588 H  HZ1  . LYS   B 1 163 ? 37.807 -41.973 -1.298  1.00 43.79 ?  163 LYS   B HZ1  1 
ATOM   6589 H  HZ2  . LYS   B 1 163 ? 39.242 -41.818 -1.426  1.00 43.79 ?  163 LYS   B HZ2  1 
ATOM   6590 H  HZ3  . LYS   B 1 163 ? 38.369 -40.681 -1.633  1.00 43.79 ?  163 LYS   B HZ3  1 
ATOM   6591 N  N    . LEU   B 1 164 ? 38.994 -38.014 -7.944  1.00 14.89 ?  164 LEU   B N    1 
ATOM   6592 C  CA   . LEU   B 1 164 ? 38.082 -36.876 -7.998  1.00 14.67 ?  164 LEU   B CA   1 
ATOM   6593 C  C    . LEU   B 1 164 ? 37.298 -36.858 -9.304  1.00 14.85 ?  164 LEU   B C    1 
ATOM   6594 O  O    . LEU   B 1 164 ? 36.075 -36.662 -9.306  1.00 16.02 ?  164 LEU   B O    1 
ATOM   6595 C  CB   . LEU   B 1 164 ? 38.883 -35.584 -7.841  1.00 14.12 ?  164 LEU   B CB   1 
ATOM   6596 C  CG   . LEU   B 1 164 ? 39.407 -35.299 -6.437  1.00 15.06 ?  164 LEU   B CG   1 
ATOM   6597 C  CD1  . LEU   B 1 164 ? 40.485 -34.229 -6.485  1.00 15.14 ?  164 LEU   B CD1  1 
ATOM   6598 C  CD2  . LEU   B 1 164 ? 38.287 -34.870 -5.512  1.00 16.68 ?  164 LEU   B CD2  1 
ATOM   6599 H  H    . LEU   B 1 164 ? 39.831 -37.798 -7.954  1.00 17.87 ?  164 LEU   B H    1 
ATOM   6600 H  HA   . LEU   B 1 164 ? 37.454 -36.936 -7.271  1.00 17.60 ?  164 LEU   B HA   1 
ATOM   6601 H  HB2  . LEU   B 1 164 ? 39.654 -35.624 -8.434  1.00 16.95 ?  164 LEU   B HB2  1 
ATOM   6602 H  HB3  . LEU   B 1 164 ? 38.321 -34.840 -8.097  1.00 16.95 ?  164 LEU   B HB3  1 
ATOM   6603 H  HG   . LEU   B 1 164 ? 39.811 -36.101 -6.077  1.00 18.08 ?  164 LEU   B HG   1 
ATOM   6604 H  HD11 . LEU   B 1 164 ? 40.801 -34.051 -5.582  1.00 18.18 ?  164 LEU   B HD11 1 
ATOM   6605 H  HD12 . LEU   B 1 164 ? 41.225 -34.540 -7.033  1.00 18.18 ?  164 LEU   B HD12 1 
ATOM   6606 H  HD13 . LEU   B 1 164 ? 40.115 -33.415 -6.866  1.00 18.18 ?  164 LEU   B HD13 1 
ATOM   6607 H  HD21 . LEU   B 1 164 ? 38.658 -34.628 -4.651  1.00 20.02 ?  164 LEU   B HD21 1 
ATOM   6608 H  HD22 . LEU   B 1 164 ? 37.827 -34.110 -5.901  1.00 20.02 ?  164 LEU   B HD22 1 
ATOM   6609 H  HD23 . LEU   B 1 164 ? 37.667 -35.612 -5.409  1.00 20.02 ?  164 LEU   B HD23 1 
ATOM   6610 N  N    . VAL   B 1 165 ? 37.988 -37.039 -10.431 1.00 16.51 ?  165 VAL   B N    1 
ATOM   6611 C  CA   . VAL   B 1 165 ? 37.332 -36.974 -11.731 1.00 17.92 ?  165 VAL   B CA   1 
ATOM   6612 C  C    . VAL   B 1 165 ? 36.408 -38.169 -11.913 1.00 19.70 ?  165 VAL   B C    1 
ATOM   6613 O  O    . VAL   B 1 165 ? 35.250 -38.026 -12.321 1.00 20.88 ?  165 VAL   B O    1 
ATOM   6614 C  CB   . VAL   B 1 165 ? 38.378 -36.896 -12.859 1.00 18.81 ?  165 VAL   B CB   1 
ATOM   6615 C  CG1  . VAL   B 1 165 ? 37.711 -37.016 -14.210 1.00 20.04 ?  165 VAL   B CG1  1 
ATOM   6616 C  CG2  . VAL   B 1 165 ? 39.161 -35.602 -12.772 1.00 18.50 ?  165 VAL   B CG2  1 
ATOM   6617 H  H    . VAL   B 1 165 ? 38.837 -37.197 -10.471 1.00 19.82 ?  165 VAL   B H    1 
ATOM   6618 H  HA   . VAL   B 1 165 ? 36.792 -36.174 -11.776 1.00 21.51 ?  165 VAL   B HA   1 
ATOM   6619 H  HB   . VAL   B 1 165 ? 39.007 -37.629 -12.766 1.00 22.58 ?  165 VAL   B HB   1 
ATOM   6620 H  HG11 . VAL   B 1 165 ? 38.322 -36.709 -14.894 1.00 24.06 ?  165 VAL   B HG11 1 
ATOM   6621 H  HG12 . VAL   B 1 165 ? 37.489 -37.949 -14.367 1.00 24.06 ?  165 VAL   B HG12 1 
ATOM   6622 H  HG13 . VAL   B 1 165 ? 36.906 -36.480 -14.214 1.00 24.06 ?  165 VAL   B HG13 1 
ATOM   6623 H  HG21 . VAL   B 1 165 ? 39.799 -35.564 -13.504 1.00 22.20 ?  165 VAL   B HG21 1 
ATOM   6624 H  HG22 . VAL   B 1 165 ? 38.545 -34.854 -12.835 1.00 22.20 ?  165 VAL   B HG22 1 
ATOM   6625 H  HG23 . VAL   B 1 165 ? 39.632 -35.570 -11.925 1.00 22.20 ?  165 VAL   B HG23 1 
ATOM   6626 N  N    . SER   B 1 166 ? 36.916 -39.370 -11.613 1.00 20.36 ?  166 SER   B N    1 
ATOM   6627 C  CA   . SER   B 1 166 ? 36.163 -40.583 -11.900 1.00 21.40 ?  166 SER   B CA   1 
ATOM   6628 C  C    . SER   B 1 166 ? 34.907 -40.673 -11.053 1.00 21.61 ?  166 SER   B C    1 
ATOM   6629 O  O    . SER   B 1 166 ? 33.940 -41.302 -11.476 1.00 22.85 ?  166 SER   B O    1 
ATOM   6630 C  CB   . SER   B 1 166 ? 37.028 -41.837 -11.718 1.00 22.30 ?  166 SER   B CB   1 
ATOM   6631 O  OG   . SER   B 1 166 ? 37.387 -42.037 -10.361 1.00 22.30 ?  166 SER   B OG   1 
ATOM   6632 H  H    . SER   B 1 166 ? 37.687 -39.507 -11.249 1.00 24.44 ?  166 SER   B H    1 
ATOM   6633 H  HA   . SER   B 1 166 ? 35.889 -40.562 -12.829 1.00 25.69 ?  166 SER   B HA   1 
ATOM   6634 H  HB2  . SER   B 1 166 ? 36.527 -42.612 -12.024 1.00 26.77 ?  166 SER   B HB2  1 
ATOM   6635 H  HB3  . SER   B 1 166 ? 37.835 -41.742 -12.249 1.00 26.77 ?  166 SER   B HB3  1 
ATOM   6636 H  HG   . SER   B 1 166 ? 37.834 -41.379 -10.086 1.00 26.76 ?  166 SER   B HG   1 
ATOM   6637 N  N    . SER   B 1 167 ? 34.887 -40.060 -9.873  1.00 20.29 ?  167 SER   B N    1 
ATOM   6638 C  CA   . SER   B 1 167 ? 33.732 -40.115 -8.984  1.00 19.49 ?  167 SER   B CA   1 
ATOM   6639 C  C    . SER   B 1 167 ? 32.817 -38.895 -9.084  1.00 19.07 ?  167 SER   B C    1 
ATOM   6640 O  O    . SER   B 1 167 ? 31.736 -38.899 -8.484  1.00 19.50 ?  167 SER   B O    1 
ATOM   6641 C  CB   . SER   B 1 167 ? 34.184 -40.298 -7.527  1.00 19.49 ?  167 SER   B CB   1 
ATOM   6642 O  OG   . SER   B 1 167 ? 34.849 -39.135 -7.051  1.00 19.33 ?  167 SER   B OG   1 
ATOM   6643 H  H    . SER   B 1 167 ? 35.538 -39.606 -9.564  1.00 24.35 ?  167 SER   B H    1 
ATOM   6644 H  HA   . SER   B 1 167 ? 33.198 -40.894 -9.222  1.00 23.39 ?  167 SER   B HA   1 
ATOM   6645 H  HB2  . SER   B 1 167 ? 33.401 -40.472 -6.977  1.00 23.40 ?  167 SER   B HB2  1 
ATOM   6646 H  HB3  . SER   B 1 167 ? 34.787 -41.062 -7.483  1.00 23.40 ?  167 SER   B HB3  1 
ATOM   6647 H  HG   . SER   B 1 167 ? 35.527 -38.991 -7.520  1.00 23.20 ?  167 SER   B HG   1 
ATOM   6648 N  N    . PHE   B 1 168 ? 33.197 -37.860 -9.834  1.00 18.66 ?  168 PHE   B N    1 
ATOM   6649 C  CA   . PHE   B 1 168 ? 32.363 -36.659 -9.898  1.00 18.38 ?  168 PHE   B CA   1 
ATOM   6650 C  C    . PHE   B 1 168 ? 31.051 -36.921 -10.633 1.00 16.31 ?  168 PHE   B C    1 
ATOM   6651 O  O    . PHE   B 1 168 ? 30.009 -36.325 -10.299 1.00 16.59 ?  168 PHE   B O    1 
ATOM   6652 C  CB   . PHE   B 1 168 ? 33.126 -35.522 -10.572 1.00 19.12 ?  168 PHE   B CB   1 
ATOM   6653 C  CG   . PHE   B 1 168 ? 32.321 -34.271 -10.713 1.00 19.10 ?  168 PHE   B CG   1 
ATOM   6654 C  CD1  . PHE   B 1 168 ? 31.979 -33.529 -9.593  1.00 20.20 ?  168 PHE   B CD1  1 
ATOM   6655 C  CD2  . PHE   B 1 168 ? 31.880 -33.850 -11.952 1.00 18.57 ?  168 PHE   B CD2  1 
ATOM   6656 C  CE1  . PHE   B 1 168 ? 31.218 -32.382 -9.706  1.00 20.53 ?  168 PHE   B CE1  1 
ATOM   6657 C  CE2  . PHE   B 1 168 ? 31.134 -32.687 -12.077 1.00 19.45 ?  168 PHE   B CE2  1 
ATOM   6658 C  CZ   . PHE   B 1 168 ? 30.794 -31.957 -10.950 1.00 19.79 ?  168 PHE   B CZ   1 
ATOM   6659 H  H    . PHE   B 1 168 ? 33.913 -37.830 -10.304 1.00 22.39 ?  168 PHE   B H    1 
ATOM   6660 H  HA   . PHE   B 1 168 ? 32.141 -36.381 -8.999  1.00 22.06 ?  168 PHE   B HA   1 
ATOM   6661 H  HB2  . PHE   B 1 168 ? 33.907 -35.311 -10.039 1.00 22.94 ?  168 PHE   B HB2  1 
ATOM   6662 H  HB3  . PHE   B 1 168 ? 33.394 -35.801 -11.460 1.00 22.94 ?  168 PHE   B HB3  1 
ATOM   6663 H  HD1  . PHE   B 1 168 ? 32.258 -33.814 -8.753  1.00 24.25 ?  168 PHE   B HD1  1 
ATOM   6664 H  HD2  . PHE   B 1 168 ? 32.106 -34.331 -12.711 1.00 22.29 ?  168 PHE   B HD2  1 
ATOM   6665 H  HE1  . PHE   B 1 168 ? 30.996 -31.893 -8.948  1.00 24.64 ?  168 PHE   B HE1  1 
ATOM   6666 H  HE2  . PHE   B 1 168 ? 30.843 -32.407 -12.919 1.00 23.34 ?  168 PHE   B HE2  1 
ATOM   6667 H  HZ   . PHE   B 1 168 ? 30.284 -31.181 -11.035 1.00 23.76 ?  168 PHE   B HZ   1 
ATOM   6668 N  N    . LEU   B 1 169 ? 31.087 -37.803 -11.629 1.00 16.35 ?  169 LEU   B N    1 
ATOM   6669 C  CA   . LEU   B 1 169 ? 29.913 -38.115 -12.432 1.00 18.55 ?  169 LEU   B CA   1 
ATOM   6670 C  C    . LEU   B 1 169 ? 29.902 -39.552 -12.930 1.00 21.10 ?  169 LEU   B C    1 
ATOM   6671 O  O    . LEU   B 1 169 ? 28.986 -39.960 -13.646 1.00 23.41 ?  169 LEU   B O    1 
ATOM   6672 C  CB   . LEU   B 1 169 ? 29.845 -37.179 -13.635 1.00 20.46 ?  169 LEU   B CB   1 
ATOM   6673 C  CG   . LEU   B 1 169 ? 28.588 -36.317 -13.732 1.00 23.00 ?  169 LEU   B CG   1 
ATOM   6674 C  CD1  . LEU   B 1 169 ? 28.531 -35.656 -15.093 1.00 23.88 ?  169 LEU   B CD1  1 
ATOM   6675 C  CD2  . LEU   B 1 169 ? 27.330 -37.129 -13.472 1.00 22.71 ?  169 LEU   B CD2  1 
ATOM   6676 O  OXT  . LEU   B 1 169 ? 30.811 -40.321 -12.640 1.00 21.97 -1 169 LEU   B OXT  1 
ATOM   6677 H  H    . LEU   B 1 169 ? 31.792 -38.234 -11.870 1.00 19.63 ?  169 LEU   B H    1 
ATOM   6678 H  HA   . LEU   B 1 169 ? 29.127 -37.978 -11.887 1.00 22.26 ?  169 LEU   B HA   1 
ATOM   6679 H  HB2  . LEU   B 1 169 ? 30.604 -36.577 -13.606 1.00 24.55 ?  169 LEU   B HB2  1 
ATOM   6680 H  HB3  . LEU   B 1 169 ? 29.887 -37.711 -14.446 1.00 24.55 ?  169 LEU   B HB3  1 
ATOM   6681 H  HG   . LEU   B 1 169 ? 28.634 -35.614 -13.064 1.00 27.61 ?  169 LEU   B HG   1 
ATOM   6682 H  HD11 . LEU   B 1 169 ? 27.746 -35.089 -15.135 1.00 28.66 ?  169 LEU   B HD11 1 
ATOM   6683 H  HD12 . LEU   B 1 169 ? 29.332 -35.125 -15.217 1.00 28.66 ?  169 LEU   B HD12 1 
ATOM   6684 H  HD13 . LEU   B 1 169 ? 28.481 -36.345 -15.773 1.00 28.66 ?  169 LEU   B HD13 1 
ATOM   6685 H  HD21 . LEU   B 1 169 ? 26.579 -36.704 -13.911 1.00 27.26 ?  169 LEU   B HD21 1 
ATOM   6686 H  HD22 . LEU   B 1 169 ? 27.456 -38.026 -13.826 1.00 27.26 ?  169 LEU   B HD22 1 
ATOM   6687 H  HD23 . LEU   B 1 169 ? 27.176 -37.172 -12.516 1.00 27.26 ?  169 LEU   B HD23 1 
HETATM 6688 C  C1   T TFA   C 2 .   ? 12.124 -1.257  1.457   0.30 11.41 ?  201 TFA   A C1   1 
HETATM 6689 C  C2   T TFA   C 2 .   ? 12.721 -1.710  0.101   0.30 13.49 ?  201 TFA   A C2   1 
HETATM 6690 O  O    T TFA   C 2 .   ? 12.824 -1.551  2.430   0.30 10.21 ?  201 TFA   A O    1 
HETATM 6691 F  F1   T TFA   C 2 .   ? 12.756 -3.053  0.054   0.30 14.77 ?  201 TFA   A F1   1 
HETATM 6692 F  F2   T TFA   C 2 .   ? 12.014 -1.319  -0.971  0.30 13.85 ?  201 TFA   A F2   1 
HETATM 6693 F  F3   T TFA   C 2 .   ? 13.960 -1.256  -0.102  0.30 14.60 ?  201 TFA   A F3   1 
HETATM 6694 O  OXT  T TFA   C 2 .   ? 11.043 -0.671  1.391   0.30 11.59 ?  201 TFA   A OXT  1 
HETATM 6695 N  N2   B A1A9W D 3 .   ? 15.020 -0.452  3.753   0.32 12.97 ?  202 A1A9W A N2   1 
HETATM 6696 C  C3   B A1A9W D 3 .   ? 15.229 0.632   2.932   0.32 12.84 ?  202 A1A9W A C3   1 
HETATM 6697 C  C6   B A1A9W D 3 .   ? 15.438 1.913   3.559   0.32 12.47 ?  202 A1A9W A C6   1 
HETATM 6698 C  C9   B A1A9W D 3 .   ? 13.413 -0.791  0.229   0.32 15.58 ?  202 A1A9W A C9   1 
HETATM 6699 C  C12  B A1A9W D 3 .   ? 12.407 -0.248  1.274   0.32 16.57 ?  202 A1A9W A C12  1 
HETATM 6700 C  C1   B A1A9W D 3 .   ? 15.923 -1.099  -0.317  0.32 13.17 ?  202 A1A9W A C1   1 
HETATM 6701 C  C10  B A1A9W D 3 .   ? 12.909 -2.223  -0.069  0.32 16.45 ?  202 A1A9W A C10  1 
HETATM 6702 C  C11  B A1A9W D 3 .   ? 11.704 -2.451  0.860   0.32 17.23 ?  202 A1A9W A C11  1 
HETATM 6703 C  C2   B A1A9W D 3 .   ? 14.891 -0.802  0.833   0.32 13.71 ?  202 A1A9W A C2   1 
HETATM 6704 C  C4   B A1A9W D 3 .   ? 15.029 -0.301  5.124   0.32 12.77 ?  202 A1A9W A C4   1 
HETATM 6705 C  C5   B A1A9W D 3 .   ? 15.424 1.914   5.009   0.32 12.12 ?  202 A1A9W A C5   1 
HETATM 6706 C  C7   B A1A9W D 3 .   ? 15.696 3.304   3.193   0.32 12.38 ?  202 A1A9W A C7   1 
HETATM 6707 C  C8   B A1A9W D 3 .   ? 15.813 4.041   4.364   0.32 12.00 ?  202 A1A9W A C8   1 
HETATM 6708 N  N1   B A1A9W D 3 .   ? 15.208 0.471   1.525   0.32 13.23 ?  202 A1A9W A N1   1 
HETATM 6709 N  N3   B A1A9W D 3 .   ? 15.222 0.826   5.807   0.32 12.45 ?  202 A1A9W A N3   1 
HETATM 6710 N  N4   B A1A9W D 3 .   ? 15.654 3.199   5.412   0.32 11.59 ?  202 A1A9W A N4   1 
HETATM 6711 O  O1   B A1A9W D 3 .   ? 17.072 -1.664  0.264   0.32 12.12 ?  202 A1A9W A O1   1 
HETATM 6712 O  O2   B A1A9W D 3 .   ? 11.565 -1.314  1.683   0.32 17.27 ?  202 A1A9W A O2   1 
HETATM 6713 H  H2   B A1A9W D 3 .   ? 13.345 -0.172  -0.706  0.32 18.70 ?  202 A1A9W A H2   1 
HETATM 6714 H  H16  B A1A9W D 3 .   ? 11.804 0.602   0.868   0.32 19.89 ?  202 A1A9W A H16  1 
HETATM 6715 H  H15  B A1A9W D 3 .   ? 12.908 0.213   2.146   0.32 19.89 ?  202 A1A9W A H15  1 
HETATM 6716 H  H5   B A1A9W D 3 .   ? 15.464 -1.783  -1.074  0.32 15.81 ?  202 A1A9W A H5   1 
HETATM 6717 H  H4   B A1A9W D 3 .   ? 16.174 -0.150  -0.840  0.32 15.81 ?  202 A1A9W A H4   1 
HETATM 6718 H  H11  B A1A9W D 3 .   ? 13.701 -3.003  0.085   0.32 19.75 ?  202 A1A9W A H11  1 
HETATM 6719 H  H12  B A1A9W D 3 .   ? 12.633 -2.338  -1.136  0.32 19.75 ?  202 A1A9W A H12  1 
HETATM 6720 H  H14  B A1A9W D 3 .   ? 11.810 -3.403  1.469   0.32 20.68 ?  202 A1A9W A H14  1 
HETATM 6721 H  H13  B A1A9W D 3 .   ? 10.753 -2.620  0.303   0.32 20.68 ?  202 A1A9W A H13  1 
HETATM 6722 H  H1   B A1A9W D 3 .   ? 14.928 -1.641  1.569   0.32 16.46 ?  202 A1A9W A H1   1 
HETATM 6723 H  H7   B A1A9W D 3 .   ? 14.855 -1.190  5.745   0.32 15.33 ?  202 A1A9W A H7   1 
HETATM 6724 H  H8   B A1A9W D 3 .   ? 15.787 3.784   2.225   0.32 14.86 ?  202 A1A9W A H8   1 
HETATM 6725 H  H9   B A1A9W D 3 .   ? 16.002 5.090   4.608   0.32 14.41 ?  202 A1A9W A H9   1 
HETATM 6726 H  H6   B A1A9W D 3 .   ? 15.402 1.254   0.894   0.32 15.88 ?  202 A1A9W A H6   1 
HETATM 6727 H  H10  B A1A9W D 3 .   ? 15.699 3.507   6.423   0.32 13.92 ?  202 A1A9W A H10  1 
HETATM 6728 H  H3   B A1A9W D 3 .   ? 17.691 -1.933  -0.415  0.32 14.55 ?  202 A1A9W A H3   1 
HETATM 6729 CL CL   B CL    E 4 .   ? 15.865 2.642   -1.047  0.32 12.39 ?  203 CL    A CL   1 
HETATM 6730 O  O    . HOH   F 5 .   ? 14.691 -4.704  20.487  1.00 44.57 ?  301 HOH   A O    1 
HETATM 6731 O  O    . HOH   F 5 .   ? 4.751  3.725   0.497   1.00 23.96 ?  302 HOH   A O    1 
HETATM 6732 O  O    . HOH   F 5 .   ? 17.113 -17.982 15.013  1.00 26.57 ?  303 HOH   A O    1 
HETATM 6733 O  O    . HOH   F 5 .   ? 18.558 -2.348  -16.399 1.00 45.67 ?  304 HOH   A O    1 
HETATM 6734 O  O    . HOH   F 5 .   ? 15.856 2.139   24.681  1.00 41.97 ?  305 HOH   A O    1 
HETATM 6735 O  O    . HOH   F 5 .   ? 21.393 -9.218  21.274  1.00 50.19 ?  306 HOH   A O    1 
HETATM 6736 O  O    . HOH   F 5 .   ? 11.890 0.366   14.673  1.00 33.96 ?  307 HOH   A O    1 
HETATM 6737 O  O    . HOH   F 5 .   ? 11.700 -10.806 -10.080 1.00 45.53 ?  308 HOH   A O    1 
HETATM 6738 O  O    . HOH   F 5 .   ? 7.572  -6.328  -6.547  1.00 38.87 ?  309 HOH   A O    1 
HETATM 6739 O  O    . HOH   F 5 .   ? 34.267 -1.834  12.540  1.00 36.01 ?  310 HOH   A O    1 
HETATM 6740 O  O    B HOH   F 5 .   ? 13.525 -1.101  -6.761  0.32 25.73 ?  311 HOH   A O    1 
HETATM 6741 O  O    . HOH   F 5 .   ? 30.911 6.210   -12.225 1.00 27.61 ?  312 HOH   A O    1 
HETATM 6742 O  O    . HOH   F 5 .   ? 22.686 12.470  1.621   1.00 14.61 ?  313 HOH   A O    1 
HETATM 6743 O  O    . HOH   F 5 .   ? 6.831  -8.026  11.777  1.00 18.45 ?  314 HOH   A O    1 
HETATM 6744 O  O    . HOH   F 5 .   ? 0.693  -4.365  0.079   1.00 32.06 ?  315 HOH   A O    1 
HETATM 6745 O  O    B HOH   F 5 .   ? 8.897  1.981   -2.456  0.32 17.55 ?  316 HOH   A O    1 
HETATM 6746 O  O    . HOH   F 5 .   ? 15.026 -12.188 18.586  1.00 39.65 ?  317 HOH   A O    1 
HETATM 6747 O  O    . HOH   F 5 .   ? 14.642 -13.908 16.659  1.00 26.42 ?  318 HOH   A O    1 
HETATM 6748 O  O    . HOH   F 5 .   ? 28.896 0.458   -9.676  1.00 21.25 ?  319 HOH   A O    1 
HETATM 6749 O  O    . HOH   F 5 .   ? 42.387 10.530  5.124   1.00 19.69 ?  320 HOH   A O    1 
HETATM 6750 O  O    . HOH   F 5 .   ? 14.445 -24.629 11.586  1.00 38.49 ?  321 HOH   A O    1 
HETATM 6751 O  O    B HOH   F 5 .   ? 21.640 3.013   -0.095  0.32 14.22 ?  322 HOH   A O    1 
HETATM 6752 O  O    . HOH   F 5 .   ? 8.837  -11.986 17.141  1.00 43.56 ?  323 HOH   A O    1 
HETATM 6753 O  O    . HOH   F 5 .   ? -0.632 -8.476  2.060   1.00 43.17 ?  324 HOH   A O    1 
HETATM 6754 O  O    . HOH   F 5 .   ? 9.204  -10.071 19.306  1.00 39.53 ?  325 HOH   A O    1 
HETATM 6755 O  O    . HOH   F 5 .   ? 30.212 -13.307 -8.490  1.00 21.21 ?  326 HOH   A O    1 
HETATM 6756 O  O    . HOH   F 5 .   ? 16.150 16.598  8.636   1.00 33.09 ?  327 HOH   A O    1 
HETATM 6757 O  O    . HOH   F 5 .   ? 14.128 -4.551  -11.874 1.00 33.74 ?  328 HOH   A O    1 
HETATM 6758 O  O    B HOH   F 5 .   ? 14.806 -3.045  3.424   0.32 16.98 ?  329 HOH   A O    1 
HETATM 6759 O  O    . HOH   F 5 .   ? 15.012 3.965   17.647  1.00 42.64 ?  330 HOH   A O    1 
HETATM 6760 O  O    . HOH   F 5 .   ? 36.109 -5.103  -0.520  1.00 31.99 ?  331 HOH   A O    1 
HETATM 6761 O  O    . HOH   F 5 .   ? 28.132 -6.267  19.634  1.00 42.64 ?  332 HOH   A O    1 
HETATM 6762 O  O    B HOH   F 5 .   ? 21.118 -2.420  -2.140  0.32 13.98 ?  333 HOH   A O    1 
HETATM 6763 O  O    . HOH   F 5 .   ? 7.915  -12.585 -0.872  1.00 22.49 ?  334 HOH   A O    1 
HETATM 6764 O  O    . HOH   F 5 .   ? 38.203 10.160  7.140   1.00 40.30 ?  335 HOH   A O    1 
HETATM 6765 O  O    . HOH   F 5 .   ? 26.458 -19.317 -1.761  1.00 14.36 ?  336 HOH   A O    1 
HETATM 6766 O  O    . HOH   F 5 .   ? 18.665 -19.335 13.552  1.00 33.13 ?  337 HOH   A O    1 
HETATM 6767 O  O    . HOH   F 5 .   ? 15.480 11.840  7.923   1.00 37.70 ?  338 HOH   A O    1 
HETATM 6768 O  O    . HOH   F 5 .   ? 9.856  -21.373 5.686   1.00 18.11 ?  339 HOH   A O    1 
HETATM 6769 O  O    . HOH   F 5 .   ? 22.254 5.350   18.960  1.00 43.42 ?  340 HOH   A O    1 
HETATM 6770 O  O    . HOH   F 5 .   ? 33.992 -1.038  -8.891  1.00 27.80 ?  341 HOH   A O    1 
HETATM 6771 O  O    . HOH   F 5 .   ? 30.993 -18.091 7.813   1.00 19.66 ?  342 HOH   A O    1 
HETATM 6772 O  O    . HOH   F 5 .   ? 37.475 2.799   10.235  1.00 27.30 ?  343 HOH   A O    1 
HETATM 6773 O  O    . HOH   F 5 .   ? 20.623 -19.717 -5.034  1.00 26.64 ?  344 HOH   A O    1 
HETATM 6774 O  O    . HOH   F 5 .   ? 18.885 -21.942 6.955   1.00 31.71 ?  345 HOH   A O    1 
HETATM 6775 O  O    . HOH   F 5 .   ? 44.277 7.127   6.412   1.00 26.47 ?  346 HOH   A O    1 
HETATM 6776 O  O    . HOH   F 5 .   ? 27.893 0.821   -7.111  1.00 14.06 ?  347 HOH   A O    1 
HETATM 6777 O  O    A HOH   F 5 .   ? 14.591 -3.632  3.088   0.68 13.71 ?  348 HOH   A O    1 
HETATM 6778 O  O    . HOH   F 5 .   ? 19.875 -12.549 -8.847  1.00 24.35 ?  349 HOH   A O    1 
HETATM 6779 O  O    . HOH   F 5 .   ? 13.537 -15.224 -7.461  1.00 25.39 ?  350 HOH   A O    1 
HETATM 6780 O  O    . HOH   F 5 .   ? 27.302 13.780  2.843   1.00 29.44 ?  351 HOH   A O    1 
HETATM 6781 O  O    . HOH   F 5 .   ? 28.306 -0.139  -13.376 1.00 33.63 ?  352 HOH   A O    1 
HETATM 6782 O  O    A HOH   F 5 .   ? 13.273 -1.416  -6.535  0.68 14.77 ?  353 HOH   A O    1 
HETATM 6783 O  O    . HOH   F 5 .   ? 14.362 -21.190 -4.258  1.00 28.53 ?  354 HOH   A O    1 
HETATM 6784 O  O    A HOH   F 5 .   ? 14.229 0.597   6.789   0.68 17.81 ?  355 HOH   A O    1 
HETATM 6785 O  O    . HOH   F 5 .   ? 38.510 4.981   7.026   1.00 15.38 ?  356 HOH   A O    1 
HETATM 6786 O  O    . HOH   F 5 .   ? 39.717 -1.041  -5.140  1.00 21.24 ?  357 HOH   A O    1 
HETATM 6787 O  O    A HOH   F 5 .   ? 17.455 -1.692  0.435   0.68 17.77 ?  358 HOH   A O    1 
HETATM 6788 O  O    . HOH   F 5 .   ? 42.509 4.280   5.420   1.00 30.14 ?  359 HOH   A O    1 
HETATM 6789 O  O    . HOH   F 5 .   ? 26.799 11.399  1.671   1.00 16.03 ?  360 HOH   A O    1 
HETATM 6790 O  O    A HOH   F 5 .   ? 3.549  -9.437  9.714   0.68 23.68 ?  361 HOH   A O    1 
HETATM 6791 O  O    . HOH   F 5 .   ? 37.172 -2.779  9.713   1.00 39.54 ?  362 HOH   A O    1 
HETATM 6792 O  O    A HOH   F 5 .   ? 8.142  -21.374 3.983   0.68 35.41 ?  363 HOH   A O    1 
HETATM 6793 O  O    . HOH   F 5 .   ? 35.727 -12.644 6.869   1.00 15.86 ?  364 HOH   A O    1 
HETATM 6794 O  O    . HOH   F 5 .   ? 23.997 -2.096  -2.086  1.00 10.76 ?  365 HOH   A O    1 
HETATM 6795 O  O    . HOH   F 5 .   ? 31.635 8.224   14.851  1.00 23.48 ?  366 HOH   A O    1 
HETATM 6796 O  O    . HOH   F 5 .   ? 22.112 -19.270 11.400  1.00 35.20 ?  367 HOH   A O    1 
HETATM 6797 O  O    A HOH   F 5 .   ? -0.521 -3.067  3.078   0.68 30.44 ?  368 HOH   A O    1 
HETATM 6798 O  O    . HOH   F 5 .   ? 25.673 -0.806  -7.353  1.00 15.39 ?  369 HOH   A O    1 
HETATM 6799 O  O    . HOH   F 5 .   ? 30.752 3.096   8.288   1.00 11.98 ?  370 HOH   A O    1 
HETATM 6800 O  O    . HOH   F 5 .   ? 16.964 -19.261 4.895   1.00 14.99 ?  371 HOH   A O    1 
HETATM 6801 O  O    . HOH   F 5 .   ? -1.247 -4.616  7.437   1.00 48.21 ?  372 HOH   A O    1 
HETATM 6802 O  O    . HOH   F 5 .   ? 6.386  -5.495  11.013  1.00 19.09 ?  373 HOH   A O    1 
HETATM 6803 O  O    . HOH   F 5 .   ? 21.843 -21.879 8.435   1.00 28.68 ?  374 HOH   A O    1 
HETATM 6804 O  O    . HOH   F 5 .   ? 31.054 -13.933 -2.435  1.00 13.69 ?  375 HOH   A O    1 
HETATM 6805 O  O    . HOH   F 5 .   ? 37.287 11.979  4.966   1.00 29.50 ?  376 HOH   A O    1 
HETATM 6806 O  O    . HOH   F 5 .   ? 43.308 7.800   2.692   1.00 27.83 ?  377 HOH   A O    1 
HETATM 6807 O  O    . HOH   F 5 .   ? 31.866 -9.316  -6.596  1.00 22.05 ?  378 HOH   A O    1 
HETATM 6808 O  O    . HOH   F 5 .   ? 17.131 -17.741 -5.029  1.00 26.24 ?  379 HOH   A O    1 
HETATM 6809 O  O    B HOH   F 5 .   ? 11.788 6.511   9.368   0.32 27.37 ?  380 HOH   A O    1 
HETATM 6810 O  O    . HOH   F 5 .   ? 33.601 -7.153  4.352   1.00 16.20 ?  381 HOH   A O    1 
HETATM 6811 O  O    . HOH   F 5 .   ? 43.885 8.428   -3.054  1.00 26.92 ?  382 HOH   A O    1 
HETATM 6812 O  O    . HOH   F 5 .   ? 18.514 9.436   8.982   1.00 21.84 ?  383 HOH   A O    1 
HETATM 6813 O  O    . HOH   F 5 .   ? 27.406 -6.125  -13.957 1.00 35.84 ?  384 HOH   A O    1 
HETATM 6814 O  O    . HOH   F 5 .   ? 18.871 -0.725  -1.636  1.00 13.15 ?  385 HOH   A O    1 
HETATM 6815 O  O    . HOH   F 5 .   ? 33.500 -16.914 8.142   1.00 19.92 ?  386 HOH   A O    1 
HETATM 6816 O  O    . HOH   F 5 .   ? 13.878 -4.944  17.353  1.00 27.84 ?  387 HOH   A O    1 
HETATM 6817 O  O    T HOH   F 5 .   ? 15.364 -0.399  2.377   0.30 12.62 ?  388 HOH   A O    1 
HETATM 6818 O  O    . HOH   F 5 .   ? 27.396 -10.584 14.091  1.00 17.75 ?  389 HOH   A O    1 
HETATM 6819 O  O    . HOH   F 5 .   ? 16.533 -22.042 1.003   1.00 28.14 ?  390 HOH   A O    1 
HETATM 6820 O  O    . HOH   F 5 .   ? 31.751 -7.320  -9.813  1.00 21.57 ?  391 HOH   A O    1 
HETATM 6821 O  O    . HOH   F 5 .   ? 24.382 3.579   -1.805  1.00 14.08 ?  392 HOH   A O    1 
HETATM 6822 O  O    . HOH   F 5 .   ? 28.574 -10.608 -13.997 1.00 40.94 ?  393 HOH   A O    1 
HETATM 6823 O  O    . HOH   F 5 .   ? 21.137 10.221  14.995  1.00 35.22 ?  394 HOH   A O    1 
HETATM 6824 O  O    . HOH   F 5 .   ? 23.867 -15.722 -9.166  1.00 36.30 ?  395 HOH   A O    1 
HETATM 6825 O  O    A HOH   F 5 .   ? 21.207 -2.376  -2.055  0.68 17.61 ?  396 HOH   A O    1 
HETATM 6826 O  O    . HOH   F 5 .   ? 24.647 -17.485 12.723  1.00 24.18 ?  397 HOH   A O    1 
HETATM 6827 O  O    . HOH   F 5 .   ? 15.194 -21.500 14.225  1.00 17.69 ?  398 HOH   A O    1 
HETATM 6828 O  O    . HOH   F 5 .   ? 24.133 -7.722  14.429  1.00 16.77 ?  399 HOH   A O    1 
HETATM 6829 O  O    . HOH   F 5 .   ? 15.144 -8.057  -9.786  1.00 22.93 ?  400 HOH   A O    1 
HETATM 6830 O  O    . HOH   F 5 .   ? 22.565 -11.872 21.804  1.00 45.12 ?  401 HOH   A O    1 
HETATM 6831 O  O    . HOH   F 5 .   ? 37.493 -2.018  5.838   1.00 26.49 ?  402 HOH   A O    1 
HETATM 6832 O  O    B HOH   F 5 .   ? 11.881 -1.764  -3.260  0.32 15.74 ?  403 HOH   A O    1 
HETATM 6833 O  O    . HOH   F 5 .   ? 6.620  -3.181  12.673  1.00 27.60 ?  404 HOH   A O    1 
HETATM 6834 O  O    . HOH   F 5 .   ? 14.041 -23.039 7.438   1.00 17.62 ?  405 HOH   A O    1 
HETATM 6835 O  O    A HOH   F 5 .   ? 11.025 -0.357  1.921   0.38 20.98 ?  406 HOH   A O    1 
HETATM 6836 O  O    B HOH   F 5 .   ? 22.603 5.554   -1.876  0.32 18.21 ?  407 HOH   A O    1 
HETATM 6837 O  O    B HOH   F 5 .   ? 10.957 2.274   11.811  0.32 21.91 ?  408 HOH   A O    1 
HETATM 6838 O  O    A HOH   F 5 .   ? 24.548 2.058   -6.990  0.68 16.25 ?  409 HOH   A O    1 
HETATM 6839 O  O    A HOH   F 5 .   ? 20.064 4.561   -7.553  0.68 17.48 ?  410 HOH   A O    1 
HETATM 6840 O  O    . HOH   F 5 .   ? 23.437 11.369  4.067   1.00 12.18 ?  411 HOH   A O    1 
HETATM 6841 O  O    . HOH   F 5 .   ? 32.720 -9.254  5.963   1.00 20.09 ?  412 HOH   A O    1 
HETATM 6842 O  O    . HOH   F 5 .   ? 30.610 1.901   16.695  1.00 21.01 ?  413 HOH   A O    1 
HETATM 6843 O  O    . HOH   F 5 .   ? 27.221 2.339   18.678  1.00 30.82 ?  414 HOH   A O    1 
HETATM 6844 O  O    . HOH   F 5 .   ? 21.756 -13.831 -8.172  1.00 39.10 ?  415 HOH   A O    1 
HETATM 6845 O  O    . HOH   F 5 .   ? 14.532 -0.547  -12.130 1.00 22.61 ?  416 HOH   A O    1 
HETATM 6846 O  O    . HOH   F 5 .   ? 20.520 -20.001 2.773   1.00 18.12 ?  417 HOH   A O    1 
HETATM 6847 O  O    . HOH   F 5 .   ? 23.904 -20.248 -1.333  1.00 16.60 ?  418 HOH   A O    1 
HETATM 6848 O  O    A HOH   F 5 .   ? 15.755 -0.922  5.261   0.68 18.42 ?  419 HOH   A O    1 
HETATM 6849 O  O    . HOH   F 5 .   ? 38.057 -1.329  -1.905  1.00 19.08 ?  420 HOH   A O    1 
HETATM 6850 O  O    . HOH   F 5 .   ? 29.982 -10.065 13.050  1.00 21.78 ?  421 HOH   A O    1 
HETATM 6851 O  O    . HOH   F 5 .   ? 5.421  2.805   4.926   1.00 32.17 ?  422 HOH   A O    1 
HETATM 6852 O  O    . HOH   F 5 .   ? 26.908 4.163   -0.651  1.00 12.38 ?  423 HOH   A O    1 
HETATM 6853 O  O    . HOH   F 5 .   ? 30.243 -12.885 13.541  1.00 20.19 ?  424 HOH   A O    1 
HETATM 6854 O  O    . HOH   F 5 .   ? 32.655 -4.295  -9.837  1.00 28.13 ?  425 HOH   A O    1 
HETATM 6855 O  O    . HOH   F 5 .   ? 40.883 -8.251  -6.803  1.00 35.52 ?  426 HOH   A O    1 
HETATM 6856 O  O    A HOH   F 5 .   ? 21.308 3.176   -0.354  0.68 10.76 ?  427 HOH   A O    1 
HETATM 6857 O  O    . HOH   F 5 .   ? 35.028 -5.226  -3.056  1.00 18.00 ?  428 HOH   A O    1 
HETATM 6858 O  O    . HOH   F 5 .   ? 19.452 -11.172 24.059  1.00 64.84 ?  429 HOH   A O    1 
HETATM 6859 O  O    A HOH   F 5 .   ? 24.055 3.978   -4.919  0.68 19.01 ?  430 HOH   A O    1 
HETATM 6860 O  O    . HOH   F 5 .   ? 36.692 -4.920  5.419   1.00 23.13 ?  431 HOH   A O    1 
HETATM 6861 O  O    . HOH   F 5 .   ? 32.471 -10.652 3.234   1.00 31.05 ?  432 HOH   A O    1 
HETATM 6862 O  O    . HOH   F 5 .   ? 11.660 -10.674 16.930  1.00 24.92 ?  433 HOH   A O    1 
HETATM 6863 O  O    . HOH   F 5 .   ? 10.368 -13.732 -1.701  1.00 16.49 ?  434 HOH   A O    1 
HETATM 6864 O  O    . HOH   F 5 .   ? 16.138 -14.150 20.165  1.00 50.05 ?  435 HOH   A O    1 
HETATM 6865 O  O    . HOH   F 5 .   ? 41.558 1.512   5.056   1.00 36.08 ?  436 HOH   A O    1 
HETATM 6866 O  O    A HOH   F 5 .   ? 10.984 1.578   12.738  0.68 21.31 ?  437 HOH   A O    1 
HETATM 6867 O  O    . HOH   F 5 .   ? 15.956 6.856   2.965   1.00 18.52 ?  438 HOH   A O    1 
HETATM 6868 O  O    . HOH   F 5 .   ? 22.562 8.150   18.332  1.00 45.81 ?  439 HOH   A O    1 
HETATM 6869 O  O    . HOH   F 5 .   ? 44.980 -0.565  3.077   1.00 41.92 ?  440 HOH   A O    1 
HETATM 6870 O  O    B HOH   F 5 .   ? 23.213 7.887   -3.134  0.32 27.92 ?  441 HOH   A O    1 
HETATM 6871 O  O    . HOH   F 5 .   ? 10.363 -22.172 -1.206  1.00 49.06 ?  442 HOH   A O    1 
HETATM 6872 O  O    . HOH   F 5 .   ? 18.504 4.947   -15.088 1.00 48.77 ?  443 HOH   A O    1 
HETATM 6873 O  O    . HOH   F 5 .   ? 23.436 -7.987  17.084  1.00 21.71 ?  444 HOH   A O    1 
HETATM 6874 O  O    . HOH   F 5 .   ? 27.019 -3.174  19.400  1.00 36.23 ?  445 HOH   A O    1 
HETATM 6875 O  O    . HOH   F 5 .   ? 23.311 -20.894 1.362   1.00 18.35 ?  446 HOH   A O    1 
HETATM 6876 O  O    . HOH   F 5 .   ? 18.838 1.969   -0.686  1.00 12.58 ?  447 HOH   A O    1 
HETATM 6877 O  O    A HOH   F 5 .   ? 9.345  -16.304 -1.993  0.68 31.63 ?  448 HOH   A O    1 
HETATM 6878 O  O    . HOH   F 5 .   ? 34.378 -8.071  -0.525  1.00 27.96 ?  449 HOH   A O    1 
HETATM 6879 O  O    A HOH   F 5 .   ? 13.984 -0.316  3.451   0.38 28.50 ?  450 HOH   A O    1 
HETATM 6880 O  O    . HOH   F 5 .   ? 37.693 -8.816  -3.408  1.00 23.49 ?  451 HOH   A O    1 
HETATM 6881 O  O    . HOH   F 5 .   ? 18.343 -15.955 16.345  1.00 36.25 ?  452 HOH   A O    1 
HETATM 6882 O  O    A HOH   F 5 .   ? 23.163 7.532   -3.241  0.68 25.99 ?  453 HOH   A O    1 
HETATM 6883 O  O    . HOH   F 5 .   ? 30.571 14.757  2.790   1.00 18.73 ?  454 HOH   A O    1 
HETATM 6884 O  O    A HOH   F 5 .   ? 16.219 2.969   -1.451  0.68 16.55 ?  455 HOH   A O    1 
HETATM 6885 O  O    . HOH   F 5 .   ? 21.472 -14.698 17.899  1.00 52.42 ?  456 HOH   A O    1 
HETATM 6886 O  O    . HOH   F 5 .   ? 31.312 -12.774 0.011   1.00 19.99 ?  457 HOH   A O    1 
HETATM 6887 O  O    . HOH   F 5 .   ? 20.538 -17.763 24.858  1.00 53.06 ?  458 HOH   A O    1 
HETATM 6888 O  O    . HOH   F 5 .   ? 27.728 7.005   -6.474  1.00 38.11 ?  459 HOH   A O    1 
HETATM 6889 O  O    . HOH   F 5 .   ? 29.797 -16.034 10.759  1.00 34.74 ?  460 HOH   A O    1 
HETATM 6890 O  O    . HOH   F 5 .   ? 29.762 -1.942  -12.745 1.00 48.33 ?  461 HOH   A O    1 
HETATM 6891 O  O    . HOH   F 5 .   ? 32.405 -15.870 10.890  1.00 31.26 ?  462 HOH   A O    1 
HETATM 6892 O  O    . HOH   F 5 .   ? 25.390 8.242   -4.847  1.00 26.88 ?  463 HOH   A O    1 
HETATM 6893 O  O    . HOH   F 5 .   ? 24.772 5.630   20.708  1.00 53.18 ?  464 HOH   A O    1 
HETATM 6894 O  O    . HOH   F 5 .   ? 19.858 -17.322 -5.033  1.00 23.54 ?  465 HOH   A O    1 
HETATM 6895 O  O    . HOH   F 5 .   ? 23.136 -22.303 -3.303  1.00 35.45 ?  466 HOH   A O    1 
HETATM 6896 O  O    . HOH   F 5 .   ? 18.724 10.866  11.280  1.00 31.67 ?  467 HOH   A O    1 
HETATM 6897 O  O    . HOH   F 5 .   ? 24.591 14.615  7.809   1.00 36.54 ?  468 HOH   A O    1 
HETATM 6898 O  O    . HOH   F 5 .   ? 23.450 13.701  5.507   1.00 18.03 ?  469 HOH   A O    1 
HETATM 6899 O  O    . HOH   F 5 .   ? 39.593 -7.053  -3.513  1.00 43.95 ?  470 HOH   A O    1 
HETATM 6900 O  O    . HOH   F 5 .   ? 15.711 -21.486 3.714   1.00 23.33 ?  471 HOH   A O    1 
HETATM 6901 O  O    . HOH   F 5 .   ? 26.876 11.623  -1.302  1.00 30.26 ?  472 HOH   A O    1 
HETATM 6902 O  O    A HOH   F 5 .   ? 21.929 5.286   -5.841  0.68 28.32 ?  473 HOH   A O    1 
HETATM 6903 O  O    . HOH   F 5 .   ? 27.436 -11.358 16.556  1.00 37.76 ?  474 HOH   A O    1 
HETATM 6904 O  O    . HOH   F 5 .   ? 18.086 -16.175 -8.866  1.00 43.05 ?  475 HOH   A O    1 
HETATM 6905 O  O    . HOH   F 5 .   ? 11.927 -13.423 16.345  1.00 51.28 ?  476 HOH   A O    1 
HETATM 6906 O  O    . HOH   F 5 .   ? 12.235 1.601   17.269  1.00 39.62 ?  477 HOH   A O    1 
HETATM 6907 O  O    . HOH   F 5 .   ? 25.818 10.773  -3.691  1.00 23.37 ?  478 HOH   A O    1 
HETATM 6908 O  O    B HOH   F 5 .   ? 12.525 2.491   -0.586  0.32 21.62 ?  479 HOH   A O    1 
HETATM 6909 O  O    B HOH   F 5 .   ? 11.251 0.452   -2.067  0.32 22.35 ?  480 HOH   A O    1 
HETATM 6910 O  O    . HOH   F 5 .   ? 10.998 -15.094 -6.125  1.00 33.58 ?  481 HOH   A O    1 
HETATM 6911 O  O    . HOH   F 5 .   ? 14.000 -10.332 -10.871 1.00 32.22 ?  482 HOH   A O    1 
HETATM 6912 O  O    . HOH   F 5 .   ? 15.678 -17.106 -6.975  1.00 29.87 ?  483 HOH   A O    1 
HETATM 6913 O  O    . HOH   F 5 .   ? 17.352 -18.672 19.854  1.00 49.24 ?  484 HOH   A O    1 
HETATM 6914 O  O    . HOH   F 5 .   ? 35.101 7.452   12.304  1.00 42.75 ?  485 HOH   A O    1 
HETATM 6915 O  O    . HOH   F 5 .   ? 16.795 -20.483 16.122  1.00 28.86 ?  486 HOH   A O    1 
HETATM 6916 O  O    . HOH   F 5 .   ? 28.770 9.064   17.514  1.00 36.78 ?  487 HOH   A O    1 
HETATM 6917 O  O    . HOH   F 5 .   ? 28.566 -4.641  -12.276 1.00 35.09 ?  488 HOH   A O    1 
HETATM 6918 O  O    . HOH   F 5 .   ? 40.988 -3.966  -0.355  1.00 37.42 ?  489 HOH   A O    1 
HETATM 6919 O  O    . HOH   F 5 .   ? 23.147 11.838  -4.040  1.00 19.04 ?  490 HOH   A O    1 
HETATM 6920 O  O    B HOH   F 5 .   ? 10.476 -1.554  -5.655  0.32 20.72 ?  491 HOH   A O    1 
HETATM 6921 O  O    . HOH   F 5 .   ? 30.863 0.730   19.141  1.00 37.87 ?  492 HOH   A O    1 
HETATM 6922 O  O    . HOH   F 5 .   ? 44.469 10.415  -1.608  1.00 31.21 ?  493 HOH   A O    1 
HETATM 6923 O  O    . HOH   F 5 .   ? 23.135 -12.802 19.305  1.00 45.37 ?  494 HOH   A O    1 
HETATM 6924 O  O    B HOH   F 5 .   ? 10.069 3.820   -0.478  0.32 24.20 ?  495 HOH   A O    1 
HETATM 6925 O  O    . HOH   F 5 .   ? 15.977 -6.797  -11.850 1.00 42.02 ?  496 HOH   A O    1 
HETATM 6926 O  O    . HOH   F 5 .   ? 41.707 9.379   -3.911  1.00 31.10 ?  497 HOH   A O    1 
HETATM 6927 O  O    . HOH   F 5 .   ? 39.121 2.427   7.489   1.00 31.12 ?  498 HOH   A O    1 
HETATM 6928 O  O    . HOH   F 5 .   ? 28.649 -7.948  -15.248 1.00 46.95 ?  499 HOH   A O    1 
HETATM 6929 O  O    . HOH   F 5 .   ? 31.423 -0.574  -10.532 1.00 29.08 ?  500 HOH   A O    1 
HETATM 6930 O  O    . HOH   F 5 .   ? 13.885 -25.214 8.917   1.00 33.14 ?  501 HOH   A O    1 
HETATM 6931 O  O    . HOH   F 5 .   ? 20.500 -16.056 -7.353  1.00 28.99 ?  502 HOH   A O    1 
HETATM 6932 O  O    . HOH   F 5 .   ? 18.379 -23.206 1.925   1.00 41.98 ?  503 HOH   A O    1 
HETATM 6933 O  O    B HOH   F 5 .   ? 10.212 5.302   10.532  0.32 34.00 ?  504 HOH   A O    1 
HETATM 6934 O  O    . HOH   F 5 .   ? 40.524 -0.252  -7.779  1.00 32.01 ?  505 HOH   A O    1 
HETATM 6935 O  O    . HOH   F 5 .   ? 30.722 5.817   -14.732 1.00 34.95 ?  506 HOH   A O    1 
HETATM 6936 O  O    . HOH   F 5 .   ? 16.166 -23.357 5.754   1.00 27.40 ?  507 HOH   A O    1 
HETATM 6937 O  O    . HOH   F 5 .   ? 20.009 -22.335 4.213   1.00 26.95 ?  508 HOH   A O    1 
HETATM 6938 O  O    . HOH   F 5 .   ? 8.104  -3.139  -5.908  1.00 49.74 ?  509 HOH   A O    1 
HETATM 6939 O  O    . HOH   F 5 .   ? 37.328 -6.628  7.625   1.00 26.41 ?  510 HOH   A O    1 
HETATM 6940 O  O    . HOH   F 5 .   ? 30.737 -5.810  -11.863 1.00 43.84 ?  511 HOH   A O    1 
HETATM 6941 O  O    . HOH   F 5 .   ? 23.133 -23.755 1.622   1.00 30.09 ?  512 HOH   A O    1 
HETATM 6942 O  O    . HOH   F 5 .   ? 14.771 8.291   4.931   1.00 38.71 ?  513 HOH   A O    1 
HETATM 6943 O  O    . HOH   F 5 .   ? 39.478 -0.010  6.643   1.00 29.75 ?  514 HOH   A O    1 
HETATM 6944 O  O    . HOH   F 5 .   ? 28.975 14.458  0.898   1.00 46.75 ?  515 HOH   A O    1 
HETATM 6945 O  O    . HOH   F 5 .   ? 37.996 13.922  6.706   1.00 38.04 ?  516 HOH   A O    1 
HETATM 6946 O  O    B HOH   F 5 .   ? 9.806  1.034   -5.337  0.32 20.16 ?  517 HOH   A O    1 
HETATM 6947 O  O    . HOH   F 5 .   ? 36.453 -6.457  10.221  1.00 45.45 ?  518 HOH   A O    1 
HETATM 6948 O  O    . HOH   F 5 .   ? 21.982 -23.987 4.520   1.00 25.57 ?  519 HOH   A O    1 
HETATM 6949 O  O    T HOH   F 5 .   ? 11.884 -2.128  -3.666  0.30 11.20 ?  520 HOH   A O    1 
HETATM 6950 O  O    . HOH   F 5 .   ? 17.290 -6.728  -14.201 1.00 43.16 ?  521 HOH   A O    1 
HETATM 6951 O  O    . HOH   F 5 .   ? 24.062 9.020   -7.192  1.00 34.62 ?  522 HOH   A O    1 
HETATM 6952 O  O    . HOH   F 5 .   ? 15.829 -12.248 27.354  1.00 42.75 ?  523 HOH   A O    1 
HETATM 6953 O  O    . HOH   F 5 .   ? 16.333 -21.109 18.728  1.00 37.41 ?  524 HOH   A O    1 
HETATM 6954 O  O    . HOH   F 5 .   ? 14.685 -22.719 19.834  1.00 33.61 ?  525 HOH   A O    1 
HETATM 6955 O  O    . HOH   G 5 .   ? 29.817 -22.397 5.524   1.00 20.14 ?  201 HOH   B O    1 
HETATM 6956 O  O    . HOH   G 5 .   ? 41.669 -35.965 -17.103 1.00 31.88 ?  202 HOH   B O    1 
HETATM 6957 O  O    . HOH   G 5 .   ? 27.689 -29.156 -1.841  1.00 35.14 ?  203 HOH   B O    1 
HETATM 6958 O  O    . HOH   G 5 .   ? 59.101 -18.720 6.861   1.00 33.61 ?  204 HOH   B O    1 
HETATM 6959 O  O    . HOH   G 5 .   ? 37.919 -39.426 -0.162  1.00 37.31 ?  205 HOH   B O    1 
HETATM 6960 O  O    . HOH   G 5 .   ? 27.856 -41.808 -15.078 1.00 36.18 ?  206 HOH   B O    1 
HETATM 6961 O  O    . HOH   G 5 .   ? 47.382 -7.411  -3.901  1.00 38.04 ?  207 HOH   B O    1 
HETATM 6962 O  O    . HOH   G 5 .   ? 48.004 -6.908  15.544  1.00 32.65 ?  208 HOH   B O    1 
HETATM 6963 O  O    . HOH   G 5 .   ? 29.891 -26.256 4.072   1.00 27.54 ?  209 HOH   B O    1 
HETATM 6964 O  O    . HOH   G 5 .   ? 41.323 -7.752  5.485   1.00 38.24 ?  210 HOH   B O    1 
HETATM 6965 O  O    . HOH   G 5 .   ? 49.368 -22.701 -19.720 1.00 46.93 ?  211 HOH   B O    1 
HETATM 6966 O  O    . HOH   G 5 .   ? 30.200 -40.979 -8.041  1.00 16.89 ?  212 HOH   B O    1 
HETATM 6967 O  O    . HOH   G 5 .   ? 54.468 -9.371  -8.687  1.00 19.27 ?  213 HOH   B O    1 
HETATM 6968 O  O    . HOH   G 5 .   ? 56.310 -19.702 7.283   1.00 31.40 ?  214 HOH   B O    1 
HETATM 6969 O  O    . HOH   G 5 .   ? 52.927 -13.453 -20.265 1.00 36.52 ?  215 HOH   B O    1 
HETATM 6970 O  O    . HOH   G 5 .   ? 50.157 -3.375  7.166   1.00 35.15 ?  216 HOH   B O    1 
HETATM 6971 O  O    . HOH   G 5 .   ? 56.640 -30.708 -7.741  1.00 31.67 ?  217 HOH   B O    1 
HETATM 6972 O  O    . HOH   G 5 .   ? 44.377 -7.213  2.059   1.00 34.22 ?  218 HOH   B O    1 
HETATM 6973 O  O    . HOH   G 5 .   ? 57.117 -26.857 -7.642  1.00 40.57 ?  219 HOH   B O    1 
HETATM 6974 O  O    . HOH   G 5 .   ? 58.177 -12.910 8.448   1.00 30.99 ?  220 HOH   B O    1 
HETATM 6975 O  O    . HOH   G 5 .   ? 57.648 -24.460 5.040   1.00 34.09 ?  221 HOH   B O    1 
HETATM 6976 O  O    . HOH   G 5 .   ? 41.477 -39.145 -14.810 1.00 22.40 ?  222 HOH   B O    1 
HETATM 6977 O  O    . HOH   G 5 .   ? 30.870 -28.750 4.340   1.00 28.43 ?  223 HOH   B O    1 
HETATM 6978 O  O    . HOH   G 5 .   ? 55.323 -16.501 -14.275 1.00 32.01 ?  224 HOH   B O    1 
HETATM 6979 O  O    . HOH   G 5 .   ? 50.750 -6.102  0.173   1.00 26.18 ?  225 HOH   B O    1 
HETATM 6980 O  O    . HOH   G 5 .   ? 34.526 -36.343 -7.135  1.00 18.49 ?  226 HOH   B O    1 
HETATM 6981 O  O    . HOH   G 5 .   ? 34.860 -24.621 13.825  1.00 32.29 ?  227 HOH   B O    1 
HETATM 6982 O  O    . HOH   G 5 .   ? 35.997 -43.292 -8.408  1.00 33.16 ?  228 HOH   B O    1 
HETATM 6983 O  O    . HOH   G 5 .   ? 37.033 -19.799 -18.102 1.00 37.79 ?  229 HOH   B O    1 
HETATM 6984 O  O    . HOH   G 5 .   ? 51.647 -6.475  4.398   1.00 19.79 ?  230 HOH   B O    1 
HETATM 6985 O  O    . HOH   G 5 .   ? 57.359 -16.252 -12.184 1.00 18.69 ?  231 HOH   B O    1 
HETATM 6986 O  O    . HOH   G 5 .   ? 48.546 -36.489 -15.445 1.00 43.30 ?  232 HOH   B O    1 
HETATM 6987 O  O    . HOH   G 5 .   ? 46.383 -1.541  13.175  1.00 27.65 ?  233 HOH   B O    1 
HETATM 6988 O  O    . HOH   G 5 .   ? 39.255 -10.857 6.127   1.00 25.13 ?  234 HOH   B O    1 
HETATM 6989 O  O    . HOH   G 5 .   ? 29.776 -34.146 -0.409  1.00 35.46 ?  235 HOH   B O    1 
HETATM 6990 O  O    . HOH   G 5 .   ? 32.776 -43.762 -11.257 1.00 20.53 ?  236 HOH   B O    1 
HETATM 6991 O  O    . HOH   G 5 .   ? 41.353 -9.605  13.071  1.00 22.80 ?  237 HOH   B O    1 
HETATM 6992 O  O    . HOH   G 5 .   ? 45.091 -34.957 6.834   1.00 41.72 ?  238 HOH   B O    1 
HETATM 6993 O  O    . HOH   G 5 .   ? 35.092 -7.994  -2.995  1.00 17.79 ?  239 HOH   B O    1 
HETATM 6994 O  O    . HOH   G 5 .   ? 40.605 -16.044 14.131  1.00 23.38 ?  240 HOH   B O    1 
HETATM 6995 O  O    . HOH   G 5 .   ? 44.465 -27.703 -0.644  1.00 22.54 ?  241 HOH   B O    1 
HETATM 6996 O  O    . HOH   G 5 .   ? 50.700 -12.966 -0.438  1.00 11.77 ?  242 HOH   B O    1 
HETATM 6997 O  O    . HOH   G 5 .   ? 25.380 -25.917 -1.276  1.00 32.45 ?  243 HOH   B O    1 
HETATM 6998 O  O    . HOH   G 5 .   ? 28.394 -19.677 -13.100 1.00 24.23 ?  244 HOH   B O    1 
HETATM 6999 O  O    . HOH   G 5 .   ? 42.535 -25.344 2.663   1.00 15.40 ?  245 HOH   B O    1 
HETATM 7000 O  O    . HOH   G 5 .   ? 43.042 -43.203 -8.179  1.00 28.67 ?  246 HOH   B O    1 
HETATM 7001 O  O    . HOH   G 5 .   ? 34.208 -18.443 11.419  1.00 25.05 ?  247 HOH   B O    1 
HETATM 7002 O  O    . HOH   G 5 .   ? 44.875 -43.546 -10.462 1.00 28.52 ?  248 HOH   B O    1 
HETATM 7003 O  O    . HOH   G 5 .   ? 38.473 -11.048 -2.229  1.00 18.60 ?  249 HOH   B O    1 
HETATM 7004 O  O    . HOH   G 5 .   ? 42.598 -22.846 3.874   1.00 11.74 ?  250 HOH   B O    1 
HETATM 7005 O  O    . HOH   G 5 .   ? 39.475 -11.102 0.364   1.00 16.54 ?  251 HOH   B O    1 
HETATM 7006 O  O    . HOH   G 5 .   ? 57.559 -24.371 -3.777  1.00 21.40 ?  252 HOH   B O    1 
HETATM 7007 O  O    . HOH   G 5 .   ? 47.981 -24.541 -17.732 1.00 30.14 ?  253 HOH   B O    1 
HETATM 7008 O  O    . HOH   G 5 .   ? 43.161 -32.363 -16.996 1.00 23.89 ?  254 HOH   B O    1 
HETATM 7009 O  O    . HOH   G 5 .   ? 58.132 -10.634 -4.026  1.00 19.37 ?  255 HOH   B O    1 
HETATM 7010 O  O    . HOH   G 5 .   ? 51.500 -13.856 11.034  1.00 25.88 ?  256 HOH   B O    1 
HETATM 7011 O  O    . HOH   G 5 .   ? 27.099 -31.804 -9.885  1.00 20.08 ?  257 HOH   B O    1 
HETATM 7012 O  O    . HOH   G 5 .   ? 41.847 -23.511 9.307   1.00 17.69 ?  258 HOH   B O    1 
HETATM 7013 O  O    . HOH   G 5 .   ? 29.693 -25.210 -10.734 1.00 17.05 ?  259 HOH   B O    1 
HETATM 7014 O  O    . HOH   G 5 .   ? 31.792 -17.919 -14.454 1.00 30.23 ?  260 HOH   B O    1 
HETATM 7015 O  O    . HOH   G 5 .   ? 38.894 -11.944 12.361  1.00 33.04 ?  261 HOH   B O    1 
HETATM 7016 O  O    . HOH   G 5 .   ? 40.296 -12.738 -11.472 1.00 15.11 ?  262 HOH   B O    1 
HETATM 7017 O  O    . HOH   G 5 .   ? 50.933 -39.927 -8.176  1.00 36.17 ?  263 HOH   B O    1 
HETATM 7018 O  O    . HOH   G 5 .   ? 49.700 -0.501  10.197  1.00 29.03 ?  264 HOH   B O    1 
HETATM 7019 O  O    . HOH   G 5 .   ? 47.957 -22.746 5.857   1.00 17.34 ?  265 HOH   B O    1 
HETATM 7020 O  O    . HOH   G 5 .   ? 30.832 -15.717 2.693   1.00 14.00 ?  266 HOH   B O    1 
HETATM 7021 O  O    . HOH   G 5 .   ? 56.111 -23.543 -14.662 1.00 27.22 ?  267 HOH   B O    1 
HETATM 7022 O  O    . HOH   G 5 .   ? 57.455 -9.222  1.464   1.00 19.55 ?  268 HOH   B O    1 
HETATM 7023 O  O    . HOH   G 5 .   ? 30.514 -42.195 -10.562 1.00 29.73 ?  269 HOH   B O    1 
HETATM 7024 O  O    . HOH   G 5 .   ? 43.338 -15.785 -12.136 1.00 14.16 ?  270 HOH   B O    1 
HETATM 7025 O  O    . HOH   G 5 .   ? 28.440 -30.871 -14.684 1.00 30.19 ?  271 HOH   B O    1 
HETATM 7026 O  O    . HOH   G 5 .   ? 56.890 -8.658  8.465   1.00 19.04 ?  272 HOH   B O    1 
HETATM 7027 O  O    . HOH   G 5 .   ? 42.305 -9.904  9.366   1.00 20.53 ?  273 HOH   B O    1 
HETATM 7028 O  O    . HOH   G 5 .   ? 34.908 -33.326 -19.121 1.00 32.80 ?  274 HOH   B O    1 
HETATM 7029 O  O    . HOH   G 5 .   ? 49.277 -28.685 -6.842  1.00 15.52 ?  275 HOH   B O    1 
HETATM 7030 O  O    . HOH   G 5 .   ? 34.451 -12.766 2.643   1.00 24.04 ?  276 HOH   B O    1 
HETATM 7031 O  O    . HOH   G 5 .   ? 28.243 -34.319 -9.370  1.00 19.04 ?  277 HOH   B O    1 
HETATM 7032 O  O    . HOH   G 5 .   ? 42.347 -34.679 3.794   1.00 26.52 ?  278 HOH   B O    1 
HETATM 7033 O  O    . HOH   G 5 .   ? 46.589 -31.236 -4.730  1.00 22.19 ?  279 HOH   B O    1 
HETATM 7034 O  O    . HOH   G 5 .   ? 46.837 -29.522 9.836   1.00 31.93 ?  280 HOH   B O    1 
HETATM 7035 O  O    . HOH   G 5 .   ? 27.931 -22.882 -7.932  1.00 17.61 ?  281 HOH   B O    1 
HETATM 7036 O  O    . HOH   G 5 .   ? 27.563 -26.678 -15.579 1.00 32.12 ?  282 HOH   B O    1 
HETATM 7037 O  O    . HOH   G 5 .   ? 41.123 -5.520  11.540  1.00 41.86 ?  283 HOH   B O    1 
HETATM 7038 O  O    . HOH   G 5 .   ? 48.370 -25.022 3.140   1.00 13.48 ?  284 HOH   B O    1 
HETATM 7039 O  O    . HOH   G 5 .   ? 59.732 -15.280 8.173   1.00 30.21 ?  285 HOH   B O    1 
HETATM 7040 O  O    . HOH   G 5 .   ? 45.315 -33.367 -15.861 1.00 24.24 ?  286 HOH   B O    1 
HETATM 7041 O  O    . HOH   G 5 .   ? 49.941 -24.635 5.820   1.00 32.33 ?  287 HOH   B O    1 
HETATM 7042 O  O    . HOH   G 5 .   ? 45.869 -40.350 -3.531  1.00 28.05 ?  288 HOH   B O    1 
HETATM 7043 O  O    . HOH   G 5 .   ? 36.785 -12.755 -1.473  1.00 25.80 ?  289 HOH   B O    1 
HETATM 7044 O  O    . HOH   G 5 .   ? 52.466 -10.388 13.010  1.00 22.34 ?  290 HOH   B O    1 
HETATM 7045 O  O    . HOH   G 5 .   ? 48.661 -20.014 5.966   1.00 13.81 ?  291 HOH   B O    1 
HETATM 7046 O  O    . HOH   G 5 .   ? 33.488 -15.275 -13.882 1.00 21.30 ?  292 HOH   B O    1 
HETATM 7047 O  O    . HOH   G 5 .   ? 57.032 -12.064 12.418  1.00 35.65 ?  293 HOH   B O    1 
HETATM 7048 O  O    . HOH   G 5 .   ? 51.181 -37.541 -9.577  1.00 25.62 ?  294 HOH   B O    1 
HETATM 7049 O  O    . HOH   G 5 .   ? 47.025 -33.956 -4.579  1.00 17.45 ?  295 HOH   B O    1 
HETATM 7050 O  O    . HOH   G 5 .   ? 42.880 -20.242 -20.666 1.00 35.80 ?  296 HOH   B O    1 
HETATM 7051 O  O    . HOH   G 5 .   ? 42.688 -12.261 -18.453 1.00 29.04 ?  297 HOH   B O    1 
HETATM 7052 O  O    . HOH   G 5 .   ? 44.589 -27.440 2.034   1.00 15.54 ?  298 HOH   B O    1 
HETATM 7053 O  O    . HOH   G 5 .   ? 42.291 -9.918  -14.845 1.00 36.80 ?  299 HOH   B O    1 
HETATM 7054 O  O    . HOH   G 5 .   ? 37.434 -18.113 13.115  1.00 30.80 ?  300 HOH   B O    1 
HETATM 7055 O  O    . HOH   G 5 .   ? 52.561 -35.632 -8.598  1.00 29.14 ?  301 HOH   B O    1 
HETATM 7056 O  O    . HOH   G 5 .   ? 43.986 -29.339 -4.631  1.00 23.44 ?  302 HOH   B O    1 
HETATM 7057 O  O    . HOH   G 5 .   ? 40.225 -10.844 -9.496  1.00 16.88 ?  303 HOH   B O    1 
HETATM 7058 O  O    . HOH   G 5 .   ? 52.961 -16.005 -12.720 1.00 25.92 ?  304 HOH   B O    1 
HETATM 7059 O  O    . HOH   G 5 .   ? 35.033 -33.520 4.572   1.00 29.28 ?  305 HOH   B O    1 
HETATM 7060 O  O    . HOH   G 5 .   ? 53.432 -30.174 4.525   1.00 18.76 ?  306 HOH   B O    1 
HETATM 7061 O  O    . HOH   G 5 .   ? 25.926 -21.466 -3.475  1.00 16.41 ?  307 HOH   B O    1 
HETATM 7062 O  O    . HOH   G 5 .   ? 32.780 -34.568 -5.835  1.00 17.23 ?  308 HOH   B O    1 
HETATM 7063 O  O    . HOH   G 5 .   ? 37.839 -10.251 -10.711 1.00 17.16 ?  309 HOH   B O    1 
HETATM 7064 O  O    . HOH   G 5 .   ? 52.464 -29.222 -13.001 1.00 25.27 ?  310 HOH   B O    1 
HETATM 7065 O  O    . HOH   G 5 .   ? 62.664 -13.559 4.808   1.00 26.45 ?  311 HOH   B O    1 
HETATM 7066 O  O    . HOH   G 5 .   ? 57.609 -22.061 3.193   1.00 28.43 ?  312 HOH   B O    1 
HETATM 7067 O  O    . HOH   G 5 .   ? 37.254 -35.655 7.242   1.00 32.26 ?  313 HOH   B O    1 
HETATM 7068 O  O    . HOH   G 5 .   ? 38.312 -12.724 7.952   1.00 18.38 ?  314 HOH   B O    1 
HETATM 7069 O  O    . HOH   G 5 .   ? 51.705 -5.923  -7.842  1.00 45.14 ?  315 HOH   B O    1 
HETATM 7070 O  O    . HOH   G 5 .   ? 41.716 -8.053  1.395   1.00 23.75 ?  316 HOH   B O    1 
HETATM 7071 O  O    . HOH   G 5 .   ? 37.077 -30.542 -20.946 1.00 29.89 ?  317 HOH   B O    1 
HETATM 7072 O  O    . HOH   G 5 .   ? 43.165 -21.417 10.695  1.00 16.09 ?  318 HOH   B O    1 
HETATM 7073 O  O    . HOH   G 5 .   ? 26.324 -21.014 -6.202  1.00 16.55 ?  319 HOH   B O    1 
HETATM 7074 O  O    . HOH   G 5 .   ? 53.622 -12.556 -22.148 1.00 31.45 ?  320 HOH   B O    1 
HETATM 7075 O  O    . HOH   G 5 .   ? 62.804 -20.170 -0.716  1.00 35.88 ?  321 HOH   B O    1 
HETATM 7076 O  O    . HOH   G 5 .   ? 51.377 -32.980 -10.778 1.00 38.89 ?  322 HOH   B O    1 
HETATM 7077 O  O    . HOH   G 5 .   ? 43.085 -34.547 0.134   1.00 21.10 ?  323 HOH   B O    1 
HETATM 7078 O  O    . HOH   G 5 .   ? 44.588 -24.588 9.598   1.00 20.49 ?  324 HOH   B O    1 
HETATM 7079 O  O    . HOH   G 5 .   ? 59.880 -17.175 -10.457 1.00 33.87 ?  325 HOH   B O    1 
HETATM 7080 O  O    . HOH   G 5 .   ? 36.690 -12.404 4.305   1.00 18.16 ?  326 HOH   B O    1 
HETATM 7081 O  O    . HOH   G 5 .   ? 48.543 -12.004 -14.085 1.00 27.14 ?  327 HOH   B O    1 
HETATM 7082 O  O    . HOH   G 5 .   ? 44.087 -1.738  7.653   1.00 45.01 ?  328 HOH   B O    1 
HETATM 7083 O  O    . HOH   G 5 .   ? 43.460 -15.379 18.166  1.00 28.50 ?  329 HOH   B O    1 
HETATM 7084 O  O    . HOH   G 5 .   ? 47.154 -24.475 8.210   1.00 24.81 ?  330 HOH   B O    1 
HETATM 7085 O  O    . HOH   G 5 .   ? 38.355 -9.338  -13.232 1.00 26.04 ?  331 HOH   B O    1 
HETATM 7086 O  O    . HOH   G 5 .   ? 33.585 -31.169 11.063  1.00 33.26 ?  332 HOH   B O    1 
HETATM 7087 O  O    . HOH   G 5 .   ? 27.839 -14.767 -9.455  1.00 34.94 ?  333 HOH   B O    1 
HETATM 7088 O  O    . HOH   G 5 .   ? 48.035 -32.624 -16.658 1.00 42.73 ?  334 HOH   B O    1 
HETATM 7089 O  O    . HOH   G 5 .   ? 47.441 -27.406 2.054   1.00 14.88 ?  335 HOH   B O    1 
HETATM 7090 O  O    . HOH   G 5 .   ? 41.178 -24.458 15.891  1.00 44.60 ?  336 HOH   B O    1 
HETATM 7091 O  O    . HOH   G 5 .   ? 45.683 -36.250 -16.028 1.00 34.59 ?  337 HOH   B O    1 
HETATM 7092 O  O    . HOH   G 5 .   ? 36.967 -15.111 -16.469 1.00 38.47 ?  338 HOH   B O    1 
HETATM 7093 O  O    . HOH   G 5 .   ? 42.773 -43.468 -14.315 1.00 41.40 ?  339 HOH   B O    1 
HETATM 7094 O  O    . HOH   G 5 .   ? 46.791 -19.875 12.284  1.00 29.05 ?  340 HOH   B O    1 
HETATM 7095 O  O    . HOH   G 5 .   ? 28.857 -42.877 -12.308 1.00 35.85 ?  341 HOH   B O    1 
HETATM 7096 O  O    . HOH   G 5 .   ? 39.485 -23.642 -20.322 1.00 36.44 ?  342 HOH   B O    1 
HETATM 7097 O  O    . HOH   G 5 .   ? 37.039 -45.187 -9.643  1.00 36.79 ?  343 HOH   B O    1 
HETATM 7098 O  O    . HOH   G 5 .   ? 38.413 -12.243 -16.210 1.00 41.83 ?  344 HOH   B O    1 
HETATM 7099 O  O    . HOH   G 5 .   ? 32.976 -14.681 1.076   1.00 18.82 ?  345 HOH   B O    1 
HETATM 7100 O  O    . HOH   G 5 .   ? 39.777 -44.230 -11.157 1.00 39.31 ?  346 HOH   B O    1 
HETATM 7101 O  O    . HOH   G 5 .   ? 34.485 -10.317 7.672   1.00 23.60 ?  347 HOH   B O    1 
HETATM 7102 O  O    . HOH   G 5 .   ? 33.661 -9.575  -8.797  1.00 31.80 ?  348 HOH   B O    1 
HETATM 7103 O  O    . HOH   G 5 .   ? 38.538 -22.323 15.037  1.00 38.55 ?  349 HOH   B O    1 
HETATM 7104 O  O    . HOH   G 5 .   ? 40.404 -43.470 -9.058  1.00 26.30 ?  350 HOH   B O    1 
HETATM 7105 O  O    . HOH   G 5 .   ? 27.766 -26.567 -0.543  1.00 29.38 ?  351 HOH   B O    1 
HETATM 7106 O  O    . HOH   G 5 .   ? 55.601 -8.249  10.820  1.00 24.86 ?  352 HOH   B O    1 
HETATM 7107 O  O    . HOH   G 5 .   ? 62.486 -20.100 -4.822  1.00 42.23 ?  353 HOH   B O    1 
HETATM 7108 O  O    . HOH   G 5 .   ? 44.137 -37.335 -17.740 1.00 33.50 ?  354 HOH   B O    1 
HETATM 7109 O  O    . HOH   G 5 .   ? 36.096 -8.538  -9.661  1.00 34.72 ?  355 HOH   B O    1 
HETATM 7110 O  O    . HOH   G 5 .   ? 56.529 -7.258  3.109   1.00 26.06 ?  356 HOH   B O    1 
HETATM 7111 O  O    . HOH   G 5 .   ? 23.173 -23.620 6.821   1.00 34.62 ?  357 HOH   B O    1 
HETATM 7112 O  O    . HOH   G 5 .   ? 34.008 -7.799  11.490  1.00 38.60 ?  358 HOH   B O    1 
HETATM 7113 O  O    . HOH   G 5 .   ? 61.454 -19.884 1.723   1.00 36.05 ?  359 HOH   B O    1 
HETATM 7114 O  O    . HOH   G 5 .   ? 56.886 -21.541 -16.313 1.00 39.01 ?  360 HOH   B O    1 
HETATM 7115 O  O    . HOH   G 5 .   ? 40.214 -8.820  9.889   1.00 35.82 ?  361 HOH   B O    1 
HETATM 7116 O  O    . HOH   G 5 .   ? 27.144 -25.926 -11.348 1.00 33.48 ?  362 HOH   B O    1 
HETATM 7117 O  O    . HOH   G 5 .   ? 43.174 -12.693 -21.150 1.00 39.15 ?  363 HOH   B O    1 
HETATM 7118 O  O    . HOH   G 5 .   ? 54.158 -5.741  2.993   1.00 34.91 ?  364 HOH   B O    1 
HETATM 7119 O  O    . HOH   G 5 .   ? 40.160 -11.343 -13.941 1.00 31.14 ?  365 HOH   B O    1 
HETATM 7120 O  O    . HOH   G 5 .   ? 32.526 -23.591 14.069  1.00 38.22 ?  366 HOH   B O    1 
HETATM 7121 O  O    . HOH   G 5 .   ? 36.118 -8.676  8.961   1.00 35.11 ?  367 HOH   B O    1 
HETATM 7122 O  O    . HOH   G 5 .   ? 48.333 -26.451 8.841   1.00 39.49 ?  368 HOH   B O    1 
HETATM 7123 O  O    . HOH   G 5 .   ? 58.873 -10.390 9.219   1.00 38.33 ?  369 HOH   B O    1 
HETATM 7124 O  O    . HOH   G 5 .   ? 39.835 -7.026  7.880   1.00 38.53 ?  370 HOH   B O    1 
HETATM 7125 O  O    . HOH   G 5 .   ? 41.769 -10.064 -17.420 1.00 52.54 ?  371 HOH   B O    1 
HETATM 7126 O  O    . HOH   G 5 .   ? 55.987 -7.803  -0.589  1.00 33.29 ?  372 HOH   B O    1 
HETATM 7127 O  O    . HOH   G 5 .   ? 62.994 -12.400 6.918   1.00 36.80 ?  373 HOH   B O    1 
HETATM 7128 O  O    . HOH   G 5 .   ? 52.014 -12.894 13.367  1.00 29.59 ?  374 HOH   B O    1 
HETATM 7129 O  O    . HOH   G 5 .   ? 41.835 -6.766  -4.839  1.00 45.39 ?  375 HOH   B O    1 
HETATM 7130 O  O    . HOH   G 5 .   ? 38.010 -10.552 10.064  1.00 27.71 ?  376 HOH   B O    1 
HETATM 7131 O  O    . HOH   G 5 .   ? 42.637 -17.088 -23.080 1.00 41.82 ?  377 HOH   B O    1 
HETATM 7132 O  O    . HOH   G 5 .   ? 36.480 -22.815 13.298  1.00 25.71 ?  378 HOH   B O    1 
HETATM 7133 O  O    . HOH   G 5 .   ? 44.023 -5.594  -3.506  1.00 40.69 ?  379 HOH   B O    1 
HETATM 7134 O  O    . HOH   G 5 .   ? 40.112 -7.629  3.212   1.00 36.74 ?  380 HOH   B O    1 
HETATM 7135 O  O    . HOH   G 5 .   ? 39.620 -14.028 15.693  1.00 46.26 ?  381 HOH   B O    1 
HETATM 7136 O  O    . HOH   G 5 .   ? 52.806 -29.861 7.226   1.00 23.39 ?  382 HOH   B O    1 
HETATM 7137 O  O    . HOH   G 5 .   ? 60.457 -22.225 2.902   1.00 44.30 ?  383 HOH   B O    1 
HETATM 7138 O  O    . HOH   G 5 .   ? 25.844 -18.858 -11.844 1.00 38.00 ?  384 HOH   B O    1 
HETATM 7139 O  O    . HOH   G 5 .   ? 46.793 -5.334  2.898   1.00 38.07 ?  385 HOH   B O    1 
HETATM 7140 O  O    . HOH   G 5 .   ? 40.945 -9.772  15.797  1.00 44.01 ?  386 HOH   B O    1 
HETATM 7141 O  O    . HOH   G 5 .   ? 23.913 -20.841 -7.606  1.00 27.15 ?  387 HOH   B O    1 
HETATM 7142 O  O    . HOH   G 5 .   ? 35.382 -33.743 7.350   1.00 39.84 ?  388 HOH   B O    1 
HETATM 7143 O  O    . HOH   G 5 .   ? 35.235 -20.315 13.304  1.00 30.68 ?  389 HOH   B O    1 
HETATM 7144 O  O    . HOH   G 5 .   ? 40.678 -6.628  -0.828  1.00 25.34 ?  390 HOH   B O    1 
HETATM 7145 O  O    . HOH   G 5 .   ? 44.061 -31.711 -3.734  1.00 36.38 ?  391 HOH   B O    1 
HETATM 7146 O  O    . HOH   G 5 .   ? 27.945 -27.056 2.244   1.00 30.80 ?  392 HOH   B O    1 
HETATM 7147 O  O    . HOH   G 5 .   ? 26.593 -27.924 -13.436 1.00 33.06 ?  393 HOH   B O    1 
HETATM 7148 O  O    . HOH   G 5 .   ? 24.576 -20.597 -10.481 1.00 37.87 ?  394 HOH   B O    1 
HETATM 7149 O  O    . HOH   G 5 .   ? 50.602 -30.785 8.717   1.00 28.73 ?  395 HOH   B O    1 
HETATM 7150 O  O    . HOH   G 5 .   ? 26.830 -30.635 -12.592 1.00 27.95 ?  396 HOH   B O    1 
HETATM 7151 O  O    . HOH   G 5 .   ? 34.323 -33.475 9.660   1.00 35.98 ?  397 HOH   B O    1 
HETATM 7152 O  O    . HOH   G 5 .   ? 57.643 -6.514  -2.306  1.00 34.90 ?  398 HOH   B O    1 
HETATM 7153 O  O    . HOH   G 5 .   ? 45.663 -20.155 15.236  1.00 48.31 ?  399 HOH   B O    1 
HETATM 7154 O  O    . HOH   G 5 .   ? 40.836 -11.766 -22.278 1.00 37.33 ?  400 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   . VAL   A 3   ? 0.5642 0.5750 0.6937 -0.0087 -0.0307 0.0785  3   VAL   A N   
2    C  CA  . VAL   A 3   ? 0.5606 0.5713 0.6770 -0.0103 -0.0308 0.0764  3   VAL   A CA  
3    C  C   . VAL   A 3   ? 0.5380 0.5530 0.6173 -0.0189 -0.0337 0.0727  3   VAL   A C   
4    O  O   . VAL   A 3   ? 0.5429 0.5564 0.6355 -0.0177 -0.0351 0.0760  3   VAL   A O   
5    C  CB  . VAL   A 3   ? 0.5763 0.5836 0.7063 -0.0055 -0.0275 0.0784  3   VAL   A CB  
6    C  CG1 . VAL   A 3   ? 0.5821 0.5882 0.7151 -0.0036 -0.0266 0.0795  3   VAL   A CG1 
7    C  CG2 . VAL   A 3   ? 0.5810 0.5873 0.7153 -0.0036 -0.0260 0.0795  3   VAL   A CG2 
16   N  N   A ASN   A 4   ? 0.5143 0.5400 0.5609 -0.0335 -0.0326 0.0784  4   ASN   A N   
17   N  N   B ASN   A 4   ? 0.5307 0.5410 0.5827 -0.0143 -0.0340 0.0593  4   ASN   A N   
18   C  CA  A ASN   A 4   ? 0.4879 0.5240 0.4956 -0.0499 -0.0316 0.0820  4   ASN   A CA  
19   C  CA  B ASN   A 4   ? 0.5204 0.5259 0.5401 -0.0112 -0.0342 0.0447  4   ASN   A CA  
20   C  C   A ASN   A 4   ? 0.4513 0.5051 0.4506 -0.0669 -0.0248 0.0597  4   ASN   A C   
21   C  C   B ASN   A 4   ? 0.4964 0.5034 0.5065 -0.0131 -0.0260 0.0329  4   ASN   A C   
22   O  O   A ASN   A 4   ? 0.4532 0.5066 0.4452 -0.0667 -0.0281 0.0607  4   ASN   A O   
23   O  O   B ASN   A 4   ? 0.4994 0.5053 0.5045 -0.0127 -0.0264 0.0334  4   ASN   A O   
24   C  CB  A ASN   A 4   ? 0.4954 0.5257 0.4679 -0.0505 -0.0373 0.1068  4   ASN   A CB  
25   C  CB  B ASN   A 4   ? 0.5316 0.5315 0.5274 -0.0071 -0.0422 0.0419  4   ASN   A CB  
26   C  CG  A ASN   A 4   ? 0.5005 0.5254 0.4400 -0.0525 -0.0410 0.1300  4   ASN   A CG  
27   C  CG  B ASN   A 4   ? 0.5401 0.5354 0.5157 -0.0040 -0.0490 0.0401  4   ASN   A CG  
28   O  OD1 A ASN   A 4   ? 0.5032 0.5241 0.4271 -0.0535 -0.0438 0.1403  4   ASN   A OD1 
29   O  OD1 B ASN   A 4   ? 0.5431 0.5365 0.5111 -0.0036 -0.0510 0.0401  4   ASN   A OD1 
30   N  ND2 A ASN   A 4   ? 0.5014 0.5255 0.4316 -0.0527 -0.0420 0.1389  4   ASN   A ND2 
31   N  ND2 B ASN   A 4   ? 0.5432 0.5367 0.5130 -0.0020 -0.0516 0.0395  4   ASN   A ND2 
44   N  N   A SER   A 5   ? 0.4119 0.4818 0.4085 -0.0847 -0.0151 0.0362  5   SER   A N   
45   N  N   B SER   A 5   ? 0.4670 0.4770 0.4749 -0.0166 -0.0170 0.0211  5   SER   A N   
46   C  CA  A SER   A 5   ? 0.3725 0.4581 0.3686 -0.0985 -0.0055 0.0125  5   SER   A CA  
47   C  CA  B SER   A 5   ? 0.4356 0.4489 0.4435 -0.0214 -0.0056 0.0113  5   SER   A CA  
48   C  C   A SER   A 5   ? 0.3348 0.4293 0.3236 -0.1082 0.0033  0.0007  5   SER   A C   
49   C  C   B SER   A 5   ? 0.4001 0.4164 0.4070 -0.0275 0.0037  0.0056  5   SER   A C   
50   O  O   A SER   A 5   ? 0.3366 0.4355 0.3219 -0.1037 -0.0007 -0.0089 5   SER   A O   
51   O  O   B SER   A 5   ? 0.3998 0.4170 0.4115 -0.0264 0.0070  0.0036  5   SER   A O   
52   C  CB  A SER   A 5   ? 0.3752 0.4632 0.3781 -0.0995 -0.0018 0.0031  5   SER   A CB  
53   C  CB  B SER   A 5   ? 0.4381 0.4523 0.4486 -0.0211 -0.0024 0.0080  5   SER   A CB  
54   O  OG  A SER   A 5   ? 0.3784 0.4665 0.3857 -0.0987 0.0021  -0.0012 5   SER   A OG  
55   O  OG  B SER   A 5   ? 0.4394 0.4544 0.4511 -0.0212 -0.0005 0.0064  5   SER   A OG  
66   N  N   A PHE   A 6   ? 0.2939 0.3936 0.2751 -0.1211 0.0181  0.0056  6   PHE   A N   
67   N  N   B PHE   A 6   ? 0.3642 0.3822 0.3625 -0.0355 0.0098  0.0048  6   PHE   A N   
68   C  CA  A PHE   A 6   ? 0.2597 0.3583 0.2272 -0.1267 0.0255  0.0197  6   PHE   A CA  
69   C  CA  B PHE   A 6   ? 0.3289 0.3478 0.3180 -0.0435 0.0160  0.0071  6   PHE   A CA  
70   C  C   A PHE   A 6   ? 0.2554 0.3546 0.2124 -0.1288 0.0335  0.0151  6   PHE   A C   
71   C  C   B PHE   A 6   ? 0.3137 0.3362 0.3113 -0.0433 0.0251  0.0052  6   PHE   A C   
72   O  O   A PHE   A 6   ? 0.2574 0.3590 0.2349 -0.1330 0.0339  0.0189  6   PHE   A O   
73   O  O   B PHE   A 6   ? 0.3143 0.3371 0.3192 -0.0464 0.0265  0.0056  6   PHE   A O   
74   C  CB  A PHE   A 6   ? 0.2423 0.3296 0.2095 -0.1204 0.0197  0.0372  6   PHE   A CB  
75   C  CB  B PHE   A 6   ? 0.3113 0.3268 0.2810 -0.0494 0.0080  0.0097  6   PHE   A CB  
76   C  CG  A PHE   A 6   ? 0.2275 0.3061 0.1982 -0.1123 0.0159  0.0454  6   PHE   A CG  
77   C  CG  B PHE   A 6   ? 0.2946 0.3081 0.2486 -0.0548 0.0013  0.0114  6   PHE   A CG  
78   C  CD1 A PHE   A 6   ? 0.2200 0.2960 0.1894 -0.0999 0.0126  0.0460  6   PHE   A CD1 
79   C  CD1 B PHE   A 6   ? 0.2871 0.2992 0.2337 -0.0557 -0.0020 0.0128  6   PHE   A CD1 
80   C  CD2 A PHE   A 6   ? 0.2356 0.3036 0.2171 -0.0952 0.0158  0.0464  6   PHE   A CD2 
81   C  CD2 B PHE   A 6   ? 0.2904 0.3013 0.2394 -0.0541 -0.0016 0.0121  6   PHE   A CD2 
82   C  CE1 A PHE   A 6   ? 0.2174 0.2908 0.2019 -0.0942 0.0176  0.0472  6   PHE   A CE1 
83   C  CE1 B PHE   A 6   ? 0.2829 0.2942 0.2301 -0.0563 -0.0025 0.0137  6   PHE   A CE1 
84   C  CE2 A PHE   A 6   ? 0.2316 0.3000 0.2271 -0.0887 0.0172  0.0406  6   PHE   A CE2 
85   C  CE2 B PHE   A 6   ? 0.2853 0.2958 0.2338 -0.0556 -0.0034 0.0108  6   PHE   A CE2 
86   C  CZ  A PHE   A 6   ? 0.2225 0.2918 0.2139 -0.0924 0.0169  0.0383  6   PHE   A CZ  
87   C  CZ  B PHE   A 6   ? 0.2829 0.2934 0.2287 -0.0559 -0.0045 0.0110  6   PHE   A CZ  
106  N  N   A SER   A 7   ? 0.2490 0.3438 0.1925 -0.1267 0.0435  0.0153  7   SER   A N   
107  N  N   B SER   A 7   ? 0.2971 0.3230 0.2967 -0.0406 0.0286  0.0032  7   SER   A N   
108  C  CA  A SER   A 7   ? 0.2513 0.3363 0.1996 -0.1115 0.0378  -0.0026 7   SER   A CA  
109  C  CA  B SER   A 7   ? 0.2844 0.3118 0.2872 -0.0341 0.0312  -0.0022 7   SER   A CA  
110  C  C   A SER   A 7   ? 0.2394 0.3058 0.1732 -0.1083 0.0440  -0.0087 7   SER   A C   
111  C  C   B SER   A 7   ? 0.2672 0.2921 0.2616 -0.0352 0.0344  -0.0027 7   SER   A C   
112  O  O   A SER   A 7   ? 0.2520 0.2982 0.1751 -0.1160 0.0481  -0.0122 7   SER   A O   
113  O  O   B SER   A 7   ? 0.2709 0.2941 0.2552 -0.0338 0.0295  -0.0049 7   SER   A O   
114  C  CB  A SER   A 7   ? 0.2705 0.3561 0.2371 -0.0936 0.0352  -0.0024 7   SER   A CB  
115  C  CB  B SER   A 7   ? 0.2886 0.3184 0.3024 -0.0271 0.0316  -0.0023 7   SER   A CB  
116  O  OG  A SER   A 7   ? 0.2870 0.3685 0.2622 -0.0803 0.0348  -0.0033 7   SER   A OG  
117  O  OG  B SER   A 7   ? 0.2914 0.3218 0.3156 -0.0226 0.0305  0.0012  7   SER   A OG  
128  N  N   A GLY   A 8   ? 0.2176 0.2796 0.1590 -0.0947 0.0426  -0.0165 8   GLY   A N   
129  N  N   B GLY   A 8   ? 0.2484 0.2707 0.2396 -0.0359 0.0405  -0.0036 8   GLY   A N   
130  C  CA  A GLY   A 8   ? 0.2029 0.2541 0.1593 -0.0721 0.0359  -0.0232 8   GLY   A CA  
131  C  CA  B GLY   A 8   ? 0.2285 0.2480 0.2220 -0.0341 0.0409  -0.0022 8   GLY   A CA  
132  C  C   A GLY   A 8   ? 0.1806 0.2324 0.1553 -0.0504 0.0330  -0.0189 8   GLY   A C   
133  C  C   B GLY   A 8   ? 0.2063 0.2259 0.1959 -0.0321 0.0408  0.0010  8   GLY   A C   
134  O  O   A GLY   A 8   ? 0.1859 0.2360 0.1766 -0.0296 0.0361  -0.0331 8   GLY   A O   
135  O  O   B GLY   A 8   ? 0.2086 0.2273 0.2020 -0.0266 0.0448  -0.0091 8   GLY   A O   
142  N  N   A TYR   A 9   ? 0.1612 0.2164 0.1613 -0.0395 0.0324  -0.0039 9   TYR   A N   
143  N  N   B TYR   A 9   ? 0.1824 0.2052 0.1781 -0.0322 0.0300  0.0126  9   TYR   A N   
144  C  CA  A TYR   A 9   ? 0.1518 0.1993 0.1626 -0.0338 0.0248  0.0018  9   TYR   A CA  
145  C  CA  B TYR   A 9   ? 0.1697 0.1880 0.1623 -0.0285 0.0270  0.0190  9   TYR   A CA  
146  C  C   A TYR   A 9   ? 0.1527 0.1755 0.1576 -0.0269 0.0291  0.0175  9   TYR   A C   
147  C  C   B TYR   A 9   ? 0.1659 0.1676 0.1522 -0.0207 0.0276  0.0161  9   TYR   A C   
148  O  O   A TYR   A 9   ? 0.1766 0.1817 0.1676 -0.0193 0.0251  0.0136  9   TYR   A O   
149  O  O   B TYR   A 9   ? 0.1780 0.1763 0.1655 -0.0203 0.0183  0.0168  9   TYR   A O   
150  C  CB  A TYR   A 9   ? 0.1482 0.2125 0.1773 -0.0282 0.0194  -0.0022 9   TYR   A CB  
151  C  CB  B TYR   A 9   ? 0.1650 0.1963 0.1744 -0.0284 0.0200  0.0214  9   TYR   A CB  
152  C  CG  A TYR   A 9   ? 0.1468 0.2188 0.1847 -0.0252 0.0245  -0.0059 9   TYR   A CG  
153  C  CG  B TYR   A 9   ? 0.1612 0.2027 0.1746 -0.0313 0.0154  0.0201  9   TYR   A CG  
154  C  CD1 A TYR   A 9   ? 0.1499 0.2198 0.1926 -0.0333 0.0351  -0.0037 9   TYR   A CD1 
155  C  CD1 B TYR   A 9   ? 0.1633 0.2049 0.1764 -0.0359 0.0177  0.0198  9   TYR   A CD1 
156  C  CD2 A TYR   A 9   ? 0.1474 0.2211 0.1993 -0.0212 0.0189  0.0027  9   TYR   A CD2 
157  C  CD2 B TYR   A 9   ? 0.1588 0.2057 0.1725 -0.0293 0.0119  0.0237  9   TYR   A CD2 
158  C  CE1 A TYR   A 9   ? 0.1587 0.2240 0.2128 -0.0327 0.0364  -0.0087 9   TYR   A CE1 
159  C  CE1 B TYR   A 9   ? 0.1638 0.2071 0.1795 -0.0386 0.0245  0.0241  9   TYR   A CE1 
160  C  CE2 A TYR   A 9   ? 0.1520 0.2232 0.2094 -0.0211 0.0265  -0.0017 9   TYR   A CE2 
161  C  CE2 B TYR   A 9   ? 0.1581 0.2077 0.1713 -0.0292 0.0193  0.0247  9   TYR   A CE2 
162  C  CZ  A TYR   A 9   ? 0.1558 0.2292 0.2265 -0.0374 0.0462  -0.0065 9   TYR   A CZ  
163  C  CZ  B TYR   A 9   ? 0.1585 0.2089 0.1780 -0.0363 0.0334  0.0260  9   TYR   A CZ  
164  O  OH  A TYR   A 9   ? 0.1657 0.2382 0.2482 -0.0521 0.0483  -0.0112 9   TYR   A OH  
165  O  OH  B TYR   A 9   ? 0.1564 0.2140 0.1823 -0.0426 0.0409  0.0311  9   TYR   A OH  
184  N  N   A LEU   A 10  ? 0.1527 0.1610 0.1575 -0.0271 0.0210  0.0204  10  LEU   A N   
185  N  N   B LEU   A 10  ? 0.1623 0.1512 0.1422 -0.0179 0.0257  0.0095  10  LEU   A N   
186  C  CA  A LEU   A 10  ? 0.1397 0.1510 0.1628 -0.0278 0.0161  0.0219  10  LEU   A CA  
187  C  CA  B LEU   A 10  ? 0.1554 0.1467 0.1493 -0.0163 0.0168  0.0063  10  LEU   A CA  
188  C  C   A LEU   A 10  ? 0.1356 0.1448 0.1768 -0.0230 0.0178  0.0288  10  LEU   A C   
189  C  C   B LEU   A 10  ? 0.1558 0.1411 0.1443 -0.0195 0.0135  0.0147  10  LEU   A C   
190  O  O   A LEU   A 10  ? 0.1387 0.1512 0.1915 -0.0115 0.0343  0.0372  10  LEU   A O   
191  O  O   B LEU   A 10  ? 0.1562 0.1369 0.1492 -0.0209 0.0265  0.0259  10  LEU   A O   
192  C  CB  A LEU   A 10  ? 0.1400 0.1571 0.1883 -0.0203 0.0105  0.0284  10  LEU   A CB  
193  C  CB  B LEU   A 10  ? 0.1532 0.1482 0.1579 -0.0166 0.0050  0.0018  10  LEU   A CB  
194  C  CG  A LEU   A 10  ? 0.1645 0.1686 0.2342 -0.0073 -0.0082 0.0233  10  LEU   A CG  
195  C  CG  B LEU   A 10  ? 0.1580 0.1596 0.1768 -0.0086 -0.0067 0.0014  10  LEU   A CG  
196  C  CD1 A LEU   A 10  ? 0.1795 0.1710 0.2564 -0.0115 0.0010  0.0162  10  LEU   A CD1 
197  C  CD1 B LEU   A 10  ? 0.1687 0.1692 0.2006 -0.0149 -0.0028 0.0009  10  LEU   A CD1 
198  C  CD2 A LEU   A 10  ? 0.1820 0.1866 0.2484 0.0034  0.0025  0.0070  10  LEU   A CD2 
199  C  CD2 B LEU   A 10  ? 0.1699 0.1687 0.1947 0.0008  -0.0152 -0.0003 10  LEU   A CD2 
222  N  N   A LYS   A 11  ? 0.1421 0.1429 0.1745 -0.0244 0.0222  0.0310  11  LYS   A N   
223  N  N   B LYS   A 11  ? 0.1623 0.1421 0.1404 -0.0217 0.0060  0.0116  11  LYS   A N   
224  C  CA  A LYS   A 11  ? 0.1431 0.1418 0.1772 -0.0316 0.0183  0.0310  11  LYS   A CA  
225  C  CA  B LYS   A 11  ? 0.1637 0.1415 0.1351 -0.0203 0.0062  0.0116  11  LYS   A CA  
226  C  C   A LYS   A 11  ? 0.1363 0.1430 0.1802 -0.0250 0.0230  0.0156  11  LYS   A C   
227  C  C   B LYS   A 11  ? 0.1503 0.1322 0.1323 -0.0202 0.0117  0.0027  11  LYS   A C   
228  O  O   A LYS   A 11  ? 0.1463 0.1657 0.2082 -0.0431 0.0253  -0.0008 11  LYS   A O   
229  O  O   B LYS   A 11  ? 0.1476 0.1311 0.1446 -0.0207 0.0177  -0.0135 11  LYS   A O   
230  C  CB  A LYS   A 11  ? 0.1559 0.1436 0.1815 -0.0338 0.0132  0.0254  11  LYS   A CB  
231  C  CB  B LYS   A 11  ? 0.1770 0.1400 0.1374 -0.0208 -0.0011 0.0072  11  LYS   A CB  
232  C  CG  A LYS   A 11  ? 0.1712 0.1425 0.1850 -0.0336 0.0156  0.0290  11  LYS   A CG  
233  C  CG  B LYS   A 11  ? 0.1874 0.1420 0.1328 -0.0255 -0.0036 0.0146  11  LYS   A CG  
234  C  CD  A LYS   A 11  ? 0.1913 0.1486 0.1916 -0.0264 0.0122  0.0362  11  LYS   A CD  
235  C  CD  B LYS   A 11  ? 0.1981 0.1514 0.1333 -0.0261 -0.0058 0.0191  11  LYS   A CD  
236  C  CE  A LYS   A 11  ? 0.1975 0.1431 0.1931 -0.0204 0.0079  0.0392  11  LYS   A CE  
237  C  CE  B LYS   A 11  ? 0.2040 0.1562 0.1323 -0.0220 -0.0038 0.0236  11  LYS   A CE  
238  N  NZ  A LYS   A 11  ? 0.1956 0.1413 0.1990 -0.0111 -0.0007 0.0252  11  LYS   A NZ  
239  N  NZ  B LYS   A 11  ? 0.2045 0.1581 0.1281 -0.0177 -0.0004 0.0336  11  LYS   A NZ  
266  N  N   A LEU   A 12  ? 0.1306 0.1355 0.1622 -0.0256 0.0199  0.0136  12  LEU   A N   
267  N  N   B LEU   A 12  ? 0.1409 0.1374 0.1330 -0.0070 0.0114  0.0004  12  LEU   A N   
268  C  CA  A LEU   A 12  ? 0.1322 0.1432 0.1659 -0.0165 0.0105  0.0159  12  LEU   A CA  
269  C  CA  B LEU   A 12  ? 0.1360 0.1428 0.1318 -0.0035 0.0157  -0.0010 12  LEU   A CA  
270  C  C   A LEU   A 12  ? 0.1373 0.1345 0.1686 -0.0222 0.0108  0.0255  12  LEU   A C   
271  C  C   B LEU   A 12  ? 0.1327 0.1417 0.1376 -0.0024 0.0286  0.0017  12  LEU   A C   
272  O  O   A LEU   A 12  ? 0.1414 0.1361 0.1709 -0.0158 0.0159  0.0094  12  LEU   A O   
273  O  O   B LEU   A 12  ? 0.1403 0.1424 0.1358 0.0037  0.0232  -0.0007 12  LEU   A O   
274  C  CB  A LEU   A 12  ? 0.1440 0.1408 0.1609 -0.0125 0.0085  0.0128  12  LEU   A CB  
275  C  CB  B LEU   A 12  ? 0.1417 0.1504 0.1502 -0.0035 0.0164  0.0015  12  LEU   A CB  
276  C  CG  A LEU   A 12  ? 0.1485 0.1493 0.1767 -0.0056 0.0192  0.0189  12  LEU   A CG  
277  C  CG  B LEU   A 12  ? 0.1435 0.1540 0.1759 0.0008  0.0204  0.0027  12  LEU   A CG  
278  C  CD1 A LEU   A 12  ? 0.1545 0.1538 0.1876 0.0088  0.0249  0.0345  12  LEU   A CD1 
279  C  CD1 B LEU   A 12  ? 0.1477 0.1643 0.1833 0.0105  0.0293  0.0050  12  LEU   A CD1 
280  C  CD2 A LEU   A 12  ? 0.1549 0.1575 0.1924 -0.0038 0.0125  0.0151  12  LEU   A CD2 
281  C  CD2 B LEU   A 12  ? 0.1422 0.1573 0.1882 -0.0006 0.0147  -0.0099 12  LEU   A CD2 
304  N  N   A THR   A 13  ? 0.1363 0.1325 0.1858 -0.0193 0.0054  0.0174  13  THR   A N   
305  N  N   B THR   A 13  ? 0.1291 0.1394 0.1532 -0.0065 0.0272  0.0104  13  THR   A N   
306  C  CA  A THR   A 13  ? 0.1359 0.1385 0.2002 -0.0146 0.0130  0.0181  13  THR   A CA  
307  C  CA  B THR   A 13  ? 0.1305 0.1424 0.1684 -0.0120 0.0269  0.0149  13  THR   A CA  
308  C  C   A THR   A 13  ? 0.1363 0.1421 0.2094 -0.0177 0.0052  0.0375  13  THR   A C   
309  C  C   B THR   A 13  ? 0.1385 0.1485 0.1799 -0.0167 0.0248  0.0229  13  THR   A C   
310  O  O   A THR   A 13  ? 0.1382 0.1467 0.2056 -0.0126 0.0032  0.0376  13  THR   A O   
311  O  O   B THR   A 13  ? 0.1497 0.1521 0.1852 -0.0202 0.0169  0.0283  13  THR   A O   
312  C  CB  A THR   A 13  ? 0.1389 0.1505 0.2145 -0.0067 0.0169  0.0212  13  THR   A CB  
313  C  CB  B THR   A 13  ? 0.1263 0.1475 0.1751 -0.0082 0.0317  0.0237  13  THR   A CB  
314  O  OG1 A THR   A 13  ? 0.1451 0.1467 0.2202 -0.0096 0.0029  0.0261  13  THR   A OG1 
315  O  OG1 B THR   A 13  ? 0.1112 0.1492 0.1887 -0.0124 0.0422  0.0353  13  THR   A OG1 
316  C  CG2 A THR   A 13  ? 0.1494 0.1658 0.2306 -0.0091 0.0256  0.0125  13  THR   A CG2 
317  C  CG2 B THR   A 13  ? 0.1268 0.1525 0.1762 0.0013  0.0318  0.0214  13  THR   A CG2 
332  N  N   A ASP   A 14  ? 0.1406 0.1453 0.2296 -0.0252 0.0028  0.0545  14  ASP   A N   
333  N  N   B ASP   A 14  ? 0.1391 0.1545 0.1947 -0.0201 0.0186  0.0309  14  ASP   A N   
334  C  CA  A ASP   A 14  ? 0.1472 0.1635 0.2450 -0.0187 -0.0050 0.0741  14  ASP   A CA  
335  C  CA  B ASP   A 14  ? 0.1448 0.1652 0.2117 -0.0183 0.0034  0.0464  14  ASP   A CA  
336  C  C   A ASP   A 14  ? 0.1539 0.1704 0.2286 -0.0237 -0.0069 0.0664  14  ASP   A C   
337  C  C   B ASP   A 14  ? 0.1389 0.1615 0.1920 -0.0152 -0.0091 0.0576  14  ASP   A C   
338  O  O   A ASP   A 14  ? 0.1598 0.1792 0.2347 -0.0353 -0.0135 0.0679  14  ASP   A O   
339  O  O   B ASP   A 14  ? 0.1376 0.1637 0.1908 -0.0099 -0.0197 0.0644  14  ASP   A O   
340  C  CB  A ASP   A 14  ? 0.1589 0.1891 0.2904 -0.0264 -0.0022 0.0926  14  ASP   A CB  
341  C  CB  B ASP   A 14  ? 0.1534 0.1808 0.2479 -0.0192 -0.0028 0.0500  14  ASP   A CB  
342  C  CG  A ASP   A 14  ? 0.1837 0.2414 0.3613 -0.0240 -0.0092 0.0800  14  ASP   A CG  
343  C  CG  B ASP   A 14  ? 0.1584 0.2066 0.2873 -0.0230 -0.0069 0.0443  14  ASP   A CG  
344  O  OD1 A ASP   A 14  ? 0.2012 0.2573 0.3831 -0.0179 -0.0248 0.0791  14  ASP   A OD1 
345  O  OD1 B ASP   A 14  ? 0.1629 0.2095 0.3013 -0.0325 -0.0027 0.0434  14  ASP   A OD1 
346  O  OD2 A ASP   A 14  ? 0.2006 0.2794 0.3994 -0.0117 -0.0179 0.0602  14  ASP   A OD2 
347  O  OD2 B ASP   A 14  ? 0.1609 0.2308 0.3078 -0.0122 -0.0168 0.0361  14  ASP   A OD2 
356  N  N   A ASN   A 15  ? 0.1386 0.1566 0.2216 -0.0220 -0.0035 0.0607  15  ASN   A N   
357  N  N   B ASN   A 15  ? 0.1248 0.1490 0.1850 -0.0179 -0.0105 0.0639  15  ASN   A N   
358  C  CA  A ASN   A 15  ? 0.1418 0.1570 0.2241 -0.0234 -0.0150 0.0495  15  ASN   A CA  
359  C  CA  B ASN   A 15  ? 0.1263 0.1469 0.1916 -0.0157 -0.0133 0.0537  15  ASN   A CA  
360  C  C   A ASN   A 15  ? 0.1389 0.1519 0.2165 -0.0283 -0.0081 0.0410  15  ASN   A C   
361  C  C   B ASN   A 15  ? 0.1273 0.1455 0.2004 -0.0159 0.0001  0.0461  15  ASN   A C   
362  O  O   A ASN   A 15  ? 0.1339 0.1516 0.2010 -0.0303 -0.0045 0.0430  15  ASN   A O   
363  O  O   B ASN   A 15  ? 0.1325 0.1494 0.2037 -0.0151 0.0126  0.0449  15  ASN   A O   
364  C  CB  A ASN   A 15  ? 0.1405 0.1575 0.2257 -0.0195 -0.0078 0.0485  15  ASN   A CB  
365  C  CB  B ASN   A 15  ? 0.1265 0.1460 0.1882 -0.0177 -0.0102 0.0498  15  ASN   A CB  
366  C  CG  A ASN   A 15  ? 0.1444 0.1591 0.2417 -0.0170 -0.0005 0.0324  15  ASN   A CG  
367  C  CG  B ASN   A 15  ? 0.1284 0.1528 0.1942 -0.0139 -0.0013 0.0386  15  ASN   A CG  
368  O  OD1 A ASN   A 15  ? 0.1584 0.1662 0.2585 -0.0301 -0.0003 0.0358  15  ASN   A OD1 
369  O  OD1 B ASN   A 15  ? 0.1353 0.1586 0.2029 -0.0210 -0.0028 0.0390  15  ASN   A OD1 
370  N  ND2 A ASN   A 15  ? 0.1441 0.1562 0.2289 -0.0144 0.0094  0.0193  15  ASN   A ND2 
371  N  ND2 B ASN   A 15  ? 0.1263 0.1512 0.1849 -0.0086 0.0058  0.0321  15  ASN   A ND2 
384  N  N   A VAL   A 16  ? 0.1365 0.1476 0.2066 -0.0201 0.0034  0.0322  16  VAL   A N   
385  N  N   B VAL   A 16  ? 0.1213 0.1410 0.1877 -0.0119 0.0048  0.0462  16  VAL   A N   
386  C  CA  A VAL   A 16  ? 0.1333 0.1483 0.2010 -0.0162 0.0101  0.0368  16  VAL   A CA  
387  C  CA  B VAL   A 16  ? 0.1281 0.1467 0.1773 -0.0116 0.0143  0.0432  16  VAL   A CA  
388  C  C   A VAL   A 16  ? 0.1332 0.1430 0.1860 -0.0193 0.0024  0.0370  16  VAL   A C   
389  C  C   B VAL   A 16  ? 0.1251 0.1529 0.1685 -0.0137 0.0085  0.0387  16  VAL   A C   
390  O  O   A VAL   A 16  ? 0.1232 0.1386 0.2000 -0.0176 0.0113  0.0216  16  VAL   A O   
391  O  O   B VAL   A 16  ? 0.1240 0.1485 0.1733 -0.0119 0.0190  0.0378  16  VAL   A O   
392  C  CB  A VAL   A 16  ? 0.1364 0.1713 0.2047 0.0019  0.0279  0.0518  16  VAL   A CB  
393  C  CB  B VAL   A 16  ? 0.1436 0.1596 0.1786 0.0010  0.0269  0.0383  16  VAL   A CB  
394  C  CG1 A VAL   A 16  ? 0.1444 0.1874 0.2146 0.0081  0.0338  0.0515  16  VAL   A CG1 
395  C  CG1 B VAL   A 16  ? 0.1532 0.1675 0.1894 0.0086  0.0253  0.0332  16  VAL   A CG1 
396  C  CG2 A VAL   A 16  ? 0.1415 0.1826 0.2141 0.0062  0.0423  0.0541  16  VAL   A CG2 
397  C  CG2 B VAL   A 16  ? 0.1470 0.1674 0.1894 0.0033  0.0356  0.0338  16  VAL   A CG2 
416  N  N   A TYR   A 17  ? 0.1290 0.1353 0.1925 -0.0198 0.0098  0.0421  17  TYR   A N   
417  N  N   B TYR   A 17  ? 0.1230 0.1538 0.1664 -0.0166 0.0014  0.0340  17  TYR   A N   
418  C  CA  A TYR   A 17  ? 0.1373 0.1421 0.1721 -0.0266 0.0040  0.0397  17  TYR   A CA  
419  C  CA  B TYR   A 17  ? 0.1256 0.1550 0.1489 -0.0183 -0.0008 0.0344  17  TYR   A CA  
420  C  C   A TYR   A 17  ? 0.1425 0.1370 0.1720 -0.0231 0.0123  0.0240  17  TYR   A C   
421  C  C   B TYR   A 17  ? 0.1258 0.1533 0.1361 -0.0172 0.0120  0.0298  17  TYR   A C   
422  O  O   A TYR   A 17  ? 0.1424 0.1271 0.1581 -0.0222 0.0171  0.0227  17  TYR   A O   
423  O  O   B TYR   A 17  ? 0.1243 0.1550 0.1334 -0.0193 0.0142  0.0241  17  TYR   A O   
424  C  CB  A TYR   A 17  ? 0.1575 0.1496 0.1774 -0.0362 -0.0057 0.0475  17  TYR   A CB  
425  C  CB  B TYR   A 17  ? 0.1407 0.1591 0.1604 -0.0193 -0.0040 0.0351  17  TYR   A CB  
426  C  CG  A TYR   A 17  ? 0.1791 0.1659 0.1910 -0.0442 -0.0257 0.0461  17  TYR   A CG  
427  C  CG  B TYR   A 17  ? 0.1539 0.1681 0.1713 -0.0184 -0.0067 0.0335  17  TYR   A CG  
428  C  CD1 A TYR   A 17  ? 0.1899 0.1752 0.2050 -0.0374 -0.0287 0.0449  17  TYR   A CD1 
429  C  CD1 B TYR   A 17  ? 0.1632 0.1711 0.1856 -0.0112 -0.0041 0.0373  17  TYR   A CD1 
430  C  CD2 A TYR   A 17  ? 0.1864 0.1720 0.1780 -0.0545 -0.0287 0.0542  17  TYR   A CD2 
431  C  CD2 B TYR   A 17  ? 0.1583 0.1745 0.1697 -0.0171 -0.0030 0.0320  17  TYR   A CD2 
432  C  CE1 A TYR   A 17  ? 0.1879 0.1728 0.2150 -0.0440 -0.0353 0.0470  17  TYR   A CE1 
433  C  CE1 B TYR   A 17  ? 0.1683 0.1732 0.1935 -0.0089 -0.0008 0.0406  17  TYR   A CE1 
434  C  CE2 A TYR   A 17  ? 0.1934 0.1755 0.1973 -0.0529 -0.0386 0.0416  17  TYR   A CE2 
435  C  CE2 B TYR   A 17  ? 0.1634 0.1757 0.1774 -0.0105 -0.0032 0.0329  17  TYR   A CE2 
436  C  CZ  A TYR   A 17  ? 0.1926 0.1686 0.2059 -0.0515 -0.0398 0.0471  17  TYR   A CZ  
437  C  CZ  B TYR   A 17  ? 0.1656 0.1743 0.1906 -0.0054 -0.0049 0.0390  17  TYR   A CZ  
438  O  OH  A TYR   A 17  ? 0.2045 0.1666 0.2079 -0.0449 -0.0347 0.0427  17  TYR   A OH  
439  O  OH  B TYR   A 17  ? 0.1627 0.1750 0.1996 0.0029  -0.0029 0.0417  17  TYR   A OH  
458  N  N   A ILE   A 18  ? 0.1454 0.1439 0.1771 -0.0197 0.0188  0.0297  18  ILE   A N   
459  N  N   B ILE   A 18  ? 0.1222 0.1499 0.1308 -0.0156 0.0187  0.0343  18  ILE   A N   
460  C  CA  A ILE   A 18  ? 0.1426 0.1428 0.1687 -0.0136 0.0180  0.0234  18  ILE   A CA  
461  C  CA  B ILE   A 18  ? 0.1228 0.1459 0.1253 -0.0091 0.0173  0.0300  18  ILE   A CA  
462  C  C   A ILE   A 18  ? 0.1490 0.1508 0.1828 -0.0287 0.0181  0.0224  18  ILE   A C   
463  C  C   B ILE   A 18  ? 0.1262 0.1529 0.1194 -0.0140 0.0116  0.0295  18  ILE   A C   
464  O  O   A ILE   A 18  ? 0.1498 0.1613 0.1901 -0.0331 0.0271  0.0262  18  ILE   A O   
465  O  O   B ILE   A 18  ? 0.1237 0.1569 0.1335 -0.0125 0.0173  0.0291  18  ILE   A O   
466  C  CB  A ILE   A 18  ? 0.1480 0.1427 0.1521 0.0016  0.0183  0.0270  18  ILE   A CB  
467  C  CB  B ILE   A 18  ? 0.1320 0.1405 0.1232 0.0015  0.0341  0.0197  18  ILE   A CB  
468  C  CG1 A ILE   A 18  ? 0.1581 0.1497 0.1425 0.0190  0.0177  0.0330  18  ILE   A CG1 
469  C  CG1 B ILE   A 18  ? 0.1486 0.1499 0.1388 -0.0036 0.0450  0.0163  18  ILE   A CG1 
470  C  CG2 A ILE   A 18  ? 0.1431 0.1348 0.1545 0.0064  0.0103  0.0102  18  ILE   A CG2 
471  C  CG2 B ILE   A 18  ? 0.1366 0.1420 0.1273 -0.0007 0.0360  0.0200  18  ILE   A CG2 
472  C  CD1 A ILE   A 18  ? 0.1760 0.1647 0.1491 0.0321  0.0201  0.0358  18  ILE   A CD1 
473  C  CD1 B ILE   A 18  ? 0.1605 0.1606 0.1519 0.0023  0.0514  0.0063  18  ILE   A CD1 
496  N  N   A LYS   A 19  ? 0.1513 0.1535 0.1698 -0.0236 0.0250  0.0181  19  LYS   A N   
497  N  N   B LYS   A 19  ? 0.1321 0.1557 0.1138 -0.0103 0.0280  0.0181  19  LYS   A N   
498  C  CA  A LYS   A 19  ? 0.1649 0.1660 0.1734 -0.0192 0.0300  0.0188  19  LYS   A CA  
499  C  CA  B LYS   A 19  ? 0.1519 0.1707 0.1326 -0.0069 0.0384  0.0086  19  LYS   A CA  
500  C  C   A LYS   A 19  ? 0.1523 0.1585 0.1947 -0.0145 0.0279  0.0315  19  LYS   A C   
501  C  C   B LYS   A 19  ? 0.1592 0.1716 0.1412 -0.0008 0.0403  0.0089  19  LYS   A C   
502  O  O   A LYS   A 19  ? 0.1487 0.1528 0.1872 -0.0103 0.0237  0.0345  19  LYS   A O   
503  O  O   B LYS   A 19  ? 0.1590 0.1688 0.1353 -0.0096 0.0360  0.0086  19  LYS   A O   
504  C  CB  A LYS   A 19  ? 0.1894 0.1883 0.1780 -0.0274 0.0379  0.0157  19  LYS   A CB  
505  C  CB  B LYS   A 19  ? 0.1632 0.1857 0.1485 -0.0092 0.0505  -0.0050 19  LYS   A CB  
506  C  CG  A LYS   A 19  ? 0.2208 0.2073 0.1891 -0.0279 0.0403  0.0061  19  LYS   A CG  
507  C  CG  B LYS   A 19  ? 0.1855 0.2008 0.1598 -0.0043 0.0558  -0.0157 19  LYS   A CG  
508  C  CD  A LYS   A 19  ? 0.2454 0.2227 0.2052 -0.0305 0.0461  -0.0012 19  LYS   A CD  
509  C  CD  B LYS   A 19  ? 0.2055 0.2117 0.1749 -0.0041 0.0591  -0.0157 19  LYS   A CD  
510  C  CE  A LYS   A 19  ? 0.2634 0.2310 0.2230 -0.0340 0.0528  -0.0082 19  LYS   A CE  
511  C  CE  B LYS   A 19  ? 0.2176 0.2200 0.1866 -0.0068 0.0643  -0.0146 19  LYS   A CE  
512  N  NZ  A LYS   A 19  ? 0.2727 0.2317 0.2222 -0.0394 0.0635  -0.0196 19  LYS   A NZ  
513  N  NZ  B LYS   A 19  ? 0.2240 0.2210 0.1941 -0.0069 0.0685  -0.0208 19  LYS   A NZ  
540  N  N   A ASN   A 20  ? 0.1521 0.1652 0.2162 -0.0183 0.0316  0.0464  20  ASN   A N   
541  N  N   B ASN   A 20  ? 0.1702 0.1833 0.1705 0.0089  0.0388  0.0074  20  ASN   A N   
542  C  CA  A ASN   A 20  ? 0.1609 0.1797 0.2383 -0.0004 0.0504  0.0430  20  ASN   A CA  
543  C  CA  B ASN   A 20  ? 0.1830 0.1970 0.2034 0.0171  0.0399  0.0083  20  ASN   A CA  
544  C  C   A ASN   A 20  ? 0.1825 0.1803 0.2491 -0.0075 0.0661  0.0304  20  ASN   A C   
545  C  C   B ASN   A 20  ? 0.1916 0.1904 0.2088 0.0134  0.0553  0.0056  20  ASN   A C   
546  O  O   A ASN   A 20  ? 0.2029 0.1832 0.2495 -0.0186 0.0684  0.0162  20  ASN   A O   
547  O  O   B ASN   A 20  ? 0.1994 0.1868 0.2104 0.0144  0.0592  0.0036  20  ASN   A O   
548  C  CB  A ASN   A 20  ? 0.1640 0.1947 0.2538 0.0167  0.0541  0.0575  20  ASN   A CB  
549  C  CB  B ASN   A 20  ? 0.1918 0.2163 0.2272 0.0276  0.0270  0.0114  20  ASN   A CB  
550  C  CG  A ASN   A 20  ? 0.1687 0.2032 0.2720 0.0333  0.0618  0.0696  20  ASN   A CG  
551  C  CG  B ASN   A 20  ? 0.2012 0.2314 0.2510 0.0359  0.0143  0.0153  20  ASN   A CG  
552  O  OD1 A ASN   A 20  ? 0.1934 0.2153 0.3035 0.0477  0.0738  0.0502  20  ASN   A OD1 
553  O  OD1 B ASN   A 20  ? 0.2126 0.2398 0.2668 0.0381  0.0114  0.0095  20  ASN   A OD1 
554  N  ND2 A ASN   A 20  ? 0.1593 0.1988 0.2819 0.0297  0.0421  0.0871  20  ASN   A ND2 
555  N  ND2 B ASN   A 20  ? 0.2023 0.2350 0.2613 0.0385  0.0017  0.0227  20  ASN   A ND2 
568  N  N   A ALA   A 21  ? 0.1845 0.1811 0.2558 -0.0039 0.0606  0.0234  21  ALA   A N   
569  N  N   B ALA   A 21  ? 0.1919 0.1866 0.2161 0.0102  0.0506  0.0049  21  ALA   A N   
570  C  CA  A ALA   A 21  ? 0.1911 0.1795 0.2486 -0.0054 0.0544  0.0294  21  ALA   A CA  
571  C  CA  B ALA   A 21  ? 0.1933 0.1816 0.2149 0.0032  0.0507  0.0122  21  ALA   A CA  
572  C  C   A ALA   A 21  ? 0.1795 0.1786 0.2400 -0.0033 0.0500  0.0364  21  ALA   A C   
573  C  C   B ALA   A 21  ? 0.1820 0.1734 0.2047 0.0011  0.0583  0.0181  21  ALA   A C   
574  O  O   A ALA   A 21  ? 0.1755 0.1824 0.2396 0.0016  0.0397  0.0397  21  ALA   A O   
575  O  O   B ALA   A 21  ? 0.1750 0.1663 0.2161 0.0081  0.0594  0.0105  21  ALA   A O   
576  C  CB  A ALA   A 21  ? 0.2026 0.1821 0.2511 -0.0057 0.0518  0.0278  21  ALA   A CB  
577  C  CB  B ALA   A 21  ? 0.1990 0.1815 0.2279 0.0035  0.0396  0.0119  21  ALA   A CB  
588  N  N   A ASP   A 22  ? 0.1783 0.1759 0.2483 -0.0101 0.0446  0.0392  22  ASP   A N   
589  N  N   B ASP   A 22  ? 0.1818 0.1714 0.1981 -0.0064 0.0574  0.0275  22  ASP   A N   
590  C  CA  A ASP   A 22  ? 0.1827 0.1819 0.2471 -0.0075 0.0368  0.0325  22  ASP   A CA  
591  C  CA  B ASP   A 22  ? 0.1841 0.1677 0.1955 -0.0096 0.0491  0.0261  22  ASP   A CA  
592  C  C   A ASP   A 22  ? 0.1718 0.1820 0.2033 -0.0069 0.0353  0.0268  22  ASP   A C   
593  C  C   B ASP   A 22  ? 0.1669 0.1691 0.1754 -0.0226 0.0528  0.0128  22  ASP   A C   
594  O  O   A ASP   A 22  ? 0.1762 0.1891 0.2084 -0.0095 0.0326  0.0154  22  ASP   A O   
595  O  O   B ASP   A 22  ? 0.1584 0.1738 0.1756 -0.0304 0.0508  -0.0099 22  ASP   A O   
596  C  CB  A ASP   A 22  ? 0.2026 0.1875 0.2981 -0.0132 0.0205  0.0326  22  ASP   A CB  
597  C  CB  B ASP   A 22  ? 0.2004 0.1659 0.2208 -0.0002 0.0410  0.0244  22  ASP   A CB  
598  C  CG  A ASP   A 22  ? 0.2230 0.1997 0.3539 -0.0154 -0.0014 0.0453  22  ASP   A CG  
599  C  CG  B ASP   A 22  ? 0.2128 0.1642 0.2365 0.0039  0.0334  0.0261  22  ASP   A CG  
600  O  OD1 A ASP   A 22  ? 0.2227 0.2014 0.3836 -0.0311 -0.0122 0.0579  22  ASP   A OD1 
601  O  OD1 B ASP   A 22  ? 0.2138 0.1593 0.2321 0.0039  0.0367  0.0232  22  ASP   A OD1 
602  O  OD2 A ASP   A 22  ? 0.2454 0.2101 0.3806 -0.0042 -0.0002 0.0363  22  ASP   A OD2 
603  O  OD2 B ASP   A 22  ? 0.2190 0.1687 0.2500 0.0047  0.0358  0.0252  22  ASP   A OD2 
612  N  N   A ILE   A 23  ? 0.1695 0.1782 0.1858 -0.0059 0.0329  0.0213  23  ILE   A N   
613  N  N   B ILE   A 23  ? 0.1626 0.1670 0.1648 -0.0241 0.0485  0.0170  23  ILE   A N   
614  C  CA  A ILE   A 23  ? 0.1683 0.1739 0.1753 -0.0109 0.0261  0.0205  23  ILE   A CA  
615  C  CA  B ILE   A 23  ? 0.1598 0.1681 0.1455 -0.0251 0.0349  0.0130  23  ILE   A CA  
616  C  C   A ILE   A 23  ? 0.1688 0.1812 0.1773 -0.0117 0.0445  0.0143  23  ILE   A C   
617  C  C   B ILE   A 23  ? 0.1685 0.1747 0.1542 -0.0389 0.0348  -0.0018 23  ILE   A C   
618  O  O   A ILE   A 23  ? 0.1776 0.1880 0.1795 -0.0063 0.0340  0.0059  23  ILE   A O   
619  O  O   B ILE   A 23  ? 0.1694 0.1717 0.1629 -0.0407 0.0310  0.0012  23  ILE   A O   
620  C  CB  A ILE   A 23  ? 0.1787 0.1740 0.1619 -0.0079 0.0238  0.0169  23  ILE   A CB  
621  C  CB  B ILE   A 23  ? 0.1558 0.1626 0.1364 -0.0144 0.0203  0.0174  23  ILE   A CB  
622  C  CG1 A ILE   A 23  ? 0.1835 0.1694 0.1612 -0.0040 0.0236  0.0102  23  ILE   A CG1 
623  C  CG1 B ILE   A 23  ? 0.1561 0.1599 0.1285 -0.0128 0.0102  0.0112  23  ILE   A CG1 
624  C  CG2 A ILE   A 23  ? 0.1823 0.1796 0.1614 -0.0059 0.0347  0.0230  23  ILE   A CG2 
625  C  CG2 B ILE   A 23  ? 0.1535 0.1614 0.1350 -0.0107 0.0154  0.0192  23  ILE   A CG2 
626  C  CD1 A ILE   A 23  ? 0.1876 0.1678 0.1587 -0.0029 0.0175  0.0012  23  ILE   A CD1 
627  C  CD1 B ILE   A 23  ? 0.1523 0.1617 0.1319 -0.0043 0.0018  0.0066  23  ILE   A CD1 
650  N  N   A VAL   A 24  ? 0.1756 0.1852 0.1957 -0.0196 0.0471  0.0077  24  VAL   A N   
651  N  N   B VAL   A 24  ? 0.1807 0.1848 0.1688 -0.0428 0.0343  -0.0129 24  VAL   A N   
652  C  CA  A VAL   A 24  ? 0.1904 0.1956 0.2193 -0.0273 0.0483  0.0006  24  VAL   A CA  
653  C  CA  B VAL   A 24  ? 0.1982 0.1933 0.1890 -0.0440 0.0377  -0.0194 24  VAL   A CA  
654  C  C   A VAL   A 24  ? 0.1965 0.2092 0.2241 -0.0381 0.0411  -0.0009 24  VAL   A C   
655  C  C   B VAL   A 24  ? 0.2039 0.2084 0.1971 -0.0433 0.0392  -0.0277 24  VAL   A C   
656  O  O   A VAL   A 24  ? 0.2078 0.2086 0.2293 -0.0375 0.0371  -0.0080 24  VAL   A O   
657  O  O   B VAL   A 24  ? 0.2113 0.2122 0.2112 -0.0431 0.0364  -0.0233 24  VAL   A O   
658  C  CB  A VAL   A 24  ? 0.1971 0.2009 0.2401 -0.0182 0.0580  0.0012  24  VAL   A CB  
659  C  CB  B VAL   A 24  ? 0.2085 0.1931 0.2051 -0.0423 0.0349  -0.0171 24  VAL   A CB  
660  C  CG1 A VAL   A 24  ? 0.2004 0.2109 0.2463 -0.0142 0.0589  -0.0064 24  VAL   A CG1 
661  C  CG1 B VAL   A 24  ? 0.2155 0.1945 0.2186 -0.0390 0.0367  -0.0134 24  VAL   A CG1 
662  C  CG2 A VAL   A 24  ? 0.2085 0.2043 0.2490 -0.0161 0.0750  0.0148  24  VAL   A CG2 
663  C  CG2 B VAL   A 24  ? 0.2129 0.1903 0.2055 -0.0461 0.0339  -0.0197 24  VAL   A CG2 
682  N  N   A GLU   A 25  ? 0.1993 0.2294 0.2184 -0.0459 0.0496  -0.0079 25  GLU   A N   
683  N  N   B GLU   A 25  ? 0.2040 0.2239 0.1993 -0.0424 0.0477  -0.0320 25  GLU   A N   
684  C  CA  A GLU   A 25  ? 0.2124 0.2588 0.2264 -0.0375 0.0573  -0.0167 25  GLU   A CA  
685  C  CA  B GLU   A 25  ? 0.2094 0.2424 0.2144 -0.0449 0.0401  -0.0334 25  GLU   A CA  
686  C  C   A GLU   A 25  ? 0.2000 0.2641 0.1966 -0.0473 0.0579  -0.0222 25  GLU   A C   
687  C  C   B GLU   A 25  ? 0.2082 0.2523 0.2067 -0.0429 0.0414  -0.0310 25  GLU   A C   
688  O  O   A GLU   A 25  ? 0.2010 0.2762 0.1945 -0.0498 0.0519  -0.0283 25  GLU   A O   
689  O  O   B GLU   A 25  ? 0.2105 0.2561 0.2103 -0.0430 0.0415  -0.0381 25  GLU   A O   
690  C  CB  A GLU   A 25  ? 0.2385 0.2862 0.2617 -0.0269 0.0576  -0.0195 25  GLU   A CB  
691  C  CB  B GLU   A 25  ? 0.2196 0.2513 0.2476 -0.0448 0.0337  -0.0346 25  GLU   A CB  
692  C  CG  A GLU   A 25  ? 0.2696 0.3096 0.3177 -0.0270 0.0405  -0.0211 25  GLU   A CG  
693  C  CG  B GLU   A 25  ? 0.2348 0.2617 0.2884 -0.0442 0.0220  -0.0349 25  GLU   A CG  
694  C  CD  A GLU   A 25  ? 0.2919 0.3296 0.3632 -0.0274 0.0249  -0.0230 25  GLU   A CD  
695  C  CD  B GLU   A 25  ? 0.2443 0.2716 0.3258 -0.0442 0.0100  -0.0327 25  GLU   A CD  
696  O  OE1 A GLU   A 25  ? 0.3009 0.3367 0.3731 -0.0249 0.0130  -0.0300 25  GLU   A OE1 
697  O  OE1 B GLU   A 25  ? 0.2484 0.2768 0.3463 -0.0440 0.0018  -0.0318 25  GLU   A OE1 
698  O  OE2 A GLU   A 25  ? 0.3020 0.3393 0.3908 -0.0286 0.0179  -0.0273 25  GLU   A OE2 
699  O  OE2 B GLU   A 25  ? 0.2505 0.2765 0.3390 -0.0423 0.0054  -0.0314 25  GLU   A OE2 
712  N  N   A GLU   A 26  ? 0.1916 0.2571 0.1912 -0.0614 0.0614  -0.0199 26  GLU   A N   
713  N  N   B GLU   A 26  ? 0.2056 0.2545 0.1962 -0.0424 0.0475  -0.0244 26  GLU   A N   
714  C  CA  A GLU   A 26  ? 0.2035 0.2588 0.1665 -0.0733 0.0546  -0.0158 26  GLU   A CA  
715  C  CA  B GLU   A 26  ? 0.2091 0.2560 0.1964 -0.0387 0.0477  -0.0146 26  GLU   A CA  
716  C  C   A GLU   A 26  ? 0.2050 0.2504 0.1393 -0.0717 0.0512  -0.0116 26  GLU   A C   
717  C  C   B GLU   A 26  ? 0.2087 0.2481 0.1873 -0.0322 0.0504  -0.0027 26  GLU   A C   
718  O  O   A GLU   A 26  ? 0.2141 0.2527 0.1357 -0.0766 0.0482  -0.0071 26  GLU   A O   
719  O  O   B GLU   A 26  ? 0.2133 0.2492 0.1805 -0.0364 0.0592  -0.0013 26  GLU   A O   
720  C  CB  A GLU   A 26  ? 0.2217 0.2651 0.1930 -0.0865 0.0492  -0.0038 26  GLU   A CB  
721  C  CB  B GLU   A 26  ? 0.2135 0.2620 0.2044 -0.0449 0.0388  -0.0122 26  GLU   A CB  
722  C  CG  A GLU   A 26  ? 0.2485 0.2837 0.2665 -0.0887 0.0459  -0.0116 26  GLU   A CG  
723  C  CG  B GLU   A 26  ? 0.2183 0.2696 0.2064 -0.0504 0.0424  -0.0145 26  GLU   A CG  
724  C  CD  A GLU   A 26  ? 0.2660 0.2958 0.3106 -0.0968 0.0584  -0.0142 26  GLU   A CD  
725  C  CD  B GLU   A 26  ? 0.2201 0.2749 0.2058 -0.0584 0.0464  -0.0157 26  GLU   A CD  
726  O  OE1 A GLU   A 26  ? 0.2641 0.3201 0.3157 -0.0855 0.0838  -0.0393 26  GLU   A OE1 
727  O  OE1 B GLU   A 26  ? 0.2273 0.2900 0.2192 -0.0493 0.0586  -0.0187 26  GLU   A OE1 
728  O  OE2 A GLU   A 26  ? 0.2893 0.3013 0.3324 -0.0944 0.0474  -0.0062 26  GLU   A OE2 
729  O  OE2 B GLU   A 26  ? 0.2160 0.2708 0.1644 -0.0671 0.0496  -0.0153 26  GLU   A OE2 
742  N  N   A ALA   A 27  ? 0.1926 0.2380 0.1346 -0.0793 0.0475  -0.0130 27  ALA   A N   
743  N  N   B ALA   A 27  ? 0.2027 0.2396 0.1758 -0.0202 0.0477  0.0077  27  ALA   A N   
744  C  CA  A ALA   A 27  ? 0.2021 0.2448 0.1391 -0.0776 0.0390  -0.0115 27  ALA   A CA  
745  C  CA  B ALA   A 27  ? 0.2068 0.2397 0.1715 -0.0078 0.0388  0.0124  27  ALA   A CA  
746  C  C   A ALA   A 27  ? 0.2267 0.2599 0.1552 -0.0864 0.0378  -0.0215 27  ALA   A C   
747  C  C   B ALA   A 27  ? 0.2192 0.2493 0.1732 -0.0023 0.0353  0.0113  27  ALA   A C   
748  O  O   A ALA   A 27  ? 0.2359 0.2545 0.1607 -0.0881 0.0308  -0.0159 27  ALA   A O   
749  O  O   B ALA   A 27  ? 0.2157 0.2468 0.1747 0.0036  0.0303  0.0130  27  ALA   A O   
750  C  CB  A ALA   A 27  ? 0.1920 0.2388 0.1352 -0.0754 0.0322  0.0005  27  ALA   A CB  
751  C  CB  B ALA   A 27  ? 0.2008 0.2353 0.1697 -0.0072 0.0352  0.0161  27  ALA   A CB  
762  N  N   A LYS   A 28  ? 0.2537 0.2830 0.1700 -0.0832 0.0293  -0.0463 28  LYS   A N   
763  N  N   B LYS   A 28  ? 0.2395 0.2617 0.1855 -0.0015 0.0336  0.0036  28  LYS   A N   
764  C  CA  A LYS   A 28  ? 0.2901 0.3111 0.1980 -0.0736 0.0336  -0.0562 28  LYS   A CA  
765  C  CA  B LYS   A 28  ? 0.2605 0.2777 0.2126 0.0008  0.0278  -0.0072 28  LYS   A CA  
766  C  C   A LYS   A 28  ? 0.3106 0.3359 0.1950 -0.0777 0.0488  -0.0430 28  LYS   A C   
767  C  C   B LYS   A 28  ? 0.2794 0.2929 0.2190 -0.0062 0.0231  -0.0019 28  LYS   A C   
768  O  O   A LYS   A 28  ? 0.3190 0.3426 0.2228 -0.0742 0.0294  -0.0355 28  LYS   A O   
769  O  O   B LYS   A 28  ? 0.2835 0.2928 0.2158 -0.0067 0.0155  0.0067  28  LYS   A O   
770  C  CB  A LYS   A 28  ? 0.3077 0.3212 0.2420 -0.0545 0.0306  -0.0610 28  LYS   A CB  
771  C  CB  B LYS   A 28  ? 0.2662 0.2815 0.2391 0.0087  0.0264  -0.0173 28  LYS   A CB  
772  C  CG  A LYS   A 28  ? 0.3238 0.3291 0.2831 -0.0398 0.0318  -0.0630 28  LYS   A CG  
773  C  CG  B LYS   A 28  ? 0.2716 0.2860 0.2647 0.0111  0.0278  -0.0178 28  LYS   A CG  
774  C  CD  A LYS   A 28  ? 0.3373 0.3422 0.3352 -0.0287 0.0293  -0.0593 28  LYS   A CD  
775  C  CD  B LYS   A 28  ? 0.2776 0.2917 0.2874 0.0127  0.0293  -0.0165 28  LYS   A CD  
776  C  CE  A LYS   A 28  ? 0.3484 0.3523 0.3743 -0.0222 0.0270  -0.0597 28  LYS   A CE  
777  C  CE  B LYS   A 28  ? 0.2823 0.2968 0.3026 0.0117  0.0319  -0.0161 28  LYS   A CE  
778  N  NZ  A LYS   A 28  ? 0.3560 0.3576 0.3971 -0.0174 0.0298  -0.0596 28  LYS   A NZ  
779  N  NZ  B LYS   A 28  ? 0.2847 0.3001 0.3065 0.0114  0.0348  -0.0169 28  LYS   A NZ  
806  N  N   A LYS   A 29  ? 0.3193 0.3561 0.1967 -0.0868 0.0837  -0.0272 29  LYS   A N   
807  N  N   B LYS   A 29  ? 0.2934 0.3083 0.2357 -0.0151 0.0300  0.0024  29  LYS   A N   
808  C  CA  A LYS   A 29  ? 0.3342 0.3778 0.2272 -0.0912 0.1009  -0.0126 29  LYS   A CA  
809  C  CA  B LYS   A 29  ? 0.3095 0.3241 0.2646 -0.0232 0.0296  0.0061  29  LYS   A CA  
810  C  C   A LYS   A 29  ? 0.3396 0.3768 0.2150 -0.1002 0.0903  -0.0076 29  LYS   A C   
811  C  C   B LYS   A 29  ? 0.3173 0.3272 0.2567 -0.0328 0.0240  0.0128  29  LYS   A C   
812  O  O   A LYS   A 29  ? 0.3511 0.3875 0.2199 -0.0954 0.0914  -0.0053 29  LYS   A O   
813  O  O   B LYS   A 29  ? 0.3240 0.3333 0.2647 -0.0323 0.0214  0.0138  29  LYS   A O   
814  C  CB  A LYS   A 29  ? 0.3448 0.3999 0.2865 -0.0809 0.1115  -0.0071 29  LYS   A CB  
815  C  CB  B LYS   A 29  ? 0.3167 0.3350 0.3026 -0.0209 0.0334  0.0043  29  LYS   A CB  
816  C  CG  A LYS   A 29  ? 0.3587 0.4183 0.3446 -0.0707 0.1113  -0.0045 29  LYS   A CG  
817  C  CG  B LYS   A 29  ? 0.3249 0.3440 0.3372 -0.0183 0.0346  0.0018  29  LYS   A CG  
818  C  CD  A LYS   A 29  ? 0.3706 0.4331 0.3955 -0.0627 0.1095  -0.0032 29  LYS   A CD  
819  C  CD  B LYS   A 29  ? 0.3314 0.3516 0.3694 -0.0155 0.0330  0.0003  29  LYS   A CD  
820  C  CE  A LYS   A 29  ? 0.3796 0.4429 0.4302 -0.0582 0.1075  -0.0016 29  LYS   A CE  
821  C  CE  B LYS   A 29  ? 0.3363 0.3575 0.3929 -0.0138 0.0321  -0.0018 29  LYS   A CE  
822  N  NZ  A LYS   A 29  ? 0.3835 0.4482 0.4544 -0.0553 0.1039  -0.0026 29  LYS   A NZ  
823  N  NZ  B LYS   A 29  ? 0.3382 0.3610 0.4062 -0.0133 0.0318  -0.0033 29  LYS   A NZ  
850  N  N   A VAL   A 30  ? 0.3292 0.3628 0.1950 -0.1148 0.0839  -0.0002 30  VAL   A N   
851  N  N   B VAL   A 30  ? 0.3181 0.3248 0.2474 -0.0412 0.0213  0.0140  30  VAL   A N   
852  C  CA  A VAL   A 30  ? 0.3229 0.3467 0.1857 -0.1289 0.0563  0.0151  30  VAL   A CA  
853  C  CA  B VAL   A 30  ? 0.3191 0.3206 0.2413 -0.0498 0.0109  0.0185  30  VAL   A CA  
854  C  C   A VAL   A 30  ? 0.3233 0.3382 0.1486 -0.1275 0.0398  0.0283  30  VAL   A C   
855  C  C   B VAL   A 30  ? 0.3218 0.3191 0.2276 -0.0548 0.0037  0.0187  30  VAL   A C   
856  O  O   A VAL   A 30  ? 0.3313 0.3411 0.1550 -0.1217 0.0344  0.0316  30  VAL   A O   
857  O  O   B VAL   A 30  ? 0.3247 0.3205 0.2254 -0.0534 0.0023  0.0197  30  VAL   A O   
858  C  CB  A VAL   A 30  ? 0.3188 0.3387 0.2203 -0.1421 0.0403  0.0142  30  VAL   A CB  
859  C  CB  B VAL   A 30  ? 0.3176 0.3171 0.2519 -0.0526 0.0071  0.0200  30  VAL   A CB  
860  C  CG1 A VAL   A 30  ? 0.3238 0.3382 0.2347 -0.1425 0.0322  0.0150  30  VAL   A CG1 
861  C  CG1 B VAL   A 30  ? 0.3194 0.3169 0.2589 -0.0526 0.0049  0.0200  30  VAL   A CG1 
862  C  CG2 A VAL   A 30  ? 0.3168 0.3377 0.2382 -0.1484 0.0438  0.0158  30  VAL   A CG2 
863  C  CG2 B VAL   A 30  ? 0.3165 0.3158 0.2565 -0.0543 0.0082  0.0235  30  VAL   A CG2 
882  N  N   A LYS   A 31  ? 0.3147 0.3234 0.1258 -0.1299 0.0171  0.0244  31  LYS   A N   
883  N  N   B LYS   A 31  ? 0.3212 0.3149 0.2217 -0.0619 -0.0054 0.0182  31  LYS   A N   
884  C  CA  A LYS   A 31  ? 0.3204 0.3193 0.1507 -0.1107 -0.0129 0.0251  31  LYS   A CA  
885  C  CA  B LYS   A 31  ? 0.3221 0.3133 0.2281 -0.0656 -0.0168 0.0224  31  LYS   A CA  
886  C  C   A LYS   A 31  ? 0.3006 0.3026 0.1223 -0.0927 -0.0176 0.0603  31  LYS   A C   
887  C  C   B LYS   A 31  ? 0.3015 0.2972 0.1741 -0.0728 -0.0212 0.0454  31  LYS   A C   
888  O  O   A LYS   A 31  ? 0.3048 0.3169 0.1326 -0.0886 -0.0168 0.0711  31  LYS   A O   
889  O  O   B LYS   A 31  ? 0.3064 0.3029 0.1790 -0.0689 -0.0249 0.0544  31  LYS   A O   
890  C  CB  A LYS   A 31  ? 0.3504 0.3370 0.2503 -0.1021 -0.0280 0.0030  31  LYS   A CB  
891  C  CB  B LYS   A 31  ? 0.3428 0.3285 0.2998 -0.0604 -0.0220 0.0077  31  LYS   A CB  
892  C  CG  A LYS   A 31  ? 0.3857 0.3587 0.3687 -0.0863 -0.0403 -0.0111 31  LYS   A CG  
893  C  CG  B LYS   A 31  ? 0.3628 0.3436 0.3756 -0.0531 -0.0270 -0.0022 31  LYS   A CG  
894  C  CD  A LYS   A 31  ? 0.4139 0.3755 0.4558 -0.0723 -0.0550 -0.0252 31  LYS   A CD  
895  C  CD  B LYS   A 31  ? 0.3787 0.3560 0.4358 -0.0469 -0.0332 -0.0112 31  LYS   A CD  
896  C  CE  A LYS   A 31  ? 0.4322 0.3877 0.5124 -0.0619 -0.0655 -0.0352 31  LYS   A CE  
897  C  CE  B LYS   A 31  ? 0.3898 0.3652 0.4762 -0.0423 -0.0376 -0.0175 31  LYS   A CE  
898  N  NZ  A LYS   A 31  ? 0.4415 0.3937 0.5439 -0.0558 -0.0707 -0.0398 31  LYS   A NZ  
899  N  NZ  B LYS   A 31  ? 0.3963 0.3698 0.4997 -0.0394 -0.0396 -0.0207 31  LYS   A NZ  
926  N  N   . PRO   A 32  ? 0.2732 0.2742 0.1264 -0.0856 -0.0199 0.0494  32  PRO   A N   
927  C  CA  . PRO   A 32  ? 0.2562 0.2555 0.1481 -0.0753 -0.0237 0.0612  32  PRO   A CA  
928  C  C   . PRO   A 32  ? 0.2493 0.2453 0.1602 -0.0613 -0.0346 0.0670  32  PRO   A C   
929  O  O   . PRO   A 32  ? 0.2439 0.2382 0.1701 -0.0604 -0.0462 0.0626  32  PRO   A O   
930  C  CB  . PRO   A 32  ? 0.2457 0.2570 0.1603 -0.0745 -0.0242 0.0444  32  PRO   A CB  
931  C  CG  . PRO   A 32  ? 0.2437 0.2593 0.1155 -0.0688 -0.0341 0.0353  32  PRO   A CG  
932  C  CD  . PRO   A 32  ? 0.2498 0.2634 0.1159 -0.0803 -0.0279 0.0355  32  PRO   A CD  
940  N  N   . THR   A 33  ? 0.2547 0.2406 0.1527 -0.0580 -0.0278 0.0716  33  THR   A N   
941  C  CA  . THR   A 33  ? 0.2538 0.2416 0.1581 -0.0480 -0.0376 0.0677  33  THR   A CA  
942  C  C   . THR   A 33  ? 0.2261 0.2219 0.1506 -0.0494 -0.0371 0.0530  33  THR   A C   
943  O  O   . THR   A 33  ? 0.2245 0.2237 0.1566 -0.0501 -0.0506 0.0517  33  THR   A O   
944  C  CB  . THR   A 33  ? 0.2778 0.2641 0.1734 -0.0367 -0.0461 0.0903  33  THR   A CB  
945  O  OG1 . THR   A 33  ? 0.3003 0.2813 0.2018 -0.0209 -0.0378 0.0988  33  THR   A OG1 
946  C  CG2 . THR   A 33  ? 0.2809 0.2733 0.1950 -0.0315 -0.0524 0.0887  33  THR   A CG2 
954  N  N   . VAL   A 34  ? 0.2019 0.2058 0.1378 -0.0499 -0.0299 0.0481  34  VAL   A N   
955  C  CA  . VAL   A 34  ? 0.1793 0.1844 0.1258 -0.0409 -0.0217 0.0428  34  VAL   A CA  
956  C  C   . VAL   A 34  ? 0.1672 0.1732 0.1216 -0.0335 -0.0097 0.0335  34  VAL   A C   
957  O  O   . VAL   A 34  ? 0.1675 0.1775 0.1480 -0.0354 -0.0129 0.0449  34  VAL   A O   
958  C  CB  . VAL   A 34  ? 0.1833 0.1801 0.1547 -0.0370 -0.0126 0.0339  34  VAL   A CB  
959  C  CG1 . VAL   A 34  ? 0.1877 0.1792 0.1567 -0.0318 0.0001  0.0215  34  VAL   A CG1 
960  C  CG2 . VAL   A 34  ? 0.1887 0.1957 0.1817 -0.0304 -0.0216 0.0352  34  VAL   A CG2 
970  N  N   . VAL   A 35  ? 0.1565 0.1629 0.1237 -0.0311 -0.0120 0.0292  35  VAL   A N   
971  C  CA  . VAL   A 35  ? 0.1475 0.1600 0.1160 -0.0253 -0.0042 0.0226  35  VAL   A CA  
972  C  C   . VAL   A 35  ? 0.1380 0.1428 0.1180 -0.0214 -0.0047 0.0216  35  VAL   A C   
973  O  O   . VAL   A 35  ? 0.1307 0.1581 0.1384 -0.0263 0.0057  0.0166  35  VAL   A O   
974  C  CB  . VAL   A 35  ? 0.1542 0.1632 0.1306 -0.0174 0.0075  0.0121  35  VAL   A CB  
975  C  CG1 . VAL   A 35  ? 0.1619 0.1688 0.1461 -0.0096 0.0005  0.0069  35  VAL   A CG1 
976  C  CG2 . VAL   A 35  ? 0.1520 0.1623 0.1541 -0.0140 0.0054  0.0062  35  VAL   A CG2 
986  N  N   . VAL   A 36  ? 0.1280 0.1394 0.1156 -0.0212 0.0051  0.0228  36  VAL   A N   
987  C  CA  . VAL   A 36  ? 0.1265 0.1300 0.1092 -0.0126 0.0024  0.0123  36  VAL   A CA  
988  C  C   . VAL   A 36  ? 0.1210 0.1358 0.1224 -0.0153 0.0048  0.0153  36  VAL   A C   
989  O  O   . VAL   A 36  ? 0.1235 0.1378 0.1434 -0.0087 0.0160  0.0193  36  VAL   A O   
990  C  CB  . VAL   A 36  ? 0.1235 0.1252 0.1244 -0.0133 0.0046  0.0199  36  VAL   A CB  
991  C  CG1 . VAL   A 36  ? 0.1313 0.1274 0.1354 -0.0161 0.0068  0.0080  36  VAL   A CG1 
992  C  CG2 . VAL   A 36  ? 0.1365 0.1314 0.1332 -0.0096 0.0000  0.0239  36  VAL   A CG2 
1002 N  N   . ASN   A 37  ? 0.1173 0.1259 0.1146 -0.0059 0.0010  0.0223  37  ASN   A N   
1003 C  CA  . ASN   A 37  ? 0.1180 0.1209 0.1128 -0.0034 0.0041  0.0154  37  ASN   A CA  
1004 C  C   . ASN   A 37  ? 0.1153 0.1211 0.1149 -0.0052 0.0071  0.0245  37  ASN   A C   
1005 O  O   . ASN   A 37  ? 0.1295 0.1295 0.1218 0.0047  0.0126  0.0108  37  ASN   A O   
1006 C  CB  . ASN   A 37  ? 0.1225 0.1224 0.1224 -0.0015 0.0035  0.0112  37  ASN   A CB  
1007 C  CG  . ASN   A 37  ? 0.1203 0.1198 0.1329 -0.0009 0.0020  0.0079  37  ASN   A CG  
1008 O  OD1 . ASN   A 37  ? 0.1212 0.1222 0.1469 -0.0016 0.0027  0.0158  37  ASN   A OD1 
1009 N  ND2 . ASN   A 37  ? 0.1232 0.1238 0.1448 -0.0046 -0.0010 0.0239  37  ASN   A ND2 
1016 N  N   A ALA   A 38  ? 0.1162 0.1249 0.1274 -0.0052 0.0151  0.0120  38  ALA   A N   
1017 N  N   B ALA   A 38  ? 0.1185 0.1280 0.1208 -0.0042 0.0052  0.0164  38  ALA   A N   
1018 C  CA  A ALA   A 38  ? 0.1242 0.1294 0.1193 -0.0059 0.0078  0.0040  38  ALA   A CA  
1019 C  CA  B ALA   A 38  ? 0.1253 0.1350 0.1243 -0.0027 -0.0050 0.0104  38  ALA   A CA  
1020 C  C   A ALA   A 38  ? 0.1234 0.1262 0.1185 -0.0003 0.0045  -0.0019 38  ALA   A C   
1021 C  C   B ALA   A 38  ? 0.1256 0.1350 0.1286 -0.0027 -0.0116 0.0056  38  ALA   A C   
1022 O  O   A ALA   A 38  ? 0.1234 0.1138 0.1173 -0.0026 -0.0078 -0.0057 38  ALA   A O   
1023 O  O   B ALA   A 38  ? 0.1218 0.1343 0.1357 -0.0045 -0.0236 0.0131  38  ALA   A O   
1024 C  CB  A ALA   A 38  ? 0.1297 0.1528 0.1283 -0.0208 0.0001  0.0010  38  ALA   A CB  
1025 C  CB  B ALA   A 38  ? 0.1295 0.1472 0.1354 -0.0042 -0.0093 0.0018  38  ALA   A CB  
1036 N  N   A ALA   A 39  ? 0.1232 0.1251 0.1267 -0.0002 0.0103  0.0116  39  ALA   A N   
1037 N  N   B ALA   A 39  ? 0.1305 0.1325 0.1283 -0.0048 -0.0059 0.0078  39  ALA   A N   
1038 C  CA  A ALA   A 39  ? 0.1208 0.1216 0.1190 -0.0005 0.0058  0.0061  39  ALA   A CA  
1039 C  CA  B ALA   A 39  ? 0.1387 0.1352 0.1249 -0.0060 0.0024  0.0129  39  ALA   A CA  
1040 C  C   A ALA   A 39  ? 0.1200 0.1252 0.1276 -0.0001 0.0025  0.0064  39  ALA   A C   
1041 C  C   B ALA   A 39  ? 0.1362 0.1282 0.1128 -0.0011 0.0145  0.0121  39  ALA   A C   
1042 O  O   A ALA   A 39  ? 0.1299 0.1280 0.1266 -0.0053 0.0000  0.0152  39  ALA   A O   
1043 O  O   B ALA   A 39  ? 0.1423 0.1282 0.1072 -0.0046 0.0143  0.0115  39  ALA   A O   
1044 C  CB  A ALA   A 39  ? 0.1208 0.1301 0.1198 -0.0013 -0.0035 0.0022  39  ALA   A CB  
1045 C  CB  B ALA   A 39  ? 0.1466 0.1413 0.1340 -0.0062 -0.0011 0.0025  39  ALA   A CB  
1056 N  N   A ASN   A 40  ? 0.1204 0.1274 0.1295 -0.0068 0.0123  0.0061  40  ASN   A N   
1057 N  N   B ASN   A 40  ? 0.1384 0.1244 0.1122 -0.0005 0.0223  0.0153  40  ASN   A N   
1058 C  CA  A ASN   A 40  ? 0.1254 0.1234 0.1280 -0.0038 0.0076  0.0053  40  ASN   A CA  
1059 C  CA  B ASN   A 40  ? 0.1358 0.1214 0.1271 0.0021  0.0140  0.0112  40  ASN   A CA  
1060 C  C   A ASN   A 40  ? 0.1275 0.1145 0.1105 -0.0048 0.0141  0.0178  40  ASN   A C   
1061 C  C   B ASN   A 40  ? 0.1318 0.1210 0.1207 0.0023  0.0150  0.0213  40  ASN   A C   
1062 O  O   A ASN   A 40  ? 0.1274 0.1227 0.1165 -0.0084 0.0125  0.0165  40  ASN   A O   
1063 O  O   B ASN   A 40  ? 0.1286 0.1248 0.1231 0.0005  0.0148  0.0209  40  ASN   A O   
1064 C  CB  A ASN   A 40  ? 0.1383 0.1322 0.1275 0.0036  0.0015  0.0086  40  ASN   A CB  
1065 C  CB  B ASN   A 40  ? 0.1480 0.1265 0.1458 -0.0032 0.0132  0.0072  40  ASN   A CB  
1066 C  CG  A ASN   A 40  ? 0.1514 0.1346 0.1500 0.0050  -0.0019 0.0163  40  ASN   A CG  
1067 C  CG  B ASN   A 40  ? 0.1536 0.1326 0.1697 -0.0075 0.0136  0.0062  40  ASN   A CG  
1068 O  OD1 A ASN   A 40  ? 0.1640 0.1311 0.1771 0.0029  -0.0055 0.0127  40  ASN   A OD1 
1069 O  OD1 B ASN   A 40  ? 0.1591 0.1327 0.1845 -0.0109 0.0121  0.0048  40  ASN   A OD1 
1070 N  ND2 A ASN   A 40  ? 0.1600 0.1478 0.1527 0.0045  0.0063  -0.0006 40  ASN   A ND2 
1071 N  ND2 B ASN   A 40  ? 0.1528 0.1451 0.1696 -0.0109 0.0276  -0.0023 40  ASN   A ND2 
1084 N  N   A VAL   A 41  ? 0.1295 0.1179 0.1211 -0.0046 0.0107  0.0176  41  VAL   A N   
1085 N  N   B VAL   A 41  ? 0.1318 0.1231 0.1258 0.0045  0.0120  0.0261  41  VAL   A N   
1086 C  CA  A VAL   A 41  ? 0.1294 0.1219 0.1369 -0.0002 0.0127  0.0149  41  VAL   A CA  
1087 C  CA  B VAL   A 41  ? 0.1352 0.1320 0.1331 0.0044  0.0226  0.0242  41  VAL   A CA  
1088 C  C   A VAL   A 41  ? 0.1247 0.1225 0.1390 0.0026  0.0174  0.0174  41  VAL   A C   
1089 C  C   B VAL   A 41  ? 0.1356 0.1352 0.1306 0.0008  0.0320  0.0210  41  VAL   A C   
1090 O  O   A VAL   A 41  ? 0.1313 0.1190 0.1588 0.0051  0.0079  0.0110  41  VAL   A O   
1091 O  O   B VAL   A 41  ? 0.1426 0.1298 0.1384 0.0013  0.0199  0.0219  41  VAL   A O   
1092 C  CB  A VAL   A 41  ? 0.1316 0.1293 0.1343 0.0044  0.0203  0.0114  41  VAL   A CB  
1093 C  CB  B VAL   A 41  ? 0.1413 0.1421 0.1438 0.0072  0.0245  0.0260  41  VAL   A CB  
1094 C  CG1 A VAL   A 41  ? 0.1433 0.1383 0.1499 0.0018  0.0031  0.0078  41  VAL   A CG1 
1095 C  CG1 B VAL   A 41  ? 0.1547 0.1462 0.1552 0.0034  0.0280  0.0229  41  VAL   A CG1 
1096 C  CG2 A VAL   A 41  ? 0.1363 0.1351 0.1314 -0.0006 0.0322  0.0067  41  VAL   A CG2 
1097 C  CG2 B VAL   A 41  ? 0.1417 0.1490 0.1523 0.0072  0.0153  0.0236  41  VAL   A CG2 
1116 N  N   A TYR   A 42  ? 0.1185 0.1178 0.1619 -0.0028 0.0197  0.0207  42  TYR   A N   
1117 N  N   B TYR   A 42  ? 0.1314 0.1382 0.1342 0.0038  0.0369  0.0229  42  TYR   A N   
1118 C  CA  A TYR   A 42  ? 0.1259 0.1140 0.1656 -0.0071 0.0223  0.0240  42  TYR   A CA  
1119 C  CA  B TYR   A 42  ? 0.1328 0.1411 0.1357 0.0024  0.0337  0.0262  42  TYR   A CA  
1120 C  C   A TYR   A 42  ? 0.1168 0.1139 0.1650 -0.0043 0.0213  0.0230  42  TYR   A C   
1121 C  C   B TYR   A 42  ? 0.1327 0.1424 0.1365 0.0004  0.0232  0.0324  42  TYR   A C   
1122 O  O   A TYR   A 42  ? 0.1214 0.1179 0.1907 -0.0172 0.0144  0.0018  42  TYR   A O   
1123 O  O   B TYR   A 42  ? 0.1316 0.1457 0.1498 -0.0018 0.0229  0.0284  42  TYR   A O   
1124 C  CB  A TYR   A 42  ? 0.1467 0.1252 0.1659 -0.0065 0.0314  0.0293  42  TYR   A CB  
1125 C  CB  B TYR   A 42  ? 0.1421 0.1442 0.1417 0.0061  0.0282  0.0292  42  TYR   A CB  
1126 C  CG  A TYR   A 42  ? 0.1579 0.1342 0.1585 -0.0066 0.0226  0.0391  42  TYR   A CG  
1127 C  CG  B TYR   A 42  ? 0.1494 0.1469 0.1397 0.0149  0.0152  0.0296  42  TYR   A CG  
1128 C  CD1 A TYR   A 42  ? 0.1642 0.1518 0.1652 -0.0163 0.0256  0.0357  42  TYR   A CD1 
1129 C  CD1 B TYR   A 42  ? 0.1514 0.1504 0.1350 0.0101  0.0162  0.0290  42  TYR   A CD1 
1130 C  CD2 A TYR   A 42  ? 0.1639 0.1528 0.1787 0.0012  0.0230  0.0312  42  TYR   A CD2 
1131 C  CD2 B TYR   A 42  ? 0.1589 0.1595 0.1535 0.0198  0.0143  0.0223  42  TYR   A CD2 
1132 C  CE1 A TYR   A 42  ? 0.1683 0.1619 0.1599 -0.0105 0.0258  0.0295  42  TYR   A CE1 
1133 C  CE1 B TYR   A 42  ? 0.1525 0.1552 0.1347 0.0108  0.0134  0.0194  42  TYR   A CE1 
1134 C  CE2 A TYR   A 42  ? 0.1701 0.1660 0.1895 -0.0071 0.0226  0.0321  42  TYR   A CE2 
1135 C  CE2 B TYR   A 42  ? 0.1603 0.1642 0.1518 0.0215  0.0122  0.0184  42  TYR   A CE2 
1136 C  CZ  A TYR   A 42  ? 0.1751 0.1694 0.1687 -0.0104 0.0308  0.0278  42  TYR   A CZ  
1137 C  CZ  B TYR   A 42  ? 0.1559 0.1614 0.1394 0.0153  0.0140  0.0145  42  TYR   A CZ  
1138 O  OH  A TYR   A 42  ? 0.1874 0.1813 0.1863 -0.0071 0.0186  0.0231  42  TYR   A OH  
1139 O  OH  B TYR   A 42  ? 0.1525 0.1676 0.1514 0.0129  0.0128  0.0099  42  TYR   A OH  
1158 N  N   A LEU   A 43  ? 0.1218 0.1147 0.1566 -0.0042 0.0163  0.0058  43  LEU   A N   
1159 N  N   B LEU   A 43  ? 0.1278 0.1386 0.1323 -0.0014 0.0067  0.0276  43  LEU   A N   
1160 C  CA  A LEU   A 43  ? 0.1176 0.1137 0.1489 -0.0071 0.0185  0.0086  43  LEU   A CA  
1161 C  CA  B LEU   A 43  ? 0.1270 0.1352 0.1308 -0.0071 0.0008  0.0225  43  LEU   A CA  
1162 C  C   A LEU   A 43  ? 0.1158 0.1245 0.1483 -0.0013 0.0075  0.0058  43  LEU   A C   
1163 C  C   B LEU   A 43  ? 0.1275 0.1383 0.1302 -0.0081 0.0008  0.0108  43  LEU   A C   
1164 O  O   A LEU   A 43  ? 0.1302 0.1287 0.1724 0.0115  -0.0061 0.0057  43  LEU   A O   
1165 O  O   B LEU   A 43  ? 0.1280 0.1397 0.1257 -0.0127 -0.0052 0.0039  43  LEU   A O   
1166 C  CB  A LEU   A 43  ? 0.1302 0.1131 0.1588 -0.0063 0.0102  0.0041  43  LEU   A CB  
1167 C  CB  B LEU   A 43  ? 0.1213 0.1271 0.1299 -0.0078 0.0001  0.0244  43  LEU   A CB  
1168 C  CG  A LEU   A 43  ? 0.1330 0.1220 0.1673 -0.0015 0.0099  0.0054  43  LEU   A CG  
1169 C  CG  B LEU   A 43  ? 0.1165 0.1282 0.1380 -0.0049 0.0037  0.0213  43  LEU   A CG  
1170 C  CD1 A LEU   A 43  ? 0.1328 0.1287 0.1750 -0.0024 0.0079  0.0140  43  LEU   A CD1 
1171 C  CD1 B LEU   A 43  ? 0.1162 0.1314 0.1549 -0.0037 0.0024  0.0195  43  LEU   A CD1 
1172 C  CD2 A LEU   A 43  ? 0.1456 0.1236 0.1714 -0.0033 0.0055  0.0165  43  LEU   A CD2 
1173 C  CD2 B LEU   A 43  ? 0.1246 0.1235 0.1471 -0.0045 -0.0004 0.0311  43  LEU   A CD2 
1196 N  N   A LYS   A 44  ? 0.1266 0.1211 0.1352 -0.0039 0.0100  0.0136  44  LYS   A N   
1197 N  N   B LYS   A 44  ? 0.1349 0.1382 0.1350 -0.0034 0.0005  0.0103  44  LYS   A N   
1198 C  CA  A LYS   A 44  ? 0.1417 0.1219 0.1405 -0.0034 0.0167  0.0176  44  LYS   A CA  
1199 C  CA  B LYS   A 44  ? 0.1457 0.1394 0.1456 0.0001  0.0034  0.0101  44  LYS   A CA  
1200 C  C   A LYS   A 44  ? 0.1304 0.1225 0.1343 0.0019  0.0019  0.0112  44  LYS   A C   
1201 C  C   B LYS   A 44  ? 0.1335 0.1290 0.1303 0.0008  0.0058  0.0074  44  LYS   A C   
1202 O  O   A LYS   A 44  ? 0.1356 0.1397 0.1538 0.0045  -0.0000 0.0028  44  LYS   A O   
1203 O  O   B LYS   A 44  ? 0.1370 0.1353 0.1257 0.0029  0.0168  -0.0069 44  LYS   A O   
1204 C  CB  A LYS   A 44  ? 0.1705 0.1384 0.1784 -0.0053 0.0276  0.0301  44  LYS   A CB  
1205 C  CB  B LYS   A 44  ? 0.1695 0.1590 0.1943 0.0045  0.0074  0.0116  44  LYS   A CB  
1206 C  CG  A LYS   A 44  ? 0.2009 0.1630 0.2281 -0.0122 0.0519  0.0440  44  LYS   A CG  
1207 C  CG  B LYS   A 44  ? 0.1898 0.1821 0.2468 0.0062  0.0137  0.0147  44  LYS   A CG  
1208 C  CD  A LYS   A 44  ? 0.2344 0.2082 0.3250 -0.0134 0.0481  0.0344  44  LYS   A CD  
1209 C  CD  B LYS   A 44  ? 0.2116 0.2105 0.3048 0.0031  0.0083  0.0142  44  LYS   A CD  
1210 C  CE  A LYS   A 44  ? 0.2491 0.2396 0.3910 -0.0095 0.0448  0.0260  44  LYS   A CE  
1211 C  CE  B LYS   A 44  ? 0.2192 0.2278 0.3429 0.0006  0.0053  0.0162  44  LYS   A CE  
1212 N  NZ  A LYS   A 44  ? 0.2547 0.2575 0.4215 -0.0087 0.0465  0.0257  44  LYS   A NZ  
1213 N  NZ  B LYS   A 44  ? 0.2274 0.2415 0.3674 -0.0085 0.0068  0.0166  44  LYS   A NZ  
1240 N  N   . HIS   A 45  ? 0.1223 0.1218 0.1398 -0.0011 0.0008  0.0153  45  HIS   A N   
1241 C  CA  . HIS   A 45  ? 0.1257 0.1202 0.1397 0.0005  -0.0053 0.0069  45  HIS   A CA  
1242 C  C   . HIS   A 45  ? 0.1301 0.1368 0.1470 0.0042  -0.0009 0.0098  45  HIS   A C   
1243 O  O   . HIS   A 45  ? 0.1477 0.1493 0.1793 0.0222  -0.0074 -0.0045 45  HIS   A O   
1244 C  CB  . HIS   A 45  ? 0.1233 0.1223 0.1383 -0.0030 -0.0021 0.0078  45  HIS   A CB  
1245 C  CG  . HIS   A 45  ? 0.1171 0.1208 0.1256 -0.0049 0.0047  0.0121  45  HIS   A CG  
1246 N  ND1 . HIS   A 45  ? 0.1145 0.1261 0.1444 -0.0038 -0.0012 0.0175  45  HIS   A ND1 
1247 C  CD2 . HIS   A 45  ? 0.1190 0.1270 0.1351 -0.0112 -0.0019 0.0177  45  HIS   A CD2 
1248 C  CE1 . HIS   A 45  ? 0.1197 0.1320 0.1350 -0.0090 0.0025  0.0193  45  HIS   A CE1 
1249 N  NE2 . HIS   A 45  ? 0.1187 0.1357 0.1356 -0.0057 0.0013  0.0217  45  HIS   A NE2 
1258 N  N   A GLY   A 46  ? 0.1443 0.1399 0.1672 0.0061  -0.0154 0.0224  46  GLY   A N   
1259 N  N   B GLY   A 46  ? 0.1367 0.1402 0.1522 0.0111  -0.0095 0.0141  46  GLY   A N   
1260 C  CA  A GLY   A 46  ? 0.1514 0.1458 0.1871 0.0093  -0.0195 0.0244  46  GLY   A CA  
1261 C  CA  B GLY   A 46  ? 0.1407 0.1434 0.1556 0.0172  -0.0151 0.0107  46  GLY   A CA  
1262 C  C   A GLY   A 46  ? 0.1538 0.1430 0.1875 0.0158  -0.0287 0.0290  46  GLY   A C   
1263 C  C   B GLY   A 46  ? 0.1411 0.1410 0.1445 0.0248  -0.0239 0.0075  46  GLY   A C   
1264 O  O   A GLY   A 46  ? 0.1533 0.1519 0.2162 0.0132  -0.0457 0.0098  46  GLY   A O   
1265 O  O   B GLY   A 46  ? 0.1401 0.1476 0.1622 0.0256  -0.0310 -0.0023 46  GLY   A O   
1272 N  N   A GLY   A 47  ? 0.1565 0.1426 0.1708 0.0178  -0.0192 0.0176  47  GLY   A N   
1273 N  N   B GLY   A 47  ? 0.1425 0.1399 0.1393 0.0265  -0.0168 -0.0015 47  GLY   A N   
1274 C  CA  A GLY   A 47  ? 0.1561 0.1458 0.1523 0.0213  -0.0305 0.0022  47  GLY   A CA  
1275 C  CA  B GLY   A 47  ? 0.1449 0.1457 0.1349 0.0228  -0.0282 -0.0038 47  GLY   A CA  
1276 C  C   A GLY   A 47  ? 0.1473 0.1377 0.1583 0.0187  -0.0397 -0.0095 47  GLY   A C   
1277 C  C   B GLY   A 47  ? 0.1425 0.1421 0.1193 0.0213  -0.0236 -0.0129 47  GLY   A C   
1278 O  O   A GLY   A 47  ? 0.1452 0.1330 0.1623 0.0220  -0.0398 0.0031  47  GLY   A O   
1279 O  O   B GLY   A 47  ? 0.1439 0.1396 0.1135 0.0274  -0.0159 0.0057  47  GLY   A O   
1286 N  N   A GLY   A 48  ? 0.1417 0.1395 0.1614 0.0209  -0.0445 -0.0082 48  GLY   A N   
1287 N  N   B GLY   A 48  ? 0.1434 0.1422 0.1413 0.0138  -0.0205 -0.0128 48  GLY   A N   
1288 C  CA  A GLY   A 48  ? 0.1410 0.1326 0.1846 0.0131  -0.0372 -0.0084 48  GLY   A CA  
1289 C  CA  B GLY   A 48  ? 0.1436 0.1364 0.1479 0.0059  -0.0168 -0.0145 48  GLY   A CA  
1290 C  C   A GLY   A 48  ? 0.1333 0.1319 0.1675 0.0018  -0.0126 -0.0055 48  GLY   A C   
1291 C  C   B GLY   A 48  ? 0.1385 0.1371 0.1427 -0.0001 0.0007  -0.0051 48  GLY   A C   
1292 O  O   A GLY   A 48  ? 0.1431 0.1307 0.1619 -0.0009 -0.0093 0.0043  48  GLY   A O   
1293 O  O   B GLY   A 48  ? 0.1508 0.1420 0.1464 -0.0047 0.0035  -0.0078 48  GLY   A O   
1300 N  N   A VAL   A 49  ? 0.1203 0.1273 0.1779 -0.0026 -0.0158 -0.0049 49  VAL   A N   
1301 N  N   B VAL   A 49  ? 0.1263 0.1320 0.1444 -0.0048 0.0013  0.0008  49  VAL   A N   
1302 C  CA  A VAL   A 49  ? 0.1287 0.1246 0.1739 -0.0044 0.0059  -0.0008 49  VAL   A CA  
1303 C  CA  B VAL   A 49  ? 0.1175 0.1314 0.1335 -0.0042 0.0056  0.0102  49  VAL   A CA  
1304 C  C   A VAL   A 49  ? 0.1273 0.1172 0.1531 -0.0023 0.0070  0.0035  49  VAL   A C   
1305 C  C   B VAL   A 49  ? 0.1182 0.1231 0.1059 0.0040  0.0064  0.0061  49  VAL   A C   
1306 O  O   A VAL   A 49  ? 0.1304 0.1250 0.1559 -0.0105 0.0102  -0.0007 49  VAL   A O   
1307 O  O   B VAL   A 49  ? 0.1244 0.1228 0.0957 0.0081  0.0123  0.0058  49  VAL   A O   
1308 C  CB  A VAL   A 49  ? 0.1396 0.1274 0.1804 -0.0073 0.0135  -0.0081 49  VAL   A CB  
1309 C  CB  B VAL   A 49  ? 0.1101 0.1275 0.1376 0.0005  0.0024  0.0068  49  VAL   A CB  
1310 C  CG1 A VAL   A 49  ? 0.1440 0.1180 0.1762 0.0006  0.0191  -0.0031 49  VAL   A CG1 
1311 C  CG1 B VAL   A 49  ? 0.0992 0.1230 0.1360 0.0113  0.0009  0.0104  49  VAL   A CG1 
1312 C  CG2 A VAL   A 49  ? 0.1543 0.1361 0.2279 -0.0187 0.0130  -0.0096 49  VAL   A CG2 
1313 C  CG2 B VAL   A 49  ? 0.1101 0.1292 0.1460 0.0031  0.0127  0.0051  49  VAL   A CG2 
1332 N  N   A ALA   A 50  ? 0.1188 0.1160 0.1430 -0.0055 -0.0104 0.0128  50  ALA   A N   
1333 N  N   B ALA   A 50  ? 0.1184 0.1199 0.0997 0.0067  0.0073  0.0073  50  ALA   A N   
1334 C  CA  A ALA   A 50  ? 0.1150 0.1166 0.1323 -0.0120 -0.0064 0.0143  50  ALA   A CA  
1335 C  CA  B ALA   A 50  ? 0.1237 0.1216 0.1039 -0.0018 -0.0009 0.0088  50  ALA   A CA  
1336 C  C   A ALA   A 50  ? 0.1160 0.1186 0.1299 -0.0098 -0.0025 0.0079  50  ALA   A C   
1337 C  C   B ALA   A 50  ? 0.1245 0.1247 0.1068 -0.0018 -0.0012 0.0025  50  ALA   A C   
1338 O  O   A ALA   A 50  ? 0.1169 0.1209 0.1467 -0.0059 -0.0071 0.0051  50  ALA   A O   
1339 O  O   B ALA   A 50  ? 0.1248 0.1267 0.1131 -0.0018 -0.0037 0.0014  50  ALA   A O   
1340 C  CB  A ALA   A 50  ? 0.1076 0.1189 0.1319 -0.0092 -0.0097 0.0028  50  ALA   A CB  
1341 C  CB  B ALA   A 50  ? 0.1288 0.1179 0.1046 0.0016  -0.0004 0.0081  50  ALA   A CB  
1352 N  N   A GLY   A 51  ? 0.1187 0.1102 0.1385 0.0015  -0.0086 0.0035  51  GLY   A N   
1353 N  N   B GLY   A 51  ? 0.1251 0.1237 0.1225 0.0014  -0.0075 -0.0032 51  GLY   A N   
1354 C  CA  A GLY   A 51  ? 0.1331 0.1131 0.1517 0.0075  -0.0170 0.0068  51  GLY   A CA  
1355 C  CA  B GLY   A 51  ? 0.1315 0.1263 0.1326 0.0026  -0.0129 -0.0040 51  GLY   A CA  
1356 C  C   A GLY   A 51  ? 0.1218 0.1225 0.1485 0.0034  -0.0041 -0.0082 51  GLY   A C   
1357 C  C   B GLY   A 51  ? 0.1251 0.1312 0.1359 0.0008  -0.0070 -0.0099 51  GLY   A C   
1358 O  O   A GLY   A 51  ? 0.1263 0.1292 0.1647 0.0029  -0.0064 -0.0110 51  GLY   A O   
1359 O  O   B GLY   A 51  ? 0.1279 0.1351 0.1403 -0.0000 -0.0109 -0.0112 51  GLY   A O   
1366 N  N   . ALA   A 52  ? 0.1227 0.1366 0.1405 0.0005  -0.0034 -0.0137 52  ALA   A N   
1367 C  CA  . ALA   A 52  ? 0.1206 0.1497 0.1543 -0.0039 0.0016  -0.0155 52  ALA   A CA  
1368 C  C   . ALA   A 52  ? 0.1228 0.1461 0.1290 -0.0110 0.0084  -0.0086 52  ALA   A C   
1369 O  O   . ALA   A 52  ? 0.1332 0.1541 0.1419 -0.0078 0.0050  -0.0114 52  ALA   A O   
1370 C  CB  . ALA   A 52  ? 0.1322 0.1791 0.1741 -0.0077 0.0003  -0.0093 52  ALA   A CB  
1377 N  N   A LEU   A 53  ? 0.1216 0.1408 0.1292 -0.0095 0.0035  -0.0032 53  LEU   A N   
1378 N  N   B LEU   A 53  ? 0.1203 0.1423 0.1283 -0.0086 0.0007  -0.0048 53  LEU   A N   
1379 C  CA  A LEU   A 53  ? 0.1323 0.1458 0.1201 -0.0076 0.0070  -0.0017 53  LEU   A CA  
1380 C  CA  B LEU   A 53  ? 0.1243 0.1435 0.1272 -0.0068 -0.0041 -0.0044 53  LEU   A CA  
1381 C  C   A LEU   A 53  ? 0.1282 0.1455 0.0931 0.0026  0.0041  0.0073  53  LEU   A C   
1382 C  C   B LEU   A 53  ? 0.1287 0.1447 0.1227 -0.0016 -0.0093 -0.0072 53  LEU   A C   
1383 O  O   A LEU   A 53  ? 0.1426 0.1587 0.1030 -0.0138 0.0061  0.0071  53  LEU   A O   
1384 O  O   B LEU   A 53  ? 0.1385 0.1474 0.1399 -0.0146 -0.0107 -0.0097 53  LEU   A O   
1385 C  CB  A LEU   A 53  ? 0.1425 0.1486 0.1342 -0.0103 0.0051  0.0102  53  LEU   A CB  
1386 C  CB  B LEU   A 53  ? 0.1218 0.1406 0.1280 -0.0050 -0.0057 0.0044  53  LEU   A CB  
1387 C  CG  A LEU   A 53  ? 0.1471 0.1458 0.1533 -0.0101 0.0039  0.0095  53  LEU   A CG  
1388 C  CG  B LEU   A 53  ? 0.1165 0.1328 0.1155 -0.0035 -0.0081 0.0073  53  LEU   A CG  
1389 C  CD1 A LEU   A 53  ? 0.1439 0.1508 0.1539 -0.0025 0.0101  0.0156  53  LEU   A CD1 
1390 C  CD1 B LEU   A 53  ? 0.1190 0.1388 0.1136 -0.0077 0.0029  -0.0009 53  LEU   A CD1 
1391 C  CD2 A LEU   A 53  ? 0.1547 0.1620 0.1600 -0.0160 0.0004  0.0149  53  LEU   A CD2 
1392 C  CD2 B LEU   A 53  ? 0.1112 0.1270 0.1066 -0.0021 -0.0009 0.0092  53  LEU   A CD2 
1415 N  N   A ASN   A 54  ? 0.1245 0.1321 0.1144 -0.0041 0.0007  0.0095  54  ASN   A N   
1416 N  N   B ASN   A 54  ? 0.1294 0.1410 0.1214 0.0002  -0.0109 -0.0085 54  ASN   A N   
1417 C  CA  A ASN   A 54  ? 0.1137 0.1297 0.1347 -0.0062 -0.0019 0.0035  54  ASN   A CA  
1418 C  CA  B ASN   A 54  ? 0.1247 0.1407 0.1177 0.0033  -0.0114 -0.0118 54  ASN   A CA  
1419 C  C   A ASN   A 54  ? 0.1230 0.1304 0.1382 -0.0119 0.0015  0.0078  54  ASN   A C   
1420 C  C   B ASN   A 54  ? 0.1324 0.1420 0.1082 0.0007  -0.0029 -0.0126 54  ASN   A C   
1421 O  O   A ASN   A 54  ? 0.1268 0.1389 0.1422 -0.0120 -0.0007 -0.0021 54  ASN   A O   
1422 O  O   B ASN   A 54  ? 0.1340 0.1483 0.1021 0.0012  -0.0015 -0.0193 54  ASN   A O   
1423 C  CB  A ASN   A 54  ? 0.1123 0.1265 0.1496 -0.0142 -0.0057 -0.0008 54  ASN   A CB  
1424 C  CB  B ASN   A 54  ? 0.1205 0.1373 0.1165 0.0094  -0.0068 -0.0140 54  ASN   A CB  
1425 C  CG  A ASN   A 54  ? 0.1174 0.1278 0.1490 -0.0082 -0.0060 0.0009  54  ASN   A CG  
1426 C  CG  B ASN   A 54  ? 0.1183 0.1307 0.0889 0.0144  -0.0020 -0.0215 54  ASN   A CG  
1427 O  OD1 A ASN   A 54  ? 0.1189 0.1292 0.1661 -0.0096 -0.0105 0.0201  54  ASN   A OD1 
1428 O  OD1 B ASN   A 54  ? 0.1135 0.1278 0.0872 0.0093  -0.0049 -0.0309 54  ASN   A OD1 
1429 N  ND2 A ASN   A 54  ? 0.1214 0.1338 0.1654 -0.0111 -0.0074 0.0081  54  ASN   A ND2 
1430 N  ND2 B ASN   A 54  ? 0.1246 0.1310 0.0899 0.0096  0.0033  -0.0085 54  ASN   A ND2 
1443 N  N   A LYS   A 55  ? 0.1236 0.1334 0.1402 -0.0071 -0.0037 -0.0016 55  LYS   A N   
1444 N  N   B LYS   A 55  ? 0.1357 0.1422 0.1130 0.0020  -0.0035 -0.0150 55  LYS   A N   
1445 C  CA  A LYS   A 55  ? 0.1303 0.1406 0.1553 -0.0025 -0.0079 -0.0115 55  LYS   A CA  
1446 C  CA  B LYS   A 55  ? 0.1420 0.1495 0.1338 0.0064  -0.0060 -0.0125 55  LYS   A CA  
1447 C  C   A LYS   A 55  ? 0.1289 0.1515 0.1478 -0.0053 0.0054  -0.0213 55  LYS   A C   
1448 C  C   B LYS   A 55  ? 0.1408 0.1536 0.1417 -0.0010 -0.0022 -0.0166 55  LYS   A C   
1449 O  O   A LYS   A 55  ? 0.1321 0.1637 0.1593 -0.0010 -0.0015 -0.0276 55  LYS   A O   
1450 O  O   B LYS   A 55  ? 0.1431 0.1552 0.1425 0.0043  -0.0042 -0.0177 55  LYS   A O   
1451 C  CB  A LYS   A 55  ? 0.1372 0.1434 0.1636 0.0065  -0.0148 -0.0293 55  LYS   A CB  
1452 C  CB  B LYS   A 55  ? 0.1462 0.1564 0.1541 0.0121  -0.0094 -0.0086 55  LYS   A CB  
1453 C  CG  A LYS   A 55  ? 0.1548 0.1753 0.1771 0.0171  -0.0266 -0.0377 55  LYS   A CG  
1454 C  CG  B LYS   A 55  ? 0.1517 0.1704 0.1841 0.0181  -0.0149 -0.0153 55  LYS   A CG  
1455 C  CD  A LYS   A 55  ? 0.1658 0.2057 0.1804 0.0260  -0.0246 -0.0397 55  LYS   A CD  
1456 C  CD  B LYS   A 55  ? 0.1569 0.1784 0.2069 0.0197  -0.0147 -0.0222 55  LYS   A CD  
1457 C  CE  A LYS   A 55  ? 0.1816 0.2328 0.1906 0.0385  -0.0317 -0.0453 55  LYS   A CE  
1458 C  CE  B LYS   A 55  ? 0.1705 0.1909 0.2313 0.0207  -0.0177 -0.0309 55  LYS   A CE  
1459 N  NZ  A LYS   A 55  ? 0.1875 0.2404 0.1963 0.0459  -0.0329 -0.0396 55  LYS   A NZ  
1460 N  NZ  B LYS   A 55  ? 0.1749 0.1965 0.2386 0.0216  -0.0206 -0.0381 55  LYS   A NZ  
1487 N  N   . ALA   A 56  ? 0.1388 0.1579 0.1473 -0.0124 0.0026  -0.0174 56  ALA   A N   
1488 C  CA  . ALA   A 56  ? 0.1480 0.1805 0.1455 -0.0177 0.0126  -0.0183 56  ALA   A CA  
1489 C  C   . ALA   A 56  ? 0.1491 0.1891 0.1249 -0.0139 0.0113  -0.0225 56  ALA   A C   
1490 O  O   . ALA   A 56  ? 0.1585 0.2208 0.1363 0.0001  0.0125  -0.0181 56  ALA   A O   
1491 C  CB  . ALA   A 56  ? 0.1551 0.1978 0.1536 -0.0222 0.0165  -0.0088 56  ALA   A CB  
1498 N  N   . THR   A 57  ? 0.1400 0.1689 0.1251 -0.0144 0.0061  -0.0166 57  THR   A N   
1499 C  CA  . THR   A 57  ? 0.1437 0.1663 0.1228 -0.0132 -0.0025 -0.0116 57  THR   A CA  
1500 C  C   . THR   A 57  ? 0.1448 0.1695 0.1310 -0.0080 -0.0052 -0.0166 57  THR   A C   
1501 O  O   . THR   A 57  ? 0.1438 0.1755 0.1549 -0.0129 -0.0160 -0.0302 57  THR   A O   
1502 C  CB  . THR   A 57  ? 0.1417 0.1657 0.1265 -0.0099 -0.0012 -0.0098 57  THR   A CB  
1503 O  OG1 . THR   A 57  ? 0.1280 0.1585 0.1312 -0.0079 -0.0014 -0.0083 57  THR   A OG1 
1504 C  CG2 . THR   A 57  ? 0.1466 0.1679 0.1298 -0.0091 -0.0031 0.0016  57  THR   A CG2 
1512 N  N   . ASN   A 58  ? 0.1434 0.1653 0.1562 -0.0082 0.0044  -0.0248 58  ASN   A N   
1513 C  CA  . ASN   A 58  ? 0.1627 0.1592 0.1732 -0.0158 0.0100  -0.0366 58  ASN   A CA  
1514 C  C   . ASN   A 58  ? 0.1434 0.1506 0.1649 -0.0082 -0.0070 -0.0224 58  ASN   A C   
1515 O  O   . ASN   A 58  ? 0.1456 0.1609 0.1732 -0.0164 -0.0031 -0.0265 58  ASN   A O   
1516 C  CB  . ASN   A 58  ? 0.2049 0.1785 0.2203 -0.0234 0.0331  -0.0535 58  ASN   A CB  
1517 C  CG  . ASN   A 58  ? 0.2499 0.2057 0.2891 -0.0206 0.0323  -0.0436 58  ASN   A CG  
1518 O  OD1 . ASN   A 58  ? 0.2801 0.2056 0.3268 0.0130  0.0648  -0.0330 58  ASN   A OD1 
1519 N  ND2 . ASN   A 58  ? 0.2614 0.2165 0.3182 -0.0217 0.0174  -0.0473 58  ASN   A ND2 
1526 N  N   . ASN   A 59  ? 0.1278 0.1415 0.1582 -0.0077 -0.0109 -0.0123 59  ASN   A N   
1527 C  CA  . ASN   A 59  ? 0.1303 0.1321 0.1546 -0.0037 -0.0087 -0.0070 59  ASN   A CA  
1528 C  C   . ASN   A 59  ? 0.1336 0.1335 0.1413 -0.0063 -0.0073 -0.0069 59  ASN   A C   
1529 O  O   . ASN   A 59  ? 0.1322 0.1380 0.1500 -0.0063 0.0005  0.0021  59  ASN   A O   
1530 C  CB  . ASN   A 59  ? 0.1341 0.1302 0.1579 0.0019  -0.0173 -0.0152 59  ASN   A CB  
1531 C  CG  . ASN   A 59  ? 0.1368 0.1399 0.1551 -0.0012 -0.0297 0.0027  59  ASN   A CG  
1532 O  OD1 . ASN   A 59  ? 0.1524 0.1449 0.1462 -0.0115 -0.0258 0.0029  59  ASN   A OD1 
1533 N  ND2 . ASN   A 59  ? 0.1438 0.1428 0.1700 -0.0140 -0.0155 0.0040  59  ASN   A ND2 
1540 N  N   . ALA   A 60  ? 0.1264 0.1420 0.1400 -0.0068 -0.0046 -0.0055 60  ALA   A N   
1541 C  CA  . ALA   A 60  ? 0.1252 0.1417 0.1496 -0.0033 -0.0134 -0.0016 60  ALA   A CA  
1542 C  C   . ALA   A 60  ? 0.1276 0.1381 0.1506 -0.0029 -0.0089 -0.0028 60  ALA   A C   
1543 O  O   . ALA   A 60  ? 0.1253 0.1350 0.1719 -0.0046 -0.0108 -0.0065 60  ALA   A O   
1544 C  CB  . ALA   A 60  ? 0.1408 0.1522 0.1491 -0.0022 -0.0137 -0.0117 60  ALA   A CB  
1550 N  N   . MET   A 61  ? 0.1199 0.1325 0.1437 -0.0081 -0.0035 -0.0060 61  MET   A N   
1551 C  CA  . MET   A 61  ? 0.1260 0.1257 0.1359 -0.0068 0.0006  -0.0000 61  MET   A CA  
1552 C  C   . MET   A 61  ? 0.1208 0.1242 0.1461 -0.0064 -0.0038 -0.0035 61  MET   A C   
1553 O  O   . MET   A 61  ? 0.1234 0.1282 0.1542 -0.0058 0.0039  0.0016  61  MET   A O   
1554 C  CB  . MET   A 61  ? 0.1306 0.1297 0.1253 -0.0108 -0.0003 -0.0028 61  MET   A CB  
1555 C  CG  . MET   A 61  ? 0.1270 0.1390 0.1520 -0.0016 -0.0028 0.0027  61  MET   A CG  
1556 S  SD  . MET   A 61  ? 0.1318 0.1383 0.1799 -0.0122 -0.0012 -0.0145 61  MET   A SD  
1557 C  CE  . MET   A 61  ? 0.1509 0.1454 0.2052 -0.0157 0.0145  -0.0077 61  MET   A CE  
1567 N  N   . GLN   A 62  ? 0.1205 0.1234 0.1447 -0.0076 -0.0045 0.0004  62  GLN   A N   
1568 C  CA  . GLN   A 62  ? 0.1275 0.1238 0.1454 -0.0070 0.0009  0.0036  62  GLN   A CA  
1569 C  C   . GLN   A 62  ? 0.1236 0.1152 0.1533 -0.0027 0.0056  0.0011  62  GLN   A C   
1570 O  O   . GLN   A 62  ? 0.1267 0.1320 0.1493 -0.0048 0.0047  0.0017  62  GLN   A O   
1571 C  CB  . GLN   A 62  ? 0.1265 0.1203 0.1494 -0.0019 0.0024  0.0098  62  GLN   A CB  
1572 C  CG  . GLN   A 62  ? 0.1311 0.1143 0.1526 -0.0045 -0.0051 0.0150  62  GLN   A CG  
1573 C  CD  . GLN   A 62  ? 0.1363 0.1220 0.1486 -0.0018 0.0048  0.0141  62  GLN   A CD  
1574 O  OE1 . GLN   A 62  ? 0.1376 0.1390 0.1545 -0.0063 0.0017  0.0049  62  GLN   A OE1 
1575 N  NE2 . GLN   A 62  ? 0.1426 0.1303 0.1533 -0.0022 0.0028  -0.0036 62  GLN   A NE2 
1584 N  N   . VAL   A 63  ? 0.1188 0.1238 0.1728 -0.0087 0.0045  -0.0150 63  VAL   A N   
1585 C  CA  . VAL   A 63  ? 0.1242 0.1371 0.1838 -0.0145 0.0051  -0.0111 63  VAL   A CA  
1586 C  C   . VAL   A 63  ? 0.1152 0.1311 0.1755 -0.0137 -0.0060 -0.0050 63  VAL   A C   
1587 O  O   . VAL   A 63  ? 0.1163 0.1353 0.1973 -0.0171 -0.0055 -0.0039 63  VAL   A O   
1588 C  CB  . VAL   A 63  ? 0.1365 0.1491 0.2191 -0.0151 -0.0042 -0.0340 63  VAL   A CB  
1589 C  CG1 . VAL   A 63  ? 0.1504 0.1649 0.2540 -0.0155 -0.0106 -0.0566 63  VAL   A CG1 
1590 C  CG2 . VAL   A 63  ? 0.1459 0.1451 0.2308 -0.0100 0.0095  -0.0233 63  VAL   A CG2 
1600 N  N   . GLU   A 64  ? 0.1203 0.1386 0.1577 -0.0069 -0.0035 -0.0051 64  GLU   A N   
1601 C  CA  . GLU   A 64  ? 0.1198 0.1357 0.1765 -0.0082 -0.0100 -0.0020 64  GLU   A CA  
1602 C  C   . GLU   A 64  ? 0.1137 0.1308 0.1750 -0.0108 0.0014  0.0041  64  GLU   A C   
1603 O  O   . GLU   A 64  ? 0.1236 0.1362 0.1740 -0.0027 -0.0010 -0.0019 64  GLU   A O   
1604 C  CB  . GLU   A 64  ? 0.1263 0.1466 0.1639 -0.0091 0.0003  -0.0012 64  GLU   A CB  
1605 C  CG  . GLU   A 64  ? 0.1357 0.1559 0.1800 -0.0114 0.0013  -0.0010 64  GLU   A CG  
1606 C  CD  . GLU   A 64  ? 0.1454 0.1620 0.1793 -0.0168 0.0098  0.0017  64  GLU   A CD  
1607 O  OE1 . GLU   A 64  ? 0.1455 0.1727 0.1966 -0.0233 0.0107  0.0014  64  GLU   A OE1 
1608 O  OE2 . GLU   A 64  ? 0.1655 0.1595 0.1716 -0.0215 -0.0065 0.0102  64  GLU   A OE2 
1615 N  N   . SER   A 65  ? 0.1095 0.1331 0.1558 -0.0010 0.0027  0.0042  65  SER   A N   
1616 C  CA  . SER   A 65  ? 0.1211 0.1277 0.1485 -0.0044 -0.0014 -0.0001 65  SER   A CA  
1617 C  C   . SER   A 65  ? 0.1193 0.1334 0.1517 -0.0047 -0.0043 -0.0030 65  SER   A C   
1618 O  O   . SER   A 65  ? 0.1291 0.1385 0.1676 -0.0001 0.0135  -0.0036 65  SER   A O   
1619 C  CB  . SER   A 65  ? 0.1276 0.1267 0.1524 -0.0091 0.0029  0.0067  65  SER   A CB  
1620 O  OG  . SER   A 65  ? 0.1229 0.1409 0.1553 -0.0093 -0.0062 0.0110  65  SER   A OG  
1626 N  N   . ASP   A 66  ? 0.1251 0.1290 0.1553 -0.0066 0.0095  0.0033  66  ASP   A N   
1627 C  CA  . ASP   A 66  ? 0.1321 0.1411 0.1793 -0.0052 0.0090  0.0165  66  ASP   A CA  
1628 C  C   . ASP   A 66  ? 0.1274 0.1387 0.1795 -0.0091 0.0082  0.0171  66  ASP   A C   
1629 O  O   . ASP   A 66  ? 0.1351 0.1466 0.1971 -0.0053 0.0286  0.0222  66  ASP   A O   
1630 C  CB  . ASP   A 66  ? 0.1402 0.1472 0.2081 0.0040  0.0169  0.0328  66  ASP   A CB  
1631 C  CG  . ASP   A 66  ? 0.1700 0.1634 0.2326 -0.0026 0.0025  0.0525  66  ASP   A CG  
1632 O  OD1 . ASP   A 66  ? 0.1710 0.1938 0.2039 -0.0104 -0.0058 0.0544  66  ASP   A OD1 
1633 O  OD2 . ASP   A 66  ? 0.1853 0.1724 0.3046 0.0170  -0.0189 0.0313  66  ASP   A OD2 
1638 N  N   . ASP   A 67  ? 0.1241 0.1368 0.1907 -0.0086 0.0070  0.0206  67  ASP   A N   
1639 C  CA  . ASP   A 67  ? 0.1230 0.1559 0.2075 -0.0047 0.0046  0.0245  67  ASP   A CA  
1640 C  C   . ASP   A 67  ? 0.1260 0.1533 0.1953 0.0004  0.0099  0.0270  67  ASP   A C   
1641 O  O   . ASP   A 67  ? 0.1237 0.1605 0.2147 0.0000  0.0245  0.0300  67  ASP   A O   
1642 C  CB  . ASP   A 67  ? 0.1339 0.1631 0.2404 -0.0089 -0.0164 0.0309  67  ASP   A CB  
1643 C  CG  . ASP   A 67  ? 0.1307 0.1763 0.2754 -0.0132 -0.0298 0.0409  67  ASP   A CG  
1644 O  OD1 . ASP   A 67  ? 0.1374 0.1945 0.3475 -0.0174 -0.0359 0.0560  67  ASP   A OD1 
1645 O  OD2 . ASP   A 67  ? 0.1335 0.1786 0.2633 -0.0019 -0.0161 0.0290  67  ASP   A OD2 
1650 N  N   . TYR   A 68  ? 0.1249 0.1417 0.1942 0.0034  0.0148  0.0286  68  TYR   A N   
1651 C  CA  . TYR   A 68  ? 0.1395 0.1383 0.1918 0.0008  0.0198  0.0261  68  TYR   A CA  
1652 C  C   . TYR   A 68  ? 0.1313 0.1408 0.1943 -0.0012 0.0192  0.0181  68  TYR   A C   
1653 O  O   . TYR   A 68  ? 0.1365 0.1451 0.1954 0.0079  0.0271  0.0176  68  TYR   A O   
1654 C  CB  . TYR   A 68  ? 0.1369 0.1339 0.2061 0.0052  0.0390  0.0232  68  TYR   A CB  
1655 C  CG  . TYR   A 68  ? 0.1464 0.1533 0.2350 0.0027  0.0474  0.0291  68  TYR   A CG  
1656 C  CD1 . TYR   A 68  ? 0.1578 0.1606 0.2553 -0.0179 0.0413  -0.0013 68  TYR   A CD1 
1657 C  CD2 . TYR   A 68  ? 0.1659 0.1562 0.2670 0.0115  0.0479  0.0447  68  TYR   A CD2 
1658 C  CE1 . TYR   A 68  ? 0.1659 0.1695 0.2852 -0.0184 0.0447  -0.0025 68  TYR   A CE1 
1659 C  CE2 . TYR   A 68  ? 0.1661 0.1627 0.2881 0.0013  0.0585  0.0245  68  TYR   A CE2 
1660 C  CZ  . TYR   A 68  ? 0.1703 0.1657 0.2947 -0.0177 0.0496  -0.0054 68  TYR   A CZ  
1661 O  OH  . TYR   A 68  ? 0.1918 0.1626 0.3099 -0.0120 0.0250  -0.0266 68  TYR   A OH  
1671 N  N   . ILE   A 69  ? 0.1251 0.1314 0.1823 -0.0015 0.0243  0.0169  69  ILE   A N   
1672 C  CA  . ILE   A 69  ? 0.1338 0.1359 0.1758 0.0053  0.0168  0.0082  69  ILE   A CA  
1673 C  C   . ILE   A 69  ? 0.1383 0.1368 0.1726 0.0067  0.0180  0.0184  69  ILE   A C   
1674 O  O   . ILE   A 69  ? 0.1440 0.1420 0.1786 -0.0002 0.0253  0.0165  69  ILE   A O   
1675 C  CB  . ILE   A 69  ? 0.1426 0.1584 0.1755 0.0033  0.0201  0.0065  69  ILE   A CB  
1676 C  CG1 . ILE   A 69  ? 0.1396 0.1649 0.1856 0.0050  0.0160  -0.0170 69  ILE   A CG1 
1677 C  CG2 . ILE   A 69  ? 0.1616 0.1773 0.1896 0.0058  0.0102  -0.0034 69  ILE   A CG2 
1678 C  CD1 . ILE   A 69  ? 0.1415 0.1775 0.2067 -0.0051 0.0120  -0.0194 69  ILE   A CD1 
1690 N  N   . ALA   A 70  ? 0.1413 0.1417 0.1848 -0.0054 0.0233  0.0213  70  ALA   A N   
1691 C  CA  . ALA   A 70  ? 0.1452 0.1542 0.2009 -0.0157 0.0290  0.0211  70  ALA   A CA  
1692 C  C   . ALA   A 70  ? 0.1386 0.1686 0.2032 -0.0111 0.0254  0.0213  70  ALA   A C   
1693 O  O   . ALA   A 70  ? 0.1591 0.2003 0.2259 0.0062  0.0432  0.0398  70  ALA   A O   
1694 C  CB  . ALA   A 70  ? 0.1493 0.1509 0.2285 -0.0229 0.0256  0.0178  70  ALA   A CB  
1700 N  N   . THR   A 71  ? 0.1334 0.1648 0.1949 -0.0037 0.0191  0.0170  71  THR   A N   
1701 C  CA  . THR   A 71  ? 0.1460 0.1790 0.2252 0.0035  0.0191  0.0210  71  THR   A CA  
1702 C  C   . THR   A 71  ? 0.1385 0.1711 0.2452 0.0085  0.0301  0.0175  71  THR   A C   
1703 O  O   . THR   A 71  ? 0.1444 0.1963 0.2901 0.0083  0.0384  -0.0016 71  THR   A O   
1704 C  CB  . THR   A 71  ? 0.1721 0.2046 0.2593 0.0143  -0.0128 0.0304  71  THR   A CB  
1705 O  OG1 . THR   A 71  ? 0.1971 0.2219 0.2692 0.0050  -0.0328 0.0281  71  THR   A OG1 
1706 C  CG2 . THR   A 71  ? 0.1834 0.2215 0.2913 0.0252  -0.0250 0.0379  71  THR   A CG2 
1714 N  N   . ASN   A 72  ? 0.1414 0.1534 0.2213 0.0090  0.0263  0.0178  72  ASN   A N   
1715 C  CA  . ASN   A 72  ? 0.1434 0.1558 0.2279 0.0126  0.0340  0.0128  72  ASN   A CA  
1716 C  C   . ASN   A 72  ? 0.1549 0.1513 0.2159 0.0068  0.0454  0.0099  72  ASN   A C   
1717 O  O   . ASN   A 72  ? 0.1766 0.1511 0.2374 0.0105  0.0458  -0.0039 72  ASN   A O   
1718 C  CB  . ASN   A 72  ? 0.1625 0.1625 0.2288 0.0104  0.0359  0.0171  72  ASN   A CB  
1719 C  CG  . ASN   A 72  ? 0.1858 0.1774 0.2353 0.0206  0.0293  0.0239  72  ASN   A CG  
1720 O  OD1 . ASN   A 72  ? 0.2003 0.2127 0.2442 0.0264  0.0364  0.0254  72  ASN   A OD1 
1721 N  ND2 . ASN   A 72  ? 0.2012 0.1711 0.2444 0.0475  0.0100  0.0159  72  ASN   A ND2 
1728 N  N   . GLY   A 73  ? 0.1576 0.1511 0.2028 0.0000  0.0402  0.0099  73  GLY   A N   
1729 C  CA  . GLY   A 73  ? 0.1613 0.1473 0.1903 -0.0074 0.0404  0.0095  73  GLY   A CA  
1730 C  C   . GLY   A 73  ? 0.1602 0.1390 0.1781 -0.0030 0.0518  0.0203  73  GLY   A C   
1731 O  O   . GLY   A 73  ? 0.1590 0.1454 0.1915 0.0094  0.0375  0.0294  73  GLY   A O   
1735 N  N   . PRO   A 74  ? 0.1739 0.1427 0.1785 -0.0175 0.0474  0.0132  74  PRO   A N   
1736 C  CA  . PRO   A 74  ? 0.1691 0.1402 0.1839 -0.0059 0.0474  0.0162  74  PRO   A CA  
1737 C  C   . PRO   A 74  ? 0.1602 0.1272 0.1872 -0.0027 0.0354  0.0039  74  PRO   A C   
1738 O  O   . PRO   A 74  ? 0.1664 0.1354 0.2130 0.0018  0.0383  -0.0021 74  PRO   A O   
1739 C  CB  . PRO   A 74  ? 0.1846 0.1659 0.2051 -0.0032 0.0437  0.0202  74  PRO   A CB  
1740 C  CG  . PRO   A 74  ? 0.2090 0.1980 0.2449 -0.0200 0.0340  0.0121  74  PRO   A CG  
1741 C  CD  . PRO   A 74  ? 0.1890 0.1751 0.1999 -0.0265 0.0321  0.0008  74  PRO   A CD  
1749 N  N   . LEU   A 75  ? 0.1564 0.1203 0.1672 -0.0018 0.0252  0.0047  75  LEU   A N   
1750 C  CA  . LEU   A 75  ? 0.1584 0.1222 0.1534 -0.0001 0.0096  0.0087  75  LEU   A CA  
1751 C  C   . LEU   A 75  ? 0.1680 0.1334 0.1539 0.0070  0.0115  0.0156  75  LEU   A C   
1752 O  O   . LEU   A 75  ? 0.2029 0.1529 0.1604 0.0120  0.0093  0.0125  75  LEU   A O   
1753 C  CB  . LEU   A 75  ? 0.1628 0.1308 0.1508 -0.0104 0.0075  0.0195  75  LEU   A CB  
1754 C  CG  . LEU   A 75  ? 0.1779 0.1684 0.1524 -0.0358 0.0014  0.0145  75  LEU   A CG  
1755 C  CD1 . LEU   A 75  ? 0.1924 0.2160 0.1679 -0.0378 -0.0011 -0.0022 75  LEU   A CD1 
1756 C  CD2 . LEU   A 75  ? 0.2060 0.2020 0.2093 -0.0116 -0.0000 0.0208  75  LEU   A CD2 
1768 N  N   . LYS   A 76  ? 0.1662 0.1339 0.1639 -0.0036 0.0116  0.0013  76  LYS   A N   
1769 C  CA  . LYS   A 76  ? 0.1669 0.1508 0.1697 -0.0047 0.0145  -0.0043 76  LYS   A CA  
1770 C  C   . LYS   A 76  ? 0.1603 0.1368 0.1420 -0.0006 0.0128  0.0097  76  LYS   A C   
1771 O  O   . LYS   A 76  ? 0.1652 0.1311 0.1450 -0.0036 0.0145  0.0133  76  LYS   A O   
1772 C  CB  . LYS   A 76  ? 0.1685 0.1740 0.2066 0.0022  0.0188  -0.0271 76  LYS   A CB  
1773 C  CG  . LYS   A 76  ? 0.1776 0.1708 0.2546 0.0073  0.0144  -0.0237 76  LYS   A CG  
1774 C  CD  . LYS   A 76  ? 0.1842 0.1696 0.3006 0.0126  0.0011  -0.0290 76  LYS   A CD  
1775 C  CE  . LYS   A 76  ? 0.1994 0.1928 0.3597 0.0024  0.0063  -0.0330 76  LYS   A CE  
1776 N  NZ  . LYS   A 76  ? 0.1972 0.1888 0.3937 -0.0111 0.0057  -0.0467 76  LYS   A NZ  
1790 N  N   . VAL   A 77  ? 0.1719 0.1415 0.1447 -0.0008 0.0209  0.0111  77  VAL   A N   
1791 C  CA  . VAL   A 77  ? 0.1686 0.1436 0.1380 0.0063  0.0167  0.0070  77  VAL   A CA  
1792 C  C   . VAL   A 77  ? 0.1622 0.1357 0.1419 0.0051  0.0136  0.0087  77  VAL   A C   
1793 O  O   . VAL   A 77  ? 0.1679 0.1425 0.1475 0.0083  0.0292  -0.0050 77  VAL   A O   
1794 C  CB  . VAL   A 77  ? 0.1820 0.1599 0.1478 0.0025  0.0106  0.0190  77  VAL   A CB  
1795 C  CG1 . VAL   A 77  ? 0.1763 0.1758 0.1707 0.0080  0.0090  0.0079  77  VAL   A CG1 
1796 C  CG2 . VAL   A 77  ? 0.2073 0.1694 0.1717 -0.0030 -0.0013 0.0241  77  VAL   A CG2 
1806 N  N   . GLY   A 78  ? 0.1535 0.1352 0.1414 0.0029  0.0176  0.0079  78  GLY   A N   
1807 C  CA  . GLY   A 78  ? 0.1521 0.1325 0.1462 0.0010  0.0225  0.0121  78  GLY   A CA  
1808 C  C   . GLY   A 78  ? 0.1410 0.1285 0.1547 0.0012  0.0259  0.0104  78  GLY   A C   
1809 O  O   . GLY   A 78  ? 0.1391 0.1375 0.1670 0.0001  0.0184  0.0227  78  GLY   A O   
1813 N  N   . GLY   A 79  ? 0.1446 0.1250 0.1482 -0.0022 0.0178  0.0159  79  GLY   A N   
1814 C  CA  . GLY   A 79  ? 0.1452 0.1317 0.1589 0.0009  0.0222  0.0149  79  GLY   A CA  
1815 C  C   . GLY   A 79  ? 0.1319 0.1257 0.1501 -0.0000 0.0142  0.0078  79  GLY   A C   
1816 O  O   . GLY   A 79  ? 0.1334 0.1349 0.1653 0.0164  0.0097  0.0067  79  GLY   A O   
1820 N  N   . SER   A 80  ? 0.1294 0.1391 0.1734 0.0000  0.0127  0.0026  80  SER   A N   
1821 C  CA  . SER   A 80  ? 0.1254 0.1300 0.1656 0.0004  0.0089  0.0036  80  SER   A CA  
1822 C  C   . SER   A 80  ? 0.1235 0.1339 0.1645 -0.0028 0.0071  0.0094  80  SER   A C   
1823 O  O   . SER   A 80  ? 0.1253 0.1555 0.1932 0.0046  0.0144  0.0006  80  SER   A O   
1824 C  CB  . SER   A 80  ? 0.1424 0.1328 0.1855 -0.0038 0.0095  0.0048  80  SER   A CB  
1825 O  OG  . SER   A 80  ? 0.1671 0.1334 0.2177 0.0034  -0.0015 0.0254  80  SER   A OG  
1831 N  N   . CYS   A 81  ? 0.1198 0.1285 0.1640 -0.0035 -0.0054 0.0140  81  CYS   A N   
1832 C  CA  . CYS   A 81  ? 0.1217 0.1414 0.1585 -0.0053 -0.0072 0.0208  81  CYS   A CA  
1833 C  C   . CYS   A 81  ? 0.1223 0.1329 0.1558 -0.0102 -0.0005 0.0303  81  CYS   A C   
1834 O  O   . CYS   A 81  ? 0.1209 0.1633 0.1702 -0.0016 -0.0001 0.0372  81  CYS   A O   
1835 C  CB  . CYS   A 81  ? 0.1285 0.1443 0.1699 -0.0141 -0.0022 0.0286  81  CYS   A CB  
1836 S  SG  . CYS   A 81  ? 0.1413 0.1327 0.1675 -0.0156 -0.0005 0.0170  81  CYS   A SG  
1842 N  N   . VAL   A 82  ? 0.1257 0.1403 0.1587 -0.0016 -0.0109 0.0261  82  VAL   A N   
1843 C  CA  . VAL   A 82  ? 0.1388 0.1454 0.1555 -0.0015 -0.0092 0.0349  82  VAL   A CA  
1844 C  C   . VAL   A 82  ? 0.1347 0.1489 0.1647 -0.0030 -0.0091 0.0319  82  VAL   A C   
1845 O  O   . VAL   A 82  ? 0.1282 0.1549 0.1906 -0.0035 -0.0108 0.0015  82  VAL   A O   
1846 C  CB  . VAL   A 82  ? 0.1670 0.1629 0.1770 0.0014  -0.0011 0.0299  82  VAL   A CB  
1847 C  CG1 . VAL   A 82  ? 0.1886 0.1695 0.1930 0.0098  -0.0001 0.0317  82  VAL   A CG1 
1848 C  CG2 . VAL   A 82  ? 0.1732 0.1690 0.2098 -0.0076 -0.0073 0.0359  82  VAL   A CG2 
1858 N  N   . LEU   A 83  ? 0.1289 0.1487 0.1507 -0.0102 -0.0127 0.0163  83  LEU   A N   
1859 C  CA  . LEU   A 83  ? 0.1322 0.1510 0.1403 -0.0141 -0.0098 0.0133  83  LEU   A CA  
1860 C  C   . LEU   A 83  ? 0.1362 0.1536 0.1443 -0.0142 -0.0159 0.0168  83  LEU   A C   
1861 O  O   . LEU   A 83  ? 0.1472 0.1558 0.1537 -0.0220 -0.0107 0.0256  83  LEU   A O   
1862 C  CB  . LEU   A 83  ? 0.1394 0.1546 0.1503 -0.0126 -0.0083 0.0146  83  LEU   A CB  
1863 C  CG  . LEU   A 83  ? 0.1501 0.1617 0.1530 -0.0114 0.0042  0.0062  83  LEU   A CG  
1864 C  CD1 . LEU   A 83  ? 0.1672 0.1589 0.1671 -0.0251 0.0000  0.0212  83  LEU   A CD1 
1865 C  CD2 . LEU   A 83  ? 0.1493 0.1775 0.1710 -0.0145 0.0127  0.0159  83  LEU   A CD2 
1877 N  N   . SER   A 84  ? 0.1511 0.1608 0.1407 -0.0174 -0.0121 0.0228  84  SER   A N   
1878 C  CA  . SER   A 84  ? 0.1601 0.1660 0.1300 -0.0190 -0.0146 0.0190  84  SER   A CA  
1879 C  C   . SER   A 84  ? 0.1621 0.1618 0.1321 -0.0234 -0.0020 0.0150  84  SER   A C   
1880 O  O   . SER   A 84  ? 0.1558 0.1734 0.1307 -0.0169 -0.0096 0.0164  84  SER   A O   
1881 C  CB  . SER   A 84  ? 0.1686 0.1896 0.1441 -0.0134 -0.0076 0.0097  84  SER   A CB  
1882 O  OG  . SER   A 84  ? 0.1729 0.2082 0.1558 -0.0158 -0.0187 -0.0031 84  SER   A OG  
1888 N  N   . GLY   A 85  ? 0.1771 0.1770 0.1395 -0.0262 0.0061  0.0121  85  GLY   A N   
1889 C  CA  . GLY   A 85  ? 0.1778 0.1799 0.1472 -0.0268 0.0115  0.0010  85  GLY   A CA  
1890 C  C   . GLY   A 85  ? 0.1727 0.1865 0.1292 -0.0242 -0.0051 0.0044  85  GLY   A C   
1891 O  O   . GLY   A 85  ? 0.1709 0.1965 0.1502 -0.0326 0.0075  -0.0106 85  GLY   A O   
1895 N  N   . HIS   A 86  ? 0.1752 0.1828 0.1252 -0.0194 -0.0104 0.0076  86  HIS   A N   
1896 C  CA  . HIS   A 86  ? 0.1918 0.1911 0.1148 -0.0223 -0.0061 0.0068  86  HIS   A CA  
1897 C  C   . HIS   A 86  ? 0.2136 0.2033 0.1126 -0.0302 -0.0140 0.0018  86  HIS   A C   
1898 O  O   . HIS   A 86  ? 0.2237 0.2294 0.1294 -0.0202 -0.0032 0.0065  86  HIS   A O   
1899 C  CB  . HIS   A 86  ? 0.1904 0.1811 0.1277 -0.0183 0.0001  0.0075  86  HIS   A CB  
1900 C  CG  . HIS   A 86  ? 0.1856 0.1797 0.1331 -0.0094 -0.0007 0.0120  86  HIS   A CG  
1901 N  ND1 . HIS   A 86  ? 0.1902 0.1752 0.1716 -0.0262 -0.0015 0.0112  86  HIS   A ND1 
1902 C  CD2 . HIS   A 86  ? 0.1809 0.1749 0.1276 0.0003  -0.0035 0.0195  86  HIS   A CD2 
1903 C  CE1 . HIS   A 86  ? 0.1801 0.1816 0.1683 -0.0174 0.0116  0.0139  86  HIS   A CE1 
1904 N  NE2 . HIS   A 86  ? 0.1785 0.1776 0.1493 0.0041  0.0074  0.0261  86  HIS   A NE2 
1912 N  N   . ASN   A 87  ? 0.2301 0.2135 0.1331 -0.0262 0.0082  -0.0124 87  ASN   A N   
1913 C  CA  . ASN   A 87  ? 0.2487 0.2224 0.1380 -0.0227 0.0303  -0.0162 87  ASN   A CA  
1914 C  C   . ASN   A 87  ? 0.2466 0.2373 0.1697 -0.0263 0.0532  -0.0010 87  ASN   A C   
1915 O  O   . ASN   A 87  ? 0.2682 0.2550 0.2096 -0.0401 0.0823  -0.0086 87  ASN   A O   
1916 C  CB  . ASN   A 87  ? 0.2643 0.2287 0.1379 -0.0138 0.0272  -0.0174 87  ASN   A CB  
1917 C  CG  . ASN   A 87  ? 0.2793 0.2399 0.1477 -0.0029 0.0397  -0.0075 87  ASN   A CG  
1918 O  OD1 . ASN   A 87  ? 0.2933 0.2406 0.1525 0.0132  0.0433  -0.0035 87  ASN   A OD1 
1919 N  ND2 . ASN   A 87  ? 0.2826 0.2611 0.1670 -0.0008 0.0437  -0.0033 87  ASN   A ND2 
1926 N  N   . LEU   A 88  ? 0.2187 0.2250 0.1603 -0.0294 0.0322  0.0113  88  LEU   A N   
1927 C  CA  . LEU   A 88  ? 0.1960 0.2219 0.1758 -0.0331 0.0322  0.0234  88  LEU   A CA  
1928 C  C   . LEU   A 88  ? 0.1910 0.2280 0.1668 -0.0331 0.0287  0.0302  88  LEU   A C   
1929 O  O   . LEU   A 88  ? 0.1939 0.2334 0.2020 -0.0306 0.0306  0.0514  88  LEU   A O   
1930 C  CB  . LEU   A 88  ? 0.1927 0.2304 0.1768 -0.0373 -0.0069 0.0346  88  LEU   A CB  
1931 C  CG  . LEU   A 88  ? 0.2116 0.2429 0.2073 -0.0397 -0.0236 0.0380  88  LEU   A CG  
1932 C  CD1 . LEU   A 88  ? 0.2250 0.2527 0.2087 -0.0417 -0.0257 0.0334  88  LEU   A CD1 
1933 C  CD2 . LEU   A 88  ? 0.2249 0.2520 0.2523 -0.0301 -0.0166 0.0270  88  LEU   A CD2 
1945 N  N   . ALA   A 89  ? 0.1888 0.2222 0.1425 -0.0333 0.0146  0.0124  89  ALA   A N   
1946 C  CA  . ALA   A 89  ? 0.1969 0.2195 0.1277 -0.0287 0.0016  0.0201  89  ALA   A CA  
1947 C  C   . ALA   A 89  ? 0.2030 0.2210 0.1427 -0.0266 -0.0131 0.0219  89  ALA   A C   
1948 O  O   . ALA   A 89  ? 0.1972 0.2175 0.1742 -0.0324 -0.0168 -0.0002 89  ALA   A O   
1949 C  CB  . ALA   A 89  ? 0.1908 0.2151 0.1210 -0.0218 -0.0005 0.0179  89  ALA   A CB  
1955 N  N   . LYS   A 90  ? 0.2110 0.2350 0.1447 -0.0353 -0.0224 0.0288  90  LYS   A N   
1956 C  CA  . LYS   A 90  ? 0.2225 0.2483 0.1526 -0.0324 -0.0363 0.0333  90  LYS   A CA  
1957 C  C   . LYS   A 90  ? 0.1992 0.2267 0.1461 -0.0344 -0.0348 0.0171  90  LYS   A C   
1958 O  O   . LYS   A 90  ? 0.2046 0.2406 0.1699 -0.0328 -0.0412 0.0104  90  LYS   A O   
1959 C  CB  . LYS   A 90  ? 0.2561 0.2909 0.1867 -0.0295 -0.0457 0.0567  90  LYS   A CB  
1960 C  CG  . LYS   A 90  ? 0.3069 0.3352 0.2927 -0.0290 -0.0441 0.0576  90  LYS   A CG  
1961 C  CD  . LYS   A 90  ? 0.3655 0.3852 0.4013 -0.0321 -0.0299 0.0582  90  LYS   A CD  
1962 C  CE  . LYS   A 90  ? 0.4080 0.4225 0.4863 -0.0343 -0.0189 0.0531  90  LYS   A CE  
1963 N  NZ  . LYS   A 90  ? 0.4363 0.4363 0.5383 -0.0361 -0.0122 0.0482  90  LYS   A NZ  
1977 N  N   . HIS   A 91  ? 0.1832 0.2004 0.1231 -0.0293 -0.0364 0.0224  91  HIS   A N   
1978 C  CA  . HIS   A 91  ? 0.1710 0.1842 0.1321 -0.0177 -0.0280 0.0246  91  HIS   A CA  
1979 C  C   . HIS   A 91  ? 0.1545 0.1694 0.1233 -0.0200 -0.0155 0.0240  91  HIS   A C   
1980 O  O   . HIS   A 91  ? 0.1515 0.1855 0.1371 -0.0263 -0.0051 0.0253  91  HIS   A O   
1981 C  CB  . HIS   A 91  ? 0.1879 0.2111 0.1736 0.0044  -0.0435 0.0318  91  HIS   A CB  
1982 C  CG  . HIS   A 91  ? 0.2289 0.2589 0.2434 0.0154  -0.0702 0.0169  91  HIS   A CG  
1983 N  ND1 . HIS   A 91  ? 0.2391 0.2865 0.2841 0.0202  -0.0825 -0.0027 91  HIS   A ND1 
1984 C  CD2 . HIS   A 91  ? 0.2554 0.2784 0.2611 0.0239  -0.0819 0.0274  91  HIS   A CD2 
1985 C  CE1 . HIS   A 91  ? 0.2525 0.2949 0.2943 0.0252  -0.0817 0.0124  91  HIS   A CE1 
1986 N  NE2 . HIS   A 91  ? 0.2660 0.2941 0.2850 0.0288  -0.0862 0.0206  91  HIS   A NE2 
1994 N  N   . CYS   A 92  ? 0.1426 0.1603 0.1303 -0.0225 -0.0161 0.0257  92  CYS   A N   
1995 C  CA  . CYS   A 92  ? 0.1383 0.1556 0.1315 -0.0149 -0.0042 0.0225  92  CYS   A CA  
1996 C  C   . CYS   A 92  ? 0.1345 0.1486 0.1267 -0.0173 0.0031  0.0215  92  CYS   A C   
1997 O  O   . CYS   A 92  ? 0.1346 0.1546 0.1477 -0.0182 -0.0062 0.0133  92  CYS   A O   
1998 C  CB  . CYS   A 92  ? 0.1411 0.1554 0.1427 -0.0114 -0.0100 0.0125  92  CYS   A CB  
1999 S  SG  . CYS   A 92  ? 0.1381 0.1391 0.1393 -0.0150 -0.0055 0.0148  92  CYS   A SG  
2005 N  N   . LEU   A 93  ? 0.1319 0.1334 0.1370 -0.0149 0.0027  0.0191  93  LEU   A N   
2006 C  CA  . LEU   A 93  ? 0.1197 0.1297 0.1393 -0.0089 -0.0027 0.0180  93  LEU   A CA  
2007 C  C   . LEU   A 93  ? 0.1193 0.1219 0.1337 -0.0044 0.0017  0.0145  93  LEU   A C   
2008 O  O   . LEU   A 93  ? 0.1184 0.1307 0.1319 -0.0035 -0.0005 0.0178  93  LEU   A O   
2009 C  CB  . LEU   A 93  ? 0.1280 0.1333 0.1550 -0.0070 -0.0072 0.0248  93  LEU   A CB  
2010 C  CG  . LEU   A 93  ? 0.1346 0.1315 0.1540 -0.0059 -0.0014 0.0218  93  LEU   A CG  
2011 C  CD1 . LEU   A 93  ? 0.1408 0.1362 0.1804 -0.0039 0.0073  0.0182  93  LEU   A CD1 
2012 C  CD2 . LEU   A 93  ? 0.1500 0.1281 0.1664 -0.0092 -0.0048 0.0171  93  LEU   A CD2 
2024 N  N   . HIS   A 94  ? 0.1184 0.1178 0.1319 -0.0066 0.0012  0.0201  94  HIS   A N   
2025 C  CA  . HIS   A 94  ? 0.1173 0.1215 0.1321 -0.0067 0.0040  0.0194  94  HIS   A CA  
2026 C  C   . HIS   A 94  ? 0.1142 0.1185 0.1400 -0.0083 0.0006  0.0086  94  HIS   A C   
2027 O  O   . HIS   A 94  ? 0.1172 0.1407 0.1684 -0.0029 0.0034  -0.0045 94  HIS   A O   
2028 C  CB  . HIS   A 94  ? 0.1161 0.1169 0.1400 -0.0045 0.0018  0.0142  94  HIS   A CB  
2029 C  CG  . HIS   A 94  ? 0.1216 0.1183 0.1304 -0.0079 -0.0095 0.0170  94  HIS   A CG  
2030 N  ND1 . HIS   A 94  ? 0.1216 0.1202 0.1390 -0.0050 -0.0004 0.0182  94  HIS   A ND1 
2031 C  CD2 . HIS   A 94  ? 0.1283 0.1303 0.1381 -0.0096 -0.0052 0.0146  94  HIS   A CD2 
2032 C  CE1 . HIS   A 94  ? 0.1269 0.1273 0.1309 -0.0106 -0.0073 0.0096  94  HIS   A CE1 
2033 N  NE2 . HIS   A 94  ? 0.1294 0.1288 0.1406 -0.0105 -0.0074 0.0056  94  HIS   A NE2 
2041 N  N   . VAL   A 95  ? 0.1120 0.1145 0.1236 -0.0033 0.0081  0.0087  95  VAL   A N   
2042 C  CA  . VAL   A 95  ? 0.1226 0.1183 0.1228 -0.0059 0.0144  0.0116  95  VAL   A CA  
2043 C  C   . VAL   A 95  ? 0.1229 0.1192 0.1144 -0.0121 0.0046  0.0135  95  VAL   A C   
2044 O  O   . VAL   A 95  ? 0.1246 0.1290 0.1254 0.0046  0.0044  0.0055  95  VAL   A O   
2045 C  CB  . VAL   A 95  ? 0.1255 0.1189 0.1432 -0.0104 0.0042  0.0089  95  VAL   A CB  
2046 C  CG1 . VAL   A 95  ? 0.1382 0.1245 0.1597 -0.0168 0.0053  0.0060  95  VAL   A CG1 
2047 C  CG2 . VAL   A 95  ? 0.1273 0.1215 0.1405 -0.0137 0.0004  0.0210  95  VAL   A CG2 
2057 N  N   . VAL   A 96  ? 0.1240 0.1197 0.1150 -0.0054 0.0070  0.0114  96  VAL   A N   
2058 C  CA  . VAL   A 96  ? 0.1328 0.1186 0.1292 -0.0035 0.0099  0.0210  96  VAL   A CA  
2059 C  C   . VAL   A 96  ? 0.1342 0.1280 0.1317 -0.0015 0.0121  0.0169  96  VAL   A C   
2060 O  O   . VAL   A 96  ? 0.1395 0.1356 0.1534 -0.0051 0.0175  0.0016  96  VAL   A O   
2061 C  CB  . VAL   A 96  ? 0.1318 0.1278 0.1328 -0.0019 0.0213  0.0141  96  VAL   A CB  
2062 C  CG1 . VAL   A 96  ? 0.1437 0.1364 0.1192 -0.0030 0.0169  0.0139  96  VAL   A CG1 
2063 C  CG2 . VAL   A 96  ? 0.1367 0.1321 0.1505 -0.0117 0.0192  0.0132  96  VAL   A CG2 
2073 N  N   A GLY   A 97  ? 0.1342 0.1309 0.1312 -0.0071 0.0050  0.0091  97  GLY   A N   
2074 N  N   B GLY   A 97  ? 0.1360 0.1299 0.1293 -0.0014 0.0057  0.0166  97  GLY   A N   
2075 C  CA  A GLY   A 97  ? 0.1451 0.1431 0.1301 -0.0071 0.0020  0.0086  97  GLY   A CA  
2076 C  CA  B GLY   A 97  ? 0.1422 0.1342 0.1292 0.0001  0.0026  0.0189  97  GLY   A CA  
2077 C  C   A GLY   A 97  ? 0.1430 0.1546 0.1189 -0.0114 0.0019  0.0043  97  GLY   A C   
2078 C  C   B GLY   A 97  ? 0.1425 0.1384 0.1295 -0.0009 0.0022  0.0200  97  GLY   A C   
2079 O  O   A GLY   A 97  ? 0.1522 0.1538 0.1400 -0.0159 0.0003  0.0105  97  GLY   A O   
2080 O  O   B GLY   A 97  ? 0.1448 0.1387 0.1302 -0.0027 -0.0060 0.0268  97  GLY   A O   
2087 N  N   A PRO   A 98  ? 0.1467 0.1599 0.1087 -0.0039 -0.0007 0.0118  98  PRO   A N   
2088 N  N   B PRO   A 98  ? 0.1463 0.1403 0.1374 0.0022  0.0050  0.0221  98  PRO   A N   
2089 C  CA  A PRO   A 98  ? 0.1561 0.1754 0.1146 -0.0036 0.0020  0.0065  98  PRO   A CA  
2090 C  CA  B PRO   A 98  ? 0.1535 0.1449 0.1445 -0.0008 0.0095  0.0101  98  PRO   A CA  
2091 C  C   A PRO   A 98  ? 0.1568 0.1803 0.1013 -0.0079 0.0010  0.0132  98  PRO   A C   
2092 C  C   B PRO   A 98  ? 0.1704 0.1421 0.1373 -0.0086 0.0098  0.0128  98  PRO   A C   
2093 O  O   A PRO   A 98  ? 0.1498 0.1663 0.1221 -0.0032 0.0002  0.0133  98  PRO   A O   
2094 O  O   B PRO   A 98  ? 0.1699 0.1400 0.1589 -0.0063 0.0168  0.0030  98  PRO   A O   
2095 C  CB  A PRO   A 98  ? 0.1644 0.1818 0.1043 0.0092  -0.0043 -0.0063 98  PRO   A CB  
2096 C  CB  B PRO   A 98  ? 0.1539 0.1445 0.1479 0.0079  0.0046  0.0162  98  PRO   A CB  
2097 C  CG  A PRO   A 98  ? 0.1605 0.1768 0.1137 0.0099  -0.0000 -0.0113 98  PRO   A CG  
2098 C  CG  B PRO   A 98  ? 0.1575 0.1452 0.1525 0.0067  0.0043  0.0203  98  PRO   A CG  
2099 C  CD  A PRO   A 98  ? 0.1534 0.1629 0.1154 0.0045  0.0023  -0.0066 98  PRO   A CD  
2100 C  CD  B PRO   A 98  ? 0.1502 0.1383 0.1396 0.0074  0.0028  0.0246  98  PRO   A CD  
2115 N  N   A ASN   A 99  ? 0.1613 0.2027 0.1078 -0.0074 0.0050  0.0296  99  ASN   A N   
2116 N  N   B ASN   A 99  ? 0.1926 0.1420 0.1172 -0.0099 0.0071  0.0215  99  ASN   A N   
2117 C  CA  A ASN   A 99  ? 0.1805 0.2180 0.1088 -0.0108 0.0035  0.0376  99  ASN   A CA  
2118 C  CA  B ASN   A 99  ? 0.2176 0.1425 0.1042 -0.0046 -0.0010 0.0302  99  ASN   A CA  
2119 C  C   A ASN   A 99  ? 0.1990 0.2483 0.1117 -0.0296 0.0069  0.0428  99  ASN   A C   
2120 C  C   B ASN   A 99  ? 0.2312 0.1477 0.1126 -0.0035 -0.0152 0.0343  99  ASN   A C   
2121 O  O   A ASN   A 99  ? 0.2092 0.2609 0.1234 -0.0276 -0.0027 0.0354  99  ASN   A O   
2122 O  O   B ASN   A 99  ? 0.2365 0.1351 0.1105 0.0056  -0.0231 0.0168  99  ASN   A O   
2123 C  CB  A ASN   A 99  ? 0.1810 0.2119 0.1209 -0.0088 -0.0025 0.0360  99  ASN   A CB  
2124 C  CB  B ASN   A 99  ? 0.2288 0.1419 0.1220 0.0012  -0.0019 0.0276  99  ASN   A CB  
2125 C  CG  A ASN   A 99  ? 0.1843 0.2041 0.1338 -0.0094 -0.0084 0.0224  99  ASN   A CG  
2126 C  CG  B ASN   A 99  ? 0.2394 0.1503 0.1325 0.0040  -0.0010 0.0318  99  ASN   A CG  
2127 O  OD1 A ASN   A 99  ? 0.1944 0.2164 0.1353 0.0034  -0.0105 0.0141  99  ASN   A OD1 
2128 O  OD1 B ASN   A 99  ? 0.2424 0.1567 0.1259 0.0080  -0.0019 0.0366  99  ASN   A OD1 
2129 N  ND2 A ASN   A 99  ? 0.1867 0.2058 0.1448 -0.0056 -0.0105 0.0282  99  ASN   A ND2 
2130 N  ND2 B ASN   A 99  ? 0.2451 0.1580 0.1531 0.0113  -0.0081 0.0173  99  ASN   A ND2 
2143 N  N   A VAL   A 100 ? 0.2150 0.2683 0.1351 -0.0431 -0.0201 0.0371  100 VAL   A N   
2144 N  N   B VAL   A 100 ? 0.2403 0.1758 0.1377 -0.0061 -0.0291 0.0413  100 VAL   A N   
2145 C  CA  A VAL   A 100 ? 0.2393 0.2876 0.1515 -0.0498 -0.0326 0.0377  100 VAL   A CA  
2146 C  CA  B VAL   A 100 ? 0.2501 0.1982 0.1744 -0.0060 -0.0310 0.0380  100 VAL   A CA  
2147 C  C   A VAL   A 100 ? 0.2473 0.2952 0.1457 -0.0555 -0.0304 0.0655  100 VAL   A C   
2148 C  C   B VAL   A 100 ? 0.2512 0.2039 0.1781 0.0013  -0.0370 0.0326  100 VAL   A C   
2149 O  O   A VAL   A 100 ? 0.2547 0.2991 0.1540 -0.0469 -0.0082 0.0689  100 VAL   A O   
2150 O  O   B VAL   A 100 ? 0.2511 0.1969 0.1841 0.0016  -0.0351 0.0263  100 VAL   A O   
2151 C  CB  A VAL   A 100 ? 0.2583 0.2955 0.1924 -0.0538 -0.0367 0.0237  100 VAL   A CB  
2152 C  CB  B VAL   A 100 ? 0.2596 0.2133 0.2138 -0.0059 -0.0271 0.0274  100 VAL   A CB  
2153 C  CG1 A VAL   A 100 ? 0.2570 0.2944 0.2029 -0.0581 -0.0335 0.0252  100 VAL   A CG1 
2154 C  CG1 B VAL   A 100 ? 0.2603 0.2142 0.2238 -0.0067 -0.0277 0.0307  100 VAL   A CG1 
2155 C  CG2 A VAL   A 100 ? 0.2682 0.2990 0.1934 -0.0538 -0.0359 0.0070  100 VAL   A CG2 
2156 C  CG2 B VAL   A 100 ? 0.2639 0.2179 0.2313 -0.0064 -0.0225 0.0181  100 VAL   A CG2 
2175 N  N   A ASN   A 101 ? 0.2538 0.3087 0.1651 -0.0619 -0.0274 0.0850  101 ASN   A N   
2176 N  N   B ASN   A 101 ? 0.2560 0.2125 0.1842 0.0066  -0.0417 0.0307  101 ASN   A N   
2177 C  CA  A ASN   A 101 ? 0.2732 0.3167 0.1782 -0.0663 -0.0269 0.1069  101 ASN   A CA  
2178 C  CA  B ASN   A 101 ? 0.2646 0.2194 0.1944 0.0107  -0.0346 0.0319  101 ASN   A CA  
2179 C  C   A ASN   A 101 ? 0.2991 0.3454 0.2093 -0.0696 0.0004  0.1281  101 ASN   A C   
2180 C  C   B ASN   A 101 ? 0.2756 0.2312 0.2048 0.0125  -0.0244 0.0466  101 ASN   A C   
2181 O  O   A ASN   A 101 ? 0.3118 0.3517 0.2502 -0.0669 -0.0016 0.1204  101 ASN   A O   
2182 O  O   B ASN   A 101 ? 0.2822 0.2350 0.1997 0.0089  -0.0263 0.0548  101 ASN   A O   
2183 C  CB  A ASN   A 101 ? 0.2709 0.2990 0.1672 -0.0638 -0.0489 0.0985  101 ASN   A CB  
2184 C  CB  B ASN   A 101 ? 0.2625 0.2160 0.1989 0.0075  -0.0301 0.0239  101 ASN   A CB  
2185 C  CG  A ASN   A 101 ? 0.2700 0.2828 0.1584 -0.0588 -0.0596 0.0720  101 ASN   A CG  
2186 C  CG  B ASN   A 101 ? 0.2631 0.2189 0.2119 0.0044  -0.0282 0.0235  101 ASN   A CG  
2187 O  OD1 A ASN   A 101 ? 0.2645 0.2810 0.1651 -0.0447 -0.0521 0.0345  101 ASN   A OD1 
2188 O  OD1 B ASN   A 101 ? 0.2708 0.2256 0.2284 -0.0016 -0.0244 0.0256  101 ASN   A OD1 
2189 N  ND2 A ASN   A 101 ? 0.2768 0.2736 0.1627 -0.0647 -0.0573 0.0771  101 ASN   A ND2 
2190 N  ND2 B ASN   A 101 ? 0.2603 0.2175 0.2201 0.0067  -0.0242 0.0125  101 ASN   A ND2 
2203 N  N   A LYS   A 102 ? 0.3081 0.3693 0.2392 -0.0757 0.0155  0.1284  102 LYS   A N   
2204 N  N   B LYS   A 102 ? 0.2799 0.2421 0.2353 0.0167  -0.0077 0.0495  102 LYS   A N   
2205 C  CA  A LYS   A 102 ? 0.3232 0.3896 0.2551 -0.0755 0.0121  0.1171  102 LYS   A CA  
2206 C  CA  B LYS   A 102 ? 0.2851 0.2521 0.2456 0.0147  0.0049  0.0511  102 LYS   A CA  
2207 C  C   A LYS   A 102 ? 0.3317 0.4084 0.2441 -0.0632 0.0092  0.1023  102 LYS   A C   
2208 C  C   B LYS   A 102 ? 0.2880 0.2537 0.2325 0.0191  0.0023  0.0647  102 LYS   A C   
2209 O  O   A LYS   A 102 ? 0.3342 0.4179 0.2475 -0.0578 0.0139  0.0938  102 LYS   A O   
2210 O  O   B LYS   A 102 ? 0.2905 0.2512 0.2278 0.0211  0.0061  0.0785  102 LYS   A O   
2211 C  CB  A LYS   A 102 ? 0.3344 0.3928 0.2966 -0.0815 0.0022  0.1011  102 LYS   A CB  
2212 C  CB  B LYS   A 102 ? 0.2877 0.2595 0.2682 0.0130  0.0086  0.0408  102 LYS   A CB  
2213 C  CG  A LYS   A 102 ? 0.3452 0.3937 0.3294 -0.0857 -0.0074 0.0847  102 LYS   A CG  
2214 C  CG  B LYS   A 102 ? 0.2902 0.2679 0.2839 0.0109  0.0131  0.0320  102 LYS   A CG  
2215 C  CD  A LYS   A 102 ? 0.3587 0.3967 0.3632 -0.0864 -0.0177 0.0649  102 LYS   A CD  
2216 C  CD  B LYS   A 102 ? 0.2950 0.2777 0.3015 0.0101  0.0144  0.0245  102 LYS   A CD  
2217 C  CE  A LYS   A 102 ? 0.3688 0.3983 0.3909 -0.0878 -0.0244 0.0533  102 LYS   A CE  
2218 C  CE  B LYS   A 102 ? 0.2990 0.2837 0.3141 0.0106  0.0141  0.0227  102 LYS   A CE  
2219 N  NZ  A LYS   A 102 ? 0.3745 0.3994 0.4064 -0.0898 -0.0243 0.0463  102 LYS   A NZ  
2220 N  NZ  B LYS   A 102 ? 0.3015 0.2867 0.3222 0.0123  0.0153  0.0213  102 LYS   A NZ  
2247 N  N   A GLY   A 103 ? 0.3355 0.4188 0.2562 -0.0528 0.0015  0.0789  103 GLY   A N   
2248 N  N   B GLY   A 103 ? 0.2879 0.2620 0.2259 0.0220  -0.0080 0.0577  103 GLY   A N   
2249 C  CA  A GLY   A 103 ? 0.3397 0.4245 0.2503 -0.0424 0.0005  0.0610  103 GLY   A CA  
2250 C  CA  B GLY   A 103 ? 0.2879 0.2640 0.2207 0.0221  -0.0138 0.0604  103 GLY   A CA  
2251 C  C   A GLY   A 103 ? 0.3382 0.4297 0.2442 -0.0358 0.0080  0.0485  103 GLY   A C   
2252 C  C   B GLY   A 103 ? 0.2837 0.2619 0.2043 0.0191  -0.0135 0.0574  103 GLY   A C   
2253 O  O   A GLY   A 103 ? 0.3481 0.4355 0.2614 -0.0316 0.0110  0.0408  103 GLY   A O   
2254 O  O   B GLY   A 103 ? 0.2907 0.2631 0.1973 0.0197  -0.0171 0.0629  103 GLY   A O   
2261 N  N   A GLU   A 104 ? 0.3213 0.4243 0.2080 -0.0390 0.0185  0.0416  104 GLU   A N   
2262 N  N   B GLU   A 104 ? 0.2709 0.2561 0.1924 0.0149  -0.0183 0.0550  104 GLU   A N   
2263 C  CA  A GLU   A 104 ? 0.3017 0.4146 0.1787 -0.0469 0.0248  0.0322  104 GLU   A CA  
2264 C  CA  B GLU   A 104 ? 0.2601 0.2493 0.1771 0.0079  -0.0208 0.0442  104 GLU   A CA  
2265 C  C   A GLU   A 104 ? 0.3043 0.4199 0.1827 -0.0480 0.0242  0.0100  104 GLU   A C   
2266 C  C   B GLU   A 104 ? 0.2618 0.2490 0.1879 0.0104  -0.0132 0.0288  104 GLU   A C   
2267 O  O   A GLU   A 104 ? 0.2986 0.4217 0.1955 -0.0486 0.0088  0.0102  104 GLU   A O   
2268 O  O   B GLU   A 104 ? 0.2582 0.2400 0.1965 0.0108  -0.0102 0.0344  104 GLU   A O   
2269 C  CB  A GLU   A 104 ? 0.2750 0.3983 0.1524 -0.0537 0.0317  0.0512  104 GLU   A CB  
2270 C  CB  B GLU   A 104 ? 0.2504 0.2446 0.1678 -0.0001 -0.0252 0.0468  104 GLU   A CB  
2271 C  CG  A GLU   A 104 ? 0.2537 0.3833 0.1649 -0.0575 0.0284  0.0646  104 GLU   A CG  
2272 C  CG  B GLU   A 104 ? 0.2466 0.2468 0.1813 -0.0070 -0.0340 0.0447  104 GLU   A CG  
2273 C  CD  A GLU   A 104 ? 0.2308 0.3682 0.1585 -0.0613 0.0312  0.0787  104 GLU   A CD  
2274 C  CD  B GLU   A 104 ? 0.2417 0.2465 0.1867 -0.0106 -0.0420 0.0447  104 GLU   A CD  
2275 O  OE1 A GLU   A 104 ? 0.2099 0.3529 0.1360 -0.0607 0.0204  0.0761  104 GLU   A OE1 
2276 O  OE1 B GLU   A 104 ? 0.2383 0.2447 0.1846 -0.0083 -0.0481 0.0459  104 GLU   A OE1 
2277 O  OE2 A GLU   A 104 ? 0.2444 0.3645 0.1785 -0.0620 0.0322  0.0947  104 GLU   A OE2 
2278 O  OE2 B GLU   A 104 ? 0.2470 0.2478 0.2060 -0.0159 -0.0376 0.0391  104 GLU   A OE2 
2291 N  N   A ASP   A 105 ? 0.3120 0.4226 0.1918 -0.0473 0.0365  -0.0159 105 ASP   A N   
2292 N  N   B ASP   A 105 ? 0.2746 0.2609 0.2076 0.0064  -0.0062 0.0103  105 ASP   A N   
2293 C  CA  A ASP   A 105 ? 0.3138 0.4235 0.2256 -0.0447 0.0403  -0.0409 105 ASP   A CA  
2294 C  CA  B ASP   A 105 ? 0.2844 0.2743 0.2359 0.0054  0.0022  -0.0145 105 ASP   A CA  
2295 C  C   A ASP   A 105 ? 0.2852 0.4062 0.1896 -0.0552 0.0275  -0.0581 105 ASP   A C   
2296 C  C   B ASP   A 105 ? 0.2841 0.2784 0.2280 -0.0035 0.0039  -0.0213 105 ASP   A C   
2297 O  O   A ASP   A 105 ? 0.2705 0.4018 0.1395 -0.0613 0.0220  -0.0808 105 ASP   A O   
2298 O  O   B ASP   A 105 ? 0.2787 0.2741 0.2054 -0.0042 0.0031  -0.0256 105 ASP   A O   
2299 C  CB  A ASP   A 105 ? 0.3395 0.4396 0.3018 -0.0340 0.0483  -0.0456 105 ASP   A CB  
2300 C  CB  B ASP   A 105 ? 0.2935 0.2845 0.2768 0.0123  0.0087  -0.0301 105 ASP   A CB  
2301 C  CG  A ASP   A 105 ? 0.3613 0.4524 0.3689 -0.0246 0.0489  -0.0510 105 ASP   A CG  
2302 C  CG  B ASP   A 105 ? 0.3016 0.2912 0.3110 0.0208  0.0118  -0.0440 105 ASP   A CG  
2303 O  OD1 A ASP   A 105 ? 0.3679 0.4583 0.3851 -0.0236 0.0481  -0.0595 105 ASP   A OD1 
2304 O  OD1 B ASP   A 105 ? 0.3056 0.2906 0.3124 0.0206  0.0088  -0.0530 105 ASP   A OD1 
2305 O  OD2 A ASP   A 105 ? 0.3727 0.4571 0.4053 -0.0216 0.0512  -0.0441 105 ASP   A OD2 
2306 O  OD2 B ASP   A 105 ? 0.3057 0.2965 0.3371 0.0236  0.0124  -0.0431 105 ASP   A OD2 
2315 N  N   A ILE   A 106 ? 0.2676 0.3913 0.2088 -0.0617 0.0079  -0.0562 106 ILE   A N   
2316 N  N   B ILE   A 106 ? 0.2869 0.2864 0.2433 -0.0105 0.0015  -0.0214 106 ILE   A N   
2317 C  CA  A ILE   A 106 ? 0.2422 0.3741 0.2256 -0.0740 -0.0138 -0.0652 106 ILE   A CA  
2318 C  CA  B ILE   A 106 ? 0.2873 0.2962 0.2608 -0.0219 -0.0009 -0.0244 106 ILE   A CA  
2319 C  C   A ILE   A 106 ? 0.2270 0.3490 0.2305 -0.0923 -0.0134 -0.0864 106 ILE   A C   
2320 C  C   B ILE   A 106 ? 0.2855 0.2948 0.2663 -0.0308 0.0064  -0.0281 106 ILE   A C   
2321 O  O   A ILE   A 106 ? 0.2101 0.3399 0.2299 -0.0987 0.0035  -0.0894 106 ILE   A O   
2322 O  O   B ILE   A 106 ? 0.2830 0.2945 0.2647 -0.0306 0.0101  -0.0302 106 ILE   A O   
2323 C  CB  A ILE   A 106 ? 0.2431 0.3838 0.2659 -0.0598 -0.0290 -0.0382 106 ILE   A CB  
2324 C  CB  B ILE   A 106 ? 0.2917 0.3080 0.2823 -0.0226 -0.0100 -0.0167 106 ILE   A CB  
2325 C  CG1 A ILE   A 106 ? 0.2331 0.3859 0.2899 -0.0453 -0.0341 -0.0139 106 ILE   A CG1 
2326 C  CG1 B ILE   A 106 ? 0.2914 0.3135 0.2960 -0.0199 -0.0134 -0.0072 106 ILE   A CG1 
2327 C  CG2 A ILE   A 106 ? 0.2518 0.3873 0.2769 -0.0582 -0.0316 -0.0399 106 ILE   A CG2 
2328 C  CG2 B ILE   A 106 ? 0.2950 0.3110 0.2867 -0.0238 -0.0120 -0.0191 106 ILE   A CG2 
2329 C  CD1 A ILE   A 106 ? 0.2308 0.3848 0.3039 -0.0314 -0.0261 -0.0009 106 ILE   A CD1 
2330 C  CD1 B ILE   A 106 ? 0.2923 0.3151 0.3029 -0.0162 -0.0118 -0.0023 106 ILE   A CD1 
2353 N  N   A GLN   A 107 ? 0.2419 0.3333 0.2522 -0.0906 -0.0044 -0.0974 107 GLN   A N   
2354 N  N   B GLN   A 107 ? 0.2866 0.2909 0.2802 -0.0376 0.0145  -0.0282 107 GLN   A N   
2355 C  CA  A GLN   A 107 ? 0.2681 0.3179 0.3223 -0.0720 0.0225  -0.0866 107 GLN   A CA  
2356 C  CA  B GLN   A 107 ? 0.2879 0.2872 0.3112 -0.0427 0.0229  -0.0296 107 GLN   A CA  
2357 C  C   A GLN   A 107 ? 0.2444 0.2723 0.3041 -0.0608 0.0475  -0.0623 107 GLN   A C   
2358 C  C   B GLN   A 107 ? 0.2558 0.2590 0.2854 -0.0480 0.0389  -0.0372 107 GLN   A C   
2359 O  O   A GLN   A 107 ? 0.2513 0.2688 0.3538 -0.0552 0.0575  -0.0612 107 GLN   A O   
2360 O  O   B GLN   A 107 ? 0.2618 0.2588 0.3064 -0.0477 0.0392  -0.0377 107 GLN   A O   
2361 C  CB  A GLN   A 107 ? 0.3099 0.3452 0.4109 -0.0723 0.0144  -0.0875 107 GLN   A CB  
2362 C  CB  B GLN   A 107 ? 0.3167 0.3102 0.3670 -0.0447 0.0123  -0.0201 107 GLN   A CB  
2363 C  CG  A GLN   A 107 ? 0.3502 0.3746 0.5062 -0.0682 0.0063  -0.0775 107 GLN   A CG  
2364 C  CG  B GLN   A 107 ? 0.3420 0.3316 0.4251 -0.0453 0.0012  -0.0081 107 GLN   A CG  
2365 C  CD  A GLN   A 107 ? 0.3822 0.3955 0.5858 -0.0652 0.0008  -0.0655 107 GLN   A CD  
2366 C  CD  B GLN   A 107 ? 0.3634 0.3495 0.4754 -0.0437 -0.0078 0.0038  107 GLN   A CD  
2367 O  OE1 A GLN   A 107 ? 0.3950 0.4039 0.6179 -0.0629 -0.0019 -0.0617 107 GLN   A OE1 
2368 O  OE1 B GLN   A 107 ? 0.3718 0.3570 0.4917 -0.0421 -0.0111 0.0089  107 GLN   A OE1 
2369 N  NE2 A GLN   A 107 ? 0.3922 0.4016 0.6119 -0.0659 -0.0017 -0.0639 107 GLN   A NE2 
2370 N  NE2 B GLN   A 107 ? 0.3693 0.3546 0.4909 -0.0432 -0.0129 0.0085  107 GLN   A NE2 
2387 N  N   . LEU   A 108 ? 0.2182 0.2309 0.2475 -0.0547 0.0470  -0.0509 108 LEU   A N   
2388 C  CA  . LEU   A 108 ? 0.1903 0.1867 0.2145 -0.0226 0.0420  -0.0204 108 LEU   A CA  
2389 C  C   . LEU   A 108 ? 0.1670 0.1463 0.2084 -0.0098 0.0376  0.0061  108 LEU   A C   
2390 O  O   . LEU   A 108 ? 0.1633 0.1492 0.2244 -0.0023 0.0394  0.0090  108 LEU   A O   
2391 C  CB  . LEU   A 108 ? 0.1938 0.1984 0.1994 -0.0268 0.0440  -0.0200 108 LEU   A CB  
2392 C  CG  . LEU   A 108 ? 0.2086 0.2246 0.2232 -0.0211 0.0614  -0.0244 108 LEU   A CG  
2393 C  CD1 . LEU   A 108 ? 0.2243 0.2288 0.2254 -0.0309 0.0626  -0.0197 108 LEU   A CD1 
2394 C  CD2 . LEU   A 108 ? 0.2087 0.2469 0.2686 -0.0104 0.0608  -0.0171 108 LEU   A CD2 
2407 N  N   . LEU   A 109 ? 0.1523 0.1485 0.1995 0.0043  0.0265  0.0133  109 LEU   A N   
2408 C  CA  . LEU   A 109 ? 0.1458 0.1408 0.1856 0.0043  0.0194  0.0138  109 LEU   A CA  
2409 C  C   . LEU   A 109 ? 0.1366 0.1323 0.1781 -0.0090 0.0151  0.0085  109 LEU   A C   
2410 O  O   . LEU   A 109 ? 0.1424 0.1240 0.1942 -0.0035 0.0026  0.0035  109 LEU   A O   
2411 C  CB  . LEU   A 109 ? 0.1546 0.1484 0.2008 0.0112  0.0094  0.0318  109 LEU   A CB  
2412 C  CG  . LEU   A 109 ? 0.1447 0.1533 0.1979 0.0066  0.0128  0.0402  109 LEU   A CG  
2413 C  CD1 . LEU   A 109 ? 0.1536 0.1433 0.2224 -0.0032 0.0195  0.0204  109 LEU   A CD1 
2414 C  CD2 . LEU   A 109 ? 0.1461 0.1762 0.2181 0.0063  0.0127  0.0421  109 LEU   A CD2 
2426 N  N   . LYS   A 110 ? 0.1401 0.1305 0.1751 -0.0060 0.0035  0.0045  110 LYS   A N   
2427 C  CA  . LYS   A 110 ? 0.1357 0.1272 0.1868 -0.0069 0.0027  0.0122  110 LYS   A CA  
2428 C  C   . LYS   A 110 ? 0.1370 0.1188 0.1684 -0.0084 0.0031  -0.0001 110 LYS   A C   
2429 O  O   . LYS   A 110 ? 0.1333 0.1232 0.1809 -0.0065 0.0053  -0.0005 110 LYS   A O   
2430 C  CB  . LYS   A 110 ? 0.1381 0.1332 0.2026 -0.0053 0.0003  0.0021  110 LYS   A CB  
2431 C  CG  . LYS   A 110 ? 0.1440 0.1308 0.2100 -0.0002 -0.0041 -0.0047 110 LYS   A CG  
2432 C  CD  . LYS   A 110 ? 0.1464 0.1358 0.2241 -0.0077 -0.0061 -0.0090 110 LYS   A CD  
2433 C  CE  . LYS   A 110 ? 0.1526 0.1407 0.2408 -0.0034 0.0099  -0.0136 110 LYS   A CE  
2434 N  NZ  . LYS   A 110 ? 0.1565 0.1450 0.2523 -0.0183 0.0132  -0.0089 110 LYS   A NZ  
2448 N  N   . SER   A 111 ? 0.1356 0.1238 0.1757 -0.0019 0.0061  0.0020  111 SER   A N   
2449 C  CA  . SER   A 111 ? 0.1290 0.1320 0.1782 -0.0016 0.0124  0.0021  111 SER   A CA  
2450 C  C   . SER   A 111 ? 0.1273 0.1256 0.1783 -0.0098 0.0116  0.0050  111 SER   A C   
2451 O  O   . SER   A 111 ? 0.1417 0.1181 0.1934 -0.0063 0.0124  0.0077  111 SER   A O   
2452 C  CB  . SER   A 111 ? 0.1493 0.1496 0.1895 -0.0046 0.0188  -0.0091 111 SER   A CB  
2453 O  OG  . SER   A 111 ? 0.1929 0.1730 0.1970 0.0011  0.0238  -0.0136 111 SER   A OG  
2459 N  N   . ALA   A 112 ? 0.1298 0.1207 0.1746 -0.0038 0.0156  0.0071  112 ALA   A N   
2460 C  CA  . ALA   A 112 ? 0.1346 0.1194 0.1790 -0.0038 0.0207  0.0054  112 ALA   A CA  
2461 C  C   . ALA   A 112 ? 0.1287 0.1134 0.1797 -0.0030 0.0110  0.0053  112 ALA   A C   
2462 O  O   . ALA   A 112 ? 0.1326 0.1159 0.1809 -0.0127 0.0175  0.0050  112 ALA   A O   
2463 C  CB  . ALA   A 112 ? 0.1461 0.1232 0.1890 -0.0064 0.0199  0.0044  112 ALA   A CB  
2469 N  N   . TYR   A 113 ? 0.1195 0.1234 0.1803 -0.0042 0.0131  0.0112  113 TYR   A N   
2470 C  CA  . TYR   A 113 ? 0.1210 0.1202 0.1733 -0.0022 0.0164  0.0124  113 TYR   A CA  
2471 C  C   . TYR   A 113 ? 0.1176 0.1178 0.1690 -0.0084 0.0103  0.0075  113 TYR   A C   
2472 O  O   . TYR   A 113 ? 0.1240 0.1229 0.1826 -0.0067 0.0109  0.0078  113 TYR   A O   
2473 C  CB  . TYR   A 113 ? 0.1212 0.1230 0.1787 -0.0071 0.0055  0.0197  113 TYR   A CB  
2474 C  CG  . TYR   A 113 ? 0.1231 0.1268 0.1741 -0.0127 0.0167  0.0202  113 TYR   A CG  
2475 C  CD1 . TYR   A 113 ? 0.1272 0.1305 0.1750 -0.0036 0.0122  0.0270  113 TYR   A CD1 
2476 C  CD2 . TYR   A 113 ? 0.1273 0.1333 0.1646 -0.0107 0.0049  0.0207  113 TYR   A CD2 
2477 C  CE1 . TYR   A 113 ? 0.1303 0.1356 0.1735 -0.0090 0.0093  0.0274  113 TYR   A CE1 
2478 C  CE2 . TYR   A 113 ? 0.1271 0.1408 0.1688 -0.0110 0.0050  0.0236  113 TYR   A CE2 
2479 C  CZ  . TYR   A 113 ? 0.1275 0.1397 0.1698 -0.0029 0.0124  0.0279  113 TYR   A CZ  
2480 O  OH  . TYR   A 113 ? 0.1248 0.1460 0.1787 0.0078  0.0107  0.0277  113 TYR   A OH  
2490 N  N   . GLU   A 114 ? 0.1217 0.1180 0.1801 -0.0057 0.0155  0.0136  114 GLU   A N   
2491 C  CA  . GLU   A 114 ? 0.1271 0.1122 0.1849 0.0004  0.0116  0.0180  114 GLU   A CA  
2492 C  C   . GLU   A 114 ? 0.1207 0.1203 0.1843 -0.0030 0.0127  0.0109  114 GLU   A C   
2493 O  O   . GLU   A 114 ? 0.1330 0.1239 0.1815 -0.0028 0.0028  0.0114  114 GLU   A O   
2494 C  CB  . GLU   A 114 ? 0.1304 0.1161 0.1836 -0.0085 0.0081  0.0183  114 GLU   A CB  
2495 C  CG  . GLU   A 114 ? 0.1336 0.1207 0.1956 -0.0010 0.0114  0.0072  114 GLU   A CG  
2496 C  CD  . GLU   A 114 ? 0.1407 0.1220 0.1982 -0.0064 0.0065  0.0033  114 GLU   A CD  
2497 O  OE1 . GLU   A 114 ? 0.1412 0.1218 0.2042 -0.0084 0.0137  -0.0067 114 GLU   A OE1 
2498 O  OE2 . GLU   A 114 ? 0.1584 0.1291 0.2190 -0.0122 0.0078  -0.0102 114 GLU   A OE2 
2505 N  N   . ASN   A 115 ? 0.1260 0.1211 0.1689 -0.0074 0.0083  0.0074  115 ASN   A N   
2506 C  CA  . ASN   A 115 ? 0.1267 0.1233 0.1774 -0.0117 0.0093  0.0144  115 ASN   A CA  
2507 C  C   . ASN   A 115 ? 0.1277 0.1223 0.1724 -0.0121 0.0062  0.0143  115 ASN   A C   
2508 O  O   . ASN   A 115 ? 0.1264 0.1336 0.1799 -0.0115 0.0105  0.0220  115 ASN   A O   
2509 C  CB  . ASN   A 115 ? 0.1376 0.1323 0.1706 -0.0150 0.0109  0.0078  115 ASN   A CB  
2510 C  CG  . ASN   A 115 ? 0.1368 0.1483 0.1825 -0.0177 0.0232  0.0074  115 ASN   A CG  
2511 O  OD1 . ASN   A 115 ? 0.1364 0.2462 0.2033 -0.0173 0.0311  0.0259  115 ASN   A OD1 
2512 N  ND2 . ASN   A 115 ? 0.1395 0.1294 0.1843 -0.0115 0.0276  0.0188  115 ASN   A ND2 
2519 N  N   . PHE   A 116 ? 0.1218 0.1241 0.1775 -0.0022 0.0131  0.0203  116 PHE   A N   
2520 C  CA  . PHE   A 116 ? 0.1236 0.1320 0.1686 -0.0021 0.0110  0.0164  116 PHE   A CA  
2521 C  C   . PHE   A 116 ? 0.1219 0.1357 0.1763 -0.0084 0.0132  0.0188  116 PHE   A C   
2522 O  O   . PHE   A 116 ? 0.1292 0.1429 0.1853 -0.0030 0.0112  0.0303  116 PHE   A O   
2523 C  CB  . PHE   A 116 ? 0.1252 0.1226 0.1801 -0.0036 0.0201  0.0205  116 PHE   A CB  
2524 C  CG  . PHE   A 116 ? 0.1262 0.1247 0.1609 -0.0075 0.0110  0.0128  116 PHE   A CG  
2525 C  CD1 . PHE   A 116 ? 0.1264 0.1243 0.1645 -0.0101 0.0141  0.0130  116 PHE   A CD1 
2526 C  CD2 . PHE   A 116 ? 0.1315 0.1322 0.1728 -0.0095 0.0155  0.0223  116 PHE   A CD2 
2527 C  CE1 . PHE   A 116 ? 0.1309 0.1218 0.1774 -0.0153 0.0093  0.0097  116 PHE   A CE1 
2528 C  CE2 . PHE   A 116 ? 0.1307 0.1310 0.1766 -0.0078 0.0167  0.0186  116 PHE   A CE2 
2529 C  CZ  . PHE   A 116 ? 0.1359 0.1175 0.1716 -0.0021 0.0049  0.0140  116 PHE   A CZ  
2539 N  N   . ASN   A 117 ? 0.1230 0.1297 0.1932 -0.0070 0.0093  0.0246  117 ASN   A N   
2540 C  CA  . ASN   A 117 ? 0.1246 0.1285 0.1974 -0.0054 0.0100  0.0255  117 ASN   A CA  
2541 C  C   . ASN   A 117 ? 0.1272 0.1382 0.1999 -0.0016 0.0176  0.0255  117 ASN   A C   
2542 O  O   . ASN   A 117 ? 0.1380 0.1429 0.2185 -0.0096 -0.0090 0.0408  117 ASN   A O   
2543 C  CB  . ASN   A 117 ? 0.1215 0.1330 0.2025 -0.0010 0.0105  0.0305  117 ASN   A CB  
2544 C  CG  . ASN   A 117 ? 0.1250 0.1294 0.2015 -0.0029 0.0140  0.0338  117 ASN   A CG  
2545 O  OD1 . ASN   A 117 ? 0.1271 0.1519 0.2113 -0.0112 0.0129  0.0233  117 ASN   A OD1 
2546 N  ND2 . ASN   A 117 ? 0.1223 0.1294 0.2052 -0.0015 0.0116  0.0274  117 ASN   A ND2 
2553 N  N   . GLN   A 118 ? 0.1268 0.1380 0.1962 -0.0097 0.0040  0.0283  118 GLN   A N   
2554 C  CA  . GLN   A 118 ? 0.1311 0.1500 0.2073 -0.0075 -0.0018 0.0236  118 GLN   A CA  
2555 C  C   . GLN   A 118 ? 0.1349 0.1589 0.2003 -0.0087 -0.0026 0.0368  118 GLN   A C   
2556 O  O   . GLN   A 118 ? 0.1317 0.1876 0.2288 -0.0041 -0.0127 0.0131  118 GLN   A O   
2557 C  CB  . GLN   A 118 ? 0.1282 0.1480 0.2220 -0.0045 0.0080  0.0258  118 GLN   A CB  
2558 C  CG  . GLN   A 118 ? 0.1267 0.1502 0.2177 -0.0045 0.0052  0.0315  118 GLN   A CG  
2559 C  CD  . GLN   A 118 ? 0.1256 0.1529 0.2275 -0.0040 0.0093  0.0262  118 GLN   A CD  
2560 O  OE1 . GLN   A 118 ? 0.1326 0.1655 0.2357 0.0055  0.0033  0.0170  118 GLN   A OE1 
2561 N  NE2 . GLN   A 118 ? 0.1350 0.1509 0.2323 -0.0006 0.0038  0.0279  118 GLN   A NE2 
2570 N  N   . HIS   A 119 ? 0.1369 0.1575 0.1818 -0.0037 0.0037  0.0377  119 HIS   A N   
2571 C  CA  . HIS   A 119 ? 0.1458 0.1652 0.1863 -0.0091 -0.0002 0.0375  119 HIS   A CA  
2572 C  C   . HIS   A 119 ? 0.1522 0.1712 0.1827 -0.0137 0.0078  0.0408  119 HIS   A C   
2573 O  O   . HIS   A 119 ? 0.1531 0.1771 0.1878 -0.0286 -0.0030 0.0414  119 HIS   A O   
2574 C  CB  . HIS   A 119 ? 0.1530 0.1575 0.2028 -0.0093 0.0181  0.0389  119 HIS   A CB  
2575 C  CG  . HIS   A 119 ? 0.1513 0.1622 0.2512 -0.0004 0.0180  0.0432  119 HIS   A CG  
2576 N  ND1 . HIS   A 119 ? 0.1621 0.1800 0.3067 -0.0117 0.0085  0.0331  119 HIS   A ND1 
2577 C  CD2 . HIS   A 119 ? 0.1630 0.1745 0.2707 0.0148  0.0366  0.0632  119 HIS   A CD2 
2578 C  CE1 . HIS   A 119 ? 0.1630 0.1788 0.3181 -0.0147 0.0263  0.0522  119 HIS   A CE1 
2579 N  NE2 . HIS   A 119 ? 0.1712 0.1743 0.3071 0.0012  0.0447  0.0699  119 HIS   A NE2 
2587 N  N   . GLU   A 120 ? 0.1587 0.1954 0.1806 -0.0150 -0.0061 0.0696  120 GLU   A N   
2588 C  CA  . GLU   A 120 ? 0.1870 0.2303 0.2055 -0.0057 -0.0123 0.1090  120 GLU   A CA  
2589 C  C   . GLU   A 120 ? 0.1644 0.2126 0.1867 -0.0182 -0.0082 0.0936  120 GLU   A C   
2590 O  O   . GLU   A 120 ? 0.1630 0.2048 0.1993 -0.0242 -0.0134 0.0893  120 GLU   A O   
2591 C  CB  . GLU   A 120 ? 0.2638 0.2962 0.2667 0.0134  -0.0088 0.1502  120 GLU   A CB  
2592 C  CG  . GLU   A 120 ? 0.3624 0.3724 0.3851 0.0248  -0.0050 0.1488  120 GLU   A CG  
2593 C  CD  . GLU   A 120 ? 0.4383 0.4334 0.5063 0.0344  0.0040  0.1308  120 GLU   A CD  
2594 O  OE1 . GLU   A 120 ? 0.4609 0.4535 0.5307 0.0372  0.0072  0.1242  120 GLU   A OE1 
2595 O  OE2 . GLU   A 120 ? 0.4868 0.4868 0.5650 0.0371  0.0076  0.1229  120 GLU   A OE2 
2602 N  N   . VAL   A 121 ? 0.1596 0.2120 0.1626 -0.0171 0.0032  0.0684  121 VAL   A N   
2603 C  CA  . VAL   A 121 ? 0.1679 0.2127 0.1522 -0.0147 0.0081  0.0717  121 VAL   A CA  
2604 C  C   . VAL   A 121 ? 0.1543 0.1954 0.1352 -0.0248 -0.0019 0.0543  121 VAL   A C   
2605 O  O   . VAL   A 121 ? 0.1557 0.2013 0.1570 -0.0303 -0.0110 0.0442  121 VAL   A O   
2606 C  CB  . VAL   A 121 ? 0.2064 0.2458 0.1924 -0.0039 0.0183  0.0762  121 VAL   A CB  
2607 C  CG1 . VAL   A 121 ? 0.2094 0.2621 0.1924 0.0022  0.0249  0.0817  121 VAL   A CG1 
2608 C  CG2 . VAL   A 121 ? 0.2291 0.2603 0.2354 -0.0091 0.0151  0.0616  121 VAL   A CG2 
2618 N  N   . LEU   A 122 ? 0.1464 0.1694 0.1459 -0.0270 0.0009  0.0484  122 LEU   A N   
2619 C  CA  . LEU   A 122 ? 0.1538 0.1562 0.1438 -0.0237 0.0165  0.0359  122 LEU   A CA  
2620 C  C   . LEU   A 122 ? 0.1476 0.1548 0.1505 -0.0279 0.0039  0.0332  122 LEU   A C   
2621 O  O   . LEU   A 122 ? 0.1462 0.1633 0.1822 -0.0287 0.0026  0.0363  122 LEU   A O   
2622 C  CB  . LEU   A 122 ? 0.1679 0.1591 0.1755 -0.0068 0.0054  0.0485  122 LEU   A CB  
2623 C  CG  . LEU   A 122 ? 0.1683 0.1669 0.1726 -0.0074 0.0164  0.0423  122 LEU   A CG  
2624 C  CD1 . LEU   A 122 ? 0.1852 0.1701 0.1881 -0.0181 0.0236  0.0414  122 LEU   A CD1 
2625 C  CD2 . LEU   A 122 ? 0.1627 0.1612 0.1705 -0.0089 0.0253  0.0299  122 LEU   A CD2 
2637 N  N   . LEU   A 123 ? 0.1433 0.1534 0.1453 -0.0273 -0.0021 0.0287  123 LEU   A N   
2638 C  CA  . LEU   A 123 ? 0.1400 0.1545 0.1434 -0.0273 -0.0003 0.0276  123 LEU   A CA  
2639 C  C   . LEU   A 123 ? 0.1404 0.1471 0.1235 -0.0212 0.0022  0.0348  123 LEU   A C   
2640 O  O   . LEU   A 123 ? 0.1354 0.1588 0.1449 -0.0284 -0.0002 0.0320  123 LEU   A O   
2641 C  CB  . LEU   A 123 ? 0.1488 0.1642 0.1361 -0.0220 0.0112  0.0260  123 LEU   A CB  
2642 C  CG  . LEU   A 123 ? 0.1560 0.1799 0.1502 -0.0219 0.0147  0.0142  123 LEU   A CG  
2643 C  CD1 . LEU   A 123 ? 0.1544 0.1887 0.1604 -0.0149 0.0145  0.0073  123 LEU   A CD1 
2644 C  CD2 . LEU   A 123 ? 0.1676 0.1867 0.1556 -0.0218 0.0073  0.0113  123 LEU   A CD2 
2656 N  N   A ALA   A 124 ? 0.1359 0.1389 0.1202 -0.0195 0.0039  0.0241  124 ALA   A N   
2657 N  N   B ALA   A 124 ? 0.1393 0.1383 0.1307 -0.0203 -0.0000 0.0220  124 ALA   A N   
2658 C  CA  A ALA   A 124 ? 0.1249 0.1317 0.1214 -0.0101 0.0028  0.0233  124 ALA   A CA  
2659 C  CA  B ALA   A 124 ? 0.1397 0.1307 0.1455 -0.0221 -0.0039 0.0219  124 ALA   A CA  
2660 C  C   A ALA   A 124 ? 0.1216 0.1308 0.1181 -0.0090 0.0071  0.0244  124 ALA   A C   
2661 C  C   B ALA   A 124 ? 0.1342 0.1221 0.1415 -0.0186 -0.0013 0.0210  124 ALA   A C   
2662 O  O   A ALA   A 124 ? 0.1212 0.1392 0.1472 -0.0087 0.0229  0.0339  124 ALA   A O   
2663 O  O   B ALA   A 124 ? 0.1312 0.1199 0.1583 -0.0137 0.0044  0.0180  124 ALA   A O   
2664 C  CB  A ALA   A 124 ? 0.1215 0.1244 0.1460 0.0029  0.0033  0.0286  124 ALA   A CB  
2665 C  CB  B ALA   A 124 ? 0.1490 0.1299 0.1613 -0.0210 -0.0007 0.0176  124 ALA   A CB  
2676 N  N   A PRO   A 125 ? 0.1170 0.1344 0.1329 -0.0007 0.0123  0.0341  125 PRO   A N   
2677 N  N   B PRO   A 125 ? 0.1222 0.1127 0.1217 -0.0108 -0.0019 0.0241  125 PRO   A N   
2678 C  CA  A PRO   A 125 ? 0.1250 0.1417 0.1486 -0.0038 0.0054  0.0278  125 PRO   A CA  
2679 C  CA  B PRO   A 125 ? 0.1275 0.1196 0.1275 -0.0097 0.0007  0.0251  125 PRO   A CA  
2680 C  C   A PRO   A 125 ? 0.1210 0.1400 0.1400 -0.0049 0.0056  0.0320  125 PRO   A C   
2681 C  C   B PRO   A 125 ? 0.1367 0.1279 0.1347 -0.0063 -0.0018 0.0257  125 PRO   A C   
2682 O  O   A PRO   A 125 ? 0.1280 0.1369 0.1493 -0.0025 0.0008  0.0242  125 PRO   A O   
2683 O  O   B PRO   A 125 ? 0.1423 0.1274 0.1404 -0.0035 -0.0071 0.0198  125 PRO   A O   
2684 C  CB  A PRO   A 125 ? 0.1342 0.1443 0.1484 -0.0098 0.0071  0.0249  125 PRO   A CB  
2685 C  CB  B PRO   A 125 ? 0.1235 0.1146 0.1164 -0.0138 -0.0015 0.0270  125 PRO   A CB  
2686 C  CG  A PRO   A 125 ? 0.1384 0.1438 0.1619 -0.0098 0.0091  0.0282  125 PRO   A CG  
2687 C  CG  B PRO   A 125 ? 0.1159 0.1053 0.1175 -0.0117 0.0045  0.0254  125 PRO   A CG  
2688 C  CD  A PRO   A 125 ? 0.1224 0.1438 0.1505 -0.0049 0.0154  0.0224  125 PRO   A CD  
2689 C  CD  B PRO   A 125 ? 0.1107 0.0955 0.1057 -0.0109 0.0026  0.0241  125 PRO   A CD  
2704 N  N   A LEU   A 126 ? 0.1094 0.1445 0.1390 0.0006  0.0077  0.0240  126 LEU   A N   
2705 N  N   B LEU   A 126 ? 0.1397 0.1376 0.1475 -0.0030 -0.0020 0.0215  126 LEU   A N   
2706 C  CA  A LEU   A 126 ? 0.1169 0.1427 0.1412 -0.0055 0.0055  0.0230  126 LEU   A CA  
2707 C  CA  B LEU   A 126 ? 0.1367 0.1360 0.1425 0.0005  -0.0005 0.0205  126 LEU   A CA  
2708 C  C   A LEU   A 126 ? 0.1243 0.1370 0.1404 0.0013  -0.0055 0.0229  126 LEU   A C   
2709 C  C   B LEU   A 126 ? 0.1296 0.1253 0.1346 0.0034  -0.0030 0.0175  126 LEU   A C   
2710 O  O   A LEU   A 126 ? 0.1353 0.1377 0.1564 0.0078  0.0091  0.0320  126 LEU   A O   
2711 O  O   B LEU   A 126 ? 0.1302 0.1247 0.1429 -0.0036 -0.0145 0.0255  126 LEU   A O   
2712 C  CB  A LEU   A 126 ? 0.1232 0.1360 0.1579 -0.0028 0.0055  0.0189  126 LEU   A CB  
2713 C  CB  B LEU   A 126 ? 0.1413 0.1424 0.1644 -0.0013 0.0029  0.0060  126 LEU   A CB  
2714 C  CG  A LEU   A 126 ? 0.1230 0.1425 0.1761 0.0008  0.0144  0.0084  126 LEU   A CG  
2715 C  CG  B LEU   A 126 ? 0.1413 0.1406 0.1775 0.0000  0.0087  -0.0048 126 LEU   A CG  
2716 C  CD1 A LEU   A 126 ? 0.1320 0.1522 0.2159 -0.0017 0.0097  0.0099  126 LEU   A CD1 
2717 C  CD1 B LEU   A 126 ? 0.1434 0.1343 0.1903 0.0029  0.0063  -0.0205 126 LEU   A CD1 
2718 C  CD2 A LEU   A 126 ? 0.1378 0.1411 0.1637 -0.0116 0.0190  0.0169  126 LEU   A CD2 
2719 C  CD2 B LEU   A 126 ? 0.1352 0.1409 0.1805 0.0034  0.0047  0.0008  126 LEU   A CD2 
2742 N  N   A LEU   A 127 ? 0.1298 0.1360 0.1436 -0.0021 0.0004  0.0153  127 LEU   A N   
2743 N  N   B LEU   A 127 ? 0.1270 0.1198 0.1258 0.0047  0.0060  0.0207  127 LEU   A N   
2744 C  CA  A LEU   A 127 ? 0.1301 0.1367 0.1364 -0.0065 -0.0033 0.0110  127 LEU   A CA  
2745 C  CA  B LEU   A 127 ? 0.1264 0.1277 0.1297 0.0050  0.0044  0.0244  127 LEU   A CA  
2746 C  C   A LEU   A 127 ? 0.1270 0.1309 0.1294 -0.0039 0.0026  0.0130  127 LEU   A C   
2747 C  C   B LEU   A 127 ? 0.1257 0.1307 0.1385 0.0049  0.0057  0.0135  127 LEU   A C   
2748 O  O   A LEU   A 127 ? 0.1341 0.1316 0.1399 -0.0137 -0.0059 0.0163  127 LEU   A O   
2749 O  O   B LEU   A 127 ? 0.1302 0.1341 0.1377 0.0032  0.0133  0.0201  127 LEU   A O   
2750 C  CB  A LEU   A 127 ? 0.1367 0.1415 0.1456 0.0069  0.0034  0.0164  127 LEU   A CB  
2751 C  CB  B LEU   A 127 ? 0.1290 0.1422 0.1362 0.0046  -0.0012 0.0196  127 LEU   A CB  
2752 C  CG  A LEU   A 127 ? 0.1429 0.1451 0.1536 0.0063  -0.0050 0.0119  127 LEU   A CG  
2753 C  CG  B LEU   A 127 ? 0.1330 0.1591 0.1337 0.0066  -0.0056 0.0211  127 LEU   A CG  
2754 C  CD1 A LEU   A 127 ? 0.1442 0.1361 0.1732 0.0014  -0.0046 0.0112  127 LEU   A CD1 
2755 C  CD1 B LEU   A 127 ? 0.1316 0.1668 0.1461 0.0123  -0.0015 0.0172  127 LEU   A CD1 
2756 C  CD2 A LEU   A 127 ? 0.1557 0.1469 0.1716 0.0158  -0.0087 0.0112  127 LEU   A CD2 
2757 C  CD2 B LEU   A 127 ? 0.1395 0.1684 0.1372 0.0053  -0.0177 0.0081  127 LEU   A CD2 
2780 N  N   A SER   A 128 ? 0.1332 0.1325 0.1171 -0.0085 0.0013  0.0189  128 SER   A N   
2781 N  N   B SER   A 128 ? 0.1277 0.1299 0.1437 -0.0039 -0.0049 0.0101  128 SER   A N   
2782 C  CA  A SER   A 128 ? 0.1436 0.1340 0.1185 0.0003  0.0057  0.0133  128 SER   A CA  
2783 C  CA  B SER   A 128 ? 0.1270 0.1255 0.1383 -0.0054 -0.0087 0.0059  128 SER   A CA  
2784 C  C   A SER   A 128 ? 0.1511 0.1403 0.1202 0.0023  0.0032  0.0162  128 SER   A C   
2785 C  C   B SER   A 128 ? 0.1252 0.1263 0.1251 -0.0093 -0.0173 0.0093  128 SER   A C   
2786 O  O   A SER   A 128 ? 0.1597 0.1569 0.1418 0.0032  0.0134  0.0158  128 SER   A O   
2787 O  O   B SER   A 128 ? 0.1212 0.1303 0.1306 -0.0095 -0.0152 0.0043  128 SER   A O   
2788 C  CB  A SER   A 128 ? 0.1415 0.1357 0.1261 -0.0017 -0.0013 0.0180  128 SER   A CB  
2789 C  CB  B SER   A 128 ? 0.1301 0.1271 0.1424 -0.0059 -0.0077 0.0080  128 SER   A CB  
2790 O  OG  A SER   A 128 ? 0.1426 0.1471 0.1395 -0.0019 0.0054  0.0162  128 SER   A OG  
2791 O  OG  B SER   A 128 ? 0.1293 0.1332 0.1493 -0.0094 0.0111  0.0235  128 SER   A OG  
2802 N  N   A ALA   A 129 ? 0.1451 0.1421 0.1422 0.0019  0.0002  0.0179  129 ALA   A N   
2803 N  N   B ALA   A 129 ? 0.1237 0.1289 0.1291 -0.0072 -0.0203 0.0168  129 ALA   A N   
2804 C  CA  A ALA   A 129 ? 0.1421 0.1467 0.1565 0.0048  0.0021  0.0135  129 ALA   A CA  
2805 C  CA  B ALA   A 129 ? 0.1249 0.1288 0.1322 -0.0044 -0.0158 0.0163  129 ALA   A CA  
2806 C  C   A ALA   A 129 ? 0.1446 0.1380 0.1430 0.0052  0.0025  0.0057  129 ALA   A C   
2807 C  C   B ALA   A 129 ? 0.1328 0.1383 0.1428 0.0031  -0.0109 0.0193  129 ALA   A C   
2808 O  O   A ALA   A 129 ? 0.1482 0.1423 0.1420 -0.0056 0.0096  0.0122  129 ALA   A O   
2809 O  O   B ALA   A 129 ? 0.1338 0.1427 0.1371 0.0037  -0.0061 0.0215  129 ALA   A O   
2810 C  CB  A ALA   A 129 ? 0.1432 0.1620 0.1847 0.0083  0.0089  0.0167  129 ALA   A CB  
2811 C  CB  B ALA   A 129 ? 0.1188 0.1208 0.1155 -0.0038 -0.0148 0.0108  129 ALA   A CB  
2822 N  N   A GLY   A 130 ? 0.1470 0.1378 0.1711 0.0006  -0.0049 0.0060  130 GLY   A N   
2823 N  N   B GLY   A 130 ? 0.1365 0.1430 0.1667 0.0020  -0.0062 0.0209  130 GLY   A N   
2824 C  CA  A GLY   A 130 ? 0.1652 0.1377 0.1564 0.0054  -0.0108 0.0097  130 GLY   A CA  
2825 C  CA  B GLY   A 130 ? 0.1472 0.1443 0.1656 0.0073  -0.0008 0.0208  130 GLY   A CA  
2826 C  C   A GLY   A 130 ? 0.1723 0.1408 0.1439 0.0070  -0.0232 0.0063  130 GLY   A C   
2827 C  C   B GLY   A 130 ? 0.1548 0.1451 0.1599 0.0088  -0.0005 0.0161  130 GLY   A C   
2828 O  O   A GLY   A 130 ? 0.1774 0.1363 0.1547 0.0088  -0.0294 0.0020  130 GLY   A O   
2829 O  O   B GLY   A 130 ? 0.1603 0.1439 0.1578 0.0044  0.0049  0.0116  130 GLY   A O   
2836 N  N   A ILE   A 131 ? 0.1850 0.1384 0.1376 -0.0034 -0.0213 0.0158  131 ILE   A N   
2837 N  N   B ILE   A 131 ? 0.1643 0.1445 0.1623 0.0064  -0.0106 0.0187  131 ILE   A N   
2838 C  CA  A ILE   A 131 ? 0.1962 0.1380 0.1271 -0.0108 -0.0332 0.0133  131 ILE   A CA  
2839 C  CA  B ILE   A 131 ? 0.1728 0.1460 0.1560 0.0024  -0.0213 0.0150  131 ILE   A CA  
2840 C  C   A ILE   A 131 ? 0.1808 0.1394 0.1249 -0.0101 -0.0206 0.0312  131 ILE   A C   
2841 C  C   B ILE   A 131 ? 0.1672 0.1486 0.1585 0.0010  -0.0169 0.0182  131 ILE   A C   
2842 O  O   A ILE   A 131 ? 0.1878 0.1432 0.1447 -0.0060 -0.0139 0.0281  131 ILE   A O   
2843 O  O   B ILE   A 131 ? 0.1660 0.1504 0.1684 0.0038  -0.0139 0.0203  131 ILE   A O   
2844 C  CB  A ILE   A 131 ? 0.2210 0.1521 0.1286 -0.0229 -0.0348 0.0063  131 ILE   A CB  
2845 C  CB  B ILE   A 131 ? 0.1851 0.1531 0.1579 -0.0053 -0.0358 0.0139  131 ILE   A CB  
2846 C  CG1 A ILE   A 131 ? 0.2268 0.1778 0.1429 -0.0393 -0.0348 0.0098  131 ILE   A CG1 
2847 C  CG1 B ILE   A 131 ? 0.1870 0.1642 0.1678 -0.0085 -0.0494 0.0232  131 ILE   A CG1 
2848 C  CG2 A ILE   A 131 ? 0.2336 0.1407 0.1344 -0.0149 -0.0264 -0.0117 131 ILE   A CG2 
2849 C  CG2 B ILE   A 131 ? 0.1914 0.1536 0.1684 -0.0066 -0.0346 0.0010  131 ILE   A CG2 
2850 C  CD1 A ILE   A 131 ? 0.2303 0.1846 0.1697 -0.0448 -0.0351 0.0031  131 ILE   A CD1 
2851 C  CD1 B ILE   A 131 ? 0.1899 0.1713 0.1733 -0.0083 -0.0545 0.0297  131 ILE   A CD1 
2874 N  N   A PHE   A 132 ? 0.1677 0.1378 0.1284 -0.0090 -0.0158 0.0280  132 PHE   A N   
2875 N  N   B PHE   A 132 ? 0.1653 0.1497 0.1600 -0.0005 -0.0155 0.0161  132 PHE   A N   
2876 C  CA  A PHE   A 132 ? 0.1716 0.1396 0.1334 -0.0157 -0.0101 0.0129  132 PHE   A CA  
2877 C  CA  B PHE   A 132 ? 0.1713 0.1520 0.1619 -0.0039 -0.0145 0.0068  132 PHE   A CA  
2878 C  C   A PHE   A 132 ? 0.1707 0.1558 0.1421 -0.0169 -0.0141 0.0125  132 PHE   A C   
2879 C  C   B PHE   A 132 ? 0.1766 0.1606 0.1700 -0.0065 -0.0251 0.0049  132 PHE   A C   
2880 O  O   A PHE   A 132 ? 0.1718 0.1649 0.1448 -0.0247 -0.0160 0.0075  132 PHE   A O   
2881 O  O   B PHE   A 132 ? 0.1852 0.1673 0.1753 -0.0163 -0.0254 -0.0005 132 PHE   A O   
2882 C  CB  A PHE   A 132 ? 0.1676 0.1336 0.1269 -0.0123 -0.0114 0.0194  132 PHE   A CB  
2883 C  CB  B PHE   A 132 ? 0.1682 0.1461 0.1501 -0.0011 -0.0092 0.0012  132 PHE   A CB  
2884 C  CG  A PHE   A 132 ? 0.1658 0.1311 0.1230 -0.0016 -0.0152 0.0219  132 PHE   A CG  
2885 C  CG  B PHE   A 132 ? 0.1654 0.1444 0.1373 0.0067  -0.0076 -0.0066 132 PHE   A CG  
2886 C  CD1 A PHE   A 132 ? 0.1661 0.1454 0.1451 0.0033  -0.0135 0.0160  132 PHE   A CD1 
2887 C  CD1 B PHE   A 132 ? 0.1655 0.1518 0.1404 0.0111  -0.0050 -0.0120 132 PHE   A CD1 
2888 C  CD2 A PHE   A 132 ? 0.1664 0.1449 0.1459 -0.0005 -0.0182 0.0167  132 PHE   A CD2 
2889 C  CD2 B PHE   A 132 ? 0.1666 0.1441 0.1412 0.0124  -0.0063 -0.0146 132 PHE   A CD2 
2890 C  CE1 A PHE   A 132 ? 0.1668 0.1543 0.1522 -0.0017 -0.0195 0.0066  132 PHE   A CE1 
2891 C  CE1 B PHE   A 132 ? 0.1642 0.1564 0.1446 0.0118  -0.0096 -0.0122 132 PHE   A CE1 
2892 C  CE2 A PHE   A 132 ? 0.1609 0.1507 0.1512 -0.0012 -0.0184 0.0183  132 PHE   A CE2 
2893 C  CE2 B PHE   A 132 ? 0.1640 0.1513 0.1533 0.0162  -0.0074 -0.0124 132 PHE   A CE2 
2894 C  CZ  A PHE   A 132 ? 0.1623 0.1539 0.1528 -0.0065 -0.0214 0.0189  132 PHE   A CZ  
2895 C  CZ  B PHE   A 132 ? 0.1632 0.1554 0.1515 0.0116  -0.0098 -0.0102 132 PHE   A CZ  
2914 N  N   A GLY   A 133 ? 0.1748 0.1599 0.1406 -0.0077 -0.0243 0.0243  133 GLY   A N   
2915 N  N   B GLY   A 133 ? 0.1770 0.1589 0.1685 -0.0034 -0.0308 0.0063  133 GLY   A N   
2916 C  CA  A GLY   A 133 ? 0.1803 0.1740 0.1449 -0.0081 -0.0281 0.0220  133 GLY   A CA  
2917 C  CA  B GLY   A 133 ? 0.1767 0.1606 0.1651 -0.0030 -0.0268 0.0028  133 GLY   A CA  
2918 C  C   A GLY   A 133 ? 0.1870 0.1843 0.1476 -0.0116 -0.0377 0.0115  133 GLY   A C   
2919 C  C   B GLY   A 133 ? 0.1770 0.1646 0.1562 -0.0005 -0.0248 -0.0091 133 GLY   A C   
2920 O  O   A GLY   A 133 ? 0.1974 0.1986 0.1445 -0.0122 -0.0333 -0.0103 133 GLY   A O   
2921 O  O   B GLY   A 133 ? 0.1789 0.1734 0.1479 0.0044  -0.0209 -0.0300 133 GLY   A O   
2928 N  N   A ALA   A 134 ? 0.1849 0.1728 0.1502 -0.0139 -0.0331 0.0050  134 ALA   A N   
2929 N  N   B ALA   A 134 ? 0.1752 0.1549 0.1554 -0.0041 -0.0204 -0.0102 134 ALA   A N   
2930 C  CA  A ALA   A 134 ? 0.1815 0.1725 0.1720 -0.0070 -0.0263 0.0003  134 ALA   A CA  
2931 C  CA  B ALA   A 134 ? 0.1719 0.1504 0.1653 -0.0012 -0.0168 -0.0112 134 ALA   A CA  
2932 C  C   A ALA   A 134 ? 0.1825 0.1703 0.1610 -0.0059 -0.0199 0.0066  134 ALA   A C   
2933 C  C   B ALA   A 134 ? 0.1717 0.1498 0.1599 0.0027  -0.0194 -0.0101 134 ALA   A C   
2934 O  O   A ALA   A 134 ? 0.1972 0.1767 0.1695 -0.0172 -0.0166 0.0024  134 ALA   A O   
2935 O  O   B ALA   A 134 ? 0.1736 0.1541 0.1671 -0.0009 -0.0105 -0.0126 134 ALA   A O   
2936 C  CB  A ALA   A 134 ? 0.1903 0.1730 0.2092 -0.0039 -0.0259 -0.0022 134 ALA   A CB  
2937 C  CB  B ALA   A 134 ? 0.1712 0.1482 0.1825 -0.0023 -0.0139 -0.0098 134 ALA   A CB  
2948 N  N   A ASP   A 135 ? 0.1808 0.1668 0.1752 -0.0060 -0.0147 0.0058  135 ASP   A N   
2949 N  N   B ASP   A 135 ? 0.1765 0.1525 0.1583 0.0003  -0.0202 -0.0038 135 ASP   A N   
2950 C  CA  A ASP   A 135 ? 0.1778 0.1741 0.1909 -0.0120 -0.0236 0.0035  135 ASP   A CA  
2951 C  CA  B ASP   A 135 ? 0.1769 0.1554 0.1726 -0.0049 -0.0241 -0.0015 135 ASP   A CA  
2952 C  C   A ASP   A 135 ? 0.1659 0.1636 0.1994 -0.0085 -0.0146 0.0113  135 ASP   A C   
2953 C  C   B ASP   A 135 ? 0.1618 0.1447 0.1683 0.0016  -0.0199 -0.0002 135 ASP   A C   
2954 O  O   A ASP   A 135 ? 0.1613 0.1568 0.2109 -0.0060 -0.0101 0.0186  135 ASP   A O   
2955 O  O   B ASP   A 135 ? 0.1579 0.1410 0.1693 0.0020  -0.0150 0.0072  135 ASP   A O   
2956 C  CB  A ASP   A 135 ? 0.1971 0.2013 0.2254 -0.0300 -0.0384 -0.0077 135 ASP   A CB  
2957 C  CB  B ASP   A 135 ? 0.1881 0.1703 0.1901 -0.0101 -0.0311 -0.0030 135 ASP   A CB  
2958 C  CG  A ASP   A 135 ? 0.2162 0.2265 0.2630 -0.0470 -0.0472 -0.0074 135 ASP   A CG  
2959 C  CG  B ASP   A 135 ? 0.1948 0.1860 0.2115 -0.0145 -0.0362 -0.0022 135 ASP   A CG  
2960 O  OD1 A ASP   A 135 ? 0.2134 0.2358 0.2638 -0.0521 -0.0540 0.0113  135 ASP   A OD1 
2961 O  OD1 B ASP   A 135 ? 0.1920 0.1830 0.2169 -0.0089 -0.0331 -0.0003 135 ASP   A OD1 
2962 O  OD2 A ASP   A 135 ? 0.2408 0.2475 0.3042 -0.0504 -0.0291 -0.0112 135 ASP   A OD2 
2963 O  OD2 B ASP   A 135 ? 0.2042 0.1980 0.2323 -0.0204 -0.0417 -0.0055 135 ASP   A OD2 
2972 N  N   A PRO   A 136 ? 0.1553 0.1634 0.2020 -0.0029 -0.0077 0.0207  136 PRO   A N   
2973 N  N   B PRO   A 136 ? 0.1528 0.1376 0.1677 0.0051  -0.0123 -0.0081 136 PRO   A N   
2974 C  CA  A PRO   A 136 ? 0.1528 0.1643 0.2154 -0.0070 -0.0037 0.0056  136 PRO   A CA  
2975 C  CA  B PRO   A 136 ? 0.1505 0.1468 0.1750 -0.0000 -0.0086 -0.0137 136 PRO   A CA  
2976 C  C   A PRO   A 136 ? 0.1329 0.1578 0.2127 -0.0012 0.0044  0.0119  136 PRO   A C   
2977 C  C   B PRO   A 136 ? 0.1429 0.1510 0.1643 0.0007  -0.0022 -0.0076 136 PRO   A C   
2978 O  O   A PRO   A 136 ? 0.1297 0.1646 0.2106 -0.0084 0.0097  0.0140  136 PRO   A O   
2979 O  O   B PRO   A 136 ? 0.1418 0.1468 0.1517 0.0063  0.0067  -0.0088 136 PRO   A O   
2980 C  CB  A PRO   A 136 ? 0.1684 0.1666 0.2232 -0.0053 0.0010  -0.0004 136 PRO   A CB  
2981 C  CB  B PRO   A 136 ? 0.1598 0.1474 0.1838 0.0030  -0.0112 -0.0199 136 PRO   A CB  
2982 C  CG  A PRO   A 136 ? 0.1750 0.1670 0.2305 0.0013  -0.0013 0.0055  136 PRO   A CG  
2983 C  CG  B PRO   A 136 ? 0.1637 0.1444 0.1855 0.0074  -0.0084 -0.0198 136 PRO   A CG  
2984 C  CD  A PRO   A 136 ? 0.1681 0.1667 0.2166 0.0070  -0.0040 0.0164  136 PRO   A CD  
2985 C  CD  B PRO   A 136 ? 0.1581 0.1353 0.1729 0.0092  -0.0082 -0.0108 136 PRO   A CD  
3000 N  N   A ILE   A 137 ? 0.1322 0.1535 0.2274 -0.0047 -0.0097 0.0172  137 ILE   A N   
3001 N  N   B ILE   A 137 ? 0.1423 0.1513 0.1780 -0.0035 -0.0055 -0.0060 137 ILE   A N   
3002 C  CA  A ILE   A 137 ? 0.1390 0.1592 0.2258 -0.0133 -0.0189 0.0215  137 ILE   A CA  
3003 C  CA  B ILE   A 137 ? 0.1464 0.1563 0.1851 -0.0030 -0.0011 -0.0087 137 ILE   A CA  
3004 C  C   A ILE   A 137 ? 0.1409 0.1631 0.1995 -0.0157 -0.0199 0.0232  137 ILE   A C   
3005 C  C   B ILE   A 137 ? 0.1414 0.1605 0.1708 -0.0090 0.0095  -0.0073 137 ILE   A C   
3006 O  O   A ILE   A 137 ? 0.1530 0.1606 0.1978 -0.0133 -0.0175 0.0182  137 ILE   A O   
3007 O  O   B ILE   A 137 ? 0.1389 0.1608 0.1686 -0.0083 0.0110  -0.0111 137 ILE   A O   
3008 C  CB  A ILE   A 137 ? 0.1481 0.1705 0.2578 -0.0156 -0.0302 0.0198  137 ILE   A CB  
3009 C  CB  B ILE   A 137 ? 0.1544 0.1562 0.2076 0.0016  -0.0077 -0.0112 137 ILE   A CB  
3010 C  CG1 A ILE   A 137 ? 0.1555 0.1839 0.2895 -0.0133 -0.0294 0.0298  137 ILE   A CG1 
3011 C  CG1 B ILE   A 137 ? 0.1648 0.1627 0.2314 0.0082  -0.0229 -0.0035 137 ILE   A CG1 
3012 C  CG2 A ILE   A 137 ? 0.1529 0.1684 0.2559 -0.0175 -0.0282 0.0050  137 ILE   A CG2 
3013 C  CG2 B ILE   A 137 ? 0.1577 0.1545 0.2162 0.0039  -0.0045 -0.0173 137 ILE   A CG2 
3014 C  CD1 A ILE   A 137 ? 0.1712 0.1984 0.3079 -0.0100 -0.0175 0.0324  137 ILE   A CD1 
3015 C  CD1 B ILE   A 137 ? 0.1715 0.1642 0.2471 0.0089  -0.0290 0.0075  137 ILE   A CD1 
3038 N  N   A HIS   A 138 ? 0.1390 0.1790 0.1984 -0.0097 -0.0127 0.0263  138 HIS   A N   
3039 N  N   B HIS   A 138 ? 0.1423 0.1683 0.1725 -0.0105 0.0151  -0.0016 138 HIS   A N   
3040 C  CA  A HIS   A 138 ? 0.1429 0.1851 0.1931 -0.0100 -0.0072 0.0246  138 HIS   A CA  
3041 C  CA  B HIS   A 138 ? 0.1447 0.1662 0.1735 -0.0111 0.0123  0.0040  138 HIS   A CA  
3042 C  C   A HIS   A 138 ? 0.1354 0.1784 0.1886 -0.0081 -0.0012 0.0290  138 HIS   A C   
3043 C  C   B HIS   A 138 ? 0.1414 0.1668 0.1787 -0.0107 0.0066  0.0201  138 HIS   A C   
3044 O  O   A HIS   A 138 ? 0.1382 0.1830 0.1934 -0.0063 0.0040  0.0239  138 HIS   A O   
3045 O  O   B HIS   A 138 ? 0.1475 0.1704 0.1894 -0.0109 -0.0002 0.0169  138 HIS   A O   
3046 C  CB  A HIS   A 138 ? 0.1673 0.2056 0.1978 -0.0083 -0.0187 0.0148  138 HIS   A CB  
3047 C  CB  B HIS   A 138 ? 0.1475 0.1692 0.1726 -0.0094 0.0140  -0.0130 138 HIS   A CB  
3048 C  CG  A HIS   A 138 ? 0.1874 0.2121 0.1990 -0.0118 -0.0182 0.0102  138 HIS   A CG  
3049 C  CG  B HIS   A 138 ? 0.1540 0.1704 0.1765 -0.0123 0.0129  -0.0215 138 HIS   A CG  
3050 N  ND1 A HIS   A 138 ? 0.2037 0.2200 0.2199 -0.0162 -0.0167 0.0061  138 HIS   A ND1 
3051 N  ND1 B HIS   A 138 ? 0.1645 0.1764 0.1960 -0.0094 0.0068  -0.0251 138 HIS   A ND1 
3052 C  CD2 A HIS   A 138 ? 0.1909 0.2151 0.1952 -0.0067 -0.0127 0.0073  138 HIS   A CD2 
3053 C  CD2 B HIS   A 138 ? 0.1526 0.1658 0.1659 -0.0111 0.0184  -0.0226 138 HIS   A CD2 
3054 C  CE1 A HIS   A 138 ? 0.2107 0.2240 0.2285 -0.0068 -0.0116 0.0001  138 HIS   A CE1 
3055 C  CE1 B HIS   A 138 ? 0.1652 0.1726 0.1915 -0.0038 0.0098  -0.0248 138 HIS   A CE1 
3056 N  NE2 A HIS   A 138 ? 0.2013 0.2211 0.2042 -0.0012 -0.0046 0.0015  138 HIS   A NE2 
3057 N  NE2 B HIS   A 138 ? 0.1588 0.1683 0.1748 -0.0052 0.0182  -0.0273 138 HIS   A NE2 
3072 N  N   . SER   A 139 ? 0.1328 0.1634 0.1840 -0.0092 -0.0051 0.0289  139 SER   A N   
3073 C  CA  . SER   A 139 ? 0.1287 0.1601 0.1793 -0.0120 0.0031  0.0295  139 SER   A CA  
3074 C  C   . SER   A 139 ? 0.1262 0.1520 0.1722 -0.0068 0.0078  0.0249  139 SER   A C   
3075 O  O   . SER   A 139 ? 0.1206 0.1500 0.1913 -0.0121 0.0044  0.0256  139 SER   A O   
3076 C  CB  . SER   A 139 ? 0.1271 0.1611 0.1818 -0.0170 -0.0060 0.0335  139 SER   A CB  
3077 O  OG  . SER   A 139 ? 0.1362 0.1614 0.1866 -0.0224 -0.0128 0.0440  139 SER   A OG  
3084 N  N   A LEU   A 140 ? 0.1250 0.1544 0.1725 -0.0054 -0.0007 0.0309  140 LEU   A N   
3085 N  N   B LEU   A 140 ? 0.1255 0.1450 0.1508 -0.0110 0.0129  0.0283  140 LEU   A N   
3086 C  CA  A LEU   A 140 ? 0.1249 0.1503 0.1795 -0.0088 -0.0053 0.0257  140 LEU   A CA  
3087 C  CA  B LEU   A 140 ? 0.1243 0.1370 0.1447 -0.0143 0.0171  0.0228  140 LEU   A CA  
3088 C  C   A LEU   A 140 ? 0.1192 0.1602 0.1746 -0.0133 0.0003  0.0221  140 LEU   A C   
3089 C  C   B LEU   A 140 ? 0.1241 0.1402 0.1449 -0.0164 0.0129  0.0240  140 LEU   A C   
3090 O  O   A LEU   A 140 ? 0.1256 0.1593 0.1854 -0.0050 0.0053  0.0164  140 LEU   A O   
3091 O  O   B LEU   A 140 ? 0.1280 0.1359 0.1559 -0.0095 0.0028  0.0141  140 LEU   A O   
3092 C  CB  A LEU   A 140 ? 0.1295 0.1532 0.1949 -0.0114 -0.0059 0.0195  140 LEU   A CB  
3093 C  CB  B LEU   A 140 ? 0.1219 0.1389 0.1391 -0.0244 0.0198  0.0211  140 LEU   A CB  
3094 C  CG  A LEU   A 140 ? 0.1333 0.1693 0.1994 -0.0131 -0.0047 0.0334  140 LEU   A CG  
3095 C  CG  B LEU   A 140 ? 0.1227 0.1490 0.1396 -0.0260 0.0205  0.0280  140 LEU   A CG  
3096 C  CD1 A LEU   A 140 ? 0.1316 0.1618 0.2103 0.0037  -0.0061 0.0243  140 LEU   A CD1 
3097 C  CD1 B LEU   A 140 ? 0.1189 0.1449 0.1300 -0.0175 0.0243  0.0331  140 LEU   A CD1 
3098 C  CD2 A LEU   A 140 ? 0.1401 0.1937 0.2125 -0.0156 -0.0002 0.0315  140 LEU   A CD2 
3099 C  CD2 B LEU   A 140 ? 0.1245 0.1656 0.1566 -0.0261 0.0222  0.0261  140 LEU   A CD2 
3122 N  N   A ARG   A 141 ? 0.1271 0.1650 0.1784 -0.0130 -0.0014 0.0116  141 ARG   A N   
3123 N  N   B ARG   A 141 ? 0.1303 0.1487 0.1486 -0.0168 0.0120  0.0251  141 ARG   A N   
3124 C  CA  A ARG   A 141 ? 0.1427 0.1781 0.1902 -0.0209 -0.0053 -0.0008 141 ARG   A CA  
3125 C  CA  B ARG   A 141 ? 0.1313 0.1572 0.1468 -0.0240 0.0125  0.0162  141 ARG   A CA  
3126 C  C   A ARG   A 141 ? 0.1442 0.1619 0.1994 -0.0131 -0.0037 0.0001  141 ARG   A C   
3127 C  C   B ARG   A 141 ? 0.1318 0.1480 0.1512 -0.0200 0.0090  0.0151  141 ARG   A C   
3128 O  O   A ARG   A 141 ? 0.1429 0.1555 0.2150 -0.0094 -0.0023 -0.0022 141 ARG   A O   
3129 O  O   B ARG   A 141 ? 0.1303 0.1450 0.1645 -0.0246 0.0002  0.0171  141 ARG   A O   
3130 C  CB  A ARG   A 141 ? 0.1526 0.2106 0.2035 -0.0266 -0.0085 -0.0142 141 ARG   A CB  
3131 C  CB  B ARG   A 141 ? 0.1339 0.1763 0.1370 -0.0327 0.0152  0.0094  141 ARG   A CB  
3132 C  CG  A ARG   A 141 ? 0.1845 0.2393 0.2337 -0.0288 -0.0159 -0.0194 141 ARG   A CG  
3133 C  CG  B ARG   A 141 ? 0.1476 0.1882 0.1381 -0.0358 0.0110  0.0033  141 ARG   A CG  
3134 C  CD  A ARG   A 141 ? 0.2036 0.2543 0.2530 -0.0364 -0.0205 -0.0145 141 ARG   A CD  
3135 C  CD  B ARG   A 141 ? 0.1617 0.1869 0.1550 -0.0385 0.0084  -0.0011 141 ARG   A CD  
3136 N  NE  A ARG   A 141 ? 0.2077 0.2672 0.2738 -0.0415 -0.0160 -0.0011 141 ARG   A NE  
3137 N  NE  B ARG   A 141 ? 0.1692 0.1976 0.1576 -0.0345 0.0193  0.0035  141 ARG   A NE  
3138 C  CZ  A ARG   A 141 ? 0.2049 0.2861 0.2822 -0.0561 -0.0150 0.0012  141 ARG   A CZ  
3139 C  CZ  B ARG   A 141 ? 0.1705 0.2039 0.1577 -0.0340 0.0310  0.0075  141 ARG   A CZ  
3140 N  NH1 A ARG   A 141 ? 0.2077 0.2972 0.2874 -0.0543 -0.0111 0.0024  141 ARG   A NH1 
3141 N  NH1 B ARG   A 141 ? 0.1719 0.2154 0.1467 -0.0353 0.0372  0.0023  141 ARG   A NH1 
3142 N  NH2 A ARG   A 141 ? 0.2019 0.2937 0.2893 -0.0597 -0.0167 0.0062  141 ARG   A NH2 
3143 N  NH2 B ARG   A 141 ? 0.1727 0.2095 0.1765 -0.0278 0.0339  0.0106  141 ARG   A NH2 
3170 N  N   A VAL   A 142 ? 0.1362 0.1578 0.1905 -0.0122 -0.0060 -0.0012 142 VAL   A N   
3171 N  N   B VAL   A 142 ? 0.1303 0.1498 0.1554 -0.0136 0.0116  0.0137  142 VAL   A N   
3172 C  CA  A VAL   A 142 ? 0.1371 0.1467 0.1906 -0.0059 0.0074  0.0071  142 VAL   A CA  
3173 C  CA  B VAL   A 142 ? 0.1353 0.1464 0.1641 -0.0059 0.0118  0.0114  142 VAL   A CA  
3174 C  C   A VAL   A 142 ? 0.1241 0.1448 0.1919 -0.0138 0.0039  0.0131  142 VAL   A C   
3175 C  C   B VAL   A 142 ? 0.1265 0.1446 0.1741 -0.0112 0.0070  0.0125  142 VAL   A C   
3176 O  O   A VAL   A 142 ? 0.1329 0.1470 0.1952 -0.0059 0.0074  0.0203  142 VAL   A O   
3177 O  O   B VAL   A 142 ? 0.1300 0.1468 0.1742 -0.0053 0.0073  0.0116  142 VAL   A O   
3178 C  CB  A VAL   A 142 ? 0.1405 0.1473 0.1881 -0.0056 0.0161  0.0099  142 VAL   A CB  
3179 C  CB  B VAL   A 142 ? 0.1416 0.1520 0.1677 0.0001  0.0133  0.0094  142 VAL   A CB  
3180 C  CG1 A VAL   A 142 ? 0.1366 0.1318 0.1795 -0.0135 0.0249  0.0126  142 VAL   A CG1 
3181 C  CG1 B VAL   A 142 ? 0.1468 0.1490 0.1776 0.0037  0.0107  0.0013  142 VAL   A CG1 
3182 C  CG2 A VAL   A 142 ? 0.1507 0.1644 0.2046 -0.0005 0.0163  0.0072  142 VAL   A CG2 
3183 C  CG2 B VAL   A 142 ? 0.1480 0.1588 0.1679 0.0044  0.0103  0.0206  142 VAL   A CG2 
3202 N  N   . CYS   A 143 ? 0.1259 0.1447 0.1797 -0.0174 0.0024  0.0138  143 CYS   A N   
3203 C  CA  . CYS   A 143 ? 0.1264 0.1464 0.1903 -0.0140 0.0068  0.0231  143 CYS   A CA  
3204 C  C   . CYS   A 143 ? 0.1233 0.1435 0.1913 -0.0118 0.0019  0.0250  143 CYS   A C   
3205 O  O   . CYS   A 143 ? 0.1230 0.1441 0.1917 -0.0076 0.0025  0.0262  143 CYS   A O   
3206 C  CB  . CYS   A 143 ? 0.1359 0.1493 0.1925 -0.0099 0.0142  0.0296  143 CYS   A CB  
3207 S  SG  . CYS   A 143 ? 0.1519 0.1558 0.1819 -0.0006 0.0098  0.0202  143 CYS   A SG  
3214 N  N   . VAL   A 144 ? 0.1219 0.1498 0.2148 -0.0119 0.0097  0.0335  144 VAL   A N   
3215 C  CA  . VAL   A 144 ? 0.1278 0.1571 0.2403 -0.0172 0.0145  0.0394  144 VAL   A CA  
3216 C  C   . VAL   A 144 ? 0.1336 0.1489 0.2354 -0.0208 -0.0079 0.0303  144 VAL   A C   
3217 O  O   . VAL   A 144 ? 0.1535 0.1506 0.2396 -0.0093 -0.0112 0.0326  144 VAL   A O   
3218 C  CB  . VAL   A 144 ? 0.1527 0.1772 0.2922 -0.0092 0.0262  0.0406  144 VAL   A CB  
3219 C  CG1 . VAL   A 144 ? 0.1712 0.1894 0.3214 -0.0166 0.0141  0.0447  144 VAL   A CG1 
3220 C  CG2 . VAL   A 144 ? 0.1392 0.1881 0.3061 -0.0051 0.0375  0.0530  144 VAL   A CG2 
3230 N  N   . ASP   A 145 ? 0.1365 0.1447 0.2403 -0.0179 0.0003  0.0202  145 ASP   A N   
3231 C  CA  . ASP   A 145 ? 0.1495 0.1495 0.2435 -0.0187 -0.0003 0.0121  145 ASP   A CA  
3232 C  C   . ASP   A 145 ? 0.1508 0.1400 0.2492 -0.0124 0.0008  0.0036  145 ASP   A C   
3233 O  O   . ASP   A 145 ? 0.1623 0.1503 0.2983 -0.0145 -0.0027 -0.0248 145 ASP   A O   
3234 C  CB  . ASP   A 145 ? 0.1627 0.1745 0.2593 -0.0242 -0.0148 0.0098  145 ASP   A CB  
3235 C  CG  . ASP   A 145 ? 0.1812 0.2134 0.2902 -0.0410 -0.0266 0.0179  145 ASP   A CG  
3236 O  OD1 . ASP   A 145 ? 0.1772 0.2285 0.2964 -0.0543 -0.0197 0.0194  145 ASP   A OD1 
3237 O  OD2 . ASP   A 145 ? 0.1981 0.2384 0.3042 -0.0502 -0.0396 0.0186  145 ASP   A OD2 
3242 N  N   . THR   A 146 ? 0.1371 0.1330 0.2117 -0.0138 0.0042  0.0127  146 THR   A N   
3243 C  CA  . THR   A 146 ? 0.1323 0.1329 0.1993 -0.0067 0.0056  0.0113  146 THR   A CA  
3244 C  C   . THR   A 146 ? 0.1264 0.1300 0.2072 -0.0045 0.0120  0.0193  146 THR   A C   
3245 O  O   . THR   A 146 ? 0.1407 0.1445 0.2214 0.0047  -0.0007 0.0133  146 THR   A O   
3246 C  CB  . THR   A 146 ? 0.1304 0.1351 0.1978 -0.0047 0.0079  0.0112  146 THR   A CB  
3247 O  OG1 . THR   A 146 ? 0.1315 0.1500 0.2026 -0.0025 0.0032  0.0110  146 THR   A OG1 
3248 C  CG2 . THR   A 146 ? 0.1298 0.1404 0.2188 -0.0029 0.0091  0.0113  146 THR   A CG2 
3256 N  N   . VAL   A 147 ? 0.1233 0.1335 0.2041 -0.0038 0.0098  0.0123  147 VAL   A N   
3257 C  CA  . VAL   A 147 ? 0.1262 0.1382 0.2072 -0.0133 0.0178  0.0220  147 VAL   A CA  
3258 C  C   . VAL   A 147 ? 0.1302 0.1370 0.2228 -0.0109 0.0210  0.0347  147 VAL   A C   
3259 O  O   . VAL   A 147 ? 0.1341 0.1434 0.2304 -0.0163 0.0097  0.0355  147 VAL   A O   
3260 C  CB  . VAL   A 147 ? 0.1323 0.1396 0.1985 -0.0143 0.0155  0.0234  147 VAL   A CB  
3261 C  CG1 . VAL   A 147 ? 0.1585 0.1466 0.2001 -0.0100 0.0105  0.0310  147 VAL   A CG1 
3262 C  CG2 . VAL   A 147 ? 0.1401 0.1362 0.1911 -0.0082 0.0121  0.0219  147 VAL   A CG2 
3272 N  N   . ARG   A 148 ? 0.1294 0.1406 0.2245 -0.0130 0.0196  0.0461  148 ARG   A N   
3273 C  CA  . ARG   A 148 ? 0.1378 0.1442 0.2189 -0.0173 0.0090  0.0568  148 ARG   A CA  
3274 C  C   . ARG   A 148 ? 0.1472 0.1468 0.2168 -0.0155 0.0110  0.0659  148 ARG   A C   
3275 O  O   . ARG   A 148 ? 0.1746 0.1618 0.2339 -0.0224 0.0153  0.0575  148 ARG   A O   
3276 C  CB  . ARG   A 148 ? 0.1445 0.1481 0.2403 -0.0116 0.0186  0.0495  148 ARG   A CB  
3277 C  CG  . ARG   A 148 ? 0.1606 0.1455 0.2736 -0.0089 0.0325  0.0366  148 ARG   A CG  
3278 C  CD  . ARG   A 148 ? 0.1729 0.1460 0.2922 -0.0045 0.0434  0.0539  148 ARG   A CD  
3279 N  NE  . ARG   A 148 ? 0.1675 0.1534 0.2844 0.0078  0.0472  0.0577  148 ARG   A NE  
3280 C  CZ  . ARG   A 148 ? 0.1672 0.1403 0.2762 0.0038  0.0455  0.0466  148 ARG   A CZ  
3281 N  NH1 . ARG   A 148 ? 0.1751 0.1427 0.2828 -0.0084 0.0467  0.0221  148 ARG   A NH1 
3282 N  NH2 . ARG   A 148 ? 0.1593 0.1556 0.2766 0.0136  0.0452  0.0488  148 ARG   A NH2 
3296 N  N   . THR   A 149 ? 0.1461 0.1568 0.2088 -0.0186 -0.0030 0.0592  149 THR   A N   
3297 C  CA  . THR   A 149 ? 0.1471 0.1647 0.2080 -0.0180 0.0018  0.0544  149 THR   A CA  
3298 C  C   . THR   A 149 ? 0.1417 0.1629 0.1980 -0.0212 0.0041  0.0543  149 THR   A C   
3299 O  O   . THR   A 149 ? 0.1443 0.1689 0.2162 -0.0262 0.0056  0.0515  149 THR   A O   
3300 C  CB  . THR   A 149 ? 0.1469 0.1747 0.2112 -0.0159 0.0008  0.0486  149 THR   A CB  
3301 O  OG1 . THR   A 149 ? 0.1503 0.1659 0.2143 -0.0265 0.0051  0.0443  149 THR   A OG1 
3302 C  CG2 . THR   A 149 ? 0.1474 0.1862 0.2309 -0.0150 -0.0100 0.0412  149 THR   A CG2 
3310 N  N   . ASN   A 150 ? 0.1470 0.1667 0.1997 -0.0121 -0.0045 0.0651  150 ASN   A N   
3311 C  CA  . ASN   A 150 ? 0.1595 0.1752 0.1954 -0.0196 0.0050  0.0582  150 ASN   A CA  
3312 C  C   . ASN   A 150 ? 0.1422 0.1612 0.1851 -0.0214 -0.0036 0.0559  150 ASN   A C   
3313 O  O   . ASN   A 150 ? 0.1531 0.1728 0.2239 -0.0223 -0.0148 0.0492  150 ASN   A O   
3314 C  CB  . ASN   A 150 ? 0.2015 0.1985 0.2228 -0.0254 0.0220  0.0751  150 ASN   A CB  
3315 C  CG  . ASN   A 150 ? 0.2564 0.2304 0.2864 -0.0232 0.0082  0.0768  150 ASN   A CG  
3316 O  OD1 . ASN   A 150 ? 0.2834 0.2372 0.2986 -0.0277 0.0049  0.0905  150 ASN   A OD1 
3317 N  ND2 . ASN   A 150 ? 0.2800 0.2522 0.3189 -0.0149 0.0010  0.0696  150 ASN   A ND2 
3324 N  N   . VAL   A 151 ? 0.1417 0.1515 0.1872 -0.0234 0.0020  0.0488  151 VAL   A N   
3325 C  CA  . VAL   A 151 ? 0.1489 0.1563 0.1737 -0.0251 0.0001  0.0468  151 VAL   A CA  
3326 C  C   . VAL   A 151 ? 0.1397 0.1515 0.1835 -0.0315 0.0009  0.0520  151 VAL   A C   
3327 O  O   . VAL   A 151 ? 0.1496 0.1606 0.2161 -0.0248 0.0042  0.0413  151 VAL   A O   
3328 C  CB  . VAL   A 151 ? 0.1718 0.1735 0.1810 -0.0110 0.0052  0.0457  151 VAL   A CB  
3329 C  CG1 . VAL   A 151 ? 0.1658 0.1939 0.1949 -0.0071 -0.0031 0.0422  151 VAL   A CG1 
3330 C  CG2 . VAL   A 151 ? 0.1781 0.1704 0.1876 -0.0024 0.0228  0.0384  151 VAL   A CG2 
3340 N  N   . TYR   A 152 ? 0.1387 0.1520 0.1889 -0.0300 -0.0014 0.0476  152 TYR   A N   
3341 C  CA  . TYR   A 152 ? 0.1420 0.1627 0.1588 -0.0285 0.0036  0.0486  152 TYR   A CA  
3342 C  C   . TYR   A 152 ? 0.1362 0.1545 0.1555 -0.0215 0.0109  0.0385  152 TYR   A C   
3343 O  O   . TYR   A 152 ? 0.1481 0.1537 0.1648 -0.0292 0.0119  0.0335  152 TYR   A O   
3344 C  CB  . TYR   A 152 ? 0.1588 0.1708 0.1635 -0.0250 0.0115  0.0488  152 TYR   A CB  
3345 C  CG  . TYR   A 152 ? 0.1665 0.1953 0.1620 -0.0261 0.0140  0.0544  152 TYR   A CG  
3346 C  CD1 . TYR   A 152 ? 0.1790 0.2180 0.1853 -0.0158 0.0171  0.0629  152 TYR   A CD1 
3347 C  CD2 . TYR   A 152 ? 0.1744 0.2066 0.1580 -0.0365 0.0105  0.0486  152 TYR   A CD2 
3348 C  CE1 . TYR   A 152 ? 0.2090 0.2335 0.1993 -0.0121 0.0072  0.0704  152 TYR   A CE1 
3349 C  CE2 . TYR   A 152 ? 0.2008 0.2229 0.1724 -0.0384 0.0085  0.0600  152 TYR   A CE2 
3350 C  CZ  . TYR   A 152 ? 0.2243 0.2311 0.1805 -0.0258 0.0032  0.0842  152 TYR   A CZ  
3351 O  OH  . TYR   A 152 ? 0.2573 0.2508 0.2175 -0.0209 0.0058  0.0977  152 TYR   A OH  
3361 N  N   . LEU   A 153 ? 0.1343 0.1513 0.1641 -0.0253 0.0105  0.0425  153 LEU   A N   
3362 C  CA  . LEU   A 153 ? 0.1273 0.1475 0.1779 -0.0193 0.0117  0.0410  153 LEU   A CA  
3363 C  C   . LEU   A 153 ? 0.1346 0.1488 0.1815 -0.0139 0.0219  0.0403  153 LEU   A C   
3364 O  O   . LEU   A 153 ? 0.1418 0.1579 0.2023 -0.0151 0.0307  0.0342  153 LEU   A O   
3365 C  CB  . LEU   A 153 ? 0.1260 0.1522 0.1831 -0.0163 0.0113  0.0374  153 LEU   A CB  
3366 C  CG  . LEU   A 153 ? 0.1360 0.1511 0.1798 -0.0173 0.0111  0.0287  153 LEU   A CG  
3367 C  CD1 . LEU   A 153 ? 0.1467 0.1527 0.1859 -0.0140 0.0033  0.0277  153 LEU   A CD1 
3368 C  CD2 . LEU   A 153 ? 0.1437 0.1585 0.1777 -0.0182 0.0189  0.0100  153 LEU   A CD2 
3380 N  N   A ALA   A 154 ? 0.1367 0.1473 0.1923 -0.0114 0.0245  0.0374  154 ALA   A N   
3381 N  N   B ALA   A 154 ? 0.1375 0.1487 0.1737 -0.0106 0.0174  0.0393  154 ALA   A N   
3382 C  CA  A ALA   A 154 ? 0.1474 0.1508 0.1959 -0.0082 0.0341  0.0355  154 ALA   A CA  
3383 C  CA  B ALA   A 154 ? 0.1445 0.1506 0.1684 -0.0086 0.0174  0.0418  154 ALA   A CA  
3384 C  C   A ALA   A 154 ? 0.1412 0.1471 0.1941 -0.0047 0.0305  0.0341  154 ALA   A C   
3385 C  C   B ALA   A 154 ? 0.1414 0.1492 0.1612 -0.0121 0.0192  0.0443  154 ALA   A C   
3386 O  O   A ALA   A 154 ? 0.1489 0.1603 0.2029 -0.0080 0.0295  0.0273  154 ALA   A O   
3387 O  O   B ALA   A 154 ? 0.1462 0.1546 0.1492 -0.0149 0.0163  0.0462  154 ALA   A O   
3388 C  CB  A ALA   A 154 ? 0.1564 0.1574 0.2005 0.0043  0.0347  0.0228  154 ALA   A CB  
3389 C  CB  B ALA   A 154 ? 0.1507 0.1521 0.1733 -0.0006 0.0111  0.0367  154 ALA   A CB  
3400 N  N   A VAL   A 155 ? 0.1273 0.1287 0.1667 0.0052  0.0359  0.0491  155 VAL   A N   
3401 N  N   B VAL   A 155 ? 0.1345 0.1380 0.1621 -0.0140 0.0253  0.0474  155 VAL   A N   
3402 C  CA  A VAL   A 155 ? 0.1448 0.1504 0.1964 0.0096  0.0234  0.0552  155 VAL   A CA  
3403 C  CA  B VAL   A 155 ? 0.1528 0.1553 0.1870 -0.0169 0.0260  0.0442  155 VAL   A CA  
3404 C  CA  T VAL   A 155 ? 0.1612 0.1694 0.1948 0.0027  0.0354  0.0513  155 VAL   A CA  
3405 C  C   A VAL   A 155 ? 0.1549 0.1619 0.2152 0.0255  0.0193  0.0595  155 VAL   A C   
3406 C  C   B VAL   A 155 ? 0.1665 0.1703 0.2067 -0.0155 0.0301  0.0481  155 VAL   A C   
3407 C  C   T VAL   A 155 ? 0.1605 0.1678 0.1859 0.0115  0.0462  0.0537  155 VAL   A C   
3408 O  O   A VAL   A 155 ? 0.1527 0.1664 0.2264 0.0354  0.0234  0.0505  155 VAL   A O   
3409 O  O   B VAL   A 155 ? 0.1644 0.1725 0.2125 -0.0129 0.0362  0.0455  155 VAL   A O   
3410 O  O   T VAL   A 155 ? 0.1543 0.1725 0.1785 0.0181  0.0524  0.0512  155 VAL   A O   
3411 C  CB  A VAL   A 155 ? 0.1507 0.1582 0.1989 0.0138  0.0073  0.0542  155 VAL   A CB  
3412 C  CB  B VAL   A 155 ? 0.1576 0.1584 0.1838 -0.0033 0.0061  0.0447  155 VAL   A CB  
3413 C  CB  T VAL   A 155 ? 0.1622 0.1717 0.1954 0.0043  0.0174  0.0511  155 VAL   A CB  
3414 C  CG1 A VAL   A 155 ? 0.1640 0.1657 0.2061 0.0118  0.0008  0.0581  155 VAL   A CG1 
3415 C  CG1 B VAL   A 155 ? 0.1678 0.1612 0.1820 -0.0016 -0.0002 0.0520  155 VAL   A CG1 
3416 C  CG1 T VAL   A 155 ? 0.1714 0.1767 0.2011 0.0046  0.0096  0.0546  155 VAL   A CG1 
3417 C  CG2 A VAL   A 155 ? 0.1558 0.1661 0.2083 0.0161  -0.0081 0.0430  155 VAL   A CG2 
3418 C  CG2 B VAL   A 155 ? 0.1643 0.1649 0.1990 0.0068  -0.0068 0.0345  155 VAL   A CG2 
3419 C  CG2 T VAL   A 155 ? 0.1619 0.1748 0.2022 0.0036  0.0076  0.0437  155 VAL   A CG2 
3445 N  N   A PHE   A 156 ? 0.1689 0.1714 0.2279 0.0329  0.0138  0.0690  156 PHE   A N   
3446 N  N   B PHE   A 156 ? 0.1849 0.1862 0.2271 -0.0138 0.0296  0.0520  156 PHE   A N   
3447 N  N   T PHE   A 156 ? 0.1693 0.1626 0.1880 0.0154  0.0510  0.0573  156 PHE   A N   
3448 C  CA  A PHE   A 156 ? 0.1874 0.1796 0.2433 0.0404  0.0107  0.0628  156 PHE   A CA  
3449 C  CA  B PHE   A 156 ? 0.2049 0.2055 0.2478 -0.0117 0.0244  0.0459  156 PHE   A CA  
3450 C  CA  T PHE   A 156 ? 0.1820 0.1593 0.1825 0.0183  0.0497  0.0540  156 PHE   A CA  
3451 C  C   A PHE   A 156 ? 0.1884 0.1847 0.2242 0.0498  0.0237  0.0588  156 PHE   A C   
3452 C  C   B PHE   A 156 ? 0.2130 0.2195 0.2479 -0.0073 0.0286  0.0549  156 PHE   A C   
3453 C  C   T PHE   A 156 ? 0.1815 0.1679 0.1818 0.0236  0.0533  0.0524  156 PHE   A C   
3454 O  O   A PHE   A 156 ? 0.1885 0.1863 0.2151 0.0422  0.0343  0.0432  156 PHE   A O   
3455 O  O   B PHE   A 156 ? 0.2108 0.2205 0.2511 -0.0146 0.0290  0.0497  156 PHE   A O   
3456 O  O   T PHE   A 156 ? 0.1864 0.1684 0.1841 0.0230  0.0558  0.0305  156 PHE   A O   
3457 C  CB  A PHE   A 156 ? 0.2056 0.1863 0.2670 0.0329  0.0020  0.0643  156 PHE   A CB  
3458 C  CB  B PHE   A 156 ? 0.2170 0.2139 0.2685 -0.0174 0.0184  0.0311  156 PHE   A CB  
3459 C  CB  T PHE   A 156 ? 0.1897 0.1456 0.1735 0.0197  0.0458  0.0546  156 PHE   A CB  
3460 C  CG  A PHE   A 156 ? 0.2198 0.1898 0.2846 0.0300  -0.0052 0.0594  156 PHE   A CG  
3461 C  CG  B PHE   A 156 ? 0.2273 0.2260 0.2878 -0.0215 0.0144  0.0154  156 PHE   A CG  
3462 C  CG  T PHE   A 156 ? 0.1960 0.1421 0.1553 0.0226  0.0397  0.0618  156 PHE   A CG  
3463 C  CD1 A PHE   A 156 ? 0.2254 0.1892 0.2876 0.0287  0.0061  0.0520  156 PHE   A CD1 
3464 C  CD1 B PHE   A 156 ? 0.2319 0.2325 0.2906 -0.0180 0.0119  0.0057  156 PHE   A CD1 
3465 C  CD1 T PHE   A 156 ? 0.2025 0.1465 0.1750 0.0241  0.0293  0.0508  156 PHE   A CD1 
3466 C  CD2 A PHE   A 156 ? 0.2260 0.1967 0.2881 0.0355  -0.0121 0.0568  156 PHE   A CD2 
3467 C  CD2 B PHE   A 156 ? 0.2306 0.2329 0.2925 -0.0233 0.0166  0.0130  156 PHE   A CD2 
3468 C  CD2 T PHE   A 156 ? 0.2009 0.1398 0.1674 0.0254  0.0289  0.0645  156 PHE   A CD2 
3469 C  CE1 A PHE   A 156 ? 0.2336 0.1893 0.2948 0.0266  0.0139  0.0501  156 PHE   A CE1 
3470 C  CE1 B PHE   A 156 ? 0.2349 0.2389 0.2928 -0.0163 0.0109  -0.0006 156 PHE   A CE1 
3471 C  CE1 T PHE   A 156 ? 0.2054 0.1491 0.1868 0.0280  0.0267  0.0437  156 PHE   A CE1 
3472 C  CE2 A PHE   A 156 ? 0.2351 0.2004 0.2901 0.0356  -0.0087 0.0469  156 PHE   A CE2 
3473 C  CE2 B PHE   A 156 ? 0.2327 0.2367 0.2910 -0.0224 0.0167  0.0125  156 PHE   A CE2 
3474 C  CE2 T PHE   A 156 ? 0.2080 0.1460 0.1782 0.0234  0.0241  0.0580  156 PHE   A CE2 
3475 C  CZ  A PHE   A 156 ? 0.2376 0.1989 0.2970 0.0344  0.0046  0.0422  156 PHE   A CZ  
3476 C  CZ  B PHE   A 156 ? 0.2351 0.2423 0.2939 -0.0143 0.0121  0.0056  156 PHE   A CZ  
3477 C  CZ  T PHE   A 156 ? 0.2055 0.1449 0.1872 0.0209  0.0284  0.0517  156 PHE   A CZ  
3505 N  N   A ASP   A 157 ? 0.1960 0.1954 0.2227 0.0607  0.0172  0.0620  157 ASP   A N   
3506 N  N   B ASP   A 157 ? 0.2248 0.2379 0.2527 0.0026  0.0281  0.0666  157 ASP   A N   
3507 N  N   T ASP   A 157 ? 0.1773 0.1832 0.1834 0.0308  0.0442  0.0646  157 ASP   A N   
3508 C  CA  A ASP   A 157 ? 0.2085 0.2173 0.2355 0.0640  0.0165  0.0625  157 ASP   A CA  
3509 C  CA  B ASP   A 157 ? 0.2365 0.2537 0.2572 0.0134  0.0250  0.0675  157 ASP   A CA  
3510 C  CA  T ASP   A 157 ? 0.1764 0.2005 0.1901 0.0377  0.0411  0.0679  157 ASP   A CA  
3511 C  C   A ASP   A 157 ? 0.1989 0.2364 0.2438 0.0654  0.0228  0.0677  157 ASP   A C   
3512 C  C   B ASP   A 157 ? 0.2397 0.2608 0.2396 0.0248  0.0299  0.0623  157 ASP   A C   
3513 C  C   T ASP   A 157 ? 0.1744 0.2230 0.1997 0.0428  0.0498  0.0730  157 ASP   A C   
3514 O  O   A ASP   A 157 ? 0.1921 0.2350 0.2419 0.0658  0.0281  0.0712  157 ASP   A O   
3515 O  O   B ASP   A 157 ? 0.2397 0.2581 0.2424 0.0266  0.0328  0.0593  157 ASP   A O   
3516 O  O   T ASP   A 157 ? 0.1658 0.2222 0.2021 0.0428  0.0586  0.0769  157 ASP   A O   
3517 C  CB  A ASP   A 157 ? 0.2255 0.2188 0.2514 0.0716  0.0113  0.0514  157 ASP   A CB  
3518 C  CB  B ASP   A 157 ? 0.2434 0.2635 0.2853 0.0151  0.0169  0.0691  157 ASP   A CB  
3519 C  CB  T ASP   A 157 ? 0.1769 0.1948 0.1990 0.0433  0.0248  0.0633  157 ASP   A CB  
3520 C  CG  A ASP   A 157 ? 0.2390 0.2228 0.2716 0.0777  0.0084  0.0473  157 ASP   A CG  
3521 C  CG  B ASP   A 157 ? 0.2476 0.2696 0.3103 0.0157  0.0139  0.0743  157 ASP   A CG  
3522 C  CG  T ASP   A 157 ? 0.1735 0.1880 0.2078 0.0443  0.0081  0.0665  157 ASP   A CG  
3523 O  OD1 A ASP   A 157 ? 0.2519 0.2271 0.2870 0.0753  0.0034  0.0415  157 ASP   A OD1 
3524 O  OD1 B ASP   A 157 ? 0.2458 0.2677 0.3211 0.0200  0.0132  0.0764  157 ASP   A OD1 
3525 O  OD1 T ASP   A 157 ? 0.1787 0.1847 0.2335 0.0398  0.0007  0.0506  157 ASP   A OD1 
3526 O  OD2 A ASP   A 157 ? 0.2366 0.2175 0.2777 0.0834  0.0124  0.0500  157 ASP   A OD2 
3527 O  OD2 B ASP   A 157 ? 0.2525 0.2764 0.3202 0.0131  0.0053  0.0734  157 ASP   A OD2 
3528 O  OD2 T ASP   A 157 ? 0.1643 0.1842 0.1958 0.0486  -0.0019 0.0781  157 ASP   A OD2 
3541 N  N   A LYS   A 158 ? 0.2028 0.2567 0.2592 0.0612  0.0343  0.0635  158 LYS   A N   
3542 N  N   B LYS   A 158 ? 0.2452 0.2729 0.2381 0.0328  0.0276  0.0554  158 LYS   A N   
3543 N  N   T LYS   A 158 ? 0.1888 0.2465 0.2133 0.0425  0.0562  0.0642  158 LYS   A N   
3544 C  CA  A LYS   A 158 ? 0.1984 0.2751 0.2760 0.0609  0.0474  0.0567  158 LYS   A CA  
3545 C  CA  B LYS   A 158 ? 0.2492 0.2847 0.2473 0.0400  0.0223  0.0428  158 LYS   A CA  
3546 C  CA  T LYS   A 158 ? 0.2017 0.2682 0.2417 0.0464  0.0525  0.0504  158 LYS   A CA  
3547 C  C   A LYS   A 158 ? 0.1782 0.2790 0.2614 0.0646  0.0394  0.0608  158 LYS   A C   
3548 C  C   B LYS   A 158 ? 0.2349 0.2841 0.2294 0.0515  0.0074  0.0391  158 LYS   A C   
3549 C  C   T LYS   A 158 ? 0.2007 0.2721 0.2396 0.0516  0.0374  0.0460  158 LYS   A C   
3550 O  O   A LYS   A 158 ? 0.1683 0.2889 0.2619 0.0589  0.0505  0.0610  158 LYS   A O   
3551 O  O   B LYS   A 158 ? 0.2298 0.2925 0.2195 0.0503  0.0069  0.0412  158 LYS   A O   
3552 O  O   T LYS   A 158 ? 0.1967 0.2762 0.2430 0.0506  0.0371  0.0424  158 LYS   A O   
3553 C  CB  A LYS   A 158 ? 0.2121 0.2842 0.3063 0.0573  0.0678  0.0531  158 LYS   A CB  
3554 C  CB  B LYS   A 158 ? 0.2654 0.2969 0.2792 0.0320  0.0312  0.0331  158 LYS   A CB  
3555 C  CB  T LYS   A 158 ? 0.2171 0.2811 0.2771 0.0432  0.0629  0.0432  158 LYS   A CB  
3556 C  CG  A LYS   A 158 ? 0.2260 0.2915 0.3320 0.0576  0.0804  0.0531  158 LYS   A CG  
3557 C  CG  B LYS   A 158 ? 0.2780 0.3083 0.3114 0.0255  0.0414  0.0252  158 LYS   A CG  
3558 C  CG  T LYS   A 158 ? 0.2330 0.2919 0.3118 0.0431  0.0659  0.0395  158 LYS   A CG  
3559 C  CD  A LYS   A 158 ? 0.2357 0.2985 0.3533 0.0539  0.0947  0.0594  158 LYS   A CD  
3560 C  CD  B LYS   A 158 ? 0.2890 0.3180 0.3462 0.0203  0.0479  0.0196  158 LYS   A CD  
3561 C  CD  T LYS   A 158 ? 0.2476 0.3013 0.3453 0.0431  0.0671  0.0408  158 LYS   A CD  
3562 C  CE  A LYS   A 158 ? 0.2415 0.3017 0.3690 0.0491  0.1024  0.0700  158 LYS   A CE  
3563 C  CE  B LYS   A 158 ? 0.2957 0.3242 0.3715 0.0166  0.0542  0.0166  158 LYS   A CE  
3564 C  CE  T LYS   A 158 ? 0.2570 0.3053 0.3711 0.0425  0.0648  0.0447  158 LYS   A CE  
3565 N  NZ  A LYS   A 158 ? 0.2427 0.3021 0.3745 0.0450  0.1081  0.0779  158 LYS   A NZ  
3566 N  NZ  B LYS   A 158 ? 0.2996 0.3277 0.3861 0.0147  0.0587  0.0159  158 LYS   A NZ  
3567 N  NZ  T LYS   A 158 ? 0.2622 0.3069 0.3838 0.0420  0.0637  0.0471  158 LYS   A NZ  
3607 N  N   A ASN   A 159 ? 0.1750 0.2698 0.2590 0.0643  0.0214  0.0580  159 ASN   A N   
3608 N  N   B ASN   A 159 ? 0.2265 0.2756 0.2260 0.0572  -0.0010 0.0281  159 ASN   A N   
3609 N  N   T ASN   A 159 ? 0.2074 0.2698 0.2448 0.0514  0.0275  0.0407  159 ASN   A N   
3610 C  CA  A ASN   A 159 ? 0.1715 0.2636 0.2515 0.0529  0.0027  0.0549  159 ASN   A CA  
3611 C  CA  B ASN   A 159 ? 0.2197 0.2663 0.2335 0.0562  -0.0160 0.0170  159 ASN   A CA  
3612 C  CA  T ASN   A 159 ? 0.2174 0.2698 0.2510 0.0438  0.0158  0.0379  159 ASN   A CA  
3613 C  C   A ASN   A 159 ? 0.1546 0.2530 0.2217 0.0399  0.0039  0.0430  159 ASN   A C   
3614 C  C   B ASN   A 159 ? 0.1971 0.2525 0.2102 0.0467  -0.0163 0.0122  159 ASN   A C   
3615 C  C   T ASN   A 159 ? 0.2234 0.2677 0.2436 0.0387  0.0192  0.0278  159 ASN   A C   
3616 O  O   A ASN   A 159 ? 0.1438 0.2502 0.2217 0.0338  -0.0111 0.0325  159 ASN   A O   
3617 O  O   B ASN   A 159 ? 0.1913 0.2600 0.2057 0.0507  -0.0244 0.0116  159 ASN   A O   
3618 O  O   T ASN   A 159 ? 0.2224 0.2647 0.2449 0.0363  0.0179  0.0203  159 ASN   A O   
3619 C  CB  A ASN   A 159 ? 0.1867 0.2717 0.2866 0.0488  -0.0096 0.0607  159 ASN   A CB  
3620 C  CB  B ASN   A 159 ? 0.2338 0.2698 0.2665 0.0596  -0.0298 0.0087  159 ASN   A CB  
3621 C  CB  T ASN   A 159 ? 0.2237 0.2748 0.2765 0.0394  0.0045  0.0451  159 ASN   A CB  
3622 C  CG  A ASN   A 159 ? 0.2022 0.2816 0.3289 0.0441  -0.0098 0.0571  159 ASN   A CG  
3623 C  CG  B ASN   A 159 ? 0.2485 0.2753 0.3009 0.0543  -0.0407 -0.0002 159 ASN   A CG  
3624 C  CG  T ASN   A 159 ? 0.2304 0.2808 0.3074 0.0347  0.0012  0.0460  159 ASN   A CG  
3625 O  OD1 A ASN   A 159 ? 0.2068 0.2882 0.3511 0.0421  -0.0018 0.0573  159 ASN   A OD1 
3626 O  OD1 B ASN   A 159 ? 0.2565 0.2731 0.3208 0.0493  -0.0470 -0.0041 159 ASN   A OD1 
3627 O  OD1 T ASN   A 159 ? 0.2299 0.2850 0.3237 0.0327  0.0084  0.0473  159 ASN   A OD1 
3628 N  ND2 A ASN   A 159 ? 0.2030 0.2829 0.3375 0.0439  -0.0151 0.0555  159 ASN   A ND2 
3629 N  ND2 B ASN   A 159 ? 0.2494 0.2785 0.3104 0.0516  -0.0428 -0.0027 159 ASN   A ND2 
3630 N  ND2 T ASN   A 159 ? 0.2307 0.2816 0.3136 0.0340  -0.0045 0.0470  159 ASN   A ND2 
3649 N  N   A LEU   A 160 ? 0.1449 0.2378 0.1899 0.0339  0.0084  0.0517  160 LEU   A N   
3650 N  N   B LEU   A 160 ? 0.1802 0.2313 0.1889 0.0324  -0.0112 0.0187  160 LEU   A N   
3651 N  N   T LEU   A 160 ? 0.2285 0.2646 0.2368 0.0361  0.0196  0.0310  160 LEU   A N   
3652 C  CA  A LEU   A 160 ? 0.1396 0.2240 0.1662 0.0192  0.0185  0.0628  160 LEU   A CA  
3653 C  CA  B LEU   A 160 ? 0.1708 0.2178 0.1818 0.0169  0.0009  0.0238  160 LEU   A CA  
3654 C  CA  T LEU   A 160 ? 0.2367 0.2618 0.2351 0.0300  0.0233  0.0369  160 LEU   A CA  
3655 C  C   A LEU   A 160 ? 0.1274 0.2156 0.1393 0.0103  0.0201  0.0540  160 LEU   A C   
3656 C  C   B LEU   A 160 ? 0.1532 0.2084 0.1649 0.0161  0.0012  0.0237  160 LEU   A C   
3657 O  O   A LEU   A 160 ? 0.1176 0.2109 0.1264 0.0036  0.0213  0.0467  160 LEU   A O   
3658 O  O   B LEU   A 160 ? 0.1528 0.2024 0.1711 0.0162  0.0014  0.0148  160 LEU   A O   
3659 C  CB  A LEU   A 160 ? 0.1441 0.2216 0.1739 0.0149  0.0185  0.0800  160 LEU   A CB  
3660 C  CB  B LEU   A 160 ? 0.1849 0.2228 0.1939 0.0053  0.0127  0.0234  160 LEU   A CB  
3661 C  CB  T LEU   A 160 ? 0.2433 0.2601 0.2376 0.0253  0.0251  0.0454  160 LEU   A CB  
3662 C  CG  A LEU   A 160 ? 0.1484 0.2245 0.1861 0.0080  0.0290  0.0841  160 LEU   A CG  
3663 C  CG  B LEU   A 160 ? 0.2031 0.2377 0.2330 -0.0016 0.0209  0.0169  160 LEU   A CG  
3664 C  CG  T LEU   A 160 ? 0.2510 0.2626 0.2434 0.0211  0.0270  0.0469  160 LEU   A CG  
3665 C  CD1 A LEU   A 160 ? 0.1586 0.2291 0.1990 0.0031  0.0414  0.0818  160 LEU   A CD1 
3666 C  CD1 B LEU   A 160 ? 0.2091 0.2432 0.2465 -0.0020 0.0233  0.0136  160 LEU   A CD1 
3667 C  CD1 T LEU   A 160 ? 0.2513 0.2603 0.2414 0.0167  0.0329  0.0478  160 LEU   A CD1 
3668 C  CD2 A LEU   A 160 ? 0.1506 0.2235 0.1971 0.0069  0.0305  0.0765  160 LEU   A CD2 
3669 C  CD2 B LEU   A 160 ? 0.2100 0.2426 0.2454 -0.0064 0.0206  0.0133  160 LEU   A CD2 
3670 C  CD2 T LEU   A 160 ? 0.2529 0.2626 0.2437 0.0221  0.0283  0.0532  160 LEU   A CD2 
3703 N  N   A TYR   A 161 ? 0.1433 0.2176 0.1685 0.0035  0.0201  0.0543  161 TYR   A N   
3704 N  N   B TYR   A 161 ? 0.1455 0.2064 0.1540 0.0162  0.0162  0.0296  161 TYR   A N   
3705 C  CA  A TYR   A 161 ? 0.1446 0.2307 0.1795 -0.0025 0.0243  0.0448  161 TYR   A CA  
3706 C  CA  B TYR   A 161 ? 0.1520 0.2094 0.1603 0.0119  0.0120  0.0455  161 TYR   A CA  
3707 C  C   A TYR   A 161 ? 0.1448 0.2561 0.2076 -0.0087 0.0190  0.0423  161 TYR   A C   
3708 C  C   B TYR   A 161 ? 0.1487 0.2178 0.1747 0.0073  0.0052  0.0491  161 TYR   A C   
3709 O  O   A TYR   A 161 ? 0.1346 0.2547 0.2139 -0.0178 0.0186  0.0489  161 TYR   A O   
3710 O  O   B TYR   A 161 ? 0.1461 0.2192 0.1749 -0.0021 0.0023  0.0567  161 TYR   A O   
3711 C  CB  A TYR   A 161 ? 0.1507 0.2269 0.1818 -0.0018 0.0282  0.0471  161 TYR   A CB  
3712 C  CB  B TYR   A 161 ? 0.1629 0.2054 0.1672 0.0102  0.0087  0.0564  161 TYR   A CB  
3713 C  CG  A TYR   A 161 ? 0.1462 0.2182 0.1963 -0.0012 0.0194  0.0488  161 TYR   A CG  
3714 C  CG  B TYR   A 161 ? 0.1702 0.2060 0.1880 0.0079  0.0065  0.0586  161 TYR   A CG  
3715 C  CD1 A TYR   A 161 ? 0.1440 0.2061 0.2081 -0.0031 0.0163  0.0431  161 TYR   A CD1 
3716 C  CD1 B TYR   A 161 ? 0.1737 0.2041 0.1979 0.0077  0.0057  0.0556  161 TYR   A CD1 
3717 C  CD2 A TYR   A 161 ? 0.1443 0.2196 0.1994 0.0075  0.0104  0.0495  161 TYR   A CD2 
3718 C  CD2 B TYR   A 161 ? 0.1749 0.2066 0.2053 0.0089  0.0088  0.0591  161 TYR   A CD2 
3719 C  CE1 A TYR   A 161 ? 0.1418 0.1915 0.2061 -0.0024 0.0080  0.0382  161 TYR   A CE1 
3720 C  CE1 B TYR   A 161 ? 0.1760 0.2048 0.2042 0.0093  0.0043  0.0522  161 TYR   A CE1 
3721 C  CE2 A TYR   A 161 ? 0.1454 0.2093 0.2066 0.0006  0.0115  0.0521  161 TYR   A CE2 
3722 C  CE2 B TYR   A 161 ? 0.1776 0.2047 0.2135 0.0060  0.0104  0.0599  161 TYR   A CE2 
3723 C  CZ  A TYR   A 161 ? 0.1501 0.1920 0.1974 -0.0066 0.0015  0.0484  161 TYR   A CZ  
3724 C  CZ  B TYR   A 161 ? 0.1833 0.2041 0.2136 0.0079  0.0073  0.0570  161 TYR   A CZ  
3725 O  OH  A TYR   A 161 ? 0.1645 0.1791 0.1985 -0.0068 -0.0041 0.0498  161 TYR   A OH  
3726 O  OH  B TYR   A 161 ? 0.1940 0.2060 0.2379 0.0094  0.0051  0.0491  161 TYR   A OH  
3745 N  N   A ASP   A 162 ? 0.1412 0.2795 0.2131 -0.0060 0.0253  0.0423  162 ASP   A N   
3746 N  N   B ASP   A 162 ? 0.1462 0.2243 0.1890 0.0075  0.0105  0.0513  162 ASP   A N   
3747 C  CA  A ASP   A 162 ? 0.1415 0.3046 0.2270 -0.0027 0.0223  0.0306  162 ASP   A CA  
3748 C  CA  B ASP   A 162 ? 0.1526 0.2402 0.2123 -0.0010 0.0127  0.0457  162 ASP   A CA  
3749 C  C   A ASP   A 162 ? 0.1377 0.3019 0.2313 -0.0050 0.0188  0.0231  162 ASP   A C   
3750 C  C   B ASP   A 162 ? 0.1482 0.2371 0.2128 -0.0077 0.0092  0.0450  162 ASP   A C   
3751 O  O   A ASP   A 162 ? 0.1397 0.3010 0.2381 -0.0033 0.0199  0.0100  162 ASP   A O   
3752 O  O   B ASP   A 162 ? 0.1462 0.2373 0.2222 -0.0196 0.0067  0.0448  162 ASP   A O   
3753 C  CB  A ASP   A 162 ? 0.1515 0.3259 0.2381 0.0068  0.0293  0.0269  162 ASP   A CB  
3754 C  CB  B ASP   A 162 ? 0.1682 0.2611 0.2423 0.0034  0.0105  0.0439  162 ASP   A CB  
3755 C  CG  A ASP   A 162 ? 0.1626 0.3443 0.2521 0.0083  0.0434  0.0399  162 ASP   A CG  
3756 C  CG  B ASP   A 162 ? 0.1830 0.2787 0.2689 0.0089  0.0054  0.0543  162 ASP   A CG  
3757 O  OD1 A ASP   A 162 ? 0.1734 0.3496 0.2547 0.0029  0.0464  0.0546  162 ASP   A OD1 
3758 O  OD1 B ASP   A 162 ? 0.1878 0.2830 0.2710 0.0147  0.0076  0.0679  162 ASP   A OD1 
3759 O  OD2 A ASP   A 162 ? 0.1733 0.3502 0.2815 0.0202  0.0498  0.0347  162 ASP   A OD2 
3760 O  OD2 B ASP   A 162 ? 0.1932 0.2875 0.2883 0.0088  0.0056  0.0525  162 ASP   A OD2 
3769 N  N   A LYS   A 163 ? 0.1453 0.3044 0.2288 -0.0007 0.0110  0.0231  163 LYS   A N   
3770 N  N   B LYS   A 163 ? 0.1507 0.2333 0.2080 -0.0040 -0.0017 0.0453  163 LYS   A N   
3771 C  CA  A LYS   A 163 ? 0.1564 0.3083 0.2359 -0.0016 -0.0044 0.0249  163 LYS   A CA  
3772 C  CA  B LYS   A 163 ? 0.1591 0.2311 0.2135 -0.0015 0.0003  0.0404  163 LYS   A CA  
3773 C  C   A LYS   A 163 ? 0.1504 0.2929 0.2278 -0.0051 0.0120  0.0343  163 LYS   A C   
3774 C  C   B LYS   A 163 ? 0.1496 0.2144 0.1988 -0.0046 0.0099  0.0333  163 LYS   A C   
3775 O  O   A LYS   A 163 ? 0.1463 0.2911 0.2354 -0.0060 0.0149  0.0216  163 LYS   A O   
3776 O  O   B LYS   A 163 ? 0.1517 0.2133 0.2113 -0.0022 0.0077  0.0299  163 LYS   A O   
3777 C  CB  A LYS   A 163 ? 0.1913 0.3286 0.2699 0.0083  -0.0188 0.0204  163 LYS   A CB  
3778 C  CB  B LYS   A 163 ? 0.1851 0.2488 0.2533 0.0009  -0.0064 0.0407  163 LYS   A CB  
3779 C  CG  A LYS   A 163 ? 0.2287 0.3472 0.3268 0.0093  -0.0188 0.0169  163 LYS   A CG  
3780 C  CG  B LYS   A 163 ? 0.2126 0.2658 0.3025 -0.0014 -0.0050 0.0412  163 LYS   A CG  
3781 C  CD  A LYS   A 163 ? 0.2607 0.3634 0.3857 0.0112  -0.0116 0.0135  163 LYS   A CD  
3782 C  CD  B LYS   A 163 ? 0.2350 0.2801 0.3496 -0.0035 -0.0046 0.0406  163 LYS   A CD  
3783 C  CE  A LYS   A 163 ? 0.2881 0.3736 0.4313 0.0118  -0.0072 0.0138  163 LYS   A CE  
3784 C  CE  B LYS   A 163 ? 0.2522 0.2911 0.3869 -0.0041 -0.0021 0.0370  163 LYS   A CE  
3785 N  NZ  A LYS   A 163 ? 0.3057 0.3811 0.4574 0.0125  -0.0051 0.0155  163 LYS   A NZ  
3786 N  NZ  B LYS   A 163 ? 0.2591 0.2971 0.4098 -0.0042 -0.0017 0.0325  163 LYS   A NZ  
3813 N  N   A LEU   A 164 ? 0.1375 0.2736 0.2105 -0.0104 0.0146  0.0462  164 LEU   A N   
3814 N  N   B LEU   A 164 ? 0.1357 0.2051 0.1814 -0.0097 0.0108  0.0354  164 LEU   A N   
3815 C  CA  A LEU   A 164 ? 0.1459 0.2629 0.2118 -0.0213 0.0207  0.0507  164 LEU   A CA  
3816 C  CA  B LEU   A 164 ? 0.1343 0.2008 0.1748 -0.0117 0.0192  0.0472  164 LEU   A CA  
3817 C  C   A LEU   A 164 ? 0.1573 0.2662 0.2136 -0.0247 0.0184  0.0530  164 LEU   A C   
3818 C  C   B LEU   A 164 ? 0.1457 0.2050 0.1729 -0.0123 0.0215  0.0498  164 LEU   A C   
3819 O  O   A LEU   A 164 ? 0.1616 0.2587 0.2193 -0.0361 0.0330  0.0509  164 LEU   A O   
3820 O  O   B LEU   A 164 ? 0.1529 0.2017 0.1645 -0.0113 0.0318  0.0473  164 LEU   A O   
3821 C  CB  A LEU   A 164 ? 0.1419 0.2529 0.2166 -0.0232 0.0178  0.0484  164 LEU   A CB  
3822 C  CB  B LEU   A 164 ? 0.1264 0.1971 0.1731 -0.0180 0.0158  0.0585  164 LEU   A CB  
3823 C  CG  A LEU   A 164 ? 0.1476 0.2538 0.2256 -0.0159 0.0211  0.0564  164 LEU   A CG  
3824 C  CG  B LEU   A 164 ? 0.1261 0.1985 0.1849 -0.0229 0.0121  0.0575  164 LEU   A CG  
3825 C  CD1 A LEU   A 164 ? 0.1367 0.2562 0.2246 -0.0133 0.0291  0.0623  164 LEU   A CD1 
3826 C  CD1 B LEU   A 164 ? 0.1176 0.1984 0.1865 -0.0344 0.0070  0.0616  164 LEU   A CD1 
3827 C  CD2 A LEU   A 164 ? 0.1489 0.2559 0.2250 -0.0136 0.0236  0.0517  164 LEU   A CD2 
3828 C  CD2 B LEU   A 164 ? 0.1284 0.2011 0.1881 -0.0136 0.0091  0.0510  164 LEU   A CD2 
3851 N  N   A VAL   A 165 ? 0.1476 0.2766 0.2075 -0.0274 0.0143  0.0623  165 VAL   A N   
3852 N  N   B VAL   A 165 ? 0.1435 0.2112 0.1814 -0.0128 0.0208  0.0511  165 VAL   A N   
3853 C  CA  A VAL   A 165 ? 0.1604 0.2872 0.1942 -0.0288 0.0167  0.0763  165 VAL   A CA  
3854 C  CA  B VAL   A 165 ? 0.1468 0.2221 0.1796 -0.0125 0.0226  0.0533  165 VAL   A CA  
3855 C  C   A VAL   A 165 ? 0.1569 0.2966 0.1883 -0.0287 0.0187  0.0801  165 VAL   A C   
3856 C  C   B VAL   A 165 ? 0.1392 0.2299 0.1852 -0.0109 0.0137  0.0608  165 VAL   A C   
3857 O  O   A VAL   A 165 ? 0.1531 0.3013 0.1825 -0.0323 0.0248  0.0736  165 VAL   A O   
3858 O  O   B VAL   A 165 ? 0.1379 0.2303 0.1788 -0.0149 0.0148  0.0687  165 VAL   A O   
3859 C  CB  A VAL   A 165 ? 0.1783 0.2890 0.2079 -0.0326 0.0223  0.0713  165 VAL   A CB  
3860 C  CB  B VAL   A 165 ? 0.1594 0.2272 0.1879 -0.0094 0.0256  0.0387  165 VAL   A CB  
3861 C  CG1 A VAL   A 165 ? 0.1822 0.2903 0.2083 -0.0388 0.0282  0.0687  165 VAL   A CG1 
3862 C  CG1 B VAL   A 165 ? 0.1634 0.2295 0.1916 -0.0126 0.0269  0.0311  165 VAL   A CG1 
3863 C  CG2 A VAL   A 165 ? 0.1855 0.2888 0.2074 -0.0319 0.0168  0.0790  165 VAL   A CG2 
3864 C  CG2 B VAL   A 165 ? 0.1652 0.2293 0.1877 -0.0051 0.0209  0.0390  165 VAL   A CG2 
3883 N  N   A SER   A 166 ? 0.1488 0.3010 0.2025 -0.0231 0.0187  0.0724  166 SER   A N   
3884 N  N   B SER   A 166 ? 0.1298 0.2332 0.1976 -0.0098 0.0089  0.0603  166 SER   A N   
3885 C  CA  A SER   A 166 ? 0.1537 0.3040 0.2250 -0.0208 0.0155  0.0634  166 SER   A CA  
3886 C  CA  B SER   A 166 ? 0.1309 0.2396 0.2082 -0.0128 0.0019  0.0595  166 SER   A CA  
3887 C  C   A SER   A 166 ? 0.1563 0.3006 0.2259 -0.0161 -0.0009 0.0588  166 SER   A C   
3888 C  C   B SER   A 166 ? 0.1330 0.2419 0.1960 -0.0183 0.0007  0.0668  166 SER   A C   
3889 O  O   A SER   A 166 ? 0.1752 0.3094 0.2445 -0.0232 -0.0020 0.0536  166 SER   A O   
3890 O  O   B SER   A 166 ? 0.1316 0.2414 0.1995 -0.0252 0.0011  0.0695  166 SER   A O   
3891 C  CB  A SER   A 166 ? 0.1634 0.3096 0.2494 -0.0109 0.0088  0.0569  166 SER   A CB  
3892 C  CB  B SER   A 166 ? 0.1374 0.2425 0.2289 -0.0116 -0.0075 0.0524  166 SER   A CB  
3893 O  OG  A SER   A 166 ? 0.1769 0.3157 0.2691 -0.0055 0.0143  0.0570  166 SER   A OG  
3894 O  OG  B SER   A 166 ? 0.1469 0.2431 0.2444 -0.0056 -0.0151 0.0508  166 SER   A OG  
3905 N  N   A SER   A 167 ? 0.1544 0.2872 0.1968 -0.0020 -0.0024 0.0641  167 SER   A N   
3906 N  N   B SER   A 167 ? 0.1426 0.2404 0.1957 -0.0147 0.0094  0.0645  167 SER   A N   
3907 C  CA  A SER   A 167 ? 0.1780 0.2774 0.1960 -0.0033 -0.0010 0.0496  167 SER   A CA  
3908 C  CA  B SER   A 167 ? 0.1584 0.2390 0.1818 -0.0113 0.0203  0.0580  167 SER   A CA  
3909 C  C   A SER   A 167 ? 0.1901 0.2720 0.2025 0.0022  0.0185  0.0573  167 SER   A C   
3910 C  C   B SER   A 167 ? 0.1490 0.2399 0.1752 -0.0042 0.0225  0.0539  167 SER   A C   
3911 O  O   A SER   A 167 ? 0.2070 0.2711 0.2269 0.0123  0.0061  0.0615  167 SER   A O   
3912 O  O   B SER   A 167 ? 0.1597 0.2446 0.1804 -0.0023 0.0156  0.0546  167 SER   A O   
3913 C  CB  A SER   A 167 ? 0.1815 0.2730 0.2040 -0.0064 0.0055  0.0413  167 SER   A CB  
3914 C  CB  B SER   A 167 ? 0.1749 0.2399 0.1811 -0.0109 0.0323  0.0437  167 SER   A CB  
3915 O  OG  A SER   A 167 ? 0.1848 0.2718 0.2152 -0.0095 0.0162  0.0351  167 SER   A OG  
3916 O  OG  B SER   A 167 ? 0.1864 0.2426 0.1812 -0.0075 0.0435  0.0279  167 SER   A OG  
3927 N  N   A PHE   A 168 ? 0.1804 0.2702 0.1930 0.0042  0.0261  0.0556  168 PHE   A N   
3928 N  N   B PHE   A 168 ? 0.1335 0.2371 0.1614 0.0024  0.0253  0.0467  168 PHE   A N   
3929 C  CA  A PHE   A 168 ? 0.1857 0.2742 0.2118 0.0023  0.0289  0.0562  168 PHE   A CA  
3930 C  CA  B PHE   A 168 ? 0.1306 0.2388 0.1564 0.0010  0.0310  0.0393  168 PHE   A CA  
3931 C  C   A PHE   A 168 ? 0.2017 0.2839 0.2512 -0.0025 0.0483  0.0450  168 PHE   A C   
3932 C  C   B PHE   A 168 ? 0.1370 0.2432 0.1715 -0.0091 0.0412  0.0285  168 PHE   A C   
3933 O  O   A PHE   A 168 ? 0.2106 0.2891 0.2907 -0.0076 0.0544  0.0533  168 PHE   A O   
3934 O  O   B PHE   A 168 ? 0.1357 0.2424 0.1654 -0.0121 0.0428  0.0226  168 PHE   A O   
3935 C  CB  A PHE   A 168 ? 0.1782 0.2718 0.1981 -0.0025 0.0144  0.0550  168 PHE   A CB  
3936 C  CB  B PHE   A 168 ? 0.1403 0.2395 0.1634 -0.0027 0.0220  0.0415  168 PHE   A CB  
3937 C  CG  A PHE   A 168 ? 0.1724 0.2709 0.1767 -0.0073 0.0046  0.0551  168 PHE   A CG  
3938 C  CG  B PHE   A 168 ? 0.1465 0.2376 0.1717 -0.0075 0.0199  0.0480  168 PHE   A CG  
3939 C  CD1 A PHE   A 168 ? 0.1710 0.2763 0.1770 -0.0159 0.0018  0.0578  168 PHE   A CD1 
3940 C  CD1 B PHE   A 168 ? 0.1504 0.2395 0.1835 -0.0111 0.0208  0.0545  168 PHE   A CD1 
3941 C  CD2 A PHE   A 168 ? 0.1698 0.2683 0.1718 -0.0107 0.0188  0.0517  168 PHE   A CD2 
3942 C  CD2 B PHE   A 168 ? 0.1507 0.2335 0.1737 -0.0074 0.0141  0.0514  168 PHE   A CD2 
3943 C  CE1 A PHE   A 168 ? 0.1644 0.2739 0.1675 -0.0189 -0.0017 0.0564  168 PHE   A CE1 
3944 C  CE1 B PHE   A 168 ? 0.1502 0.2414 0.1874 -0.0128 0.0216  0.0558  168 PHE   A CE1 
3945 C  CE2 A PHE   A 168 ? 0.1742 0.2653 0.1730 -0.0132 0.0194  0.0549  168 PHE   A CE2 
3946 C  CE2 B PHE   A 168 ? 0.1582 0.2362 0.1813 -0.0053 0.0050  0.0554  168 PHE   A CE2 
3947 C  CZ  A PHE   A 168 ? 0.1622 0.2679 0.1669 -0.0170 0.0050  0.0535  168 PHE   A CZ  
3948 C  CZ  B PHE   A 168 ? 0.1574 0.2395 0.1857 -0.0086 0.0160  0.0542  168 PHE   A CZ  
3967 N  N   A LEU   A 169 ? 0.2278 0.2877 0.2808 -0.0094 0.0495  0.0232  169 LEU   A N   
3968 N  N   B LEU   A 169 ? 0.1479 0.2510 0.2089 -0.0088 0.0385  0.0270  169 LEU   A N   
3969 C  CA  A LEU   A 169 ? 0.2572 0.2982 0.3254 -0.0104 0.0413  0.0108  169 LEU   A CA  
3970 C  CA  B LEU   A 169 ? 0.1662 0.2618 0.2472 -0.0105 0.0316  0.0180  169 LEU   A CA  
3971 C  C   A LEU   A 169 ? 0.2497 0.2940 0.3323 -0.0120 0.0549  0.0238  169 LEU   A C   
3972 C  C   B LEU   A 169 ? 0.1800 0.2692 0.2696 -0.0028 0.0292  0.0087  169 LEU   A C   
3973 O  O   A LEU   A 169 ? 0.2546 0.2963 0.3439 -0.0076 0.0449  0.0211  169 LEU   A O   
3974 O  O   B LEU   A 169 ? 0.1783 0.2725 0.2772 -0.0004 0.0249  -0.0004 169 LEU   A O   
3975 C  CB  A LEU   A 169 ? 0.2831 0.3114 0.3437 -0.0080 0.0323  -0.0079 169 LEU   A CB  
3976 C  CB  B LEU   A 169 ? 0.1725 0.2657 0.2517 -0.0171 0.0260  0.0189  169 LEU   A CB  
3977 C  CG  A LEU   A 169 ? 0.3067 0.3228 0.3603 -0.0079 0.0259  -0.0291 169 LEU   A CG  
3978 C  CG  B LEU   A 169 ? 0.1784 0.2691 0.2634 -0.0210 0.0164  0.0198  169 LEU   A CG  
3979 C  CD1 A LEU   A 169 ? 0.3177 0.3256 0.3689 -0.0088 0.0207  -0.0347 169 LEU   A CD1 
3980 C  CD1 B LEU   A 169 ? 0.1807 0.2723 0.2788 -0.0255 0.0103  0.0199  169 LEU   A CD1 
3981 C  CD2 A LEU   A 169 ? 0.3122 0.3278 0.3623 -0.0090 0.0271  -0.0373 169 LEU   A CD2 
3982 C  CD2 B LEU   A 169 ? 0.1850 0.2705 0.2640 -0.0249 0.0170  0.0179  169 LEU   A CD2 
3983 O  OXT A LEU   A 169 ? 0.2347 0.2945 0.3199 -0.0173 0.0774  0.0260  169 LEU   A OXT 
3984 O  OXT B LEU   A 169 ? 0.1962 0.2744 0.2831 -0.0048 0.0240  0.0108  169 LEU   A OXT 
4007 N  N   A SER   B 1   ? 0.3557 0.3479 0.3391 -0.1079 -0.0692 0.0322  1   SER   B N   
4008 N  N   B SER   B 1   ? 0.3338 0.3398 0.3445 -0.0701 -0.0415 0.0243  1   SER   B N   
4009 C  CA  A SER   B 1   ? 0.3470 0.3512 0.3441 -0.1129 -0.0771 0.0292  1   SER   B CA  
4010 C  CA  B SER   B 1   ? 0.3283 0.3414 0.3446 -0.0724 -0.0434 0.0251  1   SER   B CA  
4011 C  C   A SER   B 1   ? 0.3237 0.3544 0.3348 -0.1141 -0.0833 0.0483  1   SER   B C   
4012 C  C   B SER   B 1   ? 0.3140 0.3419 0.3374 -0.0737 -0.0504 0.0411  1   SER   B C   
4013 O  O   A SER   B 1   ? 0.3327 0.3590 0.3187 -0.1066 -0.0791 0.0480  1   SER   B O   
4014 O  O   B SER   B 1   ? 0.3187 0.3442 0.3300 -0.0709 -0.0473 0.0371  1   SER   B O   
4015 C  CB  A SER   B 1   ? 0.3582 0.3493 0.3576 -0.1136 -0.0714 0.0117  1   SER   B CB  
4016 C  CB  B SER   B 1   ? 0.3342 0.3410 0.3519 -0.0722 -0.0369 0.0123  1   SER   B CB  
4017 O  OG  A SER   B 1   ? 0.3718 0.3571 0.3973 -0.1103 -0.0610 0.0039  1   SER   B OG  
4018 O  OG  B SER   B 1   ? 0.3404 0.3448 0.3708 -0.0720 -0.0323 0.0054  1   SER   B OG  
4033 N  N   A MET   B 2   ? 0.2999 0.3515 0.3332 -0.1163 -0.0826 0.0843  2   MET   B N   
4034 N  N   B MET   B 2   ? 0.2971 0.3388 0.3299 -0.0765 -0.0577 0.0702  2   MET   B N   
4035 C  CA  A MET   B 2   ? 0.2869 0.3525 0.3497 -0.0992 -0.0827 0.1065  2   MET   B CA  
4036 C  CA  B MET   B 2   ? 0.2825 0.3360 0.3289 -0.0726 -0.0663 0.0960  2   MET   B CA  
4037 C  C   A MET   B 2   ? 0.2585 0.3337 0.3179 -0.0789 -0.0958 0.1323  2   MET   B C   
4038 C  C   B MET   B 2   ? 0.2584 0.3206 0.3107 -0.0735 -0.0784 0.1208  2   MET   B C   
4039 O  O   A MET   B 2   ? 0.2557 0.3458 0.3163 -0.0649 -0.1130 0.1340  2   MET   B O   
4040 O  O   B MET   B 2   ? 0.2582 0.3252 0.3117 -0.0694 -0.0830 0.1177  2   MET   B O   
4041 C  CB  A MET   B 2   ? 0.3125 0.3804 0.4252 -0.0851 -0.0617 0.0845  2   MET   B CB  
4042 C  CB  B MET   B 2   ? 0.2951 0.3516 0.3577 -0.0610 -0.0597 0.0916  2   MET   B CB  
4043 C  CG  A MET   B 2   ? 0.3377 0.4053 0.4954 -0.0674 -0.0424 0.0705  2   MET   B CG  
4044 C  CG  B MET   B 2   ? 0.3058 0.3648 0.3774 -0.0477 -0.0556 0.0957  2   MET   B CG  
4045 S  SD  A MET   B 2   ? 0.3630 0.4286 0.5634 -0.0505 -0.0305 0.0593  2   MET   B SD  
4046 S  SD  B MET   B 2   ? 0.3162 0.3782 0.3907 -0.0347 -0.0575 0.1021  2   MET   B SD  
4047 C  CE  A MET   B 2   ? 0.3649 0.4321 0.5669 -0.0504 -0.0207 0.0588  2   MET   B CE  
4048 C  CE  B MET   B 2   ? 0.3171 0.3801 0.4020 -0.0350 -0.0508 0.0939  2   MET   B CE  
4067 N  N   . VAL   B 3   ? 0.2336 0.2981 0.2952 -0.0833 -0.0832 0.1464  3   VAL   B N   
4068 C  CA  . VAL   B 3   ? 0.2166 0.2606 0.2973 -0.0728 -0.0789 0.1314  3   VAL   B CA  
4069 C  C   . VAL   B 3   ? 0.1962 0.2469 0.2610 -0.0632 -0.0751 0.1127  3   VAL   B C   
4070 O  O   . VAL   B 3   ? 0.1923 0.2647 0.2713 -0.0674 -0.0728 0.1217  3   VAL   B O   
4071 C  CB  . VAL   B 3   ? 0.2306 0.2515 0.3565 -0.0712 -0.0662 0.1191  3   VAL   B CB  
4072 C  CG1 . VAL   B 3   ? 0.2364 0.2454 0.3844 -0.0714 -0.0631 0.1104  3   VAL   B CG1 
4073 C  CG2 . VAL   B 3   ? 0.2321 0.2587 0.3768 -0.0669 -0.0562 0.1253  3   VAL   B CG2 
4084 N  N   . ASN   B 4   ? 0.1886 0.2147 0.2206 -0.0595 -0.0621 0.0897  4   ASN   B N   
4085 C  CA  . ASN   B 4   ? 0.1877 0.2123 0.1926 -0.0585 -0.0519 0.0522  4   ASN   B CA  
4086 C  C   . ASN   B 4   ? 0.1908 0.2251 0.1834 -0.0568 -0.0456 0.0391  4   ASN   B C   
4087 O  O   . ASN   B 4   ? 0.1919 0.2304 0.2030 -0.0525 -0.0336 0.0169  4   ASN   B O   
4088 C  CB  . ASN   B 4   ? 0.1862 0.2098 0.1734 -0.0536 -0.0681 0.0346  4   ASN   B CB  
4089 C  CG  . ASN   B 4   ? 0.1865 0.1930 0.1670 -0.0504 -0.0583 0.0333  4   ASN   B CG  
4090 O  OD1 . ASN   B 4   ? 0.1906 0.1757 0.1685 -0.0482 -0.0469 0.0286  4   ASN   B OD1 
4091 N  ND2 . ASN   B 4   ? 0.2035 0.1996 0.1820 -0.0295 -0.0373 0.0319  4   ASN   B ND2 
4098 N  N   . SER   B 5   ? 0.2077 0.2453 0.1874 -0.0561 -0.0361 0.0293  5   SER   B N   
4099 C  CA  . SER   B 5   ? 0.2319 0.2802 0.2119 -0.0526 -0.0163 0.0278  5   SER   B CA  
4100 C  C   . SER   B 5   ? 0.2558 0.2844 0.2475 -0.0744 0.0114  0.0357  5   SER   B C   
4101 O  O   . SER   B 5   ? 0.2750 0.2771 0.3127 -0.0691 0.0460  0.0317  5   SER   B O   
4102 C  CB  . SER   B 5   ? 0.2427 0.3041 0.2351 -0.0409 -0.0001 0.0384  5   SER   B CB  
4103 O  OG  . SER   B 5   ? 0.2662 0.3289 0.2896 -0.0282 0.0044  0.0470  5   SER   B OG  
4109 N  N   . PHE   B 6   ? 0.2761 0.3072 0.2264 -0.0823 0.0239  0.0451  6   PHE   B N   
4110 C  CA  . PHE   B 6   ? 0.2870 0.3147 0.1886 -0.1016 0.0321  0.0269  6   PHE   B CA  
4111 C  C   . PHE   B 6   ? 0.3390 0.3512 0.2368 -0.1077 0.0567  -0.0036 6   PHE   B C   
4112 O  O   . PHE   B 6   ? 0.3534 0.3791 0.2718 -0.0998 0.0440  -0.0175 6   PHE   B O   
4113 C  CB  . PHE   B 6   ? 0.2582 0.2917 0.1713 -0.0920 0.0050  0.0209  6   PHE   B CB  
4114 C  CG  . PHE   B 6   ? 0.2240 0.2582 0.1635 -0.0848 -0.0078 0.0219  6   PHE   B CG  
4115 C  CD1 . PHE   B 6   ? 0.2257 0.2288 0.1478 -0.0775 -0.0147 0.0206  6   PHE   B CD1 
4116 C  CD2 . PHE   B 6   ? 0.2004 0.2541 0.1750 -0.0697 -0.0103 0.0455  6   PHE   B CD2 
4117 C  CE1 . PHE   B 6   ? 0.2192 0.2047 0.1663 -0.0658 -0.0192 0.0209  6   PHE   B CE1 
4118 C  CE2 . PHE   B 6   ? 0.2036 0.2378 0.2128 -0.0560 -0.0034 0.0384  6   PHE   B CE2 
4119 C  CZ  . PHE   B 6   ? 0.2099 0.2133 0.1985 -0.0568 -0.0086 0.0280  6   PHE   B CZ  
4129 N  N   . SER   B 7   ? 0.3763 0.3444 0.2580 -0.1296 0.0864  -0.0284 7   SER   B N   
4130 C  CA  . SER   B 7   ? 0.4133 0.3651 0.3187 -0.1316 0.1116  -0.0354 7   SER   B CA  
4131 C  C   . SER   B 7   ? 0.4123 0.3399 0.3035 -0.1339 0.1292  -0.0494 7   SER   B C   
4132 O  O   . SER   B 7   ? 0.4216 0.3373 0.3262 -0.1364 0.1250  -0.0519 7   SER   B O   
4133 C  CB  . SER   B 7   ? 0.4361 0.3946 0.3903 -0.1311 0.1251  -0.0271 7   SER   B CB  
4134 O  OG  . SER   B 7   ? 0.4408 0.3963 0.4457 -0.1304 0.1321  -0.0206 7   SER   B OG  
4140 N  N   . GLY   B 8   ? 0.4072 0.3210 0.3007 -0.1205 0.1363  -0.0634 8   GLY   B N   
4141 C  CA  . GLY   B 8   ? 0.3965 0.3014 0.2970 -0.1099 0.1367  -0.0703 8   GLY   B CA  
4142 C  C   . GLY   B 8   ? 0.3786 0.2743 0.2888 -0.1034 0.1382  -0.0639 8   GLY   B C   
4143 O  O   . GLY   B 8   ? 0.3873 0.2772 0.3192 -0.0975 0.1407  -0.0726 8   GLY   B O   
4147 N  N   . TYR   B 9   ? 0.3605 0.2508 0.2651 -0.0912 0.1097  -0.0720 9   TYR   B N   
4148 C  CA  . TYR   B 9   ? 0.3406 0.2221 0.2383 -0.0790 0.0822  -0.0579 9   TYR   B CA  
4149 C  C   . TYR   B 9   ? 0.3341 0.2186 0.2286 -0.0724 0.0497  -0.0471 9   TYR   B C   
4150 O  O   . TYR   B 9   ? 0.3435 0.2351 0.2657 -0.0734 0.0485  -0.0372 9   TYR   B O   
4151 C  CB  . TYR   B 9   ? 0.3312 0.1994 0.2432 -0.0742 0.0778  -0.0536 9   TYR   B CB  
4152 C  CG  . TYR   B 9   ? 0.3203 0.1805 0.2396 -0.0734 0.0759  -0.0554 9   TYR   B CG  
4153 C  CD1 . TYR   B 9   ? 0.3204 0.1817 0.2501 -0.0850 0.0777  -0.0468 9   TYR   B CD1 
4154 C  CD2 . TYR   B 9   ? 0.3073 0.1750 0.2346 -0.0694 0.0712  -0.0527 9   TYR   B CD2 
4155 C  CE1 . TYR   B 9   ? 0.3156 0.1900 0.2534 -0.0874 0.0815  -0.0576 9   TYR   B CE1 
4156 C  CE2 . TYR   B 9   ? 0.3058 0.1760 0.2405 -0.0698 0.0703  -0.0545 9   TYR   B CE2 
4157 C  CZ  . TYR   B 9   ? 0.3069 0.1907 0.2485 -0.0821 0.0753  -0.0639 9   TYR   B CZ  
4158 O  OH  . TYR   B 9   ? 0.3022 0.2036 0.2670 -0.0917 0.0690  -0.0774 9   TYR   B OH  
4168 N  N   . LEU   B 10  ? 0.3169 0.1937 0.2064 -0.0683 0.0277  -0.0450 10  LEU   B N   
4169 C  CA  . LEU   B 10  ? 0.3108 0.1908 0.2045 -0.0784 -0.0148 -0.0397 10  LEU   B CA  
4170 C  C   . LEU   B 10  ? 0.2908 0.1926 0.2049 -0.0755 -0.0296 -0.0259 10  LEU   B C   
4171 O  O   . LEU   B 10  ? 0.2728 0.1914 0.2046 -0.0634 -0.0205 -0.0166 10  LEU   B O   
4172 C  CB  . LEU   B 10  ? 0.3249 0.1879 0.2239 -0.0806 -0.0347 -0.0185 10  LEU   B CB  
4173 C  CG  . LEU   B 10  ? 0.3427 0.1943 0.2602 -0.0726 -0.0540 -0.0026 10  LEU   B CG  
4174 C  CD1 . LEU   B 10  ? 0.3545 0.2035 0.2793 -0.0660 -0.0512 0.0005  10  LEU   B CD1 
4175 C  CD2 . LEU   B 10  ? 0.3508 0.2002 0.2907 -0.0724 -0.0502 0.0121  10  LEU   B CD2 
4187 N  N   . LYS   B 11  ? 0.3030 0.2154 0.2098 -0.0702 -0.0399 -0.0182 11  LYS   B N   
4188 C  CA  . LYS   B 11  ? 0.3143 0.2435 0.2507 -0.0575 -0.0489 -0.0233 11  LYS   B CA  
4189 C  C   . LYS   B 11  ? 0.2932 0.2253 0.2548 -0.0761 -0.0497 -0.0348 11  LYS   B C   
4190 O  O   . LYS   B 11  ? 0.3059 0.2426 0.2848 -0.0905 -0.0506 -0.0645 11  LYS   B O   
4191 C  CB  . LYS   B 11  ? 0.3448 0.2915 0.3193 -0.0336 -0.0501 -0.0258 11  LYS   B CB  
4192 C  CG  . LYS   B 11  ? 0.3712 0.3228 0.3902 -0.0199 -0.0500 -0.0305 11  LYS   B CG  
4193 C  CD  . LYS   B 11  ? 0.3914 0.3444 0.4522 -0.0115 -0.0482 -0.0367 11  LYS   B CD  
4194 C  CE  . LYS   B 11  ? 0.4051 0.3599 0.4994 -0.0090 -0.0460 -0.0391 11  LYS   B CE  
4195 N  NZ  . LYS   B 11  ? 0.4131 0.3697 0.5251 -0.0082 -0.0464 -0.0388 11  LYS   B NZ  
4209 N  N   . LEU   B 12  ? 0.2588 0.2005 0.2509 -0.0694 -0.0471 -0.0331 12  LEU   B N   
4210 C  CA  . LEU   B 12  ? 0.2402 0.1822 0.2641 -0.0584 -0.0338 -0.0245 12  LEU   B CA  
4211 C  C   . LEU   B 12  ? 0.2259 0.1825 0.2692 -0.0574 -0.0454 -0.0214 12  LEU   B C   
4212 O  O   . LEU   B 12  ? 0.2207 0.1821 0.2846 -0.0641 -0.0614 -0.0160 12  LEU   B O   
4213 C  CB  . LEU   B 12  ? 0.2386 0.1613 0.2615 -0.0477 -0.0252 -0.0279 12  LEU   B CB  
4214 C  CG  . LEU   B 12  ? 0.2411 0.1598 0.2593 -0.0451 -0.0168 -0.0231 12  LEU   B CG  
4215 C  CD1 . LEU   B 12  ? 0.2529 0.1608 0.2538 -0.0317 -0.0190 -0.0002 12  LEU   B CD1 
4216 C  CD2 . LEU   B 12  ? 0.2469 0.1627 0.2674 -0.0438 -0.0125 -0.0341 12  LEU   B CD2 
4228 N  N   . THR   B 13  ? 0.2169 0.1865 0.2707 -0.0605 -0.0507 -0.0374 13  THR   B N   
4229 C  CA  . THR   B 13  ? 0.2146 0.1950 0.2606 -0.0660 -0.0585 -0.0151 13  THR   B CA  
4230 C  C   . THR   B 13  ? 0.2561 0.2119 0.2669 -0.0715 -0.0733 -0.0076 13  THR   B C   
4231 O  O   . THR   B 13  ? 0.2782 0.2160 0.2838 -0.0681 -0.0467 -0.0110 13  THR   B O   
4232 C  CB  . THR   B 13  ? 0.1969 0.1955 0.2611 -0.0585 -0.0530 -0.0131 13  THR   B CB  
4233 O  OG1 . THR   B 13  ? 0.1856 0.1912 0.2686 -0.0490 -0.0386 -0.0177 13  THR   B OG1 
4234 C  CG2 . THR   B 13  ? 0.2028 0.2035 0.2599 -0.0546 -0.0463 -0.0004 13  THR   B CG2 
4242 N  N   . ASP   B 14  ? 0.2719 0.2255 0.2730 -0.0772 -0.1105 0.0063  14  ASP   B N   
4243 C  CA  . ASP   B 14  ? 0.2830 0.2420 0.3042 -0.0743 -0.1159 0.0271  14  ASP   B CA  
4244 C  C   . ASP   B 14  ? 0.2697 0.2214 0.2734 -0.0779 -0.0984 0.0211  14  ASP   B C   
4245 O  O   . ASP   B 14  ? 0.3037 0.2417 0.2848 -0.0816 -0.0932 0.0252  14  ASP   B O   
4246 C  CB  . ASP   B 14  ? 0.3048 0.2823 0.3857 -0.0632 -0.1273 0.0368  14  ASP   B CB  
4247 C  CG  . ASP   B 14  ? 0.3323 0.3199 0.4663 -0.0519 -0.1209 0.0217  14  ASP   B CG  
4248 O  OD1 . ASP   B 14  ? 0.3484 0.3327 0.4901 -0.0517 -0.1169 0.0045  14  ASP   B OD1 
4249 O  OD2 . ASP   B 14  ? 0.3364 0.3362 0.5013 -0.0501 -0.1179 0.0216  14  ASP   B OD2 
4254 N  N   . ASN   B 15  ? 0.2259 0.1897 0.2500 -0.0563 -0.0873 0.0182  15  ASN   B N   
4255 C  CA  . ASN   B 15  ? 0.1885 0.1667 0.2393 -0.0368 -0.0627 0.0064  15  ASN   B CA  
4256 C  C   . ASN   B 15  ? 0.1711 0.1527 0.2233 -0.0252 -0.0485 -0.0017 15  ASN   B C   
4257 O  O   . ASN   B 15  ? 0.1703 0.1490 0.2273 -0.0278 -0.0458 -0.0113 15  ASN   B O   
4258 C  CB  . ASN   B 15  ? 0.1834 0.1620 0.2538 -0.0201 -0.0608 0.0146  15  ASN   B CB  
4259 C  CG  . ASN   B 15  ? 0.1646 0.1601 0.2664 -0.0276 -0.0362 0.0169  15  ASN   B CG  
4260 O  OD1 . ASN   B 15  ? 0.1691 0.1874 0.2958 -0.0472 -0.0407 0.0207  15  ASN   B OD1 
4261 N  ND2 . ASN   B 15  ? 0.1632 0.1407 0.2525 -0.0168 -0.0161 -0.0041 15  ASN   B ND2 
4268 N  N   . VAL   B 16  ? 0.1771 0.1457 0.2244 -0.0327 -0.0500 0.0004  16  VAL   B N   
4269 C  CA  . VAL   B 16  ? 0.1769 0.1499 0.2091 -0.0317 -0.0373 -0.0164 16  VAL   B CA  
4270 C  C   . VAL   B 16  ? 0.1745 0.1613 0.2071 -0.0403 -0.0351 -0.0086 16  VAL   B C   
4271 O  O   . VAL   B 16  ? 0.1775 0.1726 0.2289 -0.0385 -0.0322 -0.0194 16  VAL   B O   
4272 C  CB  . VAL   B 16  ? 0.1824 0.1479 0.2154 -0.0173 -0.0343 -0.0187 16  VAL   B CB  
4273 C  CG1 . VAL   B 16  ? 0.1899 0.1432 0.2158 -0.0058 -0.0235 -0.0099 16  VAL   B CG1 
4274 C  CG2 . VAL   B 16  ? 0.1834 0.1534 0.2389 -0.0076 -0.0285 -0.0134 16  VAL   B CG2 
4284 N  N   . TYR   B 17  ? 0.1841 0.1710 0.2060 -0.0356 -0.0324 -0.0182 17  TYR   B N   
4285 C  CA  . TYR   B 17  ? 0.1894 0.1828 0.1944 -0.0457 -0.0348 0.0028  17  TYR   B CA  
4286 C  C   . TYR   B 17  ? 0.1821 0.1547 0.1902 -0.0466 -0.0179 -0.0085 17  TYR   B C   
4287 O  O   . TYR   B 17  ? 0.1779 0.1620 0.2021 -0.0370 -0.0238 -0.0362 17  TYR   B O   
4288 C  CB  . TYR   B 17  ? 0.2214 0.2244 0.2245 -0.0305 -0.0416 0.0363  17  TYR   B CB  
4289 C  CG  . TYR   B 17  ? 0.2508 0.2686 0.2701 -0.0234 -0.0512 0.0439  17  TYR   B CG  
4290 C  CD1 . TYR   B 17  ? 0.2680 0.2853 0.2887 -0.0200 -0.0606 0.0526  17  TYR   B CD1 
4291 C  CD2 . TYR   B 17  ? 0.2694 0.2929 0.2944 -0.0134 -0.0570 0.0433  17  TYR   B CD2 
4292 C  CE1 . TYR   B 17  ? 0.2854 0.3081 0.3078 -0.0119 -0.0702 0.0470  17  TYR   B CE1 
4293 C  CE2 . TYR   B 17  ? 0.2847 0.3116 0.3143 -0.0022 -0.0733 0.0452  17  TYR   B CE2 
4294 C  CZ  . TYR   B 17  ? 0.2959 0.3200 0.3196 -0.0025 -0.0795 0.0456  17  TYR   B CZ  
4295 O  OH  . TYR   B 17  ? 0.3117 0.3337 0.3335 0.0053  -0.0862 0.0419  17  TYR   B OH  
4305 N  N   . ILE   B 18  ? 0.1957 0.1562 0.1901 -0.0363 -0.0044 -0.0160 18  ILE   B N   
4306 C  CA  . ILE   B 18  ? 0.1989 0.1500 0.1913 -0.0414 -0.0053 -0.0217 18  ILE   B CA  
4307 C  C   . ILE   B 18  ? 0.2115 0.1553 0.1886 -0.0495 -0.0043 -0.0331 18  ILE   B C   
4308 O  O   . ILE   B 18  ? 0.2311 0.1716 0.2077 -0.0475 0.0015  -0.0366 18  ILE   B O   
4309 C  CB  . ILE   B 18  ? 0.2031 0.1545 0.2053 -0.0420 -0.0086 -0.0160 18  ILE   B CB  
4310 C  CG1 . ILE   B 18  ? 0.2036 0.1537 0.2098 -0.0408 -0.0074 -0.0074 18  ILE   B CG1 
4311 C  CG2 . ILE   B 18  ? 0.2064 0.1579 0.2116 -0.0454 -0.0079 -0.0206 18  ILE   B CG2 
4312 C  CD1 . ILE   B 18  ? 0.2097 0.1833 0.2276 -0.0365 -0.0168 0.0127  18  ILE   B CD1 
4324 N  N   . LYS   B 19  ? 0.2134 0.1566 0.2011 -0.0284 0.0322  -0.0420 19  LYS   B N   
4325 C  CA  . LYS   B 19  ? 0.2192 0.1632 0.2235 -0.0292 0.0310  -0.0457 19  LYS   B CA  
4326 C  C   . LYS   B 19  ? 0.2019 0.1573 0.2403 -0.0285 0.0370  -0.0523 19  LYS   B C   
4327 O  O   . LYS   B 19  ? 0.1945 0.1598 0.2200 -0.0196 0.0294  -0.0469 19  LYS   B O   
4328 C  CB  . LYS   B 19  ? 0.2423 0.1819 0.2298 -0.0375 0.0423  -0.0338 19  LYS   B CB  
4329 C  CG  . LYS   B 19  ? 0.2683 0.2024 0.2556 -0.0457 0.0518  -0.0327 19  LYS   B CG  
4330 C  CD  . LYS   B 19  ? 0.2939 0.2305 0.2641 -0.0557 0.0625  -0.0290 19  LYS   B CD  
4331 C  CE  . LYS   B 19  ? 0.3193 0.2581 0.2796 -0.0561 0.0624  -0.0359 19  LYS   B CE  
4332 N  NZ  . LYS   B 19  ? 0.3362 0.2746 0.2855 -0.0609 0.0677  -0.0322 19  LYS   B NZ  
4346 N  N   . ASN   B 20  ? 0.1968 0.1679 0.2740 -0.0241 0.0444  -0.0635 20  ASN   B N   
4347 C  CA  . ASN   B 20  ? 0.1985 0.1844 0.2974 -0.0180 0.0440  -0.0802 20  ASN   B CA  
4348 C  C   . ASN   B 20  ? 0.1978 0.2037 0.2935 -0.0227 0.0552  -0.0897 20  ASN   B C   
4349 O  O   . ASN   B 20  ? 0.2109 0.2343 0.3117 -0.0373 0.0555  -0.0900 20  ASN   B O   
4350 C  CB  . ASN   B 20  ? 0.2250 0.1898 0.3272 0.0077  0.0326  -0.0839 20  ASN   B CB  
4351 C  CG  . ASN   B 20  ? 0.2486 0.1986 0.3438 0.0336  0.0310  -0.0940 20  ASN   B CG  
4352 O  OD1 . ASN   B 20  ? 0.2777 0.2267 0.3712 0.0479  0.0301  -0.0937 20  ASN   B OD1 
4353 N  ND2 . ASN   B 20  ? 0.2391 0.2013 0.3391 0.0347  0.0207  -0.0921 20  ASN   B ND2 
4360 N  N   . ALA   B 21  ? 0.1980 0.1900 0.2928 -0.0296 0.0567  -0.0723 21  ALA   B N   
4361 C  CA  . ALA   B 21  ? 0.2099 0.1956 0.3056 -0.0365 0.0446  -0.0523 21  ALA   B CA  
4362 C  C   . ALA   B 21  ? 0.2081 0.1691 0.2896 -0.0267 0.0430  -0.0364 21  ALA   B C   
4363 O  O   . ALA   B 21  ? 0.2097 0.1555 0.2862 -0.0333 0.0382  -0.0341 21  ALA   B O   
4364 C  CB  . ALA   B 21  ? 0.2248 0.2193 0.3175 -0.0486 0.0441  -0.0375 21  ALA   B CB  
4370 N  N   . ASP   B 22  ? 0.1996 0.1595 0.2703 -0.0232 0.0388  -0.0291 22  ASP   B N   
4371 C  CA  . ASP   B 22  ? 0.1924 0.1546 0.2560 -0.0109 0.0287  -0.0237 22  ASP   B CA  
4372 C  C   . ASP   B 22  ? 0.1817 0.1535 0.2093 -0.0190 0.0203  -0.0118 22  ASP   B C   
4373 O  O   . ASP   B 22  ? 0.1797 0.1568 0.2100 -0.0168 0.0184  -0.0124 22  ASP   B O   
4374 C  CB  . ASP   B 22  ? 0.1990 0.1591 0.2942 -0.0069 0.0299  -0.0139 22  ASP   B CB  
4375 C  CG  . ASP   B 22  ? 0.1999 0.1755 0.3376 -0.0011 0.0093  -0.0086 22  ASP   B CG  
4376 O  OD1 . ASP   B 22  ? 0.2087 0.1697 0.3318 -0.0018 -0.0078 -0.0096 22  ASP   B OD1 
4377 O  OD2 . ASP   B 22  ? 0.2104 0.2037 0.3924 0.0115  -0.0108 -0.0157 22  ASP   B OD2 
4382 N  N   . ILE   B 23  ? 0.1819 0.1469 0.1872 -0.0140 0.0088  0.0148  23  ILE   B N   
4383 C  CA  . ILE   B 23  ? 0.1712 0.1427 0.1722 -0.0119 0.0022  0.0034  23  ILE   B CA  
4384 C  C   . ILE   B 23  ? 0.1632 0.1462 0.1696 -0.0070 -0.0068 0.0015  23  ILE   B C   
4385 O  O   . ILE   B 23  ? 0.1562 0.1439 0.1611 -0.0144 -0.0088 0.0053  23  ILE   B O   
4386 C  CB  . ILE   B 23  ? 0.1720 0.1512 0.1930 -0.0205 -0.0037 0.0152  23  ILE   B CB  
4387 C  CG1 . ILE   B 23  ? 0.1723 0.1622 0.1972 -0.0116 0.0009  0.0342  23  ILE   B CG1 
4388 C  CG2 . ILE   B 23  ? 0.1771 0.1739 0.2015 -0.0185 0.0027  0.0106  23  ILE   B CG2 
4389 C  CD1 . ILE   B 23  ? 0.1785 0.1744 0.2066 -0.0088 0.0087  0.0264  23  ILE   B CD1 
4401 N  N   . VAL   B 24  ? 0.1654 0.1434 0.1806 -0.0108 -0.0067 0.0021  24  VAL   B N   
4402 C  CA  . VAL   B 24  ? 0.1600 0.1517 0.2078 -0.0071 -0.0175 0.0008  24  VAL   B CA  
4403 C  C   . VAL   B 24  ? 0.1552 0.1522 0.2073 -0.0157 -0.0091 0.0000  24  VAL   B C   
4404 O  O   . VAL   B 24  ? 0.1570 0.1591 0.2180 -0.0164 -0.0026 0.0085  24  VAL   B O   
4405 C  CB  . VAL   B 24  ? 0.1696 0.1659 0.2194 -0.0002 -0.0156 0.0007  24  VAL   B CB  
4406 C  CG1 . VAL   B 24  ? 0.1704 0.1698 0.2406 -0.0128 -0.0213 0.0015  24  VAL   B CG1 
4407 C  CG2 . VAL   B 24  ? 0.1782 0.1952 0.2212 0.0062  -0.0248 -0.0082 24  VAL   B CG2 
4417 N  N   . GLU   B 25  ? 0.1780 0.1631 0.2046 -0.0140 -0.0011 0.0025  25  GLU   B N   
4418 C  CA  . GLU   B 25  ? 0.1925 0.1919 0.2226 -0.0029 0.0127  -0.0063 25  GLU   B CA  
4419 C  C   . GLU   B 25  ? 0.1858 0.1859 0.1988 -0.0127 0.0081  -0.0034 25  GLU   B C   
4420 O  O   . GLU   B 25  ? 0.1900 0.1961 0.2130 -0.0125 0.0168  0.0029  25  GLU   B O   
4421 C  CB  . GLU   B 25  ? 0.2329 0.2410 0.2862 0.0197  0.0286  -0.0102 25  GLU   B CB  
4422 C  CG  . GLU   B 25  ? 0.2698 0.3007 0.3911 0.0270  0.0235  -0.0116 25  GLU   B CG  
4423 C  CD  . GLU   B 25  ? 0.3169 0.3543 0.4778 0.0240  0.0169  -0.0103 25  GLU   B CD  
4424 O  OE1 . GLU   B 25  ? 0.3372 0.3734 0.5101 0.0283  0.0193  -0.0067 25  GLU   B OE1 
4425 O  OE2 . GLU   B 25  ? 0.3329 0.3707 0.5066 0.0228  0.0107  -0.0151 25  GLU   B OE2 
4432 N  N   . GLU   B 26  ? 0.1835 0.1760 0.1795 -0.0318 0.0039  -0.0024 26  GLU   B N   
4433 C  CA  . GLU   B 26  ? 0.1824 0.1901 0.1847 -0.0417 -0.0108 -0.0027 26  GLU   B CA  
4434 C  C   . GLU   B 26  ? 0.1672 0.1881 0.1668 -0.0287 0.0061  0.0123  26  GLU   B C   
4435 O  O   . GLU   B 26  ? 0.1885 0.2089 0.1701 -0.0226 -0.0003 0.0205  26  GLU   B O   
4436 C  CB  . GLU   B 26  ? 0.2136 0.2121 0.2034 -0.0455 -0.0077 0.0111  26  GLU   B CB  
4437 C  CG  . GLU   B 26  ? 0.2559 0.2524 0.2659 -0.0502 0.0109  -0.0066 26  GLU   B CG  
4438 C  CD  . GLU   B 26  ? 0.2783 0.2753 0.2794 -0.0699 0.0288  -0.0403 26  GLU   B CD  
4439 O  OE1 . GLU   B 26  ? 0.2963 0.2644 0.2905 -0.0831 0.0673  -0.0437 26  GLU   B OE1 
4440 O  OE2 . GLU   B 26  ? 0.2823 0.3064 0.3141 -0.0606 0.0274  -0.0340 26  GLU   B OE2 
4447 N  N   . ALA   B 27  ? 0.1507 0.1679 0.1729 -0.0222 0.0068  0.0171  27  ALA   B N   
4448 C  CA  . ALA   B 27  ? 0.1514 0.1691 0.1842 -0.0180 -0.0013 0.0341  27  ALA   B CA  
4449 C  C   . ALA   B 27  ? 0.1564 0.1799 0.2101 -0.0184 0.0058  0.0436  27  ALA   B C   
4450 O  O   . ALA   B 27  ? 0.1661 0.1880 0.2174 -0.0037 0.0047  0.0476  27  ALA   B O   
4451 C  CB  . ALA   B 27  ? 0.1655 0.1559 0.1947 -0.0205 -0.0055 0.0296  27  ALA   B CB  
4457 N  N   . LYS   B 28  ? 0.1522 0.1949 0.2443 -0.0243 0.0120  0.0621  28  LYS   B N   
4458 C  CA  . LYS   B 28  ? 0.1664 0.2329 0.2664 -0.0131 0.0430  0.0871  28  LYS   B CA  
4459 C  C   . LYS   B 28  ? 0.1875 0.2485 0.2551 -0.0053 0.0570  0.0775  28  LYS   B C   
4460 O  O   . LYS   B 28  ? 0.2110 0.2548 0.2783 -0.0055 0.0581  0.0765  28  LYS   B O   
4461 C  CB  . LYS   B 28  ? 0.1897 0.2695 0.3152 -0.0026 0.0674  0.1063  28  LYS   B CB  
4462 C  CG  . LYS   B 28  ? 0.2305 0.3201 0.3577 0.0042  0.0736  0.1199  28  LYS   B CG  
4463 C  CD  . LYS   B 28  ? 0.2887 0.3818 0.4189 0.0093  0.0864  0.1149  28  LYS   B CD  
4464 C  CE  . LYS   B 28  ? 0.3298 0.4230 0.4670 0.0145  0.0917  0.1172  28  LYS   B CE  
4465 N  NZ  . LYS   B 28  ? 0.3669 0.4392 0.4906 0.0188  0.0921  0.1213  28  LYS   B NZ  
4479 N  N   . LYS   B 29  ? 0.2069 0.2724 0.2554 0.0126  0.0608  0.0638  29  LYS   B N   
4480 C  CA  . LYS   B 29  ? 0.2519 0.3065 0.2890 0.0133  0.0565  0.0631  29  LYS   B CA  
4481 C  C   . LYS   B 29  ? 0.2468 0.3092 0.2494 0.0101  0.0433  0.0726  29  LYS   B C   
4482 O  O   . LYS   B 29  ? 0.2677 0.3314 0.2611 0.0134  0.0430  0.0753  29  LYS   B O   
4483 C  CB  . LYS   B 29  ? 0.3108 0.3426 0.3797 0.0124  0.0520  0.0522  29  LYS   B CB  
4484 C  CG  . LYS   B 29  ? 0.3612 0.3735 0.4691 0.0100  0.0524  0.0461  29  LYS   B CG  
4485 C  CD  . LYS   B 29  ? 0.4074 0.3980 0.5400 0.0063  0.0559  0.0387  29  LYS   B CD  
4486 C  CE  . LYS   B 29  ? 0.4408 0.4134 0.5881 0.0031  0.0610  0.0346  29  LYS   B CE  
4487 N  NZ  . LYS   B 29  ? 0.4507 0.4189 0.6163 0.0017  0.0632  0.0316  29  LYS   B NZ  
4501 N  N   . VAL   B 30  ? 0.2163 0.2892 0.2273 -0.0001 0.0293  0.0742  30  VAL   B N   
4502 C  CA  . VAL   B 30  ? 0.2037 0.2764 0.2529 -0.0137 -0.0031 0.0765  30  VAL   B CA  
4503 C  C   . VAL   B 30  ? 0.1863 0.2671 0.2389 -0.0138 -0.0017 0.0909  30  VAL   B C   
4504 O  O   . VAL   B 30  ? 0.2009 0.2784 0.2382 -0.0056 -0.0023 0.0989  30  VAL   B O   
4505 C  CB  . VAL   B 30  ? 0.2108 0.2749 0.2943 -0.0287 -0.0272 0.0737  30  VAL   B CB  
4506 C  CG1 . VAL   B 30  ? 0.2181 0.2844 0.2992 -0.0276 -0.0239 0.0655  30  VAL   B CG1 
4507 C  CG2 . VAL   B 30  ? 0.2220 0.2748 0.3138 -0.0390 -0.0354 0.0630  30  VAL   B CG2 
4517 N  N   . LYS   B 31  ? 0.1757 0.2335 0.2727 -0.0273 -0.0065 0.0976  31  LYS   B N   
4518 C  CA  . LYS   B 31  ? 0.1632 0.2239 0.3126 -0.0402 -0.0116 0.0979  31  LYS   B CA  
4519 C  C   . LYS   B 31  ? 0.1571 0.1880 0.2754 -0.0381 -0.0292 0.0809  31  LYS   B C   
4520 O  O   . LYS   B 31  ? 0.1662 0.2013 0.2897 -0.0294 -0.0239 0.0939  31  LYS   B O   
4521 C  CB  . LYS   B 31  ? 0.1784 0.2669 0.3632 -0.0368 0.0165  0.1099  31  LYS   B CB  
4522 C  CG  . LYS   B 31  ? 0.2110 0.3141 0.4039 -0.0384 0.0356  0.0994  31  LYS   B CG  
4523 C  CD  . LYS   B 31  ? 0.2514 0.3595 0.4454 -0.0344 0.0351  0.0882  31  LYS   B CD  
4524 C  CE  . LYS   B 31  ? 0.2761 0.3845 0.4822 -0.0327 0.0288  0.0783  31  LYS   B CE  
4525 N  NZ  . LYS   B 31  ? 0.2835 0.4014 0.4971 -0.0246 0.0189  0.0672  31  LYS   B NZ  
4539 N  N   . PRO   B 32  ? 0.1723 0.1542 0.2182 -0.0352 -0.0471 0.0494  32  PRO   B N   
4540 C  CA  . PRO   B 32  ? 0.1834 0.1519 0.1766 -0.0342 -0.0465 0.0303  32  PRO   B CA  
4541 C  C   . PRO   B 32  ? 0.1923 0.1469 0.1805 -0.0379 -0.0587 0.0351  32  PRO   B C   
4542 O  O   . PRO   B 32  ? 0.2023 0.1487 0.2090 -0.0448 -0.0753 0.0393  32  PRO   B O   
4543 C  CB  . PRO   B 32  ? 0.1968 0.1495 0.1700 -0.0375 -0.0381 0.0215  32  PRO   B CB  
4544 C  CG  . PRO   B 32  ? 0.2081 0.1358 0.1814 -0.0282 -0.0555 0.0183  32  PRO   B CG  
4545 C  CD  . PRO   B 32  ? 0.1963 0.1450 0.2037 -0.0226 -0.0615 0.0258  32  PRO   B CD  
4553 N  N   . THR   B 33  ? 0.1943 0.1353 0.1615 -0.0297 -0.0481 0.0242  33  THR   B N   
4554 C  CA  . THR   B 33  ? 0.2011 0.1468 0.1559 -0.0324 -0.0460 0.0261  33  THR   B CA  
4555 C  C   . THR   B 33  ? 0.2030 0.1350 0.1543 -0.0368 -0.0495 0.0173  33  THR   B C   
4556 O  O   . THR   B 33  ? 0.2287 0.1381 0.1666 -0.0464 -0.0598 0.0194  33  THR   B O   
4557 C  CB  . THR   B 33  ? 0.2073 0.1560 0.1654 -0.0178 -0.0492 0.0302  33  THR   B CB  
4558 O  OG1 . THR   B 33  ? 0.1958 0.1608 0.1685 -0.0270 -0.0509 0.0295  33  THR   B OG1 
4559 C  CG2 . THR   B 33  ? 0.2325 0.1614 0.1819 -0.0119 -0.0454 0.0238  33  THR   B CG2 
4567 N  N   . VAL   B 34  ? 0.1868 0.1284 0.1474 -0.0368 -0.0427 0.0166  34  VAL   B N   
4568 C  CA  . VAL   B 34  ? 0.1738 0.1304 0.1447 -0.0274 -0.0338 0.0071  34  VAL   B CA  
4569 C  C   . VAL   B 34  ? 0.1555 0.1261 0.1334 -0.0317 -0.0211 0.0090  34  VAL   B C   
4570 O  O   . VAL   B 34  ? 0.1714 0.1259 0.1431 -0.0265 -0.0351 0.0065  34  VAL   B O   
4571 C  CB  . VAL   B 34  ? 0.1777 0.1404 0.1753 -0.0103 -0.0319 0.0082  34  VAL   B CB  
4572 C  CG1 . VAL   B 34  ? 0.1767 0.1552 0.1765 -0.0092 -0.0190 -0.0007 34  VAL   B CG1 
4573 C  CG2 . VAL   B 34  ? 0.1812 0.1445 0.2018 -0.0116 -0.0282 0.0127  34  VAL   B CG2 
4583 N  N   . VAL   B 35  ? 0.1456 0.1260 0.1240 -0.0269 -0.0162 0.0050  35  VAL   B N   
4584 C  CA  . VAL   B 35  ? 0.1399 0.1243 0.1166 -0.0241 -0.0151 0.0117  35  VAL   B CA  
4585 C  C   . VAL   B 35  ? 0.1330 0.1199 0.1280 -0.0178 -0.0156 0.0088  35  VAL   B C   
4586 O  O   . VAL   B 35  ? 0.1370 0.1231 0.1338 -0.0244 -0.0052 -0.0040 35  VAL   B O   
4587 C  CB  . VAL   B 35  ? 0.1400 0.1401 0.1285 -0.0240 -0.0038 0.0088  35  VAL   B CB  
4588 C  CG1 . VAL   B 35  ? 0.1344 0.1526 0.1554 -0.0215 0.0019  0.0106  35  VAL   B CG1 
4589 C  CG2 . VAL   B 35  ? 0.1466 0.1395 0.1525 -0.0089 -0.0101 0.0018  35  VAL   B CG2 
4599 N  N   . VAL   B 36  ? 0.1319 0.1196 0.1277 -0.0182 -0.0145 0.0089  36  VAL   B N   
4600 C  CA  . VAL   B 36  ? 0.1292 0.1169 0.1286 -0.0132 -0.0083 0.0071  36  VAL   B CA  
4601 C  C   . VAL   B 36  ? 0.1250 0.1180 0.1178 -0.0106 -0.0061 0.0027  36  VAL   B C   
4602 O  O   . VAL   B 36  ? 0.1320 0.1305 0.1399 -0.0110 -0.0056 0.0011  36  VAL   B O   
4603 C  CB  . VAL   B 36  ? 0.1301 0.1276 0.1313 -0.0170 -0.0082 0.0031  36  VAL   B CB  
4604 C  CG1 . VAL   B 36  ? 0.1311 0.1332 0.1415 -0.0182 -0.0042 0.0037  36  VAL   B CG1 
4605 C  CG2 . VAL   B 36  ? 0.1385 0.1299 0.1379 -0.0123 -0.0202 0.0112  36  VAL   B CG2 
4615 N  N   . ASN   B 37  ? 0.1315 0.1209 0.1181 -0.0019 -0.0054 0.0018  37  ASN   B N   
4616 C  CA  . ASN   B 37  ? 0.1323 0.1239 0.1259 -0.0019 -0.0125 0.0074  37  ASN   B CA  
4617 C  C   . ASN   B 37  ? 0.1312 0.1279 0.1314 0.0018  -0.0099 0.0049  37  ASN   B C   
4618 O  O   . ASN   B 37  ? 0.1408 0.1352 0.1394 -0.0023 -0.0024 0.0100  37  ASN   B O   
4619 C  CB  . ASN   B 37  ? 0.1328 0.1300 0.1251 -0.0058 -0.0147 0.0031  37  ASN   B CB  
4620 C  CG  . ASN   B 37  ? 0.1336 0.1308 0.1367 0.0004  -0.0145 0.0028  37  ASN   B CG  
4621 O  OD1 . ASN   B 37  ? 0.1445 0.1335 0.1483 0.0093  -0.0166 0.0041  37  ASN   B OD1 
4622 N  ND2 . ASN   B 37  ? 0.1422 0.1284 0.1365 -0.0015 -0.0213 0.0077  37  ASN   B ND2 
4629 N  N   . ALA   B 38  ? 0.1410 0.1264 0.1313 0.0059  0.0016  0.0071  38  ALA   B N   
4630 C  CA  . ALA   B 38  ? 0.1516 0.1287 0.1315 -0.0011 -0.0012 0.0115  38  ALA   B CA  
4631 C  C   . ALA   B 38  ? 0.1452 0.1259 0.1299 0.0012  0.0038  0.0126  38  ALA   B C   
4632 O  O   . ALA   B 38  ? 0.1569 0.1374 0.1407 0.0058  -0.0037 0.0060  38  ALA   B O   
4633 C  CB  . ALA   B 38  ? 0.1713 0.1373 0.1493 -0.0111 0.0040  0.0107  38  ALA   B CB  
4639 N  N   . ALA   B 39  ? 0.1464 0.1292 0.1265 0.0098  -0.0056 0.0046  39  ALA   B N   
4640 C  CA  . ALA   B 39  ? 0.1533 0.1325 0.1187 0.0051  -0.0156 0.0031  39  ALA   B CA  
4641 C  C   . ALA   B 39  ? 0.1617 0.1353 0.1047 0.0091  -0.0052 0.0066  39  ALA   B C   
4642 O  O   . ALA   B 39  ? 0.1624 0.1453 0.1414 -0.0030 -0.0075 0.0108  39  ALA   B O   
4643 C  CB  . ALA   B 39  ? 0.1544 0.1360 0.1448 -0.0024 -0.0077 0.0027  39  ALA   B CB  
4649 N  N   . ASN   B 40  ? 0.1607 0.1570 0.1124 -0.0034 -0.0015 -0.0078 40  ASN   B N   
4650 C  CA  . ASN   B 40  ? 0.1674 0.1632 0.1325 -0.0008 -0.0042 -0.0060 40  ASN   B CA  
4651 C  C   . ASN   B 40  ? 0.1715 0.1620 0.1172 0.0059  -0.0012 0.0031  40  ASN   B C   
4652 O  O   . ASN   B 40  ? 0.1668 0.1526 0.1295 0.0082  -0.0075 0.0027  40  ASN   B O   
4653 C  CB  . ASN   B 40  ? 0.1795 0.1633 0.1469 0.0111  -0.0102 0.0118  40  ASN   B CB  
4654 C  CG  . ASN   B 40  ? 0.1825 0.1707 0.1823 0.0061  -0.0226 0.0176  40  ASN   B CG  
4655 O  OD1 . ASN   B 40  ? 0.1815 0.1676 0.2606 0.0034  -0.0338 0.0168  40  ASN   B OD1 
4656 N  ND2 . ASN   B 40  ? 0.1853 0.1713 0.1861 0.0055  -0.0205 0.0223  40  ASN   B ND2 
4663 N  N   . VAL   B 41  ? 0.1808 0.1657 0.1267 0.0152  0.0009  0.0018  41  VAL   B N   
4664 C  CA  . VAL   B 41  ? 0.1854 0.1783 0.1321 0.0079  0.0033  -0.0074 41  VAL   B CA  
4665 C  C   . VAL   B 41  ? 0.1846 0.1749 0.1215 0.0174  -0.0015 -0.0081 41  VAL   B C   
4666 O  O   . VAL   B 41  ? 0.1828 0.1737 0.1380 0.0138  -0.0109 -0.0106 41  VAL   B O   
4667 C  CB  . VAL   B 41  ? 0.1994 0.1969 0.1631 -0.0019 0.0233  -0.0225 41  VAL   B CB  
4668 C  CG1 . VAL   B 41  ? 0.1975 0.1993 0.1730 -0.0061 0.0320  -0.0297 41  VAL   B CG1 
4669 C  CG2 . VAL   B 41  ? 0.2154 0.2152 0.1661 -0.0148 0.0173  -0.0212 41  VAL   B CG2 
4679 N  N   . TYR   B 42  ? 0.1946 0.1775 0.1270 0.0167  -0.0164 0.0021  42  TYR   B N   
4680 C  CA  . TYR   B 42  ? 0.1972 0.1791 0.1282 0.0170  -0.0256 -0.0085 42  TYR   B CA  
4681 C  C   . TYR   B 42  ? 0.1803 0.1608 0.1394 0.0187  -0.0236 -0.0067 42  TYR   B C   
4682 O  O   . TYR   B 42  ? 0.1816 0.1715 0.1762 0.0123  -0.0282 -0.0127 42  TYR   B O   
4683 C  CB  . TYR   B 42  ? 0.2183 0.2026 0.1509 0.0150  -0.0292 0.0051  42  TYR   B CB  
4684 C  CG  . TYR   B 42  ? 0.2191 0.2171 0.1398 -0.0004 -0.0267 0.0126  42  TYR   B CG  
4685 C  CD1 . TYR   B 42  ? 0.2150 0.2182 0.1124 -0.0085 -0.0124 0.0091  42  TYR   B CD1 
4686 C  CD2 . TYR   B 42  ? 0.2322 0.2262 0.1815 0.0037  -0.0161 0.0171  42  TYR   B CD2 
4687 C  CE1 . TYR   B 42  ? 0.2293 0.2344 0.1197 -0.0030 -0.0094 0.0086  42  TYR   B CE1 
4688 C  CE2 . TYR   B 42  ? 0.2394 0.2388 0.1729 0.0071  0.0055  0.0274  42  TYR   B CE2 
4689 C  CZ  . TYR   B 42  ? 0.2478 0.2506 0.1473 0.0165  0.0053  0.0154  42  TYR   B CZ  
4690 O  OH  . TYR   B 42  ? 0.2761 0.2733 0.1979 0.0325  0.0191  0.0222  42  TYR   B OH  
4700 N  N   . LEU   B 43  ? 0.1704 0.1518 0.1298 0.0109  -0.0145 -0.0103 43  LEU   B N   
4701 C  CA  . LEU   B 43  ? 0.1661 0.1519 0.1288 0.0018  -0.0155 -0.0013 43  LEU   B CA  
4702 C  C   . LEU   B 43  ? 0.1667 0.1531 0.1333 0.0040  -0.0177 -0.0028 43  LEU   B C   
4703 O  O   . LEU   B 43  ? 0.1641 0.1578 0.1619 0.0061  -0.0255 0.0082  43  LEU   B O   
4704 C  CB  . LEU   B 43  ? 0.1637 0.1465 0.1500 -0.0011 -0.0235 -0.0082 43  LEU   B CB  
4705 C  CG  . LEU   B 43  ? 0.1684 0.1430 0.1558 0.0000  -0.0294 -0.0060 43  LEU   B CG  
4706 C  CD1 . LEU   B 43  ? 0.1763 0.1491 0.1810 0.0015  -0.0420 -0.0054 43  LEU   B CD1 
4707 C  CD2 . LEU   B 43  ? 0.1666 0.1466 0.1626 -0.0063 -0.0274 0.0010  43  LEU   B CD2 
4719 N  N   . LYS   B 44  ? 0.1660 0.1525 0.1465 0.0097  -0.0113 -0.0025 44  LYS   B N   
4720 C  CA  . LYS   B 44  ? 0.1789 0.1635 0.1428 0.0109  -0.0156 0.0043  44  LYS   B CA  
4721 C  C   . LYS   B 44  ? 0.1725 0.1560 0.1342 0.0074  -0.0156 0.0034  44  LYS   B C   
4722 O  O   . LYS   B 44  ? 0.1932 0.1554 0.1594 0.0016  -0.0068 0.0049  44  LYS   B O   
4723 C  CB  . LYS   B 44  ? 0.2065 0.1834 0.1527 0.0164  -0.0329 0.0039  44  LYS   B CB  
4724 C  CG  . LYS   B 44  ? 0.2453 0.2119 0.1908 0.0102  -0.0548 0.0096  44  LYS   B CG  
4725 C  CD  . LYS   B 44  ? 0.2757 0.2340 0.2678 0.0015  -0.0619 0.0087  44  LYS   B CD  
4726 C  CE  . LYS   B 44  ? 0.3033 0.2599 0.3244 -0.0030 -0.0696 0.0169  44  LYS   B CE  
4727 N  NZ  . LYS   B 44  ? 0.3153 0.2698 0.3516 -0.0034 -0.0724 0.0313  44  LYS   B NZ  
4741 N  N   . HIS   B 45  ? 0.1601 0.1571 0.1264 0.0031  -0.0157 0.0065  45  HIS   B N   
4742 C  CA  . HIS   B 45  ? 0.1627 0.1554 0.1383 0.0043  -0.0110 -0.0018 45  HIS   B CA  
4743 C  C   . HIS   B 45  ? 0.1836 0.1727 0.1828 0.0170  -0.0189 -0.0018 45  HIS   B C   
4744 O  O   . HIS   B 45  ? 0.1990 0.2026 0.2274 0.0400  0.0043  -0.0006 45  HIS   B O   
4745 C  CB  . HIS   B 45  ? 0.1579 0.1601 0.1403 0.0008  -0.0085 -0.0048 45  HIS   B CB  
4746 C  CG  . HIS   B 45  ? 0.1617 0.1523 0.1415 -0.0073 -0.0104 -0.0020 45  HIS   B CG  
4747 N  ND1 . HIS   B 45  ? 0.1627 0.1434 0.1472 -0.0005 -0.0169 -0.0079 45  HIS   B ND1 
4748 C  CD2 . HIS   B 45  ? 0.1725 0.1501 0.1622 -0.0123 -0.0196 0.0009  45  HIS   B CD2 
4749 C  CE1 . HIS   B 45  ? 0.1742 0.1391 0.1343 -0.0066 -0.0285 -0.0109 45  HIS   B CE1 
4750 N  NE2 . HIS   B 45  ? 0.1775 0.1427 0.1444 -0.0046 -0.0224 -0.0018 45  HIS   B NE2 
4758 N  N   . GLY   B 46  ? 0.1979 0.1687 0.2086 0.0181  -0.0420 0.0073  46  GLY   B N   
4759 C  CA  . GLY   B 46  ? 0.2124 0.1834 0.2457 0.0164  -0.0526 0.0079  46  GLY   B CA  
4760 C  C   . GLY   B 46  ? 0.2078 0.2001 0.2848 0.0247  -0.0486 0.0057  46  GLY   B C   
4761 O  O   . GLY   B 46  ? 0.2178 0.2254 0.3784 0.0230  -0.0197 -0.0250 46  GLY   B O   
4765 N  N   . GLY   B 47  ? 0.2035 0.2068 0.2616 0.0086  -0.0234 -0.0038 47  GLY   B N   
4766 C  CA  . GLY   B 47  ? 0.1943 0.1800 0.2205 0.0021  -0.0236 0.0019  47  GLY   B CA  
4767 C  C   . GLY   B 47  ? 0.1744 0.1600 0.1795 0.0010  -0.0075 0.0078  47  GLY   B C   
4768 O  O   . GLY   B 47  ? 0.1889 0.1462 0.1891 0.0028  -0.0099 0.0115  47  GLY   B O   
4772 N  N   . GLY   B 48  ? 0.1556 0.1503 0.1869 0.0013  -0.0158 0.0170  48  GLY   B N   
4773 C  CA  . GLY   B 48  ? 0.1555 0.1440 0.1818 -0.0030 -0.0112 0.0077  48  GLY   B CA  
4774 C  C   . GLY   B 48  ? 0.1510 0.1395 0.1717 -0.0018 -0.0010 0.0043  48  GLY   B C   
4775 O  O   . GLY   B 48  ? 0.1469 0.1448 0.2044 0.0024  -0.0109 0.0058  48  GLY   B O   
4779 N  N   . VAL   B 49  ? 0.1538 0.1460 0.1628 0.0122  -0.0010 0.0072  49  VAL   B N   
4780 C  CA  . VAL   B 49  ? 0.1528 0.1546 0.1564 0.0153  -0.0150 -0.0069 49  VAL   B CA  
4781 C  C   . VAL   B 49  ? 0.1450 0.1442 0.1377 0.0117  -0.0085 0.0040  49  VAL   B C   
4782 O  O   . VAL   B 49  ? 0.1531 0.1454 0.1562 0.0035  0.0003  0.0066  49  VAL   B O   
4783 C  CB  . VAL   B 49  ? 0.1551 0.1726 0.1727 0.0037  -0.0236 -0.0048 49  VAL   B CB  
4784 C  CG1 . VAL   B 49  ? 0.1517 0.1756 0.1708 0.0062  -0.0261 0.0041  49  VAL   B CG1 
4785 C  CG2 . VAL   B 49  ? 0.1683 0.1873 0.1902 -0.0033 -0.0393 -0.0048 49  VAL   B CG2 
4795 N  N   . ALA   B 50  ? 0.1409 0.1378 0.1418 0.0029  -0.0016 0.0037  50  ALA   B N   
4796 C  CA  . ALA   B 50  ? 0.1412 0.1315 0.1454 0.0047  -0.0052 0.0063  50  ALA   B CA  
4797 C  C   . ALA   B 50  ? 0.1485 0.1390 0.1412 0.0036  -0.0022 0.0011  50  ALA   B C   
4798 O  O   . ALA   B 50  ? 0.1488 0.1390 0.1375 0.0044  -0.0034 -0.0017 50  ALA   B O   
4799 C  CB  . ALA   B 50  ? 0.1466 0.1342 0.1458 0.0023  -0.0072 0.0049  50  ALA   B CB  
4805 N  N   . GLY   B 51  ? 0.1470 0.1510 0.1531 0.0130  -0.0142 0.0115  51  GLY   B N   
4806 C  CA  . GLY   B 51  ? 0.1478 0.1573 0.1722 0.0183  -0.0177 0.0095  51  GLY   B CA  
4807 C  C   . GLY   B 51  ? 0.1478 0.1473 0.1724 0.0140  -0.0118 0.0061  51  GLY   B C   
4808 O  O   . GLY   B 51  ? 0.1474 0.1595 0.1932 0.0086  -0.0092 0.0000  51  GLY   B O   
4812 N  N   . ALA   B 52  ? 0.1457 0.1438 0.1695 0.0143  -0.0087 0.0074  52  ALA   B N   
4813 C  CA  . ALA   B 52  ? 0.1491 0.1519 0.1687 0.0186  0.0001  -0.0047 52  ALA   B CA  
4814 C  C   . ALA   B 52  ? 0.1428 0.1516 0.1554 0.0102  -0.0025 -0.0029 52  ALA   B C   
4815 O  O   . ALA   B 52  ? 0.1437 0.1586 0.1767 0.0069  0.0021  0.0017  52  ALA   B O   
4816 C  CB  . ALA   B 52  ? 0.1646 0.1543 0.1816 0.0054  0.0072  -0.0054 52  ALA   B CB  
4822 N  N   . LEU   B 53  ? 0.1375 0.1479 0.1493 0.0163  -0.0031 0.0030  53  LEU   B N   
4823 C  CA  . LEU   B 53  ? 0.1395 0.1550 0.1491 0.0083  -0.0082 0.0042  53  LEU   B CA  
4824 C  C   . LEU   B 53  ? 0.1452 0.1463 0.1457 0.0107  0.0014  0.0045  53  LEU   B C   
4825 O  O   . LEU   B 53  ? 0.1518 0.1532 0.1630 -0.0021 0.0018  0.0122  53  LEU   B O   
4826 C  CB  . LEU   B 53  ? 0.1400 0.1616 0.1543 0.0076  -0.0012 0.0145  53  LEU   B CB  
4827 C  CG  . LEU   B 53  ? 0.1375 0.1725 0.1652 0.0039  0.0025  0.0220  53  LEU   B CG  
4828 C  CD1 . LEU   B 53  ? 0.1452 0.1868 0.2030 0.0115  -0.0016 0.0108  53  LEU   B CD1 
4829 C  CD2 . LEU   B 53  ? 0.1513 0.2022 0.1880 -0.0103 -0.0065 -0.0054 53  LEU   B CD2 
4841 N  N   . ASN   B 54  ? 0.1461 0.1416 0.1467 0.0043  -0.0046 0.0024  54  ASN   B N   
4842 C  CA  . ASN   B 54  ? 0.1468 0.1524 0.1545 0.0025  -0.0060 0.0010  54  ASN   B CA  
4843 C  C   . ASN   B 54  ? 0.1402 0.1536 0.1710 0.0013  0.0034  0.0016  54  ASN   B C   
4844 O  O   . ASN   B 54  ? 0.1402 0.1578 0.1816 -0.0030 0.0045  -0.0035 54  ASN   B O   
4845 C  CB  . ASN   B 54  ? 0.1505 0.1671 0.1613 0.0023  -0.0038 0.0043  54  ASN   B CB  
4846 C  CG  . ASN   B 54  ? 0.1511 0.1718 0.1665 0.0042  -0.0107 0.0000  54  ASN   B CG  
4847 O  OD1 . ASN   B 54  ? 0.1444 0.1714 0.1809 0.0017  -0.0123 -0.0158 54  ASN   B OD1 
4848 N  ND2 . ASN   B 54  ? 0.1659 0.1893 0.1892 -0.0016 -0.0307 0.0092  54  ASN   B ND2 
4855 N  N   . LYS   B 55  ? 0.1414 0.1590 0.1948 0.0108  -0.0010 0.0009  55  LYS   B N   
4856 C  CA  . LYS   B 55  ? 0.1450 0.1703 0.2153 0.0119  -0.0063 0.0049  55  LYS   B CA  
4857 C  C   . LYS   B 55  ? 0.1435 0.1667 0.2053 0.0108  0.0020  -0.0033 55  LYS   B C   
4858 O  O   . LYS   B 55  ? 0.1403 0.1820 0.2128 0.0123  0.0035  -0.0028 55  LYS   B O   
4859 C  CB  . LYS   B 55  ? 0.1571 0.1831 0.2486 0.0221  0.0041  0.0135  55  LYS   B CB  
4860 C  CG  . LYS   B 55  ? 0.1988 0.2104 0.3234 0.0291  0.0203  0.0250  55  LYS   B CG  
4861 C  CD  . LYS   B 55  ? 0.2369 0.2296 0.3931 0.0376  0.0306  0.0388  55  LYS   B CD  
4862 C  CE  . LYS   B 55  ? 0.2613 0.2506 0.4528 0.0370  0.0466  0.0434  55  LYS   B CE  
4863 N  NZ  . LYS   B 55  ? 0.2658 0.2649 0.4809 0.0367  0.0347  0.0528  55  LYS   B NZ  
4877 N  N   . ALA   B 56  ? 0.1461 0.1714 0.1862 0.0080  0.0032  -0.0098 56  ALA   B N   
4878 C  CA  . ALA   B 56  ? 0.1582 0.1896 0.1833 0.0021  0.0043  -0.0080 56  ALA   B CA  
4879 C  C   . ALA   B 56  ? 0.1576 0.1896 0.1800 0.0054  0.0101  -0.0059 56  ALA   B C   
4880 O  O   . ALA   B 56  ? 0.1689 0.2027 0.1936 0.0046  0.0273  0.0006  56  ALA   B O   
4881 C  CB  . ALA   B 56  ? 0.1693 0.2100 0.1817 -0.0115 0.0026  -0.0107 56  ALA   B CB  
4887 N  N   . THR   B 57  ? 0.1521 0.1797 0.1856 0.0005  0.0153  -0.0004 57  THR   B N   
4888 C  CA  . THR   B 57  ? 0.1563 0.1752 0.1766 -0.0055 0.0209  0.0034  57  THR   B CA  
4889 C  C   . THR   B 57  ? 0.1570 0.1849 0.2053 -0.0018 0.0231  0.0025  57  THR   B C   
4890 O  O   . THR   B 57  ? 0.1667 0.1856 0.2040 -0.0198 0.0190  -0.0034 57  THR   B O   
4891 C  CB  . THR   B 57  ? 0.1658 0.1591 0.1594 -0.0067 0.0155  0.0079  57  THR   B CB  
4892 O  OG1 . THR   B 57  ? 0.1610 0.1529 0.1776 -0.0039 0.0122  0.0032  57  THR   B OG1 
4893 C  CG2 . THR   B 57  ? 0.1593 0.1644 0.1653 -0.0074 0.0143  0.0090  57  THR   B CG2 
4901 N  N   . ASN   B 58  ? 0.1400 0.2053 0.2309 -0.0107 0.0117  -0.0140 58  ASN   B N   
4902 C  CA  . ASN   B 58  ? 0.1690 0.2545 0.2714 -0.0256 0.0328  -0.0063 58  ASN   B CA  
4903 C  C   . ASN   B 58  ? 0.1484 0.2271 0.2239 -0.0176 0.0018  -0.0038 58  ASN   B C   
4904 O  O   . ASN   B 58  ? 0.1561 0.2343 0.2337 -0.0214 0.0011  -0.0128 58  ASN   B O   
4905 C  CB  . ASN   B 58  ? 0.2725 0.3405 0.3942 -0.0377 0.0644  0.0077  58  ASN   B CB  
4906 C  CG  . ASN   B 58  ? 0.3857 0.4186 0.5361 -0.0394 0.0757  0.0269  58  ASN   B CG  
4907 O  OD1 . ASN   B 58  ? 0.4065 0.4393 0.5879 -0.0394 0.0780  0.0326  58  ASN   B OD1 
4908 N  ND2 . ASN   B 58  ? 0.4925 0.4925 0.5859 -0.0411 0.0812  0.0330  58  ASN   B ND2 
4915 N  N   . ASN   B 59  ? 0.1498 0.2107 0.2050 -0.0127 -0.0039 0.0029  59  ASN   B N   
4916 C  CA  . ASN   B 59  ? 0.1478 0.2061 0.1956 -0.0124 -0.0159 0.0102  59  ASN   B CA  
4917 C  C   . ASN   B 59  ? 0.1469 0.1953 0.1882 -0.0155 -0.0136 -0.0048 59  ASN   B C   
4918 O  O   . ASN   B 59  ? 0.1470 0.1964 0.1866 -0.0110 -0.0154 -0.0061 59  ASN   B O   
4919 C  CB  . ASN   B 59  ? 0.1597 0.2238 0.2066 -0.0031 -0.0259 0.0109  59  ASN   B CB  
4920 C  CG  . ASN   B 59  ? 0.1724 0.2363 0.2152 -0.0027 -0.0340 0.0120  59  ASN   B CG  
4921 O  OD1 . ASN   B 59  ? 0.1764 0.2402 0.2191 -0.0007 -0.0243 0.0275  59  ASN   B OD1 
4922 N  ND2 . ASN   B 59  ? 0.1793 0.2465 0.2241 -0.0066 -0.0349 0.0009  59  ASN   B ND2 
4929 N  N   . ALA   B 60  ? 0.1474 0.1816 0.1887 -0.0172 -0.0015 -0.0056 60  ALA   B N   
4930 C  CA  . ALA   B 60  ? 0.1567 0.1723 0.1848 -0.0175 -0.0041 0.0031  60  ALA   B CA  
4931 C  C   . ALA   B 60  ? 0.1594 0.1597 0.1664 -0.0142 -0.0043 0.0038  60  ALA   B C   
4932 O  O   . ALA   B 60  ? 0.1606 0.1605 0.1814 -0.0176 0.0002  -0.0046 60  ALA   B O   
4933 C  CB  . ALA   B 60  ? 0.1688 0.1699 0.2143 -0.0148 -0.0036 0.0067  60  ALA   B CB  
4939 N  N   . MET   B 61  ? 0.1481 0.1524 0.1573 -0.0121 -0.0025 0.0038  61  MET   B N   
4940 C  CA  . MET   B 61  ? 0.1429 0.1493 0.1572 -0.0082 -0.0098 0.0041  61  MET   B CA  
4941 C  C   . MET   B 61  ? 0.1502 0.1475 0.1572 -0.0133 -0.0147 0.0067  61  MET   B C   
4942 O  O   . MET   B 61  ? 0.1543 0.1458 0.1532 -0.0059 -0.0079 -0.0112 61  MET   B O   
4943 C  CB  . MET   B 61  ? 0.1397 0.1504 0.1516 0.0004  -0.0108 -0.0047 61  MET   B CB  
4944 C  CG  . MET   B 61  ? 0.1399 0.1504 0.1439 -0.0010 -0.0075 0.0010  61  MET   B CG  
4945 S  SD  . MET   B 61  ? 0.1431 0.1497 0.1743 -0.0034 -0.0069 -0.0100 61  MET   B SD  
4946 C  CE  . MET   B 61  ? 0.1525 0.1718 0.1887 0.0006  -0.0045 -0.0221 61  MET   B CE  
4956 N  N   . GLN   B 62  ? 0.1486 0.1570 0.1529 -0.0052 -0.0221 0.0028  62  GLN   B N   
4957 C  CA  . GLN   B 62  ? 0.1518 0.1593 0.1519 -0.0017 -0.0198 -0.0006 62  GLN   B CA  
4958 C  C   . GLN   B 62  ? 0.1488 0.1618 0.1575 -0.0048 -0.0227 -0.0076 62  GLN   B C   
4959 O  O   . GLN   B 62  ? 0.1649 0.1662 0.1617 -0.0049 -0.0281 -0.0140 62  GLN   B O   
4960 C  CB  . GLN   B 62  ? 0.1575 0.1652 0.1648 0.0021  -0.0145 0.0014  62  GLN   B CB  
4961 C  CG  . GLN   B 62  ? 0.1599 0.1670 0.1618 0.0008  -0.0250 -0.0089 62  GLN   B CG  
4962 C  CD  . GLN   B 62  ? 0.1578 0.1625 0.1482 0.0047  -0.0238 0.0052  62  GLN   B CD  
4963 O  OE1 . GLN   B 62  ? 0.1633 0.1565 0.1667 0.0017  -0.0253 -0.0032 62  GLN   B OE1 
4964 N  NE2 . GLN   B 62  ? 0.1607 0.1721 0.1571 0.0042  -0.0198 -0.0066 62  GLN   B NE2 
4973 N  N   . VAL   B 63  ? 0.1501 0.1655 0.1769 -0.0090 -0.0288 -0.0110 63  VAL   B N   
4974 C  CA  . VAL   B 63  ? 0.1608 0.1674 0.1991 -0.0145 -0.0313 -0.0090 63  VAL   B CA  
4975 C  C   . VAL   B 63  ? 0.1642 0.1590 0.1785 -0.0194 -0.0318 -0.0163 63  VAL   B C   
4976 O  O   . VAL   B 63  ? 0.1762 0.1597 0.1910 -0.0116 -0.0451 -0.0160 63  VAL   B O   
4977 C  CB  . VAL   B 63  ? 0.1601 0.1811 0.2302 -0.0205 -0.0322 -0.0110 63  VAL   B CB  
4978 C  CG1 . VAL   B 63  ? 0.1695 0.1851 0.2463 -0.0275 -0.0234 -0.0147 63  VAL   B CG1 
4979 C  CG2 . VAL   B 63  ? 0.1546 0.2028 0.2416 -0.0136 -0.0348 -0.0130 63  VAL   B CG2 
4989 N  N   . GLU   B 64  ? 0.1600 0.1522 0.1710 -0.0121 -0.0262 -0.0092 64  GLU   B N   
4990 C  CA  . GLU   B 64  ? 0.1641 0.1436 0.1666 -0.0137 -0.0312 -0.0067 64  GLU   B CA  
4991 C  C   . GLU   B 64  ? 0.1577 0.1445 0.1561 -0.0089 -0.0286 -0.0107 64  GLU   B C   
4992 O  O   . GLU   B 64  ? 0.1700 0.1541 0.1572 -0.0084 -0.0320 -0.0161 64  GLU   B O   
4993 C  CB  . GLU   B 64  ? 0.1640 0.1499 0.1680 -0.0161 -0.0219 -0.0028 64  GLU   B CB  
4994 C  CG  . GLU   B 64  ? 0.1684 0.1545 0.1699 -0.0239 -0.0282 -0.0092 64  GLU   B CG  
4995 C  CD  . GLU   B 64  ? 0.1730 0.1701 0.1729 -0.0298 -0.0262 -0.0020 64  GLU   B CD  
4996 O  OE1 . GLU   B 64  ? 0.1738 0.1858 0.1821 -0.0317 -0.0191 -0.0227 64  GLU   B OE1 
4997 O  OE2 . GLU   B 64  ? 0.1878 0.1789 0.1722 -0.0337 -0.0364 -0.0097 64  GLU   B OE2 
5004 N  N   . SER   B 65  ? 0.1568 0.1424 0.1549 -0.0073 -0.0224 -0.0137 65  SER   B N   
5005 C  CA  . SER   B 65  ? 0.1578 0.1377 0.1593 0.0001  -0.0198 -0.0164 65  SER   B CA  
5006 C  C   . SER   B 65  ? 0.1633 0.1456 0.1610 -0.0007 -0.0289 -0.0197 65  SER   B C   
5007 O  O   . SER   B 65  ? 0.1654 0.1564 0.1510 -0.0023 -0.0270 -0.0235 65  SER   B O   
5008 C  CB  . SER   B 65  ? 0.1588 0.1467 0.1506 -0.0105 -0.0192 -0.0099 65  SER   B CB  
5009 O  OG  . SER   B 65  ? 0.1624 0.1493 0.1561 -0.0088 -0.0181 -0.0212 65  SER   B OG  
5015 N  N   . ASP   B 66  ? 0.1717 0.1507 0.1569 -0.0046 -0.0289 -0.0149 66  ASP   B N   
5016 C  CA  . ASP   B 66  ? 0.1770 0.1582 0.1508 0.0023  -0.0346 -0.0085 66  ASP   B CA  
5017 C  C   . ASP   B 66  ? 0.1814 0.1607 0.1477 -0.0058 -0.0284 -0.0112 66  ASP   B C   
5018 O  O   . ASP   B 66  ? 0.1843 0.1669 0.1594 0.0060  -0.0297 -0.0253 66  ASP   B O   
5019 C  CB  . ASP   B 66  ? 0.1921 0.1692 0.1666 0.0090  -0.0476 -0.0163 66  ASP   B CB  
5020 C  CG  . ASP   B 66  ? 0.2217 0.1851 0.1950 0.0220  -0.0564 -0.0099 66  ASP   B CG  
5021 O  OD1 . ASP   B 66  ? 0.2439 0.1809 0.1985 0.0143  -0.0541 0.0002  66  ASP   B OD1 
5022 O  OD2 . ASP   B 66  ? 0.2373 0.2066 0.2531 0.0401  -0.0563 -0.0119 66  ASP   B OD2 
5027 N  N   . ASP   B 67  ? 0.1766 0.1560 0.1423 -0.0098 -0.0249 -0.0192 67  ASP   B N   
5028 C  CA  . ASP   B 67  ? 0.1892 0.1533 0.1564 -0.0074 -0.0278 -0.0097 67  ASP   B CA  
5029 C  C   . ASP   B 67  ? 0.1827 0.1504 0.1702 -0.0007 -0.0239 -0.0114 67  ASP   B C   
5030 O  O   . ASP   B 67  ? 0.1863 0.1584 0.1867 0.0032  -0.0176 -0.0215 67  ASP   B O   
5031 C  CB  . ASP   B 67  ? 0.2107 0.1628 0.1714 -0.0153 -0.0413 -0.0085 67  ASP   B CB  
5032 C  CG  . ASP   B 67  ? 0.2462 0.1700 0.1837 -0.0131 -0.0679 -0.0136 67  ASP   B CG  
5033 O  OD1 . ASP   B 67  ? 0.2654 0.1733 0.2034 -0.0133 -0.0677 -0.0103 67  ASP   B OD1 
5034 O  OD2 . ASP   B 67  ? 0.2635 0.1793 0.2020 0.0024  -0.0705 -0.0067 67  ASP   B OD2 
5039 N  N   . TYR   B 68  ? 0.1787 0.1542 0.1645 0.0011  -0.0400 -0.0203 68  TYR   B N   
5040 C  CA  . TYR   B 68  ? 0.1736 0.1698 0.1759 0.0084  -0.0404 -0.0292 68  TYR   B CA  
5041 C  C   . TYR   B 68  ? 0.1646 0.1659 0.1650 0.0057  -0.0358 -0.0336 68  TYR   B C   
5042 O  O   . TYR   B 68  ? 0.1740 0.1741 0.1818 0.0080  -0.0293 -0.0436 68  TYR   B O   
5043 C  CB  . TYR   B 68  ? 0.1788 0.1893 0.1818 0.0120  -0.0422 -0.0408 68  TYR   B CB  
5044 C  CG  . TYR   B 68  ? 0.1908 0.2029 0.1909 0.0149  -0.0369 -0.0612 68  TYR   B CG  
5045 C  CD1 . TYR   B 68  ? 0.1947 0.2075 0.2195 -0.0032 -0.0365 -0.0646 68  TYR   B CD1 
5046 C  CD2 . TYR   B 68  ? 0.1968 0.2214 0.2090 0.0214  -0.0490 -0.0473 68  TYR   B CD2 
5047 C  CE1 . TYR   B 68  ? 0.1980 0.2196 0.2400 0.0007  -0.0304 -0.0563 68  TYR   B CE1 
5048 C  CE2 . TYR   B 68  ? 0.1999 0.2227 0.2149 0.0170  -0.0318 -0.0584 68  TYR   B CE2 
5049 C  CZ  . TYR   B 68  ? 0.1919 0.2240 0.2316 0.0051  -0.0312 -0.0583 68  TYR   B CZ  
5050 O  OH  . TYR   B 68  ? 0.1817 0.2431 0.2601 0.0029  -0.0263 -0.0308 68  TYR   B OH  
5060 N  N   . ILE   B 69  ? 0.1628 0.1611 0.1623 0.0066  -0.0332 -0.0355 69  ILE   B N   
5061 C  CA  . ILE   B 69  ? 0.1702 0.1643 0.1732 0.0011  -0.0177 -0.0306 69  ILE   B CA  
5062 C  C   . ILE   B 69  ? 0.1723 0.1590 0.1680 0.0042  -0.0293 -0.0266 69  ILE   B C   
5063 O  O   . ILE   B 69  ? 0.1797 0.1689 0.1679 0.0048  -0.0216 -0.0287 69  ILE   B O   
5064 C  CB  . ILE   B 69  ? 0.1795 0.1671 0.1931 0.0010  0.0003  -0.0288 69  ILE   B CB  
5065 C  CG1 . ILE   B 69  ? 0.1813 0.1719 0.2045 -0.0029 0.0035  -0.0283 69  ILE   B CG1 
5066 C  CG2 . ILE   B 69  ? 0.1924 0.1745 0.2090 0.0016  -0.0001 -0.0277 69  ILE   B CG2 
5067 C  CD1 . ILE   B 69  ? 0.1817 0.1781 0.2133 -0.0148 0.0016  -0.0316 69  ILE   B CD1 
5079 N  N   . ALA   B 70  ? 0.1707 0.1627 0.1767 0.0049  -0.0376 -0.0204 70  ALA   B N   
5080 C  CA  . ALA   B 70  ? 0.1719 0.1619 0.1650 0.0001  -0.0416 -0.0223 70  ALA   B CA  
5081 C  C   . ALA   B 70  ? 0.1781 0.1587 0.1751 -0.0029 -0.0386 -0.0298 70  ALA   B C   
5082 O  O   . ALA   B 70  ? 0.1855 0.1582 0.1763 0.0051  -0.0378 -0.0325 70  ALA   B O   
5083 C  CB  . ALA   B 70  ? 0.1735 0.1750 0.1667 0.0004  -0.0397 -0.0242 70  ALA   B CB  
5089 N  N   . THR   B 71  ? 0.1890 0.1585 0.1836 -0.0006 -0.0489 -0.0270 71  THR   B N   
5090 C  CA  . THR   B 71  ? 0.2025 0.1648 0.2007 0.0081  -0.0656 -0.0292 71  THR   B CA  
5091 C  C   . THR   B 71  ? 0.1979 0.1716 0.2275 0.0282  -0.0628 -0.0454 71  THR   B C   
5092 O  O   . THR   B 71  ? 0.2041 0.1773 0.2654 0.0294  -0.0536 -0.0612 71  THR   B O   
5093 C  CB  . THR   B 71  ? 0.2267 0.1843 0.2262 0.0009  -0.0700 -0.0115 71  THR   B CB  
5094 O  OG1 . THR   B 71  ? 0.2402 0.2083 0.2635 -0.0182 -0.0662 0.0118  71  THR   B OG1 
5095 C  CG2 . THR   B 71  ? 0.2451 0.1825 0.2555 0.0025  -0.0611 0.0026  71  THR   B CG2 
5103 N  N   . ASN   B 72  ? 0.1850 0.1793 0.2159 0.0204  -0.0597 -0.0626 72  ASN   B N   
5104 C  CA  . ASN   B 72  ? 0.1838 0.1908 0.2267 0.0183  -0.0477 -0.0723 72  ASN   B CA  
5105 C  C   . ASN   B 72  ? 0.1815 0.2020 0.2288 0.0054  -0.0258 -0.0726 72  ASN   B C   
5106 O  O   . ASN   B 72  ? 0.1818 0.2158 0.2593 0.0068  -0.0146 -0.0723 72  ASN   B O   
5107 C  CB  . ASN   B 72  ? 0.1914 0.2040 0.2373 0.0122  -0.0653 -0.0614 72  ASN   B CB  
5108 C  CG  . ASN   B 72  ? 0.2059 0.2135 0.2460 0.0307  -0.0601 -0.0424 72  ASN   B CG  
5109 O  OD1 . ASN   B 72  ? 0.2283 0.2344 0.2503 0.0158  -0.0419 -0.0385 72  ASN   B OD1 
5110 N  ND2 . ASN   B 72  ? 0.2211 0.2221 0.2860 0.0453  -0.0475 -0.0113 72  ASN   B ND2 
5117 N  N   . GLY   B 73  ? 0.1871 0.2000 0.2037 0.0006  -0.0290 -0.0671 73  GLY   B N   
5118 C  CA  . GLY   B 73  ? 0.1799 0.2062 0.1858 -0.0009 -0.0189 -0.0530 73  GLY   B CA  
5119 C  C   . GLY   B 73  ? 0.1781 0.2027 0.1468 0.0047  -0.0174 -0.0427 73  GLY   B C   
5120 O  O   . GLY   B 73  ? 0.1713 0.1887 0.1631 0.0082  -0.0169 -0.0255 73  GLY   B O   
5124 N  N   . PRO   B 74  ? 0.1786 0.2137 0.1351 0.0032  -0.0241 -0.0360 74  PRO   B N   
5125 C  CA  . PRO   B 74  ? 0.1720 0.2144 0.1210 0.0069  -0.0197 -0.0217 74  PRO   B CA  
5126 C  C   . PRO   B 74  ? 0.1622 0.1990 0.1348 0.0070  -0.0141 -0.0181 74  PRO   B C   
5127 O  O   . PRO   B 74  ? 0.1613 0.2018 0.1788 0.0096  -0.0089 -0.0328 74  PRO   B O   
5128 C  CB  . PRO   B 74  ? 0.1864 0.2328 0.1288 0.0036  -0.0080 -0.0134 74  PRO   B CB  
5129 C  CG  . PRO   B 74  ? 0.2035 0.2426 0.1607 0.0042  -0.0087 -0.0119 74  PRO   B CG  
5130 C  CD  . PRO   B 74  ? 0.1998 0.2316 0.1548 0.0072  -0.0087 -0.0236 74  PRO   B CD  
5138 N  N   . LEU   B 75  ? 0.1612 0.1858 0.1233 0.0092  -0.0188 -0.0168 75  LEU   B N   
5139 C  CA  . LEU   B 75  ? 0.1663 0.1872 0.1303 0.0032  -0.0188 -0.0054 75  LEU   B CA  
5140 C  C   . LEU   B 75  ? 0.1696 0.1975 0.1254 0.0032  -0.0078 -0.0043 75  LEU   B C   
5141 O  O   . LEU   B 75  ? 0.1856 0.2063 0.1392 0.0004  -0.0054 -0.0014 75  LEU   B O   
5142 C  CB  . LEU   B 75  ? 0.1744 0.1901 0.1173 -0.0101 -0.0195 0.0114  75  LEU   B CB  
5143 C  CG  . LEU   B 75  ? 0.2050 0.2047 0.1401 -0.0305 -0.0117 0.0049  75  LEU   B CG  
5144 C  CD1 . LEU   B 75  ? 0.2365 0.2197 0.1393 -0.0376 0.0120  -0.0050 75  LEU   B CD1 
5145 C  CD2 . LEU   B 75  ? 0.2394 0.2218 0.2050 -0.0234 0.0064  0.0160  75  LEU   B CD2 
5157 N  N   . LYS   B 76  ? 0.1643 0.2197 0.1521 0.0017  0.0002  0.0050  76  LYS   B N   
5158 C  CA  . LYS   B 76  ? 0.1778 0.2274 0.1774 -0.0028 0.0205  0.0063  76  LYS   B CA  
5159 C  C   . LYS   B 76  ? 0.1720 0.2091 0.1553 -0.0009 0.0116  0.0244  76  LYS   B C   
5160 O  O   . LYS   B 76  ? 0.1786 0.1927 0.1567 -0.0019 0.0053  0.0187  76  LYS   B O   
5161 C  CB  . LYS   B 76  ? 0.1946 0.2342 0.2383 -0.0081 0.0379  -0.0250 76  LYS   B CB  
5162 C  CG  . LYS   B 76  ? 0.2046 0.2508 0.2824 -0.0016 0.0234  -0.0319 76  LYS   B CG  
5163 C  CD  . LYS   B 76  ? 0.2066 0.2586 0.3226 0.0064  0.0158  -0.0461 76  LYS   B CD  
5164 C  CE  . LYS   B 76  ? 0.2122 0.2727 0.3674 0.0100  0.0072  -0.0569 76  LYS   B CE  
5165 N  NZ  . LYS   B 76  ? 0.2122 0.2782 0.3852 0.0070  -0.0131 -0.0727 76  LYS   B NZ  
5179 N  N   . VAL   B 77  ? 0.1832 0.2202 0.1656 0.0079  0.0131  0.0326  77  VAL   B N   
5180 C  CA  . VAL   B 77  ? 0.1830 0.2075 0.1775 0.0146  0.0200  0.0539  77  VAL   B CA  
5181 C  C   . VAL   B 77  ? 0.1669 0.1851 0.1737 0.0135  0.0258  0.0424  77  VAL   B C   
5182 O  O   . VAL   B 77  ? 0.1710 0.1821 0.1793 0.0233  0.0293  0.0314  77  VAL   B O   
5183 C  CB  . VAL   B 77  ? 0.1919 0.2192 0.2127 0.0139  0.0305  0.0640  77  VAL   B CB  
5184 C  CG1 . VAL   B 77  ? 0.1967 0.2108 0.2425 0.0032  0.0330  0.0772  77  VAL   B CG1 
5185 C  CG2 . VAL   B 77  ? 0.2040 0.2391 0.2296 0.0133  0.0158  0.0697  77  VAL   B CG2 
5195 N  N   . GLY   B 78  ? 0.1642 0.1703 0.1713 0.0069  0.0195  0.0354  78  GLY   B N   
5196 C  CA  . GLY   B 78  ? 0.1594 0.1678 0.1655 0.0099  0.0230  0.0206  78  GLY   B CA  
5197 C  C   . GLY   B 78  ? 0.1542 0.1596 0.1568 0.0083  0.0159  0.0203  78  GLY   B C   
5198 O  O   . GLY   B 78  ? 0.1569 0.1578 0.1798 0.0155  0.0169  0.0257  78  GLY   B O   
5202 N  N   . GLY   B 79  ? 0.1482 0.1676 0.1510 0.0087  0.0142  0.0158  79  GLY   B N   
5203 C  CA  . GLY   B 79  ? 0.1533 0.1574 0.1466 0.0128  0.0069  0.0133  79  GLY   B CA  
5204 C  C   . GLY   B 79  ? 0.1414 0.1493 0.1500 0.0107  0.0090  0.0058  79  GLY   B C   
5205 O  O   . GLY   B 79  ? 0.1465 0.1471 0.1690 0.0087  0.0147  0.0147  79  GLY   B O   
5209 N  N   . SER   B 80  ? 0.1427 0.1394 0.1596 0.0055  0.0179  0.0085  80  SER   B N   
5210 C  CA  . SER   B 80  ? 0.1394 0.1416 0.1558 0.0012  0.0056  0.0087  80  SER   B CA  
5211 C  C   . SER   B 80  ? 0.1412 0.1361 0.1503 0.0072  -0.0053 0.0059  80  SER   B C   
5212 O  O   . SER   B 80  ? 0.1529 0.1366 0.1826 0.0093  0.0006  0.0022  80  SER   B O   
5213 C  CB  . SER   B 80  ? 0.1447 0.1429 0.1608 -0.0036 0.0030  0.0097  80  SER   B CB  
5214 O  OG  . SER   B 80  ? 0.1492 0.1573 0.1854 -0.0053 -0.0119 0.0134  80  SER   B OG  
5220 N  N   . CYS   B 81  ? 0.1394 0.1249 0.1582 0.0004  -0.0065 -0.0008 81  CYS   B N   
5221 C  CA  . CYS   B 81  ? 0.1480 0.1237 0.1580 0.0008  -0.0114 -0.0006 81  CYS   B CA  
5222 C  C   . CYS   B 81  ? 0.1417 0.1222 0.1371 -0.0035 -0.0132 -0.0031 81  CYS   B C   
5223 O  O   . CYS   B 81  ? 0.1616 0.1265 0.1545 0.0022  -0.0006 -0.0026 81  CYS   B O   
5224 C  CB  . CYS   B 81  ? 0.1608 0.1368 0.1583 -0.0075 -0.0182 -0.0031 81  CYS   B CB  
5225 S  SG  . CYS   B 81  ? 0.1600 0.1547 0.1550 -0.0050 -0.0269 -0.0104 81  CYS   B SG  
5231 N  N   . VAL   B 82  ? 0.1433 0.1204 0.1468 -0.0026 -0.0130 -0.0054 82  VAL   B N   
5232 C  CA  . VAL   B 82  ? 0.1523 0.1283 0.1366 -0.0068 -0.0096 0.0084  82  VAL   B CA  
5233 C  C   . VAL   B 82  ? 0.1570 0.1208 0.1518 -0.0028 -0.0077 -0.0019 82  VAL   B C   
5234 O  O   . VAL   B 82  ? 0.1637 0.1222 0.1920 -0.0048 -0.0082 -0.0151 82  VAL   B O   
5235 C  CB  . VAL   B 82  ? 0.1574 0.1468 0.1601 -0.0028 -0.0132 0.0080  82  VAL   B CB  
5236 C  CG1 . VAL   B 82  ? 0.1765 0.1652 0.1634 0.0035  -0.0132 0.0144  82  VAL   B CG1 
5237 C  CG2 . VAL   B 82  ? 0.1665 0.1601 0.1736 -0.0041 -0.0285 0.0125  82  VAL   B CG2 
5247 N  N   . LEU   B 83  ? 0.1417 0.1224 0.1504 -0.0140 -0.0185 -0.0071 83  LEU   B N   
5248 C  CA  . LEU   B 83  ? 0.1461 0.1298 0.1369 -0.0135 -0.0192 -0.0007 83  LEU   B CA  
5249 C  C   . LEU   B 83  ? 0.1485 0.1272 0.1336 -0.0151 -0.0239 0.0031  83  LEU   B C   
5250 O  O   . LEU   B 83  ? 0.1508 0.1390 0.1282 -0.0205 -0.0134 0.0047  83  LEU   B O   
5251 C  CB  . LEU   B 83  ? 0.1545 0.1396 0.1433 -0.0131 -0.0217 -0.0068 83  LEU   B CB  
5252 C  CG  . LEU   B 83  ? 0.1716 0.1609 0.1459 -0.0197 -0.0110 -0.0089 83  LEU   B CG  
5253 C  CD1 . LEU   B 83  ? 0.1851 0.1676 0.1497 -0.0112 -0.0187 -0.0023 83  LEU   B CD1 
5254 C  CD2 . LEU   B 83  ? 0.1912 0.1675 0.1549 -0.0092 -0.0102 -0.0284 83  LEU   B CD2 
5266 N  N   . SER   B 84  ? 0.1554 0.1342 0.1605 -0.0232 -0.0223 0.0008  84  SER   B N   
5267 C  CA  . SER   B 84  ? 0.1556 0.1585 0.1552 -0.0281 -0.0170 0.0145  84  SER   B CA  
5268 C  C   . SER   B 84  ? 0.1470 0.1752 0.1122 -0.0254 -0.0169 0.0177  84  SER   B C   
5269 O  O   . SER   B 84  ? 0.1527 0.1629 0.1156 -0.0197 -0.0118 0.0015  84  SER   B O   
5270 C  CB  . SER   B 84  ? 0.1707 0.1631 0.1954 -0.0303 0.0079  0.0151  84  SER   B CB  
5271 O  OG  . SER   B 84  ? 0.1692 0.1766 0.2336 -0.0360 -0.0001 0.0293  84  SER   B OG  
5277 N  N   . GLY   B 85  ? 0.1506 0.1942 0.1277 -0.0292 -0.0170 0.0227  85  GLY   B N   
5278 C  CA  . GLY   B 85  ? 0.1489 0.2011 0.1469 -0.0371 -0.0026 -0.0050 85  GLY   B CA  
5279 C  C   . GLY   B 85  ? 0.1497 0.1854 0.1392 -0.0437 -0.0060 0.0050  85  GLY   B C   
5280 O  O   . GLY   B 85  ? 0.1596 0.1832 0.1457 -0.0522 0.0144  -0.0042 85  GLY   B O   
5284 N  N   . HIS   B 86  ? 0.1498 0.1709 0.1555 -0.0342 -0.0200 0.0189  86  HIS   B N   
5285 C  CA  . HIS   B 86  ? 0.1466 0.1685 0.1542 -0.0325 -0.0185 0.0244  86  HIS   B CA  
5286 C  C   . HIS   B 86  ? 0.1494 0.1801 0.1466 -0.0415 -0.0085 0.0347  86  HIS   B C   
5287 O  O   . HIS   B 86  ? 0.1635 0.1920 0.1537 -0.0355 0.0021  0.0292  86  HIS   B O   
5288 C  CB  . HIS   B 86  ? 0.1539 0.1721 0.1663 -0.0260 -0.0223 0.0092  86  HIS   B CB  
5289 C  CG  . HIS   B 86  ? 0.1587 0.1808 0.1550 -0.0177 -0.0241 0.0132  86  HIS   B CG  
5290 N  ND1 . HIS   B 86  ? 0.1661 0.2025 0.1769 -0.0247 -0.0248 -0.0039 86  HIS   B ND1 
5291 C  CD2 . HIS   B 86  ? 0.1659 0.1845 0.1602 -0.0100 -0.0182 0.0110  86  HIS   B CD2 
5292 C  CE1 . HIS   B 86  ? 0.1758 0.1973 0.1673 -0.0137 -0.0045 -0.0181 86  HIS   B CE1 
5293 N  NE2 . HIS   B 86  ? 0.1724 0.1893 0.1543 -0.0002 -0.0081 0.0027  86  HIS   B NE2 
5301 N  N   . ASN   B 87  ? 0.1494 0.1829 0.1542 -0.0384 -0.0013 0.0279  87  ASN   B N   
5302 C  CA  . ASN   B 87  ? 0.1609 0.1994 0.1577 -0.0367 0.0232  0.0172  87  ASN   B CA  
5303 C  C   . ASN   B 87  ? 0.1750 0.1862 0.1520 -0.0350 0.0300  0.0165  87  ASN   B C   
5304 O  O   . ASN   B 87  ? 0.1961 0.1978 0.1848 -0.0270 0.0457  0.0066  87  ASN   B O   
5305 C  CB  . ASN   B 87  ? 0.1618 0.2344 0.1947 -0.0314 0.0269  0.0166  87  ASN   B CB  
5306 C  CG  . ASN   B 87  ? 0.1707 0.2506 0.2013 -0.0021 0.0257  0.0322  87  ASN   B CG  
5307 O  OD1 . ASN   B 87  ? 0.1602 0.2375 0.1853 0.0024  0.0408  0.0468  87  ASN   B OD1 
5308 N  ND2 . ASN   B 87  ? 0.2036 0.2607 0.2351 0.0057  0.0276  0.0289  87  ASN   B ND2 
5315 N  N   . LEU   B 88  ? 0.1649 0.1742 0.1350 -0.0388 0.0119  0.0104  88  LEU   B N   
5316 C  CA  . LEU   B 88  ? 0.1753 0.1714 0.1366 -0.0377 0.0087  -0.0020 88  LEU   B CA  
5317 C  C   . LEU   B 88  ? 0.1729 0.1605 0.1394 -0.0408 0.0045  0.0022  88  LEU   B C   
5318 O  O   . LEU   B 88  ? 0.1993 0.1658 0.1753 -0.0211 -0.0246 -0.0058 88  LEU   B O   
5319 C  CB  . LEU   B 88  ? 0.1899 0.1746 0.1530 -0.0447 -0.0099 0.0126  88  LEU   B CB  
5320 C  CG  . LEU   B 88  ? 0.2261 0.2032 0.1728 -0.0398 -0.0308 0.0302  88  LEU   B CG  
5321 C  CD1 . LEU   B 88  ? 0.2398 0.2310 0.1960 -0.0495 -0.0253 0.0458  88  LEU   B CD1 
5322 C  CD2 . LEU   B 88  ? 0.2601 0.2280 0.2310 -0.0033 -0.0513 0.0102  88  LEU   B CD2 
5334 N  N   . ALA   B 89  ? 0.1594 0.1600 0.1312 -0.0392 0.0151  0.0012  89  ALA   B N   
5335 C  CA  . ALA   B 89  ? 0.1602 0.1535 0.1217 -0.0396 0.0044  0.0085  89  ALA   B CA  
5336 C  C   . ALA   B 89  ? 0.1711 0.1570 0.1223 -0.0406 0.0068  0.0023  89  ALA   B C   
5337 O  O   . ALA   B 89  ? 0.1538 0.1658 0.1593 -0.0416 0.0128  -0.0270 89  ALA   B O   
5338 C  CB  . ALA   B 89  ? 0.1511 0.1527 0.1359 -0.0393 0.0031  0.0108  89  ALA   B CB  
5344 N  N   . LYS   B 90  ? 0.2043 0.1435 0.1366 -0.0470 -0.0071 0.0143  90  LYS   B N   
5345 C  CA  . LYS   B 90  ? 0.2163 0.1411 0.1302 -0.0448 -0.0151 0.0120  90  LYS   B CA  
5346 C  C   . LYS   B 90  ? 0.1982 0.1358 0.1431 -0.0454 -0.0103 0.0022  90  LYS   B C   
5347 O  O   . LYS   B 90  ? 0.2051 0.1518 0.1625 -0.0579 -0.0048 0.0029  90  LYS   B O   
5348 C  CB  . LYS   B 90  ? 0.2325 0.1512 0.1555 -0.0387 -0.0000 0.0236  90  LYS   B CB  
5349 C  CG  . LYS   B 90  ? 0.2339 0.1629 0.1665 -0.0243 0.0271  0.0167  90  LYS   B CG  
5350 C  CD  . LYS   B 90  ? 0.2585 0.1859 0.2171 -0.0146 0.0441  0.0049  90  LYS   B CD  
5351 C  CE  . LYS   B 90  ? 0.2701 0.2024 0.2623 -0.0193 0.0534  -0.0032 90  LYS   B CE  
5352 N  NZ  . LYS   B 90  ? 0.2784 0.1940 0.2555 -0.0289 0.0687  -0.0102 90  LYS   B NZ  
5366 N  N   . HIS   B 91  ? 0.1718 0.1247 0.1274 -0.0323 -0.0158 0.0055  91  HIS   B N   
5367 C  CA  . HIS   B 91  ? 0.1598 0.1278 0.1377 -0.0268 -0.0195 0.0031  91  HIS   B CA  
5368 C  C   . HIS   B 91  ? 0.1462 0.1311 0.1248 -0.0268 -0.0093 0.0031  91  HIS   B C   
5369 O  O   . HIS   B 91  ? 0.1613 0.1338 0.1235 -0.0282 -0.0175 0.0065  91  HIS   B O   
5370 C  CB  . HIS   B 91  ? 0.1765 0.1306 0.1746 -0.0087 -0.0122 0.0164  91  HIS   B CB  
5371 C  CG  . HIS   B 91  ? 0.2157 0.1481 0.2397 -0.0027 0.0165  0.0240  91  HIS   B CG  
5372 N  ND1 . HIS   B 91  ? 0.2447 0.1567 0.2989 -0.0025 0.0271  0.0129  91  HIS   B ND1 
5373 C  CD2 . HIS   B 91  ? 0.2238 0.1772 0.2857 0.0077  0.0034  0.0542  91  HIS   B CD2 
5374 C  CE1 . HIS   B 91  ? 0.2471 0.1734 0.3221 0.0116  0.0278  0.0210  91  HIS   B CE1 
5375 N  NE2 . HIS   B 91  ? 0.2376 0.1851 0.3197 0.0216  0.0181  0.0606  91  HIS   B NE2 
5383 N  N   . CYS   B 92  ? 0.1416 0.1293 0.1282 -0.0269 -0.0152 0.0001  92  CYS   B N   
5384 C  CA  . CYS   B 92  ? 0.1418 0.1255 0.1231 -0.0239 -0.0097 0.0006  92  CYS   B CA  
5385 C  C   . CYS   B 92  ? 0.1389 0.1198 0.1177 -0.0133 -0.0066 0.0047  92  CYS   B C   
5386 O  O   . CYS   B 92  ? 0.1413 0.1267 0.1398 -0.0164 -0.0091 -0.0011 92  CYS   B O   
5387 C  CB  . CYS   B 92  ? 0.1422 0.1386 0.1306 -0.0149 -0.0108 0.0027  92  CYS   B CB  
5388 S  SG  . CYS   B 92  ? 0.1402 0.1350 0.1377 -0.0122 -0.0126 0.0059  92  CYS   B SG  
5394 N  N   . LEU   B 93  ? 0.1303 0.1217 0.1248 -0.0133 -0.0106 -0.0007 93  LEU   B N   
5395 C  CA  . LEU   B 93  ? 0.1320 0.1246 0.1316 -0.0055 -0.0115 0.0044  93  LEU   B CA  
5396 C  C   . LEU   B 93  ? 0.1269 0.1196 0.1193 -0.0040 -0.0067 0.0081  93  LEU   B C   
5397 O  O   . LEU   B 93  ? 0.1332 0.1239 0.1334 -0.0078 -0.0084 0.0038  93  LEU   B O   
5398 C  CB  . LEU   B 93  ? 0.1358 0.1220 0.1465 -0.0027 -0.0099 0.0028  93  LEU   B CB  
5399 C  CG  . LEU   B 93  ? 0.1290 0.1343 0.1637 -0.0064 -0.0073 0.0135  93  LEU   B CG  
5400 C  CD1 . LEU   B 93  ? 0.1337 0.1487 0.1560 0.0018  -0.0018 -0.0000 93  LEU   B CD1 
5401 C  CD2 . LEU   B 93  ? 0.1340 0.1362 0.1722 -0.0040 -0.0087 0.0064  93  LEU   B CD2 
5413 N  N   . HIS   B 94  ? 0.1300 0.1196 0.1202 -0.0057 -0.0099 0.0103  94  HIS   B N   
5414 C  CA  . HIS   B 94  ? 0.1357 0.1182 0.1275 -0.0024 -0.0057 0.0061  94  HIS   B CA  
5415 C  C   . HIS   B 94  ? 0.1335 0.1205 0.1431 -0.0022 -0.0022 0.0098  94  HIS   B C   
5416 O  O   . HIS   B 94  ? 0.1344 0.1300 0.1771 -0.0066 0.0095  -0.0056 94  HIS   B O   
5417 C  CB  . HIS   B 94  ? 0.1322 0.1261 0.1303 -0.0041 -0.0073 0.0021  94  HIS   B CB  
5418 C  CG  . HIS   B 94  ? 0.1371 0.1239 0.1305 -0.0102 -0.0205 0.0040  94  HIS   B CG  
5419 N  ND1 . HIS   B 94  ? 0.1390 0.1271 0.1301 -0.0074 -0.0193 0.0036  94  HIS   B ND1 
5420 C  CD2 . HIS   B 94  ? 0.1394 0.1288 0.1256 -0.0007 -0.0132 0.0062  94  HIS   B CD2 
5421 C  CE1 . HIS   B 94  ? 0.1474 0.1267 0.1211 -0.0124 -0.0196 0.0034  94  HIS   B CE1 
5422 N  NE2 . HIS   B 94  ? 0.1373 0.1329 0.1319 -0.0147 -0.0151 0.0062  94  HIS   B NE2 
5430 N  N   . VAL   B 95  ? 0.1262 0.1185 0.1427 0.0008  -0.0028 0.0089  95  VAL   B N   
5431 C  CA  . VAL   B 95  ? 0.1267 0.1298 0.1323 -0.0024 0.0009  0.0170  95  VAL   B CA  
5432 C  C   . VAL   B 95  ? 0.1314 0.1291 0.1400 -0.0033 0.0068  0.0094  95  VAL   B C   
5433 O  O   . VAL   B 95  ? 0.1378 0.1284 0.1610 0.0028  0.0017  0.0165  95  VAL   B O   
5434 C  CB  . VAL   B 95  ? 0.1308 0.1306 0.1433 -0.0043 -0.0073 0.0097  95  VAL   B CB  
5435 C  CG1 . VAL   B 95  ? 0.1415 0.1416 0.1616 -0.0114 -0.0042 0.0193  95  VAL   B CG1 
5436 C  CG2 . VAL   B 95  ? 0.1411 0.1298 0.1380 0.0015  -0.0127 0.0081  95  VAL   B CG2 
5446 N  N   . VAL   B 96  ? 0.1445 0.1326 0.1323 0.0096  0.0039  0.0190  96  VAL   B N   
5447 C  CA  . VAL   B 96  ? 0.1514 0.1478 0.1367 0.0080  0.0090  0.0193  96  VAL   B CA  
5448 C  C   . VAL   B 96  ? 0.1564 0.1466 0.1463 0.0065  0.0139  0.0197  96  VAL   B C   
5449 O  O   . VAL   B 96  ? 0.1588 0.1506 0.1668 0.0026  0.0215  0.0057  96  VAL   B O   
5450 C  CB  . VAL   B 96  ? 0.1615 0.1630 0.1372 0.0068  0.0070  0.0139  96  VAL   B CB  
5451 C  CG1 . VAL   B 96  ? 0.1571 0.1764 0.1554 0.0142  0.0088  0.0068  96  VAL   B CG1 
5452 C  CG2 . VAL   B 96  ? 0.1649 0.1699 0.1576 0.0100  0.0122  0.0055  96  VAL   B CG2 
5462 N  N   . GLY   B 97  ? 0.1599 0.1470 0.1417 0.0039  0.0090  0.0240  97  GLY   B N   
5463 C  CA  . GLY   B 97  ? 0.1743 0.1528 0.1499 0.0018  0.0104  0.0211  97  GLY   B CA  
5464 C  C   . GLY   B 97  ? 0.1940 0.1600 0.1623 0.0114  0.0053  0.0202  97  GLY   B C   
5465 O  O   . GLY   B 97  ? 0.2077 0.1671 0.1578 0.0059  0.0064  0.0127  97  GLY   B O   
5469 N  N   . PRO   B 98  ? 0.2103 0.1624 0.1849 0.0087  0.0321  0.0384  98  PRO   B N   
5470 C  CA  . PRO   B 98  ? 0.2239 0.1812 0.1857 0.0197  0.0453  0.0315  98  PRO   B CA  
5471 C  C   . PRO   B 98  ? 0.2356 0.1841 0.1592 0.0395  0.0497  0.0502  98  PRO   B C   
5472 O  O   . PRO   B 98  ? 0.2295 0.1776 0.1812 0.0354  0.0493  0.0480  98  PRO   B O   
5473 C  CB  . PRO   B 98  ? 0.2109 0.1867 0.2019 0.0120  0.0562  0.0323  98  PRO   B CB  
5474 C  CG  . PRO   B 98  ? 0.2069 0.1785 0.1995 0.0089  0.0456  0.0402  98  PRO   B CG  
5475 C  CD  . PRO   B 98  ? 0.1956 0.1640 0.1929 0.0124  0.0355  0.0384  98  PRO   B CD  
5483 N  N   . ASN   B 99  ? 0.2460 0.2015 0.1744 0.0557  0.0502  0.0307  99  ASN   B N   
5484 C  CA  . ASN   B 99  ? 0.2689 0.2112 0.1770 0.0606  0.0403  0.0500  99  ASN   B CA  
5485 C  C   . ASN   B 99  ? 0.2966 0.2462 0.2109 0.0540  0.0522  0.0783  99  ASN   B C   
5486 O  O   . ASN   B 99  ? 0.3048 0.2509 0.2150 0.0530  0.0448  0.0778  99  ASN   B O   
5487 C  CB  . ASN   B 99  ? 0.2787 0.2068 0.1806 0.0559  0.0323  0.0441  99  ASN   B CB  
5488 C  CG  . ASN   B 99  ? 0.2809 0.2114 0.2021 0.0490  0.0223  0.0434  99  ASN   B CG  
5489 O  OD1 . ASN   B 99  ? 0.2802 0.2139 0.2224 0.0513  0.0260  0.0481  99  ASN   B OD1 
5490 N  ND2 . ASN   B 99  ? 0.2808 0.2071 0.2099 0.0494  -0.0019 0.0397  99  ASN   B ND2 
5497 N  N   A VAL   B 100 ? 0.3128 0.2585 0.2525 0.0407  0.0561  0.1026  100 VAL   B N   
5498 N  N   B VAL   B 100 ? 0.3163 0.2605 0.2537 0.0440  0.0453  0.0909  100 VAL   B N   
5499 C  CA  A VAL   B 100 ? 0.3373 0.2769 0.3058 0.0293  0.0523  0.1159  100 VAL   B CA  
5500 C  CA  B VAL   B 100 ? 0.3394 0.2773 0.2978 0.0349  0.0357  0.0996  100 VAL   B CA  
5501 C  C   A VAL   B 100 ? 0.3582 0.2839 0.2986 0.0336  0.0490  0.1346  100 VAL   B C   
5502 C  C   B VAL   B 100 ? 0.3581 0.2842 0.2985 0.0374  0.0339  0.1207  100 VAL   B C   
5503 O  O   A VAL   B 100 ? 0.3651 0.2953 0.2996 0.0285  0.0588  0.1289  100 VAL   B O   
5504 O  O   B VAL   B 100 ? 0.3616 0.2898 0.2975 0.0336  0.0363  0.1161  100 VAL   B O   
5505 C  CB  A VAL   B 100 ? 0.3437 0.2888 0.3684 0.0099  0.0481  0.1193  100 VAL   B CB  
5506 C  CB  B VAL   B 100 ? 0.3443 0.2863 0.3395 0.0222  0.0282  0.0928  100 VAL   B CB  
5507 C  CG1 A VAL   B 100 ? 0.3476 0.2943 0.3896 0.0047  0.0485  0.1192  100 VAL   B CG1 
5508 C  CG1 B VAL   B 100 ? 0.3470 0.2901 0.3532 0.0187  0.0267  0.0904  100 VAL   B CG1 
5509 C  CG2 A VAL   B 100 ? 0.3437 0.2927 0.3843 0.0033  0.0497  0.1258  100 VAL   B CG2 
5510 C  CG2 B VAL   B 100 ? 0.3446 0.2892 0.3519 0.0179  0.0265  0.0925  100 VAL   B CG2 
5529 N  N   . ASN   B 101 ? 0.3727 0.2874 0.3009 0.0450  0.0309  0.1367  101 ASN   B N   
5530 C  CA  . ASN   B 101 ? 0.4079 0.3038 0.3185 0.0545  0.0108  0.1452  101 ASN   B CA  
5531 C  C   . ASN   B 101 ? 0.4460 0.3417 0.3301 0.0539  -0.0001 0.1522  101 ASN   B C   
5532 O  O   . ASN   B 101 ? 0.4506 0.3556 0.3551 0.0582  0.0025  0.1269  101 ASN   B O   
5533 C  CB  . ASN   B 101 ? 0.4075 0.2907 0.3326 0.0522  0.0156  0.1244  101 ASN   B CB  
5534 C  CG  . ASN   B 101 ? 0.4054 0.2749 0.3327 0.0500  0.0194  0.1223  101 ASN   B CG  
5535 O  OD1 . ASN   B 101 ? 0.4102 0.2756 0.3556 0.0435  0.0326  0.1176  101 ASN   B OD1 
5536 N  ND2 . ASN   B 101 ? 0.3995 0.2658 0.3222 0.0524  0.0161  0.1152  101 ASN   B ND2 
5544 N  N   . LYS   B 102 ? 0.4771 0.3750 0.3540 0.0407  0.0055  0.1480  102 LYS   B N   
5545 C  CA  . LYS   B 102 ? 0.5057 0.4162 0.3905 0.0256  0.0149  0.1201  102 LYS   B CA  
5546 C  C   . LYS   B 102 ? 0.5014 0.4183 0.3662 0.0242  0.0227  0.1242  102 LYS   B C   
5547 O  O   . LYS   B 102 ? 0.5106 0.4229 0.3730 0.0252  0.0104  0.1236  102 LYS   B O   
5548 C  CB  . LYS   B 102 ? 0.5342 0.4519 0.4579 0.0139  0.0252  0.0787  102 LYS   B CB  
5549 C  CG  . LYS   B 102 ? 0.5581 0.4818 0.5254 0.0053  0.0348  0.0380  102 LYS   B CG  
5550 C  CD  . LYS   B 102 ? 0.5779 0.5058 0.5885 -0.0015 0.0431  0.0062  102 LYS   B CD  
5551 C  CE  . LYS   B 102 ? 0.5918 0.5229 0.6358 -0.0075 0.0494  -0.0158 102 LYS   B CE  
5552 N  NZ  . LYS   B 102 ? 0.5996 0.5327 0.6632 -0.0106 0.0514  -0.0281 102 LYS   B NZ  
5566 N  N   . GLY   B 103 ? 0.4847 0.4133 0.3574 0.0214  0.0430  0.1162  103 GLY   B N   
5567 C  CA  . GLY   B 103 ? 0.4654 0.4069 0.3658 0.0194  0.0617  0.0953  103 GLY   B CA  
5568 C  C   . GLY   B 103 ? 0.4424 0.3957 0.3599 0.0146  0.0774  0.0753  103 GLY   B C   
5569 O  O   . GLY   B 103 ? 0.4475 0.4021 0.3666 0.0127  0.0803  0.0771  103 GLY   B O   
5573 N  N   A GLU   B 104 ? 0.4253 0.3830 0.3420 0.0150  0.0946  0.0622  104 GLU   B N   
5574 N  N   B GLU   B 104 ? 0.4295 0.3887 0.3589 0.0118  0.0686  0.0587  104 GLU   B N   
5575 C  CA  A GLU   B 104 ? 0.4072 0.3697 0.3228 0.0190  0.1050  0.0467  104 GLU   B CA  
5576 C  CA  B GLU   B 104 ? 0.4156 0.3805 0.3528 0.0100  0.0583  0.0401  104 GLU   B CA  
5577 C  C   A GLU   B 104 ? 0.4080 0.3702 0.3289 0.0061  0.1366  0.0527  104 GLU   B C   
5578 C  C   B GLU   B 104 ? 0.4116 0.3792 0.3613 0.0048  0.0665  0.0346  104 GLU   B C   
5579 O  O   A GLU   B 104 ? 0.4079 0.3723 0.3442 0.0033  0.1381  0.0524  104 GLU   B O   
5580 O  O   B GLU   B 104 ? 0.4116 0.3795 0.3670 0.0037  0.0676  0.0332  104 GLU   B O   
5581 C  CB  A GLU   B 104 ? 0.3927 0.3535 0.3081 0.0369  0.0736  0.0160  104 GLU   B CB  
5582 C  CB  B GLU   B 104 ? 0.4071 0.3720 0.3389 0.0133  0.0387  0.0235  104 GLU   B CB  
5583 C  CG  A GLU   B 104 ? 0.3797 0.3396 0.2883 0.0540  0.0354  -0.0197 104 GLU   B CG  
5584 C  CG  B GLU   B 104 ? 0.3997 0.3647 0.3248 0.0162  0.0176  0.0053  104 GLU   B CG  
5585 C  CD  A GLU   B 104 ? 0.3667 0.3252 0.2630 0.0693  0.0052  -0.0431 104 GLU   B CD  
5586 C  CD  B GLU   B 104 ? 0.3935 0.3578 0.3112 0.0180  0.0011  -0.0075 104 GLU   B CD  
5587 O  OE1 A GLU   B 104 ? 0.3513 0.3107 0.2246 0.0832  0.0112  -0.0492 104 GLU   B OE1 
5588 O  OE1 B GLU   B 104 ? 0.3890 0.3532 0.2986 0.0182  0.0003  -0.0092 104 GLU   B OE1 
5589 O  OE2 A GLU   B 104 ? 0.3684 0.3272 0.2589 0.0678  -0.0227 -0.0588 104 GLU   B OE2 
5590 O  OE2 B GLU   B 104 ? 0.3930 0.3572 0.3084 0.0188  -0.0108 -0.0157 104 GLU   B OE2 
5603 N  N   A ASP   B 105 ? 0.4055 0.3686 0.3233 -0.0030 0.1632  0.0578  105 ASP   B N   
5604 N  N   B ASP   B 105 ? 0.4067 0.3775 0.3624 0.0007  0.0726  0.0300  105 ASP   B N   
5605 C  CA  A ASP   B 105 ? 0.4054 0.3676 0.3394 -0.0098 0.1819  0.0484  105 ASP   B CA  
5606 C  CA  B ASP   B 105 ? 0.4026 0.3751 0.3702 -0.0023 0.0765  0.0212  105 ASP   B CA  
5607 C  C   A ASP   B 105 ? 0.3894 0.3405 0.3035 -0.0203 0.1856  0.0477  105 ASP   B C   
5608 C  C   B ASP   B 105 ? 0.3936 0.3638 0.3494 -0.0054 0.0768  0.0157  105 ASP   B C   
5609 O  O   A ASP   B 105 ? 0.3725 0.3357 0.2854 -0.0169 0.1825  0.0492  105 ASP   B O   
5610 O  O   B ASP   B 105 ? 0.3928 0.3627 0.3397 -0.0047 0.0793  0.0163  105 ASP   B O   
5611 C  CB  A ASP   B 105 ? 0.4207 0.3898 0.4128 -0.0017 0.1778  0.0259  105 ASP   B CB  
5612 C  CB  B ASP   B 105 ? 0.4059 0.3824 0.4010 -0.0005 0.0781  0.0149  105 ASP   B CB  
5613 C  CG  A ASP   B 105 ? 0.4300 0.4046 0.4747 0.0018  0.1797  0.0105  105 ASP   B CG  
5614 C  CG  B ASP   B 105 ? 0.4074 0.3864 0.4283 -0.0006 0.0808  0.0113  105 ASP   B CG  
5615 O  OD1 A ASP   B 105 ? 0.4282 0.4088 0.4851 -0.0039 0.1920  0.0140  105 ASP   B OD1 
5616 O  OD1 B ASP   B 105 ? 0.4067 0.3876 0.4351 -0.0031 0.0837  0.0118  105 ASP   B OD1 
5617 O  OD2 A ASP   B 105 ? 0.4354 0.4111 0.5073 0.0080  0.1719  -0.0013 105 ASP   B OD2 
5618 O  OD2 B ASP   B 105 ? 0.4072 0.3880 0.4383 -0.0003 0.0824  0.0105  105 ASP   B OD2 
5627 N  N   A ILE   B 106 ? 0.3837 0.3179 0.3146 -0.0280 0.1751  0.0437  106 ILE   B N   
5628 N  N   B ILE   B 106 ? 0.3846 0.3528 0.3419 -0.0067 0.0719  0.0112  106 ILE   B N   
5629 C  CA  A ILE   B 106 ? 0.3653 0.2908 0.3240 -0.0439 0.1789  0.0387  106 ILE   B CA  
5630 C  CA  B ILE   B 106 ? 0.3727 0.3419 0.3403 -0.0091 0.0712  0.0059  106 ILE   B CA  
5631 C  C   A ILE   B 106 ? 0.3371 0.2813 0.3179 -0.0406 0.1762  0.0261  106 ILE   B C   
5632 C  C   B ILE   B 106 ? 0.3557 0.3349 0.3368 -0.0069 0.0708  -0.0013 106 ILE   B C   
5633 O  O   A ILE   B 106 ? 0.3262 0.2614 0.3138 -0.0427 0.1786  0.0245  106 ILE   B O   
5634 O  O   B ILE   B 106 ? 0.3533 0.3301 0.3332 -0.0085 0.0667  -0.0054 106 ILE   B O   
5635 C  CB  A ILE   B 106 ? 0.3794 0.2814 0.3469 -0.0551 0.1675  0.0408  106 ILE   B CB  
5636 C  CB  B ILE   B 106 ? 0.3781 0.3406 0.3437 -0.0128 0.0697  0.0076  106 ILE   B CB  
5637 C  CG1 A ILE   B 106 ? 0.3844 0.2798 0.3528 -0.0492 0.1581  0.0364  106 ILE   B CG1 
5638 C  CG1 B ILE   B 106 ? 0.3794 0.3393 0.3439 -0.0117 0.0671  0.0079  106 ILE   B CG1 
5639 C  CG2 A ILE   B 106 ? 0.3831 0.2813 0.3634 -0.0644 0.1687  0.0470  106 ILE   B CG2 
5640 C  CG2 B ILE   B 106 ? 0.3804 0.3425 0.3502 -0.0148 0.0705  0.0089  106 ILE   B CG2 
5641 C  CD1 A ILE   B 106 ? 0.3877 0.2813 0.3498 -0.0432 0.1544  0.0356  106 ILE   B CD1 
5642 C  CD1 B ILE   B 106 ? 0.3803 0.3388 0.3440 -0.0103 0.0659  0.0084  106 ILE   B CD1 
5665 N  N   A GLN   B 107 ? 0.3255 0.2972 0.3323 -0.0336 0.1654  0.0237  107 GLN   B N   
5666 N  N   B GLN   B 107 ? 0.3422 0.3339 0.3460 -0.0043 0.0726  -0.0014 107 GLN   B N   
5667 C  CA  A GLN   B 107 ? 0.3089 0.3106 0.3516 -0.0273 0.1480  0.0200  107 GLN   B CA  
5668 C  CA  B GLN   B 107 ? 0.3269 0.3303 0.3564 -0.0018 0.0739  0.0020  107 GLN   B CA  
5669 C  C   A GLN   B 107 ? 0.2807 0.2890 0.3234 -0.0128 0.1202  0.0091  107 GLN   B C   
5670 C  C   B GLN   B 107 ? 0.2941 0.3028 0.3224 0.0034  0.0837  0.0022  107 GLN   B C   
5671 O  O   A GLN   B 107 ? 0.2759 0.2862 0.3435 -0.0080 0.0971  -0.0081 107 GLN   B O   
5672 O  O   B GLN   B 107 ? 0.2940 0.3044 0.3286 0.0048  0.0739  -0.0056 107 GLN   B O   
5673 C  CB  A GLN   B 107 ? 0.3366 0.3468 0.4246 -0.0254 0.1199  0.0198  107 GLN   B CB  
5674 C  CB  B GLN   B 107 ? 0.3464 0.3529 0.4081 -0.0022 0.0601  0.0034  107 GLN   B CB  
5675 C  CG  A GLN   B 107 ? 0.3655 0.3791 0.4943 -0.0187 0.0825  0.0182  107 GLN   B CG  
5676 C  CG  B GLN   B 107 ? 0.3639 0.3725 0.4580 -0.0010 0.0438  0.0050  107 GLN   B CG  
5677 C  CD  A GLN   B 107 ? 0.3874 0.4034 0.5468 -0.0152 0.0570  0.0193  107 GLN   B CD  
5678 C  CD  B GLN   B 107 ? 0.3773 0.3873 0.4975 -0.0008 0.0315  0.0068  107 GLN   B CD  
5679 O  OE1 A GLN   B 107 ? 0.3947 0.4131 0.5651 -0.0118 0.0511  0.0165  107 GLN   B OE1 
5680 O  OE1 B GLN   B 107 ? 0.3816 0.3929 0.5105 0.0002  0.0287  0.0063  107 GLN   B OE1 
5681 N  NE2 A GLN   B 107 ? 0.3965 0.4106 0.5648 -0.0132 0.0469  0.0230  107 GLN   B NE2 
5682 N  NE2 B GLN   B 107 ? 0.3826 0.3920 0.5117 -0.0002 0.0269  0.0088  107 GLN   B NE2 
5699 N  N   . LEU   B 108 ? 0.2597 0.2721 0.2894 0.0114  0.1003  0.0094  108 LEU   B N   
5700 C  CA  . LEU   B 108 ? 0.2324 0.2399 0.2486 0.0278  0.0753  0.0308  108 LEU   B CA  
5701 C  C   . LEU   B 108 ? 0.1948 0.1965 0.2352 0.0269  0.0518  0.0369  108 LEU   B C   
5702 O  O   . LEU   B 108 ? 0.1953 0.1830 0.2260 0.0264  0.0410  0.0326  108 LEU   B O   
5703 C  CB  . LEU   B 108 ? 0.2473 0.2600 0.2357 0.0298  0.0747  0.0406  108 LEU   B CB  
5704 C  CG  . LEU   B 108 ? 0.2638 0.2884 0.2469 0.0293  0.0698  0.0167  108 LEU   B CG  
5705 C  CD1 . LEU   B 108 ? 0.2743 0.3010 0.2386 0.0199  0.0721  0.0165  108 LEU   B CD1 
5706 C  CD2 . LEU   B 108 ? 0.2744 0.2989 0.2611 0.0386  0.0595  0.0015  108 LEU   B CD2 
5719 N  N   . LEU   B 109 ? 0.1754 0.1739 0.2321 0.0165  0.0400  0.0301  109 LEU   B N   
5720 C  CA  . LEU   B 109 ? 0.1566 0.1457 0.2458 0.0088  0.0423  0.0324  109 LEU   B CA  
5721 C  C   . LEU   B 109 ? 0.1479 0.1340 0.2414 0.0027  0.0334  0.0212  109 LEU   B C   
5722 O  O   . LEU   B 109 ? 0.1469 0.1321 0.2298 0.0002  0.0293  0.0318  109 LEU   B O   
5723 C  CB  . LEU   B 109 ? 0.1631 0.1393 0.2491 0.0081  0.0293  0.0431  109 LEU   B CB  
5724 C  CG  . LEU   B 109 ? 0.1642 0.1402 0.2379 0.0025  0.0255  0.0333  109 LEU   B CG  
5725 C  CD1 . LEU   B 109 ? 0.1634 0.1513 0.2203 0.0138  0.0332  0.0307  109 LEU   B CD1 
5726 C  CD2 . LEU   B 109 ? 0.1728 0.1466 0.2526 0.0055  0.0154  0.0272  109 LEU   B CD2 
5738 N  N   . LYS   B 110 ? 0.1465 0.1379 0.2327 -0.0050 0.0314  0.0243  110 LYS   B N   
5739 C  CA  . LYS   B 110 ? 0.1416 0.1364 0.2275 -0.0033 0.0231  0.0222  110 LYS   B CA  
5740 C  C   . LYS   B 110 ? 0.1407 0.1355 0.2256 -0.0009 0.0314  0.0156  110 LYS   B C   
5741 O  O   . LYS   B 110 ? 0.1354 0.1360 0.2134 -0.0050 0.0247  0.0060  110 LYS   B O   
5742 C  CB  . LYS   B 110 ? 0.1440 0.1351 0.2439 -0.0046 0.0262  0.0145  110 LYS   B CB  
5743 C  CG  . LYS   B 110 ? 0.1428 0.1367 0.2564 -0.0059 0.0129  0.0176  110 LYS   B CG  
5744 C  CD  . LYS   B 110 ? 0.1468 0.1329 0.2702 -0.0087 0.0143  0.0225  110 LYS   B CD  
5745 C  CE  . LYS   B 110 ? 0.1460 0.1489 0.2891 -0.0031 0.0148  0.0096  110 LYS   B CE  
5746 N  NZ  . LYS   B 110 ? 0.1489 0.1633 0.2802 0.0013  0.0080  0.0061  110 LYS   B NZ  
5760 N  N   . SER   B 111 ? 0.1458 0.1336 0.2369 -0.0039 0.0303  0.0159  111 SER   B N   
5761 C  CA  . SER   B 111 ? 0.1541 0.1385 0.2199 0.0008  0.0243  0.0180  111 SER   B CA  
5762 C  C   . SER   B 111 ? 0.1479 0.1303 0.2053 0.0021  0.0168  0.0102  111 SER   B C   
5763 O  O   . SER   B 111 ? 0.1439 0.1347 0.2138 -0.0001 0.0145  0.0104  111 SER   B O   
5764 C  CB  . SER   B 111 ? 0.1597 0.1601 0.2260 0.0032  0.0401  0.0255  111 SER   B CB  
5765 O  OG  . SER   B 111 ? 0.1786 0.1917 0.2346 0.0096  0.0423  0.0307  111 SER   B OG  
5771 N  N   . ALA   B 112 ? 0.1381 0.1348 0.2168 0.0067  0.0200  0.0189  112 ALA   B N   
5772 C  CA  . ALA   B 112 ? 0.1378 0.1413 0.1978 -0.0005 0.0068  0.0081  112 ALA   B CA  
5773 C  C   . ALA   B 112 ? 0.1272 0.1313 0.1880 -0.0005 0.0011  0.0105  112 ALA   B C   
5774 O  O   . ALA   B 112 ? 0.1285 0.1351 0.2031 -0.0051 0.0093  0.0004  112 ALA   B O   
5775 C  CB  . ALA   B 112 ? 0.1400 0.1461 0.2072 0.0042  0.0073  0.0203  112 ALA   B CB  
5781 N  N   . TYR   B 113 ? 0.1232 0.1257 0.2003 -0.0012 0.0124  0.0127  113 TYR   B N   
5782 C  CA  . TYR   B 113 ? 0.1255 0.1220 0.1901 -0.0025 0.0099  0.0040  113 TYR   B CA  
5783 C  C   . TYR   B 113 ? 0.1247 0.1174 0.1899 -0.0090 0.0101  0.0057  113 TYR   B C   
5784 O  O   . TYR   B 113 ? 0.1289 0.1210 0.1825 -0.0098 0.0037  0.0036  113 TYR   B O   
5785 C  CB  . TYR   B 113 ? 0.1331 0.1133 0.2014 -0.0044 0.0198  0.0127  113 TYR   B CB  
5786 C  CG  . TYR   B 113 ? 0.1304 0.1225 0.2147 -0.0078 0.0107  0.0151  113 TYR   B CG  
5787 C  CD1 . TYR   B 113 ? 0.1366 0.1214 0.2270 -0.0067 0.0151  0.0235  113 TYR   B CD1 
5788 C  CD2 . TYR   B 113 ? 0.1372 0.1192 0.2120 -0.0041 0.0106  0.0133  113 TYR   B CD2 
5789 C  CE1 . TYR   B 113 ? 0.1389 0.1280 0.2138 -0.0027 0.0187  0.0134  113 TYR   B CE1 
5790 C  CE2 . TYR   B 113 ? 0.1475 0.1145 0.2225 0.0001  0.0179  0.0220  113 TYR   B CE2 
5791 C  CZ  . TYR   B 113 ? 0.1353 0.1192 0.2221 0.0034  0.0106  0.0138  113 TYR   B CZ  
5792 O  OH  . TYR   B 113 ? 0.1472 0.1171 0.2526 0.0065  0.0214  0.0099  113 TYR   B OH  
5802 N  N   . GLU   B 114 ? 0.1235 0.1167 0.2012 -0.0047 0.0107  0.0047  114 GLU   B N   
5803 C  CA  . GLU   B 114 ? 0.1232 0.1118 0.1977 0.0031  0.0079  0.0060  114 GLU   B CA  
5804 C  C   . GLU   B 114 ? 0.1225 0.1181 0.1887 -0.0025 0.0064  0.0061  114 GLU   B C   
5805 O  O   . GLU   B 114 ? 0.1223 0.1226 0.2023 -0.0011 -0.0007 0.0128  114 GLU   B O   
5806 C  CB  . GLU   B 114 ? 0.1250 0.1223 0.2097 -0.0022 0.0102  0.0108  114 GLU   B CB  
5807 C  CG  . GLU   B 114 ? 0.1290 0.1224 0.2186 -0.0009 0.0083  0.0085  114 GLU   B CG  
5808 C  CD  . GLU   B 114 ? 0.1269 0.1240 0.2194 -0.0043 0.0073  0.0110  114 GLU   B CD  
5809 O  OE1 . GLU   B 114 ? 0.1266 0.1393 0.2108 -0.0100 0.0149  0.0128  114 GLU   B OE1 
5810 O  OE2 . GLU   B 114 ? 0.1292 0.1414 0.2356 -0.0180 0.0117  0.0127  114 GLU   B OE2 
5817 N  N   . ASN   B 115 ? 0.1270 0.1123 0.1864 -0.0038 0.0021  0.0084  115 ASN   B N   
5818 C  CA  . ASN   B 115 ? 0.1269 0.1206 0.1714 -0.0081 0.0012  0.0082  115 ASN   B CA  
5819 C  C   . ASN   B 115 ? 0.1225 0.1171 0.1757 -0.0127 -0.0005 -0.0031 115 ASN   B C   
5820 O  O   . ASN   B 115 ? 0.1341 0.1190 0.1869 -0.0122 0.0073  0.0012  115 ASN   B O   
5821 C  CB  . ASN   B 115 ? 0.1356 0.1326 0.1764 -0.0105 0.0035  0.0060  115 ASN   B CB  
5822 C  CG  . ASN   B 115 ? 0.1457 0.1371 0.1752 0.0012  -0.0010 0.0020  115 ASN   B CG  
5823 O  OD1 . ASN   B 115 ? 0.1848 0.1492 0.1944 0.0013  0.0176  -0.0068 115 ASN   B OD1 
5824 N  ND2 . ASN   B 115 ? 0.1450 0.1490 0.1725 -0.0032 0.0093  0.0054  115 ASN   B ND2 
5831 N  N   . PHE   B 116 ? 0.1231 0.1225 0.1613 -0.0050 -0.0009 0.0047  116 PHE   B N   
5832 C  CA  . PHE   B 116 ? 0.1285 0.1225 0.1682 -0.0072 -0.0033 0.0050  116 PHE   B CA  
5833 C  C   . PHE   B 116 ? 0.1300 0.1094 0.1752 -0.0111 -0.0059 0.0066  116 PHE   B C   
5834 O  O   . PHE   B 116 ? 0.1322 0.1210 0.1835 -0.0032 -0.0064 0.0064  116 PHE   B O   
5835 C  CB  . PHE   B 116 ? 0.1265 0.1169 0.1651 -0.0072 -0.0123 0.0057  116 PHE   B CB  
5836 C  CG  . PHE   B 116 ? 0.1233 0.1181 0.1672 -0.0109 0.0002  0.0067  116 PHE   B CG  
5837 C  CD1 . PHE   B 116 ? 0.1293 0.1244 0.1856 -0.0042 0.0009  0.0048  116 PHE   B CD1 
5838 C  CD2 . PHE   B 116 ? 0.1277 0.1254 0.1708 -0.0065 0.0009  0.0025  116 PHE   B CD2 
5839 C  CE1 . PHE   B 116 ? 0.1319 0.1293 0.1802 -0.0047 -0.0100 0.0084  116 PHE   B CE1 
5840 C  CE2 . PHE   B 116 ? 0.1287 0.1244 0.1725 -0.0026 0.0004  0.0047  116 PHE   B CE2 
5841 C  CZ  . PHE   B 116 ? 0.1229 0.1292 0.1725 -0.0041 -0.0102 0.0081  116 PHE   B CZ  
5851 N  N   . ASN   B 117 ? 0.1265 0.1172 0.1868 -0.0051 -0.0087 0.0059  117 ASN   B N   
5852 C  CA  . ASN   B 117 ? 0.1322 0.1161 0.1892 -0.0038 -0.0078 0.0065  117 ASN   B CA  
5853 C  C   . ASN   B 117 ? 0.1346 0.1192 0.1980 0.0006  -0.0085 0.0056  117 ASN   B C   
5854 O  O   . ASN   B 117 ? 0.1439 0.1262 0.2250 -0.0054 -0.0301 0.0111  117 ASN   B O   
5855 C  CB  . ASN   B 117 ? 0.1341 0.1190 0.1972 -0.0034 -0.0077 -0.0048 117 ASN   B CB  
5856 C  CG  . ASN   B 117 ? 0.1297 0.1230 0.2066 0.0007  -0.0049 -0.0026 117 ASN   B CG  
5857 O  OD1 . ASN   B 117 ? 0.1505 0.1237 0.2169 -0.0137 0.0032  -0.0048 117 ASN   B OD1 
5858 N  ND2 . ASN   B 117 ? 0.1331 0.1284 0.2027 -0.0039 -0.0087 -0.0047 117 ASN   B ND2 
5865 N  N   . GLN   B 118 ? 0.1381 0.1132 0.1834 -0.0077 -0.0104 0.0008  118 GLN   B N   
5866 C  CA  . GLN   B 118 ? 0.1436 0.1183 0.2059 -0.0032 -0.0065 -0.0048 118 GLN   B CA  
5867 C  C   . GLN   B 118 ? 0.1439 0.1175 0.2047 -0.0023 -0.0095 -0.0039 118 GLN   B C   
5868 O  O   . GLN   B 118 ? 0.1639 0.1184 0.2410 -0.0082 0.0007  0.0057  118 GLN   B O   
5869 C  CB  . GLN   B 118 ? 0.1464 0.1228 0.2114 -0.0025 -0.0147 -0.0008 118 GLN   B CB  
5870 C  CG  . GLN   B 118 ? 0.1536 0.1226 0.2068 0.0051  -0.0038 -0.0086 118 GLN   B CG  
5871 C  CD  . GLN   B 118 ? 0.1591 0.1200 0.2041 -0.0013 -0.0093 -0.0163 118 GLN   B CD  
5872 O  OE1 . GLN   B 118 ? 0.1628 0.1190 0.2309 0.0021  0.0019  0.0030  118 GLN   B OE1 
5873 N  NE2 . GLN   B 118 ? 0.1665 0.1272 0.2043 -0.0019 -0.0118 0.0048  118 GLN   B NE2 
5882 N  N   . HIS   B 119 ? 0.1457 0.1238 0.1700 -0.0099 -0.0112 0.0065  119 HIS   B N   
5883 C  CA  . HIS   B 119 ? 0.1531 0.1323 0.1677 -0.0072 -0.0167 0.0057  119 HIS   B CA  
5884 C  C   . HIS   B 119 ? 0.1555 0.1332 0.1654 -0.0048 -0.0268 0.0078  119 HIS   B C   
5885 O  O   . HIS   B 119 ? 0.1649 0.1318 0.1864 -0.0261 -0.0260 0.0101  119 HIS   B O   
5886 C  CB  . HIS   B 119 ? 0.1531 0.1391 0.1761 -0.0046 -0.0215 0.0057  119 HIS   B CB  
5887 C  CG  . HIS   B 119 ? 0.1589 0.1636 0.1922 0.0055  -0.0365 -0.0091 119 HIS   B CG  
5888 N  ND1 . HIS   B 119 ? 0.1721 0.1832 0.2179 0.0028  -0.0504 -0.0272 119 HIS   B ND1 
5889 C  CD2 . HIS   B 119 ? 0.1769 0.1832 0.1994 0.0372  -0.0514 -0.0100 119 HIS   B CD2 
5890 C  CE1 . HIS   B 119 ? 0.1890 0.1966 0.2267 0.0138  -0.0545 -0.0450 119 HIS   B CE1 
5891 N  NE2 . HIS   B 119 ? 0.1924 0.2047 0.2171 0.0320  -0.0515 -0.0323 119 HIS   B NE2 
5899 N  N   . GLU   B 120 ? 0.1775 0.1386 0.1682 -0.0109 -0.0387 0.0193  120 GLU   B N   
5900 C  CA  . GLU   B 120 ? 0.2062 0.1556 0.1740 -0.0052 -0.0507 0.0315  120 GLU   B CA  
5901 C  C   . GLU   B 120 ? 0.1821 0.1429 0.1649 -0.0159 -0.0383 0.0273  120 GLU   B C   
5902 O  O   . GLU   B 120 ? 0.1748 0.1530 0.1672 -0.0155 -0.0357 0.0140  120 GLU   B O   
5903 C  CB  . GLU   B 120 ? 0.2736 0.1955 0.2551 0.0157  -0.0768 0.0632  120 GLU   B CB  
5904 C  CG  . GLU   B 120 ? 0.3344 0.2680 0.3629 0.0268  -0.0983 0.0770  120 GLU   B CG  
5905 C  CD  . GLU   B 120 ? 0.3812 0.3412 0.4700 0.0309  -0.1057 0.0822  120 GLU   B CD  
5906 O  OE1 . GLU   B 120 ? 0.3991 0.3655 0.5062 0.0276  -0.1026 0.0907  120 GLU   B OE1 
5907 O  OE2 . GLU   B 120 ? 0.4021 0.3722 0.5229 0.0316  -0.1040 0.0723  120 GLU   B OE2 
5914 N  N   . VAL   B 121 ? 0.1741 0.1353 0.1714 -0.0247 -0.0281 0.0194  121 VAL   B N   
5915 C  CA  . VAL   B 121 ? 0.1679 0.1471 0.1524 -0.0224 -0.0296 0.0139  121 VAL   B CA  
5916 C  C   . VAL   B 121 ? 0.1588 0.1432 0.1461 -0.0244 -0.0248 0.0121  121 VAL   B C   
5917 O  O   . VAL   B 121 ? 0.1686 0.1388 0.1703 -0.0321 -0.0282 0.0103  121 VAL   B O   
5918 C  CB  . VAL   B 121 ? 0.1898 0.1853 0.1636 -0.0106 -0.0329 0.0192  121 VAL   B CB  
5919 C  CG1 . VAL   B 121 ? 0.1906 0.1945 0.1864 -0.0210 -0.0214 0.0179  121 VAL   B CG1 
5920 C  CG2 . VAL   B 121 ? 0.2130 0.2057 0.1748 0.0003  -0.0258 0.0139  121 VAL   B CG2 
5930 N  N   . LEU   B 122 ? 0.1483 0.1364 0.1421 -0.0204 -0.0230 0.0123  122 LEU   B N   
5931 C  CA  . LEU   B 122 ? 0.1387 0.1452 0.1344 -0.0202 -0.0215 0.0069  122 LEU   B CA  
5932 C  C   . LEU   B 122 ? 0.1415 0.1342 0.1391 -0.0257 -0.0187 0.0088  122 LEU   B C   
5933 O  O   . LEU   B 122 ? 0.1493 0.1342 0.1755 -0.0297 -0.0219 0.0049  122 LEU   B O   
5934 C  CB  . LEU   B 122 ? 0.1641 0.1511 0.1662 -0.0072 -0.0275 0.0119  122 LEU   B CB  
5935 C  CG  . LEU   B 122 ? 0.1522 0.1582 0.1699 -0.0171 -0.0155 0.0120  122 LEU   B CG  
5936 C  CD1 . LEU   B 122 ? 0.1535 0.1794 0.1811 -0.0229 -0.0155 0.0076  122 LEU   B CD1 
5937 C  CD2 . LEU   B 122 ? 0.1547 0.1563 0.1574 -0.0146 -0.0135 -0.0060 122 LEU   B CD2 
5949 N  N   . LEU   B 123 ? 0.1468 0.1221 0.1374 -0.0225 -0.0175 0.0104  123 LEU   B N   
5950 C  CA  . LEU   B 123 ? 0.1483 0.1241 0.1355 -0.0228 -0.0260 0.0001  123 LEU   B CA  
5951 C  C   . LEU   B 123 ? 0.1433 0.1209 0.1352 -0.0259 -0.0186 -0.0048 123 LEU   B C   
5952 O  O   . LEU   B 123 ? 0.1520 0.1274 0.1364 -0.0306 -0.0192 0.0043  123 LEU   B O   
5953 C  CB  . LEU   B 123 ? 0.1508 0.1300 0.1536 -0.0235 -0.0144 0.0017  123 LEU   B CB  
5954 C  CG  . LEU   B 123 ? 0.1483 0.1327 0.1665 -0.0192 -0.0072 0.0081  123 LEU   B CG  
5955 C  CD1 . LEU   B 123 ? 0.1581 0.1373 0.1775 -0.0174 -0.0005 -0.0047 123 LEU   B CD1 
5956 C  CD2 . LEU   B 123 ? 0.1588 0.1431 0.1764 -0.0166 0.0018  0.0133  123 LEU   B CD2 
5968 N  N   . ALA   B 124 ? 0.1385 0.1214 0.1366 -0.0225 -0.0059 -0.0036 124 ALA   B N   
5969 C  CA  . ALA   B 124 ? 0.1306 0.1179 0.1476 -0.0155 -0.0105 -0.0065 124 ALA   B CA  
5970 C  C   . ALA   B 124 ? 0.1282 0.1185 0.1442 -0.0192 -0.0107 -0.0060 124 ALA   B C   
5971 O  O   . ALA   B 124 ? 0.1397 0.1252 0.1602 -0.0134 -0.0142 0.0031  124 ALA   B O   
5972 C  CB  . ALA   B 124 ? 0.1413 0.1296 0.1493 -0.0075 0.0003  -0.0012 124 ALA   B CB  
5978 N  N   . PRO   B 125 ? 0.1396 0.1223 0.1402 -0.0150 -0.0122 0.0126  125 PRO   B N   
5979 C  CA  . PRO   B 125 ? 0.1483 0.1247 0.1578 -0.0157 -0.0162 0.0207  125 PRO   B CA  
5980 C  C   . PRO   B 125 ? 0.1438 0.1194 0.1699 -0.0134 -0.0106 0.0143  125 PRO   B C   
5981 O  O   . PRO   B 125 ? 0.1440 0.1199 0.1954 -0.0108 -0.0040 0.0184  125 PRO   B O   
5982 C  CB  . PRO   B 125 ? 0.1516 0.1500 0.1803 -0.0225 -0.0205 0.0349  125 PRO   B CB  
5983 C  CG  . PRO   B 125 ? 0.1583 0.1555 0.1627 -0.0290 -0.0195 0.0154  125 PRO   B CG  
5984 C  CD  . PRO   B 125 ? 0.1477 0.1351 0.1480 -0.0303 -0.0119 0.0099  125 PRO   B CD  
5992 N  N   . LEU   B 126 ? 0.1460 0.1161 0.1927 -0.0124 0.0087  0.0149  126 LEU   B N   
5993 C  CA  . LEU   B 126 ? 0.1528 0.1255 0.1953 -0.0121 0.0176  0.0181  126 LEU   B CA  
5994 C  C   . LEU   B 126 ? 0.1494 0.1340 0.2027 -0.0012 0.0242  0.0248  126 LEU   B C   
5995 O  O   . LEU   B 126 ? 0.1708 0.1606 0.2201 0.0145  -0.0009 -0.0054 126 LEU   B O   
5996 C  CB  . LEU   B 126 ? 0.1711 0.1296 0.2251 -0.0156 0.0222  0.0111  126 LEU   B CB  
5997 C  CG  . LEU   B 126 ? 0.1841 0.1369 0.2446 -0.0252 0.0152  -0.0078 126 LEU   B CG  
5998 C  CD1 . LEU   B 126 ? 0.2028 0.1438 0.2928 -0.0214 0.0130  -0.0109 126 LEU   B CD1 
5999 C  CD2 . LEU   B 126 ? 0.1843 0.1497 0.2473 -0.0267 0.0130  -0.0138 126 LEU   B CD2 
6011 N  N   . LEU   B 127 ? 0.1430 0.1226 0.2136 0.0026  0.0295  0.0151  127 LEU   B N   
6012 C  CA  . LEU   B 127 ? 0.1450 0.1344 0.2254 -0.0038 0.0290  0.0209  127 LEU   B CA  
6013 C  C   . LEU   B 127 ? 0.1429 0.1292 0.2220 -0.0003 0.0194  0.0259  127 LEU   B C   
6014 O  O   . LEU   B 127 ? 0.1426 0.1360 0.2311 -0.0138 0.0100  0.0239  127 LEU   B O   
6015 C  CB  . LEU   B 127 ? 0.1588 0.1310 0.2277 -0.0024 0.0275  0.0236  127 LEU   B CB  
6016 C  CG  . LEU   B 127 ? 0.1688 0.1345 0.2379 0.0043  0.0282  0.0205  127 LEU   B CG  
6017 C  CD1 . LEU   B 127 ? 0.1818 0.1355 0.2303 0.0072  0.0179  0.0133  127 LEU   B CD1 
6018 C  CD2 . LEU   B 127 ? 0.1707 0.1403 0.2559 -0.0070 0.0219  0.0290  127 LEU   B CD2 
6030 N  N   . SER   B 128 ? 0.1446 0.1320 0.2191 0.0018  0.0062  0.0194  128 SER   B N   
6031 C  CA  . SER   B 128 ? 0.1585 0.1388 0.2141 0.0066  -0.0023 0.0267  128 SER   B CA  
6032 C  C   . SER   B 128 ? 0.1730 0.1441 0.2353 0.0098  -0.0246 0.0229  128 SER   B C   
6033 O  O   . SER   B 128 ? 0.1897 0.1453 0.2662 0.0070  -0.0204 0.0339  128 SER   B O   
6034 C  CB  . SER   B 128 ? 0.1703 0.1404 0.2095 0.0070  0.0055  0.0327  128 SER   B CB  
6035 O  OG  . SER   B 128 ? 0.1758 0.1552 0.2109 0.0103  0.0114  0.0378  128 SER   B OG  
6041 N  N   . ALA   B 129 ? 0.1853 0.1482 0.2583 0.0253  -0.0157 0.0119  129 ALA   B N   
6042 C  CA  . ALA   B 129 ? 0.1979 0.1520 0.2699 0.0295  -0.0120 0.0074  129 ALA   B CA  
6043 C  C   . ALA   B 129 ? 0.1871 0.1446 0.2586 0.0187  0.0057  0.0128  129 ALA   B C   
6044 O  O   . ALA   B 129 ? 0.1720 0.1488 0.2581 0.0172  -0.0005 0.0133  129 ALA   B O   
6045 C  CB  . ALA   B 129 ? 0.2173 0.1779 0.2979 0.0319  -0.0001 -0.0030 129 ALA   B CB  
6051 N  N   . GLY   B 130 ? 0.1844 0.1448 0.2599 0.0226  0.0053  0.0045  130 GLY   B N   
6052 C  CA  . GLY   B 130 ? 0.1920 0.1536 0.2665 0.0197  0.0178  0.0015  130 GLY   B CA  
6053 C  C   . GLY   B 130 ? 0.1946 0.1588 0.2612 0.0165  0.0155  0.0079  130 GLY   B C   
6054 O  O   . GLY   B 130 ? 0.2091 0.1649 0.2648 0.0155  0.0137  0.0187  130 GLY   B O   
6058 N  N   . ILE   B 131 ? 0.1888 0.1733 0.2693 0.0325  0.0116  0.0052  131 ILE   B N   
6059 C  CA  . ILE   B 131 ? 0.2025 0.1876 0.2668 0.0294  0.0017  0.0193  131 ILE   B CA  
6060 C  C   . ILE   B 131 ? 0.2166 0.1769 0.2293 0.0169  0.0031  0.0283  131 ILE   B C   
6061 O  O   . ILE   B 131 ? 0.2449 0.1980 0.2399 0.0155  -0.0101 0.0277  131 ILE   B O   
6062 C  CB  . ILE   B 131 ? 0.2042 0.2207 0.3059 0.0283  -0.0083 0.0283  131 ILE   B CB  
6063 C  CG1 . ILE   B 131 ? 0.2069 0.2410 0.3215 0.0051  0.0012  0.0335  131 ILE   B CG1 
6064 C  CG2 . ILE   B 131 ? 0.2030 0.2373 0.3310 0.0379  -0.0072 0.0199  131 ILE   B CG2 
6065 C  CD1 . ILE   B 131 ? 0.2165 0.2589 0.3372 -0.0108 -0.0019 0.0386  131 ILE   B CD1 
6077 N  N   . PHE   B 132 ? 0.2006 0.1628 0.2218 0.0135  0.0155  0.0250  132 PHE   B N   
6078 C  CA  . PHE   B 132 ? 0.2124 0.1634 0.2183 0.0094  0.0376  0.0184  132 PHE   B CA  
6079 C  C   . PHE   B 132 ? 0.2315 0.1791 0.2360 0.0142  0.0470  0.0144  132 PHE   B C   
6080 O  O   . PHE   B 132 ? 0.2469 0.1996 0.2531 0.0073  0.0586  0.0174  132 PHE   B O   
6081 C  CB  . PHE   B 132 ? 0.1978 0.1596 0.2089 0.0093  0.0371  0.0179  132 PHE   B CB  
6082 C  CG  . PHE   B 132 ? 0.1947 0.1626 0.2042 0.0141  0.0320  0.0233  132 PHE   B CG  
6083 C  CD1 . PHE   B 132 ? 0.2003 0.1642 0.2347 0.0116  0.0259  0.0238  132 PHE   B CD1 
6084 C  CD2 . PHE   B 132 ? 0.1930 0.1700 0.1861 0.0253  0.0298  0.0253  132 PHE   B CD2 
6085 C  CE1 . PHE   B 132 ? 0.2000 0.1666 0.2438 0.0072  0.0195  0.0241  132 PHE   B CE1 
6086 C  CE2 . PHE   B 132 ? 0.1979 0.1747 0.1922 0.0219  0.0226  0.0207  132 PHE   B CE2 
6087 C  CZ  . PHE   B 132 ? 0.1994 0.1717 0.2283 0.0123  0.0061  0.0354  132 PHE   B CZ  
6097 N  N   . GLY   B 133 ? 0.2328 0.1695 0.2399 0.0099  0.0369  0.0387  133 GLY   B N   
6098 C  CA  . GLY   B 133 ? 0.2402 0.1804 0.2581 -0.0081 0.0353  0.0458  133 GLY   B CA  
6099 C  C   . GLY   B 133 ? 0.2459 0.1839 0.2676 -0.0223 0.0391  0.0528  133 GLY   B C   
6100 O  O   . GLY   B 133 ? 0.2699 0.1950 0.3018 -0.0359 0.0388  0.0657  133 GLY   B O   
6104 N  N   . ALA   B 134 ? 0.2272 0.1818 0.2565 -0.0257 0.0376  0.0362  134 ALA   B N   
6105 C  CA  . ALA   B 134 ? 0.2197 0.1779 0.2619 -0.0193 0.0434  0.0221  134 ALA   B CA  
6106 C  C   . ALA   B 134 ? 0.2246 0.1721 0.2639 -0.0107 0.0374  0.0321  134 ALA   B C   
6107 O  O   . ALA   B 134 ? 0.2286 0.1929 0.2740 0.0017  0.0304  0.0215  134 ALA   B O   
6108 C  CB  . ALA   B 134 ? 0.2137 0.1765 0.2802 -0.0135 0.0341  0.0157  134 ALA   B CB  
6114 N  N   . ASP   B 135 ? 0.2389 0.1673 0.2718 -0.0162 0.0224  0.0370  135 ASP   B N   
6115 C  CA  . ASP   B 135 ? 0.2542 0.1575 0.2881 -0.0152 0.0086  0.0436  135 ASP   B CA  
6116 C  C   . ASP   B 135 ? 0.2344 0.1488 0.2699 -0.0064 0.0070  0.0431  135 ASP   B C   
6117 O  O   . ASP   B 135 ? 0.2242 0.1457 0.2775 -0.0047 0.0111  0.0351  135 ASP   B O   
6118 C  CB  . ASP   B 135 ? 0.2805 0.1668 0.3095 -0.0350 0.0007  0.0465  135 ASP   B CB  
6119 C  CG  . ASP   B 135 ? 0.3060 0.1715 0.3450 -0.0516 -0.0037 0.0328  135 ASP   B CG  
6120 O  OD1 . ASP   B 135 ? 0.3133 0.1562 0.3423 -0.0317 -0.0159 0.0285  135 ASP   B OD1 
6121 O  OD2 . ASP   B 135 ? 0.3256 0.2041 0.3892 -0.0659 -0.0019 0.0166  135 ASP   B OD2 
6126 N  N   . PRO   B 136 ? 0.2236 0.1531 0.2783 0.0159  -0.0111 0.0343  136 PRO   B N   
6127 C  CA  . PRO   B 136 ? 0.1991 0.1437 0.2804 0.0132  -0.0088 0.0234  136 PRO   B CA  
6128 C  C   . PRO   B 136 ? 0.1805 0.1346 0.2904 0.0135  -0.0068 0.0186  136 PRO   B C   
6129 O  O   . PRO   B 136 ? 0.1639 0.1355 0.2813 0.0073  0.0008  0.0149  136 PRO   B O   
6130 C  CB  . PRO   B 136 ? 0.2059 0.1674 0.2864 0.0274  -0.0129 0.0095  136 PRO   B CB  
6131 C  CG  . PRO   B 136 ? 0.2272 0.1771 0.3001 0.0326  -0.0067 0.0103  136 PRO   B CG  
6132 C  CD  . PRO   B 136 ? 0.2312 0.1706 0.2939 0.0357  -0.0025 0.0173  136 PRO   B CD  
6140 N  N   . ILE   B 137 ? 0.1954 0.1271 0.3020 0.0127  -0.0102 0.0156  137 ILE   B N   
6141 C  CA  . ILE   B 137 ? 0.2021 0.1271 0.3021 -0.0002 -0.0018 0.0124  137 ILE   B CA  
6142 C  C   . ILE   B 137 ? 0.1929 0.1296 0.2867 -0.0090 0.0095  0.0218  137 ILE   B C   
6143 O  O   . ILE   B 137 ? 0.1825 0.1323 0.2856 -0.0114 0.0064  0.0109  137 ILE   B O   
6144 C  CB  . ILE   B 137 ? 0.2270 0.1325 0.3443 -0.0053 -0.0010 0.0082  137 ILE   B CB  
6145 C  CG1 . ILE   B 137 ? 0.2527 0.1512 0.3843 0.0064  0.0041  -0.0057 137 ILE   B CG1 
6146 C  CG2 . ILE   B 137 ? 0.2294 0.1380 0.3568 -0.0276 -0.0020 0.0111  137 ILE   B CG2 
6147 C  CD1 . ILE   B 137 ? 0.2727 0.1816 0.4162 0.0224  -0.0008 -0.0006 137 ILE   B CD1 
6159 N  N   . HIS   B 138 ? 0.2002 0.1284 0.2880 -0.0066 0.0180  0.0261  138 HIS   B N   
6160 C  CA  . HIS   B 138 ? 0.2077 0.1384 0.2867 -0.0053 0.0337  0.0240  138 HIS   B CA  
6161 C  C   . HIS   B 138 ? 0.1881 0.1336 0.2763 -0.0053 0.0332  0.0267  138 HIS   B C   
6162 O  O   . HIS   B 138 ? 0.1767 0.1404 0.2952 -0.0012 0.0347  0.0400  138 HIS   B O   
6163 C  CB  . HIS   B 138 ? 0.2360 0.1507 0.2940 -0.0077 0.0537  0.0179  138 HIS   B CB  
6164 C  CG  . HIS   B 138 ? 0.2585 0.1687 0.3015 -0.0108 0.0759  0.0373  138 HIS   B CG  
6165 N  ND1 . HIS   B 138 ? 0.2679 0.1876 0.3281 -0.0081 0.0843  0.0325  138 HIS   B ND1 
6166 C  CD2 . HIS   B 138 ? 0.2719 0.1765 0.3031 -0.0085 0.0812  0.0287  138 HIS   B CD2 
6167 C  CE1 . HIS   B 138 ? 0.2721 0.1897 0.3266 -0.0071 0.0856  0.0306  138 HIS   B CE1 
6168 N  NE2 . HIS   B 138 ? 0.2786 0.1788 0.3089 -0.0003 0.0840  0.0215  138 HIS   B NE2 
6176 N  N   . SER   B 139 ? 0.1845 0.1279 0.2772 0.0019  0.0337  0.0187  139 SER   B N   
6177 C  CA  . SER   B 139 ? 0.1809 0.1219 0.2589 -0.0001 0.0341  0.0081  139 SER   B CA  
6178 C  C   . SER   B 139 ? 0.1577 0.1183 0.2513 0.0016  0.0234  0.0063  139 SER   B C   
6179 O  O   . SER   B 139 ? 0.1562 0.1183 0.2533 0.0008  0.0048  0.0138  139 SER   B O   
6180 C  CB  . SER   B 139 ? 0.1859 0.1222 0.2612 0.0015  0.0104  0.0087  139 SER   B CB  
6181 O  OG  . SER   B 139 ? 0.1831 0.1240 0.2626 -0.0007 -0.0041 0.0185  139 SER   B OG  
6187 N  N   . LEU   B 140 ? 0.1561 0.1150 0.2443 -0.0068 0.0233  -0.0002 140 LEU   B N   
6188 C  CA  . LEU   B 140 ? 0.1510 0.1162 0.2465 -0.0042 0.0155  0.0093  140 LEU   B CA  
6189 C  C   . LEU   B 140 ? 0.1441 0.1194 0.2621 -0.0028 -0.0009 -0.0003 140 LEU   B C   
6190 O  O   . LEU   B 140 ? 0.1450 0.1257 0.2591 -0.0034 0.0002  0.0087  140 LEU   B O   
6191 C  CB  . LEU   B 140 ? 0.1510 0.1164 0.2550 -0.0102 0.0184  -0.0025 140 LEU   B CB  
6192 C  CG  . LEU   B 140 ? 0.1572 0.1183 0.2506 -0.0119 -0.0010 0.0108  140 LEU   B CG  
6193 C  CD1 . LEU   B 140 ? 0.1694 0.1353 0.2576 -0.0112 0.0021  0.0057  140 LEU   B CD1 
6194 C  CD2 . LEU   B 140 ? 0.1784 0.1322 0.2730 -0.0133 -0.0034 -0.0144 140 LEU   B CD2 
6206 N  N   . ARG   B 141 ? 0.1363 0.1188 0.2772 -0.0111 0.0034  -0.0047 141 ARG   B N   
6207 C  CA  . ARG   B 141 ? 0.1430 0.1230 0.3090 -0.0151 0.0186  -0.0021 141 ARG   B CA  
6208 C  C   . ARG   B 141 ? 0.1361 0.1217 0.2927 -0.0156 0.0104  0.0010  141 ARG   B C   
6209 O  O   . ARG   B 141 ? 0.1439 0.1230 0.2866 -0.0133 0.0084  -0.0076 141 ARG   B O   
6210 C  CB  . ARG   B 141 ? 0.1635 0.1284 0.3261 -0.0192 0.0327  0.0030  141 ARG   B CB  
6211 C  CG  . ARG   B 141 ? 0.1933 0.1601 0.3352 -0.0166 0.0346  -0.0018 141 ARG   B CG  
6212 C  CD  . ARG   B 141 ? 0.2301 0.1860 0.3300 -0.0102 0.0135  -0.0138 141 ARG   B CD  
6213 N  NE  . ARG   B 141 ? 0.2503 0.1852 0.3219 -0.0286 0.0104  -0.0210 141 ARG   B NE  
6214 C  CZ  . ARG   B 141 ? 0.2637 0.1731 0.3086 -0.0263 0.0201  -0.0290 141 ARG   B CZ  
6215 N  NH1 . ARG   B 141 ? 0.2702 0.1607 0.3060 -0.0270 0.0191  -0.0258 141 ARG   B NH1 
6216 N  NH2 . ARG   B 141 ? 0.2743 0.1860 0.3168 -0.0152 0.0077  -0.0225 141 ARG   B NH2 
6230 N  N   . VAL   B 142 ? 0.1437 0.1187 0.2785 -0.0096 0.0124  0.0004  142 VAL   B N   
6231 C  CA  . VAL   B 142 ? 0.1373 0.1211 0.2769 -0.0049 0.0144  0.0017  142 VAL   B CA  
6232 C  C   . VAL   B 142 ? 0.1354 0.1195 0.2738 -0.0040 0.0079  0.0005  142 VAL   B C   
6233 O  O   . VAL   B 142 ? 0.1436 0.1193 0.2773 -0.0034 0.0086  -0.0009 142 VAL   B O   
6234 C  CB  . VAL   B 142 ? 0.1540 0.1319 0.2796 0.0007  0.0187  0.0112  142 VAL   B CB  
6235 C  CG1 . VAL   B 142 ? 0.1483 0.1303 0.2772 0.0033  0.0244  0.0043  142 VAL   B CG1 
6236 C  CG2 . VAL   B 142 ? 0.1703 0.1332 0.2917 0.0019  0.0176  0.0142  142 VAL   B CG2 
6246 N  N   . CYS   B 143 ? 0.1329 0.1197 0.2568 -0.0018 0.0066  0.0080  143 CYS   B N   
6247 C  CA  . CYS   B 143 ? 0.1312 0.1201 0.2630 -0.0080 0.0056  0.0064  143 CYS   B CA  
6248 C  C   . CYS   B 143 ? 0.1299 0.1219 0.2595 -0.0057 0.0062  -0.0034 143 CYS   B C   
6249 O  O   . CYS   B 143 ? 0.1322 0.1268 0.2581 -0.0058 -0.0046 -0.0013 143 CYS   B O   
6250 C  CB  . CYS   B 143 ? 0.1399 0.1277 0.2553 -0.0090 0.0019  0.0039  143 CYS   B CB  
6251 S  SG  . CYS   B 143 ? 0.1410 0.1433 0.2425 -0.0057 0.0058  0.0064  143 CYS   B SG  
6257 N  N   . VAL   B 144 ? 0.1357 0.1207 0.2703 -0.0076 -0.0018 -0.0168 144 VAL   B N   
6258 C  CA  . VAL   B 144 ? 0.1430 0.1314 0.2942 -0.0124 -0.0135 -0.0206 144 VAL   B CA  
6259 C  C   . VAL   B 144 ? 0.1366 0.1358 0.3039 -0.0094 -0.0164 -0.0019 144 VAL   B C   
6260 O  O   . VAL   B 144 ? 0.1500 0.1520 0.3167 0.0035  -0.0141 0.0154  144 VAL   B O   
6261 C  CB  . VAL   B 144 ? 0.1677 0.1443 0.3435 -0.0155 -0.0210 -0.0383 144 VAL   B CB  
6262 C  CG1 . VAL   B 144 ? 0.1886 0.1829 0.3663 -0.0050 -0.0213 -0.0334 144 VAL   B CG1 
6263 C  CG2 . VAL   B 144 ? 0.1822 0.1402 0.3381 0.0031  -0.0322 -0.0441 144 VAL   B CG2 
6273 N  N   . ASP   B 145 ? 0.1381 0.1272 0.3145 -0.0085 -0.0111 -0.0177 145 ASP   B N   
6274 C  CA  . ASP   B 145 ? 0.1388 0.1339 0.3246 -0.0054 -0.0001 -0.0060 145 ASP   B CA  
6275 C  C   . ASP   B 145 ? 0.1362 0.1338 0.3076 -0.0066 0.0031  -0.0085 145 ASP   B C   
6276 O  O   . ASP   B 145 ? 0.1412 0.1472 0.3585 -0.0133 0.0115  -0.0249 145 ASP   B O   
6277 C  CB  . ASP   B 145 ? 0.1519 0.1409 0.3540 -0.0187 0.0197  0.0013  145 ASP   B CB  
6278 C  CG  . ASP   B 145 ? 0.1645 0.1418 0.3954 -0.0252 0.0291  -0.0069 145 ASP   B CG  
6279 O  OD1 . ASP   B 145 ? 0.1683 0.1462 0.4003 -0.0241 -0.0007 -0.0162 145 ASP   B OD1 
6280 O  OD2 . ASP   B 145 ? 0.1959 0.1497 0.4355 -0.0300 0.0487  -0.0038 145 ASP   B OD2 
6285 N  N   . THR   B 146 ? 0.1282 0.1237 0.2652 -0.0114 0.0019  0.0041  146 THR   B N   
6286 C  CA  . THR   B 146 ? 0.1355 0.1217 0.2487 -0.0089 0.0075  0.0018  146 THR   B CA  
6287 C  C   . THR   B 146 ? 0.1313 0.1224 0.2389 -0.0046 0.0002  0.0045  146 THR   B C   
6288 O  O   . THR   B 146 ? 0.1364 0.1234 0.2458 -0.0047 -0.0017 0.0006  146 THR   B O   
6289 C  CB  . THR   B 146 ? 0.1396 0.1213 0.2561 -0.0086 0.0162  0.0048  146 THR   B CB  
6290 O  OG1 . THR   B 146 ? 0.1441 0.1204 0.2611 -0.0089 0.0201  0.0079  146 THR   B OG1 
6291 C  CG2 . THR   B 146 ? 0.1462 0.1277 0.2582 -0.0073 0.0141  0.0035  146 THR   B CG2 
6299 N  N   . VAL   B 147 ? 0.1385 0.1257 0.2211 -0.0024 0.0132  0.0027  147 VAL   B N   
6300 C  CA  . VAL   B 147 ? 0.1361 0.1214 0.2178 -0.0093 -0.0027 0.0002  147 VAL   B CA  
6301 C  C   . VAL   B 147 ? 0.1347 0.1247 0.2244 -0.0188 -0.0081 -0.0002 147 VAL   B C   
6302 O  O   . VAL   B 147 ? 0.1498 0.1348 0.2339 -0.0216 -0.0322 -0.0064 147 VAL   B O   
6303 C  CB  . VAL   B 147 ? 0.1418 0.1335 0.2163 -0.0090 -0.0112 0.0011  147 VAL   B CB  
6304 C  CG1 . VAL   B 147 ? 0.1421 0.1472 0.2065 -0.0121 -0.0080 0.0036  147 VAL   B CG1 
6305 C  CG2 . VAL   B 147 ? 0.1429 0.1295 0.2175 -0.0092 -0.0032 0.0022  147 VAL   B CG2 
6315 N  N   . ARG   B 148 ? 0.1373 0.1230 0.2207 -0.0091 -0.0196 -0.0034 148 ARG   B N   
6316 C  CA  . ARG   B 148 ? 0.1411 0.1345 0.2175 -0.0051 -0.0276 -0.0063 148 ARG   B CA  
6317 C  C   . ARG   B 148 ? 0.1433 0.1439 0.2056 -0.0098 -0.0273 -0.0056 148 ARG   B C   
6318 O  O   . ARG   B 148 ? 0.1669 0.1737 0.2115 -0.0242 -0.0391 0.0014  148 ARG   B O   
6319 C  CB  . ARG   B 148 ? 0.1436 0.1443 0.2240 -0.0013 -0.0278 -0.0148 148 ARG   B CB  
6320 C  CG  . ARG   B 148 ? 0.1471 0.1616 0.2452 -0.0109 -0.0248 -0.0294 148 ARG   B CG  
6321 C  CD  . ARG   B 148 ? 0.1488 0.1734 0.2508 0.0016  -0.0285 -0.0356 148 ARG   B CD  
6322 N  NE  . ARG   B 148 ? 0.1562 0.1701 0.2407 0.0173  -0.0334 -0.0341 148 ARG   B NE  
6323 C  CZ  . ARG   B 148 ? 0.1474 0.1620 0.2193 0.0136  -0.0205 -0.0217 148 ARG   B CZ  
6324 N  NH1 . ARG   B 148 ? 0.1442 0.1632 0.2245 -0.0044 -0.0023 -0.0174 148 ARG   B NH1 
6325 N  NH2 . ARG   B 148 ? 0.1643 0.1496 0.2085 0.0164  -0.0173 -0.0159 148 ARG   B NH2 
6339 N  N   . THR   B 149 ? 0.1458 0.1360 0.2095 -0.0123 -0.0282 -0.0017 149 THR   B N   
6340 C  CA  . THR   B 149 ? 0.1533 0.1417 0.1977 -0.0170 -0.0304 0.0054  149 THR   B CA  
6341 C  C   . THR   B 149 ? 0.1511 0.1374 0.1846 -0.0131 -0.0324 0.0056  149 THR   B C   
6342 O  O   . THR   B 149 ? 0.1605 0.1350 0.1960 -0.0180 -0.0173 0.0033  149 THR   B O   
6343 C  CB  . THR   B 149 ? 0.1589 0.1379 0.1994 -0.0148 -0.0338 0.0040  149 THR   B CB  
6344 O  OG1 . THR   B 149 ? 0.1590 0.1450 0.1958 -0.0262 -0.0335 0.0018  149 THR   B OG1 
6345 C  CG2 . THR   B 149 ? 0.1703 0.1423 0.2157 -0.0087 -0.0251 0.0038  149 THR   B CG2 
6353 N  N   . ASN   B 150 ? 0.1590 0.1403 0.1817 -0.0174 -0.0323 -0.0025 150 ASN   B N   
6354 C  CA  . ASN   B 150 ? 0.1652 0.1559 0.1743 -0.0206 -0.0339 -0.0055 150 ASN   B CA  
6355 C  C   . ASN   B 150 ? 0.1578 0.1467 0.1727 -0.0191 -0.0251 -0.0035 150 ASN   B C   
6356 O  O   . ASN   B 150 ? 0.1636 0.1434 0.1929 -0.0256 -0.0410 0.0013  150 ASN   B O   
6357 C  CB  . ASN   B 150 ? 0.1877 0.1890 0.1827 -0.0240 -0.0447 0.0092  150 ASN   B CB  
6358 C  CG  . ASN   B 150 ? 0.2161 0.2290 0.2168 -0.0217 -0.0495 0.0252  150 ASN   B CG  
6359 O  OD1 . ASN   B 150 ? 0.2236 0.2449 0.2288 -0.0330 -0.0587 0.0185  150 ASN   B OD1 
6360 N  ND2 . ASN   B 150 ? 0.2332 0.2500 0.2533 -0.0088 -0.0539 0.0604  150 ASN   B ND2 
6367 N  N   . VAL   B 151 ? 0.1493 0.1423 0.1815 -0.0184 -0.0329 0.0058  151 VAL   B N   
6368 C  CA  . VAL   B 151 ? 0.1500 0.1426 0.1858 -0.0236 -0.0207 -0.0026 151 VAL   B CA  
6369 C  C   . VAL   B 151 ? 0.1548 0.1395 0.1829 -0.0298 -0.0279 -0.0003 151 VAL   B C   
6370 O  O   . VAL   B 151 ? 0.1612 0.1468 0.1995 -0.0301 -0.0192 -0.0118 151 VAL   B O   
6371 C  CB  . VAL   B 151 ? 0.1696 0.1546 0.1956 -0.0094 -0.0217 -0.0023 151 VAL   B CB  
6372 C  CG1 . VAL   B 151 ? 0.1769 0.1623 0.2160 -0.0207 -0.0062 -0.0133 151 VAL   B CG1 
6373 C  CG2 . VAL   B 151 ? 0.1820 0.1640 0.1889 0.0001  -0.0180 0.0063  151 VAL   B CG2 
6383 N  N   . TYR   B 152 ? 0.1525 0.1269 0.1726 -0.0214 -0.0244 -0.0016 152 TYR   B N   
6384 C  CA  . TYR   B 152 ? 0.1517 0.1446 0.1572 -0.0292 -0.0161 -0.0091 152 TYR   B CA  
6385 C  C   . TYR   B 152 ? 0.1477 0.1329 0.1530 -0.0231 -0.0140 -0.0102 152 TYR   B C   
6386 O  O   . TYR   B 152 ? 0.1554 0.1336 0.1629 -0.0239 -0.0152 -0.0030 152 TYR   B O   
6387 C  CB  . TYR   B 152 ? 0.1686 0.1584 0.1557 -0.0310 -0.0125 0.0071  152 TYR   B CB  
6388 C  CG  . TYR   B 152 ? 0.1831 0.1647 0.1520 -0.0423 -0.0166 0.0025  152 TYR   B CG  
6389 C  CD1 . TYR   B 152 ? 0.1936 0.1789 0.1435 -0.0346 -0.0220 0.0059  152 TYR   B CD1 
6390 C  CD2 . TYR   B 152 ? 0.2053 0.1826 0.1583 -0.0448 -0.0184 -0.0011 152 TYR   B CD2 
6391 C  CE1 . TYR   B 152 ? 0.2101 0.1995 0.1618 -0.0312 -0.0314 0.0213  152 TYR   B CE1 
6392 C  CE2 . TYR   B 152 ? 0.2185 0.2041 0.1582 -0.0426 -0.0257 -0.0117 152 TYR   B CE2 
6393 C  CZ  . TYR   B 152 ? 0.2202 0.2186 0.1552 -0.0372 -0.0433 0.0170  152 TYR   B CZ  
6394 O  OH  . TYR   B 152 ? 0.2413 0.2527 0.1942 -0.0249 -0.0437 0.0142  152 TYR   B OH  
6404 N  N   . LEU   B 153 ? 0.1528 0.1276 0.1638 -0.0335 -0.0156 -0.0046 153 LEU   B N   
6405 C  CA  . LEU   B 153 ? 0.1527 0.1223 0.1502 -0.0227 -0.0078 -0.0085 153 LEU   B CA  
6406 C  C   . LEU   B 153 ? 0.1572 0.1239 0.1742 -0.0256 -0.0028 -0.0127 153 LEU   B C   
6407 O  O   . LEU   B 153 ? 0.1662 0.1469 0.1847 -0.0132 -0.0041 -0.0344 153 LEU   B O   
6408 C  CB  . LEU   B 153 ? 0.1563 0.1281 0.1718 -0.0239 -0.0076 -0.0087 153 LEU   B CB  
6409 C  CG  . LEU   B 153 ? 0.1540 0.1360 0.2003 -0.0254 -0.0057 -0.0022 153 LEU   B CG  
6410 C  CD1 . LEU   B 153 ? 0.1571 0.1517 0.2125 -0.0274 0.0011  0.0062  153 LEU   B CD1 
6411 C  CD2 . LEU   B 153 ? 0.1625 0.1480 0.2079 -0.0314 0.0101  0.0011  153 LEU   B CD2 
6423 N  N   . ALA   B 154 ? 0.1487 0.1253 0.1797 -0.0089 -0.0133 -0.0127 154 ALA   B N   
6424 C  CA  . ALA   B 154 ? 0.1592 0.1388 0.2082 -0.0029 -0.0121 -0.0138 154 ALA   B CA  
6425 C  C   . ALA   B 154 ? 0.1673 0.1388 0.2123 0.0037  -0.0198 -0.0227 154 ALA   B C   
6426 O  O   . ALA   B 154 ? 0.1973 0.1421 0.2260 0.0043  -0.0056 -0.0035 154 ALA   B O   
6427 C  CB  . ALA   B 154 ? 0.1560 0.1521 0.2264 -0.0068 -0.0121 -0.0237 154 ALA   B CB  
6433 N  N   . VAL   B 155 ? 0.1399 0.1348 0.2249 -0.0018 -0.0056 -0.0165 155 VAL   B N   
6434 C  CA  . VAL   B 155 ? 0.1353 0.1321 0.2358 -0.0010 -0.0080 -0.0096 155 VAL   B CA  
6435 C  C   . VAL   B 155 ? 0.1376 0.1313 0.2290 -0.0055 -0.0101 -0.0211 155 VAL   B C   
6436 O  O   . VAL   B 155 ? 0.1586 0.1472 0.2665 0.0007  -0.0060 -0.0424 155 VAL   B O   
6437 C  CB  . VAL   B 155 ? 0.1407 0.1507 0.2662 -0.0054 -0.0191 0.0035  155 VAL   B CB  
6438 C  CG1 . VAL   B 155 ? 0.1478 0.1469 0.2625 -0.0134 -0.0165 0.0033  155 VAL   B CG1 
6439 C  CG2 . VAL   B 155 ? 0.1378 0.1596 0.2941 -0.0078 -0.0165 0.0310  155 VAL   B CG2 
6449 N  N   . PHE   B 156 ? 0.1276 0.1402 0.2437 0.0021  -0.0033 -0.0186 156 PHE   B N   
6450 C  CA  . PHE   B 156 ? 0.1386 0.1455 0.2765 0.0019  -0.0054 -0.0174 156 PHE   B CA  
6451 C  C   . PHE   B 156 ? 0.1377 0.1563 0.3161 0.0084  -0.0062 -0.0337 156 PHE   B C   
6452 O  O   . PHE   B 156 ? 0.1584 0.1781 0.3403 0.0224  0.0016  -0.0431 156 PHE   B O   
6453 C  CB  . PHE   B 156 ? 0.1470 0.1432 0.2779 -0.0013 -0.0082 -0.0114 156 PHE   B CB  
6454 C  CG  . PHE   B 156 ? 0.1471 0.1535 0.2876 -0.0022 -0.0080 0.0049  156 PHE   B CG  
6455 C  CD1 . PHE   B 156 ? 0.1508 0.1790 0.3215 0.0067  0.0025  0.0356  156 PHE   B CD1 
6456 C  CD2 . PHE   B 156 ? 0.1511 0.1642 0.2813 0.0065  -0.0110 0.0073  156 PHE   B CD2 
6457 C  CE1 . PHE   B 156 ? 0.1545 0.1935 0.3345 0.0045  0.0009  0.0347  156 PHE   B CE1 
6458 C  CE2 . PHE   B 156 ? 0.1613 0.1873 0.3074 0.0104  -0.0138 0.0130  156 PHE   B CE2 
6459 C  CZ  . PHE   B 156 ? 0.1533 0.1945 0.3288 0.0151  -0.0180 0.0228  156 PHE   B CZ  
6469 N  N   . ASP   B 157 ? 0.1397 0.1492 0.3417 0.0098  -0.0182 -0.0187 157 ASP   B N   
6470 C  CA  . ASP   B 157 ? 0.1478 0.1566 0.3683 0.0110  -0.0222 -0.0271 157 ASP   B CA  
6471 C  C   . ASP   B 157 ? 0.1531 0.1522 0.3784 0.0115  -0.0186 -0.0477 157 ASP   B C   
6472 O  O   . ASP   B 157 ? 0.1421 0.1494 0.3595 0.0052  -0.0146 -0.0405 157 ASP   B O   
6473 C  CB  . ASP   B 157 ? 0.1727 0.1757 0.3779 0.0063  -0.0384 -0.0118 157 ASP   B CB  
6474 C  CG  . ASP   B 157 ? 0.2061 0.1867 0.3954 0.0028  -0.0205 -0.0102 157 ASP   B CG  
6475 O  OD1 . ASP   B 157 ? 0.2177 0.1751 0.4102 0.0102  -0.0152 -0.0074 157 ASP   B OD1 
6476 O  OD2 . ASP   B 157 ? 0.2300 0.2055 0.4162 0.0003  -0.0073 -0.0035 157 ASP   B OD2 
6481 N  N   . LYS   B 158 ? 0.1575 0.1769 0.3904 0.0116  -0.0082 -0.0726 158 LYS   B N   
6482 C  CA  . LYS   B 158 ? 0.1747 0.1933 0.3937 0.0066  0.0010  -0.0909 158 LYS   B CA  
6483 C  C   . LYS   B 158 ? 0.1751 0.1805 0.4022 0.0107  -0.0104 -0.0830 158 LYS   B C   
6484 O  O   . LYS   B 158 ? 0.1793 0.1800 0.4049 -0.0060 -0.0085 -0.0846 158 LYS   B O   
6485 C  CB  . LYS   B 158 ? 0.1989 0.2324 0.3921 0.0045  0.0117  -0.1067 158 LYS   B CB  
6486 C  CG  . LYS   B 158 ? 0.2328 0.2731 0.3952 0.0063  0.0209  -0.1120 158 LYS   B CG  
6487 C  CD  . LYS   B 158 ? 0.2578 0.3125 0.4011 0.0034  0.0271  -0.1060 158 LYS   B CD  
6488 C  CE  . LYS   B 158 ? 0.2795 0.3399 0.4140 0.0042  0.0270  -0.1017 158 LYS   B CE  
6489 N  NZ  . LYS   B 158 ? 0.2799 0.3534 0.4158 0.0018  0.0271  -0.1008 158 LYS   B NZ  
6503 N  N   . ASN   B 159 ? 0.1716 0.1699 0.4149 0.0094  -0.0266 -0.0742 159 ASN   B N   
6504 C  CA  . ASN   B 159 ? 0.1857 0.1632 0.4240 0.0158  -0.0367 -0.0581 159 ASN   B CA  
6505 C  C   . ASN   B 159 ? 0.1733 0.1509 0.4164 0.0105  -0.0478 -0.0413 159 ASN   B C   
6506 O  O   . ASN   B 159 ? 0.1713 0.1440 0.4352 -0.0036 -0.0536 -0.0282 159 ASN   B O   
6507 C  CB  . ASN   B 159 ? 0.2081 0.1784 0.4414 0.0257  -0.0404 -0.0558 159 ASN   B CB  
6508 C  CG  . ASN   B 159 ? 0.2353 0.2058 0.4614 0.0254  -0.0485 -0.0642 159 ASN   B CG  
6509 O  OD1 . ASN   B 159 ? 0.2508 0.2077 0.4686 0.0342  -0.0509 -0.0718 159 ASN   B OD1 
6510 N  ND2 . ASN   B 159 ? 0.2366 0.2159 0.4795 0.0266  -0.0504 -0.0589 159 ASN   B ND2 
6517 N  N   . LEU   B 160 ? 0.1585 0.1493 0.3875 0.0029  -0.0440 -0.0342 160 LEU   B N   
6518 C  CA  . LEU   B 160 ? 0.1564 0.1477 0.3521 0.0091  -0.0358 -0.0125 160 LEU   B CA  
6519 C  C   . LEU   B 160 ? 0.1495 0.1379 0.3437 -0.0017 -0.0262 -0.0248 160 LEU   B C   
6520 O  O   . LEU   B 160 ? 0.1427 0.1452 0.3405 -0.0036 -0.0272 -0.0192 160 LEU   B O   
6521 C  CB  . LEU   B 160 ? 0.1557 0.1568 0.3336 0.0087  -0.0342 0.0031  160 LEU   B CB  
6522 C  CG  . LEU   B 160 ? 0.1562 0.1699 0.3110 0.0083  -0.0354 0.0050  160 LEU   B CG  
6523 C  CD1 . LEU   B 160 ? 0.1739 0.1898 0.3087 -0.0055 -0.0312 0.0025  160 LEU   B CD1 
6524 C  CD2 . LEU   B 160 ? 0.1600 0.1779 0.3095 0.0190  -0.0274 -0.0109 160 LEU   B CD2 
6536 N  N   . TYR   B 161 ? 0.1461 0.1469 0.3544 -0.0097 -0.0045 -0.0403 161 TYR   B N   
6537 C  CA  . TYR   B 161 ? 0.1542 0.1480 0.3419 -0.0181 0.0113  -0.0502 161 TYR   B CA  
6538 C  C   . TYR   B 161 ? 0.1648 0.1493 0.3306 -0.0134 0.0156  -0.0443 161 TYR   B C   
6539 O  O   . TYR   B 161 ? 0.1683 0.1461 0.3188 -0.0224 0.0065  -0.0404 161 TYR   B O   
6540 C  CB  . TYR   B 161 ? 0.1685 0.1594 0.3417 -0.0264 0.0328  -0.0539 161 TYR   B CB  
6541 C  CG  . TYR   B 161 ? 0.1965 0.1634 0.3269 -0.0303 0.0421  -0.0611 161 TYR   B CG  
6542 C  CD1 . TYR   B 161 ? 0.2042 0.1644 0.3207 -0.0390 0.0465  -0.0576 161 TYR   B CD1 
6543 C  CD2 . TYR   B 161 ? 0.2168 0.1705 0.3128 -0.0243 0.0390  -0.0635 161 TYR   B CD2 
6544 C  CE1 . TYR   B 161 ? 0.2225 0.1840 0.3220 -0.0417 0.0416  -0.0589 161 TYR   B CE1 
6545 C  CE2 . TYR   B 161 ? 0.2382 0.1904 0.3240 -0.0305 0.0370  -0.0600 161 TYR   B CE2 
6546 C  CZ  . TYR   B 161 ? 0.2388 0.1956 0.3215 -0.0475 0.0298  -0.0561 161 TYR   B CZ  
6547 O  OH  . TYR   B 161 ? 0.2667 0.2178 0.3413 -0.0498 0.0268  -0.0531 161 TYR   B OH  
6557 N  N   . ASP   B 162 ? 0.1685 0.1436 0.3420 -0.0126 0.0044  -0.0572 162 ASP   B N   
6558 C  CA  . ASP   B 162 ? 0.1774 0.1527 0.3460 -0.0064 -0.0039 -0.0509 162 ASP   B CA  
6559 C  C   . ASP   B 162 ? 0.1720 0.1432 0.3382 -0.0101 -0.0132 -0.0397 162 ASP   B C   
6560 O  O   . ASP   B 162 ? 0.1798 0.1496 0.3360 -0.0149 -0.0260 -0.0307 162 ASP   B O   
6561 C  CB  . ASP   B 162 ? 0.1963 0.1707 0.3633 -0.0022 -0.0119 -0.0735 162 ASP   B CB  
6562 C  CG  . ASP   B 162 ? 0.1993 0.1975 0.3853 0.0030  -0.0131 -0.0839 162 ASP   B CG  
6563 O  OD1 . ASP   B 162 ? 0.1996 0.2157 0.3816 -0.0049 0.0074  -0.0809 162 ASP   B OD1 
6564 O  OD2 . ASP   B 162 ? 0.2133 0.2159 0.4089 0.0227  -0.0061 -0.0799 162 ASP   B OD2 
6569 N  N   . LYS   B 163 ? 0.1691 0.1312 0.3312 -0.0061 -0.0253 -0.0228 163 LYS   B N   
6570 C  CA  . LYS   B 163 ? 0.1789 0.1413 0.3376 -0.0129 -0.0215 -0.0042 163 LYS   B CA  
6571 C  C   . LYS   B 163 ? 0.1523 0.1374 0.3221 -0.0158 -0.0208 0.0008  163 LYS   B C   
6572 O  O   . LYS   B 163 ? 0.1494 0.1460 0.3484 -0.0168 -0.0236 0.0039  163 LYS   B O   
6573 C  CB  . LYS   B 163 ? 0.2226 0.1723 0.3747 -0.0088 -0.0315 0.0146  163 LYS   B CB  
6574 C  CG  . LYS   B 163 ? 0.2953 0.2535 0.4298 -0.0132 -0.0160 0.0150  163 LYS   B CG  
6575 C  CD  . LYS   B 163 ? 0.3522 0.3222 0.4861 -0.0222 -0.0101 0.0075  163 LYS   B CD  
6576 C  CE  . LYS   B 163 ? 0.3989 0.3703 0.5247 -0.0299 -0.0035 0.0041  163 LYS   B CE  
6577 N  NZ  . LYS   B 163 ? 0.4266 0.4098 0.5499 -0.0339 0.0005  -0.0015 163 LYS   B NZ  
6591 N  N   . LEU   B 164 ? 0.1393 0.1325 0.2938 -0.0141 -0.0184 -0.0025 164 LEU   B N   
6592 C  CA  . LEU   B 164 ? 0.1459 0.1343 0.2770 -0.0123 -0.0249 0.0006  164 LEU   B CA  
6593 C  C   . LEU   B 164 ? 0.1517 0.1325 0.2802 -0.0178 -0.0296 0.0013  164 LEU   B C   
6594 O  O   . LEU   B 164 ? 0.1552 0.1582 0.2954 -0.0148 -0.0339 0.0030  164 LEU   B O   
6595 C  CB  . LEU   B 164 ? 0.1407 0.1324 0.2635 -0.0114 -0.0259 -0.0045 164 LEU   B CB  
6596 C  CG  . LEU   B 164 ? 0.1495 0.1459 0.2769 -0.0097 -0.0124 0.0009  164 LEU   B CG  
6597 C  CD1 . LEU   B 164 ? 0.1549 0.1435 0.2769 -0.0120 -0.0161 -0.0143 164 LEU   B CD1 
6598 C  CD2 . LEU   B 164 ? 0.1683 0.1772 0.2881 -0.0122 0.0032  -0.0150 164 LEU   B CD2 
6610 N  N   . VAL   B 165 ? 0.1845 0.1427 0.3003 -0.0248 -0.0361 -0.0082 165 VAL   B N   
6611 C  CA  . VAL   B 165 ? 0.2197 0.1529 0.3085 -0.0328 -0.0518 -0.0065 165 VAL   B CA  
6612 C  C   . VAL   B 165 ? 0.2483 0.1641 0.3360 -0.0390 -0.0773 -0.0073 165 VAL   B C   
6613 O  O   . VAL   B 165 ? 0.2689 0.1787 0.3458 -0.0447 -0.0821 0.0043  165 VAL   B O   
6614 C  CB  . VAL   B 165 ? 0.2393 0.1700 0.3053 -0.0154 -0.0227 -0.0141 165 VAL   B CB  
6615 C  CG1 . VAL   B 165 ? 0.2537 0.1824 0.3254 -0.0151 -0.0158 -0.0147 165 VAL   B CG1 
6616 C  CG2 . VAL   B 165 ? 0.2338 0.1733 0.2959 -0.0110 -0.0109 -0.0100 165 VAL   B CG2 
6626 N  N   . SER   B 166 ? 0.2550 0.1531 0.3655 -0.0388 -0.0842 -0.0304 166 SER   B N   
6627 C  CA  . SER   B 166 ? 0.2486 0.1560 0.4087 -0.0371 -0.0705 -0.0346 166 SER   B CA  
6628 C  C   . SER   B 166 ? 0.2337 0.1649 0.4224 -0.0361 -0.0748 -0.0092 166 SER   B C   
6629 O  O   . SER   B 166 ? 0.2361 0.1851 0.4471 -0.0469 -0.0870 -0.0322 166 SER   B O   
6630 C  CB  . SER   B 166 ? 0.2476 0.1673 0.4326 -0.0279 -0.0644 -0.0424 166 SER   B CB  
6631 O  OG  . SER   B 166 ? 0.2365 0.1630 0.4476 -0.0216 -0.0698 -0.0255 166 SER   B OG  
6637 N  N   . SER   B 167 ? 0.2146 0.1558 0.4004 -0.0385 -0.0763 0.0252  167 SER   B N   
6638 C  CA  . SER   B 167 ? 0.2007 0.1659 0.3740 -0.0357 -0.0617 0.0232  167 SER   B CA  
6639 C  C   . SER   B 167 ? 0.1967 0.1732 0.3545 -0.0470 -0.0555 0.0410  167 SER   B C   
6640 O  O   . SER   B 167 ? 0.1969 0.1838 0.3604 -0.0529 -0.0474 0.0405  167 SER   B O   
6641 C  CB  . SER   B 167 ? 0.1896 0.1779 0.3732 -0.0322 -0.0311 0.0208  167 SER   B CB  
6642 O  OG  . SER   B 167 ? 0.1795 0.1902 0.3646 -0.0227 -0.0127 0.0192  167 SER   B OG  
6648 N  N   . PHE   B 168 ? 0.1970 0.1706 0.3414 -0.0425 -0.0365 0.0518  168 PHE   B N   
6649 C  CA  . PHE   B 168 ? 0.2036 0.1718 0.3228 -0.0462 -0.0298 0.0315  168 PHE   B CA  
6650 C  C   . PHE   B 168 ? 0.1770 0.1589 0.2839 -0.0256 -0.0157 0.0132  168 PHE   B C   
6651 O  O   . PHE   B 168 ? 0.2048 0.1514 0.2743 -0.0019 -0.0164 0.0009  168 PHE   B O   
6652 C  CB  . PHE   B 168 ? 0.2223 0.1783 0.3257 -0.0549 -0.0486 0.0399  168 PHE   B CB  
6653 C  CG  . PHE   B 168 ? 0.2488 0.1645 0.3123 -0.0574 -0.0561 0.0165  168 PHE   B CG  
6654 C  CD1 . PHE   B 168 ? 0.2755 0.1703 0.3217 -0.0517 -0.0560 0.0154  168 PHE   B CD1 
6655 C  CD2 . PHE   B 168 ? 0.2421 0.1560 0.3075 -0.0499 -0.0556 0.0222  168 PHE   B CD2 
6656 C  CE1 . PHE   B 168 ? 0.2871 0.1768 0.3160 -0.0392 -0.0466 0.0179  168 PHE   B CE1 
6657 C  CE2 . PHE   B 168 ? 0.2676 0.1623 0.3091 -0.0366 -0.0601 0.0159  168 PHE   B CE2 
6658 C  CZ  . PHE   B 168 ? 0.2790 0.1600 0.3131 -0.0252 -0.0586 0.0269  168 PHE   B CZ  
6668 N  N   . LEU   B 169 ? 0.1769 0.1711 0.2732 -0.0022 -0.0059 -0.0002 169 LEU   B N   
6669 C  CA  . LEU   B 169 ? 0.1983 0.2045 0.3019 -0.0063 -0.0029 -0.0235 169 LEU   B CA  
6670 C  C   . LEU   B 169 ? 0.2255 0.2286 0.3476 0.0085  -0.0067 -0.0495 169 LEU   B C   
6671 O  O   . LEU   B 169 ? 0.2468 0.2467 0.3960 0.0039  -0.0070 -0.0680 169 LEU   B O   
6672 C  CB  . LEU   B 169 ? 0.2201 0.2437 0.3135 -0.0114 -0.0020 -0.0036 169 LEU   B CB  
6673 C  CG  . LEU   B 169 ? 0.2558 0.2779 0.3404 -0.0013 0.0020  -0.0017 169 LEU   B CG  
6674 C  CD1 . LEU   B 169 ? 0.2695 0.2950 0.3428 -0.0020 -0.0009 0.0123  169 LEU   B CD1 
6675 C  CD2 . LEU   B 169 ? 0.2486 0.2818 0.3325 0.0156  0.0201  -0.0170 169 LEU   B CD2 
6676 O  OXT . LEU   B 169 ? 0.2467 0.2427 0.3456 0.0323  0.0023  -0.0552 169 LEU   B OXT 
6688 C  C1  T TFA   C .   ? 0.1392 0.1609 0.1333 -0.0077 0.0282  0.0204  201 TFA   A C1  
6689 C  C2  T TFA   C .   ? 0.1608 0.1820 0.1697 -0.0207 0.0145  0.0083  201 TFA   A C2  
6690 O  O   T TFA   C .   ? 0.1241 0.1443 0.1195 -0.0145 0.0302  0.0204  201 TFA   A O   
6691 F  F1  T TFA   C .   ? 0.1715 0.1895 0.2003 -0.0212 0.0011  0.0047  201 TFA   A F1  
6692 F  F2  T TFA   C .   ? 0.1740 0.1839 0.1684 -0.0207 0.0200  0.0136  201 TFA   A F2  
6693 F  F3  T TFA   C .   ? 0.1649 0.1990 0.1908 -0.0325 0.0245  -0.0010 201 TFA   A F3  
6694 O  OXT T TFA   C .   ? 0.1407 0.1559 0.1436 0.0234  0.0261  0.0179  201 TFA   A OXT 
6695 N  N2  B A1A9W D .   ? 0.1433 0.1635 0.1861 -0.0067 0.0019  0.0186  202 A1A9W A N2  
6696 C  C3  B A1A9W D .   ? 0.1437 0.1636 0.1806 -0.0073 0.0021  0.0220  202 A1A9W A C3  
6697 C  C6  B A1A9W D .   ? 0.1391 0.1549 0.1797 -0.0011 -0.0004 0.0345  202 A1A9W A C6  
6698 C  C9  B A1A9W D .   ? 0.1823 0.1864 0.2233 -0.0074 0.0102  0.0059  202 A1A9W A C9  
6699 C  C12 B A1A9W D .   ? 0.2001 0.1927 0.2366 -0.0085 0.0131  0.0044  202 A1A9W A C12 
6700 C  C1  B A1A9W D .   ? 0.1471 0.1691 0.1843 0.0038  0.0000  0.0189  202 A1A9W A C1  
6701 C  C10 B A1A9W D .   ? 0.1975 0.1947 0.2330 -0.0128 0.0086  -0.0017 202 A1A9W A C10 
6702 C  C11 B A1A9W D .   ? 0.2111 0.1999 0.2435 -0.0128 0.0130  -0.0004 202 A1A9W A C11 
6703 C  C2  B A1A9W D .   ? 0.1543 0.1725 0.1941 -0.0062 0.0079  0.0158  202 A1A9W A C2  
6704 C  C4  B A1A9W D .   ? 0.1439 0.1564 0.1850 -0.0016 0.0025  0.0267  202 A1A9W A C4  
6705 C  C5  B A1A9W D .   ? 0.1349 0.1476 0.1782 -0.0019 0.0017  0.0357  202 A1A9W A C5  
6706 C  C7  B A1A9W D .   ? 0.1325 0.1573 0.1803 0.0099  0.0026  0.0331  202 A1A9W A C7  
6707 C  C8  B A1A9W D .   ? 0.1225 0.1536 0.1799 0.0052  -0.0070 0.0358  202 A1A9W A C8  
6708 N  N1  B A1A9W D .   ? 0.1467 0.1705 0.1853 -0.0115 0.0075  0.0115  202 A1A9W A N1  
6709 N  N3  B A1A9W D .   ? 0.1418 0.1498 0.1814 -0.0019 -0.0002 0.0343  202 A1A9W A N3  
6710 N  N4  B A1A9W D .   ? 0.1260 0.1417 0.1728 0.0059  -0.0014 0.0400  202 A1A9W A N4  
6711 O  O1  B A1A9W D .   ? 0.1339 0.1594 0.1673 0.0074  0.0022  0.0184  202 A1A9W A O1  
6712 O  O2  B A1A9W D .   ? 0.2129 0.1988 0.2445 -0.0131 0.0172  0.0057  202 A1A9W A O2  
6729 CL CL  B CL    E .   ? 0.1547 0.1154 0.2006 -0.0090 -0.0209 0.0117  203 CL    A CL  
6730 O  O   . HOH   F .   ? 0.4093 0.7812 0.5030 -0.1126 0.0427  0.0969  301 HOH   A O   
6731 O  O   . HOH   F .   ? 0.3162 0.2269 0.3672 -0.0344 -0.0566 0.0378  302 HOH   A O   
6732 O  O   . HOH   F .   ? 0.3037 0.2688 0.4371 -0.0407 -0.1256 0.1202  303 HOH   A O   
6733 O  O   . HOH   F .   ? 0.6843 0.6284 0.4226 -0.1545 -0.0228 0.2320  304 HOH   A O   
6734 O  O   . HOH   F .   ? 0.5282 0.5466 0.5199 0.0366  0.0677  0.0029  305 HOH   A O   
6735 O  O   . HOH   F .   ? 0.6164 0.6213 0.6693 -0.1293 0.0055  -0.1294 306 HOH   A O   
6736 O  O   . HOH   F .   ? 0.4763 0.3663 0.4479 -0.0370 0.1191  -0.0372 307 HOH   A O   
6737 O  O   . HOH   F .   ? 0.5803 0.6110 0.5386 -0.1073 -0.1289 -0.1029 308 HOH   A O   
6738 O  O   . HOH   F .   ? 0.3112 0.5962 0.5695 -0.0730 -0.0907 0.2210  309 HOH   A O   
6739 O  O   . HOH   F .   ? 0.5591 0.4802 0.3289 0.1726  -0.1315 0.0500  310 HOH   A O   
6740 O  O   B HOH   F .   ? 0.3038 0.4033 0.2707 0.0719  0.0675  -0.0068 311 HOH   A O   
6741 O  O   . HOH   F .   ? 0.5128 0.2491 0.2870 -0.1048 0.0460  0.0315  312 HOH   A O   
6742 O  O   . HOH   F .   ? 0.1708 0.1664 0.2180 0.0148  -0.0273 0.0232  313 HOH   A O   
6743 O  O   . HOH   F .   ? 0.2248 0.2556 0.2206 -0.0413 0.0369  0.0481  314 HOH   A O   
6744 O  O   . HOH   F .   ? 0.2725 0.5603 0.3855 0.0023  -0.0578 0.0667  315 HOH   A O   
6745 O  O   B HOH   F .   ? 0.2270 0.1617 0.2780 0.0312  0.0153  -0.0132 316 HOH   A O   
6746 O  O   . HOH   F .   ? 0.5980 0.3903 0.5180 -0.0581 0.1816  0.1021  317 HOH   A O   
6747 O  O   . HOH   F .   ? 0.3549 0.3612 0.2876 -0.1438 -0.0096 0.1061  318 HOH   A O   
6748 O  O   . HOH   F .   ? 0.3112 0.3288 0.1674 -0.0467 0.0438  0.0502  319 HOH   A O   
6749 O  O   . HOH   F .   ? 0.2105 0.1841 0.3534 -0.0415 0.0156  -0.0198 320 HOH   A O   
6750 O  O   . HOH   F .   ? 0.5120 0.4028 0.5476 0.0808  0.1072  -0.1545 321 HOH   A O   
6751 O  O   B HOH   F .   ? 0.2022 0.1654 0.1726 0.0531  -0.0553 0.0494  322 HOH   A O   
6752 O  O   . HOH   F .   ? 0.6050 0.5512 0.4991 -0.1300 0.0110  0.2037  323 HOH   A O   
6753 O  O   . HOH   F .   ? 0.5936 0.4502 0.5964 0.0144  -0.0229 0.0010  324 HOH   A O   
6754 O  O   . HOH   F .   ? 0.5513 0.4668 0.4840 -0.0698 0.1257  0.2221  325 HOH   A O   
6755 O  O   . HOH   F .   ? 0.1727 0.3205 0.3128 0.0431  -0.0109 -0.0078 326 HOH   A O   
6756 O  O   . HOH   F .   ? 0.4358 0.4421 0.3795 0.1640  -0.0669 -0.1584 327 HOH   A O   
6757 O  O   . HOH   F .   ? 0.5907 0.3325 0.3587 -0.0782 -0.0725 0.0445  328 HOH   A O   
6758 O  O   B HOH   F .   ? 0.1916 0.2493 0.2043 -0.0195 -0.0004 0.0175  329 HOH   A O   
6759 O  O   . HOH   F .   ? 0.4490 0.5357 0.6354 0.1719  0.1241  -0.1023 330 HOH   A O   
6760 O  O   . HOH   F .   ? 0.3743 0.4356 0.4057 -0.0607 0.1887  0.0423  331 HOH   A O   
6761 O  O   . HOH   F .   ? 0.6551 0.5802 0.3849 -0.0714 -0.0345 0.1448  332 HOH   A O   
6762 O  O   B HOH   F .   ? 0.1912 0.1838 0.1560 0.0460  -0.0807 -0.0752 333 HOH   A O   
6763 O  O   . HOH   F .   ? 0.1556 0.4473 0.2516 -0.0130 0.0289  0.0630  334 HOH   A O   
6764 O  O   . HOH   F .   ? 0.4897 0.5906 0.4507 -0.0293 -0.1218 -0.1234 335 HOH   A O   
6765 O  O   . HOH   F .   ? 0.1535 0.1500 0.2422 -0.0208 0.0061  0.0149  336 HOH   A O   
6766 O  O   . HOH   F .   ? 0.4452 0.4060 0.4076 -0.1937 -0.0986 0.1911  337 HOH   A O   
6767 O  O   . HOH   F .   ? 0.3776 0.5108 0.5440 0.0569  -0.0197 0.1376  338 HOH   A O   
6768 O  O   . HOH   F .   ? 0.2399 0.2125 0.2357 -0.0296 0.0177  -0.0147 339 HOH   A O   
6769 O  O   . HOH   F .   ? 0.5475 0.5662 0.5360 0.0619  0.2511  -0.1000 340 HOH   A O   
6770 O  O   . HOH   F .   ? 0.3472 0.4592 0.2499 -0.0522 0.0741  0.0253  341 HOH   A O   
6771 O  O   . HOH   F .   ? 0.2386 0.2269 0.2815 0.0374  0.0306  0.0592  342 HOH   A O   
6772 O  O   . HOH   F .   ? 0.2179 0.4275 0.3919 -0.0247 -0.0627 0.1654  343 HOH   A O   
6773 O  O   . HOH   F .   ? 0.2682 0.3758 0.3682 -0.0792 -0.0557 -0.0339 344 HOH   A O   
6774 O  O   . HOH   F .   ? 0.5105 0.2098 0.4844 0.0572  -0.0089 0.0084  345 HOH   A O   
6775 O  O   . HOH   F .   ? 0.2284 0.4093 0.3682 0.0852  -0.0663 -0.0169 346 HOH   A O   
6776 O  O   . HOH   F .   ? 0.2076 0.1629 0.1640 -0.0073 0.0166  0.0228  347 HOH   A O   
6777 O  O   A HOH   F .   ? 0.1399 0.1885 0.1925 0.0343  0.0302  0.0478  348 HOH   A O   
6778 O  O   . HOH   F .   ? 0.1909 0.3363 0.3982 -0.0347 0.0339  -0.1041 349 HOH   A O   
6779 O  O   . HOH   F .   ? 0.3359 0.2731 0.3557 -0.0826 0.0034  -0.0195 350 HOH   A O   
6780 O  O   . HOH   F .   ? 0.4804 0.2017 0.4364 0.0306  -0.1525 0.0568  351 HOH   A O   
6781 O  O   . HOH   F .   ? 0.5176 0.4770 0.2832 -0.0961 0.1533  0.0802  352 HOH   A O   
6782 O  O   A HOH   F .   ? 0.1887 0.1413 0.2312 -0.0135 -0.0629 0.0170  353 HOH   A O   
6783 O  O   . HOH   F .   ? 0.3023 0.3169 0.4647 -0.0631 -0.1032 -0.0697 354 HOH   A O   
6784 O  O   A HOH   F .   ? 0.1970 0.2577 0.2220 0.0254  0.0143  0.0101  355 HOH   A O   
6785 O  O   . HOH   F .   ? 0.1510 0.2132 0.2203 0.0040  -0.0083 0.0453  356 HOH   A O   
6786 O  O   . HOH   F .   ? 0.1942 0.1984 0.4146 0.0165  0.1051  -0.0129 357 HOH   A O   
6787 O  O   A HOH   F .   ? 0.2834 0.1841 0.2077 0.0078  -0.0151 0.0045  358 HOH   A O   
6788 O  O   . HOH   F .   ? 0.3595 0.3825 0.4032 0.1626  0.0560  0.0389  359 HOH   A O   
6789 O  O   . HOH   F .   ? 0.2102 0.1635 0.2354 0.0163  -0.0335 0.0021  360 HOH   A O   
6790 O  O   A HOH   F .   ? 0.1982 0.2899 0.4117 0.0221  0.1026  0.1522  361 HOH   A O   
6791 O  O   . HOH   F .   ? 0.3681 0.6613 0.4728 -0.0497 -0.1412 0.1049  362 HOH   A O   
6792 O  O   A HOH   F .   ? 0.5703 0.2993 0.4758 -0.0302 -0.1210 0.0714  363 HOH   A O   
6793 O  O   . HOH   F .   ? 0.1437 0.1941 0.2648 0.0024  -0.0064 0.0183  364 HOH   A O   
6794 O  O   . HOH   F .   ? 0.1318 0.1319 0.1452 -0.0044 0.0117  0.0073  365 HOH   A O   
6795 O  O   . HOH   F .   ? 0.3113 0.3666 0.2141 -0.0934 -0.0215 -0.0702 366 HOH   A O   
6796 O  O   . HOH   F .   ? 0.6164 0.4030 0.3182 0.0428  0.0259  0.1525  367 HOH   A O   
6797 O  O   A HOH   F .   ? 0.2338 0.4836 0.4392 0.0773  0.0192  0.0630  368 HOH   A O   
6798 O  O   . HOH   F .   ? 0.1794 0.2164 0.1888 -0.0164 -0.0018 0.0659  369 HOH   A O   
6799 O  O   . HOH   F .   ? 0.1460 0.1519 0.1575 -0.0085 -0.0126 -0.0027 370 HOH   A O   
6800 O  O   . HOH   F .   ? 0.1669 0.1716 0.2311 -0.0213 0.0032  0.0423  371 HOH   A O   
6801 O  O   . HOH   F .   ? 0.7286 0.5664 0.5369 -0.0339 0.0733  0.1294  372 HOH   A O   
6802 O  O   . HOH   F .   ? 0.1799 0.2521 0.2933 -0.0198 0.0677  0.0626  373 HOH   A O   
6803 O  O   . HOH   F .   ? 0.3977 0.2428 0.4491 -0.1232 0.0941  0.0319  374 HOH   A O   
6804 O  O   . HOH   F .   ? 0.1517 0.1320 0.2364 -0.0046 0.0154  -0.0087 375 HOH   A O   
6805 O  O   . HOH   F .   ? 0.4416 0.2663 0.4128 -0.1563 0.1580  -0.0513 376 HOH   A O   
6806 O  O   . HOH   F .   ? 0.2904 0.3994 0.3678 -0.0764 -0.0579 0.0843  377 HOH   A O   
6807 O  O   . HOH   F .   ? 0.3843 0.2155 0.2382 0.1184  0.0509  0.0232  378 HOH   A O   
6808 O  O   . HOH   F .   ? 0.2601 0.4034 0.3334 -0.0384 0.0631  0.0200  379 HOH   A O   
6809 O  O   B HOH   F .   ? 0.3842 0.2996 0.3563 0.0371  0.0014  -0.0139 380 HOH   A O   
6810 O  O   . HOH   F .   ? 0.1839 0.1872 0.2446 -0.0361 0.0094  0.0403  381 HOH   A O   
6811 O  O   . HOH   F .   ? 0.2812 0.4388 0.3026 0.0613  0.0816  0.1803  382 HOH   A O   
6812 O  O   . HOH   F .   ? 0.2008 0.2662 0.3629 0.0283  0.0866  -0.0660 383 HOH   A O   
6813 O  O   . HOH   F .   ? 0.3493 0.6109 0.4014 -0.0286 0.0290  0.1302  384 HOH   A O   
6814 O  O   . HOH   F .   ? 0.1572 0.1560 0.1865 -0.0028 -0.0269 0.0050  385 HOH   A O   
6815 O  O   . HOH   F .   ? 0.1891 0.2810 0.2865 0.0440  0.0484  0.1045  386 HOH   A O   
6816 O  O   . HOH   F .   ? 0.3119 0.3856 0.3604 -0.1544 0.0828  -0.0271 387 HOH   A O   
6817 O  O   T HOH   F .   ? 0.1173 0.1353 0.2270 -0.0285 0.0180  0.0276  388 HOH   A O   
6818 O  O   . HOH   F .   ? 0.2028 0.2348 0.2369 -0.0365 -0.0511 0.0601  389 HOH   A O   
6819 O  O   . HOH   F .   ? 0.3187 0.2319 0.5186 -0.0727 -0.0186 -0.0069 390 HOH   A O   
6820 O  O   . HOH   F .   ? 0.2965 0.2973 0.2259 0.0254  0.0643  0.0135  391 HOH   A O   
6821 O  O   . HOH   F .   ? 0.1897 0.1818 0.1634 0.0019  0.0125  0.0131  392 HOH   A O   
6822 O  O   . HOH   F .   ? 0.5692 0.5913 0.3952 0.2213  -0.0032 0.0075  393 HOH   A O   
6823 O  O   . HOH   F .   ? 0.3396 0.6341 0.3644 0.1478  0.0748  -0.0463 394 HOH   A O   
6824 O  O   . HOH   F .   ? 0.5794 0.3104 0.4895 0.1203  -0.0638 -0.0000 395 HOH   A O   
6825 O  O   A HOH   F .   ? 0.1294 0.1692 0.3705 -0.0091 -0.0119 -0.0401 396 HOH   A O   
6826 O  O   . HOH   F .   ? 0.3326 0.2530 0.3329 -0.0112 -0.0349 0.0942  397 HOH   A O   
6827 O  O   . HOH   F .   ? 0.1920 0.2213 0.2586 -0.0155 -0.0187 0.0857  398 HOH   A O   
6828 O  O   . HOH   F .   ? 0.2575 0.2054 0.1743 -0.0642 0.0079  0.0339  399 HOH   A O   
6829 O  O   . HOH   F .   ? 0.2594 0.2884 0.3235 -0.0112 -0.0203 -0.0705 400 HOH   A O   
6830 O  O   . HOH   F .   ? 0.5416 0.4997 0.6730 -0.0608 -0.0286 0.0892  401 HOH   A O   
6831 O  O   . HOH   F .   ? 0.2516 0.3943 0.3606 -0.0381 0.0852  -0.0926 402 HOH   A O   
6832 O  O   B HOH   F .   ? 0.1455 0.1549 0.2976 -0.0148 -0.0199 0.0052  403 HOH   A O   
6833 O  O   . HOH   F .   ? 0.2934 0.3872 0.3681 -0.0448 0.1314  0.0282  404 HOH   A O   
6834 O  O   . HOH   F .   ? 0.2507 0.1790 0.2398 -0.0019 0.0076  0.0273  405 HOH   A O   
6835 O  O   A HOH   F .   ? 0.2953 0.2497 0.2522 0.0935  0.0585  0.0395  406 HOH   A O   
6836 O  O   B HOH   F .   ? 0.2104 0.2995 0.1822 0.1339  0.0603  0.0970  407 HOH   A O   
6837 O  O   B HOH   F .   ? 0.2898 0.3746 0.1682 -0.0036 0.0018  0.0035  408 HOH   A O   
6838 O  O   A HOH   F .   ? 0.1752 0.1834 0.2588 0.0049  -0.0393 0.0278  409 HOH   A O   
6839 O  O   A HOH   F .   ? 0.2111 0.2147 0.2385 0.0110  0.0132  0.0555  410 HOH   A O   
6840 O  O   . HOH   F .   ? 0.1343 0.1446 0.1839 0.0014  -0.0210 0.0053  411 HOH   A O   
6841 O  O   . HOH   F .   ? 0.1814 0.1909 0.3911 0.0338  0.0928  0.1021  412 HOH   A O   
6842 O  O   . HOH   F .   ? 0.3149 0.2759 0.2074 -0.0767 -0.0994 0.0408  413 HOH   A O   
6843 O  O   . HOH   F .   ? 0.4770 0.4811 0.2130 -0.0335 0.0943  0.1004  414 HOH   A O   
6844 O  O   . HOH   F .   ? 0.3845 0.5796 0.5215 0.1753  0.0716  0.0748  415 HOH   A O   
6845 O  O   . HOH   F .   ? 0.3185 0.3198 0.2207 -0.0396 -0.0806 0.0531  416 HOH   A O   
6846 O  O   . HOH   F .   ? 0.2246 0.1706 0.2932 0.0018  -0.0281 0.0182  417 HOH   A O   
6847 O  O   . HOH   F .   ? 0.1520 0.1612 0.3176 0.0004  -0.0039 0.0201  418 HOH   A O   
6848 O  O   A HOH   F .   ? 0.1851 0.1900 0.3246 -0.0091 0.0353  -0.0141 419 HOH   A O   
6849 O  O   . HOH   F .   ? 0.2510 0.2135 0.2604 -0.0601 -0.0030 0.0599  420 HOH   A O   
6850 O  O   . HOH   F .   ? 0.1883 0.2643 0.3750 -0.0116 -0.0293 0.0266  421 HOH   A O   
6851 O  O   . HOH   F .   ? 0.3988 0.4311 0.3925 0.1671  0.0225  -0.0607 422 HOH   A O   
6852 O  O   . HOH   F .   ? 0.1704 0.1418 0.1583 -0.0189 0.0110  0.0026  423 HOH   A O   
6853 O  O   . HOH   F .   ? 0.2073 0.2945 0.2655 -0.0199 -0.0620 0.0637  424 HOH   A O   
6854 O  O   . HOH   F .   ? 0.2858 0.6047 0.1781 -0.0332 0.0574  0.0112  425 HOH   A O   
6855 O  O   . HOH   F .   ? 0.2844 0.3681 0.6972 -0.0180 0.0768  -0.0584 426 HOH   A O   
6856 O  O   A HOH   F .   ? 0.1192 0.1553 0.1342 0.0198  -0.0363 -0.0266 427 HOH   A O   
6857 O  O   . HOH   F .   ? 0.3403 0.1306 0.2130 0.0060  -0.0531 0.0143  428 HOH   A O   
6858 O  O   . HOH   F .   ? 0.8572 0.8963 0.7100 -0.0597 -0.0133 -0.0041 429 HOH   A O   
6859 O  O   A HOH   F .   ? 0.1846 0.2089 0.3286 0.0049  -0.0258 -0.0490 430 HOH   A O   
6860 O  O   . HOH   F .   ? 0.2270 0.4031 0.2489 0.1450  0.0053  0.0334  431 HOH   A O   
6861 O  O   . HOH   F .   ? 0.4188 0.2309 0.5299 -0.0928 -0.2260 0.1178  432 HOH   A O   
6862 O  O   . HOH   F .   ? 0.3596 0.3612 0.2261 -0.0946 -0.0529 0.0461  433 HOH   A O   
6863 O  O   . HOH   F .   ? 0.1688 0.2035 0.2541 -0.0187 0.0001  0.0411  434 HOH   A O   
6864 O  O   . HOH   F .   ? 0.5984 0.6721 0.6313 -0.1192 -0.0552 -0.0193 435 HOH   A O   
6865 O  O   . HOH   F .   ? 0.4487 0.6218 0.3004 -0.1012 -0.0076 0.1177  436 HOH   A O   
6866 O  O   A HOH   F .   ? 0.2540 0.2902 0.2655 -0.0218 0.0761  -0.0237 437 HOH   A O   
6867 O  O   . HOH   F .   ? 0.2109 0.1806 0.3124 0.0267  -0.0676 0.0210  438 HOH   A O   
6868 O  O   . HOH   F .   ? 0.6189 0.6694 0.4521 0.0595  0.2806  -0.0423 439 HOH   A O   
6869 O  O   . HOH   F .   ? 0.6666 0.4253 0.5009 0.1877  -0.0951 0.1553  440 HOH   A O   
6870 O  O   B HOH   F .   ? 0.3033 0.4005 0.3571 0.0126  0.0033  -0.0328 441 HOH   A O   
6871 O  O   . HOH   F .   ? 0.5893 0.6876 0.5871 -0.1292 0.0308  0.0334  442 HOH   A O   
6872 O  O   . HOH   F .   ? 0.6500 0.7544 0.4486 0.1867  -0.1162 0.2098  443 HOH   A O   
6873 O  O   . HOH   F .   ? 0.3541 0.2796 0.1911 -0.0915 0.0108  0.0634  444 HOH   A O   
6874 O  O   . HOH   F .   ? 0.4909 0.4704 0.4151 -0.0269 -0.1515 0.0028  445 HOH   A O   
6875 O  O   . HOH   F .   ? 0.2561 0.1611 0.2800 0.0127  0.0041  0.0168  446 HOH   A O   
6876 O  O   . HOH   F .   ? 0.1655 0.1523 0.1602 -0.0055 -0.0148 -0.0063 447 HOH   A O   
6877 O  O   A HOH   F .   ? 0.4746 0.2444 0.4828 -0.0231 0.1296  -0.0663 448 HOH   A O   
6878 O  O   . HOH   F .   ? 0.3966 0.3465 0.3192 0.2090  -0.0450 -0.0357 449 HOH   A O   
6879 O  O   A HOH   F .   ? 0.4563 0.3065 0.3200 -0.0310 0.0842  0.1134  450 HOH   A O   
6880 O  O   . HOH   F .   ? 0.1865 0.2259 0.4802 -0.0213 -0.0812 0.0715  451 HOH   A O   
6881 O  O   . HOH   F .   ? 0.4487 0.4866 0.4422 -0.0927 -0.0947 -0.1239 452 HOH   A O   
6882 O  O   A HOH   F .   ? 0.2711 0.2636 0.4528 0.0199  0.0858  -0.1141 453 HOH   A O   
6883 O  O   . HOH   F .   ? 0.2309 0.1990 0.2819 0.0122  0.0294  0.0350  454 HOH   A O   
6884 O  O   A HOH   F .   ? 0.2186 0.1620 0.2481 -0.0245 -0.0217 0.0038  455 HOH   A O   
6885 O  O   . HOH   F .   ? 0.6726 0.5855 0.7337 0.0444  -0.0935 0.1487  456 HOH   A O   
6886 O  O   . HOH   F .   ? 0.2188 0.2747 0.2661 -0.0026 -0.0121 -0.0553 457 HOH   A O   
6887 O  O   . HOH   F .   ? 0.6972 0.6655 0.6534 0.0644  -0.1046 0.0039  458 HOH   A O   
6888 O  O   . HOH   F .   ? 0.4611 0.5379 0.4488 0.0222  -0.0177 0.0676  459 HOH   A O   
6889 O  O   . HOH   F .   ? 0.5345 0.3775 0.4078 0.0636  0.0365  0.0609  460 HOH   A O   
6890 O  O   . HOH   F .   ? 0.6249 0.6724 0.5390 -0.0705 0.0963  0.1602  461 HOH   A O   
6891 O  O   . HOH   F .   ? 0.3796 0.3745 0.4338 0.0097  0.0564  0.0363  462 HOH   A O   
6892 O  O   . HOH   F .   ? 0.3095 0.3705 0.3414 0.1302  -0.0388 0.0354  463 HOH   A O   
6893 O  O   . HOH   F .   ? 0.7475 0.7704 0.5026 0.0409  -0.0814 -0.0111 464 HOH   A O   
6894 O  O   . HOH   F .   ? 0.2633 0.2605 0.3707 -0.0393 0.0404  -0.0716 465 HOH   A O   
6895 O  O   . HOH   F .   ? 0.3593 0.4839 0.5038 -0.1334 0.1150  -0.1362 466 HOH   A O   
6896 O  O   . HOH   F .   ? 0.2658 0.4352 0.5024 0.0633  0.0080  -0.1902 467 HOH   A O   
6897 O  O   . HOH   F .   ? 0.3751 0.5241 0.4890 0.0485  -0.0552 0.1529  468 HOH   A O   
6898 O  O   . HOH   F .   ? 0.2677 0.1698 0.2475 0.0185  -0.0870 -0.0295 469 HOH   A O   
6899 O  O   . HOH   F .   ? 0.6282 0.3553 0.6865 0.1091  0.0292  0.2342  470 HOH   A O   
6900 O  O   . HOH   F .   ? 0.2689 0.2778 0.3398 -0.0983 0.0487  -0.0310 471 HOH   A O   
6901 O  O   . HOH   F .   ? 0.2884 0.4585 0.4028 -0.0664 -0.0116 0.0214  472 HOH   A O   
6902 O  O   A HOH   F .   ? 0.2823 0.2657 0.5280 0.0905  -0.1825 -0.1076 473 HOH   A O   
6903 O  O   . HOH   F .   ? 0.4101 0.6312 0.3934 -0.0796 -0.0677 0.2282  474 HOH   A O   
6904 O  O   . HOH   F .   ? 0.5621 0.5800 0.4937 0.1115  -0.0456 -0.0748 475 HOH   A O   
6905 O  O   . HOH   F .   ? 0.6524 0.6391 0.6571 0.0959  0.1691  0.1857  476 HOH   A O   
6906 O  O   . HOH   F .   ? 0.5563 0.4992 0.4499 -0.0158 0.0872  0.0451  477 HOH   A O   
6907 O  O   . HOH   F .   ? 0.2988 0.2369 0.3522 0.0178  0.0617  -0.0015 478 HOH   A O   
6908 O  O   B HOH   F .   ? 0.3262 0.2654 0.2300 0.0764  -0.0367 -0.0146 479 HOH   A O   
6909 O  O   B HOH   F .   ? 0.2849 0.2056 0.3587 0.0475  0.1002  -0.0672 480 HOH   A O   
6910 O  O   . HOH   F .   ? 0.3964 0.5067 0.3726 0.0456  -0.0551 -0.0832 481 HOH   A O   
6911 O  O   . HOH   F .   ? 0.4514 0.4510 0.3219 -0.0274 -0.0526 -0.0277 482 HOH   A O   
6912 O  O   . HOH   F .   ? 0.3857 0.4829 0.2665 0.0100  -0.0049 -0.0056 483 HOH   A O   
6913 O  O   . HOH   F .   ? 0.6399 0.5531 0.6780 -0.1083 0.0091  -0.0923 484 HOH   A O   
6914 O  O   . HOH   F .   ? 0.4901 0.5588 0.5754 -0.1676 -0.1360 0.0149  485 HOH   A O   
6915 O  O   . HOH   F .   ? 0.4542 0.2947 0.3478 -0.0723 -0.1444 0.0841  486 HOH   A O   
6916 O  O   . HOH   F .   ? 0.4477 0.4104 0.5392 -0.2067 -0.0459 -0.0141 487 HOH   A O   
6917 O  O   . HOH   F .   ? 0.5634 0.3865 0.3835 -0.0264 0.0950  -0.0209 488 HOH   A O   
6918 O  O   . HOH   F .   ? 0.5461 0.4401 0.4354 -0.0018 0.0269  -0.1211 489 HOH   A O   
6919 O  O   . HOH   F .   ? 0.2498 0.2260 0.2478 0.0256  0.0005  0.0014  490 HOH   A O   
6920 O  O   B HOH   F .   ? 0.2921 0.2032 0.2922 0.0679  -0.0356 0.0846  491 HOH   A O   
6921 O  O   . HOH   F .   ? 0.7132 0.4014 0.3244 -0.0343 -0.1250 0.0524  492 HOH   A O   
6922 O  O   . HOH   F .   ? 0.2974 0.4024 0.4862 -0.0064 0.1294  0.1243  493 HOH   A O   
6923 O  O   . HOH   F .   ? 0.6442 0.6248 0.4547 -0.0774 0.1352  0.1242  494 HOH   A O   
6924 O  O   B HOH   F .   ? 0.3193 0.2712 0.3290 0.0372  0.0391  0.0271  495 HOH   A O   
6925 O  O   . HOH   F .   ? 0.5950 0.5034 0.4981 -0.0833 -0.1042 -0.0829 496 HOH   A O   
6926 O  O   . HOH   F .   ? 0.2738 0.5305 0.3772 0.1011  0.1023  0.2433  497 HOH   A O   
6927 O  O   . HOH   F .   ? 0.2487 0.2553 0.6785 -0.0060 -0.1240 0.0436  498 HOH   A O   
6928 O  O   . HOH   F .   ? 0.5765 0.5459 0.6615 0.0645  0.2174  -0.1127 499 HOH   A O   
6929 O  O   . HOH   F .   ? 0.4766 0.3659 0.2623 -0.0743 0.1634  -0.0449 500 HOH   A O   
6930 O  O   . HOH   F .   ? 0.4381 0.3662 0.4548 -0.0875 0.0306  0.1402  501 HOH   A O   
6931 O  O   . HOH   F .   ? 0.2951 0.4767 0.3297 -0.0363 -0.0235 -0.0885 502 HOH   A O   
6932 O  O   . HOH   F .   ? 0.5038 0.5334 0.5579 0.0047  -0.0940 0.0665  503 HOH   A O   
6933 O  O   B HOH   F .   ? 0.4162 0.4622 0.4134 0.1451  0.0024  -0.0885 504 HOH   A O   
6934 O  O   . HOH   F .   ? 0.4276 0.3191 0.4693 -0.0161 0.2235  0.0094  505 HOH   A O   
6935 O  O   . HOH   F .   ? 0.6708 0.2558 0.4015 -0.0745 0.1063  0.0438  506 HOH   A O   
6936 O  O   . HOH   F .   ? 0.2567 0.3110 0.4732 -0.0157 0.1059  -0.0494 507 HOH   A O   
6937 O  O   . HOH   F .   ? 0.2890 0.2131 0.5219 0.0099  0.0337  0.0889  508 HOH   A O   
6938 O  O   . HOH   F .   ? 0.7385 0.6199 0.5315 0.1574  -0.1456 0.0257  509 HOH   A O   
6939 O  O   . HOH   F .   ? 0.2658 0.4015 0.3361 0.0968  -0.0420 0.0855  510 HOH   A O   
6940 O  O   . HOH   F .   ? 0.3854 0.7271 0.5534 -0.0890 -0.0300 0.1882  511 HOH   A O   
6941 O  O   . HOH   F .   ? 0.4707 0.2620 0.4105 -0.1381 0.0005  0.0134  512 HOH   A O   
6942 O  O   . HOH   F .   ? 0.3143 0.7453 0.4112 0.0776  0.0791  -0.0371 513 HOH   A O   
6943 O  O   . HOH   F .   ? 0.2639 0.4352 0.4311 0.0568  -0.0746 -0.0465 514 HOH   A O   
6944 O  O   . HOH   F .   ? 0.5576 0.6949 0.5237 0.1208  -0.0715 0.0410  515 HOH   A O   
6945 O  O   . HOH   F .   ? 0.5742 0.4044 0.4668 0.1245  0.0183  0.1030  516 HOH   A O   
6946 O  O   B HOH   F .   ? 0.2832 0.1900 0.2929 0.0412  -0.0538 0.0177  517 HOH   A O   
6947 O  O   . HOH   F .   ? 0.5185 0.6791 0.5292 0.3228  -0.0098 0.1294  518 HOH   A O   
6948 O  O   . HOH   F .   ? 0.2919 0.2324 0.4472 0.0102  0.0274  0.0517  519 HOH   A O   
6949 O  O   T HOH   F .   ? 0.1198 0.1003 0.2055 -0.0159 -0.0084 0.0346  520 HOH   A O   
6950 O  O   . HOH   F .   ? 0.5290 0.6278 0.4830 -0.0778 -0.0853 -0.1119 521 HOH   A O   
6951 O  O   . HOH   F .   ? 0.2647 0.6625 0.3882 0.0744  0.0104  -0.0562 522 HOH   A O   
6952 O  O   . HOH   F .   ? 0.4515 0.6397 0.5331 -0.0551 -0.0117 0.0457  523 HOH   A O   
6953 O  O   . HOH   F .   ? 0.5015 0.4720 0.4480 0.1516  -0.0019 0.1488  524 HOH   A O   
6954 O  O   . HOH   F .   ? 0.3288 0.4309 0.5175 -0.0357 -0.0972 0.2609  525 HOH   A O   
6955 O  O   . HOH   G .   ? 0.2382 0.2097 0.3172 0.0206  0.0835  0.0381  201 HOH   B O   
6956 O  O   . HOH   G .   ? 0.4750 0.3451 0.3911 -0.0378 0.0014  -0.1465 202 HOH   B O   
6957 O  O   . HOH   G .   ? 0.3724 0.3264 0.6365 -0.0680 0.0491  -0.0153 203 HOH   B O   
6958 O  O   . HOH   G .   ? 0.3078 0.6470 0.3223 0.0613  0.0175  0.2040  204 HOH   B O   
6959 O  O   . HOH   G .   ? 0.6655 0.3181 0.4339 0.0492  0.1103  0.0064  205 HOH   B O   
6960 O  O   . HOH   G .   ? 0.2739 0.5652 0.5356 -0.0081 0.1405  -0.1945 206 HOH   B O   
6961 O  O   . HOH   G .   ? 0.4758 0.3827 0.5870 0.0442  -0.0847 0.2493  207 HOH   B O   
6962 O  O   . HOH   G .   ? 0.4727 0.4719 0.2959 0.0162  -0.0245 -0.1315 208 HOH   B O   
6963 O  O   . HOH   G .   ? 0.3057 0.2017 0.5390 0.0096  0.1857  0.0828  209 HOH   B O   
6964 O  O   . HOH   G .   ? 0.4655 0.6269 0.3607 0.2972  -0.0779 -0.0074 210 HOH   B O   
6965 O  O   . HOH   G .   ? 0.5954 0.5966 0.5914 0.1401  0.0263  0.0484  211 HOH   B O   
6966 O  O   . HOH   G .   ? 0.1617 0.1946 0.2856 -0.0185 -0.0062 -0.0001 212 HOH   B O   
6967 O  O   . HOH   G .   ? 0.1952 0.2192 0.3178 0.0003  0.0245  -0.0294 213 HOH   B O   
6968 O  O   . HOH   G .   ? 0.2857 0.2785 0.6289 0.0508  -0.1035 0.0592  214 HOH   B O   
6969 O  O   . HOH   G .   ? 0.3986 0.4578 0.5312 -0.1113 -0.0364 -0.1287 215 HOH   B O   
6970 O  O   . HOH   G .   ? 0.4214 0.5356 0.3786 0.2486  -0.0171 0.0385  216 HOH   B O   
6971 O  O   . HOH   G .   ? 0.3253 0.3860 0.4919 0.0520  -0.0370 0.0066  217 HOH   B O   
6972 O  O   . HOH   G .   ? 0.4889 0.4523 0.3590 0.0244  0.0869  -0.1424 218 HOH   B O   
6973 O  O   . HOH   G .   ? 0.4336 0.5012 0.6067 0.0345  -0.1573 -0.0745 219 HOH   B O   
6974 O  O   . HOH   G .   ? 0.4443 0.3949 0.3385 0.0044  -0.1117 0.0461  220 HOH   B O   
6975 O  O   . HOH   G .   ? 0.3276 0.5088 0.4588 0.2022  0.0442  -0.0067 221 HOH   B O   
6976 O  O   . HOH   G .   ? 0.2219 0.2235 0.4056 -0.0413 -0.0028 -0.0453 222 HOH   B O   
6977 O  O   . HOH   G .   ? 0.3189 0.2314 0.5299 -0.0058 0.1827  0.0349  223 HOH   B O   
6978 O  O   . HOH   G .   ? 0.5338 0.2946 0.3880 -0.1613 -0.0012 0.0342  224 HOH   B O   
6979 O  O   . HOH   G .   ? 0.4901 0.2117 0.2929 -0.0035 -0.0905 0.0065  225 HOH   B O   
6980 O  O   . HOH   G .   ? 0.1768 0.2152 0.3105 -0.0177 0.0115  0.0006  226 HOH   B O   
6981 O  O   . HOH   G .   ? 0.6387 0.3203 0.2680 -0.0347 0.0693  -0.0059 227 HOH   B O   
6982 O  O   . HOH   G .   ? 0.3163 0.3631 0.5807 -0.0253 0.0741  -0.0296 228 HOH   B O   
6983 O  O   . HOH   G .   ? 0.4427 0.6102 0.3827 0.1891  0.0276  -0.0052 229 HOH   B O   
6984 O  O   . HOH   G .   ? 0.3569 0.1769 0.2182 0.0182  -0.0843 -0.0109 230 HOH   B O   
6985 O  O   . HOH   G .   ? 0.2424 0.1886 0.2792 -0.0303 0.1090  -0.0024 231 HOH   B O   
6986 O  O   . HOH   G .   ? 0.6639 0.4691 0.5122 0.1684  -0.0098 -0.1008 232 HOH   B O   
6987 O  O   . HOH   G .   ? 0.3614 0.2580 0.4313 0.0380  -0.0779 -0.1272 233 HOH   B O   
6988 O  O   . HOH   G .   ? 0.2643 0.3857 0.3047 -0.0670 0.0553  -0.0866 234 HOH   B O   
6989 O  O   . HOH   G .   ? 0.4112 0.4216 0.5146 -0.1711 0.0016  0.1267  235 HOH   B O   
6990 O  O   . HOH   G .   ? 0.2189 0.2421 0.3190 -0.0519 0.0046  -0.0278 236 HOH   B O   
6991 O  O   . HOH   G .   ? 0.2786 0.2620 0.3257 0.0470  0.0055  -0.0970 237 HOH   B O   
6992 O  O   . HOH   G .   ? 0.6358 0.6031 0.3464 0.1151  0.0389  -0.0073 238 HOH   B O   
6993 O  O   . HOH   G .   ? 0.2050 0.1326 0.3383 0.0077  -0.0612 -0.0111 239 HOH   B O   
6994 O  O   . HOH   G .   ? 0.3609 0.3089 0.2186 0.0370  0.0505  0.0461  240 HOH   B O   
6995 O  O   . HOH   G .   ? 0.2184 0.3881 0.2499 -0.0522 -0.0256 0.0617  241 HOH   B O   
6996 O  O   . HOH   G .   ? 0.1448 0.1447 0.1577 -0.0140 -0.0047 -0.0044 242 HOH   B O   
6997 O  O   . HOH   G .   ? 0.4915 0.3220 0.4194 -0.2282 0.0014  0.0156  243 HOH   B O   
6998 O  O   . HOH   G .   ? 0.2213 0.3769 0.3224 -0.0527 -0.0702 -0.0497 244 HOH   B O   
6999 O  O   . HOH   G .   ? 0.1641 0.1464 0.2748 -0.0023 0.0015  -0.0059 245 HOH   B O   
7000 O  O   . HOH   G .   ? 0.3196 0.1726 0.5973 -0.0192 -0.1380 -0.0280 246 HOH   B O   
7001 O  O   . HOH   G .   ? 0.3327 0.3772 0.2420 0.0355  0.0833  0.0319  247 HOH   B O   
7002 O  O   . HOH   G .   ? 0.3926 0.2755 0.4156 0.0913  -0.0343 -0.0447 248 HOH   B O   
7003 O  O   . HOH   G .   ? 0.2412 0.2087 0.2570 0.0706  -0.0758 -0.0544 249 HOH   B O   
7004 O  O   . HOH   G .   ? 0.1498 0.1304 0.1658 -0.0013 -0.0044 0.0113  250 HOH   B O   
7005 O  O   . HOH   G .   ? 0.2186 0.1915 0.2184 -0.0319 -0.0482 0.0185  251 HOH   B O   
7006 O  O   . HOH   G .   ? 0.2944 0.2288 0.2898 0.0853  0.0853  0.0081  252 HOH   B O   
7007 O  O   . HOH   G .   ? 0.4657 0.3429 0.3366 -0.0935 0.0819  -0.0986 253 HOH   B O   
7008 O  O   . HOH   G .   ? 0.3328 0.2546 0.3203 -0.0477 0.0181  -0.0497 254 HOH   B O   
7009 O  O   . HOH   G .   ? 0.2275 0.2983 0.2104 -0.0484 0.0247  0.0433  255 HOH   B O   
7010 O  O   . HOH   G .   ? 0.2947 0.4119 0.2768 -0.0833 -0.0356 -0.0652 256 HOH   B O   
7011 O  O   . HOH   G .   ? 0.2342 0.1972 0.3317 -0.0041 -0.0728 -0.0343 257 HOH   B O   
7012 O  O   . HOH   G .   ? 0.2469 0.2249 0.2004 0.0171  -0.0044 0.0016  258 HOH   B O   
7013 O  O   . HOH   G .   ? 0.1628 0.1685 0.3163 -0.0203 -0.0233 0.0112  259 HOH   B O   
7014 O  O   . HOH   G .   ? 0.3403 0.4642 0.3441 -0.0387 -0.1064 0.1037  260 HOH   B O   
7015 O  O   . HOH   G .   ? 0.2675 0.4295 0.5585 -0.0181 -0.0088 -0.1242 261 HOH   B O   
7016 O  O   . HOH   G .   ? 0.2129 0.1511 0.2102 -0.0309 -0.0378 0.0314  262 HOH   B O   
7017 O  O   . HOH   G .   ? 0.2525 0.5688 0.5532 0.1519  -0.0636 -0.0690 263 HOH   B O   
7018 O  O   . HOH   G .   ? 0.4088 0.2599 0.4342 -0.0154 -0.1325 -0.0443 264 HOH   B O   
7019 O  O   . HOH   G .   ? 0.2366 0.2130 0.2093 0.0150  -0.0063 -0.0001 265 HOH   B O   
7020 O  O   . HOH   G .   ? 0.1441 0.1685 0.2191 -0.0123 0.0053  0.0145  266 HOH   B O   
7021 O  O   . HOH   G .   ? 0.2625 0.3814 0.3904 0.0370  0.1235  0.0271  267 HOH   B O   
7022 O  O   . HOH   G .   ? 0.2556 0.1979 0.2894 -0.0603 0.0190  -0.0102 268 HOH   B O   
7023 O  O   . HOH   G .   ? 0.4672 0.3848 0.2777 0.0431  -0.0123 -0.1044 269 HOH   B O   
7024 O  O   . HOH   G .   ? 0.1873 0.1821 0.1687 -0.0452 -0.0390 0.0080  270 HOH   B O   
7025 O  O   . HOH   G .   ? 0.2128 0.4623 0.4718 -0.0325 -0.0183 -0.1444 271 HOH   B O   
7026 O  O   . HOH   G .   ? 0.2365 0.2508 0.2363 -0.0403 -0.0639 -0.0379 272 HOH   B O   
7027 O  O   . HOH   G .   ? 0.2541 0.2859 0.2400 -0.0426 -0.0878 0.0214  273 HOH   B O   
7028 O  O   . HOH   G .   ? 0.3382 0.3866 0.5214 0.0029  0.0128  0.0356  274 HOH   B O   
7029 O  O   . HOH   G .   ? 0.2006 0.1532 0.2359 -0.0271 -0.0140 0.0213  275 HOH   B O   
7030 O  O   . HOH   G .   ? 0.2340 0.3512 0.3281 -0.0532 0.0455  -0.1070 276 HOH   B O   
7031 O  O   . HOH   G .   ? 0.1729 0.1430 0.4075 -0.0110 -0.0243 -0.0050 277 HOH   B O   
7032 O  O   . HOH   G .   ? 0.2819 0.2082 0.5174 0.0066  0.0469  0.0509  278 HOH   B O   
7033 O  O   . HOH   G .   ? 0.2471 0.3527 0.2432 0.1223  -0.0394 -0.0510 279 HOH   B O   
7034 O  O   . HOH   G .   ? 0.3786 0.3748 0.4598 0.1417  -0.0704 -0.1075 280 HOH   B O   
7035 O  O   . HOH   G .   ? 0.1622 0.1590 0.3480 -0.0146 0.0113  -0.0039 281 HOH   B O   
7036 O  O   . HOH   G .   ? 0.2772 0.4753 0.4680 -0.1027 -0.1124 0.0665  282 HOH   B O   
7037 O  O   . HOH   G .   ? 0.2799 0.6022 0.7086 0.1034  -0.0768 -0.0976 283 HOH   B O   
7038 O  O   . HOH   G .   ? 0.1727 0.1547 0.1846 -0.0016 0.0038  0.0049  284 HOH   B O   
7039 O  O   . HOH   G .   ? 0.2480 0.6449 0.2549 0.0613  -0.0236 -0.0386 285 HOH   B O   
7040 O  O   . HOH   G .   ? 0.3446 0.2896 0.2869 -0.0344 0.0182  -0.1216 286 HOH   B O   
7041 O  O   . HOH   G .   ? 0.5449 0.3714 0.3119 0.2515  0.1093  0.0855  287 HOH   B O   
7042 O  O   . HOH   G .   ? 0.3047 0.2807 0.4803 -0.0197 -0.0625 0.1046  288 HOH   B O   
7043 O  O   . HOH   G .   ? 0.3746 0.2205 0.3851 -0.1019 -0.1984 0.0860  289 HOH   B O   
7044 O  O   . HOH   G .   ? 0.3712 0.2556 0.2220 0.0173  -0.0865 0.0076  290 HOH   B O   
7045 O  O   . HOH   G .   ? 0.1615 0.2111 0.1522 -0.0137 -0.0136 0.0027  291 HOH   B O   
7046 O  O   . HOH   G .   ? 0.2416 0.2661 0.3015 0.0055  -0.0860 0.0263  292 HOH   B O   
7047 O  O   . HOH   G .   ? 0.4243 0.4582 0.4719 0.0059  -0.1471 0.0154  293 HOH   B O   
7048 O  O   . HOH   G .   ? 0.1727 0.3308 0.4698 0.0189  -0.0018 -0.1270 294 HOH   B O   
7049 O  O   . HOH   G .   ? 0.1722 0.2031 0.2876 0.0175  0.0002  0.0122  295 HOH   B O   
7050 O  O   . HOH   G .   ? 0.4852 0.6226 0.2527 -0.0264 -0.1120 0.0771  296 HOH   B O   
7051 O  O   . HOH   G .   ? 0.4702 0.3982 0.2351 0.1301  -0.0959 0.0516  297 HOH   B O   
7052 O  O   . HOH   G .   ? 0.1846 0.1590 0.2468 0.0114  0.0086  0.0098  298 HOH   B O   
7053 O  O   . HOH   G .   ? 0.3441 0.6651 0.3891 0.1484  -0.0029 0.1464  299 HOH   B O   
7054 O  O   . HOH   G .   ? 0.4462 0.4784 0.2456 0.0030  0.0923  0.0891  300 HOH   B O   
7055 O  O   . HOH   G .   ? 0.2050 0.2911 0.6112 0.0353  -0.0369 -0.1380 301 HOH   B O   
7056 O  O   . HOH   G .   ? 0.3435 0.1902 0.3569 0.0675  0.1329  0.0484  302 HOH   B O   
7057 O  O   . HOH   G .   ? 0.2184 0.1653 0.2578 -0.0285 -0.0290 -0.0013 303 HOH   B O   
7058 O  O   . HOH   G .   ? 0.4586 0.3029 0.2234 -0.1671 0.0487  -0.0173 304 HOH   B O   
7059 O  O   . HOH   G .   ? 0.3215 0.4047 0.3862 -0.1543 0.1068  -0.0480 305 HOH   B O   
7060 O  O   . HOH   G .   ? 0.2038 0.1635 0.3455 0.0369  -0.0868 0.0012  306 HOH   B O   
7061 O  O   . HOH   G .   ? 0.1591 0.1461 0.3184 0.0057  -0.0005 -0.0063 307 HOH   B O   
7062 O  O   . HOH   G .   ? 0.1552 0.1928 0.3068 -0.0192 -0.0101 0.0107  308 HOH   B O   
7063 O  O   . HOH   G .   ? 0.2432 0.1543 0.2546 -0.0149 -0.0209 0.0332  309 HOH   B O   
7064 O  O   . HOH   G .   ? 0.2963 0.2941 0.3698 -0.0438 0.1225  -0.0880 310 HOH   B O   
7065 O  O   . HOH   G .   ? 0.2228 0.3140 0.4680 -0.0174 -0.0366 -0.0138 311 HOH   B O   
7066 O  O   . HOH   G .   ? 0.2705 0.3209 0.4889 -0.0502 -0.1469 0.1189  312 HOH   B O   
7067 O  O   . HOH   G .   ? 0.4418 0.3487 0.4354 -0.0420 0.0541  0.1059  313 HOH   B O   
7068 O  O   . HOH   G .   ? 0.1666 0.3017 0.2299 -0.0151 -0.0138 0.0797  314 HOH   B O   
7069 O  O   . HOH   G .   ? 0.6070 0.5816 0.5263 0.2676  -0.0042 -0.0227 315 HOH   B O   
7070 O  O   . HOH   G .   ? 0.4021 0.2264 0.2739 0.1372  0.1057  0.0238  316 HOH   B O   
7071 O  O   . HOH   G .   ? 0.4902 0.3915 0.2539 0.0285  -0.0452 -0.0661 317 HOH   B O   
7072 O  O   . HOH   G .   ? 0.2206 0.2025 0.1882 -0.0098 0.0207  0.0194  318 HOH   B O   
7073 O  O   . HOH   G .   ? 0.1610 0.1629 0.3052 -0.0139 -0.0148 -0.0048 319 HOH   B O   
7074 O  O   . HOH   G .   ? 0.2171 0.5351 0.4427 -0.0510 -0.0386 -0.0251 320 HOH   B O   
7075 O  O   . HOH   G .   ? 0.4670 0.3905 0.5056 0.0548  0.0056  0.0502  321 HOH   B O   
7076 O  O   . HOH   G .   ? 0.3800 0.4064 0.6911 -0.0337 -0.0910 0.1882  322 HOH   B O   
7077 O  O   . HOH   G .   ? 0.1763 0.2897 0.3359 0.0305  -0.0212 -0.0766 323 HOH   B O   
7078 O  O   . HOH   G .   ? 0.3016 0.2347 0.2421 0.0355  -0.0186 0.0307  324 HOH   B O   
7079 O  O   . HOH   G .   ? 0.4658 0.3058 0.5153 0.1145  0.2112  0.1637  325 HOH   B O   
7080 O  O   . HOH   G .   ? 0.1898 0.1973 0.3030 0.0340  0.0449  0.0255  326 HOH   B O   
7081 O  O   . HOH   G .   ? 0.2250 0.2316 0.5746 -0.0434 0.0106  0.1363  327 HOH   B O   
7082 O  O   . HOH   G .   ? 0.5751 0.4701 0.6649 0.1536  -0.0696 0.1842  328 HOH   B O   
7083 O  O   . HOH   G .   ? 0.4438 0.4203 0.2186 0.1126  -0.0679 -0.0182 329 HOH   B O   
7084 O  O   . HOH   G .   ? 0.2774 0.2027 0.4624 -0.0062 0.0014  0.0230  330 HOH   B O   
7085 O  O   . HOH   G .   ? 0.4316 0.2512 0.3067 0.0213  0.0251  0.0769  331 HOH   B O   
7086 O  O   . HOH   G .   ? 0.5417 0.3597 0.3622 0.0140  0.1055  0.1234  332 HOH   B O   
7087 O  O   . HOH   G .   ? 0.7878 0.2100 0.3297 0.0127  -0.0894 0.0030  333 HOH   B O   
7088 O  O   . HOH   G .   ? 0.6214 0.4744 0.5277 0.1129  0.1289  0.0061  334 HOH   B O   
7089 O  O   . HOH   G .   ? 0.1757 0.1475 0.2422 0.0074  -0.0144 0.0084  335 HOH   B O   
7090 O  O   . HOH   G .   ? 0.5785 0.5570 0.5592 -0.1190 -0.0593 0.1545  336 HOH   B O   
7091 O  O   . HOH   G .   ? 0.5206 0.3426 0.4512 0.0290  0.0774  -0.1487 337 HOH   B O   
7092 O  O   . HOH   G .   ? 0.4214 0.6626 0.3778 -0.0329 -0.0632 0.1838  338 HOH   B O   
7093 O  O   . HOH   G .   ? 0.5448 0.4311 0.5971 -0.0710 -0.0546 -0.0978 339 HOH   B O   
7094 O  O   . HOH   G .   ? 0.4896 0.3079 0.3062 0.0491  -0.1286 -0.0716 340 HOH   B O   
7095 O  O   . HOH   G .   ? 0.2191 0.5319 0.6112 -0.0213 -0.1052 0.0143  341 HOH   B O   
7096 O  O   . HOH   G .   ? 0.4678 0.5392 0.3777 0.0086  -0.1141 0.0020  342 HOH   B O   
7097 O  O   . HOH   G .   ? 0.3770 0.5966 0.4243 -0.1148 -0.0853 -0.0713 343 HOH   B O   
7098 O  O   . HOH   G .   ? 0.6680 0.5942 0.3271 0.0434  -0.0471 0.1234  344 HOH   B O   
7099 O  O   . HOH   G .   ? 0.2005 0.2007 0.3139 -0.0097 0.0531  -0.0168 345 HOH   B O   
7100 O  O   . HOH   G .   ? 0.3981 0.5348 0.5608 0.0187  -0.0769 0.0581  346 HOH   B O   
7101 O  O   . HOH   G .   ? 0.2926 0.1924 0.4117 0.0355  -0.1117 -0.0547 347 HOH   B O   
7102 O  O   . HOH   G .   ? 0.2466 0.6342 0.3276 0.1631  -0.0546 -0.1406 348 HOH   B O   
7103 O  O   . HOH   G .   ? 0.4965 0.5274 0.4407 -0.1171 0.0562  0.1081  349 HOH   B O   
7104 O  O   . HOH   G .   ? 0.2894 0.2388 0.4710 -0.0284 -0.0950 -0.0526 350 HOH   B O   
7105 O  O   . HOH   G .   ? 0.2176 0.4022 0.4964 0.0123  0.0539  -0.0027 351 HOH   B O   
7106 O  O   . HOH   G .   ? 0.3857 0.2229 0.3358 -0.0730 0.0220  -0.0803 352 HOH   B O   
7107 O  O   . HOH   G .   ? 0.4344 0.5650 0.6053 0.0003  0.0128  -0.0427 353 HOH   B O   
7108 O  O   . HOH   G .   ? 0.3269 0.4684 0.4776 -0.1491 0.0212  -0.0581 354 HOH   B O   
7109 O  O   . HOH   G .   ? 0.5371 0.3826 0.3994 0.0549  0.1249  -0.0615 355 HOH   B O   
7110 O  O   . HOH   G .   ? 0.3542 0.2699 0.3663 -0.0956 0.0180  -0.0637 356 HOH   B O   
7111 O  O   . HOH   G .   ? 0.4585 0.3197 0.5372 -0.1146 0.1525  0.0423  357 HOH   B O   
7112 O  O   . HOH   G .   ? 0.4740 0.5168 0.4756 0.1709  -0.1251 0.1400  358 HOH   B O   
7113 O  O   . HOH   G .   ? 0.5032 0.3602 0.5063 -0.0088 -0.1431 -0.0740 359 HOH   B O   
7114 O  O   . HOH   G .   ? 0.4851 0.4148 0.5821 0.0449  0.0930  0.1295  360 HOH   B O   
7115 O  O   . HOH   G .   ? 0.4681 0.6006 0.2923 0.2099  0.0079  0.0161  361 HOH   B O   
7116 O  O   . HOH   G .   ? 0.2207 0.4025 0.6488 -0.0961 -0.0565 -0.0645 362 HOH   B O   
7117 O  O   . HOH   G .   ? 0.4858 0.5046 0.4970 -0.0213 -0.0298 0.0472  363 HOH   B O   
7118 O  O   . HOH   G .   ? 0.5105 0.3059 0.5099 -0.1445 -0.0210 0.0179  364 HOH   B O   
7119 O  O   . HOH   G .   ? 0.5854 0.2334 0.3643 0.0039  -0.0012 0.0743  365 HOH   B O   
7120 O  O   . HOH   G .   ? 0.5904 0.4392 0.4227 0.0949  0.0431  0.0584  366 HOH   B O   
7121 O  O   . HOH   G .   ? 0.4370 0.3757 0.5212 0.1004  -0.1248 -0.0079 367 HOH   B O   
7122 O  O   . HOH   G .   ? 0.5193 0.5173 0.4639 -0.0640 -0.0508 -0.1034 368 HOH   B O   
7123 O  O   . HOH   G .   ? 0.5144 0.5967 0.3453 0.1727  -0.1404 0.0667  369 HOH   B O   
7124 O  O   . HOH   G .   ? 0.4184 0.5489 0.4967 0.2442  0.0911  0.1332  370 HOH   B O   
7125 O  O   . HOH   G .   ? 0.7468 0.7376 0.5120 0.2165  -0.1339 0.0891  371 HOH   B O   
7126 O  O   . HOH   G .   ? 0.5977 0.3671 0.3001 -0.1180 -0.1078 -0.0355 372 HOH   B O   
7127 O  O   . HOH   G .   ? 0.4493 0.4813 0.4675 -0.0695 -0.0377 0.0182  373 HOH   B O   
7128 O  O   . HOH   G .   ? 0.3915 0.3295 0.4032 0.0783  -0.1421 -0.0611 374 HOH   B O   
7129 O  O   . HOH   G .   ? 0.4563 0.6877 0.5804 0.1361  0.0426  0.2753  375 HOH   B O   
7130 O  O   . HOH   G .   ? 0.2369 0.4233 0.3924 0.0092  -0.0369 -0.0670 376 HOH   B O   
7131 O  O   . HOH   G .   ? 0.5161 0.6927 0.3800 -0.1440 0.0368  -0.1426 377 HOH   B O   
7132 O  O   . HOH   G .   ? 0.2972 0.4600 0.2195 0.0244  0.0177  0.0015  378 HOH   B O   
7133 O  O   . HOH   G .   ? 0.6752 0.3782 0.4925 -0.0861 -0.0775 0.0253  379 HOH   B O   
7134 O  O   . HOH   G .   ? 0.3854 0.4881 0.5223 0.0431  -0.0510 -0.0447 380 HOH   B O   
7135 O  O   . HOH   G .   ? 0.5264 0.6353 0.5961 -0.0159 0.1653  0.1423  381 HOH   B O   
7136 O  O   . HOH   G .   ? 0.3227 0.2668 0.2993 0.0275  0.0102  0.0269  382 HOH   B O   
7137 O  O   . HOH   G .   ? 0.3919 0.7546 0.5367 0.0375  0.1535  0.0382  383 HOH   B O   
7138 O  O   . HOH   G .   ? 0.4806 0.5103 0.4528 -0.0127 -0.0540 -0.0485 384 HOH   B O   
7139 O  O   . HOH   G .   ? 0.6461 0.4052 0.3954 0.0746  0.0868  -0.0710 385 HOH   B O   
7140 O  O   . HOH   G .   ? 0.6707 0.5717 0.4299 0.2278  0.0228  -0.0239 386 HOH   B O   
7141 O  O   . HOH   G .   ? 0.2337 0.4099 0.3881 -0.0712 -0.0909 -0.0189 387 HOH   B O   
7142 O  O   . HOH   G .   ? 0.5604 0.4284 0.5248 -0.0712 0.0346  -0.0278 388 HOH   B O   
7143 O  O   . HOH   G .   ? 0.4720 0.3616 0.3320 0.0147  0.0798  -0.0213 389 HOH   B O   
7144 O  O   . HOH   G .   ? 0.3821 0.2159 0.3650 0.0683  -0.0487 0.0148  390 HOH   B O   
7145 O  O   . HOH   G .   ? 0.5042 0.4289 0.4493 0.0312  0.0814  0.0524  391 HOH   B O   
7146 O  O   . HOH   G .   ? 0.4360 0.2227 0.5115 -0.0395 0.0758  0.0746  392 HOH   B O   
7147 O  O   . HOH   G .   ? 0.2446 0.3917 0.6199 -0.1055 -0.0567 0.0067  393 HOH   B O   
7148 O  O   . HOH   G .   ? 0.4426 0.5842 0.4121 0.1370  0.0030  -0.0731 394 HOH   B O   
7149 O  O   . HOH   G .   ? 0.3268 0.3660 0.3989 0.0064  0.0316  -0.0603 395 HOH   B O   
7150 O  O   . HOH   G .   ? 0.2073 0.2828 0.5717 -0.0626 -0.0859 0.0355  396 HOH   B O   
7151 O  O   . HOH   G .   ? 0.4593 0.4399 0.4680 0.0494  0.1103  0.1012  397 HOH   B O   
7152 O  O   . HOH   G .   ? 0.5714 0.4344 0.3203 -0.2287 -0.0414 0.1231  398 HOH   B O   
7153 O  O   . HOH   G .   ? 0.5710 0.6109 0.6535 0.0730  -0.1342 0.1536  399 HOH   B O   
7154 O  O   . HOH   G .   ? 0.5231 0.5504 0.3449 0.1421  -0.0059 -0.0283 400 HOH   B O   
# 
