data_7HDJ
# 
_entry.id   7HDJ 
# 
_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   7HDJ         pdb_00007hdj 10.2210/pdb7hdj/pdb 
WWPDB D_1001407337 ?            ?                   
# 
_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                        7HDJ 
_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 '[(7S)-6-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-6-azaspiro[3.4]octan-7-yl]methanol' 258.319   2   ? ? ? ? 
4 water       nat water                                                                          18.015    421 ? ? ? ? 
# 
_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 '[(7S)-6-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-6-azaspiro[3.4]octan-7-yl]methanol' A1A8H 
4 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 
A1A8H non-polymer         . '[(7S)-6-(7H-pyrrolo[2,3-d]pyrimidin-4-yl)-6-azaspiro[3.4]octan-7-yl]methanol' ? 'C14 H18 N4 O'   
258.319 
ALA   'L-peptide linking' y ALANINE                                                                        ? 'C3 H7 N O2'     
89.093  
ARG   'L-peptide linking' y ARGININE                                                                       ? 'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                                                                     ? 'C4 H8 N2 O3'    
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                                                                ? 'C4 H7 N O4'     
133.103 
CYS   'L-peptide linking' y CYSTEINE                                                                       ? 'C3 H7 N O2 S'   
121.158 
GLN   'L-peptide linking' y GLUTAMINE                                                                      ? 'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                                                                ? 'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                                                                        ? 'C2 H5 N O2'     
75.067  
HIS   'L-peptide linking' y HISTIDINE                                                                      ? 'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                                                          ? 'H2 O'           
18.015  
ILE   'L-peptide linking' y ISOLEUCINE                                                                     ? 'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                                                                        ? 'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                                                                         ? 'C6 H15 N2 O2 1' 
147.195 
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 A1A8H 1   202 201  A1A8H LA1 A . 
E 3 A1A8H 1   203 301  A1A8H LA2 A . 
F 4 HOH   1   301 6    HOH   HOH A . 
F 4 HOH   2   302 393  HOH   HOH A . 
F 4 HOH   3   303 192  HOH   HOH A . 
F 4 HOH   4   304 292  HOH   HOH A . 
F 4 HOH   5   305 153  HOH   HOH A . 
F 4 HOH   6   306 136  HOH   HOH A . 
F 4 HOH   7   307 196  HOH   HOH A . 
F 4 HOH   8   308 625  HOH   HOH A . 
F 4 HOH   9   309 229  HOH   HOH A . 
F 4 HOH   10  310 109  HOH   HOH A . 
F 4 HOH   11  311 952  HOH   HOH A . 
F 4 HOH   12  312 409  HOH   HOH A . 
F 4 HOH   13  313 209  HOH   HOH A . 
F 4 HOH   14  314 247  HOH   HOH A . 
F 4 HOH   15  315 1300 HOH   HOH A . 
F 4 HOH   16  316 5    HOH   HOH A . 
F 4 HOH   17  317 1296 HOH   HOH A . 
F 4 HOH   18  318 57   HOH   HOH A . 
F 4 HOH   19  319 337  HOH   HOH A . 
F 4 HOH   20  320 93   HOH   HOH A . 
F 4 HOH   21  321 1283 HOH   HOH A . 
F 4 HOH   22  322 1295 HOH   HOH A . 
F 4 HOH   23  323 661  HOH   HOH A . 
F 4 HOH   24  324 26   HOH   HOH A . 
F 4 HOH   25  325 155  HOH   HOH A . 
F 4 HOH   26  326 1301 HOH   HOH A . 
F 4 HOH   27  327 461  HOH   HOH A . 
F 4 HOH   28  328 124  HOH   HOH A . 
F 4 HOH   29  329 405  HOH   HOH A . 
F 4 HOH   30  330 86   HOH   HOH A . 
F 4 HOH   31  331 35   HOH   HOH A . 
F 4 HOH   32  332 132  HOH   HOH A . 
F 4 HOH   33  333 164  HOH   HOH A . 
F 4 HOH   34  334 354  HOH   HOH A . 
F 4 HOH   35  335 76   HOH   HOH A . 
F 4 HOH   36  336 96   HOH   HOH A . 
F 4 HOH   37  337 33   HOH   HOH A . 
F 4 HOH   38  338 18   HOH   HOH A . 
F 4 HOH   39  339 151  HOH   HOH A . 
F 4 HOH   40  340 15   HOH   HOH A . 
F 4 HOH   41  341 49   HOH   HOH A . 
F 4 HOH   42  342 281  HOH   HOH A . 
F 4 HOH   43  343 56   HOH   HOH A . 
F 4 HOH   44  344 1290 HOH   HOH A . 
F 4 HOH   45  345 21   HOH   HOH A . 
F 4 HOH   46  346 241  HOH   HOH A . 
F 4 HOH   47  347 1310 HOH   HOH A . 
F 4 HOH   48  348 630  HOH   HOH A . 
F 4 HOH   49  349 140  HOH   HOH A . 
F 4 HOH   50  350 169  HOH   HOH A . 
F 4 HOH   51  351 236  HOH   HOH A . 
F 4 HOH   52  352 83   HOH   HOH A . 
F 4 HOH   53  353 102  HOH   HOH A . 
F 4 HOH   54  354 396  HOH   HOH A . 
F 4 HOH   55  355 165  HOH   HOH A . 
F 4 HOH   56  356 39   HOH   HOH A . 
F 4 HOH   57  357 17   HOH   HOH A . 
F 4 HOH   58  358 148  HOH   HOH A . 
F 4 HOH   59  359 469  HOH   HOH A . 
F 4 HOH   60  360 225  HOH   HOH A . 
F 4 HOH   61  361 662  HOH   HOH A . 
F 4 HOH   62  362 964  HOH   HOH A . 
F 4 HOH   63  363 320  HOH   HOH A . 
F 4 HOH   64  364 36   HOH   HOH A . 
F 4 HOH   65  365 218  HOH   HOH A . 
F 4 HOH   66  366 46   HOH   HOH A . 
F 4 HOH   67  367 19   HOH   HOH A . 
F 4 HOH   68  368 2    HOH   HOH A . 
F 4 HOH   69  369 42   HOH   HOH A . 
F 4 HOH   70  370 12   HOH   HOH A . 
F 4 HOH   71  371 4    HOH   HOH A . 
F 4 HOH   72  372 8    HOH   HOH A . 
F 4 HOH   73  373 85   HOH   HOH A . 
F 4 HOH   74  374 139  HOH   HOH A . 
F 4 HOH   75  375 74   HOH   HOH A . 
F 4 HOH   76  376 66   HOH   HOH A . 
F 4 HOH   77  377 92   HOH   HOH A . 
F 4 HOH   78  378 81   HOH   HOH A . 
F 4 HOH   79  379 5    HOH   HOH A . 
F 4 HOH   80  380 105  HOH   HOH A . 
F 4 HOH   81  381 154  HOH   HOH A . 
F 4 HOH   82  382 278  HOH   HOH A . 
F 4 HOH   83  383 6    HOH   HOH A . 
F 4 HOH   84  384 162  HOH   HOH A . 
F 4 HOH   85  385 27   HOH   HOH A . 
F 4 HOH   86  386 138  HOH   HOH A . 
F 4 HOH   87  387 45   HOH   HOH A . 
F 4 HOH   88  388 3    HOH   HOH A . 
F 4 HOH   89  389 366  HOH   HOH A . 
F 4 HOH   90  390 116  HOH   HOH A . 
F 4 HOH   91  391 134  HOH   HOH A . 
F 4 HOH   92  392 140  HOH   HOH A . 
F 4 HOH   93  393 212  HOH   HOH A . 
F 4 HOH   94  394 1308 HOH   HOH A . 
F 4 HOH   95  395 1315 HOH   HOH A . 
F 4 HOH   96  396 939  HOH   HOH A . 
F 4 HOH   97  397 381  HOH   HOH A . 
F 4 HOH   98  398 67   HOH   HOH A . 
F 4 HOH   99  399 199  HOH   HOH A . 
F 4 HOH   100 400 34   HOH   HOH A . 
F 4 HOH   101 401 1313 HOH   HOH A . 
F 4 HOH   102 402 58   HOH   HOH A . 
F 4 HOH   103 403 78   HOH   HOH A . 
F 4 HOH   104 404 186  HOH   HOH A . 
F 4 HOH   105 405 2    HOH   HOH A . 
F 4 HOH   106 406 68   HOH   HOH A . 
F 4 HOH   107 407 159  HOH   HOH A . 
F 4 HOH   108 408 25   HOH   HOH A . 
F 4 HOH   109 409 115  HOH   HOH A . 
F 4 HOH   110 410 493  HOH   HOH A . 
F 4 HOH   111 411 1068 HOH   HOH A . 
F 4 HOH   112 412 122  HOH   HOH A . 
F 4 HOH   113 413 303  HOH   HOH A . 
F 4 HOH   114 414 1289 HOH   HOH A . 
F 4 HOH   115 415 333  HOH   HOH A . 
F 4 HOH   116 416 125  HOH   HOH A . 
F 4 HOH   117 417 53   HOH   HOH A . 
F 4 HOH   118 418 582  HOH   HOH A . 
F 4 HOH   119 419 24   HOH   HOH A . 
F 4 HOH   120 420 7    HOH   HOH A . 
F 4 HOH   121 421 195  HOH   HOH A . 
F 4 HOH   122 422 156  HOH   HOH A . 
F 4 HOH   123 423 944  HOH   HOH A . 
F 4 HOH   124 424 121  HOH   HOH A . 
F 4 HOH   125 425 123  HOH   HOH A . 
F 4 HOH   126 426 1222 HOH   HOH A . 
F 4 HOH   127 427 70   HOH   HOH A . 
F 4 HOH   128 428 95   HOH   HOH A . 
F 4 HOH   129 429 51   HOH   HOH A . 
F 4 HOH   130 430 40   HOH   HOH A . 
F 4 HOH   131 431 4    HOH   HOH A . 
F 4 HOH   132 432 1238 HOH   HOH A . 
F 4 HOH   133 433 397  HOH   HOH A . 
F 4 HOH   134 434 351  HOH   HOH A . 
F 4 HOH   135 435 1275 HOH   HOH A . 
F 4 HOH   136 436 80   HOH   HOH A . 
F 4 HOH   137 437 1134 HOH   HOH A . 
F 4 HOH   138 438 1279 HOH   HOH A . 
F 4 HOH   139 439 576  HOH   HOH A . 
F 4 HOH   140 440 71   HOH   HOH A . 
F 4 HOH   141 441 296  HOH   HOH A . 
F 4 HOH   142 442 16   HOH   HOH A . 
F 4 HOH   143 443 11   HOH   HOH A . 
F 4 HOH   144 444 94   HOH   HOH A . 
F 4 HOH   145 445 104  HOH   HOH A . 
F 4 HOH   146 446 7    HOH   HOH A . 
F 4 HOH   147 447 1189 HOH   HOH A . 
F 4 HOH   148 448 1094 HOH   HOH A . 
F 4 HOH   149 449 188  HOH   HOH A . 
F 4 HOH   150 450 73   HOH   HOH A . 
F 4 HOH   151 451 1309 HOH   HOH A . 
F 4 HOH   152 452 97   HOH   HOH A . 
F 4 HOH   153 453 79   HOH   HOH A . 
F 4 HOH   154 454 1286 HOH   HOH A . 
F 4 HOH   155 455 1    HOH   HOH A . 
F 4 HOH   156 456 330  HOH   HOH A . 
F 4 HOH   157 457 726  HOH   HOH A . 
F 4 HOH   158 458 509  HOH   HOH A . 
F 4 HOH   159 459 107  HOH   HOH A . 
F 4 HOH   160 460 163  HOH   HOH A . 
F 4 HOH   161 461 1119 HOH   HOH A . 
F 4 HOH   162 462 408  HOH   HOH A . 
F 4 HOH   163 463 3    HOH   HOH A . 
F 4 HOH   164 464 756  HOH   HOH A . 
F 4 HOH   165 465 370  HOH   HOH A . 
F 4 HOH   166 466 342  HOH   HOH A . 
F 4 HOH   167 467 801  HOH   HOH A . 
F 4 HOH   168 468 319  HOH   HOH A . 
F 4 HOH   169 469 361  HOH   HOH A . 
F 4 HOH   170 470 126  HOH   HOH A . 
F 4 HOH   171 471 63   HOH   HOH A . 
F 4 HOH   172 472 556  HOH   HOH A . 
F 4 HOH   173 473 1307 HOH   HOH A . 
F 4 HOH   174 474 224  HOH   HOH A . 
F 4 HOH   175 475 280  HOH   HOH A . 
F 4 HOH   176 476 1276 HOH   HOH A . 
F 4 HOH   177 477 250  HOH   HOH A . 
F 4 HOH   178 478 521  HOH   HOH A . 
F 4 HOH   179 479 1284 HOH   HOH A . 
F 4 HOH   180 480 1287 HOH   HOH A . 
F 4 HOH   181 481 202  HOH   HOH A . 
F 4 HOH   182 482 135  HOH   HOH A . 
F 4 HOH   183 483 1306 HOH   HOH A . 
F 4 HOH   184 484 674  HOH   HOH A . 
F 4 HOH   185 485 12   HOH   HOH A . 
F 4 HOH   186 486 695  HOH   HOH A . 
F 4 HOH   187 487 711  HOH   HOH A . 
F 4 HOH   188 488 318  HOH   HOH A . 
F 4 HOH   189 489 919  HOH   HOH A . 
F 4 HOH   190 490 1299 HOH   HOH A . 
F 4 HOH   191 491 267  HOH   HOH A . 
F 4 HOH   192 492 315  HOH   HOH A . 
F 4 HOH   193 493 331  HOH   HOH A . 
F 4 HOH   194 494 941  HOH   HOH A . 
F 4 HOH   195 495 309  HOH   HOH A . 
F 4 HOH   196 496 1314 HOH   HOH A . 
F 4 HOH   197 497 208  HOH   HOH A . 
F 4 HOH   198 498 805  HOH   HOH A . 
F 4 HOH   199 499 152  HOH   HOH A . 
F 4 HOH   200 500 263  HOH   HOH A . 
F 4 HOH   201 501 356  HOH   HOH A . 
F 4 HOH   202 502 326  HOH   HOH A . 
F 4 HOH   203 503 8    HOH   HOH A . 
F 4 HOH   204 504 1071 HOH   HOH A . 
F 4 HOH   205 505 350  HOH   HOH A . 
F 4 HOH   206 506 180  HOH   HOH A . 
F 4 HOH   207 507 363  HOH   HOH A . 
F 4 HOH   208 508 371  HOH   HOH A . 
F 4 HOH   209 509 313  HOH   HOH A . 
F 4 HOH   210 510 185  HOH   HOH A . 
F 4 HOH   211 511 429  HOH   HOH A . 
F 4 HOH   212 512 70   HOH   HOH A . 
F 4 HOH   213 513 772  HOH   HOH A . 
F 4 HOH   214 514 10   HOH   HOH A . 
F 4 HOH   215 515 376  HOH   HOH A . 
F 4 HOH   216 516 1074 HOH   HOH A . 
F 4 HOH   217 517 1292 HOH   HOH A . 
F 4 HOH   218 518 346  HOH   HOH A . 
F 4 HOH   219 519 9    HOH   HOH A . 
F 4 HOH   220 520 1078 HOH   HOH A . 
G 4 HOH   1   201 64   HOH   HOH B . 
G 4 HOH   2   202 240  HOH   HOH B . 
G 4 HOH   3   203 549  HOH   HOH B . 
G 4 HOH   4   204 120  HOH   HOH B . 
G 4 HOH   5   205 232  HOH   HOH B . 
G 4 HOH   6   206 1249 HOH   HOH B . 
G 4 HOH   7   207 364  HOH   HOH B . 
G 4 HOH   8   208 205  HOH   HOH B . 
G 4 HOH   9   209 50   HOH   HOH B . 
G 4 HOH   10  210 398  HOH   HOH B . 
G 4 HOH   11  211 900  HOH   HOH B . 
G 4 HOH   12  212 172  HOH   HOH B . 
G 4 HOH   13  213 452  HOH   HOH B . 
G 4 HOH   14  214 264  HOH   HOH B . 
G 4 HOH   15  215 353  HOH   HOH B . 
G 4 HOH   16  216 332  HOH   HOH B . 
G 4 HOH   17  217 1278 HOH   HOH B . 
G 4 HOH   18  218 531  HOH   HOH B . 
G 4 HOH   19  219 75   HOH   HOH B . 
G 4 HOH   20  220 743  HOH   HOH B . 
G 4 HOH   21  221 758  HOH   HOH B . 
G 4 HOH   22  222 1140 HOH   HOH B . 
G 4 HOH   23  223 654  HOH   HOH B . 
G 4 HOH   24  224 391  HOH   HOH B . 
G 4 HOH   25  225 82   HOH   HOH B . 
G 4 HOH   26  226 54   HOH   HOH B . 
G 4 HOH   27  227 444  HOH   HOH B . 
G 4 HOH   28  228 110  HOH   HOH B . 
G 4 HOH   29  229 276  HOH   HOH B . 
G 4 HOH   30  230 131  HOH   HOH B . 
G 4 HOH   31  231 1    HOH   HOH B . 
G 4 HOH   32  232 69   HOH   HOH B . 
G 4 HOH   33  233 325  HOH   HOH B . 
G 4 HOH   34  234 358  HOH   HOH B . 
G 4 HOH   35  235 181  HOH   HOH B . 
G 4 HOH   36  236 166  HOH   HOH B . 
G 4 HOH   37  237 127  HOH   HOH B . 
G 4 HOH   38  238 52   HOH   HOH B . 
G 4 HOH   39  239 60   HOH   HOH B . 
G 4 HOH   40  240 133  HOH   HOH B . 
G 4 HOH   41  241 221  HOH   HOH B . 
G 4 HOH   42  242 9    HOH   HOH B . 
G 4 HOH   43  243 62   HOH   HOH B . 
G 4 HOH   44  244 300  HOH   HOH B . 
G 4 HOH   45  245 14   HOH   HOH B . 
G 4 HOH   46  246 723  HOH   HOH B . 
G 4 HOH   47  247 41   HOH   HOH B . 
G 4 HOH   48  248 31   HOH   HOH B . 
G 4 HOH   49  249 30   HOH   HOH B . 
G 4 HOH   50  250 129  HOH   HOH B . 
G 4 HOH   51  251 103  HOH   HOH B . 
G 4 HOH   52  252 343  HOH   HOH B . 
G 4 HOH   53  253 128  HOH   HOH B . 
G 4 HOH   54  254 243  HOH   HOH B . 
G 4 HOH   55  255 144  HOH   HOH B . 
G 4 HOH   56  256 150  HOH   HOH B . 
G 4 HOH   57  257 47   HOH   HOH B . 
G 4 HOH   58  258 272  HOH   HOH B . 
G 4 HOH   59  259 10   HOH   HOH B . 
G 4 HOH   60  260 147  HOH   HOH B . 
G 4 HOH   61  261 282  HOH   HOH B . 
G 4 HOH   62  262 72   HOH   HOH B . 
G 4 HOH   63  263 287  HOH   HOH B . 
G 4 HOH   64  264 1312 HOH   HOH B . 
G 4 HOH   65  265 59   HOH   HOH B . 
G 4 HOH   66  266 242  HOH   HOH B . 
G 4 HOH   67  267 20   HOH   HOH B . 
G 4 HOH   68  268 271  HOH   HOH B . 
G 4 HOH   69  269 231  HOH   HOH B . 
G 4 HOH   70  270 302  HOH   HOH B . 
G 4 HOH   71  271 175  HOH   HOH B . 
G 4 HOH   72  272 143  HOH   HOH B . 
G 4 HOH   73  273 1277 HOH   HOH B . 
G 4 HOH   74  274 11   HOH   HOH B . 
G 4 HOH   75  275 1285 HOH   HOH B . 
G 4 HOH   76  276 347  HOH   HOH B . 
G 4 HOH   77  277 117  HOH   HOH B . 
G 4 HOH   78  278 252  HOH   HOH B . 
G 4 HOH   79  279 61   HOH   HOH B . 
G 4 HOH   80  280 114  HOH   HOH B . 
G 4 HOH   81  281 77   HOH   HOH B . 
G 4 HOH   82  282 207  HOH   HOH B . 
G 4 HOH   83  283 84   HOH   HOH B . 
G 4 HOH   84  284 1106 HOH   HOH B . 
G 4 HOH   85  285 22   HOH   HOH B . 
G 4 HOH   86  286 220  HOH   HOH B . 
G 4 HOH   87  287 197  HOH   HOH B . 
G 4 HOH   88  288 235  HOH   HOH B . 
G 4 HOH   89  289 89   HOH   HOH B . 
G 4 HOH   90  290 43   HOH   HOH B . 
G 4 HOH   91  291 13   HOH   HOH B . 
G 4 HOH   92  292 1066 HOH   HOH B . 
G 4 HOH   93  293 99   HOH   HOH B . 
G 4 HOH   94  294 216  HOH   HOH B . 
G 4 HOH   95  295 106  HOH   HOH B . 
G 4 HOH   96  296 160  HOH   HOH B . 
G 4 HOH   97  297 88   HOH   HOH B . 
G 4 HOH   98  298 316  HOH   HOH B . 
G 4 HOH   99  299 297  HOH   HOH B . 
G 4 HOH   100 300 416  HOH   HOH B . 
G 4 HOH   101 301 137  HOH   HOH B . 
G 4 HOH   102 302 635  HOH   HOH B . 
G 4 HOH   103 303 215  HOH   HOH B . 
G 4 HOH   104 304 38   HOH   HOH B . 
G 4 HOH   105 305 311  HOH   HOH B . 
G 4 HOH   106 306 112  HOH   HOH B . 
G 4 HOH   107 307 170  HOH   HOH B . 
G 4 HOH   108 308 1274 HOH   HOH B . 
G 4 HOH   109 309 32   HOH   HOH B . 
G 4 HOH   110 310 44   HOH   HOH B . 
G 4 HOH   111 311 142  HOH   HOH B . 
G 4 HOH   112 312 299  HOH   HOH B . 
G 4 HOH   113 313 1305 HOH   HOH B . 
G 4 HOH   114 314 118  HOH   HOH B . 
G 4 HOH   115 315 101  HOH   HOH B . 
G 4 HOH   116 316 100  HOH   HOH B . 
G 4 HOH   117 317 37   HOH   HOH B . 
G 4 HOH   118 318 23   HOH   HOH B . 
G 4 HOH   119 319 1294 HOH   HOH B . 
G 4 HOH   120 320 182  HOH   HOH B . 
G 4 HOH   121 321 91   HOH   HOH B . 
G 4 HOH   122 322 28   HOH   HOH B . 
G 4 HOH   123 323 48   HOH   HOH B . 
G 4 HOH   124 324 387  HOH   HOH B . 
G 4 HOH   125 325 177  HOH   HOH B . 
G 4 HOH   126 326 341  HOH   HOH B . 
G 4 HOH   127 327 161  HOH   HOH B . 
G 4 HOH   128 328 717  HOH   HOH B . 
G 4 HOH   129 329 334  HOH   HOH B . 
G 4 HOH   130 330 98   HOH   HOH B . 
G 4 HOH   131 331 29   HOH   HOH B . 
G 4 HOH   132 332 141  HOH   HOH B . 
G 4 HOH   133 333 55   HOH   HOH B . 
G 4 HOH   134 334 1291 HOH   HOH B . 
G 4 HOH   135 335 704  HOH   HOH B . 
G 4 HOH   136 336 1126 HOH   HOH B . 
G 4 HOH   137 337 65   HOH   HOH B . 
G 4 HOH   138 338 1293 HOH   HOH B . 
G 4 HOH   139 339 362  HOH   HOH B . 
G 4 HOH   140 340 234  HOH   HOH B . 
G 4 HOH   141 341 619  HOH   HOH B . 
G 4 HOH   142 342 445  HOH   HOH B . 
G 4 HOH   143 343 87   HOH   HOH B . 
G 4 HOH   144 344 339  HOH   HOH B . 
G 4 HOH   145 345 960  HOH   HOH B . 
G 4 HOH   146 346 178  HOH   HOH B . 
G 4 HOH   147 347 1304 HOH   HOH B . 
G 4 HOH   148 348 463  HOH   HOH B . 
G 4 HOH   149 349 90   HOH   HOH B . 
G 4 HOH   150 350 191  HOH   HOH B . 
G 4 HOH   151 351 203  HOH   HOH B . 
G 4 HOH   152 352 1046 HOH   HOH B . 
G 4 HOH   153 353 623  HOH   HOH B . 
G 4 HOH   154 354 1280 HOH   HOH B . 
G 4 HOH   155 355 335  HOH   HOH B . 
G 4 HOH   156 356 304  HOH   HOH B . 
G 4 HOH   157 357 290  HOH   HOH B . 
G 4 HOH   158 358 541  HOH   HOH B . 
G 4 HOH   159 359 1077 HOH   HOH B . 
G 4 HOH   160 360 479  HOH   HOH B . 
G 4 HOH   161 361 389  HOH   HOH B . 
G 4 HOH   162 362 1072 HOH   HOH B . 
G 4 HOH   163 363 718  HOH   HOH B . 
G 4 HOH   164 364 283  HOH   HOH B . 
G 4 HOH   165 365 615  HOH   HOH B . 
G 4 HOH   166 366 291  HOH   HOH B . 
G 4 HOH   167 367 340  HOH   HOH B . 
G 4 HOH   168 368 1316 HOH   HOH B . 
G 4 HOH   169 369 667  HOH   HOH B . 
G 4 HOH   170 370 898  HOH   HOH B . 
G 4 HOH   171 371 1303 HOH   HOH B . 
G 4 HOH   172 372 373  HOH   HOH B . 
G 4 HOH   173 373 431  HOH   HOH B . 
G 4 HOH   174 374 1173 HOH   HOH B . 
G 4 HOH   175 375 190  HOH   HOH B . 
G 4 HOH   176 376 310  HOH   HOH B . 
G 4 HOH   177 377 183  HOH   HOH B . 
G 4 HOH   178 378 418  HOH   HOH B . 
G 4 HOH   179 379 1163 HOH   HOH B . 
G 4 HOH   180 380 149  HOH   HOH B . 
G 4 HOH   181 381 1000 HOH   HOH B . 
G 4 HOH   182 382 491  HOH   HOH B . 
G 4 HOH   183 383 424  HOH   HOH B . 
G 4 HOH   184 384 1311 HOH   HOH B . 
G 4 HOH   185 385 176  HOH   HOH B . 
G 4 HOH   186 386 981  HOH   HOH B . 
G 4 HOH   187 387 1298 HOH   HOH B . 
G 4 HOH   188 388 470  HOH   HOH B . 
G 4 HOH   189 389 265  HOH   HOH B . 
G 4 HOH   190 390 248  HOH   HOH B . 
G 4 HOH   191 391 184  HOH   HOH B . 
G 4 HOH   192 392 360  HOH   HOH B . 
G 4 HOH   193 393 410  HOH   HOH B . 
G 4 HOH   194 394 355  HOH   HOH B . 
G 4 HOH   195 395 314  HOH   HOH B . 
G 4 HOH   196 396 274  HOH   HOH B . 
G 4 HOH   197 397 566  HOH   HOH B . 
G 4 HOH   198 398 157  HOH   HOH B . 
G 4 HOH   199 399 321  HOH   HOH B . 
G 4 HOH   200 400 792  HOH   HOH B . 
G 4 HOH   201 401 558  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           7HDJ 
_cell.length_a           88.930 
_cell.length_b           88.930 
_cell.length_c           39.412 
_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                         7HDJ 
_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          7HDJ 
# 
_exptl_crystal.id                    1 
_exptl_crystal.density_Matthews      2.15 
_exptl_crystal.density_percent_sol   42.71 
_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   2023-05-20 
_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                     7HDJ 
_reflns.pdbx_diffrn_id               1 
_reflns.pdbx_ordinal                 1 
_reflns.observed_criterion_sigma_I   ? 
_reflns.observed_criterion_sigma_F   ? 
_reflns.d_resolution_low             44.470 
_reflns.d_resolution_high            1.060 
_reflns.number_obs                   139166 
_reflns.number_all                   ? 
_reflns.percent_possible_obs         99.700 
_reflns.pdbx_Rmerge_I_obs            0.064 
_reflns.pdbx_Rsym_value              ? 
_reflns.pdbx_netI_over_sigmaI        10.400 
_reflns.B_iso_Wilson_estimate        13.820 
_reflns.pdbx_redundancy              6.400 
_reflns.pdbx_Rrim_I_all              0.070 
_reflns.pdbx_Rpim_I_all              0.028 
_reflns.pdbx_CC_half                 0.999 
_reflns.pdbx_netI_over_av_sigmaI     ? 
_reflns.pdbx_number_measured_all     891982 
_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 1.060 1.080  ? 40946 6544 ? 2.276 ? ? ? 6.300 ? 0.600  ? ? ? ? ? ? 95.000 2.481 0.976 0.391 
1 2 5.810 44.470 ? 6347  930  ? 0.026 ? ? ? 6.800 ? 39.800 ? ? ? ? ? ? 99.700 0.028 0.011 0.999 
# 
_refine.entry_id                                 7HDJ 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_d_res_high                            1.0600 
_refine.ls_d_res_low                             44.4700 
_refine.pdbx_ls_sigma_F                          1.340 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.ls_percent_reflns_obs                    99.6600 
_refine.ls_number_reflns_obs                     138979 
_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                          0.1573 
_refine.ls_R_factor_R_work                       0.1563 
_refine.ls_wR_factor_R_work                      ? 
_refine.ls_R_factor_R_free                       0.1757 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_percent_reflns_R_free                 4.8000 
_refine.ls_number_reflns_R_free                  6671 
_refine.ls_number_reflns_R_work                  132308 
_refine.ls_R_factor_R_free_error                 ? 
_refine.B_iso_mean                               20.8425 
_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                            0.1700 
_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                                91.160 
_refine.B_iso_min                                9.110 
_refine.pdbx_overall_phase_error                 21.9700 
_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                       1.0600 
_refine_hist.d_res_low                        44.4700 
_refine_hist.pdbx_number_atoms_ligand         81 
_refine_hist.number_atoms_solvent             421 
_refine_hist.number_atoms_total               3044 
_refine_hist.pdbx_number_residues_total       336 
_refine_hist.pdbx_B_iso_mean_ligand           15.56 
_refine_hist.pdbx_B_iso_mean_solvent          33.72 
_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 
1.0600 1.0700  30 92.0000  4072 . 0.5192 0.5376 . 214 0.0000 4286 . 'X-RAY DIFFRACTION' 
1.0700 1.0900  30 100.0000 4397 . 0.4471 0.4958 . 215 0.0000 4612 . 'X-RAY DIFFRACTION' 
1.0900 1.1000  30 100.0000 4432 . 0.4186 0.4110 . 208 0.0000 4640 . 'X-RAY DIFFRACTION' 
1.1000 1.1100  30 100.0000 4334 . 0.3645 0.3707 . 226 0.0000 4560 . 'X-RAY DIFFRACTION' 
1.1100 1.1300  30 100.0000 4443 . 0.3414 0.3343 . 218 0.0000 4661 . 'X-RAY DIFFRACTION' 
1.1300 1.1400  30 100.0000 4414 . 0.3004 0.3094 . 193 0.0000 4607 . 'X-RAY DIFFRACTION' 
1.1400 1.1600  30 100.0000 4425 . 0.2804 0.2924 . 217 0.0000 4642 . 'X-RAY DIFFRACTION' 
1.1600 1.1800  30 100.0000 4344 . 0.2439 0.2762 . 231 0.0000 4575 . 'X-RAY DIFFRACTION' 
1.1800 1.1900  30 100.0000 4397 . 0.2297 0.2514 . 232 0.0000 4629 . 'X-RAY DIFFRACTION' 
1.1900 1.2100  30 100.0000 4384 . 0.1985 0.2387 . 248 0.0000 4632 . 'X-RAY DIFFRACTION' 
1.2100 1.2400  30 100.0000 4488 . 0.1898 0.2226 . 182 0.0000 4670 . 'X-RAY DIFFRACTION' 
1.2400 1.2600  30 100.0000 4372 . 0.1870 0.2131 . 223 0.0000 4595 . 'X-RAY DIFFRACTION' 
1.2600 1.2800  30 100.0000 4379 . 0.1811 0.1958 . 229 0.0000 4608 . 'X-RAY DIFFRACTION' 
1.2800 1.3100  30 100.0000 4448 . 0.1722 0.1945 . 218 0.0000 4666 . 'X-RAY DIFFRACTION' 
1.3100 1.3400  30 100.0000 4340 . 0.1747 0.2096 . 245 0.0000 4585 . 'X-RAY DIFFRACTION' 
1.3400 1.3700  30 100.0000 4434 . 0.1662 0.1989 . 226 0.0000 4660 . 'X-RAY DIFFRACTION' 
1.3700 1.4000  30 100.0000 4417 . 0.1474 0.1844 . 220 0.0000 4637 . 'X-RAY DIFFRACTION' 
1.4000 1.4400  30 100.0000 4381 . 0.1378 0.1931 . 213 0.0000 4594 . 'X-RAY DIFFRACTION' 
1.4400 1.4800  30 100.0000 4468 . 0.1281 0.1453 . 215 0.0000 4683 . 'X-RAY DIFFRACTION' 
1.4800 1.5300  30 100.0000 4405 . 0.1192 0.1437 . 222 0.0000 4627 . 'X-RAY DIFFRACTION' 
1.5300 1.5800  30 100.0000 4438 . 0.1217 0.1555 . 234 0.0000 4672 . 'X-RAY DIFFRACTION' 
1.5800 1.6500  30 100.0000 4414 . 0.1245 0.1418 . 234 0.0000 4648 . 'X-RAY DIFFRACTION' 
1.6500 1.7200  30 100.0000 4424 . 0.1321 0.1535 . 193 0.0000 4617 . 'X-RAY DIFFRACTION' 
1.7200 1.8100  30 100.0000 4426 . 0.1363 0.1557 . 226 0.0000 4652 . 'X-RAY DIFFRACTION' 
1.8100 1.9300  30 100.0000 4417 . 0.1351 0.1505 . 238 0.0000 4655 . 'X-RAY DIFFRACTION' 
1.9300 2.0800  30 100.0000 4478 . 0.1435 0.1499 . 217 0.0000 4695 . 'X-RAY DIFFRACTION' 
2.0800 2.2900  30 100.0000 4386 . 0.1389 0.1524 . 263 0.0000 4649 . 'X-RAY DIFFRACTION' 
2.2900 2.6200  30 100.0000 4464 . 0.1407 0.1573 . 220 0.0000 4684 . 'X-RAY DIFFRACTION' 
2.6200 3.3000  30 100.0000 4513 . 0.1497 0.1714 . 216 0.0000 4729 . 'X-RAY DIFFRACTION' 
3.3000 44.4700 30 100.0000 4574 . 0.1459 0.1674 . 235 0.0000 4809 . 'X-RAY DIFFRACTION' 
# 
_struct.entry_id                  7HDJ 
_struct.title                     
'PanDDA analysis group deposition -- Crystal structure of SARS-CoV-2 NSP3 macrodomain in complex with AVI-0003728' 
_struct.pdbx_CASP_flag            ? 
_struct.pdbx_model_details        ? 
_struct.pdbx_model_type_details   ? 
# 
_struct_keywords.entry_id        7HDJ 
_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 3 ? 
F N N 4 ? 
G N N 4 ? 
# 
_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 7HDJ A 3 ? 169 ? P0DTD1 1025 ? 1191 ? 3 169 
2 1 7HDJ 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 7HDJ SER A 1 ? UNP P0DTD1 ? ? 'expression tag' 1 1 
1 7HDJ MET A 2 ? UNP P0DTD1 ? ? 'expression tag' 2 2 
2 7HDJ SER B 1 ? UNP P0DTD1 ? ? 'expression tag' 1 3 
2 7HDJ 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 ? PHE A 168 ? ASP A 157 PHE A 168 1 ? 12 
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 ALA B 124 ? N ALA B 124 
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                   7HDJ 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 HH  A TYR 161 ? B O A HOH 302 ? ? 1.58 
2 1 HD1 A HIS 91  ? A O A HOH 308 ? ? 1.60 
3 1 O   B HOH 218 ? ? O B HOH 287 ? ? 2.08 
4 1 OH  A TYR 161 ? B O A HOH 302 ? ? 2.19 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASN A 20 ? B -69.77  93.30   
2 1 HIS A 86 ? A 54.48   -129.52 
3 1 HIS A 86 ? B 59.37   -136.52 
4 1 SER B 5  ? ? -100.34 79.39   
5 1 HIS B 86 ? ? 57.90   -126.67 
# 
_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 518 ? 5.94 . 
2 1 O B A HOH 519 ? 6.37 . 
3 1 O ? A HOH 520 ? 7.66 . 
4 1 O ? B HOH 401 ? 6.39 . 
# 
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 
A1A8H N2   N Y N 1   
A1A8H C3   C N N 2   
A1A8H C6   C N N 3   
A1A8H C9   C Y N 4   
A1A8H C12  C Y N 5   
A1A8H C14  C Y N 6   
A1A8H C1   C N N 7   
A1A8H C10  C Y N 8   
A1A8H C11  C Y N 9   
A1A8H C13  C Y N 10  
A1A8H C2   C N S 11  
A1A8H C4   C N N 12  
A1A8H C5   C N N 13  
A1A8H C7   C N N 14  
A1A8H C8   C N N 15  
A1A8H N1   N N N 16  
A1A8H N3   N Y N 17  
A1A8H N4   N Y N 18  
A1A8H O1   O N N 19  
A1A8H H5   H N N 20  
A1A8H H6   H N N 21  
A1A8H H9   H N N 22  
A1A8H H10  H N N 23  
A1A8H H17  H N N 24  
A1A8H H3   H N N 25  
A1A8H H4   H N N 26  
A1A8H H15  H N N 27  
A1A8H H16  H N N 28  
A1A8H H1   H N N 29  
A1A8H H8   H N N 30  
A1A8H H7   H N N 31  
A1A8H H12  H N N 32  
A1A8H H11  H N N 33  
A1A8H H14  H N N 34  
A1A8H H13  H N N 35  
A1A8H H18  H N N 36  
A1A8H H2   H N N 37  
ALA   N    N N N 38  
ALA   CA   C N S 39  
ALA   C    C N N 40  
ALA   O    O N N 41  
ALA   CB   C N N 42  
ALA   OXT  O N N 43  
ALA   H    H N N 44  
ALA   H2   H N N 45  
ALA   HA   H N N 46  
ALA   HB1  H N N 47  
ALA   HB2  H N N 48  
ALA   HB3  H N N 49  
ALA   HXT  H N N 50  
ARG   N    N N N 51  
ARG   CA   C N S 52  
ARG   C    C N N 53  
ARG   O    O N N 54  
ARG   CB   C N N 55  
ARG   CG   C N N 56  
ARG   CD   C N N 57  
ARG   NE   N N N 58  
ARG   CZ   C N N 59  
ARG   NH1  N N N 60  
ARG   NH2  N N N 61  
ARG   OXT  O N N 62  
ARG   H    H N N 63  
ARG   H2   H N N 64  
ARG   HA   H N N 65  
ARG   HB2  H N N 66  
ARG   HB3  H N N 67  
ARG   HG2  H N N 68  
ARG   HG3  H N N 69  
ARG   HD2  H N N 70  
ARG   HD3  H N N 71  
ARG   HE   H N N 72  
ARG   HH11 H N N 73  
ARG   HH12 H N N 74  
ARG   HH21 H N N 75  
ARG   HH22 H N N 76  
ARG   HXT  H N N 77  
ASN   N    N N N 78  
ASN   CA   C N S 79  
ASN   C    C N N 80  
ASN   O    O N N 81  
ASN   CB   C N N 82  
ASN   CG   C N N 83  
ASN   OD1  O N N 84  
ASN   ND2  N N N 85  
ASN   OXT  O N N 86  
ASN   H    H N N 87  
ASN   H2   H N N 88  
ASN   HA   H N N 89  
ASN   HB2  H N N 90  
ASN   HB3  H N N 91  
ASN   HD21 H N N 92  
ASN   HD22 H N N 93  
ASN   HXT  H N N 94  
ASP   N    N N N 95  
ASP   CA   C N S 96  
ASP   C    C N N 97  
ASP   O    O N N 98  
ASP   CB   C N N 99  
ASP   CG   C N N 100 
ASP   OD1  O N N 101 
ASP   OD2  O N N 102 
ASP   OXT  O N N 103 
ASP   H    H N N 104 
ASP   H2   H N N 105 
ASP   HA   H N N 106 
ASP   HB2  H N N 107 
ASP   HB3  H N N 108 
ASP   HD2  H N N 109 
ASP   HXT  H N N 110 
CYS   N    N N N 111 
CYS   CA   C N R 112 
CYS   C    C N N 113 
CYS   O    O N N 114 
CYS   CB   C N N 115 
CYS   SG   S N N 116 
CYS   OXT  O N N 117 
CYS   H    H N N 118 
CYS   H2   H N N 119 
CYS   HA   H N N 120 
CYS   HB2  H N N 121 
CYS   HB3  H N N 122 
CYS   HG   H N N 123 
CYS   HXT  H N N 124 
GLN   N    N N N 125 
GLN   CA   C N S 126 
GLN   C    C N N 127 
GLN   O    O N N 128 
GLN   CB   C N N 129 
GLN   CG   C N N 130 
GLN   CD   C N N 131 
GLN   OE1  O N N 132 
GLN   NE2  N N N 133 
GLN   OXT  O N N 134 
GLN   H    H N N 135 
GLN   H2   H N N 136 
GLN   HA   H N N 137 
GLN   HB2  H N N 138 
GLN   HB3  H N N 139 
GLN   HG2  H N N 140 
GLN   HG3  H N N 141 
GLN   HE21 H N N 142 
GLN   HE22 H N N 143 
GLN   HXT  H N N 144 
GLU   N    N N N 145 
GLU   CA   C N S 146 
GLU   C    C N N 147 
GLU   O    O N N 148 
GLU   CB   C N N 149 
GLU   CG   C N N 150 
GLU   CD   C N N 151 
GLU   OE1  O N N 152 
GLU   OE2  O N N 153 
GLU   OXT  O N N 154 
GLU   H    H N N 155 
GLU   H2   H N N 156 
GLU   HA   H N N 157 
GLU   HB2  H N N 158 
GLU   HB3  H N N 159 
GLU   HG2  H N N 160 
GLU   HG3  H N N 161 
GLU   HE2  H N N 162 
GLU   HXT  H N N 163 
GLY   N    N N N 164 
GLY   CA   C N N 165 
GLY   C    C N N 166 
GLY   O    O N N 167 
GLY   OXT  O N N 168 
GLY   H    H N N 169 
GLY   H2   H N N 170 
GLY   HA2  H N N 171 
GLY   HA3  H N N 172 
GLY   HXT  H N N 173 
HIS   N    N N N 174 
HIS   CA   C N S 175 
HIS   C    C N N 176 
HIS   O    O N N 177 
HIS   CB   C N N 178 
HIS   CG   C Y N 179 
HIS   ND1  N Y N 180 
HIS   CD2  C Y N 181 
HIS   CE1  C Y N 182 
HIS   NE2  N Y N 183 
HIS   OXT  O N N 184 
HIS   H    H N N 185 
HIS   H2   H N N 186 
HIS   HA   H N N 187 
HIS   HB2  H N N 188 
HIS   HB3  H N N 189 
HIS   HD1  H N N 190 
HIS   HD2  H N N 191 
HIS   HE1  H N N 192 
HIS   HE2  H N N 193 
HIS   HXT  H N N 194 
HOH   O    O N N 195 
HOH   H1   H N N 196 
HOH   H2   H N N 197 
ILE   N    N N N 198 
ILE   CA   C N S 199 
ILE   C    C N N 200 
ILE   O    O N N 201 
ILE   CB   C N S 202 
ILE   CG1  C N N 203 
ILE   CG2  C N N 204 
ILE   CD1  C N N 205 
ILE   OXT  O N N 206 
ILE   H    H N N 207 
ILE   H2   H N N 208 
ILE   HA   H N N 209 
ILE   HB   H N N 210 
ILE   HG12 H N N 211 
ILE   HG13 H N N 212 
ILE   HG21 H N N 213 
ILE   HG22 H N N 214 
ILE   HG23 H N N 215 
ILE   HD11 H N N 216 
ILE   HD12 H N N 217 
ILE   HD13 H N N 218 
ILE   HXT  H N N 219 
LEU   N    N N N 220 
LEU   CA   C N S 221 
LEU   C    C N N 222 
LEU   O    O N N 223 
LEU   CB   C N N 224 
LEU   CG   C N N 225 
LEU   CD1  C N N 226 
LEU   CD2  C N N 227 
LEU   OXT  O N N 228 
LEU   H    H N N 229 
LEU   H2   H N N 230 
LEU   HA   H N N 231 
LEU   HB2  H N N 232 
LEU   HB3  H N N 233 
LEU   HG   H N N 234 
LEU   HD11 H N N 235 
LEU   HD12 H N N 236 
LEU   HD13 H N N 237 
LEU   HD21 H N N 238 
LEU   HD22 H N N 239 
LEU   HD23 H N N 240 
LEU   HXT  H N N 241 
LYS   N    N N N 242 
LYS   CA   C N S 243 
LYS   C    C N N 244 
LYS   O    O N N 245 
LYS   CB   C N N 246 
LYS   CG   C N N 247 
LYS   CD   C N N 248 
LYS   CE   C N N 249 
LYS   NZ   N N N 250 
LYS   OXT  O N N 251 
LYS   H    H N N 252 
LYS   H2   H N N 253 
LYS   HA   H N N 254 
LYS   HB2  H N N 255 
LYS   HB3  H N N 256 
LYS   HG2  H N N 257 
LYS   HG3  H N N 258 
LYS   HD2  H N N 259 
LYS   HD3  H N N 260 
LYS   HE2  H N N 261 
LYS   HE3  H N N 262 
LYS   HZ1  H N N 263 
LYS   HZ2  H N N 264 
LYS   HZ3  H N N 265 
LYS   HXT  H N N 266 
MET   N    N N N 267 
MET   CA   C N S 268 
MET   C    C N N 269 
MET   O    O N N 270 
MET   CB   C N N 271 
MET   CG   C N N 272 
MET   SD   S N N 273 
MET   CE   C N N 274 
MET   OXT  O N N 275 
MET   H    H N N 276 
MET   H2   H N N 277 
MET   HA   H N N 278 
MET   HB2  H N N 279 
MET   HB3  H N N 280 
MET   HG2  H N N 281 
MET   HG3  H N N 282 
MET   HE1  H N N 283 
MET   HE2  H N N 284 
MET   HE3  H N N 285 
MET   HXT  H N N 286 
PHE   N    N N N 287 
PHE   CA   C N S 288 
PHE   C    C N N 289 
PHE   O    O N N 290 
PHE   CB   C N N 291 
PHE   CG   C Y N 292 
PHE   CD1  C Y N 293 
PHE   CD2  C Y N 294 
PHE   CE1  C Y N 295 
PHE   CE2  C Y N 296 
PHE   CZ   C Y N 297 
PHE   OXT  O N N 298 
PHE   H    H N N 299 
PHE   H2   H N N 300 
PHE   HA   H N N 301 
PHE   HB2  H N N 302 
PHE   HB3  H N N 303 
PHE   HD1  H N N 304 
PHE   HD2  H N N 305 
PHE   HE1  H N N 306 
PHE   HE2  H N N 307 
PHE   HZ   H N N 308 
PHE   HXT  H N N 309 
PRO   N    N N N 310 
PRO   CA   C N S 311 
PRO   C    C N N 312 
PRO   O    O N N 313 
PRO   CB   C N N 314 
PRO   CG   C N N 315 
PRO   CD   C N N 316 
PRO   OXT  O N N 317 
PRO   H    H N N 318 
PRO   HA   H N N 319 
PRO   HB2  H N N 320 
PRO   HB3  H N N 321 
PRO   HG2  H N N 322 
PRO   HG3  H N N 323 
PRO   HD2  H N N 324 
PRO   HD3  H N N 325 
PRO   HXT  H N N 326 
SER   N    N N N 327 
SER   CA   C N S 328 
SER   C    C N N 329 
SER   O    O N N 330 
SER   CB   C N N 331 
SER   OG   O N N 332 
SER   OXT  O N N 333 
SER   H    H N N 334 
SER   H2   H N N 335 
SER   HA   H N N 336 
SER   HB2  H N N 337 
SER   HB3  H N N 338 
SER   HG   H N N 339 
SER   HXT  H N N 340 
TFA   C1   C N N 341 
TFA   C2   C N N 342 
TFA   O    O N N 343 
TFA   F1   F N N 344 
TFA   F2   F N N 345 
TFA   F3   F N N 346 
TFA   OXT  O N N 347 
TFA   HXT  H N N 348 
THR   N    N N N 349 
THR   CA   C N S 350 
THR   C    C N N 351 
THR   O    O N N 352 
THR   CB   C N R 353 
THR   OG1  O N N 354 
THR   CG2  C N N 355 
THR   OXT  O N N 356 
THR   H    H N N 357 
THR   H2   H N N 358 
THR   HA   H N N 359 
THR   HB   H N N 360 
THR   HG1  H N N 361 
THR   HG21 H N N 362 
THR   HG22 H N N 363 
THR   HG23 H N N 364 
THR   HXT  H N N 365 
TYR   N    N N N 366 
TYR   CA   C N S 367 
TYR   C    C N N 368 
TYR   O    O N N 369 
TYR   CB   C N N 370 
TYR   CG   C Y N 371 
TYR   CD1  C Y N 372 
TYR   CD2  C Y N 373 
TYR   CE1  C Y N 374 
TYR   CE2  C Y N 375 
TYR   CZ   C Y N 376 
TYR   OH   O N N 377 
TYR   OXT  O N N 378 
TYR   H    H N N 379 
TYR   H2   H N N 380 
TYR   HA   H N N 381 
TYR   HB2  H N N 382 
TYR   HB3  H N N 383 
TYR   HD1  H N N 384 
TYR   HD2  H N N 385 
TYR   HE1  H N N 386 
TYR   HE2  H N N 387 
TYR   HH   H N N 388 
TYR   HXT  H N N 389 
VAL   N    N N N 390 
VAL   CA   C N S 391 
VAL   C    C N N 392 
VAL   O    O N N 393 
VAL   CB   C N N 394 
VAL   CG1  C N N 395 
VAL   CG2  C N N 396 
VAL   OXT  O N N 397 
VAL   H    H N N 398 
VAL   H2   H N N 399 
VAL   HA   H N N 400 
VAL   HB   H N N 401 
VAL   HG11 H N N 402 
VAL   HG12 H N N 403 
VAL   HG13 H N N 404 
VAL   HG21 H N N 405 
VAL   HG22 H N N 406 
VAL   HG23 H N N 407 
VAL   HXT  H N N 408 
# 
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 
A1A8H C5  C6   sing N N 1   
A1A8H C5  C4   sing N N 2   
A1A8H C6  C7   sing N N 3   
A1A8H C3  C4   sing N N 4   
A1A8H C3  C2   sing N N 5   
A1A8H C4  C7   sing N N 6   
A1A8H C4  C8   sing N N 7   
A1A8H O1  C1   sing N N 8   
A1A8H C1  C2   sing N N 9   
A1A8H C8  N1   sing N N 10  
A1A8H C2  N1   sing N N 11  
A1A8H N1  C9   sing N N 12  
A1A8H C9  N2   doub Y N 13  
A1A8H C9  C12  sing Y N 14  
A1A8H C13 C12  sing Y N 15  
A1A8H C13 C14  doub Y N 16  
A1A8H N2  C10  sing Y N 17  
A1A8H C12 C11  doub Y N 18  
A1A8H C14 N4   sing Y N 19  
A1A8H C10 N3   doub Y N 20  
A1A8H C11 N4   sing Y N 21  
A1A8H C11 N3   sing Y N 22  
A1A8H C3  H5   sing N N 23  
A1A8H C3  H6   sing N N 24  
A1A8H C6  H9   sing N N 25  
A1A8H C6  H10  sing N N 26  
A1A8H C14 H17  sing N N 27  
A1A8H C1  H3   sing N N 28  
A1A8H C1  H4   sing N N 29  
A1A8H C10 H15  sing N N 30  
A1A8H C13 H16  sing N N 31  
A1A8H C2  H1   sing N N 32  
A1A8H C5  H8   sing N N 33  
A1A8H C5  H7   sing N N 34  
A1A8H C7  H12  sing N N 35  
A1A8H C7  H11  sing N N 36  
A1A8H C8  H14  sing N N 37  
A1A8H C8  H13  sing N N 38  
A1A8H N4  H18  sing N N 39  
A1A8H O1  H2   sing N N 40  
ALA   N   CA   sing N N 41  
ALA   N   H    sing N N 42  
ALA   N   H2   sing N N 43  
ALA   CA  C    sing N N 44  
ALA   CA  CB   sing N N 45  
ALA   CA  HA   sing N N 46  
ALA   C   O    doub N N 47  
ALA   C   OXT  sing N N 48  
ALA   CB  HB1  sing N N 49  
ALA   CB  HB2  sing N N 50  
ALA   CB  HB3  sing N N 51  
ALA   OXT HXT  sing N N 52  
ARG   N   CA   sing N N 53  
ARG   N   H    sing N N 54  
ARG   N   H2   sing N N 55  
ARG   CA  C    sing N N 56  
ARG   CA  CB   sing N N 57  
ARG   CA  HA   sing N N 58  
ARG   C   O    doub N N 59  
ARG   C   OXT  sing N N 60  
ARG   CB  CG   sing N N 61  
ARG   CB  HB2  sing N N 62  
ARG   CB  HB3  sing N N 63  
ARG   CG  CD   sing N N 64  
ARG   CG  HG2  sing N N 65  
ARG   CG  HG3  sing N N 66  
ARG   CD  NE   sing N N 67  
ARG   CD  HD2  sing N N 68  
ARG   CD  HD3  sing N N 69  
ARG   NE  CZ   sing N N 70  
ARG   NE  HE   sing N N 71  
ARG   CZ  NH1  sing N N 72  
ARG   CZ  NH2  doub N N 73  
ARG   NH1 HH11 sing N N 74  
ARG   NH1 HH12 sing N N 75  
ARG   NH2 HH21 sing N N 76  
ARG   NH2 HH22 sing N N 77  
ARG   OXT HXT  sing N N 78  
ASN   N   CA   sing N N 79  
ASN   N   H    sing N N 80  
ASN   N   H2   sing N N 81  
ASN   CA  C    sing N N 82  
ASN   CA  CB   sing N N 83  
ASN   CA  HA   sing N N 84  
ASN   C   O    doub N N 85  
ASN   C   OXT  sing N N 86  
ASN   CB  CG   sing N N 87  
ASN   CB  HB2  sing N N 88  
ASN   CB  HB3  sing N N 89  
ASN   CG  OD1  doub N N 90  
ASN   CG  ND2  sing N N 91  
ASN   ND2 HD21 sing N N 92  
ASN   ND2 HD22 sing N N 93  
ASN   OXT HXT  sing N N 94  
ASP   N   CA   sing N N 95  
ASP   N   H    sing N N 96  
ASP   N   H2   sing N N 97  
ASP   CA  C    sing N N 98  
ASP   CA  CB   sing N N 99  
ASP   CA  HA   sing N N 100 
ASP   C   O    doub N N 101 
ASP   C   OXT  sing N N 102 
ASP   CB  CG   sing N N 103 
ASP   CB  HB2  sing N N 104 
ASP   CB  HB3  sing N N 105 
ASP   CG  OD1  doub N N 106 
ASP   CG  OD2  sing N N 107 
ASP   OD2 HD2  sing N N 108 
ASP   OXT HXT  sing N N 109 
CYS   N   CA   sing N N 110 
CYS   N   H    sing N N 111 
CYS   N   H2   sing N N 112 
CYS   CA  C    sing N N 113 
CYS   CA  CB   sing N N 114 
CYS   CA  HA   sing N N 115 
CYS   C   O    doub N N 116 
CYS   C   OXT  sing N N 117 
CYS   CB  SG   sing N N 118 
CYS   CB  HB2  sing N N 119 
CYS   CB  HB3  sing N N 120 
CYS   SG  HG   sing N N 121 
CYS   OXT HXT  sing N N 122 
GLN   N   CA   sing N N 123 
GLN   N   H    sing N N 124 
GLN   N   H2   sing N N 125 
GLN   CA  C    sing N N 126 
GLN   CA  CB   sing N N 127 
GLN   CA  HA   sing N N 128 
GLN   C   O    doub N N 129 
GLN   C   OXT  sing N N 130 
GLN   CB  CG   sing N N 131 
GLN   CB  HB2  sing N N 132 
GLN   CB  HB3  sing N N 133 
GLN   CG  CD   sing N N 134 
GLN   CG  HG2  sing N N 135 
GLN   CG  HG3  sing N N 136 
GLN   CD  OE1  doub N N 137 
GLN   CD  NE2  sing N N 138 
GLN   NE2 HE21 sing N N 139 
GLN   NE2 HE22 sing N N 140 
GLN   OXT HXT  sing N N 141 
GLU   N   CA   sing N N 142 
GLU   N   H    sing N N 143 
GLU   N   H2   sing N N 144 
GLU   CA  C    sing N N 145 
GLU   CA  CB   sing N N 146 
GLU   CA  HA   sing N N 147 
GLU   C   O    doub N N 148 
GLU   C   OXT  sing N N 149 
GLU   CB  CG   sing N N 150 
GLU   CB  HB2  sing N N 151 
GLU   CB  HB3  sing N N 152 
GLU   CG  CD   sing N N 153 
GLU   CG  HG2  sing N N 154 
GLU   CG  HG3  sing N N 155 
GLU   CD  OE1  doub N N 156 
GLU   CD  OE2  sing N N 157 
GLU   OE2 HE2  sing N N 158 
GLU   OXT HXT  sing N N 159 
GLY   N   CA   sing N N 160 
GLY   N   H    sing N N 161 
GLY   N   H2   sing N N 162 
GLY   CA  C    sing N N 163 
GLY   CA  HA2  sing N N 164 
GLY   CA  HA3  sing N N 165 
GLY   C   O    doub N N 166 
GLY   C   OXT  sing N N 167 
GLY   OXT HXT  sing N N 168 
HIS   N   CA   sing N N 169 
HIS   N   H    sing N N 170 
HIS   N   H2   sing N N 171 
HIS   CA  C    sing N N 172 
HIS   CA  CB   sing N N 173 
HIS   CA  HA   sing N N 174 
HIS   C   O    doub N N 175 
HIS   C   OXT  sing N N 176 
HIS   CB  CG   sing N N 177 
HIS   CB  HB2  sing N N 178 
HIS   CB  HB3  sing N N 179 
HIS   CG  ND1  sing Y N 180 
HIS   CG  CD2  doub Y N 181 
HIS   ND1 CE1  doub Y N 182 
HIS   ND1 HD1  sing N N 183 
HIS   CD2 NE2  sing Y N 184 
HIS   CD2 HD2  sing N N 185 
HIS   CE1 NE2  sing Y N 186 
HIS   CE1 HE1  sing N N 187 
HIS   NE2 HE2  sing N N 188 
HIS   OXT HXT  sing N N 189 
HOH   O   H1   sing N N 190 
HOH   O   H2   sing N N 191 
ILE   N   CA   sing N N 192 
ILE   N   H    sing N N 193 
ILE   N   H2   sing N N 194 
ILE   CA  C    sing N N 195 
ILE   CA  CB   sing N N 196 
ILE   CA  HA   sing N N 197 
ILE   C   O    doub N N 198 
ILE   C   OXT  sing N N 199 
ILE   CB  CG1  sing N N 200 
ILE   CB  CG2  sing N N 201 
ILE   CB  HB   sing N N 202 
ILE   CG1 CD1  sing N N 203 
ILE   CG1 HG12 sing N N 204 
ILE   CG1 HG13 sing N N 205 
ILE   CG2 HG21 sing N N 206 
ILE   CG2 HG22 sing N N 207 
ILE   CG2 HG23 sing N N 208 
ILE   CD1 HD11 sing N N 209 
ILE   CD1 HD12 sing N N 210 
ILE   CD1 HD13 sing N N 211 
ILE   OXT HXT  sing N N 212 
LEU   N   CA   sing N N 213 
LEU   N   H    sing N N 214 
LEU   N   H2   sing N N 215 
LEU   CA  C    sing N N 216 
LEU   CA  CB   sing N N 217 
LEU   CA  HA   sing N N 218 
LEU   C   O    doub N N 219 
LEU   C   OXT  sing N N 220 
LEU   CB  CG   sing N N 221 
LEU   CB  HB2  sing N N 222 
LEU   CB  HB3  sing N N 223 
LEU   CG  CD1  sing N N 224 
LEU   CG  CD2  sing N N 225 
LEU   CG  HG   sing N N 226 
LEU   CD1 HD11 sing N N 227 
LEU   CD1 HD12 sing N N 228 
LEU   CD1 HD13 sing N N 229 
LEU   CD2 HD21 sing N N 230 
LEU   CD2 HD22 sing N N 231 
LEU   CD2 HD23 sing N N 232 
LEU   OXT HXT  sing N N 233 
LYS   N   CA   sing N N 234 
LYS   N   H    sing N N 235 
LYS   N   H2   sing N N 236 
LYS   CA  C    sing N N 237 
LYS   CA  CB   sing N N 238 
LYS   CA  HA   sing N N 239 
LYS   C   O    doub N N 240 
LYS   C   OXT  sing N N 241 
LYS   CB  CG   sing N N 242 
LYS   CB  HB2  sing N N 243 
LYS   CB  HB3  sing N N 244 
LYS   CG  CD   sing N N 245 
LYS   CG  HG2  sing N N 246 
LYS   CG  HG3  sing N N 247 
LYS   CD  CE   sing N N 248 
LYS   CD  HD2  sing N N 249 
LYS   CD  HD3  sing N N 250 
LYS   CE  NZ   sing N N 251 
LYS   CE  HE2  sing N N 252 
LYS   CE  HE3  sing N N 253 
LYS   NZ  HZ1  sing N N 254 
LYS   NZ  HZ2  sing N N 255 
LYS   NZ  HZ3  sing N N 256 
LYS   OXT HXT  sing N N 257 
MET   N   CA   sing N N 258 
MET   N   H    sing N N 259 
MET   N   H2   sing N N 260 
MET   CA  C    sing N N 261 
MET   CA  CB   sing N N 262 
MET   CA  HA   sing N N 263 
MET   C   O    doub N N 264 
MET   C   OXT  sing N N 265 
MET   CB  CG   sing N N 266 
MET   CB  HB2  sing N N 267 
MET   CB  HB3  sing N N 268 
MET   CG  SD   sing N N 269 
MET   CG  HG2  sing N N 270 
MET   CG  HG3  sing N N 271 
MET   SD  CE   sing N N 272 
MET   CE  HE1  sing N N 273 
MET   CE  HE2  sing N N 274 
MET   CE  HE3  sing N N 275 
MET   OXT HXT  sing N N 276 
PHE   N   CA   sing N N 277 
PHE   N   H    sing N N 278 
PHE   N   H2   sing N N 279 
PHE   CA  C    sing N N 280 
PHE   CA  CB   sing N N 281 
PHE   CA  HA   sing N N 282 
PHE   C   O    doub N N 283 
PHE   C   OXT  sing N N 284 
PHE   CB  CG   sing N N 285 
PHE   CB  HB2  sing N N 286 
PHE   CB  HB3  sing N N 287 
PHE   CG  CD1  doub Y N 288 
PHE   CG  CD2  sing Y N 289 
PHE   CD1 CE1  sing Y N 290 
PHE   CD1 HD1  sing N N 291 
PHE   CD2 CE2  doub Y N 292 
PHE   CD2 HD2  sing N N 293 
PHE   CE1 CZ   doub Y N 294 
PHE   CE1 HE1  sing N N 295 
PHE   CE2 CZ   sing Y N 296 
PHE   CE2 HE2  sing N N 297 
PHE   CZ  HZ   sing N N 298 
PHE   OXT HXT  sing N N 299 
PRO   N   CA   sing N N 300 
PRO   N   CD   sing N N 301 
PRO   N   H    sing N N 302 
PRO   CA  C    sing N N 303 
PRO   CA  CB   sing N N 304 
PRO   CA  HA   sing N N 305 
PRO   C   O    doub N N 306 
PRO   C   OXT  sing N N 307 
PRO   CB  CG   sing N N 308 
PRO   CB  HB2  sing N N 309 
PRO   CB  HB3  sing N N 310 
PRO   CG  CD   sing N N 311 
PRO   CG  HG2  sing N N 312 
PRO   CG  HG3  sing N N 313 
PRO   CD  HD2  sing N N 314 
PRO   CD  HD3  sing N N 315 
PRO   OXT HXT  sing N N 316 
SER   N   CA   sing N N 317 
SER   N   H    sing N N 318 
SER   N   H2   sing N N 319 
SER   CA  C    sing N N 320 
SER   CA  CB   sing N N 321 
SER   CA  HA   sing N N 322 
SER   C   O    doub N N 323 
SER   C   OXT  sing N N 324 
SER   CB  OG   sing N N 325 
SER   CB  HB2  sing N N 326 
SER   CB  HB3  sing N N 327 
SER   OG  HG   sing N N 328 
SER   OXT HXT  sing N N 329 
TFA   C1  C2   sing N N 330 
TFA   C1  O    doub N N 331 
TFA   C1  OXT  sing N N 332 
TFA   C2  F1   sing N N 333 
TFA   C2  F2   sing N N 334 
TFA   C2  F3   sing N N 335 
TFA   OXT HXT  sing N N 336 
THR   N   CA   sing N N 337 
THR   N   H    sing N N 338 
THR   N   H2   sing N N 339 
THR   CA  C    sing N N 340 
THR   CA  CB   sing N N 341 
THR   CA  HA   sing N N 342 
THR   C   O    doub N N 343 
THR   C   OXT  sing N N 344 
THR   CB  OG1  sing N N 345 
THR   CB  CG2  sing N N 346 
THR   CB  HB   sing N N 347 
THR   OG1 HG1  sing N N 348 
THR   CG2 HG21 sing N N 349 
THR   CG2 HG22 sing N N 350 
THR   CG2 HG23 sing N N 351 
THR   OXT HXT  sing N N 352 
TYR   N   CA   sing N N 353 
TYR   N   H    sing N N 354 
TYR   N   H2   sing N N 355 
TYR   CA  C    sing N N 356 
TYR   CA  CB   sing N N 357 
TYR   CA  HA   sing N N 358 
TYR   C   O    doub N N 359 
TYR   C   OXT  sing N N 360 
TYR   CB  CG   sing N N 361 
TYR   CB  HB2  sing N N 362 
TYR   CB  HB3  sing N N 363 
TYR   CG  CD1  doub Y N 364 
TYR   CG  CD2  sing Y N 365 
TYR   CD1 CE1  sing Y N 366 
TYR   CD1 HD1  sing N N 367 
TYR   CD2 CE2  doub Y N 368 
TYR   CD2 HD2  sing N N 369 
TYR   CE1 CZ   doub Y N 370 
TYR   CE1 HE1  sing N N 371 
TYR   CE2 CZ   sing Y N 372 
TYR   CE2 HE2  sing N N 373 
TYR   CZ  OH   sing N N 374 
TYR   OH  HH   sing N N 375 
TYR   OXT HXT  sing N N 376 
VAL   N   CA   sing N N 377 
VAL   N   H    sing N N 378 
VAL   N   H2   sing N N 379 
VAL   CA  C    sing N N 380 
VAL   CA  CB   sing N N 381 
VAL   CA  HA   sing N N 382 
VAL   C   O    doub N N 383 
VAL   C   OXT  sing N N 384 
VAL   CB  CG1  sing N N 385 
VAL   CB  CG2  sing N N 386 
VAL   CB  HB   sing N N 387 
VAL   CG1 HG11 sing N N 388 
VAL   CG1 HG12 sing N N 389 
VAL   CG1 HG13 sing N N 390 
VAL   CG2 HG21 sing N N 391 
VAL   CG2 HG22 sing N N 392 
VAL   CG2 HG23 sing N N 393 
VAL   OXT HXT  sing N N 394 
# 
_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                    7HDJ 
_atom_sites.fract_transf_matrix[1][1]   0.011245 
_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]   0.011245 
_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]   0.025373 
_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 
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    A VAL   A 1 3   ? 19.715 -16.234 22.221  0.52 60.50 ?  3   VAL   A N    1 
ATOM   2    N N    B VAL   A 1 3   ? 19.695 -15.718 22.419  0.48 59.06 ?  3   VAL   A N    1 
ATOM   3    C CA   A VAL   A 1 3   ? 18.736 -15.166 22.378  0.52 60.04 ?  3   VAL   A CA   1 
ATOM   4    C CA   B VAL   A 1 3   ? 18.676 -14.692 22.595  0.48 58.47 ?  3   VAL   A CA   1 
ATOM   5    C C    A VAL   A 1 3   ? 19.381 -13.814 22.096  0.52 58.32 ?  3   VAL   A C    1 
ATOM   6    C C    B VAL   A 1 3   ? 19.266 -13.315 22.305  0.48 56.39 ?  3   VAL   A C    1 
ATOM   7    O O    A VAL   A 1 3   ? 20.490 -13.540 22.557  0.52 58.95 ?  3   VAL   A O    1 
ATOM   8    O O    B VAL   A 1 3   ? 20.313 -12.958 22.846  0.48 56.93 ?  3   VAL   A O    1 
ATOM   9    C CB   A VAL   A 1 3   ? 18.089 -15.199 23.779  0.52 60.89 ?  3   VAL   A CB   1 
ATOM   10   C CB   B VAL   A 1 3   ? 18.057 -14.752 24.006  0.48 59.52 ?  3   VAL   A CB   1 
ATOM   11   C CG1  A VAL   A 1 3   ? 17.059 -14.087 23.921  0.52 61.11 ?  3   VAL   A CG1  1 
ATOM   12   C CG1  B VAL   A 1 3   ? 16.991 -13.679 24.164  0.48 59.81 ?  3   VAL   A CG1  1 
ATOM   13   C CG2  A VAL   A 1 3   ? 17.450 -16.557 24.040  0.52 61.11 ?  3   VAL   A CG2  1 
ATOM   14   C CG2  B VAL   A 1 3   ? 17.474 -16.135 24.277  0.48 59.85 ?  3   VAL   A CG2  1 
ATOM   15   H HA   A VAL   A 1 3   ? 18.029 -15.293 21.730  0.52 72.05 ?  3   VAL   A HA   1 
ATOM   16   H HA   B VAL   A 1 3   ? 17.963 -14.849 21.960  0.48 70.16 ?  3   VAL   A HA   1 
ATOM   17   H HB   A VAL   A 1 3   ? 18.776 -15.059 24.450  0.52 73.07 ?  3   VAL   A HB   1 
ATOM   18   H HB   B VAL   A 1 3   ? 18.749 -14.588 24.665  0.48 71.42 ?  3   VAL   A HB   1 
ATOM   19   H HG11 A VAL   A 1 3   ? 16.549 -14.232 24.733  0.52 73.33 ?  3   VAL   A HG11 1 
ATOM   20   H HG11 B VAL   A 1 3   ? 16.495 -13.846 24.981  0.48 71.77 ?  3   VAL   A HG11 1 
ATOM   21   H HG12 A VAL   A 1 3   ? 17.517 -13.233 23.968  0.52 73.33 ?  3   VAL   A HG12 1 
ATOM   22   H HG12 B VAL   A 1 3   ? 17.420 -12.811 24.210  0.48 71.77 ?  3   VAL   A HG12 1 
ATOM   23   H HG13 A VAL   A 1 3   ? 16.468 -14.105 23.152  0.52 73.33 ?  3   VAL   A HG13 1 
ATOM   24   H HG13 B VAL   A 1 3   ? 16.392 -13.716 23.402  0.48 71.77 ?  3   VAL   A HG13 1 
ATOM   25   H HG21 A VAL   A 1 3   ? 16.996 -16.533 24.897  0.52 73.34 ?  3   VAL   A HG21 1 
ATOM   26   H HG21 B VAL   A 1 3   ? 17.027 -16.126 25.138  0.48 71.82 ?  3   VAL   A HG21 1 
ATOM   27   H HG22 A VAL   A 1 3   ? 16.813 -16.746 23.333  0.52 73.34 ?  3   VAL   A HG22 1 
ATOM   28   H HG22 B VAL   A 1 3   ? 16.839 -16.352 23.576  0.48 71.82 ?  3   VAL   A HG22 1 
ATOM   29   H HG23 A VAL   A 1 3   ? 18.142 -17.236 24.052  0.52 73.34 ?  3   VAL   A HG23 1 
ATOM   30   H HG23 B VAL   A 1 3   ? 18.193 -16.786 24.285  0.48 71.82 ?  3   VAL   A HG23 1 
ATOM   31   N N    A ASN   A 1 4   ? 18.686 -12.974 21.331  0.52 55.52 ?  4   ASN   A N    1 
ATOM   32   N N    B ASN   A 1 4   ? 18.595 -12.545 21.453  0.48 53.23 ?  4   ASN   A N    1 
ATOM   33   C CA   A ASN   A 1 4   ? 19.133 -11.618 21.041  0.52 52.24 ?  4   ASN   A CA   1 
ATOM   34   C CA   B ASN   A 1 4   ? 19.023 -11.195 21.101  0.48 49.63 ?  4   ASN   A CA   1 
ATOM   35   C C    A ASN   A 1 4   ? 17.980 -10.646 21.283  0.52 49.63 ?  4   ASN   A C    1 
ATOM   36   C C    B ASN   A 1 4   ? 17.896 -10.204 21.393  0.48 46.58 ?  4   ASN   A C    1 
ATOM   37   O O    A ASN   A 1 4   ? 16.876 -11.041 21.669  0.52 49.79 ?  4   ASN   A O    1 
ATOM   38   O O    B ASN   A 1 4   ? 16.837 -10.567 21.913  0.48 46.60 ?  4   ASN   A O    1 
ATOM   39   C CB   A ASN   A 1 4   ? 19.713 -11.501 19.623  0.52 51.29 ?  4   ASN   A CB   1 
ATOM   40   C CB   B ASN   A 1 4   ? 19.520 -11.120 19.652  0.48 48.86 ?  4   ASN   A CB   1 
ATOM   41   C CG   A ASN   A 1 4   ? 18.727 -11.906 18.549  0.52 50.29 ?  4   ASN   A CG   1 
ATOM   42   C CG   B ASN   A 1 4   ? 18.489 -11.595 18.652  0.48 47.99 ?  4   ASN   A CG   1 
ATOM   43   O OD1  A ASN   A 1 4   ? 17.589 -11.438 18.524  0.52 49.93 ?  4   ASN   A OD1  1 
ATOM   44   O OD1  B ASN   A 1 4   ? 17.344 -11.144 18.659  0.48 47.61 ?  4   ASN   A OD1  1 
ATOM   45   N ND2  A ASN   A 1 4   ? 19.162 -12.786 17.652  0.52 50.04 ?  4   ASN   A ND2  1 
ATOM   46   N ND2  B ASN   A 1 4   ? 18.893 -12.518 17.783  0.48 47.82 ?  4   ASN   A ND2  1 
ATOM   47   H H    A ASN   A 1 4   ? 17.934 -13.176 20.963  0.52 66.62 ?  4   ASN   A H    1 
ATOM   48   H H    B ASN   A 1 4   ? 17.864 -12.789 21.066  0.48 63.87 ?  4   ASN   A H    1 
ATOM   49   H HA   A ASN   A 1 4   ? 19.841 -11.392 21.657  0.52 62.69 ?  4   ASN   A HA   1 
ATOM   50   H HA   B ASN   A 1 4   ? 19.772 -10.963 21.663  0.48 59.55 ?  4   ASN   A HA   1 
ATOM   51   H HB2  A ASN   A 1 4   ? 19.972 -10.579 19.462  0.52 61.54 ?  4   ASN   A HB2  1 
ATOM   52   H HB2  B ASN   A 1 4   ? 19.744 -10.197 19.439  0.48 58.63 ?  4   ASN   A HB2  1 
ATOM   53   H HB3  A ASN   A 1 4   ? 20.490 -12.078 19.551  0.52 61.54 ?  4   ASN   A HB3  1 
ATOM   54   H HB3  B ASN   A 1 4   ? 20.309 -11.677 19.555  0.48 58.63 ?  4   ASN   A HB3  1 
ATOM   55   H HD21 A ASN   A 1 4   ? 18.643 -13.048 17.019  0.52 60.05 ?  4   ASN   A HD21 1 
ATOM   56   H HD21 B ASN   A 1 4   ? 18.348 -12.821 17.191  0.48 57.38 ?  4   ASN   A HD21 1 
ATOM   57   H HD22 A ASN   A 1 4   ? 19.964 -13.094 17.704  0.52 60.05 ?  4   ASN   A HD22 1 
ATOM   58   H HD22 B ASN   A 1 4   ? 19.702 -12.813 17.812  0.48 57.38 ?  4   ASN   A HD22 1 
ATOM   59   N N    A SER   A 1 5   ? 18.246 -9.360  21.054  0.52 46.51 ?  5   SER   A N    1 
ATOM   60   N N    B SER   A 1 5   ? 18.134 -8.937  21.052  0.48 43.24 ?  5   SER   A N    1 
ATOM   61   C CA   A SER   A 1 5   ? 17.325 -8.290  21.419  0.52 43.13 ?  5   SER   A CA   1 
ATOM   62   C CA   B SER   A 1 5   ? 17.259 -7.842  21.452  0.48 39.73 ?  5   SER   A CA   1 
ATOM   63   C C    A SER   A 1 5   ? 16.477 -7.792  20.250  0.52 38.77 ?  5   SER   A C    1 
ATOM   64   C C    B SER   A 1 5   ? 16.356 -7.342  20.327  0.48 35.21 ?  5   SER   A C    1 
ATOM   65   O O    A SER   A 1 5   ? 15.839 -6.741  20.369  0.52 38.99 ?  5   SER   A O    1 
ATOM   66   O O    B SER   A 1 5   ? 15.675 -6.326  20.503  0.48 35.03 ?  5   SER   A O    1 
ATOM   67   C CB   A SER   A 1 5   ? 18.092 -7.124  22.047  0.52 44.15 ?  5   SER   A CB   1 
ATOM   68   C CB   B SER   A 1 5   ? 18.083 -6.684  22.020  0.48 40.90 ?  5   SER   A CB   1 
ATOM   69   O OG   A SER   A 1 5   ? 19.117 -6.663  21.184  0.52 44.69 ?  5   SER   A OG   1 
ATOM   70   O OG   B SER   A 1 5   ? 18.948 -6.143  21.038  0.48 41.47 ?  5   SER   A OG   1 
ATOM   71   H H    A SER   A 1 5   ? 18.967 -9.083  20.680  0.52 55.82 ?  5   SER   A H    1 
ATOM   72   H H    B SER   A 1 5   ? 18.807 -8.690  20.579  0.48 51.89 ?  5   SER   A H    1 
ATOM   73   H HA   A SER   A 1 5   ? 16.721 -8.630  22.096  0.52 51.76 ?  5   SER   A HA   1 
ATOM   74   H HA   B SER   A 1 5   ? 16.685 -8.160  22.163  0.48 47.67 ?  5   SER   A HA   1 
ATOM   75   H HB2  A SER   A 1 5   ? 17.473 -6.395  22.218  0.52 52.97 ?  5   SER   A HB2  1 
ATOM   76   H HB2  B SER   A 1 5   ? 17.478 -5.990  22.326  0.48 49.08 ?  5   SER   A HB2  1 
ATOM   77   H HB3  A SER   A 1 5   ? 18.490 -7.419  22.883  0.52 52.97 ?  5   SER   A HB3  1 
ATOM   78   H HB3  B SER   A 1 5   ? 18.614 -7.011  22.765  0.48 49.08 ?  5   SER   A HB3  1 
ATOM   79   H HG   A SER   A 1 5   ? 19.529 -6.025  21.544  0.52 53.62 ?  5   SER   A HG   1 
ATOM   80   H HG   B SER   A 1 5   ? 19.393 -5.510  21.365  0.48 49.77 ?  5   SER   A HG   1 
ATOM   81   N N    A PHE   A 1 6   ? 16.453 -8.511  19.130  0.52 33.77 ?  6   PHE   A N    1 
ATOM   82   N N    B PHE   A 1 6   ? 16.331 -8.021  19.184  0.48 30.68 ?  6   PHE   A N    1 
ATOM   83   C CA   A PHE   A 1 6   ? 15.556 -8.153  18.037  0.52 28.77 ?  6   PHE   A CA   1 
ATOM   84   C CA   B PHE   A 1 6   ? 15.375 -7.672  18.141  0.48 26.73 ?  6   PHE   A CA   1 
ATOM   85   C C    A PHE   A 1 6   ? 14.123 -8.544  18.384  0.52 27.27 ?  6   PHE   A C    1 
ATOM   86   C C    B PHE   A 1 6   ? 13.964 -8.007  18.610  0.48 26.19 ?  6   PHE   A C    1 
ATOM   87   O O    A PHE   A 1 6   ? 13.867 -9.641  18.888  0.52 28.10 ?  6   PHE   A O    1 
ATOM   88   O O    B PHE   A 1 6   ? 13.732 -9.047  19.231  0.48 26.77 ?  6   PHE   A O    1 
ATOM   89   C CB   A PHE   A 1 6   ? 15.988 -8.853  16.749  0.52 25.70 ?  6   PHE   A CB   1 
ATOM   90   C CB   B PHE   A 1 6   ? 15.694 -8.438  16.857  0.48 23.95 ?  6   PHE   A CB   1 
ATOM   91   C CG   A PHE   A 1 6   ? 17.268 -8.315  16.162  0.52 23.11 ?  6   PHE   A CG   1 
ATOM   92   C CG   B PHE   A 1 6   ? 17.018 -8.066  16.237  0.48 21.99 ?  6   PHE   A CG   1 
ATOM   93   C CD1  A PHE   A 1 6   ? 17.266 -7.154  15.406  0.52 22.11 ?  6   PHE   A CD1  1 
ATOM   94   C CD1  B PHE   A 1 6   ? 17.168 -6.870  15.555  0.48 21.16 ?  6   PHE   A CD1  1 
ATOM   95   C CD2  A PHE   A 1 6   ? 18.471 -8.974  16.362  0.52 22.90 ?  6   PHE   A CD2  1 
ATOM   96   C CD2  B PHE   A 1 6   ? 18.107 -8.917  16.330  0.48 21.95 ?  6   PHE   A CD2  1 
ATOM   97   C CE1  A PHE   A 1 6   ? 18.443 -6.655  14.862  0.52 22.02 ?  6   PHE   A CE1  1 
ATOM   98   C CE1  B PHE   A 1 6   ? 18.384 -6.525  14.981  0.48 21.16 ?  6   PHE   A CE1  1 
ATOM   99   C CE2  A PHE   A 1 6   ? 19.647 -8.483  15.819  0.52 22.75 ?  6   PHE   A CE2  1 
ATOM   100  C CE2  B PHE   A 1 6   ? 19.321 -8.581  15.757  0.48 21.94 ?  6   PHE   A CE2  1 
ATOM   101  C CZ   A PHE   A 1 6   ? 19.632 -7.321  15.069  0.52 22.46 ?  6   PHE   A CZ   1 
ATOM   102  C CZ   B PHE   A 1 6   ? 19.459 -7.382  15.083  0.48 21.72 ?  6   PHE   A CZ   1 
ATOM   103  H H    A PHE   A 1 6   ? 16.946 -9.201  18.979  0.52 40.53 ?  6   PHE   A H    1 
ATOM   104  H H    B PHE   A 1 6   ? 16.845 -8.684  18.991  0.48 36.81 ?  6   PHE   A H    1 
ATOM   105  H HA   A PHE   A 1 6   ? 15.591 -7.195  17.895  0.52 34.52 ?  6   PHE   A HA   1 
ATOM   106  H HA   B PHE   A 1 6   ? 15.423 -6.723  17.960  0.48 32.08 ?  6   PHE   A HA   1 
ATOM   107  H HB2  A PHE   A 1 6   ? 16.120 -9.797  16.937  0.52 30.84 ?  6   PHE   A HB2  1 
ATOM   108  H HB2  B PHE   A 1 6   ? 15.716 -9.387  17.057  0.48 28.75 ?  6   PHE   A HB2  1 
ATOM   109  H HB3  A PHE   A 1 6   ? 15.288 -8.745  16.088  0.52 30.84 ?  6   PHE   A HB3  1 
ATOM   110  H HB3  B PHE   A 1 6   ? 14.999 -8.255  16.205  0.48 28.75 ?  6   PHE   A HB3  1 
ATOM   111  H HD1  A PHE   A 1 6   ? 16.467 -6.702  15.264  0.52 26.53 ?  6   PHE   A HD1  1 
ATOM   112  H HD1  B PHE   A 1 6   ? 16.445 -6.287  15.485  0.48 25.39 ?  6   PHE   A HD1  1 
ATOM   113  H HD2  A PHE   A 1 6   ? 18.487 -9.758  16.866  0.52 27.48 ?  6   PHE   A HD2  1 
ATOM   114  H HD2  B PHE   A 1 6   ? 18.020 -9.725  16.783  0.48 26.34 ?  6   PHE   A HD2  1 
ATOM   115  H HE1  A PHE   A 1 6   ? 18.430 -5.873  14.357  0.52 26.42 ?  6   PHE   A HE1  1 
ATOM   116  H HE1  B PHE   A 1 6   ? 18.474 -5.716  14.527  0.48 25.39 ?  6   PHE   A HE1  1 
ATOM   117  H HE2  A PHE   A 1 6   ? 20.448 -8.935  15.962  0.52 27.30 ?  6   PHE   A HE2  1 
ATOM   118  H HE2  B PHE   A 1 6   ? 20.047 -9.161  15.828  0.48 26.33 ?  6   PHE   A HE2  1 
ATOM   119  H HZ   A PHE   A 1 6   ? 20.421 -6.991  14.706  0.52 26.95 ?  6   PHE   A HZ   1 
ATOM   120  H HZ   B PHE   A 1 6   ? 20.275 -7.154  14.699  0.48 26.07 ?  6   PHE   A HZ   1 
ATOM   121  N N    A SER   A 1 7   ? 13.180 -7.645  18.097  0.52 25.01 ?  7   SER   A N    1 
ATOM   122  N N    B SER   A 1 7   ? 13.016 -7.116  18.320  0.48 25.23 ?  7   SER   A N    1 
ATOM   123  C CA   A SER   A 1 7   ? 11.803 -7.779  18.560  0.52 24.43 ?  7   SER   A CA   1 
ATOM   124  C CA   B SER   A 1 7   ? 11.663 -7.232  18.848  0.48 25.54 ?  7   SER   A CA   1 
ATOM   125  C C    A SER   A 1 7   ? 10.819 -7.527  17.425  0.52 21.98 ?  7   SER   A C    1 
ATOM   126  C C    B SER   A 1 7   ? 10.637 -7.095  17.733  0.48 23.70 ?  7   SER   A C    1 
ATOM   127  O O    A SER   A 1 7   ? 11.011 -6.623  16.608  0.52 21.88 ?  7   SER   A O    1 
ATOM   128  O O    B SER   A 1 7   ? 10.755 -6.227  16.864  0.48 24.04 ?  7   SER   A O    1 
ATOM   129  C CB   A SER   A 1 7   ? 11.525 -6.788  19.700  0.52 26.57 ?  7   SER   A CB   1 
ATOM   130  C CB   B SER   A 1 7   ? 11.404 -6.165  19.922  0.48 27.69 ?  7   SER   A CB   1 
ATOM   131  O OG   A SER   A 1 7   ? 10.149 -6.764  20.041  0.52 28.18 ?  7   SER   A OG   1 
ATOM   132  O OG   B SER   A 1 7   ? 10.504 -6.647  20.904  0.48 29.68 ?  7   SER   A OG   1 
ATOM   133  H H    A SER   A 1 7   ? 13.323 -6.944  17.623  0.52 30.01 ?  7   SER   A H    1 
ATOM   134  H H    B SER   A 1 7   ? 13.137 -6.430  17.816  0.48 30.28 ?  7   SER   A H    1 
ATOM   135  H HA   A SER   A 1 7   ? 11.664 -8.678  18.897  0.52 29.32 ?  7   SER   A HA   1 
ATOM   136  H HA   B SER   A 1 7   ? 11.549 -8.103  19.258  0.48 30.65 ?  7   SER   A HA   1 
ATOM   137  H HB2  A SER   A 1 7   ? 12.040 -7.055  20.480  0.52 31.89 ?  7   SER   A HB2  1 
ATOM   138  H HB2  B SER   A 1 7   ? 12.247 -5.931  20.347  0.48 33.22 ?  7   SER   A HB2  1 
ATOM   139  H HB3  A SER   A 1 7   ? 11.804 -5.900  19.416  0.52 31.89 ?  7   SER   A HB3  1 
ATOM   140  H HB3  B SER   A 1 7   ? 11.018 -5.381  19.503  0.48 33.22 ?  7   SER   A HB3  1 
ATOM   141  H HG   A SER   A 1 7   ? 10.024 -6.209  20.659  0.52 33.81 ?  7   SER   A HG   1 
ATOM   142  H HG   B SER   A 1 7   ? 10.377 -6.061  21.490  0.48 35.61 ?  7   SER   A HG   1 
ATOM   143  N N    A GLY   A 1 8   ? 9.758  -8.333  17.380  0.52 20.05 ?  8   GLY   A N    1 
ATOM   144  N N    B GLY   A 1 8   ? 9.627  -7.962  17.766  0.48 22.41 ?  8   GLY   A N    1 
ATOM   145  C CA   A GLY   A 1 8   ? 8.661  -8.091  16.464  0.52 18.48 ?  8   GLY   A CA   1 
ATOM   146  C CA   B GLY   A 1 8   ? 8.513  -7.858  16.847  0.48 21.28 ?  8   GLY   A CA   1 
ATOM   147  C C    A GLY   A 1 8   ? 8.836  -8.631  15.063  0.52 17.17 ?  8   GLY   A C    1 
ATOM   148  C C    B GLY   A 1 8   ? 8.784  -8.329  15.441  0.48 19.80 ?  8   GLY   A C    1 
ATOM   149  O O    A GLY   A 1 8   ? 8.052  -8.266  14.178  0.52 17.83 ?  8   GLY   A O    1 
ATOM   150  O O    B GLY   A 1 8   ? 8.043  -7.953  14.527  0.48 20.22 ?  8   GLY   A O    1 
ATOM   151  H H    A GLY   A 1 8   ? 9.659  -9.029  17.877  0.52 24.05 ?  8   GLY   A H    1 
ATOM   152  H H    B GLY   A 1 8   ? 9.572  -8.624  18.312  0.48 26.89 ?  8   GLY   A H    1 
ATOM   153  H HA2  A GLY   A 1 8   ? 7.862  -8.493  16.830  0.52 22.17 ?  8   GLY   A HA2  1 
ATOM   154  H HA2  B GLY   A 1 8   ? 7.767  -8.369  17.199  0.48 25.54 ?  8   GLY   A HA2  1 
ATOM   155  H HA3  A GLY   A 1 8   ? 8.516  -7.132  16.407  0.52 22.17 ?  8   GLY   A HA3  1 
ATOM   156  H HA3  B GLY   A 1 8   ? 8.241  -6.932  16.786  0.48 25.54 ?  8   GLY   A HA3  1 
ATOM   157  N N    A TYR   A 1 9   ? 9.816  -9.500  14.834  0.52 15.35 ?  9   TYR   A N    1 
ATOM   158  N N    B TYR   A 1 9   ? 9.826  -9.130  15.228  0.48 18.41 ?  9   TYR   A N    1 
ATOM   159  C CA   A TYR   A 1 9   ? 10.102 -10.016 13.505  0.52 14.35 ?  9   TYR   A CA   1 
ATOM   160  C CA   B TYR   A 1 9   ? 10.106 -9.657  13.899  0.48 16.35 ?  9   TYR   A CA   1 
ATOM   161  C C    A TYR   A 1 9   ? 9.264  -11.253 13.204  0.52 13.68 ?  9   TYR   A C    1 
ATOM   162  C C    B TYR   A 1 9   ? 9.252  -10.888 13.620  0.48 15.34 ?  9   TYR   A C    1 
ATOM   163  O O    A TYR   A 1 9   ? 8.973  -12.069 14.082  0.52 14.95 ?  9   TYR   A O    1 
ATOM   164  O O    B TYR   A 1 9   ? 8.980  -11.691 14.515  0.48 16.47 ?  9   TYR   A O    1 
ATOM   165  C CB   A TYR   A 1 9   ? 11.584 -10.383 13.371  0.52 14.27 ?  9   TYR   A CB   1 
ATOM   166  C CB   B TYR   A 1 9   ? 11.595 -9.997  13.749  0.48 16.18 ?  9   TYR   A CB   1 
ATOM   167  C CG   A TYR   A 1 9   ? 12.502 -9.191  13.221  0.52 14.35 ?  9   TYR   A CG   1 
ATOM   168  C CG   B TYR   A 1 9   ? 12.450 -8.779  13.465  0.48 16.11 ?  9   TYR   A CG   1 
ATOM   169  C CD1  A TYR   A 1 9   ? 12.830 -8.402  14.318  0.52 15.23 ?  9   TYR   A CD1  1 
ATOM   170  C CD1  B TYR   A 1 9   ? 12.716 -7.856  14.463  0.48 16.15 ?  9   TYR   A CD1  1 
ATOM   171  C CD2  A TYR   A 1 9   ? 13.023 -8.844  11.983  0.52 14.74 ?  9   TYR   A CD2  1 
ATOM   172  C CD2  B TYR   A 1 9   ? 12.963 -8.539  12.195  0.48 15.51 ?  9   TYR   A CD2  1 
ATOM   173  C CE1  A TYR   A 1 9   ? 13.652 -7.300  14.187  0.52 16.06 ?  9   TYR   A CE1  1 
ATOM   174  C CE1  B TYR   A 1 9   ? 13.479 -6.733  14.212  0.48 15.85 ?  9   TYR   A CE1  1 
ATOM   175  C CE2  A TYR   A 1 9   ? 13.850 -7.750  11.841  0.52 16.00 ?  9   TYR   A CE2  1 
ATOM   176  C CE2  B TYR   A 1 9   ? 13.729 -7.415  11.933  0.48 15.77 ?  9   TYR   A CE2  1 
ATOM   177  C CZ   A TYR   A 1 9   ? 14.160 -6.982  12.943  0.52 16.59 ?  9   TYR   A CZ   1 
ATOM   178  C CZ   B TYR   A 1 9   ? 13.983 -6.515  12.945  0.48 15.46 ?  9   TYR   A CZ   1 
ATOM   179  O OH   A TYR   A 1 9   ? 14.980 -5.896  12.789  0.52 17.93 ?  9   TYR   A OH   1 
ATOM   180  O OH   B TYR   A 1 9   ? 14.740 -5.391  12.694  0.48 15.82 ?  9   TYR   A OH   1 
ATOM   181  H H    A TYR   A 1 9   ? 10.326 -9.819  15.446  0.52 18.41 ?  9   TYR   A H    1 
ATOM   182  H H    B TYR   A 1 9   ? 10.390 -9.378  15.834  0.48 22.09 ?  9   TYR   A H    1 
ATOM   183  H HA   A TYR   A 1 9   ? 9.897  -9.343  12.843  0.52 17.22 ?  9   TYR   A HA   1 
ATOM   184  H HA   B TYR   A 1 9   ? 9.888  -8.987  13.240  0.48 19.62 ?  9   TYR   A HA   1 
ATOM   185  H HB2  A TYR   A 1 9   ? 11.864 -10.891 14.149  0.52 17.13 ?  9   TYR   A HB2  1 
ATOM   186  H HB2  B TYR   A 1 9   ? 11.913 -10.408 14.570  0.48 19.41 ?  9   TYR   A HB2  1 
ATOM   187  H HB3  A TYR   A 1 9   ? 11.667 -10.924 12.574  0.52 17.13 ?  9   TYR   A HB3  1 
ATOM   188  H HB3  B TYR   A 1 9   ? 11.702 -10.620 13.011  0.48 19.41 ?  9   TYR   A HB3  1 
ATOM   189  H HD1  A TYR   A 1 9   ? 12.476 -8.619  15.155  0.52 18.28 ?  9   TYR   A HD1  1 
ATOM   190  H HD1  B TYR   A 1 9   ? 12.375 -7.999  15.318  0.48 19.38 ?  9   TYR   A HD1  1 
ATOM   191  H HD2  A TYR   A 1 9   ? 12.814 -9.360  11.236  0.52 17.69 ?  9   TYR   A HD2  1 
ATOM   192  H HD2  B TYR   A 1 9   ? 12.793 -9.144  11.510  0.48 18.61 ?  9   TYR   A HD2  1 
ATOM   193  H HE1  A TYR   A 1 9   ? 13.862 -6.782  14.929  0.52 19.27 ?  9   TYR   A HE1  1 
ATOM   194  H HE1  B TYR   A 1 9   ? 13.651 -6.127  14.894  0.48 19.01 ?  9   TYR   A HE1  1 
ATOM   195  H HE2  A TYR   A 1 9   ? 14.196 -7.530  11.007  0.52 19.19 ?  9   TYR   A HE2  1 
ATOM   196  H HE2  B TYR   A 1 9   ? 14.072 -7.267  11.080  0.48 18.92 ?  9   TYR   A HE2  1 
ATOM   197  H HH   A TYR   A 1 9   ? 15.094 -5.521  13.533  0.52 21.51 ?  9   TYR   A HH   1 
ATOM   198  H HH   B TYR   A 1 9   ? 14.815 -4.942  13.401  0.48 18.98 ?  9   TYR   A HH   1 
ATOM   199  N N    A LEU   A 1 10  ? 8.900  -11.388 11.934  0.52 13.47 ?  10  LEU   A N    1 
ATOM   200  N N    B LEU   A 1 10  ? 8.806  -11.005 12.371  0.48 14.57 ?  10  LEU   A N    1 
ATOM   201  C CA   A LEU   A 1 10  ? 8.328  -12.617 11.408  0.52 13.53 ?  10  LEU   A CA   1 
ATOM   202  C CA   B LEU   A 1 10  ? 8.154  -12.204 11.868  0.48 14.45 ?  10  LEU   A CA   1 
ATOM   203  C C    A LEU   A 1 10  ? 9.456  -13.555 10.990  0.52 13.42 ?  10  LEU   A C    1 
ATOM   204  C C    B LEU   A 1 10  ? 9.229  -13.178 11.405  0.48 13.85 ?  10  LEU   A C    1 
ATOM   205  O O    A LEU   A 1 10  ? 10.417 -13.138 10.345  0.52 12.78 ?  10  LEU   A O    1 
ATOM   206  O O    B LEU   A 1 10  ? 10.135 -12.803 10.657  0.48 13.22 ?  10  LEU   A O    1 
ATOM   207  C CB   A LEU   A 1 10  ? 7.466  -12.289 10.189  0.52 14.86 ?  10  LEU   A CB   1 
ATOM   208  C CB   B LEU   A 1 10  ? 7.246  -11.835 10.694  0.48 14.72 ?  10  LEU   A CB   1 
ATOM   209  C CG   A LEU   A 1 10  ? 6.775  -13.458 9.489   0.52 17.33 ?  10  LEU   A CG   1 
ATOM   210  C CG   B LEU   A 1 10  ? 6.686  -12.990 9.865   0.48 16.00 ?  10  LEU   A CG   1 
ATOM   211  C CD1  A LEU   A 1 10  ? 5.714  -14.048 10.396  0.52 18.48 ?  10  LEU   A CD1  1 
ATOM   212  C CD1  B LEU   A 1 10  ? 5.699  -13.789 10.685  0.48 16.93 ?  10  LEU   A CD1  1 
ATOM   213  C CD2  A LEU   A 1 10  ? 6.182  -13.016 8.166   0.52 18.54 ?  10  LEU   A CD2  1 
ATOM   214  C CD2  B LEU   A 1 10  ? 6.051  -12.461 8.588   0.48 17.05 ?  10  LEU   A CD2  1 
ATOM   215  H H    A LEU   A 1 10  ? 8.989  -10.771 11.337  0.52 16.16 ?  10  LEU   A H    1 
ATOM   216  H H    B LEU   A 1 10  ? 8.867  -10.377 11.783  0.48 17.49 ?  10  LEU   A H    1 
ATOM   217  H HA   A LEU   A 1 10  ? 7.784  -13.051 12.082  0.52 16.24 ?  10  LEU   A HA   1 
ATOM   218  H HA   B LEU   A 1 10  ? 7.619  -12.616 12.566  0.48 17.34 ?  10  LEU   A HA   1 
ATOM   219  H HB2  A LEU   A 1 10  ? 6.772  -11.676 10.467  0.52 17.83 ?  10  LEU   A HB2  1 
ATOM   220  H HB2  B LEU   A 1 10  ? 6.483  -11.339 11.041  0.48 17.66 ?  10  LEU   A HB2  1 
ATOM   221  H HB3  A LEU   A 1 10  ? 8.031  -11.858 9.529   0.52 17.83 ?  10  LEU   A HB3  1 
ATOM   222  H HB3  B LEU   A 1 10  ? 7.745  -11.264 10.091  0.48 17.66 ?  10  LEU   A HB3  1 
ATOM   223  H HG   A LEU   A 1 10  ? 7.429  -14.152 9.303   0.52 20.80 ?  10  LEU   A HG   1 
ATOM   224  H HG   B LEU   A 1 10  ? 7.410  -13.580 9.609   0.48 19.20 ?  10  LEU   A HG   1 
ATOM   225  H HD11 A LEU   A 1 10  ? 5.327  -14.828 9.968   0.52 22.17 ?  10  LEU   A HD11 1 
ATOM   226  H HD11 B LEU   A 1 10  ? 5.388  -14.543 10.157  0.48 20.31 ?  10  LEU   A HD11 1 
ATOM   227  H HD12 A LEU   A 1 10  ? 6.121  -14.304 11.239  0.52 22.17 ?  10  LEU   A HD12 1 
ATOM   228  H HD12 B LEU   A 1 10  ? 6.138  -14.108 11.489  0.48 20.31 ?  10  LEU   A HD12 1 
ATOM   229  H HD13 A LEU   A 1 10  ? 5.026  -13.382 10.554  0.52 22.17 ?  10  LEU   A HD13 1 
ATOM   230  H HD13 B LEU   A 1 10  ? 4.951  -13.220 10.921  0.48 20.31 ?  10  LEU   A HD13 1 
ATOM   231  H HD21 A LEU   A 1 10  ? 5.748  -13.776 7.747   0.52 22.24 ?  10  LEU   A HD21 1 
ATOM   232  H HD21 B LEU   A 1 10  ? 5.850  -13.211 8.006   0.48 20.46 ?  10  LEU   A HD21 1 
ATOM   233  H HD22 A LEU   A 1 10  ? 5.532  -12.315 8.333   0.52 22.24 ?  10  LEU   A HD22 1 
ATOM   234  H HD22 B LEU   A 1 10  ? 5.237  -11.984 8.813   0.48 20.46 ?  10  LEU   A HD22 1 
ATOM   235  H HD23 A LEU   A 1 10  ? 6.891  -12.684 7.597   0.52 22.24 ?  10  LEU   A HD23 1 
ATOM   236  H HD23 B LEU   A 1 10  ? 6.676  -11.864 8.148   0.48 20.46 ?  10  LEU   A HD23 1 
ATOM   237  N N    A LYS   A 1 11  ? 9.329  -14.826 11.354  0.52 13.57 ?  11  LYS   A N    1 
ATOM   238  N N    B LYS   A 1 11  ? 9.122  -14.427 11.837  0.48 14.03 ?  11  LYS   A N    1 
ATOM   239  C CA   A LYS   A 1 11  ? 10.327 -15.835 11.019  0.52 13.67 ?  11  LYS   A CA   1 
ATOM   240  C CA   B LYS   A 1 11  ? 10.097 -15.440 11.460  0.48 14.00 ?  11  LYS   A CA   1 
ATOM   241  C C    A LYS   A 1 11  ? 9.970  -16.438 9.668   0.52 14.31 ?  11  LYS   A C    1 
ATOM   242  C C    B LYS   A 1 11  ? 9.740  -15.970 10.075  0.48 13.32 ?  11  LYS   A C    1 
ATOM   243  O O    A LYS   A 1 11  ? 8.906  -17.049 9.524   0.52 15.27 ?  11  LYS   A O    1 
ATOM   244  O O    B LYS   A 1 11  ? 8.605  -16.402 9.844   0.48 14.04 ?  11  LYS   A O    1 
ATOM   245  C CB   A LYS   A 1 11  ? 10.351 -16.905 12.110  0.52 13.83 ?  11  LYS   A CB   1 
ATOM   246  C CB   B LYS   A 1 11  ? 10.092 -16.558 12.498  0.48 14.50 ?  11  LYS   A CB   1 
ATOM   247  C CG   A LYS   A 1 11  ? 11.394 -18.009 11.960  0.52 14.49 ?  11  LYS   A CG   1 
ATOM   248  C CG   B LYS   A 1 11  ? 11.067 -17.679 12.235  0.48 14.96 ?  11  LYS   A CG   1 
ATOM   249  C CD   A LYS   A 1 11  ? 11.502 -18.780 13.275  0.52 14.78 ?  11  LYS   A CD   1 
ATOM   250  C CD   B LYS   A 1 11  ? 11.076 -18.648 13.398  0.48 15.48 ?  11  LYS   A CD   1 
ATOM   251  C CE   A LYS   A 1 11  ? 12.531 -19.903 13.229  0.52 15.02 ?  11  LYS   A CE   1 
ATOM   252  C CE   B LYS   A 1 11  ? 12.048 -19.788 13.153  0.48 16.11 ?  11  LYS   A CE   1 
ATOM   253  N NZ   A LYS   A 1 11  ? 13.914 -19.411 12.988  0.52 14.84 ?  11  LYS   A NZ   1 
ATOM   254  N NZ   B LYS   A 1 11  ? 13.453 -19.313 12.979  0.48 16.60 ?  11  LYS   A NZ   1 
ATOM   255  H H    A LYS   A 1 11  ? 8.660  -15.135 11.790  0.52 16.28 ?  11  LYS   A H    1 
ATOM   256  H H    B LYS   A 1 11  ? 8.485  -14.716 12.336  0.48 16.83 ?  11  LYS   A H    1 
ATOM   257  H HA   A LYS   A 1 11  ? 11.204 -15.427 10.956  0.52 16.40 ?  11  LYS   A HA   1 
ATOM   258  H HA   B LYS   A 1 11  ? 10.983 -15.039 11.426  0.48 16.80 ?  11  LYS   A HA   1 
ATOM   259  H HB2  A LYS   A 1 11  ? 10.517 -16.467 12.958  0.52 16.60 ?  11  LYS   A HB2  1 
ATOM   260  H HB2  B LYS   A 1 11  ? 10.314 -16.174 13.362  0.48 17.40 ?  11  LYS   A HB2  1 
ATOM   261  H HB3  A LYS   A 1 11  ? 9.482  -17.335 12.134  0.52 16.60 ?  11  LYS   A HB3  1 
ATOM   262  H HB3  B LYS   A 1 11  ? 9.205  -16.942 12.530  0.48 17.40 ?  11  LYS   A HB3  1 
ATOM   263  H HG2  A LYS   A 1 11  ? 11.127 -18.625 11.258  0.52 17.39 ?  11  LYS   A HG2  1 
ATOM   264  H HG2  B LYS   A 1 11  ? 10.802 -18.160 11.436  0.48 17.95 ?  11  LYS   A HG2  1 
ATOM   265  H HG3  A LYS   A 1 11  ? 12.261 -17.619 11.758  0.52 17.39 ?  11  LYS   A HG3  1 
ATOM   266  H HG3  B LYS   A 1 11  ? 11.961 -17.315 12.133  0.48 17.95 ?  11  LYS   A HG3  1 
ATOM   267  H HD2  A LYS   A 1 11  ? 11.759 -18.169 13.982  0.52 17.74 ?  11  LYS   A HD2  1 
ATOM   268  H HD2  B LYS   A 1 11  ? 11.346 -18.183 14.206  0.48 18.57 ?  11  LYS   A HD2  1 
ATOM   269  H HD3  A LYS   A 1 11  ? 10.638 -19.177 13.479  0.52 17.74 ?  11  LYS   A HD3  1 
ATOM   270  H HD3  B LYS   A 1 11  ? 10.185 -19.024 13.510  0.48 18.57 ?  11  LYS   A HD3  1 
ATOM   271  H HE2  A LYS   A 1 11  ? 12.524 -20.372 14.080  0.52 18.03 ?  11  LYS   A HE2  1 
ATOM   272  H HE2  B LYS   A 1 11  ? 12.027 -20.394 13.908  0.48 19.34 ?  11  LYS   A HE2  1 
ATOM   273  H HE3  A LYS   A 1 11  ? 12.299 -20.515 12.514  0.52 18.03 ?  11  LYS   A HE3  1 
ATOM   274  H HE3  B LYS   A 1 11  ? 11.788 -20.256 12.342  0.48 19.34 ?  11  LYS   A HE3  1 
ATOM   275  H HZ1  A LYS   A 1 11  ? 14.477 -20.099 12.943  0.52 17.81 ?  11  LYS   A HZ1  1 
ATOM   276  H HZ1  B LYS   A 1 11  ? 14.001 -20.008 12.873  0.48 19.92 ?  11  LYS   A HZ1  1 
ATOM   277  H HZ2  A LYS   A 1 11  ? 13.945 -18.962 12.221  0.52 17.81 ?  11  LYS   A HZ2  1 
ATOM   278  H HZ2  B LYS   A 1 11  ? 13.514 -18.788 12.261  0.48 19.92 ?  11  LYS   A HZ2  1 
ATOM   279  H HZ3  A LYS   A 1 11  ? 14.165 -18.874 13.650  0.52 17.81 ?  11  LYS   A HZ3  1 
ATOM   280  H HZ3  B LYS   A 1 11  ? 13.711 -18.851 13.695  0.48 19.92 ?  11  LYS   A HZ3  1 
ATOM   281  N N    A LEU   A 1 12  ? 10.852 -16.274 8.679   0.52 13.96 ?  12  LEU   A N    1 
ATOM   282  N N    B LEU   A 1 12  ? 10.690 -15.905 9.143   0.48 13.38 ?  12  LEU   A N    1 
ATOM   283  C CA   A LEU   A 1 12  ? 10.622 -16.879 7.370   0.52 14.06 ?  12  LEU   A CA   1 
ATOM   284  C CA   B LEU   A 1 12  ? 10.472 -16.401 7.788   0.48 13.61 ?  12  LEU   A CA   1 
ATOM   285  C C    A LEU   A 1 12  ? 11.231 -18.273 7.255   0.52 13.85 ?  12  LEU   A C    1 
ATOM   286  C C    B LEU   A 1 12  ? 11.027 -17.803 7.575   0.48 13.93 ?  12  LEU   A C    1 
ATOM   287  O O    A LEU   A 1 12  ? 10.600 -19.171 6.688   0.52 13.77 ?  12  LEU   A O    1 
ATOM   288  O O    B LEU   A 1 12  ? 10.362 -18.648 6.966   0.48 14.30 ?  12  LEU   A O    1 
ATOM   289  C CB   A LEU   A 1 12  ? 11.178 -15.989 6.254   0.52 14.60 ?  12  LEU   A CB   1 
ATOM   290  C CB   B LEU   A 1 12  ? 11.088 -15.450 6.755   0.48 15.35 ?  12  LEU   A CB   1 
ATOM   291  C CG   A LEU   A 1 12  ? 10.519 -14.623 6.066   0.52 14.29 ?  12  LEU   A CG   1 
ATOM   292  C CG   B LEU   A 1 12  ? 10.417 -14.089 6.563   0.48 16.41 ?  12  LEU   A CG   1 
ATOM   293  C CD1  A LEU   A 1 12  ? 11.247 -13.835 4.983   0.52 15.12 ?  12  LEU   A CD1  1 
ATOM   294  C CD1  B LEU   A 1 12  ? 11.037 -13.356 5.375   0.48 17.38 ?  12  LEU   A CD1  1 
ATOM   295  C CD2  A LEU   A 1 12  ? 9.032  -14.762 5.736   0.52 14.57 ?  12  LEU   A CD2  1 
ATOM   296  C CD2  B LEU   A 1 12  ? 8.918  -14.263 6.378   0.48 16.93 ?  12  LEU   A CD2  1 
ATOM   297  H H    A LEU   A 1 12  ? 11.589 -15.824 8.741   0.52 16.75 ?  12  LEU   A H    1 
ATOM   298  H H    B LEU   A 1 12  ? 11.479 -15.569 9.272   0.48 16.05 ?  12  LEU   A H    1 
ATOM   299  H HA   A LEU   A 1 12  ? 9.667  -16.962 7.232   0.52 16.87 ?  12  LEU   A HA   1 
ATOM   300  H HA   B LEU   A 1 12  ? 9.519  -16.437 7.629   0.48 16.34 ?  12  LEU   A HA   1 
ATOM   301  H HB2  A LEU   A 1 12  ? 12.117 -15.830 6.429   0.52 17.52 ?  12  LEU   A HB2  1 
ATOM   302  H HB2  B LEU   A 1 12  ? 12.009 -15.276 7.012   0.48 18.42 ?  12  LEU   A HB2  1 
ATOM   303  H HB3  A LEU   A 1 12  ? 11.089 -16.467 5.413   0.52 17.52 ?  12  LEU   A HB3  1 
ATOM   304  H HB3  B LEU   A 1 12  ? 11.077 -15.893 5.893   0.48 18.42 ?  12  LEU   A HB3  1 
ATOM   305  H HG   A LEU   A 1 12  ? 10.594 -14.124 6.890   0.52 17.14 ?  12  LEU   A HG   1 
ATOM   306  H HG   B LEU   A 1 12  ? 10.564 -13.548 7.356   0.48 19.69 ?  12  LEU   A HG   1 
ATOM   307  H HD11 A LEU   A 1 12  ? 10.819 -12.970 4.875   0.52 18.14 ?  12  LEU   A HD11 1 
ATOM   308  H HD11 B LEU   A 1 12  ? 10.602 -12.495 5.272   0.48 20.86 ?  12  LEU   A HD11 1 
ATOM   309  H HD12 A LEU   A 1 12  ? 12.174 -13.711 5.250   0.52 18.14 ?  12  LEU   A HD12 1 
ATOM   310  H HD12 B LEU   A 1 12  ? 11.985 -13.230 5.539   0.48 20.86 ?  12  LEU   A HD12 1 
ATOM   311  H HD13 A LEU   A 1 12  ? 11.210 -14.328 4.148   0.52 18.14 ?  12  LEU   A HD13 1 
ATOM   312  H HD13 B LEU   A 1 12  ? 10.908 -13.889 4.574   0.48 20.86 ?  12  LEU   A HD13 1 
ATOM   313  H HD21 A LEU   A 1 12  ? 8.652  -13.881 5.611   0.52 17.48 ?  12  LEU   A HD21 1 
ATOM   314  H HD21 B LEU   A 1 12  ? 8.548  -13.447 6.017   0.48 20.32 ?  12  LEU   A HD21 1 
ATOM   315  H HD22 A LEU   A 1 12  ? 8.937  -15.278 4.922   0.52 17.48 ?  12  LEU   A HD22 1 
ATOM   316  H HD22 B LEU   A 1 12  ? 8.763  -15.001 5.769   0.48 20.32 ?  12  LEU   A HD22 1 
ATOM   317  H HD23 A LEU   A 1 12  ? 8.583  -15.214 6.468   0.52 17.48 ?  12  LEU   A HD23 1 
ATOM   318  H HD23 B LEU   A 1 12  ? 8.518  -14.458 7.242   0.48 20.32 ?  12  LEU   A HD23 1 
ATOM   319  N N    A THR   A 1 13  ? 12.446 -18.461 7.767   0.52 14.06 ?  13  THR   A N    1 
ATOM   320  N N    B THR   A 1 13  ? 12.234 -18.068 8.060   0.48 14.41 ?  13  THR   A N    1 
ATOM   321  C CA   A THR   A 1 13  ? 13.147 -19.745 7.744   0.52 14.07 ?  13  THR   A CA   1 
ATOM   322  C CA   B THR   A 1 13  ? 12.875 -19.367 7.923   0.48 15.16 ?  13  THR   A CA   1 
ATOM   323  C C    A THR   A 1 13  ? 13.899 -19.906 9.060   0.52 14.90 ?  13  THR   A C    1 
ATOM   324  C C    B THR   A 1 13  ? 13.639 -19.652 9.207   0.48 16.01 ?  13  THR   A C    1 
ATOM   325  O O    A THR   A 1 13  ? 13.765 -19.099 9.985   0.52 14.72 ?  13  THR   A O    1 
ATOM   326  O O    B THR   A 1 13  ? 13.557 -18.907 10.190  0.48 16.16 ?  13  THR   A O    1 
ATOM   327  C CB   A THR   A 1 13  ? 14.139 -19.853 6.574   0.52 14.54 ?  13  THR   A CB   1 
ATOM   328  C CB   B THR   A 1 13  ? 13.843 -19.392 6.732   0.48 15.03 ?  13  THR   A CB   1 
ATOM   329  O OG1  A THR   A 1 13  ? 15.216 -18.928 6.775   0.52 15.25 ?  13  THR   A OG1  1 
ATOM   330  O OG1  B THR   A 1 13  ? 14.915 -18.479 6.984   0.48 14.87 ?  13  THR   A OG1  1 
ATOM   331  C CG2  A THR   A 1 13  ? 13.479 -19.563 5.242   0.52 14.47 ?  13  THR   A CG2  1 
ATOM   332  C CG2  B THR   A 1 13  ? 13.150 -19.023 5.423   0.48 14.87 ?  13  THR   A CG2  1 
ATOM   333  H H    A THR   A 1 13  ? 12.899 -17.835 8.142   0.52 16.87 ?  13  THR   A H    1 
ATOM   334  H H    B THR   A 1 13  ? 12.716 -17.487 8.471   0.48 17.29 ?  13  THR   A H    1 
ATOM   335  H HA   A THR   A 1 13  ? 12.502 -20.464 7.661   0.52 16.88 ?  13  THR   A HA   1 
ATOM   336  H HA   B THR   A 1 13  ? 12.204 -20.053 7.797   0.48 18.19 ?  13  THR   A HA   1 
ATOM   337  H HB   A THR   A 1 13  ? 14.500 -20.750 6.543   0.52 17.45 ?  13  THR   A HB   1 
ATOM   338  H HB   B THR   A 1 13  ? 14.209 -20.285 6.634   0.48 18.03 ?  13  THR   A HB   1 
ATOM   339  H HG1  A THR   A 1 13  ? 15.770 -18.981 6.138   0.52 18.30 ?  13  THR   A HG1  1 
ATOM   340  H HG1  B THR   A 1 13  ? 15.455 -18.478 6.334   0.48 17.84 ?  13  THR   A HG1  1 
ATOM   341  H HG21 A THR   A 1 13  ? 14.117 -19.706 4.522   0.52 17.36 ?  13  THR   A HG21 1 
ATOM   342  H HG21 B THR   A 1 13  ? 13.774 -19.105 4.681   0.48 17.85 ?  13  THR   A HG21 1 
ATOM   343  H HG22 A THR   A 1 13  ? 12.725 -20.155 5.115   0.52 17.36 ?  13  THR   A HG22 1 
ATOM   344  H HG22 B THR   A 1 13  ? 12.400 -19.618 5.266   0.48 17.85 ?  13  THR   A HG22 1 
ATOM   345  H HG23 A THR   A 1 13  ? 13.174 -18.645 5.214   0.52 17.36 ?  13  THR   A HG23 1 
ATOM   346  H HG23 B THR   A 1 13  ? 12.828 -18.110 5.461   0.48 17.85 ?  13  THR   A HG23 1 
ATOM   347  N N    A ASP   A 1 14  ? 14.738 -20.943 9.124   0.52 15.22 ?  14  ASP   A N    1 
ATOM   348  N N    B ASP   A 1 14  ? 14.416 -20.734 9.171   0.48 16.77 ?  14  ASP   A N    1 
ATOM   349  C CA   A ASP   A 1 14  ? 15.526 -21.187 10.325  0.52 16.55 ?  14  ASP   A CA   1 
ATOM   350  C CA   B ASP   A 1 14  ? 15.307 -21.053 10.274  0.48 17.52 ?  14  ASP   A CA   1 
ATOM   351  C C    A ASP   A 1 14  ? 16.324 -19.964 10.772  0.52 15.85 ?  14  ASP   A C    1 
ATOM   352  C C    B ASP   A 1 14  ? 16.177 -19.856 10.640  0.48 15.89 ?  14  ASP   A C    1 
ATOM   353  O O    A ASP   A 1 14  ? 16.597 -19.812 11.968  0.52 16.59 ?  14  ASP   A O    1 
ATOM   354  O O    B ASP   A 1 14  ? 16.325 -19.528 11.823  0.48 16.40 ?  14  ASP   A O    1 
ATOM   355  C CB   A ASP   A 1 14  ? 16.491 -22.343 10.089  0.52 19.42 ?  14  ASP   A CB   1 
ATOM   356  C CB   B ASP   A 1 14  ? 16.177 -22.249 9.890   0.48 20.40 ?  14  ASP   A CB   1 
ATOM   357  C CG   A ASP   A 1 14  ? 17.398 -22.575 11.269  0.52 22.80 ?  14  ASP   A CG   1 
ATOM   358  C CG   B ASP   A 1 14  ? 17.150 -22.635 10.988  0.48 23.53 ?  14  ASP   A CG   1 
ATOM   359  O OD1  A ASP   A 1 14  ? 16.922 -23.148 12.275  0.52 24.35 ?  14  ASP   A OD1  1 
ATOM   360  O OD1  B ASP   A 1 14  ? 16.716 -22.703 12.159  0.48 24.53 ?  14  ASP   A OD1  1 
ATOM   361  O OD2  A ASP   A 1 14  ? 18.573 -22.165 11.193  0.52 24.41 -1 14  ASP   A OD2  1 
ATOM   362  O OD2  B ASP   A 1 14  ? 18.338 -22.880 10.687  0.48 24.82 -1 14  ASP   A OD2  1 
ATOM   363  H H    A ASP   A 1 14  ? 14.881 -21.506 8.486   0.52 18.26 ?  14  ASP   A H    1 
ATOM   364  H H    B ASP   A 1 14  ? 14.455 -21.277 8.513   0.48 20.13 ?  14  ASP   A H    1 
ATOM   365  H HA   A ASP   A 1 14  ? 14.934 -21.439 11.045  0.52 19.86 ?  14  ASP   A HA   1 
ATOM   366  H HA   B ASP   A 1 14  ? 14.778 -21.294 11.050  0.48 21.02 ?  14  ASP   A HA   1 
ATOM   367  H HB2  A ASP   A 1 14  ? 15.982 -23.161 9.941   0.52 23.31 ?  14  ASP   A HB2  1 
ATOM   368  H HB2  B ASP   A 1 14  ? 15.592 -23.009 9.698   0.48 24.48 ?  14  ASP   A HB2  1 
ATOM   369  H HB3  A ASP   A 1 14  ? 17.044 -22.156 9.315   0.52 23.31 ?  14  ASP   A HB3  1 
ATOM   370  H HB3  B ASP   A 1 14  ? 16.686 -22.028 9.094   0.48 24.48 ?  14  ASP   A HB3  1 
ATOM   371  N N    A ASN   A 1 15  ? 16.730 -19.091 9.839   0.52 15.42 ?  15  ASN   A N    1 
ATOM   372  N N    B ASN   A 1 15  ? 16.730 -19.165 9.635   0.48 14.81 ?  15  ASN   A N    1 
ATOM   373  C CA   A ASN   A 1 15  ? 17.664 -18.009 10.159  0.52 15.76 ?  15  ASN   A CA   1 
ATOM   374  C CA   B ASN   A 1 15  ? 17.757 -18.148 9.859   0.48 14.97 ?  15  ASN   A CA   1 
ATOM   375  C C    A ASN   A 1 15  ? 17.279 -16.634 9.624   0.52 15.16 ?  15  ASN   A C    1 
ATOM   376  C C    B ASN   A 1 15  ? 17.409 -16.749 9.348   0.48 15.15 ?  15  ASN   A C    1 
ATOM   377  O O    A ASN   A 1 15  ? 17.955 -15.657 9.974   0.52 14.86 ?  15  ASN   A O    1 
ATOM   378  O O    B ASN   A 1 15  ? 18.255 -15.849 9.450   0.48 14.64 ?  15  ASN   A O    1 
ATOM   379  C CB   A ASN   A 1 15  ? 19.072 -18.330 9.631   0.52 15.99 ?  15  ASN   A CB   1 
ATOM   380  C CB   B ASN   A 1 15  ? 19.103 -18.600 9.263   0.48 14.91 ?  15  ASN   A CB   1 
ATOM   381  C CG   A ASN   A 1 15  ? 19.097 -18.525 8.125   0.52 15.85 ?  15  ASN   A CG   1 
ATOM   382  C CG   B ASN   A 1 15  ? 19.096 -18.620 7.744   0.48 15.50 ?  15  ASN   A CG   1 
ATOM   383  O OD1  A ASN   A 1 15  ? 18.325 -19.322 7.583   0.52 16.36 ?  15  ASN   A OD1  1 
ATOM   384  O OD1  B ASN   A 1 15  ? 18.469 -19.484 7.129   0.48 16.35 ?  15  ASN   A OD1  1 
ATOM   385  N ND2  A ASN   A 1 15  ? 19.975 -17.790 7.438   0.52 15.66 ?  15  ASN   A ND2  1 
ATOM   386  N ND2  B ASN   A 1 15  ? 19.811 -17.675 7.130   0.48 15.52 ?  15  ASN   A ND2  1 
ATOM   387  H H    A ASN   A 1 15  ? 16.479 -19.101 9.023   0.52 18.51 ?  15  ASN   A H    1 
ATOM   388  H H    B ASN   A 1 15  ? 16.518 -19.266 8.813   0.48 17.77 ?  15  ASN   A H    1 
ATOM   389  H HA   A ASN   A 1 15  ? 17.736 -17.935 11.127  0.52 18.91 ?  15  ASN   A HA   1 
ATOM   390  H HA   B ASN   A 1 15  ? 17.898 -18.064 10.811  0.48 17.97 ?  15  ASN   A HA   1 
ATOM   391  H HB2  A ASN   A 1 15  ? 19.672 -17.589 9.849   0.52 19.18 ?  15  ASN   A HB2  1 
ATOM   392  H HB2  B ASN   A 1 15  ? 19.804 -17.986 9.550   0.48 17.89 ?  15  ASN   A HB2  1 
ATOM   393  H HB3  A ASN   A 1 15  ? 19.395 -19.142 10.049  0.52 19.18 ?  15  ASN   A HB3  1 
ATOM   394  H HB3  B ASN   A 1 15  ? 19.310 -19.496 9.576   0.48 17.89 ?  15  ASN   A HB3  1 
ATOM   395  H HD21 A ASN   A 1 15  ? 20.020 -17.865 6.581   0.52 18.79 ?  15  ASN   A HD21 1 
ATOM   396  H HD21 B ASN   A 1 15  ? 19.841 -17.648 6.269   0.48 18.62 ?  15  ASN   A HD21 1 
ATOM   397  H HD22 A ASN   A 1 15  ? 20.494 -17.237 7.846   0.52 18.79 ?  15  ASN   A HD22 1 
ATOM   398  H HD22 B ASN   A 1 15  ? 20.238 -17.086 7.590   0.48 18.62 ?  15  ASN   A HD22 1 
ATOM   399  N N    A VAL   A 1 16  ? 16.248 -16.521 8.785   0.52 15.11 ?  16  VAL   A N    1 
ATOM   400  N N    B VAL   A 1 16  ? 16.198 -16.523 8.834   0.48 15.74 ?  16  VAL   A N    1 
ATOM   401  C CA   A VAL   A 1 16  ? 15.850 -15.254 8.173   0.52 14.67 ?  16  VAL   A CA   1 
ATOM   402  C CA   B VAL   A 1 16  ? 15.796 -15.233 8.270   0.48 15.77 ?  16  VAL   A CA   1 
ATOM   403  C C    A VAL   A 1 16  ? 14.554 -14.762 8.804   0.52 14.29 ?  16  VAL   A C    1 
ATOM   404  C C    B VAL   A 1 16  ? 14.561 -14.717 9.007   0.48 15.79 ?  16  VAL   A C    1 
ATOM   405  O O    A VAL   A 1 16  ? 13.539 -15.472 8.813   0.52 13.99 ?  16  VAL   A O    1 
ATOM   406  O O    B VAL   A 1 16  ? 13.597 -15.463 9.220   0.48 15.44 ?  16  VAL   A O    1 
ATOM   407  C CB   A VAL   A 1 16  ? 15.715 -15.362 6.644   0.52 15.12 ?  16  VAL   A CB   1 
ATOM   408  C CB   B VAL   A 1 16  ? 15.541 -15.327 6.753   0.48 16.30 ?  16  VAL   A CB   1 
ATOM   409  C CG1  A VAL   A 1 16  ? 15.271 -14.020 6.051   0.52 15.94 ?  16  VAL   A CG1  1 
ATOM   410  C CG1  B VAL   A 1 16  ? 15.110 -13.975 6.184   0.48 17.11 ?  16  VAL   A CG1  1 
ATOM   411  C CG2  A VAL   A 1 16  ? 17.027 -15.817 6.020   0.52 15.85 ?  16  VAL   A CG2  1 
ATOM   412  C CG2  B VAL   A 1 16  ? 16.778 -15.852 6.018   0.48 16.90 ?  16  VAL   A CG2  1 
ATOM   413  H H    A VAL   A 1 16  ? 15.759 -17.185 8.553   0.52 18.13 ?  16  VAL   A H    1 
ATOM   414  H H    B VAL   A 1 16  ? 15.579 -17.117 8.804   0.48 18.88 ?  16  VAL   A H    1 
ATOM   415  H HA   A VAL   A 1 16  ? 16.538 -14.594 8.357   0.52 17.61 ?  16  VAL   A HA   1 
ATOM   416  H HA   B VAL   A 1 16  ? 16.517 -14.595 8.407   0.48 18.93 ?  16  VAL   A HA   1 
ATOM   417  H HB   A VAL   A 1 16  ? 15.037 -16.025 6.437   0.52 18.15 ?  16  VAL   A HB   1 
ATOM   418  H HB   B VAL   A 1 16  ? 14.822 -15.956 6.600   0.48 19.57 ?  16  VAL   A HB   1 
ATOM   419  H HG11 A VAL   A 1 16  ? 15.391 -14.049 5.091   0.52 19.13 ?  16  VAL   A HG11 1 
ATOM   420  H HG11 B VAL   A 1 16  ? 15.128 -14.025 5.215   0.48 20.53 ?  16  VAL   A HG11 1 
ATOM   421  H HG12 A VAL   A 1 16  ? 14.335 -13.875 6.263   0.52 19.13 ?  16  VAL   A HG12 1 
ATOM   422  H HG12 B VAL   A 1 16  ? 14.212 -13.778 6.488   0.48 20.53 ?  16  VAL   A HG12 1 
ATOM   423  H HG13 A VAL   A 1 16  ? 15.813 -13.313 6.433   0.52 19.13 ?  16  VAL   A HG13 1 
ATOM   424  H HG13 B VAL   A 1 16  ? 15.726 -13.294 6.491   0.48 20.53 ?  16  VAL   A HG13 1 
ATOM   425  H HG21 A VAL   A 1 16  ? 16.933 -15.818 5.056   0.52 19.02 ?  16  VAL   A HG21 1 
ATOM   426  H HG21 B VAL   A 1 16  ? 16.602 -15.857 5.063   0.48 20.28 ?  16  VAL   A HG21 1 
ATOM   427  H HG22 A VAL   A 1 16  ? 17.732 -15.209 6.285   0.52 19.02 ?  16  VAL   A HG22 1 
ATOM   428  H HG22 B VAL   A 1 16  ? 17.534 -15.276 6.211   0.48 20.28 ?  16  VAL   A HG22 1 
ATOM   429  H HG23 A VAL   A 1 16  ? 17.231 -16.714 6.333   0.52 19.02 ?  16  VAL   A HG23 1 
ATOM   430  H HG23 B VAL   A 1 16  ? 16.968 -16.757 6.319   0.48 20.28 ?  16  VAL   A HG23 1 
ATOM   431  N N    A TYR   A 1 17  ? 14.598 -13.530 9.300   0.52 13.93 ?  17  TYR   A N    1 
ATOM   432  N N    B TYR   A 1 17  ? 14.595 -13.432 9.372   0.48 15.65 ?  17  TYR   A N    1 
ATOM   433  C CA   A TYR   A 1 17  ? 13.484 -12.824 9.910   0.52 13.73 ?  17  TYR   A CA   1 
ATOM   434  C CA   B TYR   A 1 17  ? 13.542 -12.755 10.122  0.48 14.66 ?  17  TYR   A CA   1 
ATOM   435  C C    A TYR   A 1 17  ? 13.213 -11.536 9.134   0.52 13.41 ?  17  TYR   A C    1 
ATOM   436  C C    B TYR   A 1 17  ? 13.268 -11.398 9.480   0.48 14.86 ?  17  TYR   A C    1 
ATOM   437  O O    A TYR   A 1 17  ? 14.098 -11.002 8.462   0.52 12.98 ?  17  TYR   A O    1 
ATOM   438  O O    B TYR   A 1 17  ? 14.181 -10.774 8.937   0.48 14.38 ?  17  TYR   A O    1 
ATOM   439  C CB   A TYR   A 1 17  ? 13.818 -12.495 11.372  0.52 14.85 ?  17  TYR   A CB   1 
ATOM   440  C CB   B TYR   A 1 17  ? 13.988 -12.538 11.575  0.48 14.91 ?  17  TYR   A CB   1 
ATOM   441  C CG   A TYR   A 1 17  ? 13.979 -13.736 12.224  0.52 15.96 ?  17  TYR   A CG   1 
ATOM   442  C CG   B TYR   A 1 17  ? 14.253 -13.820 12.340  0.48 15.38 ?  17  TYR   A CG   1 
ATOM   443  C CD1  A TYR   A 1 17  ? 15.161 -14.472 12.206  0.52 16.91 ?  17  TYR   A CD1  1 
ATOM   444  C CD1  B TYR   A 1 17  ? 15.460 -14.500 12.212  0.48 16.38 ?  17  TYR   A CD1  1 
ATOM   445  C CD2  A TYR   A 1 17  ? 12.943 -14.184 13.029  0.52 16.59 ?  17  TYR   A CD2  1 
ATOM   446  C CD2  B TYR   A 1 17  ? 13.296 -14.345 13.196  0.48 15.31 ?  17  TYR   A CD2  1 
ATOM   447  C CE1  A TYR   A 1 17  ? 15.305 -15.629 12.972  0.52 17.22 ?  17  TYR   A CE1  1 
ATOM   448  C CE1  B TYR   A 1 17  ? 15.698 -15.681 12.912  0.48 16.63 ?  17  TYR   A CE1  1 
ATOM   449  C CE2  A TYR   A 1 17  ? 13.076 -15.340 13.798  0.52 17.30 ?  17  TYR   A CE2  1 
ATOM   450  C CE2  B TYR   A 1 17  ? 13.523 -15.521 13.898  0.48 15.87 ?  17  TYR   A CE2  1 
ATOM   451  C CZ   A TYR   A 1 17  ? 14.259 -16.053 13.770  0.52 16.89 ?  17  TYR   A CZ   1 
ATOM   452  C CZ   B TYR   A 1 17  ? 14.724 -16.182 13.756  0.48 16.41 ?  17  TYR   A CZ   1 
ATOM   453  O OH   A TYR   A 1 17  ? 14.384 -17.195 14.535  0.52 17.49 ?  17  TYR   A OH   1 
ATOM   454  O OH   B TYR   A 1 17  ? 14.940 -17.348 14.461  0.48 17.86 ?  17  TYR   A OH   1 
ATOM   455  H H    A TYR   A 1 17  ? 15.320 -13.052 9.288   0.52 16.72 ?  17  TYR   A H    1 
ATOM   456  H H    B TYR   A 1 17  ? 15.259 -12.906 9.185   0.48 18.77 ?  17  TYR   A H    1 
ATOM   457  H HA   A TYR   A 1 17  ? 12.700 -13.392 9.881   0.52 16.47 ?  17  TYR   A HA   1 
ATOM   458  H HA   B TYR   A 1 17  ? 12.733 -13.283 10.111  0.48 17.59 ?  17  TYR   A HA   1 
ATOM   459  H HB2  A TYR   A 1 17  ? 14.645 -11.986 11.401  0.52 17.82 ?  17  TYR   A HB2  1 
ATOM   460  H HB2  B TYR   A 1 17  ? 14.807 -12.019 11.573  0.48 17.89 ?  17  TYR   A HB2  1 
ATOM   461  H HB3  A TYR   A 1 17  ? 13.098 -11.965 11.736  0.52 17.82 ?  17  TYR   A HB3  1 
ATOM   462  H HB3  B TYR   A 1 17  ? 13.292 -12.052 12.041  0.48 17.89 ?  17  TYR   A HB3  1 
ATOM   463  H HD1  A TYR   A 1 17  ? 15.868 -14.186 11.669  0.52 20.30 ?  17  TYR   A HD1  1 
ATOM   464  H HD1  B TYR   A 1 17  ? 16.117 -14.165 11.643  0.48 19.66 ?  17  TYR   A HD1  1 
ATOM   465  H HD2  A TYR   A 1 17  ? 12.142 -13.715 13.053  0.52 19.90 ?  17  TYR   A HD2  1 
ATOM   466  H HD2  B TYR   A 1 17  ? 12.479 -13.908 13.293  0.48 18.37 ?  17  TYR   A HD2  1 
ATOM   467  H HE1  A TYR   A 1 17  ? 16.108 -16.108 12.952  0.52 20.67 ?  17  TYR   A HE1  1 
ATOM   468  H HE1  B TYR   A 1 17  ? 16.511 -16.125 12.817  0.48 19.95 ?  17  TYR   A HE1  1 
ATOM   469  H HE2  A TYR   A 1 17  ? 12.375 -15.632 14.335  0.52 20.76 ?  17  TYR   A HE2  1 
ATOM   470  H HE2  B TYR   A 1 17  ? 12.867 -15.857 14.464  0.48 19.05 ?  17  TYR   A HE2  1 
ATOM   471  H HH   A TYR   A 1 17  ? 13.640 -17.419 14.844  0.52 20.98 ?  17  TYR   A HH   1 
ATOM   472  H HH   B TYR   A 1 17  ? 15.672 -17.686 14.229  0.48 21.43 ?  17  TYR   A HH   1 
ATOM   473  N N    A ILE   A 1 18  ? 11.987 -11.012 9.239   0.52 13.35 ?  18  ILE   A N    1 
ATOM   474  N N    B ILE   A 1 18  ? 12.016 -10.920 9.548   0.48 14.75 ?  18  ILE   A N    1 
ATOM   475  C CA   A ILE   A 1 18  ? 11.591 -9.841  8.454   0.52 13.57 ?  18  ILE   A CA   1 
ATOM   476  C CA   B ILE   A 1 18  ? 11.639 -9.705  8.822   0.48 13.93 ?  18  ILE   A CA   1 
ATOM   477  C C    A ILE   A 1 18  ? 10.593 -8.994  9.240   0.52 14.23 ?  18  ILE   A C    1 
ATOM   478  C C    B ILE   A 1 18  ? 10.691 -8.828  9.633   0.48 14.20 ?  18  ILE   A C    1 
ATOM   479  O O    A ILE   A 1 18  ? 9.761  -9.514  9.983   0.52 13.93 ?  18  ILE   A O    1 
ATOM   480  O O    B ILE   A 1 18  ? 9.904  -9.312  10.450  0.48 15.07 ?  18  ILE   A O    1 
ATOM   481  C CB   A ILE   A 1 18  ? 11.059 -10.274 7.066   0.52 14.10 ?  18  ILE   A CB   1 
ATOM   482  C CB   B ILE   A 1 18  ? 11.034 -10.056 7.446   0.48 13.84 ?  18  ILE   A CB   1 
ATOM   483  C CG1  A ILE   A 1 18  ? 10.924 -9.075  6.129   0.52 14.42 ?  18  ILE   A CG1  1 
ATOM   484  C CG1  B ILE   A 1 18  ? 11.068 -8.856  6.498   0.48 14.99 ?  18  ILE   A CG1  1 
ATOM   485  C CG2  A ILE   A 1 18  ? 9.747  -11.060 7.205   0.52 14.08 ?  18  ILE   A CG2  1 
ATOM   486  C CG2  B ILE   A 1 18  ? 9.615  -10.595 7.603   0.48 14.80 ?  18  ILE   A CG2  1 
ATOM   487  C CD1  A ILE   A 1 18  ? 10.736 -9.473  4.678   0.52 16.68 ?  18  ILE   A CD1  1 
ATOM   488  C CD1  B ILE   A 1 18  ? 10.761 -9.236  5.071   0.48 16.35 ?  18  ILE   A CD1  1 
ATOM   489  H H    A ILE   A 1 18  ? 11.383 -11.316 9.761   0.52 16.02 ?  18  ILE   A H    1 
ATOM   490  H H    B ILE   A 1 18  ? 11.375 -11.283 9.998   0.48 17.70 ?  18  ILE   A H    1 
ATOM   491  H HA   A ILE   A 1 18  ? 12.380 -9.304  8.300   0.52 16.28 ?  18  ILE   A HA   1 
ATOM   492  H HA   B ILE   A 1 18  ? 12.446 -9.188  8.662   0.48 16.72 ?  18  ILE   A HA   1 
ATOM   493  H HB   A ILE   A 1 18  ? 11.710 -10.876 6.671   0.52 16.92 ?  18  ILE   A HB   1 
ATOM   494  H HB   B ILE   A 1 18  ? 11.576 -10.753 7.056   0.48 16.60 ?  18  ILE   A HB   1 
ATOM   495  H HG12 A ILE   A 1 18  ? 10.155 -8.549  6.397   0.52 17.30 ?  18  ILE   A HG12 1 
ATOM   496  H HG12 B ILE   A 1 18  ? 10.408 -8.204  6.782   0.48 17.99 ?  18  ILE   A HG12 1 
ATOM   497  H HG13 A ILE   A 1 18  ? 11.730 -8.538  6.188   0.52 17.30 ?  18  ILE   A HG13 1 
ATOM   498  H HG13 B ILE   A 1 18  ? 11.954 -8.460  6.515   0.48 17.99 ?  18  ILE   A HG13 1 
ATOM   499  H HG21 A ILE   A 1 18  ? 9.501  -11.426 6.338   0.52 16.89 ?  18  ILE   A HG21 1 
ATOM   500  H HG21 B ILE   A 1 18  ? 9.347  -11.018 6.770   0.48 17.76 ?  18  ILE   A HG21 1 
ATOM   501  H HG22 A ILE   A 1 18  ? 9.875  -11.782 7.840   0.52 16.89 ?  18  ILE   A HG22 1 
ATOM   502  H HG22 B ILE   A 1 18  ? 9.602  -11.243 8.322   0.48 17.76 ?  18  ILE   A HG22 1 
ATOM   503  H HG23 A ILE   A 1 18  ? 9.050  -10.464 7.518   0.52 16.89 ?  18  ILE   A HG23 1 
ATOM   504  H HG23 B ILE   A 1 18  ? 9.013  -9.861  7.806   0.48 17.76 ?  18  ILE   A HG23 1 
ATOM   505  H HD11 A ILE   A 1 18  ? 10.704 -8.670  4.133   0.52 20.01 ?  18  ILE   A HD11 1 
ATOM   506  H HD11 B ILE   A 1 18  ? 10.866 -8.457  4.504   0.48 19.63 ?  18  ILE   A HD11 1 
ATOM   507  H HD12 A ILE   A 1 18  ? 11.480 -10.029 4.404   0.52 20.01 ?  18  ILE   A HD12 1 
ATOM   508  H HD12 B ILE   A 1 18  ? 11.372 -9.935  4.791   0.48 19.63 ?  18  ILE   A HD12 1 
ATOM   509  H HD13 A ILE   A 1 18  ? 9.904  -9.964  4.591   0.52 20.01 ?  18  ILE   A HD13 1 
ATOM   510  H HD13 B ILE   A 1 18  ? 9.846  -9.559  5.020   0.48 19.63 ?  18  ILE   A HD13 1 
ATOM   511  N N    A LYS   A 1 19  ? 10.675 -7.674  9.056   0.52 15.24 ?  19  LYS   A N    1 
ATOM   512  N N    B LYS   A 1 19  ? 10.754 -7.520  9.372   0.48 15.14 ?  19  LYS   A N    1 
ATOM   513  C CA   A LYS   A 1 19  ? 9.879  -6.712  9.813   0.52 15.68 ?  19  LYS   A CA   1 
ATOM   514  C CA   B LYS   A 1 19  ? 9.917  -6.545  10.061  0.48 16.12 ?  19  LYS   A CA   1 
ATOM   515  C C    A LYS   A 1 19  ? 9.701  -5.446  8.981   0.52 14.80 ?  19  LYS   A C    1 
ATOM   516  C C    B LYS   A 1 19  ? 9.724  -5.332  9.162   0.48 15.91 ?  19  LYS   A C    1 
ATOM   517  O O    A LYS   A 1 19  ? 10.544 -5.120  8.136   0.52 14.50 ?  19  LYS   A O    1 
ATOM   518  O O    B LYS   A 1 19  ? 10.687 -4.842  8.566   0.48 16.13 ?  19  LYS   A O    1 
ATOM   519  C CB   A LYS   A 1 19  ? 10.599 -6.359  11.128  0.52 16.24 ?  19  LYS   A CB   1 
ATOM   520  C CB   B LYS   A 1 19  ? 10.587 -6.109  11.368  0.48 16.46 ?  19  LYS   A CB   1 
ATOM   521  C CG   A LYS   A 1 19  ? 9.886  -5.394  12.080  0.52 17.22 ?  19  LYS   A CG   1 
ATOM   522  C CG   B LYS   A 1 19  ? 9.788  -5.134  12.205  0.48 17.67 ?  19  LYS   A CG   1 
ATOM   523  C CD   A LYS   A 1 19  ? 10.754 -5.153  13.322  0.52 18.17 ?  19  LYS   A CD   1 
ATOM   524  C CD   B LYS   A 1 19  ? 10.538 -4.810  13.481  0.48 18.53 ?  19  LYS   A CD   1 
ATOM   525  C CE   A LYS   A 1 19  ? 10.132 -4.188  14.321  0.52 18.90 ?  19  LYS   A CE   1 
ATOM   526  C CE   B LYS   A 1 19  ? 9.752  -3.877  14.380  0.48 19.68 ?  19  LYS   A CE   1 
ATOM   527  N NZ   A LYS   A 1 19  ? 11.019 -3.983  15.508  0.52 19.06 ?  19  LYS   A NZ   1 
ATOM   528  N NZ   B LYS   A 1 19  ? 10.574 -3.461  15.546  0.48 20.29 ?  19  LYS   A NZ   1 
ATOM   529  H H    A LYS   A 1 19  ? 11.203 -7.312  8.487   0.52 18.29 ?  19  LYS   A H    1 
ATOM   530  H H    B LYS   A 1 19  ? 11.280 -7.167  8.786   0.48 18.17 ?  19  LYS   A H    1 
ATOM   531  H HA   A LYS   A 1 19  ? 9.010  -7.098  10.019  0.52 18.82 ?  19  LYS   A HA   1 
ATOM   532  H HA   B LYS   A 1 19  ? 9.052  -6.935  10.264  0.48 19.34 ?  19  LYS   A HA   1 
ATOM   533  H HB2  A LYS   A 1 19  ? 10.749 -7.182  11.621  0.52 19.49 ?  19  LYS   A HB2  1 
ATOM   534  H HB2  B LYS   A 1 19  ? 10.743 -6.896  11.914  0.48 19.75 ?  19  LYS   A HB2  1 
ATOM   535  H HB3  A LYS   A 1 19  ? 11.451 -5.960  10.905  0.52 19.49 ?  19  LYS   A HB3  1 
ATOM   536  H HB3  B LYS   A 1 19  ? 11.433 -5.686  11.157  0.48 19.75 ?  19  LYS   A HB3  1 
ATOM   537  H HG2  A LYS   A 1 19  ? 9.740  -4.542  11.639  0.52 20.66 ?  19  LYS   A HG2  1 
ATOM   538  H HG2  B LYS   A 1 19  ? 9.655  -4.311  11.709  0.48 21.21 ?  19  LYS   A HG2  1 
ATOM   539  H HG3  A LYS   A 1 19  ? 9.040  -5.776  12.367  0.52 20.66 ?  19  LYS   A HG3  1 
ATOM   540  H HG3  B LYS   A 1 19  ? 8.934  -5.532  12.440  0.48 21.21 ?  19  LYS   A HG3  1 
ATOM   541  H HD2  A LYS   A 1 19  ? 10.893 -5.999  13.778  0.52 21.80 ?  19  LYS   A HD2  1 
ATOM   542  H HD2  B LYS   A 1 19  ? 10.704 -5.634  13.967  0.48 22.24 ?  19  LYS   A HD2  1 
ATOM   543  H HD3  A LYS   A 1 19  ? 11.606 -4.785  13.044  0.52 21.80 ?  19  LYS   A HD3  1 
ATOM   544  H HD3  B LYS   A 1 19  ? 11.377 -4.382  13.253  0.48 22.24 ?  19  LYS   A HD3  1 
ATOM   545  H HE2  A LYS   A 1 19  ? 9.997  -3.326  13.895  0.52 22.68 ?  19  LYS   A HE2  1 
ATOM   546  H HE2  B LYS   A 1 19  ? 9.503  -3.084  13.878  0.48 23.62 ?  19  LYS   A HE2  1 
ATOM   547  H HE3  A LYS   A 1 19  ? 9.287  -4.544  14.634  0.52 22.68 ?  19  LYS   A HE3  1 
ATOM   548  H HE3  B LYS   A 1 19  ? 8.961  -4.334  14.705  0.48 23.62 ?  19  LYS   A HE3  1 
ATOM   549  H HZ1  A LYS   A 1 19  ? 10.641 -3.409  16.076  0.52 22.88 ?  19  LYS   A HZ1  1 
ATOM   550  H HZ1  B LYS   A 1 19  ? 10.106 -2.914  16.066  0.48 24.34 ?  19  LYS   A HZ1  1 
ATOM   551  H HZ2  A LYS   A 1 19  ? 11.149 -4.757  15.926  0.52 22.88 ?  19  LYS   A HZ2  1 
ATOM   552  H HZ2  B LYS   A 1 19  ? 10.814 -4.177  16.017  0.48 24.34 ?  19  LYS   A HZ2  1 
ATOM   553  H HZ3  A LYS   A 1 19  ? 11.804 -3.657  15.249  0.52 22.88 ?  19  LYS   A HZ3  1 
ATOM   554  H HZ3  B LYS   A 1 19  ? 11.306 -3.040  15.265  0.48 24.34 ?  19  LYS   A HZ3  1 
ATOM   555  N N    A ASN   A 1 20  ? 8.592  -4.736  9.220   0.52 15.80 ?  20  ASN   A N    1 
ATOM   556  N N    B ASN   A 1 20  ? 8.481  -4.857  9.058   0.48 16.39 ?  20  ASN   A N    1 
ATOM   557  C CA   A ASN   A 1 20  ? 8.378  -3.406  8.648   0.52 16.23 ?  20  ASN   A CA   1 
ATOM   558  C CA   B ASN   A 1 20  ? 8.208  -3.591  8.386   0.48 16.46 ?  20  ASN   A CA   1 
ATOM   559  C C    A ASN   A 1 20  ? 8.981  -2.392  9.612   0.52 16.51 ?  20  ASN   A C    1 
ATOM   560  C C    B ASN   A 1 20  ? 8.750  -2.446  9.229   0.48 17.12 ?  20  ASN   A C    1 
ATOM   561  O O    A ASN   A 1 20  ? 8.440  -2.161  10.700  0.52 15.75 ?  20  ASN   A O    1 
ATOM   562  O O    B ASN   A 1 20  ? 8.064  -1.951  10.131  0.48 18.63 ?  20  ASN   A O    1 
ATOM   563  C CB   A ASN   A 1 20  ? 6.888  -3.146  8.419   0.52 16.79 ?  20  ASN   A CB   1 
ATOM   564  C CB   B ASN   A 1 20  ? 6.701  -3.420  8.160   0.48 16.50 ?  20  ASN   A CB   1 
ATOM   565  C CG   A ASN   A 1 20  ? 6.571  -1.682  8.101   0.52 17.49 ?  20  ASN   A CG   1 
ATOM   566  C CG   B ASN   A 1 20  ? 6.340  -2.092  7.489   0.48 16.25 ?  20  ASN   A CG   1 
ATOM   567  O OD1  A ASN   A 1 20  ? 5.623  -1.119  8.648   0.52 20.09 ?  20  ASN   A OD1  1 
ATOM   568  O OD1  B ASN   A 1 20  ? 5.248  -1.547  7.713   0.48 16.16 ?  20  ASN   A OD1  1 
ATOM   569  N ND2  A ASN   A 1 20  ? 7.353  -1.069  7.210   0.52 17.06 ?  20  ASN   A ND2  1 
ATOM   570  N ND2  B ASN   A 1 20  ? 7.238  -1.578  6.652   0.48 16.71 ?  20  ASN   A ND2  1 
ATOM   571  H H    A ASN   A 1 20  ? 7.947  -5.008  9.723   0.52 18.96 ?  20  ASN   A H    1 
ATOM   572  H H    B ASN   A 1 20  ? 7.788  -5.264  9.359   0.48 19.67 ?  20  ASN   A H    1 
ATOM   573  H HA   A ASN   A 1 20  ? 8.838  -3.345  7.801   0.52 19.47 ?  20  ASN   A HA   1 
ATOM   574  H HA   B ASN   A 1 20  ? 8.655  -3.578  7.526   0.48 19.75 ?  20  ASN   A HA   1 
ATOM   575  H HB2  A ASN   A 1 20  ? 6.589  -3.683  7.670   0.52 20.15 ?  20  ASN   A HB2  1 
ATOM   576  H HB2  B ASN   A 1 20  ? 6.385  -4.138  7.594   0.48 19.80 ?  20  ASN   A HB2  1 
ATOM   577  H HB3  A ASN   A 1 20  ? 6.399  -3.387  9.219   0.52 20.15 ?  20  ASN   A HB3  1 
ATOM   578  H HB3  B ASN   A 1 20  ? 6.252  -3.461  9.019   0.48 19.80 ?  20  ASN   A HB3  1 
ATOM   579  H HD21 A ASN   A 1 20  ? 7.209  -0.246  7.002   0.52 20.48 ?  20  ASN   A HD21 1 
ATOM   580  H HD21 B ASN   A 1 20  ? 7.074  -0.836  6.262   0.48 20.05 ?  20  ASN   A HD21 1 
ATOM   581  H HD22 A ASN   A 1 20  ? 8.007  -1.494  6.846   0.52 20.48 ?  20  ASN   A HD22 1 
ATOM   582  H HD22 B ASN   A 1 20  ? 7.983  -1.986  6.508   0.48 20.05 ?  20  ASN   A HD22 1 
ATOM   583  N N    A ALA   A 1 21  ? 10.119 -1.812  9.237   0.52 17.32 ?  21  ALA   A N    1 
ATOM   584  N N    B ALA   A 1 21  ? 9.983  -2.021  8.953   0.48 17.07 ?  21  ALA   A N    1 
ATOM   585  C CA   A ALA   A 1 21  ? 10.804 -0.902  10.141  0.52 17.42 ?  21  ALA   A CA   1 
ATOM   586  C CA   B ALA   A 1 21  ? 10.610 -0.983  9.760   0.48 16.90 ?  21  ALA   A CA   1 
ATOM   587  C C    A ALA   A 1 21  ? 11.786 -0.043  9.362   0.52 17.86 ?  21  ALA   A C    1 
ATOM   588  C C    B ALA   A 1 21  ? 11.695 -0.278  8.958   0.48 15.46 ?  21  ALA   A C    1 
ATOM   589  O O    A ALA   A 1 21  ? 12.288 -0.444  8.308   0.52 18.14 ?  21  ALA   A O    1 
ATOM   590  O O    B ALA   A 1 21  ? 12.166 -0.778  7.932   0.48 14.68 ?  21  ALA   A O    1 
ATOM   591  C CB   A ALA   A 1 21  ? 11.537 -1.670  11.246  0.52 18.03 ?  21  ALA   A CB   1 
ATOM   592  C CB   B ALA   A 1 21  ? 11.204 -1.552  11.053  0.48 18.88 ?  21  ALA   A CB   1 
ATOM   593  H H    A ALA   A 1 21  ? 10.514 -1.932  8.480   0.52 20.78 ?  21  ALA   A H    1 
ATOM   594  H H    B ALA   A 1 21  ? 10.463 -2.321  8.307   0.48 20.48 ?  21  ALA   A H    1 
ATOM   595  H HA   A ALA   A 1 21  ? 10.152 -0.316  10.557  0.52 20.91 ?  21  ALA   A HA   1 
ATOM   596  H HA   B ALA   A 1 21  ? 9.933  -0.335  10.004  0.48 20.28 ?  21  ALA   A HA   1 
ATOM   597  H HB1  A ALA   A 1 21  ? 11.940 -1.033  11.853  0.52 21.64 ?  21  ALA   A HB1  1 
ATOM   598  H HB1  B ALA   A 1 21  ? 11.607 -0.828  11.558  0.48 22.66 ?  21  ALA   A HB1  1 
ATOM   599  H HB2  A ALA   A 1 21  ? 10.891 -2.218  11.726  0.52 21.64 ?  21  ALA   A HB2  1 
ATOM   600  H HB2  B ALA   A 1 21  ? 10.495 -1.963  11.577  0.48 22.66 ?  21  ALA   A HB2  1 
ATOM   601  H HB3  A ALA   A 1 21  ? 12.213 -2.232  10.846  0.52 21.64 ?  21  ALA   A HB3  1 
ATOM   602  H HB3  B ALA   A 1 21  ? 11.875 -2.215  10.831  0.48 22.66 ?  21  ALA   A HB3  1 
ATOM   603  N N    A ASP   A 1 22  ? 12.032 1.152   9.895   0.52 17.93 ?  22  ASP   A N    1 
ATOM   604  N N    B ASP   A 1 22  ? 12.080 0.898   9.456   0.48 15.04 ?  22  ASP   A N    1 
ATOM   605  C CA   A ASP   A 1 22  ? 13.105 2.018   9.425   0.52 17.54 ?  22  ASP   A CA   1 
ATOM   606  C CA   B ASP   A 1 22  ? 13.207 1.660   8.931   0.48 14.74 ?  22  ASP   A CA   1 
ATOM   607  C C    A ASP   A 1 22  ? 14.419 1.523   10.013  0.52 16.69 ?  22  ASP   A C    1 
ATOM   608  C C    B ASP   A 1 22  ? 14.487 1.134   9.577   0.48 13.16 ?  22  ASP   A C    1 
ATOM   609  O O    A ASP   A 1 22  ? 14.601 1.543   11.235  0.52 16.89 ?  22  ASP   A O    1 
ATOM   610  O O    B ASP   A 1 22  ? 14.607 1.132   10.808  0.48 13.59 ?  22  ASP   A O    1 
ATOM   611  C CB   A ASP   A 1 22  ? 12.826 3.445   9.887   0.52 19.11 ?  22  ASP   A CB   1 
ATOM   612  C CB   B ASP   A 1 22  ? 12.994 3.134   9.286   0.48 16.55 ?  22  ASP   A CB   1 
ATOM   613  C CG   A ASP   A 1 22  ? 13.860 4.442   9.389   0.52 20.11 ?  22  ASP   A CG   1 
ATOM   614  C CG   B ASP   A 1 22  ? 14.008 4.061   8.644   0.48 16.74 ?  22  ASP   A CG   1 
ATOM   615  O OD1  A ASP   A 1 22  ? 14.905 4.025   8.849   0.52 19.68 ?  22  ASP   A OD1  1 
ATOM   616  O OD1  B ASP   A 1 22  ? 15.144 3.622   8.352   0.48 14.54 ?  22  ASP   A OD1  1 
ATOM   617  O OD2  A ASP   A 1 22  ? 13.612 5.659   9.528   0.52 21.44 -1 22  ASP   A OD2  1 
ATOM   618  O OD2  B ASP   A 1 22  ? 13.663 5.247   8.440   0.48 19.36 -1 22  ASP   A OD2  1 
ATOM   619  H H    A ASP   A 1 22  ? 11.568 1.491   10.535  0.52 21.52 ?  22  ASP   A H    1 
ATOM   620  H H    B ASP   A 1 22  ? 11.681 1.283   10.118  0.48 18.05 ?  22  ASP   A H    1 
ATOM   621  H HA   A ASP   A 1 22  ? 13.155 1.992   8.457   0.52 21.04 ?  22  ASP   A HA   1 
ATOM   622  H HA   B ASP   A 1 22  ? 13.257 1.559   7.966   0.48 17.69 ?  22  ASP   A HA   1 
ATOM   623  H HB2  A ASP   A 1 22  ? 11.966 3.723   9.547   0.52 22.94 ?  22  ASP   A HB2  1 
ATOM   624  H HB2  B ASP   A 1 22  ? 12.120 3.409   8.979   0.48 19.86 ?  22  ASP   A HB2  1 
ATOM   625  H HB3  A ASP   A 1 22  ? 12.818 3.458   10.861  0.52 22.94 ?  22  ASP   A HB3  1 
ATOM   626  H HB3  B ASP   A 1 22  ? 13.058 3.234   10.248  0.48 19.86 ?  22  ASP   A HB3  1 
ATOM   627  N N    A ILE   A 1 23  ? 15.333 1.083   9.143   0.52 16.46 ?  23  ILE   A N    1 
ATOM   628  N N    B ILE   A 1 23  ? 15.437 0.674   8.754   0.48 12.92 ?  23  ILE   A N    1 
ATOM   629  C CA   A ILE   A 1 23  ? 16.580 0.475   9.601   0.52 15.31 ?  23  ILE   A CA   1 
ATOM   630  C CA   B ILE   A 1 23  ? 16.673 0.101   9.284   0.48 12.97 ?  23  ILE   A CA   1 
ATOM   631  C C    A ILE   A 1 23  ? 17.372 1.431   10.484  0.52 15.31 ?  23  ILE   A C    1 
ATOM   632  C C    B ILE   A 1 23  ? 17.389 1.089   10.196  0.48 12.92 ?  23  ILE   A C    1 
ATOM   633  O O    A ILE   A 1 23  ? 18.083 0.997   11.399  0.52 15.92 ?  23  ILE   A O    1 
ATOM   634  O O    B ILE   A 1 23  ? 18.060 0.684   11.154  0.48 13.03 ?  23  ILE   A O    1 
ATOM   635  C CB   A ILE   A 1 23  ? 17.396 -0.038  8.392   0.52 14.40 ?  23  ILE   A CB   1 
ATOM   636  C CB   B ILE   A 1 23  ? 17.592 -0.413  8.151   0.48 13.08 ?  23  ILE   A CB   1 
ATOM   637  C CG1  A ILE   A 1 23  ? 18.564 -0.916  8.860   0.52 14.23 ?  23  ILE   A CG1  1 
ATOM   638  C CG1  B ILE   A 1 23  ? 18.653 -1.359  8.726   0.48 13.42 ?  23  ILE   A CG1  1 
ATOM   639  C CG2  A ILE   A 1 23  ? 17.872 1.124   7.520   0.52 15.07 ?  23  ILE   A CG2  1 
ATOM   640  C CG2  B ILE   A 1 23  ? 18.257 0.742   7.410   0.48 13.08 ?  23  ILE   A CG2  1 
ATOM   641  C CD1  A ILE   A 1 23  ? 19.232 -1.696  7.737   0.52 14.73 ?  23  ILE   A CD1  1 
ATOM   642  C CD1  B ILE   A 1 23  ? 19.619 -1.911  7.690   0.48 13.67 ?  23  ILE   A CD1  1 
ATOM   643  H H    A ILE   A 1 23  ? 15.251 1.123   8.290   0.52 19.75 ?  23  ILE   A H    1 
ATOM   644  H H    B ILE   A 1 23  ? 15.384 0.668   7.905   0.48 15.50 ?  23  ILE   A H    1 
ATOM   645  H HA   A ILE   A 1 23  ? 16.362 -0.302  10.141  0.52 18.37 ?  23  ILE   A HA   1 
ATOM   646  H HA   B ILE   A 1 23  ? 16.433 -0.671  9.819   0.48 15.56 ?  23  ILE   A HA   1 
ATOM   647  H HB   A ILE   A 1 23  ? 16.815 -0.594  7.852   0.52 17.28 ?  23  ILE   A HB   1 
ATOM   648  H HB   B ILE   A 1 23  ? 17.056 -0.916  7.518   0.48 15.69 ?  23  ILE   A HB   1 
ATOM   649  H HG12 A ILE   A 1 23  ? 19.241 -0.355  9.269   0.52 17.08 ?  23  ILE   A HG12 1 
ATOM   650  H HG12 B ILE   A 1 23  ? 19.177 -0.883  9.389   0.48 16.10 ?  23  ILE   A HG12 1 
ATOM   651  H HG13 A ILE   A 1 23  ? 18.236 -1.560  9.508   0.52 17.08 ?  23  ILE   A HG13 1 
ATOM   652  H HG13 B ILE   A 1 23  ? 18.209 -2.116  9.143   0.48 16.10 ?  23  ILE   A HG13 1 
ATOM   653  H HG21 A ILE   A 1 23  ? 18.268 0.770   6.708   0.52 18.09 ?  23  ILE   A HG21 1 
ATOM   654  H HG21 B ILE   A 1 23  ? 18.629 0.410   6.573   0.48 15.70 ?  23  ILE   A HG21 1 
ATOM   655  H HG22 A ILE   A 1 23  ? 17.110 1.681   7.298   0.52 18.09 ?  23  ILE   A HG22 1 
ATOM   656  H HG22 B ILE   A 1 23  ? 17.595 1.422   7.228   0.48 15.70 ?  23  ILE   A HG22 1 
ATOM   657  H HG23 A ILE   A 1 23  ? 18.529 1.642   8.009   0.52 18.09 ?  23  ILE   A HG23 1 
ATOM   658  H HG23 B ILE   A 1 23  ? 18.968 1.107   7.961   0.48 15.70 ?  23  ILE   A HG23 1 
ATOM   659  H HD11 A ILE   A 1 23  ? 19.929 -2.260  8.111   0.52 17.68 ?  23  ILE   A HD11 1 
ATOM   660  H HD11 B ILE   A 1 23  ? 20.159 -2.605  8.100   0.48 16.40 ?  23  ILE   A HD11 1 
ATOM   661  H HD12 A ILE   A 1 23  ? 18.566 -2.247  7.294   0.52 17.68 ?  23  ILE   A HD12 1 
ATOM   662  H HD12 B ILE   A 1 23  ? 19.110 -2.280  6.952   0.48 16.40 ?  23  ILE   A HD12 1 
ATOM   663  H HD13 A ILE   A 1 23  ? 19.618 -1.072  7.103   0.52 17.68 ?  23  ILE   A HD13 1 
ATOM   664  H HD13 B ILE   A 1 23  ? 20.188 -1.192  7.375   0.48 16.40 ?  23  ILE   A HD13 1 
ATOM   665  N N    A VAL   A 1 24  ? 17.254 2.738   10.245  0.52 15.66 ?  24  VAL   A N    1 
ATOM   666  N N    B VAL   A 1 24  ? 17.260 2.390   9.924   0.48 13.60 ?  24  VAL   A N    1 
ATOM   667  C CA   A VAL   A 1 24  ? 17.928 3.716   11.097  0.52 16.51 ?  24  VAL   A CA   1 
ATOM   668  C CA   B VAL   A 1 24  ? 17.907 3.392   10.766  0.48 15.49 ?  24  VAL   A CA   1 
ATOM   669  C C    A VAL   A 1 24  ? 17.406 3.629   12.525  0.52 17.13 ?  24  VAL   A C    1 
ATOM   670  C C    B VAL   A 1 24  ? 17.294 3.399   12.160  0.48 16.45 ?  24  VAL   A C    1 
ATOM   671  O O    A VAL   A 1 24  ? 18.181 3.562   13.489  0.52 17.43 ?  24  VAL   A O    1 
ATOM   672  O O    B VAL   A 1 24  ? 18.008 3.458   13.168  0.48 17.55 ?  24  VAL   A O    1 
ATOM   673  C CB   A VAL   A 1 24  ? 17.760 5.131   10.520  0.52 16.95 ?  24  VAL   A CB   1 
ATOM   674  C CB   B VAL   A 1 24  ? 17.836 4.778   10.101  0.48 16.10 ?  24  VAL   A CB   1 
ATOM   675  C CG1  A VAL   A 1 24  ? 18.230 6.178   11.526  0.52 17.21 ?  24  VAL   A CG1  1 
ATOM   676  C CG1  B VAL   A 1 24  ? 18.543 5.812   10.960  0.48 17.88 ?  24  VAL   A CG1  1 
ATOM   677  C CG2  A VAL   A 1 24  ? 18.511 5.254   9.204   0.52 17.39 ?  24  VAL   A CG2  1 
ATOM   678  C CG2  B VAL   A 1 24  ? 18.431 4.730   8.704   0.48 16.14 ?  24  VAL   A CG2  1 
ATOM   679  H H    A VAL   A 1 24  ? 16.790 3.077   9.606   0.52 18.79 ?  24  VAL   A H    1 
ATOM   680  H H    B VAL   A 1 24  ? 16.801 2.710   9.273   0.48 16.32 ?  24  VAL   A H    1 
ATOM   681  H HA   A VAL   A 1 24  ? 18.875 3.511   11.114  0.52 19.81 ?  24  VAL   A HA   1 
ATOM   682  H HA   B VAL   A 1 24  ? 18.841 3.157   10.860  0.48 18.59 ?  24  VAL   A HA   1 
ATOM   683  H HB   A VAL   A 1 24  ? 16.820 5.288   10.340  0.52 20.34 ?  24  VAL   A HB   1 
ATOM   684  H HB   B VAL   A 1 24  ? 16.905 5.040   10.020  0.48 19.32 ?  24  VAL   A HB   1 
ATOM   685  H HG11 A VAL   A 1 24  ? 18.384 7.012   11.059  0.52 20.65 ?  24  VAL   A HG11 1 
ATOM   686  H HG11 B VAL   A 1 24  ? 18.643 6.629   10.450  0.48 21.46 ?  24  VAL   A HG11 1 
ATOM   687  H HG12 A VAL   A 1 24  ? 17.546 6.297   12.202  0.52 20.65 ?  24  VAL   A HG12 1 
ATOM   688  H HG12 B VAL   A 1 24  ? 18.010 5.982   11.755  0.48 21.46 ?  24  VAL   A HG12 1 
ATOM   689  H HG13 A VAL   A 1 24  ? 19.055 5.870   11.935  0.52 20.65 ?  24  VAL   A HG13 1 
ATOM   690  H HG13 B VAL   A 1 24  ? 19.414 5.469   11.214  0.48 21.46 ?  24  VAL   A HG13 1 
ATOM   691  H HG21 A VAL   A 1 24  ? 18.285 6.101   8.790   0.52 20.87 ?  24  VAL   A HG21 1 
ATOM   692  H HG21 B VAL   A 1 24  ? 18.472 5.629   8.349   0.48 19.37 ?  24  VAL   A HG21 1 
ATOM   693  H HG22 A VAL   A 1 24  ? 19.464 5.218   9.381   0.52 20.87 ?  24  VAL   A HG22 1 
ATOM   694  H HG22 B VAL   A 1 24  ? 19.323 4.351   8.756   0.48 19.37 ?  24  VAL   A HG22 1 
ATOM   695  H HG23 A VAL   A 1 24  ? 18.254 4.522   8.620   0.52 20.87 ?  24  VAL   A HG23 1 
ATOM   696  H HG23 B VAL   A 1 24  ? 17.870 4.174   8.139   0.48 19.37 ?  24  VAL   A HG23 1 
ATOM   697  N N    A GLU   A 1 25  ? 16.080 3.656   12.684  0.52 17.74 ?  25  GLU   A N    1 
ATOM   698  N N    B GLU   A 1 25  ? 15.962 3.334   12.240  0.48 16.79 ?  25  GLU   A N    1 
ATOM   699  C CA   A GLU   A 1 25  ? 15.494 3.590   14.018  0.52 19.28 ?  25  GLU   A CA   1 
ATOM   700  C CA   B GLU   A 1 25  ? 15.296 3.295   13.539  0.48 17.67 ?  25  GLU   A CA   1 
ATOM   701  C C    A GLU   A 1 25  ? 15.702 2.224   14.655  0.52 18.14 ?  25  GLU   A C    1 
ATOM   702  C C    B GLU   A 1 25  ? 15.578 1.986   14.263  0.48 17.55 ?  25  GLU   A C    1 
ATOM   703  O O    A GLU   A 1 25  ? 15.894 2.137   15.874  0.52 18.77 ?  25  GLU   A O    1 
ATOM   704  O O    B GLU   A 1 25  ? 15.786 1.978   15.482  0.48 18.66 ?  25  GLU   A O    1 
ATOM   705  C CB   A GLU   A 1 25  ? 14.011 3.966   13.963  0.52 21.50 ?  25  GLU   A CB   1 
ATOM   706  C CB   B GLU   A 1 25  ? 13.792 3.510   13.364  0.48 19.03 ?  25  GLU   A CB   1 
ATOM   707  C CG   A GLU   A 1 25  ? 13.773 5.439   13.652  0.52 24.06 ?  25  GLU   A CG   1 
ATOM   708  C CG   B GLU   A 1 25  ? 13.437 4.888   12.835  0.48 22.36 ?  25  GLU   A CG   1 
ATOM   709  C CD   A GLU   A 1 25  ? 14.588 6.373   14.536  0.52 26.29 ?  25  GLU   A CD   1 
ATOM   710  C CD   B GLU   A 1 25  ? 13.983 5.992   13.712  0.48 25.45 ?  25  GLU   A CD   1 
ATOM   711  O OE1  A GLU   A 1 25  ? 14.681 6.119   15.757  0.52 27.01 ?  25  GLU   A OE1  1 
ATOM   712  O OE1  B GLU   A 1 25  ? 13.961 5.823   14.950  0.48 26.81 ?  25  GLU   A OE1  1 
ATOM   713  O OE2  A GLU   A 1 25  ? 15.151 7.349   14.002  0.52 27.69 -1 25  GLU   A OE2  1 
ATOM   714  O OE2  B GLU   A 1 25  ? 14.443 7.018   13.169  0.48 26.37 -1 25  GLU   A OE2  1 
ATOM   715  H H    A GLU   A 1 25  ? 15.510 3.722   12.044  0.52 21.28 ?  25  GLU   A H    1 
ATOM   716  H H    B GLU   A 1 25  ? 15.428 3.319   11.565  0.48 20.15 ?  25  GLU   A H    1 
ATOM   717  H HA   A GLU   A 1 25  ? 15.945 4.231   14.584  0.52 23.13 ?  25  GLU   A HA   1 
ATOM   718  H HA   B GLU   A 1 25  ? 15.639 4.012   14.091  0.48 21.21 ?  25  GLU   A HA   1 
ATOM   719  H HB2  A GLU   A 1 25  ? 13.575 3.445   13.267  0.52 25.81 ?  25  GLU   A HB2  1 
ATOM   720  H HB2  B GLU   A 1 25  ? 13.449 2.857   12.735  0.48 22.84 ?  25  GLU   A HB2  1 
ATOM   721  H HB3  A GLU   A 1 25  ? 13.601 3.775   14.821  0.52 25.81 ?  25  GLU   A HB3  1 
ATOM   722  H HB3  B GLU   A 1 25  ? 13.355 3.402   14.224  0.48 22.84 ?  25  GLU   A HB3  1 
ATOM   723  H HG2  A GLU   A 1 25  ? 14.027 5.610   12.734  0.52 28.87 ?  25  GLU   A HG2  1 
ATOM   724  H HG2  B GLU   A 1 25  ? 13.805 4.992   11.945  0.48 26.83 ?  25  GLU   A HG2  1 
ATOM   725  H HG3  A GLU   A 1 25  ? 12.834 5.641   13.784  0.52 28.87 ?  25  GLU   A HG3  1 
ATOM   726  H HG3  B GLU   A 1 25  ? 12.474 4.986   12.814  0.48 26.83 ?  25  GLU   A HG3  1 
ATOM   727  N N    A GLU   A 1 26  ? 15.687 1.155   13.856  0.52 17.33 ?  26  GLU   A N    1 
ATOM   728  N N    B GLU   A 1 26  ? 15.595 0.871   13.531  0.48 17.44 ?  26  GLU   A N    1 
ATOM   729  C CA   A GLU   A 1 26  ? 16.000 -0.168  14.389  0.52 17.30 ?  26  GLU   A CA   1 
ATOM   730  C CA   B GLU   A 1 26  ? 15.969 -0.400  14.140  0.48 17.66 ?  26  GLU   A CA   1 
ATOM   731  C C    A GLU   A 1 26  ? 17.413 -0.203  14.964  0.52 16.71 ?  26  GLU   A C    1 
ATOM   732  C C    B GLU   A 1 26  ? 17.391 -0.349  14.682  0.48 16.74 ?  26  GLU   A C    1 
ATOM   733  O O    A GLU   A 1 26  ? 17.618 -0.631  16.106  0.52 16.74 ?  26  GLU   A O    1 
ATOM   734  O O    B GLU   A 1 26  ? 17.682 -0.930  15.734  0.48 17.08 ?  26  GLU   A O    1 
ATOM   735  C CB   A GLU   A 1 26  ? 15.847 -1.229  13.297  0.52 18.83 ?  26  GLU   A CB   1 
ATOM   736  C CB   B GLU   A 1 26  ? 15.822 -1.530  13.119  0.48 19.28 ?  26  GLU   A CB   1 
ATOM   737  C CG   A GLU   A 1 26  ? 14.442 -1.772  13.115  0.52 21.77 ?  26  GLU   A CG   1 
ATOM   738  C CG   B GLU   A 1 26  ? 14.385 -1.900  12.814  0.48 20.82 ?  26  GLU   A CG   1 
ATOM   739  C CD   A GLU   A 1 26  ? 13.966 -2.608  14.293  0.52 23.22 ?  26  GLU   A CD   1 
ATOM   740  C CD   B GLU   A 1 26  ? 13.664 -2.442  14.028  0.48 21.37 ?  26  GLU   A CD   1 
ATOM   741  O OE1  A GLU   A 1 26  ? 14.369 -3.788  14.416  0.52 23.53 ?  26  GLU   A OE1  1 
ATOM   742  O OE1  B GLU   A 1 26  ? 14.206 -3.362  14.680  0.48 22.07 ?  26  GLU   A OE1  1 
ATOM   743  O OE2  A GLU   A 1 26  ? 13.181 -2.078  15.099  0.52 24.12 -1 26  GLU   A OE2  1 
ATOM   744  O OE2  B GLU   A 1 26  ? 12.566 -1.937  14.335  0.48 20.56 -1 26  GLU   A OE2  1 
ATOM   745  H H    A GLU   A 1 26  ? 15.506 1.173   13.016  0.52 20.80 ?  26  GLU   A H    1 
ATOM   746  H H    B GLU   A 1 26  ? 15.393 0.823   12.698  0.48 20.93 ?  26  GLU   A H    1 
ATOM   747  H HA   A GLU   A 1 26  ? 15.380 -0.373  15.103  0.52 20.76 ?  26  GLU   A HA   1 
ATOM   748  H HA   B GLU   A 1 26  ? 15.376 -0.585  14.884  0.48 21.20 ?  26  GLU   A HA   1 
ATOM   749  H HB2  A GLU   A 1 26  ? 16.122 -0.842  12.452  0.52 22.60 ?  26  GLU   A HB2  1 
ATOM   750  H HB2  B GLU   A 1 26  ? 16.241 -1.256  12.287  0.48 23.13 ?  26  GLU   A HB2  1 
ATOM   751  H HB3  A GLU   A 1 26  ? 16.424 -1.976  13.517  0.52 22.60 ?  26  GLU   A HB3  1 
ATOM   752  H HB3  B GLU   A 1 26  ? 16.267 -2.322  13.463  0.48 23.13 ?  26  GLU   A HB3  1 
ATOM   753  H HG2  A GLU   A 1 26  ? 13.831 -1.027  13.005  0.52 26.12 ?  26  GLU   A HG2  1 
ATOM   754  H HG2  B GLU   A 1 26  ? 13.910 -1.111  12.513  0.48 24.98 ?  26  GLU   A HG2  1 
ATOM   755  H HG3  A GLU   A 1 26  ? 14.421 -2.337  12.328  0.52 26.12 ?  26  GLU   A HG3  1 
ATOM   756  H HG3  B GLU   A 1 26  ? 14.370 -2.584  12.127  0.48 24.98 ?  26  GLU   A HG3  1 
ATOM   757  N N    A ALA   A 1 27  ? 18.404 0.240   14.181  0.52 16.20 ?  27  ALA   A N    1 
ATOM   758  N N    B ALA   A 1 27  ? 18.293 0.344   13.983  0.48 15.02 ?  27  ALA   A N    1 
ATOM   759  C CA   A ALA   A 1 27  ? 19.789 0.176   14.638  0.52 16.31 ?  27  ALA   A CA   1 
ATOM   760  C CA   B ALA   A 1 27  ? 19.674 0.427   14.450  0.48 14.86 ?  27  ALA   A CA   1 
ATOM   761  C C    A ALA   A 1 27  ? 19.988 0.981   15.918  0.52 18.16 ?  27  ALA   A C    1 
ATOM   762  C C    B ALA   A 1 27  ? 19.775 1.270   15.716  0.48 15.73 ?  27  ALA   A C    1 
ATOM   763  O O    A ALA   A 1 27  ? 20.649 0.518   16.855  0.52 18.82 ?  27  ALA   A O    1 
ATOM   764  O O    B ALA   A 1 27  ? 20.434 0.876   16.685  0.48 16.07 ?  27  ALA   A O    1 
ATOM   765  C CB   A ALA   A 1 27  ? 20.739 0.660   13.538  0.52 15.61 ?  27  ALA   A CB   1 
ATOM   766  C CB   B ALA   A 1 27  ? 20.572 0.986   13.344  0.48 14.83 ?  27  ALA   A CB   1 
ATOM   767  H H    A ALA   A 1 27  ? 18.298 0.571   13.395  0.52 19.44 ?  27  ALA   A H    1 
ATOM   768  H H    B ALA   A 1 27  ? 18.129 0.767   13.249  0.48 18.03 ?  27  ALA   A H    1 
ATOM   769  H HA   A ALA   A 1 27  ? 20.012 -0.748  14.828  0.52 19.57 ?  27  ALA   A HA   1 
ATOM   770  H HA   B ALA   A 1 27  ? 19.984 -0.462  14.661  0.48 17.83 ?  27  ALA   A HA   1 
ATOM   771  H HB1  A ALA   A 1 27  ? 21.655 0.606   13.860  0.52 18.73 ?  27  ALA   A HB1  1 
ATOM   772  H HB1  B ALA   A 1 27  ? 21.484 1.027   13.669  0.48 17.80 ?  27  ALA   A HB1  1 
ATOM   773  H HB2  A ALA   A 1 27  ? 20.637 0.092   12.754  0.52 18.73 ?  27  ALA   A HB2  1 
ATOM   774  H HB2  B ALA   A 1 27  ? 20.522 0.403   12.570  0.48 17.80 ?  27  ALA   A HB2  1 
ATOM   775  H HB3  A ALA   A 1 27  ? 20.524 1.577   13.309  0.52 18.73 ?  27  ALA   A HB3  1 
ATOM   776  H HB3  B ALA   A 1 27  ? 20.267 1.877   13.104  0.48 17.80 ?  27  ALA   A HB3  1 
ATOM   777  N N    A LYS   A 1 28  ? 19.412 2.183   15.984  0.52 20.21 ?  28  LYS   A N    1 
ATOM   778  N N    B LYS   A 1 28  ? 19.110 2.429   15.736  0.48 17.13 ?  28  LYS   A N    1 
ATOM   779  C CA   A LYS   A 1 28  ? 19.566 3.000   17.184  0.52 23.24 ?  28  LYS   A CA   1 
ATOM   780  C CA   B LYS   A 1 28  ? 19.192 3.295   16.908  0.48 19.66 ?  28  LYS   A CA   1 
ATOM   781  C C    A LYS   A 1 28  ? 18.994 2.309   18.416  0.52 24.59 ?  28  LYS   A C    1 
ATOM   782  C C    B LYS   A 1 28  ? 18.612 2.634   18.150  0.48 20.85 ?  28  LYS   A C    1 
ATOM   783  O O    A LYS   A 1 28  ? 19.515 2.486   19.523  0.52 25.79 ?  28  LYS   A O    1 
ATOM   784  O O    B LYS   A 1 28  ? 19.089 2.883   19.263  0.48 21.69 ?  28  LYS   A O    1 
ATOM   785  C CB   A LYS   A 1 28  ? 18.934 4.378   16.980  0.52 25.91 ?  28  LYS   A CB   1 
ATOM   786  C CB   B LYS   A 1 28  ? 18.489 4.626   16.638  0.48 22.60 ?  28  LYS   A CB   1 
ATOM   787  C CG   A LYS   A 1 28  ? 19.775 5.309   16.123  0.52 28.54 ?  28  LYS   A CG   1 
ATOM   788  C CG   B LYS   A 1 28  ? 19.300 5.559   15.770  0.48 25.51 ?  28  LYS   A CG   1 
ATOM   789  C CD   A LYS   A 1 28  ? 19.278 6.741   16.181  0.52 31.09 ?  28  LYS   A CD   1 
ATOM   790  C CD   B LYS   A 1 28  ? 18.808 6.992   15.855  0.48 28.97 ?  28  LYS   A CD   1 
ATOM   791  C CE   A LYS   A 1 28  ? 17.983 6.911   15.412  0.52 32.67 ?  28  LYS   A CE   1 
ATOM   792  C CE   B LYS   A 1 28  ? 17.573 7.205   15.009  0.48 31.40 ?  28  LYS   A CE   1 
ATOM   793  N NZ   A LYS   A 1 28  ? 17.579 8.344   15.342  0.52 33.77 ?  28  LYS   A NZ   1 
ATOM   794  N NZ   B LYS   A 1 28  ? 17.221 8.650   14.923  0.48 32.56 ?  28  LYS   A NZ   1 
ATOM   795  H H    A LYS   A 1 28  ? 18.938 2.536   15.364  0.52 24.25 ?  28  LYS   A H    1 
ATOM   796  H H    B LYS   A 1 28  ? 18.616 2.732   15.098  0.48 20.55 ?  28  LYS   A H    1 
ATOM   797  H HA   A LYS   A 1 28  ? 20.510 3.134   17.350  0.52 27.88 ?  28  LYS   A HA   1 
ATOM   798  H HA   B LYS   A 1 28  ? 20.121 3.491   17.088  0.48 23.59 ?  28  LYS   A HA   1 
ATOM   799  H HB2  A LYS   A 1 28  ? 18.076 4.272   16.543  0.52 31.09 ?  28  LYS   A HB2  1 
ATOM   800  H HB2  B LYS   A 1 28  ? 17.647 4.459   16.185  0.48 27.12 ?  28  LYS   A HB2  1 
ATOM   801  H HB3  A LYS   A 1 28  ? 18.815 4.802   17.844  0.52 31.09 ?  28  LYS   A HB3  1 
ATOM   802  H HB3  B LYS   A 1 28  ? 18.323 5.076   17.483  0.48 27.12 ?  28  LYS   A HB3  1 
ATOM   803  H HG2  A LYS   A 1 28  ? 20.691 5.296   16.441  0.52 34.25 ?  28  LYS   A HG2  1 
ATOM   804  H HG2  B LYS   A 1 28  ? 20.224 5.539   16.061  0.48 30.62 ?  28  LYS   A HG2  1 
ATOM   805  H HG3  A LYS   A 1 28  ? 19.737 5.014   15.200  0.52 34.25 ?  28  LYS   A HG3  1 
ATOM   806  H HG3  B LYS   A 1 28  ? 19.231 5.271   14.847  0.48 30.62 ?  28  LYS   A HG3  1 
ATOM   807  H HD2  A LYS   A 1 28  ? 19.116 6.989   17.105  0.52 37.31 ?  28  LYS   A HD2  1 
ATOM   808  H HD2  B LYS   A 1 28  ? 18.588 7.202   16.777  0.48 34.76 ?  28  LYS   A HD2  1 
ATOM   809  H HD3  A LYS   A 1 28  ? 19.943 7.329   15.788  0.52 37.31 ?  28  LYS   A HD3  1 
ATOM   810  H HD3  B LYS   A 1 28  ? 19.505 7.586   15.535  0.48 34.76 ?  28  LYS   A HD3  1 
ATOM   811  H HE2  A LYS   A 1 28  ? 18.102 6.584   14.507  0.52 39.21 ?  28  LYS   A HE2  1 
ATOM   812  H HE2  B LYS   A 1 28  ? 17.740 6.878   14.111  0.48 37.68 ?  28  LYS   A HE2  1 
ATOM   813  H HE3  A LYS   A 1 28  ? 17.277 6.418   15.859  0.52 39.21 ?  28  LYS   A HE3  1 
ATOM   814  H HE3  B LYS   A 1 28  ? 16.826 6.731   15.407  0.48 37.68 ?  28  LYS   A HE3  1 
ATOM   815  H HZ1  A LYS   A 1 28  ? 16.818 8.424   14.886  0.52 40.52 ?  28  LYS   A HZ1  1 
ATOM   816  H HZ1  B LYS   A 1 28  ? 16.495 8.757   14.423  0.48 39.07 ?  28  LYS   A HZ1  1 
ATOM   817  H HZ2  A LYS   A 1 28  ? 17.461 8.668   16.162  0.52 40.52 ?  28  LYS   A HZ2  1 
ATOM   818  H HZ2  B LYS   A 1 28  ? 17.064 8.972   15.738  0.48 39.07 ?  28  LYS   A HZ2  1 
ATOM   819  H HZ3  A LYS   A 1 28  ? 18.211 8.819   14.932  0.52 40.52 ?  28  LYS   A HZ3  1 
ATOM   820  H HZ3  B LYS   A 1 28  ? 17.895 9.105   14.559  0.48 39.07 ?  28  LYS   A HZ3  1 
ATOM   821  N N    A LYS   A 1 29  ? 17.942 1.507   18.246  0.52 24.85 ?  29  LYS   A N    1 
ATOM   822  N N    B LYS   A 1 29  ? 17.585 1.801   17.989  0.48 21.32 ?  29  LYS   A N    1 
ATOM   823  C CA   A LYS   A 1 29  ? 17.339 0.813   19.380  0.52 26.23 ?  29  LYS   A CA   1 
ATOM   824  C CA   B LYS   A 1 29  ? 16.956 1.164   19.141  0.48 22.17 ?  29  LYS   A CA   1 
ATOM   825  C C    A LYS   A 1 29  ? 18.148 -0.421  19.771  0.52 25.67 ?  29  LYS   A C    1 
ATOM   826  C C    B LYS   A 1 29  ? 17.730 -0.062  19.601  0.48 20.93 ?  29  LYS   A C    1 
ATOM   827  O O    A LYS   A 1 29  ? 18.474 -0.615  20.948  0.52 27.26 ?  29  LYS   A O    1 
ATOM   828  O O    B LYS   A 1 29  ? 17.918 -0.258  20.806  0.48 21.53 ?  29  LYS   A O    1 
ATOM   829  C CB   A LYS   A 1 29  ? 15.901 0.415   19.038  0.52 28.47 ?  29  LYS   A CB   1 
ATOM   830  C CB   B LYS   A 1 29  ? 15.524 0.759   18.795  0.48 24.69 ?  29  LYS   A CB   1 
ATOM   831  C CG   A LYS   A 1 29  ? 15.161 -0.309  20.156  0.52 31.22 ?  29  LYS   A CG   1 
ATOM   832  C CG   B LYS   A 1 29  ? 14.781 0.059   19.926  0.48 27.72 ?  29  LYS   A CG   1 
ATOM   833  C CD   A LYS   A 1 29  ? 14.800 0.635   21.291  0.52 34.16 ?  29  LYS   A CD   1 
ATOM   834  C CD   B LYS   A 1 29  ? 14.527 1.003   21.088  0.48 30.78 ?  29  LYS   A CD   1 
ATOM   835  C CE   A LYS   A 1 29  ? 13.920 -0.054  22.325  0.52 36.05 ?  29  LYS   A CE   1 
ATOM   836  C CE   B LYS   A 1 29  ? 13.675 0.342   22.161  0.48 32.83 ?  29  LYS   A CE   1 
ATOM   837  N NZ   A LYS   A 1 29  ? 13.450 0.891   23.376  0.52 37.20 ?  29  LYS   A NZ   1 
ATOM   838  N NZ   B LYS   A 1 29  ? 13.415 1.264   23.298  0.48 34.12 ?  29  LYS   A NZ   1 
ATOM   839  H H    A LYS   A 1 29  ? 17.563 1.348   17.489  0.52 29.82 ?  29  LYS   A H    1 
ATOM   840  H H    B LYS   A 1 29  ? 17.235 1.594   17.233  0.48 25.59 ?  29  LYS   A H    1 
ATOM   841  H HA   A LYS   A 1 29  ? 17.309 1.414   20.141  0.52 31.47 ?  29  LYS   A HA   1 
ATOM   842  H HA   B LYS   A 1 29  ? 16.925 1.792   19.878  0.48 26.60 ?  29  LYS   A HA   1 
ATOM   843  H HB2  A LYS   A 1 29  ? 15.396 1.217   18.827  0.52 34.16 ?  29  LYS   A HB2  1 
ATOM   844  H HB2  B LYS   A 1 29  ? 15.024 1.555   18.567  0.48 29.63 ?  29  LYS   A HB2  1 
ATOM   845  H HB3  A LYS   A 1 29  ? 15.915 -0.173  18.268  0.52 34.16 ?  29  LYS   A HB3  1 
ATOM   846  H HB3  B LYS   A 1 29  ? 15.545 0.152   18.041  0.48 29.63 ?  29  LYS   A HB3  1 
ATOM   847  H HG2  A LYS   A 1 29  ? 14.340 -0.683  19.802  0.52 37.46 ?  29  LYS   A HG2  1 
ATOM   848  H HG2  B LYS   A 1 29  ? 13.924 -0.251  19.597  0.48 33.27 ?  29  LYS   A HG2  1 
ATOM   849  H HG3  A LYS   A 1 29  ? 15.720 -1.017  20.515  0.52 37.46 ?  29  LYS   A HG3  1 
ATOM   850  H HG3  B LYS   A 1 29  ? 15.303 -0.693  20.251  0.48 33.27 ?  29  LYS   A HG3  1 
ATOM   851  H HD2  A LYS   A 1 29  ? 15.611 0.934   21.732  0.52 40.99 ?  29  LYS   A HD2  1 
ATOM   852  H HD2  B LYS   A 1 29  ? 15.374 1.257   21.487  0.48 36.94 ?  29  LYS   A HD2  1 
ATOM   853  H HD3  A LYS   A 1 29  ? 14.313 1.395   20.933  0.52 40.99 ?  29  LYS   A HD3  1 
ATOM   854  H HD3  B LYS   A 1 29  ? 14.056 1.787   20.766  0.48 36.94 ?  29  LYS   A HD3  1 
ATOM   855  H HE2  A LYS   A 1 29  ? 13.140 -0.426  21.883  0.52 43.26 ?  29  LYS   A HE2  1 
ATOM   856  H HE2  B LYS   A 1 29  ? 12.823 0.082   21.777  0.48 39.40 ?  29  LYS   A HE2  1 
ATOM   857  H HE3  A LYS   A 1 29  ? 14.427 -0.759  22.757  0.52 43.26 ?  29  LYS   A HE3  1 
ATOM   858  H HE3  B LYS   A 1 29  ? 14.141 -0.439  22.502  0.48 39.40 ?  29  LYS   A HE3  1 
ATOM   859  H HZ1  A LYS   A 1 29  ? 12.939 0.462   23.965  0.52 44.64 ?  29  LYS   A HZ1  1 
ATOM   860  H HZ1  B LYS   A 1 29  ? 12.916 0.856   23.912  0.48 40.94 ?  29  LYS   A HZ1  1 
ATOM   861  H HZ2  A LYS   A 1 29  ? 14.148 1.243   23.801  0.52 44.64 ?  29  LYS   A HZ2  1 
ATOM   862  H HZ2  B LYS   A 1 29  ? 14.184 1.514   23.670  0.48 40.94 ?  29  LYS   A HZ2  1 
ATOM   863  H HZ3  A LYS   A 1 29  ? 12.976 1.547   23.005  0.52 44.64 ?  29  LYS   A HZ3  1 
ATOM   864  H HZ3  B LYS   A 1 29  ? 12.985 1.988   23.010  0.48 40.94 ?  29  LYS   A HZ3  1 
ATOM   865  N N    A VAL   A 1 30  ? 18.469 -1.271  18.797  0.52 24.15 ?  30  VAL   A N    1 
ATOM   866  N N    B VAL   A 1 30  ? 18.161 -0.902  18.661  0.48 19.87 ?  30  VAL   A N    1 
ATOM   867  C CA   A VAL   A 1 30  ? 19.125 -2.539  19.095  0.52 23.35 ?  30  VAL   A CA   1 
ATOM   868  C CA   B VAL   A 1 30  ? 18.797 -2.167  19.011  0.48 19.36 ?  30  VAL   A CA   1 
ATOM   869  C C    A VAL   A 1 30  ? 20.625 -2.364  19.310  0.52 21.94 ?  30  VAL   A C    1 
ATOM   870  C C    B VAL   A 1 30  ? 20.300 -2.014  19.230  0.48 18.67 ?  30  VAL   A C    1 
ATOM   871  O O    A VAL   A 1 30  ? 21.224 -3.079  20.122  0.52 23.00 ?  30  VAL   A O    1 
ATOM   872  O O    B VAL   A 1 30  ? 20.875 -2.708  20.074  0.48 19.63 ?  30  VAL   A O    1 
ATOM   873  C CB   A VAL   A 1 30  ? 18.834 -3.552  17.974  0.52 24.26 ?  30  VAL   A CB   1 
ATOM   874  C CB   B VAL   A 1 30  ? 18.497 -3.216  17.924  0.48 20.17 ?  30  VAL   A CB   1 
ATOM   875  C CG1  A VAL   A 1 30  ? 19.639 -4.830  18.179  0.52 24.28 ?  30  VAL   A CG1  1 
ATOM   876  C CG1  B VAL   A 1 30  ? 19.245 -4.514  18.203  0.48 20.69 ?  30  VAL   A CG1  1 
ATOM   877  C CG2  A VAL   A 1 30  ? 17.345 -3.858  17.906  0.52 25.11 ?  30  VAL   A CG2  1 
ATOM   878  C CG2  B VAL   A 1 30  ? 16.999 -3.466  17.826  0.48 20.47 ?  30  VAL   A CG2  1 
ATOM   879  H H    A VAL   A 1 30  ? 18.312 -1.138  17.965  0.52 28.99 ?  30  VAL   A H    1 
ATOM   880  H H    B VAL   A 1 30  ? 18.095 -0.763  17.811  0.48 23.84 ?  30  VAL   A H    1 
ATOM   881  H HA   A VAL   A 1 30  ? 18.746 -2.895  19.914  0.52 28.02 ?  30  VAL   A HA   1 
ATOM   882  H HA   B VAL   A 1 30  ? 18.402 -2.488  19.836  0.48 23.23 ?  30  VAL   A HA   1 
ATOM   883  H HB   A VAL   A 1 30  ? 19.102 -3.168  17.124  0.52 29.11 ?  30  VAL   A HB   1 
ATOM   884  H HB   B VAL   A 1 30  ? 18.801 -2.882  17.066  0.48 24.20 ?  30  VAL   A HB   1 
ATOM   885  H HG11 A VAL   A 1 30  ? 19.271 -5.526  17.611  0.52 29.14 ?  30  VAL   A HG11 1 
ATOM   886  H HG11 B VAL   A 1 30  ? 18.853 -5.227  17.672  0.48 24.83 ?  30  VAL   A HG11 1 
ATOM   887  H HG12 A VAL   A 1 30  ? 20.564 -4.667  17.943  0.52 29.14 ?  30  VAL   A HG12 1 
ATOM   888  H HG12 B VAL   A 1 30  ? 20.179 -4.403  17.962  0.48 24.83 ?  30  VAL   A HG12 1 
ATOM   889  H HG13 A VAL   A 1 30  ? 19.573 -5.098  19.109  0.52 29.14 ?  30  VAL   A HG13 1 
ATOM   890  H HG13 B VAL   A 1 30  ? 19.168 -4.726  19.145  0.48 24.83 ?  30  VAL   A HG13 1 
ATOM   891  H HG21 A VAL   A 1 30  ? 17.191 -4.519  17.214  0.52 30.13 ?  30  VAL   A HG21 1 
ATOM   892  H HG21 B VAL   A 1 30  ? 16.837 -4.161  17.168  0.48 24.56 ?  30  VAL   A HG21 1 
ATOM   893  H HG22 A VAL   A 1 30  ? 17.056 -4.203  18.765  0.52 30.13 ?  30  VAL   A HG22 1 
ATOM   894  H HG22 B VAL   A 1 30  ? 16.670 -3.751  18.693  0.48 24.56 ?  30  VAL   A HG22 1 
ATOM   895  H HG23 A VAL   A 1 30  ? 16.867 -3.041  17.697  0.52 30.13 ?  30  VAL   A HG23 1 
ATOM   896  H HG23 B VAL   A 1 30  ? 16.561 -2.646  17.557  0.48 24.56 ?  30  VAL   A HG23 1 
ATOM   897  N N    A LYS   A 1 31  ? 21.252 -1.430  18.602  0.52 20.36 ?  31  LYS   A N    1 
ATOM   898  N N    B LYS   A 1 31  ? 20.941 -1.112  18.495  0.48 18.66 ?  31  LYS   A N    1 
ATOM   899  C CA   A LYS   A 1 31  ? 22.705 -1.319  18.543  0.52 21.30 ?  31  LYS   A CA   1 
ATOM   900  C CA   B LYS   A 1 31  ? 22.394 -0.991  18.466  0.48 20.20 ?  31  LYS   A CA   1 
ATOM   901  C C    A LYS   A 1 31  ? 23.326 -2.680  18.215  0.52 18.55 ?  31  LYS   A C    1 
ATOM   902  C C    B LYS   A 1 31  ? 23.041 -2.358  18.225  0.48 18.14 ?  31  LYS   A C    1 
ATOM   903  O O    A LYS   A 1 31  ? 24.096 -3.227  19.012  0.52 18.35 ?  31  LYS   A O    1 
ATOM   904  O O    B LYS   A 1 31  ? 23.818 -2.840  19.055  0.48 19.17 ?  31  LYS   A O    1 
ATOM   905  C CB   A LYS   A 1 31  ? 23.288 -0.751  19.829  0.52 25.97 ?  31  LYS   A CB   1 
ATOM   906  C CB   B LYS   A 1 31  ? 22.938 -0.345  19.732  0.48 24.21 ?  31  LYS   A CB   1 
ATOM   907  C CG   A LYS   A 1 31  ? 22.612 0.522   20.314  0.52 30.66 ?  31  LYS   A CG   1 
ATOM   908  C CG   B LYS   A 1 31  ? 22.249 0.955   20.109  0.48 28.62 ?  31  LYS   A CG   1 
ATOM   909  C CD   A LYS   A 1 31  ? 23.629 1.565   20.758  0.52 34.26 ?  31  LYS   A CD   1 
ATOM   910  C CD   B LYS   A 1 31  ? 23.260 2.019   20.495  0.48 31.76 ?  31  LYS   A CD   1 
ATOM   911  C CE   A LYS   A 1 31  ? 22.996 2.612   21.665  0.52 36.84 ?  31  LYS   A CE   1 
ATOM   912  C CE   B LYS   A 1 31  ? 22.639 3.070   21.398  0.48 33.97 ?  31  LYS   A CE   1 
ATOM   913  N NZ   A LYS   A 1 31  ? 21.810 3.269   21.050  0.52 38.08 ?  31  LYS   A NZ   1 
ATOM   914  N NZ   B LYS   A 1 31  ? 21.316 3.533   20.900  0.48 35.37 ?  31  LYS   A NZ   1 
ATOM   915  H H    A LYS   A 1 31  ? 20.844 -0.837  18.133  0.52 24.43 ?  31  LYS   A H    1 
ATOM   916  H H    B LYS   A 1 31  ? 20.535 -0.538  17.995  0.48 22.39 ?  31  LYS   A H    1 
ATOM   917  H HA   A LYS   A 1 31  ? 22.932 -0.711  17.828  0.52 25.56 ?  31  LYS   A HA   1 
ATOM   918  H HA   B LYS   A 1 31  ? 22.626 -0.418  17.726  0.48 24.24 ?  31  LYS   A HA   1 
ATOM   919  H HB2  A LYS   A 1 31  ? 23.206 -1.418  20.526  0.52 31.17 ?  31  LYS   A HB2  1 
ATOM   920  H HB2  B LYS   A 1 31  ? 22.832 -0.959  20.472  0.48 29.05 ?  31  LYS   A HB2  1 
ATOM   921  H HB3  A LYS   A 1 31  ? 24.227 -0.548  19.680  0.52 31.17 ?  31  LYS   A HB3  1 
ATOM   922  H HB3  B LYS   A 1 31  ? 23.879 -0.151  19.595  0.48 29.05 ?  31  LYS   A HB3  1 
ATOM   923  H HG2  A LYS   A 1 31  ? 22.085 0.899   19.593  0.52 36.79 ?  31  LYS   A HG2  1 
ATOM   924  H HG2  B LYS   A 1 31  ? 21.737 1.282   19.353  0.48 34.34 ?  31  LYS   A HG2  1 
ATOM   925  H HG3  A LYS   A 1 31  ? 22.043 0.313   21.072  0.52 36.79 ?  31  LYS   A HG3  1 
ATOM   926  H HG3  B LYS   A 1 31  ? 21.665 0.801   20.869  0.48 34.34 ?  31  LYS   A HG3  1 
ATOM   927  H HD2  A LYS   A 1 31  ? 24.344 1.130   21.248  0.52 41.11 ?  31  LYS   A HD2  1 
ATOM   928  H HD2  B LYS   A 1 31  ? 23.997 1.604   20.971  0.48 38.11 ?  31  LYS   A HD2  1 
ATOM   929  H HD3  A LYS   A 1 31  ? 23.986 2.017   19.976  0.52 41.11 ?  31  LYS   A HD3  1 
ATOM   930  H HD3  B LYS   A 1 31  ? 23.584 2.458   19.692  0.48 38.11 ?  31  LYS   A HD3  1 
ATOM   931  H HE2  A LYS   A 1 31  ? 22.709 2.184   22.487  0.52 44.21 ?  31  LYS   A HE2  1 
ATOM   932  H HE2  B LYS   A 1 31  ? 22.519 2.692   22.283  0.48 40.76 ?  31  LYS   A HE2  1 
ATOM   933  H HE3  A LYS   A 1 31  ? 23.652 3.300   21.860  0.52 44.21 ?  31  LYS   A HE3  1 
ATOM   934  H HE3  B LYS   A 1 31  ? 23.231 3.836   21.444  0.48 40.76 ?  31  LYS   A HE3  1 
ATOM   935  H HZ1  A LYS   A 1 31  ? 21.481 3.884   21.604  0.52 45.70 ?  31  LYS   A HZ1  1 
ATOM   936  H HZ1  B LYS   A 1 31  ? 21.023 4.206   21.401  0.48 42.44 ?  31  LYS   A HZ1  1 
ATOM   937  H HZ2  A LYS   A 1 31  ? 22.041 3.662   20.286  0.52 45.70 ?  31  LYS   A HZ2  1 
ATOM   938  H HZ2  B LYS   A 1 31  ? 21.390 3.809   20.057  0.48 42.44 ?  31  LYS   A HZ2  1 
ATOM   939  H HZ3  A LYS   A 1 31  ? 21.178 2.664   20.884  0.52 45.70 ?  31  LYS   A HZ3  1 
ATOM   940  H HZ3  B LYS   A 1 31  ? 20.727 2.867   20.935  0.48 42.44 ?  31  LYS   A HZ3  1 
ATOM   941  N N    A PRO   A 1 32  ? 23.011 -3.245  17.052  0.52 17.10 ?  32  PRO   A N    1 
ATOM   942  N N    B PRO   A 1 32  ? 22.745 -2.994  17.095  0.48 16.74 ?  32  PRO   A N    1 
ATOM   943  C CA   A PRO   A 1 32  ? 23.485 -4.593  16.729  0.52 16.75 ?  32  PRO   A CA   1 
ATOM   944  C CA   B PRO   A 1 32  ? 23.238 -4.351  16.857  0.48 16.30 ?  32  PRO   A CA   1 
ATOM   945  C C    A PRO   A 1 32  ? 24.987 -4.627  16.506  0.52 16.61 ?  32  PRO   A C    1 
ATOM   946  C C    B PRO   A 1 32  ? 24.745 -4.362  16.664  0.48 16.25 ?  32  PRO   A C    1 
ATOM   947  O O    A PRO   A 1 32  ? 25.640 -3.606  16.287  0.52 16.15 ?  32  PRO   A O    1 
ATOM   948  O O    B PRO   A 1 32  ? 25.400 -3.330  16.502  0.48 16.17 ?  32  PRO   A O    1 
ATOM   949  C CB   A PRO   A 1 32  ? 22.747 -4.912  15.426  0.52 17.74 ?  32  PRO   A CB   1 
ATOM   950  C CB   B PRO   A 1 32  ? 22.521 -4.744  15.564  0.48 16.82 ?  32  PRO   A CB   1 
ATOM   951  C CG   A PRO   A 1 32  ? 22.568 -3.575  14.782  0.52 17.73 ?  32  PRO   A CG   1 
ATOM   952  C CG   B PRO   A 1 32  ? 22.365 -3.451  14.835  0.48 17.14 ?  32  PRO   A CG   1 
ATOM   953  C CD   A PRO   A 1 32  ? 22.281 -2.639  15.925  0.52 16.84 ?  32  PRO   A CD   1 
ATOM   954  C CD   B PRO   A 1 32  ? 22.053 -2.448  15.913  0.48 16.62 ?  32  PRO   A CD   1 
ATOM   955  H HA   A PRO   A 1 32  ? 23.230 -5.227  17.419  0.52 20.10 ?  32  PRO   A HA   1 
ATOM   956  H HA   B PRO   A 1 32  ? 22.980 -4.945  17.578  0.48 19.56 ?  32  PRO   A HA   1 
ATOM   957  H HB2  A PRO   A 1 32  ? 23.291 -5.495  14.872  0.52 21.29 ?  32  PRO   A HB2  1 
ATOM   958  H HB2  B PRO   A 1 32  ? 23.070 -5.364  15.059  0.48 20.19 ?  32  PRO   A HB2  1 
ATOM   959  H HB3  A PRO   A 1 32  ? 21.890 -5.323  15.622  0.52 21.29 ?  32  PRO   A HB3  1 
ATOM   960  H HB3  B PRO   A 1 32  ? 21.656 -5.135  15.768  0.48 20.19 ?  32  PRO   A HB3  1 
ATOM   961  H HG2  A PRO   A 1 32  ? 23.383 -3.324  14.322  0.52 21.28 ?  32  PRO   A HG2  1 
ATOM   962  H HG2  B PRO   A 1 32  ? 23.193 -3.230  14.383  0.48 20.57 ?  32  PRO   A HG2  1 
ATOM   963  H HG3  A PRO   A 1 32  ? 21.820 -3.611  14.164  0.52 21.28 ?  32  PRO   A HG3  1 
ATOM   964  H HG3  B PRO   A 1 32  ? 21.633 -3.522  14.200  0.48 20.57 ?  32  PRO   A HG3  1 
ATOM   965  H HD2  A PRO   A 1 32  ? 22.625 -1.755  15.724  0.52 20.21 ?  32  PRO   A HD2  1 
ATOM   966  H HD2  B PRO   A 1 32  ? 22.410 -1.580  15.672  0.48 19.94 ?  32  PRO   A HD2  1 
ATOM   967  H HD3  A PRO   A 1 32  ? 21.328 -2.618  16.108  0.52 20.21 ?  32  PRO   A HD3  1 
ATOM   968  H HD3  B PRO   A 1 32  ? 21.094 -2.408  16.063  0.48 19.94 ?  32  PRO   A HD3  1 
ATOM   969  N N    A THR   A 1 33  ? 25.530 -5.844  16.534  0.52 17.04 ?  33  THR   A N    1 
ATOM   970  N N    B THR   A 1 33  ? 25.290 -5.577  16.664  0.48 16.15 ?  33  THR   A N    1 
ATOM   971  C CA   A THR   A 1 33  ? 26.942 -6.016  16.221  0.52 16.77 ?  33  THR   A CA   1 
ATOM   972  C CA   B THR   A 1 33  ? 26.710 -5.750  16.389  0.48 15.86 ?  33  THR   A CA   1 
ATOM   973  C C    A THR   A 1 33  ? 27.248 -5.566  14.796  0.52 15.28 ?  33  THR   A C    1 
ATOM   974  C C    B THR   A 1 33  ? 27.049 -5.302  14.975  0.48 14.68 ?  33  THR   A C    1 
ATOM   975  O O    A THR   A 1 33  ? 28.314 -4.992  14.540  0.52 15.57 ?  33  THR   A O    1 
ATOM   976  O O    B THR   A 1 33  ? 28.045 -4.602  14.756  0.48 14.62 ?  33  THR   A O    1 
ATOM   977  C CB   A THR   A 1 33  ? 27.355 -7.475  16.436  0.52 19.02 ?  33  THR   A CB   1 
ATOM   978  C CB   B THR   A 1 33  ? 27.095 -7.214  16.586  0.48 17.90 ?  33  THR   A CB   1 
ATOM   979  O OG1  A THR   A 1 33  ? 27.111 -7.851  17.797  0.52 20.67 ?  33  THR   A OG1  1 
ATOM   980  O OG1  B THR   A 1 33  ? 26.755 -7.620  17.917  0.48 19.63 ?  33  THR   A OG1  1 
ATOM   981  C CG2  A THR   A 1 33  ? 28.831 -7.669  16.140  0.52 20.05 ?  33  THR   A CG2  1 
ATOM   982  C CG2  B THR   A 1 33  ? 28.588 -7.408  16.361  0.48 18.94 ?  33  THR   A CG2  1 
ATOM   983  H H    A THR   A 1 33  ? 25.108 -6.569  16.721  0.52 20.45 ?  33  THR   A H    1 
ATOM   984  H H    B THR   A 1 33  ? 24.862 -6.306  16.812  0.48 19.38 ?  33  THR   A H    1 
ATOM   985  H HA   A THR   A 1 33  ? 27.465 -5.467  16.823  0.52 20.13 ?  33  THR   A HA   1 
ATOM   986  H HA   B THR   A 1 33  ? 27.223 -5.210  17.007  0.48 19.03 ?  33  THR   A HA   1 
ATOM   987  H HB   A THR   A 1 33  ? 26.837 -8.048  15.846  0.52 22.82 ?  33  THR   A HB   1 
ATOM   988  H HB   B THR   A 1 33  ? 26.612 -7.764  15.944  0.48 21.48 ?  33  THR   A HB   1 
ATOM   989  H HG1  A THR   A 1 33  ? 27.540 -7.347  18.316  0.52 24.80 ?  33  THR   A HG1  1 
ATOM   990  H HG1  B THR   A 1 33  ? 27.175 -7.146  18.470  0.48 23.56 ?  33  THR   A HG1  1 
ATOM   991  H HG21 A THR   A 1 33  ? 29.114 -8.544  16.448  0.52 24.06 ?  33  THR   A HG21 1 
ATOM   992  H HG21 B THR   A 1 33  ? 28.852 -8.295  16.646  0.48 22.72 ?  33  THR   A HG21 1 
ATOM   993  H HG22 A THR   A 1 33  ? 28.991 -7.603  15.187  0.52 24.06 ?  33  THR   A HG22 1 
ATOM   994  H HG22 B THR   A 1 33  ? 28.802 -7.306  15.418  0.48 22.72 ?  33  THR   A HG22 1 
ATOM   995  H HG23 A THR   A 1 33  ? 29.350 -6.991  16.599  0.52 24.06 ?  33  THR   A HG23 1 
ATOM   996  H HG23 B THR   A 1 33  ? 29.087 -6.750  16.869  0.48 22.72 ?  33  THR   A HG23 1 
ATOM   997  N N    A VAL   A 1 34  ? 26.326 -5.807  13.859  0.52 13.55 ?  34  VAL   A N    1 
ATOM   998  N N    B VAL   A 1 34  ? 26.232 -5.702  14.001  0.48 13.70 ?  34  VAL   A N    1 
ATOM   999  C CA   A VAL   A 1 34  ? 26.526 -5.470  12.450  0.52 13.29 ?  34  VAL   A CA   1 
ATOM   1000 C CA   B VAL   A 1 34  ? 26.455 -5.387  12.596  0.48 13.60 ?  34  VAL   A CA   1 
ATOM   1001 C C    A VAL   A 1 34  ? 25.228 -4.920  11.867  0.52 12.93 ?  34  VAL   A C    1 
ATOM   1002 C C    B VAL   A 1 34  ? 25.166 -4.838  12.006  0.48 13.45 ?  34  VAL   A C    1 
ATOM   1003 O O    A VAL   A 1 34  ? 24.207 -5.619  11.859  0.52 12.91 ?  34  VAL   A O    1 
ATOM   1004 O O    B VAL   A 1 34  ? 24.098 -5.445  12.152  0.48 14.29 ?  34  VAL   A O    1 
ATOM   1005 C CB   A VAL   A 1 34  ? 26.986 -6.682  11.616  0.52 13.25 ?  34  VAL   A CB   1 
ATOM   1006 C CB   B VAL   A 1 34  ? 26.924 -6.613  11.786  0.48 14.87 ?  34  VAL   A CB   1 
ATOM   1007 C CG1  A VAL   A 1 34  ? 27.153 -6.287  10.156  0.52 13.98 ?  34  VAL   A CG1  1 
ATOM   1008 C CG1  B VAL   A 1 34  ? 27.178 -6.227  10.330  0.48 15.53 ?  34  VAL   A CG1  1 
ATOM   1009 C CG2  A VAL   A 1 34  ? 28.277 -7.283  12.167  0.52 15.21 ?  34  VAL   A CG2  1 
ATOM   1010 C CG2  B VAL   A 1 34  ? 28.168 -7.231  12.408  0.48 16.32 ?  34  VAL   A CG2  1 
ATOM   1011 H H    A VAL   A 1 34  ? 25.565 -6.182  14.020  0.52 16.27 ?  34  VAL   A H    1 
ATOM   1012 H H    B VAL   A 1 34  ? 25.519 -6.165  14.135  0.48 16.44 ?  34  VAL   A H    1 
ATOM   1013 H HA   A VAL   A 1 34  ? 27.207 -4.783  12.383  0.52 15.95 ?  34  VAL   A HA   1 
ATOM   1014 H HA   B VAL   A 1 34  ? 27.133 -4.699  12.519  0.48 16.32 ?  34  VAL   A HA   1 
ATOM   1015 H HB   A VAL   A 1 34  ? 26.305 -7.370  11.665  0.52 15.89 ?  34  VAL   A HB   1 
ATOM   1016 H HB   B VAL   A 1 34  ? 26.226 -7.284  11.795  0.48 17.84 ?  34  VAL   A HB   1 
ATOM   1017 H HG11 A VAL   A 1 34  ? 27.676 -6.968  9.704   0.52 16.77 ?  34  VAL   A HG11 1 
ATOM   1018 H HG11 B VAL   A 1 34  ? 27.659 -6.948  9.890   0.48 18.64 ?  34  VAL   A HG11 1 
ATOM   1019 H HG12 A VAL   A 1 34  ? 26.280 -6.214  9.746   0.52 16.77 ?  34  VAL   A HG12 1 
ATOM   1020 H HG12 B VAL   A 1 34  ? 26.330 -6.079  9.885   0.48 18.64 ?  34  VAL   A HG12 1 
ATOM   1021 H HG13 A VAL   A 1 34  ? 27.617 -5.435  10.113  0.52 16.77 ?  34  VAL   A HG13 1 
ATOM   1022 H HG13 B VAL   A 1 34  ? 27.713 -5.417  10.305  0.48 18.64 ?  34  VAL   A HG13 1 
ATOM   1023 H HG21 A VAL   A 1 34  ? 28.563 -8.010  11.587  0.52 18.26 ?  34  VAL   A HG21 1 
ATOM   1024 H HG21 B VAL   A 1 34  ? 28.480 -7.957  11.843  0.48 19.59 ?  34  VAL   A HG21 1 
ATOM   1025 H HG22 A VAL   A 1 34  ? 28.963 -6.597  12.194  0.52 18.26 ?  34  VAL   A HG22 1 
ATOM   1026 H HG22 B VAL   A 1 34  ? 28.858 -6.552  12.481  0.48 19.59 ?  34  VAL   A HG22 1 
ATOM   1027 H HG23 A VAL   A 1 34  ? 28.117 -7.624  13.062  0.52 18.26 ?  34  VAL   A HG23 1 
ATOM   1028 H HG23 B VAL   A 1 34  ? 27.946 -7.571  13.288  0.48 19.59 ?  34  VAL   A HG23 1 
ATOM   1029 N N    . VAL   A 1 35  ? 25.270 -3.686  11.353  1.00 12.90 ?  35  VAL   A N    1 
ATOM   1030 C CA   . VAL   A 1 35  ? 24.232 -3.163  10.468  1.00 12.33 ?  35  VAL   A CA   1 
ATOM   1031 C C    . VAL   A 1 35  ? 24.786 -3.168  9.050   1.00 11.80 ?  35  VAL   A C    1 
ATOM   1032 O O    . VAL   A 1 35  ? 25.937 -2.773  8.829   1.00 12.43 ?  35  VAL   A O    1 
ATOM   1033 C CB   . VAL   A 1 35  ? 23.720 -1.767  10.879  1.00 12.99 ?  35  VAL   A CB   1 
ATOM   1034 C CG1  . VAL   A 1 35  ? 24.795 -0.685  10.745  1.00 13.86 ?  35  VAL   A CG1  1 
ATOM   1035 C CG2  . VAL   A 1 35  ? 22.487 -1.395  10.051  1.00 13.61 ?  35  VAL   A CG2  1 
ATOM   1036 H H    A VAL   A 1 35  ? 25.903 -3.124  11.501  0.52 15.48 ?  35  VAL   A H    1 
ATOM   1037 H H    B VAL   A 1 35  ? 25.953 -3.168  11.409  0.48 15.48 ?  35  VAL   A H    1 
ATOM   1038 H HA   . VAL   A 1 35  ? 23.471 -3.766  10.494  1.00 14.80 ?  35  VAL   A HA   1 
ATOM   1039 H HB   . VAL   A 1 35  ? 23.442 -1.792  11.804  1.00 15.59 ?  35  VAL   A HB   1 
ATOM   1040 H HG11 . VAL   A 1 35  ? 24.457 0.147   11.113  1.00 16.63 ?  35  VAL   A HG11 1 
ATOM   1041 H HG12 . VAL   A 1 35  ? 25.583 -0.966  11.232  1.00 16.63 ?  35  VAL   A HG12 1 
ATOM   1042 H HG13 . VAL   A 1 35  ? 25.013 -0.563  9.805   1.00 16.63 ?  35  VAL   A HG13 1 
ATOM   1043 H HG21 . VAL   A 1 35  ? 22.143 -0.542  10.360  1.00 16.33 ?  35  VAL   A HG21 1 
ATOM   1044 H HG22 . VAL   A 1 35  ? 22.739 -1.327  9.115   1.00 16.33 ?  35  VAL   A HG22 1 
ATOM   1045 H HG23 . VAL   A 1 35  ? 21.812 -2.083  10.161  1.00 16.33 ?  35  VAL   A HG23 1 
ATOM   1046 N N    . VAL   A 1 36  ? 23.983 -3.635  8.093   1.00 11.64 ?  36  VAL   A N    1 
ATOM   1047 C CA   . VAL   A 1 36  ? 24.375 -3.651  6.687   1.00 10.71 ?  36  VAL   A CA   1 
ATOM   1048 C C    . VAL   A 1 36  ? 23.929 -2.362  6.014   1.00 11.67 ?  36  VAL   A C    1 
ATOM   1049 O O    . VAL   A 1 36  ? 22.772 -1.955  6.142   1.00 11.93 ?  36  VAL   A O    1 
ATOM   1050 C CB   . VAL   A 1 36  ? 23.778 -4.874  5.965   1.00 11.26 ?  36  VAL   A CB   1 
ATOM   1051 C CG1  . VAL   A 1 36  ? 24.068 -4.806  4.477   1.00 11.79 ?  36  VAL   A CG1  1 
ATOM   1052 C CG2  . VAL   A 1 36  ? 24.320 -6.159  6.566   1.00 12.72 ?  36  VAL   A CG2  1 
ATOM   1053 H H    . VAL   A 1 36  ? 23.187 -3.943  8.238   1.00 13.97 ?  36  VAL   A H    1 
ATOM   1054 H HA   . VAL   A 1 36  ? 25.341 -3.713  6.630   1.00 12.85 ?  36  VAL   A HA   1 
ATOM   1055 H HB   . VAL   A 1 36  ? 22.812 -4.871  6.088   1.00 13.51 ?  36  VAL   A HB   1 
ATOM   1056 H HG11 . VAL   A 1 36  ? 23.930 -5.682  4.091   1.00 14.15 ?  36  VAL   A HG11 1 
ATOM   1057 H HG12 . VAL   A 1 36  ? 23.467 -4.164  4.067   1.00 14.15 ?  36  VAL   A HG12 1 
ATOM   1058 H HG13 . VAL   A 1 36  ? 24.988 -4.528  4.352   1.00 14.15 ?  36  VAL   A HG13 1 
ATOM   1059 H HG21 . VAL   A 1 36  ? 23.942 -6.917  6.088   1.00 15.27 ?  36  VAL   A HG21 1 
ATOM   1060 H HG22 . VAL   A 1 36  ? 25.285 -6.166  6.483   1.00 15.27 ?  36  VAL   A HG22 1 
ATOM   1061 H HG23 . VAL   A 1 36  ? 24.069 -6.208  7.504   1.00 15.27 ?  36  VAL   A HG23 1 
ATOM   1062 N N    . ASN   A 1 37  ? 24.844 -1.730  5.289   1.00 10.88 ?  37  ASN   A N    1 
ATOM   1063 C CA   . ASN   A 1 37  ? 24.518 -0.620  4.405   1.00 10.51 ?  37  ASN   A CA   1 
ATOM   1064 C C    . ASN   A 1 37  ? 24.394 -1.100  2.966   1.00 10.80 ?  37  ASN   A C    1 
ATOM   1065 O O    . ASN   A 1 37  ? 25.184 -1.930  2.498   1.00 11.21 ?  37  ASN   A O    1 
ATOM   1066 C CB   . ASN   A 1 37  ? 25.599 0.462   4.485   1.00 10.88 ?  37  ASN   A CB   1 
ATOM   1067 C CG   . ASN   A 1 37  ? 25.270 1.662   3.636   1.00 11.34 ?  37  ASN   A CG   1 
ATOM   1068 O OD1  . ASN   A 1 37  ? 24.085 1.992   3.443   1.00 12.19 ?  37  ASN   A OD1  1 
ATOM   1069 N ND2  . ASN   A 1 37  ? 26.301 2.329   3.122   1.00 11.56 ?  37  ASN   A ND2  1 
ATOM   1070 H H    . ASN   A 1 37  ? 25.685 -1.931  5.291   1.00 13.06 ?  37  ASN   A H    1 
ATOM   1071 H HA   . ASN   A 1 37  ? 23.679 -0.224  4.677   1.00 12.62 ?  37  ASN   A HA   1 
ATOM   1072 H HB2  . ASN   A 1 37  ? 25.689 0.761   5.406   1.00 13.05 ?  37  ASN   A HB2  1 
ATOM   1073 H HB3  . ASN   A 1 37  ? 26.447 0.095   4.177   1.00 13.05 ?  37  ASN   A HB3  1 
ATOM   1074 H HD21 . ASN   A 1 37  ? 26.165 3.024   2.629   1.00 13.88 ?  37  ASN   A HD21 1 
ATOM   1075 H HD22 . ASN   A 1 37  ? 27.105 2.075   3.274   1.00 13.88 ?  37  ASN   A HD22 1 
ATOM   1076 N N    A ALA   A 1 38  ? 23.382 -0.563  2.281   0.52 11.00 ?  38  ALA   A N    1 
ATOM   1077 N N    B ALA   A 1 38  ? 23.386 -0.594  2.258   0.48 11.19 ?  38  ALA   A N    1 
ATOM   1078 C CA   A ALA   A 1 38  ? 23.197 -0.696  0.837   0.52 10.68 ?  38  ALA   A CA   1 
ATOM   1079 C CA   B ALA   A 1 38  ? 23.249 -0.863  0.825   0.48 11.50 ?  38  ALA   A CA   1 
ATOM   1080 C C    A ALA   A 1 38  ? 24.118 0.309   0.150   0.52 11.20 ?  38  ALA   A C    1 
ATOM   1081 C C    B ALA   A 1 38  ? 24.033 0.203   0.065   0.48 11.80 ?  38  ALA   A C    1 
ATOM   1082 O O    A ALA   A 1 38  ? 23.733 1.429   -0.202  0.52 10.39 ?  38  ALA   A O    1 
ATOM   1083 O O    B ALA   A 1 38  ? 23.500 1.215   -0.400  0.48 11.50 ?  38  ALA   A O    1 
ATOM   1084 C CB   A ALA   A 1 38  ? 21.734 -0.455  0.472   0.52 11.93 ?  38  ALA   A CB   1 
ATOM   1085 C CB   B ALA   A 1 38  ? 21.781 -0.893  0.416   0.48 12.83 ?  38  ALA   A CB   1 
ATOM   1086 H H    A ALA   A 1 38  ? 22.770 -0.086  2.651   0.52 13.20 ?  38  ALA   A H    1 
ATOM   1087 H H    B ALA   A 1 38  ? 22.773 -0.086  2.584   0.48 13.43 ?  38  ALA   A H    1 
ATOM   1088 H HA   A ALA   A 1 38  ? 23.446 -1.588  0.556   0.52 12.82 ?  38  ALA   A HA   1 
ATOM   1089 H HA   B ALA   A 1 38  ? 23.641 -1.729  0.626   0.48 13.80 ?  38  ALA   A HA   1 
ATOM   1090 H HB1  A ALA   A 1 38  ? 21.626 -0.553  -0.486  0.52 14.31 ?  38  ALA   A HB1  1 
ATOM   1091 H HB1  B ALA   A 1 38  ? 21.731 -1.034  -0.543  0.48 15.39 ?  38  ALA   A HB1  1 
ATOM   1092 H HB2  A ALA   A 1 38  ? 21.183 -1.106  0.936   0.52 14.31 ?  38  ALA   A HB2  1 
ATOM   1093 H HB2  B ALA   A 1 38  ? 21.337 -1.616  0.882   0.48 15.39 ?  38  ALA   A HB2  1 
ATOM   1094 H HB3  A ALA   A 1 38  ? 21.483 0.442   0.744   0.52 14.31 ?  38  ALA   A HB3  1 
ATOM   1095 H HB3  B ALA   A 1 38  ? 21.375 -0.045  0.645   0.48 15.39 ?  38  ALA   A HB3  1 
ATOM   1096 N N    A ALA   A 1 39  ? 25.369 -0.106  -0.029  0.52 11.18 ?  39  ALA   A N    1 
ATOM   1097 N N    B ALA   A 1 39  ? 25.338 -0.036  -0.054  0.48 12.15 ?  39  ALA   A N    1 
ATOM   1098 C CA   A ALA   A 1 39  ? 26.451 0.758   -0.478  0.52 9.96  ?  39  ALA   A CA   1 
ATOM   1099 C CA   B ALA   A 1 39  ? 26.270 0.949   -0.578  0.48 11.96 ?  39  ALA   A CA   1 
ATOM   1100 C C    A ALA   A 1 39  ? 26.618 0.723   -1.995  0.52 10.18 ?  39  ALA   A C    1 
ATOM   1101 C C    B ALA   A 1 39  ? 26.397 0.841   -2.095  0.48 11.50 ?  39  ALA   A C    1 
ATOM   1102 O O    A ALA   A 1 39  ? 26.159 -0.193  -2.682  0.52 10.76 ?  39  ALA   A O    1 
ATOM   1103 O O    B ALA   A 1 39  ? 25.911 -0.099  -2.728  0.48 12.48 ?  39  ALA   A O    1 
ATOM   1104 C CB   A ALA   A 1 39  ? 27.764 0.327   0.183   0.52 9.79  ?  39  ALA   A CB   1 
ATOM   1105 C CB   B ALA   A 1 39  ? 27.643 0.770   0.076   0.48 13.06 ?  39  ALA   A CB   1 
ATOM   1106 H H    A ALA   A 1 39  ? 25.624 -0.917  0.108   0.52 13.42 ?  39  ALA   A H    1 
ATOM   1107 H H    B ALA   A 1 39  ? 25.716 -0.785  0.153   0.48 14.58 ?  39  ALA   A H    1 
ATOM   1108 H HA   A ALA   A 1 39  ? 26.264 1.672   -0.210  0.52 11.95 ?  39  ALA   A HA   1 
ATOM   1109 H HA   B ALA   A 1 39  ? 25.947 1.837   -0.365  0.48 14.35 ?  39  ALA   A HA   1 
ATOM   1110 H HB1  A ALA   A 1 39  ? 28.478 0.914   -0.122  0.52 11.75 ?  39  ALA   A HB1  1 
ATOM   1111 H HB1  B ALA   A 1 39  ? 28.253 1.436   -0.282  0.48 15.67 ?  39  ALA   A HB1  1 
ATOM   1112 H HB2  A ALA   A 1 39  ? 27.672 0.400   1.147   0.52 11.75 ?  39  ALA   A HB2  1 
ATOM   1113 H HB2  B ALA   A 1 39  ? 27.553 0.888   1.036   0.48 15.67 ?  39  ALA   A HB2  1 
ATOM   1114 H HB3  A ALA   A 1 39  ? 27.959 -0.586  -0.065  0.52 11.75 ?  39  ALA   A HB3  1 
ATOM   1115 H HB3  B ALA   A 1 39  ? 27.974 -0.120  -0.118  0.48 15.67 ?  39  ALA   A HB3  1 
ATOM   1116 N N    A ASN   A 1 40  ? 27.309 1.739   -2.514  0.52 10.96 ?  40  ASN   A N    1 
ATOM   1117 N N    B ASN   A 1 40  ? 27.050 1.841   -2.682  0.48 10.81 ?  40  ASN   A N    1 
ATOM   1118 C CA   A ASN   A 1 40  ? 27.873 1.709   -3.859  0.52 11.67 ?  40  ASN   A CA   1 
ATOM   1119 C CA   B ASN   A 1 40  ? 27.580 1.756   -4.035  0.48 10.81 ?  40  ASN   A CA   1 
ATOM   1120 C C    A ASN   A 1 40  ? 29.396 1.598   -3.769  0.52 10.68 ?  40  ASN   A C    1 
ATOM   1121 C C    B ASN   A 1 40  ? 29.098 1.609   -3.967  0.48 10.73 ?  40  ASN   A C    1 
ATOM   1122 O O    A ASN   A 1 40  ? 29.986 1.722   -2.693  0.52 10.93 ?  40  ASN   A O    1 
ATOM   1123 O O    B ASN   A 1 40  ? 29.704 1.682   -2.895  0.48 10.99 ?  40  ASN   A O    1 
ATOM   1124 C CB   A ASN   A 1 40  ? 27.412 2.909   -4.708  0.52 12.82 ?  40  ASN   A CB   1 
ATOM   1125 C CB   B ASN   A 1 40  ? 27.164 2.968   -4.882  0.48 10.85 ?  40  ASN   A CB   1 
ATOM   1126 C CG   A ASN   A 1 40  ? 27.786 4.249   -4.104  0.52 14.12 ?  40  ASN   A CG   1 
ATOM   1127 C CG   B ASN   A 1 40  ? 27.534 4.290   -4.241  0.48 11.21 ?  40  ASN   A CG   1 
ATOM   1128 O OD1  A ASN   A 1 40  ? 28.943 4.484   -3.753  0.52 13.68 ?  40  ASN   A OD1  1 
ATOM   1129 O OD1  B ASN   A 1 40  ? 28.709 4.575   -4.017  0.48 11.24 ?  40  ASN   A OD1  1 
ATOM   1130 N ND2  A ASN   A 1 40  ? 26.799 5.143   -3.988  0.52 15.02 ?  40  ASN   A ND2  1 
ATOM   1131 N ND2  B ASN   A 1 40  ? 26.528 5.108   -3.950  0.48 12.13 ?  40  ASN   A ND2  1 
ATOM   1132 H H    A ASN   A 1 40  ? 27.468 2.477   -2.094  0.52 13.16 ?  40  ASN   A H    1 
ATOM   1133 H H    B ASN   A 1 40  ? 27.192 2.605   -2.307  0.48 12.97 ?  40  ASN   A H    1 
ATOM   1134 H HA   A ASN   A 1 40  ? 27.546 0.915   -4.304  0.52 14.00 ?  40  ASN   A HA   1 
ATOM   1135 H HA   B ASN   A 1 40  ? 27.222 0.958   -4.460  0.48 12.98 ?  40  ASN   A HA   1 
ATOM   1136 H HB2  A ASN   A 1 40  ? 27.825 2.851   -5.590  0.52 15.38 ?  40  ASN   A HB2  1 
ATOM   1137 H HB2  B ASN   A 1 40  ? 27.605 2.916   -5.742  0.48 13.02 ?  40  ASN   A HB2  1 
ATOM   1138 H HB3  A ASN   A 1 40  ? 26.446 2.886   -4.804  0.52 15.38 ?  40  ASN   A HB3  1 
ATOM   1139 H HB3  B ASN   A 1 40  ? 26.200 2.949   -5.003  0.48 13.02 ?  40  ASN   A HB3  1 
ATOM   1140 H HD21 A ASN   A 1 40  ? 26.953 5.927   -3.662  0.52 18.03 ?  40  ASN   A HD21 1 
ATOM   1141 H HD21 B ASN   A 1 40  ? 26.687 5.869   -3.582  0.48 14.56 ?  40  ASN   A HD21 1 
ATOM   1142 H HD22 A ASN   A 1 40  ? 25.999 4.939   -4.237  0.52 18.03 ?  40  ASN   A HD22 1 
ATOM   1143 H HD22 B ASN   A 1 40  ? 25.719 4.875   -4.124  0.48 14.56 ?  40  ASN   A HD22 1 
ATOM   1144 N N    A VAL   A 1 41  ? 30.032 1.319   -4.911  0.52 10.92 ?  41  VAL   A N    1 
ATOM   1145 N N    B VAL   A 1 41  ? 29.714 1.370   -5.127  0.48 11.04 ?  41  VAL   A N    1 
ATOM   1146 C CA   A VAL   A 1 41  ? 31.459 1.006   -4.908  0.52 10.96 ?  41  VAL   A CA   1 
ATOM   1147 C CA   B VAL   A 1 41  ? 31.141 1.058   -5.160  0.48 11.14 ?  41  VAL   A CA   1 
ATOM   1148 C C    A VAL   A 1 41  ? 32.311 2.169   -4.423  0.52 11.14 ?  41  VAL   A C    1 
ATOM   1149 C C    B VAL   A 1 41  ? 32.016 2.198   -4.648  0.48 10.89 ?  41  VAL   A C    1 
ATOM   1150 O O    A VAL   A 1 41  ? 33.435 1.954   -3.953  0.52 11.04 ?  41  VAL   A O    1 
ATOM   1151 O O    B VAL   A 1 41  ? 33.171 1.962   -4.279  0.48 11.31 ?  41  VAL   A O    1 
ATOM   1152 C CB   A VAL   A 1 41  ? 31.965 0.509   -6.284  0.52 10.45 ?  41  VAL   A CB   1 
ATOM   1153 C CB   B VAL   A 1 41  ? 31.598 0.615   -6.569  0.48 12.63 ?  41  VAL   A CB   1 
ATOM   1154 C CG1  A VAL   A 1 41  ? 31.235 -0.753  -6.707  0.52 12.16 ?  41  VAL   A CG1  1 
ATOM   1155 C CG1  B VAL   A 1 41  ? 30.959 -0.714  -6.948  0.48 13.91 ?  41  VAL   A CG1  1 
ATOM   1156 C CG2  A VAL   A 1 41  ? 31.866 1.600   -7.360  0.52 9.75  ?  41  VAL   A CG2  1 
ATOM   1157 C CG2  B VAL   A 1 41  ? 31.295 1.688   -7.616  0.48 13.25 ?  41  VAL   A CG2  1 
ATOM   1158 H H    A VAL   A 1 41  ? 29.666 1.297   -5.684  0.52 13.10 ?  41  VAL   A H    1 
ATOM   1159 H H    B VAL   A 1 41  ? 29.330 1.365   -5.896  0.48 13.25 ?  41  VAL   A H    1 
ATOM   1160 H HA   A VAL   A 1 41  ? 31.611 0.280   -4.287  0.52 13.15 ?  41  VAL   A HA   1 
ATOM   1161 H HA   B VAL   A 1 41  ? 31.297 0.303   -4.575  0.48 13.37 ?  41  VAL   A HA   1 
ATOM   1162 H HB   A VAL   A 1 41  ? 32.907 0.285   -6.204  0.52 12.54 ?  41  VAL   A HB   1 
ATOM   1163 H HB   B VAL   A 1 41  ? 32.560 0.484   -6.559  0.48 15.16 ?  41  VAL   A HB   1 
ATOM   1164 H HG11 A VAL   A 1 41  ? 31.584 -1.060  -7.559  0.52 14.59 ?  41  VAL   A HG11 1 
ATOM   1165 H HG11 B VAL   A 1 41  ? 31.271 -0.977  -7.828  0.48 16.70 ?  41  VAL   A HG11 1 
ATOM   1166 H HG12 A VAL   A 1 41  ? 31.366 -1.437  -6.031  0.52 14.59 ?  41  VAL   A HG12 1 
ATOM   1167 H HG12 B VAL   A 1 41  ? 31.217 -1.384  -6.293  0.48 16.70 ?  41  VAL   A HG12 1 
ATOM   1168 H HG13 A VAL   A 1 41  ? 30.286 -0.556  -6.794  0.52 14.59 ?  41  VAL   A HG13 1 
ATOM   1169 H HG13 B VAL   A 1 41  ? 29.996 -0.612  -6.954  0.48 16.70 ?  41  VAL   A HG13 1 
ATOM   1170 H HG21 A VAL   A 1 41  ? 32.090 1.210   -8.225  0.52 11.70 ?  41  VAL   A HG21 1 
ATOM   1171 H HG21 B VAL   A 1 41  ? 31.634 1.392   -8.477  0.48 15.90 ?  41  VAL   A HG21 1 
ATOM   1172 H HG22 A VAL   A 1 41  ? 30.961 1.941   -7.378  0.52 11.70 ?  41  VAL   A HG22 1 
ATOM   1173 H HG22 B VAL   A 1 41  ? 30.335 1.818   -7.668  0.48 15.90 ?  41  VAL   A HG22 1 
ATOM   1174 H HG23 A VAL   A 1 41  ? 32.489 2.311   -7.151  0.52 11.70 ?  41  VAL   A HG23 1 
ATOM   1175 H HG23 B VAL   A 1 41  ? 31.729 2.515   -7.358  0.48 15.90 ?  41  VAL   A HG23 1 
ATOM   1176 N N    A TYR   A 1 42  ? 31.817 3.401   -4.547  0.52 10.92 ?  42  TYR   A N    1 
ATOM   1177 N N    B TYR   A 1 42  ? 31.508 3.434   -4.636  0.48 11.04 ?  42  TYR   A N    1 
ATOM   1178 C CA   A TYR   A 1 42  ? 32.540 4.590   -4.104  0.52 11.31 ?  42  TYR   A CA   1 
ATOM   1179 C CA   B TYR   A 1 42  ? 32.275 4.618   -4.241  0.48 10.94 ?  42  TYR   A CA   1 
ATOM   1180 C C    A TYR   A 1 42  ? 32.226 4.950   -2.659  0.52 11.14 ?  42  TYR   A C    1 
ATOM   1181 C C    B TYR   A 1 42  ? 32.057 5.021   -2.786  0.48 10.55 ?  42  TYR   A C    1 
ATOM   1182 O O    A TYR   A 1 42  ? 32.837 5.877   -2.111  0.52 11.60 ?  42  TYR   A O    1 
ATOM   1183 O O    B TYR   A 1 42  ? 32.585 6.055   -2.357  0.48 10.55 ?  42  TYR   A O    1 
ATOM   1184 C CB   A TYR   A 1 42  ? 32.229 5.779   -5.030  0.52 12.16 ?  42  TYR   A CB   1 
ATOM   1185 C CB   B TYR   A 1 42  ? 31.915 5.806   -5.142  0.48 11.43 ?  42  TYR   A CB   1 
ATOM   1186 C CG   A TYR   A 1 42  ? 32.437 5.451   -6.496  0.52 12.19 ?  42  TYR   A CG   1 
ATOM   1187 C CG   B TYR   A 1 42  ? 32.056 5.507   -6.612  0.48 11.44 ?  42  TYR   A CG   1 
ATOM   1188 C CD1  A TYR   A 1 42  ? 33.712 5.258   -7.009  0.52 13.05 ?  42  TYR   A CD1  1 
ATOM   1189 C CD1  B TYR   A 1 42  ? 33.305 5.305   -7.181  0.48 12.01 ?  42  TYR   A CD1  1 
ATOM   1190 C CD2  A TYR   A 1 42  ? 31.357 5.298   -7.361  0.52 14.07 ?  42  TYR   A CD2  1 
ATOM   1191 C CD2  B TYR   A 1 42  ? 30.937 5.420   -7.435  0.48 12.79 ?  42  TYR   A CD2  1 
ATOM   1192 C CE1  A TYR   A 1 42  ? 33.913 4.941   -8.345  0.52 13.14 ?  42  TYR   A CE1  1 
ATOM   1193 C CE1  B TYR   A 1 42  ? 33.443 5.025   -8.528  0.48 12.29 ?  42  TYR   A CE1  1 
ATOM   1194 C CE2  A TYR   A 1 42  ? 31.550 4.991   -8.702  0.52 14.26 ?  42  TYR   A CE2  1 
ATOM   1195 C CE2  B TYR   A 1 42  ? 31.065 5.155   -8.786  0.48 13.50 ?  42  TYR   A CE2  1 
ATOM   1196 C CZ   A TYR   A 1 42  ? 32.833 4.810   -9.185  0.52 13.86 ?  42  TYR   A CZ   1 
ATOM   1197 C CZ   B TYR   A 1 42  ? 32.321 4.954   -9.328  0.48 12.92 ?  42  TYR   A CZ   1 
ATOM   1198 O OH   A TYR   A 1 42  ? 33.026 4.501   -10.510 0.52 15.08 ?  42  TYR   A OH   1 
ATOM   1199 O OH   B TYR   A 1 42  ? 32.465 4.682   -10.668 0.48 13.26 ?  42  TYR   A OH   1 
ATOM   1200 H H    A TYR   A 1 42  ? 31.044 3.569   -4.885  0.52 13.10 ?  42  TYR   A H    1 
ATOM   1201 H H    B TYR   A 1 42  ? 30.701 3.610   -4.865  0.48 13.25 ?  42  TYR   A H    1 
ATOM   1202 H HA   A TYR   A 1 42  ? 33.490 4.411   -4.166  0.52 13.57 ?  42  TYR   A HA   1 
ATOM   1203 H HA   B TYR   A 1 42  ? 33.218 4.431   -4.362  0.48 13.13 ?  42  TYR   A HA   1 
ATOM   1204 H HB2  A TYR   A 1 42  ? 31.302 6.041   -4.908  0.52 14.59 ?  42  TYR   A HB2  1 
ATOM   1205 H HB2  B TYR   A 1 42  ? 30.993 6.059   -4.976  0.48 13.71 ?  42  TYR   A HB2  1 
ATOM   1206 H HB3  A TYR   A 1 42  ? 32.814 6.518   -4.800  0.52 14.59 ?  42  TYR   A HB3  1 
ATOM   1207 H HB3  B TYR   A 1 42  ? 32.504 6.547   -4.931  0.48 13.71 ?  42  TYR   A HB3  1 
ATOM   1208 H HD1  A TYR   A 1 42  ? 34.449 5.349   -6.451  0.52 15.66 ?  42  TYR   A HD1  1 
ATOM   1209 H HD1  B TYR   A 1 42  ? 34.066 5.354   -6.645  0.48 14.41 ?  42  TYR   A HD1  1 
ATOM   1210 H HD2  A TYR   A 1 42  ? 30.492 5.424   -7.043  0.52 16.88 ?  42  TYR   A HD2  1 
ATOM   1211 H HD2  B TYR   A 1 42  ? 30.092 5.559   -7.075  0.48 15.35 ?  42  TYR   A HD2  1 
ATOM   1212 H HE1  A TYR   A 1 42  ? 34.775 4.824   -8.675  0.52 15.77 ?  42  TYR   A HE1  1 
ATOM   1213 H HE1  B TYR   A 1 42  ? 34.290 4.891   -8.893  0.48 14.74 ?  42  TYR   A HE1  1 
ATOM   1214 H HE2  A TYR   A 1 42  ? 30.815 4.897   -9.273  0.52 17.11 ?  42  TYR   A HE2  1 
ATOM   1215 H HE2  B TYR   A 1 42  ? 30.310 5.097   -9.325  0.48 16.20 ?  42  TYR   A HE2  1 
ATOM   1216 H HH   A TYR   A 1 42  ? 33.828 4.297   -10.646 0.52 18.10 ?  42  TYR   A HH   1 
ATOM   1217 H HH   B TYR   A 1 42  ? 31.716 4.659   -11.038 0.48 15.91 ?  42  TYR   A HH   1 
ATOM   1218 N N    . LEU   A 1 43  ? 31.294 4.233   -2.028  1.00 11.09 ?  43  LEU   A N    1 
ATOM   1219 C CA   . LEU   A 1 43  ? 30.839 4.572   -0.685  1.00 10.53 ?  43  LEU   A CA   1 
ATOM   1220 C C    . LEU   A 1 43  ? 30.357 6.020   -0.599  1.00 10.55 ?  43  LEU   A C    1 
ATOM   1221 O O    . LEU   A 1 43  ? 30.608 6.721   0.384   1.00 12.44 ?  43  LEU   A O    1 
ATOM   1222 C CB   . LEU   A 1 43  ? 31.885 4.262   0.389   1.00 11.97 ?  43  LEU   A CB   1 
ATOM   1223 C CG   . LEU   A 1 43  ? 32.389 2.812   0.473   1.00 12.02 ?  43  LEU   A CG   1 
ATOM   1224 C CD1  . LEU   A 1 43  ? 33.416 2.705   1.574   1.00 13.02 ?  43  LEU   A CD1  1 
ATOM   1225 C CD2  . LEU   A 1 43  ? 31.259 1.809   0.700   1.00 12.21 ?  43  LEU   A CD2  1 
ATOM   1226 H H    A LEU   A 1 43  ? 30.911 3.534   -2.358  0.52 13.31 ?  43  LEU   A H    1 
ATOM   1227 H H    B LEU   A 1 43  ? 31.021 3.454   -2.283  0.48 13.31 ?  43  LEU   A H    1 
ATOM   1228 H HA   . LEU   A 1 43  ? 30.069 4.013   -0.488  1.00 12.64 ?  43  LEU   A HA   1 
ATOM   1229 H HB2  . LEU   A 1 43  ? 32.652 4.826   0.240   1.00 14.36 ?  43  LEU   A HB2  1 
ATOM   1230 H HB3  . LEU   A 1 43  ? 31.494 4.470   1.257   1.00 14.36 ?  43  LEU   A HB3  1 
ATOM   1231 H HG   . LEU   A 1 43  ? 32.829 2.582   -0.366  1.00 14.42 ?  43  LEU   A HG   1 
ATOM   1232 H HD11 . LEU   A 1 43  ? 33.740 1.793   1.620   1.00 15.62 ?  43  LEU   A HD11 1 
ATOM   1233 H HD12 . LEU   A 1 43  ? 34.154 3.307   1.374   1.00 15.62 ?  43  LEU   A HD12 1 
ATOM   1234 H HD13 . LEU   A 1 43  ? 33.003 2.957   2.413   1.00 15.62 ?  43  LEU   A HD13 1 
ATOM   1235 H HD21 . LEU   A 1 43  ? 31.642 0.923   0.810   1.00 14.65 ?  43  LEU   A HD21 1 
ATOM   1236 H HD22 . LEU   A 1 43  ? 30.774 2.063   1.498   1.00 14.65 ?  43  LEU   A HD22 1 
ATOM   1237 H HD23 . LEU   A 1 43  ? 30.670 1.821   -0.069  1.00 14.65 ?  43  LEU   A HD23 1 
ATOM   1238 N N    A LYS   A 1 44  ? 29.656 6.469   -1.639  0.52 10.88 ?  44  LYS   A N    1 
ATOM   1239 N N    B LYS   A 1 44  ? 29.635 6.454   -1.631  0.48 11.40 ?  44  LYS   A N    1 
ATOM   1240 C CA   A LYS   A 1 44  ? 29.034 7.793   -1.640  0.52 11.62 ?  44  LYS   A CA   1 
ATOM   1241 C CA   B LYS   A 1 44  ? 28.965 7.750   -1.637  0.48 12.61 ?  44  LYS   A CA   1 
ATOM   1242 C C    A LYS   A 1 44  ? 27.602 7.625   -1.152  0.52 10.55 ?  44  LYS   A C    1 
ATOM   1243 C C    B LYS   A 1 44  ? 27.545 7.543   -1.125  0.48 12.05 ?  44  LYS   A C    1 
ATOM   1244 O O    A LYS   A 1 44  ? 26.732 7.140   -1.881  0.52 11.93 ?  44  LYS   A O    1 
ATOM   1245 O O    B LYS   A 1 44  ? 26.693 6.994   -1.833  0.48 12.61 ?  44  LYS   A O    1 
ATOM   1246 C CB   A LYS   A 1 44  ? 29.094 8.409   -3.030  0.52 13.74 ?  44  LYS   A CB   1 
ATOM   1247 C CB   B LYS   A 1 44  ? 28.954 8.331   -3.047  0.48 14.39 ?  44  LYS   A CB   1 
ATOM   1248 C CG   A LYS   A 1 44  ? 30.489 8.815   -3.466  0.52 17.64 ?  44  LYS   A CG   1 
ATOM   1249 C CG   B LYS   A 1 44  ? 30.290 8.875   -3.515  0.48 18.12 ?  44  LYS   A CG   1 
ATOM   1250 C CD   A LYS   A 1 44  ? 31.176 9.697   -2.433  0.52 22.87 ?  44  LYS   A CD   1 
ATOM   1251 C CD   B LYS   A 1 44  ? 30.954 9.718   -2.440  0.48 22.85 ?  44  LYS   A CD   1 
ATOM   1252 C CE   A LYS   A 1 44  ? 32.521 10.184  -2.928  0.52 25.73 ?  44  LYS   A CE   1 
ATOM   1253 C CE   B LYS   A 1 44  ? 32.090 10.546  -3.004  0.48 25.18 ?  44  LYS   A CE   1 
ATOM   1254 N NZ   A LYS   A 1 44  ? 33.334 10.750  -1.822  0.52 26.62 ?  44  LYS   A NZ   1 
ATOM   1255 N NZ   B LYS   A 1 44  ? 32.987 11.051  -1.931  0.48 26.79 ?  44  LYS   A NZ   1 
ATOM   1256 H H    A LYS   A 1 44  ? 29.527 6.018   -2.362  0.52 13.06 ?  44  LYS   A H    1 
ATOM   1257 H H    B LYS   A 1 44  ? 29.513 6.000   -2.353  0.48 13.69 ?  44  LYS   A H    1 
ATOM   1258 H HA   A LYS   A 1 44  ? 29.490 8.364   -1.005  0.52 13.94 ?  44  LYS   A HA   1 
ATOM   1259 H HA   B LYS   A 1 44  ? 29.412 8.354   -1.026  0.48 15.13 ?  44  LYS   A HA   1 
ATOM   1260 H HB2  A LYS   A 1 44  ? 28.755 7.767   -3.671  0.52 16.48 ?  44  LYS   A HB2  1 
ATOM   1261 H HB2  B LYS   A 1 44  ? 28.686 7.636   -3.668  0.48 17.27 ?  44  LYS   A HB2  1 
ATOM   1262 H HB3  A LYS   A 1 44  ? 28.538 9.205   -3.037  0.52 16.48 ?  44  LYS   A HB3  1 
ATOM   1263 H HB3  B LYS   A 1 44  ? 28.313 9.060   -3.078  0.48 17.27 ?  44  LYS   A HB3  1 
ATOM   1264 H HG2  A LYS   A 1 44  ? 31.028 8.019   -3.593  0.52 21.17 ?  44  LYS   A HG2  1 
ATOM   1265 H HG2  B LYS   A 1 44  ? 30.880 8.137   -3.734  0.48 21.75 ?  44  LYS   A HG2  1 
ATOM   1266 H HG3  A LYS   A 1 44  ? 30.429 9.314   -4.298  0.52 21.17 ?  44  LYS   A HG3  1 
ATOM   1267 H HG3  B LYS   A 1 44  ? 30.153 9.437   -4.296  0.48 21.75 ?  44  LYS   A HG3  1 
ATOM   1268 H HD2  A LYS   A 1 44  ? 30.611 10.464  -2.244  0.52 27.45 ?  44  LYS   A HD2  1 
ATOM   1269 H HD2  B LYS   A 1 44  ? 30.295 10.312  -2.048  0.48 27.42 ?  44  LYS   A HD2  1 
ATOM   1270 H HD3  A LYS   A 1 44  ? 31.327 9.183   -1.623  0.52 27.45 ?  44  LYS   A HD3  1 
ATOM   1271 H HD3  B LYS   A 1 44  ? 31.320 9.128   -1.758  0.48 27.42 ?  44  LYS   A HD3  1 
ATOM   1272 H HE2  A LYS   A 1 44  ? 33.008 9.439   -3.313  0.52 30.87 ?  44  LYS   A HE2  1 
ATOM   1273 H HE2  B LYS   A 1 44  ? 32.617 9.998   -3.607  0.48 30.22 ?  44  LYS   A HE2  1 
ATOM   1274 H HE3  A LYS   A 1 44  ? 32.384 10.876  -3.593  0.52 30.87 ?  44  LYS   A HE3  1 
ATOM   1275 H HE3  B LYS   A 1 44  ? 31.724 11.308  -3.477  0.48 30.22 ?  44  LYS   A HE3  1 
ATOM   1276 H HZ1  A LYS   A 1 44  ? 34.117 11.032  -2.135  0.52 31.94 ?  44  LYS   A HZ1  1 
ATOM   1277 H HZ1  B LYS   A 1 44  ? 33.645 11.533  -2.286  0.48 32.14 ?  44  LYS   A HZ1  1 
ATOM   1278 H HZ2  A LYS   A 1 44  ? 32.905 11.441  -1.454  0.52 31.94 ?  44  LYS   A HZ2  1 
ATOM   1279 H HZ2  B LYS   A 1 44  ? 32.528 11.560  -1.364  0.48 32.14 ?  44  LYS   A HZ2  1 
ATOM   1280 H HZ3  A LYS   A 1 44  ? 33.473 10.133  -1.199  0.52 31.94 ?  44  LYS   A HZ3  1 
ATOM   1281 H HZ3  B LYS   A 1 44  ? 33.341 10.366  -1.483  0.48 32.14 ?  44  LYS   A HZ3  1 
ATOM   1282 N N    A HIS   A 1 45  ? 27.360 8.019   0.096   0.52 10.03 ?  45  HIS   A N    1 
ATOM   1283 N N    B HIS   A 1 45  ? 27.294 7.967   0.111   0.48 12.28 ?  45  HIS   A N    1 
ATOM   1284 C CA   A HIS   A 1 45  ? 26.130 7.649   0.801   0.52 10.07 ?  45  HIS   A CA   1 
ATOM   1285 C CA   B HIS   A 1 45  ? 26.025 7.690   0.783   0.48 12.57 ?  45  HIS   A CA   1 
ATOM   1286 C C    A HIS   A 1 45  ? 25.073 8.750   0.640   0.52 10.56 ?  45  HIS   A C    1 
ATOM   1287 C C    B HIS   A 1 45  ? 25.083 8.866   0.557   0.48 13.28 ?  45  HIS   A C    1 
ATOM   1288 O O    A HIS   A 1 45  ? 24.700 9.459   1.578   0.52 11.21 ?  45  HIS   A O    1 
ATOM   1289 O O    B HIS   A 1 45  ? 25.007 9.796   1.362   0.48 14.74 ?  45  HIS   A O    1 
ATOM   1290 C CB   A HIS   A 1 45  ? 26.443 7.344   2.260   0.52 9.87  ?  45  HIS   A CB   1 
ATOM   1291 C CB   B HIS   A 1 45  ? 26.261 7.450   2.266   0.48 11.80 ?  45  HIS   A CB   1 
ATOM   1292 C CG   A HIS   A 1 45  ? 27.555 6.356   2.449   0.52 10.22 ?  45  HIS   A CG   1 
ATOM   1293 C CG   B HIS   A 1 45  ? 27.394 6.519   2.551   0.48 10.37 ?  45  HIS   A CG   1 
ATOM   1294 N ND1  A HIS   A 1 45  ? 27.530 5.082   1.916   0.52 10.82 ?  45  HIS   A ND1  1 
ATOM   1295 N ND1  B HIS   A 1 45  ? 27.431 5.224   2.080   0.48 11.03 ?  45  HIS   A ND1  1 
ATOM   1296 C CD2  A HIS   A 1 45  ? 28.732 6.465   3.112   0.52 10.84 ?  45  HIS   A CD2  1 
ATOM   1297 C CD2  B HIS   A 1 45  ? 28.539 6.702   3.251   0.48 9.46  ?  45  HIS   A CD2  1 
ATOM   1298 C CE1  A HIS   A 1 45  ? 28.638 4.449   2.255   0.52 11.66 ?  45  HIS   A CE1  1 
ATOM   1299 C CE1  B HIS   A 1 45  ? 28.546 4.647   2.489   0.48 9.53  ?  45  HIS   A CE1  1 
ATOM   1300 N NE2  A HIS   A 1 45  ? 29.387 5.266   2.975   0.52 11.99 ?  45  HIS   A NE2  1 
ATOM   1301 N NE2  B HIS   A 1 45  ? 29.240 5.523   3.195   0.48 9.35  ?  45  HIS   A NE2  1 
ATOM   1302 H H    A HIS   A 1 45  ? 27.892 8.512   0.559   0.52 12.04 ?  45  HIS   A H    1 
ATOM   1303 H H    B HIS   A 1 45  ? 27.849 8.426   0.586   0.48 14.74 ?  45  HIS   A H    1 
ATOM   1304 H HA   A HIS   A 1 45  ? 25.774 6.842   0.405   0.52 12.09 ?  45  HIS   A HA   1 
ATOM   1305 H HA   B HIS   A 1 45  ? 25.629 6.889   0.400   0.48 15.08 ?  45  HIS   A HA   1 
ATOM   1306 H HB2  A HIS   A 1 45  ? 26.691 8.166   2.709   0.52 11.85 ?  45  HIS   A HB2  1 
ATOM   1307 H HB2  B HIS   A 1 45  ? 26.458 8.297   2.691   0.48 14.15 ?  45  HIS   A HB2  1 
ATOM   1308 H HB3  A HIS   A 1 45  ? 25.645 6.974   2.679   0.52 11.85 ?  45  HIS   A HB3  1 
ATOM   1309 H HB3  B HIS   A 1 45  ? 25.457 7.066   2.651   0.48 14.15 ?  45  HIS   A HB3  1 
ATOM   1310 H HD2  A HIS   A 1 45  ? 29.038 7.212   3.578   0.52 13.01 ?  45  HIS   A HD2  1 
ATOM   1311 H HD2  B HIS   A 1 45  ? 28.803 7.479   3.687   0.48 11.35 ?  45  HIS   A HD2  1 
ATOM   1312 H HE1  A HIS   A 1 45  ? 28.856 3.576   2.023   0.52 14.00 ?  45  HIS   A HE1  1 
ATOM   1313 H HE1  B HIS   A 1 45  ? 28.805 3.771   2.301   0.48 11.43 ?  45  HIS   A HE1  1 
ATOM   1314 H HE2  A HIS   A 1 45  ? 30.157 5.075   3.310   0.52 14.39 ?  45  HIS   A HE2  1 
ATOM   1315 H HE2  B HIS   A 1 45  ? 30.002 5.374   3.564   0.48 11.22 ?  45  HIS   A HE2  1 
ATOM   1316 N N    A GLY   A 1 46  ? 24.568 8.865   -0.588  0.52 11.84 ?  46  GLY   A N    1 
ATOM   1317 N N    B GLY   A 1 46  ? 24.345 8.823   -0.548  0.48 13.66 ?  46  GLY   A N    1 
ATOM   1318 C CA   A GLY   A 1 46  ? 23.764 10.017  -0.972  0.52 12.95 ?  46  GLY   A CA   1 
ATOM   1319 C CA   B GLY   A 1 46  ? 23.502 9.949   -0.903  0.48 13.99 ?  46  GLY   A CA   1 
ATOM   1320 C C    A GLY   A 1 46  ? 22.266 9.893   -0.766  0.52 12.82 ?  46  GLY   A C    1 
ATOM   1321 C C    B GLY   A 1 46  ? 22.057 9.816   -0.462  0.48 13.30 ?  46  GLY   A C    1 
ATOM   1322 O O    A GLY   A 1 46  ? 21.599 10.892  -0.477  0.52 13.41 ?  46  GLY   A O    1 
ATOM   1323 O O    B GLY   A 1 46  ? 21.470 10.774  0.048   0.48 14.25 ?  46  GLY   A O    1 
ATOM   1324 H H    A GLY   A 1 46  ? 24.679 8.285   -1.212  0.52 14.20 ?  46  GLY   A H    1 
ATOM   1325 H H    B GLY   A 1 46  ? 24.324 8.160   -1.100  0.48 16.39 ?  46  GLY   A H    1 
ATOM   1326 H HA2  A GLY   A 1 46  ? 24.067 10.784  -0.467  0.52 15.54 ?  46  GLY   A HA2  1 
ATOM   1327 H HA2  B GLY   A 1 46  ? 23.872 10.752  -0.501  0.48 16.79 ?  46  GLY   A HA2  1 
ATOM   1328 H HA3  A GLY   A 1 46  ? 23.919 10.196  -1.911  0.52 15.54 ?  46  GLY   A HA3  1 
ATOM   1329 H HA3  B GLY   A 1 46  ? 23.523 10.057  -1.864  0.48 16.79 ?  46  GLY   A HA3  1 
ATOM   1330 N N    A GLY   A 1 47  ? 21.721 8.689   -0.927  0.52 12.98 ?  47  GLY   A N    1 
ATOM   1331 N N    B GLY   A 1 47  ? 21.472 8.634   -0.643  0.48 12.95 ?  47  GLY   A N    1 
ATOM   1332 C CA   A GLY   A 1 47  ? 20.288 8.477   -0.882  0.52 12.61 ?  47  GLY   A CA   1 
ATOM   1333 C CA   B GLY   A 1 47  ? 20.051 8.461   -0.433  0.48 12.72 ?  47  GLY   A CA   1 
ATOM   1334 C C    A GLY   A 1 47  ? 19.979 7.048   -0.484  0.52 12.31 ?  47  GLY   A C    1 
ATOM   1335 C C    B GLY   A 1 47  ? 19.713 7.037   -0.051  0.48 11.51 ?  47  GLY   A C    1 
ATOM   1336 O O    A GLY   A 1 47  ? 20.879 6.241   -0.238  0.52 13.38 ?  47  GLY   A O    1 
ATOM   1337 O O    B GLY   A 1 47  ? 20.588 6.175   0.067   0.48 10.96 ?  47  GLY   A O    1 
ATOM   1338 H H    A GLY   A 1 47  ? 22.170 7.971   -1.061  0.52 15.57 ?  47  GLY   A H    1 
ATOM   1339 H H    B GLY   A 1 47  ? 21.890 7.923   -0.884  0.48 15.54 ?  47  GLY   A H    1 
ATOM   1340 H HA2  A GLY   A 1 47  ? 19.880 9.083   -0.241  0.52 15.13 ?  47  GLY   A HA2  1 
ATOM   1341 H HA2  B GLY   A 1 47  ? 19.755 9.059   0.273   0.48 15.27 ?  47  GLY   A HA2  1 
ATOM   1342 H HA3  A GLY   A 1 47  ? 19.899 8.646   -1.757  0.52 15.13 ?  47  GLY   A HA3  1 
ATOM   1343 H HA3  B GLY   A 1 47  ? 19.577 8.687   -1.247  0.48 15.27 ?  47  GLY   A HA3  1 
ATOM   1344 N N    A GLY   A 1 48  ? 18.687 6.740   -0.411  0.52 11.24 ?  48  GLY   A N    1 
ATOM   1345 N N    B GLY   A 1 48  ? 18.419 6.793   0.137   0.48 11.64 ?  48  GLY   A N    1 
ATOM   1346 C CA   A GLY   A 1 48  ? 18.275 5.411   -0.012  0.52 10.81 ?  48  GLY   A CA   1 
ATOM   1347 C CA   B GLY   A 1 48  ? 17.982 5.480   0.580   0.48 11.12 ?  48  GLY   A CA   1 
ATOM   1348 C C    A GLY   A 1 48  ? 18.698 5.099   1.409   0.52 10.72 ?  48  GLY   A C    1 
ATOM   1349 C C    B GLY   A 1 48  ? 18.616 5.095   1.901   0.48 11.40 ?  48  GLY   A C    1 
ATOM   1350 O O    A GLY   A 1 48  ? 18.854 5.986   2.259   0.52 11.23 ?  48  GLY   A O    1 
ATOM   1351 O O    B GLY   A 1 48  ? 18.837 5.930   2.788   0.48 11.52 ?  48  GLY   A O    1 
ATOM   1352 H H    A GLY   A 1 48  ? 18.039 7.276   -0.584  0.52 13.49 ?  48  GLY   A H    1 
ATOM   1353 H H    B GLY   A 1 48  ? 17.778 7.361   0.012   0.48 13.97 ?  48  GLY   A H    1 
ATOM   1354 H HA2  A GLY   A 1 48  ? 17.312 5.330   -0.077  0.52 12.97 ?  48  GLY   A HA2  1 
ATOM   1355 H HA2  B GLY   A 1 48  ? 17.016 5.472   0.684   0.48 13.35 ?  48  GLY   A HA2  1 
ATOM   1356 H HA3  A GLY   A 1 48  ? 18.682 4.752   -0.599  0.52 12.97 ?  48  GLY   A HA3  1 
ATOM   1357 H HA3  B GLY   A 1 48  ? 18.225 4.816   -0.084  0.48 13.35 ?  48  GLY   A HA3  1 
ATOM   1358 N N    A VAL   A 1 49  ? 18.890 3.802   1.671   0.52 11.55 ?  49  VAL   A N    1 
ATOM   1359 N N    B VAL   A 1 49  ? 18.898 3.799   2.039   0.48 10.85 ?  49  VAL   A N    1 
ATOM   1360 C CA   A VAL   A 1 49  ? 19.385 3.364   2.976   0.52 12.32 ?  49  VAL   A CA   1 
ATOM   1361 C CA   B VAL   A 1 49  ? 19.524 3.273   3.251   0.48 10.21 ?  49  VAL   A CA   1 
ATOM   1362 C C    A VAL   A 1 49  ? 20.696 4.061   3.311   0.52 11.86 ?  49  VAL   A C    1 
ATOM   1363 C C    B VAL   A 1 49  ? 20.807 4.026   3.575   0.48 9.69  ?  49  VAL   A C    1 
ATOM   1364 O O    A VAL   A 1 49  ? 20.898 4.527   4.434   0.52 11.77 ?  49  VAL   A O    1 
ATOM   1365 O O    B VAL   A 1 49  ? 21.052 4.394   4.726   0.48 9.63  ?  49  VAL   A O    1 
ATOM   1366 C CB   A VAL   A 1 49  ? 19.542 1.832   3.002   0.52 13.51 ?  49  VAL   A CB   1 
ATOM   1367 C CB   B VAL   A 1 49  ? 19.793 1.767   3.096   0.48 11.28 ?  49  VAL   A CB   1 
ATOM   1368 C CG1  A VAL   A 1 49  ? 20.310 1.378   4.250   0.52 13.69 ?  49  VAL   A CG1  1 
ATOM   1369 C CG1  B VAL   A 1 49  ? 20.697 1.273   4.209   0.48 10.83 ?  49  VAL   A CG1  1 
ATOM   1370 C CG2  A VAL   A 1 49  ? 18.180 1.147   2.934   0.52 15.52 ?  49  VAL   A CG2  1 
ATOM   1371 C CG2  B VAL   A 1 49  ? 18.494 0.978   3.078   0.48 12.75 ?  49  VAL   A CG2  1 
ATOM   1372 H H    A VAL   A 1 49  ? 18.747 3.161   1.116   0.52 13.86 ?  49  VAL   A H    1 
ATOM   1373 H H    B VAL   A 1 49  ? 18.731 3.207   1.445   0.48 13.02 ?  49  VAL   A H    1 
ATOM   1374 H HA   A VAL   A 1 49  ? 18.736 3.602   3.658   0.52 14.79 ?  49  VAL   A HA   1 
ATOM   1375 H HA   B VAL   A 1 49  ? 18.912 3.395   3.998   0.48 12.26 ?  49  VAL   A HA   1 
ATOM   1376 H HB   A VAL   A 1 49  ? 20.055 1.555   2.228   0.52 16.21 ?  49  VAL   A HB   1 
ATOM   1377 H HB   B VAL   A 1 49  ? 20.247 1.619   2.252   0.48 13.53 ?  49  VAL   A HB   1 
ATOM   1378 H HG11 A VAL   A 1 49  ? 20.161 0.429   4.384   0.52 16.43 ?  49  VAL   A HG11 1 
ATOM   1379 H HG11 B VAL   A 1 49  ? 20.611 0.311   4.272   0.48 13.00 ?  49  VAL   A HG11 1 
ATOM   1380 H HG12 A VAL   A 1 49  ? 21.257 1.547   4.122   0.52 16.43 ?  49  VAL   A HG12 1 
ATOM   1381 H HG12 B VAL   A 1 49  ? 21.614 1.511   4.002   0.48 13.00 ?  49  VAL   A HG12 1 
ATOM   1382 H HG13 A VAL   A 1 49  ? 19.985 1.873   5.019   0.52 16.43 ?  49  VAL   A HG13 1 
ATOM   1383 H HG13 B VAL   A 1 49  ? 20.424 1.686   5.042   0.48 13.00 ?  49  VAL   A HG13 1 
ATOM   1384 H HG21 A VAL   A 1 49  ? 18.310 0.186   2.950   0.52 18.63 ?  49  VAL   A HG21 1 
ATOM   1385 H HG21 B VAL   A 1 49  ? 18.694 0.039   2.956   0.48 15.30 ?  49  VAL   A HG21 1 
ATOM   1386 H HG22 A VAL   A 1 49  ? 17.651 1.423   3.699   0.52 18.63 ?  49  VAL   A HG22 1 
ATOM   1387 H HG22 B VAL   A 1 49  ? 18.030 1.110   3.923   0.48 15.30 ?  49  VAL   A HG22 1 
ATOM   1388 H HG23 A VAL   A 1 49  ? 17.740 1.409   2.112   0.52 18.63 ?  49  VAL   A HG23 1 
ATOM   1389 H HG23 B VAL   A 1 49  ? 17.938 1.297   2.348   0.48 15.30 ?  49  VAL   A HG23 1 
ATOM   1390 N N    A ALA   A 1 50  ? 21.615 4.113   2.345   0.52 11.26 ?  50  ALA   A N    1 
ATOM   1391 N N    B ALA   A 1 50  ? 21.668 4.215   2.573   0.48 9.68  ?  50  ALA   A N    1 
ATOM   1392 C CA   A ALA   A 1 50  ? 22.944 4.657   2.604   0.52 11.18 ?  50  ALA   A CA   1 
ATOM   1393 C CA   B ALA   A 1 50  ? 22.985 4.785   2.833   0.48 9.11  ?  50  ALA   A CA   1 
ATOM   1394 C C    A ALA   A 1 50  ? 22.871 6.115   3.027   0.52 11.00 ?  50  ALA   A C    1 
ATOM   1395 C C    B ALA   A 1 50  ? 22.876 6.240   3.258   0.48 9.48  ?  50  ALA   A C    1 
ATOM   1396 O O    A ALA   A 1 50  ? 23.526 6.529   3.989   0.52 11.26 ?  50  ALA   A O    1 
ATOM   1397 O O    B ALA   A 1 50  ? 23.473 6.652   4.258   0.48 9.49  ?  50  ALA   A O    1 
ATOM   1398 C CB   A ALA   A 1 50  ? 23.801 4.512   1.351   0.52 11.53 ?  50  ALA   A CB   1 
ATOM   1399 C CB   B ALA   A 1 50  ? 23.853 4.658   1.585   0.48 9.60  ?  50  ALA   A CB   1 
ATOM   1400 H H    A ALA   A 1 50  ? 21.493 3.842   1.545   0.52 13.51 ?  50  ALA   A H    1 
ATOM   1401 H H    B ALA   A 1 50  ? 21.510 4.035   1.749   0.48 11.62 ?  50  ALA   A H    1 
ATOM   1402 H HA   A ALA   A 1 50  ? 23.362 4.163   3.326   0.52 13.41 ?  50  ALA   A HA   1 
ATOM   1403 H HA   B ALA   A 1 50  ? 23.409 4.293   3.555   0.48 10.93 ?  50  ALA   A HA   1 
ATOM   1404 H HB1  A ALA   A 1 50  ? 24.681 4.879   1.529   0.52 13.83 ?  50  ALA   A HB1  1 
ATOM   1405 H HB1  B ALA   A 1 50  ? 24.730 5.032   1.771   0.48 11.51 ?  50  ALA   A HB1  1 
ATOM   1406 H HB2  A ALA   A 1 50  ? 23.871 3.572   1.127   0.52 13.83 ?  50  ALA   A HB2  1 
ATOM   1407 H HB2  B ALA   A 1 50  ? 23.936 3.721   1.354   0.48 11.51 ?  50  ALA   A HB2  1 
ATOM   1408 H HB3  A ALA   A 1 50  ? 23.379 4.998   0.626   0.52 13.83 ?  50  ALA   A HB3  1 
ATOM   1409 H HB3  B ALA   A 1 50  ? 23.434 5.144   0.859   0.48 11.51 ?  50  ALA   A HB3  1 
ATOM   1410 N N    A GLY   A 1 51  ? 22.076 6.912   2.318   0.52 11.09 ?  51  GLY   A N    1 
ATOM   1411 N N    B GLY   A 1 51  ? 22.099 7.029   2.518   0.48 10.79 ?  51  GLY   A N    1 
ATOM   1412 C CA   A GLY   A 1 51  ? 21.900 8.295   2.726   0.52 11.80 ?  51  GLY   A CA   1 
ATOM   1413 C CA   B GLY   A 1 51  ? 21.967 8.435   2.858   0.48 10.59 ?  51  GLY   A CA   1 
ATOM   1414 C C    A GLY   A 1 51  ? 21.299 8.408   4.114   0.52 11.83 ?  51  GLY   A C    1 
ATOM   1415 C C    B GLY   A 1 51  ? 21.328 8.637   4.216   0.48 10.30 ?  51  GLY   A C    1 
ATOM   1416 O O    A GLY   A 1 51  ? 21.697 9.265   4.906   0.52 12.89 ?  51  GLY   A O    1 
ATOM   1417 O O    B GLY   A 1 51  ? 21.691 9.557   4.956   0.48 10.06 ?  51  GLY   A O    1 
ATOM   1418 H H    A GLY   A 1 51  ? 21.643 6.685   1.614   0.52 13.30 ?  51  GLY   A H    1 
ATOM   1419 H H    B GLY   A 1 51  ? 21.642 6.776   1.839   0.48 12.94 ?  51  GLY   A H    1 
ATOM   1420 H HA2  A GLY   A 1 51  ? 22.755 8.751   2.728   0.52 14.16 ?  51  GLY   A HA2  1 
ATOM   1421 H HA2  B GLY   A 1 51  ? 22.840 8.853   2.866   0.48 12.71 ?  51  GLY   A HA2  1 
ATOM   1422 H HA3  A GLY   A 1 51  ? 21.314 8.751   2.094   0.52 14.16 ?  51  GLY   A HA3  1 
ATOM   1423 H HA3  B GLY   A 1 51  ? 21.416 8.879   2.193   0.48 12.71 ?  51  GLY   A HA3  1 
ATOM   1424 N N    A ALA   A 1 52  ? 20.329 7.542   4.426   0.52 11.81 ?  52  ALA   A N    1 
ATOM   1425 N N    B ALA   A 1 52  ? 20.365 7.777   4.566   0.48 10.23 ?  52  ALA   A N    1 
ATOM   1426 C CA   A ALA   A 1 52  ? 19.679 7.579   5.731   0.52 11.87 ?  52  ALA   A CA   1 
ATOM   1427 C CA   B ALA   A 1 52  ? 19.697 7.901   5.855   0.48 10.51 ?  52  ALA   A CA   1 
ATOM   1428 C C    A ALA   A 1 52  ? 20.642 7.193   6.852   0.52 11.92 ?  52  ALA   A C    1 
ATOM   1429 C C    B ALA   A 1 52  ? 20.584 7.419   6.999   0.48 10.68 ?  52  ALA   A C    1 
ATOM   1430 O O    A ALA   A 1 52  ? 20.701 7.864   7.888   0.52 12.97 ?  52  ALA   A O    1 
ATOM   1431 O O    B ALA   A 1 52  ? 20.641 8.064   8.054   0.48 11.51 ?  52  ALA   A O    1 
ATOM   1432 C CB   A ALA   A 1 52  ? 18.456 6.657   5.721   0.52 12.64 ?  52  ALA   A CB   1 
ATOM   1433 C CB   B ALA   A 1 52  ? 18.366 7.148   5.828   0.48 11.14 ?  52  ALA   A CB   1 
ATOM   1434 H H    A ALA   A 1 52  ? 20.032 6.933   3.898   0.52 14.17 ?  52  ALA   A H    1 
ATOM   1435 H H    B ALA   A 1 52  ? 20.090 7.120   4.080   0.48 12.28 ?  52  ALA   A H    1 
ATOM   1436 H HA   A ALA   A 1 52  ? 19.364 8.480   5.903   0.52 14.25 ?  52  ALA   A HA   1 
ATOM   1437 H HA   B ALA   A 1 52  ? 19.497 8.835   6.011   0.48 12.61 ?  52  ALA   A HA   1 
ATOM   1438 H HB1  A ALA   A 1 52  ? 18.021 6.697   6.589   0.52 15.17 ?  52  ALA   A HB1  1 
ATOM   1439 H HB1  B ALA   A 1 52  ? 17.928 7.242   6.691   0.48 13.37 ?  52  ALA   A HB1  1 
ATOM   1440 H HB2  A ALA   A 1 52  ? 17.838 6.956   5.032   0.52 15.17 ?  52  ALA   A HB2  1 
ATOM   1441 H HB2  B ALA   A 1 52  ? 17.800 7.525   5.133   0.48 13.37 ?  52  ALA   A HB2  1 
ATOM   1442 H HB3  A ALA   A 1 52  ? 18.741 5.750   5.535   0.52 15.17 ?  52  ALA   A HB3  1 
ATOM   1443 H HB3  B ALA   A 1 52  ? 18.531 6.210   5.643   0.48 13.37 ?  52  ALA   A HB3  1 
ATOM   1444 N N    A LEU   A 1 53  ? 21.397 6.104   6.677   0.52 11.52 ?  53  LEU   A N    1 
ATOM   1445 N N    B LEU   A 1 53  ? 21.286 6.295   6.818   0.48 10.55 ?  53  LEU   A N    1 
ATOM   1446 C CA   A LEU   A 1 53  ? 22.342 5.710   7.719   0.52 11.81 ?  53  LEU   A CA   1 
ATOM   1447 C CA   B LEU   A 1 53  ? 22.265 5.877   7.819   0.48 10.33 ?  53  LEU   A CA   1 
ATOM   1448 C C    A LEU   A 1 53  ? 23.384 6.793   7.940   0.52 11.27 ?  53  LEU   A C    1 
ATOM   1449 C C    B LEU   A 1 53  ? 23.309 6.965   8.020   0.48 10.07 ?  53  LEU   A C    1 
ATOM   1450 O O    A LEU   A 1 53  ? 23.768 7.082   9.080   0.52 11.61 ?  53  LEU   A O    1 
ATOM   1451 O O    B LEU   A 1 53  ? 23.561 7.403   9.149   0.48 11.06 ?  53  LEU   A O    1 
ATOM   1452 C CB   A LEU   A 1 53  ? 23.024 4.390   7.353   0.52 12.41 ?  53  LEU   A CB   1 
ATOM   1453 C CB   B LEU   A 1 53  ? 22.948 4.567   7.403   0.48 11.19 ?  53  LEU   A CB   1 
ATOM   1454 C CG   A LEU   A 1 53  ? 22.108 3.161   7.367   0.52 13.00 ?  53  LEU   A CG   1 
ATOM   1455 C CG   B LEU   A 1 53  ? 22.235 3.213   7.568   0.48 11.54 ?  53  LEU   A CG   1 
ATOM   1456 C CD1  A LEU   A 1 53  ? 22.832 1.947   6.825   0.52 13.74 ?  53  LEU   A CD1  1 
ATOM   1457 C CD1  B LEU   A 1 53  ? 23.033 2.128   6.875   0.48 11.99 ?  53  LEU   A CD1  1 
ATOM   1458 C CD2  A LEU   A 1 53  ? 21.581 2.901   8.771   0.52 13.14 ?  53  LEU   A CD2  1 
ATOM   1459 C CD2  B LEU   A 1 53  ? 22.021 2.846   9.026   0.48 12.27 ?  53  LEU   A CD2  1 
ATOM   1460 H H    A LEU   A 1 53  ? 21.383 5.595   5.983   0.52 13.83 ?  53  LEU   A H    1 
ATOM   1461 H H    B LEU   A 1 53  ? 21.219 5.775   6.136   0.48 12.66 ?  53  LEU   A H    1 
ATOM   1462 H HA   A LEU   A 1 53  ? 21.862 5.586   8.551   0.52 14.17 ?  53  LEU   A HA   1 
ATOM   1463 H HA   B LEU   A 1 53  ? 21.817 5.731   8.663   0.48 12.39 ?  53  LEU   A HA   1 
ATOM   1464 H HB2  A LEU   A 1 53  ? 23.395 4.474   6.457   0.52 14.90 ?  53  LEU   A HB2  1 
ATOM   1465 H HB2  B LEU   A 1 53  ? 23.166 4.644   6.461   0.48 13.43 ?  53  LEU   A HB2  1 
ATOM   1466 H HB3  A LEU   A 1 53  ? 23.745 4.231   7.984   0.52 14.90 ?  53  LEU   A HB3  1 
ATOM   1467 H HB3  B LEU   A 1 53  ? 23.772 4.499   7.906   0.48 13.43 ?  53  LEU   A HB3  1 
ATOM   1468 H HG   A LEU   A 1 53  ? 21.349 3.339   6.790   0.52 15.60 ?  53  LEU   A HG   1 
ATOM   1469 H HG   B LEU   A 1 53  ? 21.366 3.260   7.137   0.48 13.85 ?  53  LEU   A HG   1 
ATOM   1470 H HD11 A LEU   A 1 53  ? 22.227 1.191   6.846   0.52 16.49 ?  53  LEU   A HD11 1 
ATOM   1471 H HD11 B LEU   A 1 53  ? 22.574 1.279   6.993   0.48 14.39 ?  53  LEU   A HD11 1 
ATOM   1472 H HD12 A LEU   A 1 53  ? 23.110 2.128   5.914   0.52 16.49 ?  53  LEU   A HD12 1 
ATOM   1473 H HD12 B LEU   A 1 53  ? 23.101 2.338   5.932   0.48 14.39 ?  53  LEU   A HD12 1 
ATOM   1474 H HD13 A LEU   A 1 53  ? 23.606 1.771   7.381   0.52 16.49 ?  53  LEU   A HD13 1 
ATOM   1475 H HD13 B LEU   A 1 53  ? 23.915 2.084   7.273   0.48 14.39 ?  53  LEU   A HD13 1 
ATOM   1476 H HD21 A LEU   A 1 53  ? 21.111 2.055   8.778   0.52 15.77 ?  53  LEU   A HD21 1 
ATOM   1477 H HD21 B LEU   A 1 53  ? 21.576 1.985   9.074   0.48 14.72 ?  53  LEU   A HD21 1 
ATOM   1478 H HD22 A LEU   A 1 53  ? 22.328 2.872   9.388   0.52 15.77 ?  53  LEU   A HD22 1 
ATOM   1479 H HD22 B LEU   A 1 53  ? 22.881 2.799   9.471   0.48 14.72 ?  53  LEU   A HD22 1 
ATOM   1480 H HD23 A LEU   A 1 53  ? 20.974 3.617   9.023   0.52 15.77 ?  53  LEU   A HD23 1 
ATOM   1481 H HD23 B LEU   A 1 53  ? 21.469 3.526   9.444   0.48 14.72 ?  53  LEU   A HD23 1 
ATOM   1482 N N    A ASN   A 1 54  ? 23.857 7.404   6.860   0.52 10.96 ?  54  ASN   A N    1 
ATOM   1483 N N    B ASN   A 1 54  ? 23.922 7.423   6.927   0.48 10.44 ?  54  ASN   A N    1 
ATOM   1484 C CA   A ASN   A 1 54  ? 24.918 8.388   7.007   0.52 11.53 ?  54  ASN   A CA   1 
ATOM   1485 C CA   B ASN   A 1 54  ? 24.967 8.428   7.057   0.48 10.98 ?  54  ASN   A CA   1 
ATOM   1486 C C    A ASN   A 1 54  ? 24.427 9.635   7.739   0.52 11.82 ?  54  ASN   A C    1 
ATOM   1487 C C    B ASN   A 1 54  ? 24.445 9.683   7.744   0.48 11.46 ?  54  ASN   A C    1 
ATOM   1488 O O    A ASN   A 1 54  ? 25.115 10.157  8.624   0.52 12.59 ?  54  ASN   A O    1 
ATOM   1489 O O    B ASN   A 1 54  ? 25.131 10.270  8.589   0.48 12.15 ?  54  ASN   A O    1 
ATOM   1490 C CB   A ASN   A 1 54  ? 25.494 8.739   5.644   0.52 11.88 ?  54  ASN   A CB   1 
ATOM   1491 C CB   B ASN   A 1 54  ? 25.555 8.787   5.700   0.48 11.10 ?  54  ASN   A CB   1 
ATOM   1492 C CG   A ASN   A 1 54  ? 26.577 9.775   5.745   0.52 12.17 ?  54  ASN   A CG   1 
ATOM   1493 C CG   B ASN   A 1 54  ? 26.519 9.943   5.801   0.48 10.67 ?  54  ASN   A CG   1 
ATOM   1494 O OD1  A ASN   A 1 54  ? 27.567 9.585   6.452   0.52 12.70 ?  54  ASN   A OD1  1 
ATOM   1495 O OD1  B ASN   A 1 54  ? 27.533 9.846   6.494   0.48 9.81  ?  54  ASN   A OD1  1 
ATOM   1496 N ND2  A ASN   A 1 54  ? 26.389 10.889  5.061   0.52 12.68 ?  54  ASN   A ND2  1 
ATOM   1497 N ND2  B ASN   A 1 54  ? 26.198 11.052  5.146   0.48 11.52 ?  54  ASN   A ND2  1 
ATOM   1498 H H    A ASN   A 1 54  ? 23.580 7.278   6.053   0.52 13.15 ?  54  ASN   A H    1 
ATOM   1499 H H    B ASN   A 1 54  ? 23.743 7.184   6.119   0.48 12.53 ?  54  ASN   A H    1 
ATOM   1500 H HA   A ASN   A 1 54  ? 25.624 7.999   7.537   0.52 13.84 ?  54  ASN   A HA   1 
ATOM   1501 H HA   B ASN   A 1 54  ? 25.676 8.070   7.606   0.48 13.18 ?  54  ASN   A HA   1 
ATOM   1502 H HB2  A ASN   A 1 54  ? 25.872 7.939   5.247   0.52 14.26 ?  54  ASN   A HB2  1 
ATOM   1503 H HB2  B ASN   A 1 54  ? 26.037 8.021   5.353   0.48 13.32 ?  54  ASN   A HB2  1 
ATOM   1504 H HB3  A ASN   A 1 54  ? 24.789 9.091   5.079   0.52 14.26 ?  54  ASN   A HB3  1 
ATOM   1505 H HB3  B ASN   A 1 54  ? 24.841 9.039   5.096   0.48 13.32 ?  54  ASN   A HB3  1 
ATOM   1506 H HD21 A ASN   A 1 54  ? 26.977 11.515  5.089   0.52 15.22 ?  54  ASN   A HD21 1 
ATOM   1507 H HD21 B ASN   A 1 54  ? 26.715 11.743  5.178   0.48 13.83 ?  54  ASN   A HD21 1 
ATOM   1508 H HD22 A ASN   A 1 54  ? 25.677 10.988  4.588   0.52 15.22 ?  54  ASN   A HD22 1 
ATOM   1509 H HD22 B ASN   A 1 54  ? 25.478 11.083  4.678   0.48 13.83 ?  54  ASN   A HD22 1 
ATOM   1510 N N    . LYS   A 1 55  ? 23.233 10.122  7.386   1.00 11.76 ?  55  LYS   A N    1 
ATOM   1511 C CA   . LYS   A 1 55  ? 22.656 11.282  8.056   1.00 12.64 ?  55  LYS   A CA   1 
ATOM   1512 C C    . LYS   A 1 55  ? 22.546 11.046  9.558   1.00 12.45 ?  55  LYS   A C    1 
ATOM   1513 O O    . LYS   A 1 55  ? 22.827 11.943  10.367  1.00 13.59 ?  55  LYS   A O    1 
ATOM   1514 C CB   . LYS   A 1 55  ? 21.290 11.594  7.433   1.00 13.83 ?  55  LYS   A CB   1 
ATOM   1515 C CG   . LYS   A 1 55  ? 20.549 12.768  8.053   1.00 16.50 ?  55  LYS   A CG   1 
ATOM   1516 C CD   . LYS   A 1 55  ? 19.212 13.003  7.335   1.00 18.64 ?  55  LYS   A CD   1 
ATOM   1517 C CE   . LYS   A 1 55  ? 18.394 14.127  7.968   1.00 20.80 ?  55  LYS   A CE   1 
ATOM   1518 N NZ   . LYS   A 1 55  ? 17.016 14.211  7.390   1.00 22.75 ?  55  LYS   A NZ   1 
ATOM   1519 H H    A LYS   A 1 55  ? 22.734 9.789   6.770   0.52 14.11 ?  55  LYS   A H    1 
ATOM   1520 H H    B LYS   A 1 55  ? 22.733 9.766   6.783   0.48 14.11 ?  55  LYS   A H    1 
ATOM   1521 H HA   . LYS   A 1 55  ? 23.235 12.048  7.912   1.00 15.17 ?  55  LYS   A HA   1 
ATOM   1522 H HB2  . LYS   A 1 55  ? 21.420 11.794  6.491   1.00 16.60 ?  55  LYS   A HB2  1 
ATOM   1523 H HB3  . LYS   A 1 55  ? 20.726 10.809  7.520   1.00 16.60 ?  55  LYS   A HB3  1 
ATOM   1524 H HG2  . LYS   A 1 55  ? 20.365 12.571  8.986   1.00 19.80 ?  55  LYS   A HG2  1 
ATOM   1525 H HG3  . LYS   A 1 55  ? 21.091 13.565  7.974   1.00 19.80 ?  55  LYS   A HG3  1 
ATOM   1526 H HD2  . LYS   A 1 55  ? 19.396 13.239  6.411   1.00 22.37 ?  55  LYS   A HD2  1 
ATOM   1527 H HD3  . LYS   A 1 55  ? 18.691 12.186  7.371   1.00 22.37 ?  55  LYS   A HD3  1 
ATOM   1528 H HE2  . LYS   A 1 55  ? 18.320 13.963  8.920   1.00 24.96 ?  55  LYS   A HE2  1 
ATOM   1529 H HE3  . LYS   A 1 55  ? 18.847 14.971  7.808   1.00 24.96 ?  55  LYS   A HE3  1 
ATOM   1530 H HZ1  . LYS   A 1 55  ? 16.498 14.706  7.918   1.00 27.30 ?  55  LYS   A HZ1  1 
ATOM   1531 H HZ2  . LYS   A 1 55  ? 17.045 14.585  6.583   1.00 27.30 ?  55  LYS   A HZ2  1 
ATOM   1532 H HZ3  . LYS   A 1 55  ? 16.663 13.397  7.322   1.00 27.30 ?  55  LYS   A HZ3  1 
ATOM   1533 N N    . ALA   A 1 56  ? 22.147 9.832   9.951   1.00 13.22 ?  56  ALA   A N    1 
ATOM   1534 C CA   . ALA   A 1 56  ? 22.012 9.507   11.367  1.00 13.63 ?  56  ALA   A CA   1 
ATOM   1535 C C    . ALA   A 1 56  ? 23.353 9.545   12.104  1.00 12.76 ?  56  ALA   A C    1 
ATOM   1536 O O    . ALA   A 1 56  ? 23.368 9.726   13.326  1.00 14.16 ?  56  ALA   A O    1 
ATOM   1537 C CB   . ALA   A 1 56  ? 21.305 8.156   11.542  1.00 14.95 ?  56  ALA   A CB   1 
ATOM   1538 H H    . ALA   A 1 56  ? 21.947 9.192   9.418   1.00 15.87 ?  56  ALA   A H    1 
ATOM   1539 H HA   . ALA   A 1 56  ? 21.458 10.172  11.783  1.00 16.36 ?  56  ALA   A HA   1 
ATOM   1540 H HB1  . ALA   A 1 56  ? 21.242 7.953   12.491  1.00 17.94 ?  56  ALA   A HB1  1 
ATOM   1541 H HB2  . ALA   A 1 56  ? 20.415 8.220   11.161  1.00 17.94 ?  56  ALA   A HB2  1 
ATOM   1542 H HB3  . ALA   A 1 56  ? 21.812 7.466   11.089  1.00 17.94 ?  56  ALA   A HB3  1 
ATOM   1543 N N    . THR   A 1 57  ? 24.476 9.340   11.397  1.00 12.80 ?  57  THR   A N    1 
ATOM   1544 C CA   . THR   A 1 57  ? 25.815 9.468   11.983  1.00 12.56 ?  57  THR   A CA   1 
ATOM   1545 C C    . THR   A 1 57  ? 26.373 10.889  11.909  1.00 12.85 ?  57  THR   A C    1 
ATOM   1546 O O    . THR   A 1 57  ? 27.560 11.095  12.203  1.00 13.46 ?  57  THR   A O    1 
ATOM   1547 C CB   . THR   A 1 57  ? 26.822 8.513   11.315  1.00 11.81 ?  57  THR   A CB   1 
ATOM   1548 O OG1  . THR   A 1 57  ? 27.207 9.010   10.021  1.00 12.15 ?  57  THR   A OG1  1 
ATOM   1549 C CG2  . THR   A 1 57  ? 26.283 7.095   11.219  1.00 12.61 ?  57  THR   A CG2  1 
ATOM   1550 H H    . THR   A 1 57  ? 24.493 9.098   10.566  1.00 15.36 ?  57  THR   A H    1 
ATOM   1551 H HA   . THR   A 1 57  ? 25.767 9.215   12.921  1.00 15.07 ?  57  THR   A HA   1 
ATOM   1552 H HB   . THR   A 1 57  ? 27.621 8.476   11.876  1.00 14.18 ?  57  THR   A HB   1 
ATOM   1553 H HG1  . THR   A 1 57  ? 26.526 9.088   9.535   1.00 14.58 ?  57  THR   A HG1  1 
ATOM   1554 H HG21 . THR   A 1 57  ? 26.960 6.501   10.856  1.00 15.14 ?  57  THR   A HG21 1 
ATOM   1555 H HG22 . THR   A 1 57  ? 26.023 6.772   12.097  1.00 15.14 ?  57  THR   A HG22 1 
ATOM   1556 H HG23 . THR   A 1 57  ? 25.507 7.072   10.637  1.00 15.14 ?  57  THR   A HG23 1 
ATOM   1557 N N    . ASN   A 1 58  ? 25.560 11.862  11.503  1.00 13.56 ?  58  ASN   A N    1 
ATOM   1558 C CA   . ASN   A 1 58  ? 26.030 13.241  11.416  1.00 14.32 ?  58  ASN   A CA   1 
ATOM   1559 C C    . ASN   A 1 58  ? 27.179 13.367  10.415  1.00 12.95 ?  58  ASN   A C    1 
ATOM   1560 O O    . ASN   A 1 58  ? 28.063 14.209  10.569  1.00 13.94 ?  58  ASN   A O    1 
ATOM   1561 C CB   . ASN   A 1 58  ? 26.404 13.767  12.814  1.00 16.65 ?  58  ASN   A CB   1 
ATOM   1562 C CG   . ASN   A 1 58  ? 26.802 15.227  12.827  1.00 21.29 ?  58  ASN   A CG   1 
ATOM   1563 O OD1  . ASN   A 1 58  ? 26.173 16.058  12.184  1.00 22.70 ?  58  ASN   A OD1  1 
ATOM   1564 N ND2  . ASN   A 1 58  ? 27.850 15.551  13.586  1.00 22.38 ?  58  ASN   A ND2  1 
ATOM   1565 H H    . ASN   A 1 58  ? 24.733 11.742  11.274  1.00 16.28 ?  58  ASN   A H    1 
ATOM   1566 H HA   . ASN   A 1 58  ? 25.293 13.780  11.093  1.00 17.19 ?  58  ASN   A HA   1 
ATOM   1567 H HB2  . ASN   A 1 58  ? 25.632 13.659  13.409  1.00 19.98 ?  58  ASN   A HB2  1 
ATOM   1568 H HB3  . ASN   A 1 58  ? 27.147 13.256  13.162  1.00 19.98 ?  58  ASN   A HB3  1 
ATOM   1569 H HD21 . ASN   A 1 58  ? 28.107 16.369  13.629  1.00 26.86 ?  58  ASN   A HD21 1 
ATOM   1570 H HD22 . ASN   A 1 58  ? 28.255 14.942  14.031  1.00 26.86 ?  58  ASN   A HD22 1 
ATOM   1571 N N    . ASN   A 1 59  ? 27.158 12.550  9.356   1.00 12.02 ?  59  ASN   A N    1 
ATOM   1572 C CA   . ASN   A 1 59  ? 28.142 12.524  8.267   1.00 11.49 ?  59  ASN   A CA   1 
ATOM   1573 C C    . ASN   A 1 59  ? 29.459 11.838  8.659   1.00 11.47 ?  59  ASN   A C    1 
ATOM   1574 O O    . ASN   A 1 59  ? 30.377 11.795  7.830   1.00 12.12 ?  59  ASN   A O    1 
ATOM   1575 C CB   . ASN   A 1 59  ? 28.444 13.910  7.653   1.00 11.80 ?  59  ASN   A CB   1 
ATOM   1576 C CG   . ASN   A 1 59  ? 28.799 13.826  6.178   1.00 12.37 ?  59  ASN   A CG   1 
ATOM   1577 O OD1  . ASN   A 1 59  ? 28.086 13.209  5.385   1.00 12.76 ?  59  ASN   A OD1  1 
ATOM   1578 N ND2  . ASN   A 1 59  ? 29.895 14.478  5.792   1.00 13.23 ?  59  ASN   A ND2  1 
ATOM   1579 H H    . ASN   A 1 59  ? 26.532 11.962  9.230   1.00 14.43 ?  59  ASN   A H    1 
ATOM   1580 H HA   . ASN   A 1 59  ? 27.767 11.998  7.554   1.00 13.79 ?  59  ASN   A HA   1 
ATOM   1581 H HB2  . ASN   A 1 59  ? 27.663 14.477  7.736   1.00 14.16 ?  59  ASN   A HB2  1 
ATOM   1582 H HB3  . ASN   A 1 59  ? 29.198 14.313  8.112   1.00 14.16 ?  59  ASN   A HB3  1 
ATOM   1583 H HD21 . ASN   A 1 59  ? 30.136 14.467  4.963   1.00 15.87 ?  59  ASN   A HD21 1 
ATOM   1584 H HD22 . ASN   A 1 59  ? 30.371 14.905  6.368   1.00 15.87 ?  59  ASN   A HD22 1 
ATOM   1585 N N    . ALA   A 1 60  ? 29.581 11.287  9.867   1.00 11.66 ?  60  ALA   A N    1 
ATOM   1586 C CA   . ALA   A 1 60  ? 30.815 10.602  10.228  1.00 11.63 ?  60  ALA   A CA   1 
ATOM   1587 C C    . ALA   A 1 60  ? 31.044 9.364   9.367   1.00 11.92 ?  60  ALA   A C    1 
ATOM   1588 O O    . ALA   A 1 60  ? 32.190 9.035   9.042   1.00 12.77 ?  60  ALA   A O    1 
ATOM   1589 C CB   . ALA   A 1 60  ? 30.798 10.243  11.710  1.00 12.59 ?  60  ALA   A CB   1 
ATOM   1590 H H    . ALA   A 1 60  ? 28.977 11.294  10.481  1.00 14.00 ?  60  ALA   A H    1 
ATOM   1591 H HA   . ALA   A 1 60  ? 31.561 11.208  10.083  1.00 13.95 ?  60  ALA   A HA   1 
ATOM   1592 H HB1  . ALA   A 1 60  ? 31.627 9.794   11.940  1.00 15.11 ?  60  ALA   A HB1  1 
ATOM   1593 H HB2  . ALA   A 1 60  ? 30.715 11.062  12.234  1.00 15.11 ?  60  ALA   A HB2  1 
ATOM   1594 H HB3  . ALA   A 1 60  ? 30.044 9.663   11.890  1.00 15.11 ?  60  ALA   A HB3  1 
ATOM   1595 N N    . MET   A 1 61  ? 29.977 8.664   8.987   1.00 11.34 ?  61  MET   A N    1 
ATOM   1596 C CA   . MET   A 1 61  ? 30.119 7.528   8.083   1.00 10.97 ?  61  MET   A CA   1 
ATOM   1597 C C    . MET   A 1 61  ? 30.757 7.946   6.756   1.00 11.04 ?  61  MET   A C    1 
ATOM   1598 O O    . MET   A 1 61  ? 31.652 7.261   6.246   1.00 11.94 ?  61  MET   A O    1 
ATOM   1599 C CB   . MET   A 1 61  ? 28.756 6.867   7.873   1.00 11.35 ?  61  MET   A CB   1 
ATOM   1600 C CG   . MET   A 1 61  ? 28.760 5.688   6.905   1.00 12.17 ?  61  MET   A CG   1 
ATOM   1601 S SD   . MET   A 1 61  ? 27.140 4.945   6.682   1.00 12.79 ?  61  MET   A SD   1 
ATOM   1602 C CE   . MET   A 1 61  ? 27.001 4.067   8.244   1.00 14.70 ?  61  MET   A CE   1 
ATOM   1603 H H    . MET   A 1 61  ? 29.170 8.825   9.234   1.00 13.61 ?  61  MET   A H    1 
ATOM   1604 H HA   . MET   A 1 61  ? 30.694 6.866   8.505   1.00 13.16 ?  61  MET   A HA   1 
ATOM   1605 H HB2  . MET   A 1 61  ? 28.429 6.542   8.728   1.00 13.62 ?  61  MET   A HB2  1 
ATOM   1606 H HB3  . MET   A 1 61  ? 28.138 7.528   7.522   1.00 13.62 ?  61  MET   A HB3  1 
ATOM   1607 H HG2  . MET   A 1 61  ? 29.059 5.985   6.033   1.00 14.60 ?  61  MET   A HG2  1 
ATOM   1608 H HG3  . MET   A 1 61  ? 29.356 4.999   7.244   1.00 14.60 ?  61  MET   A HG3  1 
ATOM   1609 H HE1  . MET   A 1 61  ? 26.157 3.586   8.264   1.00 17.64 ?  61  MET   A HE1  1 
ATOM   1610 H HE2  . MET   A 1 61  ? 27.739 3.449   8.331   1.00 17.64 ?  61  MET   A HE2  1 
ATOM   1611 H HE3  . MET   A 1 61  ? 27.023 4.713   8.975   1.00 17.64 ?  61  MET   A HE3  1 
ATOM   1612 N N    . GLN   A 1 62  ? 30.322 9.076   6.192   1.00 11.22 ?  62  GLN   A N    1 
ATOM   1613 C CA   . GLN   A 1 62  ? 30.888 9.548   4.931   1.00 10.96 ?  62  GLN   A CA   1 
ATOM   1614 C C    . GLN   A 1 62  ? 32.358 9.927   5.081   1.00 11.27 ?  62  GLN   A C    1 
ATOM   1615 O O    . GLN   A 1 62  ? 33.177 9.598   4.213   1.00 11.99 ?  62  GLN   A O    1 
ATOM   1616 C CB   . GLN   A 1 62  ? 30.092 10.730  4.386   1.00 11.21 ?  62  GLN   A CB   1 
ATOM   1617 C CG   . GLN   A 1 62  ? 30.488 11.089  2.965   1.00 11.90 ?  62  GLN   A CG   1 
ATOM   1618 C CD   . GLN   A 1 62  ? 30.160 9.960   2.006   1.00 11.71 ?  62  GLN   A CD   1 
ATOM   1619 O OE1  . GLN   A 1 62  ? 28.986 9.640   1.790   1.00 12.48 ?  62  GLN   A OE1  1 
ATOM   1620 N NE2  . GLN   A 1 62  ? 31.185 9.292   1.485   1.00 12.15 ?  62  GLN   A NE2  1 
ATOM   1621 H H    . GLN   A 1 62  ? 29.703 9.576   6.522   1.00 13.46 ?  62  GLN   A H    1 
ATOM   1622 H HA   . GLN   A 1 62  ? 30.838 8.827   4.289   1.00 13.16 ?  62  GLN   A HA   1 
ATOM   1623 H HB2  . GLN   A 1 62  ? 29.151 10.510  4.397   1.00 13.46 ?  62  GLN   A HB2  1 
ATOM   1624 H HB3  . GLN   A 1 62  ? 30.259 11.508  4.950   1.00 13.46 ?  62  GLN   A HB3  1 
ATOM   1625 H HG2  . GLN   A 1 62  ? 29.992 11.871  2.684   1.00 14.29 ?  62  GLN   A HG2  1 
ATOM   1626 H HG3  . GLN   A 1 62  ? 31.440 11.258  2.924   1.00 14.29 ?  62  GLN   A HG3  1 
ATOM   1627 H HE21 . GLN   A 1 62  ? 31.994 9.531   1.670   1.00 14.57 ?  62  GLN   A HE21 1 
ATOM   1628 H HE22 . GLN   A 1 62  ? 31.049 8.640   0.942   1.00 14.57 ?  62  GLN   A HE22 1 
ATOM   1629 N N    . VAL   A 1 63  ? 32.720 10.599  6.179   1.00 12.21 ?  63  VAL   A N    1 
ATOM   1630 C CA   . VAL   A 1 63  ? 34.116 10.984  6.410   1.00 12.81 ?  63  VAL   A CA   1 
ATOM   1631 C C    . VAL   A 1 63  ? 35.003 9.744   6.485   1.00 12.10 ?  63  VAL   A C    1 
ATOM   1632 O O    . VAL   A 1 63  ? 36.058 9.668   5.841   1.00 12.74 ?  63  VAL   A O    1 
ATOM   1633 C CB   . VAL   A 1 63  ? 34.212 11.854  7.678   1.00 14.49 ?  63  VAL   A CB   1 
ATOM   1634 C CG1  . VAL   A 1 63  ? 35.662 12.068  8.093   1.00 16.45 ?  63  VAL   A CG1  1 
ATOM   1635 C CG2  . VAL   A 1 63  ? 33.511 13.205  7.442   1.00 13.97 ?  63  VAL   A CG2  1 
ATOM   1636 H H    . VAL   A 1 63  ? 32.176 10.841  6.804   1.00 14.66 ?  63  VAL   A H    1 
ATOM   1637 H HA   . VAL   A 1 63  ? 34.416 11.521  5.661   1.00 15.38 ?  63  VAL   A HA   1 
ATOM   1638 H HB   . VAL   A 1 63  ? 33.751 11.404  8.405   1.00 17.39 ?  63  VAL   A HB   1 
ATOM   1639 H HG11 . VAL   A 1 63  ? 35.696 12.796  8.728   1.00 19.74 ?  63  VAL   A HG11 1 
ATOM   1640 H HG12 . VAL   A 1 63  ? 35.992 11.254  8.500   1.00 19.74 ?  63  VAL   A HG12 1 
ATOM   1641 H HG13 . VAL   A 1 63  ? 36.179 12.286  7.305   1.00 19.74 ?  63  VAL   A HG13 1 
ATOM   1642 H HG21 . VAL   A 1 63  ? 33.586 13.743  8.247   1.00 16.76 ?  63  VAL   A HG21 1 
ATOM   1643 H HG22 . VAL   A 1 63  ? 33.944 13.658  6.702   1.00 16.76 ?  63  VAL   A HG22 1 
ATOM   1644 H HG23 . VAL   A 1 63  ? 32.578 13.048  7.235   1.00 16.76 ?  63  VAL   A HG23 1 
ATOM   1645 N N    . GLU   A 1 64  ? 34.568 8.743   7.253   1.00 12.04 ?  64  GLU   A N    1 
ATOM   1646 C CA   . GLU   A 1 64  ? 35.333 7.503   7.358   1.00 11.85 ?  64  GLU   A CA   1 
ATOM   1647 C C    . GLU   A 1 64  ? 35.436 6.815   6.002   1.00 11.33 ?  64  GLU   A C    1 
ATOM   1648 O O    . GLU   A 1 64  ? 36.490 6.261   5.634   1.00 12.52 ?  64  GLU   A O    1 
ATOM   1649 C CB   . GLU   A 1 64  ? 34.643 6.595   8.379   1.00 12.63 ?  64  GLU   A CB   1 
ATOM   1650 C CG   . GLU   A 1 64  ? 35.297 5.249   8.550   1.00 14.03 ?  64  GLU   A CG   1 
ATOM   1651 C CD   . GLU   A 1 64  ? 34.413 4.251   9.269   1.00 14.86 ?  64  GLU   A CD   1 
ATOM   1652 O OE1  . GLU   A 1 64  ? 33.179 4.339   9.123   1.00 15.22 ?  64  GLU   A OE1  1 
ATOM   1653 O OE2  . GLU   A 1 64  ? 34.971 3.355   9.951   1.00 14.93 -1 64  GLU   A OE2  1 
ATOM   1654 H H    . GLU   A 1 64  ? 33.837 8.755   7.709   1.00 14.44 ?  64  GLU   A H    1 
ATOM   1655 H HA   . GLU   A 1 64  ? 36.228 7.707   7.679   1.00 14.22 ?  64  GLU   A HA   1 
ATOM   1656 H HB2  . GLU   A 1 64  ? 34.651 7.044   9.247   1.00 15.16 ?  64  GLU   A HB2  1 
ATOM   1657 H HB3  . GLU   A 1 64  ? 33.726 6.460   8.097   1.00 15.16 ?  64  GLU   A HB3  1 
ATOM   1658 H HG2  . GLU   A 1 64  ? 35.510 4.879   7.675   1.00 16.84 ?  64  GLU   A HG2  1 
ATOM   1659 H HG3  . GLU   A 1 64  ? 36.110 5.356   9.065   1.00 16.84 ?  64  GLU   A HG3  1 
ATOM   1660 N N    . SER   A 1 65  ? 34.320 6.813   5.261   1.00 11.44 ?  65  SER   A N    1 
ATOM   1661 C CA   . SER   A 1 65  ? 34.256 6.154   3.963   1.00 11.53 ?  65  SER   A CA   1 
ATOM   1662 C C    . SER   A 1 65  ? 35.191 6.806   2.955   1.00 11.84 ?  65  SER   A C    1 
ATOM   1663 O O    . SER   A 1 65  ? 35.845 6.111   2.166   1.00 12.77 ?  65  SER   A O    1 
ATOM   1664 C CB   . SER   A 1 65  ? 32.818 6.173   3.428   1.00 11.81 ?  65  SER   A CB   1 
ATOM   1665 O OG   . SER   A 1 65  ? 31.971 5.343   4.209   1.00 12.34 ?  65  SER   A OG   1 
ATOM   1666 H H    . SER   A 1 65  ? 33.584 7.203   5.494   1.00 13.73 ?  65  SER   A H    1 
ATOM   1667 H HA   . SER   A 1 65  ? 34.527 5.232   4.069   1.00 13.83 ?  65  SER   A HA   1 
ATOM   1668 H HB2  . SER   A 1 65  ? 32.482 7.084   3.459   1.00 14.18 ?  65  SER   A HB2  1 
ATOM   1669 H HB3  . SER   A 1 65  ? 32.821 5.852   2.515   1.00 14.18 ?  65  SER   A HB3  1 
ATOM   1670 H HG   . SER   A 1 65  ? 31.968 5.611   5.010   1.00 14.81 ?  65  SER   A HG   1 
ATOM   1671 N N    . ASP   A 1 66  ? 35.273 8.139   2.957   1.00 11.72 ?  66  ASP   A N    1 
ATOM   1672 C CA   . ASP   A 1 66  ? 36.148 8.819   2.008   1.00 12.98 ?  66  ASP   A CA   1 
ATOM   1673 C C    . ASP   A 1 66  ? 37.609 8.469   2.269   1.00 12.80 ?  66  ASP   A C    1 
ATOM   1674 O O    . ASP   A 1 66  ? 38.400 8.310   1.329   1.00 13.51 ?  66  ASP   A O    1 
ATOM   1675 C CB   . ASP   A 1 66  ? 35.933 10.335  2.072   1.00 14.85 ?  66  ASP   A CB   1 
ATOM   1676 C CG   . ASP   A 1 66  ? 34.595 10.793  1.472   1.00 17.01 ?  66  ASP   A CG   1 
ATOM   1677 O OD1  . ASP   A 1 66  ? 33.902 10.006  0.796   1.00 17.27 ?  66  ASP   A OD1  1 
ATOM   1678 O OD2  . ASP   A 1 66  ? 34.286 11.988  1.641   1.00 20.28 -1 66  ASP   A OD2  1 
ATOM   1679 H H    . ASP   A 1 66  ? 34.830 8.666   3.480   1.00 14.06 ?  66  ASP   A H    1 
ATOM   1680 H HA   . ASP   A 1 66  ? 35.929 8.520   1.110   1.00 15.58 ?  66  ASP   A HA   1 
ATOM   1681 H HB2  . ASP   A 1 66  ? 35.948 10.614  2.995   1.00 17.82 ?  66  ASP   A HB2  1 
ATOM   1682 H HB3  . ASP   A 1 66  ? 36.645 10.770  1.576   1.00 17.82 ?  66  ASP   A HB3  1 
ATOM   1683 N N    A ASP   A 1 67  ? 37.994 8.361   3.539   0.52 13.08 ?  67  ASP   A N    1 
ATOM   1684 N N    B ASP   A 1 67  ? 37.983 8.327   3.544   0.48 13.33 ?  67  ASP   A N    1 
ATOM   1685 C CA   A ASP   A 1 67  ? 39.347 7.907   3.839   0.52 13.65 ?  67  ASP   A CA   1 
ATOM   1686 C CA   B ASP   A 1 67  ? 39.342 7.905   3.878   0.48 14.12 ?  67  ASP   A CA   1 
ATOM   1687 C C    A ASP   A 1 67  ? 39.562 6.477   3.349   0.52 13.07 ?  67  ASP   A C    1 
ATOM   1688 C C    B ASP   A 1 67  ? 39.599 6.454   3.477   0.48 13.94 ?  67  ASP   A C    1 
ATOM   1689 O O    A ASP   A 1 67  ? 40.595 6.173   2.741   0.52 13.39 ?  67  ASP   A O    1 
ATOM   1690 O O    B ASP   A 1 67  ? 40.719 6.111   3.081   0.48 14.81 ?  67  ASP   A O    1 
ATOM   1691 C CB   A ASP   A 1 67  ? 39.628 8.042   5.336   0.52 14.39 ?  67  ASP   A CB   1 
ATOM   1692 C CB   B ASP   A 1 67  ? 39.597 8.129   5.371   0.48 14.61 ?  67  ASP   A CB   1 
ATOM   1693 C CG   A ASP   A 1 67  ? 40.944 7.399   5.740   0.52 14.82 ?  67  ASP   A CG   1 
ATOM   1694 C CG   B ASP   A 1 67  ? 40.858 7.450   5.858   0.48 14.98 ?  67  ASP   A CG   1 
ATOM   1695 O OD1  A ASP   A 1 67  ? 42.015 7.932   5.352   0.52 15.80 ?  67  ASP   A OD1  1 
ATOM   1696 O OD1  B ASP   A 1 67  ? 40.836 6.209   6.030   0.48 15.54 ?  67  ASP   A OD1  1 
ATOM   1697 O OD2  A ASP   A 1 67  ? 40.898 6.359   6.443   0.52 14.57 -1 67  ASP   A OD2  1 
ATOM   1698 O OD2  B ASP   A 1 67  ? 41.871 8.160   6.067   0.48 14.53 -1 67  ASP   A OD2  1 
ATOM   1699 H H    A ASP   A 1 67  ? 37.510 8.547   4.225   0.52 15.69 ?  67  ASP   A H    1 
ATOM   1700 H H    B ASP   A 1 67  ? 37.476 8.473   4.224   0.48 15.99 ?  67  ASP   A H    1 
ATOM   1701 H HA   A ASP   A 1 67  ? 39.981 8.483   3.373   0.52 16.37 ?  67  ASP   A HA   1 
ATOM   1702 H HA   B ASP   A 1 67  ? 39.969 8.469   3.393   0.48 16.95 ?  67  ASP   A HA   1 
ATOM   1703 H HB2  A ASP   A 1 67  ? 39.671 8.988   5.567   0.52 17.27 ?  67  ASP   A HB2  1 
ATOM   1704 H HB2  B ASP   A 1 67  ? 39.699 9.077   5.542   0.48 17.53 ?  67  ASP   A HB2  1 
ATOM   1705 H HB3  A ASP   A 1 67  ? 38.919 7.613   5.833   0.52 17.27 ?  67  ASP   A HB3  1 
ATOM   1706 H HB3  B ASP   A 1 67  ? 38.856 7.773   5.880   0.48 17.53 ?  67  ASP   A HB3  1 
ATOM   1707 N N    . TYR   A 1 68  ? 38.581 5.593   3.569   1.00 13.32 ?  68  TYR   A N    1 
ATOM   1708 C CA   . TYR   A 1 68  ? 38.717 4.209   3.109   1.00 13.36 ?  68  TYR   A CA   1 
ATOM   1709 C C    . TYR   A 1 68  ? 38.950 4.153   1.602   1.00 13.12 ?  68  TYR   A C    1 
ATOM   1710 O O    . TYR   A 1 68  ? 39.836 3.428   1.127   1.00 14.39 ?  68  TYR   A O    1 
ATOM   1711 C CB   . TYR   A 1 68  ? 37.465 3.402   3.486   1.00 13.24 ?  68  TYR   A CB   1 
ATOM   1712 C CG   . TYR   A 1 68  ? 37.487 2.017   2.854   1.00 14.88 ?  68  TYR   A CG   1 
ATOM   1713 C CD1  . TYR   A 1 68  ? 37.021 1.821   1.558   1.00 15.60 ?  68  TYR   A CD1  1 
ATOM   1714 C CD2  . TYR   A 1 68  ? 38.024 0.941   3.520   1.00 17.10 ?  68  TYR   A CD2  1 
ATOM   1715 C CE1  . TYR   A 1 68  ? 37.090 0.608   0.939   1.00 17.34 ?  68  TYR   A CE1  1 
ATOM   1716 C CE2  . TYR   A 1 68  ? 38.096 -0.319  2.900   1.00 17.75 ?  68  TYR   A CE2  1 
ATOM   1717 C CZ   . TYR   A 1 68  ? 37.630 -0.461  1.612   1.00 17.59 ?  68  TYR   A CZ   1 
ATOM   1718 O OH   . TYR   A 1 68  ? 37.714 -1.677  0.978   1.00 20.02 ?  68  TYR   A OH   1 
ATOM   1719 H H    A TYR   A 1 68  ? 37.842 5.778   3.969   0.52 15.98 ?  68  TYR   A H    1 
ATOM   1720 H H    B TYR   A 1 68  ? 37.810 5.794   3.895   0.48 15.98 ?  68  TYR   A H    1 
ATOM   1721 H HA   . TYR   A 1 68  ? 39.479 3.811   3.548   1.00 16.03 ?  68  TYR   A HA   1 
ATOM   1722 H HB2  . TYR   A 1 68  ? 37.430 3.294   4.451   1.00 15.89 ?  68  TYR   A HB2  1 
ATOM   1723 H HB3  . TYR   A 1 68  ? 36.671 3.869   3.175   1.00 15.89 ?  68  TYR   A HB3  1 
ATOM   1724 H HD1  . TYR   A 1 68  ? 36.667 2.551   1.094   1.00 18.72 ?  68  TYR   A HD1  1 
ATOM   1725 H HD2  . TYR   A 1 68  ? 38.369 1.046   4.376   1.00 20.52 ?  68  TYR   A HD2  1 
ATOM   1726 H HE1  . TYR   A 1 68  ? 36.769 0.507   0.073   1.00 20.81 ?  68  TYR   A HE1  1 
ATOM   1727 H HE2  . TYR   A 1 68  ? 38.474 -1.045  3.338   1.00 21.29 ?  68  TYR   A HE2  1 
ATOM   1728 H HH   . TYR   A 1 68  ? 38.056 -2.242  1.489   1.00 24.02 ?  68  TYR   A HH   1 
ATOM   1729 N N    . ILE   A 1 69  ? 38.173 4.922   0.829   1.00 12.66 ?  69  ILE   A N    1 
ATOM   1730 C CA   . ILE   A 1 69  ? 38.327 4.916   -0.626  1.00 12.59 ?  69  ILE   A CA   1 
ATOM   1731 C C    . ILE   A 1 69  ? 39.670 5.512   -1.040  1.00 12.94 ?  69  ILE   A C    1 
ATOM   1732 O O    . ILE   A 1 69  ? 40.318 5.024   -1.973  1.00 13.96 ?  69  ILE   A O    1 
ATOM   1733 C CB   . ILE   A 1 69  ? 37.142 5.643   -1.298  1.00 13.44 ?  69  ILE   A CB   1 
ATOM   1734 C CG1  . ILE   A 1 69  ? 35.818 4.919   -1.022  1.00 13.91 ?  69  ILE   A CG1  1 
ATOM   1735 C CG2  . ILE   A 1 69  ? 37.396 5.813   -2.804  1.00 15.00 ?  69  ILE   A CG2  1 
ATOM   1736 C CD1  . ILE   A 1 69  ? 35.629 3.645   -1.813  1.00 14.84 ?  69  ILE   A CD1  1 
ATOM   1737 H H    . ILE   A 1 69  ? 37.564 5.457   1.119   1.00 15.19 ?  69  ILE   A H    1 
ATOM   1738 H HA   . ILE   A 1 69  ? 38.312 3.995   -0.930  1.00 15.11 ?  69  ILE   A HA   1 
ATOM   1739 H HB   . ILE   A 1 69  ? 37.079 6.526   -0.910  1.00 16.13 ?  69  ILE   A HB   1 
ATOM   1740 H HG12 . ILE   A 1 69  ? 35.778 4.692   -0.076  1.00 16.69 ?  69  ILE   A HG12 1 
ATOM   1741 H HG13 . ILE   A 1 69  ? 35.085 5.520   -1.237  1.00 16.69 ?  69  ILE   A HG13 1 
ATOM   1742 H HG21 . ILE   A 1 69  ? 36.552 6.028   -3.243  1.00 18.00 ?  69  ILE   A HG21 1 
ATOM   1743 H HG22 . ILE   A 1 69  ? 38.024 6.541   -2.941  1.00 18.00 ?  69  ILE   A HG22 1 
ATOM   1744 H HG23 . ILE   A 1 69  ? 37.751 4.990   -3.166  1.00 18.00 ?  69  ILE   A HG23 1 
ATOM   1745 H HD11 . ILE   A 1 69  ? 34.842 3.185   -1.482  1.00 17.80 ?  69  ILE   A HD11 1 
ATOM   1746 H HD12 . ILE   A 1 69  ? 35.508 3.872   -2.749  1.00 17.80 ?  69  ILE   A HD12 1 
ATOM   1747 H HD13 . ILE   A 1 69  ? 36.411 3.086   -1.704  1.00 17.80 ?  69  ILE   A HD13 1 
ATOM   1748 N N    . ALA   A 1 70  ? 40.086 6.589   -0.386  1.00 14.26 ?  70  ALA   A N    1 
ATOM   1749 C CA   . ALA   A 1 70  ? 41.375 7.187   -0.723  1.00 15.65 ?  70  ALA   A CA   1 
ATOM   1750 C C    . ALA   A 1 70  ? 42.517 6.196   -0.536  1.00 16.76 ?  70  ALA   A C    1 
ATOM   1751 O O    . ALA   A 1 70  ? 43.507 6.245   -1.271  1.00 18.86 ?  70  ALA   A O    1 
ATOM   1752 C CB   . ALA   A 1 70  ? 41.598 8.449   0.116   1.00 16.38 ?  70  ALA   A CB   1 
ATOM   1753 H H    . ALA   A 1 70  ? 39.642 7.004   0.220   1.00 17.11 ?  70  ALA   A H    1 
ATOM   1754 H HA   . ALA   A 1 70  ? 41.363 7.461   -1.661  1.00 18.78 ?  70  ALA   A HA   1 
ATOM   1755 H HB1  . ALA   A 1 70  ? 42.466 8.826   -0.111  1.00 19.66 ?  70  ALA   A HB1  1 
ATOM   1756 H HB2  . ALA   A 1 70  ? 40.900 9.089   -0.076  1.00 19.66 ?  70  ALA   A HB2  1 
ATOM   1757 H HB3  . ALA   A 1 70  ? 41.582 8.205   1.054   1.00 19.66 ?  70  ALA   A HB3  1 
ATOM   1758 N N    . THR   A 1 71  ? 42.400 5.288   0.424   1.00 15.58 ?  71  THR   A N    1 
ATOM   1759 C CA   . THR   A 1 71  ? 43.442 4.300   0.685   1.00 18.45 ?  71  THR   A CA   1 
ATOM   1760 C C    . THR   A 1 71  ? 43.323 3.066   -0.198  1.00 18.03 ?  71  THR   A C    1 
ATOM   1761 O O    . THR   A 1 71  ? 44.340 2.522   -0.649  1.00 20.23 ?  71  THR   A O    1 
ATOM   1762 C CB   . THR   A 1 71  ? 43.362 3.859   2.147   1.00 21.14 ?  71  THR   A CB   1 
ATOM   1763 O OG1  . THR   A 1 71  ? 43.628 4.982   2.994   1.00 23.20 ?  71  THR   A OG1  1 
ATOM   1764 C CG2  . THR   A 1 71  ? 44.352 2.735   2.443   1.00 22.97 ?  71  THR   A CG2  1 
ATOM   1765 H H    . THR   A 1 71  ? 41.713 5.215   0.935   1.00 18.70 ?  71  THR   A H    1 
ATOM   1766 H HA   . THR   A 1 71  ? 44.309 4.700   0.524   1.00 22.14 ?  71  THR   A HA   1 
ATOM   1767 H HB   . THR   A 1 71  ? 42.469 3.530   2.328   1.00 25.37 ?  71  THR   A HB   1 
ATOM   1768 H HG1  . THR   A 1 71  ? 43.064 5.588   2.847   1.00 27.84 ?  71  THR   A HG1  1 
ATOM   1769 H HG21 . THR   A 1 71  ? 44.489 2.663   3.401   1.00 27.57 ?  71  THR   A HG21 1 
ATOM   1770 H HG22 . THR   A 1 71  ? 44.014 1.890   2.110   1.00 27.57 ?  71  THR   A HG22 1 
ATOM   1771 H HG23 . THR   A 1 71  ? 45.206 2.923   2.020   1.00 27.57 ?  71  THR   A HG23 1 
ATOM   1772 N N    . ASN   A 1 72  ? 42.098 2.587   -0.431  1.00 16.37 ?  72  ASN   A N    1 
ATOM   1773 C CA   . ASN   A 1 72  ? 41.876 1.259   -0.995  1.00 16.25 ?  72  ASN   A CA   1 
ATOM   1774 C C    . ASN   A 1 72  ? 41.262 1.251   -2.385  1.00 16.25 ?  72  ASN   A C    1 
ATOM   1775 O O    . ASN   A 1 72  ? 41.274 0.201   -3.037  1.00 17.16 ?  72  ASN   A O    1 
ATOM   1776 C CB   . ASN   A 1 72  ? 40.970 0.446   -0.063  1.00 17.17 ?  72  ASN   A CB   1 
ATOM   1777 C CG   . ASN   A 1 72  ? 41.574 0.280   1.301   1.00 17.71 ?  72  ASN   A CG   1 
ATOM   1778 O OD1  . ASN   A 1 72  ? 41.130 0.879   2.276   1.00 20.17 ?  72  ASN   A OD1  1 
ATOM   1779 N ND2  . ASN   A 1 72  ? 42.617 -0.504  1.372   1.00 18.50 ?  72  ASN   A ND2  1 
ATOM   1780 H H    . ASN   A 1 72  ? 41.367 3.017   -0.271  1.00 19.64 ?  72  ASN   A H    1 
ATOM   1781 H HA   . ASN   A 1 72  ? 42.723 0.801   -1.055  1.00 19.49 ?  72  ASN   A HA   1 
ATOM   1782 H HB2  . ASN   A 1 72  ? 40.115 0.901   0.027   1.00 20.60 ?  72  ASN   A HB2  1 
ATOM   1783 H HB3  . ASN   A 1 72  ? 40.835 -0.438  -0.443  1.00 20.60 ?  72  ASN   A HB3  1 
ATOM   1784 H HD21 . ASN   A 1 72  ? 43.004 -0.628  2.130   1.00 22.20 ?  72  ASN   A HD21 1 
ATOM   1785 H HD22 . ASN   A 1 72  ? 42.909 -0.896  0.668   1.00 22.20 ?  72  ASN   A HD22 1 
ATOM   1786 N N    . GLY   A 1 73  ? 40.716 2.367   -2.852  1.00 15.39 ?  73  GLY   A N    1 
ATOM   1787 C CA   . GLY   A 1 73  ? 39.994 2.379   -4.100  1.00 15.43 ?  73  GLY   A CA   1 
ATOM   1788 C C    . GLY   A 1 73  ? 38.597 1.810   -3.930  1.00 14.26 ?  73  GLY   A C    1 
ATOM   1789 O O    . GLY   A 1 73  ? 38.202 1.374   -2.843  1.00 14.90 ?  73  GLY   A O    1 
ATOM   1790 H H    . GLY   A 1 73  ? 40.748 3.141   -2.464  1.00 18.46 ?  73  GLY   A H    1 
ATOM   1791 H HA2  . GLY   A 1 73  ? 39.920 3.295   -4.427  1.00 18.51 ?  73  GLY   A HA2  1 
ATOM   1792 H HA3  . GLY   A 1 73  ? 40.471 1.856   -4.761  1.00 18.51 ?  73  GLY   A HA3  1 
ATOM   1793 N N    . PRO   A 1 74  ? 37.819 1.820   -5.011  1.00 15.00 ?  74  PRO   A N    1 
ATOM   1794 C CA   . PRO   A 1 74  ? 36.416 1.397   -4.928  1.00 14.99 ?  74  PRO   A CA   1 
ATOM   1795 C C    . PRO   A 1 74  ? 36.253 -0.086  -4.619  1.00 14.27 ?  74  PRO   A C    1 
ATOM   1796 O O    . PRO   A 1 74  ? 37.121 -0.916  -4.899  1.00 15.33 ?  74  PRO   A O    1 
ATOM   1797 C CB   . PRO   A 1 74  ? 35.868 1.710   -6.327  1.00 16.80 ?  74  PRO   A CB   1 
ATOM   1798 C CG   . PRO   A 1 74  ? 36.843 2.647   -6.950  1.00 20.56 ?  74  PRO   A CG   1 
ATOM   1799 C CD   . PRO   A 1 74  ? 38.170 2.317   -6.352  1.00 17.12 ?  74  PRO   A CD   1 
ATOM   1800 H HA   . PRO   A 1 74  ? 35.940 1.927   -4.266  1.00 17.99 ?  74  PRO   A HA   1 
ATOM   1801 H HB2  . PRO   A 1 74  ? 35.800 0.888   -6.840  1.00 20.16 ?  74  PRO   A HB2  1 
ATOM   1802 H HB3  . PRO   A 1 74  ? 34.993 2.130   -6.247  1.00 20.16 ?  74  PRO   A HB3  1 
ATOM   1803 H HG2  . PRO   A 1 74  ? 36.862 2.512   -7.912  1.00 24.67 ?  74  PRO   A HG2  1 
ATOM   1804 H HG3  . PRO   A 1 74  ? 36.601 3.563   -6.742  1.00 24.67 ?  74  PRO   A HG3  1 
ATOM   1805 H HD2  . PRO   A 1 74  ? 38.617 1.617   -6.868  1.00 20.54 ?  74  PRO   A HD2  1 
ATOM   1806 H HD3  . PRO   A 1 74  ? 38.725 3.111   -6.294  1.00 20.54 ?  74  PRO   A HD3  1 
ATOM   1807 N N    . LEU   A 1 75  ? 35.099 -0.409  -4.040  1.00 13.17 ?  75  LEU   A N    1 
ATOM   1808 C CA   . LEU   A 1 75  ? 34.704 -1.800  -3.899  1.00 12.38 ?  75  LEU   A CA   1 
ATOM   1809 C C    . LEU   A 1 75  ? 34.333 -2.375  -5.261  1.00 12.65 ?  75  LEU   A C    1 
ATOM   1810 O O    . LEU   A 1 75  ? 34.183 -1.663  -6.252  1.00 14.34 ?  75  LEU   A O    1 
ATOM   1811 C CB   . LEU   A 1 75  ? 33.507 -1.941  -2.960  1.00 12.79 ?  75  LEU   A CB   1 
ATOM   1812 C CG   . LEU   A 1 75  ? 33.704 -1.506  -1.514  1.00 14.20 ?  75  LEU   A CG   1 
ATOM   1813 C CD1  . LEU   A 1 75  ? 32.429 -1.733  -0.722  1.00 15.86 ?  75  LEU   A CD1  1 
ATOM   1814 C CD2  . LEU   A 1 75  ? 34.857 -2.206  -0.853  1.00 18.25 ?  75  LEU   A CD2  1 
ATOM   1815 H H    . LEU   A 1 75  ? 34.524 0.162   -3.731  1.00 15.81 ?  75  LEU   A H    1 
ATOM   1816 H HA   . LEU   A 1 75  ? 35.443 -2.306  -3.542  1.00 14.86 ?  75  LEU   A HA   1 
ATOM   1817 H HB2  . LEU   A 1 75  ? 32.772 -1.421  -3.323  1.00 15.34 ?  75  LEU   A HB2  1 
ATOM   1818 H HB3  . LEU   A 1 75  ? 33.250 -2.880  -2.942  1.00 15.34 ?  75  LEU   A HB3  1 
ATOM   1819 H HG   . LEU   A 1 75  ? 33.897 -0.550  -1.505  1.00 17.04 ?  75  LEU   A HG   1 
ATOM   1820 H HD11 . LEU   A 1 75  ? 32.572 -1.440  0.191   1.00 19.03 ?  75  LEU   A HD11 1 
ATOM   1821 H HD12 . LEU   A 1 75  ? 31.714 -1.215  -1.127  1.00 19.03 ?  75  LEU   A HD12 1 
ATOM   1822 H HD13 . LEU   A 1 75  ? 32.213 -2.674  -0.743  1.00 19.03 ?  75  LEU   A HD13 1 
ATOM   1823 H HD21 . LEU   A 1 75  ? 34.889 -1.946  0.080   1.00 21.89 ?  75  LEU   A HD21 1 
ATOM   1824 H HD22 . LEU   A 1 75  ? 34.727 -3.162  -0.929  1.00 21.89 ?  75  LEU   A HD22 1 
ATOM   1825 H HD23 . LEU   A 1 75  ? 35.683 -1.947  -1.295  1.00 21.89 ?  75  LEU   A HD23 1 
ATOM   1826 N N    . LYS   A 1 76  ? 34.186 -3.697  -5.291  1.00 13.38 ?  76  LYS   A N    1 
ATOM   1827 C CA   . LYS   A 1 76  ? 33.609 -4.416  -6.419  1.00 13.72 ?  76  LYS   A CA   1 
ATOM   1828 C C    . LYS   A 1 76  ? 32.094 -4.501  -6.247  1.00 12.39 ?  76  LYS   A C    1 
ATOM   1829 O O    . LYS   A 1 76  ? 31.594 -4.596  -5.127  1.00 12.77 ?  76  LYS   A O    1 
ATOM   1830 C CB   . LYS   A 1 76  ? 34.147 -5.855  -6.460  1.00 15.48 ?  76  LYS   A CB   1 
ATOM   1831 C CG   . LYS   A 1 76  ? 35.652 -5.977  -6.665  1.00 16.65 ?  76  LYS   A CG   1 
ATOM   1832 C CD   . LYS   A 1 76  ? 36.149 -7.397  -6.473  1.00 18.45 ?  76  LYS   A CD   1 
ATOM   1833 C CE   . LYS   A 1 76  ? 37.655 -7.464  -6.666  1.00 20.91 ?  76  LYS   A CE   1 
ATOM   1834 N NZ   . LYS   A 1 76  ? 38.194 -8.813  -6.449  1.00 21.65 ?  76  LYS   A NZ   1 
ATOM   1835 H H    . LYS   A 1 76  ? 34.417 -4.219  -4.644  1.00 16.06 ?  76  LYS   A H    1 
ATOM   1836 H HA   . LYS   A 1 76  ? 33.816 -3.965  -7.252  1.00 16.47 ?  76  LYS   A HA   1 
ATOM   1837 H HB2  . LYS   A 1 76  ? 33.928 -6.287  -5.622  1.00 18.58 ?  76  LYS   A HB2  1 
ATOM   1838 H HB3  . LYS   A 1 76  ? 33.714 -6.321  -7.192  1.00 18.58 ?  76  LYS   A HB3  1 
ATOM   1839 H HG2  . LYS   A 1 76  ? 35.873 -5.698  -7.567  1.00 19.99 ?  76  LYS   A HG2  1 
ATOM   1840 H HG3  . LYS   A 1 76  ? 36.106 -5.410  -6.020  1.00 19.99 ?  76  LYS   A HG3  1 
ATOM   1841 H HD2  . LYS   A 1 76  ? 35.936 -7.697  -5.574  1.00 22.14 ?  76  LYS   A HD2  1 
ATOM   1842 H HD3  . LYS   A 1 76  ? 35.726 -7.978  -7.129  1.00 22.14 ?  76  LYS   A HD3  1 
ATOM   1843 H HE2  . LYS   A 1 76  ? 37.866 -7.192  -7.571  1.00 25.09 ?  76  LYS   A HE2  1 
ATOM   1844 H HE3  . LYS   A 1 76  ? 38.076 -6.865  -6.030  1.00 25.09 ?  76  LYS   A HE3  1 
ATOM   1845 H HZ1  . LYS   A 1 76  ? 39.076 -8.818  -6.572  1.00 25.98 ?  76  LYS   A HZ1  1 
ATOM   1846 H HZ2  . LYS   A 1 76  ? 38.016 -9.092  -5.622  1.00 25.98 ?  76  LYS   A HZ2  1 
ATOM   1847 H HZ3  . LYS   A 1 76  ? 37.825 -9.390  -7.027  1.00 25.98 ?  76  LYS   A HZ3  1 
ATOM   1848 N N    . VAL   A 1 77  ? 31.363 -4.476  -7.365  1.00 13.22 ?  77  VAL   A N    1 
ATOM   1849 C CA   . VAL   A 1 77  ? 29.954 -4.853  -7.300  1.00 13.15 ?  77  VAL   A CA   1 
ATOM   1850 C C    . VAL   A 1 77  ? 29.881 -6.303  -6.840  1.00 13.04 ?  77  VAL   A C    1 
ATOM   1851 O O    . VAL   A 1 77  ? 30.547 -7.180  -7.401  1.00 13.71 ?  77  VAL   A O    1 
ATOM   1852 C CB   . VAL   A 1 77  ? 29.273 -4.660  -8.662  1.00 14.36 ?  77  VAL   A CB   1 
ATOM   1853 C CG1  . VAL   A 1 77  ? 27.800 -5.057  -8.577  1.00 16.26 ?  77  VAL   A CG1  1 
ATOM   1854 C CG2  . VAL   A 1 77  ? 29.419 -3.221  -9.135  1.00 16.61 ?  77  VAL   A CG2  1 
ATOM   1855 H H    . VAL   A 1 77  ? 31.652 -4.251  -8.144  1.00 15.86 ?  77  VAL   A H    1 
ATOM   1856 H HA   . VAL   A 1 77  ? 29.501 -4.301  -6.647  1.00 15.77 ?  77  VAL   A HA   1 
ATOM   1857 H HB   . VAL   A 1 77  ? 29.704 -5.237  -9.315  1.00 17.23 ?  77  VAL   A HB   1 
ATOM   1858 H HG11 . VAL   A 1 77  ? 27.359 -4.792  -9.397  1.00 19.52 ?  77  VAL   A HG11 1 
ATOM   1859 H HG12 . VAL   A 1 77  ? 27.739 -6.020  -8.464  1.00 19.52 ?  77  VAL   A HG12 1 
ATOM   1860 H HG13 . VAL   A 1 77  ? 27.399 -4.607  -7.820  1.00 19.52 ?  77  VAL   A HG13 1 
ATOM   1861 H HG21 . VAL   A 1 77  ? 28.902 -3.104  -9.944  1.00 19.93 ?  77  VAL   A HG21 1 
ATOM   1862 H HG22 . VAL   A 1 77  ? 29.095 -2.630  -8.440  1.00 19.93 ?  77  VAL   A HG22 1 
ATOM   1863 H HG23 . VAL   A 1 77  ? 30.358 -3.042  -9.311  1.00 19.93 ?  77  VAL   A HG23 1 
ATOM   1864 N N    . GLY   A 1 78  ? 29.079 -6.560  -5.808  1.00 12.42 ?  78  GLY   A N    1 
ATOM   1865 C CA   . GLY   A 1 78  ? 29.045 -7.846  -5.147  1.00 12.89 ?  78  GLY   A CA   1 
ATOM   1866 C C    . GLY   A 1 78  ? 29.954 -7.933  -3.942  1.00 12.29 ?  78  GLY   A C    1 
ATOM   1867 O O    . GLY   A 1 78  ? 29.891 -8.927  -3.202  1.00 13.27 ?  78  GLY   A O    1 
ATOM   1868 H H    . GLY   A 1 78  ? 28.520 -5.988  -5.480  1.00 14.90 ?  78  GLY   A H    1 
ATOM   1869 H HA2  . GLY   A 1 78  ? 28.137 -8.034  -4.857  1.00 15.47 ?  78  GLY   A HA2  1 
ATOM   1870 H HA3  . GLY   A 1 78  ? 29.304 -8.537  -5.781  1.00 15.47 ?  78  GLY   A HA3  1 
ATOM   1871 N N    . GLY   A 1 79  ? 30.811 -6.930  -3.724  1.00 12.40 ?  79  GLY   A N    1 
ATOM   1872 C CA   . GLY   A 1 79  ? 31.765 -6.945  -2.638  1.00 12.73 ?  79  GLY   A CA   1 
ATOM   1873 C C    . GLY   A 1 79  ? 31.309 -6.149  -1.427  1.00 11.29 ?  79  GLY   A C    1 
ATOM   1874 O O    . GLY   A 1 79  ? 30.182 -5.656  -1.347  1.00 12.65 ?  79  GLY   A O    1 
ATOM   1875 H H    . GLY   A 1 79  ? 30.860 -6.221  -4.216  1.00 14.88 ?  79  GLY   A H    1 
ATOM   1876 H HA2  . GLY   A 1 79  ? 31.926 -7.867  -2.371  1.00 15.28 ?  79  GLY   A HA2  1 
ATOM   1877 H HA3  . GLY   A 1 79  ? 32.611 -6.577  -2.953  1.00 15.28 ?  79  GLY   A HA3  1 
ATOM   1878 N N    . SER   A 1 80  ? 32.206 -6.048  -0.450  1.00 12.37 ?  80  SER   A N    1 
ATOM   1879 C CA   . SER   A 1 80  ? 31.871 -5.431  0.824   1.00 11.80 ?  80  SER   A CA   1 
ATOM   1880 C C    . SER   A 1 80  ? 33.130 -4.977  1.544   1.00 12.24 ?  80  SER   A C    1 
ATOM   1881 O O    . SER   A 1 80  ? 34.251 -5.402  1.225   1.00 13.96 ?  80  SER   A O    1 
ATOM   1882 C CB   . SER   A 1 80  ? 31.103 -6.409  1.726   1.00 13.22 ?  80  SER   A CB   1 
ATOM   1883 O OG   . SER   A 1 80  ? 31.937 -7.450  2.209   1.00 15.07 ?  80  SER   A OG   1 
ATOM   1884 H H    . SER   A 1 80  ? 33.031 -6.314  -0.509  1.00 14.84 ?  80  SER   A H    1 
ATOM   1885 H HA   . SER   A 1 80  ? 31.312 -4.660  0.650   1.00 14.16 ?  80  SER   A HA   1 
ATOM   1886 H HB2  . SER   A 1 80  ? 30.744 -5.919  2.480   1.00 15.87 ?  80  SER   A HB2  1 
ATOM   1887 H HB3  . SER   A 1 80  ? 30.375 -6.800  1.212   1.00 15.87 ?  80  SER   A HB3  1 
ATOM   1888 H HG   . SER   A 1 80  ? 32.254 -7.885  1.557   1.00 18.08 ?  80  SER   A HG   1 
ATOM   1889 N N    . CYS   A 1 81  ? 32.931 -4.119  2.542   1.00 11.91 ?  81  CYS   A N    1 
ATOM   1890 C CA   . CYS   A 1 81  ? 33.974 -3.837  3.516   1.00 12.35 ?  81  CYS   A CA   1 
ATOM   1891 C C    . CYS   A 1 81  ? 33.328 -3.597  4.874   1.00 11.85 ?  81  CYS   A C    1 
ATOM   1892 O O    . CYS   A 1 81  ? 32.168 -3.177  4.960   1.00 12.78 ?  81  CYS   A O    1 
ATOM   1893 C CB   . CYS   A 1 81  ? 34.837 -2.642  3.104   1.00 13.13 ?  81  CYS   A CB   1 
ATOM   1894 S SG   . CYS   A 1 81  ? 33.960 -1.063  3.126   1.00 13.03 ?  81  CYS   A SG   1 
ATOM   1895 H H    . CYS   A 1 81  ? 32.196 -3.685  2.677   1.00 14.29 ?  81  CYS   A H    1 
ATOM   1896 H HA   . CYS   A 1 81  ? 34.553 -4.615  3.592   1.00 14.82 ?  81  CYS   A HA   1 
ATOM   1897 H HB2  . CYS   A 1 81  ? 35.594 -2.579  3.712   1.00 15.76 ?  81  CYS   A HB2  1 
ATOM   1898 H HB3  . CYS   A 1 81  ? 35.162 -2.788  2.199   1.00 15.76 ?  81  CYS   A HB3  1 
ATOM   1899 H HG   . CYS   A 1 81  ? 34.712 -0.192  2.801   1.00 15.63 ?  81  CYS   A HG   1 
ATOM   1900 N N    . VAL   A 1 82  ? 34.089 -3.864  5.935   1.00 12.01 ?  82  VAL   A N    1 
ATOM   1901 C CA   . VAL   A 1 82  ? 33.659 -3.609  7.306   1.00 12.81 ?  82  VAL   A CA   1 
ATOM   1902 C C    . VAL   A 1 82  ? 34.255 -2.293  7.780   1.00 12.94 ?  82  VAL   A C    1 
ATOM   1903 O O    . VAL   A 1 82  ? 35.478 -2.120  7.773   1.00 13.34 ?  82  VAL   A O    1 
ATOM   1904 C CB   . VAL   A 1 82  ? 34.077 -4.750  8.247   1.00 14.40 ?  82  VAL   A CB   1 
ATOM   1905 C CG1  . VAL   A 1 82  ? 33.628 -4.466  9.668   1.00 15.77 ?  82  VAL   A CG1  1 
ATOM   1906 C CG2  . VAL   A 1 82  ? 33.525 -6.093  7.768   1.00 15.53 ?  82  VAL   A CG2  1 
ATOM   1907 H H    . VAL   A 1 82  ? 34.873 -4.226  5.882   1.00 14.41 ?  82  VAL   A H    1 
ATOM   1908 H HA   . VAL   A 1 82  ? 32.689 -3.534  7.324   1.00 15.37 ?  82  VAL   A HA   1 
ATOM   1909 H HB   . VAL   A 1 82  ? 35.043 -4.809  8.248   1.00 17.28 ?  82  VAL   A HB   1 
ATOM   1910 H HG11 . VAL   A 1 82  ? 33.730 -5.272  10.195  1.00 18.93 ?  82  VAL   A HG11 1 
ATOM   1911 H HG12 . VAL   A 1 82  ? 34.174 -3.756  10.039  1.00 18.93 ?  82  VAL   A HG12 1 
ATOM   1912 H HG13 . VAL   A 1 82  ? 32.695 -4.195  9.656   1.00 18.93 ?  82  VAL   A HG13 1 
ATOM   1913 H HG21 . VAL   A 1 82  ? 33.773 -6.779  8.407   1.00 18.63 ?  82  VAL   A HG21 1 
ATOM   1914 H HG22 . VAL   A 1 82  ? 32.561 -6.034  7.700   1.00 18.63 ?  82  VAL   A HG22 1 
ATOM   1915 H HG23 . VAL   A 1 82  ? 33.907 -6.299  6.899   1.00 18.63 ?  82  VAL   A HG23 1 
ATOM   1916 N N    . LEU   A 1 83  ? 33.400 -1.378  8.215   1.00 12.64 ?  83  LEU   A N    1 
ATOM   1917 C CA   . LEU   A 1 83  ? 33.816 -0.109  8.796   1.00 12.44 ?  83  LEU   A CA   1 
ATOM   1918 C C    . LEU   A 1 83  ? 33.091 0.074   10.128  1.00 13.16 ?  83  LEU   A C    1 
ATOM   1919 O O    . LEU   A 1 83  ? 32.349 -0.801  10.583  1.00 13.60 ?  83  LEU   A O    1 
ATOM   1920 C CB   . LEU   A 1 83  ? 33.585 1.055   7.814   1.00 12.81 ?  83  LEU   A CB   1 
ATOM   1921 C CG   . LEU   A 1 83  ? 34.472 1.045   6.566   1.00 13.38 ?  83  LEU   A CG   1 
ATOM   1922 C CD1  . LEU   A 1 83  ? 34.045 2.113   5.584   1.00 14.07 ?  83  LEU   A CD1  1 
ATOM   1923 C CD2  . LEU   A 1 83  ? 35.947 1.243   6.939   1.00 14.86 ?  83  LEU   A CD2  1 
ATOM   1924 H H    . LEU   A 1 83  ? 32.546 -1.465  8.173   1.00 15.17 ?  83  LEU   A H    1 
ATOM   1925 H HA   . LEU   A 1 83  ? 34.765 -0.140  8.984   1.00 14.92 ?  83  LEU   A HA   1 
ATOM   1926 H HB2  . LEU   A 1 83  ? 32.661 1.038   7.515   1.00 15.37 ?  83  LEU   A HB2  1 
ATOM   1927 H HB3  . LEU   A 1 83  ? 33.751 1.896   8.279   1.00 15.37 ?  83  LEU   A HB3  1 
ATOM   1928 H HG   . LEU   A 1 83  ? 34.387 0.184   6.128   1.00 16.06 ?  83  LEU   A HG   1 
ATOM   1929 H HD11 . LEU   A 1 83  ? 34.623 2.074   4.802   1.00 16.88 ?  83  LEU   A HD11 1 
ATOM   1930 H HD12 . LEU   A 1 83  ? 33.126 1.952   5.320   1.00 16.88 ?  83  LEU   A HD12 1 
ATOM   1931 H HD13 . LEU   A 1 83  ? 34.122 2.983   6.006   1.00 16.88 ?  83  LEU   A HD13 1 
ATOM   1932 H HD21 . LEU   A 1 83  ? 36.466 1.368   6.125   1.00 17.84 ?  83  LEU   A HD21 1 
ATOM   1933 H HD22 . LEU   A 1 83  ? 36.031 2.028   7.502   1.00 17.84 ?  83  LEU   A HD22 1 
ATOM   1934 H HD23 . LEU   A 1 83  ? 36.266 0.460   7.412   1.00 17.84 ?  83  LEU   A HD23 1 
ATOM   1935 N N    . SER   A 1 84  ? 33.294 1.224   10.761  1.00 13.77 ?  84  SER   A N    1 
ATOM   1936 C CA   . SER   A 1 84  ? 32.643 1.482   12.036  1.00 13.66 ?  84  SER   A CA   1 
ATOM   1937 C C    . SER   A 1 84  ? 31.124 1.594   11.880  1.00 12.97 ?  84  SER   A C    1 
ATOM   1938 O O    . SER   A 1 84  ? 30.612 2.045   10.854  1.00 13.11 ?  84  SER   A O    1 
ATOM   1939 C CB   . SER   A 1 84  ? 33.155 2.803   12.612  1.00 14.94 ?  84  SER   A CB   1 
ATOM   1940 O OG   . SER   A 1 84  ? 32.507 3.109   13.829  1.00 16.19 ?  84  SER   A OG   1 
ATOM   1941 H H    . SER   A 1 84  ? 33.789 1.864   10.473  1.00 16.53 ?  84  SER   A H    1 
ATOM   1942 H HA   . SER   A 1 84  ? 32.849 0.763   12.659  1.00 16.40 ?  84  SER   A HA   1 
ATOM   1943 H HB2  . SER   A 1 84  ? 34.113 2.726   12.763  1.00 17.93 ?  84  SER   A HB2  1 
ATOM   1944 H HB3  . SER   A 1 84  ? 32.980 3.508   11.971  1.00 17.93 ?  84  SER   A HB3  1 
ATOM   1945 H HG   . SER   A 1 84  ? 32.809 3.836   14.132  1.00 19.43 ?  84  SER   A HG   1 
ATOM   1946 N N    A GLY   A 1 85  ? 30.407 1.162   12.914  0.52 14.16 ?  85  GLY   A N    1 
ATOM   1947 N N    B GLY   A 1 85  ? 30.405 1.240   12.946  0.48 14.37 ?  85  GLY   A N    1 
ATOM   1948 C CA   A GLY   A 1 85  ? 28.981 1.385   13.002  0.52 14.50 ?  85  GLY   A CA   1 
ATOM   1949 C CA   B GLY   A 1 85  ? 28.976 1.482   13.016  0.48 14.90 ?  85  GLY   A CA   1 
ATOM   1950 C C    A GLY   A 1 85  ? 28.611 2.690   13.662  0.52 14.10 ?  85  GLY   A C    1 
ATOM   1951 C C    B GLY   A 1 85  ? 28.583 2.818   13.614  0.48 14.63 ?  85  GLY   A C    1 
ATOM   1952 O O    A GLY   A 1 85  ? 27.423 2.976   13.833  0.52 14.38 ?  85  GLY   A O    1 
ATOM   1953 O O    B GLY   A 1 85  ? 27.402 3.179   13.587  0.48 15.48 ?  85  GLY   A O    1 
ATOM   1954 H H    A GLY   A 1 85  ? 30.734 0.735   13.589  0.52 16.99 ?  85  GLY   A H    1 
ATOM   1955 H H    B GLY   A 1 85  ? 30.729 0.859   13.645  0.48 17.24 ?  85  GLY   A H    1 
ATOM   1956 H HA2  A GLY   A 1 85  ? 28.605 1.362   12.107  0.52 17.40 ?  85  GLY   A HA2  1 
ATOM   1957 H HA2  B GLY   A 1 85  ? 28.612 1.448   12.119  0.48 17.88 ?  85  GLY   A HA2  1 
ATOM   1958 H HA3  A GLY   A 1 85  ? 28.578 0.673   13.517  0.52 17.40 ?  85  GLY   A HA3  1 
ATOM   1959 H HA3  B GLY   A 1 85  ? 28.569 0.765   13.529  0.48 17.88 ?  85  GLY   A HA3  1 
ATOM   1960 N N    A HIS   A 1 86  ? 29.606 3.475   14.071  0.52 13.97 ?  86  HIS   A N    1 
ATOM   1961 N N    B HIS   A 1 86  ? 29.541 3.566   14.146  0.48 14.96 ?  86  HIS   A N    1 
ATOM   1962 C CA   A HIS   A 1 86  ? 29.403 4.820   14.623  0.52 14.45 ?  86  HIS   A CA   1 
ATOM   1963 C CA   B HIS   A 1 86  ? 29.287 4.910   14.697  0.48 15.51 ?  86  HIS   A CA   1 
ATOM   1964 C C    A HIS   A 1 86  ? 28.420 4.721   15.788  0.52 14.32 ?  86  HIS   A C    1 
ATOM   1965 C C    B HIS   A 1 86  ? 28.257 4.779   15.823  0.48 16.65 ?  86  HIS   A C    1 
ATOM   1966 O O    A HIS   A 1 86  ? 28.633 3.891   16.682  0.52 15.25 ?  86  HIS   A O    1 
ATOM   1967 O O    B HIS   A 1 86  ? 28.361 3.857   16.647  0.48 18.02 ?  86  HIS   A O    1 
ATOM   1968 C CB   A HIS   A 1 86  ? 29.046 5.790   13.504  0.52 15.02 ?  86  HIS   A CB   1 
ATOM   1969 C CB   B HIS   A 1 86  ? 28.950 5.873   13.571  0.48 14.71 ?  86  HIS   A CB   1 
ATOM   1970 C CG   A HIS   A 1 86  ? 30.108 5.874   12.460  0.52 15.76 ?  86  HIS   A CG   1 
ATOM   1971 C CG   B HIS   A 1 86  ? 30.038 5.977   12.555  0.48 14.33 ?  86  HIS   A CG   1 
ATOM   1972 N ND1  A HIS   A 1 86  ? 31.212 6.690   12.590  0.52 16.63 ?  86  HIS   A ND1  1 
ATOM   1973 N ND1  B HIS   A 1 86  ? 31.110 6.832   12.702  0.48 14.91 ?  86  HIS   A ND1  1 
ATOM   1974 C CD2  A HIS   A 1 86  ? 30.274 5.194   11.302  0.52 15.78 ?  86  HIS   A CD2  1 
ATOM   1975 C CD2  B HIS   A 1 86  ? 30.251 5.295   11.405  0.48 13.84 ?  86  HIS   A CD2  1 
ATOM   1976 C CE1  A HIS   A 1 86  ? 31.997 6.527   11.542  0.52 16.22 ?  86  HIS   A CE1  1 
ATOM   1977 C CE1  B HIS   A 1 86  ? 31.926 6.683   11.674  0.48 14.66 ?  86  HIS   A CE1  1 
ATOM   1978 N NE2  A HIS   A 1 86  ? 31.454 5.622   10.748  0.52 15.86 ?  86  HIS   A NE2  1 
ATOM   1979 N NE2  B HIS   A 1 86  ? 31.432 5.755   10.876  0.48 14.18 ?  86  HIS   A NE2  1 
ATOM   1980 H H    A HIS   A 1 86  ? 30.427 3.238   14.059  0.52 16.76 ?  86  HIS   A H    1 
ATOM   1981 H H    B HIS   A 1 86  ? 30.358 3.326   14.202  0.48 17.95 ?  86  HIS   A H    1 
ATOM   1982 H HA   A HIS   A 1 86  ? 30.240 5.119   14.996  0.52 17.34 ?  86  HIS   A HA   1 
ATOM   1983 H HA   B HIS   A 1 86  ? 30.112 5.223   15.094  0.48 18.62 ?  86  HIS   A HA   1 
ATOM   1984 H HB2  A HIS   A 1 86  ? 28.223 5.498   13.077  0.52 18.03 ?  86  HIS   A HB2  1 
ATOM   1985 H HB2  B HIS   A 1 86  ? 28.145 5.570   13.119  0.48 17.65 ?  86  HIS   A HB2  1 
ATOM   1986 H HB3  A HIS   A 1 86  ? 28.923 6.677   13.880  0.52 18.03 ?  86  HIS   A HB3  1 
ATOM   1987 H HB3  B HIS   A 1 86  ? 28.805 6.759   13.941  0.48 17.65 ?  86  HIS   A HB3  1 
ATOM   1988 H HD2  A HIS   A 1 86  ? 29.696 4.555   10.945  0.52 18.94 ?  86  HIS   A HD2  1 
ATOM   1989 H HD2  B HIS   A 1 86  ? 29.701 4.635   11.039  0.48 16.61 ?  86  HIS   A HD2  1 
ATOM   1990 H HE1  A HIS   A 1 86  ? 32.794 6.978   11.388  0.52 19.46 ?  86  HIS   A HE1  1 
ATOM   1991 H HE1  B HIS   A 1 86  ? 32.713 7.156   11.533  0.48 17.60 ?  86  HIS   A HE1  1 
ATOM   1992 H HE2  A HIS   A 1 86  ? 31.782 5.355   9.998   0.52 19.03 ?  86  HIS   A HE2  1 
ATOM   1993 H HE2  B HIS   A 1 86  ? 31.784 5.490   10.134  0.48 17.01 ?  86  HIS   A HE2  1 
ATOM   1994 N N    A ASN   A 1 87  ? 27.370 5.536   15.825  0.52 16.05 ?  87  ASN   A N    1 
ATOM   1995 N N    B ASN   A 1 87  ? 27.268 5.669   15.887  0.48 17.88 ?  87  ASN   A N    1 
ATOM   1996 C CA   A ASN   A 1 87  ? 26.380 5.519   16.891  0.52 17.11 ?  87  ASN   A CA   1 
ATOM   1997 C CA   B ASN   A 1 87  ? 26.271 5.669   16.949  0.48 18.47 ?  87  ASN   A CA   1 
ATOM   1998 C C    A ASN   A 1 87  ? 25.256 4.518   16.642  0.52 18.41 ?  87  ASN   A C    1 
ATOM   1999 C C    B ASN   A 1 87  ? 25.140 4.684   16.701  0.48 19.32 ?  87  ASN   A C    1 
ATOM   2000 O O    A ASN   A 1 87  ? 24.316 4.459   17.438  0.52 20.82 ?  87  ASN   A O    1 
ATOM   2001 O O    B ASN   A 1 87  ? 24.192 4.650   17.493  0.48 21.46 ?  87  ASN   A O    1 
ATOM   2002 C CB   A ASN   A 1 87  ? 25.793 6.927   17.078  0.52 18.55 ?  87  ASN   A CB   1 
ATOM   2003 C CB   B ASN   A 1 87  ? 25.668 7.071   17.088  0.48 18.99 ?  87  ASN   A CB   1 
ATOM   2004 C CG   A ASN   A 1 87  ? 25.321 7.541   15.771  0.52 19.12 ?  87  ASN   A CG   1 
ATOM   2005 C CG   B ASN   A 1 87  ? 25.151 7.618   15.765  0.48 19.53 ?  87  ASN   A CG   1 
ATOM   2006 O OD1  A ASN   A 1 87  ? 26.008 7.464   14.754  0.52 19.86 ?  87  ASN   A OD1  1 
ATOM   2007 O OD1  B ASN   A 1 87  ? 25.766 7.429   14.718  0.48 20.09 ?  87  ASN   A OD1  1 
ATOM   2008 N ND2  A ASN   A 1 87  ? 24.143 8.146   15.791  0.52 20.57 ?  87  ASN   A ND2  1 
ATOM   2009 N ND2  B ASN   A 1 87  ? 24.016 8.295   15.808  0.48 20.82 ?  87  ASN   A ND2  1 
ATOM   2010 H H    A ASN   A 1 87  ? 27.209 6.129   15.228  0.52 19.26 ?  87  ASN   A H    1 
ATOM   2011 H H    B ASN   A 1 87  ? 27.142 6.288   15.309  0.48 21.46 ?  87  ASN   A H    1 
ATOM   2012 H HA   A ASN   A 1 87  ? 26.807 5.265   17.724  0.52 20.53 ?  87  ASN   A HA   1 
ATOM   2013 H HA   B ASN   A 1 87  ? 26.698 5.436   17.793  0.48 22.16 ?  87  ASN   A HA   1 
ATOM   2014 H HB2  A ASN   A 1 87  ? 25.032 6.878   17.680  0.52 22.26 ?  87  ASN   A HB2  1 
ATOM   2015 H HB2  B ASN   A 1 87  ? 24.922 7.032   17.710  0.48 22.79 ?  87  ASN   A HB2  1 
ATOM   2016 H HB3  A ASN   A 1 87  ? 26.475 7.505   17.452  0.52 22.26 ?  87  ASN   A HB3  1 
ATOM   2017 H HB3  B ASN   A 1 87  ? 26.349 7.672   17.423  0.48 22.79 ?  87  ASN   A HB3  1 
ATOM   2018 H HD21 A ASN   A 1 87  ? 23.833 8.505   15.075  0.52 24.69 ?  87  ASN   A HD21 1 
ATOM   2019 H HD21 B ASN   A 1 87  ? 23.688 8.617   15.084  0.48 24.99 ?  87  ASN   A HD21 1 
ATOM   2020 H HD22 A ASN   A 1 87  ? 23.692 8.185   16.523  0.52 24.69 ?  87  ASN   A HD22 1 
ATOM   2021 H HD22 B ASN   A 1 87  ? 23.612 8.404   16.556  0.48 24.99 ?  87  ASN   A HD22 1 
ATOM   2022 N N    A LEU   A 1 88  ? 25.341 3.721   15.578  0.52 17.30 ?  88  LEU   A N    1 
ATOM   2023 N N    B LEU   A 1 88  ? 25.208 3.895   15.628  0.48 17.67 ?  88  LEU   A N    1 
ATOM   2024 C CA   A LEU   A 1 88  ? 24.246 2.846   15.165  0.52 16.38 ?  88  LEU   A CA   1 
ATOM   2025 C CA   B LEU   A 1 88  ? 24.098 3.046   15.218  0.48 17.26 ?  88  LEU   A CA   1 
ATOM   2026 C C    A LEU   A 1 88  ? 24.472 1.370   15.467  0.52 16.49 ?  88  LEU   A C    1 
ATOM   2027 C C    B LEU   A 1 88  ? 24.323 1.563   15.466  0.48 16.84 ?  88  LEU   A C    1 
ATOM   2028 O O    A LEU   A 1 88  ? 23.499 0.630   15.629  0.52 17.92 ?  88  LEU   A O    1 
ATOM   2029 O O    B LEU   A 1 88  ? 23.346 0.817   15.575  0.48 17.29 ?  88  LEU   A O    1 
ATOM   2030 C CB   A LEU   A 1 88  ? 24.002 2.994   13.658  0.52 16.87 ?  88  LEU   A CB   1 
ATOM   2031 C CB   B LEU   A 1 88  ? 23.817 3.251   13.724  0.48 17.33 ?  88  LEU   A CB   1 
ATOM   2032 C CG   A LEU   A 1 88  ? 23.717 4.397   13.119  0.52 18.07 ?  88  LEU   A CG   1 
ATOM   2033 C CG   B LEU   A 1 88  ? 23.544 4.700   13.315  0.48 17.53 ?  88  LEU   A CG   1 
ATOM   2034 C CD1  A LEU   A 1 88  ? 23.594 4.348   11.606  0.52 18.49 ?  88  LEU   A CD1  1 
ATOM   2035 C CD1  B LEU   A 1 88  ? 23.397 4.830   11.805  0.48 17.51 ?  88  LEU   A CD1  1 
ATOM   2036 C CD2  A LEU   A 1 88  ? 22.456 4.978   13.746  0.52 19.61 ?  88  LEU   A CD2  1 
ATOM   2037 C CD2  B LEU   A 1 88  ? 22.304 5.226   14.021  0.48 18.41 ?  88  LEU   A CD2  1 
ATOM   2038 H H    A LEU   A 1 88  ? 26.041 3.660   15.082  0.52 20.75 ?  88  LEU   A H    1 
ATOM   2039 H H    B LEU   A 1 88  ? 25.898 3.836   15.119  0.48 21.20 ?  88  LEU   A H    1 
ATOM   2040 H HA   A LEU   A 1 88  ? 23.437 3.124   15.622  0.52 19.66 ?  88  LEU   A HA   1 
ATOM   2041 H HA   B LEU   A 1 88  ? 23.306 3.314   15.708  0.48 20.71 ?  88  LEU   A HA   1 
ATOM   2042 H HB2  A LEU   A 1 88  ? 24.787 2.672   13.192  0.52 20.24 ?  88  LEU   A HB2  1 
ATOM   2043 H HB2  B LEU   A 1 88  ? 24.586 2.942   13.222  0.48 20.79 ?  88  LEU   A HB2  1 
ATOM   2044 H HB3  A LEU   A 1 88  ? 23.240 2.445   13.423  0.52 20.24 ?  88  LEU   A HB3  1 
ATOM   2045 H HB3  B LEU   A 1 88  ? 23.038 2.725   13.486  0.48 20.79 ?  88  LEU   A HB3  1 
ATOM   2046 H HG   A LEU   A 1 88  ? 24.458 4.982   13.338  0.52 21.69 ?  88  LEU   A HG   1 
ATOM   2047 H HG   B LEU   A 1 88  ? 24.296 5.249   13.586  0.48 21.04 ?  88  LEU   A HG   1 
ATOM   2048 H HD11 A LEU   A 1 88  ? 23.457 5.247   11.268  0.52 22.19 ?  88  LEU   A HD11 1 
ATOM   2049 H HD11 B LEU   A 1 88  ? 23.275 5.766   11.580  0.48 21.02 ?  88  LEU   A HD11 1 
ATOM   2050 H HD12 A LEU   A 1 88  ? 24.407 3.973   11.235  0.52 22.19 ?  88  LEU   A HD12 1 
ATOM   2051 H HD12 B LEU   A 1 88  ? 24.196 4.487   11.378  0.48 21.02 ?  88  LEU   A HD12 1 
ATOM   2052 H HD13 A LEU   A 1 88  ? 22.834 3.789   11.372  0.52 22.19 ?  88  LEU   A HD13 1 
ATOM   2053 H HD13 B LEU   A 1 88  ? 22.623 4.318   11.519  0.48 21.02 ?  88  LEU   A HD13 1 
ATOM   2054 H HD21 A LEU   A 1 88  ? 22.270 5.841   13.342  0.52 23.54 ?  88  LEU   A HD21 1 
ATOM   2055 H HD21 B LEU   A 1 88  ? 22.074 6.088   13.645  0.48 22.09 ?  88  LEU   A HD21 1 
ATOM   2056 H HD22 A LEU   A 1 88  ? 21.716 4.372   13.587  0.52 23.54 ?  88  LEU   A HD22 1 
ATOM   2057 H HD22 B LEU   A 1 88  ? 21.579 4.598   13.886  0.48 22.09 ?  88  LEU   A HD22 1 
ATOM   2058 H HD23 A LEU   A 1 88  ? 22.599 5.084   14.700  0.52 23.54 ?  88  LEU   A HD23 1 
ATOM   2059 H HD23 B LEU   A 1 88  ? 22.496 5.314   14.967  0.48 22.09 ?  88  LEU   A HD23 1 
ATOM   2060 N N    A ALA   A 1 89  ? 25.724 0.928   15.534  0.52 15.51 ?  89  ALA   A N    1 
ATOM   2061 N N    B ALA   A 1 89  ? 25.574 1.125   15.546  0.48 16.43 ?  89  ALA   A N    1 
ATOM   2062 C CA   A ALA   A 1 89  ? 26.073 -0.484  15.626  0.52 15.02 ?  89  ALA   A CA   1 
ATOM   2063 C CA   B ALA   A 1 89  ? 25.927 -0.282  15.665  0.48 16.24 ?  89  ALA   A CA   1 
ATOM   2064 C C    A ALA   A 1 89  ? 27.559 -0.550  15.941  0.52 15.25 ?  89  ALA   A C    1 
ATOM   2065 C C    B ALA   A 1 89  ? 27.414 -0.336  15.979  0.48 16.27 ?  89  ALA   A C    1 
ATOM   2066 O O    A ALA   A 1 89  ? 28.272 0.453   15.855  0.52 15.69 ?  89  ALA   A O    1 
ATOM   2067 O O    B ALA   A 1 89  ? 28.129 0.661   15.846  0.48 17.37 ?  89  ALA   A O    1 
ATOM   2068 C CB   A ALA   A 1 89  ? 25.793 -1.201  14.305  0.52 14.68 ?  89  ALA   A CB   1 
ATOM   2069 C CB   B ALA   A 1 89  ? 25.643 -1.026  14.360  0.48 16.37 ?  89  ALA   A CB   1 
ATOM   2070 H H    A ALA   A 1 89  ? 26.409 1.446   15.527  0.52 18.61 ?  89  ALA   A H    1 
ATOM   2071 H H    B ALA   A 1 89  ? 26.254 1.645   15.527  0.48 19.71 ?  89  ALA   A H    1 
ATOM   2072 H HA   A ALA   A 1 89  ? 25.561 -0.908  16.337  0.52 18.03 ?  89  ALA   A HA   1 
ATOM   2073 H HA   B ALA   A 1 89  ? 25.420 -0.694  16.386  0.48 19.49 ?  89  ALA   A HA   1 
ATOM   2074 H HB1  A ALA   A 1 89  ? 26.050 -2.132  14.391  0.52 17.61 ?  89  ALA   A HB1  1 
ATOM   2075 H HB1  B ALA   A 1 89  ? 25.892 -1.957  14.466  0.48 19.65 ?  89  ALA   A HB1  1 
ATOM   2076 H HB2  A ALA   A 1 89  ? 24.847 -1.136  14.099  0.52 17.61 ?  89  ALA   A HB2  1 
ATOM   2077 H HB2  B ALA   A 1 89  ? 24.697 -0.959  14.152  0.48 19.65 ?  89  ALA   A HB2  1 
ATOM   2078 H HB3  A ALA   A 1 89  ? 26.314 -0.779  13.603  0.52 17.61 ?  89  ALA   A HB3  1 
ATOM   2079 H HB3  B ALA   A 1 89  ? 26.165 -0.623  13.648  0.48 19.65 ?  89  ALA   A HB3  1 
ATOM   2080 N N    A LYS   A 1 90  ? 28.033 -1.742  16.299  0.52 16.26 ?  90  LYS   A N    1 
ATOM   2081 N N    B LYS   A 1 90  ? 27.883 -1.512  16.395  0.48 16.00 ?  90  LYS   A N    1 
ATOM   2082 C CA   A LYS   A 1 90  ? 29.474 -1.899  16.470  0.52 18.15 ?  90  LYS   A CA   1 
ATOM   2083 C CA   B LYS   A 1 90  ? 29.325 -1.677  16.548  0.48 16.52 ?  90  LYS   A CA   1 
ATOM   2084 C C    A LYS   A 1 90  ? 30.199 -1.752  15.137  0.52 17.12 ?  90  LYS   A C    1 
ATOM   2085 C C    B LYS   A 1 90  ? 30.029 -1.502  15.207  0.48 14.98 ?  90  LYS   A C    1 
ATOM   2086 O O    A LYS   A 1 90  ? 31.193 -1.019  15.034  0.52 18.93 ?  90  LYS   A O    1 
ATOM   2087 O O    B LYS   A 1 90  ? 30.928 -0.661  15.064  0.48 15.13 ?  90  LYS   A O    1 
ATOM   2088 C CB   A LYS   A 1 90  ? 29.801 -3.243  17.115  0.52 21.01 ?  90  LYS   A CB   1 
ATOM   2089 C CB   B LYS   A 1 90  ? 29.646 -3.039  17.165  0.48 19.29 ?  90  LYS   A CB   1 
ATOM   2090 C CG   A LYS   A 1 90  ? 31.284 -3.401  17.426  0.52 25.20 ?  90  LYS   A CG   1 
ATOM   2091 C CG   B LYS   A 1 90  ? 31.118 -3.211  17.525  0.48 23.79 ?  90  LYS   A CG   1 
ATOM   2092 C CD   A LYS   A 1 90  ? 31.535 -4.583  18.345  0.52 29.32 ?  90  LYS   A CD   1 
ATOM   2093 C CD   B LYS   A 1 90  ? 31.344 -4.443  18.391  0.48 27.99 ?  90  LYS   A CD   1 
ATOM   2094 C CE   A LYS   A 1 90  ? 32.960 -4.591  18.877  0.52 32.58 ?  90  LYS   A CE   1 
ATOM   2095 C CE   B LYS   A 1 90  ? 32.728 -4.440  19.024  0.48 31.26 ?  90  LYS   A CE   1 
ATOM   2096 N NZ   A LYS   A 1 90  ? 33.953 -4.988  17.844  0.52 34.72 ?  90  LYS   A NZ   1 
ATOM   2097 N NZ   B LYS   A 1 90  ? 33.813 -4.618  18.023  0.48 33.10 ?  90  LYS   A NZ   1 
ATOM   2098 H H    A LYS   A 1 90  ? 27.556 -2.445  16.446  0.52 19.51 ?  90  LYS   A H    1 
ATOM   2099 H H    B LYS   A 1 90  ? 27.402 -2.200  16.589  0.48 19.20 ?  90  LYS   A H    1 
ATOM   2100 H HA   A LYS   A 1 90  ? 29.790 -1.198  17.056  0.52 21.78 ?  90  LYS   A HA   1 
ATOM   2101 H HA   B LYS   A 1 90  ? 29.650 -0.992  17.151  0.48 19.82 ?  90  LYS   A HA   1 
ATOM   2102 H HB2  A LYS   A 1 90  ? 29.307 -3.319  17.947  0.52 25.21 ?  90  LYS   A HB2  1 
ATOM   2103 H HB2  B LYS   A 1 90  ? 29.123 -3.147  17.977  0.48 23.14 ?  90  LYS   A HB2  1 
ATOM   2104 H HB3  A LYS   A 1 90  ? 29.541 -3.955  16.510  0.52 25.21 ?  90  LYS   A HB3  1 
ATOM   2105 H HB3  B LYS   A 1 90  ? 29.409 -3.734  16.531  0.48 23.14 ?  90  LYS   A HB3  1 
ATOM   2106 H HG2  A LYS   A 1 90  ? 31.771 -3.544  16.600  0.52 30.23 ?  90  LYS   A HG2  1 
ATOM   2107 H HG2  B LYS   A 1 90  ? 31.637 -3.311  16.712  0.48 28.55 ?  90  LYS   A HG2  1 
ATOM   2108 H HG3  A LYS   A 1 90  ? 31.604 -2.598  17.867  0.52 30.23 ?  90  LYS   A HG3  1 
ATOM   2109 H HG3  B LYS   A 1 90  ? 31.418 -2.433  18.020  0.48 28.55 ?  90  LYS   A HG3  1 
ATOM   2110 H HD2  A LYS   A 1 90  ? 30.928 -4.535  19.100  0.52 35.18 ?  90  LYS   A HD2  1 
ATOM   2111 H HD2  B LYS   A 1 90  ? 30.685 -4.461  19.104  0.48 33.59 ?  90  LYS   A HD2  1 
ATOM   2112 H HD3  A LYS   A 1 90  ? 31.390 -5.406  17.851  0.52 35.18 ?  90  LYS   A HD3  1 
ATOM   2113 H HD3  B LYS   A 1 90  ? 31.264 -5.241  17.843  0.48 33.59 ?  90  LYS   A HD3  1 
ATOM   2114 H HE2  A LYS   A 1 90  ? 33.188 -3.699  19.185  0.52 39.10 ?  90  LYS   A HE2  1 
ATOM   2115 H HE2  B LYS   A 1 90  ? 32.871 -3.591  19.472  0.48 37.51 ?  90  LYS   A HE2  1 
ATOM   2116 H HE3  A LYS   A 1 90  ? 33.020 -5.221  19.611  0.52 39.10 ?  90  LYS   A HE3  1 
ATOM   2117 H HE3  B LYS   A 1 90  ? 32.788 -5.166  19.665  0.48 37.51 ?  90  LYS   A HE3  1 
ATOM   2118 H HZ1  A LYS   A 1 90  ? 33.753 -5.794  17.524  0.52 41.67 ?  90  LYS   A HZ1  1 
ATOM   2119 H HZ1  B LYS   A 1 90  ? 34.607 -4.612  18.428  0.48 39.72 ?  90  LYS   A HZ1  1 
ATOM   2120 H HZ2  A LYS   A 1 90  ? 33.946 -4.401  17.175  0.52 41.67 ?  90  LYS   A HZ2  1 
ATOM   2121 H HZ2  B LYS   A 1 90  ? 33.714 -5.397  17.602  0.48 39.72 ?  90  LYS   A HZ2  1 
ATOM   2122 H HZ3  A LYS   A 1 90  ? 34.769 -5.012  18.200  0.52 41.67 ?  90  LYS   A HZ3  1 
ATOM   2123 H HZ3  B LYS   A 1 90  ? 33.789 -3.961  17.425  0.48 39.72 ?  90  LYS   A HZ3  1 
ATOM   2124 N N    A HIS   A 1 91  ? 29.702 -2.432  14.105  0.52 15.21 ?  91  HIS   A N    1 
ATOM   2125 N N    B HIS   A 1 91  ? 29.591 -2.254  14.199  0.48 13.01 ?  91  HIS   A N    1 
ATOM   2126 C CA   A HIS   A 1 91  ? 30.281 -2.400  12.773  0.52 14.47 ?  91  HIS   A CA   1 
ATOM   2127 C CA   B HIS   A 1 91  ? 30.179 -2.232  12.871  0.48 12.20 ?  91  HIS   A CA   1 
ATOM   2128 C C    A HIS   A 1 91  ? 29.192 -2.147  11.747  0.52 12.41 ?  91  HIS   A C    1 
ATOM   2129 C C    B HIS   A 1 91  ? 29.112 -1.954  11.825  0.48 11.41 ?  91  HIS   A C    1 
ATOM   2130 O O    A HIS   A 1 91  ? 28.049 -2.587  11.910  0.52 12.24 ?  91  HIS   A O    1 
ATOM   2131 O O    B HIS   A 1 91  ? 27.924 -2.213  12.033  0.48 12.08 ?  91  HIS   A O    1 
ATOM   2132 C CB   A HIS   A 1 91  ? 30.918 -3.746  12.413  0.52 17.54 ?  91  HIS   A CB   1 
ATOM   2133 C CB   B HIS   A 1 91  ? 30.802 -3.587  12.518  0.48 15.30 ?  91  HIS   A CB   1 
ATOM   2134 C CG   A HIS   A 1 91  ? 31.914 -4.234  13.415  0.52 21.13 ?  91  HIS   A CG   1 
ATOM   2135 C CG   B HIS   A 1 91  ? 31.770 -4.093  13.537  0.48 19.20 ?  91  HIS   A CG   1 
ATOM   2136 N ND1  A HIS   A 1 91  ? 33.185 -3.712  13.512  0.52 23.17 ?  91  HIS   A ND1  1 
ATOM   2137 N ND1  B HIS   A 1 91  ? 33.059 -3.617  13.636  0.48 21.27 ?  91  HIS   A ND1  1 
ATOM   2138 C CD2  A HIS   A 1 91  ? 31.833 -5.206  14.353  0.52 22.77 ?  91  HIS   A CD2  1 
ATOM   2139 C CD2  B HIS   A 1 91  ? 31.644 -5.042  14.493  0.48 21.04 ?  91  HIS   A CD2  1 
ATOM   2140 C CE1  A HIS   A 1 91  ? 33.843 -4.336  14.473  0.52 23.67 ?  91  HIS   A CE1  1 
ATOM   2141 C CE1  B HIS   A 1 91  ? 33.685 -4.249  14.613  0.48 21.97 ?  91  HIS   A CE1  1 
ATOM   2142 N NE2  A HIS   A 1 91  ? 33.044 -5.249  14.999  0.52 23.73 ?  91  HIS   A NE2  1 
ATOM   2143 N NE2  B HIS   A 1 91  ? 32.848 -5.120  15.149  0.48 22.08 ?  91  HIS   A NE2  1 
ATOM   2144 H H    A HIS   A 1 91  ? 28.998 -2.935  14.153  0.52 18.25 ?  91  HIS   A H    1 
ATOM   2145 H H    B HIS   A 1 91  ? 28.920 -2.798  14.266  0.48 15.61 ?  91  HIS   A H    1 
ATOM   2146 H HA   A HIS   A 1 91  ? 30.945 -1.702  12.705  0.52 17.36 ?  91  HIS   A HA   1 
ATOM   2147 H HA   B HIS   A 1 91  ? 30.856 -1.542  12.822  0.48 14.63 ?  91  HIS   A HA   1 
ATOM   2148 H HB2  A HIS   A 1 91  ? 30.218 -4.414  12.343  0.52 21.04 ?  91  HIS   A HB2  1 
ATOM   2149 H HB2  B HIS   A 1 91  ? 30.092 -4.242  12.432  0.48 18.37 ?  91  HIS   A HB2  1 
ATOM   2150 H HB3  A HIS   A 1 91  ? 31.372 -3.656  11.560  0.52 21.04 ?  91  HIS   A HB3  1 
ATOM   2151 H HB3  B HIS   A 1 91  ? 31.272 -3.498  11.675  0.48 18.37 ?  91  HIS   A HB3  1 
ATOM   2152 H HD1  A HIS   A 1 91  ? 33.501 -3.075  13.023  0.52 27.81 ?  91  HIS   A HD1  1 
ATOM   2153 H HD1  B HIS   A 1 91  ? 33.405 -3.001  13.137  0.48 25.53 ?  91  HIS   A HD1  1 
ATOM   2154 H HD2  A HIS   A 1 91  ? 31.094 -5.737  14.531  0.52 27.33 ?  91  HIS   A HD2  1 
ATOM   2155 H HD2  B HIS   A 1 91  ? 30.889 -5.546  14.673  0.48 25.25 ?  91  HIS   A HD2  1 
ATOM   2156 H HE1  A HIS   A 1 91  ? 34.718 -4.160  14.734  0.52 28.41 ?  91  HIS   A HE1  1 
ATOM   2157 H HE1  B HIS   A 1 91  ? 34.569 -4.102  14.875  0.48 26.36 ?  91  HIS   A HE1  1 
ATOM   2158 N N    . CYS   A 1 92  ? 29.562 -1.461  10.671  1.00 12.13 ?  92  CYS   A N    1 
ATOM   2159 C CA   . CYS   A 1 92  ? 28.739 -1.379  9.472   1.00 11.49 ?  92  CYS   A CA   1 
ATOM   2160 C C    . CYS   A 1 92  ? 29.398 -2.204  8.374   1.00 11.80 ?  92  CYS   A C    1 
ATOM   2161 O O    . CYS   A 1 92  ? 30.555 -1.960  8.015   1.00 12.92 ?  92  CYS   A O    1 
ATOM   2162 C CB   . CYS   A 1 92  ? 28.530 0.065   9.006   1.00 12.37 ?  92  CYS   A CB   1 
ATOM   2163 S SG   . CYS   A 1 92  ? 27.538 0.162   7.497   1.00 12.19 ?  92  CYS   A SG   1 
ATOM   2164 H H    A CYS   A 1 92  ? 30.296 -1.016  10.619  0.52 14.55 ?  92  CYS   A H    1 
ATOM   2165 H H    B CYS   A 1 92  ? 30.364 -1.170  10.558  0.48 14.55 ?  92  CYS   A H    1 
ATOM   2166 H HA   . CYS   A 1 92  ? 27.868 -1.761  9.659   1.00 13.78 ?  92  CYS   A HA   1 
ATOM   2167 H HB2  . CYS   A 1 92  ? 28.070 0.564   9.706   1.00 14.84 ?  92  CYS   A HB2  1 
ATOM   2168 H HB3  . CYS   A 1 92  ? 29.394 0.472   8.829   1.00 14.84 ?  92  CYS   A HB3  1 
ATOM   2169 H HG   . CYS   A 1 92  ? 27.400 1.319   7.196   1.00 14.63 ?  92  CYS   A HG   1 
ATOM   2170 N N    . LEU   A 1 93  ? 28.673 -3.195  7.870   1.00 11.62 ?  93  LEU   A N    1 
ATOM   2171 C CA   . LEU   A 1 93  ? 29.080 -3.939  6.688   1.00 10.63 ?  93  LEU   A CA   1 
ATOM   2172 C C    . LEU   A 1 93  ? 28.487 -3.258  5.459   1.00 11.06 ?  93  LEU   A C    1 
ATOM   2173 O O    . LEU   A 1 93  ? 27.273 -3.327  5.223   1.00 11.30 ?  93  LEU   A O    1 
ATOM   2174 C CB   . LEU   A 1 93  ? 28.608 -5.389  6.802   1.00 11.64 ?  93  LEU   A CB   1 
ATOM   2175 C CG   . LEU   A 1 93  ? 29.008 -6.296  5.640   1.00 12.48 ?  93  LEU   A CG   1 
ATOM   2176 C CD1  . LEU   A 1 93  ? 30.510 -6.571  5.618   1.00 13.50 ?  93  LEU   A CD1  1 
ATOM   2177 C CD2  . LEU   A 1 93  ? 28.226 -7.619  5.687   1.00 13.35 ?  93  LEU   A CD2  1 
ATOM   2178 H H    . LEU   A 1 93  ? 27.921 -3.457  8.202   1.00 13.95 ?  93  LEU   A H    1 
ATOM   2179 H HA   . LEU   A 1 93  ? 30.046 -3.929  6.619   1.00 12.76 ?  93  LEU   A HA   1 
ATOM   2180 H HB2  . LEU   A 1 93  ? 28.982 -5.771  7.611   1.00 13.97 ?  93  LEU   A HB2  1 
ATOM   2181 H HB3  . LEU   A 1 93  ? 27.642 -5.395  6.855   1.00 13.97 ?  93  LEU   A HB3  1 
ATOM   2182 H HG   . LEU   A 1 93  ? 28.784 -5.857  4.807   1.00 14.97 ?  93  LEU   A HG   1 
ATOM   2183 H HD11 . LEU   A 1 93  ? 30.713 -7.174  4.889   1.00 16.20 ?  93  LEU   A HD11 1 
ATOM   2184 H HD12 . LEU   A 1 93  ? 30.984 -5.734  5.505   1.00 16.20 ?  93  LEU   A HD12 1 
ATOM   2185 H HD13 . LEU   A 1 93  ? 30.766 -6.982  6.465   1.00 16.20 ?  93  LEU   A HD13 1 
ATOM   2186 H HD21 . LEU   A 1 93  ? 28.499 -8.176  4.940   1.00 16.02 ?  93  LEU   A HD21 1 
ATOM   2187 H HD22 . LEU   A 1 93  ? 28.417 -8.072  6.523   1.00 16.02 ?  93  LEU   A HD22 1 
ATOM   2188 H HD23 . LEU   A 1 93  ? 27.277 -7.427  5.624   1.00 16.02 ?  93  LEU   A HD23 1 
ATOM   2189 N N    . HIS   A 1 94  ? 29.339 -2.567  4.696   1.00 10.51 ?  94  HIS   A N    1 
ATOM   2190 C CA   . HIS   A 1 94  ? 28.921 -1.900  3.465   1.00 10.88 ?  94  HIS   A CA   1 
ATOM   2191 C C    . HIS   A 1 94  ? 28.951 -2.939  2.354   1.00 10.94 ?  94  HIS   A C    1 
ATOM   2192 O O    . HIS   A 1 94  ? 30.023 -3.463  2.024   1.00 12.22 ?  94  HIS   A O    1 
ATOM   2193 C CB   . HIS   A 1 94  ? 29.872 -0.746  3.140   1.00 11.05 ?  94  HIS   A CB   1 
ATOM   2194 C CG   . HIS   A 1 94  ? 29.863 0.335   4.164   1.00 10.99 ?  94  HIS   A CG   1 
ATOM   2195 N ND1  . HIS   A 1 94  ? 29.001 1.413   4.103   1.00 11.14 ?  94  HIS   A ND1  1 
ATOM   2196 C CD2  . HIS   A 1 94  ? 30.607 0.505   5.279   1.00 11.73 ?  94  HIS   A CD2  1 
ATOM   2197 C CE1  . HIS   A 1 94  ? 29.214 2.192   5.149   1.00 11.59 ?  94  HIS   A CE1  1 
ATOM   2198 N NE2  . HIS   A 1 94  ? 30.184 1.664   5.877   1.00 11.71 ?  94  HIS   A NE2  1 
ATOM   2199 H H    . HIS   A 1 94  ? 30.181 -2.472  4.865   1.00 12.62 ?  94  HIS   A H    1 
ATOM   2200 H HA   . HIS   A 1 94  ? 28.014 -1.557  3.560   1.00 13.05 ?  94  HIS   A HA   1 
ATOM   2201 H HB2  . HIS   A 1 94  ? 30.770 -1.091  3.079   1.00 13.26 ?  94  HIS   A HB2  1 
ATOM   2202 H HB3  . HIS   A 1 94  ? 29.605 -0.353  2.291   1.00 13.26 ?  94  HIS   A HB3  1 
ATOM   2203 H HD2  . HIS   A 1 94  ? 31.276 -0.055  5.586   1.00 14.07 ?  94  HIS   A HD2  1 
ATOM   2204 H HE1  . HIS   A 1 94  ? 28.756 2.984   5.333   1.00 13.91 ?  94  HIS   A HE1  1 
ATOM   2205 H HE2  . HIS   A 1 94  ? 30.503 2.008   6.597   1.00 14.05 ?  94  HIS   A HE2  1 
ATOM   2206 N N    . VAL   A 1 95  ? 27.783 -3.267  1.797   1.00 10.55 ?  95  VAL   A N    1 
ATOM   2207 C CA   . VAL   A 1 95  ? 27.647 -4.302  0.775   1.00 10.56 ?  95  VAL   A CA   1 
ATOM   2208 C C    . VAL   A 1 95  ? 27.106 -3.669  -0.497  1.00 10.59 ?  95  VAL   A C    1 
ATOM   2209 O O    . VAL   A 1 95  ? 26.102 -2.944  -0.449  1.00 11.72 ?  95  VAL   A O    1 
ATOM   2210 C CB   . VAL   A 1 95  ? 26.713 -5.443  1.222   1.00 10.94 ?  95  VAL   A CB   1 
ATOM   2211 C CG1  . VAL   A 1 95  ? 26.597 -6.475  0.108   1.00 11.65 ?  95  VAL   A CG1  1 
ATOM   2212 C CG2  . VAL   A 1 95  ? 27.197 -6.056  2.516   1.00 11.19 ?  95  VAL   A CG2  1 
ATOM   2213 H H    . VAL   A 1 95  ? 27.029 -2.905  2.006   1.00 12.66 ?  95  VAL   A H    1 
ATOM   2214 H HA   . VAL   A 1 95  ? 28.521 -4.682  0.578   1.00 12.67 ?  95  VAL   A HA   1 
ATOM   2215 H HB   . VAL   A 1 95  ? 25.831 -5.080  1.372   1.00 13.13 ?  95  VAL   A HB   1 
ATOM   2216 H HG11 . VAL   A 1 95  ? 26.227 -7.293  0.470   1.00 13.98 ?  95  VAL   A HG11 1 
ATOM   2217 H HG12 . VAL   A 1 95  ? 26.013 -6.132  -0.590  1.00 13.98 ?  95  VAL   A HG12 1 
ATOM   2218 H HG13 . VAL   A 1 95  ? 27.480 -6.650  -0.261  1.00 13.98 ?  95  VAL   A HG13 1 
ATOM   2219 H HG21 . VAL   A 1 95  ? 26.623 -6.810  2.737   1.00 13.43 ?  95  VAL   A HG21 1 
ATOM   2220 H HG22 . VAL   A 1 95  ? 28.109 -6.357  2.403   1.00 13.43 ?  95  VAL   A HG22 1 
ATOM   2221 H HG23 . VAL   A 1 95  ? 27.146 -5.388  3.214   1.00 13.43 ?  95  VAL   A HG23 1 
ATOM   2222 N N    A VAL   A 1 96  ? 27.731 -3.979  -1.631  0.52 10.54 ?  96  VAL   A N    1 
ATOM   2223 N N    B VAL   A 1 96  ? 27.742 -3.955  -1.628  0.48 10.66 ?  96  VAL   A N    1 
ATOM   2224 C CA   A VAL   A 1 96  ? 27.353 -3.425  -2.928  0.52 11.05 ?  96  VAL   A CA   1 
ATOM   2225 C CA   B VAL   A 1 96  ? 27.320 -3.428  -2.921  0.48 11.41 ?  96  VAL   A CA   1 
ATOM   2226 C C    A VAL   A 1 96  ? 26.515 -4.451  -3.685  0.52 11.79 ?  96  VAL   A C    1 
ATOM   2227 C C    B VAL   A 1 96  ? 26.591 -4.526  -3.686  0.48 12.13 ?  96  VAL   A C    1 
ATOM   2228 O O    A VAL   A 1 96  ? 27.052 -5.356  -4.325  0.52 11.52 ?  96  VAL   A O    1 
ATOM   2229 O O    B VAL   A 1 96  ? 27.208 -5.497  -4.133  0.48 13.02 ?  96  VAL   A O    1 
ATOM   2230 C CB   A VAL   A 1 96  ? 28.572 -2.997  -3.748  0.52 11.43 ?  96  VAL   A CB   1 
ATOM   2231 C CB   B VAL   A 1 96  ? 28.499 -2.878  -3.733  0.48 11.73 ?  96  VAL   A CB   1 
ATOM   2232 C CG1  A VAL   A 1 96  ? 28.112 -2.316  -5.025  0.52 12.14 ?  96  VAL   A CG1  1 
ATOM   2233 C CG1  B VAL   A 1 96  ? 27.992 -2.313  -5.046  0.48 11.69 ?  96  VAL   A CG1  1 
ATOM   2234 C CG2  A VAL   A 1 96  ? 29.478 -2.085  -2.935  0.52 10.79 ?  96  VAL   A CG2  1 
ATOM   2235 C CG2  B VAL   A 1 96  ? 29.256 -1.815  -2.939  0.48 11.79 ?  96  VAL   A CG2  1 
ATOM   2236 H H    A VAL   A 1 96  ? 28.405 -4.519  -1.675  0.52 12.65 ?  96  VAL   A H    1 
ATOM   2237 H H    B VAL   A 1 96  ? 28.438 -4.467  -1.677  0.48 12.79 ?  96  VAL   A H    1 
ATOM   2238 H HA   A VAL   A 1 96  ? 26.802 -2.644  -2.784  0.52 13.25 ?  96  VAL   A HA   1 
ATOM   2239 H HA   B VAL   A 1 96  ? 26.699 -2.699  -2.774  0.48 13.69 ?  96  VAL   A HA   1 
ATOM   2240 H HB   A VAL   A 1 96  ? 29.081 -3.784  -3.995  0.52 13.71 ?  96  VAL   A HB   1 
ATOM   2241 H HB   B VAL   A 1 96  ? 29.115 -3.599  -3.930  0.48 14.08 ?  96  VAL   A HB   1 
ATOM   2242 H HG11 A VAL   A 1 96  ? 28.880 -1.914  -5.460  0.52 14.57 ?  96  VAL   A HG11 1 
ATOM   2243 H HG11 B VAL   A 1 96  ? 28.695 -1.779  -5.449  0.48 14.02 ?  96  VAL   A HG11 1 
ATOM   2244 H HG12 A VAL   A 1 96  ? 27.708 -2.974  -5.611  0.52 14.57 ?  96  VAL   A HG12 1 
ATOM   2245 H HG12 B VAL   A 1 96  ? 27.754 -3.044  -5.635  0.48 14.02 ?  96  VAL   A HG12 1 
ATOM   2246 H HG13 A VAL   A 1 96  ? 27.464 -1.629  -4.801  0.52 14.57 ?  96  VAL   A HG13 1 
ATOM   2247 H HG13 B VAL   A 1 96  ? 27.217 -1.757  -4.872  0.48 14.02 ?  96  VAL   A HG13 1 
ATOM   2248 H HG21 A VAL   A 1 96  ? 30.189 -1.755  -3.506  0.52 12.95 ?  96  VAL   A HG21 1 
ATOM   2249 H HG21 B VAL   A 1 96  ? 29.964 -1.449  -3.494  0.48 14.15 ?  96  VAL   A HG21 1 
ATOM   2250 H HG22 A VAL   A 1 96  ? 28.956 -1.342  -2.593  0.52 12.95 ?  96  VAL   A HG22 1 
ATOM   2251 H HG22 B VAL   A 1 96  ? 28.639 -1.109  -2.685  0.48 14.15 ?  96  VAL   A HG22 1 
ATOM   2252 H HG23 A VAL   A 1 96  ? 29.856 -2.590  -2.197  0.52 12.95 ?  96  VAL   A HG23 1 
ATOM   2253 H HG23 B VAL   A 1 96  ? 29.637 -2.221  -2.144  0.48 14.15 ?  96  VAL   A HG23 1 
ATOM   2254 N N    A GLY   A 1 97  ? 25.194 -4.292  -3.654  0.52 11.69 ?  97  GLY   A N    1 
ATOM   2255 N N    B GLY   A 1 97  ? 25.276 -4.373  -3.842  0.48 10.99 ?  97  GLY   A N    1 
ATOM   2256 C CA   A GLY   A 1 97  ? 24.341 -5.013  -4.566  0.52 12.56 ?  97  GLY   A CA   1 
ATOM   2257 C CA   B GLY   A 1 97  ? 24.530 -5.177  -4.778  0.48 11.45 ?  97  GLY   A CA   1 
ATOM   2258 C C    A GLY   A 1 97  ? 24.333 -4.338  -5.926  0.52 13.09 ?  97  GLY   A C    1 
ATOM   2259 C C    B GLY   A 1 97  ? 24.593 -4.596  -6.180  0.48 11.16 ?  97  GLY   A C    1 
ATOM   2260 O O    A GLY   A 1 97  ? 24.589 -3.133  -6.040  0.52 12.95 ?  97  GLY   A O    1 
ATOM   2261 O O    B GLY   A 1 97  ? 24.945 -3.426  -6.372  0.48 12.06 ?  97  GLY   A O    1 
ATOM   2262 H H    A GLY   A 1 97  ? 24.772 -3.769  -3.114  0.52 14.03 ?  97  GLY   A H    1 
ATOM   2263 H H    B GLY   A 1 97  ? 24.793 -3.807  -3.398  0.48 13.19 ?  97  GLY   A H    1 
ATOM   2264 H HA2  A GLY   A 1 97  ? 24.669 -5.920  -4.665  0.52 15.07 ?  97  GLY   A HA2  1 
ATOM   2265 H HA2  B GLY   A 1 97  ? 24.897 -6.073  -4.790  0.48 13.74 ?  97  GLY   A HA2  1 
ATOM   2266 H HA3  A GLY   A 1 97  ? 23.435 -5.047  -4.216  0.52 15.07 ?  97  GLY   A HA3  1 
ATOM   2267 H HA3  B GLY   A 1 97  ? 23.600 -5.227  -4.497  0.48 13.74 ?  97  GLY   A HA3  1 
ATOM   2268 N N    A PRO   A 1 98  ? 24.042 -5.090  -6.986  0.52 12.47 ?  98  PRO   A N    1 
ATOM   2269 N N    B PRO   A 1 98  ? 24.240 -5.391  -7.189  0.48 12.14 ?  98  PRO   A N    1 
ATOM   2270 C CA   A PRO   A 1 98  ? 23.947 -4.470  -8.312  0.52 12.94 ?  98  PRO   A CA   1 
ATOM   2271 C CA   B PRO   A 1 98  ? 24.224 -4.875  -8.562  0.48 13.24 ?  98  PRO   A CA   1 
ATOM   2272 C C    A PRO   A 1 98  ? 22.831 -3.439  -8.364  0.52 13.04 ?  98  PRO   A C    1 
ATOM   2273 C C    B PRO   A 1 98  ? 23.130 -3.835  -8.759  0.48 14.19 ?  98  PRO   A C    1 
ATOM   2274 O O    A PRO   A 1 98  ? 21.757 -3.627  -7.789  0.52 12.80 ?  98  PRO   A O    1 
ATOM   2275 O O    B PRO   A 1 98  ? 22.023 -3.957  -8.228  0.48 14.87 ?  98  PRO   A O    1 
ATOM   2276 C CB   A PRO   A 1 98  ? 23.666 -5.655  -9.244  0.52 13.54 ?  98  PRO   A CB   1 
ATOM   2277 C CB   B PRO   A 1 98  ? 23.950 -6.127  -9.405  0.48 13.57 ?  98  PRO   A CB   1 
ATOM   2278 C CG   A PRO   A 1 98  ? 23.088 -6.715  -8.361  0.52 13.39 ?  98  PRO   A CG   1 
ATOM   2279 C CG   B PRO   A 1 98  ? 23.241 -7.056  -8.471  0.48 13.75 ?  98  PRO   A CG   1 
ATOM   2280 C CD   A PRO   A 1 98  ? 23.783 -6.540  -7.033  0.52 12.81 ?  98  PRO   A CD   1 
ATOM   2281 C CD   B PRO   A 1 98  ? 23.868 -6.815  -7.124  0.48 12.96 ?  98  PRO   A CD   1 
ATOM   2282 H HA   A PRO   A 1 98  ? 24.790 -4.058  -8.549  0.52 15.53 ?  98  PRO   A HA   1 
ATOM   2283 H HA   B PRO   A 1 98  ? 25.088 -4.498  -8.796  0.48 15.89 ?  98  PRO   A HA   1 
ATOM   2284 H HB2  A PRO   A 1 98  ? 23.028 -5.394  -9.923  0.52 16.25 ?  98  PRO   A HB2  1 
ATOM   2285 H HB2  B PRO   A 1 98  ? 23.388 -5.894  -10.155 0.48 16.29 ?  98  PRO   A HB2  1 
ATOM   2286 H HB3  A PRO   A 1 98  ? 24.495 -5.961  -9.645  0.52 16.25 ?  98  PRO   A HB3  1 
ATOM   2287 H HB3  B PRO   A 1 98  ? 24.790 -6.511  -9.701  0.48 16.29 ?  98  PRO   A HB3  1 
ATOM   2288 H HG2  A PRO   A 1 98  ? 22.133 -6.581  -8.267  0.52 16.07 ?  98  PRO   A HG2  1 
ATOM   2289 H HG2  B PRO   A 1 98  ? 22.295 -6.840  -8.448  0.48 16.50 ?  98  PRO   A HG2  1 
ATOM   2290 H HG3  A PRO   A 1 98  ? 23.277 -7.592  -8.733  0.52 16.07 ?  98  PRO   A HG3  1 
ATOM   2291 H HG3  B PRO   A 1 98  ? 23.377 -7.973  -8.753  0.48 16.50 ?  98  PRO   A HG3  1 
ATOM   2292 H HD2  A PRO   A 1 98  ? 23.200 -6.816  -6.304  0.52 15.37 ?  98  PRO   A HD2  1 
ATOM   2293 H HD2  B PRO   A 1 98  ? 23.224 -6.965  -6.411  0.48 15.55 ?  98  PRO   A HD2  1 
ATOM   2294 H HD3  A PRO   A 1 98  ? 24.622 -7.032  -7.017  0.52 15.37 ?  98  PRO   A HD3  1 
ATOM   2295 H HD3  B PRO   A 1 98  ? 24.657 -7.373  -7.007  0.48 15.55 ?  98  PRO   A HD3  1 
ATOM   2296 N N    A ASN   A 1 99  ? 23.109 -2.333  -9.051  0.52 13.74 ?  99  ASN   A N    1 
ATOM   2297 N N    B ASN   A 1 99  ? 23.454 -2.804  -9.537  0.48 14.79 ?  99  ASN   A N    1 
ATOM   2298 C CA   A ASN   A 1 99  ? 22.131 -1.277  -9.298  0.52 15.04 ?  99  ASN   A CA   1 
ATOM   2299 C CA   B ASN   A 1 99  ? 22.507 -1.757  -9.924  0.48 15.53 ?  99  ASN   A CA   1 
ATOM   2300 C C    A ASN   A 1 99  ? 21.586 -1.466  -10.709 0.52 17.01 ?  99  ASN   A C    1 
ATOM   2301 C C    B ASN   A 1 99  ? 22.020 -2.092  -11.329 0.48 15.77 ?  99  ASN   A C    1 
ATOM   2302 O O    A ASN   A 1 99  ? 22.262 -1.156  -11.695 0.52 18.82 ?  99  ASN   A O    1 
ATOM   2303 O O    B ASN   A 1 99  ? 22.744 -1.905  -12.309 0.48 15.35 ?  99  ASN   A O    1 
ATOM   2304 C CB   A ASN   A 1 99  ? 22.780 0.092   -9.140  0.52 15.78 ?  99  ASN   A CB   1 
ATOM   2305 C CB   B ASN   A 1 99  ? 23.187 -0.392  -9.905  0.48 17.47 ?  99  ASN   A CB   1 
ATOM   2306 C CG   A ASN   A 1 99  ? 21.765 1.226   -9.134  0.52 16.79 ?  99  ASN   A CG   1 
ATOM   2307 C CG   B ASN   A 1 99  ? 22.226 0.754   -10.204 0.48 18.76 ?  99  ASN   A CG   1 
ATOM   2308 O OD1  A ASN   A 1 99  ? 20.773 1.198   -9.860  0.52 17.30 ?  99  ASN   A OD1  1 
ATOM   2309 O OD1  B ASN   A 1 99  ? 21.149 0.559   -10.764 0.48 18.79 ?  99  ASN   A OD1  1 
ATOM   2310 N ND2  A ASN   A 1 99  ? 22.015 2.230   -8.310  0.52 17.44 ?  99  ASN   A ND2  1 
ATOM   2311 N ND2  B ASN   A 1 99  ? 22.625 1.962   -9.838  0.48 20.68 ?  99  ASN   A ND2  1 
ATOM   2312 H H    A ASN   A 1 99  ? 23.889 -2.165  -9.370  0.52 16.49 ?  99  ASN   A H    1 
ATOM   2313 H H    B ASN   A 1 99  ? 24.246 -2.687  -9.852  0.48 17.75 ?  99  ASN   A H    1 
ATOM   2314 H HA   A ASN   A 1 99  ? 21.400 -1.364  -8.663  0.52 18.05 ?  99  ASN   A HA   1 
ATOM   2315 H HA   B ASN   A 1 99  ? 21.752 -1.752  -9.315  0.48 18.64 ?  99  ASN   A HA   1 
ATOM   2316 H HB2  A ASN   A 1 99  ? 23.270 0.112   -8.306  0.52 18.94 ?  99  ASN   A HB2  1 
ATOM   2317 H HB2  B ASN   A 1 99  ? 23.578 -0.245  -9.031  0.48 20.96 ?  99  ASN   A HB2  1 
ATOM   2318 H HB3  A ASN   A 1 99  ? 23.385 0.232   -9.886  0.52 18.94 ?  99  ASN   A HB3  1 
ATOM   2319 H HB3  B ASN   A 1 99  ? 23.878 -0.389  -10.585 0.48 20.96 ?  99  ASN   A HB3  1 
ATOM   2320 H HD21 A ASN   A 1 99  ? 21.471 2.891   -8.267  0.52 20.92 ?  99  ASN   A HD21 1 
ATOM   2321 H HD21 B ASN   A 1 99  ? 22.117 2.640   -9.983  0.48 24.81 ?  99  ASN   A HD21 1 
ATOM   2322 H HD22 A ASN   A 1 99  ? 22.724 2.219   -7.822  0.52 20.92 ?  99  ASN   A HD22 1 
ATOM   2323 H HD22 B ASN   A 1 99  ? 23.388 2.066   -9.462  0.48 24.81 ?  99  ASN   A HD22 1 
ATOM   2324 N N    A VAL   A 1 100 ? 20.352 -1.978  -10.797 0.52 17.69 ?  100 VAL   A N    1 
ATOM   2325 N N    B VAL   A 1 100 ? 20.785 -2.588  -11.427 0.48 17.55 ?  100 VAL   A N    1 
ATOM   2326 C CA   A VAL   A 1 100 ? 19.728 -2.232  -12.095 0.52 19.85 ?  100 VAL   A CA   1 
ATOM   2327 C CA   B VAL   A 1 100 ? 20.257 -2.984  -12.729 0.48 19.98 ?  100 VAL   A CA   1 
ATOM   2328 C C    A VAL   A 1 100 ? 19.629 -0.946  -12.905 0.52 20.83 ?  100 VAL   A C    1 
ATOM   2329 C C    B VAL   A 1 100 ? 20.043 -1.775  -13.635 0.48 20.26 ?  100 VAL   A C    1 
ATOM   2330 O O    A VAL   A 1 100 ? 19.744 -0.966  -14.137 0.52 22.21 ?  100 VAL   A O    1 
ATOM   2331 O O    B VAL   A 1 100 ? 20.060 -1.906  -14.865 0.48 20.05 ?  100 VAL   A O    1 
ATOM   2332 C CB   A VAL   A 1 100 ? 18.357 -2.923  -11.902 0.52 20.99 ?  100 VAL   A CB   1 
ATOM   2333 C CB   B VAL   A 1 100 ? 18.987 -3.838  -12.554 0.48 22.14 ?  100 VAL   A CB   1 
ATOM   2334 C CG1  A VAL   A 1 100 ? 17.637 -3.099  -13.232 0.52 21.84 ?  100 VAL   A CG1  1 
ATOM   2335 C CG1  B VAL   A 1 100 ? 18.264 -4.020  -13.881 0.48 23.09 ?  100 VAL   A CG1  1 
ATOM   2336 C CG2  A VAL   A 1 100 ? 18.537 -4.275  -11.219 0.52 21.05 ?  100 VAL   A CG2  1 
ATOM   2337 C CG2  B VAL   A 1 100 ? 19.348 -5.188  -11.958 0.48 23.35 ?  100 VAL   A CG2  1 
ATOM   2338 H H    A VAL   A 1 100 ? 19.854 -2.185  -10.120 0.52 21.22 ?  100 VAL   A H    1 
ATOM   2339 H H    B VAL   A 1 100 ? 20.247 -2.717  -10.766 0.48 21.06 ?  100 VAL   A H    1 
ATOM   2340 H HA   A VAL   A 1 100 ? 20.284 -2.852  -12.590 0.52 23.82 ?  100 VAL   A HA   1 
ATOM   2341 H HA   B VAL   A 1 100 ? 20.916 -3.549  -13.158 0.48 23.98 ?  100 VAL   A HA   1 
ATOM   2342 H HB   A VAL   A 1 100 ? 17.796 -2.376  -11.330 0.52 25.19 ?  100 VAL   A HB   1 
ATOM   2343 H HB   B VAL   A 1 100 ? 18.383 -3.389  -11.945 0.48 26.57 ?  100 VAL   A HB   1 
ATOM   2344 H HG11 A VAL   A 1 100 ? 16.882 -3.700  -13.109 0.52 26.21 ?  100 VAL   A HG11 1 
ATOM   2345 H HG11 B VAL   A 1 100 ? 17.575 -4.695  -13.771 0.48 27.70 ?  100 VAL   A HG11 1 
ATOM   2346 H HG12 A VAL   A 1 100 ? 17.321 -2.236  -13.540 0.52 26.21 ?  100 VAL   A HG12 1 
ATOM   2347 H HG12 B VAL   A 1 100 ? 17.856 -3.179  -14.142 0.48 27.70 ?  100 VAL   A HG12 1 
ATOM   2348 H HG13 A VAL   A 1 100 ? 18.254 -3.478  -13.878 0.52 26.21 ?  100 VAL   A HG13 1 
ATOM   2349 H HG13 B VAL   A 1 100 ? 18.900 -4.305  -14.554 0.48 27.70 ?  100 VAL   A HG13 1 
ATOM   2350 H HG21 A VAL   A 1 100 ? 17.673 -4.714  -11.148 0.52 25.26 ?  100 VAL   A HG21 1 
ATOM   2351 H HG21 B VAL   A 1 100 ? 18.540 -5.714  -11.857 0.48 28.02 ?  100 VAL   A HG21 1 
ATOM   2352 H HG22 A VAL   A 1 100 ? 19.140 -4.818  -11.750 0.52 25.26 ?  100 VAL   A HG22 1 
ATOM   2353 H HG22 B VAL   A 1 100 ? 19.965 -5.641  -12.556 0.48 28.02 ?  100 VAL   A HG22 1 
ATOM   2354 H HG23 A VAL   A 1 100 ? 18.909 -4.135  -10.335 0.52 25.26 ?  100 VAL   A HG23 1 
ATOM   2355 H HG23 B VAL   A 1 100 ? 19.764 -5.049  -11.095 0.48 28.02 ?  100 VAL   A HG23 1 
ATOM   2356 N N    A ASN   A 1 101 ? 19.425 0.188   -12.239 0.52 20.96 ?  101 ASN   A N    1 
ATOM   2357 N N    B ASN   A 1 101 ? 19.842 -0.584  -13.062 0.48 20.92 ?  101 ASN   A N    1 
ATOM   2358 C CA   A ASN   A 1 101 ? 19.344 1.465   -12.937 0.52 22.74 ?  101 ASN   A CA   1 
ATOM   2359 C CA   B ASN   A 1 101 ? 19.766 0.625   -13.878 0.48 22.22 ?  101 ASN   A CA   1 
ATOM   2360 C C    A ASN   A 1 101 ? 20.692 1.936   -13.477 0.52 24.90 ?  101 ASN   A C    1 
ATOM   2361 C C    B ASN   A 1 101 ? 21.108 0.986   -14.509 0.48 23.74 ?  101 ASN   A C    1 
ATOM   2362 O O    A ASN   A 1 101 ? 20.741 2.993   -14.121 0.52 26.15 ?  101 ASN   A O    1 
ATOM   2363 O O    B ASN   A 1 101 ? 21.134 1.781   -15.456 0.48 24.17 ?  101 ASN   A O    1 
ATOM   2364 C CB   A ASN   A 1 101 ? 18.723 2.516   -12.017 0.52 21.75 ?  101 ASN   A CB   1 
ATOM   2365 C CB   B ASN   A 1 101 ? 19.237 1.803   -13.053 0.48 23.12 ?  101 ASN   A CB   1 
ATOM   2366 C CG   A ASN   A 1 101 ? 17.361 2.095   -11.492 0.52 22.02 ?  101 ASN   A CG   1 
ATOM   2367 C CG   B ASN   A 1 101 ? 17.839 1.558   -12.518 0.48 24.21 ?  101 ASN   A CG   1 
ATOM   2368 O OD1  A ASN   A 1 101 ? 16.518 1.600   -12.245 0.52 22.06 ?  101 ASN   A OD1  1 
ATOM   2369 O OD1  B ASN   A 1 101 ? 17.118 0.685   -13.005 0.48 24.97 ?  101 ASN   A OD1  1 
ATOM   2370 N ND2  A ASN   A 1 101 ? 17.137 2.292   -10.196 0.52 22.71 ?  101 ASN   A ND2  1 
ATOM   2371 N ND2  B ASN   A 1 101 ? 17.448 2.329   -11.515 0.48 24.85 ?  101 ASN   A ND2  1 
ATOM   2372 H H    A ASN   A 1 101 ? 19.325 0.238   -11.386 0.52 25.16 ?  101 ASN   A H    1 
ATOM   2373 H H    B ASN   A 1 101 ? 19.728 -0.457  -12.220 0.48 25.11 ?  101 ASN   A H    1 
ATOM   2374 H HA   A ASN   A 1 101 ? 18.753 1.354   -13.694 0.52 27.28 ?  101 ASN   A HA   1 
ATOM   2375 H HA   B ASN   A 1 101 ? 19.138 0.473   -14.599 0.48 26.66 ?  101 ASN   A HA   1 
ATOM   2376 H HB2  A ASN   A 1 101 ? 19.307 2.661   -11.258 0.52 26.10 ?  101 ASN   A HB2  1 
ATOM   2377 H HB2  B ASN   A 1 101 ? 19.826 1.955   -12.297 0.48 27.74 ?  101 ASN   A HB2  1 
ATOM   2378 H HB3  A ASN   A 1 101 ? 18.609 3.339   -12.515 0.52 26.10 ?  101 ASN   A HB3  1 
ATOM   2379 H HB3  B ASN   A 1 101 ? 19.206 2.594   -13.613 0.48 27.74 ?  101 ASN   A HB3  1 
ATOM   2380 H HD21 A ASN   A 1 101 ? 16.382 2.067   -9.849  0.52 27.25 ?  101 ASN   A HD21 1 
ATOM   2381 H HD21 B ASN   A 1 101 ? 16.663 2.233   -11.178 0.48 29.82 ?  101 ASN   A HD21 1 
ATOM   2382 H HD22 A ASN   A 1 101 ? 17.748 2.642   -9.703  0.52 27.25 ?  101 ASN   A HD22 1 
ATOM   2383 H HD22 B ASN   A 1 101 ? 17.976 2.936   -11.208 0.48 29.82 ?  101 ASN   A HD22 1 
ATOM   2384 N N    A LYS   A 1 102 ? 21.772 1.187   -13.235 0.52 26.60 ?  102 LYS   A N    1 
ATOM   2385 N N    B LYS   A 1 102 ? 22.213 0.435   -14.002 0.48 24.92 ?  102 LYS   A N    1 
ATOM   2386 C CA   A LYS   A 1 102 ? 23.057 1.415   -13.886 0.52 28.00 ?  102 LYS   A CA   1 
ATOM   2387 C CA   B LYS   A 1 102 ? 23.542 0.614   -14.581 0.48 25.83 ?  102 LYS   A CA   1 
ATOM   2388 C C    A LYS   A 1 102 ? 23.407 0.328   -14.891 0.52 28.71 ?  102 LYS   A C    1 
ATOM   2389 C C    B LYS   A 1 102 ? 23.936 -0.534  -15.507 0.48 24.74 ?  102 LYS   A C    1 
ATOM   2390 O O    A LYS   A 1 102 ? 24.484 0.389   -15.494 0.52 29.75 ?  102 LYS   A O    1 
ATOM   2391 O O    B LYS   A 1 102 ? 25.082 -0.582  -15.966 0.48 25.29 ?  102 LYS   A O    1 
ATOM   2392 C CB   A LYS   A 1 102 ? 24.182 1.511   -12.848 0.52 29.36 ?  102 LYS   A CB   1 
ATOM   2393 C CB   B LYS   A 1 102 ? 24.603 0.723   -13.478 0.48 28.37 ?  102 LYS   A CB   1 
ATOM   2394 C CG   A LYS   A 1 102 ? 24.012 2.608   -11.817 0.52 30.63 ?  102 LYS   A CG   1 
ATOM   2395 C CG   B LYS   A 1 102 ? 24.537 1.960   -12.596 0.48 31.02 ?  102 LYS   A CG   1 
ATOM   2396 C CD   A LYS   A 1 102 ? 25.180 2.599   -10.843 0.52 32.29 ?  102 LYS   A CD   1 
ATOM   2397 C CD   B LYS   A 1 102 ? 25.579 1.860   -11.478 0.48 33.67 ?  102 LYS   A CD   1 
ATOM   2398 C CE   A LYS   A 1 102 ? 25.046 3.674   -9.778  0.52 33.56 ?  102 LYS   A CE   1 
ATOM   2399 C CE   B LYS   A 1 102 ? 25.523 3.046   -10.528 0.48 35.95 ?  102 LYS   A CE   1 
ATOM   2400 N NZ   A LYS   A 1 102 ? 26.140 3.577   -8.766  0.52 34.36 ?  102 LYS   A NZ   1 
ATOM   2401 N NZ   B LYS   A 1 102 ? 25.732 2.628   -9.107  0.48 37.14 ?  102 LYS   A NZ   1 
ATOM   2402 H H    A LYS   A 1 102 ? 21.784 0.522   -12.686 0.52 31.92 ?  102 LYS   A H    1 
ATOM   2403 H H    B LYS   A 1 102 ? 22.215 -0.055  -13.295 0.48 29.90 ?  102 LYS   A H    1 
ATOM   2404 H HA   A LYS   A 1 102 ? 23.025 2.252   -14.366 0.52 33.61 ?  102 LYS   A HA   1 
ATOM   2405 H HA   B LYS   A 1 102 ? 23.554 1.444   -15.088 0.48 30.99 ?  102 LYS   A HA   1 
ATOM   2406 H HB2  A LYS   A 1 102 ? 24.238 0.667   -12.373 0.52 35.23 ?  102 LYS   A HB2  1 
ATOM   2407 H HB2  B LYS   A 1 102 ? 24.520 -0.049  -12.897 0.48 34.05 ?  102 LYS   A HB2  1 
ATOM   2408 H HB3  A LYS   A 1 102 ? 25.018 1.674   -13.315 0.52 35.23 ?  102 LYS   A HB3  1 
ATOM   2409 H HB3  B LYS   A 1 102 ? 25.480 0.716   -13.896 0.48 34.05 ?  102 LYS   A HB3  1 
ATOM   2410 H HG2  A LYS   A 1 102 ? 23.988 3.469   -12.263 0.52 36.76 ?  102 LYS   A HG2  1 
ATOM   2411 H HG2  B LYS   A 1 102 ? 24.733 2.749   -13.125 0.48 37.22 ?  102 LYS   A HG2  1 
ATOM   2412 H HG3  A LYS   A 1 102 ? 23.193 2.459   -11.320 0.52 36.76 ?  102 LYS   A HG3  1 
ATOM   2413 H HG3  B LYS   A 1 102 ? 23.658 2.029   -12.194 0.48 37.22 ?  102 LYS   A HG3  1 
ATOM   2414 H HD2  A LYS   A 1 102 ? 25.217 1.736   -10.400 0.52 38.75 ?  102 LYS   A HD2  1 
ATOM   2415 H HD2  B LYS   A 1 102 ? 25.424 1.053   -10.962 0.48 40.40 ?  102 LYS   A HD2  1 
ATOM   2416 H HD3  A LYS   A 1 102 ? 26.003 2.757   -11.332 0.52 38.75 ?  102 LYS   A HD3  1 
ATOM   2417 H HD3  B LYS   A 1 102 ? 26.465 1.832   -11.873 0.48 40.40 ?  102 LYS   A HD3  1 
ATOM   2418 H HE2  A LYS   A 1 102 ? 25.096 4.548   -10.198 0.52 40.28 ?  102 LYS   A HE2  1 
ATOM   2419 H HE2  B LYS   A 1 102 ? 26.225 3.675   -10.763 0.48 43.14 ?  102 LYS   A HE2  1 
ATOM   2420 H HE3  A LYS   A 1 102 ? 24.197 3.568   -9.321  0.52 40.28 ?  102 LYS   A HE3  1 
ATOM   2421 H HE3  B LYS   A 1 102 ? 24.656 3.471   -10.597 0.48 43.14 ?  102 LYS   A HE3  1 
ATOM   2422 H HZ1  A LYS   A 1 102 ? 26.044 4.213   -8.153  0.52 41.24 ?  102 LYS   A HZ1  1 
ATOM   2423 H HZ1  B LYS   A 1 102 ? 25.548 3.306   -8.561  0.48 44.57 ?  102 LYS   A HZ1  1 
ATOM   2424 H HZ2  A LYS   A 1 102 ? 26.113 2.782   -8.366  0.52 41.24 ?  102 LYS   A HZ2  1 
ATOM   2425 H HZ2  B LYS   A 1 102 ? 25.197 1.945   -8.909  0.48 44.57 ?  102 LYS   A HZ2  1 
ATOM   2426 H HZ3  A LYS   A 1 102 ? 26.931 3.673   -9.164  0.52 41.24 ?  102 LYS   A HZ3  1 
ATOM   2427 H HZ3  B LYS   A 1 102 ? 26.576 2.376   -8.984  0.48 44.57 ?  102 LYS   A HZ3  1 
ATOM   2428 N N    A GLY   A 1 103 ? 22.535 -0.662  -15.083 0.52 29.49 ?  103 GLY   A N    1 
ATOM   2429 N N    B GLY   A 1 103 ? 23.033 -1.473  -15.771 0.48 23.15 ?  103 GLY   A N    1 
ATOM   2430 C CA   A GLY   A 1 103 ? 22.804 -1.751  -16.002 0.52 30.07 ?  103 GLY   A CA   1 
ATOM   2431 C CA   B GLY   A 1 103 ? 23.374 -2.619  -16.592 0.48 22.79 ?  103 GLY   A CA   1 
ATOM   2432 C C    A GLY   A 1 103 ? 23.638 -2.876  -15.434 0.52 30.60 ?  103 GLY   A C    1 
ATOM   2433 C C    B GLY   A 1 103 ? 24.166 -3.695  -15.882 0.48 22.50 ?  103 GLY   A C    1 
ATOM   2434 O O    A GLY   A 1 103 ? 24.164 -3.687  -16.202 0.52 31.77 ?  103 GLY   A O    1 
ATOM   2435 O O    B GLY   A 1 103 ? 24.776 -4.542  -16.543 0.48 23.42 ?  103 GLY   A O    1 
ATOM   2436 H H    A GLY   A 1 103 ? 21.774 -0.723  -14.692 0.52 35.39 ?  103 GLY   A H    1 
ATOM   2437 H H    B GLY   A 1 103 ? 22.223 -1.460  -15.490 0.48 27.78 ?  103 GLY   A H    1 
ATOM   2438 H HA2  A GLY   A 1 103 ? 21.957 -2.112  -16.326 0.52 36.08 ?  103 GLY   A HA2  1 
ATOM   2439 H HA2  B GLY   A 1 103 ? 22.557 -3.022  -16.913 0.48 27.35 ?  103 GLY   A HA2  1 
ATOM   2440 H HA3  A GLY   A 1 103 ? 23.290 -1.407  -16.762 0.52 36.08 ?  103 GLY   A HA3  1 
ATOM   2441 H HA3  B GLY   A 1 103 ? 23.880 -2.308  -17.365 0.48 27.35 ?  103 GLY   A HA3  1 
ATOM   2442 N N    A GLU   A 1 104 ? 23.785 -2.949  -14.115 0.52 29.12 ?  104 GLU   A N    1 
ATOM   2443 N N    B GLU   A 1 104 ? 24.160 -3.705  -14.553 0.48 20.40 ?  104 GLU   A N    1 
ATOM   2444 C CA   A GLU   A 1 104 ? 24.636 -3.958  -13.500 0.52 27.98 ?  104 GLU   A CA   1 
ATOM   2445 C CA   B GLU   A 1 104 ? 24.988 -4.624  -13.785 0.48 19.30 ?  104 GLU   A CA   1 
ATOM   2446 C C    A GLU   A 1 104 ? 23.932 -5.310  -13.419 0.52 28.28 ?  104 GLU   A C    1 
ATOM   2447 C C    B GLU   A 1 104 ? 24.269 -5.954  -13.575 0.48 19.41 ?  104 GLU   A C    1 
ATOM   2448 O O    A GLU   A 1 104 ? 22.712 -5.397  -13.249 0.52 28.27 ?  104 GLU   A O    1 
ATOM   2449 O O    B GLU   A 1 104 ? 23.048 -5.999  -13.396 0.48 20.13 ?  104 GLU   A O    1 
ATOM   2450 C CB   A GLU   A 1 104 ? 25.103 -3.480  -12.122 0.52 26.41 ?  104 GLU   A CB   1 
ATOM   2451 C CB   B GLU   A 1 104 ? 25.396 -3.982  -12.457 0.48 18.61 ?  104 GLU   A CB   1 
ATOM   2452 C CG   A GLU   A 1 104 ? 25.974 -2.223  -12.235 0.52 25.59 ?  104 GLU   A CG   1 
ATOM   2453 C CG   B GLU   A 1 104 ? 26.234 -2.717  -12.671 0.48 19.26 ?  104 GLU   A CG   1 
ATOM   2454 C CD   A GLU   A 1 104 ? 26.296 -1.530  -10.916 0.52 24.09 ?  104 GLU   A CD   1 
ATOM   2455 C CD   B GLU   A 1 104 ? 26.601 -1.971  -11.395 0.48 19.29 ?  104 GLU   A CD   1 
ATOM   2456 O OE1  A GLU   A 1 104 ? 25.714 -1.881  -9.870  0.52 22.12 ?  104 GLU   A OE1  1 
ATOM   2457 O OE1  B GLU   A 1 104 ? 26.054 -2.270  -10.315 0.48 19.54 ?  104 GLU   A OE1  1 
ATOM   2458 O OE2  A GLU   A 1 104 ? 27.136 -0.602  -10.939 0.52 24.99 -1 104 GLU   A OE2  1 
ATOM   2459 O OE2  B GLU   A 1 104 ? 27.443 -1.049  -11.491 0.48 19.77 -1 104 GLU   A OE2  1 
ATOM   2460 H H    A GLU   A 1 104 ? 23.414 -2.417  -13.556 0.52 34.95 ?  104 GLU   A H    1 
ATOM   2461 H H    B GLU   A 1 104 ? 23.676 -3.179  -14.074 0.48 24.48 ?  104 GLU   A H    1 
ATOM   2462 H HA   A GLU   A 1 104 ? 25.419 -4.075  -14.055 0.52 33.57 ?  104 GLU   A HA   1 
ATOM   2463 H HA   B GLU   A 1 104 ? 25.800 -4.798  -14.289 0.48 23.16 ?  104 GLU   A HA   1 
ATOM   2464 H HB2  A GLU   A 1 104 ? 24.326 -3.274  -11.579 0.52 31.69 ?  104 GLU   A HB2  1 
ATOM   2465 H HB2  B GLU   A 1 104 ? 24.602 -3.736  -11.963 0.48 22.33 ?  104 GLU   A HB2  1 
ATOM   2466 H HB3  A GLU   A 1 104 ? 25.625 -4.186  -11.707 0.52 31.69 ?  104 GLU   A HB3  1 
ATOM   2467 H HB3  B GLU   A 1 104 ? 25.931 -4.612  -11.953 0.48 22.33 ?  104 GLU   A HB3  1 
ATOM   2468 H HG2  A GLU   A 1 104 ? 26.808 -2.472  -12.662 0.52 30.71 ?  104 GLU   A HG2  1 
ATOM   2469 H HG2  B GLU   A 1 104 ? 27.052 -2.960  -13.132 0.48 23.12 ?  104 GLU   A HG2  1 
ATOM   2470 H HG3  A GLU   A 1 104 ? 25.506 -1.578  -12.785 0.52 30.71 ?  104 GLU   A HG3  1 
ATOM   2471 H HG3  B GLU   A 1 104 ? 25.724 -2.095  -13.216 0.48 23.12 ?  104 GLU   A HG3  1 
ATOM   2472 N N    A ASP   A 1 105 ? 24.728 -6.371  -13.547 0.52 28.75 ?  105 ASP   A N    1 
ATOM   2473 N N    B ASP   A 1 105 ? 25.049 -7.033  -13.624 0.48 19.93 ?  105 ASP   A N    1 
ATOM   2474 C CA   A ASP   A 1 105 ? 24.212 -7.731  -13.656 0.52 29.70 ?  105 ASP   A CA   1 
ATOM   2475 C CA   B ASP   A 1 105 ? 24.539 -8.400  -13.628 0.48 21.32 ?  105 ASP   A CA   1 
ATOM   2476 C C    A ASP   A 1 105 ? 23.518 -8.138  -12.359 0.52 28.27 ?  105 ASP   A C    1 
ATOM   2477 C C    B ASP   A 1 105 ? 23.776 -8.725  -12.345 0.48 18.96 ?  105 ASP   A C    1 
ATOM   2478 O O    A ASP   A 1 105 ? 24.122 -8.096  -11.284 0.52 27.60 ?  105 ASP   A O    1 
ATOM   2479 O O    B ASP   A 1 105 ? 24.349 -8.728  -11.253 0.48 15.96 ?  105 ASP   A O    1 
ATOM   2480 C CB   A ASP   A 1 105 ? 25.375 -8.675  -13.959 0.52 32.08 ?  105 ASP   A CB   1 
ATOM   2481 C CB   B ASP   A 1 105 ? 25.737 -9.340  -13.789 0.48 24.37 ?  105 ASP   A CB   1 
ATOM   2482 C CG   A ASP   A 1 105 ? 24.921 -10.090 -14.229 0.52 34.27 ?  105 ASP   A CG   1 
ATOM   2483 C CG   B ASP   A 1 105 ? 25.333 -10.769 -14.051 0.48 27.31 ?  105 ASP   A CG   1 
ATOM   2484 O OD1  A ASP   A 1 105 ? 23.695 -10.317 -14.311 0.52 34.63 ?  105 ASP   A OD1  1 
ATOM   2485 O OD1  B ASP   A 1 105 ? 24.120 -11.051 -14.133 0.48 27.44 ?  105 ASP   A OD1  1 
ATOM   2486 O OD2  A ASP   A 1 105 ? 25.794 -10.973 -14.366 0.52 35.66 -1 105 ASP   A OD2  1 
ATOM   2487 O OD2  B ASP   A 1 105 ? 26.247 -11.614 -14.169 0.48 28.61 -1 105 ASP   A OD2  1 
ATOM   2488 H H    A ASP   A 1 105 ? 25.586 -6.332  -13.571 0.52 34.50 ?  105 ASP   A H    1 
ATOM   2489 H H    B ASP   A 1 105 ? 25.899 -6.988  -13.685 0.48 23.91 ?  105 ASP   A H    1 
ATOM   2490 H HA   A ASP   A 1 105 ? 23.573 -7.795  -14.384 0.52 35.64 ?  105 ASP   A HA   1 
ATOM   2491 H HA   B ASP   A 1 105 ? 23.950 -8.529  -14.381 0.48 25.58 ?  105 ASP   A HA   1 
ATOM   2492 H HB2  A ASP   A 1 105 ? 25.842 -8.366  -14.754 0.52 38.50 ?  105 ASP   A HB2  1 
ATOM   2493 H HB2  B ASP   A 1 105 ? 26.292 -9.029  -14.530 0.48 29.24 ?  105 ASP   A HB2  1 
ATOM   2494 H HB3  A ASP   A 1 105 ? 25.988 -8.683  -13.204 0.52 38.50 ?  105 ASP   A HB3  1 
ATOM   2495 H HB3  B ASP   A 1 105 ? 26.259 -9.346  -12.973 0.48 29.24 ?  105 ASP   A HB3  1 
ATOM   2496 N N    A ILE   A 1 106 ? 22.247 -8.538  -12.462 0.52 27.46 ?  106 ILE   A N    1 
ATOM   2497 N N    B ILE   A 1 106 ? 22.480 -9.024  -12.477 0.48 20.26 ?  106 ILE   A N    1 
ATOM   2498 C CA   A ILE   A 1 106 ? 21.495 -8.963  -11.285 0.52 26.20 ?  106 ILE   A CA   1 
ATOM   2499 C CA   B ILE   A 1 106 ? 21.682 -9.391  -11.311 0.48 20.90 ?  106 ILE   A CA   1 
ATOM   2500 C C    A ILE   A 1 106 ? 22.036 -10.263 -10.705 0.52 24.91 ?  106 ILE   A C    1 
ATOM   2501 C C    B ILE   A 1 106 ? 22.212 -10.651 -10.646 0.48 20.90 ?  106 ILE   A C    1 
ATOM   2502 O O    A ILE   A 1 106 ? 21.812 -10.546 -9.523  0.52 23.53 ?  106 ILE   A O    1 
ATOM   2503 O O    B ILE   A 1 106 ? 21.984 -10.857 -9.450  0.48 19.80 ?  106 ILE   A O    1 
ATOM   2504 C CB   A ILE   A 1 106 ? 19.988 -9.060  -11.600 0.52 27.27 ?  106 ILE   A CB   1 
ATOM   2505 C CB   B ILE   A 1 106 ? 20.184 -9.514  -11.674 0.48 23.17 ?  106 ILE   A CB   1 
ATOM   2506 C CG1  A ILE   A 1 106 ? 19.160 -9.120  -10.312 0.52 28.15 ?  106 ILE   A CG1  1 
ATOM   2507 C CG1  B ILE   A 1 106 ? 19.312 -9.442  -10.417 0.48 24.63 ?  106 ILE   A CG1  1 
ATOM   2508 C CG2  A ILE   A 1 106 ? 19.701 -10.294 -12.424 0.52 27.50 ?  106 ILE   A CG2  1 
ATOM   2509 C CG2  B ILE   A 1 106 ? 19.915 -10.816 -12.387 0.48 23.74 ?  106 ILE   A CG2  1 
ATOM   2510 C CD1  A ILE   A 1 106 ? 19.314 -7.907  -9.425  0.52 29.04 ?  106 ILE   A CD1  1 
ATOM   2511 C CD1  B ILE   A 1 106 ? 19.409 -8.130  -9.676  0.48 25.60 ?  106 ILE   A CD1  1 
ATOM   2512 H H    A ILE   A 1 106 ? 21.805 -8.566  -13.194 0.52 32.95 ?  106 ILE   A H    1 
ATOM   2513 H H    B ILE   A 1 106 ? 22.044 -9.012  -13.213 0.48 24.31 ?  106 ILE   A H    1 
ATOM   2514 H HA   A ILE   A 1 106 ? 21.611 -8.287  -10.605 0.52 31.44 ?  106 ILE   A HA   1 
ATOM   2515 H HA   B ILE   A 1 106 ? 21.773 -8.684  -10.659 0.48 25.07 ?  106 ILE   A HA   1 
ATOM   2516 H HB   A ILE   A 1 106 ? 19.724 -8.276  -12.106 0.52 32.72 ?  106 ILE   A HB   1 
ATOM   2517 H HB   B ILE   A 1 106 ? 19.948 -8.778  -12.258 0.48 27.80 ?  106 ILE   A HB   1 
ATOM   2518 H HG12 A ILE   A 1 106 ? 18.222 -9.194  -10.549 0.52 33.78 ?  106 ILE   A HG12 1 
ATOM   2519 H HG12 B ILE   A 1 106 ? 18.386 -9.566  -10.672 0.48 29.55 ?  106 ILE   A HG12 1 
ATOM   2520 H HG13 A ILE   A 1 106 ? 19.430 -9.898  -9.800  0.52 33.78 ?  106 ILE   A HG13 1 
ATOM   2521 H HG13 B ILE   A 1 106 ? 19.583 -10.144 -9.805  0.48 29.55 ?  106 ILE   A HG13 1 
ATOM   2522 H HG21 A ILE   A 1 106 ? 18.829 -10.199 -12.833 0.52 33.00 ?  106 ILE   A HG21 1 
ATOM   2523 H HG21 B ILE   A 1 106 ? 19.057 -10.754 -12.830 0.48 28.49 ?  106 ILE   A HG21 1 
ATOM   2524 H HG22 A ILE   A 1 106 ? 20.383 -10.380 -13.104 0.52 33.00 ?  106 ILE   A HG22 1 
ATOM   2525 H HG22 B ILE   A 1 106 ? 20.618 -10.968 -13.033 0.48 28.49 ?  106 ILE   A HG22 1 
ATOM   2526 H HG23 A ILE   A 1 106 ? 19.711 -11.070 -11.841 0.52 33.00 ?  106 ILE   A HG23 1 
ATOM   2527 H HG23 B ILE   A 1 106 ? 19.901 -11.534 -11.733 0.48 28.49 ?  106 ILE   A HG23 1 
ATOM   2528 H HD11 A ILE   A 1 106 ? 18.579 -7.884  -8.795  0.52 34.85 ?  106 ILE   A HD11 1 
ATOM   2529 H HD11 B ILE   A 1 106 ? 18.648 -8.045  -9.083  0.48 30.72 ?  106 ILE   A HD11 1 
ATOM   2530 H HD12 A ILE   A 1 106 ? 20.157 -7.970  -8.947  0.52 34.85 ?  106 ILE   A HD12 1 
ATOM   2531 H HD12 B ILE   A 1 106 ? 20.232 -8.115  -9.160  0.48 30.72 ?  106 ILE   A HD12 1 
ATOM   2532 H HD13 A ILE   A 1 106 ? 19.304 -7.110  -9.978  0.52 34.85 ?  106 ILE   A HD13 1 
ATOM   2533 H HD13 B ILE   A 1 106 ? 19.409 -7.404  -10.319 0.48 30.72 ?  106 ILE   A HD13 1 
ATOM   2534 N N    A GLN   A 1 107 ? 22.764 -11.054 -11.498 0.52 26.25 ?  107 GLN   A N    1 
ATOM   2535 N N    B GLN   A 1 107 ? 22.938 -11.494 -11.388 0.48 22.42 ?  107 GLN   A N    1 
ATOM   2536 C CA   A GLN   A 1 107 ? 23.360 -12.283 -10.983 0.52 27.85 ?  107 GLN   A CA   1 
ATOM   2537 C CA   B GLN   A 1 107 ? 23.579 -12.656 -10.783 0.48 25.13 ?  107 GLN   A CA   1 
ATOM   2538 C C    A GLN   A 1 107 ? 24.345 -12.012 -9.852  0.52 24.75 ?  107 GLN   A C    1 
ATOM   2539 C C    B GLN   A 1 107 ? 24.552 -12.252 -9.681  0.48 22.78 ?  107 GLN   A C    1 
ATOM   2540 O O    A GLN   A 1 107 ? 24.579 -12.894 -9.019  0.52 25.96 ?  107 GLN   A O    1 
ATOM   2541 O O    B GLN   A 1 107 ? 24.850 -13.062 -8.794  0.48 23.70 ?  107 GLN   A O    1 
ATOM   2542 C CB   A GLN   A 1 107 ? 24.050 -13.043 -12.123 0.52 32.76 ?  107 GLN   A CB   1 
ATOM   2543 C CB   B GLN   A 1 107 ? 24.287 -13.483 -11.865 0.48 30.11 ?  107 GLN   A CB   1 
ATOM   2544 C CG   A GLN   A 1 107 ? 23.144 -13.327 -13.314 0.52 37.83 ?  107 GLN   A CG   1 
ATOM   2545 C CG   B GLN   A 1 107 ? 23.398 -13.839 -13.056 0.48 35.13 ?  107 GLN   A CG   1 
ATOM   2546 C CD   A GLN   A 1 107 ? 21.907 -14.118 -12.933 0.52 42.04 ?  107 GLN   A CD   1 
ATOM   2547 C CD   B GLN   A 1 107 ? 22.166 -14.630 -12.656 0.48 39.31 ?  107 GLN   A CD   1 
ATOM   2548 O OE1  A GLN   A 1 107 ? 21.998 -15.168 -12.294 0.52 43.60 ?  107 GLN   A OE1  1 
ATOM   2549 O OE1  B GLN   A 1 107 ? 22.241 -15.546 -11.834 0.48 40.78 ?  107 GLN   A OE1  1 
ATOM   2550 N NE2  A GLN   A 1 107 ? 20.740 -13.614 -13.319 0.52 43.37 ?  107 GLN   A NE2  1 
ATOM   2551 N NE2  B GLN   A 1 107 ? 21.021 -14.276 -13.236 0.48 40.81 ?  107 GLN   A NE2  1 
ATOM   2552 H H    A GLN   A 1 107 ? 22.932 -10.897 -12.325 0.52 31.50 ?  107 GLN   A H    1 
ATOM   2553 H H    B GLN   A 1 107 ? 23.077 -11.409 -12.234 0.48 26.90 ?  107 GLN   A H    1 
ATOM   2554 H HA   A GLN   A 1 107 ? 22.660 -12.853 -10.634 0.52 33.43 ?  107 GLN   A HA   1 
ATOM   2555 H HA   B GLN   A 1 107 ? 22.900 -13.220 -10.390 0.48 30.15 ?  107 GLN   A HA   1 
ATOM   2556 H HB2  A GLN   A 1 107 ? 24.800 -12.519 -12.445 0.52 39.32 ?  107 GLN   A HB2  1 
ATOM   2557 H HB2  B GLN   A 1 107 ? 25.043 -12.982 -12.207 0.48 36.14 ?  107 GLN   A HB2  1 
ATOM   2558 H HB3  A GLN   A 1 107 ? 24.367 -13.897 -11.788 0.52 39.32 ?  107 GLN   A HB3  1 
ATOM   2559 H HB3  B GLN   A 1 107 ? 24.595 -14.318 -11.477 0.48 36.14 ?  107 GLN   A HB3  1 
ATOM   2560 H HG2  A GLN   A 1 107 ? 22.854 -12.486 -13.701 0.52 45.39 ?  107 GLN   A HG2  1 
ATOM   2561 H HG2  B GLN   A 1 107 ? 23.100 -13.024 -13.491 0.48 42.16 ?  107 GLN   A HG2  1 
ATOM   2562 H HG3  A GLN   A 1 107 ? 23.639 -13.840 -13.973 0.52 45.39 ?  107 GLN   A HG3  1 
ATOM   2563 H HG3  B GLN   A 1 107 ? 23.907 -14.377 -13.683 0.48 42.16 ?  107 GLN   A HG3  1 
ATOM   2564 H HE21 A GLN   A 1 107 ? 20.715 -12.879 -13.764 0.52 52.04 ?  107 GLN   A HE21 1 
ATOM   2565 H HE21 B GLN   A 1 107 ? 21.006 -13.629 -13.805 0.48 48.98 ?  107 GLN   A HE21 1 
ATOM   2566 H HE22 A GLN   A 1 107 ? 20.011 -14.027 -13.126 0.52 52.04 ?  107 GLN   A HE22 1 
ATOM   2567 H HE22 B GLN   A 1 107 ? 20.294 -14.692 -13.042 0.48 48.98 ?  107 GLN   A HE22 1 
ATOM   2568 N N    A LEU   A 1 108 ? 24.906 -10.803 -9.784  0.52 20.17 ?  108 LEU   A N    1 
ATOM   2569 N N    B LEU   A 1 108 ? 25.035 -11.009 -9.700  0.48 19.56 ?  108 LEU   A N    1 
ATOM   2570 C CA   A LEU   A 1 108 ? 25.839 -10.454 -8.719  0.52 17.22 ?  108 LEU   A CA   1 
ATOM   2571 C CA   B LEU   A 1 108 ? 25.902 -10.521 -8.636  0.48 17.31 ?  108 LEU   A CA   1 
ATOM   2572 C C    A LEU   A 1 108 ? 25.151 -10.287 -7.369  0.52 15.14 ?  108 LEU   A C    1 
ATOM   2573 C C    B LEU   A 1 108 ? 25.154 -10.288 -7.330  0.48 15.27 ?  108 LEU   A C    1 
ATOM   2574 O O    A LEU   A 1 108 ? 25.838 -10.129 -6.356  0.52 15.47 ?  108 LEU   A O    1 
ATOM   2575 O O    B LEU   A 1 108 ? 25.802 -10.070 -6.301  0.48 15.58 ?  108 LEU   A O    1 
ATOM   2576 C CB   A LEU   A 1 108 ? 26.603 -9.180  -9.094  0.52 17.16 ?  108 LEU   A CB   1 
ATOM   2577 C CB   B LEU   A 1 108 ? 26.627 -9.244  -9.077  0.48 17.67 ?  108 LEU   A CB   1 
ATOM   2578 C CG   A LEU   A 1 108 ? 27.591 -9.352  -10.250 0.52 18.69 ?  108 LEU   A CG   1 
ATOM   2579 C CG   B LEU   A 1 108 ? 27.689 -9.445  -10.160 0.48 18.86 ?  108 LEU   A CG   1 
ATOM   2580 C CD1  A LEU   A 1 108 ? 28.014 -8.003  -10.808 0.52 19.60 ?  108 LEU   A CD1  1 
ATOM   2581 C CD1  B LEU   A 1 108 ? 28.180 -8.113  -10.707 0.48 19.51 ?  108 LEU   A CD1  1 
ATOM   2582 C CD2  A LEU   A 1 108 ? 28.813 -10.142 -9.802  0.52 20.02 ?  108 LEU   A CD2  1 
ATOM   2583 C CD2  B LEU   A 1 108 ? 28.860 -10.256 -9.620  0.48 20.20 ?  108 LEU   A CD2  1 
ATOM   2584 H H    A LEU   A 1 108 ? 24.754 -10.171 -10.342 0.52 24.20 ?  108 LEU   A H    1 
ATOM   2585 H H    B LEU   A 1 108 ? 24.877 -10.440 -10.318 0.48 23.47 ?  108 LEU   A H    1 
ATOM   2586 H HA   A LEU   A 1 108 ? 26.484 -11.171 -8.627  0.52 20.67 ?  108 LEU   A HA   1 
ATOM   2587 H HA   B LEU   A 1 108 ? 26.576 -11.195 -8.460  0.48 20.77 ?  108 LEU   A HA   1 
ATOM   2588 H HB2  A LEU   A 1 108 ? 25.961 -8.502  -9.356  0.52 20.59 ?  108 LEU   A HB2  1 
ATOM   2589 H HB2  B LEU   A 1 108 ? 25.970 -8.621  -9.423  0.48 21.20 ?  108 LEU   A HB2  1 
ATOM   2590 H HB3  A LEU   A 1 108 ? 27.101 -8.882  -8.321  0.52 20.59 ?  108 LEU   A HB3  1 
ATOM   2591 H HB3  B LEU   A 1 108 ? 27.066 -8.860  -8.304  0.48 21.20 ?  108 LEU   A HB3  1 
ATOM   2592 H HG   A LEU   A 1 108 ? 27.160 -9.849  -10.964 0.52 22.43 ?  108 LEU   A HG   1 
ATOM   2593 H HG   B LEU   A 1 108 ? 27.299 -9.941  -10.896 0.48 22.63 ?  108 LEU   A HG   1 
ATOM   2594 H HD11 A LEU   A 1 108 ? 28.620 -8.144  -11.553 0.52 23.51 ?  108 LEU   A HD11 1 
ATOM   2595 H HD11 B LEU   A 1 108 ? 28.838 -8.278  -11.402 0.48 23.41 ?  108 LEU   A HD11 1 
ATOM   2596 H HD12 A LEU   A 1 108 ? 27.227 -7.523  -11.108 0.52 23.51 ?  108 LEU   A HD12 1 
ATOM   2597 H HD12 B LEU   A 1 108 ? 27.427 -7.624  -11.076 0.48 23.41 ?  108 LEU   A HD12 1 
ATOM   2598 H HD13 A LEU   A 1 108 ? 28.462 -7.499  -10.110 0.52 23.51 ?  108 LEU   A HD13 1 
ATOM   2599 H HD13 B LEU   A 1 108 ? 28.583 -7.602  -9.987  0.48 23.41 ?  108 LEU   A HD13 1 
ATOM   2600 H HD21 A LEU   A 1 108 ? 29.456 -10.166 -10.526 0.52 24.02 ?  108 LEU   A HD21 1 
ATOM   2601 H HD21 B LEU   A 1 108 ? 29.584 -10.229 -10.263 0.48 24.24 ?  108 LEU   A HD21 1 
ATOM   2602 H HD22 A LEU   A 1 108 ? 29.201 -9.708  -9.026  0.52 24.02 ?  108 LEU   A HD22 1 
ATOM   2603 H HD22 B LEU   A 1 108 ? 29.148 -9.869  -8.779  0.48 24.24 ?  108 LEU   A HD22 1 
ATOM   2604 H HD23 A LEU   A 1 108 ? 28.539 -11.045 -9.572  0.52 24.02 ?  108 LEU   A HD23 1 
ATOM   2605 H HD23 B LEU   A 1 108 ? 28.571 -11.171 -9.482  0.48 24.24 ?  108 LEU   A HD23 1 
ATOM   2606 N N    . LEU   A 1 109 ? 23.816 -10.339 -7.331  1.00 14.27 ?  109 LEU   A N    1 
ATOM   2607 C CA   . LEU   A 1 109 ? 23.095 -10.196 -6.072  1.00 13.47 ?  109 LEU   A CA   1 
ATOM   2608 C C    . LEU   A 1 109 ? 23.410 -11.344 -5.117  1.00 12.35 ?  109 LEU   A C    1 
ATOM   2609 O O    . LEU   A 1 109 ? 23.538 -11.139 -3.907  1.00 13.03 ?  109 LEU   A O    1 
ATOM   2610 C CB   . LEU   A 1 109 ? 21.594 -10.111 -6.344  1.00 14.39 ?  109 LEU   A CB   1 
ATOM   2611 C CG   . LEU   A 1 109 ? 20.687 -9.829  -5.143  1.00 15.00 ?  109 LEU   A CG   1 
ATOM   2612 C CD1  . LEU   A 1 109 ? 21.123 -8.565  -4.407  1.00 14.56 ?  109 LEU   A CD1  1 
ATOM   2613 C CD2  . LEU   A 1 109 ? 19.215 -9.711  -5.575  1.00 16.49 ?  109 LEU   A CD2  1 
ATOM   2614 H H    A LEU   A 1 109 ? 23.309 -10.462 -8.017  0.52 17.12 ?  109 LEU   A H    1 
ATOM   2615 H H    B LEU   A 1 109 ? 23.320 -10.458 -8.025  0.48 17.12 ?  109 LEU   A H    1 
ATOM   2616 H HA   . LEU   A 1 109 ? 23.373 -9.369  -5.650  1.00 16.17 ?  109 LEU   A HA   1 
ATOM   2617 H HB2  . LEU   A 1 109 ? 21.443 -9.400  -6.986  1.00 17.26 ?  109 LEU   A HB2  1 
ATOM   2618 H HB3  . LEU   A 1 109 ? 21.306 -10.953 -6.724  1.00 17.26 ?  109 LEU   A HB3  1 
ATOM   2619 H HG   . LEU   A 1 109 ? 20.747 -10.566 -4.519  1.00 18.00 ?  109 LEU   A HG   1 
ATOM   2620 H HD11 . LEU   A 1 109 ? 20.441 -8.314  -3.768  1.00 17.47 ?  109 LEU   A HD11 1 
ATOM   2621 H HD12 . LEU   A 1 109 ? 21.962 -8.735  -3.954  1.00 17.47 ?  109 LEU   A HD12 1 
ATOM   2622 H HD13 . LEU   A 1 109 ? 21.241 -7.846  -5.058  1.00 17.47 ?  109 LEU   A HD13 1 
ATOM   2623 H HD21 . LEU   A 1 109 ? 18.685 -9.390  -4.825  1.00 19.79 ?  109 LEU   A HD21 1 
ATOM   2624 H HD22 . LEU   A 1 109 ? 19.146 -9.088  -6.315  1.00 19.79 ?  109 LEU   A HD22 1 
ATOM   2625 H HD23 . LEU   A 1 109 ? 18.892 -10.586 -5.852  1.00 19.79 ?  109 LEU   A HD23 1 
ATOM   2626 N N    . LYS   A 1 110 ? 23.553 -12.566 -5.638  1.00 13.37 ?  110 LYS   A N    1 
ATOM   2627 C CA   . LYS   A 1 110 ? 23.927 -13.675 -4.764  1.00 13.45 ?  110 LYS   A CA   1 
ATOM   2628 C C    . LYS   A 1 110 ? 25.310 -13.446 -4.158  1.00 12.54 ?  110 LYS   A C    1 
ATOM   2629 O O    . LYS   A 1 110 ? 25.513 -13.665 -2.958  1.00 13.18 ?  110 LYS   A O    1 
ATOM   2630 C CB   . LYS   A 1 110 ? 23.848 -15.010 -5.516  1.00 14.87 ?  110 LYS   A CB   1 
ATOM   2631 C CG   . LYS   A 1 110 ? 24.067 -16.233 -4.621  1.00 14.89 ?  110 LYS   A CG   1 
ATOM   2632 C CD   . LYS   A 1 110 ? 23.807 -17.551 -5.347  1.00 15.11 ?  110 LYS   A CD   1 
ATOM   2633 C CE   . LYS   A 1 110 ? 23.917 -18.754 -4.417  1.00 16.21 ?  110 LYS   A CE   1 
ATOM   2634 N NZ   . LYS   A 1 110 ? 22.755 -18.866 -3.503  1.00 16.48 ?  110 LYS   A NZ   1 
ATOM   2635 H H    . LYS   A 1 110 ? 23.444 -12.771 -6.463  1.00 16.04 ?  110 LYS   A H    1 
ATOM   2636 H HA   . LYS   A 1 110 ? 23.287 -13.716 -4.032  1.00 16.14 ?  110 LYS   A HA   1 
ATOM   2637 H HB2  . LYS   A 1 110 ? 22.969 -15.092 -5.917  1.00 17.84 ?  110 LYS   A HB2  1 
ATOM   2638 H HB3  . LYS   A 1 110 ? 24.529 -15.019 -6.204  1.00 17.84 ?  110 LYS   A HB3  1 
ATOM   2639 H HG2  . LYS   A 1 110 ? 24.987 -16.232 -4.309  1.00 17.87 ?  110 LYS   A HG2  1 
ATOM   2640 H HG3  . LYS   A 1 110 ? 23.463 -16.179 -3.863  1.00 17.87 ?  110 LYS   A HG3  1 
ATOM   2641 H HD2  . LYS   A 1 110 ? 22.915 -17.537 -5.717  1.00 18.13 ?  110 LYS   A HD2  1 
ATOM   2642 H HD3  . LYS   A 1 110 ? 24.464 -17.653 -6.056  1.00 18.13 ?  110 LYS   A HD3  1 
ATOM   2643 H HE2  . LYS   A 1 110 ? 23.969 -19.566 -4.950  1.00 19.45 ?  110 LYS   A HE2  1 
ATOM   2644 H HE3  . LYS   A 1 110 ? 24.724 -18.669 -3.875  1.00 19.45 ?  110 LYS   A HE3  1 
ATOM   2645 H HZ1  . LYS   A 1 110 ? 22.844 -19.576 -2.975  1.00 19.78 ?  110 LYS   A HZ1  1 
ATOM   2646 H HZ2  . LYS   A 1 110 ? 22.691 -18.136 -2.998  1.00 19.78 ?  110 LYS   A HZ2  1 
ATOM   2647 H HZ3  . LYS   A 1 110 ? 22.004 -18.953 -3.977  1.00 19.78 ?  110 LYS   A HZ3  1 
ATOM   2648 N N    . SER   A 1 111 ? 26.270 -13.000 -4.970  1.00 13.18 ?  111 SER   A N    1 
ATOM   2649 C CA   . SER   A 1 111 ? 27.597 -12.688 -4.444  1.00 12.83 ?  111 SER   A CA   1 
ATOM   2650 C C    . SER   A 1 111 ? 27.524 -11.647 -3.331  1.00 12.05 ?  111 SER   A C    1 
ATOM   2651 O O    . SER   A 1 111 ? 28.213 -11.758 -2.310  1.00 13.13 ?  111 SER   A O    1 
ATOM   2652 C CB   . SER   A 1 111 ? 28.495 -12.193 -5.577  1.00 14.32 ?  111 SER   A CB   1 
ATOM   2653 O OG   . SER   A 1 111 ? 28.583 -13.178 -6.601  1.00 16.19 ?  111 SER   A OG   1 
ATOM   2654 H H    . SER   A 1 111 ? 26.176 -12.885 -5.817  1.00 15.81 ?  111 SER   A H    1 
ATOM   2655 H HA   . SER   A 1 111 ? 27.992 -13.498 -4.083  1.00 15.40 ?  111 SER   A HA   1 
ATOM   2656 H HB2  . SER   A 1 111 ? 28.115 -11.385 -5.957  1.00 17.18 ?  111 SER   A HB2  1 
ATOM   2657 H HB3  . SER   A 1 111 ? 29.380 -12.015 -5.228  1.00 17.18 ?  111 SER   A HB3  1 
ATOM   2658 H HG   . SER   A 1 111 ? 29.089 -12.900 -7.223  1.00 19.43 ?  111 SER   A HG   1 
ATOM   2659 N N    . ALA   A 1 112 ? 26.676 -10.633 -3.507  1.00 12.42 ?  112 ALA   A N    1 
ATOM   2660 C CA   . ALA   A 1 112 ? 26.522 -9.602  -2.483  1.00 12.02 ?  112 ALA   A CA   1 
ATOM   2661 C C    . ALA   A 1 112 ? 26.029 -10.204 -1.170  1.00 11.73 ?  112 ALA   A C    1 
ATOM   2662 O O    . ALA   A 1 112 ? 26.564 -9.915  -0.096  1.00 12.65 ?  112 ALA   A O    1 
ATOM   2663 C CB   . ALA   A 1 112 ? 25.560 -8.518  -2.977  1.00 12.88 ?  112 ALA   A CB   1 
ATOM   2664 H H    . ALA   A 1 112 ? 26.186 -10.520 -4.206  1.00 14.91 ?  112 ALA   A H    1 
ATOM   2665 H HA   . ALA   A 1 112 ? 27.383 -9.184  -2.324  1.00 14.42 ?  112 ALA   A HA   1 
ATOM   2666 H HB1  . ALA   A 1 112 ? 25.475 -7.832  -2.289  1.00 15.45 ?  112 ALA   A HB1  1 
ATOM   2667 H HB2  . ALA   A 1 112 ? 25.910 -8.122  -3.789  1.00 15.45 ?  112 ALA   A HB2  1 
ATOM   2668 H HB3  . ALA   A 1 112 ? 24.691 -8.915  -3.149  1.00 15.45 ?  112 ALA   A HB3  1 
ATOM   2669 N N    . TYR   A 1 113 ? 24.986 -11.037 -1.233  1.00 12.28 ?  113 TYR   A N    1 
ATOM   2670 C CA   . TYR   A 1 113 ? 24.472 -11.643 -0.009  1.00 11.58 ?  113 TYR   A CA   1 
ATOM   2671 C C    . TYR   A 1 113 ? 25.466 -12.606 0.643   1.00 11.44 ?  113 TYR   A C    1 
ATOM   2672 O O    . TYR   A 1 113 ? 25.422 -12.791 1.864   1.00 12.16 ?  113 TYR   A O    1 
ATOM   2673 C CB   . TYR   A 1 113 ? 23.150 -12.362 -0.288  1.00 12.50 ?  113 TYR   A CB   1 
ATOM   2674 C CG   . TYR   A 1 113 ? 21.934 -11.462 -0.257  1.00 11.93 ?  113 TYR   A CG   1 
ATOM   2675 C CD1  . TYR   A 1 113 ? 21.556 -10.816 0.915   1.00 12.71 ?  113 TYR   A CD1  1 
ATOM   2676 C CD2  . TYR   A 1 113 ? 21.157 -11.271 -1.390  1.00 13.01 ?  113 TYR   A CD2  1 
ATOM   2677 C CE1  . TYR   A 1 113 ? 20.433 -10.021 0.961   1.00 13.89 ?  113 TYR   A CE1  1 
ATOM   2678 C CE2  . TYR   A 1 113 ? 20.008 -10.462 -1.351  1.00 13.68 ?  113 TYR   A CE2  1 
ATOM   2679 C CZ   . TYR   A 1 113 ? 19.664 -9.841  -0.172  1.00 13.48 ?  113 TYR   A CZ   1 
ATOM   2680 O OH   . TYR   A 1 113 ? 18.543 -9.029  -0.106  1.00 14.64 ?  113 TYR   A OH   1 
ATOM   2681 H H    . TYR   A 1 113 ? 24.581 -11.263 -1.955  1.00 14.74 ?  113 TYR   A H    1 
ATOM   2682 H HA   . TYR   A 1 113 ? 24.292 -10.942 0.630   1.00 13.90 ?  113 TYR   A HA   1 
ATOM   2683 H HB2  . TYR   A 1 113 ? 23.191 -12.765 -1.171  1.00 14.99 ?  113 TYR   A HB2  1 
ATOM   2684 H HB3  . TYR   A 1 113 ? 23.023 -13.057 0.379   1.00 14.99 ?  113 TYR   A HB3  1 
ATOM   2685 H HD1  . TYR   A 1 113 ? 22.067 -10.951 1.687   1.00 15.25 ?  113 TYR   A HD1  1 
ATOM   2686 H HD2  . TYR   A 1 113 ? 21.386 -11.701 -2.181  1.00 15.62 ?  113 TYR   A HD2  1 
ATOM   2687 H HE1  . TYR   A 1 113 ? 20.196 -9.602  1.755   1.00 16.67 ?  113 TYR   A HE1  1 
ATOM   2688 H HE2  . TYR   A 1 113 ? 19.493 -10.337 -2.116  1.00 16.41 ?  113 TYR   A HE2  1 
ATOM   2689 H HH   . TYR   A 1 113 ? 18.168 -9.005  -0.863  1.00 17.57 ?  113 TYR   A HH   1 
ATOM   2690 N N    . GLU   A 1 114 ? 26.372 -13.216 -0.135  1.00 11.82 ?  114 GLU   A N    1 
ATOM   2691 C CA   . GLU   A 1 114 ? 27.364 -14.109 0.464   1.00 12.73 ?  114 GLU   A CA   1 
ATOM   2692 C C    . GLU   A 1 114 ? 28.219 -13.400 1.516   1.00 11.98 ?  114 GLU   A C    1 
ATOM   2693 O O    . GLU   A 1 114 ? 28.693 -14.034 2.470   1.00 12.55 ?  114 GLU   A O    1 
ATOM   2694 C CB   . GLU   A 1 114 ? 28.235 -14.754 -0.624  1.00 12.47 ?  114 GLU   A CB   1 
ATOM   2695 C CG   . GLU   A 1 114 ? 27.494 -15.819 -1.417  1.00 13.48 ?  114 GLU   A CG   1 
ATOM   2696 C CD   . GLU   A 1 114 ? 28.224 -16.341 -2.658  1.00 13.89 ?  114 GLU   A CD   1 
ATOM   2697 O OE1  . GLU   A 1 114 ? 29.177 -15.711 -3.158  1.00 14.03 ?  114 GLU   A OE1  1 
ATOM   2698 O OE2  . GLU   A 1 114 ? 27.815 -17.419 -3.150  1.00 15.25 -1 114 GLU   A OE2  1 
ATOM   2699 H H    . GLU   A 1 114 ? 26.430 -13.121 -0.994  1.00 14.18 ?  114 GLU   A H    1 
ATOM   2700 H HA   . GLU   A 1 114 ? 26.891 -14.824 0.908   1.00 15.28 ?  114 GLU   A HA   1 
ATOM   2701 H HB2  . GLU   A 1 114 ? 28.526 -14.070 -1.249  1.00 14.96 ?  114 GLU   A HB2  1 
ATOM   2702 H HB3  . GLU   A 1 114 ? 29.001 -15.175 -0.210  1.00 14.96 ?  114 GLU   A HB3  1 
ATOM   2703 H HG2  . GLU   A 1 114 ? 27.340 -16.585 -0.844  1.00 16.17 ?  114 GLU   A HG2  1 
ATOM   2704 H HG3  . GLU   A 1 114 ? 26.640 -15.457 -1.707  1.00 16.17 ?  114 GLU   A HG3  1 
ATOM   2705 N N    . ASN   A 1 115 ? 28.412 -12.088 1.383   1.00 12.51 ?  115 ASN   A N    1 
ATOM   2706 C CA   . ASN   A 1 115 ? 29.173 -11.354 2.394   1.00 12.63 ?  115 ASN   A CA   1 
ATOM   2707 C C    . ASN   A 1 115 ? 28.541 -11.487 3.778   1.00 12.39 ?  115 ASN   A C    1 
ATOM   2708 O O    . ASN   A 1 115 ? 29.242 -11.404 4.792   1.00 13.39 ?  115 ASN   A O    1 
ATOM   2709 C CB   . ASN   A 1 115 ? 29.288 -9.877  2.004   1.00 12.59 ?  115 ASN   A CB   1 
ATOM   2710 C CG   . ASN   A 1 115 ? 30.083 -9.676  0.738   1.00 13.27 ?  115 ASN   A CG   1 
ATOM   2711 O OD1  . ASN   A 1 115 ? 31.299 -9.829  0.742   1.00 16.95 ?  115 ASN   A OD1  1 
ATOM   2712 N ND2  . ASN   A 1 115 ? 29.418 -9.343  -0.348  1.00 12.62 ?  115 ASN   A ND2  1 
ATOM   2713 H H    . ASN   A 1 115 ? 28.115 -11.607 0.739   1.00 15.01 ?  115 ASN   A H    1 
ATOM   2714 H HA   . ASN   A 1 115 ? 30.068 -11.725 2.441   1.00 15.16 ?  115 ASN   A HA   1 
ATOM   2715 H HB2  . ASN   A 1 115 ? 28.400 -9.519  1.874   1.00 15.11 ?  115 ASN   A HB2  1 
ATOM   2716 H HB3  . ASN   A 1 115 ? 29.743 -9.403  2.716   1.00 15.11 ?  115 ASN   A HB3  1 
ATOM   2717 H HD21 . ASN   A 1 115 ? 29.833 -9.221  -1.089  1.00 15.15 ?  115 ASN   A HD21 1 
ATOM   2718 H HD22 . ASN   A 1 115 ? 28.561 -9.244  -0.315  1.00 15.15 ?  115 ASN   A HD22 1 
ATOM   2719 N N    . PHE   A 1 116 ? 27.214 -11.661 3.847   1.00 12.34 ?  116 PHE   A N    1 
ATOM   2720 C CA   . PHE   A 1 116 ? 26.553 -11.745 5.150   1.00 12.59 ?  116 PHE   A CA   1 
ATOM   2721 C C    . PHE   A 1 116 ? 27.025 -12.972 5.929   1.00 12.56 ?  116 PHE   A C    1 
ATOM   2722 O O    . PHE   A 1 116 ? 26.962 -12.993 7.163   1.00 13.04 ?  116 PHE   A O    1 
ATOM   2723 C CB   . PHE   A 1 116 ? 25.024 -11.878 5.009   1.00 12.73 ?  116 PHE   A CB   1 
ATOM   2724 C CG   . PHE   A 1 116 ? 24.276 -10.642 4.516   1.00 12.35 ?  116 PHE   A CG   1 
ATOM   2725 C CD1  . PHE   A 1 116 ? 24.856 -9.643  3.755   1.00 12.59 ?  116 PHE   A CD1  1 
ATOM   2726 C CD2  . PHE   A 1 116 ? 22.922 -10.523 4.825   1.00 12.95 ?  116 PHE   A CD2  1 
ATOM   2727 C CE1  . PHE   A 1 116 ? 24.091 -8.566  3.312   1.00 12.78 ?  116 PHE   A CE1  1 
ATOM   2728 C CE2  . PHE   A 1 116 ? 22.160 -9.448  4.394   1.00 13.39 ?  116 PHE   A CE2  1 
ATOM   2729 C CZ   . PHE   A 1 116 ? 22.738 -8.472  3.633   1.00 12.95 ?  116 PHE   A CZ   1 
ATOM   2730 H H    . PHE   A 1 116 ? 26.686 -11.718 3.168   1.00 14.80 ?  116 PHE   A H    1 
ATOM   2731 H HA   . PHE   A 1 116 ? 26.748 -10.952 5.673   1.00 15.11 ?  116 PHE   A HA   1 
ATOM   2732 H HB2  . PHE   A 1 116 ? 24.841 -12.601 4.387   1.00 15.28 ?  116 PHE   A HB2  1 
ATOM   2733 H HB3  . PHE   A 1 116 ? 24.662 -12.111 5.882   1.00 15.28 ?  116 PHE   A HB3  1 
ATOM   2734 H HD1  . PHE   A 1 116 ? 25.757 -9.702  3.525   1.00 15.10 ?  116 PHE   A HD1  1 
ATOM   2735 H HD2  . PHE   A 1 116 ? 22.514 -11.198 5.335   1.00 15.54 ?  116 PHE   A HD2  1 
ATOM   2736 H HE1  . PHE   A 1 116 ? 24.499 -7.896  2.806   1.00 15.33 ?  116 PHE   A HE1  1 
ATOM   2737 H HE2  . PHE   A 1 116 ? 21.256 -9.401  4.623   1.00 16.06 ?  116 PHE   A HE2  1 
ATOM   2738 H HZ   . PHE   A 1 116 ? 22.242 -7.739  3.353   1.00 15.54 ?  116 PHE   A HZ   1 
ATOM   2739 N N    . ASN   A 1 117 ? 27.470 -14.014 5.228   1.00 12.34 ?  117 ASN   A N    1 
ATOM   2740 C CA   . ASN   A 1 117 ? 27.831 -15.255 5.901   1.00 13.14 ?  117 ASN   A CA   1 
ATOM   2741 C C    . ASN   A 1 117 ? 29.088 -15.131 6.743   1.00 13.59 ?  117 ASN   A C    1 
ATOM   2742 O O    . ASN   A 1 117 ? 29.383 -16.043 7.518   1.00 14.94 ?  117 ASN   A O    1 
ATOM   2743 C CB   . ASN   A 1 117 ? 27.967 -16.370 4.873   1.00 13.59 ?  117 ASN   A CB   1 
ATOM   2744 C CG   . ASN   A 1 117 ? 26.626 -16.786 4.336   1.00 13.78 ?  117 ASN   A CG   1 
ATOM   2745 O OD1  . ASN   A 1 117 ? 25.658 -16.815 5.085   1.00 14.53 ?  117 ASN   A OD1  1 
ATOM   2746 N ND2  . ASN   A 1 117 ? 26.547 -17.069 3.043   1.00 13.64 ?  117 ASN   A ND2  1 
ATOM   2747 H H    . ASN   A 1 117 ? 27.555 -14.033 4.367   1.00 14.80 ?  117 ASN   A H    1 
ATOM   2748 H HA   . ASN   A 1 117 ? 27.103 -15.497 6.495   1.00 15.77 ?  117 ASN   A HA   1 
ATOM   2749 H HB2  . ASN   A 1 117 ? 28.514 -16.053 4.130   1.00 16.30 ?  117 ASN   A HB2  1 
ATOM   2750 H HB3  . ASN   A 1 117 ? 28.388 -17.135 5.290   1.00 16.30 ?  117 ASN   A HB3  1 
ATOM   2751 H HD21 . ASN   A 1 117 ? 25.803 -17.310 2.702   1.00 16.37 ?  117 ASN   A HD21 1 
ATOM   2752 H HD22 . ASN   A 1 117 ? 27.257 -17.025 2.551   1.00 16.37 ?  117 ASN   A HD22 1 
ATOM   2753 N N    . GLN   A 1 118 ? 29.831 -14.033 6.624   1.00 13.83 ?  118 GLN   A N    1 
ATOM   2754 C CA   . GLN   A 1 118 ? 30.998 -13.801 7.465   1.00 14.07 ?  118 GLN   A CA   1 
ATOM   2755 C C    . GLN   A 1 118 ? 30.644 -13.229 8.832   1.00 14.41 ?  118 GLN   A C    1 
ATOM   2756 O O    . GLN   A 1 118 ? 31.561 -12.932 9.609   1.00 15.66 ?  118 GLN   A O    1 
ATOM   2757 C CB   . GLN   A 1 118 ? 32.005 -12.902 6.742   1.00 14.70 ?  118 GLN   A CB   1 
ATOM   2758 C CG   . GLN   A 1 118 ? 32.479 -13.476 5.416   1.00 14.36 ?  118 GLN   A CG   1 
ATOM   2759 C CD   . GLN   A 1 118 ? 33.312 -14.729 5.590   1.00 14.93 ?  118 GLN   A CD   1 
ATOM   2760 O OE1  . GLN   A 1 118 ? 34.162 -14.802 6.483   1.00 15.72 ?  118 GLN   A OE1  1 
ATOM   2761 N NE2  . GLN   A 1 118 ? 33.073 -15.727 4.735   1.00 14.69 ?  118 GLN   A NE2  1 
ATOM   2762 H H    . GLN   A 1 118 ? 29.669 -13.389 6.064   1.00 16.59 ?  118 GLN   A H    1 
ATOM   2763 H HA   . GLN   A 1 118 ? 31.423 -14.658 7.616   1.00 16.88 ?  118 GLN   A HA   1 
ATOM   2764 H HB2  . GLN   A 1 118 ? 31.590 -12.044 6.571   1.00 17.65 ?  118 GLN   A HB2  1 
ATOM   2765 H HB3  . GLN   A 1 118 ? 32.780 -12.787 7.316   1.00 17.65 ?  118 GLN   A HB3  1 
ATOM   2766 H HG2  . GLN   A 1 118 ? 31.709 -13.696 4.870   1.00 17.23 ?  118 GLN   A HG2  1 
ATOM   2767 H HG3  . GLN   A 1 118 ? 33.027 -12.813 4.967   1.00 17.23 ?  118 GLN   A HG3  1 
ATOM   2768 H HE21 . GLN   A 1 118 ? 32.468 -15.636 4.127   1.00 17.63 ?  118 GLN   A HE21 1 
ATOM   2769 H HE22 . GLN   A 1 118 ? 33.511 -16.464 4.795   1.00 17.63 ?  118 GLN   A HE22 1 
ATOM   2770 N N    . HIS   A 1 119 ? 29.352 -13.057 9.133   1.00 13.75 ?  119 HIS   A N    1 
ATOM   2771 C CA   . HIS   A 1 119 ? 28.889 -12.452 10.381  1.00 14.22 ?  119 HIS   A CA   1 
ATOM   2772 C C    . HIS   A 1 119 ? 27.742 -13.270 10.953  1.00 14.88 ?  119 HIS   A C    1 
ATOM   2773 O O    . HIS   A 1 119 ? 26.807 -13.621 10.230  1.00 14.95 ?  119 HIS   A O    1 
ATOM   2774 C CB   . HIS   A 1 119 ? 28.441 -11.014 10.116  1.00 14.46 ?  119 HIS   A CB   1 
ATOM   2775 C CG   . HIS   A 1 119 ? 29.525 -10.200 9.504   1.00 16.08 ?  119 HIS   A CG   1 
ATOM   2776 N ND1  . HIS   A 1 119 ? 30.493 -9.581  10.260  1.00 18.42 ?  119 HIS   A ND1  1 
ATOM   2777 C CD2  . HIS   A 1 119 ? 29.869 -10.011 8.210   1.00 17.26 ?  119 HIS   A CD2  1 
ATOM   2778 C CE1  . HIS   A 1 119 ? 31.365 -9.001  9.455   1.00 18.44 ?  119 HIS   A CE1  1 
ATOM   2779 N NE2  . HIS   A 1 119 ? 31.015 -9.256  8.206   1.00 18.68 ?  119 HIS   A NE2  1 
ATOM   2780 H H    . HIS   A 1 119 ? 28.698 -13.303 8.616   1.00 16.50 ?  119 HIS   A H    1 
ATOM   2781 H HA   . HIS   A 1 119 ? 29.613 -12.439 11.018  1.00 17.07 ?  119 HIS   A HA   1 
ATOM   2782 H HB2  . HIS   A 1 119 ? 27.682 -11.022 9.505   1.00 17.35 ?  119 HIS   A HB2  1 
ATOM   2783 H HB3  . HIS   A 1 119 ? 28.185 -10.602 10.955  1.00 17.35 ?  119 HIS   A HB3  1 
ATOM   2784 H HD2  . HIS   A 1 119 ? 29.417 -10.331 7.460   1.00 20.71 ?  119 HIS   A HD2  1 
ATOM   2785 H HE1  . HIS   A 1 119 ? 32.097 -8.491  9.721   1.00 22.13 ?  119 HIS   A HE1  1 
ATOM   2786 H HE2  . HIS   A 1 119 ? 31.424 -8.966  7.504   1.00 22.42 ?  119 HIS   A HE2  1 
ATOM   2787 N N    A GLU   A 1 120 ? 27.834 -13.606 12.242  0.52 15.80 ?  120 GLU   A N    1 
ATOM   2788 N N    B GLU   A 1 120 ? 27.807 -13.532 12.262  0.48 16.07 ?  120 GLU   A N    1 
ATOM   2789 C CA   A GLU   A 1 120 ? 26.877 -14.548 12.821  0.52 17.76 ?  120 GLU   A CA   1 
ATOM   2790 C CA   B GLU   A 1 120 ? 26.855 -14.445 12.890  0.48 18.26 ?  120 GLU   A CA   1 
ATOM   2791 C C    A GLU   A 1 120 ? 25.463 -13.979 12.886  0.52 16.14 ?  120 GLU   A C    1 
ATOM   2792 C C    B GLU   A 1 120 ? 25.444 -13.866 12.935  0.48 17.46 ?  120 GLU   A C    1 
ATOM   2793 O O    A GLU   A 1 120 ? 24.491 -14.742 12.788  0.52 15.62 ?  120 GLU   A O    1 
ATOM   2794 O O    B GLU   A 1 120 ? 24.464 -14.609 12.786  0.48 17.90 ?  120 GLU   A O    1 
ATOM   2795 C CB   A GLU   A 1 120 ? 27.338 -14.987 14.211  0.52 21.75 ?  120 GLU   A CB   1 
ATOM   2796 C CB   B GLU   A 1 120 ? 27.330 -14.814 14.296  0.48 21.70 ?  120 GLU   A CB   1 
ATOM   2797 C CG   A GLU   A 1 120 ? 28.532 -15.931 14.194  0.52 27.06 ?  120 GLU   A CG   1 
ATOM   2798 C CG   B GLU   A 1 120 ? 28.479 -15.811 14.322  0.48 26.73 ?  120 GLU   A CG   1 
ATOM   2799 C CD   A GLU   A 1 120 ? 28.754 -16.634 15.517  0.52 31.87 ?  120 GLU   A CD   1 
ATOM   2800 C CD   B GLU   A 1 120 ? 28.492 -16.635 15.594  0.48 31.32 ?  120 GLU   A CD   1 
ATOM   2801 O OE1  A GLU   A 1 120 ? 28.401 -16.053 16.566  0.52 33.36 ?  120 GLU   A OE1  1 
ATOM   2802 O OE1  B GLU   A 1 120 ? 28.191 -16.073 16.670  0.48 32.53 ?  120 GLU   A OE1  1 
ATOM   2803 O OE2  A GLU   A 1 120 ? 29.287 -17.765 15.505  0.52 33.63 -1 120 GLU   A OE2  1 
ATOM   2804 O OE2  B GLU   A 1 120 ? 28.782 -17.847 15.514  0.48 33.14 -1 120 GLU   A OE2  1 
ATOM   2805 H H    A GLU   A 1 120 ? 28.444 -13.324 12.784  0.52 18.96 ?  120 GLU   A H    1 
ATOM   2806 H H    B GLU   A 1 120 ? 28.399 -13.205 12.796  0.48 19.29 ?  120 GLU   A H    1 
ATOM   2807 H HA   A GLU   A 1 120 ? 26.856 -15.342 12.263  0.52 21.31 ?  120 GLU   A HA   1 
ATOM   2808 H HA   B GLU   A 1 120 ? 26.823 -15.263 12.374  0.48 21.91 ?  120 GLU   A HA   1 
ATOM   2809 H HB2  A GLU   A 1 120 ? 27.590 -14.204 14.723  0.52 26.10 ?  120 GLU   A HB2  1 
ATOM   2810 H HB2  B GLU   A 1 120 ? 27.630 -14.014 14.754  0.48 26.05 ?  120 GLU   A HB2  1 
ATOM   2811 H HB3  A GLU   A 1 120 ? 26.604 -15.446 14.652  0.52 26.10 ?  120 GLU   A HB3  1 
ATOM   2812 H HB3  B GLU   A 1 120 ? 26.591 -15.213 14.785  0.48 26.05 ?  120 GLU   A HB3  1 
ATOM   2813 H HG2  A GLU   A 1 120 ? 28.396 -16.600 13.506  0.52 32.47 ?  120 GLU   A HG2  1 
ATOM   2814 H HG2  B GLU   A 1 120 ? 28.392 -16.421 13.575  0.48 32.07 ?  120 GLU   A HG2  1 
ATOM   2815 H HG3  A GLU   A 1 120 ? 29.335 -15.425 14.018  0.52 32.47 ?  120 GLU   A HG3  1 
ATOM   2816 H HG3  B GLU   A 1 120 ? 29.321 -15.330 14.262  0.48 32.07 ?  120 GLU   A HG3  1 
ATOM   2817 N N    A VAL   A 1 121 ? 25.329 -12.668 13.090  0.52 15.31 ?  121 VAL   A N    1 
ATOM   2818 N N    B VAL   A 1 121 ? 25.313 -12.560 13.165  0.48 16.43 ?  121 VAL   A N    1 
ATOM   2819 C CA   A VAL   A 1 121 ? 24.038 -11.991 13.177  0.52 15.42 ?  121 VAL   A CA   1 
ATOM   2820 C CA   B VAL   A 1 121 ? 24.010 -11.909 13.289  0.48 16.28 ?  121 VAL   A CA   1 
ATOM   2821 C C    A VAL   A 1 121 ? 24.172 -10.632 12.499  0.52 14.75 ?  121 VAL   A C    1 
ATOM   2822 C C    B VAL   A 1 121 ? 24.093 -10.534 12.644  0.48 14.54 ?  121 VAL   A C    1 
ATOM   2823 O O    A VAL   A 1 121 ? 25.197 -9.958  12.643  0.52 15.66 ?  121 VAL   A O    1 
ATOM   2824 O O    B VAL   A 1 121 ? 25.010 -9.761  12.942  0.48 13.17 ?  121 VAL   A O    1 
ATOM   2825 C CB   A VAL   A 1 121 ? 23.596 -11.800 14.648  0.52 17.92 ?  121 VAL   A CB   1 
ATOM   2826 C CB   B VAL   A 1 121 ? 23.561 -11.771 14.760  0.48 18.83 ?  121 VAL   A CB   1 
ATOM   2827 C CG1  A VAL   A 1 121 ? 22.194 -11.213 14.719  0.52 18.77 ?  121 VAL   A CG1  1 
ATOM   2828 C CG1  B VAL   A 1 121 ? 22.209 -11.080 14.836  0.48 19.53 ?  121 VAL   A CG1  1 
ATOM   2829 C CG2  A VAL   A 1 121 ? 23.659 -13.103 15.429  0.52 20.15 ?  121 VAL   A CG2  1 
ATOM   2830 C CG2  B VAL   A 1 121 ? 23.494 -13.123 15.450  0.48 20.87 ?  121 VAL   A CG2  1 
ATOM   2831 H H    A VAL   A 1 121 ? 25.998 -12.139 13.198  0.52 18.37 ?  121 VAL   A H    1 
ATOM   2832 H H    B VAL   A 1 121 ? 25.980 -12.018 13.251  0.48 19.71 ?  121 VAL   A H    1 
ATOM   2833 H HA   A VAL   A 1 121 ? 23.366 -12.522 12.720  0.52 18.50 ?  121 VAL   A HA   1 
ATOM   2834 H HA   B VAL   A 1 121 ? 23.349 -12.433 12.818  0.48 19.53 ?  121 VAL   A HA   1 
ATOM   2835 H HB   A VAL   A 1 121 ? 24.202 -11.174 15.076  0.52 21.50 ?  121 VAL   A HB   1 
ATOM   2836 H HB   B VAL   A 1 121 ? 24.205 -11.224 15.239  0.48 22.60 ?  121 VAL   A HB   1 
ATOM   2837 H HG11 A VAL   A 1 121 ? 21.906 -11.192 15.646  0.52 22.53 ?  121 VAL   A HG11 1 
ATOM   2838 H HG11 B VAL   A 1 121 ? 21.846 -11.194 15.729  0.48 23.44 ?  121 VAL   A HG11 1 
ATOM   2839 H HG12 A VAL   A 1 121 ? 22.209 -10.312 14.360  0.52 22.53 ?  121 VAL   A HG12 1 
ATOM   2840 H HG12 B VAL   A 1 121 ? 22.321 -10.136 14.645  0.48 23.44 ?  121 VAL   A HG12 1 
ATOM   2841 H HG13 A VAL   A 1 121 ? 21.593 -11.768 14.200  0.52 22.53 ?  121 VAL   A HG13 1 
ATOM   2842 H HG13 B VAL   A 1 121 ? 21.612 -11.483 14.185  0.48 23.44 ?  121 VAL   A HG13 1 
ATOM   2843 H HG21 A VAL   A 1 121 ? 23.299 -12.953 16.322  0.52 24.18 ?  121 VAL   A HG21 1 
ATOM   2844 H HG21 B VAL   A 1 121 ? 23.156 -12.999 16.354  0.48 25.05 ?  121 VAL   A HG21 1 
ATOM   2845 H HG22 A VAL   A 1 121 ? 23.125 -13.771 14.971  0.52 24.18 ?  121 VAL   A HG22 1 
ATOM   2846 H HG22 B VAL   A 1 121 ? 22.895 -13.701 14.952  0.48 25.05 ?  121 VAL   A HG22 1 
ATOM   2847 H HG23 A VAL   A 1 121 ? 24.579 -13.396 15.490  0.52 24.18 ?  121 VAL   A HG23 1 
ATOM   2848 H HG23 B VAL   A 1 121 ? 24.381 -13.509 15.481  0.48 25.05 ?  121 VAL   A HG23 1 
ATOM   2849 N N    . LEU   A 1 122 ? 23.127 -10.215 11.781  1.00 13.45 ?  122 LEU   A N    1 
ATOM   2850 C CA   . LEU   A 1 122 ? 23.124 -8.919  11.104  1.00 13.28 ?  122 LEU   A CA   1 
ATOM   2851 C C    . LEU   A 1 122 ? 21.720 -8.332  11.050  1.00 13.53 ?  122 LEU   A C    1 
ATOM   2852 O O    . LEU   A 1 122 ? 20.742 -9.059  10.890  1.00 14.27 ?  122 LEU   A O    1 
ATOM   2853 C CB   . LEU   A 1 122 ? 23.582 -9.020  9.644   1.00 15.39 ?  122 LEU   A CB   1 
ATOM   2854 C CG   . LEU   A 1 122 ? 24.798 -9.857  9.281   1.00 15.41 ?  122 LEU   A CG   1 
ATOM   2855 C CD1  . LEU   A 1 122 ? 24.397 -11.324 9.088   1.00 15.75 ?  122 LEU   A CD1  1 
ATOM   2856 C CD2  . LEU   A 1 122 ? 25.469 -9.304  8.025   1.00 14.63 ?  122 LEU   A CD2  1 
ATOM   2857 H H    A LEU   A 1 122 ? 22.399 -10.664 11.674  0.52 16.13 ?  122 LEU   A H    1 
ATOM   2858 H H    B LEU   A 1 122 ? 22.470 -10.731 11.567  0.48 16.13 ?  122 LEU   A H    1 
ATOM   2859 H HA   . LEU   A 1 122 ? 23.711 -8.300  11.571  1.00 15.94 ?  122 LEU   A HA   1 
ATOM   2860 H HB2  . LEU   A 1 122 ? 22.854 -9.382  9.128   1.00 18.47 ?  122 LEU   A HB2  1 
ATOM   2861 H HB3  . LEU   A 1 122 ? 23.779 -8.124  9.332   1.00 18.47 ?  122 LEU   A HB3  1 
ATOM   2862 H HG   . LEU   A 1 122 ? 25.458 -9.818  9.995   1.00 18.49 ?  122 LEU   A HG   1 
ATOM   2863 H HD11 . LEU   A 1 122 ? 25.172 -11.839 8.803   1.00 18.90 ?  122 LEU   A HD11 1 
ATOM   2864 H HD12 . LEU   A 1 122 ? 24.065 -11.674 9.929   1.00 18.90 ?  122 LEU   A HD12 1 
ATOM   2865 H HD13 . LEU   A 1 122 ? 23.704 -11.376 8.411   1.00 18.90 ?  122 LEU   A HD13 1 
ATOM   2866 H HD21 . LEU   A 1 122 ? 26.227 -9.868  7.780   1.00 17.56 ?  122 LEU   A HD21 1 
ATOM   2867 H HD22 . LEU   A 1 122 ? 24.828 -9.292  7.297   1.00 17.56 ?  122 LEU   A HD22 1 
ATOM   2868 H HD23 . LEU   A 1 122 ? 25.785 -8.400  8.198   1.00 17.56 ?  122 LEU   A HD23 1 
ATOM   2869 N N    . LEU   A 1 123 ? 21.641 -6.999  11.151  1.00 13.10 ?  123 LEU   A N    1 
ATOM   2870 C CA   . LEU   A 1 123 ? 20.472 -6.210  10.754  1.00 12.55 ?  123 LEU   A CA   1 
ATOM   2871 C C    . LEU   A 1 123 ? 20.739 -5.681  9.351   1.00 12.22 ?  123 LEU   A C    1 
ATOM   2872 O O    . LEU   A 1 123 ? 21.797 -5.088  9.113   1.00 13.46 ?  123 LEU   A O    1 
ATOM   2873 C CB   . LEU   A 1 123 ? 20.317 -5.037  11.721  1.00 13.67 ?  123 LEU   A CB   1 
ATOM   2874 C CG   . LEU   A 1 123 ? 19.296 -3.960  11.364  1.00 14.42 ?  123 LEU   A CG   1 
ATOM   2875 C CD1  . LEU   A 1 123 ? 17.869 -4.519  11.343  1.00 15.23 ?  123 LEU   A CD1  1 
ATOM   2876 C CD2  . LEU   A 1 123 ? 19.417 -2.784  12.342  1.00 14.98 ?  123 LEU   A CD2  1 
ATOM   2877 H H    . LEU   A 1 123 ? 22.280 -6.510  11.470  1.00 15.72 ?  123 LEU   A H    1 
ATOM   2878 H HA   . LEU   A 1 123 ? 19.671 -6.756  10.764  1.00 15.05 ?  123 LEU   A HA   1 
ATOM   2879 H HB2  . LEU   A 1 123 ? 20.046 -5.389  12.587  1.00 16.40 ?  123 LEU   A HB2  1 
ATOM   2880 H HB3  . LEU   A 1 123 ? 21.168 -4.595  11.809  1.00 16.40 ?  123 LEU   A HB3  1 
ATOM   2881 H HG   . LEU   A 1 123 ? 19.490 -3.610  10.479  1.00 17.30 ?  123 LEU   A HG   1 
ATOM   2882 H HD11 . LEU   A 1 123 ? 17.246 -3.806  11.127  1.00 18.27 ?  123 LEU   A HD11 1 
ATOM   2883 H HD12 . LEU   A 1 123 ? 17.816 -5.218  10.674  1.00 18.27 ?  123 LEU   A HD12 1 
ATOM   2884 H HD13 . LEU   A 1 123 ? 17.660 -4.883  12.219  1.00 18.27 ?  123 LEU   A HD13 1 
ATOM   2885 H HD21 . LEU   A 1 123 ? 18.770 -2.104  12.111  1.00 17.97 ?  123 LEU   A HD21 1 
ATOM   2886 H HD22 . LEU   A 1 123 ? 19.251 -3.109  13.244  1.00 17.97 ?  123 LEU   A HD22 1 
ATOM   2887 H HD23 . LEU   A 1 123 ? 20.317 -2.421  12.287  1.00 17.97 ?  123 LEU   A HD23 1 
ATOM   2888 N N    A ALA   A 1 124 ? 19.798 -5.876  8.428   0.52 11.84 ?  124 ALA   A N    1 
ATOM   2889 N N    B ALA   A 1 124 ? 19.800 -5.889  8.429   0.48 11.78 ?  124 ALA   A N    1 
ATOM   2890 C CA   A ALA   A 1 124 ? 20.104 -5.624  7.028   0.52 11.63 ?  124 ALA   A CA   1 
ATOM   2891 C CA   B ALA   A 1 124 ? 20.079 -5.620  7.026   0.48 11.40 ?  124 ALA   A CA   1 
ATOM   2892 C C    A ALA   A 1 124 ? 18.867 -5.178  6.263   0.52 11.94 ?  124 ALA   A C    1 
ATOM   2893 C C    B ALA   A 1 124 ? 18.844 -5.113  6.293   0.48 11.94 ?  124 ALA   A C    1 
ATOM   2894 O O    A ALA   A 1 124 ? 17.734 -5.527  6.628   0.52 12.55 ?  124 ALA   A O    1 
ATOM   2895 O O    B ALA   A 1 124 ? 17.710 -5.427  6.682   0.48 12.69 ?  124 ALA   A O    1 
ATOM   2896 C CB   A ALA   A 1 124 ? 20.691 -6.863  6.347   0.52 12.22 ?  124 ALA   A CB   1 
ATOM   2897 C CB   B ALA   A 1 124 ? 20.618 -6.879  6.330   0.48 11.75 ?  124 ALA   A CB   1 
ATOM   2898 H H    A ALA   A 1 124 ? 18.993 -6.145  8.588   0.52 14.21 ?  124 ALA   A H    1 
ATOM   2899 H H    B ALA   A 1 124 ? 19.007 -6.184  8.589   0.48 14.14 ?  124 ALA   A H    1 
ATOM   2900 H HA   A ALA   A 1 124 ? 20.763 -4.917  6.989   0.52 13.96 ?  124 ALA   A HA   1 
ATOM   2901 H HA   B ALA   A 1 124 ? 20.768 -4.941  6.978   0.48 13.68 ?  124 ALA   A HA   1 
ATOM   2902 H HB1  A ALA   A 1 124 ? 20.881 -6.651  5.419   0.52 14.66 ?  124 ALA   A HB1  1 
ATOM   2903 H HB1  B ALA   A 1 124 ? 20.806 -6.679  5.402   0.48 14.10 ?  124 ALA   A HB1  1 
ATOM   2904 H HB2  A ALA   A 1 124 ? 21.510 -7.113  6.803   0.52 14.66 ?  124 ALA   A HB2  1 
ATOM   2905 H HB2  B ALA   A 1 124 ? 21.442 -7.164  6.774   0.48 14.10 ?  124 ALA   A HB2  1 
ATOM   2906 H HB3  A ALA   A 1 124 ? 20.049 -7.586  6.398   0.52 14.66 ?  124 ALA   A HB3  1 
ATOM   2907 H HB3  B ALA   A 1 124 ? 19.959 -7.588  6.392   0.48 14.10 ?  124 ALA   A HB3  1 
ATOM   2908 N N    A PRO   A 1 125 ? 19.060 -4.454  5.165   0.52 11.54 ?  125 PRO   A N    1 
ATOM   2909 N N    B PRO   A 1 125 ? 19.036 -4.350  5.219   0.48 11.95 ?  125 PRO   A N    1 
ATOM   2910 C CA   A PRO   A 1 125 ? 18.001 -4.219  4.186   0.52 11.72 ?  125 PRO   A CA   1 
ATOM   2911 C CA   B PRO   A 1 125 ? 17.940 -4.006  4.314   0.48 12.55 ?  125 PRO   A CA   1 
ATOM   2912 C C    A PRO   A 1 125 ? 18.050 -5.271  3.082   0.52 12.13 ?  125 PRO   A C    1 
ATOM   2913 C C    B PRO   A 1 125 ? 17.899 -5.042  3.193   0.48 13.10 ?  125 PRO   A C    1 
ATOM   2914 O O    A PRO   A 1 125 ? 19.003 -6.040  2.960   0.52 12.32 ?  125 PRO   A O    1 
ATOM   2915 O O    B PRO   A 1 125 ? 18.763 -5.914  3.095   0.48 12.80 ?  125 PRO   A O    1 
ATOM   2916 C CB   A PRO   A 1 125 ? 18.429 -2.869  3.602   0.52 12.04 ?  125 PRO   A CB   1 
ATOM   2917 C CB   B PRO   A 1 125 ? 18.414 -2.655  3.767   0.48 12.76 ?  125 PRO   A CB   1 
ATOM   2918 C CG   A PRO   A 1 125 ? 19.926 -3.010  3.526   0.52 12.43 ?  125 PRO   A CG   1 
ATOM   2919 C CG   B PRO   A 1 125 ? 19.902 -2.884  3.590   0.48 13.14 ?  125 PRO   A CG   1 
ATOM   2920 C CD   A PRO   A 1 125 ? 20.312 -3.777  4.775   0.52 11.84 ?  125 PRO   A CD   1 
ATOM   2921 C CD   B PRO   A 1 125 ? 20.319 -3.797  4.737   0.48 12.32 ?  125 PRO   A CD   1 
ATOM   2922 H HA   A PRO   A 1 125 ? 17.121 -4.177  4.594   0.52 14.06 ?  125 PRO   A HA   1 
ATOM   2923 H HA   B PRO   A 1 125 ? 17.097 -3.922  4.791   0.48 15.06 ?  125 PRO   A HA   1 
ATOM   2924 H HB2  A PRO   A 1 125 ? 18.037 -2.747  2.723   0.52 14.45 ?  125 PRO   A HB2  1 
ATOM   2925 H HB2  B PRO   A 1 125 ? 17.972 -2.469  2.926   0.48 15.31 ?  125 PRO   A HB2  1 
ATOM   2926 H HB3  A PRO   A 1 125 ? 18.171 -2.153  4.204   0.52 14.45 ?  125 PRO   A HB3  1 
ATOM   2927 H HB3  B PRO   A 1 125 ? 18.236 -1.951  4.419   0.48 15.31 ?  125 PRO   A HB3  1 
ATOM   2928 H HG2  A PRO   A 1 125 ? 20.166 -3.507  2.727   0.52 14.92 ?  125 PRO   A HG2  1 
ATOM   2929 H HG2  B PRO   A 1 125 ? 20.063 -3.314  2.734   0.48 15.77 ?  125 PRO   A HG2  1 
ATOM   2930 H HG3  A PRO   A 1 125 ? 20.334 -2.131  3.518   0.52 14.92 ?  125 PRO   A HG3  1 
ATOM   2931 H HG3  B PRO   A 1 125 ? 20.371 -2.036  3.636   0.48 15.77 ?  125 PRO   A HG3  1 
ATOM   2932 H HD2  A PRO   A 1 125 ? 21.008 -4.422  4.575   0.52 14.21 ?  125 PRO   A HD2  1 
ATOM   2933 H HD2  B PRO   A 1 125 ? 20.903 -4.502  4.410   0.48 14.78 ?  125 PRO   A HD2  1 
ATOM   2934 H HD3  A PRO   A 1 125 ? 20.588 -3.163  5.475   0.52 14.21 ?  125 PRO   A HD3  1 
ATOM   2935 H HD3  B PRO   A 1 125 ? 20.752 -3.278  5.435   0.48 14.78 ?  125 PRO   A HD3  1 
ATOM   2936 N N    A LEU   A 1 126 ? 17.001 -5.275  2.261   0.52 11.65 ?  126 LEU   A N    1 
ATOM   2937 N N    B LEU   A 1 126 ? 16.877 -4.942  2.338   0.48 14.29 ?  126 LEU   A N    1 
ATOM   2938 C CA   A LEU   A 1 126 ? 16.996 -6.065  1.035   0.52 12.11 ?  126 LEU   A CA   1 
ATOM   2939 C CA   B LEU   A 1 126 ? 16.842 -5.782  1.145   0.48 15.18 ?  126 LEU   A CA   1 
ATOM   2940 C C    A LEU   A 1 126 ? 17.922 -5.429  0.010   0.52 13.00 ?  126 LEU   A C    1 
ATOM   2941 C C    B LEU   A 1 126 ? 17.777 -5.183  0.099   0.48 15.08 ?  126 LEU   A C    1 
ATOM   2942 O O    A LEU   A 1 126 ? 17.647 -4.337  -0.499  0.52 14.18 ?  126 LEU   A O    1 
ATOM   2943 O O    B LEU   A 1 126 ? 17.667 -3.998  -0.230  0.48 16.57 ?  126 LEU   A O    1 
ATOM   2944 C CB   A LEU   A 1 126 ? 15.585 -6.146  0.472   0.52 12.80 ?  126 LEU   A CB   1 
ATOM   2945 C CB   B LEU   A 1 126 ? 15.415 -5.844  0.596   0.48 18.03 ?  126 LEU   A CB   1 
ATOM   2946 C CG   A LEU   A 1 126 ? 14.625 -7.069  1.203   0.52 12.66 ?  126 LEU   A CG   1 
ATOM   2947 C CG   B LEU   A 1 126 ? 14.956 -7.022  -0.266  0.48 19.77 ?  126 LEU   A CG   1 
ATOM   2948 C CD1  A LEU   A 1 126 ? 13.225 -6.921  0.628   0.52 13.07 ?  126 LEU   A CD1  1 
ATOM   2949 C CD1  B LEU   A 1 126 ? 15.144 -8.346  0.457   0.48 20.07 ?  126 LEU   A CD1  1 
ATOM   2950 C CD2  A LEU   A 1 126 ? 15.110 -8.518  1.104   0.52 12.87 ?  126 LEU   A CD2  1 
ATOM   2951 C CD2  B LEU   A 1 126 ? 13.487 -6.826  -0.633  0.48 20.31 ?  126 LEU   A CD2  1 
ATOM   2952 H H    A LEU   A 1 126 ? 16.287 -4.821  2.387   0.52 13.98 ?  126 LEU   A H    1 
ATOM   2953 H H    B LEU   A 1 126 ? 16.198 -4.406  2.409   0.48 17.15 ?  126 LEU   A H    1 
ATOM   2954 H HA   A LEU   A 1 126 ? 17.317 -6.962  1.218   0.52 14.53 ?  126 LEU   A HA   1 
ATOM   2955 H HA   B LEU   A 1 126 ? 17.142 -6.681  1.364   0.48 18.22 ?  126 LEU   A HA   1 
ATOM   2956 H HB2  A LEU   A 1 126 ? 15.200 -5.256  0.494   0.52 15.36 ?  126 LEU   A HB2  1 
ATOM   2957 H HB2  B LEU   A 1 126 ? 14.815 -5.817  1.351   0.48 21.64 ?  126 LEU   A HB2  1 
ATOM   2958 H HB3  A LEU   A 1 126 ? 15.639 -6.452  -0.446  0.52 15.36 ?  126 LEU   A HB3  1 
ATOM   2959 H HB3  B LEU   A 1 126 ? 15.281 -5.049  0.058   0.48 21.64 ?  126 LEU   A HB3  1 
ATOM   2960 H HG   A LEU   A 1 126 ? 14.595 -6.825  2.141   0.52 15.19 ?  126 LEU   A HG   1 
ATOM   2961 H HG   B LEU   A 1 126 ? 15.469 -7.045  -1.094  0.48 23.72 ?  126 LEU   A HG   1 
ATOM   2962 H HD11 A LEU   A 1 126 ? 12.624 -7.518  1.099   0.52 15.69 ?  126 LEU   A HD11 1 
ATOM   2963 H HD11 B LEU   A 1 126 ? 14.723 -9.051  -0.059  0.48 24.08 ?  126 LEU   A HD11 1 
ATOM   2964 H HD12 A LEU   A 1 126 ? 12.936 -6.003  0.736   0.52 15.69 ?  126 LEU   A HD12 1 
ATOM   2965 H HD12 B LEU   A 1 126 ? 16.092 -8.522  0.548   0.48 24.08 ?  126 LEU   A HD12 1 
ATOM   2966 H HD13 A LEU   A 1 126 ? 13.247 -7.152  -0.316  0.52 15.69 ?  126 LEU   A HD13 1 
ATOM   2967 H HD13 B LEU   A 1 126 ? 14.730 -8.285  1.332   0.48 24.08 ?  126 LEU   A HD13 1 
ATOM   2968 H HD21 A LEU   A 1 126 ? 14.403 -9.109  1.401   0.52 15.44 ?  126 LEU   A HD21 1 
ATOM   2969 H HD21 B LEU   A 1 126 ? 13.195 -7.560  -1.197  0.48 24.38 ?  126 LEU   A HD21 1 
ATOM   2970 H HD22 A LEU   A 1 126 ? 15.340 -8.712  0.182   0.52 15.44 ?  126 LEU   A HD22 1 
ATOM   2971 H HD22 B LEU   A 1 126 ? 12.958 -6.809  0.183   0.48 24.38 ?  126 LEU   A HD22 1 
ATOM   2972 H HD23 A LEU   A 1 126 ? 15.893 -8.629  1.669   0.52 15.44 ?  126 LEU   A HD23 1 
ATOM   2973 H HD23 B LEU   A 1 126 ? 13.385 -5.985  -1.107  0.48 24.38 ?  126 LEU   A HD23 1 
ATOM   2974 N N    A LEU   A 1 127 ? 19.001 -6.129  -0.321  0.52 12.74 ?  127 LEU   A N    1 
ATOM   2975 N N    B LEU   A 1 127 ? 18.707 -5.987  -0.415  0.48 14.05 ?  127 LEU   A N    1 
ATOM   2976 C CA   A LEU   A 1 127 ? 19.983 -5.609  -1.259  0.52 13.21 ?  127 LEU   A CA   1 
ATOM   2977 C CA   B LEU   A 1 127 ? 19.712 -5.451  -1.327  0.48 14.45 ?  127 LEU   A CA   1 
ATOM   2978 C C    A LEU   A 1 127 ? 19.367 -5.442  -2.638  0.52 12.45 ?  127 LEU   A C    1 
ATOM   2979 C C    B LEU   A 1 127 ? 19.175 -5.338  -2.752  0.48 14.43 ?  127 LEU   A C    1 
ATOM   2980 O O    A LEU   A 1 127 ? 18.579 -6.272  -3.099  0.52 13.34 ?  127 LEU   A O    1 
ATOM   2981 O O    B LEU   A 1 127 ? 18.278 -6.079  -3.175  0.48 13.96 ?  127 LEU   A O    1 
ATOM   2982 C CB   A LEU   A 1 127 ? 21.173 -6.563  -1.359  0.52 13.95 ?  127 LEU   A CB   1 
ATOM   2983 C CB   B LEU   A 1 127 ? 21.000 -6.288  -1.311  0.48 14.85 ?  127 LEU   A CB   1 
ATOM   2984 C CG   A LEU   A 1 127 ? 21.894 -6.886  -0.054  0.52 14.35 ?  127 LEU   A CG   1 
ATOM   2985 C CG   B LEU   A 1 127 ? 21.832 -6.295  -0.020  0.48 15.04 ?  127 LEU   A CG   1 
ATOM   2986 C CD1  A LEU   A 1 127 ? 22.979 -7.915  -0.310  0.52 15.16 ?  127 LEU   A CD1  1 
ATOM   2987 C CD1  B LEU   A 1 127 ? 23.026 -7.244  -0.139  0.48 15.22 ?  127 LEU   A CD1  1 
ATOM   2988 C CD2  A LEU   A 1 127 ? 22.486 -5.621  0.539   0.52 15.60 ?  127 LEU   A CD2  1 
ATOM   2989 C CD2  B LEU   A 1 127 ? 22.310 -4.892  0.337   0.48 15.69 ?  127 LEU   A CD2  1 
ATOM   2990 H H    A LEU   A 1 127 ? 19.186 -6.911  -0.017  0.52 15.29 ?  127 LEU   A H    1 
ATOM   2991 H H    B LEU   A 1 127 ? 18.777 -6.836  -0.252  0.48 16.86 ?  127 LEU   A H    1 
ATOM   2992 H HA   A LEU   A 1 127 ? 20.298 -4.746  -0.959  0.52 15.85 ?  127 LEU   A HA   1 
ATOM   2993 H HA   B LEU   A 1 127 ? 19.949 -4.563  -1.029  0.48 17.34 ?  127 LEU   A HA   1 
ATOM   2994 H HB2  A LEU   A 1 127 ? 20.859 -7.401  -1.732  0.52 16.74 ?  127 LEU   A HB2  1 
ATOM   2995 H HB2  B LEU   A 1 127 ? 20.771 -7.209  -1.500  0.48 17.82 ?  127 LEU   A HB2  1 
ATOM   2996 H HB3  A LEU   A 1 127 ? 21.826 -6.170  -1.959  0.52 16.74 ?  127 LEU   A HB3  1 
ATOM   2997 H HB3  B LEU   A 1 127 ? 21.584 -5.956  -2.013  0.48 17.82 ?  127 LEU   A HB3  1 
ATOM   2998 H HG   A LEU   A 1 127 ? 21.259 -7.259  0.582   0.52 17.22 ?  127 LEU   A HG   1 
ATOM   2999 H HG   B LEU   A 1 127 ? 21.279 -6.615  0.709   0.48 18.05 ?  127 LEU   A HG   1 
ATOM   3000 H HD11 A LEU   A 1 127 ? 23.396 -8.148  0.533   0.52 18.19 ?  127 LEU   A HD11 1 
ATOM   3001 H HD11 B LEU   A 1 127 ? 23.530 -7.230  0.694   0.48 18.26 ?  127 LEU   A HD11 1 
ATOM   3002 H HD12 A LEU   A 1 127 ? 22.580 -8.701  -0.713  0.52 18.19 ?  127 LEU   A HD12 1 
ATOM   3003 H HD12 B LEU   A 1 127 ? 22.702 -8.144  -0.309  0.48 18.26 ?  127 LEU   A HD12 1 
ATOM   3004 H HD13 A LEU   A 1 127 ? 23.636 -7.532  -0.911  0.52 18.19 ?  127 LEU   A HD13 1 
ATOM   3005 H HD13 B LEU   A 1 127 ? 23.593 -6.954  -0.870  0.48 18.26 ?  127 LEU   A HD13 1 
ATOM   3006 H HD21 A LEU   A 1 127 ? 23.019 -5.857  1.313   0.52 18.72 ?  127 LEU   A HD21 1 
ATOM   3007 H HD21 B LEU   A 1 127 ? 22.923 -4.947  1.087   0.48 18.82 ?  127 LEU   A HD21 1 
ATOM   3008 H HD22 A LEU   A 1 127 ? 23.044 -5.194  -0.131  0.52 18.72 ?  127 LEU   A HD22 1 
ATOM   3009 H HD22 B LEU   A 1 127 ? 22.760 -4.508  -0.432  0.48 18.82 ?  127 LEU   A HD22 1 
ATOM   3010 H HD23 A LEU   A 1 127 ? 21.767 -5.026  0.798   0.52 18.72 ?  127 LEU   A HD23 1 
ATOM   3011 H HD23 B LEU   A 1 127 ? 21.542 -4.351  0.576   0.48 18.82 ?  127 LEU   A HD23 1 
ATOM   3012 N N    A SER   A 1 128 ? 19.752 -4.362  -3.305  0.52 13.31 ?  128 SER   A N    1 
ATOM   3013 N N    B SER   A 1 128 ? 19.722 -4.366  -3.482  0.48 15.48 ?  128 SER   A N    1 
ATOM   3014 C CA   A SER   A 1 128 ? 19.328 -4.009  -4.649  0.52 13.66 ?  128 SER   A CA   1 
ATOM   3015 C CA   B SER   A 1 128 ? 19.509 -4.102  -4.903  0.48 16.51 ?  128 SER   A CA   1 
ATOM   3016 C C    A SER   A 1 128 ? 17.864 -3.604  -4.729  0.52 13.02 ?  128 SER   A C    1 
ATOM   3017 C C    B SER   A 1 128 ? 18.107 -3.626  -5.261  0.48 18.08 ?  128 SER   A C    1 
ATOM   3018 O O    A SER   A 1 128 ? 17.384 -3.324  -5.833  0.52 13.63 ?  128 SER   A O    1 
ATOM   3019 O O    B SER   A 1 128 ? 17.846 -3.380  -6.445  0.48 18.29 ?  128 SER   A O    1 
ATOM   3020 C CB   A SER   A 1 128 ? 19.681 -5.077  -5.695  0.52 14.43 ?  128 SER   A CB   1 
ATOM   3021 C CB   B SER   A 1 128 ? 19.926 -5.264  -5.818  0.48 15.36 ?  128 SER   A CB   1 
ATOM   3022 O OG   A SER   A 1 128 ? 21.090 -5.262  -5.764  0.52 14.97 ?  128 SER   A OG   1 
ATOM   3023 O OG   B SER   A 1 128 ? 21.341 -5.409  -5.819  0.48 14.24 ?  128 SER   A OG   1 
ATOM   3024 H H    A SER   A 1 128 ? 20.296 -3.783  -2.975  0.52 15.97 ?  128 SER   A H    1 
ATOM   3025 H H    B SER   A 1 128 ? 20.269 -3.793  -3.139  0.48 18.57 ?  128 SER   A H    1 
ATOM   3026 H HA   A SER   A 1 128 ? 19.822 -3.225  -4.896  0.52 16.39 ?  128 SER   A HA   1 
ATOM   3027 H HA   B SER   A 1 128 ? 20.089 -3.365  -5.129  0.48 19.81 ?  128 SER   A HA   1 
ATOM   3028 H HB2  A SER   A 1 128 ? 19.258 -5.913  -5.459  0.52 17.32 ?  128 SER   A HB2  1 
ATOM   3029 H HB2  B SER   A 1 128 ? 19.513 -6.078  -5.503  0.48 18.43 ?  128 SER   A HB2  1 
ATOM   3030 H HB3  A SER   A 1 128 ? 19.377 -4.777  -6.566  0.52 17.32 ?  128 SER   A HB3  1 
ATOM   3031 H HB3  B SER   A 1 128 ? 19.621 -5.064  -6.724  0.48 18.43 ?  128 SER   A HB3  1 
ATOM   3032 H HG   A SER   A 1 128 ? 21.468 -4.528  -5.926  0.52 17.96 ?  128 SER   A HG   1 
ATOM   3033 H HG   B SER   A 1 128 ? 21.689 -4.689  -6.083  0.48 17.09 ?  128 SER   A HG   1 
ATOM   3034 N N    A ALA   A 1 129 ? 17.150 -3.528  -3.604  0.52 13.22 ?  129 ALA   A N    1 
ATOM   3035 N N    B ALA   A 1 129 ? 17.206 -3.457  -4.298  0.48 19.40 ?  129 ALA   A N    1 
ATOM   3036 C CA   A ALA   A 1 129 ? 15.779 -3.041  -3.602  0.52 13.12 ?  129 ALA   A CA   1 
ATOM   3037 C CA   B ALA   A 1 129 ? 15.897 -2.909  -4.612  0.48 21.90 ?  129 ALA   A CA   1 
ATOM   3038 C C    A ALA   A 1 129 ? 15.764 -1.511  -3.600  0.52 14.12 ?  129 ALA   A C    1 
ATOM   3039 C C    B ALA   A 1 129 ? 15.928 -1.393  -4.421  0.48 23.30 ?  129 ALA   A C    1 
ATOM   3040 O O    A ALA   A 1 129 ? 16.804 -0.849  -3.608  0.52 15.56 ?  129 ALA   A O    1 
ATOM   3041 O O    B ALA   A 1 129 ? 16.981 -0.796  -4.185  0.48 23.38 ?  129 ALA   A O    1 
ATOM   3042 C CB   A ALA   A 1 129 ? 15.001 -3.619  -2.416  0.52 13.27 ?  129 ALA   A CB   1 
ATOM   3043 C CB   B ALA   A 1 129 ? 14.807 -3.611  -3.811  0.48 22.98 ?  129 ALA   A CB   1 
ATOM   3044 H H    A ALA   A 1 129 ? 17.438 -3.759  -2.819  0.52 15.87 ?  129 ALA   A H    1 
ATOM   3045 H H    B ALA   A 1 129 ? 17.325 -3.635  -3.459  0.48 23.28 ?  129 ALA   A H    1 
ATOM   3046 H HA   A ALA   A 1 129 ? 15.336 -3.331  -4.405  0.52 15.74 ?  129 ALA   A HA   1 
ATOM   3047 H HA   B ALA   A 1 129 ? 15.715 -3.068  -5.546  0.48 26.28 ?  129 ALA   A HA   1 
ATOM   3048 H HB1  A ALA   A 1 129 ? 14.088 -3.284  -2.435  0.52 15.92 ?  129 ALA   A HB1  1 
ATOM   3049 H HB1  B ALA   A 1 129 ? 13.956 -3.183  -3.999  0.48 27.57 ?  129 ALA   A HB1  1 
ATOM   3050 H HB2  A ALA   A 1 129 ? 14.994 -4.589  -2.477  0.52 15.92 ?  129 ALA   A HB2  1 
ATOM   3051 H HB2  B ALA   A 1 129 ? 14.780 -4.539  -4.085  0.48 27.57 ?  129 ALA   A HB2  1 
ATOM   3052 H HB3  A ALA   A 1 129 ? 15.428 -3.349  -1.584  0.52 15.92 ?  129 ALA   A HB3  1 
ATOM   3053 H HB3  B ALA   A 1 129 ? 15.018 -3.540  -2.873  0.48 27.57 ?  129 ALA   A HB3  1 
ATOM   3054 N N    A GLY   A 1 130 ? 14.568 -0.937  -3.598  0.52 13.49 ?  130 GLY   A N    1 
ATOM   3055 N N    B GLY   A 1 130 ? 14.776 -0.747  -4.544  0.48 24.86 ?  130 GLY   A N    1 
ATOM   3056 C CA   A GLY   A 1 130 ? 14.464 0.513   -3.563  0.52 14.23 ?  130 GLY   A CA   1 
ATOM   3057 C CA   B GLY   A 1 130 ? 14.769 0.702   -4.481  0.48 25.71 ?  130 GLY   A CA   1 
ATOM   3058 C C    A GLY   A 1 130 ? 15.098 1.147   -4.788  0.52 14.47 ?  130 GLY   A C    1 
ATOM   3059 C C    B GLY   A 1 130 ? 15.401 1.249   -5.743  0.48 26.36 ?  130 GLY   A C    1 
ATOM   3060 O O    A GLY   A 1 130 ? 14.885 0.704   -5.924  0.52 13.52 ?  130 GLY   A O    1 
ATOM   3061 O O    B GLY   A 1 130 ? 15.043 0.852   -6.858  0.48 26.01 ?  130 GLY   A O    1 
ATOM   3062 H H    A GLY   A 1 130 ? 13.816 -1.361  -3.615  0.52 16.19 ?  130 GLY   A H    1 
ATOM   3063 H H    B GLY   A 1 130 ? 14.008 -1.105  -4.690  0.48 29.83 ?  130 GLY   A H    1 
ATOM   3064 H HA2  A GLY   A 1 130 ? 13.527 0.765   -3.528  0.52 17.08 ?  130 GLY   A HA2  1 
ATOM   3065 H HA2  B GLY   A 1 130 ? 13.853 1.030   -4.414  0.48 30.85 ?  130 GLY   A HA2  1 
ATOM   3066 H HA3  A GLY   A 1 130 ? 14.905 0.852   -2.770  0.52 17.08 ?  130 GLY   A HA3  1 
ATOM   3067 H HA3  B GLY   A 1 130 ? 15.272 1.012   -3.707  0.48 30.85 ?  130 GLY   A HA3  1 
ATOM   3068 N N    A ILE   A 1 131 ? 15.891 2.199   -4.556  0.52 14.70 ?  131 ILE   A N    1 
ATOM   3069 N N    B ILE   A 1 131 ? 16.383 2.141   -5.580  0.48 27.15 ?  131 ILE   A N    1 
ATOM   3070 C CA   A ILE   A 1 131 ? 16.474 2.976   -5.648  0.52 15.44 ?  131 ILE   A CA   1 
ATOM   3071 C CA   B ILE   A 1 131 ? 16.947 2.833   -6.735  0.48 27.71 ?  131 ILE   A CA   1 
ATOM   3072 C C    A ILE   A 1 131 ? 17.523 2.214   -6.442  0.52 14.32 ?  131 ILE   A C    1 
ATOM   3073 C C    B ILE   A 1 131 ? 17.845 1.929   -7.571  0.48 26.67 ?  131 ILE   A C    1 
ATOM   3074 O O    A ILE   A 1 131 ? 17.980 2.717   -7.476  0.52 14.57 ?  131 ILE   A O    1 
ATOM   3075 O O    B ILE   A 1 131 ? 18.119 2.247   -8.733  0.48 26.41 ?  131 ILE   A O    1 
ATOM   3076 C CB   A ILE   A 1 131 ? 17.033 4.333   -5.168  0.52 17.55 ?  131 ILE   A CB   1 
ATOM   3077 C CB   B ILE   A 1 131 ? 17.628 4.163   -6.342  0.48 29.43 ?  131 ILE   A CB   1 
ATOM   3078 C CG1  A ILE   A 1 131 ? 18.300 4.146   -4.326  0.52 18.24 ?  131 ILE   A CG1  1 
ATOM   3079 C CG1  B ILE   A 1 131 ? 19.064 3.932   -5.858  0.48 30.87 ?  131 ILE   A CG1  1 
ATOM   3080 C CG2  A ILE   A 1 131 ? 15.971 5.093   -4.393  0.52 18.39 ?  131 ILE   A CG2  1 
ATOM   3081 C CG2  B ILE   A 1 131 ? 16.795 4.887   -5.275  0.48 29.48 ?  131 ILE   A CG2  1 
ATOM   3082 C CD1  A ILE   A 1 131 ? 18.958 5.458   -3.920  0.52 19.20 ?  131 ILE   A CD1  1 
ATOM   3083 C CD1  B ILE   A 1 131 ? 20.062 4.887   -6.471  0.48 31.78 ?  131 ILE   A CD1  1 
ATOM   3084 H H    A ILE   A 1 131 ? 16.085 2.490   -3.769  0.52 17.64 ?  131 ILE   A H    1 
ATOM   3085 H H    B ILE   A 1 131 ? 16.735 2.348   -4.825  0.48 32.58 ?  131 ILE   A H    1 
ATOM   3086 H HA   A ILE   A 1 131 ? 15.760 3.178   -6.266  0.52 18.53 ?  131 ILE   A HA   1 
ATOM   3087 H HA   B ILE   A 1 131 ? 16.221 3.076   -7.317  0.48 33.25 ?  131 ILE   A HA   1 
ATOM   3088 H HB   A ILE   A 1 131 ? 17.261 4.853   -5.950  0.52 21.06 ?  131 ILE   A HB   1 
ATOM   3089 H HB   B ILE   A 1 131 ? 17.659 4.744   -7.124  0.48 35.31 ?  131 ILE   A HB   1 
ATOM   3090 H HG12 A ILE   A 1 131 ? 18.069 3.662   -3.517  0.52 21.88 ?  131 ILE   A HG12 1 
ATOM   3091 H HG12 B ILE   A 1 131 ? 19.083 4.074   -4.906  0.48 37.05 ?  131 ILE   A HG12 1 
ATOM   3092 H HG13 A ILE   A 1 131 ? 18.951 3.640   -4.836  0.52 21.88 ?  131 ILE   A HG13 1 
ATOM   3093 H HG13 B ILE   A 1 131 ? 19.364 3.030   -6.046  0.48 37.05 ?  131 ILE   A HG13 1 
ATOM   3094 H HG21 A ILE   A 1 131 ? 16.273 6.004   -4.253  0.52 22.07 ?  131 ILE   A HG21 1 
ATOM   3095 H HG21 B ILE   A 1 131 ? 17.121 5.795   -5.170  0.48 35.38 ?  131 ILE   A HG21 1 
ATOM   3096 H HG22 A ILE   A 1 131 ? 15.147 5.093   -4.904  0.52 22.07 ?  131 ILE   A HG22 1 
ATOM   3097 H HG22 B ILE   A 1 131 ? 15.865 4.904   -5.559  0.48 35.38 ?  131 ILE   A HG22 1 
ATOM   3098 H HG23 A ILE   A 1 131 ? 15.829 4.656   -3.538  0.52 22.07 ?  131 ILE   A HG23 1 
ATOM   3099 H HG23 B ILE   A 1 131 ? 16.871 4.410   -4.434  0.48 35.38 ?  131 ILE   A HG23 1 
ATOM   3100 H HD11 A ILE   A 1 131 ? 19.807 5.265   -3.493  0.52 23.04 ?  131 ILE   A HD11 1 
ATOM   3101 H HD11 B ILE   A 1 131 ? 20.945 4.675   -6.133  0.48 38.13 ?  131 ILE   A HD11 1 
ATOM   3102 H HD12 A ILE   A 1 131 ? 19.101 5.997   -4.713  0.52 23.04 ?  131 ILE   A HD12 1 
ATOM   3103 H HD12 B ILE   A 1 131 ? 20.045 4.790   -7.437  0.48 38.13 ?  131 ILE   A HD12 1 
ATOM   3104 H HD13 A ILE   A 1 131 ? 18.376 5.927   -3.302  0.52 23.04 ?  131 ILE   A HD13 1 
ATOM   3105 H HD13 B ILE   A 1 131 ? 19.819 5.793   -6.225  0.48 38.13 ?  131 ILE   A HD13 1 
ATOM   3106 N N    A PHE   A 1 132 ? 17.916 1.013   -5.996  0.52 13.75 ?  132 PHE   A N    1 
ATOM   3107 N N    B PHE   A 1 132 ? 18.317 0.810   -7.021  0.48 25.70 ?  132 PHE   A N    1 
ATOM   3108 C CA   A PHE   A 1 132 ? 18.805 0.173   -6.789  0.52 14.17 ?  132 PHE   A CA   1 
ATOM   3109 C CA   B PHE   A 1 132 ? 19.120 -0.101  -7.828  0.48 25.50 ?  132 PHE   A CA   1 
ATOM   3110 C C    A PHE   A 1 132 ? 18.070 -0.583  -7.891  0.52 14.80 ?  132 PHE   A C    1 
ATOM   3111 C C    B PHE   A 1 132 ? 18.284 -0.911  -8.810  0.48 24.42 ?  132 PHE   A C    1 
ATOM   3112 O O    A PHE   A 1 132 ? 18.724 -1.177  -8.755  0.52 15.44 ?  132 PHE   A O    1 
ATOM   3113 O O    B PHE   A 1 132 ? 18.849 -1.673  -9.603  0.48 23.50 ?  132 PHE   A O    1 
ATOM   3114 C CB   A PHE   A 1 132 ? 19.573 -0.812  -5.896  0.52 13.41 ?  132 PHE   A CB   1 
ATOM   3115 C CB   B PHE   A 1 132 ? 19.999 -1.003  -6.948  0.48 26.57 ?  132 PHE   A CB   1 
ATOM   3116 C CG   A PHE   A 1 132 ? 20.787 -0.220  -5.212  0.52 13.16 ?  132 PHE   A CG   1 
ATOM   3117 C CG   B PHE   A 1 132 ? 21.337 -0.394  -6.599  0.48 28.30 ?  132 PHE   A CG   1 
ATOM   3118 C CD1  A PHE   A 1 132 ? 20.652 0.806   -4.290  0.52 14.28 ?  132 PHE   A CD1  1 
ATOM   3119 C CD1  B PHE   A 1 132 ? 21.644 0.907   -6.978  0.48 29.54 ?  132 PHE   A CD1  1 
ATOM   3120 C CD2  A PHE   A 1 132 ? 22.057 -0.722  -5.462  0.52 13.79 ?  132 PHE   A CD2  1 
ATOM   3121 C CD2  B PHE   A 1 132 ? 22.290 -1.124  -5.910  0.48 28.42 ?  132 PHE   A CD2  1 
ATOM   3122 C CE1  A PHE   A 1 132 ? 21.765 1.342   -3.656  0.52 14.85 ?  132 PHE   A CE1  1 
ATOM   3123 C CE1  B PHE   A 1 132 ? 22.860 1.464   -6.672  0.48 29.80 ?  132 PHE   A CE1  1 
ATOM   3124 C CE2  A PHE   A 1 132 ? 23.171 -0.197  -4.825  0.52 14.37 ?  132 PHE   A CE2  1 
ATOM   3125 C CE2  B PHE   A 1 132 ? 23.514 -0.566  -5.598  0.48 28.93 ?  132 PHE   A CE2  1 
ATOM   3126 C CZ   A PHE   A 1 132 ? 23.022 0.836   -3.921  0.52 14.22 ?  132 PHE   A CZ   1 
ATOM   3127 C CZ   B PHE   A 1 132 ? 23.799 0.729   -5.981  0.48 29.34 ?  132 PHE   A CZ   1 
ATOM   3128 H H    A PHE   A 1 132 ? 17.690 0.670   -5.233  0.52 16.50 ?  132 PHE   A H    1 
ATOM   3129 H H    B PHE   A 1 132 ? 18.184 0.566   -6.202  0.48 30.85 ?  132 PHE   A H    1 
ATOM   3130 H HA   A PHE   A 1 132 ? 19.457 0.743   -7.214  0.52 17.00 ?  132 PHE   A HA   1 
ATOM   3131 H HA   B PHE   A 1 132 ? 19.696 0.435   -8.389  0.48 30.60 ?  132 PHE   A HA   1 
ATOM   3132 H HB2  A PHE   A 1 132 ? 18.974 -1.137  -5.205  0.52 16.09 ?  132 PHE   A HB2  1 
ATOM   3133 H HB2  B PHE   A 1 132 ? 19.536 -1.190  -6.116  0.48 31.88 ?  132 PHE   A HB2  1 
ATOM   3134 H HB3  A PHE   A 1 132 ? 19.874 -1.554  -6.444  0.52 16.09 ?  132 PHE   A HB3  1 
ATOM   3135 H HB3  B PHE   A 1 132 ? 20.167 -1.831  -7.425  0.48 31.88 ?  132 PHE   A HB3  1 
ATOM   3136 H HD1  A PHE   A 1 132 ? 19.807 1.151   -4.106  0.52 17.14 ?  132 PHE   A HD1  1 
ATOM   3137 H HD1  B PHE   A 1 132 ? 21.015 1.411   -7.447  0.48 35.45 ?  132 PHE   A HD1  1 
ATOM   3138 H HD2  A PHE   A 1 132 ? 22.163 -1.414  -6.072  0.52 16.55 ?  132 PHE   A HD2  1 
ATOM   3139 H HD2  B PHE   A 1 132 ? 22.105 -1.997  -5.649  0.48 34.11 ?  132 PHE   A HD2  1 
ATOM   3140 H HE1  A PHE   A 1 132 ? 21.662 2.036   -3.043  0.52 17.82 ?  132 PHE   A HE1  1 
ATOM   3141 H HE1  B PHE   A 1 132 ? 23.045 2.338   -6.935  0.48 35.76 ?  132 PHE   A HE1  1 
ATOM   3142 H HE2  A PHE   A 1 132 ? 24.016 -0.533  -5.012  0.52 17.25 ?  132 PHE   A HE2  1 
ATOM   3143 H HE2  B PHE   A 1 132 ? 24.147 -1.063  -5.133  0.48 34.72 ?  132 PHE   A HE2  1 
ATOM   3144 H HZ   A PHE   A 1 132 ? 23.766 1.197   -3.495  0.52 17.06 ?  132 PHE   A HZ   1 
ATOM   3145 H HZ   B PHE   A 1 132 ? 24.620 1.107   -5.775  0.48 35.21 ?  132 PHE   A HZ   1 
ATOM   3146 N N    A GLY   A 1 133 ? 16.737 -0.585  -7.878  0.52 14.90 ?  133 GLY   A N    1 
ATOM   3147 N N    B GLY   A 1 133 ? 16.965 -0.754  -8.784  0.48 24.13 ?  133 GLY   A N    1 
ATOM   3148 C CA   A GLY   A 1 133 ? 15.967 -0.957  -9.045  0.52 15.31 ?  133 GLY   A CA   1 
ATOM   3149 C CA   B GLY   A 1 133 ? 16.120 -1.149  -9.886  0.48 24.04 ?  133 GLY   A CA   1 
ATOM   3150 C C    A GLY   A 1 133 ? 15.680 -2.430  -9.247  0.52 15.60 ?  133 GLY   A C    1 
ATOM   3151 C C    B GLY   A 1 133 ? 15.600 -2.569  -9.852  0.48 23.95 ?  133 GLY   A C    1 
ATOM   3152 O O    A GLY   A 1 133 ? 15.091 -2.778  -10.278 0.52 16.90 ?  133 GLY   A O    1 
ATOM   3153 O O    B GLY   A 1 133 ? 14.688 -2.888  -10.625 0.48 24.74 ?  133 GLY   A O    1 
ATOM   3154 H H    A GLY   A 1 133 ? 16.249 -0.372  -7.192  0.52 17.88 ?  133 GLY   A H    1 
ATOM   3155 H H    B GLY   A 1 133 ? 16.541 -0.410  -8.122  0.48 28.96 ?  133 GLY   A H    1 
ATOM   3156 H HA2  A GLY   A 1 133 ? 15.107 -0.509  -9.009  0.52 18.37 ?  133 GLY   A HA2  1 
ATOM   3157 H HA2  B GLY   A 1 133 ? 15.368 -0.537  -9.927  0.48 28.85 ?  133 GLY   A HA2  1 
ATOM   3158 H HA3  A GLY   A 1 133 ? 16.431 -0.647  -9.834  0.52 18.37 ?  133 GLY   A HA3  1 
ATOM   3159 H HA3  B GLY   A 1 133 ? 16.623 -1.054  -10.710 0.48 28.85 ?  133 GLY   A HA3  1 
ATOM   3160 N N    A ALA   A 1 134 ? 16.052 -3.304  -8.313  0.52 15.44 ?  134 ALA   A N    1 
ATOM   3161 N N    B ALA   A 1 134 ? 16.139 -3.432  -8.995  0.48 23.11 ?  134 ALA   A N    1 
ATOM   3162 C CA   A ALA   A 1 134 ? 15.718 -4.714  -8.460  0.52 15.96 ?  134 ALA   A CA   1 
ATOM   3163 C CA   B ALA   A 1 134 ? 15.811 -4.847  -9.069  0.48 22.81 ?  134 ALA   A CA   1 
ATOM   3164 C C    A ALA   A 1 134 ? 14.374 -5.019  -7.805  0.52 16.44 ?  134 ALA   A C    1 
ATOM   3165 C C    B ALA   A 1 134 ? 14.457 -5.144  -8.422  0.48 22.64 ?  134 ALA   A C    1 
ATOM   3166 O O    A ALA   A 1 134 ? 13.855 -4.245  -6.997  0.52 17.58 ?  134 ALA   A O    1 
ATOM   3167 O O    B ALA   A 1 134 ? 13.866 -4.316  -7.724  0.48 22.55 ?  134 ALA   A O    1 
ATOM   3168 C CB   A ALA   A 1 134 ? 16.804 -5.609  -7.862  0.52 16.06 ?  134 ALA   A CB   1 
ATOM   3169 C CB   B ALA   A 1 134 ? 16.910 -5.688  -8.425  0.48 22.83 ?  134 ALA   A CB   1 
ATOM   3170 H H    A ALA   A 1 134 ? 16.483 -3.107  -7.591  0.52 18.53 ?  134 ALA   A H    1 
ATOM   3171 H H    B ALA   A 1 134 ? 16.699 -3.222  -8.375  0.48 27.73 ?  134 ALA   A H    1 
ATOM   3172 H HA   A ALA   A 1 134 ? 15.640 -4.921  -9.401  0.52 19.15 ?  134 ALA   A HA   1 
ATOM   3173 H HA   B ALA   A 1 134 ? 15.748 -5.096  -10.002 0.48 27.38 ?  134 ALA   A HA   1 
ATOM   3174 H HB1  A ALA   A 1 134 ? 16.563 -6.535  -8.018  0.52 19.28 ?  134 ALA   A HB1  1 
ATOM   3175 H HB1  B ALA   A 1 134 ? 16.674 -6.625  -8.508  0.48 27.40 ?  134 ALA   A HB1  1 
ATOM   3176 H HB2  A ALA   A 1 134 ? 17.645 -5.406  -8.299  0.52 19.28 ?  134 ALA   A HB2  1 
ATOM   3177 H HB2  B ALA   A 1 134 ? 17.746 -5.515  -8.886  0.48 27.40 ?  134 ALA   A HB2  1 
ATOM   3178 H HB3  A ALA   A 1 134 ? 16.870 -5.435  -6.913  0.52 19.28 ?  134 ALA   A HB3  1 
ATOM   3179 H HB3  B ALA   A 1 134 ? 16.988 -5.445  -7.491  0.48 27.40 ?  134 ALA   A HB3  1 
ATOM   3180 N N    A ASP   A 1 135 ? 13.811 -6.161  -8.184  0.52 16.31 ?  135 ASP   A N    1 
ATOM   3181 N N    B ASP   A 1 135 ? 13.975 -6.360  -8.672  0.48 22.45 ?  135 ASP   A N    1 
ATOM   3182 C CA   A ASP   A 1 135 ? 12.558 -6.644  -7.614  0.52 16.49 ?  135 ASP   A CA   1 
ATOM   3183 C CA   B ASP   A 1 135 ? 12.674 -6.803  -8.182  0.48 22.67 ?  135 ASP   A CA   1 
ATOM   3184 C C    A ASP   A 1 135 ? 12.790 -7.076  -6.171  0.52 14.43 ?  135 ASP   A C    1 
ATOM   3185 C C    B ASP   A 1 135 ? 12.808 -7.287  -6.740  0.48 20.83 ?  135 ASP   A C    1 
ATOM   3186 O O    A ASP   A 1 135 ? 13.565 -8.013  -5.933  0.52 13.94 ?  135 ASP   A O    1 
ATOM   3187 O O    B ASP   A 1 135 ? 13.593 -8.205  -6.479  0.48 20.52 ?  135 ASP   A O    1 
ATOM   3188 C CB   A ASP   A 1 135 ? 12.079 -7.840  -8.434  0.52 19.34 ?  135 ASP   A CB   1 
ATOM   3189 C CB   B ASP   A 1 135 ? 12.169 -7.943  -9.060  0.48 24.77 ?  135 ASP   A CB   1 
ATOM   3190 C CG   A ASP   A 1 135 ? 10.893 -8.558  -7.806  0.52 21.93 ?  135 ASP   A CG   1 
ATOM   3191 C CG   B ASP   A 1 135 ? 10.725 -8.329  -8.760  0.48 26.52 ?  135 ASP   A CG   1 
ATOM   3192 O OD1  A ASP   A 1 135 ? 10.201 -7.972  -6.947  0.52 21.88 ?  135 ASP   A OD1  1 
ATOM   3193 O OD1  B ASP   A 1 135 ? 10.151 -7.802  -7.786  0.48 26.98 ?  135 ASP   A OD1  1 
ATOM   3194 O OD2  A ASP   A 1 135 ? 10.671 -9.731  -8.168  0.52 24.65 -1 135 ASP   A OD2  1 
ATOM   3195 O OD2  B ASP   A 1 135 ? 10.164 -9.169  -9.495  0.48 27.26 -1 135 ASP   A OD2  1 
ATOM   3196 H H    A ASP   A 1 135 ? 14.136 -6.686  -8.776  0.52 19.57 ?  135 ASP   A H    1 
ATOM   3197 H H    B ASP   A 1 135 ? 14.388 -6.954  -9.134  0.48 26.93 ?  135 ASP   A H    1 
ATOM   3198 H HA   A ASP   A 1 135 ? 11.882 -5.949  -7.653  0.52 19.79 ?  135 ASP   A HA   1 
ATOM   3199 H HA   B ASP   A 1 135 ? 12.039 -6.072  -8.239  0.48 27.20 ?  135 ASP   A HA   1 
ATOM   3200 H HB2  A ASP   A 1 135 ? 11.848 -7.537  -9.330  0.52 23.21 ?  135 ASP   A HB2  1 
ATOM   3201 H HB2  B ASP   A 1 135 ? 12.259 -7.679  -9.995  0.48 29.73 ?  135 ASP   A HB2  1 
ATOM   3202 H HB3  A ASP   A 1 135 ? 12.783 -8.500  -8.481  0.52 23.21 ?  135 ASP   A HB3  1 
ATOM   3203 H HB3  B ASP   A 1 135 ? 12.704 -8.732  -8.892  0.48 29.73 ?  135 ASP   A HB3  1 
ATOM   3204 N N    A PRO   A 1 136 ? 12.155 -6.437  -5.185  0.52 14.14 ?  136 PRO   A N    1 
ATOM   3205 N N    B PRO   A 1 136 ? 12.064 -6.718  -5.787  0.48 20.20 ?  136 PRO   A N    1 
ATOM   3206 C CA   A PRO   A 1 136 ? 12.365 -6.851  -3.786  0.52 13.88 ?  136 PRO   A CA   1 
ATOM   3207 C CA   B PRO   A 1 136 ? 12.259 -7.108  -4.378  0.48 19.41 ?  136 PRO   A CA   1 
ATOM   3208 C C    A PRO   A 1 136 ? 11.931 -8.280  -3.487  0.52 13.02 ?  136 PRO   A C    1 
ATOM   3209 C C    B PRO   A 1 136 ? 11.911 -8.559  -4.080  0.48 18.17 ?  136 PRO   A C    1 
ATOM   3210 O O    A PRO   A 1 136 ? 12.529 -8.921  -2.612  0.52 12.84 ?  136 PRO   A O    1 
ATOM   3211 O O    B PRO   A 1 136 ? 12.547 -9.169  -3.210  0.48 18.22 ?  136 PRO   A O    1 
ATOM   3212 C CB   A PRO   A 1 136 ? 11.547 -5.820  -2.993  0.52 14.92 ?  136 PRO   A CB   1 
ATOM   3213 C CB   B PRO   A 1 136 ? 11.351 -6.135  -3.610  0.48 20.08 ?  136 PRO   A CB   1 
ATOM   3214 C CG   A PRO   A 1 136 ? 10.496 -5.354  -3.970  0.52 15.87 ?  136 PRO   A CG   1 
ATOM   3215 C CG   B PRO   A 1 136 ? 11.070 -5.010  -4.566  0.48 20.60 ?  136 PRO   A CG   1 
ATOM   3216 C CD   A PRO   A 1 136 ? 11.182 -5.337  -5.300  0.52 15.57 ?  136 PRO   A CD   1 
ATOM   3217 C CD   B PRO   A 1 136 ? 11.085 -5.627  -5.926  0.48 20.47 ?  136 PRO   A CD   1 
ATOM   3218 H HA   A PRO   A 1 136 ? 13.301 -6.748  -3.542  0.52 16.66 ?  136 PRO   A HA   1 
ATOM   3219 H HA   B PRO   A 1 136 ? 13.180 -6.950  -4.112  0.48 23.29 ?  136 PRO   A HA   1 
ATOM   3220 H HB2  A PRO   A 1 136 ? 11.135 -6.244  -2.222  0.52 17.91 ?  136 PRO   A HB2  1 
ATOM   3221 H HB2  B PRO   A 1 136 ? 10.528 -6.588  -3.363  0.48 24.10 ?  136 PRO   A HB2  1 
ATOM   3222 H HB3  A PRO   A 1 136 ? 12.114 -5.081  -2.717  0.52 17.91 ?  136 PRO   A HB3  1 
ATOM   3223 H HB3  B PRO   A 1 136 ? 11.811 -5.808  -2.821  0.48 24.10 ?  136 PRO   A HB3  1 
ATOM   3224 H HG2  A PRO   A 1 136 ? 9.756  -5.978  -3.974  0.52 19.04 ?  136 PRO   A HG2  1 
ATOM   3225 H HG2  B PRO   A 1 136 ? 10.198 -4.627  -4.379  0.48 24.72 ?  136 PRO   A HG2  1 
ATOM   3226 H HG3  A PRO   A 1 136 ? 10.197 -4.464  -3.728  0.52 19.04 ?  136 PRO   A HG3  1 
ATOM   3227 H HG3  B PRO   A 1 136 ? 11.762 -4.334  -4.493  0.48 24.72 ?  136 PRO   A HG3  1 
ATOM   3228 H HD2  A PRO   A 1 136 ? 10.543 -5.526  -6.007  0.52 18.68 ?  136 PRO   A HD2  1 
ATOM   3229 H HD2  B PRO   A 1 136 ? 10.212 -5.987  -6.151  0.48 24.57 ?  136 PRO   A HD2  1 
ATOM   3230 H HD3  A PRO   A 1 136 ? 11.632 -4.489  -5.444  0.52 18.68 ?  136 PRO   A HD3  1 
ATOM   3231 H HD3  B PRO   A 1 136 ? 11.382 -4.976  -6.581  0.48 24.57 ?  136 PRO   A HD3  1 
ATOM   3232 N N    A ILE   A 1 137 ? 10.898 -8.792  -4.161  0.52 13.92 ?  137 ILE   A N    1 
ATOM   3233 N N    B ILE   A 1 137 ? 10.907 -9.123  -4.755  0.48 17.93 ?  137 ILE   A N    1 
ATOM   3234 C CA   A ILE   A 1 137 ? 10.534 -10.194 -3.973  0.52 14.46 ?  137 ILE   A CA   1 
ATOM   3235 C CA   B ILE   A 1 137 ? 10.576 -10.535 -4.564  0.48 18.80 ?  137 ILE   A CA   1 
ATOM   3236 C C    A ILE   A 1 137 ? 11.698 -11.094 -4.366  0.52 14.37 ?  137 ILE   A C    1 
ATOM   3237 C C    B ILE   A 1 137 ? 11.802 -11.402 -4.818  0.48 18.66 ?  137 ILE   A C    1 
ATOM   3238 O O    A ILE   A 1 137 ? 12.013 -12.077 -3.679  0.52 14.61 ?  137 ILE   A O    1 
ATOM   3239 O O    B ILE   A 1 137 ? 12.120 -12.313 -4.043  0.48 18.63 ?  137 ILE   A O    1 
ATOM   3240 C CB   A ILE   A 1 137 ? 9.256  -10.532 -4.764  0.52 15.55 ?  137 ILE   A CB   1 
ATOM   3241 C CB   B ILE   A 1 137 ? 9.396  -10.934 -5.470  0.48 19.35 ?  137 ILE   A CB   1 
ATOM   3242 C CG1  A ILE   A 1 137 ? 8.092  -9.642  -4.311  0.52 17.25 ?  137 ILE   A CG1  1 
ATOM   3243 C CG1  B ILE   A 1 137 ? 8.119  -10.210 -5.034  0.48 19.84 ?  137 ILE   A CG1  1 
ATOM   3244 C CG2  A ILE   A 1 137 ? 8.898  -12.008 -4.601  0.52 16.16 ?  137 ILE   A CG2  1 
ATOM   3245 C CG2  B ILE   A 1 137 ? 9.178  -12.441 -5.444  0.48 19.44 ?  137 ILE   A CG2  1 
ATOM   3246 C CD1  A ILE   A 1 137 ? 6.811  -9.868  -5.089  0.52 18.16 ?  137 ILE   A CD1  1 
ATOM   3247 C CD1  B ILE   A 1 137 ? 6.903  -10.552 -5.879  0.48 20.99 ?  137 ILE   A CD1  1 
ATOM   3248 H H    A ILE   A 1 137 ? 10.406 -8.351  -4.715  0.52 16.71 ?  137 ILE   A H    1 
ATOM   3249 H H    B ILE   A 1 137 ? 10.409 -8.714  -5.322  0.48 21.51 ?  137 ILE   A H    1 
ATOM   3250 H HA   A ILE   A 1 137 ? 10.349 -10.340 -3.037  0.52 17.35 ?  137 ILE   A HA   1 
ATOM   3251 H HA   B ILE   A 1 137 ? 10.303 -10.675 -3.647  0.48 22.56 ?  137 ILE   A HA   1 
ATOM   3252 H HB   A ILE   A 1 137 ? 9.417  -10.357 -5.702  0.52 18.66 ?  137 ILE   A HB   1 
ATOM   3253 H HB   B ILE   A 1 137 ? 9.601  -10.669 -6.382  0.48 23.21 ?  137 ILE   A HB   1 
ATOM   3254 H HG12 A ILE   A 1 137 ? 7.907  -9.818  -3.375  0.52 20.70 ?  137 ILE   A HG12 1 
ATOM   3255 H HG12 B ILE   A 1 137 ? 7.921  -10.452 -4.117  0.48 23.80 ?  137 ILE   A HG12 1 
ATOM   3256 H HG13 A ILE   A 1 137 ? 8.343  -8.710  -4.424  0.52 20.70 ?  137 ILE   A HG13 1 
ATOM   3257 H HG13 B ILE   A 1 137 ? 8.264  -9.253  -5.099  0.48 23.80 ?  137 ILE   A HG13 1 
ATOM   3258 H HG21 A ILE   A 1 137 ? 8.060  -12.190 -5.049  0.52 19.39 ?  137 ILE   A HG21 1 
ATOM   3259 H HG21 B ILE   A 1 137 ? 8.381  -12.662 -5.952  0.48 23.33 ?  137 ILE   A HG21 1 
ATOM   3260 H HG22 A ILE   A 1 137 ? 9.600  -12.544 -4.994  0.52 19.39 ?  137 ILE   A HG22 1 
ATOM   3261 H HG22 B ILE   A 1 137 ? 9.941  -12.880 -5.848  0.48 23.33 ?  137 ILE   A HG22 1 
ATOM   3262 H HG23 A ILE   A 1 137 ? 8.817  -12.204 -3.655  0.52 19.39 ?  137 ILE   A HG23 1 
ATOM   3263 H HG23 B ILE   A 1 137 ? 9.074  -12.725 -4.526  0.48 23.33 ?  137 ILE   A HG23 1 
ATOM   3264 H HD11 A ILE   A 1 137 ? 6.137  -10.229 -4.492  0.52 21.79 ?  137 ILE   A HD11 1 
ATOM   3265 H HD11 B ILE   A 1 137 ? 6.228  -9.870  -5.753  0.48 25.19 ?  137 ILE   A HD11 1 
ATOM   3266 H HD12 A ILE   A 1 137 ? 6.522  -9.021  -5.452  0.52 21.79 ?  137 ILE   A HD12 1 
ATOM   3267 H HD12 B ILE   A 1 137 ? 7.169  -10.588 -6.813  0.48 25.19 ?  137 ILE   A HD12 1 
ATOM   3268 H HD13 A ILE   A 1 137 ? 6.983  -10.490 -5.814  0.52 21.79 ?  137 ILE   A HD13 1 
ATOM   3269 H HD13 B ILE   A 1 137 ? 6.558  -11.416 -5.602  0.48 25.19 ?  137 ILE   A HD13 1 
ATOM   3270 N N    A HIS   A 1 138 ? 12.354 -10.771 -5.481  0.52 14.24 ?  138 HIS   A N    1 
ATOM   3271 N N    B HIS   A 1 138 ? 12.513 -11.127 -5.911  0.48 18.89 ?  138 HIS   A N    1 
ATOM   3272 C CA   A HIS   A 1 138 ? 13.541 -11.519 -5.882  0.52 14.59 ?  138 HIS   A CA   1 
ATOM   3273 C CA   B HIS   A 1 138 ? 13.699 -11.910 -6.236  0.48 18.46 ?  138 HIS   A CA   1 
ATOM   3274 C C    A HIS   A 1 138 ? 14.672 -11.351 -4.873  0.52 14.23 ?  138 HIS   A C    1 
ATOM   3275 C C    B HIS   A 1 138 ? 14.772 -11.761 -5.164  0.48 16.85 ?  138 HIS   A C    1 
ATOM   3276 O O    A HIS   A 1 138 ? 15.332 -12.330 -4.503  0.52 14.53 ?  138 HIS   A O    1 
ATOM   3277 O O    B HIS   A 1 138 ? 15.412 -12.746 -4.775  0.48 16.64 ?  138 HIS   A O    1 
ATOM   3278 C CB   A HIS   A 1 138 ? 13.968 -11.095 -7.288  0.52 15.21 ?  138 HIS   A CB   1 
ATOM   3279 C CB   B HIS   A 1 138 ? 14.242 -11.495 -7.602  0.48 19.07 ?  138 HIS   A CB   1 
ATOM   3280 C CG   A HIS   A 1 138 ? 15.237 -11.741 -7.757  0.52 16.33 ?  138 HIS   A CG   1 
ATOM   3281 C CG   B HIS   A 1 138 ? 15.476 -12.238 -8.009  0.48 19.87 ?  138 HIS   A CG   1 
ATOM   3282 N ND1  A HIS   A 1 138 ? 15.342 -13.095 -7.991  0.52 17.36 ?  138 HIS   A ND1  1 
ATOM   3283 N ND1  B HIS   A 1 138 ? 15.509 -13.611 -8.135  0.48 20.75 ?  138 HIS   A ND1  1 
ATOM   3284 C CD2  A HIS   A 1 138 ? 16.453 -11.216 -8.036  0.52 16.38 ?  138 HIS   A CD2  1 
ATOM   3285 C CD2  B HIS   A 1 138 ? 16.722 -11.803 -8.309  0.48 20.54 ?  138 HIS   A CD2  1 
ATOM   3286 C CE1  A HIS   A 1 138 ? 16.567 -13.376 -8.396  0.52 17.62 ?  138 HIS   A CE1  1 
ATOM   3287 C CE1  B HIS   A 1 138 ? 16.720 -13.988 -8.503  0.48 21.35 ?  138 HIS   A CE1  1 
ATOM   3288 N NE2  A HIS   A 1 138 ? 17.264 -12.254 -8.428  0.52 16.96 ?  138 HIS   A NE2  1 
ATOM   3289 N NE2  B HIS   A 1 138 ? 17.477 -12.910 -8.613  0.48 20.88 ?  138 HIS   A NE2  1 
ATOM   3290 H H    A HIS   A 1 138 ? 12.136 -10.132 -6.017  0.52 17.08 ?  138 HIS   A H    1 
ATOM   3291 H H    B HIS   A 1 138 ? 12.339 -10.491 -6.466  0.48 22.66 ?  138 HIS   A H    1 
ATOM   3292 H HA   A HIS   A 1 138 ? 13.314 -12.459 -5.918  0.52 17.51 ?  138 HIS   A HA   1 
ATOM   3293 H HA   B HIS   A 1 138 ? 13.458 -12.844 -6.285  0.48 22.15 ?  138 HIS   A HA   1 
ATOM   3294 H HB2  A HIS   A 1 138 ? 13.264 -11.332 -7.915  0.52 18.25 ?  138 HIS   A HB2  1 
ATOM   3295 H HB2  B HIS   A 1 138 ? 13.561 -11.658 -8.274  0.48 22.88 ?  138 HIS   A HB2  1 
ATOM   3296 H HB3  A HIS   A 1 138 ? 14.104 -10.134 -7.301  0.52 18.25 ?  138 HIS   A HB3  1 
ATOM   3297 H HB3  B HIS   A 1 138 ? 14.461 -10.548 -7.582  0.48 22.88 ?  138 HIS   A HB3  1 
ATOM   3298 H HD1  A HIS   A 1 138 ? 14.704 -13.668 -7.893  0.52 20.83 ?  138 HIS   A HD1  1 
ATOM   3299 H HD1  B HIS   A 1 138 ? 14.841 -14.137 -8.002  0.48 24.90 ?  138 HIS   A HD1  1 
ATOM   3300 H HD2  A HIS   A 1 138 ? 16.693 -10.321 -7.976  0.52 19.65 ?  138 HIS   A HD2  1 
ATOM   3301 H HD2  B HIS   A 1 138 ? 17.016 -10.924 -8.312  0.48 24.65 ?  138 HIS   A HD2  1 
ATOM   3302 H HE1  A HIS   A 1 138 ? 16.883 -14.223 -8.617  0.52 21.15 ?  138 HIS   A HE1  1 
ATOM   3303 H HE1  B HIS   A 1 138 ? 16.988 -14.866 -8.652  0.48 25.62 ?  138 HIS   A HE1  1 
ATOM   3304 N N    A SER   A 1 139 ? 14.909 -10.121 -4.408  0.52 13.54 ?  139 SER   A N    1 
ATOM   3305 N N    B SER   A 1 139 ? 14.981 -10.537 -4.671  0.48 15.00 ?  139 SER   A N    1 
ATOM   3306 C CA   A SER   A 1 139 ? 15.958 -9.904  -3.416  0.52 13.69 ?  139 SER   A CA   1 
ATOM   3307 C CA   B SER   A 1 139 ? 16.055 -10.304 -3.710  0.48 14.17 ?  139 SER   A CA   1 
ATOM   3308 C C    A SER   A 1 139 ? 15.738 -10.774 -2.182  0.52 13.47 ?  139 SER   A C    1 
ATOM   3309 C C    B SER   A 1 139 ? 15.814 -11.068 -2.412  0.48 14.54 ?  139 SER   A C    1 
ATOM   3310 O O    A SER   A 1 139 ? 16.699 -11.310 -1.610  0.52 13.19 ?  139 SER   A O    1 
ATOM   3311 O O    B SER   A 1 139 ? 16.729 -11.704 -1.874  0.48 14.23 ?  139 SER   A O    1 
ATOM   3312 C CB   A SER   A 1 139 ? 16.041 -8.418  -3.050  0.52 13.48 ?  139 SER   A CB   1 
ATOM   3313 C CB   B SER   A 1 139 ? 16.199 -8.806  -3.431  0.48 13.43 ?  139 SER   A CB   1 
ATOM   3314 O OG   A SER   A 1 139 ? 17.087 -8.175  -2.125  0.52 14.20 ?  139 SER   A OG   1 
ATOM   3315 O OG   B SER   A 1 139 ? 17.253 -8.588  -2.513  0.48 12.35 ?  139 SER   A OG   1 
ATOM   3316 H H    A SER   A 1 139 ? 14.486 -9.411  -4.639  0.52 16.25 ?  139 SER   A H    1 
ATOM   3317 H H    B SER   A 1 139 ? 14.523 -9.837  -4.872  0.48 18.00 ?  139 SER   A H    1 
ATOM   3318 H HA   A SER   A 1 139 ? 16.812 -10.158 -3.795  0.52 16.42 ?  139 SER   A HA   1 
ATOM   3319 H HA   B SER   A 1 139 ? 16.894 -10.613 -4.092  0.48 17.01 ?  139 SER   A HA   1 
ATOM   3320 H HB2  A SER   A 1 139 ? 16.221 -7.901  -3.853  0.52 16.17 ?  139 SER   A HB2  1 
ATOM   3321 H HB2  B SER   A 1 139 ? 16.407 -8.340  -4.257  0.48 16.11 ?  139 SER   A HB2  1 
ATOM   3322 H HB3  A SER   A 1 139 ? 15.208 -8.134  -2.652  0.52 16.17 ?  139 SER   A HB3  1 
ATOM   3323 H HB3  B SER   A 1 139 ? 15.379 -8.467  -3.050  0.48 16.11 ?  139 SER   A HB3  1 
ATOM   3324 H HG   A SER   A 1 139 ? 17.132 -7.349  -1.927  0.52 17.04 ?  139 SER   A HG   1 
ATOM   3325 H HG   B SER   A 1 139 ? 17.346 -7.768  -2.349  0.48 14.82 ?  139 SER   A HG   1 
ATOM   3326 N N    A LEU   A 1 140 ? 14.479 -10.954 -1.773  0.52 14.00 ?  140 LEU   A N    1 
ATOM   3327 N N    B LEU   A 1 140 ? 14.590 -11.000 -1.881  0.48 14.97 ?  140 LEU   A N    1 
ATOM   3328 C CA   A LEU   A 1 140 ? 14.210 -11.784 -0.603  0.52 13.98 ?  140 LEU   A CA   1 
ATOM   3329 C CA   B LEU   A 1 140 ? 14.278 -11.757 -0.671  0.48 14.70 ?  140 LEU   A CA   1 
ATOM   3330 C C    A LEU   A 1 140 ? 14.521 -13.253 -0.880  0.52 14.52 ?  140 LEU   A C    1 
ATOM   3331 C C    B LEU   A 1 140 ? 14.521 -13.245 -0.888  0.48 14.89 ?  140 LEU   A C    1 
ATOM   3332 O O    A LEU   A 1 140 ? 15.094 -13.943 -0.027  0.52 14.91 ?  140 LEU   A O    1 
ATOM   3333 O O    B LEU   A 1 140 ? 15.036 -13.938 -0.002  0.48 15.32 ?  140 LEU   A O    1 
ATOM   3334 C CB   A LEU   A 1 140 ? 12.760 -11.601 -0.154  0.52 14.54 ?  140 LEU   A CB   1 
ATOM   3335 C CB   B LEU   A 1 140 ? 12.831 -11.500 -0.245  0.48 15.09 ?  140 LEU   A CB   1 
ATOM   3336 C CG   A LEU   A 1 140 ? 12.337 -12.413 1.073   0.52 15.39 ?  140 LEU   A CG   1 
ATOM   3337 C CG   B LEU   A 1 140 ? 12.332 -12.325 0.950   0.48 15.59 ?  140 LEU   A CG   1 
ATOM   3338 C CD1  A LEU   A 1 140 ? 13.270 -12.190 2.260   0.52 15.91 ?  140 LEU   A CD1  1 
ATOM   3339 C CD1  B LEU   A 1 140 ? 13.169 -12.075 2.203   0.48 15.72 ?  140 LEU   A CD1  1 
ATOM   3340 C CD2  A LEU   A 1 140 ? 10.888 -12.092 1.446   0.52 15.99 ?  140 LEU   A CD2  1 
ATOM   3341 C CD2  B LEU   A 1 140 ? 10.847 -12.065 1.221   0.48 16.36 ?  140 LEU   A CD2  1 
ATOM   3342 H H    A LEU   A 1 140 ? 13.781 -10.615 -2.150  0.52 16.80 ?  140 LEU   A H    1 
ATOM   3343 H H    B LEU   A 1 140 ? 13.943 -10.532 -2.196  0.48 17.97 ?  140 LEU   A H    1 
ATOM   3344 H HA   A LEU   A 1 140 ? 14.784 -11.490 0.122   0.52 16.78 ?  140 LEU   A HA   1 
ATOM   3345 H HA   B LEU   A 1 140 ? 14.857 -11.460 0.046   0.48 17.64 ?  140 LEU   A HA   1 
ATOM   3346 H HB2  A LEU   A 1 140 ? 12.620 -10.664 0.055   0.52 17.44 ?  140 LEU   A HB2  1 
ATOM   3347 H HB2  B LEU   A 1 140 ? 12.742 -10.565 -0.007  0.48 18.11 ?  140 LEU   A HB2  1 
ATOM   3348 H HB3  A LEU   A 1 140 ? 12.180 -11.858 -0.888  0.52 17.44 ?  140 LEU   A HB3  1 
ATOM   3349 H HB3  B LEU   A 1 140 ? 12.250 -11.699 -0.996  0.48 18.11 ?  140 LEU   A HB3  1 
ATOM   3350 H HG   A LEU   A 1 140 ? 12.374 -13.354 0.843   0.52 18.47 ?  140 LEU   A HG   1 
ATOM   3351 H HG   B LEU   A 1 140 ? 12.416 -13.266 0.731   0.48 18.70 ?  140 LEU   A HG   1 
ATOM   3352 H HD11 A LEU   A 1 140 ? 12.892 -12.628 3.039   0.52 19.09 ?  140 LEU   A HD11 1 
ATOM   3353 H HD11 B LEU   A 1 140 ? 12.782 -12.568 2.945   0.48 18.86 ?  140 LEU   A HD11 1 
ATOM   3354 H HD12 A LEU   A 1 140 ? 14.138 -12.572 2.055   0.52 19.09 ?  140 LEU   A HD12 1 
ATOM   3355 H HD12 B LEU   A 1 140 ? 14.076 -12.383 2.043   0.48 18.86 ?  140 LEU   A HD12 1 
ATOM   3356 H HD13 A LEU   A 1 140 ? 13.353 -11.239 2.422   0.52 19.09 ?  140 LEU   A HD13 1 
ATOM   3357 H HD13 B LEU   A 1 140 ? 13.170 -11.127 2.400   0.48 18.86 ?  140 LEU   A HD13 1 
ATOM   3358 H HD21 A LEU   A 1 140 ? 10.639 -12.619 2.223   0.52 19.19 ?  140 LEU   A HD21 1 
ATOM   3359 H HD21 B LEU   A 1 140 ? 10.566 -12.605 1.980   0.48 19.63 ?  140 LEU   A HD21 1 
ATOM   3360 H HD22 A LEU   A 1 140 ? 10.814 -11.147 1.649   0.52 19.19 ?  140 LEU   A HD22 1 
ATOM   3361 H HD22 B LEU   A 1 140 ? 10.719 -11.127 1.419   0.48 19.63 ?  140 LEU   A HD22 1 
ATOM   3362 H HD23 A LEU   A 1 140 ? 10.310 -12.316 0.698   0.52 19.19 ?  140 LEU   A HD23 1 
ATOM   3363 H HD23 B LEU   A 1 140 ? 10.333 -12.314 0.435   0.48 19.63 ?  140 LEU   A HD23 1 
ATOM   3364 N N    . ARG   A 1 141 ? 14.150 -13.751 -2.065  1.00 15.54 ?  141 ARG   A N    1 
ATOM   3365 C CA   . ARG   A 1 141 ? 14.407 -15.148 -2.403  1.00 16.64 ?  141 ARG   A CA   1 
ATOM   3366 C C    . ARG   A 1 141 ? 15.902 -15.446 -2.394  1.00 15.91 ?  141 ARG   A C    1 
ATOM   3367 O O    . ARG   A 1 141 ? 16.344 -16.455 -1.829  1.00 16.75 ?  141 ARG   A O    1 
ATOM   3368 C CB   . ARG   A 1 141 ? 13.812 -15.430 -3.784  1.00 18.95 ?  141 ARG   A CB   1 
ATOM   3369 C CG   . ARG   A 1 141 ? 13.850 -16.883 -4.221  1.00 22.14 ?  141 ARG   A CG   1 
ATOM   3370 C CD   . ARG   A 1 141 ? 12.809 -17.679 -3.494  1.00 25.20 ?  141 ARG   A CD   1 
ATOM   3371 N NE   . ARG   A 1 141 ? 13.384 -18.452 -2.404  1.00 26.52 ?  141 ARG   A NE   1 
ATOM   3372 C CZ   . ARG   A 1 141 ? 12.674 -18.975 -1.412  1.00 27.25 ?  141 ARG   A CZ   1 
ATOM   3373 N NH1  . ARG   A 1 141 ? 11.386 -18.708 -1.266  1.00 26.87 ?  141 ARG   A NH1  1 
ATOM   3374 N NH2  . ARG   A 1 141 ? 13.273 -19.777 -0.537  1.00 28.09 ?  141 ARG   A NH2  1 
ATOM   3375 H H    A ARG   A 1 141 ? 13.755 -13.302 -2.685  0.52 18.65 ?  141 ARG   A H    1 
ATOM   3376 H H    B ARG   A 1 141 ? 13.751 -13.306 -2.685  0.48 18.65 ?  141 ARG   A H    1 
ATOM   3377 H HA   . ARG   A 1 141 ? 13.972 -15.726 -1.758  1.00 19.97 ?  141 ARG   A HA   1 
ATOM   3378 H HB2  . ARG   A 1 141 ? 12.885 -15.148 -3.790  1.00 22.74 ?  141 ARG   A HB2  1 
ATOM   3379 H HB3  . ARG   A 1 141 ? 14.308 -14.923 -4.443  1.00 22.74 ?  141 ARG   A HB3  1 
ATOM   3380 H HG2  . ARG   A 1 141 ? 13.673 -16.944 -5.174  1.00 26.56 ?  141 ARG   A HG2  1 
ATOM   3381 H HG3  . ARG   A 1 141 ? 14.722 -17.267 -4.020  1.00 26.56 ?  141 ARG   A HG3  1 
ATOM   3382 H HD2  . ARG   A 1 141 ? 12.151 -17.073 -3.113  1.00 30.24 ?  141 ARG   A HD2  1 
ATOM   3383 H HD3  . ARG   A 1 141 ? 12.375 -18.287 -4.115  1.00 30.24 ?  141 ARG   A HD3  1 
ATOM   3384 H HE   . ARG   A 1 141 ? 14.209 -18.682 -2.468  1.00 31.83 ?  141 ARG   A HE   1 
ATOM   3385 H HH11 . ARG   A 1 141 ? 10.981 -18.201 -1.830  1.00 32.25 ?  141 ARG   A HH11 1 
ATOM   3386 H HH12 . ARG   A 1 141 ? 10.947 -19.052 -0.610  1.00 32.25 ?  141 ARG   A HH12 1 
ATOM   3387 H HH21 . ARG   A 1 141 ? 14.111 -19.953 -0.619  1.00 33.71 ?  141 ARG   A HH21 1 
ATOM   3388 H HH22 . ARG   A 1 141 ? 12.828 -20.108 0.120   1.00 33.71 ?  141 ARG   A HH22 1 
ATOM   3389 N N    . VAL   A 1 142 ? 16.697 -14.583 -3.029  1.00 14.84 ?  142 VAL   A N    1 
ATOM   3390 C CA   . VAL   A 1 142 ? 18.146 -14.780 -3.037  1.00 15.00 ?  142 VAL   A CA   1 
ATOM   3391 C C    . VAL   A 1 142 ? 18.701 -14.743 -1.621  1.00 14.42 ?  142 VAL   A C    1 
ATOM   3392 O O    . VAL   A 1 142 ? 19.560 -15.556 -1.253  1.00 15.09 ?  142 VAL   A O    1 
ATOM   3393 C CB   . VAL   A 1 142 ? 18.847 -13.766 -3.961  1.00 15.05 ?  142 VAL   A CB   1 
ATOM   3394 C CG1  . VAL   A 1 142 ? 20.357 -13.967 -3.922  1.00 14.94 ?  142 VAL   A CG1  1 
ATOM   3395 C CG2  . VAL   A 1 142 ? 18.349 -13.902 -5.387  1.00 16.63 ?  142 VAL   A CG2  1 
ATOM   3396 H H    . VAL   A 1 142 ? 16.431 -13.880 -3.453  1.00 17.81 ?  142 VAL   A H    1 
ATOM   3397 H HA   . VAL   A 1 142 ? 18.334 -15.658 -3.392  1.00 18.00 ?  142 VAL   A HA   1 
ATOM   3398 H HB   . VAL   A 1 142 ? 18.665 -12.860 -3.657  1.00 18.06 ?  142 VAL   A HB   1 
ATOM   3399 H HG11 . VAL   A 1 142 ? 20.766 -13.472 -4.653  1.00 17.93 ?  142 VAL   A HG11 1 
ATOM   3400 H HG12 . VAL   A 1 142 ? 20.707 -13.640 -3.075  1.00 17.93 ?  142 VAL   A HG12 1 
ATOM   3401 H HG13 . VAL   A 1 142 ? 20.555 -14.912 -4.018  1.00 17.93 ?  142 VAL   A HG13 1 
ATOM   3402 H HG21 . VAL   A 1 142 ? 18.697 -13.163 -5.915  1.00 19.95 ?  142 VAL   A HG21 1 
ATOM   3403 H HG22 . VAL   A 1 142 ? 18.668 -14.742 -5.751  1.00 19.95 ?  142 VAL   A HG22 1 
ATOM   3404 H HG23 . VAL   A 1 142 ? 17.385 -13.882 -5.388  1.00 19.95 ?  142 VAL   A HG23 1 
ATOM   3405 N N    . CYS   A 1 143 ? 18.217 -13.808 -0.802  1.00 13.49 ?  143 CYS   A N    1 
ATOM   3406 C CA   . CYS   A 1 143 ? 18.678 -13.727 0.580   1.00 13.89 ?  143 CYS   A CA   1 
ATOM   3407 C C    . CYS   A 1 143 ? 18.436 -15.048 1.301   1.00 14.17 ?  143 CYS   A C    1 
ATOM   3408 O O    . CYS   A 1 143 ? 19.342 -15.621 1.914   1.00 14.65 ?  143 CYS   A O    1 
ATOM   3409 C CB   . CYS   A 1 143 ? 17.947 -12.591 1.296   1.00 14.28 ?  143 CYS   A CB   1 
ATOM   3410 S SG   . CYS   A 1 143 ? 18.412 -12.396 3.013   1.00 15.22 ?  143 CYS   A SG   1 
ATOM   3411 H H    . CYS   A 1 143 ? 17.616 -13.229 -1.014  1.00 16.19 ?  143 CYS   A H    1 
ATOM   3412 H HA   . CYS   A 1 143 ? 19.631 -13.540 0.592   1.00 16.67 ?  143 CYS   A HA   1 
ATOM   3413 H HB2  . CYS   A 1 143 ? 18.134 -11.759 0.838   1.00 17.13 ?  143 CYS   A HB2  1 
ATOM   3414 H HB3  . CYS   A 1 143 ? 16.994 -12.771 1.266   1.00 17.13 ?  143 CYS   A HB3  1 
ATOM   3415 H HG   . CYS   A 1 143 ? 17.825 -11.451 3.470   1.00 18.27 ?  143 CYS   A HG   1 
ATOM   3416 N N    . VAL   A 1 144 ? 17.207 -15.559 1.222   1.00 14.75 ?  144 VAL   A N    1 
ATOM   3417 C CA   . VAL   A 1 144 ? 16.841 -16.783 1.927   1.00 16.69 ?  144 VAL   A CA   1 
ATOM   3418 C C    . VAL   A 1 144 ? 17.668 -17.961 1.441   1.00 16.49 ?  144 VAL   A C    1 
ATOM   3419 O O    . VAL   A 1 144 ? 18.035 -18.842 2.230   1.00 17.52 ?  144 VAL   A O    1 
ATOM   3420 C CB   . VAL   A 1 144 ? 15.328 -17.026 1.767   1.00 18.87 ?  144 VAL   A CB   1 
ATOM   3421 C CG1  . VAL   A 1 144 ? 14.953 -18.471 2.069   1.00 21.00 ?  144 VAL   A CG1  1 
ATOM   3422 C CG2  . VAL   A 1 144 ? 14.569 -16.034 2.645   1.00 18.76 ?  144 VAL   A CG2  1 
ATOM   3423 H H    . VAL   A 1 144 ? 16.566 -15.205 0.766   1.00 17.70 ?  144 VAL   A H    1 
ATOM   3424 H HA   . VAL   A 1 144 ? 17.020 -16.666 2.867   1.00 20.03 ?  144 VAL   A HA   1 
ATOM   3425 H HB   . VAL   A 1 144 ? 15.076 -16.842 0.844   1.00 22.64 ?  144 VAL   A HB   1 
ATOM   3426 H HG11 . VAL   A 1 144 ? 13.994 -18.522 2.218   1.00 25.20 ?  144 VAL   A HG11 1 
ATOM   3427 H HG12 . VAL   A 1 144 ? 15.197 -19.027 1.313   1.00 25.20 ?  144 VAL   A HG12 1 
ATOM   3428 H HG13 . VAL   A 1 144 ? 15.425 -18.758 2.864   1.00 25.20 ?  144 VAL   A HG13 1 
ATOM   3429 H HG21 . VAL   A 1 144 ? 13.617 -16.194 2.560   1.00 22.51 ?  144 VAL   A HG21 1 
ATOM   3430 H HG22 . VAL   A 1 144 ? 14.842 -16.154 3.568   1.00 22.51 ?  144 VAL   A HG22 1 
ATOM   3431 H HG23 . VAL   A 1 144 ? 14.777 -15.128 2.357   1.00 22.51 ?  144 VAL   A HG23 1 
ATOM   3432 N N    . ASP   A 1 145 ? 17.958 -18.010 0.140   1.00 17.48 ?  145 ASP   A N    1 
ATOM   3433 C CA   . ASP   A 1 145 ? 18.687 -19.123 -0.461  1.00 18.12 ?  145 ASP   A CA   1 
ATOM   3434 C C    . ASP   A 1 145 ? 20.205 -18.970 -0.396  1.00 17.30 ?  145 ASP   A C    1 
ATOM   3435 O O    . ASP   A 1 145 ? 20.916 -19.874 -0.840  1.00 19.76 ?  145 ASP   A O    1 
ATOM   3436 C CB   . ASP   A 1 145 ? 18.266 -19.303 -1.923  1.00 19.96 ?  145 ASP   A CB   1 
ATOM   3437 C CG   . ASP   A 1 145 ? 16.815 -19.745 -2.071  1.00 22.14 ?  145 ASP   A CG   1 
ATOM   3438 O OD1  . ASP   A 1 145 ? 16.212 -20.235 -1.091  1.00 23.08 ?  145 ASP   A OD1  1 
ATOM   3439 O OD2  . ASP   A 1 145 ? 16.273 -19.596 -3.183  1.00 23.56 -1 145 ASP   A OD2  1 
ATOM   3440 H H    . ASP   A 1 145 ? 17.731 -17.402 -0.429  1.00 20.98 ?  145 ASP   A H    1 
ATOM   3441 H HA   . ASP   A 1 145 ? 18.452 -19.935 0.011   1.00 21.75 ?  145 ASP   A HA   1 
ATOM   3442 H HB2  . ASP   A 1 145 ? 18.376 -18.456 -2.389  1.00 23.95 ?  145 ASP   A HB2  1 
ATOM   3443 H HB3  . ASP   A 1 145 ? 18.834 -19.977 -2.333  1.00 23.95 ?  145 ASP   A HB3  1 
ATOM   3444 N N    . THR   A 1 146 ? 20.720 -17.870 0.141   1.00 14.88 ?  146 THR   A N    1 
ATOM   3445 C CA   . THR   A 1 146 ? 22.157 -17.612 0.170   1.00 14.73 ?  146 THR   A CA   1 
ATOM   3446 C C    . THR   A 1 146 ? 22.711 -17.413 1.571   1.00 14.67 ?  146 THR   A C    1 
ATOM   3447 O O    . THR   A 1 146 ? 23.776 -17.959 1.897   1.00 15.68 ?  146 THR   A O    1 
ATOM   3448 C CB   . THR   A 1 146 ? 22.472 -16.366 -0.679  1.00 14.23 ?  146 THR   A CB   1 
ATOM   3449 O OG1  . THR   A 1 146 ? 21.975 -16.547 -2.006  1.00 14.84 ?  146 THR   A OG1  1 
ATOM   3450 C CG2  . THR   A 1 146 ? 23.973 -16.109 -0.743  1.00 15.24 ?  146 THR   A CG2  1 
ATOM   3451 H H    . THR   A 1 146 ? 20.251 -17.248 0.507   1.00 17.85 ?  146 THR   A H    1 
ATOM   3452 H HA   . THR   A 1 146 ? 22.624 -18.355 -0.228  1.00 17.67 ?  146 THR   A HA   1 
ATOM   3453 H HB   . THR   A 1 146 ? 22.049 -15.583 -0.289  1.00 17.07 ?  146 THR   A HB   1 
ATOM   3454 H HG1  . THR   A 1 146 ? 21.144 -16.646 -1.995  1.00 17.81 ?  146 THR   A HG1  1 
ATOM   3455 H HG21 . THR   A 1 146 ? 24.169 -15.455 -1.435  1.00 18.29 ?  146 THR   A HG21 1 
ATOM   3456 H HG22 . THR   A 1 146 ? 24.287 -15.764 0.108   1.00 18.29 ?  146 THR   A HG22 1 
ATOM   3457 H HG23 . THR   A 1 146 ? 24.440 -16.931 -0.946  1.00 18.29 ?  146 THR   A HG23 1 
ATOM   3458 N N    . VAL   A 1 147 ? 22.022 -16.644 2.404   1.00 13.52 ?  147 VAL   A N    1 
ATOM   3459 C CA   . VAL   A 1 147 ? 22.495 -16.328 3.745   1.00 13.75 ?  147 VAL   A CA   1 
ATOM   3460 C C    . VAL   A 1 147 ? 22.172 -17.494 4.671   1.00 14.75 ?  147 VAL   A C    1 
ATOM   3461 O O    . VAL   A 1 147 ? 21.031 -17.978 4.712   1.00 15.01 ?  147 VAL   A O    1 
ATOM   3462 C CB   . VAL   A 1 147 ? 21.853 -15.021 4.246   1.00 13.91 ?  147 VAL   A CB   1 
ATOM   3463 C CG1  . VAL   A 1 147 ? 22.353 -14.700 5.633   1.00 15.10 ?  147 VAL   A CG1  1 
ATOM   3464 C CG2  . VAL   A 1 147 ? 22.114 -13.862 3.276   1.00 14.55 ?  147 VAL   A CG2  1 
ATOM   3465 H H    . VAL   A 1 147 ? 21.263 -16.286 2.215   1.00 16.22 ?  147 VAL   A H    1 
ATOM   3466 H HA   . VAL   A 1 147 ? 23.459 -16.210 3.725   1.00 16.50 ?  147 VAL   A HA   1 
ATOM   3467 H HB   . VAL   A 1 147 ? 20.897 -15.155 4.303   1.00 16.69 ?  147 VAL   A HB   1 
ATOM   3468 H HG11 . VAL   A 1 147 ? 22.091 -13.795 5.857   1.00 18.12 ?  147 VAL   A HG11 1 
ATOM   3469 H HG12 . VAL   A 1 147 ? 21.948 -15.323 6.266   1.00 18.12 ?  147 VAL   A HG12 1 
ATOM   3470 H HG13 . VAL   A 1 147 ? 23.314 -14.787 5.654   1.00 18.12 ?  147 VAL   A HG13 1 
ATOM   3471 H HG21 . VAL   A 1 147 ? 21.747 -13.048 3.655   1.00 17.47 ?  147 VAL   A HG21 1 
ATOM   3472 H HG22 . VAL   A 1 147 ? 23.066 -13.768 3.140   1.00 17.47 ?  147 VAL   A HG22 1 
ATOM   3473 H HG23 . VAL   A 1 147 ? 21.674 -14.057 2.431   1.00 17.47 ?  147 VAL   A HG23 1 
ATOM   3474 N N    . ARG   A 1 148 ? 23.187 -17.954 5.405   1.00 14.87 ?  148 ARG   A N    1 
ATOM   3475 C CA   . ARG   A 1 148 ? 23.050 -19.029 6.373   1.00 14.98 ?  148 ARG   A CA   1 
ATOM   3476 C C    . ARG   A 1 148 ? 23.164 -18.558 7.812   1.00 15.42 ?  148 ARG   A C    1 
ATOM   3477 O O    . ARG   A 1 148 ? 22.746 -19.279 8.725   1.00 16.85 ?  148 ARG   A O    1 
ATOM   3478 C CB   . ARG   A 1 148 ? 24.098 -20.120 6.112   1.00 15.83 ?  148 ARG   A CB   1 
ATOM   3479 C CG   . ARG   A 1 148 ? 23.950 -20.778 4.753   1.00 17.60 ?  148 ARG   A CG   1 
ATOM   3480 C CD   . ARG   A 1 148 ? 25.056 -21.808 4.491   1.00 18.32 ?  148 ARG   A CD   1 
ATOM   3481 N NE   . ARG   A 1 148 ? 26.392 -21.216 4.503   1.00 18.38 ?  148 ARG   A NE   1 
ATOM   3482 C CZ   . ARG   A 1 148 ? 26.904 -20.503 3.509   1.00 17.02 ?  148 ARG   A CZ   1 
ATOM   3483 N NH1  . ARG   A 1 148 ? 26.227 -20.285 2.393   1.00 17.45 ?  148 ARG   A NH1  1 
ATOM   3484 N NH2  . ARG   A 1 148 ? 28.119 -19.972 3.647   1.00 17.05 ?  148 ARG   A NH2  1 
ATOM   3485 H H    . ARG   A 1 148 ? 23.991 -17.643 5.351   1.00 17.85 ?  148 ARG   A H    1 
ATOM   3486 H HA   . ARG   A 1 148 ? 22.176 -19.435 6.264   1.00 17.98 ?  148 ARG   A HA   1 
ATOM   3487 H HB2  . ARG   A 1 148 ? 24.985 -19.731 6.154   1.00 19.00 ?  148 ARG   A HB2  1 
ATOM   3488 H HB3  . ARG   A 1 148 ? 24.010 -20.816 6.785   1.00 19.00 ?  148 ARG   A HB3  1 
ATOM   3489 H HG2  . ARG   A 1 148 ? 23.094 -21.236 4.714   1.00 21.12 ?  148 ARG   A HG2  1 
ATOM   3490 H HG3  . ARG   A 1 148 ? 23.996 -20.097 4.065   1.00 21.12 ?  148 ARG   A HG3  1 
ATOM   3491 H HD2  . ARG   A 1 148 ? 25.024 -22.487 5.180   1.00 21.99 ?  148 ARG   A HD2  1 
ATOM   3492 H HD3  . ARG   A 1 148 ? 24.912 -22.209 3.620   1.00 21.99 ?  148 ARG   A HD3  1 
ATOM   3493 H HE   . ARG   A 1 148 ? 26.878 -21.336 5.199   1.00 22.05 ?  148 ARG   A HE   1 
ATOM   3494 H HH11 . ARG   A 1 148 ? 25.439 -20.602 2.296   1.00 20.94 ?  148 ARG   A HH11 1 
ATOM   3495 H HH12 . ARG   A 1 148 ? 26.578 -19.803 1.766   1.00 20.94 ?  148 ARG   A HH12 1 
ATOM   3496 H HH21 . ARG   A 1 148 ? 28.569 -20.104 4.368   1.00 20.45 ?  148 ARG   A HH21 1 
ATOM   3497 H HH22 . ARG   A 1 148 ? 28.464 -19.501 3.011   1.00 20.45 ?  148 ARG   A HH22 1 
ATOM   3498 N N    . THR   A 1 149 ? 23.706 -17.367 8.026   1.00 15.45 ?  149 THR   A N    1 
ATOM   3499 C CA   . THR   A 1 149 ? 23.776 -16.759 9.341   1.00 15.49 ?  149 THR   A CA   1 
ATOM   3500 C C    . THR   A 1 149 ? 22.445 -16.067 9.637   1.00 15.22 ?  149 THR   A C    1 
ATOM   3501 O O    . THR   A 1 149 ? 21.518 -16.063 8.817   1.00 15.49 ?  149 THR   A O    1 
ATOM   3502 C CB   . THR   A 1 149 ? 24.976 -15.822 9.391   1.00 16.06 ?  149 THR   A CB   1 
ATOM   3503 O OG1  . THR   A 1 149 ? 24.858 -14.906 8.303   1.00 15.58 ?  149 THR   A OG1  1 
ATOM   3504 C CG2  . THR   A 1 149 ? 26.288 -16.633 9.274   1.00 16.24 ?  149 THR   A CG2  1 
ATOM   3505 H H    . THR   A 1 149 ? 24.055 -16.875 7.404   1.00 18.54 ?  149 THR   A H    1 
ATOM   3506 H HA   . THR   A 1 149 ? 23.903 -17.464 9.998   1.00 18.58 ?  149 THR   A HA   1 
ATOM   3507 H HB   . THR   A 1 149 ? 24.973 -15.347 10.234  1.00 19.27 ?  149 THR   A HB   1 
ATOM   3508 H HG1  . THR   A 1 149 ? 25.514 -14.375 8.308   1.00 18.70 ?  149 THR   A HG1  1 
ATOM   3509 H HG21 . THR   A 1 149 ? 27.050 -16.038 9.332   1.00 19.48 ?  149 THR   A HG21 1 
ATOM   3510 H HG22 . THR   A 1 149 ? 26.345 -17.289 9.989   1.00 19.48 ?  149 THR   A HG22 1 
ATOM   3511 H HG23 . THR   A 1 149 ? 26.318 -17.101 8.422   1.00 19.48 ?  149 THR   A HG23 1 
ATOM   3512 N N    . ASN   A 1 150 ? 22.309 -15.538 10.845  1.00 15.41 ?  150 ASN   A N    1 
ATOM   3513 C CA   . ASN   A 1 150 ? 21.020 -15.016 11.302  1.00 15.60 ?  150 ASN   A CA   1 
ATOM   3514 C C    . ASN   A 1 150 ? 20.853 -13.575 10.832  1.00 14.73 ?  150 ASN   A C    1 
ATOM   3515 O O    . ASN   A 1 150 ? 21.598 -12.681 11.252  1.00 15.78 ?  150 ASN   A O    1 
ATOM   3516 C CB   . ASN   A 1 150 ? 20.920 -15.129 12.818  1.00 18.78 ?  150 ASN   A CB   1 
ATOM   3517 C CG   . ASN   A 1 150 ? 20.857 -16.561 13.283  1.00 23.26 ?  150 ASN   A CG   1 
ATOM   3518 O OD1  . ASN   A 1 150 ? 20.296 -17.414 12.598  1.00 24.61 ?  150 ASN   A OD1  1 
ATOM   3519 N ND2  . ASN   A 1 150 ? 21.444 -16.840 14.448  1.00 26.44 ?  150 ASN   A ND2  1 
ATOM   3520 H H    . ASN   A 1 150 ? 22.943 -15.482 11.425  1.00 18.49 ?  150 ASN   A H    1 
ATOM   3521 H HA   . ASN   A 1 150 ? 20.305 -15.555 10.914  1.00 18.72 ?  150 ASN   A HA   1 
ATOM   3522 H HB2  . ASN   A 1 150 ? 21.696 -14.717 13.220  1.00 22.53 ?  150 ASN   A HB2  1 
ATOM   3523 H HB3  . ASN   A 1 150 ? 20.110 -14.684 13.116  1.00 22.53 ?  150 ASN   A HB3  1 
ATOM   3524 H HD21 . ASN   A 1 150 ? 21.438 -17.643 14.766  1.00 31.73 ?  150 ASN   A HD21 1 
ATOM   3525 H HD22 . ASN   A 1 150 ? 21.830 -16.212 14.897  1.00 31.73 ?  150 ASN   A HD22 1 
ATOM   3526 N N    . VAL   A 1 151 ? 19.879 -13.348 9.960   1.00 14.11 ?  151 VAL   A N    1 
ATOM   3527 C CA   . VAL   A 1 151 ? 19.669 -12.049 9.347   1.00 13.96 ?  151 VAL   A CA   1 
ATOM   3528 C C    . VAL   A 1 151 ? 18.281 -11.527 9.694   1.00 14.39 ?  151 VAL   A C    1 
ATOM   3529 O O    . VAL   A 1 151 ? 17.272 -12.235 9.542   1.00 16.35 ?  151 VAL   A O    1 
ATOM   3530 C CB   . VAL   A 1 151 ? 19.955 -12.071 7.832   1.00 15.82 ?  151 VAL   A CB   1 
ATOM   3531 C CG1  . VAL   A 1 151 ? 19.096 -13.069 7.103   1.00 17.15 ?  151 VAL   A CG1  1 
ATOM   3532 C CG2  . VAL   A 1 151 ? 19.818 -10.659 7.240   1.00 15.79 ?  151 VAL   A CG2  1 
ATOM   3533 H H    . VAL   A 1 151 ? 19.315 -13.951 9.704   1.00 16.94 ?  151 VAL   A H    1 
ATOM   3534 H HA   . VAL   A 1 151 ? 20.311 -11.434 9.742   1.00 16.75 ?  151 VAL   A HA   1 
ATOM   3535 H HB   . VAL   A 1 151 ? 20.877 -12.341 7.705   1.00 18.99 ?  151 VAL   A HB   1 
ATOM   3536 H HG11 . VAL   A 1 151 ? 19.306 -13.046 6.157   1.00 20.58 ?  151 VAL   A HG11 1 
ATOM   3537 H HG12 . VAL   A 1 151 ? 19.276 -13.961 7.456   1.00 20.58 ?  151 VAL   A HG12 1 
ATOM   3538 H HG13 . VAL   A 1 151 ? 18.159 -12.852 7.239   1.00 20.58 ?  151 VAL   A HG13 1 
ATOM   3539 H HG21 . VAL   A 1 151 ? 20.112 -10.676 6.311   1.00 18.95 ?  151 VAL   A HG21 1 
ATOM   3540 H HG22 . VAL   A 1 151 ? 18.896 -10.374 7.287   1.00 18.95 ?  151 VAL   A HG22 1 
ATOM   3541 H HG23 . VAL   A 1 151 ? 20.382 -10.044 7.743   1.00 18.95 ?  151 VAL   A HG23 1 
ATOM   3542 N N    A TYR   A 1 152 ? 18.247 -10.280 10.158  0.52 14.25 ?  152 TYR   A N    1 
ATOM   3543 N N    B TYR   A 1 152 ? 18.250 -10.294 10.189  0.48 14.08 ?  152 TYR   A N    1 
ATOM   3544 C CA   A TYR   A 1 152 ? 17.035 -9.563  10.532  0.52 13.82 ?  152 TYR   A CA   1 
ATOM   3545 C CA   B TYR   A 1 152 ? 17.035 -9.568  10.530  0.48 13.70 ?  152 TYR   A CA   1 
ATOM   3546 C C    A TYR   A 1 152 ? 16.822 -8.450  9.518   0.52 13.58 ?  152 TYR   A C    1 
ATOM   3547 C C    B TYR   A 1 152 ? 16.859 -8.483  9.479   0.48 13.21 ?  152 TYR   A C    1 
ATOM   3548 O O    A TYR   A 1 152 ? 17.545 -7.448  9.526   0.52 14.09 ?  152 TYR   A O    1 
ATOM   3549 O O    B TYR   A 1 152 ? 17.655 -7.539  9.412   0.48 12.86 ?  152 TYR   A O    1 
ATOM   3550 C CB   A TYR   A 1 152 ? 17.170 -9.030  11.954  0.52 14.65 ?  152 TYR   A CB   1 
ATOM   3551 C CB   B TYR   A 1 152 ? 17.154 -8.987  11.935  0.48 14.59 ?  152 TYR   A CB   1 
ATOM   3552 C CG   A TYR   A 1 152 ? 17.169 -10.155 12.957  0.52 15.61 ?  152 TYR   A CG   1 
ATOM   3553 C CG   B TYR   A 1 152 ? 17.066 -10.054 12.999  0.48 15.80 ?  152 TYR   A CG   1 
ATOM   3554 C CD1  A TYR   A 1 152 ? 18.337 -10.833 13.282  0.52 16.64 ?  152 TYR   A CD1  1 
ATOM   3555 C CD1  B TYR   A 1 152 ? 18.144 -10.890 13.267  0.48 17.18 ?  152 TYR   A CD1  1 
ATOM   3556 C CD2  A TYR   A 1 152 ? 15.987 -10.571 13.551  0.52 16.13 ?  152 TYR   A CD2  1 
ATOM   3557 C CD2  B TYR   A 1 152 ? 15.896 -10.243 13.723  0.48 15.79 ?  152 TYR   A CD2  1 
ATOM   3558 C CE1  A TYR   A 1 152 ? 18.331 -11.885 14.184  0.52 17.68 ?  152 TYR   A CE1  1 
ATOM   3559 C CE1  B TYR   A 1 152 ? 18.061 -11.882 14.230  0.48 18.39 ?  152 TYR   A CE1  1 
ATOM   3560 C CE2  A TYR   A 1 152 ? 15.967 -11.626 14.455  0.52 17.13 ?  152 TYR   A CE2  1 
ATOM   3561 C CE2  B TYR   A 1 152 ? 15.802 -11.234 14.692  0.48 17.18 ?  152 TYR   A CE2  1 
ATOM   3562 C CZ   A TYR   A 1 152 ? 17.142 -12.278 14.768  0.52 17.54 ?  152 TYR   A CZ   1 
ATOM   3563 C CZ   B TYR   A 1 152 ? 16.887 -12.049 14.940  0.48 18.65 ?  152 TYR   A CZ   1 
ATOM   3564 O OH   A TYR   A 1 152 ? 17.127 -13.330 15.664  0.52 19.62 ?  152 TYR   A OH   1 
ATOM   3565 O OH   B TYR   A 1 152 ? 16.807 -13.032 15.900  0.48 21.62 ?  152 TYR   A OH   1 
ATOM   3566 H H    A TYR   A 1 152 ? 18.960 -9.800  10.263  0.52 17.09 ?  152 TYR   A H    1 
ATOM   3567 H H    B TYR   A 1 152 ? 18.964 -9.826  10.333  0.48 16.90 ?  152 TYR   A H    1 
ATOM   3568 H HA   A TYR   A 1 152 ? 16.279 -10.168 10.491  0.52 16.58 ?  152 TYR   A HA   1 
ATOM   3569 H HA   B TYR   A 1 152 ? 16.274 -10.170 10.497  0.48 16.44 ?  152 TYR   A HA   1 
ATOM   3570 H HB2  A TYR   A 1 152 ? 18.007 -8.553  12.035  0.52 17.58 ?  152 TYR   A HB2  1 
ATOM   3571 H HB2  B TYR   A 1 152 ? 18.012 -8.545  12.023  0.48 17.51 ?  152 TYR   A HB2  1 
ATOM   3572 H HB3  A TYR   A 1 152 ? 16.425 -8.445  12.147  0.52 17.58 ?  152 TYR   A HB3  1 
ATOM   3573 H HB3  B TYR   A 1 152 ? 16.434 -8.356  12.079  0.48 17.51 ?  152 TYR   A HB3  1 
ATOM   3574 H HD1  A TYR   A 1 152 ? 19.137 -10.576 12.888  0.52 19.96 ?  152 TYR   A HD1  1 
ATOM   3575 H HD1  B TYR   A 1 152 ? 18.932 -10.781 12.787  0.48 20.62 ?  152 TYR   A HD1  1 
ATOM   3576 H HD2  A TYR   A 1 152 ? 15.187 -10.138 13.338  0.52 19.35 ?  152 TYR   A HD2  1 
ATOM   3577 H HD2  B TYR   A 1 152 ? 15.158 -9.698  13.557  0.48 18.95 ?  152 TYR   A HD2  1 
ATOM   3578 H HE1  A TYR   A 1 152 ? 19.120 -12.326 14.401  0.52 21.21 ?  152 TYR   A HE1  1 
ATOM   3579 H HE1  B TYR   A 1 152 ? 18.794 -12.433 14.399  0.48 22.07 ?  152 TYR   A HE1  1 
ATOM   3580 H HE2  A TYR   A 1 152 ? 15.164 -11.884 14.850  0.52 20.55 ?  152 TYR   A HE2  1 
ATOM   3581 H HE2  B TYR   A 1 152 ? 15.012 -11.351 15.173  0.48 20.62 ?  152 TYR   A HE2  1 
ATOM   3582 H HH   A TYR   A 1 152 ? 16.339 -13.446 15.950  0.52 23.55 ?  152 TYR   A HH   1 
ATOM   3583 H HH   B TYR   A 1 152 ? 16.071 -12.993 16.298  0.48 25.94 ?  152 TYR   A HH   1 
ATOM   3584 N N    . LEU   A 1 153 ? 15.842 -8.641  8.639   1.00 13.89 ?  153 LEU   A N    1 
ATOM   3585 C CA   . LEU   A 1 153 ? 15.593 -7.743  7.522   1.00 13.20 ?  153 LEU   A CA   1 
ATOM   3586 C C    . LEU   A 1 153 ? 14.580 -6.673  7.903   1.00 14.09 ?  153 LEU   A C    1 
ATOM   3587 O O    . LEU   A 1 153 ? 13.477 -6.988  8.368   1.00 15.44 ?  153 LEU   A O    1 
ATOM   3588 C CB   . LEU   A 1 153 ? 15.044 -8.524  6.326   1.00 13.88 ?  153 LEU   A CB   1 
ATOM   3589 C CG   . LEU   A 1 153 ? 15.994 -9.529  5.678   1.00 14.10 ?  153 LEU   A CG   1 
ATOM   3590 C CD1  . LEU   A 1 153 ? 15.229 -10.405 4.698   1.00 14.79 ?  153 LEU   A CD1  1 
ATOM   3591 C CD2  . LEU   A 1 153 ? 17.135 -8.809  4.987   1.00 15.09 ?  153 LEU   A CD2  1 
ATOM   3592 H H    A LEU   A 1 153 ? 15.283 -9.299  8.678   0.52 16.67 ?  153 LEU   A H    1 
ATOM   3593 H H    B LEU   A 1 153 ? 15.262 -9.280  8.698   0.48 16.67 ?  153 LEU   A H    1 
ATOM   3594 H HA   . LEU   A 1 153 ? 16.417 -7.314  7.266   1.00 15.84 ?  153 LEU   A HA   1 
ATOM   3595 H HB2  . LEU   A 1 153 ? 14.258 -9.010  6.618   1.00 16.65 ?  153 LEU   A HB2  1 
ATOM   3596 H HB3  . LEU   A 1 153 ? 14.789 -7.884  5.641   1.00 16.65 ?  153 LEU   A HB3  1 
ATOM   3597 H HG   . LEU   A 1 153 ? 16.368 -10.099 6.372   1.00 16.92 ?  153 LEU   A HG   1 
ATOM   3598 H HD11 . LEU   A 1 153 ? 15.816 -11.096 4.376   1.00 17.74 ?  153 LEU   A HD11 1 
ATOM   3599 H HD12 . LEU   A 1 153 ? 14.466 -10.786 5.152   1.00 17.74 ?  153 LEU   A HD12 1 
ATOM   3600 H HD13 . LEU   A 1 153 ? 14.930 -9.844  3.960   1.00 17.74 ?  153 LEU   A HD13 1 
ATOM   3601 H HD21 . LEU   A 1 153 ? 17.695 -9.463  4.549   1.00 18.11 ?  153 LEU   A HD21 1 
ATOM   3602 H HD22 . LEU   A 1 153 ? 16.765 -8.193  4.338   1.00 18.11 ?  153 LEU   A HD22 1 
ATOM   3603 H HD23 . LEU   A 1 153 ? 17.649 -8.321  5.651   1.00 18.11 ?  153 LEU   A HD23 1 
ATOM   3604 N N    A ALA   A 1 154 ? 14.959 -5.415  7.693   0.52 14.45 ?  154 ALA   A N    1 
ATOM   3605 N N    B ALA   A 1 154 ? 14.948 -5.413  7.693   0.48 14.04 ?  154 ALA   A N    1 
ATOM   3606 C CA   A ALA   A 1 154 ? 14.089 -4.268  7.907   0.52 15.21 ?  154 ALA   A CA   1 
ATOM   3607 C CA   B ALA   A 1 154 ? 14.069 -4.273  7.915   0.48 14.41 ?  154 ALA   A CA   1 
ATOM   3608 C C    A ALA   A 1 154 ? 13.593 -3.772  6.555   0.52 15.39 ?  154 ALA   A C    1 
ATOM   3609 C C    B ALA   A 1 154 ? 13.609 -3.756  6.558   0.48 14.12 ?  154 ALA   A C    1 
ATOM   3610 O O    A ALA   A 1 154 ? 14.398 -3.432  5.681   0.52 16.01 ?  154 ALA   A O    1 
ATOM   3611 O O    B ALA   A 1 154 ? 14.429 -3.290  5.758   0.48 14.67 ?  154 ALA   A O    1 
ATOM   3612 C CB   A ALA   A 1 154 ? 14.840 -3.147  8.626   0.52 15.36 ?  154 ALA   A CB   1 
ATOM   3613 C CB   B ALA   A 1 154 ? 14.802 -3.171  8.684   0.48 14.51 ?  154 ALA   A CB   1 
ATOM   3614 H H    A ALA   A 1 154 ? 15.747 -5.197  7.416   0.52 17.34 ?  154 ALA   A H    1 
ATOM   3615 H H    B ALA   A 1 154 ? 15.730 -5.185  7.408   0.48 16.85 ?  154 ALA   A H    1 
ATOM   3616 H HA   A ALA   A 1 154 ? 13.329 -4.525  8.444   0.52 18.25 ?  154 ALA   A HA   1 
ATOM   3617 H HA   B ALA   A 1 154 ? 13.294 -4.545  8.430   0.48 17.30 ?  154 ALA   A HA   1 
ATOM   3618 H HB1  A ALA   A 1 154 ? 14.239 -2.394  8.752   0.52 18.44 ?  154 ALA   A HB1  1 
ATOM   3619 H HB1  B ALA   A 1 154 ? 14.199 -2.422  8.822   0.48 17.42 ?  154 ALA   A HB1  1 
ATOM   3620 H HB2  A ALA   A 1 154 ? 15.147 -3.471  9.486   0.52 18.44 ?  154 ALA   A HB2  1 
ATOM   3621 H HB2  B ALA   A 1 154 ? 15.094 -3.520  9.542   0.48 17.42 ?  154 ALA   A HB2  1 
ATOM   3622 H HB3  A ALA   A 1 154 ? 15.600 -2.873  8.085   0.52 18.44 ?  154 ALA   A HB3  1 
ATOM   3623 H HB3  B ALA   A 1 154 ? 15.573 -2.881  8.168   0.48 17.42 ?  154 ALA   A HB3  1 
ATOM   3624 N N    A VAL   A 1 155 ? 12.273 -3.747  6.390   0.32 15.17 ?  155 VAL   A N    1 
ATOM   3625 N N    B VAL   A 1 155 ? 12.303 -3.845  6.304   0.48 13.53 ?  155 VAL   A N    1 
ATOM   3626 C CA   A VAL   A 1 155 ? 11.609 -3.266  5.181   0.32 16.18 ?  155 VAL   A CA   1 
ATOM   3627 C CA   B VAL   A 1 155 ? 11.690 -3.478  5.028   0.48 14.95 ?  155 VAL   A CA   1 
ATOM   3628 C CA   T VAL   A 1 155 ? 11.584 -3.348  5.236   0.20 16.98 ?  155 VAL   A CA   1 
ATOM   3629 C C    A VAL   A 1 155 ? 10.912 -1.959  5.544   0.32 16.47 ?  155 VAL   A C    1 
ATOM   3630 C C    B VAL   A 1 155 ? 10.912 -2.182  5.234   0.48 14.92 ?  155 VAL   A C    1 
ATOM   3631 C C    T VAL   A 1 155 ? 10.967 -1.978  5.532   0.20 16.67 ?  155 VAL   A C    1 
ATOM   3632 O O    A VAL   A 1 155 ? 9.957  -1.952  6.329   0.32 16.98 ?  155 VAL   A O    1 
ATOM   3633 O O    B VAL   A 1 155 ? 9.935  -2.150  5.987   0.48 14.18 ?  155 VAL   A O    1 
ATOM   3634 O O    T VAL   A 1 155 ? 10.069 -1.852  6.363   0.20 16.67 ?  155 VAL   A O    1 
ATOM   3635 C CB   A VAL   A 1 155 ? 10.606 -4.300  4.644   0.32 16.47 ?  155 VAL   A CB   1 
ATOM   3636 C CB   B VAL   A 1 155 ? 10.789 -4.607  4.492   0.48 16.41 ?  155 VAL   A CB   1 
ATOM   3637 C CB   T VAL   A 1 155 ? 10.551 -4.352  4.678   0.20 17.08 ?  155 VAL   A CB   1 
ATOM   3638 C CG1  A VAL   A 1 155 ? 9.997  -3.830  3.331   0.32 17.42 ?  155 VAL   A CG1  1 
ATOM   3639 C CG1  B VAL   A 1 155 ? 9.911  -4.115  3.354   0.48 17.41 ?  155 VAL   A CG1  1 
ATOM   3640 C CG1  T VAL   A 1 155 ? 9.912  -3.810  3.413   0.20 17.74 ?  155 VAL   A CG1  1 
ATOM   3641 C CG2  A VAL   A 1 155 ? 11.277 -5.664  4.468   0.32 16.90 ?  155 VAL   A CG2  1 
ATOM   3642 C CG2  B VAL   A 1 155 ? 11.645 -5.786  4.020   0.48 17.16 ?  155 VAL   A CG2  1 
ATOM   3643 C CG2  T VAL   A 1 155 ? 11.209 -5.707  4.407   0.20 17.20 ?  155 VAL   A CG2  1 
ATOM   3644 H H    A VAL   A 1 155 ? 11.721 -4.027  6.987   0.32 18.21 ?  155 VAL   A H    1 
ATOM   3645 H H    B VAL   A 1 155 ? 11.731 -4.132  6.881   0.48 16.24 ?  155 VAL   A H    1 
ATOM   3646 H HA   A VAL   A 1 155 ? 12.270 -3.088  4.495   0.32 19.42 ?  155 VAL   A HA   1 
ATOM   3647 H HA   B VAL   A 1 155 ? 12.381 -3.312  4.375   0.48 17.94 ?  155 VAL   A HA   1 
ATOM   3648 H HB   A VAL   A 1 155 ? 9.887  -4.404  5.288   0.32 19.77 ?  155 VAL   A HB   1 
ATOM   3649 H HB   B VAL   A 1 155 ? 10.213 -4.925  5.205   0.48 19.69 ?  155 VAL   A HB   1 
ATOM   3650 H HB   T VAL   A 1 155 ? 9.856  -4.485  5.338   0.20 20.50 ?  155 VAL   A HB   1 
ATOM   3651 H HG11 A VAL   A 1 155 ? 9.432  -4.535  2.976   0.32 20.91 ?  155 VAL   A HG11 1 
ATOM   3652 H HG11 B VAL   A 1 155 ? 9.574  -4.878  2.860   0.48 20.89 ?  155 VAL   A HG11 1 
ATOM   3653 H HG11 T VAL   A 1 155 ? 9.377  -4.508  3.008   0.20 21.29 ?  155 VAL   A HG11 1 
ATOM   3654 H HG12 A VAL   A 1 155 ? 9.466  -3.034  3.496   0.32 20.91 ?  155 VAL   A HG12 1 
ATOM   3655 H HG12 B VAL   A 1 155 ? 9.170  -3.608  3.720   0.48 20.89 ?  155 VAL   A HG12 1 
ATOM   3656 H HG12 T VAL   A 1 155 ? 9.352  -3.053  3.643   0.20 21.29 ?  155 VAL   A HG12 1 
ATOM   3657 H HG13 A VAL   A 1 155 ? 10.710 -3.630  2.706   0.32 20.91 ?  155 VAL   A HG13 1 
ATOM   3658 H HG13 B VAL   A 1 155 ? 10.441 -3.551  2.767   0.48 20.89 ?  155 VAL   A HG13 1 
ATOM   3659 H HG13 T VAL   A 1 155 ? 10.612 -3.532  2.801   0.20 21.29 ?  155 VAL   A HG13 1 
ATOM   3660 H HG21 A VAL   A 1 155 ? 10.653 -6.271  4.039   0.32 20.28 ?  155 VAL   A HG21 1 
ATOM   3661 H HG21 B VAL   A 1 155 ? 11.078 -6.431  3.571   0.48 20.59 ?  155 VAL   A HG21 1 
ATOM   3662 H HG21 T VAL   A 1 155 ? 10.540 -6.320  4.061   0.20 20.64 ?  155 VAL   A HG21 1 
ATOM   3663 H HG22 A VAL   A 1 155 ? 12.068 -5.558  3.915   0.32 20.28 ?  155 VAL   A HG22 1 
ATOM   3664 H HG22 B VAL   A 1 155 ? 12.321 -5.457  3.404   0.48 20.59 ?  155 VAL   A HG22 1 
ATOM   3665 H HG22 T VAL   A 1 155 ? 11.918 -5.591  3.754   0.20 20.64 ?  155 VAL   A HG22 1 
ATOM   3666 H HG23 A VAL   A 1 155 ? 11.529 -6.010  5.339   0.32 20.28 ?  155 VAL   A HG23 1 
ATOM   3667 H HG23 B VAL   A 1 155 ? 12.073 -6.196  4.788   0.48 20.59 ?  155 VAL   A HG23 1 
ATOM   3668 H HG23 T VAL   A 1 155 ? 11.577 -6.054  5.235   0.20 20.64 ?  155 VAL   A HG23 1 
ATOM   3669 N N    A PHE   A 1 156 ? 11.376 -0.847  4.970   0.32 16.75 ?  156 PHE   A N    1 
ATOM   3670 N N    B PHE   A 1 156 ? 11.336 -1.119  4.547   0.48 15.69 ?  156 PHE   A N    1 
ATOM   3671 N N    T PHE   A 1 156 ? 11.463 -0.953  4.837   0.20 16.60 ?  156 PHE   A N    1 
ATOM   3672 C CA   A PHE   A 1 156 ? 10.854 0.458   5.377   0.32 17.03 ?  156 PHE   A CA   1 
ATOM   3673 C CA   B PHE   A 1 156 ? 10.826 0.231   4.812   0.48 16.63 ?  156 PHE   A CA   1 
ATOM   3674 C CA   T PHE   A 1 156 ? 11.033 0.418   5.108   0.20 16.72 ?  156 PHE   A CA   1 
ATOM   3675 C C    A PHE   A 1 156 ? 9.404  0.658   4.943   0.32 17.39 ?  156 PHE   A C    1 
ATOM   3676 C C    B PHE   A 1 156 ? 9.350  0.377   4.446   0.48 17.94 ?  156 PHE   A C    1 
ATOM   3677 C C    T PHE   A 1 156 ? 9.581  0.645   4.701   0.20 17.02 ?  156 PHE   A C    1 
ATOM   3678 O O    A PHE   A 1 156 ? 8.610  1.255   5.681   0.32 17.88 ?  156 PHE   A O    1 
ATOM   3679 O O    B PHE   A 1 156 ? 8.571  0.948   5.217   0.48 18.72 ?  156 PHE   A O    1 
ATOM   3680 O O    T PHE   A 1 156 ? 8.817  1.282   5.435   0.20 17.56 ?  156 PHE   A O    1 
ATOM   3681 C CB   A PHE   A 1 156 ? 11.737 1.579   4.826   0.32 17.42 ?  156 PHE   A CB   1 
ATOM   3682 C CB   B PHE   A 1 156 ? 11.677 1.234   4.024   0.48 16.10 ?  156 PHE   A CB   1 
ATOM   3683 C CB   T PHE   A 1 156 ? 11.952 1.384   4.358   0.20 16.28 ?  156 PHE   A CB   1 
ATOM   3684 C CG   A PHE   A 1 156 ? 11.210 2.961   5.113   0.32 18.45 ?  156 PHE   A CG   1 
ATOM   3685 C CG   B PHE   A 1 156 ? 11.394 2.698   4.325   0.48 16.57 ?  156 PHE   A CG   1 
ATOM   3686 C CG   T PHE   A 1 156 ? 11.593 2.838   4.527   0.20 16.28 ?  156 PHE   A CG   1 
ATOM   3687 C CD1  A PHE   A 1 156 ? 11.036 3.391   6.419   0.32 18.47 ?  156 PHE   A CD1  1 
ATOM   3688 C CD1  B PHE   A 1 156 ? 11.937 3.306   5.449   0.48 17.99 ?  156 PHE   A CD1  1 
ATOM   3689 C CD1  T PHE   A 1 156 ? 11.924 3.516   5.689   0.20 16.68 ?  156 PHE   A CD1  1 
ATOM   3690 C CD2  A PHE   A 1 156 ? 10.892 3.830   4.080   0.32 19.27 ?  156 PHE   A CD2  1 
ATOM   3691 C CD2  B PHE   A 1 156 ? 10.636 3.474   3.458   0.48 17.99 ?  156 PHE   A CD2  1 
ATOM   3692 C CD2  T PHE   A 1 156 ? 10.955 3.533   3.511   0.20 16.52 ?  156 PHE   A CD2  1 
ATOM   3693 C CE1  A PHE   A 1 156 ? 10.549 4.658   6.690   0.32 18.87 ?  156 PHE   A CE1  1 
ATOM   3694 C CE1  B PHE   A 1 156 ? 11.706 4.650   5.722   0.48 19.19 ?  156 PHE   A CE1  1 
ATOM   3695 C CE1  T PHE   A 1 156 ? 11.609 4.856   5.843   0.20 16.91 ?  156 PHE   A CE1  1 
ATOM   3696 C CE2  A PHE   A 1 156 ? 10.405 5.100   4.345   0.32 19.71 ?  156 PHE   A CE2  1 
ATOM   3697 C CE2  B PHE   A 1 156 ? 10.402 4.819   3.725   0.48 18.95 ?  156 PHE   A CE2  1 
ATOM   3698 C CE2  T PHE   A 1 156 ? 10.639 4.872   3.659   0.20 16.51 ?  156 PHE   A CE2  1 
ATOM   3699 C CZ   A PHE   A 1 156 ? 10.235 5.514   5.653   0.32 19.63 ?  156 PHE   A CZ   1 
ATOM   3700 C CZ   B PHE   A 1 156 ? 10.943 5.407   4.859   0.48 19.84 ?  156 PHE   A CZ   1 
ATOM   3701 C CZ   T PHE   A 1 156 ? 10.967 5.534   4.828   0.20 17.00 ?  156 PHE   A CZ   1 
ATOM   3702 H H    A PHE   A 1 156 ? 11.975 -0.822  4.356   0.32 20.10 ?  156 PHE   A H    1 
ATOM   3703 H H    B PHE   A 1 156 ? 11.920 -1.153  3.927   0.48 18.82 ?  156 PHE   A H    1 
ATOM   3704 H H    T PHE   A 1 156 ? 12.047 -1.026  4.210   0.20 19.92 ?  156 PHE   A H    1 
ATOM   3705 H HA   A PHE   A 1 156 ? 10.880 0.514   6.343   0.32 20.44 ?  156 PHE   A HA   1 
ATOM   3706 H HA   B PHE   A 1 156 ? 10.919 0.428   5.757   0.48 19.96 ?  156 PHE   A HA   1 
ATOM   3707 H HA   T PHE   A 1 156 ? 11.117 0.595   6.058   0.20 20.06 ?  156 PHE   A HA   1 
ATOM   3708 H HB2  A PHE   A 1 156 ? 12.618 1.508   5.226   0.32 20.91 ?  156 PHE   A HB2  1 
ATOM   3709 H HB2  B PHE   A 1 156 ? 12.607 1.069   4.234   0.48 19.32 ?  156 PHE   A HB2  1 
ATOM   3710 H HB2  T PHE   A 1 156 ? 12.858 1.263   4.679   0.20 19.54 ?  156 PHE   A HB2  1 
ATOM   3711 H HB3  A PHE   A 1 156 ? 11.804 1.481   3.863   0.32 20.91 ?  156 PHE   A HB3  1 
ATOM   3712 H HB3  B PHE   A 1 156 ? 11.522 1.095   3.078   0.48 19.32 ?  156 PHE   A HB3  1 
ATOM   3713 H HB3  T PHE   A 1 156 ? 11.908 1.178   3.411   0.20 19.54 ?  156 PHE   A HB3  1 
ATOM   3714 H HD1  A PHE   A 1 156 ? 11.246 2.816   7.121   0.32 22.16 ?  156 PHE   A HD1  1 
ATOM   3715 H HD1  B PHE   A 1 156 ? 12.452 2.799   6.040   0.48 21.59 ?  156 PHE   A HD1  1 
ATOM   3716 H HD1  T PHE   A 1 156 ? 12.356 3.060   6.379   0.20 20.01 ?  156 PHE   A HD1  1 
ATOM   3717 H HD2  A PHE   A 1 156 ? 11.005 3.555   3.198   0.32 23.13 ?  156 PHE   A HD2  1 
ATOM   3718 H HD2  B PHE   A 1 156 ? 10.272 3.089   2.698   0.48 21.59 ?  156 PHE   A HD2  1 
ATOM   3719 H HD2  T PHE   A 1 156 ? 10.730 3.092   2.725   0.20 19.82 ?  156 PHE   A HD2  1 
ATOM   3720 H HE1  A PHE   A 1 156 ? 10.438 4.933   7.573   0.32 22.64 ?  156 PHE   A HE1  1 
ATOM   3721 H HE1  B PHE   A 1 156 ? 12.066 5.036   6.491   0.48 23.02 ?  156 PHE   A HE1  1 
ATOM   3722 H HE1  T PHE   A 1 156 ? 11.830 5.294   6.634   0.20 20.29 ?  156 PHE   A HE1  1 
ATOM   3723 H HE2  A PHE   A 1 156 ? 10.197 5.673   3.644   0.32 23.65 ?  156 PHE   A HE2  1 
ATOM   3724 H HE2  B PHE   A 1 156 ? 9.885  5.328   3.147   0.48 22.74 ?  156 PHE   A HE2  1 
ATOM   3725 H HE2  T PHE   A 1 156 ? 10.202 5.326   2.976   0.20 19.82 ?  156 PHE   A HE2  1 
ATOM   3726 H HZ   A PHE   A 1 156 ? 9.912  6.365   5.835   0.32 23.55 ?  156 PHE   A HZ   1 
ATOM   3727 H HZ   B PHE   A 1 156 ? 10.781 6.304   5.047   0.48 23.81 ?  156 PHE   A HZ   1 
ATOM   3728 H HZ   T PHE   A 1 156 ? 10.751 6.430   4.934   0.20 20.40 ?  156 PHE   A HZ   1 
ATOM   3729 N N    A ASP   A 1 157 ? 9.044  0.186   3.753   0.32 17.77 ?  157 ASP   A N    1 
ATOM   3730 N N    B ASP   A 1 157 ? 8.942  -0.132  3.287   0.48 19.61 ?  157 ASP   A N    1 
ATOM   3731 N N    T ASP   A 1 157 ? 9.189  0.140   3.536   0.20 17.44 ?  157 ASP   A N    1 
ATOM   3732 C CA   A ASP   A 1 157 ? 7.726  0.428   3.173   0.32 18.84 ?  157 ASP   A CA   1 
ATOM   3733 C CA   B ASP   A 1 157 ? 7.618  0.150   2.739   0.48 20.61 ?  157 ASP   A CA   1 
ATOM   3734 C CA   T ASP   A 1 157 ? 7.875  0.401   2.960   0.20 18.17 ?  157 ASP   A CA   1 
ATOM   3735 C C    A ASP   A 1 157 ? 6.737  -0.624  3.672   0.32 19.55 ?  157 ASP   A C    1 
ATOM   3736 C C    B ASP   A 1 157 ? 6.603  -0.887  3.207   0.48 19.40 ?  157 ASP   A C    1 
ATOM   3737 C C    T ASP   A 1 157 ? 6.864  -0.593  3.526   0.20 19.11 ?  157 ASP   A C    1 
ATOM   3738 O O    A ASP   A 1 157 ? 6.924  -1.820  3.428   0.32 19.51 ?  157 ASP   A O    1 
ATOM   3739 O O    B ASP   A 1 157 ? 6.775  -2.086  2.969   0.48 18.63 ?  157 ASP   A O    1 
ATOM   3740 O O    T ASP   A 1 157 ? 7.018  -1.806  3.353   0.20 19.20 ?  157 ASP   A O    1 
ATOM   3741 C CB   A ASP   A 1 157 ? 7.828  0.365   1.650   0.32 19.34 ?  157 ASP   A CB   1 
ATOM   3742 C CB   B ASP   A 1 157 ? 7.677  0.156   1.215   0.48 22.60 ?  157 ASP   A CB   1 
ATOM   3743 C CB   T ASP   A 1 157 ? 7.971  0.245   1.444   0.20 18.01 ?  157 ASP   A CB   1 
ATOM   3744 C CG   A ASP   A 1 157 ? 6.538  0.792   0.959   0.32 20.17 ?  157 ASP   A CG   1 
ATOM   3745 C CG   B ASP   A 1 157 ? 6.429  0.715   0.586   0.48 24.29 ?  157 ASP   A CG   1 
ATOM   3746 C CG   T ASP   A 1 157 ? 6.830  0.904   0.709   0.20 17.67 ?  157 ASP   A CG   1 
ATOM   3747 O OD1  A ASP   A 1 157 ? 6.117  1.963   1.108   0.32 20.99 ?  157 ASP   A OD1  1 
ATOM   3748 O OD1  B ASP   A 1 157 ? 5.325  0.282   0.977   0.48 25.08 ?  157 ASP   A OD1  1 
ATOM   3749 O OD1  T ASP   A 1 157 ? 6.936  2.117   0.424   0.20 17.08 ?  157 ASP   A OD1  1 
ATOM   3750 O OD2  A ASP   A 1 157 ? 5.933  -0.055  0.269   0.32 20.55 -1 157 ASP   A OD2  1 
ATOM   3751 O OD2  B ASP   A 1 157 ? 6.557  1.592   -0.299  0.48 25.23 -1 157 ASP   A OD2  1 
ATOM   3752 O OD2  T ASP   A 1 157 ? 5.838  0.209   0.402   0.20 17.94 -1 157 ASP   A OD2  1 
ATOM   3753 H H    A ASP   A 1 157 ? 9.554  -0.288  3.251   0.32 21.32 ?  157 ASP   A H    1 
ATOM   3754 H H    B ASP   A 1 157 ? 9.414  -0.656  2.798   0.48 23.54 ?  157 ASP   A H    1 
ATOM   3755 H H    T ASP   A 1 157 ? 9.681  -0.366  3.046   0.20 20.93 ?  157 ASP   A H    1 
ATOM   3756 H HA   A ASP   A 1 157 ? 7.406  1.311   3.426   0.32 22.60 ?  157 ASP   A HA   1 
ATOM   3757 H HA   B ASP   A 1 157 ? 7.319  1.016   3.050   0.48 24.73 ?  157 ASP   A HA   1 
ATOM   3758 H HA   T ASP   A 1 157 ? 7.589  1.303   3.175   0.20 21.80 ?  157 ASP   A HA   1 
ATOM   3759 H HB2  A ASP   A 1 157 ? 8.581  0.915   1.362   0.32 23.20 ?  157 ASP   A HB2  1 
ATOM   3760 H HB2  B ASP   A 1 157 ? 8.419  0.696   0.939   0.48 27.12 ?  157 ASP   A HB2  1 
ATOM   3761 H HB2  T ASP   A 1 157 ? 8.782  0.668   1.138   0.20 21.61 ?  157 ASP   A HB2  1 
ATOM   3762 H HB3  A ASP   A 1 157 ? 7.989  -0.557  1.384   0.32 23.20 ?  157 ASP   A HB3  1 
ATOM   3763 H HB3  B ASP   A 1 157 ? 7.776  -0.754  0.902   0.48 27.12 ?  157 ASP   A HB3  1 
ATOM   3764 H HB3  T ASP   A 1 157 ? 7.986  -0.700  1.229   0.20 21.61 ?  157 ASP   A HB3  1 
ATOM   3765 N N    A LYS   A 1 158 ? 5.668  -0.176  4.340   0.32 20.51 ?  158 LYS   A N    1 
ATOM   3766 N N    B LYS   A 1 158 ? 5.519  -0.409  3.826   0.48 19.89 ?  158 LYS   A N    1 
ATOM   3767 N N    T LYS   A 1 158 ? 5.820  -0.078  4.185   0.20 20.19 ?  158 LYS   A N    1 
ATOM   3768 C CA   A LYS   A 1 158 ? 4.710  -1.118  4.919   0.32 21.49 ?  158 LYS   A CA   1 
ATOM   3769 C CA   B LYS   A 1 158 ? 4.461  -1.299  4.299   0.48 20.35 ?  158 LYS   A CA   1 
ATOM   3770 C CA   T LYS   A 1 158 ? 4.836  -0.960  4.809   0.20 21.39 ?  158 LYS   A CA   1 
ATOM   3771 C C    A LYS   A 1 158 ? 3.952  -1.884  3.840   0.32 21.20 ?  158 LYS   A C    1 
ATOM   3772 C C    B LYS   A 1 158 ? 3.872  -2.110  3.149   0.48 19.89 ?  158 LYS   A C    1 
ATOM   3773 C C    T LYS   A 1 158 ? 4.071  -1.771  3.769   0.20 21.42 ?  158 LYS   A C    1 
ATOM   3774 O O    A LYS   A 1 158 ? 3.696  -3.084  3.989   0.32 20.94 ?  158 LYS   A O    1 
ATOM   3775 O O    B LYS   A 1 158 ? 3.672  -3.326  3.266   0.48 19.57 ?  158 LYS   A O    1 
ATOM   3776 O O    T LYS   A 1 158 ? 3.836  -2.969  3.962   0.20 21.31 ?  158 LYS   A O    1 
ATOM   3777 C CB   A LYS   A 1 158 ? 3.738  -0.384  5.847   0.32 22.65 ?  158 LYS   A CB   1 
ATOM   3778 C CB   B LYS   A 1 158 ? 3.370  -0.474  4.993   0.48 21.98 ?  158 LYS   A CB   1 
ATOM   3779 C CB   T LYS   A 1 158 ? 3.873  -0.150  5.682   0.20 22.70 ?  158 LYS   A CB   1 
ATOM   3780 C CG   A LYS   A 1 158 ? 2.517  -1.198  6.289   0.32 23.82 ?  158 LYS   A CG   1 
ATOM   3781 C CG   B LYS   A 1 158 ? 2.068  -1.237  5.251   0.48 23.76 ?  158 LYS   A CG   1 
ATOM   3782 C CG   T LYS   A 1 158 ? 2.649  -0.928  6.169   0.20 24.03 ?  158 LYS   A CG   1 
ATOM   3783 C CD   A LYS   A 1 158 ? 2.887  -2.451  7.086   0.32 24.83 ?  158 LYS   A CD   1 
ATOM   3784 C CD   B LYS   A 1 158 ? 0.876  -0.299  5.344   0.48 25.35 ?  158 LYS   A CD   1 
ATOM   3785 C CD   T LYS   A 1 158 ? 3.032  -2.135  7.021   0.20 25.45 ?  158 LYS   A CD   1 
ATOM   3786 C CE   A LYS   A 1 158 ? 1.632  -3.134  7.637   0.32 25.09 ?  158 LYS   A CE   1 
ATOM   3787 C CE   B LYS   A 1 158 ? 0.293  -0.266  6.745   0.48 27.06 ?  158 LYS   A CE   1 
ATOM   3788 C CE   T LYS   A 1 158 ? 1.799  -2.934  7.431   0.20 26.50 ?  158 LYS   A CE   1 
ATOM   3789 N NZ   A LYS   A 1 158 ? 1.892  -4.501  8.174   0.32 24.86 ?  158 LYS   A NZ   1 
ATOM   3790 N NZ   B LYS   A 1 158 ? -0.826 0.710   6.854   0.48 28.29 ?  158 LYS   A NZ   1 
ATOM   3791 N NZ   T LYS   A 1 158 ? 2.143  -4.152  8.217   0.20 27.07 ?  158 LYS   A NZ   1 
ATOM   3792 H H    A LYS   A 1 158 ? 5.479  0.652   4.469   0.32 24.62 ?  158 LYS   A H    1 
ATOM   3793 H H    B LYS   A 1 158 ? 5.368  0.422   3.979   0.48 23.87 ?  158 LYS   A H    1 
ATOM   3794 H H    T LYS   A 1 158 ? 5.661  0.761   4.281   0.20 24.23 ?  158 LYS   A H    1 
ATOM   3795 H HA   A LYS   A 1 158 ? 5.194  -1.764  5.454   0.32 25.79 ?  158 LYS   A HA   1 
ATOM   3796 H HA   B LYS   A 1 158 ? 4.817  -1.918  4.954   0.48 24.42 ?  158 LYS   A HA   1 
ATOM   3797 H HA   T LYS   A 1 158 ? 5.298  -1.585  5.388   0.20 25.67 ?  158 LYS   A HA   1 
ATOM   3798 H HB2  A LYS   A 1 158 ? 4.217  -0.122  6.650   0.32 27.18 ?  158 LYS   A HB2  1 
ATOM   3799 H HB2  B LYS   A 1 158 ? 3.702  -0.172  5.861   0.48 26.38 ?  158 LYS   A HB2  1 
ATOM   3800 H HB2  T LYS   A 1 158 ? 4.351  0.159   6.469   0.20 27.24 ?  158 LYS   A HB2  1 
ATOM   3801 H HB3  A LYS   A 1 158 ? 3.411  0.407   5.392   0.32 27.18 ?  158 LYS   A HB3  1 
ATOM   3802 H HB3  B LYS   A 1 158 ? 3.161  0.297   4.444   0.48 26.38 ?  158 LYS   A HB3  1 
ATOM   3803 H HB3  T LYS   A 1 158 ? 3.553  0.610   5.174   0.20 27.24 ?  158 LYS   A HB3  1 
ATOM   3804 H HG2  A LYS   A 1 158 ? 1.963  -0.641  6.857   0.32 28.58 ?  158 LYS   A HG2  1 
ATOM   3805 H HG2  B LYS   A 1 158 ? 1.883  -1.864  4.537   0.48 28.51 ?  158 LYS   A HG2  1 
ATOM   3806 H HG2  T LYS   A 1 158 ? 2.103  -0.342  6.715   0.20 28.83 ?  158 LYS   A HG2  1 
ATOM   3807 H HG3  A LYS   A 1 158 ? 2.009  -1.474  5.509   0.32 28.58 ?  158 LYS   A HG3  1 
ATOM   3808 H HG3  B LYS   A 1 158 ? 2.147  -1.711  6.092   0.48 28.51 ?  158 LYS   A HG3  1 
ATOM   3809 H HG3  T LYS   A 1 158 ? 2.133  -1.241  5.409   0.20 28.83 ?  158 LYS   A HG3  1 
ATOM   3810 H HD2  A LYS   A 1 158 ? 3.347  -3.078  6.508   0.32 29.79 ?  158 LYS   A HD2  1 
ATOM   3811 H HD2  B LYS   A 1 158 ? 1.148  0.601   5.109   0.48 30.42 ?  158 LYS   A HD2  1 
ATOM   3812 H HD2  T LYS   A 1 158 ? 3.615  -2.720  6.513   0.20 30.54 ?  158 LYS   A HD2  1 
ATOM   3813 H HD3  A LYS   A 1 158 ? 3.454  -2.200  7.833   0.32 29.79 ?  158 LYS   A HD3  1 
ATOM   3814 H HD3  B LYS   A 1 158 ? 0.186  -0.608  4.735   0.48 30.42 ?  158 LYS   A HD3  1 
ATOM   3815 H HD3  T LYS   A 1 158 ? 3.480  -1.831  7.827   0.20 30.54 ?  158 LYS   A HD3  1 
ATOM   3816 H HE2  A LYS   A 1 158 ? 1.264  -2.593  8.353   0.32 30.10 ?  158 LYS   A HE2  1 
ATOM   3817 H HE2  B LYS   A 1 158 ? -0.048 -1.147  6.968   0.48 32.47 ?  158 LYS   A HE2  1 
ATOM   3818 H HE2  T LYS   A 1 158 ? 1.221  -2.375  7.975   0.20 31.80 ?  158 LYS   A HE2  1 
ATOM   3819 H HE3  A LYS   A 1 158 ? 0.984  -3.214  6.924   0.32 30.10 ?  158 LYS   A HE3  1 
ATOM   3820 H HE3  B LYS   A 1 158 ? 0.986  -0.008  7.372   0.48 32.47 ?  158 LYS   A HE3  1 
ATOM   3821 H HE3  T LYS   A 1 158 ? 1.327  -3.217  6.633   0.20 31.80 ?  158 LYS   A HE3  1 
ATOM   3822 H HZ1  A LYS   A 1 158 ? 1.137  -4.855  8.483   0.32 29.84 ?  158 LYS   A HZ1  1 
ATOM   3823 H HZ1  B LYS   A 1 158 ? -1.149 0.710   7.683   0.48 33.95 ?  158 LYS   A HZ1  1 
ATOM   3824 H HZ1  T LYS   A 1 158 ? 1.401  -4.592  8.438   0.20 32.49 ?  158 LYS   A HZ1  1 
ATOM   3825 H HZ2  A LYS   A 1 158 ? 2.215  -5.023  7.529   0.32 29.84 ?  158 LYS   A HZ2  1 
ATOM   3826 H HZ2  B LYS   A 1 158 ? -0.536 1.528   6.657   0.48 33.95 ?  158 LYS   A HZ2  1 
ATOM   3827 H HZ2  T LYS   A 1 158 ? 2.663  -4.689  7.733   0.20 32.49 ?  158 LYS   A HZ2  1 
ATOM   3828 H HZ3  A LYS   A 1 158 ? 2.486  -4.461  8.837   0.32 29.84 ?  158 LYS   A HZ3  1 
ATOM   3829 H HZ3  B LYS   A 1 158 ? -1.478 0.491   6.289   0.48 33.95 ?  158 LYS   A HZ3  1 
ATOM   3830 H HZ3  T LYS   A 1 158 ? 2.576  -3.924  8.960   0.20 32.49 ?  158 LYS   A HZ3  1 
ATOM   3831 N N    A ASN   A 1 159 ? 3.563  -1.208  2.757   0.32 21.34 ?  159 ASN   A N    1 
ATOM   3832 N N    B ASN   A 1 159 ? 3.549  -1.442  2.040   0.48 20.35 ?  159 ASN   A N    1 
ATOM   3833 N N    T ASN   A 1 159 ? 3.661  -1.141  2.674   0.20 21.84 ?  159 ASN   A N    1 
ATOM   3834 C CA   A ASN   A 1 159 ? 2.854  -1.899  1.685   0.32 21.21 ?  159 ASN   A CA   1 
ATOM   3835 C CA   B ASN   A 1 159 ? 2.995  -2.149  0.891   0.48 21.86 ?  159 ASN   A CA   1 
ATOM   3836 C CA   T ASN   A 1 159 ? 2.908  -1.841  1.637   0.20 21.97 ?  159 ASN   A CA   1 
ATOM   3837 C C    A ASN   A 1 159 ? 3.727  -2.978  1.059   0.32 20.40 ?  159 ASN   A C    1 
ATOM   3838 C C    B ASN   A 1 159 ? 3.942  -3.246  0.427   0.48 21.92 ?  159 ASN   A C    1 
ATOM   3839 C C    T ASN   A 1 159 ? 3.729  -2.954  0.997   0.20 21.98 ?  159 ASN   A C    1 
ATOM   3840 O O    A ASN   A 1 159 ? 3.260  -4.091  0.793   0.32 19.83 ?  159 ASN   A O    1 
ATOM   3841 O O    B ASN   A 1 159 ? 3.514  -4.365  0.113   0.48 21.91 ?  159 ASN   A O    1 
ATOM   3842 O O    T ASN   A 1 159 ? 3.190  -3.990  0.615   0.20 21.92 ?  159 ASN   A O    1 
ATOM   3843 C CB   A ASN   A 1 159 ? 2.374  -0.894  0.636   0.32 22.20 ?  159 ASN   A CB   1 
ATOM   3844 C CB   B ASN   A 1 159 ? 2.704  -1.150  -0.234  0.48 23.69 ?  159 ASN   A CB   1 
ATOM   3845 C CB   T ASN   A 1 159 ? 2.416  -0.862  0.568   0.20 22.39 ?  159 ASN   A CB   1 
ATOM   3846 C CG   A ASN   A 1 159 ? 1.176  -0.090  1.107   0.32 23.17 ?  159 ASN   A CG   1 
ATOM   3847 C CG   B ASN   A 1 159 ? 1.592  -0.174  0.121   0.48 25.97 ?  159 ASN   A CG   1 
ATOM   3848 C CG   T ASN   A 1 159 ? 1.225  -0.044  1.033   0.20 22.79 ?  159 ASN   A CG   1 
ATOM   3849 O OD1  A ASN   A 1 159 ? 0.320  -0.604  1.824   0.32 23.74 ?  159 ASN   A OD1  1 
ATOM   3850 O OD1  B ASN   A 1 159 ? 1.706  1.031   -0.120  0.48 27.45 ?  159 ASN   A OD1  1 
ATOM   3851 O OD1  T ASN   A 1 159 ? 0.403  -0.520  1.814   0.20 23.09 ?  159 ASN   A OD1  1 
ATOM   3852 N ND2  A ASN   A 1 159 ? 1.107  1.174   0.705   0.32 23.94 ?  159 ASN   A ND2  1 
ATOM   3853 N ND2  B ASN   A 1 159 ? 0.508  -0.692  0.689   0.48 26.32 ?  159 ASN   A ND2  1 
ATOM   3854 N ND2  T ASN   A 1 159 ? 1.126  1.188   0.554   0.20 23.18 ?  159 ASN   A ND2  1 
ATOM   3855 H H    A ASN   A 1 159 ? 3.696  -0.372  2.623   0.32 25.61 ?  159 ASN   A H    1 
ATOM   3856 H H    B ASN   A 1 159 ? 3.646  -0.595  1.932   0.48 24.42 ?  159 ASN   A H    1 
ATOM   3857 H H    T ASN   A 1 159 ? 3.800  -0.310  2.510   0.20 26.21 ?  159 ASN   A H    1 
ATOM   3858 H HA   A ASN   A 1 159 ? 2.073  -2.337  2.056   0.32 25.45 ?  159 ASN   A HA   1 
ATOM   3859 H HA   B ASN   A 1 159 ? 2.159  -2.568  1.142   0.48 26.23 ?  159 ASN   A HA   1 
ATOM   3860 H HA   T ASN   A 1 159 ? 2.131  -2.253  2.040   0.20 26.37 ?  159 ASN   A HA   1 
ATOM   3861 H HB2  A ASN   A 1 159 ? 3.089  -0.271  0.440   0.32 26.64 ?  159 ASN   A HB2  1 
ATOM   3862 H HB2  B ASN   A 1 159 ? 3.501  -0.625  -0.416  0.48 28.42 ?  159 ASN   A HB2  1 
ATOM   3863 H HB2  T ASN   A 1 159 ? 3.132  -0.249  0.346   0.20 26.87 ?  159 ASN   A HB2  1 
ATOM   3864 H HB3  A ASN   A 1 159 ? 2.116  -1.371  -0.168  0.32 26.64 ?  159 ASN   A HB3  1 
ATOM   3865 H HB3  B ASN   A 1 159 ? 2.432  -1.628  -1.031  0.48 28.42 ?  159 ASN   A HB3  1 
ATOM   3866 H HB3  T ASN   A 1 159 ? 2.150  -1.363  -0.220  0.20 26.87 ?  159 ASN   A HB3  1 
ATOM   3867 H HD21 A ASN   A 1 159 ? 0.445  1.666   0.947   0.32 28.73 ?  159 ASN   A HD21 1 
ATOM   3868 H HD21 B ASN   A 1 159 ? -0.151 -0.184  0.907   0.48 31.58 ?  159 ASN   A HD21 1 
ATOM   3869 H HD21 T ASN   A 1 159 ? 0.467  1.687   0.790   0.20 27.81 ?  159 ASN   A HD21 1 
ATOM   3870 H HD22 A ASN   A 1 159 ? 1.724  1.498   0.207   0.32 28.73 ?  159 ASN   A HD22 1 
ATOM   3871 H HD22 B ASN   A 1 159 ? 0.463  -1.537  0.844   0.48 31.58 ?  159 ASN   A HD22 1 
ATOM   3872 H HD22 T ASN   A 1 159 ? 1.720  1.486   0.013   0.20 27.81 ?  159 ASN   A HD22 1 
ATOM   3873 N N    A LEU   A 1 160 ? 5.005  -2.676  0.839   0.32 19.75 ?  160 LEU   A N    1 
ATOM   3874 N N    B LEU   A 1 160 ? 5.241  -2.950  0.410   0.48 21.66 ?  160 LEU   A N    1 
ATOM   3875 N N    T LEU   A 1 160 ? 5.034  -2.738  0.885   0.20 21.96 ?  160 LEU   A N    1 
ATOM   3876 C CA   A LEU   A 1 160 ? 5.908  -3.688  0.305   0.32 19.23 ?  160 LEU   A CA   1 
ATOM   3877 C CA   B LEU   A 1 160 ? 6.231  -3.945  0.014   0.48 21.25 ?  160 LEU   A CA   1 
ATOM   3878 C CA   T LEU   A 1 160 ? 5.922  -3.745  0.321   0.20 21.93 ?  160 LEU   A CA   1 
ATOM   3879 C C    A LEU   A 1 160 ? 6.110  -4.820  1.302   0.32 18.46 ?  160 LEU   A C    1 
ATOM   3880 C C    B LEU   A 1 160 ? 6.243  -5.119  0.985   0.48 19.78 ?  160 LEU   A C    1 
ATOM   3881 O O    A LEU   A 1 160 ? 6.158  -5.995  0.917   0.32 18.79 ?  160 LEU   A O    1 
ATOM   3882 O O    B LEU   A 1 160 ? 6.198  -6.288  0.579   0.48 19.54 ?  160 LEU   A O    1 
ATOM   3883 C CB   A LEU   A 1 160 ? 7.248  -3.057  -0.062  0.32 19.29 ?  160 LEU   A CB   1 
ATOM   3884 C CB   B LEU   A 1 160 ? 7.610  -3.288  -0.027  0.48 22.93 ?  160 LEU   A CB   1 
ATOM   3885 C CB   T LEU   A 1 160 ? 7.290  -3.140  0.014   0.20 21.86 ?  160 LEU   A CB   1 
ATOM   3886 C CG   A LEU   A 1 160 ? 8.334  -4.055  -0.458  0.32 19.91 ?  160 LEU   A CG   1 
ATOM   3887 C CG   B LEU   A 1 160 ? 8.768  -4.226  -0.352  0.48 24.81 ?  160 LEU   A CG   1 
ATOM   3888 C CG   T LEU   A 1 160 ? 8.367  -4.134  -0.420  0.20 22.08 ?  160 LEU   A CG   1 
ATOM   3889 C CD1  A LEU   A 1 160 ? 7.887  -4.880  -1.648  0.32 20.59 ?  160 LEU   A CD1  1 
ATOM   3890 C CD1  B LEU   A 1 160 ? 8.524  -4.880  -1.688  0.48 25.32 ?  160 LEU   A CD1  1 
ATOM   3891 C CD1  T LEU   A 1 160 ? 7.931  -4.903  -1.651  0.20 22.36 ?  160 LEU   A CD1  1 
ATOM   3892 C CD2  A LEU   A 1 160 ? 9.629  -3.329  -0.760  0.32 19.58 ?  160 LEU   A CD2  1 
ATOM   3893 C CD2  B LEU   A 1 160 ? 10.086 -3.480  -0.357  0.48 25.48 ?  160 LEU   A CD2  1 
ATOM   3894 C CD2  T LEU   A 1 160 ? 9.674  -3.410  -0.678  0.20 21.90 ?  160 LEU   A CD2  1 
ATOM   3895 H H    A LEU   A 1 160 ? 5.372  -1.915  1.000   0.32 23.70 ?  160 LEU   A H    1 
ATOM   3896 H H    B LEU   A 1 160 ? 5.573  -2.186  0.642   0.48 25.99 ?  160 LEU   A H    1 
ATOM   3897 H H    T LEU   A 1 160 ? 5.434  -2.015  1.128   0.20 26.36 ?  160 LEU   A H    1 
ATOM   3898 H HA   A LEU   A 1 160 ? 5.525  -4.061  -0.500  0.32 23.08 ?  160 LEU   A HA   1 
ATOM   3899 H HA   B LEU   A 1 160 ? 6.016  -4.270  -0.871  0.48 25.50 ?  160 LEU   A HA   1 
ATOM   3900 H HB2  A LEU   A 1 160 ? 7.116  -2.452  -0.811  0.32 23.15 ?  160 LEU   A HB2  1 
ATOM   3901 H HB2  B LEU   A 1 160 ? 7.603  -2.583  -0.694  0.48 27.51 ?  160 LEU   A HB2  1 
ATOM   3902 H HB2  T LEU   A 1 160 ? 7.189  -2.484  -0.696  0.20 26.23 ?  160 LEU   A HB2  1 
ATOM   3903 H HB3  A LEU   A 1 160 ? 7.577  -2.561  0.703   0.32 23.15 ?  160 LEU   A HB3  1 
ATOM   3904 H HB3  B LEU   A 1 160 ? 7.789  -2.904  0.848   0.48 27.51 ?  160 LEU   A HB3  1 
ATOM   3905 H HB3  T LEU   A 1 160 ? 7.617  -2.705  0.816   0.20 26.23 ?  160 LEU   A HB3  1 
ATOM   3906 H HG   A LEU   A 1 160 ? 8.508  -4.657  0.282   0.32 23.89 ?  160 LEU   A HG   1 
ATOM   3907 H HG   B LEU   A 1 160 ? 8.821  -4.921  0.326   0.48 29.77 ?  160 LEU   A HG   1 
ATOM   3908 H HG   T LEU   A 1 160 ? 8.518  -4.769  0.298   0.20 26.50 ?  160 LEU   A HG   1 
ATOM   3909 H HD11 A LEU   A 1 160 ? 8.629  -5.430  -1.943  0.32 24.70 ?  160 LEU   A HD11 1 
ATOM   3910 H HD11 B LEU   A 1 160 ? 9.329  -5.339  -1.958  0.48 30.39 ?  160 LEU   A HD11 1 
ATOM   3911 H HD11 T LEU   A 1 160 ? 8.669  -5.454  -1.955  0.20 26.83 ?  160 LEU   A HD11 1 
ATOM   3912 H HD12 A LEU   A 1 160 ? 7.145  -5.443  -1.379  0.32 24.70 ?  160 LEU   A HD12 1 
ATOM   3913 H HD12 B LEU   A 1 160 ? 7.792  -5.508  -1.602  0.48 30.39 ?  160 LEU   A HD12 1 
ATOM   3914 H HD12 T LEU   A 1 160 ? 7.174  -5.462  -1.421  0.20 26.83 ?  160 LEU   A HD12 1 
ATOM   3915 H HD13 A LEU   A 1 160 ? 7.613  -4.282  -2.359  0.32 24.70 ?  160 LEU   A HD13 1 
ATOM   3916 H HD13 B LEU   A 1 160 ? 8.299  -4.191  -2.334  0.48 30.39 ?  160 LEU   A HD13 1 
ATOM   3917 H HD13 T LEU   A 1 160 ? 7.682  -4.271  -2.343  0.20 26.83 ?  160 LEU   A HD13 1 
ATOM   3918 H HD21 A LEU   A 1 160 ? 10.309 -3.979  -1.006  0.32 23.50 ?  160 LEU   A HD21 1 
ATOM   3919 H HD21 B LEU   A 1 160 ? 10.810 -4.123  -0.380  0.48 30.58 ?  160 LEU   A HD21 1 
ATOM   3920 H HD21 T LEU   A 1 160 ? 10.331 -4.047  -0.998  0.20 26.28 ?  160 LEU   A HD21 1 
ATOM   3921 H HD22 A LEU   A 1 160 ? 9.485  -2.710  -1.492  0.32 23.50 ?  160 LEU   A HD22 1 
ATOM   3922 H HD22 B LEU   A 1 160 ? 10.121 -2.913  -1.143  0.48 30.58 ?  160 LEU   A HD22 1 
ATOM   3923 H HD22 T LEU   A 1 160 ? 9.527  -2.722  -1.347  0.20 26.28 ?  160 LEU   A HD22 1 
ATOM   3924 H HD23 A LEU   A 1 160 ? 9.914  -2.842  0.032   0.32 23.50 ?  160 LEU   A HD23 1 
ATOM   3925 H HD23 B LEU   A 1 160 ? 10.148 -2.940  0.446   0.48 30.58 ?  160 LEU   A HD23 1 
ATOM   3926 H HD23 T LEU   A 1 160 ? 9.981  -3.006  0.149   0.20 26.28 ?  160 LEU   A HD23 1 
ATOM   3927 N N    A TYR   A 1 161 ? 6.238  -4.487  2.586   0.52 19.13 ?  161 TYR   A N    1 
ATOM   3928 N N    B TYR   A 1 161 ? 6.341  -4.818  2.280   0.48 19.83 ?  161 TYR   A N    1 
ATOM   3929 C CA   A TYR   A 1 161 ? 6.384  -5.526  3.598   0.52 18.71 ?  161 TYR   A CA   1 
ATOM   3930 C CA   B TYR   A 1 161 ? 6.339  -5.853  3.308   0.48 19.88 ?  161 TYR   A CA   1 
ATOM   3931 C C    A TYR   A 1 161 ? 5.235  -6.525  3.527   0.52 19.49 ?  161 TYR   A C    1 
ATOM   3932 C C    B TYR   A 1 161 ? 5.166  -6.811  3.128   0.48 20.74 ?  161 TYR   A C    1 
ATOM   3933 O O    A TYR   A 1 161 ? 5.461  -7.740  3.471   0.52 19.30 ?  161 TYR   A O    1 
ATOM   3934 O O    B TYR   A 1 161 ? 5.312  -8.025  3.310   0.48 20.63 ?  161 TYR   A O    1 
ATOM   3935 C CB   A TYR   A 1 161 ? 6.489  -4.916  4.995   0.52 18.98 ?  161 TYR   A CB   1 
ATOM   3936 C CB   B TYR   A 1 161 ? 6.310  -5.171  4.680   0.48 19.78 ?  161 TYR   A CB   1 
ATOM   3937 C CG   A TYR   A 1 161 ? 6.419  -5.971  6.070   0.52 18.84 ?  161 TYR   A CG   1 
ATOM   3938 C CG   B TYR   A 1 161 ? 6.251  -6.083  5.887   0.48 19.92 ?  161 TYR   A CG   1 
ATOM   3939 C CD1  A TYR   A 1 161 ? 7.553  -6.689  6.436   0.52 18.86 ?  161 TYR   A CD1  1 
ATOM   3940 C CD1  B TYR   A 1 161 ? 7.397  -6.713  6.368   0.48 20.62 ?  161 TYR   A CD1  1 
ATOM   3941 C CD2  A TYR   A 1 161 ? 5.216  -6.276  6.699   0.52 19.24 ?  161 TYR   A CD2  1 
ATOM   3942 C CD2  B TYR   A 1 161 ? 5.059  -6.273  6.581   0.48 20.19 ?  161 TYR   A CD2  1 
ATOM   3943 C CE1  A TYR   A 1 161 ? 7.494  -7.668  7.400   0.52 18.83 ?  161 TYR   A CE1  1 
ATOM   3944 C CE1  B TYR   A 1 161 ? 7.348  -7.533  7.481   0.48 20.60 ?  161 TYR   A CE1  1 
ATOM   3945 C CE2  A TYR   A 1 161 ? 5.148  -7.257  7.666   0.52 18.85 ?  161 TYR   A CE2  1 
ATOM   3946 C CE2  B TYR   A 1 161 ? 5.001  -7.092  7.698   0.48 20.19 ?  161 TYR   A CE2  1 
ATOM   3947 C CZ   A TYR   A 1 161 ? 6.293  -7.948  8.012   0.52 18.79 ?  161 TYR   A CZ   1 
ATOM   3948 C CZ   B TYR   A 1 161 ? 6.150  -7.717  8.144   0.48 21.06 ?  161 TYR   A CZ   1 
ATOM   3949 O OH   A TYR   A 1 161 ? 6.244  -8.926  8.975   0.52 18.78 ?  161 TYR   A OH   1 
ATOM   3950 O OH   B TYR   A 1 161 ? 6.108  -8.532  9.254   0.48 22.61 ?  161 TYR   A OH   1 
ATOM   3951 H H    A TYR   A 1 161 ? 6.239  -3.686  2.893   0.52 22.95 ?  161 TYR   A H    1 
ATOM   3952 H H    B TYR   A 1 161 ? 6.409  -4.021  2.589   0.48 23.79 ?  161 TYR   A H    1 
ATOM   3953 H HA   A TYR   A 1 161 ? 7.201  -6.017  3.432   0.52 22.45 ?  161 TYR   A HA   1 
ATOM   3954 H HA   B TYR   A 1 161 ? 7.156  -6.369  3.245   0.48 23.85 ?  161 TYR   A HA   1 
ATOM   3955 H HB2  A TYR   A 1 161 ? 7.340  -4.455  5.081   0.52 22.78 ?  161 TYR   A HB2  1 
ATOM   3956 H HB2  B TYR   A 1 161 ? 7.114  -4.632  4.768   0.48 23.74 ?  161 TYR   A HB2  1 
ATOM   3957 H HB3  A TYR   A 1 161 ? 5.757  -4.295  5.134   0.52 22.78 ?  161 TYR   A HB3  1 
ATOM   3958 H HB3  B TYR   A 1 161 ? 5.533  -4.594  4.720   0.48 23.74 ?  161 TYR   A HB3  1 
ATOM   3959 H HD1  A TYR   A 1 161 ? 8.365  -6.505  6.024   0.52 22.63 ?  161 TYR   A HD1  1 
ATOM   3960 H HD1  B TYR   A 1 161 ? 8.205  -6.595  5.926   0.48 24.75 ?  161 TYR   A HD1  1 
ATOM   3961 H HD2  A TYR   A 1 161 ? 4.444  -5.814  6.469   0.52 23.09 ?  161 TYR   A HD2  1 
ATOM   3962 H HD2  B TYR   A 1 161 ? 4.285  -5.853  6.286   0.48 24.22 ?  161 TYR   A HD2  1 
ATOM   3963 H HE1  A TYR   A 1 161 ? 8.260  -8.142  7.639   0.52 22.60 ?  161 TYR   A HE1  1 
ATOM   3964 H HE1  B TYR   A 1 161 ? 8.119  -7.957  7.787   0.48 24.72 ?  161 TYR   A HE1  1 
ATOM   3965 H HE2  A TYR   A 1 161 ? 4.338  -7.453  8.086   0.52 22.62 ?  161 TYR   A HE2  1 
ATOM   3966 H HE2  B TYR   A 1 161 ? 4.195  -7.218  8.150   0.48 24.23 ?  161 TYR   A HE2  1 
ATOM   3967 H HH   A TYR   A 1 161 ? 5.437  -9.116  9.152   0.52 22.54 ?  161 TYR   A HH   1 
ATOM   3968 H HH   B TYR   A 1 161 ? 5.509  -8.264  9.787   0.48 27.13 ?  161 TYR   A HH   1 
ATOM   3969 N N    A ASP   A 1 162 ? 3.991  -6.027  3.521   0.52 18.97 ?  162 ASP   A N    1 
ATOM   3970 N N    B ASP   A 1 162 ? 3.999  -6.279  2.745   0.48 21.43 ?  162 ASP   A N    1 
ATOM   3971 C CA   A ASP   A 1 162 ? 2.835  -6.923  3.468   0.52 19.06 ?  162 ASP   A CA   1 
ATOM   3972 C CA   B ASP   A 1 162 ? 2.817  -7.112  2.535   0.48 23.17 ?  162 ASP   A CA   1 
ATOM   3973 C C    A ASP   A 1 162 ? 2.873  -7.789  2.213   0.52 18.50 ?  162 ASP   A C    1 
ATOM   3974 C C    B ASP   A 1 162 ? 2.957  -7.970  1.282   0.48 23.56 ?  162 ASP   A C    1 
ATOM   3975 O O    A ASP   A 1 162 ? 2.495  -8.966  2.247   0.52 18.38 ?  162 ASP   A O    1 
ATOM   3976 O O    B ASP   A 1 162 ? 2.591  -9.153  1.290   0.48 23.73 ?  162 ASP   A O    1 
ATOM   3977 C CB   A ASP   A 1 162 ? 1.525  -6.125  3.506   0.52 20.64 ?  162 ASP   A CB   1 
ATOM   3978 C CB   B ASP   A 1 162 ? 1.567  -6.232  2.430   0.48 24.90 ?  162 ASP   A CB   1 
ATOM   3979 C CG   A ASP   A 1 162 ? 1.254  -5.465  4.841   0.52 21.77 ?  162 ASP   A CG   1 
ATOM   3980 C CG   B ASP   A 1 162 ? 1.318  -5.402  3.682   0.48 26.42 ?  162 ASP   A CG   1 
ATOM   3981 O OD1  A ASP   A 1 162 ? 1.915  -5.803  5.838   0.52 22.48 ?  162 ASP   A OD1  1 
ATOM   3982 O OD1  B ASP   A 1 162 ? 1.864  -5.749  4.750   0.48 26.78 ?  162 ASP   A OD1  1 
ATOM   3983 O OD2  A ASP   A 1 162 ? 0.352  -4.596  4.880   0.52 22.42 -1 162 ASP   A OD2  1 
ATOM   3984 O OD2  B ASP   A 1 162 ? 0.548  -4.417  3.604   0.48 27.61 -1 162 ASP   A OD2  1 
ATOM   3985 H H    A ASP   A 1 162 ? 3.792  -5.186  3.540   0.52 22.77 ?  162 ASP   A H    1 
ATOM   3986 H H    B ASP   A 1 162 ? 3.870  -5.444  2.598   0.48 25.72 ?  162 ASP   A H    1 
ATOM   3987 H HA   A ASP   A 1 162 ? 2.853  -7.509  4.237   0.52 22.87 ?  162 ASP   A HA   1 
ATOM   3988 H HA   B ASP   A 1 162 ? 2.704  -7.705  3.289   0.48 27.81 ?  162 ASP   A HA   1 
ATOM   3989 H HB2  A ASP   A 1 162 ? 1.553  -5.424  2.851   0.52 24.77 ?  162 ASP   A HB2  1 
ATOM   3990 H HB2  B ASP   A 1 162 ? 1.663  -5.643  1.661   0.48 29.88 ?  162 ASP   A HB2  1 
ATOM   3991 H HB3  A ASP   A 1 162 ? 0.783  -6.724  3.344   0.52 24.77 ?  162 ASP   A HB3  1 
ATOM   3992 H HB3  B ASP   A 1 162 ? 0.789  -6.795  2.316   0.48 29.88 ?  162 ASP   A HB3  1 
ATOM   3993 N N    A LYS   A 1 163 ? 3.316  -7.221  1.088   0.52 19.63 ?  163 LYS   A N    1 
ATOM   3994 N N    B LYS   A 1 163 ? 3.460  -7.385  0.190   0.48 23.82 ?  163 LYS   A N    1 
ATOM   3995 C CA   A LYS   A 1 163 ? 3.405  -8.005  -0.139  0.52 20.76 ?  163 LYS   A CA   1 
ATOM   3996 C CA   B LYS   A 1 163 ? 3.650  -8.143  -1.044  0.48 24.77 ?  163 LYS   A CA   1 
ATOM   3997 C C    A LYS   A 1 163 ? 4.502  -9.060  -0.037  0.52 19.57 ?  163 LYS   A C    1 
ATOM   3998 C C    B LYS   A 1 163 ? 4.617  -9.303  -0.831  0.48 22.31 ?  163 LYS   A C    1 
ATOM   3999 O O    A LYS   A 1 163 ? 4.332  -10.191 -0.505  0.52 19.63 ?  163 LYS   A O    1 
ATOM   4000 O O    B LYS   A 1 163 ? 4.371  -10.425 -1.291  0.48 22.16 ?  163 LYS   A O    1 
ATOM   4001 C CB   A LYS   A 1 163 ? 3.652  -7.080  -1.332  0.52 23.96 ?  163 LYS   A CB   1 
ATOM   4002 C CB   B LYS   A 1 163 ? 4.160  -7.211  -2.155  0.48 28.44 ?  163 LYS   A CB   1 
ATOM   4003 C CG   A LYS   A 1 163 ? 3.768  -7.807  -2.662  0.52 27.51 ?  163 LYS   A CG   1 
ATOM   4004 C CG   B LYS   A 1 163 ? 3.214  -7.046  -3.350  0.48 31.69 ?  163 LYS   A CG   1 
ATOM   4005 C CD   A LYS   A 1 163 ? 4.249  -6.876  -3.759  0.52 31.36 ?  163 LYS   A CD   1 
ATOM   4006 C CD   B LYS   A 1 163 ? 3.938  -7.217  -4.690  0.48 34.63 ?  163 LYS   A CD   1 
ATOM   4007 C CE   A LYS   A 1 163 ? 4.126  -7.527  -5.126  0.52 34.20 ?  163 LYS   A CE   1 
ATOM   4008 C CE   B LYS   A 1 163 ? 4.792  -6.005  -5.055  0.48 36.63 ?  163 LYS   A CE   1 
ATOM   4009 N NZ   A LYS   A 1 163 ? 4.801  -6.729  -6.185  0.52 35.68 ?  163 LYS   A NZ   1 
ATOM   4010 N NZ   B LYS   A 1 163 ? 5.594  -6.235  -6.298  0.48 37.72 ?  163 LYS   A NZ   1 
ATOM   4011 H H    A LYS   A 1 163 ? 3.563  -6.397  1.016   0.52 23.56 ?  163 LYS   A H    1 
ATOM   4012 H H    B LYS   A 1 163 ? 3.694  -6.557  0.141   0.48 28.58 ?  163 LYS   A H    1 
ATOM   4013 H HA   A LYS   A 1 163 ? 2.559  -8.457  -0.284  0.52 24.92 ?  163 LYS   A HA   1 
ATOM   4014 H HA   B LYS   A 1 163 ? 2.800  -8.507  -1.326  0.48 29.72 ?  163 LYS   A HA   1 
ATOM   4015 H HB2  A LYS   A 1 163 ? 2.910  -6.452  -1.403  0.52 28.75 ?  163 LYS   A HB2  1 
ATOM   4016 H HB2  B LYS   A 1 163 ? 4.307  -6.324  -1.784  0.48 34.12 ?  163 LYS   A HB2  1 
ATOM   4017 H HB3  A LYS   A 1 163 ? 4.476  -6.592  -1.186  0.52 28.75 ?  163 LYS   A HB3  1 
ATOM   4018 H HB3  B LYS   A 1 163 ? 4.999  -7.558  -2.496  0.48 34.12 ?  163 LYS   A HB3  1 
ATOM   4019 H HG2  A LYS   A 1 163 ? 4.408  -8.532  -2.584  0.52 33.02 ?  163 LYS   A HG2  1 
ATOM   4020 H HG2  B LYS   A 1 163 ? 2.513  -7.712  -3.304  0.48 38.02 ?  163 LYS   A HG2  1 
ATOM   4021 H HG3  A LYS   A 1 163 ? 2.898  -8.154  -2.914  0.52 33.02 ?  163 LYS   A HG3  1 
ATOM   4022 H HG3  B LYS   A 1 163 ? 2.829  -6.154  -3.330  0.48 38.02 ?  163 LYS   A HG3  1 
ATOM   4023 H HD2  A LYS   A 1 163 ? 3.709  -6.071  -3.755  0.52 37.63 ?  163 LYS   A HD2  1 
ATOM   4024 H HD2  B LYS   A 1 163 ? 4.522  -7.991  -4.644  0.48 41.55 ?  163 LYS   A HD2  1 
ATOM   4025 H HD3  A LYS   A 1 163 ? 5.182  -6.657  -3.607  0.52 37.63 ?  163 LYS   A HD3  1 
ATOM   4026 H HD3  B LYS   A 1 163 ? 3.281  -7.340  -5.393  0.48 41.55 ?  163 LYS   A HD3  1 
ATOM   4027 H HE2  A LYS   A 1 163 ? 4.525  -8.410  -5.099  0.52 41.04 ?  163 LYS   A HE2  1 
ATOM   4028 H HE2  B LYS   A 1 163 ? 4.213  -5.241  -5.210  0.48 43.95 ?  163 LYS   A HE2  1 
ATOM   4029 H HE3  A LYS   A 1 163 ? 3.189  -7.597  -5.358  0.52 41.04 ?  163 LYS   A HE3  1 
ATOM   4030 H HE3  B LYS   A 1 163 ? 5.408  -5.817  -4.332  0.48 43.95 ?  163 LYS   A HE3  1 
ATOM   4031 H HZ1  A LYS   A 1 163 ? 4.714  -7.132  -6.973  0.52 42.82 ?  163 LYS   A HZ1  1 
ATOM   4032 H HZ1  B LYS   A 1 163 ? 6.080  -5.513  -6.487  0.48 45.27 ?  163 LYS   A HZ1  1 
ATOM   4033 H HZ2  A LYS   A 1 163 ? 4.435  -5.918  -6.233  0.52 42.82 ?  163 LYS   A HZ2  1 
ATOM   4034 H HZ2  B LYS   A 1 163 ? 6.140  -6.929  -6.185  0.48 45.27 ?  163 LYS   A HZ2  1 
ATOM   4035 H HZ3  A LYS   A 1 163 ? 5.667  -6.643  -5.998  0.52 42.82 ?  163 LYS   A HZ3  1 
ATOM   4036 H HZ3  B LYS   A 1 163 ? 5.051  -6.404  -6.985  0.48 45.27 ?  163 LYS   A HZ3  1 
ATOM   4037 N N    A LEU   A 1 164 ? 5.638  -8.702  0.563   0.52 17.18 ?  164 LEU   A N    1 
ATOM   4038 N N    B LEU   A 1 164 ? 5.718  -9.051  -0.119  0.48 20.78 ?  164 LEU   A N    1 
ATOM   4039 C CA   A LEU   A 1 164 ? 6.721  -9.666  0.739   0.52 15.81 ?  164 LEU   A CA   1 
ATOM   4040 C CA   B LEU   A 1 164 ? 6.756  -10.065 0.056   0.48 20.01 ?  164 LEU   A CA   1 
ATOM   4041 C C    A LEU   A 1 164 ? 6.271  -10.841 1.595   0.52 16.21 ?  164 LEU   A C    1 
ATOM   4042 C C    B LEU   A 1 164 ? 6.247  -11.246 0.867   0.48 20.41 ?  164 LEU   A C    1 
ATOM   4043 O O    A LEU   A 1 164 ? 6.566  -12.002 1.285   0.52 15.70 ?  164 LEU   A O    1 
ATOM   4044 O O    B LEU   A 1 164 ? 6.511  -12.404 0.522   0.48 20.71 ?  164 LEU   A O    1 
ATOM   4045 C CB   A LEU   A 1 164 ? 7.911  -8.969  1.390   0.52 15.58 ?  164 LEU   A CB   1 
ATOM   4046 C CB   B LEU   A 1 164 ? 7.967  -9.442  0.746   0.48 18.95 ?  164 LEU   A CB   1 
ATOM   4047 C CG   A LEU   A 1 164 ? 8.723  -8.004  0.524   0.52 15.66 ?  164 LEU   A CG   1 
ATOM   4048 C CG   B LEU   A 1 164 ? 8.782  -8.440  -0.071  0.48 18.94 ?  164 LEU   A CG   1 
ATOM   4049 C CD1  A LEU   A 1 164 ? 9.661  -7.185  1.396   0.52 15.46 ?  164 LEU   A CD1  1 
ATOM   4050 C CD1  B LEU   A 1 164 ? 9.781  -7.715  0.821   0.48 18.53 ?  164 LEU   A CD1  1 
ATOM   4051 C CD2  A LEU   A 1 164 ? 9.507  -8.763  -0.536  0.52 15.63 ?  164 LEU   A CD2  1 
ATOM   4052 C CD2  B LEU   A 1 164 ? 9.500  -9.142  -1.209  0.48 19.68 ?  164 LEU   A CD2  1 
ATOM   4053 H H    A LEU   A 1 164 ? 5.802  -7.910  0.872   0.52 20.62 ?  164 LEU   A H    1 
ATOM   4054 H H    B LEU   A 1 164 ? 5.883  -8.308  0.272   0.48 24.93 ?  164 LEU   A H    1 
ATOM   4055 H HA   A LEU   A 1 164 ? 6.992  -9.998  -0.129  0.52 18.97 ?  164 LEU   A HA   1 
ATOM   4056 H HA   B LEU   A 1 164 ? 7.034  -10.395 -0.811  0.48 24.01 ?  164 LEU   A HA   1 
ATOM   4057 H HB2  A LEU   A 1 164 ? 7.583  -8.460  2.149   0.52 18.69 ?  164 LEU   A HB2  1 
ATOM   4058 H HB2  B LEU   A 1 164 ? 7.659  -8.982  1.541   0.48 22.75 ?  164 LEU   A HB2  1 
ATOM   4059 H HB3  A LEU   A 1 164 ? 8.520  -9.651  1.701   0.52 18.69 ?  164 LEU   A HB3  1 
ATOM   4060 H HB3  B LEU   A 1 164 ? 8.569  -10.158 1.003   0.48 22.75 ?  164 LEU   A HB3  1 
ATOM   4061 H HG   A LEU   A 1 164 ? 8.120  -7.390  0.075   0.52 18.79 ?  164 LEU   A HG   1 
ATOM   4062 H HG   B LEU   A 1 164 ? 8.183  -7.778  -0.451  0.48 22.73 ?  164 LEU   A HG   1 
ATOM   4063 H HD11 A LEU   A 1 164 ? 10.169 -6.579  0.834   0.52 18.56 ?  164 LEU   A HD11 1 
ATOM   4064 H HD11 B LEU   A 1 164 ? 10.287 -7.086  0.284   0.48 22.23 ?  164 LEU   A HD11 1 
ATOM   4065 H HD12 A LEU   A 1 164 ? 9.138  -6.679  2.038   0.52 18.56 ?  164 LEU   A HD12 1 
ATOM   4066 H HD12 B LEU   A 1 164 ? 9.299  -7.242  1.519   0.48 22.23 ?  164 LEU   A HD12 1 
ATOM   4067 H HD13 A LEU   A 1 164 ? 10.264 -7.786  1.862   0.52 18.56 ?  164 LEU   A HD13 1 
ATOM   4068 H HD13 B LEU   A 1 164 ? 10.381 -8.367  1.219   0.48 22.23 ?  164 LEU   A HD13 1 
ATOM   4069 H HD21 A LEU   A 1 164 ? 10.058 -8.136  -1.032  0.52 18.75 ?  164 LEU   A HD21 1 
ATOM   4070 H HD21 B LEU   A 1 164 ? 10.082 -8.508  -1.653  0.48 23.62 ?  164 LEU   A HD21 1 
ATOM   4071 H HD22 A LEU   A 1 164 ? 10.069 -9.423  -0.101  0.52 18.75 ?  164 LEU   A HD22 1 
ATOM   4072 H HD22 B LEU   A 1 164 ? 10.022 -9.875  -0.846  0.48 23.62 ?  164 LEU   A HD22 1 
ATOM   4073 H HD23 A LEU   A 1 164 ? 8.885  -9.202  -1.137  0.52 18.75 ?  164 LEU   A HD23 1 
ATOM   4074 H HD23 B LEU   A 1 164 ? 8.841  -9.484  -1.834  0.48 23.62 ?  164 LEU   A HD23 1 
ATOM   4075 N N    A VAL   A 1 165 ? 5.557  -10.555 2.681   0.52 16.41 ?  165 VAL   A N    1 
ATOM   4076 N N    B VAL   A 1 165 ? 5.535  -10.973 1.960   0.48 21.11 ?  165 VAL   A N    1 
ATOM   4077 C CA   A VAL   A 1 165 ? 5.086  -11.610 3.569   0.52 16.34 ?  165 VAL   A CA   1 
ATOM   4078 C CA   B VAL   A 1 165 ? 4.969  -12.047 2.769   0.48 22.55 ?  165 VAL   A CA   1 
ATOM   4079 C C    A VAL   A 1 165 ? 4.066  -12.494 2.858   0.52 17.37 ?  165 VAL   A C    1 
ATOM   4080 C C    B VAL   A 1 165 ? 3.954  -12.845 1.962   0.48 23.45 ?  165 VAL   A C    1 
ATOM   4081 O O    A VAL   A 1 165 ? 4.192  -13.724 2.836   0.52 17.56 ?  165 VAL   A O    1 
ATOM   4082 O O    B VAL   A 1 165 ? 3.930  -14.082 2.014   0.48 23.31 ?  165 VAL   A O    1 
ATOM   4083 C CB   A VAL   A 1 165 ? 4.525  -10.989 4.861   0.52 17.42 ?  165 VAL   A CB   1 
ATOM   4084 C CB   B VAL   A 1 165 ? 4.347  -11.470 4.053   0.48 23.38 ?  165 VAL   A CB   1 
ATOM   4085 C CG1  A VAL   A 1 165 ? 3.760  -12.020 5.677   0.52 17.64 ?  165 VAL   A CG1  1 
ATOM   4086 C CG1  B VAL   A 1 165 ? 3.634  -12.569 4.823   0.48 23.68 ?  165 VAL   A CG1  1 
ATOM   4087 C CG2  A VAL   A 1 165 ? 5.658  -10.376 5.681   0.52 18.23 ?  165 VAL   A CG2  1 
ATOM   4088 C CG2  B VAL   A 1 165 ? 5.414  -10.807 4.907   0.48 23.44 ?  165 VAL   A CG2  1 
ATOM   4089 H H    A VAL   A 1 165 ? 5.324  -9.761  2.921   0.52 19.69 ?  165 VAL   A H    1 
ATOM   4090 H H    B VAL   A 1 165 ? 5.370  -10.182 2.252   0.48 25.33 ?  165 VAL   A H    1 
ATOM   4091 H HA   A VAL   A 1 165 ? 5.834  -12.169 3.815   0.52 19.61 ?  165 VAL   A HA   1 
ATOM   4092 H HA   B VAL   A 1 165 ? 5.679  -12.650 3.030   0.48 27.06 ?  165 VAL   A HA   1 
ATOM   4093 H HB   A VAL   A 1 165 ? 3.908  -10.276 4.633   0.52 20.91 ?  165 VAL   A HB   1 
ATOM   4094 H HB   B VAL   A 1 165 ? 3.689  -10.798 3.812   0.48 28.06 ?  165 VAL   A HB   1 
ATOM   4095 H HG11 A VAL   A 1 165 ? 3.653  -11.691 6.586   0.52 21.17 ?  165 VAL   A HG11 1 
ATOM   4096 H HG11 B VAL   A 1 165 ? 3.469  -12.259 5.725   0.48 28.42 ?  165 VAL   A HG11 1 
ATOM   4097 H HG12 A VAL   A 1 165 ? 2.885  -12.158 5.277   0.52 21.17 ?  165 VAL   A HG12 1 
ATOM   4098 H HG12 B VAL   A 1 165 ? 2.794  -12.773 4.383   0.48 28.42 ?  165 VAL   A HG12 1 
ATOM   4099 H HG13 A VAL   A 1 165 ? 4.257  -12.851 5.686   0.52 21.17 ?  165 VAL   A HG13 1 
ATOM   4100 H HG13 B VAL   A 1 165 ? 4.200  -13.357 4.841   0.48 28.42 ?  165 VAL   A HG13 1 
ATOM   4101 H HG21 A VAL   A 1 165 ? 5.300  -10.059 6.526   0.52 21.88 ?  165 VAL   A HG21 1 
ATOM   4102 H HG21 B VAL   A 1 165 ? 4.992  -10.398 5.677   0.48 28.12 ?  165 VAL   A HG21 1 
ATOM   4103 H HG22 A VAL   A 1 165 ? 6.333  -11.052 5.841   0.52 21.88 ?  165 VAL   A HG22 1 
ATOM   4104 H HG22 B VAL   A 1 165 ? 6.049  -11.481 5.196   0.48 28.12 ?  165 VAL   A HG22 1 
ATOM   4105 H HG23 A VAL   A 1 165 ? 6.039  -9.635  5.185   0.52 21.88 ?  165 VAL   A HG23 1 
ATOM   4106 H HG23 B VAL   A 1 165 ? 5.869  -10.131 4.380   0.48 28.12 ?  165 VAL   A HG23 1 
ATOM   4107 N N    A SER   A 1 166 ? 3.055  -11.879 2.245   0.52 18.19 ?  166 SER   A N    1 
ATOM   4108 N N    B SER   A 1 166 ? 3.107  -12.150 1.199   0.48 25.32 ?  166 SER   A N    1 
ATOM   4109 C CA   A SER   A 1 166 ? 1.953  -12.642 1.667   0.52 19.49 ?  166 SER   A CA   1 
ATOM   4110 C CA   B SER   A 1 166 ? 2.006  -12.803 0.498   0.48 27.26 ?  166 SER   A CA   1 
ATOM   4111 C C    A SER   A 1 166 ? 2.374  -13.462 0.455   0.52 19.89 ?  166 SER   A C    1 
ATOM   4112 C C    B SER   A 1 166 ? 2.492  -13.677 -0.649  0.48 28.86 ?  166 SER   A C    1 
ATOM   4113 O O    A SER   A 1 166 ? 1.665  -14.408 0.092   0.52 21.53 ?  166 SER   A O    1 
ATOM   4114 O O    B SER   A 1 166 ? 1.858  -14.693 -0.960  0.48 28.81 ?  166 SER   A O    1 
ATOM   4115 C CB   A SER   A 1 166 ? 0.816  -11.703 1.255   0.52 21.16 ?  166 SER   A CB   1 
ATOM   4116 C CB   B SER   A 1 166 ? 1.041  -11.744 -0.036  0.48 27.64 ?  166 SER   A CB   1 
ATOM   4117 O OG   A SER   A 1 166 ? 0.314  -10.974 2.362   0.52 23.12 ?  166 SER   A OG   1 
ATOM   4118 O OG   B SER   A 1 166 ? 0.704  -10.816 0.977   0.48 28.23 ?  166 SER   A OG   1 
ATOM   4119 H H    A SER   A 1 166 ? 2.971  -11.028 2.167   0.52 21.83 ?  166 SER   A H    1 
ATOM   4120 H H    B SER   A 1 166 ? 3.147  -11.301 1.073   0.48 30.38 ?  166 SER   A H    1 
ATOM   4121 H HA   A SER   A 1 166 ? 1.596  -13.250 2.337   0.52 23.39 ?  166 SER   A HA   1 
ATOM   4122 H HA   B SER   A 1 166 ? 1.519  -13.368 1.115   0.48 32.71 ?  166 SER   A HA   1 
ATOM   4123 H HB2  A SER   A 1 166 ? 1.151  -11.077 0.593   0.52 25.39 ?  166 SER   A HB2  1 
ATOM   4124 H HB2  B SER   A 1 166 ? 1.461  -11.269 -0.771  0.48 33.17 ?  166 SER   A HB2  1 
ATOM   4125 H HB3  A SER   A 1 166 ? 0.092  -12.227 0.876   0.52 25.39 ?  166 SER   A HB3  1 
ATOM   4126 H HB3  B SER   A 1 166 ? 0.228  -12.177 -0.346  0.48 33.17 ?  166 SER   A HB3  1 
ATOM   4127 H HG   A SER   A 1 166 ? 0.928  -10.505 2.701   0.52 27.74 ?  166 SER   A HG   1 
ATOM   4128 H HG   B SER   A 1 166 ? 1.389  -10.395 1.222   0.48 33.88 ?  166 SER   A HG   1 
ATOM   4129 N N    A SER   A 1 167 ? 3.486  -13.117 -0.192  0.52 19.53 ?  167 SER   A N    1 
ATOM   4130 N N    B SER   A 1 167 ? 3.597  -13.303 -1.291  0.48 30.11 ?  167 SER   A N    1 
ATOM   4131 C CA   A SER   A 1 167 ? 3.951  -13.851 -1.359  0.52 19.90 ?  167 SER   A CA   1 
ATOM   4132 C CA   B SER   A 1 167 ? 4.084  -13.998 -2.475  0.48 31.61 ?  167 SER   A CA   1 
ATOM   4133 C C    A SER   A 1 167 ? 5.104  -14.796 -1.052  0.52 20.03 ?  167 SER   A C    1 
ATOM   4134 C C    B SER   A 1 167 ? 5.294  -14.875 -2.188  0.48 32.40 ?  167 SER   A C    1 
ATOM   4135 O O    A SER   A 1 167 ? 5.579  -15.483 -1.965  0.52 20.65 ?  167 SER   A O    1 
ATOM   4136 O O    B SER   A 1 167 ? 5.895  -15.409 -3.126  0.48 32.86 ?  167 SER   A O    1 
ATOM   4137 C CB   A SER   A 1 167 ? 4.377  -12.881 -2.468  0.52 20.58 ?  167 SER   A CB   1 
ATOM   4138 C CB   B SER   A 1 167 ? 4.413  -12.993 -3.583  0.48 31.84 ?  167 SER   A CB   1 
ATOM   4139 O OG   A SER   A 1 167 ? 5.418  -12.019 -2.042  0.52 21.31 ?  167 SER   A OG   1 
ATOM   4140 O OG   B SER   A 1 167 ? 5.545  -12.212 -3.241  0.48 32.19 ?  167 SER   A OG   1 
ATOM   4141 H H    A SER   A 1 167 ? 3.977  -12.446 0.023   0.52 23.43 ?  167 SER   A H    1 
ATOM   4142 H H    B SER   A 1 167 ? 4.092  -12.639 -1.051  0.48 36.13 ?  167 SER   A H    1 
ATOM   4143 H HA   A SER   A 1 167 ? 3.212  -14.383 -1.700  0.52 23.87 ?  167 SER   A HA   1 
ATOM   4144 H HA   B SER   A 1 167 ? 3.386  -14.576 -2.808  0.48 37.93 ?  167 SER   A HA   1 
ATOM   4145 H HB2  A SER   A 1 167 ? 4.688  -13.403 -3.225  0.52 24.70 ?  167 SER   A HB2  1 
ATOM   4146 H HB2  B SER   A 1 167 ? 4.598  -13.475 -4.407  0.48 38.21 ?  167 SER   A HB2  1 
ATOM   4147 H HB3  A SER   A 1 167 ? 3.612  -12.347 -2.723  0.52 24.70 ?  167 SER   A HB3  1 
ATOM   4148 H HB3  B SER   A 1 167 ? 3.649  -12.404 -3.716  0.48 38.21 ?  167 SER   A HB3  1 
ATOM   4149 H HG   A SER   A 1 167 ? 5.157  -11.576 -1.374  0.52 25.57 ?  167 SER   A HG   1 
ATOM   4150 H HG   B SER   A 1 167 ? 5.395  -11.782 -2.537  0.48 38.62 ?  167 SER   A HG   1 
ATOM   4151 N N    A PHE   A 1 168 ? 5.567  -14.851 0.194   0.52 19.60 ?  168 PHE   A N    1 
ATOM   4152 N N    B PHE   A 1 168 ? 5.659  -15.050 -0.921  0.48 32.50 ?  168 PHE   A N    1 
ATOM   4153 C CA   A PHE   A 1 168 ? 6.746  -15.647 0.506   0.52 20.02 ?  168 PHE   A CA   1 
ATOM   4154 C CA   B PHE   A 1 168 ? 6.868  -15.794 -0.599  0.48 32.58 ?  168 PHE   A CA   1 
ATOM   4155 C C    A PHE   A 1 168 ? 6.425  -17.129 0.408   0.52 22.05 ?  168 PHE   A C    1 
ATOM   4156 C C    B PHE   A 1 168 ? 6.685  -17.269 -0.934  0.48 34.65 ?  168 PHE   A C    1 
ATOM   4157 O O    A PHE   A 1 168 ? 5.424  -17.598 0.957   0.52 23.66 ?  168 PHE   A O    1 
ATOM   4158 O O    B PHE   A 1 168 ? 5.689  -17.888 -0.545  0.48 35.27 ?  168 PHE   A O    1 
ATOM   4159 C CB   A PHE   A 1 168 ? 7.263  -15.325 1.905   0.52 18.45 ?  168 PHE   A CB   1 
ATOM   4160 C CB   B PHE   A 1 168 ? 7.221  -15.626 0.876   0.48 30.65 ?  168 PHE   A CB   1 
ATOM   4161 C CG   A PHE   A 1 168 ? 8.531  -16.054 2.249   0.52 17.33 ?  168 PHE   A CG   1 
ATOM   4162 C CG   B PHE   A 1 168 ? 8.531  -16.252 1.256   0.48 28.96 ?  168 PHE   A CG   1 
ATOM   4163 C CD1  A PHE   A 1 168 ? 9.729  -15.684 1.668   0.52 17.10 ?  168 PHE   A CD1  1 
ATOM   4164 C CD1  B PHE   A 1 168 ? 9.710  -15.826 0.668   0.48 28.15 ?  168 PHE   A CD1  1 
ATOM   4165 C CD2  A PHE   A 1 168 ? 8.526  -17.125 3.130   0.52 16.06 ?  168 PHE   A CD2  1 
ATOM   4166 C CD2  B PHE   A 1 168 ? 8.584  -17.264 2.199   0.48 28.03 ?  168 PHE   A CD2  1 
ATOM   4167 C CE1  A PHE   A 1 168 ? 10.899 -16.351 1.972   0.52 16.78 ?  168 PHE   A CE1  1 
ATOM   4168 C CE1  B PHE   A 1 168 ? 10.918 -16.400 1.012   0.48 27.42 ?  168 PHE   A CE1  1 
ATOM   4169 C CE2  A PHE   A 1 168 ? 9.700  -17.795 3.441   0.52 16.15 ?  168 PHE   A CE2  1 
ATOM   4170 C CE2  B PHE   A 1 168 ? 9.790  -17.842 2.547   0.48 27.37 ?  168 PHE   A CE2  1 
ATOM   4171 C CZ   A PHE   A 1 168 ? 10.883 -17.409 2.857   0.52 16.78 ?  168 PHE   A CZ   1 
ATOM   4172 C CZ   B PHE   A 1 168 ? 10.959 -17.409 1.953   0.48 27.11 ?  168 PHE   A CZ   1 
ATOM   4173 H H    A PHE   A 1 168 ? 5.225  -14.438 0.871   0.52 23.52 ?  168 PHE   A H    1 
ATOM   4174 H H    B PHE   A 1 168 ? 5.225  -14.753 -0.240  0.48 39.00 ?  168 PHE   A H    1 
ATOM   4175 H HA   A PHE   A 1 168 ? 7.444  -15.446 -0.132  0.52 24.03 ?  168 PHE   A HA   1 
ATOM   4176 H HA   B PHE   A 1 168 ? 7.602  -15.448 -1.131  0.48 39.09 ?  168 PHE   A HA   1 
ATOM   4177 H HB2  A PHE   A 1 168 ? 7.442  -14.373 1.963   0.52 22.14 ?  168 PHE   A HB2  1 
ATOM   4178 H HB2  B PHE   A 1 168 ? 7.273  -14.680 1.080   0.48 36.78 ?  168 PHE   A HB2  1 
ATOM   4179 H HB3  A PHE   A 1 168 ? 6.590  -15.575 2.558   0.52 22.14 ?  168 PHE   A HB3  1 
ATOM   4180 H HB3  B PHE   A 1 168 ? 6.527  -16.041 1.412   0.48 36.78 ?  168 PHE   A HB3  1 
ATOM   4181 H HD1  A PHE   A 1 168 ? 9.754  -14.969 1.074   0.52 20.53 ?  168 PHE   A HD1  1 
ATOM   4182 H HD1  B PHE   A 1 168 ? 9.689  -15.146 0.031   0.48 33.78 ?  168 PHE   A HD1  1 
ATOM   4183 H HD2  A PHE   A 1 168 ? 7.730  -17.389 3.530   0.52 19.27 ?  168 PHE   A HD2  1 
ATOM   4184 H HD2  B PHE   A 1 168 ? 7.799  -17.559 2.599   0.48 33.63 ?  168 PHE   A HD2  1 
ATOM   4185 H HE1  A PHE   A 1 168 ? 11.704 -16.088 1.580   0.52 20.13 ?  168 PHE   A HE1  1 
ATOM   4186 H HE1  B PHE   A 1 168 ? 11.705 -16.104 0.610   0.48 32.90 ?  168 PHE   A HE1  1 
ATOM   4187 H HE2  A PHE   A 1 168 ? 9.684  -18.509 4.038   0.52 19.37 ?  168 PHE   A HE2  1 
ATOM   4188 H HE2  B PHE   A 1 168 ? 9.814  -18.521 3.181   0.48 32.84 ?  168 PHE   A HE2  1 
ATOM   4189 H HZ   A PHE   A 1 168 ? 11.674 -17.861 3.065   0.52 20.14 ?  168 PHE   A HZ   1 
ATOM   4190 H HZ   B PHE   A 1 168 ? 11.772 -17.795 2.187   0.48 32.53 ?  168 PHE   A HZ   1 
ATOM   4191 N N    A LEU   A 1 169 ? 7.280  -17.869 -0.289  0.52 23.49 ?  169 LEU   A N    1 
ATOM   4192 N N    B LEU   A 1 169 ? 7.654  -17.827 -1.655  0.48 35.78 ?  169 LEU   A N    1 
ATOM   4193 C CA   A LEU   A 1 169 ? 7.091  -19.303 -0.434  0.52 26.36 ?  169 LEU   A CA   1 
ATOM   4194 C CA   B LEU   A 1 169 ? 7.591  -19.212 -2.108  0.48 36.58 ?  169 LEU   A CA   1 
ATOM   4195 C C    A LEU   A 1 169 ? 7.937  -20.043 0.593   0.52 26.84 ?  169 LEU   A C    1 
ATOM   4196 C C    B LEU   A 1 169 ? 8.670  -20.052 -1.433  0.48 37.34 ?  169 LEU   A C    1 
ATOM   4197 O O    A LEU   A 1 169 ? 7.393  -20.585 1.555   0.52 26.92 ?  169 LEU   A O    1 
ATOM   4198 O O    B LEU   A 1 169 ? 8.963  -19.893 -0.248  0.48 37.55 ?  169 LEU   A O    1 
ATOM   4199 C CB   A LEU   A 1 169 ? 7.433  -19.744 -1.861  0.52 28.33 ?  169 LEU   A CB   1 
ATOM   4200 C CB   B LEU   A 1 169 ? 7.765  -19.285 -3.627  0.48 36.78 ?  169 LEU   A CB   1 
ATOM   4201 C CG   A LEU   A 1 169 ? 7.014  -21.159 -2.271  0.52 30.14 ?  169 LEU   A CG   1 
ATOM   4202 C CG   B LEU   A 1 169 ? 6.710  -18.570 -4.474  0.48 36.77 ?  169 LEU   A CG   1 
ATOM   4203 C CD1  A LEU   A 1 169 ? 5.553  -21.412 -1.935  0.52 30.90 ?  169 LEU   A CD1  1 
ATOM   4204 C CD1  B LEU   A 1 169 ? 6.895  -18.900 -5.950  0.48 36.66 ?  169 LEU   A CD1  1 
ATOM   4205 C CD2  A LEU   A 1 169 ? 7.261  -21.372 -3.757  0.52 30.52 ?  169 LEU   A CD2  1 
ATOM   4206 C CD2  B LEU   A 1 169 ? 5.314  -18.941 -4.008  0.48 36.91 ?  169 LEU   A CD2  1 
ATOM   4207 O OXT  A LEU   A 1 169 ? 9.167  -20.100 0.507   0.52 26.78 -1 169 LEU   A OXT  1 
ATOM   4208 O OXT  B LEU   A 1 169 ? 9.281  -20.915 -2.065  0.48 37.93 -1 169 LEU   A OXT  1 
ATOM   4209 H H    A LEU   A 1 169 ? 7.972  -17.561 -0.691  0.52 28.18 ?  169 LEU   A H    1 
ATOM   4210 H H    B LEU   A 1 169 ? 8.372  -17.418 -1.893  0.48 42.94 ?  169 LEU   A H    1 
ATOM   4211 H HA   A LEU   A 1 169 ? 6.167  -19.521 -0.255  0.52 31.63 ?  169 LEU   A HA   1 
ATOM   4212 H HA   B LEU   A 1 169 ? 6.723  -19.583 -1.883  0.48 43.89 ?  169 LEU   A HA   1 
ATOM   4213 H HB2  A LEU   A 1 169 ? 6.999  -19.132 -2.477  0.52 34.00 ?  169 LEU   A HB2  1 
ATOM   4214 H HB2  B LEU   A 1 169 ? 8.624  -18.896 -3.852  0.48 44.14 ?  169 LEU   A HB2  1 
ATOM   4215 H HB3  A LEU   A 1 169 ? 8.392  -19.687 -1.976  0.52 34.00 ?  169 LEU   A HB3  1 
ATOM   4216 H HB3  B LEU   A 1 169 ? 7.757  -20.218 -3.888  0.48 44.14 ?  169 LEU   A HB3  1 
ATOM   4217 H HG   A LEU   A 1 169 ? 7.552  -21.804 -1.784  0.52 36.16 ?  169 LEU   A HG   1 
ATOM   4218 H HG   B LEU   A 1 169 ? 6.817  -17.612 -4.369  0.48 44.12 ?  169 LEU   A HG   1 
ATOM   4219 H HD11 A LEU   A 1 169 ? 5.256  -22.209 -2.400  0.52 37.08 ?  169 LEU   A HD11 1 
ATOM   4220 H HD11 B LEU   A 1 169 ? 6.219  -18.432 -6.465  0.48 43.99 ?  169 LEU   A HD11 1 
ATOM   4221 H HD12 A LEU   A 1 169 ? 5.467  -21.535 -0.977  0.52 37.08 ?  169 LEU   A HD12 1 
ATOM   4222 H HD12 B LEU   A 1 169 ? 7.779  -18.615 -6.229  0.48 43.99 ?  169 LEU   A HD12 1 
ATOM   4223 H HD13 A LEU   A 1 169 ? 5.029  -20.647 -2.221  0.52 37.08 ?  169 LEU   A HD13 1 
ATOM   4224 H HD13 B LEU   A 1 169 ? 6.801  -19.858 -6.073  0.48 43.99 ?  169 LEU   A HD13 1 
ATOM   4225 H HD21 A LEU   A 1 169 ? 6.999  -22.275 -3.996  0.52 36.62 ?  169 LEU   A HD21 1 
ATOM   4226 H HD21 B LEU   A 1 169 ? 4.672  -18.645 -4.669  0.48 44.30 ?  169 LEU   A HD21 1 
ATOM   4227 H HD22 A LEU   A 1 169 ? 6.733  -20.731 -4.259  0.52 36.62 ?  169 LEU   A HD22 1 
ATOM   4228 H HD22 B LEU   A 1 169 ? 5.265  -19.905 -3.904  0.48 44.30 ?  169 LEU   A HD22 1 
ATOM   4229 H HD23 A LEU   A 1 169 ? 8.204  -21.241 -3.943  0.52 36.62 ?  169 LEU   A HD23 1 
ATOM   4230 H HD23 B LEU   A 1 169 ? 5.141  -18.508 -3.157  0.48 44.30 ?  169 LEU   A HD23 1 
ATOM   4231 N N    A SER   B 1 1   ? 50.932 -9.274  -23.673 0.52 27.97 ?  1   SER   B N    1 
ATOM   4232 N N    B SER   B 1 1   ? 50.950 -9.494  -23.611 0.48 24.97 ?  1   SER   B N    1 
ATOM   4233 C CA   A SER   B 1 1   ? 51.469 -10.337 -22.803 0.52 28.19 ?  1   SER   B CA   1 
ATOM   4234 C CA   B SER   B 1 1   ? 51.414 -10.470 -22.596 0.48 25.29 ?  1   SER   B CA   1 
ATOM   4235 C C    A SER   B 1 1   ? 50.417 -11.408 -22.567 0.52 26.95 ?  1   SER   B C    1 
ATOM   4236 C C    B SER   B 1 1   ? 50.415 -11.618 -22.420 0.48 23.75 ?  1   SER   B C    1 
ATOM   4237 O O    A SER   B 1 1   ? 49.225 -11.218 -22.842 0.52 26.94 ?  1   SER   B O    1 
ATOM   4238 O O    B SER   B 1 1   ? 49.199 -11.458 -22.612 0.48 23.97 ?  1   SER   B O    1 
ATOM   4239 C CB   A SER   B 1 1   ? 51.934 -9.762  -21.469 0.52 28.97 ?  1   SER   B CB   1 
ATOM   4240 C CB   B SER   B 1 1   ? 51.634 -9.775  -21.257 0.48 26.73 ?  1   SER   B CB   1 
ATOM   4241 O OG   A SER   B 1 1   ? 50.841 -9.556  -20.597 0.52 30.59 ?  1   SER   B OG   1 
ATOM   4242 O OG   B SER   B 1 1   ? 50.396 -9.425  -20.663 0.48 28.76 ?  1   SER   B OG   1 
ATOM   4243 H H1   A SER   B 1 1   ? 50.803 -9.605  -24.487 0.52 33.57 ?  1   SER   B H1   1 
ATOM   4244 H H1   B SER   B 1 1   ? 51.599 -9.360  -24.207 0.48 29.97 ?  1   SER   B H1   1 
ATOM   4245 H H2   A SER   B 1 1   ? 50.165 -8.986  -23.338 0.52 33.57 ?  1   SER   B H2   1 
ATOM   4246 H H2   B SER   B 1 1   ? 50.232 -9.817  -24.017 0.48 29.97 ?  1   SER   B H2   1 
ATOM   4247 H H3   A SER   B 1 1   ? 51.519 -8.610  -23.707 0.52 33.57 ?  1   SER   B H3   1 
ATOM   4248 H H3   B SER   B 1 1   ? 50.753 -8.728  -23.208 0.48 29.97 ?  1   SER   B H3   1 
ATOM   4249 H HA   A SER   B 1 1   ? 52.226 -10.741 -23.245 0.52 33.83 ?  1   SER   B HA   1 
ATOM   4250 H HA   B SER   B 1 1   ? 52.264 -10.826 -22.900 0.48 30.34 ?  1   SER   B HA   1 
ATOM   4251 H HB2  A SER   B 1 1   ? 52.539 -10.390 -21.053 0.52 34.77 ?  1   SER   B HB2  1 
ATOM   4252 H HB2  B SER   B 1 1   ? 52.106 -10.383 -20.672 0.48 32.08 ?  1   SER   B HB2  1 
ATOM   4253 H HB3  A SER   B 1 1   ? 52.389 -8.918  -21.631 0.52 34.77 ?  1   SER   B HB3  1 
ATOM   4254 H HB3  B SER   B 1 1   ? 52.161 -8.970  -21.397 0.48 32.08 ?  1   SER   B HB3  1 
ATOM   4255 H HG   A SER   B 1 1   ? 51.107 -9.203  -19.882 0.52 36.71 ?  1   SER   B HG   1 
ATOM   4256 H HG   B SER   B 1 1   ? 50.535 -9.041  -19.927 0.48 34.52 ?  1   SER   B HG   1 
ATOM   4257 N N    A MET   B 1 2   ? 50.879 -12.539 -22.052 0.52 26.02 ?  2   MET   B N    1 
ATOM   4258 N N    B MET   B 1 2   ? 50.942 -12.782 -22.051 0.48 22.56 ?  2   MET   B N    1 
ATOM   4259 C CA   A MET   B 1 2   ? 50.058 -13.725 -21.865 0.52 25.61 ?  2   MET   B CA   1 
ATOM   4260 C CA   B MET   B 1 2   ? 50.156 -14.012 -21.974 0.48 21.57 ?  2   MET   B CA   1 
ATOM   4261 C C    A MET   B 1 2   ? 49.769 -13.871 -20.376 0.52 23.16 ?  2   MET   B C    1 
ATOM   4262 C C    B MET   B 1 2   ? 49.820 -14.359 -20.532 0.48 20.33 ?  2   MET   B C    1 
ATOM   4263 O O    A MET   B 1 2   ? 50.694 -14.051 -19.577 0.52 22.40 ?  2   MET   B O    1 
ATOM   4264 O O    B MET   B 1 2   ? 50.598 -15.021 -19.841 0.48 21.75 ?  2   MET   B O    1 
ATOM   4265 C CB   A MET   B 1 2   ? 50.807 -14.941 -22.412 0.52 29.65 ?  2   MET   B CB   1 
ATOM   4266 C CB   B MET   B 1 2   ? 50.934 -15.145 -22.606 0.48 23.51 ?  2   MET   B CB   1 
ATOM   4267 C CG   A MET   B 1 2   ? 49.961 -16.188 -22.613 0.52 33.74 ?  2   MET   B CG   1 
ATOM   4268 C CG   B MET   B 1 2   ? 50.101 -16.407 -22.844 0.48 25.36 ?  2   MET   B CG   1 
ATOM   4269 S SD   A MET   B 1 2   ? 50.823 -17.403 -23.630 0.52 38.16 ?  2   MET   B SD   1 
ATOM   4270 S SD   B MET   B 1 2   ? 50.849 -17.453 -24.100 0.48 27.29 ?  2   MET   B SD   1 
ATOM   4271 C CE   A MET   B 1 2   ? 51.285 -16.378 -25.020 0.52 38.36 ?  2   MET   B CE   1 
ATOM   4272 C CE   B MET   B 1 2   ? 51.614 -16.182 -25.070 0.48 28.67 ?  2   MET   B CE   1 
ATOM   4273 H H    A MET   B 1 2   ? 51.693 -12.654 -21.791 0.52 31.23 ?  2   MET   B H    1 
ATOM   4274 H H    B MET   B 1 2   ? 51.781 -12.886 -21.872 0.48 27.07 ?  2   MET   B H    1 
ATOM   4275 H HA   A MET   B 1 2   ? 49.228 -13.642 -22.358 0.52 30.73 ?  2   MET   B HA   1 
ATOM   4276 H HA   B MET   B 1 2   ? 49.340 -13.892 -22.479 0.48 25.89 ?  2   MET   B HA   1 
ATOM   4277 H HB2  A MET   B 1 2   ? 51.189 -14.685 -23.268 0.52 35.57 ?  2   MET   B HB2  1 
ATOM   4278 H HB2  B MET   B 1 2   ? 51.282 -14.748 -23.405 0.48 28.21 ?  2   MET   B HB2  1 
ATOM   4279 H HB3  A MET   B 1 2   ? 51.519 -15.182 -21.806 0.52 35.57 ?  2   MET   B HB3  1 
ATOM   4280 H HB3  B MET   B 1 2   ? 51.662 -15.406 -22.037 0.48 28.21 ?  2   MET   B HB3  1 
ATOM   4281 H HG2  A MET   B 1 2   ? 49.778 -16.596 -21.750 0.52 40.49 ?  2   MET   B HG2  1 
ATOM   4282 H HG2  B MET   B 1 2   ? 50.034 -16.910 -22.004 0.48 30.43 ?  2   MET   B HG2  1 
ATOM   4283 H HG3  A MET   B 1 2   ? 49.131 -15.955 -23.057 0.52 40.49 ?  2   MET   B HG3  1 
ATOM   4284 H HG3  B MET   B 1 2   ? 49.214 -16.165 -23.151 0.48 30.43 ?  2   MET   B HG3  1 
ATOM   4285 H HE1  A MET   B 1 2   ? 51.377 -16.930 -25.804 0.52 46.03 ?  2   MET   B HE1  1 
ATOM   4286 H HE1  B MET   B 1 2   ? 51.714 -16.563 -25.917 0.48 34.41 ?  2   MET   B HE1  1 
ATOM   4287 H HE2  A MET   B 1 2   ? 50.593 -15.709 -25.162 0.52 46.03 ?  2   MET   B HE2  1 
ATOM   4288 H HE2  B MET   B 1 2   ? 51.014 -15.421 -25.158 0.48 34.41 ?  2   MET   B HE2  1 
ATOM   4289 H HE3  A MET   B 1 2   ? 52.128 -15.937 -24.818 0.52 46.03 ?  2   MET   B HE3  1 
ATOM   4290 H HE3  B MET   B 1 2   ? 52.482 -15.903 -24.686 0.48 34.41 ?  2   MET   B HE3  1 
ATOM   4291 N N    A VAL   B 1 3   ? 48.497 -13.743 -20.003 0.52 20.44 ?  3   VAL   B N    1 
ATOM   4292 N N    B VAL   B 1 3   ? 48.628 -13.969 -20.105 0.48 18.10 ?  3   VAL   B N    1 
ATOM   4293 C CA   A VAL   B 1 3   ? 48.050 -13.941 -18.629 0.52 19.18 ?  3   VAL   B CA   1 
ATOM   4294 C CA   B VAL   B 1 3   ? 48.191 -14.164 -18.733 0.48 16.54 ?  3   VAL   B CA   1 
ATOM   4295 C C    A VAL   B 1 3   ? 46.793 -14.802 -18.626 0.52 17.66 ?  3   VAL   B C    1 
ATOM   4296 C C    B VAL   B 1 3   ? 46.943 -15.035 -18.732 0.48 15.06 ?  3   VAL   B C    1 
ATOM   4297 O O    A VAL   B 1 3   ? 45.989 -14.771 -19.563 0.52 18.30 ?  3   VAL   B O    1 
ATOM   4298 O O    B VAL   B 1 3   ? 46.268 -15.203 -19.753 0.48 13.71 ?  3   VAL   B O    1 
ATOM   4299 C CB   A VAL   B 1 3   ? 47.800 -12.607 -17.882 0.52 20.23 ?  3   VAL   B CB   1 
ATOM   4300 C CB   B VAL   B 1 3   ? 47.918 -12.825 -18.021 0.48 18.29 ?  3   VAL   B CB   1 
ATOM   4301 C CG1  A VAL   B 1 3   ? 49.087 -11.781 -17.784 0.52 20.90 ?  3   VAL   B CG1  1 
ATOM   4302 C CG1  B VAL   B 1 3   ? 49.193 -11.986 -17.931 0.48 19.47 ?  3   VAL   B CG1  1 
ATOM   4303 C CG2  A VAL   B 1 3   ? 46.686 -11.811 -18.549 0.52 20.57 ?  3   VAL   B CG2  1 
ATOM   4304 C CG2  B VAL   B 1 3   ? 46.814 -12.060 -18.738 0.48 18.84 ?  3   VAL   B CG2  1 
ATOM   4305 H H    A VAL   B 1 3   ? 47.860 -13.533 -20.545 0.52 24.53 ?  3   VAL   B H    1 
ATOM   4306 H H    B VAL   B 1 3   ? 48.037 -13.611 -20.622 0.48 21.73 ?  3   VAL   B H    1 
ATOM   4307 H HA   A VAL   B 1 3   ? 48.733 -14.422 -18.145 0.52 23.01 ?  3   VAL   B HA   1 
ATOM   4308 H HA   B VAL   B 1 3   ? 48.891 -14.632 -18.251 0.48 19.85 ?  3   VAL   B HA   1 
ATOM   4309 H HB   A VAL   B 1 3   ? 47.516 -12.807 -16.976 0.52 24.28 ?  3   VAL   B HB   1 
ATOM   4310 H HB   B VAL   B 1 3   ? 47.622 -13.018 -17.118 0.48 21.95 ?  3   VAL   B HB   1 
ATOM   4311 H HG11 A VAL   B 1 3   ? 48.898 -10.961 -17.303 0.52 25.08 ?  3   VAL   B HG11 1 
ATOM   4312 H HG11 B VAL   B 1 3   ? 48.990 -11.166 -17.458 0.48 23.36 ?  3   VAL   B HG11 1 
ATOM   4313 H HG12 A VAL   B 1 3   ? 49.755 -12.299 -17.308 0.52 25.08 ?  3   VAL   B HG12 1 
ATOM   4314 H HG12 B VAL   B 1 3   ? 49.868 -12.490 -17.449 0.48 23.36 ?  3   VAL   B HG12 1 
ATOM   4315 H HG13 A VAL   B 1 3   ? 49.398 -11.579 -18.678 0.52 25.08 ?  3   VAL   B HG13 1 
ATOM   4316 H HG13 B VAL   B 1 3   ? 49.502 -11.789 -18.827 0.48 23.36 ?  3   VAL   B HG13 1 
ATOM   4317 H HG21 A VAL   B 1 3   ? 46.659 -10.923 -18.162 0.52 24.69 ?  3   VAL   B HG21 1 
ATOM   4318 H HG21 B VAL   B 1 3   ? 46.739 -11.180 -18.341 0.48 22.60 ?  3   VAL   B HG21 1 
ATOM   4319 H HG22 A VAL   B 1 3   ? 46.867 -11.753 -19.499 0.52 24.69 ?  3   VAL   B HG22 1 
ATOM   4320 H HG22 B VAL   B 1 3   ? 47.041 -11.982 -19.678 0.48 22.60 ?  3   VAL   B HG22 1 
ATOM   4321 H HG23 A VAL   B 1 3   ? 45.842 -12.264 -18.399 0.52 24.69 ?  3   VAL   B HG23 1 
ATOM   4322 H HG23 B VAL   B 1 3   ? 45.978 -12.541 -18.638 0.48 22.60 ?  3   VAL   B HG23 1 
ATOM   4323 N N    . ASN   B 1 4   ? 46.633 -15.583 -17.560 1.00 15.70 ?  4   ASN   B N    1 
ATOM   4324 C CA   . ASN   B 1 4   ? 45.482 -16.463 -17.397 1.00 15.49 ?  4   ASN   B CA   1 
ATOM   4325 C C    . ASN   B 1 4   ? 45.402 -17.443 -18.562 1.00 15.71 ?  4   ASN   B C    1 
ATOM   4326 O O    . ASN   B 1 4   ? 44.346 -17.657 -19.149 1.00 16.47 ?  4   ASN   B O    1 
ATOM   4327 C CB   . ASN   B 1 4   ? 44.181 -15.664 -17.252 1.00 14.90 ?  4   ASN   B CB   1 
ATOM   4328 C CG   . ASN   B 1 4   ? 44.125 -14.871 -15.957 1.00 14.34 ?  4   ASN   B CG   1 
ATOM   4329 O OD1  . ASN   B 1 4   ? 44.397 -15.386 -14.875 1.00 14.19 ?  4   ASN   B OD1  1 
ATOM   4330 N ND2  . ASN   B 1 4   ? 43.786 -13.592 -16.071 1.00 16.16 ?  4   ASN   B ND2  1 
ATOM   4331 H H    A ASN   B 1 4   ? 47.200 -15.634 -16.920 0.52 18.84 ?  4   ASN   B H    1 
ATOM   4332 H H    B ASN   B 1 4   ? 47.081 -15.459 -16.842 0.48 18.84 ?  4   ASN   B H    1 
ATOM   4333 H HA   . ASN   B 1 4   ? 45.599 -16.981 -16.589 1.00 18.59 ?  4   ASN   B HA   1 
ATOM   4334 H HB2  . ASN   B 1 4   ? 44.105 -15.041 -17.997 1.00 17.88 ?  4   ASN   B HB2  1 
ATOM   4335 H HB3  . ASN   B 1 4   ? 43.429 -16.279 -17.265 1.00 17.88 ?  4   ASN   B HB3  1 
ATOM   4336 H HD21 . ASN   B 1 4   ? 43.738 -13.093 -15.369 1.00 19.39 ?  4   ASN   B HD21 1 
ATOM   4337 H HD22 . ASN   B 1 4   ? 43.604 -13.254 -16.843 1.00 19.39 ?  4   ASN   B HD22 1 
ATOM   4338 N N    . SER   B 1 5   ? 46.552 -18.027 -18.917 1.00 16.97 ?  5   SER   B N    1 
ATOM   4339 C CA   . SER   B 1 5   ? 46.643 -18.943 -20.054 1.00 18.89 ?  5   SER   B CA   1 
ATOM   4340 C C    . SER   B 1 5   ? 46.633 -20.356 -19.490 1.00 20.91 ?  5   SER   B C    1 
ATOM   4341 O O    . SER   B 1 5   ? 47.667 -20.998 -19.321 1.00 23.37 ?  5   SER   B O    1 
ATOM   4342 C CB   . SER   B 1 5   ? 47.901 -18.664 -20.876 1.00 21.37 ?  5   SER   B CB   1 
ATOM   4343 O OG   . SER   B 1 5   ? 49.076 -18.862 -20.107 1.00 25.31 ?  5   SER   B OG   1 
ATOM   4344 H H    . SER   B 1 5   ? 47.304 -17.925 -18.510 1.00 20.36 ?  5   SER   B H    1 
ATOM   4345 H HA   . SER   B 1 5   ? 45.872 -18.840 -20.628 1.00 22.67 ?  5   SER   B HA   1 
ATOM   4346 H HB2  . SER   B 1 5   ? 47.918 -19.263 -21.643 1.00 25.64 ?  5   SER   B HB2  1 
ATOM   4347 H HB3  . SER   B 1 5   ? 47.872 -17.745 -21.181 1.00 25.64 ?  5   SER   B HB3  1 
ATOM   4348 H HG   . SER   B 1 5   ? 49.128 -19.666 -19.870 1.00 30.37 ?  5   SER   B HG   1 
ATOM   4349 N N    . PHE   B 1 6   ? 45.431 -20.817 -19.153 1.00 22.15 ?  6   PHE   B N    1 
ATOM   4350 C CA   . PHE   B 1 6   ? 45.233 -22.155 -18.615 1.00 21.75 ?  6   PHE   B CA   1 
ATOM   4351 C C    . PHE   B 1 6   ? 45.131 -23.136 -19.773 1.00 27.13 ?  6   PHE   B C    1 
ATOM   4352 O O    . PHE   B 1 6   ? 44.416 -22.882 -20.746 1.00 29.97 ?  6   PHE   B O    1 
ATOM   4353 C CB   . PHE   B 1 6   ? 43.950 -22.197 -17.783 1.00 19.73 ?  6   PHE   B CB   1 
ATOM   4354 C CG   . PHE   B 1 6   ? 43.980 -21.320 -16.563 1.00 18.43 ?  6   PHE   B CG   1 
ATOM   4355 C CD1  . PHE   B 1 6   ? 44.477 -21.791 -15.362 1.00 17.04 ?  6   PHE   B CD1  1 
ATOM   4356 C CD2  . PHE   B 1 6   ? 43.514 -20.016 -16.625 1.00 17.44 ?  6   PHE   B CD2  1 
ATOM   4357 C CE1  . PHE   B 1 6   ? 44.498 -20.979 -14.237 1.00 16.57 ?  6   PHE   B CE1  1 
ATOM   4358 C CE2  . PHE   B 1 6   ? 43.543 -19.193 -15.515 1.00 18.09 ?  6   PHE   B CE2  1 
ATOM   4359 C CZ   . PHE   B 1 6   ? 44.036 -19.666 -14.320 1.00 17.29 ?  6   PHE   B CZ   1 
ATOM   4360 H H    . PHE   B 1 6   ? 44.704 -20.370 -19.239 1.00 26.58 ?  6   PHE   B H    1 
ATOM   4361 H HA   . PHE   B 1 6   ? 45.978 -22.410 -18.056 1.00 26.09 ?  6   PHE   B HA   1 
ATOM   4362 H HB2  . PHE   B 1 6   ? 43.206 -21.908 -18.337 1.00 23.68 ?  6   PHE   B HB2  1 
ATOM   4363 H HB3  . PHE   B 1 6   ? 43.796 -23.110 -17.485 1.00 23.68 ?  6   PHE   B HB3  1 
ATOM   4364 H HD1  . PHE   B 1 6   ? 44.795 -22.667 -15.306 1.00 20.45 ?  6   PHE   B HD1  1 
ATOM   4365 H HD2  . PHE   B 1 6   ? 43.178 -19.692 -17.427 1.00 20.92 ?  6   PHE   B HD2  1 
ATOM   4366 H HE1  . PHE   B 1 6   ? 44.839 -21.302 -13.433 1.00 19.89 ?  6   PHE   B HE1  1 
ATOM   4367 H HE2  . PHE   B 1 6   ? 43.217 -18.325 -15.575 1.00 21.71 ?  6   PHE   B HE2  1 
ATOM   4368 H HZ   . PHE   B 1 6   ? 44.048 -19.123 -13.566 1.00 20.75 ?  6   PHE   B HZ   1 
ATOM   4369 N N    A SER   B 1 7   ? 45.858 -24.246 -19.669 0.52 28.16 ?  7   SER   B N    1 
ATOM   4370 N N    B SER   B 1 7   ? 45.851 -24.250 -19.674 0.48 28.21 ?  7   SER   B N    1 
ATOM   4371 C CA   A SER   B 1 7   ? 45.943 -25.227 -20.741 0.52 30.85 ?  7   SER   B CA   1 
ATOM   4372 C CA   B SER   B 1 7   ? 45.901 -25.226 -20.752 0.48 30.74 ?  7   SER   B CA   1 
ATOM   4373 C C    A SER   B 1 7   ? 45.856 -26.628 -20.159 0.52 29.97 ?  7   SER   B C    1 
ATOM   4374 C C    B SER   B 1 7   ? 45.831 -26.632 -20.180 0.48 29.93 ?  7   SER   B C    1 
ATOM   4375 O O    A SER   B 1 7   ? 46.469 -26.923 -19.129 0.52 30.60 ?  7   SER   B O    1 
ATOM   4376 O O    B SER   B 1 7   ? 46.460 -26.930 -19.161 0.48 30.55 ?  7   SER   B O    1 
ATOM   4377 C CB   A SER   B 1 7   ? 47.259 -25.076 -21.516 0.52 33.78 ?  7   SER   B CB   1 
ATOM   4378 C CB   B SER   B 1 7   ? 47.183 -25.065 -21.580 0.48 33.51 ?  7   SER   B CB   1 
ATOM   4379 O OG   A SER   B 1 7   ? 47.326 -25.990 -22.598 0.52 36.02 ?  7   SER   B OG   1 
ATOM   4380 O OG   B SER   B 1 7   ? 47.120 -25.834 -22.769 0.48 35.60 ?  7   SER   B OG   1 
ATOM   4381 H H    A SER   B 1 7   ? 46.325 -24.453 -18.976 0.52 33.79 ?  7   SER   B H    1 
ATOM   4382 H H    B SER   B 1 7   ? 46.329 -24.461 -18.988 0.48 33.85 ?  7   SER   B H    1 
ATOM   4383 H HA   A SER   B 1 7   ? 45.207 -25.107 -21.356 0.52 37.01 ?  7   SER   B HA   1 
ATOM   4384 H HA   B SER   B 1 7   ? 45.143 -25.101 -21.340 0.48 36.88 ?  7   SER   B HA   1 
ATOM   4385 H HB2  A SER   B 1 7   ? 47.319 -24.169 -21.861 0.52 40.53 ?  7   SER   B HB2  1 
ATOM   4386 H HB2  B SER   B 1 7   ? 47.292 -24.129 -21.816 0.48 40.21 ?  7   SER   B HB2  1 
ATOM   4387 H HB3  A SER   B 1 7   ? 48.003 -25.248 -20.917 0.52 40.53 ?  7   SER   B HB3  1 
ATOM   4388 H HB3  B SER   B 1 7   ? 47.942 -25.362 -21.053 0.48 40.21 ?  7   SER   B HB3  1 
ATOM   4389 H HG   A SER   B 1 7   ? 48.048 -25.886 -23.017 0.52 43.22 ?  7   SER   B HG   1 
ATOM   4390 H HG   B SER   B 1 7   ? 47.829 -25.735 -23.212 0.48 42.72 ?  7   SER   B HG   1 
ATOM   4391 N N    A GLY   B 1 8   ? 45.089 -27.487 -20.828 0.52 29.49 ?  8   GLY   B N    1 
ATOM   4392 N N    B GLY   B 1 8   ? 45.063 -27.492 -20.847 0.48 29.37 ?  8   GLY   B N    1 
ATOM   4393 C CA   A GLY   B 1 8   ? 45.013 -28.880 -20.446 0.52 28.47 ?  8   GLY   B CA   1 
ATOM   4394 C CA   B GLY   B 1 8   ? 44.993 -28.886 -20.470 0.48 28.38 ?  8   GLY   B CA   1 
ATOM   4395 C C    A GLY   B 1 8   ? 44.091 -29.185 -19.295 0.52 27.10 ?  8   GLY   B C    1 
ATOM   4396 C C    B GLY   B 1 8   ? 44.071 -29.198 -19.319 0.48 27.03 ?  8   GLY   B C    1 
ATOM   4397 O O    A GLY   B 1 8   ? 44.262 -30.222 -18.645 0.52 28.30 ?  8   GLY   B O    1 
ATOM   4398 O O    B GLY   B 1 8   ? 44.226 -30.252 -18.692 0.48 28.10 ?  8   GLY   B O    1 
ATOM   4399 H H    A GLY   B 1 8   ? 44.608 -27.280 -21.507 0.52 35.39 ?  8   GLY   B H    1 
ATOM   4400 H H    B GLY   B 1 8   ? 44.579 -27.284 -21.525 0.48 35.25 ?  8   GLY   B H    1 
ATOM   4401 H HA2  A GLY   B 1 8   ? 44.708 -29.399 -21.204 0.52 34.16 ?  8   GLY   B HA2  1 
ATOM   4402 H HA2  B GLY   B 1 8   ? 44.688 -29.403 -21.230 0.48 34.06 ?  8   GLY   B HA2  1 
ATOM   4403 H HA3  A GLY   B 1 8   ? 45.896 -29.192 -20.201 0.52 34.16 ?  8   GLY   B HA3  1 
ATOM   4404 H HA3  B GLY   B 1 8   ? 45.877 -29.195 -20.228 0.48 34.06 ?  8   GLY   B HA3  1 
ATOM   4405 N N    . TYR   B 1 9   ? 43.100 -28.334 -19.032 1.00 25.58 ?  9   TYR   B N    1 
ATOM   4406 C CA   . TYR   B 1 9   ? 42.158 -28.582 -17.950 1.00 22.69 ?  9   TYR   B CA   1 
ATOM   4407 C C    . TYR   B 1 9   ? 40.956 -29.369 -18.438 1.00 22.70 ?  9   TYR   B C    1 
ATOM   4408 O O    . TYR   B 1 9   ? 40.506 -29.232 -19.580 1.00 24.78 ?  9   TYR   B O    1 
ATOM   4409 C CB   . TYR   B 1 9   ? 41.677 -27.285 -17.300 1.00 21.58 ?  9   TYR   B CB   1 
ATOM   4410 C CG   . TYR   B 1 9   ? 42.719 -26.682 -16.385 1.00 20.70 ?  9   TYR   B CG   1 
ATOM   4411 C CD1  . TYR   B 1 9   ? 43.810 -26.001 -16.907 1.00 21.75 ?  9   TYR   B CD1  1 
ATOM   4412 C CD2  . TYR   B 1 9   ? 42.623 -26.796 -15.001 1.00 19.43 ?  9   TYR   B CD2  1 
ATOM   4413 C CE1  . TYR   B 1 9   ? 44.779 -25.465 -16.088 1.00 21.19 ?  9   TYR   B CE1  1 
ATOM   4414 C CE2  . TYR   B 1 9   ? 43.595 -26.258 -14.169 1.00 19.90 ?  9   TYR   B CE2  1 
ATOM   4415 C CZ   . TYR   B 1 9   ? 44.669 -25.585 -14.721 1.00 21.09 ?  9   TYR   B CZ   1 
ATOM   4416 O OH   . TYR   B 1 9   ? 45.644 -25.039 -13.915 1.00 22.33 ?  9   TYR   B OH   1 
ATOM   4417 H H    A TYR   B 1 9   ? 42.935 -27.618 -19.480 0.52 30.70 ?  9   TYR   B H    1 
ATOM   4418 H H    B TYR   B 1 9   ? 42.947 -27.607 -19.465 0.48 30.70 ?  9   TYR   B H    1 
ATOM   4419 H HA   . TYR   B 1 9   ? 42.589 -29.104 -17.264 1.00 27.23 ?  9   TYR   B HA   1 
ATOM   4420 H HB2  . TYR   B 1 9   ? 41.456 -26.631 -17.986 1.00 25.90 ?  9   TYR   B HB2  1 
ATOM   4421 H HB3  . TYR   B 1 9   ? 40.895 -27.485 -16.767 1.00 25.90 ?  9   TYR   B HB3  1 
ATOM   4422 H HD1  . TYR   B 1 9   ? 43.890 -25.919 -17.830 1.00 26.10 ?  9   TYR   B HD1  1 
ATOM   4423 H HD2  . TYR   B 1 9   ? 41.894 -27.256 -14.630 1.00 23.32 ?  9   TYR   B HD2  1 
ATOM   4424 H HE1  . TYR   B 1 9   ? 45.496 -25.015 -16.457 1.00 25.43 ?  9   TYR   B HE1  1 
ATOM   4425 H HE2  . TYR   B 1 9   ? 43.509 -26.347 -13.246 1.00 23.87 ?  9   TYR   B HE2  1 
ATOM   4426 H HH   . TYR   B 1 9   ? 46.220 -24.666 -14.390 1.00 26.80 ?  9   TYR   B HH   1 
ATOM   4427 N N    . LEU   B 1 10  ? 40.449 -30.213 -17.550 1.00 20.51 ?  10  LEU   B N    1 
ATOM   4428 C CA   . LEU   B 1 10  ? 39.240 -30.976 -17.792 1.00 20.09 ?  10  LEU   B CA   1 
ATOM   4429 C C    . LEU   B 1 10  ? 38.061 -30.192 -17.243 1.00 19.58 ?  10  LEU   B C    1 
ATOM   4430 O O    . LEU   B 1 10  ? 38.075 -29.777 -16.081 1.00 19.37 ?  10  LEU   B O    1 
ATOM   4431 C CB   . LEU   B 1 10  ? 39.338 -32.319 -17.074 1.00 21.58 ?  10  LEU   B CB   1 
ATOM   4432 C CG   . LEU   B 1 10  ? 38.234 -33.318 -17.409 1.00 23.09 ?  10  LEU   B CG   1 
ATOM   4433 C CD1  . LEU   B 1 10  ? 38.443 -33.867 -18.814 1.00 24.40 ?  10  LEU   B CD1  1 
ATOM   4434 C CD2  . LEU   B 1 10  ? 38.180 -34.445 -16.387 1.00 23.70 ?  10  LEU   B CD2  1 
ATOM   4435 H H    . LEU   B 1 10  ? 40.791 -30.358 -16.768 1.00 24.61 ?  10  LEU   B H    1 
ATOM   4436 H HA   . LEU   B 1 10  ? 39.115 -31.123 -18.738 1.00 24.11 ?  10  LEU   B HA   1 
ATOM   4437 H HB2  . LEU   B 1 10  ? 40.183 -32.731 -17.307 1.00 25.90 ?  10  LEU   B HB2  1 
ATOM   4438 H HB3  . LEU   B 1 10  ? 39.306 -32.164 -16.115 1.00 25.90 ?  10  LEU   B HB3  1 
ATOM   4439 H HG   . LEU   B 1 10  ? 37.377 -32.863 -17.392 1.00 27.71 ?  10  LEU   B HG   1 
ATOM   4440 H HD11 . LEU   B 1 10  ? 37.776 -34.546 -18.989 1.00 29.28 ?  10  LEU   B HD11 1 
ATOM   4441 H HD12 . LEU   B 1 10  ? 38.354 -33.140 -19.450 1.00 29.28 ?  10  LEU   B HD12 1 
ATOM   4442 H HD13 . LEU   B 1 10  ? 39.332 -34.250 -18.870 1.00 29.28 ?  10  LEU   B HD13 1 
ATOM   4443 H HD21 . LEU   B 1 10  ? 37.469 -35.060 -16.633 1.00 28.45 ?  10  LEU   B HD21 1 
ATOM   4444 H HD22 . LEU   B 1 10  ? 39.031 -34.907 -16.382 1.00 28.45 ?  10  LEU   B HD22 1 
ATOM   4445 H HD23 . LEU   B 1 10  ? 38.000 -34.068 -15.511 1.00 28.45 ?  10  LEU   B HD23 1 
ATOM   4446 N N    . LYS   B 1 11  ? 37.050 -29.990 -18.084 1.00 21.11 ?  11  LYS   B N    1 
ATOM   4447 C CA   . LYS   B 1 11  ? 35.838 -29.291 -17.679 1.00 24.43 ?  11  LYS   B CA   1 
ATOM   4448 C C    . LYS   B 1 11  ? 34.985 -30.223 -16.824 1.00 23.06 ?  11  LYS   B C    1 
ATOM   4449 O O    . LYS   B 1 11  ? 34.616 -31.320 -17.264 1.00 25.09 ?  11  LYS   B O    1 
ATOM   4450 C CB   . LYS   B 1 11  ? 35.078 -28.860 -18.933 1.00 29.46 ?  11  LYS   B CB   1 
ATOM   4451 C CG   . LYS   B 1 11  ? 33.933 -27.893 -18.710 1.00 34.30 ?  11  LYS   B CG   1 
ATOM   4452 C CD   . LYS   B 1 11  ? 33.278 -27.539 -20.043 1.00 38.14 ?  11  LYS   B CD   1 
ATOM   4453 C CE   . LYS   B 1 11  ? 32.234 -26.444 -19.897 1.00 40.95 ?  11  LYS   B CE   1 
ATOM   4454 N NZ   . LYS   B 1 11  ? 32.845 -25.106 -19.670 1.00 42.55 ?  11  LYS   B NZ   1 
ATOM   4455 H H    . LYS   B 1 11  ? 37.041 -30.247 -18.909 1.00 25.34 ?  11  LYS   B H    1 
ATOM   4456 H HA   . LYS   B 1 11  ? 36.065 -28.502 -17.165 1.00 29.32 ?  11  LYS   B HA   1 
ATOM   4457 H HB2  . LYS   B 1 11  ? 35.702 -28.428 -19.539 1.00 35.36 ?  11  LYS   B HB2  1 
ATOM   4458 H HB3  . LYS   B 1 11  ? 34.709 -29.649 -19.359 1.00 35.36 ?  11  LYS   B HB3  1 
ATOM   4459 H HG2  . LYS   B 1 11  ? 33.267 -28.308 -18.141 1.00 41.16 ?  11  LYS   B HG2  1 
ATOM   4460 H HG3  . LYS   B 1 11  ? 34.269 -27.079 -18.306 1.00 41.16 ?  11  LYS   B HG3  1 
ATOM   4461 H HD2  . LYS   B 1 11  ? 33.960 -27.227 -20.659 1.00 45.77 ?  11  LYS   B HD2  1 
ATOM   4462 H HD3  . LYS   B 1 11  ? 32.842 -28.328 -20.403 1.00 45.77 ?  11  LYS   B HD3  1 
ATOM   4463 H HE2  . LYS   B 1 11  ? 31.704 -26.400 -20.709 1.00 49.14 ?  11  LYS   B HE2  1 
ATOM   4464 H HE3  . LYS   B 1 11  ? 31.664 -26.650 -19.139 1.00 49.14 ?  11  LYS   B HE3  1 
ATOM   4465 H HZ1  . LYS   B 1 11  ? 32.208 -24.489 -19.591 1.00 51.06 ?  11  LYS   B HZ1  1 
ATOM   4466 H HZ2  . LYS   B 1 11  ? 33.331 -25.115 -18.925 1.00 51.06 ?  11  LYS   B HZ2  1 
ATOM   4467 H HZ3  . LYS   B 1 11  ? 33.371 -24.891 -20.356 1.00 51.06 ?  11  LYS   B HZ3  1 
ATOM   4468 N N    . LEU   B 1 12  ? 34.669 -29.791 -15.604 1.00 21.15 ?  12  LEU   B N    1 
ATOM   4469 C CA   . LEU   B 1 12  ? 33.714 -30.497 -14.755 1.00 19.68 ?  12  LEU   B CA   1 
ATOM   4470 C C    . LEU   B 1 12  ? 32.324 -29.885 -14.830 1.00 19.82 ?  12  LEU   B C    1 
ATOM   4471 O O    . LEU   B 1 12  ? 31.334 -30.602 -14.979 1.00 20.88 ?  12  LEU   B O    1 
ATOM   4472 C CB   . LEU   B 1 12  ? 34.177 -30.521 -13.293 1.00 19.17 ?  12  LEU   B CB   1 
ATOM   4473 C CG   . LEU   B 1 12  ? 35.512 -31.213 -13.014 1.00 18.91 ?  12  LEU   B CG   1 
ATOM   4474 C CD1  . LEU   B 1 12  ? 35.856 -31.144 -11.539 1.00 19.25 ?  12  LEU   B CD1  1 
ATOM   4475 C CD2  . LEU   B 1 12  ? 35.514 -32.665 -13.500 1.00 19.64 ?  12  LEU   B CD2  1 
ATOM   4476 H H    . LEU   B 1 12  ? 34.993 -29.081 -15.243 1.00 25.37 ?  12  LEU   B H    1 
ATOM   4477 H HA   . LEU   B 1 12  ? 33.638 -31.412 -15.062 1.00 23.61 ?  12  LEU   B HA   1 
ATOM   4478 H HB2  . LEU   B 1 12  ? 34.248 -29.610 -12.981 1.00 23.01 ?  12  LEU   B HB2  1 
ATOM   4479 H HB3  . LEU   B 1 12  ? 33.497 -30.986 -12.772 1.00 23.01 ?  12  LEU   B HB3  1 
ATOM   4480 H HG   . LEU   B 1 12  ? 36.203 -30.740 -13.498 1.00 22.70 ?  12  LEU   B HG   1 
ATOM   4481 H HD11 . LEU   B 1 12  ? 36.711 -31.587 -11.394 1.00 23.10 ?  12  LEU   B HD11 1 
ATOM   4482 H HD12 . LEU   B 1 12  ? 35.919 -30.215 -11.268 1.00 23.10 ?  12  LEU   B HD12 1 
ATOM   4483 H HD13 . LEU   B 1 12  ? 35.165 -31.592 -11.027 1.00 23.10 ?  12  LEU   B HD13 1 
ATOM   4484 H HD21 . LEU   B 1 12  ? 36.334 -33.091 -13.211 1.00 23.56 ?  12  LEU   B HD21 1 
ATOM   4485 H HD22 . LEU   B 1 12  ? 34.748 -33.126 -13.120 1.00 23.56 ?  12  LEU   B HD22 1 
ATOM   4486 H HD23 . LEU   B 1 12  ? 35.457 -32.673 -14.468 1.00 23.56 ?  12  LEU   B HD23 1 
ATOM   4487 N N    . THR   B 1 13  ? 32.239 -28.565 -14.715 1.00 19.99 ?  13  THR   B N    1 
ATOM   4488 C CA   . THR   B 1 13  ? 31.015 -27.813 -14.934 1.00 19.67 ?  13  THR   B CA   1 
ATOM   4489 C C    . THR   B 1 13  ? 31.360 -26.632 -15.834 1.00 21.85 ?  13  THR   B C    1 
ATOM   4490 O O    . THR   B 1 13  ? 32.506 -26.463 -16.263 1.00 23.33 ?  13  THR   B O    1 
ATOM   4491 C CB   . THR   B 1 13  ? 30.417 -27.314 -13.612 1.00 19.33 ?  13  THR   B CB   1 
ATOM   4492 O OG1  . THR   B 1 13  ? 31.256 -26.287 -13.078 1.00 18.47 ?  13  THR   B OG1  1 
ATOM   4493 C CG2  . THR   B 1 13  ? 30.321 -28.433 -12.591 1.00 20.03 ?  13  THR   B CG2  1 
ATOM   4494 H H    . THR   B 1 13  ? 32.903 -28.066 -14.493 1.00 23.99 ?  13  THR   B H    1 
ATOM   4495 H HA   . THR   B 1 13  ? 30.356 -28.372 -15.375 1.00 23.60 ?  13  THR   B HA   1 
ATOM   4496 H HB   . THR   B 1 13  ? 29.526 -26.952 -13.769 1.00 23.20 ?  13  THR   B HB   1 
ATOM   4497 H HG1  . THR   B 1 13  ? 30.920 -25.518 -13.234 1.00 22.16 ?  13  THR   B HG1  1 
ATOM   4498 H HG21 . THR   B 1 13  ? 29.833 -28.127 -11.809 1.00 24.04 ?  13  THR   B HG21 1 
ATOM   4499 H HG22 . THR   B 1 13  ? 29.857 -29.189 -12.976 1.00 24.04 ?  13  THR   B HG22 1 
ATOM   4500 H HG23 . THR   B 1 13  ? 31.209 -28.708 -12.318 1.00 24.04 ?  13  THR   B HG23 1 
ATOM   4501 N N    A ASP   B 1 14  ? 30.358 -25.797 -16.112 0.52 22.81 ?  14  ASP   B N    1 
ATOM   4502 N N    B ASP   B 1 14  ? 30.361 -25.792 -16.112 0.48 22.74 ?  14  ASP   B N    1 
ATOM   4503 C CA   A ASP   B 1 14  ? 30.596 -24.644 -16.969 0.52 24.04 ?  14  ASP   B CA   1 
ATOM   4504 C CA   B ASP   B 1 14  ? 30.594 -24.640 -16.975 0.48 23.81 ?  14  ASP   B CA   1 
ATOM   4505 C C    A ASP   B 1 14  ? 31.709 -23.758 -16.424 0.52 22.19 ?  14  ASP   B C    1 
ATOM   4506 C C    B ASP   B 1 14  ? 31.625 -23.674 -16.408 0.48 22.02 ?  14  ASP   B C    1 
ATOM   4507 O O    A ASP   B 1 14  ? 32.426 -23.122 -17.208 0.52 23.81 ?  14  ASP   B O    1 
ATOM   4508 O O    B ASP   B 1 14  ? 32.162 -22.858 -17.165 0.48 23.40 ?  14  ASP   B O    1 
ATOM   4509 C CB   A ASP   B 1 14  ? 29.305 -23.845 -17.156 0.52 27.49 ?  14  ASP   B CB   1 
ATOM   4510 C CB   B ASP   B 1 14  ? 29.293 -23.877 -17.227 0.48 27.10 ?  14  ASP   B CB   1 
ATOM   4511 C CG   A ASP   B 1 14  ? 28.306 -24.543 -18.066 0.52 31.54 ?  14  ASP   B CG   1 
ATOM   4512 C CG   B ASP   B 1 14  ? 28.421 -24.542 -18.275 0.48 30.93 ?  14  ASP   B CG   1 
ATOM   4513 O OD1  A ASP   B 1 14  ? 28.662 -25.558 -18.709 0.52 32.27 ?  14  ASP   B OD1  1 
ATOM   4514 O OD1  B ASP   B 1 14  ? 28.967 -25.246 -19.154 0.48 31.95 ?  14  ASP   B OD1  1 
ATOM   4515 O OD2  A ASP   B 1 14  ? 27.150 -24.078 -18.127 0.52 33.13 -1 14  ASP   B OD2  1 
ATOM   4516 O OD2  B ASP   B 1 14  ? 27.186 -24.366 -18.221 0.48 32.20 -1 14  ASP   B OD2  1 
ATOM   4517 H H    A ASP   B 1 14  ? 29.556 -25.863 -15.815 0.52 27.38 ?  14  ASP   B H    1 
ATOM   4518 H H    B ASP   B 1 14  ? 29.557 -25.864 -15.820 0.48 27.29 ?  14  ASP   B H    1 
ATOM   4519 H HA   A ASP   B 1 14  ? 30.886 -24.947 -17.838 0.52 28.85 ?  14  ASP   B HA   1 
ATOM   4520 H HA   B ASP   B 1 14  ? 30.927 -24.952 -17.829 0.48 28.58 ?  14  ASP   B HA   1 
ATOM   4521 H HB2  A ASP   B 1 14  ? 28.866 -23.737 -16.300 0.52 32.98 ?  14  ASP   B HB2  1 
ATOM   4522 H HB2  B ASP   B 1 14  ? 28.790 -23.830 -16.400 0.48 32.51 ?  14  ASP   B HB2  1 
ATOM   4523 H HB3  A ASP   B 1 14  ? 29.519 -22.972 -17.531 0.52 32.98 ?  14  ASP   B HB3  1 
ATOM   4524 H HB3  B ASP   B 1 14  ? 29.512 -22.975 -17.528 0.48 32.51 ?  14  ASP   B HB3  1 
ATOM   4525 N N    . ASN   B 1 15  ? 31.894 -23.718 -15.098 1.00 19.84 ?  15  ASN   B N    1 
ATOM   4526 C CA   . ASN   B 1 15  ? 32.859 -22.804 -14.486 1.00 17.31 ?  15  ASN   B CA   1 
ATOM   4527 C C    . ASN   B 1 15  ? 33.962 -23.462 -13.662 1.00 16.09 ?  15  ASN   B C    1 
ATOM   4528 O O    . ASN   B 1 15  ? 34.820 -22.741 -13.143 1.00 15.70 ?  15  ASN   B O    1 
ATOM   4529 C CB   . ASN   B 1 15  ? 32.152 -21.749 -13.615 1.00 17.72 ?  15  ASN   B CB   1 
ATOM   4530 C CG   . ASN   B 1 15  ? 31.533 -22.353 -12.370 1.00 16.85 ?  15  ASN   B CG   1 
ATOM   4531 O OD1  . ASN   B 1 15  ? 30.582 -23.139 -12.457 1.00 19.67 ?  15  ASN   B OD1  1 
ATOM   4532 N ND2  . ASN   B 1 15  ? 32.066 -22.013 -11.208 1.00 16.23 ?  15  ASN   B ND2  1 
ATOM   4533 H H    A ASN   B 1 15  ? 31.468 -24.211 -14.533 0.52 23.80 ?  15  ASN   B H    1 
ATOM   4534 H H    B ASN   B 1 15  ? 31.500 -24.241 -14.538 0.48 23.80 ?  15  ASN   B H    1 
ATOM   4535 H HA   . ASN   B 1 15  ? 33.307 -22.313 -15.182 1.00 20.77 ?  15  ASN   B HA   1 
ATOM   4536 H HB2  . ASN   B 1 15  ? 32.799 -21.070 -13.337 1.00 21.27 ?  15  ASN   B HB2  1 
ATOM   4537 H HB3  . ASN   B 1 15  ? 31.444 -21.322 -14.131 1.00 21.27 ?  15  ASN   B HB3  1 
ATOM   4538 H HD21 . ASN   B 1 15  ? 31.738 -22.328 -10.473 1.00 19.48 ?  15  ASN   B HD21 1 
ATOM   4539 H HD22 . ASN   B 1 15  ? 32.738 -21.474 -11.171 1.00 19.48 ?  15  ASN   B HD22 1 
ATOM   4540 N N    . VAL   B 1 16  ? 33.962 -24.786 -13.503 1.00 15.91 ?  16  VAL   B N    1 
ATOM   4541 C CA   . VAL   B 1 16  ? 34.959 -25.478 -12.694 1.00 15.45 ?  16  VAL   B CA   1 
ATOM   4542 C C    . VAL   B 1 16  ? 35.740 -26.420 -13.591 1.00 15.47 ?  16  VAL   B C    1 
ATOM   4543 O O    . VAL   B 1 16  ? 35.152 -27.297 -14.244 1.00 15.98 ?  16  VAL   B O    1 
ATOM   4544 C CB   . VAL   B 1 16  ? 34.321 -26.242 -11.517 1.00 15.43 ?  16  VAL   B CB   1 
ATOM   4545 C CG1  . VAL   B 1 16  ? 35.383 -26.990 -10.710 1.00 15.75 ?  16  VAL   B CG1  1 
ATOM   4546 C CG2  . VAL   B 1 16  ? 33.532 -25.288 -10.633 1.00 16.43 ?  16  VAL   B CG2  1 
ATOM   4547 H H    . VAL   B 1 16  ? 33.375 -25.312 -13.859 1.00 19.09 ?  16  VAL   B H    1 
ATOM   4548 H HA   . VAL   B 1 16  ? 35.572 -24.833 -12.323 1.00 18.54 ?  16  VAL   B HA   1 
ATOM   4549 H HB   . VAL   B 1 16  ? 33.698 -26.903 -11.868 1.00 18.51 ?  16  VAL   B HB   1 
ATOM   4550 H HG11 . VAL   B 1 16  ? 34.982 -27.312 -9.884  1.00 18.90 ?  16  VAL   B HG11 1 
ATOM   4551 H HG12 . VAL   B 1 16  ? 35.713 -27.737 -11.228 1.00 18.90 ?  16  VAL   B HG12 1 
ATOM   4552 H HG13 . VAL   B 1 16  ? 36.108 -26.378 -10.504 1.00 18.90 ?  16  VAL   B HG13 1 
ATOM   4553 H HG21 . VAL   B 1 16  ? 33.190 -25.777 -9.867  1.00 19.71 ?  16  VAL   B HG21 1 
ATOM   4554 H HG22 . VAL   B 1 16  ? 34.118 -24.577 -10.337 1.00 19.71 ?  16  VAL   B HG22 1 
ATOM   4555 H HG23 . VAL   B 1 16  ? 32.794 -24.921 -11.145 1.00 19.71 ?  16  VAL   B HG23 1 
ATOM   4556 N N    . TYR   B 1 17  ? 37.062 -26.266 -13.569 1.00 16.06 ?  17  TYR   B N    1 
ATOM   4557 C CA   . TYR   B 1 17  ? 38.012 -27.017 -14.377 1.00 16.02 ?  17  TYR   B CA   1 
ATOM   4558 C C    . TYR   B 1 17  ? 39.069 -27.620 -13.456 1.00 14.73 ?  17  TYR   B C    1 
ATOM   4559 O O    . TYR   B 1 17  ? 39.342 -27.090 -12.376 1.00 14.80 ?  17  TYR   B O    1 
ATOM   4560 C CB   . TYR   B 1 17  ? 38.721 -26.100 -15.388 1.00 20.43 ?  17  TYR   B CB   1 
ATOM   4561 C CG   . TYR   B 1 17  ? 37.795 -25.329 -16.296 1.00 24.87 ?  17  TYR   B CG   1 
ATOM   4562 C CD1  . TYR   B 1 17  ? 37.239 -24.121 -15.897 1.00 27.33 ?  17  TYR   B CD1  1 
ATOM   4563 C CD2  . TYR   B 1 17  ? 37.476 -25.810 -17.561 1.00 27.51 ?  17  TYR   B CD2  1 
ATOM   4564 C CE1  . TYR   B 1 17  ? 36.386 -23.411 -16.730 1.00 29.38 ?  17  TYR   B CE1  1 
ATOM   4565 C CE2  . TYR   B 1 17  ? 36.628 -25.108 -18.402 1.00 29.68 ?  17  TYR   B CE2  1 
ATOM   4566 C CZ   . TYR   B 1 17  ? 36.085 -23.910 -17.980 1.00 31.15 ?  17  TYR   B CZ   1 
ATOM   4567 O OH   . TYR   B 1 17  ? 35.242 -23.209 -18.811 1.00 32.55 ?  17  TYR   B OH   1 
ATOM   4568 H H    . TYR   B 1 17  ? 37.455 -25.692 -13.056 1.00 19.27 ?  17  TYR   B H    1 
ATOM   4569 H HA   . TYR   B 1 17  ? 37.546 -27.724 -14.855 1.00 19.23 ?  17  TYR   B HA   1 
ATOM   4570 H HB2  . TYR   B 1 17  ? 39.268 -25.461 -14.908 1.00 24.52 ?  17  TYR   B HB2  1 
ATOM   4571 H HB3  . TYR   B 1 17  ? 39.274 -26.650 -15.955 1.00 24.52 ?  17  TYR   B HB3  1 
ATOM   4572 H HD1  . TYR   B 1 17  ? 37.437 -23.780 -15.057 1.00 32.80 ?  17  TYR   B HD1  1 
ATOM   4573 H HD2  . TYR   B 1 17  ? 37.833 -26.615 -17.851 1.00 33.01 ?  17  TYR   B HD2  1 
ATOM   4574 H HE1  . TYR   B 1 17  ? 36.020 -22.602 -16.450 1.00 35.25 ?  17  TYR   B HE1  1 
ATOM   4575 H HE2  . TYR   B 1 17  ? 36.417 -25.442 -19.247 1.00 35.62 ?  17  TYR   B HE2  1 
ATOM   4576 H HH   . TYR   B 1 17  ? 35.141 -23.620 -19.537 1.00 39.06 ?  17  TYR   B HH   1 
ATOM   4577 N N    . ILE   B 1 18  ? 39.682 -28.728 -13.883 1.00 15.55 ?  18  ILE   B N    1 
ATOM   4578 C CA   . ILE   B 1 18  ? 40.605 -29.461 -13.021 1.00 15.52 ?  18  ILE   B CA   1 
ATOM   4579 C C    . ILE   B 1 18  ? 41.761 -30.029 -13.842 1.00 15.85 ?  18  ILE   B C    1 
ATOM   4580 O O    . ILE   B 1 18  ? 41.597 -30.431 -14.998 1.00 17.16 ?  18  ILE   B O    1 
ATOM   4581 C CB   . ILE   B 1 18  ? 39.850 -30.566 -12.226 1.00 15.39 ?  18  ILE   B CB   1 
ATOM   4582 C CG1  . ILE   B 1 18  ? 40.714 -31.126 -11.087 1.00 16.04 ?  18  ILE   B CG1  1 
ATOM   4583 C CG2  . ILE   B 1 18  ? 39.310 -31.674 -13.165 1.00 16.18 ?  18  ILE   B CG2  1 
ATOM   4584 C CD1  . ILE   B 1 18  ? 39.916 -31.980 -10.088 1.00 17.99 ?  18  ILE   B CD1  1 
ATOM   4585 H H    . ILE   B 1 18  ? 39.584 -29.064 -14.662 1.00 18.65 ?  18  ILE   B H    1 
ATOM   4586 H HA   . ILE   B 1 18  ? 40.963 -28.842 -12.361 1.00 18.62 ?  18  ILE   B HA   1 
ATOM   4587 H HB   . ILE   B 1 18  ? 39.076 -30.154 -11.806 1.00 18.47 ?  18  ILE   B HB   1 
ATOM   4588 H HG12 . ILE   B 1 18  ? 41.409 -31.683 -11.462 1.00 19.25 ?  18  ILE   B HG12 1 
ATOM   4589 H HG13 . ILE   B 1 18  ? 41.104 -30.387 -10.596 1.00 19.25 ?  18  ILE   B HG13 1 
ATOM   4590 H HG21 . ILE   B 1 18  ? 38.738 -32.272 -12.655 1.00 19.41 ?  18  ILE   B HG21 1 
ATOM   4591 H HG22 . ILE   B 1 18  ? 38.794 -31.254 -13.873 1.00 19.41 ?  18  ILE   B HG22 1 
ATOM   4592 H HG23 . ILE   B 1 18  ? 40.053 -32.163 -13.539 1.00 19.41 ?  18  ILE   B HG23 1 
ATOM   4593 H HD11 . ILE   B 1 18  ? 40.507 -32.260 -9.372  1.00 21.59 ?  18  ILE   B HD11 1 
ATOM   4594 H HD12 . ILE   B 1 18  ? 39.189 -31.447 -9.727  1.00 21.59 ?  18  ILE   B HD12 1 
ATOM   4595 H HD13 . ILE   B 1 18  ? 39.561 -32.755 -10.549 1.00 21.59 ?  18  ILE   B HD13 1 
ATOM   4596 N N    . LYS   B 1 19  ? 42.942 -30.063 -13.228 1.00 16.32 ?  19  LYS   B N    1 
ATOM   4597 C CA   . LYS   B 1 19  ? 44.140 -30.545 -13.898 1.00 17.64 ?  19  LYS   B CA   1 
ATOM   4598 C C    . LYS   B 1 19  ? 45.042 -31.226 -12.878 1.00 16.81 ?  19  LYS   B C    1 
ATOM   4599 O O    . LYS   B 1 19  ? 45.137 -30.788 -11.730 1.00 16.76 ?  19  LYS   B O    1 
ATOM   4600 C CB   . LYS   B 1 19  ? 44.890 -29.376 -14.551 1.00 19.53 ?  19  LYS   B CB   1 
ATOM   4601 C CG   . LYS   B 1 19  ? 46.080 -29.797 -15.388 1.00 22.25 ?  19  LYS   B CG   1 
ATOM   4602 C CD   . LYS   B 1 19  ? 46.774 -28.585 -15.987 1.00 24.28 ?  19  LYS   B CD   1 
ATOM   4603 C CE   . LYS   B 1 19  ? 47.991 -28.971 -16.805 1.00 26.82 ?  19  LYS   B CE   1 
ATOM   4604 N NZ   . LYS   B 1 19  ? 48.696 -27.774 -17.340 1.00 28.24 ?  19  LYS   B NZ   1 
ATOM   4605 H H    . LYS   B 1 19  ? 43.058 -29.817 -12.412 1.00 19.58 ?  19  LYS   B H    1 
ATOM   4606 H HA   . LYS   B 1 19  ? 43.886 -31.187 -14.585 1.00 21.17 ?  19  LYS   B HA   1 
ATOM   4607 H HB2  . LYS   B 1 19  ? 44.270 -28.901 -15.129 1.00 23.43 ?  19  LYS   B HB2  1 
ATOM   4608 H HB3  . LYS   B 1 19  ? 45.200 -28.783 -13.848 1.00 23.43 ?  19  LYS   B HB3  1 
ATOM   4609 H HG2  . LYS   B 1 19  ? 46.709 -30.274 -14.828 1.00 26.69 ?  19  LYS   B HG2  1 
ATOM   4610 H HG3  . LYS   B 1 19  ? 45.770 -30.369 -16.111 1.00 26.69 ?  19  LYS   B HG3  1 
ATOM   4611 H HD2  . LYS   B 1 19  ? 46.151 -28.115 -16.566 1.00 29.14 ?  19  LYS   B HD2  1 
ATOM   4612 H HD3  . LYS   B 1 19  ? 47.062 -27.998 -15.267 1.00 29.14 ?  19  LYS   B HD3  1 
ATOM   4613 H HE2  . LYS   B 1 19  ? 48.607 -29.463 -16.241 1.00 32.18 ?  19  LYS   B HE2  1 
ATOM   4614 H HE3  . LYS   B 1 19  ? 47.707 -29.520 -17.552 1.00 32.18 ?  19  LYS   B HE3  1 
ATOM   4615 H HZ1  . LYS   B 1 19  ? 49.388 -28.027 -17.840 1.00 33.88 ?  19  LYS   B HZ1  1 
ATOM   4616 H HZ2  . LYS   B 1 19  ? 48.140 -27.291 -17.841 1.00 33.88 ?  19  LYS   B HZ2  1 
ATOM   4617 H HZ3  . LYS   B 1 19  ? 48.993 -27.269 -16.671 1.00 33.88 ?  19  LYS   B HZ3  1 
ATOM   4618 N N    . ASN   B 1 20  ? 45.730 -32.280 -13.312 1.00 18.96 ?  20  ASN   B N    1 
ATOM   4619 C CA   . ASN   B 1 20  ? 46.753 -32.913 -12.484 1.00 19.79 ?  20  ASN   B CA   1 
ATOM   4620 C C    . ASN   B 1 20  ? 48.039 -32.114 -12.654 1.00 20.03 ?  20  ASN   B C    1 
ATOM   4621 O O    . ASN   B 1 20  ? 48.684 -32.187 -13.708 1.00 22.45 ?  20  ASN   B O    1 
ATOM   4622 C CB   . ASN   B 1 20  ? 46.920 -34.369 -12.921 1.00 21.90 ?  20  ASN   B CB   1 
ATOM   4623 C CG   . ASN   B 1 20  ? 48.089 -35.082 -12.240 1.00 23.27 ?  20  ASN   B CG   1 
ATOM   4624 O OD1  . ASN   B 1 20  ? 48.756 -35.918 -12.860 1.00 25.93 ?  20  ASN   B OD1  1 
ATOM   4625 N ND2  . ASN   B 1 20  ? 48.324 -34.786 -10.970 1.00 22.75 ?  20  ASN   B ND2  1 
ATOM   4626 H H    . ASN   B 1 20  ? 45.626 -32.634 -14.086 1.00 22.75 ?  20  ASN   B H    1 
ATOM   4627 H HA   . ASN   B 1 20  ? 46.469 -32.891 -11.554 1.00 23.74 ?  20  ASN   B HA   1 
ATOM   4628 H HB2  . ASN   B 1 20  ? 46.098 -34.852 -12.710 1.00 26.28 ?  20  ASN   B HB2  1 
ATOM   4629 H HB3  . ASN   B 1 20  ? 47.066 -34.387 -13.879 1.00 26.28 ?  20  ASN   B HB3  1 
ATOM   4630 H HD21 . ASN   B 1 20  ? 48.970 -35.164 -10.554 1.00 27.29 ?  20  ASN   B HD21 1 
ATOM   4631 H HD22 . ASN   B 1 20  ? 47.837 -34.198 -10.562 1.00 27.29 ?  20  ASN   B HD22 1 
ATOM   4632 N N    . ALA   B 1 21  ? 48.411 -31.339 -11.635 1.00 19.60 ?  21  ALA   B N    1 
ATOM   4633 C CA   . ALA   B 1 21  ? 49.524 -30.411 -11.802 1.00 19.92 ?  21  ALA   B CA   1 
ATOM   4634 C C    . ALA   B 1 21  ? 49.997 -29.888 -10.451 1.00 18.25 ?  21  ALA   B C    1 
ATOM   4635 O O    . ALA   B 1 21  ? 49.260 -29.898 -9.459  1.00 17.75 ?  21  ALA   B O    1 
ATOM   4636 C CB   . ALA   B 1 21  ? 49.124 -29.245 -12.706 1.00 21.73 ?  21  ALA   B CB   1 
ATOM   4637 H H    . ALA   B 1 21  ? 48.039 -31.330 -10.851 1.00 23.52 ?  21  ALA   B H    1 
ATOM   4638 H HA   . ALA   B 1 21  ? 50.257 -30.886 -12.221 1.00 23.91 ?  21  ALA   B HA   1 
ATOM   4639 H HB1  . ALA   B 1 21  ? 49.907 -28.704 -12.864 1.00 26.08 ?  21  ALA   B HB1  1 
ATOM   4640 H HB2  . ALA   B 1 21  ? 48.790 -29.604 -13.544 1.00 26.08 ?  21  ALA   B HB2  1 
ATOM   4641 H HB3  . ALA   B 1 21  ? 48.433 -28.731 -12.266 1.00 26.08 ?  21  ALA   B HB3  1 
ATOM   4642 N N    . ASP   B 1 22  ? 51.252 -29.434 -10.443 1.00 17.66 ?  22  ASP   B N    1 
ATOM   4643 C CA   . ASP   B 1 22  ? 51.873 -28.747 -9.315  1.00 16.68 ?  22  ASP   B CA   1 
ATOM   4644 C C    . ASP   B 1 22  ? 51.466 -27.276 -9.391  1.00 15.18 ?  22  ASP   B C    1 
ATOM   4645 O O    . ASP   B 1 22  ? 51.777 -26.598 -10.375 1.00 15.68 ?  22  ASP   B O    1 
ATOM   4646 C CB   . ASP   B 1 22  ? 53.390 -28.936 -9.470  1.00 17.99 ?  22  ASP   B CB   1 
ATOM   4647 C CG   . ASP   B 1 22  ? 54.231 -28.180 -8.442  1.00 19.90 ?  22  ASP   B CG   1 
ATOM   4648 O OD1  . ASP   B 1 22  ? 53.891 -27.048 -8.061  1.00 20.13 ?  22  ASP   B OD1  1 
ATOM   4649 O OD2  . ASP   B 1 22  ? 55.295 -28.709 -8.046  1.00 22.85 -1 22  ASP   B OD2  1 
ATOM   4650 H H    . ASP   B 1 22  ? 51.785 -29.512 -11.119 1.00 21.19 ?  22  ASP   B H    1 
ATOM   4651 H HA   . ASP   B 1 22  ? 51.577 -29.136 -8.473  1.00 20.01 ?  22  ASP   B HA   1 
ATOM   4652 H HB2  . ASP   B 1 22  ? 53.602 -29.873 -9.388  1.00 21.59 ?  22  ASP   B HB2  1 
ATOM   4653 H HB3  . ASP   B 1 22  ? 53.652 -28.609 -10.346 1.00 21.59 ?  22  ASP   B HB3  1 
ATOM   4654 N N    . ILE   B 1 23  ? 50.754 -26.788 -8.366  1.00 14.66 ?  23  ILE   B N    1 
ATOM   4655 C CA   . ILE   B 1 23  ? 50.170 -25.440 -8.428  1.00 13.61 ?  23  ILE   B CA   1 
ATOM   4656 C C    . ILE   B 1 23  ? 51.231 -24.349 -8.570  1.00 13.35 ?  23  ILE   B C    1 
ATOM   4657 O O    . ILE   B 1 23  ? 50.965 -23.308 -9.180  1.00 12.75 ?  23  ILE   B O    1 
ATOM   4658 C CB   . ILE   B 1 23  ? 49.238 -25.190 -7.225  1.00 14.37 ?  23  ILE   B CB   1 
ATOM   4659 C CG1  . ILE   B 1 23  ? 48.422 -23.912 -7.429  1.00 14.63 ?  23  ILE   B CG1  1 
ATOM   4660 C CG2  . ILE   B 1 23  ? 50.019 -25.172 -5.917  1.00 15.28 ?  23  ILE   B CG2  1 
ATOM   4661 C CD1  . ILE   B 1 23  ? 47.294 -23.752 -6.425  1.00 16.37 ?  23  ILE   B CD1  1 
ATOM   4662 H H    . ILE   B 1 23  ? 50.593 -27.213 -7.637  1.00 17.60 ?  23  ILE   B H    1 
ATOM   4663 H HA   . ILE   B 1 23  ? 49.617 -25.396 -9.221  1.00 16.33 ?  23  ILE   B HA   1 
ATOM   4664 H HB   . ILE   B 1 23  ? 48.610 -25.929 -7.183  1.00 17.24 ?  23  ILE   B HB   1 
ATOM   4665 H HG12 . ILE   B 1 23  ? 49.020 -23.146 -7.334  1.00 17.55 ?  23  ILE   B HG12 1 
ATOM   4666 H HG13 . ILE   B 1 23  ? 48.044 -23.919 -8.320  1.00 17.55 ?  23  ILE   B HG13 1 
ATOM   4667 H HG21 . ILE   B 1 23  ? 49.398 -25.150 -5.176  1.00 18.33 ?  23  ILE   B HG21 1 
ATOM   4668 H HG22 . ILE   B 1 23  ? 50.564 -25.979 -5.865  1.00 18.33 ?  23  ILE   B HG22 1 
ATOM   4669 H HG23 . ILE   B 1 23  ? 50.592 -24.391 -5.899  1.00 18.33 ?  23  ILE   B HG23 1 
ATOM   4670 H HD11 . ILE   B 1 23  ? 46.786 -22.958 -6.650  1.00 19.64 ?  23  ILE   B HD11 1 
ATOM   4671 H HD12 . ILE   B 1 23  ? 46.724 -24.535 -6.474  1.00 19.64 ?  23  ILE   B HD12 1 
ATOM   4672 H HD13 . ILE   B 1 23  ? 47.669 -23.668 -5.537  1.00 19.64 ?  23  ILE   B HD13 1 
ATOM   4673 N N    . VAL   B 1 24  ? 52.430 -24.554 -8.015  1.00 13.53 ?  24  VAL   B N    1 
ATOM   4674 C CA   . VAL   B 1 24  ? 53.503 -23.566 -8.176  1.00 14.24 ?  24  VAL   B CA   1 
ATOM   4675 C C    . VAL   B 1 24  ? 53.967 -23.519 -9.625  1.00 14.37 ?  24  VAL   B C    1 
ATOM   4676 O O    . VAL   B 1 24  ? 54.103 -22.443 -10.226 1.00 15.27 ?  24  VAL   B O    1 
ATOM   4677 C CB   . VAL   B 1 24  ? 54.676 -23.888 -7.227  1.00 14.42 ?  24  VAL   B CB   1 
ATOM   4678 C CG1  . VAL   B 1 24  ? 55.890 -23.001 -7.540  1.00 15.87 ?  24  VAL   B CG1  1 
ATOM   4679 C CG2  . VAL   B 1 24  ? 54.251 -23.733 -5.787  1.00 15.60 ?  24  VAL   B CG2  1 
ATOM   4680 H H    . VAL   B 1 24  ? 52.644 -25.245 -7.552  1.00 16.24 ?  24  VAL   B H    1 
ATOM   4681 H HA   . VAL   B 1 24  ? 53.159 -22.690 -7.940  1.00 17.09 ?  24  VAL   B HA   1 
ATOM   4682 H HB   . VAL   B 1 24  ? 54.940 -24.810 -7.357  1.00 17.31 ?  24  VAL   B HB   1 
ATOM   4683 H HG11 . VAL   B 1 24  ? 56.488 -23.005 -6.775  1.00 19.05 ?  24  VAL   B HG11 1 
ATOM   4684 H HG12 . VAL   B 1 24  ? 56.349 -23.357 -8.317  1.00 19.05 ?  24  VAL   B HG12 1 
ATOM   4685 H HG13 . VAL   B 1 24  ? 55.587 -22.097 -7.716  1.00 19.05 ?  24  VAL   B HG13 1 
ATOM   4686 H HG21 . VAL   B 1 24  ? 54.971 -24.024 -5.209  1.00 18.72 ?  24  VAL   B HG21 1 
ATOM   4687 H HG22 . VAL   B 1 24  ? 54.046 -22.799 -5.616  1.00 18.72 ?  24  VAL   B HG22 1 
ATOM   4688 H HG23 . VAL   B 1 24  ? 53.459 -24.276 -5.628  1.00 18.72 ?  24  VAL   B HG23 1 
ATOM   4689 N N    . GLU   B 1 25  ? 54.242 -24.693 -10.201 1.00 15.15 ?  25  GLU   B N    1 
ATOM   4690 C CA   . GLU   B 1 25  ? 54.627 -24.750 -11.603 1.00 17.09 ?  25  GLU   B CA   1 
ATOM   4691 C C    . GLU   B 1 25  ? 53.519 -24.204 -12.491 1.00 16.07 ?  25  GLU   B C    1 
ATOM   4692 O O    . GLU   B 1 25  ? 53.789 -23.477 -13.456 1.00 17.05 ?  25  GLU   B O    1 
ATOM   4693 C CB   . GLU   B 1 25  ? 55.006 -26.179 -11.988 1.00 22.71 ?  25  GLU   B CB   1 
ATOM   4694 C CG   . GLU   B 1 25  ? 56.304 -26.642 -11.331 1.00 29.78 ?  25  GLU   B CG   1 
ATOM   4695 C CD   . GLU   B 1 25  ? 57.432 -25.620 -11.420 1.00 35.82 ?  25  GLU   B CD   1 
ATOM   4696 O OE1  . GLU   B 1 25  ? 57.810 -25.240 -12.549 1.00 38.34 ?  25  GLU   B OE1  1 
ATOM   4697 O OE2  . GLU   B 1 25  ? 57.934 -25.183 -10.357 1.00 37.88 -1 25  GLU   B OE2  1 
ATOM   4698 H H    . GLU   B 1 25  ? 54.209 -25.455 -9.802  1.00 18.18 ?  25  GLU   B H    1 
ATOM   4699 H HA   . GLU   B 1 25  ? 55.392 -24.174 -11.736 1.00 20.51 ?  25  GLU   B HA   1 
ATOM   4700 H HB2  . GLU   B 1 25  ? 54.294 -26.781 -11.704 1.00 27.25 ?  25  GLU   B HB2  1 
ATOM   4701 H HB3  . GLU   B 1 25  ? 55.113 -26.229 -12.950 1.00 27.25 ?  25  GLU   B HB3  1 
ATOM   4702 H HG2  . GLU   B 1 25  ? 56.141 -26.802 -10.395 1.00 35.73 ?  25  GLU   B HG2  1 
ATOM   4703 H HG3  . GLU   B 1 25  ? 56.602 -27.450 -11.772 1.00 35.73 ?  25  GLU   B HG3  1 
ATOM   4704 N N    A GLU   B 1 26  ? 52.266 -24.533 -12.173 0.52 14.71 ?  26  GLU   B N    1 
ATOM   4705 N N    B GLU   B 1 26  ? 52.263 -24.528 -12.170 0.48 15.07 ?  26  GLU   B N    1 
ATOM   4706 C CA   A GLU   B 1 26  ? 51.145 -23.996 -12.937 0.52 15.65 ?  26  GLU   B CA   1 
ATOM   4707 C CA   B GLU   B 1 26  ? 51.142 -24.000 -12.944 0.48 16.22 ?  26  GLU   B CA   1 
ATOM   4708 C C    A GLU   B 1 26  ? 51.111 -22.478 -12.865 0.52 14.84 ?  26  GLU   B C    1 
ATOM   4709 C C    B GLU   B 1 26  ? 51.074 -22.482 -12.860 0.48 15.00 ?  26  GLU   B C    1 
ATOM   4710 O O    A GLU   B 1 26  ? 50.946 -21.803 -13.886 0.52 16.14 ?  26  GLU   B O    1 
ATOM   4711 O O    B GLU   B 1 26  ? 50.834 -21.812 -13.869 0.48 15.96 ?  26  GLU   B O    1 
ATOM   4712 C CB   A GLU   B 1 26  ? 49.829 -24.579 -12.425 0.52 16.46 ?  26  GLU   B CB   1 
ATOM   4713 C CB   B GLU   B 1 26  ? 49.823 -24.606 -12.460 0.48 18.09 ?  26  GLU   B CB   1 
ATOM   4714 C CG   A GLU   B 1 26  ? 49.484 -25.933 -13.009 0.52 19.31 ?  26  GLU   B CG   1 
ATOM   4715 C CG   B GLU   B 1 26  ? 49.355 -25.822 -13.241 0.48 21.79 ?  26  GLU   B CG   1 
ATOM   4716 C CD   A GLU   B 1 26  ? 49.293 -25.915 -14.528 0.52 19.54 ?  26  GLU   B CD   1 
ATOM   4717 C CD   B GLU   B 1 26  ? 48.981 -25.485 -14.683 0.48 22.31 ?  26  GLU   B CD   1 
ATOM   4718 O OE1  A GLU   B 1 26  ? 48.461 -25.133 -15.038 0.52 19.28 ?  26  GLU   B OE1  1 
ATOM   4719 O OE1  B GLU   B 1 26  ? 47.870 -24.958 -14.925 0.48 23.46 ?  26  GLU   B OE1  1 
ATOM   4720 O OE2  A GLU   B 1 26  ? 49.972 -26.705 -15.208 0.52 20.77 -1 26  GLU   B OE2  1 
ATOM   4721 O OE2  B GLU   B 1 26  ? 49.794 -25.751 -15.578 0.48 22.47 -1 26  GLU   B OE2  1 
ATOM   4722 H H    A GLU   B 1 26  ? 52.039 -25.054 -11.524 0.52 17.65 ?  26  GLU   B H    1 
ATOM   4723 H H    B GLU   B 1 26  ? 52.036 -25.042 -11.518 0.48 18.08 ?  26  GLU   B H    1 
ATOM   4724 H HA   A GLU   B 1 26  ? 51.247 -24.250 -13.865 0.52 18.78 ?  26  GLU   B HA   1 
ATOM   4725 H HA   B GLU   B 1 26  ? 51.264 -24.242 -13.874 0.48 19.47 ?  26  GLU   B HA   1 
ATOM   4726 H HB2  A GLU   B 1 26  ? 49.887 -24.678 -11.455 0.52 19.75 ?  26  GLU   B HB2  1 
ATOM   4727 H HB2  B GLU   B 1 26  ? 49.924 -24.868 -11.532 0.48 21.71 ?  26  GLU   B HB2  1 
ATOM   4728 H HB3  A GLU   B 1 26  ? 49.108 -23.964 -12.640 0.52 19.75 ?  26  GLU   B HB3  1 
ATOM   4729 H HB3  B GLU   B 1 26  ? 49.129 -23.929 -12.533 0.48 21.71 ?  26  GLU   B HB3  1 
ATOM   4730 H HG2  A GLU   B 1 26  ? 50.215 -26.529 -12.823 0.52 23.17 ?  26  GLU   B HG2  1 
ATOM   4731 H HG2  B GLU   B 1 26  ? 50.059 -26.494 -13.210 0.48 26.15 ?  26  GLU   B HG2  1 
ATOM   4732 H HG3  A GLU   B 1 26  ? 48.668 -26.243 -12.592 0.52 23.17 ?  26  GLU   B HG3  1 
ATOM   4733 H HG3  B GLU   B 1 26  ? 48.551 -26.168 -12.833 0.48 26.15 ?  26  GLU   B HG3  1 
ATOM   4734 N N    . ALA   B 1 27  ? 51.247 -21.921 -11.659 1.00 14.05 ?  27  ALA   B N    1 
ATOM   4735 C CA   . ALA   B 1 27  ? 51.197 -20.470 -11.514 1.00 13.46 ?  27  ALA   B CA   1 
ATOM   4736 C C    . ALA   B 1 27  ? 52.259 -19.803 -12.380 1.00 14.74 ?  27  ALA   B C    1 
ATOM   4737 O O    . ALA   B 1 27  ? 51.982 -18.816 -13.075 1.00 15.28 ?  27  ALA   B O    1 
ATOM   4738 C CB   . ALA   B 1 27  ? 51.350 -20.076 -10.044 1.00 13.87 ?  27  ALA   B CB   1 
ATOM   4739 H H    A ALA   B 1 27  ? 51.366 -22.355 -10.925 0.52 16.86 ?  27  ALA   B H    1 
ATOM   4740 H H    B ALA   B 1 27  ? 51.378 -22.355 -10.927 0.48 16.86 ?  27  ALA   B H    1 
ATOM   4741 H HA   . ALA   B 1 27  ? 50.334 -20.155 -11.814 1.00 16.15 ?  27  ALA   B HA   1 
ATOM   4742 H HB1  . ALA   B 1 27  ? 51.308 -19.108 -9.971  1.00 16.65 ?  27  ALA   B HB1  1 
ATOM   4743 H HB2  . ALA   B 1 27  ? 50.627 -20.475 -9.534  1.00 16.65 ?  27  ALA   B HB2  1 
ATOM   4744 H HB3  . ALA   B 1 27  ? 52.203 -20.395 -9.715  1.00 16.65 ?  27  ALA   B HB3  1 
ATOM   4745 N N    . LYS   B 1 28  ? 53.482 -20.342 -12.374 1.00 16.33 ?  28  LYS   B N    1 
ATOM   4746 C CA   . LYS   B 1 28  ? 54.547 -19.729 -13.157 1.00 18.02 ?  28  LYS   B CA   1 
ATOM   4747 C C    . LYS   B 1 28  ? 54.289 -19.833 -14.657 1.00 18.68 ?  28  LYS   B C    1 
ATOM   4748 O O    . LYS   B 1 28  ? 54.705 -18.946 -15.415 1.00 20.09 ?  28  LYS   B O    1 
ATOM   4749 C CB   . LYS   B 1 28  ? 55.911 -20.309 -12.762 1.00 21.82 ?  28  LYS   B CB   1 
ATOM   4750 C CG   . LYS   B 1 28  ? 56.297 -19.988 -11.315 1.00 25.59 ?  28  LYS   B CG   1 
ATOM   4751 C CD   . LYS   B 1 28  ? 57.719 -20.415 -10.957 1.00 31.49 ?  28  LYS   B CD   1 
ATOM   4752 C CE   . LYS   B 1 28  ? 57.806 -21.898 -10.714 1.00 36.50 ?  28  LYS   B CE   1 
ATOM   4753 N NZ   . LYS   B 1 28  ? 59.142 -22.293 -10.178 1.00 39.04 ?  28  LYS   B NZ   1 
ATOM   4754 H H    . LYS   B 1 28  ? 53.715 -21.045 -11.934 1.00 19.60 ?  28  LYS   B H    1 
ATOM   4755 H HA   . LYS   B 1 28  ? 54.572 -18.786 -12.947 1.00 21.63 ?  28  LYS   B HA   1 
ATOM   4756 H HB2  . LYS   B 1 28  ? 55.890 -21.271 -12.857 1.00 26.18 ?  28  LYS   B HB2  1 
ATOM   4757 H HB3  . LYS   B 1 28  ? 56.595 -19.932 -13.341 1.00 26.18 ?  28  LYS   B HB3  1 
ATOM   4758 H HG2  . LYS   B 1 28  ? 56.228 -19.028 -11.181 1.00 30.71 ?  28  LYS   B HG2  1 
ATOM   4759 H HG3  . LYS   B 1 28  ? 55.688 -20.449 -10.722 1.00 30.71 ?  28  LYS   B HG3  1 
ATOM   4760 H HD2  . LYS   B 1 28  ? 58.312 -20.186 -11.691 1.00 37.79 ?  28  LYS   B HD2  1 
ATOM   4761 H HD3  . LYS   B 1 28  ? 57.992 -19.951 -10.150 1.00 37.79 ?  28  LYS   B HD3  1 
ATOM   4762 H HE2  . LYS   B 1 28  ? 57.130 -22.155 -10.066 1.00 43.80 ?  28  LYS   B HE2  1 
ATOM   4763 H HE3  . LYS   B 1 28  ? 57.662 -22.368 -11.550 1.00 43.80 ?  28  LYS   B HE3  1 
ATOM   4764 H HZ1  . LYS   B 1 28  ? 59.168 -23.171 -10.043 1.00 46.84 ?  28  LYS   B HZ1  1 
ATOM   4765 H HZ2  . LYS   B 1 28  ? 59.779 -22.069 -10.758 1.00 46.84 ?  28  LYS   B HZ2  1 
ATOM   4766 H HZ3  . LYS   B 1 28  ? 59.295 -21.876 -9.406  1.00 46.84 ?  28  LYS   B HZ3  1 
ATOM   4767 N N    A LYS   B 1 29  ? 53.616 -20.895 -15.107 0.52 19.99 ?  29  LYS   B N    1 
ATOM   4768 N N    B LYS   B 1 29  ? 53.587 -20.877 -15.104 0.48 20.06 ?  29  LYS   B N    1 
ATOM   4769 C CA   A LYS   B 1 29  ? 53.342 -21.035 -16.534 0.52 22.17 ?  29  LYS   B CA   1 
ATOM   4770 C CA   B LYS   B 1 29  ? 53.335 -21.064 -16.529 0.48 22.13 ?  29  LYS   B CA   1 
ATOM   4771 C C    A LYS   B 1 29  ? 52.105 -20.249 -16.959 0.52 20.74 ?  29  LYS   B C    1 
ATOM   4772 C C    B LYS   B 1 29  ? 52.071 -20.356 -17.007 0.48 20.60 ?  29  LYS   B C    1 
ATOM   4773 O O    A LYS   B 1 29  ? 52.135 -19.551 -17.979 0.52 22.29 ?  29  LYS   B O    1 
ATOM   4774 O O    B LYS   B 1 29  ? 52.036 -19.860 -18.138 0.48 21.57 ?  29  LYS   B O    1 
ATOM   4775 C CB   A LYS   B 1 29  ? 53.205 -22.512 -16.910 0.52 26.40 ?  29  LYS   B CB   1 
ATOM   4776 C CB   B LYS   B 1 29  ? 53.226 -22.554 -16.864 0.48 26.30 ?  29  LYS   B CB   1 
ATOM   4777 C CG   A LYS   B 1 29  ? 52.957 -22.749 -18.394 0.52 30.69 ?  29  LYS   B CG   1 
ATOM   4778 C CG   B LYS   B 1 29  ? 52.968 -22.826 -18.340 0.48 30.52 ?  29  LYS   B CG   1 
ATOM   4779 C CD   A LYS   B 1 29  ? 53.138 -24.214 -18.757 0.52 33.63 ?  29  LYS   B CD   1 
ATOM   4780 C CD   B LYS   B 1 29  ? 53.128 -24.301 -18.685 0.48 33.49 ?  29  LYS   B CD   1 
ATOM   4781 C CE   A LYS   B 1 29  ? 52.109 -25.091 -18.066 0.52 35.65 ?  29  LYS   B CE   1 
ATOM   4782 C CE   B LYS   B 1 29  ? 51.981 -25.142 -18.147 0.48 35.56 ?  29  LYS   B CE   1 
ATOM   4783 N NZ   A LYS   B 1 29  ? 52.329 -26.531 -18.368 0.52 36.77 ?  29  LYS   B NZ   1 
ATOM   4784 N NZ   B LYS   B 1 29  ? 52.186 -26.593 -18.429 0.48 36.67 ?  29  LYS   B NZ   1 
ATOM   4785 H H    A LYS   B 1 29  ? 53.314 -21.539 -14.617 0.52 23.98 ?  29  LYS   B H    1 
ATOM   4786 H H    B LYS   B 1 29  ? 53.239 -21.488 -14.602 0.48 24.07 ?  29  LYS   B H    1 
ATOM   4787 H HA   A LYS   B 1 29  ? 54.090 -20.682 -17.030 0.52 26.60 ?  29  LYS   B HA   1 
ATOM   4788 H HA   B LYS   B 1 29  ? 54.087 -20.706 -17.025 0.48 26.55 ?  29  LYS   B HA   1 
ATOM   4789 H HB2  A LYS   B 1 29  ? 54.027 -22.977 -16.675 0.52 31.68 ?  29  LYS   B HB2  1 
ATOM   4790 H HB2  B LYS   B 1 29  ? 54.056 -22.992 -16.624 0.48 31.56 ?  29  LYS   B HB2  1 
ATOM   4791 H HB3  A LYS   B 1 29  ? 52.462 -22.896 -16.422 0.52 31.68 ?  29  LYS   B HB3  1 
ATOM   4792 H HB3  B LYS   B 1 29  ? 52.491 -22.936 -16.361 0.48 31.56 ?  29  LYS   B HB3  1 
ATOM   4793 H HG2  A LYS   B 1 29  ? 52.047 -22.494 -18.614 0.52 36.82 ?  29  LYS   B HG2  1 
ATOM   4794 H HG2  B LYS   B 1 29  ? 52.061 -22.560 -18.560 0.48 36.63 ?  29  LYS   B HG2  1 
ATOM   4795 H HG3  A LYS   B 1 29  ? 53.588 -22.227 -18.915 0.52 36.82 ?  29  LYS   B HG3  1 
ATOM   4796 H HG3  B LYS   B 1 29  ? 53.602 -22.318 -18.872 0.48 36.63 ?  29  LYS   B HG3  1 
ATOM   4797 H HD2  A LYS   B 1 29  ? 53.036 -24.323 -19.716 0.52 40.36 ?  29  LYS   B HD2  1 
ATOM   4798 H HD2  B LYS   B 1 29  ? 53.150 -24.403 -19.649 0.48 40.18 ?  29  LYS   B HD2  1 
ATOM   4799 H HD3  A LYS   B 1 29  ? 54.021 -24.505 -18.480 0.52 40.36 ?  29  LYS   B HD3  1 
ATOM   4800 H HD3  B LYS   B 1 29  ? 53.953 -24.632 -18.296 0.48 40.18 ?  29  LYS   B HD3  1 
ATOM   4801 H HE2  A LYS   B 1 29  ? 52.175 -24.973 -17.106 0.52 42.79 ?  29  LYS   B HE2  1 
ATOM   4802 H HE2  B LYS   B 1 29  ? 51.920 -25.026 -17.187 0.48 42.67 ?  29  LYS   B HE2  1 
ATOM   4803 H HE3  A LYS   B 1 29  ? 51.222 -24.844 -18.374 0.52 42.79 ?  29  LYS   B HE3  1 
ATOM   4804 H HE3  B LYS   B 1 29  ? 51.154 -24.865 -18.573 0.48 42.67 ?  29  LYS   B HE3  1 
ATOM   4805 H HZ1  A LYS   B 1 29  ? 51.716 -27.024 -17.954 0.52 44.12 ?  29  LYS   B HZ1  1 
ATOM   4806 H HZ1  B LYS   B 1 29  ? 51.504 -27.065 -18.106 0.48 44.00 ?  29  LYS   B HZ1  1 
ATOM   4807 H HZ2  A LYS   B 1 29  ? 52.269 -26.670 -19.245 0.52 44.12 ?  29  LYS   B HZ2  1 
ATOM   4808 H HZ2  B LYS   B 1 29  ? 52.241 -26.729 -19.307 0.48 44.00 ?  29  LYS   B HZ2  1 
ATOM   4809 H HZ3  A LYS   B 1 29  ? 53.137 -26.779 -18.090 0.52 44.12 ?  29  LYS   B HZ3  1 
ATOM   4810 H HZ3  B LYS   B 1 29  ? 52.939 -26.874 -18.046 0.48 44.00 ?  29  LYS   B HZ3  1 
ATOM   4811 N N    . VAL   B 1 30  ? 51.022 -20.337 -16.182 1.00 19.03 ?  30  VAL   B N    1 
ATOM   4812 C CA   . VAL   B 1 30  ? 49.739 -19.745 -16.577 1.00 19.06 ?  30  VAL   B CA   1 
ATOM   4813 C C    . VAL   B 1 30  ? 49.721 -18.235 -16.405 1.00 17.12 ?  30  VAL   B C    1 
ATOM   4814 O O    . VAL   B 1 30  ? 48.957 -17.532 -17.090 1.00 17.71 ?  30  VAL   B O    1 
ATOM   4815 C CB   . VAL   B 1 30  ? 48.635 -20.380 -15.707 1.00 21.79 ?  30  VAL   B CB   1 
ATOM   4816 C CG1  . VAL   B 1 30  ? 47.328 -19.609 -15.810 1.00 24.27 ?  30  VAL   B CG1  1 
ATOM   4817 C CG2  . VAL   B 1 30  ? 48.454 -21.862 -16.058 1.00 22.58 ?  30  VAL   B CG2  1 
ATOM   4818 H H    A VAL   B 1 30  ? 51.002 -20.735 -15.416 0.52 22.84 ?  30  VAL   B H    1 
ATOM   4819 H H    B VAL   B 1 30  ? 51.013 -20.697 -15.398 0.48 22.84 ?  30  VAL   B H    1 
ATOM   4820 H HA   . VAL   B 1 30  ? 49.553 -19.965 -17.505 1.00 22.87 ?  30  VAL   B HA   1 
ATOM   4821 H HB   . VAL   B 1 30  ? 48.916 -20.344 -14.780 1.00 26.15 ?  30  VAL   B HB   1 
ATOM   4822 H HG11 . VAL   B 1 30  ? 46.601 -20.212 -15.577 1.00 29.13 ?  30  VAL   B HG11 1 
ATOM   4823 H HG12 . VAL   B 1 30  ? 47.346 -18.866 -15.193 1.00 29.13 ?  30  VAL   B HG12 1 
ATOM   4824 H HG13 . VAL   B 1 30  ? 47.211 -19.303 -16.717 1.00 29.13 ?  30  VAL   B HG13 1 
ATOM   4825 H HG21 . VAL   B 1 30  ? 47.753 -22.241 -15.500 1.00 27.09 ?  30  VAL   B HG21 1 
ATOM   4826 H HG22 . VAL   B 1 30  ? 48.202 -21.939 -16.994 1.00 27.09 ?  30  VAL   B HG22 1 
ATOM   4827 H HG23 . VAL   B 1 30  ? 49.287 -22.332 -15.901 1.00 27.09 ?  30  VAL   B HG23 1 
ATOM   4828 N N    A LYS   B 1 31  ? 50.532 -17.714 -15.491 0.52 16.66 ?  31  LYS   B N    1 
ATOM   4829 N N    B LYS   B 1 31  ? 50.532 -17.717 -15.490 0.48 16.75 ?  31  LYS   B N    1 
ATOM   4830 C CA   A LYS   B 1 31  ? 50.540 -16.298 -15.143 0.52 17.35 ?  31  LYS   B CA   1 
ATOM   4831 C CA   B LYS   B 1 31  ? 50.541 -16.302 -15.141 0.48 17.37 ?  31  LYS   B CA   1 
ATOM   4832 C C    A LYS   B 1 31  ? 49.144 -15.796 -14.755 0.52 15.44 ?  31  LYS   B C    1 
ATOM   4833 C C    B LYS   B 1 31  ? 49.143 -15.804 -14.760 0.48 15.42 ?  31  LYS   B C    1 
ATOM   4834 O O    A LYS   B 1 31  ? 48.608 -14.879 -15.383 0.52 15.61 ?  31  LYS   B O    1 
ATOM   4835 O O    B LYS   B 1 31  ? 48.600 -14.901 -15.405 0.48 15.51 ?  31  LYS   B O    1 
ATOM   4836 C CB   A LYS   B 1 31  ? 51.150 -15.459 -16.260 0.52 20.37 ?  31  LYS   B CB   1 
ATOM   4837 C CB   B LYS   B 1 31  ? 51.155 -15.468 -16.258 0.48 20.31 ?  31  LYS   B CB   1 
ATOM   4838 C CG   A LYS   B 1 31  ? 52.601 -15.849 -16.560 0.52 23.34 ?  31  LYS   B CG   1 
ATOM   4839 C CG   B LYS   B 1 31  ? 52.587 -15.911 -16.588 0.48 23.20 ?  31  LYS   B CG   1 
ATOM   4840 C CD   A LYS   B 1 31  ? 53.193 -15.034 -17.694 0.52 26.96 ?  31  LYS   B CD   1 
ATOM   4841 C CD   B LYS   B 1 31  ? 53.171 -15.160 -17.767 0.48 26.55 ?  31  LYS   B CD   1 
ATOM   4842 C CE   A LYS   B 1 31  ? 54.678 -15.304 -17.840 0.52 29.86 ?  31  LYS   B CE   1 
ATOM   4843 C CE   B LYS   B 1 31  ? 54.675 -15.351 -17.841 0.48 29.14 ?  31  LYS   B CE   1 
ATOM   4844 N NZ   A LYS   B 1 31  ? 55.424 -14.936 -16.601 0.52 31.05 ?  31  LYS   B NZ   1 
ATOM   4845 N NZ   B LYS   B 1 31  ? 55.352 -14.829 -16.617 0.48 30.17 ?  31  LYS   B NZ   1 
ATOM   4846 H H    A LYS   B 1 31  ? 51.113 -18.183 -15.059 0.52 19.99 ?  31  LYS   B H    1 
ATOM   4847 H H    B LYS   B 1 31  ? 51.113 -18.188 -15.059 0.48 20.09 ?  31  LYS   B H    1 
ATOM   4848 H HA   A LYS   B 1 31  ? 51.109 -16.198 -14.371 0.52 20.82 ?  31  LYS   B HA   1 
ATOM   4849 H HA   B LYS   B 1 31  ? 51.105 -16.201 -14.366 0.48 20.85 ?  31  LYS   B HA   1 
ATOM   4850 H HB2  A LYS   B 1 31  ? 50.636 -15.581 -17.072 0.52 24.44 ?  31  LYS   B HB2  1 
ATOM   4851 H HB2  B LYS   B 1 31  ? 50.623 -15.560 -17.061 0.48 24.37 ?  31  LYS   B HB2  1 
ATOM   4852 H HB3  A LYS   B 1 31  ? 51.142 -14.530 -15.991 0.52 24.44 ?  31  LYS   B HB3  1 
ATOM   4853 H HB3  B LYS   B 1 31  ? 51.186 -14.542 -15.976 0.48 24.37 ?  31  LYS   B HB3  1 
ATOM   4854 H HG2  A LYS   B 1 31  ? 53.138 -15.701 -15.766 0.52 28.01 ?  31  LYS   B HG2  1 
ATOM   4855 H HG2  B LYS   B 1 31  ? 53.151 -15.752 -15.815 0.48 27.83 ?  31  LYS   B HG2  1 
ATOM   4856 H HG3  A LYS   B 1 31  ? 52.636 -16.786 -16.813 0.52 28.01 ?  31  LYS   B HG3  1 
ATOM   4857 H HG3  B LYS   B 1 31  ? 52.587 -16.857 -16.807 0.48 27.83 ?  31  LYS   B HG3  1 
ATOM   4858 H HD2  A LYS   B 1 31  ? 52.752 -15.277 -18.523 0.52 32.35 ?  31  LYS   B HD2  1 
ATOM   4859 H HD2  B LYS   B 1 31  ? 52.779 -15.501 -18.587 0.48 31.86 ?  31  LYS   B HD2  1 
ATOM   4860 H HD3  A LYS   B 1 31  ? 53.069 -14.092 -17.507 0.52 32.35 ?  31  LYS   B HD3  1 
ATOM   4861 H HD3  B LYS   B 1 31  ? 52.985 -14.216 -17.668 0.48 31.86 ?  31  LYS   B HD3  1 
ATOM   4862 H HE2  A LYS   B 1 31  ? 54.818 -16.251 -18.008 0.52 35.83 ?  31  LYS   B HE2  1 
ATOM   4863 H HE2  B LYS   B 1 31  ? 54.876 -16.298 -17.920 0.48 34.97 ?  31  LYS   B HE2  1 
ATOM   4864 H HE3  A LYS   B 1 31  ? 55.029 -14.778 -18.575 0.52 35.83 ?  31  LYS   B HE3  1 
ATOM   4865 H HE3  B LYS   B 1 31  ? 55.021 -14.870 -18.608 0.48 34.97 ?  31  LYS   B HE3  1 
ATOM   4866 H HZ1  A LYS   B 1 31  ? 56.300 -14.989 -16.745 0.52 37.26 ?  31  LYS   B HZ1  1 
ATOM   4867 H HZ1  B LYS   B 1 31  ? 56.232 -14.802 -16.744 0.48 36.20 ?  31  LYS   B HZ1  1 
ATOM   4868 H HZ2  A LYS   B 1 31  ? 55.221 -14.103 -16.361 0.52 37.26 ?  31  LYS   B HZ2  1 
ATOM   4869 H HZ2  B LYS   B 1 31  ? 55.060 -14.009 -16.434 0.48 36.20 ?  31  LYS   B HZ2  1 
ATOM   4870 H HZ3  A LYS   B 1 31  ? 55.207 -15.488 -15.937 0.52 37.26 ?  31  LYS   B HZ3  1 
ATOM   4871 H HZ3  B LYS   B 1 31  ? 55.178 -15.359 -15.922 0.48 36.20 ?  31  LYS   B HZ3  1 
ATOM   4872 N N    . PRO   B 1 32  ? 48.543 -16.370 -13.712 1.00 14.14 ?  32  PRO   B N    1 
ATOM   4873 C CA   . PRO   B 1 32  ? 47.172 -15.995 -13.343 1.00 13.59 ?  32  PRO   B CA   1 
ATOM   4874 C C    . PRO   B 1 32  ? 47.102 -14.656 -12.623 1.00 13.64 ?  32  PRO   B C    1 
ATOM   4875 O O    . PRO   B 1 32  ? 48.036 -14.238 -11.931 1.00 15.00 ?  32  PRO   B O    1 
ATOM   4876 C CB   . PRO   B 1 32  ? 46.771 -17.109 -12.370 1.00 14.17 ?  32  PRO   B CB   1 
ATOM   4877 C CG   . PRO   B 1 32  ? 48.080 -17.440 -11.688 1.00 14.07 ?  32  PRO   B CG   1 
ATOM   4878 C CD   . PRO   B 1 32  ? 49.133 -17.327 -12.755 1.00 14.23 ?  32  PRO   B CD   1 
ATOM   4879 H HA   . PRO   B 1 32  ? 46.587 -16.000 -14.126 1.00 16.31 ?  32  PRO   B HA   1 
ATOM   4880 H HB2  . PRO   B 1 32  ? 46.117 -16.772 -11.738 1.00 17.00 ?  32  PRO   B HB2  1 
ATOM   4881 H HB3  . PRO   B 1 32  ? 46.424 -17.872 -12.859 1.00 17.00 ?  32  PRO   B HB3  1 
ATOM   4882 H HG2  . PRO   B 1 32  ? 48.247 -16.803 -10.974 1.00 16.88 ?  32  PRO   B HG2  1 
ATOM   4883 H HG3  . PRO   B 1 32  ? 48.046 -18.344 -11.337 1.00 16.88 ?  32  PRO   B HG3  1 
ATOM   4884 H HD2  . PRO   B 1 32  ? 49.952 -16.966 -12.382 1.00 17.08 ?  32  PRO   B HD2  1 
ATOM   4885 H HD3  . PRO   B 1 32  ? 49.279 -18.187 -13.175 1.00 17.08 ?  32  PRO   B HD3  1 
ATOM   4886 N N    . THR   B 1 33  ? 45.951 -13.989 -12.775 1.00 13.45 ?  33  THR   B N    1 
ATOM   4887 C CA   . THR   B 1 33  ? 45.677 -12.814 -11.956 1.00 13.28 ?  33  THR   B CA   1 
ATOM   4888 C C    . THR   B 1 33  ? 45.646 -13.173 -10.475 1.00 12.89 ?  33  THR   B C    1 
ATOM   4889 O O    . THR   B 1 33  ? 46.137 -12.406 -9.634  1.00 14.24 ?  33  THR   B O    1 
ATOM   4890 C CB   . THR   B 1 33  ? 44.356 -12.173 -12.387 1.00 14.18 ?  33  THR   B CB   1 
ATOM   4891 O OG1  . THR   B 1 33  ? 44.374 -11.917 -13.795 1.00 14.45 ?  33  THR   B OG1  1 
ATOM   4892 C CG2  . THR   B 1 33  ? 44.124 -10.872 -11.639 1.00 16.27 ?  33  THR   B CG2  1 
ATOM   4893 H H    . THR   B 1 33  ? 45.328 -14.205 -13.334 1.00 16.14 ?  33  THR   B H    1 
ATOM   4894 H HA   . THR   B 1 33  ? 46.385 -12.169 -12.101 1.00 15.94 ?  33  THR   B HA   1 
ATOM   4895 H HB   . THR   B 1 33  ? 43.628 -12.786 -12.188 1.00 17.02 ?  33  THR   B HB   1 
ATOM   4896 H HG1  . THR   B 1 33  ? 43.649 -11.562 -14.036 1.00 17.33 ?  33  THR   B HG1  1 
ATOM   4897 H HG21 . THR   B 1 33  ? 43.364 -10.409 -12.014 1.00 19.52 ?  33  THR   B HG21 1 
ATOM   4898 H HG22 . THR   B 1 33  ? 43.951 -11.060 -10.702 1.00 19.52 ?  33  THR   B HG22 1 
ATOM   4899 H HG23 . THR   B 1 33  ? 44.909 -10.309 -11.709 1.00 19.52 ?  33  THR   B HG23 1 
ATOM   4900 N N    . VAL   B 1 34  ? 45.059 -14.325 -10.131 1.00 12.53 ?  34  VAL   B N    1 
ATOM   4901 C CA   . VAL   B 1 34  ? 44.852 -14.719 -8.741  1.00 12.20 ?  34  VAL   B CA   1 
ATOM   4902 C C    . VAL   B 1 34  ? 45.271 -16.171 -8.568  1.00 11.41 ?  34  VAL   B C    1 
ATOM   4903 O O    . VAL   B 1 34  ? 44.748 -17.055 -9.256  1.00 12.39 ?  34  VAL   B O    1 
ATOM   4904 C CB   . VAL   B 1 34  ? 43.375 -14.564 -8.307  1.00 13.68 ?  34  VAL   B CB   1 
ATOM   4905 C CG1  . VAL   B 1 34  ? 43.193 -15.020 -6.860  1.00 14.45 ?  34  VAL   B CG1  1 
ATOM   4906 C CG2  . VAL   B 1 34  ? 42.897 -13.132 -8.508  1.00 14.78 ?  34  VAL   B CG2  1 
ATOM   4907 H H    . VAL   B 1 34  ? 44.783 -14.917 -10.702 1.00 15.04 ?  34  VAL   B H    1 
ATOM   4908 H HA   . VAL   B 1 34  ? 45.402 -14.175 -8.164  1.00 14.64 ?  34  VAL   B HA   1 
ATOM   4909 H HB   . VAL   B 1 34  ? 42.828 -15.132 -8.872  1.00 16.41 ?  34  VAL   B HB   1 
ATOM   4910 H HG11 . VAL   B 1 34  ? 42.336 -14.698 -6.532  1.00 17.34 ?  34  VAL   B HG11 1 
ATOM   4911 H HG12 . VAL   B 1 34  ? 43.206 -15.992 -6.827  1.00 17.34 ?  34  VAL   B HG12 1 
ATOM   4912 H HG13 . VAL   B 1 34  ? 43.909 -14.660 -6.317  1.00 17.34 ?  34  VAL   B HG13 1 
ATOM   4913 H HG21 . VAL   B 1 34  ? 41.979 -13.062 -8.206  1.00 17.73 ?  34  VAL   B HG21 1 
ATOM   4914 H HG22 . VAL   B 1 34  ? 43.463 -12.534 -8.001  1.00 17.73 ?  34  VAL   B HG22 1 
ATOM   4915 H HG23 . VAL   B 1 34  ? 42.947 -12.911 -9.456  1.00 17.73 ?  34  VAL   B HG23 1 
ATOM   4916 N N    . VAL   B 1 35  ? 46.156 -16.426 -7.610  1.00 10.78 ?  35  VAL   B N    1 
ATOM   4917 C CA   . VAL   B 1 35  ? 46.377 -17.775 -7.091  1.00 11.04 ?  35  VAL   B CA   1 
ATOM   4918 C C    . VAL   B 1 35  ? 45.827 -17.830 -5.672  1.00 10.70 ?  35  VAL   B C    1 
ATOM   4919 O O    . VAL   B 1 35  ? 46.045 -16.912 -4.874  1.00 10.96 ?  35  VAL   B O    1 
ATOM   4920 C CB   . VAL   B 1 35  ? 47.855 -18.222 -7.165  1.00 11.44 ?  35  VAL   B CB   1 
ATOM   4921 C CG1  . VAL   B 1 35  ? 48.757 -17.381 -6.249  1.00 12.72 ?  35  VAL   B CG1  1 
ATOM   4922 C CG2  . VAL   B 1 35  ? 47.979 -19.716 -6.841  1.00 12.66 ?  35  VAL   B CG2  1 
ATOM   4923 H H    . VAL   B 1 35  ? 46.651 -15.826 -7.236  1.00 12.94 ?  35  VAL   B H    1 
ATOM   4924 H HA   . VAL   B 1 35  ? 45.864 -18.399 -7.620  1.00 13.25 ?  35  VAL   B HA   1 
ATOM   4925 H HB   . VAL   B 1 35  ? 48.168 -18.103 -8.076  1.00 13.73 ?  35  VAL   B HB   1 
ATOM   4926 H HG11 . VAL   B 1 35  ? 49.685 -17.619 -6.414  1.00 15.26 ?  35  VAL   B HG11 1 
ATOM   4927 H HG12 . VAL   B 1 35  ? 48.616 -16.444 -6.441  1.00 15.26 ?  35  VAL   B HG12 1 
ATOM   4928 H HG13 . VAL   B 1 35  ? 48.532 -17.569 -5.322  1.00 15.26 ?  35  VAL   B HG13 1 
ATOM   4929 H HG21 . VAL   B 1 35  ? 48.898 -19.994 -6.947  1.00 15.19 ?  35  VAL   B HG21 1 
ATOM   4930 H HG22 . VAL   B 1 35  ? 47.693 -19.865 -5.920  1.00 15.19 ?  35  VAL   B HG22 1 
ATOM   4931 H HG23 . VAL   B 1 35  ? 47.406 -20.222 -7.442  1.00 15.19 ?  35  VAL   B HG23 1 
ATOM   4932 N N    . VAL   B 1 36  ? 45.116 -18.915 -5.352  1.00 10.76 ?  36  VAL   B N    1 
ATOM   4933 C CA   . VAL   B 1 36  ? 44.570 -19.111 -4.018  1.00 9.88  ?  36  VAL   B CA   1 
ATOM   4934 C C    . VAL   B 1 36  ? 45.581 -19.866 -3.163  1.00 9.68  ?  36  VAL   B C    1 
ATOM   4935 O O    . VAL   B 1 36  ? 46.118 -20.903 -3.580  1.00 11.10 ?  36  VAL   B O    1 
ATOM   4936 C CB   . VAL   B 1 36  ? 43.233 -19.873 -4.088  1.00 10.43 ?  36  VAL   B CB   1 
ATOM   4937 C CG1  . VAL   B 1 36  ? 42.723 -20.222 -2.689  1.00 11.13 ?  36  VAL   B CG1  1 
ATOM   4938 C CG2  . VAL   B 1 36  ? 42.224 -19.060 -4.858  1.00 11.43 ?  36  VAL   B CG2  1 
ATOM   4939 H H    . VAL   B 1 36  ? 44.941 -19.556 -5.896  1.00 12.91 ?  36  VAL   B H    1 
ATOM   4940 H HA   . VAL   B 1 36  ? 44.407 -18.250 -3.604  1.00 11.85 ?  36  VAL   B HA   1 
ATOM   4941 H HB   . VAL   B 1 36  ? 43.367 -20.701 -4.566  1.00 12.51 ?  36  VAL   B HB   1 
ATOM   4942 H HG11 . VAL   B 1 36  ? 41.785 -20.472 -2.744  1.00 13.35 ?  36  VAL   B HG11 1 
ATOM   4943 H HG12 . VAL   B 1 36  ? 43.239 -20.965 -2.338  1.00 13.35 ?  36  VAL   B HG12 1 
ATOM   4944 H HG13 . VAL   B 1 36  ? 42.820 -19.447 -2.110  1.00 13.35 ?  36  VAL   B HG13 1 
ATOM   4945 H HG21 . VAL   B 1 36  ? 41.373 -19.532 -4.857  1.00 13.71 ?  36  VAL   B HG21 1 
ATOM   4946 H HG22 . VAL   B 1 36  ? 42.125 -18.195 -4.441  1.00 13.71 ?  36  VAL   B HG22 1 
ATOM   4947 H HG23 . VAL   B 1 36  ? 42.537 -18.958 -5.772  1.00 13.71 ?  36  VAL   B HG23 1 
ATOM   4948 N N    . ASN   B 1 37  ? 45.796 -19.379 -1.944  1.00 9.91  ?  37  ASN   B N    1 
ATOM   4949 C CA   . ASN   B 1 37  ? 46.539 -20.102 -0.923  1.00 10.27 ?  37  ASN   B CA   1 
ATOM   4950 C C    . ASN   B 1 37  ? 45.586 -20.777 0.061   1.00 11.09 ?  37  ASN   B C    1 
ATOM   4951 O O    . ASN   B 1 37  ? 44.577 -20.196 0.473   1.00 11.36 ?  37  ASN   B O    1 
ATOM   4952 C CB   . ASN   B 1 37  ? 47.461 -19.155 -0.151  1.00 9.95  ?  37  ASN   B CB   1 
ATOM   4953 C CG   . ASN   B 1 37  ? 48.313 -19.873 0.866   1.00 10.74 ?  37  ASN   B CG   1 
ATOM   4954 O OD1  . ASN   B 1 37  ? 48.657 -21.047 0.686   1.00 12.13 ?  37  ASN   B OD1  1 
ATOM   4955 N ND2  . ASN   B 1 37  ? 48.676 -19.171 1.939   1.00 11.25 ?  37  ASN   B ND2  1 
ATOM   4956 H H    . ASN   B 1 37  ? 45.507 -18.610 -1.675  1.00 11.89 ?  37  ASN   B H    1 
ATOM   4957 H HA   . ASN   B 1 37  ? 47.085 -20.786 -1.336  1.00 12.33 ?  37  ASN   B HA   1 
ATOM   4958 H HB2  . ASN   B 1 37  ? 48.058 -18.712 -0.773  1.00 11.94 ?  37  ASN   B HB2  1 
ATOM   4959 H HB3  . ASN   B 1 37  ? 46.926 -18.495 0.321   1.00 11.94 ?  37  ASN   B HB3  1 
ATOM   4960 H HD21 . ASN   B 1 37  ? 49.171 -19.530 2.545   1.00 13.50 ?  37  ASN   B HD21 1 
ATOM   4961 H HD22 . ASN   B 1 37  ? 48.432 -18.352 2.027   1.00 13.50 ?  37  ASN   B HD22 1 
ATOM   4962 N N    . ALA   B 1 38  ? 45.935 -22.004 0.446   1.00 11.22 ?  38  ALA   B N    1 
ATOM   4963 C CA   . ALA   B 1 38  ? 45.271 -22.741 1.517   1.00 11.33 ?  38  ALA   B CA   1 
ATOM   4964 C C    . ALA   B 1 38  ? 45.857 -22.257 2.841   1.00 11.82 ?  38  ALA   B C    1 
ATOM   4965 O O    . ALA   B 1 38  ? 46.756 -22.875 3.430   1.00 12.40 ?  38  ALA   B O    1 
ATOM   4966 C CB   . ALA   B 1 38  ? 45.490 -24.240 1.332   1.00 12.78 ?  38  ALA   B CB   1 
ATOM   4967 H H    . ALA   B 1 38  ? 46.594 -22.434 0.098   1.00 13.47 ?  38  ALA   B H    1 
ATOM   4968 H HA   . ALA   B 1 38  ? 44.322 -22.550 1.511   1.00 13.60 ?  38  ALA   B HA   1 
ATOM   4969 H HB1  . ALA   B 1 38  ? 45.038 -24.713 2.055   1.00 15.34 ?  38  ALA   B HB1  1 
ATOM   4970 H HB2  . ALA   B 1 38  ? 45.110 -24.507 0.482   1.00 15.34 ?  38  ALA   B HB2  1 
ATOM   4971 H HB3  . ALA   B 1 38  ? 46.435 -24.429 1.355   1.00 15.34 ?  38  ALA   B HB3  1 
ATOM   4972 N N    . ALA   B 1 39  ? 45.342 -21.113 3.299   1.00 10.79 ?  39  ALA   B N    1 
ATOM   4973 C CA   . ALA   B 1 39  ? 45.886 -20.390 4.441   1.00 11.21 ?  39  ALA   B CA   1 
ATOM   4974 C C    . ALA   B 1 39  ? 45.270 -20.839 5.769   1.00 10.65 ?  39  ALA   B C    1 
ATOM   4975 O O    . ALA   B 1 39  ? 44.234 -21.505 5.819   1.00 12.88 ?  39  ALA   B O    1 
ATOM   4976 C CB   . ALA   B 1 39  ? 45.661 -18.882 4.261   1.00 12.22 ?  39  ALA   B CB   1 
ATOM   4977 H H    . ALA   B 1 39  ? 44.650 -20.732 2.967   1.00 12.94 ?  39  ALA   B H    1 
ATOM   4978 H HA   . ALA   B 1 39  ? 46.846 -20.540 4.491   1.00 13.45 ?  39  ALA   B HA   1 
ATOM   4979 H HB1  . ALA   B 1 39  ? 46.030 -18.407 5.022   1.00 14.66 ?  39  ALA   B HB1  1 
ATOM   4980 H HB2  . ALA   B 1 39  ? 46.101 -18.591 3.446   1.00 14.66 ?  39  ALA   B HB2  1 
ATOM   4981 H HB3  . ALA   B 1 39  ? 44.707 -18.711 4.197   1.00 14.66 ?  39  ALA   B HB3  1 
ATOM   4982 N N    . ASN   B 1 40  ? 45.912 -20.429 6.861   1.00 11.42 ?  40  ASN   B N    1 
ATOM   4983 C CA   . ASN   B 1 40  ? 45.354 -20.478 8.200   1.00 12.24 ?  40  ASN   B CA   1 
ATOM   4984 C C    . ASN   B 1 40  ? 45.160 -19.048 8.718   1.00 12.43 ?  40  ASN   B C    1 
ATOM   4985 O O    . ASN   B 1 40  ? 45.565 -18.065 8.084   1.00 12.59 ?  40  ASN   B O    1 
ATOM   4986 C CB   . ASN   B 1 40  ? 46.211 -21.343 9.140   1.00 13.56 ?  40  ASN   B CB   1 
ATOM   4987 C CG   . ASN   B 1 40  ? 47.666 -20.926 9.165   1.00 15.19 ?  40  ASN   B CG   1 
ATOM   4988 O OD1  . ASN   B 1 40  ? 47.979 -19.735 9.220   1.00 17.24 ?  40  ASN   B OD1  1 
ATOM   4989 N ND2  . ASN   B 1 40  ? 48.569 -21.902 9.124   1.00 15.34 ?  40  ASN   B ND2  1 
ATOM   4990 H H    . ASN   B 1 40  ? 46.717 -20.110 6.840   1.00 13.71 ?  40  ASN   B H    1 
ATOM   4991 H HA   . ASN   B 1 40  ? 44.473 -20.880 8.148   1.00 14.68 ?  40  ASN   B HA   1 
ATOM   4992 H HB2  . ASN   B 1 40  ? 45.851 -21.272 10.041  1.00 16.27 ?  40  ASN   B HB2  1 
ATOM   4993 H HB3  . ASN   B 1 40  ? 46.163 -22.265 8.841   1.00 16.27 ?  40  ASN   B HB3  1 
ATOM   4994 H HD21 . ASN   B 1 40  ? 49.407 -21.717 9.146   1.00 18.41 ?  40  ASN   B HD21 1 
ATOM   4995 H HD22 . ASN   B 1 40  ? 48.311 -22.723 9.078   1.00 18.41 ?  40  ASN   B HD22 1 
ATOM   4996 N N    . VAL   B 1 41  ? 44.504 -18.925 9.874   1.00 12.92 ?  41  VAL   B N    1 
ATOM   4997 C CA   . VAL   B 1 41  ? 44.040 -17.606 10.324  1.00 13.80 ?  41  VAL   B CA   1 
ATOM   4998 C C    . VAL   B 1 41  ? 45.187 -16.644 10.607  1.00 13.74 ?  41  VAL   B C    1 
ATOM   4999 O O    . VAL   B 1 41  ? 45.017 -15.423 10.489  1.00 14.23 ?  41  VAL   B O    1 
ATOM   5000 C CB   . VAL   B 1 41  ? 43.076 -17.695 11.525  1.00 15.25 ?  41  VAL   B CB   1 
ATOM   5001 C CG1  . VAL   B 1 41  ? 41.760 -18.373 11.138  1.00 16.07 ?  41  VAL   B CG1  1 
ATOM   5002 C CG2  . VAL   B 1 41  ? 43.745 -18.364 12.721  1.00 16.34 ?  41  VAL   B CG2  1 
ATOM   5003 H H    . VAL   B 1 41  ? 44.309 -19.574 10.399  1.00 15.50 ?  41  VAL   B H    1 
ATOM   5004 H HA   . VAL   B 1 41  ? 43.527 -17.218 9.598   1.00 16.55 ?  41  VAL   B HA   1 
ATOM   5005 H HB   . VAL   B 1 41  ? 42.849 -16.789 11.799  1.00 18.30 ?  41  VAL   B HB   1 
ATOM   5006 H HG11 . VAL   B 1 41  ? 41.171 -18.390 11.909  1.00 19.28 ?  41  VAL   B HG11 1 
ATOM   5007 H HG12 . VAL   B 1 41  ? 41.346 -17.874 10.417  1.00 19.28 ?  41  VAL   B HG12 1 
ATOM   5008 H HG13 . VAL   B 1 41  ? 41.948 -19.280 10.847  1.00 19.28 ?  41  VAL   B HG13 1 
ATOM   5009 H HG21 . VAL   B 1 41  ? 43.111 -18.414 13.452  1.00 19.61 ?  41  VAL   B HG21 1 
ATOM   5010 H HG22 . VAL   B 1 41  ? 44.023 -19.258 12.464  1.00 19.61 ?  41  VAL   B HG22 1 
ATOM   5011 H HG23 . VAL   B 1 41  ? 44.515 -17.840 12.984  1.00 19.61 ?  41  VAL   B HG23 1 
ATOM   5012 N N    A TYR   B 1 42  ? 46.355 -17.155 10.994  0.52 13.91 ?  42  TYR   B N    1 
ATOM   5013 N N    B TYR   B 1 42  ? 46.353 -17.158 10.994  0.48 13.79 ?  42  TYR   B N    1 
ATOM   5014 C CA   A TYR   B 1 42  ? 47.505 -16.304 11.270  0.52 13.90 ?  42  TYR   B CA   1 
ATOM   5015 C CA   B TYR   B 1 42  ? 47.504 -16.315 11.277  0.48 13.68 ?  42  TYR   B CA   1 
ATOM   5016 C C    A TYR   B 1 42  ? 48.477 -16.220 10.094  0.52 12.94 ?  42  TYR   B C    1 
ATOM   5017 C C    B TYR   B 1 42  ? 48.481 -16.234 10.102  0.48 12.93 ?  42  TYR   B C    1 
ATOM   5018 O O    A TYR   B 1 42  ? 49.563 -15.645 10.235  0.52 14.77 ?  42  TYR   B O    1 
ATOM   5019 O O    B TYR   B 1 42  ? 49.575 -15.677 10.253  0.48 14.66 ?  42  TYR   B O    1 
ATOM   5020 C CB   A TYR   B 1 42  ? 48.192 -16.721 12.576  0.52 16.08 ?  42  TYR   B CB   1 
ATOM   5021 C CB   B TYR   B 1 42  ? 48.181 -16.747 12.584  0.48 15.42 ?  42  TYR   B CB   1 
ATOM   5022 C CG   A TYR   B 1 42  ? 47.606 -16.028 13.796  0.52 15.79 ?  42  TYR   B CG   1 
ATOM   5023 C CG   B TYR   B 1 42  ? 47.682 -15.975 13.802  0.48 14.59 ?  42  TYR   B CG   1 
ATOM   5024 C CD1  A TYR   B 1 42  ? 47.801 -14.664 13.997  0.52 15.20 ?  42  TYR   B CD1  1 
ATOM   5025 C CD1  B TYR   B 1 42  ? 47.945 -14.617 13.930  0.48 13.73 ?  42  TYR   B CD1  1 
ATOM   5026 C CD2  A TYR   B 1 42  ? 46.854 -16.722 14.735  0.52 17.10 ?  42  TYR   B CD2  1 
ATOM   5027 C CD2  B TYR   B 1 42  ? 46.952 -16.592 14.815  0.48 14.96 ?  42  TYR   B CD2  1 
ATOM   5028 C CE1  A TYR   B 1 42  ? 47.276 -14.019 15.098  0.52 15.86 ?  42  TYR   B CE1  1 
ATOM   5029 C CE1  B TYR   B 1 42  ? 47.506 -13.895 15.022  0.48 13.53 ?  42  TYR   B CE1  1 
ATOM   5030 C CE2  A TYR   B 1 42  ? 46.328 -16.085 15.842  0.52 17.32 ?  42  TYR   B CE2  1 
ATOM   5031 C CE2  B TYR   B 1 42  ? 46.511 -15.871 15.927  0.48 14.73 ?  42  TYR   B CE2  1 
ATOM   5032 C CZ   A TYR   B 1 42  ? 46.537 -14.730 16.017  0.52 17.38 ?  42  TYR   B CZ   1 
ATOM   5033 C CZ   B TYR   B 1 42  ? 46.794 -14.516 16.019  0.48 13.81 ?  42  TYR   B CZ   1 
ATOM   5034 O OH   A TYR   B 1 42  ? 46.014 -14.079 17.112  0.52 19.71 ?  42  TYR   B OH   1 
ATOM   5035 O OH   B TYR   B 1 42  ? 46.377 -13.766 17.104  0.48 14.38 ?  42  TYR   B OH   1 
ATOM   5036 H H    A TYR   B 1 42  ? 46.504 -18.000 11.096  0.52 16.69 ?  42  TYR   B H    1 
ATOM   5037 H H    B TYR   B 1 42  ? 46.500 -18.004 11.090  0.48 16.55 ?  42  TYR   B H    1 
ATOM   5038 H HA   A TYR   B 1 42  ? 47.170 -15.408 11.409  0.52 16.69 ?  42  TYR   B HA   1 
ATOM   5039 H HA   B TYR   B 1 42  ? 47.171 -15.418 11.421  0.48 16.41 ?  42  TYR   B HA   1 
ATOM   5040 H HB2  A TYR   B 1 42  ? 48.088 -17.676 12.700  0.52 19.29 ?  42  TYR   B HB2  1 
ATOM   5041 H HB2  B TYR   B 1 42  ? 48.005 -17.687 12.738  0.48 18.50 ?  42  TYR   B HB2  1 
ATOM   5042 H HB3  A TYR   B 1 42  ? 49.131 -16.490 12.524  0.52 19.29 ?  42  TYR   B HB3  1 
ATOM   5043 H HB3  B TYR   B 1 42  ? 49.136 -16.596 12.505  0.48 18.50 ?  42  TYR   B HB3  1 
ATOM   5044 H HD1  A TYR   B 1 42  ? 48.301 -14.176 13.377  0.52 18.24 ?  42  TYR   B HD1  1 
ATOM   5045 H HD1  B TYR   B 1 42  ? 48.434 -14.182 13.265  0.48 16.47 ?  42  TYR   B HD1  1 
ATOM   5046 H HD2  A TYR   B 1 42  ? 46.710 -17.632 14.619  0.52 20.51 ?  42  TYR   B HD2  1 
ATOM   5047 H HD2  B TYR   B 1 42  ? 46.766 -17.501 14.753  0.48 17.96 ?  42  TYR   B HD2  1 
ATOM   5048 H HE1  A TYR   B 1 42  ? 47.421 -13.104 15.215  0.52 19.03 ?  42  TYR   B HE1  1 
ATOM   5049 H HE1  B TYR   B 1 42  ? 47.703 -12.985 15.089  0.48 16.24 ?  42  TYR   B HE1  1 
ATOM   5050 H HE2  A TYR   B 1 42  ? 45.825 -16.561 16.463  0.52 20.78 ?  42  TYR   B HE2  1 
ATOM   5051 H HE2  B TYR   B 1 42  ? 46.026 -16.295 16.598  0.48 17.67 ?  42  TYR   B HE2  1 
ATOM   5052 H HH   A TYR   B 1 42  ? 46.223 -13.263 17.090  0.52 23.66 ?  42  TYR   B HH   1 
ATOM   5053 H HH   B TYR   B 1 42  ? 45.945 -14.254 17.647  0.48 17.25 ?  42  TYR   B HH   1 
ATOM   5054 N N    . LEU   B 1 43  ? 48.097 -16.748 8.933   1.00 12.27 ?  43  LEU   B N    1 
ATOM   5055 C CA   . LEU   B 1 43  ? 48.915 -16.662 7.723   1.00 12.19 ?  43  LEU   B CA   1 
ATOM   5056 C C    . LEU   B 1 43  ? 50.332 -17.169 7.976   1.00 12.47 ?  43  LEU   B C    1 
ATOM   5057 O O    . LEU   B 1 43  ? 51.316 -16.576 7.528   1.00 14.08 ?  43  LEU   B O    1 
ATOM   5058 C CB   . LEU   B 1 43  ? 48.925 -15.250 7.128   1.00 12.95 ?  43  LEU   B CB   1 
ATOM   5059 C CG   . LEU   B 1 43  ? 47.572 -14.639 6.743   1.00 13.15 ?  43  LEU   B CG   1 
ATOM   5060 C CD1  . LEU   B 1 43  ? 47.778 -13.231 6.181   1.00 13.92 ?  43  LEU   B CD1  1 
ATOM   5061 C CD2  . LEU   B 1 43  ? 46.807 -15.516 5.765   1.00 13.39 ?  43  LEU   B CD2  1 
ATOM   5062 H H    A LEU   B 1 43  ? 47.360 -17.176 8.818   0.52 14.73 ?  43  LEU   B H    1 
ATOM   5063 H H    B LEU   B 1 43  ? 47.358 -17.172 8.816   0.48 14.73 ?  43  LEU   B H    1 
ATOM   5064 H HA   . LEU   B 1 43  ? 48.519 -17.242 7.057   1.00 14.63 ?  43  LEU   B HA   1 
ATOM   5065 H HB2  . LEU   B 1 43  ? 49.337 -14.653 7.769   1.00 15.53 ?  43  LEU   B HB2  1 
ATOM   5066 H HB3  . LEU   B 1 43  ? 49.463 -15.273 6.320   1.00 15.53 ?  43  LEU   B HB3  1 
ATOM   5067 H HG   . LEU   B 1 43  ? 47.037 -14.554 7.543   1.00 15.78 ?  43  LEU   B HG   1 
ATOM   5068 H HD11 . LEU   B 1 43  ? 46.908 -12.855 5.943   1.00 16.70 ?  43  LEU   B HD11 1 
ATOM   5069 H HD12 . LEU   B 1 43  ? 48.194 -12.672 6.857   1.00 16.70 ?  43  LEU   B HD12 1 
ATOM   5070 H HD13 . LEU   B 1 43  ? 48.339 -13.273 5.394   1.00 16.70 ?  43  LEU   B HD13 1 
ATOM   5071 H HD21 . LEU   B 1 43  ? 45.999 -15.053 5.486   1.00 16.07 ?  43  LEU   B HD21 1 
ATOM   5072 H HD22 . LEU   B 1 43  ? 47.364 -15.699 4.992   1.00 16.07 ?  43  LEU   B HD22 1 
ATOM   5073 H HD23 . LEU   B 1 43  ? 46.570 -16.349 6.205   1.00 16.07 ?  43  LEU   B HD23 1 
ATOM   5074 N N    . LYS   B 1 44  ? 50.432 -18.290 8.692   1.00 12.92 ?  44  LYS   B N    1 
ATOM   5075 C CA   . LYS   B 1 44  ? 51.700 -18.969 8.933   1.00 13.61 ?  44  LYS   B CA   1 
ATOM   5076 C C    . LYS   B 1 44  ? 51.820 -20.090 7.911   1.00 13.49 ?  44  LYS   B C    1 
ATOM   5077 O O    . LYS   B 1 44  ? 51.130 -21.109 8.008   1.00 15.01 ?  44  LYS   B O    1 
ATOM   5078 C CB   . LYS   B 1 44  ? 51.764 -19.483 10.369  1.00 15.54 ?  44  LYS   B CB   1 
ATOM   5079 C CG   . LYS   B 1 44  ? 51.990 -18.377 11.387  1.00 18.91 ?  44  LYS   B CG   1 
ATOM   5080 C CD   . LYS   B 1 44  ? 53.155 -17.492 10.933  1.00 23.06 ?  44  LYS   B CD   1 
ATOM   5081 C CE   . LYS   B 1 44  ? 53.944 -16.871 12.061  1.00 26.80 ?  44  LYS   B CE   1 
ATOM   5082 N NZ   . LYS   B 1 44  ? 54.860 -15.813 11.599  1.00 27.47 ?  44  LYS   B NZ   1 
ATOM   5083 H H    . LYS   B 1 44  ? 49.761 -18.682 9.057   1.00 15.50 ?  44  LYS   B H    1 
ATOM   5084 H HA   . LYS   B 1 44  ? 52.428 -18.356 8.761   1.00 16.33 ?  44  LYS   B HA   1 
ATOM   5085 H HB2  . LYS   B 1 44  ? 50.919 -19.919 10.585  1.00 18.64 ?  44  LYS   B HB2  1 
ATOM   5086 H HB3  . LYS   B 1 44  ? 52.489 -20.122 10.447  1.00 18.64 ?  44  LYS   B HB3  1 
ATOM   5087 H HG2  . LYS   B 1 44  ? 51.195 -17.836 11.463  1.00 22.70 ?  44  LYS   B HG2  1 
ATOM   5088 H HG3  . LYS   B 1 44  ? 52.223 -18.772 12.245  1.00 22.70 ?  44  LYS   B HG3  1 
ATOM   5089 H HD2  . LYS   B 1 44  ? 53.768 -18.041 10.410  1.00 27.67 ?  44  LYS   B HD2  1 
ATOM   5090 H HD3  . LYS   B 1 44  ? 52.796 -16.783 10.374  1.00 27.67 ?  44  LYS   B HD3  1 
ATOM   5091 H HE2  . LYS   B 1 44  ? 53.356 -16.443 12.672  1.00 32.16 ?  44  LYS   B HE2  1 
ATOM   5092 H HE3  . LYS   B 1 44  ? 54.450 -17.566 12.511  1.00 32.16 ?  44  LYS   B HE3  1 
ATOM   5093 H HZ1  . LYS   B 1 44  ? 55.298 -15.471 12.293  1.00 32.96 ?  44  LYS   B HZ1  1 
ATOM   5094 H HZ2  . LYS   B 1 44  ? 55.442 -16.145 11.018  1.00 32.96 ?  44  LYS   B HZ2  1 
ATOM   5095 H HZ3  . LYS   B 1 44  ? 54.395 -15.161 11.203  1.00 32.96 ?  44  LYS   B HZ3  1 
ATOM   5096 N N    . HIS   B 1 45  ? 52.674 -19.880 6.912   1.00 13.10 ?  45  HIS   B N    1 
ATOM   5097 C CA   . HIS   B 1 45  ? 52.699 -20.718 5.712   1.00 12.94 ?  45  HIS   B CA   1 
ATOM   5098 C C    . HIS   B 1 45  ? 53.727 -21.839 5.876   1.00 15.60 ?  45  HIS   B C    1 
ATOM   5099 O O    . HIS   B 1 45  ? 54.796 -21.850 5.272   1.00 18.56 ?  45  HIS   B O    1 
ATOM   5100 C CB   . HIS   B 1 45  ? 53.005 -19.867 4.491   1.00 13.10 ?  45  HIS   B CB   1 
ATOM   5101 C CG   . HIS   B 1 45  ? 52.143 -18.656 4.388   1.00 12.62 ?  45  HIS   B CG   1 
ATOM   5102 N ND1  . HIS   B 1 45  ? 50.763 -18.727 4.355   1.00 13.00 ?  45  HIS   B ND1  1 
ATOM   5103 C CD2  . HIS   B 1 45  ? 52.463 -17.346 4.284   1.00 13.66 ?  45  HIS   B CD2  1 
ATOM   5104 C CE1  . HIS   B 1 45  ? 50.278 -17.504 4.243   1.00 12.61 ?  45  HIS   B CE1  1 
ATOM   5105 N NE2  . HIS   B 1 45  ? 51.284 -16.649 4.209   1.00 13.52 ?  45  HIS   B NE2  1 
ATOM   5106 H H    . HIS   B 1 45  ? 53.253 -19.241 6.902   1.00 15.72 ?  45  HIS   B H    1 
ATOM   5107 H HA   . HIS   B 1 45  ? 51.819 -21.119 5.588   1.00 15.53 ?  45  HIS   B HA   1 
ATOM   5108 H HB2  . HIS   B 1 45  ? 53.924 -19.576 4.529   1.00 15.72 ?  45  HIS   B HB2  1 
ATOM   5109 H HB3  . HIS   B 1 45  ? 52.861 -20.405 3.689   1.00 15.72 ?  45  HIS   B HB3  1 
ATOM   5110 H HD2  . HIS   B 1 45  ? 53.319 -16.981 4.287   1.00 16.40 ?  45  HIS   B HD2  1 
ATOM   5111 H HE1  . HIS   B 1 45  ? 49.372 -17.279 4.199   1.00 15.13 ?  45  HIS   B HE1  1 
ATOM   5112 H HE2  . HIS   B 1 45  ? 51.207 -15.793 4.144   1.00 16.22 ?  45  HIS   B HE2  1 
ATOM   5113 N N    A GLY   B 1 46  ? 53.358 -22.823 6.691   0.52 16.83 ?  46  GLY   B N    1 
ATOM   5114 N N    B GLY   B 1 46  ? 53.369 -22.806 6.711   0.48 16.75 ?  46  GLY   B N    1 
ATOM   5115 C CA   A GLY   B 1 46  ? 54.294 -23.868 7.071   0.52 19.24 ?  46  GLY   B CA   1 
ATOM   5116 C CA   B GLY   B 1 46  ? 54.297 -23.867 7.041   0.48 18.87 ?  46  GLY   B CA   1 
ATOM   5117 C C    A GLY   B 1 46  ? 54.337 -25.107 6.197   0.52 21.40 ?  46  GLY   B C    1 
ATOM   5118 C C    B GLY   B 1 46  ? 54.313 -25.009 6.044   0.48 20.91 ?  46  GLY   B C    1 
ATOM   5119 O O    A GLY   B 1 46  ? 55.422 -25.569 5.830   0.52 23.81 ?  46  GLY   B O    1 
ATOM   5120 O O    B GLY   B 1 46  ? 55.334 -25.271 5.400   0.48 22.94 ?  46  GLY   B O    1 
ATOM   5121 H H    A GLY   B 1 46  ? 52.577 -22.891 7.051   0.52 20.19 ?  46  GLY   B H    1 
ATOM   5122 H H    B GLY   B 1 46  ? 52.602 -22.861 7.102   0.48 20.10 ?  46  GLY   B H    1 
ATOM   5123 H HA2  A GLY   B 1 46  ? 55.186 -23.489 7.093   0.52 23.09 ?  46  GLY   B HA2  1 
ATOM   5124 H HA2  B GLY   B 1 46  ? 55.192 -23.498 7.090   0.48 22.64 ?  46  GLY   B HA2  1 
ATOM   5125 H HA3  A GLY   B 1 46  ? 54.076 -24.167 7.965   0.52 23.09 ?  46  GLY   B HA3  1 
ATOM   5126 H HA3  B GLY   B 1 46  ? 54.071 -24.219 7.918   0.48 22.64 ?  46  GLY   B HA3  1 
ATOM   5127 N N    . GLY   B 1 47  ? 53.181 -25.692 5.888   1.00 20.57 ?  47  GLY   B N    1 
ATOM   5128 C CA   . GLY   B 1 47  ? 53.129 -26.952 5.175   1.00 17.74 ?  47  GLY   B CA   1 
ATOM   5129 C C    . GLY   B 1 47  ? 52.198 -26.925 3.978   1.00 14.78 ?  47  GLY   B C    1 
ATOM   5130 O O    . GLY   B 1 47  ? 51.532 -25.929 3.705   1.00 15.17 ?  47  GLY   B O    1 
ATOM   5131 H H    A GLY   B 1 47  ? 52.407 -25.386 6.108   0.52 24.69 ?  47  GLY   B H    1 
ATOM   5132 H H    B GLY   B 1 47  ? 52.416 -25.431 6.184   0.48 24.69 ?  47  GLY   B H    1 
ATOM   5133 H HA2  . GLY   B 1 47  ? 54.013 -27.191 4.858   1.00 21.29 ?  47  GLY   B HA2  1 
ATOM   5134 H HA3  . GLY   B 1 47  ? 52.825 -27.649 5.778   1.00 21.29 ?  47  GLY   B HA3  1 
ATOM   5135 N N    . GLY   B 1 48  ? 52.151 -28.060 3.281   1.00 14.48 ?  48  GLY   B N    1 
ATOM   5136 C CA   . GLY   B 1 48  ? 51.227 -28.205 2.171   1.00 14.42 ?  48  GLY   B CA   1 
ATOM   5137 C C    . GLY   B 1 48  ? 51.370 -27.094 1.157   1.00 13.22 ?  48  GLY   B C    1 
ATOM   5138 O O    . GLY   B 1 48  ? 52.473 -26.637 0.852   1.00 13.80 ?  48  GLY   B O    1 
ATOM   5139 H H    . GLY   B 1 48  ? 52.638 -28.748 3.427   1.00 17.37 ?  48  GLY   B H    1 
ATOM   5140 H HA2  . GLY   B 1 48  ? 51.384 -29.055 1.722   1.00 17.30 ?  48  GLY   B HA2  1 
ATOM   5141 H HA3  . GLY   B 1 48  ? 50.313 -28.199 2.497   1.00 17.30 ?  48  GLY   B HA3  1 
ATOM   5142 N N    . VAL   B 1 49  ? 50.230 -26.659 0.619   1.00 13.00 ?  49  VAL   B N    1 
ATOM   5143 C CA   . VAL   B 1 49  ? 50.220 -25.634 -0.422  1.00 12.89 ?  49  VAL   B CA   1 
ATOM   5144 C C    . VAL   B 1 49  ? 50.876 -24.348 0.071   1.00 11.56 ?  49  VAL   B C    1 
ATOM   5145 O O    . VAL   B 1 49  ? 51.667 -23.727 -0.646  1.00 12.97 ?  49  VAL   B O    1 
ATOM   5146 C CB   . VAL   B 1 49  ? 48.775 -25.379 -0.901  1.00 14.27 ?  49  VAL   B CB   1 
ATOM   5147 C CG1  . VAL   B 1 49  ? 48.688 -24.112 -1.768  1.00 14.35 ?  49  VAL   B CG1  1 
ATOM   5148 C CG2  . VAL   B 1 49  ? 48.236 -26.588 -1.656  1.00 16.50 ?  49  VAL   B CG2  1 
ATOM   5149 H H    . VAL   B 1 49  ? 49.445 -26.939 0.841   1.00 15.60 ?  49  VAL   B H    1 
ATOM   5150 H HA   . VAL   B 1 49  ? 50.723 -25.954 -1.186  1.00 15.47 ?  49  VAL   B HA   1 
ATOM   5151 H HB   . VAL   B 1 49  ? 48.207 -25.239 -0.128  1.00 17.13 ?  49  VAL   B HB   1 
ATOM   5152 H HG11 . VAL   B 1 49  ? 47.854 -24.119 -2.261  1.00 17.22 ?  49  VAL   B HG11 1 
ATOM   5153 H HG12 . VAL   B 1 49  ? 48.721 -23.329 -1.191  1.00 17.22 ?  49  VAL   B HG12 1 
ATOM   5154 H HG13 . VAL   B 1 49  ? 49.437 -24.099 -2.385  1.00 17.22 ?  49  VAL   B HG13 1 
ATOM   5155 H HG21 . VAL   B 1 49  ? 47.327 -26.402 -1.946  1.00 19.79 ?  49  VAL   B HG21 1 
ATOM   5156 H HG22 . VAL   B 1 49  ? 48.799 -26.756 -2.427  1.00 19.79 ?  49  VAL   B HG22 1 
ATOM   5157 H HG23 . VAL   B 1 49  ? 48.242 -27.355 -1.065  1.00 19.79 ?  49  VAL   B HG23 1 
ATOM   5158 N N    . ALA   B 1 50  ? 50.524 -23.905 1.276   1.00 11.84 ?  50  ALA   B N    1 
ATOM   5159 C CA   . ALA   B 1 50  ? 51.041 -22.625 1.755   1.00 11.51 ?  50  ALA   B CA   1 
ATOM   5160 C C    . ALA   B 1 50  ? 52.559 -22.657 1.867   1.00 11.78 ?  50  ALA   B C    1 
ATOM   5161 O O    . ALA   B 1 50  ? 53.238 -21.688 1.502   1.00 12.18 ?  50  ALA   B O    1 
ATOM   5162 C CB   . ALA   B 1 50  ? 50.404 -22.263 3.093   1.00 12.19 ?  50  ALA   B CB   1 
ATOM   5163 H H    . ALA   B 1 50  ? 49.987 -24.301 1.814   1.00 14.21 ?  50  ALA   B H    1 
ATOM   5164 H HA   . ALA   B 1 50  ? 50.814 -21.928 1.120   1.00 13.82 ?  50  ALA   B HA   1 
ATOM   5165 H HB1  . ALA   B 1 50  ? 50.760 -21.412 3.396   1.00 14.63 ?  50  ALA   B HB1  1 
ATOM   5166 H HB2  . ALA   B 1 50  ? 49.442 -22.192 2.975   1.00 14.63 ?  50  ALA   B HB2  1 
ATOM   5167 H HB3  . ALA   B 1 50  ? 50.607 -22.955 3.740   1.00 14.63 ?  50  ALA   B HB3  1 
ATOM   5168 N N    . GLY   B 1 51  ? 53.113 -23.755 2.377   1.00 12.61 ?  51  GLY   B N    1 
ATOM   5169 C CA   . GLY   B 1 51  ? 54.560 -23.851 2.457   1.00 13.65 ?  51  GLY   B CA   1 
ATOM   5170 C C    . GLY   B 1 51  ? 55.215 -23.811 1.090   1.00 13.49 ?  51  GLY   B C    1 
ATOM   5171 O O    . GLY   B 1 51  ? 56.267 -23.186 0.912   1.00 14.37 ?  51  GLY   B O    1 
ATOM   5172 H H    . GLY   B 1 51  ? 52.689 -24.447 2.662   1.00 15.13 ?  51  GLY   B H    1 
ATOM   5173 H HA2  . GLY   B 1 51  ? 54.905 -23.108 2.978   1.00 16.38 ?  51  GLY   B HA2  1 
ATOM   5174 H HA3  . GLY   B 1 51  ? 54.812 -24.678 2.892   1.00 16.38 ?  51  GLY   B HA3  1 
ATOM   5175 N N    . ALA   B 1 52  ? 54.609 -24.477 0.105   1.00 12.37 ?  52  ALA   B N    1 
ATOM   5176 C CA   . ALA   B 1 52  ? 55.177 -24.488 -1.238  1.00 13.05 ?  52  ALA   B CA   1 
ATOM   5177 C C    . ALA   B 1 52  ? 55.097 -23.108 -1.886  1.00 12.54 ?  52  ALA   B C    1 
ATOM   5178 O O    . ALA   B 1 52  ? 56.065 -22.655 -2.516  1.00 13.62 ?  52  ALA   B O    1 
ATOM   5179 C CB   . ALA   B 1 52  ? 54.472 -25.529 -2.103  1.00 13.35 ?  52  ALA   B CB   1 
ATOM   5180 H H    . ALA   B 1 52  ? 53.869 -24.916 0.187   1.00 14.84 ?  52  ALA   B H    1 
ATOM   5181 H HA   . ALA   B 1 52  ? 56.113 -24.729 -1.173  1.00 15.66 ?  52  ALA   B HA   1 
ATOM   5182 H HB1  . ALA   B 1 52  ? 54.872 -25.516 -2.987  1.00 16.01 ?  52  ALA   B HB1  1 
ATOM   5183 H HB2  . ALA   B 1 52  ? 54.588 -26.399 -1.698  1.00 16.01 ?  52  ALA   B HB2  1 
ATOM   5184 H HB3  . ALA   B 1 52  ? 53.533 -25.305 -2.159  1.00 16.01 ?  52  ALA   B HB3  1 
ATOM   5185 N N    . LEU   B 1 53  ? 53.950 -22.428 -1.761  1.00 12.47 ?  53  LEU   B N    1 
ATOM   5186 C CA   . LEU   B 1 53  ? 53.835 -21.090 -2.337  1.00 12.12 ?  53  LEU   B CA   1 
ATOM   5187 C C    . LEU   B 1 53  ? 54.838 -20.143 -1.688  1.00 12.04 ?  53  LEU   B C    1 
ATOM   5188 O O    . LEU   B 1 53  ? 55.547 -19.398 -2.381  1.00 13.04 ?  53  LEU   B O    1 
ATOM   5189 C CB   . LEU   B 1 53  ? 52.406 -20.552 -2.182  1.00 13.06 ?  53  LEU   B CB   1 
ATOM   5190 C CG   . LEU   B 1 53  ? 51.266 -21.283 -2.899  1.00 12.90 ?  53  LEU   B CG   1 
ATOM   5191 C CD1  . LEU   B 1 53  ? 49.916 -20.648 -2.587  1.00 14.21 ?  53  LEU   B CD1  1 
ATOM   5192 C CD2  . LEU   B 1 53  ? 51.496 -21.338 -4.403  1.00 14.90 ?  53  LEU   B CD2  1 
ATOM   5193 H H    . LEU   B 1 53  ? 53.247 -22.713 -1.352  1.00 14.97 ?  53  LEU   B H    1 
ATOM   5194 H HA   . LEU   B 1 53  ? 54.045 -21.146 -3.284  1.00 14.54 ?  53  LEU   B HA   1 
ATOM   5195 H HB2  . LEU   B 1 53  ? 52.192 -20.564 -1.239  1.00 15.68 ?  53  LEU   B HB2  1 
ATOM   5196 H HB3  . LEU   B 1 53  ? 52.401 -19.645 -2.505  1.00 15.68 ?  53  LEU   B HB3  1 
ATOM   5197 H HG   . LEU   B 1 53  ? 51.231 -22.201 -2.579  1.00 15.48 ?  53  LEU   B HG   1 
ATOM   5198 H HD11 . LEU   B 1 53  ? 49.220 -21.138 -3.055  1.00 17.06 ?  53  LEU   B HD11 1 
ATOM   5199 H HD12 . LEU   B 1 53  ? 49.763 -20.696 -1.628  1.00 17.06 ?  53  LEU   B HD12 1 
ATOM   5200 H HD13 . LEU   B 1 53  ? 49.928 -19.727 -2.876  1.00 17.06 ?  53  LEU   B HD13 1 
ATOM   5201 H HD21 . LEU   B 1 53  ? 50.787 -21.862 -4.816  1.00 17.88 ?  53  LEU   B HD21 1 
ATOM   5202 H HD22 . LEU   B 1 53  ? 51.489 -20.440 -4.760  1.00 17.88 ?  53  LEU   B HD22 1 
ATOM   5203 H HD23 . LEU   B 1 53  ? 52.353 -21.761 -4.581  1.00 17.88 ?  53  LEU   B HD23 1 
ATOM   5204 N N    . ASN   B 1 54  ? 54.928 -20.170 -0.356  1.00 11.89 ?  54  ASN   B N    1 
ATOM   5205 C CA   . ASN   B 1 54  ? 55.843 -19.260 0.319   1.00 12.05 ?  54  ASN   B CA   1 
ATOM   5206 C C    . ASN   B 1 54  ? 57.288 -19.547 -0.071  1.00 12.76 ?  54  ASN   B C    1 
ATOM   5207 O O    . ASN   B 1 54  ? 58.071 -18.615 -0.302  1.00 13.47 ?  54  ASN   B O    1 
ATOM   5208 C CB   . ASN   B 1 54  ? 55.666 -19.326 1.828   1.00 13.16 ?  54  ASN   B CB   1 
ATOM   5209 C CG   . ASN   B 1 54  ? 56.657 -18.432 2.546   1.00 13.54 ?  54  ASN   B CG   1 
ATOM   5210 O OD1  . ASN   B 1 54  ? 56.688 -17.221 2.313   1.00 14.43 ?  54  ASN   B OD1  1 
ATOM   5211 N ND2  . ASN   B 1 54  ? 57.472 -19.015 3.415   1.00 15.82 ?  54  ASN   B ND2  1 
ATOM   5212 H H    . ASN   B 1 54  ? 54.483 -20.695 0.162   1.00 14.27 ?  54  ASN   B H    1 
ATOM   5213 H HA   . ASN   B 1 54  ? 55.637 -18.356 0.038   1.00 14.46 ?  54  ASN   B HA   1 
ATOM   5214 H HB2  . ASN   B 1 54  ? 54.765 -19.031 2.060   1.00 15.79 ?  54  ASN   B HB2  1 
ATOM   5215 H HB3  . ASN   B 1 54  ? 55.805 -20.233 2.134   1.00 15.79 ?  54  ASN   B HB3  1 
ATOM   5216 H HD21 . ASN   B 1 54  ? 58.053 -18.546 3.847   1.00 18.99 ?  54  ASN   B HD21 1 
ATOM   5217 H HD22 . ASN   B 1 54  ? 57.425 -19.862 3.547   1.00 18.99 ?  54  ASN   B HD22 1 
ATOM   5218 N N    . LYS   B 1 55  ? 57.669 -20.829 -0.139  1.00 13.89 ?  55  LYS   B N    1 
ATOM   5219 C CA   . LYS   B 1 55  ? 59.029 -21.166 -0.549  1.00 15.01 ?  55  LYS   B CA   1 
ATOM   5220 C C    . LYS   B 1 55  ? 59.328 -20.625 -1.942  1.00 14.79 ?  55  LYS   B C    1 
ATOM   5221 O O    . LYS   B 1 55  ? 60.427 -20.111 -2.192  1.00 15.58 ?  55  LYS   B O    1 
ATOM   5222 C CB   . LYS   B 1 55  ? 59.242 -22.682 -0.491  1.00 17.03 ?  55  LYS   B CB   1 
ATOM   5223 C CG   . LYS   B 1 55  ? 60.637 -23.138 -0.911  1.00 21.89 ?  55  LYS   B CG   1 
ATOM   5224 C CD   . LYS   B 1 55  ? 60.798 -24.647 -0.774  1.00 26.26 ?  55  LYS   B CD   1 
ATOM   5225 C CE   . LYS   B 1 55  ? 60.849 -25.082 0.687   1.00 29.55 ?  55  LYS   B CE   1 
ATOM   5226 N NZ   . LYS   B 1 55  ? 61.195 -26.520 0.825   1.00 31.55 ?  55  LYS   B NZ   1 
ATOM   5227 H H    . LYS   B 1 55  ? 57.165 -21.502 0.042   1.00 16.66 ?  55  LYS   B H    1 
ATOM   5228 H HA   . LYS   B 1 55  ? 59.653 -20.757 0.067   1.00 18.01 ?  55  LYS   B HA   1 
ATOM   5229 H HB2  . LYS   B 1 55  ? 59.093 -22.976 0.423   1.00 20.44 ?  55  LYS   B HB2  1 
ATOM   5230 H HB3  . LYS   B 1 55  ? 58.600 -23.109 -1.079  1.00 20.44 ?  55  LYS   B HB3  1 
ATOM   5231 H HG2  . LYS   B 1 55  ? 60.784 -22.900 -1.839  1.00 26.27 ?  55  LYS   B HG2  1 
ATOM   5232 H HG3  . LYS   B 1 55  ? 61.295 -22.707 -0.344  1.00 26.27 ?  55  LYS   B HG3  1 
ATOM   5233 H HD2  . LYS   B 1 55  ? 60.044 -25.092 -1.196  1.00 31.52 ?  55  LYS   B HD2  1 
ATOM   5234 H HD3  . LYS   B 1 55  ? 61.627 -24.920 -1.200  1.00 31.52 ?  55  LYS   B HD3  1 
ATOM   5235 H HE2  . LYS   B 1 55  ? 61.524 -24.556 1.148   1.00 35.46 ?  55  LYS   B HE2  1 
ATOM   5236 H HE3  . LYS   B 1 55  ? 59.979 -24.934 1.092   1.00 35.46 ?  55  LYS   B HE3  1 
ATOM   5237 H HZ1  . LYS   B 1 55  ? 61.212 -26.742 1.686   1.00 37.85 ?  55  LYS   B HZ1  1 
ATOM   5238 H HZ2  . LYS   B 1 55  ? 60.586 -27.015 0.407   1.00 37.85 ?  55  LYS   B HZ2  1 
ATOM   5239 H HZ3  . LYS   B 1 55  ? 61.993 -26.673 0.467   1.00 37.85 ?  55  LYS   B HZ3  1 
ATOM   5240 N N    . ALA   B 1 56  ? 58.359 -20.722 -2.861  1.00 14.00 ?  56  ALA   B N    1 
ATOM   5241 C CA   . ALA   B 1 56  ? 58.574 -20.216 -4.211  1.00 14.64 ?  56  ALA   B CA   1 
ATOM   5242 C C    . ALA   B 1 56  ? 58.862 -18.720 -4.212  1.00 14.52 ?  56  ALA   B C    1 
ATOM   5243 O O    . ALA   B 1 56  ? 59.601 -18.235 -5.081  1.00 15.59 ?  56  ALA   B O    1 
ATOM   5244 C CB   . ALA   B 1 56  ? 57.369 -20.534 -5.096  1.00 16.06 ?  56  ALA   B CB   1 
ATOM   5245 H H    . ALA   B 1 56  ? 57.576 -21.060 -2.725  1.00 16.80 ?  56  ALA   B H    1 
ATOM   5246 H HA   . ALA   B 1 56  ? 59.348 -20.656 -4.588  1.00 17.57 ?  56  ALA   B HA   1 
ATOM   5247 H HB1  . ALA   B 1 56  ? 57.535 -20.192 -5.990  1.00 19.27 ?  56  ALA   B HB1  1 
ATOM   5248 H HB2  . ALA   B 1 56  ? 57.252 -21.497 -5.130  1.00 19.27 ?  56  ALA   B HB2  1 
ATOM   5249 H HB3  . ALA   B 1 56  ? 56.579 -20.117 -4.723  1.00 19.27 ?  56  ALA   B HB3  1 
ATOM   5250 N N    . THR   B 1 57  ? 58.291 -17.974 -3.262  1.00 14.53 ?  57  THR   B N    1 
ATOM   5251 C CA   . THR   B 1 57  ? 58.535 -16.539 -3.153  1.00 14.35 ?  57  THR   B CA   1 
ATOM   5252 C C    . THR   B 1 57  ? 59.780 -16.210 -2.345  1.00 14.94 ?  57  THR   B C    1 
ATOM   5253 O O    . THR   B 1 57  ? 60.011 -15.035 -2.047  1.00 15.62 ?  57  THR   B O    1 
ATOM   5254 C CB   . THR   B 1 57  ? 57.335 -15.803 -2.515  1.00 12.96 ?  57  THR   B CB   1 
ATOM   5255 O OG1  . THR   B 1 57  ? 57.313 -16.018 -1.094  1.00 13.88 ?  57  THR   B OG1  1 
ATOM   5256 C CG2  . THR   B 1 57  ? 56.017 -16.219 -3.153  1.00 14.17 ?  57  THR   B CG2  1 
ATOM   5257 H H    . THR   B 1 57  ? 57.739 -18.273 -2.668  1.00 17.44 ?  57  THR   B H    1 
ATOM   5258 H HA   . THR   B 1 57  ? 58.653 -16.174 -4.044  1.00 17.22 ?  57  THR   B HA   1 
ATOM   5259 H HB   . THR   B 1 57  ? 57.438 -14.846 -2.676  1.00 15.55 ?  57  THR   B HB   1 
ATOM   5260 H HG1  . THR   B 1 57  ? 57.225 -16.846 -0.941  1.00 16.66 ?  57  THR   B HG1  1 
ATOM   5261 H HG21 . THR   B 1 57  ? 55.293 -15.669 -2.826  1.00 17.00 ?  57  THR   B HG21 1 
ATOM   5262 H HG22 . THR   B 1 57  ? 56.071 -16.130 -4.120  1.00 17.00 ?  57  THR   B HG22 1 
ATOM   5263 H HG23 . THR   B 1 57  ? 55.827 -17.149 -2.940  1.00 17.00 ?  57  THR   B HG23 1 
ATOM   5264 N N    . ASN   B 1 58  ? 60.564 -17.212 -1.967  1.00 16.56 ?  58  ASN   B N    1 
ATOM   5265 C CA   . ASN   B 1 58  ? 61.758 -16.996 -1.157  1.00 19.39 ?  58  ASN   B CA   1 
ATOM   5266 C C    . ASN   B 1 58  ? 61.421 -16.273 0.149   1.00 16.42 ?  58  ASN   B C    1 
ATOM   5267 O O    . ASN   B 1 58  ? 62.157 -15.397 0.612   1.00 17.82 ?  58  ASN   B O    1 
ATOM   5268 C CB   . ASN   B 1 58  ? 62.849 -16.255 -1.940  1.00 29.10 ?  58  ASN   B CB   1 
ATOM   5269 C CG   . ASN   B 1 58  ? 64.225 -16.420 -1.321  1.00 40.62 ?  58  ASN   B CG   1 
ATOM   5270 O OD1  . ASN   B 1 58  ? 64.526 -17.447 -0.712  1.00 43.49 ?  58  ASN   B OD1  1 
ATOM   5271 N ND2  . ASN   B 1 58  ? 65.069 -15.406 -1.476  1.00 47.15 ?  58  ASN   B ND2  1 
ATOM   5272 H H    . ASN   B 1 58  ? 60.421 -18.038 -2.166  1.00 19.87 ?  58  ASN   B H    1 
ATOM   5273 H HA   . ASN   B 1 58  ? 62.120 -17.867 -0.927  1.00 23.27 ?  58  ASN   B HA   1 
ATOM   5274 H HB2  . ASN   B 1 58  ? 62.882 -16.603 -2.847  1.00 34.92 ?  58  ASN   B HB2  1 
ATOM   5275 H HB3  . ASN   B 1 58  ? 62.641 -15.309 -1.956  1.00 34.92 ?  58  ASN   B HB3  1 
ATOM   5276 H HD21 . ASN   B 1 58  ? 65.862 -15.453 -1.145  1.00 56.58 ?  58  ASN   B HD21 1 
ATOM   5277 H HD22 . ASN   B 1 58  ? 64.823 -14.704 -1.905  1.00 56.58 ?  58  ASN   B HD22 1 
ATOM   5278 N N    . ASN   B 1 59  ? 60.299 -16.655 0.757   1.00 15.29 ?  59  ASN   B N    1 
ATOM   5279 C CA   . ASN   B 1 59  ? 59.819 -16.177 2.053   1.00 15.40 ?  59  ASN   B CA   1 
ATOM   5280 C C    . ASN   B 1 59  ? 59.229 -14.770 1.989   1.00 14.64 ?  59  ASN   B C    1 
ATOM   5281 O O    . ASN   B 1 59  ? 58.811 -14.253 3.033   1.00 15.13 ?  59  ASN   B O    1 
ATOM   5282 C CB   . ASN   B 1 59  ? 60.891 -16.216 3.158   1.00 16.74 ?  59  ASN   B CB   1 
ATOM   5283 C CG   . ASN   B 1 59  ? 60.302 -16.399 4.539   1.00 18.17 ?  59  ASN   B CG   1 
ATOM   5284 O OD1  . ASN   B 1 59  ? 59.481 -17.294 4.769   1.00 17.76 ?  59  ASN   B OD1  1 
ATOM   5285 N ND2  . ASN   B 1 59  ? 60.717 -15.551 5.472   1.00 19.07 ?  59  ASN   B ND2  1 
ATOM   5286 H H    . ASN   B 1 59  ? 59.760 -17.242 0.415   1.00 18.35 ?  59  ASN   B H    1 
ATOM   5287 H HA   . ASN   B 1 59  ? 59.110 -16.773 2.342   1.00 18.48 ?  59  ASN   B HA   1 
ATOM   5288 H HB2  . ASN   B 1 59  ? 61.493 -16.958 2.999   1.00 20.09 ?  59  ASN   B HB2  1 
ATOM   5289 H HB3  . ASN   B 1 59  ? 61.382 -15.381 3.156   1.00 20.09 ?  59  ASN   B HB3  1 
ATOM   5290 H HD21 . ASN   B 1 59  ? 60.409 -15.606 6.276   1.00 22.88 ?  59  ASN   B HD21 1 
ATOM   5291 H HD22 . ASN   B 1 59  ? 61.284 -14.933 5.276   1.00 22.88 ?  59  ASN   B HD22 1 
ATOM   5292 N N    . ALA   B 1 60  ? 59.165 -14.133 0.813   1.00 14.45 ?  60  ALA   B N    1 
ATOM   5293 C CA   . ALA   B 1 60  ? 58.568 -12.802 0.740   1.00 14.40 ?  60  ALA   B CA   1 
ATOM   5294 C C    . ALA   B 1 60  ? 57.099 -12.831 1.137   1.00 13.67 ?  60  ALA   B C    1 
ATOM   5295 O O    . ALA   B 1 60  ? 56.600 -11.884 1.755   1.00 14.40 ?  60  ALA   B O    1 
ATOM   5296 C CB   . ALA   B 1 60  ? 58.730 -12.214 -0.661  1.00 15.76 ?  60  ALA   B CB   1 
ATOM   5297 H H    . ALA   B 1 60  ? 59.462 -14.447 0.068   1.00 17.34 ?  60  ALA   B H    1 
ATOM   5298 H HA   . ALA   B 1 60  ? 59.032 -12.225 1.365   1.00 17.27 ?  60  ALA   B HA   1 
ATOM   5299 H HB1  . ALA   B 1 60  ? 58.326 -11.335 -0.675  1.00 18.91 ?  60  ALA   B HB1  1 
ATOM   5300 H HB2  . ALA   B 1 60  ? 59.676 -12.150 -0.867  1.00 18.91 ?  60  ALA   B HB2  1 
ATOM   5301 H HB3  . ALA   B 1 60  ? 58.290 -12.796 -1.298  1.00 18.91 ?  60  ALA   B HB3  1 
ATOM   5302 N N    . MET   B 1 61  ? 56.394 -13.914 0.798   1.00 13.15 ?  61  MET   B N    1 
ATOM   5303 C CA   . MET   B 1 61  ? 54.996 -14.034 1.188   1.00 12.72 ?  61  MET   B CA   1 
ATOM   5304 C C    . MET   B 1 61  ? 54.850 -14.032 2.706   1.00 12.69 ?  61  MET   B C    1 
ATOM   5305 O O    . MET   B 1 61  ? 53.939 -13.392 3.250   1.00 12.77 ?  61  MET   B O    1 
ATOM   5306 C CB   . MET   B 1 61  ? 54.420 -15.311 0.570   1.00 13.07 ?  61  MET   B CB   1 
ATOM   5307 C CG   . MET   B 1 61  ? 52.956 -15.581 0.937   1.00 12.39 ?  61  MET   B CG   1 
ATOM   5308 S SD   . MET   B 1 61  ? 52.338 -17.110 0.210   1.00 13.12 ?  61  MET   B SD   1 
ATOM   5309 C CE   . MET   B 1 61  ? 52.086 -16.554 -1.465  1.00 14.07 ?  61  MET   B CE   1 
ATOM   5310 H H    . MET   B 1 61  ? 56.700 -14.588 0.341   1.00 15.78 ?  61  MET   B H    1 
ATOM   5311 H HA   . MET   B 1 61  ? 54.506 -13.288 0.819   1.00 15.26 ?  61  MET   B HA   1 
ATOM   5312 H HB2  . MET   B 1 61  ? 54.472 -15.245 -0.400  1.00 15.68 ?  61  MET   B HB2  1 
ATOM   5313 H HB3  . MET   B 1 61  ? 54.944 -16.073 0.869   1.00 15.68 ?  61  MET   B HB3  1 
ATOM   5314 H HG2  . MET   B 1 61  ? 52.878 -15.660 1.900   1.00 14.86 ?  61  MET   B HG2  1 
ATOM   5315 H HG3  . MET   B 1 61  ? 52.409 -14.848 0.616   1.00 14.86 ?  61  MET   B HG3  1 
ATOM   5316 H HE1  . MET   B 1 61  ? 51.727 -17.285 -1.990  1.00 16.88 ?  61  MET   B HE1  1 
ATOM   5317 H HE2  . MET   B 1 61  ? 51.461 -15.810 -1.462  1.00 16.88 ?  61  MET   B HE2  1 
ATOM   5318 H HE3  . MET   B 1 61  ? 52.936 -16.266 -1.835  1.00 16.88 ?  61  MET   B HE3  1 
ATOM   5319 N N    . GLN   B 1 62  ? 55.727 -14.745 3.414   1.00 12.16 ?  62  GLN   B N    1 
ATOM   5320 C CA   . GLN   B 1 62  ? 55.622 -14.801 4.870   1.00 12.70 ?  62  GLN   B CA   1 
ATOM   5321 C C    . GLN   B 1 62  ? 55.896 -13.440 5.496   1.00 13.37 ?  62  GLN   B C    1 
ATOM   5322 O O    . GLN   B 1 62  ? 55.215 -13.040 6.448   1.00 14.14 ?  62  GLN   B O    1 
ATOM   5323 C CB   . GLN   B 1 62  ? 56.572 -15.858 5.444   1.00 13.22 ?  62  GLN   B CB   1 
ATOM   5324 C CG   . GLN   B 1 62  ? 56.340 -16.137 6.917   1.00 13.73 ?  62  GLN   B CG   1 
ATOM   5325 C CD   . GLN   B 1 62  ? 54.967 -16.719 7.160   1.00 13.66 ?  62  GLN   B CD   1 
ATOM   5326 O OE1  . GLN   B 1 62  ? 54.712 -17.870 6.808   1.00 13.98 ?  62  GLN   B OE1  1 
ATOM   5327 N NE2  . GLN   B 1 62  ? 54.060 -15.924 7.732   1.00 13.88 ?  62  GLN   B NE2  1 
ATOM   5328 H H    . GLN   B 1 62  ? 56.381 -15.201 3.082   1.00 14.60 ?  62  GLN   B H    1 
ATOM   5329 H HA   . GLN   B 1 62  ? 54.713 -15.057 5.103   1.00 15.24 ?  62  GLN   B HA   1 
ATOM   5330 H HB2  . GLN   B 1 62  ? 56.447 -16.690 4.959   1.00 15.87 ?  62  GLN   B HB2  1 
ATOM   5331 H HB3  . GLN   B 1 62  ? 57.483 -15.549 5.341   1.00 15.87 ?  62  GLN   B HB3  1 
ATOM   5332 H HG2  . GLN   B 1 62  ? 56.999 -16.777 7.227   1.00 16.48 ?  62  GLN   B HG2  1 
ATOM   5333 H HG3  . GLN   B 1 62  ? 56.406 -15.313 7.417   1.00 16.48 ?  62  GLN   B HG3  1 
ATOM   5334 H HE21 . GLN   B 1 62  ? 54.273 -15.127 7.957   1.00 16.66 ?  62  GLN   B HE21 1 
ATOM   5335 H HE22 . GLN   B 1 62  ? 53.265 -16.221 7.882   1.00 16.66 ?  62  GLN   B HE22 1 
ATOM   5336 N N    . VAL   B 1 63  ? 56.916 -12.732 5.009   1.00 13.81 ?  63  VAL   B N    1 
ATOM   5337 C CA   . VAL   B 1 63  ? 57.216 -11.406 5.550   1.00 14.82 ?  63  VAL   B CA   1 
ATOM   5338 C C    . VAL   B 1 63  ? 56.015 -10.477 5.362   1.00 13.85 ?  63  VAL   B C    1 
ATOM   5339 O O    . VAL   B 1 63  ? 55.592 -9.768  6.287   1.00 14.68 ?  63  VAL   B O    1 
ATOM   5340 C CB   . VAL   B 1 63  ? 58.510 -10.847 4.924   1.00 15.76 ?  63  VAL   B CB   1 
ATOM   5341 C CG1  . VAL   B 1 63  ? 58.741 -9.401  5.371   1.00 16.74 ?  63  VAL   B CG1  1 
ATOM   5342 C CG2  . VAL   B 1 63  ? 59.711 -11.719 5.305   1.00 16.86 ?  63  VAL   B CG2  1 
ATOM   5343 H H    . VAL   B 1 63  ? 57.440 -12.999 4.377   1.00 16.57 ?  63  VAL   B H    1 
ATOM   5344 H HA   . VAL   B 1 63  ? 57.376 -11.496 6.501   1.00 17.79 ?  63  VAL   B HA   1 
ATOM   5345 H HB   . VAL   B 1 63  ? 58.432 -10.858 3.957   1.00 18.91 ?  63  VAL   B HB   1 
ATOM   5346 H HG11 . VAL   B 1 63  ? 59.655 -9.148  5.156   1.00 20.08 ?  63  VAL   B HG11 1 
ATOM   5347 H HG12 . VAL   B 1 63  ? 58.122 -8.822  4.905   1.00 20.08 ?  63  VAL   B HG12 1 
ATOM   5348 H HG13 . VAL   B 1 63  ? 58.602 -9.342  6.329   1.00 20.08 ?  63  VAL   B HG13 1 
ATOM   5349 H HG21 . VAL   B 1 63  ? 60.516 -11.340 4.915   1.00 20.23 ?  63  VAL   B HG21 1 
ATOM   5350 H HG22 . VAL   B 1 63  ? 59.792 -11.738 6.273   1.00 20.23 ?  63  VAL   B HG22 1 
ATOM   5351 H HG23 . VAL   B 1 63  ? 59.573 -12.617 4.967   1.00 20.23 ?  63  VAL   B HG23 1 
ATOM   5352 N N    . GLU   B 1 64  ? 55.444 -10.476 4.159   1.00 13.63 ?  64  GLU   B N    1 
ATOM   5353 C CA   . GLU   B 1 64  ? 54.274 -9.645  3.882   1.00 13.18 ?  64  GLU   B CA   1 
ATOM   5354 C C    . GLU   B 1 64  ? 53.091 -10.049 4.758   1.00 13.22 ?  64  GLU   B C    1 
ATOM   5355 O O    . GLU   B 1 64  ? 52.333 -9.188  5.243   1.00 13.65 ?  64  GLU   B O    1 
ATOM   5356 C CB   . GLU   B 1 64  ? 53.929 -9.782  2.401   1.00 13.31 ?  64  GLU   B CB   1 
ATOM   5357 C CG   . GLU   B 1 64  ? 52.671 -9.043  1.958   1.00 13.72 ?  64  GLU   B CG   1 
ATOM   5358 C CD   . GLU   B 1 64  ? 52.152 -9.527  0.616   1.00 14.87 ?  64  GLU   B CD   1 
ATOM   5359 O OE1  . GLU   B 1 64  ? 52.326 -10.739 0.297   1.00 15.60 ?  64  GLU   B OE1  1 
ATOM   5360 O OE2  . GLU   B 1 64  ? 51.530 -8.711  -0.108  1.00 15.67 -1 64  GLU   B OE2  1 
ATOM   5361 H H    . GLU   B 1 64  ? 55.715 -10.945 3.486   1.00 16.36 ?  64  GLU   B H    1 
ATOM   5362 H HA   . GLU   B 1 64  ? 54.487 -8.720  4.065   1.00 15.82 ?  64  GLU   B HA   1 
ATOM   5363 H HB2  . GLU   B 1 64  ? 54.664 -9.429  1.874   1.00 15.97 ?  64  GLU   B HB2  1 
ATOM   5364 H HB3  . GLU   B 1 64  ? 53.802 -10.719 2.194   1.00 15.97 ?  64  GLU   B HB3  1 
ATOM   5365 H HG2  . GLU   B 1 64  ? 51.960 -9.179  2.608   1.00 16.46 ?  64  GLU   B HG2  1 
ATOM   5366 H HG3  . GLU   B 1 64  ? 52.864 -8.097  1.877   1.00 16.46 ?  64  GLU   B HG3  1 
ATOM   5367 N N    . SER   B 1 65  ? 52.915 -11.358 4.963   1.00 12.68 ?  65  SER   B N    1 
ATOM   5368 C CA   . SER   B 1 65  ? 51.801 -11.860 5.762   1.00 12.41 ?  65  SER   B CA   1 
ATOM   5369 C C    . SER   B 1 65  ? 51.922 -11.452 7.226   1.00 12.82 ?  65  SER   B C    1 
ATOM   5370 O O    . SER   B 1 65  ? 50.921 -11.069 7.856   1.00 13.28 ?  65  SER   B O    1 
ATOM   5371 C CB   . SER   B 1 65  ? 51.724 -13.384 5.636   1.00 12.50 ?  65  SER   B CB   1 
ATOM   5372 O OG   . SER   B 1 65  ? 51.380 -13.786 4.319   1.00 12.92 ?  65  SER   B OG   1 
ATOM   5373 H H    . SER   B 1 65  ? 53.432 -11.980 4.660   1.00 15.22 ?  65  SER   B H    1 
ATOM   5374 H HA   . SER   B 1 65  ? 50.974 -11.492 5.419   1.00 14.89 ?  65  SER   B HA   1 
ATOM   5375 H HB2  . SER   B 1 65  ? 52.583 -13.764 5.868   1.00 15.00 ?  65  SER   B HB2  1 
ATOM   5376 H HB3  . SER   B 1 65  ? 51.044 -13.713 6.251   1.00 15.00 ?  65  SER   B HB3  1 
ATOM   5377 H HG   . SER   B 1 65  ? 51.959 -13.498 3.774   1.00 15.50 ?  65  SER   B HG   1 
ATOM   5378 N N    . ASP   B 1 66  ? 53.130 -11.541 7.797   1.00 13.42 ?  66  ASP   B N    1 
ATOM   5379 C CA   . ASP   B 1 66  ? 53.314 -11.138 9.186   1.00 13.10 ?  66  ASP   B CA   1 
ATOM   5380 C C    . ASP   B 1 66  ? 53.006 -9.658  9.371   1.00 13.60 ?  66  ASP   B C    1 
ATOM   5381 O O    . ASP   B 1 66  ? 52.435 -9.259  10.392  1.00 14.29 ?  66  ASP   B O    1 
ATOM   5382 C CB   . ASP   B 1 66  ? 54.747 -11.434 9.647   1.00 15.06 ?  66  ASP   B CB   1 
ATOM   5383 C CG   . ASP   B 1 66  ? 55.035 -12.929 9.802   1.00 16.87 ?  66  ASP   B CG   1 
ATOM   5384 O OD1  . ASP   B 1 66  ? 54.087 -13.746 9.714   1.00 17.34 ?  66  ASP   B OD1  1 
ATOM   5385 O OD2  . ASP   B 1 66  ? 56.219 -13.279 10.030  1.00 20.31 -1 66  ASP   B OD2  1 
ATOM   5386 H H    . ASP   B 1 66  ? 53.840 -11.825 7.410   1.00 16.10 ?  66  ASP   B H    1 
ATOM   5387 H HA   . ASP   B 1 66  ? 52.710 -11.636 9.756   1.00 15.71 ?  66  ASP   B HA   1 
ATOM   5388 H HB2  . ASP   B 1 66  ? 55.368 -11.072 8.996   1.00 18.07 ?  66  ASP   B HB2  1 
ATOM   5389 H HB3  . ASP   B 1 66  ? 54.896 -11.012 10.512  1.00 18.07 ?  66  ASP   B HB3  1 
ATOM   5390 N N    . ASP   B 1 67  ? 53.386 -8.825  8.401   1.00 13.29 ?  67  ASP   B N    1 
ATOM   5391 C CA   . ASP   B 1 67  ? 53.033 -7.414  8.471   1.00 14.06 ?  67  ASP   B CA   1 
ATOM   5392 C C    . ASP   B 1 67  ? 51.520 -7.214  8.398   1.00 14.08 ?  67  ASP   B C    1 
ATOM   5393 O O    . ASP   B 1 67  ? 50.964 -6.389  9.133   1.00 14.74 ?  67  ASP   B O    1 
ATOM   5394 C CB   . ASP   B 1 67  ? 53.744 -6.655  7.356   1.00 15.32 ?  67  ASP   B CB   1 
ATOM   5395 C CG   . ASP   B 1 67  ? 53.306 -5.213  7.292   1.00 16.73 ?  67  ASP   B CG   1 
ATOM   5396 O OD1  . ASP   B 1 67  ? 53.799 -4.395  8.099   1.00 18.32 ?  67  ASP   B OD1  1 
ATOM   5397 O OD2  . ASP   B 1 67  ? 52.436 -4.913  6.462   1.00 17.94 -1 67  ASP   B OD2  1 
ATOM   5398 H H    . ASP   B 1 67  ? 53.858 -9.049  7.716   1.00 15.95 ?  67  ASP   B H    1 
ATOM   5399 H HA   . ASP   B 1 67  ? 53.344 -7.047  9.315   1.00 16.87 ?  67  ASP   B HA   1 
ATOM   5400 H HB2  . ASP   B 1 67  ? 54.704 -6.686  7.505   1.00 18.38 ?  67  ASP   B HB2  1 
ATOM   5401 H HB3  . ASP   B 1 67  ? 53.534 -7.077  6.501   1.00 18.38 ?  67  ASP   B HB3  1 
ATOM   5402 N N    . TYR   B 1 68  ? 50.838 -7.934  7.499   1.00 14.16 ?  68  TYR   B N    1 
ATOM   5403 C CA   . TYR   B 1 68  ? 49.380 -7.857  7.431   1.00 14.55 ?  68  TYR   B CA   1 
ATOM   5404 C C    . TYR   B 1 68  ? 48.752 -8.198  8.780   1.00 14.31 ?  68  TYR   B C    1 
ATOM   5405 O O    . TYR   B 1 68  ? 47.818 -7.520  9.232   1.00 14.61 ?  68  TYR   B O    1 
ATOM   5406 C CB   . TYR   B 1 68  ? 48.847 -8.792  6.337   1.00 15.51 ?  68  TYR   B CB   1 
ATOM   5407 C CG   . TYR   B 1 68  ? 47.339 -8.944  6.391   1.00 16.72 ?  68  TYR   B CG   1 
ATOM   5408 C CD1  . TYR   B 1 68  ? 46.751 -9.899  7.212   1.00 16.99 ?  68  TYR   B CD1  1 
ATOM   5409 C CD2  . TYR   B 1 68  ? 46.504 -8.109  5.661   1.00 18.19 ?  68  TYR   B CD2  1 
ATOM   5410 C CE1  . TYR   B 1 68  ? 45.382 -10.022 7.305   1.00 18.38 ?  68  TYR   B CE1  1 
ATOM   5411 C CE2  . TYR   B 1 68  ? 45.119 -8.240  5.735   1.00 17.96 ?  68  TYR   B CE2  1 
ATOM   5412 C CZ   . TYR   B 1 68  ? 44.578 -9.200  6.561   1.00 18.20 ?  68  TYR   B CZ   1 
ATOM   5413 O OH   . TYR   B 1 68  ? 43.208 -9.325  6.672   1.00 19.24 ?  68  TYR   B OH   1 
ATOM   5414 H H    . TYR   B 1 68  ? 51.198 -8.483  6.933   1.00 16.99 ?  68  TYR   B H    1 
ATOM   5415 H HA   . TYR   B 1 68  ? 49.131 -6.951  7.206   1.00 17.46 ?  68  TYR   B HA   1 
ATOM   5416 H HB2  . TYR   B 1 68  ? 49.078 -8.427  5.469   1.00 18.61 ?  68  TYR   B HB2  1 
ATOM   5417 H HB3  . TYR   B 1 68  ? 49.242 -9.670  6.446   1.00 18.61 ?  68  TYR   B HB3  1 
ATOM   5418 H HD1  . TYR   B 1 68  ? 47.294 -10.465 7.716   1.00 20.39 ?  68  TYR   B HD1  1 
ATOM   5419 H HD2  . TYR   B 1 68  ? 46.875 -7.456  5.115   1.00 21.82 ?  68  TYR   B HD2  1 
ATOM   5420 H HE1  . TYR   B 1 68  ? 45.005 -10.681 7.845   1.00 22.06 ?  68  TYR   B HE1  1 
ATOM   5421 H HE2  . TYR   B 1 68  ? 44.561 -7.676  5.246   1.00 21.55 ?  68  TYR   B HE2  1 
ATOM   5422 H HH   . TYR   B 1 68  ? 42.815 -8.783  6.161   1.00 23.09 ?  68  TYR   B HH   1 
ATOM   5423 N N    . ILE   B 1 69  ? 49.251 -9.252  9.434   1.00 13.57 ?  69  ILE   B N    1 
ATOM   5424 C CA   . ILE   B 1 69  ? 48.699 -9.676  10.723  1.00 13.78 ?  69  ILE   B CA   1 
ATOM   5425 C C    . ILE   B 1 69  ? 48.941 -8.610  11.789  1.00 13.95 ?  69  ILE   B C    1 
ATOM   5426 O O    . ILE   B 1 69  ? 48.064 -8.322  12.615  1.00 14.29 ?  69  ILE   B O    1 
ATOM   5427 C CB   . ILE   B 1 69  ? 49.276 -11.048 11.138  1.00 14.88 ?  69  ILE   B CB   1 
ATOM   5428 C CG1  . ILE   B 1 69  ? 48.765 -12.178 10.229  1.00 15.44 ?  69  ILE   B CG1  1 
ATOM   5429 C CG2  . ILE   B 1 69  ? 48.970 -11.344 12.600  1.00 15.81 ?  69  ILE   B CG2  1 
ATOM   5430 C CD1  . ILE   B 1 69  ? 47.275 -12.486 10.357  1.00 16.09 ?  69  ILE   B CD1  1 
ATOM   5431 H H    . ILE   B 1 69  ? 49.908 -9.744  9.151   1.00 16.28 ?  69  ILE   B H    1 
ATOM   5432 H HA   . ILE   B 1 69  ? 47.746 -9.784  10.621  1.00 16.53 ?  69  ILE   B HA   1 
ATOM   5433 H HB   . ILE   B 1 69  ? 50.244 -11.008 11.045  1.00 17.86 ?  69  ILE   B HB   1 
ATOM   5434 H HG12 . ILE   B 1 69  ? 48.940 -11.932 9.306   1.00 18.53 ?  69  ILE   B HG12 1 
ATOM   5435 H HG13 . ILE   B 1 69  ? 49.255 -12.991 10.442  1.00 18.53 ?  69  ILE   B HG13 1 
ATOM   5436 H HG21 . ILE   B 1 69  ? 49.123 -12.288 12.767  1.00 18.97 ?  69  ILE   B HG21 1 
ATOM   5437 H HG22 . ILE   B 1 69  ? 49.551 -10.814 13.165  1.00 18.97 ?  69  ILE   B HG22 1 
ATOM   5438 H HG23 . ILE   B 1 69  ? 48.041 -11.127 12.776  1.00 18.97 ?  69  ILE   B HG23 1 
ATOM   5439 H HD11 . ILE   B 1 69  ? 47.056 -13.218 9.759   1.00 19.31 ?  69  ILE   B HD11 1 
ATOM   5440 H HD12 . ILE   B 1 69  ? 47.081 -12.738 11.272  1.00 19.31 ?  69  ILE   B HD12 1 
ATOM   5441 H HD13 . ILE   B 1 69  ? 46.767 -11.698 10.112  1.00 19.31 ?  69  ILE   B HD13 1 
ATOM   5442 N N    . ALA   B 1 70  ? 50.133 -8.016  11.802  1.00 13.44 ?  70  ALA   B N    1 
ATOM   5443 C CA   . ALA   B 1 70  ? 50.414 -6.968  12.779  1.00 13.28 ?  70  ALA   B CA   1 
ATOM   5444 C C    . ALA   B 1 70  ? 49.407 -5.832  12.671  1.00 14.49 ?  70  ALA   B C    1 
ATOM   5445 O O    . ALA   B 1 70  ? 48.995 -5.261  13.683  1.00 14.81 ?  70  ALA   B O    1 
ATOM   5446 C CB   . ALA   B 1 70  ? 51.832 -6.429  12.587  1.00 14.14 ?  70  ALA   B CB   1 
ATOM   5447 H H    . ALA   B 1 70  ? 50.782 -8.206  11.278  1.00 16.12 ?  70  ALA   B H    1 
ATOM   5448 H HA   . ALA   B 1 70  ? 50.358 -7.338  13.677  1.00 15.94 ?  70  ALA   B HA   1 
ATOM   5449 H HB1  . ALA   B 1 70  ? 52.018 -5.766  13.272  1.00 16.97 ?  70  ALA   B HB1  1 
ATOM   5450 H HB2  . ALA   B 1 70  ? 52.466 -7.162  12.662  1.00 16.97 ?  70  ALA   B HB2  1 
ATOM   5451 H HB3  . ALA   B 1 70  ? 51.903 -6.025  11.707  1.00 16.97 ?  70  ALA   B HB3  1 
ATOM   5452 N N    . THR   B 1 71  ? 49.009 -5.489  11.451  1.00 14.71 ?  71  THR   B N    1 
ATOM   5453 C CA   . THR   B 1 71  ? 48.087 -4.375  11.249  1.00 16.22 ?  71  THR   B CA   1 
ATOM   5454 C C    . THR   B 1 71  ? 46.630 -4.773  11.471  1.00 16.70 ?  71  THR   B C    1 
ATOM   5455 O O    . THR   B 1 71  ? 45.844 -3.978  12.006  1.00 18.15 ?  71  THR   B O    1 
ATOM   5456 C CB   . THR   B 1 71  ? 48.292 -3.792  9.848   1.00 18.45 ?  71  THR   B CB   1 
ATOM   5457 O OG1  . THR   B 1 71  ? 49.601 -3.213  9.763   1.00 21.23 ?  71  THR   B OG1  1 
ATOM   5458 C CG2  . THR   B 1 71  ? 47.245 -2.734  9.527   1.00 19.99 ?  71  THR   B CG2  1 
ATOM   5459 H H    . THR   B 1 71  ? 49.248 -5.895  10.728  1.00 17.66 ?  71  THR   B H    1 
ATOM   5460 H HA   . THR   B 1 71  ? 48.305 -3.683  11.889  1.00 19.46 ?  71  THR   B HA   1 
ATOM   5461 H HB   . THR   B 1 71  ? 48.225 -4.500  9.187   1.00 22.14 ?  71  THR   B HB   1 
ATOM   5462 H HG1  . THR   B 1 71  ? 49.719 -2.876  8.994   1.00 25.48 ?  71  THR   B HG1  1 
ATOM   5463 H HG21 . THR   B 1 71  ? 47.532 -2.204  8.766   1.00 23.99 ?  71  THR   B HG21 1 
ATOM   5464 H HG22 . THR   B 1 71  ? 46.400 -3.156  9.315   1.00 23.99 ?  71  THR   B HG22 1 
ATOM   5465 H HG23 . THR   B 1 71  ? 47.127 -2.146  10.289  1.00 23.99 ?  71  THR   B HG23 1 
ATOM   5466 N N    . ASN   B 1 72  ? 46.252 -5.990  11.082  1.00 16.03 ?  72  ASN   B N    1 
ATOM   5467 C CA   . ASN   B 1 72  ? 44.849 -6.359  10.964  1.00 17.14 ?  72  ASN   B CA   1 
ATOM   5468 C C    . ASN   B 1 72  ? 44.388 -7.453  11.915  1.00 17.71 ?  72  ASN   B C    1 
ATOM   5469 O O    . ASN   B 1 72  ? 43.172 -7.609  12.092  1.00 18.76 ?  72  ASN   B O    1 
ATOM   5470 C CB   . ASN   B 1 72  ? 44.532 -6.793  9.523   1.00 17.85 ?  72  ASN   B CB   1 
ATOM   5471 C CG   . ASN   B 1 72  ? 44.788 -5.690  8.518   1.00 18.94 ?  72  ASN   B CG   1 
ATOM   5472 O OD1  . ASN   B 1 72  ? 45.806 -5.689  7.810   1.00 20.95 ?  72  ASN   B OD1  1 
ATOM   5473 N ND2  . ASN   B 1 72  ? 43.893 -4.725  8.473   1.00 20.75 ?  72  ASN   B ND2  1 
ATOM   5474 H H    . ASN   B 1 72  ? 46.799 -6.633  10.894  1.00 19.24 ?  72  ASN   B H    1 
ATOM   5475 H HA   . ASN   B 1 72  ? 44.314 -5.576  11.154  1.00 20.56 ?  72  ASN   B HA   1 
ATOM   5476 H HB2  . ASN   B 1 72  ? 45.097 -7.545  9.287   1.00 21.42 ?  72  ASN   B HB2  1 
ATOM   5477 H HB3  . ASN   B 1 72  ? 43.601 -7.037  9.463   1.00 21.42 ?  72  ASN   B HB3  1 
ATOM   5478 H HD21 . ASN   B 1 72  ? 43.988 -4.066  7.922   1.00 24.90 ?  72  ASN   B HD21 1 
ATOM   5479 H HD22 . ASN   B 1 72  ? 43.198 -4.753  8.982   1.00 24.90 ?  72  ASN   B HD22 1 
ATOM   5480 N N    . GLY   B 1 73  ? 45.295 -8.208  12.523  1.00 16.65 ?  73  GLY   B N    1 
ATOM   5481 C CA   . GLY   B 1 73  ? 44.905 -9.356  13.305  1.00 16.15 ?  73  GLY   B CA   1 
ATOM   5482 C C    . GLY   B 1 73  ? 44.566 -10.540 12.423  1.00 13.51 ?  73  GLY   B C    1 
ATOM   5483 O O    . GLY   B 1 73  ? 44.548 -10.441 11.192  1.00 14.10 ?  73  GLY   B O    1 
ATOM   5484 H H    . GLY   B 1 73  ? 46.147 -8.070  12.499  1.00 19.98 ?  73  GLY   B H    1 
ATOM   5485 H HA2  . GLY   B 1 73  ? 45.626 -9.605  13.902  1.00 19.38 ?  73  GLY   B HA2  1 
ATOM   5486 H HA3  . GLY   B 1 73  ? 44.124 -9.131  13.840  1.00 19.38 ?  73  GLY   B HA3  1 
ATOM   5487 N N    . PRO   B 1 74  ? 44.274 -11.681 13.051  1.00 14.66 ?  74  PRO   B N    1 
ATOM   5488 C CA   . PRO   B 1 74  ? 44.025 -12.912 12.293  1.00 14.04 ?  74  PRO   B CA   1 
ATOM   5489 C C    . PRO   B 1 74  ? 42.718 -12.861 11.513  1.00 13.44 ?  74  PRO   B C    1 
ATOM   5490 O O    . PRO   B 1 74  ? 41.775 -12.137 11.856  1.00 15.66 ?  74  PRO   B O    1 
ATOM   5491 C CB   . PRO   B 1 74  ? 43.960 -13.985 13.388  1.00 15.16 ?  74  PRO   B CB   1 
ATOM   5492 C CG   . PRO   B 1 74  ? 43.489 -13.253 14.595  1.00 17.03 ?  74  PRO   B CG   1 
ATOM   5493 C CD   . PRO   B 1 74  ? 44.142 -11.895 14.502  1.00 16.05 ?  74  PRO   B CD   1 
ATOM   5494 H HA   . PRO   B 1 74  ? 44.767 -13.095 11.692  1.00 16.84 ?  74  PRO   B HA   1 
ATOM   5495 H HB2  . PRO   B 1 74  ? 43.328 -14.674 13.131  1.00 18.20 ?  74  PRO   B HB2  1 
ATOM   5496 H HB3  . PRO   B 1 74  ? 44.842 -14.360 13.533  1.00 18.20 ?  74  PRO   B HB3  1 
ATOM   5497 H HG2  . PRO   B 1 74  ? 42.520 -13.169 14.573  1.00 20.44 ?  74  PRO   B HG2  1 
ATOM   5498 H HG3  . PRO   B 1 74  ? 43.774 -13.717 15.396  1.00 20.44 ?  74  PRO   B HG3  1 
ATOM   5499 H HD2  . PRO   B 1 74  ? 43.569 -11.216 14.901  1.00 19.26 ?  74  PRO   B HD2  1 
ATOM   5500 H HD3  . PRO   B 1 74  ? 45.015 -11.910 14.919  1.00 19.26 ?  74  PRO   B HD3  1 
ATOM   5501 N N    . LEU   B 1 75  ? 42.677 -13.650 10.446  1.00 13.16 ?  75  LEU   B N    1 
ATOM   5502 C CA   . LEU   B 1 75  ? 41.460 -13.860 9.679   1.00 12.58 ?  75  LEU   B CA   1 
ATOM   5503 C C    . LEU   B 1 75  ? 40.474 -14.697 10.488  1.00 13.77 ?  75  LEU   B C    1 
ATOM   5504 O O    . LEU   B 1 75  ? 40.819 -15.303 11.501  1.00 14.80 ?  75  LEU   B O    1 
ATOM   5505 C CB   . LEU   B 1 75  ? 41.779 -14.593 8.376   1.00 12.65 ?  75  LEU   B CB   1 
ATOM   5506 C CG   . LEU   B 1 75  ? 42.591 -13.819 7.332   1.00 15.09 ?  75  LEU   B CG   1 
ATOM   5507 C CD1  . LEU   B 1 75  ? 42.813 -14.646 6.082   1.00 16.59 ?  75  LEU   B CD1  1 
ATOM   5508 C CD2  . LEU   B 1 75  ? 41.934 -12.508 6.986   1.00 18.87 ?  75  LEU   B CD2  1 
ATOM   5509 H H    . LEU   B 1 75  ? 43.361 -14.084 10.143  1.00 15.80 ?  75  LEU   B H    1 
ATOM   5510 H HA   . LEU   B 1 75  ? 41.054 -13.005 9.475   1.00 15.09 ?  75  LEU   B HA   1 
ATOM   5511 H HB2  . LEU   B 1 75  ? 42.285 -15.397 8.594   1.00 15.18 ?  75  LEU   B HB2  1 
ATOM   5512 H HB3  . LEU   B 1 75  ? 40.943 -14.850 7.959   1.00 15.18 ?  75  LEU   B HB3  1 
ATOM   5513 H HG   . LEU   B 1 75  ? 43.462 -13.616 7.709   1.00 18.11 ?  75  LEU   B HG   1 
ATOM   5514 H HD11 . LEU   B 1 75  ? 43.340 -14.128 5.449   1.00 19.90 ?  75  LEU   B HD11 1 
ATOM   5515 H HD12 . LEU   B 1 75  ? 43.292 -15.457 6.319   1.00 19.90 ?  75  LEU   B HD12 1 
ATOM   5516 H HD13 . LEU   B 1 75  ? 41.956 -14.870 5.691   1.00 19.90 ?  75  LEU   B HD13 1 
ATOM   5517 H HD21 . LEU   B 1 75  ? 42.382 -12.124 6.220   1.00 22.64 ?  75  LEU   B HD21 1 
ATOM   5518 H HD22 . LEU   B 1 75  ? 41.000 -12.671 6.779   1.00 22.64 ?  75  LEU   B HD22 1 
ATOM   5519 H HD23 . LEU   B 1 75  ? 42.003 -11.909 7.747   1.00 22.64 ?  75  LEU   B HD23 1 
ATOM   5520 N N    . LYS   B 1 76  ? 39.234 -14.747 10.006  1.00 15.63 ?  76  LYS   B N    1 
ATOM   5521 C CA   . LYS   B 1 76  ? 38.246 -15.704 10.486  1.00 16.98 ?  76  LYS   B CA   1 
ATOM   5522 C C    . LYS   B 1 76  ? 38.340 -16.984 9.663   1.00 15.47 ?  76  LYS   B C    1 
ATOM   5523 O O    . LYS   B 1 76  ? 38.620 -16.945 8.466   1.00 15.00 ?  76  LYS   B O    1 
ATOM   5524 C CB   . LYS   B 1 76  ? 36.828 -15.149 10.291  1.00 18.79 ?  76  LYS   B CB   1 
ATOM   5525 C CG   . LYS   B 1 76  ? 36.541 -13.779 10.922  1.00 20.59 ?  76  LYS   B CG   1 
ATOM   5526 C CD   . LYS   B 1 76  ? 35.130 -13.279 10.569  1.00 21.89 ?  76  LYS   B CD   1 
ATOM   5527 C CE   . LYS   B 1 76  ? 34.849 -11.908 11.176  1.00 24.63 ?  76  LYS   B CE   1 
ATOM   5528 N NZ   . LYS   B 1 76  ? 33.599 -11.274 10.672  1.00 24.90 ?  76  LYS   B NZ   1 
ATOM   5529 H H    . LYS   B 1 76  ? 38.936 -14.225 9.386   1.00 18.76 ?  76  LYS   B H    1 
ATOM   5530 H HA   . LYS   B 1 76  ? 38.394 -15.907 11.422  1.00 20.38 ?  76  LYS   B HA   1 
ATOM   5531 H HB2  . LYS   B 1 76  ? 36.663 -15.068 9.339   1.00 22.55 ?  76  LYS   B HB2  1 
ATOM   5532 H HB3  . LYS   B 1 76  ? 36.201 -15.780 10.675  1.00 22.55 ?  76  LYS   B HB3  1 
ATOM   5533 H HG2  . LYS   B 1 76  ? 36.608 -13.850 11.887  1.00 24.71 ?  76  LYS   B HG2  1 
ATOM   5534 H HG3  . LYS   B 1 76  ? 37.185 -13.131 10.589  1.00 24.71 ?  76  LYS   B HG3  1 
ATOM   5535 H HD2  . LYS   B 1 76  ? 35.045 -13.210 9.604   1.00 26.26 ?  76  LYS   B HD2  1 
ATOM   5536 H HD3  . LYS   B 1 76  ? 34.473 -13.906 10.916  1.00 26.26 ?  76  LYS   B HD3  1 
ATOM   5537 H HE2  . LYS   B 1 76  ? 34.770 -12.004 12.136  1.00 29.56 ?  76  LYS   B HE2  1 
ATOM   5538 H HE3  . LYS   B 1 76  ? 35.591 -11.319 10.963  1.00 29.56 ?  76  LYS   B HE3  1 
ATOM   5539 H HZ1  . LYS   B 1 76  ? 33.487 -10.477 11.055  1.00 29.88 ?  76  LYS   B HZ1  1 
ATOM   5540 H HZ2  . LYS   B 1 76  ? 33.648 -11.162 9.788   1.00 29.88 ?  76  LYS   B HZ2  1 
ATOM   5541 H HZ3  . LYS   B 1 76  ? 32.898 -11.787 10.859  1.00 29.88 ?  76  LYS   B HZ3  1 
ATOM   5542 N N    . VAL   B 1 77  ? 38.094 -18.129 10.310  1.00 16.51 ?  77  VAL   B N    1 
ATOM   5543 C CA   . VAL   B 1 77  ? 37.885 -19.353 9.540   1.00 16.63 ?  77  VAL   B CA   1 
ATOM   5544 C C    . VAL   B 1 77  ? 36.703 -19.132 8.605   1.00 14.81 ?  77  VAL   B C    1 
ATOM   5545 O O    . VAL   B 1 77  ? 35.633 -18.685 9.037   1.00 14.98 ?  77  VAL   B O    1 
ATOM   5546 C CB   . VAL   B 1 77  ? 37.671 -20.558 10.468  1.00 19.32 ?  77  VAL   B CB   1 
ATOM   5547 C CG1  . VAL   B 1 77  ? 37.376 -21.804 9.638   1.00 19.46 ?  77  VAL   B CG1  1 
ATOM   5548 C CG2  . VAL   B 1 77  ? 38.891 -20.776 11.371  1.00 20.63 ?  77  VAL   B CG2  1 
ATOM   5549 H H    . VAL   B 1 77  ? 38.050 -18.221 11.162  1.00 19.81 ?  77  VAL   B H    1 
ATOM   5550 H HA   . VAL   B 1 77  ? 38.669 -19.524 8.995   1.00 19.96 ?  77  VAL   B HA   1 
ATOM   5551 H HB   . VAL   B 1 77  ? 36.902 -20.385 11.034  1.00 23.18 ?  77  VAL   B HB   1 
ATOM   5552 H HG11 . VAL   B 1 77  ? 37.412 -22.580 10.218  1.00 23.35 ?  77  VAL   B HG11 1 
ATOM   5553 H HG12 . VAL   B 1 77  ? 36.488 -21.726 9.250   1.00 23.35 ?  77  VAL   B HG12 1 
ATOM   5554 H HG13 . VAL   B 1 77  ? 38.039 -21.881 8.938   1.00 23.35 ?  77  VAL   B HG13 1 
ATOM   5555 H HG21 . VAL   B 1 77  ? 38.742 -21.567 11.910  1.00 24.76 ?  77  VAL   B HG21 1 
ATOM   5556 H HG22 . VAL   B 1 77  ? 39.674 -20.894 10.814  1.00 24.76 ?  77  VAL   B HG22 1 
ATOM   5557 H HG23 . VAL   B 1 77  ? 39.001 -20.000 11.941  1.00 24.76 ?  77  VAL   B HG23 1 
ATOM   5558 N N    . GLY   B 1 78  ? 36.892 -19.429 7.315   1.00 14.23 ?  78  GLY   B N    1 
ATOM   5559 C CA   . GLY   B 1 78  ? 35.926 -19.106 6.289   1.00 13.31 ?  78  GLY   B CA   1 
ATOM   5560 C C    . GLY   B 1 78  ? 36.173 -17.790 5.585   1.00 13.50 ?  78  GLY   B C    1 
ATOM   5561 O O    . GLY   B 1 78  ? 35.477 -17.490 4.604   1.00 14.15 ?  78  GLY   B O    1 
ATOM   5562 H H    . GLY   B 1 78  ? 37.590 -19.837 7.014   1.00 17.07 ?  78  GLY   B H    1 
ATOM   5563 H HA2  . GLY   B 1 78  ? 35.933 -19.804 5.618   1.00 15.97 ?  78  GLY   B HA2  1 
ATOM   5564 H HA3  . GLY   B 1 78  ? 35.042 -19.078 6.687   1.00 15.97 ?  78  GLY   B HA3  1 
ATOM   5565 N N    . GLY   B 1 79  ? 37.123 -16.986 6.062   1.00 13.59 ?  79  GLY   B N    1 
ATOM   5566 C CA   . GLY   B 1 79  ? 37.422 -15.696 5.475   1.00 13.20 ?  79  GLY   B CA   1 
ATOM   5567 C C    . GLY   B 1 79  ? 38.656 -15.716 4.588   1.00 12.77 ?  79  GLY   B C    1 
ATOM   5568 O O    . GLY   B 1 79  ? 39.275 -16.755 4.349   1.00 12.96 ?  79  GLY   B O    1 
ATOM   5569 H H    . GLY   B 1 79  ? 37.623 -17.173 6.737   1.00 16.31 ?  79  GLY   B H    1 
ATOM   5570 H HA2  . GLY   B 1 79  ? 36.666 -15.405 4.932   1.00 15.85 ?  79  GLY   B HA2  1 
ATOM   5571 H HA3  . GLY   B 1 79  ? 37.563 -15.044 6.173   1.00 15.85 ?  79  GLY   B HA3  1 
ATOM   5572 N N    . SER   B 1 80  ? 39.030 -14.523 4.112   1.00 12.83 ?  80  SER   B N    1 
ATOM   5573 C CA   . SER   B 1 80  ? 40.133 -14.384 3.168   1.00 12.15 ?  80  SER   B CA   1 
ATOM   5574 C C    . SER   B 1 80  ? 40.706 -12.973 3.217   1.00 12.08 ?  80  SER   B C    1 
ATOM   5575 O O    . SER   B 1 80  ? 40.095 -12.040 3.738   1.00 13.34 ?  80  SER   B O    1 
ATOM   5576 C CB   . SER   B 1 80  ? 39.686 -14.693 1.737   1.00 12.49 ?  80  SER   B CB   1 
ATOM   5577 O OG   . SER   B 1 80  ? 38.855 -13.671 1.230   1.00 13.57 ?  80  SER   B OG   1 
ATOM   5578 H H    . SER   B 1 80  ? 38.660 -13.783 4.324   1.00 15.39 ?  80  SER   B H    1 
ATOM   5579 H HA   . SER   B 1 80  ? 40.831 -15.008 3.411   1.00 14.58 ?  80  SER   B HA   1 
ATOM   5580 H HB2  . SER   B 1 80  ? 40.467 -14.763 1.162   1.00 14.99 ?  80  SER   B HB2  1 
ATOM   5581 H HB3  . SER   B 1 80  ? 39.195 -15.530 1.726   1.00 14.99 ?  80  SER   B HB3  1 
ATOM   5582 H HG   . SER   B 1 80  ? 38.160 -13.594 1.712   1.00 16.28 ?  80  SER   B HG   1 
ATOM   5583 N N    . CYS   B 1 81  ? 41.891 -12.833 2.634   1.00 12.15 ?  81  CYS   B N    1 
ATOM   5584 C CA   . CYS   B 1 81  ? 42.444 -11.521 2.331   1.00 11.91 ?  81  CYS   B CA   1 
ATOM   5585 C C    . CYS   B 1 81  ? 43.231 -11.610 1.031   1.00 10.97 ?  81  CYS   B C    1 
ATOM   5586 O O    . CYS   B 1 81  ? 43.750 -12.674 0.673   1.00 12.62 ?  81  CYS   B O    1 
ATOM   5587 C CB   . CYS   B 1 81  ? 43.326 -10.989 3.462   1.00 12.67 ?  81  CYS   B CB   1 
ATOM   5588 S SG   . CYS   B 1 81  ? 44.866 -11.916 3.702   1.00 13.00 ?  81  CYS   B SG   1 
ATOM   5589 H H    . CYS   B 1 81  ? 42.398 -13.484 2.391   1.00 14.58 ?  81  CYS   B H    1 
ATOM   5590 H HA   . CYS   B 1 81  ? 41.713 -10.890 2.200   1.00 14.29 ?  81  CYS   B HA   1 
ATOM   5591 H HB2  . CYS   B 1 81  ? 43.560 -10.067 3.275   1.00 15.20 ?  81  CYS   B HB2  1 
ATOM   5592 H HB3  . CYS   B 1 81  ? 42.821 -11.030 4.295   1.00 15.20 ?  81  CYS   B HB3  1 
ATOM   5593 H HG   . CYS   B 1 81  ? 45.478 -11.424 4.613   1.00 15.60 ?  81  CYS   B HG   1 
ATOM   5594 N N    . VAL   B 1 82  ? 43.341 -10.469 0.347   1.00 11.65 ?  82  VAL   B N    1 
ATOM   5595 C CA   . VAL   B 1 82  ? 44.108 -10.342 -0.891  1.00 11.67 ?  82  VAL   B CA   1 
ATOM   5596 C C    . VAL   B 1 82  ? 45.445 -9.705  -0.566  1.00 11.98 ?  82  VAL   B C    1 
ATOM   5597 O O    . VAL   B 1 82  ? 45.497 -8.593  -0.029  1.00 13.25 ?  82  VAL   B O    1 
ATOM   5598 C CB   . VAL   B 1 82  ? 43.373 -9.506  -1.953  1.00 12.65 ?  82  VAL   B CB   1 
ATOM   5599 C CG1  . VAL   B 1 82  ? 44.232 -9.370  -3.213  1.00 14.42 ?  82  VAL   B CG1  1 
ATOM   5600 C CG2  . VAL   B 1 82  ? 42.009 -10.105 -2.270  1.00 13.71 ?  82  VAL   B CG2  1 
ATOM   5601 H H    . VAL   B 1 82  ? 42.957 -9.727  0.580   1.00 13.98 ?  82  VAL   B H    1 
ATOM   5602 H HA   . VAL   B 1 82  ? 44.271 -11.225 -1.254  1.00 14.01 ?  82  VAL   B HA   1 
ATOM   5603 H HB   . VAL   B 1 82  ? 43.234 -8.618  -1.604  1.00 15.17 ?  82  VAL   B HB   1 
ATOM   5604 H HG11 . VAL   B 1 82  ? 43.682 -9.041  -3.938  1.00 17.30 ?  82  VAL   B HG11 1 
ATOM   5605 H HG12 . VAL   B 1 82  ? 44.960 -8.750  -3.042  1.00 17.30 ?  82  VAL   B HG12 1 
ATOM   5606 H HG13 . VAL   B 1 82  ? 44.596 -10.244 -3.448  1.00 17.30 ?  82  VAL   B HG13 1 
ATOM   5607 H HG21 . VAL   B 1 82  ? 41.590 -9.581  -2.971  1.00 16.46 ?  82  VAL   B HG21 1 
ATOM   5608 H HG22 . VAL   B 1 82  ? 42.125 -11.022 -2.568  1.00 16.46 ?  82  VAL   B HG22 1 
ATOM   5609 H HG23 . VAL   B 1 82  ? 41.463 -10.084 -1.470  1.00 16.46 ?  82  VAL   B HG23 1 
ATOM   5610 N N    . LEU   B 1 83  ? 46.525 -10.389 -0.934  1.00 11.95 ?  83  LEU   B N    1 
ATOM   5611 C CA   . LEU   B 1 83  ? 47.888 -9.873  -0.814  1.00 11.84 ?  83  LEU   B CA   1 
ATOM   5612 C C    . LEU   B 1 83  ? 48.586 -10.021 -2.168  1.00 11.56 ?  83  LEU   B C    1 
ATOM   5613 O O    . LEU   B 1 83  ? 47.984 -10.450 -3.156  1.00 11.84 ?  83  LEU   B O    1 
ATOM   5614 C CB   . LEU   B 1 83  ? 48.632 -10.551 0.342   1.00 12.28 ?  83  LEU   B CB   1 
ATOM   5615 C CG   . LEU   B 1 83  ? 48.138 -10.195 1.747   1.00 13.66 ?  83  LEU   B CG   1 
ATOM   5616 C CD1  . LEU   B 1 83  ? 48.775 -11.076 2.814   1.00 14.22 ?  83  LEU   B CD1  1 
ATOM   5617 C CD2  . LEU   B 1 83  ? 48.330 -8.698  2.074   1.00 14.59 ?  83  LEU   B CD2  1 
ATOM   5618 H H    . LEU   B 1 83  ? 46.488 -11.186 -1.275  1.00 14.34 ?  83  LEU   B H    1 
ATOM   5619 H HA   . LEU   B 1 83  ? 47.832 -8.929  -0.624  1.00 14.21 ?  83  LEU   B HA   1 
ATOM   5620 H HB2  . LEU   B 1 83  ? 48.549 -11.511 0.236   1.00 14.74 ?  83  LEU   B HB2  1 
ATOM   5621 H HB3  . LEU   B 1 83  ? 49.566 -10.299 0.282   1.00 14.74 ?  83  LEU   B HB3  1 
ATOM   5622 H HG   . LEU   B 1 83  ? 47.188 -10.365 1.775   1.00 16.40 ?  83  LEU   B HG   1 
ATOM   5623 H HD11 . LEU   B 1 83  ? 48.434 -10.817 3.686   1.00 17.06 ?  83  LEU   B HD11 1 
ATOM   5624 H HD12 . LEU   B 1 83  ? 48.545 -12.005 2.637   1.00 17.06 ?  83  LEU   B HD12 1 
ATOM   5625 H HD13 . LEU   B 1 83  ? 49.738 -10.967 2.791   1.00 17.06 ?  83  LEU   B HD13 1 
ATOM   5626 H HD21 . LEU   B 1 83  ? 48.107 -8.548  3.008   1.00 17.51 ?  83  LEU   B HD21 1 
ATOM   5627 H HD22 . LEU   B 1 83  ? 49.250 -8.448  1.910   1.00 17.51 ?  83  LEU   B HD22 1 
ATOM   5628 H HD23 . LEU   B 1 83  ? 47.738 -8.172  1.510   1.00 17.51 ?  83  LEU   B HD23 1 
ATOM   5629 N N    . SER   B 1 84  ? 49.863 -9.655  -2.227  1.00 12.69 ?  84  SER   B N    1 
ATOM   5630 C CA   . SER   B 1 84  ? 50.592 -9.799  -3.479  1.00 13.13 ?  84  SER   B CA   1 
ATOM   5631 C C    . SER   B 1 84  ? 50.770 -11.272 -3.855  1.00 10.95 ?  84  SER   B C    1 
ATOM   5632 O O    . SER   B 1 84  ? 50.888 -12.142 -2.996  1.00 11.94 ?  84  SER   B O    1 
ATOM   5633 C CB   . SER   B 1 84  ? 51.972 -9.150  -3.361  1.00 14.62 ?  84  SER   B CB   1 
ATOM   5634 O OG   . SER   B 1 84  ? 52.728 -9.410  -4.529  1.00 16.26 ?  84  SER   B OG   1 
ATOM   5635 H H    . SER   B 1 84  ? 50.307 -9.307  -1.582  1.00 15.23 ?  84  SER   B H    1 
ATOM   5636 H HA   . SER   B 1 84  ? 50.108 -9.366  -4.195  1.00 15.76 ?  84  SER   B HA   1 
ATOM   5637 H HB2  . SER   B 1 84  ? 51.862 -8.190  -3.260  1.00 17.54 ?  84  SER   B HB2  1 
ATOM   5638 H HB3  . SER   B 1 84  ? 52.434 -9.514  -2.590  1.00 17.54 ?  84  SER   B HB3  1 
ATOM   5639 H HG   . SER   B 1 84  ? 53.495 -9.046  -4.461  1.00 19.52 ?  84  SER   B HG   1 
ATOM   5640 N N    . GLY   B 1 85  ? 50.841 -11.530 -5.161  1.00 12.00 ?  85  GLY   B N    1 
ATOM   5641 C CA   . GLY   B 1 85  ? 51.203 -12.826 -5.681  1.00 13.48 ?  85  GLY   B CA   1 
ATOM   5642 C C    . GLY   B 1 85  ? 52.669 -12.998 -5.993  1.00 13.25 ?  85  GLY   B C    1 
ATOM   5643 O O    . GLY   B 1 85  ? 53.060 -14.081 -6.429  1.00 13.76 ?  85  GLY   B O    1 
ATOM   5644 H H    . GLY   B 1 85  ? 50.685 -10.964 -5.774  1.00 14.41 ?  85  GLY   B H    1 
ATOM   5645 H HA2  . GLY   B 1 85  ? 50.949 -13.517 -5.040  1.00 16.18 ?  85  GLY   B HA2  1 
ATOM   5646 H HA3  . GLY   B 1 85  ? 50.705 -12.996 -6.499  1.00 16.18 ?  85  GLY   B HA3  1 
ATOM   5647 N N    . HIS   B 1 86  ? 53.504 -11.981 -5.789  1.00 13.19 ?  86  HIS   B N    1 
ATOM   5648 C CA   . HIS   B 1 86  ? 54.967 -12.127 -5.872  1.00 13.01 ?  86  HIS   B CA   1 
ATOM   5649 C C    . HIS   B 1 86  ? 55.344 -12.648 -7.257  1.00 13.02 ?  86  HIS   B C    1 
ATOM   5650 O O    . HIS   B 1 86  ? 54.955 -12.040 -8.267  1.00 14.26 ?  86  HIS   B O    1 
ATOM   5651 C CB   . HIS   B 1 86  ? 55.472 -12.952 -4.682  1.00 13.41 ?  86  HIS   B CB   1 
ATOM   5652 C CG   . HIS   B 1 86  ? 55.146 -12.342 -3.357  1.00 13.47 ?  86  HIS   B CG   1 
ATOM   5653 N ND1  . HIS   B 1 86  ? 55.956 -11.411 -2.743  1.00 15.55 ?  86  HIS   B ND1  1 
ATOM   5654 C CD2  . HIS   B 1 86  ? 54.080 -12.515 -2.540  1.00 14.21 ?  86  HIS   B CD2  1 
ATOM   5655 C CE1  . HIS   B 1 86  ? 55.391 -11.024 -1.611  1.00 15.64 ?  86  HIS   B CE1  1 
ATOM   5656 N NE2  . HIS   B 1 86  ? 54.248 -11.671 -1.469  1.00 14.82 ?  86  HIS   B NE2  1 
ATOM   5657 H H    . HIS   B 1 86  ? 53.246 -11.185 -5.602  1.00 15.82 ?  86  HIS   B H    1 
ATOM   5658 H HA   . HIS   B 1 86  ? 55.363 -11.247 -5.780  1.00 15.61 ?  86  HIS   B HA   1 
ATOM   5659 H HB2  . HIS   B 1 86  ? 55.070 -13.833 -4.715  1.00 16.10 ?  86  HIS   B HB2  1 
ATOM   5660 H HB3  . HIS   B 1 86  ? 56.439 -13.029 -4.737  1.00 16.10 ?  86  HIS   B HB3  1 
ATOM   5661 H HD2  . HIS   B 1 86  ? 53.345 -13.079 -2.695  1.00 17.05 ?  86  HIS   B HD2  1 
ATOM   5662 H HE1  . HIS   B 1 86  ? 55.741 -10.421 -1.002  1.00 18.77 ?  86  HIS   B HE1  1 
ATOM   5663 H HE2  . HIS   B 1 86  ? 53.708 -11.613 -0.795  1.00 17.78 ?  86  HIS   B HE2  1 
ATOM   5664 N N    . ASN   B 1 87  ? 56.106 -13.737 -7.358  1.00 13.45 ?  87  ASN   B N    1 
ATOM   5665 C CA   . ASN   B 1 87  ? 56.514 -14.317 -8.628  1.00 14.52 ?  87  ASN   B CA   1 
ATOM   5666 C C    . ASN   B 1 87  ? 55.544 -15.368 -9.130  1.00 13.89 ?  87  ASN   B C    1 
ATOM   5667 O O    . ASN   B 1 87  ? 55.870 -16.076 -10.089 1.00 16.30 ?  87  ASN   B O    1 
ATOM   5668 C CB   . ASN   B 1 87  ? 57.913 -14.940 -8.505  1.00 16.57 ?  87  ASN   B CB   1 
ATOM   5669 C CG   . ASN   B 1 87  ? 57.973 -16.048 -7.457  1.00 17.28 ?  87  ASN   B CG   1 
ATOM   5670 O OD1  . ASN   B 1 87  ? 57.352 -15.955 -6.396  1.00 16.47 ?  87  ASN   B OD1  1 
ATOM   5671 N ND2  . ASN   B 1 87  ? 58.722 -17.118 -7.761  1.00 19.70 ?  87  ASN   B ND2  1 
ATOM   5672 H H    . ASN   B 1 87  ? 56.399 -14.177 -6.679  1.00 16.14 ?  87  ASN   B H    1 
ATOM   5673 H HA   . ASN   B 1 87  ? 56.556 -13.620 -9.293  1.00 17.42 ?  87  ASN   B HA   1 
ATOM   5674 H HB2  . ASN   B 1 87  ? 58.169 -15.320 -9.363  1.00 19.88 ?  87  ASN   B HB2  1 
ATOM   5675 H HB3  . ASN   B 1 87  ? 58.543 -14.248 -8.251  1.00 19.88 ?  87  ASN   B HB3  1 
ATOM   5676 H HD21 . ASN   B 1 87  ? 58.798 -17.765 -7.202  1.00 23.64 ?  87  ASN   B HD21 1 
ATOM   5677 H HD22 . ASN   B 1 87  ? 59.146 -17.153 -8.514  1.00 23.64 ?  87  ASN   B HD22 1 
ATOM   5678 N N    . LEU   B 1 88  ? 54.366 -15.478 -8.515  1.00 13.04 ?  88  LEU   B N    1 
ATOM   5679 C CA   . LEU   B 1 88  ? 53.382 -16.504 -8.850  1.00 13.33 ?  88  LEU   B CA   1 
ATOM   5680 C C    . LEU   B 1 88  ? 52.150 -15.979 -9.569  1.00 13.61 ?  88  LEU   B C    1 
ATOM   5681 O O    . LEU   B 1 88  ? 51.548 -16.711 -10.361 1.00 15.37 ?  88  LEU   B O    1 
ATOM   5682 C CB   . LEU   B 1 88  ? 52.906 -17.197 -7.571  1.00 14.85 ?  88  LEU   B CB   1 
ATOM   5683 C CG   . LEU   B 1 88  ? 54.036 -17.846 -6.781  1.00 17.17 ?  88  LEU   B CG   1 
ATOM   5684 C CD1  . LEU   B 1 88  ? 53.559 -18.280 -5.410  1.00 18.90 ?  88  LEU   B CD1  1 
ATOM   5685 C CD2  . LEU   B 1 88  ? 54.592 -19.018 -7.562  1.00 21.47 ?  88  LEU   B CD2  1 
ATOM   5686 H H    . LEU   B 1 88  ? 54.101 -14.963 -7.876  1.00 15.65 ?  88  LEU   B H    1 
ATOM   5687 H HA   . LEU   B 1 88  ? 53.790 -17.173 -9.416  1.00 16.00 ?  88  LEU   B HA   1 
ATOM   5688 H HB2  . LEU   B 1 88  ? 52.471 -16.549 -6.995  1.00 17.82 ?  88  LEU   B HB2  1 
ATOM   5689 H HB3  . LEU   B 1 88  ? 52.268 -17.900 -7.806  1.00 17.82 ?  88  LEU   B HB3  1 
ATOM   5690 H HG   . LEU   B 1 88  ? 54.744 -17.196 -6.662  1.00 20.61 ?  88  LEU   B HG   1 
ATOM   5691 H HD11 . LEU   B 1 88  ? 54.267 -18.775 -4.975  1.00 22.68 ?  88  LEU   B HD11 1 
ATOM   5692 H HD12 . LEU   B 1 88  ? 53.330 -17.494 -4.892  1.00 22.68 ?  88  LEU   B HD12 1 
ATOM   5693 H HD13 . LEU   B 1 88  ? 52.776 -18.844 -5.519  1.00 22.68 ?  88  LEU   B HD13 1 
ATOM   5694 H HD21 . LEU   B 1 88  ? 55.200 -19.510 -6.993  1.00 25.77 ?  88  LEU   B HD21 1 
ATOM   5695 H HD22 . LEU   B 1 88  ? 53.859 -19.587 -7.840  1.00 25.77 ?  88  LEU   B HD22 1 
ATOM   5696 H HD23 . LEU   B 1 88  ? 55.064 -18.682 -8.341  1.00 25.77 ?  88  LEU   B HD23 1 
ATOM   5697 N N    . ALA   B 1 89  ? 51.739 -14.749 -9.286  1.00 13.17 ?  89  ALA   B N    1 
ATOM   5698 C CA   . ALA   B 1 89  ? 50.456 -14.234 -9.747  1.00 12.16 ?  89  ALA   B CA   1 
ATOM   5699 C C    . ALA   B 1 89  ? 50.443 -12.744 -9.451  1.00 12.43 ?  89  ALA   B C    1 
ATOM   5700 O O    . ALA   B 1 89  ? 51.259 -12.248 -8.676  1.00 13.36 ?  89  ALA   B O    1 
ATOM   5701 C CB   . ALA   B 1 89  ? 49.298 -14.894 -9.004  1.00 12.68 ?  89  ALA   B CB   1 
ATOM   5702 H H    . ALA   B 1 89  ? 52.185 -14.186 -8.820  1.00 15.80 ?  89  ALA   B H    1 
ATOM   5703 H HA   . ALA   B 1 89  ? 50.353 -14.373 -10.710 1.00 14.59 ?  89  ALA   B HA   1 
ATOM   5704 H HB1  . ALA   B 1 89  ? 48.461 -14.536 -9.346  1.00 15.22 ?  89  ALA   B HB1  1 
ATOM   5705 H HB2  . ALA   B 1 89  ? 49.334 -15.850 -9.155  1.00 15.22 ?  89  ALA   B HB2  1 
ATOM   5706 H HB3  . ALA   B 1 89  ? 49.383 -14.698 -8.062  1.00 15.22 ?  89  ALA   B HB3  1 
ATOM   5707 N N    . LYS   B 1 90  ? 49.483 -12.032 -10.035 1.00 13.13 ?  90  LYS   B N    1 
ATOM   5708 C CA   . LYS   B 1 90  ? 49.300 -10.645 -9.618  1.00 12.89 ?  90  LYS   B CA   1 
ATOM   5709 C C    . LYS   B 1 90  ? 48.954 -10.574 -8.133  1.00 12.68 ?  90  LYS   B C    1 
ATOM   5710 O O    . LYS   B 1 90  ? 49.600 -9.843  -7.369  1.00 13.60 ?  90  LYS   B O    1 
ATOM   5711 C CB   . LYS   B 1 90  ? 48.245 -9.959  -10.482 1.00 14.64 ?  90  LYS   B CB   1 
ATOM   5712 C CG   . LYS   B 1 90  ? 47.915 -8.531  -10.055 1.00 14.78 ?  90  LYS   B CG   1 
ATOM   5713 C CD   . LYS   B 1 90  ? 49.114 -7.612  -10.057 1.00 17.95 ?  90  LYS   B CD   1 
ATOM   5714 C CE   . LYS   B 1 90  ? 48.624 -6.200  -9.777  1.00 20.07 ?  90  LYS   B CE   1 
ATOM   5715 N NZ   . LYS   B 1 90  ? 49.741 -5.228  -9.727  1.00 20.02 ?  90  LYS   B NZ   1 
ATOM   5716 H H    . LYS   B 1 90  ? 48.948 -12.316 -10.642 1.00 15.76 ?  90  LYS   B H    1 
ATOM   5717 H HA   . LYS   B 1 90  ? 50.141 -10.177 -9.745  1.00 15.47 ?  90  LYS   B HA   1 
ATOM   5718 H HB2  . LYS   B 1 90  ? 48.570 -9.928  -11.396 1.00 17.56 ?  90  LYS   B HB2  1 
ATOM   5719 H HB3  . LYS   B 1 90  ? 47.430 -10.481 -10.443 1.00 17.56 ?  90  LYS   B HB3  1 
ATOM   5720 H HG2  . LYS   B 1 90  ? 47.260 -8.168  -10.670 1.00 17.73 ?  90  LYS   B HG2  1 
ATOM   5721 H HG3  . LYS   B 1 90  ? 47.546 -8.546  -9.156  1.00 17.73 ?  90  LYS   B HG3  1 
ATOM   5722 H HD2  . LYS   B 1 90  ? 49.735 -7.868  -9.354  1.00 21.54 ?  90  LYS   B HD2  1 
ATOM   5723 H HD3  . LYS   B 1 90  ? 49.548 -7.627  -10.923 1.00 21.54 ?  90  LYS   B HD3  1 
ATOM   5724 H HE2  . LYS   B 1 90  ? 48.018 -5.920  -10.484 1.00 24.08 ?  90  LYS   B HE2  1 
ATOM   5725 H HE3  . LYS   B 1 90  ? 48.170 -6.172  -8.920  1.00 24.08 ?  90  LYS   B HE3  1 
ATOM   5726 H HZ1  . LYS   B 1 90  ? 49.433 -4.404  -9.567  1.00 24.02 ?  90  LYS   B HZ1  1 
ATOM   5727 H HZ2  . LYS   B 1 90  ? 50.315 -5.447  -9.084  1.00 24.02 ?  90  LYS   B HZ2  1 
ATOM   5728 H HZ3  . LYS   B 1 90  ? 50.177 -5.216  -10.507 1.00 24.02 ?  90  LYS   B HZ3  1 
ATOM   5729 N N    . HIS   B 1 91  ? 47.963 -11.361 -7.699  1.00 11.51 ?  91  HIS   B N    1 
ATOM   5730 C CA   . HIS   B 1 91  ? 47.491 -11.390 -6.324  1.00 11.59 ?  91  HIS   B CA   1 
ATOM   5731 C C    . HIS   B 1 91  ? 47.492 -12.823 -5.810  1.00 10.44 ?  91  HIS   B C    1 
ATOM   5732 O O    . HIS   B 1 91  ? 47.263 -13.764 -6.579  1.00 11.64 ?  91  HIS   B O    1 
ATOM   5733 C CB   . HIS   B 1 91  ? 46.031 -10.923 -6.240  1.00 13.26 ?  91  HIS   B CB   1 
ATOM   5734 C CG   . HIS   B 1 91  ? 45.831 -9.501  -6.646  1.00 16.42 ?  91  HIS   B CG   1 
ATOM   5735 N ND1  . HIS   B 1 91  ? 46.443 -8.441  -6.010  1.00 19.48 ?  91  HIS   B ND1  1 
ATOM   5736 C CD2  . HIS   B 1 91  ? 45.052 -8.962  -7.611  1.00 19.77 ?  91  HIS   B CD2  1 
ATOM   5737 C CE1  . HIS   B 1 91  ? 46.059 -7.309  -6.576  1.00 20.83 ?  91  HIS   B CE1  1 
ATOM   5738 N NE2  . HIS   B 1 91  ? 45.215 -7.599  -7.551  1.00 21.53 ?  91  HIS   B NE2  1 
ATOM   5739 H H    . HIS   B 1 91  ? 47.532 -11.906 -8.208  1.00 13.81 ?  91  HIS   B H    1 
ATOM   5740 H HA   . HIS   B 1 91  ? 48.046 -10.828 -5.755  1.00 13.90 ?  91  HIS   B HA   1 
ATOM   5741 H HB2  . HIS   B 1 91  ? 45.491 -11.478 -6.823  1.00 15.91 ?  91  HIS   B HB2  1 
ATOM   5742 H HB3  . HIS   B 1 91  ? 45.725 -11.016 -5.322  1.00 15.91 ?  91  HIS   B HB3  1 
ATOM   5743 H HD2  . HIS   B 1 91  ? 44.513 -9.424  -8.213  1.00 23.72 ?  91  HIS   B HD2  1 
ATOM   5744 H HE1  . HIS   B 1 91  ? 46.333 -6.455  -6.331  1.00 25.00 ?  91  HIS   B HE1  1 
ATOM   5745 H HE2  . HIS   B 1 91  ? 44.834 -7.023  -8.068  1.00 25.83 ?  91  HIS   B HE2  1 
ATOM   5746 N N    . CYS   B 1 92  ? 47.678 -12.972 -4.507  1.00 10.62 ?  92  CYS   B N    1 
ATOM   5747 C CA   . CYS   B 1 92  ? 47.367 -14.213 -3.798  1.00 10.69 ?  92  CYS   B CA   1 
ATOM   5748 C C    . CYS   B 1 92  ? 46.140 -13.973 -2.923  1.00 10.42 ?  92  CYS   B C    1 
ATOM   5749 O O    . CYS   B 1 92  ? 46.140 -13.064 -2.084  1.00 11.76 ?  92  CYS   B O    1 
ATOM   5750 C CB   . CYS   B 1 92  ? 48.544 -14.671 -2.937  1.00 10.85 ?  92  CYS   B CB   1 
ATOM   5751 S SG   . CYS   B 1 92  ? 48.172 -16.193 -2.030  1.00 11.40 ?  92  CYS   B SG   1 
ATOM   5752 H H    . CYS   B 1 92  ? 48.020 -12.362 -3.997  1.00 12.75 ?  92  CYS   B H    1 
ATOM   5753 H HA   . CYS   B 1 92  ? 47.168 -14.908 -4.447  1.00 12.83 ?  92  CYS   B HA   1 
ATOM   5754 H HB2  . CYS   B 1 92  ? 49.309 -14.838 -3.508  1.00 13.02 ?  92  CYS   B HB2  1 
ATOM   5755 H HB3  . CYS   B 1 92  ? 48.748 -13.981 -2.292  1.00 13.02 ?  92  CYS   B HB3  1 
ATOM   5756 H HG   . CYS   B 1 92  ? 49.143 -16.509 -1.401  1.00 13.68 ?  92  CYS   B HG   1 
ATOM   5757 N N    . LEU   B 1 93  ? 45.098 -14.773 -3.134  1.00 10.43 ?  93  LEU   B N    1 
ATOM   5758 C CA   . LEU   B 1 93  ? 43.922 -14.782 -2.271  1.00 10.33 ?  93  LEU   B CA   1 
ATOM   5759 C C    . LEU   B 1 93  ? 44.140 -15.840 -1.199  1.00 9.95  ?  93  LEU   B C    1 
ATOM   5760 O O    . LEU   B 1 93  ? 44.094 -17.044 -1.488  1.00 11.24 ?  93  LEU   B O    1 
ATOM   5761 C CB   . LEU   B 1 93  ? 42.659 -15.068 -3.081  1.00 11.04 ?  93  LEU   B CB   1 
ATOM   5762 C CG   . LEU   B 1 93  ? 41.351 -15.081 -2.280  1.00 11.90 ?  93  LEU   B CG   1 
ATOM   5763 C CD1  . LEU   B 1 93  ? 40.978 -13.693 -1.803  1.00 12.35 ?  93  LEU   B CD1  1 
ATOM   5764 C CD2  . LEU   B 1 93  ? 40.224 -15.679 -3.097  1.00 12.46 ?  93  LEU   B CD2  1 
ATOM   5765 H H    . LEU   B 1 93  ? 45.045 -15.338 -3.792  1.00 12.52 ?  93  LEU   B H    1 
ATOM   5766 H HA   . LEU   B 1 93  ? 43.829 -13.914 -1.848  1.00 12.39 ?  93  LEU   B HA   1 
ATOM   5767 H HB2  . LEU   B 1 93  ? 42.574 -14.388 -3.768  1.00 13.25 ?  93  LEU   B HB2  1 
ATOM   5768 H HB3  . LEU   B 1 93  ? 42.754 -15.938 -3.497  1.00 13.25 ?  93  LEU   B HB3  1 
ATOM   5769 H HG   . LEU   B 1 93  ? 41.469 -15.634 -1.496  1.00 14.28 ?  93  LEU   B HG   1 
ATOM   5770 H HD11 . LEU   B 1 93  ? 40.129 -13.738 -1.339  1.00 14.83 ?  93  LEU   B HD11 1 
ATOM   5771 H HD12 . LEU   B 1 93  ? 41.668 -13.365 -1.213  1.00 14.83 ?  93  LEU   B HD12 1 
ATOM   5772 H HD13 . LEU   B 1 93  ? 40.898 -13.108 -2.579  1.00 14.83 ?  93  LEU   B HD13 1 
ATOM   5773 H HD21 . LEU   B 1 93  ? 39.407 -15.664 -2.568  1.00 14.95 ?  93  LEU   B HD21 1 
ATOM   5774 H HD22 . LEU   B 1 93  ? 40.098 -15.151 -3.904  1.00 14.95 ?  93  LEU   B HD22 1 
ATOM   5775 H HD23 . LEU   B 1 93  ? 40.447 -16.592 -3.331  1.00 14.95 ?  93  LEU   B HD23 1 
ATOM   5776 N N    . HIS   B 1 94  ? 44.419 -15.404 0.028   1.00 10.23 ?  94  HIS   B N    1 
ATOM   5777 C CA   . HIS   B 1 94  ? 44.628 -16.305 1.157   1.00 9.80  ?  94  HIS   B CA   1 
ATOM   5778 C C    . HIS   B 1 94  ? 43.263 -16.655 1.736   1.00 11.23 ?  94  HIS   B C    1 
ATOM   5779 O O    . HIS   B 1 94  ? 42.591 -15.784 2.289   1.00 12.25 ?  94  HIS   B O    1 
ATOM   5780 C CB   . HIS   B 1 94  ? 45.504 -15.646 2.214   1.00 10.93 ?  94  HIS   B CB   1 
ATOM   5781 C CG   . HIS   B 1 94  ? 46.884 -15.337 1.740   1.00 10.96 ?  94  HIS   B CG   1 
ATOM   5782 N ND1  . HIS   B 1 94  ? 47.914 -16.246 1.832   1.00 11.74 ?  94  HIS   B ND1  1 
ATOM   5783 C CD2  . HIS   B 1 94  ? 47.395 -14.227 1.154   1.00 11.27 ?  94  HIS   B CD2  1 
ATOM   5784 C CE1  . HIS   B 1 94  ? 49.005 -15.700 1.323   1.00 11.83 ?  94  HIS   B CE1  1 
ATOM   5785 N NE2  . HIS   B 1 94  ? 48.720 -14.478 0.906   1.00 11.85 ?  94  HIS   B NE2  1 
ATOM   5786 H H    . HIS   B 1 94  ? 44.501 -14.564 0.230   1.00 12.28 ?  94  HIS   B H    1 
ATOM   5787 H HA   . HIS   B 1 94  ? 45.056 -17.118 0.843   1.00 11.76 ?  94  HIS   B HA   1 
ATOM   5788 H HB2  . HIS   B 1 94  ? 45.092 -14.816 2.482   1.00 13.12 ?  94  HIS   B HB2  1 
ATOM   5789 H HB3  . HIS   B 1 94  ? 45.578 -16.248 2.966   1.00 13.12 ?  94  HIS   B HB3  1 
ATOM   5790 H HD2  . HIS   B 1 94  ? 46.940 -13.443 0.960   1.00 13.53 ?  94  HIS   B HD2  1 
ATOM   5791 H HE1  . HIS   B 1 94  ? 49.835 -16.120 1.262   1.00 14.19 ?  94  HIS   B HE1  1 
ATOM   5792 H HE2  . HIS   B 1 94  ? 49.279 -13.935 0.545   1.00 14.21 ?  94  HIS   B HE2  1 
ATOM   5793 N N    . VAL   B 1 95  ? 42.829 -17.910 1.581   1.00 11.08 ?  95  VAL   B N    1 
ATOM   5794 C CA   . VAL   B 1 95  ? 41.499 -18.357 2.010   1.00 10.73 ?  95  VAL   B CA   1 
ATOM   5795 C C    . VAL   B 1 95  ? 41.652 -19.398 3.108   1.00 10.87 ?  95  VAL   B C    1 
ATOM   5796 O O    . VAL   B 1 95  ? 42.428 -20.348 2.955   1.00 11.97 ?  95  VAL   B O    1 
ATOM   5797 C CB   . VAL   B 1 95  ? 40.692 -18.967 0.847   1.00 11.42 ?  95  VAL   B CB   1 
ATOM   5798 C CG1  . VAL   B 1 95  ? 39.305 -19.431 1.333   1.00 13.03 ?  95  VAL   B CG1  1 
ATOM   5799 C CG2  . VAL   B 1 95  ? 40.558 -17.983 -0.306  1.00 11.59 ?  95  VAL   B CG2  1 
ATOM   5800 H H    . VAL   B 1 95  ? 43.293 -18.538 1.211   1.00 13.30 ?  95  VAL   B H    1 
ATOM   5801 H HA   . VAL   B 1 95  ? 41.001 -17.607 2.364   1.00 12.88 ?  95  VAL   B HA   1 
ATOM   5802 H HB   . VAL   B 1 95  ? 41.156 -19.748 0.513   1.00 13.70 ?  95  VAL   B HB   1 
ATOM   5803 H HG11 . VAL   B 1 95  ? 38.743 -19.625 0.559   1.00 15.64 ?  95  VAL   B HG11 1 
ATOM   5804 H HG12 . VAL   B 1 95  ? 39.400 -20.233 1.870   1.00 15.64 ?  95  VAL   B HG12 1 
ATOM   5805 H HG13 . VAL   B 1 95  ? 38.895 -18.726 1.859   1.00 15.64 ?  95  VAL   B HG13 1 
ATOM   5806 H HG21 . VAL   B 1 95  ? 39.994 -18.374 -0.987  1.00 13.91 ?  95  VAL   B HG21 1 
ATOM   5807 H HG22 . VAL   B 1 95  ? 40.160 -17.166 0.031   1.00 13.91 ?  95  VAL   B HG22 1 
ATOM   5808 H HG23 . VAL   B 1 95  ? 41.440 -17.805 -0.659  1.00 13.91 ?  95  VAL   B HG23 1 
ATOM   5809 N N    . VAL   B 1 96  ? 40.921 -19.228 4.205   1.00 11.39 ?  96  VAL   B N    1 
ATOM   5810 C CA   . VAL   B 1 96  ? 41.005 -20.137 5.350   1.00 11.28 ?  96  VAL   B CA   1 
ATOM   5811 C C    . VAL   B 1 96  ? 39.819 -21.098 5.310   1.00 13.19 ?  96  VAL   B C    1 
ATOM   5812 O O    . VAL   B 1 96  ? 38.700 -20.736 5.688   1.00 13.67 ?  96  VAL   B O    1 
ATOM   5813 C CB   . VAL   B 1 96  ? 41.055 -19.394 6.687   1.00 12.86 ?  96  VAL   B CB   1 
ATOM   5814 C CG1  . VAL   B 1 96  ? 41.226 -20.380 7.832   1.00 13.67 ?  96  VAL   B CG1  1 
ATOM   5815 C CG2  . VAL   B 1 96  ? 42.178 -18.358 6.691   1.00 13.38 ?  96  VAL   B CG2  1 
ATOM   5816 H H    . VAL   B 1 96  ? 40.349 -18.594 4.311   1.00 13.67 ?  96  VAL   B H    1 
ATOM   5817 H HA   . VAL   B 1 96  ? 41.818 -20.664 5.273   1.00 13.53 ?  96  VAL   B HA   1 
ATOM   5818 H HB   . VAL   B 1 96  ? 40.215 -18.927 6.817   1.00 15.43 ?  96  VAL   B HB   1 
ATOM   5819 H HG11 . VAL   B 1 96  ? 41.423 -19.888 8.646   1.00 16.40 ?  96  VAL   B HG11 1 
ATOM   5820 H HG12 . VAL   B 1 96  ? 40.411 -20.891 7.944   1.00 16.40 ?  96  VAL   B HG12 1 
ATOM   5821 H HG13 . VAL   B 1 96  ? 41.967 -20.978 7.627   1.00 16.40 ?  96  VAL   B HG13 1 
ATOM   5822 H HG21 . VAL   B 1 96  ? 42.222 -17.945 7.566   1.00 16.06 ?  96  VAL   B HG21 1 
ATOM   5823 H HG22 . VAL   B 1 96  ? 43.014 -18.796 6.484   1.00 16.06 ?  96  VAL   B HG22 1 
ATOM   5824 H HG23 . VAL   B 1 96  ? 41.984 -17.681 6.017   1.00 16.06 ?  96  VAL   B HG23 1 
ATOM   5825 N N    . GLY   B 1 97  ? 40.056 -22.336 4.875   1.00 13.03 ?  97  GLY   B N    1 
ATOM   5826 C CA   . GLY   B 1 97  ? 39.081 -23.387 5.047   1.00 14.22 ?  97  GLY   B CA   1 
ATOM   5827 C C    . GLY   B 1 97  ? 39.217 -23.991 6.428   1.00 15.46 ?  97  GLY   B C    1 
ATOM   5828 O O    . GLY   B 1 97  ? 40.262 -23.869 7.083   1.00 16.13 ?  97  GLY   B O    1 
ATOM   5829 H H    . GLY   B 1 97  ? 40.781 -22.584 4.472   1.00 15.64 ?  97  GLY   B H    1 
ATOM   5830 H HA2  . GLY   B 1 97  ? 38.190 -23.019 4.936   1.00 17.07 ?  97  GLY   B HA2  1 
ATOM   5831 H HA3  . GLY   B 1 97  ? 39.219 -24.077 4.376   1.00 17.07 ?  97  GLY   B HA3  1 
ATOM   5832 N N    . PRO   B 1 98  ? 38.172 -24.668 6.898   1.00 17.03 ?  98  PRO   B N    1 
ATOM   5833 C CA   . PRO   B 1 98  ? 38.275 -25.368 8.183   1.00 18.31 ?  98  PRO   B CA   1 
ATOM   5834 C C    . PRO   B 1 98  ? 39.309 -26.485 8.128   1.00 18.38 ?  98  PRO   B C    1 
ATOM   5835 O O    . PRO   B 1 98  ? 39.403 -27.223 7.148   1.00 17.87 ?  98  PRO   B O    1 
ATOM   5836 C CB   . PRO   B 1 98  ? 36.861 -25.923 8.396   1.00 18.95 ?  98  PRO   B CB   1 
ATOM   5837 C CG   . PRO   B 1 98  ? 36.270 -26.007 7.032   1.00 18.79 ?  98  PRO   B CG   1 
ATOM   5838 C CD   . PRO   B 1 98  ? 36.841 -24.838 6.284   1.00 18.14 ?  98  PRO   B CD   1 
ATOM   5839 H HA   . PRO   B 1 98  ? 38.497 -24.751 8.893   1.00 21.98 ?  98  PRO   B HA   1 
ATOM   5840 H HB2  . PRO   B 1 98  ? 36.915 -26.805 8.803   1.00 22.74 ?  98  PRO   B HB2  1 
ATOM   5841 H HB3  . PRO   B 1 98  ? 36.354 -25.317 8.953   1.00 22.74 ?  98  PRO   B HB3  1 
ATOM   5842 H HG2  . PRO   B 1 98  ? 36.532 -26.847 6.616   1.00 22.55 ?  98  PRO   B HG2  1 
ATOM   5843 H HG3  . PRO   B 1 98  ? 35.305 -25.945 7.093   1.00 22.55 ?  98  PRO   B HG3  1 
ATOM   5844 H HD2  . PRO   B 1 98  ? 36.924 -25.048 5.337   1.00 21.77 ?  98  PRO   B HD2  1 
ATOM   5845 H HD3  . PRO   B 1 98  ? 36.300 -24.045 6.424   1.00 21.77 ?  98  PRO   B HD3  1 
ATOM   5846 N N    . ASN   B 1 99  ? 40.093 -26.601 9.203   1.00 20.26 ?  99  ASN   B N    1 
ATOM   5847 C CA   . ASN   B 1 99  ? 41.083 -27.668 9.367   1.00 21.01 ?  99  ASN   B CA   1 
ATOM   5848 C C    . ASN   B 1 99  ? 40.482 -28.741 10.272  1.00 23.38 ?  99  ASN   B C    1 
ATOM   5849 O O    . ASN   B 1 99  ? 40.465 -28.598 11.499  1.00 24.66 ?  99  ASN   B O    1 
ATOM   5850 C CB   . ASN   B 1 99  ? 42.369 -27.104 9.962   1.00 21.17 ?  99  ASN   B CB   1 
ATOM   5851 C CG   . ASN   B 1 99  ? 43.510 -28.116 9.968   1.00 22.01 ?  99  ASN   B CG   1 
ATOM   5852 O OD1  . ASN   B 1 99  ? 43.305 -29.302 10.195  1.00 22.77 ?  99  ASN   B OD1  1 
ATOM   5853 N ND2  . ASN   B 1 99  ? 44.714 -27.646 9.696   1.00 22.03 ?  99  ASN   B ND2  1 
ATOM   5854 H H    . ASN   B 1 99  ? 40.067 -26.054 9.863   1.00 24.31 ?  99  ASN   B H    1 
ATOM   5855 H HA   . ASN   B 1 99  ? 41.283 -28.067 8.507   1.00 25.22 ?  99  ASN   B HA   1 
ATOM   5856 H HB2  . ASN   B 1 99  ? 42.643 -26.336 9.445   1.00 25.40 ?  99  ASN   B HB2  1 
ATOM   5857 H HB3  . ASN   B 1 99  ? 42.197 -26.844 10.883  1.00 25.40 ?  99  ASN   B HB3  1 
ATOM   5858 H HD21 . ASN   B 1 99  ? 45.386 -28.171 9.678   1.00 26.44 ?  99  ASN   B HD21 1 
ATOM   5859 H HD22 . ASN   B 1 99  ? 44.814 -26.803 9.539   1.00 26.44 ?  99  ASN   B HD22 1 
ATOM   5860 N N    . VAL   B 1 100 ? 39.990 -29.822 9.659   1.00 26.62 ?  100 VAL   B N    1 
ATOM   5861 C CA   . VAL   B 1 100 ? 39.379 -30.908 10.424  1.00 30.02 ?  100 VAL   B CA   1 
ATOM   5862 C C    . VAL   B 1 100 ? 40.397 -31.581 11.338  1.00 30.83 ?  100 VAL   B C    1 
ATOM   5863 O O    . VAL   B 1 100 ? 40.044 -32.070 12.418  1.00 31.98 ?  100 VAL   B O    1 
ATOM   5864 C CB   . VAL   B 1 100 ? 38.681 -31.904 9.475   1.00 32.43 ?  100 VAL   B CB   1 
ATOM   5865 C CG1  . VAL   B 1 100 ? 38.234 -33.147 10.230  1.00 33.53 ?  100 VAL   B CG1  1 
ATOM   5866 C CG2  . VAL   B 1 100 ? 37.486 -31.230 8.807   1.00 33.29 ?  100 VAL   B CG2  1 
ATOM   5867 H H    . VAL   B 1 100 ? 39.986 -29.941 8.803   1.00 31.94 ?  100 VAL   B H    1 
ATOM   5868 H HA   . VAL   B 1 100 ? 38.683 -30.527 10.985  1.00 36.03 ?  100 VAL   B HA   1 
ATOM   5869 H HB   . VAL   B 1 100 ? 39.301 -32.176 8.780   1.00 38.92 ?  100 VAL   B HB   1 
ATOM   5870 H HG11 . VAL   B 1 100 ? 37.608 -33.640 9.676   1.00 40.24 ?  100 VAL   B HG11 1 
ATOM   5871 H HG12 . VAL   B 1 100 ? 39.008 -33.695 10.423  1.00 40.24 ?  100 VAL   B HG12 1 
ATOM   5872 H HG13 . VAL   B 1 100 ? 37.801 -32.874 11.053  1.00 40.24 ?  100 VAL   B HG13 1 
ATOM   5873 H HG21 . VAL   B 1 100 ? 37.048 -31.870 8.224   1.00 39.95 ?  100 VAL   B HG21 1 
ATOM   5874 H HG22 . VAL   B 1 100 ? 36.868 -30.934 9.495   1.00 39.95 ?  100 VAL   B HG22 1 
ATOM   5875 H HG23 . VAL   B 1 100 ? 37.797 -30.471 8.292   1.00 39.95 ?  100 VAL   B HG23 1 
ATOM   5876 N N    A ASN   B 1 101 ? 41.668 -31.622 10.933  0.52 31.42 ?  101 ASN   B N    1 
ATOM   5877 N N    B ASN   B 1 101 ? 41.662 -31.644 10.915  0.48 31.34 ?  101 ASN   B N    1 
ATOM   5878 C CA   A ASN   B 1 101 ? 42.702 -32.144 11.821  0.52 32.59 ?  101 ASN   B CA   1 
ATOM   5879 C CA   B ASN   B 1 101 ? 42.713 -32.179 11.775  0.48 32.35 ?  101 ASN   B CA   1 
ATOM   5880 C C    A ASN   B 1 101 ? 42.911 -31.272 13.053  0.52 35.51 ?  101 ASN   B C    1 
ATOM   5881 C C    B ASN   B 1 101 ? 42.933 -31.334 13.022  0.48 34.96 ?  101 ASN   B C    1 
ATOM   5882 O O    A ASN   B 1 101 ? 43.598 -31.704 13.987  0.52 36.37 ?  101 ASN   B O    1 
ATOM   5883 O O    B ASN   B 1 101 ? 43.607 -31.794 13.952  0.48 35.69 ?  101 ASN   B O    1 
ATOM   5884 C CB   A ASN   B 1 101 ? 44.022 -32.324 11.066  0.52 32.05 ?  101 ASN   B CB   1 
ATOM   5885 C CB   B ASN   B 1 101 ? 44.022 -32.328 10.992  0.48 31.78 ?  101 ASN   B CB   1 
ATOM   5886 C CG   A ASN   B 1 101 ? 43.973 -33.473 10.073  0.52 31.43 ?  101 ASN   B CG   1 
ATOM   5887 C CG   B ASN   B 1 101 ? 43.996 -33.504 10.030  0.48 31.09 ?  101 ASN   B CG   1 
ATOM   5888 O OD1  A ASN   B 1 101 ? 43.262 -34.455 10.280  0.52 31.52 ?  101 ASN   B OD1  1 
ATOM   5889 O OD1  B ASN   B 1 101 ? 43.293 -34.488 10.256  0.48 31.15 ?  101 ASN   B OD1  1 
ATOM   5890 N ND2  A ASN   B 1 101 ? 44.727 -33.352 8.988   0.52 30.68 ?  101 ASN   B ND2  1 
ATOM   5891 N ND2  B ASN   B 1 101 ? 44.765 -33.407 8.952   0.48 30.36 ?  101 ASN   B ND2  1 
ATOM   5892 H H    A ASN   B 1 101 ? 41.945 -31.371 10.160  0.52 37.70 ?  101 ASN   B H    1 
ATOM   5893 H H    B ASN   B 1 101 ? 41.926 -31.399 10.138  0.48 37.61 ?  101 ASN   B H    1 
ATOM   5894 H HA   A ASN   B 1 101 ? 42.421 -33.018 12.128  0.52 39.11 ?  101 ASN   B HA   1 
ATOM   5895 H HA   B ASN   B 1 101 ? 42.446 -33.061 12.068  0.48 38.82 ?  101 ASN   B HA   1 
ATOM   5896 H HB2  A ASN   B 1 101 ? 44.224 -31.512 10.578  0.52 38.46 ?  101 ASN   B HB2  1 
ATOM   5897 H HB2  B ASN   B 1 101 ? 44.181 -31.523 10.475  0.48 38.13 ?  101 ASN   B HB2  1 
ATOM   5898 H HB3  A ASN   B 1 101 ? 44.727 -32.512 11.706  0.52 38.46 ?  101 ASN   B HB3  1 
ATOM   5899 H HB3  B ASN   B 1 101 ? 44.749 -32.470 11.617  0.48 38.13 ?  101 ASN   B HB3  1 
ATOM   5900 H HD21 A ASN   B 1 101 ? 44.730 -33.975 8.396   0.52 36.82 ?  101 ASN   B HD21 1 
ATOM   5901 H HD21 B ASN   B 1 101 ? 44.783 -34.047 8.378   0.48 36.43 ?  101 ASN   B HD21 1 
ATOM   5902 H HD22 A ASN   B 1 101 ? 45.213 -32.651 8.878   0.52 36.82 ?  101 ASN   B HD22 1 
ATOM   5903 H HD22 B ASN   B 1 101 ? 45.245 -32.705 8.828   0.48 36.43 ?  101 ASN   B HD22 1 
ATOM   5904 N N    A LYS   B 1 102 ? 42.348 -30.063 13.073  0.52 37.97 ?  102 LYS   B N    1 
ATOM   5905 N N    B LYS   B 1 102 ? 42.394 -30.115 13.059  0.48 37.30 ?  102 LYS   B N    1 
ATOM   5906 C CA   A LYS   B 1 102 ? 42.283 -29.227 14.264  0.52 40.29 ?  102 LYS   B CA   1 
ATOM   5907 C CA   B LYS   B 1 102 ? 42.325 -29.310 14.270  0.48 39.58 ?  102 LYS   B CA   1 
ATOM   5908 C C    A LYS   B 1 102 ? 40.894 -29.220 14.891  0.52 40.19 ?  102 LYS   B C    1 
ATOM   5909 C C    B LYS   B 1 102 ? 40.924 -29.299 14.871  0.48 39.64 ?  102 LYS   B C    1 
ATOM   5910 O O    A LYS   B 1 102 ? 40.635 -28.411 15.788  0.52 40.04 ?  102 LYS   B O    1 
ATOM   5911 O O    B LYS   B 1 102 ? 40.657 -28.513 15.784  0.48 39.56 ?  102 LYS   B O    1 
ATOM   5912 C CB   A LYS   B 1 102 ? 42.686 -27.789 13.930  0.52 42.62 ?  102 LYS   B CB   1 
ATOM   5913 C CB   B LYS   B 1 102 ? 42.768 -27.874 13.982  0.48 41.79 ?  102 LYS   B CB   1 
ATOM   5914 C CG   A LYS   B 1 102 ? 44.138 -27.596 13.534  0.52 44.64 ?  102 LYS   B CG   1 
ATOM   5915 C CG   B LYS   B 1 102 ? 44.225 -27.720 13.580  0.48 43.79 ?  102 LYS   B CG   1 
ATOM   5916 C CD   A LYS   B 1 102 ? 44.381 -26.143 13.150  0.52 46.57 ?  102 LYS   B CD   1 
ATOM   5917 C CD   B LYS   B 1 102 ? 44.516 -26.281 13.182  0.48 45.80 ?  102 LYS   B CD   1 
ATOM   5918 C CE   A LYS   B 1 102 ? 45.840 -25.864 12.838  0.52 47.89 ?  102 LYS   B CE   1 
ATOM   5919 C CE   B LYS   B 1 102 ? 45.989 -26.055 12.892  0.48 47.22 ?  102 LYS   B CE   1 
ATOM   5920 N NZ   A LYS   B 1 102 ? 46.044 -24.439 12.441  0.52 48.72 ?  102 LYS   B NZ   1 
ATOM   5921 N NZ   B LYS   B 1 102 ? 46.248 -24.646 12.473  0.48 48.19 ?  102 LYS   B NZ   1 
ATOM   5922 H H    A LYS   B 1 102 ? 41.993 -29.694 12.384  0.52 45.56 ?  102 LYS   B H    1 
ATOM   5923 H H    B LYS   B 1 102 ? 42.051 -29.725 12.374  0.48 44.76 ?  102 LYS   B H    1 
ATOM   5924 H HA   A LYS   B 1 102 ? 42.907 -29.565 14.922  0.52 48.35 ?  102 LYS   B HA   1 
ATOM   5925 H HA   B LYS   B 1 102 ? 42.934 -29.679 14.928  0.48 47.50 ?  102 LYS   B HA   1 
ATOM   5926 H HB2  A LYS   B 1 102 ? 42.139 -27.480 13.192  0.52 51.14 ?  102 LYS   B HB2  1 
ATOM   5927 H HB2  B LYS   B 1 102 ? 42.226 -27.523 13.260  0.48 50.15 ?  102 LYS   B HB2  1 
ATOM   5928 H HB3  A LYS   B 1 102 ? 42.522 -27.234 14.710  0.52 51.14 ?  102 LYS   B HB3  1 
ATOM   5929 H HB3  B LYS   B 1 102 ? 42.628 -27.342 14.782  0.48 50.15 ?  102 LYS   B HB3  1 
ATOM   5930 H HG2  A LYS   B 1 102 ? 44.712 -27.818 14.284  0.52 53.57 ?  102 LYS   B HG2  1 
ATOM   5931 H HG2  B LYS   B 1 102 ? 44.795 -27.952 14.330  0.48 52.54 ?  102 LYS   B HG2  1 
ATOM   5932 H HG3  A LYS   B 1 102 ? 44.343 -28.156 12.769  0.52 53.57 ?  102 LYS   B HG3  1 
ATOM   5933 H HG3  B LYS   B 1 102 ? 44.413 -28.293 12.820  0.48 52.54 ?  102 LYS   B HG3  1 
ATOM   5934 H HD2  A LYS   B 1 102 ? 43.858 -25.932 12.360  0.52 55.88 ?  102 LYS   B HD2  1 
ATOM   5935 H HD2  B LYS   B 1 102 ? 44.013 -26.065 12.381  0.48 54.96 ?  102 LYS   B HD2  1 
ATOM   5936 H HD3  A LYS   B 1 102 ? 44.115 -25.571 13.887  0.52 55.88 ?  102 LYS   B HD3  1 
ATOM   5937 H HD3  B LYS   B 1 102 ? 44.256 -25.692 13.908  0.48 54.96 ?  102 LYS   B HD3  1 
ATOM   5938 H HE2  A LYS   B 1 102 ? 46.377 -26.040 13.627  0.52 57.46 ?  102 LYS   B HE2  1 
ATOM   5939 H HE2  B LYS   B 1 102 ? 46.505 -26.234 13.694  0.48 56.67 ?  102 LYS   B HE2  1 
ATOM   5940 H HE3  A LYS   B 1 102 ? 46.126 -26.429 12.103  0.52 57.46 ?  102 LYS   B HE3  1 
ATOM   5941 H HE3  B LYS   B 1 102 ? 46.268 -26.643 12.173  0.48 56.67 ?  102 LYS   B HE3  1 
ATOM   5942 H HZ1  A LYS   B 1 102 ? 46.903 -24.293 12.262  0.52 58.46 ?  102 LYS   B HZ1  1 
ATOM   5943 H HZ1  B LYS   B 1 102 ? 47.115 -24.533 12.308  0.48 57.83 ?  102 LYS   B HZ1  1 
ATOM   5944 H HZ2  A LYS   B 1 102 ? 45.562 -24.254 11.716  0.52 58.46 ?  102 LYS   B HZ2  1 
ATOM   5945 H HZ2  B LYS   B 1 102 ? 45.786 -24.458 11.736  0.48 57.83 ?  102 LYS   B HZ2  1 
ATOM   5946 H HZ3  A LYS   B 1 102 ? 45.790 -23.900 13.102  0.52 58.46 ?  102 LYS   B HZ3  1 
ATOM   5947 H HZ3  B LYS   B 1 102 ? 46.001 -24.086 13.120  0.48 57.83 ?  102 LYS   B HZ3  1 
ATOM   5948 N N    A GLY   B 1 103 ? 39.991 -30.082 14.430  0.52 40.54 ?  103 GLY   B N    1 
ATOM   5949 N N    B GLY   B 1 103 ? 40.020 -30.138 14.365  0.48 40.05 ?  103 GLY   B N    1 
ATOM   5950 C CA   A GLY   B 1 103 ? 38.658 -30.154 14.990  0.52 41.05 ?  103 GLY   B CA   1 
ATOM   5951 C CA   B GLY   B 1 103 ? 38.682 -30.255 14.907  0.48 40.64 ?  103 GLY   B CA   1 
ATOM   5952 C C    A GLY   B 1 103 ? 37.703 -29.083 14.519  0.52 41.09 ?  103 GLY   B C    1 
ATOM   5953 C C    B GLY   B 1 103 ? 37.704 -29.190 14.461  0.48 40.71 ?  103 GLY   B C    1 
ATOM   5954 O O    A GLY   B 1 103 ? 36.586 -29.002 15.041  0.52 41.41 ?  103 GLY   B O    1 
ATOM   5955 O O    B GLY   B 1 103 ? 36.566 -29.179 14.949  0.48 41.02 ?  103 GLY   B O    1 
ATOM   5956 H H    A GLY   B 1 103 ? 40.128 -30.632 13.786  0.52 48.65 ?  103 GLY   B H    1 
ATOM   5957 H H    B GLY   B 1 103 ? 40.164 -30.653 13.693  0.48 48.06 ?  103 GLY   B H    1 
ATOM   5958 H HA2  A GLY   B 1 103 ? 38.272 -31.018 14.778  0.52 49.26 ?  103 GLY   B HA2  1 
ATOM   5959 H HA2  B GLY   B 1 103 ? 38.320 -31.120 14.659  0.48 48.76 ?  103 GLY   B HA2  1 
ATOM   5960 H HA3  A GLY   B 1 103 ? 38.716 -30.081 15.955  0.52 49.26 ?  103 GLY   B HA3  1 
ATOM   5961 H HA3  B GLY   B 1 103 ? 38.732 -30.219 15.874  0.48 48.76 ?  103 GLY   B HA3  1 
ATOM   5962 N N    A GLU   B 1 104 ? 38.101 -28.258 13.554  0.52 40.33 ?  104 GLU   B N    1 
ATOM   5963 N N    B GLU   B 1 104 ? 38.098 -28.302 13.553  0.48 40.00 ?  104 GLU   B N    1 
ATOM   5964 C CA   A GLU   B 1 104 ? 37.242 -27.177 13.096  0.52 39.61 ?  104 GLU   B CA   1 
ATOM   5965 C CA   B GLU   B 1 104 ? 37.227 -27.215 13.136  0.48 39.31 ?  104 GLU   B CA   1 
ATOM   5966 C C    A GLU   B 1 104 ? 36.062 -27.722 12.295  0.52 39.99 ?  104 GLU   B C    1 
ATOM   5967 C C    B GLU   B 1 104 ? 36.044 -27.747 12.328  0.48 39.82 ?  104 GLU   B C    1 
ATOM   5968 O O    A GLU   B 1 104 ? 36.120 -28.808 11.712  0.52 40.34 ?  104 GLU   B O    1 
ATOM   5969 O O    B GLU   B 1 104 ? 36.079 -28.846 11.766  0.48 40.16 ?  104 GLU   B O    1 
ATOM   5970 C CB   A GLU   B 1 104 ? 38.053 -26.175 12.271  0.52 38.78 ?  104 GLU   B CB   1 
ATOM   5971 C CB   B GLU   B 1 104 ? 38.022 -26.181 12.338  0.48 38.40 ?  104 GLU   B CB   1 
ATOM   5972 C CG   A GLU   B 1 104 ? 39.116 -25.462 13.099  0.52 37.92 ?  104 GLU   B CG   1 
ATOM   5973 C CG   B GLU   B 1 104 ? 39.119 -25.528 13.166  0.48 37.45 ?  104 GLU   B CG   1 
ATOM   5974 C CD   A GLU   B 1 104 ? 40.050 -24.599 12.277  0.52 37.23 ?  104 GLU   B CD   1 
ATOM   5975 C CD   B GLU   B 1 104 ? 40.075 -24.686 12.346  0.48 36.64 ?  104 GLU   B CD   1 
ATOM   5976 O OE1  A GLU   B 1 104 ? 40.041 -24.707 11.033  0.52 36.05 ?  104 GLU   B OE1  1 
ATOM   5977 O OE1  B GLU   B 1 104 ? 40.021 -24.743 11.100  0.48 35.65 ?  104 GLU   B OE1  1 
ATOM   5978 O OE2  A GLU   B 1 104 ? 40.804 -23.811 12.886  0.52 36.97 -1 104 GLU   B OE2  1 
ATOM   5979 O OE2  B GLU   B 1 104 ? 40.888 -23.962 12.959  0.48 36.18 -1 104 GLU   B OE2  1 
ATOM   5980 H H    A GLU   B 1 104 ? 38.861 -28.299 13.155  0.52 48.39 ?  104 GLU   B H    1 
ATOM   5981 H H    B GLU   B 1 104 ? 38.867 -28.303 13.171  0.48 48.00 ?  104 GLU   B H    1 
ATOM   5982 H HA   A GLU   B 1 104 ? 36.886 -26.710 13.865  0.52 47.53 ?  104 GLU   B HA   1 
ATOM   5983 H HA   B GLU   B 1 104 ? 36.873 -26.777 13.922  0.48 47.17 ?  104 GLU   B HA   1 
ATOM   5984 H HB2  A GLU   B 1 104 ? 38.499 -26.643 11.550  0.52 46.54 ?  104 GLU   B HB2  1 
ATOM   5985 H HB2  B GLU   B 1 104 ? 38.436 -26.617 11.577  0.48 46.08 ?  104 GLU   B HB2  1 
ATOM   5986 H HB3  A GLU   B 1 104 ? 37.453 -25.502 11.910  0.52 46.54 ?  104 GLU   B HB3  1 
ATOM   5987 H HB3  B GLU   B 1 104 ? 37.419 -25.484 12.034  0.48 46.08 ?  104 GLU   B HB3  1 
ATOM   5988 H HG2  A GLU   B 1 104 ? 38.677 -24.893 13.752  0.52 45.51 ?  104 GLU   B HG2  1 
ATOM   5989 H HG2  B GLU   B 1 104 ? 38.710 -24.948 13.827  0.48 44.94 ?  104 GLU   B HG2  1 
ATOM   5990 H HG3  A GLU   B 1 104 ? 39.660 -26.123 13.550  0.52 45.51 ?  104 GLU   B HG3  1 
ATOM   5991 H HG3  B GLU   B 1 104 ? 39.634 -26.220 13.608  0.48 44.94 ?  104 GLU   B HG3  1 
ATOM   5992 N N    . ASP   B 1 105 ? 34.980 -26.946 12.281  1.00 39.06 ?  105 ASP   B N    1 
ATOM   5993 C CA   . ASP   B 1 105 ? 33.720 -27.385 11.695  1.00 39.40 ?  105 ASP   B CA   1 
ATOM   5994 C C    . ASP   B 1 105 ? 33.809 -27.399 10.175  1.00 36.61 ?  105 ASP   B C    1 
ATOM   5995 O O    . ASP   B 1 105 ? 34.016 -26.355 9.548   1.00 35.76 ?  105 ASP   B O    1 
ATOM   5996 C CB   . ASP   B 1 105 ? 32.595 -26.455 12.149  1.00 42.51 ?  105 ASP   B CB   1 
ATOM   5997 C CG   . ASP   B 1 105 ? 31.224 -26.939 11.714  1.00 46.10 ?  105 ASP   B CG   1 
ATOM   5998 O OD1  . ASP   B 1 105 ? 31.139 -28.017 11.091  1.00 46.56 ?  105 ASP   B OD1  1 
ATOM   5999 O OD2  . ASP   B 1 105 ? 30.225 -26.244 12.005  1.00 47.83 -1 105 ASP   B OD2  1 
ATOM   6000 H H    A ASP   B 1 105 ? 34.950 -26.152 12.609  0.52 46.87 ?  105 ASP   B H    1 
ATOM   6001 H H    B ASP   B 1 105 ? 34.964 -26.141 12.580  0.48 46.87 ?  105 ASP   B H    1 
ATOM   6002 H HA   . ASP   B 1 105 ? 33.514 -28.281 11.997  1.00 47.28 ?  105 ASP   B HA   1 
ATOM   6003 H HB2  . ASP   B 1 105 ? 32.592 -26.408 13.116  1.00 51.01 ?  105 ASP   B HB2  1 
ATOM   6004 H HB3  . ASP   B 1 105 ? 32.742 -25.570 11.774  1.00 51.01 ?  105 ASP   B HB3  1 
ATOM   6005 N N    . ILE   B 1 106 ? 33.609 -28.583 9.586   1.00 34.82 ?  106 ILE   B N    1 
ATOM   6006 C CA   . ILE   B 1 106 ? 33.608 -28.738 8.137   1.00 33.12 ?  106 ILE   B CA   1 
ATOM   6007 C C    . ILE   B 1 106 ? 32.511 -27.910 7.473   1.00 30.38 ?  106 ILE   B C    1 
ATOM   6008 O O    . ILE   B 1 106 ? 32.600 -27.615 6.276   1.00 29.74 ?  106 ILE   B O    1 
ATOM   6009 C CB   . ILE   B 1 106 ? 33.509 -30.244 7.784   1.00 33.51 ?  106 ILE   B CB   1 
ATOM   6010 C CG1  . ILE   B 1 106 ? 33.804 -30.485 6.303   1.00 33.54 ?  106 ILE   B CG1  1 
ATOM   6011 C CG2  . ILE   B 1 106 ? 32.133 -30.792 8.139   1.00 35.02 ?  106 ILE   B CG2  1 
ATOM   6012 C CD1  . ILE   B 1 106 ? 35.156 -29.986 5.872   1.00 33.13 ?  106 ILE   B CD1  1 
ATOM   6013 H H    . ILE   B 1 106 ? 33.468 -29.314 10.011  1.00 41.78 ?  106 ILE   B H    1 
ATOM   6014 H HA   . ILE   B 1 106 ? 34.452 -28.409 7.801   1.00 39.74 ?  106 ILE   B HA   1 
ATOM   6015 H HB   . ILE   B 1 106 ? 34.169 -30.722 8.307   1.00 40.22 ?  106 ILE   B HB   1 
ATOM   6016 H HG12 . ILE   B 1 106 ? 33.776 -31.441 6.129   1.00 40.25 ?  106 ILE   B HG12 1 
ATOM   6017 H HG13 . ILE   B 1 106 ? 33.135 -30.034 5.767   1.00 40.25 ?  106 ILE   B HG13 1 
ATOM   6018 H HG21 . ILE   B 1 106 ? 32.153 -31.759 8.068   1.00 42.03 ?  106 ILE   B HG21 1 
ATOM   6019 H HG22 . ILE   B 1 106 ? 31.916 -30.530 9.046   1.00 42.03 ?  106 ILE   B HG22 1 
ATOM   6020 H HG23 . ILE   B 1 106 ? 31.478 -30.429 7.522   1.00 42.03 ?  106 ILE   B HG23 1 
ATOM   6021 H HD11 . ILE   B 1 106 ? 35.396 -30.406 5.032   1.00 39.76 ?  106 ILE   B HD11 1 
ATOM   6022 H HD12 . ILE   B 1 106 ? 35.116 -29.022 5.757   1.00 39.76 ?  106 ILE   B HD12 1 
ATOM   6023 H HD13 . ILE   B 1 106 ? 35.810 -30.211 6.553   1.00 39.76 ?  106 ILE   B HD13 1 
ATOM   6024 N N    A GLN   B 1 107 ? 31.475 -27.521 8.222   0.52 30.86 ?  107 GLN   B N    1 
ATOM   6025 N N    B GLN   B 1 107 ? 31.477 -27.522 8.223   0.48 30.81 ?  107 GLN   B N    1 
ATOM   6026 C CA   A GLN   B 1 107 ? 30.394 -26.737 7.635   0.52 31.03 ?  107 GLN   B CA   1 
ATOM   6027 C CA   B GLN   B 1 107 ? 30.388 -26.737 7.650   0.48 30.93 ?  107 GLN   B CA   1 
ATOM   6028 C C    A GLN   B 1 107 ? 30.875 -25.385 7.126   0.52 28.59 ?  107 GLN   B C    1 
ATOM   6029 C C    B GLN   B 1 107 ? 30.854 -25.372 7.158   0.48 28.53 ?  107 GLN   B C    1 
ATOM   6030 O O    A GLN   B 1 107 ? 30.252 -24.821 6.222   0.52 28.80 ?  107 GLN   B O    1 
ATOM   6031 O O    B GLN   B 1 107 ? 30.194 -24.783 6.296   0.48 28.81 ?  107 GLN   B O    1 
ATOM   6032 C CB   A GLN   B 1 107 ? 29.267 -26.543 8.653   0.52 34.84 ?  107 GLN   B CB   1 
ATOM   6033 C CB   B GLN   B 1 107 ? 29.268 -26.576 8.682   0.48 34.56 ?  107 GLN   B CB   1 
ATOM   6034 C CG   A GLN   B 1 107 ? 27.951 -26.046 8.059   0.52 38.22 ?  107 GLN   B CG   1 
ATOM   6035 C CG   B GLN   B 1 107 ? 27.925 -26.144 8.103   0.48 37.80 ?  107 GLN   B CG   1 
ATOM   6036 C CD   A GLN   B 1 107 ? 27.883 -24.532 7.941   0.52 41.03 ?  107 GLN   B CD   1 
ATOM   6037 C CD   B GLN   B 1 107 ? 27.780 -24.636 8.006   0.48 40.49 ?  107 GLN   B CD   1 
ATOM   6038 O OE1  A GLN   B 1 107 ? 28.704 -23.814 8.512   0.52 41.87 ?  107 GLN   B OE1  1 
ATOM   6039 O OE1  B GLN   B 1 107 ? 28.548 -23.885 8.608   0.48 41.26 ?  107 GLN   B OE1  1 
ATOM   6040 N NE2  A GLN   B 1 107 ? 26.893 -24.040 7.198   0.52 41.84 ?  107 GLN   B NE2  1 
ATOM   6041 N NE2  B GLN   B 1 107 ? 26.785 -24.186 7.249   0.48 41.31 ?  107 GLN   B NE2  1 
ATOM   6042 H H    A GLN   B 1 107 ? 31.385 -27.686 9.058   0.52 37.04 ?  107 GLN   B H    1 
ATOM   6043 H H    B GLN   B 1 107 ? 31.386 -27.697 9.056   0.48 36.97 ?  107 GLN   B H    1 
ATOM   6044 H HA   A GLN   B 1 107 ? 30.030 -27.226 6.879   0.52 37.24 ?  107 GLN   B HA   1 
ATOM   6045 H HA   B GLN   B 1 107 ? 30.024 -27.217 6.890   0.48 37.12 ?  107 GLN   B HA   1 
ATOM   6046 H HB2  A GLN   B 1 107 ? 29.092 -27.393 9.080   0.52 41.81 ?  107 GLN   B HB2  1 
ATOM   6047 H HB2  B GLN   B 1 107 ? 29.134 -27.427 9.122   0.48 41.47 ?  107 GLN   B HB2  1 
ATOM   6048 H HB3  A GLN   B 1 107 ? 29.556 -25.897 9.316   0.52 41.81 ?  107 GLN   B HB3  1 
ATOM   6049 H HB3  B GLN   B 1 107 ? 29.539 -25.910 9.332   0.48 41.47 ?  107 GLN   B HB3  1 
ATOM   6050 H HG2  A GLN   B 1 107 ? 27.843 -26.418 7.171   0.52 45.86 ?  107 GLN   B HG2  1 
ATOM   6051 H HG2  B GLN   B 1 107 ? 27.831 -26.510 7.210   0.48 45.36 ?  107 GLN   B HG2  1 
ATOM   6052 H HG3  A GLN   B 1 107 ? 27.220 -26.338 8.629   0.52 45.86 ?  107 GLN   B HG3  1 
ATOM   6053 H HG3  B GLN   B 1 107 ? 27.214 -26.482 8.674   0.48 45.36 ?  107 GLN   B HG3  1 
ATOM   6054 H HE21 A GLN   B 1 107 ? 26.338 -24.573 6.812   0.52 50.21 ?  107 GLN   B HE21 1 
ATOM   6055 H HE21 B GLN   B 1 107 ? 26.268 -24.740 6.842   0.48 49.57 ?  107 GLN   B HE21 1 
ATOM   6056 H HE22 A GLN   B 1 107 ? 26.807 -23.189 7.103   0.52 50.21 ?  107 GLN   B HE22 1 
ATOM   6057 H HE22 B GLN   B 1 107 ? 26.658 -23.339 7.166   0.48 49.57 ?  107 GLN   B HE22 1 
ATOM   6058 N N    . LEU   B 1 108 ? 31.975 -24.859 7.674   1.00 26.15 ?  108 LEU   B N    1 
ATOM   6059 C CA   . LEU   B 1 108 ? 32.506 -23.562 7.244   1.00 22.27 ?  108 LEU   B CA   1 
ATOM   6060 C C    . LEU   B 1 108 ? 33.160 -23.597 5.869   1.00 18.48 ?  108 LEU   B C    1 
ATOM   6061 O O    . LEU   B 1 108 ? 33.599 -22.544 5.376   1.00 17.54 ?  108 LEU   B O    1 
ATOM   6062 C CB   . LEU   B 1 108 ? 33.501 -23.033 8.279   1.00 22.96 ?  108 LEU   B CB   1 
ATOM   6063 C CG   . LEU   B 1 108 ? 32.865 -22.490 9.557   1.00 24.65 ?  108 LEU   B CG   1 
ATOM   6064 C CD1  . LEU   B 1 108 ? 33.838 -22.551 10.712  1.00 25.86 ?  108 LEU   B CD1  1 
ATOM   6065 C CD2  . LEU   B 1 108 ? 32.393 -21.060 9.340   1.00 25.59 ?  108 LEU   B CD2  1 
ATOM   6066 H H    A LEU   B 1 108 ? 32.420 -25.230 8.307   0.52 31.38 ?  108 LEU   B H    1 
ATOM   6067 H H    B LEU   B 1 108 ? 32.440 -25.242 8.285   0.48 31.38 ?  108 LEU   B H    1 
ATOM   6068 H HA   . LEU   B 1 108 ? 31.770 -22.935 7.203   1.00 26.72 ?  108 LEU   B HA   1 
ATOM   6069 H HB2  . LEU   B 1 108 ? 34.096 -23.752 8.537   1.00 27.55 ?  108 LEU   B HB2  1 
ATOM   6070 H HB3  . LEU   B 1 108 ? 34.008 -22.312 7.880   1.00 27.55 ?  108 LEU   B HB3  1 
ATOM   6071 H HG   . LEU   B 1 108 ? 32.088 -23.028 9.788   1.00 29.58 ?  108 LEU   B HG   1 
ATOM   6072 H HD11 . LEU   B 1 108 ? 33.399 -22.228 11.517  1.00 31.03 ?  108 LEU   B HD11 1 
ATOM   6073 H HD12 . LEU   B 1 108 ? 34.121 -23.469 10.838  1.00 31.03 ?  108 LEU   B HD12 1 
ATOM   6074 H HD13 . LEU   B 1 108 ? 34.604 -21.992 10.509  1.00 31.03 ?  108 LEU   B HD13 1 
ATOM   6075 H HD21 . LEU   B 1 108 ? 31.981 -20.733 10.155  1.00 30.70 ?  108 LEU   B HD21 1 
ATOM   6076 H HD22 . LEU   B 1 108 ? 33.158 -20.508 9.112   1.00 30.70 ?  108 LEU   B HD22 1 
ATOM   6077 H HD23 . LEU   B 1 108 ? 31.748 -21.047 8.616   1.00 30.70 ?  108 LEU   B HD23 1 
ATOM   6078 N N    . LEU   B 1 109 ? 33.223 -24.769 5.238   1.00 17.02 ?  109 LEU   B N    1 
ATOM   6079 C CA   . LEU   B 1 109 ? 33.856 -24.886 3.931   1.00 16.00 ?  109 LEU   B CA   1 
ATOM   6080 C C    . LEU   B 1 109 ? 33.092 -24.109 2.862   1.00 14.73 ?  109 LEU   B C    1 
ATOM   6081 O O    . LEU   B 1 109 ? 33.706 -23.529 1.957   1.00 14.51 ?  109 LEU   B O    1 
ATOM   6082 C CB   . LEU   B 1 109 ? 33.985 -26.368 3.569   1.00 15.51 ?  109 LEU   B CB   1 
ATOM   6083 C CG   . LEU   B 1 109 ? 34.753 -26.716 2.295   1.00 15.06 ?  109 LEU   B CG   1 
ATOM   6084 C CD1  . LEU   B 1 109 ? 36.122 -26.047 2.275   1.00 15.20 ?  109 LEU   B CD1  1 
ATOM   6085 C CD2  . LEU   B 1 109 ? 34.889 -28.235 2.172   1.00 15.77 ?  109 LEU   B CD2  1 
ATOM   6086 H H    . LEU   B 1 109 ? 32.918 -25.510 5.547   1.00 20.42 ?  109 LEU   B H    1 
ATOM   6087 H HA   . LEU   B 1 109 ? 34.750 -24.509 3.982   1.00 19.20 ?  109 LEU   B HA   1 
ATOM   6088 H HB2  . LEU   B 1 109 ? 34.439 -26.817 4.299   1.00 18.61 ?  109 LEU   B HB2  1 
ATOM   6089 H HB3  . LEU   B 1 109 ? 33.095 -26.734 3.473   1.00 18.61 ?  109 LEU   B HB3  1 
ATOM   6090 H HG   . LEU   B 1 109 ? 34.249 -26.408 1.525   1.00 18.08 ?  109 LEU   B HG   1 
ATOM   6091 H HD11 . LEU   B 1 109 ? 36.640 -26.408 1.537   1.00 18.24 ?  109 LEU   B HD11 1 
ATOM   6092 H HD12 . LEU   B 1 109 ? 36.003 -25.094 2.161   1.00 18.24 ?  109 LEU   B HD12 1 
ATOM   6093 H HD13 . LEU   B 1 109 ? 36.574 -26.232 3.114   1.00 18.24 ?  109 LEU   B HD13 1 
ATOM   6094 H HD21 . LEU   B 1 109 ? 35.447 -28.442 1.400   1.00 18.93 ?  109 LEU   B HD21 1 
ATOM   6095 H HD22 . LEU   B 1 109 ? 35.306 -28.583 2.976   1.00 18.93 ?  109 LEU   B HD22 1 
ATOM   6096 H HD23 . LEU   B 1 109 ? 34.012 -28.631 2.056   1.00 18.93 ?  109 LEU   B HD23 1 
ATOM   6097 N N    . LYS   B 1 110 ? 31.756 -24.070 2.944   1.00 14.55 ?  110 LYS   B N    1 
ATOM   6098 C CA   . LYS   B 1 110 ? 31.000 -23.303 1.954   1.00 14.52 ?  110 LYS   B CA   1 
ATOM   6099 C C    . LYS   B 1 110 ? 31.338 -21.818 2.039   1.00 14.27 ?  110 LYS   B C    1 
ATOM   6100 O O    . LYS   B 1 110 ? 31.598 -21.171 1.018   1.00 14.83 ?  110 LYS   B O    1 
ATOM   6101 C CB   . LYS   B 1 110 ? 29.493 -23.549 2.107   1.00 15.16 ?  110 LYS   B CB   1 
ATOM   6102 C CG   . LYS   B 1 110 ? 28.693 -22.972 0.939   1.00 15.83 ?  110 LYS   B CG   1 
ATOM   6103 C CD   . LYS   B 1 110 ? 27.211 -23.386 0.971   1.00 15.78 ?  110 LYS   B CD   1 
ATOM   6104 C CE   . LYS   B 1 110 ? 26.449 -22.858 -0.245  1.00 17.33 ?  110 LYS   B CE   1 
ATOM   6105 N NZ   . LYS   B 1 110 ? 26.788 -23.568 -1.510  1.00 17.58 ?  110 LYS   B NZ   1 
ATOM   6106 H H    . LYS   B 1 110 ? 31.281 -24.457 3.549   1.00 17.46 ?  110 LYS   B H    1 
ATOM   6107 H HA   . LYS   B 1 110 ? 31.255 -23.610 1.072   1.00 17.42 ?  110 LYS   B HA   1 
ATOM   6108 H HB2  . LYS   B 1 110 ? 29.327 -24.503 2.145   1.00 18.19 ?  110 LYS   B HB2  1 
ATOM   6109 H HB3  . LYS   B 1 110 ? 29.180 -23.124 2.921   1.00 18.19 ?  110 LYS   B HB3  1 
ATOM   6110 H HG2  . LYS   B 1 110 ? 28.728 -22.008 0.972   1.00 19.00 ?  110 LYS   B HG2  1 
ATOM   6111 H HG3  . LYS   B 1 110 ? 29.071 -23.297 0.107   1.00 19.00 ?  110 LYS   B HG3  1 
ATOM   6112 H HD2  . LYS   B 1 110 ? 27.144 -24.360 0.970   1.00 18.94 ?  110 LYS   B HD2  1 
ATOM   6113 H HD3  . LYS   B 1 110 ? 26.789 -23.030 1.769   1.00 18.94 ?  110 LYS   B HD3  1 
ATOM   6114 H HE2  . LYS   B 1 110 ? 25.498 -22.967 -0.095  1.00 20.80 ?  110 LYS   B HE2  1 
ATOM   6115 H HE3  . LYS   B 1 110 ? 26.663 -21.923 -0.364  1.00 20.80 ?  110 LYS   B HE3  1 
ATOM   6116 H HZ1  . LYS   B 1 110 ? 26.327 -23.225 -2.186  1.00 21.10 ?  110 LYS   B HZ1  1 
ATOM   6117 H HZ2  . LYS   B 1 110 ? 27.661 -23.481 -1.682  1.00 21.10 ?  110 LYS   B HZ2  1 
ATOM   6118 H HZ3  . LYS   B 1 110 ? 26.597 -24.434 -1.436  1.00 21.10 ?  110 LYS   B HZ3  1 
ATOM   6119 N N    . SER   B 1 111 ? 31.364 -21.270 3.258   1.00 15.00 ?  111 SER   B N    1 
ATOM   6120 C CA   . SER   B 1 111 ? 31.756 -19.873 3.430   1.00 15.01 ?  111 SER   B CA   1 
ATOM   6121 C C    . SER   B 1 111 ? 33.135 -19.617 2.833   1.00 14.03 ?  111 SER   B C    1 
ATOM   6122 O O    . SER   B 1 111 ? 33.352 -18.596 2.172   1.00 13.87 ?  111 SER   B O    1 
ATOM   6123 C CB   . SER   B 1 111 ? 31.751 -19.504 4.911   1.00 16.32 ?  111 SER   B CB   1 
ATOM   6124 O OG   . SER   B 1 111 ? 30.443 -19.514 5.451   1.00 17.78 ?  111 SER   B OG   1 
ATOM   6125 H H    . SER   B 1 111 ? 31.172 -21.683 3.989   1.00 18.00 ?  111 SER   B H    1 
ATOM   6126 H HA   . SER   B 1 111 ? 31.119 -19.304 2.973   1.00 18.01 ?  111 SER   B HA   1 
ATOM   6127 H HB2  . SER   B 1 111 ? 32.296 -20.144 5.397   1.00 19.59 ?  111 SER   B HB2  1 
ATOM   6128 H HB3  . SER   B 1 111 ? 32.126 -18.614 5.014   1.00 19.59 ?  111 SER   B HB3  1 
ATOM   6129 H HG   . SER   B 1 111 ? 30.472 -19.306 6.272   1.00 21.33 ?  111 SER   B HG   1 
ATOM   6130 N N    . ALA   B 1 112 ? 34.077 -20.538 3.041   1.00 13.77 ?  112 ALA   B N    1 
ATOM   6131 C CA   . ALA   B 1 112 ? 35.421 -20.364 2.495   1.00 12.97 ?  112 ALA   B CA   1 
ATOM   6132 C C    . ALA   B 1 112 ? 35.394 -20.276 0.971   1.00 12.81 ?  112 ALA   B C    1 
ATOM   6133 O O    . ALA   B 1 112 ? 36.010 -19.383 0.373   1.00 13.51 ?  112 ALA   B O    1 
ATOM   6134 C CB   . ALA   B 1 112 ? 36.320 -21.503 2.974   1.00 13.83 ?  112 ALA   B CB   1 
ATOM   6135 H H    . ALA   B 1 112 ? 33.966 -21.262 3.497   1.00 16.53 ?  112 ALA   B H    1 
ATOM   6136 H HA   . ALA   B 1 112 ? 35.790 -19.535 2.837   1.00 15.56 ?  112 ALA   B HA   1 
ATOM   6137 H HB1  . ALA   B 1 112 ? 37.214 -21.374 2.615   1.00 16.60 ?  112 ALA   B HB1  1 
ATOM   6138 H HB2  . ALA   B 1 112 ? 36.358 -21.491 3.948   1.00 16.60 ?  112 ALA   B HB2  1 
ATOM   6139 H HB3  . ALA   B 1 112 ? 35.959 -22.347 2.671   1.00 16.60 ?  112 ALA   B HB3  1 
ATOM   6140 N N    . TYR   B 1 113 ? 34.668 -21.190 0.317   1.00 12.68 ?  113 TYR   B N    1 
ATOM   6141 C CA   . TYR   B 1 113 ? 34.586 -21.147 -1.138  1.00 12.22 ?  113 TYR   B CA   1 
ATOM   6142 C C    . TYR   B 1 113 ? 33.881 -19.891 -1.651  1.00 12.57 ?  113 TYR   B C    1 
ATOM   6143 O O    . TYR   B 1 113 ? 34.160 -19.445 -2.771  1.00 12.52 ?  113 TYR   B O    1 
ATOM   6144 C CB   . TYR   B 1 113 ? 33.917 -22.410 -1.690  1.00 12.61 ?  113 TYR   B CB   1 
ATOM   6145 C CG   . TYR   B 1 113 ? 34.880 -23.562 -1.936  1.00 13.37 ?  113 TYR   B CG   1 
ATOM   6146 C CD1  . TYR   B 1 113 ? 35.863 -23.472 -2.910  1.00 13.64 ?  113 TYR   B CD1  1 
ATOM   6147 C CD2  . TYR   B 1 113 ? 34.788 -24.742 -1.215  1.00 13.72 ?  113 TYR   B CD2  1 
ATOM   6148 C CE1  . TYR   B 1 113 ? 36.748 -24.495 -3.143  1.00 13.89 ?  113 TYR   B CE1  1 
ATOM   6149 C CE2  . TYR   B 1 113 ? 35.668 -25.804 -1.451  1.00 13.28 ?  113 TYR   B CE2  1 
ATOM   6150 C CZ   . TYR   B 1 113 ? 36.632 -25.673 -2.429  1.00 13.52 ?  113 TYR   B CZ   1 
ATOM   6151 O OH   . TYR   B 1 113 ? 37.529 -26.686 -2.695  1.00 14.83 ?  113 TYR   B OH   1 
ATOM   6152 H H    . TYR   B 1 113 ? 34.209 -21.819 0.689   1.00 15.22 ?  113 TYR   B H    1 
ATOM   6153 H HA   . TYR   B 1 113 ? 35.485 -21.121 -1.482  1.00 14.66 ?  113 TYR   B HA   1 
ATOM   6154 H HB2  . TYR   B 1 113 ? 33.248 -22.715 -1.054  1.00 15.14 ?  113 TYR   B HB2  1 
ATOM   6155 H HB3  . TYR   B 1 113 ? 33.487 -22.192 -2.534  1.00 15.14 ?  113 TYR   B HB3  1 
ATOM   6156 H HD1  . TYR   B 1 113 ? 35.942 -22.677 -3.402  1.00 16.37 ?  113 TYR   B HD1  1 
ATOM   6157 H HD2  . TYR   B 1 113 ? 34.127 -24.831 -0.565  1.00 16.47 ?  113 TYR   B HD2  1 
ATOM   6158 H HE1  . TYR   B 1 113 ? 37.396 -24.407 -3.803  1.00 16.67 ?  113 TYR   B HE1  1 
ATOM   6159 H HE2  . TYR   B 1 113 ? 35.593 -26.595 -0.962  1.00 15.94 ?  113 TYR   B HE2  1 
ATOM   6160 H HH   . TYR   B 1 113 ? 37.356 -27.350 -2.208  1.00 17.80 ?  113 TYR   B HH   1 
ATOM   6161 N N    . GLU   B 1 114 ? 32.956 -19.314 -0.871  1.00 12.75 ?  114 GLU   B N    1 
ATOM   6162 C CA   . GLU   B 1 114 ? 32.277 -18.099 -1.326  1.00 12.87 ?  114 GLU   B CA   1 
ATOM   6163 C C    . GLU   B 1 114 ? 33.261 -16.972 -1.628  1.00 12.55 ?  114 GLU   B C    1 
ATOM   6164 O O    . GLU   B 1 114 ? 32.981 -16.118 -2.472  1.00 12.84 ?  114 GLU   B O    1 
ATOM   6165 C CB   . GLU   B 1 114 ? 31.219 -17.665 -0.310  1.00 13.50 ?  114 GLU   B CB   1 
ATOM   6166 C CG   . GLU   B 1 114 ? 29.971 -18.569 -0.398  1.00 13.58 ?  114 GLU   B CG   1 
ATOM   6167 C CD   . GLU   B 1 114 ? 28.951 -18.393 0.727   1.00 13.84 ?  114 GLU   B CD   1 
ATOM   6168 O OE1  . GLU   B 1 114 ? 29.249 -17.779 1.773   1.00 14.00 ?  114 GLU   B OE1  1 
ATOM   6169 O OE2  . GLU   B 1 114 ? 27.822 -18.922 0.571   1.00 14.93 -1 114 GLU   B OE2  1 
ATOM   6170 H H    . GLU   B 1 114 ? 32.704 -19.605 -0.098  1.00 15.30 ?  114 GLU   B H    1 
ATOM   6171 H HA   . GLU   B 1 114 ? 31.811 -18.302 -2.149  1.00 15.45 ?  114 GLU   B HA   1 
ATOM   6172 H HB2  . GLU   B 1 114 ? 31.581 -17.735 0.588   1.00 16.20 ?  114 GLU   B HB2  1 
ATOM   6173 H HB3  . GLU   B 1 114 ? 30.948 -16.752 -0.494  1.00 16.20 ?  114 GLU   B HB3  1 
ATOM   6174 H HG2  . GLU   B 1 114 ? 29.508 -18.372 -1.226  1.00 16.30 ?  114 GLU   B HG2  1 
ATOM   6175 H HG3  . GLU   B 1 114 ? 30.256 -19.490 -0.390  1.00 16.30 ?  114 GLU   B HG3  1 
ATOM   6176 N N    . ASN   B 1 115 ? 34.430 -16.969 -0.985  1.00 12.18 ?  115 ASN   B N    1 
ATOM   6177 C CA   . ASN   B 1 115 ? 35.420 -15.941 -1.285  1.00 11.57 ?  115 ASN   B CA   1 
ATOM   6178 C C    . ASN   B 1 115 ? 35.837 -15.961 -2.750  1.00 12.03 ?  115 ASN   B C    1 
ATOM   6179 O O    . ASN   B 1 115 ? 36.220 -14.923 -3.307  1.00 12.63 ?  115 ASN   B O    1 
ATOM   6180 C CB   . ASN   B 1 115 ? 36.655 -16.120 -0.391  1.00 12.49 ?  115 ASN   B CB   1 
ATOM   6181 C CG   . ASN   B 1 115 ? 36.372 -15.845 1.070   1.00 12.68 ?  115 ASN   B CG   1 
ATOM   6182 O OD1  . ASN   B 1 115 ? 36.365 -14.690 1.505   1.00 15.60 ?  115 ASN   B OD1  1 
ATOM   6183 N ND2  . ASN   B 1 115 ? 36.188 -16.905 1.856   1.00 13.60 ?  115 ASN   B ND2  1 
ATOM   6184 H H    . ASN   B 1 115 ? 34.665 -17.530 -0.372  1.00 14.62 ?  115 ASN   B H    1 
ATOM   6185 H HA   . ASN   B 1 115 ? 35.046 -15.068 -1.096  1.00 13.88 ?  115 ASN   B HA   1 
ATOM   6186 H HB2  . ASN   B 1 115 ? 36.976 -17.030 -0.467  1.00 14.99 ?  115 ASN   B HB2  1 
ATOM   6187 H HB3  . ASN   B 1 115 ? 37.346 -15.500 -0.674  1.00 14.99 ?  115 ASN   B HB3  1 
ATOM   6188 H HD21 . ASN   B 1 115 ? 36.041 -16.797 2.699   1.00 16.32 ?  115 ASN   B HD21 1 
ATOM   6189 H HD22 . ASN   B 1 115 ? 36.221 -17.698 1.527   1.00 16.32 ?  115 ASN   B HD22 1 
ATOM   6190 N N    . PHE   B 1 116 ? 35.828 -17.138 -3.379  1.00 11.58 ?  116 PHE   B N    1 
ATOM   6191 C CA   . PHE   B 1 116 ? 36.253 -17.239 -4.768  1.00 11.67 ?  116 PHE   B CA   1 
ATOM   6192 C C    . PHE   B 1 116 ? 35.353 -16.415 -5.684  1.00 11.41 ?  116 PHE   B C    1 
ATOM   6193 O O    . PHE   B 1 116 ? 35.785 -15.980 -6.757  1.00 12.47 ?  116 PHE   B O    1 
ATOM   6194 C CB   . PHE   B 1 116 ? 36.204 -18.692 -5.277  1.00 11.02 ?  116 PHE   B CB   1 
ATOM   6195 C CG   . PHE   B 1 116 ? 37.275 -19.648 -4.732  1.00 11.10 ?  116 PHE   B CG   1 
ATOM   6196 C CD1  . PHE   B 1 116 ? 37.921 -19.456 -3.522  1.00 12.10 ?  116 PHE   B CD1  1 
ATOM   6197 C CD2  . PHE   B 1 116 ? 37.578 -20.795 -5.466  1.00 11.80 ?  116 PHE   B CD2  1 
ATOM   6198 C CE1  . PHE   B 1 116 ? 38.844 -20.397 -3.061  1.00 12.59 ?  116 PHE   B CE1  1 
ATOM   6199 C CE2  . PHE   B 1 116 ? 38.519 -21.710 -5.022  1.00 12.18 ?  116 PHE   B CE2  1 
ATOM   6200 C CZ   . PHE   B 1 116 ? 39.140 -21.518 -3.825  1.00 12.06 ?  116 PHE   B CZ   1 
ATOM   6201 H H    . PHE   B 1 116 ? 35.567 -17.888 -3.027  1.00 13.89 ?  116 PHE   B H    1 
ATOM   6202 H HA   . PHE   B 1 116 ? 37.153 -16.922 -4.859  1.00 14.01 ?  116 PHE   B HA   1 
ATOM   6203 H HB2  . PHE   B 1 116 ? 35.331 -19.075 -5.050  1.00 13.22 ?  116 PHE   B HB2  1 
ATOM   6204 H HB3  . PHE   B 1 116 ? 36.292 -18.687 -6.246  1.00 13.22 ?  116 PHE   B HB3  1 
ATOM   6205 H HD1  . PHE   B 1 116 ? 37.710 -18.713 -3.001  1.00 14.52 ?  116 PHE   B HD1  1 
ATOM   6206 H HD2  . PHE   B 1 116 ? 37.149 -20.938 -6.279  1.00 14.16 ?  116 PHE   B HD2  1 
ATOM   6207 H HE1  . PHE   B 1 116 ? 39.285 -20.257 -2.252  1.00 15.10 ?  116 PHE   B HE1  1 
ATOM   6208 H HE2  . PHE   B 1 116 ? 38.708 -22.457 -5.534  1.00 14.62 ?  116 PHE   B HE2  1 
ATOM   6209 H HZ   . PHE   B 1 116 ? 39.776 -22.127 -3.527  1.00 14.48 ?  116 PHE   B HZ   1 
ATOM   6210 N N    . ASN   B 1 117 ? 34.082 -16.216 -5.303  1.00 12.12 ?  117 ASN   B N    1 
ATOM   6211 C CA   . ASN   B 1 117 ? 33.141 -15.511 -6.178  1.00 12.84 ?  117 ASN   B CA   1 
ATOM   6212 C C    . ASN   B 1 117 ? 33.451 -14.026 -6.328  1.00 12.92 ?  117 ASN   B C    1 
ATOM   6213 O O    . ASN   B 1 117 ? 32.865 -13.372 -7.195  1.00 14.06 ?  117 ASN   B O    1 
ATOM   6214 C CB   . ASN   B 1 117 ? 31.716 -15.730 -5.676  1.00 13.23 ?  117 ASN   B CB   1 
ATOM   6215 C CG   . ASN   B 1 117 ? 31.244 -17.138 -5.933  1.00 13.36 ?  117 ASN   B CG   1 
ATOM   6216 O OD1  . ASN   B 1 117 ? 31.602 -17.736 -6.950  1.00 14.41 ?  117 ASN   B OD1  1 
ATOM   6217 N ND2  . ASN   B 1 117 ? 30.501 -17.701 -4.998  1.00 13.10 ?  117 ASN   B ND2  1 
ATOM   6218 H H    . ASN   B 1 117 ? 33.745 -16.475 -4.550  1.00 14.54 ?  117 ASN   B H    1 
ATOM   6219 H HA   . ASN   B 1 117 ? 33.196 -15.911 -7.057  1.00 15.41 ?  117 ASN   B HA   1 
ATOM   6220 H HB2  . ASN   B 1 117 ? 31.682 -15.570 -4.715  1.00 15.88 ?  117 ASN   B HB2  1 
ATOM   6221 H HB3  . ASN   B 1 117 ? 31.117 -15.116 -6.132  1.00 15.88 ?  117 ASN   B HB3  1 
ATOM   6222 H HD21 . ASN   B 1 117 ? 30.205 -18.505 -5.105  1.00 15.72 ?  117 ASN   B HD21 1 
ATOM   6223 H HD22 . ASN   B 1 117 ? 30.272 -17.256 -4.296  1.00 15.72 ?  117 ASN   B HD22 1 
ATOM   6224 N N    . GLN   B 1 118 ? 34.376 -13.500 -5.544  1.00 12.61 ?  118 GLN   B N    1 
ATOM   6225 C CA   . GLN   B 1 118 ? 34.811 -12.116 -5.685  1.00 13.40 ?  118 GLN   B CA   1 
ATOM   6226 C C    . GLN   B 1 118 ? 35.886 -11.929 -6.753  1.00 13.89 ?  118 GLN   B C    1 
ATOM   6227 O O    . GLN   B 1 118 ? 36.366 -10.802 -6.927  1.00 15.28 ?  118 GLN   B O    1 
ATOM   6228 C CB   . GLN   B 1 118 ? 35.275 -11.585 -4.324  1.00 14.21 ?  118 GLN   B CB   1 
ATOM   6229 C CG   . GLN   B 1 118 ? 34.190 -11.637 -3.261  1.00 14.05 ?  118 GLN   B CG   1 
ATOM   6230 C CD   . GLN   B 1 118 ? 33.029 -10.709 -3.582  1.00 14.05 ?  118 GLN   B CD   1 
ATOM   6231 O OE1  . GLN   B 1 118 ? 33.237 -9.568  -4.016  1.00 15.15 ?  118 GLN   B OE1  1 
ATOM   6232 N NE2  . GLN   B 1 118 ? 31.807 -11.187 -3.384  1.00 14.74 ?  118 GLN   B NE2  1 
ATOM   6233 H H    . GLN   B 1 118 ? 34.788 -13.925 -4.920  1.00 15.13 ?  118 GLN   B H    1 
ATOM   6234 H HA   . GLN   B 1 118 ? 34.050 -11.584 -5.959  1.00 16.08 ?  118 GLN   B HA   1 
ATOM   6235 H HB2  . GLN   B 1 118 ? 36.025 -12.111 -4.015  1.00 17.05 ?  118 GLN   B HB2  1 
ATOM   6236 H HB3  . GLN   B 1 118 ? 35.541 -10.654 -4.421  1.00 17.05 ?  118 GLN   B HB3  1 
ATOM   6237 H HG2  . GLN   B 1 118 ? 33.848 -12.549 -3.202  1.00 16.87 ?  118 GLN   B HG2  1 
ATOM   6238 H HG3  . GLN   B 1 118 ? 34.567 -11.374 -2.406  1.00 16.87 ?  118 GLN   B HG3  1 
ATOM   6239 H HE21 . GLN   B 1 118 ? 31.704 -11.988 -3.077  1.00 17.68 ?  118 GLN   B HE21 1 
ATOM   6240 H HE22 . GLN   B 1 118 ? 31.127 -10.701 -3.554  1.00 17.68 ?  118 GLN   B HE22 1 
ATOM   6241 N N    . HIS   B 1 119 ? 36.248 -12.983 -7.491  1.00 12.75 ?  119 HIS   B N    1 
ATOM   6242 C CA   . HIS   B 1 119 ? 37.292 -12.932 -8.504  1.00 13.11 ?  119 HIS   B CA   1 
ATOM   6243 C C    . HIS   B 1 119 ? 36.811 -13.666 -9.742  1.00 13.00 ?  119 HIS   B C    1 
ATOM   6244 O O    . HIS   B 1 119 ? 36.300 -14.785 -9.639  1.00 14.12 ?  119 HIS   B O    1 
ATOM   6245 C CB   . HIS   B 1 119 ? 38.567 -13.576 -7.952  1.00 13.52 ?  119 HIS   B CB   1 
ATOM   6246 C CG   . HIS   B 1 119 ? 39.040 -12.895 -6.715  1.00 14.77 ?  119 HIS   B CG   1 
ATOM   6247 N ND1  . HIS   B 1 119 ? 39.853 -11.781 -6.746  1.00 15.95 ?  119 HIS   B ND1  1 
ATOM   6248 C CD2  . HIS   B 1 119 ? 38.733 -13.104 -5.413  1.00 15.55 ?  119 HIS   B CD2  1 
ATOM   6249 C CE1  . HIS   B 1 119 ? 40.050 -11.354 -5.512  1.00 16.92 ?  119 HIS   B CE1  1 
ATOM   6250 N NE2  . HIS   B 1 119 ? 39.372 -12.131 -4.687  1.00 17.34 ?  119 HIS   B NE2  1 
ATOM   6251 H H    . HIS   B 1 119 ? 35.881 -13.762 -7.425  1.00 15.30 ?  119 HIS   B H    1 
ATOM   6252 H HA   . HIS   B 1 119 ? 37.481 -12.006 -8.737  1.00 15.74 ?  119 HIS   B HA   1 
ATOM   6253 H HB2  . HIS   B 1 119 ? 38.384 -14.505 -7.740  1.00 16.23 ?  119 HIS   B HB2  1 
ATOM   6254 H HB3  . HIS   B 1 119 ? 39.268 -13.517 -8.620  1.00 16.23 ?  119 HIS   B HB3  1 
ATOM   6255 H HD2  . HIS   B 1 119 ? 38.185 -13.777 -5.077  1.00 18.66 ?  119 HIS   B HD2  1 
ATOM   6256 H HE1  . HIS   B 1 119 ? 40.585 -10.638 -5.262  1.00 20.30 ?  119 HIS   B HE1  1 
ATOM   6257 H HE2  . HIS   B 1 119 ? 39.367 -12.066 -3.827  1.00 20.81 ?  119 HIS   B HE2  1 
ATOM   6258 N N    . GLU   B 1 120 ? 36.978 -13.047 -10.913 1.00 13.65 ?  120 GLU   B N    1 
ATOM   6259 C CA   . GLU   B 1 120 ? 36.396 -13.613 -12.121 1.00 14.94 ?  120 GLU   B CA   1 
ATOM   6260 C C    . GLU   B 1 120 ? 37.067 -14.912 -12.541 1.00 13.65 ?  120 GLU   B C    1 
ATOM   6261 O O    . GLU   B 1 120 ? 36.403 -15.775 -13.123 1.00 14.57 ?  120 GLU   B O    1 
ATOM   6262 C CB   . GLU   B 1 120 ? 36.407 -12.594 -13.259 1.00 19.75 ?  120 GLU   B CB   1 
ATOM   6263 C CG   . GLU   B 1 120 ? 35.418 -11.459 -13.049 1.00 26.37 ?  120 GLU   B CG   1 
ATOM   6264 C CD   . GLU   B 1 120 ? 35.304 -10.529 -14.244 1.00 33.09 ?  120 GLU   B CD   1 
ATOM   6265 O OE1  . GLU   B 1 120 ? 36.311 -10.345 -14.965 1.00 35.43 ?  120 GLU   B OE1  1 
ATOM   6266 O OE2  . GLU   B 1 120 ? 34.202 -9.979  -14.457 1.00 36.12 -1 120 GLU   B OE2  1 
ATOM   6267 H H    . GLU   B 1 120 ? 37.423 -12.309 -11.034 1.00 16.39 ?  120 GLU   B H    1 
ATOM   6268 H HA   . GLU   B 1 120 ? 35.476 -13.827 -11.932 1.00 17.93 ?  120 GLU   B HA   1 
ATOM   6269 H HB2  . GLU   B 1 120 ? 37.291 -12.208 -13.333 1.00 23.70 ?  120 GLU   B HB2  1 
ATOM   6270 H HB3  . GLU   B 1 120 ? 36.170 -13.045 -14.085 1.00 23.70 ?  120 GLU   B HB3  1 
ATOM   6271 H HG2  . GLU   B 1 120 ? 34.536 -11.832 -12.887 1.00 31.64 ?  120 GLU   B HG2  1 
ATOM   6272 H HG3  . GLU   B 1 120 ? 35.699 -10.929 -12.290 1.00 31.64 ?  120 GLU   B HG3  1 
ATOM   6273 N N    . VAL   B 1 121 ? 38.360 -15.066 -12.269 1.00 13.38 ?  121 VAL   B N    1 
ATOM   6274 C CA   . VAL   B 1 121 ? 39.101 -16.276 -12.622 1.00 12.69 ?  121 VAL   B CA   1 
ATOM   6275 C C    . VAL   B 1 121 ? 40.217 -16.488 -11.606 1.00 12.91 ?  121 VAL   B C    1 
ATOM   6276 O O    . VAL   B 1 121 ? 40.898 -15.534 -11.213 1.00 13.67 ?  121 VAL   B O    1 
ATOM   6277 C CB   . VAL   B 1 121 ? 39.608 -16.221 -14.083 1.00 14.92 ?  121 VAL   B CB   1 
ATOM   6278 C CG1  . VAL   B 1 121 ? 40.470 -14.984 -14.330 1.00 16.53 ?  121 VAL   B CG1  1 
ATOM   6279 C CG2  . VAL   B 1 121 ? 40.354 -17.501 -14.448 1.00 16.65 ?  121 VAL   B CG2  1 
ATOM   6280 H H    . VAL   B 1 121 ? 38.854 -14.471 -11.886 1.00 16.06 ?  121 VAL   B H    1 
ATOM   6281 H HA   . VAL   B 1 121 ? 38.487 -17.029 -12.560 1.00 15.22 ?  121 VAL   B HA   1 
ATOM   6282 H HB   . VAL   B 1 121 ? 38.835 -16.163 -14.675 1.00 17.90 ?  121 VAL   B HB   1 
ATOM   6283 H HG11 . VAL   B 1 121 ? 40.784 -14.999 -15.248 1.00 19.83 ?  121 VAL   B HG11 1 
ATOM   6284 H HG12 . VAL   B 1 121 ? 39.931 -14.192 -14.178 1.00 19.83 ?  121 VAL   B HG12 1 
ATOM   6285 H HG13 . VAL   B 1 121 ? 41.221 -15.000 -13.720 1.00 19.83 ?  121 VAL   B HG13 1 
ATOM   6286 H HG21 . VAL   B 1 121 ? 40.551 -17.493 -15.400 1.00 19.98 ?  121 VAL   B HG21 1 
ATOM   6287 H HG22 . VAL   B 1 121 ? 41.179 -17.542 -13.942 1.00 19.98 ?  121 VAL   B HG22 1 
ATOM   6288 H HG23 . VAL   B 1 121 ? 39.796 -18.267 -14.237 1.00 19.98 ?  121 VAL   B HG23 1 
ATOM   6289 N N    . LEU   B 1 122 ? 40.397 -17.742 -11.177 1.00 12.51 ?  122 LEU   B N    1 
ATOM   6290 C CA   . LEU   B 1 122 ? 41.372 -18.092 -10.147 1.00 11.53 ?  122 LEU   B CA   1 
ATOM   6291 C C    . LEU   B 1 122 ? 42.027 -19.425 -10.465 1.00 11.55 ?  122 LEU   B C    1 
ATOM   6292 O O    . LEU   B 1 122 ? 41.365 -20.344 -10.967 1.00 13.07 ?  122 LEU   B O    1 
ATOM   6293 C CB   . LEU   B 1 122 ? 40.723 -18.314 -8.768  1.00 14.08 ?  122 LEU   B CB   1 
ATOM   6294 C CG   . LEU   B 1 122 ? 39.674 -17.312 -8.281  1.00 14.48 ?  122 LEU   B CG   1 
ATOM   6295 C CD1  . LEU   B 1 122 ? 38.293 -17.716 -8.753  1.00 14.87 ?  122 LEU   B CD1  1 
ATOM   6296 C CD2  . LEU   B 1 122 ? 39.708 -17.188 -6.771  1.00 13.93 ?  122 LEU   B CD2  1 
ATOM   6297 H H    . LEU   B 1 122 ? 39.967 -18.427 -11.478 1.00 15.01 ?  122 LEU   B H    1 
ATOM   6298 H HA   . LEU   B 1 122 ? 42.050 -17.403 -10.067 1.00 13.83 ?  122 LEU   B HA   1 
ATOM   6299 H HB2  . LEU   B 1 122 ? 40.287 -19.177 -8.778  1.00 16.89 ?  122 LEU   B HB2  1 
ATOM   6300 H HB3  . LEU   B 1 122 ? 41.421 -18.315 -8.101  1.00 16.89 ?  122 LEU   B HB3  1 
ATOM   6301 H HG   . LEU   B 1 122 ? 39.866 -16.436 -8.656  1.00 17.38 ?  122 LEU   B HG   1 
ATOM   6302 H HD11 . LEU   B 1 122 ? 37.642 -17.075 -8.427  1.00 17.85 ?  122 LEU   B HD11 1 
ATOM   6303 H HD12 . LEU   B 1 122 ? 38.282 -17.728 -9.726  1.00 17.85 ?  122 LEU   B HD12 1 
ATOM   6304 H HD13 . LEU   B 1 122 ? 38.088 -18.600 -8.412  1.00 17.85 ?  122 LEU   B HD13 1 
ATOM   6305 H HD21 . LEU   B 1 122 ? 39.013 -16.568 -6.486  1.00 16.72 ?  122 LEU   B HD21 1 
ATOM   6306 H HD22 . LEU   B 1 122 ? 39.553 -18.058 -6.378  1.00 16.72 ?  122 LEU   B HD22 1 
ATOM   6307 H HD23 . LEU   B 1 122 ? 40.576 -16.849 -6.503  1.00 16.72 ?  122 LEU   B HD23 1 
ATOM   6308 N N    . LEU   B 1 123 ? 43.311 -19.541 -10.107 1.00 10.70 ?  123 LEU   B N    1 
ATOM   6309 C CA   . LEU   B 1 123 ? 44.005 -20.822 -9.988  1.00 11.80 ?  123 LEU   B CA   1 
ATOM   6310 C C    . LEU   B 1 123 ? 43.979 -21.207 -8.515  1.00 10.91 ?  123 LEU   B C    1 
ATOM   6311 O O    . LEU   B 1 123 ? 44.333 -20.386 -7.666  1.00 11.30 ?  123 LEU   B O    1 
ATOM   6312 C CB   . LEU   B 1 123 ? 45.463 -20.656 -10.439 1.00 12.28 ?  123 LEU   B CB   1 
ATOM   6313 C CG   . LEU   B 1 123 ? 46.409 -21.837 -10.213 1.00 12.30 ?  123 LEU   B CG   1 
ATOM   6314 C CD1  . LEU   B 1 123 ? 45.972 -23.084 -10.982 1.00 12.95 ?  123 LEU   B CD1  1 
ATOM   6315 C CD2  . LEU   B 1 123 ? 47.825 -21.446 -10.601 1.00 13.07 ?  123 LEU   B CD2  1 
ATOM   6316 H H    . LEU   B 1 123 ? 43.814 -18.864 -9.894  1.00 12.84 ?  123 LEU   B H    1 
ATOM   6317 H HA   . LEU   B 1 123 ? 43.566 -21.498 -10.510 1.00 14.16 ?  123 LEU   B HA   1 
ATOM   6318 H HB2  . LEU   B 1 123 ? 45.457 -20.471 -11.390 1.00 14.74 ?  123 LEU   B HB2  1 
ATOM   6319 H HB3  . LEU   B 1 123 ? 45.841 -19.893 -9.969  1.00 14.74 ?  123 LEU   B HB3  1 
ATOM   6320 H HG   . LEU   B 1 123 ? 46.419 -22.058 -9.269  1.00 14.77 ?  123 LEU   B HG   1 
ATOM   6321 H HD11 . LEU   B 1 123 ? 46.607 -23.796 -10.814 1.00 15.54 ?  123 LEU   B HD11 1 
ATOM   6322 H HD12 . LEU   B 1 123 ? 45.089 -23.348 -10.675 1.00 15.54 ?  123 LEU   B HD12 1 
ATOM   6323 H HD13 . LEU   B 1 123 ? 45.945 -22.877 -11.929 1.00 15.54 ?  123 LEU   B HD13 1 
ATOM   6324 H HD21 . LEU   B 1 123 ? 48.412 -22.202 -10.458 1.00 15.68 ?  123 LEU   B HD21 1 
ATOM   6325 H HD22 . LEU   B 1 123 ? 47.833 -21.194 -11.541 1.00 15.68 ?  123 LEU   B HD22 1 
ATOM   6326 H HD23 . LEU   B 1 123 ? 48.106 -20.695 -10.057 1.00 15.68 ?  123 LEU   B HD23 1 
ATOM   6327 N N    . ALA   B 1 124 ? 43.544 -22.437 -8.203  1.00 10.93 ?  124 ALA   B N    1 
ATOM   6328 C CA   . ALA   B 1 124 ? 43.287 -22.770 -6.807  1.00 10.92 ?  124 ALA   B CA   1 
ATOM   6329 C C    . ALA   B 1 124 ? 43.567 -24.227 -6.473  1.00 9.73  ?  124 ALA   B C    1 
ATOM   6330 O O    . ALA   B 1 124 ? 43.419 -25.102 -7.336  1.00 11.61 ?  124 ALA   B O    1 
ATOM   6331 C CB   . ALA   B 1 124 ? 41.830 -22.461 -6.427  1.00 12.05 ?  124 ALA   B CB   1 
ATOM   6332 H H    . ALA   B 1 124 ? 43.389 -23.076 -8.769  1.00 13.12 ?  124 ALA   B H    1 
ATOM   6333 H HA   . ALA   B 1 124 ? 43.851 -22.222 -6.259  1.00 13.11 ?  124 ALA   B HA   1 
ATOM   6334 H HB1  . ALA   B 1 124 ? 41.680 -22.692 -5.499  1.00 14.47 ?  124 ALA   B HB1  1 
ATOM   6335 H HB2  . ALA   B 1 124 ? 41.663 -21.512 -6.563  1.00 14.47 ?  124 ALA   B HB2  1 
ATOM   6336 H HB3  . ALA   B 1 124 ? 41.230 -22.978 -6.996  1.00 14.47 ?  124 ALA   B HB3  1 
ATOM   6337 N N    . PRO   B 1 125 ? 43.868 -24.517 -5.207  1.00 10.98 ?  125 PRO   B N    1 
ATOM   6338 C CA   . PRO   B 1 125 ? 43.797 -25.887 -4.683  1.00 11.98 ?  125 PRO   B CA   1 
ATOM   6339 C C    . PRO   B 1 125 ? 42.388 -26.150 -4.141  1.00 12.50 ?  125 PRO   B C    1 
ATOM   6340 O O    . PRO   B 1 125 ? 41.596 -25.234 -3.933  1.00 12.90 ?  125 PRO   B O    1 
ATOM   6341 C CB   . PRO   B 1 125 ? 44.779 -25.825 -3.508  1.00 13.20 ?  125 PRO   B CB   1 
ATOM   6342 C CG   . PRO   B 1 125 ? 44.536 -24.419 -2.938  1.00 12.94 ?  125 PRO   B CG   1 
ATOM   6343 C CD   . PRO   B 1 125 ? 44.182 -23.549 -4.140  1.00 11.21 ?  125 PRO   B CD   1 
ATOM   6344 H HA   . PRO   B 1 125 ? 44.074 -26.558 -5.334  1.00 14.38 ?  125 PRO   B HA   1 
ATOM   6345 H HB2  . PRO   B 1 125 ? 44.563 -26.505 -2.851  1.00 15.83 ?  125 PRO   B HB2  1 
ATOM   6346 H HB3  . PRO   B 1 125 ? 45.693 -25.917 -3.820  1.00 15.83 ?  125 PRO   B HB3  1 
ATOM   6347 H HG2  . PRO   B 1 125 ? 43.799 -24.439 -2.305  1.00 15.53 ?  125 PRO   B HG2  1 
ATOM   6348 H HG3  . PRO   B 1 125 ? 45.343 -24.090 -2.505  1.00 15.53 ?  125 PRO   B HG3  1 
ATOM   6349 H HD2  . PRO   B 1 125 ? 43.403 -23.001 -3.952  1.00 13.45 ?  125 PRO   B HD2  1 
ATOM   6350 H HD3  . PRO   B 1 125 ? 44.943 -22.998 -4.397  1.00 13.45 ?  125 PRO   B HD3  1 
ATOM   6351 N N    . LEU   B 1 126 ? 42.114 -27.424 -3.839  1.00 13.09 ?  126 LEU   B N    1 
ATOM   6352 C CA   . LEU   B 1 126 ? 40.897 -27.789 -3.117  1.00 13.88 ?  126 LEU   B CA   1 
ATOM   6353 C C    . LEU   B 1 126 ? 41.008 -27.388 -1.651  1.00 13.98 ?  126 LEU   B C    1 
ATOM   6354 O O    . LEU   B 1 126 ? 41.889 -27.859 -0.927  1.00 15.76 ?  126 LEU   B O    1 
ATOM   6355 C CB   . LEU   B 1 126 ? 40.648 -29.288 -3.223  1.00 15.38 ?  126 LEU   B CB   1 
ATOM   6356 C CG   . LEU   B 1 126 ? 40.121 -29.793 -4.567  1.00 16.34 ?  126 LEU   B CG   1 
ATOM   6357 C CD1  . LEU   B 1 126 ? 40.154 -31.308 -4.620  1.00 18.41 ?  126 LEU   B CD1  1 
ATOM   6358 C CD2  . LEU   B 1 126 ? 38.706 -29.300 -4.839  1.00 16.33 ?  126 LEU   B CD2  1 
ATOM   6359 H H    . LEU   B 1 126 ? 42.629 -28.094 -4.034  1.00 15.71 ?  126 LEU   B H    1 
ATOM   6360 H HA   . LEU   B 1 126 ? 40.149 -27.319 -3.506  1.00 16.66 ?  126 LEU   B HA   1 
ATOM   6361 H HB2  . LEU   B 1 126 ? 41.477 -29.753 -3.046  1.00 18.45 ?  126 LEU   B HB2  1 
ATOM   6362 H HB3  . LEU   B 1 126 ? 39.990 -29.532 -2.550  1.00 18.45 ?  126 LEU   B HB3  1 
ATOM   6363 H HG   . LEU   B 1 126 ? 40.696 -29.446 -5.274  1.00 19.61 ?  126 LEU   B HG   1 
ATOM   6364 H HD11 . LEU   B 1 126 ? 39.819 -31.599 -5.481  1.00 22.09 ?  126 LEU   B HD11 1 
ATOM   6365 H HD12 . LEU   B 1 126 ? 41.067 -31.606 -4.498  1.00 22.09 ?  126 LEU   B HD12 1 
ATOM   6366 H HD13 . LEU   B 1 126 ? 39.592 -31.656 -3.909  1.00 22.09 ?  126 LEU   B HD13 1 
ATOM   6367 H HD21 . LEU   B 1 126 ? 38.384 -29.710 -5.658  1.00 19.59 ?  126 LEU   B HD21 1 
ATOM   6368 H HD22 . LEU   B 1 126 ? 38.138 -29.554 -4.096  1.00 19.59 ?  126 LEU   B HD22 1 
ATOM   6369 H HD23 . LEU   B 1 126 ? 38.713 -28.334 -4.936  1.00 19.59 ?  126 LEU   B HD23 1 
ATOM   6370 N N    . LEU   B 1 127 ? 40.081 -26.558 -1.188  1.00 13.67 ?  127 LEU   B N    1 
ATOM   6371 C CA   . LEU   B 1 127 ? 40.145 -26.067 0.176   1.00 14.14 ?  127 LEU   B CA   1 
ATOM   6372 C C    . LEU   B 1 127 ? 39.863 -27.185 1.174   1.00 13.68 ?  127 LEU   B C    1 
ATOM   6373 O O    . LEU   B 1 127 ? 39.032 -28.072 0.948   1.00 14.18 ?  127 LEU   B O    1 
ATOM   6374 C CB   . LEU   B 1 127 ? 39.125 -24.949 0.391   1.00 14.46 ?  127 LEU   B CB   1 
ATOM   6375 C CG   . LEU   B 1 127 ? 39.313 -23.680 -0.442  1.00 14.43 ?  127 LEU   B CG   1 
ATOM   6376 C CD1  . LEU   B 1 127 ? 38.178 -22.708 -0.146  1.00 15.26 ?  127 LEU   B CD1  1 
ATOM   6377 C CD2  . LEU   B 1 127 ? 40.685 -23.048 -0.198  1.00 15.54 ?  127 LEU   B CD2  1 
ATOM   6378 H H    . LEU   B 1 127 ? 39.417 -26.258 -1.647  1.00 16.41 ?  127 LEU   B H    1 
ATOM   6379 H HA   . LEU   B 1 127 ? 41.035 -25.708 0.351   1.00 16.96 ?  127 LEU   B HA   1 
ATOM   6380 H HB2  . LEU   B 1 127 ? 38.245 -25.304 0.180   1.00 17.35 ?  127 LEU   B HB2  1 
ATOM   6381 H HB3  . LEU   B 1 127 ? 39.151 -24.691 1.325   1.00 17.35 ?  127 LEU   B HB3  1 
ATOM   6382 H HG   . LEU   B 1 127 ? 39.256 -23.909 -1.378  1.00 17.32 ?  127 LEU   B HG   1 
ATOM   6383 H HD11 . LEU   B 1 127 ? 38.310 -21.896 -0.669  1.00 18.31 ?  127 LEU   B HD11 1 
ATOM   6384 H HD12 . LEU   B 1 127 ? 37.333 -23.116 -0.382  1.00 18.31 ?  127 LEU   B HD12 1 
ATOM   6385 H HD13 . LEU   B 1 127 ? 38.185 -22.485 0.802   1.00 18.31 ?  127 LEU   B HD13 1 
ATOM   6386 H HD21 . LEU   B 1 127 ? 40.723 -22.187 -0.643  1.00 18.65 ?  127 LEU   B HD21 1 
ATOM   6387 H HD22 . LEU   B 1 127 ? 40.815 -22.929 0.758   1.00 18.65 ?  127 LEU   B HD22 1 
ATOM   6388 H HD23 . LEU   B 1 127 ? 41.370 -23.635 -0.553  1.00 18.65 ?  127 LEU   B HD23 1 
ATOM   6389 N N    . SER   B 1 128 ? 40.532 -27.094 2.314   1.00 13.90 ?  128 SER   B N    1 
ATOM   6390 C CA   . SER   B 1 128 ? 40.408 -28.007 3.440   1.00 14.67 ?  128 SER   B CA   1 
ATOM   6391 C C    . SER   B 1 128 ? 40.908 -29.419 3.135   1.00 15.98 ?  128 SER   B C    1 
ATOM   6392 O O    . SER   B 1 128 ? 40.801 -30.290 3.997   1.00 18.37 ?  128 SER   B O    1 
ATOM   6393 C CB   . SER   B 1 128 ? 38.994 -28.014 4.047   1.00 14.94 ?  128 SER   B CB   1 
ATOM   6394 O OG   . SER   B 1 128 ? 38.699 -26.738 4.609   1.00 15.61 ?  128 SER   B OG   1 
ATOM   6395 H H    . SER   B 1 128 ? 41.095 -26.462 2.465   1.00 16.68 ?  128 SER   B H    1 
ATOM   6396 H HA   . SER   B 1 128 ? 40.988 -27.666 4.129   1.00 17.60 ?  128 SER   B HA   1 
ATOM   6397 H HB2  . SER   B 1 128 ? 38.344 -28.223 3.358   1.00 17.93 ?  128 SER   B HB2  1 
ATOM   6398 H HB3  . SER   B 1 128 ? 38.957 -28.693 4.749   1.00 17.93 ?  128 SER   B HB3  1 
ATOM   6399 H HG   . SER   B 1 128 ? 39.256 -26.559 5.210   1.00 18.73 ?  128 SER   B HG   1 
ATOM   6400 N N    . ALA   B 1 129 ? 41.496 -29.657 1.956   1.00 17.12 ?  129 ALA   B N    1 
ATOM   6401 C CA   . ALA   B 1 129 ? 42.043 -30.959 1.602   1.00 18.99 ?  129 ALA   B CA   1 
ATOM   6402 C C    . ALA   B 1 129 ? 43.438 -31.141 2.192   1.00 18.31 ?  129 ALA   B C    1 
ATOM   6403 O O    . ALA   B 1 129 ? 43.996 -30.249 2.842   1.00 17.55 ?  129 ALA   B O    1 
ATOM   6404 C CB   . ALA   B 1 129 ? 42.098 -31.119 0.083   1.00 21.51 ?  129 ALA   B CB   1 
ATOM   6405 H H    . ALA   B 1 129 ? 41.584 -29.068 1.328   1.00 20.54 ?  129 ALA   B H    1 
ATOM   6406 H HA   . ALA   B 1 129 ? 41.469 -31.654 1.958   1.00 22.79 ?  129 ALA   B HA   1 
ATOM   6407 H HB1  . ALA   B 1 129 ? 42.450 -32.000 -0.133  1.00 25.81 ?  129 ALA   B HB1  1 
ATOM   6408 H HB2  . ALA   B 1 129 ? 41.204 -31.026 -0.281  1.00 25.81 ?  129 ALA   B HB2  1 
ATOM   6409 H HB3  . ALA   B 1 129 ? 42.679 -30.435 -0.290  1.00 25.81 ?  129 ALA   B HB3  1 
ATOM   6410 N N    . GLY   B 1 130 ? 44.009 -32.315 1.942   1.00 18.72 ?  130 GLY   B N    1 
ATOM   6411 C CA   . GLY   B 1 130 ? 45.400 -32.539 2.288   1.00 18.94 ?  130 GLY   B CA   1 
ATOM   6412 C C    . GLY   B 1 130 ? 45.622 -32.454 3.781   1.00 18.57 ?  130 GLY   B C    1 
ATOM   6413 O O    . GLY   B 1 130 ? 44.920 -33.098 4.575   1.00 19.96 ?  130 GLY   B O    1 
ATOM   6414 H H    . GLY   B 1 130 ? 43.621 -32.984 1.568   1.00 22.46 ?  130 GLY   B H    1 
ATOM   6415 H HA2  . GLY   B 1 130 ? 45.677 -33.419 1.982   1.00 22.73 ?  130 GLY   B HA2  1 
ATOM   6416 H HA3  . GLY   B 1 130 ? 45.961 -31.875 1.854   1.00 22.73 ?  130 GLY   B HA3  1 
ATOM   6417 N N    A ILE   B 1 131 ? 46.612 -31.647 4.177   0.52 18.97 ?  131 ILE   B N    1 
ATOM   6418 N N    B ILE   B 1 131 ? 46.610 -31.647 4.182   0.48 18.99 ?  131 ILE   B N    1 
ATOM   6419 C CA   A ILE   B 1 131 ? 46.980 -31.520 5.578   0.52 20.01 ?  131 ILE   B CA   1 
ATOM   6420 C CA   B ILE   B 1 131 ? 46.972 -31.531 5.587   0.48 19.98 ?  131 ILE   B CA   1 
ATOM   6421 C C    A ILE   B 1 131 ? 45.869 -30.917 6.422   0.52 18.67 ?  131 ILE   B C    1 
ATOM   6422 C C    B ILE   B 1 131 ? 45.856 -30.934 6.426   0.48 18.69 ?  131 ILE   B C    1 
ATOM   6423 O O    A ILE   B 1 131 ? 45.960 -30.945 7.650   0.52 20.27 ?  131 ILE   B O    1 
ATOM   6424 O O    B ILE   B 1 131 ? 45.928 -30.987 7.655   0.48 20.20 ?  131 ILE   B O    1 
ATOM   6425 C CB   A ILE   B 1 131 ? 48.291 -30.716 5.753   0.52 21.81 ?  131 ILE   B CB   1 
ATOM   6426 C CB   B ILE   B 1 131 ? 48.291 -30.741 5.781   0.48 21.66 ?  131 ILE   B CB   1 
ATOM   6427 C CG1  A ILE   B 1 131 ? 48.086 -29.247 5.368   0.52 22.98 ?  131 ILE   B CG1  1 
ATOM   6428 C CG1  B ILE   B 1 131 ? 48.086 -29.250 5.487   0.48 22.65 ?  131 ILE   B CG1  1 
ATOM   6429 C CG2  A ILE   B 1 131 ? 49.420 -31.336 4.929   0.52 22.60 ?  131 ILE   B CG2  1 
ATOM   6430 C CG2  B ILE   B 1 131 ? 49.400 -31.324 4.905   0.48 22.50 ?  131 ILE   B CG2  1 
ATOM   6431 C CD1  A ILE   B 1 131 ? 49.303 -28.371 5.611   0.52 24.29 ?  131 ILE   B CD1  1 
ATOM   6432 C CD1  B ILE   B 1 131 ? 49.271 -28.377 5.864   0.48 23.74 ?  131 ILE   B CD1  1 
ATOM   6433 H H    A ILE   B 1 131 ? 47.086 -31.161 3.649   0.52 22.76 ?  131 ILE   B H    1 
ATOM   6434 H H    B ILE   B 1 131 ? 47.081 -31.154 3.659   0.48 22.79 ?  131 ILE   B H    1 
ATOM   6435 H HA   A ILE   B 1 131 ? 47.146 -32.407 5.928   0.52 24.01 ?  131 ILE   B HA   1 
ATOM   6436 H HA   B ILE   B 1 131 ? 47.128 -32.419 5.937   0.48 23.97 ?  131 ILE   B HA   1 
ATOM   6437 H HB   A ILE   B 1 131 ? 48.546 -30.752 6.689   0.52 26.17 ?  131 ILE   B HB   1 
ATOM   6438 H HB   B ILE   B 1 131 ? 48.567 -30.830 6.707   0.48 26.00 ?  131 ILE   B HB   1 
ATOM   6439 H HG12 A ILE   B 1 131 ? 47.869 -29.202 4.425   0.52 27.58 ?  131 ILE   B HG12 1 
ATOM   6440 H HG12 B ILE   B 1 131 ? 47.923 -29.141 4.539   0.48 27.19 ?  131 ILE   B HG12 1 
ATOM   6441 H HG13 A ILE   B 1 131 ? 47.357 -28.878 5.891   0.52 27.58 ?  131 ILE   B HG13 1 
ATOM   6442 H HG13 B ILE   B 1 131 ? 47.324 -28.923 5.990   0.48 27.19 ?  131 ILE   B HG13 1 
ATOM   6443 H HG21 A ILE   B 1 131 ? 50.259 -30.922 5.182   0.52 27.12 ?  131 ILE   B HG21 1 
ATOM   6444 H HG21 B ILE   B 1 131 ? 50.244 -30.915 5.150   0.48 27.00 ?  131 ILE   B HG21 1 
ATOM   6445 H HG22 A ILE   B 1 131 ? 49.451 -32.287 5.105   0.52 27.12 ?  131 ILE   B HG22 1 
ATOM   6446 H HG22 B ILE   B 1 131 ? 49.441 -32.282 5.047   0.48 27.00 ?  131 ILE   B HG22 1 
ATOM   6447 H HG23 A ILE   B 1 131 ? 49.242 -31.178 3.988   0.52 27.12 ?  131 ILE   B HG23 1 
ATOM   6448 H HG23 B ILE   B 1 131 ? 49.198 -31.136 3.975   0.48 27.00 ?  131 ILE   B HG23 1 
ATOM   6449 H HD11 A ILE   B 1 131 ? 49.058 -27.445 5.456   0.52 29.15 ?  131 ILE   B HD11 1 
ATOM   6450 H HD11 B ILE   B 1 131 ? 49.036 -27.448 5.713   0.48 28.48 ?  131 ILE   B HD11 1 
ATOM   6451 H HD12 A ILE   B 1 131 ? 49.597 -28.487 6.528   0.52 29.15 ?  131 ILE   B HD12 1 
ATOM   6452 H HD12 B ILE   B 1 131 ? 49.482 -28.517 6.800   0.48 28.48 ?  131 ILE   B HD12 1 
ATOM   6453 H HD13 A ILE   B 1 131 ? 50.009 -28.633 5.001   0.52 29.15 ?  131 ILE   B HD13 1 
ATOM   6454 H HD13 B ILE   B 1 131 ? 50.030 -28.620 5.313   0.48 28.48 ?  131 ILE   B HD13 1 
ATOM   6455 N N    . PHE   B 1 132 ? 44.826 -30.365 5.795   1.00 17.55 ?  132 PHE   B N    1 
ATOM   6456 C CA   . PHE   B 1 132 ? 43.677 -29.844 6.530   1.00 18.17 ?  132 PHE   B CA   1 
ATOM   6457 C C    . PHE   B 1 132 ? 42.645 -30.922 6.868   1.00 20.03 ?  132 PHE   B C    1 
ATOM   6458 O O    . PHE   B 1 132 ? 41.755 -30.667 7.685   1.00 21.53 ?  132 PHE   B O    1 
ATOM   6459 C CB   . PHE   B 1 132 ? 42.996 -28.722 5.733   1.00 17.02 ?  132 PHE   B CB   1 
ATOM   6460 C CG   . PHE   B 1 132 ? 43.684 -27.372 5.832   1.00 16.60 ?  132 PHE   B CG   1 
ATOM   6461 C CD1  . PHE   B 1 132 ? 44.981 -27.183 5.369   1.00 18.40 ?  132 PHE   B CD1  1 
ATOM   6462 C CD2  . PHE   B 1 132 ? 42.993 -26.280 6.348   1.00 16.29 ?  132 PHE   B CD2  1 
ATOM   6463 C CE1  . PHE   B 1 132 ? 45.594 -25.935 5.458   1.00 18.64 ?  132 PHE   B CE1  1 
ATOM   6464 C CE2  . PHE   B 1 132 ? 43.595 -25.025 6.428   1.00 17.51 ?  132 PHE   B CE2  1 
ATOM   6465 C CZ   . PHE   B 1 132 ? 44.895 -24.860 5.985   1.00 17.74 ?  132 PHE   B CZ   1 
ATOM   6466 H H    A PHE   B 1 132 ? 44.763 -30.284 4.940   0.52 21.06 ?  132 PHE   B H    1 
ATOM   6467 H H    B PHE   B 1 132 ? 44.766 -30.282 4.941   0.48 21.06 ?  132 PHE   B H    1 
ATOM   6468 H HA   . PHE   B 1 132 ? 43.994 -29.460 7.361   1.00 21.81 ?  132 PHE   B HA   1 
ATOM   6469 H HB2  . PHE   B 1 132 ? 42.984 -28.973 4.798   1.00 20.42 ?  132 PHE   B HB2  1 
ATOM   6470 H HB3  . PHE   B 1 132 ? 42.089 -28.619 6.060   1.00 20.42 ?  132 PHE   B HB3  1 
ATOM   6471 H HD1  . PHE   B 1 132 ? 45.450 -27.911 5.024   1.00 22.08 ?  132 PHE   B HD1  1 
ATOM   6472 H HD2  . PHE   B 1 132 ? 42.118 -26.390 6.653   1.00 19.55 ?  132 PHE   B HD2  1 
ATOM   6473 H HE1  . PHE   B 1 132 ? 46.465 -25.825 5.159   1.00 22.36 ?  132 PHE   B HE1  1 
ATOM   6474 H HE2  . PHE   B 1 132 ? 43.128 -24.303 6.789   1.00 21.01 ?  132 PHE   B HE2  1 
ATOM   6475 H HZ   . PHE   B 1 132 ? 45.302 -24.022 6.044   1.00 21.29 ?  132 PHE   B HZ   1 
ATOM   6476 N N    . GLY   B 1 133 ? 42.718 -32.105 6.248   1.00 19.63 ?  133 GLY   B N    1 
ATOM   6477 C CA   . GLY   B 1 133 ? 42.015 -33.276 6.741   1.00 21.00 ?  133 GLY   B CA   1 
ATOM   6478 C C    . GLY   B 1 133 ? 40.606 -33.523 6.234   1.00 21.30 ?  133 GLY   B C    1 
ATOM   6479 O O    . GLY   B 1 133 ? 40.016 -34.538 6.616   1.00 23.59 ?  133 GLY   B O    1 
ATOM   6480 H H    . GLY   B 1 133 ? 43.175 -32.243 5.533   1.00 23.55 ?  133 GLY   B H    1 
ATOM   6481 H HA2  . GLY   B 1 133 ? 42.542 -34.057 6.521   1.00 25.20 ?  133 GLY   B HA2  1 
ATOM   6482 H HA3  . GLY   B 1 133 ? 41.968 -33.215 7.707   1.00 25.20 ?  133 GLY   B HA3  1 
ATOM   6483 N N    . ALA   B 1 134 ? 40.039 -32.647 5.407   1.00 19.77 ?  134 ALA   B N    1 
ATOM   6484 C CA   . ALA   B 1 134 ? 38.710 -32.928 4.876   1.00 20.26 ?  134 ALA   B CA   1 
ATOM   6485 C C    . ALA   B 1 134 ? 38.798 -33.916 3.715   1.00 19.72 ?  134 ALA   B C    1 
ATOM   6486 O O    . ALA   B 1 134 ? 39.859 -34.117 3.111   1.00 20.47 ?  134 ALA   B O    1 
ATOM   6487 C CB   . ALA   B 1 134 ? 38.029 -31.641 4.412   1.00 20.54 ?  134 ALA   B CB   1 
ATOM   6488 H H    . ALA   B 1 134 ? 40.388 -31.900 5.155   1.00 23.73 ?  134 ALA   B H    1 
ATOM   6489 H HA   . ALA   B 1 134 ? 38.167 -33.321 5.574   1.00 24.32 ?  134 ALA   B HA   1 
ATOM   6490 H HB1  . ALA   B 1 134 ? 37.141 -31.856 4.085   1.00 24.65 ?  134 ALA   B HB1  1 
ATOM   6491 H HB2  . ALA   B 1 134 ? 37.964 -31.026 5.161   1.00 24.65 ?  134 ALA   B HB2  1 
ATOM   6492 H HB3  . ALA   B 1 134 ? 38.554 -31.240 3.702   1.00 24.65 ?  134 ALA   B HB3  1 
ATOM   6493 N N    . ASP   B 1 135 ? 37.665 -34.530 3.406   1.00 20.40 ?  135 ASP   B N    1 
ATOM   6494 C CA   . ASP   B 1 135 ? 37.581 -35.427 2.263   1.00 21.28 ?  135 ASP   B CA   1 
ATOM   6495 C C    . ASP   B 1 135 ? 37.665 -34.596 0.988   1.00 19.27 ?  135 ASP   B C    1 
ATOM   6496 O O    . ASP   B 1 135 ? 36.804 -33.729 0.765   1.00 19.59 ?  135 ASP   B O    1 
ATOM   6497 C CB   . ASP   B 1 135 ? 36.254 -36.177 2.320   1.00 23.15 ?  135 ASP   B CB   1 
ATOM   6498 C CG   . ASP   B 1 135 ? 36.086 -37.183 1.197   1.00 25.24 ?  135 ASP   B CG   1 
ATOM   6499 O OD1  . ASP   B 1 135 ? 36.946 -37.250 0.295   1.00 24.94 ?  135 ASP   B OD1  1 
ATOM   6500 O OD2  . ASP   B 1 135 ? 35.079 -37.922 1.228   1.00 28.87 -1 135 ASP   B OD2  1 
ATOM   6501 H H    . ASP   B 1 135 ? 36.931 -34.441 3.840   1.00 24.48 ?  135 ASP   B H    1 
ATOM   6502 H HA   . ASP   B 1 135 ? 38.313 -36.067 2.299   1.00 25.54 ?  135 ASP   B HA   1 
ATOM   6503 H HB2  . ASP   B 1 135 ? 36.201 -36.650 3.162   1.00 27.78 ?  135 ASP   B HB2  1 
ATOM   6504 H HB3  . ASP   B 1 135 ? 35.534 -35.537 2.246   1.00 27.78 ?  135 ASP   B HB3  1 
ATOM   6505 N N    . PRO   B 1 136 ? 38.678 -34.798 0.139   1.00 19.36 ?  136 PRO   B N    1 
ATOM   6506 C CA   . PRO   B 1 136 ? 38.764 -33.990 -1.088  1.00 18.67 ?  136 PRO   B CA   1 
ATOM   6507 C C    . PRO   B 1 136 ? 37.564 -34.151 -2.005  1.00 17.60 ?  136 PRO   B C    1 
ATOM   6508 O O    . PRO   B 1 136 ? 37.243 -33.211 -2.741  1.00 16.57 ?  136 PRO   B O    1 
ATOM   6509 C CB   . PRO   B 1 136 ? 40.074 -34.465 -1.740  1.00 19.43 ?  136 PRO   B CB   1 
ATOM   6510 C CG   . PRO   B 1 136 ? 40.312 -35.845 -1.159  1.00 21.38 ?  136 PRO   B CG   1 
ATOM   6511 C CD   . PRO   B 1 136 ? 39.781 -35.772 0.242   1.00 20.68 ?  136 PRO   B CD   1 
ATOM   6512 H HA   . PRO   B 1 136 ? 38.851 -33.053 -0.867  1.00 22.41 ?  136 PRO   B HA   1 
ATOM   6513 H HB2  . PRO   B 1 136 ? 39.975 -34.505 -2.707  1.00 23.31 ?  136 PRO   B HB2  1 
ATOM   6514 H HB3  . PRO   B 1 136 ? 40.798 -33.858 -1.501  1.00 23.31 ?  136 PRO   B HB3  1 
ATOM   6515 H HG2  . PRO   B 1 136 ? 39.823 -36.507 -1.675  1.00 25.66 ?  136 PRO   B HG2  1 
ATOM   6516 H HG3  . PRO   B 1 136 ? 41.261 -36.045 -1.157  1.00 25.66 ?  136 PRO   B HG3  1 
ATOM   6517 H HD2  . PRO   B 1 136 ? 39.446 -36.638 0.520   1.00 24.82 ?  136 PRO   B HD2  1 
ATOM   6518 H HD3  . PRO   B 1 136 ? 40.467 -35.444 0.848   1.00 24.82 ?  136 PRO   B HD3  1 
ATOM   6519 N N    . ILE   B 1 137 ? 36.901 -35.315 -1.991  1.00 18.22 ?  137 ILE   B N    1 
ATOM   6520 C CA   . ILE   B 1 137 ? 35.683 -35.490 -2.781  1.00 18.32 ?  137 ILE   B CA   1 
ATOM   6521 C C    . ILE   B 1 137 ? 34.602 -34.525 -2.308  1.00 17.68 ?  137 ILE   B C    1 
ATOM   6522 O O    . ILE   B 1 137 ? 33.884 -33.916 -3.114  1.00 16.78 ?  137 ILE   B O    1 
ATOM   6523 C CB   . ILE   B 1 137 ? 35.215 -36.960 -2.712  1.00 20.35 ?  137 ILE   B CB   1 
ATOM   6524 C CG1  . ILE   B 1 137 ? 36.217 -37.870 -3.425  1.00 22.40 ?  137 ILE   B CG1  1 
ATOM   6525 C CG2  . ILE   B 1 137 ? 33.828 -37.126 -3.319  1.00 20.82 ?  137 ILE   B CG2  1 
ATOM   6526 C CD1  . ILE   B 1 137 ? 35.911 -39.353 -3.279  1.00 25.12 ?  137 ILE   B CD1  1 
ATOM   6527 H H    . ILE   B 1 137 ? 37.129 -36.009 -1.535  1.00 21.86 ?  137 ILE   B H    1 
ATOM   6528 H HA   . ILE   B 1 137 ? 35.877 -35.287 -3.710  1.00 21.98 ?  137 ILE   B HA   1 
ATOM   6529 H HB   . ILE   B 1 137 ? 35.173 -37.224 -1.782  1.00 24.42 ?  137 ILE   B HB   1 
ATOM   6530 H HG12 . ILE   B 1 137 ? 36.214 -37.663 -4.373  1.00 26.88 ?  137 ILE   B HG12 1 
ATOM   6531 H HG13 . ILE   B 1 137 ? 37.100 -37.716 -3.057  1.00 26.88 ?  137 ILE   B HG13 1 
ATOM   6532 H HG21 . ILE   B 1 137 ? 33.569 -38.060 -3.283  1.00 24.98 ?  137 ILE   B HG21 1 
ATOM   6533 H HG22 . ILE   B 1 137 ? 33.190 -36.604 -2.812  1.00 24.98 ?  137 ILE   B HG22 1 
ATOM   6534 H HG23 . ILE   B 1 137 ? 33.850 -36.825 -4.239  1.00 24.98 ?  137 ILE   B HG23 1 
ATOM   6535 H HD11 . ILE   B 1 137 ? 36.544 -39.843 -3.821  1.00 30.14 ?  137 ILE   B HD11 1 
ATOM   6536 H HD12 . ILE   B 1 137 ? 36.001 -39.607 -2.346  1.00 30.14 ?  137 ILE   B HD12 1 
ATOM   6537 H HD13 . ILE   B 1 137 ? 35.012 -39.539 -3.590  1.00 30.14 ?  137 ILE   B HD13 1 
ATOM   6538 N N    . HIS   B 1 138 ? 34.476 -34.362 -0.993  1.00 18.73 ?  138 HIS   B N    1 
ATOM   6539 C CA   . HIS   B 1 138 ? 33.527 -33.392 -0.460  1.00 18.95 ?  138 HIS   B CA   1 
ATOM   6540 C C    . HIS   B 1 138 ? 33.941 -31.964 -0.790  1.00 17.43 ?  138 HIS   B C    1 
ATOM   6541 O O    . HIS   B 1 138 ? 33.095 -31.120 -1.100  1.00 18.16 ?  138 HIS   B O    1 
ATOM   6542 C CB   . HIS   B 1 138 ? 33.408 -33.566 1.047   1.00 20.51 ?  138 HIS   B CB   1 
ATOM   6543 C CG   . HIS   B 1 138 ? 32.479 -32.584 1.676   1.00 21.78 ?  138 HIS   B CG   1 
ATOM   6544 N ND1  . HIS   B 1 138 ? 31.140 -32.523 1.356   1.00 24.14 ?  138 HIS   B ND1  1 
ATOM   6545 C CD2  . HIS   B 1 138 ? 32.698 -31.599 2.578   1.00 22.34 ?  138 HIS   B CD2  1 
ATOM   6546 C CE1  . HIS   B 1 138 ? 30.570 -31.551 2.046   1.00 24.04 ?  138 HIS   B CE1  1 
ATOM   6547 N NE2  . HIS   B 1 138 ? 31.493 -30.976 2.798   1.00 22.89 ?  138 HIS   B NE2  1 
ATOM   6548 H H    . HIS   B 1 138 ? 34.924 -34.797 -0.401  1.00 22.48 ?  138 HIS   B H    1 
ATOM   6549 H HA   . HIS   B 1 138 ? 32.655 -33.558 -0.851  1.00 22.74 ?  138 HIS   B HA   1 
ATOM   6550 H HB2  . HIS   B 1 138 ? 33.074 -34.460 1.239   1.00 24.62 ?  138 HIS   B HB2  1 
ATOM   6551 H HB3  . HIS   B 1 138 ? 34.283 -33.451 1.450   1.00 24.62 ?  138 HIS   B HB3  1 
ATOM   6552 H HD1  . HIS   B 1 138 ? 30.738 -33.042 0.797   1.00 28.97 ?  138 HIS   B HD1  1 
ATOM   6553 H HD2  . HIS   B 1 138 ? 33.503 -31.392 2.987   1.00 26.81 ?  138 HIS   B HD2  1 
ATOM   6554 H HE1  . HIS   B 1 138 ? 29.668 -31.320 2.012   1.00 28.84 ?  138 HIS   B HE1  1 
ATOM   6555 N N    . SER   B 1 139 ? 35.237 -31.665 -0.724  1.00 16.64 ?  139 SER   B N    1 
ATOM   6556 C CA   . SER   B 1 139 ? 35.674 -30.315 -1.048  1.00 15.79 ?  139 SER   B CA   1 
ATOM   6557 C C    . SER   B 1 139 ? 35.339 -29.961 -2.490  1.00 14.40 ?  139 SER   B C    1 
ATOM   6558 O O    . SER   B 1 139 ? 34.895 -28.845 -2.773  1.00 15.22 ?  139 SER   B O    1 
ATOM   6559 C CB   . SER   B 1 139 ? 37.169 -30.172 -0.786  1.00 16.41 ?  139 SER   B CB   1 
ATOM   6560 O OG   . SER   B 1 139 ? 37.586 -28.825 -0.995  1.00 16.30 ?  139 SER   B OG   1 
ATOM   6561 H H    . SER   B 1 139 ? 35.863 -32.210 -0.504  1.00 19.96 ?  139 SER   B H    1 
ATOM   6562 H HA   . SER   B 1 139 ? 35.206 -29.688 -0.480  1.00 18.95 ?  139 SER   B HA   1 
ATOM   6563 H HB2  . SER   B 1 139 ? 37.351 -30.429 0.132   1.00 19.69 ?  139 SER   B HB2  1 
ATOM   6564 H HB3  . SER   B 1 139 ? 37.656 -30.744 -1.396  1.00 19.69 ?  139 SER   B HB3  1 
ATOM   6565 H HG   . SER   B 1 139 ? 37.177 -28.313 -0.450  1.00 19.56 ?  139 SER   B HG   1 
ATOM   6566 N N    . LEU   B 1 140 ? 35.536 -30.904 -3.413  1.00 14.24 ?  140 LEU   B N    1 
ATOM   6567 C CA   . LEU   B 1 140 ? 35.175 -30.662 -4.806  1.00 14.52 ?  140 LEU   B CA   1 
ATOM   6568 C C    . LEU   B 1 140 ? 33.674 -30.425 -4.943  1.00 14.89 ?  140 LEU   B C    1 
ATOM   6569 O O    . LEU   B 1 140 ? 33.245 -29.535 -5.679  1.00 14.98 ?  140 LEU   B O    1 
ATOM   6570 C CB   . LEU   B 1 140 ? 35.645 -31.833 -5.681  1.00 15.00 ?  140 LEU   B CB   1 
ATOM   6571 C CG   . LEU   B 1 140 ? 35.293 -31.716 -7.159  1.00 15.21 ?  140 LEU   B CG   1 
ATOM   6572 C CD1  . LEU   B 1 140 ? 35.880 -30.443 -7.764  1.00 16.09 ?  140 LEU   B CD1  1 
ATOM   6573 C CD2  . LEU   B 1 140 ? 35.768 -32.948 -7.909  1.00 16.47 ?  140 LEU   B CD2  1 
ATOM   6574 H H    . LEU   B 1 140 ? 35.873 -31.681 -3.265  1.00 17.09 ?  140 LEU   B H    1 
ATOM   6575 H HA   . LEU   B 1 140 ? 35.636 -29.866 -5.115  1.00 17.43 ?  140 LEU   B HA   1 
ATOM   6576 H HB2  . LEU   B 1 140 ? 36.616 -31.899 -5.623  1.00 18.00 ?  140 LEU   B HB2  1 
ATOM   6577 H HB3  . LEU   B 1 140 ? 35.246 -32.651 -5.355  1.00 18.00 ?  140 LEU   B HB3  1 
ATOM   6578 H HG   . LEU   B 1 140 ? 34.330 -31.667 -7.248  1.00 18.25 ?  140 LEU   B HG   1 
ATOM   6579 H HD11 . LEU   B 1 140 ? 35.759 -30.466 -8.724  1.00 19.31 ?  140 LEU   B HD11 1 
ATOM   6580 H HD12 . LEU   B 1 140 ? 35.421 -29.673 -7.391  1.00 19.31 ?  140 LEU   B HD12 1 
ATOM   6581 H HD13 . LEU   B 1 140 ? 36.826 -30.399 -7.550  1.00 19.31 ?  140 LEU   B HD13 1 
ATOM   6582 H HD21 . LEU   B 1 140 ? 35.531 -32.853 -8.845  1.00 19.77 ?  140 LEU   B HD21 1 
ATOM   6583 H HD22 . LEU   B 1 140 ? 36.728 -33.023 -7.814  1.00 19.77 ?  140 LEU   B HD22 1 
ATOM   6584 H HD23 . LEU   B 1 140 ? 35.332 -33.727 -7.533  1.00 19.77 ?  140 LEU   B HD23 1 
ATOM   6585 N N    . ARG   B 1 141 ? 32.869 -31.230 -4.248  1.00 15.57 ?  141 ARG   B N    1 
ATOM   6586 C CA   . ARG   B 1 141 ? 31.422 -31.052 -4.221  1.00 16.39 ?  141 ARG   B CA   1 
ATOM   6587 C C    . ARG   B 1 141 ? 31.039 -29.638 -3.803  1.00 15.39 ?  141 ARG   B C    1 
ATOM   6588 O O    . ARG   B 1 141 ? 30.243 -28.961 -4.474  1.00 16.42 ?  141 ARG   B O    1 
ATOM   6589 C CB   . ARG   B 1 141 ? 30.852 -32.067 -3.223  1.00 18.31 ?  141 ARG   B CB   1 
ATOM   6590 C CG   . ARG   B 1 141 ? 29.382 -31.959 -2.900  1.00 20.75 ?  141 ARG   B CG   1 
ATOM   6591 C CD   . ARG   B 1 141 ? 28.594 -32.615 -3.960  1.00 23.05 ?  141 ARG   B CD   1 
ATOM   6592 N NE   . ARG   B 1 141 ? 28.305 -31.712 -5.061  1.00 23.54 ?  141 ARG   B NE   1 
ATOM   6593 C CZ   . ARG   B 1 141 ? 28.309 -32.057 -6.341  1.00 22.67 ?  141 ARG   B CZ   1 
ATOM   6594 N NH1  . ARG   B 1 141 ? 28.777 -33.229 -6.745  1.00 22.09 ?  141 ARG   B NH1  1 
ATOM   6595 N NH2  . ARG   B 1 141 ? 27.829 -31.204 -7.241  1.00 23.85 ?  141 ARG   B NH2  1 
ATOM   6596 H H    . ARG   B 1 141 ? 33.147 -31.893 -3.780  1.00 18.69 ?  141 ARG   B H    1 
ATOM   6597 H HA   . ARG   B 1 141 ? 31.049 -31.220 -5.094  1.00 19.67 ?  141 ARG   B HA   1 
ATOM   6598 H HB2  . ARG   B 1 141 ? 31.016 -32.955 -3.576  1.00 21.97 ?  141 ARG   B HB2  1 
ATOM   6599 H HB3  . ARG   B 1 141 ? 31.331 -31.969 -2.387  1.00 21.97 ?  141 ARG   B HB3  1 
ATOM   6600 H HG2  . ARG   B 1 141 ? 29.207 -32.403 -2.058  1.00 24.90 ?  141 ARG   B HG2  1 
ATOM   6601 H HG3  . ARG   B 1 141 ? 29.117 -31.023 -2.847  1.00 24.90 ?  141 ARG   B HG3  1 
ATOM   6602 H HD2  . ARG   B 1 141 ? 29.091 -33.378 -4.302  1.00 27.65 ?  141 ARG   B HD2  1 
ATOM   6603 H HD3  . ARG   B 1 141 ? 27.757 -32.917 -3.585  1.00 27.65 ?  141 ARG   B HD3  1 
ATOM   6604 H HE   . ARG   B 1 141 ? 28.084 -30.902 -4.865  1.00 28.25 ?  141 ARG   B HE   1 
ATOM   6605 H HH11 . ARG   B 1 141 ? 29.077 -33.799 -6.176  1.00 26.50 ?  141 ARG   B HH11 1 
ATOM   6606 H HH12 . ARG   B 1 141 ? 28.776 -33.424 -7.581  1.00 26.50 ?  141 ARG   B HH12 1 
ATOM   6607 H HH21 . ARG   B 1 141 ? 27.533 -30.433 -6.992  1.00 28.62 ?  141 ARG   B HH21 1 
ATOM   6608 H HH22 . ARG   B 1 141 ? 27.847 -31.402 -8.078  1.00 28.62 ?  141 ARG   B HH22 1 
ATOM   6609 N N    . VAL   B 1 142 ? 31.581 -29.182 -2.673  1.00 15.45 ?  142 VAL   B N    1 
ATOM   6610 C CA   . VAL   B 1 142 ? 31.255 -27.845 -2.192  1.00 14.73 ?  142 VAL   B CA   1 
ATOM   6611 C C    . VAL   B 1 142 ? 31.740 -26.787 -3.182  1.00 14.76 ?  142 VAL   B C    1 
ATOM   6612 O O    . VAL   B 1 142 ? 31.042 -25.798 -3.445  1.00 15.19 ?  142 VAL   B O    1 
ATOM   6613 C CB   . VAL   B 1 142 ? 31.808 -27.619 -0.771  1.00 16.08 ?  142 VAL   B CB   1 
ATOM   6614 C CG1  . VAL   B 1 142 ? 31.510 -26.197 -0.296  1.00 16.23 ?  142 VAL   B CG1  1 
ATOM   6615 C CG2  . VAL   B 1 142 ? 31.220 -28.640 0.198   1.00 17.10 ?  142 VAL   B CG2  1 
ATOM   6616 H H    . VAL   B 1 142 ? 32.124 -29.625 -2.166  1.00 18.53 ?  142 VAL   B H    1 
ATOM   6617 H HA   . VAL   B 1 142 ? 30.297 -27.764 -2.134  1.00 17.67 ?  142 VAL   B HA   1 
ATOM   6618 H HB   . VAL   B 1 142 ? 32.773 -27.739 -0.778  1.00 19.29 ?  142 VAL   B HB   1 
ATOM   6619 H HG11 . VAL   B 1 142 ? 31.702 -26.136 0.654   1.00 19.47 ?  142 VAL   B HG11 1 
ATOM   6620 H HG12 . VAL   B 1 142 ? 32.079 -25.577 -0.783  1.00 19.47 ?  142 VAL   B HG12 1 
ATOM   6621 H HG13 . VAL   B 1 142 ? 30.580 -25.997 -0.462  1.00 19.47 ?  142 VAL   B HG13 1 
ATOM   6622 H HG21 . VAL   B 1 142 ? 31.547 -28.454 1.091   1.00 20.52 ?  142 VAL   B HG21 1 
ATOM   6623 H HG22 . VAL   B 1 142 ? 30.255 -28.576 0.174   1.00 20.52 ?  142 VAL   B HG22 1 
ATOM   6624 H HG23 . VAL   B 1 142 ? 31.501 -29.531 -0.076  1.00 20.52 ?  142 VAL   B HG23 1 
ATOM   6625 N N    . CYS   B 1 143 ? 32.933 -26.982 -3.756  1.00 14.26 ?  143 CYS   B N    1 
ATOM   6626 C CA   . CYS   B 1 143 ? 33.429 -26.055 -4.771  1.00 14.40 ?  143 CYS   B CA   1 
ATOM   6627 C C    . CYS   B 1 143 ? 32.421 -25.914 -5.912  1.00 14.34 ?  143 CYS   B C    1 
ATOM   6628 O O    . CYS   B 1 143 ? 32.011 -24.804 -6.269  1.00 14.91 ?  143 CYS   B O    1 
ATOM   6629 C CB   . CYS   B 1 143 ? 34.788 -26.541 -5.292  1.00 14.40 ?  143 CYS   B CB   1 
ATOM   6630 S SG   . CYS   B 1 143 ? 35.532 -25.441 -6.521  1.00 14.86 ?  143 CYS   B SG   1 
ATOM   6631 H H    . CYS   B 1 143 ? 33.471 -27.630 -3.566  1.00 17.11 ?  143 CYS   B H    1 
ATOM   6632 H HA   . CYS   B 1 143 ? 33.560 -25.180 -4.365  1.00 17.27 ?  143 CYS   B HA   1 
ATOM   6633 H HB2  . CYS   B 1 143 ? 35.411 -26.615 -4.546  1.00 17.28 ?  143 CYS   B HB2  1 
ATOM   6634 H HB3  . CYS   B 1 143 ? 34.674 -27.409 -5.699  1.00 17.28 ?  143 CYS   B HB3  1 
ATOM   6635 H HG   . CYS   B 1 143 ? 36.604 -25.885 -6.839  1.00 17.84 ?  143 CYS   B HG   1 
ATOM   6636 N N    . VAL   B 1 144 ? 32.000 -27.038 -6.494  1.00 14.98 ?  144 VAL   B N    1 
ATOM   6637 C CA   . VAL   B 1 144 ? 31.110 -26.978 -7.647  1.00 16.35 ?  144 VAL   B CA   1 
ATOM   6638 C C    . VAL   B 1 144 ? 29.760 -26.363 -7.286  1.00 16.49 ?  144 VAL   B C    1 
ATOM   6639 O O    . VAL   B 1 144 ? 29.132 -25.688 -8.113  1.00 17.68 ?  144 VAL   B O    1 
ATOM   6640 C CB   . VAL   B 1 144 ? 30.951 -28.404 -8.198  1.00 19.30 ?  144 VAL   B CB   1 
ATOM   6641 C CG1  . VAL   B 1 144 ? 29.660 -28.554 -8.986  1.00 22.28 ?  144 VAL   B CG1  1 
ATOM   6642 C CG2  . VAL   B 1 144 ? 32.178 -28.804 -9.021  1.00 18.75 ?  144 VAL   B CG2  1 
ATOM   6643 H H    . VAL   B 1 144 ? 32.230 -27.830 -6.246  1.00 17.98 ?  144 VAL   B H    1 
ATOM   6644 H HA   . VAL   B 1 144 ? 31.516 -26.434 -8.337  1.00 19.62 ?  144 VAL   B HA   1 
ATOM   6645 H HB   . VAL   B 1 144 ? 30.904 -29.020 -7.448  1.00 23.16 ?  144 VAL   B HB   1 
ATOM   6646 H HG11 . VAL   B 1 144 ? 29.722 -29.358 -9.531  1.00 26.73 ?  144 VAL   B HG11 1 
ATOM   6647 H HG12 . VAL   B 1 144 ? 28.919 -28.637 -8.369  1.00 26.73 ?  144 VAL   B HG12 1 
ATOM   6648 H HG13 . VAL   B 1 144 ? 29.545 -27.782 -9.556  1.00 26.73 ?  144 VAL   B HG13 1 
ATOM   6649 H HG21 . VAL   B 1 144 ? 32.059 -29.708 -9.355  1.00 22.50 ?  144 VAL   B HG21 1 
ATOM   6650 H HG22 . VAL   B 1 144 ? 32.271 -28.189 -9.770  1.00 22.50 ?  144 VAL   B HG22 1 
ATOM   6651 H HG23 . VAL   B 1 144 ? 32.968 -28.760 -8.461  1.00 22.50 ?  144 VAL   B HG23 1 
ATOM   6652 N N    . ASP   B 1 145 ? 29.282 -26.607 -6.067  1.00 16.41 ?  145 ASP   B N    1 
ATOM   6653 C CA   . ASP   B 1 145 ? 27.982 -26.115 -5.633  1.00 17.55 ?  145 ASP   B CA   1 
ATOM   6654 C C    . ASP   B 1 145 ? 28.024 -24.694 -5.092  1.00 16.84 ?  145 ASP   B C    1 
ATOM   6655 O O    . ASP   B 1 145 ? 26.969 -24.152 -4.761  1.00 19.27 ?  145 ASP   B O    1 
ATOM   6656 C CB   . ASP   B 1 145 ? 27.412 -27.032 -4.540  1.00 19.68 ?  145 ASP   B CB   1 
ATOM   6657 C CG   . ASP   B 1 145 ? 27.018 -28.410 -5.053  1.00 21.69 ?  145 ASP   B CG   1 
ATOM   6658 O OD1  . ASP   B 1 145 ? 26.909 -28.626 -6.284  1.00 20.81 ?  145 ASP   B OD1  1 
ATOM   6659 O OD2  . ASP   B 1 145 ? 26.810 -29.287 -4.193  1.00 23.78 -1 145 ASP   B OD2  1 
ATOM   6660 H H    . ASP   B 1 145 ? 29.709 -27.047 -5.470  1.00 19.69 ?  145 ASP   B H    1 
ATOM   6661 H HA   . ASP   B 1 145 ? 27.374 -26.116 -6.383  1.00 21.06 ?  145 ASP   B HA   1 
ATOM   6662 H HB2  . ASP   B 1 145 ? 28.085 -27.157 -3.854  1.00 23.62 ?  145 ASP   B HB2  1 
ATOM   6663 H HB3  . ASP   B 1 145 ? 26.625 -26.613 -4.161  1.00 23.62 ?  145 ASP   B HB3  1 
ATOM   6664 N N    . THR   B 1 146 ? 29.202 -24.092 -4.976  1.00 15.59 ?  146 THR   B N    1 
ATOM   6665 C CA   . THR   B 1 146 ? 29.343 -22.760 -4.383  1.00 15.37 ?  146 THR   B CA   1 
ATOM   6666 C C    . THR   B 1 146 ? 29.976 -21.741 -5.313  1.00 14.43 ?  146 THR   B C    1 
ATOM   6667 O O    . THR   B 1 146 ? 29.504 -20.591 -5.385  1.00 14.78 ?  146 THR   B O    1 
ATOM   6668 C CB   . THR   B 1 146 ? 30.162 -22.855 -3.088  1.00 15.40 ?  146 THR   B CB   1 
ATOM   6669 O OG1  . THR   B 1 146 ? 29.574 -23.838 -2.219  1.00 15.61 ?  146 THR   B OG1  1 
ATOM   6670 C CG2  . THR   B 1 146 ? 30.227 -21.503 -2.383  1.00 15.48 ?  146 THR   B CG2  1 
ATOM   6671 H H    . THR   B 1 146 ? 29.951 -24.419 -5.246  1.00 18.71 ?  146 THR   B H    1 
ATOM   6672 H HA   . THR   B 1 146 ? 28.469 -22.423 -4.143  1.00 18.44 ?  146 THR   B HA   1 
ATOM   6673 H HB   . THR   B 1 146 ? 31.076 -23.117 -3.302  1.00 18.48 ?  146 THR   B HB   1 
ATOM   6674 H HG1  . THR   B 1 146 ? 29.607 -24.599 -2.582  1.00 18.73 ?  146 THR   B HG1  1 
ATOM   6675 H HG21 . THR   B 1 146 ? 30.571 -21.614 -1.482  1.00 18.57 ?  146 THR   B HG21 1 
ATOM   6676 H HG22 . THR   B 1 146 ? 30.818 -20.902 -2.868  1.00 18.57 ?  146 THR   B HG22 1 
ATOM   6677 H HG23 . THR   B 1 146 ? 29.344 -21.112 -2.337  1.00 18.57 ?  146 THR   B HG23 1 
ATOM   6678 N N    . VAL   B 1 147 ? 31.040 -22.118 -6.011  1.00 13.78 ?  147 VAL   B N    1 
ATOM   6679 C CA   . VAL   B 1 147 ? 31.761 -21.176 -6.856  1.00 13.29 ?  147 VAL   B CA   1 
ATOM   6680 C C    . VAL   B 1 147 ? 31.033 -21.032 -8.183  1.00 14.23 ?  147 VAL   B C    1 
ATOM   6681 O O    . VAL   B 1 147 ? 30.658 -22.027 -8.821  1.00 15.32 ?  147 VAL   B O    1 
ATOM   6682 C CB   . VAL   B 1 147 ? 33.221 -21.620 -7.046  1.00 13.51 ?  147 VAL   B CB   1 
ATOM   6683 C CG1  . VAL   B 1 147 ? 33.974 -20.584 -7.869  1.00 13.35 ?  147 VAL   B CG1  1 
ATOM   6684 C CG2  . VAL   B 1 147 ? 33.890 -21.817 -5.696  1.00 13.94 ?  147 VAL   B CG2  1 
ATOM   6685 H H    . VAL   B 1 147 ? 31.363 -22.919 -6.015  1.00 16.54 ?  147 VAL   B H    1 
ATOM   6686 H HA   . VAL   B 1 147 ? 31.770 -20.310 -6.420  1.00 15.95 ?  147 VAL   B HA   1 
ATOM   6687 H HB   . VAL   B 1 147 ? 33.246 -22.462 -7.526  1.00 16.21 ?  147 VAL   B HB   1 
ATOM   6688 H HG11 . VAL   B 1 147 ? 34.922 -20.785 -7.854  1.00 16.01 ?  147 VAL   B HG11 1 
ATOM   6689 H HG12 . VAL   B 1 147 ? 33.649 -20.597 -8.784  1.00 16.01 ?  147 VAL   B HG12 1 
ATOM   6690 H HG13 . VAL   B 1 147 ? 33.824 -19.700 -7.484  1.00 16.01 ?  147 VAL   B HG13 1 
ATOM   6691 H HG21 . VAL   B 1 147 ? 34.832 -21.985 -5.830  1.00 16.73 ?  147 VAL   B HG21 1 
ATOM   6692 H HG22 . VAL   B 1 147 ? 33.768 -21.009 -5.167  1.00 16.73 ?  147 VAL   B HG22 1 
ATOM   6693 H HG23 . VAL   B 1 147 ? 33.475 -22.569 -5.247  1.00 16.73 ?  147 VAL   B HG23 1 
ATOM   6694 N N    . ARG   B 1 148 ? 30.825 -19.777 -8.592  1.00 14.06 ?  148 ARG   B N    1 
ATOM   6695 C CA   . ARG   B 1 148 ? 30.203 -19.448 -9.862  1.00 14.41 ?  148 ARG   B CA   1 
ATOM   6696 C C    . ARG   B 1 148 ? 31.163 -18.777 -10.835 1.00 14.16 ?  148 ARG   B C    1 
ATOM   6697 O O    . ARG   B 1 148 ? 30.877 -18.754 -12.037 1.00 15.91 ?  148 ARG   B O    1 
ATOM   6698 C CB   . ARG   B 1 148 ? 28.968 -18.556 -9.638  1.00 15.08 ?  148 ARG   B CB   1 
ATOM   6699 C CG   . ARG   B 1 148 ? 27.892 -19.270 -8.835  1.00 15.66 ?  148 ARG   B CG   1 
ATOM   6700 C CD   . ARG   B 1 148 ? 26.678 -18.389 -8.536  1.00 16.79 ?  148 ARG   B CD   1 
ATOM   6701 N NE   . ARG   B 1 148 ? 27.047 -17.186 -7.799  1.00 16.47 ?  148 ARG   B NE   1 
ATOM   6702 C CZ   . ARG   B 1 148 ? 27.362 -17.156 -6.509  1.00 15.75 ?  148 ARG   B CZ   1 
ATOM   6703 N NH1  . ARG   B 1 148 ? 27.309 -18.247 -5.755  1.00 15.56 ?  148 ARG   B NH1  1 
ATOM   6704 N NH2  . ARG   B 1 148 ? 27.752 -16.005 -5.964  1.00 16.31 ?  148 ARG   B NH2  1 
ATOM   6705 H H    . ARG   B 1 148 ? 31.049 -19.079 -8.133  1.00 16.87 ?  148 ARG   B H    1 
ATOM   6706 H HA   . ARG   B 1 148 ? 29.898 -20.267 -10.278 1.00 17.29 ?  148 ARG   B HA   1 
ATOM   6707 H HB2  . ARG   B 1 148 ? 29.236 -17.762 -9.149  1.00 18.09 ?  148 ARG   B HB2  1 
ATOM   6708 H HB3  . ARG   B 1 148 ? 28.594 -18.310 -10.497 1.00 18.09 ?  148 ARG   B HB3  1 
ATOM   6709 H HG2  . ARG   B 1 148 ? 27.589 -20.041 -9.340  1.00 18.79 ?  148 ARG   B HG2  1 
ATOM   6710 H HG3  . ARG   B 1 148 ? 28.273 -19.558 -7.990  1.00 18.79 ?  148 ARG   B HG3  1 
ATOM   6711 H HD2  . ARG   B 1 148 ? 26.272 -18.122 -9.372  1.00 20.15 ?  148 ARG   B HD2  1 
ATOM   6712 H HD3  . ARG   B 1 148 ? 26.051 -18.894 -7.999  1.00 20.15 ?  148 ARG   B HD3  1 
ATOM   6713 H HE   . ARG   B 1 148 ? 27.083 -16.448 -8.237  1.00 19.76 ?  148 ARG   B HE   1 
ATOM   6714 H HH11 . ARG   B 1 148 ? 27.058 -18.998 -6.095  1.00 18.67 ?  148 ARG   B HH11 1 
ATOM   6715 H HH12 . ARG   B 1 148 ? 27.506 -18.203 -4.920  1.00 18.67 ?  148 ARG   B HH12 1 
ATOM   6716 H HH21 . ARG   B 1 148 ? 27.794 -15.295 -6.446  1.00 19.58 ?  148 ARG   B HH21 1 
ATOM   6717 H HH22 . ARG   B 1 148 ? 27.951 -15.971 -5.129  1.00 19.58 ?  148 ARG   B HH22 1 
ATOM   6718 N N    . THR   B 1 149 ? 32.280 -18.237 -10.350 1.00 14.38 ?  149 THR   B N    1 
ATOM   6719 C CA   . THR   B 1 149 ? 33.319 -17.672 -11.199 1.00 14.25 ?  149 THR   B CA   1 
ATOM   6720 C C    . THR   B 1 149 ? 34.194 -18.811 -11.721 1.00 13.61 ?  149 THR   B C    1 
ATOM   6721 O O    . THR   B 1 149 ? 33.991 -19.982 -11.386 1.00 14.21 ?  149 THR   B O    1 
ATOM   6722 C CB   . THR   B 1 149 ? 34.095 -16.623 -10.412 1.00 14.25 ?  149 THR   B CB   1 
ATOM   6723 O OG1  . THR   B 1 149 ? 34.556 -17.221 -9.199  1.00 14.35 ?  149 THR   B OG1  1 
ATOM   6724 C CG2  . THR   B 1 149 ? 33.207 -15.429 -10.100 1.00 15.50 ?  149 THR   B CG2  1 
ATOM   6725 H H    . THR   B 1 149 ? 32.451 -18.174 -9.508  1.00 17.26 ?  149 THR   B H    1 
ATOM   6726 H HA   . THR   B 1 149 ? 32.903 -17.231 -11.957 1.00 17.10 ?  149 THR   B HA   1 
ATOM   6727 H HB   . THR   B 1 149 ? 34.852 -16.320 -10.932 1.00 17.10 ?  149 THR   B HB   1 
ATOM   6728 H HG1  . THR   B 1 149 ? 34.986 -16.657 -8.739  1.00 17.22 ?  149 THR   B HG1  1 
ATOM   6729 H HG21 . THR   B 1 149 ? 33.712 -14.756 -9.619  1.00 18.60 ?  149 THR   B HG21 1 
ATOM   6730 H HG22 . THR   B 1 149 ? 32.868 -15.045 -10.922 1.00 18.60 ?  149 THR   B HG22 1 
ATOM   6731 H HG23 . THR   B 1 149 ? 32.455 -15.709 -9.550  1.00 18.60 ?  149 THR   B HG23 1 
ATOM   6732 N N    . ASN   B 1 150 ? 35.157 -18.490 -12.576 1.00 13.43 ?  150 ASN   B N    1 
ATOM   6733 C CA   . ASN   B 1 150 ? 35.933 -19.514 -13.267 1.00 14.11 ?  150 ASN   B CA   1 
ATOM   6734 C C    . ASN   B 1 150 ? 37.100 -19.959 -12.393 1.00 13.11 ?  150 ASN   B C    1 
ATOM   6735 O O    . ASN   B 1 150 ? 38.040 -19.196 -12.154 1.00 14.30 ?  150 ASN   B O    1 
ATOM   6736 C CB   . ASN   B 1 150 ? 36.404 -19.002 -14.622 1.00 16.50 ?  150 ASN   B CB   1 
ATOM   6737 C CG   . ASN   B 1 150 ? 35.258 -18.770 -15.565 1.00 19.44 ?  150 ASN   B CG   1 
ATOM   6738 O OD1  . ASN   B 1 150 ? 34.337 -19.572 -15.626 1.00 20.35 ?  150 ASN   B OD1  1 
ATOM   6739 N ND2  . ASN   B 1 150 ? 35.280 -17.655 -16.276 1.00 21.90 ?  150 ASN   B ND2  1 
ATOM   6740 H H    . ASN   B 1 150 ? 35.382 -17.678 -12.771 1.00 16.12 ?  150 ASN   B H    1 
ATOM   6741 H HA   . ASN   B 1 150 ? 35.355 -20.282 -13.424 1.00 16.93 ?  150 ASN   B HA   1 
ATOM   6742 H HB2  . ASN   B 1 150 ? 36.864 -18.158 -14.501 1.00 19.80 ?  150 ASN   B HB2  1 
ATOM   6743 H HB3  . ASN   B 1 150 ? 36.994 -19.655 -15.021 1.00 19.80 ?  150 ASN   B HB3  1 
ATOM   6744 H HD21 . ASN   B 1 150 ? 34.643 -17.476 -16.835 1.00 26.28 ?  150 ASN   B HD21 1 
ATOM   6745 H HD22 . ASN   B 1 150 ? 35.937 -17.105 -16.198 1.00 26.28 ?  150 ASN   B HD22 1 
ATOM   6746 N N    . VAL   B 1 151 ? 37.054 -21.202 -11.925 1.00 12.80 ?  151 VAL   B N    1 
ATOM   6747 C CA   . VAL   B 1 151 ? 38.068 -21.735 -11.026 1.00 12.91 ?  151 VAL   B CA   1 
ATOM   6748 C C    . VAL   B 1 151 ? 38.764 -22.913 -11.697 1.00 12.84 ?  151 VAL   B C    1 
ATOM   6749 O O    . VAL   B 1 151 ? 38.113 -23.841 -12.200 1.00 14.72 ?  151 VAL   B O    1 
ATOM   6750 C CB   . VAL   B 1 151 ? 37.505 -22.072 -9.628  1.00 14.58 ?  151 VAL   B CB   1 
ATOM   6751 C CG1  . VAL   B 1 151 ? 36.338 -23.073 -9.697  1.00 16.63 ?  151 VAL   B CG1  1 
ATOM   6752 C CG2  . VAL   B 1 151 ? 38.618 -22.581 -8.723  1.00 14.64 ?  151 VAL   B CG2  1 
ATOM   6753 H H    . VAL   B 1 151 ? 36.430 -21.771 -12.125 1.00 15.36 ?  151 VAL   B H    1 
ATOM   6754 H HA   . VAL   B 1 151 ? 38.736 -21.045 -10.897 1.00 15.49 ?  151 VAL   B HA   1 
ATOM   6755 H HB   . VAL   B 1 151 ? 37.159 -21.251 -9.233  1.00 17.49 ?  151 VAL   B HB   1 
ATOM   6756 H HG11 . VAL   B 1 151 ? 36.018 -23.247 -8.795  1.00 19.96 ?  151 VAL   B HG11 1 
ATOM   6757 H HG12 . VAL   B 1 151 ? 35.620 -22.691 -10.229 1.00 19.96 ?  151 VAL   B HG12 1 
ATOM   6758 H HG13 . VAL   B 1 151 ? 36.650 -23.895 -10.101 1.00 19.96 ?  151 VAL   B HG13 1 
ATOM   6759 H HG21 . VAL   B 1 151 ? 38.278 -22.642 -7.815  1.00 17.57 ?  151 VAL   B HG21 1 
ATOM   6760 H HG22 . VAL   B 1 151 ? 38.900 -23.454 -9.030  1.00 17.57 ?  151 VAL   B HG22 1 
ATOM   6761 H HG23 . VAL   B 1 151 ? 39.360 -21.958 -8.755  1.00 17.57 ?  151 VAL   B HG23 1 
ATOM   6762 N N    . TYR   B 1 152 ? 40.091 -22.839 -11.725 1.00 12.79 ?  152 TYR   B N    1 
ATOM   6763 C CA   . TYR   B 1 152 ? 40.988 -23.836 -12.298 1.00 12.81 ?  152 TYR   B CA   1 
ATOM   6764 C C    . TYR   B 1 152 ? 41.715 -24.509 -11.138 1.00 11.84 ?  152 TYR   B C    1 
ATOM   6765 O O    . TYR   B 1 152 ? 42.571 -23.892 -10.494 1.00 12.70 ?  152 TYR   B O    1 
ATOM   6766 C CB   . TYR   B 1 152 ? 41.961 -23.150 -13.263 1.00 13.41 ?  152 TYR   B CB   1 
ATOM   6767 C CG   . TYR   B 1 152 ? 41.284 -22.674 -14.528 1.00 14.17 ?  152 TYR   B CG   1 
ATOM   6768 C CD1  . TYR   B 1 152 ? 40.640 -21.440 -14.587 1.00 14.66 ?  152 TYR   B CD1  1 
ATOM   6769 C CD2  . TYR   B 1 152 ? 41.271 -23.469 -15.661 1.00 15.11 ?  152 TYR   B CD2  1 
ATOM   6770 C CE1  . TYR   B 1 152 ? 40.001 -21.021 -15.736 1.00 15.84 ?  152 TYR   B CE1  1 
ATOM   6771 C CE2  . TYR   B 1 152 ? 40.631 -23.069 -16.815 1.00 16.13 ?  152 TYR   B CE2  1 
ATOM   6772 C CZ   . TYR   B 1 152 ? 40.000 -21.838 -16.852 1.00 15.93 ?  152 TYR   B CZ   1 
ATOM   6773 O OH   . TYR   B 1 152 ? 39.371 -21.445 -18.004 1.00 19.77 ?  152 TYR   B OH   1 
ATOM   6774 H H    . TYR   B 1 152 ? 40.527 -22.172 -11.383 1.00 15.35 ?  152 TYR   B H    1 
ATOM   6775 H HA   . TYR   B 1 152 ? 40.467 -24.497 -12.782 1.00 15.37 ?  152 TYR   B HA   1 
ATOM   6776 H HB2  . TYR   B 1 152 ? 42.351 -22.380 -12.821 1.00 16.09 ?  152 TYR   B HB2  1 
ATOM   6777 H HB3  . TYR   B 1 152 ? 42.655 -23.781 -13.507 1.00 16.09 ?  152 TYR   B HB3  1 
ATOM   6778 H HD1  . TYR   B 1 152 ? 40.634 -20.897 -13.835 1.00 17.60 ?  152 TYR   B HD1  1 
ATOM   6779 H HD2  . TYR   B 1 152 ? 41.684 -24.307 -15.639 1.00 18.13 ?  152 TYR   B HD2  1 
ATOM   6780 H HE1  . TYR   B 1 152 ? 39.572 -20.192 -15.770 1.00 19.01 ?  152 TYR   B HE1  1 
ATOM   6781 H HE2  . TYR   B 1 152 ? 40.633 -23.618 -17.568 1.00 19.36 ?  152 TYR   B HE2  1 
ATOM   6782 H HH   . TYR   B 1 152 ? 39.454 -22.027 -18.604 1.00 23.73 ?  152 TYR   B HH   1 
ATOM   6783 N N    . LEU   B 1 153 ? 41.342 -25.761 -10.857 1.00 12.44 ?  153 LEU   B N    1 
ATOM   6784 C CA   . LEU   B 1 153 ? 41.854 -26.506 -9.718  1.00 12.36 ?  153 LEU   B CA   1 
ATOM   6785 C C    . LEU   B 1 153 ? 43.078 -27.317 -10.114 1.00 12.37 ?  153 LEU   B C    1 
ATOM   6786 O O    . LEU   B 1 153 ? 43.051 -28.048 -11.108 1.00 13.66 ?  153 LEU   B O    1 
ATOM   6787 C CB   . LEU   B 1 153 ? 40.782 -27.466 -9.200  1.00 12.84 ?  153 LEU   B CB   1 
ATOM   6788 C CG   . LEU   B 1 153 ? 39.525 -26.806 -8.636  1.00 13.89 ?  153 LEU   B CG   1 
ATOM   6789 C CD1  . LEU   B 1 153 ? 38.424 -27.846 -8.493  1.00 14.82 ?  153 LEU   B CD1  1 
ATOM   6790 C CD2  . LEU   B 1 153 ? 39.815 -26.127 -7.296  1.00 13.99 ?  153 LEU   B CD2  1 
ATOM   6791 H H    . LEU   B 1 153 ? 40.775 -26.213 -11.333 1.00 14.92 ?  153 LEU   B H    1 
ATOM   6792 H HA   . LEU   B 1 153 ? 42.087 -25.887 -9.011  1.00 14.84 ?  153 LEU   B HA   1 
ATOM   6793 H HB2  . LEU   B 1 153 ? 40.509 -28.044 -9.925  1.00 15.40 ?  153 LEU   B HB2  1 
ATOM   6794 H HB3  . LEU   B 1 153 ? 41.172 -28.001 -8.486  1.00 15.40 ?  153 LEU   B HB3  1 
ATOM   6795 H HG   . LEU   B 1 153 ? 39.221 -26.124 -9.257  1.00 16.67 ?  153 LEU   B HG   1 
ATOM   6796 H HD11 . LEU   B 1 153 ? 37.623 -27.405 -8.167  1.00 17.79 ?  153 LEU   B HD11 1 
ATOM   6797 H HD12 . LEU   B 1 153 ? 38.257 -28.244 -9.357  1.00 17.79 ?  153 LEU   B HD12 1 
ATOM   6798 H HD13 . LEU   B 1 153 ? 38.713 -28.518 -7.860  1.00 17.79 ?  153 LEU   B HD13 1 
ATOM   6799 H HD21 . LEU   B 1 153 ? 38.995 -25.751 -6.944  1.00 16.79 ?  153 LEU   B HD21 1 
ATOM   6800 H HD22 . LEU   B 1 153 ? 40.166 -26.790 -6.676  1.00 16.79 ?  153 LEU   B HD22 1 
ATOM   6801 H HD23 . LEU   B 1 153 ? 40.473 -25.425 -7.429  1.00 16.79 ?  153 LEU   B HD23 1 
ATOM   6802 N N    . ALA   B 1 154 ? 44.133 -27.202 -9.313  1.00 12.63 ?  154 ALA   B N    1 
ATOM   6803 C CA   . ALA   B 1 154 ? 45.356 -27.978 -9.494  1.00 13.79 ?  154 ALA   B CA   1 
ATOM   6804 C C    . ALA   B 1 154 ? 45.422 -29.056 -8.416  1.00 14.32 ?  154 ALA   B C    1 
ATOM   6805 O O    . ALA   B 1 154 ? 45.384 -28.752 -7.217  1.00 16.31 ?  154 ALA   B O    1 
ATOM   6806 C CB   . ALA   B 1 154 ? 46.591 -27.081 -9.438  1.00 14.91 ?  154 ALA   B CB   1 
ATOM   6807 H H    . ALA   B 1 154 ? 44.158 -26.662 -8.639  1.00 15.16 ?  154 ALA   B H    1 
ATOM   6808 H HA   . ALA   B 1 154 ? 45.328 -28.407 -10.360 1.00 16.54 ?  154 ALA   B HA   1 
ATOM   6809 H HB1  . ALA   B 1 154 ? 47.380 -27.629 -9.563  1.00 17.89 ?  154 ALA   B HB1  1 
ATOM   6810 H HB2  . ALA   B 1 154 ? 46.535 -26.417 -10.145 1.00 17.89 ?  154 ALA   B HB2  1 
ATOM   6811 H HB3  . ALA   B 1 154 ? 46.625 -26.640 -8.575  1.00 17.89 ?  154 ALA   B HB3  1 
ATOM   6812 N N    . VAL   B 1 155 ? 45.525 -30.309 -8.847  1.00 13.58 ?  155 VAL   B N    1 
ATOM   6813 C CA   . VAL   B 1 155 ? 45.638 -31.460 -7.954  1.00 14.66 ?  155 VAL   B CA   1 
ATOM   6814 C C    . VAL   B 1 155 ? 46.977 -32.133 -8.236  1.00 14.25 ?  155 VAL   B C    1 
ATOM   6815 O O    . VAL   B 1 155 ? 47.209 -32.622 -9.348  1.00 15.79 ?  155 VAL   B O    1 
ATOM   6816 C CB   . VAL   B 1 155 ? 44.475 -32.448 -8.145  1.00 15.90 ?  155 VAL   B CB   1 
ATOM   6817 C CG1  . VAL   B 1 155 ? 44.648 -33.644 -7.230  1.00 16.41 ?  155 VAL   B CG1  1 
ATOM   6818 C CG2  . VAL   B 1 155 ? 43.132 -31.753 -7.893  1.00 16.65 ?  155 VAL   B CG2  1 
ATOM   6819 H H    . VAL   B 1 155 ? 45.548 -30.524 -9.683  1.00 16.30 ?  155 VAL   B H    1 
ATOM   6820 H HA   . VAL   B 1 155 ? 45.634 -31.157 -7.037  1.00 17.60 ?  155 VAL   B HA   1 
ATOM   6821 H HB   . VAL   B 1 155 ? 44.476 -32.766 -9.063  1.00 19.08 ?  155 VAL   B HB   1 
ATOM   6822 H HG11 . VAL   B 1 155 ? 43.820 -34.150 -7.206  1.00 19.69 ?  155 VAL   B HG11 1 
ATOM   6823 H HG12 . VAL   B 1 155 ? 45.365 -34.207 -7.568  1.00 19.69 ?  155 VAL   B HG12 1 
ATOM   6824 H HG13 . VAL   B 1 155 ? 44.867 -33.333 -6.337  1.00 19.69 ?  155 VAL   B HG13 1 
ATOM   6825 H HG21 . VAL   B 1 155 ? 42.415 -32.403 -7.979  1.00 19.98 ?  155 VAL   B HG21 1 
ATOM   6826 H HG22 . VAL   B 1 155 ? 43.130 -31.380 -6.996  1.00 19.98 ?  155 VAL   B HG22 1 
ATOM   6827 H HG23 . VAL   B 1 155 ? 43.010 -31.042 -8.543  1.00 19.98 ?  155 VAL   B HG23 1 
ATOM   6828 N N    . PHE   B 1 156 ? 47.853 -32.158 -7.228  1.00 14.89 ?  156 PHE   B N    1 
ATOM   6829 C CA   . PHE   B 1 156 ? 49.228 -32.625 -7.429  1.00 15.81 ?  156 PHE   B CA   1 
ATOM   6830 C C    . PHE   B 1 156 ? 49.312 -34.127 -7.706  1.00 17.18 ?  156 PHE   B C    1 
ATOM   6831 O O    . PHE   B 1 156 ? 50.026 -34.560 -8.622  1.00 18.90 ?  156 PHE   B O    1 
ATOM   6832 C CB   . PHE   B 1 156 ? 50.064 -32.261 -6.207  1.00 15.87 ?  156 PHE   B CB   1 
ATOM   6833 C CG   . PHE   B 1 156 ? 51.490 -32.731 -6.279  1.00 16.72 ?  156 PHE   B CG   1 
ATOM   6834 C CD1  . PHE   B 1 156 ? 52.365 -32.195 -7.207  1.00 18.00 ?  156 PHE   B CD1  1 
ATOM   6835 C CD2  . PHE   B 1 156 ? 51.957 -33.694 -5.408  1.00 17.27 ?  156 PHE   B CD2  1 
ATOM   6836 C CE1  . PHE   B 1 156 ? 53.694 -32.616 -7.268  1.00 18.94 ?  156 PHE   B CE1  1 
ATOM   6837 C CE2  . PHE   B 1 156 ? 53.280 -34.118 -5.465  1.00 18.51 ?  156 PHE   B CE2  1 
ATOM   6838 C CZ   . PHE   B 1 156 ? 54.141 -33.575 -6.401  1.00 18.94 ?  156 PHE   B CZ   1 
ATOM   6839 H H    . PHE   B 1 156 ? 47.672 -31.914 -6.420  1.00 17.87 ?  156 PHE   B H    1 
ATOM   6840 H HA   . PHE   B 1 156 ? 49.600 -32.164 -8.189  1.00 18.97 ?  156 PHE   B HA   1 
ATOM   6841 H HB2  . PHE   B 1 156 ? 50.071 -31.296 -6.117  1.00 19.05 ?  156 PHE   B HB2  1 
ATOM   6842 H HB3  . PHE   B 1 156 ? 49.660 -32.660 -5.419  1.00 19.05 ?  156 PHE   B HB3  1 
ATOM   6843 H HD1  . PHE   B 1 156 ? 52.064 -31.535 -7.798  1.00 21.61 ?  156 PHE   B HD1  1 
ATOM   6844 H HD2  . PHE   B 1 156 ? 51.383 -34.064 -4.778  1.00 20.72 ?  156 PHE   B HD2  1 
ATOM   6845 H HE1  . PHE   B 1 156 ? 54.273 -32.245 -7.901  1.00 22.73 ?  156 PHE   B HE1  1 
ATOM   6846 H HE2  . PHE   B 1 156 ? 53.584 -34.773 -4.879  1.00 22.21 ?  156 PHE   B HE2  1 
ATOM   6847 H HZ   . PHE   B 1 156 ? 55.024 -33.861 -6.442  1.00 22.73 ?  156 PHE   B HZ   1 
ATOM   6848 N N    . ASP   B 1 157 ? 48.651 -34.945 -6.895  1.00 18.36 ?  157 ASP   B N    1 
ATOM   6849 C CA   . ASP   B 1 157 ? 48.793 -36.395 -6.995  1.00 19.56 ?  157 ASP   B CA   1 
ATOM   6850 C C    . ASP   B 1 157 ? 47.877 -36.947 -8.085  1.00 19.38 ?  157 ASP   B C    1 
ATOM   6851 O O    . ASP   B 1 157 ? 46.654 -36.815 -7.994  1.00 18.78 ?  157 ASP   B O    1 
ATOM   6852 C CB   . ASP   B 1 157 ? 48.440 -37.003 -5.644  1.00 21.77 ?  157 ASP   B CB   1 
ATOM   6853 C CG   . ASP   B 1 157 ? 48.579 -38.506 -5.624  1.00 25.48 ?  157 ASP   B CG   1 
ATOM   6854 O OD1  . ASP   B 1 157 ? 48.946 -39.101 -6.663  1.00 26.34 ?  157 ASP   B OD1  1 
ATOM   6855 O OD2  . ASP   B 1 157 ? 48.322 -39.092 -4.555  1.00 27.84 -1 157 ASP   B OD2  1 
ATOM   6856 H H    . ASP   B 1 157 ? 48.126 -34.686 -6.270  1.00 22.03 ?  157 ASP   B H    1 
ATOM   6857 H HA   . ASP   B 1 157 ? 49.715 -36.627 -7.209  1.00 23.47 ?  157 ASP   B HA   1 
ATOM   6858 H HB2  . ASP   B 1 157 ? 49.015 -36.624 -4.961  1.00 26.12 ?  157 ASP   B HB2  1 
ATOM   6859 H HB3  . ASP   B 1 157 ? 47.515 -36.798 -5.441  1.00 26.12 ?  157 ASP   B HB3  1 
ATOM   6860 N N    A LYS   B 1 158 ? 48.469 -37.598 -9.092  0.52 20.31 ?  158 LYS   B N    1 
ATOM   6861 N N    B LYS   B 1 158 ? 48.469 -37.589 -9.098  0.48 20.55 ?  158 LYS   B N    1 
ATOM   6862 C CA   A LYS   B 1 158 ? 47.687 -38.197 -10.175 0.52 21.48 ?  158 LYS   B CA   1 
ATOM   6863 C CA   B LYS   B 1 158 ? 47.686 -38.151 -10.198 0.48 21.96 ?  158 LYS   B CA   1 
ATOM   6864 C C    A LYS   B 1 158 ? 46.630 -39.164 -9.643  0.52 21.39 ?  158 LYS   B C    1 
ATOM   6865 C C    B LYS   B 1 158 ? 46.633 -39.136 -9.699  0.48 22.02 ?  158 LYS   B C    1 
ATOM   6866 O O    A LYS   B 1 158 ? 45.519 -39.244 -10.184 0.52 21.49 ?  158 LYS   B O    1 
ATOM   6867 O O    B LYS   B 1 158 ? 45.541 -39.226 -10.275 0.48 22.28 ?  158 LYS   B O    1 
ATOM   6868 C CB   A LYS   B 1 158 ? 48.629 -38.903 -11.156 0.52 23.11 ?  158 LYS   B CB   1 
ATOM   6869 C CB   B LYS   B 1 158 ? 48.624 -38.828 -11.204 0.48 23.59 ?  158 LYS   B CB   1 
ATOM   6870 C CG   A LYS   B 1 158 ? 47.950 -39.828 -12.157 0.52 25.37 ?  158 LYS   B CG   1 
ATOM   6871 C CG   B LYS   B 1 158 ? 47.945 -39.749 -12.213 0.48 25.62 ?  158 LYS   B CG   1 
ATOM   6872 C CD   A LYS   B 1 158 ? 47.081 -39.069 -13.138 0.52 27.71 ?  158 LYS   B CD   1 
ATOM   6873 C CD   B LYS   B 1 158 ? 47.056 -38.992 -13.181 0.48 27.88 ?  158 LYS   B CD   1 
ATOM   6874 C CE   A LYS   B 1 158 ? 46.495 -40.010 -14.177 0.52 29.19 ?  158 LYS   B CE   1 
ATOM   6875 C CE   B LYS   B 1 158 ? 46.475 -39.931 -14.232 0.48 29.28 ?  158 LYS   B CE   1 
ATOM   6876 N NZ   A LYS   B 1 158 ? 45.442 -39.352 -14.999 0.52 29.60 ?  158 LYS   B NZ   1 
ATOM   6877 N NZ   B LYS   B 1 158 ? 45.419 -39.274 -15.054 0.48 29.77 ?  158 LYS   B NZ   1 
ATOM   6878 H H    A LYS   B 1 158 ? 49.320 -37.709 -9.165  0.52 24.37 ?  158 LYS   B H    1 
ATOM   6879 H H    B LYS   B 1 158 ? 49.316 -37.722 -9.161  0.48 24.66 ?  158 LYS   B H    1 
ATOM   6880 H HA   A LYS   B 1 158 ? 47.234 -37.489 -10.660 0.52 25.78 ?  158 LYS   B HA   1 
ATOM   6881 H HA   B LYS   B 1 158 ? 47.234 -37.427 -10.659 0.48 26.35 ?  158 LYS   B HA   1 
ATOM   6882 H HB2  A LYS   B 1 158 ? 49.108 -38.227 -11.667 0.52 27.73 ?  158 LYS   B HB2  1 
ATOM   6883 H HB2  B LYS   B 1 158 ? 49.086 -38.136 -11.707 0.48 28.30 ?  158 LYS   B HB2  1 
ATOM   6884 H HB3  A LYS   B 1 158 ? 49.264 -39.433 -10.651 0.52 27.73 ?  158 LYS   B HB3  1 
ATOM   6885 H HB3  B LYS   B 1 158 ? 49.271 -39.357 -10.714 0.48 28.30 ?  158 LYS   B HB3  1 
ATOM   6886 H HG2  A LYS   B 1 158 ? 48.633 -40.291 -12.666 0.52 30.44 ?  158 LYS   B HG2  1 
ATOM   6887 H HG2  B LYS   B 1 158 ? 48.631 -40.195 -12.733 0.48 30.74 ?  158 LYS   B HG2  1 
ATOM   6888 H HG3  A LYS   B 1 158 ? 47.397 -40.477 -11.693 0.52 30.44 ?  158 LYS   B HG3  1 
ATOM   6889 H HG3  B LYS   B 1 158 ? 47.406 -40.411 -11.753 0.48 30.74 ?  158 LYS   B HG3  1 
ATOM   6890 H HD2  A LYS   B 1 158 ? 46.351 -38.644 -12.663 0.52 33.26 ?  158 LYS   B HD2  1 
ATOM   6891 H HD2  B LYS   B 1 158 ? 46.323 -38.586 -12.695 0.48 33.46 ?  158 LYS   B HD2  1 
ATOM   6892 H HD3  A LYS   B 1 158 ? 47.619 -38.404 -13.597 0.52 33.26 ?  158 LYS   B HD3  1 
ATOM   6893 H HD3  B LYS   B 1 158 ? 47.580 -38.313 -13.634 0.48 33.46 ?  158 LYS   B HD3  1 
ATOM   6894 H HE2  A LYS   B 1 158 ? 47.200 -40.306 -14.773 0.52 35.03 ?  158 LYS   B HE2  1 
ATOM   6895 H HE2  B LYS   B 1 158 ? 47.184 -40.220 -14.828 0.48 35.13 ?  158 LYS   B HE2  1 
ATOM   6896 H HE3  A LYS   B 1 158 ? 46.096 -40.773 -13.729 0.52 35.03 ?  158 LYS   B HE3  1 
ATOM   6897 H HE3  B LYS   B 1 158 ? 46.080 -40.699 -13.790 0.48 35.13 ?  158 LYS   B HE3  1 
ATOM   6898 H HZ1  A LYS   B 1 158 ? 45.118 -39.926 -15.596 0.52 35.52 ?  158 LYS   B HZ1  1 
ATOM   6899 H HZ1  B LYS   B 1 158 ? 45.101 -39.847 -15.656 0.48 35.73 ?  158 LYS   B HZ1  1 
ATOM   6900 H HZ2  A LYS   B 1 158 ? 44.778 -39.072 -14.476 0.52 35.52 ?  158 LYS   B HZ2  1 
ATOM   6901 H HZ2  B LYS   B 1 158 ? 44.751 -39.004 -14.531 0.48 35.73 ?  158 LYS   B HZ2  1 
ATOM   6902 H HZ3  A LYS   B 1 158 ? 45.786 -38.651 -15.428 0.52 35.52 ?  158 LYS   B HZ3  1 
ATOM   6903 H HZ3  B LYS   B 1 158 ? 45.759 -38.569 -15.477 0.48 35.73 ?  158 LYS   B HZ3  1 
ATOM   6904 N N    A ASN   B 1 159 ? 46.956 -39.918 -8.593  0.52 21.67 ?  159 ASN   B N    1 
ATOM   6905 N N    B ASN   B 1 159 ? 46.939 -39.888 -8.642  0.48 22.18 ?  159 ASN   B N    1 
ATOM   6906 C CA   A ASN   B 1 159 ? 45.998 -40.893 -8.078  0.52 22.51 ?  159 ASN   B CA   1 
ATOM   6907 C CA   B ASN   B 1 159 ? 45.978 -40.865 -8.140  0.48 22.73 ?  159 ASN   B CA   1 
ATOM   6908 C C    A ASN   B 1 159 ? 44.799 -40.205 -7.421  0.52 21.11 ?  159 ASN   B C    1 
ATOM   6909 C C    B ASN   B 1 159 ? 44.794 -40.194 -7.441  0.48 21.32 ?  159 ASN   B C    1 
ATOM   6910 O O    A ASN   B 1 159 ? 43.661 -40.686 -7.527  0.52 20.90 ?  159 ASN   B O    1 
ATOM   6911 O O    B ASN   B 1 159 ? 43.660 -40.682 -7.536  0.48 21.15 ?  159 ASN   B O    1 
ATOM   6912 C CB   A ASN   B 1 159 ? 46.697 -41.856 -7.119  0.52 24.60 ?  159 ASN   B CB   1 
ATOM   6913 C CB   B ASN   B 1 159 ? 46.684 -41.872 -7.231  0.48 24.40 ?  159 ASN   B CB   1 
ATOM   6914 C CG   A ASN   B 1 159 ? 47.706 -42.746 -7.821  0.52 26.72 ?  159 ASN   B CG   1 
ATOM   6915 C CG   B ASN   B 1 159 ? 47.685 -42.732 -7.983  0.48 26.34 ?  159 ASN   B CG   1 
ATOM   6916 O OD1  A ASN   B 1 159 ? 47.447 -43.259 -8.915  0.52 27.54 ?  159 ASN   B OD1  1 
ATOM   6917 O OD1  B ASN   B 1 159 ? 47.416 -43.185 -9.100  0.48 26.84 ?  159 ASN   B OD1  1 
ATOM   6918 N ND2  A ASN   B 1 159 ? 48.864 -42.936 -7.195  0.52 27.40 ?  159 ASN   B ND2  1 
ATOM   6919 N ND2  B ASN   B 1 159 ? 48.848 -42.960 -7.377  0.48 26.92 ?  159 ASN   B ND2  1 
ATOM   6920 H H    A ASN   B 1 159 ? 47.706 -39.885 -8.178  0.52 26.00 ?  159 ASN   B H    1 
ATOM   6921 H H    B ASN   B 1 159 ? 47.684 -39.851 -8.218  0.48 26.62 ?  159 ASN   B H    1 
ATOM   6922 H HA   A ASN   B 1 159 ? 45.665 -41.416 -8.825  0.52 27.01 ?  159 ASN   B HA   1 
ATOM   6923 H HA   B ASN   B 1 159 ? 45.627 -41.358 -8.899  0.48 27.27 ?  159 ASN   B HA   1 
ATOM   6924 H HB2  A ASN   B 1 159 ? 47.165 -41.343 -6.442  0.52 29.52 ?  159 ASN   B HB2  1 
ATOM   6925 H HB2  B ASN   B 1 159 ? 47.162 -41.393 -6.538  0.48 29.28 ?  159 ASN   B HB2  1 
ATOM   6926 H HB3  A ASN   B 1 159 ? 46.033 -42.427 -6.712  0.52 29.52 ?  159 ASN   B HB3  1 
ATOM   6927 H HB3  B ASN   B 1 159 ? 46.023 -42.460 -6.840  0.48 29.28 ?  159 ASN   B HB3  1 
ATOM   6928 H HD21 A ASN   B 1 159 ? 49.471 -43.431 -7.553  0.52 32.88 ?  159 ASN   B HD21 1 
ATOM   6929 H HD21 B ASN   B 1 159 ? 49.452 -43.440 -7.761  0.48 32.31 ?  159 ASN   B HD21 1 
ATOM   6930 H HD22 A ASN   B 1 159 ? 49.004 -42.574 -6.428  0.52 32.88 ?  159 ASN   B HD22 1 
ATOM   6931 H HD22 B ASN   B 1 159 ? 48.997 -42.635 -6.594  0.48 32.31 ?  159 ASN   B HD22 1 
ATOM   6932 N N    . LEU   B 1 160 ? 45.023 -39.074 -6.750  1.00 20.98 ?  160 LEU   B N    1 
ATOM   6933 C CA   . LEU   B 1 160 ? 43.899 -38.335 -6.183  1.00 19.78 ?  160 LEU   B CA   1 
ATOM   6934 C C    . LEU   B 1 160 ? 43.097 -37.661 -7.285  1.00 18.29 ?  160 LEU   B C    1 
ATOM   6935 O O    . LEU   B 1 160 ? 41.858 -37.650 -7.244  1.00 17.95 ?  160 LEU   B O    1 
ATOM   6936 C CB   . LEU   B 1 160 ? 44.379 -37.307 -5.157  1.00 18.83 ?  160 LEU   B CB   1 
ATOM   6937 C CG   . LEU   B 1 160 ? 43.246 -36.405 -4.635  1.00 18.41 ?  160 LEU   B CG   1 
ATOM   6938 C CD1  . LEU   B 1 160 ? 42.130 -37.238 -4.007  1.00 19.97 ?  160 LEU   B CD1  1 
ATOM   6939 C CD2  . LEU   B 1 160 ? 43.776 -35.372 -3.647  1.00 18.37 ?  160 LEU   B CD2  1 
ATOM   6940 H H    A LEU   B 1 160 ? 45.797 -38.726 -6.617  0.52 25.17 ?  160 LEU   B H    1 
ATOM   6941 H H    B LEU   B 1 160 ? 45.798 -38.734 -6.607  0.48 25.17 ?  160 LEU   B H    1 
ATOM   6942 H HA   . LEU   B 1 160 ? 43.316 -38.965 -5.731  1.00 23.74 ?  160 LEU   B HA   1 
ATOM   6943 H HB2  . LEU   B 1 160 ? 44.768 -37.781 -4.401  1.00 22.59 ?  160 LEU   B HB2  1 
ATOM   6944 H HB3  . LEU   B 1 160 ? 45.055 -36.746 -5.573  1.00 22.59 ?  160 LEU   B HB3  1 
ATOM   6945 H HG   . LEU   B 1 160 ? 42.869 -35.921 -5.384  1.00 22.09 ?  160 LEU   B HG   1 
ATOM   6946 H HD11 . LEU   B 1 160 ? 41.512 -36.643 -3.560  1.00 23.97 ?  160 LEU   B HD11 1 
ATOM   6947 H HD12 . LEU   B 1 160 ? 41.668 -37.733 -4.704  1.00 23.97 ?  160 LEU   B HD12 1 
ATOM   6948 H HD13 . LEU   B 1 160 ? 42.518 -37.857 -3.366  1.00 23.97 ?  160 LEU   B HD13 1 
ATOM   6949 H HD21 . LEU   B 1 160 ? 43.043 -34.804 -3.368  1.00 22.04 ?  160 LEU   B HD21 1 
ATOM   6950 H HD22 . LEU   B 1 160 ? 44.155 -35.829 -2.882  1.00 22.04 ?  160 LEU   B HD22 1 
ATOM   6951 H HD23 . LEU   B 1 160 ? 44.461 -34.837 -4.085  1.00 22.04 ?  160 LEU   B HD23 1 
ATOM   6952 N N    . TYR   B 1 161 ? 43.788 -37.098 -8.283  1.00 19.06 ?  161 TYR   B N    1 
ATOM   6953 C CA   . TYR   B 1 161 ? 43.109 -36.530 -9.443  1.00 18.76 ?  161 TYR   B CA   1 
ATOM   6954 C C    . TYR   B 1 161 ? 42.154 -37.550 -10.052 1.00 18.39 ?  161 TYR   B C    1 
ATOM   6955 O O    . TYR   B 1 161 ? 40.980 -37.254 -10.301 1.00 17.65 ?  161 TYR   B O    1 
ATOM   6956 C CB   . TYR   B 1 161 ? 44.148 -36.062 -10.478 1.00 19.62 ?  161 TYR   B CB   1 
ATOM   6957 C CG   . TYR   B 1 161 ? 43.560 -35.590 -11.796 1.00 20.26 ?  161 TYR   B CG   1 
ATOM   6958 C CD1  . TYR   B 1 161 ? 43.170 -34.265 -11.966 1.00 19.93 ?  161 TYR   B CD1  1 
ATOM   6959 C CD2  . TYR   B 1 161 ? 43.388 -36.465 -12.867 1.00 20.55 ?  161 TYR   B CD2  1 
ATOM   6960 C CE1  . TYR   B 1 161 ? 42.627 -33.823 -13.158 1.00 20.91 ?  161 TYR   B CE1  1 
ATOM   6961 C CE2  . TYR   B 1 161 ? 42.841 -36.038 -14.061 1.00 21.94 ?  161 TYR   B CE2  1 
ATOM   6962 C CZ   . TYR   B 1 161 ? 42.461 -34.715 -14.201 1.00 21.62 ?  161 TYR   B CZ   1 
ATOM   6963 O OH   . TYR   B 1 161 ? 41.915 -34.280 -15.385 1.00 24.04 ?  161 TYR   B OH   1 
ATOM   6964 H H    . TYR   B 1 161 ? 44.645 -37.034 -8.309  1.00 22.87 ?  161 TYR   B H    1 
ATOM   6965 H HA   . TYR   B 1 161 ? 42.592 -35.759 -9.164  1.00 22.51 ?  161 TYR   B HA   1 
ATOM   6966 H HB2  . TYR   B 1 161 ? 44.648 -35.322 -10.103 1.00 23.54 ?  161 TYR   B HB2  1 
ATOM   6967 H HB3  . TYR   B 1 161 ? 44.745 -36.797 -10.675 1.00 23.54 ?  161 TYR   B HB3  1 
ATOM   6968 H HD1  . TYR   B 1 161 ? 43.273 -33.660 -11.268 1.00 23.91 ?  161 TYR   B HD1  1 
ATOM   6969 H HD2  . TYR   B 1 161 ? 43.630 -37.356 -12.778 1.00 24.66 ?  161 TYR   B HD2  1 
ATOM   6970 H HE1  . TYR   B 1 161 ? 42.364 -32.932 -13.254 1.00 25.09 ?  161 TYR   B HE1  1 
ATOM   6971 H HE2  . TYR   B 1 161 ? 42.721 -36.634 -14.768 1.00 26.33 ?  161 TYR   B HE2  1 
ATOM   6972 H HH   . TYR   B 1 161 ? 41.865 -34.916 -15.936 1.00 28.85 ?  161 TYR   B HH   1 
ATOM   6973 N N    . ASP   B 1 162 ? 42.638 -38.774 -10.270 1.00 19.22 ?  162 ASP   B N    1 
ATOM   6974 C CA   . ASP   B 1 162 ? 41.808 -39.797 -10.892 1.00 19.43 ?  162 ASP   B CA   1 
ATOM   6975 C C    . ASP   B 1 162 ? 40.606 -40.138 -10.022 1.00 18.61 ?  162 ASP   B C    1 
ATOM   6976 O O    . ASP   B 1 162 ? 39.499 -40.341 -10.531 1.00 19.22 ?  162 ASP   B O    1 
ATOM   6977 C CB   . ASP   B 1 162 ? 42.633 -41.061 -11.142 1.00 21.04 ?  162 ASP   B CB   1 
ATOM   6978 C CG   . ASP   B 1 162 ? 43.636 -40.908 -12.277 1.00 23.02 ?  162 ASP   B CG   1 
ATOM   6979 O OD1  . ASP   B 1 162 ? 43.498 -39.981 -13.097 1.00 23.23 ?  162 ASP   B OD1  1 
ATOM   6980 O OD2  . ASP   B 1 162 ? 44.550 -41.757 -12.373 1.00 24.51 -1 162 ASP   B OD2  1 
ATOM   6981 H H    . ASP   B 1 162 ? 43.436 -39.029 -10.075 1.00 23.07 ?  162 ASP   B H    1 
ATOM   6982 H HA   . ASP   B 1 162 ? 41.483 -39.476 -11.747 1.00 23.32 ?  162 ASP   B HA   1 
ATOM   6983 H HB2  . ASP   B 1 162 ? 43.131 -41.283 -10.340 1.00 25.25 ?  162 ASP   B HB2  1 
ATOM   6984 H HB3  . ASP   B 1 162 ? 42.036 -41.793 -11.372 1.00 25.25 ?  162 ASP   B HB3  1 
ATOM   6985 N N    A LYS   B 1 163 ? 40.808 -40.227 -8.706  0.52 18.22 ?  163 LYS   B N    1 
ATOM   6986 N N    B LYS   B 1 163 ? 40.806 -40.216 -8.704  0.48 18.26 ?  163 LYS   B N    1 
ATOM   6987 C CA   A LYS   B 1 163 ? 39.687 -40.499 -7.814  0.52 18.93 ?  163 LYS   B CA   1 
ATOM   6988 C CA   B LYS   B 1 163 ? 39.691 -40.497 -7.807  0.48 18.94 ?  163 LYS   B CA   1 
ATOM   6989 C C    A LYS   B 1 163 ? 38.654 -39.378 -7.875  0.52 17.51 ?  163 LYS   B C    1 
ATOM   6990 C C    B LYS   B 1 163 ? 38.657 -39.376 -7.844  0.48 17.47 ?  163 LYS   B C    1 
ATOM   6991 O O    A LYS   B 1 163 ? 37.441 -39.637 -7.875  0.52 17.98 ?  163 LYS   B O    1 
ATOM   6992 O O    B LYS   B 1 163 ? 37.445 -39.634 -7.792  0.48 17.86 ?  163 LYS   B O    1 
ATOM   6993 C CB   A LYS   B 1 163 ? 40.181 -40.687 -6.382  0.52 21.89 ?  163 LYS   B CB   1 
ATOM   6994 C CB   B LYS   B 1 163 ? 40.204 -40.695 -6.382  0.48 21.87 ?  163 LYS   B CB   1 
ATOM   6995 C CG   A LYS   B 1 163 ? 39.108 -41.234 -5.460  0.52 26.39 ?  163 LYS   B CG   1 
ATOM   6996 C CG   B LYS   B 1 163 ? 39.135 -41.193 -5.431  0.48 26.16 ?  163 LYS   B CG   1 
ATOM   6997 C CD   A LYS   B 1 163 ? 39.529 -41.247 -4.005  0.52 30.42 ?  163 LYS   B CD   1 
ATOM   6998 C CD   B LYS   B 1 163 ? 39.650 -41.365 -4.016  0.48 30.08 ?  163 LYS   B CD   1 
ATOM   6999 C CE   A LYS   B 1 163 ? 38.455 -41.910 -3.154  0.52 33.63 ?  163 LYS   B CE   1 
ATOM   7000 C CE   B LYS   B 1 163 ? 38.584 -42.010 -3.142  0.48 33.23 ?  163 LYS   B CE   1 
ATOM   7001 N NZ   A LYS   B 1 163 ? 38.560 -41.550 -1.715  0.52 34.85 ?  163 LYS   B NZ   1 
ATOM   7002 N NZ   B LYS   B 1 163 ? 38.840 -41.818 -1.689  0.48 34.32 ?  163 LYS   B NZ   1 
ATOM   7003 H H    A LYS   B 1 163 ? 41.572 -40.142 -8.317  0.52 21.86 ?  163 LYS   B H    1 
ATOM   7004 H H    B LYS   B 1 163 ? 41.567 -40.117 -8.315  0.48 21.92 ?  163 LYS   B H    1 
ATOM   7005 H HA   A LYS   B 1 163 ? 39.254 -41.319 -8.092  0.52 22.72 ?  163 LYS   B HA   1 
ATOM   7006 H HA   B LYS   B 1 163 ? 39.256 -41.316 -8.088  0.48 22.73 ?  163 LYS   B HA   1 
ATOM   7007 H HB2  A LYS   B 1 163 ? 40.924 -41.315 -6.382  0.52 26.27 ?  163 LYS   B HB2  1 
ATOM   7008 H HB2  B LYS   B 1 163 ? 40.922 -41.350 -6.392  0.48 26.24 ?  163 LYS   B HB2  1 
ATOM   7009 H HB3  A LYS   B 1 163 ? 40.473 -39.833 -6.030  0.52 26.27 ?  163 LYS   B HB3  1 
ATOM   7010 H HB3  B LYS   B 1 163 ? 40.535 -39.850 -6.043  0.48 26.24 ?  163 LYS   B HB3  1 
ATOM   7011 H HG2  A LYS   B 1 163 ? 38.314 -40.683 -5.534  0.52 31.67 ?  163 LYS   B HG2  1 
ATOM   7012 H HG2  B LYS   B 1 163 ? 38.406 -40.554 -5.409  0.48 31.39 ?  163 LYS   B HG2  1 
ATOM   7013 H HG3  A LYS   B 1 163 ? 38.903 -42.147 -5.720  0.52 31.67 ?  163 LYS   B HG3  1 
ATOM   7014 H HG3  B LYS   B 1 163 ? 38.813 -42.055 -5.741  0.48 31.39 ?  163 LYS   B HG3  1 
ATOM   7015 H HD2  A LYS   B 1 163 ? 40.352 -41.754 -3.910  0.52 36.50 ?  163 LYS   B HD2  1 
ATOM   7016 H HD2  B LYS   B 1 163 ? 40.432 -41.940 -4.024  0.48 36.10 ?  163 LYS   B HD2  1 
ATOM   7017 H HD3  A LYS   B 1 163 ? 39.652 -40.337 -3.694  0.52 36.50 ?  163 LYS   B HD3  1 
ATOM   7018 H HD3  B LYS   B 1 163 ? 39.869 -40.497 -3.645  0.48 36.10 ?  163 LYS   B HD3  1 
ATOM   7019 H HE2  A LYS   B 1 163 ? 37.580 -41.643 -3.475  0.52 40.36 ?  163 LYS   B HE2  1 
ATOM   7020 H HE2  B LYS   B 1 163 ? 37.721 -41.620 -3.353  0.48 39.87 ?  163 LYS   B HE2  1 
ATOM   7021 H HE3  A LYS   B 1 163 ? 38.549 -42.872 -3.228  0.52 40.36 ?  163 LYS   B HE3  1 
ATOM   7022 H HE3  B LYS   B 1 163 ? 38.566 -42.964 -3.320  0.48 39.87 ?  163 LYS   B HE3  1 
ATOM   7023 H HZ1  A LYS   B 1 163 ? 37.915 -41.955 -1.254  0.52 41.82 ?  163 LYS   B HZ1  1 
ATOM   7024 H HZ1  B LYS   B 1 163 ? 38.196 -42.207 -1.213  0.48 41.18 ?  163 LYS   B HZ1  1 
ATOM   7025 H HZ2  A LYS   B 1 163 ? 39.349 -41.806 -1.396  0.52 41.82 ?  163 LYS   B HZ2  1 
ATOM   7026 H HZ2  B LYS   B 1 163 ? 39.622 -42.178 -1.468  0.48 41.18 ?  163 LYS   B HZ2  1 
ATOM   7027 H HZ3  A LYS   B 1 163 ? 38.478 -40.669 -1.616  0.52 41.82 ?  163 LYS   B HZ3  1 
ATOM   7028 H HZ3  B LYS   B 1 163 ? 38.856 -40.948 -1.496  0.48 41.18 ?  163 LYS   B HZ3  1 
ATOM   7029 N N    . LEU   B 1 164 ? 39.121 -38.123 -7.926  1.00 16.44 ?  164 LEU   B N    1 
ATOM   7030 C CA   . LEU   B 1 164 ? 38.211 -36.982 -7.971  1.00 16.14 ?  164 LEU   B CA   1 
ATOM   7031 C C    . LEU   B 1 164 ? 37.412 -36.966 -9.270  1.00 16.67 ?  164 LEU   B C    1 
ATOM   7032 O O    . LEU   B 1 164 ? 36.186 -36.767 -9.259  1.00 18.08 ?  164 LEU   B O    1 
ATOM   7033 C CB   . LEU   B 1 164 ? 39.012 -35.683 -7.807  1.00 14.82 ?  164 LEU   B CB   1 
ATOM   7034 C CG   . LEU   B 1 164 ? 39.555 -35.407 -6.406  1.00 16.03 ?  164 LEU   B CG   1 
ATOM   7035 C CD1  . LEU   B 1 164 ? 40.636 -34.342 -6.472  1.00 16.16 ?  164 LEU   B CD1  1 
ATOM   7036 C CD2  . LEU   B 1 164 ? 38.455 -34.955 -5.464  1.00 17.64 ?  164 LEU   B CD2  1 
ATOM   7037 H H    A LEU   B 1 164 ? 39.962 -37.911 -7.930  0.52 19.73 ?  164 LEU   B H    1 
ATOM   7038 H H    B LEU   B 1 164 ? 39.962 -37.912 -7.951  0.48 19.73 ?  164 LEU   B H    1 
ATOM   7039 H HA   . LEU   B 1 164 ? 37.593 -37.045 -7.236  1.00 19.37 ?  164 LEU   B HA   1 
ATOM   7040 H HB2  . LEU   B 1 164 ? 39.776 -35.711 -8.408  1.00 17.78 ?  164 LEU   B HB2  1 
ATOM   7041 H HB3  . LEU   B 1 164 ? 38.442 -34.940 -8.046  1.00 17.78 ?  164 LEU   B HB3  1 
ATOM   7042 H HG   . LEU   B 1 164 ? 39.951 -36.215 -6.048  1.00 19.24 ?  164 LEU   B HG   1 
ATOM   7043 H HD11 . LEU   B 1 164 ? 40.970 -34.163 -5.574  1.00 19.39 ?  164 LEU   B HD11 1 
ATOM   7044 H HD12 . LEU   B 1 164 ? 41.370 -34.659 -7.029  1.00 19.39 ?  164 LEU   B HD12 1 
ATOM   7045 H HD13 . LEU   B 1 164 ? 40.269 -33.527 -6.850  1.00 19.39 ?  164 LEU   B HD13 1 
ATOM   7046 H HD21 . LEU   B 1 164 ? 38.840 -34.746 -4.599  1.00 21.17 ?  164 LEU   B HD21 1 
ATOM   7047 H HD22 . LEU   B 1 164 ? 38.024 -34.167 -5.832  1.00 21.17 ?  164 LEU   B HD22 1 
ATOM   7048 H HD23 . LEU   B 1 164 ? 37.806 -35.671 -5.371  1.00 21.17 ?  164 LEU   B HD23 1 
ATOM   7049 N N    . VAL   B 1 165 ? 38.095 -37.141 -10.404 1.00 18.54 ?  165 VAL   B N    1 
ATOM   7050 C CA   . VAL   B 1 165 ? 37.419 -37.082 -11.696 1.00 20.02 ?  165 VAL   B CA   1 
ATOM   7051 C C    . VAL   B 1 165 ? 36.483 -38.274 -11.859 1.00 22.81 ?  165 VAL   B C    1 
ATOM   7052 O O    . VAL   B 1 165 ? 35.313 -38.129 -12.242 1.00 24.25 ?  165 VAL   B O    1 
ATOM   7053 C CB   . VAL   B 1 165 ? 38.446 -37.013 -12.842 1.00 21.27 ?  165 VAL   B CB   1 
ATOM   7054 C CG1  . VAL   B 1 165 ? 37.747 -37.103 -14.179 1.00 23.55 ?  165 VAL   B CG1  1 
ATOM   7055 C CG2  . VAL   B 1 165 ? 39.259 -35.735 -12.757 1.00 21.00 ?  165 VAL   B CG2  1 
ATOM   7056 H H    . VAL   B 1 165 ? 38.948 -37.293 -10.452 1.00 22.25 ?  165 VAL   B H    1 
ATOM   7057 H HA   . VAL   B 1 165 ? 36.892 -36.270 -11.733 1.00 24.02 ?  165 VAL   B HA   1 
ATOM   7058 H HB   . VAL   B 1 165 ? 39.065 -37.759 -12.768 1.00 25.52 ?  165 VAL   B HB   1 
ATOM   7059 H HG11 . VAL   B 1 165 ? 38.345 -36.792 -14.874 1.00 28.26 ?  165 VAL   B HG11 1 
ATOM   7060 H HG12 . VAL   B 1 165 ? 37.507 -38.028 -14.343 1.00 28.26 ?  165 VAL   B HG12 1 
ATOM   7061 H HG13 . VAL   B 1 165 ? 36.949 -36.553 -14.154 1.00 28.26 ?  165 VAL   B HG13 1 
ATOM   7062 H HG21 . VAL   B 1 165 ? 39.884 -35.701 -13.501 1.00 25.20 ?  165 VAL   B HG21 1 
ATOM   7063 H HG22 . VAL   B 1 165 ? 38.657 -34.973 -12.803 1.00 25.20 ?  165 VAL   B HG22 1 
ATOM   7064 H HG23 . VAL   B 1 165 ? 39.746 -35.717 -11.918 1.00 25.20 ?  165 VAL   B HG23 1 
ATOM   7065 N N    . SER   B 1 166 ? 36.995 -39.476 -11.572 1.00 24.30 ?  166 SER   B N    1 
ATOM   7066 C CA   . SER   B 1 166 ? 36.241 -40.688 -11.854 1.00 25.77 ?  166 SER   B CA   1 
ATOM   7067 C C    . SER   B 1 166 ? 34.986 -40.769 -11.000 1.00 25.71 ?  166 SER   B C    1 
ATOM   7068 O O    . SER   B 1 166 ? 34.011 -41.399 -11.408 1.00 27.51 ?  166 SER   B O    1 
ATOM   7069 C CB   . SER   B 1 166 ? 37.116 -41.941 -11.694 1.00 26.54 ?  166 SER   B CB   1 
ATOM   7070 O OG   . SER   B 1 166 ? 37.483 -42.181 -10.344 1.00 26.45 ?  166 SER   B OG   1 
ATOM   7071 H H    . SER   B 1 166 ? 37.777 -39.607 -11.222 1.00 29.15 ?  166 SER   B H    1 
ATOM   7072 H HA   . SER   B 1 166 ? 35.961 -40.652 -12.784 1.00 30.92 ?  166 SER   B HA   1 
ATOM   7073 H HB2  . SER   B 1 166 ? 36.620 -42.703 -12.029 1.00 31.85 ?  166 SER   B HB2  1 
ATOM   7074 H HB3  . SER   B 1 166 ? 37.926 -41.822 -12.215 1.00 31.85 ?  166 SER   B HB3  1 
ATOM   7075 H HG   . SER   B 1 166 ? 37.900 -41.521 -10.041 1.00 31.74 ?  166 SER   B HG   1 
ATOM   7076 N N    . SER   B 1 167 ? 34.972 -40.140 -9.829  1.00 24.04 ?  167 SER   B N    1 
ATOM   7077 C CA   . SER   B 1 167 ? 33.811 -40.180 -8.948  1.00 24.00 ?  167 SER   B CA   1 
ATOM   7078 C C    . SER   B 1 167 ? 32.910 -38.945 -9.044  1.00 22.91 ?  167 SER   B C    1 
ATOM   7079 O O    . SER   B 1 167 ? 31.827 -38.940 -8.443  1.00 22.93 ?  167 SER   B O    1 
ATOM   7080 C CB   . SER   B 1 167 ? 34.257 -40.384 -7.492  1.00 24.05 ?  167 SER   B CB   1 
ATOM   7081 O OG   . SER   B 1 167 ? 34.946 -39.235 -7.004  1.00 24.28 ?  167 SER   B OG   1 
ATOM   7082 H H    . SER   B 1 167 ? 35.632 -39.691 -9.522  1.00 28.85 ?  167 SER   B H    1 
ATOM   7083 H HA   . SER   B 1 167 ? 33.271 -40.950 -9.196  1.00 28.80 ?  167 SER   B HA   1 
ATOM   7084 H HB2  . SER   B 1 167 ? 33.466 -40.545 -6.948  1.00 28.86 ?  167 SER   B HB2  1 
ATOM   7085 H HB3  . SER   B 1 167 ? 34.837 -41.168 -7.452  1.00 28.86 ?  167 SER   B HB3  1 
ATOM   7086 H HG   . SER   B 1 167 ? 35.639 -39.119 -7.456  1.00 29.14 ?  167 SER   B HG   1 
ATOM   7087 N N    . PHE   B 1 168 ? 33.302 -37.910 -9.790  1.00 22.63 ?  168 PHE   B N    1 
ATOM   7088 C CA   . PHE   B 1 168 ? 32.468 -36.710 -9.873  1.00 20.69 ?  168 PHE   B CA   1 
ATOM   7089 C C    . PHE   B 1 168 ? 31.162 -36.993 -10.611 1.00 17.53 ?  168 PHE   B C    1 
ATOM   7090 O O    . PHE   B 1 168 ? 30.110 -36.404 -10.294 1.00 18.03 ?  168 PHE   B O    1 
ATOM   7091 C CB   . PHE   B 1 168 ? 33.238 -35.577 -10.557 1.00 21.86 ?  168 PHE   B CB   1 
ATOM   7092 C CG   . PHE   B 1 168 ? 32.417 -34.342 -10.765 1.00 21.16 ?  168 PHE   B CG   1 
ATOM   7093 C CD1  . PHE   B 1 168 ? 32.030 -33.567 -9.682  1.00 24.11 ?  168 PHE   B CD1  1 
ATOM   7094 C CD2  . PHE   B 1 168 ? 32.007 -33.962 -12.033 1.00 20.96 ?  168 PHE   B CD2  1 
ATOM   7095 C CE1  . PHE   B 1 168 ? 31.254 -32.440 -9.858  1.00 24.03 ?  168 PHE   B CE1  1 
ATOM   7096 C CE2  . PHE   B 1 168 ? 31.243 -32.822 -12.221 1.00 22.74 ?  168 PHE   B CE2  1 
ATOM   7097 C CZ   . PHE   B 1 168 ? 30.863 -32.057 -11.131 1.00 23.31 ?  168 PHE   B CZ   1 
ATOM   7098 H H    . PHE   B 1 168 ? 34.036 -37.878 -10.247 1.00 27.15 ?  168 PHE   B H    1 
ATOM   7099 H HA   . PHE   B 1 168 ? 32.249 -36.422 -8.978  1.00 24.83 ?  168 PHE   B HA   1 
ATOM   7100 H HB2  . PHE   B 1 168 ? 34.000 -35.335 -10.005 1.00 26.23 ?  168 PHE   B HB2  1 
ATOM   7101 H HB3  . PHE   B 1 168 ? 33.545 -35.877 -11.426 1.00 26.23 ?  168 PHE   B HB3  1 
ATOM   7102 H HD1  . PHE   B 1 168 ? 32.289 -33.819 -8.828  1.00 28.93 ?  168 PHE   B HD1  1 
ATOM   7103 H HD2  . PHE   B 1 168 ? 32.262 -34.470 -12.768 1.00 25.15 ?  168 PHE   B HD2  1 
ATOM   7104 H HE1  . PHE   B 1 168 ? 31.002 -31.927 -9.125  1.00 28.84 ?  168 PHE   B HE1  1 
ATOM   7105 H HE2  . PHE   B 1 168 ? 30.975 -32.578 -13.077 1.00 27.29 ?  168 PHE   B HE2  1 
ATOM   7106 H HZ   . PHE   B 1 168 ? 30.341 -31.299 -11.253 1.00 27.98 ?  168 PHE   B HZ   1 
ATOM   7107 N N    . LEU   B 1 169 ? 31.221 -37.860 -11.619 1.00 17.47 ?  169 LEU   B N    1 
ATOM   7108 C CA   . LEU   B 1 169 ? 30.057 -38.200 -12.431 1.00 20.51 ?  169 LEU   B CA   1 
ATOM   7109 C C    . LEU   B 1 169 ? 30.059 -39.641 -12.920 1.00 24.10 ?  169 LEU   B C    1 
ATOM   7110 O O    . LEU   B 1 169 ? 29.172 -40.051 -13.670 1.00 26.40 ?  169 LEU   B O    1 
ATOM   7111 C CB   . LEU   B 1 169 ? 29.989 -37.289 -13.653 1.00 23.06 ?  169 LEU   B CB   1 
ATOM   7112 C CG   . LEU   B 1 169 ? 28.761 -36.388 -13.775 1.00 26.39 ?  169 LEU   B CG   1 
ATOM   7113 C CD1  . LEU   B 1 169 ? 28.671 -35.847 -15.183 1.00 27.14 ?  169 LEU   B CD1  1 
ATOM   7114 C CD2  . LEU   B 1 169 ? 27.485 -37.119 -13.401 1.00 26.39 ?  169 LEU   B CD2  1 
ATOM   7115 O OXT  . LEU   B 1 169 ? 30.947 -40.413 -12.601 1.00 24.92 -1 169 LEU   B OXT  1 
ATOM   7116 H H    . LEU   B 1 169 ? 31.944 -38.257 -11.872 1.00 20.96 ?  169 LEU   B H    1 
ATOM   7117 H HA   . LEU   B 1 169 ? 29.271 -38.052 -11.890 1.00 24.61 ?  169 LEU   B HA   1 
ATOM   7118 H HB2  . LEU   B 1 169 ? 30.767 -36.708 -13.653 1.00 27.67 ?  169 LEU   B HB2  1 
ATOM   7119 H HB3  . LEU   B 1 169 ? 30.009 -37.845 -14.448 1.00 27.67 ?  169 LEU   B HB3  1 
ATOM   7120 H HG   . LEU   B 1 169 ? 28.860 -35.632 -13.174 1.00 31.67 ?  169 LEU   B HG   1 
ATOM   7121 H HD11 . LEU   B 1 169 ? 27.912 -35.246 -15.241 1.00 32.56 ?  169 LEU   B HD11 1 
ATOM   7122 H HD12 . LEU   B 1 169 ? 29.489 -35.371 -15.389 1.00 32.56 ?  169 LEU   B HD12 1 
ATOM   7123 H HD13 . LEU   B 1 169 ? 28.554 -36.589 -15.796 1.00 32.56 ?  169 LEU   B HD13 1 
ATOM   7124 H HD21 . LEU   B 1 169 ? 26.736 -36.701 -13.847 1.00 31.66 ?  169 LEU   B HD21 1 
ATOM   7125 H HD22 . LEU   B 1 169 ? 27.564 -38.047 -13.684 1.00 31.66 ?  169 LEU   B HD22 1 
ATOM   7126 H HD23 . LEU   B 1 169 ? 27.369 -37.078 -12.440 1.00 31.66 ?  169 LEU   B HD23 1 
HETATM 7127 C C1   T TFA   C 2 .   ? 12.108 -1.397  1.373   0.20 12.92 ?  201 TFA   A C1   1 
HETATM 7128 C C2   T TFA   C 2 .   ? 12.783 -1.746  0.020   0.20 15.22 ?  201 TFA   A C2   1 
HETATM 7129 O O    T TFA   C 2 .   ? 12.873 -1.510  2.337   0.20 12.74 ?  201 TFA   A O    1 
HETATM 7130 F F1   T TFA   C 2 .   ? 12.999 -3.073  -0.067  0.20 16.75 ?  201 TFA   A F1   1 
HETATM 7131 F F2   T TFA   C 2 .   ? 12.023 -1.434  -1.044  0.20 15.45 ?  201 TFA   A F2   1 
HETATM 7132 F F3   T TFA   C 2 .   ? 13.956 -1.122  -0.155  0.20 16.35 ?  201 TFA   A F3   1 
HETATM 7133 O OXT  T TFA   C 2 .   ? 10.919 -1.070  1.315   0.20 10.85 ?  201 TFA   A OXT  1 
HETATM 7134 N N2   B A1A8H D 3 .   ? 14.908 -0.171  3.740   0.24 11.89 ?  202 A1A8H A N2   1 
HETATM 7135 C C3   B A1A8H D 3 .   ? 14.129 0.259   -0.614  0.24 15.35 ?  202 A1A8H A C3   1 
HETATM 7136 C C6   B A1A8H D 3 .   ? 11.790 2.256   -1.489  0.24 15.35 ?  202 A1A8H A C6   1 
HETATM 7137 C C9   B A1A8H D 3 .   ? 15.063 0.998   3.032   0.24 11.81 ?  202 A1A8H A C9   1 
HETATM 7138 C C12  B A1A8H D 3 .   ? 15.300 2.216   3.778   0.24 10.87 ?  202 A1A8H A C12  1 
HETATM 7139 C C14  B A1A8H D 3 .   ? 15.689 4.258   4.815   0.24 9.98  ?  202 A1A8H A C14  1 
HETATM 7140 C C1   B A1A8H D 3 .   ? 16.002 -1.079  0.527   0.24 15.02 ?  202 A1A8H A C1   1 
HETATM 7141 C C10  B A1A8H D 3 .   ? 14.966 -0.164  5.127   0.24 11.10 ?  202 A1A8H A C10  1 
HETATM 7142 C C11  B A1A8H D 3 .   ? 15.334 2.056   5.206   0.24 10.23 ?  202 A1A8H A C11  1 
HETATM 7143 C C13  B A1A8H D 3 .   ? 15.535 3.654   3.562   0.24 10.43 ?  202 A1A8H A C13  1 
HETATM 7144 C C2   B A1A8H D 3 .   ? 14.687 -0.242  0.765   0.24 14.77 ?  202 A1A8H A C2   1 
HETATM 7145 C C4   B A1A8H D 3 .   ? 13.704 1.728   -0.432  0.24 14.73 ?  202 A1A8H A C4   1 
HETATM 7146 C C5   B A1A8H D 3 .   ? 13.293 2.593   -1.701  0.24 15.03 ?  202 A1A8H A C5   1 
HETATM 7147 C C7   B A1A8H D 3 .   ? 12.172 1.858   -0.049  0.24 14.23 ?  202 A1A8H A C7   1 
HETATM 7148 C C8   B A1A8H D 3 .   ? 14.649 2.166   0.747   0.24 13.79 ?  202 A1A8H A C8   1 
HETATM 7149 N N1   B A1A8H D 3 .   ? 15.004 0.973   1.582   0.24 13.42 ?  202 A1A8H A N1   1 
HETATM 7150 N N3   B A1A8H D 3 .   ? 15.177 0.904   5.901   0.24 10.41 ?  202 A1A8H A N3   1 
HETATM 7151 N N4   B A1A8H D 3 .   ? 15.567 3.291   5.750   0.24 10.06 ?  202 A1A8H A N4   1 
HETATM 7152 O O1   B A1A8H D 3 .   ? 15.661 -2.278  -0.141  0.24 15.76 ?  202 A1A8H A O1   1 
HETATM 7153 H H5   B A1A8H D 3 .   ? 14.878 0.088   -1.425  0.24 18.41 ?  202 A1A8H A H5   1 
HETATM 7154 H H6   B A1A8H D 3 .   ? 13.245 -0.375  -0.926  0.24 18.41 ?  202 A1A8H A H6   1 
HETATM 7155 H H9   B A1A8H D 3 .   ? 11.392 1.408   -2.108  0.24 18.42 ?  202 A1A8H A H9   1 
HETATM 7156 H H10  B A1A8H D 3 .   ? 11.059 3.097   -1.574  0.24 18.42 ?  202 A1A8H A H10  1 
HETATM 7157 H H17  B A1A8H D 3 .   ? 15.871 5.287   5.163   0.24 11.97 ?  202 A1A8H A H17  1 
HETATM 7158 H H3   B A1A8H D 3 .   ? 16.714 -0.493  -0.092  0.24 18.03 ?  202 A1A8H A H3   1 
HETATM 7159 H H4   B A1A8H D 3 .   ? 16.484 -1.304  1.506   0.24 18.03 ?  202 A1A8H A H4   1 
HETATM 7160 H H15  B A1A8H D 3 .   ? 14.832 -1.123  5.715   0.24 13.33 ?  202 A1A8H A H15  1 
HETATM 7161 H H16  B A1A8H D 3 .   ? 15.586 4.216   2.648   0.24 12.51 ?  202 A1A8H A H16  1 
HETATM 7162 H H1   B A1A8H D 3 .   ? 13.909 -0.880  1.292   0.24 17.73 ?  202 A1A8H A H1   1 
HETATM 7163 H H8   B A1A8H D 3 .   ? 13.479 3.671   -1.655  0.24 18.04 ?  202 A1A8H A H8   1 
HETATM 7164 H H7   B A1A8H D 3 .   ? 13.631 2.230   -2.678  0.24 18.04 ?  202 A1A8H A H7   1 
HETATM 7165 H H12  B A1A8H D 3 .   ? 11.702 0.911   0.297   0.24 17.08 ?  202 A1A8H A H12  1 
HETATM 7166 H H11  B A1A8H D 3 .   ? 11.954 2.663   0.683   0.24 17.08 ?  202 A1A8H A H11  1 
HETATM 7167 H H14  B A1A8H D 3 .   ? 14.062 2.899   1.370   0.24 16.54 ?  202 A1A8H A H14  1 
HETATM 7168 H H13  B A1A8H D 3 .   ? 15.552 2.698   0.415   0.24 16.54 ?  202 A1A8H A H13  1 
HETATM 7169 H H18  B A1A8H D 3 .   ? 15.638 3.457   6.795   0.24 12.07 ?  202 A1A8H A H18  1 
HETATM 7170 H H2   B A1A8H D 3 .   ? 16.450 -2.859  -0.204  0.24 18.91 ?  202 A1A8H A H2   1 
HETATM 7171 N N2   C A1A8H E 3 .   ? 14.950 -0.238  3.867   0.24 13.20 ?  203 A1A8H A N2   1 
HETATM 7172 C C3   C A1A8H E 3 .   ? 13.963 -0.037  -0.409  0.24 17.36 ?  203 A1A8H A C3   1 
HETATM 7173 C C6   C A1A8H E 3 .   ? 11.214 2.125   -0.143  0.24 16.45 ?  203 A1A8H A C6   1 
HETATM 7174 C C9   C A1A8H E 3 .   ? 15.096 0.899   3.114   0.24 13.35 ?  203 A1A8H A C9   1 
HETATM 7175 C C12  C A1A8H E 3 .   ? 15.318 2.138   3.818   0.24 11.72 ?  203 A1A8H A C12  1 
HETATM 7176 C C14  C A1A8H E 3 .   ? 15.689 4.220   4.765   0.24 10.45 ?  203 A1A8H A C14  1 
HETATM 7177 C C1   C A1A8H E 3 .   ? 16.094 -1.176  0.519   0.24 17.77 ?  203 A1A8H A C1   1 
HETATM 7178 C C10  C A1A8H E 3 .   ? 15.009 -0.195  5.256   0.24 13.02 ?  203 A1A8H A C10  1 
HETATM 7179 C C11  C A1A8H E 3 .   ? 15.356 2.028   5.262   0.24 11.41 ?  203 A1A8H A C11  1 
HETATM 7180 C C13  C A1A8H E 3 .   ? 15.540 3.572   3.538   0.24 10.94 ?  203 A1A8H A C13  1 
HETATM 7181 C C2   C A1A8H E 3 .   ? 14.747 -0.443  0.895   0.24 17.05 ?  203 A1A8H A C2   1 
HETATM 7182 C C4   C A1A8H E 3 .   ? 13.292 1.292   -0.063  0.24 17.11 ?  203 A1A8H A C4   1 
HETATM 7183 C C5   C A1A8H E 3 .   ? 12.414 2.075   -1.133  0.24 16.59 ?  203 A1A8H A C5   1 
HETATM 7184 C C7   C A1A8H E 3 .   ? 11.949 1.096   0.734   0.24 16.48 ?  203 A1A8H A C7   1 
HETATM 7185 C C8   C A1A8H E 3 .   ? 14.413 1.926   0.825   0.24 16.47 ?  203 A1A8H A C8   1 
HETATM 7186 N N1   C A1A8H E 3 .   ? 15.029 0.831   1.656   0.24 15.60 ?  203 A1A8H A N1   1 
HETATM 7187 N N3   C A1A8H E 3 .   ? 15.214 0.895   6.026   0.24 12.20 ?  203 A1A8H A N3   1 
HETATM 7188 N N4   C A1A8H E 3 .   ? 15.578 3.285   5.737   0.24 10.85 ?  203 A1A8H A N4   1 
HETATM 7189 O O1   C A1A8H E 3 .   ? 15.778 -2.357  -0.199  0.24 18.68 ?  203 A1A8H A O1   1 
HETATM 7190 H H5   C A1A8H E 3 .   ? 14.649 -0.008  -1.304  0.24 20.83 ?  203 A1A8H A H5   1 
HETATM 7191 H H6   C A1A8H E 3 .   ? 13.194 -0.807  -0.673  0.24 20.83 ?  203 A1A8H A H6   1 
HETATM 7192 H H9   C A1A8H E 3 .   ? 10.246 1.764   -0.560  0.24 19.74 ?  203 A1A8H A H9   1 
HETATM 7193 H H10  C A1A8H E 3 .   ? 11.030 3.099   0.355   0.24 19.74 ?  203 A1A8H A H10  1 
HETATM 7194 H H17  C A1A8H E 3 .   ? 15.861 5.266   5.071   0.24 12.55 ?  203 A1A8H A H17  1 
HETATM 7195 H H3   C A1A8H E 3 .   ? 16.732 -0.509  -0.102  0.24 21.33 ?  203 A1A8H A H3   1 
HETATM 7196 H H4   C A1A8H E 3 .   ? 16.646 -1.427  1.453   0.24 21.33 ?  203 A1A8H A H4   1 
HETATM 7197 H H15  C A1A8H E 3 .   ? 14.882 -1.142  5.829   0.24 15.63 ?  203 A1A8H A H15  1 
HETATM 7198 H H16  C A1A8H E 3 .   ? 15.587 4.112   2.593   0.24 13.13 ?  203 A1A8H A H16  1 
HETATM 7199 H H1   C A1A8H E 3 .   ? 14.098 -1.115  1.517   0.24 20.46 ?  203 A1A8H A H1   1 
HETATM 7200 H H8   C A1A8H E 3 .   ? 12.748 3.096   -1.428  0.24 19.90 ?  203 A1A8H A H8   1 
HETATM 7201 H H7   C A1A8H E 3 .   ? 12.150 1.520   -2.063  0.24 19.90 ?  203 A1A8H A H7   1 
HETATM 7202 H H12  C A1A8H E 3 .   ? 11.544 0.069   0.669   0.24 19.78 ?  203 A1A8H A H12  1 
HETATM 7203 H H11  C A1A8H E 3 .   ? 12.017 1.408   1.795   0.24 19.78 ?  203 A1A8H A H11  1 
HETATM 7204 H H14  C A1A8H E 3 .   ? 15.180 2.381   0.144   0.24 19.76 ?  203 A1A8H A H14  1 
HETATM 7205 H H13  C A1A8H E 3 .   ? 14.049 2.768   1.454   0.24 19.76 ?  203 A1A8H A H13  1 
HETATM 7206 H H18  C A1A8H E 3 .   ? 15.646 3.492   6.767   0.24 13.02 ?  203 A1A8H A H18  1 
HETATM 7207 H H2   C A1A8H E 3 .   ? 16.586 -2.890  -0.331  0.24 22.42 ?  203 A1A8H A H2   1 
HETATM 7208 O O    B HOH   F 4 .   ? 18.980 -0.194  -3.811  0.48 37.10 ?  301 HOH   A O    1 
HETATM 7209 O O    . HOH   F 4 .   ? 4.179  -9.033  10.150  1.00 46.43 ?  302 HOH   A O    1 
HETATM 7210 O O    . HOH   F 4 .   ? 14.348 -4.526  -12.146 1.00 46.38 ?  303 HOH   A O    1 
HETATM 7211 O O    A HOH   F 4 .   ? 14.822 -4.620  20.362  0.52 38.55 ?  304 HOH   A O    1 
HETATM 7212 O O    . HOH   F 4 .   ? 17.171 -18.021 14.899  1.00 32.03 ?  305 HOH   A O    1 
HETATM 7213 O O    . HOH   F 4 .   ? 14.689 -13.846 16.708  1.00 29.24 ?  306 HOH   A O    1 
HETATM 7214 O O    A HOH   F 4 .   ? 4.782  3.887   0.524   0.52 23.48 ?  307 HOH   A O    1 
HETATM 7215 O O    . HOH   F 4 .   ? 34.408 -1.851  12.550  1.00 40.50 ?  308 HOH   A O    1 
HETATM 7216 O O    . HOH   F 4 .   ? 11.855 0.380   14.510  1.00 34.26 ?  309 HOH   A O    1 
HETATM 7217 O O    . HOH   F 4 .   ? 29.058 0.441   -9.845  1.00 24.36 ?  310 HOH   A O    1 
HETATM 7218 O O    . HOH   F 4 .   ? 9.585  -16.495 -2.429  1.00 45.50 ?  311 HOH   A O    1 
HETATM 7219 O O    A HOH   F 4 .   ? -0.397 -3.119  2.999   0.52 35.39 ?  312 HOH   A O    1 
HETATM 7220 O O    . HOH   F 4 .   ? 15.038 -12.125 18.587  1.00 45.43 ?  313 HOH   A O    1 
HETATM 7221 O O    . HOH   F 4 .   ? 0.861  -4.411  -0.214  1.00 40.27 ?  314 HOH   A O    1 
HETATM 7222 O O    . HOH   F 4 .   ? 22.253 5.406   18.893  1.00 46.67 ?  315 HOH   A O    1 
HETATM 7223 O O    B HOH   F 4 .   ? 18.798 -1.993  -1.275  0.48 34.02 ?  316 HOH   A O    1 
HETATM 7224 O O    . HOH   F 4 .   ? 19.397 -10.931 24.059  1.00 91.16 ?  317 HOH   A O    1 
HETATM 7225 O O    . HOH   F 4 .   ? 9.982  -21.394 5.640   1.00 25.96 ?  318 HOH   A O    1 
HETATM 7226 O O    . HOH   F 4 .   ? 18.981 -21.980 6.881   1.00 38.29 ?  319 HOH   A O    1 
HETATM 7227 O O    . HOH   F 4 .   ? 26.945 11.456  1.631   1.00 17.87 ?  320 HOH   A O    1 
HETATM 7228 O O    . HOH   F 4 .   ? 14.921 3.983   17.396  1.00 44.54 ?  321 HOH   A O    1 
HETATM 7229 O O    . HOH   F 4 .   ? 28.108 -6.174  19.581  1.00 47.10 ?  322 HOH   A O    1 
HETATM 7230 O O    . HOH   F 4 .   ? 9.216  -10.017 19.284  1.00 45.97 ?  323 HOH   A O    1 
HETATM 7231 O O    . HOH   F 4 .   ? 25.842 -0.855  -7.497  1.00 23.02 ?  324 HOH   A O    1 
HETATM 7232 O O    . HOH   F 4 .   ? 13.644 -15.374 -7.793  1.00 31.96 ?  325 HOH   A O    1 
HETATM 7233 O O    . HOH   F 4 .   ? 11.917 -10.990 -10.100 1.00 59.42 ?  326 HOH   A O    1 
HETATM 7234 O O    . HOH   F 4 .   ? 22.511 -11.976 21.838  1.00 57.56 ?  327 HOH   A O    1 
HETATM 7235 O O    . HOH   F 4 .   ? 30.338 -13.329 -8.537  1.00 23.08 ?  328 HOH   A O    1 
HETATM 7236 O O    . HOH   F 4 .   ? 8.837  -11.957 17.120  1.00 38.24 ?  329 HOH   A O    1 
HETATM 7237 O O    A HOH   F 4 .   ? 7.005  -8.185  11.771  0.52 17.01 ?  330 HOH   A O    1 
HETATM 7238 O O    . HOH   F 4 .   ? 24.194 -7.735  14.412  1.00 17.83 ?  331 HOH   A O    1 
HETATM 7239 O O    . HOH   F 4 .   ? 10.911 1.746   12.203  1.00 24.90 ?  332 HOH   A O    1 
HETATM 7240 O O    . HOH   F 4 .   ? 37.525 2.831   10.340  1.00 27.99 ?  333 HOH   A O    1 
HETATM 7241 O O    . HOH   F 4 .   ? 42.653 4.329   5.656   1.00 35.14 ?  334 HOH   A O    1 
HETATM 7242 O O    . HOH   F 4 .   ? 42.457 10.518  4.964   1.00 20.47 ?  335 HOH   A O    1 
HETATM 7243 O O    . HOH   F 4 .   ? 15.323 -8.185  -10.050 1.00 30.15 ?  336 HOH   A O    1 
HETATM 7244 O O    A HOH   F 4 .   ? 14.347 0.545   6.736   0.52 30.35 ?  337 HOH   A O    1 
HETATM 7245 O O    . HOH   F 4 .   ? 22.778 12.509  1.576   1.00 16.46 ?  338 HOH   A O    1 
HETATM 7246 O O    . HOH   F 4 .   ? 20.147 -12.661 -8.788  1.00 29.16 ?  339 HOH   A O    1 
HETATM 7247 O O    . HOH   F 4 .   ? 26.609 -19.358 -1.775  1.00 15.99 ?  340 HOH   A O    1 
HETATM 7248 O O    . HOH   F 4 .   ? 17.075 -19.307 4.863   1.00 18.03 ?  341 HOH   A O    1 
HETATM 7249 O O    . HOH   F 4 .   ? 30.949 6.214   -12.239 1.00 27.78 ?  342 HOH   A O    1 
HETATM 7250 O O    . HOH   F 4 .   ? 18.558 9.509   8.895   1.00 22.72 ?  343 HOH   A O    1 
HETATM 7251 O O    . HOH   F 4 .   ? -0.714 -8.542  1.958   1.00 49.83 ?  344 HOH   A O    1 
HETATM 7252 O O    A HOH   F 4 .   ? 14.716 -3.685  3.037   0.52 20.09 ?  345 HOH   A O    1 
HETATM 7253 O O    . HOH   F 4 .   ? 27.410 13.844  2.872   1.00 34.65 ?  346 HOH   A O    1 
HETATM 7254 O O    . HOH   F 4 .   ? 28.770 -10.710 -14.123 1.00 47.88 ?  347 HOH   A O    1 
HETATM 7255 O O    . HOH   F 4 .   ? 18.712 -19.454 13.588  1.00 42.14 ?  348 HOH   A O    1 
HETATM 7256 O O    . HOH   F 4 .   ? 31.095 -18.102 7.809   1.00 20.79 ?  349 HOH   A O    1 
HETATM 7257 O O    . HOH   F 4 .   ? 14.510 -21.342 -4.254  1.00 33.48 ?  350 HOH   A O    1 
HETATM 7258 O O    . HOH   F 4 .   ? 36.331 -5.144  -0.494  1.00 36.51 ?  351 HOH   A O    1 
HETATM 7259 O O    . HOH   F 4 .   ? 30.533 1.950   16.758  1.00 24.70 ?  352 HOH   A O    1 
HETATM 7260 O O    . HOH   F 4 .   ? 31.711 8.199   14.975  1.00 29.31 ?  353 HOH   A O    1 
HETATM 7261 O O    . HOH   F 4 .   ? 22.204 -19.370 11.389  1.00 39.31 ?  354 HOH   A O    1 
HETATM 7262 O O    . HOH   F 4 .   ? 44.415 7.259   6.452   1.00 28.12 ?  355 HOH   A O    1 
HETATM 7263 O O    . HOH   F 4 .   ? 13.401 -1.557  -6.984  1.00 27.19 ?  356 HOH   A O    1 
HETATM 7264 O O    . HOH   F 4 .   ? 21.345 -2.278  -2.545  1.00 19.64 ?  357 HOH   A O    1 
HETATM 7265 O O    . HOH   F 4 .   ? 13.772 -4.736  17.214  1.00 29.82 ?  358 HOH   A O    1 
HETATM 7266 O O    . HOH   F 4 .   ? 38.381 10.494  7.017   1.00 56.10 ?  359 HOH   A O    1 
HETATM 7267 O O    . HOH   F 4 .   ? 34.143 -1.126  -8.933  1.00 29.05 ?  360 HOH   A O    1 
HETATM 7268 O O    . HOH   F 4 .   ? 7.928  -21.602 4.037   1.00 52.63 ?  361 HOH   A O    1 
HETATM 7269 O O    A HOH   F 4 .   ? 28.349 -0.242  -13.364 0.52 27.29 ?  362 HOH   A O    1 
HETATM 7270 O O    . HOH   F 4 .   ? 20.744 -19.768 -5.124  1.00 33.29 ?  363 HOH   A O    1 
HETATM 7271 O O    A HOH   F 4 .   ? 17.584 -1.747  0.389   0.52 31.41 ?  364 HOH   A O    1 
HETATM 7272 O O    . HOH   F 4 .   ? 43.413 7.701   2.714   1.00 48.46 ?  365 HOH   A O    1 
HETATM 7273 O O    . HOH   F 4 .   ? 27.427 -10.549 14.126  1.00 19.43 ?  366 HOH   A O    1 
HETATM 7274 O O    . HOH   F 4 .   ? 31.173 -13.966 -2.455  1.00 15.49 ?  367 HOH   A O    1 
HETATM 7275 O O    . HOH   F 4 .   ? 24.129 -2.157  -2.185  1.00 13.12 ?  368 HOH   A O    1 
HETATM 7276 O O    . HOH   F 4 .   ? 38.599 5.000   7.082   1.00 16.04 ?  369 HOH   A O    1 
HETATM 7277 O O    . HOH   F 4 .   ? 23.515 11.408  4.049   1.00 13.34 ?  370 HOH   A O    1 
HETATM 7278 O O    B HOH   F 4 .   ? 14.984 -2.806  2.935   0.48 13.81 ?  371 HOH   A O    1 
HETATM 7279 O O    . HOH   F 4 .   ? 28.024 0.782   -7.225  1.00 16.26 ?  372 HOH   A O    1 
HETATM 7280 O O    A HOH   F 4 .   ? 24.692 2.001   -7.024  0.52 18.25 ?  373 HOH   A O    1 
HETATM 7281 O O    . HOH   F 4 .   ? 17.299 -17.971 -5.164  1.00 33.82 ?  374 HOH   A O    1 
HETATM 7282 O O    . HOH   F 4 .   ? 15.199 -21.528 14.207  1.00 22.10 ?  375 HOH   A O    1 
HETATM 7283 O O    . HOH   F 4 .   ? 35.850 -12.656 6.892   1.00 16.73 ?  376 HOH   A O    1 
HETATM 7284 O O    . HOH   F 4 .   ? 39.873 -1.079  -5.100  1.00 24.22 ?  377 HOH   A O    1 
HETATM 7285 O O    . HOH   F 4 .   ? 32.104 -9.325  -6.584  1.00 25.83 ?  378 HOH   A O    1 
HETATM 7286 O O    . HOH   F 4 .   ? 30.838 3.083   8.290   1.00 13.54 ?  379 HOH   A O    1 
HETATM 7287 O O    A HOH   F 4 .   ? 8.086  -12.629 -0.953  0.52 20.02 ?  380 HOH   A O    1 
HETATM 7288 O O    . HOH   F 4 .   ? 24.665 -17.521 12.770  1.00 27.27 ?  381 HOH   A O    1 
HETATM 7289 O O    . HOH   F 4 .   ? 16.251 16.631  8.545   1.00 47.76 ?  382 HOH   A O    1 
HETATM 7290 O O    . HOH   F 4 .   ? 21.336 2.969   -0.198  1.00 15.57 ?  383 HOH   A O    1 
HETATM 7291 O O    . HOH   F 4 .   ? 37.351 11.990  4.972   1.00 27.09 ?  384 HOH   A O    1 
HETATM 7292 O O    . HOH   F 4 .   ? 24.403 3.614   -1.816  1.00 19.59 ?  385 HOH   A O    1 
HETATM 7293 O O    . HOH   F 4 .   ? 21.898 -21.939 8.541   1.00 30.16 ?  386 HOH   A O    1 
HETATM 7294 O O    . HOH   F 4 .   ? 33.698 -7.160  4.372   1.00 18.59 ?  387 HOH   A O    1 
HETATM 7295 O O    . HOH   F 4 .   ? 26.984 4.160   -0.679  1.00 13.55 ?  388 HOH   A O    1 
HETATM 7296 O O    . HOH   F 4 .   ? 21.182 10.169  15.041  1.00 36.52 ?  389 HOH   A O    1 
HETATM 7297 O O    . HOH   F 4 .   ? 37.567 -2.147  5.885   1.00 27.76 ?  390 HOH   A O    1 
HETATM 7298 O O    . HOH   F 4 .   ? 32.029 -7.406  -9.792  1.00 23.89 ?  391 HOH   A O    1 
HETATM 7299 O O    T HOH   F 4 .   ? 15.490 -0.453  2.326   0.20 14.46 ?  392 HOH   A O    1 
HETATM 7300 O O    . HOH   F 4 .   ? 26.849 -3.026  19.630  1.00 38.39 ?  393 HOH   A O    1 
HETATM 7301 O O    . HOH   F 4 .   ? 27.766 -6.384  -14.083 1.00 40.17 ?  394 HOH   A O    1 
HETATM 7302 O O    . HOH   F 4 .   ? 27.130 2.399   18.741  1.00 43.47 ?  395 HOH   A O    1 
HETATM 7303 O O    . HOH   F 4 .   ? 37.235 -2.974  9.825   1.00 50.18 ?  396 HOH   A O    1 
HETATM 7304 O O    . HOH   F 4 .   ? 5.295  2.664   4.670   1.00 32.96 ?  397 HOH   A O    1 
HETATM 7305 O O    . HOH   F 4 .   ? 20.608 -20.045 2.811   1.00 22.18 ?  398 HOH   A O    1 
HETATM 7306 O O    . HOH   F 4 .   ? 24.030 -15.758 -9.198  1.00 38.92 ?  399 HOH   A O    1 
HETATM 7307 O O    . HOH   F 4 .   ? 14.104 -23.112 7.390   1.00 21.92 ?  400 HOH   A O    1 
HETATM 7308 O O    . HOH   F 4 .   ? 15.787 2.122   24.624  1.00 54.58 ?  401 HOH   A O    1 
HETATM 7309 O O    . HOH   F 4 .   ? 32.849 -9.253  6.022   1.00 20.88 ?  402 HOH   A O    1 
HETATM 7310 O O    A HOH   F 4 .   ? 20.209 4.504   -7.596  0.52 21.90 ?  403 HOH   A O    1 
HETATM 7311 O O    . HOH   F 4 .   ? 16.610 -22.197 0.953   1.00 30.91 ?  404 HOH   A O    1 
HETATM 7312 O O    B HOH   F 4 .   ? 13.255 -3.290  -1.329  0.48 30.51 ?  405 HOH   A O    1 
HETATM 7313 O O    . HOH   F 4 .   ? 38.174 -1.354  -1.837  1.00 20.93 ?  406 HOH   A O    1 
HETATM 7314 O O    . HOH   F 4 .   ? 43.882 8.453   -3.069  1.00 32.53 ?  407 HOH   A O    1 
HETATM 7315 O O    . HOH   F 4 .   ? 24.041 -20.316 -1.360  1.00 20.63 ?  408 HOH   A O    1 
HETATM 7316 O O    A HOH   F 4 .   ? 11.152 -0.411  1.862   0.56 32.63 ?  409 HOH   A O    1 
HETATM 7317 O O    A HOH   F 4 .   ? 7.819  -6.366  -6.588  0.52 34.70 ?  410 HOH   A O    1 
HETATM 7318 O O    . HOH   F 4 .   ? 41.045 -8.361  -6.693  1.00 39.03 ?  411 HOH   A O    1 
HETATM 7319 O O    . HOH   F 4 .   ? 24.023 3.936   -4.823  1.00 24.84 ?  412 HOH   A O    1 
HETATM 7320 O O    A HOH   F 4 .   ? 15.876 -0.975  5.212   0.52 29.85 ?  413 HOH   A O    1 
HETATM 7321 O O    A HOH   F 4 .   ? 18.706 -2.507  -16.388 0.52 32.93 ?  414 HOH   A O    1 
HETATM 7322 O O    . HOH   F 4 .   ? 21.927 -13.900 -8.321  1.00 51.54 ?  415 HOH   A O    1 
HETATM 7323 O O    . HOH   F 4 .   ? 32.867 -4.426  -9.873  1.00 30.29 ?  416 HOH   A O    1 
HETATM 7324 O O    . HOH   F 4 .   ? 35.149 -5.269  -3.018  1.00 19.89 ?  417 HOH   A O    1 
HETATM 7325 O O    . HOH   F 4 .   ? 16.279 -14.189 20.182  1.00 51.90 ?  418 HOH   A O    1 
HETATM 7326 O O    A HOH   F 4 .   ? 6.525  -5.629  11.097  0.52 19.07 ?  419 HOH   A O    1 
HETATM 7327 O O    . HOH   F 4 .   ? 16.072 6.914   2.775   1.00 21.86 ?  420 HOH   A O    1 
HETATM 7328 O O    . HOH   F 4 .   ? 14.503 -0.585  -12.579 1.00 37.57 ?  421 HOH   A O    1 
HETATM 7329 O O    . HOH   F 4 .   ? 32.578 -10.613 3.270   1.00 34.34 ?  422 HOH   A O    1 
HETATM 7330 O O    . HOH   F 4 .   ? 18.427 -15.926 16.126  1.00 40.31 ?  423 HOH   A O    1 
HETATM 7331 O O    . HOH   F 4 .   ? 30.070 -10.078 13.131  1.00 26.54 ?  424 HOH   A O    1 
HETATM 7332 O O    . HOH   F 4 .   ? 30.360 -12.867 13.575  1.00 21.42 ?  425 HOH   A O    1 
HETATM 7333 O O    . HOH   F 4 .   ? 22.582 8.126   18.383  1.00 50.52 ?  426 HOH   A O    1 
HETATM 7334 O O    . HOH   F 4 .   ? 11.703 -10.676 16.908  1.00 29.35 ?  427 HOH   A O    1 
HETATM 7335 O O    . HOH   F 4 .   ? 36.748 -5.054  5.429   1.00 26.42 ?  428 HOH   A O    1 
HETATM 7336 O O    . HOH   F 4 .   ? 10.456 -13.867 -1.909  1.00 21.17 ?  429 HOH   A O    1 
HETATM 7337 O O    . HOH   F 4 .   ? 16.265 2.956   -1.719  1.00 34.80 ?  430 HOH   A O    1 
HETATM 7338 O O    A HOH   F 4 .   ? 19.053 -0.704  -1.676  0.52 18.77 ?  431 HOH   A O    1 
HETATM 7339 O O    A HOH   F 4 .   ? 18.566 4.799   -15.083 0.52 45.56 ?  432 HOH   A O    1 
HETATM 7340 O O    . HOH   F 4 .   ? 41.717 1.460   5.146   1.00 42.90 ?  433 HOH   A O    1 
HETATM 7341 O O    . HOH   F 4 .   ? 6.601  -3.394  12.705  1.00 34.37 ?  434 HOH   A O    1 
HETATM 7342 O O    . HOH   F 4 .   ? 14.436 -24.607 11.491  1.00 42.50 ?  435 HOH   A O    1 
HETATM 7343 O O    . HOH   F 4 .   ? 23.507 -20.980 1.347   1.00 21.43 ?  436 HOH   A O    1 
HETATM 7344 O O    . HOH   F 4 .   ? 29.974 -1.969  -12.835 1.00 53.25 ?  437 HOH   A O    1 
HETATM 7345 O O    . HOH   F 4 .   ? 45.151 -0.720  3.026   1.00 44.24 ?  438 HOH   A O    1 
HETATM 7346 O O    . HOH   F 4 .   ? 21.411 -14.836 17.796  1.00 55.88 ?  439 HOH   A O    1 
HETATM 7347 O O    . HOH   F 4 .   ? 23.491 -8.038  17.113  1.00 24.64 ?  440 HOH   A O    1 
HETATM 7348 O O    . HOH   F 4 .   ? 15.419 11.633  7.780   1.00 51.53 ?  441 HOH   A O    1 
HETATM 7349 O O    A HOH   F 4 .   ? 18.955 1.999   -0.803  0.52 15.88 ?  442 HOH   A O    1 
HETATM 7350 O O    B HOH   F 4 .   ? 4.879  4.083   0.313   0.48 38.61 ?  443 HOH   A O    1 
HETATM 7351 O O    . HOH   F 4 .   ? 34.362 -8.232  -0.485  1.00 32.21 ?  444 HOH   A O    1 
HETATM 7352 O O    . HOH   F 4 .   ? 31.401 -12.805 -0.008  1.00 22.08 ?  445 HOH   A O    1 
HETATM 7353 O O    B HOH   F 4 .   ? 18.481 2.036   -0.441  0.48 14.43 ?  446 HOH   A O    1 
HETATM 7354 O O    . HOH   F 4 .   ? 20.503 -17.699 24.804  1.00 60.92 ?  447 HOH   A O    1 
HETATM 7355 O O    . HOH   F 4 .   ? -1.421 -5.154  7.338   1.00 55.70 ?  448 HOH   A O    1 
HETATM 7356 O O    . HOH   F 4 .   ? 23.320 7.364   -3.232  1.00 40.27 ?  449 HOH   A O    1 
HETATM 7357 O O    . HOH   F 4 .   ? 37.851 -8.844  -3.349  1.00 24.67 ?  450 HOH   A O    1 
HETATM 7358 O O    A HOH   F 4 .   ? 10.600 -22.212 -1.320  0.52 33.64 ?  451 HOH   A O    1 
HETATM 7359 O O    . HOH   F 4 .   ? 30.606 14.782  2.720   1.00 20.34 ?  452 HOH   A O    1 
HETATM 7360 O O    A HOH   F 4 .   ? 14.108 -0.369  3.398   0.32 37.71 ?  453 HOH   A O    1 
HETATM 7361 O O    . HOH   F 4 .   ? 21.483 -9.118  21.334  1.00 63.26 ?  454 HOH   A O    1 
HETATM 7362 O O    B HOH   F 4 .   ? 11.862 -1.535  -3.296  0.48 25.75 ?  455 HOH   A O    1 
HETATM 7363 O O    . HOH   F 4 .   ? 29.790 -16.057 10.773  1.00 32.95 ?  456 HOH   A O    1 
HETATM 7364 O O    . HOH   F 4 .   ? 24.771 5.582   20.690  1.00 56.61 ?  457 HOH   A O    1 
HETATM 7365 O O    . HOH   F 4 .   ? 32.438 -15.932 10.965  1.00 30.96 ?  458 HOH   A O    1 
HETATM 7366 O O    . HOH   F 4 .   ? 25.446 8.254   -4.839  1.00 38.78 ?  459 HOH   A O    1 
HETATM 7367 O O    . HOH   F 4 .   ? 19.998 -17.491 -5.026  1.00 30.44 ?  460 HOH   A O    1 
HETATM 7368 O O    . HOH   F 4 .   ? 27.895 7.155   -6.711  1.00 42.38 ?  461 HOH   A O    1 
HETATM 7369 O O    . HOH   F 4 .   ? 23.282 -22.439 -3.255  1.00 36.43 ?  462 HOH   A O    1 
HETATM 7370 O O    B HOH   F 4 .   ? 12.559 -3.308  1.486   0.48 20.16 ?  463 HOH   A O    1 
HETATM 7371 O O    . HOH   F 4 .   ? 24.763 14.737  7.653   1.00 38.29 ?  464 HOH   A O    1 
HETATM 7372 O O    . HOH   F 4 .   ? 18.433 -16.422 -9.028  1.00 48.76 ?  465 HOH   A O    1 
HETATM 7373 O O    . HOH   F 4 .   ? 11.159 -15.159 -6.210  1.00 39.72 ?  466 HOH   A O    1 
HETATM 7374 O O    . HOH   F 4 .   ? 27.400 -11.407 16.685  1.00 43.76 ?  467 HOH   A O    1 
HETATM 7375 O O    . HOH   F 4 .   ? 18.811 10.992  11.226  1.00 34.96 ?  468 HOH   A O    1 
HETATM 7376 O O    . HOH   F 4 .   ? 26.983 11.680  -1.421  1.00 39.11 ?  469 HOH   A O    1 
HETATM 7377 O O    . HOH   F 4 .   ? 15.865 -21.624 3.688   1.00 27.34 ?  470 HOH   A O    1 
HETATM 7378 O O    . HOH   F 4 .   ? 23.510 13.739  5.515   1.00 20.89 ?  471 HOH   A O    1 
HETATM 7379 O O    . HOH   F 4 .   ? 39.788 -7.112  -3.406  1.00 45.75 ?  472 HOH   A O    1 
HETATM 7380 O O    . HOH   F 4 .   ? 12.301 1.556   17.134  1.00 43.07 ?  473 HOH   A O    1 
HETATM 7381 O O    . HOH   F 4 .   ? 15.994 -17.279 -7.056  1.00 39.22 ?  474 HOH   A O    1 
HETATM 7382 O O    A HOH   F 4 .   ? 22.072 5.228   -5.881  0.52 27.91 ?  475 HOH   A O    1 
HETATM 7383 O O    . HOH   F 4 .   ? 12.038 -13.360 16.222  1.00 57.09 ?  476 HOH   A O    1 
HETATM 7384 O O    . HOH   F 4 .   ? 25.917 10.903  -3.734  1.00 30.88 ?  477 HOH   A O    1 
HETATM 7385 O O    . HOH   F 4 .   ? 28.705 -4.761  -12.362 1.00 48.79 ?  478 HOH   A O    1 
HETATM 7386 O O    . HOH   F 4 .   ? 8.193  -3.199  -5.860  1.00 62.36 ?  479 HOH   A O    1 
HETATM 7387 O O    . HOH   F 4 .   ? 28.898 8.956   17.634  1.00 44.66 ?  480 HOH   A O    1 
HETATM 7388 O O    . HOH   F 4 .   ? 16.904 -20.512 16.099  1.00 36.42 ?  481 HOH   A O    1 
HETATM 7389 O O    . HOH   F 4 .   ? 23.195 11.926  -4.094  1.00 24.24 ?  482 HOH   A O    1 
HETATM 7390 O O    . HOH   F 4 .   ? 35.193 7.588   12.250  1.00 55.11 ?  483 HOH   A O    1 
HETATM 7391 O O    . HOH   F 4 .   ? 41.252 -3.964  -0.343  1.00 39.74 ?  484 HOH   A O    1 
HETATM 7392 O O    B HOH   F 4 .   ? 9.973  -0.502  -1.333  0.48 34.00 ?  485 HOH   A O    1 
HETATM 7393 O O    . HOH   F 4 .   ? 17.546 -18.779 19.766  1.00 53.87 ?  486 HOH   A O    1 
HETATM 7394 O O    . HOH   F 4 .   ? 16.298 -6.886  -12.117 1.00 53.56 ?  487 HOH   A O    1 
HETATM 7395 O O    . HOH   F 4 .   ? 44.404 10.306  -1.796  1.00 43.69 ?  488 HOH   A O    1 
HETATM 7396 O O    . HOH   F 4 .   ? 30.754 0.782   19.281  1.00 42.31 ?  489 HOH   A O    1 
HETATM 7397 O O    . HOH   F 4 .   ? 23.225 -12.862 19.360  1.00 58.18 ?  490 HOH   A O    1 
HETATM 7398 O O    . HOH   F 4 .   ? 14.133 -10.357 -11.052 1.00 37.28 ?  491 HOH   A O    1 
HETATM 7399 O O    . HOH   F 4 .   ? 31.616 -0.583  -10.565 1.00 31.87 ?  492 HOH   A O    1 
HETATM 7400 O O    . HOH   F 4 .   ? 39.290 2.367   7.223   1.00 33.60 ?  493 HOH   A O    1 
HETATM 7401 O O    . HOH   F 4 .   ? 13.793 -25.146 8.935   1.00 35.42 ?  494 HOH   A O    1 
HETATM 7402 O O    . HOH   F 4 .   ? 41.868 9.425   -3.699  1.00 40.72 ?  495 HOH   A O    1 
HETATM 7403 O O    . HOH   F 4 .   ? 28.959 -8.085  -15.200 1.00 56.22 ?  496 HOH   A O    1 
HETATM 7404 O O    . HOH   F 4 .   ? 16.278 -23.453 5.856   1.00 33.42 ?  497 HOH   A O    1 
HETATM 7405 O O    . HOH   F 4 .   ? 18.625 -23.191 1.883   1.00 51.40 ?  498 HOH   A O    1 
HETATM 7406 O O    . HOH   F 4 .   ? 20.195 -22.376 4.250   1.00 36.17 ?  499 HOH   A O    1 
HETATM 7407 O O    . HOH   F 4 .   ? 40.797 -0.225  -7.687  1.00 35.86 ?  500 HOH   A O    1 
HETATM 7408 O O    . HOH   F 4 .   ? 30.753 5.824   -14.716 1.00 40.43 ?  501 HOH   A O    1 
HETATM 7409 O O    . HOH   F 4 .   ? 20.768 -16.043 -7.565  1.00 32.69 ?  502 HOH   A O    1 
HETATM 7410 O O    B HOH   F 4 .   ? 14.749 7.888   4.851   0.48 27.63 ?  503 HOH   A O    1 
HETATM 7411 O O    . HOH   F 4 .   ? 30.865 -5.897  -11.865 1.00 57.51 ?  504 HOH   A O    1 
HETATM 7412 O O    . HOH   F 4 .   ? 23.337 -23.861 1.617   1.00 34.60 ?  505 HOH   A O    1 
HETATM 7413 O O    . HOH   F 4 .   ? 37.485 -6.641  7.582   1.00 26.60 ?  506 HOH   A O    1 
HETATM 7414 O O    . HOH   F 4 .   ? 39.576 -0.073  6.730   1.00 33.99 ?  507 HOH   A O    1 
HETATM 7415 O O    . HOH   F 4 .   ? 29.028 14.391  0.835   1.00 59.11 ?  508 HOH   A O    1 
HETATM 7416 O O    . HOH   F 4 .   ? 38.028 13.990  6.623   1.00 28.45 ?  509 HOH   A O    1 
HETATM 7417 O O    . HOH   F 4 .   ? 22.165 -24.054 4.561   1.00 28.90 ?  510 HOH   A O    1 
HETATM 7418 O O    . HOH   F 4 .   ? 36.506 -6.485  10.225  1.00 50.47 ?  511 HOH   A O    1 
HETATM 7419 O O    T HOH   F 4 .   ? 12.021 -2.183  -3.722  0.20 12.95 ?  512 HOH   A O    1 
HETATM 7420 O O    . HOH   F 4 .   ? 17.416 -7.078  -14.158 1.00 62.63 ?  513 HOH   A O    1 
HETATM 7421 O O    B HOH   F 4 .   ? 5.604  6.567   1.394   0.48 29.57 ?  514 HOH   A O    1 
HETATM 7422 O O    A HOH   F 4 .   ? 14.929 8.621   4.822   0.52 40.49 ?  515 HOH   A O    1 
HETATM 7423 O O    . HOH   F 4 .   ? 24.153 9.036   -7.202  1.00 47.86 ?  516 HOH   A O    1 
HETATM 7424 O O    . HOH   F 4 .   ? 15.818 -12.403 27.293  1.00 48.16 ?  517 HOH   A O    1 
HETATM 7425 O O    . HOH   F 4 .   ? 16.385 -21.189 18.755  1.00 45.04 ?  518 HOH   A O    1 
HETATM 7426 O O    B HOH   F 4 .   ? 8.271  7.275   2.013   0.48 34.49 ?  519 HOH   A O    1 
HETATM 7427 O O    . HOH   F 4 .   ? 14.786 -22.740 19.893  1.00 40.05 ?  520 HOH   A O    1 
HETATM 7428 O O    . HOH   G 4 .   ? 29.941 -22.536 5.527   1.00 22.84 ?  201 HOH   B O    1 
HETATM 7429 O O    . HOH   G 4 .   ? 27.761 -29.205 -1.876  1.00 37.26 ?  202 HOH   B O    1 
HETATM 7430 O O    . HOH   G 4 .   ? 41.689 -36.091 -17.160 1.00 35.50 ?  203 HOH   B O    1 
HETATM 7431 O O    . HOH   G 4 .   ? 54.649 -9.495  -8.576  1.00 20.39 ?  204 HOH   B O    1 
HETATM 7432 O O    . HOH   G 4 .   ? 30.077 -26.367 4.139   1.00 31.04 ?  205 HOH   B O    1 
HETATM 7433 O O    . HOH   G 4 .   ? 38.113 -39.545 -0.075  1.00 40.71 ?  206 HOH   B O    1 
HETATM 7434 O O    . HOH   G 4 .   ? 59.254 -18.781 6.911   1.00 42.13 ?  207 HOH   B O    1 
HETATM 7435 O O    . HOH   G 4 .   ? 31.081 -28.773 4.486   1.00 30.92 ?  208 HOH   B O    1 
HETATM 7436 O O    . HOH   G 4 .   ? 30.295 -41.024 -8.008  1.00 19.45 ?  209 HOH   B O    1 
HETATM 7437 O O    . HOH   G 4 .   ? 27.921 -41.824 -15.154 1.00 37.20 ?  210 HOH   B O    1 
HETATM 7438 O O    . HOH   G 4 .   ? 49.543 -22.798 -19.731 1.00 52.56 ?  211 HOH   B O    1 
HETATM 7439 O O    . HOH   G 4 .   ? 34.935 -24.796 13.806  1.00 40.50 ?  212 HOH   B O    1 
HETATM 7440 O O    . HOH   G 4 .   ? 57.851 -24.560 5.059   1.00 39.11 ?  213 HOH   B O    1 
HETATM 7441 O O    . HOH   G 4 .   ? 58.319 -12.937 8.452   1.00 31.03 ?  214 HOH   B O    1 
HETATM 7442 O O    . HOH   G 4 .   ? 50.237 -3.345  7.193   1.00 34.09 ?  215 HOH   B O    1 
HETATM 7443 O O    . HOH   G 4 .   ? 56.851 -30.844 -7.770  1.00 32.48 ?  216 HOH   B O    1 
HETATM 7444 O O    . HOH   G 4 .   ? 37.244 -19.831 -18.168 1.00 42.68 ?  217 HOH   B O    1 
HETATM 7445 O O    . HOH   G 4 .   ? 53.198 -13.536 -20.374 1.00 40.89 ?  218 HOH   B O    1 
HETATM 7446 O O    . HOH   G 4 .   ? 34.647 -36.490 -7.074  1.00 20.99 ?  219 HOH   B O    1 
HETATM 7447 O O    . HOH   G 4 .   ? 56.499 -19.749 7.518   1.00 33.99 ?  220 HOH   B O    1 
HETATM 7448 O O    . HOH   G 4 .   ? 41.376 -7.792  5.428   1.00 41.09 ?  221 HOH   B O    1 
HETATM 7449 O O    . HOH   G 4 .   ? 57.294 -26.938 -7.679  1.00 42.55 ?  222 HOH   B O    1 
HETATM 7450 O O    . HOH   G 4 .   ? 47.510 -7.336  -3.790  1.00 46.11 ?  223 HOH   B O    1 
HETATM 7451 O O    . HOH   G 4 .   ? 51.038 -39.963 -8.139  1.00 39.19 ?  224 HOH   B O    1 
HETATM 7452 O O    . HOH   G 4 .   ? 41.577 -39.231 -14.854 1.00 24.40 ?  225 HOH   B O    1 
HETATM 7453 O O    . HOH   G 4 .   ? 57.471 -16.312 -12.266 1.00 18.60 ?  226 HOH   B O    1 
HETATM 7454 O O    . HOH   G 4 .   ? 44.572 -7.204  2.112   1.00 35.30 ?  227 HOH   B O    1 
HETATM 7455 O O    . HOH   G 4 .   ? 35.219 -8.060  -2.934  1.00 18.89 ?  228 HOH   B O    1 
HETATM 7456 O O    . HOH   G 4 .   ? 29.772 -34.129 -0.355  1.00 36.33 ?  229 HOH   B O    1 
HETATM 7457 O O    . HOH   G 4 .   ? 50.825 -6.097  0.184   1.00 28.50 ?  230 HOH   B O    1 
HETATM 7458 O O    . HOH   G 4 .   ? 50.875 -13.031 -0.411  1.00 12.39 ?  231 HOH   B O    1 
HETATM 7459 O O    . HOH   G 4 .   ? 32.828 -43.857 -11.229 1.00 24.28 ?  232 HOH   B O    1 
HETATM 7460 O O    . HOH   G 4 .   ? 46.375 -1.598  13.248  1.00 31.54 ?  233 HOH   B O    1 
HETATM 7461 O O    . HOH   G 4 .   ? 48.021 -6.968  15.595  1.00 32.04 ?  234 HOH   B O    1 
HETATM 7462 O O    . HOH   G 4 .   ? 28.570 -19.666 -13.211 1.00 29.03 ?  235 HOH   B O    1 
HETATM 7463 O O    . HOH   G 4 .   ? 44.978 -43.687 -10.469 1.00 30.15 ?  236 HOH   B O    1 
HETATM 7464 O O    . HOH   G 4 .   ? 41.487 -9.691  13.084  1.00 23.93 ?  237 HOH   B O    1 
HETATM 7465 O O    . HOH   G 4 .   ? 57.797 -24.418 -3.727  1.00 22.34 ?  238 HOH   B O    1 
HETATM 7466 O O    . HOH   G 4 .   ? 51.745 -6.559  4.366   1.00 20.68 ?  239 HOH   B O    1 
HETATM 7467 O O    . HOH   G 4 .   ? 44.632 -27.795 -0.642  1.00 22.41 ?  240 HOH   B O    1 
HETATM 7468 O O    . HOH   G 4 .   ? 30.598 -42.276 -10.596 1.00 33.75 ?  241 HOH   B O    1 
HETATM 7469 O O    . HOH   G 4 .   ? 42.758 -22.915 3.932   1.00 12.83 ?  242 HOH   B O    1 
HETATM 7470 O O    . HOH   G 4 .   ? 33.624 -16.975 8.199   1.00 20.45 ?  243 HOH   B O    1 
HETATM 7471 O O    . HOH   G 4 .   ? 25.418 -25.952 -1.184  1.00 35.07 ?  244 HOH   B O    1 
HETATM 7472 O O    . HOH   G 4 .   ? 42.706 -25.421 2.702   1.00 16.42 ?  245 HOH   B O    1 
HETATM 7473 O O    . HOH   G 4 .   ? 45.305 -35.012 6.755   1.00 48.95 ?  246 HOH   B O    1 
HETATM 7474 O O    . HOH   G 4 .   ? 38.561 -11.136 -2.225  1.00 20.54 ?  247 HOH   B O    1 
HETATM 7475 O O    . HOH   G 4 .   ? 40.508 -12.798 -11.490 1.00 16.51 ?  248 HOH   B O    1 
HETATM 7476 O O    . HOH   G 4 .   ? 39.606 -11.155 0.324   1.00 18.00 ?  249 HOH   B O    1 
HETATM 7477 O O    . HOH   G 4 .   ? 43.128 -43.344 -8.134  1.00 30.95 ?  250 HOH   B O    1 
HETATM 7478 O O    . HOH   G 4 .   ? 27.174 -31.890 -9.856  1.00 25.16 ?  251 HOH   B O    1 
HETATM 7479 O O    . HOH   G 4 .   ? 55.379 -16.502 -14.270 1.00 30.38 ?  252 HOH   B O    1 
HETATM 7480 O O    . HOH   G 4 .   ? 40.729 -16.115 14.162  1.00 22.87 ?  253 HOH   B O    1 
HETATM 7481 O O    . HOH   G 4 .   ? 28.570 -30.878 -14.765 1.00 35.06 ?  254 HOH   B O    1 
HETATM 7482 O O    . HOH   G 4 .   ? 34.278 -18.457 11.461  1.00 27.65 ?  255 HOH   B O    1 
HETATM 7483 O O    . HOH   G 4 .   ? 58.309 -10.622 -4.010  1.00 23.42 ?  256 HOH   B O    1 
HETATM 7484 O O    . HOH   G 4 .   ? 29.826 -25.232 -10.774 1.00 19.20 ?  257 HOH   B O    1 
HETATM 7485 O O    . HOH   G 4 .   ? 39.363 -10.885 6.182   1.00 27.28 ?  258 HOH   B O    1 
HETATM 7486 O O    . HOH   G 4 .   ? 30.951 -15.758 2.705   1.00 15.18 ?  259 HOH   B O    1 
HETATM 7487 O O    . HOH   G 4 .   ? 42.493 -34.749 3.857   1.00 30.32 ?  260 HOH   B O    1 
HETATM 7488 O O    . HOH   G 4 .   ? 36.118 -43.499 -8.271  1.00 45.99 ?  261 HOH   B O    1 
HETATM 7489 O O    . HOH   G 4 .   ? 42.029 -23.595 9.380   1.00 21.61 ?  262 HOH   B O    1 
HETATM 7490 O O    . HOH   G 4 .   ? 47.080 -29.609 9.862   1.00 33.40 ?  263 HOH   B O    1 
HETATM 7491 O O    . HOH   G 4 .   ? 48.705 -36.594 -15.594 1.00 49.13 ?  264 HOH   B O    1 
HETATM 7492 O O    . HOH   G 4 .   ? 48.167 -22.847 5.873   1.00 18.82 ?  265 HOH   B O    1 
HETATM 7493 O O    . HOH   G 4 .   ? 56.321 -23.689 -14.683 1.00 28.88 ?  266 HOH   B O    1 
HETATM 7494 O O    . HOH   G 4 .   ? 49.426 -28.789 -6.869  1.00 16.43 ?  267 HOH   B O    1 
HETATM 7495 O O    . HOH   G 4 .   ? 31.884 -17.933 -14.547 1.00 30.66 ?  268 HOH   B O    1 
HETATM 7496 O O    . HOH   G 4 .   ? 51.604 -13.884 11.093  1.00 29.14 ?  269 HOH   B O    1 
HETATM 7497 O O    . HOH   G 4 .   ? 49.720 -0.421  10.213  1.00 31.83 ?  270 HOH   B O    1 
HETATM 7498 O O    . HOH   G 4 .   ? 34.598 -12.799 2.653   1.00 23.66 ?  271 HOH   B O    1 
HETATM 7499 O O    . HOH   G 4 .   ? 43.251 -32.404 -17.129 1.00 25.94 ?  272 HOH   B O    1 
HETATM 7500 O O    . HOH   G 4 .   ? 35.082 -33.424 -19.103 1.00 31.71 ?  273 HOH   B O    1 
HETATM 7501 O O    . HOH   G 4 .   ? 43.541 -15.830 -12.191 1.00 15.12 ?  274 HOH   B O    1 
HETATM 7502 O O    . HOH   G 4 .   ? 51.756 -6.006  -7.891  1.00 43.46 ?  275 HOH   B O    1 
HETATM 7503 O O    . HOH   G 4 .   ? 39.010 -11.990 12.464  1.00 34.93 ?  276 HOH   B O    1 
HETATM 7504 O O    . HOH   G 4 .   ? 42.412 -9.954  9.377   1.00 21.23 ?  277 HOH   B O    1 
HETATM 7505 O O    . HOH   G 4 .   ? 48.056 -24.650 -17.813 1.00 34.42 ?  278 HOH   B O    1 
HETATM 7506 O O    . HOH   G 4 .   ? 57.624 -9.242  1.443   1.00 21.25 ?  279 HOH   B O    1 
HETATM 7507 O O    . HOH   G 4 .   ? 46.719 -31.292 -4.759  1.00 24.46 ?  280 HOH   B O    1 
HETATM 7508 O O    . HOH   G 4 .   ? 28.316 -34.413 -9.316  1.00 21.50 ?  281 HOH   B O    1 
HETATM 7509 O O    . HOH   G 4 .   ? 48.691 -12.160 -14.515 1.00 25.90 ?  282 HOH   B O    1 
HETATM 7510 O O    . HOH   G 4 .   ? 57.060 -8.636  8.459   1.00 20.21 ?  283 HOH   B O    1 
HETATM 7511 O O    . HOH   G 4 .   ? 57.190 -12.101 12.449  1.00 40.69 ?  284 HOH   B O    1 
HETATM 7512 O O    . HOH   G 4 .   ? 48.529 -25.105 3.152   1.00 14.84 ?  285 HOH   B O    1 
HETATM 7513 O O    . HOH   G 4 .   ? 50.126 -24.673 5.871   1.00 36.04 ?  286 HOH   B O    1 
HETATM 7514 O O    . HOH   G 4 .   ? 53.811 -12.666 -22.165 1.00 35.41 ?  287 HOH   B O    1 
HETATM 7515 O O    . HOH   G 4 .   ? 27.652 -26.609 -15.562 1.00 35.26 ?  288 HOH   B O    1 
HETATM 7516 O O    . HOH   G 4 .   ? 47.201 -34.040 -4.578  1.00 19.52 ?  289 HOH   B O    1 
HETATM 7517 O O    . HOH   G 4 .   ? 28.052 -22.916 -7.978  1.00 19.68 ?  290 HOH   B O    1 
HETATM 7518 O O    . HOH   G 4 .   ? 48.832 -20.092 6.007   1.00 14.85 ?  291 HOH   B O    1 
HETATM 7519 O O    . HOH   G 4 .   ? 36.895 -12.802 -1.470  1.00 27.34 ?  292 HOH   B O    1 
HETATM 7520 O O    . HOH   G 4 .   ? 45.408 -33.485 -15.924 1.00 25.72 ?  293 HOH   B O    1 
HETATM 7521 O O    . HOH   G 4 .   ? 59.917 -15.271 8.242   1.00 32.26 ?  294 HOH   B O    1 
HETATM 7522 O O    . HOH   G 4 .   ? 33.655 -15.362 -13.965 1.00 23.89 ?  295 HOH   B O    1 
HETATM 7523 O O    . HOH   G 4 .   ? 43.037 -12.106 -18.455 1.00 25.75 ?  296 HOH   B O    1 
HETATM 7524 O O    . HOH   G 4 .   ? 52.594 -10.387 13.071  1.00 24.48 ?  297 HOH   B O    1 
HETATM 7525 O O    . HOH   G 4 .   ? 52.680 -35.750 -8.764  1.00 31.71 ?  298 HOH   B O    1 
HETATM 7526 O O    . HOH   G 4 .   ? 35.176 -33.646 4.637   1.00 36.21 ?  299 HOH   B O    1 
HETATM 7527 O O    . HOH   G 4 .   ? 43.050 -20.184 -20.710 1.00 37.12 ?  300 HOH   B O    1 
HETATM 7528 O O    . HOH   G 4 .   ? 51.342 -37.707 -9.630  1.00 29.12 ?  301 HOH   B O    1 
HETATM 7529 O O    . HOH   G 4 .   ? 37.418 -35.741 7.221   1.00 34.76 ?  302 HOH   B O    1 
HETATM 7530 O O    . HOH   G 4 .   ? 53.077 -15.969 -12.748 1.00 23.70 ?  303 HOH   B O    1 
HETATM 7531 O O    . HOH   G 4 .   ? 26.055 -21.491 -3.450  1.00 19.42 ?  304 HOH   B O    1 
HETATM 7532 O O    . HOH   G 4 .   ? 37.517 -17.951 13.183  1.00 33.16 ?  305 HOH   B O    1 
HETATM 7533 O O    . HOH   G 4 .   ? 44.742 -27.515 2.053   1.00 16.94 ?  306 HOH   B O    1 
HETATM 7534 O O    . HOH   G 4 .   ? 62.825 -13.611 4.783   1.00 27.96 ?  307 HOH   B O    1 
HETATM 7535 O O    . HOH   G 4 .   ? 51.454 -33.147 -10.779 1.00 48.95 ?  308 HOH   B O    1 
HETATM 7536 O O    . HOH   G 4 .   ? 40.411 -10.904 -9.510  1.00 17.70 ?  309 HOH   B O    1 
HETATM 7537 O O    . HOH   G 4 .   ? 38.428 -12.726 8.008   1.00 19.88 ?  310 HOH   B O    1 
HETATM 7538 O O    . HOH   G 4 .   ? 44.158 -29.432 -4.609  1.00 25.12 ?  311 HOH   B O    1 
HETATM 7539 O O    . HOH   G 4 .   ? 45.914 -40.485 -3.539  1.00 35.13 ?  312 HOH   B O    1 
HETATM 7540 O O    . HOH   G 4 .   ? 41.186 -5.474  11.566  1.00 49.17 ?  313 HOH   B O    1 
HETATM 7541 O O    . HOH   G 4 .   ? 52.632 -29.355 -13.069 1.00 26.95 ?  314 HOH   B O    1 
HETATM 7542 O O    . HOH   G 4 .   ? 53.544 -30.323 4.606   1.00 19.58 ?  315 HOH   B O    1 
HETATM 7543 O O    . HOH   G 4 .   ? 44.793 -24.675 9.659   1.00 24.25 ?  316 HOH   B O    1 
HETATM 7544 O O    . HOH   G 4 .   ? 38.044 -10.277 -10.753 1.00 18.57 ?  317 HOH   B O    1 
HETATM 7545 O O    . HOH   G 4 .   ? 43.312 -21.519 10.717  1.00 18.26 ?  318 HOH   B O    1 
HETATM 7546 O O    . HOH   G 4 .   ? 44.173 -1.852  7.734   1.00 50.90 ?  319 HOH   B O    1 
HETATM 7547 O O    . HOH   G 4 .   ? 38.567 -9.375  -13.265 1.00 29.60 ?  320 HOH   B O    1 
HETATM 7548 O O    . HOH   G 4 .   ? 41.858 -8.111  1.445   1.00 25.63 ?  321 HOH   B O    1 
HETATM 7549 O O    . HOH   G 4 .   ? 26.440 -21.083 -6.217  1.00 18.46 ?  322 HOH   B O    1 
HETATM 7550 O O    . HOH   G 4 .   ? 32.910 -34.691 -5.846  1.00 19.11 ?  323 HOH   B O    1 
HETATM 7551 O O    . HOH   G 4 .   ? 42.645 -9.685  -14.820 1.00 42.47 ?  324 HOH   B O    1 
HETATM 7552 O O    . HOH   G 4 .   ? 37.207 -30.657 -21.012 1.00 33.62 ?  325 HOH   B O    1 
HETATM 7553 O O    . HOH   G 4 .   ? 43.522 -15.438 18.153  1.00 29.34 ?  326 HOH   B O    1 
HETATM 7554 O O    . HOH   G 4 .   ? 60.135 -17.307 -10.433 1.00 39.37 ?  327 HOH   B O    1 
HETATM 7555 O O    . HOH   G 4 .   ? 33.731 -31.204 11.101  1.00 39.31 ?  328 HOH   B O    1 
HETATM 7556 O O    . HOH   G 4 .   ? 27.807 -14.741 -9.450  1.00 38.18 ?  329 HOH   B O    1 
HETATM 7557 O O    . HOH   G 4 .   ? 47.359 -24.554 8.233   1.00 29.99 ?  330 HOH   B O    1 
HETATM 7558 O O    . HOH   G 4 .   ? 36.813 -12.436 4.307   1.00 18.89 ?  331 HOH   B O    1 
HETATM 7559 O O    . HOH   G 4 .   ? 57.702 -22.060 3.392   1.00 34.32 ?  332 HOH   B O    1 
HETATM 7560 O O    . HOH   G 4 .   ? 43.260 -34.668 0.142   1.00 24.71 ?  333 HOH   B O    1 
HETATM 7561 O O    . HOH   G 4 .   ? 48.214 -32.759 -16.682 1.00 47.89 ?  334 HOH   B O    1 
HETATM 7562 O O    . HOH   G 4 .   ? 63.107 -20.274 -0.700  1.00 41.38 ?  335 HOH   B O    1 
HETATM 7563 O O    . HOH   G 4 .   ? 41.486 -24.604 15.908  1.00 50.57 ?  336 HOH   B O    1 
HETATM 7564 O O    . HOH   G 4 .   ? 47.599 -27.501 2.043   1.00 16.56 ?  337 HOH   B O    1 
HETATM 7565 O O    . HOH   G 4 .   ? 37.151 -15.173 -16.583 1.00 41.46 ?  338 HOH   B O    1 
HETATM 7566 O O    . HOH   G 4 .   ? 28.957 -42.896 -12.368 1.00 50.61 ?  339 HOH   B O    1 
HETATM 7567 O O    . HOH   G 4 .   ? 42.981 -43.632 -14.349 1.00 48.16 ?  340 HOH   B O    1 
HETATM 7568 O O    . HOH   G 4 .   ? 46.832 -20.003 12.302  1.00 29.40 ?  341 HOH   B O    1 
HETATM 7569 O O    . HOH   G 4 .   ? 45.788 -36.335 -16.201 1.00 35.98 ?  342 HOH   B O    1 
HETATM 7570 O O    . HOH   G 4 .   ? 34.589 -10.376 7.769   1.00 24.79 ?  343 HOH   B O    1 
HETATM 7571 O O    . HOH   G 4 .   ? 39.756 -23.526 -20.423 1.00 37.44 ?  344 HOH   B O    1 
HETATM 7572 O O    . HOH   G 4 .   ? 38.663 -12.211 -16.211 1.00 47.56 ?  345 HOH   B O    1 
HETATM 7573 O O    . HOH   G 4 .   ? 37.171 -45.374 -9.619  1.00 38.63 ?  346 HOH   B O    1 
HETATM 7574 O O    . HOH   G 4 .   ? 38.667 -22.521 15.044  1.00 46.82 ?  347 HOH   B O    1 
HETATM 7575 O O    . HOH   G 4 .   ? 39.904 -44.252 -11.211 1.00 45.51 ?  348 HOH   B O    1 
HETATM 7576 O O    . HOH   G 4 .   ? 33.080 -14.724 1.110   1.00 23.81 ?  349 HOH   B O    1 
HETATM 7577 O O    . HOH   G 4 .   ? 40.502 -43.586 -9.102  1.00 27.58 ?  350 HOH   B O    1 
HETATM 7578 O O    . HOH   G 4 .   ? 23.392 -23.735 6.926   1.00 36.27 ?  351 HOH   B O    1 
HETATM 7579 O O    . HOH   G 4 .   ? 62.706 -20.092 -4.788  1.00 51.08 ?  352 HOH   B O    1 
HETATM 7580 O O    . HOH   G 4 .   ? 33.950 -9.291  -8.881  1.00 32.46 ?  353 HOH   B O    1 
HETATM 7581 O O    . HOH   G 4 .   ? 44.274 -37.371 -17.717 1.00 39.28 ?  354 HOH   B O    1 
HETATM 7582 O O    . HOH   G 4 .   ? 27.876 -26.696 -0.432  1.00 31.88 ?  355 HOH   B O    1 
HETATM 7583 O O    . HOH   G 4 .   ? 55.773 -8.261  10.898  1.00 26.18 ?  356 HOH   B O    1 
HETATM 7584 O O    . HOH   G 4 .   ? 56.644 -7.276  3.068   1.00 30.31 ?  357 HOH   B O    1 
HETATM 7585 O O    . HOH   G 4 .   ? 36.340 -8.538  -9.751  1.00 34.65 ?  358 HOH   B O    1 
HETATM 7586 O O    . HOH   G 4 .   ? 34.182 -7.771  11.467  1.00 41.17 ?  359 HOH   B O    1 
HETATM 7587 O O    . HOH   G 4 .   ? 43.321 -12.793 -21.136 1.00 31.37 ?  360 HOH   B O    1 
HETATM 7588 O O    . HOH   G 4 .   ? 61.673 -19.937 1.885   1.00 41.25 ?  361 HOH   B O    1 
HETATM 7589 O O    . HOH   G 4 .   ? 27.238 -25.981 -11.317 1.00 36.38 ?  362 HOH   B O    1 
HETATM 7590 O O    . HOH   G 4 .   ? 57.054 -21.690 -16.401 1.00 43.39 ?  363 HOH   B O    1 
HETATM 7591 O O    . HOH   G 4 .   ? 40.323 -8.864  9.890   1.00 41.71 ?  364 HOH   B O    1 
HETATM 7592 O O    . HOH   G 4 .   ? 48.343 -26.529 8.957   1.00 48.20 ?  365 HOH   B O    1 
HETATM 7593 O O    . HOH   G 4 .   ? 40.488 -11.327 -13.979 1.00 34.45 ?  366 HOH   B O    1 
HETATM 7594 O O    . HOH   G 4 .   ? 36.219 -8.688  9.084   1.00 38.32 ?  367 HOH   B O    1 
HETATM 7595 O O    . HOH   G 4 .   ? 54.335 -5.801  3.007   1.00 37.17 ?  368 HOH   B O    1 
HETATM 7596 O O    . HOH   G 4 .   ? 39.933 -7.057  7.786   1.00 44.24 ?  369 HOH   B O    1 
HETATM 7597 O O    . HOH   G 4 .   ? 32.759 -23.739 14.114  1.00 40.64 ?  370 HOH   B O    1 
HETATM 7598 O O    . HOH   G 4 .   ? 42.029 -10.078 -17.418 1.00 62.87 ?  371 HOH   B O    1 
HETATM 7599 O O    . HOH   G 4 .   ? 59.104 -10.329 9.332   1.00 39.70 ?  372 HOH   B O    1 
HETATM 7600 O O    . HOH   G 4 .   ? 63.060 -12.395 6.977   1.00 40.16 ?  373 HOH   B O    1 
HETATM 7601 O O    . HOH   G 4 .   ? 42.052 -6.718  -4.854  1.00 48.95 ?  374 HOH   B O    1 
HETATM 7602 O O    . HOH   G 4 .   ? 56.127 -7.761  -0.569  1.00 34.11 ?  375 HOH   B O    1 
HETATM 7603 O O    . HOH   G 4 .   ? 52.097 -13.023 13.436  1.00 26.64 ?  376 HOH   B O    1 
HETATM 7604 O O    . HOH   G 4 .   ? 36.632 -22.919 13.339  1.00 36.41 ?  377 HOH   B O    1 
HETATM 7605 O O    . HOH   G 4 .   ? 40.221 -7.767  3.216   1.00 45.27 ?  378 HOH   B O    1 
HETATM 7606 O O    . HOH   G 4 .   ? 44.294 -5.653  -3.517  1.00 43.89 ?  379 HOH   B O    1 
HETATM 7607 O O    . HOH   G 4 .   ? 38.122 -10.529 10.071  1.00 30.90 ?  380 HOH   B O    1 
HETATM 7608 O O    . HOH   G 4 .   ? 42.834 -17.107 -23.206 1.00 41.50 ?  381 HOH   B O    1 
HETATM 7609 O O    . HOH   G 4 .   ? 46.736 -5.521  2.968   1.00 37.07 ?  382 HOH   B O    1 
HETATM 7610 O O    . HOH   G 4 .   ? 60.561 -22.351 2.920   1.00 41.86 ?  383 HOH   B O    1 
HETATM 7611 O O    . HOH   G 4 .   ? 39.713 -14.056 15.675  1.00 44.57 ?  384 HOH   B O    1 
HETATM 7612 O O    . HOH   G 4 .   ? 53.010 -29.994 7.331   1.00 24.97 ?  385 HOH   B O    1 
HETATM 7613 O O    . HOH   G 4 .   ? 25.919 -18.921 -11.883 1.00 44.05 ?  386 HOH   B O    1 
HETATM 7614 O O    . HOH   G 4 .   ? 41.085 -9.863  15.846  1.00 48.38 ?  387 HOH   B O    1 
HETATM 7615 O O    . HOH   G 4 .   ? 35.451 -33.821 7.395   1.00 44.18 ?  388 HOH   B O    1 
HETATM 7616 O O    . HOH   G 4 .   ? 35.353 -20.417 13.333  1.00 39.18 ?  389 HOH   B O    1 
HETATM 7617 O O    . HOH   G 4 .   ? 24.019 -20.931 -7.684  1.00 29.22 ?  390 HOH   B O    1 
HETATM 7618 O O    . HOH   G 4 .   ? 40.889 -6.606  -0.867  1.00 26.65 ?  391 HOH   B O    1 
HETATM 7619 O O    . HOH   G 4 .   ? 44.283 -31.867 -3.782  1.00 41.06 ?  392 HOH   B O    1 
HETATM 7620 O O    . HOH   G 4 .   ? 28.066 -27.122 2.293   1.00 34.71 ?  393 HOH   B O    1 
HETATM 7621 O O    . HOH   G 4 .   ? 26.741 -28.041 -13.569 1.00 42.23 ?  394 HOH   B O    1 
HETATM 7622 O O    . HOH   G 4 .   ? 50.757 -30.965 8.819   1.00 32.34 ?  395 HOH   B O    1 
HETATM 7623 O O    . HOH   G 4 .   ? 24.750 -20.607 -10.550 1.00 45.68 ?  396 HOH   B O    1 
HETATM 7624 O O    . HOH   G 4 .   ? 34.445 -33.485 9.661   1.00 42.78 ?  397 HOH   B O    1 
HETATM 7625 O O    . HOH   G 4 .   ? 26.893 -30.698 -12.521 1.00 31.33 ?  398 HOH   B O    1 
HETATM 7626 O O    . HOH   G 4 .   ? 57.785 -6.607  -2.242  1.00 35.49 ?  399 HOH   B O    1 
HETATM 7627 O O    . HOH   G 4 .   ? 45.857 -20.085 15.329  1.00 38.14 ?  400 HOH   B O    1 
HETATM 7628 O O    . HOH   G 4 .   ? 41.042 -11.800 -22.306 1.00 37.13 ?  401 HOH   B O    1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   A VAL   A 3   ? 0.7328 0.7376 0.8285 0.0057  -0.0329 0.0804  3   VAL   A N   
2    N N   B VAL   A 3   ? 0.7258 0.7084 0.8099 -0.0061 -0.0262 0.0680  3   VAL   A N   
3    C CA  A VAL   A 3   ? 0.7299 0.7345 0.8170 0.0034  -0.0305 0.0820  3   VAL   A CA  
4    C CA  B VAL   A 3   ? 0.7224 0.7040 0.7952 -0.0076 -0.0249 0.0695  3   VAL   A CA  
5    C C   A VAL   A 3   ? 0.7126 0.7198 0.7836 -0.0069 -0.0327 0.0863  3   VAL   A C   
6    C C   B VAL   A 3   ? 0.7032 0.6857 0.7536 -0.0161 -0.0275 0.0697  3   VAL   A C   
7    O O   A VAL   A 3   ? 0.7160 0.7234 0.8006 -0.0043 -0.0359 0.0889  3   VAL   A O   
8    O O   B VAL   A 3   ? 0.7073 0.6897 0.7662 -0.0142 -0.0296 0.0687  3   VAL   A O   
9    C CB  A VAL   A 3   ? 0.7407 0.7437 0.8291 0.0091  -0.0262 0.0792  3   VAL   A CB  
10   C CB  B VAL   A 3   ? 0.7347 0.7160 0.8107 -0.0023 -0.0212 0.0692  3   VAL   A CB  
11   C CG1 A VAL   A 3   ? 0.7443 0.7462 0.8314 0.0116  -0.0252 0.0786  3   VAL   A CG1 
12   C CG1 B VAL   A 3   ? 0.7385 0.7192 0.8147 -0.0000 -0.0204 0.0698  3   VAL   A CG1 
13   C CG2 A VAL   A 3   ? 0.7443 0.7469 0.8309 0.0107  -0.0247 0.0791  3   VAL   A CG2 
14   C CG2 B VAL   A 3   ? 0.7389 0.7200 0.8152 -0.0006 -0.0199 0.0698  3   VAL   A CG2 
31   N N   A ASN   A 4   ? 0.6892 0.6994 0.7208 -0.0207 -0.0296 0.0869  4   ASN   A N   
32   N N   B ASN   A 4   ? 0.6765 0.6594 0.6864 -0.0276 -0.0263 0.0713  4   ASN   A N   
33   C CA  A ASN   A 4   ? 0.6614 0.6757 0.6479 -0.0349 -0.0257 0.0838  4   ASN   A CA  
34   C CA  B ASN   A 4   ? 0.6455 0.6302 0.6099 -0.0399 -0.0239 0.0699  4   ASN   A CA  
35   C C   A ASN   A 4   ? 0.6189 0.6472 0.6195 -0.0499 -0.0156 0.0613  4   ASN   A C   
36   C C   B ASN   A 4   ? 0.6009 0.5981 0.5708 -0.0560 -0.0076 0.0558  4   ASN   A C   
37   O O   A ASN   A 4   ? 0.6210 0.6493 0.6214 -0.0514 -0.0146 0.0632  4   ASN   A O   
38   O O   B ASN   A 4   ? 0.6030 0.6002 0.5673 -0.0570 -0.0062 0.0598  4   ASN   A O   
39   C CB  A ASN   A 4   ? 0.6731 0.6788 0.5967 -0.0353 -0.0301 0.1021  4   ASN   A CB  
40   C CB  B ASN   A 4   ? 0.6568 0.6320 0.5676 -0.0379 -0.0356 0.0826  4   ASN   A CB  
41   C CG  A ASN   A 4   ? 0.6817 0.6801 0.5488 -0.0356 -0.0334 0.1174  4   ASN   A CG  
42   C CG  B ASN   A 4   ? 0.6647 0.6319 0.5270 -0.0364 -0.0458 0.0925  4   ASN   A CG  
43   O OD1 A ASN   A 4   ? 0.6857 0.6814 0.5299 -0.0361 -0.0344 0.1229  4   ASN   A OD1 
44   O OD1 B ASN   A 4   ? 0.6678 0.6313 0.5099 -0.0356 -0.0498 0.0966  4   ASN   A OD1 
45   N ND2 A ASN   A 4   ? 0.6835 0.6800 0.5377 -0.0354 -0.0341 0.1239  4   ASN   A ND2 
46   N ND2 B ASN   A 4   ? 0.6666 0.6314 0.5191 -0.0351 -0.0488 0.0979  4   ASN   A ND2 
59   N N   A SER   A 5   ? 0.5706 0.6142 0.5826 -0.0651 -0.0068 0.0368  5   SER   A N   
60   N N   B SER   A 5   ? 0.5510 0.5617 0.5303 -0.0717 0.0082  0.0379  5   SER   A N   
61   C CA  A SER   A 5   ? 0.5188 0.5785 0.5415 -0.0805 0.0075  0.0154  5   SER   A CA  
62   C CA  B SER   A 5   ? 0.4984 0.5226 0.4885 -0.0890 0.0301  0.0226  5   SER   A CA  
63   C C   A SER   A 5   ? 0.4599 0.5324 0.4809 -0.0940 0.0283  0.0095  5   SER   A C   
64   C C   B SER   A 5   ? 0.4423 0.4771 0.4183 -0.1008 0.0606  0.0189  5   SER   A C   
65   O O   A SER   A 5   ? 0.4638 0.5351 0.4827 -0.0945 0.0324  0.0041  5   SER   A O   
66   O O   B SER   A 5   ? 0.4445 0.4787 0.4076 -0.1027 0.0711  0.0084  5   SER   A O   
67   C CB  A SER   A 5   ? 0.5256 0.5873 0.5644 -0.0830 0.0028  0.0041  5   SER   A CB  
68   C CB  B SER   A 5   ? 0.5027 0.5292 0.5222 -0.0908 0.0238  0.0153  5   SER   A CB  
69   O OG  A SER   A 5   ? 0.5293 0.5914 0.5771 -0.0856 -0.0005 -0.0026 5   SER   A OG  
70   O OG  B SER   A 5   ? 0.5055 0.5312 0.5390 -0.0941 0.0186  0.0109  5   SER   A OG  
81   N N   A PHE   A 6   ? 0.3949 0.4818 0.4065 -0.1053 0.0472  0.0154  6   PHE   A N   
82   N N   B PHE   A 6   ? 0.3830 0.4316 0.3510 -0.1093 0.0783  0.0252  6   PHE   A N   
83   C CA  A PHE   A 6   ? 0.3308 0.4271 0.3353 -0.1149 0.0628  0.0263  6   PHE   A CA  
84   C CA  B PHE   A 6   ? 0.3280 0.3859 0.3019 -0.1135 0.0870  0.0320  6   PHE   A CA  
85   C C   A PHE   A 6   ? 0.3081 0.4153 0.3125 -0.1277 0.0803  0.0231  6   PHE   A C   
86   C C   B PHE   A 6   ? 0.3207 0.3787 0.2959 -0.1159 0.1051  0.0225  6   PHE   A C   
87   O O   A PHE   A 6   ? 0.3090 0.4154 0.3431 -0.1340 0.0658  0.0233  6   PHE   A O   
88   O O   B PHE   A 6   ? 0.3269 0.3791 0.3112 -0.1116 0.1097  0.0316  6   PHE   A O   
89   C CB  A PHE   A 6   ? 0.2997 0.3850 0.2917 -0.1056 0.0568  0.0391  6   PHE   A CB  
90   C CB  B PHE   A 6   ? 0.2902 0.3489 0.2711 -0.1089 0.0679  0.0452  6   PHE   A CB  
91   C CG  A PHE   A 6   ? 0.2686 0.3467 0.2627 -0.0966 0.0488  0.0413  6   PHE   A CG  
92   C CG  B PHE   A 6   ? 0.2607 0.3222 0.2525 -0.0980 0.0450  0.0387  6   PHE   A CG  
93   C CD1 A PHE   A 6   ? 0.2532 0.3292 0.2577 -0.0868 0.0387  0.0373  6   PHE   A CD1 
94   C CD1 B PHE   A 6   ? 0.2465 0.3097 0.2477 -0.0879 0.0341  0.0345  6   PHE   A CD1 
95   C CD2 A PHE   A 6   ? 0.2644 0.3343 0.2713 -0.0850 0.0474  0.0416  6   PHE   A CD2 
96   C CD2 B PHE   A 6   ? 0.2570 0.3150 0.2620 -0.0860 0.0432  0.0350  6   PHE   A CD2 
97   C CE1 A PHE   A 6   ? 0.2501 0.3208 0.2656 -0.0822 0.0431  0.0388  6   PHE   A CE1 
98   C CE1 B PHE   A 6   ? 0.2431 0.3003 0.2605 -0.0853 0.0320  0.0341  6   PHE   A CE1 
99   C CE2 A PHE   A 6   ? 0.2602 0.3275 0.2767 -0.0787 0.0470  0.0439  6   PHE   A CE2 
100  C CE2 B PHE   A 6   ? 0.2526 0.3091 0.2720 -0.0795 0.0297  0.0310  6   PHE   A CE2 
101  C CZ  A PHE   A 6   ? 0.2559 0.3236 0.2737 -0.0749 0.0423  0.0345  6   PHE   A CZ  
102  C CZ  B PHE   A 6   ? 0.2481 0.3047 0.2725 -0.0786 0.0241  0.0266  6   PHE   A CZ  
121  N N   A SER   A 7   ? 0.2838 0.3990 0.2674 -0.1295 0.0976  0.0159  7   SER   A N   
122  N N   B SER   A 7   ? 0.3073 0.3684 0.2829 -0.1148 0.1053  0.0000  7   SER   A N   
123  C CA  A SER   A 7   ? 0.2748 0.3922 0.2614 -0.1123 0.0916  -0.0202 7   SER   A CA  
124  C CA  B SER   A 7   ? 0.3040 0.3648 0.3016 -0.1017 0.0950  -0.0248 7   SER   A CA  
125  C C   A SER   A 7   ? 0.2497 0.3600 0.2254 -0.0998 0.1059  -0.0293 7   SER   A C   
126  C C   B SER   A 7   ? 0.2828 0.3477 0.2700 -0.0939 0.1013  -0.0194 7   SER   A C   
127  O O   A SER   A 7   ? 0.2593 0.3554 0.2166 -0.0980 0.1139  -0.0364 7   SER   A O   
128  O O   B SER   A 7   ? 0.2862 0.3531 0.2741 -0.0929 0.1082  -0.0139 7   SER   A O   
129  C CB  A SER   A 7   ? 0.2926 0.4175 0.2995 -0.1021 0.0736  -0.0349 7   SER   A CB  
130  C CB  B SER   A 7   ? 0.3205 0.3827 0.3487 -0.0987 0.0857  -0.0428 7   SER   A CB  
131  O OG  A SER   A 7   ? 0.3135 0.4315 0.3257 -0.0938 0.0485  -0.0487 7   SER   A OG  
132  O OG  B SER   A 7   ? 0.3384 0.3915 0.3977 -0.0953 0.0626  -0.0588 7   SER   A OG  
143  N N   A GLY   A 8   ? 0.2296 0.3283 0.2037 -0.0845 0.0966  -0.0411 8   GLY   A N   
144  N N   B GLY   A 8   ? 0.2642 0.3320 0.2553 -0.0817 0.0888  -0.0153 8   GLY   A N   
145  C CA  A GLY   A 8   ? 0.2095 0.2958 0.1968 -0.0636 0.1029  -0.0269 8   GLY   A CA  
146  C CA  B GLY   A 8   ? 0.2528 0.3060 0.2497 -0.0630 0.0719  -0.0063 8   GLY   A CA  
147  C C   A GLY   A 8   ? 0.1889 0.2650 0.1986 -0.0414 0.0820  -0.0223 8   GLY   A C   
148  C C   B GLY   A 8   ? 0.2350 0.2766 0.2406 -0.0435 0.0523  -0.0038 8   GLY   A C   
149  O O   A GLY   A 8   ? 0.1799 0.2728 0.2248 -0.0135 0.0736  -0.0287 8   GLY   A O   
150  O O   B GLY   A 8   ? 0.2335 0.2802 0.2545 -0.0222 0.0432  -0.0204 8   GLY   A O   
157  N N   A TYR   A 9   ? 0.1695 0.2324 0.1811 -0.0352 0.0765  -0.0150 9   TYR   A N   
158  N N   B TYR   A 9   ? 0.2146 0.2450 0.2399 -0.0390 0.0443  0.0235  9   TYR   A N   
159  C CA  A TYR   A 9   ? 0.1611 0.2131 0.1708 -0.0305 0.0586  0.0071  9   TYR   A CA  
160  C CA  B TYR   A 9   ? 0.1950 0.2145 0.2117 -0.0338 0.0432  0.0370  9   TYR   A CA  
161  C C   A TYR   A 9   ? 0.1642 0.1918 0.1638 -0.0184 0.0513  0.0230  9   TYR   A C   
162  C C   B TYR   A 9   ? 0.1922 0.1949 0.1956 -0.0216 0.0468  0.0320  9   TYR   A C   
163  O O   A TYR   A 9   ? 0.1859 0.2045 0.1778 -0.0213 0.0476  0.0057  9   TYR   A O   
164  O O   B TYR   A 9   ? 0.2069 0.2085 0.2102 -0.0309 0.0380  0.0344  9   TYR   A O   
165  C CB  A TYR   A 9   ? 0.1462 0.2113 0.1848 -0.0219 0.0452  0.0069  9   TYR   A CB  
166  C CB  B TYR   A 9   ? 0.1843 0.2190 0.2115 -0.0217 0.0357  0.0371  9   TYR   A CB  
167  C CG  A TYR   A 9   ? 0.1464 0.2142 0.1846 -0.0107 0.0499  0.0072  9   TYR   A CG  
168  C CG  B TYR   A 9   ? 0.1827 0.2215 0.2079 -0.0178 0.0297  0.0326  9   TYR   A CG  
169  C CD1 A TYR   A 9   ? 0.1511 0.2169 0.2108 -0.0137 0.0392  -0.0046 9   TYR   A CD1 
170  C CD1 B TYR   A 9   ? 0.1903 0.2117 0.2115 -0.0243 0.0326  0.0289  9   TYR   A CD1 
171  C CD2 A TYR   A 9   ? 0.1422 0.2187 0.1992 -0.0055 0.0455  0.0195  9   TYR   A CD2 
172  C CD2 B TYR   A 9   ? 0.1732 0.2193 0.1969 -0.0045 0.0307  0.0369  9   TYR   A CD2 
173  C CE1 A TYR   A 9   ? 0.1589 0.2192 0.2322 -0.0094 0.0459  -0.0069 9   TYR   A CE1 
174  C CE1 B TYR   A 9   ? 0.1885 0.2082 0.2054 -0.0204 0.0460  0.0278  9   TYR   A CE1 
175  C CE2 A TYR   A 9   ? 0.1567 0.2236 0.2274 -0.0140 0.0360  0.0038  9   TYR   A CE2 
176  C CE2 B TYR   A 9   ? 0.1783 0.2224 0.1984 -0.0025 0.0305  0.0366  9   TYR   A CE2 
177  C CZ  A TYR   A 9   ? 0.1593 0.2236 0.2475 -0.0284 0.0469  -0.0066 9   TYR   A CZ  
178  C CZ  B TYR   A 9   ? 0.1769 0.2104 0.2002 -0.0098 0.0553  0.0420  9   TYR   A CZ  
179  O OH  A TYR   A 9   ? 0.1715 0.2300 0.2796 -0.0423 0.0343  -0.0068 9   TYR   A OH  
180  O OH  B TYR   A 9   ? 0.1643 0.2185 0.2181 -0.0056 0.0485  0.0534  9   TYR   A OH  
199  N N   A LEU   A 10  ? 0.1717 0.1683 0.1718 -0.0148 0.0354  0.0174  10  LEU   A N   
200  N N   B LEU   A 10  ? 0.1883 0.1762 0.1891 -0.0161 0.0407  0.0077  10  LEU   A N   
201  C CA  A LEU   A 10  ? 0.1679 0.1667 0.1797 -0.0240 0.0330  0.0262  10  LEU   A CA  
202  C CA  B LEU   A 10  ? 0.1841 0.1718 0.1931 -0.0132 0.0291  -0.0023 10  LEU   A CA  
203  C C   A LEU   A 10  ? 0.1585 0.1634 0.1880 -0.0207 0.0277  0.0296  10  LEU   A C   
204  C C   B LEU   A 10  ? 0.1808 0.1504 0.1951 -0.0203 0.0240  0.0065  10  LEU   A C   
205  O O   A LEU   A 10  ? 0.1568 0.1542 0.1747 -0.0164 0.0436  0.0334  10  LEU   A O   
206  O O   B LEU   A 10  ? 0.1739 0.1456 0.1826 -0.0137 0.0332  0.0061  10  LEU   A O   
207  C CB  A LEU   A 10  ? 0.1756 0.1726 0.2163 -0.0238 0.0288  0.0404  10  LEU   A CB  
208  C CB  B LEU   A 10  ? 0.1910 0.1745 0.1937 -0.0171 0.0137  0.0123  10  LEU   A CB  
209  C CG  A LEU   A 10  ? 0.2005 0.1874 0.2706 -0.0258 0.0039  0.0563  10  LEU   A CG  
210  C CG  B LEU   A 10  ? 0.2027 0.1797 0.2257 0.0017  -0.0206 0.0174  10  LEU   A CG  
211  C CD1 A LEU   A 10  ? 0.2045 0.2033 0.2943 -0.0267 0.0031  0.0609  10  LEU   A CD1 
212  C CD1 B LEU   A 10  ? 0.2077 0.1883 0.2471 0.0045  -0.0255 0.0146  10  LEU   A CD1 
213  C CD2 A LEU   A 10  ? 0.2219 0.1944 0.2879 -0.0266 0.0052  0.0454  10  LEU   A CD2 
214  C CD2 B LEU   A 10  ? 0.2196 0.1921 0.2362 -0.0064 -0.0373 0.0209  10  LEU   A CD2 
237  N N   A LYS   A 11  ? 0.1565 0.1609 0.1982 -0.0098 0.0261  0.0275  11  LYS   A N   
238  N N   B LYS   A 11  ? 0.1810 0.1461 0.2059 -0.0282 0.0141  0.0236  11  LYS   A N   
239  C CA  A LYS   A 11  ? 0.1519 0.1499 0.2175 -0.0155 0.0309  0.0343  11  LYS   A CA  
240  C CA  B LYS   A 11  ? 0.1738 0.1475 0.2105 -0.0336 0.0069  0.0355  11  LYS   A CA  
241  C C   A LYS   A 11  ? 0.1563 0.1511 0.2364 -0.0177 0.0461  0.0047  11  LYS   A C   
242  C C   B LYS   A 11  ? 0.1639 0.1369 0.2053 -0.0337 0.0070  0.0267  11  LYS   A C   
243  O O   A LYS   A 11  ? 0.1581 0.1634 0.2587 -0.0340 0.0487  -0.0038 11  LYS   A O   
244  O O   B LYS   A 11  ? 0.1679 0.1429 0.2228 -0.0297 0.0122  0.0096  11  LYS   A O   
245  C CB  A LYS   A 11  ? 0.1553 0.1482 0.2221 -0.0156 0.0333  0.0350  11  LYS   A CB  
246  C CB  B LYS   A 11  ? 0.1810 0.1542 0.2158 -0.0358 -0.0053 0.0245  11  LYS   A CB  
247  C CG  A LYS   A 11  ? 0.1625 0.1589 0.2292 -0.0099 0.0214  0.0389  11  LYS   A CG  
248  C CG  B LYS   A 11  ? 0.1831 0.1728 0.2123 -0.0273 -0.0004 0.0404  11  LYS   A CG  
249  C CD  A LYS   A 11  ? 0.1671 0.1723 0.2222 -0.0181 0.0111  0.0426  11  LYS   A CD  
250  C CD  B LYS   A 11  ? 0.1920 0.1769 0.2192 -0.0214 0.0146  0.0475  11  LYS   A CD  
251  C CE  A LYS   A 11  ? 0.1727 0.1815 0.2166 -0.0123 0.0080  0.0482  11  LYS   A CE  
252  C CE  B LYS   A 11  ? 0.2028 0.1796 0.2298 -0.0199 0.0066  0.0421  11  LYS   A CE  
253  N NZ  A LYS   A 11  ? 0.1709 0.1848 0.2083 0.0019  0.0057  0.0574  11  LYS   A NZ  
254  N NZ  B LYS   A 11  ? 0.2073 0.1824 0.2410 -0.0256 0.0066  0.0449  11  LYS   A NZ  
281  N N   A LEU   A 12  ? 0.1487 0.1499 0.2317 -0.0226 0.0423  -0.0018 12  LEU   A N   
282  N N   B LEU   A 12  ? 0.1538 0.1472 0.2072 -0.0142 -0.0195 0.0160  12  LEU   A N   
283  C CA  A LEU   A 12  ? 0.1522 0.1585 0.2235 -0.0165 0.0275  0.0065  12  LEU   A CA  
284  C CA  B LEU   A 12  ? 0.1607 0.1565 0.2001 -0.0089 -0.0115 0.0385  12  LEU   A CA  
285  C C   A LEU   A 12  ? 0.1606 0.1462 0.2194 -0.0163 0.0197  0.0118  12  LEU   A C   
286  C C   B LEU   A 12  ? 0.1608 0.1578 0.2107 -0.0120 0.0054  0.0315  12  LEU   A C   
287  O O   A LEU   A 12  ? 0.1638 0.1452 0.2143 -0.0124 0.0241  -0.0021 12  LEU   A O   
288  O O   B LEU   A 12  ? 0.1666 0.1538 0.2229 -0.0013 0.0129  0.0376  12  LEU   A O   
289  C CB  A LEU   A 12  ? 0.1632 0.1595 0.2321 -0.0153 0.0134  0.0124  12  LEU   A CB  
290  C CB  B LEU   A 12  ? 0.1809 0.1806 0.2216 -0.0087 0.0058  0.0413  12  LEU   A CB  
291  C CG  A LEU   A 12  ? 0.1599 0.1687 0.2142 0.0024  0.0339  0.0231  12  LEU   A CG  
292  C CG  B LEU   A 12  ? 0.1840 0.1947 0.2449 -0.0086 0.0162  0.0487  12  LEU   A CG  
293  C CD1 A LEU   A 12  ? 0.1746 0.1727 0.2271 0.0161  0.0336  0.0319  12  LEU   A CD1 
294  C CD1 B LEU   A 12  ? 0.1890 0.2104 0.2610 0.0033  0.0387  0.0396  12  LEU   A CD1 
295  C CD2 A LEU   A 12  ? 0.1582 0.1687 0.2266 0.0007  0.0344  0.0209  12  LEU   A CD2 
296  C CD2 B LEU   A 12  ? 0.1863 0.2055 0.2516 -0.0057 0.0122  0.0408  12  LEU   A CD2 
319  N N   A THR   A 13  ? 0.1603 0.1414 0.2326 -0.0287 0.0145  0.0250  13  THR   A N   
320  N N   B THR   A 13  ? 0.1614 0.1593 0.2266 -0.0144 0.0061  0.0121  13  THR   A N   
321  C CA  A THR   A 13  ? 0.1501 0.1501 0.2341 -0.0224 0.0243  0.0302  13  THR   A CA  
322  C CA  B THR   A 13  ? 0.1712 0.1703 0.2344 -0.0256 0.0212  0.0264  13  THR   A CA  
323  C C   A THR   A 13  ? 0.1581 0.1518 0.2562 -0.0192 0.0146  0.0448  13  THR   A C   
324  C C   B THR   A 13  ? 0.1747 0.1844 0.2493 -0.0425 0.0237  0.0321  13  THR   A C   
325  O O   A THR   A 13  ? 0.1560 0.1579 0.2455 -0.0076 0.0106  0.0472  13  THR   A O   
326  O O   B THR   A 13  ? 0.1816 0.1941 0.2383 -0.0465 0.0113  0.0394  13  THR   A O   
327  C CB  A THR   A 13  ? 0.1534 0.1687 0.2303 -0.0130 0.0167  0.0192  13  THR   A CB  
328  C CB  B THR   A 13  ? 0.1765 0.1694 0.2250 -0.0127 0.0213  0.0479  13  THR   A CB  
329  O OG1 A THR   A 13  ? 0.1571 0.1708 0.2515 -0.0189 0.0109  0.0138  13  THR   A OG1 
330  O OG1 B THR   A 13  ? 0.1687 0.1578 0.2383 -0.0145 0.0238  0.0611  13  THR   A OG1 
331  C CG2 A THR   A 13  ? 0.1583 0.1790 0.2123 -0.0014 0.0223  0.0108  13  THR   A CG2 
332  C CG2 B THR   A 13  ? 0.1795 0.1663 0.2193 0.0014  0.0237  0.0427  13  THR   A CG2 
347  N N   A ASP   A 14  ? 0.1587 0.1534 0.2661 -0.0215 -0.0021 0.0623  14  ASP   A N   
348  N N   B ASP   A 14  ? 0.1718 0.1906 0.2750 -0.0478 0.0092  0.0335  14  ASP   A N   
349  C CA  A ASP   A 14  ? 0.1731 0.1795 0.2762 -0.0282 -0.0087 0.0620  14  ASP   A CA  
350  C CA  B ASP   A 14  ? 0.1825 0.1997 0.2834 -0.0393 -0.0033 0.0342  14  ASP   A CA  
351  C C   A ASP   A 14  ? 0.1727 0.1861 0.2434 -0.0293 -0.0022 0.0720  14  ASP   A C   
352  C C   B ASP   A 14  ? 0.1674 0.1869 0.2493 -0.0372 -0.0167 0.0528  14  ASP   A C   
353  O O   A ASP   A 14  ? 0.1892 0.1922 0.2491 -0.0457 -0.0135 0.0691  14  ASP   A O   
354  O O   B ASP   A 14  ? 0.1820 0.1805 0.2606 -0.0460 -0.0335 0.0696  14  ASP   A O   
355  C CB  A ASP   A 14  ? 0.2054 0.2046 0.3279 -0.0387 -0.0124 0.0826  14  ASP   A CB  
356  C CB  B ASP   A 14  ? 0.2078 0.2323 0.3350 -0.0226 -0.0136 0.0372  14  ASP   A CB  
357  C CG  A ASP   A 14  ? 0.2376 0.2369 0.3917 -0.0434 -0.0087 0.0832  14  ASP   A CG  
358  C CG  B ASP   A 14  ? 0.2342 0.2733 0.3867 -0.0042 -0.0140 0.0327  14  ASP   A CG  
359  O OD1 A ASP   A 14  ? 0.2574 0.2538 0.4141 -0.0234 -0.0281 0.1065  14  ASP   A OD1 
360  O OD1 B ASP   A 14  ? 0.2420 0.2809 0.4092 0.0213  -0.0193 0.0422  14  ASP   A OD1 
361  O OD2 A ASP   A 14  ? 0.2464 0.2559 0.4253 -0.0523 -0.0172 0.0492  14  ASP   A OD2 
362  O OD2 B ASP   A 14  ? 0.2363 0.2881 0.4187 -0.0063 -0.0175 0.0202  14  ASP   A OD2 
371  N N   A ASN   A 15  ? 0.1628 0.1908 0.2324 -0.0263 0.0135  0.0724  15  ASN   A N   
372  N N   B ASN   A 15  ? 0.1485 0.1769 0.2374 -0.0370 0.0005  0.0510  15  ASN   A N   
373  C CA  A ASN   A 15  ? 0.1677 0.1912 0.2398 -0.0216 -0.0011 0.0600  15  ASN   A CA  
374  C CA  B ASN   A 15  ? 0.1501 0.1697 0.2492 -0.0295 -0.0099 0.0361  15  ASN   A CA  
375  C C   A ASN   A 15  ? 0.1584 0.1839 0.2338 -0.0321 0.0000  0.0502  15  ASN   A C   
376  C C   B ASN   A 15  ? 0.1428 0.1761 0.2566 -0.0223 0.0056  0.0409  15  ASN   A C   
377  O O   A ASN   A 15  ? 0.1551 0.1764 0.2330 -0.0311 0.0031  0.0334  15  ASN   A O   
378  O O   B ASN   A 15  ? 0.1311 0.1666 0.2586 -0.0126 0.0203  0.0324  15  ASN   A O   
379  C CB  A ASN   A 15  ? 0.1732 0.1920 0.2422 -0.0174 0.0063  0.0641  15  ASN   A CB  
380  C CB  B ASN   A 15  ? 0.1528 0.1705 0.2431 -0.0379 -0.0214 0.0299  15  ASN   A CB  
381  C CG  A ASN   A 15  ? 0.1679 0.1906 0.2436 -0.0206 0.0273  0.0527  15  ASN   A CG  
382  C CG  B ASN   A 15  ? 0.1559 0.1803 0.2529 -0.0310 -0.0202 0.0337  15  ASN   A CG  
383  O OD1 A ASN   A 15  ? 0.1754 0.1908 0.2553 -0.0299 0.0318  0.0423  15  ASN   A OD1 
384  O OD1 B ASN   A 15  ? 0.1713 0.1861 0.2639 -0.0285 -0.0089 0.0215  15  ASN   A OD1 
385  N ND2 A ASN   A 15  ? 0.1652 0.1848 0.2450 -0.0220 0.0353  0.0561  15  ASN   A ND2 
386  N ND2 B ASN   A 15  ? 0.1634 0.1770 0.2492 -0.0233 -0.0294 0.0385  15  ASN   A ND2 
399  N N   A VAL   A 16  ? 0.1558 0.1865 0.2317 -0.0236 -0.0001 0.0556  16  VAL   A N   
400  N N   B VAL   A 16  ? 0.1511 0.1927 0.2540 -0.0138 0.0017  0.0554  16  VAL   A N   
401  C CA  A VAL   A 16  ? 0.1549 0.1818 0.2208 -0.0236 0.0042  0.0584  16  VAL   A CA  
402  C CA  B VAL   A 16  ? 0.1584 0.2029 0.2381 -0.0088 0.0056  0.0632  16  VAL   A CA  
403  C C   A VAL   A 16  ? 0.1536 0.1686 0.2208 -0.0338 0.0063  0.0490  16  VAL   A C   
404  C C   B VAL   A 16  ? 0.1594 0.2088 0.2316 -0.0162 0.0083  0.0632  16  VAL   A C   
405  O O   A VAL   A 16  ? 0.1503 0.1648 0.2163 -0.0453 0.0052  0.0389  16  VAL   A O   
406  O O   B VAL   A 16  ? 0.1611 0.2136 0.2121 -0.0253 0.0117  0.0598  16  VAL   A O   
407  C CB  A VAL   A 16  ? 0.1605 0.1839 0.2302 -0.0075 0.0214  0.0728  16  VAL   A CB  
408  C CB  B VAL   A 16  ? 0.1704 0.2051 0.2440 0.0020  0.0183  0.0687  16  VAL   A CB  
409  C CG1 A VAL   A 16  ? 0.1723 0.1953 0.2381 0.0024  0.0267  0.0597  16  VAL   A CG1 
410  C CG1 B VAL   A 16  ? 0.1827 0.2145 0.2527 0.0084  0.0169  0.0570  16  VAL   A CG1 
411  C CG2 A VAL   A 16  ? 0.1639 0.1851 0.2532 -0.0015 0.0319  0.0603  16  VAL   A CG2 
412  C CG2 B VAL   A 16  ? 0.1781 0.2069 0.2570 -0.0021 0.0236  0.0620  16  VAL   A CG2 
431  N N   A TYR   A 17  ? 0.1546 0.1507 0.2242 -0.0242 0.0167  0.0537  17  TYR   A N   
432  N N   B TYR   A 17  ? 0.1597 0.2033 0.2314 -0.0096 0.0076  0.0612  17  TYR   A N   
433  C CA  A TYR   A 17  ? 0.1579 0.1595 0.2042 -0.0360 0.0095  0.0581  17  TYR   A CA  
434  C CA  B TYR   A 17  ? 0.1570 0.2040 0.1961 -0.0238 -0.0024 0.0621  17  TYR   A CA  
435  C C   A TYR   A 17  ? 0.1473 0.1600 0.2022 -0.0299 0.0072  0.0473  17  TYR   A C   
436  C C   B TYR   A 17  ? 0.1628 0.2009 0.2008 -0.0251 -0.0047 0.0665  17  TYR   A C   
437  O O   A TYR   A 17  ? 0.1307 0.1564 0.2060 -0.0303 0.0064  0.0458  17  TYR   A O   
438  O O   B TYR   A 17  ? 0.1564 0.1910 0.1991 -0.0423 -0.0010 0.0614  17  TYR   A O   
439  C CB  A TYR   A 17  ? 0.1846 0.1607 0.2188 -0.0390 -0.0180 0.0719  17  TYR   A CB  
440  C CB  B TYR   A 17  ? 0.1565 0.2057 0.2041 -0.0288 -0.0164 0.0546  17  TYR   A CB  
441  C CG  A TYR   A 17  ? 0.2077 0.1684 0.2305 -0.0335 -0.0376 0.0795  17  TYR   A CG  
442  C CG  B TYR   A 17  ? 0.1630 0.2144 0.2070 -0.0190 -0.0134 0.0507  17  TYR   A CG  
443  C CD1 A TYR   A 17  ? 0.2144 0.1786 0.2496 -0.0300 -0.0585 0.0697  17  TYR   A CD1 
444  C CD1 B TYR   A 17  ? 0.1727 0.2203 0.2295 -0.0052 -0.0052 0.0543  17  TYR   A CD1 
445  C CD2 A TYR   A 17  ? 0.2200 0.1806 0.2296 -0.0449 -0.0282 0.0893  17  TYR   A CD2 
446  C CD2 B TYR   A 17  ? 0.1665 0.2208 0.1945 -0.0220 -0.0160 0.0563  17  TYR   A CD2 
447  C CE1 A TYR   A 17  ? 0.2216 0.1843 0.2484 -0.0363 -0.0606 0.0710  17  TYR   A CE1 
448  C CE1 B TYR   A 17  ? 0.1807 0.2227 0.2283 -0.0054 0.0019  0.0550  17  TYR   A CE1 
449  C CE2 A TYR   A 17  ? 0.2286 0.1876 0.2412 -0.0434 -0.0486 0.0794  17  TYR   A CE2 
450  C CE2 B TYR   A 17  ? 0.1719 0.2193 0.2119 -0.0138 -0.0053 0.0542  17  TYR   A CE2 
451  C CZ  A TYR   A 17  ? 0.2279 0.1795 0.2343 -0.0429 -0.0616 0.0705  17  TYR   A CZ  
452  C CZ  B TYR   A 17  ? 0.1805 0.2186 0.2244 -0.0042 -0.0023 0.0574  17  TYR   A CZ  
453  O OH  A TYR   A 17  ? 0.2331 0.1837 0.2477 -0.0413 -0.0559 0.0502  17  TYR   A OH  
454  O OH  B TYR   A 17  ? 0.1914 0.2256 0.2615 0.0057  0.0026  0.0490  17  TYR   A OH  
473  N N   A ILE   A 18  ? 0.1503 0.1568 0.2000 -0.0335 0.0238  0.0572  18  ILE   A N   
474  N N   B ILE   A 18  ? 0.1637 0.1959 0.2007 -0.0264 -0.0003 0.0646  18  ILE   A N   
475  C CA  A ILE   A 18  ? 0.1568 0.1682 0.1905 -0.0235 0.0334  0.0537  18  ILE   A CA  
476  C CA  B ILE   A 18  ? 0.1629 0.1959 0.1704 -0.0098 -0.0064 0.0555  18  ILE   A CA  
477  C C   A ILE   A 18  ? 0.1725 0.1752 0.1930 -0.0349 0.0444  0.0557  18  ILE   A C   
478  C C   B ILE   A 18  ? 0.1661 0.2091 0.1643 -0.0125 -0.0085 0.0572  18  ILE   A C   
479  O O   A ILE   A 18  ? 0.1649 0.1850 0.1795 -0.0520 0.0349  0.0430  18  ILE   A O   
480  O O   B ILE   A 18  ? 0.1677 0.2259 0.1791 -0.0263 -0.0008 0.0405  18  ILE   A O   
481  C CB  A ILE   A 18  ? 0.1739 0.1845 0.1772 -0.0128 0.0283  0.0506  18  ILE   A CB  
482  C CB  B ILE   A 18  ? 0.1789 0.1996 0.1472 0.0070  0.0015  0.0607  18  ILE   A CB  
483  C CG1 A ILE   A 18  ? 0.1829 0.2024 0.1625 -0.0178 0.0115  0.0436  18  ILE   A CG1 
484  C CG1 B ILE   A 18  ? 0.1942 0.2164 0.1590 0.0082  0.0074  0.0782  18  ILE   A CG1 
485  C CG2 A ILE   A 18  ? 0.1771 0.1842 0.1735 -0.0052 0.0252  0.0420  18  ILE   A CG2 
486  C CG2 B ILE   A 18  ? 0.1893 0.2065 0.1666 0.0016  0.0056  0.0518  18  ILE   A CG2 
487  C CD1 A ILE   A 18  ? 0.2071 0.2231 0.2034 -0.0054 0.0100  0.0385  18  ILE   A CD1 
488  C CD1 B ILE   A 18  ? 0.2176 0.2334 0.1704 0.0112  0.0053  0.0818  18  ILE   A CD1 
511  N N   A LYS   A 19  ? 0.1768 0.1781 0.2242 -0.0271 0.0619  0.0563  19  LYS   A N   
512  N N   B LYS   A 19  ? 0.1726 0.2106 0.1920 0.0021  0.0180  0.0479  19  LYS   A N   
513  C CA  A LYS   A 19  ? 0.1876 0.1855 0.2228 -0.0187 0.0503  0.0454  19  LYS   A CA  
514  C CA  B LYS   A 19  ? 0.1803 0.2198 0.2123 0.0136  0.0297  0.0432  19  LYS   A CA  
515  C C   A LYS   A 19  ? 0.1745 0.1779 0.2100 -0.0127 0.0666  0.0391  19  LYS   A C   
516  C C   B LYS   A 19  ? 0.1588 0.2113 0.2342 0.0137  0.0323  0.0506  19  LYS   A C   
517  O O   A LYS   A 19  ? 0.1644 0.1703 0.2162 -0.0104 0.0621  0.0452  19  LYS   A O   
518  O O   B LYS   A 19  ? 0.1510 0.2053 0.2567 0.0091  0.0056  0.0555  19  LYS   A O   
519  C CB  A LYS   A 19  ? 0.1991 0.2054 0.2127 -0.0122 0.0554  0.0576  19  LYS   A CB  
520  C CB  B LYS   A 19  ? 0.1951 0.2271 0.2030 0.0191  0.0472  0.0240  19  LYS   A CB  
521  C CG  A LYS   A 19  ? 0.2178 0.2168 0.2195 0.0050  0.0555  0.0654  19  LYS   A CG  
522  C CG  B LYS   A 19  ? 0.2192 0.2484 0.2039 0.0270  0.0563  0.0147  19  LYS   A CG  
523  C CD  A LYS   A 19  ? 0.2386 0.2232 0.2286 0.0173  0.0667  0.0636  19  LYS   A CD  
524  C CD  B LYS   A 19  ? 0.2388 0.2657 0.1996 0.0350  0.0645  0.0136  19  LYS   A CD  
525  C CE  A LYS   A 19  ? 0.2490 0.2238 0.2453 0.0110  0.0662  0.0588  19  LYS   A CE  
526  C CE  B LYS   A 19  ? 0.2491 0.2819 0.2167 0.0283  0.0603  0.0107  19  LYS   A CE  
527  N NZ  A LYS   A 19  ? 0.2516 0.2240 0.2487 -0.0043 0.0851  0.0534  19  LYS   A NZ  
528  N NZ  B LYS   A 19  ? 0.2568 0.2875 0.2265 0.0313  0.0522  0.0040  19  LYS   A NZ  
555  N N   A ASN   A 20  ? 0.1887 0.1974 0.2142 -0.0138 0.0472  0.0461  20  ASN   A N   
556  N N   B ASN   A 20  ? 0.1546 0.2181 0.2502 0.0045  0.0227  0.0587  20  ASN   A N   
557  C CA  A ASN   A 20  ? 0.1921 0.2150 0.2094 0.0041  0.0324  0.0438  20  ASN   A CA  
558  C CA  B ASN   A 20  ? 0.1465 0.2287 0.2502 0.0204  0.0167  0.0601  20  ASN   A CA  
559  C C   A ASN   A 20  ? 0.1963 0.2316 0.1994 0.0048  0.0376  0.0364  20  ASN   A C   
560  C C   B ASN   A 20  ? 0.1687 0.2335 0.2482 0.0180  0.0308  0.0720  20  ASN   A C   
561  O O   A ASN   A 20  ? 0.1921 0.2406 0.1657 -0.0061 0.0331  0.0324  20  ASN   A O   
562  O O   B ASN   A 20  ? 0.1894 0.2460 0.2727 0.0178  0.0266  0.0788  20  ASN   A O   
563  C CB  A ASN   A 20  ? 0.2047 0.2122 0.2211 0.0090  0.0273  0.0328  20  ASN   A CB  
564  C CB  B ASN   A 20  ? 0.1430 0.2340 0.2500 0.0140  0.0123  0.0562  20  ASN   A CB  
565  C CG  A ASN   A 20  ? 0.2227 0.2114 0.2306 0.0169  0.0289  0.0218  20  ASN   A CG  
566  C CG  B ASN   A 20  ? 0.1436 0.2346 0.2392 0.0172  0.0121  0.0534  20  ASN   A CG  
567  O OD1 A ASN   A 20  ? 0.2530 0.2317 0.2786 0.0203  0.0266  0.0184  20  ASN   A OD1 
568  O OD1 B ASN   A 20  ? 0.1473 0.2278 0.2389 0.0293  0.0239  0.0588  20  ASN   A OD1 
569  N ND2 A ASN   A 20  ? 0.2312 0.1896 0.2275 0.0134  0.0224  0.0326  20  ASN   A ND2 
570  N ND2 B ASN   A 20  ? 0.1608 0.2379 0.2360 0.0158  -0.0032 0.0644  20  ASN   A ND2 
583  N N   A ALA   A 21  ? 0.2043 0.2315 0.2223 0.0045  0.0332  0.0239  21  ALA   A N   
584  N N   B ALA   A 21  ? 0.1802 0.2237 0.2447 -0.0019 0.0525  0.0562  21  ALA   A N   
585  C CA  A ALA   A 21  ? 0.2143 0.2230 0.2247 0.0011  0.0193  0.0467  21  ALA   A CA  
586  C CA  B ALA   A 21  ? 0.1960 0.2077 0.2384 -0.0138 0.0518  0.0673  21  ALA   A CA  
587  C C   A ALA   A 21  ? 0.2248 0.2211 0.2328 -0.0015 0.0173  0.0221  21  ALA   A C   
588  C C   B ALA   A 21  ? 0.1856 0.1896 0.2123 -0.0157 0.0494  0.0437  21  ALA   A C   
589  O O   A ALA   A 21  ? 0.2239 0.2308 0.2344 -0.0087 0.0184  0.0042  21  ALA   A O   
590  O O   B ALA   A 21  ? 0.1752 0.1805 0.2022 -0.0203 0.0484  0.0205  21  ALA   A O   
591  C CB  A ALA   A 21  ? 0.2121 0.2338 0.2392 -0.0073 0.0033  0.0643  21  ALA   A CB  
592  C CB  B ALA   A 21  ? 0.2161 0.2307 0.2706 -0.0194 0.0334  0.0639  21  ALA   A CB  
603  N N   A ASP   A 22  ? 0.2337 0.2091 0.2385 -0.0028 0.0229  0.0162  22  ASP   A N   
604  N N   B ASP   A 22  ? 0.1841 0.1827 0.2046 -0.0150 0.0683  0.0312  22  ASP   A N   
605  C CA  A ASP   A 22  ? 0.2402 0.1994 0.2267 0.0057  0.0162  0.0303  22  ASP   A CA  
606  C CA  B ASP   A 22  ? 0.1943 0.1739 0.1919 -0.0079 0.0655  0.0218  22  ASP   A CA  
607  C C   A ASP   A 22  ? 0.2309 0.2012 0.2021 0.0013  0.0076  0.0386  22  ASP   A C   
608  C C   B ASP   A 22  ? 0.1807 0.1661 0.1532 -0.0237 0.0749  0.0088  22  ASP   A C   
609  O O   A ASP   A 22  ? 0.2300 0.2060 0.2057 0.0005  -0.0003 0.0258  22  ASP   A O   
610  O O   B ASP   A 22  ? 0.1750 0.1761 0.1652 -0.0370 0.0781  -0.0119 22  ASP   A O   
611  C CB  A ASP   A 22  ? 0.2653 0.2031 0.2579 0.0124  0.0189  0.0149  22  ASP   A CB  
612  C CB  B ASP   A 22  ? 0.2248 0.1841 0.2199 0.0097  0.0686  0.0078  22  ASP   A CB  
613  C CG  A ASP   A 22  ? 0.2768 0.2116 0.2756 0.0026  0.0058  0.0300  22  ASP   A CG  
614  C CG  B ASP   A 22  ? 0.2383 0.1687 0.2291 0.0230  0.0634  0.0086  22  ASP   A CG  
615  O OD1 A ASP   A 22  ? 0.2627 0.2073 0.2776 -0.0222 -0.0119 0.0568  22  ASP   A OD1 
616  O OD1 B ASP   A 22  ? 0.2234 0.1468 0.1824 0.0025  0.0575  0.0045  22  ASP   A OD1 
617  O OD2 A ASP   A 22  ? 0.2988 0.2219 0.2940 0.0092  0.0075  0.0043  22  ASP   A OD2 
618  O OD2 B ASP   A 22  ? 0.2719 0.1900 0.2738 0.0238  0.0635  0.0214  22  ASP   A OD2 
627  N N   A ILE   A 23  ? 0.2257 0.2017 0.1980 -0.0098 0.0113  0.0317  23  ILE   A N   
628  N N   B ILE   A 23  ? 0.1743 0.1571 0.1595 -0.0243 0.0646  0.0214  23  ILE   A N   
629  C CA  A ILE   A 23  ? 0.2130 0.1937 0.1749 -0.0128 0.0191  0.0309  23  ILE   A CA  
630  C CA  B ILE   A 23  ? 0.1648 0.1686 0.1594 -0.0185 0.0446  0.0203  23  ILE   A CA  
631  C C   A ILE   A 23  ? 0.1985 0.2011 0.1821 -0.0081 0.0345  0.0226  23  ILE   A C   
632  C C   B ILE   A 23  ? 0.1625 0.1762 0.1523 -0.0261 0.0450  0.0150  23  ILE   A C   
633  O O   A ILE   A 23  ? 0.2023 0.2065 0.1960 -0.0164 0.0225  0.0108  23  ILE   A O   
634  O O   B ILE   A 23  ? 0.1622 0.1718 0.1611 -0.0300 0.0228  0.0096  23  ILE   A O   
635  C CB  A ILE   A 23  ? 0.2201 0.1863 0.1407 -0.0164 0.0253  0.0248  23  ILE   A CB  
636  C CB  B ILE   A 23  ? 0.1663 0.1712 0.1594 0.0057  0.0378  0.0223  23  ILE   A CB  
637  C CG1 A ILE   A 23  ? 0.2244 0.1849 0.1315 -0.0228 0.0250  0.0176  23  ILE   A CG1 
638  C CG1 B ILE   A 23  ? 0.1655 0.1723 0.1720 0.0087  0.0279  0.0149  23  ILE   A CG1 
639  C CG2 A ILE   A 23  ? 0.2205 0.1921 0.1601 -0.0116 0.0441  0.0314  23  ILE   A CG2 
640  C CG2 B ILE   A 23  ? 0.1632 0.1688 0.1651 0.0355  0.0499  0.0215  23  ILE   A CG2 
641  C CD1 A ILE   A 23  ? 0.2272 0.1885 0.1442 -0.0249 0.0131  0.0135  23  ILE   A CD1 
642  C CD1 B ILE   A 23  ? 0.1467 0.1786 0.1939 0.0189  0.0099  0.0093  23  ILE   A CD1 
665  N N   A VAL   A 24  ? 0.1939 0.2081 0.1929 -0.0136 0.0310  0.0166  24  VAL   A N   
666  N N   B VAL   A 24  ? 0.1718 0.1877 0.1573 -0.0312 0.0395  -0.0076 24  VAL   A N   
667  C CA  A VAL   A 24  ? 0.2034 0.2127 0.2112 -0.0191 0.0189  0.0053  24  VAL   A CA  
668  C CA  B VAL   A 24  ? 0.1938 0.1936 0.2012 -0.0318 0.0256  0.0058  24  VAL   A CA  
669  C C   A VAL   A 24  ? 0.1961 0.2265 0.2283 -0.0308 0.0050  -0.0011 24  VAL   A C   
670  C C   B VAL   A 24  ? 0.1934 0.2102 0.2213 -0.0351 0.0318  -0.0044 24  VAL   A C   
671  O O   A VAL   A 24  ? 0.1979 0.2267 0.2377 -0.0214 0.0134  0.0164  24  VAL   A O   
672  O O   B VAL   A 24  ? 0.2053 0.2147 0.2468 -0.0292 0.0357  0.0085  24  VAL   A O   
673  C CB  A VAL   A 24  ? 0.2088 0.2147 0.2206 -0.0245 0.0276  0.0151  24  VAL   A CB  
674  C CB  B VAL   A 24  ? 0.2008 0.1944 0.2164 -0.0400 0.0145  0.0139  24  VAL   A CB  
675  C CG1 A VAL   A 24  ? 0.2129 0.2274 0.2136 -0.0116 0.0385  -0.0041 24  VAL   A CG1 
676  C CG1 B VAL   A 24  ? 0.2202 0.2162 0.2431 -0.0316 0.0039  0.0178  24  VAL   A CG1 
677  C CG2 A VAL   A 24  ? 0.2178 0.2133 0.2297 -0.0233 0.0372  0.0237  24  VAL   A CG2 
678  C CG2 B VAL   A 24  ? 0.2066 0.1841 0.2225 -0.0481 0.0098  0.0019  24  VAL   A CG2 
697  N N   A GLU   A 25  ? 0.1996 0.2505 0.2238 -0.0411 0.0071  -0.0185 25  GLU   A N   
698  N N   B GLU   A 25  ? 0.1881 0.2353 0.2145 -0.0313 0.0519  -0.0076 25  GLU   A N   
699  C CA  A GLU   A 25  ? 0.2198 0.2759 0.2368 -0.0321 0.0082  -0.0128 25  GLU   A CA  
700  C CA  B GLU   A 25  ? 0.1969 0.2574 0.2173 -0.0247 0.0532  -0.0097 25  GLU   A CA  
701  C C   A GLU   A 25  ? 0.2129 0.2787 0.1978 -0.0373 0.0335  -0.0047 25  GLU   A C   
702  C C   B GLU   A 25  ? 0.1913 0.2641 0.2113 -0.0244 0.0616  -0.0036 25  GLU   A C   
703  O O   A GLU   A 25  ? 0.2153 0.2949 0.2029 -0.0374 0.0294  -0.0110 25  GLU   A O   
704  O O   B GLU   A 25  ? 0.2073 0.2754 0.2263 -0.0220 0.0709  -0.0142 25  GLU   A O   
705  C CB  A GLU   A 25  ? 0.2446 0.2952 0.2773 -0.0310 -0.0049 -0.0171 25  GLU   A CB  
706  C CB  B GLU   A 25  ? 0.2141 0.2710 0.2379 -0.0279 0.0601  -0.0124 25  GLU   A CB  
707  C CG  A GLU   A 25  ? 0.2716 0.3172 0.3254 -0.0355 -0.0285 -0.0278 25  GLU   A CG  
708  C CG  B GLU   A 25  ? 0.2508 0.2907 0.3079 -0.0365 0.0378  -0.0228 25  GLU   A CG  
709  C CD  A GLU   A 25  ? 0.2894 0.3430 0.3665 -0.0313 -0.0479 -0.0302 25  GLU   A CD  
710  C CD  B GLU   A 25  ? 0.2799 0.3066 0.3805 -0.0406 0.0192  -0.0285 25  GLU   A CD  
711  O OE1 A GLU   A 25  ? 0.2999 0.3543 0.3719 -0.0245 -0.0658 -0.0410 25  GLU   A OE1 
712  O OE1 B GLU   A 25  ? 0.2900 0.3171 0.4116 -0.0415 0.0117  -0.0313 25  GLU   A OE1 
713  O OE2 A GLU   A 25  ? 0.2954 0.3568 0.4000 -0.0304 -0.0485 -0.0254 25  GLU   A OE2 
714  O OE2 B GLU   A 25  ? 0.2838 0.3087 0.4093 -0.0460 0.0133  -0.0283 25  GLU   A OE2 
727  N N   A GLU   A 26  ? 0.2060 0.2698 0.1826 -0.0601 0.0417  -0.0037 26  GLU   A N   
728  N N   B GLU   A 26  ? 0.1855 0.2652 0.2120 -0.0297 0.0532  0.0012  26  GLU   A N   
729  C CA  A GLU   A 26  ? 0.2205 0.2634 0.1735 -0.0689 0.0493  0.0115  26  GLU   A CA  
730  C CA  B GLU   A 26  ? 0.1988 0.2672 0.2050 -0.0249 0.0437  0.0127  26  GLU   A CA  
731  C C   A GLU   A 26  ? 0.2205 0.2466 0.1680 -0.0630 0.0406  0.0075  26  GLU   A C   
732  C C   B GLU   A 26  ? 0.1989 0.2470 0.1901 -0.0136 0.0348  0.0234  26  GLU   A C   
733  O O   A GLU   A 26  ? 0.2264 0.2453 0.1642 -0.0683 0.0387  0.0032  26  GLU   A O   
734  O O   B GLU   A 26  ? 0.2123 0.2520 0.1845 -0.0252 0.0447  0.0176  26  GLU   A O   
735  C CB  A GLU   A 26  ? 0.2380 0.2693 0.2083 -0.0792 0.0533  0.0316  26  GLU   A CB  
736  C CB  B GLU   A 26  ? 0.2110 0.2913 0.2301 -0.0267 0.0276  0.0028  26  GLU   A CB  
737  C CG  A GLU   A 26  ? 0.2511 0.2877 0.2882 -0.0822 0.0604  0.0170  26  GLU   A CG  
738  C CG  B GLU   A 26  ? 0.2185 0.3119 0.2606 -0.0304 0.0341  0.0012  26  GLU   A CG  
739  C CD  A GLU   A 26  ? 0.2513 0.2953 0.3356 -0.0867 0.0798  0.0097  26  GLU   A CD  
740  C CD  B GLU   A 26  ? 0.2156 0.3234 0.2732 -0.0332 0.0494  0.0069  26  GLU   A CD  
741  O OE1 A GLU   A 26  ? 0.2419 0.3016 0.3507 -0.0738 0.1018  -0.0252 26  GLU   A OE1 
742  O OE1 B GLU   A 26  ? 0.2219 0.3349 0.2818 -0.0286 0.0658  0.0055  26  GLU   A OE1 
743  O OE2 A GLU   A 26  ? 0.2622 0.3061 0.3483 -0.0888 0.0770  0.0225  26  GLU   A OE2 
744  O OE2 B GLU   A 26  ? 0.2137 0.3280 0.2396 -0.0346 0.0605  0.0158  26  GLU   A OE2 
757  N N   A ALA   A 27  ? 0.2051 0.2353 0.1753 -0.0626 0.0436  0.0094  27  ALA   A N   
758  N N   B ALA   A 27  ? 0.1796 0.2231 0.1681 0.0008  0.0214  0.0429  27  ALA   A N   
759  C CA  A ALA   A 27  ? 0.2043 0.2369 0.1783 -0.0516 0.0537  0.0132  27  ALA   A CA  
760  C CA  B ALA   A 27  ? 0.1791 0.2175 0.1679 0.0107  0.0157  0.0486  27  ALA   A CA  
761  C C   A ALA   A 27  ? 0.2223 0.2651 0.2028 -0.0515 0.0566  0.0083  27  ALA   A C   
762  C C   B ALA   A 27  ? 0.1893 0.2370 0.1715 0.0135  0.0105  0.0479  27  ALA   A C   
763  O O   A ALA   A 27  ? 0.2270 0.2650 0.2229 -0.0525 0.0389  -0.0019 27  ALA   A O   
764  O O   B ALA   A 27  ? 0.1816 0.2366 0.1925 0.0041  0.0122  0.0455  27  ALA   A O   
765  C CB  A ALA   A 27  ? 0.1963 0.2146 0.1821 -0.0489 0.0453  0.0144  27  ALA   A CB  
766  C CB  B ALA   A 27  ? 0.1727 0.2044 0.1863 -0.0026 0.0192  0.0318  27  ALA   A CB  
777  N N   A LYS   A 28  ? 0.2500 0.2933 0.2246 -0.0488 0.0561  -0.0170 28  LYS   A N   
778  N N   B LYS   A 28  ? 0.2127 0.2550 0.1831 0.0312  -0.0009 0.0192  28  LYS   A N   
779  C CA  A LYS   A 28  ? 0.2860 0.3313 0.2655 -0.0273 0.0559  -0.0313 28  LYS   A CA  
780  C CA  B LYS   A 28  ? 0.2490 0.2916 0.2064 0.0546  -0.0101 -0.0203 28  LYS   A CA  
781  C C   A LYS   A 28  ? 0.3010 0.3605 0.2727 -0.0335 0.0652  -0.0258 28  LYS   A C   
782  C C   B LYS   A 28  ? 0.2705 0.3154 0.2064 0.0615  -0.0110 -0.0112 28  LYS   A C   
783  O O   A LYS   A 28  ? 0.3063 0.3687 0.3051 -0.0229 0.0564  -0.0354 28  LYS   A O   
784  O O   B LYS   A 28  ? 0.2831 0.3275 0.2135 0.0586  -0.0366 -0.0107 28  LYS   A O   
785  C CB  A LYS   A 28  ? 0.3126 0.3475 0.3244 -0.0084 0.0464  -0.0364 28  LYS   A CB  
786  C CB  B LYS   A 28  ? 0.2781 0.3110 0.2695 0.0679  -0.0254 -0.0456 28  LYS   A CB  
787  C CG  A LYS   A 28  ? 0.3388 0.3641 0.3816 0.0100  0.0421  -0.0375 28  LYS   A CG  
788  C CG  B LYS   A 28  ? 0.3030 0.3330 0.3334 0.0739  -0.0302 -0.0562 28  LYS   A CG  
789  C CD  A LYS   A 28  ? 0.3575 0.3825 0.4412 0.0239  0.0301  -0.0381 28  LYS   A CD  
790  C CD  B LYS   A 28  ? 0.3303 0.3588 0.4115 0.0759  -0.0415 -0.0557 28  LYS   A CD  
791  C CE  A LYS   A 28  ? 0.3715 0.3926 0.4773 0.0347  0.0213  -0.0444 28  LYS   A CE  
792  C CE  B LYS   A 28  ? 0.3536 0.3761 0.4633 0.0741  -0.0518 -0.0613 28  LYS   A CE  
793  N NZ  A LYS   A 28  ? 0.3805 0.3984 0.5042 0.0419  0.0229  -0.0559 28  LYS   A NZ  
794  N NZ  B LYS   A 28  ? 0.3622 0.3836 0.4912 0.0787  -0.0582 -0.0707 28  LYS   A NZ  
821  N N   A LYS   A 29  ? 0.3065 0.3828 0.2551 -0.0539 0.0927  0.0023  29  LYS   A N   
822  N N   B LYS   A 29  ? 0.2721 0.3298 0.2083 0.0592  0.0278  0.0101  29  LYS   A N   
823  C CA  A LYS   A 29  ? 0.3241 0.4091 0.2633 -0.0623 0.1044  0.0144  29  LYS   A CA  
824  C CA  B LYS   A 29  ? 0.2805 0.3482 0.2135 0.0575  0.0479  0.0280  29  LYS   A CA  
825  C C   A LYS   A 29  ? 0.3243 0.4042 0.2469 -0.0759 0.0868  0.0240  29  LYS   A C   
826  C C   B LYS   A 29  ? 0.2752 0.3368 0.1832 0.0469  0.0412  0.0450  29  LYS   A C   
827  O O   A LYS   A 29  ? 0.3342 0.4176 0.2838 -0.0714 0.0795  0.0151  29  LYS   A O   
828  O O   B LYS   A 29  ? 0.2770 0.3480 0.1930 0.0554  0.0285  0.0421  29  LYS   A O   
829  C CB  A LYS   A 29  ? 0.3395 0.4378 0.3044 -0.0546 0.1223  0.0135  29  LYS   A CB  
830  C CB  B LYS   A 29  ? 0.2999 0.3772 0.2610 0.0608  0.0770  0.0185  29  LYS   A CB  
831  C CG  A LYS   A 29  ? 0.3598 0.4653 0.3610 -0.0430 0.1225  0.0129  29  LYS   A CG  
832  C CG  B LYS   A 29  ? 0.3255 0.4051 0.3228 0.0635  0.0902  0.0144  29  LYS   A CG  
833  C CD  A LYS   A 29  ? 0.3804 0.4877 0.4298 -0.0338 0.1168  0.0083  29  LYS   A CD  
834  C CD  B LYS   A 29  ? 0.3478 0.4272 0.3945 0.0667  0.0943  0.0112  29  LYS   A CD  
835  C CE  A LYS   A 29  ? 0.3957 0.5019 0.4721 -0.0277 0.1174  0.0067  29  LYS   A CE  
836  C CE  B LYS   A 29  ? 0.3631 0.4426 0.4417 0.0676  0.0993  0.0066  29  LYS   A CE  
837  N NZ  A LYS   A 29  ? 0.4012 0.5098 0.5024 -0.0228 0.1162  0.0052  29  LYS   A NZ  
838  N NZ  B LYS   A 29  ? 0.3690 0.4509 0.4764 0.0698  0.0973  0.0077  29  LYS   A NZ  
865  N N   A VAL   A 30  ? 0.3171 0.3841 0.2165 -0.0893 0.0750  0.0386  30  VAL   A N   
866  N N   B VAL   A 30  ? 0.2649 0.3181 0.1718 0.0251  0.0500  0.0536  30  VAL   A N   
867  C CA  A VAL   A 30  ? 0.3172 0.3644 0.2056 -0.0981 0.0533  0.0451  30  VAL   A CA  
868  C CA  B VAL   A 30  ? 0.2561 0.2969 0.1826 -0.0014 0.0320  0.0576  30  VAL   A CA  
869  C C   A VAL   A 30  ? 0.3154 0.3454 0.1728 -0.0867 0.0435  0.0454  30  VAL   A C   
870  C C   B VAL   A 30  ? 0.2594 0.2889 0.1612 -0.0097 0.0208  0.0490  30  VAL   A C   
871  O O   A VAL   A 30  ? 0.3226 0.3521 0.1993 -0.0749 0.0279  0.0426  30  VAL   A O   
872  O O   B VAL   A 30  ? 0.2713 0.2938 0.1809 -0.0108 0.0017  0.0492  30  VAL   A O   
873  C CB  A VAL   A 30  ? 0.3174 0.3618 0.2425 -0.1175 0.0436  0.0489  30  VAL   A CB  
874  C CB  B VAL   A 30  ? 0.2502 0.2853 0.2307 -0.0190 0.0258  0.0667  30  VAL   A CB  
875  C CG1 A VAL   A 30  ? 0.3216 0.3566 0.2444 -0.1235 0.0390  0.0530  30  VAL   A CG1 
876  C CG1 B VAL   A 30  ? 0.2584 0.2819 0.2459 -0.0203 0.0170  0.0629  30  VAL   A CG1 
877  C CG2 A VAL   A 30  ? 0.3157 0.3672 0.2712 -0.1242 0.0492  0.0452  30  VAL   A CG2 
878  C CG2 B VAL   A 30  ? 0.2446 0.2816 0.2515 -0.0252 0.0280  0.0818  30  VAL   A CG2 
897  N N   A LYS   A 31  ? 0.3019 0.3199 0.1516 -0.0846 0.0376  0.0362  31  LYS   A N   
898  N N   B LYS   A 31  ? 0.2542 0.2808 0.1740 -0.0182 0.0218  0.0310  31  LYS   A N   
899  C CA  A LYS   A 31  ? 0.3122 0.3144 0.1828 -0.0660 0.0089  0.0307  31  LYS   A CA  
900  C CA  B LYS   A 31  ? 0.2675 0.2871 0.2130 -0.0141 0.0067  0.0237  31  LYS   A CA  
901  C C   A LYS   A 31  ? 0.2903 0.2849 0.1295 -0.0498 -0.0107 0.0498  31  LYS   A C   
902  C C   B LYS   A 31  ? 0.2464 0.2721 0.1709 -0.0064 0.0041  0.0396  31  LYS   A C   
903  O O   A LYS   A 31  ? 0.2928 0.2897 0.1147 -0.0391 -0.0257 0.0547  31  LYS   A O   
904  O O   B LYS   A 31  ? 0.2554 0.2770 0.1960 -0.0012 0.0037  0.0317  31  LYS   A O   
905  C CB  A LYS   A 31  ? 0.3499 0.3449 0.2920 -0.0582 -0.0149 0.0063  31  LYS   A CB  
906  C CB  B LYS   A 31  ? 0.3019 0.3155 0.3024 -0.0169 -0.0132 -0.0041 31  LYS   A CB  
907  C CG  A LYS   A 31  ? 0.3891 0.3738 0.4020 -0.0491 -0.0341 -0.0108 31  LYS   A CG  
908  C CG  B LYS   A 31  ? 0.3411 0.3455 0.4007 -0.0164 -0.0327 -0.0257 31  LYS   A CG  
909  C CD  A LYS   A 31  ? 0.4227 0.3942 0.4848 -0.0421 -0.0492 -0.0222 31  LYS   A CD  
910  C CD  B LYS   A 31  ? 0.3673 0.3653 0.4739 -0.0149 -0.0538 -0.0446 31  LYS   A CD  
911  C CE  A LYS   A 31  ? 0.4435 0.4134 0.5429 -0.0368 -0.0602 -0.0299 31  LYS   A CE  
912  C CE  B LYS   A 31  ? 0.3831 0.3847 0.5229 -0.0169 -0.0724 -0.0589 31  LYS   A CE  
913  N NZ  A LYS   A 31  ? 0.4539 0.4190 0.5742 -0.0315 -0.0688 -0.0330 31  LYS   A NZ  
914  N NZ  B LYS   A 31  ? 0.3966 0.3959 0.5513 -0.0169 -0.0784 -0.0691 31  LYS   A NZ  
941  N N   A PRO   A 32  ? 0.2645 0.2544 0.1307 -0.0534 -0.0045 0.0402  32  PRO   A N   
942  N N   B PRO   A 32  ? 0.2239 0.2531 0.1591 -0.0102 0.0140  0.0324  32  PRO   A N   
943  C CA  A PRO   A 32  ? 0.2535 0.2388 0.1441 -0.0505 -0.0111 0.0572  32  PRO   A CA  
944  C CA  B PRO   A 32  ? 0.2152 0.2481 0.1560 -0.0095 0.0100  0.0479  32  PRO   A CA  
945  C C   A PRO   A 32  ? 0.2432 0.2335 0.1546 -0.0400 -0.0106 0.0536  32  PRO   A C   
946  C C   B PRO   A 32  ? 0.2107 0.2489 0.1577 0.0003  0.0031  0.0449  32  PRO   A C   
947  O O   A PRO   A 32  ? 0.2345 0.2257 0.1533 -0.0507 -0.0170 0.0295  32  PRO   A O   
948  O O   B PRO   A 32  ? 0.2041 0.2515 0.1587 0.0001  0.0012  0.0442  32  PRO   A O   
949  C CB  A PRO   A 32  ? 0.2579 0.2486 0.1675 -0.0540 -0.0070 0.0446  32  PRO   A CB  
950  C CB  B PRO   A 32  ? 0.2106 0.2541 0.1744 -0.0147 0.0182  0.0314  32  PRO   A CB  
951  C CG  A PRO   A 32  ? 0.2576 0.2540 0.1620 -0.0519 -0.0099 0.0337  32  PRO   A CG  
952  C CG  B PRO   A 32  ? 0.2170 0.2599 0.1742 -0.0103 0.0192  0.0182  32  PRO   A CG  
953  C CD  A PRO   A 32  ? 0.2556 0.2514 0.1328 -0.0540 -0.0087 0.0367  32  PRO   A CD  
954  C CD  B PRO   A 32  ? 0.2169 0.2582 0.1562 -0.0113 0.0216  0.0197  32  PRO   A CD  
969  N N   A THR   A 33  ? 0.2468 0.2356 0.1652 -0.0291 -0.0113 0.0578  33  THR   A N   
970  N N   B THR   A 33  ? 0.2148 0.2457 0.1533 0.0044  -0.0031 0.0407  33  THR   A N   
971  C CA  A THR   A 33  ? 0.2380 0.2378 0.1616 -0.0245 -0.0309 0.0460  33  THR   A CA  
972  C CA  B THR   A 33  ? 0.2154 0.2395 0.1475 0.0145  -0.0250 0.0424  33  THR   A CA  
973  C C   A THR   A 33  ? 0.2088 0.2224 0.1494 -0.0284 -0.0292 0.0386  33  THR   A C   
974  C C   B THR   A 33  ? 0.1934 0.2172 0.1470 0.0141  -0.0088 0.0279  33  THR   A C   
975  O O   A THR   A 33  ? 0.1991 0.2193 0.1731 -0.0320 -0.0196 0.0400  33  THR   A O   
976  O O   B THR   A 33  ? 0.1846 0.2007 0.1704 0.0138  0.0016  0.0163  33  THR   A O   
977  C CB  A THR   A 33  ? 0.2608 0.2600 0.2019 -0.0160 -0.0231 0.0596  33  THR   A CB  
978  C CB  B THR   A 33  ? 0.2473 0.2615 0.1711 0.0163  -0.0160 0.0636  33  THR   A CB  
979  O OG1 A THR   A 33  ? 0.2812 0.2769 0.2273 -0.0028 -0.0161 0.0761  33  THR   A OG1 
980  O OG1 B THR   A 33  ? 0.2678 0.2846 0.1936 0.0283  -0.0243 0.0846  33  THR   A OG1 
981  C CG2 A THR   A 33  ? 0.2664 0.2675 0.2279 -0.0128 -0.0350 0.0569  33  THR   A CG2 
982  C CG2 B THR   A 33  ? 0.2539 0.2688 0.1969 0.0117  -0.0114 0.0545  33  THR   A CG2 
997  N N   A VAL   A 34  ? 0.1890 0.2108 0.1152 -0.0367 -0.0234 0.0373  34  VAL   A N   
998  N N   B VAL   A 34  ? 0.1778 0.2117 0.1309 -0.0020 0.0018  0.0283  34  VAL   A N   
999  C CA  A VAL   A 34  ? 0.1846 0.1999 0.1205 -0.0310 -0.0153 0.0259  34  VAL   A CA  
1000 C CA  B VAL   A 34  ? 0.1772 0.2062 0.1334 -0.0020 0.0029  0.0260  34  VAL   A CA  
1001 C C   A VAL   A 34  ? 0.1761 0.1857 0.1296 -0.0297 0.0042  0.0275  34  VAL   A C   
1002 C C   B VAL   A 34  ? 0.1745 0.1927 0.1439 -0.0138 0.0112  0.0402  34  VAL   A C   
1003 O O   A VAL   A 34  ? 0.1710 0.1885 0.1310 -0.0317 0.0101  0.0075  34  VAL   A O   
1004 O O   B VAL   A 34  ? 0.1825 0.1961 0.1642 -0.0243 0.0099  0.0526  34  VAL   A O   
1005 C CB  A VAL   A 34  ? 0.1900 0.1975 0.1158 -0.0361 0.0002  0.0146  34  VAL   A CB  
1006 C CB  B VAL   A 34  ? 0.1816 0.2103 0.1729 -0.0047 0.0051  0.0129  34  VAL   A CB  
1007 C CG1 A VAL   A 34  ? 0.2026 0.2027 0.1257 -0.0345 0.0132  0.0159  34  VAL   A CG1 
1008 C CG1 B VAL   A 34  ? 0.1969 0.2154 0.1779 0.0020  0.0090  0.0083  34  VAL   A CG1 
1009 C CG2 A VAL   A 34  ? 0.2051 0.2082 0.1648 -0.0206 0.0018  0.0008  34  VAL   A CG2 
1010 C CG2 B VAL   A 34  ? 0.1898 0.2203 0.2100 -0.0029 0.0050  0.0152  34  VAL   A CG2 
1029 N N   . VAL   A 35  ? 0.1687 0.1795 0.1420 -0.0278 -0.0008 0.0327  35  VAL   A N   
1030 C CA  . VAL   A 35  ? 0.1572 0.1676 0.1437 -0.0257 0.0140  0.0291  35  VAL   A CA  
1031 C C   . VAL   A 35  ? 0.1513 0.1555 0.1416 -0.0142 0.0249  0.0195  35  VAL   A C   
1032 O O   . VAL   A 35  ? 0.1510 0.1689 0.1524 -0.0188 0.0216  0.0136  35  VAL   A O   
1033 C CB  . VAL   A 35  ? 0.1721 0.1740 0.1474 -0.0153 0.0123  0.0055  35  VAL   A CB  
1034 C CG1 . VAL   A 35  ? 0.1886 0.1827 0.1554 -0.0134 0.0167  0.0057  35  VAL   A CG1 
1035 C CG2 . VAL   A 35  ? 0.1768 0.1755 0.1646 -0.0155 0.0215  0.0051  35  VAL   A CG2 
1046 N N   . VAL   A 36  ? 0.1494 0.1584 0.1344 -0.0176 0.0016  0.0270  36  VAL   A N   
1047 C CA  . VAL   A 36  ? 0.1337 0.1475 0.1256 -0.0064 -0.0017 0.0066  36  VAL   A CA  
1048 C C   . VAL   A 36  ? 0.1403 0.1536 0.1497 -0.0150 0.0170  0.0195  36  VAL   A C   
1049 O O   . VAL   A 36  ? 0.1424 0.1481 0.1628 -0.0145 0.0261  0.0192  36  VAL   A O   
1050 C CB  . VAL   A 36  ? 0.1375 0.1516 0.1387 -0.0112 0.0046  0.0210  36  VAL   A CB  
1051 C CG1 . VAL   A 36  ? 0.1430 0.1608 0.1442 -0.0216 0.0061  -0.0012 36  VAL   A CG1 
1052 C CG2 . VAL   A 36  ? 0.1474 0.1610 0.1751 -0.0074 -0.0002 0.0354  36  VAL   A CG2 
1062 N N   . ASN   A 37  ? 0.1367 0.1392 0.1375 -0.0096 0.0084  0.0166  37  ASN   A N   
1063 C CA  . ASN   A 37  ? 0.1387 0.1327 0.1280 -0.0081 0.0011  0.0281  37  ASN   A CA  
1064 C C   . ASN   A 37  ? 0.1457 0.1359 0.1288 -0.0124 0.0067  0.0371  37  ASN   A C   
1065 O O   . ASN   A 37  ? 0.1433 0.1495 0.1331 -0.0028 0.0041  0.0103  37  ASN   A O   
1066 C CB  . ASN   A 37  ? 0.1313 0.1356 0.1464 0.0062  0.0054  0.0264  37  ASN   A CB  
1067 C CG  . ASN   A 37  ? 0.1385 0.1400 0.1522 -0.0072 0.0199  0.0108  37  ASN   A CG  
1068 O OD1 . ASN   A 37  ? 0.1323 0.1465 0.1844 -0.0080 0.0139  0.0177  37  ASN   A OD1 
1069 N ND2 . ASN   A 37  ? 0.1378 0.1410 0.1606 -0.0021 0.0087  0.0347  37  ASN   A ND2 
1076 N N   A ALA   A 38  ? 0.1442 0.1422 0.1315 -0.0044 0.0060  0.0243  38  ALA   A N   
1077 N N   B ALA   A 38  ? 0.1407 0.1477 0.1368 -0.0080 0.0042  0.0425  38  ALA   A N   
1078 C CA  A ALA   A 38  ? 0.1461 0.1423 0.1173 -0.0071 0.0027  0.0036  38  ALA   A CA  
1079 C CA  B ALA   A 38  ? 0.1400 0.1577 0.1393 -0.0074 0.0004  0.0403  38  ALA   A CA  
1080 C C   A ALA   A 38  ? 0.1430 0.1425 0.1403 -0.0021 0.0009  -0.0072 38  ALA   A C   
1081 C C   B ALA   A 38  ? 0.1363 0.1549 0.1571 -0.0014 -0.0032 0.0302  38  ALA   A C   
1082 O O   A ALA   A 38  ? 0.1307 0.1267 0.1374 -0.0047 -0.0024 -0.0050 38  ALA   A O   
1083 O O   B ALA   A 38  ? 0.1229 0.1503 0.1637 -0.0094 -0.0099 0.0252  38  ALA   A O   
1084 C CB  A ALA   A 38  ? 0.1508 0.1506 0.1518 -0.0126 0.0020  0.0122  38  ALA   A CB  
1085 C CB  B ALA   A 38  ? 0.1476 0.1709 0.1689 -0.0103 -0.0125 0.0200  38  ALA   A CB  
1096 N N   A ALA   A 39  ? 0.1324 0.1407 0.1517 -0.0012 0.0053  0.0086  39  ALA   A N   
1097 N N   B ALA   A 39  ? 0.1373 0.1541 0.1702 0.0077  0.0035  0.0421  39  ALA   A N   
1098 C CA  A ALA   A 39  ? 0.1244 0.1262 0.1277 0.0005  0.0046  0.0008  39  ALA   A CA  
1099 C CA  B ALA   A 39  ? 0.1435 0.1561 0.1548 0.0030  0.0078  0.0411  39  ALA   A CA  
1100 C C   A ALA   A 39  ? 0.1261 0.1367 0.1240 0.0024  -0.0169 -0.0004 39  ALA   A C   
1101 C C   B ALA   A 39  ? 0.1279 0.1495 0.1597 0.0003  0.0142  0.0294  39  ALA   A C   
1102 O O   A ALA   A 39  ? 0.1447 0.1378 0.1265 -0.0030 -0.0034 -0.0141 39  ALA   A O   
1103 O O   B ALA   A 39  ? 0.1332 0.1503 0.1908 0.0008  0.0117  0.0449  39  ALA   A O   
1104 C CB  A ALA   A 39  ? 0.1119 0.1118 0.1481 -0.0058 0.0037  0.0030  39  ALA   A CB  
1105 C CB  B ALA   A 39  ? 0.1640 0.1659 0.1662 0.0158  0.0001  0.0317  39  ALA   A CB  
1116 N N   A ASN   A 40  ? 0.1295 0.1409 0.1462 -0.0101 0.0046  0.0053  40  ASN   A N   
1117 N N   B ASN   A 40  ? 0.1189 0.1377 0.1541 -0.0055 0.0211  0.0234  40  ASN   A N   
1118 C CA  A ASN   A 40  ? 0.1358 0.1567 0.1507 -0.0120 0.0060  0.0052  40  ASN   A CA  
1119 C CA  B ASN   A 40  ? 0.1302 0.1386 0.1421 0.0029  0.0051  0.0308  40  ASN   A CA  
1120 C C   A ASN   A 40  ? 0.1317 0.1456 0.1287 -0.0053 0.0074  0.0120  40  ASN   A C   
1121 C C   B ASN   A 40  ? 0.1318 0.1370 0.1391 -0.0034 0.0058  0.0310  40  ASN   A C   
1122 O O   A ASN   A 40  ? 0.1255 0.1552 0.1348 0.0005  0.0164  0.0106  40  ASN   A O   
1123 O O   B ASN   A 40  ? 0.1268 0.1359 0.1548 -0.0090 -0.0059 0.0318  40  ASN   A O   
1124 C CB  A ASN   A 40  ? 0.1455 0.1635 0.1781 -0.0080 -0.0025 0.0029  40  ASN   A CB  
1125 C CB  B ASN   A 40  ? 0.1320 0.1360 0.1440 0.0068  -0.0016 0.0161  40  ASN   A CB  
1126 C CG  A ASN   A 40  ? 0.1617 0.1622 0.2126 -0.0102 -0.0082 0.0117  40  ASN   A CG  
1127 C CG  B ASN   A 40  ? 0.1430 0.1322 0.1507 0.0018  -0.0062 0.0135  40  ASN   A CG  
1128 O OD1 A ASN   A 40  ? 0.1673 0.1536 0.1990 -0.0048 -0.0142 0.0289  40  ASN   A OD1 
1129 O OD1 B ASN   A 40  ? 0.1493 0.1223 0.1553 0.0078  -0.0058 0.0087  40  ASN   A OD1 
1130 N ND2 A ASN   A 40  ? 0.1700 0.1737 0.2271 -0.0100 -0.0147 -0.0053 40  ASN   A ND2 
1131 N ND2 B ASN   A 40  ? 0.1481 0.1444 0.1685 0.0020  0.0035  -0.0105 40  ASN   A ND2 
1144 N N   A VAL   A 41  ? 0.1355 0.1418 0.1377 -0.0033 0.0035  0.0170  41  VAL   A N   
1145 N N   B VAL   A 41  ? 0.1352 0.1365 0.1477 0.0008  0.0088  0.0230  41  VAL   A N   
1146 C CA  A VAL   A 41  ? 0.1378 0.1438 0.1349 0.0009  0.0099  0.0055  41  VAL   A CA  
1147 C CA  B VAL   A 41  ? 0.1311 0.1413 0.1510 0.0020  0.0227  0.0221  41  VAL   A CA  
1148 C C   A VAL   A 41  ? 0.1426 0.1477 0.1329 0.0105  0.0105  0.0058  41  VAL   A C   
1149 C C   B VAL   A 41  ? 0.1343 0.1467 0.1328 0.0037  0.0283  0.0199  41  VAL   A C   
1150 O O   A VAL   A 41  ? 0.1459 0.1378 0.1358 0.0079  -0.0002 0.0091  41  VAL   A O   
1151 O O   B VAL   A 41  ? 0.1424 0.1477 0.1395 -0.0022 0.0242  0.0244  41  VAL   A O   
1152 C CB  A VAL   A 41  ? 0.1431 0.1373 0.1168 -0.0097 0.0112  -0.0033 41  VAL   A CB  
1153 C CB  B VAL   A 41  ? 0.1474 0.1576 0.1748 0.0015  0.0312  0.0173  41  VAL   A CB  
1154 C CG1 A VAL   A 41  ? 0.1660 0.1467 0.1493 -0.0050 0.0038  -0.0052 41  VAL   A CG1 
1155 C CG1 B VAL   A 41  ? 0.1741 0.1705 0.1841 0.0022  0.0502  0.0033  41  VAL   A CG1 
1156 C CG2 A VAL   A 41  ? 0.1302 0.1300 0.1101 -0.0054 0.0184  0.0020  41  VAL   A CG2 
1157 C CG2 B VAL   A 41  ? 0.1536 0.1638 0.1861 0.0073  0.0200  0.0046  41  VAL   A CG2 
1176 N N   A TYR   A 42  ? 0.1246 0.1414 0.1487 0.0052  0.0104  0.0049  42  TYR   A N   
1177 N N   B TYR   A 42  ? 0.1312 0.1388 0.1495 0.0041  0.0380  0.0342  42  TYR   A N   
1178 C CA  A TYR   A 42  ? 0.1277 0.1422 0.1599 -0.0013 0.0187  0.0184  42  TYR   A CA  
1179 C CA  B TYR   A 42  ? 0.1365 0.1399 0.1392 0.0085  0.0237  0.0433  42  TYR   A CA  
1180 C C   A TYR   A 42  ? 0.1337 0.1318 0.1578 0.0033  0.0064  0.0103  42  TYR   A C   
1181 C C   B TYR   A 42  ? 0.1339 0.1362 0.1308 -0.0062 0.0257  0.0400  42  TYR   A C   
1182 O O   A TYR   A 42  ? 0.1350 0.1274 0.1782 0.0094  -0.0024 -0.0103 42  TYR   A O   
1183 O O   B TYR   A 42  ? 0.1165 0.1364 0.1479 -0.0309 0.0145  0.0356  42  TYR   A O   
1184 C CB  A TYR   A 42  ? 0.1393 0.1562 0.1665 -0.0001 0.0202  0.0195  42  TYR   A CB  
1185 C CB  B TYR   A 42  ? 0.1437 0.1494 0.1411 0.0130  0.0176  0.0494  42  TYR   A CB  
1186 C CG  A TYR   A 42  ? 0.1457 0.1580 0.1594 -0.0040 0.0283  0.0247  42  TYR   A CG  
1187 C CG  B TYR   A 42  ? 0.1486 0.1510 0.1352 0.0236  0.0089  0.0519  42  TYR   A CG  
1188 C CD1 A TYR   A 42  ? 0.1510 0.1702 0.1745 -0.0109 0.0286  0.0198  42  TYR   A CD1 
1189 C CD1 B TYR   A 42  ? 0.1486 0.1534 0.1542 0.0026  0.0206  0.0500  42  TYR   A CD1 
1190 C CD2 A TYR   A 42  ? 0.1579 0.1708 0.2058 -0.0017 0.0178  0.0191  42  TYR   A CD2 
1191 C CD2 B TYR   A 42  ? 0.1564 0.1681 0.1616 0.0231  0.0111  0.0418  42  TYR   A CD2 
1192 C CE1 A TYR   A 42  ? 0.1510 0.1761 0.1722 -0.0079 0.0247  0.0029  42  TYR   A CE1 
1193 C CE1 B TYR   A 42  ? 0.1498 0.1683 0.1487 0.0011  0.0323  0.0505  42  TYR   A CE1 
1194 C CE2 A TYR   A 42  ? 0.1512 0.1780 0.2125 -0.0132 0.0264  0.0225  42  TYR   A CE2 
1195 C CE2 B TYR   A 42  ? 0.1641 0.1810 0.1678 0.0218  0.0244  0.0428  42  TYR   A CE2 
1196 C CZ  A TYR   A 42  ? 0.1540 0.1813 0.1911 -0.0096 0.0271  0.0073  42  TYR   A CZ  
1197 C CZ  B TYR   A 42  ? 0.1664 0.1795 0.1449 0.0105  0.0304  0.0415  42  TYR   A CZ  
1198 O OH  A TYR   A 42  ? 0.1614 0.1835 0.2281 -0.0049 0.0058  -0.0027 42  TYR   A OH  
1199 O OH  B TYR   A 42  ? 0.1673 0.1806 0.1558 0.0087  0.0318  0.0255  42  TYR   A OH  
1218 N N   . LEU   A 43  ? 0.1402 0.1344 0.1469 -0.0101 0.0191  0.0158  43  LEU   A N   
1219 C CA  . LEU   A 43  ? 0.1336 0.1344 0.1321 -0.0128 0.0135  0.0160  43  LEU   A CA  
1220 C C   . LEU   A 43  ? 0.1392 0.1389 0.1227 -0.0079 0.0067  0.0078  43  LEU   A C   
1221 O O   . LEU   A 43  ? 0.1482 0.1467 0.1776 -0.0017 -0.0047 0.0046  43  LEU   A O   
1222 C CB  . LEU   A 43  ? 0.1467 0.1338 0.1742 -0.0114 0.0073  0.0183  43  LEU   A CB  
1223 C CG  . LEU   A 43  ? 0.1490 0.1312 0.1765 -0.0038 0.0017  0.0123  43  LEU   A CG  
1224 C CD1 . LEU   A 43  ? 0.1573 0.1491 0.1881 -0.0026 0.0081  0.0154  43  LEU   A CD1 
1225 C CD2 . LEU   A 43  ? 0.1555 0.1436 0.1647 -0.0092 -0.0041 0.0294  43  LEU   A CD2 
1238 N N   A LYS   A 44  ? 0.1363 0.1375 0.1397 -0.0072 0.0197  0.0060  44  LYS   A N   
1239 N N   B LYS   A 44  ? 0.1456 0.1407 0.1470 -0.0022 0.0057  0.0129  44  LYS   A N   
1240 C CA  A LYS   A 44  ? 0.1546 0.1398 0.1470 -0.0099 0.0340  0.0111  44  LYS   A CA  
1241 C CA  B LYS   A 44  ? 0.1706 0.1456 0.1630 0.0016  0.0081  0.0209  44  LYS   A CA  
1242 C C   A LYS   A 44  ? 0.1365 0.1310 0.1335 -0.0026 0.0136  -0.0001 44  LYS   A C   
1243 C C   B LYS   A 44  ? 0.1613 0.1445 0.1522 0.0058  -0.0096 0.0075  44  LYS   A C   
1244 O O   A LYS   A 44  ? 0.1453 0.1347 0.1731 0.0039  0.0114  -0.0084 44  LYS   A O   
1245 O O   B LYS   A 44  ? 0.1666 0.1410 0.1714 -0.0061 -0.0047 -0.0060 44  LYS   A O   
1246 C CB  A LYS   A 44  ? 0.1798 0.1581 0.1839 -0.0105 0.0423  0.0043  44  LYS   A CB  
1247 C CB  B LYS   A 44  ? 0.1894 0.1541 0.2033 0.0124  0.0098  0.0274  44  LYS   A CB  
1248 C CG  A LYS   A 44  ? 0.2142 0.1886 0.2674 -0.0222 0.0648  0.0092  44  LYS   A CG  
1249 C CG  B LYS   A 44  ? 0.2131 0.1885 0.2870 0.0118  0.0218  0.0354  44  LYS   A CG  
1250 C CD  A LYS   A 44  ? 0.2586 0.2457 0.3646 -0.0202 0.0559  0.0052  44  LYS   A CD  
1251 C CD  B LYS   A 44  ? 0.2451 0.2461 0.3769 0.0022  0.0085  0.0422  44  LYS   A CD  
1252 C CE  A LYS   A 44  ? 0.2794 0.2741 0.4240 -0.0133 0.0546  0.0008  44  LYS   A CE  
1253 C CE  B LYS   A 44  ? 0.2575 0.2711 0.4283 -0.0059 -0.0015 0.0502  44  LYS   A CE  
1254 N NZ  A LYS   A 44  ? 0.2826 0.2871 0.4417 -0.0150 0.0557  -0.0041 44  LYS   A NZ  
1255 N NZ  B LYS   A 44  ? 0.2657 0.2935 0.4585 -0.0237 -0.0076 0.0501  44  LYS   A NZ  
1282 N N   A HIS   A 45  ? 0.1206 0.1226 0.1378 -0.0128 0.0205  0.0086  45  HIS   A N   
1283 N N   B HIS   A 45  ? 0.1570 0.1479 0.1617 0.0051  -0.0123 0.0168  45  HIS   A N   
1284 C CA  A HIS   A 45  ? 0.1238 0.1209 0.1380 -0.0116 0.0269  0.0048  45  HIS   A CA  
1285 C CA  B HIS   A 45  ? 0.1584 0.1575 0.1616 0.0100  -0.0069 0.0107  45  HIS   A CA  
1286 C C   A HIS   A 45  ? 0.1314 0.1231 0.1468 -0.0011 0.0143  0.0164  45  HIS   A C   
1287 C C   B HIS   A 45  ? 0.1680 0.1628 0.1738 0.0167  -0.0070 0.0132  45  HIS   A C   
1288 O O   A HIS   A 45  ? 0.1360 0.1169 0.1732 -0.0065 0.0118  0.0118  45  HIS   A O   
1289 O O   B HIS   A 45  ? 0.1811 0.1699 0.2091 0.0292  0.0042  0.0115  45  HIS   A O   
1290 C CB  A HIS   A 45  ? 0.1286 0.1153 0.1313 -0.0167 0.0229  0.0073  45  HIS   A CB  
1291 C CB  B HIS   A 45  ? 0.1560 0.1545 0.1377 0.0153  -0.0174 0.0111  45  HIS   A CB  
1292 C CG  A HIS   A 45  ? 0.1335 0.1122 0.1428 -0.0088 0.0204  0.0108  45  HIS   A CG  
1293 C CG  B HIS   A 45  ? 0.1452 0.1403 0.1083 0.0117  0.0069  0.0115  45  HIS   A CG  
1294 N ND1 A HIS   A 45  ? 0.1368 0.1121 0.1621 0.0032  0.0226  0.0012  45  HIS   A ND1 
1295 N ND1 B HIS   A 45  ? 0.1456 0.1421 0.1314 0.0153  -0.0059 0.0205  45  HIS   A ND1 
1296 C CD2 A HIS   A 45  ? 0.1293 0.1175 0.1650 -0.0141 0.0023  0.0076  45  HIS   A CD2 
1297 C CD2 B HIS   A 45  ? 0.1333 0.1190 0.1070 0.0118  0.0145  0.0051  45  HIS   A CD2 
1298 C CE1 A HIS   A 45  ? 0.1411 0.1228 0.1793 0.0011  0.0168  0.0068  45  HIS   A CE1 
1299 C CE1 B HIS   A 45  ? 0.1363 0.1113 0.1143 0.0022  0.0011  0.0189  45  HIS   A CE1 
1300 N NE2 A HIS   A 45  ? 0.1383 0.1255 0.1919 0.0008  0.0196  0.0089  45  HIS   A NE2 
1301 N NE2 B HIS   A 45  ? 0.1302 0.1143 0.1108 -0.0027 0.0191  0.0082  45  HIS   A NE2 
1316 N N   A GLY   A 46  ? 0.1378 0.1431 0.1688 0.0045  -0.0012 0.0270  46  GLY   A N   
1317 N N   B GLY   A 46  ? 0.1667 0.1673 0.1848 0.0105  -0.0069 0.0126  46  GLY   A N   
1318 C CA  A GLY   A 46  ? 0.1475 0.1586 0.1861 0.0125  -0.0077 0.0439  46  GLY   A CA  
1319 C CA  B GLY   A 46  ? 0.1516 0.1781 0.2018 0.0117  -0.0074 0.0151  46  GLY   A CA  
1320 C C   A GLY   A 46  ? 0.1478 0.1621 0.1773 0.0259  -0.0190 0.0499  46  GLY   A C   
1321 C C   B GLY   A 46  ? 0.1428 0.1754 0.1872 0.0090  0.0110  -0.0010 46  GLY   A C   
1322 O O   A GLY   A 46  ? 0.1505 0.1669 0.1920 0.0298  -0.0383 0.0401  46  GLY   A O   
1323 O O   B GLY   A 46  ? 0.1504 0.1823 0.2089 0.0098  0.0022  -0.0134 46  GLY   A O   
1330 N N   A GLY   A 47  ? 0.1507 0.1641 0.1783 0.0313  -0.0135 0.0245  47  GLY   A N   
1331 N N   B GLY   A 47  ? 0.1490 0.1707 0.1722 0.0071  0.0271  -0.0098 47  GLY   A N   
1332 C CA  A GLY   A 47  ? 0.1520 0.1658 0.1614 0.0237  -0.0190 0.0061  47  GLY   A CA  
1333 C CA  B GLY   A 47  ? 0.1449 0.1695 0.1689 0.0058  0.0259  -0.0065 47  GLY   A CA  
1334 C C   A GLY   A 47  ? 0.1432 0.1539 0.1706 0.0195  -0.0231 0.0182  47  GLY   A C   
1335 C C   B GLY   A 47  ? 0.1413 0.1544 0.1418 0.0056  0.0303  0.0014  47  GLY   A C   
1336 O O   A GLY   A 47  ? 0.1477 0.1549 0.2057 0.0185  -0.0332 0.0190  47  GLY   A O   
1337 O O   B GLY   A 47  ? 0.1404 0.1450 0.1312 0.0038  0.0332  0.0069  47  GLY   A O   
1344 N N   A GLY   A 48  ? 0.1360 0.1477 0.1434 0.0184  -0.0014 0.0226  48  GLY   A N   
1345 N N   B GLY   A 48  ? 0.1440 0.1557 0.1425 0.0089  0.0256  -0.0029 48  GLY   A N   
1346 C CA  A GLY   A 48  ? 0.1338 0.1396 0.1373 0.0136  0.0058  0.0082  48  GLY   A CA  
1347 C CA  B GLY   A 48  ? 0.1442 0.1432 0.1352 0.0063  0.0232  -0.0120 48  GLY   A CA  
1348 C C   A GLY   A 48  ? 0.1371 0.1413 0.1291 0.0030  0.0118  0.0060  48  GLY   A C   
1349 C C   B GLY   A 48  ? 0.1433 0.1488 0.1410 -0.0022 0.0196  0.0017  48  GLY   A C   
1350 O O   A GLY   A 48  ? 0.1430 0.1490 0.1348 0.0020  0.0027  0.0128  48  GLY   A O   
1351 O O   B GLY   A 48  ? 0.1442 0.1593 0.1344 0.0082  0.0098  -0.0039 48  GLY   A O   
1358 N N   A VAL   A 49  ? 0.1379 0.1379 0.1630 -0.0033 -0.0023 0.0115  49  VAL   A N   
1359 N N   B VAL   A 49  ? 0.1346 0.1417 0.1359 -0.0102 -0.0085 -0.0014 49  VAL   A N   
1360 C CA  A VAL   A 49  ? 0.1473 0.1427 0.1782 -0.0129 -0.0131 0.0271  49  VAL   A CA  
1361 C CA  B VAL   A 49  ? 0.1281 0.1427 0.1173 -0.0180 0.0012  -0.0005 49  VAL   A CA  
1362 C C   A VAL   A 49  ? 0.1394 0.1403 0.1710 -0.0171 -0.0030 0.0476  49  VAL   A C   
1363 C C   B VAL   A 49  ? 0.1313 0.1392 0.0977 -0.0167 0.0087  -0.0088 49  VAL   A C   
1364 O O   A VAL   A 49  ? 0.1401 0.1424 0.1648 -0.0150 -0.0272 0.0378  49  VAL   A O   
1365 O O   B VAL   A 49  ? 0.1356 0.1390 0.0914 0.0026  0.0200  -0.0052 49  VAL   A O   
1366 C CB  A VAL   A 49  ? 0.1477 0.1523 0.2133 -0.0078 -0.0192 0.0128  49  VAL   A CB  
1367 C CB  B VAL   A 49  ? 0.1326 0.1438 0.1520 -0.0147 -0.0082 0.0086  49  VAL   A CB  
1368 C CG1 A VAL   A 49  ? 0.1370 0.1450 0.2383 0.0031  -0.0078 0.0162  49  VAL   A CG1 
1369 C CG1 B VAL   A 49  ? 0.1351 0.1273 0.1493 0.0017  -0.0003 0.0181  49  VAL   A CG1 
1370 C CG2 A VAL   A 49  ? 0.1669 0.1680 0.2548 -0.0323 -0.0215 0.0200  49  VAL   A CG2 
1371 C CG2 B VAL   A 49  ? 0.1432 0.1459 0.1955 -0.0118 -0.0200 0.0319  49  VAL   A CG2 
1390 N N   A ALA   A 50  ? 0.1282 0.1313 0.1683 -0.0072 -0.0174 0.0439  50  ALA   A N   
1391 N N   B ALA   A 50  ? 0.1290 0.1324 0.1063 -0.0076 -0.0178 -0.0210 50  ALA   A N   
1392 C CA  A ALA   A 50  ? 0.1340 0.1282 0.1625 -0.0186 -0.0069 0.0476  50  ALA   A CA  
1393 C CA  B ALA   A 50  ? 0.1313 0.1249 0.0898 -0.0028 -0.0069 -0.0305 50  ALA   A CA  
1394 C C   A ALA   A 50  ? 0.1270 0.1196 0.1714 -0.0198 -0.0014 0.0315  50  ALA   A C   
1395 C C   B ALA   A 50  ? 0.1340 0.1278 0.0984 0.0013  0.0057  -0.0398 50  ALA   A C   
1396 O O   A ALA   A 50  ? 0.1243 0.1179 0.1855 -0.0109 0.0051  0.0322  50  ALA   A O   
1397 O O   B ALA   A 50  ? 0.1419 0.1321 0.0864 0.0099  -0.0027 -0.0386 50  ALA   A O   
1398 C CB  A ALA   A 50  ? 0.1356 0.1309 0.1715 -0.0133 -0.0043 0.0356  50  ALA   A CB  
1399 C CB  B ALA   A 50  ? 0.1377 0.1220 0.1049 0.0006  0.0191  -0.0343 50  ALA   A CB  
1410 N N   A GLY   A 51  ? 0.1303 0.1186 0.1723 -0.0074 -0.0315 0.0258  51  GLY   A N   
1411 N N   B GLY   A 51  ? 0.1313 0.1364 0.1422 0.0099  -0.0018 -0.0306 51  GLY   A N   
1412 C CA  A GLY   A 51  ? 0.1321 0.1257 0.1905 -0.0031 -0.0273 0.0334  51  GLY   A CA  
1413 C CA  B GLY   A 51  ? 0.1371 0.1311 0.1343 -0.0003 -0.0070 -0.0228 51  GLY   A CA  
1414 C C   A GLY   A 51  ? 0.1236 0.1352 0.1907 -0.0016 -0.0150 -0.0015 51  GLY   A C   
1415 C C   B GLY   A 51  ? 0.1364 0.1301 0.1250 0.0028  -0.0017 -0.0308 51  GLY   A C   
1416 O O   A GLY   A 51  ? 0.1392 0.1422 0.2083 -0.0037 -0.0263 -0.0002 51  GLY   A O   
1417 O O   B GLY   A 51  ? 0.1371 0.1242 0.1211 0.0045  0.0053  -0.0176 51  GLY   A O   
1424 N N   A ALA   A 52  ? 0.1198 0.1400 0.1888 -0.0091 -0.0104 -0.0022 52  ALA   A N   
1425 N N   B ALA   A 52  ? 0.1397 0.1226 0.1265 0.0018  0.0086  -0.0340 52  ALA   A N   
1426 C CA  A ALA   A 52  ? 0.1215 0.1520 0.1776 -0.0088 -0.0053 -0.0091 52  ALA   A CA  
1427 C CA  B ALA   A 52  ? 0.1395 0.1261 0.1338 0.0033  0.0099  -0.0143 52  ALA   A CA  
1428 C C   A ALA   A 52  ? 0.1232 0.1539 0.1758 -0.0152 0.0169  -0.0115 52  ALA   A C   
1429 C C   B ALA   A 52  ? 0.1455 0.1259 0.1342 0.0045  0.0156  -0.0057 52  ALA   A C   
1430 O O   A ALA   A 52  ? 0.1336 0.1637 0.1954 -0.0044 0.0146  -0.0158 52  ALA   A O   
1431 O O   B ALA   A 52  ? 0.1518 0.1406 0.1448 0.0088  0.0119  -0.0145 52  ALA   A O   
1432 C CB  A ALA   A 52  ? 0.1197 0.1684 0.1923 -0.0020 -0.0269 -0.0106 52  ALA   A CB  
1433 C CB  B ALA   A 52  ? 0.1500 0.1288 0.1443 0.0116  0.0083  -0.0154 52  ALA   A CB  
1444 N N   A LEU   A 53  ? 0.1204 0.1556 0.1618 -0.0151 0.0141  -0.0038 53  LEU   A N   
1445 N N   B LEU   A 53  ? 0.1453 0.1294 0.1263 0.0041  0.0012  0.0028  53  LEU   A N   
1446 C CA  A LEU   A 53  ? 0.1389 0.1560 0.1538 -0.0100 0.0163  0.0104  53  LEU   A CA  
1447 C CA  B LEU   A 53  ? 0.1495 0.1348 0.1080 -0.0048 -0.0014 -0.0111 53  LEU   A CA  
1448 C C   A LEU   A 53  ? 0.1388 0.1559 0.1334 -0.0017 0.0112  0.0106  53  LEU   A C   
1449 C C   B LEU   A 53  ? 0.1416 0.1419 0.0991 0.0073  0.0015  -0.0093 53  LEU   A C   
1450 O O   A LEU   A 53  ? 0.1386 0.1456 0.1569 -0.0054 0.0201  -0.0006 53  LEU   A O   
1451 O O   B LEU   A 53  ? 0.1457 0.1385 0.1361 0.0086  0.0013  -0.0001 53  LEU   A O   
1452 C CB  A LEU   A 53  ? 0.1366 0.1611 0.1740 -0.0124 0.0093  0.0173  53  LEU   A CB  
1453 C CB  B LEU   A 53  ? 0.1459 0.1439 0.1355 -0.0075 0.0025  -0.0107 53  LEU   A CB  
1454 C CG  A LEU   A 53  ? 0.1540 0.1642 0.1757 -0.0347 0.0082  0.0161  53  LEU   A CG  
1455 C CG  B LEU   A 53  ? 0.1515 0.1563 0.1307 -0.0129 0.0055  -0.0074 53  LEU   A CG  
1456 C CD1 A LEU   A 53  ? 0.1588 0.1762 0.1870 -0.0311 -0.0012 0.0346  53  LEU   A CD1 
1457 C CD1 B LEU   A 53  ? 0.1601 0.1649 0.1308 -0.0180 -0.0047 -0.0110 53  LEU   A CD1 
1458 C CD2 A LEU   A 53  ? 0.1604 0.1712 0.1678 -0.0485 -0.0126 0.0110  53  LEU   A CD2 
1459 C CD2 B LEU   A 53  ? 0.1503 0.1654 0.1505 -0.0261 0.0022  0.0064  53  LEU   A CD2 
1482 N N   A ASN   A 54  ? 0.1278 0.1544 0.1343 -0.0103 -0.0127 0.0100  54  ASN   A N   
1483 N N   B ASN   A 54  ? 0.1294 0.1482 0.1189 0.0004  -0.0038 -0.0127 54  ASN   A N   
1484 C CA  A ASN   A 54  ? 0.1254 0.1551 0.1576 -0.0106 -0.0059 0.0142  54  ASN   A CA  
1485 C CA  B ASN   A 54  ? 0.1231 0.1533 0.1410 -0.0037 0.0093  -0.0077 54  ASN   A CA  
1486 C C   A ASN   A 54  ? 0.1315 0.1588 0.1589 -0.0097 -0.0055 0.0060  54  ASN   A C   
1487 C C   B ASN   A 54  ? 0.1305 0.1532 0.1518 -0.0139 -0.0092 -0.0113 54  ASN   A C   
1488 O O   A ASN   A 54  ? 0.1277 0.1672 0.1835 0.0022  0.0119  0.0094  54  ASN   A O   
1489 O O   B ASN   A 54  ? 0.1324 0.1456 0.1837 -0.0168 -0.0112 -0.0163 54  ASN   A O   
1490 C CB  A ASN   A 54  ? 0.1317 0.1547 0.1651 -0.0229 -0.0229 0.0146  54  ASN   A CB  
1491 C CB  B ASN   A 54  ? 0.1215 0.1574 0.1428 0.0003  0.0164  -0.0043 54  ASN   A CB  
1492 C CG  A ASN   A 54  ? 0.1487 0.1583 0.1553 -0.0208 -0.0320 0.0128  54  ASN   A CG  
1493 C CG  B ASN   A 54  ? 0.1295 0.1532 0.1229 -0.0001 0.0050  -0.0090 54  ASN   A CG  
1494 O OD1 A ASN   A 54  ? 0.1474 0.1448 0.1905 -0.0060 -0.0287 0.0211  54  ASN   A OD1 
1495 O OD1 B ASN   A 54  ? 0.1286 0.1332 0.1110 -0.0055 0.0129  -0.0320 54  ASN   A OD1 
1496 N ND2 A ASN   A 54  ? 0.1526 0.1659 0.1634 -0.0254 -0.0342 0.0200  54  ASN   A ND2 
1497 N ND2 B ASN   A 54  ? 0.1224 0.1598 0.1556 -0.0020 0.0041  0.0162  54  ASN   A ND2 
1510 N N   . LYS   A 55  ? 0.1362 0.1569 0.1537 -0.0100 0.0003  -0.0067 55  LYS   A N   
1511 C CA  . LYS   A 55  ? 0.1533 0.1674 0.1596 0.0065  -0.0056 -0.0208 55  LYS   A CA  
1512 C C   . LYS   A 55  ? 0.1539 0.1739 0.1453 -0.0066 -0.0117 -0.0211 55  LYS   A C   
1513 O O   . LYS   A 55  ? 0.1683 0.1929 0.1552 -0.0013 -0.0048 -0.0291 55  LYS   A O   
1514 C CB  . LYS   A 55  ? 0.1630 0.1820 0.1806 0.0203  0.0033  -0.0190 55  LYS   A CB  
1515 C CG  . LYS   A 55  ? 0.1894 0.2262 0.2112 0.0442  -0.0215 -0.0397 55  LYS   A CG  
1516 C CD  . LYS   A 55  ? 0.2186 0.2600 0.2297 0.0654  -0.0284 -0.0440 55  LYS   A CD  
1517 C CE  . LYS   A 55  ? 0.2445 0.2999 0.2459 0.0843  -0.0406 -0.0474 55  LYS   A CE  
1518 N NZ  . LYS   A 55  ? 0.2590 0.3366 0.2688 0.0986  -0.0567 -0.0332 55  LYS   A NZ  
1533 N N   . ALA   A 56  ? 0.1571 0.1802 0.1651 -0.0096 0.0059  -0.0175 56  ALA   A N   
1534 C CA  . ALA   A 56  ? 0.1638 0.2010 0.1531 -0.0148 0.0038  -0.0149 56  ALA   A CA  
1535 C C   . ALA   A 56  ? 0.1758 0.2079 0.1010 -0.0172 0.0188  -0.0193 56  ALA   A C   
1536 O O   . ALA   A 56  ? 0.1745 0.2319 0.1314 -0.0021 0.0228  -0.0098 56  ALA   A O   
1537 C CB  . ALA   A 56  ? 0.1573 0.2169 0.1939 -0.0261 0.0125  0.0015  56  ALA   A CB  
1543 N N   . THR   A 57  ? 0.1601 0.1933 0.1328 -0.0157 0.0204  -0.0211 57  THR   A N   
1544 C CA  . THR   A 57  ? 0.1570 0.1792 0.1411 -0.0262 -0.0044 -0.0185 57  THR   A CA  
1545 C C   . THR   A 57  ? 0.1533 0.1874 0.1475 -0.0081 0.0045  -0.0202 57  THR   A C   
1546 O O   . THR   A 57  ? 0.1529 0.1923 0.1664 -0.0193 -0.0040 -0.0214 57  THR   A O   
1547 C CB  . THR   A 57  ? 0.1606 0.1826 0.1056 -0.0123 0.0019  -0.0200 57  THR   A CB  
1548 O OG1 . THR   A 57  ? 0.1408 0.1834 0.1374 -0.0107 0.0106  -0.0052 57  THR   A OG1 
1549 C CG2 . THR   A 57  ? 0.1635 0.1851 0.1307 -0.0096 0.0055  -0.0042 57  THR   A CG2 
1557 N N   . ASN   A 58  ? 0.1468 0.1872 0.1814 -0.0071 0.0124  -0.0156 58  ASN   A N   
1558 C CA  . ASN   A 58  ? 0.1710 0.1837 0.1895 -0.0099 0.0166  -0.0333 58  ASN   A CA  
1559 C C   . ASN   A 58  ? 0.1598 0.1671 0.1649 -0.0017 -0.0004 -0.0228 58  ASN   A C   
1560 O O   . ASN   A 58  ? 0.1634 0.1716 0.1947 -0.0215 -0.0029 -0.0321 58  ASN   A O   
1561 C CB  . ASN   A 58  ? 0.2179 0.1911 0.2237 -0.0118 0.0530  -0.0435 58  ASN   A CB  
1562 C CG  . ASN   A 58  ? 0.2708 0.2182 0.3201 -0.0142 0.0357  -0.0151 58  ASN   A CG  
1563 O OD1 . ASN   A 58  ? 0.2960 0.1963 0.3701 0.0242  0.0731  -0.0009 58  ASN   A OD1 
1564 N ND2 . ASN   A 58  ? 0.2791 0.2339 0.3373 -0.0115 0.0202  -0.0192 58  ASN   A ND2 
1571 N N   . ASN   A 59  ? 0.1513 0.1607 0.1448 -0.0089 0.0040  -0.0160 59  ASN   A N   
1572 C CA  . ASN   A 59  ? 0.1566 0.1435 0.1365 -0.0027 -0.0055 -0.0140 59  ASN   A CA  
1573 C C   . ASN   A 59  ? 0.1592 0.1510 0.1255 -0.0095 0.0023  0.0055  59  ASN   A C   
1574 O O   . ASN   A 59  ? 0.1554 0.1587 0.1463 -0.0062 0.0038  0.0060  59  ASN   A O   
1575 C CB  . ASN   A 59  ? 0.1641 0.1365 0.1477 0.0061  -0.0193 -0.0124 59  ASN   A CB  
1576 C CG  . ASN   A 59  ? 0.1609 0.1413 0.1677 0.0007  -0.0288 0.0053  59  ASN   A CG  
1577 O OD1 . ASN   A 59  ? 0.1631 0.1548 0.1670 -0.0127 -0.0200 0.0028  59  ASN   A OD1 
1578 N ND2 . ASN   A 59  ? 0.1717 0.1461 0.1848 -0.0137 -0.0162 0.0092  59  ASN   A ND2 
1585 N N   . ALA   A 60  ? 0.1422 0.1597 0.1412 -0.0029 0.0025  -0.0006 60  ALA   A N   
1586 C CA  . ALA   A 60  ? 0.1411 0.1607 0.1400 0.0013  -0.0177 -0.0012 60  ALA   A CA  
1587 C C   . ALA   A 60  ? 0.1487 0.1558 0.1483 -0.0039 -0.0043 0.0112  60  ALA   A C   
1588 O O   . ALA   A 60  ? 0.1433 0.1579 0.1841 -0.0040 -0.0028 0.0006  60  ALA   A O   
1589 C CB  . ALA   A 60  ? 0.1598 0.1666 0.1521 -0.0018 -0.0201 -0.0306 60  ALA   A CB  
1595 N N   . MET   A 61  ? 0.1361 0.1357 0.1593 -0.0043 0.0068  -0.0036 61  MET   A N   
1596 C CA  . MET   A 61  ? 0.1231 0.1266 0.1669 -0.0072 0.0047  0.0113  61  MET   A CA  
1597 C C   . MET   A 61  ? 0.1236 0.1367 0.1592 -0.0195 -0.0029 0.0035  61  MET   A C   
1598 O O   . MET   A 61  ? 0.1388 0.1415 0.1734 -0.0038 0.0109  0.0072  61  MET   A O   
1599 C CB  . MET   A 61  ? 0.1435 0.1440 0.1438 -0.0079 0.0140  -0.0017 61  MET   A CB  
1600 C CG  . MET   A 61  ? 0.1423 0.1607 0.1593 -0.0090 0.0047  0.0043  61  MET   A CG  
1601 S SD  . MET   A 61  ? 0.1464 0.1572 0.1824 -0.0153 0.0011  -0.0126 61  MET   A SD  
1602 C CE  . MET   A 61  ? 0.1710 0.1706 0.2170 -0.0075 0.0069  -0.0208 61  MET   A CE  
1612 N N   . GLN   A 62  ? 0.1260 0.1393 0.1610 -0.0084 0.0059  0.0128  62  GLN   A N   
1613 C CA  . GLN   A 62  ? 0.1263 0.1389 0.1513 -0.0145 0.0013  0.0039  62  GLN   A CA  
1614 C C   . GLN   A 62  ? 0.1457 0.1283 0.1543 -0.0014 0.0057  0.0056  62  GLN   A C   
1615 O O   . GLN   A 62  ? 0.1351 0.1460 0.1745 -0.0034 0.0034  0.0071  62  GLN   A O   
1616 C CB  . GLN   A 62  ? 0.1477 0.1310 0.1474 -0.0061 -0.0063 -0.0018 62  GLN   A CB  
1617 C CG  . GLN   A 62  ? 0.1446 0.1410 0.1667 -0.0071 0.0063  0.0142  62  GLN   A CG  
1618 C CD  . GLN   A 62  ? 0.1560 0.1307 0.1582 -0.0096 0.0074  -0.0019 62  GLN   A CD  
1619 O OE1 . GLN   A 62  ? 0.1558 0.1474 0.1712 -0.0038 -0.0034 -0.0011 62  GLN   A OE1 
1620 N NE2 . GLN   A 62  ? 0.1587 0.1376 0.1652 0.0012  0.0114  -0.0175 62  GLN   A NE2 
1629 N N   . VAL   A 63  ? 0.1440 0.1364 0.1836 -0.0190 0.0085  -0.0147 63  VAL   A N   
1630 C CA  . VAL   A 63  ? 0.1458 0.1550 0.1860 -0.0201 -0.0012 -0.0099 63  VAL   A CA  
1631 C C   . VAL   A 63  ? 0.1338 0.1475 0.1785 -0.0259 0.0072  -0.0091 63  VAL   A C   
1632 O O   . VAL   A 63  ? 0.1394 0.1472 0.1973 -0.0272 0.0080  -0.0125 63  VAL   A O   
1633 C CB  . VAL   A 63  ? 0.1592 0.1667 0.2246 -0.0246 -0.0048 -0.0338 63  VAL   A CB  
1634 C CG1 . VAL   A 63  ? 0.1537 0.1883 0.2829 -0.0271 -0.0122 -0.0612 63  VAL   A CG1 
1635 C CG2 . VAL   A 63  ? 0.1692 0.1553 0.2062 -0.0131 0.0117  -0.0302 63  VAL   A CG2 
1645 N N   . GLU   A 64  ? 0.1296 0.1519 0.1759 -0.0132 0.0020  -0.0056 64  GLU   A N   
1646 C CA  . GLU   A 64  ? 0.1262 0.1575 0.1666 -0.0103 -0.0055 0.0070  64  GLU   A CA  
1647 C C   . GLU   A 64  ? 0.1318 0.1395 0.1593 -0.0078 -0.0106 0.0176  64  GLU   A C   
1648 O O   . GLU   A 64  ? 0.1447 0.1524 0.1784 0.0057  0.0014  0.0075  64  GLU   A O   
1649 C CB  . GLU   A 64  ? 0.1303 0.1695 0.1802 -0.0055 -0.0022 0.0020  64  GLU   A CB  
1650 C CG  . GLU   A 64  ? 0.1418 0.1782 0.2132 -0.0049 0.0044  -0.0010 64  GLU   A CG  
1651 C CD  . GLU   A 64  ? 0.1580 0.1850 0.2214 -0.0172 0.0088  0.0104  64  GLU   A CD  
1652 O OE1 . GLU   A 64  ? 0.1567 0.1853 0.2362 -0.0228 0.0169  0.0084  64  GLU   A OE1 
1653 O OE2 . GLU   A 64  ? 0.1756 0.1772 0.2145 -0.0275 -0.0018 0.0097  64  GLU   A OE2 
1660 N N   . SER   A 65  ? 0.1345 0.1453 0.1549 -0.0003 0.0031  0.0071  65  SER   A N   
1661 C CA  . SER   A 65  ? 0.1385 0.1442 0.1553 -0.0057 0.0109  -0.0078 65  SER   A CA  
1662 C C   . SER   A 65  ? 0.1446 0.1435 0.1618 -0.0038 0.0043  -0.0039 65  SER   A C   
1663 O O   . SER   A 65  ? 0.1465 0.1488 0.1900 -0.0024 0.0192  -0.0104 65  SER   A O   
1664 C CB  . SER   A 65  ? 0.1342 0.1477 0.1669 -0.0049 0.0120  0.0035  65  SER   A CB  
1665 O OG  . SER   A 65  ? 0.1417 0.1561 0.1711 -0.0130 0.0047  0.0216  65  SER   A OG  
1671 N N   . ASP   A 66  ? 0.1427 0.1418 0.1607 -0.0013 0.0247  0.0116  66  ASP   A N   
1672 C CA  . ASP   A 66  ? 0.1443 0.1577 0.1913 0.0036  0.0186  0.0127  66  ASP   A CA  
1673 C C   . ASP   A 66  ? 0.1317 0.1603 0.1944 -0.0013 0.0130  0.0209  66  ASP   A C   
1674 O O   . ASP   A 66  ? 0.1495 0.1639 0.1998 -0.0050 0.0281  0.0215  66  ASP   A O   
1675 C CB  . ASP   A 66  ? 0.1612 0.1690 0.2341 0.0100  0.0243  0.0344  66  ASP   A CB  
1676 C CG  . ASP   A 66  ? 0.1883 0.1902 0.2680 -0.0127 0.0147  0.0663  66  ASP   A CG  
1677 O OD1 . ASP   A 66  ? 0.1907 0.2206 0.2449 -0.0167 0.0058  0.0741  66  ASP   A OD1 
1678 O OD2 . ASP   A 66  ? 0.1957 0.2209 0.3541 0.0123  -0.0104 0.0247  66  ASP   A OD2 
1683 N N   A ASP   A 67  ? 0.1306 0.1578 0.2084 -0.0032 0.0082  0.0240  67  ASP   A N   
1684 N N   B ASP   A 67  ? 0.1326 0.1591 0.2146 -0.0048 0.0001  0.0109  67  ASP   A N   
1685 C CA  A ASP   A 67  ? 0.1277 0.1716 0.2191 -0.0067 0.0083  0.0382  67  ASP   A CA  
1686 C CA  B ASP   A 67  ? 0.1351 0.1730 0.2284 -0.0064 -0.0079 0.0124  67  ASP   A CA  
1687 C C   A ASP   A 67  ? 0.1198 0.1702 0.2068 -0.0028 0.0250  0.0280  67  ASP   A C   
1688 C C   B ASP   A 67  ? 0.1341 0.1717 0.2238 -0.0059 0.0164  0.0095  67  ASP   A C   
1689 O O   A ASP   A 67  ? 0.1169 0.1683 0.2235 0.0021  0.0163  0.0339  67  ASP   A O   
1690 O O   B ASP   A 67  ? 0.1487 0.1727 0.2414 -0.0060 0.0139  0.0109  67  ASP   A O   
1691 C CB  A ASP   A 67  ? 0.1427 0.1720 0.2322 -0.0065 0.0048  0.0551  67  ASP   A CB  
1692 C CB  B ASP   A 67  ? 0.1460 0.1737 0.2353 -0.0031 -0.0237 0.0099  67  ASP   A CB  
1693 C CG  A ASP   A 67  ? 0.1442 0.1777 0.2413 -0.0146 -0.0013 0.0598  67  ASP   A CG  
1694 C CG  B ASP   A 67  ? 0.1498 0.1851 0.2341 -0.0054 -0.0365 -0.0006 67  ASP   A CG  
1695 O OD1 A ASP   A 67  ? 0.1398 0.1792 0.2813 -0.0127 -0.0064 0.0462  67  ASP   A OD1 
1696 O OD1 B ASP   A 67  ? 0.1454 0.1900 0.2548 0.0050  -0.0493 -0.0008 67  ASP   A OD1 
1697 O OD2 A ASP   A 67  ? 0.1476 0.1823 0.2237 0.0024  0.0125  0.0492  67  ASP   A OD2 
1698 O OD2 B ASP   A 67  ? 0.1535 0.1876 0.2111 0.0012  -0.0211 -0.0202 67  ASP   A OD2 
1707 N N   . TYR   A 68  ? 0.1320 0.1661 0.2079 0.0059  0.0159  0.0208  68  TYR   A N   
1708 C CA  . TYR   A 68  ? 0.1482 0.1580 0.2012 -0.0024 0.0296  0.0185  68  TYR   A CA  
1709 C C   . TYR   A 68  ? 0.1428 0.1453 0.2105 0.0022  0.0373  0.0118  68  TYR   A C   
1710 O O   . TYR   A 68  ? 0.1575 0.1535 0.2356 0.0122  0.0363  0.0207  68  TYR   A O   
1711 C CB  . TYR   A 68  ? 0.1526 0.1382 0.2123 0.0068  0.0365  0.0284  68  TYR   A CB  
1712 C CG  . TYR   A 68  ? 0.1553 0.1586 0.2516 0.0098  0.0527  0.0295  68  TYR   A CG  
1713 C CD1 . TYR   A 68  ? 0.1637 0.1582 0.2710 -0.0200 0.0425  -0.0058 68  TYR   A CD1 
1714 C CD2 . TYR   A 68  ? 0.1734 0.1667 0.3097 0.0040  0.0719  0.0249  68  TYR   A CD2 
1715 C CE1 . TYR   A 68  ? 0.1711 0.1750 0.3127 -0.0298 0.0504  -0.0056 68  TYR   A CE1 
1716 C CE2 . TYR   A 68  ? 0.1805 0.1625 0.3312 -0.0064 0.0648  0.0057  68  TYR   A CE2 
1717 C CZ  . TYR   A 68  ? 0.1742 0.1588 0.3353 -0.0254 0.0569  -0.0257 68  TYR   A CZ  
1718 O OH  . TYR   A 68  ? 0.2077 0.1772 0.3757 -0.0219 0.0414  -0.0514 68  TYR   A OH  
1729 N N   . ILE   A 69  ? 0.1433 0.1399 0.1977 0.0000  0.0262  0.0155  69  ILE   A N   
1730 C CA  . ILE   A 69  ? 0.1524 0.1372 0.1890 -0.0012 0.0298  0.0122  69  ILE   A CA  
1731 C C   . ILE   A 69  ? 0.1583 0.1378 0.1953 0.0088  0.0442  0.0065  69  ILE   A C   
1732 O O   . ILE   A 69  ? 0.1615 0.1541 0.2150 0.0008  0.0381  0.0041  69  ILE   A O   
1733 C CB  . ILE   A 69  ? 0.1617 0.1633 0.1856 0.0047  0.0275  -0.0029 69  ILE   A CB  
1734 C CG1 . ILE   A 69  ? 0.1669 0.1669 0.1945 0.0072  0.0354  -0.0095 69  ILE   A CG1 
1735 C CG2 . ILE   A 69  ? 0.1772 0.1876 0.2052 0.0098  0.0296  -0.0158 69  ILE   A CG2 
1736 C CD1 . ILE   A 69  ? 0.1620 0.1872 0.2145 0.0027  0.0359  -0.0151 69  ILE   A CD1 
1748 N N   . ALA   A 70  ? 0.1622 0.1416 0.2379 -0.0075 0.0502  0.0097  70  ALA   A N   
1749 C CA  . ALA   A 70  ? 0.1669 0.1602 0.2675 -0.0223 0.0592  0.0148  70  ALA   A CA  
1750 C C   . ALA   A 70  ? 0.1676 0.1836 0.2856 -0.0197 0.0566  0.0039  70  ALA   A C   
1751 O O   . ALA   A 70  ? 0.1863 0.2178 0.3127 0.0088  0.0752  0.0228  70  ALA   A O   
1752 C CB  . ALA   A 70  ? 0.1711 0.1650 0.2865 -0.0232 0.0568  0.0100  70  ALA   A CB  
1758 N N   . THR   A 71  ? 0.1576 0.1709 0.2635 -0.0032 0.0261  0.0053  71  THR   A N   
1759 C CA  . THR   A 71  ? 0.1886 0.1897 0.3226 0.0067  0.0285  0.0192  71  THR   A CA  
1760 C C   . THR   A 71  ? 0.1669 0.1773 0.3408 0.0153  0.0525  0.0159  71  THR   A C   
1761 O O   . THR   A 71  ? 0.1699 0.1989 0.3999 0.0051  0.0545  -0.0281 71  THR   A O   
1762 C CB  . THR   A 71  ? 0.2248 0.2159 0.3625 0.0140  -0.0224 0.0256  71  THR   A CB  
1763 O OG1 . THR   A 71  ? 0.2494 0.2457 0.3863 0.0077  -0.0377 0.0081  71  THR   A OG1 
1764 C CG2 . THR   A 71  ? 0.2354 0.2407 0.3967 0.0118  -0.0489 0.0564  71  THR   A CG2 
1772 N N   . ASN   A 72  ? 0.1613 0.1671 0.2935 0.0028  0.0474  0.0151  72  ASN   A N   
1773 C CA  . ASN   A 72  ? 0.1698 0.1659 0.2815 0.0170  0.0588  0.0154  72  ASN   A CA  
1774 C C   . ASN   A 72  ? 0.1733 0.1763 0.2678 0.0063  0.0639  0.0155  72  ASN   A C   
1775 O O   . ASN   A 72  ? 0.1885 0.1784 0.2851 0.0052  0.0563  0.0108  72  ASN   A O   
1776 C CB  . ASN   A 72  ? 0.1917 0.1795 0.2811 0.0224  0.0582  0.0153  72  ASN   A CB  
1777 C CG  . ASN   A 72  ? 0.2126 0.1929 0.2673 0.0196  0.0562  0.0282  72  ASN   A CG  
1778 O OD1 . ASN   A 72  ? 0.2383 0.2381 0.2899 0.0219  0.0492  0.0225  72  ASN   A OD1 
1779 N ND2 . ASN   A 72  ? 0.2319 0.1879 0.2831 0.0500  0.0366  0.0319  72  ASN   A ND2 
1786 N N   . GLY   A 73  ? 0.1756 0.1621 0.2469 0.0039  0.0596  -0.0031 73  GLY   A N   
1787 C CA  . GLY   A 73  ? 0.1808 0.1654 0.2399 -0.0120 0.0646  0.0114  73  GLY   A CA  
1788 C C   . GLY   A 73  ? 0.1747 0.1475 0.2198 -0.0028 0.0691  0.0228  73  GLY   A C   
1789 O O   . GLY   A 73  ? 0.1747 0.1568 0.2345 0.0107  0.0541  0.0282  73  GLY   A O   
1793 N N   . PRO   A 74  ? 0.1850 0.1560 0.2287 -0.0082 0.0644  0.0045  74  PRO   A N   
1794 C CA  . PRO   A 74  ? 0.1805 0.1496 0.2393 0.0014  0.0512  0.0180  74  PRO   A CA  
1795 C C   . PRO   A 74  ? 0.1812 0.1292 0.2318 -0.0044 0.0483  0.0070  74  PRO   A C   
1796 O O   . PRO   A 74  ? 0.1815 0.1452 0.2558 -0.0022 0.0475  -0.0061 74  PRO   A O   
1797 C CB  . PRO   A 74  ? 0.1951 0.1889 0.2543 -0.0007 0.0594  0.0282  74  PRO   A CB  
1798 C CG  . PRO   A 74  ? 0.2301 0.2369 0.3141 -0.0222 0.0425  0.0135  74  PRO   A CG  
1799 C CD  . PRO   A 74  ? 0.1992 0.1969 0.2543 -0.0209 0.0569  -0.0058 74  PRO   A CD  
1807 N N   . LEU   A 75  ? 0.1800 0.1311 0.1894 0.0057  0.0379  0.0009  75  LEU   A N   
1808 C CA  . LEU   A 75  ? 0.1882 0.1385 0.1439 0.0118  0.0194  0.0132  75  LEU   A CA  
1809 C C   . LEU   A 75  ? 0.1980 0.1455 0.1371 0.0122  0.0295  0.0318  75  LEU   A C   
1810 O O   . LEU   A 75  ? 0.2202 0.1563 0.1684 0.0081  0.0145  0.0142  75  LEU   A O   
1811 C CB  . LEU   A 75  ? 0.1896 0.1358 0.1604 0.0057  0.0256  0.0167  75  LEU   A CB  
1812 C CG  . LEU   A 75  ? 0.2097 0.1675 0.1624 -0.0274 0.0230  0.0032  75  LEU   A CG  
1813 C CD1 . LEU   A 75  ? 0.2092 0.2167 0.1767 -0.0429 0.0249  -0.0090 75  LEU   A CD1 
1814 C CD2 . LEU   A 75  ? 0.2465 0.2142 0.2325 -0.0081 0.0275  0.0217  75  LEU   A CD2 
1826 N N   . LYS   A 76  ? 0.1942 0.1448 0.1694 -0.0008 0.0080  0.0081  76  LYS   A N   
1827 C CA  . LYS   A 76  ? 0.1833 0.1634 0.1747 -0.0078 0.0079  0.0029  76  LYS   A CA  
1828 C C   . LYS   A 76  ? 0.1821 0.1531 0.1355 0.0015  0.0131  0.0079  76  LYS   A C   
1829 O O   . LYS   A 76  ? 0.1827 0.1397 0.1626 -0.0041 0.0185  0.0093  76  LYS   A O   
1830 C CB  . LYS   A 76  ? 0.1778 0.1937 0.2167 0.0019  0.0139  -0.0254 76  LYS   A CB  
1831 C CG  . LYS   A 76  ? 0.1931 0.1867 0.2530 0.0018  0.0012  -0.0414 76  LYS   A CG  
1832 C CD  . LYS   A 76  ? 0.2097 0.1858 0.3055 0.0169  -0.0019 -0.0272 76  LYS   A CD  
1833 C CE  . LYS   A 76  ? 0.2186 0.2132 0.3625 0.0120  0.0039  -0.0290 76  LYS   A CE  
1834 N NZ  . LYS   A 76  ? 0.2082 0.2114 0.4029 0.0005  0.0001  -0.0428 76  LYS   A NZ  
1848 N N   . VAL   A 77  ? 0.2011 0.1587 0.1425 -0.0038 0.0236  0.0122  77  VAL   A N   
1849 C CA  . VAL   A 77  ? 0.1941 0.1620 0.1434 -0.0022 0.0081  0.0130  77  VAL   A CA  
1850 C C   . VAL   A 77  ? 0.1895 0.1509 0.1552 0.0090  0.0151  0.0060  77  VAL   A C   
1851 O O   . VAL   A 77  ? 0.1927 0.1625 0.1655 0.0055  0.0364  0.0040  77  VAL   A O   
1852 C CB  . VAL   A 77  ? 0.2046 0.1710 0.1700 -0.0055 -0.0029 0.0269  77  VAL   A CB  
1853 C CG1 . VAL   A 77  ? 0.2131 0.1842 0.2206 -0.0014 -0.0022 0.0095  77  VAL   A CG1 
1854 C CG2 . VAL   A 77  ? 0.2244 0.1880 0.2186 -0.0044 -0.0285 0.0324  77  VAL   A CG2 
1864 N N   . GLY   A 78  ? 0.1810 0.1472 0.1437 0.0084  0.0150  0.0151  78  GLY   A N   
1865 C CA  . GLY   A 78  ? 0.1872 0.1598 0.1429 0.0087  0.0284  0.0152  78  GLY   A CA  
1866 C C   . GLY   A 78  ? 0.1683 0.1598 0.1390 0.0062  0.0198  0.0322  78  GLY   A C   
1867 O O   . GLY   A 78  ? 0.1638 0.1587 0.1819 -0.0024 0.0137  0.0333  78  GLY   A O   
1871 N N   . GLY   A 79  ? 0.1617 0.1495 0.1600 -0.0112 0.0114  0.0135  79  GLY   A N   
1872 C CA  . GLY   A 79  ? 0.1497 0.1558 0.1783 -0.0071 0.0128  0.0089  79  GLY   A CA  
1873 C C   . GLY   A 79  ? 0.1419 0.1395 0.1477 -0.0046 0.0150  0.0152  79  GLY   A C   
1874 O O   . GLY   A 79  ? 0.1515 0.1559 0.1732 0.0158  0.0123  0.0104  79  GLY   A O   
1878 N N   . SER   A 80  ? 0.1411 0.1591 0.1699 0.0012  0.0079  -0.0013 80  SER   A N   
1879 C CA  . SER   A 80  ? 0.1348 0.1498 0.1639 -0.0034 0.0026  0.0056  80  SER   A CA  
1880 C C   . SER   A 80  ? 0.1394 0.1548 0.1708 -0.0076 0.0274  0.0181  80  SER   A C   
1881 O O   . SER   A 80  ? 0.1403 0.1773 0.2129 0.0001  0.0218  -0.0079 80  SER   A O   
1882 C CB  . SER   A 80  ? 0.1597 0.1487 0.1940 -0.0073 0.0124  0.0266  80  SER   A CB  
1883 O OG  . SER   A 80  ? 0.1814 0.1516 0.2395 -0.0021 0.0020  0.0414  80  SER   A OG  
1889 N N   . CYS   A 81  ? 0.1348 0.1380 0.1796 -0.0035 0.0051  0.0224  81  CYS   A N   
1890 C CA  . CYS   A 81  ? 0.1296 0.1590 0.1807 -0.0040 0.0057  0.0291  81  CYS   A CA  
1891 C C   . CYS   A 81  ? 0.1319 0.1563 0.1619 -0.0115 0.0060  0.0466  81  CYS   A C   
1892 O O   . CYS   A 81  ? 0.1288 0.1757 0.1809 -0.0016 0.0080  0.0329  81  CYS   A O   
1893 C CB  . CYS   A 81  ? 0.1518 0.1650 0.1823 -0.0187 0.0030  0.0344  81  CYS   A CB  
1894 S SG  . CYS   A 81  ? 0.1599 0.1466 0.1885 -0.0137 0.0042  0.0201  81  CYS   A SG  
1900 N N   . VAL   A 82  ? 0.1391 0.1564 0.1609 -0.0053 -0.0069 0.0271  82  VAL   A N   
1901 C CA  . VAL   A 82  ? 0.1504 0.1746 0.1618 -0.0045 -0.0048 0.0333  82  VAL   A CA  
1902 C C   . VAL   A 82  ? 0.1435 0.1723 0.1760 -0.0090 -0.0029 0.0156  82  VAL   A C   
1903 O O   . VAL   A 82  ? 0.1439 0.1675 0.1954 -0.0036 -0.0016 0.0010  82  VAL   A O   
1904 C CB  . VAL   A 82  ? 0.1803 0.1835 0.1832 -0.0011 0.0069  0.0262  82  VAL   A CB  
1905 C CG1 . VAL   A 82  ? 0.2018 0.1907 0.2069 0.0034  -0.0081 0.0137  82  VAL   A CG1 
1906 C CG2 . VAL   A 82  ? 0.1833 0.1953 0.2114 -0.0044 0.0150  0.0271  82  VAL   A CG2 
1916 N N   . LEU   A 83  ? 0.1470 0.1691 0.1643 -0.0123 -0.0063 0.0120  83  LEU   A N   
1917 C CA  . LEU   A 83  ? 0.1466 0.1732 0.1527 -0.0210 -0.0101 0.0158  83  LEU   A CA  
1918 C C   . LEU   A 83  ? 0.1560 0.1793 0.1649 -0.0137 -0.0074 0.0151  83  LEU   A C   
1919 O O   . LEU   A 83  ? 0.1591 0.1819 0.1758 -0.0177 -0.0039 0.0239  83  LEU   A O   
1920 C CB  . LEU   A 83  ? 0.1500 0.1768 0.1598 -0.0177 -0.0146 0.0338  83  LEU   A CB  
1921 C CG  . LEU   A 83  ? 0.1659 0.1784 0.1643 -0.0213 0.0004  0.0247  83  LEU   A CG  
1922 C CD1 . LEU   A 83  ? 0.1641 0.1868 0.1837 -0.0284 -0.0042 0.0279  83  LEU   A CD1 
1923 C CD2 . LEU   A 83  ? 0.1755 0.1967 0.1925 -0.0185 0.0105  0.0261  83  LEU   A CD2 
1935 N N   . SER   A 84  ? 0.1693 0.1810 0.1730 -0.0096 -0.0179 0.0181  84  SER   A N   
1936 C CA  . SER   A 84  ? 0.1876 0.1823 0.1492 -0.0086 -0.0175 0.0143  84  SER   A CA  
1937 C C   . SER   A 84  ? 0.1872 0.1784 0.1271 -0.0213 0.0052  0.0132  84  SER   A C   
1938 O O   . SER   A 84  ? 0.1649 0.1938 0.1392 -0.0120 -0.0069 0.0171  84  SER   A O   
1939 C CB  . SER   A 84  ? 0.2008 0.2054 0.1614 -0.0173 -0.0091 -0.0010 84  SER   A CB  
1940 O OG  . SER   A 84  ? 0.1974 0.2299 0.1880 -0.0166 -0.0292 -0.0125 84  SER   A OG  
1946 N N   A GLY   A 85  ? 0.1977 0.1905 0.1498 -0.0205 0.0230  0.0179  85  GLY   A N   
1947 N N   B GLY   A 85  ? 0.1993 0.1892 0.1574 -0.0106 0.0069  0.0162  85  GLY   A N   
1948 C CA  A GLY   A 85  ? 0.1933 0.2020 0.1557 -0.0276 0.0304  0.0060  85  GLY   A CA  
1949 C CA  B GLY   A 85  ? 0.1993 0.2032 0.1635 -0.0025 0.0036  -0.0012 85  GLY   A CA  
1950 C C   A GLY   A 85  ? 0.1904 0.2069 0.1384 -0.0298 0.0052  0.0115  85  GLY   A C   
1951 C C   B GLY   A 85  ? 0.2014 0.2093 0.1451 0.0079  -0.0322 0.0064  85  GLY   A C   
1952 O O   A GLY   A 85  ? 0.1913 0.2104 0.1447 -0.0394 0.0105  -0.0117 85  GLY   A O   
1953 O O   B GLY   A 85  ? 0.2050 0.2224 0.1607 0.0087  -0.0235 -0.0034 85  GLY   A O   
1960 N N   A HIS   A 86  ? 0.1925 0.2092 0.1290 -0.0265 0.0033  0.0131  86  HIS   A N   
1961 N N   B HIS   A 86  ? 0.2049 0.2111 0.1523 0.0134  -0.0335 0.0043  86  HIS   A N   
1962 C CA  A HIS   A 86  ? 0.2082 0.2157 0.1251 -0.0321 0.0042  0.0101  86  HIS   A CA  
1963 C CA  B HIS   A 86  ? 0.2185 0.2118 0.1591 0.0106  -0.0296 0.0027  86  HIS   A CA  
1964 C C   A HIS   A 86  ? 0.2258 0.2218 0.0965 -0.0332 0.0112  0.0044  86  HIS   A C   
1965 C C   B HIS   A 86  ? 0.2415 0.2275 0.1636 0.0078  -0.0239 0.0098  86  HIS   A C   
1966 O O   A HIS   A 86  ? 0.2271 0.2398 0.1124 -0.0327 0.0086  0.0016  86  HIS   A O   
1967 O O   B HIS   A 86  ? 0.2523 0.2426 0.1899 0.0116  -0.0177 0.0068  86  HIS   A O   
1968 C CB  A HIS   A 86  ? 0.2092 0.2126 0.1490 -0.0276 0.0051  0.0207  86  HIS   A CB  
1969 C CB  B HIS   A 86  ? 0.2061 0.1981 0.1547 0.0119  -0.0147 0.0088  86  HIS   A CB  
1970 C CG  A HIS   A 86  ? 0.2058 0.2098 0.1831 -0.0214 -0.0028 0.0346  86  HIS   A CG  
1971 C CG  B HIS   A 86  ? 0.1968 0.1893 0.1582 0.0095  -0.0006 0.0078  86  HIS   A CG  
1972 N ND1 A HIS   A 86  ? 0.2105 0.2102 0.2111 -0.0280 -0.0114 0.0388  86  HIS   A ND1 
1973 N ND1 B HIS   A 86  ? 0.2023 0.1875 0.1767 -0.0022 0.0019  0.0009  86  HIS   A ND1 
1974 C CD2 A HIS   A 86  ? 0.2028 0.2077 0.1891 -0.0119 0.0018  0.0392  86  HIS   A CD2 
1975 C CD2 B HIS   A 86  ? 0.1918 0.1836 0.1505 0.0144  0.0083  0.0004  86  HIS   A CD2 
1976 C CE1 A HIS   A 86  ? 0.2025 0.2049 0.2087 -0.0219 0.0027  0.0355  86  HIS   A CE1 
1977 C CE1 B HIS   A 86  ? 0.1930 0.1858 0.1783 0.0038  0.0177  -0.0044 86  HIS   A CE1 
1978 N NE2 A HIS   A 86  ? 0.2017 0.2013 0.1996 -0.0116 0.0091  0.0473  86  HIS   A NE2 
1979 N NE2 B HIS   A 86  ? 0.1906 0.1799 0.1682 0.0164  0.0183  0.0007  86  HIS   A NE2 
1994 N N   A ASN   A 87  ? 0.2463 0.2294 0.1341 -0.0208 0.0341  -0.0162 87  ASN   A N   
1995 N N   B ASN   A 87  ? 0.2536 0.2382 0.1877 0.0142  -0.0048 0.0041  87  ASN   A N   
1996 C CA  A ASN   A 87  ? 0.2709 0.2349 0.1444 -0.0133 0.0547  -0.0181 87  ASN   A CA  
1997 C CA  B ASN   A 87  ? 0.2683 0.2478 0.1856 0.0170  0.0195  0.0038  87  ASN   A CA  
1998 C C   A ASN   A 87  ? 0.2677 0.2418 0.1899 -0.0166 0.0672  -0.0093 87  ASN   A C   
1999 C C   B ASN   A 87  ? 0.2624 0.2615 0.2100 0.0052  0.0421  -0.0026 87  ASN   A C   
2000 O O   A ASN   A 87  ? 0.2954 0.2642 0.2316 -0.0252 0.0997  -0.0173 87  ASN   A O   
2001 O O   B ASN   A 87  ? 0.2915 0.2835 0.2405 -0.0059 0.0721  -0.0188 87  ASN   A O   
2002 C CB  A ASN   A 87  ? 0.2931 0.2429 0.1689 -0.0066 0.0565  -0.0152 87  ASN   A CB  
2003 C CB  B ASN   A 87  ? 0.2822 0.2494 0.1900 0.0276  0.0236  0.0104  87  ASN   A CB  
2004 C CG  A ASN   A 87  ? 0.3071 0.2544 0.1651 -0.0001 0.0714  -0.0144 87  ASN   A CG  
2005 C CG  B ASN   A 87  ? 0.2940 0.2613 0.1869 0.0314  0.0307  0.0161  87  ASN   A CG  
2006 O OD1 A ASN   A 87  ? 0.3227 0.2595 0.1723 0.0086  0.0694  -0.0056 87  ASN   A OD1 
2007 O OD1 B ASN   A 87  ? 0.3045 0.2629 0.1959 0.0359  0.0270  0.0269  87  ASN   A OD1 
2008 N ND2 A ASN   A 87  ? 0.3179 0.2761 0.1876 0.0022  0.0626  -0.0114 87  ASN   A ND2 
2009 N ND2 B ASN   A 87  ? 0.3041 0.2823 0.2048 0.0315  0.0227  0.0218  87  ASN   A ND2 
2022 N N   A LEU   A 88  ? 0.2436 0.2245 0.1890 -0.0141 0.0414  0.0052  88  LEU   A N   
2023 N N   B LEU   A 88  ? 0.2320 0.2453 0.1940 0.0023  0.0269  0.0024  88  LEU   A N   
2024 C CA  A LEU   A 88  ? 0.2224 0.2162 0.1838 -0.0173 0.0475  0.0305  88  LEU   A CA  
2025 C CA  B LEU   A 88  ? 0.2106 0.2486 0.1964 -0.0023 0.0358  0.0193  88  LEU   A CA  
2026 C C   A LEU   A 88  ? 0.2176 0.2199 0.1891 -0.0253 0.0503  0.0400  88  LEU   A C   
2027 C C   B LEU   A 88  ? 0.1993 0.2542 0.1863 0.0030  0.0277  0.0406  88  LEU   A C   
2028 O O   A LEU   A 88  ? 0.2158 0.2266 0.2386 -0.0198 0.0709  0.0426  88  LEU   A O   
2029 O O   B LEU   A 88  ? 0.2028 0.2524 0.2016 0.0090  0.0276  0.0670  88  LEU   A O   
2030 C CB  A LEU   A 88  ? 0.2158 0.2245 0.2006 -0.0144 0.0106  0.0506  88  LEU   A CB  
2031 C CB  B LEU   A 88  ? 0.2021 0.2515 0.2047 -0.0102 0.0282  0.0090  88  LEU   A CB  
2032 C CG  A LEU   A 88  ? 0.2235 0.2351 0.2281 -0.0174 -0.0027 0.0549  88  LEU   A CG  
2033 C CG  B LEU   A 88  ? 0.2045 0.2485 0.2131 -0.0126 0.0361  -0.0033 88  LEU   A CG  
2034 C CD1 A LEU   A 88  ? 0.2273 0.2448 0.2307 -0.0184 -0.0044 0.0461  88  LEU   A CD1 
2035 C CD1 B LEU   A 88  ? 0.2074 0.2450 0.2130 -0.0134 0.0415  -0.0145 88  LEU   A CD1 
2036 C CD2 A LEU   A 88  ? 0.2362 0.2396 0.2694 -0.0115 -0.0004 0.0532  88  LEU   A CD2 
2037 C CD2 B LEU   A 88  ? 0.2111 0.2529 0.2356 -0.0073 0.0417  -0.0076 88  LEU   A CD2 
2060 N N   A ALA   A 89  ? 0.2160 0.2114 0.1618 -0.0278 0.0286  0.0137  89  ALA   A N   
2061 N N   B ALA   A 89  ? 0.1901 0.2559 0.1781 0.0063  0.0090  0.0237  89  ALA   A N   
2062 C CA  A ALA   A 89  ? 0.2138 0.2124 0.1445 -0.0211 0.0151  0.0207  89  ALA   A CA  
2063 C CA  B ALA   A 89  ? 0.1853 0.2585 0.1732 0.0089  -0.0103 0.0357  89  ALA   A CA  
2064 C C   A ALA   A 89  ? 0.2139 0.2089 0.1567 -0.0219 0.0037  0.0155  89  ALA   A C   
2065 C C   B ALA   A 89  ? 0.1890 0.2529 0.1763 0.0061  -0.0129 0.0370  89  ALA   A C   
2066 O O   A ALA   A 89  ? 0.2050 0.2031 0.1879 -0.0403 0.0066  -0.0147 89  ALA   A O   
2067 O O   B ALA   A 89  ? 0.1890 0.2530 0.2180 0.0004  -0.0100 0.0247  89  ALA   A O   
2068 C CB  A ALA   A 89  ? 0.2081 0.2162 0.1333 -0.0206 0.0099  0.0183  89  ALA   A CB  
2069 C CB  B ALA   A 89  ? 0.1817 0.2577 0.1827 0.0035  -0.0192 0.0268  89  ALA   A CB  
2080 N N   A LYS   A 90  ? 0.2294 0.2263 0.1620 -0.0223 -0.0086 0.0229  90  LYS   A N   
2081 N N   B LYS   A 90  ? 0.2024 0.2522 0.1532 -0.0000 -0.0124 0.0316  90  LYS   A N   
2082 C CA  A LYS   A 90  ? 0.2358 0.2518 0.2020 -0.0183 -0.0116 0.0287  90  LYS   A CA  
2083 C CA  B LYS   A 90  ? 0.2129 0.2518 0.1631 0.0045  -0.0186 0.0425  90  LYS   A CA  
2084 C C   A LYS   A 90  ? 0.2126 0.2400 0.1980 -0.0230 -0.0146 0.0117  90  LYS   A C   
2085 C C   B LYS   A 90  ? 0.1939 0.2242 0.1509 0.0002  -0.0239 0.0290  90  LYS   A C   
2086 O O   A LYS   A 90  ? 0.2171 0.2565 0.2459 -0.0257 -0.0235 -0.0022 90  LYS   A O   
2087 O O   B LYS   A 90  ? 0.2040 0.2127 0.1582 0.0008  -0.0358 0.0255  90  LYS   A O   
2088 C CB  A LYS   A 90  ? 0.2565 0.2905 0.2513 -0.0194 -0.0177 0.0507  90  LYS   A CB  
2089 C CB  B LYS   A 90  ? 0.2389 0.2869 0.2070 -0.0021 -0.0241 0.0536  90  LYS   A CB  
2090 C CG  A LYS   A 90  ? 0.2917 0.3224 0.3432 -0.0165 -0.0106 0.0618  90  LYS   A CG  
2091 C CG  B LYS   A 90  ? 0.2759 0.3157 0.3122 0.0000  -0.0182 0.0522  90  LYS   A CG  
2092 C CD  A LYS   A 90  ? 0.3281 0.3535 0.4322 -0.0162 0.0053  0.0674  90  LYS   A CD  
2093 C CD  B LYS   A 90  ? 0.3122 0.3425 0.4089 -0.0005 -0.0002 0.0451  90  LYS   A CD  
2094 C CE  A LYS   A 90  ? 0.3580 0.3819 0.4982 -0.0167 0.0178  0.0675  90  LYS   A CE  
2095 C CE  B LYS   A 90  ? 0.3415 0.3677 0.4785 -0.0017 0.0129  0.0371  90  LYS   A CE  
2096 N NZ  A LYS   A 90  ? 0.3759 0.3964 0.5470 -0.0164 0.0236  0.0677  90  LYS   A NZ  
2097 N NZ  B LYS   A 90  ? 0.3534 0.3791 0.5251 -0.0004 0.0240  0.0320  90  LYS   A NZ  
2124 N N   A HIS   A 91  ? 0.2025 0.2208 0.1546 -0.0270 -0.0280 0.0159  91  HIS   A N   
2125 N N   B HIS   A 91  ? 0.1815 0.2014 0.1113 -0.0046 -0.0252 0.0284  91  HIS   A N   
2126 C CA  A HIS   A 91  ? 0.1981 0.2078 0.1437 -0.0268 -0.0282 0.0222  91  HIS   A CA  
2127 C CA  B HIS   A 91  ? 0.1683 0.1843 0.1108 0.0044  -0.0150 0.0195  91  HIS   A CA  
2128 C C   A HIS   A 91  ? 0.1809 0.1830 0.1077 -0.0226 -0.0285 0.0285  91  HIS   A C   
2129 C C   B HIS   A 91  ? 0.1679 0.1634 0.1022 0.0016  -0.0061 0.0167  91  HIS   A C   
2130 O O   A HIS   A 91  ? 0.1624 0.1762 0.1265 -0.0338 -0.0116 0.0264  91  HIS   A O   
2131 O O   B HIS   A 91  ? 0.1630 0.1604 0.1357 0.0001  0.0202  0.0172  91  HIS   A O   
2132 C CB  A HIS   A 91  ? 0.2240 0.2358 0.2065 -0.0093 -0.0340 0.0211  91  HIS   A CB  
2133 C CB  B HIS   A 91  ? 0.1802 0.2188 0.1825 0.0238  -0.0235 0.0207  91  HIS   A CB  
2134 C CG  A HIS   A 91  ? 0.2662 0.2803 0.2562 0.0015  -0.0539 0.0045  91  HIS   A CG  
2135 C CG  B HIS   A 91  ? 0.2162 0.2669 0.2463 0.0303  -0.0439 0.0053  91  HIS   A CG  
2136 N ND1 A HIS   A 91  ? 0.2798 0.3042 0.2964 0.0081  -0.0669 -0.0158 91  HIS   A ND1 
2137 N ND1 B HIS   A 91  ? 0.2216 0.2934 0.2932 0.0343  -0.0559 -0.0143 91  HIS   A ND1 
2138 C CD2 A HIS   A 91  ? 0.2846 0.3014 0.2794 0.0092  -0.0723 0.0043  91  HIS   A CD2 
2139 C CD2 B HIS   A 91  ? 0.2369 0.2915 0.2711 0.0340  -0.0622 0.0083  91  HIS   A CD2 
2140 C CE1 A HIS   A 91  ? 0.2882 0.3120 0.2993 0.0125  -0.0742 -0.0090 91  HIS   A CE1 
2141 C CE1 B HIS   A 91  ? 0.2367 0.3020 0.2961 0.0340  -0.0611 -0.0049 91  HIS   A CE1 
2142 N NE2 A HIS   A 91  ? 0.2935 0.3137 0.2945 0.0160  -0.0804 -0.0078 91  HIS   A NE2 
2143 N NE2 B HIS   A 91  ? 0.2421 0.3066 0.2901 0.0374  -0.0674 -0.0053 91  HIS   A NE2 
2158 N N   . CYS   A 92  ? 0.1638 0.1747 0.1223 -0.0115 -0.0005 0.0267  92  CYS   A N   
2159 C CA  . CYS   A 92  ? 0.1552 0.1724 0.1088 -0.0114 0.0026  0.0269  92  CYS   A CA  
2160 C C   . CYS   A 92  ? 0.1430 0.1594 0.1458 -0.0238 0.0032  0.0213  92  CYS   A C   
2161 O O   . CYS   A 92  ? 0.1487 0.1699 0.1723 -0.0211 0.0030  0.0171  92  CYS   A O   
2162 C CB  . CYS   A 92  ? 0.1590 0.1655 0.1455 -0.0217 0.0003  0.0169  92  CYS   A CB  
2163 S SG  . CYS   A 92  ? 0.1548 0.1621 0.1461 -0.0161 0.0006  0.0156  92  CYS   A SG  
2170 N N   . LEU   A 93  ? 0.1454 0.1529 0.1433 -0.0159 0.0103  0.0166  93  LEU   A N   
2171 C CA  . LEU   A 93  ? 0.1341 0.1435 0.1264 -0.0152 0.0013  0.0228  93  LEU   A CA  
2172 C C   . LEU   A 93  ? 0.1434 0.1507 0.1263 -0.0065 0.0157  0.0205  93  LEU   A C   
2173 O O   . LEU   A 93  ? 0.1304 0.1565 0.1426 -0.0085 0.0111  0.0214  93  LEU   A O   
2174 C CB  . LEU   A 93  ? 0.1444 0.1517 0.1462 -0.0119 -0.0022 0.0208  93  LEU   A CB  
2175 C CG  . LEU   A 93  ? 0.1506 0.1485 0.1750 -0.0114 -0.0002 0.0246  93  LEU   A CG  
2176 C CD1 . LEU   A 93  ? 0.1493 0.1630 0.2007 -0.0118 0.0045  0.0218  93  LEU   A CD1 
2177 C CD2 . LEU   A 93  ? 0.1659 0.1402 0.2012 -0.0122 0.0047  0.0302  93  LEU   A CD2 
2189 N N   . HIS   A 94  ? 0.1317 0.1262 0.1415 -0.0044 0.0045  0.0219  94  HIS   A N   
2190 C CA  . HIS   A 94  ? 0.1327 0.1421 0.1384 -0.0065 0.0154  0.0331  94  HIS   A CA  
2191 C C   . HIS   A 94  ? 0.1330 0.1317 0.1510 -0.0133 0.0066  0.0070  94  HIS   A C   
2192 O O   . HIS   A 94  ? 0.1309 0.1497 0.1836 -0.0010 0.0090  -0.0150 94  HIS   A O   
2193 C CB  . HIS   A 94  ? 0.1248 0.1496 0.1454 -0.0096 0.0047  0.0150  94  HIS   A CB  
2194 C CG  . HIS   A 94  ? 0.1308 0.1386 0.1484 -0.0109 0.0029  0.0107  94  HIS   A CG  
2195 N ND1 . HIS   A 94  ? 0.1406 0.1256 0.1571 -0.0111 0.0065  0.0184  94  HIS   A ND1 
2196 C CD2 . HIS   A 94  ? 0.1326 0.1446 0.1684 -0.0086 -0.0032 -0.0075 94  HIS   A CD2 
2197 C CE1 . HIS   A 94  ? 0.1386 0.1371 0.1646 -0.0110 -0.0139 0.0139  94  HIS   A CE1 
2198 N NE2 . HIS   A 94  ? 0.1432 0.1462 0.1555 -0.0124 -0.0104 -0.0045 94  HIS   A NE2 
2206 N N   . VAL   A 95  ? 0.1285 0.1233 0.1491 -0.0061 0.0117  0.0033  95  VAL   A N   
2207 C CA  . VAL   A 95  ? 0.1385 0.1412 0.1213 -0.0037 0.0206  0.0110  95  VAL   A CA  
2208 C C   . VAL   A 95  ? 0.1420 0.1294 0.1308 -0.0225 0.0121  0.0206  95  VAL   A C   
2209 O O   . VAL   A 95  ? 0.1378 0.1478 0.1595 0.0110  0.0120  0.0084  95  VAL   A O   
2210 C CB  . VAL   A 95  ? 0.1424 0.1442 0.1290 -0.0154 0.0136  0.0040  95  VAL   A CB  
2211 C CG1 . VAL   A 95  ? 0.1519 0.1417 0.1489 -0.0147 0.0012  0.0052  95  VAL   A CG1 
2212 C CG2 . VAL   A 95  ? 0.1451 0.1354 0.1448 -0.0167 0.0096  0.0171  95  VAL   A CG2 
2222 N N   A VAL   A 96  ? 0.1450 0.1324 0.1230 -0.0118 0.0108  0.0244  96  VAL   A N   
2223 N N   B VAL   A 96  ? 0.1518 0.1307 0.1226 -0.0075 0.0086  0.0237  96  VAL   A N   
2224 C CA  A VAL   A 96  ? 0.1489 0.1445 0.1262 -0.0100 0.0108  0.0213  96  VAL   A CA  
2225 C CA  B VAL   A 96  ? 0.1619 0.1432 0.1284 -0.0055 0.0069  0.0220  96  VAL   A CA  
2226 C C   A VAL   A 96  ? 0.1472 0.1526 0.1483 -0.0107 0.0140  0.0083  96  VAL   A C   
2227 C C   B VAL   A 96  ? 0.1650 0.1475 0.1483 0.0064  0.0070  0.0138  96  VAL   A C   
2228 O O   A VAL   A 96  ? 0.1451 0.1480 0.1447 -0.0262 0.0158  -0.0007 96  VAL   A O   
2229 O O   B VAL   A 96  ? 0.1771 0.1489 0.1686 0.0118  0.0114  -0.0023 96  VAL   A O   
2230 C CB  A VAL   A 96  ? 0.1457 0.1452 0.1433 -0.0024 0.0155  0.0169  96  VAL   A CB  
2231 C CB  B VAL   A 96  ? 0.1599 0.1473 0.1385 -0.0091 0.0163  0.0146  96  VAL   A CB  
2232 C CG1 A VAL   A 96  ? 0.1562 0.1576 0.1475 -0.0128 0.0132  0.0135  96  VAL   A CG1 
2233 C CG1 B VAL   A 96  ? 0.1579 0.1575 0.1286 -0.0139 0.0326  0.0249  96  VAL   A CG1 
2234 C CG2 A VAL   A 96  ? 0.1222 0.1360 0.1519 0.0110  0.0194  0.0154  96  VAL   A CG2 
2235 C CG2 B VAL   A 96  ? 0.1519 0.1476 0.1483 -0.0139 0.0033  0.0001  96  VAL   A CG2 
2254 N N   A GLY   A 97  ? 0.1496 0.1474 0.1474 -0.0082 0.0153  0.0026  97  GLY   A N   
2255 N N   B GLY   A 97  ? 0.1594 0.1380 0.1204 0.0029  0.0032  0.0227  97  GLY   A N   
2256 C CA  A GLY   A 97  ? 0.1628 0.1579 0.1564 -0.0112 -0.0037 0.0004  97  GLY   A CA  
2257 C CA  B GLY   A 97  ? 0.1565 0.1486 0.1300 0.0033  -0.0062 0.0198  97  GLY   A CA  
2258 C C   A GLY   A 97  ? 0.1702 0.1723 0.1548 -0.0129 -0.0107 -0.0017 97  GLY   A C   
2259 C C   B GLY   A 97  ? 0.1582 0.1489 0.1169 0.0073  -0.0032 0.0185  97  GLY   A C   
2260 O O   A GLY   A 97  ? 0.1737 0.1649 0.1534 -0.0113 0.0029  -0.0007 97  GLY   A O   
2261 O O   B GLY   A 97  ? 0.1726 0.1399 0.1456 -0.0030 0.0119  0.0285  97  GLY   A O   
2268 N N   A PRO   A 98  ? 0.1748 0.1556 0.1436 -0.0107 -0.0045 0.0054  98  PRO   A N   
2269 N N   B PRO   A 98  ? 0.1744 0.1605 0.1261 0.0136  0.0059  0.0339  98  PRO   A N   
2270 C CA  A PRO   A 98  ? 0.1798 0.1788 0.1331 -0.0095 0.0003  -0.0123 98  PRO   A CA  
2271 C CA  B PRO   A 98  ? 0.1966 0.1708 0.1357 0.0131  -0.0059 0.0132  98  PRO   A CA  
2272 C C   A PRO   A 98  ? 0.1834 0.1920 0.1202 -0.0186 0.0066  0.0043  98  PRO   A C   
2273 C C   B PRO   A 98  ? 0.2174 0.1719 0.1500 0.0126  -0.0090 0.0239  98  PRO   A C   
2274 O O   A PRO   A 98  ? 0.1794 0.1794 0.1275 -0.0180 0.0171  0.0002  98  PRO   A O   
2275 O O   B PRO   A 98  ? 0.2181 0.1684 0.1784 0.0188  0.0116  0.0294  98  PRO   A O   
2276 C CB  A PRO   A 98  ? 0.1809 0.1807 0.1527 0.0084  0.0026  -0.0124 98  PRO   A CB  
2277 C CB  B PRO   A 98  ? 0.2047 0.1763 0.1348 0.0140  0.0009  0.0082  98  PRO   A CB  
2278 C CG  A PRO   A 98  ? 0.1921 0.1699 0.1467 0.0105  0.0024  -0.0128 98  PRO   A CG  
2279 C CG  B PRO   A 98  ? 0.2077 0.1764 0.1385 0.0079  0.0015  0.0041  98  PRO   A CG  
2280 C CD  A PRO   A 98  ? 0.1811 0.1602 0.1454 -0.0047 -0.0009 0.0030  98  PRO   A CD  
2281 C CD  B PRO   A 98  ? 0.1863 0.1704 0.1355 0.0096  0.0024  0.0272  98  PRO   A CD  
2296 N N   A ASN   A 99  ? 0.1875 0.2164 0.1182 -0.0198 0.0099  0.0212  99  ASN   A N   
2297 N N   B ASN   A 99  ? 0.2405 0.1791 0.1424 0.0200  -0.0145 0.0406  99  ASN   A N   
2298 C CA  A ASN   A 99  ? 0.2058 0.2449 0.1208 -0.0187 0.0059  0.0258  99  ASN   A CA  
2299 C CA  B ASN   A 99  ? 0.2591 0.1781 0.1529 0.0228  -0.0168 0.0413  99  ASN   A CA  
2300 C C   A ASN   A 99  ? 0.2254 0.2793 0.1414 -0.0228 0.0217  0.0260  99  ASN   A C   
2301 C C   B ASN   A 99  ? 0.2658 0.1922 0.1413 0.0217  -0.0072 0.0387  99  ASN   A C   
2302 O O   A ASN   A 99  ? 0.2364 0.3045 0.1740 -0.0126 0.0149  0.0155  99  ASN   A O   
2303 O O   B ASN   A 99  ? 0.2631 0.1860 0.1341 0.0277  -0.0037 0.0476  99  ASN   A O   
2304 C CB  A ASN   A 99  ? 0.2062 0.2405 0.1531 -0.0056 -0.0121 0.0276  99  ASN   A CB  
2305 C CB  B ASN   A 99  ? 0.2811 0.1798 0.2026 0.0265  -0.0261 0.0384  99  ASN   A CB  
2306 C CG  A ASN   A 99  ? 0.2103 0.2387 0.1892 0.0022  -0.0211 0.0323  99  ASN   A CG  
2307 C CG  B ASN   A 99  ? 0.3000 0.1837 0.2291 0.0211  -0.0339 0.0415  99  ASN   A CG  
2308 O OD1 A ASN   A 99  ? 0.2199 0.2404 0.1969 0.0057  -0.0151 0.0188  99  ASN   A OD1 
2309 O OD1 B ASN   A 99  ? 0.2982 0.1900 0.2258 0.0396  -0.0444 0.0510  99  ASN   A OD1 
2310 N ND2 A ASN   A 99  ? 0.2115 0.2325 0.2185 0.0027  -0.0250 0.0531  99  ASN   A ND2 
2311 N ND2 B ASN   A 99  ? 0.3145 0.1914 0.2799 0.0125  -0.0368 0.0299  99  ASN   A ND2 
2324 N N   A VAL   A 100 ? 0.2371 0.2867 0.1482 -0.0355 0.0053  0.0199  100 VAL   A N   
2325 N N   B VAL   A 100 ? 0.2766 0.2271 0.1631 0.0195  -0.0090 0.0260  100 VAL   A N   
2326 C CA  A VAL   A 100 ? 0.2575 0.3059 0.1908 -0.0374 0.0099  0.0167  100 VAL   A CA  
2327 C CA  B VAL   A 100 ? 0.3038 0.2548 0.2007 0.0155  -0.0126 0.0206  100 VAL   A CA  
2328 C C   A VAL   A 100 ? 0.2661 0.3234 0.2021 -0.0549 0.0038  0.0410  100 VAL   A C   
2329 C C   B VAL   A 100 ? 0.3149 0.2622 0.1929 0.0262  -0.0132 0.0101  100 VAL   A C   
2330 O O   A VAL   A 100 ? 0.2769 0.3305 0.2364 -0.0545 0.0165  0.0436  100 VAL   A O   
2331 O O   B VAL   A 100 ? 0.3204 0.2658 0.1756 0.0275  -0.0112 -0.0021 100 VAL   A O   
2332 C CB  A VAL   A 100 ? 0.2713 0.3056 0.2207 -0.0306 0.0264  0.0001  100 VAL   A CB  
2333 C CB  B VAL   A 100 ? 0.3170 0.2731 0.2513 0.0025  -0.0094 0.0109  100 VAL   A CB  
2334 C CG1 A VAL   A 100 ? 0.2733 0.3102 0.2463 -0.0320 0.0435  -0.0126 100 VAL   A CG1 
2335 C CG1 B VAL   A 100 ? 0.3196 0.2794 0.2781 -0.0014 -0.0197 0.0021  100 VAL   A CG1 
2336 C CG2 A VAL   A 100 ? 0.2777 0.3083 0.2138 -0.0274 0.0387  0.0048  100 VAL   A CG2 
2337 C CG2 B VAL   A 100 ? 0.3251 0.2816 0.2805 0.0029  -0.0002 0.0105  100 VAL   A CG2 
2356 N N   A ASN   A 101 ? 0.2738 0.3290 0.1938 -0.0715 -0.0181 0.0811  101 ASN   A N   
2357 N N   B ASN   A 101 ? 0.3248 0.2727 0.1975 0.0296  -0.0060 0.0053  101 ASN   A N   
2358 C CA  A ASN   A 101 ? 0.2949 0.3456 0.2234 -0.0675 -0.0309 0.1021  101 ASN   A CA  
2359 C CA  B ASN   A 101 ? 0.3413 0.2900 0.2130 0.0422  -0.0058 0.0196  101 ASN   A CA  
2360 C C   A ASN   A 101 ? 0.3215 0.3707 0.2541 -0.0572 -0.0177 0.1293  101 ASN   A C   
2361 C C   B ASN   A 101 ? 0.3613 0.3043 0.2362 0.0364  0.0033  0.0254  101 ASN   A C   
2362 O O   A ASN   A 101 ? 0.3323 0.3760 0.2851 -0.0546 -0.0215 0.1205  101 ASN   A O   
2363 O O   B ASN   A 101 ? 0.3678 0.3064 0.2441 0.0343  -0.0050 0.0385  101 ASN   A O   
2364 C CB  A ASN   A 101 ? 0.2934 0.3295 0.2035 -0.0733 -0.0557 0.0934  101 ASN   A CB  
2365 C CB  B ASN   A 101 ? 0.3450 0.2978 0.2355 0.0477  -0.0036 0.0183  101 ASN   A CB  
2366 C CG  A ASN   A 101 ? 0.3024 0.3244 0.2100 -0.0742 -0.0577 0.0663  101 ASN   A CG  
2367 C CG  B ASN   A 101 ? 0.3534 0.3040 0.2625 0.0502  0.0005  0.0076  101 ASN   A CG  
2368 O OD1 A ASN   A 101 ? 0.2986 0.3212 0.2183 -0.0678 -0.0532 0.0359  101 ASN   A OD1 
2369 O OD1 B ASN   A 101 ? 0.3574 0.3111 0.2802 0.0550  0.0031  0.0062  101 ASN   A OD1 
2370 N ND2 A ASN   A 101 ? 0.3118 0.3295 0.2214 -0.0713 -0.0682 0.0583  101 ASN   A ND2 
2371 N ND2 B ASN   A 101 ? 0.3637 0.3117 0.2687 0.0412  0.0115  0.0027  101 ASN   A ND2 
2384 N N   A LYS   A 102 ? 0.3327 0.3978 0.2802 -0.0502 -0.0137 0.1309  102 LYS   A N   
2385 N N   B LYS   A 102 ? 0.3672 0.3148 0.2648 0.0415  0.0160  0.0107  102 LYS   A N   
2386 C CA  A LYS   A 102 ? 0.3483 0.4213 0.2944 -0.0417 -0.0223 0.1166  102 LYS   A CA  
2387 C CA  B LYS   A 102 ? 0.3757 0.3372 0.2683 0.0378  0.0314  0.0064  102 LYS   A CA  
2388 C C   A LYS   A 102 ? 0.3583 0.4414 0.2911 -0.0304 -0.0143 0.1172  102 LYS   A C   
2389 C C   B LYS   A 102 ? 0.3621 0.3313 0.2466 0.0483  0.0445  0.0232  102 LYS   A C   
2390 O O   A LYS   A 102 ? 0.3642 0.4542 0.3119 -0.0254 -0.0146 0.1095  102 LYS   A O   
2391 O O   B LYS   A 102 ? 0.3587 0.3313 0.2707 0.0568  0.0628  0.0235  102 LYS   A O   
2392 C CB  A LYS   A 102 ? 0.3556 0.4260 0.3339 -0.0455 -0.0388 0.0866  102 LYS   A CB  
2393 C CB  B LYS   A 102 ? 0.3972 0.3624 0.3184 0.0225  0.0227  -0.0160 102 LYS   A CB  
2394 C CG  A LYS   A 102 ? 0.3623 0.4288 0.3726 -0.0448 -0.0559 0.0543  102 LYS   A CG  
2395 C CG  B LYS   A 102 ? 0.4168 0.3862 0.3755 0.0083  0.0089  -0.0248 102 LYS   A CG  
2396 C CD  A LYS   A 102 ? 0.3739 0.4351 0.4180 -0.0437 -0.0666 0.0191  102 LYS   A CD  
2397 C CD  B LYS   A 102 ? 0.4329 0.4070 0.4394 -0.0006 -0.0025 -0.0321 102 LYS   A CD  
2398 C CE  A LYS   A 102 ? 0.3826 0.4380 0.4546 -0.0410 -0.0683 -0.0043 102 LYS   A CE  
2399 C CE  B LYS   A 102 ? 0.4484 0.4257 0.4920 -0.0076 -0.0127 -0.0338 102 LYS   A CE  
2400 N NZ  A LYS   A 102 ? 0.3898 0.4419 0.4740 -0.0424 -0.0675 -0.0226 102 LYS   A NZ  
2401 N NZ  B LYS   A 102 ? 0.4553 0.4317 0.5243 -0.0103 -0.0177 -0.0339 102 LYS   A NZ  
2428 N N   A GLY   A 103 ? 0.3622 0.4505 0.3078 -0.0220 -0.0121 0.1034  103 GLY   A N   
2429 N N   B GLY   A 103 ? 0.3475 0.3273 0.2048 0.0591  0.0381  0.0179  103 GLY   A N   
2430 C CA  A GLY   A 103 ? 0.3646 0.4561 0.3216 -0.0140 0.0032  0.0892  103 GLY   A CA  
2431 C CA  B GLY   A 103 ? 0.3336 0.3218 0.2106 0.0732  0.0183  0.0333  103 GLY   A CA  
2432 C C   A GLY   A 103 ? 0.3627 0.4612 0.3387 -0.0087 0.0208  0.0728  103 GLY   A C   
2433 C C   B GLY   A 103 ? 0.3200 0.3187 0.2164 0.0784  0.0009  0.0382  103 GLY   A C   
2434 O O   A GLY   A 103 ? 0.3706 0.4696 0.3669 0.0015  0.0232  0.0633  103 GLY   A O   
2435 O O   B GLY   A 103 ? 0.3307 0.3273 0.2320 0.0832  0.0007  0.0260  103 GLY   A O   
2442 N N   A GLU   A 104 ? 0.3469 0.4548 0.3047 -0.0200 0.0400  0.0650  104 GLU   A N   
2443 N N   B GLU   A 104 ? 0.2899 0.2997 0.1855 0.0719  -0.0170 0.0587  104 GLU   A N   
2444 C CA  A GLU   A 104 ? 0.3320 0.4446 0.2864 -0.0301 0.0407  0.0527  104 GLU   A CA  
2445 C CA  B GLU   A 104 ? 0.2680 0.2921 0.1731 0.0548  -0.0182 0.0543  104 GLU   A CA  
2446 C C   A GLU   A 104 ? 0.3363 0.4508 0.2876 -0.0262 0.0280  0.0311  104 GLU   A C   
2447 C C   B GLU   A 104 ? 0.2564 0.2960 0.1850 0.0472  -0.0089 0.0279  104 GLU   A C   
2448 O O   A GLU   A 104 ? 0.3316 0.4500 0.2925 -0.0292 0.0179  0.0302  104 GLU   A O   
2449 O O   B GLU   A 104 ? 0.2482 0.2935 0.2232 0.0391  -0.0164 0.0196  104 GLU   A O   
2450 C CB  A GLU   A 104 ? 0.3090 0.4265 0.2678 -0.0445 0.0544  0.0638  104 GLU   A CB  
2451 C CB  B GLU   A 104 ? 0.2614 0.2807 0.1652 0.0341  -0.0226 0.0793  104 GLU   A CB  
2452 C CG  A GLU   A 104 ? 0.2938 0.4081 0.2706 -0.0546 0.0489  0.0662  104 GLU   A CG  
2453 C CG  B GLU   A 104 ? 0.2633 0.2787 0.1899 0.0094  -0.0217 0.0819  104 GLU   A CG  
2454 C CD  A GLU   A 104 ? 0.2743 0.3899 0.2510 -0.0627 0.0474  0.0785  104 GLU   A CD  
2455 C CD  B GLU   A 104 ? 0.2652 0.2761 0.1915 -0.0088 -0.0334 0.0872  104 GLU   A CD  
2456 O OE1 A GLU   A 104 ? 0.2619 0.3784 0.2001 -0.0697 0.0451  0.0925  104 GLU   A OE1 
2457 O OE1 B GLU   A 104 ? 0.2660 0.2719 0.2045 -0.0111 -0.0412 0.0864  104 GLU   A OE1 
2458 O OE2 A GLU   A 104 ? 0.2767 0.3881 0.2848 -0.0602 0.0476  0.0702  104 GLU   A OE2 
2459 O OE2 B GLU   A 104 ? 0.2713 0.2762 0.2036 -0.0266 -0.0239 0.0770  104 GLU   A OE2 
2472 N N   A ASP   A 105 ? 0.3383 0.4567 0.2974 -0.0198 0.0218  0.0033  105 ASP   A N   
2473 N N   B ASP   A 105 ? 0.2618 0.2951 0.2003 0.0393  -0.0032 0.0156  105 ASP   A N   
2474 C CA  A ASP   A 105 ? 0.3383 0.4625 0.3277 -0.0124 0.0114  -0.0288 105 ASP   A CA  
2475 C CA  B ASP   A 105 ? 0.2663 0.2958 0.2479 0.0360  0.0096  -0.0161 105 ASP   A CA  
2476 C C   A ASP   A 105 ? 0.3143 0.4519 0.3081 -0.0294 -0.0005 -0.0472 105 ASP   A C   
2477 C C   B ASP   A 105 ? 0.2496 0.2719 0.1988 0.0193  0.0049  -0.0268 105 ASP   A C   
2478 O O   A ASP   A 105 ? 0.3033 0.4534 0.2918 -0.0314 -0.0077 -0.0610 105 ASP   A O   
2479 O O   B ASP   A 105 ? 0.2258 0.2480 0.1325 0.0189  -0.0041 -0.0292 105 ASP   A O   
2480 C CB  A ASP   A 105 ? 0.3616 0.4777 0.3797 0.0093  0.0173  -0.0459 105 ASP   A CB  
2481 C CB  B ASP   A 105 ? 0.2844 0.3164 0.3251 0.0504  0.0253  -0.0398 105 ASP   A CB  
2482 C CG  A ASP   A 105 ? 0.3829 0.4905 0.4287 0.0277  0.0174  -0.0629 105 ASP   A CG  
2483 C CG  B ASP   A 105 ? 0.3033 0.3370 0.3976 0.0649  0.0396  -0.0652 105 ASP   A CG  
2484 O OD1 A ASP   A 105 ? 0.3849 0.4970 0.4340 0.0333  0.0117  -0.0772 105 ASP   A OD1 
2485 O OD1 B ASP   A 105 ? 0.3074 0.3403 0.3951 0.0657  0.0383  -0.0848 105 ASP   A OD1 
2486 O OD2 A ASP   A 105 ? 0.3942 0.4957 0.4651 0.0350  0.0241  -0.0612 105 ASP   A OD2 
2487 O OD2 B ASP   A 105 ? 0.3065 0.3417 0.4389 0.0722  0.0521  -0.0685 105 ASP   A OD2 
2496 N N   A ILE   A 106 ? 0.2972 0.4351 0.3111 -0.0460 -0.0171 -0.0587 106 ILE   A N   
2497 N N   B ILE   A 106 ? 0.2565 0.2829 0.2303 0.0102  -0.0059 -0.0292 106 ILE   A N   
2498 C CA  A ILE   A 106 ? 0.2748 0.4115 0.3092 -0.0640 -0.0297 -0.0702 106 ILE   A CA  
2499 C CA  B ILE   A 106 ? 0.2588 0.2852 0.2498 -0.0151 -0.0168 -0.0478 106 ILE   A CA  
2500 C C   A ILE   A 106 ? 0.2594 0.3795 0.3077 -0.0918 -0.0224 -0.0990 106 ILE   A C   
2501 C C   B ILE   A 106 ? 0.2659 0.2746 0.2534 -0.0284 -0.0052 -0.0471 106 ILE   A C   
2502 O O   A ILE   A 106 ? 0.2336 0.3648 0.2957 -0.1052 -0.0071 -0.0991 106 ILE   A O   
2503 O O   B ILE   A 106 ? 0.2482 0.2623 0.2418 -0.0298 0.0153  -0.0376 106 ILE   A O   
2504 C CB  A ILE   A 106 ? 0.2789 0.4202 0.3370 -0.0453 -0.0401 -0.0396 106 ILE   A CB  
2505 C CB  B ILE   A 106 ? 0.2738 0.3118 0.2946 -0.0159 -0.0255 -0.0479 106 ILE   A CB  
2506 C CG1 A ILE   A 106 ? 0.2754 0.4230 0.3712 -0.0350 -0.0354 -0.0182 106 ILE   A CG1 
2507 C CG1 B ILE   A 106 ? 0.2739 0.3290 0.3328 -0.0123 -0.0173 -0.0392 106 ILE   A CG1 
2508 C CG2 A ILE   A 106 ? 0.2823 0.4212 0.3413 -0.0418 -0.0489 -0.0345 106 ILE   A CG2 
2509 C CG2 B ILE   A 106 ? 0.2812 0.3171 0.3039 -0.0190 -0.0274 -0.0515 106 ILE   A CG2 
2510 C CD1 A ILE   A 106 ? 0.2825 0.4252 0.3958 -0.0239 -0.0272 -0.0074 106 ILE   A CD1 
2511 C CD1 B ILE   A 106 ? 0.2801 0.3363 0.3563 -0.0068 -0.0037 -0.0420 106 ILE   A CD1 
2534 N N   A GLN   A 107 ? 0.2897 0.3678 0.3397 -0.0881 -0.0125 -0.1144 107 GLN   A N   
2535 N N   B GLN   A 107 ? 0.2979 0.2704 0.2835 -0.0329 0.0006  -0.0478 107 GLN   A N   
2536 C CA  A GLN   A 107 ? 0.3148 0.3520 0.3916 -0.0761 0.0128  -0.1093 107 GLN   A CA  
2537 C CA  B GLN   A 107 ? 0.3279 0.2784 0.3484 -0.0362 0.0116  -0.0380 107 GLN   A CA  
2538 C C   A GLN   A 107 ? 0.2782 0.2957 0.3663 -0.0659 0.0406  -0.0866 107 GLN   A C   
2539 C C   B GLN   A 107 ? 0.2972 0.2380 0.3304 -0.0362 0.0300  -0.0215 107 GLN   A C   
2540 O O   A GLN   A 107 ? 0.2790 0.2889 0.4184 -0.0593 0.0610  -0.0951 107 GLN   A O   
2541 O O   B GLN   A 107 ? 0.3032 0.2330 0.3641 -0.0471 0.0311  -0.0236 107 GLN   A O   
2542 C CB  A GLN   A 107 ? 0.3717 0.3922 0.4810 -0.0790 0.0051  -0.1037 107 GLN   A CB  
2543 C CB  B GLN   A 107 ? 0.3797 0.3318 0.4326 -0.0457 -0.0014 -0.0412 107 GLN   A CB  
2544 C CG  A GLN   A 107 ? 0.4244 0.4324 0.5805 -0.0751 -0.0029 -0.0863 107 GLN   A CG  
2545 C CG  B GLN   A 107 ? 0.4262 0.3838 0.5248 -0.0469 -0.0171 -0.0279 107 GLN   A CG  
2546 C CD  A GLN   A 107 ? 0.4661 0.4633 0.6678 -0.0705 -0.0098 -0.0664 107 GLN   A CD  
2547 C CD  B GLN   A 107 ? 0.4669 0.4185 0.6083 -0.0461 -0.0273 -0.0125 107 GLN   A CD  
2548 O OE1 A GLN   A 107 ? 0.4810 0.4744 0.7013 -0.0690 -0.0104 -0.0588 107 GLN   A OE1 
2549 O OE1 B GLN   A 107 ? 0.4784 0.4359 0.6352 -0.0474 -0.0294 -0.0046 107 GLN   A OE1 
2550 N NE2 A GLN   A 107 ? 0.4781 0.4726 0.6970 -0.0689 -0.0148 -0.0635 107 GLN   A NE2 
2551 N NE2 B GLN   A 107 ? 0.4768 0.4375 0.6365 -0.0454 -0.0360 -0.0099 107 GLN   A NE2 
2568 N N   A LEU   A 108 ? 0.2419 0.2434 0.2810 -0.0595 0.0495  -0.0713 108 LEU   A N   
2569 N N   B LEU   A 108 ? 0.2644 0.2106 0.2683 -0.0300 0.0394  -0.0116 108 LEU   A N   
2570 C CA  A LEU   A 108 ? 0.2165 0.2091 0.2288 -0.0448 0.0396  -0.0299 108 LEU   A CA  
2571 C CA  B LEU   A 108 ? 0.2378 0.1909 0.2289 -0.0180 0.0349  0.0000  108 LEU   A CA  
2572 C C   A LEU   A 108 ? 0.1988 0.1729 0.2037 -0.0268 0.0214  -0.0068 108 LEU   A C   
2573 C C   B LEU   A 108 ? 0.2105 0.1662 0.2037 -0.0136 0.0179  0.0055  108 LEU   A C   
2574 O O   A LEU   A 108 ? 0.1975 0.1713 0.2189 -0.0218 0.0252  -0.0019 108 LEU   A O   
2575 O O   B LEU   A 108 ? 0.2094 0.1665 0.2160 -0.0100 0.0204  0.0058  108 LEU   A O   
2576 C CB  A LEU   A 108 ? 0.2176 0.2227 0.2115 -0.0514 0.0431  -0.0212 108 LEU   A CB  
2577 C CB  B LEU   A 108 ? 0.2441 0.2068 0.2205 -0.0140 0.0365  0.0013  108 LEU   A CB  
2578 C CG  A LEU   A 108 ? 0.2312 0.2434 0.2357 -0.0323 0.0491  -0.0192 108 LEU   A CG  
2579 C CG  B LEU   A 108 ? 0.2553 0.2184 0.2429 0.0075  0.0396  0.0027  108 LEU   A CG  
2580 C CD1 A LEU   A 108 ? 0.2421 0.2524 0.2500 -0.0410 0.0539  -0.0134 108 LEU   A CD1 
2581 C CD1 B LEU   A 108 ? 0.2671 0.2251 0.2490 0.0002  0.0478  0.0104  108 LEU   A CD1 
2582 C CD2 A LEU   A 108 ? 0.2321 0.2608 0.2676 -0.0230 0.0508  -0.0107 108 LEU   A CD2 
2583 C CD2 B LEU   A 108 ? 0.2554 0.2359 0.2762 0.0166  0.0350  0.0051  108 LEU   A CD2 
2606 N N   . LEU   A 109 ? 0.1905 0.1583 0.1934 -0.0024 0.0174  0.0058  109 LEU   A N   
2607 C CA  . LEU   A 109 ? 0.1756 0.1598 0.1765 0.0020  0.0047  0.0173  109 LEU   A CA  
2608 C C   . LEU   A 109 ? 0.1559 0.1544 0.1589 -0.0082 0.0141  -0.0019 109 LEU   A C   
2609 O O   . LEU   A 109 ? 0.1705 0.1431 0.1816 -0.0082 0.0041  -0.0015 109 LEU   A O   
2610 C CB  . LEU   A 109 ? 0.1811 0.1662 0.1994 0.0101  0.0051  0.0186  109 LEU   A CB  
2611 C CG  . LEU   A 109 ? 0.1770 0.1762 0.2166 0.0047  0.0105  0.0310  109 LEU   A CG  
2612 C CD1 . LEU   A 109 ? 0.1795 0.1569 0.2166 -0.0062 0.0085  0.0127  109 LEU   A CD1 
2613 C CD2 . LEU   A 109 ? 0.1709 0.2018 0.2539 -0.0065 -0.0117 0.0403  109 LEU   A CD2 
2626 N N   . LYS   A 110 ? 0.1611 0.1587 0.1881 -0.0097 -0.0018 -0.0003 110 LYS   A N   
2627 C CA  . LYS   A 110 ? 0.1611 0.1439 0.2059 -0.0093 -0.0074 0.0101  110 LYS   A CA  
2628 C C   . LYS   A 110 ? 0.1617 0.1330 0.1816 -0.0228 0.0013  -0.0018 110 LYS   A C   
2629 O O   . LYS   A 110 ? 0.1548 0.1378 0.2083 -0.0077 0.0041  -0.0099 110 LYS   A O   
2630 C CB  . LYS   A 110 ? 0.1795 0.1520 0.2333 -0.0074 -0.0143 0.0031  110 LYS   A CB  
2631 C CG  . LYS   A 110 ? 0.1787 0.1519 0.2350 -0.0031 -0.0174 -0.0017 110 LYS   A CG  
2632 C CD  . LYS   A 110 ? 0.1702 0.1697 0.2341 -0.0127 -0.0079 -0.0099 110 LYS   A CD  
2633 C CE  . LYS   A 110 ? 0.1823 0.1726 0.2610 -0.0176 -0.0017 0.0027  110 LYS   A CE  
2634 N NZ  . LYS   A 110 ? 0.1796 0.1645 0.2820 -0.0178 0.0115  0.0072  110 LYS   A NZ  
2648 N N   . SER   A 111 ? 0.1689 0.1400 0.1917 -0.0108 -0.0044 -0.0020 111 SER   A N   
2649 C CA  . SER   A 111 ? 0.1512 0.1524 0.1840 -0.0106 0.0049  0.0064  111 SER   A CA  
2650 C C   . SER   A 111 ? 0.1496 0.1453 0.1628 -0.0119 0.0073  0.0030  111 SER   A C   
2651 O O   . SER   A 111 ? 0.1619 0.1378 0.1993 -0.0079 0.0098  0.0057  111 SER   A O   
2652 C CB  . SER   A 111 ? 0.1764 0.1719 0.1957 -0.0077 0.0200  -0.0115 111 SER   A CB  
2653 O OG  . SER   A 111 ? 0.2256 0.1883 0.2013 -0.0021 0.0219  -0.0125 111 SER   A OG  
2659 N N   . ALA   A 112 ? 0.1491 0.1383 0.1847 -0.0037 0.0055  0.0079  112 ALA   A N   
2660 C CA  . ALA   A 112 ? 0.1550 0.1280 0.1736 -0.0055 0.0154  -0.0017 112 ALA   A CA  
2661 C C   . ALA   A 112 ? 0.1414 0.1286 0.1758 0.0036  0.0025  -0.0036 112 ALA   A C   
2662 O O   . ALA   A 112 ? 0.1556 0.1328 0.1924 -0.0160 0.0123  0.0127  112 ALA   A O   
2663 C CB  . ALA   A 112 ? 0.1657 0.1389 0.1846 -0.0060 0.0078  0.0137  112 ALA   A CB  
2669 N N   . TYR   A 113 ? 0.1345 0.1436 0.1885 -0.0105 0.0135  0.0104  113 TYR   A N   
2670 C CA  . TYR   A 113 ? 0.1428 0.1294 0.1680 -0.0154 0.0226  0.0103  113 TYR   A CA  
2671 C C   . TYR   A 113 ? 0.1534 0.1269 0.1545 -0.0103 0.0122  0.0130  113 TYR   A C   
2672 O O   . TYR   A 113 ? 0.1449 0.1346 0.1826 -0.0060 0.0193  0.0134  113 TYR   A O   
2673 C CB  . TYR   A 113 ? 0.1376 0.1575 0.1796 -0.0130 0.0076  0.0127  113 TYR   A CB  
2674 C CG  . TYR   A 113 ? 0.1424 0.1486 0.1623 -0.0189 0.0098  0.0178  113 TYR   A CG  
2675 C CD1 . TYR   A 113 ? 0.1340 0.1562 0.1927 -0.0037 0.0144  0.0129  113 TYR   A CD1 
2676 C CD2 . TYR   A 113 ? 0.1512 0.1560 0.1872 -0.0195 0.0044  0.0082  113 TYR   A CD2 
2677 C CE1 . TYR   A 113 ? 0.1565 0.1726 0.1988 -0.0079 0.0188  0.0091  113 TYR   A CE1 
2678 C CE2 . TYR   A 113 ? 0.1527 0.1704 0.1967 -0.0080 0.0020  0.0141  113 TYR   A CE2 
2679 C CZ  . TYR   A 113 ? 0.1454 0.1642 0.2026 0.0024  0.0174  0.0206  113 TYR   A CZ  
2680 O OH  . TYR   A 113 ? 0.1543 0.1684 0.2336 0.0049  0.0031  0.0261  113 TYR   A OH  
2690 N N   . GLU   A 114 ? 0.1422 0.1319 0.1749 -0.0068 0.0111  0.0229  114 GLU   A N   
2691 C CA  . GLU   A 114 ? 0.1533 0.1386 0.1920 -0.0036 0.0100  0.0159  114 GLU   A CA  
2692 C C   . GLU   A 114 ? 0.1271 0.1295 0.1985 0.0048  0.0063  0.0217  114 GLU   A C   
2693 O O   . GLU   A 114 ? 0.1529 0.1349 0.1890 0.0038  0.0060  0.0140  114 GLU   A O   
2694 C CB  . GLU   A 114 ? 0.1487 0.1327 0.1923 -0.0096 0.0033  0.0081  114 GLU   A CB  
2695 C CG  . GLU   A 114 ? 0.1463 0.1357 0.2301 -0.0005 0.0100  0.0014  114 GLU   A CG  
2696 C CD  . GLU   A 114 ? 0.1574 0.1356 0.2349 -0.0076 0.0013  -0.0012 114 GLU   A CD  
2697 O OE1 . GLU   A 114 ? 0.1755 0.1297 0.2280 -0.0101 0.0128  -0.0038 114 GLU   A OE1 
2698 O OE2 . GLU   A 114 ? 0.1852 0.1468 0.2475 -0.0092 0.0135  -0.0134 114 GLU   A OE2 
2705 N N   . ASN   A 115 ? 0.1348 0.1341 0.2064 -0.0085 0.0158  0.0175  115 ASN   A N   
2706 C CA  . ASN   A 115 ? 0.1408 0.1344 0.2048 -0.0123 0.0074  0.0135  115 ASN   A CA  
2707 C C   . ASN   A 115 ? 0.1465 0.1399 0.1842 -0.0116 0.0009  0.0177  115 ASN   A C   
2708 O O   . ASN   A 115 ? 0.1462 0.1538 0.2090 -0.0148 0.0220  0.0200  115 ASN   A O   
2709 C CB  . ASN   A 115 ? 0.1595 0.1378 0.1810 -0.0141 0.0113  0.0101  115 ASN   A CB  
2710 C CG  . ASN   A 115 ? 0.1564 0.1703 0.1774 -0.0125 0.0233  0.0112  115 ASN   A CG  
2711 O OD1 . ASN   A 115 ? 0.1533 0.2735 0.2173 -0.0139 0.0313  0.0302  115 ASN   A OD1 
2712 N ND2 . ASN   A 115 ? 0.1495 0.1461 0.1840 -0.0128 0.0210  0.0172  115 ASN   A ND2 
2719 N N   . PHE   A 116 ? 0.1326 0.1409 0.1952 -0.0053 0.0110  0.0191  116 PHE   A N   
2720 C CA  . PHE   A 116 ? 0.1374 0.1600 0.1811 0.0040  0.0227  0.0231  116 PHE   A CA  
2721 C C   . PHE   A 116 ? 0.1391 0.1642 0.1741 -0.0068 0.0143  0.0164  116 PHE   A C   
2722 O O   . PHE   A 116 ? 0.1424 0.1656 0.1875 0.0010  0.0214  0.0340  116 PHE   A O   
2723 C CB  . PHE   A 116 ? 0.1373 0.1498 0.1968 -0.0064 0.0226  0.0359  116 PHE   A CB  
2724 C CG  . PHE   A 116 ? 0.1358 0.1504 0.1829 -0.0075 0.0142  0.0286  116 PHE   A CG  
2725 C CD1 . PHE   A 116 ? 0.1405 0.1496 0.1880 -0.0102 0.0064  0.0194  116 PHE   A CD1 
2726 C CD2 . PHE   A 116 ? 0.1402 0.1648 0.1869 -0.0104 0.0138  0.0250  116 PHE   A CD2 
2727 C CE1 . PHE   A 116 ? 0.1443 0.1497 0.1914 -0.0190 0.0104  0.0145  116 PHE   A CE1 
2728 C CE2 . PHE   A 116 ? 0.1431 0.1558 0.2097 -0.0104 0.0059  0.0098  116 PHE   A CE2 
2729 C CZ  . PHE   A 116 ? 0.1476 0.1397 0.2046 -0.0044 0.0132  0.0181  116 PHE   A CZ  
2739 N N   . ASN   A 117 ? 0.1331 0.1484 0.1871 -0.0111 0.0154  0.0302  117 ASN   A N   
2740 C CA  . ASN   A 117 ? 0.1367 0.1496 0.2132 -0.0056 0.0226  0.0263  117 ASN   A CA  
2741 C C   . ASN   A 117 ? 0.1346 0.1628 0.2190 0.0030  0.0183  0.0320  117 ASN   A C   
2742 O O   . ASN   A 117 ? 0.1573 0.1597 0.2507 -0.0003 0.0049  0.0419  117 ASN   A O   
2743 C CB  . ASN   A 117 ? 0.1463 0.1558 0.2141 -0.0047 0.0156  0.0339  117 ASN   A CB  
2744 C CG  . ASN   A 117 ? 0.1482 0.1493 0.2260 -0.0131 0.0150  0.0305  117 ASN   A CG  
2745 O OD1 . ASN   A 117 ? 0.1490 0.1756 0.2274 -0.0245 0.0161  0.0234  117 ASN   A OD1 
2746 N ND2 . ASN   A 117 ? 0.1429 0.1432 0.2323 -0.0039 0.0085  0.0322  117 ASN   A ND2 
2753 N N   . GLN   A 118 ? 0.1360 0.1633 0.2261 -0.0145 0.0082  0.0352  118 GLN   A N   
2754 C CA  . GLN   A 118 ? 0.1464 0.1707 0.2175 -0.0126 0.0031  0.0376  118 GLN   A CA  
2755 C C   . GLN   A 118 ? 0.1511 0.1731 0.2233 -0.0122 0.0004  0.0483  118 GLN   A C   
2756 O O   . GLN   A 118 ? 0.1512 0.1990 0.2449 -0.0094 -0.0015 0.0257  118 GLN   A O   
2757 C CB  . GLN   A 118 ? 0.1589 0.1685 0.2313 -0.0030 0.0299  0.0196  118 GLN   A CB  
2758 C CG  . GLN   A 118 ? 0.1449 0.1692 0.2314 0.0005  0.0198  0.0344  118 GLN   A CG  
2759 C CD  . GLN   A 118 ? 0.1543 0.1758 0.2372 0.0029  0.0093  0.0139  118 GLN   A CD  
2760 O OE1 . GLN   A 118 ? 0.1490 0.1820 0.2662 0.0073  0.0059  0.0103  118 GLN   A OE1 
2761 N NE2 . GLN   A 118 ? 0.1561 0.1782 0.2239 0.0064  0.0187  0.0272  118 GLN   A NE2 
2770 N N   . HIS   A 119 ? 0.1567 0.1620 0.2037 -0.0037 0.0174  0.0425  119 HIS   A N   
2771 C CA  . HIS   A 119 ? 0.1624 0.1693 0.2087 -0.0082 0.0113  0.0458  119 HIS   A CA  
2772 C C   . HIS   A 119 ? 0.1796 0.1809 0.2048 -0.0110 0.0275  0.0490  119 HIS   A C   
2773 O O   . HIS   A 119 ? 0.1782 0.1789 0.2111 -0.0258 -0.0009 0.0440  119 HIS   A O   
2774 C CB  . HIS   A 119 ? 0.1579 0.1751 0.2164 -0.0045 0.0262  0.0391  119 HIS   A CB  
2775 C CG  . HIS   A 119 ? 0.1692 0.1843 0.2575 -0.0090 0.0240  0.0523  119 HIS   A CG  
2776 N ND1 . HIS   A 119 ? 0.1735 0.1982 0.3284 -0.0095 0.0305  0.0366  119 HIS   A ND1 
2777 C CD2 . HIS   A 119 ? 0.1789 0.1882 0.2886 0.0104  0.0358  0.0658  119 HIS   A CD2 
2778 C CE1 . HIS   A 119 ? 0.1781 0.1897 0.3329 -0.0070 0.0417  0.0527  119 HIS   A CE1 
2779 N NE2 . HIS   A 119 ? 0.1895 0.1925 0.3279 -0.0012 0.0502  0.0724  119 HIS   A NE2 
2787 N N   A GLU   A 120 ? 0.1889 0.2032 0.2081 -0.0041 0.0183  0.0744  120 GLU   A N   
2788 N N   B GLU   A 120 ? 0.1931 0.2048 0.2128 -0.0032 0.0113  0.0747  120 GLU   A N   
2789 C CA  A GLU   A 120 ? 0.2088 0.2257 0.2401 0.0025  0.0127  0.1040  120 GLU   A CA  
2790 C CA  B GLU   A 120 ? 0.2175 0.2329 0.2434 0.0048  -0.0013 0.0984  120 GLU   A CA  
2791 C C   A GLU   A 120 ? 0.1832 0.2133 0.2169 -0.0128 0.0290  0.1077  120 GLU   A C   
2792 C C   B GLU   A 120 ? 0.2006 0.2315 0.2314 -0.0050 0.0049  0.0843  120 GLU   A C   
2793 O O   A GLU   A 120 ? 0.1765 0.1920 0.2250 -0.0099 0.0175  0.1095  120 GLU   A O   
2794 O O   B GLU   A 120 ? 0.2045 0.2332 0.2424 -0.0096 -0.0098 0.0678  120 GLU   A O   
2795 C CB  A GLU   A 120 ? 0.2520 0.2680 0.3065 0.0167  0.0131  0.1251  120 GLU   A CB  
2796 C CB  B GLU   A 120 ? 0.2576 0.2673 0.2998 0.0125  -0.0005 0.1253  120 GLU   A CB  
2797 C CG  A GLU   A 120 ? 0.3084 0.3093 0.4105 0.0323  0.0128  0.1144  120 GLU   A CG  
2798 C CG  B GLU   A 120 ? 0.3095 0.3059 0.4001 0.0243  -0.0024 0.1105  120 GLU   A CG  
2799 C CD  A GLU   A 120 ? 0.3609 0.3484 0.5017 0.0459  0.0219  0.0969  120 GLU   A CD  
2800 C CD  B GLU   A 120 ? 0.3569 0.3449 0.4882 0.0338  0.0023  0.0883  120 GLU   A CD  
2801 O OE1 A GLU   A 120 ? 0.3791 0.3629 0.5253 0.0456  0.0197  0.0867  120 GLU   A OE1 
2802 O OE1 B GLU   A 120 ? 0.3734 0.3582 0.5042 0.0354  0.0055  0.0813  120 GLU   A OE1 
2803 O OE2 A GLU   A 120 ? 0.3781 0.3589 0.5407 0.0483  0.0247  0.0914  120 GLU   A OE2 
2804 O OE2 B GLU   A 120 ? 0.3766 0.3537 0.5289 0.0297  0.0036  0.0772  120 GLU   A OE2 
2817 N N   A VAL   A 121 ? 0.1709 0.2193 0.1915 -0.0138 0.0233  0.0880  121 VAL   A N   
2818 N N   B VAL   A 121 ? 0.1884 0.2290 0.2068 0.0000  0.0026  0.0702  121 VAL   A N   
2819 C CA  A VAL   A 121 ? 0.1806 0.2324 0.1727 -0.0166 0.0334  0.0910  121 VAL   A CA  
2820 C CA  B VAL   A 121 ? 0.1909 0.2364 0.1911 0.0008  0.0138  0.0632  121 VAL   A CA  
2821 C C   A VAL   A 121 ? 0.1765 0.2146 0.1693 -0.0264 0.0216  0.0648  121 VAL   A C   
2822 C C   B VAL   A 121 ? 0.1801 0.2112 0.1610 -0.0049 0.0106  0.0566  121 VAL   A C   
2823 O O   A VAL   A 121 ? 0.1768 0.2147 0.2034 -0.0380 0.0211  0.0405  121 VAL   A O   
2824 O O   B VAL   A 121 ? 0.1739 0.1946 0.1318 0.0083  0.0096  0.0417  121 VAL   A O   
2825 C CB  A VAL   A 121 ? 0.2019 0.2708 0.2081 -0.0100 0.0429  0.0959  121 VAL   A CB  
2826 C CB  B VAL   A 121 ? 0.2097 0.2735 0.2324 0.0068  0.0221  0.0604  121 VAL   A CB  
2827 C CG1 A VAL   A 121 ? 0.2003 0.2805 0.2325 -0.0046 0.0469  0.0887  121 VAL   A CG1 
2828 C CG1 B VAL   A 121 ? 0.2077 0.2828 0.2516 0.0115  0.0277  0.0575  121 VAL   A CG1 
2829 C CG2 A VAL   A 121 ? 0.2153 0.2913 0.2590 -0.0188 0.0367  0.0835  121 VAL   A CG2 
2830 C CG2 B VAL   A 121 ? 0.2252 0.2942 0.2735 -0.0002 0.0157  0.0464  121 VAL   A CG2 
2849 N N   . LEU   A 122 ? 0.1633 0.1901 0.1574 -0.0204 0.0110  0.0535  122 LEU   A N   
2850 C CA  . LEU   A 122 ? 0.1710 0.1694 0.1644 -0.0304 0.0180  0.0561  122 LEU   A CA  
2851 C C   . LEU   A 122 ? 0.1678 0.1720 0.1744 -0.0218 -0.0002 0.0327  122 LEU   A C   
2852 O O   . LEU   A 122 ? 0.1608 0.1849 0.1964 -0.0410 0.0000  0.0364  122 LEU   A O   
2853 C CB  . LEU   A 122 ? 0.2019 0.1715 0.2114 -0.0203 0.0142  0.0627  122 LEU   A CB  
2854 C CG  . LEU   A 122 ? 0.2005 0.1698 0.2154 -0.0093 0.0312  0.0319  122 LEU   A CG  
2855 C CD1 . LEU   A 122 ? 0.2176 0.1763 0.2045 -0.0133 0.0339  0.0391  122 LEU   A CD1 
2856 C CD2 . LEU   A 122 ? 0.2007 0.1561 0.1992 -0.0056 0.0383  0.0345  122 LEU   A CD2 
2869 N N   . LEU   A 123 ? 0.1615 0.1624 0.1737 -0.0200 0.0113  0.0371  123 LEU   A N   
2870 C CA  . LEU   A 123 ? 0.1531 0.1635 0.1601 -0.0180 0.0143  0.0388  123 LEU   A CA  
2871 C C   . LEU   A 123 ? 0.1581 0.1578 0.1484 -0.0154 0.0078  0.0361  123 LEU   A C   
2872 O O   . LEU   A 123 ? 0.1490 0.1710 0.1914 -0.0280 0.0070  0.0374  123 LEU   A O   
2873 C CB  . LEU   A 123 ? 0.1620 0.1731 0.1842 -0.0191 0.0231  0.0474  123 LEU   A CB  
2874 C CG  . LEU   A 123 ? 0.1849 0.1872 0.1756 -0.0207 0.0269  0.0323  123 LEU   A CG  
2875 C CD1 . LEU   A 123 ? 0.1894 0.1875 0.2016 -0.0251 0.0241  0.0158  123 LEU   A CD1 
2876 C CD2 . LEU   A 123 ? 0.1938 0.1874 0.1879 -0.0174 0.0186  0.0323  123 LEU   A CD2 
2888 N N   A ALA   A 124 ? 0.1555 0.1554 0.1391 -0.0247 0.0082  0.0320  124 ALA   A N   
2889 N N   B ALA   A 124 ? 0.1545 0.1544 0.1388 -0.0180 0.0055  0.0303  124 ALA   A N   
2890 C CA  A ALA   A 124 ? 0.1512 0.1470 0.1438 -0.0194 0.0016  0.0319  124 ALA   A CA  
2891 C CA  B ALA   A 124 ? 0.1487 0.1437 0.1407 -0.0071 -0.0033 0.0311  124 ALA   A CA  
2892 C C   A ALA   A 124 ? 0.1460 0.1483 0.1594 -0.0261 0.0192  0.0342  124 ALA   A C   
2893 C C   B ALA   A 124 ? 0.1495 0.1495 0.1547 -0.0155 0.0196  0.0349  124 ALA   A C   
2894 O O   A ALA   A 124 ? 0.1444 0.1573 0.1752 -0.0279 0.0053  0.0373  124 ALA   A O   
2895 O O   B ALA   A 124 ? 0.1522 0.1602 0.1696 -0.0070 0.0243  0.0506  124 ALA   A O   
2896 C CB  A ALA   A 124 ? 0.1533 0.1515 0.1595 -0.0269 0.0143  0.0358  124 ALA   A CB  
2897 C CB  B ALA   A 124 ? 0.1445 0.1452 0.1569 -0.0065 -0.0032 0.0332  124 ALA   A CB  
2908 N N   A PRO   A 125 ? 0.1410 0.1396 0.1579 -0.0082 0.0138  0.0388  125 PRO   A N   
2909 N N   B PRO   A 125 ? 0.1523 0.1492 0.1527 -0.0171 0.0126  0.0336  125 PRO   A N   
2910 C CA  A PRO   A 125 ? 0.1466 0.1460 0.1525 -0.0075 0.0020  0.0378  125 PRO   A CA  
2911 C CA  B PRO   A 125 ? 0.1649 0.1579 0.1540 -0.0208 -0.0016 0.0275  125 PRO   A CA  
2912 C C   A PRO   A 125 ? 0.1404 0.1475 0.1730 -0.0025 0.0175  0.0254  125 PRO   A C   
2913 C C   B PRO   A 125 ? 0.1707 0.1597 0.1671 -0.0124 0.0121  0.0056  125 PRO   A C   
2914 O O   A PRO   A 125 ? 0.1409 0.1335 0.1938 0.0056  0.0095  0.0111  125 PRO   A O   
2915 O O   B PRO   A 125 ? 0.1579 0.1399 0.1885 -0.0275 0.0224  0.0083  125 PRO   A O   
2916 C CB  A PRO   A 125 ? 0.1491 0.1464 0.1621 -0.0056 0.0104  0.0196  125 PRO   A CB  
2917 C CB  B PRO   A 125 ? 0.1646 0.1523 0.1680 -0.0363 0.0039  0.0221  125 PRO   A CB  
2918 C CG  A PRO   A 125 ? 0.1554 0.1460 0.1711 -0.0110 0.0146  0.0296  125 PRO   A CG  
2919 C CG  B PRO   A 125 ? 0.1708 0.1545 0.1739 -0.0308 0.0023  0.0247  125 PRO   A CG  
2920 C CD  A PRO   A 125 ? 0.1445 0.1469 0.1584 -0.0163 0.0306  0.0406  125 PRO   A CD  
2921 C CD  B PRO   A 125 ? 0.1568 0.1541 0.1571 -0.0296 0.0193  0.0330  125 PRO   A CD  
2936 N N   A LEU   A 126 ? 0.1299 0.1464 0.1664 -0.0013 0.0347  0.0201  126 LEU   A N   
2937 N N   B LEU   A 126 ? 0.1858 0.1722 0.1850 0.0017  -0.0024 -0.0040 126 LEU   A N   
2938 C CA  A LEU   A 126 ? 0.1350 0.1493 0.1757 -0.0057 0.0158  0.0161  126 LEU   A CA  
2939 C CA  B LEU   A 126 ? 0.1923 0.1740 0.2106 0.0095  -0.0170 0.0022  126 LEU   A CA  
2940 C C   A LEU   A 126 ? 0.1507 0.1490 0.1943 -0.0033 0.0060  0.0086  126 LEU   A C   
2941 C C   B LEU   A 126 ? 0.1896 0.1700 0.2135 0.0239  -0.0196 -0.0040 126 LEU   A C   
2942 O O   A LEU   A 126 ? 0.1679 0.1453 0.2254 0.0018  0.0310  0.0054  126 LEU   A O   
2943 O O   B LEU   A 126 ? 0.2113 0.1707 0.2477 0.0280  0.0186  -0.0018 126 LEU   A O   
2944 C CB  A LEU   A 126 ? 0.1423 0.1612 0.1829 -0.0180 -0.0034 0.0052  126 LEU   A CB  
2945 C CB  B LEU   A 126 ? 0.2125 0.2060 0.2668 -0.0068 -0.0222 -0.0069 126 LEU   A CB  
2946 C CG  A LEU   A 126 ? 0.1267 0.1807 0.1734 -0.0229 0.0032  0.0011  126 LEU   A CG  
2947 C CG  B LEU   A 126 ? 0.2240 0.2239 0.3033 -0.0041 -0.0313 -0.0004 126 LEU   A CG  
2948 C CD1 A LEU   A 126 ? 0.1258 0.1861 0.1848 -0.0197 -0.0016 -0.0121 126 LEU   A CD1 
2949 C CD1 B LEU   A 126 ? 0.2263 0.2318 0.3044 -0.0046 -0.0232 0.0050  126 LEU   A CD1 
2950 C CD2 A LEU   A 126 ? 0.1385 0.1815 0.1690 -0.0338 0.0104  0.0225  126 LEU   A CD2 
2951 C CD2 B LEU   A 126 ? 0.2253 0.2283 0.3182 -0.0026 -0.0400 0.0075  126 LEU   A CD2 
2974 N N   A LEU   A 127 ? 0.1391 0.1582 0.1868 -0.0030 0.0145  0.0233  127 LEU   A N   
2975 N N   B LEU   A 127 ? 0.1725 0.1673 0.1939 0.0280  -0.0329 -0.0062 127 LEU   A N   
2976 C CA  A LEU   A 127 ? 0.1457 0.1716 0.1846 0.0003  0.0238  0.0313  127 LEU   A CA  
2977 C CA  B LEU   A 127 ? 0.1784 0.1783 0.1924 0.0260  -0.0275 0.0082  127 LEU   A CA  
2978 C C   A LEU   A 127 ? 0.1468 0.1551 0.1713 0.0008  0.0238  0.0304  127 LEU   A C   
2979 C C   B LEU   A 127 ? 0.1841 0.1779 0.1864 0.0060  -0.0394 0.0083  127 LEU   A C   
2980 O O   A LEU   A 127 ? 0.1587 0.1456 0.2025 -0.0115 0.0240  0.0212  127 LEU   A O   
2981 O O   B LEU   A 127 ? 0.1911 0.1644 0.1748 -0.0106 -0.0624 0.0097  127 LEU   A O   
2982 C CB  A LEU   A 127 ? 0.1514 0.1893 0.1894 0.0121  0.0185  0.0158  127 LEU   A CB  
2983 C CB  B LEU   A 127 ? 0.1755 0.1926 0.1961 0.0243  -0.0176 0.0086  127 LEU   A CB  
2984 C CG  A LEU   A 127 ? 0.1706 0.1871 0.1874 0.0103  0.0056  0.0358  127 LEU   A CG  
2985 C CG  B LEU   A 127 ? 0.1753 0.2133 0.1830 0.0209  -0.0046 0.0241  127 LEU   A CG  
2986 C CD1 A LEU   A 127 ? 0.1809 0.1893 0.2059 0.0119  0.0204  0.0382  127 LEU   A CD1 
2987 C CD1 B LEU   A 127 ? 0.1787 0.2171 0.1824 0.0217  -0.0018 0.0396  127 LEU   A CD1 
2988 C CD2 A LEU   A 127 ? 0.1853 0.1913 0.2162 0.0117  -0.0147 0.0405  127 LEU   A CD2 
2989 C CD2 B LEU   A 127 ? 0.1819 0.2245 0.1896 0.0214  -0.0083 0.0230  127 LEU   A CD2 
3012 N N   A SER   A 128 ? 0.1568 0.1571 0.1916 -0.0015 0.0184  0.0310  128 SER   A N   
3013 N N   B SER   A 128 ? 0.1913 0.1894 0.2074 0.0015  -0.0333 0.0117  128 SER   A N   
3014 C CA  A SER   A 128 ? 0.1658 0.1694 0.1837 -0.0026 0.0076  0.0396  128 SER   A CA  
3015 C CA  B SER   A 128 ? 0.2028 0.2113 0.2133 0.0016  -0.0306 0.0115  128 SER   A CA  
3016 C C   A SER   A 128 ? 0.1738 0.1695 0.1515 0.0114  -0.0014 0.0548  128 SER   A C   
3017 C C   B SER   A 128 ? 0.2292 0.2265 0.2313 0.0026  -0.0254 0.0330  128 SER   A C   
3018 O O   A SER   A 128 ? 0.1831 0.1996 0.1351 0.0140  0.0026  0.0256  128 SER   A O   
3019 O O   B SER   A 128 ? 0.2198 0.2232 0.2521 -0.0028 -0.0104 0.0194  128 SER   A O   
3020 C CB  A SER   A 128 ? 0.1694 0.1823 0.1967 -0.0179 0.0034  0.0522  128 SER   A CB  
3021 C CB  B SER   A 128 ? 0.1881 0.2153 0.1802 -0.0085 -0.0418 0.0187  128 SER   A CB  
3022 O OG  A SER   A 128 ? 0.1658 0.1871 0.2158 -0.0189 0.0143  0.0456  128 SER   A OG  
3023 O OG  B SER   A 128 ? 0.1691 0.2141 0.1578 -0.0178 -0.0362 0.0051  128 SER   A OG  
3034 N N   A ALA   A 129 ? 0.1635 0.1691 0.1698 0.0005  0.0006  0.0614  129 ALA   A N   
3035 N N   B ALA   A 129 ? 0.2604 0.2565 0.2203 0.0116  -0.0291 0.0653  129 ALA   A N   
3036 C CA  A ALA   A 129 ? 0.1611 0.1691 0.1682 -0.0082 0.0079  0.0462  129 ALA   A CA  
3037 C CA  B ALA   A 129 ? 0.2991 0.2878 0.2453 0.0167  -0.0350 0.0585  129 ALA   A CA  
3038 C C   A ALA   A 129 ? 0.1825 0.1695 0.1844 0.0076  0.0146  0.0201  129 ALA   A C   
3039 C C   B ALA   A 129 ? 0.3287 0.3080 0.2488 0.0274  -0.0423 0.0547  129 ALA   A C   
3040 O O   A ALA   A 129 ? 0.1987 0.1704 0.2221 0.0010  0.0055  0.0313  129 ALA   A O   
3041 O O   B ALA   A 129 ? 0.3327 0.3077 0.2481 0.0343  -0.0442 0.0594  129 ALA   A O   
3042 C CB  A ALA   A 129 ? 0.1489 0.1737 0.1816 -0.0048 0.0014  0.0463  129 ALA   A CB  
3043 C CB  B ALA   A 129 ? 0.3056 0.2961 0.2714 0.0135  -0.0311 0.0530  129 ALA   A CB  
3054 N N   A GLY   A 130 ? 0.1885 0.1596 0.1646 0.0014  0.0115  0.0296  130 GLY   A N   
3055 N N   B GLY   A 130 ? 0.3502 0.3311 0.2633 0.0274  -0.0377 0.0370  130 GLY   A N   
3056 C CA  A GLY   A 130 ? 0.2097 0.1581 0.1728 0.0057  0.0020  0.0236  130 GLY   A CA  
3057 C CA  B GLY   A 130 ? 0.3641 0.3409 0.2718 0.0240  -0.0363 0.0258  130 GLY   A CA  
3058 C C   A GLY   A 130 ? 0.2214 0.1628 0.1657 -0.0106 -0.0112 0.0094  130 GLY   A C   
3059 C C   B GLY   A 130 ? 0.3735 0.3493 0.2787 0.0229  -0.0422 0.0175  130 GLY   A C   
3060 O O   A GLY   A 130 ? 0.2208 0.1428 0.1500 -0.0147 -0.0297 0.0172  130 GLY   A O   
3061 O O   B GLY   A 130 ? 0.3794 0.3515 0.2572 0.0190  -0.0497 0.0057  130 GLY   A O   
3068 N N   A ILE   A 131 ? 0.2366 0.1613 0.1606 -0.0209 -0.0116 0.0162  131 ILE   A N   
3069 N N   B ILE   A 131 ? 0.3715 0.3501 0.3100 0.0229  -0.0364 0.0106  131 ILE   A N   
3070 C CA  A ILE   A 131 ? 0.2473 0.1796 0.1599 -0.0302 -0.0284 0.0240  131 ILE   A CA  
3071 C CA  B ILE   A 131 ? 0.3689 0.3482 0.3357 0.0192  -0.0305 0.0093  131 ILE   A CA  
3072 C C   A ILE   A 131 ? 0.2161 0.1734 0.1546 -0.0338 -0.0363 0.0323  131 ILE   A C   
3073 C C   B ILE   A 131 ? 0.3519 0.3423 0.3190 0.0129  -0.0428 0.0286  131 ILE   A C   
3074 O O   A ILE   A 131 ? 0.2114 0.1726 0.1695 -0.0193 -0.0492 0.0202  131 ILE   A O   
3075 O O   B ILE   A 131 ? 0.3486 0.3445 0.3104 0.0120  -0.0365 0.0427  131 ILE   A O   
3076 C CB  A ILE   A 131 ? 0.2797 0.2020 0.1852 -0.0360 -0.0250 0.0113  131 ILE   A CB  
3077 C CB  B ILE   A 131 ? 0.3810 0.3568 0.3802 0.0180  -0.0182 -0.0110 131 ILE   A CB  
3078 C CG1 A ILE   A 131 ? 0.2875 0.2137 0.1918 -0.0444 -0.0347 -0.0023 131 ILE   A CG1 
3079 C CG1 B ILE   A 131 ? 0.3899 0.3606 0.4227 0.0150  -0.0099 -0.0215 131 ILE   A CG1 
3080 C CG2 A ILE   A 131 ? 0.2963 0.1958 0.2067 -0.0358 -0.0060 0.0184  131 ILE   A CG2 
3081 C CG2 B ILE   A 131 ? 0.3822 0.3570 0.3811 0.0194  -0.0139 -0.0170 131 ILE   A CG2 
3082 C CD1 A ILE   A 131 ? 0.2978 0.2188 0.2129 -0.0410 -0.0289 -0.0035 131 ILE   A CD1 
3083 C CD1 B ILE   A 131 ? 0.3933 0.3648 0.4493 0.0142  -0.0028 -0.0253 131 ILE   A CD1 
3106 N N   A PHE   A 132 ? 0.2042 0.1691 0.1492 -0.0335 -0.0276 0.0482  132 PHE   A N   
3107 N N   B PHE   A 132 ? 0.3368 0.3293 0.3106 0.0045  -0.0595 0.0355  132 PHE   A N   
3108 C CA  A PHE   A 132 ? 0.2009 0.1923 0.1451 -0.0355 -0.0243 0.0116  132 PHE   A CA  
3109 C CA  B PHE   A 132 ? 0.3210 0.3261 0.3218 -0.0084 -0.0727 0.0312  132 PHE   A CA  
3110 C C   A PHE   A 132 ? 0.1985 0.2095 0.1545 -0.0270 -0.0203 0.0092  132 PHE   A C   
3111 C C   B PHE   A 132 ? 0.3083 0.3221 0.2975 -0.0151 -0.0698 0.0275  132 PHE   A C   
3112 O O   A PHE   A 132 ? 0.2011 0.2148 0.1709 -0.0167 -0.0183 0.0058  132 PHE   A O   
3113 O O   B PHE   A 132 ? 0.3032 0.3164 0.2731 -0.0144 -0.0734 0.0266  132 PHE   A O   
3114 C CB  A PHE   A 132 ? 0.1971 0.1816 0.1308 -0.0267 -0.0394 0.0111  132 PHE   A CB  
3115 C CB  B PHE   A 132 ? 0.3185 0.3268 0.3643 -0.0103 -0.0847 0.0294  132 PHE   A CB  
3116 C CG  A PHE   A 132 ? 0.2006 0.1761 0.1233 -0.0191 -0.0561 0.0138  132 PHE   A CG  
3117 C CG  B PHE   A 132 ? 0.3257 0.3311 0.4185 -0.0157 -0.0834 0.0273  132 PHE   A CG  
3118 C CD1 A PHE   A 132 ? 0.2052 0.1906 0.1468 -0.0037 -0.0452 -0.0088 132 PHE   A CD1 
3119 C CD1 B PHE   A 132 ? 0.3318 0.3365 0.4540 -0.0140 -0.0805 0.0245  132 PHE   A CD1 
3120 C CD2 A PHE   A 132 ? 0.2068 0.1695 0.1478 -0.0139 -0.0528 0.0231  132 PHE   A CD2 
3121 C CD2 B PHE   A 132 ? 0.3221 0.3314 0.4265 -0.0156 -0.0858 0.0251  132 PHE   A CD2 
3122 C CE1 A PHE   A 132 ? 0.2074 0.1989 0.1580 0.0056  -0.0619 -0.0053 132 PHE   A CE1 
3123 C CE1 B PHE   A 132 ? 0.3315 0.3375 0.4633 -0.0130 -0.0853 0.0202  132 PHE   A CE1 
3124 C CE2 A PHE   A 132 ? 0.2030 0.1776 0.1655 0.0022  -0.0552 0.0238  132 PHE   A CE2 
3125 C CE2 B PHE   A 132 ? 0.3242 0.3327 0.4424 -0.0180 -0.0890 0.0199  132 PHE   A CE2 
3126 C CZ  A PHE   A 132 ? 0.2015 0.1843 0.1544 -0.0077 -0.0530 0.0113  132 PHE   A CZ  
3127 C CZ  B PHE   A 132 ? 0.3260 0.3354 0.4536 -0.0164 -0.0937 0.0183  132 PHE   A CZ  
3146 N N   A GLY   A 133 ? 0.1942 0.2266 0.1452 -0.0208 -0.0390 0.0331  133 GLY   A N   
3147 N N   B GLY   A 133 ? 0.2983 0.3187 0.3000 -0.0220 -0.0594 0.0221  133 GLY   A N   
3148 C CA  A GLY   A 133 ? 0.1937 0.2442 0.1437 -0.0225 -0.0466 0.0213  133 GLY   A CA  
3149 C CA  B GLY   A 133 ? 0.2883 0.3204 0.3049 -0.0328 -0.0619 0.0093  133 GLY   A CA  
3150 C C   A GLY   A 133 ? 0.1962 0.2539 0.1426 -0.0330 -0.0564 0.0187  133 GLY   A C   
3151 C C   B GLY   A 133 ? 0.2816 0.3223 0.3060 -0.0478 -0.0602 -0.0083 133 GLY   A C   
3152 O O   A GLY   A 133 ? 0.2033 0.2734 0.1653 -0.0506 -0.0592 0.0010  133 GLY   A O   
3153 O O   B GLY   A 133 ? 0.2831 0.3369 0.3199 -0.0479 -0.0781 -0.0068 133 GLY   A O   
3160 N N   A ALA   A 134 ? 0.1999 0.2399 0.1468 -0.0279 -0.0406 0.0182  134 ALA   A N   
3161 N N   B ALA   A 134 ? 0.2749 0.3088 0.2942 -0.0551 -0.0444 -0.0161 134 ALA   A N   
3162 C CA  A ALA   A 134 ? 0.1975 0.2380 0.1709 -0.0230 -0.0300 0.0117  134 ALA   A CA  
3163 C CA  B ALA   A 134 ? 0.2751 0.3061 0.2856 -0.0579 -0.0386 -0.0158 134 ALA   A CA  
3164 C C   A ALA   A 134 ? 0.1967 0.2431 0.1847 -0.0196 -0.0390 0.0143  134 ALA   A C   
3165 C C   B ALA   A 134 ? 0.2740 0.3085 0.2779 -0.0572 -0.0322 -0.0010 134 ALA   A C   
3166 O O   A ALA   A 134 ? 0.2032 0.2457 0.2191 -0.0135 -0.0261 0.0131  134 ALA   A O   
3167 O O   B ALA   A 134 ? 0.2744 0.3055 0.2768 -0.0621 -0.0306 0.0059  134 ALA   A O   
3168 C CB  A ALA   A 134 ? 0.1991 0.2292 0.1820 -0.0217 -0.0181 0.0060  134 ALA   A CB  
3169 C CB  B ALA   A 134 ? 0.2768 0.2999 0.2908 -0.0568 -0.0377 -0.0298 134 ALA   A CB  
3180 N N   A ASP   A 135 ? 0.2009 0.2405 0.1782 -0.0242 -0.0451 0.0289  135 ASP   A N   
3181 N N   B ASP   A 135 ? 0.2742 0.3085 0.2702 -0.0521 -0.0292 0.0179  135 ASP   A N   
3182 C CA  A ASP   A 135 ? 0.1981 0.2523 0.1761 -0.0324 -0.0492 0.0353  135 ASP   A CA  
3183 C CA  B ASP   A 135 ? 0.2782 0.3156 0.2675 -0.0442 -0.0245 0.0257  135 ASP   A CA  
3184 C C   A ASP   A 135 ? 0.1744 0.2377 0.1362 -0.0212 -0.0548 0.0424  135 ASP   A C   
3185 C C   B ASP   A 135 ? 0.2609 0.2998 0.2309 -0.0359 -0.0260 0.0197  135 ASP   A C   
3186 O O   A ASP   A 135 ? 0.1703 0.2219 0.1375 -0.0277 -0.0468 0.0449  135 ASP   A O   
3187 O O   B ASP   A 135 ? 0.2613 0.2920 0.2262 -0.0444 -0.0145 0.0171  135 ASP   A O   
3188 C CB  A ASP   A 135 ? 0.2224 0.2852 0.2274 -0.0540 -0.0599 0.0364  135 ASP   A CB  
3189 C CB  B ASP   A 135 ? 0.3009 0.3356 0.3047 -0.0490 -0.0179 0.0274  135 ASP   A CB  
3190 C CG  A ASP   A 135 ? 0.2401 0.3092 0.2840 -0.0677 -0.0582 0.0304  135 ASP   A CG  
3191 C CG  B ASP   A 135 ? 0.3177 0.3503 0.3398 -0.0481 -0.0189 0.0279  135 ASP   A CG  
3192 O OD1 A ASP   A 135 ? 0.2296 0.3209 0.2810 -0.0817 -0.0726 0.0453  135 ASP   A OD1 
3193 O OD1 B ASP   A 135 ? 0.3183 0.3604 0.3466 -0.0415 -0.0098 0.0362  135 ASP   A OD1 
3194 O OD2 A ASP   A 135 ? 0.2673 0.3246 0.3448 -0.0582 -0.0272 0.0312  135 ASP   A OD2 
3195 O OD2 B ASP   A 135 ? 0.3249 0.3545 0.3564 -0.0551 -0.0268 0.0254  135 ASP   A OD2 
3204 N N   A PRO   A 136 ? 0.1600 0.2324 0.1449 -0.0083 -0.0337 0.0336  136 PRO   A N   
3205 N N   B PRO   A 136 ? 0.2504 0.2900 0.2270 -0.0145 -0.0220 0.0207  136 PRO   A N   
3206 C CA  A PRO   A 136 ? 0.1546 0.2167 0.1560 -0.0122 -0.0110 0.0223  136 PRO   A CA  
3207 C CA  B PRO   A 136 ? 0.2380 0.2734 0.2259 -0.0081 -0.0214 0.0198  136 PRO   A CA  
3208 C C   A PRO   A 136 ? 0.1359 0.2101 0.1486 -0.0104 -0.0115 0.0233  136 PRO   A C   
3209 C C   B PRO   A 136 ? 0.2168 0.2578 0.2157 -0.0049 -0.0240 -0.0022 136 PRO   A C   
3210 O O   A PRO   A 136 ? 0.1424 0.2071 0.1384 -0.0120 -0.0222 0.0261  136 PRO   A O   
3211 O O   B PRO   A 136 ? 0.2207 0.2651 0.2063 -0.0078 -0.0128 -0.0030 136 PRO   A O   
3212 C CB  A PRO   A 136 ? 0.1680 0.2170 0.1820 -0.0009 -0.0098 0.0242  136 PRO   A CB  
3213 C CB  B PRO   A 136 ? 0.2530 0.2801 0.2299 0.0021  -0.0230 0.0340  136 PRO   A CB  
3214 C CG  A PRO   A 136 ? 0.1749 0.2266 0.2015 0.0050  0.0043  0.0394  136 PRO   A CG  
3215 C CG  B PRO   A 136 ? 0.2611 0.2869 0.2349 0.0034  -0.0200 0.0326  136 PRO   A CG  
3216 C CD  A PRO   A 136 ? 0.1782 0.2333 0.1801 0.0006  -0.0176 0.0283  136 PRO   A CD  
3217 C CD  B PRO   A 136 ? 0.2574 0.2917 0.2287 -0.0063 -0.0282 0.0222  136 PRO   A CD  
3232 N N   A ILE   A 137 ? 0.1502 0.2160 0.1628 -0.0108 -0.0168 0.0039  137 ILE   A N   
3233 N N   B ILE   A 137 ? 0.2105 0.2540 0.2167 -0.0035 -0.0263 -0.0146 137 ILE   A N   
3234 C CA  A ILE   A 137 ? 0.1656 0.2227 0.1609 -0.0187 -0.0277 -0.0039 137 ILE   A CA  
3235 C CA  B ILE   A 137 ? 0.2109 0.2581 0.2452 -0.0065 -0.0232 -0.0256 137 ILE   A CA  
3236 C C   A ILE   A 137 ? 0.1651 0.2124 0.1687 -0.0238 -0.0139 0.0043  137 ILE   A C   
3237 C C   B ILE   A 137 ? 0.2057 0.2532 0.2502 -0.0021 -0.0188 -0.0225 137 ILE   A C   
3238 O O   A ILE   A 137 ? 0.1650 0.2039 0.1863 -0.0426 0.0014  -0.0004 137 ILE   A O   
3239 O O   B ILE   A 137 ? 0.1994 0.2415 0.2671 -0.0024 -0.0005 -0.0379 137 ILE   A O   
3240 C CB  A ILE   A 137 ? 0.1815 0.2330 0.1762 -0.0232 -0.0427 -0.0169 137 ILE   A CB  
3241 C CB  B ILE   A 137 ? 0.2141 0.2680 0.2529 -0.0063 -0.0266 -0.0380 137 ILE   A CB  
3242 C CG1 A ILE   A 137 ? 0.2034 0.2538 0.1982 -0.0122 -0.0439 -0.0178 137 ILE   A CG1 
3243 C CG1 B ILE   A 137 ? 0.2205 0.2775 0.2557 -0.0050 -0.0400 -0.0590 137 ILE   A CG1 
3244 C CG2 A ILE   A 137 ? 0.1921 0.2355 0.1863 -0.0187 -0.0458 -0.0268 137 ILE   A CG2 
3245 C CG2 B ILE   A 137 ? 0.2240 0.2691 0.2455 -0.0127 -0.0296 -0.0400 137 ILE   A CG2 
3246 C CD1 A ILE   A 137 ? 0.2196 0.2618 0.2085 -0.0027 -0.0349 -0.0146 137 ILE   A CD1 
3247 C CD1 B ILE   A 137 ? 0.2339 0.2897 0.2741 -0.0070 -0.0386 -0.0620 137 ILE   A CD1 
3270 N N   A HIS   A 138 ? 0.1638 0.2117 0.1655 -0.0171 0.0147  -0.0014 138 HIS   A N   
3271 N N   B HIS   A 138 ? 0.2072 0.2631 0.2472 0.0131  -0.0092 -0.0200 138 HIS   A N   
3272 C CA  A HIS   A 138 ? 0.1641 0.1963 0.1941 -0.0147 0.0227  0.0077  138 HIS   A CA  
3273 C CA  B HIS   A 138 ? 0.2023 0.2556 0.2435 0.0146  0.0044  -0.0194 138 HIS   A CA  
3274 C C   A HIS   A 138 ? 0.1669 0.1807 0.1933 -0.0169 0.0071  0.0071  138 HIS   A C   
3275 C C   B HIS   A 138 ? 0.1805 0.2385 0.2213 0.0099  -0.0102 -0.0078 138 HIS   A C   
3276 O O   A HIS   A 138 ? 0.1743 0.1790 0.1988 -0.0253 -0.0024 0.0055  138 HIS   A O   
3277 O O   B HIS   A 138 ? 0.1748 0.2427 0.2149 0.0118  -0.0069 -0.0153 138 HIS   A O   
3278 C CB  A HIS   A 138 ? 0.1739 0.2048 0.1992 -0.0130 0.0092  -0.0061 138 HIS   A CB  
3279 C CB  B HIS   A 138 ? 0.2242 0.2573 0.2429 0.0203  0.0112  -0.0283 138 HIS   A CB  
3280 C CG  A HIS   A 138 ? 0.1863 0.2082 0.2258 -0.0183 0.0080  -0.0310 138 HIS   A CG  
3281 C CG  B HIS   A 138 ? 0.2424 0.2549 0.2576 0.0201  0.0205  -0.0372 138 HIS   A CG  
3282 N ND1 A HIS   A 138 ? 0.2018 0.2103 0.2474 -0.0274 0.0087  -0.0535 138 HIS   A ND1 
3283 N ND1 B HIS   A 138 ? 0.2538 0.2592 0.2756 0.0183  0.0229  -0.0450 138 HIS   A ND1 
3284 C CD2 A HIS   A 138 ? 0.1867 0.2065 0.2292 -0.0175 0.0035  -0.0364 138 HIS   A CD2 
3285 C CD2 B HIS   A 138 ? 0.2518 0.2562 0.2725 0.0168  0.0158  -0.0392 138 HIS   A CD2 
3286 C CE1 A HIS   A 138 ? 0.2041 0.2072 0.2583 -0.0157 0.0088  -0.0534 138 HIS   A CE1 
3287 C CE1 B HIS   A 138 ? 0.2619 0.2597 0.2895 0.0180  0.0175  -0.0434 138 HIS   A CE1 
3288 N NE2 A HIS   A 138 ? 0.1988 0.2068 0.2389 -0.0117 0.0029  -0.0473 138 HIS   A NE2 
3289 N NE2 B HIS   A 138 ? 0.2572 0.2576 0.2785 0.0214  0.0141  -0.0413 138 HIS   A NE2 
3304 N N   A SER   A 139 ? 0.1647 0.1643 0.1854 -0.0183 0.0034  0.0158  139 SER   A N   
3305 N N   B SER   A 139 ? 0.1613 0.2153 0.1933 0.0130  -0.0053 0.0084  139 SER   A N   
3306 C CA  A SER   A 139 ? 0.1571 0.1651 0.1979 -0.0214 -0.0033 0.0032  139 SER   A CA  
3307 C CA  B SER   A 139 ? 0.1531 0.1981 0.1873 -0.0023 0.0107  0.0176  139 SER   A CA  
3308 C C   A SER   A 139 ? 0.1475 0.1692 0.1951 -0.0287 -0.0010 0.0138  139 SER   A C   
3309 C C   B SER   A 139 ? 0.1447 0.1915 0.2162 -0.0112 0.0203  0.0251  139 SER   A C   
3310 O O   A SER   A 139 ? 0.1464 0.1589 0.1958 -0.0241 -0.0201 0.0225  139 SER   A O   
3311 O O   B SER   A 139 ? 0.1315 0.1770 0.2320 0.0004  0.0178  0.0034  139 SER   A O   
3312 C CB  A SER   A 139 ? 0.1521 0.1578 0.2022 -0.0155 0.0096  -0.0030 139 SER   A CB  
3313 C CB  B SER   A 139 ? 0.1513 0.1810 0.1778 0.0030  0.0353  0.0183  139 SER   A CB  
3314 O OG  A SER   A 139 ? 0.1568 0.1583 0.2244 -0.0128 -0.0073 -0.0104 139 SER   A OG  
3315 O OG  B SER   A 139 ? 0.1411 0.1663 0.1619 0.0131  0.0201  0.0182  139 SER   A OG  
3326 N N   A LEU   A 140 ? 0.1474 0.1980 0.1866 -0.0180 -0.0003 0.0354  140 LEU   A N   
3327 N N   B LEU   A 140 ? 0.1524 0.2013 0.2151 -0.0114 0.0151  0.0381  140 LEU   A N   
3328 C CA  A LEU   A 140 ? 0.1368 0.1982 0.1963 -0.0191 -0.0014 0.0342  140 LEU   A CA  
3329 C CA  B LEU   A 140 ? 0.1482 0.1905 0.2199 -0.0204 0.0114  0.0356  140 LEU   A CA  
3330 C C   A LEU   A 140 ? 0.1442 0.1989 0.2085 -0.0289 -0.0071 0.0338  140 LEU   A C   
3331 C C   B LEU   A 140 ? 0.1506 0.1959 0.2194 -0.0288 -0.0016 0.0334  140 LEU   A C   
3332 O O   A LEU   A 140 ? 0.1481 0.1929 0.2256 -0.0194 0.0001  0.0346  140 LEU   A O   
3333 O O   B LEU   A 140 ? 0.1547 0.1912 0.2362 -0.0191 0.0015  0.0333  140 LEU   A O   
3334 C CB  A LEU   A 140 ? 0.1340 0.2123 0.2060 -0.0138 0.0002  0.0331  140 LEU   A CB  
3335 C CB  B LEU   A 140 ? 0.1491 0.1903 0.2342 -0.0253 0.0239  0.0358  140 LEU   A CB  
3336 C CG  A LEU   A 140 ? 0.1404 0.2216 0.2229 -0.0217 -0.0005 0.0412  140 LEU   A CG  
3337 C CG  B LEU   A 140 ? 0.1562 0.1877 0.2483 -0.0416 0.0317  0.0434  140 LEU   A CG  
3338 C CD1 A LEU   A 140 ? 0.1475 0.2170 0.2399 -0.0117 -0.0124 0.0410  140 LEU   A CD1 
3339 C CD1 B LEU   A 140 ? 0.1694 0.1807 0.2470 -0.0372 0.0276  0.0503  140 LEU   A CD1 
3340 C CD2 A LEU   A 140 ? 0.1516 0.2314 0.2247 -0.0156 -0.0086 0.0455  140 LEU   A CD2 
3341 C CD2 B LEU   A 140 ? 0.1621 0.1988 0.2607 -0.0345 0.0278  0.0363  140 LEU   A CD2 
3364 N N   . ARG   A 141 ? 0.1616 0.2003 0.2285 -0.0304 -0.0149 0.0161  141 ARG   A N   
3365 C CA  . ARG   A 141 ? 0.1728 0.2041 0.2554 -0.0396 -0.0301 0.0105  141 ARG   A CA  
3366 C C   . ARG   A 141 ? 0.1622 0.2030 0.2393 -0.0295 -0.0203 0.0012  141 ARG   A C   
3367 O O   . ARG   A 141 ? 0.1607 0.2037 0.2721 -0.0297 -0.0000 -0.0004 141 ARG   A O   
3368 C CB  . ARG   A 141 ? 0.1947 0.2287 0.2967 -0.0434 -0.0228 -0.0137 141 ARG   A CB  
3369 C CG  . ARG   A 141 ? 0.2384 0.2682 0.3345 -0.0540 -0.0044 -0.0226 141 ARG   A CG  
3370 C CD  . ARG   A 141 ? 0.2770 0.3080 0.3723 -0.0682 -0.0012 -0.0212 141 ARG   A CD  
3371 N NE  . ARG   A 141 ? 0.2743 0.3467 0.3867 -0.0661 0.0034  -0.0129 141 ARG   A NE  
3372 C CZ  . ARG   A 141 ? 0.2741 0.3742 0.3869 -0.0837 0.0079  -0.0141 141 ARG   A CZ  
3373 N NH1 . ARG   A 141 ? 0.2591 0.3769 0.3851 -0.0973 0.0200  -0.0321 141 ARG   A NH1 
3374 N NH2 . ARG   A 141 ? 0.2890 0.3890 0.3894 -0.0830 -0.0057 -0.0092 141 ARG   A NH2 
3389 N N   . VAL   A 142 ? 0.1503 0.2012 0.2123 -0.0215 -0.0136 0.0031  142 VAL   A N   
3390 C CA  . VAL   A 142 ? 0.1645 0.1977 0.2077 -0.0226 0.0153  -0.0045 142 VAL   A CA  
3391 C C   . VAL   A 142 ? 0.1597 0.1841 0.2041 -0.0291 0.0059  0.0067  142 VAL   A C   
3392 O O   . VAL   A 142 ? 0.1610 0.1842 0.2281 -0.0151 0.0160  0.0068  142 VAL   A O   
3393 C CB  . VAL   A 142 ? 0.1645 0.2028 0.2045 -0.0162 0.0137  0.0194  142 VAL   A CB  
3394 C CG1 . VAL   A 142 ? 0.1570 0.1900 0.2207 -0.0278 0.0174  0.0084  142 VAL   A CG1 
3395 C CG2 . VAL   A 142 ? 0.1829 0.2217 0.2272 -0.0049 0.0150  0.0309  142 VAL   A CG2 
3405 N N   . CYS   A 143 ? 0.1519 0.1762 0.1843 -0.0224 0.0039  0.0058  143 CYS   A N   
3406 C CA  . CYS   A 143 ? 0.1599 0.1717 0.1964 -0.0237 0.0145  0.0194  143 CYS   A CA  
3407 C C   . CYS   A 143 ? 0.1707 0.1556 0.2119 -0.0218 0.0019  0.0374  143 CYS   A C   
3408 O O   . CYS   A 143 ? 0.1649 0.1576 0.2341 -0.0119 0.0051  0.0281  143 CYS   A O   
3409 C CB  . CYS   A 143 ? 0.1579 0.1728 0.2117 -0.0136 0.0235  0.0231  143 CYS   A CB  
3410 S SG  . CYS   A 143 ? 0.1800 0.1810 0.2174 0.0006  0.0080  0.0231  143 CYS   A SG  
3416 N N   . VAL   A 144 ? 0.1643 0.1567 0.2394 -0.0298 0.0102  0.0287  144 VAL   A N   
3417 C CA  . VAL   A 144 ? 0.1685 0.1883 0.2774 -0.0245 0.0251  0.0418  144 VAL   A CA  
3418 C C   . VAL   A 144 ? 0.1588 0.1823 0.2855 -0.0285 -0.0224 0.0350  144 VAL   A C   
3419 O O   . VAL   A 144 ? 0.1771 0.1794 0.3093 -0.0143 -0.0009 0.0442  144 VAL   A O   
3420 C CB  . VAL   A 144 ? 0.1847 0.2088 0.3233 -0.0166 0.0390  0.0432  144 VAL   A CB  
3421 C CG1 . VAL   A 144 ? 0.1894 0.2346 0.3739 -0.0259 0.0178  0.0309  144 VAL   A CG1 
3422 C CG2 . VAL   A 144 ? 0.1850 0.2070 0.3207 -0.0097 0.0225  0.0489  144 VAL   A CG2 
3432 N N   . ASP   A 145 ? 0.1670 0.1828 0.3145 -0.0329 -0.0012 0.0050  145 ASP   A N   
3433 C CA  . ASP   A 145 ? 0.1766 0.1959 0.3160 -0.0275 -0.0062 -0.0047 145 ASP   A CA  
3434 C C   . ASP   A 145 ? 0.1729 0.1777 0.3066 -0.0197 -0.0022 0.0048  145 ASP   A C   
3435 O O   . ASP   A 145 ? 0.1928 0.1829 0.3751 -0.0209 -0.0064 -0.0308 145 ASP   A O   
3436 C CB  . ASP   A 145 ? 0.1848 0.2231 0.3503 -0.0458 -0.0192 -0.0036 145 ASP   A CB  
3437 C CG  . ASP   A 145 ? 0.2070 0.2493 0.3849 -0.0584 -0.0354 0.0055  145 ASP   A CG  
3438 O OD1 . ASP   A 145 ? 0.1987 0.2733 0.4049 -0.0739 -0.0216 0.0169  145 ASP   A OD1 
3439 O OD2 . ASP   A 145 ? 0.2260 0.2700 0.3989 -0.0643 -0.0689 0.0097  145 ASP   A OD2 
3444 N N   . THR   A 146 ? 0.1626 0.1538 0.2490 -0.0289 0.0029  0.0102  146 THR   A N   
3445 C CA  . THR   A 146 ? 0.1593 0.1650 0.2353 -0.0136 -0.0048 0.0191  146 THR   A CA  
3446 C C   . THR   A 146 ? 0.1548 0.1606 0.2421 -0.0054 0.0088  0.0120  146 THR   A C   
3447 O O   . THR   A 146 ? 0.1602 0.1579 0.2776 -0.0013 0.0040  0.0174  146 THR   A O   
3448 C CB  . THR   A 146 ? 0.1533 0.1730 0.2143 -0.0115 0.0073  0.0184  146 THR   A CB  
3449 O OG1 . THR   A 146 ? 0.1540 0.1785 0.2312 -0.0106 0.0029  0.0066  146 THR   A OG1 
3450 C CG2 . THR   A 146 ? 0.1502 0.1850 0.2438 -0.0223 0.0149  0.0196  146 THR   A CG2 
3458 N N   . VAL   A 147 ? 0.1432 0.1551 0.2153 -0.0032 0.0071  0.0167  147 VAL   A N   
3459 C CA  . VAL   A 147 ? 0.1417 0.1624 0.2183 -0.0195 0.0225  0.0303  147 VAL   A CA  
3460 C C   . VAL   A 147 ? 0.1622 0.1574 0.2409 -0.0204 0.0200  0.0419  147 VAL   A C   
3461 O O   . VAL   A 147 ? 0.1647 0.1530 0.2527 -0.0224 0.0143  0.0361  147 VAL   A O   
3462 C CB  . VAL   A 147 ? 0.1559 0.1524 0.2204 -0.0096 0.0258  0.0214  147 VAL   A CB  
3463 C CG1 . VAL   A 147 ? 0.1816 0.1668 0.2254 -0.0020 0.0159  0.0350  147 VAL   A CG1 
3464 C CG2 . VAL   A 147 ? 0.1561 0.1566 0.2403 -0.0121 0.0110  0.0260  147 VAL   A CG2 
3474 N N   . ARG   A 148 ? 0.1704 0.1562 0.2385 -0.0156 0.0108  0.0576  148 ARG   A N   
3475 C CA  . ARG   A 148 ? 0.1616 0.1535 0.2541 -0.0137 0.0115  0.0520  148 ARG   A CA  
3476 C C   . ARG   A 148 ? 0.1750 0.1568 0.2539 -0.0195 0.0177  0.0697  148 ARG   A C   
3477 O O   . ARG   A 148 ? 0.1981 0.1589 0.2833 -0.0190 0.0302  0.0528  148 ARG   A O   
3478 C CB  . ARG   A 148 ? 0.1730 0.1537 0.2748 -0.0097 0.0243  0.0470  148 ARG   A CB  
3479 C CG  . ARG   A 148 ? 0.1901 0.1634 0.3152 -0.0150 0.0523  0.0318  148 ARG   A CG  
3480 C CD  . ARG   A 148 ? 0.2030 0.1557 0.3375 -0.0098 0.0699  0.0475  148 ARG   A CD  
3481 N NE  . ARG   A 148 ? 0.1998 0.1644 0.3341 -0.0004 0.0661  0.0604  148 ARG   A NE  
3482 C CZ  . ARG   A 148 ? 0.1881 0.1493 0.3092 0.0027  0.0614  0.0368  148 ARG   A CZ  
3483 N NH1 . ARG   A 148 ? 0.1945 0.1496 0.3190 -0.0141 0.0546  0.0148  148 ARG   A NH1 
3484 N NH2 . ARG   A 148 ? 0.1764 0.1810 0.2902 0.0066  0.0520  0.0425  148 ARG   A NH2 
3498 N N   . THR   A 149 ? 0.1805 0.1631 0.2435 -0.0191 0.0113  0.0529  149 THR   A N   
3499 C CA  . THR   A 149 ? 0.1765 0.1622 0.2497 -0.0175 0.0264  0.0497  149 THR   A CA  
3500 C C   . THR   A 149 ? 0.1669 0.1740 0.2373 -0.0268 0.0155  0.0562  149 THR   A C   
3501 O O   . THR   A 149 ? 0.1663 0.1725 0.2498 -0.0258 0.0062  0.0591  149 THR   A O   
3502 C CB  . THR   A 149 ? 0.1683 0.1864 0.2553 -0.0100 0.0268  0.0541  149 THR   A CB  
3503 O OG1 . THR   A 149 ? 0.1643 0.1666 0.2611 -0.0212 0.0175  0.0445  149 THR   A OG1 
3504 C CG2 . THR   A 149 ? 0.1653 0.2019 0.2497 -0.0121 0.0130  0.0405  149 THR   A CG2 
3512 N N   . ASN   A 150 ? 0.1639 0.1746 0.2470 -0.0120 0.0068  0.0755  150 ASN   A N   
3513 C CA  . ASN   A 150 ? 0.1806 0.1846 0.2276 -0.0172 -0.0048 0.0608  150 ASN   A CA  
3514 C C   . ASN   A 150 ? 0.1585 0.1830 0.2181 -0.0249 -0.0032 0.0632  150 ASN   A C   
3515 O O   . ASN   A 150 ? 0.1578 0.1971 0.2447 -0.0224 -0.0113 0.0590  150 ASN   A O   
3516 C CB  . ASN   A 150 ? 0.2381 0.2103 0.2651 -0.0194 0.0082  0.0884  150 ASN   A CB  
3517 C CG  . ASN   A 150 ? 0.2917 0.2500 0.3422 -0.0244 0.0066  0.0942  150 ASN   A CG  
3518 O OD1 . ASN   A 150 ? 0.3059 0.2595 0.3696 -0.0389 0.0280  0.1115  150 ASN   A OD1 
3519 N ND2 . ASN   A 150 ? 0.3304 0.2792 0.3951 -0.0192 -0.0059 0.0905  150 ASN   A ND2 
3526 N N   . VAL   A 151 ? 0.1567 0.1696 0.2099 -0.0299 -0.0092 0.0506  151 VAL   A N   
3527 C CA  . VAL   A 151 ? 0.1586 0.1631 0.2085 -0.0206 0.0086  0.0655  151 VAL   A CA  
3528 C C   . VAL   A 151 ? 0.1537 0.1721 0.2209 -0.0282 0.0144  0.0560  151 VAL   A C   
3529 O O   . VAL   A 151 ? 0.1670 0.1785 0.2756 -0.0247 0.0244  0.0585  151 VAL   A O   
3530 C CB  . VAL   A 151 ? 0.2000 0.1884 0.2127 -0.0199 0.0122  0.0674  151 VAL   A CB  
3531 C CG1 . VAL   A 151 ? 0.1993 0.2144 0.2377 -0.0248 -0.0059 0.0434  151 VAL   A CG1 
3532 C CG2 . VAL   A 151 ? 0.2065 0.1947 0.1989 -0.0188 0.0269  0.0559  151 VAL   A CG2 
3542 N N   A TYR   A 152 ? 0.1596 0.1723 0.2093 -0.0240 0.0092  0.0546  152 TYR   A N   
3543 N N   B TYR   A 152 ? 0.1605 0.1693 0.2052 -0.0218 0.0165  0.0571  152 TYR   A N   
3544 C CA  A TYR   A 152 ? 0.1581 0.1830 0.1840 -0.0321 -0.0003 0.0493  152 TYR   A CA  
3545 C CA  B TYR   A 152 ? 0.1616 0.1805 0.1784 -0.0247 0.0167  0.0499  152 TYR   A CA  
3546 C C   A TYR   A 152 ? 0.1520 0.1774 0.1867 -0.0319 -0.0010 0.0537  152 TYR   A C   
3547 C C   B TYR   A 152 ? 0.1520 0.1732 0.1767 -0.0289 0.0220  0.0482  152 TYR   A C   
3548 O O   A TYR   A 152 ? 0.1564 0.1643 0.2146 -0.0255 -0.0060 0.0403  152 TYR   A O   
3549 O O   B TYR   A 152 ? 0.1491 0.1532 0.1864 -0.0231 0.0459  0.0263  152 TYR   A O   
3550 C CB  A TYR   A 152 ? 0.1742 0.1850 0.1976 -0.0294 0.0078  0.0611  152 TYR   A CB  
3551 C CB  B TYR   A 152 ? 0.1819 0.1844 0.1880 -0.0149 0.0221  0.0609  152 TYR   A CB  
3552 C CG  A TYR   A 152 ? 0.1879 0.2054 0.1998 -0.0276 0.0165  0.0702  152 TYR   A CG  
3553 C CG  B TYR   A 152 ? 0.2008 0.2099 0.1897 -0.0061 0.0299  0.0642  152 TYR   A CG  
3554 C CD1 A TYR   A 152 ? 0.1955 0.2183 0.2183 -0.0223 0.0119  0.0689  152 TYR   A CD1 
3555 C CD1 B TYR   A 152 ? 0.2120 0.2299 0.2110 0.0010  0.0333  0.0624  152 TYR   A CD1 
3556 C CD2 A TYR   A 152 ? 0.1943 0.2175 0.2008 -0.0401 0.0212  0.0642  152 TYR   A CD2 
3557 C CD2 B TYR   A 152 ? 0.2020 0.2194 0.1785 -0.0109 0.0335  0.0526  152 TYR   A CD2 
3558 C CE1 A TYR   A 152 ? 0.2154 0.2249 0.2313 -0.0176 0.0143  0.0818  152 TYR   A CE1 
3559 C CE1 B TYR   A 152 ? 0.2263 0.2450 0.2274 0.0112  0.0302  0.0679  152 TYR   A CE1 
3560 C CE2 A TYR   A 152 ? 0.2159 0.2221 0.2128 -0.0381 0.0266  0.0743  152 TYR   A CE2 
3561 C CE2 B TYR   A 152 ? 0.2233 0.2359 0.1936 -0.0023 0.0373  0.0579  152 TYR   A CE2 
3562 C CZ  A TYR   A 152 ? 0.2317 0.2175 0.2171 -0.0255 0.0236  0.1018  152 TYR   A CZ  
3563 C CZ  B TYR   A 152 ? 0.2390 0.2488 0.2208 0.0044  0.0393  0.0804  152 TYR   A CZ  
3564 O OH  A TYR   A 152 ? 0.2556 0.2365 0.2534 -0.0066 0.0221  0.1072  152 TYR   A OH  
3565 O OH  B TYR   A 152 ? 0.2656 0.2839 0.2718 0.0079  0.0469  0.0895  152 TYR   A OH  
3584 N N   . LEU   A 153 ? 0.1570 0.1735 0.1974 -0.0337 0.0055  0.0546  153 LEU   A N   
3585 C CA  . LEU   A 153 ? 0.1488 0.1621 0.1908 -0.0267 0.0201  0.0500  153 LEU   A CA  
3586 C C   . LEU   A 153 ? 0.1532 0.1690 0.2133 -0.0170 0.0293  0.0534  153 LEU   A C   
3587 O O   . LEU   A 153 ? 0.1664 0.1721 0.2481 -0.0089 0.0562  0.0543  153 LEU   A O   
3588 C CB  . LEU   A 153 ? 0.1408 0.1758 0.2107 -0.0179 0.0201  0.0425  153 LEU   A CB  
3589 C CG  . LEU   A 153 ? 0.1461 0.1746 0.2152 -0.0236 0.0182  0.0359  153 LEU   A CG  
3590 C CD1 . LEU   A 153 ? 0.1610 0.1774 0.2234 -0.0207 -0.0028 0.0326  153 LEU   A CD1 
3591 C CD2 . LEU   A 153 ? 0.1661 0.1890 0.2183 -0.0294 0.0121  0.0169  153 LEU   A CD2 
3604 N N   A ALA   A 154 ? 0.1648 0.1632 0.2210 -0.0091 0.0374  0.0480  154 ALA   A N   
3605 N N   B ALA   A 154 ? 0.1546 0.1620 0.2169 -0.0156 0.0381  0.0485  154 ALA   A N   
3606 C CA  A ALA   A 154 ? 0.1848 0.1714 0.2218 0.0009  0.0328  0.0435  154 ALA   A CA  
3607 C CA  B ALA   A 154 ? 0.1661 0.1681 0.2134 -0.0105 0.0357  0.0458  154 ALA   A CA  
3608 C C   A ALA   A 154 ? 0.1959 0.1704 0.2183 0.0070  0.0363  0.0520  154 ALA   A C   
3609 C C   B ALA   A 154 ? 0.1686 0.1636 0.2044 -0.0088 0.0438  0.0568  154 ALA   A C   
3610 O O   A ALA   A 154 ? 0.1977 0.1733 0.2373 0.0120  0.0385  0.0503  154 ALA   A O   
3611 O O   B ALA   A 154 ? 0.1746 0.1706 0.2123 -0.0151 0.0435  0.0489  154 ALA   A O   
3612 C CB  A ALA   A 154 ? 0.1842 0.1770 0.2226 0.0032  0.0328  0.0352  154 ALA   A CB  
3613 C CB  B ALA   A 154 ? 0.1637 0.1740 0.2137 -0.0089 0.0346  0.0365  154 ALA   A CB  
3624 N N   A VAL   A 155 ? 0.1964 0.1732 0.2070 0.0255  0.0238  0.0476  155 VAL   A N   
3625 N N   B VAL   A 155 ? 0.1565 0.1609 0.1967 0.0149  0.0395  0.0551  155 VAL   A N   
3626 C CA  A VAL   A 155 ? 0.2114 0.1890 0.2144 0.0286  0.0134  0.0419  155 VAL   A CA  
3627 C CA  B VAL   A 155 ? 0.1727 0.1796 0.2155 0.0008  0.0417  0.0525  155 VAL   A CA  
3628 C CA  T VAL   A 155 ? 0.2124 0.2162 0.2166 0.0127  0.0090  0.0265  155 VAL   A CA  
3629 C C   A VAL   A 155 ? 0.2116 0.1995 0.2148 0.0390  0.0030  0.0378  155 VAL   A C   
3630 C C   B VAL   A 155 ? 0.1655 0.1825 0.2191 -0.0035 0.0416  0.0520  155 VAL   A C   
3631 C C   T VAL   A 155 ? 0.2039 0.2167 0.2127 0.0198  0.0082  0.0287  155 VAL   A C   
3632 O O   A VAL   A 155 ? 0.2105 0.2096 0.2249 0.0398  -0.0101 0.0290  155 VAL   A O   
3633 O O   B VAL   A 155 ? 0.1532 0.1645 0.2209 -0.0078 0.0579  0.0401  155 VAL   A O   
3634 O O   T VAL   A 155 ? 0.1997 0.2223 0.2115 0.0183  0.0008  0.0257  155 VAL   A O   
3635 C CB  A VAL   A 155 ? 0.2248 0.1899 0.2113 0.0354  0.0007  0.0397  155 VAL   A CB  
3636 C CB  B VAL   A 155 ? 0.2010 0.1874 0.2351 0.0054  0.0061  0.0374  155 VAL   A CB  
3637 C CB  T VAL   A 155 ? 0.2203 0.2135 0.2153 0.0126  0.0015  0.0218  155 VAL   A CB  
3638 C CG1 A VAL   A 155 ? 0.2398 0.2004 0.2218 0.0386  -0.0065 0.0347  155 VAL   A CG1 
3639 C CG1 B VAL   A 155 ? 0.2127 0.1900 0.2586 -0.0055 -0.0051 0.0277  155 VAL   A CG1 
3640 C CG1 T VAL   A 155 ? 0.2315 0.2190 0.2236 0.0138  -0.0046 0.0174  155 VAL   A CG1 
3641 C CG2 A VAL   A 155 ? 0.2261 0.1956 0.2203 0.0330  -0.0020 0.0374  155 VAL   A CG2 
3642 C CG2 B VAL   A 155 ? 0.2055 0.2011 0.2452 0.0218  -0.0064 0.0253  155 VAL   A CG2 
3643 C CG2 T VAL   A 155 ? 0.2205 0.2141 0.2188 0.0094  -0.0006 0.0197  155 VAL   A CG2 
3669 N N   A PHE   A 156 ? 0.2087 0.1961 0.2318 0.0429  0.0133  0.0458  156 PHE   A N   
3670 N N   B PHE   A 156 ? 0.1623 0.1810 0.2527 -0.0087 0.0395  0.0582  156 PHE   A N   
3671 N N   T PHE   A 156 ? 0.1971 0.2093 0.2244 0.0246  0.0177  0.0376  156 PHE   A N   
3672 C CA  A PHE   A 156 ? 0.2103 0.1894 0.2474 0.0484  0.0188  0.0503  156 PHE   A CA  
3673 C CA  B PHE   A 156 ? 0.1684 0.1856 0.2779 -0.0146 0.0202  0.0752  156 PHE   A CA  
3674 C CA  T PHE   A 156 ? 0.1970 0.2032 0.2349 0.0245  0.0249  0.0455  156 PHE   A CA  
3675 C C   A PHE   A 156 ? 0.2072 0.1882 0.2652 0.0551  0.0318  0.0524  156 PHE   A C   
3676 C C   B PHE   A 156 ? 0.1765 0.2036 0.3014 -0.0119 0.0270  0.0773  156 PHE   A C   
3677 C C   T PHE   A 156 ? 0.1982 0.2064 0.2421 0.0227  0.0385  0.0511  156 PHE   A C   
3678 O O   A PHE   A 156 ? 0.2016 0.1903 0.2873 0.0579  0.0480  0.0472  156 PHE   A O   
3679 O O   B PHE   A 156 ? 0.1710 0.2119 0.3283 -0.0148 0.0228  0.0806  156 PHE   A O   
3680 O O   T PHE   A 156 ? 0.1977 0.2113 0.2583 0.0213  0.0510  0.0483  156 PHE   A O   
3681 C CB  A PHE   A 156 ? 0.2228 0.1959 0.2434 0.0429  0.0060  0.0573  156 PHE   A CB  
3682 C CB  B PHE   A 156 ? 0.1794 0.1750 0.2575 -0.0118 -0.0007 0.0805  156 PHE   A CB  
3683 C CB  T PHE   A 156 ? 0.1965 0.1949 0.2273 0.0243  0.0259  0.0540  156 PHE   A CB  
3684 C CG  A PHE   A 156 ? 0.2368 0.2028 0.2617 0.0424  -0.0106 0.0342  156 PHE   A CG  
3685 C CG  B PHE   A 156 ? 0.1987 0.1793 0.2516 -0.0061 -0.0125 0.0783  156 PHE   A CG  
3686 C CG  T PHE   A 156 ? 0.2004 0.1889 0.2291 0.0243  0.0292  0.0579  156 PHE   A CG  
3687 C CD1 A PHE   A 156 ? 0.2413 0.2038 0.2567 0.0424  -0.0080 0.0361  156 PHE   A CD1 
3688 C CD1 B PHE   A 156 ? 0.2217 0.1934 0.2685 0.0029  -0.0207 0.0548  156 PHE   A CD1 
3689 C CD1 T PHE   A 156 ? 0.2061 0.1861 0.2414 0.0276  0.0182  0.0622  156 PHE   A CD1 
3690 C CD2 A PHE   A 156 ? 0.2490 0.2079 0.2754 0.0457  -0.0218 0.0202  156 PHE   A CD2 
3691 C CD2 B PHE   A 156 ? 0.2204 0.1857 0.2773 -0.0071 -0.0169 0.0624  156 PHE   A CD2 
3692 C CD2 T PHE   A 156 ? 0.2060 0.1901 0.2315 0.0189  0.0363  0.0520  156 PHE   A CD2 
3693 C CE1 A PHE   A 156 ? 0.2454 0.2063 0.2650 0.0436  -0.0070 0.0275  156 PHE   A CE1 
3694 C CE1 B PHE   A 156 ? 0.2343 0.2061 0.2886 0.0012  -0.0119 0.0373  156 PHE   A CE1 
3695 C CE1 T PHE   A 156 ? 0.2090 0.1880 0.2454 0.0237  0.0188  0.0589  156 PHE   A CE1 
3696 C CE2 A PHE   A 156 ? 0.2586 0.2126 0.2775 0.0476  -0.0302 0.0161  156 PHE   A CE2 
3697 C CE2 B PHE   A 156 ? 0.2401 0.1913 0.2885 -0.0038 -0.0270 0.0473  156 PHE   A CE2 
3698 C CE2 T PHE   A 156 ? 0.2097 0.1870 0.2308 0.0192  0.0320  0.0531  156 PHE   A CE2 
3699 C CZ  A PHE   A 156 ? 0.2541 0.2116 0.2801 0.0513  -0.0093 0.0128  156 PHE   A CZ  
3700 C CZ  B PHE   A 156 ? 0.2437 0.2050 0.3051 -0.0087 -0.0134 0.0412  156 PHE   A CZ  
3701 C CZ  T PHE   A 156 ? 0.2117 0.1876 0.2465 0.0138  0.0258  0.0588  156 PHE   A CZ  
3729 N N   A ASP   A 157 ? 0.2114 0.2034 0.2602 0.0610  0.0169  0.0579  157 ASP   A N   
3730 N N   B ASP   A 157 ? 0.1968 0.2386 0.3099 -0.0056 0.0181  0.0885  157 ASP   A N   
3731 N N   T ASP   A 157 ? 0.2051 0.2182 0.2393 0.0230  0.0280  0.0634  157 ASP   A N   
3732 C CA  A ASP   A 157 ? 0.2235 0.2254 0.2668 0.0625  0.0061  0.0566  157 ASP   A CA  
3733 C CA  B ASP   A 157 ? 0.2176 0.2631 0.3023 0.0018  0.0097  0.0921  157 ASP   A CA  
3734 C CA  T ASP   A 157 ? 0.2174 0.2323 0.2406 0.0269  0.0201  0.0629  157 ASP   A CA  
3735 C C   A ASP   A 157 ? 0.2206 0.2518 0.2703 0.0588  0.0010  0.0647  157 ASP   A C   
3736 C C   B ASP   A 157 ? 0.2018 0.2655 0.2699 0.0098  0.0068  0.0906  157 ASP   A C   
3737 C C   T ASP   A 157 ? 0.2271 0.2524 0.2467 0.0271  0.0195  0.0616  157 ASP   A C   
3738 O O   A ASP   A 157 ? 0.2119 0.2565 0.2730 0.0643  -0.0002 0.0677  157 ASP   A O   
3739 O O   B ASP   A 157 ? 0.1863 0.2650 0.2565 0.0193  0.0035  0.0845  157 ASP   A O   
3740 O O   T ASP   A 157 ? 0.2237 0.2560 0.2499 0.0270  0.0206  0.0621  157 ASP   A O   
3741 C CB  A ASP   A 157 ? 0.2375 0.2251 0.2721 0.0708  0.0040  0.0590  157 ASP   A CB  
3742 C CB  B ASP   A 157 ? 0.2498 0.2843 0.3246 0.0037  0.0092  0.1044  157 ASP   A CB  
3743 C CB  T ASP   A 157 ? 0.2191 0.2294 0.2359 0.0328  0.0169  0.0715  157 ASP   A CB  
3744 C CG  A ASP   A 157 ? 0.2530 0.2263 0.2872 0.0818  0.0056  0.0560  157 ASP   A CG  
3745 C CG  B ASP   A 157 ? 0.2819 0.2983 0.3426 0.0118  0.0080  0.1156  157 ASP   A CG  
3746 C CG  T ASP   A 157 ? 0.2206 0.2237 0.2272 0.0416  0.0202  0.0807  157 ASP   A CG  
3747 O OD1 A ASP   A 157 ? 0.2674 0.2284 0.3018 0.0790  0.0087  0.0516  157 ASP   A OD1 
3748 O OD1 B ASP   A 157 ? 0.2869 0.3024 0.3635 0.0178  0.0080  0.1273  157 ASP   A OD1 
3749 O OD1 T ASP   A 157 ? 0.2188 0.2185 0.2117 0.0401  0.0150  0.0877  157 ASP   A OD1 
3750 O OD2 A ASP   A 157 ? 0.2534 0.2270 0.3005 0.0842  0.0128  0.0644  157 ASP   A OD2 
3751 O OD2 B ASP   A 157 ? 0.3038 0.3085 0.3462 0.0109  0.0077  0.1113  157 ASP   A OD2 
3752 O OD2 T ASP   A 157 ? 0.2181 0.2233 0.2404 0.0459  0.0337  0.0755  157 ASP   A OD2 
3765 N N   A LYS   A 158 ? 0.2302 0.2714 0.2778 0.0501  0.0005  0.0578  158 LYS   A N   
3766 N N   B LYS   A 158 ? 0.2132 0.2816 0.2610 0.0132  0.0131  0.0744  158 LYS   A N   
3767 N N   T LYS   A 158 ? 0.2437 0.2684 0.2551 0.0264  0.0178  0.0504  158 LYS   A N   
3768 C CA  A LYS   A 158 ? 0.2353 0.2934 0.2880 0.0438  0.0071  0.0543  158 LYS   A CA  
3769 C CA  B LYS   A 158 ? 0.2292 0.2989 0.2452 0.0155  0.0208  0.0569  158 LYS   A CA  
3770 C CA  T LYS   A 158 ? 0.2587 0.2861 0.2682 0.0268  0.0165  0.0441  158 LYS   A CA  
3771 C C   A LYS   A 158 ? 0.2297 0.3059 0.2700 0.0470  -0.0006 0.0599  158 LYS   A C   
3772 C C   B LYS   A 158 ? 0.2247 0.3069 0.2240 0.0273  0.0283  0.0536  158 LYS   A C   
3773 C C   T LYS   A 158 ? 0.2600 0.2929 0.2611 0.0311  0.0107  0.0396  158 LYS   A C   
3774 O O   A LYS   A 158 ? 0.2266 0.3115 0.2576 0.0450  -0.0007 0.0627  158 LYS   A O   
3775 O O   B LYS   A 158 ? 0.2176 0.3158 0.2102 0.0129  0.0223  0.0525  158 LYS   A O   
3776 O O   T LYS   A 158 ? 0.2600 0.2945 0.2553 0.0330  0.0092  0.0373  158 LYS   A O   
3777 C CB  A LYS   A 158 ? 0.2487 0.3006 0.3114 0.0364  0.0251  0.0469  158 LYS   A CB  
3778 C CB  B LYS   A 158 ? 0.2495 0.3150 0.2709 0.0094  0.0030  0.0427  158 LYS   A CB  
3779 C CB  T LYS   A 158 ? 0.2756 0.2956 0.2914 0.0234  0.0221  0.0403  158 LYS   A CB  
3780 C CG  A LYS   A 158 ? 0.2636 0.3034 0.3380 0.0298  0.0461  0.0510  158 LYS   A CG  
3781 C CG  B LYS   A 158 ? 0.2734 0.3289 0.3005 0.0063  -0.0117 0.0356  158 LYS   A CG  
3782 C CG  T LYS   A 158 ? 0.2921 0.3027 0.3181 0.0210  0.0294  0.0406  158 LYS   A CG  
3783 C CD  A LYS   A 158 ? 0.2735 0.3051 0.3646 0.0226  0.0730  0.0556  158 LYS   A CD  
3784 C CD  B LYS   A 158 ? 0.2945 0.3377 0.3310 0.0035  -0.0225 0.0246  158 LYS   A CD  
3785 C CD  T LYS   A 158 ? 0.3064 0.3109 0.3498 0.0223  0.0368  0.0426  158 LYS   A CD  
3786 C CE  A LYS   A 158 ? 0.2807 0.3015 0.3709 0.0148  0.1015  0.0720  158 LYS   A CE  
3787 C CE  B LYS   A 158 ? 0.3169 0.3470 0.3642 0.0040  -0.0411 0.0127  158 LYS   A CE  
3788 C CE  T LYS   A 158 ? 0.3188 0.3167 0.3714 0.0249  0.0417  0.0444  158 LYS   A CE  
3789 N NZ  A LYS   A 158 ? 0.2773 0.2969 0.3704 0.0063  0.1259  0.0867  158 LYS   A NZ  
3790 N NZ  B LYS   A 158 ? 0.3296 0.3514 0.3940 -0.0002 -0.0495 0.0035  158 LYS   A NZ  
3791 N NZ  T LYS   A 158 ? 0.3248 0.3201 0.3839 0.0301  0.0427  0.0461  158 LYS   A NZ  
3831 N N   A ASN   A 159 ? 0.2194 0.3101 0.2815 0.0531  -0.0014 0.0618  159 ASN   A N   
3832 N N   B ASN   A 159 ? 0.2260 0.3154 0.2318 0.0555  0.0281  0.0515  159 ASN   A N   
3833 N N   T ASN   A 159 ? 0.2592 0.2962 0.2744 0.0334  0.0092  0.0356  159 ASN   A N   
3834 C CA  A ASN   A 159 ? 0.2215 0.3084 0.2759 0.0536  0.0038  0.0634  159 ASN   A CA  
3835 C CA  B ASN   A 159 ? 0.2446 0.3204 0.2655 0.0727  0.0258  0.0610  159 ASN   A CA  
3836 C CA  T ASN   A 159 ? 0.2629 0.2951 0.2768 0.0333  0.0134  0.0328  159 ASN   A CA  
3837 C C   A ASN   A 159 ? 0.2079 0.3103 0.2570 0.0533  0.0195  0.0649  159 ASN   A C   
3838 C C   B ASN   A 159 ? 0.2420 0.3271 0.2636 0.0739  0.0289  0.0585  159 ASN   A C   
3839 C C   T ASN   A 159 ? 0.2647 0.2981 0.2725 0.0326  0.0260  0.0307  159 ASN   A C   
3840 O O   A ASN   A 159 ? 0.1974 0.3142 0.2417 0.0608  0.0192  0.0560  159 ASN   A O   
3841 O O   B ASN   A 159 ? 0.2309 0.3414 0.2600 0.0730  0.0176  0.0644  159 ASN   A O   
3842 O O   T ASN   A 159 ? 0.2641 0.3000 0.2687 0.0355  0.0318  0.0218  159 ASN   A O   
3843 C CB  A ASN   A 159 ? 0.2327 0.3078 0.3029 0.0593  -0.0022 0.0590  159 ASN   A CB  
3844 C CB  B ASN   A 159 ? 0.2711 0.3208 0.3081 0.0763  0.0374  0.0698  159 ASN   A CB  
3845 C CB  T ASN   A 159 ? 0.2646 0.2943 0.2918 0.0362  0.0084  0.0314  159 ASN   A CB  
3846 C CG  A ASN   A 159 ? 0.2452 0.3082 0.3271 0.0526  -0.0005 0.0524  159 ASN   A CG  
3847 C CG  B ASN   A 159 ? 0.2978 0.3259 0.3631 0.0661  0.0538  0.0628  159 ASN   A CG  
3848 C CG  T ASN   A 159 ? 0.2665 0.2927 0.3066 0.0338  0.0094  0.0295  159 ASN   A CG  
3849 O OD1 A ASN   A 159 ? 0.2523 0.3151 0.3346 0.0411  0.0052  0.0514  159 ASN   A OD1 
3850 O OD1 B ASN   A 159 ? 0.3158 0.3379 0.3894 0.0552  0.0682  0.0509  159 ASN   A OD1 
3851 O OD1 T ASN   A 159 ? 0.2673 0.2971 0.3130 0.0290  0.0147  0.0289  159 ASN   A OD1 
3852 N ND2 A ASN   A 159 ? 0.2481 0.3123 0.3492 0.0500  0.0064  0.0398  159 ASN   A ND2 
3853 N ND2 B ASN   A 159 ? 0.2929 0.3309 0.3762 0.0611  0.0603  0.0594  159 ASN   A ND2 
3854 N ND2 T ASN   A 159 ? 0.2675 0.2948 0.3184 0.0330  0.0119  0.0236  159 ASN   A ND2 
3873 N N   A LEU   A 160 ? 0.1890 0.3020 0.2595 0.0503  0.0118  0.0797  160 LEU   A N   
3874 N N   B LEU   A 160 ? 0.2338 0.3256 0.2636 0.0750  0.0251  0.0710  160 LEU   A N   
3875 N N   T LEU   A 160 ? 0.2605 0.2951 0.2789 0.0290  0.0242  0.0387  160 LEU   A N   
3876 C CA  A LEU   A 160 ? 0.1832 0.2985 0.2492 0.0350  0.0305  0.0967  160 LEU   A CA  
3877 C CA  B LEU   A 160 ? 0.2293 0.3183 0.2600 0.0754  0.0323  0.0805  160 LEU   A CA  
3878 C CA  T LEU   A 160 ? 0.2604 0.2938 0.2788 0.0233  0.0303  0.0494  160 LEU   A CA  
3879 C C   A LEU   A 160 ? 0.1711 0.3018 0.2283 0.0251  0.0290  0.0982  160 LEU   A C   
3880 C C   B LEU   A 160 ? 0.2114 0.2952 0.2450 0.0608  0.0282  0.0708  160 LEU   A C   
3881 O O   A LEU   A 160 ? 0.1718 0.3138 0.2285 0.0200  0.0197  0.0901  160 LEU   A O   
3882 O O   B LEU   A 160 ? 0.2088 0.2879 0.2458 0.0554  0.0272  0.0495  160 LEU   A O   
3883 C CB  A LEU   A 160 ? 0.1876 0.2955 0.2499 0.0309  0.0399  0.1041  160 LEU   A CB  
3884 C CB  B LEU   A 160 ? 0.2571 0.3320 0.2820 0.0725  0.0471  0.0880  160 LEU   A CB  
3885 C CB  T LEU   A 160 ? 0.2604 0.2941 0.2761 0.0180  0.0345  0.0567  160 LEU   A CB  
3886 C CG  A LEU   A 160 ? 0.1917 0.3012 0.2636 0.0252  0.0456  0.0881  160 LEU   A CG  
3887 C CG  B LEU   A 160 ? 0.2821 0.3497 0.3109 0.0760  0.0481  0.0773  160 LEU   A CG  
3888 C CG  T LEU   A 160 ? 0.2610 0.2983 0.2797 0.0135  0.0370  0.0531  160 LEU   A CG  
3889 C CD1 A LEU   A 160 ? 0.1956 0.3050 0.2816 0.0174  0.0543  0.0833  160 LEU   A CD1 
3890 C CD1 B LEU   A 160 ? 0.2845 0.3550 0.3227 0.0735  0.0483  0.0760  160 LEU   A CD1 
3891 C CD1 T LEU   A 160 ? 0.2615 0.3007 0.2874 0.0102  0.0406  0.0519  160 LEU   A CD1 
3892 C CD2 A LEU   A 160 ? 0.1876 0.3021 0.2545 0.0264  0.0420  0.0805  160 LEU   A CD2 
3893 C CD2 B LEU   A 160 ? 0.2957 0.3544 0.3180 0.0754  0.0523  0.0768  160 LEU   A CD2 
3894 C CD2 T LEU   A 160 ? 0.2600 0.2984 0.2739 0.0116  0.0364  0.0513  160 LEU   A CD2 
3927 N N   A TYR   A 161 ? 0.1760 0.3033 0.2475 0.0203  0.0237  0.1013  161 TYR   A N   
3928 N N   B TYR   A 161 ? 0.2068 0.2977 0.2487 0.0556  0.0284  0.0786  161 TYR   A N   
3929 C CA  A TYR   A 161 ? 0.1782 0.2991 0.2336 0.0026  0.0297  0.1031  161 TYR   A CA  
3930 C CA  B TYR   A 161 ? 0.2099 0.2974 0.2480 0.0363  0.0168  0.0863  161 TYR   A CA  
3931 C C   A TYR   A 161 ? 0.1775 0.3235 0.2394 -0.0002 0.0238  0.0908  161 TYR   A C   
3932 C C   B TYR   A 161 ? 0.2197 0.3088 0.2594 0.0259  -0.0038 0.0746  161 TYR   A C   
3933 O O   A TYR   A 161 ? 0.1629 0.3313 0.2390 0.0006  0.0246  0.0872  161 TYR   A O   
3934 O O   B TYR   A 161 ? 0.2196 0.3099 0.2543 0.0218  -0.0128 0.0709  161 TYR   A O   
3935 C CB  A TYR   A 161 ? 0.1847 0.2886 0.2480 -0.0041 0.0173  0.0923  161 TYR   A CB  
3936 C CB  B TYR   A 161 ? 0.2040 0.2932 0.2543 0.0342  0.0203  0.0823  161 TYR   A CB  
3937 C CG  A TYR   A 161 ? 0.1861 0.2751 0.2548 -0.0081 -0.0053 0.0828  161 TYR   A CG  
3938 C CG  B TYR   A 161 ? 0.2006 0.2905 0.2657 0.0341  0.0199  0.0855  161 TYR   A CG  
3939 C CD1 A TYR   A 161 ? 0.1723 0.2652 0.2792 -0.0110 -0.0132 0.0726  161 TYR   A CD1 
3940 C CD1 B TYR   A 161 ? 0.1951 0.2880 0.3005 0.0368  0.0220  0.0792  161 TYR   A CD1 
3941 C CD2 A TYR   A 161 ? 0.1929 0.2744 0.2638 -0.0045 -0.0187 0.0712  161 TYR   A CD2 
3942 C CD2 B TYR   A 161 ? 0.2020 0.2905 0.2745 0.0413  0.0085  0.0890  161 TYR   A CD2 
3943 C CE1 A TYR   A 161 ? 0.1787 0.2561 0.2807 -0.0102 -0.0127 0.0764  161 TYR   A CE1 
3944 C CE1 B TYR   A 161 ? 0.1958 0.2832 0.3035 0.0460  0.0147  0.0918  161 TYR   A CE1 
3945 C CE2 A TYR   A 161 ? 0.1936 0.2565 0.2661 -0.0087 -0.0256 0.0873  161 TYR   A CE2 
3946 C CE2 B TYR   A 161 ? 0.2041 0.2807 0.2822 0.0388  -0.0014 0.1106  161 TYR   A CE2 
3947 C CZ  A TYR   A 161 ? 0.1993 0.2449 0.2698 -0.0086 -0.0244 0.0888  161 TYR   A CZ  
3948 C CZ  B TYR   A 161 ? 0.2147 0.2809 0.3044 0.0371  0.0066  0.1059  161 TYR   A CZ  
3949 O OH  A TYR   A 161 ? 0.2192 0.2228 0.2718 -0.0056 -0.0291 0.0904  161 TYR   A OH  
3950 O OH  B TYR   A 161 ? 0.2396 0.2809 0.3386 0.0309  0.0069  0.1039  161 TYR   A OH  
3969 N N   A ASP   A 162 ? 0.1740 0.3327 0.2142 0.0112  0.0246  0.0978  162 ASP   A N   
3970 N N   B ASP   A 162 ? 0.2248 0.3212 0.2683 0.0285  -0.0135 0.0779  162 ASP   A N   
3971 C CA  A ASP   A 162 ? 0.1671 0.3494 0.2076 0.0113  0.0168  0.0868  162 ASP   A CA  
3972 C CA  B ASP   A 162 ? 0.2371 0.3425 0.3009 0.0239  -0.0257 0.0660  162 ASP   A CA  
3973 C C   A ASP   A 162 ? 0.1612 0.3519 0.1897 0.0101  0.0088  0.0862  162 ASP   A C   
3974 C C   B ASP   A 162 ? 0.2429 0.3540 0.2983 0.0174  -0.0238 0.0529  162 ASP   A C   
3975 O O   A ASP   A 162 ? 0.1471 0.3552 0.1958 0.0005  -0.0015 0.0595  162 ASP   A O   
3976 O O   B ASP   A 162 ? 0.2438 0.3624 0.2956 0.0210  -0.0177 0.0602  162 ASP   A O   
3977 C CB  A ASP   A 162 ? 0.1770 0.3692 0.2380 0.0159  0.0094  0.0670  162 ASP   A CB  
3978 C CB  B ASP   A 162 ? 0.2482 0.3554 0.3424 0.0291  -0.0333 0.0683  162 ASP   A CB  
3979 C CG  A ASP   A 162 ? 0.1846 0.3877 0.2548 0.0228  0.0311  0.0497  162 ASP   A CG  
3980 C CG  B ASP   A 162 ? 0.2574 0.3632 0.3833 0.0363  -0.0502 0.0763  162 ASP   A CG  
3981 O OD1 A ASP   A 162 ? 0.1954 0.3993 0.2593 0.0272  0.0232  0.0510  162 ASP   A OD1 
3982 O OD1 B ASP   A 162 ? 0.2578 0.3647 0.3950 0.0433  -0.0581 0.0863  162 ASP   A OD1 
3983 O OD2 A ASP   A 162 ? 0.1956 0.3933 0.2630 0.0316  0.0374  0.0308  162 ASP   A OD2 
3984 O OD2 B ASP   A 162 ? 0.2682 0.3718 0.4091 0.0365  -0.0451 0.0717  162 ASP   A OD2 
3993 N N   A LYS   A 163 ? 0.1852 0.3589 0.2018 0.0206  -0.0041 0.0801  163 LYS   A N   
3994 N N   B LYS   A 163 ? 0.2511 0.3613 0.2927 0.0071  -0.0094 0.0393  163 LYS   A N   
3995 C CA  A LYS   A 163 ? 0.2091 0.3680 0.2119 0.0217  0.0047  0.0758  163 LYS   A CA  
3996 C CA  B LYS   A 163 ? 0.2634 0.3674 0.3102 -0.0041 0.0027  0.0173  163 LYS   A CA  
3997 C C   A LYS   A 163 ? 0.2036 0.3571 0.1830 0.0210  0.0094  0.0664  163 LYS   A C   
3998 C C   B LYS   A 163 ? 0.2423 0.3463 0.2592 -0.0137 0.0149  -0.0018 163 LYS   A C   
3999 O O   A LYS   A 163 ? 0.1928 0.3717 0.1813 0.0196  0.0035  0.0548  163 LYS   A O   
4000 O O   B LYS   A 163 ? 0.2356 0.3579 0.2486 -0.0100 0.0328  -0.0025 163 LYS   A O   
4001 C CB  A LYS   A 163 ? 0.2513 0.3904 0.2685 0.0288  0.0032  0.0753  163 LYS   A CB  
4002 C CB  B LYS   A 163 ? 0.3022 0.3933 0.3848 -0.0069 0.0137  0.0273  163 LYS   A CB  
4003 C CG  A LYS   A 163 ? 0.2903 0.4116 0.3435 0.0270  0.0048  0.0694  163 LYS   A CG  
4004 C CG  B LYS   A 163 ? 0.3352 0.4151 0.4537 -0.0149 0.0279  0.0287  163 LYS   A CG  
4005 C CD  A LYS   A 163 ? 0.3343 0.4345 0.4227 0.0277  0.0107  0.0576  163 LYS   A CD  
4006 C CD  B LYS   A 163 ? 0.3637 0.4313 0.5207 -0.0169 0.0402  0.0282  163 LYS   A CD  
4007 C CE  A LYS   A 163 ? 0.3659 0.4462 0.4875 0.0272  0.0132  0.0544  163 LYS   A CE  
4008 C CE  B LYS   A 163 ? 0.3865 0.4412 0.5641 -0.0204 0.0542  0.0311  163 LYS   A CE  
4009 N NZ  A LYS   A 163 ? 0.3802 0.4557 0.5198 0.0238  0.0171  0.0541  163 LYS   A NZ  
4010 N NZ  B LYS   A 163 ? 0.3945 0.4462 0.5927 -0.0224 0.0604  0.0330  163 LYS   A NZ  
4037 N N   A LEU   A 164 ? 0.1870 0.3251 0.1406 0.0181  0.0091  0.0557  164 LEU   A N   
4038 N N   B LEU   A 164 ? 0.2250 0.3222 0.2422 -0.0332 0.0128  -0.0063 164 LEU   A N   
4039 C CA  A LEU   A 164 ? 0.1800 0.3055 0.1152 0.0069  0.0217  0.0392  164 LEU   A CA  
4040 C CA  B LEU   A 164 ? 0.2219 0.3003 0.2381 -0.0346 0.0302  -0.0106 164 LEU   A CA  
4041 C C   A LEU   A 164 ? 0.1696 0.3138 0.1326 -0.0090 -0.0023 0.0230  164 LEU   A C   
4042 C C   B LEU   A 164 ? 0.2200 0.3030 0.2524 -0.0357 0.0236  -0.0021 164 LEU   A C   
4043 O O   A LEU   A 164 ? 0.1661 0.3149 0.1157 -0.0236 0.0109  0.0088  164 LEU   A O   
4044 O O   B LEU   A 164 ? 0.2212 0.3069 0.2589 -0.0332 0.0207  -0.0033 164 LEU   A O   
4045 C CB  A LEU   A 164 ? 0.1814 0.2816 0.1287 0.0052  0.0373  0.0425  164 LEU   A CB  
4046 C CB  B LEU   A 164 ? 0.2236 0.2830 0.2136 -0.0414 0.0520  -0.0205 164 LEU   A CB  
4047 C CG  A LEU   A 164 ? 0.1960 0.2587 0.1404 0.0064  0.0264  0.0389  164 LEU   A CG  
4048 C CG  B LEU   A 164 ? 0.2224 0.2749 0.2224 -0.0345 0.0569  -0.0186 164 LEU   A CG  
4049 C CD1 A LEU   A 164 ? 0.1965 0.2528 0.1382 0.0068  0.0113  0.0296  164 LEU   A CD1 
4050 C CD1 B LEU   A 164 ? 0.2192 0.2657 0.2191 -0.0341 0.0500  -0.0192 164 LEU   A CD1 
4051 C CD2 A LEU   A 164 ? 0.2015 0.2478 0.1444 0.0005  0.0327  0.0303  164 LEU   A CD2 
4052 C CD2 B LEU   A 164 ? 0.2280 0.2808 0.2391 -0.0254 0.0523  -0.0171 164 LEU   A CD2 
4075 N N   A VAL   A 165 ? 0.1673 0.3206 0.1354 -0.0114 -0.0020 0.0332  165 VAL   A N   
4076 N N   B VAL   A 165 ? 0.2342 0.3092 0.2587 -0.0337 0.0291  0.0051  165 VAL   A N   
4077 C CA  A VAL   A 165 ? 0.1663 0.3272 0.1275 -0.0232 0.0039  0.0357  165 VAL   A CA  
4078 C CA  B VAL   A 165 ? 0.2445 0.3207 0.2914 -0.0381 0.0224  0.0160  165 VAL   A CA  
4079 C C   A VAL   A 165 ? 0.1677 0.3439 0.1482 -0.0274 -0.0001 0.0318  165 VAL   A C   
4080 C C   B VAL   A 165 ? 0.2508 0.3316 0.3087 -0.0488 -0.0005 0.0082  165 VAL   A C   
4081 O O   A VAL   A 165 ? 0.1530 0.3504 0.1639 -0.0227 0.0081  0.0267  165 VAL   A O   
4082 O O   B VAL   A 165 ? 0.2424 0.3339 0.3095 -0.0455 -0.0091 0.0147  165 VAL   A O   
4083 C CB  A VAL   A 165 ? 0.1890 0.3201 0.1529 -0.0251 0.0197  0.0440  165 VAL   A CB  
4084 C CB  B VAL   A 165 ? 0.2561 0.3211 0.3112 -0.0343 0.0256  0.0332  165 VAL   A CB  
4085 C CG1 A VAL   A 165 ? 0.1846 0.3221 0.1634 -0.0290 0.0402  0.0393  165 VAL   A CG1 
4086 C CG1 B VAL   A 165 ? 0.2571 0.3235 0.3192 -0.0312 0.0277  0.0449  165 VAL   A CG1 
4087 C CG2 A VAL   A 165 ? 0.2061 0.3187 0.1678 -0.0154 0.0084  0.0514  165 VAL   A CG2 
4088 C CG2 B VAL   A 165 ? 0.2611 0.3181 0.3114 -0.0288 0.0299  0.0329  165 VAL   A CG2 
4107 N N   A SER   A 166 ? 0.1640 0.3473 0.1798 -0.0227 0.0097  0.0278  166 SER   A N   
4108 N N   B SER   A 166 ? 0.2704 0.3515 0.3400 -0.0439 -0.0169 0.0018  166 SER   A N   
4109 C CA  A SER   A 166 ? 0.1698 0.3593 0.2114 -0.0257 0.0155  0.0371  166 SER   A CA  
4110 C CA  B SER   A 166 ? 0.2927 0.3688 0.3743 -0.0398 -0.0371 -0.0145 166 SER   A CA  
4111 C C   A SER   A 166 ? 0.1706 0.3629 0.2220 -0.0259 0.0084  0.0343  166 SER   A C   
4112 C C   B SER   A 166 ? 0.3112 0.3799 0.4053 -0.0406 -0.0239 -0.0184 166 SER   A C   
4113 O O   A SER   A 166 ? 0.1831 0.3716 0.2635 -0.0343 0.0021  0.0199  166 SER   A O   
4114 O O   B SER   A 166 ? 0.3052 0.3826 0.4069 -0.0485 -0.0304 -0.0261 166 SER   A O   
4115 C CB  A SER   A 166 ? 0.1920 0.3696 0.2423 -0.0125 0.0190  0.0422  166 SER   A CB  
4116 C CB  B SER   A 166 ? 0.2968 0.3784 0.3750 -0.0304 -0.0673 -0.0210 166 SER   A CB  
4117 O OG  A SER   A 166 ? 0.2148 0.3833 0.2804 -0.0083 0.0285  0.0501  166 SER   A OG  
4118 O OG  B SER   A 166 ? 0.3079 0.3854 0.3793 -0.0287 -0.0802 -0.0173 166 SER   A OG  
4129 N N   A SER   A 167 ? 0.1768 0.3656 0.1996 -0.0127 -0.0016 0.0349  167 SER   A N   
4130 N N   B SER   A 167 ? 0.3311 0.3879 0.4251 -0.0323 -0.0024 -0.0103 167 SER   A N   
4131 C CA  A SER   A 167 ? 0.2017 0.3602 0.1940 -0.0092 -0.0175 0.0279  167 SER   A CA  
4132 C CA  B SER   A 167 ? 0.3532 0.3962 0.4515 -0.0271 0.0143  -0.0030 167 SER   A CA  
4133 C C   A SER   A 167 ? 0.2057 0.3562 0.1989 -0.0018 0.0071  0.0196  167 SER   A C   
4134 C C   B SER   A 167 ? 0.3646 0.4015 0.4649 -0.0241 0.0142  0.0015  167 SER   A C   
4135 O O   A SER   A 167 ? 0.2127 0.3583 0.2137 0.0047  -0.0089 0.0189  167 SER   A O   
4136 O O   B SER   A 167 ? 0.3678 0.4013 0.4794 -0.0246 0.0155  -0.0006 167 SER   A O   
4137 C CB  A SER   A 167 ? 0.2154 0.3609 0.2059 -0.0066 -0.0192 0.0267  167 SER   A CB  
4138 C CB  B SER   A 167 ? 0.3582 0.3963 0.4552 -0.0245 0.0291  -0.0023 167 SER   A CB  
4139 O OG  A SER   A 167 ? 0.2298 0.3656 0.2142 -0.0031 -0.0204 0.0263  167 SER   A OG  
4140 O OG  B SER   A 167 ? 0.3624 0.3984 0.4621 -0.0184 0.0333  -0.0076 167 SER   A OG  
4151 N N   A PHE   A 168 ? 0.2027 0.3468 0.1953 -0.0017 0.0079  0.0285  168 PHE   A N   
4152 N N   B PHE   A 168 ? 0.3702 0.4066 0.4581 -0.0191 0.0120  -0.0006 168 PHE   A N   
4153 C CA  A PHE   A 168 ? 0.2140 0.3388 0.2080 -0.0112 0.0041  0.0313  168 PHE   A CA  
4154 C CA  B PHE   A 168 ? 0.3757 0.4126 0.4495 -0.0156 0.0141  -0.0024 168 PHE   A CA  
4155 C C   A PHE   A 168 ? 0.2413 0.3479 0.2487 -0.0314 0.0092  0.0301  168 PHE   A C   
4156 C C   B PHE   A 168 ? 0.3907 0.4392 0.4865 -0.0087 0.0228  -0.0116 168 PHE   A C   
4157 O O   A PHE   A 168 ? 0.2449 0.3548 0.2991 -0.0467 0.0207  0.0417  168 PHE   A O   
4158 O O   B PHE   A 168 ? 0.3949 0.4415 0.5036 -0.0059 0.0308  -0.0126 168 PHE   A O   
4159 C CB  A PHE   A 168 ? 0.1999 0.3199 0.1813 -0.0108 -0.0115 0.0316  168 PHE   A CB  
4160 C CB  B PHE   A 168 ? 0.3665 0.3941 0.4038 -0.0207 0.0097  0.0060  168 PHE   A CB  
4161 C CG  A PHE   A 168 ? 0.1957 0.3036 0.1592 -0.0105 -0.0132 0.0317  168 PHE   A CG  
4162 C CG  B PHE   A 168 ? 0.3615 0.3769 0.3620 -0.0270 0.0036  0.0103  168 PHE   A CG  
4163 C CD1 A PHE   A 168 ? 0.1915 0.2992 0.1592 -0.0116 -0.0088 0.0409  168 PHE   A CD1 
4164 C CD1 B PHE   A 168 ? 0.3554 0.3707 0.3437 -0.0316 -0.0039 0.0106  168 PHE   A CD1 
4165 C CD2 A PHE   A 168 ? 0.1838 0.2898 0.1366 -0.0105 0.0060  0.0361  168 PHE   A CD2 
4166 C CD2 B PHE   A 168 ? 0.3582 0.3684 0.3383 -0.0301 0.0015  0.0111  168 PHE   A CD2 
4167 C CE1 A PHE   A 168 ? 0.1775 0.2906 0.1693 -0.0190 -0.0165 0.0461  168 PHE   A CE1 
4168 C CE1 B PHE   A 168 ? 0.3513 0.3646 0.3258 -0.0339 -0.0121 0.0114  168 PHE   A CE1 
4169 C CE2 A PHE   A 168 ? 0.1848 0.2795 0.1492 -0.0206 -0.0042 0.0465  168 PHE   A CE2 
4170 C CE2 B PHE   A 168 ? 0.3536 0.3617 0.3244 -0.0329 -0.0025 0.0126  168 PHE   A CE2 
4171 C CZ  A PHE   A 168 ? 0.1815 0.2815 0.1748 -0.0233 -0.0156 0.0459  168 PHE   A CZ  
4172 C CZ  B PHE   A 168 ? 0.3503 0.3606 0.3190 -0.0345 -0.0122 0.0111  168 PHE   A CZ  
4191 N N   A LEU   A 169 ? 0.2734 0.3484 0.2706 -0.0469 -0.0001 0.0173  169 LEU   A N   
4192 N N   B LEU   A 169 ? 0.4006 0.4615 0.4974 -0.0009 0.0195  -0.0215 169 LEU   A N   
4193 C CA  A LEU   A 169 ? 0.3180 0.3607 0.3228 -0.0426 -0.0149 0.0109  169 LEU   A CA  
4194 C CA  B LEU   A 169 ? 0.4084 0.4834 0.4979 0.0045  0.0196  -0.0254 169 LEU   A CA  
4195 C C   A LEU   A 169 ? 0.3260 0.3619 0.3319 -0.0440 -0.0096 0.0256  169 LEU   A C   
4196 C C   B LEU   A 169 ? 0.4168 0.4955 0.5065 0.0104  0.0229  -0.0340 169 LEU   A C   
4197 O O   A LEU   A 169 ? 0.3283 0.3612 0.3331 -0.0453 0.0025  0.0289  169 LEU   A O   
4198 O O   B LEU   A 169 ? 0.4174 0.4979 0.5113 0.0126  0.0288  -0.0339 169 LEU   A O   
4199 C CB  A LEU   A 169 ? 0.3487 0.3707 0.3571 -0.0401 -0.0304 -0.0060 169 LEU   A CB  
4200 C CB  B LEU   A 169 ? 0.4092 0.4937 0.4948 0.0040  0.0148  -0.0199 169 LEU   A CB  
4201 C CG  A LEU   A 169 ? 0.3722 0.3815 0.3914 -0.0396 -0.0471 -0.0288 169 LEU   A CG  
4202 C CG  B LEU   A 169 ? 0.4084 0.5006 0.4881 0.0026  0.0083  -0.0159 169 LEU   A CG  
4203 C CD1 A LEU   A 169 ? 0.3797 0.3855 0.4090 -0.0360 -0.0529 -0.0324 169 LEU   A CD1 
4204 C CD1 B LEU   A 169 ? 0.4103 0.5018 0.4807 0.0020  0.0095  -0.0123 169 LEU   A CD1 
4205 C CD2 A LEU   A 169 ? 0.3789 0.3856 0.3951 -0.0407 -0.0549 -0.0402 169 LEU   A CD2 
4206 C CD2 B LEU   A 169 ? 0.4071 0.5039 0.4915 0.0031  0.0054  -0.0189 169 LEU   A CD2 
4207 O OXT A LEU   A 169 ? 0.3227 0.3641 0.3306 -0.0473 -0.0092 0.0301  169 LEU   A OXT 
4208 O OXT B LEU   A 169 ? 0.4236 0.5031 0.5144 0.0118  0.0205  -0.0365 169 LEU   A OXT 
4231 N N   A SER   B 1   ? 0.3720 0.3347 0.3563 -0.1049 -0.0641 0.0102  1   SER   B N   
4232 N N   B SER   B 1   ? 0.3167 0.2953 0.3367 -0.0676 -0.0430 -0.0052 1   SER   B N   
4233 C CA  A SER   B 1   ? 0.3637 0.3450 0.3625 -0.1097 -0.0719 0.0082  1   SER   B CA  
4234 C CA  B SER   B 1   ? 0.3050 0.3131 0.3427 -0.0746 -0.0460 -0.0140 1   SER   B CA  
4235 C C   A SER   B 1   ? 0.3355 0.3433 0.3453 -0.1214 -0.0841 0.0347  1   SER   B C   
4236 C C   B SER   B 1   ? 0.2735 0.3138 0.3151 -0.0769 -0.0579 -0.0096 1   SER   B C   
4237 O O   A SER   B 1   ? 0.3434 0.3497 0.3307 -0.1129 -0.0870 0.0370  1   SER   B O   
4238 O O   B SER   B 1   ? 0.2788 0.3205 0.3113 -0.0784 -0.0545 -0.0268 1   SER   B O   
4239 C CB  A SER   B 1   ? 0.3756 0.3457 0.3796 -0.1083 -0.0616 -0.0180 1   SER   B CB  
4240 C CB  B SER   B 1   ? 0.3193 0.3160 0.3803 -0.0755 -0.0374 -0.0372 1   SER   B CB  
4241 O OG  A SER   B 1   ? 0.3891 0.3557 0.4176 -0.1073 -0.0479 -0.0323 1   SER   B OG  
4242 O OG  B SER   B 1   ? 0.3354 0.3316 0.4259 -0.0749 -0.0317 -0.0402 1   SER   B OG  
4257 N N   A MET   B 2   ? 0.3138 0.3376 0.3373 -0.1344 -0.0754 0.0769  2   MET   B N   
4258 N N   B MET   B 2   ? 0.2581 0.3133 0.2858 -0.0653 -0.0584 0.0125  2   MET   B N   
4259 C CA  A MET   B 2   ? 0.3017 0.3365 0.3347 -0.1248 -0.0774 0.1013  2   MET   B CA  
4260 C CA  B MET   B 2   ? 0.2465 0.3131 0.2600 -0.0462 -0.0634 0.0346  2   MET   B CA  
4261 C C   A MET   B 2   ? 0.2678 0.3107 0.3016 -0.1121 -0.0927 0.1164  2   MET   B C   
4262 C C   B MET   B 2   ? 0.2272 0.2937 0.2515 -0.0292 -0.0580 0.0609  2   MET   B C   
4263 O O   A MET   B 2   ? 0.2523 0.3003 0.2987 -0.1241 -0.1274 0.1068  2   MET   B O   
4264 O O   B MET   B 2   ? 0.2429 0.3128 0.2709 -0.0111 -0.0577 0.0595  2   MET   B O   
4265 C CB  A MET   B 2   ? 0.3334 0.3731 0.4199 -0.1106 -0.0545 0.0771  2   MET   B CB  
4266 C CB  B MET   B 2   ? 0.2625 0.3379 0.2928 -0.0379 -0.0485 0.0261  2   MET   B CB  
4267 C CG  A MET   B 2   ? 0.3669 0.4063 0.5087 -0.0911 -0.0282 0.0664  2   MET   B CG  
4268 C CG  B MET   B 2   ? 0.2827 0.3593 0.3215 -0.0214 -0.0420 0.0334  2   MET   B CG  
4269 S SD  A MET   B 2   ? 0.4014 0.4500 0.5986 -0.0700 -0.0042 0.0542  2   MET   B SD  
4270 S SD  B MET   B 2   ? 0.3099 0.3915 0.3357 -0.0026 -0.0301 0.0360  2   MET   B SD  
4271 C CE  A MET   B 2   ? 0.4041 0.4490 0.6043 -0.0714 0.0073  0.0578  2   MET   B CE  
4272 C CE  B MET   B 2   ? 0.3114 0.3974 0.3806 -0.0113 -0.0253 0.0382  2   MET   B CE  
4291 N N   A VAL   B 3   ? 0.2346 0.2742 0.2680 -0.1058 -0.0793 0.1388  3   VAL   B N   
4292 N N   B VAL   B 3   ? 0.2007 0.2540 0.2332 -0.0310 -0.0588 0.0692  3   VAL   B N   
4293 C CA  A VAL   B 3   ? 0.2171 0.2508 0.2606 -0.0840 -0.0768 0.1071  3   VAL   B CA  
4294 C CA  B VAL   B 3   ? 0.1908 0.2183 0.2193 -0.0395 -0.0613 0.0506  3   VAL   B CA  
4295 C C   A VAL   B 3   ? 0.2047 0.2356 0.2308 -0.0631 -0.0638 0.0911  3   VAL   B C   
4296 C C   B VAL   B 3   ? 0.1836 0.2008 0.1880 -0.0411 -0.0526 0.0375  3   VAL   B C   
4297 O O   A VAL   B 3   ? 0.1998 0.2406 0.2551 -0.0491 -0.0585 0.1124  3   VAL   B O   
4298 O O   B VAL   B 3   ? 0.1695 0.1739 0.1775 -0.0252 -0.0339 0.0200  3   VAL   B O   
4299 C CB  A VAL   B 3   ? 0.2262 0.2399 0.3028 -0.0780 -0.0701 0.0993  3   VAL   B CB  
4300 C CB  B VAL   B 3   ? 0.2069 0.2162 0.2717 -0.0454 -0.0523 0.0274  3   VAL   B CB  
4301 C CG1 A VAL   B 3   ? 0.2334 0.2303 0.3304 -0.0813 -0.0664 0.0928  3   VAL   B CG1 
4302 C CG1 B VAL   B 3   ? 0.2172 0.2193 0.3032 -0.0511 -0.0563 0.0301  3   VAL   B CG1 
4303 C CG2 A VAL   B 3   ? 0.2328 0.2417 0.3071 -0.0669 -0.0569 0.1157  3   VAL   B CG2 
4304 C CG2 B VAL   B 3   ? 0.2172 0.2173 0.2812 -0.0317 -0.0330 0.0190  3   VAL   B CG2 
4323 N N   . ASN   B 4   ? 0.1948 0.2051 0.1968 -0.0554 -0.0535 0.0605  4   ASN   B N   
4324 C CA  . ASN   B 4   ? 0.2086 0.2147 0.1652 -0.0508 -0.0565 0.0417  4   ASN   B CA  
4325 C C   . ASN   B 4   ? 0.2101 0.2233 0.1635 -0.0596 -0.0464 0.0332  4   ASN   B C   
4326 O O   . ASN   B 4   ? 0.2106 0.2285 0.1867 -0.0550 -0.0478 0.0098  4   ASN   B O   
4327 C CB  . ASN   B 4   ? 0.2087 0.2101 0.1471 -0.0587 -0.0547 0.0317  4   ASN   B CB  
4328 C CG  . ASN   B 4   ? 0.2077 0.2009 0.1364 -0.0532 -0.0619 0.0444  4   ASN   B CG  
4329 O OD1 . ASN   B 4   ? 0.2032 0.1814 0.1546 -0.0441 -0.0462 0.0341  4   ASN   B OD1 
4330 N ND2 . ASN   B 4   ? 0.2327 0.2027 0.1786 -0.0394 -0.0520 0.0499  4   ASN   B ND2 
4338 N N   . SER   B 5   ? 0.2129 0.2350 0.1968 -0.0542 -0.0274 0.0233  5   SER   B N   
4339 C CA  . SER   B 5   ? 0.2266 0.2698 0.2215 -0.0530 -0.0119 0.0258  5   SER   B CA  
4340 C C   . SER   B 5   ? 0.2537 0.2746 0.2663 -0.0696 0.0121  0.0211  5   SER   B C   
4341 O O   . SER   B 5   ? 0.2847 0.2623 0.3410 -0.0493 0.0566  0.0159  5   SER   B O   
4342 C CB  . SER   B 5   ? 0.2464 0.3002 0.2652 -0.0362 0.0016  0.0578  5   SER   B CB  
4343 O OG  . SER   B 5   ? 0.2911 0.3320 0.3386 -0.0230 0.0120  0.0599  5   SER   B OG  
4349 N N   . PHE   B 6   ? 0.2823 0.3069 0.2525 -0.0887 0.0251  0.0413  6   PHE   B N   
4350 C CA  . PHE   B 6   ? 0.3045 0.3262 0.1955 -0.1171 0.0210  0.0068  6   PHE   B CA  
4351 C C   . PHE   B 6   ? 0.3796 0.3802 0.2712 -0.1319 0.0739  -0.0174 6   PHE   B C   
4352 O O   . PHE   B 6   ? 0.3938 0.4298 0.3150 -0.1273 0.0551  -0.0317 6   PHE   B O   
4353 C CB  . PHE   B 6   ? 0.2685 0.3077 0.1735 -0.1045 0.0041  0.0201  6   PHE   B CB  
4354 C CG  . PHE   B 6   ? 0.2329 0.2792 0.1881 -0.0970 -0.0070 0.0328  6   PHE   B CG  
4355 C CD1 . PHE   B 6   ? 0.2299 0.2509 0.1666 -0.0888 -0.0331 0.0277  6   PHE   B CD1 
4356 C CD2 . PHE   B 6   ? 0.2000 0.2748 0.1877 -0.0778 -0.0278 0.0700  6   PHE   B CD2 
4357 C CE1 . PHE   B 6   ? 0.2278 0.2245 0.1774 -0.0655 -0.0387 0.0357  6   PHE   B CE1 
4358 C CE2 . PHE   B 6   ? 0.2015 0.2626 0.2234 -0.0596 -0.0088 0.0710  6   PHE   B CE2 
4359 C CZ  . PHE   B 6   ? 0.2114 0.2366 0.2090 -0.0556 -0.0402 0.0459  6   PHE   B CZ  
4369 N N   A SER   B 7   ? 0.4141 0.3656 0.2903 -0.1472 0.1085  -0.0321 7   SER   B N   
4370 N N   B SER   B 7   ? 0.4114 0.3661 0.2941 -0.1465 0.1037  -0.0335 7   SER   B N   
4371 C CA  A SER   B 7   ? 0.4485 0.3751 0.3484 -0.1401 0.1273  -0.0406 7   SER   B CA  
4372 C CA  B SER   B 7   ? 0.4432 0.3737 0.3509 -0.1404 0.1193  -0.0432 7   SER   B CA  
4373 C C   A SER   B 7   ? 0.4489 0.3589 0.3310 -0.1494 0.1375  -0.0527 7   SER   B C   
4374 C C   B SER   B 7   ? 0.4438 0.3579 0.3353 -0.1485 0.1292  -0.0544 7   SER   B C   
4375 O O   A SER   B 7   ? 0.4586 0.3583 0.3458 -0.1552 0.1437  -0.0512 7   SER   B O   
4376 O O   B SER   B 7   ? 0.4532 0.3574 0.3504 -0.1537 0.1340  -0.0532 7   SER   B O   
4377 C CB  A SER   B 7   ? 0.4680 0.3945 0.4209 -0.1275 0.1373  -0.0341 7   SER   B CB  
4378 C CB  B SER   B 7   ? 0.4610 0.3914 0.4208 -0.1306 0.1265  -0.0383 7   SER   B CB  
4379 O OG  A SER   B 7   ? 0.4816 0.4089 0.4779 -0.1189 0.1387  -0.0233 7   SER   B OG  
4380 O OG  B SER   B 7   ? 0.4737 0.4043 0.4747 -0.1246 0.1257  -0.0287 7   SER   B OG  
4391 N N   A GLY   B 8   ? 0.4510 0.3518 0.3177 -0.1411 0.1369  -0.0640 8   GLY   B N   
4392 N N   B GLY   B 8   ? 0.4459 0.3499 0.3202 -0.1409 0.1303  -0.0651 8   GLY   B N   
4393 C CA  A GLY   B 8   ? 0.4391 0.3358 0.3068 -0.1349 0.1423  -0.0702 8   GLY   B CA  
4394 C CA  B GLY   B 8   ? 0.4357 0.3341 0.3086 -0.1344 0.1374  -0.0702 8   GLY   B CA  
4395 C C   A GLY   B 8   ? 0.4230 0.3128 0.2939 -0.1313 0.1445  -0.0661 8   GLY   B C   
4396 C C   B GLY   B 8   ? 0.4213 0.3115 0.2943 -0.1310 0.1416  -0.0667 8   GLY   B C   
4397 O O   A GLY   B 8   ? 0.4366 0.3234 0.3155 -0.1180 0.1404  -0.0834 8   GLY   B O   
4398 O O   B GLY   B 8   ? 0.4334 0.3197 0.3146 -0.1204 0.1382  -0.0832 8   GLY   B O   
4405 N N   . TYR   B 9   ? 0.4049 0.2871 0.2800 -0.1298 0.1217  -0.0768 9   TYR   B N   
4406 C CA  . TYR   B 9   ? 0.3757 0.2556 0.2308 -0.0935 0.0921  -0.0641 9   TYR   B CA  
4407 C C   . TYR   B 9   ? 0.3657 0.2606 0.2363 -0.0799 0.0602  -0.0643 9   TYR   B C   
4408 O O   . TYR   B 9   ? 0.3671 0.2799 0.2945 -0.0887 0.0544  -0.0547 9   TYR   B O   
4409 C CB  . TYR   B 9   ? 0.3674 0.2160 0.2366 -0.0846 0.0821  -0.0525 9   TYR   B CB  
4410 C CG  . TYR   B 9   ? 0.3548 0.2027 0.2290 -0.0890 0.0608  -0.0601 9   TYR   B CG  
4411 C CD1 . TYR   B 9   ? 0.3572 0.2126 0.2567 -0.0995 0.0665  -0.0556 9   TYR   B CD1 
4412 C CD2 . TYR   B 9   ? 0.3415 0.1858 0.2110 -0.0814 0.0518  -0.0667 9   TYR   B CD2 
4413 C CE1 . TYR   B 9   ? 0.3474 0.2228 0.2349 -0.1033 0.0812  -0.0659 9   TYR   B CE1 
4414 C CE2 . TYR   B 9   ? 0.3398 0.1907 0.2253 -0.0813 0.0622  -0.0449 9   TYR   B CE2 
4415 C CZ  . TYR   B 9   ? 0.3443 0.2128 0.2442 -0.0979 0.0672  -0.0758 9   TYR   B CZ  
4416 O OH  . TYR   B 9   ? 0.3346 0.2299 0.2840 -0.1118 0.0756  -0.0854 9   TYR   B OH  
4427 N N   . LEU   B 10  ? 0.3449 0.2304 0.2040 -0.0850 0.0377  -0.0598 10  LEU   B N   
4428 C CA  . LEU   B 10  ? 0.3474 0.2178 0.1980 -0.1076 -0.0052 -0.0337 10  LEU   B CA  
4429 C C   . LEU   B 10  ? 0.3333 0.2236 0.1871 -0.1051 -0.0237 -0.0189 10  LEU   B C   
4430 O O   . LEU   B 10  ? 0.3182 0.2247 0.1929 -0.0903 -0.0193 -0.0102 10  LEU   B O   
4431 C CB  . LEU   B 10  ? 0.3721 0.2238 0.2240 -0.1110 -0.0272 -0.0091 10  LEU   B CB  
4432 C CG  . LEU   B 10  ? 0.3927 0.2362 0.2483 -0.1047 -0.0581 0.0113  10  LEU   B CG  
4433 C CD1 . LEU   B 10  ? 0.4062 0.2418 0.2792 -0.1005 -0.0526 0.0025  10  LEU   B CD1 
4434 C CD2 . LEU   B 10  ? 0.3943 0.2424 0.2640 -0.1070 -0.0529 0.0414  10  LEU   B CD2 
4446 N N   . LYS   B 11  ? 0.3454 0.2540 0.2028 -0.0972 -0.0353 -0.0192 11  LYS   B N   
4447 C CA  . LYS   B 11  ? 0.3710 0.2924 0.2650 -0.0844 -0.0430 -0.0241 11  LYS   B CA  
4448 C C   . LYS   B 11  ? 0.3408 0.2592 0.2761 -0.1029 -0.0389 -0.0337 11  LYS   B C   
4449 O O   . LYS   B 11  ? 0.3543 0.2874 0.3117 -0.1218 -0.0463 -0.0654 11  LYS   B O   
4450 C CB  . LYS   B 11  ? 0.4185 0.3531 0.3479 -0.0495 -0.0464 -0.0255 11  LYS   B CB  
4451 C CG  . LYS   B 11  ? 0.4591 0.3950 0.4492 -0.0298 -0.0482 -0.0307 11  LYS   B CG  
4452 C CD  . LYS   B 11  ? 0.4896 0.4234 0.5361 -0.0167 -0.0449 -0.0374 11  LYS   B CD  
4453 C CE  . LYS   B 11  ? 0.5090 0.4428 0.6042 -0.0148 -0.0456 -0.0481 11  LYS   B CE  
4454 N NZ  . LYS   B 11  ? 0.5215 0.4546 0.6404 -0.0146 -0.0454 -0.0512 11  LYS   B NZ  
4468 N N   . LEU   B 12  ? 0.2993 0.2317 0.2724 -0.0900 -0.0492 -0.0365 12  LEU   B N   
4469 C CA  . LEU   B 12  ? 0.2760 0.2021 0.2695 -0.0795 -0.0372 -0.0339 12  LEU   B CA  
4470 C C   . LEU   B 12  ? 0.2584 0.2085 0.2860 -0.0808 -0.0586 -0.0336 12  LEU   B C   
4471 O O   . LEU   B 12  ? 0.2561 0.2098 0.3275 -0.0771 -0.0712 -0.0361 12  LEU   B O   
4472 C CB  . LEU   B 12  ? 0.2731 0.1807 0.2747 -0.0610 -0.0280 -0.0209 12  LEU   B CB  
4473 C CG  . LEU   B 12  ? 0.2635 0.1812 0.2739 -0.0530 -0.0190 -0.0202 12  LEU   B CG  
4474 C CD1 . LEU   B 12  ? 0.2726 0.1914 0.2673 -0.0376 -0.0215 -0.0026 12  LEU   B CD1 
4475 C CD2 . LEU   B 12  ? 0.2681 0.1902 0.2878 -0.0547 -0.0092 -0.0334 12  LEU   B CD2 
4487 N N   . THR   B 13  ? 0.2498 0.2090 0.3008 -0.0802 -0.0574 -0.0413 13  THR   B N   
4488 C CA  . THR   B 13  ? 0.2507 0.2203 0.2763 -0.0810 -0.0873 -0.0203 13  THR   B CA  
4489 C C   . THR   B 13  ? 0.2908 0.2386 0.3007 -0.0884 -0.1013 -0.0121 13  THR   B C   
4490 O O   . THR   B 13  ? 0.3177 0.2453 0.3236 -0.0799 -0.0750 -0.0170 13  THR   B O   
4491 C CB  . THR   B 13  ? 0.2310 0.2297 0.2739 -0.0699 -0.0839 -0.0054 13  THR   B CB  
4492 O OG1 . THR   B 13  ? 0.2099 0.2101 0.2818 -0.0653 -0.0488 -0.0140 13  THR   B OG1 
4493 C CG2 . THR   B 13  ? 0.2409 0.2401 0.2800 -0.0667 -0.0699 0.0166  13  THR   B CG2 
4501 N N   A ASP   B 14  ? 0.3012 0.2580 0.3076 -0.0947 -0.1235 -0.0028 14  ASP   B N   
4502 N N   B ASP   B 14  ? 0.3025 0.2570 0.3044 -0.0900 -0.1186 0.0024  14  ASP   B N   
4503 C CA  A ASP   B 14  ? 0.3086 0.2722 0.3325 -0.0908 -0.1262 0.0193  14  ASP   B CA  
4504 C CA  B ASP   B 14  ? 0.3110 0.2707 0.3231 -0.0831 -0.1192 0.0273  14  ASP   B CA  
4505 C C   A ASP   B 14  ? 0.3008 0.2495 0.2926 -0.0954 -0.1191 0.0256  14  ASP   B C   
4506 C C   B ASP   B 14  ? 0.3004 0.2509 0.2854 -0.0896 -0.1226 0.0277  14  ASP   B C   
4507 O O   A ASP   B 14  ? 0.3332 0.2633 0.3081 -0.0881 -0.0982 0.0400  14  ASP   B O   
4508 O O   B ASP   B 14  ? 0.3313 0.2625 0.2954 -0.0821 -0.1134 0.0407  14  ASP   B O   
4509 C CB  A ASP   B 14  ? 0.3208 0.3101 0.4134 -0.0860 -0.1354 0.0189  14  ASP   B CB  
4510 C CB  B ASP   B 14  ? 0.3277 0.3059 0.3959 -0.0722 -0.1141 0.0371  14  ASP   B CB  
4511 C CG  A ASP   B 14  ? 0.3416 0.3556 0.5012 -0.0751 -0.1309 0.0042  14  ASP   B CG  
4512 C CG  B ASP   B 14  ? 0.3507 0.3486 0.4760 -0.0561 -0.0993 0.0304  14  ASP   B CG  
4513 O OD1 A ASP   B 14  ? 0.3484 0.3571 0.5204 -0.0828 -0.1352 -0.0073 14  ASP   B OD1 
4514 O OD1 B ASP   B 14  ? 0.3628 0.3585 0.4925 -0.0515 -0.0909 0.0305  14  ASP   B OD1 
4515 O OD2 A ASP   B 14  ? 0.3460 0.3677 0.5451 -0.0708 -0.1280 0.0021  14  ASP   B OD2 
4516 O OD2 B ASP   B 14  ? 0.3548 0.3542 0.5145 -0.0551 -0.0970 0.0281  14  ASP   B OD2 
4525 N N   . ASN   B 15  ? 0.2679 0.2207 0.2651 -0.0789 -0.1229 0.0355  15  ASN   B N   
4526 C CA  . ASN   B 15  ? 0.2235 0.1925 0.2418 -0.0516 -0.0903 0.0204  15  ASN   B CA  
4527 C C   . ASN   B 15  ? 0.2082 0.1758 0.2272 -0.0364 -0.0695 0.0176  15  ASN   B C   
4528 O O   . ASN   B 15  ? 0.1920 0.1606 0.2440 -0.0290 -0.0637 -0.0030 15  ASN   B O   
4529 C CB  . ASN   B 15  ? 0.2202 0.1884 0.2649 -0.0273 -0.0873 0.0195  15  ASN   B CB  
4530 C CG  . ASN   B 15  ? 0.1934 0.1766 0.2703 -0.0306 -0.0587 0.0428  15  ASN   B CG  
4531 O OD1 . ASN   B 15  ? 0.2048 0.2225 0.3201 -0.0688 -0.0470 0.0290  15  ASN   B OD1 
4532 N ND2 . ASN   B 15  ? 0.1852 0.1733 0.2583 -0.0111 -0.0065 0.0057  15  ASN   B ND2 
4540 N N   . VAL   B 16  ? 0.2097 0.1602 0.2346 -0.0452 -0.0798 0.0254  16  VAL   B N   
4541 C CA  . VAL   B 16  ? 0.2148 0.1541 0.2181 -0.0440 -0.0635 -0.0116 16  VAL   B CA  
4542 C C   . VAL   B 16  ? 0.2122 0.1673 0.2082 -0.0523 -0.0539 -0.0025 16  VAL   B C   
4543 O O   . VAL   B 16  ? 0.1997 0.1781 0.2294 -0.0392 -0.0459 -0.0137 16  VAL   B O   
4544 C CB  . VAL   B 16  ? 0.2142 0.1626 0.2093 -0.0254 -0.0468 -0.0076 16  VAL   B CB  
4545 C CG1 . VAL   B 16  ? 0.2245 0.1527 0.2212 -0.0258 -0.0399 -0.0150 16  VAL   B CG1 
4546 C CG2 . VAL   B 16  ? 0.2194 0.1618 0.2430 -0.0183 -0.0304 -0.0182 16  VAL   B CG2 
4556 N N   . TYR   B 17  ? 0.2222 0.1904 0.1975 -0.0593 -0.0468 -0.0013 17  TYR   B N   
4557 C CA  . TYR   B 17  ? 0.2315 0.2160 0.1612 -0.0674 -0.0602 0.0193  17  TYR   B CA  
4558 C C   . TYR   B 17  ? 0.2189 0.1853 0.1554 -0.0618 -0.0437 -0.0017 17  TYR   B C   
4559 O O   . TYR   B 17  ? 0.2075 0.1838 0.1709 -0.0476 -0.0328 -0.0212 17  TYR   B O   
4560 C CB  . TYR   B 17  ? 0.2725 0.2843 0.2194 -0.0662 -0.0568 0.0734  17  TYR   B CB  
4561 C CG  . TYR   B 17  ? 0.3062 0.3622 0.2765 -0.0630 -0.0782 0.1116  17  TYR   B CG  
4562 C CD1 . TYR   B 17  ? 0.3233 0.3950 0.3202 -0.0596 -0.0999 0.1264  17  TYR   B CD1 
4563 C CD2 . TYR   B 17  ? 0.3316 0.4016 0.3121 -0.0512 -0.1002 0.1147  17  TYR   B CD2 
4564 C CE1 . TYR   B 17  ? 0.3429 0.4291 0.3442 -0.0478 -0.1173 0.1256  17  TYR   B CE1 
4565 C CE2 . TYR   B 17  ? 0.3534 0.4352 0.3391 -0.0344 -0.1198 0.1254  17  TYR   B CE2 
4566 C CZ  . TYR   B 17  ? 0.3640 0.4562 0.3634 -0.0330 -0.1254 0.1282  17  TYR   B CZ  
4567 O OH  . TYR   B 17  ? 0.3805 0.4691 0.3873 -0.0208 -0.1339 0.1314  17  TYR   B OH  
4577 N N   . ILE   B 18  ? 0.2440 0.1825 0.1642 -0.0660 -0.0195 -0.0038 18  ILE   B N   
4578 C CA  . ILE   B 18  ? 0.2468 0.1752 0.1676 -0.0638 -0.0012 -0.0111 18  ILE   B CA  
4579 C C   . ILE   B 18  ? 0.2566 0.1852 0.1604 -0.0753 0.0049  -0.0345 18  ILE   B C   
4580 O O   . ILE   B 18  ? 0.2744 0.1879 0.1897 -0.0666 0.0079  -0.0348 18  ILE   B O   
4581 C CB  . ILE   B 18  ? 0.2419 0.1703 0.1727 -0.0606 -0.0012 -0.0088 18  ILE   B CB  
4582 C CG1 . ILE   B 18  ? 0.2484 0.1709 0.1901 -0.0567 -0.0087 -0.0113 18  ILE   B CG1 
4583 C CG2 . ILE   B 18  ? 0.2505 0.1843 0.1798 -0.0659 -0.0178 -0.0044 18  ILE   B CG2 
4584 C CD1 . ILE   B 18  ? 0.2442 0.2119 0.2275 -0.0573 -0.0313 0.0310  18  ILE   B CD1 
4596 N N   . LYS   B 19  ? 0.2568 0.1832 0.1800 -0.0497 0.0497  -0.0403 19  LYS   B N   
4597 C CA  . LYS   B 19  ? 0.2538 0.1907 0.2259 -0.0570 0.0453  -0.0564 19  LYS   B CA  
4598 C C   . LYS   B 19  ? 0.2301 0.1793 0.2292 -0.0442 0.0391  -0.0833 19  LYS   B C   
4599 O O   . LYS   B 19  ? 0.2211 0.1798 0.2360 -0.0417 0.0327  -0.0544 19  LYS   B O   
4600 C CB  . LYS   B 19  ? 0.2876 0.2093 0.2451 -0.0704 0.0706  -0.0538 19  LYS   B CB  
4601 C CG  . LYS   B 19  ? 0.3240 0.2351 0.2861 -0.0827 0.0912  -0.0489 19  LYS   B CG  
4602 C CD  . LYS   B 19  ? 0.3602 0.2654 0.2969 -0.0810 0.1112  -0.0481 19  LYS   B CD  
4603 C CE  . LYS   B 19  ? 0.3981 0.2830 0.3378 -0.0880 0.0992  -0.0488 19  LYS   B CE  
4604 N NZ  . LYS   B 19  ? 0.4249 0.2974 0.3505 -0.0859 0.1004  -0.0470 19  LYS   B NZ  
4618 N N   . ASN   B 20  ? 0.2402 0.2032 0.2771 -0.0444 0.0484  -0.0892 20  ASN   B N   
4619 C CA  . ASN   B 20  ? 0.2302 0.2135 0.3081 -0.0400 0.0691  -0.0994 20  ASN   B CA  
4620 C C   . ASN   B 20  ? 0.2223 0.2397 0.2990 -0.0408 0.0822  -0.1121 20  ASN   B C   
4621 O O   . ASN   B 20  ? 0.2545 0.2836 0.3150 -0.0513 0.0782  -0.1124 20  ASN   B O   
4622 C CB  . ASN   B 20  ? 0.2636 0.2204 0.3481 -0.0136 0.0484  -0.0951 20  ASN   B CB  
4623 C CG  . ASN   B 20  ? 0.3004 0.2219 0.3617 0.0255  0.0473  -0.1175 20  ASN   B CG  
4624 O OD1 . ASN   B 20  ? 0.3453 0.2584 0.3815 0.0373  0.0396  -0.1234 20  ASN   B OD1 
4625 N ND2 . ASN   B 20  ? 0.2894 0.2122 0.3627 0.0407  0.0225  -0.1021 20  ASN   B ND2 
4632 N N   . ALA   B 21  ? 0.2303 0.2148 0.2995 -0.0454 0.0790  -0.0929 21  ALA   B N   
4633 C CA  . ALA   B 21  ? 0.2350 0.2101 0.3119 -0.0385 0.0726  -0.0749 21  ALA   B CA  
4634 C C   . ALA   B 21  ? 0.2329 0.1871 0.2733 -0.0326 0.0634  -0.0549 21  ALA   B C   
4635 O O   . ALA   B 21  ? 0.2365 0.1790 0.2587 -0.0438 0.0492  -0.0526 21  ALA   B O   
4636 C CB  . ALA   B 21  ? 0.2561 0.2363 0.3334 -0.0601 0.0766  -0.0449 21  ALA   B CB  
4642 N N   . ASP   B 22  ? 0.2203 0.1790 0.2717 -0.0270 0.0375  -0.0440 22  ASP   B N   
4643 C CA  . ASP   B 22  ? 0.2075 0.1683 0.2579 -0.0134 0.0167  -0.0174 22  ASP   B CA  
4644 C C   . ASP   B 22  ? 0.2032 0.1592 0.2144 -0.0294 0.0194  -0.0125 22  ASP   B C   
4645 O O   . ASP   B 22  ? 0.2028 0.1688 0.2241 -0.0160 0.0245  -0.0139 22  ASP   B O   
4646 C CB  . ASP   B 22  ? 0.2035 0.1759 0.3042 -0.0024 0.0302  -0.0007 22  ASP   B CB  
4647 C CG  . ASP   B 22  ? 0.2025 0.1942 0.3595 0.0113  0.0201  0.0080  22  ASP   B CG  
4648 O OD1 . ASP   B 22  ? 0.2177 0.1832 0.3640 0.0172  -0.0154 0.0187  22  ASP   B OD1 
4649 O OD2 . ASP   B 22  ? 0.2208 0.2145 0.4329 0.0176  -0.0020 -0.0241 22  ASP   B OD2 
4654 N N   . ILE   B 23  ? 0.1976 0.1655 0.1940 -0.0095 -0.0090 0.0174  23  ILE   B N   
4655 C CA  . ILE   B 23  ? 0.1800 0.1693 0.1677 -0.0118 -0.0072 0.0088  23  ILE   B CA  
4656 C C   . ILE   B 23  ? 0.1744 0.1759 0.1571 -0.0135 -0.0137 0.0048  23  ILE   B C   
4657 O O   . ILE   B 23  ? 0.1713 0.1634 0.1497 -0.0074 -0.0087 0.0047  23  ILE   B O   
4658 C CB  . ILE   B 23  ? 0.1739 0.1726 0.1994 -0.0290 -0.0027 0.0195  23  ILE   B CB  
4659 C CG1 . ILE   B 23  ? 0.1778 0.1758 0.2022 -0.0148 0.0120  0.0301  23  ILE   B CG1 
4660 C CG2 . ILE   B 23  ? 0.1880 0.1877 0.2048 -0.0205 -0.0076 0.0242  23  ILE   B CG2 
4661 C CD1 . ILE   B 23  ? 0.2003 0.1839 0.2377 -0.0171 0.0097  0.0366  23  ILE   B CD1 
4673 N N   . VAL   B 24  ? 0.1771 0.1686 0.1685 -0.0161 -0.0107 0.0066  24  VAL   B N   
4674 C CA  . VAL   B 24  ? 0.1824 0.1772 0.1815 -0.0174 -0.0166 0.0032  24  VAL   B CA  
4675 C C   . VAL   B 24  ? 0.1835 0.1802 0.1822 -0.0145 -0.0121 0.0107  24  VAL   B C   
4676 O O   . VAL   B 24  ? 0.1790 0.1953 0.2059 -0.0225 0.0018  0.0206  24  VAL   B O   
4677 C CB  . VAL   B 24  ? 0.1854 0.1834 0.1793 -0.0073 -0.0263 0.0021  24  VAL   B CB  
4678 C CG1 . VAL   B 24  ? 0.1865 0.1926 0.2239 -0.0094 -0.0247 0.0012  24  VAL   B CG1 
4679 C CG2 . VAL   B 24  ? 0.1906 0.2184 0.1837 0.0022  -0.0228 0.0048  24  VAL   B CG2 
4689 N N   . GLU   B 25  ? 0.1963 0.1892 0.1902 -0.0150 0.0029  0.0006  25  GLU   B N   
4690 C CA  . GLU   B 25  ? 0.2176 0.2082 0.2237 -0.0137 0.0127  -0.0027 25  GLU   B CA  
4691 C C   . GLU   B 25  ? 0.2223 0.1967 0.1917 -0.0298 0.0118  -0.0046 25  GLU   B C   
4692 O O   . GLU   B 25  ? 0.2142 0.2169 0.2169 -0.0289 0.0259  -0.0009 25  GLU   B O   
4693 C CB  . GLU   B 25  ? 0.2620 0.2707 0.3302 0.0196  0.0237  -0.0021 25  GLU   B CB  
4694 C CG  . GLU   B 25  ? 0.3151 0.3572 0.4592 0.0332  0.0310  -0.0043 25  GLU   B CG  
4695 C CD  . GLU   B 25  ? 0.3522 0.4456 0.5631 0.0337  0.0389  -0.0087 25  GLU   B CD  
4696 O OE1 . GLU   B 25  ? 0.3915 0.4658 0.5993 0.0409  0.0466  -0.0100 25  GLU   B OE1 
4697 O OE2 . GLU   B 25  ? 0.3820 0.4639 0.5935 0.0331  0.0368  -0.0143 25  GLU   B OE2 
4704 N N   A GLU   B 26  ? 0.2193 0.1776 0.1620 -0.0406 0.0181  0.0002  26  GLU   B N   
4705 N N   B GLU   B 26  ? 0.2159 0.1795 0.1772 -0.0413 0.0155  0.0105  26  GLU   B N   
4706 C CA  A GLU   B 26  ? 0.2251 0.1922 0.1772 -0.0418 0.0114  0.0114  26  GLU   B CA  
4707 C CA  B GLU   B 26  ? 0.2162 0.1933 0.2069 -0.0422 0.0079  0.0247  26  GLU   B CA  
4708 C C   A GLU   B 26  ? 0.2038 0.1934 0.1667 -0.0292 -0.0006 0.0173  26  GLU   B C   
4709 C C   B GLU   B 26  ? 0.1962 0.1945 0.1792 -0.0279 0.0028  0.0256  26  GLU   B C   
4710 O O   A GLU   B 26  ? 0.2191 0.2134 0.1805 -0.0336 0.0006  0.0132  26  GLU   B O   
4711 O O   B GLU   B 26  ? 0.2052 0.2150 0.1864 -0.0283 0.0109  0.0254  26  GLU   B O   
4712 C CB  A GLU   B 26  ? 0.2531 0.1994 0.1728 -0.0424 0.0384  0.0181  26  GLU   B CB  
4713 C CB  B GLU   B 26  ? 0.2364 0.2021 0.2488 -0.0454 0.0194  0.0393  26  GLU   B CB  
4714 C CG  A GLU   B 26  ? 0.2916 0.2229 0.2193 -0.0421 0.0480  -0.0005 26  GLU   B CG  
4715 C CG  B GLU   B 26  ? 0.2643 0.2306 0.3331 -0.0443 0.0187  0.0277  26  GLU   B CG  
4716 C CD  A GLU   B 26  ? 0.3088 0.2256 0.2080 -0.0610 0.0635  -0.0216 26  GLU   B CD  
4717 C CD  B GLU   B 26  ? 0.2637 0.2278 0.3563 -0.0626 0.0172  0.0285  26  GLU   B CD  
4718 O OE1 A GLU   B 26  ? 0.3237 0.2125 0.1965 -0.0701 0.1041  -0.0319 26  GLU   B OE1 
4719 O OE1 B GLU   B 26  ? 0.2589 0.2328 0.3997 -0.0675 0.0515  0.0087  26  GLU   B OE1 
4720 O OE2 A GLU   B 26  ? 0.3123 0.2405 0.2364 -0.0734 0.0663  0.0097  26  GLU   B OE2 
4721 O OE2 B GLU   B 26  ? 0.2656 0.2276 0.3605 -0.0670 0.0111  0.0193  26  GLU   B OE2 
4734 N N   . ALA   B 27  ? 0.1767 0.1821 0.1752 -0.0254 -0.0014 0.0244  27  ALA   B N   
4735 C CA  . ALA   B 27  ? 0.1713 0.1791 0.1610 -0.0081 -0.0004 0.0303  27  ALA   B CA  
4736 C C   . ALA   B 27  ? 0.1828 0.1907 0.1866 -0.0063 0.0058  0.0300  27  ALA   B C   
4737 O O   . ALA   B 27  ? 0.1690 0.1966 0.2148 -0.0039 -0.0037 0.0433  27  ALA   B O   
4738 C CB  . ALA   B 27  ? 0.1822 0.1683 0.1767 -0.0074 0.0053  0.0295  27  ALA   B CB  
4745 N N   . LYS   B 28  ? 0.1782 0.2040 0.2384 -0.0143 0.0178  0.0502  28  LYS   B N   
4746 C CA  . LYS   B 28  ? 0.1866 0.2344 0.2638 -0.0039 0.0602  0.0896  28  LYS   B CA  
4747 C C   . LYS   B 28  ? 0.2177 0.2532 0.2387 0.0001  0.0645  0.0796  28  LYS   B C   
4748 O O   . LYS   B 28  ? 0.2311 0.2596 0.2728 -0.0192 0.0583  0.0626  28  LYS   B O   
4749 C CB  . LYS   B 28  ? 0.2130 0.2791 0.3369 0.0120  0.0781  0.1217  28  LYS   B CB  
4750 C CG  . LYS   B 28  ? 0.2375 0.3366 0.3984 0.0300  0.0726  0.1422  28  LYS   B CG  
4751 C CD  . LYS   B 28  ? 0.3116 0.4102 0.4748 0.0375  0.0942  0.1490  28  LYS   B CD  
4752 C CE  . LYS   B 28  ? 0.3765 0.4694 0.5409 0.0475  0.0869  0.1558  28  LYS   B CE  
4753 N NZ  . LYS   B 28  ? 0.4227 0.4900 0.5705 0.0549  0.0818  0.1636  28  LYS   B NZ  
4767 N N   A LYS   B 29  ? 0.2377 0.2749 0.2468 0.0069  0.0481  0.0610  29  LYS   B N   
4768 N N   B LYS   B 29  ? 0.2413 0.2716 0.2493 0.0102  0.0504  0.0602  29  LYS   B N   
4769 C CA  A LYS   B 29  ? 0.2739 0.2967 0.2717 -0.0021 0.0285  0.0565  29  LYS   B CA  
4770 C CA  B LYS   B 29  ? 0.2780 0.2897 0.2730 0.0052  0.0338  0.0546  29  LYS   B CA  
4771 C C   A LYS   B 29  ? 0.2619 0.2905 0.2357 -0.0131 0.0142  0.0604  29  LYS   B C   
4772 C C   B LYS   B 29  ? 0.2682 0.2785 0.2361 -0.0027 0.0247  0.0563  29  LYS   B C   
4773 O O   A LYS   B 29  ? 0.2748 0.3175 0.2547 -0.0123 0.0099  0.0596  29  LYS   B O   
4774 O O   B LYS   B 29  ? 0.2876 0.2882 0.2438 0.0100  0.0307  0.0535  29  LYS   B O   
4775 C CB  A LYS   B 29  ? 0.3225 0.3297 0.3509 0.0007  0.0229  0.0362  29  LYS   B CB  
4776 C CB  B LYS   B 29  ? 0.3255 0.3235 0.3503 0.0081  0.0263  0.0350  29  LYS   B CB  
4777 C CG  A LYS   B 29  ? 0.3635 0.3606 0.4419 -0.0008 0.0255  0.0283  29  LYS   B CG  
4778 C CG  B LYS   B 29  ? 0.3653 0.3552 0.4393 0.0075  0.0256  0.0263  29  LYS   B CG  
4779 C CD  A LYS   B 29  ? 0.3924 0.3800 0.5056 -0.0063 0.0373  0.0197  29  LYS   B CD  
4780 C CD  B LYS   B 29  ? 0.3930 0.3762 0.5031 0.0027  0.0346  0.0169  29  LYS   B CD  
4781 C CE  A LYS   B 29  ? 0.4168 0.3925 0.5454 -0.0109 0.0513  0.0100  29  LYS   B CE  
4782 C CE  B LYS   B 29  ? 0.4171 0.3893 0.5447 -0.0013 0.0458  0.0068  29  LYS   B CE  
4783 N NZ  A LYS   B 29  ? 0.4270 0.4012 0.5688 -0.0123 0.0576  0.0042  29  LYS   B NZ  
4784 N NZ  B LYS   B 29  ? 0.4273 0.3979 0.5679 -0.0033 0.0505  0.0003  29  LYS   B NZ  
4811 N N   . VAL   B 30  ? 0.2366 0.2634 0.2232 -0.0263 0.0056  0.0518  30  VAL   B N   
4812 C CA  . VAL   B 30  ? 0.2279 0.2518 0.2444 -0.0256 -0.0291 0.0578  30  VAL   B CA  
4813 C C   . VAL   B 30  ? 0.1922 0.2459 0.2124 -0.0254 -0.0333 0.0642  30  VAL   B C   
4814 O O   . VAL   B 30  ? 0.1934 0.2662 0.2133 -0.0247 -0.0257 0.0727  30  VAL   B O   
4815 C CB  . VAL   B 30  ? 0.2475 0.2435 0.3369 -0.0457 -0.0442 0.0813  30  VAL   B CB  
4816 C CG1 . VAL   B 30  ? 0.2790 0.2677 0.3756 -0.0423 -0.0139 0.0600  30  VAL   B CG1 
4817 C CG2 . VAL   B 30  ? 0.2628 0.2388 0.3562 -0.0587 -0.0577 0.0569  30  VAL   B CG2 
4828 N N   A LYS   B 31  ? 0.1845 0.2229 0.2257 -0.0371 -0.0178 0.0668  31  LYS   B N   
4829 N N   B LYS   B 31  ? 0.1878 0.2248 0.2236 -0.0355 -0.0213 0.0597  31  LYS   B N   
4830 C CA  A LYS   B 31  ? 0.1796 0.2266 0.2528 -0.0388 -0.0126 0.0731  31  LYS   B CA  
4831 C CA  B LYS   B 31  ? 0.1860 0.2272 0.2469 -0.0368 -0.0186 0.0601  31  LYS   B CA  
4832 C C   A LYS   B 31  ? 0.1769 0.1930 0.2166 -0.0353 -0.0271 0.0584  31  LYS   B C   
4833 C C   B LYS   B 31  ? 0.1809 0.1932 0.2116 -0.0352 -0.0311 0.0467  31  LYS   B C   
4834 O O   A LYS   B 31  ? 0.1675 0.2016 0.2240 -0.0298 -0.0204 0.0635  31  LYS   B O   
4835 O O   B LYS   B 31  ? 0.1736 0.1995 0.2161 -0.0325 -0.0277 0.0432  31  LYS   B O   
4836 C CB  A LYS   B 31  ? 0.1935 0.2761 0.3042 -0.0327 0.0117  0.0880  31  LYS   B CB  
4837 C CB  B LYS   B 31  ? 0.2031 0.2735 0.2949 -0.0298 -0.0005 0.0672  31  LYS   B CB  
4838 C CG  A LYS   B 31  ? 0.2192 0.3181 0.3497 -0.0389 0.0235  0.1028  31  LYS   B CG  
4839 C CG  B LYS   B 31  ? 0.2288 0.3130 0.3396 -0.0346 0.0065  0.0744  31  LYS   B CG  
4840 C CD  A LYS   B 31  ? 0.2475 0.3687 0.4083 -0.0342 0.0100  0.0974  31  LYS   B CD  
4841 C CD  B LYS   B 31  ? 0.2546 0.3581 0.3961 -0.0314 -0.0068 0.0679  31  LYS   B CD  
4842 C CE  A LYS   B 31  ? 0.2743 0.4014 0.4587 -0.0256 -0.0025 0.0909  31  LYS   B CE  
4843 C CE  B LYS   B 31  ? 0.2778 0.3841 0.4455 -0.0251 -0.0174 0.0626  31  LYS   B CE  
4844 N NZ  A LYS   B 31  ? 0.2844 0.4209 0.4744 -0.0130 -0.0145 0.0867  31  LYS   B NZ  
4845 N NZ  B LYS   B 31  ? 0.2839 0.4026 0.4598 -0.0131 -0.0313 0.0589  31  LYS   B NZ  
4872 N N   . PRO   B 32  ? 0.1805 0.1703 0.1865 -0.0367 -0.0400 0.0428  32  PRO   B N   
4873 C CA  . PRO   B 32  ? 0.1906 0.1720 0.1539 -0.0392 -0.0377 0.0253  32  PRO   B CA  
4874 C C   . PRO   B 32  ? 0.1977 0.1582 0.1622 -0.0385 -0.0515 0.0295  32  PRO   B C   
4875 O O   . PRO   B 32  ? 0.2093 0.1511 0.2097 -0.0371 -0.0724 0.0219  32  PRO   B O   
4876 C CB  . PRO   B 32  ? 0.2070 0.1743 0.1571 -0.0390 -0.0257 0.0097  32  PRO   B CB  
4877 C CG  . PRO   B 32  ? 0.2307 0.1546 0.1492 -0.0280 -0.0527 0.0165  32  PRO   B CG  
4878 C CD  . PRO   B 32  ? 0.2130 0.1520 0.1756 -0.0250 -0.0440 0.0175  32  PRO   B CD  
4886 N N   . THR   B 33  ? 0.2061 0.1485 0.1564 -0.0376 -0.0391 0.0090  33  THR   B N   
4887 C CA  . THR   B 33  ? 0.2135 0.1531 0.1379 -0.0386 -0.0394 0.0299  33  THR   B CA  
4888 C C   . THR   B 33  ? 0.2168 0.1496 0.1235 -0.0361 -0.0449 0.0097  33  THR   B C   
4889 O O   . THR   B 33  ? 0.2328 0.1622 0.1459 -0.0535 -0.0480 0.0149  33  THR   B O   
4890 C CB  . THR   B 33  ? 0.2264 0.1655 0.1471 -0.0178 -0.0579 0.0260  33  THR   B CB  
4891 O OG1 . THR   B 33  ? 0.2073 0.1669 0.1747 -0.0242 -0.0573 0.0301  33  THR   B OG1 
4892 C CG2 . THR   B 33  ? 0.2557 0.1795 0.1830 -0.0140 -0.0343 0.0304  33  THR   B CG2 
4900 N N   . VAL   B 34  ? 0.1998 0.1396 0.1368 -0.0385 -0.0325 0.0083  34  VAL   B N   
4901 C CA  . VAL   B 34  ? 0.1879 0.1518 0.1239 -0.0262 -0.0402 0.0037  34  VAL   B CA  
4902 C C   . VAL   B 34  ? 0.1713 0.1456 0.1168 -0.0303 -0.0310 -0.0026 34  VAL   B C   
4903 O O   . VAL   B 34  ? 0.1882 0.1496 0.1329 -0.0296 -0.0319 0.0136  34  VAL   B O   
4904 C CB  . VAL   B 34  ? 0.1978 0.1690 0.1529 -0.0104 -0.0222 0.0057  34  VAL   B CB  
4905 C CG1 . VAL   B 34  ? 0.1814 0.1822 0.1853 -0.0110 0.0053  -0.0127 34  VAL   B CG1 
4906 C CG2 . VAL   B 34  ? 0.1941 0.1796 0.1876 -0.0196 -0.0281 0.0093  34  VAL   B CG2 
4916 N N   . VAL   B 35  ? 0.1732 0.1333 0.1031 -0.0343 -0.0252 0.0104  35  VAL   B N   
4917 C CA  . VAL   B 35  ? 0.1664 0.1365 0.1165 -0.0177 -0.0153 0.0072  35  VAL   B CA  
4918 C C   . VAL   B 35  ? 0.1495 0.1306 0.1266 -0.0168 -0.0089 -0.0003 35  VAL   B C   
4919 O O   . VAL   B 35  ? 0.1534 0.1431 0.1199 -0.0210 0.0057  -0.0055 35  VAL   B O   
4920 C CB  . VAL   B 35  ? 0.1531 0.1582 0.1233 -0.0212 -0.0068 -0.0035 35  VAL   B CB  
4921 C CG1 . VAL   B 35  ? 0.1574 0.1828 0.1429 -0.0272 0.0036  0.0017  35  VAL   B CG1 
4922 C CG2 . VAL   B 35  ? 0.1674 0.1592 0.1545 -0.0184 -0.0008 -0.0119 35  VAL   B CG2 
4932 N N   . VAL   B 36  ? 0.1463 0.1354 0.1271 -0.0211 -0.0211 0.0213  36  VAL   B N   
4933 C CA  . VAL   B 36  ? 0.1454 0.1314 0.0986 -0.0166 -0.0114 0.0135  36  VAL   B CA  
4934 C C   . VAL   B 36  ? 0.1429 0.1381 0.0866 -0.0107 -0.0133 0.0023  36  VAL   B C   
4935 O O   . VAL   B 36  ? 0.1521 0.1390 0.1308 -0.0143 -0.0183 -0.0071 36  VAL   B O   
4936 C CB  . VAL   B 36  ? 0.1523 0.1349 0.1090 -0.0230 -0.0108 0.0154  36  VAL   B CB  
4937 C CG1 . VAL   B 36  ? 0.1438 0.1468 0.1322 -0.0250 -0.0257 0.0172  36  VAL   B CG1 
4938 C CG2 . VAL   B 36  ? 0.1659 0.1514 0.1170 -0.0280 -0.0194 0.0211  36  VAL   B CG2 
4948 N N   . ASN   B 37  ? 0.1470 0.1391 0.0902 -0.0034 -0.0104 0.0121  37  ASN   B N   
4949 C CA  . ASN   B 37  ? 0.1569 0.1295 0.1040 -0.0043 -0.0238 0.0015  37  ASN   B CA  
4950 C C   . ASN   B 37  ? 0.1535 0.1437 0.1244 0.0076  -0.0108 0.0101  37  ASN   B C   
4951 O O   . ASN   B 37  ? 0.1597 0.1398 0.1321 -0.0007 0.0031  0.0077  37  ASN   B O   
4952 C CB  . ASN   B 37  ? 0.1504 0.1335 0.0941 -0.0053 -0.0236 0.0051  37  ASN   B CB  
4953 C CG  . ASN   B 37  ? 0.1620 0.1439 0.1022 -0.0030 -0.0152 0.0039  37  ASN   B CG  
4954 O OD1 . ASN   B 37  ? 0.1602 0.1395 0.1614 0.0077  -0.0267 -0.0054 37  ASN   B OD1 
4955 N ND2 . ASN   B 37  ? 0.1680 0.1496 0.1098 0.0029  -0.0152 0.0037  37  ASN   B ND2 
4962 N N   . ALA   B 38  ? 0.1643 0.1457 0.1163 0.0144  0.0040  0.0158  38  ALA   B N   
4963 C CA  . ALA   B 38  ? 0.1704 0.1506 0.1096 0.0054  -0.0046 0.0069  38  ALA   B CA  
4964 C C   . ALA   B 38  ? 0.1724 0.1464 0.1303 0.0070  0.0015  0.0105  38  ALA   B C   
4965 O O   . ALA   B 38  ? 0.1871 0.1477 0.1364 0.0068  -0.0043 0.0193  38  ALA   B O   
4966 C CB  . ALA   B 38  ? 0.1948 0.1584 0.1325 -0.0075 0.0060  -0.0029 38  ALA   B CB  
4972 N N   . ALA   B 39  ? 0.1693 0.1531 0.0874 0.0199  -0.0015 0.0013  39  ALA   B N   
4973 C CA  . ALA   B 39  ? 0.1903 0.1691 0.0664 0.0256  -0.0203 -0.0110 39  ALA   B CA  
4974 C C   . ALA   B 39  ? 0.1905 0.1627 0.0513 0.0209  -0.0083 -0.0062 39  ALA   B C   
4975 O O   . ALA   B 39  ? 0.1890 0.1667 0.1336 -0.0099 -0.0026 0.0063  39  ALA   B O   
4976 C CB  . ALA   B 39  ? 0.1791 0.1596 0.1256 0.0047  -0.0028 0.0039  39  ALA   B CB  
4982 N N   . ASN   B 40  ? 0.1998 0.1828 0.0515 0.0114  -0.0030 -0.0021 40  ASN   B N   
4983 C CA  . ASN   B 40  ? 0.2129 0.1862 0.0659 0.0193  -0.0211 -0.0083 40  ASN   B CA  
4984 C C   . ASN   B 40  ? 0.1990 0.1833 0.0898 0.0230  -0.0132 0.0025  40  ASN   B C   
4985 O O   . ASN   B 40  ? 0.2001 0.1729 0.1054 0.0218  -0.0071 0.0042  40  ASN   B O   
4986 C CB  . ASN   B 40  ? 0.2175 0.1765 0.1212 0.0162  -0.0089 0.0185  40  ASN   B CB  
4987 C CG  . ASN   B 40  ? 0.2198 0.1819 0.1756 0.0218  -0.0241 0.0109  40  ASN   B CG  
4988 O OD1 . ASN   B 40  ? 0.2183 0.1613 0.2754 0.0212  -0.0441 0.0172  40  ASN   B OD1 
4989 N ND2 . ASN   B 40  ? 0.2158 0.1841 0.1830 0.0206  -0.0180 0.0190  40  ASN   B ND2 
4996 N N   . VAL   B 41  ? 0.2083 0.1825 0.1001 0.0252  0.0151  -0.0044 41  VAL   B N   
4997 C CA  . VAL   B 41  ? 0.2132 0.1963 0.1147 0.0241  -0.0041 -0.0106 41  VAL   B CA  
4998 C C   . VAL   B 41  ? 0.2024 0.1905 0.1291 0.0336  -0.0170 -0.0044 41  VAL   B C   
4999 O O   . VAL   B 41  ? 0.2019 0.1870 0.1516 0.0335  -0.0177 -0.0051 41  VAL   B O   
5000 C CB  . VAL   B 41  ? 0.2310 0.2124 0.1360 0.0048  0.0209  -0.0185 41  VAL   B CB  
5001 C CG1 . VAL   B 41  ? 0.2333 0.2119 0.1654 -0.0020 0.0276  -0.0161 41  VAL   B CG1 
5002 C CG2 . VAL   B 41  ? 0.2330 0.2367 0.1513 -0.0095 0.0177  -0.0182 41  VAL   B CG2 
5012 N N   A TYR   B 42  ? 0.2079 0.1918 0.1287 0.0285  -0.0178 -0.0113 42  TYR   B N   
5013 N N   B TYR   B 42  ? 0.2056 0.1874 0.1311 0.0263  -0.0226 -0.0107 42  TYR   B N   
5014 C CA  A TYR   B 42  ? 0.2192 0.1964 0.1127 0.0309  -0.0249 -0.0125 42  TYR   B CA  
5015 C CA  B TYR   B 42  ? 0.2142 0.1874 0.1181 0.0266  -0.0332 -0.0121 42  TYR   B CA  
5016 C C   A TYR   B 42  ? 0.2087 0.1793 0.1037 0.0306  -0.0243 -0.0174 42  TYR   B C   
5017 C C   B TYR   B 42  ? 0.2061 0.1740 0.1113 0.0282  -0.0267 -0.0145 42  TYR   B C   
5018 O O   A TYR   B 42  ? 0.2032 0.1908 0.1674 0.0310  -0.0325 -0.0231 42  TYR   B O   
5019 O O   B TYR   B 42  ? 0.2012 0.1839 0.1721 0.0294  -0.0335 -0.0172 42  TYR   B O   
5020 C CB  A TYR   B 42  ? 0.2383 0.2218 0.1508 0.0283  -0.0193 0.0071  42  TYR   B CB  
5021 C CB  B TYR   B 42  ? 0.2296 0.2054 0.1508 0.0204  -0.0384 -0.0006 42  TYR   B CB  
5022 C CG  A TYR   B 42  ? 0.2295 0.2314 0.1392 0.0169  0.0002  0.0200  42  TYR   B CG  
5023 C CG  B TYR   B 42  ? 0.2168 0.2072 0.1303 0.0027  -0.0398 -0.0015 42  TYR   B CG  
5024 C CD1 A TYR   B 42  ? 0.2190 0.2269 0.1317 0.0066  0.0189  0.0241  42  TYR   B CD1 
5025 C CD1 B TYR   B 42  ? 0.2047 0.2001 0.1167 -0.0154 -0.0368 -0.0020 42  TYR   B CD1 
5026 C CD2 A TYR   B 42  ? 0.2316 0.2387 0.1792 0.0188  -0.0004 0.0235  42  TYR   B CD2 
5027 C CD2 B TYR   B 42  ? 0.2094 0.2051 0.1540 -0.0002 -0.0410 -0.0048 42  TYR   B CD2 
5028 C CE1 A TYR   B 42  ? 0.2239 0.2351 0.1435 0.0071  0.0147  0.0290  42  TYR   B CE1 
5029 C CE1 B TYR   B 42  ? 0.1995 0.2044 0.1103 -0.0220 -0.0343 -0.0071 42  TYR   B CE1 
5030 C CE2 A TYR   B 42  ? 0.2311 0.2451 0.1819 0.0094  0.0274  0.0399  42  TYR   B CE2 
5031 C CE2 B TYR   B 42  ? 0.2008 0.2121 0.1467 -0.0156 -0.0179 0.0094  42  TYR   B CE2 
5032 C CZ  A TYR   B 42  ? 0.2390 0.2516 0.1697 0.0198  0.0344  0.0255  42  TYR   B CZ  
5033 C CZ  B TYR   B 42  ? 0.1961 0.2094 0.1192 -0.0197 -0.0202 -0.0063 42  TYR   B CZ  
5034 O OH  A TYR   B 42  ? 0.2636 0.2716 0.2138 0.0280  0.0399  0.0297  42  TYR   B OH  
5035 O OH  B TYR   B 42  ? 0.1935 0.2077 0.1450 -0.0342 -0.0156 0.0049  42  TYR   B OH  
5054 N N   . LEU   B 43  ? 0.1971 0.1672 0.1020 0.0160  -0.0132 -0.0151 43  LEU   B N   
5055 C CA  . LEU   B 43  ? 0.1997 0.1624 0.1013 0.0073  -0.0264 -0.0082 43  LEU   B CA  
5056 C C   . LEU   B 43  ? 0.1995 0.1480 0.1264 0.0090  -0.0191 -0.0099 43  LEU   B C   
5057 O O   . LEU   B 43  ? 0.2019 0.1598 0.1734 0.0070  -0.0206 -0.0126 43  LEU   B O   
5058 C CB  . LEU   B 43  ? 0.1864 0.1620 0.1435 0.0032  -0.0252 -0.0071 43  LEU   B CB  
5059 C CG  . LEU   B 43  ? 0.1819 0.1618 0.1560 0.0024  -0.0358 -0.0058 43  LEU   B CG  
5060 C CD1 . LEU   B 43  ? 0.1860 0.1665 0.1765 -0.0024 -0.0474 -0.0130 43  LEU   B CD1 
5061 C CD2 . LEU   B 43  ? 0.1847 0.1637 0.1606 -0.0097 -0.0380 -0.0026 43  LEU   B CD2 
5074 N N   . LYS   B 44  ? 0.1924 0.1525 0.1460 0.0186  -0.0182 -0.0152 44  LYS   B N   
5075 C CA  . LYS   B 44  ? 0.2058 0.1749 0.1364 0.0135  -0.0211 -0.0073 44  LYS   B CA  
5076 C C   . LYS   B 44  ? 0.2008 0.1731 0.1388 0.0218  -0.0152 0.0101  44  LYS   B C   
5077 O O   . LYS   B 44  ? 0.2217 0.1747 0.1740 0.0122  -0.0045 0.0046  44  LYS   B O   
5078 C CB  . LYS   B 44  ? 0.2380 0.1951 0.1573 0.0252  -0.0330 -0.0190 44  LYS   B CB  
5079 C CG  . LYS   B 44  ? 0.2831 0.2255 0.2101 0.0197  -0.0580 -0.0107 44  LYS   B CG  
5080 C CD  . LYS   B 44  ? 0.3279 0.2458 0.3025 -0.0062 -0.0771 -0.0212 44  LYS   B CD  
5081 C CE  . LYS   B 44  ? 0.3750 0.2685 0.3749 -0.0126 -0.0870 0.0062  44  LYS   B CE  
5082 N NZ  . LYS   B 44  ? 0.3851 0.2748 0.3837 -0.0100 -0.1078 0.0336  44  LYS   B NZ  
5096 N N   . HIS   B 45  ? 0.1934 0.1729 0.1314 -0.0085 -0.0137 0.0157  45  HIS   B N   
5097 C CA  . HIS   B 45  ? 0.1974 0.1675 0.1269 0.0068  -0.0136 -0.0081 45  HIS   B CA  
5098 C C   . HIS   B 45  ? 0.2225 0.1883 0.1817 0.0234  -0.0273 -0.0091 45  HIS   B C   
5099 O O   . HIS   B 45  ? 0.2440 0.2217 0.2396 0.0498  0.0028  -0.0005 45  HIS   B O   
5100 C CB  . HIS   B 45  ? 0.1870 0.1777 0.1330 0.0081  -0.0124 -0.0162 45  HIS   B CB  
5101 C CG  . HIS   B 45  ? 0.1851 0.1693 0.1252 0.0050  -0.0188 0.0019  45  HIS   B CG  
5102 N ND1 . HIS   B 45  ? 0.1930 0.1593 0.1415 0.0115  -0.0329 -0.0090 45  HIS   B ND1 
5103 C CD2 . HIS   B 45  ? 0.1957 0.1664 0.1570 -0.0089 -0.0304 0.0011  45  HIS   B CD2 
5104 C CE1 . HIS   B 45  ? 0.1866 0.1427 0.1499 0.0096  -0.0374 -0.0170 45  HIS   B CE1 
5105 N NE2 . HIS   B 45  ? 0.2067 0.1552 0.1516 -0.0042 -0.0306 -0.0062 45  HIS   B NE2 
5113 N N   A GLY   B 46  ? 0.2362 0.1819 0.2212 0.0311  -0.0448 -0.0054 46  GLY   B N   
5114 N N   B GLY   B 46  ? 0.2354 0.1877 0.2134 0.0314  -0.0450 0.0010  46  GLY   B N   
5115 C CA  A GLY   B 46  ? 0.2544 0.1994 0.2772 0.0246  -0.0536 -0.0066 46  GLY   B CA  
5116 C CA  B GLY   B 46  ? 0.2526 0.2071 0.2572 0.0270  -0.0561 0.0058  46  GLY   B CA  
5117 C C   A GLY   B 46  ? 0.2692 0.2186 0.3252 0.0239  -0.0452 -0.0061 46  GLY   B C   
5118 C C   B GLY   B 46  ? 0.2677 0.2286 0.2984 0.0280  -0.0505 0.0112  46  GLY   B C   
5119 O O   A GLY   B 46  ? 0.2786 0.2192 0.4068 0.0322  -0.0228 -0.0381 46  GLY   B O   
5120 O O   B GLY   B 46  ? 0.2783 0.2465 0.3467 0.0309  -0.0313 0.0023  46  GLY   B O   
5127 N N   . GLY   B 47  ? 0.2656 0.2333 0.2828 0.0043  -0.0403 -0.0001 47  GLY   B N   
5128 C CA  . GLY   B 47  ? 0.2412 0.2041 0.2287 -0.0024 -0.0257 -0.0063 47  GLY   B CA  
5129 C C   . GLY   B 47  ? 0.2116 0.1823 0.1677 -0.0032 -0.0057 0.0053  47  GLY   B C   
5130 O O   . GLY   B 47  ? 0.2287 0.1657 0.1821 0.0059  -0.0151 0.0079  47  GLY   B O   
5135 N N   . GLY   B 48  ? 0.1957 0.1713 0.1830 0.0052  -0.0233 0.0165  48  GLY   B N   
5136 C CA  . GLY   B 48  ? 0.2009 0.1725 0.1744 -0.0024 -0.0128 0.0119  48  GLY   B CA  
5137 C C   . GLY   B 48  ? 0.1776 0.1560 0.1686 0.0075  0.0021  -0.0012 48  GLY   B C   
5138 O O   . GLY   B 48  ? 0.1622 0.1463 0.2159 0.0064  -0.0054 0.0002  48  GLY   B O   
5142 N N   . VAL   B 49  ? 0.1724 0.1597 0.1619 0.0166  -0.0035 -0.0026 49  VAL   B N   
5143 C CA  . VAL   B 49  ? 0.1705 0.1802 0.1393 0.0185  -0.0250 -0.0184 49  VAL   B CA  
5144 C C   . VAL   B 49  ? 0.1604 0.1673 0.1115 0.0080  -0.0195 -0.0213 49  VAL   B C   
5145 O O   . VAL   B 49  ? 0.1640 0.1741 0.1546 0.0066  -0.0052 -0.0083 49  VAL   B O   
5146 C CB  . VAL   B 49  ? 0.1707 0.1996 0.1719 0.0024  -0.0370 -0.0122 49  VAL   B CB  
5147 C CG1 . VAL   B 49  ? 0.1750 0.1972 0.1731 0.0188  -0.0366 -0.0034 49  VAL   B CG1 
5148 C CG2 . VAL   B 49  ? 0.1920 0.2176 0.2172 -0.0032 -0.0518 -0.0398 49  VAL   B CG2 
5158 N N   . ALA   B 50  ? 0.1659 0.1459 0.1381 -0.0049 -0.0071 -0.0112 50  ALA   B N   
5159 C CA  . ALA   B 50  ? 0.1631 0.1409 0.1334 0.0081  -0.0077 0.0032  50  ALA   B CA  
5160 C C   . ALA   B 50  ? 0.1566 0.1518 0.1393 0.0060  -0.0087 0.0047  50  ALA   B C   
5161 O O   . ALA   B 50  ? 0.1620 0.1448 0.1562 0.0056  -0.0008 0.0016  50  ALA   B O   
5162 C CB  . ALA   B 50  ? 0.1908 0.1377 0.1348 0.0034  -0.0027 0.0077  50  ALA   B CB  
5168 N N   . GLY   B 51  ? 0.1688 0.1601 0.1502 0.0127  -0.0198 0.0058  51  GLY   B N   
5169 C CA  . GLY   B 51  ? 0.1703 0.1694 0.1791 0.0198  -0.0350 0.0010  51  GLY   B CA  
5170 C C   . GLY   B 51  ? 0.1675 0.1748 0.1702 0.0283  -0.0212 -0.0076 51  GLY   B C   
5171 O O   . GLY   B 51  ? 0.1612 0.1948 0.1901 0.0141  -0.0135 -0.0163 51  GLY   B O   
5175 N N   . ALA   B 52  ? 0.1625 0.1594 0.1480 0.0174  -0.0164 -0.0042 52  ALA   B N   
5176 C CA  . ALA   B 52  ? 0.1705 0.1639 0.1616 0.0177  -0.0082 -0.0242 52  ALA   B CA  
5177 C C   . ALA   B 52  ? 0.1674 0.1615 0.1477 0.0099  0.0025  -0.0134 52  ALA   B C   
5178 O O   . ALA   B 52  ? 0.1617 0.1698 0.1859 0.0123  -0.0134 -0.0021 52  ALA   B O   
5179 C CB  . ALA   B 52  ? 0.1837 0.1674 0.1560 0.0102  -0.0066 -0.0099 52  ALA   B CB  
5185 N N   . LEU   B 53  ? 0.1603 0.1617 0.1519 0.0116  -0.0137 -0.0035 53  LEU   B N   
5186 C CA  . LEU   B 53  ? 0.1522 0.1686 0.1395 0.0068  -0.0106 -0.0093 53  LEU   B CA  
5187 C C   . LEU   B 53  ? 0.1698 0.1693 0.1185 0.0029  0.0007  -0.0049 53  LEU   B C   
5188 O O   . LEU   B 53  ? 0.1605 0.1795 0.1553 0.0028  -0.0026 0.0054  53  LEU   B O   
5189 C CB  . LEU   B 53  ? 0.1596 0.1736 0.1632 0.0128  -0.0073 0.0059  53  LEU   B CB  
5190 C CG  . LEU   B 53  ? 0.1601 0.1745 0.1557 -0.0000 -0.0121 0.0145  53  LEU   B CG  
5191 C CD1 . LEU   B 53  ? 0.1698 0.1976 0.1727 0.0237  0.0012  -0.0019 53  LEU   B CD1 
5192 C CD2 . LEU   B 53  ? 0.1686 0.2086 0.1890 -0.0140 -0.0236 -0.0137 53  LEU   B CD2 
5204 N N   . ASN   B 54  ? 0.1656 0.1506 0.1356 0.0020  -0.0095 -0.0024 54  ASN   B N   
5205 C CA  . ASN   B 54  ? 0.1640 0.1686 0.1254 0.0074  -0.0211 -0.0135 54  ASN   B CA  
5206 C C   . ASN   B 54  ? 0.1473 0.1717 0.1657 0.0072  -0.0023 -0.0160 54  ASN   B C   
5207 O O   . ASN   B 54  ? 0.1567 0.1761 0.1789 -0.0025 0.0007  -0.0187 54  ASN   B O   
5208 C CB  . ASN   B 54  ? 0.1713 0.1826 0.1460 0.0080  -0.0109 -0.0100 54  ASN   B CB  
5209 C CG  . ASN   B 54  ? 0.1688 0.1962 0.1495 0.0085  -0.0157 -0.0149 54  ASN   B CG  
5210 O OD1 . ASN   B 54  ? 0.1627 0.1876 0.1980 0.0065  -0.0144 -0.0168 54  ASN   B OD1 
5211 N ND2 . ASN   B 54  ? 0.1933 0.2105 0.1973 0.0027  -0.0353 0.0023  54  ASN   B ND2 
5218 N N   . LYS   B 55  ? 0.1442 0.1742 0.2092 0.0115  -0.0026 -0.0196 55  LYS   B N   
5219 C CA  . LYS   B 55  ? 0.1697 0.1790 0.2216 0.0103  -0.0007 -0.0146 55  LYS   B CA  
5220 C C   . LYS   B 55  ? 0.1627 0.1891 0.2101 0.0100  0.0036  -0.0225 55  LYS   B C   
5221 O O   . LYS   B 55  ? 0.1600 0.1998 0.2320 0.0125  -0.0088 -0.0193 55  LYS   B O   
5222 C CB  . LYS   B 55  ? 0.1875 0.1826 0.2770 0.0312  0.0220  -0.0085 55  LYS   B CB  
5223 C CG  . LYS   B 55  ? 0.2318 0.2273 0.3727 0.0405  0.0223  0.0101  55  LYS   B CG  
5224 C CD  . LYS   B 55  ? 0.2754 0.2629 0.4596 0.0528  0.0392  0.0281  55  LYS   B CD  
5225 C CE  . LYS   B 55  ? 0.3071 0.2844 0.5311 0.0530  0.0727  0.0373  55  LYS   B CE  
5226 N NZ  . LYS   B 55  ? 0.3127 0.3065 0.5794 0.0454  0.0599  0.0515  55  LYS   B NZ  
5240 N N   . ALA   B 56  ? 0.1607 0.1904 0.1810 0.0070  -0.0088 -0.0202 56  ALA   B N   
5241 C CA  . ALA   B 56  ? 0.1705 0.2044 0.1814 0.0028  -0.0105 -0.0189 56  ALA   B CA  
5242 C C   . ALA   B 56  ? 0.1763 0.2003 0.1750 -0.0014 0.0156  -0.0094 56  ALA   B C   
5243 O O   . ALA   B 56  ? 0.1900 0.2025 0.1998 -0.0006 0.0309  -0.0112 56  ALA   B O   
5244 C CB  . ALA   B 56  ? 0.1902 0.2291 0.1908 -0.0184 -0.0186 -0.0022 56  ALA   B CB  
5250 N N   . THR   B 57  ? 0.1719 0.1910 0.1891 -0.0051 0.0168  -0.0189 57  THR   B N   
5251 C CA  . THR   B 57  ? 0.1752 0.1809 0.1891 -0.0045 0.0221  -0.0156 57  THR   B CA  
5252 C C   . THR   B 57  ? 0.1691 0.1922 0.2064 -0.0070 0.0261  -0.0125 57  THR   B C   
5253 O O   . THR   B 57  ? 0.1740 0.1978 0.2217 -0.0181 0.0062  -0.0181 57  THR   B O   
5254 C CB  . THR   B 57  ? 0.1877 0.1609 0.1438 -0.0069 0.0185  -0.0070 57  THR   B CB  
5255 O OG1 . THR   B 57  ? 0.1790 0.1708 0.1778 -0.0142 0.0172  -0.0017 57  THR   B OG1 
5256 C CG2 . THR   B 57  ? 0.1982 0.1693 0.1709 -0.0243 0.0255  -0.0115 57  THR   B CG2 
5264 N N   . ASN   B 58  ? 0.1736 0.2136 0.2419 -0.0162 0.0056  -0.0481 58  ASN   B N   
5265 C CA  . ASN   B 58  ? 0.1969 0.2622 0.2777 -0.0390 0.0377  -0.0317 58  ASN   B CA  
5266 C C   . ASN   B 58  ? 0.1607 0.2453 0.2178 -0.0150 -0.0079 -0.0357 58  ASN   B C   
5267 O O   . ASN   B 58  ? 0.1640 0.2651 0.2481 -0.0148 -0.0242 -0.0365 58  ASN   B O   
5268 C CB  . ASN   B 58  ? 0.3086 0.3669 0.4303 -0.0613 0.0991  -0.0158 58  ASN   B CB  
5269 C CG  . ASN   B 58  ? 0.4524 0.4823 0.6086 -0.0587 0.1417  0.0121  58  ASN   B CG  
5270 O OD1 . ASN   B 58  ? 0.4697 0.5027 0.6802 -0.0596 0.1515  0.0207  58  ASN   B OD1 
5271 N ND2 . ASN   B 58  ? 0.5642 0.5642 0.6630 -0.0587 0.1578  0.0175  58  ASN   B ND2 
5278 N N   . ASN   B 59  ? 0.1583 0.2310 0.1917 -0.0098 -0.0126 -0.0083 59  ASN   B N   
5279 C CA  . ASN   B 59  ? 0.1669 0.2232 0.1951 -0.0208 -0.0220 -0.0023 59  ASN   B CA  
5280 C C   . ASN   B 59  ? 0.1530 0.2154 0.1877 -0.0248 -0.0293 -0.0253 59  ASN   B C   
5281 O O   . ASN   B 59  ? 0.1603 0.2124 0.2021 -0.0113 -0.0184 -0.0212 59  ASN   B O   
5282 C CB  . ASN   B 59  ? 0.1818 0.2427 0.2116 -0.0080 -0.0302 -0.0047 59  ASN   B CB  
5283 C CG  . ASN   B 59  ? 0.1937 0.2636 0.2330 -0.0007 -0.0419 0.0011  59  ASN   B CG  
5284 O OD1 . ASN   B 59  ? 0.1783 0.2627 0.2339 -0.0014 -0.0310 0.0144  59  ASN   B OD1 
5285 N ND2 . ASN   B 59  ? 0.1982 0.2717 0.2547 -0.0085 -0.0477 -0.0111 59  ASN   B ND2 
5292 N N   . ALA   B 60  ? 0.1574 0.1992 0.1923 -0.0165 -0.0001 -0.0192 60  ALA   B N   
5293 C CA  . ALA   B 60  ? 0.1709 0.1926 0.1835 -0.0232 0.0035  -0.0040 60  ALA   B CA  
5294 C C   . ALA   B 60  ? 0.1705 0.1848 0.1639 -0.0166 -0.0043 -0.0189 60  ALA   B C   
5295 O O   . ALA   B 60  ? 0.1790 0.1806 0.1876 -0.0173 -0.0061 -0.0192 60  ALA   B O   
5296 C CB  . ALA   B 60  ? 0.1913 0.1906 0.2167 -0.0281 0.0055  -0.0114 60  ALA   B CB  
5302 N N   . MET   B 61  ? 0.1667 0.1706 0.1624 -0.0124 -0.0022 -0.0111 61  MET   B N   
5303 C CA  . MET   B 61  ? 0.1665 0.1667 0.1500 -0.0098 -0.0159 -0.0063 61  MET   B CA  
5304 C C   . MET   B 61  ? 0.1702 0.1625 0.1495 -0.0140 -0.0191 -0.0040 61  MET   B C   
5305 O O   . MET   B 61  ? 0.1620 0.1622 0.1610 -0.0003 -0.0144 -0.0275 61  MET   B O   
5306 C CB  . MET   B 61  ? 0.1649 0.1708 0.1607 -0.0019 -0.0249 -0.0210 61  MET   B CB  
5307 C CG  . MET   B 61  ? 0.1513 0.1527 0.1667 -0.0018 -0.0095 0.0032  61  MET   B CG  
5308 S SD  . MET   B 61  ? 0.1615 0.1642 0.1727 -0.0025 -0.0092 -0.0151 61  MET   B SD  
5309 C CE  . MET   B 61  ? 0.1647 0.1794 0.1904 -0.0028 -0.0087 -0.0359 61  MET   B CE  
5319 N N   . GLN   B 62  ? 0.1735 0.1600 0.1287 -0.0071 -0.0339 0.0093  62  GLN   B N   
5320 C CA  . GLN   B 62  ? 0.1822 0.1654 0.1349 0.0038  -0.0357 0.0068  62  GLN   B CA  
5321 C C   . GLN   B 62  ? 0.1754 0.1787 0.1540 0.0037  -0.0347 -0.0149 62  GLN   B C   
5322 O O   . GLN   B 62  ? 0.1970 0.1686 0.1718 0.0043  -0.0324 -0.0156 62  GLN   B O   
5323 C CB  . GLN   B 62  ? 0.1916 0.1671 0.1437 0.0096  -0.0275 0.0061  62  GLN   B CB  
5324 C CG  . GLN   B 62  ? 0.1978 0.1722 0.1516 0.0103  -0.0407 -0.0182 62  GLN   B CG  
5325 C CD  . GLN   B 62  ? 0.1906 0.1756 0.1527 0.0190  -0.0308 -0.0196 62  GLN   B CD  
5326 O OE1 . GLN   B 62  ? 0.1896 0.1662 0.1752 0.0154  -0.0371 -0.0192 62  GLN   B OE1 
5327 N NE2 . GLN   B 62  ? 0.1977 0.1771 0.1527 0.0109  -0.0309 -0.0195 62  GLN   B NE2 
5336 N N   . VAL   B 63  ? 0.1667 0.1786 0.1793 -0.0002 -0.0213 -0.0331 63  VAL   B N   
5337 C CA  . VAL   B 63  ? 0.1837 0.1843 0.1953 -0.0009 -0.0260 -0.0176 63  VAL   B CA  
5338 C C   . VAL   B 63  ? 0.1836 0.1673 0.1754 -0.0175 -0.0414 -0.0380 63  VAL   B C   
5339 O O   . VAL   B 63  ? 0.2060 0.1709 0.1807 -0.0027 -0.0555 -0.0294 63  VAL   B O   
5340 C CB  . VAL   B 63  ? 0.1810 0.1860 0.2319 -0.0124 -0.0373 -0.0156 63  VAL   B CB  
5341 C CG1 . VAL   B 63  ? 0.1903 0.1874 0.2582 -0.0198 -0.0153 -0.0173 63  VAL   B CG1 
5342 C CG2 . VAL   B 63  ? 0.1790 0.2137 0.2479 -0.0010 -0.0396 -0.0207 63  VAL   B CG2 
5352 N N   . GLU   B 64  ? 0.1818 0.1593 0.1770 -0.0108 -0.0418 -0.0246 64  GLU   B N   
5353 C CA  . GLU   B 64  ? 0.1781 0.1605 0.1623 -0.0123 -0.0460 -0.0047 64  GLU   B CA  
5354 C C   . GLU   B 64  ? 0.1756 0.1587 0.1679 0.0068  -0.0406 -0.0029 64  GLU   B C   
5355 O O   . GLU   B 64  ? 0.1774 0.1641 0.1771 -0.0030 -0.0329 -0.0128 64  GLU   B O   
5356 C CB  . GLU   B 64  ? 0.1737 0.1672 0.1646 -0.0221 -0.0357 0.0009  64  GLU   B CB  
5357 C CG  . GLU   B 64  ? 0.1803 0.1720 0.1690 -0.0160 -0.0346 -0.0094 64  GLU   B CG  
5358 C CD  . GLU   B 64  ? 0.1822 0.1983 0.1847 -0.0252 -0.0333 -0.0077 64  GLU   B CD  
5359 O OE1 . GLU   B 64  ? 0.1889 0.2032 0.2008 -0.0332 -0.0187 -0.0345 64  GLU   B OE1 
5360 O OE2 . GLU   B 64  ? 0.1932 0.2090 0.1931 -0.0406 -0.0479 -0.0106 64  GLU   B OE2 
5367 N N   . SER   B 65  ? 0.1814 0.1581 0.1424 0.0009  -0.0266 -0.0205 65  SER   B N   
5368 C CA  . SER   B 65  ? 0.1789 0.1540 0.1385 0.0077  -0.0249 -0.0141 65  SER   B CA  
5369 C C   . SER   B 65  ? 0.1851 0.1592 0.1430 0.0120  -0.0407 -0.0196 65  SER   B C   
5370 O O   . SER   B 65  ? 0.1773 0.1640 0.1632 0.0033  -0.0249 -0.0147 65  SER   B O   
5371 C CB  . SER   B 65  ? 0.1832 0.1551 0.1368 0.0019  -0.0200 -0.0088 65  SER   B CB  
5372 O OG  . SER   B 65  ? 0.1904 0.1554 0.1450 -0.0030 -0.0141 -0.0156 65  SER   B OG  
5378 N N   . ASP   B 66  ? 0.1971 0.1740 0.1388 0.0025  -0.0525 -0.0230 66  ASP   B N   
5379 C CA  . ASP   B 66  ? 0.1899 0.1706 0.1371 0.0078  -0.0496 -0.0118 66  ASP   B CA  
5380 C C   . ASP   B 66  ? 0.1906 0.1763 0.1500 -0.0057 -0.0382 -0.0223 66  ASP   B C   
5381 O O   . ASP   B 66  ? 0.2020 0.1811 0.1599 0.0136  -0.0371 -0.0252 66  ASP   B O   
5382 C CB  . ASP   B 66  ? 0.1992 0.1881 0.1850 0.0188  -0.0489 -0.0293 66  ASP   B CB  
5383 C CG  . ASP   B 66  ? 0.2310 0.2009 0.2092 0.0264  -0.0689 -0.0136 66  ASP   B CG  
5384 O OD1 . ASP   B 66  ? 0.2591 0.1927 0.2071 0.0210  -0.0516 -0.0023 66  ASP   B OD1 
5385 O OD2 . ASP   B 66  ? 0.2579 0.2247 0.2891 0.0527  -0.0674 -0.0136 66  ASP   B OD2 
5390 N N   . ASP   B 67  ? 0.1822 0.1710 0.1519 -0.0035 -0.0318 -0.0314 67  ASP   B N   
5391 C CA  . ASP   B 67  ? 0.2074 0.1644 0.1624 -0.0068 -0.0292 -0.0160 67  ASP   B CA  
5392 C C   . ASP   B 67  ? 0.2009 0.1657 0.1683 0.0073  -0.0305 -0.0255 67  ASP   B C   
5393 O O   . ASP   B 67  ? 0.2011 0.1760 0.1830 0.0027  -0.0194 -0.0329 67  ASP   B O   
5394 C CB  . ASP   B 67  ? 0.2232 0.1807 0.1780 -0.0127 -0.0520 -0.0255 67  ASP   B CB  
5395 C CG  . ASP   B 67  ? 0.2580 0.1916 0.1860 -0.0116 -0.0830 -0.0272 67  ASP   B CG  
5396 O OD1 . ASP   B 67  ? 0.2825 0.1902 0.2233 -0.0009 -0.0710 -0.0165 67  ASP   B OD1 
5397 O OD2 . ASP   B 67  ? 0.2772 0.1893 0.2153 0.0072  -0.0806 -0.0144 67  ASP   B OD2 
5402 N N   . TYR   B 68  ? 0.1873 0.1633 0.1875 0.0123  -0.0287 -0.0315 68  TYR   B N   
5403 C CA  . TYR   B 68  ? 0.1850 0.1751 0.1928 0.0169  -0.0404 -0.0468 68  TYR   B CA  
5404 C C   . TYR   B 68  ? 0.1825 0.1701 0.1911 0.0109  -0.0361 -0.0367 68  TYR   B C   
5405 O O   . TYR   B 68  ? 0.1878 0.1692 0.1981 0.0102  -0.0400 -0.0406 68  TYR   B O   
5406 C CB  . TYR   B 68  ? 0.1889 0.2013 0.1991 0.0188  -0.0487 -0.0499 68  TYR   B CB  
5407 C CG  . TYR   B 68  ? 0.2065 0.2187 0.2103 0.0219  -0.0420 -0.0605 68  TYR   B CG  
5408 C CD1 . TYR   B 68  ? 0.2172 0.2207 0.2078 -0.0003 -0.0398 -0.0662 68  TYR   B CD1 
5409 C CD2 . TYR   B 68  ? 0.2136 0.2362 0.2411 0.0244  -0.0611 -0.0607 68  TYR   B CD2 
5410 C CE1 . TYR   B 68  ? 0.2262 0.2377 0.2346 -0.0008 -0.0312 -0.0733 68  TYR   B CE1 
5411 C CE2 . TYR   B 68  ? 0.2043 0.2389 0.2393 0.0206  -0.0516 -0.0853 68  TYR   B CE2 
5412 C CZ  . TYR   B 68  ? 0.2060 0.2382 0.2475 0.0121  -0.0376 -0.0811 68  TYR   B CZ  
5413 O OH  . TYR   B 68  ? 0.1974 0.2535 0.2802 0.0019  -0.0203 -0.0564 68  TYR   B OH  
5423 N N   . ILE   B 69  ? 0.1759 0.1592 0.1804 0.0130  -0.0395 -0.0317 69  ILE   B N   
5424 C CA  . ILE   B 69  ? 0.1818 0.1679 0.1737 -0.0011 -0.0303 -0.0233 69  ILE   B CA  
5425 C C   . ILE   B 69  ? 0.1855 0.1674 0.1771 0.0051  -0.0406 -0.0211 69  ILE   B C   
5426 O O   . ILE   B 69  ? 0.1899 0.1743 0.1787 0.0023  -0.0390 -0.0190 69  ILE   B O   
5427 C CB  . ILE   B 69  ? 0.1915 0.1730 0.2009 -0.0035 -0.0130 -0.0266 69  ILE   B CB  
5428 C CG1 . ILE   B 69  ? 0.1943 0.1803 0.2120 -0.0109 -0.0024 -0.0327 69  ILE   B CG1 
5429 C CG2 . ILE   B 69  ? 0.1965 0.1832 0.2209 -0.0035 -0.0015 -0.0248 69  ILE   B CG2 
5430 C CD1 . ILE   B 69  ? 0.2044 0.1891 0.2179 -0.0321 -0.0001 -0.0507 69  ILE   B CD1 
5442 N N   . ALA   B 70  ? 0.1861 0.1614 0.1630 0.0069  -0.0413 -0.0205 70  ALA   B N   
5443 C CA  . ALA   B 70  ? 0.1828 0.1715 0.1503 0.0007  -0.0418 -0.0270 70  ALA   B CA  
5444 C C   . ALA   B 70  ? 0.1922 0.1720 0.1864 -0.0095 -0.0442 -0.0358 70  ALA   B C   
5445 O O   . ALA   B 70  ? 0.1930 0.1693 0.2004 -0.0012 -0.0444 -0.0276 70  ALA   B O   
5446 C CB  . ALA   B 70  ? 0.1915 0.1756 0.1702 0.0044  -0.0328 -0.0225 70  ALA   B CB  
5452 N N   . THR   B 71  ? 0.2084 0.1691 0.1816 0.0064  -0.0594 -0.0280 71  THR   B N   
5453 C CA  . THR   B 71  ? 0.2372 0.1796 0.1994 0.0194  -0.0755 -0.0219 71  THR   B CA  
5454 C C   . THR   B 71  ? 0.2312 0.1733 0.2301 0.0416  -0.0641 -0.0531 71  THR   B C   
5455 O O   . THR   B 71  ? 0.2352 0.1810 0.2732 0.0418  -0.0587 -0.0608 71  THR   B O   
5456 C CB  . THR   B 71  ? 0.2629 0.2028 0.2355 0.0133  -0.0879 -0.0011 71  THR   B CB  
5457 O OG1 . THR   B 71  ? 0.2836 0.2344 0.2887 -0.0197 -0.0781 0.0271  71  THR   B OG1 
5458 C CG2 . THR   B 71  ? 0.2898 0.2006 0.2691 0.0172  -0.0693 0.0161  71  THR   B CG2 
5466 N N   . ASN   B 72  ? 0.1988 0.1868 0.2235 0.0239  -0.0739 -0.0705 72  ASN   B N   
5467 C CA  . ASN   B 72  ? 0.2057 0.1926 0.2528 0.0285  -0.0636 -0.0678 72  ASN   B CA  
5468 C C   . ASN   B 72  ? 0.2117 0.2034 0.2579 0.0158  -0.0330 -0.0650 72  ASN   B C   
5469 O O   . ASN   B 72  ? 0.2080 0.2176 0.2872 0.0207  -0.0146 -0.0730 72  ASN   B O   
5470 C CB  . ASN   B 72  ? 0.2115 0.2064 0.2604 0.0201  -0.0766 -0.0631 72  ASN   B CB  
5471 C CG  . ASN   B 72  ? 0.2385 0.2278 0.2531 0.0351  -0.0793 -0.0363 72  ASN   B CG  
5472 O OD1 . ASN   B 72  ? 0.2667 0.2601 0.2694 0.0223  -0.0407 -0.0344 72  ASN   B OD1 
5473 N ND2 . ASN   B 72  ? 0.2579 0.2274 0.3031 0.0545  -0.0847 -0.0027 72  ASN   B ND2 
5480 N N   . GLY   B 73  ? 0.2151 0.2008 0.2166 0.0122  -0.0368 -0.0650 73  GLY   B N   
5481 C CA  . GLY   B 73  ? 0.2130 0.2239 0.1767 0.0067  -0.0216 -0.0640 73  GLY   B CA  
5482 C C   . GLY   B 73  ? 0.1951 0.2171 0.1012 0.0111  -0.0302 -0.0381 73  GLY   B C   
5483 O O   . GLY   B 73  ? 0.1967 0.2002 0.1390 0.0202  -0.0257 -0.0432 73  GLY   B O   
5487 N N   . PRO   B 74  ? 0.1932 0.2276 0.1362 0.0102  -0.0257 -0.0312 74  PRO   B N   
5488 C CA  . PRO   B 74  ? 0.1922 0.2313 0.1098 0.0117  -0.0246 -0.0198 74  PRO   B CA  
5489 C C   . PRO   B 74  ? 0.1808 0.2121 0.1178 0.0076  -0.0112 -0.0151 74  PRO   B C   
5490 O O   . PRO   B 74  ? 0.1928 0.2161 0.1859 0.0130  -0.0106 -0.0423 74  PRO   B O   
5491 C CB  . PRO   B 74  ? 0.1944 0.2532 0.1286 0.0082  -0.0189 -0.0107 74  PRO   B CB  
5492 C CG  . PRO   B 74  ? 0.2197 0.2616 0.1658 -0.0007 -0.0261 0.0010  74  PRO   B CG  
5493 C CD  . PRO   B 74  ? 0.2136 0.2463 0.1501 0.0146  -0.0130 -0.0206 74  PRO   B CD  
5501 N N   . LEU   B 75  ? 0.1853 0.1924 0.1224 0.0088  -0.0232 -0.0181 75  LEU   B N   
5502 C CA  . LEU   B 75  ? 0.1908 0.1856 0.1015 0.0045  -0.0135 -0.0047 75  LEU   B CA  
5503 C C   . LEU   B 75  ? 0.1967 0.2085 0.1181 0.0152  -0.0075 0.0083  75  LEU   B C   
5504 O O   . LEU   B 75  ? 0.2068 0.2174 0.1383 -0.0047 -0.0110 0.0119  75  LEU   B O   
5505 C CB  . LEU   B 75  ? 0.1921 0.1885 0.1000 -0.0058 -0.0179 0.0035  75  LEU   B CB  
5506 C CG  . LEU   B 75  ? 0.2180 0.2110 0.1444 -0.0326 -0.0111 -0.0015 75  LEU   B CG  
5507 C CD1 . LEU   B 75  ? 0.2500 0.2299 0.1503 -0.0428 0.0148  -0.0087 75  LEU   B CD1 
5508 C CD2 . LEU   B 75  ? 0.2564 0.2324 0.2281 -0.0123 0.0138  0.0137  75  LEU   B CD2 
5520 N N   . LYS   B 76  ? 0.2001 0.2327 0.1612 0.0045  0.0030  0.0103  76  LYS   B N   
5521 C CA  . LYS   B 76  ? 0.2019 0.2462 0.1971 -0.0040 0.0219  0.0030  76  LYS   B CA  
5522 C C   . LYS   B 76  ? 0.2035 0.2319 0.1524 0.0001  0.0188  0.0300  76  LYS   B C   
5523 O O   . LYS   B 76  ? 0.2007 0.1997 0.1697 -0.0053 0.0137  0.0229  76  LYS   B O   
5524 C CB  . LYS   B 76  ? 0.2104 0.2406 0.2629 -0.0138 0.0326  -0.0382 76  LYS   B CB  
5525 C CG  . LYS   B 76  ? 0.2143 0.2580 0.3102 -0.0071 0.0288  -0.0500 76  LYS   B CG  
5526 C CD  . LYS   B 76  ? 0.2151 0.2603 0.3562 -0.0042 0.0335  -0.0532 76  LYS   B CD  
5527 C CE  . LYS   B 76  ? 0.2209 0.2836 0.4313 -0.0034 0.0231  -0.0490 76  LYS   B CE  
5528 N NZ  . LYS   B 76  ? 0.2138 0.2886 0.4437 -0.0107 -0.0016 -0.0751 76  LYS   B NZ  
5542 N N   . VAL   B 77  ? 0.2124 0.2464 0.1684 0.0096  0.0209  0.0299  77  VAL   B N   
5543 C CA  . VAL   B 77  ? 0.2234 0.2429 0.1656 0.0006  0.0239  0.0622  77  VAL   B CA  
5544 C C   . VAL   B 77  ? 0.2077 0.2143 0.1408 0.0085  0.0362  0.0385  77  VAL   B C   
5545 O O   . VAL   B 77  ? 0.2051 0.2032 0.1609 0.0116  0.0426  0.0114  77  VAL   B O   
5546 C CB  . VAL   B 77  ? 0.2408 0.2570 0.2361 -0.0033 0.0260  0.0785  77  VAL   B CB  
5547 C CG1 . VAL   B 77  ? 0.2271 0.2511 0.2612 -0.0016 0.0431  0.0899  77  VAL   B CG1 
5548 C CG2 . VAL   B 77  ? 0.2642 0.2686 0.2510 -0.0122 0.0005  0.0765  77  VAL   B CG2 
5558 N N   . GLY   B 78  ? 0.1998 0.1904 0.1504 0.0142  0.0173  0.0274  78  GLY   B N   
5559 C CA  . GLY   B 78  ? 0.2002 0.1803 0.1252 0.0059  0.0281  0.0196  78  GLY   B CA  
5560 C C   . GLY   B 78  ? 0.1877 0.1783 0.1468 0.0110  0.0262  0.0346  78  GLY   B C   
5561 O O   . GLY   B 78  ? 0.1782 0.1651 0.1944 0.0198  0.0215  0.0397  78  GLY   B O   
5565 N N   . GLY   B 79  ? 0.1676 0.1832 0.1657 0.0054  0.0130  0.0182  79  GLY   B N   
5566 C CA  . GLY   B 79  ? 0.1716 0.1644 0.1656 0.0054  0.0142  0.0237  79  GLY   B CA  
5567 C C   . GLY   B 79  ? 0.1719 0.1640 0.1492 0.0099  0.0123  0.0105  79  GLY   B C   
5568 O O   . GLY   B 79  ? 0.1744 0.1616 0.1565 0.0084  0.0157  0.0189  79  GLY   B O   
5572 N N   . SER   B 80  ? 0.1710 0.1568 0.1596 0.0087  0.0215  0.0068  80  SER   B N   
5573 C CA  . SER   B 80  ? 0.1635 0.1535 0.1448 0.0036  0.0161  0.0087  80  SER   B CA  
5574 C C   . SER   B 80  ? 0.1516 0.1461 0.1614 0.0045  -0.0044 -0.0065 80  SER   B C   
5575 O O   . SER   B 80  ? 0.1679 0.1542 0.1847 0.0110  -0.0001 -0.0022 80  SER   B O   
5576 C CB  . SER   B 80  ? 0.1659 0.1596 0.1492 -0.0006 0.0008  0.0156  80  SER   B CB  
5577 O OG  . SER   B 80  ? 0.1668 0.1666 0.1821 -0.0057 -0.0033 0.0144  80  SER   B OG  
5583 N N   . CYS   B 81  ? 0.1522 0.1358 0.1736 -0.0001 -0.0088 -0.0009 81  CYS   B N   
5584 C CA  . CYS   B 81  ? 0.1715 0.1357 0.1451 0.0003  -0.0191 0.0060  81  CYS   B CA  
5585 C C   . CYS   B 81  ? 0.1551 0.1410 0.1208 0.0049  -0.0232 0.0093  81  CYS   B C   
5586 O O   . CYS   B 81  ? 0.1780 0.1285 0.1731 0.0097  -0.0040 0.0076  81  CYS   B O   
5587 C CB  . CYS   B 81  ? 0.1810 0.1406 0.1597 -0.0019 -0.0131 0.0083  81  CYS   B CB  
5588 S SG  . CYS   B 81  ? 0.1766 0.1680 0.1493 -0.0034 -0.0267 -0.0111 81  CYS   B SG  
5594 N N   . VAL   B 82  ? 0.1605 0.1460 0.1361 0.0065  -0.0184 0.0019  82  VAL   B N   
5595 C CA  . VAL   B 82  ? 0.1724 0.1419 0.1291 -0.0038 -0.0083 0.0048  82  VAL   B CA  
5596 C C   . VAL   B 82  ? 0.1854 0.1303 0.1393 -0.0092 -0.0070 -0.0016 82  VAL   B C   
5597 O O   . VAL   B 82  ? 0.1856 0.1376 0.1801 -0.0011 -0.0142 -0.0131 82  VAL   B O   
5598 C CB  . VAL   B 82  ? 0.1758 0.1570 0.1477 0.0010  -0.0127 0.0142  82  VAL   B CB  
5599 C CG1 . VAL   B 82  ? 0.2065 0.1774 0.1638 0.0084  -0.0148 0.0300  82  VAL   B CG1 
5600 C CG2 . VAL   B 82  ? 0.1827 0.1617 0.1767 0.0058  -0.0304 0.0095  82  VAL   B CG2 
5610 N N   . LEU   B 83  ? 0.1656 0.1379 0.1505 -0.0147 -0.0203 -0.0082 83  LEU   B N   
5611 C CA  . LEU   B 83  ? 0.1758 0.1437 0.1305 -0.0165 -0.0300 -0.0057 83  LEU   B CA  
5612 C C   . LEU   B 83  ? 0.1691 0.1381 0.1319 -0.0262 -0.0313 -0.0064 83  LEU   B C   
5613 O O   . LEU   B 83  ? 0.1599 0.1572 0.1326 -0.0250 -0.0152 -0.0009 83  LEU   B O   
5614 C CB  . LEU   B 83  ? 0.1716 0.1566 0.1385 -0.0176 -0.0248 -0.0223 83  LEU   B CB  
5615 C CG  . LEU   B 83  ? 0.1882 0.1705 0.1604 -0.0122 -0.0216 -0.0101 83  LEU   B CG  
5616 C CD1 . LEU   B 83  ? 0.1934 0.1772 0.1696 -0.0100 -0.0206 -0.0017 83  LEU   B CD1 
5617 C CD2 . LEU   B 83  ? 0.2023 0.1668 0.1855 -0.0076 -0.0307 -0.0190 83  LEU   B CD2 
5629 N N   . SER   B 84  ? 0.1743 0.1516 0.1562 -0.0260 -0.0280 -0.0013 84  SER   B N   
5630 C CA  . SER   B 84  ? 0.1687 0.1758 0.1545 -0.0242 -0.0179 0.0058  84  SER   B CA  
5631 C C   . SER   B 84  ? 0.1548 0.1968 0.0644 -0.0278 -0.0237 0.0294  84  SER   B C   
5632 O O   . SER   B 84  ? 0.1761 0.1714 0.1061 -0.0215 -0.0159 -0.0022 84  SER   B O   
5633 C CB  . SER   B 84  ? 0.1824 0.1786 0.1945 -0.0234 0.0176  -0.0044 84  SER   B CB  
5634 O OG  . SER   B 84  ? 0.1733 0.1971 0.2476 -0.0426 0.0024  0.0114  84  SER   B OG  
5640 N N   . GLY   B 85  ? 0.1495 0.2006 0.1060 -0.0229 -0.0183 0.0289  85  GLY   B N   
5641 C CA  . GLY   B 85  ? 0.1678 0.2046 0.1399 -0.0325 0.0091  -0.0183 85  GLY   B CA  
5642 C C   . GLY   B 85  ? 0.1567 0.1985 0.1484 -0.0394 -0.0048 -0.0011 85  GLY   B C   
5643 O O   . GLY   B 85  ? 0.1806 0.1957 0.1463 -0.0554 0.0131  -0.0195 85  GLY   B O   
5647 N N   . HIS   B 86  ? 0.1525 0.1875 0.1610 -0.0318 -0.0110 0.0119  86  HIS   B N   
5648 C CA  . HIS   B 86  ? 0.1653 0.1918 0.1371 -0.0385 -0.0203 0.0121  86  HIS   B CA  
5649 C C   . HIS   B 86  ? 0.1680 0.1961 0.1308 -0.0513 -0.0004 0.0234  86  HIS   B C   
5650 O O   . HIS   B 86  ? 0.1866 0.2034 0.1519 -0.0463 0.0059  0.0239  86  HIS   B O   
5651 C CB  . HIS   B 86  ? 0.1766 0.1949 0.1381 -0.0250 -0.0297 0.0024  86  HIS   B CB  
5652 C CG  . HIS   B 86  ? 0.1729 0.2042 0.1346 -0.0153 -0.0452 0.0086  86  HIS   B CG  
5653 N ND1 . HIS   B 86  ? 0.1821 0.2274 0.1814 -0.0204 -0.0325 -0.0107 86  HIS   B ND1 
5654 C CD2 . HIS   B 86  ? 0.1795 0.2059 0.1546 -0.0157 -0.0300 -0.0008 86  HIS   B CD2 
5655 C CE1 . HIS   B 86  ? 0.1959 0.2174 0.1810 -0.0097 -0.0093 -0.0408 86  HIS   B CE1 
5656 N NE2 . HIS   B 86  ? 0.1871 0.2140 0.1619 -0.0031 -0.0250 -0.0056 86  HIS   B NE2 
5664 N N   . ASN   B 87  ? 0.1703 0.1814 0.1592 -0.0310 0.0057  0.0105  87  ASN   B N   
5665 C CA  . ASN   B 87  ? 0.1839 0.1981 0.1697 -0.0240 0.0208  0.0204  87  ASN   B CA  
5666 C C   . ASN   B 87  ? 0.1958 0.1886 0.1433 -0.0313 0.0370  0.0108  87  ASN   B C   
5667 O O   . ASN   B 87  ? 0.2182 0.2032 0.1977 -0.0301 0.0621  -0.0033 87  ASN   B O   
5668 C CB  . ASN   B 87  ? 0.1859 0.2367 0.2069 -0.0209 0.0188  0.0089  87  ASN   B CB  
5669 C CG  . ASN   B 87  ? 0.1968 0.2561 0.2035 0.0103  0.0356  0.0240  87  ASN   B CG  
5670 O OD1 . ASN   B 87  ? 0.1839 0.2501 0.1920 0.0133  0.0413  0.0267  87  ASN   B OD1 
5671 N ND2 . ASN   B 87  ? 0.2293 0.2652 0.2542 0.0171  0.0476  0.0261  87  ASN   B ND2 
5678 N N   . LEU   B 88  ? 0.1788 0.1882 0.1284 -0.0332 0.0096  -0.0020 88  LEU   B N   
5679 C CA  . LEU   B 88  ? 0.1920 0.1799 0.1346 -0.0368 0.0017  -0.0049 88  LEU   B CA  
5680 C C   . LEU   B 88  ? 0.1947 0.1818 0.1405 -0.0445 -0.0134 -0.0121 88  LEU   B C   
5681 O O   . LEU   B 88  ? 0.2182 0.1882 0.1777 -0.0193 -0.0353 -0.0146 88  LEU   B O   
5682 C CB  . LEU   B 88  ? 0.2083 0.1904 0.1655 -0.0432 -0.0103 0.0041  88  LEU   B CB  
5683 C CG  . LEU   B 88  ? 0.2518 0.2144 0.1862 -0.0391 -0.0321 0.0228  88  LEU   B CG  
5684 C CD1 . LEU   B 88  ? 0.2678 0.2382 0.2121 -0.0592 -0.0167 0.0490  88  LEU   B CD1 
5685 C CD2 . LEU   B 88  ? 0.2979 0.2497 0.2683 0.0044  -0.0493 0.0011  88  LEU   B CD2 
5697 N N   . ALA   B 89  ? 0.1775 0.1749 0.1480 -0.0446 0.0116  -0.0071 89  ALA   B N   
5698 C CA  . ALA   B 89  ? 0.1786 0.1666 0.1168 -0.0394 -0.0060 0.0153  89  ALA   B CA  
5699 C C   . ALA   B 89  ? 0.1866 0.1571 0.1286 -0.0440 0.0168  0.0059  89  ALA   B C   
5700 O O   . ALA   B 89  ? 0.1610 0.1738 0.1728 -0.0450 0.0123  -0.0184 89  ALA   B O   
5701 C CB  . ALA   B 89  ? 0.1707 0.1639 0.1473 -0.0424 -0.0044 0.0221  89  ALA   B CB  
5707 N N   . LYS   B 90  ? 0.2149 0.1512 0.1329 -0.0506 -0.0036 0.0136  90  LYS   B N   
5708 C CA  . LYS   B 90  ? 0.2136 0.1511 0.1251 -0.0428 -0.0019 0.0049  90  LYS   B CA  
5709 C C   . LYS   B 90  ? 0.1959 0.1516 0.1342 -0.0386 -0.0121 -0.0084 90  LYS   B C   
5710 O O   . LYS   B 90  ? 0.2037 0.1637 0.1493 -0.0548 -0.0040 -0.0005 90  LYS   B O   
5711 C CB  . LYS   B 90  ? 0.2239 0.1592 0.1729 -0.0511 0.0075  0.0164  90  LYS   B CB  
5712 C CG  . LYS   B 90  ? 0.2172 0.1727 0.1716 -0.0363 0.0291  0.0048  90  LYS   B CG  
5713 C CD  . LYS   B 90  ? 0.2491 0.2014 0.2315 -0.0118 0.0497  -0.0147 90  LYS   B CD  
5714 C CE  . LYS   B 90  ? 0.2560 0.2195 0.2870 -0.0117 0.0620  -0.0181 90  LYS   B CE  
5715 N NZ  . LYS   B 90  ? 0.2692 0.2140 0.2773 -0.0298 0.0864  -0.0112 90  LYS   B NZ  
5729 N N   . HIS   B 91  ? 0.1770 0.1467 0.1134 -0.0377 -0.0194 0.0165  91  HIS   B N   
5730 C CA  . HIS   B 91  ? 0.1719 0.1484 0.1199 -0.0312 -0.0181 0.0084  91  HIS   B CA  
5731 C C   . HIS   B 91  ? 0.1629 0.1627 0.0710 -0.0323 -0.0096 -0.0092 91  HIS   B C   
5732 O O   . HIS   B 91  ? 0.1762 0.1659 0.1003 -0.0317 -0.0188 -0.0007 91  HIS   B O   
5733 C CB  . HIS   B 91  ? 0.1879 0.1417 0.1743 -0.0118 -0.0159 0.0152  91  HIS   B CB  
5734 C CG  . HIS   B 91  ? 0.2232 0.1663 0.2344 -0.0053 0.0332  0.0101  91  HIS   B CG  
5735 N ND1 . HIS   B 91  ? 0.2627 0.1703 0.3071 -0.0008 0.0456  -0.0061 91  HIS   B ND1 
5736 C CD2 . HIS   B 91  ? 0.2490 0.1910 0.3111 0.0202  0.0141  0.0494  91  HIS   B CD2 
5737 C CE1 . HIS   B 91  ? 0.2632 0.1927 0.3357 0.0222  0.0417  0.0070  91  HIS   B CE1 
5738 N NE2 . HIS   B 91  ? 0.2727 0.2045 0.3407 0.0277  0.0233  0.0600  91  HIS   B NE2 
5746 N N   . CYS   B 92  ? 0.1538 0.1468 0.1031 -0.0296 -0.0073 -0.0120 92  CYS   B N   
5747 C CA  . CYS   B 92  ? 0.1694 0.1412 0.0957 -0.0264 -0.0091 0.0102  92  CYS   B CA  
5748 C C   . CYS   B 92  ? 0.1583 0.1405 0.0970 -0.0173 -0.0019 -0.0073 92  CYS   B C   
5749 O O   . CYS   B 92  ? 0.1663 0.1478 0.1327 -0.0160 -0.0002 -0.0012 92  CYS   B O   
5750 C CB  . CYS   B 92  ? 0.1661 0.1514 0.0948 -0.0146 -0.0082 -0.0040 92  CYS   B CB  
5751 S SG  . CYS   B 92  ? 0.1552 0.1486 0.1293 -0.0135 -0.0154 0.0083  92  CYS   B SG  
5757 N N   . LEU   B 93  ? 0.1484 0.1364 0.1116 -0.0193 -0.0073 0.0002  93  LEU   B N   
5758 C CA  . LEU   B 93  ? 0.1565 0.1461 0.0898 -0.0097 -0.0175 0.0021  93  LEU   B CA  
5759 C C   . LEU   B 93  ? 0.1420 0.1469 0.0892 0.0002  -0.0120 0.0216  93  LEU   B C   
5760 O O   . LEU   B 93  ? 0.1583 0.1369 0.1317 -0.0024 -0.0069 -0.0040 93  LEU   B O   
5761 C CB  . LEU   B 93  ? 0.1558 0.1343 0.1293 0.0018  -0.0110 0.0054  93  LEU   B CB  
5762 C CG  . LEU   B 93  ? 0.1454 0.1546 0.1523 -0.0097 -0.0133 0.0206  93  LEU   B CG  
5763 C CD1 . LEU   B 93  ? 0.1394 0.1663 0.1638 0.0054  0.0008  0.0096  93  LEU   B CD1 
5764 C CD2 . LEU   B 93  ? 0.1547 0.1546 0.1640 0.0049  -0.0092 0.0161  93  LEU   B CD2 
5776 N N   . HIS   B 94  ? 0.1492 0.1373 0.1022 -0.0007 -0.0104 0.0117  94  HIS   B N   
5777 C CA  . HIS   B 94  ? 0.1530 0.1298 0.0896 -0.0014 -0.0074 0.0004  94  HIS   B CA  
5778 C C   . HIS   B 94  ? 0.1463 0.1311 0.1493 -0.0033 -0.0102 0.0041  94  HIS   B C   
5779 O O   . HIS   B 94  ? 0.1490 0.1426 0.1738 -0.0011 0.0090  -0.0087 94  HIS   B O   
5780 C CB  . HIS   B 94  ? 0.1543 0.1371 0.1240 0.0044  -0.0138 0.0018  94  HIS   B CB  
5781 C CG  . HIS   B 94  ? 0.1537 0.1315 0.1313 -0.0107 -0.0261 -0.0030 94  HIS   B CG  
5782 N ND1 . HIS   B 94  ? 0.1639 0.1376 0.1445 -0.0001 -0.0267 0.0013  94  HIS   B ND1 
5783 C CD2 . HIS   B 94  ? 0.1522 0.1385 0.1376 -0.0023 -0.0071 -0.0033 94  HIS   B CD2 
5784 C CE1 . HIS   B 94  ? 0.1619 0.1358 0.1516 -0.0133 -0.0091 0.0025  94  HIS   B CE1 
5785 N NE2 . HIS   B 94  ? 0.1437 0.1534 0.1530 -0.0087 -0.0085 -0.0015 94  HIS   B NE2 
5793 N N   . VAL   B 95  ? 0.1445 0.1301 0.1466 -0.0014 -0.0052 -0.0011 95  VAL   B N   
5794 C CA  . VAL   B 95  ? 0.1455 0.1457 0.1165 0.0012  -0.0081 0.0162  95  VAL   B CA  
5795 C C   . VAL   B 95  ? 0.1684 0.1490 0.0957 -0.0009 0.0161  0.0179  95  VAL   B C   
5796 O O   . VAL   B 95  ? 0.1636 0.1410 0.1501 0.0046  0.0099  0.0220  95  VAL   B O   
5797 C CB  . VAL   B 95  ? 0.1590 0.1407 0.1342 0.0000  -0.0132 0.0215  95  VAL   B CB  
5798 C CG1 . VAL   B 95  ? 0.1579 0.1686 0.1686 -0.0044 -0.0035 0.0279  95  VAL   B CG1 
5799 C CG2 . VAL   B 95  ? 0.1678 0.1406 0.1319 0.0044  -0.0226 0.0028  95  VAL   B CG2 
5809 N N   . VAL   B 96  ? 0.1745 0.1588 0.0995 0.0049  0.0103  0.0192  96  VAL   B N   
5810 C CA  . VAL   B 96  ? 0.1828 0.1650 0.0807 0.0122  0.0150  0.0303  96  VAL   B CA  
5811 C C   . VAL   B 96  ? 0.1883 0.1669 0.1459 0.0114  0.0281  0.0256  96  VAL   B C   
5812 O O   . VAL   B 96  ? 0.1847 0.1620 0.1726 0.0011  0.0309  0.0069  96  VAL   B O   
5813 C CB  . VAL   B 96  ? 0.1939 0.2021 0.0927 0.0104  0.0043  0.0177  96  VAL   B CB  
5814 C CG1 . VAL   B 96  ? 0.1920 0.2227 0.1046 0.0201  0.0052  0.0007  96  VAL   B CG1 
5815 C CG2 . VAL   B 96  ? 0.2028 0.1875 0.1182 0.0042  0.0030  0.0011  96  VAL   B CG2 
5825 N N   . GLY   B 97  ? 0.1913 0.1670 0.1369 0.0071  0.0047  0.0261  97  GLY   B N   
5826 C CA  . GLY   B 97  ? 0.2155 0.1680 0.1569 -0.0014 0.0031  0.0297  97  GLY   B CA  
5827 C C   . GLY   B 97  ? 0.2491 0.1683 0.1698 0.0090  0.0050  0.0256  97  GLY   B C   
5828 O O   . GLY   B 97  ? 0.2780 0.1743 0.1605 0.0075  -0.0041 0.0137  97  GLY   B O   
5832 N N   . PRO   B 98  ? 0.2735 0.1883 0.1852 0.0094  0.0550  0.0350  98  PRO   B N   
5833 C CA  . PRO   B 98  ? 0.2902 0.2036 0.2020 0.0300  0.0526  0.0420  98  PRO   B CA  
5834 C C   . PRO   B 98  ? 0.3112 0.2042 0.1828 0.0547  0.0709  0.0556  98  PRO   B C   
5835 O O   . PRO   B 98  ? 0.2884 0.1870 0.2036 0.0446  0.0732  0.0573  98  PRO   B O   
5836 C CB  . PRO   B 98  ? 0.2848 0.2222 0.2128 0.0292  0.0792  0.0667  98  PRO   B CB  
5837 C CG  . PRO   B 98  ? 0.2782 0.2041 0.2316 0.0252  0.0693  0.0773  98  PRO   B CG  
5838 C CD  . PRO   B 98  ? 0.2658 0.1898 0.2336 0.0139  0.0744  0.0706  98  PRO   B CD  
5846 N N   . ASN   B 99  ? 0.3309 0.2382 0.2006 0.0834  0.0814  0.0476  99  ASN   B N   
5847 C CA  . ASN   B 99  ? 0.3598 0.2562 0.1825 0.1005  0.0626  0.0820  99  ASN   B CA  
5848 C C   . ASN   B 99  ? 0.3783 0.2977 0.2125 0.1080  0.0977  0.1146  99  ASN   B C   
5849 O O   . ASN   B 99  ? 0.3920 0.3162 0.2287 0.1176  0.1101  0.1211  99  ASN   B O   
5850 C CB  . ASN   B 99  ? 0.3658 0.2484 0.1902 0.1011  0.0448  0.0586  99  ASN   B CB  
5851 C CG  . ASN   B 99  ? 0.3772 0.2470 0.2121 0.0881  0.0384  0.0430  99  ASN   B CG  
5852 O OD1 . ASN   B 99  ? 0.3765 0.2460 0.2426 0.0937  0.0476  0.0549  99  ASN   B OD1 
5853 N ND2 . ASN   B 99  ? 0.3683 0.2489 0.2199 0.0948  0.0214  0.0241  99  ASN   B ND2 
5860 N N   . VAL   B 100 ? 0.3960 0.3166 0.2989 0.0806  0.1049  0.1362  100 VAL   B N   
5861 C CA  . VAL   B 100 ? 0.4280 0.3385 0.3742 0.0650  0.0840  0.1642  100 VAL   B CA  
5862 C C   . VAL   B 100 ? 0.4651 0.3575 0.3489 0.0589  0.0733  0.1780  100 VAL   B C   
5863 O O   . VAL   B 100 ? 0.4765 0.3757 0.3627 0.0537  0.1096  0.1650  100 VAL   B O   
5864 C CB  . VAL   B 100 ? 0.4269 0.3426 0.4628 0.0283  0.0839  0.1886  100 VAL   B CB  
5865 C CG1 . VAL   B 100 ? 0.4344 0.3478 0.4918 0.0242  0.0800  0.1952  100 VAL   B CG1 
5866 C CG2 . VAL   B 100 ? 0.4228 0.3469 0.4951 0.0154  0.0844  0.1967  100 VAL   B CG2 
5876 N N   A ASN   B 101 ? 0.4798 0.3635 0.3506 0.0591  0.0452  0.1710  101 ASN   B N   
5877 N N   B ASN   B 101 ? 0.4769 0.3625 0.3515 0.0612  0.0462  0.1652  101 ASN   B N   
5878 C CA  A ASN   B 101 ? 0.4988 0.3759 0.3636 0.0538  0.0243  0.1564  101 ASN   B CA  
5879 C CA  B ASN   B 101 ? 0.4926 0.3731 0.3633 0.0592  0.0253  0.1472  101 ASN   B CA  
5880 C C   A ASN   B 101 ? 0.5287 0.4138 0.4066 0.0446  0.0236  0.1384  101 ASN   B C   
5881 C C   B ASN   B 101 ? 0.5201 0.4082 0.4000 0.0517  0.0218  0.1331  101 ASN   B C   
5882 O O   A ASN   B 101 ? 0.5281 0.4185 0.4352 0.0480  0.0291  0.1170  101 ASN   B O   
5883 O O   B ASN   B 101 ? 0.5192 0.4125 0.4242 0.0563  0.0265  0.1141  101 ASN   B O   
5884 C CB  A ASN   B 101 ? 0.4912 0.3608 0.3659 0.0518  0.0113  0.1293  101 ASN   B CB  
5885 C CB  B ASN   B 101 ? 0.4840 0.3577 0.3657 0.0589  0.0146  0.1165  101 ASN   B CB  
5886 C CG  A ASN   B 101 ? 0.4826 0.3457 0.3659 0.0525  0.0012  0.1136  101 ASN   B CG  
5887 C CG  B ASN   B 101 ? 0.4747 0.3420 0.3646 0.0613  0.0049  0.0991  101 ASN   B CG  
5888 O OD1 A ASN   B 101 ? 0.4815 0.3404 0.3758 0.0503  0.0099  0.1096  101 ASN   B OD1 
5889 O OD1 B ASN   B 101 ? 0.4730 0.3374 0.3731 0.0601  0.0134  0.0945  101 ASN   B OD1 
5890 N ND2 A ASN   B 101 ? 0.4777 0.3373 0.3507 0.0560  -0.0084 0.1089  101 ASN   B ND2 
5891 N ND2 B ASN   B 101 ? 0.4699 0.3334 0.3502 0.0648  -0.0048 0.0942  101 ASN   B ND2 
5904 N N   A LYS   B 102 ? 0.5578 0.4485 0.4363 0.0311  0.0250  0.1265  102 LYS   B N   
5905 N N   B LYS   B 102 ? 0.5479 0.4420 0.4273 0.0384  0.0207  0.1222  102 LYS   B N   
5906 C CA  A LYS   B 102 ? 0.5842 0.4864 0.4603 0.0146  0.0281  0.1087  102 LYS   B CA  
5907 C CA  B LYS   B 102 ? 0.5736 0.4792 0.4512 0.0214  0.0206  0.1057  102 LYS   B CA  
5908 C C   A LYS   B 102 ? 0.5924 0.4955 0.4391 0.0174  0.0341  0.1359  102 LYS   B C   
5909 C C   B LYS   B 102 ? 0.5810 0.4881 0.4371 0.0215  0.0278  0.1312  102 LYS   B C   
5910 O O   A LYS   B 102 ? 0.5987 0.4957 0.4271 0.0164  0.0246  0.1444  102 LYS   B O   
5911 O O   B LYS   B 102 ? 0.5869 0.4880 0.4283 0.0206  0.0189  0.1373  102 LYS   B O   
5912 C CB  A LYS   B 102 ? 0.5988 0.5124 0.5080 -0.0038 0.0359  0.0603  102 LYS   B CB  
5913 C CB  B LYS   B 102 ? 0.5886 0.5052 0.4941 0.0051  0.0239  0.0590  102 LYS   B CB  
5914 C CG  A LYS   B 102 ? 0.6107 0.5347 0.5506 -0.0184 0.0446  0.0160  102 LYS   B CG  
5915 C CG  B LYS   B 102 ? 0.6009 0.5282 0.5346 -0.0073 0.0277  0.0167  102 LYS   B CG  
5916 C CD  A LYS   B 102 ? 0.6218 0.5532 0.5945 -0.0289 0.0534  -0.0178 102 LYS   B CD  
5917 C CD  B LYS   B 102 ? 0.6124 0.5475 0.5802 -0.0165 0.0332  -0.0161 102 LYS   B CD  
5918 C CE  A LYS   B 102 ? 0.6296 0.5654 0.6245 -0.0369 0.0601  -0.0429 102 LYS   B CE  
5919 C CE  B LYS   B 102 ? 0.6204 0.5608 0.6131 -0.0235 0.0368  -0.0405 102 LYS   B CE  
5920 N NZ  A LYS   B 102 ? 0.6345 0.5729 0.6436 -0.0397 0.0630  -0.0571 102 LYS   B NZ  
5921 N NZ  B LYS   B 102 ? 0.6257 0.5694 0.6359 -0.0263 0.0382  -0.0546 102 LYS   B NZ  
5948 N N   A GLY   B 103 ? 0.5915 0.5012 0.4476 0.0225  0.0501  0.1426  103 GLY   B N   
5949 N N   B GLY   B 103 ? 0.5802 0.4935 0.4480 0.0234  0.0438  0.1401  103 GLY   B N   
5950 C CA  A GLY   B 103 ? 0.5900 0.5048 0.4650 0.0297  0.0672  0.1386  103 GLY   B CA  
5951 C CA  B GLY   B 103 ? 0.5789 0.4973 0.4678 0.0273  0.0599  0.1380  103 GLY   B CA  
5952 C C   A GLY   B 103 ? 0.5854 0.5043 0.4716 0.0371  0.0836  0.1320  103 GLY   B C   
5953 C C   B GLY   B 103 ? 0.5751 0.4976 0.4740 0.0313  0.0758  0.1331  103 GLY   B C   
5954 O O   A GLY   B 103 ? 0.5891 0.5077 0.4766 0.0371  0.0892  0.1401  103 GLY   B O   
5955 O O   B GLY   B 103 ? 0.5776 0.5005 0.4803 0.0310  0.0786  0.1439  103 GLY   B O   
5962 N N   A GLU   B 104 ? 0.5740 0.4966 0.4617 0.0434  0.0931  0.1106  104 GLU   B N   
5963 N N   B GLU   B 104 ? 0.5658 0.4908 0.4631 0.0342  0.0876  0.1100  104 GLU   B N   
5964 C CA  A GLU   B 104 ? 0.5614 0.4882 0.4554 0.0526  0.0952  0.0853  104 GLU   B CA  
5965 C CA  B GLU   B 104 ? 0.5557 0.4837 0.4542 0.0400  0.0928  0.0836  104 GLU   B CA  
5966 C C   A GLU   B 104 ? 0.5613 0.4890 0.4689 0.0431  0.1364  0.0915  104 GLU   B C   
5967 C C   B GLU   B 104 ? 0.5581 0.4868 0.4681 0.0368  0.1347  0.0897  104 GLU   B C   
5968 O O   A GLU   B 104 ? 0.5617 0.4892 0.4819 0.0401  0.1391  0.0956  104 GLU   B O   
5969 O O   B GLU   B 104 ? 0.5579 0.4868 0.4812 0.0336  0.1368  0.0919  104 GLU   B O   
5970 C CB  A GLU   B 104 ? 0.5528 0.4805 0.4402 0.0708  0.0567  0.0473  104 GLU   B CB  
5971 C CB  B GLU   B 104 ? 0.5475 0.4754 0.4362 0.0490  0.0568  0.0444  104 GLU   B CB  
5972 C CG  A GLU   B 104 ? 0.5441 0.4738 0.4229 0.0899  0.0163  0.0097  104 GLU   B CG  
5973 C CG  B GLU   B 104 ? 0.5391 0.4677 0.4162 0.0593  0.0193  0.0060  104 GLU   B CG  
5974 C CD  A GLU   B 104 ? 0.5387 0.4683 0.4075 0.1054  -0.0192 -0.0201 104 GLU   B CD  
5975 C CD  B GLU   B 104 ? 0.5338 0.4611 0.3971 0.0675  -0.0137 -0.0245 104 GLU   B CD  
5976 O OE1 A GLU   B 104 ? 0.5337 0.4600 0.3760 0.1159  -0.0207 -0.0383 104 GLU   B OE1 
5977 O OE1 B GLU   B 104 ? 0.5295 0.4537 0.3714 0.0731  -0.0187 -0.0432 104 GLU   B OE1 
5978 O OE2 A GLU   B 104 ? 0.5356 0.4702 0.3991 0.1089  -0.0452 -0.0313 104 GLU   B OE2 
5979 O OE2 B GLU   B 104 ? 0.5306 0.4613 0.3827 0.0686  -0.0357 -0.0359 104 GLU   B OE2 
5992 N N   . ASP   B 105 ? 0.5506 0.4815 0.4521 0.0400  0.1736  0.0912  105 ASP   B N   
5993 C CA  . ASP   B 105 ? 0.5506 0.4800 0.4664 0.0330  0.2238  0.0702  105 ASP   B CA  
5994 C C   . ASP   B 105 ? 0.5228 0.4412 0.4268 0.0156  0.2498  0.0596  105 ASP   B C   
5995 O O   . ASP   B 105 ? 0.5148 0.4337 0.4103 0.0234  0.2655  0.0671  105 ASP   B O   
5996 C CB  . ASP   B 105 ? 0.5670 0.5087 0.5395 0.0486  0.2426  0.0486  105 ASP   B CB  
5997 C CG  . ASP   B 105 ? 0.5855 0.5397 0.6265 0.0535  0.2538  0.0397  105 ASP   B CG  
5998 O OD1 . ASP   B 105 ? 0.5864 0.5425 0.6403 0.0497  0.2727  0.0533  105 ASP   B OD1 
5999 O OD2 . ASP   B 105 ? 0.5928 0.5479 0.6764 0.0610  0.2462  0.0260  105 ASP   B OD2 
6005 N N   . ILE   B 106 ? 0.4957 0.4058 0.4214 0.0002  0.2415  0.0508  106 ILE   B N   
6006 C CA  . ILE   B 106 ? 0.4656 0.3727 0.4202 -0.0162 0.2384  0.0317  106 ILE   B CA  
6007 C C   . ILE   B 106 ? 0.4131 0.3562 0.3851 -0.0157 0.2332  0.0103  106 ILE   B C   
6008 O O   . ILE   B 106 ? 0.4092 0.3231 0.3977 -0.0254 0.2251  0.0199  106 ILE   B O   
6009 C CB  . ILE   B 106 ? 0.4827 0.3579 0.4328 -0.0279 0.2477  0.0354  106 ILE   B CB  
6010 C CG1 . ILE   B 106 ? 0.4936 0.3550 0.4259 -0.0138 0.2292  0.0224  106 ILE   B CG1 
6011 C CG2 . ILE   B 106 ? 0.4899 0.3652 0.4756 -0.0331 0.2507  0.0288  106 ILE   B CG2 
6012 C CD1 . ILE   B 106 ? 0.4965 0.3538 0.4087 -0.0040 0.2252  0.0243  106 ILE   B CD1 
6024 N N   A GLN   B 107 ? 0.3969 0.3730 0.4029 -0.0228 0.2112  0.0060  107 GLN   B N   
6025 N N   B GLN   B 107 ? 0.3985 0.3713 0.4007 -0.0217 0.2098  0.0059  107 GLN   B N   
6026 C CA  A GLN   B 107 ? 0.3829 0.3880 0.4083 -0.0245 0.1764  0.0061  107 GLN   B CA  
6027 C CA  B GLN   B 107 ? 0.3860 0.3845 0.4047 -0.0224 0.1747  0.0060  107 GLN   B CA  
6028 C C   A GLN   B 107 ? 0.3547 0.3618 0.3698 -0.0142 0.1511  -0.0032 107 GLN   B C   
6029 C C   B GLN   B 107 ? 0.3568 0.3606 0.3666 -0.0132 0.1520  -0.0025 107 GLN   B C   
6030 O O   A GLN   B 107 ? 0.3451 0.3660 0.3832 -0.0074 0.1302  -0.0265 107 GLN   B O   
6031 O O   B GLN   B 107 ? 0.3491 0.3659 0.3795 -0.0077 0.1334  -0.0230 107 GLN   B O   
6032 C CB  A GLN   B 107 ? 0.4093 0.4301 0.4845 -0.0256 0.1380  0.0038  107 GLN   B CB  
6033 C CB  B GLN   B 107 ? 0.4134 0.4231 0.4767 -0.0224 0.1357  0.0043  107 GLN   B CB  
6034 C CG  A GLN   B 107 ? 0.4354 0.4662 0.5505 -0.0214 0.1001  0.0049  107 GLN   B CG  
6035 C CG  B GLN   B 107 ? 0.4402 0.4564 0.5395 -0.0175 0.0965  0.0055  107 GLN   B CG  
6036 C CD  A GLN   B 107 ? 0.4550 0.5015 0.6026 -0.0234 0.0743  0.0100  107 GLN   B CD  
6037 C CD  B GLN   B 107 ? 0.4621 0.4870 0.5893 -0.0181 0.0683  0.0094  107 GLN   B CD  
6038 O OE1 A GLN   B 107 ? 0.4622 0.5059 0.6226 -0.0240 0.0717  0.0110  107 GLN   B OE1 
6039 O OE1 B GLN   B 107 ? 0.4686 0.4924 0.6069 -0.0192 0.0644  0.0115  107 GLN   B OE1 
6040 N NE2 A GLN   B 107 ? 0.4621 0.5065 0.6212 -0.0214 0.0617  0.0111  107 GLN   B NE2 
6041 N NE2 B GLN   B 107 ? 0.4687 0.4936 0.6073 -0.0153 0.0556  0.0089  107 GLN   B NE2 
6058 N N   . LEU   B 108 ? 0.3320 0.3341 0.3275 -0.0003 0.1414  0.0027  108 LEU   B N   
6059 C CA  . LEU   B 108 ? 0.2936 0.2923 0.2602 0.0138  0.1108  0.0298  108 LEU   B CA  
6060 C C   . LEU   B 108 ? 0.2243 0.2336 0.2444 0.0206  0.0735  0.0260  108 LEU   B C   
6061 O O   . LEU   B 108 ? 0.2138 0.2213 0.2314 0.0183  0.0657  0.0273  108 LEU   B O   
6062 C CB  . LEU   B 108 ? 0.3064 0.3191 0.2469 0.0179  0.1146  0.0555  108 LEU   B CB  
6063 C CG  . LEU   B 108 ? 0.3177 0.3548 0.2640 0.0290  0.1108  0.0448  108 LEU   B CG  
6064 C CD1 . LEU   B 108 ? 0.3333 0.3722 0.2769 0.0342  0.0996  0.0464  108 LEU   B CD1 
6065 C CD2 . LEU   B 108 ? 0.3271 0.3681 0.2770 0.0419  0.0815  0.0249  108 LEU   B CD2 
6078 N N   . LEU   B 109 ? 0.2024 0.2014 0.2429 0.0183  0.0536  0.0127  109 LEU   B N   
6079 C CA  . LEU   B 109 ? 0.1896 0.1686 0.2496 0.0092  0.0442  0.0236  109 LEU   B CA  
6080 C C   . LEU   B 109 ? 0.1705 0.1480 0.2411 -0.0016 0.0458  0.0257  109 LEU   B C   
6081 O O   . LEU   B 109 ? 0.1676 0.1520 0.2317 0.0059  0.0358  0.0420  109 LEU   B O   
6082 C CB  . LEU   B 109 ? 0.1927 0.1477 0.2487 0.0078  0.0235  0.0374  109 LEU   B CB  
6083 C CG  . LEU   B 109 ? 0.1864 0.1406 0.2454 -0.0023 0.0226  0.0252  109 LEU   B CG  
6084 C CD1 . LEU   B 109 ? 0.1766 0.1666 0.2343 0.0058  0.0202  0.0187  109 LEU   B CD1 
6085 C CD2 . LEU   B 109 ? 0.1950 0.1479 0.2565 -0.0036 0.0204  0.0296  109 LEU   B CD2 
6097 N N   . LYS   B 110 ? 0.1703 0.1449 0.2376 -0.0111 0.0326  0.0215  110 LYS   B N   
6098 C CA  . LYS   B 110 ? 0.1735 0.1349 0.2431 -0.0056 0.0384  0.0231  110 LYS   B CA  
6099 C C   . LYS   B 110 ? 0.1658 0.1343 0.2422 -0.0083 0.0445  0.0079  110 LYS   B C   
6100 O O   . LYS   B 110 ? 0.1593 0.1503 0.2541 -0.0082 0.0241  0.0046  110 LYS   B O   
6101 C CB  . LYS   B 110 ? 0.1744 0.1410 0.2607 -0.0008 0.0518  0.0278  110 LYS   B CB  
6102 C CG  . LYS   B 110 ? 0.1829 0.1383 0.2803 -0.0098 0.0118  0.0206  110 LYS   B CG  
6103 C CD  . LYS   B 110 ? 0.1771 0.1297 0.2928 -0.0172 0.0097  0.0211  110 LYS   B CD  
6104 C CE  . LYS   B 110 ? 0.1765 0.1549 0.3272 -0.0115 0.0228  -0.0022 110 LYS   B CE  
6105 N NZ  . LYS   B 110 ? 0.1793 0.1613 0.3273 -0.0031 0.0101  0.0160  110 LYS   B NZ  
6119 N N   . SER   B 111 ? 0.1713 0.1481 0.2505 -0.0081 0.0404  0.0045  111 SER   B N   
6120 C CA  . SER   B 111 ? 0.1841 0.1504 0.2358 -0.0010 0.0326  0.0120  111 SER   B CA  
6121 C C   . SER   B 111 ? 0.1736 0.1469 0.2125 -0.0016 0.0260  0.0094  111 SER   B C   
6122 O O   . SER   B 111 ? 0.1571 0.1573 0.2126 -0.0095 0.0161  0.0089  111 SER   B O   
6123 C CB  . SER   B 111 ? 0.1986 0.1797 0.2418 0.0001  0.0421  0.0298  111 SER   B CB  
6124 O OG  . SER   B 111 ? 0.2142 0.2069 0.2544 0.0053  0.0579  0.0396  111 SER   B OG  
6130 N N   . ALA   B 112 ? 0.1698 0.1401 0.2134 -0.0026 0.0401  0.0080  112 ALA   B N   
6131 C CA  . ALA   B 112 ? 0.1570 0.1517 0.1841 0.0006  0.0206  0.0095  112 ALA   B CA  
6132 C C   . ALA   B 112 ? 0.1388 0.1550 0.1929 -0.0032 0.0199  0.0122  112 ALA   B C   
6133 O O   . ALA   B 112 ? 0.1493 0.1592 0.2048 -0.0072 0.0145  -0.0050 112 ALA   B O   
6134 C CB  . ALA   B 112 ? 0.1754 0.1560 0.1942 0.0030  0.0107  0.0246  112 ALA   B CB  
6140 N N   . TYR   B 113 ? 0.1422 0.1394 0.2002 -0.0067 0.0216  0.0094  113 TYR   B N   
6141 C CA  . TYR   B 113 ? 0.1361 0.1416 0.1866 -0.0061 0.0264  0.0075  113 TYR   B CA  
6142 C C   . TYR   B 113 ? 0.1345 0.1396 0.2034 -0.0105 0.0177  0.0042  113 TYR   B C   
6143 O O   . TYR   B 113 ? 0.1415 0.1441 0.1902 -0.0074 0.0068  -0.0078 113 TYR   B O   
6144 C CB  . TYR   B 113 ? 0.1506 0.1247 0.2040 0.0062  0.0170  0.0058  113 TYR   B CB  
6145 C CG  . TYR   B 113 ? 0.1550 0.1328 0.2202 -0.0114 0.0170  0.0202  113 TYR   B CG  
6146 C CD1 . TYR   B 113 ? 0.1551 0.1363 0.2269 -0.0077 0.0240  0.0268  113 TYR   B CD1 
6147 C CD2 . TYR   B 113 ? 0.1656 0.1360 0.2199 -0.0079 0.0118  0.0140  113 TYR   B CD2 
6148 C CE1 . TYR   B 113 ? 0.1647 0.1459 0.2172 -0.0107 0.0143  0.0080  113 TYR   B CE1 
6149 C CE2 . TYR   B 113 ? 0.1665 0.1267 0.2116 -0.0048 0.0097  0.0118  113 TYR   B CE2 
6150 C CZ  . TYR   B 113 ? 0.1597 0.1408 0.2131 0.0030  0.0166  0.0208  113 TYR   B CZ  
6151 O OH  . TYR   B 113 ? 0.1797 0.1434 0.2404 0.0052  0.0204  0.0051  113 TYR   B OH  
6161 N N   . GLU   B 114 ? 0.1315 0.1335 0.2194 -0.0054 0.0115  0.0059  114 GLU   B N   
6162 C CA  . GLU   B 114 ? 0.1388 0.1363 0.2140 0.0028  0.0034  0.0067  114 GLU   B CA  
6163 C C   . GLU   B 114 ? 0.1439 0.1333 0.1997 0.0047  -0.0001 0.0064  114 GLU   B C   
6164 O O   . GLU   B 114 ? 0.1405 0.1348 0.2124 0.0019  -0.0052 0.0058  114 GLU   B O   
6165 C CB  . GLU   B 114 ? 0.1345 0.1377 0.2409 -0.0030 0.0239  0.0043  114 GLU   B CB  
6166 C CG  . GLU   B 114 ? 0.1361 0.1299 0.2500 -0.0076 0.0060  0.0004  114 GLU   B CG  
6167 C CD  . GLU   B 114 ? 0.1451 0.1315 0.2493 -0.0171 0.0135  0.0100  114 GLU   B CD  
6168 O OE1 . GLU   B 114 ? 0.1433 0.1527 0.2359 -0.0133 0.0221  0.0051  114 GLU   B OE1 
6169 O OE2 . GLU   B 114 ? 0.1539 0.1523 0.2612 -0.0250 0.0147  0.0028  114 GLU   B OE2 
6176 N N   . ASN   B 115 ? 0.1515 0.1355 0.1760 -0.0058 0.0008  -0.0020 115 ASN   B N   
6177 C CA  . ASN   B 115 ? 0.1481 0.1394 0.1521 -0.0180 0.0016  0.0032  115 ASN   B CA  
6178 C C   . ASN   B 115 ? 0.1429 0.1502 0.1642 -0.0146 -0.0053 -0.0016 115 ASN   B C   
6179 O O   . ASN   B 115 ? 0.1481 0.1463 0.1855 -0.0152 0.0038  0.0091  115 ASN   B O   
6180 C CB  . ASN   B 115 ? 0.1568 0.1500 0.1677 -0.0133 0.0026  0.0129  115 ASN   B CB  
6181 C CG  . ASN   B 115 ? 0.1610 0.1670 0.1539 -0.0013 -0.0013 0.0082  115 ASN   B CG  
6182 O OD1 . ASN   B 115 ? 0.2103 0.1732 0.2092 0.0005  0.0172  -0.0068 115 ASN   B OD1 
6183 N ND2 . ASN   B 115 ? 0.1579 0.1811 0.1777 -0.0090 0.0098  0.0272  115 ASN   B ND2 
6190 N N   . PHE   B 116 ? 0.1513 0.1474 0.1412 -0.0111 -0.0078 -0.0034 116 PHE   B N   
6191 C CA  . PHE   B 116 ? 0.1562 0.1456 0.1418 -0.0106 -0.0009 0.0047  116 PHE   B CA  
6192 C C   . PHE   B 116 ? 0.1539 0.1220 0.1578 -0.0145 0.0043  0.0102  116 PHE   B C   
6193 O O   . PHE   B 116 ? 0.1559 0.1344 0.1834 -0.0056 -0.0122 0.0119  116 PHE   B O   
6194 C CB  . PHE   B 116 ? 0.1369 0.1395 0.1423 -0.0097 -0.0061 0.0017  116 PHE   B CB  
6195 C CG  . PHE   B 116 ? 0.1287 0.1455 0.1477 -0.0083 -0.0042 0.0128  116 PHE   B CG  
6196 C CD1 . PHE   B 116 ? 0.1521 0.1457 0.1620 0.0027  -0.0056 0.0090  116 PHE   B CD1 
6197 C CD2 . PHE   B 116 ? 0.1466 0.1486 0.1533 -0.0174 -0.0046 -0.0054 116 PHE   B CD2 
6198 C CE1 . PHE   B 116 ? 0.1566 0.1466 0.1750 -0.0052 -0.0211 0.0017  116 PHE   B CE1 
6199 C CE2 . PHE   B 116 ? 0.1363 0.1487 0.1778 -0.0053 -0.0068 0.0099  116 PHE   B CE2 
6200 C CZ  . PHE   B 116 ? 0.1307 0.1532 0.1746 0.0005  -0.0150 0.0222  116 PHE   B CZ  
6210 N N   . ASN   B 117 ? 0.1591 0.1211 0.1803 -0.0067 -0.0071 0.0105  117 ASN   B N   
6211 C CA  . ASN   B 117 ? 0.1701 0.1275 0.1903 -0.0002 -0.0099 0.0106  117 ASN   B CA  
6212 C C   . ASN   B 117 ? 0.1665 0.1268 0.1978 -0.0029 -0.0155 0.0149  117 ASN   B C   
6213 O O   . ASN   B 117 ? 0.1639 0.1330 0.2372 -0.0099 -0.0365 0.0162  117 ASN   B O   
6214 C CB  . ASN   B 117 ? 0.1676 0.1298 0.2053 -0.0037 -0.0092 -0.0026 117 ASN   B CB  
6215 C CG  . ASN   B 117 ? 0.1516 0.1330 0.2231 -0.0013 -0.0078 -0.0043 117 ASN   B CG  
6216 O OD1 . ASN   B 117 ? 0.1726 0.1444 0.2306 -0.0215 -0.0085 -0.0133 117 ASN   B OD1 
6217 N ND2 . ASN   B 117 ? 0.1570 0.1300 0.2109 -0.0108 -0.0018 0.0014  117 ASN   B ND2 
6224 N N   . GLN   B 118 ? 0.1493 0.1282 0.2015 -0.0046 -0.0172 -0.0001 118 GLN   B N   
6225 C CA  . GLN   B 118 ? 0.1675 0.1361 0.2055 0.0025  -0.0197 0.0064  118 GLN   B CA  
6226 C C   . GLN   B 118 ? 0.1610 0.1370 0.2299 -0.0019 -0.0151 0.0021  118 GLN   B C   
6227 O O   . GLN   B 118 ? 0.1755 0.1390 0.2661 -0.0108 -0.0063 0.0150  118 GLN   B O   
6228 C CB  . GLN   B 118 ? 0.1880 0.1435 0.2084 -0.0071 -0.0158 0.0064  118 GLN   B CB  
6229 C CG  . GLN   B 118 ? 0.1906 0.1413 0.2021 0.0079  -0.0187 -0.0020 118 GLN   B CG  
6230 C CD  . GLN   B 118 ? 0.1897 0.1301 0.2143 0.0003  -0.0284 -0.0033 118 GLN   B CD  
6231 O OE1 . GLN   B 118 ? 0.1904 0.1391 0.2461 0.0036  -0.0019 0.0085  118 GLN   B OE1 
6232 N NE2 . GLN   B 118 ? 0.1997 0.1231 0.2371 -0.0089 -0.0219 0.0046  118 GLN   B NE2 
6241 N N   . HIS   B 119 ? 0.1647 0.1394 0.1802 -0.0144 -0.0173 0.0163  119 HIS   B N   
6242 C CA  . HIS   B 119 ? 0.1745 0.1555 0.1683 -0.0035 -0.0288 0.0145  119 HIS   B CA  
6243 C C   . HIS   B 119 ? 0.1812 0.1569 0.1558 0.0012  -0.0524 0.0186  119 HIS   B C   
6244 O O   . HIS   B 119 ? 0.1827 0.1545 0.1993 -0.0386 -0.0292 0.0123  119 HIS   B O   
6245 C CB  . HIS   B 119 ? 0.1789 0.1621 0.1729 -0.0004 -0.0253 0.0021  119 HIS   B CB  
6246 C CG  . HIS   B 119 ? 0.1778 0.1863 0.1972 0.0051  -0.0605 -0.0066 119 HIS   B CG  
6247 N ND1 . HIS   B 119 ? 0.1869 0.2011 0.2179 -0.0025 -0.0542 -0.0284 119 HIS   B ND1 
6248 C CD2 . HIS   B 119 ? 0.1854 0.2000 0.2054 0.0368  -0.0651 -0.0152 119 HIS   B CD2 
6249 C CE1 . HIS   B 119 ? 0.2124 0.2136 0.2168 0.0162  -0.0636 -0.0354 119 HIS   B CE1 
6250 N NE2 . HIS   B 119 ? 0.2139 0.2277 0.2173 0.0278  -0.0581 -0.0307 119 HIS   B NE2 
6258 N N   . GLU   B 120 ? 0.1998 0.1433 0.1758 -0.0143 -0.0518 0.0246  120 GLU   B N   
6259 C CA  . GLU   B 120 ? 0.2304 0.1666 0.1707 -0.0072 -0.0524 0.0366  120 GLU   B CA  
6260 C C   . GLU   B 120 ? 0.1956 0.1544 0.1689 -0.0226 -0.0494 0.0273  120 GLU   B C   
6261 O O   . GLU   B 120 ? 0.1909 0.1745 0.1884 -0.0282 -0.0523 0.0241  120 GLU   B O   
6262 C CB  . GLU   B 120 ? 0.2998 0.2085 0.2422 0.0127  -0.0926 0.0588  120 GLU   B CB  
6263 C CG  . GLU   B 120 ? 0.3615 0.2849 0.3553 0.0263  -0.1115 0.0767  120 GLU   B CG  
6264 C CD  . GLU   B 120 ? 0.4099 0.3706 0.4768 0.0337  -0.1156 0.0894  120 GLU   B CD  
6265 O OE1 . GLU   B 120 ? 0.4385 0.3851 0.5228 0.0222  -0.1018 0.1020  120 GLU   B OE1 
6266 O OE2 . GLU   B 120 ? 0.4372 0.3912 0.5441 0.0343  -0.1134 0.0771  120 GLU   B OE2 
6273 N N   . VAL   B 121 ? 0.1838 0.1518 0.1730 -0.0284 -0.0374 0.0215  121 VAL   B N   
6274 C CA  . VAL   B 121 ? 0.1779 0.1568 0.1473 -0.0229 -0.0327 0.0208  121 VAL   B CA  
6275 C C   . VAL   B 121 ? 0.1793 0.1620 0.1494 -0.0292 -0.0257 0.0200  121 VAL   B C   
6276 O O   . VAL   B 121 ? 0.1852 0.1602 0.1742 -0.0414 -0.0360 0.0205  121 VAL   B O   
6277 C CB  . VAL   B 121 ? 0.2065 0.2017 0.1587 -0.0071 -0.0437 0.0252  121 VAL   B CB  
6278 C CG1 . VAL   B 121 ? 0.2127 0.2136 0.2017 -0.0130 -0.0334 0.0172  121 VAL   B CG1 
6279 C CG2 . VAL   B 121 ? 0.2398 0.2361 0.1567 0.0031  -0.0258 0.0216  121 VAL   B CG2 
6289 N N   . LEU   B 122 ? 0.1750 0.1580 0.1424 -0.0227 -0.0266 0.0135  122 LEU   B N   
6290 C CA  . LEU   B 122 ? 0.1547 0.1695 0.1138 -0.0226 -0.0216 0.0157  122 LEU   B CA  
6291 C C   . LEU   B 122 ? 0.1481 0.1559 0.1349 -0.0338 -0.0276 0.0098  122 LEU   B C   
6292 O O   . LEU   B 122 ? 0.1567 0.1585 0.1813 -0.0341 -0.0368 0.0071  122 LEU   B O   
6293 C CB  . LEU   B 122 ? 0.1821 0.1824 0.1705 0.0010  -0.0421 0.0133  122 LEU   B CB  
6294 C CG  . LEU   B 122 ? 0.1666 0.1828 0.2008 -0.0139 -0.0166 -0.0021 122 LEU   B CG  
6295 C CD1 . LEU   B 122 ? 0.1756 0.1961 0.1934 -0.0220 -0.0273 -0.0038 122 LEU   B CD1 
6296 C CD2 . LEU   B 122 ? 0.1760 0.1821 0.1712 -0.0071 -0.0126 -0.0123 122 LEU   B CD2 
6308 N N   . LEU   B 123 ? 0.1500 0.1335 0.1231 -0.0300 -0.0295 0.0119  123 LEU   B N   
6309 C CA  . LEU   B 123 ? 0.1679 0.1415 0.1391 -0.0347 -0.0270 0.0030  123 LEU   B CA  
6310 C C   . LEU   B 123 ? 0.1589 0.1387 0.1169 -0.0299 -0.0290 0.0004  123 LEU   B C   
6311 O O   . LEU   B 123 ? 0.1646 0.1509 0.1141 -0.0301 -0.0177 0.0005  123 LEU   B O   
6312 C CB  . LEU   B 123 ? 0.1725 0.1575 0.1366 -0.0287 -0.0219 -0.0051 123 LEU   B CB  
6313 C CG  . LEU   B 123 ? 0.1636 0.1549 0.1490 -0.0190 -0.0148 0.0128  123 LEU   B CG  
6314 C CD1 . LEU   B 123 ? 0.1812 0.1582 0.1526 -0.0153 -0.0087 -0.0165 123 LEU   B CD1 
6315 C CD2 . LEU   B 123 ? 0.1774 0.1554 0.1636 -0.0235 -0.0078 0.0206  123 LEU   B CD2 
6327 N N   . ALA   B 124 ? 0.1621 0.1348 0.1185 -0.0096 -0.0279 0.0025  124 ALA   B N   
6328 C CA  . ALA   B 124 ? 0.1538 0.1387 0.1225 -0.0101 -0.0206 0.0038  124 ALA   B CA  
6329 C C   . ALA   B 124 ? 0.1477 0.1359 0.0862 -0.0167 -0.0126 -0.0014 124 ALA   B C   
6330 O O   . ALA   B 124 ? 0.1571 0.1414 0.1427 -0.0151 -0.0158 -0.0006 124 ALA   B O   
6331 C CB  . ALA   B 124 ? 0.1478 0.1483 0.1619 -0.0043 -0.0036 0.0039  124 ALA   B CB  
6337 N N   . PRO   B 125 ? 0.1560 0.1432 0.1180 -0.0192 -0.0124 0.0153  125 PRO   B N   
6338 C CA  . PRO   B 125 ? 0.1737 0.1431 0.1385 -0.0224 -0.0223 0.0326  125 PRO   B CA  
6339 C C   . PRO   B 125 ? 0.1656 0.1325 0.1766 -0.0156 -0.0117 0.0220  125 PRO   B C   
6340 O O   . PRO   B 125 ? 0.1569 0.1420 0.1914 -0.0045 -0.0037 0.0193  125 PRO   B O   
6341 C CB  . PRO   B 125 ? 0.1729 0.1712 0.1572 -0.0215 -0.0315 0.0318  125 PRO   B CB  
6342 C CG  . PRO   B 125 ? 0.1735 0.1753 0.1428 -0.0262 -0.0303 0.0238  125 PRO   B CG  
6343 C CD  . PRO   B 125 ? 0.1668 0.1614 0.0976 -0.0340 -0.0172 -0.0054 125 PRO   B CD  
6351 N N   . LEU   B 126 ? 0.1581 0.1384 0.2008 -0.0166 0.0129  0.0197  126 LEU   B N   
6352 C CA  . LEU   B 126 ? 0.1850 0.1371 0.2053 -0.0164 0.0135  0.0292  126 LEU   B CA  
6353 C C   . LEU   B 126 ? 0.1916 0.1465 0.1930 0.0041  0.0009  0.0279  126 LEU   B C   
6354 O O   . LEU   B 126 ? 0.1966 0.1801 0.2221 0.0202  -0.0098 -0.0111 126 LEU   B O   
6355 C CB  . LEU   B 126 ? 0.2024 0.1406 0.2413 -0.0176 0.0199  0.0319  126 LEU   B CB  
6356 C CG  . LEU   B 126 ? 0.2109 0.1519 0.2580 -0.0304 0.0160  -0.0025 126 LEU   B CG  
6357 C CD1 . LEU   B 126 ? 0.2205 0.1632 0.3157 -0.0287 0.0179  -0.0070 126 LEU   B CD1 
6358 C CD2 . LEU   B 126 ? 0.2155 0.1619 0.2430 -0.0353 0.0095  -0.0162 126 LEU   B CD2 
6370 N N   . LEU   B 127 ? 0.1820 0.1297 0.2079 -0.0049 0.0230  0.0120  127 LEU   B N   
6371 C CA  . LEU   B 127 ? 0.1783 0.1566 0.2022 -0.0064 0.0318  0.0255  127 LEU   B CA  
6372 C C   . LEU   B 127 ? 0.1582 0.1546 0.2069 -0.0051 0.0218  0.0167  127 LEU   B C   
6373 O O   . LEU   B 127 ? 0.1641 0.1583 0.2163 -0.0200 0.0111  0.0174  127 LEU   B O   
6374 C CB  . LEU   B 127 ? 0.1888 0.1484 0.2120 -0.0003 0.0206  0.0161  127 LEU   B CB  
6375 C CG  . LEU   B 127 ? 0.1988 0.1414 0.2082 0.0042  0.0293  0.0164  127 LEU   B CG  
6376 C CD1 . LEU   B 127 ? 0.2056 0.1436 0.2305 0.0175  0.0144  0.0135  127 LEU   B CD1 
6377 C CD2 . LEU   B 127 ? 0.2100 0.1635 0.2171 -0.0146 0.0287  0.0171  127 LEU   B CD2 
6389 N N   . SER   B 128 ? 0.1699 0.1475 0.2107 0.0019  0.0025  0.0138  128 SER   B N   
6390 C CA  . SER   B 128 ? 0.1772 0.1666 0.2135 0.0159  -0.0061 0.0264  128 SER   B CA  
6391 C C   . SER   B 128 ? 0.1914 0.1561 0.2595 0.0067  -0.0251 0.0333  128 SER   B C   
6392 O O   . SER   B 128 ? 0.2124 0.1597 0.3257 0.0027  -0.0215 0.0445  128 SER   B O   
6393 C CB  . SER   B 128 ? 0.1783 0.1801 0.2093 0.0048  0.0138  0.0437  128 SER   B CB  
6394 O OG  . SER   B 128 ? 0.1801 0.1848 0.2282 0.0124  0.0229  0.0376  128 SER   B OG  
6400 N N   . ALA   B 129 ? 0.2112 0.1520 0.2873 0.0271  -0.0029 0.0129  129 ALA   B N   
6401 C CA  . ALA   B 129 ? 0.2317 0.1780 0.3120 0.0363  -0.0069 0.0012  129 ALA   B CA  
6402 C C   . ALA   B 129 ? 0.2184 0.1786 0.2987 0.0282  0.0041  -0.0014 129 ALA   B C   
6403 O O   . ALA   B 129 ? 0.2119 0.1707 0.2842 0.0267  -0.0056 0.0087  129 ALA   B O   
6404 C CB  . ALA   B 129 ? 0.2573 0.2046 0.3553 0.0423  0.0120  -0.0066 129 ALA   B CB  
6410 N N   . GLY   B 130 ? 0.2279 0.1814 0.3018 0.0318  0.0022  -0.0034 130 GLY   B N   
6411 C CA  . GLY   B 130 ? 0.2257 0.1864 0.3076 0.0255  0.0288  0.0077  130 GLY   B CA  
6412 C C   . GLY   B 130 ? 0.2359 0.1849 0.2848 0.0242  0.0231  0.0234  130 GLY   B C   
6413 O O   . GLY   B 130 ? 0.2418 0.2023 0.3143 0.0212  0.0140  0.0333  130 GLY   B O   
6417 N N   A ILE   B 131 ? 0.2343 0.1913 0.2951 0.0355  0.0183  0.0137  131 ILE   B N   
6418 N N   B ILE   B 131 ? 0.2359 0.1921 0.2936 0.0326  0.0135  0.0122  131 ILE   B N   
6419 C CA  A ILE   B 131 ? 0.2586 0.2072 0.2945 0.0287  0.0088  0.0235  131 ILE   B CA  
6420 C CA  B ILE   B 131 ? 0.2595 0.2077 0.2918 0.0257  0.0007  0.0178  131 ILE   B CA  
6421 C C   A ILE   B 131 ? 0.2633 0.1980 0.2482 0.0217  0.0094  0.0286  131 ILE   B C   
6422 C C   B ILE   B 131 ? 0.2634 0.1989 0.2480 0.0214  0.0037  0.0235  131 ILE   B C   
6423 O O   A ILE   B 131 ? 0.2883 0.2160 0.2660 0.0186  0.0018  0.0375  131 ILE   B O   
6424 O O   B ILE   B 131 ? 0.2872 0.2163 0.2639 0.0204  -0.0065 0.0288  131 ILE   B O   
6425 C CB  A ILE   B 131 ? 0.2621 0.2298 0.3367 0.0237  -0.0048 0.0280  131 ILE   B CB  
6426 C CB  B ILE   B 131 ? 0.2638 0.2296 0.3297 0.0188  -0.0188 0.0186  131 ILE   B CB  
6427 C CG1 A ILE   B 131 ? 0.2691 0.2444 0.3597 -0.0042 -0.0068 0.0341  131 ILE   B CG1 
6428 C CG1 B ILE   B 131 ? 0.2688 0.2432 0.3487 -0.0073 -0.0303 0.0216  131 ILE   B CG1 
6429 C CG2 A ILE   B 131 ? 0.2671 0.2382 0.3534 0.0305  -0.0058 0.0209  131 ILE   B CG2 
6430 C CG2 B ILE   B 131 ? 0.2691 0.2385 0.3474 0.0238  -0.0181 0.0110  131 ILE   B CG2 
6431 C CD1 A ILE   B 131 ? 0.2787 0.2586 0.3857 -0.0140 -0.0124 0.0361  131 ILE   B CD1 
6432 C CD1 B ILE   B 131 ? 0.2772 0.2563 0.3684 -0.0150 -0.0391 0.0222  131 ILE   B CD1 
6455 N N   . PHE   B 132 ? 0.2542 0.1842 0.2285 0.0171  0.0175  0.0278  132 PHE   B N   
6456 C CA  . PHE   B 132 ? 0.2641 0.1912 0.2352 0.0052  0.0587  0.0267  132 PHE   B CA  
6457 C C   . PHE   B 132 ? 0.2862 0.2135 0.2614 0.0058  0.0643  0.0279  132 PHE   B C   
6458 O O   . PHE   B 132 ? 0.2991 0.2364 0.2824 -0.0009 0.0774  0.0276  132 PHE   B O   
6459 C CB  . PHE   B 132 ? 0.2401 0.1849 0.2217 0.0011  0.0561  0.0218  132 PHE   B CB  
6460 C CG  . PHE   B 132 ? 0.2179 0.1932 0.2198 0.0076  0.0315  0.0242  132 PHE   B CG  
6461 C CD1 . PHE   B 132 ? 0.2327 0.1912 0.2751 -0.0010 0.0249  0.0336  132 PHE   B CD1 
6462 C CD2 . PHE   B 132 ? 0.2181 0.1946 0.2063 0.0141  0.0250  0.0354  132 PHE   B CD2 
6463 C CE1 . PHE   B 132 ? 0.2313 0.2019 0.2748 -0.0031 0.0116  0.0308  132 PHE   B CE1 
6464 C CE2 . PHE   B 132 ? 0.2232 0.2076 0.2345 0.0165  0.0162  0.0352  132 PHE   B CE2 
6465 C CZ  . PHE   B 132 ? 0.2213 0.2056 0.2471 0.0087  0.0040  0.0445  132 PHE   B CZ  
6476 N N   . GLY   B 133 ? 0.2661 0.2042 0.2755 -0.0024 0.0406  0.0487  133 GLY   B N   
6477 C CA  . GLY   B 133 ? 0.2849 0.2136 0.2994 -0.0158 0.0330  0.0532  133 GLY   B CA  
6478 C C   . GLY   B 133 ? 0.2861 0.2214 0.3018 -0.0372 0.0486  0.0714  133 GLY   B C   
6479 O O   . GLY   B 133 ? 0.3075 0.2415 0.3473 -0.0571 0.0458  0.0706  133 GLY   B O   
6483 N N   . ALA   B 134 ? 0.2614 0.2121 0.2778 -0.0317 0.0470  0.0439  134 ALA   B N   
6484 C CA  . ALA   B 134 ? 0.2712 0.2132 0.2856 -0.0250 0.0497  0.0315  134 ALA   B CA  
6485 C C   . ALA   B 134 ? 0.2743 0.1918 0.2831 -0.0213 0.0477  0.0539  134 ALA   B C   
6486 O O   . ALA   B 134 ? 0.2746 0.2133 0.2899 -0.0024 0.0404  0.0425  134 ALA   B O   
6487 C CB  . ALA   B 134 ? 0.2737 0.2155 0.2913 -0.0182 0.0377  0.0243  134 ALA   B CB  
6493 N N   . ASP   B 135 ? 0.2894 0.1875 0.2983 -0.0172 0.0222  0.0588  135 ASP   B N   
6494 C CA  . ASP   B 135 ? 0.3024 0.1819 0.3245 -0.0171 0.0134  0.0555  135 ASP   B CA  
6495 C C   . ASP   B 135 ? 0.2724 0.1564 0.3033 -0.0119 0.0128  0.0499  135 ASP   B C   
6496 O O   . ASP   B 135 ? 0.2538 0.1617 0.3287 -0.0129 0.0195  0.0524  135 ASP   B O   
6497 C CB  . ASP   B 135 ? 0.3389 0.1902 0.3505 -0.0429 0.0160  0.0635  135 ASP   B CB  
6498 C CG  . ASP   B 135 ? 0.3650 0.1944 0.3998 -0.0685 0.0178  0.0593  135 ASP   B CG  
6499 O OD1 . ASP   B 135 ? 0.3735 0.1774 0.3967 -0.0479 0.0004  0.0547  135 ASP   B OD1 
6500 O OD2 . ASP   B 135 ? 0.3903 0.2452 0.4614 -0.0907 0.0257  0.0287  135 ASP   B OD2 
6505 N N   . PRO   B 136 ? 0.2572 0.1636 0.3146 0.0048  -0.0127 0.0321  136 PRO   B N   
6506 C CA  . PRO   B 136 ? 0.2326 0.1613 0.3155 0.0040  -0.0132 0.0170  136 PRO   B CA  
6507 C C   . PRO   B 136 ? 0.2011 0.1468 0.3206 0.0138  -0.0080 0.0143  136 PRO   B C   
6508 O O   . PRO   B 136 ? 0.1717 0.1529 0.3050 0.0044  -0.0121 0.0106  136 PRO   B O   
6509 C CB  . PRO   B 136 ? 0.2385 0.1735 0.3262 0.0177  -0.0125 -0.0017 136 PRO   B CB  
6510 C CG  . PRO   B 136 ? 0.2707 0.1950 0.3468 0.0241  0.0066  0.0047  136 PRO   B CG  
6511 C CD  . PRO   B 136 ? 0.2745 0.1824 0.3289 0.0288  0.0050  0.0270  136 PRO   B CD  
6519 N N   . ILE   B 137 ? 0.2141 0.1490 0.3290 0.0116  -0.0082 0.0162  137 ILE   B N   
6520 C CA  . ILE   B 137 ? 0.2200 0.1447 0.3314 0.0047  -0.0026 0.0207  137 ILE   B CA  
6521 C C   . ILE   B 137 ? 0.2128 0.1467 0.3123 -0.0014 0.0185  0.0214  137 ILE   B C   
6522 O O   . ILE   B 137 ? 0.1947 0.1408 0.3020 -0.0075 0.0143  0.0055  137 ILE   B O   
6523 C CB  . ILE   B 137 ? 0.2457 0.1490 0.3784 0.0017  -0.0111 0.0171  137 ILE   B CB  
6524 C CG1 . ILE   B 137 ? 0.2663 0.1640 0.4207 0.0117  -0.0070 0.0030  137 ILE   B CG1 
6525 C CG2 . ILE   B 137 ? 0.2545 0.1512 0.3854 -0.0279 -0.0140 0.0222  137 ILE   B CG2 
6526 C CD1 . ILE   B 137 ? 0.2905 0.1924 0.4715 0.0173  -0.0065 0.0098  137 ILE   B CD1 
6538 N N   . HIS   B 138 ? 0.2249 0.1582 0.3286 -0.0037 0.0369  0.0122  138 HIS   B N   
6539 C CA  . HIS   B 138 ? 0.2415 0.1567 0.3219 -0.0122 0.0486  0.0168  138 HIS   B CA  
6540 C C   . HIS   B 138 ? 0.2187 0.1388 0.3046 -0.0217 0.0472  0.0404  138 HIS   B C   
6541 O O   . HIS   B 138 ? 0.2082 0.1564 0.3255 -0.0025 0.0389  0.0353  138 HIS   B O   
6542 C CB  . HIS   B 138 ? 0.2761 0.1751 0.3282 -0.0284 0.0857  0.0225  138 HIS   B CB  
6543 C CG  . HIS   B 138 ? 0.3029 0.1940 0.3305 -0.0253 0.0979  0.0327  138 HIS   B CG  
6544 N ND1 . HIS   B 138 ? 0.3183 0.2249 0.3739 -0.0210 0.1073  0.0289  138 HIS   B ND1 
6545 C CD2 . HIS   B 138 ? 0.3183 0.2103 0.3203 -0.0278 0.1117  0.0246  138 HIS   B CD2 
6546 C CE1 . HIS   B 138 ? 0.3229 0.2209 0.3695 -0.0173 0.1164  0.0238  138 HIS   B CE1 
6547 N NE2 . HIS   B 138 ? 0.3218 0.2217 0.3262 -0.0148 0.1211  0.0128  138 HIS   B NE2 
6555 N N   . SER   B 139 ? 0.2121 0.1276 0.2924 -0.0034 0.0370  0.0141  139 SER   B N   
6556 C CA  . SER   B 139 ? 0.2020 0.1368 0.2612 -0.0130 0.0310  0.0186  139 SER   B CA  
6557 C C   . SER   B 139 ? 0.1730 0.1309 0.2433 -0.0081 0.0288  0.0030  139 SER   B C   
6558 O O   . SER   B 139 ? 0.1807 0.1332 0.2644 -0.0010 0.0123  0.0172  139 SER   B O   
6559 C CB  . SER   B 139 ? 0.2124 0.1534 0.2577 -0.0067 0.0189  0.0098  139 SER   B CB  
6560 O OG  . SER   B 139 ? 0.2234 0.1368 0.2592 -0.0033 -0.0083 0.0281  139 SER   B OG  
6566 N N   . LEU   B 140 ? 0.1776 0.1170 0.2467 -0.0099 0.0253  -0.0012 140 LEU   B N   
6567 C CA  . LEU   B 140 ? 0.1691 0.1254 0.2574 -0.0080 0.0236  0.0076  140 LEU   B CA  
6568 C C   . LEU   B 140 ? 0.1584 0.1285 0.2786 -0.0097 0.0090  -0.0089 140 LEU   B C   
6569 O O   . LEU   B 140 ? 0.1631 0.1451 0.2609 -0.0044 0.0022  0.0142  140 LEU   B O   
6570 C CB  . LEU   B 140 ? 0.1722 0.1370 0.2607 -0.0059 0.0326  0.0136  140 LEU   B CB  
6571 C CG  . LEU   B 140 ? 0.1735 0.1437 0.2606 -0.0104 0.0034  0.0197  140 LEU   B CG  
6572 C CD1 . LEU   B 140 ? 0.1898 0.1471 0.2747 -0.0239 0.0114  0.0142  140 LEU   B CD1 
6573 C CD2 . LEU   B 140 ? 0.1924 0.1639 0.2695 -0.0027 0.0124  0.0267  140 LEU   B CD2 
6585 N N   . ARG   B 141 ? 0.1668 0.1346 0.2904 -0.0129 0.0158  -0.0004 141 ARG   B N   
6586 C CA  . ARG   B 141 ? 0.1679 0.1374 0.3177 -0.0211 0.0279  0.0089  141 ARG   B CA  
6587 C C   . ARG   B 141 ? 0.1574 0.1272 0.3002 -0.0167 0.0176  0.0112  141 ARG   B C   
6588 O O   . ARG   B 141 ? 0.1690 0.1472 0.3078 -0.0164 0.0048  -0.0098 141 ARG   B O   
6589 C CB  . ARG   B 141 ? 0.1817 0.1548 0.3591 -0.0279 0.0398  0.0062  141 ARG   B CB  
6590 C CG  . ARG   B 141 ? 0.2351 0.1738 0.3796 -0.0256 0.0303  0.0103  141 ARG   B CG  
6591 C CD  . ARG   B 141 ? 0.2823 0.2166 0.3767 -0.0265 0.0153  -0.0129 141 ARG   B CD  
6592 N NE  . ARG   B 141 ? 0.3124 0.2130 0.3691 -0.0461 0.0298  -0.0305 141 ARG   B NE  
6593 C CZ  . ARG   B 141 ? 0.3322 0.2033 0.3260 -0.0446 0.0420  -0.0404 141 ARG   B CZ  
6594 N NH1 . ARG   B 141 ? 0.3492 0.1908 0.2991 -0.0388 0.0336  -0.0315 141 ARG   B NH1 
6595 N NH2 . ARG   B 141 ? 0.3449 0.2090 0.3523 -0.0261 0.0305  -0.0185 141 ARG   B NH2 
6609 N N   . VAL   B 142 ? 0.1654 0.1351 0.2864 -0.0087 0.0198  0.0066  142 VAL   B N   
6610 C CA  . VAL   B 142 ? 0.1521 0.1259 0.2816 -0.0016 0.0279  -0.0003 142 VAL   B CA  
6611 C C   . VAL   B 142 ? 0.1500 0.1311 0.2799 -0.0110 0.0160  -0.0028 142 VAL   B C   
6612 O O   . VAL   B 142 ? 0.1554 0.1315 0.2902 -0.0006 0.0112  0.0073  142 VAL   B O   
6613 C CB  . VAL   B 142 ? 0.1675 0.1544 0.2891 -0.0077 0.0326  0.0108  142 VAL   B CB  
6614 C CG1 . VAL   B 142 ? 0.1607 0.1536 0.3022 -0.0011 0.0215  -0.0010 142 VAL   B CG1 
6615 C CG2 . VAL   B 142 ? 0.1867 0.1677 0.2954 -0.0072 0.0262  0.0290  142 VAL   B CG2 
6625 N N   . CYS   B 143 ? 0.1449 0.1513 0.2457 -0.0123 0.0145  0.0152  143 CYS   B N   
6626 C CA  . CYS   B 143 ? 0.1465 0.1530 0.2475 -0.0100 0.0115  0.0037  143 CYS   B CA  
6627 C C   . CYS   B 143 ? 0.1406 0.1510 0.2534 -0.0124 0.0014  -0.0074 143 CYS   B C   
6628 O O   . CYS   B 143 ? 0.1499 0.1577 0.2588 0.0012  -0.0109 -0.0018 143 CYS   B O   
6629 C CB  . CYS   B 143 ? 0.1487 0.1560 0.2424 0.0022  -0.0111 0.0117  143 CYS   B CB  
6630 S SG  . CYS   B 143 ? 0.1603 0.1600 0.2445 -0.0078 0.0088  0.0105  143 CYS   B SG  
6636 N N   . VAL   B 144 ? 0.1504 0.1559 0.2630 -0.0149 -0.0077 -0.0074 144 VAL   B N   
6637 C CA  . VAL   B 144 ? 0.1719 0.1660 0.2834 -0.0170 -0.0238 -0.0177 144 VAL   B CA  
6638 C C   . VAL   B 144 ? 0.1593 0.1574 0.3097 -0.0057 -0.0261 0.0094  144 VAL   B C   
6639 O O   . VAL   B 144 ? 0.1565 0.1696 0.3456 -0.0053 -0.0231 0.0289  144 VAL   B O   
6640 C CB  . VAL   B 144 ? 0.1970 0.1882 0.3481 -0.0118 -0.0243 -0.0482 144 VAL   B CB  
6641 C CG1 . VAL   B 144 ? 0.2259 0.2280 0.3925 -0.0106 -0.0177 -0.0419 144 VAL   B CG1 
6642 C CG2 . VAL   B 144 ? 0.2084 0.1585 0.3456 -0.0043 -0.0402 -0.0640 144 VAL   B CG2 
6652 N N   . ASP   B 145 ? 0.1483 0.1533 0.3218 -0.0031 -0.0101 -0.0253 145 ASP   B N   
6653 C CA  . ASP   B 145 ? 0.1602 0.1528 0.3538 -0.0119 0.0023  -0.0067 145 ASP   B CA  
6654 C C   . ASP   B 145 ? 0.1585 0.1383 0.3431 -0.0077 0.0084  -0.0071 145 ASP   B C   
6655 O O   . ASP   B 145 ? 0.1670 0.1635 0.4016 -0.0191 0.0110  -0.0115 145 ASP   B O   
6656 C CB  . ASP   B 145 ? 0.1792 0.1619 0.4069 -0.0231 0.0105  0.0088  145 ASP   B CB  
6657 C CG  . ASP   B 145 ? 0.1937 0.1701 0.4604 -0.0227 0.0215  0.0042  145 ASP   B CG  
6658 O OD1 . ASP   B 145 ? 0.1864 0.1616 0.4426 -0.0239 -0.0225 0.0001  145 ASP   B OD1 
6659 O OD2 . ASP   B 145 ? 0.2236 0.1740 0.5058 -0.0355 0.0442  -0.0002 145 ASP   B OD2 
6664 N N   . THR   B 146 ? 0.1493 0.1430 0.3002 -0.0127 0.0138  -0.0043 146 THR   B N   
6665 C CA  . THR   B 146 ? 0.1530 0.1566 0.2743 -0.0160 0.0204  -0.0023 146 THR   B CA  
6666 C C   . THR   B 146 ? 0.1472 0.1555 0.2458 -0.0059 0.0053  0.0061  146 THR   B C   
6667 O O   . THR   B 146 ? 0.1557 0.1570 0.2488 -0.0031 -0.0014 0.0080  146 THR   B O   
6668 C CB  . THR   B 146 ? 0.1546 0.1563 0.2743 -0.0163 0.0248  -0.0023 146 THR   B CB  
6669 O OG1 . THR   B 146 ? 0.1502 0.1559 0.2869 -0.0111 0.0185  0.0106  146 THR   B OG1 
6670 C CG2 . THR   B 146 ? 0.1729 0.1544 0.2608 -0.0215 0.0058  -0.0183 146 THR   B CG2 
6678 N N   . VAL   B 147 ? 0.1552 0.1559 0.2127 -0.0026 0.0173  0.0081  147 VAL   B N   
6679 C CA  . VAL   B 147 ? 0.1502 0.1479 0.2070 -0.0174 -0.0038 0.0070  147 VAL   B CA  
6680 C C   . VAL   B 147 ? 0.1513 0.1463 0.2429 -0.0257 -0.0118 -0.0009 147 VAL   B C   
6681 O O   . VAL   B 147 ? 0.1678 0.1610 0.2533 -0.0214 -0.0330 0.0086  147 VAL   B O   
6682 C CB  . VAL   B 147 ? 0.1595 0.1551 0.1987 -0.0057 -0.0034 0.0112  147 VAL   B CB  
6683 C CG1 . VAL   B 147 ? 0.1592 0.1621 0.1857 -0.0147 0.0010  0.0077  147 VAL   B CG1 
6684 C CG2 . VAL   B 147 ? 0.1664 0.1511 0.2122 -0.0117 0.0040  0.0049  147 VAL   B CG2 
6694 N N   . ARG   B 148 ? 0.1547 0.1399 0.2394 -0.0070 -0.0143 0.0059  148 ARG   B N   
6695 C CA  . ARG   B 148 ? 0.1672 0.1494 0.2310 -0.0030 -0.0299 -0.0143 148 ARG   B CA  
6696 C C   . ARG   B 148 ? 0.1712 0.1539 0.2130 -0.0097 -0.0464 0.0039  148 ARG   B C   
6697 O O   . ARG   B 148 ? 0.1898 0.1922 0.2223 -0.0353 -0.0471 0.0146  148 ARG   B O   
6698 C CB  . ARG   B 148 ? 0.1696 0.1545 0.2487 -0.0047 -0.0352 -0.0152 148 ARG   B CB  
6699 C CG  . ARG   B 148 ? 0.1673 0.1672 0.2603 -0.0139 -0.0312 -0.0285 148 ARG   B CG  
6700 C CD  . ARG   B 148 ? 0.1641 0.2054 0.2684 0.0086  -0.0366 -0.0426 148 ARG   B CD  
6701 N NE  . ARG   B 148 ? 0.1752 0.2009 0.2496 0.0210  -0.0360 -0.0347 148 ARG   B NE  
6702 C CZ  . ARG   B 148 ? 0.1678 0.1883 0.2422 0.0124  -0.0285 -0.0269 148 ARG   B CZ  
6703 N NH1 . ARG   B 148 ? 0.1560 0.1880 0.2472 -0.0009 -0.0149 -0.0247 148 ARG   B NH1 
6704 N NH2 . ARG   B 148 ? 0.1950 0.1721 0.2528 0.0157  -0.0266 -0.0400 148 ARG   B NH2 
6718 N N   . THR   B 149 ? 0.1717 0.1472 0.2276 -0.0204 -0.0360 0.0049  149 THR   B N   
6719 C CA  . THR   B 149 ? 0.1779 0.1488 0.2149 -0.0256 -0.0370 0.0128  149 THR   B CA  
6720 C C   . THR   B 149 ? 0.1766 0.1484 0.1923 -0.0166 -0.0307 -0.0009 149 THR   B C   
6721 O O   . THR   B 149 ? 0.1769 0.1540 0.2090 -0.0152 -0.0262 0.0022  149 THR   B O   
6722 C CB  . THR   B 149 ? 0.1820 0.1428 0.2167 -0.0197 -0.0428 0.0030  149 THR   B CB  
6723 O OG1 . THR   B 149 ? 0.1809 0.1554 0.2090 -0.0234 -0.0487 0.0092  149 THR   B OG1 
6724 C CG2 . THR   B 149 ? 0.1970 0.1557 0.2360 -0.0173 -0.0323 0.0153  149 THR   B CG2 
6732 N N   . ASN   B 150 ? 0.1841 0.1378 0.1885 -0.0216 -0.0492 0.0094  150 ASN   B N   
6733 C CA  . ASN   B 150 ? 0.1991 0.1650 0.1721 -0.0293 -0.0417 -0.0050 150 ASN   B CA  
6734 C C   . ASN   B 150 ? 0.1772 0.1625 0.1584 -0.0189 -0.0342 -0.0042 150 ASN   B C   
6735 O O   . ASN   B 150 ? 0.1816 0.1624 0.1994 -0.0269 -0.0421 0.0008  150 ASN   B O   
6736 C CB  . ASN   B 150 ? 0.2242 0.2091 0.1935 -0.0391 -0.0655 0.0179  150 ASN   B CB  
6737 C CG  . ASN   B 150 ? 0.2477 0.2476 0.2433 -0.0396 -0.0624 0.0516  150 ASN   B CG  
6738 O OD1 . ASN   B 150 ? 0.2497 0.2671 0.2563 -0.0505 -0.0762 0.0426  150 ASN   B OD1 
6739 N ND2 . ASN   B 150 ? 0.2621 0.2691 0.3009 -0.0292 -0.0758 0.0999  150 ASN   B ND2 
6746 N N   . VAL   B 151 ? 0.1720 0.1600 0.1543 -0.0222 -0.0407 -0.0037 151 VAL   B N   
6747 C CA  . VAL   B 151 ? 0.1799 0.1588 0.1517 -0.0299 -0.0523 0.0213  151 VAL   B CA  
6748 C C   . VAL   B 151 ? 0.1812 0.1472 0.1596 -0.0473 -0.0358 0.0067  151 VAL   B C   
6749 O O   . VAL   B 151 ? 0.1866 0.1620 0.2108 -0.0325 -0.0312 -0.0063 151 VAL   B O   
6750 C CB  . VAL   B 151 ? 0.2027 0.1698 0.1814 -0.0181 -0.0407 0.0099  151 VAL   B CB  
6751 C CG1 . VAL   B 151 ? 0.2150 0.1750 0.2419 -0.0274 -0.0312 -0.0010 151 VAL   B CG1 
6752 C CG2 . VAL   B 151 ? 0.2153 0.1916 0.1493 -0.0115 -0.0226 0.0223  151 VAL   B CG2 
6762 N N   . TYR   B 152 ? 0.1678 0.1487 0.1694 -0.0345 -0.0321 0.0007  152 TYR   B N   
6763 C CA  . TYR   B 152 ? 0.1717 0.1658 0.1492 -0.0407 -0.0267 0.0014  152 TYR   B CA  
6764 C C   . TYR   B 152 ? 0.1688 0.1411 0.1399 -0.0253 -0.0259 -0.0049 152 TYR   B C   
6765 O O   . TYR   B 152 ? 0.1824 0.1487 0.1513 -0.0304 -0.0258 0.0072  152 TYR   B O   
6766 C CB  . TYR   B 152 ? 0.1898 0.1901 0.1296 -0.0425 -0.0166 0.0159  152 TYR   B CB  
6767 C CG  . TYR   B 152 ? 0.2059 0.2013 0.1313 -0.0627 -0.0149 0.0138  152 TYR   B CG  
6768 C CD1 . TYR   B 152 ? 0.2173 0.2128 0.1270 -0.0589 -0.0293 0.0098  152 TYR   B CD1 
6769 C CD2 . TYR   B 152 ? 0.2267 0.2163 0.1310 -0.0615 -0.0175 -0.0047 152 TYR   B CD2 
6770 C CE1 . TYR   B 152 ? 0.2323 0.2303 0.1393 -0.0526 -0.0370 0.0287  152 TYR   B CE1 
6771 C CE2 . TYR   B 152 ? 0.2431 0.2339 0.1359 -0.0581 -0.0405 -0.0038 152 TYR   B CE2 
6772 C CZ  . TYR   B 152 ? 0.2438 0.2538 0.1076 -0.0517 -0.0632 0.0293  152 TYR   B CZ  
6773 O OH  . TYR   B 152 ? 0.2678 0.2945 0.1890 -0.0392 -0.0641 0.0292  152 TYR   B OH  
6783 N N   . LEU   B 153 ? 0.1706 0.1413 0.1606 -0.0321 -0.0208 -0.0042 153 LEU   B N   
6784 C CA  . LEU   B 153 ? 0.1843 0.1406 0.1448 -0.0232 -0.0170 -0.0120 153 LEU   B CA  
6785 C C   . LEU   B 153 ? 0.1931 0.1388 0.1380 -0.0261 -0.0284 -0.0310 153 LEU   B C   
6786 O O   . LEU   B 153 ? 0.1894 0.1631 0.1664 -0.0204 -0.0150 -0.0257 153 LEU   B O   
6787 C CB  . LEU   B 153 ? 0.1775 0.1355 0.1748 -0.0252 -0.0017 -0.0022 153 LEU   B CB  
6788 C CG  . LEU   B 153 ? 0.1712 0.1510 0.2055 -0.0303 -0.0054 -0.0010 153 LEU   B CG  
6789 C CD1 . LEU   B 153 ? 0.1854 0.1663 0.2113 -0.0335 0.0054  0.0182  153 LEU   B CD1 
6790 C CD2 . LEU   B 153 ? 0.1678 0.1706 0.1932 -0.0273 -0.0135 0.0048  153 LEU   B CD2 
6802 N N   . ALA   B 154 ? 0.1781 0.1451 0.1567 -0.0080 -0.0223 -0.0211 154 ALA   B N   
6803 C CA  . ALA   B 154 ? 0.1870 0.1578 0.1790 -0.0047 -0.0159 -0.0296 154 ALA   B CA  
6804 C C   . ALA   B 154 ? 0.1961 0.1678 0.1802 0.0096  -0.0293 -0.0341 154 ALA   B C   
6805 O O   . ALA   B 154 ? 0.2409 0.1602 0.2183 0.0148  -0.0280 -0.0082 154 ALA   B O   
6806 C CB  . ALA   B 154 ? 0.1967 0.1629 0.2070 -0.0014 -0.0120 -0.0309 154 ALA   B CB  
6812 N N   . VAL   B 155 ? 0.1615 0.1597 0.1949 -0.0027 0.0081  -0.0175 155 VAL   B N   
6813 C CA  . VAL   B 155 ? 0.1651 0.1602 0.2319 0.0005  -0.0042 -0.0086 155 VAL   B CA  
6814 C C   . VAL   B 155 ? 0.1643 0.1562 0.2210 0.0010  -0.0121 -0.0337 155 VAL   B C   
6815 O O   . VAL   B 155 ? 0.1756 0.1683 0.2561 -0.0026 -0.0083 -0.0537 155 VAL   B O   
6816 C CB  . VAL   B 155 ? 0.1688 0.1742 0.2612 -0.0072 -0.0081 0.0054  155 VAL   B CB  
6817 C CG1 . VAL   B 155 ? 0.1846 0.1738 0.2652 -0.0038 -0.0172 0.0054  155 VAL   B CG1 
6818 C CG2 . VAL   B 155 ? 0.1604 0.1753 0.2969 -0.0125 -0.0023 0.0265  155 VAL   B CG2 
6828 N N   . PHE   B 156 ? 0.1576 0.1630 0.2452 -0.0013 -0.0050 -0.0134 156 PHE   B N   
6829 C CA  . PHE   B 156 ? 0.1481 0.1706 0.2819 0.0171  -0.0038 -0.0322 156 PHE   B CA  
6830 C C   . PHE   B 156 ? 0.1573 0.1760 0.3196 0.0149  -0.0086 -0.0477 156 PHE   B C   
6831 O O   . PHE   B 156 ? 0.1756 0.1986 0.3441 0.0245  0.0045  -0.0605 156 PHE   B O   
6832 C CB  . PHE   B 156 ? 0.1543 0.1745 0.2743 0.0065  -0.0145 -0.0196 156 PHE   B CB  
6833 C CG  . PHE   B 156 ? 0.1601 0.1868 0.2883 0.0061  -0.0120 -0.0084 156 PHE   B CG  
6834 C CD1 . PHE   B 156 ? 0.1717 0.2020 0.3104 0.0159  0.0031  0.0174  156 PHE   B CD1 
6835 C CD2 . PHE   B 156 ? 0.1651 0.2008 0.2902 0.0074  -0.0180 0.0045  156 PHE   B CD2 
6836 C CE1 . PHE   B 156 ? 0.1688 0.2177 0.3331 0.0061  -0.0043 0.0293  156 PHE   B CE1 
6837 C CE2 . PHE   B 156 ? 0.1692 0.2174 0.3165 0.0117  -0.0187 0.0101  156 PHE   B CE2 
6838 C CZ  . PHE   B 156 ? 0.1597 0.2163 0.3437 0.0152  -0.0146 0.0124  156 PHE   B CZ  
6848 N N   . ASP   B 157 ? 0.1659 0.1676 0.3640 0.0210  -0.0335 -0.0200 157 ASP   B N   
6849 C CA  . ASP   B 157 ? 0.1881 0.1696 0.3853 0.0109  -0.0272 -0.0403 157 ASP   B CA  
6850 C C   . ASP   B 157 ? 0.1726 0.1830 0.3809 0.0066  -0.0154 -0.0787 157 ASP   B C   
6851 O O   . ASP   B 157 ? 0.1488 0.1814 0.3834 0.0133  -0.0110 -0.0495 157 ASP   B O   
6852 C CB  . ASP   B 157 ? 0.2293 0.1865 0.4114 0.0040  -0.0562 -0.0132 157 ASP   B CB  
6853 C CG  . ASP   B 157 ? 0.3032 0.2062 0.4586 -0.0077 -0.0506 -0.0175 157 ASP   B CG  
6854 O OD1 . ASP   B 157 ? 0.3098 0.2132 0.4779 0.0141  -0.0405 -0.0152 157 ASP   B OD1 
6855 O OD2 . ASP   B 157 ? 0.3455 0.2237 0.4887 -0.0078 -0.0352 -0.0127 157 ASP   B OD2 
6860 N N   A LYS   B 158 ? 0.1753 0.2098 0.3865 0.0051  -0.0028 -0.1007 158 LYS   B N   
6861 N N   B LYS   B 158 ? 0.1832 0.2168 0.3809 0.0066  -0.0029 -0.0963 158 LYS   B N   
6862 C CA  A LYS   B 158 ? 0.1952 0.2310 0.3899 0.0045  -0.0006 -0.1130 158 LYS   B CA  
6863 C CA  B LYS   B 158 ? 0.2076 0.2455 0.3811 0.0080  0.0004  -0.1047 158 LYS   B CA  
6864 C C   A LYS   B 158 ? 0.1939 0.2104 0.4084 0.0037  -0.0220 -0.0979 158 LYS   B C   
6865 C C   B LYS   B 158 ? 0.2083 0.2333 0.3950 0.0078  -0.0179 -0.0870 158 LYS   B C   
6866 O O   A LYS   B 158 ? 0.1862 0.2014 0.4289 -0.0029 -0.0173 -0.1049 158 LYS   B O   
6867 O O   B LYS   B 158 ? 0.2038 0.2335 0.4092 0.0048  -0.0141 -0.0868 158 LYS   B O   
6868 C CB  A LYS   B 158 ? 0.2156 0.2787 0.3838 0.0044  0.0029  -0.1317 158 LYS   B CB  
6869 C CB  B LYS   B 158 ? 0.2295 0.2893 0.3773 0.0096  0.0051  -0.1229 158 LYS   B CB  
6870 C CG  A LYS   B 158 ? 0.2487 0.3266 0.3884 0.0074  0.0092  -0.1413 158 LYS   B CG  
6871 C CG  B LYS   B 158 ? 0.2602 0.3317 0.3815 0.0137  0.0141  -0.1347 158 LYS   B CG  
6872 C CD  A LYS   B 158 ? 0.2750 0.3728 0.4052 0.0020  0.0086  -0.1309 158 LYS   B CD  
6873 C CD  B LYS   B 158 ? 0.2866 0.3749 0.3980 0.0082  0.0147  -0.1282 158 LYS   B CD  
6874 C CE  A LYS   B 158 ? 0.2935 0.4036 0.4119 0.0068  0.0080  -0.1270 158 LYS   B CE  
6875 C CE  B LYS   B 158 ? 0.3054 0.4015 0.4055 0.0121  0.0149  -0.1257 158 LYS   B CE  
6876 N NZ  A LYS   B 158 ? 0.2926 0.4190 0.4130 0.0050  0.0091  -0.1225 158 LYS   B NZ  
6877 N NZ  B LYS   B 158 ? 0.3072 0.4161 0.4080 0.0106  0.0179  -0.1227 158 LYS   B NZ  
6904 N N   A ASN   B 159 ? 0.1950 0.1903 0.4381 0.0032  -0.0355 -0.0660 159 ASN   B N   
6905 N N   B ASN   B 159 ? 0.2084 0.2131 0.4213 0.0059  -0.0305 -0.0627 159 ASN   B N   
6906 C CA  A ASN   B 159 ? 0.2162 0.1812 0.4577 0.0166  -0.0509 -0.0510 159 ASN   B CA  
6907 C CA  B ASN   B 159 ? 0.2232 0.2005 0.4399 0.0159  -0.0460 -0.0514 159 ASN   B CA  
6908 C C   A ASN   B 159 ? 0.1967 0.1594 0.4459 0.0121  -0.0622 -0.0556 159 ASN   B C   
6909 C C   B ASN   B 159 ? 0.2017 0.1710 0.4374 0.0119  -0.0582 -0.0561 159 ASN   B C   
6910 O O   A ASN   B 159 ? 0.1866 0.1498 0.4578 0.0055  -0.0725 -0.0454 159 ASN   B O   
6911 O O   B ASN   B 159 ? 0.1933 0.1618 0.4485 0.0068  -0.0666 -0.0475 159 ASN   B O   
6912 C CB  A ASN   B 159 ? 0.2449 0.2051 0.4846 0.0340  -0.0600 -0.0463 159 ASN   B CB  
6913 C CB  B ASN   B 159 ? 0.2473 0.2218 0.4579 0.0326  -0.0538 -0.0465 159 ASN   B CB  
6914 C CG  A ASN   B 159 ? 0.2766 0.2301 0.5084 0.0439  -0.0772 -0.0463 159 ASN   B CG  
6915 C CG  B ASN   B 159 ? 0.2742 0.2495 0.4773 0.0428  -0.0693 -0.0437 159 ASN   B CG  
6916 O OD1 A ASN   B 159 ? 0.2918 0.2394 0.5152 0.0500  -0.0810 -0.0476 159 ASN   B OD1 
6917 O OD1 B ASN   B 159 ? 0.2860 0.2575 0.4762 0.0492  -0.0755 -0.0447 159 ASN   B OD1 
6918 N ND2 A ASN   B 159 ? 0.2736 0.2442 0.5232 0.0463  -0.0832 -0.0477 159 ASN   B ND2 
6919 N ND2 B ASN   B 159 ? 0.2703 0.2586 0.4941 0.0479  -0.0726 -0.0404 159 ASN   B ND2 
6932 N N   . LEU   B 160 ? 0.1938 0.1669 0.4364 0.0070  -0.0532 -0.0579 160 LEU   B N   
6933 C CA  . LEU   B 160 ? 0.1882 0.1766 0.3868 0.0088  -0.0412 -0.0297 160 LEU   B CA  
6934 C C   . LEU   B 160 ? 0.1711 0.1593 0.3646 -0.0079 -0.0199 -0.0372 160 LEU   B C   
6935 O O   . LEU   B 160 ? 0.1597 0.1602 0.3620 -0.0032 -0.0236 -0.0086 160 LEU   B O   
6936 C CB  . LEU   B 160 ? 0.1738 0.1785 0.3632 0.0096  -0.0377 -0.0147 160 LEU   B CB  
6937 C CG  . LEU   B 160 ? 0.1749 0.1904 0.3341 -0.0034 -0.0322 -0.0071 160 LEU   B CG  
6938 C CD1 . LEU   B 160 ? 0.1920 0.2163 0.3506 -0.0142 -0.0172 -0.0106 160 LEU   B CD1 
6939 C CD2 . LEU   B 160 ? 0.1749 0.1942 0.3287 0.0257  -0.0348 -0.0127 160 LEU   B CD2 
6952 N N   . TYR   B 161 ? 0.1679 0.1759 0.3805 -0.0148 0.0022  -0.0540 161 TYR   B N   
6953 C CA  . TYR   B 161 ? 0.1731 0.1780 0.3617 -0.0331 0.0147  -0.0521 161 TYR   B CA  
6954 C C   . TYR   B 161 ? 0.1827 0.1774 0.3386 -0.0144 0.0265  -0.0431 161 TYR   B C   
6955 O O   . TYR   B 161 ? 0.1890 0.1718 0.3098 -0.0220 0.0198  -0.0283 161 TYR   B O   
6956 C CB  . TYR   B 161 ? 0.1892 0.1822 0.3739 -0.0316 0.0331  -0.0559 161 TYR   B CB  
6957 C CG  . TYR   B 161 ? 0.2210 0.1865 0.3624 -0.0318 0.0442  -0.0558 161 TYR   B CG  
6958 C CD1 . TYR   B 161 ? 0.2186 0.1813 0.3573 -0.0341 0.0448  -0.0652 161 TYR   B CD1 
6959 C CD2 . TYR   B 161 ? 0.2405 0.1925 0.3476 -0.0173 0.0381  -0.0619 161 TYR   B CD2 
6960 C CE1 . TYR   B 161 ? 0.2439 0.2021 0.3485 -0.0483 0.0493  -0.0676 161 TYR   B CE1 
6961 C CE2 . TYR   B 161 ? 0.2649 0.2071 0.3615 -0.0351 0.0481  -0.0547 161 TYR   B CE2 
6962 C CZ  . TYR   B 161 ? 0.2635 0.2080 0.3499 -0.0568 0.0386  -0.0503 161 TYR   B CZ  
6963 O OH  . TYR   B 161 ? 0.2912 0.2461 0.3763 -0.0610 0.0365  -0.0562 161 TYR   B OH  
6973 N N   . ASP   B 162 ? 0.1850 0.1843 0.3612 -0.0111 0.0136  -0.0786 162 ASP   B N   
6974 C CA  . ASP   B 162 ? 0.1871 0.1894 0.3618 -0.0103 0.0105  -0.0743 162 ASP   B CA  
6975 C C   . ASP   B 162 ? 0.1910 0.1646 0.3515 -0.0179 -0.0047 -0.0482 162 ASP   B C   
6976 O O   . ASP   B 162 ? 0.1951 0.1682 0.3672 -0.0241 -0.0290 -0.0465 162 ASP   B O   
6977 C CB  . ASP   B 162 ? 0.2082 0.2036 0.3875 0.0009  -0.0042 -0.0958 162 ASP   B CB  
6978 C CG  . ASP   B 162 ? 0.2216 0.2296 0.4233 0.0105  -0.0048 -0.1040 162 ASP   B CG  
6979 O OD1 . ASP   B 162 ? 0.2255 0.2414 0.4158 -0.0035 0.0087  -0.0992 162 ASP   B OD1 
6980 O OD2 . ASP   B 162 ? 0.2333 0.2496 0.4484 0.0340  -0.0060 -0.1007 162 ASP   B OD2 
6985 N N   A LYS   B 163 ? 0.1978 0.1533 0.3413 -0.0139 -0.0195 -0.0305 163 LYS   B N   
6986 N N   B LYS   B 163 ? 0.1978 0.1564 0.3397 -0.0169 -0.0192 -0.0285 163 LYS   B N   
6987 C CA  A LYS   B 163 ? 0.2114 0.1656 0.3424 -0.0163 -0.0123 -0.0185 163 LYS   B CA  
6988 C CA  B LYS   B 163 ? 0.2111 0.1695 0.3391 -0.0208 -0.0139 -0.0141 163 LYS   B CA  
6989 C C   A LYS   B 163 ? 0.1788 0.1594 0.3271 -0.0251 -0.0183 -0.0052 163 LYS   B C   
6990 C C   B LYS   B 163 ? 0.1793 0.1607 0.3237 -0.0262 -0.0209 -0.0017 163 LYS   B C   
6991 O O   A LYS   B 163 ? 0.1779 0.1645 0.3408 -0.0292 -0.0188 0.0117  163 LYS   B O   
6992 O O   B LYS   B 163 ? 0.1787 0.1646 0.3352 -0.0283 -0.0241 0.0151  163 LYS   B O   
6993 C CB  A LYS   B 163 ? 0.2592 0.2021 0.3704 -0.0129 -0.0118 -0.0170 163 LYS   B CB  
6994 C CB  B LYS   B 163 ? 0.2570 0.2077 0.3663 -0.0213 -0.0137 -0.0105 163 LYS   B CB  
6995 C CG  A LYS   B 163 ? 0.3280 0.2603 0.4145 -0.0101 -0.0059 -0.0114 163 LYS   B CG  
6996 C CG  B LYS   B 163 ? 0.3216 0.2635 0.4087 -0.0190 -0.0094 -0.0032 163 LYS   B CG  
6997 C CD  A LYS   B 163 ? 0.3854 0.3093 0.4610 -0.0199 -0.0025 -0.0132 163 LYS   B CD  
6998 C CD  B LYS   B 163 ? 0.3763 0.3113 0.4553 -0.0285 -0.0073 -0.0023 163 LYS   B CD  
6999 C CE  A LYS   B 163 ? 0.4285 0.3576 0.4918 -0.0243 0.0030  -0.0140 163 LYS   B CE  
7000 C CE  B LYS   B 163 ? 0.4185 0.3575 0.4864 -0.0335 -0.0017 -0.0017 163 LYS   B CE  
7001 N NZ  A LYS   B 163 ? 0.4468 0.3641 0.5134 -0.0265 0.0045  -0.0163 163 LYS   B NZ  
7002 N NZ  B LYS   B 163 ? 0.4341 0.3628 0.5070 -0.0356 0.0003  -0.0033 163 LYS   B NZ  
7029 N N   . LEU   B 164 ? 0.1652 0.1529 0.3068 -0.0199 -0.0214 0.0046  164 LEU   B N   
7030 C CA  . LEU   B 164 ? 0.1643 0.1576 0.2914 -0.0118 -0.0302 0.0070  164 LEU   B CA  
7031 C C   . LEU   B 164 ? 0.1700 0.1608 0.3025 -0.0222 -0.0434 0.0140  164 LEU   B C   
7032 O O   . LEU   B 164 ? 0.1717 0.1851 0.3301 -0.0251 -0.0435 0.0176  164 LEU   B O   
7033 C CB  . LEU   B 164 ? 0.1459 0.1541 0.2630 -0.0093 -0.0113 0.0027  164 LEU   B CB  
7034 C CG  . LEU   B 164 ? 0.1713 0.1610 0.2769 -0.0107 -0.0065 0.0057  164 LEU   B CG  
7035 C CD1 . LEU   B 164 ? 0.1812 0.1603 0.2726 -0.0272 -0.0092 -0.0112 164 LEU   B CD1 
7036 C CD2 . LEU   B 164 ? 0.1863 0.1888 0.2951 -0.0058 -0.0023 0.0125  164 LEU   B CD2 
7049 N N   . VAL   B 165 ? 0.2066 0.1699 0.3279 -0.0362 -0.0598 0.0057  165 VAL   B N   
7050 C CA  . VAL   B 165 ? 0.2352 0.1871 0.3384 -0.0463 -0.0855 0.0005  165 VAL   B CA  
7051 C C   . VAL   B 165 ? 0.2702 0.2143 0.3823 -0.0442 -0.1216 0.0086  165 VAL   B C   
7052 O O   . VAL   B 165 ? 0.3014 0.2283 0.3917 -0.0494 -0.1274 0.0220  165 VAL   B O   
7053 C CB  . VAL   B 165 ? 0.2641 0.1933 0.3507 -0.0325 -0.0474 -0.0291 165 VAL   B CB  
7054 C CG1 . VAL   B 165 ? 0.2924 0.2150 0.3874 -0.0271 -0.0300 -0.0183 165 VAL   B CG1 
7055 C CG2 . VAL   B 165 ? 0.2612 0.1851 0.3516 -0.0303 -0.0155 -0.0359 165 VAL   B CG2 
7065 N N   . SER   B 166 ? 0.2875 0.2083 0.4274 -0.0514 -0.1406 -0.0110 166 SER   B N   
7066 C CA  . SER   B 166 ? 0.2890 0.2112 0.4789 -0.0514 -0.1196 -0.0113 166 SER   B CA  
7067 C C   . SER   B 166 ? 0.2688 0.2174 0.4906 -0.0675 -0.1033 0.0270  166 SER   B C   
7068 O O   . SER   B 166 ? 0.2690 0.2452 0.5309 -0.0874 -0.1242 -0.0115 166 SER   B O   
7069 C CB  . SER   B 166 ? 0.2837 0.2170 0.5078 -0.0370 -0.1048 -0.0149 166 SER   B CB  
7070 O OG  . SER   B 166 ? 0.2682 0.2025 0.5343 -0.0258 -0.0954 0.0048  166 SER   B OG  
7076 N N   . SER   B 167 ? 0.2427 0.2188 0.4521 -0.0745 -0.1161 0.0701  167 SER   B N   
7077 C CA  . SER   B 167 ? 0.2445 0.2195 0.4478 -0.0614 -0.0689 0.0713  167 SER   B CA  
7078 C C   . SER   B 167 ? 0.2311 0.2263 0.4132 -0.0743 -0.0648 0.0879  167 SER   B C   
7079 O O   . SER   B 167 ? 0.2296 0.2381 0.4035 -0.0828 -0.0658 0.0868  167 SER   B O   
7080 C CB  . SER   B 167 ? 0.2262 0.2088 0.4787 -0.0567 -0.0353 0.0560  167 SER   B CB  
7081 O OG  . SER   B 167 ? 0.2297 0.2115 0.4815 -0.0449 -0.0062 0.0441  167 SER   B OG  
7087 N N   . PHE   B 168 ? 0.2338 0.2233 0.4026 -0.0634 -0.0543 0.0867  168 PHE   B N   
7088 C CA  . PHE   B 168 ? 0.2331 0.2092 0.3440 -0.0648 -0.0463 0.0472  168 PHE   B CA  
7089 C C   . PHE   B 168 ? 0.2062 0.1797 0.2801 -0.0309 -0.0193 0.0203  168 PHE   B C   
7090 O O   . PHE   B 168 ? 0.2366 0.1756 0.2728 -0.0085 -0.0173 -0.0091 168 PHE   B O   
7091 C CB  . PHE   B 168 ? 0.2461 0.2187 0.3656 -0.0764 -0.0491 0.0546  168 PHE   B CB  
7092 C CG  . PHE   B 168 ? 0.2804 0.1893 0.3345 -0.0769 -0.0423 0.0331  168 PHE   B CG  
7093 C CD1 . PHE   B 168 ? 0.3230 0.2259 0.3672 -0.0542 -0.0391 0.0293  168 PHE   B CD1 
7094 C CD2 . PHE   B 168 ? 0.2730 0.1847 0.3387 -0.0609 -0.0403 0.0420  168 PHE   B CD2 
7095 C CE1 . PHE   B 168 ? 0.3340 0.2201 0.3592 -0.0517 -0.0256 0.0467  168 PHE   B CE1 
7096 C CE2 . PHE   B 168 ? 0.3093 0.2021 0.3527 -0.0422 -0.0262 0.0511  168 PHE   B CE2 
7097 C CZ  . PHE   B 168 ? 0.3256 0.2037 0.3565 -0.0396 -0.0307 0.0666  168 PHE   B CZ  
7107 N N   . LEU   B 169 ? 0.2173 0.1845 0.2620 -0.0034 -0.0022 0.0057  169 LEU   B N   
7108 C CA  . LEU   B 169 ? 0.2727 0.2145 0.2922 -0.0025 0.0023  -0.0376 169 LEU   B CA  
7109 C C   . LEU   B 169 ? 0.3125 0.2523 0.3510 0.0117  -0.0000 -0.0522 169 LEU   B C   
7110 O O   . LEU   B 169 ? 0.3254 0.2691 0.4087 0.0089  -0.0016 -0.0784 169 LEU   B O   
7111 C CB  . LEU   B 169 ? 0.3049 0.2559 0.3152 -0.0081 -0.0112 -0.0052 169 LEU   B CB  
7112 C CG  . LEU   B 169 ? 0.3504 0.2928 0.3595 -0.0058 -0.0056 -0.0052 169 LEU   B CG  
7113 C CD1 . LEU   B 169 ? 0.3628 0.3082 0.3601 -0.0139 -0.0073 0.0167  169 LEU   B CD1 
7114 C CD2 . LEU   B 169 ? 0.3406 0.2986 0.3633 0.0020  0.0104  -0.0199 169 LEU   B CD2 
7115 O OXT . LEU   B 169 ? 0.3325 0.2664 0.3479 0.0499  0.0217  -0.0470 169 LEU   B OXT 
7127 C C1  T TFA   C .   ? 0.1757 0.1936 0.1217 -0.0441 0.0218  0.0108  201 TFA   A C1  
7128 C C2  T TFA   C .   ? 0.2053 0.2074 0.1657 -0.0366 0.0036  0.0144  201 TFA   A C2  
7129 O O   T TFA   C .   ? 0.1616 0.1867 0.1358 -0.0538 0.0344  -0.0046 201 TFA   A O   
7130 F F1  T TFA   C .   ? 0.2158 0.2092 0.2115 -0.0227 -0.0141 0.0168  201 TFA   A F1  
7131 F F2  T TFA   C .   ? 0.2185 0.2161 0.1526 -0.0473 0.0023  0.0210  201 TFA   A F2  
7132 F F3  T TFA   C .   ? 0.2181 0.2193 0.1839 -0.0369 0.0183  0.0221  201 TFA   A F3  
7133 O OXT T TFA   C .   ? 0.1488 0.1836 0.0798 -0.0376 0.0285  0.0089  201 TFA   A OXT 
7134 N N2  B A1A8H D .   ? 0.1292 0.1564 0.1660 0.0095  -0.0068 0.0330  202 A1A8H A N2  
7135 C C3  B A1A8H D .   ? 0.2108 0.1710 0.2012 0.0060  -0.0001 0.0153  202 A1A8H A C3  
7136 C C6  B A1A8H D .   ? 0.2163 0.1760 0.1908 0.0163  -0.0053 0.0390  202 A1A8H A C6  
7137 C C9  B A1A8H D .   ? 0.1438 0.1544 0.1507 0.0229  -0.0096 0.0277  202 A1A8H A C9  
7138 C C12 B A1A8H D .   ? 0.1353 0.1472 0.1305 0.0121  -0.0055 0.0280  202 A1A8H A C12 
7139 C C14 B A1A8H D .   ? 0.1344 0.1445 0.1003 -0.0049 -0.0131 0.0326  202 A1A8H A C14 
7140 C C1  B A1A8H D .   ? 0.1848 0.1577 0.2283 0.0014  -0.0074 0.0094  202 A1A8H A C1  
7141 C C10 B A1A8H D .   ? 0.1254 0.1552 0.1413 0.0102  0.0155  0.0485  202 A1A8H A C10 
7142 C C11 B A1A8H D .   ? 0.1321 0.1380 0.1186 0.0087  0.0021  0.0276  202 A1A8H A C11 
7143 C C13 B A1A8H D .   ? 0.1386 0.1466 0.1110 -0.0029 -0.0004 0.0397  202 A1A8H A C13 
7144 C C2  B A1A8H D .   ? 0.1927 0.1609 0.2078 0.0116  -0.0090 0.0068  202 A1A8H A C2  
7145 C C4  B A1A8H D .   ? 0.2112 0.1654 0.1833 0.0077  0.0031  0.0368  202 A1A8H A C4  
7146 C C5  B A1A8H D .   ? 0.2174 0.1708 0.1830 0.0160  0.0022  0.0355  202 A1A8H A C5  
7147 C C7  B A1A8H D .   ? 0.2101 0.1635 0.1671 0.0133  -0.0071 0.0547  202 A1A8H A C7  
7148 C C8  B A1A8H D .   ? 0.1899 0.1504 0.1835 0.0172  0.0047  0.0374  202 A1A8H A C8  
7149 N N1  B A1A8H D .   ? 0.1738 0.1537 0.1826 0.0194  -0.0114 0.0267  202 A1A8H A N1  
7150 N N3  B A1A8H D .   ? 0.1338 0.1442 0.1176 0.0018  0.0262  0.0481  202 A1A8H A N3  
7151 N N4  B A1A8H D .   ? 0.1370 0.1394 0.1058 0.0050  -0.0202 0.0245  202 A1A8H A N4  
7152 O O1  B A1A8H D .   ? 0.1814 0.1656 0.2517 -0.0116 -0.0150 0.0086  202 A1A8H A O1  
7171 N N2  C A1A8H E .   ? 0.1560 0.1647 0.1809 -0.0047 -0.0156 0.0152  203 A1A8H A N2  
7172 C C3  C A1A8H E .   ? 0.2296 0.2010 0.2289 0.0143  -0.0092 -0.0177 203 A1A8H A C3  
7173 C C6  C A1A8H E .   ? 0.2248 0.2000 0.2003 0.0218  -0.0092 -0.0104 203 A1A8H A C6  
7174 C C9  C A1A8H E .   ? 0.1728 0.1697 0.1648 0.0073  -0.0134 0.0117  203 A1A8H A C9  
7175 C C12 C A1A8H E .   ? 0.1574 0.1551 0.1328 -0.0005 -0.0057 0.0257  203 A1A8H A C12 
7176 C C14 C A1A8H E .   ? 0.1532 0.1506 0.0935 -0.0111 -0.0106 0.0293  203 A1A8H A C14 
7177 C C1  C A1A8H E .   ? 0.2227 0.2019 0.2506 0.0052  -0.0111 -0.0078 203 A1A8H A C1  
7178 C C10 C A1A8H E .   ? 0.1526 0.1657 0.1766 -0.0042 0.0050  0.0245  203 A1A8H A C10 
7179 C C11 C A1A8H E .   ? 0.1543 0.1471 0.1321 -0.0016 0.0006  0.0192  203 A1A8H A C11 
7180 C C13 C A1A8H E .   ? 0.1564 0.1541 0.1053 -0.0110 0.0005  0.0372  203 A1A8H A C13 
7181 C C2  C A1A8H E .   ? 0.2219 0.1935 0.2325 0.0124  -0.0154 -0.0142 203 A1A8H A C2  
7182 C C4  C A1A8H E .   ? 0.2293 0.1991 0.2217 0.0195  -0.0084 -0.0170 203 A1A8H A C4  
7183 C C5  C A1A8H E .   ? 0.2222 0.1983 0.2097 0.0168  -0.0102 -0.0226 203 A1A8H A C5  
7184 C C7  C A1A8H E .   ? 0.2243 0.1951 0.2069 0.0237  -0.0100 -0.0144 203 A1A8H A C7  
7185 C C8  C A1A8H E .   ? 0.2210 0.1837 0.2211 0.0278  -0.0160 -0.0107 203 A1A8H A C8  
7186 N N1  C A1A8H E .   ? 0.2045 0.1811 0.2070 0.0146  -0.0226 -0.0012 203 A1A8H A N1  
7187 N N3  C A1A8H E .   ? 0.1576 0.1539 0.1519 -0.0062 0.0180  0.0281  203 A1A8H A N3  
7188 N N4  C A1A8H E .   ? 0.1563 0.1470 0.1089 -0.0036 -0.0160 0.0192  203 A1A8H A N4  
7189 O O1  C A1A8H E .   ? 0.2260 0.2132 0.2707 -0.0053 -0.0131 -0.0061 203 A1A8H A O1  
7208 O O   B HOH   F .   ? 0.4404 0.4936 0.4755 0.0314  -0.0460 0.0940  301 HOH   A O   
7209 O O   . HOH   F .   ? 0.4983 0.5881 0.6778 -0.1188 0.0858  0.3112  302 HOH   A O   
7210 O O   . HOH   F .   ? 0.6309 0.6190 0.5121 -0.0891 -0.1526 0.0737  303 HOH   A O   
7211 O O   A HOH   F .   ? 0.3806 0.6877 0.3963 -0.0799 -0.0073 0.1287  304 HOH   A O   
7212 O O   . HOH   F .   ? 0.3355 0.2859 0.5957 -0.0281 -0.1384 0.1323  305 HOH   A O   
7213 O O   . HOH   F .   ? 0.3526 0.3766 0.3817 -0.1007 -0.0138 0.1245  306 HOH   A O   
7214 O O   A HOH   F .   ? 0.2339 0.2519 0.4063 -0.0049 -0.0781 0.0387  307 HOH   A O   
7215 O O   . HOH   F .   ? 0.6586 0.5520 0.3283 0.1956  -0.0730 0.0763  308 HOH   A O   
7216 O O   . HOH   F .   ? 0.4962 0.3646 0.4410 0.0115  0.1294  0.0311  309 HOH   A O   
7217 O O   . HOH   F .   ? 0.3472 0.3706 0.2078 -0.0241 0.0541  0.0467  310 HOH   A O   
7218 O O   . HOH   F .   ? 0.4136 0.6246 0.6905 0.0365  0.0474  -0.1214 311 HOH   A O   
7219 O O   A HOH   F .   ? 0.2917 0.4751 0.5779 0.0425  0.0593  0.1067  312 HOH   A O   
7220 O O   . HOH   F .   ? 0.5211 0.5428 0.6622 -0.0170 0.1479  0.2459  313 HOH   A O   
7221 O O   . HOH   F .   ? 0.3980 0.7198 0.4122 0.0209  -0.0484 0.0220  314 HOH   A O   
7222 O O   . HOH   F .   ? 0.5788 0.6534 0.5412 0.0116  0.2918  -0.1498 315 HOH   A O   
7223 O O   B HOH   F .   ? 0.2857 0.4916 0.5155 -0.1008 0.0604  -0.1035 316 HOH   A O   
7224 O O   . HOH   F .   ? 1.2567 1.1740 1.0329 -0.0756 -0.0884 -0.0454 317 HOH   A O   
7225 O O   . HOH   F .   ? 0.3481 0.2849 0.3535 -0.0386 0.0675  -0.0571 318 HOH   A O   
7226 O O   . HOH   F .   ? 0.5344 0.2593 0.6611 0.0621  -0.0211 -0.0907 319 HOH   A O   
7227 O O   . HOH   F .   ? 0.2212 0.2004 0.2575 0.0335  -0.0454 0.0077  320 HOH   A O   
7228 O O   . HOH   F .   ? 0.4713 0.7408 0.4801 0.2560  0.0311  -0.1572 321 HOH   A O   
7229 O O   . HOH   F .   ? 0.7024 0.6699 0.4174 -0.0979 -0.0015 0.1151  322 HOH   A O   
7230 O O   . HOH   F .   ? 0.5152 0.5641 0.6673 -0.0877 0.1514  0.2858  323 HOH   A O   
7231 O O   . HOH   F .   ? 0.2437 0.3001 0.3311 -0.0856 -0.0588 0.1487  324 HOH   A O   
7232 O O   . HOH   F .   ? 0.4405 0.3375 0.4363 -0.0820 -0.0454 -0.0435 325 HOH   A O   
7233 O O   . HOH   F .   ? 0.7349 0.7652 0.7575 -0.1072 -0.1379 -0.0624 326 HOH   A O   
7234 O O   . HOH   F .   ? 0.6672 0.5871 0.9325 -0.1370 -0.0900 0.1838  327 HOH   A O   
7235 O O   . HOH   F .   ? 0.2429 0.2820 0.3521 0.0164  0.0002  -0.0393 328 HOH   A O   
7236 O O   . HOH   F .   ? 0.6361 0.4329 0.3841 -0.1471 -0.0742 0.1457  329 HOH   A O   
7237 O O   A HOH   F .   ? 0.1846 0.2120 0.2496 -0.0273 0.0455  0.0707  330 HOH   A O   
7238 O O   . HOH   F .   ? 0.2534 0.2213 0.2029 -0.0545 0.0151  0.0434  331 HOH   A O   
7239 O O   . HOH   F .   ? 0.2530 0.3555 0.3376 -0.0270 0.0873  -0.0233 332 HOH   A O   
7240 O O   . HOH   F .   ? 0.2528 0.3361 0.4747 -0.0278 -0.1017 0.1370  333 HOH   A O   
7241 O O   . HOH   F .   ? 0.3578 0.4471 0.5301 0.1558  0.1125  0.0830  334 HOH   A O   
7242 O O   . HOH   F .   ? 0.2322 0.2027 0.3427 -0.0512 0.0119  -0.0117 335 HOH   A O   
7243 O O   . HOH   F .   ? 0.4003 0.4249 0.3203 -0.0409 -0.0721 -0.0261 336 HOH   A O   
7244 O O   A HOH   F .   ? 0.2870 0.4898 0.3762 0.1391  -0.0311 -0.0859 337 HOH   A O   
7245 O O   . HOH   F .   ? 0.1892 0.1893 0.2469 0.0075  -0.0303 0.0309  338 HOH   A O   
7246 O O   . HOH   F .   ? 0.2375 0.3619 0.5086 -0.0640 0.0865  -0.1007 339 HOH   A O   
7247 O O   . HOH   F .   ? 0.1796 0.1804 0.2474 -0.0346 0.0024  -0.0011 340 HOH   A O   
7248 O O   . HOH   F .   ? 0.1886 0.2124 0.2841 -0.0283 0.0092  0.0498  341 HOH   A O   
7249 O O   . HOH   F .   ? 0.4786 0.2769 0.3000 -0.0893 0.0094  0.0220  342 HOH   A O   
7250 O O   . HOH   F .   ? 0.1988 0.2723 0.3920 0.0100  0.0671  -0.0753 343 HOH   A O   
7251 O O   . HOH   F .   ? 0.7189 0.5910 0.5834 -0.0964 0.0118  0.0172  344 HOH   A O   
7252 O O   A HOH   F .   ? 0.1702 0.3555 0.2377 0.0762  0.0351  0.0557  345 HOH   A O   
7253 O O   . HOH   F .   ? 0.5967 0.2196 0.5001 -0.0003 -0.1398 0.0975  346 HOH   A O   
7254 O O   . HOH   F .   ? 0.5181 0.8355 0.4655 0.2457  -0.0582 -0.0553 347 HOH   A O   
7255 O O   . HOH   F .   ? 0.6434 0.4382 0.5197 -0.1958 -0.1109 0.2323  348 HOH   A O   
7256 O O   . HOH   F .   ? 0.2458 0.2140 0.3301 0.0320  0.0238  0.0238  349 HOH   A O   
7257 O O   . HOH   F .   ? 0.3472 0.3969 0.5281 -0.0729 -0.0863 -0.0900 350 HOH   A O   
7258 O O   . HOH   F .   ? 0.2999 0.4572 0.6301 -0.0827 0.1786  -0.0079 351 HOH   A O   
7259 O O   . HOH   F .   ? 0.3576 0.2811 0.2999 -0.0688 -0.1113 0.0525  352 HOH   A O   
7260 O O   . HOH   F .   ? 0.4280 0.4190 0.2665 -0.1814 -0.0273 -0.0513 353 HOH   A O   
7261 O O   . HOH   F .   ? 0.7460 0.3745 0.3729 0.0932  0.0136  0.0974  354 HOH   A O   
7262 O O   . HOH   F .   ? 0.2821 0.3881 0.3982 0.0918  -0.0911 -0.0328 355 HOH   A O   
7263 O O   . HOH   F .   ? 0.2769 0.2937 0.4623 -0.0401 -0.0084 -0.0339 356 HOH   A O   
7264 O O   . HOH   F .   ? 0.1927 0.2004 0.3532 0.0045  -0.0272 -0.0193 357 HOH   A O   
7265 O O   . HOH   F .   ? 0.3230 0.4259 0.3842 -0.1424 0.1014  0.0209  358 HOH   A O   
7266 O O   . HOH   F .   ? 0.8445 0.8068 0.4801 0.2080  -0.0905 -0.0505 359 HOH   A O   
7267 O O   . HOH   F .   ? 0.3686 0.4456 0.2896 -0.0135 0.0730  0.0382  360 HOH   A O   
7268 O O   . HOH   F .   ? 0.8121 0.5136 0.6741 -0.1046 -0.1432 0.0979  361 HOH   A O   
7269 O O   A HOH   F .   ? 0.3233 0.4202 0.2933 -0.1413 0.0161  0.0309  362 HOH   A O   
7270 O O   . HOH   F .   ? 0.3239 0.4249 0.5159 -0.1450 -0.1325 0.0345  363 HOH   A O   
7271 O O   A HOH   F .   ? 0.4195 0.4844 0.2896 -0.0020 -0.0014 -0.1316 364 HOH   A O   
7272 O O   . HOH   F .   ? 0.5857 0.7767 0.4789 0.1277  -0.0988 0.1994  365 HOH   A O   
7273 O O   . HOH   F .   ? 0.1999 0.2602 0.2781 -0.0333 -0.0393 0.0723  366 HOH   A O   
7274 O O   . HOH   F .   ? 0.1756 0.1546 0.2582 -0.0212 0.0253  -0.0127 367 HOH   A O   
7275 O O   . HOH   F .   ? 0.1483 0.1506 0.1998 -0.0029 0.0176  0.0107  368 HOH   A O   
7276 O O   . HOH   F .   ? 0.1604 0.2234 0.2256 -0.0039 -0.0109 0.0435  369 HOH   A O   
7277 O O   . HOH   F .   ? 0.1522 0.1598 0.1948 -0.0029 -0.0211 0.0060  370 HOH   A O   
7278 O O   B HOH   F .   ? 0.1967 0.1577 0.1704 0.0258  -0.0144 -0.0057 371 HOH   A O   
7279 O O   . HOH   F .   ? 0.2233 0.1703 0.2243 -0.0049 0.0266  0.0239  372 HOH   A O   
7280 O O   A HOH   F .   ? 0.2095 0.1937 0.2904 0.0131  -0.0626 0.0223  373 HOH   A O   
7281 O O   . HOH   F .   ? 0.2943 0.5245 0.4661 -0.0566 0.0480  -0.0551 374 HOH   A O   
7282 O O   . HOH   F .   ? 0.2540 0.2527 0.3331 -0.0374 -0.0478 0.0981  375 HOH   A O   
7283 O O   . HOH   F .   ? 0.1773 0.1992 0.2590 0.0071  0.0023  0.0037  376 HOH   A O   
7284 O O   . HOH   F .   ? 0.2359 0.2020 0.4825 0.0205  0.1293  -0.0071 377 HOH   A O   
7285 O O   . HOH   F .   ? 0.4527 0.2239 0.3048 0.1412  0.0715  0.0392  378 HOH   A O   
7286 O O   . HOH   F .   ? 0.1620 0.1819 0.1704 -0.0075 -0.0167 -0.0036 379 HOH   A O   
7287 O O   A HOH   F .   ? 0.1653 0.2929 0.3025 -0.0022 0.0202  0.1051  380 HOH   A O   
7288 O O   . HOH   F .   ? 0.3455 0.3334 0.3570 -0.0023 0.0072  0.1285  381 HOH   A O   
7289 O O   . HOH   F .   ? 0.5034 0.7206 0.5905 0.1642  -0.1062 -0.1558 382 HOH   A O   
7290 O O   . HOH   F .   ? 0.1716 0.1986 0.2212 0.0079  -0.0343 -0.0257 383 HOH   A O   
7291 O O   . HOH   F .   ? 0.3834 0.2498 0.3960 -0.1137 0.1321  -0.0452 384 HOH   A O   
7292 O O   . HOH   F .   ? 0.2528 0.2424 0.2493 -0.0285 0.0366  0.0068  385 HOH   A O   
7293 O O   . HOH   F .   ? 0.4490 0.2622 0.4346 -0.1273 0.0771  0.0505  386 HOH   A O   
7294 O O   . HOH   F .   ? 0.1926 0.2329 0.2806 -0.0340 0.0174  0.0256  387 HOH   A O   
7295 O O   . HOH   F .   ? 0.1754 0.1568 0.1827 -0.0238 0.0132  -0.0027 388 HOH   A O   
7296 O O   . HOH   F .   ? 0.3668 0.6194 0.4011 0.0963  0.1141  -0.0511 389 HOH   A O   
7297 O O   . HOH   F .   ? 0.2872 0.3664 0.4010 -0.0361 0.1197  -0.0746 390 HOH   A O   
7298 O O   . HOH   F .   ? 0.3561 0.3308 0.2208 0.0370  0.0828  0.0032  391 HOH   A O   
7299 O O   T HOH   F .   ? 0.1721 0.1410 0.2362 -0.0709 -0.0482 0.0697  392 HOH   A O   
7300 O O   . HOH   F .   ? 0.5240 0.5161 0.4186 0.0078  -0.1601 -0.0346 393 HOH   A O   
7301 O O   . HOH   F .   ? 0.3600 0.7698 0.3965 -0.0864 -0.0344 0.1672  394 HOH   A O   
7302 O O   . HOH   F .   ? 0.5658 0.8013 0.2845 -0.1230 -0.0433 -0.1112 395 HOH   A O   
7303 O O   . HOH   F .   ? 0.4423 0.8914 0.5729 -0.0940 -0.1033 -0.0183 396 HOH   A O   
7304 O O   . HOH   F .   ? 0.3533 0.4395 0.4596 0.1252  0.0697  -0.0092 397 HOH   A O   
7305 O O   . HOH   F .   ? 0.2389 0.2092 0.3947 0.0052  -0.0426 0.0118  398 HOH   A O   
7306 O O   . HOH   F .   ? 0.5352 0.3825 0.5610 0.1878  -0.0845 -0.0591 399 HOH   A O   
7307 O O   . HOH   F .   ? 0.3066 0.2483 0.2779 -0.0313 0.0078  0.0430  400 HOH   A O   
7308 O O   . HOH   F .   ? 0.7144 0.7051 0.6545 0.0531  0.1688  0.0762  401 HOH   A O   
7309 O O   . HOH   F .   ? 0.2004 0.1959 0.3969 0.0312  0.0884  0.0857  402 HOH   A O   
7310 O O   A HOH   F .   ? 0.2520 0.2591 0.3210 0.0395  0.0083  -0.0248 403 HOH   A O   
7311 O O   . HOH   F .   ? 0.4133 0.2669 0.4943 -0.0828 -0.0344 -0.0170 404 HOH   A O   
7312 O O   B HOH   F .   ? 0.4697 0.3201 0.3695 -0.1778 0.1244  -0.0630 405 HOH   A O   
7313 O O   . HOH   F .   ? 0.2747 0.2166 0.3040 -0.0573 -0.0211 0.0566  406 HOH   A O   
7314 O O   . HOH   F .   ? 0.3103 0.5926 0.3331 0.0757  0.0863  0.2272  407 HOH   A O   
7315 O O   . HOH   F .   ? 0.1960 0.1906 0.3971 0.0065  0.0040  0.0287  408 HOH   A O   
7316 O O   A HOH   F .   ? 0.4062 0.4591 0.3745 0.2322  0.0622  0.1035  409 HOH   A O   
7317 O O   A HOH   F .   ? 0.2973 0.5873 0.4338 -0.0544 -0.0666 0.1686  410 HOH   A O   
7318 O O   . HOH   F .   ? 0.2222 0.4084 0.8522 -0.0352 0.0377  -0.0007 411 HOH   A O   
7319 O O   . HOH   F .   ? 0.2463 0.2733 0.4244 0.0140  -0.0430 -0.0253 412 HOH   A O   
7320 O O   A HOH   F .   ? 0.3499 0.3827 0.4015 -0.0869 -0.0128 0.0751  413 HOH   A O   
7321 O O   A HOH   F .   ? 0.5098 0.4132 0.3283 -0.1583 0.0006  0.1595  414 HOH   A O   
7322 O O   . HOH   F .   ? 0.6127 0.7318 0.6137 0.3447  0.1977  0.0567  415 HOH   A O   
7323 O O   . HOH   F .   ? 0.3235 0.6373 0.1902 -0.0172 0.0640  0.0407  416 HOH   A O   
7324 O O   . HOH   F .   ? 0.3686 0.1378 0.2491 -0.0043 -0.0782 0.0113  417 HOH   A O   
7325 O O   . HOH   F .   ? 0.5352 0.7360 0.7007 0.0261  -0.0349 0.0718  418 HOH   A O   
7326 O O   A HOH   F .   ? 0.1769 0.2726 0.2749 -0.0464 0.0730  0.0774  419 HOH   A O   
7327 O O   . HOH   F .   ? 0.2701 0.2495 0.3110 0.0262  -0.1053 0.0298  420 HOH   A O   
7328 O O   . HOH   F .   ? 0.4342 0.6360 0.3573 -0.1647 -0.0186 -0.0130 421 HOH   A O   
7329 O O   . HOH   F .   ? 0.4189 0.2506 0.6353 -0.0926 -0.2543 0.1105  422 HOH   A O   
7330 O O   . HOH   F .   ? 0.4659 0.5114 0.5544 -0.1096 -0.0816 -0.1216 423 HOH   A O   
7331 O O   . HOH   F .   ? 0.2077 0.2979 0.5026 -0.0198 -0.0221 0.0808  424 HOH   A O   
7332 O O   . HOH   F .   ? 0.2377 0.2591 0.3170 -0.0041 -0.0671 0.0476  425 HOH   A O   
7333 O O   . HOH   F .   ? 0.6399 0.7894 0.4904 0.1182  0.3101  -0.0056 426 HOH   A O   
7334 O O   . HOH   F .   ? 0.4341 0.4033 0.2779 -0.1229 -0.0090 0.0469  427 HOH   A O   
7335 O O   . HOH   F .   ? 0.2572 0.4094 0.3371 0.1503  0.0140  0.0456  428 HOH   A O   
7336 O O   . HOH   F .   ? 0.2293 0.2475 0.3275 -0.0484 -0.0173 0.0311  429 HOH   A O   
7337 O O   . HOH   F .   ? 0.6634 0.3110 0.3480 -0.1591 -0.0455 -0.0632 430 HOH   A O   
7338 O O   A HOH   F .   ? 0.1815 0.2133 0.3182 0.0130  -0.0715 -0.0453 431 HOH   A O   
7339 O O   A HOH   F .   ? 0.6498 0.6916 0.3896 0.1610  -0.1607 0.1360  432 HOH   A O   
7340 O O   . HOH   F .   ? 0.4472 0.8150 0.3677 -0.1099 0.0058  0.1073  433 HOH   A O   
7341 O O   . HOH   F .   ? 0.3637 0.4430 0.4994 -0.0492 0.1571  -0.0276 434 HOH   A O   
7342 O O   . HOH   F .   ? 0.4990 0.4757 0.6402 0.1144  0.1522  -0.1339 435 HOH   A O   
7343 O O   . HOH   F .   ? 0.2740 0.1904 0.3500 0.0088  0.0182  0.0085  436 HOH   A O   
7344 O O   . HOH   F .   ? 0.6655 0.7450 0.6129 -0.1032 0.0542  0.2107  437 HOH   A O   
7345 O O   . HOH   F .   ? 0.7278 0.4225 0.5308 0.1777  -0.1114 0.1518  438 HOH   A O   
7346 O O   . HOH   F .   ? 0.7053 0.5979 0.8198 -0.0142 -0.1235 0.1906  439 HOH   A O   
7347 O O   . HOH   F .   ? 0.3895 0.3247 0.2219 -0.0900 0.0026  0.0730  440 HOH   A O   
7348 O O   . HOH   F .   ? 0.5857 0.6825 0.6895 0.0190  -0.1112 0.2564  441 HOH   A O   
7349 O O   A HOH   F .   ? 0.2000 0.2297 0.1735 0.0216  0.0532  -0.0134 442 HOH   A O   
7350 O O   B HOH   F .   ? 0.4917 0.5781 0.3973 0.0633  0.0176  -0.0315 443 HOH   A O   
7351 O O   . HOH   F .   ? 0.4203 0.4397 0.3638 0.2540  -0.0461 -0.0610 444 HOH   A O   
7352 O O   . HOH   F .   ? 0.2370 0.3047 0.2973 -0.0075 0.0069  -0.0724 445 HOH   A O   
7353 O O   B HOH   F .   ? 0.1669 0.2297 0.1518 -0.0377 0.0134  -0.0092 446 HOH   A O   
7354 O O   . HOH   F .   ? 0.8343 0.6748 0.8055 0.1201  -0.0057 -0.0408 447 HOH   A O   
7355 O O   . HOH   F .   ? 0.9868 0.6090 0.5204 -0.0800 0.2622  0.0586  448 HOH   A O   
7356 O O   . HOH   F .   ? 0.3524 0.4849 0.6928 0.0238  0.0727  -0.2322 449 HOH   A O   
7357 O O   . HOH   F .   ? 0.1980 0.2452 0.4940 -0.0228 -0.1048 0.0769  450 HOH   A O   
7358 O O   A HOH   F .   ? 0.4277 0.3635 0.4870 -0.0471 -0.0189 -0.0338 451 HOH   A O   
7359 O O   . HOH   F .   ? 0.2360 0.2100 0.3268 -0.0051 0.0263  0.0224  452 HOH   A O   
7360 O O   A HOH   F .   ? 0.4930 0.4961 0.4437 0.0586  0.0902  0.0211  453 HOH   A O   
7361 O O   . HOH   F .   ? 0.8520 0.7130 0.8387 -0.1233 0.1139  -0.1379 454 HOH   A O   
7362 O O   B HOH   F .   ? 0.2289 0.2580 0.4916 0.0093  -0.0161 0.1505  455 HOH   A O   
7363 O O   . HOH   F .   ? 0.3580 0.4240 0.4699 0.0797  0.1158  0.0637  456 HOH   A O   
7364 O O   . HOH   F .   ? 0.8226 0.8288 0.4993 0.0038  -0.0314 -0.0491 457 HOH   A O   
7365 O O   . HOH   F .   ? 0.3759 0.3735 0.4268 0.0105  0.0574  0.0299  458 HOH   A O   
7366 O O   . HOH   F .   ? 0.4868 0.4839 0.5029 0.2555  -0.0585 0.0704  459 HOH   A O   
7367 O O   . HOH   F .   ? 0.3091 0.2993 0.5481 -0.0575 0.0507  -0.1223 460 HOH   A O   
7368 O O   . HOH   F .   ? 0.5281 0.6282 0.4538 0.0094  -0.0238 0.1452  461 HOH   A O   
7369 O O   . HOH   F .   ? 0.3802 0.5382 0.4658 -0.1474 0.0474  -0.1237 462 HOH   A O   
7370 O O   B HOH   F .   ? 0.1947 0.1956 0.3756 -0.0321 -0.0178 0.0200  463 HOH   A O   
7371 O O   . HOH   F .   ? 0.3300 0.5912 0.5338 0.0684  -0.0569 0.1329  464 HOH   A O   
7372 O O   . HOH   F .   ? 0.6938 0.6163 0.5425 0.1641  0.0363  -0.0642 465 HOH   A O   
7373 O O   . HOH   F .   ? 0.4804 0.5950 0.4336 0.0601  -0.1072 -0.1037 466 HOH   A O   
7374 O O   . HOH   F .   ? 0.4126 0.7218 0.5284 -0.0944 -0.1562 0.3014  467 HOH   A O   
7375 O O   . HOH   F .   ? 0.2605 0.4462 0.6216 0.0442  0.0026  -0.2040 468 HOH   A O   
7376 O O   . HOH   F .   ? 0.4787 0.4768 0.5304 -0.1089 0.0784  -0.0356 469 HOH   A O   
7377 O O   . HOH   F .   ? 0.3326 0.3181 0.3881 -0.1247 0.0325  -0.0250 470 HOH   A O   
7378 O O   . HOH   F .   ? 0.2797 0.1989 0.3152 0.0334  -0.0885 -0.0365 471 HOH   A O   
7379 O O   . HOH   F .   ? 0.5991 0.3298 0.8094 0.0892  0.1128  0.2124  472 HOH   A O   
7380 O O   . HOH   F .   ? 0.5692 0.5055 0.5619 -0.0449 0.0800  0.0206  473 HOH   A O   
7381 O O   . HOH   F .   ? 0.5143 0.6416 0.3344 -0.0310 -0.0040 0.0457  474 HOH   A O   
7382 O O   A HOH   F .   ? 0.3138 0.2880 0.4585 0.0554  -0.1244 -0.0484 475 HOH   A O   
7383 O O   . HOH   F .   ? 0.8306 0.6911 0.6476 0.1055  0.1430  0.2490  476 HOH   A O   
7384 O O   . HOH   F .   ? 0.4206 0.3254 0.4272 0.0461  0.1269  0.0575  477 HOH   A O   
7385 O O   . HOH   F .   ? 0.8684 0.4210 0.5644 -0.0364 0.1042  0.0270  478 HOH   A O   
7386 O O   . HOH   F .   ? 0.8140 0.9255 0.6299 0.3355  -0.1460 0.0139  479 HOH   A O   
7387 O O   . HOH   F .   ? 0.5193 0.4996 0.6780 -0.1697 -0.0821 -0.1132 480 HOH   A O   
7388 O O   . HOH   F .   ? 0.6301 0.3606 0.3929 -0.0466 -0.1201 0.0238  481 HOH   A O   
7389 O O   . HOH   F .   ? 0.2969 0.3257 0.2983 0.0754  -0.0285 -0.0042 482 HOH   A O   
7390 O O   . HOH   F .   ? 0.6649 0.7660 0.6630 -0.1215 -0.1407 -0.0193 483 HOH   A O   
7391 O O   . HOH   F .   ? 0.5081 0.4699 0.5318 -0.0075 -0.0012 -0.1193 484 HOH   A O   
7392 O O   B HOH   F .   ? 0.5179 0.3172 0.4568 -0.0972 0.0856  -0.1060 485 HOH   A O   
7393 O O   . HOH   F .   ? 0.6006 0.6341 0.8121 -0.1559 0.0613  -0.0955 486 HOH   A O   
7394 O O   . HOH   F .   ? 0.8333 0.5786 0.6231 -0.1299 0.0225  -0.1014 487 HOH   A O   
7395 O O   . HOH   F .   ? 0.6553 0.4870 0.5176 -0.1131 0.2589  0.1194  488 HOH   A O   
7396 O O   . HOH   F .   ? 0.8374 0.4150 0.3552 -0.0578 -0.1421 0.0462  489 HOH   A O   
7397 O O   . HOH   F .   ? 0.8704 0.7908 0.5494 -0.1298 0.2384  0.1755  490 HOH   A O   
7398 O O   . HOH   F .   ? 0.4784 0.5574 0.3806 0.0420  -0.0337 0.0129  491 HOH   A O   
7399 O O   . HOH   F .   ? 0.5060 0.3873 0.3175 -0.1330 0.1483  -0.0976 492 HOH   A O   
7400 O O   . HOH   F .   ? 0.2553 0.2544 0.7670 -0.0162 -0.1468 0.0230  493 HOH   A O   
7401 O O   . HOH   F .   ? 0.4851 0.3750 0.4856 -0.0600 0.0703  0.1549  494 HOH   A O   
7402 O O   . HOH   F .   ? 0.3140 0.6957 0.5375 0.1383  0.1330  0.3235  495 HOH   A O   
7403 O O   . HOH   F .   ? 0.6010 0.7553 0.7799 0.0194  0.2747  -0.1350 496 HOH   A O   
7404 O O   . HOH   F .   ? 0.3103 0.3195 0.6401 -0.0212 0.0931  -0.0702 497 HOH   A O   
7405 O O   . HOH   F .   ? 0.6690 0.7204 0.5636 0.2247  -0.0956 0.0441  498 HOH   A O   
7406 O O   . HOH   F .   ? 0.3040 0.2640 0.8065 0.0045  0.1104  0.0336  499 HOH   A O   
7407 O O   . HOH   F .   ? 0.4362 0.3314 0.5949 0.0236  0.2625  0.0756  500 HOH   A O   
7408 O O   . HOH   F .   ? 0.7053 0.2736 0.5571 -0.0207 0.1671  0.1142  501 HOH   A O   
7409 O O   . HOH   F .   ? 0.3427 0.5051 0.3941 -0.0006 -0.0631 -0.0092 502 HOH   A O   
7410 O O   B HOH   F .   ? 0.2142 0.4585 0.3773 -0.0351 0.0492  -0.0204 503 HOH   A O   
7411 O O   . HOH   F .   ? 0.4771 1.0694 0.6383 -0.0223 -0.0692 0.1688  504 HOH   A O   
7412 O O   . HOH   F .   ? 0.4762 0.2964 0.5421 -0.1553 -0.0056 0.0774  505 HOH   A O   
7413 O O   . HOH   F .   ? 0.2740 0.3854 0.3513 0.0394  -0.0327 0.0996  506 HOH   A O   
7414 O O   . HOH   F .   ? 0.2793 0.4999 0.5122 -0.0098 -0.0901 0.0515  507 HOH   A O   
7415 O O   . HOH   F .   ? 0.6426 0.9539 0.6494 0.1439  0.0014  0.2647  508 HOH   A O   
7416 O O   . HOH   F .   ? 0.4339 0.2358 0.4112 0.0192  -0.1681 0.0214  509 HOH   A O   
7417 O O   . HOH   F .   ? 0.3590 0.2386 0.5006 0.0120  0.0135  0.0672  510 HOH   A O   
7418 O O   . HOH   F .   ? 0.5412 0.8483 0.5283 0.3234  -0.0593 0.1515  511 HOH   A O   
7419 O O   T HOH   F .   ? 0.1442 0.1723 0.1757 -0.0149 -0.0186 0.0636  512 HOH   A O   
7420 O O   . HOH   F .   ? 0.8363 0.8958 0.6477 -0.1253 -0.1493 -0.1485 513 HOH   A O   
7421 O O   B HOH   F .   ? 0.3391 0.3199 0.4645 0.0483  -0.0065 0.1790  514 HOH   A O   
7422 O O   A HOH   F .   ? 0.4701 0.7092 0.3593 0.2899  -0.0346 0.0544  515 HOH   A O   
7423 O O   . HOH   F .   ? 0.4946 0.7480 0.5759 0.1488  0.0209  -0.1178 516 HOH   A O   
7424 O O   . HOH   F .   ? 0.5577 0.7553 0.5167 -0.0978 -0.0052 0.1434  517 HOH   A O   
7425 O O   . HOH   F .   ? 0.6731 0.4651 0.5730 0.0752  0.1883  0.1463  518 HOH   A O   
7426 O O   B HOH   F .   ? 0.3942 0.4653 0.4508 0.0979  -0.0273 0.0625  519 HOH   A O   
7427 O O   . HOH   F .   ? 0.2980 0.5433 0.6804 -0.0362 -0.0582 0.3198  520 HOH   A O   
7428 O O   . HOH   G .   ? 0.2455 0.3062 0.3161 -0.0044 0.0659  0.0288  201 HOH   B O   
7429 O O   . HOH   G .   ? 0.3614 0.3025 0.7518 -0.0330 0.0045  -0.0471 202 HOH   B O   
7430 O O   . HOH   G .   ? 0.5070 0.3735 0.4683 -0.0031 -0.0004 -0.1793 203 HOH   B O   
7431 O O   . HOH   G .   ? 0.2095 0.2334 0.3320 -0.0081 0.0154  -0.0318 204 HOH   B O   
7432 O O   . HOH   G .   ? 0.3605 0.2121 0.6068 -0.0052 0.2253  0.0515  205 HOH   B O   
7433 O O   . HOH   G .   ? 0.7507 0.3439 0.4520 0.0109  0.0802  -0.0206 206 HOH   B O   
7434 O O   . HOH   G .   ? 0.3893 0.7273 0.4840 -0.0599 -0.0637 0.3049  207 HOH   B O   
7435 O O   . HOH   G .   ? 0.3453 0.2309 0.5985 -0.0310 0.2238  -0.0009 208 HOH   B O   
7436 O O   . HOH   G .   ? 0.1855 0.2348 0.3187 -0.0394 -0.0051 0.0173  209 HOH   B O   
7437 O O   . HOH   G .   ? 0.3049 0.5954 0.5130 -0.0246 0.1578  -0.2099 210 HOH   B O   
7438 O O   . HOH   G .   ? 0.6865 0.6924 0.6180 0.2861  0.0703  -0.0127 211 HOH   B O   
7439 O O   . HOH   G .   ? 0.7723 0.4163 0.3500 -0.1226 -0.0243 0.0825  212 HOH   B O   
7440 O O   . HOH   G .   ? 0.3708 0.5572 0.5579 0.2190  0.0435  -0.0739 213 HOH   B O   
7441 O O   . HOH   G .   ? 0.4258 0.3971 0.3561 0.0150  -0.1194 0.0380  214 HOH   B O   
7442 O O   . HOH   G .   ? 0.4044 0.4745 0.4164 0.1800  -0.0557 -0.0152 215 HOH   B O   
7443 O O   . HOH   G .   ? 0.4282 0.2899 0.5162 0.0801  0.0015  0.0113  216 HOH   B O   
7444 O O   . HOH   G .   ? 0.5238 0.6929 0.4050 0.2595  0.1154  0.1514  217 HOH   B O   
7445 O O   . HOH   G .   ? 0.4523 0.4797 0.6215 -0.0949 -0.0362 -0.1382 218 HOH   B O   
7446 O O   . HOH   G .   ? 0.1878 0.2579 0.3521 -0.0209 0.0136  -0.0221 219 HOH   B O   
7447 O O   . HOH   G .   ? 0.3369 0.2803 0.6743 0.0752  -0.1127 0.0684  220 HOH   B O   
7448 O O   . HOH   G .   ? 0.5254 0.6564 0.3794 0.3006  -0.1166 -0.0018 221 HOH   B O   
7449 O O   . HOH   G .   ? 0.5221 0.3590 0.7355 0.0285  -0.1792 -0.0825 222 HOH   B O   
7450 O O   . HOH   G .   ? 0.6473 0.3963 0.7085 0.0841  -0.0589 0.2701  223 HOH   B O   
7451 O O   . HOH   G .   ? 0.2657 0.6801 0.5431 0.1276  -0.0695 -0.0741 224 HOH   B O   
7452 O O   . HOH   G .   ? 0.2628 0.2422 0.4221 -0.0338 -0.0008 -0.0616 225 HOH   B O   
7453 O O   . HOH   G .   ? 0.2470 0.1979 0.2619 -0.0383 0.0809  -0.0058 226 HOH   B O   
7454 O O   . HOH   G .   ? 0.5022 0.4151 0.4239 0.0276  0.0973  -0.1918 227 HOH   B O   
7455 O O   . HOH   G .   ? 0.2299 0.1467 0.3410 0.0115  -0.0566 -0.0164 228 HOH   B O   
7456 O O   . HOH   G .   ? 0.4269 0.3868 0.5666 -0.1638 0.0485  0.0529  229 HOH   B O   
7457 O O   . HOH   G .   ? 0.5193 0.2336 0.3300 0.0152  -0.0527 0.0094  230 HOH   B O   
7458 O O   . HOH   G .   ? 0.1782 0.1578 0.1346 -0.0126 -0.0137 0.0028  231 HOH   B O   
7459 O O   . HOH   G .   ? 0.2743 0.3291 0.3191 -0.1070 0.0137  -0.0216 232 HOH   B O   
7460 O O   . HOH   G .   ? 0.3958 0.2950 0.5077 0.0546  -0.1195 -0.1763 233 HOH   B O   
7461 O O   . HOH   G .   ? 0.3392 0.6086 0.2697 0.0149  -0.0711 -0.1505 234 HOH   B O   
7462 O O   . HOH   G .   ? 0.2738 0.4781 0.3511 -0.0406 -0.1082 -0.0558 235 HOH   B O   
7463 O O   . HOH   G .   ? 0.3783 0.2969 0.4701 0.0748  -0.0108 -0.0511 236 HOH   B O   
7464 O O   . HOH   G .   ? 0.2482 0.3445 0.3167 0.0297  0.0133  -0.1068 237 HOH   B O   
7465 O O   . HOH   G .   ? 0.2764 0.2456 0.3269 0.0664  0.0580  -0.0186 238 HOH   B O   
7466 O O   . HOH   G .   ? 0.3883 0.2021 0.1952 0.0230  -0.0838 -0.0160 239 HOH   B O   
7467 O O   . HOH   G .   ? 0.2524 0.3668 0.2321 -0.0157 -0.0167 0.0470  240 HOH   B O   
7468 O O   . HOH   G .   ? 0.4832 0.4899 0.3092 0.0397  -0.0030 -0.0777 241 HOH   B O   
7469 O O   . HOH   G .   ? 0.1716 0.1494 0.1665 -0.0021 -0.0109 -0.0030 242 HOH   B O   
7470 O O   . HOH   G .   ? 0.1974 0.2797 0.2999 0.0293  0.0528  0.0708  243 HOH   B O   
7471 O O   . HOH   G .   ? 0.6013 0.3062 0.4251 -0.2242 -0.0220 0.0118  244 HOH   B O   
7472 O O   . HOH   G .   ? 0.1734 0.1805 0.2701 -0.0032 0.0063  -0.0083 245 HOH   B O   
7473 O O   . HOH   G .   ? 0.6992 0.7459 0.4147 -0.0109 0.1531  0.0516  246 HOH   B O   
7474 O O   . HOH   G .   ? 0.2549 0.2574 0.2683 0.0851  -0.0800 -0.0742 247 HOH   B O   
7475 O O   . HOH   G .   ? 0.2323 0.1736 0.2213 -0.0371 -0.0600 0.0349  248 HOH   B O   
7476 O O   . HOH   G .   ? 0.2334 0.2149 0.2356 -0.0324 -0.0372 0.0399  249 HOH   B O   
7477 O O   . HOH   G .   ? 0.3147 0.1899 0.6712 -0.0055 -0.1153 -0.0027 250 HOH   B O   
7478 O O   . HOH   G .   ? 0.2199 0.2157 0.5205 -0.0009 -0.0537 -0.0735 251 HOH   B O   
7479 O O   . HOH   G .   ? 0.4513 0.2974 0.4057 -0.1295 -0.0697 0.0560  252 HOH   B O   
7480 O O   . HOH   G .   ? 0.3625 0.2971 0.2095 0.0145  0.0562  0.0134  253 HOH   B O   
7481 O O   . HOH   G .   ? 0.2521 0.5046 0.5753 -0.0933 -0.0676 -0.1128 254 HOH   B O   
7482 O O   . HOH   G .   ? 0.3990 0.3685 0.2833 0.0006  0.1241  0.0037  255 HOH   B O   
7483 O O   . HOH   G .   ? 0.2729 0.3776 0.2395 -0.0751 0.0153  0.0628  256 HOH   B O   
7484 O O   . HOH   G .   ? 0.1849 0.1866 0.3579 -0.0325 -0.0217 0.0326  257 HOH   B O   
7485 O O   . HOH   G .   ? 0.3137 0.3633 0.3595 -0.0673 0.0195  -0.0770 258 HOH   B O   
7486 O O   . HOH   G .   ? 0.1646 0.1863 0.2260 -0.0161 0.0048  0.0191  259 HOH   B O   
7487 O O   . HOH   G .   ? 0.3834 0.2282 0.5404 0.0328  0.0340  0.0582  260 HOH   B O   
7488 O O   . HOH   G .   ? 0.3891 0.6132 0.7449 0.0687  0.1719  0.1007  261 HOH   B O   
7489 O O   . HOH   G .   ? 0.3545 0.2561 0.2105 0.0324  -0.0469 -0.0169 262 HOH   B O   
7490 O O   . HOH   G .   ? 0.4095 0.3781 0.4814 0.1190  -0.0551 -0.1036 263 HOH   B O   
7491 O O   . HOH   G .   ? 0.7805 0.5111 0.5753 0.1429  0.0181  -0.1416 264 HOH   B O   
7492 O O   . HOH   G .   ? 0.2506 0.2659 0.1985 0.0063  -0.0057 -0.0076 265 HOH   B O   
7493 O O   . HOH   G .   ? 0.2617 0.4182 0.4176 0.0248  0.1194  0.0339  266 HOH   B O   
7494 O O   . HOH   G .   ? 0.2195 0.1763 0.2283 -0.0241 -0.0196 0.0113  267 HOH   B O   
7495 O O   . HOH   G .   ? 0.3334 0.4324 0.3990 -0.0216 -0.1024 0.1031  268 HOH   B O   
7496 O O   . HOH   G .   ? 0.2557 0.5389 0.3127 -0.0794 -0.0422 -0.0641 269 HOH   B O   
7497 O O   . HOH   G .   ? 0.4326 0.3069 0.4699 -0.0101 -0.1091 -0.0546 270 HOH   B O   
7498 O O   . HOH   G .   ? 0.2590 0.3005 0.3397 -0.0348 0.0258  -0.0780 271 HOH   B O   
7499 O O   . HOH   G .   ? 0.3444 0.2979 0.3433 -0.0726 0.0442  -0.0618 272 HOH   B O   
7500 O O   . HOH   G .   ? 0.4776 0.3029 0.4243 0.0034  -0.0441 -0.0669 273 HOH   B O   
7501 O O   . HOH   G .   ? 0.2082 0.1973 0.1688 -0.0526 -0.0495 0.0223  274 HOH   B O   
7502 O O   . HOH   G .   ? 0.5731 0.5866 0.4915 0.2326  -0.0760 0.0702  275 HOH   B O   
7503 O O   . HOH   G .   ? 0.2724 0.4585 0.5961 -0.0508 0.0496  -0.0376 276 HOH   B O   
7504 O O   . HOH   G .   ? 0.2551 0.2878 0.2638 -0.0365 -0.0769 0.0413  277 HOH   B O   
7505 O O   . HOH   G .   ? 0.5412 0.3269 0.4399 -0.1051 0.0333  -0.1131 278 HOH   B O   
7506 O O   . HOH   G .   ? 0.2899 0.2085 0.3092 -0.0668 0.0086  -0.0166 279 HOH   B O   
7507 O O   . HOH   G .   ? 0.2883 0.3980 0.2429 0.1284  -0.0732 -0.0554 280 HOH   B O   
7508 O O   . HOH   G .   ? 0.2071 0.1619 0.4478 -0.0062 -0.0496 -0.0264 281 HOH   B O   
7509 O O   . HOH   G .   ? 0.2368 0.2374 0.5100 -0.0628 0.0089  0.1165  282 HOH   B O   
7510 O O   . HOH   G .   ? 0.2610 0.2805 0.2262 -0.0317 -0.0661 -0.0653 283 HOH   B O   
7511 O O   . HOH   G .   ? 0.4572 0.5746 0.5143 0.0517  -0.1637 0.0658  284 HOH   B O   
7512 O O   . HOH   G .   ? 0.1940 0.1652 0.2045 -0.0019 0.0129  -0.0026 285 HOH   B O   
7513 O O   . HOH   G .   ? 0.6177 0.3966 0.3549 0.2696  0.1494  0.1018  286 HOH   B O   
7514 O O   . HOH   G .   ? 0.2230 0.6159 0.5066 -0.1167 -0.0201 -0.0394 287 HOH   B O   
7515 O O   . HOH   G .   ? 0.3001 0.5050 0.5346 -0.0936 -0.1293 0.0827  288 HOH   B O   
7516 O O   . HOH   G .   ? 0.2010 0.2258 0.3148 0.0084  0.0081  0.0115  289 HOH   B O   
7517 O O   . HOH   G .   ? 0.1978 0.1701 0.3800 -0.0148 0.0068  0.0039  290 HOH   B O   
7518 O O   . HOH   G .   ? 0.1796 0.2145 0.1701 -0.0135 -0.0163 0.0107  291 HOH   B O   
7519 O O   . HOH   G .   ? 0.3815 0.2218 0.4356 -0.0913 -0.1963 0.0802  292 HOH   B O   
7520 O O   . HOH   G .   ? 0.3904 0.3124 0.2745 -0.0490 0.0427  -0.1321 293 HOH   B O   
7521 O O   . HOH   G .   ? 0.2841 0.6898 0.2518 0.0692  -0.0406 -0.0669 294 HOH   B O   
7522 O O   . HOH   G .   ? 0.2997 0.3023 0.3058 0.0076  -0.0957 0.0311  295 HOH   B O   
7523 O O   . HOH   G .   ? 0.3726 0.3409 0.2649 0.0622  -0.0649 0.0731  296 HOH   B O   
7524 O O   . HOH   G .   ? 0.3855 0.3053 0.2393 0.0248  -0.0840 0.0116  297 HOH   B O   
7525 O O   . HOH   G .   ? 0.2437 0.2980 0.6631 0.0588  -0.0623 -0.1354 298 HOH   B O   
7526 O O   . HOH   G .   ? 0.4020 0.4893 0.4846 -0.2002 0.1734  -0.1025 299 HOH   B O   
7527 O O   . HOH   G .   ? 0.4514 0.6714 0.2878 0.0161  -0.1171 0.0073  300 HOH   B O   
7528 O O   . HOH   G .   ? 0.2059 0.3319 0.5685 0.0450  0.0003  -0.1396 301 HOH   B O   
7529 O O   . HOH   G .   ? 0.5145 0.3724 0.4340 -0.1008 0.0260  0.1018  302 HOH   B O   
7530 O O   . HOH   G .   ? 0.3830 0.2610 0.2565 -0.1285 0.0047  0.0255  303 HOH   B O   
7531 O O   . HOH   G .   ? 0.1795 0.1589 0.3993 0.0085  0.0053  0.0038  304 HOH   B O   
7532 O O   . HOH   G .   ? 0.4666 0.5554 0.2381 0.0153  0.1069  0.0993  305 HOH   B O   
7533 O O   . HOH   G .   ? 0.2002 0.1882 0.2553 0.0133  0.0049  0.0148  306 HOH   B O   
7534 O O   . HOH   G .   ? 0.2357 0.3371 0.4896 -0.0199 -0.0468 -0.0566 307 HOH   B O   
7535 O O   . HOH   G .   ? 0.4370 0.4714 0.9513 -0.0432 -0.1279 0.2911  308 HOH   B O   
7536 O O   . HOH   G .   ? 0.2286 0.1884 0.2556 -0.0344 -0.0267 -0.0039 309 HOH   B O   
7537 O O   . HOH   G .   ? 0.1897 0.3198 0.2459 -0.0296 -0.0229 0.0734  310 HOH   B O   
7538 O O   . HOH   G .   ? 0.3504 0.2069 0.3971 0.0626  0.1450  0.0674  311 HOH   B O   
7539 O O   . HOH   G .   ? 0.4047 0.3051 0.6248 -0.0473 -0.0535 0.1633  312 HOH   B O   
7540 O O   . HOH   G .   ? 0.3272 0.8257 0.7155 0.1761  -0.0802 -0.1667 313 HOH   B O   
7541 O O   . HOH   G .   ? 0.3050 0.3067 0.4123 -0.0451 0.1273  -0.1171 314 HOH   B O   
7542 O O   . HOH   G .   ? 0.2225 0.1851 0.3362 0.0344  -0.0953 0.0113  315 HOH   B O   
7543 O O   . HOH   G .   ? 0.3999 0.2603 0.2611 0.0412  -0.0278 0.0533  316 HOH   B O   
7544 O O   . HOH   G .   ? 0.2818 0.1666 0.2572 -0.0170 -0.0300 0.0226  317 HOH   B O   
7545 O O   . HOH   G .   ? 0.2537 0.2069 0.2330 -0.0108 0.0121  0.0438  318 HOH   B O   
7546 O O   . HOH   G .   ? 0.6083 0.5486 0.7769 0.1995  -0.1199 0.2365  319 HOH   B O   
7547 O O   . HOH   G .   ? 0.4884 0.2771 0.3591 0.0442  0.0265  0.0851  320 HOH   B O   
7548 O O   . HOH   G .   ? 0.4557 0.2217 0.2963 0.1446  0.0901  0.0357  321 HOH   B O   
7549 O O   . HOH   G .   ? 0.1983 0.1778 0.3252 -0.0246 -0.0112 -0.0119 322 HOH   B O   
7550 O O   . HOH   G .   ? 0.1894 0.2064 0.3303 -0.0330 -0.0038 0.0234  323 HOH   B O   
7551 O O   . HOH   G .   ? 0.5310 0.6251 0.4574 0.0388  -0.1285 0.1503  324 HOH   B O   
7552 O O   . HOH   G .   ? 0.5861 0.3888 0.3027 -0.0083 -0.0254 -0.0147 325 HOH   B O   
7553 O O   . HOH   G .   ? 0.4621 0.4188 0.2339 0.1435  -0.1334 -0.0388 326 HOH   B O   
7554 O O   . HOH   G .   ? 0.5049 0.3286 0.6624 0.1485  0.2854  0.1808  327 HOH   B O   
7555 O O   . HOH   G .   ? 0.6348 0.3893 0.4695 0.0950  0.1430  0.1919  328 HOH   B O   
7556 O O   . HOH   G .   ? 0.7816 0.2357 0.4333 0.0279  -0.1030 -0.0407 329 HOH   B O   
7557 O O   . HOH   G .   ? 0.3031 0.2334 0.6028 -0.0015 -0.0337 0.0744  330 HOH   B O   
7558 O O   . HOH   G .   ? 0.2362 0.2092 0.2723 0.0458  0.0564  0.0077  331 HOH   B O   
7559 O O   . HOH   G .   ? 0.2838 0.4220 0.5984 -0.0752 -0.1878 0.1720  332 HOH   B O   
7560 O O   . HOH   G .   ? 0.2209 0.3265 0.3913 0.0321  -0.0164 -0.0930 333 HOH   B O   
7561 O O   . HOH   G .   ? 0.6768 0.4872 0.6557 0.1494  0.2362  -0.0090 334 HOH   B O   
7562 O O   . HOH   G .   ? 0.5687 0.4262 0.5776 -0.0082 0.0815  -0.0274 335 HOH   B O   
7563 O O   . HOH   G .   ? 0.6103 0.6441 0.6670 -0.1089 -0.1217 0.2427  336 HOH   B O   
7564 O O   . HOH   G .   ? 0.2112 0.1662 0.2520 0.0133  -0.0299 0.0056  337 HOH   B O   
7565 O O   . HOH   G .   ? 0.4477 0.7138 0.4138 -0.0527 -0.1031 0.1662  338 HOH   B O   
7566 O O   . HOH   G .   ? 0.5042 0.6198 0.7988 0.0076  0.0611  -0.0033 339 HOH   B O   
7567 O O   . HOH   G .   ? 0.6634 0.5243 0.6422 -0.1154 -0.1363 -0.1485 340 HOH   B O   
7568 O O   . HOH   G .   ? 0.4808 0.3159 0.3205 0.0611  -0.1209 -0.0699 341 HOH   B O   
7569 O O   . HOH   G .   ? 0.5196 0.3887 0.4589 0.0061  0.1268  -0.1370 342 HOH   B O   
7570 O O   . HOH   G .   ? 0.3193 0.2012 0.4213 0.0281  -0.1204 -0.0495 343 HOH   B O   
7571 O O   . HOH   G .   ? 0.5261 0.5259 0.3708 -0.0425 -0.1154 0.0309  344 HOH   B O   
7572 O O   . HOH   G .   ? 0.8037 0.6182 0.3851 0.0150  -0.0508 0.1766  345 HOH   B O   
7573 O O   . HOH   G .   ? 0.4026 0.6197 0.4454 -0.1040 -0.1047 -0.0703 346 HOH   B O   
7574 O O   . HOH   G .   ? 0.6081 0.5437 0.6271 -0.1149 0.0800  0.1515  347 HOH   B O   
7575 O O   . HOH   G .   ? 0.3981 0.6616 0.6694 0.0055  -0.1313 -0.0596 348 HOH   B O   
7576 O O   . HOH   G .   ? 0.2390 0.2282 0.4377 -0.0138 0.1086  -0.0463 349 HOH   B O   
7577 O O   . HOH   G .   ? 0.3259 0.2267 0.4952 -0.0319 -0.0687 -0.0494 350 HOH   B O   
7578 O O   . HOH   G .   ? 0.5135 0.3186 0.5460 -0.0817 0.1086  0.0584  351 HOH   B O   
7579 O O   . HOH   G .   ? 0.5096 0.6778 0.7534 0.0201  0.0568  -0.0662 352 HOH   B O   
7580 O O   . HOH   G .   ? 0.2593 0.5934 0.3806 0.1380  -0.0913 -0.1345 353 HOH   B O   
7581 O O   . HOH   G .   ? 0.4020 0.6422 0.4483 -0.1809 0.0553  -0.0368 354 HOH   B O   
7582 O O   . HOH   G .   ? 0.2981 0.4258 0.4876 0.0308  0.0119  -0.0078 355 HOH   B O   
7583 O O   . HOH   G .   ? 0.4208 0.2233 0.3507 -0.0716 0.0410  -0.0893 356 HOH   B O   
7584 O O   . HOH   G .   ? 0.4573 0.2727 0.4215 -0.0789 -0.0317 -0.0759 357 HOH   B O   
7585 O O   . HOH   G .   ? 0.5213 0.3753 0.4200 0.0046  0.1113  -0.0627 358 HOH   B O   
7586 O O   . HOH   G .   ? 0.4862 0.5293 0.5489 0.1972  -0.1241 0.0623  359 HOH   B O   
7587 O O   . HOH   G .   ? 0.3775 0.3491 0.4653 -0.0016 -0.0764 0.0256  360 HOH   B O   
7588 O O   . HOH   G .   ? 0.6967 0.3771 0.4935 0.0026  -0.1622 -0.0981 361 HOH   B O   
7589 O O   . HOH   G .   ? 0.2604 0.4350 0.6869 -0.1262 -0.0605 -0.0801 362 HOH   B O   
7590 O O   . HOH   G .   ? 0.5815 0.4779 0.5890 0.0486  0.1459  0.2204  363 HOH   B O   
7591 O O   . HOH   G .   ? 0.4241 0.8072 0.3533 0.2432  0.0548  0.0925  364 HOH   B O   
7592 O O   . HOH   G .   ? 0.5738 0.6488 0.6088 -0.0538 -0.0279 -0.1241 365 HOH   B O   
7593 O O   . HOH   G .   ? 0.6858 0.2460 0.3772 -0.0400 -0.0492 0.0830  366 HOH   B O   
7594 O O   . HOH   G .   ? 0.4527 0.3902 0.6130 0.1291  -0.1514 0.0005  367 HOH   B O   
7595 O O   . HOH   G .   ? 0.5364 0.3165 0.5592 -0.1260 -0.0275 0.0022  368 HOH   B O   
7596 O O   . HOH   G .   ? 0.4585 0.7033 0.5192 0.3074  0.1038  0.1740  369 HOH   B O   
7597 O O   . HOH   G .   ? 0.6362 0.4726 0.4352 0.1427  0.0281  0.0695  370 HOH   B O   
7598 O O   . HOH   G .   ? 0.8775 0.8887 0.6227 0.3191  -0.1432 0.0020  371 HOH   B O   
7599 O O   . HOH   G .   ? 0.5256 0.6602 0.3227 0.1774  -0.1086 0.0722  372 HOH   B O   
7600 O O   . HOH   G .   ? 0.4371 0.5293 0.5593 -0.0598 -0.0211 0.0288  373 HOH   B O   
7601 O O   . HOH   G .   ? 0.4722 0.6959 0.6917 0.0913  -0.0070 0.3340  374 HOH   B O   
7602 O O   . HOH   G .   ? 0.5908 0.4090 0.2961 -0.0832 -0.1481 -0.0385 375 HOH   B O   
7603 O O   . HOH   G .   ? 0.3186 0.3328 0.3610 0.0605  -0.0665 -0.0460 376 HOH   B O   
7604 O O   . HOH   G .   ? 0.3510 0.7690 0.2635 -0.0423 -0.0101 -0.0383 377 HOH   B O   
7605 O O   . HOH   G .   ? 0.3370 0.6122 0.7708 0.1122  -0.0727 0.1047  378 HOH   B O   
7606 O O   . HOH   G .   ? 0.7252 0.3608 0.5815 -0.0393 -0.1030 0.0270  379 HOH   B O   
7607 O O   . HOH   G .   ? 0.2481 0.3802 0.5458 0.0225  -0.0795 -0.0646 380 HOH   B O   
7608 O O   . HOH   G .   ? 0.5276 0.6937 0.3554 -0.1339 -0.0030 -0.1693 381 HOH   B O   
7609 O O   . HOH   G .   ? 0.5116 0.4513 0.4455 0.0970  0.0035  -0.0323 382 HOH   B O   
7610 O O   . HOH   G .   ? 0.3064 0.8041 0.4799 0.0658  0.0188  0.1113  383 HOH   B O   
7611 O O   . HOH   G .   ? 0.3962 0.6858 0.6115 -0.0130 0.1429  0.1760  384 HOH   B O   
7612 O O   . HOH   G .   ? 0.2805 0.2875 0.3806 0.0054  0.0267  0.0110  385 HOH   B O   
7613 O O   . HOH   G .   ? 0.5290 0.5865 0.5583 0.0423  -0.1050 -0.1013 386 HOH   B O   
7614 O O   . HOH   G .   ? 0.7343 0.5688 0.5350 0.1955  -0.0353 -0.1030 387 HOH   B O   
7615 O O   . HOH   G .   ? 0.6808 0.4797 0.5182 -0.0816 -0.0037 0.1043  388 HOH   B O   
7616 O O   . HOH   G .   ? 0.5201 0.5016 0.4669 -0.0398 0.2150  -0.0459 389 HOH   B O   
7617 O O   . HOH   G .   ? 0.2585 0.4141 0.4375 -0.0475 -0.1043 0.0087  390 HOH   B O   
7618 O O   . HOH   G .   ? 0.4342 0.2446 0.3339 0.0876  -0.0366 -0.0015 391 HOH   B O   
7619 O O   . HOH   G .   ? 0.6245 0.4462 0.4894 0.0736  0.0897  0.0656  392 HOH   B O   
7620 O O   . HOH   G .   ? 0.4564 0.2322 0.6301 -0.0301 0.0736  0.1239  393 HOH   B O   
7621 O O   . HOH   G .   ? 0.2622 0.6232 0.7191 -0.1509 -0.1062 -0.0008 394 HOH   B O   
7622 O O   . HOH   G .   ? 0.3647 0.4736 0.3907 0.0125  0.0468  -0.0871 395 HOH   B O   
7623 O O   . HOH   G .   ? 0.4651 0.7926 0.4778 0.0314  0.0589  -0.1253 396 HOH   B O   
7624 O O   . HOH   G .   ? 0.5946 0.5273 0.5036 0.1503  0.1886  0.1192  397 HOH   B O   
7625 O O   . HOH   G .   ? 0.2238 0.2945 0.6722 -0.0441 -0.0732 -0.0168 398 HOH   B O   
7626 O O   . HOH   G .   ? 0.5807 0.4448 0.3230 -0.2267 -0.0664 0.0531  399 HOH   B O   
7627 O O   . HOH   G .   ? 0.5068 0.4729 0.4695 -0.1170 -0.1601 0.1980  400 HOH   B O   
7628 O O   . HOH   G .   ? 0.5744 0.4902 0.3460 0.1372  -0.0386 -0.0319 401 HOH   B O   
# 
